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***  1asp_test2  ***

elNémo ID: 181203223208140935

Job options:

ID        	=	 181203223208140935
JOBID     	=	 1asp_test2
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER 1asp_test2

HEADER    RIBONUCLEASE                            07-JAN-98   1A2P              
TITLE     BARNASE WILDTYPE STRUCTURE AT 1.5 ANGSTROMS RESOLUTION                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BARNASE;                                                   
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 EC: 3.1.27.-;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS AMYLOLIQUEFACIENS;                     
SOURCE   3 ORGANISM_TAXID: 1390;                                                
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   6 EXPRESSION_SYSTEM_PLASMID: PMJ1002                                   
KEYWDS    RIBONUCLEASE, MICROBIAL RIBONUCLEASE, ALPHA/BETA PROTEIN              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.MARTIN,V.RICHARD,M.SALEM,R.W.HARTLEY,Y.MAUGUEN                      
REVDAT   2   24-FEB-09 1A2P    1       VERSN                                    
REVDAT   1   29-APR-98 1A2P    0                                                
JRNL        AUTH   C.MARTIN,V.RICHARD,M.SALEM,R.HARTLEY,Y.MAUGUEN               
JRNL        TITL   REFINEMENT AND STRUCTURAL ANALYSIS OF BARNASE AT             
JRNL        TITL 2 1.5 A RESOLUTION.                                            
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  55   386 1999              
JRNL        REFN                   ISSN 0907-4449                               
JRNL        PMID   10089345                                                     
JRNL        DOI    10.1107/S0907444998010865                                    
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : SHELXL-93, X-PLOR                                    
REMARK   3   AUTHORS     : G.M.SHELDRICK                                        
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.4                           
REMARK   3   CROSS-VALIDATION METHOD           : FREE R VALUE                   
REMARK   3   FREE R VALUE TEST SET SELECTION   : EVERY 10TH REFLECTION          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).                         
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : 0.115                  
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.111                  
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.174                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 10.000                 
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 4812                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 48118                  
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).                     
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : 0.111                  
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : 44595                  
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS      : 2624                                          
REMARK   3   NUCLEIC ACID ATOMS : 0                                             
REMARK   3   HETEROGEN ATOMS    : 3                                             
REMARK   3   SOLVENT ATOMS      : 415                                           
REMARK   3                                                                      
REMARK   3  MODEL REFINEMENT.                                                   
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : 2972.00                 
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : 2417.50                 
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : 10                      
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : 27377                   
REMARK   3   NUMBER OF RESTRAINTS                     : 33057                   
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.                        
REMARK   3   BOND LENGTHS                         (A) : 0.013                   
REMARK   3   ANGLE DISTANCES                      (A) : 1.760                   
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : NULL                    
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : NULL                    
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : 0.273                   
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.200                   
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : 0.100                   
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : 0.010                   
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : 0.064                   
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : 0.100                   
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED: NULL                                                  
REMARK   3                                                                      
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER                      
REMARK   3   SPECIAL CASE: NULL                                                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: INITIAL POSITIONAL AND B-FACTOR           
REMARK   3  REFINEMENT WAS CARRIED OUT WITH X-PLOR (BRUNGER, 1992) FOR          
REMARK   3  DATA IN THE RESOLUTION RANGE 7.0 - 1.5 ANGSTROMS. AT R-VALUES       
REMARK   3  OF R=0.174 FOR F.GREATER THAN 3 SIGMA(F), THE REFINEMENT WAS        
REMARK   3  CONTINUED WITH THE PROGRAM SHELXL-93. ANISOU RECORDS CONTAIN        
REMARK   3  ANISOTROPIC DISPLACEMENT PARAMETERS U11 U22 U33 U23 U13 U12         
REMARK   3  (ANGSTROMS**2) MULTIPLIED BY 10000. ISOTROPIC EQUIVALENTS OF        
REMARK   3  ANISOTROPIC TEMPERATURE FACTORS ARE ALSO PRESENTED IN THIS          
REMARK   3  ENTRY.                                                              
REMARK   4                                                                      
REMARK   4 1A2P COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NOV-93                             
REMARK 200  TEMPERATURE           (KELVIN) : 287                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : LURE                               
REMARK 200  BEAMLINE                       : DW32                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.92                               
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : MULTILAYER MIRROR                  
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 48463                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 19.900                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.9                               
REMARK 200  DATA REDUNDANCY                : 2.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.03800                            
REMARK 200   FOR THE DATA SET  : 11.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.58                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.90                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.15800                            
REMARK 200   FOR SHELL         : 4.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: SHELXL-93, X-PLOR                                     
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.5                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       54.38667            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       27.19333            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ALA A     1                                                      
REMARK 465     GLN A     2                                                      
REMARK 465     ALA B     1                                                      
REMARK 465     GLN B     2                                                      
REMARK 465     ALA C     1                                                      
REMARK 465     GLN C     2                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     ARG A   59   CB    CG    CD    NE    CZ    NH1   NH2             
REMARK 480     VAL B    3   N                                                   
REMARK 480     ARG B   59   CG    CD    NE    CZ    NH1   NH2                   
REMARK 480     SER B   67   CB    OG                                            
REMARK 480     LYS C   39   CE    NZ                                            
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   CG2  THR A    16     NH2  ARG A    59     3675     2.01            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG C  72   CD  -  NE  -  CZ  ANGL. DEV. =   8.7 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A   5       23.54   -141.90                                   
REMARK 500    THR A  79      -50.02   -124.87                                   
REMARK 500    ASN B   5       22.77   -145.06                                   
REMARK 500    TRP B  94       30.23     70.65                                   
REMARK 500    ASN C   5       24.51   -143.95                                   
REMARK 500    THR C  79      -54.96   -125.06                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    ARG A  59         0.21    SIDE_CHAIN                              
REMARK 500    ARG B  59         0.08    SIDE_CHAIN                              
REMARK 500    ARG B  72         0.09    SIDE_CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                            
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 112  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  18   ND1                                                    
REMARK 620 2 HOH A 227   O   100.2                                              
REMARK 620 3 GLU A  60   OE2 112.2 147.3                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 112  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B  60   OE1                                                    
REMARK 620 2 GLU B  60   OE2  58.5                                              
REMARK 620 3 HOH B 260   O   135.8  87.3                                        
REMARK 620 4 HIS B  18   ND1 110.3 153.5 111.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 112  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C  60   OE1                                                    
REMARK 620 2 GLU C  60   OE2  58.7                                              
REMARK 620 3 LYS C  62   NZ   93.4 110.0                                        
REMARK 620 4 HOH C 139   O   148.6  89.9  99.8                                  
REMARK 620 5 HIS C  18   ND1  97.6 132.9 111.6 103.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 112                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 112                  
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 112                  
DBREF  1A2P A    1   110  UNP    P00648   RNBR_BACAM      48    157             
DBREF  1A2P B    1   110  UNP    P00648   RNBR_BACAM      48    157             
DBREF  1A2P C    1   110  UNP    P00648   RNBR_BACAM      48    157             
SEQRES   1 A  110  ALA GLN VAL ILE ASN THR PHE ASP GLY VAL ALA ASP TYR          
SEQRES   2 A  110  LEU GLN THR TYR HIS LYS LEU PRO ASP ASN TYR ILE THR          
SEQRES   3 A  110  LYS SER GLU ALA GLN ALA LEU GLY TRP VAL ALA SER LYS          
SEQRES   4 A  110  GLY ASN LEU ALA ASP VAL ALA PRO GLY LYS SER ILE GLY          
SEQRES   5 A  110  GLY ASP ILE PHE SER ASN ARG GLU GLY LYS LEU PRO GLY          
SEQRES   6 A  110  LYS SER GLY ARG THR TRP ARG GLU ALA ASP ILE ASN TYR          
SEQRES   7 A  110  THR SER GLY PHE ARG ASN SER ASP ARG ILE LEU TYR SER          
SEQRES   8 A  110  SER ASP TRP LEU ILE TYR LYS THR THR ASP HIS TYR GLN          
SEQRES   9 A  110  THR PHE THR LYS ILE ARG                                      
SEQRES   1 B  110  ALA GLN VAL ILE ASN THR PHE ASP GLY VAL ALA ASP TYR          
SEQRES   2 B  110  LEU GLN THR TYR HIS LYS LEU PRO ASP ASN TYR ILE THR          
SEQRES   3 B  110  LYS SER GLU ALA GLN ALA LEU GLY TRP VAL ALA SER LYS          
SEQRES   4 B  110  GLY ASN LEU ALA ASP VAL ALA PRO GLY LYS SER ILE GLY          
SEQRES   5 B  110  GLY ASP ILE PHE SER ASN ARG GLU GLY LYS LEU PRO GLY          
SEQRES   6 B  110  LYS SER GLY ARG THR TRP ARG GLU ALA ASP ILE ASN TYR          
SEQRES   7 B  110  THR SER GLY PHE ARG ASN SER ASP ARG ILE LEU TYR SER          
SEQRES   8 B  110  SER ASP TRP LEU ILE TYR LYS THR THR ASP HIS TYR GLN          
SEQRES   9 B  110  THR PHE THR LYS ILE ARG                                      
SEQRES   1 C  110  ALA GLN VAL ILE ASN THR PHE ASP GLY VAL ALA ASP TYR          
SEQRES   2 C  110  LEU GLN THR TYR HIS LYS LEU PRO ASP ASN TYR ILE THR          
SEQRES   3 C  110  LYS SER GLU ALA GLN ALA LEU GLY TRP VAL ALA SER LYS          
SEQRES   4 C  110  GLY ASN LEU ALA ASP VAL ALA PRO GLY LYS SER ILE GLY          
SEQRES   5 C  110  GLY ASP ILE PHE SER ASN ARG GLU GLY LYS LEU PRO GLY          
SEQRES   6 C  110  LYS SER GLY ARG THR TRP ARG GLU ALA ASP ILE ASN TYR          
SEQRES   7 C  110  THR SER GLY PHE ARG ASN SER ASP ARG ILE LEU TYR SER          
SEQRES   8 C  110  SER ASP TRP LEU ILE TYR LYS THR THR ASP HIS TYR GLN          
SEQRES   9 C  110  THR PHE THR LYS ILE ARG                                      
HET     ZN  A 112       1                                                       
HET     ZN  B 112       1                                                       
HET     ZN  C 112       1                                                       
HETNAM      ZN ZINC ION                                                         
FORMUL   4   ZN    3(ZN 2+)                                                     
FORMUL   7  HOH   *415(H2 O)                                                    
HELIX    1   1 PHE A    7  TYR A   17  1                                  11    
HELIX    2   2 LYS A   27  LEU A   33  1                                   7    
HELIX    3   3 ALA A   37  LYS A   39  5                                   3    
HELIX    4   4 LEU A   42  VAL A   45  1                                   4    
HELIX    5   5 PHE B    7  TYR B   17  1                                  11    
HELIX    6   6 LYS B   27  LEU B   33  1                                   7    
HELIX    7   7 ALA B   37  LYS B   39  5                                   3    
HELIX    8   8 LEU B   42  VAL B   45  1                                   4    
HELIX    9   9 PHE C    7  TYR C   17  1                                  11    
HELIX   10  10 LYS C   27  LEU C   33  1                                   7    
HELIX   11  11 ALA C   37  LYS C   39  5                                   3    
HELIX   12  12 LEU C   42  VAL C   45  1                                   4    
SHEET    1   A 4 ILE A  96  THR A  99  0                                        
SHEET    2   A 4 ARG A  87  SER A  91 -1  N  LEU A  89   O  TYR A  97           
SHEET    3   A 4 TRP A  71  ASP A  75 -1  N  ALA A  74   O  ILE A  88           
SHEET    4   A 4 GLY A  52  ILE A  55 -1  N  ASP A  54   O  GLU A  73           
SHEET    1   B 4 ILE B  96  THR B  99  0                                        
SHEET    2   B 4 ARG B  87  SER B  91 -1  N  LEU B  89   O  TYR B  97           
SHEET    3   B 4 TRP B  71  ASP B  75 -1  N  ALA B  74   O  ILE B  88           
SHEET    4   B 4 GLY B  52  PHE B  56 -1  N  PHE B  56   O  TRP B  71           
SHEET    1   C 4 ILE C  96  THR C  99  0                                        
SHEET    2   C 4 ARG C  87  SER C  91 -1  N  LEU C  89   O  TYR C  97           
SHEET    3   C 4 TRP C  71  ASP C  75 -1  N  ALA C  74   O  ILE C  88           
SHEET    4   C 4 GLY C  52  ILE C  55 -1  N  ASP C  54   O  GLU C  73           
LINK        ZN    ZN A 112                 ND1 HIS A  18     1555   1555  2.36  
LINK        ZN    ZN B 112                 OE1 GLU B  60     1555   1555  2.25  
LINK        ZN    ZN B 112                 OE2 GLU B  60     1555   1555  2.32  
LINK        ZN    ZN C 112                 OE1 GLU C  60     1555   1555  2.32  
LINK        ZN    ZN C 112                 OE2 GLU C  60     1555   1555  2.12  
LINK        ZN    ZN C 112                 NZ  LYS C  62     1555   1555  2.09  
LINK        ZN    ZN A 112                 O   HOH A 227     1555   1555  2.25  
LINK        ZN    ZN B 112                 O   HOH B 260     1555   1555  2.42  
LINK        ZN    ZN C 112                 O   HOH C 139     1555   1555  1.99  
LINK        ZN    ZN A 112                 OE2 GLU A  60     1555   3675  2.21  
LINK        ZN    ZN B 112                 ND1 HIS B  18     1555   3565  2.21  
LINK        ZN    ZN C 112                 ND1 HIS C  18     1555   3665  2.06  
SITE     1 AC1  4 HIS A  18  GLU A  60  LYS A  62  HOH A 227                    
SITE     1 AC2  4 HIS B  18  GLU B  60  LYS B  62  HOH B 260                    
SITE     1 AC3  4 HIS C  18  GLU C  60  LYS C  62  HOH C 139                    
CRYST1   58.970   58.970   81.580  90.00  90.00 120.00 P 32          9          
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      0.016958  0.009791  0.000000        0.00000                         
SCALE2      0.000000  0.019581  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012258        0.00000                         
MTRIX1   1  0.757790  0.647480  0.080780      -58.48021    1                    
MTRIX2   1  0.646210 -0.761860  0.044460       51.57518    1                    
MTRIX3   1  0.090330  0.018510 -0.995740       98.15767    1                    
MTRIX1   2  0.589870  0.805830  0.051860      -30.43273    1                    
MTRIX2   2  0.803110 -0.592140  0.066190       20.75484    1                    
MTRIX3   2  0.084050  0.002600 -0.996460       81.77702    1                    
ATOM      1  N   VAL A   3      16.875  37.901  43.478  1.00 47.79           N  
ANISOU    1  N   VAL A   3     9390   4614   4155  -4533    401   -753       N  
ATOM      2  CA  VAL A   3      17.997  38.577  42.795  1.00 41.49           C  
ANISOU    2  CA  VAL A   3     8639   3247   3879  -3472    364   -656       C  
ATOM      3  C   VAL A   3      18.147  39.997  43.309  1.00 34.47           C  
ANISOU    3  C   VAL A   3     6453   3086   3558  -1855   1056   -986       C  
ATOM      4  O   VAL A   3      17.180  40.763  43.281  1.00 34.84           O  
ANISOU    4  O   VAL A   3     4963   4293   3980   -772    665   -408       O  
ATOM      5  CB  VAL A   3      17.786  38.593  41.279  1.00 42.12           C  
ANISOU    5  CB  VAL A   3     9192   2946   3865  -2868    317   -534       C  
ATOM      6  CG1 VAL A   3      18.621  39.606  40.573  1.00 38.29           C  
ANISOU    6  CG1 VAL A   3     7961   2821   3766  -1985    505   -958       C  
ATOM      7  CG2 VAL A   3      18.024  37.190  40.696  1.00 45.14           C  
ANISOU    7  CG2 VAL A   3    10180   2879   4091  -2690   -275    338       C  
ATOM      8  N   ILE A   4      19.355  40.377  43.690  1.00 27.18           N  
ANISOU    8  N   ILE A   4     6192   1979   2157  -1048    963   -541       N  
ATOM      9  CA  ILE A   4      19.568  41.805  44.109  1.00 24.08           C  
ANISOU    9  CA  ILE A   4     5555   1936   1657   -496   1087   -363       C  
ATOM     10  C   ILE A   4      20.355  42.488  42.992  1.00 21.31           C  
ANISOU   10  C   ILE A   4     4589   1708   1800   -226   1563   -508       C  
ATOM     11  O   ILE A   4      21.489  42.115  42.701  1.00 21.63           O  
ANISOU   11  O   ILE A   4     4643   1345   2232    326   1473     56       O  
ATOM     12  CB  ILE A   4      20.430  41.800  45.396  1.00 24.83           C  
ANISOU   12  CB  ILE A   4     5759   1933   1741   -527   1185   -366       C  
ATOM     13  CG1 ILE A   4      19.774  40.976  46.525  1.00 27.01           C  
ANISOU   13  CG1 ILE A   4     6723   1861   1679   -813    674    -41       C  
ATOM     14  CG2 ILE A   4      20.779  43.192  45.823  1.00 24.93           C  
ANISOU   14  CG2 ILE A   4     5356   2036   2080   -802   1479   -345       C  
ATOM     15  CD1 ILE A   4      20.598  40.921  47.787  1.00 33.25           C  
ANISOU   15  CD1 ILE A   4     7583   3635   1415  -1878   1016    317       C  
ATOM     16  N   ASN A   5      19.676  43.364  42.248  1.00 20.12           N  
ANISOU   16  N   ASN A   5     4182   1613   1849  -1126   1387   -212       N  
ATOM     17  CA  ASN A   5      20.308  43.996  41.102  1.00 19.67           C  
ANISOU   17  CA  ASN A   5     4137   1513   1823   -995   1153   -334       C  
ATOM     18  C   ASN A   5      19.925  45.450  40.923  1.00 17.24           C  
ANISOU   18  C   ASN A   5     3246   1607   1696  -1042    592   -108       C  
ATOM     19  O   ASN A   5      20.142  45.981  39.825  1.00 17.10           O  
ANISOU   19  O   ASN A   5     3261   1615   1620   -264    517   -167       O  
ATOM     20  CB  ASN A   5      20.074  43.224  39.803  1.00 20.04           C  
ANISOU   20  CB  ASN A   5     4178   1616   1821   -872   1271   -872       C  
ATOM     21  CG  ASN A   5      18.623  43.365  39.320  1.00 20.89           C  
ANISOU   21  CG  ASN A   5     4058   2019   1862   -924   1060  -1096       C  
ATOM     22  OD1 ASN A   5      17.758  43.768  40.083  1.00 21.76           O  
ANISOU   22  OD1 ASN A   5     3406   2983   1881   -849    817   -776       O  
ATOM     23  ND2 ASN A   5      18.405  43.073  38.050  1.00 22.93           N  
ANISOU   23  ND2 ASN A   5     3783   3095   1835   -754    206  -1443       N  
ATOM     24  N   THR A   6      19.502  46.115  41.979  1.00 15.82           N  
ANISOU   24  N   THR A   6     2496   1777   1737   -531    611   -363       N  
ATOM     25  CA  THR A   6      19.178  47.556  41.906  1.00 16.81           C  
ANISOU   25  CA  THR A   6     2268   1791   2328   -275    764   -454       C  
ATOM     26  C   THR A   6      20.299  48.405  42.457  1.00 14.04           C  
ANISOU   26  C   THR A   6     2024   1573   1736     95    460   -432       C  
ATOM     27  O   THR A   6      21.154  47.941  43.191  1.00 14.38           O  
ANISOU   27  O   THR A   6     2588   1626   1248   -301    345   -188       O  
ATOM     28  CB  THR A   6      17.889  47.828  42.737  1.00 17.16           C  
ANISOU   28  CB  THR A   6     1956   2162   2403    -38    679    -18       C  
ATOM     29  OG1 THR A   6      18.098  47.384  44.059  1.00 23.19           O  
ANISOU   29  OG1 THR A   6     3490   3171   2148   -902    722   -640       O  
ATOM     30  CG2 THR A   6      16.696  47.101  42.162  1.00 22.55           C  
ANISOU   30  CG2 THR A   6     2141   3656   2770   -682    937   -160       C  
ATOM     31  N   PHE A   7      20.276  49.727  42.144  1.00 14.44           N  
ANISOU   31  N   PHE A   7     2385   1641   1459   -294    525   -714       N  
ATOM     32  CA  PHE A   7      21.281  50.600  42.712  1.00 14.94           C  
ANISOU   32  CA  PHE A   7     2609   1593   1474   -315    429   -489       C  
ATOM     33  C   PHE A   7      21.304  50.540  44.237  1.00 15.96           C  
ANISOU   33  C   PHE A   7     3036   1545   1485   -978   1007   -325       C  
ATOM     34  O   PHE A   7      22.364  50.392  44.837  1.00 15.42           O  
ANISOU   34  O   PHE A   7     2672   1756   1430   -341    860   -354       O  
ATOM     35  CB  PHE A   7      21.193  52.025  42.242  1.00 15.65           C  
ANISOU   35  CB  PHE A   7     2846   1564   1537   -268    333   -374       C  
ATOM     36  CG  PHE A   7      21.669  52.260  40.821  1.00 15.01           C  
ANISOU   36  CG  PHE A   7     2806   1372   1526    -61    214   -403       C  
ATOM     37  CD1 PHE A   7      23.019  52.178  40.526  1.00 15.42           C  
ANISOU   37  CD1 PHE A   7     2804   1477   1579   -141    176   -426       C  
ATOM     38  CD2 PHE A   7      20.801  52.613  39.818  1.00 15.77           C  
ANISOU   38  CD2 PHE A   7     2640   1793   1558    -55    709   -426       C  
ATOM     39  CE1 PHE A   7      23.466  52.380  39.234  1.00 17.19           C  
ANISOU   39  CE1 PHE A   7     2884   1957   1690   -626    795   -539       C  
ATOM     40  CE2 PHE A   7      21.231  52.736  38.512  1.00 16.36           C  
ANISOU   40  CE2 PHE A   7     2857   1836   1522   -226    596   -462       C  
ATOM     41  CZ  PHE A   7      22.588  52.649  38.217  1.00 16.36           C  
ANISOU   41  CZ  PHE A   7     3156   1536   1526   -548    650   -378       C  
ATOM     42  N   ASP A   8      20.153  50.663  44.861  1.00 16.64           N  
ANISOU   42  N   ASP A   8     2733   2055   1533   -746    972   -683       N  
ATOM     43  CA  ASP A   8      20.096  50.718  46.322  1.00 15.99           C  
ANISOU   43  CA  ASP A   8     2335   2250   1490    -44    890   -719       C  
ATOM     44  C   ASP A   8      20.397  49.363  46.940  1.00 17.56           C  
ANISOU   44  C   ASP A   8     2887   2173   1611    101    396   -825       C  
ATOM     45  O   ASP A   8      21.150  49.259  47.909  1.00 16.79           O  
ANISOU   45  O   ASP A   8     2712   1876   1790    162    343   -239       O  
ATOM     46  CB  ASP A   8      18.756  51.282  46.783  1.00 17.03           C  
ANISOU   46  CB  ASP A   8     1862   2751   1857    499    760   -784       C  
ATOM     47  CG  ASP A   8      18.706  52.795  46.591  1.00 20.95           C  
ANISOU   47  CG  ASP A   8     1769   2758   3432   1170    324   -421       C  
ATOM     48  OD1 ASP A   8      19.571  53.503  47.112  1.00 21.91           O  
ANISOU   48  OD1 ASP A   8     2982   2594   2751    387   -462   -581       O  
ATOM     49  OD2 ASP A   8      17.795  53.254  45.873  1.00 22.61           O  
ANISOU   49  OD2 ASP A   8     2560   2374   3655    306    -81   -550       O  
ATOM     50  N   GLY A   9      19.913  48.292  46.302  1.00 18.86           N  
ANISOU   50  N   GLY A   9     3177   2261   1727   -221   1112   -709       N  
ATOM     51  CA  GLY A   9      20.126  46.945  46.826  1.00 20.19           C  
ANISOU   51  CA  GLY A   9     3732   2213   1726   -787   1408   -663       C  
ATOM     52  C   GLY A   9      21.580  46.537  46.842  1.00 18.58           C  
ANISOU   52  C   GLY A   9     3834   1857   1368   -525   1144   -669       C  
ATOM     53  O   GLY A   9      22.105  46.026  47.839  1.00 19.40           O  
ANISOU   53  O   GLY A   9     4023   1971   1377   -179    891   -112       O  
ATOM     54  N   VAL A  10      22.248  46.736  45.696  1.00 16.97           N  
ANISOU   54  N   VAL A  10     3683   1399   1364    -63    930   -292       N  
ATOM     55  CA  VAL A  10      23.649  46.415  45.562  1.00 16.53           C  
ANISOU   55  CA  VAL A  10     3723   1481   1076    -77   1084   -144       C  
ATOM     56  C   VAL A  10      24.524  47.334  46.400  1.00 15.21           C  
ANISOU   56  C   VAL A  10     3316   1474    988    331   -103    114       C  
ATOM     57  O   VAL A  10      25.443  46.858  47.074  1.00 15.57           O  
ANISOU   57  O   VAL A  10     3417   1615    885    285    132   -147       O  
ATOM     58  CB  VAL A  10      24.087  46.345  44.109  1.00 15.47           C  
ANISOU   58  CB  VAL A  10     3774   1038   1064    295   1211   -445       C  
ATOM     59  CG1 VAL A  10      25.562  45.981  43.977  1.00 16.57           C  
ANISOU   59  CG1 VAL A  10     3330   1701   1266    518    372    -35       C  
ATOM     60  CG2 VAL A  10      23.226  45.294  43.368  1.00 17.03           C  
ANISOU   60  CG2 VAL A  10     4036   1267   1169   -123    338   -483       C  
ATOM     61  N   ALA A  11      24.256  48.622  46.409  1.00 15.54           N  
ANISOU   61  N   ALA A  11     2857   1478   1569    -29    299   -165       N  
ATOM     62  CA  ALA A  11      25.065  49.567  47.199  1.00 13.83           C  
ANISOU   62  CA  ALA A  11     2345   1390   1519    474    -15   -109       C  
ATOM     63  C   ALA A  11      25.039  49.171  48.677  1.00 18.78           C  
ANISOU   63  C   ALA A  11     4171   1528   1438    170   -604   -146       C  
ATOM     64  O   ALA A  11      26.051  49.157  49.362  1.00 18.74           O  
ANISOU   64  O   ALA A  11     3894   2080   1146    569    290   -398       O  
ATOM     65  CB  ALA A  11      24.464  50.973  47.068  1.00 15.91           C  
ANISOU   65  CB  ALA A  11     2833   1290   1921     71     28   -186       C  
ATOM     66  N   ASP A  12      23.834  48.873  49.177  1.00 19.06           N  
ANISOU   66  N   ASP A  12     4453   1759   1031    -92    351   -271       N  
ATOM     67  CA  ASP A  12      23.726  48.524  50.582  1.00 22.03           C  
ANISOU   67  CA  ASP A  12     5526   1874    970    -39    974   -285       C  
ATOM     68  C   ASP A  12      24.334  47.159  50.888  1.00 23.78           C  
ANISOU   68  C   ASP A  12     6126   1807   1104    131    356    -70       C  
ATOM     69  O   ASP A  12      24.933  46.981  51.939  1.00 22.94           O  
ANISOU   69  O   ASP A  12     5304   2017   1393    484    543   -400       O  
ATOM     70  CB  ASP A  12      22.315  48.609  51.112  1.00 22.28           C  
ANISOU   70  CB  ASP A  12     5410   2430    624   -134   1198    -81       C  
ATOM     71  CG  ASP A  12      21.807  50.042  51.271  1.00 22.67           C  
ANISOU   71  CG  ASP A  12     4670   2650   1296    688   1558   -303       C  
ATOM     72  OD1 ASP A  12      22.633  50.960  51.336  1.00 26.27           O  
ANISOU   72  OD1 ASP A  12     5353   2310   2319    387    837    369       O  
ATOM     73  OD2 ASP A  12      20.584  50.220  51.156  1.00 25.64           O  
ANISOU   73  OD2 ASP A  12     4028   3636   2078   1354    654   -406       O  
ATOM     74  N   TYR A  13      24.253  46.232  49.937  1.00 22.66           N  
ANISOU   74  N   TYR A  13     5415   1826   1368    484    411   -154       N  
ATOM     75  CA  TYR A  13      24.888  44.902  50.143  1.00 22.08           C  
ANISOU   75  CA  TYR A  13     5294   1921   1176    758   1118   -371       C  
ATOM     76  C   TYR A  13      26.393  45.040  50.199  1.00 22.77           C  
ANISOU   76  C   TYR A  13     5342   1864   1446    796    304   -346       C  
ATOM     77  O   TYR A  13      27.049  44.481  51.062  1.00 23.52           O  
ANISOU   77  O   TYR A  13     5385   1964   1587    365   -359    -15       O  
ATOM     78  CB  TYR A  13      24.434  43.966  49.031  1.00 22.78           C  
ANISOU   78  CB  TYR A  13     5527   1922   1206    740   1177    -71       C  
ATOM     79  CG  TYR A  13      24.753  42.512  49.244  1.00 25.55           C  
ANISOU   79  CG  TYR A  13     6268   1868   1571    423   1012    584       C  
ATOM     80  CD1 TYR A  13      26.033  41.994  49.022  1.00 25.49           C  
ANISOU   80  CD1 TYR A  13     6464   1573   1648    629    336    511       C  
ATOM     81  CD2 TYR A  13      23.762  41.624  49.621  1.00 29.01           C  
ANISOU   81  CD2 TYR A  13     6865   2055   2102   -106   1256    323       C  
ATOM     82  CE1 TYR A  13      26.295  40.649  49.212  1.00 27.24           C  
ANISOU   82  CE1 TYR A  13     7080   1601   1670    524    810    146       C  
ATOM     83  CE2 TYR A  13      24.019  40.283  49.832  1.00 31.36           C  
ANISOU   83  CE2 TYR A  13     7545   2009   2361   -272   1057    194       C  
ATOM     84  CZ  TYR A  13      25.295  39.800  49.601  1.00 30.49           C  
ANISOU   84  CZ  TYR A  13     7805   1660   2119    -99    569     84       C  
ATOM     85  OH  TYR A  13      25.535  38.473  49.847  1.00 34.08           O  
ANISOU   85  OH  TYR A  13     8689   1648   2611    -14   -221   -162       O  
ATOM     86  N   LEU A  14      26.983  45.832  49.302  1.00 23.45           N  
ANISOU   86  N   LEU A  14     5510   1719   1681    460     44   -620       N  
ATOM     87  CA  LEU A  14      28.432  46.024  49.278  1.00 23.42           C  
ANISOU   87  CA  LEU A  14     5063   2061   1775    913   -434   -449       C  
ATOM     88  C   LEU A  14      28.948  46.628  50.562  1.00 22.83           C  
ANISOU   88  C   LEU A  14     4630   2287   1758   1194   -866   -547       C  
ATOM     89  O   LEU A  14      29.991  46.250  51.112  1.00 23.07           O  
ANISOU   89  O   LEU A  14     4928   2075   1762    962  -1129   -296       O  
ATOM     90  CB  LEU A  14      28.776  47.001  48.100  1.00 22.33           C  
ANISOU   90  CB  LEU A  14     4747   2015   1723    878    -52   -684       C  
ATOM     91  CG  LEU A  14      28.713  46.343  46.707  1.00 22.65           C  
ANISOU   91  CG  LEU A  14     5012   1819   1776    503    -11   -520       C  
ATOM     92  CD1 LEU A  14      28.674  47.413  45.615  1.00 21.22           C  
ANISOU   92  CD1 LEU A  14     4411   1940   1711   -107   -513   -121       C  
ATOM     93  CD2 LEU A  14      29.926  45.426  46.535  1.00 22.24           C  
ANISOU   93  CD2 LEU A  14     4854   1929   1668    435     40   -550       C  
ATOM     94  N   GLN A  15      28.274  47.685  51.058  1.00 23.85           N  
ANISOU   94  N   GLN A  15     4947   2133   1983   1127   -214   -566       N  
ATOM     95  CA  GLN A  15      28.831  48.366  52.222  1.00 25.55           C  
ANISOU   95  CA  GLN A  15     5459   2339   1908   1377   -261   -769       C  
ATOM     96  C   GLN A  15      28.710  47.530  53.484  1.00 27.95           C  
ANISOU   96  C   GLN A  15     6398   2294   1929   1612    143   -707       C  
ATOM     97  O   GLN A  15      29.341  47.874  54.492  1.00 33.34           O  
ANISOU   97  O   GLN A  15     7508   3319   1842    730    321   -329       O  
ATOM     98  CB  GLN A  15      28.183  49.734  52.409  1.00 23.08           C  
ANISOU   98  CB  GLN A  15     5042   2393   1333   1241   -543   -735       C  
ATOM     99  CG  GLN A  15      28.612  50.746  51.359  1.00 22.31           C  
ANISOU   99  CG  GLN A  15     4617   2414   1444    927   -795   -798       C  
ATOM    100  CD  GLN A  15      28.340  52.167  51.799  1.00 21.02           C  
ANISOU  100  CD  GLN A  15     3991   2399   1596    775   -664   -453       C  
ATOM    101  OE1 GLN A  15      27.246  52.494  52.266  1.00 22.24           O  
ANISOU  101  OE1 GLN A  15     4052   2344   2053    365   -110    398       O  
ATOM    102  NE2 GLN A  15      29.303  53.040  51.577  1.00 19.61           N  
ANISOU  102  NE2 GLN A  15     3467   2566   1416   1066   -261   -278       N  
ATOM    103  N   THR A  16      27.874  46.515  53.446  1.00 31.82           N  
ANISOU  103  N   THR A  16     7806   2246   2038    867   -118     29       N  
ATOM    104  CA  THR A  16      27.596  45.638  54.566  1.00 32.67           C  
ANISOU  104  CA  THR A  16     7922   2516   1977    738    526     71       C  
ATOM    105  C   THR A  16      28.441  44.368  54.534  1.00 33.16           C  
ANISOU  105  C   THR A  16     8308   2393   1900    829    108    407       C  
ATOM    106  O   THR A  16      28.986  44.005  55.591  1.00 32.28           O  
ANISOU  106  O   THR A  16     7457   2928   1881    912    585   -448       O  
ATOM    107  CB  THR A  16      26.099  45.203  54.585  1.00 34.89           C  
ANISOU  107  CB  THR A  16     7782   3400   2073    546   1688    358       C  
ATOM    108  OG1 THR A  16      25.296  46.396  54.726  1.00 39.32           O  
ANISOU  108  OG1 THR A  16     7035   3821   4085   1102   1540    292       O  
ATOM    109  CG2 THR A  16      25.823  44.320  55.792  1.00 38.07           C  
ANISOU  109  CG2 THR A  16     8487   4000   1977   -130   1389    511       C  
ATOM    110  N   TYR A  17      28.487  43.698  53.397  1.00 27.51           N  
ANISOU  110  N   TYR A  17     5735   2786   1933   1029   -116    141       N  
ATOM    111  CA  TYR A  17      29.085  42.372  53.251  1.00 27.26           C  
ANISOU  111  CA  TYR A  17     6005   2715   1636   1024   -594    451       C  
ATOM    112  C   TYR A  17      30.474  42.451  52.595  1.00 26.76           C  
ANISOU  112  C   TYR A  17     6292   2093   1783    937   -788    173       C  
ATOM    113  O   TYR A  17      31.179  41.423  52.554  1.00 27.90           O  
ANISOU  113  O   TYR A  17     6479   2064   2057   1405  -1087   -123       O  
ATOM    114  CB  TYR A  17      28.210  41.506  52.345  1.00 31.07           C  
ANISOU  114  CB  TYR A  17     6672   2867   2265    346    520    738       C  
ATOM    115  CG  TYR A  17      26.935  41.007  52.932  1.00 34.48           C  
ANISOU  115  CG  TYR A  17     6713   3604   2783     59    475   1368       C  
ATOM    116  CD1 TYR A  17      25.781  41.773  52.971  1.00 36.48           C  
ANISOU  116  CD1 TYR A  17     6425   3846   3590   -167    746   1200       C  
ATOM    117  CD2 TYR A  17      26.869  39.692  53.411  0.30 36.61           C  
ANISOU  117  CD2 TYR A  17     7081   3603   3226   -616    669   1286       C  
ATOM    118  CE1 TYR A  17      24.608  41.263  53.516  1.00 39.05           C  
ANISOU  118  CE1 TYR A  17     6662   4314   3860   -609   1149   1361       C  
ATOM    119  CE2 TYR A  17      25.713  39.187  53.946  0.80 39.75           C  
ANISOU  119  CE2 TYR A  17     7122   4127   3853   -921    670   1228       C  
ATOM    120  CZ  TYR A  17      24.580  39.978  53.997  0.50 39.88           C  
ANISOU  120  CZ  TYR A  17     6857   4328   3967   -899    865   1302       C  
ATOM    121  OH  TYR A  17      23.425  39.438  54.532  0.50 41.76           O  
ANISOU  121  OH  TYR A  17     6978   4796   4092  -1203   1061    598       O  
ATOM    122  N   HIS A  18      30.790  43.584  52.015  1.00 24.69           N  
ANISOU  122  N   HIS A  18     5892   2071   1419   1291   -635   -560       N  
ATOM    123  CA  HIS A  18      32.077  43.832  51.377  1.00 25.26           C  
ANISOU  123  CA  HIS A  18     5925   2529   1143   1206  -1171   -603       C  
ATOM    124  C   HIS A  18      32.339  42.866  50.238  1.00 23.85           C  
ANISOU  124  C   HIS A  18     5522   1951   1589   1099  -1177   -771       C  
ATOM    125  O   HIS A  18      33.477  42.490  49.976  1.00 26.01           O  
ANISOU  125  O   HIS A  18     5110   2432   2340   1416  -1020   -884       O  
ATOM    126  CB  HIS A  18      33.224  43.797  52.400  1.00 26.85           C  
ANISOU  126  CB  HIS A  18     5534   3364   1303   1202  -1203   -950       C  
ATOM    127  CG  HIS A  18      32.991  44.748  53.538  1.00 25.45           C  
ANISOU  127  CG  HIS A  18     4909   3446   1314   1113   -622   -547       C  
ATOM    128  ND1 HIS A  18      33.016  44.372  54.853  1.00 23.27           N  
ANISOU  128  ND1 HIS A  18     3967   3561   1314   1033   -803   -683       N  
ATOM    129  CD2 HIS A  18      32.614  46.056  53.525  1.00 26.66           C  
ANISOU  129  CD2 HIS A  18     5433   3348   1349    774   -248   -516       C  
ATOM    130  CE1 HIS A  18      32.701  45.402  55.613  1.00 24.47           C  
ANISOU  130  CE1 HIS A  18     4482   3483   1331    786   -383   -863       C  
ATOM    131  NE2 HIS A  18      32.446  46.439  54.820  1.00 24.12           N  
ANISOU  131  NE2 HIS A  18     4362   3476   1327    819   -257   -968       N  
ATOM    132  N   LYS A  19      31.258  42.503  49.554  1.00 22.82           N  
ANISOU  132  N   LYS A  19     5447   1887   1337   1237  -1292   -807       N  
ATOM    133  CA  LYS A  19      31.246  41.624  48.419  1.00 23.19           C  
ANISOU  133  CA  LYS A  19     5506   1831   1473   1159   -994   -610       C  
ATOM    134  C   LYS A  19      29.982  41.803  47.599  1.00 23.98           C  
ANISOU  134  C   LYS A  19     5816   1776   1518    388  -1094   -388       C  
ATOM    135  O   LYS A  19      28.964  42.309  48.081  1.00 22.78           O  
ANISOU  135  O   LYS A  19     5456   2215    984    643    203    -21       O  
ATOM    136  CB  LYS A  19      31.427  40.158  48.846  1.00 26.82           C  
ANISOU  136  CB  LYS A  19     5596   1715   2881   1088   -677   -651       C  
ATOM    137  CG  LYS A  19      30.255  39.568  49.598  1.00 32.80           C  
ANISOU  137  CG  LYS A  19     6822   2078   3561   -348   -316     54       C  
ATOM    138  CD  LYS A  19      30.350  38.057  49.730  1.00 36.90           C  
ANISOU  138  CD  LYS A  19     7941   2044   4036   -488   -461     53       C  
ATOM    139  CE  LYS A  19      30.031  37.589  51.127  1.00 40.46           C  
ANISOU  139  CE  LYS A  19     9242   2054   4078  -1648   -314   -263       C  
ATOM    140  NZ  LYS A  19      28.765  36.817  51.229  1.00 53.44           N  
ANISOU  140  NZ  LYS A  19    11276   4437   4591  -4079    458   -270       N  
ATOM    141  N   LEU A  20      30.025  41.352  46.333  1.00 21.22           N  
ANISOU  141  N   LEU A  20     5157   1266   1638    305   -560   -655       N  
ATOM    142  CA  LEU A  20      28.790  41.406  45.543  1.00 22.01           C  
ANISOU  142  CA  LEU A  20     4966   1687   1710    235     12   -512       C  
ATOM    143  C   LEU A  20      27.888  40.236  45.925  1.00 21.56           C  
ANISOU  143  C   LEU A  20     5200   1681   1312    117    214   -590       C  
ATOM    144  O   LEU A  20      28.354  39.167  46.348  1.00 23.54           O  
ANISOU  144  O   LEU A  20     5580   1690   1675    471   -322   -361       O  
ATOM    145  CB  LEU A  20      29.126  41.320  44.048  1.00 21.19           C  
ANISOU  145  CB  LEU A  20     4842   1502   1706    -96    379   -735       C  
ATOM    146  CG  LEU A  20      29.642  42.585  43.377  1.00 19.63           C  
ANISOU  146  CG  LEU A  20     3877   1707   1872     -7    517   -445       C  
ATOM    147  CD1 LEU A  20      30.254  42.256  42.019  1.00 19.39           C  
ANISOU  147  CD1 LEU A  20     3612   1964   1793    501   -112   -553       C  
ATOM    148  CD2 LEU A  20      28.602  43.669  43.278  1.00 19.28           C  
ANISOU  148  CD2 LEU A  20     4124   1576   1627   -123    194   -145       C  
ATOM    149  N   PRO A  21      26.581  40.396  45.744  1.00 22.14           N  
ANISOU  149  N   PRO A  21     5117   2069   1226    -19    220   -253       N  
ATOM    150  CA  PRO A  21      25.700  39.233  45.951  1.00 23.89           C  
ANISOU  150  CA  PRO A  21     5338   2305   1434   -281    303   -473       C  
ATOM    151  C   PRO A  21      26.038  38.117  44.946  1.00 24.39           C  
ANISOU  151  C   PRO A  21     5472   2180   1614   -273    -91    338       C  
ATOM    152  O   PRO A  21      26.682  38.344  43.922  1.00 22.07           O  
ANISOU  152  O   PRO A  21     4867   1667   1850    -93    172   -324       O  
ATOM    153  CB  PRO A  21      24.318  39.780  45.660  1.00 24.15           C  
ANISOU  153  CB  PRO A  21     5120   2467   1589   -142    565   -619       C  
ATOM    154  CG  PRO A  21      24.423  41.205  45.399  1.00 22.98           C  
ANISOU  154  CG  PRO A  21     4826   2508   1396    -93     57    252       C  
ATOM    155  CD  PRO A  21      25.844  41.604  45.381  1.00 21.56           C  
ANISOU  155  CD  PRO A  21     4566   2280   1345    243    420   -252       C  
ATOM    156  N   ASP A  22      25.537  36.929  45.226  1.00 24.36           N  
ANISOU  156  N   ASP A  22     5303   2313   1638   -407   -118    -60       N  
ATOM    157  CA  ASP A  22      25.684  35.718  44.532  1.00 25.88           C  
ANISOU  157  CA  ASP A  22     5928   2216   1688   -496   -626    -36       C  
ATOM    158  C   ASP A  22      25.255  35.639  43.099  1.00 23.95           C  
ANISOU  158  C   ASP A  22     5469   1904   1728   -154     14   -499       C  
ATOM    159  O   ASP A  22      25.589  34.678  42.364  1.00 28.97           O  
ANISOU  159  O   ASP A  22     7484   1630   1892    105   -734   -311       O  
ATOM    160  CB  ASP A  22      25.126  34.524  45.338  1.00 33.00           C  
ANISOU  160  CB  ASP A  22     8175   2651   1711  -1982  -1151    508       C  
ATOM    161  CG  ASP A  22      23.611  34.477  45.288  1.00 39.47           C  
ANISOU  161  CG  ASP A  22     8469   4271   2258  -3289   -885    455       C  
ATOM    162  OD1 ASP A  22      23.063  34.652  44.164  0.50 40.60           O  
ANISOU  162  OD1 ASP A  22     7230   5241   2391  -2404   -758    870       O  
ATOM    163  OD2 ASP A  22      22.968  34.271  46.324  0.50 48.30           O  
ANISOU  163  OD2 ASP A  22     8750   6535   2395  -4561   -710    144       O  
ATOM    164  N   ASN A  23      24.443  36.574  42.625  1.00 23.62           N  
ANISOU  164  N   ASN A  23     5125   1982   1867   -562   -157    -54       N  
ATOM    165  CA  ASN A  23      23.982  36.568  41.258  1.00 22.51           C  
ANISOU  165  CA  ASN A  23     4736   1915   1903   -938    124   -553       C  
ATOM    166  C   ASN A  23      24.969  37.232  40.305  1.00 22.21           C  
ANISOU  166  C   ASN A  23     4568   2005   1866   -832     70   -592       C  
ATOM    167  O   ASN A  23      24.660  37.348  39.116  1.00 22.47           O  
ANISOU  167  O   ASN A  23     4182   2501   1854  -1073   -182   -142       O  
ATOM    168  CB  ASN A  23      22.615  37.236  41.119  1.00 24.11           C  
ANISOU  168  CB  ASN A  23     4560   2031   2571   -818   -272   -626       C  
ATOM    169  CG  ASN A  23      22.598  38.628  41.742  1.00 24.25           C  
ANISOU  169  CG  ASN A  23     4656   1963   2594   -788    -47   -233       C  
ATOM    170  OD1 ASN A  23      22.844  38.720  42.951  1.00 27.96           O  
ANISOU  170  OD1 ASN A  23     5549   2109   2576      0    423   -634       O  
ATOM    171  ND2 ASN A  23      22.343  39.657  40.983  1.00 24.60           N  
ANISOU  171  ND2 ASN A  23     4290   2071   2642   -513   1122   -499       N  
ATOM    172  N   TYR A  24      26.138  37.653  40.787  1.00 19.12           N  
ANISOU  172  N   TYR A  24     4007   1605   1651   -157    510   -527       N  
ATOM    173  CA  TYR A  24      27.133  38.257  39.920  1.00 16.78           C  
ANISOU  173  CA  TYR A  24     3418   1626   1332    420   -198   -428       C  
ATOM    174  C   TYR A  24      28.235  37.285  39.514  1.00 18.03           C  
ANISOU  174  C   TYR A  24     3492   1636   1722    721   -824   -361       C  
ATOM    175  O   TYR A  24      28.753  36.520  40.340  1.00 19.18           O  
ANISOU  175  O   TYR A  24     3931   1534   1823    841   -639   -413       O  
ATOM    176  CB  TYR A  24      27.744  39.502  40.622  1.00 15.70           C  
ANISOU  176  CB  TYR A  24     2821   1647   1496    474    -18   -661       C  
ATOM    177  CG  TYR A  24      26.814  40.701  40.551  1.00 14.38           C  
ANISOU  177  CG  TYR A  24     2806   1633   1025    268     52   -678       C  
ATOM    178  CD1 TYR A  24      26.745  41.501  39.415  1.00 13.39           C  
ANISOU  178  CD1 TYR A  24     2429   1669    991    -48    125    -78       C  
ATOM    179  CD2 TYR A  24      25.939  41.003  41.587  1.00 14.54           C  
ANISOU  179  CD2 TYR A  24     3279   1404    841    254     48   -150       C  
ATOM    180  CE1 TYR A  24      25.886  42.578  39.322  1.00 13.84           C  
ANISOU  180  CE1 TYR A  24     2602   1635   1021     82    126   -277       C  
ATOM    181  CE2 TYR A  24      25.036  42.054  41.483  1.00 14.96           C  
ANISOU  181  CE2 TYR A  24     3428   1376    880    398   -315    -46       C  
ATOM    182  CZ  TYR A  24      25.006  42.833  40.357  1.00 13.51           C  
ANISOU  182  CZ  TYR A  24     2802   1481    849    487    -62    115       C  
ATOM    183  OH  TYR A  24      24.134  43.905  40.274  1.00 14.50           O  
ANISOU  183  OH  TYR A  24     3084   1407   1018    304    245    219       O  
ATOM    184  N   ILE A  25      28.650  37.354  38.259  1.00 16.05           N  
ANISOU  184  N   ILE A  25     2495   1780   1825    934   -857   -596       N  
ATOM    185  CA  ILE A  25      29.846  36.674  37.770  1.00 17.22           C  
ANISOU  185  CA  ILE A  25     2836   1483   2223    477  -1075   -734       C  
ATOM    186  C   ILE A  25      30.745  37.629  37.016  1.00 16.20           C  
ANISOU  186  C   ILE A  25     2522   1550   2085    746   -981   -832       C  
ATOM    187  O   ILE A  25      30.260  38.631  36.451  1.00 16.75           O  
ANISOU  187  O   ILE A  25     2508   1482   2374    371   -427   -924       O  
ATOM    188  CB  ILE A  25      29.468  35.478  36.849  1.00 18.23           C  
ANISOU  188  CB  ILE A  25     3297   1421   2209    449   -557   -615       C  
ATOM    189  CG1 ILE A  25      28.563  35.946  35.693  1.00 18.49           C  
ANISOU  189  CG1 ILE A  25     3319   1448   2257    -47     46  -1044       C  
ATOM    190  CG2 ILE A  25      28.761  34.434  37.706  1.00 21.88           C  
ANISOU  190  CG2 ILE A  25     4680   1350   2283   -171  -1049   -157       C  
ATOM    191  CD1 ILE A  25      28.230  34.794  34.745  1.00 19.54           C  
ANISOU  191  CD1 ILE A  25     3483   1283   2660   -715    252   -645       C  
ATOM    192  N   THR A  26      32.039  37.346  36.928  1.00 17.56           N  
ANISOU  192  N   THR A  26     2518   1661   2492    666   -909  -1255       N  
ATOM    193  CA  THR A  26      32.931  38.271  36.209  1.00 19.93           C  
ANISOU  193  CA  THR A  26     2754   2230   2590    197   -828  -1267       C  
ATOM    194  C   THR A  26      32.806  38.054  34.703  1.00 16.65           C  
ANISOU  194  C   THR A  26     2152   1571   2602    433   -975   -947       C  
ATOM    195  O   THR A  26      32.291  37.035  34.256  1.00 16.79           O  
ANISOU  195  O   THR A  26     2045   1583   2751    240   -684  -1065       O  
ATOM    196  CB  THR A  26      34.396  38.073  36.601  1.00 19.08           C  
ANISOU  196  CB  THR A  26     2472   2555   2222    485  -1098  -1961       C  
ATOM    197  OG1 THR A  26      34.810  36.757  36.189  1.00 21.28           O  
ANISOU  197  OG1 THR A  26     2484   2553   3048    697  -1462  -1395       O  
ATOM    198  CG2 THR A  26      34.610  38.189  38.089  1.00 23.10           C  
ANISOU  198  CG2 THR A  26     2965   3567   2246    -87   -938  -1713       C  
ATOM    199  N   LYS A  27      33.385  38.997  33.926  1.00 16.97           N  
ANISOU  199  N   LYS A  27     2207   1512   2730    298   -743  -1046       N  
ATOM    200  CA  LYS A  27      33.330  38.851  32.466  1.00 16.09           C  
ANISOU  200  CA  LYS A  27     1538   1888   2687    -39   -378   -712       C  
ATOM    201  C   LYS A  27      34.018  37.561  32.017  1.00 16.03           C  
ANISOU  201  C   LYS A  27     1735   1929   2429    -39   -368   -799       C  
ATOM    202  O   LYS A  27      33.513  36.901  31.116  1.00 17.02           O  
ANISOU  202  O   LYS A  27     2291   2126   2049     61   -489   -940       O  
ATOM    203  CB  LYS A  27      33.950  40.054  31.747  1.00 18.54           C  
ANISOU  203  CB  LYS A  27     2155   1958   2930   -446    187  -1105       C  
ATOM    204  CG  LYS A  27      33.018  41.264  31.660  1.00 24.27           C  
ANISOU  204  CG  LYS A  27     3543   1774   3904    511   -324   -857       C  
ATOM    205  CD  LYS A  27      33.600  42.351  30.792  1.00 29.19           C  
ANISOU  205  CD  LYS A  27     4868   1775   4449   -265    106  -1032       C  
ATOM    206  CE  LYS A  27      34.768  43.056  31.394  1.00 34.13           C  
ANISOU  206  CE  LYS A  27     5460   2908   4600  -1136    112  -1251       C  
ATOM    207  NZ  LYS A  27      34.448  43.939  32.547  1.00 39.24           N  
ANISOU  207  NZ  LYS A  27     7357   3978   3576  -1922    341  -1361       N  
ATOM    208  N   SER A  28      35.129  37.202  32.662  1.00 16.57           N  
ANISOU  208  N   SER A  28     1722   1812   2761    250   -483  -1056       N  
ATOM    209  CA  SER A  28      35.883  35.991  32.293  1.00 18.89           C  
ANISOU  209  CA  SER A  28     1841   1893   3441    403    -11  -1316       C  
ATOM    210  C   SER A  28      35.094  34.731  32.577  1.00 16.17           C  
ANISOU  210  C   SER A  28     1579   1746   2818    708   -610   -991       C  
ATOM    211  O   SER A  28      35.067  33.786  31.794  1.00 17.45           O  
ANISOU  211  O   SER A  28     2227   1765   2637    738   -613  -1400       O  
ATOM    212  CB ASER A  28      37.212  35.963  33.077  0.50 20.70           C  
ANISOU  212  CB ASER A  28     1234   2258   4372    743   -108   -937       C  
ATOM    213  CB BSER A  28      37.182  35.960  33.149  0.50 20.32           C  
ANISOU  213  CB BSER A  28     1283   2090   4347    770   -126   -909       C  
ATOM    214  OG ASER A  28      37.920  34.770  32.764  0.50 22.79           O  
ANISOU  214  OG ASER A  28     1731   2012   4916    133    174  -1421       O  
ATOM    215  OG BSER A  28      38.218  36.566  32.408  0.50 28.61           O  
ANISOU  215  OG BSER A  28     2485   3380   5005   -842   -129   -368       O  
ATOM    216  N   GLU A  29      34.386  34.742  33.705  1.00 16.57           N  
ANISOU  216  N   GLU A  29     2015   1651   2629    662   -870   -340       N  
ATOM    217  CA  GLU A  29      33.523  33.636  34.065  1.00 15.02           C  
ANISOU  217  CA  GLU A  29     2136   1485   2083    708   -897   -557       C  
ATOM    218  C   GLU A  29      32.356  33.496  33.099  1.00 14.20           C  
ANISOU  218  C   GLU A  29     2300   1176   1917    590   -590   -287       C  
ATOM    219  O   GLU A  29      32.048  32.360  32.668  1.00 13.77           O  
ANISOU  219  O   GLU A  29     2546   1089   1596    628   -371    -19       O  
ATOM    220  CB  GLU A  29      32.998  33.850  35.510  1.00 20.67           C  
ANISOU  220  CB  GLU A  29     3279   2706   1871    589  -1262   -580       C  
ATOM    221  CG  GLU A  29      34.124  33.674  36.518  1.00 22.53           C  
ANISOU  221  CG  GLU A  29     3046   3493   2021    905   -746   -639       C  
ATOM    222  CD  GLU A  29      33.610  33.870  37.939  1.00 25.07           C  
ANISOU  222  CD  GLU A  29     4157   3543   1824   1388   -674   -357       C  
ATOM    223  OE1 GLU A  29      32.796  34.773  38.162  1.00 24.78           O  
ANISOU  223  OE1 GLU A  29     4147   3480   1789   1318   -810   -139       O  
ATOM    224  OE2 GLU A  29      34.078  33.111  38.813  1.00 29.03           O  
ANISOU  224  OE2 GLU A  29     5840   3084   2107   1795   -346     -5       O  
ATOM    225  N   ALA A  30      31.756  34.596  32.701  1.00 13.59           N  
ANISOU  225  N   ALA A  30     2572   1116   1476    385   -546   -481       N  
ATOM    226  CA  ALA A  30      30.644  34.567  31.714  1.00 13.09           C  
ANISOU  226  CA  ALA A  30     2512   1153   1308    446   -655   -309       C  
ATOM    227  C   ALA A  30      31.133  34.062  30.380  1.00 11.94           C  
ANISOU  227  C   ALA A  30     1882   1214   1439    407   -448   -265       C  
ATOM    228  O   ALA A  30      30.469  33.238  29.731  1.00 12.45           O  
ANISOU  228  O   ALA A  30     2185   1351   1196    127   -326   -251       O  
ATOM    229  CB  ALA A  30      30.048  35.977  31.611  1.00 12.69           C  
ANISOU  229  CB  ALA A  30     2462   1147   1213    307   -231   -283       C  
ATOM    230  N   GLN A  31      32.280  34.565  29.910  1.00 13.57           N  
ANISOU  230  N   GLN A  31     2144   1407   1606    121   -371   -346       N  
ATOM    231  CA  GLN A  31      32.806  34.074  28.628  1.00 12.83           C  
ANISOU  231  CA  GLN A  31     1796   1359   1720    125     71   -248       C  
ATOM    232  C   GLN A  31      33.025  32.575  28.662  1.00 13.43           C  
ANISOU  232  C   GLN A  31     2106   1395   1601    181    -32   -322       C  
ATOM    233  O   GLN A  31      32.737  31.881  27.678  1.00 13.31           O  
ANISOU  233  O   GLN A  31     2114   1339   1604    161     -2   -865       O  
ATOM    234  CB AGLN A  31      34.121  34.800  28.298  0.50 14.93           C  
ANISOU  234  CB AGLN A  31     1909   1620   2145    -88    497    -78       C  
ATOM    235  CB BGLN A  31      34.089  34.824  28.267  0.50 14.96           C  
ANISOU  235  CB BGLN A  31     1882   1655   2147    -82    454    -55       C  
ATOM    236  CG AGLN A  31      33.931  36.266  27.895  0.50 18.22           C  
ANISOU  236  CG AGLN A  31     2796   1558   2569   -412    366    184       C  
ATOM    237  CG BGLN A  31      33.849  36.319  28.007  0.50 19.11           C  
ANISOU  237  CG BGLN A  31     3092   1561   2609   -588    456    145       C  
ATOM    238  CD AGLN A  31      35.248  37.013  27.794  0.50 21.48           C  
ANISOU  238  CD AGLN A  31     3565   1894   2703  -1128    836     69       C  
ATOM    239  CD BGLN A  31      35.100  37.025  27.530  0.50 22.41           C  
ANISOU  239  CD BGLN A  31     3740   2001   2774  -1266    983     26       C  
ATOM    240  OE1AGLN A  31      36.187  36.774  28.552  0.50 22.62           O  
ANISOU  240  OE1AGLN A  31     3286   2444   2864  -1369   -139     67       O  
ATOM    241  OE1BGLN A  31      35.825  36.527  26.657  0.50 22.37           O  
ANISOU  241  OE1BGLN A  31     2923   2758   2820   -829    886   -181       O  
ATOM    242  NE2AGLN A  31      35.376  37.916  26.823  0.50 25.73           N  
ANISOU  242  NE2AGLN A  31     4955   2396   2426  -1939    968     79       N  
ATOM    243  NE2BGLN A  31      35.375  38.209  28.073  0.50 27.83           N  
ANISOU  243  NE2BGLN A  31     5679   2435   2460  -2617    373    -57       N  
ATOM    244  N   ALA A  32      33.563  32.060  29.773  1.00 13.39           N  
ANISOU  244  N   ALA A  32     2103   1382   1604    214   -127   -378       N  
ATOM    245  CA  ALA A  32      33.842  30.617  29.829  1.00 14.36           C  
ANISOU  245  CA  ALA A  32     2464   1358   1635    197   -515   -130       C  
ATOM    246  C   ALA A  32      32.565  29.811  29.725  1.00 13.16           C  
ANISOU  246  C   ALA A  32     2213   1229   1559    461   -474   -764       C  
ATOM    247  O   ALA A  32      32.604  28.674  29.197  1.00 13.34           O  
ANISOU  247  O   ALA A  32     2460   1227   1383    431    -35   -590       O  
ATOM    248  CB  ALA A  32      34.696  30.226  30.980  1.00 14.61           C  
ANISOU  248  CB  ALA A  32     2250   1375   1926    303   -457   -147       C  
ATOM    249  N   LEU A  33      31.478  30.300  30.279  1.00 12.44           N  
ANISOU  249  N   LEU A  33     2149   1485   1094    503   -164   -301       N  
ATOM    250  CA  LEU A  33      30.179  29.646  30.226  1.00 12.30           C  
ANISOU  250  CA  LEU A  33     2191   1334   1151    450    -95   -170       C  
ATOM    251  C   LEU A  33      29.500  29.717  28.887  1.00 11.98           C  
ANISOU  251  C   LEU A  33     2283   1092   1176    214   -272   -329       C  
ATOM    252  O   LEU A  33      28.469  29.068  28.637  1.00 14.07           O  
ANISOU  252  O   LEU A  33     2747   1286   1313   -302   -127   -198       O  
ATOM    253  CB  LEU A  33      29.243  30.216  31.314  1.00 12.72           C  
ANISOU  253  CB  LEU A  33     2109   1581   1143    525   -108   -259       C  
ATOM    254  CG  LEU A  33      29.512  29.793  32.724  1.00 15.14           C  
ANISOU  254  CG  LEU A  33     3011   1611   1131    349   -160   -589       C  
ATOM    255  CD1 LEU A  33      29.008  30.699  33.798  1.00 16.96           C  
ANISOU  255  CD1 LEU A  33     3764   1562   1118    255    442   -283       C  
ATOM    256  CD2 LEU A  33      29.096  28.344  32.960  1.00 21.14           C  
ANISOU  256  CD2 LEU A  33     5195   1464   1373     -9   -314   -259       C  
ATOM    257  N   GLY A  34      30.010  30.521  27.948  1.00 10.85           N  
ANISOU  257  N   GLY A  34     1762   1233   1127    272   -216   -238       N  
ATOM    258  CA  GLY A  34      29.417  30.655  26.661  1.00 11.10           C  
ANISOU  258  CA  GLY A  34     1947   1134   1136    186   -185   -208       C  
ATOM    259  C   GLY A  34      28.848  32.003  26.308  1.00  9.73           C  
ANISOU  259  C   GLY A  34     1560   1111   1025   -197   -287   -382       C  
ATOM    260  O   GLY A  34      28.189  32.125  25.263  1.00  9.98           O  
ANISOU  260  O   GLY A  34     1571   1359    862   -123      0   -288       O  
ATOM    261  N   TRP A  35      29.019  33.030  27.143  1.00  9.98           N  
ANISOU  261  N   TRP A  35     1779   1069    944    -52   -259     80       N  
ATOM    262  CA  TRP A  35      28.562  34.368  26.828  1.00 10.03           C  
ANISOU  262  CA  TRP A  35     1564   1113   1134     80   -255    -59       C  
ATOM    263  C   TRP A  35      29.345  34.918  25.618  1.00  9.77           C  
ANISOU  263  C   TRP A  35     1578    896   1237    -28   -335     10       C  
ATOM    264  O   TRP A  35      30.561  34.996  25.627  1.00 11.96           O  
ANISOU  264  O   TRP A  35     1502   1352   1693   -131   -220   -351       O  
ATOM    265  CB  TRP A  35      28.731  35.315  27.997  1.00 10.42           C  
ANISOU  265  CB  TRP A  35     1764   1039   1155    206    -17   -312       C  
ATOM    266  CG  TRP A  35      28.349  36.738  27.692  1.00 10.80           C  
ANISOU  266  CG  TRP A  35     1571   1070   1465    178   -157   -214       C  
ATOM    267  CD1 TRP A  35      27.179  37.220  27.176  1.00 11.56           C  
ANISOU  267  CD1 TRP A  35     1595   1028   1768     85   -263   -181       C  
ATOM    268  CD2 TRP A  35      29.165  37.891  27.954  1.00 10.24           C  
ANISOU  268  CD2 TRP A  35     1827   1144    921    -52   -155   -116       C  
ATOM    269  NE1 TRP A  35      27.196  38.583  27.100  1.00 11.40           N  
ANISOU  269  NE1 TRP A  35     1679   1084   1567    130   -311   -187       N  
ATOM    270  CE2 TRP A  35      28.418  39.035  27.534  1.00 11.16           C  
ANISOU  270  CE2 TRP A  35     1961   1093   1186   -157    -27   -167       C  
ATOM    271  CE3 TRP A  35      30.450  38.069  28.453  1.00 11.38           C  
ANISOU  271  CE3 TRP A  35     1637   1347   1338     69   -102    -91       C  
ATOM    272  CZ2 TRP A  35      28.941  40.322  27.629  1.00 13.30           C  
ANISOU  272  CZ2 TRP A  35     2225   1100   1729   -199     18    -84       C  
ATOM    273  CZ3 TRP A  35      30.955  39.353  28.541  1.00 14.66           C  
ANISOU  273  CZ3 TRP A  35     1811   1588   2173   -356   -679     64       C  
ATOM    274  CH2 TRP A  35      30.209  40.451  28.137  1.00 14.80           C  
ANISOU  274  CH2 TRP A  35     2530   1265   1830   -703    406    151       C  
ATOM    275  N   VAL A  36      28.575  35.366  24.657  1.00 10.30           N  
ANISOU  275  N   VAL A  36     1572   1226   1117    -38    291    -27       N  
ATOM    276  CA  VAL A  36      29.057  36.031  23.462  1.00 11.44           C  
ANISOU  276  CA  VAL A  36     1852   1461   1033    -94     99    258       C  
ATOM    277  C   VAL A  36      28.386  37.405  23.391  1.00 10.12           C  
ANISOU  277  C   VAL A  36     1589   1475    782    -13   -382    315       C  
ATOM    278  O   VAL A  36      27.197  37.504  23.129  1.00 12.00           O  
ANISOU  278  O   VAL A  36     1625   1614   1322   -120   -332    269       O  
ATOM    279  CB  VAL A  36      28.772  35.211  22.216  1.00 13.16           C  
ANISOU  279  CB  VAL A  36     2451   1421   1128    121     78    655       C  
ATOM    280  CG1 VAL A  36      29.278  35.948  20.973  1.00 15.35           C  
ANISOU  280  CG1 VAL A  36     3094   1813    924    642     -4    236       C  
ATOM    281  CG2 VAL A  36      29.420  33.822  22.343  1.00 15.70           C  
ANISOU  281  CG2 VAL A  36     2969   1422   1573    316    947    371       C  
ATOM    282  N   ALA A  37      29.186  38.442  23.664  1.00 11.46           N  
ANISOU  282  N   ALA A  37     1518   1494   1344    -28    -83    -21       N  
ATOM    283  CA  ALA A  37      28.622  39.770  23.814  1.00 11.89           C  
ANISOU  283  CA  ALA A  37     1796   1419   1301   -150    -29    254       C  
ATOM    284  C   ALA A  37      27.738  40.156  22.651  1.00 11.89           C  
ANISOU  284  C   ALA A  37     1902   1412   1205    120    269   -263       C  
ATOM    285  O   ALA A  37      26.695  40.790  22.789  1.00 11.19           O  
ANISOU  285  O   ALA A  37     1960   1370    923    -91    178    134       O  
