CNRS Nantes University UFIP UFIP
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***  METAL TRANSPORT 03-MAY-00 1EXR  ***

elNémo ID: 21073116495352931

Job options:

ID        	=	 21073116495352931
JOBID     	=	 METAL TRANSPORT 03-MAY-00 1EXR
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


HEADER    METAL TRANSPORT                         03-MAY-00   1EXR              
TITLE     THE 1.0 ANGSTROM CRYSTAL STRUCTURE OF CA+2 BOUND CALMODULIN           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CALMODULIN;                                                
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PARAMECIUM TETRAURELIA;                         
SOURCE   3 ORGANISM_TAXID: 5888;                                                
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: JM109;                                     
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PKK233-3                                  
KEYWDS    CALMODULIN, HIGH RESOLUTION, DISORDER, METAL TRANSPORT                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.A.WILSON,A.T.BRUNGER                                                
REVDAT   4   24-JUL-19 1EXR    1       REMARK                                   
REVDAT   3   24-FEB-09 1EXR    1       VERSN                                    
REVDAT   2   09-SEP-03 1EXR    1       JRNL   REMARK DBREF  MASTER              
REVDAT   1   20-SEP-00 1EXR    0                                                
JRNL        AUTH   M.A.WILSON,A.T.BRUNGER                                       
JRNL        TITL   THE 1.0 A CRYSTAL STRUCTURE OF CA(2+)-BOUND CALMODULIN: AN   
JRNL        TITL 2 ANALYSIS OF DISORDER AND IMPLICATIONS FOR FUNCTIONALLY       
JRNL        TITL 3 RELEVANT PLASTICITY                                          
JRNL        REF    J.MOL.BIOL.                   V. 301  1237 2000              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   10966818                                                     
JRNL        DOI    10.1006/JMBI.2000.4029                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : SHELXL-97                                            
REMARK   3   AUTHORS     : G.M.SHELDRICK                                        
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 500.00                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.0                           
REMARK   3   CROSS-VALIDATION METHOD           : FREE R                         
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).                         
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : 0.136                  
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.134                  
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.163                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 10.000                 
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 7782                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 77150                  
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).                     
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : 0.124                  
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : 0.122                  
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : 0.151                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 10.000                 
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : 6361                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : 63169                  
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS      : 1150                                          
REMARK   3   NUCLEIC ACID ATOMS : 0                                             
REMARK   3   HETEROGEN ATOMS    : 5                                             
REMARK   3   SOLVENT ATOMS      : 178                                           
REMARK   3                                                                      
REMARK   3  MODEL REFINEMENT.                                                   
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : 1327.0                  
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : 1089.0                  
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : 36                      
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : 14894                   
REMARK   3   NUMBER OF RESTRAINTS                     : 22732                   
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.                        
REMARK   3   BOND LENGTHS                         (A) : 0.010                   
REMARK   3   ANGLE DISTANCES                      (A) : 0.030                   
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000                   
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : 0.023                   
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : 0.070                   
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.080                   
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : 0.080                   
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : 0.000                   
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : 0.050                   
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : 0.100                   
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED: MOEWS & KRETSINGER, J.MOL.BIOL.91 (1973)201-228       
REMARK   3                                                                      
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER                      
REMARK   3   SPECIAL CASE: NULL                                                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: ANISOTROPIC REFINEMENT REDUCED FREE R     
REMARK   3  (NO CUTOFF) BY 9%                                                   
REMARK   4                                                                      
REMARK   4 1EXR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-MAY-00.                  
REMARK 100 THE DEPOSITION ID IS D_1000011001.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-JUL-99                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 5.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL9-2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.886                              
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL                     
REMARK 200  OPTICS                         : MIRROR                             
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 78247                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.9                               
REMARK 200  DATA REDUNDANCY                : 5.400                              
REMARK 200  R MERGE                    (I) : 0.07300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 17.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.04                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 83.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.50600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: UNPUBLISHED 1.1 A PARAMECIUM TETRAURELIA             
REMARK 200  CALMODULIN                                                          
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 40.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.99                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: MPD, CALCIUM CHLORIDE, SODIUM            
REMARK 280  CACODYLATE, PH 5.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE      
REMARK 280  278K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     LYS A   148                                                      
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    GLU A  54   OE1 -  CD  -  OE2 ANGL. DEV. =  12.9 DEGREES          
REMARK 500    LEU A  69   CA  -  CB  -  CG  ANGL. DEV. =  14.1 DEGREES          
REMARK 500    ARG A  74   CD  -  NE  -  CZ  ANGL. DEV. =  16.7 DEGREES          
REMARK 500    ARG A  74   NE  -  CZ  -  NH1 ANGL. DEV. =   8.4 DEGREES          
REMARK 500    ARG A  74   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    GLU A  78   OE1 -  CD  -  OE2 ANGL. DEV. =  -7.4 DEGREES          
REMARK 500    ASP A 119   CB  -  CG  -  OD2 ANGL. DEV. =  -5.5 DEGREES          
REMARK 500    ASP A 122   CB  -  CG  -  OD1 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    ARG A 126   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.7 DEGREES          
REMARK 500    ARG A 143   CG  -  CD  -  NE  ANGL. DEV. =  29.0 DEGREES          
REMARK 500    ARG A 143   CD  -  NE  -  CZ  ANGL. DEV. =  17.1 DEGREES          
REMARK 500    ARG A 143   NE  -  CZ  -  NH1 ANGL. DEV. =   4.1 DEGREES          
REMARK 500    ARG A 143   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.9 DEGREES          
REMARK 500    SER A 147   CA  -  C   -  O   ANGL. DEV. =  15.0 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    GLN A   3      -70.65   -175.69                                   
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                              CA A1000  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A2122   O                                                      
REMARK 620 2 GLU A  31   OE1  83.1                                              
REMARK 620 3 THR A  26   O   105.7  75.8                                        
REMARK 620 4 ASP A  22   OD1  86.7 126.8 156.1                                  
REMARK 620 5 GLU A  31   OE2  90.1  53.0 124.2  75.0                            
REMARK 620 6 ASP A  20   OD1 164.1 112.7  80.2  82.9  98.7                      
REMARK 620 7 ASP A  24   OD1  81.8 146.3  79.6  82.2 156.2  84.9                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A1001  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  56   OD1                                                    
REMARK 620 2 ASN A  60   OD1  85.9                                              
REMARK 620 3 THR A  62   O    79.3  79.5                                        
REMARK 620 4 HOH A2011   O   143.3  73.0  67.7                                  
REMARK 620 5 GLU A  67   OE1 103.1 157.1  81.6  88.0                            
REMARK 620 6 ASP A  58   OD1  77.6  76.5 147.6 123.8 125.8                      
REMARK 620 7 HOH A2127   O   152.8  92.7 127.2  60.1  88.5  75.7                
REMARK 620 8 GLU A  67   OE2  87.4 151.1 126.7 124.9  51.5  74.6  80.7          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A1002  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 140   OE1                                                    
REMARK 620 2 ASP A 133   OD1 147.3                                              
REMARK 620 3 ASP A 129   OD1 108.7  93.5                                        
REMARK 620 4 GLU A 140   OE2  52.3 158.4  81.8                                  
REMARK 620 5 HOH A2129   O    83.0  79.2 166.2 100.6                            
REMARK 620 6 HIS A 135   O    79.6  76.9  89.4 123.9 100.2                      
REMARK 620 7 ASP A 131   OD1 126.8  78.1  83.6  80.4  83.4 153.5                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A1003  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A2123   O                                                      
REMARK 620 2 GLU A  47   OE1  85.4                                              
REMARK 620 3 GLU A  47   OE2 133.3  52.8                                        
REMARK 620 4 HOH A2125   O    81.6  86.9  76.7                                  
REMARK 620 5 HOH A2126   O   148.9 110.5  74.4 124.3                            
REMARK 620 6 HOH A2124   O    76.2  91.1 118.9 157.8  77.0                      
REMARK 620 7 ASP A  58   OD2  88.5 169.7 128.9  84.0  78.8  95.5                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A1004  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  93   OD1                                                    
REMARK 620 2 ASP A  95   OD1  86.8                                              
REMARK 620 3 LEU A  99   O    86.9 155.4                                        
REMARK 620 4 GLU A 104   OE1  98.6 126.8  77.7                                  
REMARK 620 5 GLU A 104   OE2 100.3  74.6 130.0  52.3                            
REMARK 620 6 HOH A2128   O   174.2  88.4  96.2  86.9  81.5                      
REMARK 620 7 ASN A  97   OD1  87.5  77.4  78.7 155.2 150.3  88.3                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1000                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1004                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1CLM   RELATED DB: PDB                                   
REMARK 900 1.8 ANGSTROM STRUCTURE OF WILD TYPE PARAMECIUM TETRAURELIA           
REMARK 900 CALMODULIN                                                           
REMARK 900 RELATED ID: 1OSA   RELATED DB: PDB                                   
REMARK 900 1.68 ANGSTROM STRUCTURE OF RECOMBINANT PARAMECIUM TETRAURELIA        
REMARK 900 CALMODULIN                                                           
DBREF  1EXR A    1   148  UNP    P07463   CALM_PARTE       2    149             
SEQRES   1 A  148  ALA GLU GLN LEU THR GLU GLU GLN ILE ALA GLU PHE LYS          
SEQRES   2 A  148  GLU ALA PHE ALA LEU PHE ASP LYS ASP GLY ASP GLY THR          
SEQRES   3 A  148  ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER LEU          
SEQRES   4 A  148  GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET ILE          
SEQRES   5 A  148  ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP PHE          
SEQRES   6 A  148  PRO GLU PHE LEU SER LEU MET ALA ARG LYS MET LYS GLU          
SEQRES   7 A  148  GLN ASP SER GLU GLU GLU LEU ILE GLU ALA PHE LYS VAL          
SEQRES   8 A  148  PHE ASP ARG ASP GLY ASN GLY LEU ILE SER ALA ALA GLU          
SEQRES   9 A  148  LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU THR          
SEQRES  10 A  148  ASP ASP GLU VAL ASP GLU MET ILE ARG GLU ALA ASP ILE          
SEQRES  11 A  148  ASP GLY ASP GLY HIS ILE ASN TYR GLU GLU PHE VAL ARG          
SEQRES  12 A  148  MET MET VAL SER LYS                                          
HET     CA  A1000       1                                                       
HET     CA  A1001       1                                                       
HET     CA  A1002       1                                                       
HET     CA  A1003       1                                                       
HET     CA  A1004       1                                                       
HETNAM      CA CALCIUM ION                                                      
FORMUL   2   CA    5(CA 2+)                                                     
FORMUL   7  HOH   *178(H2 O)                                                    
HELIX    1   1 THR A    5  ASP A   20  1                                  16    
HELIX    2   2 THR A   28  LEU A   39  1                                  12    
HELIX    3   3 THR A   44  GLU A   54  1                                  11    
HELIX    4   4 PHE A   65  ASP A   93  1                                  29    
HELIX    5   5 SER A  101  LEU A  112  1                                  12    
HELIX    6   6 THR A  117  ASP A  129  1                                  13    
HELIX    7   7 ASN A  137  SER A  147  1                                  11    
SHEET    1   A 2 THR A  26  ILE A  27  0                                        
SHEET    2   A 2 ILE A  63  ASP A  64 -1  N  ILE A  63   O  ILE A  27           
LINK        CA    CA A1000                 O   HOH A2122     1555   1555  2.35  
LINK        CA    CA A1000                 OE1 GLU A  31     1555   1555  2.47  
LINK        CA    CA A1000                 O   THR A  26     1555   1555  2.36  
LINK        CA    CA A1000                 OD1 ASP A  22     1555   1555  2.44  
LINK        CA    CA A1000                 OE2 GLU A  31     1555   1555  2.48  
LINK        CA    CA A1000                 OD1 ASP A  20     1555   1555  2.31  
LINK        CA    CA A1000                 OD1 ASP A  24     1555   1555  2.35  
LINK        CA    CA A1001                 OD1 ASP A  56     1555   1555  2.34  
LINK        CA    CA A1001                 OD1 ASN A  60     1555   1555  2.40  
LINK        CA    CA A1001                 O   THR A  62     1555   1555  2.41  
LINK        CA    CA A1001                 O   HOH A2011     1555   1555  2.90  
LINK        CA    CA A1001                 OE1 GLU A  67     1555   1555  2.47  
LINK        CA    CA A1001                 OD1 ASP A  58     1555   1555  2.44  
LINK        CA    CA A1001                 O   HOH A2127     1555   1555  2.42  
LINK        CA    CA A1001                 OE2 GLU A  67     1555   1555  2.60  
LINK        CA    CA A1002                 OE1 GLU A 140     1555   1555  2.44  
LINK        CA    CA A1002                 OD1 ASP A 133     1555   1555  2.39  
LINK        CA    CA A1002                 OD1 ASP A 129     1555   1555  2.30  
LINK        CA    CA A1002                 OE2 GLU A 140     1555   1555  2.55  
LINK        CA    CA A1002                 O   HOH A2129     1555   1555  2.42  
LINK        CA    CA A1002                 O   HIS A 135     1555   1555  2.35  
LINK        CA    CA A1002                 OD1 ASP A 131     1555   1555  2.35  
LINK        CA    CA A1003                 O   HOH A2123     1555   1555  2.41  
LINK        CA    CA A1003                 OE1 GLU A  47     1555   1555  2.50  
LINK        CA    CA A1003                 OE2 GLU A  47     1555   1555  2.45  
LINK        CA    CA A1003                 O   HOH A2125     1555   1555  2.40  
LINK        CA    CA A1003                 O   HOH A2126     1555   1555  2.36  
LINK        CA    CA A1003                 O   HOH A2124     1555   1555  2.41  
LINK        CA    CA A1004                 OD1 ASP A  93     1555   1555  2.30  
LINK        CA    CA A1004                 OD1 ASP A  95     1555   1555  2.33  
LINK        CA    CA A1004                 O   LEU A  99     1555   1555  2.28  
LINK        CA    CA A1004                 OE1 GLU A 104     1555   1555  2.46  
LINK        CA    CA A1004                 OE2 GLU A 104     1555   1555  2.54  
LINK        CA    CA A1004                 O   HOH A2128     1555   1555  2.37  
LINK        CA    CA A1004                 OD1 ASN A  97     1555   1555  2.42  
LINK        CA    CA A1003                 OD2 ASP A  58     1555   1545  2.38  
SITE     1 AC1  6 ASP A  20  ASP A  22  ASP A  24  THR A  26                    
SITE     2 AC1  6 GLU A  31  HOH A2122                                          
SITE     1 AC2  7 ASP A  56  ASP A  58  ASN A  60  THR A  62                    
SITE     2 AC2  7 GLU A  67  HOH A2011  HOH A2127                               
SITE     1 AC3  6 ASP A 129  ASP A 131  ASP A 133  HIS A 135                    
SITE     2 AC3  6 GLU A 140  HOH A2129                                          
SITE     1 AC4  6 GLU A  47  ASP A  58  HOH A2123  HOH A2124                    
SITE     2 AC4  6 HOH A2125  HOH A2126                                          
SITE     1 AC5  6 ASP A  93  ASP A  95  ASN A  97  LEU A  99                    
SITE     2 AC5  6 GLU A 104  HOH A2128                                          
CRYST1   25.015   29.415   52.761  89.54  86.10  82.39 P 1           1          
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      0.039976 -0.005341 -0.002731        0.00000                         
SCALE2      0.000000  0.034298  0.000034        0.00000                         
SCALE3      0.000000  0.000000  0.018997        0.00000                         
ATOM      1  N   GLU A   2      43.445  22.193  16.450  1.00 73.63           N  
ANISOU    1  N   GLU A   2    10821   6903  10252   2913    678  -3029       N  
ATOM      2  CA  GLU A   2      44.063  20.888  16.709  1.00 54.51           C  
ANISOU    2  CA  GLU A   2     5247   7113   8351   1480   1726  -1999       C  
ATOM      3  C   GLU A   2      43.253  19.758  16.065  1.00 43.35           C  
ANISOU    3  C   GLU A   2     4470   6363   5639   1361   1887   -217       C  
ATOM      4  O   GLU A   2      42.032  19.888  16.012  1.00 56.10           O  
ANISOU    4  O   GLU A   2     4505   7071   9741   1301   1176   1385       O  
ATOM      5  CB  GLU A   2      44.191  20.638  18.194  1.00 47.59           C  
ANISOU    5  CB  GLU A   2     2385   7778   7918    372   2340  -2864       C  
ATOM      6  CG  GLU A   2      44.656  19.300  18.619  1.00 45.96           C  
ANISOU    6  CG  GLU A   2     2506   7992   6964   -232    650  -2519       C  
ATOM      7  CD  GLU A   2      43.705  18.165  18.854  1.00 48.36           C  
ANISOU    7  CD  GLU A   2     1406   7640   9329    295    131  -2609       C  
ATOM      8  OE1 GLU A   2      43.991  17.337  19.725  1.00 57.68           O  
ANISOU    8  OE1 GLU A   2     2541   6219  13156     58  -1026  -1530       O  
ATOM      9  OE2 GLU A   2      42.673  18.032  18.165  1.00 67.34           O  
ANISOU    9  OE2 GLU A   2     3276  13352   8958  -2242   -843  -1859       O  
ATOM     10  N   GLN A   3      44.017  18.747  15.676  1.00 43.35           N  
ANISOU   10  N   GLN A   3     6161   5708   4604   2258    621    350       N  
ATOM     11  CA  GLN A   3      43.537  17.695  14.807  1.00 43.98           C  
ANISOU   11  CA  GLN A   3     4857   8152   3702   3008    429   -946       C  
ATOM     12  C   GLN A   3      44.577  16.589  14.589  1.00 32.96           C  
ANISOU   12  C   GLN A   3     3143   7390   1991   1992  -1068  -1051       C  
ATOM     13  O   GLN A   3      44.279  15.499  15.107  1.00 32.39           O  
ANISOU   13  O   GLN A   3     2268   7297   2741   1297   -686  -1546       O  
ATOM     14  CB  GLN A   3      43.084  18.249  13.460  1.00 55.09           C  
ANISOU   14  CB  GLN A   3     6475   9073   5384   4718   -881   -183       C  
ATOM     15  CG  GLN A   3      42.109  17.382  12.679  1.00 54.76           C  
ANISOU   15  CG  GLN A   3     5513  10285   5010   4907  -1304    161       C  
ATOM     16  CD  GLN A   3      40.860  17.060  13.478  1.00 56.67           C  
ANISOU   16  CD  GLN A   3     8340   8986   4205   3073   -552   1570       C  
ATOM     17  OE1 GLN A   3      40.994  16.649  14.628  1.00 69.10           O  
ANISOU   17  OE1 GLN A   3    14801   7863   3590   7630    584    440       O  
ATOM     18  NE2 GLN A   3      39.641  17.205  12.979  1.00 57.86           N  
ANISOU   18  NE2 GLN A   3     6432   9081   6471   3758   1612   2237       N  
ATOM     19  N   LEU A   4      45.660  16.805  13.868  1.00 30.29           N  
ANISOU   19  N   LEU A   4     3783   6249   1475   2510   -776   -357       N  
ATOM     20  CA  LEU A   4      46.704  15.831  13.550  1.00 29.51           C  
ANISOU   20  CA  LEU A   4     3353   6103   1759   2153  -1296  -1419       C  
ATOM     21  C   LEU A   4      48.129  16.353  13.615  1.00 28.22           C  
ANISOU   21  C   LEU A   4     3559   5792   1371   1859  -1123   -968       C  
ATOM     22  O   LEU A   4      48.508  17.449  13.168  1.00 32.63           O  
ANISOU   22  O   LEU A   4     4314   5139   2943   2114  -1446  -1021       O  
ATOM     23  CB  LEU A   4      46.537  15.239  12.129  1.00 32.41           C  
ANISOU   23  CB  LEU A   4     3079   7462   1772   1995  -1335  -1555       C  
ATOM     24  CG  LEU A   4      45.227  14.533  11.821  1.00 34.37           C  
ANISOU   24  CG  LEU A   4     3344   7442   2273   1731  -1308  -1842       C  
ATOM     25  CD1 LEU A   4      45.072  14.269  10.326  1.00 36.23           C  
ANISOU   25  CD1 LEU A   4     3852   7473   2440   1899  -1753  -1959       C  
ATOM     26  CD2 LEU A   4      45.137  13.224  12.585  1.00 35.72           C  
ANISOU   26  CD2 LEU A   4     3306   7584   2683   1818  -1207  -1601       C  
ATOM     27  N   THR A   5      49.020  15.460  14.115  1.00 24.13           N  
ANISOU   27  N   THR A   5     2946   4924   1296   1323   -918  -1167       N  
ATOM     28  CA  THR A   5      50.447  15.810  14.079  1.00 23.38           C  
ANISOU   28  CA  THR A   5     3172   4470   1241   1093   -939   -721       C  
ATOM     29  C   THR A   5      51.039  15.570  12.684  1.00 22.54           C  
ANISOU   29  C   THR A   5     3035   4509   1022    385  -1020   -657       C  
ATOM     30  O   THR A   5      50.461  14.847  11.858  1.00 19.96           O  
ANISOU   30  O   THR A   5     2985   3520   1081    321   -634   -520       O  
ATOM     31  CB  THR A   5      51.236  14.959  15.073  1.00 19.48           C  
ANISOU   31  CB  THR A   5     2373   3971   1058    623   -462   -572       C  
ATOM     32  OG1 THR A   5      51.155  13.611  14.632  1.00 18.67           O  
ANISOU   32  OG1 THR A   5     1970   4091   1032    318   -398   -575       O  
ATOM     33  CG2 THR A   5      50.648  15.068  16.495  1.00 22.08           C  
ANISOU   33  CG2 THR A   5     2805   4618    969   -141   -445   -769       C  
ATOM     34  N   GLU A   6      52.224  16.134  12.437  1.00 24.24           N  
ANISOU   34  N   GLU A   6     3620   4190   1401   -117   -852   -921       N  
ATOM     35  CA  GLU A   6      52.947  15.908  11.180  1.00 23.41           C  
ANISOU   35  CA  GLU A   6     3530   4065   1300   -244   -729   -405       C  
ATOM     36  C   GLU A   6      53.233  14.406  11.037  1.00 21.17           C  
ANISOU   36  C   GLU A   6     2756   4230   1057     62   -372   -271       C  
ATOM     37  O   GLU A   6      53.136  13.822   9.913  1.00 20.41           O  
ANISOU   37  O   GLU A   6     2690   3943   1121   -555   -481   -220       O  
ATOM     38  CB  GLU A   6      54.201  16.766  11.171  1.00 29.54           C  
ANISOU   38  CB  GLU A   6     3963   4952   2309   -875   -662   -992       C  
ATOM     39  CG  GLU A   6      54.891  16.943   9.799  1.00 34.48           C  
ANISOU   39  CG  GLU A   6     4984   4430   3686   -355    511    739       C  
ATOM     40  CD  GLU A   6      55.262  18.434   9.823  1.00 41.97           C  
ANISOU   40  CD  GLU A   6     7150   3939   4858    424    836    195       C  
ATOM     41  OE1 GLU A   6      54.687  18.992  10.803  1.00 58.16           O  
ANISOU   41  OE1 GLU A   6    11624   6703   3771   3540   -904  -1012       O  
ATOM     42  OE2 GLU A   6      56.009  18.919   9.000  1.00 59.80           O  
ANISOU   42  OE2 GLU A   6     6138   5293  11288  -2129   2556    305       O  
ATOM     43  N   GLU A   7      53.533  13.702  12.116  1.00 20.13           N  
ANISOU   43  N   GLU A   7     2165   4220   1262   -334   -373   -135       N  
ATOM     44  CA  GLU A   7      53.762  12.263  12.038  1.00 18.74           C  
ANISOU   44  CA  GLU A   7     1656   4340   1124    108   -470   -177       C  
ATOM     45  C   GLU A   7      52.498  11.484  11.693  1.00 16.59           C  
ANISOU   45  C   GLU A   7     1625   3792    888    310   -347   -274       C  
ATOM     46  O   GLU A   7      52.569  10.583  10.885  1.00 17.01           O  
ANISOU   46  O   GLU A   7     1644   3692   1128    494   -374   -322       O  
ATOM     47  CB  GLU A   7      54.372  11.761  13.341  1.00 20.40           C  
ANISOU   47  CB  GLU A   7     1515   5030   1205   -318   -461    297       C  
ATOM     48  CG  GLU A   7      54.593  10.273  13.376  1.00 25.03           C  
ANISOU   48  CG  GLU A   7     3005   5273   1233    604   -981    253       C  
ATOM     49  CD  GLU A   7      55.520   9.719  12.310  1.00 28.18           C  
ANISOU   49  CD  GLU A   7     3212   5821   1675   1431   -829    620       C  
ATOM     50  OE1 GLU A   7      56.482  10.353  11.807  1.00 41.67           O  
ANISOU   50  OE1 GLU A   7     2978   7764   5090   1280    591    426       O  
ATOM     51  OE2 GLU A   7      55.305   8.552  11.930  1.00 33.78           O  
ANISOU   51  OE2 GLU A   7     3733   6252   2849   1979  -1138   -518       O  
ATOM     52  N   GLN A   8      51.345  11.827  12.274  1.00 16.10           N  
ANISOU   52  N   GLN A   8     1606   3693    820    377   -360   -202       N  
ATOM     53  CA  GLN A   8      50.125  11.194  11.846  1.00 15.79           C  
ANISOU   53  CA  GLN A   8     1603   3596    802    340   -439   -149       C  
ATOM     54  C   GLN A   8      49.860  11.431  10.346  1.00 14.53           C  
ANISOU   54  C   GLN A   8     1676   3012    834    335   -299   -187       C  
ATOM     55  O   GLN A   8      49.477  10.500   9.631  1.00 14.74           O  
ANISOU   55  O   GLN A   8     1746   2968    887    282   -398   -150       O  
ATOM     56  CB  GLN A   8      48.901  11.729  12.636  1.00 17.49           C  
ANISOU   56  CB  GLN A   8     1570   4211    865    362   -308   -146       C  
ATOM     57  CG  GLN A   8      48.898  11.267  14.104  1.00 19.61           C  
ANISOU   57  CG  GLN A   8     1712   4811    929    -61   -237    -66       C  
ATOM     58  CD  GLN A   8      47.721  11.984  14.800  1.00 22.58           C  
ANISOU   58  CD  GLN A   8     1907   5782    890    194   -286   -480       C  
ATOM     59  OE1 GLN A   8      47.751  13.197  14.980  1.00 23.84           O  
ANISOU   59  OE1 GLN A   8     1583   5869   1605    416   -332   -822       O  
ATOM     60  NE2 GLN A   8      46.715  11.193  15.121  1.00 25.44           N  
ANISOU   60  NE2 GLN A   8     1702   6546   1416   -258   -188  -1222       N  
ATOM     61  N  AILE A   9      50.042  12.619   9.863  0.60 15.47           N  
ANISOU   61  N  AILE A   9     1965   2991    922    202   -781   -308       N  
ATOM     62  N  BILE A   9      50.064  12.669   9.955  0.40 15.79           N  
ANISOU   62  N  BILE A   9     2130   2878    993    465   -167   -275       N  
ATOM     63  CA AILE A   9      49.760  12.880   8.443  0.60 16.16           C  
ANISOU   63  CA AILE A   9     2382   3000    756    385   -545   -300       C  
ATOM     64  CA BILE A   9      49.894  13.068   8.557  0.40 14.97           C  
ANISOU   64  CA BILE A   9     2288   2477    923    -33   -270   -374       C  
ATOM     65  C  AILE A   9      50.740  12.096   7.568  0.60 16.68           C  
ANISOU   65  C  AILE A   9     2239   3039   1059    311   -573   -379       C  
ATOM     66  C  BILE A   9      50.739  12.182   7.629  0.40 15.01           C  
ANISOU   66  C  BILE A   9     2285   2689    729    302   -548   -222       C  
ATOM     67  O  AILE A   9      50.344  11.527   6.549  0.60 13.30           O  
ANISOU   67  O  AILE A   9     2127   2080    845    387   -510    -91       O  
ATOM     68  O  BILE A   9      50.215  11.661   6.634  0.40 13.83           O  
ANISOU   68  O  BILE A   9     1927   2592    737   -175   -109   -359       O  
ATOM     69  CB AILE A   9      49.712  14.388   8.233  0.60 17.94           C  
ANISOU   69  CB AILE A   9     2984   3034    796    414   -406   -347       C  
ATOM     70  CB BILE A   9      50.201  14.546   8.306  0.40 15.90           C  
ANISOU   70  CB BILE A   9     2289   2546   1204    -86   -466   -365       C  
ATOM     71  CG1AILE A   9      48.529  15.065   8.881  0.60 19.71           C  
ANISOU   71  CG1AILE A   9     2456   3151   1883    413   -672   -810       C  
ATOM     72  CG1BILE A   9      49.111  15.466   8.868  0.40 14.83           C  
ANISOU   72  CG1BILE A   9     2099   2377   1158   -108   -545   -224       C  
ATOM     73  CG2AILE A   9      49.644  14.632   6.712  0.60 18.98           C  
ANISOU   73  CG2AILE A   9     2856   3403    954    399  -1131    -62       C  
ATOM     74  CG2BILE A   9      50.339  14.857   6.814  0.40 13.92           C  
ANISOU   74  CG2BILE A   9     1554   2455   1279   -617   -478   -279       C  
ATOM     75  CD1AILE A   9      48.524  16.563   9.024  0.60 23.19           C  
ANISOU   75  CD1AILE A   9     3229   3191   2390    507   -920   -988       C  
ATOM     76  CD1BILE A   9      49.568  16.907   8.941  0.40 21.29           C  
ANISOU   76  CD1BILE A   9     3756   2333   1999   -249   -881   -495       C  
ATOM     77  N   ALA A  10      52.006  12.040   7.976  1.00 16.22           N  
ANISOU   77  N   ALA A  10     2140   2976   1047     96   -428   -316       N  
ATOM     78  CA  ALA A  10      52.970  11.271   7.207  1.00 15.86           C  
ANISOU   78  CA  ALA A  10     2032   3012    983   -114   -280   -258       C  
ATOM     79  C   ALA A  10      52.525   9.824   7.134  1.00 14.08           C  
ANISOU   79  C   ALA A  10     1514   2837    999    143   -389    -98       C  
ATOM     80  O   ALA A  10      52.586   9.200   6.066  1.00 14.53           O  
ANISOU   80  O   ALA A  10     1636   2715   1170    140   -266   -110       O  
ATOM     81  CB  ALA A  10      54.346  11.404   7.820  1.00 18.40           C  
ANISOU   81  CB  ALA A  10     1848   3480   1663   -359   -211   -704       C  
ATOM     82  N  AGLU A  11      52.061   9.296   8.275  0.44 15.90           N  
ANISOU   82  N  AGLU A  11     1831   3026   1186    246   -330    151       N  
ATOM     83  N  BGLU A  11      52.057   9.197   8.209  0.56 15.09           N  
ANISOU   83  N  BGLU A  11     1665   2902   1165    433   -482    269       N  
ATOM     84  CA AGLU A  11      51.546   7.936   8.363  0.44 14.66           C  
ANISOU   84  CA AGLU A  11     1882   2833    856    460   -290    113       C  
ATOM     85  CA BGLU A  11      51.682   7.783   8.120  0.56 15.80           C  
ANISOU   85  CA BGLU A  11     2067   2757   1179    592   -547    425       C  
ATOM     86  C  AGLU A  11      50.383   7.727   7.397  0.44 13.66           C  
ANISOU   86  C  AGLU A  11     1864   2650    678    294   -196    291       C  
ATOM     87  C  BGLU A  11      50.422   7.562   7.298  0.56 14.26           C  
ANISOU   87  C  BGLU A  11     1683   2643   1091    413   -107     64       C  
ATOM     88  O  AGLU A  11      50.391   6.775   6.606  0.44 12.45           O  
ANISOU   88  O  AGLU A  11     1812   1781   1137   -214   -195    611       O  
ATOM     89  O  BGLU A  11      50.190   6.519   6.668  0.56 17.23           O  
ANISOU   89  O  BGLU A  11     2665   2656   1227    718   -516    -85       O  
ATOM     90  CB AGLU A  11      51.112   7.561   9.802  0.44 17.94           C  
ANISOU   90  CB AGLU A  11     2935   3147    734    350   -485    358       C  
ATOM     91  CB BGLU A  11      51.550   7.251   9.567  0.56 16.15           C  
ANISOU   91  CB BGLU A  11     1706   3260   1169    -32   -211    333       C  
ATOM     92  CG AGLU A  11      52.323   7.209  10.666  0.44 21.16           C  
ANISOU   92  CG AGLU A  11     3062   3861   1116    374   -698    432       C  
ATOM     93  CG BGLU A  11      52.838   7.443  10.375  0.56 20.25           C  
ANISOU   93  CG BGLU A  11     2411   3868   1415   -199   -868    717       C  
ATOM     94  CD AGLU A  11      52.011   7.191  12.138  0.44 25.14           C  
ANISOU   94  CD AGLU A  11     4149   4432    971    744   -895    485       C  
ATOM     95  CD BGLU A  11      52.867   6.691  11.676  0.56 22.28           C  
ANISOU   95  CD BGLU A  11     3111   3902   1452    180   -621    808       C  
ATOM     96  OE1AGLU A  11      50.841   7.137  12.571  0.44 31.42           O  
ANISOU   96  OE1AGLU A  11     4924   5490   1523    835    277    930       O  
ATOM     97  OE1BGLU A  11      51.880   5.993  12.030  0.56 32.07           O  
ANISOU   97  OE1BGLU A  11     2816   6477   2893    154   -342   2594       O  
ATOM     98  OE2AGLU A  11      52.985   7.223  12.925  0.44 28.65           O  
ANISOU   98  OE2AGLU A  11     5697   3481   1709   1159  -2106   -124       O  
ATOM     99  OE2BGLU A  11      53.923   6.803  12.349  0.56 26.18           O  
ANISOU   99  OE2BGLU A  11     3245   4686   2018    462   -993   1298       O  
ATOM    100  N  APHE A  12      49.411   8.638   7.472  0.74 12.88           N  
ANISOU  100  N  APHE A  12     1674   2288    930     18   -214    370       N  
ATOM    101  N  BPHE A  12      49.598   8.607   7.312  0.26 13.92           N  
ANISOU  101  N  BPHE A  12     1671   2721    895    440   -304   -236       N  
ATOM    102  CA APHE A  12      48.304   8.548   6.541  0.74 12.86           C  
ANISOU  102  CA APHE A  12     1631   2357    897    -88   -231    288       C  
ATOM    103  CA BPHE A  12      48.330   8.560   6.599  0.26 13.28           C  
ANISOU  103  CA BPHE A  12     1701   2406    939    104   -350    315       C  
