CNRS Nantes University UFIP UFIP
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***  3FIA_test  ***

elNémo ID: 190814212755137892

Job options:

ID        	=	 190814212755137892
JOBID     	=	 3FIA_test
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 3FIA_test

HEADER    PROTEIN BINDING                         11-DEC-08   3FIA              
TITLE     CRYSTAL STRUCTURE OF THE EH 1 DOMAIN FROM HUMAN INTERSECTIN-1 PROTEIN.
TITLE    2 NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET HR3646E.             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INTERSECTIN-1;                                             
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 1-111;                                            
COMPND   5 SYNONYM: SH3 DOMAIN-CONTAINING PROTEIN 1A, SH3P17;                   
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: ITSN, ITSN1, SH3D1A;                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3) +MAGIC;                         
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET 14-15C                                
KEYWDS    INTERSECTIN-1; EH 1 DOMAIN; NESG, STRUCTURAL GENOMICS, PSI-2, PROTEIN 
KEYWDS   2 STRUCTURE INITIATIVE, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM,      
KEYWDS   3 ALTERNATIVE SPLICING, CALCIUM, CELL JUNCTION, CELL PROJECTION,       
KEYWDS   4 COILED COIL, ENDOCYTOSIS, MEMBRANE, PHOSPHOPROTEIN, SH3 DOMAIN,      
KEYWDS   5 SYNAPSE, SYNAPTOSOME, PROTEIN BINDING                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.M.VOROBIEV,Y.CHEN,J.SEETHARAMAN,C.DEVICES,L.ZHAO,E.L.FOOTE,         
AUTHOR   2 C.CICCOSANTI,L.MAO,R.XIAO,T.B.ACTON,G.T.MONTELIONE,J.F.HUNT,L.TONG,  
AUTHOR   3 NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG)                      
REVDAT   2   25-OCT-17 3FIA    1       REMARK                                   
REVDAT   1   30-DEC-08 3FIA    0                                                
JRNL        AUTH   S.M.VOROBIEV,Y.CHEN,J.SEETHARAMAN,C.DEVICES,L.ZHAO,          
JRNL        AUTH 2 E.L.FOOTE,C.CICCOSANTI,L.MAO,R.XIAO,T.B.ACTON,               
JRNL        AUTH 3 G.T.MONTELIONE,J.F.HUNT,L.TONG                               
JRNL        TITL   CRYSTAL STRUCTURE OF THE EH 1 DOMAIN FROM HUMAN              
JRNL        TITL 2 INTERSECTIN-1 PROTEIN.                                       
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.45 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.45                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.50                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 16237                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.160                           
REMARK   3   R VALUE            (WORKING SET) : 0.160                           
REMARK   3   FREE R VALUE                     : 0.176                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 866                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.45                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.49                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1155                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.75                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1390                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 61                           
REMARK   3   BIN FREE R VALUE                    : 0.2020                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 771                                     
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 6                                       
REMARK   3   SOLVENT ATOMS            : 133                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 17.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.34000                                             
REMARK   3    B22 (A**2) : 0.44000                                              
REMARK   3    B33 (A**2) : -0.07000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.04000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.080         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.062         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.027         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.427         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.963                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.960                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):   804 ; 0.006 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1091 ; 0.831 ; 1.963       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):    99 ; 5.142 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    36 ;39.613 ;25.000       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   136 ;14.597 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     3 ; 9.558 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   116 ; 0.065 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):   616 ; 0.015 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   396 ; 0.237 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):   581 ; 0.321 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):    74 ; 0.152 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     6 ; 0.064 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    48 ; 0.183 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    25 ; 0.194 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):   506 ; 2.699 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):   799 ; 3.364 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   315 ; 4.506 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   292 ; 6.253 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):   821 ; 2.895 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   134 ;10.275 ; 3.000       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):   784 ; 6.239 ; 3.000       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3FIA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-DEC-08.                  
REMARK 100 THE DEPOSITION ID IS D_1000050625.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-DEC-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X4C                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97869                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 31879                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.450                              
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     (%) : 96.1                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : 0.04000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 33.7500                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.45                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.50                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.22200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 4.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SNB, RESOLVE                                          
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 29.89                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.75                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.5M AMMONIUM SULFATE, 12% GLYCEROL,     
REMARK 280  0.1M TRISHCL, PH 8.5, MICROBATCH UNDER OIL , TEMPERATURE 277K       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       47.42400            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       16.01050            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       47.42400            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       16.01050            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: MONOMER ACCORDING TO AGGREGATION SCREENING                   
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     MSE A    -9                                                      
REMARK 465     GLY A    -8                                                      
REMARK 465     HIS A    -7                                                      
REMARK 465     HIS A    -6                                                      
REMARK 465     HIS A    -5                                                      
REMARK 465     HIS A    -4                                                      
REMARK 465     HIS A    -3                                                      