ATOM    286  CB  ALA A  37      29.683  40.826  24.071  1.00 14.41           C  
ANISOU  286  CB  ALA A  37     1918   1561   1997   -327   -259    283       C  
ATOM    287  N   SER A  38      28.224  39.900  21.429  1.00 11.54           N  
ANISOU  287  N   SER A  38     1582   1543   1259    313   -225   -148       N  
ATOM    288  CA  SER A  38      27.536  40.357  20.243  1.00 12.39           C  
ANISOU  288  CA  SER A  38     1815   1682   1210    204   -111    127       C  
ATOM    289  C   SER A  38      26.226  39.622  19.978  1.00 12.42           C  
ANISOU  289  C   SER A  38     1608   1884   1228    297   -296     14       C  
ATOM    290  O   SER A  38      25.481  40.058  19.114  1.00 13.44           O  
ANISOU  290  O   SER A  38     2007   2016   1085    -60   -283    251       O  
ATOM    291  CB ASER A  38      28.441  40.228  19.005  0.50 12.91           C  
ANISOU  291  CB ASER A  38     1801   1851   1254     75    -12    -81       C  
ATOM    292  CB BSER A  38      28.450  40.187  19.006  0.50 12.02           C  
ANISOU  292  CB BSER A  38     1740   1553   1272    242    -16    -80       C  
ATOM    293  OG ASER A  38      29.486  41.180  19.027  0.50 12.45           O  
ANISOU  293  OG ASER A  38     1967   1529   1235    104    435   -206       O  
ATOM    294  OG BSER A  38      28.744  38.805  18.871  0.50 14.16           O  
ANISOU  294  OG BSER A  38     2115   1444   1822    -57    296    -97       O  
ATOM    295  N   LYS A  39      25.965  38.519  20.677  1.00 13.31           N  
ANISOU  295  N   LYS A  39     1917   1983   1156    -92   -199   -182       N  
ATOM    296  CA  LYS A  39      24.705  37.792  20.548  1.00 14.28           C  
ANISOU  296  CA  LYS A  39     1898   2195   1331   -144   -392    -12       C  
ATOM    297  C   LYS A  39      23.722  38.118  21.651  1.00 14.79           C  
ANISOU  297  C   LYS A  39     2192   2135   1291   -552   -564    408       C  
ATOM    298  O   LYS A  39      22.606  37.611  21.679  1.00 13.44           O  
ANISOU  298  O   LYS A  39     1798   1558   1751    -15   -273   -158       O  
ATOM    299  CB  LYS A  39      24.940  36.282  20.512  1.00 18.02           C  
ANISOU  299  CB  LYS A  39     2198   2151   2500   -132    284   -637       C  
ATOM    300  CG  LYS A  39      25.678  35.787  19.289  1.00 18.78           C  
ANISOU  300  CG  LYS A  39     2632   2017   2486     71    503   -991       C  
ATOM    301  CD  LYS A  39      26.022  34.326  19.463  1.00 24.34           C  
ANISOU  301  CD  LYS A  39     3744   1958   3547    251    756  -1305       C  
ATOM    302  CE  LYS A  39      26.279  33.590  18.175  1.00 28.55           C  
ANISOU  302  CE  LYS A  39     5426   1818   3603    433   -209   -747       C  
ATOM    303  NZ  LYS A  39      26.017  32.130  18.329  1.00 40.73           N  
ANISOU  303  NZ  LYS A  39     9188   1879   4410   -299   -931  -1441       N  
ATOM    304  N   GLY A  40      24.145  38.902  22.656  1.00 11.90           N  
ANISOU  304  N   GLY A  40     1458   1475   1589    167    172    134       N  
ATOM    305  CA  GLY A  40      23.188  39.271  23.716  1.00 11.88           C  
ANISOU  305  CA  GLY A  40     1481   1329   1704    135     29    433       C  
ATOM    306  C   GLY A  40      22.638  38.091  24.476  1.00 12.38           C  
ANISOU  306  C   GLY A  40     1976   1299   1430   -174   -127    218       C  
ATOM    307  O   GLY A  40      21.446  38.142  24.893  1.00 11.97           O  
ANISOU  307  O   GLY A  40     1853   1302   1395    107    -66    328       O  
ATOM    308  N   ASN A  41      23.419  37.055  24.711  1.00 10.36           N  
ANISOU  308  N   ASN A  41     1528   1449    960   -145    -32    320       N  
ATOM    309  CA  ASN A  41      22.957  35.782  25.205  1.00  9.76           C  
ANISOU  309  CA  ASN A  41     1478   1313    916   -203    -16    166       C  
ATOM    310  C   ASN A  41      23.226  35.464  26.639  1.00  9.17           C  
ANISOU  310  C   ASN A  41     1407   1106    973    -35    262   -140       C  
ATOM    311  O   ASN A  41      23.081  34.322  27.093  1.00 11.10           O  
ANISOU  311  O   ASN A  41     2029   1076   1112   -119    182      0       O  
ATOM    312  CB  ASN A  41      23.460  34.623  24.286  1.00 10.43           C  
ANISOU  312  CB  ASN A  41     1658   1439    865   -289   -293   -123       C  
ATOM    313  CG  ASN A  41      24.945  34.349  24.494  1.00 11.02           C  
ANISOU  313  CG  ASN A  41     1769   1031   1388   -259   -238     47       C  
ATOM    314  OD1 ASN A  41      25.654  35.174  25.091  1.00 11.11           O  
ANISOU  314  OD1 ASN A  41     1565   1257   1399   -195    275   -219       O  
ATOM    315  ND2 ASN A  41      25.448  33.259  23.933  1.00 13.81           N  
ANISOU  315  ND2 ASN A  41     2260   1108   1880    437    167   -354       N  
ATOM    316  N   LEU A  42      23.583  36.452  27.480  1.00 10.76           N  
ANISOU  316  N   LEU A  42     2124   1067    899     56     29   -196       N  
ATOM    317  CA  LEU A  42      23.941  36.128  28.861  1.00 10.63           C  
ANISOU  317  CA  LEU A  42     2021   1145    872    314   -239    -98       C  
ATOM    318  C   LEU A  42      22.890  35.354  29.604  1.00 11.33           C  
ANISOU  318  C   LEU A  42     2325   1014    966     47    184     -6       C  
ATOM    319  O   LEU A  42      23.154  34.395  30.324  1.00 12.42           O  
ANISOU  319  O   LEU A  42     2565    993   1162     71     66     23       O  
ATOM    320  CB  LEU A  42      24.329  37.422  29.627  1.00 11.60           C  
ANISOU  320  CB  LEU A  42     1916   1456   1034    -86    -57   -676       C  
ATOM    321  CG  LEU A  42      24.851  37.229  31.027  1.00 11.35           C  
ANISOU  321  CG  LEU A  42     1607   1670   1035   -190     82   -615       C  
ATOM    322  CD1 LEU A  42      26.154  36.386  30.999  1.00 12.40           C  
ANISOU  322  CD1 LEU A  42     1750   1650   1312    382   -160   -229       C  
ATOM    323  CD2 LEU A  42      25.123  38.574  31.700  1.00 12.49           C  
ANISOU  323  CD2 LEU A  42     2216   1528   1004    301   -159   -542       C  
ATOM    324  N   ALA A  43      21.610  35.746  29.481  1.00 12.31           N  
ANISOU  324  N   ALA A  43     2323   1095   1259     34    537     71       N  
ATOM    325  CA  ALA A  43      20.551  35.125  30.244  1.00 13.73           C  
ANISOU  325  CA  ALA A  43     2192   1248   1775    -62    509    -13       C  
ATOM    326  C   ALA A  43      20.242  33.707  29.800  1.00 13.92           C  
ANISOU  326  C   ALA A  43     2043   1225   2020     28    180    184       C  
ATOM    327  O   ALA A  43      19.668  32.915  30.575  1.00 17.39           O  
ANISOU  327  O   ALA A  43     2917   1594   2096   -762    461    -16       O  
ATOM    328  CB  ALA A  43      19.286  35.964  30.218  1.00 16.02           C  
ANISOU  328  CB  ALA A  43     2103   1296   2689    284    904    139       C  
ATOM    329  N   ASP A  44      20.678  33.335  28.624  1.00 13.85           N  
ANISOU  329  N   ASP A  44     2001   1217   2046    315    569    126       N  
ATOM    330  CA  ASP A  44      20.502  31.962  28.156  1.00 13.56           C  
ANISOU  330  CA  ASP A  44     1911   1236   2006    146     46    117       C  
ATOM    331  C   ASP A  44      21.581  31.018  28.703  1.00 14.45           C  
ANISOU  331  C   ASP A  44     1860   1212   2418    216    126      0       C  
ATOM    332  O   ASP A  44      21.337  29.814  28.935  1.00 14.29           O  
ANISOU  332  O   ASP A  44     2268   1229   1932     68    -88    174       O  
ATOM    333  CB  ASP A  44      20.553  31.897  26.633  1.00 20.23           C  
ANISOU  333  CB  ASP A  44     3512   2338   1838   -384   -190    563       C  
ATOM    334  CG  ASP A  44      19.444  32.664  25.956  1.00 20.02           C  
ANISOU  334  CG  ASP A  44     3727   2337   1541     33    441    716       C  
ATOM    335  OD1 ASP A  44      18.299  32.583  26.452  1.00 26.75           O  
ANISOU  335  OD1 ASP A  44     2610   3437   4115    593   -432     62       O  
ATOM    336  OD2 ASP A  44      19.693  33.268  24.897  1.00 27.73           O  
ANISOU  336  OD2 ASP A  44     5978   3216   1344    711   -510    517       O  
ATOM    337  N   VAL A  45      22.795  31.534  28.826  1.00 11.38           N  
ANISOU  337  N   VAL A  45     1906   1091   1325    263     91   -238       N  
ATOM    338  CA  VAL A  45      23.944  30.700  29.196  1.00 11.67           C  
ANISOU  338  CA  VAL A  45     2035   1103   1295    -58    471   -360       C  
ATOM    339  C   VAL A  45      24.238  30.699  30.663  1.00 11.24           C  
ANISOU  339  C   VAL A  45     1886   1149   1234     24    207   -504       C  
ATOM    340  O   VAL A  45      24.949  29.820  31.168  1.00 12.28           O  
ANISOU  340  O   VAL A  45     2021   1336   1308    522   -151    -92       O  
ATOM    341  CB  VAL A  45      25.182  31.059  28.371  1.00 11.02           C  
ANISOU  341  CB  VAL A  45     1811   1211   1167    335      9    161       C  
ATOM    342  CG1 VAL A  45      24.890  31.029  26.894  1.00 16.15           C  
ANISOU  342  CG1 VAL A  45     3342   1760   1035    834    224    464       C  
ATOM    343  CG2 VAL A  45      25.781  32.387  28.824  1.00 16.39           C  
ANISOU  343  CG2 VAL A  45     2764   1655   1810   -796    616   -315       C  
ATOM    344  N   ALA A  46      23.757  31.743  31.357  1.00 12.49           N  
ANISOU  344  N   ALA A  46     2363   1124   1257     36    201   -448       N  
ATOM    345  CA  ALA A  46      24.001  31.898  32.790  1.00 13.30           C  
ANISOU  345  CA  ALA A  46     2686   1163   1205   -211    -53    -75       C  
ATOM    346  C   ALA A  46      22.736  32.521  33.421  1.00 12.88           C  
ANISOU  346  C   ALA A  46     2361   1327   1205      8     19   -102       C  
ATOM    347  O   ALA A  46      22.723  33.683  33.780  1.00 12.95           O  
ANISOU  347  O   ALA A  46     2315   1294   1311    -13    389    -31       O  
ATOM    348  CB  ALA A  46      25.186  32.816  33.045  1.00 13.61           C  
ANISOU  348  CB  ALA A  46     2314   1583   1275    -59     56   -529       C  
ATOM    349  N   PRO A  47      21.673  31.739  33.465  1.00 16.12           N  
ANISOU  349  N   PRO A  47     2665   1556   1903   -399    524   -468       N  
ATOM    350  CA  PRO A  47      20.380  32.226  33.919  1.00 16.44           C  
ANISOU  350  CA  PRO A  47     2486   1794   1966   -412    376    -66       C  
ATOM    351  C   PRO A  47      20.476  32.863  35.309  1.00 16.37           C  
ANISOU  351  C   PRO A  47     2347   1953   1921   -349    444   -105       C  
ATOM    352  O   PRO A  47      21.052  32.276  36.223  1.00 18.11           O  
ANISOU  352  O   PRO A  47     3282   1678   1922   -378    653   -234       O  
ATOM    353  CB  PRO A  47      19.515  30.955  34.020  1.00 18.87           C  
ANISOU  353  CB  PRO A  47     2849   2084   2235   -815    472   -594       C  
ATOM    354  CG  PRO A  47      20.219  29.916  33.257  1.00 20.71           C  
ANISOU  354  CG  PRO A  47     3148   1766   2953   -823    594   -386       C  
ATOM    355  CD  PRO A  47      21.625  30.331  33.039  1.00 18.73           C  
ANISOU  355  CD  PRO A  47     2985   1493   2640   -606    501   -776       C  
ATOM    356  N   GLY A  48      19.905  34.044  35.447  1.00 15.97           N  
ANISOU  356  N   GLY A  48     2343   1944   1782   -441    726   -541       N  
ATOM    357  CA  GLY A  48      19.815  34.761  36.691  1.00 16.89           C  
ANISOU  357  CA  GLY A  48     2558   2013   1846   -391    749   -910       C  
ATOM    358  C   GLY A  48      21.073  35.511  37.065  1.00 16.89           C  
ANISOU  358  C   GLY A  48     2979   1674   1766   -716    473   -915       C  
ATOM    359  O   GLY A  48      21.102  36.174  38.097  1.00 19.14           O  
ANISOU  359  O   GLY A  48     3618   2093   1561   -829   1096   -652       O  
ATOM    360  N   LYS A  49      22.096  35.475  36.210  1.00 16.21           N  
ANISOU  360  N   LYS A  49     2851   1461   1848   -469   1055   -300       N  
ATOM    361  CA  LYS A  49      23.344  36.151  36.471  1.00 15.45           C  
ANISOU  361  CA  LYS A  49     2894   1548   1429   -560    117   -178       C  
ATOM    362  C   LYS A  49      23.484  37.516  35.810  1.00 15.51           C  
ANISOU  362  C   LYS A  49     2802   1480   1610   -356    -99   -117       C  
ATOM    363  O   LYS A  49      22.875  37.759  34.786  1.00 15.15           O  
ANISOU  363  O   LYS A  49     2646   1283   1825   -440    268   -360       O  
ATOM    364  CB  LYS A  49      24.543  35.277  36.173  1.00 17.43           C  
ANISOU  364  CB  LYS A  49     2931   1435   2258   -525    230   -465       C  
ATOM    365  CG  LYS A  49      24.553  33.922  36.837  1.00 20.02           C  
ANISOU  365  CG  LYS A  49     3967   1446   2193   -215   -344   -150       C  
ATOM    366  CD  LYS A  49      24.672  33.954  38.332  1.00 26.36           C  
ANISOU  366  CD  LYS A  49     5723   2146   2147   -143    479     23       C  
ATOM    367  CE  LYS A  49      25.129  32.623  38.917  1.00 27.97           C  
ANISOU  367  CE  LYS A  49     6596   2205   1825    175   -216    438       C  
ATOM    368  NZ  LYS A  49      24.668  32.442  40.323  1.00 34.81           N  
ANISOU  368  NZ  LYS A  49     8450   3004   1772   -868    187    193       N  
ATOM    369  N   SER A  50      24.273  38.401  36.428  1.00 13.94           N  
ANISOU  369  N   SER A  50     2821   1247   1227    -90    274   -386       N  
ATOM    370  CA  SER A  50      24.649  39.681  35.870  1.00 13.08           C  
ANISOU  370  CA  SER A  50     2373   1328   1267     -6    -74   -398       C  
ATOM    371  C   SER A  50      26.197  39.789  35.888  1.00 12.20           C  
ANISOU  371  C   SER A  50     2097   1453   1087    315   -484   -196       C  
ATOM    372  O   SER A  50      26.791  39.119  36.714  1.00 13.27           O  
ANISOU  372  O   SER A  50     2295   1666   1079    160    -67    -78       O  
ATOM    373  CB  SER A  50      24.127  40.854  36.727  1.00 13.95           C  
ANISOU  373  CB  SER A  50     2212   1213   1877    144    -73   -461       C  
ATOM    374  OG  SER A  50      22.716  40.956  36.639  1.00 14.40           O  
ANISOU  374  OG  SER A  50     2052   1506   1911    226     64     23       O  
ATOM    375  N   ILE A  51      26.768  40.561  34.976  1.00 13.24           N  
ANISOU  375  N   ILE A  51     2276   1634   1121    -78    257   -379       N  
ATOM    376  CA  ILE A  51      28.227  40.759  35.002  1.00 13.41           C  
ANISOU  376  CA  ILE A  51     2145   1421   1527    129     55   -587       C  
ATOM    377  C   ILE A  51      28.595  41.750  36.114  1.00 13.36           C  
ANISOU  377  C   ILE A  51     2203   1302   1571    100     -7   -351       C  
ATOM    378  O   ILE A  51      27.996  42.821  36.265  1.00 13.98           O  
ANISOU  378  O   ILE A  51     2394   1316   1600    237     32   -292       O  
ATOM    379  CB  ILE A  51      28.679  41.405  33.650  1.00 14.71           C  
ANISOU  379  CB  ILE A  51     1998   2074   1516   -203    523  -1030       C  
ATOM    380  CG1 ILE A  51      28.351  40.598  32.400  1.00 16.48           C  
ANISOU  380  CG1 ILE A  51     2719   1890   1652   -612    411   -403       C  
ATOM    381  CG2 ILE A  51      30.191  41.674  33.736  1.00 16.64           C  
ANISOU  381  CG2 ILE A  51     2033   2392   1899   -306   -132   -747       C  
ATOM    382  CD1 ILE A  51      28.956  39.259  32.425  1.00 19.44           C  
ANISOU  382  CD1 ILE A  51     2675   1811   2901   -536   -124   -869       C  
ATOM    383  N   GLY A  52      29.633  41.423  36.874  1.00 13.20           N  
ANISOU  383  N   GLY A  52     2472   1289   1252    282    -27   -503       N  
ATOM    384  CA  GLY A  52      30.119  42.327  37.916  1.00 13.83           C  
ANISOU  384  CA  GLY A  52     2640   1506   1108    396     79   -386       C  
ATOM    385  C   GLY A  52      31.352  41.815  38.606  1.00 14.19           C  
ANISOU  385  C   GLY A  52     2526   1483   1384    479   -536   -233       C  
ATOM    386  O   GLY A  52      31.602  40.606  38.651  1.00 16.98           O  
ANISOU  386  O   GLY A  52     2739   1398   2316    117   -779   -490       O  
ATOM    387  N   GLY A  53      32.142  42.732  39.188  1.00 14.92           N  
ANISOU  387  N   GLY A  53     2282   1315   2073    576   -694   -711       N  
ATOM    388  CA  GLY A  53      33.276  42.391  39.986  1.00 16.20           C  
ANISOU  388  CA  GLY A  53     2127   1642   2387    497  -1095   -500       C  
ATOM    389  C   GLY A  53      34.624  42.633  39.361  1.00 18.25           C  
ANISOU  389  C   GLY A  53     2235   1994   2705    228   -747  -1143       C  
ATOM    390  O   GLY A  53      35.651  42.459  40.015  1.00 19.64           O  
ANISOU  390  O   GLY A  53     2049   2724   2689    133   -695   -767       O  
ATOM    391  N   ASP A  54      34.663  43.080  38.105  1.00 19.50           N  
ANISOU  391  N   ASP A  54     2137   2644   2629    309      0  -1487       N  
ATOM    392  CA  ASP A  54      35.890  43.398  37.427  1.00 21.32           C  
ANISOU  392  CA  ASP A  54     2445   3085   2572    -41   -427  -1271       C  
ATOM    393  C   ASP A  54      36.470  44.740  37.856  1.00 19.77           C  
ANISOU  393  C   ASP A  54     2030   2955   2528    243   -200  -1599       C  
ATOM    394  O   ASP A  54      35.750  45.691  38.205  1.00 19.70           O  
ANISOU  394  O   ASP A  54     1746   3184   2557    813   -376  -1448       O  
ATOM    395  CB  ASP A  54      35.766  43.324  35.912  1.00 20.87           C  
ANISOU  395  CB  ASP A  54     2666   2715   2550    246   -317  -1552       C  
ATOM    396  CG  ASP A  54      35.431  41.935  35.407  1.00 22.92           C  
ANISOU  396  CG  ASP A  54     3326   2579   2803    116   -265  -1851       C  
ATOM    397  OD1 ASP A  54      36.254  41.038  35.646  1.00 27.93           O  
ANISOU  397  OD1 ASP A  54     2773   2730   5110    158   -982  -1926       O  
ATOM    398  OD2 ASP A  54      34.350  41.737  34.818  1.00 24.19           O  
ANISOU  398  OD2 ASP A  54     3388   2334   3468   -123   -446  -1990       O  
ATOM    399  N   ILE A  55      37.787  44.830  37.789  1.00 21.91           N  
ANISOU  399  N   ILE A  55     1996   2990   3340    341   -339  -1657       N  
ATOM    400  CA  ILE A  55      38.484  46.081  38.041  1.00 24.26           C  
ANISOU  400  CA  ILE A  55     2114   3136   3968     81    136  -1692       C  
ATOM    401  C   ILE A  55      38.180  47.102  36.939  1.00 23.86           C  
ANISOU  401  C   ILE A  55     2033   3082   3951    120   1214  -2419       C  
ATOM    402  O   ILE A  55      38.128  46.771  35.753  1.00 24.90           O  
ANISOU  402  O   ILE A  55     2939   2523   3997   -338   1070  -1531       O  
ATOM    403  CB  ILE A  55      40.024  45.845  38.073  1.00 26.11           C  
ANISOU  403  CB  ILE A  55     2000   2984   4935    360    -55   -698       C  
ATOM    404  CG1 ILE A  55      40.426  44.998  39.299  1.00 26.93           C  
ANISOU  404  CG1 ILE A  55     1840   3086   5306    952    194   -210       C  
ATOM    405  CG2 ILE A  55      40.720  47.205  38.143  1.00 30.14           C  
ANISOU  405  CG2 ILE A  55     2460   3230   5762   -265    -81  -1924       C  
ATOM    406  CD1 ILE A  55      41.821  45.319  39.797  1.00 31.50           C  
ANISOU  406  CD1 ILE A  55     3057   4161   4751    472   1111   -281       C  
ATOM    407  N   PHE A  56      37.870  48.306  37.378  1.00 22.83           N  
ANISOU  407  N   PHE A  56     1992   3221   3461    328    201  -1963       N  
ATOM    408  CA  PHE A  56      37.642  49.446  36.484  1.00 24.68           C  
ANISOU  408  CA  PHE A  56     2578   3055   3744    206    500  -1818       C  
ATOM    409  C   PHE A  56      38.884  50.362  36.556  1.00 26.75           C  
ANISOU  409  C   PHE A  56     2598   3117   4448    168   1216  -1717       C  
ATOM    410  O   PHE A  56      39.256  50.781  37.644  1.00 27.76           O  
ANISOU  410  O   PHE A  56     2106   3928   4513   -212    278  -2331       O  
ATOM    411  CB  PHE A  56      36.427  50.231  37.020  1.00 24.50           C  
ANISOU  411  CB  PHE A  56     2764   2914   3631     39   -305  -1039       C  
ATOM    412  CG  PHE A  56      36.119  51.459  36.192  1.00 24.27           C  
ANISOU  412  CG  PHE A  56     2700   3000   3521    212   -209   -332       C  
ATOM    413  CD1 PHE A  56      35.537  51.313  34.937  1.00 25.66           C  
ANISOU  413  CD1 PHE A  56     3018   3291   3440     17     61    -87       C  
ATOM    414  CD2 PHE A  56      36.401  52.724  36.673  1.00 24.28           C  
ANISOU  414  CD2 PHE A  56     2786   2930   3508    434   -327     19       C  
ATOM    415  CE1 PHE A  56      35.175  52.434  34.215  1.00 26.88           C  
ANISOU  415  CE1 PHE A  56     3755   3328   3130   -102    865   -530       C  
ATOM    416  CE2 PHE A  56      36.122  53.848  35.897  1.00 25.62           C  
ANISOU  416  CE2 PHE A  56     3433   3005   3296     73    202   -202       C  
ATOM    417  CZ  PHE A  56      35.574  53.687  34.642  1.00 26.47           C  
ANISOU  417  CZ  PHE A  56     3546   3281   3228     39    493    -83       C  
ATOM    418  N   SER A  57      39.541  50.592  35.437  1.00 27.27           N  
ANISOU  418  N   SER A  57     2446   3397   4520    185   1180   -927       N  
ATOM    419  CA  SER A  57      40.767  51.317  35.370  1.00 28.58           C  
ANISOU  419  CA  SER A  57     2605   3571   4685     17   1712   -796       C  
ATOM    420  C   SER A  57      40.763  52.725  35.881  1.00 31.53           C  
ANISOU  420  C   SER A  57     3120   3447   5412   -189   1789   -308       C  
ATOM    421  O   SER A  57      41.834  53.193  36.359  1.00 32.73           O  
ANISOU  421  O   SER A  57     3199   3228   6010   -278    990     90       O  
ATOM    422  CB  SER A  57      41.440  51.259  33.989  1.00 32.50           C  
ANISOU  422  CB  SER A  57     3431   4435   4483   -915   1913   -800       C  
ATOM    423  OG  SER A  57      42.480  52.221  33.915  1.00 42.69           O  
ANISOU  423  OG  SER A  57     5356   6505   4358  -2920   1694   -891       O  
ATOM    424  N   ASN A  58      39.716  53.477  35.690  1.00 32.30           N  
ANISOU  424  N   ASN A  58     2991   3478   5805     64   1824     52       N  
ATOM    425  CA  ASN A  58      39.654  54.897  36.058  1.00 35.12           C  
ANISOU  425  CA  ASN A  58     3812   3365   6168    -86   1862   -200       C  
ATOM    426  C   ASN A  58      40.737  55.685  35.308  1.00 34.49           C  
ANISOU  426  C   ASN A  58     3663   3308   6135    108   1042    499       C  
ATOM    427  O   ASN A  58      41.336  56.596  35.896  1.00 36.23           O  
ANISOU  427  O   ASN A  58     3599   4291   5874   -434   1651    252       O  
ATOM    428  CB  ASN A  58      39.840  55.116  37.555  1.00 34.67           C  
ANISOU  428  CB  ASN A  58     3946   3054   6173   -167   1861   -599       C  
ATOM    429  CG  ASN A  58      39.370  56.488  38.005  1.00 34.08           C  
ANISOU  429  CG  ASN A  58     3526   3075   6346   -150   1213   -762       C  
ATOM    430  OD1 ASN A  58      38.495  57.097  37.376  1.00 33.82           O  
ANISOU  430  OD1 ASN A  58     3373   3170   6308   -459   1428   -304       O  
ATOM    431  ND2 ASN A  58      39.981  57.015  39.067  1.00 32.88           N  
ANISOU  431  ND2 ASN A  58     3100   2891   6502   -194    -41  -1538       N  
ATOM    432  N   ARG A  59      40.973  55.327  34.066  0.50 35.56           N  
ANISOU  432  N   ARG A  59     3881   3572   6057    216   1347    275       N  
ATOM    433  CA  ARG A  59      41.962  55.950  33.217  0.50 39.38           C  
ANISOU  433  CA  ARG A  59     5219   3917   5827   -781   1802     34       C  
ATOM    434  C   ARG A  59      41.767  57.466  33.108  0.50 40.97           C  
ANISOU  434  C   ARG A  59     5787   3881   5897   -720   2121   -195       C  
ATOM    435  O   ARG A  59      42.747  58.204  33.257  0.50 43.04           O  
ANISOU  435  O   ARG A  59     6041   3833   6481   -883   3011  -1407       O  
ATOM    436  CB  ARG A  59      41.957  55.330  31.817  0.00 39.75           C  
ANISOU  436  CB  ARG A  59     5361   3893   5850   -806   1802     34       C  
ATOM    437  CG  ARG A  59      41.180  54.026  31.720  0.00 39.65           C  
ANISOU  437  CG  ARG A  59     5341   3882   5844   -789   1801     34       C  
ATOM    438  CD  ARG A  59      40.039  54.137  30.724  0.00 39.63           C  
ANISOU  438  CD  ARG A  59     5349   3869   5840   -786   1801     34       C  
ATOM    439  NE  ARG A  59      40.223  53.249  29.579  0.00 39.61           N  
ANISOU  439  NE  ARG A  59     5345   3861   5844   -784   1800     34       N  
ATOM    440  CZ  ARG A  59      39.339  53.088  28.604  0.00 39.58           C  
ANISOU  440  CZ  ARG A  59     5348   3849   5842   -781   1800     34       C  
ATOM    441  NH1 ARG A  59      38.755  54.143  28.052  0.00 39.61           N  
ANISOU  441  NH1 ARG A  59     5365   3843   5844   -790   1800     34       N  
ATOM    442  NH2 ARG A  59      39.034  51.871  28.175  0.00 39.55           N  
ANISOU  442  NH2 ARG A  59     5338   3845   5843   -770   1800     34       N  
ATOM    443  N   GLU A  60      40.552  57.887  32.815  1.00 41.02           N  
ANISOU  443  N   GLU A  60     5661   3917   6010   -348   1967    -26       N  
ATOM    444  CA  GLU A  60      40.154  59.258  32.621  1.00 41.67           C  
ANISOU  444  CA  GLU A  60     5778   3910   6146   -499   1602    220       C  
ATOM    445  C   GLU A  60      40.240  60.090  33.895  1.00 40.83           C  
ANISOU  445  C   GLU A  60     5505   3833   6176   -516   1124    541       C  
ATOM    446  O   GLU A  60      40.055  61.308  33.871  1.00 41.53           O  
ANISOU  446  O   GLU A  60     5409   3828   6541   -295   1693   -130       O  
ATOM    447  CB  GLU A  60      38.735  59.356  32.048  1.00 40.92           C  
ANISOU  447  CB  GLU A  60     5633   4033   5880   -231   1299     94       C  
ATOM    448  CG  GLU A  60      38.577  58.774  30.651  1.00 44.10           C  
ANISOU  448  CG  GLU A  60     6300   4678   5779   -580   1573   -253       C  
ATOM    449  CD  GLU A  60      37.129  58.755  30.191  1.00 43.55           C  
ANISOU  449  CD  GLU A  60     6220   4832   5496   -517   2103   -732       C  
ATOM    450  OE1 GLU A  60      36.227  58.900  31.045  0.50 40.93           O  
ANISOU  450  OE1 GLU A  60     5674   4259   5617    935   3723   -661       O  
ATOM    451  OE2 GLU A  60      36.897  58.615  28.972  0.50 43.79           O  
ANISOU  451  OE2 GLU A  60     6873   4265   5498   -788   3761  -3048       O  
ATOM    452  N   GLY A  61      40.447  59.416  35.024  1.00 36.76           N  
ANISOU  452  N   GLY A  61     3775   4015   6178   -216    832    407       N  
ATOM    453  CA  GLY A  61      40.555  60.064  36.306  1.00 36.48           C  
ANISOU  453  CA  GLY A  61     3386   4297   6179   -734   1027     25       C  
ATOM    454  C   GLY A  61      39.296  60.751  36.749  1.00 35.94           C  
ANISOU  454  C   GLY A  61     3776   3921   5960   -990    447     26       C  
ATOM    455  O   GLY A  61      39.334  61.724  37.514  1.00 36.85           O  
ANISOU  455  O   GLY A  61     4088   3902   6011  -1723    510    517       O  
ATOM    456  N   LYS A  62      38.139  60.259  36.296  1.00 30.38           N  
ANISOU  456  N   LYS A  62     3640   3213   4691   -455    740   -218       N  
ATOM    457  CA  LYS A  62      36.881  60.920  36.685  1.00 29.82           C  
ANISOU  457  CA  LYS A  62     3733   3069   4528   -331    563   -439       C  
ATOM    458  C   LYS A  62      36.529  60.613  38.121  1.00 29.74           C  
ANISOU  458  C   LYS A  62     3841   2895   4564   -684    861   -753       C  
ATOM    459  O   LYS A  62      36.080  61.456  38.908  1.00 30.04           O  
ANISOU  459  O   LYS A  62     3815   3083   4517   -120    221    -74       O  
ATOM    460  CB  LYS A  62      35.776  60.523  35.723  1.00 30.86           C  
ANISOU  460  CB  LYS A  62     3337   3827   4560   -218    474   -341       C  
ATOM    461  CG  LYS A  62      36.141  60.686  34.247  1.00 39.17           C  
ANISOU  461  CG  LYS A  62     5506   4905   4470  -1584    397   -217       C  
ATOM    462  CD  LYS A  62      35.011  61.267  33.453  1.00 39.15           C  
ANISOU  462  CD  LYS A  62     5458   5326   4092  -1564    349   -286       C  
ATOM    463  CE  LYS A  62      34.338  60.212  32.574  1.00 43.67           C  
ANISOU  463  CE  LYS A  62     6851   5710   4032  -2224    933   -262       C  
ATOM    464  NZ  LYS A  62      34.395  60.601  31.120  1.00 46.84           N  
ANISOU  464  NZ  LYS A  62     7973   5893   3930  -2143   2369    405       N  
ATOM    465  N   LEU A  63      36.814  59.389  38.558  1.00 26.33           N  
ANISOU  465  N   LEU A  63     2526   3019   4458   -675    319   -610       N  
ATOM    466  CA  LEU A  63      36.478  59.064  39.964  1.00 26.04           C  
ANISOU  466  CA  LEU A  63     2581   2859   4453   -592    268   -959       C  
ATOM    467  C   LEU A  63      37.657  59.477  40.845  1.00 25.25           C  
ANISOU  467  C   LEU A  63     2413   2693   4489   -365   -192   -786       C  
ATOM    468  O   LEU A  63      38.808  59.392  40.422  1.00 25.93           O  
ANISOU  468  O   LEU A  63     2508   2302   5042   -319    346   -661       O  
ATOM    469  CB  LEU A  63      36.259  57.548  40.081  1.00 23.12           C  
ANISOU  469  CB  LEU A  63     1813   2805   4165   -104   -420   -820       C  
ATOM    470  CG  LEU A  63      35.020  57.013  39.335  1.00 22.79           C  
ANISOU  470  CG  LEU A  63     1826   2689   4145    -90    100   -811       C  
ATOM    471  CD1 LEU A  63      35.138  55.493  39.264  1.00 30.30           C  
ANISOU  471  CD1 LEU A  63     4286   2579   4646  -1065  -1357  -1115       C  
ATOM    472  CD2 LEU A  63      33.750  57.405  40.071  1.00 22.23           C  
ANISOU  472  CD2 LEU A  63     1849   3669   2928   -555   -635    128       C  
ATOM    473  N   PRO A  64      37.364  59.871  42.072  1.00 27.45           N  
ANISOU  473  N   PRO A  64     2933   3123   4376   -670   -591  -1102       N  
ATOM    474  CA  PRO A  64      38.416  60.294  42.990  1.00 28.54           C  
ANISOU  474  CA  PRO A  64     3162   3229   4452   -913   -397  -1322       C  
ATOM    475  C   PRO A  64      39.454  59.201  43.224  1.00 29.53           C  
ANISOU  475  C   PRO A  64     2593   3542   5084   -790   -570  -1125       C  
ATOM    476  O   PRO A  64      39.114  58.059  43.545  1.00 25.46           O  
ANISOU  476  O   PRO A  64     2318   3458   3896   -294   -229   -411       O  
ATOM    477  CB  PRO A  64      37.695  60.613  44.278  1.00 28.76           C  
ANISOU  477  CB  PRO A  64     3274   3286   4367   -862   -522  -1180       C  
ATOM    478  CG  PRO A  64      36.319  60.109  44.144  1.00 28.36           C  
ANISOU  478  CG  PRO A  64     3110   3379   4286   -723   -309  -1079       C  
ATOM    479  CD  PRO A  64      36.030  59.913  42.685  1.00 26.15           C  
ANISOU  479  CD  PRO A  64     2792   2911   4233   -246   -247  -1188       C  
ATOM    480  N   GLY A  65      40.712  59.609  43.100  1.00 33.23           N  
ANISOU  480  N   GLY A  65     2451   4373   5801   -858   -739  -1094       N  
ATOM    481  CA  GLY A  65      41.845  58.759  43.236  1.00 33.22           C  
ANISOU  481  CA  GLY A  65     1962   4752   5909   -520   -776  -1045       C  
ATOM    482  C   GLY A  65      42.564  58.898  44.564  1.00 33.72           C  
ANISOU  482  C   GLY A  65     2207   4785   5819   -660   -767   -815       C  
ATOM    483  O   GLY A  65      42.542  59.958  45.196  1.00 38.12           O  
ANISOU  483  O   GLY A  65     4075   4703   5707   -565  -1256  -1543       O  
ATOM    484  N   LYS A  66      43.205  57.816  44.975  1.00 34.34           N  
ANISOU  484  N   LYS A  66     2824   4742   5482   -633  -1242    -76       N  
ATOM    485  CA  LYS A  66      44.002  57.846  46.222  1.00 34.40           C  
ANISOU  485  CA  LYS A  66     3074   4506   5491   -677   -910   -337       C  
ATOM    486  C   LYS A  66      44.966  56.666  46.213  1.00 35.61           C  
ANISOU  486  C   LYS A  66     2803   4646   6083   -471  -1480   -295       C  
ATOM    487  O   LYS A  66      44.656  55.613  45.641  1.00 34.49           O  
ANISOU  487  O   LYS A  66     2803   4636   5667   -116  -1236   -840       O  
ATOM    488  CB  LYS A  66      43.008  57.693  47.398  1.00 34.58           C  
ANISOU  488  CB  LYS A  66     3155   4529   5453   -643   -557   -671       C  
ATOM    489  CG  LYS A  66      43.630  57.866  48.754  1.00 33.43           C  
ANISOU  489  CG  LYS A  66     2416   4782   5506   -456   -745   -693       C  
ATOM    490  CD  LYS A  66      42.630  57.606  49.886  1.00 34.07           C  
ANISOU  490  CD  LYS A  66     2390   5081   5474   -595    -24   -958       C  
ATOM    491  CE  LYS A  66      43.322  57.840  51.227  0.50 34.52           C  
ANISOU  491  CE  LYS A  66     2400   5205   5511   -849    273  -1458       C  
ATOM    492  NZ  LYS A  66      42.405  57.716  52.375  0.50 36.00           N  
ANISOU  492  NZ  LYS A  66     2812   5398   5467  -1379   1840  -2614       N  
ATOM    493  N   SER A  67      46.145  56.847  46.803  1.00 38.01           N  
ANISOU  493  N   SER A  67     2865   4668   6911   -734  -1354   -323       N  
ATOM    494  CA  SER A  67      47.110  55.738  46.878  1.00 39.15           C  
ANISOU  494  CA  SER A  67     2615   4779   7482   -576  -1624   -511       C  
ATOM    495  C   SER A  67      46.448  54.512  47.511  1.00 37.81           C  
ANISOU  495  C   SER A  67     2758   4667   6940   -545  -1762   -581       C  
ATOM    496  O   SER A  67      45.785  54.612  48.544  1.00 36.27           O  
ANISOU  496  O   SER A  67     2663   4252   6867    422  -1574  -1281       O  
ATOM    497  CB  SER A  67      48.336  56.147  47.697  1.00 40.52           C  
ANISOU  497  CB  SER A  67     2459   5122   7814   -595  -1201   -614       C  
ATOM    498  OG  SER A  67      48.342  57.535  47.973  1.00 49.44           O  
ANISOU  498  OG  SER A  67     4778   5122   8885  -2409  -1144  -1020       O  
ATOM    499  N   GLY A  68      46.581  53.366  46.848  1.00 36.25           N  
ANISOU  499  N   GLY A  68     2725   4812   6238   -680  -1530   -735       N  
ATOM    500  CA  GLY A  68      46.013  52.121  47.328  1.00 30.85           C  
ANISOU  500  CA  GLY A  68     1940   4515   5267    177  -1567   -900       C  
ATOM    501  C   GLY A  68      44.543  51.967  47.140  1.00 28.89           C  
ANISOU  501  C   GLY A  68     2143   4054   4779      4  -1603   -616       C  
ATOM    502  O   GLY A  68      43.928  50.979  47.589  1.00 31.77           O  
ANISOU  502  O   GLY A  68     2939   3887   5245   -420  -1700   -442       O  
ATOM    503  N   ARG A  69      43.879  52.879  46.412  1.00 28.03           N  
ANISOU  503  N   ARG A  69     2330   4249   4074   -299  -2120   -879       N  
ATOM    504  CA  ARG A  69      42.469  52.700  46.140  1.00 25.96           C  
ANISOU  504  CA  ARG A  69     2674   3555   3636   -392  -1261  -1038       C  
ATOM    505  C   ARG A  69      42.256  52.074  44.754  1.00 24.78           C  
ANISOU  505  C   ARG A  69     2485   3293   3637     94  -1324   -822       C  
ATOM    506  O   ARG A  69      42.770  52.588  43.758  1.00 27.30           O  
ANISOU  506  O   ARG A  69     3185   3550   3636   -586   -462   -443       O  
ATOM    507  CB  ARG A  69      41.690  53.992  46.274  1.00 24.68           C  
ANISOU  507  CB  ARG A  69     2926   3525   2927   -322  -1197  -1287       C  
ATOM    508  CG  ARG A  69      40.248  53.893  45.810  1.00 22.23           C  
ANISOU  508  CG  ARG A  69     2982   3160   2305   -143  -1015  -1181       C  
ATOM    509  CD  ARG A  69      39.599  55.276  45.756  1.00 23.67           C  
ANISOU  509  CD  ARG A  69     3373   3112   2507   -242   -738   -643       C  
ATOM    510  NE  ARG A  69      39.316  55.767  47.088  1.00 22.09           N  
ANISOU  510  NE  ARG A  69     2847   2980   2567   -138   -797   -496       N  
ATOM    511  CZ  ARG A  69      39.323  57.034  47.471  1.00 21.85           C  
ANISOU  511  CZ  ARG A  69     2546   2943   2814    -55  -1049   -230       C  
ATOM    512  NH1 ARG A  69      39.357  57.987  46.548  1.00 25.96           N  
ANISOU  512  NH1 ARG A  69     4083   2933   2849   -721   -531    328       N  
ATOM    513  NH2 ARG A  69      39.117  57.340  48.733  1.00 25.99           N  
ANISOU  513  NH2 ARG A  69     4363   2693   2821   -399   -888   -647       N  
ATOM    514  N   THR A  70      41.532  50.990  44.741  1.00 22.99           N  
ANISOU  514  N   THR A  70     2012   3280   3444    313   -640   -933       N  
ATOM    515  CA  THR A  70      41.138  50.235  43.562  1.00 21.85           C  
ANISOU  515  CA  THR A  70     1714   3226   3364    677   -222  -1205       C  
ATOM    516  C   THR A  70      39.624  50.427  43.342  1.00 21.81           C  
ANISOU  516  C   THR A  70     1898   3000   3387    504    241  -1667       C  
ATOM    517  O   THR A  70      38.855  50.489  44.312  1.00 22.33           O  
ANISOU  517  O   THR A  70     1855   3206   3424    441   -662   -942       O  
ATOM    518  CB  THR A  70      41.412  48.719  43.771  1.00 23.89           C  
ANISOU  518  CB  THR A  70     2056   3170   3850   1278   -345  -1627       C  
ATOM    519  OG1 THR A  70      42.842  48.505  43.830  1.00 29.49           O  
ANISOU  519  OG1 THR A  70     2621   2818   5766    649    -85   -736       O  
ATOM    520  CG2 THR A  70      40.955  47.906  42.576  1.00 26.48           C  
ANISOU  520  CG2 THR A  70     3095   3168   3799   1047     96   -663       C  
ATOM    521  N   TRP A  71      39.230  50.539  42.089  1.00 20.46           N  
ANISOU  521  N   TRP A  71     2001   2329   3445    183   -421  -1680       N  
ATOM    522  CA  TRP A  71      37.821  50.625  41.710  1.00 20.70           C  
ANISOU  522  CA  TRP A  71     2150   2139   3577      5    -80  -1611       C  
ATOM    523  C   TRP A  71      37.395  49.337  40.990  1.00 18.50           C  
ANISOU  523  C   TRP A  71     1522   2191   3316    485   -587  -1274       C  
ATOM    524  O   TRP A  71      38.162  48.781  40.223  1.00 18.82           O  
ANISOU  524  O   TRP A  71     1648   2515   2985   -108    156  -1512       O  
ATOM    525  CB  TRP A  71      37.607  51.830  40.755  1.00 20.31           C  
ANISOU  525  CB  TRP A  71     2278   2165   3275    188    347  -1592       C  
ATOM    526  CG  TRP A  71      37.715  53.145  41.478  1.00 19.20           C  
ANISOU  526  CG  TRP A  71     1998   2195   3103    -18   -537   -810       C  
ATOM    527  CD1 TRP A  71      38.809  53.938  41.576  1.00 19.14           C  
ANISOU  527  CD1 TRP A  71     1880   2354   3036     72   -421   -885       C  
ATOM    528  CD2 TRP A  71      36.669  53.792  42.219  1.00 18.30           C  
ANISOU  528  CD2 TRP A  71     2068   2342   2542    -96   -353  -1236       C  
ATOM    529  NE1 TRP A  71      38.519  55.059  42.323  1.00 19.34           N  
ANISOU  529  NE1 TRP A  71     1959   2390   3001    -79     60  -1196       N  
ATOM    530  CE2 TRP A  71      37.213  55.003  42.729  1.00 18.59           C  
ANISOU  530  CE2 TRP A  71     1785   2275   3003    126   -175  -1238       C  
ATOM    531  CE3 TRP A  71      35.340  53.505  42.493  1.00 17.00           C  
ANISOU  531  CE3 TRP A  71     2147   2090   2222    -18   -355   -495       C  
ATOM    532  CZ2 TRP A  71      36.468  55.901  43.493  1.00 18.88           C  
ANISOU  532  CZ2 TRP A  71     2266   2287   2619   -142   -839   -480       C  
ATOM    533  CZ3 TRP A  71      34.594  54.385  43.259  1.00 17.34           C  
ANISOU  533  CZ3 TRP A  71     2196   2060   2334     48   -532   -342       C  
ATOM    534  CH2 TRP A  71      35.167  55.570  43.760  1.00 16.87           C  
ANISOU  534  CH2 TRP A  71     1962   2059   2388    308   -391   -707       C  
ATOM    535  N   ARG A  72      36.162  48.940  41.228  1.00 16.50           N  
ANISOU  535  N   ARG A  72     1882   2458   1928    -47   -757  -1112       N  
ATOM    536  CA  ARG A  72      35.509  47.836  40.546  1.00 15.27           C  
ANISOU  536  CA  ARG A  72     1712   2347   1743    269   -886   -945       C  
ATOM    537  C   ARG A  72      34.104  48.247  40.126  1.00 15.39           C  
ANISOU  537  C   ARG A  72     2186   1812   1851   -271   -549  -1322       C  
ATOM    538  O   ARG A  72      33.551  49.229  40.623  1.00 15.08           O  
ANISOU  538  O   ARG A  72     2272   1811   1646      7   -316  -1084       O  
ATOM    539  CB  ARG A  72      35.444  46.596  41.446  1.00 16.24           C  
ANISOU  539  CB  ARG A  72     2024   2295   1853    557   -883   -931       C  
ATOM    540  CG  ARG A  72      36.801  46.007  41.779  1.00 18.83           C  
ANISOU  540  CG  ARG A  72     2036   2230   2888    869   -660   -461       C  
ATOM    541  CD  ARG A  72      36.722  44.792  42.655  1.00 21.89           C  
ANISOU  541  CD  ARG A  72     3207   2007   3103   1219  -1029   -713       C  
ATOM    542  NE  ARG A  72      38.003  44.195  42.893  1.00 25.56           N  
ANISOU  542  NE  ARG A  72     3349   1917   4445   1732  -1265   -610       N  
ATOM    543  CZ  ARG A  72      38.716  43.410  42.138  1.00 23.20           C  
ANISOU  543  CZ  ARG A  72     2124   2879   3811   1564   -716   -958       C  
ATOM    544  NH1 ARG A  72      38.183  42.826  41.050  1.00 29.44           N  
ANISOU  544  NH1 ARG A  72     4225   3228   3733     14  -1673   -807       N  
ATOM    545  NH2 ARG A  72      39.987  43.133  42.457  1.00 31.78           N  
ANISOU  545  NH2 ARG A  72     1718   3852   6505    780   -819   -721       N  
ATOM    546  N   GLU A  73      33.552  47.491  39.172  1.00 13.40           N  
ANISOU  546  N   GLU A  73     1634   1493   1965    380   -314   -762       N  
ATOM    547  CA  GLU A  73      32.251  47.799  38.616  1.00 13.62           C  
ANISOU  547  CA  GLU A  73     1619   1523   2032    172   -240   -628       C  
ATOM    548  C   GLU A  73      31.320  46.597  38.647  1.00 13.26           C  
ANISOU  548  C   GLU A  73     1746   1442   1848    190     40   -747       C  
ATOM    549  O   GLU A  73      31.776  45.453  38.685  1.00 13.95           O  
ANISOU  549  O   GLU A  73     1900   1437   1965    231   -303   -720       O  
ATOM    550  CB  GLU A  73      32.393  48.305  37.172  1.00 14.21           C  
ANISOU  550  CB  GLU A  73     1821   1582   1998    167    184   -628       C  
ATOM    551  CG  GLU A  73      33.074  47.318  36.230  1.00 15.49           C  
ANISOU  551  CG  GLU A  73     2292   1520   2074    259   -168   -291       C  
ATOM    552  CD  GLU A  73      32.856  47.705  34.769  1.00 17.41           C  
ANISOU  552  CD  GLU A  73     2604   2061   1950     -8    229    177       C  
ATOM    553  OE1 GLU A  73      31.677  47.799  34.359  1.00 19.05           O  
ANISOU  553  OE1 GLU A  73     2456   3181   1603   -342    -39    151       O  
ATOM    554  OE2 GLU A  73      33.842  47.915  34.055  1.00 23.91           O  
ANISOU  554  OE2 GLU A  73     2444   4438   2204   -795    275    351       O  
ATOM    555  N   ALA A  74      30.033  46.874  38.548  1.00 12.04           N  
ANISOU  555  N   ALA A  74     1933   1324   1319   -125   -123   -690       N  
ATOM    556  CA  ALA A  74      29.023  45.824  38.369  1.00 10.65           C  
ANISOU  556  CA  ALA A  74     1917   1205    923    -38   -112   -236       C  
ATOM    557  C   ALA A  74      27.802  46.375  37.626  1.00 10.64           C  
ANISOU  557  C   ALA A  74     1857   1204    982    -76    125   -731       C  
ATOM    558  O   ALA A  74      27.473  47.566  37.741  1.00 11.25           O  
ANISOU  558  O   ALA A  74     1903   1178   1194    -82   -158   -559       O  
ATOM    559  CB  ALA A  74      28.606  45.273  39.717  1.00 12.85           C  
ANISOU  559  CB  ALA A  74     2290   1853    741   -160   -427    231       C  
ATOM    560  N   ASP A  75      27.199  45.515  36.827  1.00  9.96           N  
ANISOU  560  N   ASP A  75     1675   1176    932      9     10   -299       N  
ATOM    561  CA  ASP A  75      26.023  45.885  36.049  1.00  9.59           C  
ANISOU  561  CA  ASP A  75     1640   1143    861    247   -120   -301       C  
ATOM    562  C   ASP A  75      24.793  45.992  36.975  1.00 10.08           C  
ANISOU  562  C   ASP A  75     1776   1220    833   -320    293    -81       C  
ATOM    563  O   ASP A  75      24.593  45.136  37.823  1.00 11.03           O  
ANISOU  563  O   ASP A  75     2048   1275    870    -44    260     50       O  
ATOM    564  CB  ASP A  75      25.736  44.837  34.984  1.00  9.60           C  
ANISOU  564  CB  ASP A  75     1537   1206    906   -176    111   -236       C  
ATOM    565  CG  ASP A  75      26.655  44.878  33.806  1.00 10.58           C  
ANISOU  565  CG  ASP A  75     1725   1450    846   -369     19   -347       C  
ATOM    566  OD1 ASP A  75      27.771  45.399  33.891  1.00 11.28           O  
ANISOU  566  OD1 ASP A  75     1573   1898    814   -373    222   -409       O  
ATOM    567  OD2 ASP A  75      26.230  44.306  32.745  1.00 11.43           O  
ANISOU  567  OD2 ASP A  75     1923   1596    824   -504     92   -342       O  
ATOM    568  N   ILE A  76      23.952  46.980  36.692  1.00  9.92           N  
ANISOU  568  N   ILE A  76     1781   1195    793   -232    281    -15       N  
ATOM    569  CA  ILE A  76      22.729  47.200  37.466  1.00 10.89           C  
ANISOU  569  CA  ILE A  76     1816   1149   1173   -239    372   -258       C  
ATOM    570  C   ILE A  76      21.505  47.148  36.571  1.00 11.54           C  
ANISOU  570  C   ILE A  76     1701   1363   1319   -192    344   -533       C  
ATOM    571  O   ILE A  76      21.562  47.530  35.376  1.00 11.88           O  
ANISOU  571  O   ILE A  76     1838   1440   1238   -246     35   -149       O  
ATOM    572  CB  ILE A  76      22.822  48.530  38.213  1.00 10.63           C  
ANISOU  572  CB  ILE A  76     1670   1184   1185    150    508   -334       C  
ATOM    573  CG1 ILE A  76      23.977  48.549  39.224  1.00 11.17           C  
ANISOU  573  CG1 ILE A  76     1675   1474   1094   -121   -230    150       C  
ATOM    574  CG2 ILE A  76      21.533  49.036  38.791  1.00 11.74           C  
ANISOU  574  CG2 ILE A  76     1543   1362   1554    269    226   -401       C  
ATOM    575  CD1 ILE A  76      23.733  47.645  40.411  1.00 14.19           C  
ANISOU  575  CD1 ILE A  76     2584   1899    907   -205    188     19       C  
ATOM    576  N   ASN A  77      20.395  46.640  37.093  1.00 12.72           N  
ANISOU  576  N   ASN A  77     1576   1917   1342   -164    168   -532       N  
ATOM    577  CA  ASN A  77      19.152  46.550  36.366  1.00 13.16           C  
ANISOU  577  CA  ASN A  77     1803   1566   1631   -408     35   -511       C  
ATOM    578  C   ASN A  77      19.148  45.563  35.221  1.00 13.65           C  
ANISOU  578  C   ASN A  77     2112   1640   1433   -468    -92   -383       C  
ATOM    579  O   ASN A  77      18.254  45.624  34.355  1.00 14.54           O  
ANISOU  579  O   ASN A  77     1818   2115   1591   -102    -33   -711       O  
ATOM    580  CB  ASN A  77      18.670  47.921  35.894  1.00 14.76           C  
ANISOU  580  CB  ASN A  77     1788   1679   2142     50   -118   -697       C  
ATOM    581  CG  ASN A  77      18.337  48.891  36.988  1.00 15.28           C  
ANISOU  581  CG  ASN A  77     2092   1681   2032    212    -28   -176       C  
ATOM    582  OD1 ASN A  77      17.820  48.498  38.030  1.00 18.52           O  
ANISOU  582  OD1 ASN A  77     2584   2519   1936   -225    738   -509       O  
ATOM    583  ND2 ASN A  77      18.618  50.172  36.762  1.00 18.53           N  
ANISOU  583  ND2 ASN A  77     2756   1791   2493   -376    262   -386       N  
ATOM    584  N   TYR A  78      20.084  44.628  35.158  1.00 12.62           N  
ANISOU  584  N   TYR A  78     2217   1635    941   -370    284   -391       N  
ATOM    585  CA  TYR A  78      20.085  43.667  34.048  1.00 12.04           C  
ANISOU  585  CA  TYR A  78     1868   1689   1017   -146    534   -167       C  
ATOM    586  C   TYR A  78      19.173  42.488  34.326  1.00 12.99           C  
ANISOU  586  C   TYR A  78     2008   1713   1213   -308    641   -130       C  
ATOM    587  O   TYR A  78      19.223  41.883  35.405  1.00 14.11           O  
ANISOU  587  O   TYR A  78     2399   1751   1213   -307    479   -334       O  
ATOM    588  CB  TYR A  78      21.560  43.132  33.890  1.00 12.14           C  
ANISOU  588  CB  TYR A  78     1852   1728   1032   -123   -169   -301       C  
ATOM    589  CG  TYR A  78      21.630  42.147  32.736  1.00 11.71           C  
ANISOU  589  CG  TYR A  78     1828   1619   1004    -39     35   -290       C  
ATOM    590  CD1 TYR A  78      21.570  42.594  31.428  1.00 11.82           C  
ANISOU  590  CD1 TYR A  78     2010   1460   1021    -78    -84   -223       C  
ATOM    591  CD2 TYR A  78      21.592  40.783  32.971  1.00 12.35           C  
ANISOU  591  CD2 TYR A  78     2106   1673    913     -9   -429   -219       C  
ATOM    592  CE1 TYR A  78      21.561  41.704  30.348  1.00 11.32           C  
ANISOU  592  CE1 TYR A  78     1904   1421    978   -309    140   -403       C  
ATOM    593  CE2 TYR A  78      21.525  39.900  31.916  1.00 11.94           C  
ANISOU  593  CE2 TYR A  78     2081   1566    891   -138   -469    -40       C  
ATOM    594  CZ  TYR A  78      21.518  40.343  30.623  1.00 11.01           C  
ANISOU  594  CZ  TYR A  78     1854   1410    918   -183   -440   -695       C  
ATOM    595  OH  TYR A  78      21.506  39.423  29.613  1.00 10.74           O  
ANISOU  595  OH  TYR A  78     1649   1494    938   -155    131    -85       O  
ATOM    596  N   THR A  79      18.393  42.087  33.328  1.00 12.78           N  
ANISOU  596  N   THR A  79     1998   1556   1300   -146    -39   -183       N  
ATOM    597  CA  THR A  79      17.623  40.866  33.371  1.00 16.35           C  
ANISOU  597  CA  THR A  79     2626   2037   1550   -957    -53   -219       C  
ATOM    598  C   THR A  79      17.921  39.962  32.191  1.00 15.21           C  
ANISOU  598  C   THR A  79     2360   1947   1471  -1139     82     -4       C  
ATOM    599  O   THR A  79      18.090  38.748  32.342  1.00 15.67           O  
ANISOU  599  O   THR A  79     2641   1916   1397   -826    336    -68       O  
ATOM    600  CB  THR A  79      16.114  41.103  33.489  1.00 17.82           C  
ANISOU  600  CB  THR A  79     2128   2077   2568   -313    282   -400       C  
ATOM    601  OG1 THR A  79      15.695  41.935  32.416  1.00 19.65           O  
ANISOU  601  OG1 THR A  79     2420   2339   2709    142    503   -220       O  
ATOM    602  CG2 THR A  79      15.770  41.830  34.760  1.00 18.47           C  
ANISOU  602  CG2 THR A  79     2146   2234   2639   -387    353   -992       C  
ATOM    603  N   SER A  80      17.883  40.487  30.976  1.00 11.95           N  
ANISOU  603  N   SER A  80     1299   1696   1546   -193    126   -334       N  
ATOM    604  CA  SER A  80      18.072  39.656  29.786  1.00 12.04           C  
ANISOU  604  CA  SER A  80     1586   1526   1463   -436    -32   -279       C  
ATOM    605  C   SER A  80      18.465  40.546  28.609  1.00 10.89           C  
ANISOU  605  C   SER A  80     1260   1396   1484   -187   -269   -416       C  
ATOM    606  O   SER A  80      18.291  41.762  28.651  1.00 13.93           O  
ANISOU  606  O   SER A  80     2376   1375   1542   -183    138   -433       O  
ATOM    607  CB  SER A  80      16.829  38.849  29.447  1.00 15.22           C  
ANISOU  607  CB  SER A  80     1965   2372   1447  -1003    -96   -486       C  
ATOM    608  OG  SER A  80      15.748  39.662  29.099  1.00 17.95           O  
ANISOU  608  OG  SER A  80     1282   2972   2566   -693   -403   -182       O  
ATOM    609  N   GLY A  81      18.992  39.928  27.564  1.00 11.25           N  
ANISOU  609  N   GLY A  81     1345   1428   1503   -305    -43   -233       N  
ATOM    610  CA  GLY A  81      19.406  40.644  26.380  1.00 10.96           C  
ANISOU  610  CA  GLY A  81     1373   1321   1470   -287     70   -460       C  
ATOM    611  C   GLY A  81      20.803  41.208  26.451  1.00  8.92           C  
ANISOU  611  C   GLY A  81     1056   1147   1187     91    -58     -3       C  
ATOM    612  O   GLY A  81      21.649  40.774  27.211  1.00  9.54           O  
ANISOU  612  O   GLY A  81     1159   1461   1004    118    -96     34       O  
ATOM    613  N   PHE A  82      21.038  42.222  25.603  1.00 11.10           N  
ANISOU  613  N   PHE A  82     1808   1311   1099   -402   -261    172       N  
ATOM    614  CA  PHE A  82      22.309  42.916  25.637  1.00 12.09           C  
ANISOU  614  CA  PHE A  82     2022   1433   1138   -662    -59   -115       C  
ATOM    615  C   PHE A  82      22.463  43.632  26.968  1.00 10.20           C  
ANISOU  615  C   PHE A  82     1339   1406   1130    -86    300     11       C  
ATOM    616  O   PHE A  82      21.474  44.026  27.598  1.00 11.13           O  
ANISOU  616  O   PHE A  82     1321   1387   1522    -73    290   -224       O  
ATOM    617  CB  PHE A  82      22.380  43.926  24.483  1.00 10.60           C  
ANISOU  617  CB  PHE A  82     1655   1183   1191   -300    -38   -111       C  
ATOM    618  CG  PHE A  82      22.528  43.258  23.121  1.00 11.12           C  
ANISOU  618  CG  PHE A  82     1716   1359   1151    -12   -394     13       C  
ATOM    619  CD1 PHE A  82      23.772  42.918  22.638  1.00 11.21           C  
ANISOU  619  CD1 PHE A  82     1671   1682    908   -186   -434    -16       C  
ATOM    620  CD2 PHE A  82      21.422  42.951  22.350  1.00 11.71           C  
ANISOU  620  CD2 PHE A  82     1404   1961   1084    229     -2     16       C  
ATOM    621  CE1 PHE A  82      23.915  42.280  21.428  1.00 11.86           C  
ANISOU  621  CE1 PHE A  82     1919   1622    967   -197    431     33       C  
ATOM    622  CE2 PHE A  82      21.549  42.267  21.164  1.00 13.03           C  
ANISOU  622  CE2 PHE A  82     1722   2120   1108    -47   -249    132       C  
ATOM    623  CZ  PHE A  82      22.808  41.935  20.694  1.00 12.21           C  
ANISOU  623  CZ  PHE A  82     2099   1642    900   -218   -183    255       C  
ATOM    624  N   ARG A  83      23.691  43.879  27.402  1.00 11.02           N  
ANISOU  624  N   ARG A  83     1383   1683   1121   -257     70   -291       N  
ATOM    625  CA  ARG A  83      23.909  44.707  28.580  1.00 11.54           C  
ANISOU  625  CA  ARG A  83     1788   1703    892   -198     14    -48       C  
ATOM    626  C   ARG A  83      23.401  46.127  28.376  1.00 11.11           C  
ANISOU  626  C   ARG A  83     1753   1723    747   -344     23      0       C  
ATOM    627  O   ARG A  83      23.337  46.653  27.280  1.00 13.20           O  
ANISOU  627  O   ARG A  83     2464   1747    803     32    220   -129       O  
ATOM    628  CB  ARG A  83      25.395  44.722  28.950  1.00 11.86           C  
ANISOU  628  CB  ARG A  83     1997   1555    955   -524    -15   -425       C  
ATOM    629  CG  ARG A  83      25.930  43.345  29.333  1.00 12.53           C  
ANISOU  629  CG  ARG A  83     1965   1596   1200   -198    -32   -521       C  
ATOM    630  CD  ARG A  83      27.446  43.306  29.404  1.00 12.84           C  
ANISOU  630  CD  ARG A  83     1617   2010   1253    159    -82   -461       C  
ATOM    631  NE  ARG A  83      27.974  44.076  30.505  1.00 13.33           N  
ANISOU  631  NE  ARG A  83     1459   2473   1132    230      4   -354       N  
ATOM    632  CZ  ARG A  83      29.227  44.480  30.652  1.00 15.19           C  
ANISOU  632  CZ  ARG A  83     1614   2837   1318    -93    -79   -299       C  
ATOM    633  NH1 ARG A  83      30.071  44.370  29.626  1.00 17.20           N  
ANISOU  633  NH1 ARG A  83     1736   3634   1167   -437    319   -505       N  
ATOM    634  NH2 ARG A  83      29.601  45.151  31.724  1.00 16.82           N  
ANISOU  634  NH2 ARG A  83     1711   3467   1214   -110    335   -855       N  
ATOM    635  N   ASN A  84      22.994  46.747  29.472  1.00 10.79           N  
ANISOU  635  N   ASN A  84     1586   1729    784   -203    219   -468       N  
ATOM    636  CA  ASN A  84      22.495  48.118  29.438  1.00 12.47           C  
ANISOU  636  CA  ASN A  84     1843   1709   1188    -86    206   -276       C  
ATOM    637  C   ASN A  84      23.620  49.106  29.755  1.00 12.98           C  
ANISOU  637  C   ASN A  84     2013   1686   1233   -182    212   -608       C  
ATOM    638  O   ASN A  84      24.810  48.745  29.675  1.00 14.07           O  
ANISOU  638  O   ASN A  84     2214   1515   1617   -402    162   -259       O  
ATOM    639  CB  ASN A  84      21.315  48.259  30.407  1.00 12.26           C  
ANISOU  639  CB  ASN A  84     1855   1563   1238     42   -173   -131       C  
ATOM    640  CG  ASN A  84      21.707  47.949  31.845  1.00 11.88           C  
ANISOU  640  CG  ASN A  84     1971   1346   1195    -50    917   -214       C  
ATOM    641  OD1 ASN A  84      22.874  48.117  32.210  1.00 13.50           O  
ANISOU  641  OD1 ASN A  84     1924   1946   1258   -173    174   -332       O  
ATOM    642  ND2 ASN A  84      20.737  47.554  32.646  1.00 15.93           N  
ANISOU  642  ND2 ASN A  84     2187   2617   1249   -572    449   -468       N  
ATOM    643  N   SER A  85      23.293  50.320  30.113  1.00 12.40           N  
ANISOU  643  N   SER A  85     2141   1683    887    -36    -59   -355       N  
ATOM    644  CA  SER A  85      24.215  51.406  30.348  1.00 14.94           C  
ANISOU  644  CA  SER A  85     3050   1762    863   -561   -384   -514       C  
ATOM    645  C   SER A  85      24.400  51.755  31.819  1.00 13.95           C  
ANISOU  645  C   SER A  85     2594   1836    870   -476    -72   -556       C  
ATOM    646  O   SER A  85      25.062  52.741  32.136  1.00 16.60           O  
ANISOU  646  O   SER A  85     3583   1809    917   -941   -137     51       O  
ATOM    647  CB ASER A  85      23.780  52.657  29.570  0.50 16.95           C  
ANISOU  647  CB ASER A  85     3866   1748    827   -603   -357   -135       C  
ATOM    648  CB BSER A  85      23.738  52.663  29.587  0.50 15.92           C  
ANISOU  648  CB BSER A  85     3459   1760    829   -508   -343   -137       C  
ATOM    649  OG ASER A  85      22.561  53.163  30.077  0.50 19.20           O  
ANISOU  649  OG ASER A  85     4002   1330   1962   -372   -159   -217       O  
ATOM    650  OG BSER A  85      23.943  52.472  28.194  0.50 22.18           O  
ANISOU  650  OG BSER A  85     5331   2357    738  -1213   -864    284       O  
ATOM    651  N   ASP A  86      23.807  50.958  32.689  1.00 11.96           N  
ANISOU  651  N   ASP A  86     2092   1607    845    -91   -261   -134       N  
ATOM    652  CA  ASP A  86      23.785  51.236  34.118  1.00 10.56           C  
ANISOU  652  CA  ASP A  86     1997   1175    839     -7     31     67       C  
ATOM    653  C   ASP A  86      24.859  50.422  34.841  1.00 10.75           C  
ANISOU  653  C   ASP A  86     2024   1148    911   -153    467   -260       C  
ATOM    654  O   ASP A  86      24.920  49.213  34.747  1.00 11.00           O  
ANISOU  654  O   ASP A  86     1725   1203   1249    -72    -44   -182       O  
ATOM    655  CB  ASP A  86      22.422  50.871  34.699  1.00 12.76           C  
ANISOU  655  CB  ASP A  86     1495   2249   1104    168   -281   -170       C  
ATOM    656  CG  ASP A  86      21.253  51.693  34.206  1.00 14.93           C  
ANISOU  656  CG  ASP A  86     1528   2057   2087    186   -206   -379       C  
ATOM    657  OD1 ASP A  86      21.454  52.751  33.585  1.00 19.19           O  
ANISOU  657  OD1 ASP A  86     2590   1727   2976    233   -227    128       O  
ATOM    658  OD2 ASP A  86      20.092  51.265  34.445  1.00 19.15           O  
ANISOU  658  OD2 ASP A  86     1468   2720   3088     13   -235   -186       O  
ATOM    659  N   ARG A  87      25.652  51.116  35.668  1.00 10.04           N  
ANISOU  659  N   ARG A  87     1869    906   1038    -17    344   -186       N  
ATOM    660  CA  ARG A  87      26.719  50.464  36.390  1.00  9.90           C  
ANISOU  660  CA  ARG A  87     1653   1004   1103    182    536    -83       C  
ATOM    661  C   ARG A  87      26.854  51.127  37.789  1.00  9.18           C  
ANISOU  661  C   ARG A  87     1345   1012   1132    573    136   -117       C  
ATOM    662  O   ARG A  87      26.684  52.319  37.936  1.00 11.19           O  
ANISOU  662  O   ARG A  87     2143    992   1119    199   -210    -94       O  
ATOM    663  CB  ARG A  87      28.091  50.564  35.712  1.00 10.61           C  
ANISOU  663  CB  ARG A  87     1782   1236   1012    -63     29   -242       C  
ATOM    664  CG  ARG A  87      28.128  50.129  34.275  1.00 11.81           C  
ANISOU  664  CG  ARG A  87     2078   1472    938   -184    277   -797       C  
ATOM    665  CD  ARG A  87      28.193  48.652  34.044  1.00 11.15           C  
ANISOU  665  CD  ARG A  87     1804   1466    965   -104    189   -539       C  
ATOM    666  NE  ARG A  87      28.305  48.321  32.619  1.00 11.78           N  
ANISOU  666  NE  ARG A  87     1837   1636   1003   -111    285   -615       N  
ATOM    667  CZ  ARG A  87      27.292  48.176  31.795  1.00 11.84           C  
ANISOU  667  CZ  ARG A  87     1834   1734    929    -36    -31   -693       C  
ATOM    668  NH1 ARG A  87      26.016  48.170  32.271  1.00 13.04           N  
ANISOU  668  NH1 ARG A  87     1734   1683   1540     42   -308   -797       N  
ATOM    669  NH2 ARG A  87      27.476  47.936  30.525  1.00 15.27           N  
ANISOU  669  NH2 ARG A  87     2546   2362    895   -211    -11  -1166       N  
ATOM    670  N   ILE A  88      27.256  50.282  38.720  1.00 10.57           N  
ANISOU  670  N   ILE A  88     1888   1020   1108     83   -391   -306       N  
ATOM    671  CA  ILE A  88      27.701  50.725  40.044  1.00 11.19           C  
ANISOU  671  CA  ILE A  88     1848   1323   1081    301   -214   -250       C  
ATOM    672  C   ILE A  88      29.227  50.639  40.063  1.00 10.18           C  
ANISOU  672  C   ILE A  88     1819   1424    625    383   -243   -718       C  
ATOM    673  O   ILE A  88      29.783  49.672  39.508  1.00 11.68           O  
ANISOU  673  O   ILE A  88     1779   1286   1374     66    133   -754       O  
ATOM    674  CB  ILE A  88      27.052  49.954  41.168  1.00 12.86           C  
ANISOU  674  CB  ILE A  88     2213   1578   1094   -122    166     26       C  
ATOM    675  CG1 ILE A  88      26.833  50.623  42.470  1.00 15.93           C  
ANISOU  675  CG1 ILE A  88     3286   1714   1051    -82    612   -279       C  
ATOM    676  CG2 ILE A  88      27.491  48.527  41.236  1.00 18.43           C  
ANISOU  676  CG2 ILE A  88     3907   1398   1697   -415   -151   -370       C  
ATOM    677  CD1 ILE A  88      26.009  49.949  43.523  1.00 16.61           C  
ANISOU  677  CD1 ILE A  88     3474   1868    969   -222    876   -349       C  
ATOM    678  N   LEU A  89      29.852  51.655  40.639  1.00 10.80           N  
ANISOU  678  N   LEU A  89     1649   1293   1162    500   -497   -929       N  
ATOM    679  CA  LEU A  89      31.310  51.741  40.770  1.00 12.15           C  
ANISOU  679  CA  LEU A  89     1777   1053   1786    420   -785   -665       C  
ATOM    680  C   LEU A  89      31.603  51.790  42.268  1.00 12.67           C  
ANISOU  680  C   LEU A  89     1584   1429   1800     77   -553  -1049       C  
ATOM    681  O   LEU A  89      31.058  52.622  42.983  1.00 13.69           O  