ATOM    104  C  APHE A  12      48.737   8.638   5.082  0.74 10.52           C  
ANISOU  104  C  APHE A  12     1469   1587    943    148   -223     93       C  
ATOM    105  C  BPHE A  12      48.559   8.720   5.105  0.26 12.24           C  
ANISOU  105  C  BPHE A  12     1437   2278    937    230   -249    171       C  
ATOM    106  O  APHE A  12      48.228   7.899   4.227  0.74 10.86           O  
ANISOU  106  O  APHE A  12     1282   1715   1128    259   -266    -12       O  
ATOM    107  O  BPHE A  12      47.882   8.163   4.245  0.26  8.55           O  
ANISOU  107  O  BPHE A  12      728   1626    893    533   -113    372       O  
ATOM    108  CB APHE A  12      47.233   9.654   6.827  0.74 13.43           C  
ANISOU  108  CB APHE A  12     1516   2905    682     74   -261   -133       C  
ATOM    109  CB BPHE A  12      47.404   9.653   7.146  0.26 14.93           C  
ANISOU  109  CB BPHE A  12     1644   3229    801    470   -210    245       C  
ATOM    110  CG APHE A  12      46.406   9.387   8.081  0.74 15.90           C  
ANISOU  110  CG APHE A  12     1522   3568    950   -439   -177   -191       C  
ATOM    111  CG BPHE A  12      46.779   9.369   8.508  0.26 18.63           C  
ANISOU  111  CG BPHE A  12     1868   4193   1019   -816     47   -219       C  
ATOM    112  CD1APHE A  12      45.729   8.177   8.186  0.74 22.70           C  
ANISOU  112  CD1APHE A  12     2592   4631   1403  -1692    511   -951       C  
ATOM    113  CD1BPHE A  12      46.363   8.099   8.866  0.26 22.51           C  
ANISOU  113  CD1BPHE A  12     2286   4506   1761  -1195    860   -239       C  
ATOM    114  CD2APHE A  12      46.355  10.237   9.122  0.74 15.13           C  
ANISOU  114  CD2APHE A  12     1375   3374    998   -167    -71   -164       C  
ATOM    115  CD2BPHE A  12      46.611  10.372   9.442  0.26 18.09           C  
ANISOU  115  CD2BPHE A  12     2022   4183    668    171   -363     53       C  
ATOM    116  CE1APHE A  12      45.018   7.857   9.320  0.74 24.63           C  
ANISOU  116  CE1APHE A  12     3016   4877   1464  -1686    412   -313       C  
ATOM    117  CE1BPHE A  12      45.792   7.812  10.087  0.26 20.64           C  
ANISOU  117  CE1BPHE A  12     1481   4958   1404  -1364    272   -211       C  
ATOM    118  CE2APHE A  12      45.581   9.970  10.240  0.74 18.86           C  
ANISOU  118  CE2APHE A  12     1439   4836    893   -801   -213   -347       C  
ATOM    119  CE2BPHE A  12      46.019  10.110  10.665  0.26 19.05           C  
ANISOU  119  CE2BPHE A  12     2004   4757    478   -375   -640    -44       C  
ATOM    120  CZ APHE A  12      44.940   8.767  10.347  0.74 21.27           C  
ANISOU  120  CZ APHE A  12     1691   5343   1047  -1284    249   -355       C  
ATOM    121  CZ BPHE A  12      45.596   8.836  10.984  0.26 21.51           C  
ANISOU  121  CZ BPHE A  12     2052   5044   1079   -690    -67    -54       C  
ATOM    122  N  ALYS A  13      49.695   9.522   4.764  0.60 11.31           N  
ANISOU  122  N  ALYS A  13     1421   1923    954     41   -184    233       N  
ATOM    123  N  BLYS A  13      49.588   9.511   4.789  0.40 11.20           N  
ANISOU  123  N  BLYS A  13     1573   2039    644    144   -252   -222       N  
ATOM    124  CA ALYS A  13      50.180   9.678   3.402  0.60 10.51           C  
ANISOU  124  CA ALYS A  13     1492   1590    911    -22   -297     75       C  
ATOM    125  CA BLYS A  13      50.030   9.641   3.407  0.40 10.54           C  
ANISOU  125  CA BLYS A  13     1569   1678    760    126   -194   -203       C  
ATOM    126  C  ALYS A  13      50.851   8.423   2.882  0.60  9.38           C  
ANISOU  126  C  ALYS A  13     1187   1366   1011   -270   -166    211       C  
ATOM    127  C  BLYS A  13      50.691   8.339   2.963  0.40  9.21           C  
ANISOU  127  C  BLYS A  13     1178   1618    705     -5     39     90       C  
ATOM    128  O  ALYS A  13      50.784   8.019   1.699  0.60  8.81           O  
ANISOU  128  O  ALYS A  13      977   1342   1027   -368     -7    216       O  
ATOM    129  O  BLYS A  13      50.352   7.902   1.842  0.40  8.43           O  
ANISOU  129  O  BLYS A  13     1023   1402    779    -64    202    -20       O  
ATOM    130  CB ALYS A  13      51.173  10.843   3.303  0.60 12.72           C  
ANISOU  130  CB ALYS A  13     2131   1434   1270   -202     64     89       C  
ATOM    131  CB BLYS A  13      50.949  10.841   3.242  0.40 10.09           C  
ANISOU  131  CB BLYS A  13     1382   1764    687     17   -498   -316       C  
ATOM    132  CG ALYS A  13      50.554  12.228   3.335  0.60 12.59           C  
ANISOU  132  CG ALYS A  13     2189   1533   1063    -98   -388   -110       C  
ATOM    133  CG BLYS A  13      51.423  11.239   1.864  0.40 14.79           C  
ANISOU  133  CG BLYS A  13     2183   2402   1035    -89   -189    290       C  
ATOM    134  CD ALYS A  13      51.479  13.381   3.018  0.60 18.14           C  
ANISOU  134  CD ALYS A  13     3360   1456   2075   -551   -179   -272       C  
ATOM    135  CD BLYS A  13      51.239  12.694   1.508  0.40 29.52           C  
ANISOU  135  CD BLYS A  13     4350   3420   3444   1755   1073   1838       C  
ATOM    136  CE ALYS A  13      50.713  14.710   2.957  0.60 22.58           C  
ANISOU  136  CE ALYS A  13     5076   1494   2011     -8    385   -136       C  
ATOM    137  CE BLYS A  13      50.819  13.045   0.081  0.40 37.43           C  
ANISOU  137  CE BLYS A  13     6485   4456   3280   3071   1589   2220       C  
ATOM    138  NZ ALYS A  13      51.606  15.877   2.828  0.60 29.13           N  
ANISOU  138  NZ ALYS A  13     5726   1526   3816   -110   1640    147       N  
ATOM    139  NZ BLYS A  13      51.381  14.371  -0.347  0.40 30.33           N  
ANISOU  139  NZ BLYS A  13     5235   4254   2036   3109   1281   1490       N  
ATOM    140  N   GLU A  14      51.571   7.722   3.759  1.00 10.98           N  
ANISOU  140  N   GLU A  14     1347   1675   1150    -18   -197    236       N  
ATOM    141  CA  GLU A  14      52.197   6.459   3.379  1.00 11.86           C  
ANISOU  141  CA  GLU A  14     1455   1747   1304     96   -123    168       C  
ATOM    142  C   GLU A  14      51.131   5.406   3.064  1.00 11.82           C  
ANISOU  142  C   GLU A  14     1486   1587   1420    119   -166    385       C  
ATOM    143  O   GLU A  14      51.230   4.617   2.102  1.00 12.70           O  
ANISOU  143  O   GLU A  14     1497   1554   1776    263   -221     95       O  
ATOM    144  CB  GLU A  14      53.140   5.974   4.522  1.00 15.01           C  
ANISOU  144  CB  GLU A  14     1469   2064   2168    163   -446    433       C  
ATOM    145  CG  GLU A  14      54.369   6.835   4.703  1.00 18.80           C  
ANISOU  145  CG  GLU A  14     1574   2933   2637   -120   -456    273       C  
ATOM    146  CD  GLU A  14      55.151   6.551   5.982  1.00 27.48           C  
ANISOU  146  CD  GLU A  14     1914   5971   2555     28   -802   -358       C  
ATOM    147  OE1 GLU A  14      54.567   6.274   7.043  1.00 27.17           O  
ANISOU  147  OE1 GLU A  14     2854   4832   2638    423   -835    271       O  
ATOM    148  OE2 GLU A  14      56.400   6.660   5.994  1.00 34.88           O  
ANISOU  148  OE2 GLU A  14     1873   6901   4478    622  -1047    156       O  
ATOM    149  N   ALA A  15      50.061   5.384   3.877  1.00 11.67           N  
ANISOU  149  N   ALA A  15     1490   1646   1297      8   -226    494       N  
ATOM    150  CA  ALA A  15      48.960   4.448   3.626  1.00 11.89           C  
ANISOU  150  CA  ALA A  15     1565   1354   1598     76   -200    661       C  
ATOM    151  C   ALA A  15      48.280   4.775   2.282  1.00 10.70           C  
ANISOU  151  C   ALA A  15     1467   1100   1499    -50   -192    496       C  
ATOM    152  O   ALA A  15      47.969   3.888   1.488  1.00 13.00           O  
ANISOU  152  O   ALA A  15     1874   1094   1973   -183   -442    509       O  
ATOM    153  CB  ALA A  15      47.971   4.470   4.762  1.00 14.35           C  
ANISOU  153  CB  ALA A  15     1697   2067   1687      2     -9    935       C  
ATOM    154  N   PHE A  16      48.001   6.075   2.071  1.00  9.34           N  
ANISOU  154  N   PHE A  16     1288   1201   1057     61   -145    364       N  
ATOM    155  CA  PHE A  16      47.395   6.480   0.792  1.00  8.45           C  
ANISOU  155  CA  PHE A  16     1162   1007   1040    -80   -188    204       C  
ATOM    156  C   PHE A  16      48.233   6.057  -0.379  1.00  8.21           C  
ANISOU  156  C   PHE A  16     1226    835   1058    -35   -109    135       C  
ATOM    157  O   PHE A  16      47.686   5.591  -1.412  1.00  8.95           O  
ANISOU  157  O   PHE A  16     1329    813   1259    103   -228     97       O  
ATOM    158  CB  PHE A  16      47.218   8.009   0.814  1.00  8.36           C  
ANISOU  158  CB  PHE A  16     1231    994    950    -15   -154     90       C  
ATOM    159  CG  PHE A  16      46.484   8.571  -0.372  1.00  7.37           C  
ANISOU  159  CG  PHE A  16     1157    766    877   -138   -109     86       C  
ATOM    160  CD1 PHE A  16      45.107   8.614  -0.414  1.00  8.53           C  
ANISOU  160  CD1 PHE A  16     1117    941   1181   -145   -109    236       C  
ATOM    161  CD2 PHE A  16      47.190   9.084  -1.436  1.00  8.44           C  
ANISOU  161  CD2 PHE A  16     1212    929   1067    -64    -40    165       C  
ATOM    162  CE1 PHE A  16      44.442   9.156  -1.508  1.00  8.92           C  
ANISOU  162  CE1 PHE A  16     1217    812   1361   -159   -316    149       C  
ATOM    163  CE2 PHE A  16      46.553   9.620  -2.534  1.00  9.01           C  
ANISOU  163  CE2 PHE A  16     1548    841   1036    -92    -50    235       C  
ATOM    164  CZ  PHE A  16      45.163   9.663  -2.573  1.00  9.14           C  
ANISOU  164  CZ  PHE A  16     1594    600   1279   -121   -381    221       C  
ATOM    165  N   ALA A  17      49.537   6.223  -0.276  1.00  8.73           N  
ANISOU  165  N   ALA A  17     1193    969   1155    -62    -74    109       N  
ATOM    166  CA  ALA A  17      50.459   5.882  -1.385  1.00  9.18           C  
ANISOU  166  CA  ALA A  17     1273   1083   1133     86    -69     79       C  
ATOM    167  C   ALA A  17      50.368   4.440  -1.777  1.00 10.51           C  
ANISOU  167  C   ALA A  17     1424   1056   1515    224   -125     -7       C  
ATOM    168  O   ALA A  17      50.576   4.108  -2.971  1.00 12.06           O  
ANISOU  168  O   ALA A  17     1739   1241   1601    201    -30   -157       O  
ATOM    169  CB  ALA A  17      51.864   6.313  -0.985  1.00 10.81           C  
ANISOU  169  CB  ALA A  17     1244   1553   1312   -171     76    120       C  
ATOM    170  N   LEU A  18      50.110   3.524  -0.834  1.00 10.59           N  
ANISOU  170  N   LEU A  18     1372   1091   1559    261   -321     88       N  
ATOM    171  CA  LEU A  18      49.972   2.115  -1.220  1.00 11.42           C  
ANISOU  171  CA  LEU A  18     1441    981   1915    347   -265     10       C  
ATOM    172  C   LEU A  18      48.882   1.885  -2.202  1.00 10.28           C  
ANISOU  172  C   LEU A  18     1376    761   1769    215   -112    119       C  
ATOM    173  O   LEU A  18      48.956   1.002  -3.054  1.00 12.65           O  
ANISOU  173  O   LEU A  18     1439    973   2395    306   -314   -268       O  
ATOM    174  CB  LEU A  18      49.698   1.259   0.036  1.00 19.09           C  
ANISOU  174  CB  LEU A  18     3617   1256   2380    405   -900    725       C  
ATOM    175  CG  LEU A  18      49.301  -0.206  -0.323  1.00 21.34           C  
ANISOU  175  CG  LEU A  18     3608   1227   3273    265   -544    576       C  
ATOM    176  CD1 LEU A  18      50.511  -0.957  -0.886  1.00 30.08           C  
ANISOU  176  CD1 LEU A  18     4137   1663   5631    528     41     30       C  
ATOM    177  CD2 LEU A  18      48.688  -0.926   0.841  1.00 29.88           C  
ANISOU  177  CD2 LEU A  18     5620   1848   3883   -109     49   1039       C  
ATOM    178  N   PHE A  19      47.807   2.685  -2.112  1.00  9.03           N  
ANISOU  178  N   PHE A  19     1285    745   1402    118    -92    225       N  
ATOM    179  CA  PHE A  19      46.708   2.595  -3.048  1.00  8.68           C  
ANISOU  179  CA  PHE A  19     1162    598   1537    -56    -80    243       C  
ATOM    180  C   PHE A  19      46.953   3.396  -4.326  1.00  8.07           C  
ANISOU  180  C   PHE A  19     1072    547   1447    -69   -175    106       C  
ATOM    181  O   PHE A  19      46.590   2.958  -5.419  1.00  8.74           O  
ANISOU  181  O   PHE A  19     1114    653   1555   -208   -225     62       O  
ATOM    182  CB  PHE A  19      45.399   3.110  -2.401  1.00  9.31           C  
ANISOU  182  CB  PHE A  19     1210    694   1635    -52    -24    194       C  
ATOM    183  CG  PHE A  19      44.885   2.254  -1.272  1.00  9.51           C  
ANISOU  183  CG  PHE A  19     1174    773   1667    -34    -58    326       C  
ATOM    184  CD1 PHE A  19      43.982   1.216  -1.516  1.00 11.46           C  
ANISOU  184  CD1 PHE A  19     1342   1170   1843   -324    -51    370       C  
ATOM    185  CD2 PHE A  19      45.312   2.478   0.019  1.00 11.34           C  
ANISOU  185  CD2 PHE A  19     1629   1086   1591   -301    129    153       C  
ATOM    186  CE1 PHE A  19      43.539   0.401  -0.518  1.00 12.98           C  
ANISOU  186  CE1 PHE A  19     1603   1352   1976   -434     23    553       C  
ATOM    187  CE2 PHE A  19      44.855   1.623   1.036  1.00 14.14           C  
ANISOU  187  CE2 PHE A  19     2076   1616   1682   -455   -198    542       C  
ATOM    188  CZ  PHE A  19      43.939   0.627   0.753  1.00 12.90           C  
ANISOU  188  CZ  PHE A  19     1771   1275   1854   -296    166    561       C  
ATOM    189  N   ASP A  20      47.543   4.587  -4.198  1.00  8.52           N  
ANISOU  189  N   ASP A  20     1329    631   1278   -281   -234    216       N  
ATOM    190  CA  ASP A  20      47.768   5.491  -5.306  1.00  7.43           C  
ANISOU  190  CA  ASP A  20     1118    538   1166   -112   -222     87       C  
ATOM    191  C   ASP A  20      49.013   5.082  -6.062  1.00  8.75           C  
ANISOU  191  C   ASP A  20     1186    618   1521    -47   -131    228       C  
ATOM    192  O   ASP A  20      50.085   5.715  -6.020  1.00 10.32           O  
ANISOU  192  O   ASP A  20     1035    920   1963   -191   -249    310       O  
ATOM    193  CB  ASP A  20      47.839   6.934  -4.815  1.00  8.19           C  
ANISOU  193  CB  ASP A  20     1316    574   1221   -222   -297    158       C  
ATOM    194  CG  ASP A  20      48.078   7.909  -5.950  1.00  7.50           C  
ANISOU  194  CG  ASP A  20     1044    538   1269   -136   -315    150       C  
ATOM    195  OD1 ASP A  20      47.863   7.544  -7.118  1.00  7.79           O  
ANISOU  195  OD1 ASP A  20     1037    703   1219   -187   -205    170       O  
ATOM    196  OD2 ASP A  20      48.484   9.062  -5.656  1.00  8.56           O  
ANISOU  196  OD2 ASP A  20     1247    559   1447   -266   -292    156       O  
ATOM    197  N   LYS A  21      48.898   3.976  -6.798  1.00  9.97           N  
ANISOU  197  N   LYS A  21     1254    666   1867     26    144     27       N  
ATOM    198  CA  LYS A  21      49.964   3.285  -7.532  1.00 12.02           C  
ANISOU  198  CA  LYS A  21     1460    721   2385    149    349    156       C  
ATOM    199  C   LYS A  21      50.726   4.183  -8.470  1.00 10.89           C  
ANISOU  199  C   LYS A  21     1324    904   1909    173    113     32       C  
ATOM    200  O   LYS A  21      51.946   4.020  -8.611  1.00 12.86           O  
ANISOU  200  O   LYS A  21     1314   1409   2164    341    273    360       O  
ATOM    201  CB  LYS A  21      49.421   2.068  -8.298  1.00 15.07           C  
ANISOU  201  CB  LYS A  21     2263    807   2655     24    547   -209       C  
ATOM    202  CG  LYS A  21      48.752   1.002  -7.488  1.00 13.01           C  
ANISOU  202  CG  LYS A  21     1328   1196   2420   -159    -29   -204       C  
ATOM    203  CD  LYS A  21      49.673   0.566  -6.366  1.00 15.84           C  
ANISOU  203  CD  LYS A  21      919   2255   2843   -248   -120    611       C  
ATOM    204  CE  LYS A  21      49.214  -0.839  -5.808  1.00 15.69           C  
ANISOU  204  CE  LYS A  21     1483   1393   3087   -179   -414    -53       C  
ATOM    205  NZ  LYS A  21      49.951  -1.144  -4.547  1.00 12.29           N  
ANISOU  205  NZ  LYS A  21     1341    695   2634   -102    227     79       N  
ATOM    206  N   ASP A  22      50.005   5.067  -9.128  1.00 10.00           N  
ANISOU  206  N   ASP A  22     1098    867   1834     26    121     27       N  
ATOM    207  CA  ASP A  22      50.622   5.935 -10.122  1.00  9.95           C  
ANISOU  207  CA  ASP A  22     1048   1059   1674    -68    130     -7       C  
ATOM    208  C   ASP A  22      50.954   7.307  -9.605  1.00  9.63           C  
ANISOU  208  C   ASP A  22     1056    932   1670     19   -118    108       C  
ATOM    209  O   ASP A  22      51.445   8.143 -10.357  1.00 10.89           O  
ANISOU  209  O   ASP A  22     1373   1191   1576   -294     30    229       O  
ATOM    210  CB  ASP A  22      49.844   6.029 -11.426  1.00 11.01           C  
ANISOU  210  CB  ASP A  22     1241   1202   1742     14     -1   -121       C  
ATOM    211  CG  ASP A  22      48.534   6.778 -11.338  1.00 10.36           C  
ANISOU  211  CG  ASP A  22     1309    985   1641     42   -210   -241       C  
ATOM    212  OD1 ASP A  22      48.113   7.194 -10.234  1.00  9.48           O  
ANISOU  212  OD1 ASP A  22     1050    883   1668   -135    -56    -87       O  
ATOM    213  OD2 ASP A  22      47.940   6.899 -12.427  1.00 13.80           O  
ANISOU  213  OD2 ASP A  22     1744   1709   1789    513   -345   -355       O  
ATOM    214  N   GLY A  23      50.758   7.567  -8.294  1.00  9.13           N  
ANISOU  214  N   GLY A  23      996    807   1667   -141    -73    200       N  
ATOM    215  CA  GLY A  23      51.165   8.826  -7.701  1.00  9.50           C  
ANISOU  215  CA  GLY A  23     1154    924   1532   -197   -186    155       C  
ATOM    216  C   GLY A  23      50.452  10.034  -8.231  1.00  8.83           C  
ANISOU  216  C   GLY A  23     1053    875   1426   -386   -289    217       C  
ATOM    217  O   GLY A  23      51.048  11.142  -8.196  1.00 12.42           O  
ANISOU  217  O   GLY A  23     1492    945   2284   -480   -759    394       O  
ATOM    218  N   ASP A  24      49.237   9.932  -8.723  1.00  8.29           N  
ANISOU  218  N   ASP A  24      995    722   1434   -230   -185    134       N  
ATOM    219  CA  ASP A  24      48.518  11.082  -9.243  1.00  8.33           C  
ANISOU  219  CA  ASP A  24     1049    825   1292   -261   -201    152       C  
ATOM    220  C   ASP A  24      47.675  11.791  -8.228  1.00  7.68           C  
ANISOU  220  C   ASP A  24     1086    614   1216   -233   -300    166       C  
ATOM    221  O   ASP A  24      46.955  12.739  -8.570  1.00  8.88           O  
ANISOU  221  O   ASP A  24     1318    708   1350   -133   -272    120       O  
ATOM    222  CB  ASP A  24      47.656  10.734 -10.479  1.00  8.32           C  
ANISOU  222  CB  ASP A  24     1191    842   1127   -177    -99    131       C  
ATOM    223  CG  ASP A  24      46.299  10.171 -10.065  1.00  7.96           C  
ANISOU  223  CG  ASP A  24     1212    739   1071   -320   -238    129       C  
ATOM    224  OD1 ASP A  24      46.270   9.452  -9.049  1.00  7.74           O  
ANISOU  224  OD1 ASP A  24     1264    599   1078   -223   -182     58       O  
ATOM    225  OD2 ASP A  24      45.304  10.417 -10.768  1.00  9.50           O  
ANISOU  225  OD2 ASP A  24     1197   1021   1393   -358   -214    424       O  
ATOM    226  N   GLY A  25      47.744  11.412  -6.951  1.00  7.54           N  
ANISOU  226  N   GLY A  25      987    589   1289   -185   -319     62       N  
ATOM    227  CA  GLY A  25      46.928  12.066  -5.933  1.00  7.50           C  
ANISOU  227  CA  GLY A  25     1106    563   1182   -257   -301    104       C  
ATOM    228  C   GLY A  25      45.518  11.603  -5.832  1.00  6.87           C  
ANISOU  228  C   GLY A  25     1082    485   1043   -140   -251    179       C  
ATOM    229  O   GLY A  25      44.725  12.228  -5.118  1.00  7.44           O  
ANISOU  229  O   GLY A  25     1158    469   1201   -118   -271     63       O  
ATOM    230  N   THR A  26      45.172  10.515  -6.498  1.00  7.15           N  
ANISOU  230  N   THR A  26     1003    455   1259   -171   -181     87       N  
ATOM    231  CA  THR A  26      43.815   9.967  -6.428  1.00  7.23           C  
ANISOU  231  CA  THR A  26     1085    492   1170   -225   -165    148       C  
ATOM    232  C   THR A  26      43.920   8.447  -6.389  1.00  7.12           C  
ANISOU  232  C   THR A  26      972    403   1328   -150   -179     44       C  
ATOM    233  O   THR A  26      44.880   7.857  -6.907  1.00  7.79           O  
ANISOU  233  O   THR A  26     1093    506   1362   -228   -119     37       O  
ATOM    234  CB  THR A  26      42.906  10.362  -7.595  1.00  7.78           C  
ANISOU  234  CB  THR A  26     1038    549   1367   -141   -215     57       C  
ATOM    235  OG1 THR A  26      43.195   9.637  -8.799  1.00  9.17           O  
ANISOU  235  OG1 THR A  26     1298    864   1321    -82   -388   -143       O  
ATOM    236  CG2 THR A  26      42.944  11.850  -7.864  1.00  8.63           C  
ANISOU  236  CG2 THR A  26     1350    652   1275   -136   -423    134       C  
ATOM    237  N   ILE A  27      42.899   7.839  -5.799  1.00  7.30           N  
ANISOU  237  N   ILE A  27     1001    404   1366   -135    -64     77       N  
ATOM    238  CA  ILE A  27      42.705   6.385  -5.817  1.00  7.78           C  
ANISOU  238  CA  ILE A  27     1015    439   1502   -202   -116    146       C  
ATOM    239  C   ILE A  27      41.475   6.112  -6.709  1.00  8.23           C  
ANISOU  239  C   ILE A  27     1091    442   1594   -241   -195    231       C  
ATOM    240  O   ILE A  27      40.357   6.587  -6.399  1.00  8.36           O  
ANISOU  240  O   ILE A  27     1019    613   1544   -134   -166    214       O  
ATOM    241  CB  ILE A  27      42.504   5.789  -4.439  1.00  8.29           C  
ANISOU  241  CB  ILE A  27     1036    561   1555    -91   -142    194       C  
ATOM    242  CG1 ILE A  27      43.641   6.122  -3.466  1.00  8.26           C  
ANISOU  242  CG1 ILE A  27     1220    538   1381    -80   -152     92       C  
ATOM    243  CG2 ILE A  27      42.276   4.267  -4.544  1.00  9.78           C  
ANISOU  243  CG2 ILE A  27     1296    574   1845   -324   -408    338       C  
ATOM    244  CD1 ILE A  27      43.331   5.832  -2.049  1.00 10.08           C  
ANISOU  244  CD1 ILE A  27     1552    850   1429     16     -1    173       C  
ATOM    245  N   THR A  28      41.688   5.355  -7.772  1.00  8.54           N  
ANISOU  245  N   THR A  28      977    500   1768   -204   -298     85       N  
ATOM    246  CA  THR A  28      40.654   4.920  -8.685  1.00  9.03           C  
ANISOU  246  CA  THR A  28      941    734   1757   -225   -347    136       C  
ATOM    247  C   THR A  28      40.079   3.575  -8.289  1.00  9.38           C  
ANISOU  247  C   THR A  28      974    613   1977   -206   -344    113       C  
ATOM    248  O   THR A  28      40.661   2.835  -7.470  1.00  8.88           O  
ANISOU  248  O   THR A  28     1106    615   1652   -257   -329     93       O  
ATOM    249  CB  THR A  28      41.171   4.831 -10.130  1.00 10.13           C  
ANISOU  249  CB  THR A  28     1330    813   1707   -151   -299    135       C  
ATOM    250  OG1 THR A  28      42.194   3.834 -10.095  1.00 10.90           O  
ANISOU  250  OG1 THR A  28     1397    923   1822    -38   -209    121       O  
ATOM    251  CG2 THR A  28      41.709   6.140 -10.668  1.00 11.16           C  
ANISOU  251  CG2 THR A  28     1398    977   1866   -177   -191    231       C  
ATOM    252  N   THR A  29      38.943   3.197  -8.898  1.00 10.72           N  
ANISOU  252  N   THR A  29     1343    902   1830   -400   -623    311       N  
ATOM    253  CA  THR A  29      38.451   1.837  -8.728  1.00 11.81           C  
ANISOU  253  CA  THR A  29     1648    958   1881   -681   -720    238       C  
ATOM    254  C   THR A  29      39.528   0.822  -9.148  1.00 11.45           C  
ANISOU  254  C   THR A  29     1800    807   1742   -700   -730    112       C  
ATOM    255  O   THR A  29      39.679  -0.193  -8.483  1.00 13.27           O  
ANISOU  255  O   THR A  29     1761    986   2295   -762   -805    460       O  
ATOM    256  CB  THR A  29      37.166   1.580  -9.528  1.00 12.84           C  
ANISOU  256  CB  THR A  29     1545   1361   1973   -794   -585    310       C  
ATOM    257  OG1 THR A  29      37.435   1.928 -10.894  1.00 15.81           O  
ANISOU  257  OG1 THR A  29     1876   2131   1999   -839   -856    706       O  
ATOM    258  CG2 THR A  29      35.962   2.315  -8.967  1.00 16.17           C  
ANISOU  258  CG2 THR A  29     1689   1960   2497   -318   -841    154       C  
ATOM    259  N   LYS A  30      40.242   1.124 -10.249  1.00 12.26           N  
ANISOU  259  N   LYS A  30     2011   1031   1614   -526   -681     86       N  
ATOM    260  CA  LYS A  30      41.260   0.174 -10.730  1.00 14.05           C  
ANISOU  260  CA  LYS A  30     2459   1239   1640   -307   -669   -186       C  
ATOM    261  C   LYS A  30      42.340  -0.019  -9.668  1.00 11.59           C  
ANISOU  261  C   LYS A  30     1877    892   1633   -326   -360   -236       C  
ATOM    262  O   LYS A  30      42.767  -1.169  -9.415  1.00 13.55           O  
ANISOU  262  O   LYS A  30     2331    771   2046   -353   -556   -238       O  
ATOM    263  CB  LYS A  30      41.855   0.637 -12.053  1.00 20.00           C  
ANISOU  263  CB  LYS A  30     2974   3010   1616    177   -430     84       C  
ATOM    264  CG  LYS A  30      42.490  -0.532 -12.785  1.00 40.41           C  
ANISOU  264  CG  LYS A  30     5830   5266   4259   2717   2134    403       C  
ATOM    265  CD  LYS A  30      43.951  -0.705 -12.427  1.00 55.99           C  
ANISOU  265  CD  LYS A  30     6299   6762   8212   3700   1173    334       C  
ATOM    266  CE  LYS A  30      44.265  -2.129 -12.010  1.00 59.77           C  
ANISOU  266  CE  LYS A  30     6650   6592   9467   4128   1356      3       C  
ATOM    267  NZ  LYS A  30      44.100  -3.070 -13.168  1.00 68.75           N  
ANISOU  267  NZ  LYS A  30     6620   7709  11793   1119   3740  -1940       N  
ATOM    268  N   GLU A  31      42.822   1.066  -9.058  1.00 10.25           N  
ANISOU  268  N   GLU A  31     1596    658   1642   -217   -330    -99       N  
ATOM    269  CA  GLU A  31      43.863   0.972  -8.061  1.00  9.87           C  
ANISOU  269  CA  GLU A  31     1586    474   1690   -281   -284    -81       C  
ATOM    270  C   GLU A  31      43.429   0.286  -6.801  1.00  9.32           C  
ANISOU  270  C   GLU A  31     1358    473   1710   -193   -317    -85       C  
ATOM    271  O   GLU A  31      44.145  -0.502  -6.208  1.00 10.13           O  
ANISOU  271  O   GLU A  31     1376    525   1949   -172   -304     98       O  
ATOM    272  CB  GLU A  31      44.377   2.411  -7.762  1.00  9.48           C  
ANISOU  272  CB  GLU A  31     1402    516   1685   -254   -278     -8       C  
ATOM    273  CG  GLU A  31      45.245   2.934  -8.865  1.00  9.96           C  
ANISOU  273  CG  GLU A  31     1136    589   2060   -204   -131   -134       C  
ATOM    274  CD  GLU A  31      45.654   4.366  -8.696  1.00  9.16           C  
ANISOU  274  CD  GLU A  31     1171    471   1837   -116   -302      3       C  
ATOM    275  OE1 GLU A  31      44.840   5.164  -8.141  1.00  8.71           O  
ANISOU  275  OE1 GLU A  31     1226    475   1607   -188    -72     58       O  
ATOM    276  OE2 GLU A  31      46.750   4.748  -9.169  1.00 10.82           O  
ANISOU  276  OE2 GLU A  31     1012    639   2459   -178   -120   -190       O  
ATOM    277  N   LEU A  32      42.208   0.600  -6.351  1.00  9.70           N  
ANISOU  277  N   LEU A  32     1393    387   1903   -154   -320    135       N  
ATOM    278  CA  LEU A  32      41.670  -0.112  -5.196  1.00  9.76           C  
ANISOU  278  CA  LEU A  32     1358    478   1873   -156   -233     82       C  
ATOM    279  C   LEU A  32      41.609  -1.636  -5.512  1.00  9.26           C  
ANISOU  279  C   LEU A  32     1435    439   1643    -41   -105     26       C  
ATOM    280  O   LEU A  32      41.970  -2.483  -4.725  1.00  9.89           O  
ANISOU  280  O   LEU A  32     1465    493   1799    -87    -48    113       O  
ATOM    281  CB  LEU A  32      40.278   0.415  -4.858  1.00  9.73           C  
ANISOU  281  CB  LEU A  32     1522    493   1683    -24   -313     22       C  
ATOM    282  CG  LEU A  32      39.548  -0.343  -3.748  1.00 10.00           C  
ANISOU  282  CG  LEU A  32     1483    720   1595    -92   -131   -141       C  
ATOM    283  CD1 LEU A  32      40.339  -0.384  -2.470  1.00 12.02           C  
ANISOU  283  CD1 LEU A  32     1835   1222   1512    -18    -99    -88       C  
ATOM    284  CD2 LEU A  32      38.167   0.281  -3.587  1.00 12.66           C  
ANISOU  284  CD2 LEU A  32     1682   1187   1940    250      3    -33       C  
ATOM    285  N   GLY A  33      41.190  -1.946  -6.746  1.00  9.51           N  
ANISOU  285  N   GLY A  33     1291    536   1785   -138   -168     -5       N  
ATOM    286  CA  GLY A  33      41.182  -3.354  -7.159  1.00  9.58           C  
ANISOU  286  CA  GLY A  33     1354    505   1780   -122   -298    -42       C  
ATOM    287  C   GLY A  33      42.573  -3.992  -7.139  1.00  8.73           C  
ANISOU  287  C   GLY A  33     1392    485   1443   -139   -197      9       C  
ATOM    288  O   GLY A  33      42.692  -5.121  -6.661  1.00  9.51           O  
ANISOU  288  O   GLY A  33     1407    470   1737   -123   -105      7       O  
ATOM    289  N   THR A  34      43.589  -3.286  -7.595  1.00  9.22           N  
ANISOU  289  N   THR A  34     1438    437   1629   -101    -84     35       N  
ATOM    290  CA  THR A  34      44.935  -3.839  -7.535  1.00  9.32           C  
ANISOU  290  CA  THR A  34     1410    613   1518    -37    -10    -35       C  
ATOM    291  C   THR A  34      45.311  -4.230  -6.117  1.00  9.04           C  
ANISOU  291  C   THR A  34     1391    519   1526   -157   -118    -66       C  
ATOM    292  O   THR A  34      45.851  -5.320  -5.878  1.00  9.49           O  
ANISOU  292  O   THR A  34     1501    575   1530    -21   -194   -126       O  
ATOM    293  CB  THR A  34      45.921  -2.846  -8.112  1.00 10.72           C  
ANISOU  293  CB  THR A  34     1671    624   1780     23     92    105       C  
ATOM    294  OG1 THR A  34      45.516  -2.497  -9.484  1.00 12.35           O  
ANISOU  294  OG1 THR A  34     1730   1030   1934    -84    147    415       O  
ATOM    295  CG2 THR A  34      47.326  -3.412  -8.094  1.00 11.87           C  
ANISOU  295  CG2 THR A  34     1536    893   2081   -111    101     64       C  
ATOM    296  N   VAL A  35      45.037  -3.348  -5.163  1.00  9.46           N  
ANISOU  296  N   VAL A  35     1435    594   1564   -189   -137   -127       N  
ATOM    297  CA  VAL A  35      45.359  -3.620  -3.778  1.00  9.59           C  
ANISOU  297  CA  VAL A  35     1474    671   1499   -327    -82   -115       C  
ATOM    298  C   VAL A  35      44.587  -4.801  -3.223  1.00  9.99           C  
ANISOU  298  C   VAL A  35     1546    676   1576   -336   -260    -34       C  
ATOM    299  O   VAL A  35      45.106  -5.718  -2.595  1.00 10.98           O  
ANISOU  299  O   VAL A  35     1812    710   1650   -294   -435    -30       O  
ATOM    300  CB  VAL A  35      45.177  -2.379  -2.892  1.00 10.18           C  
ANISOU  300  CB  VAL A  35     1513    687   1667   -284    -38   -200       C  
ATOM    301  CG1 VAL A  35      45.423  -2.743  -1.456  1.00 13.35           C  
ANISOU  301  CG1 VAL A  35     2470   1072   1529   -584     91   -234       C  
ATOM    302  CG2 VAL A  35      46.150  -1.296  -3.347  1.00 10.52           C  
ANISOU  302  CG2 VAL A  35     1407    726   1865   -293    -72    -79       C  
ATOM    303  N  AMET A  36      43.265  -4.829  -3.463  0.61  9.55           N  
ANISOU  303  N  AMET A  36     1529    622   1479   -402   -194     -8       N  
ATOM    304  N  BMET A  36      43.279  -4.765  -3.543  0.40  9.62           N  
ANISOU  304  N  BMET A  36     1391    511   1754   -199    -13   -352       N  
ATOM    305  CA AMET A  36      42.563  -5.997  -2.912  0.61  9.67           C  
ANISOU  305  CA AMET A  36     1511    689   1473   -182    191     94       C  
ATOM    306  CA BMET A  36      42.392  -5.820  -3.083  0.40  8.43           C  
ANISOU  306  CA BMET A  36     1514    502   1189   -208   -419    -22       C  
ATOM    307  C  AMET A  36      43.010  -7.283  -3.537  0.61  8.91           C  
ANISOU  307  C  AMET A  36     1441    619   1326   -153   -338     16       C  
ATOM    308  C  BMET A  36      42.842  -7.187  -3.590  0.40  8.25           C  
ANISOU  308  C  BMET A  36     1276    505   1352    -74   -344     54       C  
ATOM    309  O  AMET A  36      43.154  -8.328  -2.887  0.61  8.86           O  
ANISOU  309  O  AMET A  36     1335    654   1378   -135   -400     90       O  
ATOM    310  O  BMET A  36      42.792  -8.167  -2.830  0.40  9.28           O  
ANISOU  310  O  BMET A  36     1774    481   1271   -262   -306     -3       O  
ATOM    311  CB AMET A  36      41.068  -5.722  -3.160  0.61  8.82           C  
ANISOU  311  CB AMET A  36     1549    394   1408   -253     55    138       C  
ATOM    312  CB BMET A  36      40.950  -5.559  -3.541  0.40  9.24           C  
ANISOU  312  CB BMET A  36     1304    641   1565    -27     92    306       C  
ATOM    313  CG AMET A  36      40.593  -4.532  -2.319  0.61  9.04           C  
ANISOU  313  CG AMET A  36     1407    807   1221   -200     24    -63       C  
ATOM    314  CG BMET A  36      40.216  -4.404  -2.910  0.40 10.79           C  
ANISOU  314  CG BMET A  36     1358   1227   1516   -126    348   -135       C  
ATOM    315  SD AMET A  36      38.887  -4.074  -2.591  0.61 10.33           S  
ANISOU  315  SD AMET A  36     1564    699   1663    -82   -152     51       S  
ATOM    316  SD BMET A  36      40.166  -4.292  -1.131  0.40 17.38           S  
ANISOU  316  SD BMET A  36     3104   2006   1492    869     -7     72       S  
ATOM    317  CE AMET A  36      38.075  -5.513  -1.865  0.61 15.46           C  
ANISOU  317  CE AMET A  36     1525    943   3408   -101    561    252       C  
ATOM    318  CE BMET A  36      39.991  -6.002  -0.672  0.40 37.98           C  
ANISOU  318  CE BMET A  36     8122   3349   2960  -2581  -1598   1724       C  
ATOM    319  N   ARG A  37      43.263  -7.249  -4.852  1.00  8.85           N  
ANISOU  319  N   ARG A  37     1412    560   1389   -182   -315     40       N  
ATOM    320  CA  ARG A  37      43.728  -8.469  -5.523  1.00  8.72           C  
ANISOU  320  CA  ARG A  37     1352    557   1404   -107   -256     13       C  
ATOM    321  C   ARG A  37      45.013  -8.946  -4.884  1.00  9.08           C  
ANISOU  321  C   ARG A  37     1343    593   1515   -166   -301    117       C  
ATOM    322  O   ARG A  37      45.238 -10.171  -4.765  1.00 10.13           O  
ANISOU  322  O   ARG A  37     1591    643   1616     13   -496     82       O  
ATOM    323  CB  ARG A  37      43.895  -8.238  -7.027  1.00  9.06           C  
ANISOU  323  CB  ARG A  37     1395    657   1391    -96   -199     57       C  
ATOM    324  CG  ARG A  37      42.607  -8.086  -7.778  1.00  9.04           C  
ANISOU  324  CG  ARG A  37     1422    605   1408    -79   -164     38       C  
ATOM    325  CD  ARG A  37      42.750  -8.045  -9.295  1.00 11.49           C  
ANISOU  325  CD  ARG A  37     1843   1063   1459    118   -292    244       C  
ATOM    326  NE  ARG A  37      43.191  -6.785  -9.813  1.00 13.02           N  
ANISOU  326  NE  ARG A  37     1810   1358   1780   -111   -181    461       N  
ATOM    327  CZ  ARG A  37      42.399  -5.726 -10.064  1.00 12.41           C  
ANISOU  327  CZ  ARG A  37     1966   1080   1670   -208   -247    506       C  
ATOM    328  NH1 ARG A  37      41.136  -5.769  -9.835  1.00 13.99           N  