REMARK 465     HIS A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     VAL A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     GLN A     3                                                      
REMARK 465     PHE A     4                                                      
REMARK 465     PRO A     5                                                      
REMARK 465     GLN A   104                                                      
REMARK 465     GLN A   105                                                      
REMARK 465     PRO A   106                                                      
REMARK 465     VAL A   107                                                      
REMARK 465     ALA A   108                                                      
REMARK 465     ILE A   109                                                      
REMARK 465     SER A   110                                                      
REMARK 465     SER A   111                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     THR A   6    OG1  CG2                                            
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 A 201  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  66   OD1                                                    
REMARK 620 2 ASN A  68   OD1  86.1                                              
REMARK 620 3 ASP A  70   OD1  89.3  75.5                                        
REMARK 620 4 ARG A  72   O    89.8 151.8  76.5                                  
REMARK 620 5 GLU A  77   OE1 104.5 127.5 153.2  80.5                            
REMARK 620 6 GLU A  77   OE2  92.3  75.3 150.6 132.8  53.4                      
REMARK 620 7 HOH A 403   O   167.2  86.8  78.6  91.4  88.3  96.2                
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 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 301                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: HR3646E   RELATED DB: TARGETDB                           
DBREF  3FIA A    1   111  UNP    Q15811   ITSN1_HUMAN      1    111             
SEQADV 3FIA MSE A   -9  UNP  Q15811              EXPRESSION TAG                 
SEQADV 3FIA GLY A   -8  UNP  Q15811              EXPRESSION TAG                 
SEQADV 3FIA HIS A   -7  UNP  Q15811              EXPRESSION TAG                 
SEQADV 3FIA HIS A   -6  UNP  Q15811              EXPRESSION TAG                 
SEQADV 3FIA HIS A   -5  UNP  Q15811              EXPRESSION TAG                 
SEQADV 3FIA HIS A   -4  UNP  Q15811              EXPRESSION TAG                 
SEQADV 3FIA HIS A   -3  UNP  Q15811              EXPRESSION TAG                 
SEQADV 3FIA HIS A   -2  UNP  Q15811              EXPRESSION TAG                 
SEQADV 3FIA SER A   -1  UNP  Q15811              EXPRESSION TAG                 
SEQADV 3FIA HIS A    0  UNP  Q15811              EXPRESSION TAG                 
SEQADV 3FIA VAL A    1  UNP  Q15811    MET     1 ENGINEERED                     
SEQADV 3FIA THR A   14  UNP  Q15811    ILE    14 ENGINEERED                     
SEQRES   1 A  121  MSE GLY HIS HIS HIS HIS HIS HIS SER HIS VAL ALA GLN          
SEQRES   2 A  121  PHE PRO THR PRO PHE GLY GLY SER LEU ASP THR TRP ALA          
SEQRES   3 A  121  ILE THR VAL GLU GLU ARG ALA LYS HIS ASP GLN GLN PHE          
SEQRES   4 A  121  HIS SER LEU LYS PRO ILE SER GLY PHE ILE THR GLY ASP          
SEQRES   5 A  121  GLN ALA ARG ASN PHE PHE PHE GLN SER GLY LEU PRO GLN          
SEQRES   6 A  121  PRO VAL LEU ALA GLN ILE TRP ALA LEU ALA ASP MSE ASN          
SEQRES   7 A  121  ASN ASP GLY ARG MSE ASP GLN VAL GLU PHE SER ILE ALA          
SEQRES   8 A  121  MSE LYS LEU ILE LYS LEU LYS LEU GLN GLY TYR GLN LEU          
SEQRES   9 A  121  PRO SER ALA LEU PRO PRO VAL MSE LYS GLN GLN PRO VAL          
SEQRES  10 A  121  ALA ILE SER SER                                              
MODRES 3FIA MSE A   67  MET  SELENOMETHIONINE                                   
MODRES 3FIA MSE A   73  MET  SELENOMETHIONINE                                   
MODRES 3FIA MSE A   82  MET  SELENOMETHIONINE                                   
MODRES 3FIA MSE A  102  MET  SELENOMETHIONINE                                   
HET    MSE  A  67       8                                                       
HET    MSE  A  73       8                                                       
HET    MSE  A  82       8                                                       
HET    MSE  A 102       8                                                       
HET     CA  A 201       1                                                       
HET    SO4  A 301       5                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM      CA CALCIUM ION                                                      
HETNAM     SO4 SULFATE ION                                                      
FORMUL   1  MSE    4(C5 H11 N O2 SE)                                            
FORMUL   2   CA    CA 2+                                                        
FORMUL   3  SO4    O4 S 2-                                                      
FORMUL   4  HOH   *133(H2 O)                                                    
HELIX    1   1 THR A   18  LEU A   32  1                                  15    
HELIX    2   2 GLY A   41  PHE A   49  1                                   9    
HELIX    3   3 GLN A   50  GLY A   52  5                                   3    
HELIX    4   4 PRO A   54  ASP A   66  1                                  13    
HELIX    5   5 ASP A   74  GLN A   90  1                                  17    
HELIX    6   6 PRO A   99  LYS A  103  5                                   5    
SHEET    1   A 2 ILE A  39  THR A  40  0                                        
SHEET    2   A 2 ARG A  72  MSE A  73 -1  O  MSE A  73   N  ILE A  39           
LINK         C   ASP A  66                 N   MSE A  67     1555   1555  1.33  
LINK         C   MSE A  67                 N   ASN A  68     1555   1555  1.33  
LINK         C   ARG A  72                 N   MSE A  73     1555   1555  1.33  
LINK         C   MSE A  73                 N   ASP A  74     1555   1555  1.33  
LINK         C   ALA A  81                 N   MSE A  82     1555   1555  1.33  
LINK         C   MSE A  82                 N   LYS A  83     1555   1555  1.33  
LINK         C   VAL A 101                 N   MSE A 102     1555   1555  1.33  
LINK         C   MSE A 102                 N   LYS A 103     1555   1555  1.33  
LINK         OD1 ASP A  66                CA    CA A 201     1555   1555  2.29  
LINK         OD1 ASN A  68                CA    CA A 201     1555   1555  2.39  
LINK         OD1 ASP A  70                CA    CA A 201     1555   1555  2.38  
LINK         O   ARG A  72                CA    CA A 201     1555   1555  2.36  
LINK         OE1 GLU A  77                CA    CA A 201     1555   1555  2.41  
LINK         OE2 GLU A  77                CA    CA A 201     1555   1555  2.50  
LINK        CA    CA A 201                 O   HOH A 403     1555   1555  2.41  
SITE     1 AC1  6 ASP A  66  ASN A  68  ASP A  70  ARG A  72                    
SITE     2 AC1  6 GLU A  77  HOH A 403                                          
SITE     1 AC2  8 GLU A  21  LYS A  86  GLN A  90  PRO A  95                    
SITE     2 AC2  8 SER A  96  HOH A 465  HOH A 485  HOH A 503                    
CRYST1   94.848   32.021   33.287  90.00 106.45  90.00 C 1 2 1       4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.010543  0.000000  0.003113        0.00000                         
SCALE2      0.000000  0.031230  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.031324        0.00000                         
ATOM      1  N   THR A   6      15.234  14.939   8.082  1.00 31.38           N  
ANISOU    1  N   THR A   6     4039   4070   3812     53    108   -120       N  
ATOM      2  CA  THR A   6      15.487  14.155   6.838  1.00 30.26           C  
ANISOU    2  CA  THR A   6     3764   3937   3797    -24     14   -136       C  
ATOM      3  C   THR A   6      14.319  13.218   6.543  1.00 26.71           C  
ANISOU    3  C   THR A   6     3459   3331   3357    118   -124   -206       C  
ATOM      4  O   THR A   6      13.507  12.943   7.423  1.00 27.59           O  
ANISOU    4  O   THR A   6     3498   3225   3758    305   -135   -415       O  
ATOM      5  CB  THR A   6      16.784  13.364   6.967  1.00 32.07           C  