ANISOU  681  O   LEU A  89     2005   1600   1596    665   -316   -782       O  
ATOM    682  CB  LEU A  89      31.852  52.986  40.058  1.00 15.13           C  
ANISOU  682  CB  LEU A  89     2254   1710   1784   -221   -178   -589       C  
ATOM    683  CG  LEU A  89      32.111  52.895  38.571  1.00 16.78           C  
ANISOU  683  CG  LEU A  89     2565   2059   1753   -269   -214   -334       C  
ATOM    684  CD1 LEU A  89      33.290  52.024  38.207  1.00 17.34           C  
ANISOU  684  CD1 LEU A  89     3334   1597   1657     35    804   -488       C  
ATOM    685  CD2 LEU A  89      30.879  52.547  37.777  1.00 21.29           C  
ANISOU  685  CD2 LEU A  89     3051   3227   1811  -1221   -603    279       C  
ATOM    686  N   TYR A  90      32.414  50.838  42.759  1.00 13.10           N  
ANISOU  686  N   TYR A  90     2092   1338   1547    116   -293   -676       N  
ATOM    687  CA  TYR A  90      32.742  50.761  44.158  1.00 13.64           C  
ANISOU  687  CA  TYR A  90     1967   1630   1587     18   -341   -447       C  
ATOM    688  C   TYR A  90      34.241  50.653  44.391  1.00 14.29           C  
ANISOU  688  C   TYR A  90     1662   1990   1776    298   -647   -555       C  
ATOM    689  O   TYR A  90      34.929  49.939  43.666  1.00 15.57           O  
ANISOU  689  O   TYR A  90     1797   1635   2483    318   -378   -672       O  
ATOM    690  CB  TYR A  90      31.991  49.643  44.858  1.00 13.47           C  
ANISOU  690  CB  TYR A  90     1991   1609   1518     90   -181   -244       C  
ATOM    691  CG  TYR A  90      32.251  48.255  44.318  1.00 15.86           C  
ANISOU  691  CG  TYR A  90     2734   1537   1756     35   -416   -669       C  
ATOM    692  CD1 TYR A  90      31.605  47.780  43.183  1.00 16.58           C  
ANISOU  692  CD1 TYR A  90     3035   1576   1690     36   -453   -277       C  
ATOM    693  CD2 TYR A  90      33.071  47.380  45.017  1.00 16.05           C  
ANISOU  693  CD2 TYR A  90     2751   1532   1817    305   -543   -556       C  
ATOM    694  CE1 TYR A  90      31.823  46.507  42.709  1.00 18.04           C  
ANISOU  694  CE1 TYR A  90     3396   1535   1924   -278   -359   -402       C  
ATOM    695  CE2 TYR A  90      33.282  46.084  44.537  1.00 17.45           C  
ANISOU  695  CE2 TYR A  90     3157   1561   1913    421   -516   -620       C  
ATOM    696  CZ  TYR A  90      32.670  45.657  43.394  1.00 18.19           C  
ANISOU  696  CZ  TYR A  90     3443   1556   1913    126    -13  -1064       C  
ATOM    697  OH  TYR A  90      32.853  44.348  42.927  1.00 19.13           O  
ANISOU  697  OH  TYR A  90     3615   1642   2013    215   -476   -472       O  
ATOM    698  N   SER A  91      34.726  51.367  45.395  1.00 16.53           N  
ANISOU  698  N   SER A  91     2076   2271   1933   -354   -410   -804       N  
ATOM    699  CA  SER A  91      36.151  51.404  45.698  1.00 16.94           C  
ANISOU  699  CA  SER A  91     1946   2464   2027   -194   -504   -780       C  
ATOM    700  C   SER A  91      36.489  50.455  46.843  1.00 17.17           C  
ANISOU  700  C   SER A  91     2006   2460   2059    327     24   -618       C  
ATOM    701  O   SER A  91      35.587  49.958  47.532  1.00 16.81           O  
ANISOU  701  O   SER A  91     2158   2072   2156    393   -459   -509       O  
ATOM    702  CB  SER A  91      36.586  52.827  46.061  1.00 16.27           C  
ANISOU  702  CB  SER A  91     1480   2436   2268    -10   -926   -688       C  
ATOM    703  OG  SER A  91      35.998  53.194  47.336  1.00 17.78           O  
ANISOU  703  OG  SER A  91     2399   2203   2155      1   -244   -347       O  
ATOM    704  N   SER A  92      37.767  50.221  47.032  1.00 18.11           N  
ANISOU  704  N   SER A  92     1782   2662   2437    658   -750   -802       N  
ATOM    705  CA  SER A  92      38.284  49.342  48.058  1.00 18.36           C  
ANISOU  705  CA  SER A  92     1881   2479   2614    369   -890   -604       C  
ATOM    706  C   SER A  92      38.041  49.920  49.451  1.00 19.91           C  
ANISOU  706  C   SER A  92     2528   2528   2507    575  -1340   -518       C  
ATOM    707  O   SER A  92      38.030  49.181  50.443  1.00 23.28           O  
ANISOU  707  O   SER A  92     3720   2514   2610    635   -799     83       O  
ATOM    708  CB  SER A  92      39.777  49.076  47.858  1.00 20.49           C  
ANISOU  708  CB  SER A  92     1716   2721   3349    517   -747   -398       C  
ATOM    709  OG  SER A  92      40.449  50.239  47.486  1.00 27.50           O  
ANISOU  709  OG  SER A  92     2447   3732   4271   -733  -1008    439       O  
ATOM    710  N   ASP A  93      37.670  51.190  49.491  1.00 19.65           N  
ANISOU  710  N   ASP A  93     2205   2523   2739    567  -1181   -630       N  
ATOM    711  CA  ASP A  93      37.288  51.858  50.714  1.00 19.47           C  
ANISOU  711  CA  ASP A  93     2214   2573   2610    545  -1047   -831       C  
ATOM    712  C   ASP A  93      35.823  52.181  50.786  1.00 18.67           C  
ANISOU  712  C   ASP A  93     2248   2610   2234    470   -481   -310       C  
ATOM    713  O   ASP A  93      35.352  52.975  51.591  1.00 17.88           O  
ANISOU  713  O   ASP A  93     2128   2850   1815    186    -48   -198       O  
ATOM    714  CB  ASP A  93      38.187  52.996  51.090  1.00 20.58           C  
ANISOU  714  CB  ASP A  93     2323   3017   2480    219   -924   -710       C  
ATOM    715  CG  ASP A  93      38.342  54.104  50.095  1.00 21.73           C  
ANISOU  715  CG  ASP A  93     2560   3110   2587   -325  -1447   -567       C  
ATOM    716  OD1 ASP A  93      38.025  53.906  48.911  1.00 19.83           O  
ANISOU  716  OD1 ASP A  93     2667   2261   2608     73  -1026   -353       O  
ATOM    717  OD2 ASP A  93      38.842  55.207  50.493  1.00 24.26           O  
ANISOU  717  OD2 ASP A  93     3230   3451   2536   -957   -858   -430       O  
ATOM    718  N   TRP A  94      35.005  51.560  49.918  1.00 16.89           N  
ANISOU  718  N   TRP A  94     2211   2139   2067    800   -200   -411       N  
ATOM    719  CA  TRP A  94      33.585  51.604  50.050  1.00 17.13           C  
ANISOU  719  CA  TRP A  94     1904   2638   1966    956   -234   -234       C  
ATOM    720  C   TRP A  94      32.859  52.853  49.721  1.00 16.24           C  
ANISOU  720  C   TRP A  94     1632   2732   1807    842   -244   -557       C  
ATOM    721  O   TRP A  94      31.681  53.071  50.084  1.00 17.68           O  
ANISOU  721  O   TRP A  94     1993   2454   2271    400    135    302       O  
ATOM    722  CB  TRP A  94      33.081  50.848  51.268  1.00 20.14           C  
ANISOU  722  CB  TRP A  94     2883   2573   2196     42   -393    154       C  
ATOM    723  CG  TRP A  94      33.759  49.506  51.378  1.00 22.03           C  
ANISOU  723  CG  TRP A  94     3254   2553   2563    320   -890    408       C  
ATOM    724  CD1 TRP A  94      34.700  49.131  52.294  1.00 22.23           C  
ANISOU  724  CD1 TRP A  94     3171   2465   2811    376   -495     47       C  
ATOM    725  CD2 TRP A  94      33.605  48.402  50.478  1.00 24.21           C  
ANISOU  725  CD2 TRP A  94     4095   2566   2537    269   -773     34       C  
ATOM    726  NE1 TRP A  94      35.117  47.850  52.028  1.00 24.16           N  
ANISOU  726  NE1 TRP A  94     3576   2425   3179    367   -451    230       N  
ATOM    727  CE2 TRP A  94      34.449  47.375  50.927  1.00 25.63           C  
ANISOU  727  CE2 TRP A  94     4326   2454   2959    197    -56   -130       C  
ATOM    728  CE3 TRP A  94      32.811  48.175  49.350  1.00 25.72           C  
ANISOU  728  CE3 TRP A  94     4786   2645   2342    -38   -404   -402       C  
ATOM    729  CZ2 TRP A  94      34.528  46.144  50.284  1.00 27.25           C  
ANISOU  729  CZ2 TRP A  94     4848   2505   3002    388   -831    141       C  
ATOM    730  CZ3 TRP A  94      32.885  46.945  48.711  1.00 27.39           C  
ANISOU  730  CZ3 TRP A  94     5308   2613   2487     34   -724     29       C  
ATOM    731  CH2 TRP A  94      33.736  45.939  49.185  1.00 28.37           C  
ANISOU  731  CH2 TRP A  94     5387   2652   2741    256   -567    234       C  
ATOM    732  N   LEU A  95      33.462  53.668  48.843  1.00 16.63           N  
ANISOU  732  N   LEU A  95     1871   2565   1882    680   -710  -1253       N  
ATOM    733  CA  LEU A  95      32.736  54.759  48.180  1.00 15.78           C  
ANISOU  733  CA  LEU A  95     1573   2542   1881    518   -609  -1007       C  
ATOM    734  C   LEU A  95      31.932  54.165  47.013  1.00 16.02           C  
ANISOU  734  C   LEU A  95     2015   2148   1923    244   -563   -902       C  
ATOM    735  O   LEU A  95      32.433  53.212  46.350  1.00 16.65           O  
ANISOU  735  O   LEU A  95     2050   2192   2086    574   -791   -965       O  
ATOM    736  CB  LEU A  95      33.759  55.732  47.602  1.00 17.28           C  
ANISOU  736  CB  LEU A  95     1506   2350   2709    499   -765   -698       C  
ATOM    737  CG  LEU A  95      34.725  56.433  48.533  1.00 20.23           C  
ANISOU  737  CG  LEU A  95     2193   2691   2802     35   -673  -1214       C  
ATOM    738  CD1 LEU A  95      35.655  57.339  47.697  1.00 24.99           C  
ANISOU  738  CD1 LEU A  95     3190   2761   3542   -921   -743   -579       C  
ATOM    739  CD2 LEU A  95      33.986  57.294  49.548  1.00 22.76           C  
ANISOU  739  CD2 LEU A  95     3550   2349   2747    381  -1285   -867       C  
ATOM    740  N   ILE A  96      30.723  54.622  46.813  1.00 13.46           N  
ANISOU  740  N   ILE A  96     2239   1946    929    251   -337   -753       N  
ATOM    741  CA  ILE A  96      29.869  54.035  45.760  1.00 12.81           C  
ANISOU  741  CA  ILE A  96     2331   1389   1147    270   -103   -634       C  
ATOM    742  C   ILE A  96      29.335  55.142  44.842  1.00 11.36           C  
ANISOU  742  C   ILE A  96     1651   1344   1323    135    409  -1099       C  
ATOM    743  O   ILE A  96      28.756  56.096  45.329  1.00 11.74           O  
ANISOU  743  O   ILE A  96     2165   1323    972    117    450   -443       O  
ATOM    744  CB AILE A  96      28.623  53.376  46.423  0.50 13.28           C  
ANISOU  744  CB AILE A  96     2515   1423   1110    121   -525   -230       C  
ATOM    745  CB BILE A  96      28.716  53.221  46.329  0.50 13.18           C  
ANISOU  745  CB BILE A  96     2453   1446   1110    193   -506   -248       C  
ATOM    746  CG1AILE A  96      28.976  52.574  47.680  0.50 14.18           C  
ANISOU  746  CG1AILE A  96     2836   1484   1069    120   -344   -264       C  
ATOM    747  CG1BILE A  96      29.162  52.165  47.360  0.50 13.90           C  
ANISOU  747  CG1BILE A  96     2767   1470   1043    130   -575   -182       C  
ATOM    748  CG2AILE A  96      27.901  52.505  45.412  0.50 14.91           C  
ANISOU  748  CG2AILE A  96     2937   1597   1129   -283   -192   -198       C  
ATOM    749  CG2BILE A  96      27.910  52.556  45.217  0.50 13.78           C  
ANISOU  749  CG2BILE A  96     2378   1667   1191     65   -312   -155       C  
ATOM    750  CD1AILE A  96      29.596  51.228  47.356  0.50 14.47           C  
ANISOU  750  CD1AILE A  96     3934   1228    335   -313   -234   -365       C  
ATOM    751  CD1BILE A  96      28.036  51.337  47.902  0.50 17.78           C  
ANISOU  751  CD1BILE A  96     3798   1986    972   -819    368    -78       C  
ATOM    752  N   TYR A  97      29.557  54.974  43.556  1.00 10.22           N  
ANISOU  752  N   TYR A  97     1605    942   1337    107    132   -826       N  
ATOM    753  CA  TYR A  97      29.127  55.886  42.523  1.00 10.88           C  
ANISOU  753  CA  TYR A  97     1792   1056   1285    211    -45   -240       C  
ATOM    754  C   TYR A  97      28.232  55.128  41.538  1.00 11.72           C  
ANISOU  754  C   TYR A  97     2358    938   1156    -23   -253   -109       C  
ATOM    755  O   TYR A  97      28.293  53.906  41.391  1.00 12.21           O  
ANISOU  755  O   TYR A  97     2110   1027   1503    197   -326   -297       O  
ATOM    756  CB  TYR A  97      30.327  56.512  41.782  1.00 12.41           C  
ANISOU  756  CB  TYR A  97     2197   1320   1199    -76    485   -658       C  
ATOM    757  CG  TYR A  97      31.008  57.600  42.569  1.00 11.71           C  
ANISOU  757  CG  TYR A  97     1883    948   1619    241    233   -481       C  
ATOM    758  CD1 TYR A  97      31.861  57.282  43.633  1.00 11.99           C  
ANISOU  758  CD1 TYR A  97     1703   1086   1768    -60   -663   -454       C  
ATOM    759  CD2 TYR A  97      30.825  58.949  42.286  1.00 12.71           C  
ANISOU  759  CD2 TYR A  97     2085   1010   1736    265    415   -274       C  
ATOM    760  CE1 TYR A  97      32.477  58.253  44.403  1.00 13.43           C  
ANISOU  760  CE1 TYR A  97     2153   1142   1808   -193   -618   -325       C  
ATOM    761  CE2 TYR A  97      31.464  59.915  43.052  1.00 14.09           C  
ANISOU  761  CE2 TYR A  97     2341   1037   1974   -131    432   -569       C  
ATOM    762  CZ  TYR A  97      32.329  59.571  44.056  1.00 14.00           C  
ANISOU  762  CZ  TYR A  97     2080   1089   2148   -216    100   -416       C  
ATOM    763  OH  TYR A  97      32.913  60.557  44.840  1.00 14.92           O  
ANISOU  763  OH  TYR A  97     2359   1140   2170    -95   -484   -502       O  
ATOM    764  N   LYS A  98      27.439  55.905  40.842  1.00 11.31           N  
ANISOU  764  N   LYS A  98     2682    946    670    -45   -133   -261       N  
ATOM    765  CA  LYS A  98      26.570  55.380  39.791  1.00 14.92           C  
ANISOU  765  CA  LYS A  98     3370   1811    489   -498    206    200       C  
ATOM    766  C   LYS A  98      26.864  56.075  38.476  1.00 11.02           C  
ANISOU  766  C   LYS A  98     2258   1327    601    144    404    -88       C  
ATOM    767  O   LYS A  98      27.154  57.276  38.444  1.00 14.20           O  
ANISOU  767  O   LYS A  98     2921   1594    879   -853     88   -116       O  
ATOM    768  CB  LYS A  98      25.141  55.574  40.212  1.00 19.73           C  
ANISOU  768  CB  LYS A  98     2991   3566    938  -1443    228    646       C  
ATOM    769  CG  LYS A  98      24.180  56.287  39.373  1.00 22.04           C  
ANISOU  769  CG  LYS A  98     2804   2917   2653   -268   1044    714       C  
ATOM    770  CD  LYS A  98      22.767  56.173  39.905  1.00 23.86           C  
ANISOU  770  CD  LYS A  98     2899   3126   3039   -420    860   -118       C  
ATOM    771  CE  LYS A  98      22.158  57.511  40.237  1.00 25.31           C  
ANISOU  771  CE  LYS A  98     2666   3109   3840   -295    223    254       C  
ATOM    772  NZ  LYS A  98      20.653  57.400  40.132  1.00 32.15           N  
ANISOU  772  NZ  LYS A  98     2340   3771   6104   -122   1263    239       N  
ATOM    773  N   THR A  99      26.703  55.332  37.396  1.00 11.21           N  
ANISOU  773  N   THR A  99     2332   1282    643    168    579    -63       N  
ATOM    774  CA  THR A  99      26.631  55.867  36.065  1.00 13.28           C  
ANISOU  774  CA  THR A  99     3166   1289    590    -77    693    -84       C  
ATOM    775  C   THR A  99      25.416  55.268  35.345  1.00 13.45           C  
ANISOU  775  C   THR A  99     3208   1356    548   -135   -288   -273       C  
ATOM    776  O   THR A  99      25.129  54.072  35.519  1.00 13.47           O  
ANISOU  776  O   THR A  99     2633   1421   1065     -4   -194      1       O  
ATOM    777  CB  THR A  99      27.894  55.709  35.235  1.00 13.61           C  
ANISOU  777  CB  THR A  99     3073   1547    553   -102    355   -166       C  
ATOM    778  OG1 THR A  99      27.742  56.188  33.910  1.00 14.56           O  
ANISOU  778  OG1 THR A  99     3136   1811    583   -120    385     49       O  
ATOM    779  CG2 THR A  99      28.291  54.230  35.090  1.00 13.95           C  
ANISOU  779  CG2 THR A  99     2473   1693   1133    353    771    -64       C  
ATOM    780  N   THR A 100      24.715  56.060  34.566  1.00 14.21           N  
ANISOU  780  N   THR A 100     2991   1328   1080    -31   -417    -20       N  
ATOM    781  CA  THR A 100      23.619  55.522  33.745  1.00 15.00           C  
ANISOU  781  CA  THR A 100     2987   1531   1182    -70   -480    305       C  
ATOM    782  C   THR A 100      23.861  55.860  32.280  1.00 15.62           C  
ANISOU  782  C   THR A 100     3365   1452   1117    154   -492    129       C  
ATOM    783  O   THR A 100      22.961  55.769  31.450  1.00 18.33           O  
ANISOU  783  O   THR A 100     3477   2353   1136   -207   -466    116       O  
ATOM    784  CB  THR A 100      22.255  56.088  34.187  1.00 15.50           C  
ANISOU  784  CB  THR A 100     2828   1741   1320     91   -412    359       C  
ATOM    785  OG1 THR A 100      22.323  57.510  34.193  1.00 19.63           O  
ANISOU  785  OG1 THR A 100     3140   1686   2634    666   -384    -10       O  
ATOM    786  CG2 THR A 100      21.916  55.646  35.595  1.00 18.50           C  
ANISOU  786  CG2 THR A 100     2892   2895   1242   -298     -2     91       C  
ATOM    787  N   ASP A 101      25.092  56.285  31.982  1.00 17.78           N  
ANISOU  787  N   ASP A 101     4099   1642   1013   -714     87   -287       N  
ATOM    788  CA  ASP A 101      25.448  56.719  30.639  1.00 18.50           C  
ANISOU  788  CA  ASP A 101     4368   1710    953   -556   -204     51       C  
ATOM    789  C   ASP A 101      26.698  56.096  30.100  1.00 18.57           C  
ANISOU  789  C   ASP A 101     4228   1909    919   -863    798     60       C  
ATOM    790  O   ASP A 101      27.512  56.725  29.412  1.00 21.06           O  
ANISOU  790  O   ASP A 101     4588   2523    892  -1240    666    -45       O  
ATOM    791  CB  ASP A 101      25.473  58.242  30.555  1.00 18.97           C  
ANISOU  791  CB  ASP A 101     4766   1801    640   -572    -46     28       C  
ATOM    792  CG  ASP A 101      26.502  58.918  31.411  1.00 18.39           C  
ANISOU  792  CG  ASP A 101     4631   1476    880   -470    260   -346       C  
ATOM    793  OD1 ASP A 101      27.330  58.261  32.057  1.00 18.63           O  
ANISOU  793  OD1 ASP A 101     4124   1643   1312   -391     66    -46       O  
ATOM    794  OD2 ASP A 101      26.501  60.183  31.418  1.00 22.23           O  
ANISOU  794  OD2 ASP A 101     4882   1488   2077   -331   -380    161       O  
ATOM    795  N   HIS A 102      26.937  54.822  30.461  1.00 19.35           N  
ANISOU  795  N   HIS A 102     3804   1943   1607   -558      3    147       N  
ATOM    796  CA  HIS A 102      28.104  54.110  29.968  1.00 18.33           C  
ANISOU  796  CA  HIS A 102     3420   2444   1102     29    371   -210       C  
ATOM    797  C   HIS A 102      29.412  54.793  30.363  1.00 17.70           C  
ANISOU  797  C   HIS A 102     3248   2224   1255    216   1446   -671       C  
ATOM    798  O   HIS A 102      30.316  54.941  29.549  1.00 20.81           O  
ANISOU  798  O   HIS A 102     4049   2917    942   -695   1103   -933       O  
ATOM    799  CB  HIS A 102      28.066  53.916  28.440  1.00 23.18           C  
ANISOU  799  CB  HIS A 102     4484   3313   1009   -420    822   -652       C  
ATOM    800  CG  HIS A 102      27.578  52.571  28.033  1.00 26.09           C  
ANISOU  800  CG  HIS A 102     5461   3480    973   -970    216   -555       C  
ATOM    801  ND1 HIS A 102      26.337  52.378  27.444  1.00 30.22           N  
ANISOU  801  ND1 HIS A 102     5498   3868   2115  -1459    968   -685       N  
ATOM    802  CD2 HIS A 102      28.104  51.325  28.205  1.00 28.68           C  
ANISOU  802  CD2 HIS A 102     6170   3353   1373  -1104   -453    -70       C  
ATOM    803  CE1 HIS A 102      26.132  51.100  27.275  1.00 33.19           C  
ANISOU  803  CE1 HIS A 102     6389   3936   2284  -1966   1463   -753       C  
ATOM    804  NE2 HIS A 102      27.185  50.440  27.744  1.00 32.82           N  
ANISOU  804  NE2 HIS A 102     6792   3614   2065  -1690    787   -164       N  
ATOM    805  N   TYR A 103      29.534  55.160  31.633  1.00 17.45           N  
ANISOU  805  N   TYR A 103     3409   2043   1179   -132    960    -21       N  
ATOM    806  CA  TYR A 103      30.778  55.637  32.213  1.00 19.43           C  
ANISOU  806  CA  TYR A 103     3692   2181   1510   -490    646    -72       C  
ATOM    807  C   TYR A 103      31.152  57.036  31.801  1.00 20.70           C  
ANISOU  807  C   TYR A 103     4194   2220   1452   -716   1015   -620       C  
ATOM    808  O   TYR A 103      32.322  57.451  31.990  1.00 22.74           O  
ANISOU  808  O   TYR A 103     4208   2129   2304   -694    966   -566       O  
ATOM    809  CB  TYR A 103      31.941  54.690  31.970  1.00 20.36           C  
ANISOU  809  CB  TYR A 103     3535   2269   1932   -794    421     27       C  
ATOM    810  CG  TYR A 103      31.699  53.215  32.088  1.00 19.16           C  
ANISOU  810  CG  TYR A 103     3452   2216   1610   -396    558   -317       C  
ATOM    811  CD1 TYR A 103      31.786  52.519  33.276  1.00 17.53           C  
ANISOU  811  CD1 TYR A 103     2777   2309   1574      9    343    -49       C  
ATOM    812  CD2 TYR A 103      31.517  52.456  30.912  1.00 21.63           C  
ANISOU  812  CD2 TYR A 103     4370   2287   1562   -601    392   -510       C  
ATOM    813  CE1 TYR A 103      31.599  51.129  33.312  1.00 15.87           C  
ANISOU  813  CE1 TYR A 103     2400   2361   1270    -63    512   -208       C  
ATOM    814  CE2 TYR A 103      31.280  51.108  30.953  1.00 19.00           C  
ANISOU  814  CE2 TYR A 103     3664   2308   1245   -326   -418    149       C  
ATOM    815  CZ  TYR A 103      31.347  50.437  32.168  1.00 15.41           C  
ANISOU  815  CZ  TYR A 103     2311   2265   1280    128    356   -120       C  
ATOM    816  OH  TYR A 103      31.143  49.061  32.161  1.00 18.13           O  
ANISOU  816  OH  TYR A 103     2907   2255   1729   -165    325   -216       O  
ATOM    817  N   GLN A 104      30.238  57.807  31.221  1.00 19.88           N  
ANISOU  817  N   GLN A 104     4417   2215    920   -839    882   -373       N  
ATOM    818  CA  GLN A 104      30.617  59.181  30.831  1.00 21.35           C  
ANISOU  818  CA  GLN A 104     4565   2207   1339   -700    770    -62       C  
ATOM    819  C   GLN A 104      30.586  60.118  32.026  1.00 21.37           C  
ANISOU  819  C   GLN A 104     4571   2091   1458   -760   1017     12       C  
ATOM    820  O   GLN A 104      31.447  60.985  32.169  1.00 24.13           O  
ANISOU  820  O   GLN A 104     4993   2366   1809  -1203   1258    -33       O  
ATOM    821  CB  GLN A 104      29.657  59.691  29.760  1.00 21.71           C  
ANISOU  821  CB  GLN A 104     4652   2102   1495   -393    738   -158       C  
ATOM    822  CG  GLN A 104      29.776  58.921  28.453  1.00 32.05           C  
ANISOU  822  CG  GLN A 104     7785   3324   1068  -1655   1133   -582       C  
ATOM    823  CD  GLN A 104      28.840  59.460  27.391  1.00 32.02           C  
ANISOU  823  CD  GLN A 104     7349   3549   1269  -1142   1063   -122       C  
ATOM    824  OE1 GLN A 104      29.242  60.269  26.570  1.00 32.95           O  
ANISOU  824  OE1 GLN A 104     8024   2670   1824   -919    243    241       O  
ATOM    825  NE2 GLN A 104      27.583  59.008  27.445  1.00 35.06           N  
ANISOU  825  NE2 GLN A 104     6690   4389   2241   -662    640    151       N  
ATOM    826  N   THR A 105      29.555  59.966  32.856  1.00 21.35           N  
ANISOU  826  N   THR A 105     5122   1987   1001  -1059    897    -57       N  
ATOM    827  CA  THR A 105      29.432  60.791  34.054  1.00 22.99           C  
ANISOU  827  CA  THR A 105     5962   1793    980  -1464   1126   -456       C  
ATOM    828  C   THR A 105      29.050  59.899  35.245  1.00 18.49           C  
ANISOU  828  C   THR A 105     4253   1838    936  -1048    810   -641       C  
ATOM    829  O   THR A 105      28.453  58.859  35.090  1.00 15.88           O  
ANISOU  829  O   THR A 105     3609   1608    815   -583    -62    -94       O  
ATOM    830  CB  THR A 105      28.388  61.894  33.902  1.00 25.14           C  
ANISOU  830  CB  THR A 105     6708   1513   1331  -1100   1283   -362       C  
ATOM    831  OG1 THR A 105      27.090  61.367  33.781  1.00 23.71           O  
ANISOU  831  OG1 THR A 105     5446   1778   1786    111    186     24       O  
ATOM    832  CG2 THR A 105      28.656  62.762  32.683  1.00 24.95           C  
ANISOU  832  CG2 THR A 105     6453   2084    942   -319    850     88       C  
ATOM    833  N   PHE A 106      29.443  60.377  36.418  1.00 16.86           N  
ANISOU  833  N   PHE A 106     3893   1594    919   -667    912   -209       N  
ATOM    834  CA  PHE A 106      29.228  59.634  37.647  1.00 14.44           C  
ANISOU  834  CA  PHE A 106     2891   1727    867   -590    277   -208       C  
ATOM    835  C   PHE A 106      28.630  60.571  38.706  1.00 13.97           C  
ANISOU  835  C   PHE A 106     2781   1506   1024   -458    422   -312       C  
ATOM    836  O   PHE A 106      29.004  61.739  38.750  1.00 17.83           O  
ANISOU  836  O   PHE A 106     3805   1556   1415  -1030    360    -52       O  
ATOM    837  CB  PHE A 106      30.584  59.122  38.171  1.00 15.80           C  
ANISOU  837  CB  PHE A 106     2758   1605   1641   -221    548   -399       C  
ATOM    838  CG  PHE A 106      31.277  58.166  37.234  1.00 16.33           C  
ANISOU  838  CG  PHE A 106     3078   1686   1443   -265    860   -811       C  
ATOM    839  CD1 PHE A 106      30.988  56.812  37.196  1.00 16.79           C  
ANISOU  839  CD1 PHE A 106     2973   1616   1791     45    558   -711       C  
ATOM    840  CD2 PHE A 106      32.234  58.675  36.352  1.00 16.89           C  
ANISOU  840  CD2 PHE A 106     3136   1912   1370   -348    658   -638       C  
ATOM    841  CE1 PHE A 106      31.595  55.960  36.282  1.00 16.81           C  
ANISOU  841  CE1 PHE A 106     2744   1646   1997    119    424   -336       C  
ATOM    842  CE2 PHE A 106      32.853  57.816  35.462  1.00 17.23           C  
ANISOU  842  CE2 PHE A 106     3170   1883   1493   -146    536   -668       C  
ATOM    843  CZ  PHE A 106      32.576  56.472  35.473  1.00 17.40           C  
ANISOU  843  CZ  PHE A 106     2847   1862   1904     25    174   -495       C  
ATOM    844  N   THR A 107      27.826  59.993  39.569  1.00 13.00           N  
ANISOU  844  N   THR A 107     2623   1440    877   -242    476    -30       N  
ATOM    845  CA  THR A 107      27.361  60.727  40.752  1.00 13.97           C  
ANISOU  845  CA  THR A 107     3071   1353    884   -453    608    152       C  
ATOM    846  C   THR A 107      27.481  59.830  41.978  1.00 13.43           C  
ANISOU  846  C   THR A 107     2904   1347    852   -618    831   -293       C  
ATOM    847  O   THR A 107      27.308  58.600  41.877  1.00 11.77           O  
ANISOU  847  O   THR A 107     2425   1206    839   -173   -141    -30       O  
ATOM    848  CB  THR A 107      25.901  61.175  40.593  1.00 14.59           C  
ANISOU  848  CB  THR A 107     2704   1519   1320    109    793    360       C  
ATOM    849  OG1 THR A 107      25.065  60.072  40.377  1.00 19.65           O  
ANISOU  849  OG1 THR A 107     2905   2167   2396   -440   -352    203       O  
ATOM    850  CG2 THR A 107      25.764  62.162  39.467  1.00 16.06           C  
ANISOU  850  CG2 THR A 107     2900   1795   1406    455    687    724       C  
ATOM    851  N   LYS A 108      27.772  60.423  43.111  1.00 11.11           N  
ANISOU  851  N   LYS A 108     2351    913    956   -182    171   -372       N  
ATOM    852  CA  LYS A 108      27.924  59.599  44.349  1.00 10.65           C  
ANISOU  852  CA  LYS A 108     2226    994    827    133     36   -185       C  
ATOM    853  C   LYS A 108      26.552  59.170  44.858  1.00 10.00           C  
ANISOU  853  C   LYS A 108     2123    903    776    240    341   -210       C  
ATOM    854  O   LYS A 108      25.592  59.958  44.873  1.00 11.99           O  
ANISOU  854  O   LYS A 108     2242    907   1408    187     55     63       O  
ATOM    855  CB  LYS A 108      28.537  60.542  45.403  1.00 12.38           C  
ANISOU  855  CB  LYS A 108     2500   1255    949   -255   -103   -173       C  
ATOM    856  CG  LYS A 108      28.868  59.876  46.714  1.00 12.26           C  
ANISOU  856  CG  LYS A 108     2031   1715    914   -204    112    -53       C  
ATOM    857  CD  LYS A 108      29.582  60.886  47.647  1.00 15.49           C  
ANISOU  857  CD  LYS A 108     2555   2386    944   -750   -207    -94       C  
ATOM    858  CE  LYS A 108      29.741  60.298  49.034  1.00 14.76           C  
ANISOU  858  CE  LYS A 108     2107   2595    907    -85     18   -197       C  
ATOM    859  NZ  LYS A 108      30.747  59.205  49.066  1.00 18.56           N  
ANISOU  859  NZ  LYS A 108     3050   2317   1684    498   -398   -232       N  
ATOM    860  N   ILE A 109      26.435  57.920  45.294  1.00 10.25           N  
ANISOU  860  N   ILE A 109     2001    929    963    254    353    -35       N  
ATOM    861  CA  ILE A 109      25.209  57.445  45.913  1.00 10.96           C  
ANISOU  861  CA  ILE A 109     1991   1145   1028    194    326     11       C  
ATOM    862  C   ILE A 109      25.423  56.879  47.315  1.00 11.60           C  
ANISOU  862  C   ILE A 109     2415   1017    977   -112     98     -5       C  
ATOM    863  O   ILE A 109      24.428  56.729  48.032  1.00 12.61           O  
ANISOU  863  O   ILE A 109     2093   1700    999     -1    309    257       O  
ATOM    864  CB  ILE A 109      24.488  56.412  45.036  1.00 11.43           C  
ANISOU  864  CB  ILE A 109     1978   1411    953     28    143   -193       C  
ATOM    865  CG1 ILE A 109      25.244  55.151  44.716  1.00 12.61           C  
ANISOU  865  CG1 ILE A 109     2541   1308    943    -36    294   -429       C  
ATOM    866  CG2 ILE A 109      23.931  57.101  43.806  1.00 12.56           C  
ANISOU  866  CG2 ILE A 109     2369   1565    837    227   -122   -212       C  
ATOM    867  CD1 ILE A 109      24.460  53.993  44.160  1.00 13.99           C  
ANISOU  867  CD1 ILE A 109     2435   1326   1556     25   -165   -318       C  
ATOM    868  N   ARG A 110      26.646  56.621  47.736  1.00 12.10           N  
ANISOU  868  N   ARG A 110     2234   1272   1092    -57   -295   -101       N  
ATOM    869  CA  ARG A 110      27.033  56.297  49.061  1.00 12.73           C  
ANISOU  869  CA  ARG A 110     2187   1535   1115     59   -258     40       C  
ATOM    870  C   ARG A 110      28.442  56.843  49.414  1.00 14.19           C  
ANISOU  870  C   ARG A 110     2236   2305    849   -203    -40     68       C  
ATOM    871  O   ARG A 110      28.707  57.047  50.614  1.00 20.57           O  
ANISOU  871  O   ARG A 110     3472   3489    854  -1153   -452   -204       O  
ATOM    872  CB  ARG A 110      26.957  54.879  49.506  1.00 13.31           C  
ANISOU  872  CB  ARG A 110     2386   1461   1212    217    130     76       C  
ATOM    873  CG  ARG A 110      25.692  54.073  49.245  1.00 13.37           C  
ANISOU  873  CG  ARG A 110     2412   1332   1336    174    267   -397       C  
ATOM    874  CD  ARG A 110      24.573  54.428  50.204  1.00 14.07           C  
ANISOU  874  CD  ARG A 110     2655   1435   1255   -119    218    417       C  
ATOM    875  NE  ARG A 110      23.404  53.563  50.069  1.00 14.69           N  
ANISOU  875  NE  ARG A 110     2424   1569   1589     64    532    287       N  
ATOM    876  CZ  ARG A 110      22.439  53.681  49.181  1.00 13.99           C  
ANISOU  876  CZ  ARG A 110     2135   1286   1895    258    815    106       C  
ATOM    877  NH1 ARG A 110      22.472  54.683  48.314  1.00 14.54           N  
ANISOU  877  NH1 ARG A 110     2360   1352   1810    -76    550    154       N  
ATOM    878  NH2 ARG A 110      21.426  52.821  49.119  1.00 16.55           N  
ANISOU  878  NH2 ARG A 110     2892   1416   1980   -366    731    -43       N  
ATOM    879  OXT ARG A 110      29.332  56.795  48.546  1.00 14.66           O  
ANISOU  879  OXT ARG A 110     2272   2261   1036   -298    372   -276       O  
TER     880      ARG A 110                                                      
ATOM    881  N   VAL B   3     -17.297  34.921  57.728  0.00 35.21           N  
ANISOU  881  N   VAL B   3     3188   5019   5170   -525    121   -961       N  
ATOM    882  CA  VAL B   3     -15.997  35.558  57.909  1.00 29.99           C  
ANISOU  882  CA  VAL B   3     2709   4727   3958      0    120   -961       C  
ATOM    883  C   VAL B   3     -14.868  34.655  57.423  1.00 30.05           C  
ANISOU  883  C   VAL B   3     3261   4269   3887     27    347   -985       C  
ATOM    884  O   VAL B   3     -15.027  33.427  57.376  1.00 35.82           O  
ANISOU  884  O   VAL B   3     4050   4322   5239   -804    703  -1297       O  
ATOM    885  CB  VAL B   3     -15.746  35.867  59.414  1.00 31.20           C  
ANISOU  885  CB  VAL B   3     3268   4740   3845    859   1129  -1240       C  
ATOM    886  CG1 VAL B   3     -17.005  36.280  60.111  1.00 32.55           C  
ANISOU  886  CG1 VAL B   3     3109   5564   3694    -66      4    343       C  
ATOM    887  CG2 VAL B   3     -15.081  34.680  60.080  1.00 34.75           C  
ANISOU  887  CG2 VAL B   3     4965   4530   3709   1215  -1617    237       C  
ATOM    888  N   ILE B   4     -13.701  35.226  57.118  1.00 22.20           N  
ANISOU  888  N   ILE B   4     3087   3174   2173    658    198   -639       N  
ATOM    889  CA  ILE B   4     -12.550  34.355  56.756  1.00 20.52           C  
ANISOU  889  CA  ILE B   4     3417   3087   1291   1080   -189   -545       C  
ATOM    890  C   ILE B   4     -11.611  34.326  57.968  1.00 19.66           C  
ANISOU  890  C   ILE B   4     3248   2793   1428   1012    -98   -870       C  
ATOM    891  O   ILE B   4     -11.014  35.333  58.311  1.00 19.67           O  
ANISOU  891  O   ILE B   4     2895   2614   1966   1113   -572   -864       O  
ATOM    892  CB  ILE B   4     -11.781  34.947  55.554  1.00 21.92           C  
ANISOU  892  CB  ILE B   4     3055   3927   1346   1068   -907   -544       C  
ATOM    893  CG1 ILE B   4     -12.634  35.216  54.330  1.00 22.02           C  
ANISOU  893  CG1 ILE B   4     3376   3731   1260   1002   -284   -474       C  
ATOM    894  CG2 ILE B   4     -10.584  34.064  55.215  1.00 22.88           C  
ANISOU  894  CG2 ILE B   4     2656   4248   1792   1039   -455   -986       C  
ATOM    895  CD1 ILE B   4     -11.955  35.880  53.180  1.00 29.45           C  
ANISOU  895  CD1 ILE B   4     5066   4962   1161   -345   -670    658       C  
ATOM    896  N   ASN B   5     -11.580  33.181  58.642  1.00 16.71           N  
ANISOU  896  N   ASN B   5     1931   2780   1640    536   -312   -756       N  
ATOM    897  CA  ASN B   5     -10.778  33.049  59.854  1.00 15.80           C  
ANISOU  897  CA  ASN B   5     1798   2451   1755    764   -159   -804       C  
ATOM    898  C   ASN B   5     -10.174  31.667  60.014  1.00 16.61           C  
ANISOU  898  C   ASN B   5     2292   2400   1618    523   -167   -539       C  
ATOM    899  O   ASN B   5      -9.814  31.323  61.139  1.00 16.39           O  
ANISOU  899  O   ASN B   5     2313   2349   1564    671    210   -465       O  
ATOM    900  CB  ASN B   5     -11.646  33.408  61.069  1.00 16.35           C  
ANISOU  900  CB  ASN B   5     1761   2770   1682    777    -63   -594       C  
ATOM    901  CG  ASN B   5     -12.636  32.323  61.415  1.00 19.11           C  
ANISOU  901  CG  ASN B   5     1785   3539   1937    339    968  -1026       C  
ATOM    902  OD1 ASN B   5     -13.002  31.498  60.575  1.00 22.34           O  
ANISOU  902  OD1 ASN B   5     2572   3953   1963   -619     57   -920       O  
ATOM    903  ND2 ASN B   5     -13.127  32.379  62.649  1.00 22.05           N  
ANISOU  903  ND2 ASN B   5     2446   4037   1895   -123    740   -923       N  
ATOM    904  N   THR B   6     -10.022  30.924  58.918  1.00 14.70           N  
ANISOU  904  N   THR B   6     1635   2339   1612    462   -534   -663       N  
ATOM    905  CA  THR B   6      -9.349  29.617  58.956  1.00 15.00           C  
ANISOU  905  CA  THR B   6     1582   2355   1763    384   -233   -306       C  
ATOM    906  C   THR B   6      -7.895  29.735  58.533  1.00 14.02           C  
ANISOU  906  C   THR B   6     1953   1790   1586    225   -186   -838       C  
ATOM    907  O   THR B   6      -7.498  30.711  57.861  1.00 13.44           O  
ANISOU  907  O   THR B   6     1962   1792   1351    340   -137   -608       O  
ATOM    908  CB  THR B   6     -10.035  28.581  58.043  1.00 16.44           C  
ANISOU  908  CB  THR B   6     1892   2384   1971    104    -95   -440       C  
ATOM    909  OG1 THR B   6     -10.063  29.066  56.710  1.00 18.33           O  
ANISOU  909  OG1 THR B   6     2006   3131   1829    197   -261   -692       O  
ATOM    910  CG2 THR B   6     -11.474  28.358  58.490  1.00 19.59           C  
ANISOU  910  CG2 THR B   6     2016   3194   2232   -352    362   -970       C  
ATOM    911  N   PHE B   7      -7.086  28.748  58.886  1.00 14.12           N  
ANISOU  911  N   PHE B   7     2105   1654   1605    293    226   -438       N  
ATOM    912  CA  PHE B   7      -5.661  28.820  58.494  1.00 14.03           C  
ANISOU  912  CA  PHE B   7     2058   1505   1766    419    -96   -341       C  
ATOM    913  C   PHE B   7      -5.544  28.927  56.970  1.00 13.08           C  
ANISOU  913  C   PHE B   7     1755   1422   1793    397   -145   -242       C  
ATOM    914  O   PHE B   7      -4.785  29.740  56.464  1.00 14.34           O  
ANISOU  914  O   PHE B   7     1913   1564   1971     87    356   -577       O  
ATOM    915  CB  PHE B   7      -4.919  27.572  58.968  1.00 14.48           C  
ANISOU  915  CB  PHE B   7     2250   1449   1803    421    245     62       C  
ATOM    916  CG  PHE B   7      -4.530  27.607  60.423  1.00 14.65           C  
ANISOU  916  CG  PHE B   7     2142   1609   1816    556    255      9       C  
ATOM    917  CD1 PHE B   7      -3.618  28.577  60.884  1.00 14.13           C  
ANISOU  917  CD1 PHE B   7     1694   1940   1736    723   -298   -157       C  
ATOM    918  CD2 PHE B   7      -5.049  26.719  61.333  1.00 15.74           C  
ANISOU  918  CD2 PHE B   7     2433   1779   1767    457   -122    147       C  
ATOM    919  CE1 PHE B   7      -3.265  28.621  62.188  1.00 15.19           C  
ANISOU  919  CE1 PHE B   7     2037   1971   1764    652    -21   -665       C  
ATOM    920  CE2 PHE B   7      -4.698  26.775  62.665  1.00 16.68           C  
ANISOU  920  CE2 PHE B   7     2532   2037   1769    385    409     -8       C  
ATOM    921  CZ  PHE B   7      -3.807  27.726  63.099  1.00 15.72           C  
ANISOU  921  CZ  PHE B   7     2303   1958   1712    616    305   -438       C  
ATOM    922  N   ASP B   8      -6.255  28.047  56.246  1.00 13.87           N  
ANISOU  922  N   ASP B   8     1634   1946   1689    183    334   -274       N  
ATOM    923  CA  ASP B   8      -6.118  28.049  54.774  1.00 15.11           C  
ANISOU  923  CA  ASP B   8     1754   2339   1649    528     33   -846       C  
ATOM    924  C   ASP B   8      -6.745  29.288  54.166  1.00 15.00           C  
ANISOU  924  C   ASP B   8     1887   2368   1445    382   -122   -580       C  
ATOM    925  O   ASP B   8      -6.184  29.892  53.253  1.00 16.65           O  
ANISOU  925  O   ASP B   8     2373   2660   1292    199     61   -187       O  
ATOM    926  CB  ASP B   8      -6.736  26.782  54.194  1.00 19.11           C  
ANISOU  926  CB  ASP B   8     3296   2480   1484   -138     65   -561       C  
ATOM    927  CG  ASP B   8      -5.872  25.554  54.355  1.00 23.86           C  
ANISOU  927  CG  ASP B   8     4274   2247   2543     84    385    -38       C  
ATOM    928  OD1 ASP B   8      -4.680  25.583  54.006  1.00 21.59           O  
ANISOU  928  OD1 ASP B   8     3910   1956   2338    915    281   -498       O  
ATOM    929  OD2 ASP B   8      -6.361  24.577  54.966  1.00 27.25           O  
ANISOU  929  OD2 ASP B   8     4626   2297   3429    -32    369    238       O  
ATOM    930  N   GLY B   9      -7.892  29.729  54.699  1.00 15.34           N  
ANISOU  930  N   GLY B   9     2253   1925   1651    154    -46   -365       N  
ATOM    931  CA  GLY B   9      -8.560  30.912  54.119  1.00 16.02           C  
ANISOU  931  CA  GLY B   9     2472   1918   1698    109    135   -184       C  
ATOM    932  C   GLY B   9      -7.760  32.179  54.310  1.00 13.87           C  
ANISOU  932  C   GLY B   9     2086   1864   1322    393    384   -226       C  
ATOM    933  O   GLY B   9      -7.551  32.960  53.362  1.00 14.95           O  
ANISOU  933  O   GLY B   9     2398   1939   1344    374   -115   -406       O  
ATOM    934  N   VAL B  10      -7.204  32.377  55.508  1.00 13.27           N  
ANISOU  934  N   VAL B  10     1860   1853   1330    603   -138   -442       N  
ATOM    935  CA  VAL B  10      -6.375  33.550  55.755  1.00 12.86           C  
ANISOU  935  CA  VAL B  10     2180   1577   1130    673   -294     10       C  
ATOM    936  C   VAL B  10      -5.037  33.461  55.058  1.00 13.33           C  
ANISOU  936  C   VAL B  10     2347   1534   1183    281    -47    114       C  
ATOM    937  O   VAL B  10      -4.558  34.463  54.480  1.00 13.76           O  
ANISOU  937  O   VAL B  10     2533   1552   1144    394    -64    208       O  
ATOM    938  CB  VAL B  10      -6.229  33.816  57.268  1.00 13.78           C  
ANISOU  938  CB  VAL B  10     2361   1766   1110    545    121    -72       C  
ATOM    939  CG1 VAL B  10      -5.375  35.069  57.498  1.00 14.70           C  
ANISOU  939  CG1 VAL B  10     2713   1797   1074    329    148   -375       C  
ATOM    940  CG2 VAL B  10      -7.632  34.070  57.857  1.00 13.98           C  
ANISOU  940  CG2 VAL B  10     2637   1591   1085    384   -100   -189       C  
ATOM    941  N   ALA B  11      -4.422  32.289  55.000  1.00 13.04           N  
ANISOU  941  N   ALA B  11     2139   1603   1211    466    245   -133       N  
ATOM    942  CA  ALA B  11      -3.158  32.111  54.309  1.00 13.33           C  
ANISOU  942  CA  ALA B  11     2071   1686   1306    339   -125   -586       C  
ATOM    943  C   ALA B  11      -3.264  32.499  52.839  1.00 14.11           C  
ANISOU  943  C   ALA B  11     2123   1966   1271    564   -161   -228       C  
ATOM    944  O   ALA B  11      -2.429  33.254  52.307  1.00 15.16           O  
ANISOU  944  O   ALA B  11     2553   1881   1325    329     95   -391       O  
ATOM    945  CB  ALA B  11      -2.626  30.699  54.433  1.00 13.79           C  
ANISOU  945  CB  ALA B  11     1875   1770   1597    631     43   -695       C  
ATOM    946  N   ASP B  12      -4.311  32.029  52.197  1.00 13.82           N  
ANISOU  946  N   ASP B  12     2094   1988   1168    664   -514   -422       N  
ATOM    947  CA  ASP B  12      -4.542  32.284  50.770  1.00 15.33           C  
ANISOU  947  CA  ASP B  12     2369   2342   1112    903   -635   -372       C  
ATOM    948  C   ASP B  12      -4.846  33.749  50.515  1.00 14.71           C  
ANISOU  948  C   ASP B  12     2344   2354    891    877    -58    -36       C  
ATOM    949  O   ASP B  12      -4.318  34.328  49.575  1.00 16.91           O  
ANISOU  949  O   ASP B  12     3229   2515    682    691    151    176       O  
ATOM    950  CB  ASP B  12      -5.567  31.367  50.188  1.00 17.59           C  
ANISOU  950  CB  ASP B  12     3425   2470    789    338  -1184   -793       C  
ATOM    951  CG  ASP B  12      -5.089  29.933  50.031  1.00 22.40           C  
ANISOU  951  CG  ASP B  12     5006   2340   1164    497   -914   -959       C  
ATOM    952  OD1 ASP B  12      -3.859  29.706  50.123  1.00 24.16           O  
ANISOU  952  OD1 ASP B  12     4605   2179   2396   1783  -1313   -705       O  
ATOM    953  OD2 ASP B  12      -5.958  29.070  49.841  1.00 29.38           O  
ANISOU  953  OD2 ASP B  12     6663   2622   1878   -664    447   -617       O  
ATOM    954  N   TYR B  13      -5.646  34.340  51.421  1.00 15.17           N  
ANISOU  954  N   TYR B  13     2542   2291    932    847    229    138       N  
ATOM    955  CA  TYR B  13      -5.997  35.766  51.284  1.00 15.51           C  
ANISOU  955  CA  TYR B  13     2693   2268    931    785    237    162       C  
ATOM    956  C   TYR B  13      -4.759  36.634  51.408  1.00 16.14           C  
ANISOU  956  C   TYR B  13     2947   2269    916    567    325    215       C  
ATOM    957  O   TYR B  13      -4.540  37.553  50.607  1.00 16.58           O  
ANISOU  957  O   TYR B  13     3038   2157   1107    623    418     75       O  
ATOM    958  CB  TYR B  13      -7.058  36.157  52.294  1.00 15.55           C  
ANISOU  958  CB  TYR B  13     2632   2379    898    973    444    301       C  
ATOM    959  CG  TYR B  13      -7.754  37.476  52.060  1.00 16.34           C  
ANISOU  959  CG  TYR B  13     2924   2411    873   1389     -5     72       C  
ATOM    960  CD1 TYR B  13      -7.198  38.691  52.444  1.00 19.16           C  
ANISOU  960  CD1 TYR B  13     3780   2424   1078    903    725    -60       C  
ATOM    961  CD2 TYR B  13      -9.024  37.513  51.479  1.00 17.20           C  
ANISOU  961  CD2 TYR B  13     2703   2422   1409   1619   -655   -132       C  
ATOM    962  CE1 TYR B  13      -7.868  39.896  52.219  1.00 20.50           C  
ANISOU  962  CE1 TYR B  13     4064   2394   1332    822    427    -46       C  
ATOM    963  CE2 TYR B  13      -9.704  38.691  51.307  1.00 19.27           C  
ANISOU  963  CE2 TYR B  13     3129   2324   1867   1392   -738   -115       C  
ATOM    964  CZ  TYR B  13      -9.125  39.887  51.656  1.00 21.18           C  
ANISOU  964  CZ  TYR B  13     3877   2333   1837   1013     38   -158       C  
ATOM    965  OH  TYR B  13      -9.821  41.084  51.508  1.00 23.87           O  
ANISOU  965  OH  TYR B  13     4032   2407   2630   1278   -222    -43       O  
ATOM    966  N   LEU B  14      -3.908  36.370  52.387  1.00 15.34           N  
ANISOU  966  N   LEU B  14     2693   2037   1097    719    468    208       N  
ATOM    967  CA  LEU B  14      -2.670  37.108  52.571  1.00 15.36           C  
ANISOU  967  CA  LEU B  14     2596   1934   1306    858    149     10       C  
ATOM    968  C   LEU B  14      -1.754  37.049  51.368  1.00 15.91           C  
ANISOU  968  C   LEU B  14     2479   2232   1335    779    733    192       C  
ATOM    969  O   LEU B  14      -1.191  38.058  50.948  1.00 17.17           O  
ANISOU  969  O   LEU B  14     3121   2250   1154    493    326     98       O  
ATOM    970  CB  LEU B  14      -1.920  36.626  53.810  1.00 15.73           C  
ANISOU  970  CB  LEU B  14     2654   2027   1297    508    -25   -570       C  
ATOM    971  CG  LEU B  14      -2.472  37.065  55.155  1.00 16.12           C  
ANISOU  971  CG  LEU B  14     2497   2351   1278    316    614   -910       C  
ATOM    972  CD1 LEU B  14      -1.906  36.170  56.258  1.00 16.47           C  
ANISOU  972  CD1 LEU B  14     2755   2247   1257    120    192    339       C  
ATOM    973  CD2 LEU B  14      -2.253  38.538  55.438  1.00 18.47           C  
ANISOU  973  CD2 LEU B  14     3533   2274   1211    938    -18   -550       C  
ATOM    974  N   GLN B  15      -1.550  35.849  50.813  1.00 15.90           N  
ANISOU  974  N   GLN B  15     2682   2274   1086    938    397   -172       N  
ATOM    975  CA  GLN B  15      -0.611  35.706  49.682  1.00 17.07           C  
ANISOU  975  CA  GLN B  15     3203   2250   1034    804    504   -292       C  
ATOM    976  C   GLN B  15      -1.130  36.372  48.424  1.00 16.88           C  
ANISOU  976  C   GLN B  15     3069   2331   1016    996    173    109       C  
ATOM    977  O   GLN B  15      -0.349  36.808  47.577  1.00 19.47           O  
ANISOU  977  O   GLN B  15     3566   2690   1141    234    189     91       O  
ATOM    978  CB  GLN B  15      -0.285  34.241  49.444  1.00 17.26           C  
ANISOU  978  CB  GLN B  15     2842   2289   1429    980    684   -248       C  
ATOM    979  CG  GLN B  15       0.520  33.590  50.552  1.00 18.34           C  
ANISOU  979  CG  GLN B  15     3394   2239   1337   1007    117    175       C  
ATOM    980  CD  GLN B  15       1.306  32.383  50.087  1.00 18.72           C  
ANISOU  980  CD  GLN B  15     3182   2214   1717   1136    697    -70       C  
ATOM    981  OE1 GLN B  15       0.740  31.441  49.499  1.00 22.92           O  
ANISOU  981  OE1 GLN B  15     3699   1906   3102    488    869   -234       O  
ATOM    982  NE2 GLN B  15       2.597  32.370  50.359  1.00 21.07           N  
ANISOU  982  NE2 GLN B  15     3302   2387   2316    801   1151    448       N  
ATOM    983  N   THR B  16      -2.439  36.476  48.274  1.00 18.25           N  
ANISOU  983  N   THR B  16     3246   2268   1421    701    456    161       N  
ATOM    984  CA  THR B  16      -3.085  37.045  47.123  1.00 18.11           C  
ANISOU  984  CA  THR B  16     3064   2262   1556    660    -96    261       C  
ATOM    985  C   THR B  16      -3.287  38.554  47.204  1.00 19.59           C  
ANISOU  985  C   THR B  16     3825   2209   1410    687    108    420       C  
ATOM    986  O   THR B  16      -3.039  39.266  46.218  1.00 21.99           O  
ANISOU  986  O   THR B  16     4611   2388   1355    467    117    348       O  
ATOM    987  CB  THR B  16      -4.457  36.391  46.838  1.00 21.71           C  
ANISOU  987  CB  THR B  16     3589   3050   1610   -116   -622   -169       C  
ATOM    988  OG1 THR B  16      -4.295  34.960  46.727  1.00 28.19           O  
ANISOU  988  OG1 THR B  16     4800   2983   2928   -775    344   -689       O  
ATOM    989  CG2 THR B  16      -5.037  36.871  45.531  1.00 22.18           C  
ANISOU  989  CG2 THR B  16     3007   3910   1511    191   -487    214       C  
ATOM    990  N   TYR B  17      -3.790  39.042  48.343  1.00 19.41           N  
ANISOU  990  N   TYR B  17     3670   2270   1436   1040     77    229       N  
ATOM    991  CA  TYR B  17      -4.140  40.426  48.527  1.00 19.68           C  
ANISOU  991  CA  TYR B  17     3714   2216   1548    945    129    476       C  
ATOM    992  C   TYR B  17      -3.231  41.226  49.419  1.00 19.50           C  
ANISOU  992  C   TYR B  17     3773   2135   1503    929    341    514       C  
ATOM    993  O   TYR B  17      -3.352  42.475  49.509  1.00 22.22           O  
ANISOU  993  O   TYR B  17     4240   2030   2171    682     60    246       O  
ATOM    994  CB  TYR B  17      -5.612  40.587  48.952  1.00 21.87           C  
ANISOU  994  CB  TYR B  17     3483   2459   2366   1120     62    382       C  
ATOM    995  CG  TYR B  17      -6.556  39.849  48.029  1.00 25.07           C  
ANISOU  995  CG  TYR B  17     3763   3286   2475    539   -453    248       C  
ATOM    996  CD1 TYR B  17      -6.705  40.263  46.705  1.00 30.60           C  
ANISOU  996  CD1 TYR B  17     5221   4117   2288   -570   -676    248       C  
ATOM    997  CD2 TYR B  17      -7.249  38.733  48.454  1.00 24.78           C  
ANISOU  997  CD2 TYR B  17     3567   3250   2598    669   -419    497       C  
ATOM    998  CE1 TYR B  17      -7.561  39.589  45.841  1.00 32.93           C  
ANISOU  998  CE1 TYR B  17     5306   4863   2342   -856  -1048    676       C  
ATOM    999  CE2 TYR B  17      -8.103  38.054  47.603  1.00 29.41           C  
ANISOU  999  CE2 TYR B  17     4273   4216   2686   -277   -304    405       C  
ATOM   1000  CZ  TYR B  17      -8.253  38.490  46.302  1.00 33.42           C  
ANISOU 1000  CZ  TYR B  17     5025   5131   2541  -1023  -1099    600       C  
ATOM   1001  OH  TYR B  17      -9.089  37.790  45.447  1.00 41.94           O  
ANISOU 1001  OH  TYR B  17     6472   6923   2539  -2686   -696     73       O  
ATOM   1002  N   HIS B  18      -2.329  40.590  50.129  1.00 19.22           N  
ANISOU 1002  N   HIS B  18     3748   2172   1384    885    553    454       N  
ATOM   1003  CA  HIS B  18      -1.281  41.242  50.886  1.00 20.19           C  
ANISOU 1003  CA  HIS B  18     4070   2331   1270    534    845    -81       C  
ATOM   1004  C   HIS B  18      -1.800  42.114  52.006  1.00 19.90           C  
ANISOU 1004  C   HIS B  18     3975   2037   1550    559    923   -108       C  
ATOM   1005  O   HIS B  18      -1.192  43.120  52.382  1.00 23.27           O  
ANISOU 1005  O   HIS B  18     4941   2189   1710   -113    941   -292       O  
ATOM   1006  CB  HIS B  18      -0.371  42.062  49.967  1.00 24.02           C  
ANISOU 1006  CB  HIS B  18     5010   2874   1243   -329    978   -355       C  
ATOM   1007  CG  HIS B  18       0.013  41.296  48.734  1.00 24.00           C  
ANISOU 1007  CG  HIS B  18     5068   2832   1220   -837   1184   -472       C  
ATOM   1008  ND1 HIS B  18      -0.243  41.715  47.450  1.00 25.40           N  
ANISOU 1008  ND1 HIS B  18     5696   2726   1227   -993   1008   -334       N  
ATOM   1009  CD2 HIS B  18       0.570  40.051  48.645  1.00 24.79           C  
ANISOU 1009  CD2 HIS B  18     5307   2785   1325   -687    854   -265       C  
ATOM   1010  CE1 HIS B  18       0.182  40.779  46.616  1.00 25.26           C  
ANISOU 1010  CE1 HIS B  18     5513   2830   1254   -643   1164   -276       C  
ATOM   1011  NE2 HIS B  18       0.669  39.768  47.315  1.00 25.72           N  
ANISOU 1011  NE2 HIS B  18     5658   2787   1327   -764   1035     90       N  
ATOM   1012  N   LYS B  19      -2.900  41.693  52.588  1.00 20.48           N  
ANISOU 1012  N   LYS B  19     4303   2591    887    215    853    367       N  
ATOM   1013  CA  LYS B  19      -3.470  42.341  53.773  1.00 21.34           C  
ANISOU 1013  CA  LYS B  19     4999   2462    648    108    370    472       C  
ATOM   1014  C   LYS B  19      -4.427  41.322  54.404  1.00 17.52           C  
ANISOU 1014  C   LYS B  19     3282   2383    991   1086    582   -403       C  
ATOM   1015  O   LYS B  19      -4.768  40.326  53.743  1.00 20.08           O  
ANISOU 1015  O   LYS B  19     4241   2409    977    597    224   -262       O  
ATOM   1016  CB  LYS B  19      -4.234  43.601  53.381  1.00 23.97           C  
ANISOU 1016  CB  LYS B  19     5019   2398   1690    268    301    681       C  
ATOM   1017  CG  LYS B  19      -5.443  43.403  52.485  1.00 24.78           C  
ANISOU 1017  CG  LYS B  19     4169   2682   2566    613    694    521       C  
ATOM   1018  CD  LYS B  19      -5.986  44.783  52.048  1.00 25.99           C  
ANISOU 1018  CD  LYS B  19     4090   2739   3048    880   -518    764       C  
ATOM   1019  CE  LYS B  19      -7.390  44.662  51.497  0.50 26.16           C  
ANISOU 1019  CE  LYS B  19     4329   2515   3096    564   -559    155       C  
ATOM   1020  NZ  LYS B  19      -7.457  43.665  50.380  0.50 31.03           N  
ANISOU 1020  NZ  LYS B  19     6005   3071   2714   -238    293   -931       N  
ATOM   1021  N   LEU B  20      -4.837  41.580  55.634  1.00 17.45           N  
ANISOU 1021  N   LEU B  20     3092   2512   1027    865    328   -481       N  
ATOM   1022  CA  LEU B  20      -5.816  40.704  56.268  1.00 18.43           C  
ANISOU 1022  CA  LEU B  20     2997   2848   1156    727    -38   -262       C  
ATOM   1023  C   LEU B  20      -7.216  41.026  55.742  1.00 17.47           C  
ANISOU 1023  C   LEU B  20     3175   2595    868    700    391   -532       C  
ATOM   1024  O   LEU B  20      -7.516  42.184  55.409  1.00 21.05           O  
ANISOU 1024  O   LEU B  20     3567   2522   1908    855   -220      0       O  
ATOM   1025  CB  LEU B  20      -5.781  40.848  57.788  1.00 15.96           C  
ANISOU 1025  CB  LEU B  20     2573   2293   1197    601   -382   -774       C  
ATOM   1026  CG  LEU B  20      -4.549  40.293  58.514  1.00 16.41           C  
ANISOU 1026  CG  LEU B  20     2518   2316   1400     44   -308   -794       C  
ATOM   1027  CD1 LEU B  20      -4.425  40.918  59.897  1.00 16.83           C  
ANISOU 1027  CD1 LEU B  20     2590   2487   1317    362    -78   -267       C  
ATOM   1028  CD2 LEU B  20      -4.553  38.794  58.592  1.00 15.75           C  
ANISOU 1028  CD2 LEU B  20     2001   2331   1654    232   -215   -252       C  
ATOM   1029  N   PRO B  21      -8.095  40.045  55.844  1.00 18.84           N  
ANISOU 1029  N   PRO B  21     3157   2737   1264    565   -104   -261       N  
ATOM   1030  CA  PRO B  21      -9.520  40.255  55.545  1.00 19.40           C  
ANISOU 1030  CA  PRO B  21     2838   2925   1608    987    217   -387       C  
ATOM   1031  C   PRO B  21     -10.135  41.270  56.506  1.00 19.89           C  
ANISOU 1031  C   PRO B  21     2880   3004   1674   1133    -91   -111       C  
ATOM   1032  O   PRO B  21      -9.566  41.613  57.544  1.00 18.98           O  
ANISOU 1032  O   PRO B  21     3037   2505   1671   1339   -318   -232       O  
ATOM   1033  CB  PRO B  21     -10.131  38.887  55.687  1.00 21.19           C  
ANISOU 1033  CB  PRO B  21     2734   2996   2321    831    -20   -523       C  
ATOM   1034  CG  PRO B  21      -9.048  37.921  55.921  1.00 21.48           C  
ANISOU 1034  CG  PRO B  21     3019   2824   2317    455   -351    158       C  
ATOM   1035  CD  PRO B  21      -7.806  38.668  56.231  1.00 18.87           C  
ANISOU 1035  CD  PRO B  21     3044   2682   1445    517     87   -376       C  
ATOM   1036  N   ASP B  22     -11.301  41.784  56.125  1.00 20.35           N  
ANISOU 1036  N   ASP B  22     2783   3063   1887   1421    -25   -209       N  
ATOM   1037  CA  ASP B  22     -11.949  42.855  56.815  1.00 21.29           C  
ANISOU 1037  CA  ASP B  22     3177   2898   2013   1350   -559     11       C  
ATOM   1038  C   ASP B  22     -12.428  42.592  58.203  1.00 21.52           C  
ANISOU 1038  C   ASP B  22     3436   2889   1850   1278   -257   -530       C  
ATOM   1039  O   ASP B  22     -12.738  43.551  58.960  1.00 24.77           O  
ANISOU 1039  O   ASP B  22     4598   2897   1915   1549    274   -150       O  
ATOM   1040  CB  ASP B  22     -13.022  43.512  55.921  1.00 21.58           C  
ANISOU 1040  CB  ASP B  22     3572   2801   1826   1522   -653    411       C  
ATOM   1041  CG  ASP B  22     -12.378  44.074  54.658  1.00 27.32           C  
ANISOU 1041  CG  ASP B  22     4753   3385   1864    214  -1010    393       C  
ATOM   1042  OD1 ASP B  22     -11.495  44.974  54.826  1.00 40.07           O  
ANISOU 1042  OD1 ASP B  22     5702   5243   3722  -1446   -940   -257       O  
ATOM   1043  OD2 ASP B  22     -12.765  43.688  53.555  0.30 38.37           O  
ANISOU 1043  OD2 ASP B  22     7769   4513   1761  -1221   -429   -514       O  
ATOM   1044  N   ASN B  23     -12.484  41.352  58.644  1.00 20.51           N  
ANISOU 1044  N   ASN B  23     3031   2906   1854   1028   -483   -182       N  
ATOM   1045  CA  ASN B  23     -12.894  40.966  59.977  1.00 18.55           C  
ANISOU 1045  CA  ASN B  23     2154   2956   1939    982     67   -246       C  
ATOM   1046  C   ASN B  23     -11.802  41.086  61.025  1.00 17.95           C  
ANISOU 1046  C   ASN B  23     2211   2709   1901    959    -93   -265       C  
ATOM   1047  O   ASN B  23     -12.062  40.785  62.214  1.00 20.51           O  
ANISOU 1047  O   ASN B  23     2052   3826   1915    390    107    106       O  
ATOM   1048  CB  ASN B  23     -13.531  39.578  59.999  1.00 21.14           C  
ANISOU 1048  CB  ASN B  23     2348   3197   2486    561    674   -563       C  
ATOM   1049  CG  ASN B  23     -12.621  38.512  59.422  1.00 21.07           C  
ANISOU 1049  CG  ASN B  23     3151   2889   1966    211   1059   -512       C  
ATOM   1050  OD1 ASN B  23     -12.189  38.685  58.280  1.00 24.05           O  
ANISOU 1050  OD1 ASN B  23     3708   3310   1784    933   1232   -312       O  
ATOM   1051  ND2 ASN B  23     -12.273  37.519  60.181  1.00 22.47           N  
ANISOU 1051  ND2 ASN B  23     3273   2900   2052    326   -248   -735       N  
ATOM   1052  N   TYR B  24     -10.622  41.569  60.682  1.00 16.31           N  
ANISOU 1052  N   TYR B  24     2482   2364   1351    808   -209   -340       N  
ATOM   1053  CA  TYR B  24      -9.523  41.764  61.600  1.00 14.79           C  
ANISOU 1053  CA  TYR B  24     2563   1699   1357    899    257   -440       C  
ATOM   1054  C   TYR B  24      -9.354  43.204  62.072  1.00 15.15           C  
ANISOU 1054  C   TYR B  24     2586   1678   1491    837    173   -239       C  
ATOM   1055  O   TYR B  24      -9.431  44.158  61.289  1.00 18.30           O  
ANISOU 1055  O   TYR B  24     3753   1815   1386    624    577    133       O  
ATOM   1056  CB  TYR B  24      -8.196  41.237  61.035  1.00 15.61           C  
ANISOU 1056  CB  TYR B  24     2720   1654   1555    753     88   -165       C  
ATOM   1057  CG  TYR B  24      -8.140  39.717  61.038  1.00 13.03           C  
ANISOU 1057  CG  TYR B  24     2027   1710   1215    653   -355    -72       C  
ATOM   1058  CD1 TYR B  24      -7.712  39.016  62.165  1.00 12.55           C  
ANISOU 1058  CD1 TYR B  24     1924   1774   1071    494   -278   -325       C  
ATOM   1059  CD2 TYR B  24      -8.587  38.984  59.948  1.00 13.59           C  
ANISOU 1059  CD2 TYR B  24     2373   1801    988    839    -71    -42       C  
ATOM   1060  CE1 TYR B  24      -7.695  37.630  62.184  1.00 11.91           C  
ANISOU 1060  CE1 TYR B  24     1730   1812    984    730    -30   -604       C  
ATOM   1061  CE2 TYR B  24      -8.555  37.596  59.953  1.00 12.66           C  
ANISOU 1061  CE2 TYR B  24     2068   1823    919    660   -451   -305       C  
ATOM   1062  CZ  TYR B  24      -8.113  36.923  61.068  1.00 11.87           C  
ANISOU 1062  CZ  TYR B  24     1804   1712    993    623   -255   -500       C  
ATOM   1063  OH  TYR B  24      -8.091  35.542  61.065  1.00 15.66           O  
ANISOU 1063  OH  TYR B  24     2723   1668   1558    621   -244   -735       O  
ATOM   1064  N   ILE B  25      -9.102  43.352  63.363  1.00 14.60           N  
ANISOU 1064  N   ILE B  25     2370   1679   1500    499    330   -489       N  
ATOM   1065  CA  ILE B  25      -8.671  44.641  63.949  1.00 13.68           C  
ANISOU 1065  CA  ILE B  25     2066   1595   1539    684    514   -354       C  
ATOM   1066  C   ILE B  25      -7.458  44.392  64.832  1.00 13.80           C  
ANISOU 1066  C   ILE B  25     2054   1167   2022    519    569     13       C  
ATOM   1067  O   ILE B  25      -7.278  43.306  65.385  1.00 13.11           O  
ANISOU 1067  O   ILE B  25     2027   1253   1701    301    294    -59       O  
ATOM   1068  CB  ILE B  25      -9.813  45.266  64.780  1.00 14.61           C  
ANISOU 1068  CB  ILE B  25     1710   1749   2094    657    216     40       C  
ATOM   1069  CG1 ILE B  25     -10.335  44.337  65.893  1.00 16.77           C  
ANISOU 1069  CG1 ILE B  25     1858   2637   1877    193    662   -424       C  
ATOM   1070  CG2 ILE B  25     -10.964  45.721  63.874  1.00 16.27           C  
ANISOU 1070  CG2 ILE B  25     1946   1816   2419    576     87    262       C  
ATOM   1071  CD1 ILE B  25     -11.387  45.022  66.753  1.00 16.75           C  
ANISOU 1071  CD1 ILE B  25     2278   2707   1379    924     27   -607       C  
ATOM   1072  N   THR B  26      -6.626  45.417  65.048  1.00 15.27           N  
ANISOU 1072  N   THR B  26     2474   1270   2059    172    752    257       N  
ATOM   1073  CA  THR B  26      -5.454  45.232  65.895  1.00 15.05           C  
ANISOU 1073  CA  THR B  26     2101   1430   2187    274    790     54       C  
ATOM   1074  C   THR B  26      -5.823  45.300  67.374  1.00 14.45           C  
ANISOU 1074  C   THR B  26     2204   1110   2178    261    521    334       C  
ATOM   1075  O   THR B  26      -6.892  45.720  67.749  1.00 14.60           O  
ANISOU 1075  O   THR B  26     1973   1488   2085    436    311    -49       O  
ATOM   1076  CB  THR B  26      -4.399  46.316  65.650  1.00 17.61           C  
ANISOU 1076  CB  THR B  26     2996   1575   2121   -414   1773   -180       C  