ANISOU  328  NH1 ARG A  37     1830   1004   2481   -185   -586    412       N  
ATOM    329  NH2 ARG A  37      42.920  -4.644 -10.524  1.00 14.76           N  
ANISOU  329  NH2 ARG A  37     1914   1485   2209   -313   -259    794       N  
ATOM    330  N   SER A  38      45.882  -8.040  -4.481  1.00  9.97           N  
ANISOU  330  N   SER A  38     1335    761   1692   -185   -354     70       N  
ATOM    331  CA  SER A  38      47.143  -8.421  -3.841  1.00 12.32           C  
ANISOU  331  CA  SER A  38     1660   1042   1980   -105   -731     33       C  
ATOM    332  C   SER A  38      46.908  -9.115  -2.537  1.00 14.32           C  
ANISOU  332  C   SER A  38     2050   1410   1981   -129   -876    220       C  
ATOM    333  O   SER A  38      47.789  -9.873  -2.066  1.00 18.89           O  
ANISOU  333  O   SER A  38     2368   1925   2885     96  -1047    691       O  
ATOM    334  CB  SER A  38      48.060  -7.234  -3.628  1.00 13.93           C  
ANISOU  334  CB  SER A  38     1422   1319   2553   -234   -680    -68       C  
ATOM    335  OG  SER A  38      47.684  -6.460  -2.462  1.00 18.65           O  
ANISOU  335  OG  SER A  38     1942   1843   3300   -257   -776   -959       O  
ATOM    336  N  ALEU A  39      45.783  -8.876  -1.911  0.53 13.54           N  
ANISOU  336  N  ALEU A  39     2156   1271   1717   -357   -815    170       N  
ATOM    337  N  BLEU A  39      45.772  -8.924  -1.907  0.47 14.47           N  
ANISOU  337  N  BLEU A  39     2205   1573   1722   -248   -783    222       N  
ATOM    338  CA ALEU A  39      45.351  -9.363  -0.626  0.53 15.72           C  
ANISOU  338  CA ALEU A  39     2721   1819   1433   -310   -949    144       C  
ATOM    339  CA BLEU A  39      45.500  -9.545  -0.623  0.47 16.08           C  
ANISOU  339  CA BLEU A  39     2850   1576   1684   -405   -792    177       C  
ATOM    340  C  ALEU A  39      44.531 -10.645  -0.765  0.53 14.17           C  
ANISOU  340  C  ALEU A  39     2606   1395   1382   -162   -563    373       C  
ATOM    341  C  BLEU A  39      44.423 -10.610  -0.748  0.47 15.17           C  
ANISOU  341  C  BLEU A  39     2436   1750   1579   -361   -652    196       C  
ATOM    342  O  ALEU A  39      44.232 -11.250   0.251  0.53 19.14           O  
ANISOU  342  O  ALEU A  39     3005   2694   1573   -119   -476    984       O  
ATOM    343  O  BLEU A  39      43.821 -11.011   0.230  0.47 17.74           O  
ANISOU  343  O  BLEU A  39     2545   2639   1556   -458   -366    -65       O  
ATOM    344  CB ALEU A  39      44.552  -8.289   0.135  0.53 18.16           C  
ANISOU  344  CB ALEU A  39     3988   1719   1192   -271   -827    -83       C  
ATOM    345  CB BLEU A  39      45.124  -8.453   0.385  0.47 19.21           C  
ANISOU  345  CB BLEU A  39     3474   2142   1683   -415   -916   -231       C  
ATOM    346  CG ALEU A  39      45.299  -7.041   0.601  0.53 19.15           C  
ANISOU  346  CG ALEU A  39     3191   2473   1614   -809    -26   -487       C  
ATOM    347  CG BLEU A  39      46.082  -7.269   0.493  0.47 20.27           C  
ANISOU  347  CG BLEU A  39     3413   2490   1798   -597   -743   -691       C  
ATOM    348  CD1ALEU A  39      44.377  -5.968   1.169  0.53 20.90           C  
ANISOU  348  CD1ALEU A  39     4673   1809   1458   -481    -16   -270       C  
ATOM    349  CD1BLEU A  39      45.413  -6.124   1.241  0.47 20.56           C  
ANISOU  349  CD1BLEU A  39     3664   1992   2155   -574   -227   -145       C  
ATOM    350  CD2ALEU A  39      46.317  -7.478   1.651  0.53 26.65           C  
ANISOU  350  CD2ALEU A  39     4239   3530   2357   -157  -1145  -1407       C  
ATOM    351  CD2BLEU A  39      47.382  -7.707   1.158  0.47 22.49           C  
ANISOU  351  CD2BLEU A  39     3575   2210   2760   -512  -1033   -605       C  
ATOM    352  N   GLY A  40      44.204 -11.115  -1.967  1.00 12.04           N  
ANISOU  352  N   GLY A  40     2007   1065   1502   -138   -459    344       N  
ATOM    353  CA  GLY A  40      43.453 -12.323  -2.149  1.00 12.21           C  
ANISOU  353  CA  GLY A  40     2014    922   1705     95   -357    285       C  
ATOM    354  C   GLY A  40      41.968 -12.180  -2.412  1.00 10.59           C  
ANISOU  354  C   GLY A  40     1914    668   1440   -171   -176    268       C  
ATOM    355  O   GLY A  40      41.243 -13.157  -2.329  1.00 12.30           O  
ANISOU  355  O   GLY A  40     2145    764   1765   -242    141    239       O  
ATOM    356  N   GLN A  41      41.539 -10.952  -2.757  1.00 10.43           N  
ANISOU  356  N   GLN A  41     1753    817   1394   -254   -560    264       N  
ATOM    357  CA  GLN A  41      40.122 -10.769  -3.117  1.00 10.24           C  
ANISOU  357  CA  GLN A  41     1600    988   1304   -353   -431    237       C  
ATOM    358  C   GLN A  41      40.076 -10.156  -4.496  1.00  8.24           C  
ANISOU  358  C   GLN A  41     1336    693   1102   -191   -191    105       C  
ATOM    359  O   GLN A  41      40.897  -9.260  -4.812  1.00  9.91           O  
ANISOU  359  O   GLN A  41     1558    897   1312   -302   -294    219       O  
ATOM    360  CB  GLN A  41      39.422  -9.912  -2.096  1.00 14.59           C  
ANISOU  360  CB  GLN A  41     2000   2517   1027   -260     39    103       C  
ATOM    361  CG  GLN A  41      37.914 -10.024  -2.204  1.00 14.86           C  
ANISOU  361  CG  GLN A  41     2037   1430   2181     80   -126     74       C  
ATOM    362  CD  GLN A  41      37.240  -9.317  -1.010  1.00 18.34           C  
ANISOU  362  CD  GLN A  41     2499   1301   3168   -351    849   -118       C  
ATOM    363  OE1 GLN A  41      37.747  -8.424  -0.429  1.00 19.79           O  
ANISOU  363  OE1 GLN A  41     2892   1926   2702   -149    478   -556       O  
ATOM    364  NE2 GLN A  41      36.123  -9.895  -0.602  1.00 25.29           N  
ANISOU  364  NE2 GLN A  41     2621   1981   5006   -230   1543   -351       N  
ATOM    365  N   ASN A  42      39.138 -10.564  -5.336  1.00  8.08           N  
ANISOU  365  N   ASN A  42     1374    655   1040   -114   -191     98       N  
ATOM    366  CA  ASN A  42      39.061 -10.138  -6.732  1.00  7.42           C  
ANISOU  366  CA  ASN A  42     1215    623    981   -114    -99    111       C  
ATOM    367  C   ASN A  42      37.691  -9.551  -6.984  1.00  7.86           C  
ANISOU  367  C   ASN A  42     1247    558   1183    -85   -219     69       C  
ATOM    368  O   ASN A  42      36.837 -10.148  -7.654  1.00  8.94           O  
ANISOU  368  O   ASN A  42     1307    747   1341   -129   -363     21       O  
ATOM    369  CB  ASN A  42      39.394 -11.271  -7.686  1.00  7.97           C  
ANISOU  369  CB  ASN A  42     1292    580   1156    -61   -214     31       C  
ATOM    370  CG  ASN A  42      40.852 -11.647  -7.563  1.00  8.06           C  
ANISOU  370  CG  ASN A  42     1274    544   1245   -154   -192    105       C  
ATOM    371  OD1 ASN A  42      41.264 -12.217  -6.537  1.00  8.84           O  
ANISOU  371  OD1 ASN A  42     1382    801   1176     10   -263    165       O  
ATOM    372  ND2 ASN A  42      41.650 -11.287  -8.557  1.00  8.06           N  
ANISOU  372  ND2 ASN A  42     1246    589   1226   -167   -127     56       N  
ATOM    373  N  APRO A  43      37.463  -8.342  -6.471  0.63  7.64           N  
ANISOU  373  N  APRO A  43     1224    498   1180   -117    -90    102       N  
ATOM    374  N  BPRO A  43      37.357  -8.412  -6.373  0.37  9.96           N  
ANISOU  374  N  BPRO A  43     1518    718   1547    100   -501   -181       N  
ATOM    375  CA APRO A  43      36.142  -7.719  -6.570  0.63  8.37           C  
ANISOU  375  CA APRO A  43     1256    508   1415    -92   -150    195       C  
ATOM    376  CA BPRO A  43      36.008  -7.850  -6.523  0.37  9.77           C  
ANISOU  376  CA BPRO A  43     1557    858   1298    210   -410   -203       C  
ATOM    377  C  APRO A  43      35.873  -7.352  -8.028  0.63  9.14           C  
ANISOU  377  C  APRO A  43     1362    840   1270    154   -190    -20       C  
ATOM    378  C  BPRO A  43      35.843  -7.388  -7.971  0.37  8.75           C  
ANISOU  378  C  BPRO A  43     1368    605   1351   -229   -313     38       C  
ATOM    379  O  APRO A  43      36.755  -7.035  -8.834  0.63  9.24           O  
ANISOU  379  O  APRO A  43     1521    762   1228    203   -253    248       O  
ATOM    380  O  BPRO A  43      36.823  -7.091  -8.663  0.37 13.07           O  
ANISOU  380  O  BPRO A  43     1732   1327   1907     97    362   -122       O  
ATOM    381  CB APRO A  43      36.273  -6.491  -5.676  0.63  8.22           C  
ANISOU  381  CB APRO A  43     1188    725   1212    -62   -181     65       C  
ATOM    382  CB BPRO A  43      35.980  -6.659  -5.571  0.37 10.65           C  
ANISOU  382  CB BPRO A  43     1445   1036   1567   -113   -319   -468       C  
ATOM    383  CG APRO A  43      37.736  -6.145  -5.756  0.63  9.18           C  
ANISOU  383  CG APRO A  43     1263    558   1668   -123   -232      3       C  
ATOM    384  CG BPRO A  43      37.206  -6.747  -4.726  0.37 10.55           C  
ANISOU  384  CG BPRO A  43     1564    848   1597   -243   -370   -275       C  
ATOM    385  CD APRO A  43      38.432  -7.484  -5.799  0.63  8.27           C  
ANISOU  385  CD APRO A  43     1235    624   1284   -136    -26   -141       C  
ATOM    386  CD BPRO A  43      38.192  -7.576  -5.510  0.37  9.88           C  
ANISOU  386  CD BPRO A  43     1441    778   1533   -230   -332   -102       C  
ATOM    387  N   THR A  44      34.572  -7.297  -8.349  1.00  9.89           N  
ANISOU  387  N   THR A  44     1541    618   1599    -61   -458      6       N  
ATOM    388  CA  THR A  44      34.194  -6.809  -9.657  1.00  9.95           C  
ANISOU  388  CA  THR A  44     1598    728   1452    -45   -434     12       C  
ATOM    389  C   THR A  44      34.203  -5.287  -9.677  1.00 10.18           C  
ANISOU  389  C   THR A  44     1686    714   1468     21   -466    -20       C  
ATOM    390  O   THR A  44      34.267  -4.600  -8.661  1.00  9.39           O  
ANISOU  390  O   THR A  44     1413    690   1465    -18   -361    -12       O  
ATOM    391  CB  THR A  44      32.780  -7.293 -10.004  1.00 11.86           C  
ANISOU  391  CB  THR A  44     1652    837   2016     24   -632    -24       C  
ATOM    392  OG1 THR A  44      31.885  -6.664  -9.073  1.00 11.69           O  
ANISOU  392  OG1 THR A  44     1472    876   2093    -88   -529    269       O  
ATOM    393  CG2 THR A  44      32.700  -8.800  -9.937  1.00 12.33           C  
ANISOU  393  CG2 THR A  44     2241    756   1688   -234   -549     85       C  
ATOM    394  N   GLU A  45      34.106  -4.735 -10.884  1.00 11.19           N  
ANISOU  394  N   GLU A  45     2050    808   1393    117   -487      5       N  
ATOM    395  CA  GLU A  45      34.024  -3.296 -11.046  1.00 10.91           C  
ANISOU  395  CA  GLU A  45     1825    722   1598    102   -378     50       C  
ATOM    396  C   GLU A  45      32.859  -2.710 -10.254  1.00 10.24           C  
ANISOU  396  C   GLU A  45     1509    693   1690     47   -516    138       C  
ATOM    397  O   GLU A  45      32.985  -1.663  -9.641  1.00 10.21           O  
ANISOU  397  O   GLU A  45     1540    692   1647      7   -309     70       O  
ATOM    398  CB  GLU A  45      33.982  -2.896 -12.524  1.00 13.87           C  
ANISOU  398  CB  GLU A  45     2390   1214   1664    -25   -269    340       C  
ATOM    399  CG  GLU A  45      34.012  -1.377 -12.677  1.00 15.02           C  
ANISOU  399  CG  GLU A  45     2616   1217   1875   -145   -112    397       C  
ATOM    400  CD  GLU A  45      35.293  -0.664 -12.345  1.00 18.42           C  
ANISOU  400  CD  GLU A  45     2525   1378   3094   -142   -531    782       C  
ATOM    401  OE1 GLU A  45      36.325  -1.270 -12.129  1.00 22.57           O  
ANISOU  401  OE1 GLU A  45     2353   2203   4019    300    228    956       O  
ATOM    402  OE2 GLU A  45      35.291   0.598 -12.275  1.00 19.02           O  
ANISOU  402  OE2 GLU A  45     3064   1469   2693   -277   -375    274       O  
ATOM    403  N   ALA A  46      31.689  -3.401 -10.257  1.00 11.49           N  
ANISOU  403  N   ALA A  46     1573    834   1958    -33   -736    111       N  
ATOM    404  CA  ALA A  46      30.532  -2.900  -9.503  1.00 11.63           C  
ANISOU  404  CA  ALA A  46     1305    950   2165    -35   -671    323       C  
ATOM    405  C   ALA A  46      30.806  -2.833  -8.006  1.00 10.38           C  
ANISOU  405  C   ALA A  46     1125    640   2177     44   -484    216       C  
ATOM    406  O   ALA A  46      30.468  -1.860  -7.337  1.00 11.14           O  
ANISOU  406  O   ALA A  46     1090    656   2485    114   -404    173       O  
ATOM    407  CB  ALA A  46      29.299  -3.751  -9.824  1.00 13.84           C  
ANISOU  407  CB  ALA A  46     1641   1094   2522   -181   -813     63       C  
ATOM    408  N   GLU A  47      31.461  -3.847  -7.473  1.00  9.97           N  
ANISOU  408  N   GLU A  47     1158    573   2056   -127   -544    202       N  
ATOM    409  CA  GLU A  47      31.804  -3.861  -6.070  1.00  9.34           C  
ANISOU  409  CA  GLU A  47     1287    562   1699    -96   -321    209       C  
ATOM    410  C   GLU A  47      32.816  -2.752  -5.754  1.00  9.06           C  
ANISOU  410  C   GLU A  47     1253    689   1500    -71   -261    169       C  
ATOM    411  O   GLU A  47      32.706  -2.078  -4.725  1.00  9.24           O  
ANISOU  411  O   GLU A  47     1184    723   1601    -50   -162     61       O  
ATOM    412  CB  GLU A  47      32.423  -5.228  -5.694  1.00  9.14           C  
ANISOU  412  CB  GLU A  47      992    670   1809    -74   -196    198       C  
ATOM    413  CG  GLU A  47      31.378  -6.339  -5.686  1.00 10.97           C  
ANISOU  413  CG  GLU A  47     1166    666   2334   -162   -372    343       C  
ATOM    414  CD  GLU A  47      31.918  -7.724  -5.482  1.00 10.63           C  
ANISOU  414  CD  GLU A  47     1193    623   2222   -156   -184     33       C  
ATOM    415  OE1 GLU A  47      32.996  -8.036  -6.051  1.00 10.34           O  
ANISOU  415  OE1 GLU A  47     1286    671   1972    -47   -295    180       O  
ATOM    416  OE2 GLU A  47      31.201  -8.553  -4.889  1.00 15.87           O  
ANISOU  416  OE2 GLU A  47     1700    871   3460    104    532    656       O  
ATOM    417  N   LEU A  48      33.809  -2.554  -6.615  1.00  8.44           N  
ANISOU  417  N   LEU A  48     1076    597   1536    -39   -328    -53       N  
ATOM    418  CA  LEU A  48      34.792  -1.522  -6.399  1.00  8.88           C  
ANISOU  418  CA  LEU A  48     1167    514   1693   -121   -281     37       C  
ATOM    419  C   LEU A  48      34.136  -0.133  -6.430  1.00  8.80           C  
ANISOU  419  C   LEU A  48     1105    581   1656    -92   -289     60       C  
ATOM    420  O   LEU A  48      34.505   0.753  -5.658  1.00  9.21           O  
ANISOU  420  O   LEU A  48     1152    571   1776    -88   -271    -44       O  
ATOM    421  CB  LEU A  48      35.877  -1.639  -7.439  1.00  9.43           C  
ANISOU  421  CB  LEU A  48     1207    602   1774   -106   -293    -68       C  
ATOM    422  CG  LEU A  48      36.815  -2.845  -7.295  1.00  9.53           C  
ANISOU  422  CG  LEU A  48     1271    615   1734    -82   -242    -72       C  
ATOM    423  CD1 LEU A  48      37.596  -3.125  -8.547  1.00 10.64           C  
ANISOU  423  CD1 LEU A  48     1225    868   1949   -112   -222   -232       C  
ATOM    424  CD2 LEU A  48      37.710  -2.653  -6.085  1.00 12.06           C  
ANISOU  424  CD2 LEU A  48     1555   1195   1834     90   -404    -44       C  
ATOM    425  N   GLN A  49      33.192   0.058  -7.343  1.00  9.18           N  
ANISOU  425  N   GLN A  49     1163    480   1847     -5   -382    -64       N  
ATOM    426  CA  GLN A  49      32.508   1.341  -7.432  1.00  9.62           C  
ANISOU  426  CA  GLN A  49     1182    616   1858     90   -184     68       C  
ATOM    427  C   GLN A  49      31.743   1.654  -6.195  1.00  9.16           C  
ANISOU  427  C   GLN A  49     1049    629   1804    -23   -230    131       C  
ATOM    428  O   GLN A  49      31.718   2.819  -5.734  1.00  9.49           O  
ANISOU  428  O   GLN A  49     1287    577   1741     14   -240     38       O  
ATOM    429  CB  GLN A  49      31.633   1.364  -8.706  1.00 10.38           C  
ANISOU  429  CB  GLN A  49     1322    860   1762    209   -181    155       C  
ATOM    430  CG  GLN A  49      31.076   2.760  -8.971  1.00 11.87           C  
ANISOU  430  CG  GLN A  49     1843   1041   1627    489     32    301       C  
ATOM    431  CD  GLN A  49      32.182   3.712  -9.319  1.00 16.01           C  
ANISOU  431  CD  GLN A  49     2386   1098   2600    564    842    678       C  
ATOM    432  OE1 GLN A  49      32.403   4.758  -8.681  1.00 17.54           O  
ANISOU  432  OE1 GLN A  49     2057   1291   3316     77     66    666       O  
ATOM    433  NE2 GLN A  49      32.885   3.455 -10.382  1.00 22.80           N  
ANISOU  433  NE2 GLN A  49     3615   1701   3345   1165   1951   1347       N  
ATOM    434  N   ASP A  50      31.080   0.663  -5.615  1.00  9.52           N  
ANISOU  434  N   ASP A  50     1192    634   1790   -101   -287     74       N  
ATOM    435  CA  ASP A  50      30.364   0.892  -4.370  1.00 10.37           C  
ANISOU  435  CA  ASP A  50     1196    824   1921    -71   -128    136       C  
ATOM    436  C   ASP A  50      31.347   1.297  -3.290  1.00 10.69           C  
ANISOU  436  C   ASP A  50     1438    959   1666    -76    -87    197       C  
ATOM    437  O   ASP A  50      31.034   2.182  -2.484  1.00 11.16           O  
ANISOU  437  O   ASP A  50     1425   1192   1624    -88      9    208       O  
ATOM    438  CB  ASP A  50      29.587  -0.327  -3.948  1.00 11.57           C  
ANISOU  438  CB  ASP A  50     1181   1028   2186    -91      5    156       C  
ATOM    439  CG  ASP A  50      28.287  -0.528  -4.671  1.00 13.93           C  
ANISOU  439  CG  ASP A  50     1306   1177   2810   -284   -116     96       C  
ATOM    440  OD1 ASP A  50      27.784   0.387  -5.322  1.00 14.25           O  
ANISOU  440  OD1 ASP A  50     1282   1420   2711    305   -173    -86       O  
ATOM    441  OD2 ASP A  50      27.759  -1.666  -4.571  1.00 16.94           O  
ANISOU  441  OD2 ASP A  50     1518   1568   3352   -512   -223    208       O  
ATOM    442  N   MET A  51      32.512   0.661  -3.226  1.00 10.31           N  
ANISOU  442  N   MET A  51     1330    963   1623   -141   -261    308       N  
ATOM    443  CA  MET A  51      33.489   1.018  -2.206  1.00 10.93           C  
ANISOU  443  CA  MET A  51     1596    962   1595    -44   -317    248       C  
ATOM    444  C   MET A  51      33.957   2.444  -2.385  1.00 10.67           C  
ANISOU  444  C   MET A  51     1601    905   1547     -1   -419    167       C  
ATOM    445  O   MET A  51      34.062   3.206  -1.390  1.00 12.53           O  
ANISOU  445  O   MET A  51     1961   1096   1704      0   -326    -85       O  
ATOM    446  CB  MET A  51      34.687   0.051  -2.252  1.00 10.90           C  
ANISOU  446  CB  MET A  51     1544    927   1670    -29   -320    292       C  
ATOM    447  CG  MET A  51      34.349  -1.383  -1.879  1.00 12.65           C  
ANISOU  447  CG  MET A  51     1880    954   1973    -62   -551    268       C  
ATOM    448  SD  MET A  51      35.692  -2.528  -2.020  1.00 15.60           S  
ANISOU  448  SD  MET A  51     2216    983   2727    181   -621    366       S  
ATOM    449  CE  MET A  51      36.658  -2.067  -0.588  1.00 20.70           C  
ANISOU  449  CE  MET A  51     2317   2188   3359   -133  -1206    538       C  
ATOM    450  N  AILE A  52      34.269   2.924  -3.574  0.52  9.30           N  
ANISOU  450  N  AILE A  52     1012    873   1648   -350   -524    136       N  
ATOM    451  N  BILE A  52      34.273   2.797  -3.619  0.48  9.90           N  
ANISOU  451  N  BILE A  52     1606    453   1701     88   -187     54       N  
ATOM    452  CA AILE A  52      34.702   4.316  -3.822  0.52  9.63           C  
ANISOU  452  CA AILE A  52     1268    742   1650   -307   -359     -8       C  
ATOM    453  CA BILE A  52      34.667   4.198  -3.912  0.48  9.34           C  
ANISOU  453  CA BILE A  52     1416    411   1722      5   -529    -28       C  
ATOM    454  C  AILE A  52      33.544   5.238  -3.514  0.52  9.56           C  
ANISOU  454  C  AILE A  52     1363    743   1528   -323    -88    214       C  
ATOM    455  C  BILE A  52      33.573   5.185  -3.569  0.48  9.48           C  
ANISOU  455  C  BILE A  52     1471    382   1747    -78   -342     79       C  
ATOM    456  O  AILE A  52      33.655   6.281  -2.865  0.52 12.36           O  
ANISOU  456  O  AILE A  52     1636   1417   1642     82   -420   -444       O  
ATOM    457  O  BILE A  52      33.871   6.232  -2.950  0.48  9.57           O  
ANISOU  457  O  BILE A  52     1809    321   1508   -109    -86    104       O  
ATOM    458  CB AILE A  52      35.245   4.446  -5.254  0.52  9.07           C  
ANISOU  458  CB AILE A  52     1311    447   1688   -133   -245   -144       C  
ATOM    459  CB BILE A  52      35.118   4.297  -5.382  0.48 10.26           C  
ANISOU  459  CB BILE A  52     1199    725   1976   -186   -204     95       C  
ATOM    460  CG1AILE A  52      36.490   3.596  -5.578  0.52 11.72           C  
ANISOU  460  CG1AILE A  52     1136    602   2714   -141     45     72       C  
ATOM    461  CG1BILE A  52      36.406   3.460  -5.519  0.48 15.19           C  
ANISOU  461  CG1BILE A  52     1515   1345   2910    179    209    180       C  
ATOM    462  CG2AILE A  52      35.464   5.933  -5.570  0.52  9.32           C  
ANISOU  462  CG2AILE A  52     1346    545   1650    -25      1   -106       C  
ATOM    463  CG2BILE A  52      35.225   5.730  -5.880  0.48 11.38           C  
ANISOU  463  CG2BILE A  52     1990    680   1654   -321   -246   -113       C  
ATOM    464  CD1AILE A  52      37.727   3.880  -4.815  0.52 14.61           C  
ANISOU  464  CD1AILE A  52     1519    458   3572   -168   -614    262       C  
ATOM    465  CD1BILE A  52      37.675   4.193  -5.373  0.48 17.44           C  
ANISOU  465  CD1BILE A  52     1301   1399   3927    211    531    451       C  
ATOM    466  N   ASN A  53      32.326   4.884  -3.952  1.00  9.60           N  
ANISOU  466  N   ASN A  53     1298    669   1680    -89     52    -96       N  
ATOM    467  CA  ASN A  53      31.204   5.787  -3.722  1.00 10.19           C  
ANISOU  467  CA  ASN A  53     1490    731   1652     37    106    -36       C  
ATOM    468  C   ASN A  53      30.979   6.063  -2.257  1.00 11.56           C  
ANISOU  468  C   ASN A  53     1506   1173   1713     68    147   -161       C  
ATOM    469  O   ASN A  53      30.532   7.158  -1.907  1.00 12.03           O  
ANISOU  469  O   ASN A  53     1626   1203   1741    201    169   -133       O  
ATOM    470  CB  ASN A  53      29.925   5.245  -4.345  1.00 11.24           C  
ANISOU  470  CB  ASN A  53     1345   1042   1882     36    192    -46       C  
ATOM    471  CG  ASN A  53      29.854   5.298  -5.847  1.00 10.22           C  
ANISOU  471  CG  ASN A  53     1291    773   1819    150     69    -46       C  
ATOM    472  OD1 ASN A  53      28.868   4.704  -6.405  1.00 14.13           O  
ANISOU  472  OD1 ASN A  53     1461   1562   2347    135   -113   -285       O  
ATOM    473  ND2 ASN A  53      30.780   5.883  -6.500  1.00  9.88           N  
ANISOU  473  ND2 ASN A  53     1708    706   1341     65    -94    -13       N  
ATOM    474  N   GLU A  54      31.267   5.106  -1.386  1.00 14.78           N  
ANISOU  474  N   GLU A  54     2779   1056   1780      3    556    103       N  
ATOM    475  CA  GLU A  54      31.153   5.347   0.058  1.00 17.10           C  
ANISOU  475  CA  GLU A  54     3281   1452   1763   -157    739    238       C  
ATOM    476  C   GLU A  54      32.100   6.390   0.620  1.00 17.45           C  
ANISOU  476  C   GLU A  54     3701   1436   1493    -77    158    223       C  
ATOM    477  O   GLU A  54      31.804   6.920   1.721  1.00 23.28           O  
ANISOU  477  O   GLU A  54     5280   1852   1715   -300    705    -91       O  
ATOM    478  CB  GLU A  54      31.378   4.019   0.816  1.00 22.44           C  
ANISOU  478  CB  GLU A  54     4971   1459   2098   -153   1313    510       C  
ATOM    479  CG  GLU A  54      30.444   2.959   0.470  1.00 23.76           C  
ANISOU  479  CG  GLU A  54     3779   1821   3427   -122   1533    838       C  
ATOM    480  CD  GLU A  54      29.067   3.203  -0.048  1.00 34.26           C  
ANISOU  480  CD  GLU A  54     4297   5043   3677    499    840    157       C  
ATOM    481  OE1 GLU A  54      28.328   3.516   0.907  1.00 33.61           O  
ANISOU  481  OE1 GLU A  54     4235   5245   3290   2106    751   1802       O  
ATOM    482  OE2 GLU A  54      28.926   3.037  -1.303  1.00 46.97           O  
ANISOU  482  OE2 GLU A  54     5939   8299   3607   2642    593    188       O  
ATOM    483  N  AVAL A  55      33.214   6.624  -0.055  0.44 14.25           N  
ANISOU  483  N  AVAL A  55     2568    901   1945    548   -386    109       N  
ATOM    484  N  BVAL A  55      33.142   6.754  -0.095  0.56 14.38           N  
ANISOU  484  N  BVAL A  55     2852   1324   1289      4   -509      0       N  
ATOM    485  CA AVAL A  55      34.359   7.427   0.344  0.44 15.60           C  
ANISOU  485  CA AVAL A  55     2728   1437   1762    590   -870    -74       C  
ATOM    486  CA BVAL A  55      34.178   7.613   0.500  0.56 15.76           C  
ANISOU  486  CA BVAL A  55     3372    830   1787    169   -863   -219       C  
ATOM    487  C  AVAL A  55      34.396   8.791  -0.350  0.44 15.69           C  
ANISOU  487  C  AVAL A  55     2786   1582   1595   -211   -676    -61       C  
ATOM    488  C  BVAL A  55      34.516   8.800  -0.382  0.56 12.87           C  
ANISOU  488  C  BVAL A  55     2350    710   1832    492   -873   -183       C  
ATOM    489  O  AVAL A  55      34.767   9.793   0.294  0.44  9.59           O  
ANISOU  489  O  AVAL A  55     1103   1534   1005    466    105   -361       O  
ATOM    490  O  BVAL A  55      35.243   9.747  -0.036  0.56 10.18           O  
ANISOU  490  O  BVAL A  55     1250   1239   1380    336    -20   -432       O  
ATOM    491  CB AVAL A  55      35.722   6.680   0.143  0.44 14.02           C  
ANISOU  491  CB AVAL A  55     2318   2465    545    248    576    702       C  
ATOM    492  CB BVAL A  55      35.375   6.670   0.806  0.56 18.78           C  
ANISOU  492  CB BVAL A  55     3918   1110   2106    204  -2125    205       C  
ATOM    493  CG1AVAL A  55      36.858   7.533   0.712  0.44 13.81           C  
ANISOU  493  CG1AVAL A  55     2095   1172   1980    489    962    609       C  
ATOM    494  CG1BVAL A  55      36.670   7.419   1.113  0.56 19.46           C  
ANISOU  494  CG1BVAL A  55     3031   3614    748   -437   -229    304       C  
ATOM    495  CG2AVAL A  55      35.670   5.366   0.860  0.44 12.15           C  
ANISOU  495  CG2AVAL A  55     1973   1107   1537    297   -243   -341       C  
ATOM    496  CG2BVAL A  55      35.012   5.715   1.953  0.56 21.35           C  
ANISOU  496  CG2BVAL A  55     3856   1044   3214   -586  -1879    404       C  
ATOM    497  N   ASP A  56      34.005   8.834  -1.615  1.00 17.25           N  
ANISOU  497  N   ASP A  56     3858    900   1794   -149  -1161    -70       N  
ATOM    498  CA  ASP A  56      34.204   9.907  -2.558  1.00 15.46           C  
ANISOU  498  CA  ASP A  56     3448    507   1920    147  -1108    -55       C  
ATOM    499  C   ASP A  56      33.243  11.039  -2.338  1.00 12.45           C  
ANISOU  499  C   ASP A  56     1987    907   1836   -411   -561    189       C  
ATOM    500  O   ASP A  56      32.173  11.151  -2.957  1.00 15.88           O  
ANISOU  500  O   ASP A  56     2173   1558   2303   -605   -874    225       O  
ATOM    501  CB  ASP A  56      34.072   9.349  -3.985  1.00 16.84           C  
ANISOU  501  CB  ASP A  56     3815    726   1859    -50  -1180     32       C  
ATOM    502  CG  ASP A  56      34.135  10.417  -5.068  1.00 12.12           C  
ANISOU  502  CG  ASP A  56     1958    696   1952      7   -689    106       C  
ATOM    503  OD1 ASP A  56      34.725  11.455  -4.805  1.00 11.25           O  
ANISOU  503  OD1 ASP A  56     1409    777   2088    114   -504   -259       O  
ATOM    504  OD2 ASP A  56      33.553  10.124  -6.139  1.00 13.16           O  
ANISOU  504  OD2 ASP A  56     2268    887   1844   -136   -893    117       O  
ATOM    505  N   ALA A  57      33.590  11.959  -1.458  1.00 12.46           N  
ANISOU  505  N   ALA A  57     1615    873   2247   -115   -397   -137       N  
ATOM    506  CA  ALA A  57      32.721  13.009  -1.023  1.00 13.59           C  
ANISOU  506  CA  ALA A  57     1703   1140   2322    -90   -194     25       C  
ATOM    507  C   ALA A  57      32.321  13.972  -2.148  1.00 12.49           C  
ANISOU  507  C   ALA A  57     1309    893   2544    -60   -126    138       C  
ATOM    508  O   ALA A  57      31.155  14.491  -2.043  1.00 16.56           O  
ANISOU  508  O   ALA A  57     1468   1865   2961    272     17    128       O  
ATOM    509  CB  ALA A  57      33.315  13.755   0.183  1.00 14.84           C  
ANISOU  509  CB  ALA A  57     1924   1411   2304    113    -28   -345       C  
ATOM    510  N   ASP A  58      33.167  14.296  -3.085  1.00 12.82           N  
ANISOU  510  N   ASP A  58     1339    968   2565   -105   -149    114       N  
ATOM    511  CA  ASP A  58      32.787  15.300  -4.096  1.00 12.17           C  
ANISOU  511  CA  ASP A  58     1060   1061   2505    229   -135    178       C  
ATOM    512  C   ASP A  58      32.242  14.620  -5.352  1.00 14.17           C  
ANISOU  512  C   ASP A  58     1150   1158   3077     -4   -616    242       C  
ATOM    513  O   ASP A  58      31.861  15.310  -6.284  1.00 15.93           O  
ANISOU  513  O   ASP A  58     1843   1338   2869    380   -846    137       O  
ATOM    514  CB  ASP A  58      33.922  16.255  -4.425  1.00 12.14           C  
ANISOU  514  CB  ASP A  58     1338    691   2583     41   -249     12       C  
ATOM    515  CG  ASP A  58      35.182  15.636  -4.962  1.00 10.58           C  
ANISOU  515  CG  ASP A  58     1145    569   2305     32   -381    383       C  
ATOM    516  OD1 ASP A  58      35.152  14.395  -5.178  1.00 10.30           O  
ANISOU  516  OD1 ASP A  58     1539    589   1784     66   -592      8       O  
ATOM    517  OD2 ASP A  58      36.145  16.393  -5.209  1.00 10.39           O  
ANISOU  517  OD2 ASP A  58     1344    613   1990    -42   -331    119       O  
ATOM    518  N   GLY A  59      32.173  13.282  -5.408  1.00 14.69           N  
ANISOU  518  N   GLY A  59     1650   1093   2840   -146   -542    196       N  
ATOM    519  CA  GLY A  59      31.512  12.626  -6.522  1.00 16.07           C  
ANISOU  519  CA  GLY A  59     1370   1507   3227      9  -1054     69       C  
ATOM    520  C   GLY A  59      32.329  12.708  -7.800  1.00 14.80           C  
ANISOU  520  C   GLY A  59     1671    967   2986    -86  -1048    -69       C  
ATOM    521  O   GLY A  59      31.713  12.494  -8.863  1.00 17.34           O  
ANISOU  521  O   GLY A  59     1704   1767   3117    -24  -1257    -28       O  
ATOM    522  N   ASN A  60      33.616  12.979  -7.798  1.00 13.93           N  
ANISOU  522  N   ASN A  60     1659    834   2802   -267  -1189    490       N  
ATOM    523  CA  ASN A  60      34.395  13.043  -9.011  1.00 15.63           C  
ANISOU  523  CA  ASN A  60     2002   1308   2628   -657  -1259    934       C  
ATOM    524  C   ASN A  60      34.849  11.676  -9.428  1.00 14.22           C  
ANISOU  524  C   ASN A  60     1600   1593   2211   -584   -943    621       C  
ATOM    525  O   ASN A  60      35.497  11.598 -10.498  1.00 17.75           O  
ANISOU  525  O   ASN A  60     1912   2630   2204   -807   -790    827       O  
ATOM    526  CB  ASN A  60      35.533  14.043  -8.916  1.00 15.69           C  
ANISOU  526  CB  ASN A  60     1963   1471   2526   -642  -1392    841       C  
ATOM    527  CG  ASN A  60      36.616  13.666  -7.960  1.00  9.01           C  
ANISOU  527  CG  ASN A  60     1299    785   1338    -38   -428    148       C  
ATOM    528  OD1 ASN A  60      36.522  12.667  -7.198  1.00  9.98           O  
ANISOU  528  OD1 ASN A  60     1413    728   1652   -110   -553    258       O  
ATOM    529  ND2 ASN A  60      37.638  14.489  -7.969  1.00 10.09           N  
ANISOU  529  ND2 ASN A  60     1264    938   1632   -207   -479    415       N  
ATOM    530  N   GLY A  61      34.535  10.599  -8.680  1.00 11.70           N  
ANISOU  530  N   GLY A  61     1400   1140   1905   -301   -754    301       N  
ATOM    531  CA  GLY A  61      34.841   9.258  -9.131  1.00 11.82           C  
ANISOU  531  CA  GLY A  61     1274   1379   1839   -265   -569    116       C  
ATOM    532  C   GLY A  61      36.078   8.633  -8.527  1.00  9.90           C  
ANISOU  532  C   GLY A  61     1174   1228   1359   -266   -315      7       C  
ATOM    533  O   GLY A  61      36.330   7.471  -8.747  1.00 11.11           O  
ANISOU  533  O   GLY A  61     1345   1142   1735   -325   -397    -87       O  
ATOM    534  N   THR A  62      36.865   9.455  -7.805  1.00  9.11           N  
ANISOU  534  N   THR A  62     1140    960   1361   -201   -414    131       N  
ATOM    535  CA  THR A  62      38.110   8.977  -7.198  1.00  8.43           C  
ANISOU  535  CA  THR A  62     1154    862   1188   -151   -296    161       C  
ATOM    536  C   THR A  62      38.230   9.489  -5.779  1.00  7.85           C  
ANISOU  536  C   THR A  62     1140    612   1229    -38   -299    175       C  
ATOM    537  O   THR A  62      37.498  10.387  -5.389  1.00  8.59           O  
ANISOU  537  O   THR A  62     1234    817   1214     71   -299    163       O  
ATOM    538  CB  THR A  62      39.328   9.369  -8.034  1.00  8.31           C  
ANISOU  538  CB  THR A  62     1223    845   1091   -281   -324    111       C  
ATOM    539  OG1 THR A  62      39.438  10.810  -7.955  1.00  8.31           O  
ANISOU  539  OG1 THR A  62     1202    768   1186   -149   -199     25       O  
ATOM    540  CG2 THR A  62      39.275   8.884  -9.459  1.00  9.30           C  
ANISOU  540  CG2 THR A  62     1414    951   1167   -172   -163     -9       C  
ATOM    541  N   ILE A  63      39.124   8.894  -5.001  1.00  7.76           N  
ANISOU  541  N   ILE A  63     1180    709   1058    -68   -229    101       N  
ATOM    542  CA  ILE A  63      39.366   9.286  -3.619  1.00  7.21           C  
ANISOU  542  CA  ILE A  63     1053    569   1116    -22   -219     95       C  
ATOM    543  C   ILE A  63      40.680  10.068  -3.542  1.00  7.24           C  
ANISOU  543  C   ILE A  63     1109    570   1073    -42   -166    204       C  
ATOM    544  O   ILE A  63      41.724   9.562  -3.960  1.00  8.41           O  
ANISOU  544  O   ILE A  63     1096    742   1357   -141   -173    102       O  
ATOM    545  CB  ILE A  63      39.455   8.058  -2.709  1.00  8.03           C  
ANISOU  545  CB  ILE A  63     1213    680   1158   -106   -156    247       C  
ATOM    546  CG1 ILE A  63      38.219   7.169  -2.781  1.00  9.46           C  
ANISOU  546  CG1 ILE A  63     1362    848   1384   -263    -97    173       C  
ATOM    547  CG2 ILE A  63      39.756   8.477  -1.283  1.00  9.19           C  
ANISOU  547  CG2 ILE A  63     1535    822   1135   -174   -224    228       C  
ATOM    548  CD1 ILE A  63      38.439   5.778  -2.148  1.00 15.25           C  
ANISOU  548  CD1 ILE A  63     2459    926   2408   -392   -106    367       C  
ATOM    549  N   ASP A  64      40.625  11.283  -3.005  1.00  7.71           N  
ANISOU  549  N   ASP A  64     1154    673   1100   -132   -236    224       N  
ATOM    550  CA  ASP A  64      41.840  12.071  -2.809  1.00  7.73           C  
ANISOU  550  CA  ASP A  64     1284    704    949   -165   -197    182       C  
ATOM    551  C   ASP A  64      42.294  11.964  -1.356  1.00  7.85           C  
ANISOU  551  C   ASP A  64     1308    698    978   -200   -260    246       C  
ATOM    552  O   ASP A  64      41.684  11.287  -0.519  1.00  7.94           O  