ANISOU    5  CB  THR A   6     4096   4212   3877     21     -7      8       C  
ATOM      6  N   PRO A   7      14.259  12.694   5.307  1.00 27.18           N  
ANISOU    6  N   PRO A   7     3454   3377   3494    224   -135   -105       N  
ATOM      7  CA  PRO A   7      13.325  11.631   4.939  1.00 25.35           C  
ANISOU    7  CA  PRO A   7     3266   3043   3323    195    -17     41       C  
ATOM      8  C   PRO A   7      13.567  10.318   5.691  1.00 24.05           C  
ANISOU    8  C   PRO A   7     3060   2891   3184    235    -19     -3       C  
ATOM      9  O   PRO A   7      12.648   9.509   5.805  1.00 26.41           O  
ANISOU    9  O   PRO A   7     3254   3144   3637    333    168    -92       O  
ATOM     10  CB  PRO A   7      13.572  11.437   3.436  1.00 26.88           C  
ANISOU   10  CB  PRO A   7     3395   3378   3436    262   -111     26       C  
ATOM     11  CG  PRO A   7      14.829  12.188   3.122  1.00 27.07           C  
ANISOU   11  CG  PRO A   7     3632   3287   3366    108   -186    -69       C  
ATOM     12  CD  PRO A   7      14.945  13.265   4.138  1.00 27.48           C  
ANISOU   12  CD  PRO A   7     3485   3521   3435     72    -88   -185       C  
ATOM     13  N   PHE A   8      14.749  10.181   6.292  1.00 20.08           N  
ANISOU   13  N   PHE A   8     2475   2821   2332    346      3   -136       N  
ATOM     14  CA  PHE A   8      15.218   8.916   6.874  1.00 16.66           C  
ANISOU   14  CA  PHE A   8     2003   2304   2023    -30    311   -228       C  
ATOM     15  C   PHE A   8      15.222   8.960   8.397  1.00 19.53           C  
ANISOU   15  C   PHE A   8     2333   2613   2474     18     57   -223       C  
ATOM     16  O   PHE A   8      15.781   8.084   9.048  1.00 18.82           O  
ANISOU   16  O   PHE A   8     2476   2608   2065   -276    140   -173       O  
ATOM     17  CB  PHE A   8      16.639   8.598   6.379  1.00 13.48           C  
ANISOU   17  CB  PHE A   8     1685   1840   1596     35    115   -252       C  
ATOM     18  CG  PHE A   8      16.728   8.426   4.896  1.00 11.19           C  
ANISOU   18  CG  PHE A   8     1238   1407   1604      0    308      6       C  
ATOM     19  CD1 PHE A   8      16.301   7.243   4.306  1.00 11.26           C  
ANISOU   19  CD1 PHE A   8     1202   1154   1921   -172    148   -110       C  
ATOM     20  CD2 PHE A   8      17.112   9.476   4.085  1.00 12.26           C  
ANISOU   20  CD2 PHE A   8     1215   1752   1689     20    440    -48       C  
ATOM     21  CE1 PHE A   8      16.234   7.116   2.930  1.00 11.51           C  
ANISOU   21  CE1 PHE A   8     1440   1377   1557    253    308     60       C  
ATOM     22  CE2 PHE A   8      17.109   9.337   2.701  1.00 12.30           C  
ANISOU   22  CE2 PHE A   8     1933   1357   1384     59    492   -129       C  
ATOM     23  CZ  PHE A   8      16.639   8.159   2.124  1.00 11.76           C  
ANISOU   23  CZ  PHE A   8     1554   1334   1577     20    207     -7       C  
ATOM     24  N   GLY A   9      14.667  10.031   8.954  1.00 20.68           N  
ANISOU   24  N   GLY A   9     2402   3047   2409     59    156   -601       N  
ATOM     25  CA  GLY A   9      14.643  10.206  10.400  1.00 21.70           C  
ANISOU   25  CA  GLY A   9     2607   3151   2485     -3    153   -409       C  
ATOM     26  C   GLY A   9      15.971  10.685  10.950  1.00 21.93           C  
ANISOU   26  C   GLY A   9     2487   3303   2540     44    121   -300       C  
ATOM     27  O   GLY A   9      16.165  10.709  12.169  1.00 23.53           O  
ANISOU   27  O   GLY A   9     2778   3595   2565    -31    220   -234       O  
ATOM     28  N   GLY A  10      16.851  11.143  10.060  1.00 19.94           N  
ANISOU   28  N   GLY A  10     2249   2888   2439     -3     31   -331       N  
ATOM     29  CA  GLY A  10      18.134  11.721  10.458  1.00 19.61           C  
ANISOU   29  CA  GLY A  10     2197   2778   2474     68    155   -308       C  
ATOM     30  C   GLY A  10      19.182  11.588   9.368  1.00 17.50           C  
ANISOU   30  C   GLY A  10     2177   2532   1939    -31     33   -148       C  
ATOM     31  O   GLY A  10      18.951  10.935   8.352  1.00 19.45           O  
ANISOU   31  O   GLY A  10     2268   2729   2393   -119    207   -534       O  
ATOM     32  N   SER A  11      20.308  12.268   9.553  1.00 17.24           N  
ANISOU   32  N   SER A  11     2017   2484   2047    104   -103   -230       N  
ATOM     33  CA  SER A  11      21.421  12.220   8.612  1.00 15.81           C  
ANISOU   33  CA  SER A  11     2087   2093   1827     44   -105   -232       C  
ATOM     34  C   SER A  11      22.663  11.632   9.276  1.00 15.61           C  
ANISOU   34  C   SER A  11     2019   1941   1970    -39      8   -167       C  
ATOM     35  O   SER A  11      22.661  11.335  10.468  1.00 14.25           O  
ANISOU   35  O   SER A  11     1913   1790   1711   -174     28   -111       O  
ATOM     36  CB  SER A  11      21.750  13.626   8.106  1.00 17.98           C  
ANISOU   36  CB  SER A  11     2548   2237   2044    -64   -105   -100       C  
ATOM     37  OG  SER A  11      22.508  14.337   9.080  1.00 18.66           O  
ANISOU   37  OG  SER A  11     2749   2034   2305    400   -215   -177       O  
ATOM     38  N   LEU A  12      23.758  11.579   8.529  1.00 14.00           N  
ANISOU   38  N   LEU A  12     1882   1639   1798   -229    119   -205       N  
ATOM     39  CA  LEU A  12      25.040  11.193   9.101  1.00 13.17           C  
ANISOU   39  CA  LEU A  12     1752   1614   1638   -201    218   -287       C  
ATOM     40  C   LEU A  12      25.457  12.104  10.252  1.00 13.12           C  
ANISOU   40  C   LEU A  12     1795   1685   1504     71    157   -206       C  
ATOM     41  O   LEU A  12      26.288  11.722  11.079  1.00 15.50           O  
ANISOU   41  O   LEU A  12     2307   1927   1652    218   -208   -315       O  
ATOM     42  CB  LEU A  12      26.117  11.213   8.021  1.00 13.50           C  
ANISOU   42  CB  LEU A  12     1802   1705   1622   -428    422   -429       C  
ATOM     43  CG  LEU A  12      26.059  10.071   7.015  1.00 15.11           C  
ANISOU   43  CG  LEU A  12     1829   2138   1774   -383    303   -504       C  
ATOM     44  CD1 LEU A  12      26.982  10.374   5.851  1.00 18.10           C  
ANISOU   44  CD1 LEU A  12     2030   2562   2284   -872    566   -532       C  
ATOM     45  CD2 LEU A  12      26.438   8.770   7.693  1.00 19.20           C  
ANISOU   45  CD2 LEU A  12     2256   2124   2913   -127    103   -375       C  
ATOM     46  N   ASP A  13      24.933  13.327  10.271  1.00 12.73           N  
ANISOU   46  N   ASP A  13     1835   1577   1426   -125    231   -328       N  
ATOM     47  CA  ASP A  13      25.371  14.314  11.248  1.00 13.36           C  
ANISOU   47  CA  ASP A  13     1886   1645   1543     42    310   -337       C  
ATOM     48  C   ASP A  13      24.381  14.542  12.382  1.00 13.07           C  
ANISOU   48  C   ASP A  13     1730   1687   1548   -246    278   -322       C  
ATOM     49  O   ASP A  13      24.679  15.288  13.313  1.00 15.32           O  
ANISOU   49  O   ASP A  13     2091   1915   1814   -365    312   -794       O  
ATOM     50  CB  ASP A  13      25.696  15.631  10.549  1.00 13.57           C  
ANISOU   50  CB  ASP A  13     2086   1563   1505    -25    532   -335       C  
ATOM     51  CG  ASP A  13      26.898  15.515   9.623  1.00 13.37           C  
ANISOU   51  CG  ASP A  13     2059   1619   1400     34    373   -151       C  
ATOM     52  OD1 ASP A  13      27.907  14.931  10.067  1.00 18.93           O  
ANISOU   52  OD1 ASP A  13     2131   3077   1982    166    311   -180       O  
ATOM     53  OD2 ASP A  13      26.803  15.906   8.440  1.00 14.77           O  
ANISOU   53  OD2 ASP A  13     2220   1837   1552     29    429   -183       O  
ATOM     54  N   THR A  14      23.222  13.885  12.337  1.00 10.91           N  
ANISOU   54  N   THR A  14     1425   1376   1343    -47    390   -179       N  
ATOM     55  CA  THR A  14      22.195  14.147  13.341  1.00 12.08           C  
ANISOU   55  CA  THR A  14     1639   1523   1427    -26     99   -225       C  
ATOM     56  C   THR A  14      22.688  13.826  14.752  1.00 12.39           C  
ANISOU   56  C   THR A  14     1724   1610   1371     48     80   -289       C  
ATOM     57  O   THR A  14      22.587  14.659  15.657  1.00 15.36           O  