ATOM   1077  OG1 THR B  26      -4.952  47.563  66.054  1.00 18.07           O  
ANISOU 1077  OG1 THR B  26     2750   1656   2459    -84    669   -538       O  
ATOM   1078  CG2 THR B  26      -4.016  46.413  64.180  1.00 18.83           C  
ANISOU 1078  CG2 THR B  26     2685   2335   2134   -611    583   -155       C  
ATOM   1079  N   LYS B  27      -4.853  44.875  68.225  1.00 14.66           N  
ANISOU 1079  N   LYS B  27     2392    865   2312    289    249    144       N  
ATOM   1080  CA  LYS B  27      -5.077  44.882  69.655  1.00 15.02           C  
ANISOU 1080  CA  LYS B  27     1865   1628   2216     68    203     18       C  
ATOM   1081  C   LYS B  27      -5.429  46.286  70.151  1.00 13.82           C  
ANISOU 1081  C   LYS B  27     1706   1575   1971    -89    257    150       C  
ATOM   1082  O   LYS B  27      -6.337  46.451  70.946  1.00 13.78           O  
ANISOU 1082  O   LYS B  27     2041   1539   1657   -132    309   -324       O  
ATOM   1083  CB  LYS B  27      -3.888  44.342  70.454  1.00 15.51           C  
ANISOU 1083  CB  LYS B  27     1612   1794   2487    385     35   -351       C  
ATOM   1084  CG  LYS B  27      -3.704  42.859  70.399  1.00 22.12           C  
ANISOU 1084  CG  LYS B  27     2808   1695   3903    846   -283     89       C  
ATOM   1085  CD  LYS B  27      -2.624  42.338  71.301  1.00 23.27           C  
ANISOU 1085  CD  LYS B  27     2447   1631   4766    717   -580    217       C  
ATOM   1086  CE  LYS B  27      -1.216  42.535  70.752  1.00 25.87           C  
ANISOU 1086  CE  LYS B  27     2602   3155   4071     66   -871    -83       C  
ATOM   1087  NZ  LYS B  27      -1.078  42.066  69.345  1.00 31.70           N  
ANISOU 1087  NZ  LYS B  27     3908   4344   3793  -1068   -297   -986       N  
ATOM   1088  N   SER B  28      -4.703  47.281  69.647  1.00 15.26           N  
ANISOU 1088  N   SER B  28     1796   1678   2323   -254    698   -102       N  
ATOM   1089  CA  SER B  28      -4.973  48.659  70.047  1.00 17.35           C  
ANISOU 1089  CA  SER B  28     2251   1581   2760   -288    699   -230       C  
ATOM   1090  C   SER B  28      -6.314  49.168  69.571  1.00 16.38           C  
ANISOU 1090  C   SER B  28     2403   1412   2409   -156    569   -391       C  
ATOM   1091  O   SER B  28      -7.022  49.872  70.292  1.00 16.83           O  
ANISOU 1091  O   SER B  28     2875   1041   2479     -2    233   -475       O  
ATOM   1092  CB ASER B  28      -3.844  49.592  69.663  0.50 19.65           C  
ANISOU 1092  CB ASER B  28     2715   1824   2928   -716    994   -483       C  
ATOM   1093  CB BSER B  28      -3.845  49.574  69.548  0.50 18.81           C  
ANISOU 1093  CB BSER B  28     2706   1808   2635   -690   1004   -500       C  
ATOM   1094  OG ASER B  28      -2.662  49.301  70.374  0.50 20.73           O  
ANISOU 1094  OG ASER B  28     2404   1651   3820   -481    -14   -648       O  
ATOM   1095  OG BSER B  28      -3.841  49.632  68.127  0.50 24.23           O  
ANISOU 1095  OG BSER B  28     4042   2571   2594  -1211    291    -46       O  
ATOM   1096  N   GLU B  29      -6.731  48.787  68.350  1.00 15.95           N  
ANISOU 1096  N   GLU B  29     2528   1097   2436    -44    409    -57       N  
ATOM   1097  CA  GLU B  29      -8.070  49.185  67.898  1.00 15.27           C  
ANISOU 1097  CA  GLU B  29     2713    861   2227   -139    784   -283       C  
ATOM   1098  C   GLU B  29      -9.134  48.534  68.771  1.00 15.12           C  
ANISOU 1098  C   GLU B  29     2579   1004   2160    -99     95    109       C  
ATOM   1099  O   GLU B  29     -10.163  49.142  69.076  1.00 14.74           O  
ANISOU 1099  O   GLU B  29     2193   1313   2094    646    303     50       O  
ATOM   1100  CB  GLU B  29      -8.283  48.737  66.440  1.00 16.68           C  
ANISOU 1100  CB  GLU B  29     2693   1453   2191    331    719    -77       C  
ATOM   1101  CG  GLU B  29      -7.623  49.662  65.453  1.00 23.60           C  
ANISOU 1101  CG  GLU B  29     4705   2102   2162   -746    812    204       C  
ATOM   1102  CD  GLU B  29      -7.435  49.141  64.061  1.00 28.98           C  
ANISOU 1102  CD  GLU B  29     6480   2534   2000  -1345   1071    364       C  
ATOM   1103  OE1 GLU B  29      -7.676  47.939  63.771  1.00 23.36           O  
ANISOU 1103  OE1 GLU B  29     4379   2245   2254     -2     80    103       O  
ATOM   1104  OE2 GLU B  29      -7.024  49.959  63.211  1.00 30.39           O  
ANISOU 1104  OE2 GLU B  29     7057   2479   2010   -949    744    290       O  
ATOM   1105  N   ALA B  30      -8.924  47.258  69.097  1.00 11.80           N  
ANISOU 1105  N   ALA B  30     2017   1150   1317     81    341     53       N  
ATOM   1106  CA  ALA B  30      -9.880  46.574  69.943  1.00 10.60           C  
ANISOU 1106  CA  ALA B  30     1526   1084   1417    417     12   -247       C  
ATOM   1107  C   ALA B  30      -9.992  47.259  71.304  1.00  9.99           C  
ANISOU 1107  C   ALA B  30     1331   1118   1347    698    300   -246       C  
ATOM   1108  O   ALA B  30     -11.102  47.449  71.791  1.00 10.75           O  
ANISOU 1108  O   ALA B  30     1501   1166   1417    457    -41    -41       O  
ATOM   1109  CB  ALA B  30      -9.575  45.103  70.080  1.00 12.01           C  
ANISOU 1109  CB  ALA B  30     2418    969   1179     43     30   -173       C  
ATOM   1110  N   GLN B  31      -8.839  47.564  71.898  1.00 12.06           N  
ANISOU 1110  N   GLN B  31     1465   1740   1378    282   -293    -75       N  
ATOM   1111  CA  GLN B  31      -8.854  48.279  73.205  1.00 13.80           C  
ANISOU 1111  CA  GLN B  31     2346   1647   1250     39   -364   -563       C  
ATOM   1112  C   GLN B  31      -9.632  49.571  73.119  1.00 15.25           C  
ANISOU 1112  C   GLN B  31     2524   1617   1652    120   -393   -438       C  
ATOM   1113  O   GLN B  31     -10.378  49.898  74.075  1.00 14.98           O  
ANISOU 1113  O   GLN B  31     2167   1611   1915    324   -149   -147       O  
ATOM   1114  CB  GLN B  31      -7.408  48.533  73.650  1.00 15.71           C  
ANISOU 1114  CB  GLN B  31     2392   1985   1592   -225   -569   -414       C  
ATOM   1115  CG  GLN B  31      -6.703  47.239  74.075  1.00 19.09           C  
ANISOU 1115  CG  GLN B  31     2063   2061   3131    182   -768     75       C  
ATOM   1116  CD  GLN B  31      -5.237  47.430  74.382  1.00 23.68           C  
ANISOU 1116  CD  GLN B  31     1751   2440   4807    319  -1212    962       C  
ATOM   1117  OE1 GLN B  31      -4.625  48.413  73.952  1.00 32.43           O  
ANISOU 1117  OE1 GLN B  31     3355   2784   6182  -1141  -1547   -102       O  
ATOM   1118  NE2 GLN B  31      -4.632  46.458  75.020  1.00 24.68           N  
ANISOU 1118  NE2 GLN B  31     1442   2793   5144    517   -527    558       N  
ATOM   1119  N   ALA B  32      -9.521  50.304  72.018  1.00 15.41           N  
ANISOU 1119  N   ALA B  32     2517   1522   1817     40   -292   -362       N  
ATOM   1120  CA  ALA B  32     -10.247  51.573  71.874  1.00 17.15           C  
ANISOU 1120  CA  ALA B  32     2867   1433   2217    -43    -75   -606       C  
ATOM   1121  C   ALA B  32     -11.754  51.402  71.843  1.00 15.58           C  
ANISOU 1121  C   ALA B  32     2525   1562   1834    348    281   -757       C  
ATOM   1122  O   ALA B  32     -12.487  52.380  72.154  1.00 17.31           O  
ANISOU 1122  O   ALA B  32     2823   1483   2271    203    666   -262       O  
ATOM   1123  CB  ALA B  32      -9.781  52.332  70.641  1.00 16.66           C  
ANISOU 1123  CB  ALA B  32     2625   1354   2352    138    601    108       C  
ATOM   1124  N   LEU B  33     -12.234  50.240  71.458  1.00 14.55           N  
ANISOU 1124  N   LEU B  33     2105   1546   1879    497   -250   -693       N  
ATOM   1125  CA  LEU B  33     -13.636  49.910  71.391  1.00 15.35           C  
ANISOU 1125  CA  LEU B  33     1943   1998   1892    561   -302   -452       C  
ATOM   1126  C   LEU B  33     -14.223  49.478  72.701  1.00 14.89           C  
ANISOU 1126  C   LEU B  33     1741   1982   1933    646      5   -298       C  
ATOM   1127  O   LEU B  33     -15.420  49.232  72.823  1.00 19.83           O  
ANISOU 1127  O   LEU B  33     1409   4255   1869    353    -76   -402       O  
ATOM   1128  CB  LEU B  33     -13.966  48.909  70.277  1.00 16.17           C  
ANISOU 1128  CB  LEU B  33     1898   2333   1912    352   -369     -7       C  
ATOM   1129  CG  LEU B  33     -13.662  49.353  68.860  1.00 17.79           C  
ANISOU 1129  CG  LEU B  33     2401   2467   1892    319   -314   -101       C  
ATOM   1130  CD1 LEU B  33     -13.847  48.199  67.873  1.00 18.55           C  
ANISOU 1130  CD1 LEU B  33     2702   2456   1892    593     23   -408       C  
ATOM   1131  CD2 LEU B  33     -14.561  50.527  68.461  1.00 19.09           C  
ANISOU 1131  CD2 LEU B  33     2867   2363   2026    420   -737    289       C  
ATOM   1132  N   GLY B  34     -13.360  49.147  73.674  1.00 13.96           N  
ANISOU 1132  N   GLY B  34     2181   1146   1978    699   -165    180       N  
ATOM   1133  CA  GLY B  34     -13.819  48.648  74.925  1.00 13.65           C  
ANISOU 1133  CA  GLY B  34     1856   1242   2087    377   -345    203       C  
ATOM   1134  C   GLY B  34     -13.505  47.193  75.175  1.00 11.49           C  
ANISOU 1134  C   GLY B  34     1393   1274   1698    305   -290      6       C  
ATOM   1135  O   GLY B  34     -14.035  46.620  76.131  1.00 13.15           O  
ANISOU 1135  O   GLY B  34     2056   1647   1295    354    -34   -154       O  
ATOM   1136  N   TRP B  35     -12.679  46.557  74.357  1.00 11.68           N  
ANISOU 1136  N   TRP B  35     1784   1229   1424    578   -206   -328       N  
ATOM   1137  CA  TRP B  35     -12.256  45.173  74.635  1.00 11.01           C  
ANISOU 1137  CA  TRP B  35     1761   1210   1212    418     90   -571       C  
ATOM   1138  C   TRP B  35     -11.392  45.159  75.921  1.00 11.03           C  
ANISOU 1138  C   TRP B  35     1693   1239   1259    145   -399   -250       C  
ATOM   1139  O   TRP B  35     -10.448  45.942  76.037  1.00 13.00           O  
ANISOU 1139  O   TRP B  35     1659   1464   1819      4   -482   -209       O  
ATOM   1140  CB  TRP B  35     -11.342  44.708  73.489  1.00 11.33           C  
ANISOU 1140  CB  TRP B  35     1769   1263   1274    646   -388   -307       C  
ATOM   1141  CG  TRP B  35     -10.756  43.332  73.697  1.00 10.58           C  
ANISOU 1141  CG  TRP B  35     1799   1194   1028    572   -141   -130       C  
ATOM   1142  CD1 TRP B  35     -11.407  42.196  74.049  1.00 12.08           C  
ANISOU 1142  CD1 TRP B  35     1819   1334   1435    380   -129   -208       C  
ATOM   1143  CD2 TRP B  35      -9.372  42.978  73.579  1.00 10.94           C  
ANISOU 1143  CD2 TRP B  35     1849   1192   1117    416   -165   -323       C  
ATOM   1144  NE1 TRP B  35     -10.535  41.137  74.155  1.00 12.32           N  
ANISOU 1144  NE1 TRP B  35     2245   1115   1323    177    425    -65       N  
ATOM   1145  CE2 TRP B  35      -9.275  41.590  73.838  1.00 10.48           C  
ANISOU 1145  CE2 TRP B  35     1787   1222    971    680     84   -188       C  
ATOM   1146  CE3 TRP B  35      -8.213  43.678  73.240  1.00 13.02           C  
ANISOU 1146  CE3 TRP B  35     1909   1436   1601    309    116   -210       C  
ATOM   1147  CZ2 TRP B  35      -8.063  40.910  73.787  1.00 12.26           C  
ANISOU 1147  CZ2 TRP B  35     2055   1147   1456    438    350    -70       C  
ATOM   1148  CZ3 TRP B  35      -7.007  42.978  73.173  1.00 13.66           C  
ANISOU 1148  CZ3 TRP B  35     1922   1508   1760     68    -38   -123       C  
ATOM   1149  CH2 TRP B  35      -6.957  41.619  73.441  1.00 13.07           C  
ANISOU 1149  CH2 TRP B  35     1782   1539   1644    494    -39    143       C  
ATOM   1150  N   VAL B  36     -11.722  44.268  76.806  1.00 10.19           N  
ANISOU 1150  N   VAL B  36     1381   1296   1197    270   -320     27       N  
ATOM   1151  CA  VAL B  36     -10.987  43.983  78.034  1.00 11.15           C  
ANISOU 1151  CA  VAL B  36     1648   1512   1076    309   -354     88       C  
ATOM   1152  C   VAL B  36     -10.527  42.509  77.997  1.00 10.82           C  
ANISOU 1152  C   VAL B  36     1568   1407   1136    143   -105     -6       C  
ATOM   1153  O   VAL B  36     -11.325  41.598  78.097  1.00 10.72           O  
ANISOU 1153  O   VAL B  36     1307   1608   1157    200    -69    -54       O  
ATOM   1154  CB  VAL B  36     -11.837  44.235  79.284  1.00 11.19           C  
ANISOU 1154  CB  VAL B  36     1514   1579   1159    480   -147   -129       C  
ATOM   1155  CG1 VAL B  36     -11.024  43.978  80.549  1.00 13.16           C  
ANISOU 1155  CG1 VAL B  36     2116   1902    983    441   -375   -813       C  
ATOM   1156  CG2 VAL B  36     -12.479  45.579  79.268  1.00 13.74           C  
ANISOU 1156  CG2 VAL B  36     2197   1527   1496    519   -562   -250       C  
ATOM   1157  N   ALA B  37      -9.216  42.354  77.752  1.00 11.33           N  
ANISOU 1157  N   ALA B  37     1567   1416   1321     88   -314     37       N  
ATOM   1158  CA  ALA B  37      -8.673  41.014  77.552  1.00 10.23           C  
ANISOU 1158  CA  ALA B  37     1407   1509    973    214    -20    -38       C  
ATOM   1159  C   ALA B  37      -9.083  40.081  78.666  1.00  9.59           C  
ANISOU 1159  C   ALA B  37     1238   1447    960    435    -49    -81       C  
ATOM   1160  O   ALA B  37      -9.408  38.907  78.455  1.00 11.78           O  
ANISOU 1160  O   ALA B  37     1911   1477   1086     89     33    207       O  
ATOM   1161  CB  ALA B  37      -7.189  41.043  77.319  1.00 11.92           C  
ANISOU 1161  CB  ALA B  37     1284   1674   1572    256    315   -184       C  
ATOM   1162  N   SER B  38      -9.001  40.568  79.904  1.00 10.41           N  
ANISOU 1162  N   SER B  38     1336   1662    958    397    -99     44       N  
ATOM   1163  CA  SER B  38      -9.278  39.770  81.076  1.00 11.18           C  
ANISOU 1163  CA  SER B  38     1458   1818    974    250   -208     -4       C  
ATOM   1164  C   SER B  38     -10.725  39.355  81.231  1.00 12.08           C  
ANISOU 1164  C   SER B  38     1666   1580   1343     47     82    137       C  
ATOM   1165  O   SER B  38     -11.009  38.459  82.039  1.00 13.69           O  
ANISOU 1165  O   SER B  38     2094   1669   1438     16    -49    586       O  
ATOM   1166  CB ASER B  38      -8.761  40.456  82.344  0.50 11.57           C  
ANISOU 1166  CB ASER B  38     1471   1964    963    223   -346    -16       C  
ATOM   1167  CB BSER B  38      -8.783  40.463  82.351  0.50 11.42           C  
ANISOU 1167  CB BSER B  38     1471   1908    962    255   -332    -22       C  
ATOM   1168  OG ASER B  38      -7.352  40.674  82.319  0.50 11.96           O  
ANISOU 1168  OG ASER B  38     1528   2388    630    -25   -632   -329       O  
ATOM   1169  OG BSER B  38      -9.563  41.614  82.590  0.50 15.37           O  
ANISOU 1169  OG BSER B  38     2638   1655   1545    679    235    -39       O  
ATOM   1170  N   LYS B  39     -11.671  39.938  80.475  1.00 12.21           N  
ANISOU 1170  N   LYS B  39     1444   1698   1495    148   -278     63       N  
ATOM   1171  CA  LYS B  39     -13.052  39.523  80.489  1.00 13.31           C  
ANISOU 1171  CA  LYS B  39     1453   2312   1294    -64     58   -141       C  
ATOM   1172  C   LYS B  39     -13.416  38.610  79.336  1.00 13.64           C  
ANISOU 1172  C   LYS B  39     1545   2348   1288   -176   -218    317       C  
ATOM   1173  O   LYS B  39     -14.524  38.054  79.259  1.00 15.72           O  
ANISOU 1173  O   LYS B  39     1814   2675   1485   -495    221   -380       O  
ATOM   1174  CB  LYS B  39     -14.006  40.763  80.412  1.00 15.40           C  
ANISOU 1174  CB  LYS B  39     1181   2256   2415   -152     86  -1008       C  
ATOM   1175  CG  LYS B  39     -14.073  41.583  81.654  1.00 23.83           C  
ANISOU 1175  CG  LYS B  39     4721   1504   2829   -418   -273   -978       C  
ATOM   1176  CD  LYS B  39     -14.752  42.949  81.441  1.00 25.26           C  
ANISOU 1176  CD  LYS B  39     3922   1753   3923   -160     61   -984       C  
ATOM   1177  CE  LYS B  39     -16.222  42.838  81.775  1.00 29.36           C  
ANISOU 1177  CE  LYS B  39     4006   2323   4828   -688   -665   -443       C  
ATOM   1178  NZ  LYS B  39     -16.986  44.073  81.627  1.00 33.82           N  
ANISOU 1178  NZ  LYS B  39     2649   3096   7105    839   -296  -1990       N  
ATOM   1179  N   GLY B  40     -12.547  38.546  78.310  1.00 11.24           N  
ANISOU 1179  N   GLY B  40     1586   1197   1488     32    248    240       N  
ATOM   1180  CA  GLY B  40     -12.884  37.675  77.179  1.00 12.24           C  
ANISOU 1180  CA  GLY B  40     1604   1538   1509    -12    227    -36       C  
ATOM   1181  C   GLY B  40     -14.068  38.176  76.384  1.00 12.12           C  
ANISOU 1181  C   GLY B  40     1501   1645   1458     35    359    -71       C  
ATOM   1182  O   GLY B  40     -14.857  37.348  75.903  1.00 13.42           O  
ANISOU 1182  O   GLY B  40     1900   1700   1498   -297   -139   -172       O  
ATOM   1183  N   ASN B  41     -14.207  39.487  76.223  1.00 11.30           N  
ANISOU 1183  N   ASN B  41     1421   1624   1247    -47     60    221       N  
ATOM   1184  CA  ASN B  41     -15.390  40.117  75.704  1.00 11.24           C  
ANISOU 1184  CA  ASN B  41     1255   1791   1224    292   -196     10       C  
ATOM   1185  C   ASN B  41     -15.300  40.656  74.309  1.00 10.98           C  
ANISOU 1185  C   ASN B  41     1244   1682   1245    580   -373     21       C  
ATOM   1186  O   ASN B  41     -16.190  41.440  73.880  1.00 11.02           O  
ANISOU 1186  O   ASN B  41     1355   1669   1164    463   -311   -231       O  
ATOM   1187  CB  ASN B  41     -15.896  41.223  76.665  1.00 11.85           C  
ANISOU 1187  CB  ASN B  41     1393   1903   1206    517    -58   -443       C  
ATOM   1188  CG  ASN B  41     -15.022  42.452  76.623  1.00 12.33           C  
ANISOU 1188  CG  ASN B  41     1719   1824   1144    395   -434   -487       C  
ATOM   1189  OD1 ASN B  41     -13.916  42.416  76.096  1.00 13.80           O  
ANISOU 1189  OD1 ASN B  41     1569   1957   1719    314   -180   -300       O  
ATOM   1190  ND2 ASN B  41     -15.466  43.592  77.177  1.00 15.44           N  
ANISOU 1190  ND2 ASN B  41     1832   1784   2252    506   -294   -809       N  
ATOM   1191  N   LEU B  42     -14.314  40.218  73.519  1.00 11.00           N  
ANISOU 1191  N   LEU B  42     1228   1724   1229    536   -407   -587       N  
ATOM   1192  CA  LEU B  42     -14.191  40.772  72.170  1.00 11.64           C  
ANISOU 1192  CA  LEU B  42     1546   1748   1129    790   -111   -409       C  
ATOM   1193  C   LEU B  42     -15.464  40.679  71.370  1.00 12.22           C  
ANISOU 1193  C   LEU B  42     1511   1894   1237    611    -42   -187       C  
ATOM   1194  O   LEU B  42     -15.888  41.657  70.725  1.00 12.33           O  
ANISOU 1194  O   LEU B  42     1737   1912   1034    546     89     47       O  
ATOM   1195  CB  LEU B  42     -13.001  40.220  71.400  1.00 11.68           C  
ANISOU 1195  CB  LEU B  42     1506   1765   1166    684      1   -241       C  
ATOM   1196  CG  LEU B  42     -12.666  40.811  70.040  1.00 11.91           C  
ANISOU 1196  CG  LEU B  42     1735   1506   1285    131     58   -190       C  
ATOM   1197  CD1 LEU B  42     -12.271  42.278  70.116  1.00 17.11           C  
ANISOU 1197  CD1 LEU B  42     2699   1474   2330    -10    659   -215       C  
ATOM   1198  CD2 LEU B  42     -11.535  40.013  69.376  1.00 12.42           C  
ANISOU 1198  CD2 LEU B  42     1640   1696   1381   -148    843   -351       C  
ATOM   1199  N   ALA B  43     -16.096  39.493  71.337  1.00 13.34           N  
ANISOU 1199  N   ALA B  43     1863   1813   1391    526   -267   -456       N  
ATOM   1200  CA  ALA B  43     -17.269  39.312  70.493  1.00 14.98           C  
ANISOU 1200  CA  ALA B  43     1829   2245   1620    242  -1066   -414       C  
ATOM   1201  C   ALA B  43     -18.475  40.111  70.950  1.00 15.34           C  
ANISOU 1201  C   ALA B  43     1680   2264   1883    324  -1005   -200       C  
ATOM   1202  O   ALA B  43     -19.415  40.352  70.188  1.00 15.94           O  
ANISOU 1202  O   ALA B  43     1599   2727   1732    593   -541    -86       O  
ATOM   1203  CB  ALA B  43     -17.628  37.816  70.422  1.00 17.70           C  
ANISOU 1203  CB  ALA B  43     1473   2224   3027    366   -976   -686       C  
ATOM   1204  N   ASP B  44     -18.517  40.534  72.210  1.00 13.88           N  
ANISOU 1204  N   ASP B  44     1127   2220   1927    133   -863   -205       N  
ATOM   1205  CA  ASP B  44     -19.613  41.379  72.680  1.00 13.88           C  
ANISOU 1205  CA  ASP B  44     1059   2419   1798    546    -18   -241       C  
ATOM   1206  C   ASP B  44     -19.420  42.834  72.246  1.00 14.32           C  
ANISOU 1206  C   ASP B  44     1286   2338   1815    725    227   -559       C  
ATOM   1207  O   ASP B  44     -20.389  43.538  71.926  1.00 15.84           O  
ANISOU 1207  O   ASP B  44     1241   2314   2461    478      5   -454       O  
ATOM   1208  CB  ASP B  44     -19.613  41.334  74.213  1.00 16.67           C  
ANISOU 1208  CB  ASP B  44     1834   2785   1716    576    184     11       C  
ATOM   1209  CG  ASP B  44     -20.052  40.001  74.775  1.00 25.69           C  
ANISOU 1209  CG  ASP B  44     5069   2861   1830   -696   -199    640       C  
ATOM   1210  OD1 ASP B  44     -20.861  39.292  74.157  1.00 29.14           O  
ANISOU 1210  OD1 ASP B  44     4256   3528   3287  -1011    349     17       O  
ATOM   1211  OD2 ASP B  44     -19.693  39.773  75.946  1.00 38.96           O  
ANISOU 1211  OD2 ASP B  44     9737   3661   1405  -2106   -763    639       O  
ATOM   1212  N   VAL B  45     -18.166  43.286  72.275  1.00 12.02           N  
ANISOU 1212  N   VAL B  45     1265   1812   1489    951   -539   -145       N  
ATOM   1213  CA  VAL B  45     -17.867  44.669  71.947  1.00 13.14           C  
ANISOU 1213  CA  VAL B  45     1495   1798   1701    853  -1098   -384       C  
ATOM   1214  C   VAL B  45     -17.793  44.915  70.452  1.00 12.87           C  
ANISOU 1214  C   VAL B  45     1540   1645   1704    938  -1187    -17       C  
ATOM   1215  O   VAL B  45     -18.260  45.950  69.971  1.00 12.96           O  
ANISOU 1215  O   VAL B  45     1505   1720   1702    901     25    -33       O  
ATOM   1216  CB  VAL B  45     -16.627  45.191  72.662  1.00 16.56           C  
ANISOU 1216  CB  VAL B  45     1853   2719   1721    216   -543     13       C  
ATOM   1217  CG1 VAL B  45     -16.763  45.098  74.169  1.00 18.93           C  
ANISOU 1217  CG1 VAL B  45     2957   2532   1702     70    -35    146       C  
ATOM   1218  CG2 VAL B  45     -15.335  44.673  72.134  1.00 18.98           C  
ANISOU 1218  CG2 VAL B  45     1590   3162   2461    -19   -602    312       C  
ATOM   1219  N   ALA B  46     -17.269  43.944  69.707  1.00 13.88           N  
ANISOU 1219  N   ALA B  46     2165   1474   1635    511   -306   -673       N  
ATOM   1220  CA  ALA B  46     -17.096  44.079  68.256  1.00 13.19           C  
ANISOU 1220  CA  ALA B  46     1675   1658   1678    537   -247   -573       C  
ATOM   1221  C   ALA B  46     -17.493  42.774  67.563  1.00 12.11           C  
ANISOU 1221  C   ALA B  46     1278   1773   1548    561   -362   -534       C  
ATOM   1222  O   ALA B  46     -16.641  41.972  67.166  1.00 12.06           O  
ANISOU 1222  O   ALA B  46     1377   1664   1540    444    -54   -300       O  
ATOM   1223  CB  ALA B  46     -15.638  44.432  67.941  1.00 16.34           C  
ANISOU 1223  CB  ALA B  46     2292   1800   2117   -241   -259   -298       C  
ATOM   1224  N   PRO B  47     -18.792  42.506  67.519  1.00 13.09           N  
ANISOU 1224  N   PRO B  47     1022   2407   1544    593   -415   -315       N  
ATOM   1225  CA  PRO B  47     -19.258  41.228  66.927  1.00 15.23           C  
ANISOU 1225  CA  PRO B  47     1562   2626   1599    112   -377   -462       C  
ATOM   1226  C   PRO B  47     -18.639  41.014  65.557  1.00 15.14           C  
ANISOU 1226  C   PRO B  47     1710   2470   1571    239    -63   -748       C  
ATOM   1227  O   PRO B  47     -18.550  41.938  64.731  1.00 16.80           O  
ANISOU 1227  O   PRO B  47     2436   2564   1382    815   -354   -574       O  
ATOM   1228  CB  PRO B  47     -20.767  41.385  66.853  1.00 16.62           C  
ANISOU 1228  CB  PRO B  47     1581   2883   1851    -92    -14  -1025       C  
ATOM   1229  CG  PRO B  47     -21.115  42.555  67.677  1.00 15.71           C  
ANISOU 1229  CG  PRO B  47     1111   3011   1848    151    -56   -933       C  
ATOM   1230  CD  PRO B  47     -19.910  43.331  67.990  1.00 13.47           C  
ANISOU 1230  CD  PRO B  47      872   2680   1566    444     80   -325       C  
ATOM   1231  N   GLY B  48     -18.194  39.793  65.329  1.00 15.23           N  
ANISOU 1231  N   GLY B  48     1362   2501   1925    350    308  -1025       N  
ATOM   1232  CA  GLY B  48     -17.619  39.316  64.125  1.00 15.75           C  
ANISOU 1232  CA  GLY B  48     1678   2315   1992    159    448  -1004       C  
ATOM   1233  C   GLY B  48     -16.173  39.600  63.881  1.00 15.48           C  
ANISOU 1233  C   GLY B  48     1860   2600   1421   -165    619   -749       C  
ATOM   1234  O   GLY B  48     -15.625  39.286  62.822  1.00 15.78           O  
ANISOU 1234  O   GLY B  48     1724   2873   1399    524    -99   -919       O  
ATOM   1235  N   LYS B  49     -15.520  40.344  64.787  1.00 13.19           N  
ANISOU 1235  N   LYS B  49     1391   2066   1553    423   -183   -602       N  
ATOM   1236  CA  LYS B  49     -14.134  40.716  64.606  1.00 12.40           C  
ANISOU 1236  CA  LYS B  49     1291   1887   1531    517     96     50       C  
ATOM   1237  C   LYS B  49     -13.177  39.730  65.284  1.00 12.15           C  
ANISOU 1237  C   LYS B  49     1481   1735   1402    283    291   -514       C  
ATOM   1238  O   LYS B  49     -13.557  39.114  66.286  1.00 13.13           O  
ANISOU 1238  O   LYS B  49     1495   2109   1384    326     34   -147       O  
ATOM   1239  CB  LYS B  49     -13.900  42.126  65.172  1.00 14.59           C  
ANISOU 1239  CB  LYS B  49     1265   1810   2468    656    140   -352       C  
ATOM   1240  CG  LYS B  49     -14.625  43.227  64.400  1.00 16.64           C  
ANISOU 1240  CG  LYS B  49     2112   1902   2308   1204   -116   -512       C  
ATOM   1241  CD  LYS B  49     -14.333  43.224  62.941  1.00 25.07           C  
ANISOU 1241  CD  LYS B  49     4484   2928   2114    399    251    443       C  
ATOM   1242  CE  LYS B  49     -14.835  44.460  62.215  1.00 24.58           C  
ANISOU 1242  CE  LYS B  49     4260   3066   2015    714    376    142       C  
ATOM   1243  NZ  LYS B  49     -16.229  44.765  62.563  1.00 30.77           N  
ANISOU 1243  NZ  LYS B  49     3933   3411   4348    770   -942   -398       N  
ATOM   1244  N   SER B  50     -11.958  39.620  64.790  1.00 11.22           N  
ANISOU 1244  N   SER B  50     1443   1640   1181    587    -59   -332       N  
ATOM   1245  CA  SER B  50     -10.884  38.901  65.419  1.00 11.25           C  
ANISOU 1245  CA  SER B  50     1268   1762   1244    392    244   -304       C  
ATOM   1246  C   SER B  50      -9.653  39.850  65.563  1.00 12.05           C  
ANISOU 1246  C   SER B  50     1629   1550   1399    180    726   -239       C  
ATOM   1247  O   SER B  50      -9.517  40.772  64.757  1.00 12.70           O  
ANISOU 1247  O   SER B  50     1782   1762   1282     74    267   -192       O  
ATOM   1248  CB  SER B  50     -10.425  37.711  64.531  1.00 12.39           C  
ANISOU 1248  CB  SER B  50     1528   1515   1665    332    -84   -154       C  
ATOM   1249  OG  SER B  50     -11.442  36.700  64.477  1.00 13.02           O  
ANISOU 1249  OG  SER B  50     1551   1729   1667    209   -113   -261       O  
ATOM   1250  N   ILE B  51      -8.753  39.554  66.479  1.00 11.41           N  
ANISOU 1250  N   ILE B  51     1409   1217   1708    191    342    158       N  
ATOM   1251  CA  ILE B  51      -7.518  40.334  66.610  1.00 11.26           C  
ANISOU 1251  CA  ILE B  51     1450   1325   1502    212    374    -71       C  
ATOM   1252  C   ILE B  51      -6.500  39.875  65.557  1.00 10.35           C  
ANISOU 1252  C   ILE B  51     1305   1297   1332    334     17    230       C  
ATOM   1253  O   ILE B  51      -6.267  38.651  65.412  1.00 11.16           O  
ANISOU 1253  O   ILE B  51     1634   1332   1275    317    276      2       O  
ATOM   1254  CB  ILE B  51      -6.872  40.099  68.001  1.00 13.85           C  
ANISOU 1254  CB  ILE B  51     1989   1977   1299   -414    749   -354       C  
ATOM   1255  CG1 ILE B  51      -7.776  40.450  69.163  1.00 13.90           C  
ANISOU 1255  CG1 ILE B  51     1775   1903   1602   -376     17   -131       C  
ATOM   1256  CG2 ILE B  51      -5.537  40.786  68.102  1.00 12.50           C  
ANISOU 1256  CG2 ILE B  51     1636   1832   1283    -41    382   -215       C  
ATOM   1257  CD1 ILE B  51      -8.097  41.879  69.282  1.00 16.39           C  
ANISOU 1257  CD1 ILE B  51     1315   1929   2985    198    173   -421       C  
ATOM   1258  N   GLY B  52      -5.880  40.826  64.879  1.00 12.15           N  
ANISOU 1258  N   GLY B  52     1855   1467   1293   -111    779    174       N  
ATOM   1259  CA  GLY B  52      -4.772  40.513  63.976  1.00 12.14           C  
ANISOU 1259  CA  GLY B  52     1951   1460   1202   -221    791    -57       C  
ATOM   1260  C   GLY B  52      -4.152  41.747  63.355  1.00 12.00           C  
ANISOU 1260  C   GLY B  52     1971   1376   1212   -100    546    157       C  
ATOM   1261  O   GLY B  52      -4.760  42.846  63.312  1.00 14.41           O  
ANISOU 1261  O   GLY B  52     2221   1471   1781    310    786     74       O  
ATOM   1262  N   GLY B  53      -2.920  41.608  62.880  1.00 13.03           N  
ANISOU 1262  N   GLY B  53     1727   1783   1441   -180    657   -208       N  
ATOM   1263  CA  GLY B  53      -2.184  42.632  62.211  1.00 13.20           C  
ANISOU 1263  CA  GLY B  53     1575   1276   2163    135    808     -2       C  
ATOM   1264  C   GLY B  53      -1.071  43.284  62.984  1.00 15.38           C  
ANISOU 1264  C   GLY B  53     1892   1714   2237   -305    678   -152       C  
ATOM   1265  O   GLY B  53      -0.304  44.120  62.450  1.00 17.73           O  
ANISOU 1265  O   GLY B  53     2607   1875   2253   -743    853   -405       O  
ATOM   1266  N   ASP B  54      -0.883  42.922  64.260  1.00 14.33           N  
ANISOU 1266  N   ASP B  54     1552   1624   2270     53    141   -289       N  
ATOM   1267  CA  ASP B  54       0.197  43.505  65.045  1.00 15.66           C  
ANISOU 1267  CA  ASP B  54     1463   2197   2291     50    400   -440       C  
ATOM   1268  C   ASP B  54       1.538  42.887  64.654  1.00 16.08           C  
ANISOU 1268  C   ASP B  54     1704   2047   2359   -397    467   -535       C  
ATOM   1269  O   ASP B  54       1.654  41.732  64.249  1.00 15.64           O  
ANISOU 1269  O   ASP B  54     1793   2066   2082    -51    775   -726       O  
ATOM   1270  CB  ASP B  54      -0.070  43.344  66.531  1.00 16.16           C  
ANISOU 1270  CB  ASP B  54     1376   2500   2263    332    578   -571       C  
ATOM   1271  CG  ASP B  54      -1.244  44.146  67.029  1.00 16.24           C  
ANISOU 1271  CG  ASP B  54     1996   1860   2316    -98   1286   -633       C  
ATOM   1272  OD1 ASP B  54      -1.144  45.394  67.028  1.00 25.06           O  
ANISOU 1272  OD1 ASP B  54     3713   1914   3895   -260   1342   -795       O  
ATOM   1273  OD2 ASP B  54      -2.299  43.527  67.341  1.00 18.11           O  
ANISOU 1273  OD2 ASP B  54     1543   2657   2681     33    783   -152       O  
ATOM   1274  N   ILE B  55       2.608  43.649  64.854  1.00 19.30           N  
ANISOU 1274  N   ILE B  55     1883   2434   3018   -723   1272  -1219       N  
ATOM   1275  CA  ILE B  55       3.963  43.154  64.686  1.00 19.79           C  
ANISOU 1275  CA  ILE B  55     1402   2875   3243   -264   1041  -1018       C  
ATOM   1276  C   ILE B  55       4.303  42.087  65.714  1.00 19.96           C  
ANISOU 1276  C   ILE B  55     1462   2864   3258   -222    541   -801       C  
ATOM   1277  O   ILE B  55       3.940  42.177  66.888  1.00 21.19           O  
ANISOU 1277  O   ILE B  55     1800   3028   3223    135    224   -985       O  
ATOM   1278  CB  ILE B  55       4.987  44.330  64.785  1.00 21.63           C  
ANISOU 1278  CB  ILE B  55     1563   2903   3752   -364   1226  -1134       C  
ATOM   1279  CG1 ILE B  55       4.915  45.179  63.498  1.00 24.60           C  
ANISOU 1279  CG1 ILE B  55     2621   2979   3749   -935   1219   -199       C  
ATOM   1280  CG2 ILE B  55       6.396  43.742  64.923  1.00 24.67           C  
ANISOU 1280  CG2 ILE B  55     1399   3247   4728   -438   1344  -1078       C  
ATOM   1281  CD1 ILE B  55       5.630  46.485  63.537  1.00 30.76           C  
ANISOU 1281  CD1 ILE B  55     4297   1893   5496   -291    -83    315       C  
ATOM   1282  N   PHE B  56       4.948  41.027  65.274  1.00 20.75           N  
ANISOU 1282  N   PHE B  56     1813   2836   3236    -44    433   -957       N  
ATOM   1283  CA  PHE B  56       5.448  39.977  66.144  1.00 21.39           C  
ANISOU 1283  CA  PHE B  56     1939   2842   3346    211    281  -1401       C  
ATOM   1284  C   PHE B  56       6.992  40.029  66.151  1.00 21.12           C  
ANISOU 1284  C   PHE B  56     1508   3229   3289    616   -153  -1627       C  
ATOM   1285  O   PHE B  56       7.626  39.909  65.108  1.00 21.97           O  
ANISOU 1285  O   PHE B  56     1658   3392   3296    201    398  -1030       O  
ATOM   1286  CB  PHE B  56       4.985  38.610  65.630  1.00 23.00           C  
ANISOU 1286  CB  PHE B  56     2447   2795   3497    -57     86  -1067       C  
ATOM   1287  CG  PHE B  56       5.440  37.453  66.504  1.00 22.24           C  
ANISOU 1287  CG  PHE B  56     2024   2858   3568      7     37   -898       C  
ATOM   1288  CD1 PHE B  56       4.780  37.166  67.684  1.00 23.09           C  
ANISOU 1288  CD1 PHE B  56     2368   2869   3536   -259   -747   -126       C  
ATOM   1289  CD2 PHE B  56       6.522  36.672  66.129  1.00 23.07           C  
ANISOU 1289  CD2 PHE B  56     2076   2855   3837     34   -482   -719       C  
ATOM   1290  CE1 PHE B  56       5.154  36.079  68.456  1.00 23.41           C  
ANISOU 1290  CE1 PHE B  56     2406   2967   3521   -128   -474     69       C  
ATOM   1291  CE2 PHE B  56       6.887  35.577  66.885  1.00 23.37           C  
ANISOU 1291  CE2 PHE B  56     2200   2801   3880      3   -258   -580       C  
ATOM   1292  CZ  PHE B  56       6.192  35.268  68.046  1.00 24.00           C  
ANISOU 1292  CZ  PHE B  56     2363   2974   3783     89   -310   -125       C  
ATOM   1293  N   SER B  57       7.553  40.306  67.314  1.00 25.76           N  
ANISOU 1293  N   SER B  57     2110   4398   3281   -259    123  -1708       N  
ATOM   1294  CA  SER B  57       8.942  40.589  67.494  1.00 26.35           C  
ANISOU 1294  CA  SER B  57     1974   4800   3239   -214   -510  -1564       C  
ATOM   1295  C   SER B  57       9.925  39.570  67.049  1.00 26.96           C  
ANISOU 1295  C   SER B  57     1862   4786   3594     40   -120  -1610       C  
ATOM   1296  O   SER B  57      11.058  39.922  66.605  1.00 31.88           O  
ANISOU 1296  O   SER B  57     1709   4653   5751    -24    295  -1589       O  
ATOM   1297  CB  SER B  57       9.258  41.205  68.839  1.00 27.91           C  
ANISOU 1297  CB  SER B  57     2414   5025   3167   -406   -659  -1093       C  
ATOM   1298  OG  SER B  57       9.639  40.231  69.791  1.00 36.83           O  
ANISOU 1298  OG  SER B  57     6209   4942   2841    151    149   -550       O  
ATOM   1299  N   ASN B  58       9.654  38.282  67.199  1.00 28.85           N  
ANISOU 1299  N   ASN B  58     2919   4727   3316   -355   -338  -1056       N  
ATOM   1300  CA  ASN B  58      10.552  37.220  66.861  1.00 29.34           C  
ANISOU 1300  CA  ASN B  58     2898   4777   3475    167   -356  -1181       C  
ATOM   1301  C   ASN B  58      11.805  37.139  67.680  1.00 29.73           C  
ANISOU 1301  C   ASN B  58     2779   4989   3527    239   -201  -1353       C  
ATOM   1302  O   ASN B  58      12.834  36.598  67.291  1.00 31.22           O  
ANISOU 1302  O   ASN B  58     2354   5408   4102    585     54  -1371       O  
ATOM   1303  CB  ASN B  58      10.748  37.000  65.386  1.00 28.88           C  
ANISOU 1303  CB  ASN B  58     2821   4642   3512    228    -33  -1625       C  
ATOM   1304  CG  ASN B  58      11.341  35.653  65.034  1.00 28.00           C  
ANISOU 1304  CG  ASN B  58     2427   4678   3532     67    127  -1224       C  
ATOM   1305  OD1 ASN B  58      10.975  34.631  65.621  1.00 27.69           O  
ANISOU 1305  OD1 ASN B  58     2937   4669   2914    305    472  -1050       O  
ATOM   1306  ND2 ASN B  58      12.252  35.646  64.073  1.00 28.28           N  
ANISOU 1306  ND2 ASN B  58     2187   4907   3650    -41    -59     -5       N  
ATOM   1307  N   ARG B  59      11.736  37.619  68.946  1.00 32.58           N  
ANISOU 1307  N   ARG B  59     3339   5621   3417   -106  -1041  -1434       N  
ATOM   1308  CA  ARG B  59      12.858  37.550  69.851  0.50 32.41           C  
ANISOU 1308  CA  ARG B  59     3162   5692   3461    153  -1418  -1122       C  
ATOM   1309  C   ARG B  59      13.355  36.148  70.134  1.00 33.66           C  
ANISOU 1309  C   ARG B  59     2940   5791   4058    730  -1284   -798       C  
ATOM   1310  O   ARG B  59      14.561  35.922  70.290  1.00 34.10           O  
ANISOU 1310  O   ARG B  59     2677   6119   4161   1028   -452   -266       O  
ATOM   1311  CB  ARG B  59      12.577  38.300  71.162  0.50 31.73           C  
ANISOU 1311  CB  ARG B  59     2876   5728   3454    -36  -1556  -1132       C  
ATOM   1312  CG  ARG B  59      13.396  39.568  71.330  0.00 31.78           C  
ANISOU 1312  CG  ARG B  59     2827   5739   3509    -22  -1558  -1131       C  
ATOM   1313  CD  ARG B  59      12.619  40.793  70.873  0.00 31.79           C  
ANISOU 1313  CD  ARG B  59     2840   5727   3510    -47  -1559  -1129       C  
ATOM   1314  NE  ARG B  59      11.575  41.164  71.824  0.00 31.80           N  
ANISOU 1314  NE  ARG B  59     2853   5720   3511    -64  -1560  -1129       N  
ATOM   1315  CZ  ARG B  59      10.870  42.286  71.763  0.00 31.81           C  
ANISOU 1315  CZ  ARG B  59     2854   5718   3512    -75  -1561  -1128       C  
ATOM   1316  NH1 ARG B  59      11.279  43.290  70.998  0.00 31.79           N  
ANISOU 1316  NH1 ARG B  59     2848   5718   3514    -77  -1561  -1128       N  
ATOM   1317  NH2 ARG B  59       9.753  42.411  72.467  0.00 31.82           N  
ANISOU 1317  NH2 ARG B  59     2860   5712   3518    -88  -1561  -1128       N  
ATOM   1318  N   GLU B  60      12.456  35.176  70.268  1.00 33.82           N  
ANISOU 1318  N   GLU B  60     3083   5599   4167    740  -1086   -793       N  
ATOM   1319  CA  GLU B  60      12.870  33.804  70.576  1.00 33.27           C  
ANISOU 1319  CA  GLU B  60     2866   5708   4065    952   -785  -1018       C  
ATOM   1320  C   GLU B  60      13.613  33.166  69.406  1.00 33.51           C  
ANISOU 1320  C   GLU B  60     2974   5727   4032   1184   -713   -496       C  
ATOM   1321  O   GLU B  60      14.238  32.106  69.568  1.00 34.72           O  
ANISOU 1321  O   GLU B  60     3567   5528   4099   1056   -709  -1379       O  
ATOM   1322  CB  GLU B  60      11.691  33.001  71.114  0.50 34.67           C  
ANISOU 1322  CB  GLU B  60     3252   5663   4259    633   -505  -1415       C  
ATOM   1323  CG  GLU B  60      11.578  32.960  72.656  0.50 35.48           C  
ANISOU 1323  CG  GLU B  60     3335   5889   4256    331   -450  -1858       C  
ATOM   1324  CD  GLU B  60      10.649  31.849  73.045  0.50 38.57           C  
ANISOU 1324  CD  GLU B  60     4056   6171   4429   -283   -283  -2163       C  
ATOM   1325  OE1 GLU B  60       9.440  31.844  72.590  0.50 44.09           O  
ANISOU 1325  OE1 GLU B  60     5999   6251   4503  -1661  -1543   -685       O  
ATOM   1326  OE2 GLU B  60      11.069  30.914  73.806  0.50 37.22           O  
ANISOU 1326  OE2 GLU B  60     3460   6193   4489     33    -21  -2638       O  
ATOM   1327  N   GLY B  61      13.532  33.778  68.238  1.00 34.02           N  
ANISOU 1327  N   GLY B  61     3295   5609   4024    958    -82   -559       N  
ATOM   1328  CA  GLY B  61      14.215  33.338  67.043  1.00 34.03           C  
ANISOU 1328  CA  GLY B  61     3120   5781   4029    812      4   -713       C  
ATOM   1329  C   GLY B  61      13.660  32.084  66.425  1.00 33.71           C  
ANISOU 1329  C   GLY B  61     3267   5977   3565    653    158   -773       C  
ATOM   1330  O   GLY B  61      14.349  31.421  65.622  1.00 32.97           O  
ANISOU 1330  O   GLY B  61     2841   5905   3780    -11   -187   -692       O  
ATOM   1331  N   LYS B  62      12.433  31.721  66.754  1.00 28.17           N  
ANISOU 1331  N   LYS B  62     2970   5066   2666   1242   -160   -251       N  
ATOM   1332  CA  LYS B  62      11.788  30.530  66.263  1.00 27.24           C  
ANISOU 1332  CA  LYS B  62     2967   4813   2570   1396    386   -286       C  
ATOM   1333  C   LYS B  62      11.363  30.582  64.800  1.00 27.28           C  
ANISOU 1333  C   LYS B  62     3557   4151   2657   1102    176   -600       C  
ATOM   1334  O   LYS B  62      11.112  29.526  64.200  1.00 29.68           O  
ANISOU 1334  O   LYS B  62     4694   4052   2533   1223   -356   -395       O  
ATOM   1335  CB  LYS B  62      10.617  30.141  67.150  1.00 31.97           C  
ANISOU 1335  CB  LYS B  62     3516   5929   2701    479    475    109       C  
ATOM   1336  CG  LYS B  62      11.024  29.775  68.590  1.00 36.84           C  
ANISOU 1336  CG  LYS B  62     4825   6664   2508   -462    217    589       C  
ATOM   1337  CD  LYS B  62       9.900  28.921  69.195  1.00 42.98           C  
ANISOU 1337  CD  LYS B  62     6025   7729   2577  -1726   -324    962       C  
ATOM   1338  CE  LYS B  62       9.801  29.076  70.685  1.00 45.42           C  
ANISOU 1338  CE  LYS B  62     6439   8266   2552  -2317   -221    671       C  
ATOM   1339  NZ  LYS B  62       9.834  27.750  71.396  1.00 50.23           N  
ANISOU 1339  NZ  LYS B  62     8288   8283   2515  -3710    799    506       N  
ATOM   1340  N   LEU B  63      11.208  31.766  64.248  1.00 24.10           N  
ANISOU 1340  N   LEU B  63     2218   4066   2872   1244    666   -714       N  
ATOM   1341  CA  LEU B  63      10.862  31.957  62.838  1.00 23.92           C  
ANISOU 1341  CA  LEU B  63     2204   3987   2896   1048    312   -578       C  
ATOM   1342  C   LEU B  63      12.098  32.434  62.085  1.00 23.94           C  
ANISOU 1342  C   LEU B  63     2114   4076   2906   1173    442   -821       C  
ATOM   1343  O   LEU B  63      12.987  33.039  62.695  1.00 27.39           O  
ANISOU 1343  O   LEU B  63     2180   5225   3001    664    618   -873       O  
ATOM   1344  CB  LEU B  63       9.736  32.989  62.712  1.00 23.34           C  
ANISOU 1344  CB  LEU B  63     2328   3934   2606    780    525   -368       C  
ATOM   1345  CG  LEU B  63       8.415  32.619  63.371  1.00 21.85           C  
ANISOU 1345  CG  LEU B  63     2483   3677   2142    762    935    -14       C  
ATOM   1346  CD1 LEU B  63       7.461  33.798  63.413  1.00 24.98           C  
ANISOU 1346  CD1 LEU B  63     2159   3918   3415   1108   1030    320       C  
ATOM   1347  CD2 LEU B  63       7.782  31.415  62.692  1.00 25.38           C  
ANISOU 1347  CD2 LEU B  63     3420   3916   2309     29    177     15       C  
ATOM   1348  N   PRO B  64      12.233  32.080  60.812  1.00 25.24           N  
ANISOU 1348  N   PRO B  64     2479   4254   2857   1147    635   -330       N  
ATOM   1349  CA  PRO B  64      13.437  32.439  60.073  1.00 24.87           C  
ANISOU 1349  CA  PRO B  64     2423   4197   2829   1274    536   -376       C  
ATOM   1350  C   PRO B  64      13.578  33.938  59.844  1.00 27.85           C  
ANISOU 1350  C   PRO B  64     2471   4217   3893    926    930   -265       C  
ATOM   1351  O   PRO B  64      12.658  34.619  59.427  1.00 27.67           O  
ANISOU 1351  O   PRO B  64     2670   4087   3756   1149    836    689       O  
ATOM   1352  CB  PRO B  64      13.270  31.715  58.737  1.00 26.29           C  
ANISOU 1352  CB  PRO B  64     2708   4477   2803    951    539   -522       C  
ATOM   1353  CG  PRO B  64      11.780  31.540  58.610  1.00 26.34           C  
ANISOU 1353  CG  PRO B  64     2682   4517   2811    956    758   -580       C  
ATOM   1354  CD  PRO B  64      11.302  31.272  60.014  1.00 24.55           C  
ANISOU 1354  CD  PRO B  64     2492   4038   2796   1299    754   -182       C  
ATOM   1355  N   GLY B  65      14.798  34.442  60.069  1.00 34.20           N  
ANISOU 1355  N   GLY B  65     2572   4947   5475    556    980   -431       N  
ATOM   1356  CA  GLY B  65      15.052  35.857  59.819  1.00 35.80           C  
ANISOU 1356  CA  GLY B  65     2791   4990   5822    279   1294   -649       C  
ATOM   1357  C   GLY B  65      15.728  36.048  58.454  1.00 38.16           C  
ANISOU 1357  C   GLY B  65     3786   5080   5633    -24   1437   -409       C  
ATOM   1358  O   GLY B  65      16.221  35.086  57.870  1.00 38.95           O  
ANISOU 1358  O   GLY B  65     4311   5195   5293    583   1481   -221       O  
ATOM   1359  N   LYS B  66      15.702  37.264  57.981  1.00 37.44           N  
ANISOU 1359  N   LYS B  66     3348   5098   5778     39   1695   -183       N  
ATOM   1360  CA  LYS B  66      16.273  37.699  56.724  1.00 36.36           C  
ANISOU 1360  CA  LYS B  66     3083   4897   5835    265   1982   -423       C  
ATOM   1361  C   LYS B  66      16.284  39.245  56.731  1.00 38.10           C  
ANISOU 1361  C   LYS B  66     3244   4901   6331    -24   2362   -350       C  
ATOM   1362  O   LYS B  66      15.367  39.834  57.318  1.00 39.67           O  
ANISOU 1362  O   LYS B  66     2899   4810   7363    123   1877     37       O  
ATOM   1363  CB  LYS B  66      15.401  37.229  55.539  1.00 39.84           C  
ANISOU 1363  CB  LYS B  66     4095   5282   5760   -482   2436   -609       C  
ATOM   1364  CG  LYS B  66      15.864  37.818  54.203  1.00 44.08           C  
ANISOU 1364  CG  LYS B  66     5045   5933   5770  -1334   2038   -399       C  
ATOM   1365  CD  LYS B  66      15.108  37.197  53.046  1.00 45.33           C  
ANISOU 1365  CD  LYS B  66     5309   6166   5750  -1563   2027   -517       C  
ATOM   1366  CE  LYS B  66      15.988  36.976  51.833  0.50 44.86           C  
ANISOU 1366  CE  LYS B  66     5199   6094   5751  -1377   2042   -622       C  
ATOM   1367  NZ  LYS B  66      15.265  37.224  50.555  0.50 43.72           N  
ANISOU 1367  NZ  LYS B  66     5198   5642   5770   -797   1986   -879       N  
ATOM   1368  N   SER B  67      17.309  39.811  56.140  0.50 39.30           N  
ANISOU 1368  N   SER B  67     3185   5083   6664   -154   3083   -527       N  
ATOM   1369  CA  SER B  67      17.447  41.268  56.088  0.50 39.90           C  
ANISOU 1369  CA  SER B  67     3478   5081   6601   -334   3201   -629       C  
ATOM   1370  C   SER B  67      16.209  41.892  55.463  1.00 38.19           C  
ANISOU 1370  C   SER B  67     3731   4931   5850   -671   3064   -693       C  
ATOM   1371  O   SER B  67      15.755  41.470  54.390  1.00 42.65           O  
ANISOU 1371  O   SER B  67     5037   5360   5810  -1825   2141   -371       O  
ATOM   1372  CB  SER B  67      18.694  41.651  55.287  0.00 39.99           C  
ANISOU 1372  CB  SER B  67     3481   5125   6589   -332   3200   -629       C  
ATOM   1373  OG  SER B  67      19.875  41.297  55.986  0.00 40.02           O  
ANISOU 1373  OG  SER B  67     3478   5133   6595   -360   3202   -631       O  
ATOM   1374  N   GLY B  68      15.600  42.819  56.177  1.00 38.74           N  
ANISOU 1374  N   GLY B  68     3805   4740   6174  -1072   2019    -80       N  
ATOM   1375  CA  GLY B  68      14.425  43.513  55.734  1.00 37.74           C  
ANISOU 1375  CA  GLY B  68     4270   4454   5618  -1299   1699    621       C  
ATOM   1376  C   GLY B  68      13.115  42.839  56.019  1.00 34.25           C  
ANISOU 1376  C   GLY B  68     3736   4138   5139   -704   2037    822       C  
ATOM   1377  O   GLY B  68      12.063  43.386  55.650  1.00 36.97           O  
ANISOU 1377  O   GLY B  68     3615   3951   6481     21   1674   1426       O  
ATOM   1378  N   ARG B  69      13.124  41.648  56.613  1.00 31.18           N  
ANISOU 1378  N   ARG B  69     3114   4340   4391   -493   2169    497       N  
ATOM   1379  CA  ARG B  69      11.897  40.912  56.879  1.00 27.84           C  
ANISOU 1379  CA  ARG B  69     2505   3834   4237    234   2024    198       C  
ATOM   1380  C   ARG B  69      11.303  41.246  58.246  1.00 28.43           C  
ANISOU 1380  C   ARG B  69     2971   3637   4194   -197   1584     32       C  
ATOM   1381  O   ARG B  69      11.984  41.123  59.271  1.00 28.75           O  
ANISOU 1381  O   ARG B  69     2634   4043   4247   -263      7   -120       O  
ATOM   1382  CB  ARG B  69      12.215  39.385  56.873  1.00 27.61           C  
ANISOU 1382  CB  ARG B  69     2238   3876   4377    555   2025    179       C  
ATOM   1383  CG  ARG B  69      10.967  38.545  57.172  1.00 27.36           C  
ANISOU 1383  CG  ARG B  69     2620   3844   3931    256   1955    332       C  
ATOM   1384  CD  ARG B  69      11.337  37.054  57.202  1.00 28.24           C  
ANISOU 1384  CD  ARG B  69     2857   3874   3999    420   1981     64       C  
ATOM   1385  NE  ARG B  69      11.509  36.513  55.855  1.00 29.25           N  
ANISOU 1385  NE  ARG B  69     3219   3898   3998    715   1959    -45       N  
ATOM   1386  CZ  ARG B  69      12.228  35.464  55.513  1.00 28.90           C  
ANISOU 1386  CZ  ARG B  69     3086   3997   3898    843   2167    -19       C  
ATOM   1387  NH1 ARG B  69      12.810  34.712  56.439  1.00 29.52           N  
ANISOU 1387  NH1 ARG B  69     3357   3952   3907   1144   1193    793       N  
ATOM   1388  NH2 ARG B  69      12.331  35.114  54.228  1.00 30.45           N  
ANISOU 1388  NH2 ARG B  69     3522   4157   3890   1391   1859    516       N  
ATOM   1389  N   THR B  70      10.015  41.558  58.251  1.00 27.13           N  
ANISOU 1389  N   THR B  70     3194   3683   3430   -900   2057   -540       N  
ATOM   1390  CA  THR B  70       9.275  41.727  59.502  1.00 26.91           C  
ANISOU 1390  CA  THR B  70     3748   3118   3359  -1192   1558   -265       C  
ATOM   1391  C   THR B  70       8.189  40.667  59.593  1.00 22.42           C  
ANISOU 1391  C   THR B  70     2614   2828   3078   -253   1212   -430       C  
ATOM   1392  O   THR B  70       7.716  40.178  58.555  1.00 26.04           O  
ANISOU 1392  O   THR B  70     3226   3605   3061   -923   1730   -371       O  
ATOM   1393  CB  THR B  70       8.643  43.133  59.577  1.00 29.62           C  
ANISOU 1393  CB  THR B  70     4230   3041   3983   -910    839    451       C  
ATOM   1394  OG1 THR B  70       7.955  43.391  58.344  1.00 30.21           O  
ANISOU 1394  OG1 THR B  70     4400   3117   3961      8   1004    -65       O  
ATOM   1395  CG2 THR B  70       9.709  44.204  59.695  1.00 34.79           C  
ANISOU 1395  CG2 THR B  70     4822   3068   5329  -1239   1967    791       C  
ATOM   1396  N   TRP B  71       7.775  40.339  60.813  1.00 18.76           N  
ANISOU 1396  N   TRP B  71     1631   2381   3117    203    892   -154       N  
ATOM   1397  CA  TRP B  71       6.708  39.337  61.002  1.00 18.38           C  
ANISOU 1397  CA  TRP B  71     1434   2667   2883    289    777    -62       C  
ATOM   1398  C   TRP B  71       5.517  40.019  61.695  1.00 17.94           C  
ANISOU 1398  C   TRP B  71     1599   2598   2618     60    626     95       C  
ATOM   1399  O   TRP B  71       5.673  40.881  62.559  1.00 18.34           O  
ANISOU 1399  O   TRP B  71     1740   2759   2471   -159    423   -266       O  
ATOM   1400  CB  TRP B  71       7.226  38.210  61.902  1.00 18.97           C  
ANISOU 1400  CB  TRP B  71     2094   2446   2668    121    752    -88       C  
ATOM   1401  CG  TRP B  71       8.201  37.296  61.232  1.00 18.01           C  
ANISOU 1401  CG  TRP B  71     1822   2648   2372    456    634    -88       C  
ATOM   1402  CD1 TRP B  71       9.554  37.391  61.229  1.00 18.86           C  
ANISOU 1402  CD1 TRP B  71     2014   2638   2514    239    341   -418       C  
ATOM   1403  CD2 TRP B  71       7.874  36.159  60.406  1.00 17.50           C  
ANISOU 1403  CD2 TRP B  71     1750   2714   2187    509    942   -153       C  
ATOM   1404  NE1 TRP B  71      10.096  36.363  60.482  1.00 18.59           N  
ANISOU 1404  NE1 TRP B  71     1794   2765   2505    373    223   -372       N  
ATOM   1405  CE2 TRP B  71       9.083  35.594  59.979  1.00 18.38           C  
ANISOU 1405  CE2 TRP B  71     1989   2574   2420    300    766   -126       C  
ATOM   1406  CE3 TRP B  71       6.674  35.542  60.027  1.00 17.25           C  
ANISOU 1406  CE3 TRP B  71     2032   2292   2231    465    844    147       C  
ATOM   1407  CZ2 TRP B  71       9.144  34.461  59.168  1.00 18.27           C  
ANISOU 1407  CZ2 TRP B  71     1890   2599   2452    471    682   -346       C  
ATOM   1408  CZ3 TRP B  71       6.738  34.416  59.223  1.00 16.38           C  
ANISOU 1408  CZ3 TRP B  71     1767   2341   2116    807    755    -95       C  
ATOM   1409  CH2 TRP B  71       7.964  33.883  58.809  1.00 17.44           C  
ANISOU 1409  CH2 TRP B  71     1855   2305   2466    606    432    120       C  
ATOM   1410  N   ARG B  72       4.340  39.546  61.313  1.00 15.63           N  
ANISOU 1410  N   ARG B  72     1573   2221   2146    204   1287   -212       N  
ATOM   1411  CA  ARG B  72       3.096  39.973  61.952  1.00 15.43           C  
ANISOU 1411  CA  ARG B  72     1797   2170   1897   -154    708    -16       C  
ATOM   1412  C   ARG B  72       2.253  38.730  62.275  1.00 13.98           C  
ANISOU 1412  C   ARG B  72     1539   1968   1805    253    717   -249       C  
ATOM   1413  O   ARG B  72       2.480  37.660  61.695  1.00 13.98           O  
ANISOU 1413  O   ARG B  72     1719   1945   1647    115    603   -525       O  
ATOM   1414  CB  ARG B  72       2.344  40.929  61.041  1.00 16.53           C  
ANISOU 1414  CB  ARG B  72     1844   1915   2521     59    706   -389       C  
ATOM   1415  CG  ARG B  72       2.971  42.317  60.930  1.00 19.90           C  
ANISOU 1415  CG  ARG B  72     2200   2055   3305   -196    984   -397       C  
ATOM   1416  CD  ARG B  72       2.252  43.146  59.881  1.00 21.33           C  
ANISOU 1416  CD  ARG B  72     2689   1630   3786    341   1053   -386       C  
ATOM   1417  NE  ARG B  72       2.794  44.454  59.701  1.00 27.36           N  
ANISOU 1417  NE  ARG B  72     3949   1756   4692   -193   1079   -452       N  
ATOM   1418  CZ  ARG B  72       2.757  45.505  60.473  1.00 29.28           C  
ANISOU 1418  CZ  ARG B  72     4758   1915   4450  -1105   1123     14       C  
ATOM   1419  NH1 ARG B  72       1.818  45.671  61.406  1.00 29.42           N  
ANISOU 1419  NH1 ARG B  72     4405   2976   3797    -47   1701    253       N  
ATOM   1420  NH2 ARG B  72       3.637  46.481  60.283  1.00 40.88           N  
ANISOU 1420  NH2 ARG B  72     6720   3101   5713  -3041   -723    774       N  
ATOM   1421  N   GLU B  73       1.280  38.906  63.153  1.00 13.87           N  
ANISOU 1421  N   GLU B  73     1752   1523   1994    -39    594   -384       N  
ATOM   1422  CA  GLU B  73       0.432  37.789  63.583  1.00 12.99           C  
ANISOU 1422  CA  GLU B  73     1618   1360   1957    132    175   -131       C  
ATOM   1423  C   GLU B  73      -1.035  38.108  63.378  1.00 12.09           C  
ANISOU 1423  C   GLU B  73     1697   1253   1642     95    265    311       C  
ATOM   1424  O   GLU B  73      -1.436  39.260  63.321  1.00 11.83           O  
ANISOU 1424  O   GLU B  73     1621   1285   1589    102    539     96       O  
ATOM   1425  CB  GLU B  73       0.729  37.438  65.031  1.00 12.80           C  
ANISOU 1425  CB  GLU B  73     1312   1561   1990    236     11     19       C  
ATOM   1426  CG  GLU B  73       0.557  38.630  65.984  1.00 13.50           C  
ANISOU 1426  CG  GLU B  73     1525   1647   1957    130    338   -411       C  
ATOM   1427  CD  GLU B  73       0.494  38.140  67.429  1.00 17.94           C  
ANISOU 1427  CD  GLU B  73     2654   2278   1884     23    110   -535       C  
ATOM   1428  OE1 GLU B  73      -0.306  37.224  67.683  1.00 17.74           O  
ANISOU 1428  OE1 GLU B  73     2423   2943   1375   -119     23    176       O  
ATOM   1429  OE2 GLU B  73       1.272  38.657  68.247  1.00 24.80           O  
ANISOU 1429  OE2 GLU B  73     3925   3660   1839  -1462   -565   -244       O  
ATOM   1430  N   ALA B  74      -1.856  37.041  63.390  1.00 10.05           N  
ANISOU 1430  N   ALA B  74     1576   1130   1112    256    115    -10       N  
ATOM   1431  CA  ALA B  74      -3.285  37.169  63.390  1.00 10.42           C  
ANISOU 1431  CA  ALA B  74     1428   1363   1168    317    164    295       C  
ATOM   1432  C   ALA B  74      -3.912  35.934  64.066  1.00 10.31           C  
ANISOU 1432  C   ALA B  74     1365   1365   1188    344    298   -294       C  
ATOM   1433  O   ALA B  74      -3.450  34.813  63.872  1.00 11.81           O  
ANISOU 1433  O   ALA B  74     1568   1399   1520    361    604   -177       O  
ATOM   1434  CB  ALA B  74      -3.861  37.293  61.988  1.00 12.20           C  
ANISOU 1434  CB  ALA B  74     1765   1708   1165   -381   -139    166       C  
ATOM   1435  N   ASP B  75      -5.008  36.172  64.779  1.00 10.51           N  
ANISOU 1435  N   ASP B  75     1387   1453   1153    310    154     12       N  
ATOM   1436  CA  ASP B  75      -5.736  35.097  65.416  1.00  9.74           C  
ANISOU 1436  CA  ASP B  75     1372   1295   1032    495    268   -135       C  
ATOM   1437  C   ASP B  75      -6.504  34.254  64.396  1.00 11.44           C  
ANISOU 1437  C   ASP B  75     1899   1444   1004     76    -46   -226       C  
ATOM   1438  O   ASP B  75      -7.171  34.815  63.528  1.00 11.39           O  
ANISOU 1438  O   ASP B  75     1753   1418   1157     97   -119   -223       O  
ATOM   1439  CB  ASP B  75      -6.721  35.612  66.471  1.00  9.44           C  
ANISOU 1439  CB  ASP B  75     1210   1342   1035    307    223   -245       C  
ATOM   1440  CG  ASP B  75      -6.041  36.142  67.713  1.00 10.18           C  
ANISOU 1440  CG  ASP B  75     1480   1379   1007   -148    440   -255       C  
ATOM   1441  OD1 ASP B  75      -4.853  36.497  67.706  1.00 10.62           O  
ANISOU 1441  OD1 ASP B  75     1317   1683   1035   -109    267   -115       O  
ATOM   1442  OD2 ASP B  75      -6.781  36.273  68.719  1.00 10.36           O  
ANISOU 1442  OD2 ASP B  75     1255   1637   1046     63     42   -111       O  
ATOM   1443  N   ILE B  76      -6.537  32.954  64.619  1.00 10.67           N  
ANISOU 1443  N   ILE B  76     1468   1429   1158    267    -98   -125       N  
ATOM   1444  CA  ILE B  76      -7.291  32.032  63.738  1.00 11.36           C  
ANISOU 1444  CA  ILE B  76     1423   1483   1412    170    240   -433       C  
ATOM   1445  C   ILE B  76      -8.307  31.251  64.560  1.00 11.37           C  
ANISOU 1445  C   ILE B  76     1512   1419   1387    198   -412    -68       C  
ATOM   1446  O   ILE B  76      -8.073  30.945  65.730  1.00 12.67           O  
ANISOU 1446  O   ILE B  76     1904   1503   1406    -41    192   -104       O  
ATOM   1447  CB  ILE B  76      -6.259  31.097  63.075  1.00 11.47           C  
ANISOU 1447  CB  ILE B  76     1667   1457   1233    267      4   -253       C  
ATOM   1448  CG1 ILE B  76      -5.317  31.876  62.137  1.00 12.29           C  
ANISOU 1448  CG1 ILE B  76     1629   1849   1190    104    384   -264       C  
ATOM   1449  CG2 ILE B  76      -6.877  29.937  62.338  1.00 12.92           C  
ANISOU 1449  CG2 ILE B  76     2073   1397   1441    137   -362   -637       C  
ATOM   1450  CD1 ILE B  76      -6.048  32.470  60.950  1.00 13.83           C  
ANISOU 1450  CD1 ILE B  76     2563   1653   1040    305   -164   -355       C  
ATOM   1451  N   ASN B  77      -9.425  30.881  63.953  1.00 12.92           N  
ANISOU 1451  N   ASN B  77     1545   1732   1632    -98     54   -561       N  
ATOM   1452  CA  ASN B  77     -10.458  30.086  64.566  1.00 13.90           C  
ANISOU 1452  CA  ASN B  77     1631   1809   1841   -112    936   -783       C  
ATOM   1453  C   ASN B  77     -11.186  30.761  65.712  1.00 14.13           C  
ANISOU 1453  C   ASN B  77     2001   1845   1521   -451    873   -261       C  
ATOM   1454  O   ASN B  77     -11.798  30.055  66.543  1.00 16.07           O  
ANISOU 1454  O   ASN B  77     2227   2089   1791   -840    948   -495       O  
ATOM   1455  CB  ASN B  77      -9.965  28.706  65.000  1.00 18.62           C  
ANISOU 1455  CB  ASN B  77     3039   1570   2467   -390    485   -718       C  
ATOM   1456  CG  ASN B  77      -9.531  27.812  63.878  1.00 18.98           C  
ANISOU 1456  CG  ASN B  77     3203   1579   2428   -189    611   -220       C  
ATOM   1457  OD1 ASN B  77     -10.087  27.830  62.777  1.00 20.29           O  
ANISOU 1457  OD1 ASN B  77     3055   2207   2446   -427    471  -1087       O  
ATOM   1458  ND2 ASN B  77      -8.491  27.012  64.121  1.00 20.14           N  
ANISOU 1458  ND2 ASN B  77     3256   1664   2733    212    469   -361       N  
ATOM   1459  N   TYR B  78     -11.134  32.084  65.779  1.00 13.04           N  
ANISOU 1459  N   TYR B  78     1528   1847   1578   -167    260   -317       N  
ATOM   1460  CA  TYR B  78     -11.828  32.809  66.855  1.00 13.24           C  
ANISOU 1460  CA  TYR B  78     1450   1769   1812    -51    538   -725       C  
ATOM   1461  C   TYR B  78     -13.280  33.094  66.511  1.00 12.32           C  
ANISOU 1461  C   TYR B  78     1534   1814   1332   -167     74   -566       C  
ATOM   1462  O   TYR B  78     -13.561  33.586  65.430  1.00 13.87           O  
ANISOU 1462  O   TYR B  78     1758   2326   1187    -73    354    -70       O  
ATOM   1463  CB  TYR B  78     -11.084  34.118  67.166  1.00 12.93           C  
ANISOU 1463  CB  TYR B  78     1565   1786   1561   -203    469   -394       C  
ATOM   1464  CG  TYR B  78     -11.746  34.877  68.300  1.00 12.43           C  
ANISOU 1464  CG  TYR B  78     1312   1807   1605   -148    295   -534       C  
ATOM   1465  CD1 TYR B  78     -11.546  34.499  69.617  1.00 11.84           C  
ANISOU 1465  CD1 TYR B  78     1159   1696   1644   -163    291   -372       C  
ATOM   1466  CD2 TYR B  78     -12.677  35.883  68.042  1.00 12.02           C  
ANISOU 1466  CD2 TYR B  78     1410   1756   1400   -361    -11   -123       C  
ATOM   1467  CE1 TYR B  78     -12.176  35.159  70.655  1.00 12.25           C  
ANISOU 1467  CE1 TYR B  78     1459   1624   1574   -437    626   -617       C  
ATOM   1468  CE2 TYR B  78     -13.323  36.547  69.077  1.00 12.45           C  
ANISOU 1468  CE2 TYR B  78     1601   1713   1415   -103     40    -45       C  
ATOM   1469  CZ  TYR B  78     -13.082  36.170  70.365  1.00 11.67           C  
ANISOU 1469  CZ  TYR B  78     1371   1639   1424   -297    538   -570       C  
ATOM   1470  OH  TYR B  78     -13.704  36.827  71.399  1.00 13.25           O  
ANISOU 1470  OH  TYR B  78     2167   1444   1423    -94    661   -222       O  
ATOM   1471  N   THR B  79     -14.184  32.774  67.441  1.00 11.75           N  
ANISOU 1471  N   THR B  79     1503   1679   1283    -74    317   -485       N  