ANISOU  552  O   ASP A  64     1241    776    999   -212   -173    280       O  
ATOM    553  CB  ASP A  64      41.623  13.526  -3.250  1.00  8.77           C  
ANISOU  553  CB  ASP A  64     1625    676   1030   -301   -287    255       C  
ATOM    554  CG  ASP A  64      40.617  14.269  -2.468  1.00  9.08           C  
ANISOU  554  CG  ASP A  64     1705    582   1163   -153   -440    250       C  
ATOM    555  OD1 ASP A  64      40.310  13.864  -1.340  1.00 10.12           O  
ANISOU  555  OD1 ASP A  64     1917    739   1189    -57   -275    212       O  
ATOM    556  OD2 ASP A  64      40.151  15.308  -2.978  1.00 11.34           O  
ANISOU  556  OD2 ASP A  64     2141    676   1493    -73   -330    293       O  
ATOM    557  N   PHE A  65      43.455  12.584  -1.079  1.00  8.91           N  
ANISOU  557  N   PHE A  65     1418    962   1004   -464   -323    398       N  
ATOM    558  CA  PHE A  65      44.018  12.419   0.278  1.00  9.05           C  
ANISOU  558  CA  PHE A  65     1306   1089   1043   -409   -343    312       C  
ATOM    559  C   PHE A  65      43.115  12.983   1.337  1.00  9.19           C  
ANISOU  559  C   PHE A  65     1456    905   1131   -394   -304    344       C  
ATOM    560  O   PHE A  65      42.893  12.306   2.353  1.00  9.70           O  
ANISOU  560  O   PHE A  65     1469   1098   1119   -315   -244    350       O  
ATOM    561  CB  PHE A  65      45.458  12.975   0.279  1.00 11.01           C  
ANISOU  561  CB  PHE A  65     1466   1632   1085   -661   -259    473       C  
ATOM    562  CG  PHE A  65      46.075  12.788   1.656  1.00 10.76           C  
ANISOU  562  CG  PHE A  65     1300   1810    979   -660   -212    287       C  
ATOM    563  CD1 PHE A  65      46.267  11.529   2.155  1.00 10.29           C  
ANISOU  563  CD1 PHE A  65     1245   1747    918    -43    -76    120       C  
ATOM    564  CD2 PHE A  65      46.438  13.875   2.420  1.00 14.84           C  
ANISOU  564  CD2 PHE A  65     2515   1827   1297  -1014   -548    292       C  
ATOM    565  CE1 PHE A  65      46.864  11.320   3.415  1.00 12.17           C  
ANISOU  565  CE1 PHE A  65     1512   2070   1042     83   -245     39       C  
ATOM    566  CE2 PHE A  65      47.066  13.693   3.644  1.00 16.76           C  
ANISOU  566  CE2 PHE A  65     2924   2217   1228   -949   -580     97       C  
ATOM    567  CZ  PHE A  65      47.305  12.426   4.103  1.00 15.22           C  
ANISOU  567  CZ  PHE A  65     2335   2472    977   -250   -476    -16       C  
ATOM    568  N   PRO A  66      42.545  14.197   1.220  1.00 10.73           N  
ANISOU  568  N   PRO A  66     1925    880   1271   -400   -336    177       N  
ATOM    569  CA  PRO A  66      41.582  14.635   2.221  1.00 11.62           C  
ANISOU  569  CA  PRO A  66     1896    916   1605    -74   -453    -33       C  
ATOM    570  C   PRO A  66      40.412  13.679   2.475  1.00  9.86           C  
ANISOU  570  C   PRO A  66     1698    946   1103     97   -358     38       C  
ATOM    571  O   PRO A  66      39.979  13.435   3.617  1.00 10.97           O  
ANISOU  571  O   PRO A  66     1864   1110   1195     41   -292    -45       O  
ATOM    572  CB  PRO A  66      41.105  16.015   1.748  1.00 16.58           C  
ANISOU  572  CB  PRO A  66     2826    807   2667    -60   -587     88       C  
ATOM    573  CG  PRO A  66      42.156  16.448   0.851  1.00 18.23           C  
ANISOU  573  CG  PRO A  66     3831   1200   1895    114   -452    466       C  
ATOM    574  CD  PRO A  66      42.806  15.258   0.250  1.00 12.69           C  
ANISOU  574  CD  PRO A  66     2474    733   1616   -569   -716    467       C  
ATOM    575  N   GLU A  67      39.864  13.126   1.396  1.00  8.85           N  
ANISOU  575  N   GLU A  67     1500    743   1119     21   -234     72       N  
ATOM    576  CA  GLU A  67      38.763  12.166   1.543  1.00  9.06           C  
ANISOU  576  CA  GLU A  67     1453    915   1075     79   -205     36       C  
ATOM    577  C   GLU A  67      39.218  10.906   2.271  1.00  8.08           C  
ANISOU  577  C   GLU A  67     1244    882    943    -20    -64     84       C  
ATOM    578  O   GLU A  67      38.492  10.324   3.091  1.00  9.22           O  
ANISOU  578  O   GLU A  67     1224   1202   1078    -49    -58    204       O  
ATOM    579  CB  GLU A  67      38.209  11.798   0.132  1.00  8.30           C  
ANISOU  579  CB  GLU A  67     1262    772   1120     10   -224      8       C  
ATOM    580  CG  GLU A  67      37.403  12.941  -0.474  1.00  9.37           C  
ANISOU  580  CG  GLU A  67     1484    822   1253    214   -281    -49       C  
ATOM    581  CD  GLU A  67      37.087  12.757  -1.954  1.00  9.06           C  
ANISOU  581  CD  GLU A  67     1426    656   1361    156   -393    -52       C  
ATOM    582  OE1 GLU A  67      37.765  11.985  -2.645  1.00  8.97           O  
ANISOU  582  OE1 GLU A  67     1560    667   1179    101   -422      2       O  
ATOM    583  OE2 GLU A  67      36.151  13.473  -2.442  1.00 10.71           O  
ANISOU  583  OE2 GLU A  67     1615    901   1554    244   -567    -76       O  
ATOM    584  N  APHE A  68      40.413  10.448   1.957  0.59  8.66           N  
ANISOU  584  N  APHE A  68     1280    874   1138     32    -11    376       N  
ATOM    585  N  BPHE A  68      40.412  10.448   1.958  0.41  9.08           N  
ANISOU  585  N  BPHE A  68     1313    839   1299     -3     76    351       N  
ATOM    586  CA APHE A  68      41.006   9.276   2.617  0.59  9.62           C  
ANISOU  586  CA APHE A  68     1251   1076   1327     70    111    625       C  
ATOM    587  CA BPHE A  68      41.019   9.332   2.669  0.41 10.27           C  
ANISOU  587  CA BPHE A  68     1431    995   1477    153    200    474       C  
ATOM    588  C  APHE A  68      41.330   9.563   4.070  0.59 10.14           C  
ANISOU  588  C  APHE A  68     1296   1281   1275     24    117    698       C  
ATOM    589  C  BPHE A  68      41.172   9.601   4.155  0.41 10.40           C  
ANISOU  589  C  BPHE A  68     1256   1266   1429     59     98    525       C  
ATOM    590  O  APHE A  68      41.069   8.680   4.927  0.59 10.76           O  
ANISOU  590  O  APHE A  68     1287   1391   1412    107    281    816       O  
ATOM    591  O  BPHE A  68      40.736   8.815   5.013  0.41 11.37           O  
ANISOU  591  O  BPHE A  68     1488   1270   1560    -39    -50    695       O  
ATOM    592  CB APHE A  68      42.212   8.847   1.772  0.59  9.69           C  
ANISOU  592  CB APHE A  68     1227    982   1472     45    140    557       C  
ATOM    593  CB BPHE A  68      42.413   9.091   2.083  0.41  9.19           C  
ANISOU  593  CB BPHE A  68     1138   1084   1268   -120    -66    479       C  
ATOM    594  CG APHE A  68      42.954   7.627   2.250  0.59  8.66           C  
ANISOU  594  CG APHE A  68     1229    923   1139    -58     87    479       C  
ATOM    595  CG BPHE A  68      43.147   7.930   2.721  0.41  7.66           C  
ANISOU  595  CG BPHE A  68     1145    935    831   -138    -63    268       C  
ATOM    596  CD1APHE A  68      42.627   6.369   1.821  0.59  9.26           C  
ANISOU  596  CD1APHE A  68     1298    963   1256     37     48    309       C  
ATOM    597  CD1BPHE A  68      44.239   8.152   3.524  0.41  9.27           C  
ANISOU  597  CD1BPHE A  68     1260   1305    958    -96   -216     78       C  
ATOM    598  CD2APHE A  68      44.000   7.759   3.133  0.59  8.74           C  
ANISOU  598  CD2APHE A  68     1315    950   1055    -70     66    389       C  
ATOM    599  CD2BPHE A  68      42.705   6.648   2.465  0.41 11.08           C  
ANISOU  599  CD2BPHE A  68     1669    969   1573     12   -629    -79       C  
ATOM    600  CE1APHE A  68      43.365   5.270   2.273  0.59 11.54           C  
ANISOU  600  CE1APHE A  68     1726    938   1721     68   -181    334       C  
ATOM    601  CE1BPHE A  68      44.928   7.061   4.084  0.41 10.54           C  
ANISOU  601  CE1BPHE A  68     1113   1677   1214    -10   -241    289       C  
ATOM    602  CE2APHE A  68      44.764   6.657   3.589  0.59 10.09           C  
ANISOU  602  CE2APHE A  68     1437   1247   1150    162    -19    351       C  
ATOM    603  CE2BPHE A  68      43.395   5.558   3.000  0.41 12.11           C  
ANISOU  603  CE2BPHE A  68     1615    953   2033     -3   -286    192       C  
ATOM    604  CZ APHE A  68      44.414   5.407   3.139  0.59 10.16           C  
ANISOU  604  CZ APHE A  68     1247   1066   1547    261    175    454       C  
ATOM    605  CZ BPHE A  68      44.501   5.784   3.787  0.41 11.46           C  
ANISOU  605  CZ BPHE A  68     1438   1394   1523    394   -114    164       C  
ATOM    606  N   LEU A  69      41.790  10.744   4.426  1.00 11.01           N  
ANISOU  606  N   LEU A  69     1335   1445   1403   -161   -124    735       N  
ATOM    607  CA  LEU A  69      42.046  11.111   5.832  1.00 13.94           C  
ANISOU  607  CA  LEU A  69     1891   1945   1460   -574   -568    853       C  
ATOM    608  C   LEU A  69      40.736  11.117   6.588  1.00 13.06           C  
ANISOU  608  C   LEU A  69     2229   1672   1060   -173   -470    215       C  
ATOM    609  O   LEU A  69      40.652  10.629   7.739  1.00 15.68           O  
ANISOU  609  O   LEU A  69     2183   2655   1118   -465   -403    539       O  
ATOM    610  CB  LEU A  69      42.695  12.449   5.856  1.00 19.23           C  
ANISOU  610  CB  LEU A  69     2993   2064   2250  -1048  -1315    944       C  
ATOM    611  CG  LEU A  69      44.091  12.789   5.760  1.00 18.98           C  
ANISOU  611  CG  LEU A  69     3003   1918   2291   -988   -821    368       C  
ATOM    612  CD1 LEU A  69      44.321  14.323   5.947  1.00 23.21           C  
ANISOU  612  CD1 LEU A  69     2971   2017   3828   -879  -1184   -278       C  
ATOM    613  CD2 LEU A  69      44.899  12.115   6.810  1.00 20.92           C  
ANISOU  613  CD2 LEU A  69     2966   2714   2267   -484  -1066     74       C  
ATOM    614  N  ASER A  70      39.690  11.654   6.026  0.78 12.65           N  
ANISOU  614  N  ASER A  70     2100   1806    899   -197   -256    117       N  
ATOM    615  N  BSER A  70      39.683  11.625   5.973  0.22 13.63           N  
ANISOU  615  N  BSER A  70     2138   2054    985    -73   -431     -4       N  
ATOM    616  CA ASER A  70      38.429  11.737   6.721  0.78 14.51           C  
ANISOU  616  CA ASER A  70     2410   2216    887    251    -89   -241       C  
ATOM    617  CA BSER A  70      38.345  11.614   6.524  0.22 15.88           C  
ANISOU  617  CA BSER A  70     2343   2511   1181    307   -142   -100       C  
ATOM    618  C  ASER A  70      37.887  10.352   7.027  0.78 14.26           C  
ANISOU  618  C  ASER A  70     1871   2580    967    103    238    178       C  
ATOM    619  C  BSER A  70      37.880  10.200   6.847  0.22 15.09           C  
ANISOU  619  C  BSER A  70     1711   2858   1166    163   -239    363       C  
ATOM    620  O  ASER A  70      37.539  10.065   8.163  0.78 20.07           O  
ANISOU  620  O  ASER A  70     2621   3893   1111    369    381    665       O  
ATOM    621  O  BSER A  70      37.331   9.930   7.906  0.22 15.31           O  
ANISOU  621  O  BSER A  70     1921   3061    835    579   -425    359       O  
ATOM    622  CB ASER A  70      37.512  12.582   5.842  0.78 15.13           C  
ANISOU  622  CB ASER A  70     2508   2030   1210    465    -90   -423       C  
ATOM    623  CB BSER A  70      37.369  12.244   5.522  0.22 14.49           C  
ANISOU  623  CB BSER A  70     2289   1636   1579    343   -355   -504       C  
ATOM    624  OG ASER A  70      36.227  12.646   6.408  0.78 20.57           O  
ANISOU  624  OG ASER A  70     2523   3235   2057    671    151   -329       O  
ATOM    625  OG BSER A  70      37.358  13.640   5.727  0.22 16.30           O  
ANISOU  625  OG BSER A  70     2280   1397   2517   -646    226     98       O  
ATOM    626  N  ALEU A  71      37.804   9.453   6.054  0.53 12.15           N  
ANISOU  626  N  ALEU A  71     1369   2036   1213     53     54    410       N  
ATOM    627  N  BLEU A  71      38.108   9.306   5.896  0.47 12.71           N  
ANISOU  627  N  BLEU A  71     1338   2276   1214   -248    204    610       N  
ATOM    628  CA ALEU A  71      37.275   8.094   6.213  0.53 12.64           C  
ANISOU  628  CA ALEU A  71     1254   2422   1126   -394    -53    787       C  
ATOM    629  CA BLEU A  71      37.825   7.871   6.048  0.47 16.16           C  
ANISOU  629  CA BLEU A  71     1722   2355   2063   -458    -25   1068       C  
ATOM    630  C  ALEU A  71      38.131   7.209   7.110  0.53 12.91           C  
ANISOU  630  C  ALEU A  71     1342   2264   1299   -500   -162    837       C  
ATOM    631  C  BLEU A  71      38.581   7.412   7.293  0.47 16.18           C  
ANISOU  631  C  BLEU A  71     1741   2682   1725   -180    353   1141       C  
ATOM    632  O  ALEU A  71      37.686   6.366   7.897  0.53 15.63           O  
ANISOU  632  O  ALEU A  71     1532   2323   2084   -949   -378   1223       O  
ATOM    633  O  BLEU A  71      37.994   6.927   8.278  0.47 17.81           O  
ANISOU  633  O  BLEU A  71     2380   2603   1783   -929    442    956       O  
ATOM    634  CB ALEU A  71      37.175   7.388   4.842  0.53 13.80           C  
ANISOU  634  CB ALEU A  71     1640   2302   1300   -925   -295    838       C  
ATOM    635  CB BLEU A  71      38.215   7.114   4.769  0.47 16.24           C  
ANISOU  635  CB BLEU A  71     2409   1677   2083   -698   -529    940       C  
ATOM    636  CG ALEU A  71      37.583   5.899   4.967  0.53 24.20           C  
ANISOU  636  CG ALEU A  71     3262   2610   3323     50    848    200       C  
ATOM    637  CG BLEU A  71      38.549   5.603   4.814  0.47 21.46           C  
ANISOU  637  CG BLEU A  71     3692   2100   2362    281   -846   1227       C  
ATOM    638  CD1ALEU A  71      36.466   4.935   4.686  0.53 32.24           C  
ANISOU  638  CD1ALEU A  71     4563   2006   5681   -673   1340    271       C  
ATOM    639  CD1BLEU A  71      37.592   4.912   3.867  0.47 28.35           C  
ANISOU  639  CD1BLEU A  71     4177   2533   4062   -693     70   -738       C  
ATOM    640  CD2ALEU A  71      38.776   5.772   4.033  0.53 23.71           C  
ANISOU  640  CD2ALEU A  71     2953   4770   1287    264   -107   -118       C  
ATOM    641  CD2BLEU A  71      39.971   5.407   4.357  0.47 29.31           C  
ANISOU  641  CD2BLEU A  71     3668   2934   4536    801   -743   1436       C  
ATOM    642  N  AMET A  72      39.474   7.386   7.028  0.67 13.09           N  
ANISOU  642  N  AMET A  72     1306   2273   1395   -435    -83    908       N  
ATOM    643  N  BMET A  72      39.904   7.599   7.290  0.33 14.06           N  
ANISOU  643  N  BMET A  72     1671   2305   1366    111    346    994       N  
ATOM    644  CA AMET A  72      40.367   6.603   7.893  0.67 14.57           C  
ANISOU  644  CA AMET A  72     1462   2245   1828   -497   -234   1080       C  
ATOM    645  CA BMET A  72      40.795   7.164   8.365  0.33 13.83           C  
ANISOU  645  CA BMET A  72     2047   1562   1647    -28     19   1049       C  
ATOM    646  C  AMET A  72      40.298   7.013   9.318  0.67 16.84           C  
ANISOU  646  C  AMET A  72     2045   2702   1652   -661   -504   1178       C  
ATOM    647  C  BMET A  72      40.263   7.478   9.746  0.33 17.29           C  
ANISOU  647  C  BMET A  72     2416   2644   1508    147    -15   1135       C  
ATOM    648  O  AMET A  72      40.174   6.200  10.235  0.67 19.71           O  
ANISOU  648  O  AMET A  72     2867   2841   1782   -571   -603   1413       O  
ATOM    649  O  BMET A  72      40.369   6.722  10.710  0.33 16.98           O  
ANISOU  649  O  BMET A  72     1703   3067   1680   -266   -180   1454       O  
ATOM    650  CB AMET A  72      41.848   6.809   7.512  0.67 16.21           C  
ANISOU  650  CB AMET A  72     1477   2081   2599   -274   -161   1526       C  
ATOM    651  CB BMET A  72      42.179   7.842   8.295  0.33 18.67           C  
ANISOU  651  CB BMET A  72     1862   2592   2640   -172    -54   1358       C  
ATOM    652  CG AMET A  72      42.166   6.091   6.243  0.67 18.79           C  
ANISOU  652  CG AMET A  72     2128   2274   2740    345    392   1694       C  
ATOM    653  CG BMET A  72      43.055   7.287   7.190  0.33 19.97           C  
ANISOU  653  CG BMET A  72     2096   2458   3036   -260    304   1309       C  
ATOM    654  SD AMET A  72      42.076   4.339   6.456  0.67 23.78           S  
ANISOU  654  SD AMET A  72     3707   2244   3085    563    677   1424       S  
ATOM    655  SD BMET A  72      43.119   5.490   7.272  0.33 24.09           S  
ANISOU  655  SD BMET A  72     3883   2338   2933   -589   -635    624       S  
ATOM    656  CE AMET A  72      43.386   4.004   7.615  0.67 35.74           C  
ANISOU  656  CE AMET A  72     5244   4514   3820   2553    217   2557       C  
ATOM    657  CE BMET A  72      44.857   5.209   7.039  0.33 30.16           C  
ANISOU  657  CE BMET A  72     5255   4085   2120   1939   1666   1337       C  
ATOM    658  N  AALA A  73      40.418   8.307   9.560  0.54 14.98           N  
ANISOU  658  N  AALA A  73     1465   2636   1591   -136   -171   1050       N  
ATOM    659  N  BALA A  73      39.668   8.655   9.843  0.46 16.19           N  
ANISOU  659  N  BALA A  73     1948   2989   1215    337    144    886       N  
ATOM    660  CA AALA A  73      40.338   8.769  10.932  0.54 17.68           C  
ANISOU  660  CA AALA A  73     1627   3417   1673   -272   -245    736       C  
ATOM    661  CA BALA A  73      39.261   9.082  11.177  0.46 16.55           C  
ANISOU  661  CA BALA A  73     1863   3428    998   -103   -132    806       C  
ATOM    662  C  AALA A  73      39.041   8.301  11.600  0.54 17.58           C  
ANISOU  662  C  AALA A  73     1767   3639   1273   -336   -312    947       C  
ATOM    663  C  BALA A  73      38.035   8.292  11.586  0.46 16.51           C  
ANISOU  663  C  BALA A  73     1786   3487   1000    -30    -29    706       C  
ATOM    664  O  AALA A  73      39.056   7.927  12.777  0.54 21.10           O  
ANISOU  664  O  AALA A  73     2003   4506   1507    -79   -371   1410       O  
ATOM    665  O  BALA A  73      37.963   7.813  12.716  0.46 16.36           O  
ANISOU  665  O  BALA A  73     2032   3099   1083   -430   -306    738       O  
ATOM    666  CB AALA A  73      40.422  10.273  10.996  0.54 18.04           C  
ANISOU  666  CB AALA A  73     1402   3456   1997   -414   -449    379       C  
ATOM    667  CB BALA A  73      38.976  10.557  11.188  0.46 21.88           C  
ANISOU  667  CB BALA A  73     3603   3309   1403   -252    643    270       C  
ATOM    668  N  AARG A  74      37.942   8.291  10.862  0.51 16.68           N  
ANISOU  668  N  AARG A  74     1508   3502   1326     13   -140    997       N  
ATOM    669  N  BARG A  74      37.075   8.163  10.692  0.49 15.34           N  
ANISOU  669  N  BARG A  74     1629   2979   1221    227   -147    830       N  
ATOM    670  CA AARG A  74      36.694   7.773  11.398  0.51 16.59           C  
ANISOU  670  CA AARG A  74     1473   3394   1438    167    -52    919       C  
ATOM    671  CA BARG A  74      35.920   7.332  11.012  0.49 17.15           C  
ANISOU  671  CA BARG A  74     1521   3387   1606    191     79    948       C  
ATOM    672  C  AARG A  74      36.752   6.254  11.532  0.51 18.92           C  
ANISOU  672  C  AARG A  74     2091   3422   1674    372    512   1397       C  
ATOM    673  C  BARG A  74      36.319   5.950  11.439  0.49 18.66           C  
ANISOU  673  C  BARG A  74     1852   3451   1786    195    352   1347       C  
ATOM    674  O  AARG A  74      36.329   5.765  12.595  0.51 23.26           O  
ANISOU  674  O  AARG A  74     2527   4192   2120    703   1023   1785       O  
ATOM    675  O  BARG A  74      35.891   5.365  12.424  0.49 24.55           O  
ANISOU  675  O  BARG A  74     2278   4621   2430    570    825   2123       O  
ATOM    676  CB AARG A  74      35.525   8.256  10.548  0.51 17.54           C  
ANISOU  676  CB AARG A  74     1448   3633   1582    309     98   1142       C  
ATOM    677  CB BARG A  74      34.994   7.272   9.776  0.49 18.13           C  
ANISOU  677  CB BARG A  74     1557   3283   2049    108   -226    911       C  
ATOM    678  CG AARG A  74      35.327   9.766  10.636  0.51 21.74           C  
ANISOU  678  CG AARG A  74     2076   3579   2606    198   -336   1517       C  
ATOM    679  CG BARG A  74      34.195   8.596   9.900  0.49 20.42           C  
ANISOU  679  CG BARG A  74     2036   3578   2146    417  -1001   -202       C  
ATOM    680  CD AARG A  74      34.302  10.310   9.659  0.51 21.88           C  
ANISOU  680  CD AARG A  74     1585   3699   3028    340   -445   1142       C  
ATOM    681  CD BARG A  74      32.913   8.183  10.666  0.49 26.32           C  
ANISOU  681  CD BARG A  74     2669   3903   3427   1148    189    347       C  
ATOM    682  NE AARG A  74      33.072   9.557   9.606  0.51 20.82           N  
ANISOU  682  NE AARG A  74     1526   3449   2935    389    151   1308       N  
ATOM    683  NE BARG A  74      31.808   8.339   9.758  0.49 26.77           N  
ANISOU  683  NE BARG A  74     1859   4084   4230    464    436   1755       N  
ATOM    684  CZ AARG A  74      32.563   8.803   8.641  0.51 24.04           C  
ANISOU  684  CZ AARG A  74     1428   4225   3482    217   -784   1361       C  
ATOM    685  CZ BARG A  74      30.881   7.635   9.182  0.49 35.02           C  
ANISOU  685  CZ BARG A  74     3281   5328   4696    576   -639    568       C  
ATOM    686  NH1AARG A  74      33.220   8.641   7.485  0.51 32.15           N  
ANISOU  686  NH1AARG A  74     3992   6029   2196  -3214   -682   1214       N  
ATOM    687  NH1BARG A  74      30.644   6.333   9.284  0.49 37.71           N  
ANISOU  687  NH1BARG A  74     6834   5729   1766  -1107  -1467    -29       N  
ATOM    688  NH2AARG A  74      31.393   8.172   8.776  0.51 26.55           N  
ANISOU  688  NH2AARG A  74     1755   4204   4129    -70   -758   2097       N  
ATOM    689  NH2BARG A  74      30.040   8.299   8.380  0.49 48.87           N  
ANISOU  689  NH2BARG A  74     6373   7275   4920    817  -2713    640       N  
ATOM    690  N   LYS A  75      37.229   5.418  10.614  1.00 19.83           N  
ANISOU  690  N   LYS A  75     2555   3263   1716    484    484   1422       N  
ATOM    691  CA  LYS A  75      37.442   3.966  10.753  1.00 22.03           C  
ANISOU  691  CA  LYS A  75     2984   3276   2111    415    554   1413       C  
ATOM    692  C   LYS A  75      38.219   3.702  12.012  1.00 20.78           C  
ANISOU  692  C   LYS A  75     2285   3139   2471    634    694   1735       C  
ATOM    693  O   LYS A  75      37.989   2.747  12.748  1.00 22.48           O  
ANISOU  693  O   LYS A  75     2628   3243   2672    563    831   1939       O  
ATOM    694  CB  LYS A  75      38.121   3.398   9.485  1.00 23.99           C  
ANISOU  694  CB  LYS A  75     3419   2961   2737   -611   1080    689       C  
ATOM    695  CG  LYS A  75      37.109   3.135   8.363  1.00 34.70           C  
ANISOU  695  CG  LYS A  75     6082   4501   2601    104   -264    865       C  
ATOM    696  CD  LYS A  75      37.787   2.423   7.204  1.00 42.14           C  
ANISOU  696  CD  LYS A  75     8026   4719   3266   1413   -927    -19       C  
ATOM    697  CE  LYS A  75      36.930   1.452   6.424  1.00 51.60           C  
ANISOU  697  CE  LYS A  75     8855   6371   4382   1291  -1848   -913       C  
ATOM    698  NZ  LYS A  75      37.336   1.351   4.982  1.00 60.20           N  
ANISOU  698  NZ  LYS A  75    10628   6522   5724  -1121    260  -3055       N  
ATOM    699  N  AMET A  76      39.168   4.546  12.387  0.60 22.19           N  
ANISOU  699  N  AMET A  76     2672   3398   2360    357    450   1897       N  
ATOM    700  N  BMET A  76      39.189   4.574  12.275  0.40 21.46           N  
ANISOU  700  N  BMET A  76     2600   3333   2221    426    529   1875       N  
ATOM    701  CA AMET A  76      39.962   4.230  13.588  0.60 22.35           C  
ANISOU  701  CA AMET A  76     2896   3127   2470     93    401   2084       C  
ATOM    702  CA BMET A  76      40.015   4.503  13.474  0.40 22.95           C  
ANISOU  702  CA BMET A  76     3278   3211   2233    206    312   1986       C  
ATOM    703  C  AMET A  76      39.234   4.607  14.852  0.60 23.16           C  
ANISOU  703  C  AMET A  76     3711   2780   2310    138    486   2001       C  
ATOM    704  C  BMET A  76      39.116   4.451  14.710  0.40 23.38           C  
ANISOU  704  C  BMET A  76     3880   2848   2156    352    502   1606       C  
ATOM    705  O  AMET A  76      39.565   4.174  15.974  0.60 27.59           O  
ANISOU  705  O  AMET A  76     4752   3568   2162    557   -282   1446       O  
ATOM    706  O  BMET A  76      39.251   3.575  15.594  0.40 15.46           O  
ANISOU  706  O  BMET A  76     2480   1927   1467   -490     -3    846       O  
ATOM    707  CB AMET A  76      41.265   4.995  13.470  0.60 21.85           C  
ANISOU  707  CB AMET A  76     3072   2568   2663     11    150   1854       C  
ATOM    708  CB BMET A  76      40.958   5.707  13.556  0.40 23.54           C  
ANISOU  708  CB BMET A  76     3507   3016   2422    276     52   1861       C  
ATOM    709  CG AMET A  76      41.977   4.702  12.151  0.60 25.41           C  
ANISOU  709  CG AMET A  76     2557   4113   2985   -495    319   1563       C  
ATOM    710  CG BMET A  76      42.320   5.501  12.962  0.40 26.37           C  
ANISOU  710  CG BMET A  76     3580   4020   2420   -215    399   2216       C  
ATOM    711  SD AMET A  76      43.286   5.863  11.871  0.60 27.17           S  
ANISOU  711  SD AMET A  76     3068   4389   2867  -1066    143   1267       S  
ATOM    712  SD BMET A  76      43.679   6.613  13.327  0.40 37.03           S  
ANISOU  712  SD BMET A  76     4551   4482   5035  -1171   1578   1153       S  
ATOM    713  CE AMET A  76      43.081   7.156  13.087  0.60 36.85           C  
ANISOU  713  CE AMET A  76     6020   2272   5709    473    544   1340       C  
ATOM    714  CE BMET A  76      42.869   8.209  13.366  0.40 26.95           C  
ANISOU  714  CE BMET A  76     2949   4416   2875  -1471    -19   2751       C  
ATOM    715  N   LYS A  77      38.194   5.414  14.734  1.00 22.41           N  
ANISOU  715  N   LYS A  77     3846   2473   2196    104    401   1469       N  
ATOM    716  CA  LYS A  77      37.319   5.569  15.927  1.00 25.50           C  
ANISOU  716  CA  LYS A  77     4985   2177   2525    264    906    943       C  
ATOM    717  C   LYS A  77      36.402   4.392  16.057  1.00 21.01           C  
ANISOU  717  C   LYS A  77     3571   2311   2100    716    762   1137       C  
ATOM    718  O   LYS A  77      36.095   3.838  17.136  1.00 22.36           O  
ANISOU  718  O   LYS A  77     4364   2240   1890    506   1002    758       O  
ATOM    719  CB  LYS A  77      36.528   6.892  15.811  1.00 32.34           C  
ANISOU  719  CB  LYS A  77     7437   2200   2652   1034   1437    957       C  
ATOM    720  CG  LYS A  77      37.274   8.189  16.076  1.00 44.16           C  
ANISOU  720  CG  LYS A  77     9962   2251   4568     65   2761    445       C  
ATOM    721  CD  LYS A  77      36.396   9.416  15.855  1.00 50.35           C  
ANISOU  721  CD  LYS A  77     9575   2120   7434   -287   1121   -160       C  
ATOM    722  CE  LYS A  77      37.056  10.566  15.129  1.00 52.43           C  
ANISOU  722  CE  LYS A  77    10166   2339   7415    109    363    926       C  
ATOM    723  NZ  LYS A  77      36.129  11.175  14.121  1.00 59.77           N  
ANISOU  723  NZ  LYS A  77    10508   3418   8782   1563     -6    646       N  
ATOM    724  N  AGLU A  78      35.918   3.940  14.899  0.58 20.26           N  
ANISOU  724  N  AGLU A  78     2793   2897   2006    654    972   1196       N  
ATOM    725  N  BGLU A  78      35.904   3.837  14.950  0.42 18.75           N  
ANISOU  725  N  BGLU A  78     2409   2730   1985    975    724   1303       N  
ATOM    726  CA AGLU A  78      35.115   2.729  14.852  0.58 19.93           C  
ANISOU  726  CA AGLU A  78     2482   3068   2022    598    914   1137       C  
ATOM    727  CA BGLU A  78      35.032   2.669  15.101  0.42 20.38           C  
ANISOU  727  CA BGLU A  78     2380   3418   1947    497    239   1522       C  
ATOM    728  C  AGLU A  78      35.859   1.580  15.510  0.58 19.18           C  
ANISOU  728  C  AGLU A  78     2415   2918   1955    270    735   1189       C  
ATOM    729  C  BGLU A  78      35.830   1.436  15.462  0.42 16.78           C  
ANISOU  729  C  BGLU A  78     1963   2715   1697   -119      7   1077       C  
ATOM    730  O  AGLU A  78      35.327   0.857  16.378  0.58 17.77           O  
ANISOU  730  O  AGLU A  78     2470   2702   1579   -377    343    835       O  
ATOM    731  O  BGLU A  78      35.319   0.495  16.092  0.42 23.24           O  
ANISOU  731  O  BGLU A  78     2534   3854   2442    100    489   2275       O  
ATOM    732  CB AGLU A  78      34.779   2.385  13.397  0.58 24.34           C  
ANISOU  732  CB AGLU A  78     3661   3504   2082    291    392   1337       C  
ATOM    733  CB BGLU A  78      34.247   2.457  13.810  0.42 22.00           C  
ANISOU  733  CB BGLU A  78     3138   3395   1828    899     43   1294       C  
ATOM    734  CG AGLU A  78      33.350   2.523  12.935  0.58 29.15           C  
ANISOU  734  CG AGLU A  78     3639   4537   2900    -73     56    618       C  
ATOM    735  CG BGLU A  78      33.771   1.056  13.468  0.42 27.10           C  
ANISOU  735  CG BGLU A  78     3620   4034   2643    259    431    528       C  
ATOM    736  CD AGLU A  78      33.016   3.192  11.631  0.58 31.19           C  
ANISOU  736  CD AGLU A  78     3636   5163   3053     -2   -661    565       C  
ATOM    737  CD BGLU A  78      33.422   0.981  11.990  0.42 34.22           C  
ANISOU  737  CD BGLU A  78     5215   4426   3360   1250  -1321    271       C  
ATOM    738  OE1AGLU A  78      33.609   2.876  10.573  0.58 39.96           O  
ANISOU  738  OE1AGLU A  78     7659   4987   2535  -1179   -261   -440       O  
ATOM    739  OE1BGLU A  78      33.184   2.063  11.403  0.42 38.35           O  
ANISOU  739  OE1BGLU A  78     6041   5046   3487    785    -53   1406       O  
ATOM    740  OE2AGLU A  78      32.122   4.072  11.518  0.58 42.80           O  
ANISOU  740  OE2AGLU A  78     2622   7129   6511    255  -1541   1769       O  
ATOM    741  OE2BGLU A  78      33.388  -0.119  11.389  0.42 52.25           O  
ANISOU  741  OE2BGLU A  78     9877   5596   4380   3217  -2996  -1093       O  
ATOM    742  N   GLN A  79      37.108   1.399  15.084  1.00 18.48           N  
ANISOU  742  N   GLN A  79     2179   2918   1926    177    429   1344       N  
ATOM    743  CA  GLN A  79      37.882   0.234  15.502  1.00 18.67           C  
ANISOU  743  CA  GLN A  79     2189   2773   2131    117    417   1145       C  
ATOM    744  C   GLN A  79      38.166   0.301  16.983  1.00 18.14           C  
ANISOU  744  C   GLN A  79     2317   2466   2108    195    441   1205       C  
ATOM    745  O   GLN A  79      38.151  -0.727  17.681  1.00 18.74           O  
ANISOU  745  O   GLN A  79     2288   2549   2285    -31    523   1358       O  
ATOM    746  CB  GLN A  79      39.108   0.177  14.577  1.00 25.77           C  
ANISOU  746  CB  GLN A  79     3485   3532   2773   1068   1516   1487       C  
ATOM    747  CG  GLN A  79      38.747  -0.351  13.185  1.00 39.28           C  
ANISOU  747  CG  GLN A  79     6660   5905   2358    111   1832   1396       C  
ATOM    748  CD  GLN A  79      39.916  -0.689  12.287  1.00 46.38           C  
ANISOU  748  CD  GLN A  79     6828   7354   3441    484   1643   -823       C  
ATOM    749  OE1 GLN A  79      39.881  -1.559  11.409  1.00 61.45           O  
ANISOU  749  OE1 GLN A  79     8974   8925   5448   5108  -1684  -2698       O  
ATOM    750  NE2 GLN A  79      41.046   0.006  12.488  1.00 66.58           N  
ANISOU  750  NE2 GLN A  79     6736  11273   7289  -1052   2585   -746       N  
ATOM    751  N  AASP A  80      38.453   1.475  17.540  0.31 18.38           N  
ANISOU  751  N  AASP A  80     2376   2448   2160    165    241   1266       N  
ATOM    752  N  BASP A  80      38.399   1.490  17.507  0.69 18.43           N  
ANISOU  752  N  BASP A  80     2349   2475   2177    -50    362   1227       N  
ATOM    753  CA AASP A  80      38.646   1.539  18.987  0.31 19.26           C  
ANISOU  753  CA AASP A  80     2569   2548   2203   -402    124   1352       C  
ATOM    754  CA BASP A  80      38.672   1.642  18.929  0.69 19.64           C  
ANISOU  754  CA BASP A  80     2504   2592   2366   -281    -20   1229       C  
ATOM    755  C  AASP A  80      37.393   1.016  19.689  0.31 18.83           C  
ANISOU  755  C  AASP A  80     2655   2354   2146   -366    207   1234       C  
ATOM    756  C  BASP A  80      37.432   1.324  19.748  0.69 18.51           C  
ANISOU  756  C  BASP A  80     2902   2339   1793   -516    108    725       C  
ATOM    757  O  AASP A  80      37.450   0.073  20.479  0.31 19.57           O  
ANISOU  757  O  AASP A  80     2600   3097   1741   -497    -29   1496       O  
ATOM    758  O  BASP A  80      37.485   0.721  20.823  0.69 20.94           O  
ANISOU  758  O  BASP A  80     3604   2598   1755  -1160   -230    758       O  
ATOM    759  CB AASP A  80      38.946   2.962  19.427  0.31 22.62           C  
ANISOU  759  CB AASP A  80     2687   2971   2937   -866    -13    894       C  
ATOM    760  CB BASP A  80      39.201   3.048  19.135  0.69 24.01           C  
ANISOU  760  CB BASP A  80     3294   3027   2803   -940    397    863       C  
ATOM    761  CG AASP A  80      40.066   3.580  18.625  0.31 27.10           C  
ANISOU  761  CG AASP A  80     3328   3370   3599  -1293    275   1170       C  
ATOM    762  CG BASP A  80      40.668   3.143  18.763  0.69 27.04           C  
ANISOU  762  CG BASP A  80     3183   3305   3788  -1013    168   1006       C  
ATOM    763  OD1AASP A  80      40.996   2.825  18.247  0.31 33.96           O  
ANISOU  763  OD1AASP A  80     4381   4338   4186  -1007   1858   1178       O  
ATOM    764  OD1BASP A  80      41.381   2.111  18.795  0.69 31.66           O  
ANISOU  764  OD1BASP A  80     3910   4307   3814     15    648   1077       O  
ATOM    765  OD2AASP A  80      39.998   4.801  18.366  0.31 32.20           O  
ANISOU  765  OD2AASP A  80     3240   3660   5336  -1658   -953   2055       O  
ATOM    766  OD2BASP A  80      41.056   4.293  18.426  0.69 36.98           O  
ANISOU  766  OD2BASP A  80     3670   4041   6339  -1775   -124   1974       O  
ATOM    767  N  ASER A  81      36.268   1.625  19.339  0.46 19.08           N  
ANISOU  767  N  ASER A  81     2725   2279   2245   -101    445   1158       N  
ATOM    768  N  BSER A  81      36.239   1.651  19.236  0.54 18.78           N  
ANISOU  768  N  BSER A  81     2732   2323   2078    -89    436    573       N  
ATOM    769  CA ASER A  81      34.956   1.250  19.875  0.46 21.04           C  
ANISOU  769  CA ASER A  81     2894   3098   2001    137    915    945       C  
ATOM    770  CA BSER A  81      35.029   1.241  19.972  0.54 20.47           C  
ANISOU  770  CA BSER A  81     3003   2823   1952    394    856    847       C  
ATOM    771  C  ASER A  81      34.755  -0.249  19.855  0.46 18.93           C  
ANISOU  771  C  ASER A  81     2163   3212   1816   -423    468   1138       C  
ATOM    772  C  BSER A  81      34.736  -0.241  19.838  0.54 18.30           C  
ANISOU  772  C  BSER A  81     2237   3147   1570   -336    137    890       C  
ATOM    773  O  ASER A  81      34.410  -0.916  20.839  0.46 18.83           O  
ANISOU  773  O  ASER A  81     1380   3584   2193    328    707   1612       O  
ATOM    774  O  BSER A  81      34.143  -0.857  20.735  0.54 26.66           O  
ANISOU  774  O  BSER A  81     4883   3829   1418  -1190    449    965       O  
ATOM    775  CB ASER A  81      33.860   1.963  19.077  0.46 22.72           C  
ANISOU  775  CB ASER A  81     2757   3569   2306    681   1201    870       C  
ATOM    776  CB BSER A  81      33.784   2.008  19.520  0.54 22.60           C  
ANISOU  776  CB BSER A  81     3020   3704   1861    641    548    603       C  