ANISOU   57  O   THR A  14     2180   2066   1587    -62    156   -347       O  
ATOM     58  CB  THR A  14      20.902  13.373  13.045  1.00 11.58           C  
ANISOU   58  CB  THR A  14     1578   1410   1411     -2    190   -109       C  
ATOM     59  OG1 THR A  14      20.429  13.738  11.743  1.00 14.87           O  
ANISOU   59  OG1 THR A  14     1938   2072   1638    135     74   -132       O  
ATOM     60  CG2 THR A  14      19.828  13.690  14.096  1.00 12.78           C  
ANISOU   60  CG2 THR A  14     1900   1350   1606     20    200   -259       C  
ATOM     61  N   TRP A  15      23.178  12.606  14.951  1.00 14.43           N  
ANISOU   61  N   TRP A  15     1827   2137   1518     41     55    136       N  
ATOM     62  CA  TRP A  15      23.478  12.125  16.300  1.00 15.64           C  
ANISOU   62  CA  TRP A  15     1795   2488   1658     52    161    178       C  
ATOM     63  C   TRP A  15      24.960  12.140  16.632  1.00 18.32           C  
ANISOU   63  C   TRP A  15     1966   3041   1952     59     70    142       C  
ATOM     64  O   TRP A  15      25.348  11.875  17.761  1.00 22.57           O  
ANISOU   64  O   TRP A  15     2458   3803   2312    -12     18    606       O  
ATOM     65  CB  TRP A  15      22.925  10.720  16.519  1.00 17.83           C  
ANISOU   65  CB  TRP A  15     1934   2541   2300    -30    265    112       C  
ATOM     66  CG  TRP A  15      21.460  10.624  16.328  1.00 16.20           C  
ANISOU   66  CG  TRP A  15     1954   2232   1970    219    295    369       C  
ATOM     67  CD1 TRP A  15      20.483  11.037  17.193  1.00 15.83           C  
ANISOU   67  CD1 TRP A  15     2194   1641   2177    149    329    -87       C  
ATOM     68  CD2 TRP A  15      20.789  10.118  15.177  1.00 14.78           C  
ANISOU   68  CD2 TRP A  15     2329   1059   2226    -33    274     19       C  
ATOM     69  NE1 TRP A  15      19.249  10.791  16.655  1.00 17.90           N  
ANISOU   69  NE1 TRP A  15     2710   1862   2226   -288    147    -94       N  
ATOM     70  CE2 TRP A  15      19.409  10.241  15.409  1.00 15.58           C  
ANISOU   70  CE2 TRP A  15     2256   1434   2228   -200    415     41       C  
ATOM     71  CE3 TRP A  15      21.224   9.582  13.959  1.00 17.64           C  
ANISOU   71  CE3 TRP A  15     2257   1956   2486    -55    650   -171       C  
ATOM     72  CZ2 TRP A  15      18.458   9.883  14.457  1.00 21.35           C  
ANISOU   72  CZ2 TRP A  15     2993   2502   2615   -118    239   -244       C  
ATOM     73  CZ3 TRP A  15      20.281   9.204  13.027  1.00 23.58           C  
ANISOU   73  CZ3 TRP A  15     3176   2722   3060     58    197   -177       C  
ATOM     74  CH2 TRP A  15      18.913   9.325  13.291  1.00 20.71           C  
ANISOU   74  CH2 TRP A  15     2972   2305   2592     36    314   -213       C  
ATOM     75  N   ALA A  16      25.794  12.344  15.624  1.00 16.37           N  
ANISOU   75  N   ALA A  16     1712   2646   1859   -151    214     96       N  
ATOM     76  CA  ALA A  16      27.223  12.473  15.863  1.00 17.35           C  
ANISOU   76  CA  ALA A  16     1922   2752   1918    -19    108      0       C  
ATOM     77  C   ALA A  16      27.543  13.813  16.512  1.00 19.14           C  
ANISOU   77  C   ALA A  16     2140   2855   2276     11     23     69       C  
ATOM     78  O   ALA A  16      26.878  14.820  16.259  1.00 20.08           O  
ANISOU   78  O   ALA A  16     2343   2869   2416    150   -261    -96       O  
ATOM     79  CB  ALA A  16      27.984  12.309  14.568  1.00 18.07           C  
ANISOU   79  CB  ALA A  16     1883   2922   2061   -163    560    -68       C  
ATOM     80  N   ILE A  17      28.540  13.808  17.388  1.00 15.03           N  
ANISOU   80  N   ILE A  17     1630   2442   1637   -148     70    188       N  
ATOM     81  CA  ILE A  17      29.004  15.028  18.024  1.00 15.08           C  
ANISOU   81  CA  ILE A  17     1636   2553   1539    -64    139    393       C  
ATOM     82  C   ILE A  17      30.308  15.475  17.377  1.00 16.54           C  
ANISOU   82  C   ILE A  17     1857   2642   1783   -120    157    292       C  
ATOM     83  O   ILE A  17      31.280  14.724  17.325  1.00 17.38           O  
ANISOU   83  O   ILE A  17     1867   2772   1961   -246    346    364       O  
ATOM     84  CB  ILE A  17      29.191  14.819  19.539  1.00 14.55           C  
ANISOU   84  CB  ILE A  17     1677   2455   1396   -117    256    338       C  
ATOM     85  CG1 ILE A  17      27.854  14.394  20.160  1.00 14.77           C  
ANISOU   85  CG1 ILE A  17     1470   2792   1349   -126    196     44       C  
ATOM     86  CG2 ILE A  17      29.724  16.080  20.180  1.00 16.31           C  
ANISOU   86  CG2 ILE A  17     1924   2500   1771     40      0    288       C  
ATOM     87  CD1 ILE A  17      27.944  13.900  21.588  1.00 15.77           C  
ANISOU   87  CD1 ILE A  17     1911   2625   1455    168    173    241       C  
ATOM     88  N   THR A  18      30.300  16.683  16.831  1.00 14.88           N  
ANISOU   88  N   THR A  18     1662   2702   1289   -336    165    326       N  
ATOM     89  CA  THR A  18      31.457  17.164  16.088  1.00 16.35           C  
ANISOU   89  CA  THR A  18     1785   2878   1547   -263    240    428       C  
ATOM     90  C   THR A  18      32.556  17.606  17.046  1.00 15.70           C  
ANISOU   90  C   THR A  18     1601   2784   1579   -137    134    236       C  
ATOM     91  O   THR A  18      32.316  17.780  18.241  1.00 16.16           O  
ANISOU   91  O   THR A  18     1810   2971   1359      0    294    441       O  
ATOM     92  CB  THR A  18      31.102  18.348  15.173  1.00 16.70           C  
ANISOU   92  CB  THR A  18     1998   2776   1570   -307    -87    443       C  
ATOM     93  OG1 THR A  18      30.725  19.476  15.970  1.00 18.51           O  
ANISOU   93  OG1 THR A  18     2199   2986   1847   -452    184    466       O  
ATOM     94  CG2 THR A  18      29.973  17.983  14.212  1.00 18.22           C  
ANISOU   94  CG2 THR A  18     2318   3234   1371   -370   -253    573       C  
ATOM     95  N   VAL A  19      33.751  17.834  16.514  1.00 17.27           N  
ANISOU   95  N   VAL A  19     1949   2809   1803   -344    160    320       N  
ATOM     96  CA  VAL A  19      34.846  18.359  17.314  1.00 17.07           C  
ANISOU   96  CA  VAL A  19     1768   2862   1853   -255    140    206       C  
ATOM     97  C   VAL A  19      34.481  19.723  17.892  1.00 16.66           C  
ANISOU   97  C   VAL A  19     1694   2690   1943   -316    173    319       C  
ATOM     98  O   VAL A  19      34.749  20.008  19.062  1.00 15.75           O  
ANISOU   98  O   VAL A  19     1637   2521   1824   -469     76    294       O  
ATOM     99  CB  VAL A  19      36.130  18.478  16.473  1.00 19.53           C  
ANISOU   99  CB  VAL A  19     1849   3114   2456   -348     98    -67       C  
ATOM    100  CG1 VAL A  19      37.228  19.177  17.258  1.00 21.25           C  
ANISOU  100  CG1 VAL A  19     2148   3497   2428   -265    -49    137       C  
ATOM    101  CG2 VAL A  19      36.572  17.105  16.004  1.00 21.11           C  
ANISOU  101  CG2 VAL A  19     2204   3092   2724   -227     79     88       C  
ATOM    102  N   GLU A  20      33.868  20.567  17.067  1.00 17.64           N  
ANISOU  102  N   GLU A  20     1619   2959   2122   -229    195    413       N  
ATOM    103  CA  GLU A  20      33.462  21.887  17.517  1.00 19.06           C  
ANISOU  103  CA  GLU A  20     2171   2778   2292   -242     74    472       C  
ATOM    104  C   GLU A  20      32.408  21.805  18.622  1.00 16.56           C  
ANISOU  104  C   GLU A  20     1918   2484   1889   -159    -78    488       C  
ATOM    105  O   GLU A  20      32.458  22.566  19.581  1.00 16.95           O  
ANISOU  105  O   GLU A  20     1941   2725   1771   -349    128    603       O  
ATOM    106  CB  GLU A  20      32.951  22.728  16.342  1.00 22.43           C  
ANISOU  106  CB  GLU A  20     2656   3219   2645    -51    -19    485       C  
ATOM    107  CG  GLU A  20      32.303  24.052  16.750  1.00 27.18           C  
ANISOU  107  CG  GLU A  20     3409   3650   3268    -56     29    277       C  
ATOM    108  CD  GLU A  20      32.034  24.967  15.563  1.00 35.15           C  
ANISOU  108  CD  GLU A  20     4358   4544   4451    -54    -80    174       C  
ATOM    109  OE1 GLU A  20      31.712  24.451  14.471  1.00 39.86           O  