ATOM   1472  CA  THR B  79     -15.581  33.110  67.362  1.00 13.87           C  
ANISOU 1472  CA  THR B  79     1079   2483   1708     63    410   -256       C  
ATOM   1473  C   THR B  79     -16.071  33.963  68.518  1.00 12.95           C  
ANISOU 1473  C   THR B  79      604   2588   1727    374    346   -200       C  
ATOM   1474  O   THR B  79     -16.652  35.034  68.323  1.00 16.26           O  
ANISOU 1474  O   THR B  79     2105   2392   1683    510   -133   -825       O  
ATOM   1475  CB  THR B  79     -16.484  31.904  67.186  1.00 16.67           C  
ANISOU 1475  CB  THR B  79     1382   2664   2289   -282     40   -569       C  
ATOM   1476  OG1 THR B  79     -16.254  30.948  68.254  1.00 23.08           O  
ANISOU 1476  OG1 THR B  79     3904   2458   2406   -919    294    -21       O  
ATOM   1477  CG2 THR B  79     -16.210  31.174  65.922  1.00 18.13           C  
ANISOU 1477  CG2 THR B  79     2019   2557   2311   -424    624  -1210       C  
ATOM   1478  N   SER B  80     -15.750  33.555  69.740  1.00 14.05           N  
ANISOU 1478  N   SER B  80     1314   2339   1685   -186   -198   -148       N  
ATOM   1479  CA  SER B  80     -16.069  34.318  70.923  1.00 14.55           C  
ANISOU 1479  CA  SER B  80     1457   2351   1720   -349    198   -818       C  
ATOM   1480  C   SER B  80     -15.188  33.907  72.114  1.00 14.56           C  
ANISOU 1480  C   SER B  80     1943   1924   1663   -857    612   -701       C  
ATOM   1481  O   SER B  80     -14.572  32.822  72.091  1.00 15.84           O  
ANISOU 1481  O   SER B  80     2635   1878   1507   -503    264   -468       O  
ATOM   1482  CB  SER B  80     -17.539  34.123  71.336  1.00 15.45           C  
ANISOU 1482  CB  SER B  80     1301   2996   1572   -404     32   -605       C  
ATOM   1483  OG  SER B  80     -17.777  32.867  71.864  1.00 24.20           O  
ANISOU 1483  OG  SER B  80     3079   3171   2945  -1976   1474  -1404       O  
ATOM   1484  N   GLY B  81     -15.291  34.674  73.176  1.00 13.57           N  
ANISOU 1484  N   GLY B  81     1490   1956   1711   -413    388   -895       N  
ATOM   1485  CA  GLY B  81     -14.654  34.409  74.447  1.00 15.38           C  
ANISOU 1485  CA  GLY B  81     2174   2098   1572   -858    314   -650       C  
ATOM   1486  C   GLY B  81     -13.211  34.845  74.488  1.00 12.74           C  
ANISOU 1486  C   GLY B  81     1995   2031    815   -636    658   -264       C  
ATOM   1487  O   GLY B  81     -12.790  35.787  73.788  1.00 11.67           O  
ANISOU 1487  O   GLY B  81     1554   1852   1030   -256    479   -208       O  
ATOM   1488  N   PHE B  82     -12.428  34.251  75.359  1.00 12.90           N  
ANISOU 1488  N   PHE B  82     1994   1691   1218   -124    603    211       N  
ATOM   1489  CA  PHE B  82     -10.986  34.515  75.430  1.00 12.61           C  
ANISOU 1489  CA  PHE B  82     1829   1737   1224     -7    807    188       C  
ATOM   1490  C   PHE B  82     -10.330  34.127  74.111  1.00 13.39           C  
ANISOU 1490  C   PHE B  82     1925   1972   1192   -298    813   -240       C  
ATOM   1491  O   PHE B  82     -10.750  33.222  73.420  1.00 15.26           O  
ANISOU 1491  O   PHE B  82     2420   1979   1399   -681    586   -192       O  
ATOM   1492  CB  PHE B  82     -10.370  33.720  76.589  1.00 12.78           C  
ANISOU 1492  CB  PHE B  82     1908   1778   1172    410    601    323       C  
ATOM   1493  CG  PHE B  82     -10.738  34.250  77.955  1.00 11.10           C  
ANISOU 1493  CG  PHE B  82     1158   1843   1215    153     88    286       C  
ATOM   1494  CD1 PHE B  82     -10.188  35.397  78.467  1.00 12.10           C  
ANISOU 1494  CD1 PHE B  82     1650   1633   1315     34    -29    130       C  
ATOM   1495  CD2 PHE B  82     -11.655  33.557  78.756  1.00 13.60           C  
ANISOU 1495  CD2 PHE B  82     1285   2496   1387   -304    127    379       C  
ATOM   1496  CE1 PHE B  82     -10.530  35.879  79.718  1.00 12.31           C  
ANISOU 1496  CE1 PHE B  82     1646   1782   1251    -61    -29    488       C  
ATOM   1497  CE2 PHE B  82     -12.011  34.038  79.989  1.00 18.05           C  
ANISOU 1497  CE2 PHE B  82     2704   3175    979  -1545   -134    308       C  
ATOM   1498  CZ  PHE B  82     -11.468  35.221  80.479  1.00 14.36           C  
ANISOU 1498  CZ  PHE B  82     1710   2430   1317   -280   -484    648       C  
ATOM   1499  N   ARG B  83      -9.207  34.825  73.808  1.00 12.82           N  
ANISOU 1499  N   ARG B  83     1750   1894   1226   -243    845   -277       N  
ATOM   1500  CA  ARG B  83      -8.428  34.433  72.656  1.00 12.76           C  
ANISOU 1500  CA  ARG B  83     1811   1763   1275   -212    589   -177       C  
ATOM   1501  C   ARG B  83      -7.921  33.002  72.819  1.00 13.26           C  
ANISOU 1501  C   ARG B  83     2046   1732   1262   -399    663     54       C  
ATOM   1502  O   ARG B  83      -7.690  32.535  73.943  1.00 15.75           O  
ANISOU 1502  O   ARG B  83     3058   1655   1272   -258    856    -11       O  
ATOM   1503  CB  ARG B  83      -7.260  35.374  72.358  1.00 11.61           C  
ANISOU 1503  CB  ARG B  83     1475   1534   1401     84    377   -371       C  
ATOM   1504  CG  ARG B  83      -7.715  36.807  72.048  1.00 11.37           C  
ANISOU 1504  CG  ARG B  83     1624   1525   1171     69    159   -332       C  
ATOM   1505  CD  ARG B  83      -6.575  37.798  72.054  1.00 11.85           C  
ANISOU 1505  CD  ARG B  83     1937   1644    921   -168    419   -278       C  
ATOM   1506  NE  ARG B  83      -5.619  37.573  70.996  1.00 11.42           N  
ANISOU 1506  NE  ARG B  83     1760   1367   1212   -102    -87   -218       N  
ATOM   1507  CZ  ARG B  83      -4.378  37.992  70.966  1.00 13.02           C  
ANISOU 1507  CZ  ARG B  83     2008   1687   1251   -445   -644    -63       C  
ATOM   1508  NH1 ARG B  83      -3.896  38.637  72.034  1.00 13.57           N  
ANISOU 1508  NH1 ARG B  83     2062   1825   1269   -461   -154   -248       N  
ATOM   1509  NH2 ARG B  83      -3.602  37.746  69.929  1.00 14.36           N  
ANISOU 1509  NH2 ARG B  83     1706   2764    987   -534    323   -157       N  
ATOM   1510  N   ASN B  84      -7.848  32.299  71.709  1.00 13.35           N  
ANISOU 1510  N   ASN B  84     2011   1775   1289     55    282   -138       N  
ATOM   1511  CA  ASN B  84      -7.460  30.886  71.748  1.00 14.48           C  
ANISOU 1511  CA  ASN B  84     2345   1750   1406    -80    928    183       C  
ATOM   1512  C   ASN B  84      -5.970  30.749  71.491  1.00 13.97           C  
ANISOU 1512  C   ASN B  84     2150   1794   1363    227    552   -109       C  
ATOM   1513  O   ASN B  84      -5.227  31.717  71.644  1.00 15.50           O  
ANISOU 1513  O   ASN B  84     2317   1982   1590    -94    309   -146       O  
ATOM   1514  CB  ASN B  84      -8.298  30.117  70.747  1.00 14.22           C  
ANISOU 1514  CB  ASN B  84     2275   1692   1437     43    857     -1       C  
ATOM   1515  CG  ASN B  84      -8.034  30.537  69.317  1.00 13.94           C  
ANISOU 1515  CG  ASN B  84     2281   1581   1435   -192    573   -170       C  
ATOM   1516  OD1 ASN B  84      -6.986  31.100  68.995  1.00 14.31           O  
ANISOU 1516  OD1 ASN B  84     2208   1716   1512   -235    397   -272       O  
ATOM   1517  ND2 ASN B  84      -9.014  30.265  68.454  1.00 16.51           N  
ANISOU 1517  ND2 ASN B  84     2512   2331   1429   -613    358   -250       N  
ATOM   1518  N   SER B  85      -5.520  29.535  71.214  1.00 15.48           N  
ANISOU 1518  N   SER B  85     2460   1829   1595    562    352    -21       N  
ATOM   1519  CA  SER B  85      -4.101  29.269  71.072  1.00 14.99           C  
ANISOU 1519  CA  SER B  85     2347   1835   1515    722    527   -125       C  
ATOM   1520  C   SER B  85      -3.587  29.331  69.655  1.00 15.57           C  
ANISOU 1520  C   SER B  85     2140   2199   1577    731   1139   -247       C  
ATOM   1521  O   SER B  85      -2.380  29.052  69.434  1.00 15.04           O  
ANISOU 1521  O   SER B  85     2401   1978   1336    501    283      2       O  
ATOM   1522  CB  SER B  85      -3.740  27.911  71.706  1.00 18.00           C  
ANISOU 1522  CB  SER B  85     2975   1777   2087   1079    -33    145       C  
ATOM   1523  OG  SER B  85      -4.423  26.879  71.040  1.00 26.67           O  
ANISOU 1523  OG  SER B  85     5400   1964   2769   -100    808   -320       O  
ATOM   1524  N   ASP B  86      -4.440  29.631  68.695  1.00 14.92           N  
ANISOU 1524  N   ASP B  86     2520   1711   1440    234     66    270       N  
ATOM   1525  CA  ASP B  86      -4.154  29.505  67.290  1.00 12.94           C  
ANISOU 1525  CA  ASP B  86     2019   1354   1544    306   -223    241       C  
ATOM   1526  C   ASP B  86      -3.783  30.843  66.649  1.00 10.97           C  
ANISOU 1526  C   ASP B  86     1472   1390   1305    563    252    -14       C  
ATOM   1527  O   ASP B  86      -4.541  31.814  66.707  1.00 12.07           O  
ANISOU 1527  O   ASP B  86     1464   1341   1782    238    177   -115       O  
ATOM   1528  CB  ASP B  86      -5.368  28.911  66.565  1.00 15.54           C  
ANISOU 1528  CB  ASP B  86     2515   1769   1620   -272    465   -250       C  
ATOM   1529  CG  ASP B  86      -5.702  27.504  66.979  1.00 19.19           C  
ANISOU 1529  CG  ASP B  86     2842   1654   2797   -274    851   -209       C  
ATOM   1530  OD1 ASP B  86      -4.871  26.836  67.659  1.00 20.15           O  
ANISOU 1530  OD1 ASP B  86     3234   1587   2836    -61    121   -111       O  
ATOM   1531  OD2 ASP B  86      -6.780  26.990  66.581  1.00 22.78           O  
ANISOU 1531  OD2 ASP B  86     3118   1901   3638   -691    570   -443       O  
ATOM   1532  N   ARG B  87      -2.661  30.841  65.926  1.00 10.55           N  
ANISOU 1532  N   ARG B  87     1488   1456   1065    599    204   -146       N  
ATOM   1533  CA  ARG B  87      -2.247  32.058  65.235  1.00 11.68           C  
ANISOU 1533  CA  ARG B  87     1928   1456   1055    372   -109    -62       C  
ATOM   1534  C   ARG B  87      -1.611  31.746  63.878  1.00 10.78           C  
ANISOU 1534  C   ARG B  87     1296   1695   1104    509    118     16       C  
ATOM   1535  O   ARG B  87      -0.964  30.715  63.710  1.00 12.23           O  
ANISOU 1535  O   ARG B  87     1724   1712   1210    921    432    287       O  
ATOM   1536  CB  ARG B  87      -1.151  32.805  66.051  1.00 11.16           C  
ANISOU 1536  CB  ARG B  87     1734   1450   1054    383     84   -285       C  
ATOM   1537  CG  ARG B  87      -1.539  33.082  67.481  1.00 11.58           C  
ANISOU 1537  CG  ARG B  87     1683   1696   1019    437     95   -474       C  
ATOM   1538  CD  ARG B  87      -2.370  34.269  67.714  1.00 11.58           C  
ANISOU 1538  CD  ARG B  87     1751   1613   1035    298    275   -520       C  
ATOM   1539  NE  ARG B  87      -2.623  34.541  69.140  1.00 12.24           N  
ANISOU 1539  NE  ARG B  87     1922   1691   1036    378    378   -349       N  
ATOM   1540  CZ  ARG B  87      -3.597  33.997  69.853  1.00 11.75           C  
ANISOU 1540  CZ  ARG B  87     1941   1578    945    465    535   -639       C  
ATOM   1541  NH1 ARG B  87      -4.436  33.138  69.292  1.00 13.36           N  
ANISOU 1541  NH1 ARG B  87     2362   1485   1228    123    470   -160       N  
ATOM   1542  NH2 ARG B  87      -3.728  34.243  71.148  1.00 14.88           N  
ANISOU 1542  NH2 ARG B  87     2789   2014    852    535    274   -494       N  
ATOM   1543  N   ILE B  88      -1.780  32.663  62.959  1.00 11.66           N  
ANISOU 1543  N   ILE B  88     1692   1584   1154    371    228    -92       N  
ATOM   1544  CA  ILE B  88      -1.041  32.704  61.719  1.00 12.43           C  
ANISOU 1544  CA  ILE B  88     1572   2045   1104    240    -76   -159       C  
ATOM   1545  C   ILE B  88       0.066  33.758  61.826  1.00 10.92           C  
ANISOU 1545  C   ILE B  88     1288   1695   1166    735    131   -342       C  
ATOM   1546  O   ILE B  88      -0.194  34.832  62.374  1.00 11.72           O  
ANISOU 1546  O   ILE B  88     1426   1677   1351    264    443   -321       O  
ATOM   1547  CB  ILE B  88      -1.898  32.921  60.492  1.00 12.04           C  
ANISOU 1547  CB  ILE B  88     1674   1737   1164    510     96   -213       C  
ATOM   1548  CG1 ILE B  88      -1.446  32.354  59.186  1.00 16.62           C  
ANISOU 1548  CG1 ILE B  88     2973   2271   1073    822   -301   -331       C  
ATOM   1549  CG2 ILE B  88      -2.622  34.230  60.436  1.00 17.18           C  
ANISOU 1549  CG2 ILE B  88     1728   1800   2999    709    809   -112       C  
ATOM   1550  CD1 ILE B  88      -2.495  32.269  58.122  1.00 19.81           C  
ANISOU 1550  CD1 ILE B  88     3075   3459    994    478   -889   -596       C  
ATOM   1551  N   LEU B  89       1.280  33.367  61.465  1.00 11.99           N  
ANISOU 1551  N   LEU B  89     1283   1696   1576    618    307   -349       N  
ATOM   1552  CA  LEU B  89       2.423  34.289  61.418  1.00 13.02           C  
ANISOU 1552  CA  LEU B  89     1485   1750   1714    480    762   -388       C  
ATOM   1553  C   LEU B  89       2.800  34.516  59.947  1.00 13.13           C  
ANISOU 1553  C   LEU B  89     1618   1654   1717    425    523   -255       C  
ATOM   1554  O   LEU B  89       3.009  33.530  59.234  1.00 15.55           O  
ANISOU 1554  O   LEU B  89     2670   1594   1646    569    694   -168       O  
ATOM   1555  CB  LEU B  89       3.616  33.690  62.147  1.00 13.13           C  
ANISOU 1555  CB  LEU B  89     1314   1928   1747    496    185   -430       C  
ATOM   1556  CG  LEU B  89       3.657  33.807  63.656  1.00 16.09           C  
ANISOU 1556  CG  LEU B  89     2070   2379   1664    273   -223     26       C  
ATOM   1557  CD1 LEU B  89       3.902  35.268  64.053  1.00 20.97           C  
ANISOU 1557  CD1 LEU B  89     3994   2299   1673    443   -145  -1318       C  
ATOM   1558  CD2 LEU B  89       2.480  33.234  64.354  1.00 22.79           C  
ANISOU 1558  CD2 LEU B  89     2446   4665   1547   -564   -683   1017       C  
ATOM   1559  N   TYR B  90       2.863  35.771  59.535  1.00 14.58           N  
ANISOU 1559  N   TYR B  90     2423   1653   1465    390    882   -132       N  
ATOM   1560  CA  TYR B  90       3.157  36.065  58.125  1.00 14.70           C  
ANISOU 1560  CA  TYR B  90     2021   2145   1418    629    726    158       C  
ATOM   1561  C   TYR B  90       4.276  37.081  58.014  1.00 16.91           C  
ANISOU 1561  C   TYR B  90     2329   2681   1415    220    882     62       C  
ATOM   1562  O   TYR B  90       4.292  38.060  58.791  1.00 16.81           O  
ANISOU 1562  O   TYR B  90     2130   2626   1633     16    996   -166       O  
ATOM   1563  CB  TYR B  90       1.913  36.516  57.404  1.00 14.50           C  
ANISOU 1563  CB  TYR B  90     1877   2293   1339    963    580    -91       C  
ATOM   1564  CG  TYR B  90       1.168  37.704  57.919  1.00 14.62           C  
ANISOU 1564  CG  TYR B  90     2040   2198   1315   1006    632     51       C  
ATOM   1565  CD1 TYR B  90       0.262  37.596  58.969  1.00 14.42           C  
ANISOU 1565  CD1 TYR B  90     2035   2051   1394    684    525     83       C  
ATOM   1566  CD2 TYR B  90       1.282  38.956  57.303  1.00 16.34           C  
ANISOU 1566  CD2 TYR B  90     2731   2162   1314    323    673    259       C  
ATOM   1567  CE1 TYR B  90      -0.454  38.685  59.442  1.00 15.36           C  
ANISOU 1567  CE1 TYR B  90     2233   1977   1626    740    384    386       C  
ATOM   1568  CE2 TYR B  90       0.565  40.044  57.767  1.00 16.94           C  
ANISOU 1568  CE2 TYR B  90     2754   2121   1560    554    616   -201       C  
ATOM   1569  CZ  TYR B  90      -0.288  39.913  58.828  1.00 16.18           C  
ANISOU 1569  CZ  TYR B  90     2457   2014   1678    596   1053   -616       C  
ATOM   1570  OH  TYR B  90      -1.034  40.985  59.298  1.00 17.40           O  
ANISOU 1570  OH  TYR B  90     2806   1905   1901    394    928   -420       O  
ATOM   1571  N   SER B  91       5.177  36.899  57.067  1.00 17.00           N  
ANISOU 1571  N   SER B  91     1791   3008   1660    647    897    155       N  
ATOM   1572  CA  SER B  91       6.308  37.803  56.899  1.00 19.21           C  
ANISOU 1572  CA  SER B  91     1845   3222   2234    438   1228    234       C  
ATOM   1573  C   SER B  91       6.024  38.842  55.806  1.00 19.80           C  
ANISOU 1573  C   SER B  91     2107   3008   2409    731   1031    668       C  
ATOM   1574  O   SER B  91       5.089  38.693  55.015  1.00 19.89           O  
ANISOU 1574  O   SER B  91     2408   2906   2244    751    756    785       O  
ATOM   1575  CB  SER B  91       7.594  37.040  56.555  1.00 18.32           C  
ANISOU 1575  CB  SER B  91     2139   2947   1877    203   1129    216       C  
ATOM   1576  OG  SER B  91       7.507  36.445  55.256  1.00 20.12           O  
ANISOU 1576  OG  SER B  91     2408   3495   1741    572    698    -66       O  
ATOM   1577  N   SER B  92       6.886  39.836  55.731  1.00 21.68           N  
ANISOU 1577  N   SER B  92     2433   2850   2953    679   1512    860       N  
ATOM   1578  CA  SER B  92       6.779  40.897  54.741  1.00 25.71           C  
ANISOU 1578  CA  SER B  92     3834   2944   2993    292   1256    856       C  
ATOM   1579  C   SER B  92       7.037  40.371  53.338  1.00 26.00           C  
ANISOU 1579  C   SER B  92     3578   3375   2927    740   1071    821       C  
ATOM   1580  O   SER B  92       6.619  40.979  52.352  1.00 25.36           O  
ANISOU 1580  O   SER B  92     3192   3428   3016    675    769    899       O  
ATOM   1581  CB  SER B  92       7.672  42.069  55.102  1.00 27.97           C  
ANISOU 1581  CB  SER B  92     4246   2894   3486     77   1306    948       C  
ATOM   1582  OG  SER B  92       8.941  41.639  55.580  1.00 30.34           O  
ANISOU 1582  OG  SER B  92     3633   3607   4287    166   1484    763       O  
ATOM   1583  N   ASP B  93       7.630  39.179  53.253  1.00 25.64           N  
ANISOU 1583  N   ASP B  93     3569   3461   2711    999   1794    398       N  
ATOM   1584  CA  ASP B  93       7.865  38.477  52.020  1.00 25.36           C  
ANISOU 1584  CA  ASP B  93     3320   3670   2645   1406   1663    561       C  
ATOM   1585  C   ASP B  93       6.991  37.264  51.812  1.00 25.38           C  
ANISOU 1585  C   ASP B  93     3738   3753   2152   1081   1306    550       C  
ATOM   1586  O   ASP B  93       7.208  36.444  50.911  1.00 25.87           O  
ANISOU 1586  O   ASP B  93     3889   3846   2096   1262   1636    351       O  
ATOM   1587  CB  ASP B  93       9.308  38.248  51.696  1.00 26.17           C  
ANISOU 1587  CB  ASP B  93     3050   4083   2811   1632   1541    967       C  
ATOM   1588  CG  ASP B  93      10.080  37.492  52.758  1.00 26.12           C  
ANISOU 1588  CG  ASP B  93     3018   4019   2887   1711   2191    737       C  
ATOM   1589  OD1 ASP B  93       9.579  37.367  53.897  1.00 27.47           O  
ANISOU 1589  OD1 ASP B  93     3469   4165   2803   1711   1430    601       O  
ATOM   1590  OD2 ASP B  93      11.160  36.981  52.445  1.00 28.41           O  
ANISOU 1590  OD2 ASP B  93     2914   4118   3761   1216   1652    426       O  
ATOM   1591  N   TRP B  94       5.923  37.152  52.606  1.00 24.54           N  
ANISOU 1591  N   TRP B  94     3574   3549   2200   1287   1124    819       N  
ATOM   1592  CA  TRP B  94       4.860  36.233  52.418  1.00 24.28           C  
ANISOU 1592  CA  TRP B  94     3816   3908   1503   1006    815   1011       C  
ATOM   1593  C   TRP B  94       5.130  34.798  52.657  1.00 22.39           C  
ANISOU 1593  C   TRP B  94     3467   3881   1158    643    906    540       C  
ATOM   1594  O   TRP B  94       4.434  33.881  52.183  1.00 21.76           O  
ANISOU 1594  O   TRP B  94     2761   3970   1537    935    -52    385       O  
ATOM   1595  CB  TRP B  94       4.026  36.542  51.154  1.00 24.31           C  
ANISOU 1595  CB  TRP B  94     3882   3800   1555   1209    832   1106       C  
ATOM   1596  CG  TRP B  94       3.759  38.023  51.054  1.00 25.60           C  
ANISOU 1596  CG  TRP B  94     4019   3753   1955   1063    713   1336       C  
ATOM   1597  CD1 TRP B  94       4.357  38.909  50.209  1.00 26.13           C  
ANISOU 1597  CD1 TRP B  94     3945   3759   2226    885    551   1235       C  
ATOM   1598  CD2 TRP B  94       2.880  38.790  51.877  1.00 25.53           C  
ANISOU 1598  CD2 TRP B  94     3443   3850   2410   1246    836   1270       C  
ATOM   1599  NE1 TRP B  94       3.866  40.178  50.438  1.00 27.24           N  
ANISOU 1599  NE1 TRP B  94     3949   3718   2683    786    764    822       N  
ATOM   1600  CE2 TRP B  94       2.972  40.127  51.462  1.00 26.72           C  
ANISOU 1600  CE2 TRP B  94     3552   3802   2799   1137    725    857       C  
ATOM   1601  CE3 TRP B  94       2.000  38.476  52.918  1.00 25.42           C  
ANISOU 1601  CE3 TRP B  94     3280   3998   2379   1447    761   1273       C  
ATOM   1602  CZ2 TRP B  94       2.233  41.141  52.064  1.00 26.95           C  
ANISOU 1602  CZ2 TRP B  94     3506   3838   2895   1133    426    912       C  
ATOM   1603  CZ3 TRP B  94       1.279  39.482  53.521  1.00 25.64           C  
ANISOU 1603  CZ3 TRP B  94     3293   3924   2527   1354    887   1026       C  
ATOM   1604  CH2 TRP B  94       1.399  40.807  53.083  1.00 27.08           C  
ANISOU 1604  CH2 TRP B  94     3621   3926   2741   1190    109   1094       C  
ATOM   1605  N   LEU B  95       6.067  34.545  53.584  1.00 22.60           N  
ANISOU 1605  N   LEU B  95     3771   3849    969    285   1384    334       N  
ATOM   1606  CA  LEU B  95       6.195  33.242  54.222  1.00 20.51           C  
ANISOU 1606  CA  LEU B  95     2449   3687   1657    273   1028     30       C  
ATOM   1607  C   LEU B  95       5.035  33.136  55.259  1.00 18.17           C  
ANISOU 1607  C   LEU B  95     2342   2883   1680    506    565    638       C  
ATOM   1608  O   LEU B  95       4.746  34.135  55.899  1.00 19.83           O  
ANISOU 1608  O   LEU B  95     2788   2701   2045    131   1187   -239       O  
ATOM   1609  CB  LEU B  95       7.507  33.194  55.038  1.00 22.97           C  
ANISOU 1609  CB  LEU B  95     1921   4054   2752    596    688    536       C  
ATOM   1610  CG  LEU B  95       8.803  32.993  54.278  1.00 23.77           C  
ANISOU 1610  CG  LEU B  95     2273   3989   2771    391    595    235       C  
ATOM   1611  CD1 LEU B  95       9.913  32.593  55.269  1.00 24.40           C  
ANISOU 1611  CD1 LEU B  95     1579   4606   3084    903   -375    380       C  
ATOM   1612  CD2 LEU B  95       8.632  31.891  53.231  1.00 27.09           C  
ANISOU 1612  CD2 LEU B  95     3759   4225   2309    741    837    -26       C  
ATOM   1613  N   ILE B  96       4.406  31.999  55.354  1.00 15.72           N  
ANISOU 1613  N   ILE B  96     2039   2649   1287    854    787    -81       N  
ATOM   1614  CA  ILE B  96       3.277  31.740  56.231  1.00 13.89           C  
ANISOU 1614  CA  ILE B  96     2123   1874   1280    967    285   -276       C  
ATOM   1615  C   ILE B  96       3.515  30.537  57.147  1.00 14.18           C  
ANISOU 1615  C   ILE B  96     2159   1919   1309    822     61   -481       C  
ATOM   1616  O   ILE B  96       3.745  29.422  56.705  1.00 13.59           O  
ANISOU 1616  O   ILE B  96     2108   1886   1170    616     33   -540       O  
ATOM   1617  CB AILE B  96       1.928  31.640  55.554  0.50 14.44           C  
ANISOU 1617  CB AILE B  96     2207   1857   1423    887     21   -132       C  
ATOM   1618  CB BILE B  96       2.006  31.476  55.377  0.50 14.47           C  
ANISOU 1618  CB BILE B  96     2225   1987   1286    811   -170     44       C  
ATOM   1619  CG1AILE B  96       1.610  32.623  54.449  0.50 13.64           C  
ANISOU 1619  CG1AILE B  96     1780   1813   1588   1140   -264     -5       C  
ATOM   1620  CG1BILE B  96       1.859  32.448  54.197  0.50 14.60           C  
ANISOU 1620  CG1BILE B  96     2302   1923   1324    831   -126    -66       C  
ATOM   1621  CG2AILE B  96       0.803  31.589  56.586  0.50 17.08           C  
ANISOU 1621  CG2AILE B  96     2630   2190   1672    -98  -1141     84       C  
ATOM   1622  CG2BILE B  96       0.777  31.487  56.251  0.50 14.28           C  
ANISOU 1622  CG2BILE B  96     2248   1774   1405    775    116   -817       C  
ATOM   1623  CD1AILE B  96       1.543  34.065  54.861  0.50 13.36           C  
ANISOU 1623  CD1AILE B  96     1780   1769   1528    224   -543   -116       C  
ATOM   1624  CD1BILE B  96       0.675  33.372  54.336  0.50 15.47           C  
ANISOU 1624  CD1BILE B  96     2189   2045   1644   1049   -664    201       C  
ATOM   1625  N   TYR B  97       3.406  30.795  58.446  1.00 12.40           N  
ANISOU 1625  N   TYR B  97     1436   1964   1313    771    219   -510       N  
ATOM   1626  CA  TYR B  97       3.571  29.772  59.463  1.00 13.02           C  
ANISOU 1626  CA  TYR B  97     1749   1986   1212    956   -523   -395       C  
ATOM   1627  C   TYR B  97       2.277  29.762  60.317  1.00 13.11           C  
ANISOU 1627  C   TYR B  97     2001   1848   1131    855   -158     38       C  
ATOM   1628  O   TYR B  97       1.554  30.751  60.401  1.00 13.56           O  
ANISOU 1628  O   TYR B  97     1907   1761   1486    382    227   -114       O  
ATOM   1629  CB  TYR B  97       4.766  30.068  60.367  1.00 14.52           C  
ANISOU 1629  CB  TYR B  97     1985   2502   1030    624    406   -312       C  
ATOM   1630  CG  TYR B  97       6.110  29.626  59.849  1.00 15.42           C  
ANISOU 1630  CG  TYR B  97     1709   2609   1541    689     42   -373       C  
ATOM   1631  CD1 TYR B  97       6.740  30.294  58.806  1.00 15.82           C  
ANISOU 1631  CD1 TYR B  97     1829   2646   1537    666    255   -185       C  
ATOM   1632  CD2 TYR B  97       6.779  28.522  60.381  1.00 16.16           C  
ANISOU 1632  CD2 TYR B  97     1952   2638   1549    898    223   -187       C  
ATOM   1633  CE1 TYR B  97       7.966  29.908  58.308  1.00 16.02           C  
ANISOU 1633  CE1 TYR B  97     1922   2644   1522    650    251     -6       C  
ATOM   1634  CE2 TYR B  97       8.022  28.138  59.900  1.00 16.45           C  
ANISOU 1634  CE2 TYR B  97     2133   2380   1738   1025    133    -46       C  
ATOM   1635  CZ  TYR B  97       8.615  28.830  58.886  1.00 16.41           C  
ANISOU 1635  CZ  TYR B  97     1818   2715   1700   1062    -37     53       C  
ATOM   1636  OH  TYR B  97       9.833  28.423  58.397  1.00 18.78           O  
ANISOU 1636  OH  TYR B  97     1584   2981   2572   1094    490   -115       O  
ATOM   1637  N   LYS B  98       2.100  28.652  61.006  1.00 12.67           N  
ANISOU 1637  N   LYS B  98     1941   1953    922   1150    -26   -194       N  
ATOM   1638  CA  LYS B  98       1.048  28.517  61.983  1.00 13.79           C  
ANISOU 1638  CA  LYS B  98     1920   2472    850    899     91   -353       C  
ATOM   1639  C   LYS B  98       1.622  28.067  63.330  1.00 13.98           C  
ANISOU 1639  C   LYS B  98     2430   1978    905   1141   -102   -356       C  
ATOM   1640  O   LYS B  98       2.642  27.394  63.345  1.00 13.59           O  
ANISOU 1640  O   LYS B  98     2199   2210    757   1047    110   -121       O  
ATOM   1641  CB  LYS B  98      -0.073  27.634  61.563  1.00 17.09           C  
ANISOU 1641  CB  LYS B  98     2463   2587   1444    450     31   -151       C  
ATOM   1642  CG  LYS B  98       0.103  26.175  61.568  1.00 18.85           C  
ANISOU 1642  CG  LYS B  98     2953   2567   1642    477   -164     10       C  
ATOM   1643  CD  LYS B  98      -1.140  25.409  61.215  1.00 24.45           C  
ANISOU 1643  CD  LYS B  98     4123   2944   2221   -623    344   -288       C  
ATOM   1644  CE  LYS B  98      -0.878  23.917  61.078  1.00 27.96           C  
ANISOU 1644  CE  LYS B  98     4908   2883   2831   -740    425   -141       C  
ATOM   1645  NZ  LYS B  98      -2.183  23.198  60.823  1.00 33.71           N  
ANISOU 1645  NZ  LYS B  98     5566   3018   4225  -1384  -1019   -403       N  
ATOM   1646  N   THR B  99       0.867  28.405  64.357  1.00 13.79           N  
ANISOU 1646  N   THR B  99     2408   1960    872   1289   -203     22       N  
ATOM   1647  CA  THR B  99       1.036  27.876  65.701  1.00 13.92           C  
ANISOU 1647  CA  THR B  99     2267   2108    916   1101     60   -376       C  
ATOM   1648  C   THR B  99      -0.364  27.525  66.249  1.00 14.10           C  
ANISOU 1648  C   THR B  99     2422   1738   1196   1035    261   -325       C  
ATOM   1649  O   THR B  99      -1.311  28.276  66.001  1.00 14.33           O  
ANISOU 1649  O   THR B  99     2331   1814   1298   1108    104     96       O  
ATOM   1650  CB  THR B  99       1.765  28.787  66.664  1.00 13.44           C  
ANISOU 1650  CB  THR B  99     2101   2206    801   1205   -410   -298       C  
ATOM   1651  OG1 THR B  99       1.956  28.228  67.943  1.00 15.54           O  
ANISOU 1651  OG1 THR B  99     2821   2224    861   1131   -290    -69       O  
ATOM   1652  CG2 THR B  99       1.129  30.152  66.851  1.00 15.44           C  
ANISOU 1652  CG2 THR B  99     2782   2150    934   1150   -268   -187       C  
ATOM   1653  N   THR B 100      -0.402  26.402  66.968  1.00 15.79           N  
ANISOU 1653  N   THR B 100     2883   1607   1510    851     -3    178       N  
ATOM   1654  CA  THR B 100      -1.618  26.000  67.664  1.00 17.56           C  
ANISOU 1654  CA  THR B 100     3251   1770   1652    372     -9    637       C  
ATOM   1655  C   THR B 100      -1.355  25.807  69.150  1.00 17.66           C  
ANISOU 1655  C   THR B 100     3458   1666   1588    879    465    707       C  
ATOM   1656  O   THR B 100      -2.177  25.291  69.900  1.00 20.52           O  
ANISOU 1656  O   THR B 100     4058   2015   1725    225    367    127       O  
ATOM   1657  CB  THR B 100      -2.227  24.734  67.069  1.00 19.34           C  
ANISOU 1657  CB  THR B 100     3950   1599   1800    224     32    470       C  
ATOM   1658  OG1 THR B 100      -1.251  23.675  67.102  1.00 23.11           O  
ANISOU 1658  OG1 THR B 100     4013   1823   2946   1152    381    469       O  
ATOM   1659  CG2 THR B 100      -2.668  24.932  65.643  1.00 21.24           C  
ANISOU 1659  CG2 THR B 100     4054   2210   1804   -868    293   -575       C  
ATOM   1660  N   ASP B 101      -0.202  26.318  69.606  1.00 19.76           N  
ANISOU 1660  N   ASP B 101     3434   2639   1436    637    502    530       N  
ATOM   1661  CA  ASP B 101       0.160  26.192  71.010  1.00 20.86           C  
ANISOU 1661  CA  ASP B 101     3601   2913   1413    880    163    197       C  
ATOM   1662  C   ASP B 101       0.721  27.464  71.587  1.00 19.29           C  
ANISOU 1662  C   ASP B 101     3109   2913   1307   1150    -80    245       C  
ATOM   1663  O   ASP B 101       1.698  27.445  72.357  1.00 19.89           O  
ANISOU 1663  O   ASP B 101     3079   2907   1572   1137    -79    105       O  
ATOM   1664  CB  ASP B 101       1.119  25.020  71.210  1.00 21.04           C  
ANISOU 1664  CB  ASP B 101     3872   2864   1258   1133    213    282       C  
ATOM   1665  CG  ASP B 101       2.380  25.099  70.407  1.00 20.22           C  
ANISOU 1665  CG  ASP B 101     3730   2741   1211   1517    119    723       C  
ATOM   1666  OD1 ASP B 101       2.686  26.141  69.799  1.00 19.35           O  
ANISOU 1666  OD1 ASP B 101     3406   2878   1070   1482   -274    359       O  
ATOM   1667  OD2 ASP B 101       3.129  24.078  70.390  1.00 23.78           O  
ANISOU 1667  OD2 ASP B 101     3787   2771   2475   1651    248    120       O  
ATOM   1668  N   HIS B 102       0.134  28.624  71.255  1.00 20.00           N  
ANISOU 1668  N   HIS B 102     2811   2926   1861   1298    100    121       N  
ATOM   1669  CA  HIS B 102       0.593  29.873  71.861  1.00 21.66           C  
ANISOU 1669  CA  HIS B 102     3551   2975   1704    895   -140    184       C  
ATOM   1670  C   HIS B 102       2.072  30.139  71.586  1.00 21.05           C  
ANISOU 1670  C   HIS B 102     3788   2729   1481    677   -574     38       C  
ATOM   1671  O   HIS B 102       2.804  30.525  72.502  1.00 20.42           O  
ANISOU 1671  O   HIS B 102     3409   3007   1343   1098    -89   -567       O  
ATOM   1672  CB  HIS B 102       0.386  29.884  73.376  1.00 25.05           C  
ANISOU 1672  CB  HIS B 102     3681   4227   1611    360    268   -185       C  
ATOM   1673  CG  HIS B 102      -0.993  30.196  73.810  1.00 25.87           C  
ANISOU 1673  CG  HIS B 102     3489   4765   1577    249    111     37       C  
ATOM   1674  ND1 HIS B 102      -1.798  29.273  74.464  1.00 29.13           N  
ANISOU 1674  ND1 HIS B 102     3970   5069   2029   -341   -499    248       N  
ATOM   1675  CD2 HIS B 102      -1.700  31.365  73.721  1.00 26.02           C  
ANISOU 1675  CD2 HIS B 102     2847   4987   2054    509     50    184       C  
ATOM   1676  CE1 HIS B 102      -2.964  29.864  74.725  1.00 30.31           C  
ANISOU 1676  CE1 HIS B 102     3615   5459   2443   -344     11    281       C  
ATOM   1677  NE2 HIS B 102      -2.914  31.107  74.288  1.00 29.12           N  
ANISOU 1677  NE2 HIS B 102     2924   5422   2720    111    103   -116       N  
ATOM   1678  N   TYR B 103       2.500  30.008  70.350  1.00 19.61           N  
ANISOU 1678  N   TYR B 103     3514   2536   1402   1093   -356   -212       N  
ATOM   1679  CA  TYR B 103       3.819  30.428  69.923  1.00 20.72           C  
ANISOU 1679  CA  TYR B 103     3325   3184   1365   1129   -342    -21       C  
ATOM   1680  C   TYR B 103       4.944  29.566  70.428  1.00 19.93           C  
ANISOU 1680  C   TYR B 103     3019   3366   1187   1361   -301   -504       C  
ATOM   1681  O   TYR B 103       6.108  29.982  70.422  1.00 22.88           O  
ANISOU 1681  O   TYR B 103     2664   4359   1672   1443   -586   -410       O  
ATOM   1682  CB  TYR B 103       4.076  31.893  70.204  1.00 19.04           C  
ANISOU 1682  CB  TYR B 103     2623   3230   1383   1028   -182     14       C  
ATOM   1683  CG  TYR B 103       2.982  32.882  70.066  1.00 17.76           C  
ANISOU 1683  CG  TYR B 103     2535   3109   1105    403     20   -314       C  
ATOM   1684  CD1 TYR B 103       2.671  33.517  68.869  1.00 16.98           C  
ANISOU 1684  CD1 TYR B 103     2245   3138   1068    -16    202   -119       C  
ATOM   1685  CD2 TYR B 103       2.312  33.356  71.214  1.00 18.34           C  
ANISOU 1685  CD2 TYR B 103     3153   2789   1027    582   -172   -221       C  
ATOM   1686  CE1 TYR B 103       1.686  34.487  68.780  1.00 17.19           C  
ANISOU 1686  CE1 TYR B 103     2597   2836   1096   -283    280   -267       C  
ATOM   1687  CE2 TYR B 103       1.323  34.306  71.117  1.00 18.58           C  
ANISOU 1687  CE2 TYR B 103     3311   2666   1081    532      7   -295       C  
ATOM   1688  CZ  TYR B 103       1.017  34.882  69.910  1.00 17.42           C  
ANISOU 1688  CZ  TYR B 103     2868   2657   1096     79   -522     59       C  
ATOM   1689  OH  TYR B 103       0.011  35.838  69.851  1.00 17.35           O  
ANISOU 1689  OH  TYR B 103     2110   3130   1352    580   -284    204       O  
ATOM   1690  N   GLN B 104       4.643  28.348  70.889  1.00 21.54           N  
ANISOU 1690  N   GLN B 104     3771   3341   1072   1455   -847   -387       N  
ATOM   1691  CA  GLN B 104       5.718  27.473  71.362  1.00 22.94           C  
ANISOU 1691  CA  GLN B 104     3907   3359   1450   1846   -646   -276       C  
ATOM   1692  C   GLN B 104       6.406  26.741  70.221  1.00 22.36           C  
ANISOU 1692  C   GLN B 104     3501   3532   1463   1752   -903   -126       C  
ATOM   1693  O   GLN B 104       7.620  26.597  70.213  1.00 24.14           O  
ANISOU 1693  O   GLN B 104     3372   4174   1626   1462   -323   -345       O  
ATOM   1694  CB  GLN B 104       5.210  26.507  72.410  1.00 23.47           C  
ANISOU 1694  CB  GLN B 104     4149   3366   1401   1941   -353   -228       C  
ATOM   1695  CG  GLN B 104       4.899  27.236  73.740  1.00 26.54           C  
ANISOU 1695  CG  GLN B 104     4777   3948   1359   2044   -229   -451       C  
ATOM   1696  CD  GLN B 104       4.243  26.291  74.732  1.00 31.63           C  
ANISOU 1696  CD  GLN B 104     6125   4751   1143    969   -212   -147       C  
ATOM   1697  OE1 GLN B 104       4.843  25.922  75.727  1.00 31.53           O  
ANISOU 1697  OE1 GLN B 104     5988   4659   1332   1588   -712    447       O  
ATOM   1698  NE2 GLN B 104       2.996  25.909  74.465  1.00 33.00           N  
ANISOU 1698  NE2 GLN B 104     6643   4217   1677    489   -474     -7       N  
ATOM   1699  N   THR B 105       5.598  26.280  69.277  1.00 21.62           N  
ANISOU 1699  N   THR B 105     3212   3715   1286   1967   -705   -407       N  
ATOM   1700  CA  THR B 105       6.044  25.589  68.105  1.00 21.02           C  
ANISOU 1700  CA  THR B 105     3111   3553   1322   1901   -386   -351       C  
ATOM   1701  C   THR B 105       5.370  26.164  66.853  1.00 19.89           C  
ANISOU 1701  C   THR B 105     2274   3997   1287   2097   -492   -662       C  
ATOM   1702  O   THR B 105       4.256  26.646  66.901  1.00 19.90           O  
ANISOU 1702  O   THR B 105     2652   3723   1188   1622    -65   -298       O  
ATOM   1703  CB  THR B 105       5.857  24.087  68.150  1.00 25.17           C  
ANISOU 1703  CB  THR B 105     4326   3609   1630   1285   -382   -136       C  
ATOM   1704  OG1 THR B 105       4.499  23.708  68.167  1.00 26.51           O  
ANISOU 1704  OG1 THR B 105     4201   3481   2392   1458   -311   -780       O  
ATOM   1705  CG2 THR B 105       6.557  23.444  69.319  1.00 25.30           C  
ANISOU 1705  CG2 THR B 105     4466   3327   1819   1504   -169    676       C  
ATOM   1706  N   PHE B 106       6.096  26.140  65.749  1.00 20.39           N  
ANISOU 1706  N   PHE B 106     2581   3897   1270   1584   -554   -599       N  
ATOM   1707  CA  PHE B 106       5.599  26.684  64.500  1.00 18.57           C  
ANISOU 1707  CA  PHE B 106     2153   3592   1310   1453   -467  -1246       C  
ATOM   1708  C   PHE B 106       5.756  25.652  63.371  1.00 19.50           C  
ANISOU 1708  C   PHE B 106     2647   3433   1329   1408   -310   -980       C  
ATOM   1709  O   PHE B 106       6.711  24.888  63.380  1.00 20.21           O  
ANISOU 1709  O   PHE B 106     2335   3636   1707   1639   -156   -613       O  
ATOM   1710  CB  PHE B 106       6.377  27.950  64.128  1.00 21.82           C  
ANISOU 1710  CB  PHE B 106     2873   3602   1815    944   -581  -1055       C  
ATOM   1711  CG  PHE B 106       6.204  29.066  65.143  1.00 21.54           C  
ANISOU 1711  CG  PHE B 106     2717   3682   1785    990   -243  -1269       C  
ATOM   1712  CD1 PHE B 106       5.117  29.939  65.055  1.00 21.50           C  
ANISOU 1712  CD1 PHE B 106     2636   3745   1789   1284   -194  -1062       C  
ATOM   1713  CD2 PHE B 106       7.088  29.237  66.184  1.00 22.15           C  
ANISOU 1713  CD2 PHE B 106     2735   3833   1846    824   -466  -1080       C  
ATOM   1714  CE1 PHE B 106       5.016  31.016  65.906  1.00 22.50           C  
ANISOU 1714  CE1 PHE B 106     2980   3660   1909    968    355  -1009       C  
ATOM   1715  CE2 PHE B 106       6.975  30.307  67.063  1.00 22.79           C  
ANISOU 1715  CE2 PHE B 106     2968   3819   1870    635   -250  -1418       C  
ATOM   1716  CZ  PHE B 106       5.882  31.151  66.976  1.00 22.76           C  
ANISOU 1716  CZ  PHE B 106     2968   3790   1889    830    373  -1438       C  
ATOM   1717  N   THR B 107       4.824  25.699  62.433  1.00 18.65           N  
ANISOU 1717  N   THR B 107     2982   2863   1243   1298   -508   -599       N  
ATOM   1718  CA  THR B 107       4.874  24.797  61.262  1.00 16.86           C  
ANISOU 1718  CA  THR B 107     2624   2402   1380   1800   -413   -457       C  
ATOM   1719  C   THR B 107       4.668  25.689  60.026  1.00 15.72           C  
ANISOU 1719  C   THR B 107     2276   2398   1299   1677   -361   -400       C  
ATOM   1720  O   THR B 107       3.737  26.521  60.006  1.00 15.69           O  
ANISOU 1720  O   THR B 107     2384   2283   1294   1437    -13   -135       O  
ATOM   1721  CB  THR B 107       3.680  23.805  61.329  1.00 22.09           C  
ANISOU 1721  CB  THR B 107     4266   2306   1822    744   -433    356       C  
ATOM   1722  OG1 THR B 107       3.822  22.974  62.497  1.00 23.34           O  
ANISOU 1722  OG1 THR B 107     4468   2616   1784    672   -428    -69       O  
ATOM   1723  CG2 THR B 107       3.657  22.901  60.111  1.00 23.97           C  
ANISOU 1723  CG2 THR B 107     4919   2423   1768    539    423   -541       C  
ATOM   1724  N   LYS B 108       5.499  25.514  59.019  1.00 15.46           N  
ANISOU 1724  N   LYS B 108     1935   2482   1457   1445   -497   -525       N  
ATOM   1725  CA  LYS B 108       5.318  26.285  57.768  1.00 14.49           C  
ANISOU 1725  CA  LYS B 108     1603   2411   1491    997   -634   -347       C  
ATOM   1726  C   LYS B 108       4.157  25.670  56.983  1.00 13.64           C  
ANISOU 1726  C   LYS B 108     1895   1612   1675    914   -502   -549       C  
ATOM   1727  O   LYS B 108       4.099  24.461  56.792  1.00 17.57           O  
ANISOU 1727  O   LYS B 108     3420   1544   1713    851   -396   -488       O  
ATOM   1728  CB  LYS B 108       6.598  26.124  56.918  1.00 15.44           C  
ANISOU 1728  CB  LYS B 108     1436   2839   1590   1209    302   -121       C  
ATOM   1729  CG  LYS B 108       6.606  27.001  55.664  1.00 19.26           C  
ANISOU 1729  CG  LYS B 108     2429   3999    891   1308    399      5       C  
ATOM   1730  CD  LYS B 108       8.058  27.218  55.216  1.00 19.87           C  
ANISOU 1730  CD  LYS B 108     2431   4423    698   1186    934    298       C  
ATOM   1731  CE  LYS B 108       8.204  28.011  53.970  1.00 23.00           C  
ANISOU 1731  CE  LYS B 108     3448   4378    913    642    227    580       C  
ATOM   1732  NZ  LYS B 108       8.575  27.200  52.786  1.00 23.48           N  
ANISOU 1732  NZ  LYS B 108     4043   4195    684  -1141    408    -54       N  
ATOM   1733  N   ILE B 109       3.263  26.543  56.506  1.00 12.32           N  
ANISOU 1733  N   ILE B 109     1755   1749   1177   1024   -296   -212       N  
ATOM   1734  CA  ILE B 109       2.111  26.094  55.765  1.00 12.45           C  
ANISOU 1734  CA  ILE B 109     2096   1534   1100    682   -255    231       C  
ATOM   1735  C   ILE B 109       1.997  26.679  54.369  1.00 12.37           C  
ANISOU 1735  C   ILE B 109     1961   1597   1143    544    -82   -127       C  
ATOM   1736  O   ILE B 109       1.086  26.259  53.623  1.00 12.23           O  
ANISOU 1736  O   ILE B 109     2035   1527   1084    396     98   -147       O  
ATOM   1737  CB  ILE B 109       0.795  26.311  56.533  1.00 12.23           C  
ANISOU 1737  CB  ILE B 109     2252   1368   1027    452    147    224       C  
ATOM   1738  CG1 ILE B 109       0.494  27.757  56.887  1.00 13.67           C  
ANISOU 1738  CG1 ILE B 109     2020   1408   1764    680    384   -385       C  
ATOM   1739  CG2 ILE B 109       0.761  25.443  57.805  1.00 14.11           C  
ANISOU 1739  CG2 ILE B 109     2835   1518   1010    189    390     97       C  
ATOM   1740  CD1 ILE B 109      -0.944  28.003  57.303  1.00 15.05           C  
ANISOU 1740  CD1 ILE B 109     2053   1429   2235    537    510    -65       C  
ATOM   1741  N   ARG B 110       2.838  27.617  53.959  1.00 14.00           N  
ANISOU 1741  N   ARG B 110     2166   1660   1493    259   -298    365       N  
ATOM   1742  CA  ARG B 110       2.881  28.028  52.549  1.00 15.36           C  
ANISOU 1742  CA  ARG B 110     2126   2166   1543    -50   -667    633       C  
ATOM   1743  C   ARG B 110       4.381  28.341  52.201  1.00 20.64           C  
ANISOU 1743  C   ARG B 110     2367   3042   2432   -905  -1270   1368       C  
ATOM   1744  O   ARG B 110       4.567  29.040  51.223  1.00 21.90           O  
ANISOU 1744  O   ARG B 110     1672   4066   2583   -458    211   1653       O  
ATOM   1745  CB  ARG B 110       2.077  29.272  52.241  1.00 15.50           C  
ANISOU 1745  CB  ARG B 110     3030   1761   1098   -608   -661    238       C  
ATOM   1746  CG  ARG B 110       0.565  29.150  52.408  1.00 14.19           C  
ANISOU 1746  CG  ARG B 110     2831   1482   1080   -340   -137   -101       C  
ATOM   1747  CD  ARG B 110      -0.068  28.312  51.339  1.00 11.39           C  
ANISOU 1747  CD  ARG B 110     1840   1761    729    494    485   -305       C  
ATOM   1748  NE  ARG B 110      -1.524  28.215  51.435  1.00 11.93           N  
ANISOU 1748  NE  ARG B 110     1517   2259    758    756    141   -241       N  
ATOM   1749  CZ  ARG B 110      -2.221  27.417  52.223  1.00 12.63           C  
ANISOU 1749  CZ  ARG B 110     1620   2115   1064    578   -155   -433       C  
ATOM   1750  NH1 ARG B 110      -1.639  26.590  53.099  1.00 12.93           N  
ANISOU 1750  NH1 ARG B 110     2035   1867   1009    155    180   -372       N  
ATOM   1751  NH2 ARG B 110      -3.544  27.456  52.232  1.00 14.70           N  
ANISOU 1751  NH2 ARG B 110     1748   1714   2125    519   -161   -128       N  
ATOM   1752  OXT ARG B 110       5.209  27.880  52.949  1.00 32.87           O  
ANISOU 1752  OXT ARG B 110     2585   7218   2686  -2403  -1205   2246       O  
TER    1753      ARG B 110                                                      
ATOM   1754  N   VAL C   3      12.546  16.119  39.565  1.00 29.94           N  
ANISOU 1754  N   VAL C   3     1725   4705   4946    341   -637   -636       N  
ATOM   1755  CA  VAL C   3      13.625  16.080  40.546  1.00 29.61           C  
ANISOU 1755  CA  VAL C   3     1603   4679   4968    196   -122  -1243       C  
ATOM   1756  C   VAL C   3      14.768  15.209  40.007  1.00 29.36           C  
ANISOU 1756  C   VAL C   3     1934   4458   4765    259     36  -1346       C  
ATOM   1757  O   VAL C   3      14.537  14.086  39.567  1.00 35.00           O  
ANISOU 1757  O   VAL C   3     2432   4178   6688    -99   -763  -2038       O  
ATOM   1758  CB  VAL C   3      13.148  15.541  41.898  1.00 31.21           C  
ANISOU 1758  CB  VAL C   3     1636   5340   4885     53    934  -1532       C  
ATOM   1759  CG1 VAL C   3      14.304  15.320  42.869  1.00 31.29           C  
ANISOU 1759  CG1 VAL C   3     2307   4757   4823   -419    527  -1163       C  
ATOM   1760  CG2 VAL C   3      12.108  16.467  42.545  1.00 31.24           C  
ANISOU 1760  CG2 VAL C   3     2133   4987   4751   -616    325   -570       C  
ATOM   1761  N   ILE C   4      15.986  15.730  40.008  1.00 21.89           N  
ANISOU 1761  N   ILE C   4     1813   4014   2489    520   -946    156       N  
ATOM   1762  CA  ILE C   4      17.143  14.869  39.592  1.00 19.90           C  
ANISOU 1762  CA  ILE C   4     2237   3811   1513    329   -367    232       C  
ATOM   1763  C   ILE C   4      18.137  14.923  40.758  1.00 19.68           C  
ANISOU 1763  C   ILE C   4     2162   3649   1668    -46    161    -46       C  
ATOM   1764  O   ILE C   4      18.532  16.051  41.110  1.00 19.08           O  
ANISOU 1764  O   ILE C   4     1973   3450   1824    299    140    526       O  
ATOM   1765  CB  ILE C   4      17.806  15.508  38.367  1.00 23.48           C  
ANISOU 1765  CB  ILE C   4     2438   4916   1566   -221   -634    428       C  
ATOM   1766  CG1 ILE C   4      16.855  15.598  37.167  1.00 23.16           C  
ANISOU 1766  CG1 ILE C   4     2409   4975   1415    -56   -212    185       C  
ATOM   1767  CG2 ILE C   4      19.113  14.896  38.003  1.00 24.16           C  
ANISOU 1767  CG2 ILE C   4     1816   5644   1720    121    -30    453       C  
ATOM   1768  CD1 ILE C   4      17.457  16.327  35.982  1.00 32.19           C  
ANISOU 1768  CD1 ILE C   4     5271   5587   1374  -1833   1063     79       C  
ATOM   1769  N   ASN C   5      18.389  13.837  41.430  1.00 17.49           N  
ANISOU 1769  N   ASN C   5     1147   3471   2028   -438   -250    212       N  
ATOM   1770  CA  ASN C   5      19.236  13.876  42.626  1.00 17.47           C  
ANISOU 1770  CA  ASN C   5      981   3596   2061     19   -621    677       C  
ATOM   1771  C   ASN C   5      20.110  12.644  42.776  1.00 16.67           C  
ANISOU 1771  C   ASN C   5     1707   3280   1347   -444   -471    648       C  
ATOM   1772  O   ASN C   5      20.549  12.357  43.906  1.00 17.36           O  
ANISOU 1772  O   ASN C   5     1615   3755   1225    -31   -103    766       O  
ATOM   1773  CB  ASN C   5      18.412  14.058  43.896  1.00 17.88           C  
ANISOU 1773  CB  ASN C   5     1314   3470   2012    153   -173    368       C  
ATOM   1774  CG  ASN C   5      17.592  12.836  44.239  1.00 18.14           C  
ANISOU 1774  CG  ASN C   5      770   3931   2192    -49    742    119       C  
ATOM   1775  OD1 ASN C   5      17.358  11.980  43.375  1.00 23.60           O  
ANISOU 1775  OD1 ASN C   5     2430   4466   2070  -1397    394   -229       O  
ATOM   1776  ND2 ASN C   5      17.155  12.725  45.481  1.00 22.14           N  
ANISOU 1776  ND2 ASN C   5     2413   3906   2094   -727    315    398       N  
ATOM   1777  N   THR C   6      20.414  11.956  41.690  1.00 16.34           N  
ANISOU 1777  N   THR C   6     1626   3294   1288   -532   -548    602       N  
ATOM   1778  CA  THR C   6      21.345  10.815  41.750  1.00 17.42           C  
ANISOU 1778  CA  THR C   6     1906   3146   1567   -489   -629    187       C  
ATOM   1779  C   THR C   6      22.721  11.241  41.206  1.00 14.55           C  
ANISOU 1779  C   THR C   6     2133   2292   1103   -441   -742    273       C  
ATOM   1780  O   THR C   6      22.858  12.262  40.540  1.00 14.00           O  
ANISOU 1780  O   THR C   6     1761   2391   1167     80   -363    -46       O  
ATOM   1781  CB  THR C   6      20.832   9.691  40.828  1.00 17.26           C  
ANISOU 1781  CB  THR C   6     1751   3203   1605   -521   -493    551       C  
ATOM   1782  OG1 THR C   6      20.734  10.225  39.500  1.00 18.36           O  
ANISOU 1782  OG1 THR C   6     2657   2668   1651   -675   -494     80       O  
ATOM   1783  CG2 THR C   6      19.489   9.169  41.225  1.00 18.49           C  
ANISOU 1783  CG2 THR C   6     1770   3159   2095   -499   -505    398       C  
ATOM   1784  N   PHE C   7      23.760  10.490  41.530  1.00 14.51           N  
ANISOU 1784  N   PHE C   7     2010   2377   1125     77   -703    236       N  
ATOM   1785  CA  PHE C   7      25.111  10.824  41.081  1.00 13.49           C  
ANISOU 1785  CA  PHE C   7     1965   1816   1345    346   -587    165       C  
ATOM   1786  C   PHE C   7      25.191  11.010  39.583  1.00 12.98           C  
ANISOU 1786  C   PHE C   7     1884   1679   1368    168   -671    352       C  
ATOM   1787  O   PHE C   7      25.701  12.013  39.051  1.00 13.67           O  
ANISOU 1787  O   PHE C   7     2125   1689   1379      7     94    275       O  
ATOM   1788  CB  PHE C   7      26.133   9.805  41.545  1.00 14.48           C  
ANISOU 1788  CB  PHE C   7     2379   1622   1502    354   -488    328       C  
ATOM   1789  CG  PHE C   7      26.552   9.924  42.994  1.00 14.04           C  
ANISOU 1789  CG  PHE C   7     1746   2059   1529    562   -396   -156       C  
ATOM   1790  CD1 PHE C   7      27.255  11.047  43.428  1.00 14.19           C  
ANISOU 1790  CD1 PHE C   7     1685   2144   1562    620      6   -373       C  
ATOM   1791  CD2 PHE C   7      26.255   8.931  43.916  1.00 15.38           C  
ANISOU 1791  CD2 PHE C   7     2158   2305   1380    321   -175    201       C  
ATOM   1792  CE1 PHE C   7      27.620  11.180  44.743  1.00 16.06           C  
ANISOU 1792  CE1 PHE C   7     1634   2899   1569    336   -335   -455       C  
ATOM   1793  CE2 PHE C   7      26.647   9.059  45.252  1.00 16.19           C  
ANISOU 1793  CE2 PHE C   7     1940   2787   1425    419    -38     94       C  
ATOM   1794  CZ  PHE C   7      27.318  10.187  45.663  1.00 15.68           C  
ANISOU 1794  CZ  PHE C   7     1365   3169   1423    323   -255   -175       C  
ATOM   1795  N   ASP C   8      24.692   9.987  38.861  1.00 14.62           N  
ANISOU 1795  N   ASP C   8     2296   1919   1340   -111    -37   -122       N  
ATOM   1796  CA  ASP C   8      24.801  10.050  37.400  1.00 16.15           C  
ANISOU 1796  CA  ASP C   8     2556   2267   1313      9   -227   -199       C  
ATOM   1797  C   ASP C   8      23.921  11.140  36.823  1.00 15.14           C  
ANISOU 1797  C   ASP C   8     2177   2340   1237    -13    -95      3       C  
ATOM   1798  O   ASP C   8      24.300  11.873  35.896  1.00 15.76           O  
ANISOU 1798  O   ASP C   8     2355   2230   1403   -290   -325     -2       O  
ATOM   1799  CB  ASP C   8      24.469   8.693  36.795  1.00 21.52           C  
ANISOU 1799  CB  ASP C   8     4606   2216   1354   -367    138   -798       C  
ATOM   1800  CG  ASP C   8      25.585   7.681  36.963  1.00 25.54           C  
ANISOU 1800  CG  ASP C   8     4932   2040   2732    -75   -463   -264       C  
ATOM   1801  OD1 ASP C   8      26.729   7.994  36.581  1.00 26.53           O  
ANISOU 1801  OD1 ASP C   8     3753   3192   3137    934   -968    182       O  
ATOM   1802  OD2 ASP C   8      25.321   6.599  37.541  1.00 29.91           O  
ANISOU 1802  OD2 ASP C   8     6415   1994   2955    -49   -455    538       O  
ATOM   1803  N   GLY C   9      22.704  11.275  37.382  1.00 16.19           N  
ANISOU 1803  N   GLY C   9     2509   2204   1438   -471   -344     30       N  
ATOM   1804  CA  GLY C   9      21.786  12.267  36.815  1.00 15.86           C  
ANISOU 1804  CA  GLY C   9     2067   2406   1555   -690   -158    438       C  
ATOM   1805  C   GLY C   9      22.302  13.664  37.001  1.00 12.99           C  
ANISOU 1805  C   GLY C   9     1554   2244   1138   -213   -184   1118       C  
ATOM   1806  O   GLY C   9      22.210  14.499  36.096  1.00 13.69           O  
ANISOU 1806  O   GLY C   9     1746   2392   1064   -238   -563    628       O  
ATOM   1807  N   VAL C  10      22.812  13.967  38.188  1.00 12.78           N  
ANISOU 1807  N   VAL C  10     1653   2109   1094      8   -393    190       N  
ATOM   1808  CA  VAL C  10      23.303  15.318  38.420  1.00 11.66           C  
ANISOU 1808  CA  VAL C  10     1489   1964    976    274    -86    281       C  
ATOM   1809  C   VAL C  10      24.591  15.580  37.679  1.00 10.98           C  
ANISOU 1809  C   VAL C  10     1578   1649    946    258   -156    449       C  
ATOM   1810  O   VAL C  10      24.757  16.698  37.101  1.00 11.99           O  
ANISOU 1810  O   VAL C  10     1874   1619   1062    276     12    272       O  
ATOM   1811  CB  VAL C  10      23.397  15.663  39.912  1.00 11.46           C  
ANISOU 1811  CB  VAL C  10     1004   2414    938     35   -394     84       C  
ATOM   1812  CG1 VAL C  10      23.944  17.060  40.135  1.00 13.25           C  
ANISOU 1812  CG1 VAL C  10     1464   2462   1107   -281   -119     40       C  
ATOM   1813  CG2 VAL C  10      22.023  15.484  40.577  1.00 12.23           C  
ANISOU 1813  CG2 VAL C  10      902   2612   1132     -3     16    416       C  
ATOM   1814  N   ALA C  11      25.492  14.613  37.641  1.00 11.19           N  
ANISOU 1814  N   ALA C  11     1678   1569   1006     79    -53    326       N  
ATOM   1815  CA  ALA C  11      26.765  14.785  36.905  1.00 11.07           C  
ANISOU 1815  CA  ALA C  11     1792   1375   1039    -60     34    139       C  
ATOM   1816  C   ALA C  11      26.502  15.146  35.464  1.00 11.01           C  
ANISOU 1816  C   ALA C  11     1486   1627   1070     80    -21    373       C  
ATOM   1817  O   ALA C  11      27.162  16.038  34.875  1.00 12.04           O  
ANISOU 1817  O   ALA C  11     1689   1800   1087    -51    281    205       O  
ATOM   1818  CB  ALA C  11      27.645  13.559  37.047  1.00 11.74           C  
ANISOU 1818  CB  ALA C  11     1776   1522   1161    193   -245     24       C  
ATOM   1819  N   ASP C  12      25.605  14.389  34.828  1.00 11.94           N  
ANISOU 1819  N   ASP C  12     1390   2161    985     -5   -110      7       N  
ATOM   1820  CA  ASP C  12      25.339  14.603  33.418  1.00 12.81           C  
ANISOU 1820  CA  ASP C  12     1597   2341    927    495     26    -83       C  
ATOM   1821  C   ASP C  12      24.666  15.944  33.156  1.00 12.93           C  
ANISOU 1821  C   ASP C  12     1773   2292    847    310   -328    132       C  
ATOM   1822  O   ASP C  12      24.972  16.602  32.162  1.00 13.71           O  
ANISOU 1822  O   ASP C  12     2026   2367    815    414   -119    467       O  
ATOM   1823  CB  ASP C  12      24.589  13.453  32.817  1.00 16.35           C  
ANISOU 1823  CB  ASP C  12     3237   2395    581    -97   -538   -118       C  
ATOM   1824  CG  ASP C  12      25.392  12.176  32.661  1.00 21.02           C  
ANISOU 1824  CG  ASP C  12     4246   2234   1508     81   -150   -110       C  
ATOM   1825  OD1 ASP C  12      26.617  12.263  32.521  1.00 22.82           O  
ANISOU 1825  OD1 ASP C  12     3668   2088   2913   1146   -749   -130       O  
ATOM   1826  OD2 ASP C  12      24.774  11.106  32.598  1.00 27.91           O  
ANISOU 1826  OD2 ASP C  12     5980   2291   2333   -730    596   -225       O  
ATOM   1827  N   TYR C  13      23.770  16.346  34.051  1.00 13.21           N  
ANISOU 1827  N   TYR C  13     1730   2236   1051     94     11    244       N  
ATOM   1828  CA  TYR C  13      23.066  17.636  33.892  1.00 13.01           C  
ANISOU 1828  CA  TYR C  13     1425   2381   1137    191    287    384       C  
ATOM   1829  C   TYR C  13      24.054  18.783  34.003  1.00 12.45           C  
ANISOU 1829  C   TYR C  13     1548   2229    953    228    108    497       C  
ATOM   1830  O   TYR C  13      24.026  19.718  33.197  1.00 12.90           O  
ANISOU 1830  O   TYR C  13     1607   2228   1066    217     83    575       O  
ATOM   1831  CB  TYR C  13      21.992  17.726  34.986  1.00 13.44           C  
ANISOU 1831  CB  TYR C  13     1457   2526   1122    144   -227    840       C  
ATOM   1832  CG  TYR C  13      20.967  18.795  34.741  1.00 13.36           C  
ANISOU 1832  CG  TYR C  13     1279   2611   1186    476   -352    813       C  
ATOM   1833  CD1 TYR C  13      21.197  20.098  35.154  1.00 15.67           C  
ANISOU 1833  CD1 TYR C  13     2434   2544    975    128    517     68       C  
ATOM   1834  CD2 TYR C  13      19.770  18.521  34.077  1.00 15.24           C  
ANISOU 1834  CD2 TYR C  13     1116   2816   1861    384   -168    602       C  
ATOM   1835  CE1 TYR C  13      20.284  21.102  34.941  1.00 16.80           C  
ANISOU 1835  CE1 TYR C  13     2762   2468   1152    182    321   -119       C  
ATOM   1836  CE2 TYR C  13      18.832  19.541  33.871  1.00 15.76           C  
ANISOU 1836  CE2 TYR C  13     1204   2800   1986    517   -513    617       C  
ATOM   1837  CZ  TYR C  13      19.092  20.810  34.284  1.00 17.22           C  
ANISOU 1837  CZ  TYR C  13     2118   2768   1655    626   -302    280       C  
ATOM   1838  OH  TYR C  13      18.173  21.833  34.124  1.00 21.48           O  
ANISOU 1838  OH  TYR C  13     2293   2798   3072   1003     -9    614       O  
ATOM   1839  N   LEU C  14      24.960  18.699  34.986  1.00 12.04           N  
ANISOU 1839  N   LEU C  14     1322   2176   1077    421   -137    383       N  
ATOM   1840  CA  LEU C  14      25.987  19.714  35.143  1.00 11.62           C  
ANISOU 1840  CA  LEU C  14     1495   2041    880    342    -15    370       C  
ATOM   1841  C   LEU C  14      26.845  19.889  33.906  1.00 11.78           C  
ANISOU 1841  C   LEU C  14     1976   1686    813    189      0    780       C  
ATOM   1842  O   LEU C  14      27.121  21.001  33.433  1.00 10.83           O  
ANISOU 1842  O   LEU C  14     1770   1628    717    498    277    475       O  
ATOM   1843  CB  LEU C  14      26.868  19.463  36.350  1.00 11.16           C  
ANISOU 1843  CB  LEU C  14     1475   1902    862    489   -189    101       C  
ATOM   1844  CG  LEU C  14      26.274  19.735  37.727  1.00 11.97           C  
ANISOU 1844  CG  LEU C  14     1791   1896    863    440    -36     25       C  
ATOM   1845  CD1 LEU C  14      27.095  19.016  38.780  1.00 11.94           C  
ANISOU 1845  CD1 LEU C  14     1665   2002    869    -41    165    -71       C  
ATOM   1846  CD2 LEU C  14      26.198  21.243  37.993  1.00 13.38           C  
ANISOU 1846  CD2 LEU C  14     2316   1924    845    216    286    -45       C  
ATOM   1847  N   GLN C  15      27.386  18.782  33.391  1.00 12.36           N  
ANISOU 1847  N   GLN C  15     2187   1619    890    318    152    117       N  
ATOM   1848  CA  GLN C  15      28.332  18.912  32.283  1.00 11.92           C  
ANISOU 1848  CA  GLN C  15     1746   1686   1098    432    423    515       C  
ATOM   1849  C   GLN C  15      27.648  19.358  31.000  1.00 12.15           C  
ANISOU 1849  C   GLN C  15     1967   1664    988    424    708    309       C  
ATOM   1850  O   GLN C  15      28.313  19.885  30.096  1.00 13.29           O  
ANISOU 1850  O   GLN C  15     1866   2166   1019    313    560    618       O  
ATOM   1851  CB  GLN C  15      29.014  17.543  32.041  1.00 13.86           C  
ANISOU 1851  CB  GLN C  15     1971   1717   1580    854    289    439       C  
ATOM   1852  CG  GLN C  15      29.965  17.123  33.120  1.00 14.39           C  
ANISOU 1852  CG  GLN C  15     2085   1748   1634    928    132    396       C  
ATOM   1853  CD  GLN C  15      30.988  16.110  32.647  1.00 13.55           C  
ANISOU 1853  CD  GLN C  15     1719   1845   1583    668   -121    699       C  
ATOM   1854  OE1 GLN C  15      30.651  15.074  32.061  1.00 16.87           O  
ANISOU 1854  OE1 GLN C  15     2192   1488   2730    452    271    -77       O  
ATOM   1855  NE2 GLN C  15      32.262  16.362  32.971  1.00 15.85           N  
ANISOU 1855  NE2 GLN C  15     1486   3085   1451    520   -375    211       N  
ATOM   1856  N   THR C  16      26.358  19.088  30.876  1.00 12.22           N  
ANISOU 1856  N   THR C  16     1722   1774   1148    664    505    448       N  
ATOM   1857  CA  THR C  16      25.586  19.411  29.689  1.00 12.54           C  
ANISOU 1857  CA  THR C  16     1800   1757   1207    665   -187    651       C  
ATOM   1858  C   THR C  16      25.019  20.811  29.720  1.00 12.08           C  
ANISOU 1858  C   THR C  16     1960   1767    865    765    -96    703       C  
ATOM   1859  O   THR C  16      25.100  21.538  28.714  1.00 13.10           O  
ANISOU 1859  O   THR C  16     2349   1833    795    263   -309    321       O  
ATOM   1860  CB  THR C  16      24.477  18.386  29.439  1.00 13.06           C  
ANISOU 1860  CB  THR C  16     1800   1916   1247    559   -428   -214       C  
ATOM   1861  OG1 THR C  16      25.089  17.065  29.429  1.00 17.17           O  
ANISOU 1861  OG1 THR C  16     3341   1711   1471    407   -101     24       O  
ATOM   1862  CG2 THR C  16      23.758  18.556  28.148  1.00 15.62           C  
ANISOU 1862  CG2 THR C  16     2789   2045   1101    -88   -306    181       C  
ATOM   1863  N   TYR C  17      24.388  21.214  30.825  1.00 11.73           N  
ANISOU 1863  N   TYR C  17     2007   1649    802    556    251    172       N  
ATOM   1864  CA  TYR C  17      23.647  22.448  30.925  1.00 12.70           C  
ANISOU 1864  CA  TYR C  17     1927   1615   1283    290   -168     36       C  
ATOM   1865  C   TYR C  17      24.272  23.508  31.798  1.00 12.30           C  
ANISOU 1865  C   TYR C  17     1890   1492   1293    297     76   -224       C  
ATOM   1866  O   TYR C  17      23.825  24.673  31.824  1.00 14.14           O  
ANISOU 1866  O   TYR C  17     2207   1557   1608    459    260    150       O  
ATOM   1867  CB  TYR C  17      22.196  22.146  31.407  1.00 16.08           C  