ATOM    777  OG ASER A  81      33.758   3.337  19.417  0.46 29.00           O  
ANISOU  777  OG ASER A  81     4470   3031   3519    328   1186   1786       O  
ATOM    778  OG BSER A  81      32.575   1.286  19.725  0.54 30.44           O  
ANISOU  778  OG BSER A  81     2898   5070   3599    778   1463   1521       O  
ATOM    779  N  AGLU A  82      34.983  -0.836  18.675  0.56 17.40           N  
ANISOU  779  N  AGLU A  82     1885   2823   1902   -242    365   1267       N  
ATOM    780  N  BGLU A  82      35.125  -0.804  18.695  0.44 17.09           N  
ANISOU  780  N  BGLU A  82     2093   2630   1770   -220    222   1011       N  
ATOM    781  CA AGLU A  82      34.787  -2.278  18.567  0.56 18.44           C  
ANISOU  781  CA AGLU A  82     2052   2867   2089   -343     34   1278       C  
ATOM    782  CA BGLU A  82      34.895  -2.233  18.479  0.44 16.89           C  
ANISOU  782  CA BGLU A  82     1780   2639   1999   -344    310   1131       C  
ATOM    783  C  AGLU A  82      35.764  -3.020  19.467  0.56 15.59           C  
ANISOU  783  C  AGLU A  82     2061   2449   1413   -495     -1    846       C  
ATOM    784  C  BGLU A  82      35.763  -3.019  19.454  0.44 16.39           C  
ANISOU  784  C  BGLU A  82     1985   2456   1787   -451     73    915       C  
ATOM    785  O  AGLU A  82      35.429  -4.041  20.074  0.56 18.16           O  
ANISOU  785  O  AGLU A  82     2198   3267   1436   -985   -286   1416       O  
ATOM    786  O  BGLU A  82      35.332  -3.995  20.067  0.44 19.09           O  
ANISOU  786  O  BGLU A  82     1952   2006   3295   -353   -148   1234       O  
ATOM    787  CB AGLU A  82      34.877  -2.755  17.120  0.56 20.09           C  
ANISOU  787  CB AGLU A  82     2656   3036   1942   -436   -702   1261       C  
ATOM    788  CB BGLU A  82      35.152  -2.645  17.037  0.44 19.94           C  
ANISOU  788  CB BGLU A  82     2811   2938   1829  -1225   -319    788       C  
ATOM    789  CG AGLU A  82      34.857  -4.242  17.014  0.56 27.92           C  
ANISOU  789  CG AGLU A  82     4915   3075   2618   -327   -745    927       C  
ATOM    790  CG BGLU A  82      34.127  -2.000  16.103  0.44 24.37           C  
ANISOU  790  CG BGLU A  82     3022   4170   2066   -259     -2    978       C  
ATOM    791  CD AGLU A  82      34.173  -5.034  15.954  0.56 29.69           C  
ANISOU  791  CD AGLU A  82     5849   3410   2021  -1405    -78   1054       C  
ATOM    792  CD BGLU A  82      34.581  -2.030  14.657  0.44 33.41           C  
ANISOU  792  CD BGLU A  82     4661   5951   2084    337    372   2087       C  
ATOM    793  OE1AGLU A  82      34.719  -5.035  14.827  0.56 44.98           O  
ANISOU  793  OE1AGLU A  82     9073   6186   1831  -2168    551   1354       O  
ATOM    794  OE1BGLU A  82      35.806  -2.087  14.408  0.44 39.09           O  
ANISOU  794  OE1BGLU A  82     4966   7677   2211    939   1029   1390       O  
ATOM    795  OE2AGLU A  82      33.139  -5.712  16.208  0.56 40.68           O  
ANISOU  795  OE2AGLU A  82     8092   4241   3123  -3386   -601   2146       O  
ATOM    796  OE2BGLU A  82      33.690  -1.994  13.781  0.44 43.13           O  
ANISOU  796  OE2BGLU A  82     5706   8682   2000   2046    -37   2183       O  
ATOM    797  N   GLU A  83      37.002  -2.565  19.581  1.00 16.72           N  
ANISOU  797  N   GLU A  83     2112   2400   1841   -526    -30   1127       N  
ATOM    798  CA  GLU A  83      37.978  -3.254  20.443  1.00 17.69           C  
ANISOU  798  CA  GLU A  83     2066   2699   1956   -517   -116   1172       C  
ATOM    799  C   GLU A  83      37.511  -3.262  21.861  1.00 18.01           C  
ANISOU  799  C   GLU A  83     2066   2850   1925   -858   -320   1224       C  
ATOM    800  O   GLU A  83      37.679  -4.245  22.593  1.00 19.20           O  
ANISOU  800  O   GLU A  83     1989   3138   2168   -987   -582   1566       O  
ATOM    801  CB  GLU A  83      39.366  -2.565  20.362  1.00 22.30           C  
ANISOU  801  CB  GLU A  83     2007   3831   2636   -666    -40   1685       C  
ATOM    802  CG  GLU A  83      40.368  -3.334  21.200  1.00 21.57           C  
ANISOU  802  CG  GLU A  83     2105   3417   2673   -515   -159   1263       C  
ATOM    803  CD  GLU A  83      40.507  -4.806  20.825  1.00 23.03           C  
ANISOU  803  CD  GLU A  83     2742   3612   2397   -433    -16    993       C  
ATOM    804  OE1 GLU A  83      40.422  -5.129  19.605  1.00 33.67           O  
ANISOU  804  OE1 GLU A  83     5469   4831   2492    487   -367    572       O  
ATOM    805  OE2 GLU A  83      40.727  -5.625  21.693  1.00 24.78           O  
ANISOU  805  OE2 GLU A  83     3591   3279   2544   -119     70    949       O  
ATOM    806  N   GLU A  84      36.922  -2.184  22.331  1.00 17.67           N  
ANISOU  806  N   GLU A  84     1895   2983   1834   -976   -201    913       N  
ATOM    807  CA  GLU A  84      36.393  -2.147  23.682  1.00 21.94           C  
ANISOU  807  CA  GLU A  84     3203   3444   1691  -1892   -134    449       C  
ATOM    808  C   GLU A  84      35.289  -3.205  23.887  1.00 18.82           C  
ANISOU  808  C   GLU A  84     2382   3203   1564  -1330   -219    705       C  
ATOM    809  O   GLU A  84      35.201  -3.849  24.937  1.00 18.42           O  
ANISOU  809  O   GLU A  84     2147   3311   1540  -1069   -190    732       O  
ATOM    810  CB  GLU A  84      35.763  -0.788  24.032  1.00 27.85           C  
ANISOU  810  CB  GLU A  84     4409   3579   2595  -2230    704   -530       C  
ATOM    811  CG  GLU A  84      35.160  -0.722  25.422  1.00 43.83           C  
ANISOU  811  CG  GLU A  84     7790   5464   3398  -1628   2311   -577       C  
ATOM    812  CD  GLU A  84      34.911   0.686  25.941  1.00 60.49           C  
ANISOU  812  CD  GLU A  84    10902   6743   5339   -891   3107  -2320       C  
ATOM    813  OE1 GLU A  84      34.438   1.590  25.209  1.00 72.38           O  
ANISOU  813  OE1 GLU A  84    15567   4550   7384  -1257   1738  -2549       O  
ATOM    814  OE2 GLU A  84      35.198   0.893  27.146  1.00 76.69           O  
ANISOU  814  OE2 GLU A  84    13858   9456   5824   -349   2500  -3710       O  
ATOM    815  N  ALEU A  85      34.395  -3.404  22.900  0.51 16.08           N  
ANISOU  815  N  ALEU A  85     2007   2507   1597   -717   -174    704       N  
ATOM    816  N  BLEU A  85      34.432  -3.311  22.863  0.49 15.63           N  
ANISOU  816  N  BLEU A  85     1889   2687   1362   -804     86    723       N  
ATOM    817  CA ALEU A  85      33.347  -4.417  23.071  0.51 14.30           C  
ANISOU  817  CA ALEU A  85     1708   2286   1439   -460   -223    461       C  
ATOM    818  CA BLEU A  85      33.362  -4.293  22.873  0.49 13.88           C  
ANISOU  818  CA BLEU A  85     1426   2519   1328   -466    -16    692       C  
ATOM    819  C  ALEU A  85      33.902  -5.819  22.942  0.51 14.71           C  
ANISOU  819  C  ALEU A  85     1384   2399   1806   -360    116    818       C  
ATOM    820  C  BLEU A  85      33.936  -5.703  22.946  0.49 13.14           C  
ANISOU  820  C  BLEU A  85     1122   2577   1295   -484   -179    692       C  
ATOM    821  O  ALEU A  85      33.453  -6.788  23.593  0.51 13.37           O  
ANISOU  821  O  ALEU A  85     1301   2534   1245   -383   -173   1048       O  
ATOM    822  O  BLEU A  85      33.436  -6.503  23.790  0.49 12.75           O  
ANISOU  822  O  BLEU A  85     1273   2333   1238   -754    -73    524       O  
ATOM    823  CB ALEU A  85      32.236  -4.134  22.072  0.51 14.03           C  
ANISOU  823  CB ALEU A  85     1535   2375   1420    -97      8    353       C  
ATOM    824  CB BLEU A  85      32.461  -4.102  21.657  0.49 13.53           C  
ANISOU  824  CB BLEU A  85     1539   2303   1298   -295     54    789       C  
ATOM    825  CG ALEU A  85      31.422  -2.855  22.324  0.51 15.95           C  
ANISOU  825  CG ALEU A  85     1423   2152   2487   -319    408    598       C  
ATOM    826  CG BLEU A  85      31.526  -2.880  21.772  0.49 16.24           C  
ANISOU  826  CG BLEU A  85     1888   2305   1978   -161     22    822       C  
ATOM    827  CD1ALEU A  85      30.501  -2.558  21.165  0.51 22.53           C  
ANISOU  827  CD1ALEU A  85     2172   2727   3660    -17   -184   1745       C  
ATOM    828  CD1BLEU A  85      30.995  -2.555  20.374  0.49 17.18           C  
ANISOU  828  CD1BLEU A  85     2277   1897   2354   -411   -200   1296       C  
ATOM    829  CD2ALEU A  85      30.624  -2.973  23.620  0.51 23.91           C  
ANISOU  829  CD2ALEU A  85     2119   3857   3107    607   1207    594       C  
ATOM    830  CD2BLEU A  85      30.379  -3.063  22.747  0.49 20.35           C  
ANISOU  830  CD2BLEU A  85     1765   4043   1925    238    104    202       C  
ATOM    831  N   ILE A  86      34.903  -5.986  22.100  1.00 13.12           N  
ANISOU  831  N   ILE A  86     1312   2435   1239   -417    -93    906       N  
ATOM    832  CA  ILE A  86      35.545  -7.291  22.044  1.00 13.46           C  
ANISOU  832  CA  ILE A  86     1233   2546   1336   -289   -150    880       C  
ATOM    833  C   ILE A  86      36.190  -7.633  23.379  1.00 13.88           C  
ANISOU  833  C   ILE A  86     1094   2773   1409   -515   -208   1041       C  
ATOM    834  O   ILE A  86      36.045  -8.745  23.865  1.00 15.02           O  
ANISOU  834  O   ILE A  86     1140   2906   1662   -595   -240   1300       O  
ATOM    835  CB  ILE A  86      36.566  -7.272  20.878  1.00 15.15           C  
ANISOU  835  CB  ILE A  86     1357   2987   1413   -232   -131    703       C  
ATOM    836  CG1 ILE A  86      35.848  -7.171  19.557  1.00 16.08           C  
ANISOU  836  CG1 ILE A  86     1825   2949   1336   -198   -128    849       C  
ATOM    837  CG2 ILE A  86      37.499  -8.447  20.991  1.00 20.40           C  
ANISOU  837  CG2 ILE A  86     1837   3950   1964    609    195   1157       C  
ATOM    838  CD1 ILE A  86      36.735  -6.895  18.340  1.00 21.08           C  
ANISOU  838  CD1 ILE A  86     2271   4141   1596    219    280   1196       C  
ATOM    839  N  AGLU A  87      36.954  -6.682  23.950  0.58 15.36           N  
ANISOU  839  N  AGLU A  87     1496   2904   1434   -645   -261   1059       N  
ATOM    840  N  BGLU A  87      36.901  -6.664  23.966  0.42 15.08           N  
ANISOU  840  N  BGLU A  87     1240   3063   1425   -794   -241   1171       N  
ATOM    841  CA AGLU A  87      37.572  -7.046  25.234  0.58 16.18           C  
ANISOU  841  CA AGLU A  87     1191   3410   1545   -954   -377   1121       C  
ATOM    842  CA BGLU A  87      37.573  -6.752  25.256  0.42 16.41           C  
ANISOU  842  CA BGLU A  87     1295   3503   1436  -1072   -285   1162       C  
ATOM    843  C  AGLU A  87      36.497  -7.342  26.257  0.58 15.63           C  
ANISOU  843  C  AGLU A  87     1305   3228   1406  -1153   -386    912       C  
ATOM    844  C  BGLU A  87      36.635  -7.115  26.393  0.42 16.66           C  
ANISOU  844  C  BGLU A  87     1329   3600   1402  -1065   -334   1158       C  
ATOM    845  O  AGLU A  87      36.682  -8.390  26.920  0.58 16.03           O  
ANISOU  845  O  AGLU A  87     1356   3575   1160  -1162   -556   1091       O  
ATOM    846  O  BGLU A  87      36.851  -7.899  27.331  0.42 17.33           O  
ANISOU  846  O  BGLU A  87     1195   4357   1033  -1221   -538   1223       O  
ATOM    847  CB AGLU A  87      38.543  -5.950  25.674  0.58 15.05           C  
ANISOU  847  CB AGLU A  87     1304   2626   1790   -719   -284   1136       C  
ATOM    848  CB BGLU A  87      38.255  -5.414  25.567  0.42 15.91           C  
ANISOU  848  CB BGLU A  87     1403   3238   1406   -861   -424   1275       C  
ATOM    849  CG AGLU A  87      39.697  -5.821  24.693  0.58 14.59           C  
ANISOU  849  CG AGLU A  87     1134   2448   1962   -581   -215    692       C  
ATOM    850  CG BGLU A  87      39.510  -5.150  24.746  0.42 15.55           C  
ANISOU  850  CG BGLU A  87     1595   2673   1639   -972   -132    856       C  
ATOM    851  CD AGLU A  87      40.474  -4.530  24.875  0.58 17.38           C  
ANISOU  851  CD AGLU A  87     1425   2506   2673   -745    122    595       C  
ATOM    852  CD BGLU A  87      40.561  -6.203  25.066  0.42 19.53           C  
ANISOU  852  CD BGLU A  87     1502   3174   2744   -790   -277    885       C  
ATOM    853  OE1AGLU A  87      41.462  -4.360  24.170  0.58 20.46           O  
ANISOU  853  OE1AGLU A  87     1387   2698   3689   -643    460    697       O  
ATOM    854  OE1BGLU A  87      40.459  -7.347  24.568  0.42 19.23           O  
ANISOU  854  OE1BGLU A  87     1428   3529   2347    -56   -375    438       O  
ATOM    855  OE2AGLU A  87      40.031  -3.721  25.713  0.58 30.39           O  
ANISOU  855  OE2AGLU A  87     3318   4215   4014  -2508   1535  -1385       O  
ATOM    856  OE2BGLU A  87      41.465  -5.816  25.849  0.42 27.40           O  
ANISOU  856  OE2BGLU A  87     2109   3510   4790   -656  -1450    524       O  
ATOM    857  N   ALA A  88      35.471  -6.502  26.341  1.00 16.65           N  
ANISOU  857  N   ALA A  88     1331   3482   1513  -1077   -273    959       N  
ATOM    858  CA  ALA A  88      34.431  -6.809  27.355  1.00 16.77           C  
ANISOU  858  CA  ALA A  88     1570   3570   1232  -1122   -176    644       C  
ATOM    859  C   ALA A  88      33.833  -8.185  27.133  1.00 15.56           C  
ANISOU  859  C   ALA A  88     1246   3455   1209  -1011   -228    859       C  
ATOM    860  O   ALA A  88      33.648  -8.970  28.086  1.00 17.40           O  
ANISOU  860  O   ALA A  88     1458   3811   1341   -992   -224   1094       O  
ATOM    861  CB  ALA A  88      33.381  -5.723  27.338  1.00 17.83           C  
ANISOU  861  CB  ALA A  88     1839   3552   1383   -984   -174    418       C  
ATOM    862  N   PHE A  89      33.517  -8.535  25.882  1.00 14.06           N  
ANISOU  862  N   PHE A  89     1298   2740   1303   -799   -293    941       N  
ATOM    863  CA  PHE A  89      32.947  -9.835  25.610  1.00 12.77           C  
ANISOU  863  CA  PHE A  89     1085   2553   1215   -389   -259    838       C  
ATOM    864  C   PHE A  89      33.857 -10.945  26.139  1.00 14.13           C  
ANISOU  864  C   PHE A  89      960   2828   1582   -407   -287   1115       C  
ATOM    865  O   PHE A  89      33.395 -11.907  26.729  1.00 14.94           O  
ANISOU  865  O   PHE A  89     1097   2949   1629   -405   -242   1404       O  
ATOM    866  CB  PHE A  89      32.695  -9.983  24.094  1.00 11.93           C  
ANISOU  866  CB  PHE A  89     1010   2295   1228   -225    -98    816       C  
ATOM    867  CG  PHE A  89      32.048 -11.290  23.781  1.00 11.55           C  
ANISOU  867  CG  PHE A  89      963   2256   1168   -220    -88    707       C  
ATOM    868  CD1 PHE A  89      30.666 -11.411  23.837  1.00 11.62           C  
ANISOU  868  CD1 PHE A  89     1016   2234   1165   -185   -135    504       C  
ATOM    869  CD2 PHE A  89      32.771 -12.422  23.466  1.00 14.33           C  
ANISOU  869  CD2 PHE A  89     1125   2341   1978    -39   -276    772       C  
ATOM    870  CE1 PHE A  89      30.027 -12.604  23.616  1.00 12.36           C  
ANISOU  870  CE1 PHE A  89     1075   2471   1148   -297     15    187       C  
ATOM    871  CE2 PHE A  89      32.156 -13.650  23.215  1.00 14.55           C  
ANISOU  871  CE2 PHE A  89     1368   2292   1866     95   -172    474       C  
ATOM    872  CZ  PHE A  89      30.780 -13.710  23.299  1.00 13.44           C  
ANISOU  872  CZ  PHE A  89     1427   2357   1324   -202    -67    323       C  
ATOM    873  N  ALYS A  90      35.160 -10.937  25.756  0.51 14.25           N  
ANISOU  873  N  ALYS A  90     1000   2629   1783   -387   -294   1324       N  
ATOM    874  N  BLYS A  90      35.152 -10.616  26.002  0.49 16.06           N  
ANISOU  874  N  BLYS A  90      992   3095   2015   -523   -406   1443       N  
ATOM    875  CA ALYS A  90      36.035 -12.103  25.959  0.51 11.05           C  
ANISOU  875  CA ALYS A  90      833   2218   1145   -635   -471    570       C  
ATOM    876  CA BLYS A  90      36.158 -11.518  26.548  0.49 12.55           C  
ANISOU  876  CA BLYS A  90      973   2491   1304   -483   -609    325       C  
ATOM    877  C  ALYS A  90      36.248 -12.375  27.440  0.51 10.13           C  
ANISOU  877  C  ALYS A  90      957   1731   1161   -427   -257    543       C  
ATOM    878  C  BLYS A  90      36.204 -11.508  28.066  0.49 12.04           C  
ANISOU  878  C  BLYS A  90     1140   2147   1287   -368   -404    358       C  
ATOM    879  O  ALYS A  90      36.521 -13.495  27.856  0.51 11.17           O  
ANISOU  879  O  ALYS A  90     1197   1754   1291   -191   -199    575       O  
ATOM    880  O  BLYS A  90      36.588 -12.574  28.590  0.49 13.23           O  
ANISOU  880  O  BLYS A  90     1462   2211   1356    -80   -350    333       O  
ATOM    881  CB ALYS A  90      37.404 -11.881  25.285  0.51 11.72           C  
ANISOU  881  CB ALYS A  90     1134   1961   1358   -569   -129    621       C  
ATOM    882  CB BLYS A  90      37.483 -11.168  25.839  0.49 12.67           C  
ANISOU  882  CB BLYS A  90     1100   2245   1469   -352   -337    557       C  
ATOM    883  CG ALYS A  90      37.407 -12.124  23.785  0.51 12.34           C  
ANISOU  883  CG ALYS A  90     1478   1716   1495   -129     54    329       C  
ATOM    884  CG BLYS A  90      37.399 -11.451  24.324  0.49 13.60           C  
ANISOU  884  CG BLYS A  90     1416   2275   1478    -94   -399    438       C  
ATOM    885  CD ALYS A  90      38.709 -12.002  23.064  0.51 13.23           C  
ANISOU  885  CD ALYS A  90     1302   2276   1450     77    -61    627       C  
ATOM    886  CD BLYS A  90      38.717 -11.466  23.627  0.49 16.28           C  
ANISOU  886  CD BLYS A  90     1485   2944   1756    610   -315   -365       C  
ATOM    887  CE ALYS A  90      39.474 -10.740  23.409  0.51 13.05           C  
ANISOU  887  CE ALYS A  90     1364   2280   1313    -57    187    647       C  
ATOM    888  CE BLYS A  90      38.927 -11.329  22.150  0.49 18.73           C  
ANISOU  888  CE BLYS A  90     1043   3839   2235    269    -50   1178       C  
ATOM    889  NZ ALYS A  90      40.837 -10.800  22.749  0.51 16.79           N  
ANISOU  889  NZ ALYS A  90     1285   2972   2125   -130    173   -124       N  
ATOM    890  NZ BLYS A  90      40.351 -10.847  21.932  0.49 25.86           N  
ANISOU  890  NZ BLYS A  90     1530   3153   5143   -308    121   2315       N  
ATOM    891  N  AVAL A  91      36.145 -11.311  28.232  0.54 10.86           N  
ANISOU  891  N  AVAL A  91     1108   1839   1180    -44   -174    494       N  
ATOM    892  N  BVAL A  91      35.822 -10.469  28.795  0.46 10.85           N  
ANISOU  892  N  BVAL A  91     1010   1999   1113   -381   -227    661       N  
ATOM    893  CA AVAL A  91      36.129 -11.496  29.681  0.54 12.30           C  
ANISOU  893  CA AVAL A  91     1184   2329   1159   -472   -224    374       C  
ATOM    894  CA BVAL A  91      35.761 -10.569  30.264  0.46 12.13           C  
ANISOU  894  CA BVAL A  91     1311   2224   1073   -757   -417    497       C  
ATOM    895  C  AVAL A  91      34.863 -12.223  30.115  0.54 10.49           C  
ANISOU  895  C  AVAL A  91     1192   1776   1019   -295   -273    379       C  
ATOM    896  C  BVAL A  91      34.662 -11.546  30.671  0.46 10.23           C  
ANISOU  896  C  BVAL A  91     1029   2007    850   -490   -155    281       C  
ATOM    897  O  AVAL A  91      34.974 -13.144  30.907  0.54 12.54           O  
ANISOU  897  O  AVAL A  91     1328   2130   1308    -59    -94    639       O  
ATOM    898  O  BVAL A  91      34.861 -12.339  31.582  0.46 11.23           O  
ANISOU  898  O  BVAL A  91     1027   2066   1173   -279   -132    524       O  
ATOM    899  CB AVAL A  91      36.205 -10.131  30.406  0.54 15.43           C  
ANISOU  899  CB AVAL A  91     2152   2441   1270  -1063   -298    299       C  
ATOM    900  CB BVAL A  91      35.560  -9.202  30.952  0.46 14.00           C  
ANISOU  900  CB BVAL A  91     1867   2278   1175  -1031   -421    313       C  
ATOM    901  CG1AVAL A  91      36.067 -10.255  31.897  0.54 16.63           C  
ANISOU  901  CG1AVAL A  91     2523   2603   1193   -887   -655    214       C  
ATOM    902  CG1BVAL A  91      35.295  -9.281  32.447  0.46 13.53           C  
ANISOU  902  CG1BVAL A  91     1448   2280   1411   -381     84    489       C  
ATOM    903  CG2AVAL A  91      37.528  -9.488  30.145  0.54 19.00           C  
ANISOU  903  CG2AVAL A  91     2257   3032   1930  -1408  -1037   1129       C  
ATOM    904  CG2BVAL A  91      36.776  -8.320  30.715  0.46 12.49           C  
ANISOU  904  CG2BVAL A  91     1587   1900   1256   -544    -31    281       C  
ATOM    905  N  APHE A  92      33.682 -11.744  29.707  0.61 12.36           N  
ANISOU  905  N  APHE A  92     1106   2092   1499   -261   -130    721       N  
ATOM    906  N  BPHE A  92      33.513 -11.548  29.994  0.39 10.92           N  
ANISOU  906  N  BPHE A  92     1024   2032   1092   -440   -217    428       N  
ATOM    907  CA APHE A  92      32.450 -12.437  30.120  0.61 11.45           C  
ANISOU  907  CA APHE A  92     1136   1949   1265   -269    -54    605       C  
ATOM    908  CA BPHE A  92      32.393 -12.450  30.271  0.39 10.60           C  
ANISOU  908  CA BPHE A  92      930   1907   1191   -375   -265    535       C  
ATOM    909  C  APHE A  92      32.549 -13.906  29.746  0.61 11.15           C  
ANISOU  909  C  APHE A  92      971   1961   1304    -54   -131    612       C  
ATOM    910  C  BPHE A  92      32.477 -13.848  29.679  0.39 12.57           C  
ANISOU  910  C  BPHE A  92     1403   1699   1674   -300    498    697       C  
ATOM    911  O  APHE A  92      32.163 -14.813  30.485  0.61 11.44           O  
ANISOU  911  O  APHE A  92     1447   1872   1029   -135    -22    342       O  
ATOM    912  O  BPHE A  92      31.933 -14.773  30.312  0.39 11.82           O  
ANISOU  912  O  BPHE A  92      724   1752   2017     76    276   1099       O  
ATOM    913  CB APHE A  92      31.204 -11.809  29.509  0.61 10.42           C  
ANISOU  913  CB APHE A  92     1122   1604   1234   -334    -60    552       C  
ATOM    914  CB BPHE A  92      31.053 -11.829  29.827  0.39 11.10           C  
ANISOU  914  CB BPHE A  92      982   2239    996    -87   -154    317       C  
ATOM    915  CG APHE A  92      30.753 -10.562  30.253  0.61  9.76           C  
ANISOU  915  CG APHE A  92      975   1702   1033   -420   -114    565       C  
ATOM    916  CG BPHE A  92      30.664 -10.627  30.690  0.39 13.48           C  
ANISOU  916  CG BPHE A  92     1590   2043   1487   -180    534    388       C  
ATOM    917  CD1APHE A  92      30.155 -10.652  31.512  0.61 15.09           C  
ANISOU  917  CD1APHE A  92     1930   2347   1455   -189    508    562       C  
ATOM    918  CD1BPHE A  92      29.916 -10.760  31.865  0.39 12.69           C  
ANISOU  918  CD1BPHE A  92     1584   2366    871   -489     77    313       C  
ATOM    919  CD2APHE A  92      30.897  -9.305  29.742  0.61 13.83           C  
ANISOU  919  CD2APHE A  92     2252   1610   1393   -266    374    413       C  
ATOM    920  CD2BPHE A  92      31.075  -9.370  30.280  0.39 15.00           C  
ANISOU  920  CD2BPHE A  92     2325   2124   1251   -121    528    620       C  
ATOM    921  CE1APHE A  92      29.732  -9.504  32.177  0.61 16.83           C  
ANISOU  921  CE1APHE A  92     2282   2459   1654   -781    662     28       C  
ATOM    922  CE1BPHE A  92      29.591  -9.608  32.569  0.39 14.82           C  
ANISOU  922  CE1BPHE A  92     1914   2619   1099   -646    408     69       C  
ATOM    923  CE2APHE A  92      30.502  -8.167  30.380  0.61 15.51           C  
ANISOU  923  CE2APHE A  92     2475   1802   1615   -186    354    192       C  
ATOM    924  CE2BPHE A  92      30.746  -8.238  30.995  0.39 13.96           C  
ANISOU  924  CE2BPHE A  92     2096   2011   1197   -439    -26    441       C  
ATOM    925  CZ APHE A  92      29.879  -8.270  31.609  0.61 16.56           C  
ANISOU  925  CZ APHE A  92     2536   2307   1449   -425    296    -40       C  
ATOM    926  CZ BPHE A  92      29.986  -8.372  32.141  0.39 14.31           C  
ANISOU  926  CZ BPHE A  92     1788   2416   1235   -543     -9    -42       C  
ATOM    927  N   ASP A  93      33.054 -14.137  28.512  1.00 12.14           N  
ANISOU  927  N   ASP A  93     1167   2049   1395    -71    175    666       N  
ATOM    928  CA  ASP A  93      33.108 -15.474  27.968  1.00 12.43           C  
ANISOU  928  CA  ASP A  93     1247   2123   1354    -39    122    665       C  
ATOM    929  C   ASP A  93      34.299 -16.248  28.524  1.00 13.83           C  
ANISOU  929  C   ASP A  93     1291   2353   1610    184    228    687       C  
ATOM    930  O   ASP A  93      35.365 -16.416  27.925  1.00 16.02           O  
ANISOU  930  O   ASP A  93     1507   2697   1880    439    454    867       O  
ATOM    931  CB  ASP A  93      33.220 -15.399  26.440  1.00 13.55           C  
ANISOU  931  CB  ASP A  93     1486   2293   1369    160    302    572       C  
ATOM    932  CG  ASP A  93      33.299 -16.766  25.770  1.00 14.63           C  
ANISOU  932  CG  ASP A  93     1496   2353   1710    412    469    508       C  
ATOM    933  OD1 ASP A  93      32.902 -17.725  26.409  1.00 16.02           O  
ANISOU  933  OD1 ASP A  93     2107   2261   1719    272    536    437       O  
ATOM    934  OD2 ASP A  93      33.756 -16.820  24.604  1.00 15.56           O  
ANISOU  934  OD2 ASP A  93     1473   2860   1579    352    461    286       O  
ATOM    935  N   ARG A  94      34.136 -16.706  29.792  1.00 13.44           N  
ANISOU  935  N   ARG A  94     1242   2283   1583     56     92    728       N  
ATOM    936  CA  ARG A  94      35.261 -17.201  30.584  1.00 15.05           C  
ANISOU  936  CA  ARG A  94     1367   2183   2169    144     27   1015       C  
ATOM    937  C   ARG A  94      35.967 -18.368  29.930  1.00 15.88           C  
ANISOU  937  C   ARG A  94     1238   2324   2471    144    223   1088       C  
ATOM    938  O   ARG A  94      37.204 -18.484  30.059  1.00 19.56           O  
ANISOU  938  O   ARG A  94     1205   2765   3460    191    153    957       O  
ATOM    939  CB  ARG A  94      34.779 -17.552  31.990  1.00 16.59           C  
ANISOU  939  CB  ARG A  94     1446   2919   1939    400   -235   1074       C  
ATOM    940  CG  ARG A  94      34.216 -16.398  32.818  1.00 19.74           C  
ANISOU  940  CG  ARG A  94     1877   3312   2311    603    195    934       C  
ATOM    941  CD  ARG A  94      33.862 -16.888  34.231  1.00 21.05           C  
ANISOU  941  CD  ARG A  94     2643   3292   2062    527   -112    822       C  
ATOM    942  NE  ARG A  94      35.044 -17.164  35.019  1.00 23.55           N  
ANISOU  942  NE  ARG A  94     2107   4210   2632    719    246   1468       N  
ATOM    943  CZ  ARG A  94      35.279 -18.159  35.849  1.00 24.35           C  
ANISOU  943  CZ  ARG A  94     3906   3048   2298    436  -1420    379       C  
ATOM    944  NH1 ARG A  94      34.386 -19.122  36.089  1.00 39.46           N  
ANISOU  944  NH1 ARG A  94     3733   3266   7995   1083   -176   2508       N  
ATOM    945  NH2 ARG A  94      36.442 -18.178  36.481  1.00 31.24           N  
ANISOU  945  NH2 ARG A  94     3266   5241   3362   2173   -980      9       N  
ATOM    946  N   ASP A  95      35.262 -19.269  29.271  1.00 15.98           N  
ANISOU  946  N   ASP A  95     1283   2485   2302    450    233    680       N  
ATOM    947  CA  ASP A  95      35.906 -20.421  28.638  1.00 17.81           C  
ANISOU  947  CA  ASP A  95     1461   2757   2550    912    129    644       C  
ATOM    948  C   ASP A  95      36.289 -20.205  27.175  1.00 19.22           C  
ANISOU  948  C   ASP A  95     1983   2782   2538   1077    188    514       C  
ATOM    949  O   ASP A  95      36.813 -21.108  26.504  1.00 22.32           O  
ANISOU  949  O   ASP A  95     2320   3119   3044   1393    784    545       O  
ATOM    950  CB  ASP A  95      35.086 -21.702  28.719  1.00 19.56           C  
ANISOU  950  CB  ASP A  95     2047   2558   2827    884    212    405       C  
ATOM    951  CG  ASP A  95      33.776 -21.739  27.956  1.00 17.85           C  
ANISOU  951  CG  ASP A  95     2150   2134   2497    635    191    321       C  
ATOM    952  OD1 ASP A  95      33.492 -20.727  27.267  1.00 17.47           O  
ANISOU  952  OD1 ASP A  95     2080   2218   2340    853    327    307       O  
ATOM    953  OD2 ASP A  95      33.072 -22.760  28.118  1.00 24.93           O  
ANISOU  953  OD2 ASP A  95     2982   2409   4081    130   -255    664       O  
ATOM    954  N   GLY A  96      36.076 -19.040  26.617  1.00 17.90           N  
ANISOU  954  N   GLY A  96     1609   2576   2618    546    722    612       N  
ATOM    955  CA  GLY A  96      36.487 -18.732  25.243  1.00 21.74           C  
ANISOU  955  CA  GLY A  96     1999   3674   2586    977    827    774       C  
ATOM    956  C   GLY A  96      35.733 -19.402  24.130  1.00 22.16           C  
ANISOU  956  C   GLY A  96     2284   3588   2547   1484    690    559       C  
ATOM    957  O   GLY A  96      36.215 -19.335  22.988  1.00 26.10           O  
ANISOU  957  O   GLY A  96     2654   4511   2753   1341   1031     90       O  
ATOM    958  N   ASN A  97      34.568 -19.960  24.372  1.00 21.35           N  
ANISOU  958  N   ASN A  97     2106   3656   2348   1487    388    276       N  
ATOM    959  CA  ASN A  97      33.880 -20.725  23.317  1.00 21.86           C  
ANISOU  959  CA  ASN A  97     2887   3208   2209   1524    710    -48       C  
ATOM    960  C   ASN A  97      32.966 -19.853  22.462  1.00 20.99           C  
ANISOU  960  C   ASN A  97     2711   3422   1840   1264    534    -73       C  
ATOM    961  O   ASN A  97      32.316 -20.429  21.591  1.00 26.22           O  
ANISOU  961  O   ASN A  97     4514   3535   1914   1470     15   -392       O  
ATOM    962  CB  ASN A  97      33.174 -21.935  23.939  1.00 24.85           C  
ANISOU  962  CB  ASN A  97     3483   2905   3055   1533   1042    -50       C  
ATOM    963  CG  ASN A  97      31.832 -21.554  24.547  1.00 20.57           C  
ANISOU  963  CG  ASN A  97     2913   2445   2459   1001    494   -314       C  
ATOM    964  OD1 ASN A  97      31.638 -20.375  24.975  1.00 17.88           O  
ANISOU  964  OD1 ASN A  97     2599   2306   1888   1058    216   -214       O  
ATOM    965  ND2 ASN A  97      30.900 -22.512  24.621  1.00 23.12           N  
ANISOU  965  ND2 ASN A  97     3070   2551   3164    738   -261   -719       N  
ATOM    966  N   GLY A  98      32.971 -18.537  22.683  1.00 19.31           N  
ANISOU  966  N   GLY A  98     2185   3205   1947   1124    608    195       N  
ATOM    967  CA  GLY A  98      32.236 -17.597  21.873  1.00 18.47           C  
ANISOU  967  CA  GLY A  98     2067   3271   1678    708    206     58       C  
ATOM    968  C   GLY A  98      30.782 -17.413  22.320  1.00 15.47           C  
ANISOU  968  C   GLY A  98     2012   2378   1488    601    229    -45       C  
ATOM    969  O   GLY A  98      30.038 -16.711  21.667  1.00 16.46           O  
ANISOU  969  O   GLY A  98     2143   2670   1443    448     51    145       O  
ATOM    970  N   LEU A  99      30.420 -18.008  23.444  1.00 15.63           N  
ANISOU  970  N   LEU A  99     1826   2666   1446    643     67     67       N  
ATOM    971  CA  LEU A  99      29.066 -17.939  23.994  1.00 13.28           C  
ANISOU  971  CA  LEU A  99     1757   2016   1274    540     32     45       C  
ATOM    972  C   LEU A  99      29.151 -17.604  25.460  1.00 13.78           C  
ANISOU  972  C   LEU A  99     1666   2286   1282    783    -31    -31       C  
ATOM    973  O   LEU A  99      29.819 -18.349  26.199  1.00 17.25           O  
ANISOU  973  O   LEU A  99     2758   2515   1282   1394    215    249       O  
ATOM    974  CB  LEU A  99      28.310 -19.248  23.788  1.00 14.88           C  
ANISOU  974  CB  LEU A  99     2160   1745   1748    583    229    -85       C  
ATOM    975  CG  LEU A  99      28.083 -19.739  22.366  1.00 16.59           C  
ANISOU  975  CG  LEU A  99     1884   2513   1906    440     28   -321       C  
ATOM    976  CD1 LEU A  99      27.464 -21.132  22.354  1.00 23.60           C  
ANISOU  976  CD1 LEU A  99     3195   2305   3465    451   -502   -893       C  
ATOM    977  CD2 LEU A  99      27.172 -18.819  21.607  1.00 18.10           C  
ANISOU  977  CD2 LEU A  99     1923   3040   1915    424     26      8       C  
ATOM    978  N  AILE A 100      28.538 -16.516  25.902  0.90 10.61           N  
ANISOU  978  N  AILE A 100     1296   1742    994    255    -37    125       N  
ATOM    979  N  BILE A 100      28.470 -16.544  25.873  0.09 10.69           N  
ANISOU  979  N  BILE A 100     1055   1795   1211    262    -14    105       N  
ATOM    980  CA AILE A 100      28.485 -16.246  27.333  0.90  9.81           C  
ANISOU  980  CA AILE A 100     1142   1653    933    154    -36     88       C  
ATOM    981  CA BILE A 100      28.350 -16.259  27.295  0.09  9.32           C  
ANISOU  981  CA BILE A 100      801   1536   1204    167    -33    110       C  
ATOM    982  C  AILE A 100      27.322 -17.050  27.872  0.90  9.50           C  
ANISOU  982  C  AILE A 100     1237   1444    928    -70   -177    -20       C  
ATOM    983  C  BILE A 100      27.232 -17.098  27.891  0.09  8.80           C  
ANISOU  983  C  BILE A 100      906   1362   1075    -63   -252      3       C  
ATOM    984  O  AILE A 100      26.158 -16.850  27.474  0.90 10.13           O  
ANISOU  984  O  AILE A 100     1305   1502   1043     -3   -210    115       O  
ATOM    985  O  BILE A 100      26.055 -16.970  27.549  0.09  9.08           O  
ANISOU  985  O  BILE A 100      866   1423   1163    -25   -237   -247       O  
ATOM    986  CB AILE A 100      28.273 -14.768  27.612  0.90  9.13           C  
ANISOU  986  CB AILE A 100      932   1553    985    -18    -59    172       C  
ATOM    987  CB BILE A 100      28.064 -14.777  27.575  0.09  9.74           C  
ANISOU  987  CB BILE A 100      953   1393   1354    -98   -238    127       C  
ATOM    988  CG1AILE A 100      29.339 -13.864  27.005  0.90 10.36           C  
ANISOU  988  CG1AILE A 100      930   1873   1134     -5    -91    364       C  
ATOM    989  CG1BILE A 100      29.238 -13.874  27.184  0.09 10.04           C  
ANISOU  989  CG1BILE A 100     1082   1825    907   -244   -205    309       C  
ATOM    990  CG2AILE A 100      28.137 -14.537  29.108  0.90  9.18           C  
ANISOU  990  CG2AILE A 100      880   1538   1070   -211    -26     76       C  
ATOM    991  CG2BILE A 100      27.660 -14.567  29.020  0.09  6.20           C  
ANISOU  991  CG2BILE A 100     -109   1021   1444   -145   -327     65       C  
ATOM    992  CD1AILE A 100      28.949 -12.423  26.938  0.90 10.75           C  
ANISOU  992  CD1AILE A 100     1241   1735   1109   -136   -196    430       C  
ATOM    993  CD1BILE A 100      30.524 -14.681  27.121  0.09 17.34           C  
ANISOU  993  CD1BILE A 100     1137   3066   2385    194    324   1969       C  
ATOM    994  N   SER A 101      27.617 -17.988  28.811  1.00  9.89           N  
ANISOU  994  N   SER A 101     1199   1393   1166     70   -184     49       N  
ATOM    995  CA  SER A 101      26.572 -18.758  29.475  1.00 10.27           C  
ANISOU  995  CA  SER A 101     1393   1349   1158   -150   -287     71       C  
ATOM    996  C   SER A 101      26.039 -18.034  30.674  1.00  9.74           C  
ANISOU  996  C   SER A 101     1246   1387   1068   -240   -230    132       C  
ATOM    997  O   SER A 101      26.607 -17.067  31.197  1.00  9.49           O  
ANISOU  997  O   SER A 101     1092   1401   1114   -300   -188     68       O  
ATOM    998  CB  SER A 101      27.165 -20.108  29.887  1.00 12.14           C  
ANISOU  998  CB  SER A 101     1618   1398   1598   -171   -292     48       C  
ATOM    999  OG  SER A 101      28.049 -19.890  30.983  1.00 11.29           O  
ANISOU  999  OG  SER A 101     1516   1356   1417   -119   -310    269       O  
ATOM   1000  N   ALA A 102      24.902 -18.528  31.178  1.00 10.81           N  
ANISOU 1000  N   ALA A 102     1387   1535   1185   -576   -204     82       N  
ATOM   1001  CA  ALA A 102      24.374 -18.005  32.427  1.00 10.69           C  