ANISOU  109  OE1 GLU A  20     5278   5346   4521     38   -268    201       O  
ATOM    110  OE2 GLU A  20      32.187  26.199  15.715  1.00 38.13           O  
ANISOU  110  OE2 GLU A  20     5015   4285   5184    203    -54    152       O  
ATOM    111  N   GLU A  21      31.423  20.923  18.455  1.00 15.77           N  
ANISOU  111  N   GLU A  21     1972   2602   1415   -223      0    641       N  
ATOM    112  CA  GLU A  21      30.385  20.750  19.466  1.00 14.35           C  
ANISOU  112  CA  GLU A  21     1585   2284   1583   -118   -120    538       C  
ATOM    113  C   GLU A  21      31.015  20.309  20.779  1.00 13.01           C  
ANISOU  113  C   GLU A  21     1457   2083   1401   -103    -44    315       C  
ATOM    114  O   GLU A  21      30.703  20.851  21.845  1.00 14.05           O  
ANISOU  114  O   GLU A  21     1692   2069   1577     21    124    302       O  
ATOM    115  CB  GLU A  21      29.350  19.724  19.000  1.00 15.29           C  
ANISOU  115  CB  GLU A  21     1770   2519   1520    -51   -237    433       C  
ATOM    116  CG  GLU A  21      28.348  20.291  18.007  1.00 18.17           C  
ANISOU  116  CG  GLU A  21     1896   3011   1996   -133   -236    675       C  
ATOM    117  CD  GLU A  21      27.359  19.257  17.506  1.00 16.30           C  
ANISOU  117  CD  GLU A  21     1962   2495   1733    -85   -172    558       C  
ATOM    118  OE1 GLU A  21      27.754  18.095  17.280  1.00 18.86           O  
ANISOU  118  OE1 GLU A  21     1713   3137   2313     11     28    745       O  
ATOM    119  OE2 GLU A  21      26.208  19.649  17.201  1.00 23.00           O  
ANISOU  119  OE2 GLU A  21     1550   3869   3318     -2   -311    426       O  
ATOM    120  N   ARG A  22      31.891  19.316  20.703  1.00 13.30           N  
ANISOU  120  N   ARG A  22     1330   2079   1643   -246    -61    468       N  
ATOM    121  CA  ARG A  22      32.514  18.792  21.909  1.00 12.83           C  
ANISOU  121  CA  ARG A  22     1395   1934   1543    -79    -93    279       C  
ATOM    122  C   ARG A  22      33.342  19.850  22.626  1.00 12.30           C  
ANISOU  122  C   ARG A  22     1309   1803   1561   -241    151    520       C  
ATOM    123  O   ARG A  22      33.330  19.919  23.853  1.00 14.01           O  
ANISOU  123  O   ARG A  22     1592   2010   1722    -83    -96    438       O  
ATOM    124  CB  ARG A  22      33.353  17.548  21.603  1.00 12.13           C  
ANISOU  124  CB  ARG A  22     1331   1719   1559    174      2    447       C  
ATOM    125  CG  ARG A  22      34.135  16.990  22.785  1.00 12.49           C  
ANISOU  125  CG  ARG A  22     1308   1935   1501    -86    178    426       C  
ATOM    126  CD  ARG A  22      33.227  16.636  23.950  1.00 12.98           C  
ANISOU  126  CD  ARG A  22     1662   2000   1268   -276     92    510       C  
ATOM    127  NE  ARG A  22      33.979  16.035  25.052  1.00 11.06           N  
ANISOU  127  NE  ARG A  22     1244   1540   1416      9    135    491       N  
ATOM    128  CZ  ARG A  22      34.404  14.772  25.079  1.00 12.75           C  
ANISOU  128  CZ  ARG A  22     1522   1853   1468    243     42    -58       C  
ATOM    129  NH1 ARG A  22      33.939  13.890  24.204  1.00 14.19           N  
ANISOU  129  NH1 ARG A  22     1495   2301   1593     67    163    -14       N  
ATOM    130  NH2 ARG A  22      35.231  14.372  26.041  1.00 12.75           N  
ANISOU  130  NH2 ARG A  22     1362   1783   1701     44     61    186       N  
ATOM    131  N   ALA A  23      33.990  20.725  21.858  1.00 13.89           N  
ANISOU  131  N   ALA A  23     1445   1856   1974   -271    -96    546       N  
ATOM    132  CA  ALA A  23      34.775  21.794  22.464  1.00 14.62           C  
ANISOU  132  CA  ALA A  23     1777   1785   1991   -527      2    547       C  
ATOM    133  C   ALA A  23      33.879  22.778  23.227  1.00 14.73           C  
ANISOU  133  C   ALA A  23     1746   1794   2056   -254   -118    516       C  
ATOM    134  O   ALA A  23      34.209  23.201  24.339  1.00 15.92           O  
ANISOU  134  O   ALA A  23     1947   1926   2176   -382    -66    654       O  
ATOM    135  CB  ALA A  23      35.610  22.519  21.403  1.00 15.94           C  
ANISOU  135  CB  ALA A  23     1935   1900   2221   -498    104    513       C  
ATOM    136  N   LYS A  24      32.718  23.100  22.655  1.00 14.92           N  
ANISOU  136  N   LYS A  24     1844   1920   1904   -210   -161    692       N  
ATOM    137  CA  LYS A  24      31.719  23.914  23.346  1.00 15.50           C  
ANISOU  137  CA  LYS A  24     2120   1910   1857   -220   -142    585       C  
ATOM    138  C   LYS A  24      31.188  23.227  24.614  1.00 14.29           C  
ANISOU  138  C   LYS A  24     2067   1484   1878   -212    -16    442       C  
ATOM    139  O   LYS A  24      31.066  23.846  25.672  1.00 16.86           O  
ANISOU  139  O   LYS A  24     2145   2074   2184   -187      0    417       O  
ATOM    140  CB  LYS A  24      30.568  24.280  22.401  1.00 16.98           C  
ANISOU  140  CB  LYS A  24     2243   2063   2145   -295    -94    732       C  
ATOM    141  CG  LYS A  24      30.965  25.244  21.277  1.00 21.31           C  
ANISOU  141  CG  LYS A  24     2527   3035   2534   -188    -22    656       C  
ATOM    142  CD  LYS A  24      29.743  25.747  20.514  1.00 25.33           C  
ANISOU  142  CD  LYS A  24     2993   3450   3181     39    -32    521       C  
ATOM    143  CE  LYS A  24      28.769  26.468  21.445  1.00 33.13           C  
ANISOU  143  CE  LYS A  24     3920   4447   4219     88    142   -132       C  
ATOM    144  NZ  LYS A  24      27.428  25.808  21.506  1.00 38.80           N  
ANISOU  144  NZ  LYS A  24     4611   5058   5070   -222    -89    103       N  
ATOM    145  N   HIS A  25      30.886  21.939  24.509  1.00 13.57           N  
ANISOU  145  N   HIS A  25     1895   1536   1722   -121    -39    460       N  
ATOM    146  CA  HIS A  25      30.403  21.194  25.662  1.00 12.65           C  
ANISOU  146  CA  HIS A  25     1818   1698   1289    -52    -86    307       C  
ATOM    147  C   HIS A  25      31.443  21.190  26.774  1.00 12.04           C  
ANISOU  147  C   HIS A  25     1490   1582   1502   -112   -127    181       C  
ATOM    148  O   HIS A  25      31.113  21.404  27.932  1.00 12.48           O  
ANISOU  148  O   HIS A  25     1620   1579   1543   -224   -166    133       O  
ATOM    149  CB  HIS A  25      30.087  19.766  25.259  1.00 12.34           C  
ANISOU  149  CB  HIS A  25     1699   1630   1357    -70   -160     73       C  
ATOM    150  CG  HIS A  25      29.029  19.662  24.208  1.00 11.27           C  
ANISOU  150  CG  HIS A  25     1345   1750   1184    -97      7    332       C  
ATOM    151  ND1 HIS A  25      28.862  18.534  23.435  1.00 12.49           N  
ANISOU  151  ND1 HIS A  25     1564   1944   1235   -278     84    368       N  
ATOM    152  CD2 HIS A  25      28.110  20.559  23.774  1.00 12.86           C  
ANISOU  152  CD2 HIS A  25     1648   1782   1455   -193    131    459       C  
ATOM    153  CE1 HIS A  25      27.873  18.733  22.584  1.00 12.61           C  
ANISOU  153  CE1 HIS A  25     1430   2092   1269    -90    -43    392       C  
ATOM    154  NE2 HIS A  25      27.432  19.971  22.734  1.00 13.46           N  
ANISOU  154  NE2 HIS A  25     1798   1867   1447    -50    110    372       N  
ATOM    155  N   ASP A  26      32.707  20.986  26.407  1.00 13.41           N  
ANISOU  155  N   ASP A  26     1611   1751   1732   -156   -171    227       N  
ATOM    156  CA  ASP A  26      33.777  20.925  27.387  1.00 13.80           C  
ANISOU  156  CA  ASP A  26     1707   1710   1826   -108   -250    137       C  
ATOM    157  C   ASP A  26      33.916  22.254  28.121  1.00 13.72           C  
ANISOU  157  C   ASP A  26     1804   1627   1780   -352   -448    308       C  
ATOM    158  O   ASP A  26      34.213  22.289  29.313  1.00 15.88           O  
ANISOU  158  O   ASP A  26     1999   2139   1893   -388   -229    319       O  
ATOM    159  CB  ASP A  26      35.105  20.532  26.728  1.00 14.64           C  
ANISOU  159  CB  ASP A  26     1630   1995   1937   -173    -38    161       C  
ATOM    160  CG  ASP A  26      35.144  19.072  26.302  1.00 13.64           C  
ANISOU  160  CG  ASP A  26     1306   2141   1733   -202   -265    214       C  
ATOM    161  OD1 ASP A  26      34.216  18.318  26.653  1.00 12.77           O  