ANISOU 1867  CB  TYR C  17     1812   1862   2437    185   -402    -67       C  
ATOM   1868  CG  TYR C  17      21.489  21.166  30.479  1.00 16.15           C  
ANISOU 1868  CG  TYR C  17     1878   1820   2437    321   -674    183       C  
ATOM   1869  CD1 TYR C  17      21.249  21.509  29.144  1.00 20.78           C  
ANISOU 1869  CD1 TYR C  17     3008   2587   2301    -41  -1116    477       C  
ATOM   1870  CD2 TYR C  17      21.056  19.937  30.922  1.00 19.16           C  
ANISOU 1870  CD2 TYR C  17     2441   1936   2903   -190   -581    147       C  
ATOM   1871  CE1 TYR C  17      20.621  20.614  28.309  1.00 23.62           C  
ANISOU 1871  CE1 TYR C  17     3624   3082   2267   -540  -1105    488       C  
ATOM   1872  CE2 TYR C  17      20.396  19.049  30.092  1.00 22.16           C  
ANISOU 1872  CE2 TYR C  17     3373   2130   2918   -642    -69    -10       C  
ATOM   1873  CZ  TYR C  17      20.170  19.401  28.786  1.00 23.99           C  
ANISOU 1873  CZ  TYR C  17     3362   2934   2820   -573   -872    111       C  
ATOM   1874  OH  TYR C  17      19.512  18.518  27.941  1.00 31.42           O  
ANISOU 1874  OH  TYR C  17     4681   4292   2966  -2283   -638      2       O  
ATOM   1875  N   HIS C  18      25.317  23.173  32.546  1.00 12.28           N  
ANISOU 1875  N   HIS C  18     1894   1626   1148    385    112    169       N  
ATOM   1876  CA  HIS C  18      26.160  24.110  33.214  1.00 12.30           C  
ANISOU 1876  CA  HIS C  18     2026   1647   1002    339    618    195       C  
ATOM   1877  C   HIS C  18      25.558  24.813  34.388  1.00 12.62           C  
ANISOU 1877  C   HIS C  18     2159   1526   1109    928    299    177       C  
ATOM   1878  O   HIS C  18      25.890  25.972  34.710  1.00 14.82           O  
ANISOU 1878  O   HIS C  18     2752   1594   1285    601    571      6       O  
ATOM   1879  CB  HIS C  18      26.787  25.124  32.214  1.00 11.67           C  
ANISOU 1879  CB  HIS C  18     1928   1405   1103    497    193    -79       C  
ATOM   1880  CG  HIS C  18      27.328  24.434  31.002  1.00 11.72           C  
ANISOU 1880  CG  HIS C  18     2170   1273   1012    376   -361     -9       C  
ATOM   1881  ND1 HIS C  18      26.924  24.722  29.739  1.00 10.77           N  
ANISOU 1881  ND1 HIS C  18     1579   1474   1038    540   -251    -91       N  
ATOM   1882  CD2 HIS C  18      28.048  23.284  30.920  1.00 12.56           C  
ANISOU 1882  CD2 HIS C  18     2579   1255    938    647    123   -260       C  
ATOM   1883  CE1 HIS C  18      27.454  23.843  28.898  1.00 12.10           C  
ANISOU 1883  CE1 HIS C  18     2386   1200   1012    566    379    119       C  
ATOM   1884  NE2 HIS C  18      28.165  22.962  29.587  1.00 12.32           N  
ANISOU 1884  NE2 HIS C  18     2549   1232    902    413    515    -92       N  
ATOM   1885  N   LYS C  19      24.642  24.130  35.040  1.00 14.73           N  
ANISOU 1885  N   LYS C  19     2738   2160    698    298    606    366       N  
ATOM   1886  CA  LYS C  19      23.929  24.589  36.215  1.00 15.83           C  
ANISOU 1886  CA  LYS C  19     3280   2006    727    433    567    492       C  
ATOM   1887  C   LYS C  19      23.349  23.359  36.925  1.00 13.17           C  
ANISOU 1887  C   LYS C  19     2167   2111    725    840    620    424       C  
ATOM   1888  O   LYS C  19      23.255  22.299  36.314  1.00 14.03           O  
ANISOU 1888  O   LYS C  19     2390   2082    860    479    117    110       O  
ATOM   1889  CB  LYS C  19      22.818  25.569  35.849  1.00 18.45           C  
ANISOU 1889  CB  LYS C  19     3319   1850   1843    613    845    685       C  
ATOM   1890  CG  LYS C  19      21.668  24.995  35.043  1.00 22.21           C  
ANISOU 1890  CG  LYS C  19     2584   2864   2990    460    674    291       C  
ATOM   1891  CD  LYS C  19      20.733  26.091  34.490  1.00 22.53           C  
ANISOU 1891  CD  LYS C  19     2308   3091   3160    600     46    550       C  
ATOM   1892  CE  LYS C  19      19.632  25.445  33.668  1.00 25.38           C  
ANISOU 1892  CE  LYS C  19     2142   4000   3501    269    -32    518       C  
ATOM   1893  NZ  LYS C  19      18.403  26.238  33.502  1.00 32.91           N  
ANISOU 1893  NZ  LYS C  19     2282   3839   6384   -685   -429   -576       N  
ATOM   1894  N   LEU C  20      22.988  23.496  38.178  1.00 12.82           N  
ANISOU 1894  N   LEU C  20     1481   2599    792    949    476    541       N  
ATOM   1895  CA  LEU C  20      22.263  22.435  38.864  1.00 14.15           C  
ANISOU 1895  CA  LEU C  20     1920   2579    879    570    536    897       C  
ATOM   1896  C   LEU C  20      20.821  22.356  38.392  1.00 15.16           C  
ANISOU 1896  C   LEU C  20     1606   3125   1029    733    355    585       C  
ATOM   1897  O   LEU C  20      20.221  23.381  37.998  1.00 16.80           O  
ANISOU 1897  O   LEU C  20     1581   3036   1769    775    375    496       O  
ATOM   1898  CB  LEU C  20      22.298  22.664  40.379  1.00 14.27           C  
ANISOU 1898  CB  LEU C  20     2179   2300    945    340    298    429       C  
ATOM   1899  CG  LEU C  20      23.633  22.376  41.073  1.00 14.06           C  
ANISOU 1899  CG  LEU C  20     1817   2669    857    563   -100    446       C  
ATOM   1900  CD1 LEU C  20      23.589  22.871  42.520  1.00 18.44           C  
ANISOU 1900  CD1 LEU C  20     2990   3295    723    370    133     97       C  
ATOM   1901  CD2 LEU C  20      23.908  20.864  41.088  1.00 15.14           C  
ANISOU 1901  CD2 LEU C  20     1148   2700   1905    418    -72   1167       C  
ATOM   1902  N   PRO C  21      20.222  21.183  38.539  1.00 15.36           N  
ANISOU 1902  N   PRO C  21     1539   3202   1095    675    289    959       N  
ATOM   1903  CA  PRO C  21      18.774  21.040  38.308  1.00 17.20           C  
ANISOU 1903  CA  PRO C  21     1327   3669   1539    769    567    791       C  
ATOM   1904  C   PRO C  21      17.962  21.883  39.290  1.00 17.45           C  
ANISOU 1904  C   PRO C  21     1063   3952   1615   1122    298   1249       C  
ATOM   1905  O   PRO C  21      18.445  22.296  40.336  1.00 17.49           O  
ANISOU 1905  O   PRO C  21     1555   3502   1590   1309    329    683       O  
ATOM   1906  CB  PRO C  21      18.517  19.575  38.541  1.00 19.86           C  
ANISOU 1906  CB  PRO C  21     1532   3728   2287    415    -11    437       C  
ATOM   1907  CG  PRO C  21      19.816  18.876  38.509  1.00 19.20           C  
ANISOU 1907  CG  PRO C  21     1915   3378   2003    184   -846    900       C  
ATOM   1908  CD  PRO C  21      20.839  19.887  38.881  1.00 17.03           C  
ANISOU 1908  CD  PRO C  21     1676   3132   1662    431   -351    796       C  
ATOM   1909  N   ASP C  22      16.679  22.025  38.976  1.00 20.28           N  
ANISOU 1909  N   ASP C  22      845   4238   2622   1307    156   1095       N  
ATOM   1910  CA  ASP C  22      15.750  22.910  39.567  1.00 20.54           C  
ANISOU 1910  CA  ASP C  22     1205   3925   2674   1625    220   1592       C  
ATOM   1911  C   ASP C  22      15.373  22.605  41.007  1.00 23.28           C  
ANISOU 1911  C   ASP C  22     1852   4522   2471   1281    879    882       C  
ATOM   1912  O   ASP C  22      14.791  23.441  41.678  1.00 26.16           O  
ANISOU 1912  O   ASP C  22     3160   4502   2279   1972    998    931       O  
ATOM   1913  CB  ASP C  22      14.477  23.040  38.721  1.00 20.67           C  
ANISOU 1913  CB  ASP C  22     1626   3529   2699   1257   -372   1417       C  
ATOM   1914  CG  ASP C  22      14.745  23.493  37.311  1.00 26.40           C  
ANISOU 1914  CG  ASP C  22     3055   4074   2536    483   -838   1236       C  
ATOM   1915  OD1 ASP C  22      15.667  24.349  37.108  1.00 34.24           O  
ANISOU 1915  OD1 ASP C  22     4571   5162   2800  -1053    575   1062       O  
ATOM   1916  OD2 ASP C  22      14.019  23.101  36.381  1.00 36.82           O  
ANISOU 1916  OD2 ASP C  22     4446   6405   2627  -1337   -213     37       O  
ATOM   1917  N   ASN C  23      15.730  21.421  41.462  1.00 21.49           N  
ANISOU 1917  N   ASN C  23     1540   4598   2027   1156    493    851       N  
ATOM   1918  CA  ASN C  23      15.420  20.971  42.790  1.00 20.93           C  
ANISOU 1918  CA  ASN C  23      956   4991   2005    750    466    774       C  
ATOM   1919  C   ASN C  23      16.477  21.347  43.820  1.00 20.78           C  
ANISOU 1919  C   ASN C  23     1346   4525   2025    452    256    866       C  
ATOM   1920  O   ASN C  23      16.292  20.999  44.993  1.00 22.29           O  
ANISOU 1920  O   ASN C  23     1523   5006   1940    243    -88   1092       O  
ATOM   1921  CB  ASN C  23      15.129  19.474  42.829  1.00 22.01           C  
ANISOU 1921  CB  ASN C  23     1477   5179   1707    -23    181    661       C  
ATOM   1922  CG  ASN C  23      16.221  18.631  42.220  1.00 22.09           C  
ANISOU 1922  CG  ASN C  23     2149   4698   1547   -182     61    896       C  
ATOM   1923  OD1 ASN C  23      16.334  18.580  40.975  1.00 24.39           O  
ANISOU 1923  OD1 ASN C  23     3214   4178   1537   -652    135    390       O  
ATOM   1924  ND2 ASN C  23      16.949  17.880  42.998  1.00 23.81           N  
ANISOU 1924  ND2 ASN C  23     2571   4529   1613    140     26    218       N  
ATOM   1925  N   TYR C  24      17.481  22.117  43.488  1.00 19.11           N  
ANISOU 1925  N   TYR C  24     1393   3901   1967    631    652    917       N  
ATOM   1926  CA  TYR C  24      18.539  22.487  44.414  1.00 15.87           C  
ANISOU 1926  CA  TYR C  24     1066   2858   2105   1207    884    576       C  
ATOM   1927  C   TYR C  24      18.433  23.925  44.895  1.00 17.49           C  
ANISOU 1927  C   TYR C  24     1682   2810   2152   1351    699    861       C  
ATOM   1928  O   TYR C  24      18.059  24.841  44.144  1.00 21.81           O  
ANISOU 1928  O   TYR C  24     3343   2811   2132   1740    158   1047       O  
ATOM   1929  CB  TYR C  24      19.928  22.287  43.735  1.00 14.87           C  
ANISOU 1929  CB  TYR C  24     1429   2769   1451   1033   -102   1083       C  
ATOM   1930  CG  TYR C  24      20.354  20.835  43.755  1.00 13.51           C  
ANISOU 1930  CG  TYR C  24     1189   2752   1194    868    582   1097       C  
ATOM   1931  CD1 TYR C  24      20.901  20.240  44.879  1.00 14.39           C  
ANISOU 1931  CD1 TYR C  24     1582   2684   1203    740    -96    877       C  
ATOM   1932  CD2 TYR C  24      20.104  20.044  42.633  1.00 15.33           C  
ANISOU 1932  CD2 TYR C  24     1930   2718   1177    719     -6   1281       C  
ATOM   1933  CE1 TYR C  24      21.224  18.886  44.889  1.00 13.93           C  
ANISOU 1933  CE1 TYR C  24     1499   2680   1114    763    232    776       C  
ATOM   1934  CE2 TYR C  24      20.397  18.700  42.648  1.00 14.08           C  
ANISOU 1934  CE2 TYR C  24     1424   2796   1130    898    271    544       C  
ATOM   1935  CZ  TYR C  24      21.006  18.137  43.757  1.00 14.02           C  
ANISOU 1935  CZ  TYR C  24     1486   2741   1099    618    348    799       C  
ATOM   1936  OH  TYR C  24      21.315  16.802  43.732  1.00 14.49           O  
ANISOU 1936  OH  TYR C  24     1851   2647   1009    264   -459    501       O  
ATOM   1937  N   ILE C  25      18.702  24.127  46.177  1.00 18.54           N  
ANISOU 1937  N   ILE C  25     1830   3093   2120   1006    799    533       N  
ATOM   1938  CA  ILE C  25      18.739  25.462  46.790  1.00 17.61           C  
ANISOU 1938  CA  ILE C  25     1509   3040   2143   1213   1068    990       C  
ATOM   1939  C   ILE C  25      20.011  25.565  47.636  1.00 17.17           C  
ANISOU 1939  C   ILE C  25     1608   2622   2294   1094    765    982       C  
ATOM   1940  O   ILE C  25      20.483  24.545  48.163  1.00 17.50           O  
ANISOU 1940  O   ILE C  25     1908   2564   2178    945    613    744       O  
ATOM   1941  CB  ILE C  25      17.511  25.744  47.679  1.00 18.39           C  
ANISOU 1941  CB  ILE C  25     1391   3306   2291   1095   1069   1032       C  
ATOM   1942  CG1 ILE C  25      17.235  24.700  48.745  1.00 21.58           C  
ANISOU 1942  CG1 ILE C  25     2289   3738   2173    348   1733    748       C  
ATOM   1943  CG2 ILE C  25      16.301  26.001  46.804  1.00 19.92           C  
ANISOU 1943  CG2 ILE C  25     1292   3774   2504    793    660    670       C  
ATOM   1944  CD1 ILE C  25      16.072  25.053  49.678  1.00 21.89           C  
ANISOU 1944  CD1 ILE C  25     2291   3859   2167    473    929    905       C  
ATOM   1945  N   THR C  26      20.594  26.753  47.701  1.00 17.97           N  
ANISOU 1945  N   THR C  26     1650   2468   2711   1229    833   1131       N  
ATOM   1946  CA  THR C  26      21.779  26.957  48.512  1.00 18.09           C  
ANISOU 1946  CA  THR C  26     1901   2164   2809    870    949    643       C  
ATOM   1947  C   THR C  26      21.449  26.946  50.004  1.00 18.90           C  
ANISOU 1947  C   THR C  26     2173   2221   2788    744   1108    511       C  
ATOM   1948  O   THR C  26      20.328  27.120  50.410  1.00 18.98           O  
ANISOU 1948  O   THR C  26     1898   2748   2564    930    899    956       O  
ATOM   1949  CB  THR C  26      22.493  28.268  48.193  1.00 21.25           C  
ANISOU 1949  CB  THR C  26     3090   2148   2836    275   1530    567       C  
ATOM   1950  OG1 THR C  26      21.668  29.373  48.547  1.00 22.79           O  
ANISOU 1950  OG1 THR C  26     3109   2212   3337    790   1674    266       O  
ATOM   1951  CG2 THR C  26      22.864  28.369  46.736  1.00 23.39           C  
ANISOU 1951  CG2 THR C  26     4058   2052   2777    -54   1388    819       C  
ATOM   1952  N   LYS C  27      22.506  26.803  50.832  1.00 19.67           N  
ANISOU 1952  N   LYS C  27     2013   2656   2803    713   1030    249       N  
ATOM   1953  CA  LYS C  27      22.314  26.823  52.277  1.00 22.56           C  
ANISOU 1953  CA  LYS C  27     3142   2728   2702    917   1489    -36       C  
ATOM   1954  C   LYS C  27      21.649  28.110  52.737  1.00 22.56           C  
ANISOU 1954  C   LYS C  27     3136   2708   2728    932   1290    504       C  
ATOM   1955  O   LYS C  27      20.763  28.107  53.587  1.00 22.72           O  
ANISOU 1955  O   LYS C  27     2826   2929   2878   1165   1502    244       O  
ATOM   1956  CB  LYS C  27      23.639  26.636  53.022  1.00 22.24           C  
ANISOU 1956  CB  LYS C  27     3328   2609   2512    898    766    -68       C  
ATOM   1957  CG  LYS C  27      24.131  25.197  53.074  1.00 24.37           C  
ANISOU 1957  CG  LYS C  27     3494   2644   3120   1388    645   -197       C  
ATOM   1958  CD  LYS C  27      25.520  25.079  53.715  1.00 25.64           C  
ANISOU 1958  CD  LYS C  27     3384   2722   3634   1495    422    -87       C  
ATOM   1959  CE  LYS C  27      26.592  24.921  52.657  1.00 27.88           C  
ANISOU 1959  CE  LYS C  27     3165   3695   3732   1123     53    -97       C  
ATOM   1960  NZ  LYS C  27      27.973  25.068  53.135  1.00 36.22           N  
ANISOU 1960  NZ  LYS C  27     3667   4878   5215   -318     17   -390       N  
ATOM   1961  N   SER C  28      22.077  29.238  52.195  1.00 23.44           N  
ANISOU 1961  N   SER C  28     2834   2720   3354    972   1811    221       N  
ATOM   1962  CA  SER C  28      21.506  30.521  52.675  1.00 26.61           C  
ANISOU 1962  CA  SER C  28     3185   2663   4261   1020   2308    202       C  
ATOM   1963  C   SER C  28      20.080  30.668  52.210  1.00 26.09           C  
ANISOU 1963  C   SER C  28     3093   2556   4264   1291   2319    489       C  
ATOM   1964  O   SER C  28      19.219  31.175  52.950  1.00 26.24           O  
ANISOU 1964  O   SER C  28     3046   2763   4163   1291   1971    180       O  
ATOM   1965  CB  SER C  28      22.409  31.649  52.152  1.00 27.96           C  
ANISOU 1965  CB  SER C  28     3731   2750   4141    656   1582     21       C  
ATOM   1966  OG  SER C  28      22.383  31.678  50.754  1.00 38.23           O  
ANISOU 1966  OG  SER C  28     5961   4447   4118   -968   2353   -281       O  
ATOM   1967  N   GLU C  29      19.746  30.158  51.017  1.00 25.51           N  
ANISOU 1967  N   GLU C  29     2919   2450   4323   1358   2016   1076       N  
ATOM   1968  CA  GLU C  29      18.344  30.228  50.571  1.00 26.59           C  
ANISOU 1968  CA  GLU C  29     3061   2714   4329   1023   2004   1686       C  
ATOM   1969  C   GLU C  29      17.467  29.318  51.448  1.00 26.43           C  
ANISOU 1969  C   GLU C  29     3015   2732   4295   1101   1271   1855       C  
ATOM   1970  O   GLU C  29      16.352  29.702  51.833  1.00 25.08           O  
ANISOU 1970  O   GLU C  29     2755   2933   3840   1556   1613   1444       O  
ATOM   1971  CB  GLU C  29      18.248  29.741  49.108  1.00 27.56           C  
ANISOU 1971  CB  GLU C  29     2994   3175   4304   1291   2157   1698       C  
ATOM   1972  CG  GLU C  29      18.805  30.722  48.119  1.00 32.53           C  
ANISOU 1972  CG  GLU C  29     4688   3460   4212    828   1678   1653       C  
ATOM   1973  CD  GLU C  29      19.004  30.216  46.721  1.00 37.88           C  
ANISOU 1973  CD  GLU C  29     6447   3839   4106    366   1113   1889       C  
ATOM   1974  OE1 GLU C  29      19.008  29.008  46.467  1.00 35.11           O  
ANISOU 1974  OE1 GLU C  29     5558   3819   3962   1921    455   1602       O  
ATOM   1975  OE2 GLU C  29      19.198  31.085  45.821  1.00 40.65           O  
ANISOU 1975  OE2 GLU C  29     7368   3949   4130    446    888   1515       O  
ATOM   1976  N   ALA C  30      17.983  28.139  51.751  1.00 23.88           N  
ANISOU 1976  N   ALA C  30     2671   2883   3520   1288   1759   1682       N  
ATOM   1977  CA  ALA C  30      17.247  27.172  52.569  1.00 21.66           C  
ANISOU 1977  CA  ALA C  30     1916   2979   3336   1679   1714   1904       C  
ATOM   1978  C   ALA C  30      17.003  27.768  53.946  1.00 22.82           C  
ANISOU 1978  C   ALA C  30     2478   2780   3414   2100   2402   1058       C  
ATOM   1979  O   ALA C  30      15.899  27.701  54.465  1.00 22.79           O  
ANISOU 1979  O   ALA C  30     2648   3200   2811   1974   1823   1027       O  
ATOM   1980  CB  ALA C  30      18.006  25.858  52.650  1.00 18.81           C  
ANISOU 1980  CB  ALA C  30     1459   2930   2756    979    922   1390       C  
ATOM   1981  N   GLN C  31      18.035  28.390  54.517  1.00 25.41           N  
ANISOU 1981  N   GLN C  31     3141   3391   3122   1475   2126    729       N  
ATOM   1982  CA  GLN C  31      17.851  29.009  55.845  1.00 27.81           C  
ANISOU 1982  CA  GLN C  31     4481   2902   3186   1704   2546    629       C  
ATOM   1983  C   GLN C  31      16.779  30.080  55.813  1.00 29.71           C  
ANISOU 1983  C   GLN C  31     4626   2909   3755   2024   3304    821       C  
ATOM   1984  O   GLN C  31      15.951  30.164  56.737  1.00 29.50           O  
ANISOU 1984  O   GLN C  31     4139   3110   3958   2405   2256   1123       O  
ATOM   1985  CB  GLN C  31      19.193  29.583  56.332  1.00 28.16           C  
ANISOU 1985  CB  GLN C  31     5174   2632   2893   1145   2029    184       C  
ATOM   1986  CG  GLN C  31      20.139  28.526  56.880  1.00 30.79           C  
ANISOU 1986  CG  GLN C  31     4393   2863   4443   1336   1318    381       C  
ATOM   1987  CD  GLN C  31      21.593  28.847  56.728  1.00 37.70           C  
ANISOU 1987  CD  GLN C  31     4738   3557   6031    637     14    784       C  
ATOM   1988  OE1 GLN C  31      21.978  29.954  56.365  1.00 47.79           O  
ANISOU 1988  OE1 GLN C  31     6414   3700   8046   -611  -1958    915       O  
ATOM   1989  NE2 GLN C  31      22.462  27.835  56.905  1.00 41.42           N  
ANISOU 1989  NE2 GLN C  31     3813   4051   7875    920    105   -186       N  
ATOM   1990  N   ALA C  32      16.758  30.916  54.783  1.00 29.93           N  
ANISOU 1990  N   ALA C  32     4685   2728   3960   1924   3110   1168       N  
ATOM   1991  CA  ALA C  32      15.800  32.021  54.729  1.00 31.34           C  
ANISOU 1991  CA  ALA C  32     4783   2707   4418   1763   2830   1245       C  
ATOM   1992  C   ALA C  32      14.370  31.523  54.611  1.00 31.40           C  
ANISOU 1992  C   ALA C  32     4274   3403   4255   2087   2311   1193       C  
ATOM   1993  O   ALA C  32      13.413  32.221  54.993  1.00 33.08           O  
ANISOU 1993  O   ALA C  32     4301   3294   4976   2349   2228    872       O  
ATOM   1994  CB  ALA C  32      16.140  32.973  53.618  1.00 30.86           C  
ANISOU 1994  CB  ALA C  32     4668   2579   4479   2077   2290   1604       C  
ATOM   1995  N   LEU C  33      14.212  30.283  54.132  1.00 28.93           N  
ANISOU 1995  N   LEU C  33     3591   3457   3943   2086   2232   1291       N  
ATOM   1996  CA  LEU C  33      12.908  29.710  53.963  1.00 30.40           C  
ANISOU 1996  CA  LEU C  33     3387   4140   4022   2126   1684   1657       C  
ATOM   1997  C   LEU C  33      12.455  28.798  55.049  1.00 28.48           C  
ANISOU 1997  C   LEU C  33     2567   4102   4153   2391   1893   2138       C  
ATOM   1998  O   LEU C  33      11.303  28.300  55.072  1.00 32.85           O  
ANISOU 1998  O   LEU C  33     2546   5263   4674   2065   1993   3065       O  
ATOM   1999  CB  LEU C  33      12.579  29.245  52.591  1.00 32.58           C  
ANISOU 1999  CB  LEU C  33     3842   4430   4106   1540   1521   1238       C  
ATOM   2000  CG  LEU C  33      13.258  27.995  52.047  1.00 32.04           C  
ANISOU 2000  CG  LEU C  33     4060   4350   3764   1402   1195   1542       C  
ATOM   2001  CD1 LEU C  33      12.992  26.795  52.930  1.00 35.19           C  
ANISOU 2001  CD1 LEU C  33     5107   4350   3914   1030   1703    715       C  
ATOM   2002  CD2 LEU C  33      12.837  27.763  50.609  1.00 32.24           C  
ANISOU 2002  CD2 LEU C  33     3498   4929   3822   1050   -159   1593       C  
ATOM   2003  N   GLY C  34      13.284  28.641  56.091  1.00 27.43           N  
ANISOU 2003  N   GLY C  34     3180   3020   4223   2115   2009   1985       N  
ATOM   2004  CA  GLY C  34      12.859  27.976  57.301  1.00 25.20           C  
ANISOU 2004  CA  GLY C  34     2290   2901   4385   1879   2149   1909       C  
ATOM   2005  C   GLY C  34      13.684  26.778  57.684  1.00 21.90           C  
ANISOU 2005  C   GLY C  34     1722   3085   3515   1742   2058   1437       C  
ATOM   2006  O   GLY C  34      13.388  26.147  58.705  1.00 24.06           O  
ANISOU 2006  O   GLY C  34     2492   3501   3148   1300   1933   1575       O  
ATOM   2007  N   TRP C  35      14.677  26.374  56.882  1.00 21.28           N  
ANISOU 2007  N   TRP C  35     1964   2972   3148   1836   1435   1583       N  
ATOM   2008  CA  TRP C  35      15.463  25.160  57.202  1.00 19.94           C  
ANISOU 2008  CA  TRP C  35     1990   2871   2716   1579   1548    821       C  
ATOM   2009  C   TRP C  35      16.291  25.451  58.481  1.00 20.51           C  
ANISOU 2009  C   TRP C  35     2268   2814   2710   1475    716   1050       C  
ATOM   2010  O   TRP C  35      16.995  26.460  58.521  1.00 22.29           O  
ANISOU 2010  O   TRP C  35     2752   2970   2749   1113   1071    469       O  
ATOM   2011  CB  TRP C  35      16.476  24.887  56.081  1.00 19.80           C  
ANISOU 2011  CB  TRP C  35     2033   2765   2725   1498    894    668       C  
ATOM   2012  CG  TRP C  35      17.431  23.763  56.352  1.00 18.07           C  
ANISOU 2012  CG  TRP C  35     2047   2680   2139   1017    888    585       C  
ATOM   2013  CD1 TRP C  35      17.109  22.517  56.789  1.00 18.16           C  
ANISOU 2013  CD1 TRP C  35     1793   2681   2427   1041    671    851       C  
ATOM   2014  CD2 TRP C  35      18.854  23.770  56.185  1.00 17.21           C  
ANISOU 2014  CD2 TRP C  35     2051   2747   1741    915    903    447       C  
ATOM   2015  NE1 TRP C  35      18.223  21.747  56.932  1.00 17.24           N  
ANISOU 2015  NE1 TRP C  35     1756   2705   2088   1021    528    648       N  
ATOM   2016  CE2 TRP C  35      19.318  22.487  56.550  1.00 15.53           C  
ANISOU 2016  CE2 TRP C  35     1762   2853   1284   1002    542    214       C  
ATOM   2017  CE3 TRP C  35      19.786  24.719  55.764  1.00 17.94           C  
ANISOU 2017  CE3 TRP C  35     2125   2757   1936    907    859    494       C  
ATOM   2018  CZ2 TRP C  35      20.667  22.137  56.519  1.00 17.52           C  
ANISOU 2018  CZ2 TRP C  35     1847   2841   1968    915    667    332       C  
ATOM   2019  CZ3 TRP C  35      21.128  24.359  55.725  1.00 18.07           C  
ANISOU 2019  CZ3 TRP C  35     2075   2869   1923    817    410    756       C  
ATOM   2020  CH2 TRP C  35      21.549  23.076  56.082  1.00 17.26           C  
ANISOU 2020  CH2 TRP C  35     1736   2956   1866    946    803    467       C  
ATOM   2021  N   VAL C  36      16.212  24.542  59.403  1.00 20.59           N  
ANISOU 2021  N   VAL C  36     2400   2789   2636   1484    690   1137       N  
ATOM   2022  CA  VAL C  36      16.988  24.586  60.658  1.00 21.01           C  
ANISOU 2022  CA  VAL C  36     2420   2885   2678   1395    863    595       C  
ATOM   2023  C   VAL C  36      17.755  23.253  60.744  1.00 19.97           C  
ANISOU 2023  C   VAL C  36     2539   2665   2382    897    868    111       C  
ATOM   2024  O   VAL C  36      17.168  22.184  60.888  1.00 19.11           O  
ANISOU 2024  O   VAL C  36     2473   2826   1962    772    114    344       O  
ATOM   2025  CB  VAL C  36      16.047  24.746  61.852  1.00 20.72           C  
ANISOU 2025  CB  VAL C  36     2479   2762   2630   1639     82    643       C  
ATOM   2026  CG1 VAL C  36      16.787  24.761  63.162  1.00 22.12           C  
ANISOU 2026  CG1 VAL C  36     2808   2929   2667    732   -560   -101       C  
ATOM   2027  CG2 VAL C  36      15.128  25.931  61.688  1.00 22.35           C  
ANISOU 2027  CG2 VAL C  36     3225   2303   2963    891    207    453       C  
ATOM   2028  N   ALA C  37      19.047  23.317  60.422  1.00 18.69           N  
ANISOU 2028  N   ALA C  37     2750   2622   1728    627    508    516       N  
ATOM   2029  CA  ALA C  37      19.837  22.102  60.273  1.00 17.92           C  
ANISOU 2029  CA  ALA C  37     2618   2563   1627    120     17    514       C  
ATOM   2030  C   ALA C  37      19.666  21.145  61.452  1.00 16.99           C  
ANISOU 2030  C   ALA C  37     2312   2618   1524    231    458    207       C  
ATOM   2031  O   ALA C  37      19.593  19.926  61.268  1.00 15.94           O  
ANISOU 2031  O   ALA C  37     2083   2577   1396    628    285    458       O  
ATOM   2032  CB  ALA C  37      21.335  22.472  60.173  1.00 19.79           C  
ANISOU 2032  CB  ALA C  37     2818   2883   1820   -318   -526    754       C  
ATOM   2033  N   SER C  38      19.718  21.677  62.675  1.00 16.18           N  
ANISOU 2033  N   SER C  38     2082   2455   1611    488    331   -114       N  
ATOM   2034  CA  SER C  38      19.689  20.863  63.873  1.00 17.99           C  
ANISOU 2034  CA  SER C  38     2573   2774   1490    196    476     20       C  
ATOM   2035  C   SER C  38      18.346  20.194  64.106  1.00 17.83           C  
ANISOU 2035  C   SER C  38     2307   3564    904    186    576    -47       C  
ATOM   2036  O   SER C  38      18.240  19.263  64.913  1.00 17.64           O  
ANISOU 2036  O   SER C  38     2046   3142   1513    220    219     95       O  
ATOM   2037  CB  SER C  38      20.118  21.655  65.097  1.00 18.41           C  
ANISOU 2037  CB  SER C  38     2423   2964   1609    121    567    124       C  
ATOM   2038  OG  SER C  38      21.457  22.054  65.056  1.00 24.05           O  
ANISOU 2038  OG  SER C  38     2626   3835   2676   -422     22    168       O  
ATOM   2039  N   LYS C  39      17.327  20.573  63.357  1.00 18.20           N  
ANISOU 2039  N   LYS C  39     2269   3589   1060    392    404    522       N  
ATOM   2040  CA  LYS C  39      16.020  19.943  63.434  1.00 18.19           C  
ANISOU 2040  CA  LYS C  39     1812   3879   1219    709    880     21       C  
ATOM   2041  C   LYS C  39      15.779  18.939  62.313  1.00 17.71           C  
ANISOU 2041  C   LYS C  39     1512   3929   1289    559    537    443       C  
ATOM   2042  O   LYS C  39      14.758  18.230  62.318  1.00 21.32           O  
ANISOU 2042  O   LYS C  39     1957   4371   1775     75    480    549       O  
ATOM   2043  CB  LYS C  39      14.918  20.999  63.399  1.00 21.85           C  
ANISOU 2043  CB  LYS C  39     2080   3739   2483    881    913   -803       C  
ATOM   2044  CG  LYS C  39      14.794  21.900  64.598  1.00 24.69           C  
ANISOU 2044  CG  LYS C  39     3275   3180   2926    895    715   -925       C  
ATOM   2045  CD  LYS C  39      13.604  22.838  64.497  0.80 26.53           C  
ANISOU 2045  CD  LYS C  39     3312   3163   3604    809    705   -716       C  
ATOM   2046  CE  LYS C  39      12.458  22.197  63.734  0.00 26.21           C  
ANISOU 2046  CE  LYS C  39     3204   3127   3628    900    706   -715       C  
ATOM   2047  NZ  LYS C  39      11.303  23.125  63.587  0.00 26.33           N  
ANISOU 2047  NZ  LYS C  39     3282   3076   3645    936    704   -715       N  
ATOM   2048  N   GLY C  40      16.681  18.848  61.348  1.00 17.33           N  
ANISOU 2048  N   GLY C  40     1890   3503   1190    533    372    503       N  
ATOM   2049  CA  GLY C  40      16.518  17.922  60.231  1.00 16.29           C  
ANISOU 2049  CA  GLY C  40     1575   3002   1612    576     22   1193       C  
ATOM   2050  C   GLY C  40      15.212  18.142  59.500  1.00 15.74           C  
ANISOU 2050  C   GLY C  40     1329   3065   1585    708    362   1157       C  
ATOM   2051  O   GLY C  40      14.576  17.180  59.075  1.00 16.89           O  
ANISOU 2051  O   GLY C  40     1954   3007   1457    422    119    514       O  
ATOM   2052  N   ASN C  41      14.822  19.399  59.272  1.00 16.56           N  
ANISOU 2052  N   ASN C  41     1600   3021   1670    740    164    892       N  
ATOM   2053  CA  ASN C  41      13.524  19.742  58.756  1.00 16.51           C  
ANISOU 2053  CA  ASN C  41     1615   2963   1695    910     99    540       C  
ATOM   2054  C   ASN C  41      13.455  20.158  57.316  1.00 16.66           C  
ANISOU 2054  C   ASN C  41     1616   3006   1710   1146    -45   1132       C  
ATOM   2055  O   ASN C  41      12.440  20.722  56.855  1.00 16.76           O  
ANISOU 2055  O   ASN C  41     1582   3150   1635   1024    202   1005       O  
ATOM   2056  CB  ASN C  41      12.856  20.810  59.633  1.00 17.11           C  
ANISOU 2056  CB  ASN C  41     1858   2952   1690    993     54    373       C  
ATOM   2057  CG  ASN C  41      13.420  22.194  59.411  1.00 19.25           C  
ANISOU 2057  CG  ASN C  41     2430   2933   1950    790    117    383       C  
ATOM   2058  OD1 ASN C  41      14.543  22.343  58.885  1.00 21.27           O  
ANISOU 2058  OD1 ASN C  41     2076   2992   3014    832   1039    566       O  
ATOM   2059  ND2 ASN C  41      12.648  23.208  59.784  1.00 21.49           N  
ANISOU 2059  ND2 ASN C  41     2321   2925   2920    892    772     53       N  
ATOM   2060  N   LEU C  42      14.480  19.900  56.515  1.00 17.22           N  
ANISOU 2060  N   LEU C  42     1496   3320   1728    753    419   1272       N  
ATOM   2061  CA  LEU C  42      14.454  20.397  55.141  1.00 17.73           C  
ANISOU 2061  CA  LEU C  42     1630   3382   1725   1052    733   1015       C  
ATOM   2062  C   LEU C  42      13.243  19.985  54.368  1.00 18.01           C  
ANISOU 2062  C   LEU C  42     1582   3618   1642   1025    401   1326       C  
ATOM   2063  O   LEU C  42      12.620  20.839  53.671  1.00 18.48           O  
ANISOU 2063  O   LEU C  42     1604   3667   1749   1255    519   1148       O  
ATOM   2064  CB  LEU C  42      15.768  20.088  54.432  1.00 17.05           C  
ANISOU 2064  CB  LEU C  42     1622   3246   1612   1078   1100    680       C  
ATOM   2065  CG  LEU C  42      15.882  20.646  52.998  1.00 18.79           C  
ANISOU 2065  CG  LEU C  42     2299   3211   1628    728   1276    453       C  
ATOM   2066  CD1 LEU C  42      15.923  22.169  53.041  1.00 19.46           C  
ANISOU 2066  CD1 LEU C  42     2519   3214   1661    803   1005    648       C  
ATOM   2067  CD2 LEU C  42      17.187  20.114  52.379  1.00 18.75           C  
ANISOU 2067  CD2 LEU C  42     2506   3131   1487    274   1105    457       C  
ATOM   2068  N   ALA C  43      12.838  18.713  54.423  1.00 19.07           N  
ANISOU 2068  N   ALA C  43     1697   3693   1854    853    574   1164       N  
ATOM   2069  CA  ALA C  43      11.705  18.225  53.665  1.00 22.00           C  
ANISOU 2069  CA  ALA C  43     1704   4234   2420    540   -169   1211       C  
ATOM   2070  C   ALA C  43      10.377  18.771  54.185  1.00 22.97           C  
ANISOU 2070  C   ALA C  43     1478   4337   2912    716    536   1340       C  
ATOM   2071  O   ALA C  43       9.358  18.703  53.484  1.00 24.86           O  
ANISOU 2071  O   ALA C  43     1244   5209   2991    609    392   1847       O  
ATOM   2072  CB  ALA C  43      11.644  16.704  53.632  1.00 21.61           C  
ANISOU 2072  CB  ALA C  43     1553   4231   2428    423   -135   1044       C  
ATOM   2073  N   ASP C  44      10.370  19.277  55.406  1.00 22.18           N  
ANISOU 2073  N   ASP C  44     1054   4433   2940   1224    614   1895       N  
ATOM   2074  CA  ASP C  44       9.168  19.867  55.964  1.00 22.65           C  
ANISOU 2074  CA  ASP C  44     1455   4225   2928    791    512   1887       C  
ATOM   2075  C   ASP C  44       8.940  21.278  55.420  1.00 22.96           C  
ANISOU 2075  C   ASP C  44     1612   4246   2864   1066    810   1630       C  
ATOM   2076  O   ASP C  44       7.795  21.640  55.135  1.00 23.66           O  
ANISOU 2076  O   ASP C  44     1819   4086   3085    733    270   1813       O  
ATOM   2077  CB  ASP C  44       9.205  19.905  57.483  1.00 24.71           C  
ANISOU 2077  CB  ASP C  44     2329   4217   2843    873    477   1429       C  
ATOM   2078  CG  ASP C  44       9.318  18.544  58.121  1.00 28.89           C  
ANISOU 2078  CG  ASP C  44     3775   4112   3090    587    121   1598       C  
ATOM   2079  OD1 ASP C  44       8.533  17.640  57.755  1.00 31.85           O  
ANISOU 2079  OD1 ASP C  44     3590   4276   4237    416    631   2023       O  
ATOM   2080  OD2 ASP C  44      10.188  18.357  58.988  1.00 29.15           O  
ANISOU 2080  OD2 ASP C  44     4465   3441   3168    216   -675    732       O  
ATOM   2081  N   VAL C  45      10.014  22.046  55.268  1.00 20.32           N  
ANISOU 2081  N   VAL C  45     1363   3931   2427   1352    301   1646       N  
ATOM   2082  CA  VAL C  45       9.926  23.408  54.800  1.00 21.11           C  
ANISOU 2082  CA  VAL C  45     1741   3887   2393   1632    771   1663       C  
ATOM   2083  C   VAL C  45      10.112  23.566  53.294  1.00 20.64           C  
ANISOU 2083  C   VAL C  45     1556   3841   2446   1190    747   2091       C  
ATOM   2084  O   VAL C  45       9.642  24.533  52.684  1.00 21.15           O  
ANISOU 2084  O   VAL C  45     1778   3846   2411   1432    495   1511       O  
ATOM   2085  CB  VAL C  45      10.868  24.355  55.545  1.00 21.30           C  
ANISOU 2085  CB  VAL C  45     1988   3722   2384   1563    867   1269       C  
ATOM   2086  CG1 VAL C  45      10.570  24.329  57.037  1.00 21.82           C  
ANISOU 2086  CG1 VAL C  45     2507   3401   2382   1540    694    992       C  
ATOM   2087  CG2 VAL C  45      12.341  23.954  55.317  1.00 22.21           C  
ANISOU 2087  CG2 VAL C  45     2027   3768   2643   1342    637    356       C  
ATOM   2088  N   ALA C  46      10.725  22.582  52.668  1.00 20.56           N  
ANISOU 2088  N   ALA C  46     1520   3912   2380   1304    896   1684       N  
ATOM   2089  CA  ALA C  46      10.980  22.587  51.251  1.00 20.70           C  
ANISOU 2089  CA  ALA C  46     1142   4352   2372   1237    897   1939       C  
ATOM   2090  C   ALA C  46      10.904  21.198  50.647  1.00 19.79           C  
ANISOU 2090  C   ALA C  46      909   4341   2269   1296    888   1932       C  
ATOM   2091  O   ALA C  46      11.927  20.682  50.167  1.00 20.12           O  
ANISOU 2091  O   ALA C  46      984   4372   2289   1014    613   1628       O  
ATOM   2092  CB  ALA C  46      12.240  23.322  50.877  1.00 22.39           C  
ANISOU 2092  CB  ALA C  46     1451   4453   2605    945    844   1115       C  
ATOM   2093  N   PRO C  47       9.691  20.612  50.678  1.00 21.72           N  
ANISOU 2093  N   PRO C  47      967   4497   2787   1140   1096   2052       N  
ATOM   2094  CA  PRO C  47       9.530  19.272  50.112  1.00 22.12           C  
ANISOU 2094  CA  PRO C  47     1343   4661   2402    870    602   1752       C  
ATOM   2095  C   PRO C  47      10.101  19.214  48.691  1.00 23.57           C  
ANISOU 2095  C   PRO C  47     1113   5580   2265   1011    715   2167       C  
ATOM   2096  O   PRO C  47       9.838  20.087  47.858  1.00 25.16           O  
ANISOU 2096  O   PRO C  47     1579   5581   2400   1128    420   2560       O  
ATOM   2097  CB  PRO C  47       8.048  19.009  50.105  1.00 23.10           C  
ANISOU 2097  CB  PRO C  47     1527   4693   2555    666    669   1614       C  
ATOM   2098  CG  PRO C  47       7.438  20.006  51.006  1.00 22.13           C  
ANISOU 2098  CG  PRO C  47     1269   4863   2275    666    525   1086       C  
ATOM   2099  CD  PRO C  47       8.396  21.127  51.175  1.00 22.40           C  
ANISOU 2099  CD  PRO C  47     1052   4591   2868    848   1100   1774       C  
ATOM   2100  N   GLY C  48      10.805  18.128  48.407  1.00 21.62           N  
ANISOU 2100  N   GLY C  48      957   5560   1699    529    109   1321       N  
ATOM   2101  CA  GLY C  48      11.388  17.919  47.112  1.00 22.82           C  
ANISOU 2101  CA  GLY C  48     1210   5810   1649    173    314    911       C  
ATOM   2102  C   GLY C  48      12.681  18.623  46.846  1.00 22.48           C  
ANISOU 2102  C   GLY C  48     1328   5702   1511     75    599    610       C  
ATOM   2103  O   GLY C  48      13.283  18.361  45.773  1.00 27.01           O  
ANISOU 2103  O   GLY C  48     1547   7765    952   -103     -4   -116       O  
ATOM   2104  N   LYS C  49      13.146  19.519  47.706  1.00 20.37           N  
ANISOU 2104  N   LYS C  49      759   5035   1946    584      0   1035       N  
ATOM   2105  CA  LYS C  49      14.367  20.261  47.513  1.00 18.04           C  
ANISOU 2105  CA  LYS C  49      588   4432   1836    958    143    951       C  
ATOM   2106  C   LYS C  49      15.575  19.616  48.197  1.00 17.60           C  
ANISOU 2106  C   LYS C  49      857   4387   1442    576    236    843       C  
ATOM   2107  O   LYS C  49      15.416  18.889  49.178  1.00 17.97           O  
ANISOU 2107  O   LYS C  49     1043   4324   1459    703     53    856       O  
ATOM   2108  CB ALYS C  49      14.236  21.726  47.882  0.50 21.89           C  
ANISOU 2108  CB ALYS C  49     1447   4372   2499   1076    288   1347       C  
ATOM   2109  CB BLYS C  49      14.243  21.707  48.015  0.50 21.78           C  
ANISOU 2109  CB BLYS C  49     1504   4353   2420   1066    233   1364       C  
ATOM   2110  CG ALYS C  49      13.097  22.462  47.197  0.50 21.81           C  
ANISOU 2110  CG ALYS C  49     1656   4214   2417   1029    230   1358       C  
ATOM   2111  CG BLYS C  49      13.052  22.473  47.511  0.50 21.85           C  
ANISOU 2111  CG BLYS C  49     1686   4200   2416   1045    155   1409       C  
ATOM   2112  CD ALYS C  49      13.290  22.553  45.698  0.50 23.90           C  
ANISOU 2112  CD ALYS C  49     2469   4223   2391    669   -329   1346       C  
ATOM   2113  CD BLYS C  49      13.008  22.596  46.011  0.50 22.33           C  
ANISOU 2113  CD BLYS C  49     1985   4105   2396    847   -347   1411       C  
ATOM   2114  CE ALYS C  49      12.269  23.508  45.073  0.50 24.06           C  
ANISOU 2114  CE ALYS C  49     2705   4084   2351    578   -249   1107       C  
ATOM   2115  CE BLYS C  49      11.725  23.290  45.550  0.50 22.30           C  
ANISOU 2115  CE BLYS C  49     2029   4018   2425    823    450    830       C  
ATOM   2116  NZ ALYS C  49      11.741  23.034  43.785  0.50 23.33           N  
ANISOU 2116  NZ ALYS C  49     2905   3567   2392    636   -268   1291       N  
ATOM   2117  NZ BLYS C  49      10.570  22.370  45.584  0.50 23.83           N  
ANISOU 2117  NZ BLYS C  49     1962   3651   3441   1026   -572    656       N  
ATOM   2118  N   SER C  50      16.757  19.845  47.653  1.00 15.12           N  
ANISOU 2118  N   SER C  50     1009   3409   1327    785     60    975       N  
ATOM   2119  CA  SER C  50      18.024  19.417  48.241  1.00 14.17           C  
ANISOU 2119  CA  SER C  50     1351   3039    995    367    -83    439       C  
ATOM   2120  C   SER C  50      18.991  20.617  48.312  1.00 14.32           C  
ANISOU 2120  C   SER C  50     1273   2823   1344    600    391    700       C  
ATOM   2121  O   SER C  50      18.915  21.541  47.497  1.00 15.89           O  
ANISOU 2121  O   SER C  50     1787   2732   1519    445    488    700       O  
ATOM   2122  CB  SER C  50      18.694  18.347  47.354  1.00 16.07           C  
ANISOU 2122  CB  SER C  50     1548   2806   1754    326   -331    -37       C  
ATOM   2123  OG  SER C  50      17.965  17.137  47.354  1.00 15.66           O  
ANISOU 2123  OG  SER C  50     1434   2871   1643    280   -378    112       O  
ATOM   2124  N   ILE C  51      19.899  20.560  49.260  1.00 13.99           N  
ANISOU 2124  N   ILE C  51      938   2684   1695    614     43    549       N  
ATOM   2125  CA  ILE C  51      20.930  21.607  49.381  1.00 13.77           C  
ANISOU 2125  CA  ILE C  51     1273   2135   1825    617    373    601       C  
ATOM   2126  C   ILE C  51      21.992  21.406  48.295  1.00 13.56           C  
ANISOU 2126  C   ILE C  51     1121   2173   1858    529    235    889       C  
ATOM   2127  O   ILE C  51      22.483  20.276  48.098  1.00 13.21           O  
ANISOU 2127  O   ILE C  51     1303   2183   1531    484    293    450       O  
ATOM   2128  CB  ILE C  51      21.619  21.533  50.757  1.00 15.35           C  
ANISOU 2128  CB  ILE C  51     1417   2596   1817    333    755     87       C  
ATOM   2129  CG1 ILE C  51      20.696  21.736  51.956  1.00 15.71           C  
ANISOU 2129  CG1 ILE C  51     1844   2231   1895     37    437     14       C  
ATOM   2130  CG2 ILE C  51      22.830  22.450  50.816  1.00 16.48           C  
ANISOU 2130  CG2 ILE C  51     1447   2957   1859    177    585    297       C  
ATOM   2131  CD1 ILE C  51      20.002  23.043  51.999  1.00 17.76           C  
ANISOU 2131  CD1 ILE C  51     1927   2278   2544    468    494     58       C  
ATOM   2132  N   GLY C  52      22.330  22.462  47.580  1.00 13.78           N  
ANISOU 2132  N   GLY C  52     1333   2190   1713    522    426    479       N  
ATOM   2133  CA  GLY C  52      23.441  22.410  46.627  1.00 13.48           C  
ANISOU 2133  CA  GLY C  52     1206   2082   1835    629    602    572       C  
ATOM   2134  C   GLY C  52      23.739  23.768  46.030  1.00 12.60           C  
ANISOU 2134  C   GLY C  52     1341   2137   1309    879    731    612       C  
ATOM   2135  O   GLY C  52      22.881  24.638  46.012  1.00 14.20           O  
ANISOU 2135  O   GLY C  52     1437   2168   1790    959    483    443       O  
ATOM   2136  N   GLY C  53      24.959  23.907  45.498  1.00 12.48           N  
ANISOU 2136  N   GLY C  53     1534   1964   1245    658    350    114       N  
ATOM   2137  CA  GLY C  53      25.413  25.065  44.815  1.00 13.65           C  
ANISOU 2137  CA  GLY C  53     1772   1952   1461    519    289    479       C  
ATOM   2138  C   GLY C  53      26.389  25.935  45.574  1.00 14.60           C  
ANISOU 2138  C   GLY C  53     2135   1826   1585    382     82    456       C  
ATOM   2139  O   GLY C  53      26.873  26.931  44.989  1.00 17.19           O  
ANISOU 2139  O   GLY C  53     2876   1786   1870     62    205    407       O  
ATOM   2140  N   ASP C  54      26.729  25.604  46.812  1.00 13.32           N  
ANISOU 2140  N   ASP C  54     1493   1913   1655    593     -9    103       N  
ATOM   2141  CA  ASP C  54      27.647  26.420  47.599  1.00 14.02           C  
ANISOU 2141  CA  ASP C  54     1806   1833   1686    502    -24    -92       C  
ATOM   2142  C   ASP C  54      29.110  26.120  47.254  1.00 15.02           C  
ANISOU 2142  C   ASP C  54     1795   1994   1916    226    267   -179       C  
ATOM   2143  O   ASP C  54      29.471  25.026  46.865  1.00 14.05           O  
ANISOU 2143  O   ASP C  54     1497   1927   1915   -202    574     98       O  
ATOM   2144  CB  ASP C  54      27.432  26.187  49.098  1.00 16.31           C  
ANISOU 2144  CB  ASP C  54     2347   2241   1608    177    531   -475       C  
ATOM   2145  CG  ASP C  54      26.092  26.749  49.568  1.00 15.57           C  
ANISOU 2145  CG  ASP C  54     2305   2196   1416    676    791    191       C  
ATOM   2146  OD1 ASP C  54      25.935  27.979  49.420  1.00 26.40           O  
ANISOU 2146  OD1 ASP C  54     3098   2232   4701   1208    934     35       O  
ATOM   2147  OD2 ASP C  54      25.253  25.998  50.033  1.00 18.76           O  
ANISOU 2147  OD2 ASP C  54     1710   2974   2444    624   1215    271       O  
ATOM   2148  N   ILE C  55      29.950  27.118  47.391  1.00 16.10           N  
ANISOU 2148  N   ILE C  55     2141   1782   2195    110    472    -32       N  
ATOM   2149  CA  ILE C  55      31.415  26.908  47.196  1.00 15.74           C  
ANISOU 2149  CA  ILE C  55     2290   1867   1823   -228    484    334       C  
ATOM   2150  C   ILE C  55      31.950  25.988  48.291  1.00 15.05           C  
ANISOU 2150  C   ILE C  55     1853   2179   1686   -212    765   -300       C  
ATOM   2151  O   ILE C  55      31.495  26.106  49.424  1.00 16.69           O  
ANISOU 2151  O   ILE C  55     1963   2711   1666     73    331    167       O  
ATOM   2152  CB  ILE C  55      32.088  28.313  47.341  1.00 21.69           C  
ANISOU 2152  CB  ILE C  55     3280   2152   2808  -1026    331    493       C  
ATOM   2153  CG1 ILE C  55      31.659  29.188  46.146  1.00 23.67           C  
ANISOU 2153  CG1 ILE C  55     4117   1671   3205   -714    965    412       C  
ATOM   2154  CG2 ILE C  55      33.598  28.170  47.380  1.00 23.93           C  
ANISOU 2154  CG2 ILE C  55     2907   3070   3114  -1069    535    253       C  
ATOM   2155  CD1 ILE C  55      32.284  30.535  46.169  1.00 30.05           C  
ANISOU 2155  CD1 ILE C  55     6469   2176   2773  -1093    173    307       C  
ATOM   2156  N   PHE C  56      32.812  25.080  47.897  1.00 15.61           N  
ANISOU 2156  N   PHE C  56     1923   2168   1842     80    578   -125       N  
ATOM   2157  CA  PHE C  56      33.541  24.173  48.783  1.00 15.60           C  
ANISOU 2157  CA  PHE C  56     1840   2207   1879    126    -98   -138       C  
ATOM   2158  C   PHE C  56      35.022  24.613  48.788  1.00 16.39           C  
ANISOU 2158  C   PHE C  56     1892   2342   1995     11   -666    638       C  
ATOM   2159  O   PHE C  56      35.632  24.712  47.735  1.00 19.92           O  
ANISOU 2159  O   PHE C  56     2090   3483   1997   -648    -42    592       O  
ATOM   2160  CB  PHE C  56      33.481  22.749  48.226  1.00 14.54           C  
ANISOU 2160  CB  PHE C  56     1436   2249   1840    244     75    -78       C  
ATOM   2161  CG  PHE C  56      34.150  21.700  49.091  1.00 15.41           C  
ANISOU 2161  CG  PHE C  56     1755   2109   1991   -285    115      8       C  
ATOM   2162  CD1 PHE C  56      33.535  21.230  50.236  1.00 17.84           C  
ANISOU 2162  CD1 PHE C  56     2771   2175   1833   -635   -394    412       C  
ATOM   2163  CD2 PHE C  56      35.374  21.162  48.737  1.00 17.11           C  
ANISOU 2163  CD2 PHE C  56     1998   1774   2728   -102   -240   -116       C  
ATOM   2164  CE1 PHE C  56      34.130  20.268  51.022  1.00 18.90           C  
ANISOU 2164  CE1 PHE C  56     3098   2004   2080   -507   -729    334       C  
ATOM   2165  CE2 PHE C  56      36.003  20.239  49.541  1.00 18.06           C  
ANISOU 2165  CE2 PHE C  56     2299   1711   2851     89  -1077    475       C  
ATOM   2166  CZ  PHE C  56      35.387  19.790  50.690  1.00 20.10           C  
ANISOU 2166  CZ  PHE C  56     2945   2040   2652   -182   -842    211       C  
ATOM   2167  N   SER C  57      35.565  24.818  49.980  1.00 17.61           N  
ANISOU 2167  N   SER C  57     1729   2973   1989     87   -425     97       N  
ATOM   2168  CA  SER C  57      36.892  25.374  50.132  1.00 20.13           C  
ANISOU 2168  CA  SER C  57     1809   3593   2248   -155   -816   -367       C  
ATOM   2169  C   SER C  57      38.058  24.506  49.761  1.00 23.00           C  
ANISOU 2169  C   SER C  57     1567   3715   3458   -161   -848   -479       C  
ATOM   2170  O   SER C  57      39.156  25.022  49.448  1.00 26.82           O  
ANISOU 2170  O   SER C  57     1640   4284   4265   -401    -39   -467       O  
ATOM   2171  CB  SER C  57      37.061  26.030  51.497  1.00 25.31           C  
ANISOU 2171  CB  SER C  57     3178   4348   2089  -1230   -874   -172       C  
ATOM   2172  OG  SER C  57      37.728  25.205  52.409  1.00 29.03           O  
ANISOU 2172  OG  SER C  57     4728   4492   1810    138   -155    -65       O  
ATOM   2173  N   ASN C  58      37.980  23.190  49.867  1.00 22.49           N  
ANISOU 2173  N   ASN C  58     1954   3630   2960    241   -940    -97       N  
ATOM   2174  CA  ASN C  58      39.116  22.338  49.544  1.00 20.42           C  
ANISOU 2174  CA  ASN C  58     1718   3869   2170    475   -249   -115       C  
ATOM   2175  C   ASN C  58      40.356  22.658  50.362  1.00 19.84           C  
ANISOU 2175  C   ASN C  58     2020   3389   2130    387   -160     64       C  
ATOM   2176  O   ASN C  58      41.482  22.489  49.885  1.00 20.39           O  
ANISOU 2176  O   ASN C  58     2293   3246   2209    -62    754    119       O  
ATOM   2177  CB  ASN C  58      39.436  22.360  48.054  1.00 23.04           C  
ANISOU 2177  CB  ASN C  58     2407   4227   2122   -133     44    175       C  
ATOM   2178  CG  ASN C  58      40.258  21.168  47.604  1.00 21.43           C  
ANISOU 2178  CG  ASN C  58     2156   4343   1643   -188   -151    220       C  
ATOM   2179  OD1 ASN C  58      40.151  20.074  48.157  1.00 20.13           O  
ANISOU 2179  OD1 ASN C  58     1889   4318   1443     96    405   -512       O  
ATOM   2180  ND2 ASN C  58      41.048  21.341  46.541  1.00 22.90           N  
ANISOU 2180  ND2 ASN C  58     2339   4595   1766   -750    186   -371       N  
ATOM   2181  N   ARG C  59      40.174  23.033  51.615  1.00 20.51           N  
ANISOU 2181  N   ARG C  59     2415   3222   2157    204   -247   -412       N  
ATOM   2182  CA  ARG C  59      41.288  23.373  52.500  1.00 20.85           C  
ANISOU 2182  CA  ARG C  59     2611   3221   2090    111   -182   -147       C  
ATOM   2183  C   ARG C  59      42.212  22.222  52.798  1.00 20.47           C  
ANISOU 2183  C   ARG C  59     2440   3190   2149   -327    218   -349       C  
ATOM   2184  O   ARG C  59      43.413  22.425  53.040  1.00 22.68           O  
ANISOU 2184  O   ARG C  59     2998   2833   2787   -990    462   -309       O  
ATOM   2185  CB  ARG C  59      40.698  24.010  53.786  1.00 22.27           C  
ANISOU 2185  CB  ARG C  59     3193   3117   2152    599   -614    -90       C  
ATOM   2186  CG  ARG C  59      40.040  25.357  53.539  0.30 27.21           C  
ANISOU 2186  CG  ARG C  59     4212   2620   3508    488   -376   -195       C  
ATOM   2187  CD  ARG C  59      39.373  25.954  54.743  0.80 27.08           C  
ANISOU 2187  CD  ARG C  59     3757   2689   3843    765   -162   -246       C  
ATOM   2188  NE  ARG C  59      38.326  26.932  54.406  0.80 30.53           N  
ANISOU 2188  NE  ARG C  59     4059   2632   4910   1038    387   -864       N  
ATOM   2189  CZ  ARG C  59      37.667  27.682  55.274  0.80 30.96           C  
ANISOU 2189  CZ  ARG C  59     4626   2327   4812    909    388   -901       C  
ATOM   2190  NH1 ARG C  59      37.784  27.419  56.580  0.30 36.83           N  
ANISOU 2190  NH1 ARG C  59     6428   2860   4705   -661    831  -1031       N  
ATOM   2191  NH2 ARG C  59      36.876  28.677  54.887  0.30 34.53           N  
ANISOU 2191  NH2 ARG C  59     4585   2307   6228    990    224  -1125       N  
ATOM   2192  N   GLU C  60      41.715  20.978  52.787  1.00 16.78           N  
ANISOU 2192  N   GLU C  60     1551   3178   1646   -141   -517    188       N  
ATOM   2193  CA  GLU C  60      42.542  19.794  53.071  1.00 16.69           C  
ANISOU 2193  CA  GLU C  60     1366   3232   1742   -226   -229    248       C  
ATOM   2194  C   GLU C  60      43.300  19.307  51.845  1.00 16.82           C  
ANISOU 2194  C   GLU C  60     1332   3346   1713    158    -94     -6       C  
ATOM   2195  O   GLU C  60      44.053  18.336  51.908  1.00 17.28           O  
ANISOU 2195  O   GLU C  60     1200   3470   1897    469      0    212       O  
ATOM   2196  CB  GLU C  60      41.678  18.652  53.629  1.00 16.33           C  
ANISOU 2196  CB  GLU C  60     1376   3074   1754     58    563   -142       C  
ATOM   2197  CG  GLU C  60      41.111  18.931  55.018  1.00 14.88           C  
ANISOU 2197  CG  GLU C  60     1301   2574   1780      0    347    -28       C  
ATOM   2198  CD  GLU C  60      40.309  17.737  55.525  1.00 15.96           C  
ANISOU 2198  CD  GLU C  60     1451   2560   2054   -149    205    -58       C  
ATOM   2199  OE1 GLU C  60      39.134  17.600  55.170  1.00 17.24           O  
ANISOU 2199  OE1 GLU C  60     1380   2658   2511    -67     34    -22       O  
ATOM   2200  OE2 GLU C  60      40.886  16.921  56.283  1.00 16.79           O  
ANISOU 2200  OE2 GLU C  60     1756   2249   2375   -240     56   -198       O  
ATOM   2201  N   GLY C  61      43.029  19.880  50.671  1.00 17.13           N  
ANISOU 2201  N   GLY C  61     1359   3387   1762     85    122   -333       N  
ATOM   2202  CA  GLY C  61      43.754  19.530  49.464  1.00 18.49           C  
ANISOU 2202  CA  GLY C  61     1418   3939   1667   -610    310   -428       C  
ATOM   2203  C   GLY C  61      43.382  18.224  48.834  1.00 17.85           C  
ANISOU 2203  C   GLY C  61     1438   3829   1515   -274    193   -419       C  
ATOM   2204  O   GLY C  61      44.110  17.691  47.980  1.00 18.13           O  
ANISOU 2204  O   GLY C  61     1235   4155   1500   -213    276     -4       O  
ATOM   2205  N   LYS C  62      42.277  17.599  49.235  1.00 16.63           N  
ANISOU 2205  N   LYS C  62     1183   3595   1540   -139   -307   -217       N  
ATOM   2206  CA  LYS C  62      41.926  16.277  48.706  1.00 16.85           C  
ANISOU 2206  CA  LYS C  62     1259   3656   1486    -21    -41   -201       C  
ATOM   2207  C   LYS C  62      41.472  16.308  47.267  1.00 18.43           C  
ANISOU 2207  C   LYS C  62     1613   4002   1387   -121    444   -701       C  
ATOM   2208  O   LYS C  62      41.540  15.270  46.585  1.00 21.57           O  
ANISOU 2208  O   LYS C  62     2691   4062   1442    388   -115   -478       O  
ATOM   2209  CB  LYS C  62      40.855  15.635  49.605  1.00 15.67           C  
ANISOU 2209  CB  LYS C  62     1381   3184   1390     12    201    -73       C  
ATOM   2210  CG  LYS C  62      41.301  15.522  51.064  1.00 15.69           C  
ANISOU 2210  CG  LYS C  62     1268   3309   1385    182    319     30       C  
ATOM   2211  CD  LYS C  62      40.251  14.905  51.940  1.00 17.45           C  
ANISOU 2211  CD  LYS C  62     1560   3768   1301   -210    214   -240       C  
ATOM   2212  CE  LYS C  62      40.525  15.053  53.416  1.00 16.00           C  
ANISOU 2212  CE  LYS C  62     1088   3678   1316     78   -215    -99       C  
ATOM   2213  NZ  LYS C  62      39.423  14.531  54.278  1.00 12.98           N  
ANISOU 2213  NZ  LYS C  62     1367   2371   1195    276   -290   -634       N  
ATOM   2214  N   LEU C  63      40.994  17.445  46.771  1.00 17.45           N  
ANISOU 2214  N   LEU C  63     1145   4105   1381    109   -168   -193       N  
ATOM   2215  CA  LEU C  63      40.598  17.562  45.353  1.00 17.11           C  
ANISOU 2215  CA  LEU C  63      544   4563   1394    281   -290    -82       C  
ATOM   2216  C   LEU C  63      41.688  18.329  44.572  1.00 18.33           C  
ANISOU 2216  C   LEU C  63      706   4844   1416      3    444   -446       C  
ATOM   2217  O   LEU C  63      42.376  19.186  45.113  1.00 21.14           O  
ANISOU 2217  O   LEU C  63     1627   4919   1487   -603    222   -777       O  
ATOM   2218  CB  LEU C  63      39.288  18.343  45.263  1.00 17.24           C  
ANISOU 2218  CB  LEU C  63     1075   4152   1324   -258    -34    298       C  
ATOM   2219  CG  LEU C  63      38.026  17.743  45.876  1.00 18.30           C  
ANISOU 2219  CG  LEU C  63     1065   3996   1891   -297    157    485       C  
ATOM   2220  CD1 LEU C  63      36.934  18.817  45.934  1.00 21.38           C  
ANISOU 2220  CD1 LEU C  63      893   4158   3073    155    194    923       C  
ATOM   2221  CD2 LEU C  63      37.515  16.571  45.031  1.00 23.27           C  
ANISOU 2221  CD2 LEU C  63     2505   3915   2422  -1127   -846    303       C  
ATOM   2222  N   PRO C  64      41.812  18.101  43.269  1.00 19.16           N  
ANISOU 2222  N   PRO C  64     1117   4765   1399     92    457   -136       N  
ATOM   2223  CA  PRO C  64      42.817  18.816  42.459  1.00 20.41           C  
ANISOU 2223  CA  PRO C  64     1832   4695   1228   -343    710    236       C  
ATOM   2224  C   PRO C  64      42.562  20.294  42.311  1.00 21.74           C  
ANISOU 2224  C   PRO C  64     1613   4712   1934   -251    810    170       C  
ATOM   2225  O   PRO C  64      41.482  20.758  41.924  1.00 22.50           O  
ANISOU 2225  O   PRO C  64     1386   4883   2280   -147    120    148       O  
ATOM   2226  CB  PRO C  64      42.799  18.094  41.131  1.00 22.39           C  
ANISOU 2226  CB  PRO C  64     2418   4806   1281   -704    415    394       C  
ATOM   2227  CG  PRO C  64      41.581  17.278  41.089  1.00 22.33           C  
ANISOU 2227  CG  PRO C  64     2423   4636   1425   -639    464     71       C  
ATOM   2228  CD  PRO C  64      41.072  17.104  42.468  1.00 20.16           C  
ANISOU 2228  CD  PRO C  64     1521   4670   1467    -81    414   -317       C  
ATOM   2229  N   GLY C  65      43.625  21.114  42.457  1.00 21.12           N  
ANISOU 2229  N   GLY C  65     1366   4476   2181     33    375     50       N  
ATOM   2230  CA  GLY C  65      43.459  22.561  42.333  1.00 22.13           C  
ANISOU 2230  CA  GLY C  65     1522   4473   2414    127    278    -54       C  
ATOM   2231  C   GLY C  65      44.088  23.166  41.109  1.00 21.09           C  
ANISOU 2231  C   GLY C  65     1340   4160   2513    297    209    237       C  
ATOM   2232  O   GLY C  65      44.872  22.544  40.416  1.00 21.35           O  
ANISOU 2232  O   GLY C  65     1900   4085   2126    567      5    210       O  
ATOM   2233  N   LYS C  66      43.677  24.420  40.786  1.00 21.94           N  
ANISOU 2233  N   LYS C  66     1513   4080   2741    157    212    734       N  
ATOM   2234  CA  LYS C  66      44.269  25.116  39.645  1.00 21.88           C  
ANISOU 2234  CA  LYS C  66     1531   3969   2814    -47   -319   1017       C  
ATOM   2235  C   LYS C  66      43.973  26.604  39.725  1.00 24.96           C  
ANISOU 2235  C   LYS C  66     2037   3967   3480   -206    606    652       C  
ATOM   2236  O   LYS C  66      42.902  27.000  40.212  1.00 22.93           O  
ANISOU 2236  O   LYS C  66     2412   3705   2596    -26   -433    410       O  
ATOM   2237  CB  LYS C  66      43.662  24.545  38.345  1.00 23.86           C  
ANISOU 2237  CB  LYS C  66     2035   4248   2783   -182    244    759       C  
ATOM   2238  CG  LYS C  66      44.080  25.290  37.103  1.00 27.40           C  
ANISOU 2238  CG  LYS C  66     3011   4641   2759   -535    466    463       C  
ATOM   2239  CD  LYS C  66      43.335  24.770  35.866  1.00 34.58           C  
ANISOU 2239  CD  LYS C  66     4757   5661   2720  -1729    268    188       C  
ATOM   2240  CE  LYS C  66      43.948  25.349  34.596  0.80 35.38           C  
ANISOU 2240  CE  LYS C  66     4615   6092   2735  -1817   -169    -84       C  
ATOM   2241  NZ  LYS C  66      43.702  24.479  33.411  0.80 37.38           N  
ANISOU 2241  NZ  LYS C  66     5608   5880   2715  -1112    836  -1009       N  
ATOM   2242  N   SER C  67      44.860  27.430  39.181  1.00 28.13           N  
ANISOU 2242  N   SER C  67     2483   3964   4243   -717   1366   1285       N  
ATOM   2243  CA  SER C  67      44.604  28.896  39.216  1.00 31.50           C  
ANISOU 2243  CA  SER C  67     2820   3930   5218   -267   1038   1083       C  
ATOM   2244  C   SER C  67      43.216  29.119  38.568  1.00 31.23           C  
ANISOU 2244  C   SER C  67     2887   3821   5158   -238   1364    618       C  
ATOM   2245  O   SER C  67      43.031  28.650  37.440  1.00 31.38           O  
ANISOU 2245  O   SER C  67     2914   3917   5092     90    980    881       O  
ATOM   2246  CB  SER C  67      45.630  29.625  38.339  1.00 33.99           C  
ANISOU 2246  CB  SER C  67     3543   3815   5558  -1044   1082   1153       C  
ATOM   2247  OG  SER C  67      46.949  29.590  38.888  1.00 33.75           O  
ANISOU 2247  OG  SER C  67     3299   4330   5193   -864   1306   1917       O  
ATOM   2248  N   GLY C  68      42.355  29.847  39.239  1.00 31.32           N  
ANISOU 2248  N   GLY C  68     3129   3611   5161   -619   1189   1229       N  
ATOM   2249  CA  GLY C  68      41.060  30.254  38.754  1.00 31.35           C  
ANISOU 2249  CA  GLY C  68     3044   3653   5213   -345   1026   1457       C  
ATOM   2250  C   GLY C  68      39.960  29.238  38.883  1.00 30.51           C  
ANISOU 2250  C   GLY C  68     2754   3968   4870   -341    289   1574       C  
ATOM   2251  O   GLY C  68      38.785  29.551  38.574  1.00 33.82           O  
ANISOU 2251  O   GLY C  68     2589   3741   6520    205    396   2085       O  
ATOM   2252  N   ARG C  69      40.262  28.038  39.341  1.00 27.34           N  
ANISOU 2252  N   ARG C  69     2137   4057   4195   -632    414   1000       N  
ATOM   2253  CA  ARG C  69      39.287  26.972  39.521  1.00 24.56           C  
ANISOU 2253  CA  ARG C  69     1753   4127   3451   -389    238   1235       C  
ATOM   2254  C   ARG C  69      38.577  27.061  40.872  1.00 24.77           C  
ANISOU 2254  C   ARG C  69     2125   3945   3343   -218      7   1090       C  
ATOM   2255  O   ARG C  69      39.245  27.147  41.914  1.00 29.17           O  
ANISOU 2255  O   ARG C  69     2829   4825   3428  -1900    409    934       O  
ATOM   2256  CB  ARG C  69      39.985  25.586  39.431  1.00 23.70           C  
ANISOU 2256  CB  ARG C  69     1473   4110   3422   -672    346   1118       C  
ATOM   2257  CG  ARG C  69      39.009  24.443  39.705  1.00 24.05           C  
ANISOU 2257  CG  ARG C  69     1496   4121   3519   -579    114   1501       C  
ATOM   2258  CD  ARG C  69      39.746  23.101  39.644  1.00 24.29           C  
ANISOU 2258  CD  ARG C  69     1870   4107   3252   -162     63   1315       C  
ATOM   2259  NE  ARG C  69      39.961  22.711  38.247  1.00 25.21           N  
ANISOU 2259  NE  ARG C  69     1786   4534   3257    293    -54   1217       N  
ATOM   2260  CZ  ARG C  69      40.826  21.789  37.869  1.00 24.73           C  
ANISOU 2260  CZ  ARG C  69     1914   4611   2871    646   -824   1480       C  
ATOM   2261  NH1 ARG C  69      41.528  21.159  38.786  1.00 26.27           N  
ANISOU 2261  NH1 ARG C  69     3228   3847   2905    397    742   1051       N  
ATOM   2262  NH2 ARG C  69      41.154  21.676  36.583  1.00 27.12           N  