ANISOU 1001  CA  ALA A 102     1240   1619   1200   -452   -181    167       C  
ATOM   1002  C   ALA A 102      25.383 -18.132  33.574  1.00 10.27           C  
ANISOU 1002  C   ALA A 102     1139   1620   1142   -513   -111    231       C  
ATOM   1003  O   ALA A 102      25.510 -17.211  34.399  1.00 11.11           O  
ANISOU 1003  O   ALA A 102     1330   1795   1097   -464    -91     94       O  
ATOM   1004  CB  ALA A 102      23.071 -18.711  32.730  1.00 13.52           C  
ANISOU 1004  CB  ALA A 102     1044   2527   1565   -573   -190     10       C  
ATOM   1005  N   ALA A 103      26.078 -19.251  33.669  1.00 11.12           N  
ANISOU 1005  N   ALA A 103     1428   1503   1295   -491   -242    334       N  
ATOM   1006  CA  ALA A 103      27.044 -19.412  34.744  1.00 11.64           C  
ANISOU 1006  CA  ALA A 103     1386   1750   1286   -517   -186    434       C  
ATOM   1007  C   ALA A 103      28.186 -18.414  34.623  1.00  9.77           C  
ANISOU 1007  C   ALA A 103     1248   1340   1124   -223   -212    511       C  
ATOM   1008  O   ALA A 103      28.620 -17.809  35.617  1.00 10.63           O  
ANISOU 1008  O   ALA A 103     1336   1610   1093   -417   -268    425       O  
ATOM   1009  CB  ALA A 103      27.572 -20.847  34.756  1.00 14.26           C  
ANISOU 1009  CB  ALA A 103     1862   1563   1992   -653   -574    729       C  
ATOM   1010  N   GLU A 104      28.647 -18.214  33.408  1.00  9.68           N  
ANISOU 1010  N   GLU A 104     1191   1358   1129   -361   -143    303       N  
ATOM   1011  CA  GLU A 104      29.733 -17.224  33.187  1.00  9.38           C  
ANISOU 1011  CA  GLU A 104      985   1418   1161   -202    -98    364       C  
ATOM   1012  C   GLU A 104      29.282 -15.833  33.521  1.00  9.15           C  
ANISOU 1012  C   GLU A 104     1026   1359   1091   -259   -114    273       C  
ATOM   1013  O   GLU A 104      29.995 -15.072  34.194  1.00 10.22           O  
ANISOU 1013  O   GLU A 104     1244   1476   1164   -422   -297    300       O  
ATOM   1014  CB  GLU A 104      30.184 -17.298  31.725  1.00  9.64           C  
ANISOU 1014  CB  GLU A 104     1132   1332   1199   -152    -15    327       C  
ATOM   1015  CG  GLU A 104      30.993 -18.518  31.406  1.00 11.21           C  
ANISOU 1015  CG  GLU A 104     1193   1549   1518    122     94    486       C  
ATOM   1016  CD  GLU A 104      31.281 -18.734  29.941  1.00 12.08           C  
ANISOU 1016  CD  GLU A 104     1384   1670   1535    381    235    479       C  
ATOM   1017  OE1 GLU A 104      30.537 -18.227  29.084  1.00 11.43           O  
ANISOU 1017  OE1 GLU A 104     1428   1557   1356    204    -25    245       O  
ATOM   1018  OE2 GLU A 104      32.279 -19.456  29.640  1.00 14.06           O  
ANISOU 1018  OE2 GLU A 104     1542   2084   1717    649    202    510       O  
ATOM   1019  N   LEU A 105      28.110 -15.456  33.036  1.00  9.14           N  
ANISOU 1019  N   LEU A 105     1126   1273   1075   -221   -248    201       N  
ATOM   1020  CA  LEU A 105      27.597 -14.119  33.312  1.00  9.41           C  
ANISOU 1020  CA  LEU A 105     1242   1290   1042   -239   -204    222       C  
ATOM   1021  C   LEU A 105      27.441 -13.890  34.810  1.00  9.46           C  
ANISOU 1021  C   LEU A 105     1179   1309   1105   -260   -245    177       C  
ATOM   1022  O   LEU A 105      27.818 -12.847  35.342  1.00 10.16           O  
ANISOU 1022  O   LEU A 105     1523   1273   1064   -319   -332    243       O  
ATOM   1023  CB  LEU A 105      26.258 -13.914  32.583  1.00  9.91           C  
ANISOU 1023  CB  LEU A 105     1334   1433    999   -132   -220    189       C  
ATOM   1024  CG  LEU A 105      25.613 -12.573  32.772  1.00 10.76           C  
ANISOU 1024  CG  LEU A 105     1403   1625   1058     54   -141    231       C  
ATOM   1025  CD1 LEU A 105      26.540 -11.423  32.394  1.00 11.78           C  
ANISOU 1025  CD1 LEU A 105     1617   1493   1365    -77   -113    312       C  
ATOM   1026  CD2 LEU A 105      24.310 -12.489  31.952  1.00 12.76           C  
ANISOU 1026  CD2 LEU A 105     1580   1713   1555    -10   -506    216       C  
ATOM   1027  N   ARG A 106      26.895 -14.883  35.508  1.00  9.22           N  
ANISOU 1027  N   ARG A 106     1224   1234   1043   -231   -173    136       N  
ATOM   1028  CA  ARG A 106      26.719 -14.722  36.953  1.00  9.65           C  
ANISOU 1028  CA  ARG A 106     1425   1214   1027   -229   -228    160       C  
ATOM   1029  C   ARG A 106      28.056 -14.566  37.655  1.00  9.45           C  
ANISOU 1029  C   ARG A 106     1550   1164    878   -290   -212    202       C  
ATOM   1030  O   ARG A 106      28.210 -13.758  38.572  1.00 10.64           O  
ANISOU 1030  O   ARG A 106     1605   1354   1083   -341   -257     38       O  
ATOM   1031  CB  ARG A 106      25.870 -15.881  37.488  1.00  9.92           C  
ANISOU 1031  CB  ARG A 106     1580   1118   1071   -245   -105     45       C  
ATOM   1032  CG  ARG A 106      25.440 -15.634  38.915  1.00 11.16           C  
ANISOU 1032  CG  ARG A 106     1712   1444   1085   -441   -125     16       C  
ATOM   1033  CD  ARG A 106      24.342 -16.590  39.346  1.00 11.19           C  
ANISOU 1033  CD  ARG A 106     1669   1292   1290   -276     83     91       C  
ATOM   1034  NE  ARG A 106      24.571 -17.943  39.133  1.00 12.34           N  
ANISOU 1034  NE  ARG A 106     1841   1334   1514   -297   -164    218       N  
ATOM   1035  CZ  ARG A 106      25.209 -18.729  39.967  1.00 12.70           C  
ANISOU 1035  CZ  ARG A 106     1914   1616   1296      1    -77    248       C  
ATOM   1036  NH1 ARG A 106      25.783 -18.243  41.075  1.00 13.78           N  
ANISOU 1036  NH1 ARG A 106     1710   2065   1461    -61   -148    267       N  
ATOM   1037  NH2 ARG A 106      25.363 -20.040  39.717  1.00 18.51           N  
ANISOU 1037  NH2 ARG A 106     3315   1395   2324   -102   -613    491       N  
ATOM   1038  N  AHIS A 107      29.019 -15.368  37.207  0.34  8.71           N  
ANISOU 1038  N  AHIS A 107     1338   1275    698   -394   -167    278       N  
ATOM   1039  N  BHIS A 107      29.054 -15.396  37.312  0.66 10.87           N  
ANISOU 1039  N  BHIS A 107     1564   1243   1322   -137   -313     89       N  
ATOM   1040  CA AHIS A 107      30.341 -15.358  37.814  0.34 10.82           C  
ANISOU 1040  CA AHIS A 107     1341   1812    957   -526   -254     99       C  
ATOM   1041  CA BHIS A 107      30.352 -15.252  37.989  0.66 10.92           C  
ANISOU 1041  CA BHIS A 107     1699   1429   1020    -78   -407    103       C  
ATOM   1042  C  AHIS A 107      31.077 -14.031  37.693  0.34 12.08           C  
ANISOU 1042  C  AHIS A 107     1434   1933   1225   -608   -250    220       C  
ATOM   1043  C  BHIS A 107      30.956 -13.870  37.775  0.66 11.22           C  
ANISOU 1043  C  BHIS A 107     1529   1508   1228   -114   -458    152       C  
ATOM   1044  O  AHIS A 107      31.706 -13.553  38.647  0.34 10.34           O  
ANISOU 1044  O  AHIS A 107     1185   1313   1430   -333   -574    536       O  
ATOM   1045  O  BHIS A 107      31.380 -13.167  38.696  0.66 11.35           O  
ANISOU 1045  O  BHIS A 107     1425   1552   1338     32   -565    -22       O  
ATOM   1046  CB AHIS A 107      31.184 -16.457  37.142  0.34 11.82           C  
ANISOU 1046  CB AHIS A 107     1495   1992   1002    -49   -738    143       C  
ATOM   1047  CB BHIS A 107      31.290 -16.355  37.492  0.66 11.21           C  
ANISOU 1047  CB BHIS A 107     1582   1529   1148   -119   -360      0       C  
ATOM   1048  CG AHIS A 107      32.441 -16.649  37.944  0.34 14.84           C  
ANISOU 1048  CG AHIS A 107     1867   1761   2012   -231  -1208    429       C  
ATOM   1049  CG BHIS A 107      32.739 -16.176  37.885  0.66 13.34           C  
ANISOU 1049  CG BHIS A 107     1600   1881   1588   -106   -497    320       C  
ATOM   1050  ND1AHIS A 107      33.504 -15.796  37.976  0.34 15.41           N  
ANISOU 1050  ND1AHIS A 107     1653   2031   2172   -184  -1192    460       N  
ATOM   1051  ND1BHIS A 107      33.159 -16.647  39.130  0.66 16.57           N  
ANISOU 1051  ND1BHIS A 107     1780   2900   1615    246   -608    392       N  
ATOM   1052  CD2AHIS A 107      32.745 -17.648  38.805  0.34 17.00           C  
ANISOU 1052  CD2AHIS A 107     2150   1900   2408   -208  -1576    617       C  
ATOM   1053  CD2BHIS A 107      33.826 -15.605  37.308  0.66 17.50           C  
ANISOU 1053  CD2BHIS A 107     1734   2369   2546   -538   -846    932       C  
ATOM   1054  CE1AHIS A 107      34.432 -16.266  38.805  0.34 16.26           C  
ANISOU 1054  CE1AHIS A 107     1611   2672   1897   -226   -997    917       C  
ATOM   1055  CE1BHIS A 107      34.453 -16.356  39.258  0.66 16.43           C  
ANISOU 1055  CE1BHIS A 107     1833   2463   1946    236   -754     -2       C  
ATOM   1056  NE2AHIS A 107      33.988 -17.399  39.330  0.34 16.81           N  
ANISOU 1056  NE2AHIS A 107     1992   2032   2363   -207  -1290    511       N  
ATOM   1057  NE2BHIS A 107      34.900 -15.723  38.175  0.66 16.67           N  
ANISOU 1057  NE2BHIS A 107     1648   2367   2319     -8   -711    140       N  
ATOM   1058  N   VAL A 108      30.977 -13.409  36.516  1.00 11.16           N  
ANISOU 1058  N   VAL A 108     1430   1596   1215   -411   -345     99       N  
ATOM   1059  CA  VAL A 108      31.596 -12.123  36.256  1.00 11.53           C  
ANISOU 1059  CA  VAL A 108     1309   1750   1322   -500   -195    150       C  
ATOM   1060  C   VAL A 108      30.769 -11.023  36.930  1.00 11.56           C  
ANISOU 1060  C   VAL A 108     1444   1521   1426   -458   -223    204       C  
ATOM   1061  O   VAL A 108      31.342 -10.062  37.513  1.00 12.76           O  
ANISOU 1061  O   VAL A 108     1533   1794   1522   -642   -118     14       O  
ATOM   1062  CB  VAL A 108      31.797 -11.899  34.755  1.00 13.24           C  
ANISOU 1062  CB  VAL A 108     1521   2127   1382   -551   -220    254       C  
ATOM   1063  CG1 VAL A 108      32.393 -10.525  34.485  1.00 16.48           C  
ANISOU 1063  CG1 VAL A 108     2430   2328   1502   -907   -419    539       C  
ATOM   1064  CG2 VAL A 108      32.707 -13.012  34.228  1.00 15.11           C  
ANISOU 1064  CG2 VAL A 108     1690   2541   1509   -577    -41    -57       C  
ATOM   1065  N   MET A 109      29.428 -11.088  36.943  1.00 10.64           N  
ANISOU 1065  N   MET A 109     1487   1281   1275   -457   -182    227       N  
ATOM   1066  CA  MET A 109      28.666 -10.046  37.624  1.00 10.52           C  
ANISOU 1066  CA  MET A 109     1643   1102   1250   -457   -138    182       C  
ATOM   1067  C   MET A 109      28.987 -10.007  39.125  1.00 11.37           C  
ANISOU 1067  C   MET A 109     1689   1371   1259   -723   -241    127       C  
ATOM   1068  O   MET A 109      29.093  -8.902  39.674  1.00 11.98           O  
ANISOU 1068  O   MET A 109     1696   1448   1409   -648   -246    136       O  
ATOM   1069  CB  MET A 109      27.164 -10.222  37.416  1.00 11.30           C  
ANISOU 1069  CB  MET A 109     1620   1337   1336   -334   -275    175       C  
ATOM   1070  CG  MET A 109      26.722  -9.953  35.979  1.00 12.45           C  
ANISOU 1070  CG  MET A 109     1683   1642   1404   -247   -365    382       C  
ATOM   1071  SD  MET A 109      27.062  -8.306  35.343  1.00 16.69           S  
ANISOU 1071  SD  MET A 109     2467   1701   2175   -164   -516    573       S  
ATOM   1072  CE  MET A 109      25.967  -7.417  36.328  1.00 21.47           C  
ANISOU 1072  CE  MET A 109     4936   1711   1510   -375    532    174       C  
ATOM   1073  N   THR A 110      29.187 -11.175  39.754  1.00 11.08           N  
ANISOU 1073  N   THR A 110     1682   1393   1136   -691   -235    228       N  
ATOM   1074  CA  THR A 110      29.596 -11.157  41.171  1.00 11.80           C  
ANISOU 1074  CA  THR A 110     1691   1629   1161   -519   -261     55       C  
ATOM   1075  C   THR A 110      30.881 -10.390  41.314  1.00 11.50           C  
ANISOU 1075  C   THR A 110     1652   1411   1308   -441   -369    165       C  
ATOM   1076  O   THR A 110      31.060  -9.583  42.258  1.00 12.59           O  
ANISOU 1076  O   THR A 110     1734   1601   1450   -441   -469    143       O  
ATOM   1077  CB  THR A 110      29.715 -12.619  41.665  1.00 14.17           C  
ANISOU 1077  CB  THR A 110     2201   1864   1320   -894   -481    515       C  
ATOM   1078  OG1 THR A 110      28.415 -13.216  41.608  1.00 18.55           O  
ANISOU 1078  OG1 THR A 110     2584   2643   1822  -1402   -510    633       O  
ATOM   1079  CG2 THR A 110      30.144 -12.649  43.113  1.00 21.50           C  
ANISOU 1079  CG2 THR A 110     3647   2947   1576  -1607  -1122    922       C  
ATOM   1080  N  AASN A 111      31.845 -10.634  40.457  0.72 11.72           N  
ANISOU 1080  N  AASN A 111     1473   1537   1443   -487   -484    125       N  
ATOM   1081  N  BASN A 111      31.778 -10.642  40.375  0.28 11.41           N  
ANISOU 1081  N  BASN A 111     1573   1090   1671   -117   -238    416       N  
ATOM   1082  CA AASN A 111      33.111  -9.834  40.563  0.72 10.91           C  
ANISOU 1082  CA AASN A 111     1423   1157   1564   -216   -409   -124       C  
ATOM   1083  CA BASN A 111      33.114 -10.070  40.212  0.28 11.93           C  
ANISOU 1083  CA BASN A 111     1564   1283   1687   -165   -293    -49       C  
ATOM   1084  C  AASN A 111      32.887  -8.368  40.312  0.72 10.52           C  
ANISOU 1084  C  AASN A 111     1163   1266   1567   -204   -281    187       C  
ATOM   1085  C  BASN A 111      33.055  -8.580  39.879  0.28 11.88           C  
ANISOU 1085  C  BASN A 111     1444   1471   1600   -322   -262    550       C  
ATOM   1086  O  AASN A 111      33.646  -7.556  40.907  0.72 12.14           O  
ANISOU 1086  O  AASN A 111     1534   1135   1946   -241   -566    -71       O  
ATOM   1087  O  BASN A 111      34.093  -7.890  39.997  0.28 15.67           O  
ANISOU 1087  O  BASN A 111     1583   1638   2733   -484   -401    -54       O  
ATOM   1088  CB AASN A 111      34.138 -10.489  39.672  0.72 12.73           C  
ANISOU 1088  CB AASN A 111     1267   1689   1880   -169   -507   -402       C  
ATOM   1089  CB BASN A 111      33.896 -10.846  39.145  0.28 15.73           C  
ANISOU 1089  CB BASN A 111     1653   2340   1984    128   -155   -302       C  
ATOM   1090  CG AASN A 111      34.671 -11.785  40.267  0.72 15.99           C  
ANISOU 1090  CG AASN A 111     1335   1742   2997    198   -650   -333       C  
ATOM   1091  CG BASN A 111      35.370 -10.896  39.477  0.28 19.65           C  
ANISOU 1091  CG BASN A 111     1390   2986   3089   -487    243   -218       C  
ATOM   1092  OD1AASN A 111      35.190 -12.663  39.560  0.72 19.42           O  
ANISOU 1092  OD1AASN A 111     1830   2230   3317    324   -760   -719       O  
ATOM   1093  OD1BASN A 111      35.791 -10.030  40.232  0.28 36.84           O  
ANISOU 1093  OD1BASN A 111     3093   5201   5705  -2046   -725  -1532       O  
ATOM   1094  ND2AASN A 111      34.605 -12.004  41.573  0.72 15.05           N  
ANISOU 1094  ND2AASN A 111     1571   1204   2942    413  -1201   -353       N  
ATOM   1095  ND2BASN A 111      36.139 -11.837  38.963  0.28 29.48           N  
ANISOU 1095  ND2BASN A 111     2146   5504   3552   1186   1321    360       N  
ATOM   1096  N   LEU A 112      31.937  -8.018  39.487  1.00 12.23           N  
ANISOU 1096  N   LEU A 112     1596   1354   1696   -309   -546    194       N  
ATOM   1097  CA  LEU A 112      31.610  -6.611  39.254  1.00 12.32           C  
ANISOU 1097  CA  LEU A 112     1326   1393   1964   -377   -453    531       C  
ATOM   1098  C   LEU A 112      30.797  -6.029  40.410  1.00 12.84           C  
ANISOU 1098  C   LEU A 112     1651   1205   2023   -262   -513    352       C  
ATOM   1099  O   LEU A 112      30.411  -4.857  40.312  1.00 15.85           O  
ANISOU 1099  O   LEU A 112     2048   1466   2510    -87   -700    268       O  
ATOM   1100  CB  LEU A 112      30.911  -6.438  37.907  1.00 13.96           C  
ANISOU 1100  CB  LEU A 112     1828   1567   1908   -731   -522    582       C  
ATOM   1101  CG  LEU A 112      31.781  -6.800  36.683  1.00 16.37           C  
ANISOU 1101  CG  LEU A 112     2403   1921   1895   -839   -328    600       C  
ATOM   1102  CD1 LEU A 112      30.943  -6.765  35.414  1.00 17.70           C  
ANISOU 1102  CD1 LEU A 112     2493   2376   1855   -242   -263    522       C  
ATOM   1103  CD2 LEU A 112      33.015  -5.878  36.584  1.00 23.78           C  
ANISOU 1103  CD2 LEU A 112     2959   3862   2215  -1852    241    270       C  
ATOM   1104  N   GLY A 113      30.573  -6.805  41.478  1.00 12.63           N  
ANISOU 1104  N   GLY A 113     1447   1319   2031   -538    -90    113       N  
ATOM   1105  CA  GLY A 113      29.920  -6.340  42.661  1.00 11.96           C  
ANISOU 1105  CA  GLY A 113     1384   1136   2024   -368   -373    -98       C  
ATOM   1106  C   GLY A 113      28.448  -6.612  42.751  1.00 10.77           C  
ANISOU 1106  C   GLY A 113     1437    846   1808   -400   -153    -89       C  
ATOM   1107  O   GLY A 113      27.837  -6.080  43.670  1.00 12.21           O  
ANISOU 1107  O   GLY A 113     1610   1251   1779   -263   -344   -325       O  
ATOM   1108  N   GLU A 114      27.901  -7.412  41.862  1.00 10.83           N  
ANISOU 1108  N   GLU A 114     1457    999   1659   -404   -156   -117       N  
ATOM   1109  CA  GLU A 114      26.501  -7.716  41.763  1.00 10.90           C  
ANISOU 1109  CA  GLU A 114     1500   1094   1547   -485   -201    -33       C  
ATOM   1110  C   GLU A 114      26.278  -9.211  41.970  1.00 10.53           C  
ANISOU 1110  C   GLU A 114     1542   1085   1373   -444   -186    -50       C  
ATOM   1111  O   GLU A 114      26.577  -9.996  41.073  1.00 12.62           O  
ANISOU 1111  O   GLU A 114     1878   1342   1576   -612    201   -378       O  
ATOM   1112  CB  GLU A 114      25.964  -7.282  40.420  1.00 12.25           C  
ANISOU 1112  CB  GLU A 114     1808   1359   1488   -336   -258     -4       C  
ATOM   1113  CG  GLU A 114      26.014  -5.799  40.224  1.00 13.47           C  
ANISOU 1113  CG  GLU A 114     2053   1422   1642   -224   -460     65       C  
ATOM   1114  CD  GLU A 114      25.043  -5.069  41.132  1.00 13.60           C  
ANISOU 1114  CD  GLU A 114     2043   1242   1883   -347   -355     89       C  
ATOM   1115  OE1 GLU A 114      25.117  -3.832  41.051  1.00 20.40           O  
ANISOU 1115  OE1 GLU A 114     3909   1235   2607     -2    399    186       O  
ATOM   1116  OE2 GLU A 114      24.254  -5.684  41.843  1.00 15.09           O  
ANISOU 1116  OE2 GLU A 114     1562   1634   2536   -212   -206     97       O  
ATOM   1117  N  ALYS A 115      25.682  -9.508  43.109  0.67 10.04           N  
ANISOU 1117  N  ALYS A 115     1489    997   1330   -278    -79    -66       N  
ATOM   1118  N  BLYS A 115      25.797  -9.656  43.134  0.33  8.64           N  
ANISOU 1118  N  BLYS A 115     1343    805   1135   -204   -413   -159       N  
ATOM   1119  CA ALYS A 115      25.405 -10.896  43.486  0.67 10.41           C  
ANISOU 1119  CA ALYS A 115     1692    959   1306   -327   -183    -21       C  
ATOM   1120  CA BLYS A 115      25.539 -11.059  43.429  0.33  8.47           C  
ANISOU 1120  CA BLYS A 115     1218    692   1309    133   -208     15       C  
ATOM   1121  C  ALYS A 115      23.973 -11.208  43.054  0.67 10.09           C  
ANISOU 1121  C  ALYS A 115     1661   1001   1172   -373     64   -337       C  
ATOM   1122  C  BLYS A 115      24.137 -11.435  42.948  0.33  6.77           C  
ANISOU 1122  C  BLYS A 115     1295    372    906     25    -77    180       C  
ATOM   1123  O  ALYS A 115      23.013 -10.824  43.730  0.67 12.99           O  
ANISOU 1123  O  ALYS A 115     1756   1448   1732   -231    197   -559       O  
ATOM   1124  O  BLYS A 115      23.202 -11.044  43.648  0.33  5.93           O  
ANISOU 1124  O  BLYS A 115     1110    307    835   -172   -284     37       O  
ATOM   1125  CB ALYS A 115      25.733 -11.038  44.979  0.67 11.16           C  
ANISOU 1125  CB ALYS A 115     1927   1002   1311      9   -143    -66       C  
ATOM   1126  CB BLYS A 115      25.545 -11.421  44.920  0.33 10.13           C  
ANISOU 1126  CB BLYS A 115     1638    944   1269   -217   -392    -59       C  
ATOM   1127  CG ALYS A 115      25.739 -12.481  45.437  0.67 11.67           C  
ANISOU 1127  CG ALYS A 115     1761   1024   1650   -301   -353    128       C  
ATOM   1128  CG BLYS A 115      26.870 -11.226  45.599  0.33  9.76           C  
ANISOU 1128  CG BLYS A 115     1449   1046   1215   -422   -207    174       C  
ATOM   1129  CD ALYS A 115      26.931 -13.306  45.018  0.67 13.90           C  
ANISOU 1129  CD ALYS A 115     2532   1009   1739     63     30    259       C  
ATOM   1130  CD BLYS A 115      26.906 -11.726  47.045  0.33  9.94           C  
ANISOU 1130  CD BLYS A 115     1464   1081   1233     19   -168    211       C  
ATOM   1131  CE ALYS A 115      26.858 -14.688  45.624  0.67 14.31           C  
ANISOU 1131  CE ALYS A 115     3151    841   1447    -53    -26     46       C  
ATOM   1132  CE BLYS A 115      28.299 -11.434  47.614  0.33 19.02           C  
ANISOU 1132  CE BLYS A 115     1911   3209   2106   -738   -816   1103       C  
ATOM   1133  NZ ALYS A 115      25.554 -15.404  45.345  0.67 17.14           N  
ANISOU 1133  NZ ALYS A 115     3780    702   2029   -360   -726   -209       N  
ATOM   1134  NZ BLYS A 115      28.347 -11.456  49.093  0.33 20.50           N  
ANISOU 1134  NZ BLYS A 115     1611   4085   2091   -675   -790    795       N  
ATOM   1135  N  ALEU A 116      23.812 -11.835  41.890  0.58  8.48           N  
ANISOU 1135  N  ALEU A 116     1437    726   1059   -335     69    -41       N  
ATOM   1136  N  BLEU A 116      23.988 -12.078  41.810  0.41  8.29           N  
ANISOU 1136  N  BLEU A 116     1441    783    927     50    -95    -25       N  
ATOM   1137  CA ALEU A 116      22.532 -12.052  41.240  0.58  8.35           C  
ANISOU 1137  CA ALEU A 116     1499    673   1002   -261     47    -18       C  
ATOM   1138  CA BLEU A 116      22.736 -12.250  41.087  0.41  8.35           C  
ANISOU 1138  CA BLEU A 116     1168    989   1017   -116    153    -69       C  
ATOM   1139  C  ALEU A 116      22.152 -13.522  41.314  0.58  7.76           C  
ANISOU 1139  C  ALEU A 116     1429    699    821   -276   -183    -41       C  
ATOM   1140  C  BLEU A 116      22.175 -13.641  41.227  0.41  9.99           C  
ANISOU 1140  C  BLEU A 116     1465   1053   1278   -307    293     44       C  
ATOM   1141  O  ALEU A 116      23.021 -14.432  41.331  0.58 10.11           O  
ANISOU 1141  O  ALEU A 116     1507    660   1672   -227   -115      7       O  
ATOM   1142  O  BLEU A 116      22.897 -14.663  41.261  0.41  9.40           O  
ANISOU 1142  O  BLEU A 116     1342   1057   1171   -307    -61    102       O  
ATOM   1143  CB ALEU A 116      22.543 -11.623  39.777  0.58  8.33           C  
ANISOU 1143  CB ALEU A 116     1322    824   1020   -259    171     -1       C  
ATOM   1144  CB BLEU A 116      22.961 -11.902  39.614  0.41  7.50           C  
ANISOU 1144  CB BLEU A 116     1088    782    979    -21    -15    -60       C  
ATOM   1145  CG ALEU A 116      22.967 -10.178  39.508  0.58 10.10           C  
ANISOU 1145  CG ALEU A 116     1634    887   1318   -207    207    208       C  
ATOM   1146  CG BLEU A 116      23.448 -10.473  39.341  0.41 10.45           C  
ANISOU 1146  CG BLEU A 116     2058    802   1112    -42    207    -20       C  
ATOM   1147  CD1ALEU A 116      23.186  -9.995  38.021  0.58 12.13           C  
ANISOU 1147  CD1ALEU A 116     1982   1199   1428    -88    259    483       C  
ATOM   1148  CD1BLEU A 116      23.731 -10.307  37.853  0.41 11.53           C  
ANISOU 1148  CD1BLEU A 116     1581   1712   1089   -145   -239    496       C  
ATOM   1149  CD2ALEU A 116      21.892  -9.242  40.010  0.58 12.56           C  
ANISOU 1149  CD2ALEU A 116     2014    801   1958    -52    487    282       C  
ATOM   1150  CD2BLEU A 116      22.427  -9.452  39.821  0.41 12.10           C  
ANISOU 1150  CD2BLEU A 116     1872    637   2088     -8    367    391       C  
ATOM   1151  N   THR A 117      20.835 -13.742  41.308  1.00  8.50           N  
ANISOU 1151  N   THR A 117     1503    777    949   -253   -177     97       N  
ATOM   1152  CA  THR A 117      20.290 -15.094  41.300  1.00  8.53           C  
ANISOU 1152  CA  THR A 117     1681    727    832   -396   -219    129       C  
ATOM   1153  C   THR A 117      20.243 -15.648  39.897  1.00  8.10           C  
ANISOU 1153  C   THR A 117     1394    824    860   -165   -208     28       C  
ATOM   1154  O   THR A 117      20.332 -14.919  38.892  1.00  8.77           O  
ANISOU 1154  O   THR A 117     1602    868    861   -305   -203    126       O  
ATOM   1155  CB  THR A 117      18.875 -15.127  41.899  1.00  8.96           C  
ANISOU 1155  CB  THR A 117     1758    796    851   -301   -145    143       C  
ATOM   1156  OG1 THR A 117      17.973 -14.530  40.989  1.00  9.85           O  
ANISOU 1156  OG1 THR A 117     1572    940   1231   -183    -98     54       O  
ATOM   1157  CG2 THR A 117      18.784 -14.480  43.253  1.00 10.72           C  
ANISOU 1157  CG2 THR A 117     2395    642   1034   -377    148    -15       C  
ATOM   1158  N   ASP A 118      20.031 -16.969  39.790  1.00  8.45           N  
ANISOU 1158  N   ASP A 118     1547    805    859   -324   -265     43       N  
ATOM   1159  CA  ASP A 118      19.826 -17.590  38.493  1.00  8.68           C  
ANISOU 1159  CA  ASP A 118     1519    977    802   -298   -152     20       C  
ATOM   1160  C   ASP A 118      18.645 -16.980  37.745  1.00  9.14           C  
ANISOU 1160  C   ASP A 118     1518   1012    943   -307   -288    -20       C  
ATOM   1161  O   ASP A 118      18.727 -16.776  36.534  1.00 10.44           O  
ANISOU 1161  O   ASP A 118     1811   1385    771   -196   -224     -3       O  
ATOM   1162  CB  ASP A 118      19.624 -19.082  38.653  1.00  9.07           C  
ANISOU 1162  CB  ASP A 118     1432    860   1153   -218   -213   -171       C  
ATOM   1163  CG  ASP A 118      20.854 -19.832  39.074  1.00  9.39           C  
ANISOU 1163  CG  ASP A 118     1383    959   1228   -147   -159   -199       C  
ATOM   1164  OD1 ASP A 118      21.989 -19.372  38.903  1.00 11.58           O  
ANISOU 1164  OD1 ASP A 118     1410   1469   1521   -351   -111   -154       O  
ATOM   1165  OD2 ASP A 118      20.610 -20.969  39.618  1.00 11.36           O  
ANISOU 1165  OD2 ASP A 118     1506   1003   1807    -53   -131     30       O  
ATOM   1166  N  AASP A 119      17.580 -16.656  38.457  0.34  8.94           N  
ANISOU 1166  N  AASP A 119     1346   1263    787   -291   -375     83       N  
ATOM   1167  N  BASP A 119      17.556 -16.687  38.419  0.66  8.99           N  
ANISOU 1167  N  BASP A 119     1574    994    849   -301   -255     51       N  
ATOM   1168  CA AASP A 119      16.379 -16.069  37.854  0.34  8.53           C  
ANISOU 1168  CA AASP A 119     1329   1254    658   -368   -324    173       C  
ATOM   1169  CA BASP A 119      16.428 -16.100  37.662  0.66 10.11           C  
ANISOU 1169  CA BASP A 119     1673   1024   1146   -150   -222    173       C  
ATOM   1170  C  AASP A 119      16.650 -14.679  37.279  0.34  8.66           C  
ANISOU 1170  C  AASP A 119     1060   1284    948   -181    -91    179       C  
ATOM   1171  C  BASP A 119      16.837 -14.731  37.126  0.66  8.54           C  
ANISOU 1171  C  BASP A 119     1176   1058   1012    -65   -257     26       C  
ATOM   1172  O  AASP A 119      16.090 -14.294  36.242  0.34  6.57           O  
ANISOU 1172  O  AASP A 119      537   1190    769    102    288    236       O  
ATOM   1173  O  BASP A 119      16.543 -14.410  35.961  0.66  8.09           O  
ANISOU 1173  O  BASP A 119      974   1327    772     53    102    151       O  
ATOM   1174  CB AASP A 119      15.227 -15.989  38.848  0.34  8.93           C  
ANISOU 1174  CB AASP A 119     1304   1075   1013    -79   -215    454       C  
ATOM   1175  CB BASP A 119      15.180 -16.037  38.509  0.66 11.81           C  
ANISOU 1175  CB BASP A 119     1420   1699   1366   -480   -278    215       C  
ATOM   1176  CG AASP A 119      14.437 -17.290  38.953  0.34  9.03           C  
ANISOU 1176  CG AASP A 119     1129   1488    815   -353   -139    -82       C  
ATOM   1177  CG BASP A 119      13.933 -15.929  37.672  0.66 18.19           C  
ANISOU 1177  CG BASP A 119     1685   3622   1605  -1125   -541    288       C  
ATOM   1178  OD1AASP A 119      14.661 -18.205  38.150  0.34 10.97           O  
ANISOU 1178  OD1AASP A 119     1409   1445   1314   -450    184   -151       O  
ATOM   1179  OD1BASP A 119      13.105 -15.097  37.998  0.66 32.94           O  
ANISOU 1179  OD1BASP A 119     3448   3365   5703    883  -3170    142       O  
ATOM   1180  OD2AASP A 119      13.596 -17.271  39.874  0.34 10.12           O  
ANISOU 1180  OD2AASP A 119     1037   1778   1030   -393    -47     13       O  
ATOM   1181  OD2BASP A 119      13.752 -16.725  36.715  0.66 27.56           O  
ANISOU 1181  OD2BASP A 119     3507   5035   1930  -2534   -831   -228       O  
ATOM   1182  N   GLU A 120      17.489 -13.909  37.951  1.00  9.37           N  
ANISOU 1182  N   GLU A 120     1717    909    933   -207   -145    129       N  
ATOM   1183  CA  GLU A 120      17.926 -12.592  37.475  1.00  9.37           C  
ANISOU 1183  CA  GLU A 120     1689    905    965    -75    -29    130       C  
ATOM   1184  C   GLU A 120      18.822 -12.696  36.260  1.00  8.87           C  
ANISOU 1184  C   GLU A 120     1414   1029    925   -137   -106    100       C  
ATOM   1185  O   GLU A 120      18.641 -11.972  35.268  1.00  9.62           O  
ANISOU 1185  O   GLU A 120     1455   1107   1094    -41    -10    270       O  
ATOM   1186  CB  GLU A 120      18.610 -11.837  38.627  1.00  9.10           C  
ANISOU 1186  CB  GLU A 120     1555    891   1011   -140     -9     87       C  
ATOM   1187  CG  GLU A 120      17.670 -11.346  39.719  1.00 10.18           C  
ANISOU 1187  CG  GLU A 120     1835    935   1097     21    -29     37       C  
ATOM   1188  CD  GLU A 120      18.350 -10.772  40.944  1.00  9.58           C  
ANISOU 1188  CD  GLU A 120     1841    695   1105    -53    133      6       C  
ATOM   1189  OE1 GLU A 120      19.423 -11.212  41.330  1.00 10.95           O  
ANISOU 1189  OE1 GLU A 120     2148    886   1127    -54   -282     58       O  
ATOM   1190  OE2 GLU A 120      17.738  -9.834  41.506  1.00 13.57           O  
ANISOU 1190  OE2 GLU A 120     2406   1224   1526    232   -124   -317       O  
ATOM   1191  N   VAL A 121      19.812 -13.583  36.330  1.00  8.69           N  
ANISOU 1191  N   VAL A 121     1449   1009    846   -127   -224    128       N  
ATOM   1192  CA  VAL A 121      20.704 -13.740  35.193  1.00  9.39           C  
ANISOU 1192  CA  VAL A 121     1531   1073    962   -144   -172     18       C  
ATOM   1193  C   VAL A 121      19.965 -14.294  33.983  1.00  9.26           C  
ANISOU 1193  C   VAL A 121     1366   1211    941   -130   -271    147       C  
ATOM   1194  O   VAL A 121      20.222 -13.877  32.835  1.00  9.56           O  
ANISOU 1194  O   VAL A 121     1315   1401    918   -186   -204    140       O  
ATOM   1195  CB  VAL A 121      21.917 -14.604  35.620  1.00 11.33           C  
ANISOU 1195  CB  VAL A 121     1448   1815   1042     31   -359    -75       C  
ATOM   1196  CG1 VAL A 121      22.753 -14.972  34.456  1.00 13.67           C  
ANISOU 1196  CG1 VAL A 121     1449   2579   1165     22    -45     10       C  
ATOM   1197  CG2 VAL A 121      22.759 -13.878  36.666  1.00 13.14           C  
ANISOU 1197  CG2 VAL A 121     1701   1894   1399    -61   -396   -289       C  
ATOM   1198  N   ASP A 122      19.062 -15.232  34.195  1.00  9.34           N  
ANISOU 1198  N   ASP A 122     1407   1264    877   -183   -199     55       N  
ATOM   1199  CA  ASP A 122      18.298 -15.786  33.106  1.00  9.65           C  
ANISOU 1199  CA  ASP A 122     1417   1402    850   -176   -260      9       C  
ATOM   1200  C   ASP A 122      17.495 -14.706  32.394  1.00  9.66           C  
ANISOU 1200  C   ASP A 122     1210   1510    949   -217   -212     96       C  
ATOM   1201  O   ASP A 122      17.394 -14.682  31.167  1.00 10.63           O  
ANISOU 1201  O   ASP A 122     1567   1644    826   -199   -304     75       O  
ATOM   1202  CB  ASP A 122      17.414 -16.926  33.603  1.00 11.21           C  
ANISOU 1202  CB  ASP A 122     1696   1602    960   -469   -417     54       C  
ATOM   1203  CG  ASP A 122      18.238 -18.161  33.995  1.00 14.82           C  
ANISOU 1203  CG  ASP A 122     2127   1765   1740   -284   -336    419       C  
ATOM   1204  OD1 ASP A 122      19.452 -18.301  33.757  1.00 17.52           O  
ANISOU 1204  OD1 ASP A 122     2130   2204   2323   -101   -198    150       O  
ATOM   1205  OD2 ASP A 122      17.598 -19.076  34.573  1.00 18.06           O  
ANISOU 1205  OD2 ASP A 122     2635   1845   2381   -200    -82    500       O  
ATOM   1206  N   GLU A 123      16.897 -13.795  33.152  1.00 10.14           N  
ANISOU 1206  N   GLU A 123     1560   1452    843    -87   -185    191       N  
ATOM   1207  CA  GLU A 123      16.165 -12.682  32.536  1.00 10.75           C  
ANISOU 1207  CA  GLU A 123     1437   1616   1030    -25   -212    309       C  
ATOM   1208  C   GLU A 123      17.113 -11.798  31.722  1.00 10.38           C  
ANISOU 1208  C   GLU A 123     1516   1440    987    -13   -134    212       C  
ATOM   1209  O   GLU A 123      16.767 -11.369  30.613  1.00 11.66           O  
ANISOU 1209  O   GLU A 123     1768   1752    910     33   -252    329       O  
ATOM   1210  CB  GLU A 123      15.441 -11.887  33.623  1.00 11.79           C  
ANISOU 1210  CB  GLU A 123     1454   1922   1105     93   -128    207       C  
ATOM   1211  CG  GLU A 123      14.717 -10.684  33.072  1.00 16.77           C  
ANISOU 1211  CG  GLU A 123     2039   2478   1855    708   -291    366       C  
ATOM   1212  CD  GLU A 123      13.848  -9.963  34.069  1.00 20.94           C  
ANISOU 1212  CD  GLU A 123     2158   2554   3245    571    453    202       C  
ATOM   1213  OE1 GLU A 123      13.739  -8.701  33.917  1.00 23.44           O  
ANISOU 1213  OE1 GLU A 123     3861   2549   2496    891     24    -38       O  
ATOM   1214  OE2 GLU A 123      13.260 -10.690  34.905  1.00 21.23           O  
ANISOU 1214  OE2 GLU A 123     2265   2986   2817    244    552    -57       O  
ATOM   1215  N   MET A 124      18.320 -11.480  32.251  1.00 10.27           N  
ANISOU 1215  N   MET A 124     1523   1445    933   -132   -139    129       N  
ATOM   1216  CA  MET A 124      19.295 -10.710  31.464  1.00 10.60           C  
ANISOU 1216  CA  MET A 124     1477   1583    966    -88    -92    234       C  
ATOM   1217  C   MET A 124      19.601 -11.382  30.173  1.00 10.70           C  
ANISOU 1217  C   MET A 124     1387   1733    947   -222   -243    208       C  
ATOM   1218  O   MET A 124      19.688 -10.779  29.097  1.00 12.78           O  
ANISOU 1218  O   MET A 124     1782   2089    985   -433   -155    420       O  
ATOM   1219  CB  MET A 124      20.545 -10.506  32.328  1.00 11.74           C  
ANISOU 1219  CB  MET A 124     1752   1634   1076   -378   -225     71       C  
ATOM   1220  CG  MET A 124      20.388  -9.623  33.508  1.00 14.03           C  
ANISOU 1220  CG  MET A 124     2692   1603   1038   -353   -222    103       C  
ATOM   1221  SD  MET A 124      21.899  -9.653  34.558  1.00 18.86           S  
ANISOU 1221  SD  MET A 124     3500   1891   1775   -332  -1137    -50       S  
ATOM   1222  CE  MET A 124      23.026  -8.794  33.470  1.00 23.40           C  
ANISOU 1222  CE  MET A 124     2240   3864   2787     91   -345     44       C  
ATOM   1223  N  AILE A 125      19.834 -12.693  30.203  0.61 10.10           N  
ANISOU 1223  N  AILE A 125     1368   1735    733   -272   -281     54       N  
ATOM   1224  N  BILE A 125      19.827 -12.699  30.209  0.39 10.71           N  
ANISOU 1224  N  BILE A 125     1526   1804    741   -119    -89    118       N  
ATOM   1225  CA AILE A 125      20.125 -13.328  28.930  0.61 11.16           C  
ANISOU 1225  CA AILE A 125     1442   1970    829      3   -306     -9       C  