ANISOU  161  OD1 ASP A  26     1222   1953   1674   -240     52    396       O  
ATOM    162  OD2 ASP A  26      36.102  18.671  25.597  1.00 15.86           O  
ANISOU  162  OD2 ASP A  26     1570   2649   1807    163    -10    400       O  
ATOM    163  N   GLN A  27      33.709  23.350  27.400  1.00 15.49           N  
ANISOU  163  N   GLN A  27     2030   1605   2249   -342   -525    149       N  
ATOM    164  CA  GLN A  27      33.736  24.669  28.022  1.00 17.67           C  
ANISOU  164  CA  GLN A  27     2445   1771   2498   -269   -318    222       C  
ATOM    165  C   GLN A  27      32.601  24.857  29.030  1.00 17.61           C  
ANISOU  165  C   GLN A  27     2362   2017   2312    -72   -447    186       C  
ATOM    166  O   GLN A  27      32.809  25.392  30.121  1.00 18.75           O  
ANISOU  166  O   GLN A  27     2605   1943   2576   -508   -300    231       O  
ATOM    167  CB  GLN A  27      33.697  25.768  26.959  1.00 19.11           C  
ANISOU  167  CB  GLN A  27     2762   1881   2616   -314   -144    303       C  
ATOM    168  CG  GLN A  27      35.016  25.967  26.232  1.00 26.54           C  
ANISOU  168  CG  GLN A  27     3343   3110   3630    -10   -152     85       C  
ATOM    169  CD  GLN A  27      36.124  26.473  27.145  1.00 32.77           C  
ANISOU  169  CD  GLN A  27     4125   4017   4306    -85   -284    157       C  
ATOM    170  OE1 GLN A  27      35.864  27.107  28.170  1.00 31.21           O  
ANISOU  170  OE1 GLN A  27     4354   3491   4013   -362   -346    163       O  
ATOM    171  NE2 GLN A  27      37.369  26.197  26.771  1.00 38.05           N  
ANISOU  171  NE2 GLN A  27     4689   4813   4953    -28   -161    292       N  
ATOM    172  N   GLN A  28      31.398  24.415  28.664  1.00 16.59           N  
ANISOU  172  N   GLN A  28     2234   1639   2428   -407   -340    311       N  
ATOM    173  CA  GLN A  28      30.255  24.496  29.571  1.00 16.48           C  
ANISOU  173  CA  GLN A  28     2253   1721   2288    -94   -460    173       C  
ATOM    174  C   GLN A  28      30.458  23.582  30.780  1.00 14.55           C  
ANISOU  174  C   GLN A  28     1873   1464   2190    -19   -284    134       C  
ATOM    175  O   GLN A  28      30.137  23.947  31.906  1.00 16.84           O  
ANISOU  175  O   GLN A  28     2446   1667   2283    -25   -199    129       O  
ATOM    176  CB  GLN A  28      28.946  24.152  28.845  1.00 17.70           C  
ANISOU  176  CB  GLN A  28     2611   1450   2661   -237   -566    207       C  
ATOM    177  CG  GLN A  28      28.408  25.254  27.936  1.00 20.00           C  
ANISOU  177  CG  GLN A  28     3055   1962   2580   -115   -275    191       C  
ATOM    178  CD  GLN A  28      28.190  26.559  28.677  1.00 27.13           C  
ANISOU  178  CD  GLN A  28     3755   3049   3502     27     43    -35       C  
ATOM    179  OE1 GLN A  28      27.453  26.610  29.663  1.00 30.88           O  
ANISOU  179  OE1 GLN A  28     3846   3776   4107    223    175    -11       O  
ATOM    180  NE2 GLN A  28      28.876  27.610  28.240  1.00 32.69           N  
ANISOU  180  NE2 GLN A  28     4483   3704   4233   -114     55    251       N  
ATOM    181  N   PHE A  29      31.009  22.398  30.550  1.00 13.52           N  
ANISOU  181  N   PHE A  29     1880   1327   1928   -134   -256    146       N  
ATOM    182  CA  PHE A  29      31.259  21.472  31.642  1.00 12.67           C  
ANISOU  182  CA  PHE A  29     1773   1443   1596   -106   -252    -62       C  
ATOM    183  C   PHE A  29      32.218  22.088  32.654  1.00 13.37           C  
ANISOU  183  C   PHE A  29     1919   1443   1715    -87   -154    -37       C  
ATOM    184  O   PHE A  29      31.979  22.040  33.858  1.00 14.46           O  
ANISOU  184  O   PHE A  29     2020   1801   1670   -214   -297   -406       O  
ATOM    185  CB  PHE A  29      31.848  20.176  31.081  1.00 11.16           C  
ANISOU  185  CB  PHE A  29     1705    961   1571    126     -5    -93       C  
ATOM    186  CG  PHE A  29      31.957  19.056  32.096  1.00 10.71           C  
ANISOU  186  CG  PHE A  29     1437   1409   1222   -194   -365    -15       C  
ATOM    187  CD1 PHE A  29      30.825  18.544  32.710  1.00 10.59           C  
ANISOU  187  CD1 PHE A  29     1448   1320   1253   -129     35   -154       C  
ATOM    188  CD2 PHE A  29      33.189  18.507  32.417  1.00 11.50           C  
ANISOU  188  CD2 PHE A  29     1249   1667   1453   -196    -48     17       C  
ATOM    189  CE1 PHE A  29      30.912  17.465  33.584  1.00 10.99           C  
ANISOU  189  CE1 PHE A  29     1507   1391   1276   -208   -102   -302       C  
ATOM    190  CE2 PHE A  29      33.296  17.473  33.344  1.00 12.52           C  
ANISOU  190  CE2 PHE A  29     1399   1583   1774   -180   -119    -13       C  
ATOM    191  CZ  PHE A  29      32.150  16.932  33.901  1.00 11.02           C  
ANISOU  191  CZ  PHE A  29     1615   1400   1171   -223    -42    -29       C  
ATOM    192  N   HIS A  30      33.281  22.704  32.149  1.00 14.43           N  
ANISOU  192  N   HIS A  30     1955   1713   1815   -367   -353   -224       N  
ATOM    193  CA  HIS A  30      34.260  23.357  33.008  1.00 16.21           C  
ANISOU  193  CA  HIS A  30     2131   1853   2175   -326   -213   -163       C  
ATOM    194  C   HIS A  30      33.636  24.460  33.861  1.00 17.62           C  
ANISOU  194  C   HIS A  30     2274   2015   2405    -48   -248   -138       C  
ATOM    195  O   HIS A  30      33.976  24.616  35.033  1.00 18.23           O  
ANISOU  195  O   HIS A  30     2586   1904   2435   -193   -406   -180       O  
ATOM    196  CB  HIS A  30      35.401  23.921  32.169  1.00 17.23           C  
ANISOU  196  CB  HIS A  30     2061   2190   2295   -365   -295     82       C  
ATOM    197  CG  HIS A  30      36.479  24.567  32.979  1.00 18.71           C  
ANISOU  197  CG  HIS A  30     2522   2144   2439   -267   -258   -273       C  
ATOM    198  ND1 HIS A  30      37.322  23.848  33.799  1.00 19.69           N  
ANISOU  198  ND1 HIS A  30     2264   2897   2320   -124   -189   -322       N  
ATOM    199  CD2 HIS A  30      36.868  25.860  33.078  1.00 24.41           C  
ANISOU  199  CD2 HIS A  30     2976   2867   3431   -166   -149   -171       C  
ATOM    200  CE1 HIS A  30      38.174  24.673  34.382  1.00 23.07           C  
ANISOU  200  CE1 HIS A  30     2594   3159   3009   -313   -172    -92       C  
ATOM    201  NE2 HIS A  30      37.922  25.899  33.958  1.00 23.24           N  
ANISOU  201  NE2 HIS A  30     2777   2985   3066    -34   -561    -39       N  
ATOM    202  N   SER A  31      32.676  25.180  33.290  1.00 18.56           N  
ANISOU  202  N   SER A  31     2589   1915   2547     -6   -380   -104       N  
ATOM    203  CA  SER A  31      32.015  26.270  33.999  1.00 19.69           C  
ANISOU  203  CA  SER A  31     2771   2100   2609     34   -267   -245       C  
ATOM    204  C   SER A  31      31.225  25.794  35.219  1.00 19.86           C  
ANISOU  204  C   SER A  31     2666   2209   2670     27   -169   -379       C  
ATOM    205  O   SER A  31      30.948  26.577  36.129  1.00 20.81           O  
ANISOU  205  O   SER A  31     2830   2179   2895    -76    -71   -520       O  
ATOM    206  CB  SER A  31      31.099  27.045  33.049  1.00 22.82           C  
ANISOU  206  CB  SER A  31     3015   2431   3223    104   -377    -19       C  
ATOM    207  OG  SER A  31      29.815  26.444  32.967  1.00 25.57           O  
ANISOU  207  OG  SER A  31     3539   2590   3587    -65   -438     19       O  
ATOM    208  N   LEU A  32      30.876  24.509  35.240  1.00 16.87           N  
ANISOU  208  N   LEU A  32     2381   1826   2200    -86   -227   -254       N  
ATOM    209  CA  LEU A  32      30.163  23.924  36.375  1.00 17.46           C  
ANISOU  209  CA  LEU A  32     2285   1984   2362    -76   -122   -572       C  
ATOM    210  C   LEU A  32      31.102  23.514  37.507  1.00 18.71           C  
ANISOU  210  C   LEU A  32     2523   2178   2408     -2    -73   -409       C  
ATOM    211  O   LEU A  32      30.651  23.014  38.538  1.00 19.59           O  
ANISOU  211  O   LEU A  32     2643   2592   2208    -11     32   -396       O  
ATOM    212  CB  LEU A  32      29.324  22.721  35.928  1.00 17.99           C  
ANISOU  212  CB  LEU A  32     2610   1770   2453   -178   -232   -457       C  
ATOM    213  CG  LEU A  32      28.202  23.025  34.936  1.00 18.20           C  