ANISOU 2262  NH2 ARG C  69     2987   4505   2812    -38    909    438       N  
ATOM   2263  N   THR C  70      37.265  27.006  40.823  1.00 24.05           N  
ANISOU 2263  N   THR C  70     3002   3675   2461  -1452      5   1156       N  
ATOM   2264  CA  THR C  70      36.391  27.019  41.995  1.00 22.06           C  
ANISOU 2264  CA  THR C  70     3195   2840   2347  -1015   1405    226       C  
ATOM   2265  C   THR C  70      35.669  25.641  42.060  1.00 18.93           C  
ANISOU 2265  C   THR C  70     2559   2715   1917   -665    679    288       C  
ATOM   2266  O   THR C  70      35.300  25.104  41.024  1.00 23.72           O  
ANISOU 2266  O   THR C  70     4153   2993   1867  -1556   1144    205       O  
ATOM   2267  CB  THR C  70      35.287  28.097  41.806  1.00 25.75           C  
ANISOU 2267  CB  THR C  70     3705   2713   3367   -294   2391   -129       C  
ATOM   2268  OG1 THR C  70      35.909  29.394  41.767  1.00 30.30           O  
ANISOU 2268  OG1 THR C  70     4241   2883   4389   -518    507    469       O  
ATOM   2269  CG2 THR C  70      34.270  28.066  42.902  1.00 24.74           C  
ANISOU 2269  CG2 THR C  70     2975   2784   3642    597    -82    463       C  
ATOM   2270  N   TRP C  71      35.549  25.115  43.257  1.00 15.84           N  
ANISOU 2270  N   TRP C  71     1154   2977   1886   -427    194    483       N  
ATOM   2271  CA  TRP C  71      34.793  23.895  43.529  1.00 14.65           C  
ANISOU 2271  CA  TRP C  71     1001   3100   1463   -335   -180    492       C  
ATOM   2272  C   TRP C  71      33.483  24.278  44.251  1.00 13.87           C  
ANISOU 2272  C   TRP C  71     1435   2700   1135   -501     30    270       C  
ATOM   2273  O   TRP C  71      33.512  25.145  45.128  1.00 15.01           O  
ANISOU 2273  O   TRP C  71     1829   2528   1345   -625    -66     54       O  
ATOM   2274  CB  TRP C  71      35.598  22.967  44.446  1.00 14.65           C  
ANISOU 2274  CB  TRP C  71     1044   3149   1375    -87    117     70       C  
ATOM   2275  CG  TRP C  71      36.750  22.282  43.783  1.00 14.69           C  
ANISOU 2275  CG  TRP C  71      936   3229   1418    -42    462     12       C  
ATOM   2276  CD1 TRP C  71      38.069  22.667  43.757  1.00 15.52           C  
ANISOU 2276  CD1 TRP C  71     1021   3274   1600   -164    581    -74       C  
ATOM   2277  CD2 TRP C  71      36.676  21.104  42.961  1.00 15.70           C  
ANISOU 2277  CD2 TRP C  71     1094   2975   1896   -183   -147    509       C  
ATOM   2278  NE1 TRP C  71      38.824  21.766  43.049  1.00 15.96           N  
ANISOU 2278  NE1 TRP C  71      987   3257   1821   -161    475    239       N  
ATOM   2279  CE2 TRP C  71      37.985  20.811  42.527  1.00 16.07           C  
ANISOU 2279  CE2 TRP C  71     1097   2979   2028    -37    254    501       C  
ATOM   2280  CE3 TRP C  71      35.620  20.256  42.588  1.00 16.11           C  
ANISOU 2280  CE3 TRP C  71     1260   3324   1535   -369    250    403       C  
ATOM   2281  CZ2 TRP C  71      38.271  19.718  41.715  1.00 15.79           C  
ANISOU 2281  CZ2 TRP C  71      918   3087   1994     75    600   -103       C  
ATOM   2282  CZ3 TRP C  71      35.920  19.175  41.790  1.00 15.88           C  
ANISOU 2282  CZ3 TRP C  71     1228   3287   1517   -319   -180    351       C  
ATOM   2283  CH2 TRP C  71      37.232  18.918  41.354  1.00 16.71           C  
ANISOU 2283  CH2 TRP C  71     1211   3348   1792   -327     55    128       C  
ATOM   2284  N   ARG C  72      32.421  23.608  43.883  1.00 12.32           N  
ANISOU 2284  N   ARG C  72      984   2375   1324     30    358    -84       N  
ATOM   2285  CA  ARG C  72      31.123  23.691  44.517  1.00 12.32           C  
ANISOU 2285  CA  ARG C  72     1048   1929   1705    125    256     35       C  
ATOM   2286  C   ARG C  72      30.602  22.290  44.848  1.00 11.49           C  
ANISOU 2286  C   ARG C  72     1052   1880   1435    125    264    -14       C  
ATOM   2287  O   ARG C  72      31.107  21.299  44.297  1.00 11.55           O  
ANISOU 2287  O   ARG C  72     1442   1923   1025     67    489   -139       O  
ATOM   2288  CB  ARG C  72      30.110  24.438  43.627  1.00 12.82           C  
ANISOU 2288  CB  ARG C  72     1309   1823   1738    251    -36    243       C  
ATOM   2289  CG  ARG C  72      30.444  25.950  43.561  1.00 15.58           C  
ANISOU 2289  CG  ARG C  72     1699   1856   2365    181   -222    275       C  
ATOM   2290  CD  ARG C  72      29.565  26.653  42.556  1.00 16.72           C  
ANISOU 2290  CD  ARG C  72     2437   1607   2307      9    194    363       C  
ATOM   2291  NE  ARG C  72      29.811  28.043  42.383  1.00 22.61           N  
ANISOU 2291  NE  ARG C  72     3874   1533   3184   -148   -288    495       N  
ATOM   2292  CZ  ARG C  72      29.419  29.098  43.055  1.00 23.71           C  
ANISOU 2292  CZ  ARG C  72     4377   1571   3061   -240    316    650       C  
ATOM   2293  NH1 ARG C  72      28.606  29.000  44.105  1.00 25.11           N  
ANISOU 2293  NH1 ARG C  72     4776   2262   2501    274   1110    308       N  
ATOM   2294  NH2 ARG C  72      29.838  30.318  42.692  1.00 29.09           N  
ANISOU 2294  NH2 ARG C  72     5367   1594   4094   -824   -643   1001       N  
ATOM   2295  N   GLU C  73      29.632  22.191  45.720  1.00 11.28           N  
ANISOU 2295  N   GLU C  73     1199   1531   1557    202    432    299       N  
ATOM   2296  CA  GLU C  73      29.091  20.905  46.169  1.00 11.45           C  
ANISOU 2296  CA  GLU C  73     1273   1520   1556     73    492    -44       C  
ATOM   2297  C   GLU C  73      27.562  20.862  46.018  1.00 11.42           C  
ANISOU 2297  C   GLU C  73     1255   1519   1564    152    680    -55       C  
ATOM   2298  O   GLU C  73      26.909  21.905  46.020  1.00 11.39           O  
ANISOU 2298  O   GLU C  73     1367   1493   1465    281    277    146       O  
ATOM   2299  CB  GLU C  73      29.446  20.640  47.624  1.00 11.46           C  
ANISOU 2299  CB  GLU C  73     1281   1483   1590    267    204   -222       C  
ATOM   2300  CG  GLU C  73      29.095  21.732  48.600  1.00 11.90           C  
ANISOU 2300  CG  GLU C  73     1507   1463   1552     30   -267    121       C  
ATOM   2301  CD  GLU C  73      29.113  21.237  50.046  1.00 12.46           C  
ANISOU 2301  CD  GLU C  73     1364   1835   1535    367   -290    -53       C  
ATOM   2302  OE1 GLU C  73      28.543  20.166  50.271  1.00 13.57           O  
ANISOU 2302  OE1 GLU C  73     2141   1786   1228    145   -136    515       O  
ATOM   2303  OE2 GLU C  73      29.695  21.905  50.916  1.00 20.13           O  
ANISOU 2303  OE2 GLU C  73     2865   3249   1535  -1173   -408    117       O  
ATOM   2304  N   ALA C  74      27.041  19.646  45.997  1.00  9.68           N  
ANISOU 2304  N   ALA C  74     1013   1473   1192    250    275    -80       N  
ATOM   2305  CA  ALA C  74      25.582  19.433  46.006  1.00  9.28           C  
ANISOU 2305  CA  ALA C  74     1023   1541    960    268    241    136       C  
ATOM   2306  C   ALA C  74      25.267  18.094  46.678  1.00  9.49           C  
ANISOU 2306  C   ALA C  74      949   1476   1182    280     70    379       C  
ATOM   2307  O   ALA C  74      26.033  17.133  46.552  1.00 10.10           O  
ANISOU 2307  O   ALA C  74     1147   1482   1210    428    379    137       O  
ATOM   2308  CB  ALA C  74      24.994  19.496  44.627  1.00 11.04           C  
ANISOU 2308  CB  ALA C  74     1118   2220    856    -35    216    384       C  
ATOM   2309  N   ASP C  75      24.184  18.061  47.453  1.00  9.60           N  
ANISOU 2309  N   ASP C  75      906   1590   1154    303    193    290       N  
ATOM   2310  CA  ASP C  75      23.736  16.850  48.113  1.00  9.27           C  
ANISOU 2310  CA  ASP C  75      790   1660   1073    328     67    376       C  
ATOM   2311  C   ASP C  75      23.103  15.853  47.095  1.00 10.98           C  
ANISOU 2311  C   ASP C  75     1429   1821    921     13    142    167       C  
ATOM   2312  O   ASP C  75      22.380  16.253  46.217  1.00 11.38           O  
ANISOU 2312  O   ASP C  75     1734   1832    758    114   -354    255       O  
ATOM   2313  CB  ASP C  75      22.710  17.112  49.194  1.00  9.99           C  
ANISOU 2313  CB  ASP C  75      729   2092    975    283    278    149       C  
ATOM   2314  CG  ASP C  75      23.226  17.821  50.427  1.00 11.22           C  
ANISOU 2314  CG  ASP C  75     1455   1804   1006    -17    -35    -15       C  
ATOM   2315  OD1 ASP C  75      24.339  18.393  50.381  1.00 11.31           O  
ANISOU 2315  OD1 ASP C  75     1224   2020   1051     60    167    199       O  
ATOM   2316  OD2 ASP C  75      22.552  17.740  51.458  1.00 11.23           O  
ANISOU 2316  OD2 ASP C  75     1200   2051   1014    153     24    474       O  
ATOM   2317  N   ILE C  76      23.451  14.583  47.308  1.00 10.30           N  
ANISOU 2317  N   ILE C  76     1197   1802    915    -73    -45     55       N  
ATOM   2318  CA  ILE C  76      22.969  13.488  46.444  1.00  9.98           C  
ANISOU 2318  CA  ILE C  76      880   1875   1036     66    189    150       C  
ATOM   2319  C   ILE C  76      22.163  12.504  47.291  1.00 11.54           C  
ANISOU 2319  C   ILE C  76     1132   2106   1147   -247     10    305       C  
ATOM   2320  O   ILE C  76      22.457  12.304  48.463  1.00 11.79           O  
ANISOU 2320  O   ILE C  76     1135   2215   1131   -241   -334    485       O  
ATOM   2321  CB  ILE C  76      24.146  12.830  45.734  1.00 10.12           C  
ANISOU 2321  CB  ILE C  76     1088   1876    881    164    121    136       C  
ATOM   2322  CG1 ILE C  76      24.891  13.787  44.770  1.00 10.57           C  
ANISOU 2322  CG1 ILE C  76     1085   2176    754    -93     97    515       C  
ATOM   2323  CG2 ILE C  76      23.776  11.568  44.982  1.00 12.42           C  
ANISOU 2323  CG2 ILE C  76     1661   1775   1285     41   -163   -322       C  
ATOM   2324  CD1 ILE C  76      24.039  14.256  43.619  1.00 11.30           C  
ANISOU 2324  CD1 ILE C  76     1434   2098    760   -231     34    257       C  
ATOM   2325  N   ASN C  77      21.126  11.903  46.707  1.00 12.40           N  
ANISOU 2325  N   ASN C  77     1240   2210   1261   -353   -121    308       N  
ATOM   2326  CA  ASN C  77      20.313  10.902  47.341  1.00 14.27           C  
ANISOU 2326  CA  ASN C  77     1480   2278   1664   -519     63    -71       C  
ATOM   2327  C   ASN C  77      19.439  11.387  48.469  1.00 14.07           C  
ANISOU 2327  C   ASN C  77     1170   2678   1498   -472    -30    429       C  
ATOM   2328  O   ASN C  77      18.932  10.605  49.267  1.00 17.15           O  
ANISOU 2328  O   ASN C  77     2221   2725   1571   -863    475    329       O  
ATOM   2329  CB  ASN C  77      21.119   9.678  47.736  1.00 16.79           C  
ANISOU 2329  CB  ASN C  77     2427   2077   1874   -291    109   -143       C  
ATOM   2330  CG  ASN C  77      21.751   8.936  46.585  1.00 16.67           C  
ANISOU 2330  CG  ASN C  77     2295   2080   1959    -25   -575    -22       C  
ATOM   2331  OD1 ASN C  77      21.173   8.785  45.496  1.00 18.15           O  
ANISOU 2331  OD1 ASN C  77     2797   2253   1845   -381   -179   -300       O  
ATOM   2332  ND2 ASN C  77      22.976   8.440  46.798  1.00 18.51           N  
ANISOU 2332  ND2 ASN C  77     1966   2459   2609    323   -152   -215       N  
ATOM   2333  N   TYR C  78      19.260  12.701  48.613  1.00 13.18           N  
ANISOU 2333  N   TYR C  78     1249   2673   1087   -186     85    212       N  
ATOM   2334  CA  TYR C  78      18.477  13.173  49.766  1.00 13.69           C  
ANISOU 2334  CA  TYR C  78     1222   2762   1219   -177   -176    -74       C  
ATOM   2335  C   TYR C  78      16.979  13.120  49.453  1.00 14.79           C  
ANISOU 2335  C   TYR C  78     1072   2971   1578   -144   -426    183       C  
ATOM   2336  O   TYR C  78      16.551  13.557  48.389  1.00 16.42           O  
ANISOU 2336  O   TYR C  78     1106   3688   1446   -332   -271    366       O  
ATOM   2337  CB  TYR C  78      18.875  14.643  50.079  1.00 13.29           C  
ANISOU 2337  CB  TYR C  78     1286   2772    992   -252   -129    -19       C  
ATOM   2338  CG  TYR C  78      18.031  15.213  51.196  1.00 12.90           C  
ANISOU 2338  CG  TYR C  78      895   2959   1049     82    236     83       C  
ATOM   2339  CD1 TYR C  78      18.306  14.870  52.520  1.00 13.70           C  
ANISOU 2339  CD1 TYR C  78     1370   2826   1009    267   -145    232       C  
ATOM   2340  CD2 TYR C  78      16.941  16.031  50.957  1.00 13.73           C  
ANISOU 2340  CD2 TYR C  78     1096   2877   1244    105    549   -152       C  
ATOM   2341  CE1 TYR C  78      17.521  15.351  53.552  1.00 14.12           C  
ANISOU 2341  CE1 TYR C  78     1808   2531   1027    259    243    119       C  
ATOM   2342  CE2 TYR C  78      16.160  16.527  51.975  1.00 13.66           C  
ANISOU 2342  CE2 TYR C  78     1366   2566   1258    324     49   -105       C  
ATOM   2343  CZ  TYR C  78      16.477  16.200  53.284  1.00 14.40           C  
ANISOU 2343  CZ  TYR C  78     1529   2719   1223    391    103     41       C  
ATOM   2344  OH  TYR C  78      15.686  16.637  54.298  1.00 14.85           O  
ANISOU 2344  OH  TYR C  78     1474   2918   1253    469     79    520       O  
ATOM   2345  N   THR C  79      16.193  12.684  50.435  1.00 16.73           N  
ANISOU 2345  N   THR C  79     1222   3553   1582   -485    155    131       N  
ATOM   2346  CA  THR C  79      14.743  12.655  50.355  1.00 18.90           C  
ANISOU 2346  CA  THR C  79     1144   4269   1770   -698   -200    560       C  
ATOM   2347  C   THR C  79      14.104  13.396  51.499  1.00 18.30           C  
ANISOU 2347  C   THR C  79      652   4558   1743   -358    -20    508       C  
ATOM   2348  O   THR C  79      13.294  14.310  51.285  1.00 19.20           O  
ANISOU 2348  O   THR C  79     1367   4470   1457    416    -78     58       O  
ATOM   2349  CB  THR C  79      14.178  11.265  50.152  1.00 22.80           C  
ANISOU 2349  CB  THR C  79     1827   4495   2342  -1319   -100    399       C  
ATOM   2350  OG1 THR C  79      14.618  10.347  51.140  1.00 28.32           O  
ANISOU 2350  OG1 THR C  79     4041   4183   2536  -1389    548    461       O  
ATOM   2351  CG2 THR C  79      14.605  10.678  48.817  1.00 22.36           C  
ANISOU 2351  CG2 THR C  79     1942   4048   2505  -1342    494   -499       C  
ATOM   2352  N   SER C  80      14.453  13.023  52.741  1.00 18.52           N  
ANISOU 2352  N   SER C  80     1509   3763   1768   -483   -187    366       N  
ATOM   2353  CA  SER C  80      13.924  13.692  53.924  1.00 17.50           C  
ANISOU 2353  CA  SER C  80     1164   3753   1733    -83   -150    485       C  
ATOM   2354  C   SER C  80      14.844  13.456  55.132  1.00 17.36           C  
ANISOU 2354  C   SER C  80     1413   3454   1728   -194    -12    618       C  
ATOM   2355  O   SER C  80      15.679  12.556  55.106  1.00 17.43           O  
ANISOU 2355  O   SER C  80     1683   3398   1543    -65    316   -204       O  
ATOM   2356  CB  SER C  80      12.520  13.216  54.267  1.00 18.64           C  
ANISOU 2356  CB  SER C  80     1307   3647   2129   -198   -615    514       C  
ATOM   2357  OG  SER C  80      12.458  11.871  54.584  1.00 24.96           O  
ANISOU 2357  OG  SER C  80     2934   3712   2839  -1066    244   -175       O  
ATOM   2358  N   GLY C  81      14.594  14.224  56.168  1.00 16.56           N  
ANISOU 2358  N   GLY C  81     1158   3395   1737   -297     32    344       N  
ATOM   2359  CA  GLY C  81      15.286  14.144  57.442  1.00 15.20           C  
ANISOU 2359  CA  GLY C  81     1015   3003   1760     27    106    163       C  
ATOM   2360  C   GLY C  81      16.594  14.916  57.445  1.00 13.16           C  
ANISOU 2360  C   GLY C  81     1188   2491   1322     48    395    217       C  
ATOM   2361  O   GLY C  81      16.742  15.873  56.717  1.00 13.60           O  
ANISOU 2361  O   GLY C  81     1409   2643   1115     99    172    480       O  
ATOM   2362  N   PHE C  82      17.530  14.478  58.291  1.00 12.80           N  
ANISOU 2362  N   PHE C  82     1200   2544   1117    130    350    423       N  
ATOM   2363  CA  PHE C  82      18.847  15.077  58.323  1.00 11.78           C  
ANISOU 2363  CA  PHE C  82     1019   2352   1107    372    328    524       C  
ATOM   2364  C   PHE C  82      19.559  14.798  57.000  1.00 11.97           C  
ANISOU 2364  C   PHE C  82     1214   2192   1142    214    179    -18       C  
ATOM   2365  O   PHE C  82      19.295  13.810  56.339  1.00 13.23           O  
ANISOU 2365  O   PHE C  82     1554   2427   1045    -49    426    -38       O  
ATOM   2366  CB  PHE C  82      19.695  14.546  59.476  1.00 12.17           C  
ANISOU 2366  CB  PHE C  82     1089   2330   1204    470     12    583       C  
ATOM   2367  CG  PHE C  82      19.213  15.054  60.823  1.00 12.46           C  
ANISOU 2367  CG  PHE C  82     1157   2457   1121    216     13    459       C  
ATOM   2368  CD1 PHE C  82      19.642  16.260  61.316  1.00 13.27           C  
ANISOU 2368  CD1 PHE C  82     1488   2467   1088    155   -219    617       C  
ATOM   2369  CD2 PHE C  82      18.257  14.325  61.533  1.00 16.27           C  
ANISOU 2369  CD2 PHE C  82     2079   3005   1097   -646    -46    216       C  
ATOM   2370  CE1 PHE C  82      19.164  16.720  62.540  1.00 13.91           C  
ANISOU 2370  CE1 PHE C  82     1578   2703   1005    228   -268    262       C  
ATOM   2371  CE2 PHE C  82      17.829  14.752  62.782  1.00 16.74           C  
ANISOU 2371  CE2 PHE C  82     1818   3438   1103   -562     68    535       C  
ATOM   2372  CZ  PHE C  82      18.220  16.007  63.222  1.00 15.40           C  
ANISOU 2372  CZ  PHE C  82     1742   3141    967    -12   -149    404       C  
ATOM   2373  N   ARG C  83      20.468  15.694  56.643  1.00 11.99           N  
ANISOU 2373  N   ARG C  83     1375   2219    960    156    165   -168       N  
ATOM   2374  CA  ARG C  83      21.278  15.468  55.461  1.00 12.11           C  
ANISOU 2374  CA  ARG C  83     1559   2138    904     49   -305     24       C  
ATOM   2375  C   ARG C  83      22.101  14.187  55.615  1.00 12.26           C  
ANISOU 2375  C   ARG C  83     1457   2074   1128   -155   -338    236       C  
ATOM   2376  O   ARG C  83      22.521  13.824  56.708  1.00 12.63           O  
ANISOU 2376  O   ARG C  83     1341   2323   1135    111     -8   -108       O  
ATOM   2377  CB  ARG C  83      22.167  16.674  55.221  1.00 11.46           C  
ANISOU 2377  CB  ARG C  83     1544   2099    711    119    -45    103       C  
ATOM   2378  CG  ARG C  83      21.424  17.900  54.730  1.00 12.92           C  
ANISOU 2378  CG  ARG C  83     1523   2089   1297    408    218    397       C  
ATOM   2379  CD  ARG C  83      22.320  19.144  54.789  1.00 13.20           C  
ANISOU 2379  CD  ARG C  83     1732   2155   1128    207    477     23       C  
ATOM   2380  NE  ARG C  83      23.379  19.110  53.771  1.00 12.59           N  
ANISOU 2380  NE  ARG C  83     1702   1920   1163    264   -180    -11       N  
ATOM   2381  CZ  ARG C  83      24.428  19.896  53.713  1.00 12.89           C  
ANISOU 2381  CZ  ARG C  83     1811   1922   1166    191    104   -277       C  
ATOM   2382  NH1 ARG C  83      24.773  20.712  54.718  1.00 13.91           N  
ANISOU 2382  NH1 ARG C  83     2186   1894   1205     -2    229   -550       N  
ATOM   2383  NH2 ARG C  83      25.198  19.887  52.620  1.00 14.05           N  
ANISOU 2383  NH2 ARG C  83     1638   2580   1119    167   -199   -369       N  
ATOM   2384  N   ASN C  84      22.329  13.508  54.495  1.00 12.24           N  
ANISOU 2384  N   ASN C  84     1490   2040   1120    -16   -261     11       N  
ATOM   2385  CA  ASN C  84      23.085  12.269  54.451  1.00 11.96           C  
ANISOU 2385  CA  ASN C  84     1432   2046   1065    -38    584     64       C  
ATOM   2386  C   ASN C  84      24.562  12.533  54.189  1.00 11.63           C  
ANISOU 2386  C   ASN C  84     1470   2007    944    -84    386     63       C  
ATOM   2387  O   ASN C  84      25.000  13.689  54.361  1.00 12.52           O  
ANISOU 2387  O   ASN C  84     1552   1988   1217    -48   -132    252       O  
ATOM   2388  CB  ASN C  84      22.483  11.338  53.402  1.00 12.43           C  
ANISOU 2388  CB  ASN C  84     1572   1982   1168   -146    165    293       C  
ATOM   2389  CG  ASN C  84      22.616  11.864  51.986  1.00 10.95           C  
ANISOU 2389  CG  ASN C  84     1314   1721   1124     -8     71     16       C  
ATOM   2390  OD1 ASN C  84      23.483  12.702  51.730  1.00 12.04           O  
ANISOU 2390  OD1 ASN C  84     1298   1910   1368   -173    -97    -98       O  
ATOM   2391  ND2 ASN C  84      21.777  11.357  51.080  1.00 15.39           N  
ANISOU 2391  ND2 ASN C  84     1925   2724   1198   -860   -140    -26       N  
ATOM   2392  N   SER C  85      25.351  11.516  53.877  1.00 11.40           N  
ANISOU 2392  N   SER C  85     1373   2058    902     29    163    121       N  
ATOM   2393  CA  SER C  85      26.793  11.611  53.742  1.00 12.12           C  
ANISOU 2393  CA  SER C  85      926   2572   1107    378   -206    427       C  
ATOM   2394  C   SER C  85      27.261  11.780  52.289  1.00 12.05           C  
ANISOU 2394  C   SER C  85     1142   2270   1165     87     17     68       C  
ATOM   2395  O   SER C  85      28.478  11.809  52.066  1.00 11.70           O  
ANISOU 2395  O   SER C  85     1242   2009   1194    123   -309    107       O  
ATOM   2396  CB  SER C  85      27.496  10.350  54.298  1.00 12.65           C  
ANISOU 2396  CB  SER C  85      852   2644   1309    498   -131    342       C  
ATOM   2397  OG  SER C  85      27.048   9.192  53.644  1.00 22.34           O  
ANISOU 2397  OG  SER C  85     2894   2526   3069   -304   -333    597       O  
ATOM   2398  N   ASP C  86      26.353  11.873  51.347  1.00 10.98           N  
ANISOU 2398  N   ASP C  86     1188   1853   1132    319    303   -118       N  
ATOM   2399  CA  ASP C  86      26.668  11.800  49.912  1.00 10.15           C  
ANISOU 2399  CA  ASP C  86      978   1748   1133    267    243   -144       C  
ATOM   2400  C   ASP C  86      26.664  13.192  49.273  1.00 10.43           C  
ANISOU 2400  C   ASP C  86     1113   1832   1018    151    172     29       C  
ATOM   2401  O   ASP C  86      25.714  13.965  49.411  1.00  9.93           O  
ANISOU 2401  O   ASP C  86     1190   1691    891    150   -175    -22       O  
ATOM   2402  CB  ASP C  86      25.589  10.949  49.207  1.00 11.39           C  
ANISOU 2402  CB  ASP C  86     1251   1853   1223     85   -241    349       C  
ATOM   2403  CG  ASP C  86      25.561   9.515  49.623  1.00 15.61           C  
ANISOU 2403  CG  ASP C  86     2686   1816   1429   -331   -433    283       C  
ATOM   2404  OD1 ASP C  86      26.432   9.051  50.372  1.00 16.29           O  
ANISOU 2404  OD1 ASP C  86     2681   1411   2098   -145   -476    162       O  
ATOM   2405  OD2 ASP C  86      24.639   8.786  49.194  1.00 18.79           O  
ANISOU 2405  OD2 ASP C  86     2399   2004   2735   -363   -520    173       O  
ATOM   2406  N   ARG C  87      27.752  13.492  48.565  1.00  9.35           N  
ANISOU 2406  N   ARG C  87     1055   1771    727    338    -68    218       N  
ATOM   2407  CA  ARG C  87      27.857  14.780  47.861  1.00  9.78           C  
ANISOU 2407  CA  ARG C  87     1144   1835    738    261   -243     -5       C  
ATOM   2408  C   ARG C  87      28.505  14.564  46.500  1.00  9.22           C  
ANISOU 2408  C   ARG C  87     1001   1666    834     46    242    186       C  
ATOM   2409  O   ARG C  87      29.420  13.751  46.346  1.00 10.56           O  
ANISOU 2409  O   ARG C  87     1138   1729   1146    420     50     45       O  
ATOM   2410  CB  ARG C  87      28.717  15.759  48.659  1.00  8.98           C  
ANISOU 2410  CB  ARG C  87      791   1811    810    492    -12   -210       C  
ATOM   2411  CG  ARG C  87      28.375  15.877  50.133  1.00 10.35           C  
ANISOU 2411  CG  ARG C  87     1296   1872    765    410    202   -127       C  
ATOM   2412  CD  ARG C  87      27.204  16.820  50.379  1.00 10.19           C  
ANISOU 2412  CD  ARG C  87     1488   1638    744    247     14     20       C  
ATOM   2413  NE  ARG C  87      26.963  16.993  51.838  1.00 10.87           N  
ANISOU 2413  NE  ARG C  87     1348   1997    786     67     91   -114       N  
ATOM   2414  CZ  ARG C  87      26.207  16.203  52.573  1.00 11.21           C  
ANISOU 2414  CZ  ARG C  87     1473   2071    715     95     98    257       C  
ATOM   2415  NH1 ARG C  87      25.462  15.269  51.993  1.00 11.94           N  
ANISOU 2415  NH1 ARG C  87     1606   2112    820    -61     39     70       N  
ATOM   2416  NH2 ARG C  87      26.054  16.396  53.875  1.00 13.62           N  
ANISOU 2416  NH2 ARG C  87     2107   2351    718    161    356    210       N  
ATOM   2417  N   ILE C  88      28.114  15.431  45.578  1.00  9.64           N  
ANISOU 2417  N   ILE C  88     1258   1694    711    311    270    314       N  
ATOM   2418  CA  ILE C  88      28.849  15.600  44.331  1.00 11.43           C  
ANISOU 2418  CA  ILE C  88     1575   2063    705    -67   -224    248       C  
ATOM   2419  C   ILE C  88      29.662  16.893  44.415  1.00  9.14           C  
ANISOU 2419  C   ILE C  88      880   1806    787    630    671   -154       C  
ATOM   2420  O   ILE C  88      29.162  17.865  44.999  1.00 10.03           O  
ANISOU 2420  O   ILE C  88      871   1774   1167    482    395   -243       O  
ATOM   2421  CB  ILE C  88      27.915  15.582  43.140  1.00 11.82           C  
ANISOU 2421  CB  ILE C  88     1292   2484    716    280    115     55       C  
ATOM   2422  CG1 ILE C  88      28.430  15.097  41.846  1.00 15.16           C  
ANISOU 2422  CG1 ILE C  88     2438   2647    675    621     24    -87       C  
ATOM   2423  CG2 ILE C  88      26.919  16.707  43.100  1.00 14.70           C  
ANISOU 2423  CG2 ILE C  88     1155   2578   1853    276    225    431       C  
ATOM   2424  CD1 ILE C  88      27.428  14.865  40.758  1.00 17.13           C  
ANISOU 2424  CD1 ILE C  88     2245   3639    623    772   -882   -659       C  
ATOM   2425  N   LEU C  89      30.910  16.845  43.997  1.00 10.68           N  
ANISOU 2425  N   LEU C  89     1102   1671   1284    369    605      0       N  
ATOM   2426  CA  LEU C  89      31.802  18.008  43.997  1.00 10.92           C  
ANISOU 2426  CA  LEU C  89     1201   1697   1251    336    604    -24       C  
ATOM   2427  C   LEU C  89      32.103  18.344  42.533  1.00 10.58           C  
ANISOU 2427  C   LEU C  89      837   1938   1245    374    417   -455       C  
ATOM   2428  O   LEU C  89      32.458  17.411  41.775  1.00 11.96           O  
ANISOU 2428  O   LEU C  89     1399   1851   1293    216    518     33       O  
ATOM   2429  CB  LEU C  89      33.140  17.691  44.715  1.00 11.77           C  
ANISOU 2429  CB  LEU C  89     1001   2290   1181    288     60    367       C  
ATOM   2430  CG  LEU C  89      33.142  17.924  46.222  1.00 13.96           C  
ANISOU 2430  CG  LEU C  89     1377   2741   1187     54     59    -52       C  
ATOM   2431  CD1 LEU C  89      33.153  19.380  46.568  1.00 16.44           C  
ANISOU 2431  CD1 LEU C  89     2537   2704   1006    845     21   -416       C  
ATOM   2432  CD2 LEU C  89      32.025  17.167  46.919  1.00 16.91           C  
ANISOU 2432  CD2 LEU C  89     1203   4027   1194   -147    362    575       C  
ATOM   2433  N   TYR C  90      31.830  19.563  42.127  1.00 12.16           N  
ANISOU 2433  N   TYR C  90     1795   1839    986     69    490     37       N  
ATOM   2434  CA  TYR C  90      32.017  19.932  40.730  1.00 11.31           C  
ANISOU 2434  CA  TYR C  90     1140   2160    997    170    416    428       C  
ATOM   2435  C   TYR C  90      32.858  21.179  40.590  1.00 12.17           C  
ANISOU 2435  C   TYR C  90     1217   2243   1163     34    282    742       C  
ATOM   2436  O   TYR C  90      32.680  22.159  41.334  1.00 13.58           O  
ANISOU 2436  O   TYR C  90     1764   2132   1264    -47    328    124       O  
ATOM   2437  CB  TYR C  90      30.711  20.025  39.991  1.00 11.81           C  
ANISOU 2437  CB  TYR C  90     1138   2257   1092     83    196    478       C  
ATOM   2438  CG  TYR C  90      29.715  21.026  40.496  1.00 12.37           C  
ANISOU 2438  CG  TYR C  90     1139   2176   1386    -54    131    381       C  
ATOM   2439  CD1 TYR C  90      28.907  20.756  41.581  1.00 12.61           C  
ANISOU 2439  CD1 TYR C  90     1140   2315   1338     53      0    198       C  
ATOM   2440  CD2 TYR C  90      29.584  22.270  39.886  1.00 14.00           C  
ANISOU 2440  CD2 TYR C  90     1809   2173   1337    110    206    125       C  
ATOM   2441  CE1 TYR C  90      27.993  21.651  42.064  1.00 13.28           C  
ANISOU 2441  CE1 TYR C  90     1154   2346   1544     18    206     73       C  
ATOM   2442  CE2 TYR C  90      28.645  23.187  40.354  1.00 15.24           C  
ANISOU 2442  CE2 TYR C  90     2013   2039   1740    104    430    194       C  
ATOM   2443  CZ  TYR C  90      27.839  22.863  41.424  1.00 14.62           C  
ANISOU 2443  CZ  TYR C  90     1400   2380   1776    496    529     13       C  
ATOM   2444  OH  TYR C  90      26.928  23.751  41.914  1.00 16.50           O  
ANISOU 2444  OH  TYR C  90     1623   2327   2320    276    148    -35       O  
ATOM   2445  N   SER C  91      33.778  21.203  39.617  1.00 13.82           N  
ANISOU 2445  N   SER C  91     1212   2960   1080   -198    140    403       N  
ATOM   2446  CA  SER C  91      34.640  22.374  39.445  1.00 17.04           C  
ANISOU 2446  CA  SER C  91     1658   3260   1555   -684    262    519       C  
ATOM   2447  C   SER C  91      34.112  23.296  38.355  1.00 17.64           C  
ANISOU 2447  C   SER C  91     2045   3028   1630   -624    538    604       C  
ATOM   2448  O   SER C  91      33.222  22.915  37.586  1.00 16.38           O  
ANISOU 2448  O   SER C  91     1546   2781   1896   -138    157    900       O  
ATOM   2449  CB  SER C  91      36.061  21.921  39.114  1.00 16.60           C  
ANISOU 2449  CB  SER C  91     1497   3514   1297   -706    122    636       C  
ATOM   2450  OG  SER C  91      36.164  21.416  37.820  1.00 17.94           O  
ANISOU 2450  OG  SER C  91     1608   3879   1328    100     33    181       O  
ATOM   2451  N   SER C  92      34.629  24.515  38.325  1.00 19.19           N  
ANISOU 2451  N   SER C  92     2086   3056   2150   -604    234    826       N  
ATOM   2452  CA  SER C  92      34.214  25.510  37.346  1.00 21.50           C  
ANISOU 2452  CA  SER C  92     2998   3005   2167   -888    -62   1294       C  
ATOM   2453  C   SER C  92      34.542  25.081  35.921  1.00 21.63           C  
ANISOU 2453  C   SER C  92     2549   3528   2142   -807   -369   1712       C  
ATOM   2454  O   SER C  92      33.920  25.557  34.965  1.00 22.06           O  
ANISOU 2454  O   SER C  92     2740   3484   2157    -51   -550   1031       O  
ATOM   2455  CB  SER C  92      34.789  26.866  37.683  1.00 24.88           C  
ANISOU 2455  CB  SER C  92     3733   2948   2773   -912   -124   1056       C  
ATOM   2456  OG  SER C  92      36.167  26.754  38.019  1.00 29.39           O  
ANISOU 2456  OG  SER C  92     3913   3725   3530  -2006   -298   1326       O  
ATOM   2457  N   ASP C  93      35.472  24.132  35.814  1.00 21.20           N  
ANISOU 2457  N   ASP C  93     2223   3694   2138   -486    533   1031       N  
ATOM   2458  CA  ASP C  93      35.869  23.504  34.592  1.00 21.37           C  
ANISOU 2458  CA  ASP C  93     2124   3946   2050   -816    393    569       C  
ATOM   2459  C   ASP C  93      35.327  22.106  34.408  1.00 20.15           C  
ANISOU 2459  C   ASP C  93     2103   3766   1787   -500    -85    128       C  
ATOM   2460  O   ASP C  93      35.669  21.355  33.495  1.00 21.30           O  
ANISOU 2460  O   ASP C  93     2555   4229   1309   -675    387    516       O  
ATOM   2461  CB  ASP C  93      37.340  23.663  34.294  1.00 23.32           C  
ANISOU 2461  CB  ASP C  93     2040   4684   2137   -881   -125    814       C  
ATOM   2462  CG  ASP C  93      38.268  23.038  35.300  1.00 23.09           C  
ANISOU 2462  CG  ASP C  93     1321   5339   2115   -368   -606    866       C  
ATOM   2463  OD1 ASP C  93      37.848  22.781  36.452  1.00 26.25           O  
ANISOU 2463  OD1 ASP C  93     2257   5758   1959   -434    186    673       O  
ATOM   2464  OD2 ASP C  93      39.458  22.824  34.972  1.00 26.32           O  
ANISOU 2464  OD2 ASP C  93     1340   5404   3255   -416    493    624       O  
ATOM   2465  N   TRP C  94      34.308  21.747  35.198  1.00 18.33           N  
ANISOU 2465  N   TRP C  94     2289   3041   1636   -478   -468    745       N  
ATOM   2466  CA  TRP C  94      33.507  20.584  35.029  1.00 17.35           C  
ANISOU 2466  CA  TRP C  94     2611   2862   1121   -429   -113    391       C  
ATOM   2467  C   TRP C  94      34.159  19.256  35.260  1.00 17.31           C  
ANISOU 2467  C   TRP C  94     2318   2983   1277     61     73    387       C  
ATOM   2468  O   TRP C  94      33.705  18.214  34.742  1.00 19.12           O  
ANISOU 2468  O   TRP C  94     2860   2973   1432    -42   -437    376       O  
ATOM   2469  CB  TRP C  94      32.641  20.600  33.760  1.00 16.86           C  
ANISOU 2469  CB  TRP C  94     1987   3028   1391   -127   -284    417       C  
ATOM   2470  CG  TRP C  94      31.953  21.922  33.581  1.00 17.44           C  
ANISOU 2470  CG  TRP C  94     2128   2981   1516    -51   -427    668       C  
ATOM   2471  CD1 TRP C  94      32.227  22.877  32.641  1.00 17.54           C  
ANISOU 2471  CD1 TRP C  94     2162   2994   1507     41   -108    832       C  
ATOM   2472  CD2 TRP C  94      30.915  22.447  34.402  1.00 17.65           C  
ANISOU 2472  CD2 TRP C  94     2155   2988   1563   -249   -321   1038       C  
ATOM   2473  NE1 TRP C  94      31.394  23.958  32.822  1.00 18.08           N  
ANISOU 2473  NE1 TRP C  94     2288   2916   1666   -100   -230    800       N  
ATOM   2474  CE2 TRP C  94      30.595  23.730  33.899  1.00 18.09           C  
ANISOU 2474  CE2 TRP C  94     2080   2959   1834   -148   -339    790       C  
ATOM   2475  CE3 TRP C  94      30.224  21.971  35.523  1.00 18.26           C  
ANISOU 2475  CE3 TRP C  94     2104   3370   1465   -200    -43    812       C  
ATOM   2476  CZ2 TRP C  94      29.609  24.532  34.477  1.00 18.51           C  
ANISOU 2476  CZ2 TRP C  94     1938   3059   2035   -268   -278    936       C  
ATOM   2477  CZ3 TRP C  94      29.259  22.778  36.083  1.00 18.43           C  
ANISOU 2477  CZ3 TRP C  94     1834   3482   1686   -178    -80    832       C  
ATOM   2478  CH2 TRP C  94      28.960  24.041  35.560  1.00 18.62           C  
ANISOU 2478  CH2 TRP C  94     1804   3537   1735    202    -14   1139       C  
ATOM   2479  N   LEU C  95      35.101  19.198  36.191  1.00 18.09           N  
ANISOU 2479  N   LEU C  95     2075   3109   1689    -70    490    433       N  
ATOM   2480  CA  LEU C  95      35.535  17.872  36.720  1.00 16.39           C  
ANISOU 2480  CA  LEU C  95     1455   3216   1558    375    619    133       C  
ATOM   2481  C   LEU C  95      34.466  17.498  37.794  1.00 14.20           C  
ANISOU 2481  C   LEU C  95     1171   2580   1645    770    635    150       C  
ATOM   2482  O   LEU C  95      33.935  18.395  38.454  1.00 15.00           O  
ANISOU 2482  O   LEU C  95     2081   2438   1181    497    523    451       O  
ATOM   2483  CB  LEU C  95      36.844  18.063  37.483  1.00 19.92           C  
ANISOU 2483  CB  LEU C  95     1428   3576   2566    138    -52    415       C  
ATOM   2484  CG  LEU C  95      38.113  18.312  36.696  1.00 20.72           C  
ANISOU 2484  CG  LEU C  95     1484   3820   2569    126   -219   -198       C  
ATOM   2485  CD1 LEU C  95      39.306  18.395  37.633  1.00 25.52           C  
ANISOU 2485  CD1 LEU C  95     1741   5317   2638   -907   -424     89       C  
ATOM   2486  CD2 LEU C  95      38.288  17.185  35.677  1.00 22.47           C  
ANISOU 2486  CD2 LEU C  95     2261   4004   2274    203    210     73       C  
ATOM   2487  N   ILE C  96      34.143  16.234  37.900  1.00 14.17           N  
ANISOU 2487  N   ILE C  96     2091   2505    790    594    235    147       N  
ATOM   2488  CA  ILE C  96      33.087  15.803  38.834  1.00 12.22           C  
ANISOU 2488  CA  ILE C  96     1739   2056    847    967    -46   -200       C  
ATOM   2489  C   ILE C  96      33.634  14.652  39.687  1.00 12.38           C  
ANISOU 2489  C   ILE C  96     1787   1997    921    806    557   -541       C  
ATOM   2490  O   ILE C  96      34.118  13.645  39.186  1.00 12.66           O  
ANISOU 2490  O   ILE C  96     2001   2001    808    825    164   -171       O  
ATOM   2491  CB AILE C  96      31.906  15.243  37.984  0.50 12.35           C  
ANISOU 2491  CB AILE C  96     1920   1974    800    896    104     16       C  
ATOM   2492  CB BILE C  96      31.805  15.381  38.142  0.50 12.85           C  
ANISOU 2492  CB BILE C  96     2063   2027    793    739    285    -47       C  
ATOM   2493  CG1AILE C  96      31.593  16.180  36.780  0.50 12.84           C  
ANISOU 2493  CG1AILE C  96     2174   1900    803    681    518   -361       C  
ATOM   2494  CG1BILE C  96      31.243  16.418  37.157  0.50 12.44           C  
ANISOU 2494  CG1BILE C  96     1645   1889   1194   1023    145   -187       C  
ATOM   2495  CG2AILE C  96      30.678  15.073  38.848  0.50 14.29           C  
ANISOU 2495  CG2AILE C  96     2478   1970    982    105   -114    522       C  
ATOM   2496  CG2BILE C  96      30.742  14.989  39.172  0.50 14.13           C  
ANISOU 2496  CG2BILE C  96     2020   2231   1119    532    464   -231       C  
ATOM   2497  CD1AILE C  96      30.738  17.367  37.214  0.70 15.12           C  
ANISOU 2497  CD1AILE C  96     2823   1694   1230    823    151    247       C  
ATOM   2498  CD1BILE C  96      29.966  16.011  36.487  0.50 13.83           C  
ANISOU 2498  CD1BILE C  96     2061   2093   1100    567     71   -479       C  
ATOM   2499  N   TYR C  97      33.523  14.807  40.996  1.00 10.66           N  
ANISOU 2499  N   TYR C  97     1141   1996    913    503    232   -524       N  
ATOM   2500  CA  TYR C  97      33.958  13.811  41.964  1.00 11.20           C  
ANISOU 2500  CA  TYR C  97     1401   2056    799    655    -91    116       C  
ATOM   2501  C   TYR C  97      32.773  13.505  42.900  1.00 11.27           C  
ANISOU 2501  C   TYR C  97     1338   2145    801    818     18    119       C  
ATOM   2502  O   TYR C  97      31.849  14.316  43.043  1.00 12.55           O  
ANISOU 2502  O   TYR C  97     1306   2135   1327    472     38    -13       O  
ATOM   2503  CB  TYR C  97      35.118  14.360  42.822  1.00 13.05           C  
ANISOU 2503  CB  TYR C  97     1527   2881    549    487    225    197       C  
ATOM   2504  CG  TYR C  97      36.461  14.312  42.122  1.00 14.17           C  
ANISOU 2504  CG  TYR C  97     1190   3300    896    598    485     82       C  
ATOM   2505  CD1 TYR C  97      36.752  15.168  41.057  1.00 15.94           C  
ANISOU 2505  CD1 TYR C  97     1597   3556    906     89    516   -215       C  
ATOM   2506  CD2 TYR C  97      37.441  13.408  42.493  1.00 15.96           C  
ANISOU 2506  CD2 TYR C  97     1120   3363   1582    935   -189    -26       C  
ATOM   2507  CE1 TYR C  97      37.947  15.093  40.387  1.00 17.04           C  
ANISOU 2507  CE1 TYR C  97     1365   3851   1258     77    583    303       C  
ATOM   2508  CE2 TYR C  97      38.644  13.327  41.829  1.00 17.68           C  
ANISOU 2508  CE2 TYR C  97     1107   3498   2112    635   -160    -72       C  
ATOM   2509  CZ  TYR C  97      38.912  14.181  40.784  1.00 18.39           C  
ANISOU 2509  CZ  TYR C  97     1288   3893   1806    493    549    141       C  
ATOM   2510  OH  TYR C  97      40.128  14.146  40.135  1.00 20.52           O  
ANISOU 2510  OH  TYR C  97     1212   4081   2502    283    243   -335       O  
ATOM   2511  N   LYS C  98      32.838  12.362  43.536  1.00 11.35           N  
ANISOU 2511  N   LYS C  98     1461   2190    663    625     77    270       N  
ATOM   2512  CA  LYS C  98      31.821  11.958  44.500  1.00 11.79           C  
ANISOU 2512  CA  LYS C  98     1186   2673    621    708   -201   -140       C  
ATOM   2513  C   LYS C  98      32.499  11.618  45.837  1.00 11.26           C  
ANISOU 2513  C   LYS C  98     1367   2241    669    710   -150   -127       C  
ATOM   2514  O   LYS C  98      33.643  11.173  45.894  1.00 11.53           O  
ANISOU 2514  O   LYS C  98     1160   2479    742    702   -106   -115       O  
ATOM   2515  CB  LYS C  98      31.051  10.771  43.989  1.00 17.01           C  
ANISOU 2515  CB  LYS C  98     2237   3241    986   -326   -639    129       C  
ATOM   2516  CG  LYS C  98      31.377   9.416  44.446  1.00 24.40           C  
ANISOU 2516  CG  LYS C  98     3862   2945   2466   -465  -1562   -325       C  
ATOM   2517  CD  LYS C  98      30.384   8.366  43.992  1.00 24.15           C  
ANISOU 2517  CD  LYS C  98     3229   3062   2883   -125  -1264     51       C  
ATOM   2518  CE  LYS C  98      31.019   7.087  43.574  1.00 29.00           C  
ANISOU 2518  CE  LYS C  98     4545   2761   3713   -123  -1876     70       C  
ATOM   2519  NZ  LYS C  98      29.984   6.000  43.421  1.00 39.72           N  
ANISOU 2519  NZ  LYS C  98     6599   3086   5405  -1526  -2912   -195       N  
ATOM   2520  N   THR C  99      31.738  11.899  46.893  1.00 10.59           N  
ANISOU 2520  N   THR C  99     1336   2034    654    598   -257    171       N  
ATOM   2521  CA  THR C  99      32.020  11.438  48.224  1.00 10.12           C  
ANISOU 2521  CA  THR C  99     1067   2120    660    636   -237   -161       C  
ATOM   2522  C   THR C  99      30.756  10.791  48.809  1.00 10.43           C  
ANISOU 2522  C   THR C  99     1452   1775    735    387   -574    104       C  
ATOM   2523  O   THR C  99      29.657  11.291  48.581  1.00 10.51           O  
ANISOU 2523  O   THR C  99     1354   1770    868    417   -324    220       O  
ATOM   2524  CB  THR C  99      32.589  12.479  49.157  1.00 10.51           C  
ANISOU 2524  CB  THR C  99     1125   2196    671    427   -199    -66       C  
ATOM   2525  OG1 THR C  99      32.878  11.951  50.456  1.00 11.50           O  
ANISOU 2525  OG1 THR C  99     1587   2120    664    418   -417    -87       O  
ATOM   2526  CG2 THR C  99      31.663  13.650  49.367  1.00 11.67           C  
ANISOU 2526  CG2 THR C  99     1547   2104    783    506   -341     34       C  
ATOM   2527  N   THR C 100      30.957   9.697  49.524  1.00 10.40           N  
ANISOU 2527  N   THR C 100     1300   1697    956    568   -278    394       N  
ATOM   2528  CA  THR C 100      29.880   9.053  50.269  1.00 11.52           C  
ANISOU 2528  CA  THR C 100     1516   1705   1158    177   -477    129       C  
ATOM   2529  C   THR C 100      30.170   8.966  51.747  1.00 11.17           C  
ANISOU 2529  C   THR C 100     1268   1853   1122    211   -611    321       C  
ATOM   2530  O   THR C 100      29.525   8.199  52.480  1.00 13.86           O  
ANISOU 2530  O   THR C 100     2224   1813   1228   -223   -379    124       O  
ATOM   2531  CB  THR C 100      29.552   7.669  49.707  1.00 14.30           C  
ANISOU 2531  CB  THR C 100     2518   1743   1173    -84   -484   -125       C  
ATOM   2532  OG1 THR C 100      30.702   6.798  49.792  1.00 19.45           O  
ANISOU 2532  OG1 THR C 100     2960   1534   2896    438    227    -74       O  
ATOM   2533  CG2 THR C 100      29.133   7.765  48.268  1.00 19.32           C  
ANISOU 2533  CG2 THR C 100     4282   2010   1048   -873   -423     68       C  
ATOM   2534  N   ASP C 101      31.192   9.681  52.201  1.00 11.66           N  
ANISOU 2534  N   ASP C 101     1284   2039   1106    212   -188    132       N  
ATOM   2535  CA  ASP C 101      31.676   9.602  53.569  1.00 11.37           C  
ANISOU 2535  CA  ASP C 101     1288   1956   1074    349   -507     46       C  
ATOM   2536  C   ASP C 101      32.017  10.973  54.132  1.00 11.00           C  
ANISOU 2536  C   ASP C 101     1070   1973   1139    180      2   -273       C  
ATOM   2537  O   ASP C 101      32.941  11.147  54.894  1.00 11.79           O  
ANISOU 2537  O   ASP C 101     1305   2131   1045    196   -186   -220       O  
ATOM   2538  CB  ASP C 101      32.845   8.634  53.665  1.00 11.63           C  
ANISOU 2538  CB  ASP C 101     1484   1966    968    432   -429   -217       C  
ATOM   2539  CG  ASP C 101      34.059   9.037  52.866  1.00 11.91           C  
ANISOU 2539  CG  ASP C 101     1290   1933   1303    427   -191    -99       C  
ATOM   2540  OD1 ASP C 101      34.090  10.150  52.296  1.00 11.85           O  
ANISOU 2540  OD1 ASP C 101     1360   1899   1242    265   -356     31       O  
ATOM   2541  OD2 ASP C 101      35.028   8.260  52.822  1.00 13.41           O  
ANISOU 2541  OD2 ASP C 101     1409   1983   1702    646   -196      4       O  
ATOM   2542  N   HIS C 102      31.169  11.970  53.849  1.00 11.25           N  
ANISOU 2542  N   HIS C 102     1235   1972   1067    207   -159   -235       N  
ATOM   2543  CA  HIS C 102      31.341  13.296  54.424  1.00 11.08           C  
ANISOU 2543  CA  HIS C 102     1238   1978    996    275    184   -229       C  
ATOM   2544  C   HIS C 102      32.704  13.890  54.097  1.00 10.40           C  
ANISOU 2544  C   HIS C 102     1289   1772    892    297   -267    121       C  
ATOM   2545  O   HIS C 102      33.371  14.462  54.954  1.00 11.68           O  
ANISOU 2545  O   HIS C 102     1386   2304    747    120   -326   -416       O  
ATOM   2546  CB  HIS C 102      31.071  13.358  55.908  1.00 13.85           C  
ANISOU 2546  CB  HIS C 102     1741   2679    842     42    704   -758       C  
ATOM   2547  CG  HIS C 102      29.652  13.278  56.335  1.00 16.25           C  
ANISOU 2547  CG  HIS C 102     1787   3437    950   -375    359   -574       C  
ATOM   2548  ND1 HIS C 102      29.132  12.177  56.946  1.00 19.69           N  
ANISOU 2548  ND1 HIS C 102     2544   3561   1376   -925    475   -220       N  
ATOM   2549  CD2 HIS C 102      28.629  14.165  56.276  1.00 18.45           C  
ANISOU 2549  CD2 HIS C 102     1519   3587   1905   -627     76   -204       C  
ATOM   2550  CE1 HIS C 102      27.850  12.346  57.223  1.00 20.32           C  
ANISOU 2550  CE1 HIS C 102     2444   4009   1266  -1116    608   -372       C  
ATOM   2551  NE2 HIS C 102      27.540  13.596  56.825  1.00 20.31           N  
ANISOU 2551  NE2 HIS C 102     1744   4036   1935   -869    326   -485       N  
ATOM   2552  N   TYR C 103      33.064  13.886  52.822  1.00  9.70           N  
ANISOU 2552  N   TYR C 103     1169   1694    821    371   -559   -351       N  
ATOM   2553  CA  TYR C 103      34.251  14.621  52.378  1.00 10.30           C  
ANISOU 2553  CA  TYR C 103     1414   1700    799    137   -325   -312       C  
ATOM   2554  C   TYR C 103      35.539  14.025  52.873  1.00 10.24           C  
ANISOU 2554  C   TYR C 103     1181   1841    870    277   -296   -190       C  
ATOM   2555  O   TYR C 103      36.591  14.694  52.800  1.00 11.80           O  
ANISOU 2555  O   TYR C 103     1207   1995   1282    312   -263   -124       O  
ATOM   2556  CB  TYR C 103      34.170  16.100  52.685  1.00 10.89           C  
ANISOU 2556  CB  TYR C 103     1476   1707    956    256    205    -65       C  
ATOM   2557  CG  TYR C 103      32.876  16.836  52.573  1.00 10.84           C  
ANISOU 2557  CG  TYR C 103     1263   1837   1019    501    256   -169       C  
ATOM   2558  CD1 TYR C 103      32.374  17.322  51.373  1.00 10.90           C  
ANISOU 2558  CD1 TYR C 103     1163   1942   1037    235    161   -357       C  
ATOM   2559  CD2 TYR C 103      32.084  17.067  53.708  1.00 11.22           C  
ANISOU 2559  CD2 TYR C 103     1247   1960   1055    356   -380   -114       C  
ATOM   2560  CE1 TYR C 103      31.166  18.012  51.305  1.00 11.25           C  
ANISOU 2560  CE1 TYR C 103     1144   1945   1185    199   -176   -208       C  
ATOM   2561  CE2 TYR C 103      30.911  17.770  53.652  1.00 11.36           C  
ANISOU 2561  CE2 TYR C 103     1026   2111   1180    504   -297     43       C  
ATOM   2562  CZ  TYR C 103      30.439  18.238  52.440  1.00 11.13           C  
ANISOU 2562  CZ  TYR C 103     1025   1997   1207    297   -117   -422       C  
ATOM   2563  OH  TYR C 103      29.227  18.911  52.410  1.00 11.34           O  
ANISOU 2563  OH  TYR C 103     1277   1784   1246    342    103    306       O  
ATOM   2564  N   GLN C 104      35.546  12.781  53.317  1.00 10.13           N  
ANISOU 2564  N   GLN C 104      906   1927   1017    419   -116    -12       N  
ATOM   2565  CA  GLN C 104      36.759  12.102  53.743  1.00 10.44           C  
ANISOU 2565  CA  GLN C 104      961   1943   1062    502    -37     32       C  
ATOM   2566  C   GLN C 104      37.555  11.549  52.600  1.00 10.57           C  
ANISOU 2566  C   GLN C 104      794   2170   1053    624   -440     24       C  
ATOM   2567  O   GLN C 104      38.780  11.721  52.533  1.00 11.21           O  
ANISOU 2567  O   GLN C 104      931   2318   1012    415   -220     33       O  
ATOM   2568  CB  GLN C 104      36.479  11.042  54.816  1.00 10.85           C  
ANISOU 2568  CB  GLN C 104     1038   2009   1074    433   -251   -226       C  
ATOM   2569  CG  GLN C 104      36.089  11.731  56.134  1.00 12.50           C  
ANISOU 2569  CG  GLN C 104     1261   2472   1018    651   -152   -487       C  
ATOM   2570  CD  GLN C 104      35.750  10.700  57.207  1.00 14.75           C  
ANISOU 2570  CD  GLN C 104     1961   2731    912    300   -625    153       C  
ATOM   2571  OE1 GLN C 104      36.451  10.585  58.210  1.00 14.99           O  
ANISOU 2571  OE1 GLN C 104     1648   3148    901    668   -120      8       O  
ATOM   2572  NE2 GLN C 104      34.675   9.966  56.970  1.00 14.15           N  
ANISOU 2572  NE2 GLN C 104     2092   2380    904    340   -115   -216       N  
ATOM   2573  N   THR C 105      36.867  10.846  51.707  1.00 11.95           N  
ANISOU 2573  N   THR C 105      916   2839    786    442   -105   -224       N  
ATOM   2574  CA  THR C 105      37.481  10.339  50.490  1.00 12.72           C  
ANISOU 2574  CA  THR C 105     1120   2892    819    810   -334     97       C  
ATOM   2575  C   THR C 105      36.633  10.732  49.273  1.00 12.67           C  
ANISOU 2575  C   THR C 105      920   3106    789    852    167   -220       C  
ATOM   2576  O   THR C 105      35.418  10.958  49.380  1.00 12.82           O  
ANISOU 2576  O   THR C 105     1027   2897    947    849    -28   -283       O  
ATOM   2577  CB  THR C 105      37.651   8.820  50.509  1.00 14.86           C  
ANISOU 2577  CB  THR C 105     1444   2828   1375    966   -257   -248       C  
ATOM   2578  OG1 THR C 105      36.376   8.172  50.582  1.00 16.98           O  
ANISOU 2578  OG1 THR C 105     1641   2804   2005    782   -477   -541       O  
ATOM   2579  CG2 THR C 105      38.481   8.370  51.696  1.00 15.43           C  
ANISOU 2579  CG2 THR C 105     1660   2666   1538   1067   -465    125       C  
ATOM   2580  N   PHE C 106      37.322  10.785  48.123  1.00 13.89           N  
ANISOU 2580  N   PHE C 106      890   3543    844    779     25   -139       N  
ATOM   2581  CA  PHE C 106      36.650  11.170  46.898  1.00 15.18           C  
ANISOU 2581  CA  PHE C 106     1595   3415    756    547   -382    -88       C  
ATOM   2582  C   PHE C 106      37.059  10.219  45.760  1.00 15.03           C  
ANISOU 2582  C   PHE C 106     1487   3382    840   1275   -537   -411       C  
ATOM   2583  O   PHE C 106      38.209   9.786  45.708  1.00 16.83           O  
ANISOU 2583  O   PHE C 106     1386   3632   1377   1293   -457   -403       O  
ATOM   2584  CB  PHE C 106      37.034  12.581  46.478  1.00 15.64           C  
ANISOU 2584  CB  PHE C 106     1367   3363   1212    355   -116    -59       C  
ATOM   2585  CG  PHE C 106      36.624  13.684  47.424  1.00 15.14           C  
ANISOU 2585  CG  PHE C 106     1260   3410   1083     78     75   -477       C  
ATOM   2586  CD1 PHE C 106      35.386  14.269  47.340  1.00 15.30           C  
ANISOU 2586  CD1 PHE C 106     1560   3139   1114    -14     69    393       C  
ATOM   2587  CD2 PHE C 106      37.505  14.143  48.400  1.00 16.70           C  
ANISOU 2587  CD2 PHE C 106     1591   3355   1401   -453    -57   -742       C  
ATOM   2588  CE1 PHE C 106      34.993  15.291  48.192  1.00 16.08           C  
ANISOU 2588  CE1 PHE C 106     1909   3025   1176   -149    257    140       C  
ATOM   2589  CE2 PHE C 106      37.141  15.182  49.227  1.00 17.73           C  
ANISOU 2589  CE2 PHE C 106     2014   3201   1520   -555   -130   -687       C  
ATOM   2590  CZ  PHE C 106      35.879  15.753  49.140  1.00 16.86           C  
ANISOU 2590  CZ  PHE C 106     2063   3091   1253   -395    309   -286       C  
ATOM   2591  N   THR C 107      36.150  10.058  44.836  1.00 14.97           N  
ANISOU 2591  N   THR C 107     1861   2994    834   1030   -344   -176       N  
ATOM   2592  CA  THR C 107      36.404   9.280  43.608  1.00 14.40           C  
ANISOU 2592  CA  THR C 107     1579   3011    883   1347   -309   -149       C  
ATOM   2593  C   THR C 107      35.963  10.132  42.422  1.00 13.92           C  
ANISOU 2593  C   THR C 107     1476   2934    879   1398   -188   -306       C  
ATOM   2594  O   THR C 107      34.886  10.721  42.407  1.00 13.70           O  
ANISOU 2594  O   THR C 107     1678   2863    664   1240     82    -92       O  
ATOM   2595  CB  THR C 107      35.474   8.013  43.637  1.00 21.31           C  
ANISOU 2595  CB  THR C 107     3710   2739   1647    547   -417    319       C  
ATOM   2596  OG1 THR C 107      35.742   7.313  44.858  1.00 22.18           O  
ANISOU 2596  OG1 THR C 107     3903   2832   1693    857    -52     95       O  
ATOM   2597  CG2 THR C 107      35.858   7.078  42.494  1.00 24.96           C  
ANISOU 2597  CG2 THR C 107     5138   2672   1672    931   -360   -164       C  
ATOM   2598  N   LYS C 108      36.791  10.108  41.373  1.00 14.22           N  
ANISOU 2598  N   LYS C 108     1777   2703    923    853     12   -190       N  
ATOM   2599  CA  LYS C 108      36.387  10.806  40.142  1.00 14.47           C  
ANISOU 2599  CA  LYS C 108     1921   2598    979   1007   -210     33       C  
ATOM   2600  C   LYS C 108      35.275   9.994  39.464  1.00 13.28           C  
ANISOU 2600  C   LYS C 108     2089   2169    789   1062    250   -201       C  
ATOM   2601  O   LYS C 108      35.395   8.778  39.323  1.00 15.44           O  
ANISOU 2601  O   LYS C 108     2582   2168   1116   1190   -338   -226       O  
ATOM   2602  CB  LYS C 108      37.615  10.835  39.214  1.00 16.80           C  
ANISOU 2602  CB  LYS C 108     2102   3398    883    695    364   -120       C  
ATOM   2603  CG  LYS C 108      37.363  11.462  37.865  1.00 19.43           C  
ANISOU 2603  CG  LYS C 108     2920   3585    878    517    793    -88       C  
ATOM   2604  CD  LYS C 108      38.632  11.389  36.986  1.00 20.84           C  
ANISOU 2604  CD  LYS C 108     3252   3840    824   -139    819   -148       C  
ATOM   2605  CE  LYS C 108      38.387  12.032  35.655  1.00 22.04           C  
ANISOU 2605  CE  LYS C 108     4290   3099    987     -2    -30   -367       C  
ATOM   2606  NZ  LYS C 108      37.948  13.457  35.795  1.00 33.94           N  
ANISOU 2606  NZ  LYS C 108     6758   2788   3351   -441   -829   -587       N  
ATOM   2607  N   ILE C 109      34.247  10.696  39.001  1.00 13.09           N  
ANISOU 2607  N   ILE C 109     2146   2109    718    860   -240   -115       N  
ATOM   2608  CA  ILE C 109      33.143  10.119  38.302  1.00 13.22           C  
ANISOU 2608  CA  ILE C 109     2316   1834    873    765   -266   -335       C  
ATOM   2609  C   ILE C 109      32.874  10.612  36.906  1.00 12.55           C  
ANISOU 2609  C   ILE C 109     2157   1746    864    547   -301   -103       C  
ATOM   2610  O   ILE C 109      32.131   9.986  36.142  1.00 13.41           O  
ANISOU 2610  O   ILE C 109     2410   1724    962    352   -488    -55       O  
ATOM   2611  CB  ILE C 109      31.859  10.003  39.107  1.00 13.70           C  
ANISOU 2611  CB  ILE C 109     2453   2000    754    528    -73    218       C  
ATOM   2612  CG1 ILE C 109      31.209  11.354  39.434  1.00 13.08           C  
ANISOU 2612  CG1 ILE C 109     1884   2149    936    712     77   -494       C  
ATOM   2613  CG2 ILE C 109      32.027   9.133  40.331  1.00 14.47           C  
ANISOU 2613  CG2 ILE C 109     2625   2087    786    676    135    273       C  
ATOM   2614  CD1 ILE C 109      29.774  11.240  39.866  1.00 16.83           C  
ANISOU 2614  CD1 ILE C 109     1736   2642   2017    464    196   -171       C  
ATOM   2615  N   ARG C 110      33.481  11.720  36.509  1.00 13.75           N  
ANISOU 2615  N   ARG C 110     2480   1770    975    401   -707     86       N  
ATOM   2616  CA  ARG C 110      33.465  12.268  35.202  1.00 14.11           C  
ANISOU 2616  CA  ARG C 110     2633   1850    878    278  -1019    560       C  
ATOM   2617  C   ARG C 110      34.789  13.062  34.976  1.00 19.46           C  
ANISOU 2617  C   ARG C 110     3211   2737   1447   -630    -35    245       C  
ATOM   2618  O   ARG C 110      35.188  13.130  33.803  1.00 19.68           O  
ANISOU 2618  O   ARG C 110     2435   3593   1451   -176    141    259       O  
ATOM   2619  CB  ARG C 110      32.313  13.163  34.846  1.00 14.58           C  
ANISOU 2619  CB  ARG C 110     2955   1607    977    333   -967    229       C  
ATOM   2620  CG  ARG C 110      30.911  12.700  34.907  1.00 14.60           C  
ANISOU 2620  CG  ARG C 110     2676   1686   1188    521   -390   -115       C  
ATOM   2621  CD  ARG C 110      30.517  11.663  33.897  1.00 14.09           C  
ANISOU 2621  CD  ARG C 110     2350   2293    709    524    -86   -130       C  
ATOM   2622  NE  ARG C 110      29.089  11.336  33.982  1.00 16.48           N  
ANISOU 2622  NE  ARG C 110     2399   2761   1101    306   -477    180       N  
ATOM   2623  CZ  ARG C 110      28.586  10.407  34.783  1.00 16.20           C  
ANISOU 2623  CZ  ARG C 110     2218   2802   1135    417   -768    326       C  
ATOM   2624  NH1 ARG C 110      29.338   9.775  35.667  1.00 17.11           N  
ANISOU 2624  NH1 ARG C 110     2567   2594   1340    508   -351    234       N  
ATOM   2625  NH2 ARG C 110      27.269  10.154  34.725  1.00 19.89           N  
ANISOU 2625  NH2 ARG C 110     2557   2703   2296     -6   -469   -875       N  
ATOM   2626  OXT ARG C 110      35.186  13.726  35.951  1.00 20.92           O  
ANISOU 2626  OXT ARG C 110     2769   3762   1418   -678    247   -118       O  
TER    2627      ARG C 110                                                      
HETATM 2628 ZN    ZN A 112      33.898  42.301  55.562  0.30 41.80          ZN  
ANISOU 2628 ZN    ZN A 112     6550   5943   3390   1326  -1310   2128      ZN  
HETATM 2629 ZN    ZN B 112       8.869  30.194  74.011  0.35 32.13          ZN  
ANISOU 2629 ZN    ZN B 112     3821   4909   3479   1260    990    201      ZN  
HETATM 2630 ZN    ZN C 112      39.324  15.495  56.124  1.00 12.86          ZN  
ANISOU 2630 ZN    ZN C 112     1419   2253   1215    328   -127    -77      ZN  
HETATM 2631  O   HOH A 113      22.075  43.686  37.103  1.00 12.40           O  
ANISOU 2631  O   HOH A 113     2039   1599   1075    -86    114   -133       O  
HETATM 2632  O   HOH A 114      30.344  45.360  35.202  1.00 15.19           O  
ANISOU 2632  O   HOH A 114     1678   2182   1910    106   -341   -630       O  
HETATM 2633  O   HOH A 115      23.736  45.450  31.979  1.00 12.56           O  
ANISOU 2633  O   HOH A 115     1995   1491   1288   -381    -32    -38       O  
HETATM 2634  O   HOH A 116      20.156  37.244  27.180  1.00 13.73           O  
ANISOU 2634  O   HOH A 116     2169   1598   1449     59    598   -293       O  
HETATM 2635  O   HOH A 117      24.281  39.654  26.872  1.00 14.36           O  
ANISOU 2635  O   HOH A 117     2127   1719   1610    427   -227    -73       O  
HETATM 2636  O   HOH A 118      25.796  41.292  25.354  1.00 15.66           O  
ANISOU 2636  O   HOH A 118     1646   3034   1270    108    123     49       O  
HETATM 2637  O   HOH A 119      25.460  58.912  34.827  1.00 20.28           O  
ANISOU 2637  O   HOH A 119     4111   1295   2300    -33    259    297       O  
HETATM 2638  O   HOH A 120      21.259  39.055  38.119  1.00 17.67           O  
ANISOU 2638  O   HOH A 120     3124   1851   1739   -289    838     44       O  
HETATM 2639  O   HOH A 121      25.005  41.844  33.184  1.00 14.40           O  
ANISOU 2639  O   HOH A 121     1891   1672   1910   -374    -48   -196       O  
HETATM 2640  O   HOH A 122      27.190  57.065  52.614  1.00 18.76           O  
ANISOU 2640  O   HOH A 122     2970   2228   1928     -2   -266   -916       O  
HETATM 2641  O   HOH A 123      32.439  43.504  35.943  1.00 20.07           O  
ANISOU 2641  O   HOH A 123     2802   2208   2616    370   -337   -994       O  
HETATM 2642  O   HOH A 124      26.854  43.786  25.914  1.00 21.27           O  
ANISOU 2642  O   HOH A 124     4403   2512   1165   -126    539   -207       O  
HETATM 2643  O   HOH A 125      35.162  56.866  32.422  1.00 39.68           O  
ANISOU 2643  O   HOH A 125     4541   5263   5272   -196   1859   -164       O  
HETATM 2644  O   HOH A 126      29.599  44.007  26.684  1.00 20.40           O  
ANISOU 2644  O   HOH A 126     4257   2533    960    111     78   -346       O  
HETATM 2645  O   HOH A 127      18.100  43.698  31.036  1.00 20.34           O  
ANISOU 2645  O   HOH A 127     3332   2108   2290   -344   -544   -140       O  
HETATM 2646  O   HOH A 128      18.047  50.209  40.385  1.00 20.68           O  
ANISOU 2646  O   HOH A 128     2566   2673   2620   -312   -277   -435       O  
HETATM 2647  O   HOH A 129      38.447  53.103  32.464  1.00 51.01           O  
ANISOU 2647  O   HOH A 129     4974   7480   6928     56   2737    121       O  
HETATM 2648  O   HOH A 130      17.662  51.541  43.534  1.00 24.43           O  
ANISOU 2648  O   HOH A 130     2501   3964   2818   -269     56   -888       O  
HETATM 2649  O   HOH A 131      37.506  57.710  34.639  1.00 36.21           O  
ANISOU 2649  O   HOH A 131     5760   3280   4719    433   1313   1277       O  
HETATM 2650  O   HOH A 132      36.818  48.003  44.653  1.00 23.60           O  
ANISOU 2650  O   HOH A 132     3687   2507   2775    858   -949   -438       O  
HETATM 2651  O   HOH A 133      22.715  30.149  36.521  1.00 40.99           O  
ANISOU 2651  O   HOH A 133     7768   4255   3553    615  -1373    467       O  
HETATM 2652  O   HOH A 134      41.094  50.670  39.858  1.00 26.69           O  
ANISOU 2652  O   HOH A 134     2110   3975   4056   -258   -263  -1226       O  
HETATM 2653  O   HOH A 135      19.040  39.392  36.599  1.00 24.01           O  
ANISOU 2653  O   HOH A 135     3646   2653   2823   -743   -225    564       O  
HETATM 2654  O   HOH A 136      20.562  44.898  49.885  1.00 38.33           O  
ANISOU 2654  O   HOH A 136     7068   4943   2552  -1217   2061     49       O  
HETATM 2655  O   HOH A 137      24.619  51.671  52.841  1.00 30.72           O  
ANISOU 2655  O   HOH A 137     4067   3117   4487     36   1945   -229       O  
HETATM 2656  O   HOH A 138      28.376  29.874  23.509  1.00 18.34           O  
ANISOU 2656  O   HOH A 138     3325   1948   1695    366   -178   -821       O  
HETATM 2657  O   HOH A 139      24.613  62.234  43.882  1.00 24.15           O  
ANISOU 2657  O   HOH A 139     4339   2746   2092    367   -328    140       O  