ATOM   1226  CA BILE A 125      20.127 -13.570  29.096  0.39 11.33           C  
ANISOU 1226  CA BILE A 125     1314   2091    901   -193    -64    -98       C  
ATOM   1227  C  AILE A 125      18.904 -13.332  28.029  0.61  9.53           C  
ANISOU 1227  C  AILE A 125     1206   1720    697     34   -185    189       C  
ATOM   1228  C  BILE A 125      18.965 -13.605  28.090  0.39 11.16           C  
ANISOU 1228  C  BILE A 125     1332   1916    992   -208   -224    166       C  
ATOM   1229  O  AILE A 125      19.047 -13.021  26.836  0.61  9.15           O  
ANISOU 1229  O  AILE A 125     1372   1413    692    128   -136     52       O  
ATOM   1230  O  BILE A 125      19.182 -13.580  26.873  0.39 12.04           O  
ANISOU 1230  O  BILE A 125     1571   1983   1022    -64   -144    -55       O  
ATOM   1231  CB AILE A 125      20.625 -14.745  29.177  0.61 11.25           C  
ANISOU 1231  CB AILE A 125     1419   2110    745    276   -297     53       C  
ATOM   1232  CB BILE A 125      20.420 -15.020  29.517  0.39 11.22           C  
ANISOU 1232  CB BILE A 125     1344   2185    732    190   -243   -259       C  
ATOM   1233  CG1AILE A 125      22.000 -14.610  29.850  0.61 12.96           C  
ANISOU 1233  CG1AILE A 125     1332   2767    823    483   -157   -303       C  
ATOM   1234  CG1BILE A 125      21.666 -15.223  30.391  0.39 14.53           C  
ANISOU 1234  CG1BILE A 125     1409   3104   1008     57   -409     34       C  
ATOM   1235  CG2AILE A 125      20.648 -15.581  27.925  0.61 13.92           C  
ANISOU 1235  CG2AILE A 125     2168   2214    908    539   -560   -147       C  
ATOM   1236  CG2BILE A 125      20.445 -15.900  28.265  0.39 14.25           C  
ANISOU 1236  CG2BILE A 125     1996   2525    895    449   -308   -490       C  
ATOM   1237  CD1AILE A 125      22.517 -15.974  30.335  0.61 20.00           C  
ANISOU 1237  CD1AILE A 125     2484   3304   1811   1591  -1069   -659       C  
ATOM   1238  CD1BILE A 125      22.964 -15.183  29.569  0.39 21.27           C  
ANISOU 1238  CD1BILE A 125     1242   5294   1545   -537   -377   -559       C  
ATOM   1239  N   ARG A 126      17.716 -13.660  28.551  1.00 11.02           N  
ANISOU 1239  N   ARG A 126     1442   1914    828   -353   -236    126       N  
ATOM   1240  CA  ARG A 126      16.539 -13.658  27.653  1.00 11.30           C  
ANISOU 1240  CA  ARG A 126     1292   2008    994   -175   -281     11       C  
ATOM   1241  C   ARG A 126      16.372 -12.342  26.918  1.00 11.97           C  
ANISOU 1241  C   ARG A 126     1423   2166    958     16   -154    142       C  
ATOM   1242  O   ARG A 126      16.005 -12.337  25.748  1.00 12.83           O  
ANISOU 1242  O   ARG A 126     1459   2474    944     10   -321     94       O  
ATOM   1243  CB  ARG A 126      15.257 -13.974  28.392  1.00 14.12           C  
ANISOU 1243  CB  ARG A 126     1548   2625   1191   -376   -120    419       C  
ATOM   1244  CG  ARG A 126      15.102 -15.397  28.805  1.00 15.95           C  
ANISOU 1244  CG  ARG A 126     1929   2532   1598   -523   -383    482       C  
ATOM   1245  CD  ARG A 126      13.690 -15.825  29.053  1.00 18.87           C  
ANISOU 1245  CD  ARG A 126     1796   2688   2685   -593   -445    833       C  
ATOM   1246  NE  ARG A 126      12.984 -14.957  29.956  1.00 18.33           N  
ANISOU 1246  NE  ARG A 126     1769   2964   2230   -240   -676   1045       N  
ATOM   1247  CZ  ARG A 126      13.124 -14.986  31.285  1.00 20.06           C  
ANISOU 1247  CZ  ARG A 126     1906   3475   2241   -387   -963    984       C  
ATOM   1248  NH1 ARG A 126      13.908 -15.819  31.897  1.00 29.89           N  
ANISOU 1248  NH1 ARG A 126     2194   5535   3628   -210  -1305   2480       N  
ATOM   1249  NH2 ARG A 126      12.387 -14.116  31.958  1.00 31.46           N  
ANISOU 1249  NH2 ARG A 126     2952   5615   3386     68  -1055  -1068       N  
ATOM   1250  N   GLU A 127      16.633 -11.202  27.589  1.00 11.44           N  
ANISOU 1250  N   GLU A 127     1428   2074    844     42    -59    183       N  
ATOM   1251  CA  GLU A 127      16.505  -9.895  26.987  1.00 13.24           C  
ANISOU 1251  CA  GLU A 127     1628   2141   1260    273      0    337       C  
ATOM   1252  C   GLU A 127      17.405  -9.749  25.780  1.00 13.55           C  
ANISOU 1252  C   GLU A 127     1966   1986   1197      9    106    308       C  
ATOM   1253  O   GLU A 127      17.067  -9.057  24.784  1.00 17.27           O  
ANISOU 1253  O   GLU A 127     2493   2761   1309    174   -148    583       O  
ATOM   1254  CB  GLU A 127      16.871  -8.811  28.021  1.00 15.78           C  
ANISOU 1254  CB  GLU A 127     2572   1971   1454    532    187     92       C  
ATOM   1255  CG  GLU A 127      15.854  -8.616  29.107  1.00 15.70           C  
ANISOU 1255  CG  GLU A 127     2113   2334   1519   -144    163    205       C  
ATOM   1256  CD  GLU A 127      14.651  -7.870  28.655  1.00 18.96           C  
ANISOU 1256  CD  GLU A 127     1720   3046   2438   -190    -58    217       C  
ATOM   1257  OE1 GLU A 127      13.882  -8.665  27.984  1.00 26.39           O  
ANISOU 1257  OE1 GLU A 127     2645   4687   2693  -1486   -621    633       O  
ATOM   1258  OE2 GLU A 127      14.388  -6.681  28.943  1.00 30.29           O  
ANISOU 1258  OE2 GLU A 127     2614   2599   6295    179    139    869       O  
ATOM   1259  N   ALA A 128      18.597 -10.326  25.833  1.00 12.83           N  
ANISOU 1259  N   ALA A 128     1803   1987   1087    -80    135    202       N  
ATOM   1260  CA  ALA A 128      19.595 -10.149  24.779  1.00 13.38           C  
ANISOU 1260  CA  ALA A 128     1954   1918   1213   -348    221    175       C  
ATOM   1261  C   ALA A 128      19.624 -11.312  23.775  1.00 11.41           C  
ANISOU 1261  C   ALA A 128     1402   2003    930    -93    -99    243       C  
ATOM   1262  O   ALA A 128      20.235 -11.144  22.712  1.00 12.07           O  
ANISOU 1262  O   ALA A 128     1515   2101    969   -236    -59    218       O  
ATOM   1263  CB  ALA A 128      20.994  -9.986  25.432  1.00 16.33           C  
ANISOU 1263  CB  ALA A 128     2132   2718   1355  -1054    220   -220       C  
ATOM   1264  N   ASP A 129      19.001 -12.427  24.107  1.00 11.64           N  
ANISOU 1264  N   ASP A 129     1533   2046    842   -188     53     18       N  
ATOM   1265  CA  ASP A 129      19.113 -13.634  23.321  1.00 11.01           C  
ANISOU 1265  CA  ASP A 129     1259   2126    798   -304    -58    -67       C  
ATOM   1266  C   ASP A 129      18.226 -13.501  22.097  1.00 12.37           C  
ANISOU 1266  C   ASP A 129     1298   2513    887    -61    -36    108       C  
ATOM   1267  O   ASP A 129      17.025 -13.191  22.230  1.00 15.64           O  
ANISOU 1267  O   ASP A 129     1276   3231   1436     74    -62    118       O  
ATOM   1268  CB  ASP A 129      18.673 -14.832  24.154  1.00 11.77           C  
ANISOU 1268  CB  ASP A 129     1522   2064    886   -136     45     58       C  
ATOM   1269  CG  ASP A 129      19.058 -16.181  23.593  1.00 11.96           C  
ANISOU 1269  CG  ASP A 129     1394   2097   1052   -386    -62    -65       C  
ATOM   1270  OD1 ASP A 129      19.882 -16.270  22.638  1.00 11.78           O  
ANISOU 1270  OD1 ASP A 129     1426   2034   1017   -252    -67   -129       O  
ATOM   1271  OD2 ASP A 129      18.564 -17.201  24.118  1.00 12.90           O  
ANISOU 1271  OD2 ASP A 129     1434   1937   1531   -176    208     69       O  
ATOM   1272  N   ILE A 130      18.800 -13.687  20.919  1.00 11.70           N  
ANISOU 1272  N   ILE A 130     1034   2500    911   -201   -137     77       N  
ATOM   1273  CA  ILE A 130      18.120 -13.580  19.661  1.00 12.45           C  
ANISOU 1273  CA  ILE A 130     1185   2604    941    -48   -242     39       C  
ATOM   1274  C   ILE A 130      17.918 -14.959  19.049  1.00 12.82           C  
ANISOU 1274  C   ILE A 130     1288   2694    888   -118   -271    -39       C  
ATOM   1275  O   ILE A 130      16.827 -15.278  18.579  1.00 15.29           O  
ANISOU 1275  O   ILE A 130     1283   3077   1449   -150   -387   -238       O  
ATOM   1276  CB  ILE A 130      18.873 -12.655  18.666  1.00 12.83           C  
ANISOU 1276  CB  ILE A 130     1397   2580    897     36   -255     95       C  
ATOM   1277  CG1 ILE A 130      18.906 -11.247  19.213  1.00 14.12           C  
ANISOU 1277  CG1 ILE A 130     1640   2532   1194     19   -330    197       C  
ATOM   1278  CG2 ILE A 130      18.216 -12.756  17.261  1.00 15.31           C  
ANISOU 1278  CG2 ILE A 130     1875   2911   1029     55   -444    228       C  
ATOM   1279  CD1 ILE A 130      19.792 -10.306  18.470  1.00 15.40           C  
ANISOU 1279  CD1 ILE A 130     1998   2427   1427     97   -120    363       C  
ATOM   1280  N   ASP A 131      18.923 -15.781  19.040  1.00 12.60           N  
ANISOU 1280  N   ASP A 131     1225   2656    908   -117   -110   -105       N  
ATOM   1281  CA  ASP A 131      18.873 -17.126  18.450  1.00 14.06           C  
ANISOU 1281  CA  ASP A 131     1516   2822   1004    -95   -239   -261       C  
ATOM   1282  C   ASP A 131      18.258 -18.155  19.387  1.00 14.22           C  
ANISOU 1282  C   ASP A 131     1526   2593   1284   -263   -272   -391       C  
ATOM   1283  O   ASP A 131      17.993 -19.266  18.966  1.00 18.56           O  
ANISOU 1283  O   ASP A 131     2315   3034   1703   -697   -253   -546       O  
ATOM   1284  CB  ASP A 131      20.223 -17.553  17.893  1.00 13.91           C  
ANISOU 1284  CB  ASP A 131     1674   2547   1065    -47   -176   -345       C  
ATOM   1285  CG  ASP A 131      21.295 -17.707  18.949  1.00 13.35           C  
ANISOU 1285  CG  ASP A 131     1515   2446   1111   -196   -183   -314       C  
ATOM   1286  OD1 ASP A 131      20.947 -17.777  20.151  1.00 12.41           O  
ANISOU 1286  OD1 ASP A 131     1513   2163   1041   -285    -93   -181       O  
ATOM   1287  OD2 ASP A 131      22.477 -17.704  18.551  1.00 16.01           O  
ANISOU 1287  OD2 ASP A 131     1640   3397   1046    126    -31   -196       O  
ATOM   1288  N   GLY A 132      17.952 -17.786  20.631  1.00 13.64           N  
ANISOU 1288  N   GLY A 132     1442   2501   1238   -283    -81    -73       N  
ATOM   1289  CA  GLY A 132      17.216 -18.664  21.533  1.00 14.95           C  
ANISOU 1289  CA  GLY A 132     1386   2522   1772   -303     35    -70       C  
ATOM   1290  C   GLY A 132      18.030 -19.773  22.180  1.00 15.58           C  
ANISOU 1290  C   GLY A 132     1580   2743   1598   -572   -304    287       C  
ATOM   1291  O   GLY A 132      17.408 -20.621  22.799  1.00 17.82           O  
ANISOU 1291  O   GLY A 132     1995   2706   2071   -818   -123    177       O  
ATOM   1292  N   ASP A 133      19.346 -19.753  22.096  1.00 14.03           N  
ANISOU 1292  N   ASP A 133     1465   2282   1584   -422   -267    -10       N  
ATOM   1293  CA  ASP A 133      20.161 -20.822  22.653  1.00 14.21           C  
ANISOU 1293  CA  ASP A 133     1764   2009   1628   -264   -203   -406       C  
ATOM   1294  C   ASP A 133      20.470 -20.622  24.149  1.00 13.90           C  
ANISOU 1294  C   ASP A 133     1878   1823   1582   -339   -287   -102       C  
ATOM   1295  O   ASP A 133      21.230 -21.404  24.724  1.00 15.49           O  
ANISOU 1295  O   ASP A 133     2127   1760   1997   -351   -487     63       O  
ATOM   1296  CB  ASP A 133      21.453 -20.983  21.843  1.00 14.67           C  
ANISOU 1296  CB  ASP A 133     1976   1748   1851   -186     17   -409       C  
ATOM   1297  CG  ASP A 133      22.472 -19.875  22.040  1.00 12.97           C  
ANISOU 1297  CG  ASP A 133     1730   1848   1351   -119    -90   -178       C  
ATOM   1298  OD1 ASP A 133      22.101 -18.863  22.674  1.00 12.15           O  
ANISOU 1298  OD1 ASP A 133     1616   1733   1266   -196   -125    -51       O  
ATOM   1299  OD2 ASP A 133      23.634 -20.050  21.609  1.00 15.35           O  
ANISOU 1299  OD2 ASP A 133     1785   2108   1939     -8    -21   -300       O  
ATOM   1300  N   GLY A 134      19.882 -19.609  24.801  1.00 12.75           N  
ANISOU 1300  N   GLY A 134     1598   1935   1310   -472    -40    -82       N  
ATOM   1301  CA  GLY A 134      20.151 -19.402  26.217  1.00 12.69           C  
ANISOU 1301  CA  GLY A 134     1583   1917   1322   -497   -100    128       C  
ATOM   1302  C   GLY A 134      21.520 -18.950  26.582  1.00 11.23           C  
ANISOU 1302  C   GLY A 134     1419   1624   1223   -145   -105     45       C  
ATOM   1303  O   GLY A 134      21.878 -18.934  27.740  1.00 12.48           O  
ANISOU 1303  O   GLY A 134     1684   1857   1201   -167   -159    256       O  
ATOM   1304  N   HIS A 135      22.262 -18.487  25.583  1.00 10.65           N  
ANISOU 1304  N   HIS A 135     1339   1587   1120   -232   -222     17       N  
ATOM   1305  CA  HIS A 135      23.592 -17.964  25.708  1.00 10.74           C  
ANISOU 1305  CA  HIS A 135     1312   1593   1177   -131    -69    -17       C  
ATOM   1306  C   HIS A 135      23.663 -16.625  24.943  1.00  9.80           C  
ANISOU 1306  C   HIS A 135     1166   1600    956    -73   -177     56       C  
ATOM   1307  O   HIS A 135      22.819 -16.377  24.083  1.00 10.62           O  
ANISOU 1307  O   HIS A 135     1254   1724   1055   -233   -223    -16       O  
ATOM   1308  CB  HIS A 135      24.632 -18.908  25.112  1.00 11.75           C  
ANISOU 1308  CB  HIS A 135     1440   1728   1298     33    -46     21       C  
ATOM   1309  CG  HIS A 135      24.770 -20.221  25.825  1.00 12.54           C  
ANISOU 1309  CG  HIS A 135     1920   1560   1283     72   -292   -228       C  
ATOM   1310  ND1 HIS A 135      23.791 -21.162  25.867  1.00 14.75           N  
ANISOU 1310  ND1 HIS A 135     2202   1657   1744   -111   -290   -104       N  
ATOM   1311  CD2 HIS A 135      25.839 -20.693  26.494  1.00 14.36           C  
ANISOU 1311  CD2 HIS A 135     2071   1883   1501    227   -289     73       C  
ATOM   1312  CE1 HIS A 135      24.204 -22.213  26.567  1.00 17.51           C  
ANISOU 1312  CE1 HIS A 135     3048   1433   2174   -103   -672   -170       C  
ATOM   1313  NE2 HIS A 135      25.443 -21.954  26.963  1.00 16.16           N  
ANISOU 1313  NE2 HIS A 135     2601   1590   1950    346   -233    -63       N  
ATOM   1314  N  AILE A 136      24.678 -15.819  25.205  0.71  9.88           N  
ANISOU 1314  N  AILE A 136     1105   1630   1019    -59   -133     82       N  
ATOM   1315  N  BILE A 136      24.655 -15.791  25.209  0.29 10.01           N  
ANISOU 1315  N  BILE A 136     1221   1621    961   -106   -226     92       N  
ATOM   1316  CA AILE A 136      24.876 -14.565  24.480  0.71  9.61           C  
ANISOU 1316  CA AILE A 136     1006   1685    961    -33   -239    141       C  
ATOM   1317  CA BILE A 136      24.838 -14.521  24.513  0.29  9.64           C  
ANISOU 1317  CA BILE A 136     1100   1555   1009     42    -96     67       C  
ATOM   1318  C  AILE A 136      26.127 -14.728  23.623  0.71  9.93           C  
ANISOU 1318  C  AILE A 136     1114   1643   1017   -236   -190     95       C  
ATOM   1319  C  BILE A 136      26.084 -14.587  23.633  0.29  8.42           C  
ANISOU 1319  C  BILE A 136      995   1191   1014    170   -199     93       C  
ATOM   1320  O  AILE A 136      27.245 -14.925  24.143  0.71 10.63           O  
ANISOU 1320  O  AILE A 136     1054   2032    952     21    -45     63       O  
ATOM   1321  O  BILE A 136      27.214 -14.600  24.154  0.29  8.58           O  
ANISOU 1321  O  BILE A 136     1025    951   1286    -39   -319    186       O  
ATOM   1322  CB AILE A 136      24.931 -13.381  25.453  0.71 10.39           C  
ANISOU 1322  CB AILE A 136     1190   1580   1176     80   -317    101       C  
ATOM   1323  CB BILE A 136      24.957 -13.349  25.507  0.29  9.21           C  
ANISOU 1323  CB BILE A 136      990   1630    880   -147     21     76       C  
ATOM   1324  CG1AILE A 136      23.610 -13.285  26.242  0.71 10.88           C  
ANISOU 1324  CG1AILE A 136     1501   1555   1078    -43   -146     18       C  
ATOM   1325  CG1BILE A 136      23.850 -13.334  26.562  0.29  9.71           C  
ANISOU 1325  CG1BILE A 136      948   1877    865   -174    -10     78       C  
ATOM   1326  CG2AILE A 136      25.280 -12.101  24.690  0.71 10.63           C  
ANISOU 1326  CG2AILE A 136     1412   1689    937   -129   -388     39       C  
ATOM   1327  CG2BILE A 136      25.042 -12.036  24.732  0.29 12.86           C  
ANISOU 1327  CG2BILE A 136     1418   1427   2041    483   1140    241       C  
ATOM   1328  CD1AILE A 136      22.353 -13.198  25.337  0.71 14.80           C  
ANISOU 1328  CD1AILE A 136     1205   2553   1867    357    -89     -2       C  
ATOM   1329  CD1BILE A 136      23.945 -12.201  27.562  0.29 10.99           C  
ANISOU 1329  CD1BILE A 136     1234   1987    956    155    -65    -53       C  
ATOM   1330  N   ASN A 137      25.925 -14.621  22.319  1.00 10.13           N  
ANISOU 1330  N   ASN A 137     1033   1800   1017     33   -131    -13       N  
ATOM   1331  CA  ASN A 137      27.063 -14.577  21.388  1.00 10.65           C  
ANISOU 1331  CA  ASN A 137     1165   1804   1077     90    -61    -16       C  
ATOM   1332  C   ASN A 137      27.506 -13.130  21.175  1.00 10.20           C  
ANISOU 1332  C   ASN A 137     1041   1890    945     61   -112     49       C  
ATOM   1333  O   ASN A 137      26.960 -12.179  21.722  1.00 10.48           O  
ANISOU 1333  O   ASN A 137     1125   1860    998     19   -110     78       O  
ATOM   1334  CB  ASN A 137      26.753 -15.363  20.120  1.00 12.30           C  
ANISOU 1334  CB  ASN A 137     1358   2076   1241    -43    -19   -224       C  
ATOM   1335  CG  ASN A 137      25.835 -14.630  19.160  1.00 12.91           C  
ANISOU 1335  CG  ASN A 137     1689   2125   1090   -141   -184   -114       C  
ATOM   1336  OD1 ASN A 137      25.464 -13.484  19.300  1.00 13.08           O  
ANISOU 1336  OD1 ASN A 137     1566   2251   1151     54   -260    -75       O  
ATOM   1337  ND2 ASN A 137      25.456 -15.404  18.142  1.00 17.67           N  
ANISOU 1337  ND2 ASN A 137     2309   2860   1545    139   -534   -693       N  
ATOM   1338  N  ATYR A 138      28.601 -12.898  20.410  0.62 11.24           N  
ANISOU 1338  N  ATYR A 138     1183   2035   1052    -43    -54     77       N  
ATOM   1339  N  BTYR A 138      28.549 -13.012  20.355  0.38 12.52           N  
ANISOU 1339  N  BTYR A 138     1456   2144   1155     66    213    250       N  
ATOM   1340  CA ATYR A 138      29.139 -11.533  20.318  0.62 11.57           C  
ANISOU 1340  CA ATYR A 138     1049   2051   1298    -16     56    169       C  
ATOM   1341  CA BTYR A 138      29.168 -11.698  20.210  0.38 11.47           C  
ANISOU 1341  CA BTYR A 138     1330   2176    852      8    104    123       C  
ATOM   1342  C  ATYR A 138      28.145 -10.598  19.645  0.62 11.03           C  
ANISOU 1342  C  ATYR A 138     1147   2133    909     -4     89    124       C  
ATOM   1343  C  BTYR A 138      28.202 -10.683  19.631  0.38 11.23           C  
ANISOU 1343  C  BTYR A 138     1280   2147    838    -75     90    173       C  
ATOM   1344  O  ATYR A 138      27.965  -9.464  20.090  0.62 11.46           O  
ANISOU 1344  O  ATYR A 138     1273   1935   1146    -76   -160    239       O  
ATOM   1345  O  BTYR A 138      28.052  -9.563  20.129  0.38 11.67           O  
ANISOU 1345  O  BTYR A 138     1071   2203   1160     -9      3     43       O  
ATOM   1346  CB ATYR A 138      30.504 -11.526  19.611  0.62 11.58           C  
ANISOU 1346  CB ATYR A 138     1295   1989   1118    123    343    162       C  
ATOM   1347  CB BTYR A 138      30.454 -11.923  19.397  0.38 12.51           C  
ANISOU 1347  CB BTYR A 138     1468   2117   1167     20    337     25       C  
ATOM   1348  CG ATYR A 138      31.102 -10.134  19.453  0.62 11.63           C  
ANISOU 1348  CG ATYR A 138     1105   2074   1241    -57     80    272       C  
ATOM   1349  CG BTYR A 138      31.088 -10.573  19.136  0.38 11.75           C  
ANISOU 1349  CG BTYR A 138     1328   2116   1019     90    206     75       C  
ATOM   1350  CD1ATYR A 138      31.630  -9.407  20.494  0.62 13.43           C  
ANISOU 1350  CD1ATYR A 138     1225   2595   1283   -407    -73    377       C  
ATOM   1351  CD1BTYR A 138      31.582  -9.811  20.168  0.38 12.75           C  
ANISOU 1351  CD1BTYR A 138     1159   2630   1056   -423   -121    347       C  
ATOM   1352  CD2ATYR A 138      31.129  -9.501  18.213  0.62 12.62           C  
ANISOU 1352  CD2ATYR A 138     1609   2125   1060     59    432    110       C  
ATOM   1353  CD2BTYR A 138      31.143 -10.115  17.828  0.38 13.80           C  
ANISOU 1353  CD2BTYR A 138     1558   2671   1015   -328    208    183       C  
ATOM   1354  CE1ATYR A 138      32.169  -8.146  20.363  0.62 13.62           C  
ANISOU 1354  CE1ATYR A 138     1243   2548   1383   -428    -14     45       C  
ATOM   1355  CE1BTYR A 138      32.164  -8.570  19.956  0.38 12.13           C  
ANISOU 1355  CE1BTYR A 138      793   2461   1354   -192    -49    297       C  
ATOM   1356  CE2ATYR A 138      31.657  -8.235  18.055  0.62 13.84           C  
ANISOU 1356  CE2ATYR A 138     1526   2416   1316   -111     27    610       C  
ATOM   1357  CE2BTYR A 138      31.714  -8.882  17.616  0.38 13.76           C  
ANISOU 1357  CE2BTYR A 138     1422   2657   1149   -199    455    225       C  
ATOM   1358  CZ ATYR A 138      32.174  -7.567  19.119  0.62 14.20           C  
ANISOU 1358  CZ ATYR A 138     1715   1940   1739     22    292    208       C  
ATOM   1359  CZ BTYR A 138      32.200  -8.134  18.649  0.38 12.44           C  
ANISOU 1359  CZ BTYR A 138      965   2358   1402    -72    179    326       C  
ATOM   1360  OH ATYR A 138      32.691  -6.313  18.944  0.62 18.58           O  
ANISOU 1360  OH ATYR A 138     1676   2304   3079   -366   -188    640       O  
ATOM   1361  OH BTYR A 138      32.771  -6.914  18.382  0.38 17.62           O  
ANISOU 1361  OH BTYR A 138     2008   2544   2142   -469    -58    678       O  
ATOM   1362  N   GLU A 139      27.507 -11.037  18.565  1.00 12.23           N  
ANISOU 1362  N   GLU A 139     1441   2190   1016      9    -49    113       N  
ATOM   1363  CA  GLU A 139      26.509 -10.119  17.954  1.00 12.62           C  
ANISOU 1363  CA  GLU A 139     1501   2276   1019    -68   -134    169       C  
ATOM   1364  C   GLU A 139      25.437  -9.725  18.941  1.00 11.70           C  
ANISOU 1364  C   GLU A 139     1247   2167   1033    -55   -235    244       C  
ATOM   1365  O   GLU A 139      25.050  -8.564  18.981  1.00 12.48           O  
ANISOU 1365  O   GLU A 139     1528   2072   1142    -17   -242    282       O  
ATOM   1366  CB  GLU A 139      25.898 -10.791  16.718  1.00 14.60           C  
ANISOU 1366  CB  GLU A 139     1886   2691    970   -303   -216    170       C  
ATOM   1367  CG  GLU A 139      24.786  -9.935  16.138  1.00 16.29           C  
ANISOU 1367  CG  GLU A 139     2256   2801   1134   -226   -563    239       C  
ATOM   1368  CD  GLU A 139      24.171 -10.532  14.873  1.00 18.94           C  
ANISOU 1368  CD  GLU A 139     2547   3223   1427   -485   -787    161       C  
ATOM   1369  OE1 GLU A 139      24.709 -11.550  14.351  1.00 25.46           O  
ANISOU 1369  OE1 GLU A 139     4119   3939   1616    227  -1436   -615       O  
ATOM   1370  OE2 GLU A 139      23.200  -9.930  14.412  1.00 22.86           O  
ANISOU 1370  OE2 GLU A 139     2687   4150   1850   -266  -1126     68       O  
ATOM   1371  N   GLU A 140      24.904 -10.690  19.703  1.00 10.87           N  
ANISOU 1371  N   GLU A 140     1266   1935    929    -70   -254     50       N  
ATOM   1372  CA  GLU A 140      23.851 -10.374  20.685  1.00 10.88           C  
ANISOU 1372  CA  GLU A 140     1143   1999    991   -129   -189    121       C  
ATOM   1373  C   GLU A 140      24.372  -9.404  21.732  1.00 10.19           C  
ANISOU 1373  C   GLU A 140     1018   1801   1051    -87   -102    180       C  
ATOM   1374  O   GLU A 140      23.643  -8.506  22.185  1.00 11.84           O  
ANISOU 1374  O   GLU A 140     1197   1900   1402     41   -231     64       O  
ATOM   1375  CB  GLU A 140      23.353 -11.674  21.314  1.00 10.64           C  
ANISOU 1375  CB  GLU A 140     1226   1806   1008    -31   -197     44       C  
ATOM   1376  CG  GLU A 140      22.596 -12.575  20.327  1.00 11.64           C  
ANISOU 1376  CG  GLU A 140     1200   2147   1077   -245   -441    245       C  
ATOM   1377  CD  GLU A 140      22.381 -13.972  20.819  1.00 10.30           C  
ANISOU 1377  CD  GLU A 140     1115   1978    820   -160    -83     49       C  
ATOM   1378  OE1 GLU A 140      23.155 -14.459  21.708  1.00 11.28           O  
ANISOU 1378  OE1 GLU A 140     1139   2077   1070   -129   -256    149       O  
ATOM   1379  OE2 GLU A 140      21.417 -14.652  20.364  1.00 11.33           O  
ANISOU 1379  OE2 GLU A 140     1211   2125    969   -223   -256     38       O  
ATOM   1380  N  APHE A 141      25.615  -9.612  22.151  0.53 10.23           N  
ANISOU 1380  N  APHE A 141     1117   1732   1039    -51   -206    109       N  
ATOM   1381  N  BPHE A 141      25.607  -9.618  22.156  0.47 10.37           N  
ANISOU 1381  N  BPHE A 141     1119   1825    997    -23   -185     41       N  
ATOM   1382  CA APHE A 141      26.249  -8.753  23.133  0.53 10.57           C  
ANISOU 1382  CA APHE A 141     1089   1908   1020   -110   -118     72       C  
ATOM   1383  CA BPHE A 141      26.241  -8.740  23.123  0.47 10.57           C  
ANISOU 1383  CA BPHE A 141     1108   1858   1051   -148    -89     37       C  
ATOM   1384  C  APHE A 141      26.373  -7.309  22.641  0.53 11.42           C  
ANISOU 1384  C  APHE A 141     1172   1918   1249   -217   -155     59       C  
ATOM   1385  C  BPHE A 141      26.305  -7.302  22.613  0.47 12.26           C  
ANISOU 1385  C  BPHE A 141     1368   1904   1386   -173      7    111       C  
ATOM   1386  O  APHE A 141      26.015  -6.358  23.321  0.53 13.10           O  
ANISOU 1386  O  APHE A 141     1620   1880   1478   -219    -69    -26       O  
ATOM   1387  O  BPHE A 141      25.855  -6.355  23.241  0.47 12.32           O  
ANISOU 1387  O  BPHE A 141     1492   1845   1344    -43   -153    153       O  
ATOM   1388  CB APHE A 141      27.604  -9.328  23.501  0.53 10.77           C  
ANISOU 1388  CB APHE A 141     1028   2187    879    -99    -67    115       C  
ATOM   1389  CB BPHE A 141      27.620  -9.284  23.420  0.47 11.51           C  
ANISOU 1389  CB BPHE A 141     1086   2057   1231   -139   -153    -58       C  
ATOM   1390  CG APHE A 141      28.401  -8.512  24.494  0.53 11.51           C  
ANISOU 1390  CG APHE A 141     1101   2261   1009   -302    -54    116       C  
ATOM   1391  CG BPHE A 141      28.434  -8.569  24.470  0.47 11.83           C  
ANISOU 1391  CG BPHE A 141     1129   2219   1148   -415    -69     78       C  
ATOM   1392  CD1APHE A 141      28.037  -8.501  25.850  0.53 11.44           C  
ANISOU 1392  CD1APHE A 141     1019   2253   1076   -438    112   -239       C  
ATOM   1393  CD1BPHE A 141      28.329  -8.946  25.817  0.47 11.36           C  
ANISOU 1393  CD1BPHE A 141     1417   1772   1127     32    -96     86       C  
ATOM   1394  CD2APHE A 141      29.506  -7.770  24.084  0.53 10.93           C  
ANISOU 1394  CD2APHE A 141     1115   1976   1063   -133    120     63       C  
ATOM   1395  CD2BPHE A 141      29.306  -7.547  24.112  0.47 12.44           C  
ANISOU 1395  CD2BPHE A 141     1308   1987   1432   -355   -135    160       C  
ATOM   1396  CE1APHE A 141      28.782  -7.762  26.760  0.53 14.05           C  
ANISOU 1396  CE1APHE A 141     1349   2760   1231   -476   -239   -206       C  
ATOM   1397  CE1BPHE A 141      29.101  -8.312  26.769  0.47 13.87           C  
ANISOU 1397  CE1BPHE A 141     1919   2161   1190   -269   -244    165       C  
ATOM   1398  CE2APHE A 141      30.239  -7.050  25.021  0.53 13.97           C  
ANISOU 1398  CE2APHE A 141     1058   2719   1532   -386   -187     13       C  
ATOM   1399  CE2BPHE A 141      30.067  -6.916  25.091  0.47 14.08           C  
ANISOU 1399  CE2BPHE A 141     1140   2693   1515   -680    -60    104       C  
ATOM   1400  CZ APHE A 141      29.871  -7.038  26.339  0.53 15.57           C  
ANISOU 1400  CZ APHE A 141     1401   3062   1452   -757   -332   -460       C  
ATOM   1401  CZ BPHE A 141      29.951  -7.303  26.403  0.47 15.41           C  
ANISOU 1401  CZ BPHE A 141     1560   2893   1402   -575    -71    -61       C  
ATOM   1402  N   VAL A 142      26.880  -7.163  21.407  1.00 11.84           N  
ANISOU 1402  N   VAL A 142     1214   1994   1292   -161   -130    230       N  
ATOM   1403  CA  VAL A 142      27.032  -5.837  20.820  1.00 13.02           C  
ANISOU 1403  CA  VAL A 142     1547   1907   1491   -198   -146    235       C  
ATOM   1404  C   VAL A 142      25.696  -5.170  20.666  1.00 14.52           C  
ANISOU 1404  C   VAL A 142     1521   1940   2056   -115     55    430       C  
ATOM   1405  O   VAL A 142      25.537  -3.995  21.022  1.00 16.40           O  
ANISOU 1405  O   VAL A 142     1876   1849   2504   -101    161    420       O  
ATOM   1406  CB  VAL A 142      27.748  -5.896  19.448  1.00 15.32           C  
ANISOU 1406  CB  VAL A 142     1637   2324   1859     19    145    644       C  
ATOM   1407  CG1 VAL A 142      27.741  -4.547  18.742  1.00 17.14           C  
ANISOU 1407  CG1 VAL A 142     2203   2429   1882    -71    -49    689       C  
ATOM   1408  CG2 VAL A 142      29.195  -6.327  19.651  1.00 16.14           C  
ANISOU 1408  CG2 VAL A 142     1503   2631   1997    -88     72    572       C  
ATOM   1409  N  AARG A 143      24.658  -5.867  20.143  0.48 13.09           N  
ANISOU 1409  N  AARG A 143     1358   1833   1784    -52     69    765       N  
ATOM   1410  N  BARG A 143      24.738  -5.948  20.138  0.52 15.49           N  
ANISOU 1410  N  BARG A 143     1481   2355   2048    181   -170    -60       N  
ATOM   1411  CA AARG A 143      23.375  -5.186  19.950  0.48 16.92           C  
ANISOU 1411  CA AARG A 143     1505   2485   2441    280     -5    957       C  
ATOM   1412  CA BARG A 143      23.436  -5.352  19.888  0.52 15.37           C  
ANISOU 1412  CA BARG A 143     1572   2156   2114    121   -157    816       C  
ATOM   1413  C  AARG A 143      22.788  -4.782  21.272  0.48 17.47           C  
ANISOU 1413  C  AARG A 143     1655   2196   2787    342    415    943       C  
ATOM   1414  C  BARG A 143      22.848  -4.751  21.136  0.52 16.52           C  
ANISOU 1414  C  BARG A 143     1452   2419   2406    424    196    920       C  
ATOM   1415  O  AARG A 143      22.081  -3.787  21.510  0.48 25.79           O  
ANISOU 1415  O  AARG A 143     3288   2491   4021   1078   1691   1635       O  
ATOM   1416  O  BARG A 143      22.340  -3.621  21.110  0.52 17.37           O  
ANISOU 1416  O  BARG A 143     2067   2399   2134    458    153    987       O  
ATOM   1417  CB AARG A 143      22.413  -6.070  19.148  0.48 15.79           C  
ANISOU 1417  CB AARG A 143     1377   2146   2477    290   -149   1395       C  
ATOM   1418  CB BARG A 143      22.551  -6.424  19.247  0.52 16.33           C  
ANISOU 1418  CB BARG A 143     1451   2180   2573     -9   -270   1073       C  
ATOM   1419  CG AARG A 143      23.006  -6.543  17.831  0.48 17.08           C  
ANISOU 1419  CG AARG A 143     1430   2865   2195    358   -523   1152       C  
ATOM   1420  CG BARG A 143      22.545  -6.266  17.721  0.52 18.56           C  
ANISOU 1420  CG BARG A 143     2157   2396   2499    -89   -639    676       C  
ATOM   1421  CD AARG A 143      22.082  -7.373  17.042  0.48 19.77           C  
ANISOU 1421  CD AARG A 143     2045   3037   2431   -190   -810   1431       C  
ATOM   1422  CD BARG A 143      21.104  -6.426  17.194  0.52 25.74           C  
ANISOU 1422  CD BARG A 143     2566   3669   3544     10  -1325    269       C  
ATOM   1423  NE AARG A 143      21.784  -8.715  16.782  0.48 27.69           N  
ANISOU 1423  NE AARG A 143     3402   3249   3869     43  -1205    540       N  
ATOM   1424  NE BARG A 143      21.003  -7.587  16.371  0.52 21.60           N  
ANISOU 1424  NE BARG A 143     2484   2993   2731   -172  -1569   1143       N  
ATOM   1425  CZ AARG A 143      20.983  -9.086  15.763  0.48 28.04           C  
ANISOU 1425  CZ AARG A 143     3542   3460   3651    179   -897    -26       C  
ATOM   1426  CZ BARG A 143      20.125  -8.267  15.690  0.52 18.59           C  
ANISOU 1426  CZ BARG A 143     1966   3023   2075    -62  -1120   1164       C  
ATOM   1427  NH1AARG A 143      20.414  -8.251  14.923  0.48 30.24           N  
ANISOU 1427  NH1AARG A 143     3583   4129   3780   -901  -1453    681       N  
ATOM   1428  NH1BARG A 143      18.846  -7.940  15.634  0.52 20.93           N  
ANISOU 1428  NH1BARG A 143     1878   3056   3017   -223   -770    956       N  
ATOM   1429  NH2AARG A 143      20.781 -10.389  15.646  0.48 39.02           N  
ANISOU 1429  NH2AARG A 143     5905   3331   5589   1231  -1969  -1283       N  
ATOM   1430  NH2BARG A 143      20.552  -9.343  15.034  0.52 21.02           N  
ANISOU 1430  NH2BARG A 143     2307   2987   2693      9   -879    998       N  
ATOM   1431  N  AMET A 144      23.047  -5.567  22.330  0.73 15.87           N  
ANISOU 1431  N  AMET A 144     1645   1991   2394     73    272    551       N  
ATOM   1432  N  BMET A 144      22.894  -5.446  22.256  0.27 14.60           N  
ANISOU 1432  N  BMET A 144     1432   1910   2205    634    112    523       N  
ATOM   1433  CA AMET A 144      22.470  -5.063  23.570  0.73 17.91           C  
ANISOU 1433  CA AMET A 144     2090   2116   2599    198    378    406       C  
ATOM   1434  CA BMET A 144      22.379  -5.018  23.543  0.27 16.96           C  
ANISOU 1434  CA BMET A 144     1956   2195   2292    402    293    408       C  
ATOM   1435  C  AMET A 144      23.234  -3.844  24.042  0.73 19.05           C  
ANISOU 1435  C  AMET A 144     2359   2174   2706     -5    954    203       C  
ATOM   1436  C  BMET A 144      23.252  -3.970  24.212  0.27 19.69           C  
ANISOU 1436  C  BMET A 144     2205   2446   2829    335    537   -187       C  
ATOM   1437  O  AMET A 144      22.658  -2.849  24.455  0.73 23.19           O  
ANISOU 1437  O  AMET A 144     2891   1788   4134      9   1377    449       O  
ATOM   1438  O  BMET A 144      22.733  -3.159  24.986  0.27 24.03           O  
ANISOU 1438  O  BMET A 144     3385   2199   3547   -176   1766   -239       O  
ATOM   1439  CB AMET A 144      22.452  -6.204  24.592  0.73 16.63           C  
ANISOU 1439  CB AMET A 144     1898   2145   2275    233    389    340       C  
ATOM   1440  CB BMET A 144      22.208  -6.258  24.442  0.27 18.71           C  
ANISOU 1440  CB BMET A 144     3168   2225   1715    469   -203    348       C  
ATOM   1441  CG AMET A 144      21.903  -5.792  25.947  0.73 19.80           C  
ANISOU 1441  CG AMET A 144     2383   3172   1968    274   -209   -117       C  
ATOM   1442  CG BMET A 144      21.330  -6.070  25.665  0.27 21.28           C  
ANISOU 1442  CG BMET A 144     2656   2986   2442   -205    308    553       C  
ATOM   1443  SD AMET A 144      20.260  -5.027  25.910  0.73 20.95           S  
ANISOU 1443  SD AMET A 144     2403   2217   3339    249   1055     84       S  
ATOM   1444  SD BMET A 144      19.574  -6.430  25.425  0.27 25.43           S  
ANISOU 1444  SD BMET A 144     2752   2230   4681    -18   -443    836       S  
ATOM   1445  CE AMET A 144      19.693  -5.647  27.489  0.73 43.25           C  
ANISOU 1445  CE AMET A 144     5606   5619   5208   1101   3236   1791       C  
ATOM   1446  CE BMET A 144      18.960  -4.748  25.277  0.27 36.14           C  
ANISOU 1446  CE BMET A 144     4698   2898   6137   1941    -19  -1330       C  
ATOM   1447  N   MET A 145      24.565  -3.924  23.977  1.00 19.22           N  
ANISOU 1447  N   MET A 145     2357   2495   2452   -199    717     26       N  
ATOM   1448  CA  MET A 145      25.390  -2.897  24.568  1.00 23.30           C  
ANISOU 1448  CA  MET A 145     2722   2579   3553   -333    752   -289       C  
ATOM   1449  C   MET A 145      25.225  -1.570  23.860  1.00 26.92           C  
ANISOU 1449  C   MET A 145     4104   2359   3765   -145   1938   -286       C  
ATOM   1450  O   MET A 145      25.295  -0.510  24.471  1.00 37.49           O  