ANISOU  213  CG  LEU A  32     2173   1718   3023      0   -224   -575       C  
ATOM    214  CD1 LEU A  32      27.485  21.747  34.519  1.00 18.31           C  
ANISOU  214  CD1 LEU A  32     2357   2196   2401   -272   -353   -695       C  
ATOM    215  CD2 LEU A  32      27.216  24.037  35.525  1.00 20.25           C  
ANISOU  215  CD2 LEU A  32     2555   2297   2840     82   -242   -612       C  
ATOM    216  N   LYS A  33      32.404  23.710  37.302  1.00 17.41           N  
ANISOU  216  N   LYS A  33     2211   2229   2172    -46   -249   -467       N  
ATOM    217  CA  LYS A  33      33.415  23.361  38.302  1.00 19.76           C  
ANISOU  217  CA  LYS A  33     2609   2522   2375    -60   -306   -265       C  
ATOM    218  C   LYS A  33      33.312  21.901  38.743  1.00 17.13           C  
ANISOU  218  C   LYS A  33     2127   2436   1942    -66   -322   -236       C  
ATOM    219  O   LYS A  33      33.151  21.609  39.929  1.00 20.13           O  
ANISOU  219  O   LYS A  33     2364   2884   2399    -11    -85   -260       O  
ATOM    220  CB  LYS A  33      33.324  24.292  39.515  1.00 22.05           C  
ANISOU  220  CB  LYS A  33     3008   2678   2691    107   -255   -253       C  
ATOM    221  CG  LYS A  33      33.319  25.773  39.162  1.00 28.91           C  
ANISOU  221  CG  LYS A  33     4009   3439   3534     68   -169     37       C  
ATOM    222  CD  LYS A  33      34.736  26.300  38.977  1.00 37.37           C  
ANISOU  222  CD  LYS A  33     4570   4663   4964   -135     39     27       C  
ATOM    223  CE  LYS A  33      34.736  27.742  38.484  1.00 39.27           C  
ANISOU  223  CE  LYS A  33     4902   4834   5185   -119     -5     99       C  
ATOM    224  NZ  LYS A  33      36.117  28.246  38.225  1.00 42.52           N  
ANISOU  224  NZ  LYS A  33     5188   5371   5595    -57    106    107       N  
ATOM    225  N   PRO A  34      33.484  20.972  37.798  1.00 15.15           N  
ANISOU  225  N   PRO A  34     1815   2193   1749   -141   -160   -139       N  
ATOM    226  CA  PRO A  34      33.500  19.562  38.173  1.00 14.28           C  
ANISOU  226  CA  PRO A  34     1686   2224   1516    -56   -152   -114       C  
ATOM    227  C   PRO A  34      34.586  19.292  39.205  1.00 15.11           C  
ANISOU  227  C   PRO A  34     1754   2460   1524   -142    -99    -77       C  
ATOM    228  O   PRO A  34      35.628  19.950  39.196  1.00 15.65           O  
ANISOU  228  O   PRO A  34     1601   2649   1697   -236   -199   -181       O  
ATOM    229  CB  PRO A  34      33.826  18.845  36.860  1.00 14.16           C  
ANISOU  229  CB  PRO A  34     1820   1971   1589    -98   -210   -255       C  
ATOM    230  CG  PRO A  34      33.616  19.861  35.775  1.00 17.63           C  
ANISOU  230  CG  PRO A  34     2498   2113   2085    -30    190    -52       C  
ATOM    231  CD  PRO A  34      33.850  21.189  36.390  1.00 15.46           C  
ANISOU  231  CD  PRO A  34     1947   2423   1504   -194   -259   -351       C  
ATOM    232  N   ILE A  35      34.368  18.275  40.027  1.00 14.17           N  
ANISOU  232  N   ILE A  35     1595   2402   1384    -41   -174      3       N  
ATOM    233  CA  ILE A  35      35.336  17.876  41.035  1.00 15.08           C  
ANISOU  233  CA  ILE A  35     1658   2564   1507    -75     59     27       C  
ATOM    234  C   ILE A  35      35.995  16.587  40.576  1.00 12.81           C  
ANISOU  234  C   ILE A  35     1319   2098   1448   -150     70    136       C  
ATOM    235  O   ILE A  35      35.323  15.575  40.397  1.00 13.26           O  
ANISOU  235  O   ILE A  35     1504   2157   1375   -113     97   -161       O  
ATOM    236  CB  ILE A  35      34.653  17.638  42.403  1.00 14.45           C  
ANISOU  236  CB  ILE A  35     1518   2550   1420      7    -38    220       C  
ATOM    237  CG1 ILE A  35      33.938  18.909  42.862  1.00 16.34           C  
ANISOU  237  CG1 ILE A  35     1740   2629   1840    -10    -11    -77       C  
ATOM    238  CG2 ILE A  35      35.688  17.220  43.444  1.00 16.05           C  
ANISOU  238  CG2 ILE A  35     1247   2938   1912    221   -361    200       C  
ATOM    239  CD1 ILE A  35      33.123  18.736  44.133  1.00 19.08           C  
ANISOU  239  CD1 ILE A  35     2163   2901   2183     71    254   -101       C  
ATOM    240  N   SER A  36      37.289  16.664  40.266  1.00 13.77           N  
ANISOU  240  N   SER A  36     1325   2375   1531   -151    139   -129       N  
ATOM    241  CA  SER A  36      38.007  15.515  39.721  1.00 13.62           C  
ANISOU  241  CA  SER A  36     1403   2112   1659    -98   -113    -36       C  
ATOM    242  C   SER A  36      37.296  14.941  38.504  1.00 13.79           C  
ANISOU  242  C   SER A  36     1286   2308   1644   -119    -68    -55       C  
ATOM    243  O   SER A  36      37.233  13.725  38.334  1.00 15.63           O  
ANISOU  243  O   SER A  36     1418   2383   2136   -187    -13     22       O  
ATOM    244  CB  SER A  36      38.194  14.419  40.773  1.00 13.87           C  
ANISOU  244  CB  SER A  36     1507   2036   1725   -132     12    141       C  
ATOM    245  OG  SER A  36      39.215  14.752  41.698  1.00 17.79           O  
ANISOU  245  OG  SER A  36     2263   2471   2025   -125   -233    234       O  
ATOM    246  N   GLY A  37      36.718  15.819  37.690  1.00 12.60           N  
ANISOU  246  N   GLY A  37     1078   2195   1511    -38   -190    -37       N  
ATOM    247  CA  GLY A  37      36.146  15.410  36.407  1.00 14.01           C  
ANISOU  247  CA  GLY A  37     1148   2597   1577   -170   -109   -112       C  
ATOM    248  C   GLY A  37      34.686  14.979  36.453  1.00 12.53           C  
ANISOU  248  C   GLY A  37     1113   2342   1306      2     13     12       C  
ATOM    249  O   GLY A  37      34.164  14.488  35.462  1.00 12.60           O  
ANISOU  249  O   GLY A  37     1286   2165   1335    -14   -164    -49       O  
ATOM    250  N   PHE A  38      34.036  15.133  37.605  1.00 11.97           N  
ANISOU  250  N   PHE A  38     1215   1914   1419   -128    139   -133       N  
ATOM    251  CA  PHE A  38      32.645  14.707  37.754  1.00 11.19           C  
ANISOU  251  CA  PHE A  38     1106   1905   1238     -5     -2    -16       C  
ATOM    252  C   PHE A  38      31.785  15.832  38.303  1.00 11.14           C  
ANISOU  252  C   PHE A  38     1119   1837   1277    -94     49    -17       C  
ATOM    253  O   PHE A  38      32.203  16.557  39.211  1.00 11.90           O  
ANISOU  253  O   PHE A  38     1182   1851   1487   -108   -181    -51       O  
ATOM    254  CB  PHE A  38      32.544  13.501  38.700  1.00 12.99           C  
ANISOU  254  CB  PHE A  38     1699   2020   1215    -23     23     75       C  
ATOM    255  CG  PHE A  38      33.186  12.258  38.166  1.00 14.56           C  
ANISOU  255  CG  PHE A  38     1739   1976   1815    202   -115    208       C  
ATOM    256  CD1 PHE A  38      32.504  11.424  37.296  1.00 12.44           C  
ANISOU  256  CD1 PHE A  38     1294   1924   1506     80    166    110       C  
ATOM    257  CD2 PHE A  38      34.466  11.904  38.559  1.00 15.44           C  
ANISOU  257  CD2 PHE A  38     1582   2078   2203    344     99    370       C  
ATOM    258  CE1 PHE A  38      33.085  10.255  36.820  1.00 16.14           C  
ANISOU  258  CE1 PHE A  38     1766   2213   2151    177   -137    270       C  
ATOM    259  CE2 PHE A  38      35.057  10.744  38.083  1.00 17.60           C  
ANISOU  259  CE2 PHE A  38     2077   2128   2482    414   -149    145       C  
ATOM    260  CZ  PHE A  38      34.378   9.930  37.200  1.00 17.63           C  
ANISOU  260  CZ  PHE A  38     2054   2194   2450    209    104    130       C  
ATOM    261  N   ILE A  39      30.545  15.895  37.820  1.00 11.16           N  
ANISOU  261  N   ILE A  39     1008   1933   1296    116    -50     19       N  
ATOM    262  CA  ILE A  39      29.479  16.611  38.522  1.00 11.64           C  
ANISOU  262  CA  ILE A  39     1208   1764   1451    111    -12    163       C  
ATOM    263  C   ILE A  39      28.434  15.630  39.034  1.00 10.90           C  
ANISOU  263  C   ILE A  39     1330   1621   1187    119     -6     23       C  
ATOM    264  O   ILE A  39      28.309  14.513  38.526  1.00 11.36           O  
ANISOU  264  O   ILE A  39     1347   1762   1203    147    -26     99       O  
ATOM    265  CB  ILE A  39      28.812  17.689  37.632  1.00 11.07           C  