HETATM 2658  O   HOH A 140      31.464  62.552  36.153  1.00 32.37           O  
ANISOU 2658  O   HOH A 140     6171   3478   2652  -2873   1319   -577       O  
HETATM 2659  O   HOH A 141      32.585  40.486  45.245  1.00 31.53           O  
ANISOU 2659  O   HOH A 141     5549   3476   2954    477   -479   -205       O  
HETATM 2660  O   HOH A 142      25.989  53.979  54.203  1.00 37.48           O  
ANISOU 2660  O   HOH A 142     5970   4283   3990   1431   -735   -780       O  
HETATM 2661  O   HOH A 143      21.070  52.865  53.078  1.00 22.85           O  
ANISOU 2661  O   HOH A 143     4405   2265   2014   -614   -124    -78       O  
HETATM 2662  O   HOH A 144      21.725  36.320  33.066  1.00 23.83           O  
ANISOU 2662  O   HOH A 144     3253   3030   2770    330   -250    479       O  
HETATM 2663  O   HOH A 145      18.261  55.786  48.154  1.00 22.65           O  
ANISOU 2663  O   HOH A 145     2642   2505   3461   -380    905   -936       O  
HETATM 2664  O   HOH A 146      29.962  48.125  28.939  1.00 28.64           O  
ANISOU 2664  O   HOH A 146     3883   3494   3502    418   1443   -220       O  
HETATM 2665  O   HOH A 147      37.000  39.111  34.162  1.00 27.16           O  
ANISOU 2665  O   HOH A 147     2338   3375   4609    510   -609  -2265       O  
HETATM 2666  O   HOH A 148      32.181  32.817  25.159  1.00 20.90           O  
ANISOU 2666  O   HOH A 148     2665   2582   2695    487    407    -78       O  
HETATM 2667  O   HOH A 149      31.818  38.607  40.612  1.00 29.22           O  
ANISOU 2667  O   HOH A 149     6561   2368   2174    714   -643   -599       O  
HETATM 2668  O   HOH A 150      34.237  42.610  44.563  1.00 30.72           O  
ANISOU 2668  O   HOH A 150     5492   2081   4097   1245  -1523   -166       O  
HETATM 2669  O   HOH A 151      32.618  45.825  31.846  1.00 29.02           O  
ANISOU 2669  O   HOH A 151     3001   4129   3896     18    219  -1611       O  
HETATM 2670  O   HOH A 152      19.676  37.424  34.344  1.00 30.58           O  
ANISOU 2670  O   HOH A 152     5339   3656   2623   -452    861   1263       O  
HETATM 2671  O   HOH A 153      18.898  28.703  28.943  1.00 32.81           O  
ANISOU 2671  O   HOH A 153     2675   3955   5837  -1292   1454   -873       O  
HETATM 2672  O   HOH A 154      31.726  37.622  24.942  1.00 24.36           O  
ANISOU 2672  O   HOH A 154     3294   3569   2394    335   -209    433       O  
HETATM 2673  O   HOH A 155      20.157  34.645  40.244  1.00 41.26           O  
ANISOU 2673  O   HOH A 155     7759   4808   3110  -2601   -106   1016       O  
HETATM 2674  O   HOH A 156      19.528  45.059  29.308  1.00 30.55           O  
ANISOU 2674  O   HOH A 156     3379   4023   4207    505   1753   -991       O  
HETATM 2675  O   HOH A 157      30.821  55.890  51.549  1.00 31.42           O  
ANISOU 2675  O   HOH A 157     4224   3639   4076   1315   -682   -512       O  
HETATM 2676  O   HOH A 158      32.951  30.105  34.126  1.00 24.58           O  
ANISOU 2676  O   HOH A 158     4136   2166   3036   1039  -1184    206       O  
HETATM 2677  O   HOH A 159      24.134  39.882  16.809  1.00 33.08           O  
ANISOU 2677  O   HOH A 159     4223   5482   2862  -2445  -1905    715       O  
HETATM 2678  O   HOH A 160      33.118  40.259  25.697  1.00 39.62           O  
ANISOU 2678  O   HOH A 160     5271   5890   3891  -1355    226   -407       O  
HETATM 2679  O   HOH A 161      36.127  46.574  33.877  1.00 32.81           O  
ANISOU 2679  O   HOH A 161     4315   4654   3496   1327    554    445       O  
HETATM 2680  O   HOH A 162      42.622  55.192  43.224  1.00 39.26           O  
ANISOU 2680  O   HOH A 162     5282   5156   4480  -1373     17  -1481       O  
HETATM 2681  O   HOH A 163      40.673  60.980  40.830  1.00 79.58           O  
ANISOU 2681  O   HOH A 163    10404  10231   9601   -554    591    -13       O  
HETATM 2682  O   HOH A 164      42.102  53.362  38.915  1.00 55.21           O  
ANISOU 2682  O   HOH A 164     6697   6554   7726    922    503   -610       O  
HETATM 2683  O   HOH A 165      38.976  42.323  36.345  1.00 39.80           O  
ANISOU 2683  O   HOH A 165     4694   3951   6479   1101   -700   -457       O  
HETATM 2684  O   HOH A 166      38.133  49.733  32.675  1.00 41.02           O  
ANISOU 2684  O   HOH A 166     5148   5725   4714   -224   1129  -2129       O  
HETATM 2685  O   HOH A 167      17.725  47.807  31.846  1.00 37.66           O  
ANISOU 2685  O   HOH A 167     4658   6062   3590  -1347   -915    160       O  
HETATM 2686  O   HOH A 168      24.861  59.568  37.511  1.00 29.62           O  
ANISOU 2686  O   HOH A 168     5882   3331   2042   -166   -230   -966       O  
HETATM 2687  O   HOH A 169      29.106  37.192  43.135  1.00 37.42           O  
ANISOU 2687  O   HOH A 169     6176   5196   2845    319   -931   -428       O  
HETATM 2688  O   HOH A 170      32.509  45.662  28.427  1.00 58.76           O  
ANISOU 2688  O   HOH A 170     6875   8226   7225   -261    858    -14       O  
HETATM 2689  O   HOH A 171      34.546  55.332  52.565  1.00 47.89           O  
ANISOU 2689  O   HOH A 171     7102   4493   6602   2200   1283  -1322       O  
HETATM 2690  O   HOH A 172      19.765  54.198  32.252  1.00 38.56           O  
ANISOU 2690  O   HOH A 172     5400   4279   4971    136  -2230   1073       O  
HETATM 2691  O   HOH A 173      32.033  35.814  40.665  1.00 36.16           O  
ANISOU 2691  O   HOH A 173     7190   3584   2966    558  -1314   -720       O  
HETATM 2692  O   HOH A 174      35.135  41.851  48.091  1.00 52.99           O  
ANISOU 2692  O   HOH A 174     7643   6539   5953     34   -358  -1566       O  
HETATM 2693  O   HOH A 175      39.491  45.381  44.719  1.00 67.81           O  
ANISOU 2693  O   HOH A 175     9311   7856   8599   -524   -750   -164       O  
HETATM 2694  O   HOH A 176      31.414  59.290  51.754  1.00 46.05           O  
ANISOU 2694  O   HOH A 176     9293   4751   3454   1881  -2110  -1352       O  
HETATM 2695  O   HOH A 177      35.605  41.168  42.502  1.00 37.55           O  
ANISOU 2695  O   HOH A 177     4933   4563   4772    819   -412   -178       O  
HETATM 2696  O   HOH A 178      26.194  30.752  20.668  1.00 43.82           O  
ANISOU 2696  O   HOH A 178     6045   4928   5677    209    472    -74       O  
HETATM 2697  O   HOH A 179      20.601  51.463  30.291  1.00 46.27           O  
ANISOU 2697  O   HOH A 179     4742   4814   8024   1703   -354   -361       O  
HETATM 2698  O   HOH A 180      41.651  51.114  49.854  1.00 42.99           O  
ANISOU 2698  O   HOH A 180     3844   7344   5148   -548  -2207   -964       O  
HETATM 2699  O   HOH A 181      31.808  38.481  43.395  1.00 41.21           O  
ANISOU 2699  O   HOH A 181     5269   4391   5999    956    228  -1495       O  
HETATM 2700  O   HOH A 182      33.517  30.379  39.027  1.00 42.61           O  
ANISOU 2700  O   HOH A 182     6341   4588   5260    784     29    493       O  
HETATM 2701  O   HOH A 183      17.283  52.784  38.328  1.00 39.81           O  
ANISOU 2701  O   HOH A 183     5731   4561   4834    184   -657    415       O  
HETATM 2702  O   HOH A 184      35.240  43.908  46.517  1.00 41.41           O  
ANISOU 2702  O   HOH A 184     5764   5222   4749    119  -1013    428       O  
HETATM 2703  O   HOH A 185      17.734  34.375  33.183  1.00 42.00           O  
ANISOU 2703  O   HOH A 185     5046   4615   6295   1098    381   1759       O  
HETATM 2704  O   HOH A 186      17.625  44.856  44.377  1.00 49.50           O  
ANISOU 2704  O   HOH A 186     6874   6540   5393  -1109   1715    828       O  
HETATM 2705  O   HOH A 187      37.033  35.626  37.079  1.00 38.42           O  
ANISOU 2705  O   HOH A 187     4672   4801   5124   1521   -763   -211       O  
HETATM 2706  O   HOH A 188      28.552  37.160  16.948  1.00 49.96           O  
ANISOU 2706  O   HOH A 188     9195   5084   4702  -1634   1198  -1320       O  
HETATM 2707  O   HOH A 189      17.975  37.168  37.582  1.00 60.75           O  
ANISOU 2707  O   HOH A 189     8130   7337   7614   -129   -931    308       O  
HETATM 2708  O   HOH A 190      37.684  39.820  38.331  1.00 46.19           O  
ANISOU 2708  O   HOH A 190     4732   4897   7922    748   -667   -205       O  
HETATM 2709  O   HOH A 191      37.392  62.667  40.882  1.00 49.76           O  
ANISOU 2709  O   HOH A 191     5612   6158   7134   -127  -1595   -368       O  
HETATM 2710  O   HOH A 192      30.300  38.584  54.042  1.00 55.74           O  
ANISOU 2710  O   HOH A 192     7138   6459   7580   1267  -2468    766       O  
HETATM 2711  O   HOH A 193      16.847  32.349  28.817  1.00 51.42           O  
ANISOU 2711  O   HOH A 193     4277   7992   7269  -1508  -1142     12       O  
HETATM 2712  O   HOH A 194      21.411  35.109  21.283  1.00 26.17           O  
ANISOU 2712  O   HOH A 194     2878   2922   4142   -652  -1667    933       O  
HETATM 2713  O   HOH A 195      29.001  64.283  37.636  1.00 26.44           O  
ANISOU 2713  O   HOH A 195     4804   2901   2341   -857   -350    467       O  
HETATM 2714  O   HOH A 196      18.005  35.794  26.129  1.00 28.97           O  
ANISOU 2714  O   HOH A 196     3880   2630   4498   -830  -1388   -116       O  
HETATM 2715  O   HOH A 197      30.230  41.047  15.992  1.00 34.65           O  
ANISOU 2715  O   HOH A 197     5516   3892   3758    136    504    678       O  
HETATM 2716  O   HOH A 198      37.321  33.010  30.226  1.00 31.57           O  
ANISOU 2716  O   HOH A 198     3786   4555   3655    496    -19  -1267       O  
HETATM 2717  O   HOH A 199      22.559  60.429  41.641  1.00 35.04           O  
ANISOU 2717  O   HOH A 199     4561   4970   3784   -411    517     30       O  
HETATM 2718  O   HOH A 200      33.040  60.087  47.731  1.00 30.29           O  
ANISOU 2718  O   HOH A 200     2958   4937   3614     79   -406   -172       O  
HETATM 2719  O   HOH A 201      15.453  49.310  44.930  1.00 47.89           O  
ANISOU 2719  O   HOH A 201     6212   6567   5418  -1497   2602  -3043       O  
HETATM 2720  O   HOH A 202      16.124  46.332  38.572  1.00 33.34           O  
ANISOU 2720  O   HOH A 202     4370   4439   3860  -1476   1072  -1457       O  
HETATM 2721  O   HOH A 203      35.784  53.091  54.575  1.00 40.23           O  
ANISOU 2721  O   HOH A 203     5462   5497   4328    628    793   -820       O  
HETATM 2722  O   HOH A 204      36.054  30.123  26.540  1.00 42.98           O  
ANISOU 2722  O   HOH A 204     6811   5588   3931  -2485   1054  -1933       O  
HETATM 2723  O   HOH A 205      13.367  38.604  31.292  1.00 57.94           O  
ANISOU 2723  O   HOH A 205     4914   8207   8894   -990   -397   -167       O  
HETATM 2724  O   HOH A 206      43.320  49.326  39.344  1.00 39.18           O  
ANISOU 2724  O   HOH A 206     5017   5056   4814     17    821   -962       O  
HETATM 2725  O   HOH A 207      20.422  58.444  42.640  1.00 45.82           O  
ANISOU 2725  O   HOH A 207     6147   5575   5690    723    -41   -265       O  
HETATM 2726  O   HOH A 208      23.879  36.866  47.601  1.00 45.77           O  
ANISOU 2726  O   HOH A 208     9803   5067   2521  -1480   1336  -1020       O  
HETATM 2727  O   HOH A 209      18.076  51.888  50.745  1.00 45.24           O  
ANISOU 2727  O   HOH A 209     5008   6883   5299   1018    487   -854       O  
HETATM 2728  O   HOH A 210      38.863  60.310  48.377  1.00 57.58           O  
ANISOU 2728  O   HOH A 210     9325   5143   7412    -51   -856  -1753       O  
HETATM 2729  O   HOH A 211      23.998  31.739  22.075  1.00 32.88           O  
ANISOU 2729  O   HOH A 211     4438   3353   4702   -725   -579  -1318       O  
HETATM 2730  O   HOH A 212      28.245  33.605  41.319  1.00 50.53           O  
ANISOU 2730  O   HOH A 212     8591   5675   4932   -914   2734  -1157       O  
HETATM 2731  O   HOH A 213      20.683  38.143  44.457  1.00 45.73           O  
ANISOU 2731  O   HOH A 213     5445   6284   5647   -572   1436  -1486       O  
HETATM 2732  O   HOH A 214      20.237  35.822  43.644  1.00 55.03           O  
ANISOU 2732  O   HOH A 214     8210   6240   6461   -646   2065    419       O  
HETATM 2733  O   HOH A 215      32.774  37.498  22.209  1.00 45.63           O  
ANISOU 2733  O   HOH A 215     4498   7718   5121    675  -1599    754       O  
HETATM 2734  O   HOH A 216      15.409  44.088  37.608  1.00 57.61           O  
ANISOU 2734  O   HOH A 216     5868   8882   7140     79   1059  -1291       O  
HETATM 2735  O   HOH A 217      28.902  44.049  58.286  1.00 46.81           O  
ANISOU 2735  O   HOH A 217     6560   6804   4422  -1966     61    201       O  
HETATM 2736  O   HOH A 218      26.664  47.857  27.300  1.00 38.07           O  
ANISOU 2736  O   HOH A 218     6337   5610   2517  -1084    604   -779       O  
HETATM 2737  O   HOH A 219      32.346  48.034  29.443  1.00 55.19           O  
ANISOU 2737  O   HOH A 219     6858   6292   7820   1204    269   -845       O  
HETATM 2738  O   HOH A 220      20.790  50.642  55.199  1.00 48.68           O  
ANISOU 2738  O   HOH A 220     7464   6153   4879     73   -591    797       O  
HETATM 2739  O   HOH A 221      32.759  63.600  33.967  1.00 63.47           O  
ANISOU 2739  O   HOH A 221     8711   7929   7477    -97   3067  -2615       O  
HETATM 2740  O   HOH A 222      20.394  46.818  26.416  1.00 38.14           O  
ANISOU 2740  O   HOH A 222     5029   4559   4904     55  -1841    360       O  
HETATM 2741  O   HOH A 223      41.489  55.117  51.655  1.00 44.05           O  
ANISOU 2741  O   HOH A 223     4881   5739   6119   -399  -1088  -1192       O  
HETATM 2742  O   HOH A 224      50.992  57.054  49.113  1.00 50.60           O  
ANISOU 2742  O   HOH A 224     6303   7134   5789  -1630  -1520   1413       O  
HETATM 2743  O   HOH A 225      22.269  33.475  41.523  1.00 46.13           O  
ANISOU 2743  O   HOH A 225     4888   5718   6919    315   -721    800       O  
HETATM 2744  O   HOH A 226      35.674  34.966  41.283  1.00 60.45           O  
ANISOU 2744  O   HOH A 226     7516   7706   7748    972   -605   1155       O  
HETATM 2745  O   HOH A 227      36.080  42.635  55.143  0.30 27.39           O  
ANISOU 2745  O   HOH A 227     3273   4568   2564   -572  -1435   -348       O  
HETATM 2746  O   HOH A 228      38.778  46.413  50.965  1.00 46.29           O  
ANISOU 2746  O   HOH A 228     4515   5582   7491    852     87   -234       O  
HETATM 2747  O   HOH A 229      21.927  56.920  29.038  1.00 68.89           O  
ANISOU 2747  O   HOH A 229     8536   8699   8940    357  -2457   1018       O  
HETATM 2748  O   HOH A 230      41.527  45.114  46.600  1.00 58.26           O  
ANISOU 2748  O   HOH A 230     7406   7717   7015    383  -1581    134       O  
HETATM 2749  O   HOH A 231      32.810  57.017  53.309  1.00 44.90           O  
ANISOU 2749  O   HOH A 231     6521   6210   4329      9  -1866   -207       O  
HETATM 2750  O   HOH A 232      40.269  40.837  40.239  1.00 55.46           O  
ANISOU 2750  O   HOH A 232     7806   6217   7049    542   2344  -1233       O  
HETATM 2751  O   HOH A 233      18.606  53.644  35.436  1.00 46.84           O  
ANISOU 2751  O   HOH A 233     5818   5375   6605   1071   -421   -146       O  
HETATM 2752  O   HOH A 234      36.031  46.610  46.877  1.00 40.22           O  
ANISOU 2752  O   HOH A 234     3293   6760   5229     56  -1356    -45       O  
HETATM 2753  O   HOH A 235      42.034  55.770  40.707  1.00 40.44           O  
ANISOU 2753  O   HOH A 235     4414   5904   5050   -483   1197   -889       O  
HETATM 2754  O   HOH A 236      25.037  61.897  29.641  1.00 48.74           O  
ANISOU 2754  O   HOH A 236     7898   4989   5632   -195  -2130   1768       O  
HETATM 2755  O   HOH A 237      24.036  60.482  33.006  1.00 53.36           O  
ANISOU 2755  O   HOH A 237     7601   5366   7307    232  -2992   2554       O  
HETATM 2756  O   HOH A 238      31.323  37.706  18.151  1.00 40.40           O  
ANISOU 2756  O   HOH A 238     4169   5704   5477    368   -737   -809       O  
HETATM 2757  O   HOH A 239      34.990  38.861  41.649  1.00 52.49           O  
ANISOU 2757  O   HOH A 239     6233   7641   6071  -1425  -2027   1211       O  
HETATM 2758  O   HOH A 240      16.275  36.693  32.772  1.00 40.12           O  
ANISOU 2758  O   HOH A 240     3742   4821   6680    408    153   1278       O  
HETATM 2759  O   HOH A 241      17.296  54.323  40.415  1.00 63.60           O  
ANISOU 2759  O   HOH A 241     6567   8176   9422   1458   2749   -840       O  
HETATM 2760  O   HOH A 242      17.452  29.661  26.963  1.00 58.00           O  
ANISOU 2760  O   HOH A 242     6345   7221   8471   -630  -1943    655       O  
HETATM 2761  O   HOH A 243      34.461  49.201  31.835  1.00 46.31           O  
ANISOU 2761  O   HOH A 243     6619   4928   6049   -406   1291   -257       O  
HETATM 2762  O   HOH A 244      13.781  38.715  34.562  1.00 54.52           O  
ANISOU 2762  O   HOH A 244     8383   5647   6687  -2250     85   1746       O  
HETATM 2763  O   HOH A 245      35.523  30.077  35.036  1.00 39.47           O  
ANISOU 2763  O   HOH A 245     5117   4602   5280   1423  -2496     81       O  
HETATM 2764  O   HOH A 246      36.350  27.694  33.186  1.00 42.93           O  
ANISOU 2764  O   HOH A 246     4895   6098   5317   1126   -557   1809       O  
HETATM 2765  O   HOH B 137     -10.066  34.208  63.981  1.00 13.30           O  
ANISOU 2765  O   HOH B 137     1783   1730   1542    217   -153   -264       O  
HETATM 2766  O   HOH B 138      -2.867  38.264  66.549  1.00 13.90           O  
ANISOU 2766  O   HOH B 138     1738   1918   1624   -352    286    133       O  
HETATM 2767  O   HOH B 139      -8.050  33.793  69.257  1.00 12.64           O  
ANISOU 2767  O   HOH B 139     1881   1731   1192   -389    384   -120       O  
HETATM 2768  O   HOH B 140     -16.429  37.383  73.557  1.00 16.30           O  
ANISOU 2768  O   HOH B 140     2109   2625   1460   -130      8   -739       O  
HETATM 2769  O   HOH B 141     -11.489  38.370  74.186  1.00 15.52           O  
ANISOU 2769  O   HOH B 141     2472   1526   1898   -218     94    -92       O  
HETATM 2770  O   HOH B 142      -9.375  37.879  75.949  1.00 14.66           O  
ANISOU 2770  O   HOH B 142     2376   1713   1481   -499     12      3       O  
HETATM 2771  O   HOH B 143       1.973  24.589  66.897  1.00 20.00           O  
ANISOU 2771  O   HOH B 143     3209   2528   1864   1161    -58    420       O  
HETATM 2772  O   HOH B 144     -13.559  37.216  62.821  1.00 15.81           O  
ANISOU 2772  O   HOH B 144     1781   2714   1513    383   -183   -149       O  
HETATM 2773  O   HOH B 145      -9.351  37.277  68.204  1.00 12.56           O  
ANISOU 2773  O   HOH B 145     1341   1533   1900     13    195   -155       O  
HETATM 2774  O   HOH B 146       7.782  26.899  75.769  1.00 61.43           O  
ANISOU 2774  O   HOH B 146     7945   7442   7953   1300  -2777   1427       O  
HETATM 2775  O   HOH B 147      -2.373  41.046  66.168  1.00 20.69           O  
ANISOU 2775  O   HOH B 147     2275   3075   2513   -453    853   -169       O  
HETATM 2776  O   HOH B 148     -18.260  45.113  79.660  1.00 33.01           O  
ANISOU 2776  O   HOH B 148     3931   2656   5955    356   -421    127       O  
HETATM 2777  O   HOH B 149       8.158  31.976  69.855  1.00 40.69           O  
ANISOU 2777  O   HOH B 149     5037   5748   4675   -812   -509    510       O  
HETATM 2778  O   HOH B 150      -8.532  44.538  83.195  1.00 41.50           O  
ANISOU 2778  O   HOH B 150     7107   5008   3653  -1802   -515    -33       O  
HETATM 2779  O   HOH B 151      -4.753  38.556  74.998  1.00 19.36           O  
ANISOU 2779  O   HOH B 151     2530   3125   1702    447   -302   -170       O  
HETATM 2780  O   HOH B 152      -4.157  27.081  48.507  1.00 19.49           O  
ANISOU 2780  O   HOH B 152     2642   2765   2000     58    219   -619       O  
HETATM 2781  O   HOH B 153      -8.547  26.754  60.594  1.00 22.39           O  
ANISOU 2781  O   HOH B 153     3553   2701   2256    -81    217    142       O  
HETATM 2782  O   HOH B 154      -6.951  36.726  75.591  1.00 21.80           O  
ANISOU 2782  O   HOH B 154     2498   3635   2148    -65    -53   -572       O  
HETATM 2783  O   HOH B 155      10.206  33.213  68.009  1.00 32.19           O  
ANISOU 2783  O   HOH B 155     3633   4794   3805   1502    120    371       O  
HETATM 2784  O   HOH B 156       4.516  40.913  57.928  1.00 21.75           O  
ANISOU 2784  O   HOH B 156     2838   2542   2885   -211   1034   -209       O  
HETATM 2785  O   HOH B 157      -7.684  44.690  76.868  1.00 25.72           O  
ANISOU 2785  O   HOH B 157     3308   2970   3495   -390   -188    445       O  
HETATM 2786  O   HOH B 158       3.244  28.176  48.840  1.00 23.80           O  
ANISOU 2786  O   HOH B 158     2520   3862   2661    860    557    892       O  
HETATM 2787  O   HOH B 159     -15.123  35.288  64.156  1.00 27.58           O  
ANISOU 2787  O   HOH B 159     2142   4741   3596   -315   -323   1461       O  
HETATM 2788  O   HOH B 160      -7.779  25.654  57.381  1.00 24.19           O  
ANISOU 2788  O   HOH B 160     4169   2268   2755   -320    443   -587       O  
HETATM 2789  O   HOH B 161      -1.936  35.676  72.815  1.00 30.28           O  
ANISOU 2789  O   HOH B 161     4532   3561   3414    748   -205   -990       O  
HETATM 2790  O   HOH B 162      -7.589  43.170  80.559  1.00 19.64           O  
ANISOU 2790  O   HOH B 162     2013   2629   2821     29   -720   -441       O  
HETATM 2791  O   HOH B 163       9.076  41.300  63.233  1.00 24.82           O  
ANISOU 2791  O   HOH B 163     2718   3404   3310   -485    757   -299       O  
HETATM 2792  O   HOH B 164      -0.870  39.149  70.453  1.00 26.64           O  
ANISOU 2792  O   HOH B 164     2463   4027   3632   -723    371  -1275       O  
HETATM 2793  O   HOH B 165     -10.931  51.249  67.193  1.00 24.53           O  
ANISOU 2793  O   HOH B 165     3951   2292   3078    969     93    498       O  
HETATM 2794  O   HOH B 166       7.373  23.261  59.250  1.00 23.71           O  
ANISOU 2794  O   HOH B 166     2756   3242   3010   1531    297     97       O  
HETATM 2795  O   HOH B 167       5.760  22.224  57.168  1.00 28.36           O  
ANISOU 2795  O   HOH B 167     3672   3576   3530    703    244   -171       O  
HETATM 2796  O   HOH B 168      -1.632  30.355  48.856  1.00 27.98           O  
ANISOU 2796  O   HOH B 168     3763   3480   3388    633   -961   -557       O  
HETATM 2797  O   HOH B 169     -15.714  39.361  67.886  1.00 26.87           O  
ANISOU 2797  O   HOH B 169     3811   3378   3022   -405    351   -200       O  
HETATM 2798  O   HOH B 170       2.143  30.348  47.316  1.00 30.17           O  
ANISOU 2798  O   HOH B 170     4507   3206   3752   1429  -1173   -578       O  
HETATM 2799  O   HOH B 171     -12.221  31.260  72.372  1.00 27.50           O  
ANISOU 2799  O   HOH B 171     3722   2245   4484    -97   -611   -727       O  
HETATM 2800  O   HOH B 172      -3.564  41.023  44.523  1.00 39.74           O  
ANISOU 2800  O   HOH B 172     6811   4328   3963    637   -312   1496       O  
HETATM 2801  O   HOH B 173     -10.107  48.468  76.740  1.00 33.74           O  
ANISOU 2801  O   HOH B 173     6382   2820   3618   -905    196   -835       O  
HETATM 2802  O   HOH B 174      -3.702  43.923  57.093  1.00 26.25           O  
ANISOU 2802  O   HOH B 174     4762   2732   2482    237    334    294       O  
HETATM 2803  O   HOH B 175      -5.872  44.497  61.312  1.00 28.20           O  
ANISOU 2803  O   HOH B 175     5249   2368   3097   1358   -220    372       O  
HETATM 2804  O   HOH B 176       5.736  39.675  69.992  1.00 34.27           O  
ANISOU 2804  O   HOH B 176     3540   5653   3827    -65   -188    548       O  
HETATM 2805  O   HOH B 177     -16.189  37.235  66.460  1.00 27.53           O  
ANISOU 2805  O   HOH B 177     3709   3814   2936    220  -1105     -6       O  
HETATM 2806  O   HOH B 178      -6.970  47.114  61.413  1.00 34.15           O  
ANISOU 2806  O   HOH B 178     5945   3526   3503    969   1034   -840       O  
HETATM 2807  O   HOH B 179      -9.285  33.015  51.106  1.00 29.92           O  
ANISOU 2807  O   HOH B 179     4112   4554   2701   -346  -1442   -439       O  
HETATM 2808  O   HOH B 180       8.813  25.376  66.212  1.00 32.34           O  
ANISOU 2808  O   HOH B 180     3545   4491   4253   1693   -672   -779       O  
HETATM 2809  O   HOH B 181       1.734  23.875  64.152  1.00 33.85           O  
ANISOU 2809  O   HOH B 181     5655   3896   3309   1653    540   -450       O  
HETATM 2810  O   HOH B 182       8.121  37.981  69.622  1.00 41.77           O  
ANISOU 2810  O   HOH B 182     6671   5145   4055    325   -468   -983       O  
HETATM 2811  O   HOH B 183       2.082  41.161  68.622  1.00 33.44           O  
ANISOU 2811  O   HOH B 183     4946   4667   3094  -1459   1072   -201       O  
HETATM 2812  O   HOH B 184      -5.120  43.857  76.030  1.00 29.28           O  
ANISOU 2812  O   HOH B 184     3045   4355   3727   -654   -727    619       O  
HETATM 2813  O   HOH B 185       5.518  31.071  50.376  1.00 33.62           O  
ANISOU 2813  O   HOH B 185     3990   4344   4441     41   1266    960       O  
HETATM 2814  O   HOH B 186     -16.388  46.132  78.066  1.00 33.85           O  
ANISOU 2814  O   HOH B 186     4252   4322   4288   1033   -389    -97       O  
HETATM 2815  O   HOH B 187     -14.320  29.001  67.726  1.00 30.82           O  
ANISOU 2815  O   HOH B 187     3582   3239   4891   -143    599   -683       O  
HETATM 2816  O   HOH B 188      -0.948  43.298  57.896  1.00 29.19           O  
ANISOU 2816  O   HOH B 188     4741   2097   4253    255    734    176       O  
HETATM 2817  O   HOH B 189     -17.367  38.136  79.076  1.00 31.66           O  
ANISOU 2817  O   HOH B 189     2576   3614   5839    139    181    607       O  
HETATM 2818  O   HOH B 190      -8.654  26.274  68.361  1.00 34.41           O  
ANISOU 2818  O   HOH B 190     4189   3637   5250   -502   1761    395       O  
HETATM 2819  O   HOH B 191     -19.020  36.901  74.191  1.00 35.98           O  
ANISOU 2819  O   HOH B 191     3668   5121   4881   1193   1314   -330       O  
HETATM 2820  O   HOH B 192      -8.239  44.179  58.673  1.00 31.90           O  
ANISOU 2820  O   HOH B 192     5244   3695   3183   1027     55    936       O  
HETATM 2821  O   HOH B 193     -12.517  40.924  53.807  1.00 38.30           O  
ANISOU 2821  O   HOH B 193     4522   6116   3914   1181  -1442   -983       O  
HETATM 2822  O   HOH B 194     -14.568  53.541  70.669  1.00 35.19           O  
ANISOU 2822  O   HOH B 194     5345   3061   4966   1225    -43   -394       O  
HETATM 2823  O   HOH B 195     -11.246  28.541  72.027  1.00 47.13           O  
ANISOU 2823  O   HOH B 195     4831   6480   6598   -940   2052    804       O  
HETATM 2824  O   HOH B 196      -9.176  43.058  53.387  1.00 34.78           O  
ANISOU 2824  O   HOH B 196     5745   3966   3504    627   -291    188       O  
HETATM 2825  O   HOH B 197      -5.435  24.803  69.168  1.00 40.15           O  
ANISOU 2825  O   HOH B 197     5989   4696   4568  -1280    356   1068       O  
HETATM 2826  O   HOH B 198     -18.632  44.165  77.618  1.00 31.56           O  
ANISOU 2826  O   HOH B 198     2116   4778   5099   -871    102     53       O  
HETATM 2827  O   HOH B 199      -0.975  45.197  59.894  1.00 35.11           O  
ANISOU 2827  O   HOH B 199     5444   3345   4553   -137    182    106       O  
HETATM 2828  O   HOH B 200      -6.589  24.316  65.711  1.00 40.59           O  
ANISOU 2828  O   HOH B 200     5527   3826   6070     20  -1328     66       O  
HETATM 2829  O   HOH B 201     -19.619  37.594  66.790  1.00 47.75           O  
ANISOU 2829  O   HOH B 201     7274   4705   6163   -836   -823   -410       O  
HETATM 2830  O   HOH B 202     -12.034  38.056  84.498  1.00 35.97           O  
ANISOU 2830  O   HOH B 202     4268   5798   3602    565   1086    722       O  
HETATM 2831  O   HOH B 203     -12.669  28.838  61.765  1.00 37.98           O  
ANISOU 2831  O   HOH B 203     4894   5682   3856  -1295   1262  -1073       O  
HETATM 2832  O   HOH B 204      12.200  28.035  61.952  1.00 46.10           O  
ANISOU 2832  O   HOH B 204     5111   7573   4831   -528    560   -903       O  
HETATM 2833  O   HOH B 205      -6.875  41.347  85.201  1.00 35.12           O  
ANISOU 2833  O   HOH B 205     4756   4120   4467   -189   -543   1703       O  
HETATM 2834  O   HOH B 206       3.226  41.628  55.606  1.00 35.50           O  
ANISOU 2834  O   HOH B 206     3387   5760   4341     54   -150    818       O  
HETATM 2835  O   HOH B 207     -19.274  41.864  83.167  1.00 63.80           O  
ANISOU 2835  O   HOH B 207     8389   7824   8028    -92    172    323       O  
HETATM 2836  O   HOH B 208      -1.931  22.134  70.404  1.00 60.14           O  
ANISOU 2836  O   HOH B 208     8300   6885   7665   -240   -679    985       O  
HETATM 2837  O   HOH B 209      -6.073  30.420  75.054  1.00 37.71           O  
ANISOU 2837  O   HOH B 209     5274   4447   4605   1292   -166     47       O  
HETATM 2838  O   HOH B 210     -11.417  28.735  69.605  1.00 36.95           O  
ANISOU 2838  O   HOH B 210     2241   5797   6001  -1074   -557    844       O  
HETATM 2839  O   HOH B 211      -7.164  26.930  70.957  1.00 39.88           O  
ANISOU 2839  O   HOH B 211     5136   2944   7071   1438    514   -509       O  
HETATM 2840  O   HOH B 212     -12.128  50.415  64.787  1.00 45.94           O  
ANISOU 2840  O   HOH B 212     6377   6296   4783   -205    218   1018       O  
HETATM 2841  O   HOH B 213       3.815  22.491  72.388  1.00 50.77           O  
ANISOU 2841  O   HOH B 213     7357   4574   7360   2323   -661   1606       O  
HETATM 2842  O   HOH B 214      -6.488  21.386  52.269  1.00 42.33           O  
ANISOU 2842  O   HOH B 214     3993   5585   6504   -868    681   -961       O  
HETATM 2843  O   HOH B 215      -7.183  27.275  73.460  1.00 47.90           O  
ANISOU 2843  O   HOH B 215     6148   5375   6679    183    720   1160       O  
HETATM 2844  O   HOH B 216      -2.387  44.733  73.268  1.00 56.85           O  
ANISOU 2844  O   HOH B 216     7304   6650   7647    429   1726   1417       O  
HETATM 2845  O   HOH B 217     -21.337  42.873  81.995  1.00 54.10           O  
ANISOU 2845  O   HOH B 217     7115   7518   5922   -735   1348  -1072       O  
HETATM 2846  O   HOH B 218      -8.665  34.305  49.055  1.00 40.49           O  
ANISOU 2846  O   HOH B 218     6806   5155   3424   -349  -1923     66       O  
HETATM 2847  O   HOH B 219       9.578  35.581  70.046  1.00 33.31           O  
ANISOU 2847  O   HOH B 219     3025   5536   4096   -395   -390    338       O  
HETATM 2848  O   HOH B 220      13.070  37.912  62.449  1.00 38.72           O  
ANISOU 2848  O   HOH B 220     5015   5889   3808  -1617    825     20       O  
HETATM 2849  O   HOH B 221      -8.395  53.171  67.409  1.00 42.96           O  
ANISOU 2849  O   HOH B 221     7570   3412   5339   -809   1396   -155       O  
HETATM 2850  O   HOH B 222     -17.802  42.782  62.353  1.00 44.98           O  
ANISOU 2850  O   HOH B 222     4239   6938   5914   -108  -1274   -113       O  
HETATM 2851  O   HOH B 223     -10.696  26.555  55.309  1.00 46.19           O  
ANISOU 2851  O   HOH B 223     4701   7343   5505   -297    386  -1574       O  
HETATM 2852  O   HOH B 224      -7.954  24.222  62.897  1.00 50.45           O  
ANISOU 2852  O   HOH B 224     8483   5167   5519      3   2382  -2588       O  
HETATM 2853  O   HOH B 225      17.024  32.727  60.687  1.00 47.40           O  
ANISOU 2853  O   HOH B 225     3977   6117   7914   1321   -347    -45       O  
HETATM 2854  O   HOH B 226      13.276  38.506  59.997  1.00 45.16           O  
ANISOU 2854  O   HOH B 226     4309   5705   7146   1971   -253    414       O  
HETATM 2855  O   HOH B 227       6.859  36.597  47.861  1.00 53.78           O  
ANISOU 2855  O   HOH B 227     8429   5859   6147   -131    172    927       O  
HETATM 2856  O   HOH B 228      11.504  26.696  64.624  1.00 89.05           O  
ANISOU 2856  O   HOH B 228    12159  10954  10721   -736    335    282       O  
HETATM 2857  O   HOH B 229      21.483  39.249  57.878  1.00 54.95           O  
ANISOU 2857  O   HOH B 229     7127   7276   6475   -137    229   1313       O  
HETATM 2858  O   HOH B 230     -13.809  31.279  57.643  1.00 47.50           O  
ANISOU 2858  O   HOH B 230     6917   6163   4966  -1318  -2353    196       O  
HETATM 2859  O   HOH B 231       9.935  43.794  63.676  1.00 43.77           O  
ANISOU 2859  O   HOH B 231     4771   4771   7089   -442   -834    216       O  
HETATM 2860  O   HOH B 232      -9.151  30.251  75.247  1.00 36.34           O  
ANISOU 2860  O   HOH B 232     5723   3867   4217   -638   1787    327       O  
HETATM 2861  O   HOH B 233     -17.189  40.221  60.522  1.00 31.49           O  
ANISOU 2861  O   HOH B 233     3616   5018   3330   1380     74    144       O  
HETATM 2862  O   HOH B 234      15.842  32.370  62.950  1.00 54.24           O  
ANISOU 2862  O   HOH B 234     5441   8503   6664  -1202    964   -216       O  
HETATM 2863  O   HOH B 235      -5.405  44.932  58.695  1.00 46.84           O  
ANISOU 2863  O   HOH B 235     7524   4633   5642    942    163   -527       O  
HETATM 2864  O   HOH B 236     -21.746  38.890  70.021  1.00 41.31           O  
ANISOU 2864  O   HOH B 236     3765   6033   5898  -1921  -1233   1310       O  
HETATM 2865  O   HOH B 237      10.740  41.720  53.249  1.00 47.65           O  
ANISOU 2865  O   HOH B 237     7522   5251   5331    963   3099   -257       O  
HETATM 2866  O   HOH B 238     -13.696  37.807  56.419  1.00 36.80           O  
ANISOU 2866  O   HOH B 238     5563   5546   2873   -668   -626   -705       O  
HETATM 2867  O   HOH B 239       5.787  30.475  53.275  1.00 31.47           O  
ANISOU 2867  O   HOH B 239     4411   4283   3263   1711   1128  -1521       O  
HETATM 2868  O   HOH B 240       5.406  43.549  52.042  1.00 45.79           O  
ANISOU 2868  O   HOH B 240     5013   5013   7372   1596   1190   -427       O  
HETATM 2869  O   HOH B 241      10.106  44.051  66.209  1.00 51.50           O  
ANISOU 2869  O   HOH B 241     6164   6577   6826   -780   -504   1350       O  
HETATM 2870  O   HOH B 242      11.624  40.375  62.574  1.00 58.67           O  
ANISOU 2870  O   HOH B 242     5943   7506   8845    797    102   -387       O  
HETATM 2871  O   HOH B 243       2.488  23.872  76.602  1.00 63.73           O  
ANISOU 2871  O   HOH B 243     8036   8396   7783    486   1820   -286       O  
HETATM 2872  O   HOH B 244     -18.735  37.708  76.927  1.00 52.13           O  
ANISOU 2872  O   HOH B 244     5008   7479   7322    -60  -2093    359       O  
HETATM 2873  O   HOH B 245     -13.480  31.504  76.049  1.00 24.93           O  
ANISOU 2873  O   HOH B 245     4508   2501   2464  -1249   1355   -300       O  
HETATM 2874  O   HOH B 246     -13.356  31.090  69.779  1.00 24.11           O  
ANISOU 2874  O   HOH B 246     3331   3335   2493   -225    647    321       O  
HETATM 2875  O   HOH B 247     -15.063  36.497  81.826  1.00 34.15           O  
ANISOU 2875  O   HOH B 247     5439   3995   3540  -1219   1630    193       O  
HETATM 2876  O   HOH B 248      -1.907  47.217  68.584  1.00 27.45           O  
ANISOU 2876  O   HOH B 248     3315   2655   4460   -312   1364  -1317       O  
HETATM 2877  O   HOH B 249       7.590  28.298  50.593  1.00 29.55           O  
ANISOU 2877  O   HOH B 249     3103   3981   4143    302   -729     48       O  
HETATM 2878  O   HOH B 250     -17.775  30.581  70.542  1.00 28.10           O  
ANISOU 2878  O   HOH B 250     4154   3571   2950  -1429    908   -485       O  
HETATM 2879  O   HOH B 251      -3.274  49.704  65.639  1.00 30.27           O  
ANISOU 2879  O   HOH B 251     4738   2745   4019  -1867    606   -361       O  
HETATM 2880  O   HOH B 252      -5.868  52.322  71.120  1.00 35.80           O  
ANISOU 2880  O   HOH B 252     4234   2647   6723  -1400   1230   -814       O  
HETATM 2881  O   HOH B 253       0.392  46.904  63.198  1.00 52.19           O  
ANISOU 2881  O   HOH B 253     7151   7458   5222  -1947   1077   -134       O  
HETATM 2882  O   HOH B 254      14.638  29.274  63.841  1.00 58.25           O  
ANISOU 2882  O   HOH B 254     5623   8561   7946   1445   3760  -2639       O  
HETATM 2883  O   HOH B 255     -15.624  47.064  64.512  1.00 53.06           O  
ANISOU 2883  O   HOH B 255     7565   7015   5579      5  -1554   1551       O  
HETATM 2884  O   HOH B 256      14.162  29.758  61.371  1.00 42.32           O  
ANISOU 2884  O   HOH B 256     6184   4199   5697    637    868  -1570       O  
HETATM 2885  O   HOH B 257     -19.437  35.386  68.022  1.00 42.06           O  
ANISOU 2885  O   HOH B 257     3603   5871   6507    246  -1651  -1351       O  
HETATM 2886  O   HOH B 259      -0.228  45.814  70.919  1.00 66.80           O  
ANISOU 2886  O   HOH B 259     7386   9578   8418  -1339  -1162    351       O  
HETATM 2887  O   HOH B 260       9.758  28.015  74.593  0.30 26.47           O  
ANISOU 2887  O   HOH B 260     2799   4542   2717    126    768   -195       O  
HETATM 2888  O   HOH B 261     -11.880  45.596  60.468  1.00 56.40           O  
ANISOU 2888  O   HOH B 261     6893   6116   8422   1887   -176   -785       O  
HETATM 2889  O   HOH B 262     -20.591  35.002  72.356  1.00 45.68           O  
ANISOU 2889  O   HOH B 262     2454   7428   7477    -80   -168    843       O  
HETATM 2890  O   HOH B 263      -6.581  33.513  46.678  1.00 42.52           O  
ANISOU 2890  O   HOH B 263     4630   6040   5487    214  -2010   1795       O  
HETATM 2891  O   HOH B 264     -10.302  27.473  52.900  1.00 67.67           O  
ANISOU 2891  O   HOH B 264     7402   9213   9096    300   -530    -93       O  
HETATM 2892  O   HOH B 265      -7.247  44.564  56.333  1.00 44.58           O  
ANISOU 2892  O   HOH B 265     5403   4678   6857   2048    693  -1025       O  
HETATM 2893  O   HOH B 266     -19.172  41.847  77.920  1.00 58.50           O  
ANISOU 2893  O   HOH B 266     6826   8241   7162   -522   3968  -1826       O  
HETATM 2894  O   HOH B 267      12.834  33.099  51.837  1.00 54.73           O  
ANISOU 2894  O   HOH B 267     6101   6298   8396   2032   2045   -206       O  
HETATM 2895  O   HOH B 269      18.027  33.018  57.931  1.00 49.58           O  
ANISOU 2895  O   HOH B 269     5859   6273   6707    896  -1167  -1331       O  
HETATM 2896  O   HOH B 270      12.982  39.133  50.872  1.00 46.70           O  
ANISOU 2896  O   HOH B 270     3825   7662   6255  -1209   1464   -394       O  
HETATM 2897  O   HOH B 271      -9.405  29.700  50.533  1.00 59.00           O  
ANISOU 2897  O   HOH B 271     8428   7712   6277  -1547    218  -1564       O  
HETATM 2898  O   HOH B 272       0.971  43.463  56.197  1.00 56.87           O  
ANISOU 2898  O   HOH B 272     7686   6988   6936   -458   1259    201       O  
HETATM 2899  O   HOH B 273       4.406  43.796  55.158  1.00 61.06           O  
ANISOU 2899  O   HOH B 273     7627   7595   7977   1296  -1414    552       O  
HETATM 2900  O   HOH B 274       5.245  43.579  58.343  1.00 50.01           O  
ANISOU 2900  O   HOH B 274     7672   5596   5733  -1812    970    172       O  
HETATM 2901  O   HOH B 275       2.380  38.304  70.634  1.00 48.48           O  
ANISOU 2901  O   HOH B 275     5568   5580   7274   -187  -2882     61       O  
HETATM 2902  O   HOH B 276      -4.369  50.857  63.420  1.00 47.42           O  
ANISOU 2902  O   HOH B 276     6919   5816   5283  -2183    -85     20       O  
HETATM 2903  O   HOH B 277       1.808  22.055  67.735  1.00 52.14           O  
ANISOU 2903  O   HOH B 277     5696   5628   8485   1374   -909   1405       O  
HETATM 2904  O   HOH B 278       7.859  33.433  50.556  1.00 49.69           O  
ANISOU 2904  O   HOH B 278     5988   6336   6555    930    654    213       O  
HETATM 2905  O   HOH C 113      22.308  29.498  40.311  1.00 56.61           O  
ANISOU 2905  O   HOH C 113     8625   5710   7174    -16    608    729       O  
HETATM 2906  O   HOH C 114      31.633  29.762  36.466  1.00 44.49           O  
ANISOU 2906  O   HOH C 114     6021   6140   4743   -429    610    278       O  
HETATM 2907  O   HOH C 115      16.117   9.240  43.374  1.00 59.34           O  
ANISOU 2907  O   HOH C 115     7014   8665   6866  -1729   1487   -980       O  
HETATM 2908  O   HOH C 116      24.366  28.836  38.875  1.00 38.28           O  
ANISOU 2908  O   HOH C 116     6462   3317   4767   -759    674   1489       O  
HETATM 2909  O   HOH C 117      27.673  30.396  37.219  1.00 43.10           O  
ANISOU 2909  O   HOH C 117     6970   4770   4637   -842   1481    359       O  
HETATM 2910  O   HOH C 118      16.927  34.013  50.044  1.00 48.69           O  
ANISOU 2910  O   HOH C 118     6519   5376   6606    228    863   -561       O  
HETATM 2911  O   HOH C 119      19.772  15.055  46.846  1.00 14.31           O  
ANISOU 2911  O   HOH C 119     1469   2845   1122   -239   -446    460       O  
HETATM 2912  O   HOH C 120      25.830  20.533  49.238  1.00 14.46           O  
ANISOU 2912  O   HOH C 120     2117   1852   1526    -35    181     33       O  
HETATM 2913  O   HOH C 121      21.885  15.059  51.981  1.00 12.98           O  
ANISOU 2913  O   HOH C 121     1614   2160   1159    -83     99    480       O  
HETATM 2914  O   HOH C 122      13.085  16.624  56.703  1.00 17.45           O  
ANISOU 2914  O   HOH C 122     1759   3253   1617    -80   -128    399       O  
HETATM 2915  O   HOH C 123      17.349  18.654  57.084  1.00 16.71           O  
ANISOU 2915  O   HOH C 123     1629   2477   2242    262   -146    545       O  
HETATM 2916  O   HOH C 124      19.628  18.972  58.707  1.00 17.84           O  
ANISOU 2916  O   HOH C 124     1574   3017   2189     -3   -149    204       O  
HETATM 2917  O   HOH C 125      33.656   8.414  49.371  1.00 15.20           O  
ANISOU 2917  O   HOH C 125     1560   2555   1660    456   -389   -260       O  
HETATM 2918  O   HOH C 126      15.724  17.031  45.720  1.00 22.58           O  
ANISOU 2918  O   HOH C 126     1843   5466   1271   -717   -219    279       O  
HETATM 2919  O   HOH C 127      19.839  18.181  50.943  1.00 14.64           O  
ANISOU 2919  O   HOH C 127     1086   2139   2340    109   -169    140       O  
HETATM 2920  O   HOH C 128      36.722  26.342  45.744  1.00 23.40           O  
ANISOU 2920  O   HOH C 128     3031   3939   1920  -1013    473    -45       O  
HETATM 2921  O   HOH C 129      25.660  23.390  48.705  1.00 18.76           O  
ANISOU 2921  O   HOH C 129     2683   2370   2073    310    982    -47       O  
HETATM 2922  O   HOH C 130       9.722  25.374  62.117  1.00 51.66           O  
ANISOU 2922  O   HOH C 130     4089   7297   8242   1022    526    136       O  
HETATM 2923  O   HOH C 131      37.705  17.278  51.827  1.00 21.59           O  
ANISOU 2923  O   HOH C 131     2057   3608   2536     40      9   -374       O  
HETATM 2924  O   HOH C 132      40.818   6.497  49.660  1.00 37.53           O  
ANISOU 2924  O   HOH C 132     3820   5915   4523  -1184    208  -1270       O  
HETATM 2925  O   HOH C 133      45.251  15.983  50.851  1.00 24.40           O  
ANISOU 2925  O   HOH C 133     2689   4185   2397   1219   -589   -322       O  
HETATM 2926  O   HOH C 134      18.500   8.879  44.853  1.00 38.21           O  
ANISOU 2926  O   HOH C 134     3317   6748   4455   -485     48  -1172       O  
HETATM 2927  O   HOH C 135      24.947  28.564  33.833  1.00 26.21           O  
ANISOU 2927  O   HOH C 135     5270   2480   2209    640    638    816       O  
HETATM 2928  O   HOH C 136      16.825   9.073  50.057  1.00 41.37           O  
ANISOU 2928  O   HOH C 136     4680   5026   6013  -1636   -318   1458       O  
HETATM 2929  O   HOH C 137      39.853  18.980  50.579  1.00 17.87           O  
ANISOU 2929  O   HOH C 137     1306   3256   2229    333    -12   -112       O  
HETATM 2930  O   HOH C 138      32.140  24.951  40.571  1.00 22.02           O  
ANISOU 2930  O   HOH C 138     2506   3289   2570   -352    210    454       O  
HETATM 2931  O   HOH C 139      40.382  14.218  57.232  1.00 11.96           O  
ANISOU 2931  O   HOH C 139     1174   2209   1163    116   -292   -274       O  
HETATM 2932  O   HOH C 140      36.130   6.963  55.058  1.00 20.66           O  
ANISOU 2932  O   HOH C 140     2536   2002   3311     56  -1380    494       O  
HETATM 2933  O   HOH C 141      14.521  15.079  47.195  1.00 29.59           O  
ANISOU 2933  O   HOH C 141     2255   5733   3256    -53   -483   1314       O  
HETATM 2934  O   HOH C 142      23.874   7.325  39.890  1.00 26.27           O  
ANISOU 2934  O   HOH C 142     4727   2682   2571   -645    100   -191       O  
HETATM 2935  O   HOH C 143      20.646  13.988  33.738  1.00 24.55           O  
ANISOU 2935  O   HOH C 143     2631   3742   2955   -144   -956    404       O  
HETATM 2936  O   HOH C 144      26.894   9.648  31.035  1.00 21.44           O  
ANISOU 2936  O   HOH C 144     3404   2590   2154    372   -149   -391       O  
HETATM 2937  O   HOH C 145      28.602  13.552  31.158  1.00 24.72           O  
ANISOU 2937  O   HOH C 145     2839   2959   3596     52   -131   -615       O  
HETATM 2938  O   HOH C 146      11.191  26.747  60.097  1.00 26.58           O  
ANISOU 2938  O   HOH C 146     2520   3909   3670    771   1180    132       O  
HETATM 2939  O   HOH C 147      37.501   6.935  39.315  1.00 30.87           O  
ANISOU 2939  O   HOH C 147     4065   3670   3995   1159  -1090   -242       O  
HETATM 2940  O   HOH C 148      10.075  23.031  61.145  1.00 49.45           O  
ANISOU 2940  O   HOH C 148     4388   8213   6188      5   3508  -1891       O  
HETATM 2941  O   HOH C 149      40.401  10.666  48.401  1.00 25.51           O  
ANISOU 2941  O   HOH C 149     1708   5569   2417    723     58   -666       O  
HETATM 2942  O   HOH C 150      23.604  26.006  39.584  1.00 22.17           O  
ANISOU 2942  O   HOH C 150     3831   2605   1988    611   -268   -133       O  
HETATM 2943  O   HOH C 151      13.530  18.544  51.009  1.00 28.54           O  
ANISOU 2943  O   HOH C 151     3981   4489   2373    874    456    987       O  
HETATM 2944  O   HOH C 152      16.347   8.742  52.966  1.00 56.89           O  
ANISOU 2944  O   HOH C 152     6614   7978   7023  -1224  -1629    739       O  
HETATM 2945  O   HOH C 153      37.305  18.971  53.787  1.00 19.59           O  
ANISOU 2945  O   HOH C 153     2138   3984   1321     99    511     51       O  
HETATM 2946  O   HOH C 154      24.090  20.198  57.698  1.00 19.37           O  
ANISOU 2946  O   HOH C 154     2333   3743   1284    368    -97    458       O  
HETATM 2947  O   HOH C 155      17.219  11.255  52.709  1.00 24.76           O  
ANISOU 2947  O   HOH C 155     3243   4461   1702   -402     20    320       O  
HETATM 2948  O   HOH C 156      22.849   8.192  43.203  1.00 20.70           O  
ANISOU 2948  O   HOH C 156     3214   2655   1995   -352   -262    548       O  
HETATM 2949  O   HOH C 157      38.683  20.582  52.362  1.00 31.58           O  
ANISOU 2949  O   HOH C 157     2686   4470   4841    242    180    272       O  
HETATM 2950  O   HOH C 158      13.365  16.404  49.437  1.00 32.00           O  
ANISOU 2950  O   HOH C 158     4305   4548   3306    358  -2102    574       O  
HETATM 2951  O   HOH C 159      32.359  14.124  29.923  1.00 23.75           O  
ANISOU 2951  O   HOH C 159     3812   2654   2556    945   -167   -239       O  
HETATM 2952  O   HOH C 160      33.824  12.230  31.606  1.00 16.81           O  
ANISOU 2952  O   HOH C 160     2628   2216   1542    393    217    -36       O  
HETATM 2953  O   HOH C 161      28.724  32.885  43.683  1.00 49.11           O  
ANISOU 2953  O   HOH C 161     6905   5028   6729    434   -344   -882       O  
HETATM 2954  O   HOH C 162      22.179  18.153  58.337  1.00 17.50           O  
ANISOU 2954  O   HOH C 162     2182   2904   1565    612    397   -288       O  
HETATM 2955  O   HOH C 163      27.529   5.259  36.220  1.00 31.39           O  
ANISOU 2955  O   HOH C 163     3183   4196   4550   -476    138  -1122       O  
HETATM 2956  O   HOH C 164      27.670  18.514  55.272  1.00 24.78           O  
ANISOU 2956  O   HOH C 164     2351   3513   3550    -21    504   -880       O  
HETATM 2957  O   HOH C 165      24.691  29.742  50.927  1.00 28.66           O  
ANISOU 2957  O   HOH C 165     3226   3535   4130   -208   2134   -537       O  
HETATM 2958  O   HOH C 166      15.841  29.003  59.077  1.00 38.37           O  
ANISOU 2958  O   HOH C 166     4771   3732   6078   1175   1886  -1244       O  
HETATM 2959  O   HOH C 167      21.599  26.183  44.018  1.00 27.13           O  
ANISOU 2959  O   HOH C 167     3464   3738   3107    749    -16   1111       O  
HETATM 2960  O   HOH C 168      26.296  26.044  40.497  1.00 28.06           O  
ANISOU 2960  O   HOH C 168     3583   3115   3963   1300   -597    787       O  
HETATM 2961  O   HOH C 169      27.443  21.895  52.893  1.00 29.91           O  
ANISOU 2961  O   HOH C 169     3902   3303   4160  -1106   2161  -1476       O  
HETATM 2962  O   HOH C 170      10.591  15.514  57.167  1.00 45.38           O  
ANISOU 2962  O   HOH C 170     2830   7075   7338   -538   2597     97       O  
HETATM 2963  O   HOH C 171      17.094  11.694  59.244  1.00 30.67           O  
ANISOU 2963  O   HOH C 171     4897   3495   3263   -277  -1101     17       O  
HETATM 2964  O   HOH C 172      19.816  25.764  59.300  1.00 37.37           O  
ANISOU 2964  O   HOH C 172     5389   3576   5233    -47   1009   1537       O  
HETATM 2965  O   HOH C 173      18.890  11.509  54.906  1.00 35.15           O  
ANISOU 2965  O   HOH C 173     4558   4025   4772   -271  -1178  -1070       O  
HETATM 2966  O   HOH C 174      35.237  15.692  32.772  1.00 26.63           O  
ANISOU 2966  O   HOH C 174     3003   3967   3147   1033   1025   1340       O  
HETATM 2967  O   HOH C 175      14.989  31.744  50.602  1.00 34.05           O  
ANISOU 2967  O   HOH C 175     4284   3668   4986    904    254   1581       O  
HETATM 2968  O   HOH C 176      17.032  18.388  66.952  1.00 44.05           O  
ANISOU 2968  O   HOH C 176     6409   6065   4261    300     48   1622       O  
HETATM 2969  O   HOH C 177      25.161   7.483  31.810  1.00 50.95           O  
ANISOU 2969  O   HOH C 177     6267   6485   6609   -847  -1941   1764       O  
HETATM 2970  O   HOH C 178      47.401  26.502  38.101  1.00 26.59           O  
ANISOU 2970  O   HOH C 178     2834   4780   2488  -1031    977    -63       O  
HETATM 2971  O   HOH C 179      30.038  24.495  51.175  1.00 29.07           O  
ANISOU 2971  O   HOH C 179     5108   3493   2445   -991    275    109       O  
HETATM 2972  O   HOH C 180      41.316  25.006  42.462  1.00 31.33           O  
ANISOU 2972  O   HOH C 180     4785   4676   2442    284    447    704       O  
HETATM 2973  O   HOH C 181      41.264  24.088  45.114  1.00 33.54           O  
ANISOU 2973  O   HOH C 181     4039   4824   3881   -500    497   1562       O  
HETATM 2974  O   HOH C 182      28.626  29.473  48.666  1.00 32.98           O  
ANISOU 2974  O   HOH C 182     6024   2960   3546    362   -662   -771       O  
HETATM 2975  O   HOH C 183      33.512   6.066  51.167  1.00 44.46           O  
ANISOU 2975  O   HOH C 183     5542   5262   6087   -719    497   -957       O  
HETATM 2976  O   HOH C 184      34.123  24.268  52.660  1.00 41.44           O  
ANISOU 2976  O   HOH C 184     7046   5502   3198  -1131   1682    353       O  
HETATM 2977  O   HOH C 185      19.942   9.112  51.935  1.00 33.67           O  
ANISOU 2977  O   HOH C 185     3807   5004   3984  -2150   -551   1531       O  
HETATM 2978  O   HOH C 186      33.577   7.582  46.519  1.00 33.58           O  
ANISOU 2978  O   HOH C 186     4558   4915   3285   1125   -570    667       O  
HETATM 2979  O   HOH C 187      19.186  25.125  41.496  1.00 38.13           O  
ANISOU 2979  O   HOH C 187     6239   3865   4384   1073     68    839       O  
HETATM 2980  O   HOH C 188      26.814  22.298  56.178  1.00 36.25           O  
ANISOU 2980  O   HOH C 188     5212   4796   3766  -1625  -1347   -326       O  
HETATM 2981  O   HOH C 189      36.366  18.267  32.688  1.00 48.52           O  
ANISOU 2981  O   HOH C 189     5878   6278   6280   -613  -1571   -535       O  
HETATM 2982  O   HOH C 190      26.431   6.616  51.421  1.00 34.59           O  
ANISOU 2982  O   HOH C 190     4965   3086   5093    -18     70   1572       O  
HETATM 2983  O   HOH C 191      19.892  28.233  44.350  1.00 44.62           O  
ANISOU 2983  O   HOH C 191     7065   4778   5111    636   1510    225       O  
HETATM 2984  O   HOH C 192      26.842  27.486  36.911  1.00 34.29           O  
ANISOU 2984  O   HOH C 192     6933   3771   2325     62  -1028   -463       O  
HETATM 2985  O   HOH C 193      31.756  27.530  40.221  1.00 49.58           O  
ANISOU 2985  O   HOH C 193     4957   7765   6117  -1305   -505   1373       O  
HETATM 2986  O   HOH C 194      21.006  11.348  57.694  1.00 36.68           O  
ANISOU 2986  O   HOH C 194     6195   4236   3507   -202     -9    650       O  
HETATM 2987  O   HOH C 195      25.435  28.015  42.725  1.00 34.79           O  
ANISOU 2987  O   HOH C 195     6545   2653   4021   -484  -1401   1153       O  
HETATM 2988  O   HOH C 196      24.355   8.485  53.716  1.00 40.32           O  
ANISOU 2988  O   HOH C 196     4219   3564   7537    769   -191   -124       O  
HETATM 2989  O   HOH C 197      21.777  26.446  41.494  1.00 36.16           O  
ANISOU 2989  O   HOH C 197     5682   4240   3817   1278   2125    246       O  
HETATM 2990  O   HOH C 198      31.937   8.176  57.718  1.00 49.53           O  
ANISOU 2990  O   HOH C 198     6705   6595   5518   -477   1739    777       O  
HETATM 2991  O   HOH C 199      16.607  11.700  40.368  1.00 41.25           O  
ANISOU 2991  O   HOH C 199     6107   4538   5029   -938  -2456    -82       O  
HETATM 2992  O   HOH C 200      28.136  26.921  38.883  1.00 34.43           O  
ANISOU 2992  O   HOH C 200     3448   5515   4118   -233   -175    445       O  
HETATM 2993  O   HOH C 201       8.653  15.465  50.938  1.00 46.24           O  
ANISOU 2993  O   HOH C 201     3927   5476   8165    394   1427    281       O  
HETATM 2994  O   HOH C 202      22.505  31.870  47.719  1.00 39.47           O  
ANISOU 2994  O   HOH C 202     4651   4347   5997   -575    983    523       O  
HETATM 2995  O   HOH C 203      26.477  30.186  47.379  1.00 44.20           O  
ANISOU 2995  O   HOH C 203     4784   5163   6846    758   -114   -362       O  
HETATM 2996  O   HOH C 204      44.955  17.158  45.506  1.00 41.89           O  
ANISOU 2996  O   HOH C 204     4031   6909   4976    459   2130   -567       O  
HETATM 2997  O   HOH C 205      20.120  27.002  30.975  1.00 51.32           O  
ANISOU 2997  O   HOH C 205     5757   6761   6981   1059    399  -1007       O  
HETATM 2998  O   HOH C 206       7.413  16.391  53.050  1.00 38.28           O  
ANISOU 2998  O   HOH C 206     4779   4032   5734    538   -907    690       O  
HETATM 2999  O   HOH C 207      36.569  28.237  59.289  1.00 53.23           O  
ANISOU 2999  O   HOH C 207     7428   4544   8255    958    -78   1151       O  
HETATM 3000  O   HOH C 208      41.783  17.974  58.583  1.00 26.88           O  
ANISOU 3000  O   HOH C 208     3336   3000   3878    529  -1342   -319       O  
HETATM 3001  O   HOH C 209      47.119  18.449  47.925  1.00 29.01           O  
ANISOU 3001  O   HOH C 209     2433   3884   4708    247    920   1074       O  
HETATM 3002  O   HOH C 210      25.311  30.165  35.678  1.00 37.01           O  
ANISOU 3002  O   HOH C 210     7444   2705   3912    263    123    -45       O  
HETATM 3003  O   HOH C 211      39.375   8.720  41.612  1.00 31.63           O  
ANISOU 3003  O   HOH C 211     4033   5058   2926   1751   -893   -183       O  
HETATM 3004  O   HOH C 212      22.745  15.057  29.604  1.00 35.78           O  
ANISOU 3004  O   HOH C 212     5349   3919   4326   -604   -128    501       O  
HETATM 3005  O   HOH C 213      25.401   6.175  48.560  1.00 38.86           O  
ANISOU 3005  O   HOH C 213     5152   2839   6775    -69    128   -297       O  
HETATM 3006  O   HOH C 214      30.844  25.321  38.102  1.00 34.39           O  
ANISOU 3006  O   HOH C 214     4514   4854   3698   -548   -654   1852       O  
HETATM 3007  O   HOH C 215      30.836  21.581  53.233  1.00 48.09           O  
ANISOU 3007  O   HOH C 215     6360   5609   6304   -281  -2366    831       O  
HETATM 3008  O   HOH C 216      18.334  23.878  36.079  1.00 34.30           O  
ANISOU 3008  O   HOH C 216     3758   5287   3986    640    364   1183       O  
HETATM 3009  O   HOH C 217      30.265   9.943  57.696  1.00 34.80           O  
ANISOU 3009  O   HOH C 217     4164   4177   4880    563   -235    725       O  
HETATM 3010  O   HOH C 218      13.886  15.124  60.694  1.00 39.55           O  
ANISOU 3010  O   HOH C 218     5829   4966   4233  -1167   1523   -493       O  
HETATM 3011  O   HOH C 219      28.641   7.144  40.791  1.00 29.74           O  
ANISOU 3011  O   HOH C 219     3596   4004   3699   -378   -899   -186       O  
HETATM 3012  O   HOH C 220      46.511  14.943  47.308  1.00 37.44           O  
ANISOU 3012  O   HOH C 220     3628   4907   5689  -1102   -445   1062       O  
HETATM 3013  O   HOH C 221      38.005  13.564  32.749  1.00 41.04           O  
ANISOU 3013  O   HOH C 221     6044   4873   4677    898    256   -603       O  
HETATM 3014  O   HOH C 222      36.846   8.871  60.322  1.00 32.45           O  
ANISOU 3014  O   HOH C 222     3438   5018   3874   1219   1004   2154       O  
HETATM 3015  O   HOH C 223      24.561  11.900  57.627  1.00 33.64           O  
ANISOU 3015  O   HOH C 223     4407   4795   3578   1239   -890    227       O  
HETATM 3016  O   HOH C 224      45.940  19.831  40.385  1.00 41.33           O  
ANISOU 3016  O   HOH C 224     4045   5248   6411   -601   1246   -496       O  
HETATM 3017  O   HOH C 225      44.248  28.727  35.252  1.00 44.22           O  
ANISOU 3017  O   HOH C 225     6903   5336   4564   -570    757   1199       O  
HETATM 3018  O   HOH C 226      31.200  27.293  36.175  1.00 35.42           O  
ANISOU 3018  O   HOH C 226     4976   4515   3967   1082  -1607   -571       O  
HETATM 3019  O   HOH C 227      31.237   5.251  52.189  1.00 52.70           O  
ANISOU 3019  O   HOH C 227     6849   5858   7316   -230  -1687    797       O  
HETATM 3020  O   HOH C 228      34.132   7.450  58.818  1.00 45.51           O  
ANISOU 3020  O   HOH C 228     6695   5224   5374    409   2491    317       O  
HETATM 3021  O   HOH C 229      39.448  26.132  45.824  1.00 49.35           O  
ANISOU 3021  O   HOH C 229     5465   5846   7442   -299    669   -115       O  
HETATM 3022  O   HOH C 230      17.148   9.010  47.577  1.00 50.75           O  
ANISOU 3022  O   HOH C 230     4035   7974   7275  -2637   -315    948       O  
HETATM 3023  O   HOH C 231      35.470   3.830  41.591  1.00 44.60           O  
ANISOU 3023  O   HOH C 231     5515   5280   6149   -577   -134   -735       O  
HETATM 3024  O   HOH C 232      42.013  11.961  41.130  1.00 43.46           O  
ANISOU 3024  O   HOH C 232     3198   7632   5685   1752   1893    -96       O  
HETATM 3025  O   HOH C 233      23.592   8.924  56.281  1.00 45.93           O  
ANISOU 3025  O   HOH C 233     6633   5169   5650    662   -389   2120       O  
HETATM 3026  O   HOH C 234      11.070  24.168  36.833  1.00 47.63           O  
ANISOU 3026  O   HOH C 234     5281   6288   6528   2284    180    935       O  
HETATM 3027  O   HOH C 235      11.667  14.207  59.596  1.00 53.87           O  
ANISOU 3027  O   HOH C 235     5960   6488   8020   1347    800   -487       O  
HETATM 3028  O   HOH C 236      21.984  30.936  44.291  1.00 45.18           O  
ANISOU 3028  O   HOH C 236     6168   5404   5594   -379   -277    322       O  
HETATM 3029  O   HOH C 237      37.213  22.366  52.155  1.00 35.45           O  
ANISOU 3029  O   HOH C 237     3322   6036   4112    522    -81  -2540       O  
HETATM 3030  O   HOH C 238      40.764  12.299  45.964  1.00 51.94           O  
ANISOU 3030  O   HOH C 238     4738   7388   7608    365  -1673    755       O  
HETATM 3031  O   HOH C 239      21.035  15.500  31.569  1.00 37.89           O  
ANISOU 3031  O   HOH C 239     6496   4244   3657    344  -1893    727       O  
HETATM 3032  O   HOH C 240      22.963   7.373  50.757  1.00 38.00           O  
ANISOU 3032  O   HOH C 240     4548   4946   4943   -970     82   1110       O  
HETATM 3033  O   HOH C 241      15.968  20.939  36.452  1.00 42.82           O  
ANISOU 3033  O   HOH C 241     3543   7959   4766    218  -1505   -249       O  
HETATM 3034  O   HOH C 242      21.321  11.221  33.046  1.00 44.59           O  
ANISOU 3034  O   HOH C 242     7510   4641   4791  -2231   -419  -1466       O  
HETATM 3035  O   HOH C 243      18.862  28.385  60.476  1.00 68.52           O  
ANISOU 3035  O   HOH C 243     8802   8356   8877    -69      0   -287       O  
HETATM 3036  O   HOH C 244      11.547  15.750  36.647  1.00 53.54           O  
ANISOU 3036  O   HOH C 244     5318   8126   6898   -878  -2467    263       O  
HETATM 3037  O   HOH C 245      44.537  21.127  45.828  1.00 37.65           O  
ANISOU 3037  O   HOH C 245     4083   5415   4808  -1244   -384   1195       O  
HETATM 3038  O   HOH C 246      38.620  20.131  31.589  1.00 77.07           O  
ANISOU 3038  O   HOH C 246     9612   9821   9849    625   2046  -1330       O  
HETATM 3039  O   HOH C 247      10.006  14.403  47.823  1.00 55.92           O  
ANISOU 3039  O   HOH C 247     7159   7330   6759  -1157    427   -209       O  
HETATM 3040  O   HOH C 248      19.882  33.110  54.844  1.00 50.69           O  
ANISOU 3040  O   HOH C 248     6615   5603   7041   -553   2291  -2148       O  
HETATM 3041  O   HOH C 249      19.266  15.941  29.153  1.00 50.15           O  
ANISOU 3041  O   HOH C 249     8455   4209   6391  -1165   -394    282       O  
HETATM 3042  O   HOH C 250      26.205  29.064  53.931  1.00 73.83           O  
ANISOU 3042  O   HOH C 250     9818   8998   9234   -195   -435    164       O  
HETATM 3043  O   HOH C 251      26.434  15.156  27.840  1.00 39.83           O  
ANISOU 3043  O   HOH C 251     6194   4068   4869   -374   1090    394       O  
HETATM 3044  O   HOH C 252      14.616  12.461  60.951  1.00 53.15           O  
ANISOU 3044  O   HOH C 252     7330   6979   5884  -1144   -660    694       O  
HETATM 3045  O   HOH C 253      37.200  28.915  46.426  1.00 42.29           O  
ANISOU 3045  O   HOH C 253     5717   4352   5999  -1258    486   -212       O  
CONECT  128 2628                                                                
CONECT 1325 2629                                                                
CONECT 1326 2629                                                                
CONECT 2199 2630                                                                
CONECT 2200 2630                                                                
CONECT 2213 2630                                                                
CONECT 2628  128 2745                                                           
CONECT 2629 1325 1326 2887                                                      
CONECT 2630 2199 2200 2213 2931                                                 
CONECT 2745 2628                                                                
CONECT 2887 2629                                                                
CONECT 2931 2630                                                                
MASTER      340    0    3   12   12    0    3   12 3042    3   12   27          
END                                                                             



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