ANISOU 1450  O   MET A 145     7055   2591   4600   -271   2411   -838       O  
ATOM   1451  CB  MET A 145      26.892  -3.256  24.504  1.00 24.29           C  
ANISOU 1451  CB  MET A 145     2596   3612   3022   -468    417  -1345       C  
ATOM   1452  CG  MET A 145      27.267  -4.404  25.410  1.00 26.10           C  
ANISOU 1452  CG  MET A 145     3175   3867   2875    268   -763  -1897       C  
ATOM   1453  SD  MET A 145      27.021  -4.174  27.148  1.00 35.69           S  
ANISOU 1453  SD  MET A 145     5435   5324   2800    206    225  -1330       S  
ATOM   1454  CE  MET A 145      25.397  -4.813  27.441  1.00 87.86           C  
ANISOU 1454  CE  MET A 145    10721  12955   9706  -6473   6217  -6376       C  
ATOM   1455  N   VAL A 146      24.997  -1.636  22.552  1.00 26.75           N  
ANISOU 1455  N   VAL A 146     4101   2230   3835   -301   1589    167       N  
ATOM   1456  CA  VAL A 146      24.857  -0.329  21.867  1.00 30.36           C  
ANISOU 1456  CA  VAL A 146     4249   2394   4893    -83   2020    623       C  
ATOM   1457  C   VAL A 146      23.396   0.103  21.704  1.00 34.19           C  
ANISOU 1457  C   VAL A 146     4430   2695   5865    128   2079   1238       C  
ATOM   1458  O   VAL A 146      23.211   1.192  21.177  1.00 38.65           O  
ANISOU 1458  O   VAL A 146     5842   2925   5920    719   1689   1174       O  
ATOM   1459  CB  VAL A 146      25.536  -0.395  20.500  1.00 31.65           C  
ANISOU 1459  CB  VAL A 146     4308   3201   4515    113   1588   1163       C  
ATOM   1460  CG1 VAL A 146      26.973  -0.899  20.708  1.00 34.55           C  
ANISOU 1460  CG1 VAL A 146     3889   2998   6241   -123   2159    678       C  
ATOM   1461  CG2 VAL A 146      24.761  -1.253  19.521  1.00 31.34           C  
ANISOU 1461  CG2 VAL A 146     4886   2586   4437    331   1471   1182       C  
ATOM   1462  N   SER A 147      22.457  -0.728  22.138  1.00 42.05           N  
ANISOU 1462  N   SER A 147     4338   3855   7786     12   3105   1274       N  
ATOM   1463  CA  SER A 147      21.035  -0.555  21.893  1.00 49.83           C  
ANISOU 1463  CA  SER A 147     4726   5049   9159   -885   1231   2093       C  
ATOM   1464  C   SER A 147      20.156  -1.376  22.809  1.00 44.39           C  
ANISOU 1464  C   SER A 147     3643   3666   9559   -970   1280   1031       C  
ATOM   1465  O   SER A 147      20.339  -2.042  23.820  1.00 43.47           O  
ANISOU 1465  O   SER A 147     4227   3007   9284    158   2931    904       O  
ATOM   1466  CB  SER A 147      20.729  -0.885  20.424  1.00 55.45           C  
ANISOU 1466  CB  SER A 147     6665   5178   9226   1015   1128   1380       C  
ATOM   1467  OG  SER A 147      21.172  -2.131  19.875  1.00 50.29           O  
ANISOU 1467  OG  SER A 147     5747   4965   8395   2358    906   2864       O  
TER    1468      SER A 147                                                      
HETATM 1469 CA    CA A1000      46.224   7.128  -8.698  1.00  7.59          CA  
ANISOU 1469 CA    CA A1000     1024    529   1331   -178   -193     33      CA  
HETATM 1470 CA    CA A1001      36.763  12.606  -4.815  1.00 10.83          CA  
ANISOU 1470 CA    CA A1001     2049    526   1538    133   -782    -18      CA  
HETATM 1471 CA    CA A1002      22.026 -16.616  21.879  1.00 10.84          CA  
ANISOU 1471 CA    CA A1002     1227   1912    981   -198   -186    -32      CA  
HETATM 1472 CA    CA A1003      32.674 -10.435  -5.410  1.00 10.87          CA  
ANISOU 1472 CA    CA A1003     1374    673   2082   -102   -294    225      CA  
HETATM 1473 CA    CA A1004      31.568 -19.422  27.202  1.00 14.02          CA  
ANISOU 1473 CA    CA A1004     1781   1881   1666    585    235    275      CA  
HETATM 1474  O   HOH A2000      40.789  16.842  -5.083  1.00  9.89           O  
ANISOU 1474  O   HOH A2000     1318    765   1674   -196   -139    256       O  
HETATM 1475  O   HOH A2001      42.295  10.880 -11.518  1.00 10.57           O  
ANISOU 1475  O   HOH A2001     1520   1232   1265   -167   -306    -12       O  
HETATM 1476  O   HOH A2002      41.705 -15.715  -2.868  1.00 10.01           O  
ANISOU 1476  O   HOH A2002     1710    890   1203   -384   -226    257       O  
HETATM 1477  O   HOH A2003      14.809 -17.116  42.346  1.00 10.54           O  
ANISOU 1477  O   HOH A2003     1581   1114   1308     13   -139     85       O  
HETATM 1478  O   HOH A2004      17.979  -8.051  43.547  1.00 10.03           O  
ANISOU 1478  O   HOH A2004     1550    932   1329    -18   -109    188       O  
HETATM 1479  O   HOH A2005      20.902  -8.716  21.717  1.00 13.83           O  
ANISOU 1479  O   HOH A2005     1326   2395   1533    -52   -167    488       O  
HETATM 1480  O   HOH A2006      39.631 -14.352  -5.796  1.00 10.60           O  
ANISOU 1480  O   HOH A2006     1647    863   1517    -23   -105    286       O  
HETATM 1481  O   HOH A2007      25.821  -7.292  45.147  1.00 11.30           O  
ANISOU 1481  O   HOH A2007     1685   1004   1605     26   -208   -273       O  
HETATM 1482  O   HOH A2008      36.202  16.090  -1.527  1.00 13.74           O  
ANISOU 1482  O   HOH A2008     2183    821   2215     98   -378    104       O  
HETATM 1483  O   HOH A2009      43.816 -12.458  -5.592  1.00 11.57           O  
ANISOU 1483  O   HOH A2009     1594    766   2035   -195   -444    249       O  
HETATM 1484  O   HOH A2010      52.000   7.240  -4.484  1.00 12.61           O  
ANISOU 1484  O   HOH A2010     1508   1433   1848    -32   -285     22       O  
HETATM 1485  O   HOH A2011      39.438  12.591  -5.939  1.00 14.76           O  
ANISOU 1485  O   HOH A2011     2127   1702   1778    645  -1049   -645       O  
HETATM 1486  O   HOH A2012      23.594 -20.291  29.426  1.00 14.53           O  
ANISOU 1486  O   HOH A2012     1887   1811   1825   -451   -435    -82       O  
HETATM 1487  O   HOH A2013      36.982 -12.298  42.999  1.00 11.44           O  
ANISOU 1487  O   HOH A2013     1751    890   1707   -140   -330    239       O  
HETATM 1488  O   HOH A2014      26.036 -12.451  39.997  1.00 14.73           O  
ANISOU 1488  O   HOH A2014     2215   1561   1821   -861    463   -286       O  
HETATM 1489  O   HOH A2015      35.716  10.477   2.709  1.00 14.74           O  
ANISOU 1489  O   HOH A2015     1380   2379   1840     75    -89   -758       O  
HETATM 1490  O   HOH A2016      27.219   2.992  -4.838  1.00 15.82           O  
ANISOU 1490  O   HOH A2016     1744   1582   2685    166    540    130       O  
HETATM 1491  O   HOH A2017      37.759   5.553 -10.145  1.00 17.36           O  
ANISOU 1491  O   HOH A2017     1629   1413   3555   -124   -878    334       O  
HETATM 1492  O   HOH A2018      29.677  -8.242  -8.575  1.00 15.18           O  
ANISOU 1492  O   HOH A2018     1771   1812   2183   -416   -281    231       O  
HETATM 1493  O   HOH A2019      15.594 -14.445  42.575  1.00 15.21           O  
ANISOU 1493  O   HOH A2019     2105   1375   2298   -263    303   -108       O  
HETATM 1494  O   HOH A2020      34.849  -5.298  40.077  1.00 15.75           O  
ANISOU 1494  O   HOH A2020     2204   1532   2246   -387  -1002    151       O  
HETATM 1495  O   HOH A2021      52.321  11.732  16.151  1.00 20.53           O  
ANISOU 1495  O   HOH A2021     2114   4519   1168    446   -133    -99       O  
HETATM 1496  O   HOH A2022      30.227 -15.187  19.454  1.00 16.24           O  
ANISOU 1496  O   HOH A2022     1832   2640   1697    495    479    186       O  
HETATM 1497  O   HOH A2023      25.425 -15.277  42.324  1.00 20.37           O  
ANISOU 1497  O   HOH A2023     2678   2671   2390    228   -986   -139       O  
HETATM 1498  O   HOH A2024      37.556  -5.765 -11.157  1.00 18.63           O  
ANISOU 1498  O   HOH A2024     3099   1655   2325    743    579    560       O  
HETATM 1499  O   HOH A2025      15.998 -20.312  39.410  1.00 15.31           O  
ANISOU 1499  O   HOH A2025     2310   1700   1807   -124   -743   -349       O  
HETATM 1500  O   HOH A2026      38.753  17.085  -1.700  1.00 17.50           O  
ANISOU 1500  O   HOH A2026     2335   1342   2974     74   -435   -612       O  
HETATM 1501  O   HOH A2027      15.168 -10.056  42.106  1.00 17.48           O  
ANISOU 1501  O   HOH A2027     2573   2104   1966      0   -671   -248       O  
HETATM 1502  O   HOH A2028      31.388  -3.465  -2.591  1.00 17.30           O  
ANISOU 1502  O   HOH A2028     2121   2158   2294   -437     65    222       O  
HETATM 1503  O   HOH A2029      14.857 -14.876  24.857  1.00 18.72           O  
ANISOU 1503  O   HOH A2029     1591   3297   2223    150   -447   -159       O  
HETATM 1504  O   HOH A2030      30.080   9.422  -3.288  1.00 25.13           O  
ANISOU 1504  O   HOH A2030     4448   1999   3100  -1048  -1775    523       O  
HETATM 1505  O   HOH A2031      28.414 -19.030  38.108  1.00 21.58           O  
ANISOU 1505  O   HOH A2031     3345   3068   1786   -663   -346   1031       O  
HETATM 1506  O   HOH A2032      37.256 -15.167  25.836  1.00 19.46           O  
ANISOU 1506  O   HOH A2032     1600   3695   2098   -188   -101   1177       O  
HETATM 1507  O   HOH A2033      35.576 -14.982  23.690  1.00 20.02           O  
ANISOU 1507  O   HOH A2033     1659   3898   2049   -161    210    677       O  
HETATM 1508  O   HOH A2034      49.137  -3.694  -3.983  1.00 25.91           O  
ANISOU 1508  O   HOH A2034     1797   1104   6943    -91    215    892       O  
HETATM 1509  O   HOH A2035      48.451  15.002  -7.827  1.00 20.97           O  
ANISOU 1509  O   HOH A2035     3576   1511   2880  -1106    554   -697       O  
HETATM 1510  O   HOH A2036      23.660 -18.477  36.405  1.00 18.12           O  
ANISOU 1510  O   HOH A2036     2422   2817   1646   -894    -73   -175       O  
HETATM 1511  O   HOH A2037      28.956  -4.454  45.659  1.00 29.98           O  
ANISOU 1511  O   HOH A2037     2068   3536   5787    428  -1277  -3095       O  
HETATM 1512  O   HOH A2038      34.472   6.204 -10.276  1.00 20.50           O  
ANISOU 1512  O   HOH A2038     2733   2217   2839  -1216  -1045    355       O  
HETATM 1513  O   HOH A2039      33.741  16.608  -8.484  1.00 20.72           O  
ANISOU 1513  O   HOH A2039     2883   2058   2931   -145   -631    134       O  
HETATM 1514  O   HOH A2040      24.111 -14.449  48.050  1.00 18.73           O  
ANISOU 1514  O   HOH A2040     2142   1555   3420    143     -1    949       O  
HETATM 1515  O  AHOH A2041      44.207   4.663 -11.870  0.33  8.04           O  
ANISOU 1515  O  AHOH A2041     1265    769   1023   -355     32    -43       O  
HETATM 1516  O  BHOH A2042      44.917   5.551 -12.815  0.33 11.39           O  
ANISOU 1516  O  BHOH A2042     1655   1283   1388   -186     63   -542       O  
HETATM 1517  O  CHOH A2043      43.481   3.315 -12.617  0.33 10.33           O  
ANISOU 1517  O  CHOH A2043     1649   1064   1211   -330   -108   -338       O  
HETATM 1518  O  AHOH A2044      50.218   9.127  -3.434  0.33  9.19           O  
ANISOU 1518  O  AHOH A2044     1117   1001   1374    199   -334   -183       O  
HETATM 1519  O  BHOH A2045      49.736  10.701  -4.027  0.33  7.48           O  
ANISOU 1519  O  BHOH A2045     1018    726   1097   -123   -512   -122       O  
HETATM 1520  O  CHOH A2046      51.287   9.050  -2.513  0.33 11.21           O  
ANISOU 1520  O  CHOH A2046     1748   1097   1416    374   -333     62       O  
HETATM 1521  O   HOH A2047      47.397   3.482 -11.670  1.00 20.63           O  
ANISOU 1521  O   HOH A2047     2579   2275   2984   -186    468   -864       O  
HETATM 1522  O   HOH A2048      16.293 -17.085  25.525  1.00 30.98           O  
ANISOU 1522  O   HOH A2048     3938   2807   5026   -269   3132     72       O  
HETATM 1523  O   HOH A2049      25.164 -21.850  32.473  1.00 21.55           O  
ANISOU 1523  O   HOH A2049     3106   1886   3196  -1009  -1134    515       O  
HETATM 1524  O   HOH A2050      25.731 -13.988  14.636  1.00 24.46           O  
ANISOU 1524  O   HOH A2050     2866   4590   1837   -183   -798   -469       O  
HETATM 1525  O   HOH A2051      31.745   8.394  -7.046  1.00 25.10           O  
ANISOU 1525  O   HOH A2051     5320   1669   2547  -1788  -1586    668       O  
HETATM 1526  O   HOH A2052      26.999 -17.592  47.052  1.00 34.68           O  
ANISOU 1526  O   HOH A2052     6884   1673   4618   -820  -3553    570       O  
HETATM 1527  O   HOH A2053      15.486 -21.459  23.871  1.00 25.28           O  
ANISOU 1527  O   HOH A2053     2687   2558   4359  -1118   1656   -863       O  
HETATM 1528  O   HOH A2054      31.784 -19.349  35.227  1.00 24.96           O  
ANISOU 1528  O   HOH A2054     2962   3319   3204    563   -524   1205       O  
HETATM 1529  O   HOH A2055      20.516  -8.178  28.667  1.00 21.77           O  
ANISOU 1529  O   HOH A2055     3056   2487   2728   -597   -258    -64       O  
HETATM 1530  O   HOH A2056      33.690  -6.382 -13.311  1.00 26.11           O  
ANISOU 1530  O   HOH A2056     4594   2986   2340    414   -715  -1124       O  
HETATM 1531  O   HOH A2057      18.395 -21.278  35.724  1.00 29.60           O  
ANISOU 1531  O   HOH A2057     5373   2809   3064   -589    829    441       O  
HETATM 1532  O   HOH A2058      28.258 -13.517  16.993  1.00 26.77           O  
ANISOU 1532  O   HOH A2058     4393   3632   2145    304    890   -717       O  
HETATM 1533  O   HOH A2059      33.145 -21.122  31.767  1.00 27.90           O  
ANISOU 1533  O   HOH A2059     3806   3703   3092   1795    326   1349       O  
HETATM 1534  O   HOH A2060      46.453  -0.102 -10.432  1.00 24.45           O  
ANISOU 1534  O   HOH A2060     4282   1463   3544    225   1548    596       O  
HETATM 1535  O   HOH A2061      15.569 -18.233  30.784  1.00 30.01           O  
ANISOU 1535  O   HOH A2061     3443   3683   4275    986   -632    358       O  
HETATM 1536  O   HOH A2062      50.446   9.900  -0.399  1.00 24.97           O  
ANISOU 1536  O   HOH A2062     3612   3117   2758    384   -878    -91       O  
HETATM 1537  O   HOH A2063      40.283  -3.190 -10.892  1.00 29.39           O  
ANISOU 1537  O   HOH A2063     5875   2085   3208   1422   1155   1090       O  
HETATM 1538  O   HOH A2064      39.387   3.086 -12.642  1.00 26.45           O  
ANISOU 1538  O   HOH A2064     4416   3057   2576    511   -861   -537       O  
HETATM 1539  O   HOH A2065      36.943 -15.021  40.078  1.00 30.53           O  
ANISOU 1539  O   HOH A2065     2017   3403   6179    658    448   1391       O  
HETATM 1540  O  AHOH A2066      28.229  -0.346  -7.875  0.50 16.14           O  
ANISOU 1540  O  AHOH A2066      889   1620   3621    546   -354    332       O  
HETATM 1541  O  BHOH A2067      28.242   1.640  -7.765  0.50 18.24           O  
ANISOU 1541  O  BHOH A2067     1546   1273   4111    432    292    940       O  
HETATM 1542  O   HOH A2068      18.045 -17.159  29.531  1.00 22.90           O  
ANISOU 1542  O   HOH A2068     2382   3397   2922    -36   -656   -386       O  
HETATM 1543  O   HOH A2069      31.525 -17.270  41.211  1.00 31.52           O  
ANISOU 1543  O   HOH A2069     2671   6699   2606  -1672  -1059   1043       O  
HETATM 1544  O   HOH A2070      32.863   1.752 -12.347  1.00 31.70           O  
ANISOU 1544  O   HOH A2070     5844   3564   2639   2412   -268    309       O  
HETATM 1545  O   HOH A2071      20.972 -18.610  35.394  1.00 28.01           O  
ANISOU 1545  O   HOH A2071     3017   4667   2958   -975   1383   -583       O  
HETATM 1546  O   HOH A2072      28.748  -3.705  -3.267  1.00 34.68           O  
ANISOU 1546  O   HOH A2072     2096   2647   8433    -79    321   2826       O  
HETATM 1547  O   HOH A2073      15.587 -16.467  16.379  1.00 32.32           O  
ANISOU 1547  O   HOH A2073     1796   7329   3156    236   -441  -2028       O  
HETATM 1548  O   HOH A2074      29.658 -22.002  31.223  1.00 29.80           O  
ANISOU 1548  O   HOH A2074     3148   2023   6152    777  -1103   -157       O  
HETATM 1549  O   HOH A2075      11.848 -19.490  39.935  1.00 31.49           O  
ANISOU 1549  O   HOH A2075     2628   3687   5652   -588   -420   1449       O  
HETATM 1550  O   HOH A2076      15.520 -15.402  22.225  1.00 31.54           O  
ANISOU 1550  O   HOH A2076     4672   4970   2341  -1503    119   -235       O  
HETATM 1551  O   HOH A2077      39.228 -19.578  28.304  1.00 30.97           O  
ANISOU 1551  O   HOH A2077     2360   4808   4598    426    319    327       O  
HETATM 1552  O   HOH A2078      11.322  -9.487  36.308  1.00 32.13           O  
ANISOU 1552  O   HOH A2078     3370   5299   3537    943    695   -263       O  
HETATM 1553  O   HOH A2079      41.463  -8.024  20.962  1.00 29.34           O  
ANISOU 1553  O   HOH A2079     2080   4803   4265   -814   -869   -134       O  
HETATM 1554  O   HOH A2080      46.531   0.288  -6.478  1.00 30.19           O  
ANISOU 1554  O   HOH A2080     2682   2419   6372    -92    891   -817       O  
HETATM 1555  O   HOH A2081      28.505 -22.554  26.178  1.00 35.77           O  
ANISOU 1555  O   HOH A2081     2961   2821   7810    653  -2212   -717       O  
HETATM 1556  O   HOH A2082      26.111 -18.062  17.264  1.00 35.20           O  
ANISOU 1556  O   HOH A2082     4451   3739   5184   1023   -285  -2081       O  
HETATM 1557  O   HOH A2083      28.956  -8.336  -3.895  1.00 40.58           O  
ANISOU 1557  O   HOH A2083     3825   4834   6758    771   1988   2585       O  
HETATM 1558  O   HOH A2084      28.838  11.990  -8.810  1.00 30.27           O  
ANISOU 1558  O   HOH A2084     1832   5945   3724   -567   -461   1226       O  
HETATM 1559  O   HOH A2085      14.146 -15.462  34.876  1.00 28.44           O  
ANISOU 1559  O   HOH A2085     1966   4936   3905   -341   -835    761       O  
HETATM 1560  O   HOH A2086      41.018  14.774  -6.961  1.00 13.41           O  
ANISOU 1560  O   HOH A2086     2018   1042   2036    332   -391    -85       O  
HETATM 1561  O   HOH A2087      23.068 -16.227  49.942  1.00 16.27           O  
ANISOU 1561  O   HOH A2087     2237   1668   2279   -388   -883    609       O  
HETATM 1562  O   HOH A2088      28.790   9.197  -5.602  1.00 18.68           O  
ANISOU 1562  O   HOH A2088     2085   2560   2451   -624   -714    483       O  
HETATM 1563  O   HOH A2089      13.505 -21.891  40.162  1.00 21.85           O  
ANISOU 1563  O   HOH A2089     2307   3116   2880   -509   -489   -601       O  
HETATM 1564  O   HOH A2090      17.746 -22.206  38.316  1.00 22.80           O  
ANISOU 1564  O   HOH A2090     3076   2731   2857   -557   -124   -658       O  
HETATM 1565  O   HOH A2091      49.941   2.266 -12.115  1.00 30.06           O  
ANISOU 1565  O   HOH A2091     3859   2894   4668    780   1954   -351       O  
HETATM 1566  O   HOH A2092      29.078 -17.394  40.211  1.00 24.67           O  
ANISOU 1566  O   HOH A2092     2279   5146   1948   -617   -412    668       O  
HETATM 1567  O   HOH A2093      14.282 -12.479  41.334  1.00 18.84           O  
ANISOU 1567  O   HOH A2093     2765   2104   2290   -433   -215    286       O  
HETATM 1568  O   HOH A2094      45.616   1.495 -12.291  1.00 22.63           O  
ANISOU 1568  O   HOH A2094     3109   2305   3185    132   -180   -263       O  
HETATM 1569  O   HOH A2095      43.962  -6.979  20.675  1.00 23.43           O  
ANISOU 1569  O   HOH A2095     2145   3534   3224    436   -620   -122       O  
HETATM 1570  O   HOH A2096      34.096  -2.838  38.969  1.00 27.61           O  
ANISOU 1570  O   HOH A2096     4038   3072   3380    399  -1060    901       O  
HETATM 1571  O   HOH A2097      37.858  -3.308 -12.223  1.00 30.27           O  
ANISOU 1571  O   HOH A2097     4549   2581   4373   1177   1488   1705       O  
HETATM 1572  O   HOH A2098      27.988  13.514 -10.750  1.00 30.50           O  
ANISOU 1572  O   HOH A2098     4411   4001   3175   -151  -1748    705       O  
HETATM 1573  O   HOH A2099      31.491  -2.699  39.010  1.00 34.83           O  
ANISOU 1573  O   HOH A2099     4619   3171   5443   -629    606   1848       O  
HETATM 1574  O   HOH A2100      30.500  -0.552 -12.203  1.00 34.35           O  
ANISOU 1574  O   HOH A2100     5618   3391   4042    925  -1358   1000       O  
HETATM 1575  O   HOH A2101      23.055 -22.517  30.895  1.00 41.33           O  
ANISOU 1575  O   HOH A2101     6061   4378   5266  -3240  -2015   2137       O  
HETATM 1576  O   HOH A2102      32.697 -14.477  41.218  1.00 30.96           O  
ANISOU 1576  O   HOH A2102     3725   4325   3712     41   -760   1758       O  
HETATM 1577  O   HOH A2103      26.549 -23.790  28.538  1.00 37.33           O  
ANISOU 1577  O   HOH A2103     6377   3851   3956   2119  -1668    716       O  
HETATM 1578  O   HOH A2104      11.478 -14.774  35.326  1.00 31.02           O  
ANISOU 1578  O   HOH A2104     1989   5453   4343   -244   -743   1086       O  
HETATM 1579  O   HOH A2105      28.056  -6.616  -6.850  1.00 38.06           O  
ANISOU 1579  O   HOH A2105     2896   7786   3780    294   -670  -1041       O  
HETATM 1580  O   HOH A2106      36.197  -2.990  27.461  1.00 29.68           O  
ANISOU 1580  O   HOH A2106     4127   4742   2408  -1148    261    -88       O  
HETATM 1581  O   HOH A2107      16.712  -7.855  39.856  1.00 30.20           O  
ANISOU 1581  O   HOH A2107     6475   2478   2523   1899  -1087   -330       O  
HETATM 1582  O   HOH A2108      12.346  -4.992  29.012  1.00 45.21           O  
ANISOU 1582  O   HOH A2108     3953   5986   7238     85    132   2059       O  
HETATM 1583  O   HOH A2109      10.155 -12.003  36.709  1.00 30.46           O  
ANISOU 1583  O   HOH A2109     3040   5391   3144    499   -143   -659       O  
HETATM 1584  O   HOH A2110      40.058  15.687   5.385  1.00 31.23           O  
ANISOU 1584  O   HOH A2110     4408   4397   3061   -502   -159   -743       O  
HETATM 1585  O   HOH A2111      34.298  10.749   6.300  1.00 36.71           O  
ANISOU 1585  O   HOH A2111     3130   6610   4206  -1274  -1161   1748       O  
HETATM 1586  O   HOH A2112      49.250  -0.811 -10.669  1.00 34.23           O  
ANISOU 1586  O   HOH A2112     3312   5350   4343    326    811  -1704       O  
HETATM 1587  O   HOH A2113      54.037   8.829   0.426  1.00 32.37           O  
ANISOU 1587  O   HOH A2113     2490   4792   5020  -1216    564   -798       O  
HETATM 1588  O   HOH A2114      27.204 -23.904  33.047  1.00 39.38           O  
ANISOU 1588  O   HOH A2114     7651   3085   4228  -1065    450    568       O  
HETATM 1589  O   HOH A2115      31.012 -20.152  38.014  1.00 34.73           O  
ANISOU 1589  O   HOH A2115     3086   5025   5083   1158     50    933       O  
HETATM 1590  O   HOH A2116      46.425  19.891  13.066  1.00 38.24           O  
ANISOU 1590  O   HOH A2116     4236   4889   5405    402   -419   1227       O  
HETATM 1591  O   HOH A2117      13.323 -22.008  24.319  1.00 34.66           O  
ANISOU 1591  O   HOH A2117     5075   4313   3780    770   1437   -455       O  
HETATM 1592  O   HOH A2118      34.988  13.024   3.462  1.00 37.72           O  
ANISOU 1592  O   HOH A2118     5139   4743   4448   1985  -1852  -2073       O  
HETATM 1593  O   HOH A2119      43.378  15.388  18.789  1.00 37.05           O  
ANISOU 1593  O   HOH A2119     1755   5343   6978    846   -665   -818       O  
HETATM 1594  O   HOH A2120      11.628  -7.194  35.152  1.00 34.74           O  
ANISOU 1594  O   HOH A2120     5382   4614   3205    562    110   -319       O  
HETATM 1595  O   HOH A2121      35.496   1.898   0.764  1.00 38.61           O  
ANISOU 1595  O   HOH A2121     8466   2921   3283    923  -2247   -207       O  
HETATM 1596  O   HOH A2122      44.846   7.205 -10.602  1.00 10.47           O  
ANISOU 1596  O   HOH A2122     1196   1221   1563   -288   -311    -76       O  
HETATM 1597  O   HOH A2123      34.133 -10.927  -7.266  1.00 11.31           O  
ANISOU 1597  O   HOH A2123     1535    882   1882   -223   -523    177       O  
HETATM 1598  O   HOH A2124      34.869 -10.511  -4.411  1.00 12.42           O  
ANISOU 1598  O   HOH A2124     1507   1129   2082     68   -393    -93       O  
HETATM 1599  O   HOH A2125      31.016 -10.538  -7.141  1.00 14.55           O  
ANISOU 1599  O   HOH A2125     1686   1230   2611   -322   -567    507       O  
HETATM 1600  O   HOH A2126      32.204 -10.618  -3.104  1.00 13.84           O  
ANISOU 1600  O   HOH A2126     2118    977   2165    -32   -280    119       O  
HETATM 1601  O   HOH A2127      38.095  14.626  -4.782  1.00 10.00           O  
ANISOU 1601  O   HOH A2127     1390    940   1472    101   -287     15       O  
HETATM 1602  O   HOH A2128      30.336 -21.323  27.900  1.00 20.07           O  
ANISOU 1602  O   HOH A2128     2637   2157   2833   -361    720   -496       O  
HETATM 1603  O   HOH A2129      24.034 -17.418  20.784  1.00 13.22           O  
ANISOU 1603  O   HOH A2129     1336   2307   1380     13   -104   -166       O  
HETATM 1604  O   HOH A2130      54.504  10.989   0.679  1.00 31.62           O  
ANISOU 1604  O   HOH A2130     2390   5962   3662  -1983   1059  -1732       O  
HETATM 1605  O   HOH A2131      14.288 -12.648  38.691  1.00 26.44           O  
ANISOU 1605  O   HOH A2131     2821   3485   3738   -145   -281   -805       O  
HETATM 1606  O   HOH A2132      51.344   8.866  15.549  1.00 34.98           O  
ANISOU 1606  O   HOH A2132     5324   3380   4587   -417    -41   -444       O  
HETATM 1607  O   HOH A2133      35.549  16.220   0.968  1.00 29.81           O  
ANISOU 1607  O   HOH A2133     4368   4442   2515  -1362   -180   -594       O  
HETATM 1608  O   HOH A2134      50.710  18.958  12.127  1.00 38.85           O  
ANISOU 1608  O   HOH A2134     6513   5317   2930    321  -2981     69       O  
HETATM 1609  O   HOH A2135      26.874  -2.390  39.940  1.00 31.54           O  
ANISOU 1609  O   HOH A2135     5196   3069   3718   -523    260   -225       O  
HETATM 1610  O   HOH A2136      24.232 -22.923  34.520  1.00 36.16           O  
ANISOU 1610  O   HOH A2136     5527   3831   4382  -1972    631   -202       O  
HETATM 1611  O   HOH A2137      37.758   2.743   1.818  1.00 34.10           O  
ANISOU 1611  O   HOH A2137     3859   5122   3975    155    608     42       O  
HETATM 1612  O   HOH A2138      32.486 -23.743  19.584  1.00 36.99           O  
ANISOU 1612  O   HOH A2138     7124   2770   4161   -809   1801   -500       O  
HETATM 1613  O   HOH A2139      28.537  10.101 -10.082  1.00 38.26           O  
ANISOU 1613  O   HOH A2139     4266   5226   5047  -2026  -1457   2017       O  
HETATM 1614  O   HOH A2140      48.262   7.843  12.020  1.00 33.39           O  
ANISOU 1614  O   HOH A2140     3796   4932   3959    146    158    279       O  
HETATM 1615  O   HOH A2141      20.126 -18.971  29.987  1.00 38.03           O  
ANISOU 1615  O   HOH A2141     3862   7056   3533   -658    559   2159       O  
HETATM 1616  O   HOH A2142      31.325 -21.709  33.349  1.00 41.34           O  
ANISOU 1616  O   HOH A2142     4909   6175   4624     42   -482   3036       O  
HETATM 1617  O   HOH A2143      17.558  -9.167  35.767  1.00 31.17           O  
ANISOU 1617  O   HOH A2143     4455   3474   3913     17    -30    341       O  
HETATM 1618  O   HOH A2144      14.755 -10.646  37.436  1.00 39.09           O  
ANISOU 1618  O   HOH A2144     5216   6296   3342    508  -1175   1263       O  
HETATM 1619  O   HOH A2145      28.210   0.410 -10.786  1.00 39.91           O  
ANISOU 1619  O   HOH A2145     4518   4790   5856   1062   -460   -947       O  
HETATM 1620  O   HOH A2146      31.958  -8.877  -0.889  1.00 41.14           O  
ANISOU 1620  O   HOH A2146     6785   4193   4654   1804  -1029  -2411       O  
HETATM 1621  O   HOH A2147      52.336   2.719 -11.133  1.00 39.73           O  
ANISOU 1621  O   HOH A2147     4678   3833   6584   -447   1558  -2356       O  
HETATM 1622  O   HOH A2148      15.782 -25.622  38.405  1.00 49.95           O  
ANISOU 1622  O   HOH A2148     4982   8385   5612  -2872  -2171    -44       O  
HETATM 1623  O   HOH A2149      25.784 -13.682  49.774  1.00 41.68           O  
ANISOU 1623  O   HOH A2149     4563   6245   5028  -1688     75    975       O  
HETATM 1624  O   HOH A2150      24.095 -21.106  35.938  1.00 43.78           O  
ANISOU 1624  O   HOH A2150     5573   3715   7344     60   2629   1675       O  
HETATM 1625  O   HOH A2151      55.502  10.834   3.254  1.00 44.34           O  
ANISOU 1625  O   HOH A2151     2987   6732   7129     73    776    569       O  
HETATM 1626  O   HOH A2152      39.636  15.429   7.957  1.00 40.60           O  
ANISOU 1626  O   HOH A2152     5747   4545   5135   -149   -465  -2376       O  
HETATM 1627  O   HOH A2153      15.626 -18.799  36.163  1.00 40.93           O  
ANISOU 1627  O   HOH A2153     6110   4452   4989    312    463  -1955       O  
HETATM 1628  O   HOH A2154      30.627 -22.589  20.476  1.00 41.87           O  
ANISOU 1628  O   HOH A2154     6985   4112   4811  -1786   2608   -714       O  
HETATM 1629  O   HOH A2155      28.295  -8.221  46.335  1.00 27.60           O  
ANISOU 1629  O   HOH A2155     3930   2901   3655  -1036  -1376   1248       O  
HETATM 1630  O   HOH A2156      35.232   4.130 -11.736  1.00 33.35           O  
ANISOU 1630  O   HOH A2156     5015   4039   3616  -1341   -837   -553       O  
HETATM 1631  O   HOH A2157      29.782  -9.676  44.753  1.00 25.48           O  
ANISOU 1631  O   HOH A2157     3546   3281   2855    -26    269    363       O  
HETATM 1632  O   HOH A2158      27.322 -21.607  37.930  1.00 38.67           O  
ANISOU 1632  O   HOH A2158     5444   4155   5092  -1964   -405    400       O  
HETATM 1633  O   HOH A2159      39.004 -22.581  27.995  1.00 37.05           O  
ANISOU 1633  O   HOH A2159     3922   6049   4106    -15    421     26       O  
HETATM 1634  O   HOH A2160      31.707   8.248 -10.026  1.00 38.85           O  
ANISOU 1634  O   HOH A2160     2787   6406   5566  -1599  -1048   2082       O  
HETATM 1635  O   HOH A2161      12.461 -17.449  40.907  0.60 18.47           O  
ANISOU 1635  O   HOH A2161     1998   3164   1856   -146   -892    777       O  
HETATM 1636  O   HOH A2162      20.148 -20.536  31.989  1.00 38.29           O  
ANISOU 1636  O   HOH A2162     4009   7624   2917  -2727  -1119   1574       O  
HETATM 1637  O   HOH A2163      13.610  -8.988  39.913  1.00 35.06           O  
ANISOU 1637  O   HOH A2163     6338   3072   3913    824    719    166       O  
HETATM 1638  O   HOH A2164      31.426  -2.634  -0.089  1.00 42.14           O  
ANISOU 1638  O   HOH A2164     5008   5203   5799  -1938    215  -1721       O  
HETATM 1639  O   HOH A2165      46.501   8.766  14.370  1.00 47.02           O  
ANISOU 1639  O   HOH A2165     5001   5698   7167  -1765   1128  -1584       O  
HETATM 1640  O   HOH A2166      38.771  17.316  18.874  1.00 49.37           O  
ANISOU 1640  O   HOH A2166     4083   6573   8102   1386   -247  -2279       O  
HETATM 1641  O   HOH A2167      29.639  -1.703  43.748  1.00 44.48           O  
ANISOU 1641  O   HOH A2167     2803   7178   6919   1904   -659  -1772       O  
HETATM 1642  O   HOH A2168      50.504  -5.523  -4.771  1.00 34.24           O  
ANISOU 1642  O   HOH A2168     3314   4699   4997   -911   -357   -738       O  
HETATM 1643  O   HOH A2169      23.084  -7.778  29.256  1.00 42.05           O  
ANISOU 1643  O   HOH A2169     3828   6752   5396  -1253    735   -932       O  
HETATM 1644  O   HOH A2170      27.942 -16.414  49.674  1.00 42.67           O  
ANISOU 1644  O   HOH A2170     5750   4861   5603  -2378    430  -1587       O  
HETATM 1645  O   HOH A2171      42.750  -2.232  25.172  1.00 40.65           O  
ANISOU 1645  O   HOH A2171     4187   3405   7851   -599   1874   -493       O  
HETATM 1646  O   HOH A2172      25.329  -7.136  30.407  1.00 36.12           O  
ANISOU 1646  O   HOH A2172     3941   5373   4411  -1079  -1045    969       O  
HETATM 1647  O   HOH A2173      11.730 -12.749  34.283  1.00 40.97           O  
ANISOU 1647  O   HOH A2173     4388   4054   7124    125   1621    762       O  
HETATM 1648  O   HOH A2174      40.613  17.745  17.101  1.00 40.87           O  
ANISOU 1648  O   HOH A2174     4378   5789   5360    634  -1192    640       O  
HETATM 1649  O   HOH A2175      47.441   1.538   3.068  1.00 39.60           O  
ANISOU 1649  O   HOH A2175     5682   4324   5039  -1542    436    284       O  
HETATM 1650  O   HOH A2176      33.898  -7.037  -2.077  1.00 45.34           O  
ANISOU 1650  O   HOH A2176     7010   3666   6552    518  -1305   1918       O  
HETATM 1651  O   HOH A2177      43.807  -4.841  21.930  1.00 47.83           O  
ANISOU 1651  O   HOH A2177     4646   7132   6395   -435   -914    592       O  
CONECT  195 1469                                                                
CONECT  212 1469                                                                
CONECT  224 1469                                                                
CONECT  233 1469                                                                
CONECT  275 1469                                                                
CONECT  276 1469                                                                
CONECT  415 1472                                                                
CONECT  416 1472                                                                
CONECT  503 1470                                                                
CONECT  516 1470                                                                
CONECT  528 1470                                                                
CONECT  537 1470                                                                
CONECT  582 1470                                                                
CONECT  583 1470                                                                
CONECT  933 1473                                                                
CONECT  952 1473                                                                
CONECT  964 1473                                                                
CONECT  973 1473                                                                
CONECT 1017 1473                                                                
CONECT 1018 1473                                                                
CONECT 1270 1471                                                                
CONECT 1286 1471                                                                
CONECT 1298 1471                                                                
CONECT 1307 1471                                                                
CONECT 1378 1471                                                                
CONECT 1379 1471                                                                
CONECT 1469  195  212  224  233                                                 
CONECT 1469  275  276 1596                                                      
CONECT 1470  503  516  528  537                                                 
CONECT 1470  582  583 1485 1601                                                 
CONECT 1471 1270 1286 1298 1307                                                 
CONECT 1471 1378 1379 1603                                                      
CONECT 1472  415  416 1597 1598                                                 
CONECT 1472 1599 1600                                                           
CONECT 1473  933  952  964  973                                                 
CONECT 1473 1017 1018 1602                                                      
CONECT 1485 1470                                                                
CONECT 1596 1469                                                                
CONECT 1597 1472                                                                
CONECT 1598 1472                                                                
CONECT 1599 1472                                                                
CONECT 1600 1472                                                                
CONECT 1601 1470                                                                
CONECT 1602 1473                                                                
CONECT 1603 1471                                                                
MASTER      321    0    5    7    2    0   10    6 1333    1   45   12          
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.