ANISOU  265  CB  ILE A  39     1185   1620   1400    -18    -80    126       C  
ATOM    266  CG1 ILE A  39      28.158  17.055  36.395  1.00 12.57           C  
ANISOU  266  CG1 ILE A  39     1343   1843   1587     28   -113    216       C  
ATOM    267  CG2 ILE A  39      29.838  18.728  37.222  1.00 13.60           C  
ANISOU  267  CG2 ILE A  39     1534   1698   1933   -131     90    163       C  
ATOM    268  CD1 ILE A  39      27.497  18.054  35.473  1.00 13.12           C  
ANISOU  268  CD1 ILE A  39     1554   1879   1552    -64     44    446       C  
ATOM    269  N   THR A  40      27.759  15.995  40.117  1.00 11.84           N  
ANISOU  269  N   THR A  40     1305   2186   1005    -68     27     45       N  
ATOM    270  CA  THR A  40      26.736  15.110  40.658  1.00 11.88           C  
ANISOU  270  CA  THR A  40     1444   1831   1237    -65      2     98       C  
ATOM    271  C   THR A  40      25.533  15.083  39.725  1.00 11.44           C  
ANISOU  271  C   THR A  40     1307   1638   1398    -75     -9    -23       C  
ATOM    272  O   THR A  40      25.322  16.001  38.940  1.00 11.17           O  
ANISOU  272  O   THR A  40     1519   1531   1193    -55     46    -17       O  
ATOM    273  CB  THR A  40      26.275  15.546  42.053  1.00 12.68           C  
ANISOU  273  CB  THR A  40     1571   2089   1156     87   -134     72       C  
ATOM    274  OG1 THR A  40      25.658  16.836  41.972  1.00 14.41           O  
ANISOU  274  OG1 THR A  40     1783   2169   1521     35    -35   -140       O  
ATOM    275  CG2 THR A  40      27.453  15.589  43.010  1.00 15.52           C  
ANISOU  275  CG2 THR A  40     1787   2586   1520     54   -288    180       C  
ATOM    276  N   GLY A  41      24.716  14.045  39.838  1.00 11.93           N  
ANISOU  276  N   GLY A  41     1260   1814   1458   -278    163    237       N  
ATOM    277  CA  GLY A  41      23.480  13.994  39.073  1.00 11.18           C  
ANISOU  277  CA  GLY A  41     1125   1800   1319    -51    -87     46       C  
ATOM    278  C   GLY A  41      22.588  15.189  39.344  1.00 11.50           C  
ANISOU  278  C   GLY A  41     1345   1824   1198   -219    -21    -53       C  
ATOM    279  O   GLY A  41      22.017  15.759  38.420  1.00 12.04           O  
ANISOU  279  O   GLY A  41     1339   1853   1380   -111    -18    163       O  
ATOM    280  N   ASP A  42      22.474  15.597  40.604  1.00 11.82           N  
ANISOU  280  N   ASP A  42     1355   1849   1286   -241     57    -87       N  
ATOM    281  CA  ASP A  42      21.600  16.727  40.899  1.00 13.01           C  
ANISOU  281  CA  ASP A  42     1777   1967   1197    -46    109    -81       C  
ATOM    282  C   ASP A  42      22.127  18.019  40.294  1.00 12.80           C  
ANISOU  282  C   ASP A  42     1561   2128   1175   -120    114   -182       C  
ATOM    283  O   ASP A  42      21.369  18.816  39.761  1.00 12.62           O  
ANISOU  283  O   ASP A  42     1724   2147    924     61     67   -146       O  
ATOM    284  CB  ASP A  42      21.359  16.886  42.401  1.00 15.32           C  
ANISOU  284  CB  ASP A  42     2193   2438   1190    -40    218   -162       C  
ATOM    285  CG  ASP A  42      22.630  17.150  43.171  1.00 19.51           C  
ANISOU  285  CG  ASP A  42     2689   2706   2017   -102   -110    103       C  
ATOM    286  OD1 ASP A  42      23.378  16.181  43.411  1.00 25.43           O  
ANISOU  286  OD1 ASP A  42     3013   3617   3029    327   -275   -302       O  
ATOM    287  OD2 ASP A  42      22.858  18.313  43.582  1.00 26.29           O  
ANISOU  287  OD2 ASP A  42     3852   3504   2631    -51   -128   -261       O  
ATOM    288  N   GLN A  43      23.445  18.168  40.283  1.00 12.70           N  
ANISOU  288  N   GLN A  43     1577   2093   1152   -112     95     24       N  
ATOM    289  CA  GLN A  43      24.062  19.321  39.664  1.00 12.56           C  
ANISOU  289  CA  GLN A  43     1601   1811   1359   -174    -22    -94       C  
ATOM    290  C   GLN A  43      23.800  19.354  38.165  1.00 10.83           C  
ANISOU  290  C   GLN A  43     1344   1512   1258   -171     10   -119       C  
ATOM    291  O   GLN A  43      23.474  20.397  37.602  1.00 12.27           O  
ANISOU  291  O   GLN A  43     1648   1538   1474   -200     12    -33       O  
ATOM    292  CB  GLN A  43      25.561  19.264  39.924  1.00 14.64           C  
ANISOU  292  CB  GLN A  43     1534   2230   1798   -499    -13   -190       C  
ATOM    293  CG  GLN A  43      26.355  20.462  39.503  1.00 22.19           C  
ANISOU  293  CG  GLN A  43     2755   3022   2652   -261     39    -54       C  
ATOM    294  CD  GLN A  43      27.799  20.302  39.912  1.00 23.57           C  
ANISOU  294  CD  GLN A  43     2757   3272   2924    175   -251   -145       C  
ATOM    295  OE1 GLN A  43      28.163  19.312  40.566  1.00 23.07           O  
ANISOU  295  OE1 GLN A  43     2336   3192   3238    -88   -331   -970       O  
ATOM    296  NE2 GLN A  43      28.623  21.289  39.582  1.00 27.04           N  
ANISOU  296  NE2 GLN A  43     3336   3843   3092    -79    -13   -211       N  
ATOM    297  N   ALA A  44      24.011  18.222  37.510  1.00 10.11           N  
ANISOU  297  N   ALA A  44     1260   1590    990   -166     16   -117       N  
ATOM    298  CA  ALA A  44      23.765  18.127  36.081  1.00  8.81           C  
ANISOU  298  CA  ALA A  44     1229   1349    768   -128     60    -11       C  
ATOM    299  C   ALA A  44      22.311  18.445  35.758  1.00  9.54           C  
ANISOU  299  C   ALA A  44     1338   1383    904    -93    242    176       C  
ATOM    300  O   ALA A  44      22.022  19.256  34.878  1.00  9.83           O  
ANISOU  300  O   ALA A  44     1554   1114   1067     74    123     31       O  
ATOM    301  CB  ALA A  44      24.126  16.735  35.585  1.00 10.84           C  
ANISOU  301  CB  ALA A  44     1510   1416   1190    139    208      3       C  
ATOM    302  N   ARG A  45      21.392  17.800  36.471  1.00  9.04           N  
ANISOU  302  N   ARG A  45     1107   1230   1097    -37    219     -7       N  
ATOM    303  CA  ARG A  45      19.982  17.962  36.160  1.00  9.46           C  
ANISOU  303  CA  ARG A  45     1140   1281   1172    -22    160    -15       C  
ATOM    304  C   ARG A  45      19.510  19.388  36.431  1.00 10.49           C  
ANISOU  304  C   ARG A  45     1438   1515   1030    -50    149   -173       C  
ATOM    305  O   ARG A  45      18.736  19.951  35.656  1.00 10.53           O  
ANISOU  305  O   ARG A  45     1326   1389   1283    -85    219   -139       O  
ATOM    306  CB  ARG A  45      19.139  16.935  36.915  1.00 10.39           C  
ANISOU  306  CB  ARG A  45     1237   1454   1256   -323    353   -211       C  
ATOM    307  CG  ARG A  45      19.356  15.499  36.415  1.00 10.90           C  
ANISOU  307  CG  ARG A  45     1675   1415   1050   -210    101   -171       C  
ATOM    308  CD  ARG A  45      18.418  14.501  37.105  1.00 11.15           C  
ANISOU  308  CD  ARG A  45     1503   1453   1279   -154     25    240       C  
ATOM    309  NE  ARG A  45      18.773  14.295  38.511  1.00 11.11           N  
ANISOU  309  NE  ARG A  45     1320   1745   1154   -298    145    350       N  
ATOM    310  CZ  ARG A  45      19.678  13.413  38.937  1.00 11.71           C  
ANISOU  310  CZ  ARG A  45     1707   1266   1476   -135    211    -21       C  
ATOM    311  NH1 ARG A  45      20.307  12.631  38.073  1.00 11.53           N  
ANISOU  311  NH1 ARG A  45     1562   1077   1740    -21    125    -31       N  
ATOM    312  NH2 ARG A  45      19.926  13.287  40.234  1.00 11.49           N  
ANISOU  312  NH2 ARG A  45     1562   1636   1166   -247    235    318       N  
ATOM    313  N   ASN A  46      20.067  20.009  37.464  1.00 12.19           N  
ANISOU  313  N   ASN A  46     1569   1684   1377     -9    267   -213       N  
ATOM    314  CA  ASN A  46      19.751  21.404  37.735  1.00 14.15           C  
ANISOU  314  CA  ASN A  46     2069   1783   1524    -71    -15   -214       C  
ATOM    315  C   ASN A  46      20.218  22.340  36.629  1.00 11.78           C  
ANISOU  315  C   ASN A  46     1591   1422   1462    143     31   -277       C  
ATOM    316  O   ASN A  46      19.486  23.247  36.208  1.00 12.48           O  
ANISOU  316  O   ASN A  46     1796   1354   1589     65    135   -198       O  
ATOM    317  CB  ASN A  46      20.315  21.833  39.088  1.00 15.34           C  
ANISOU  317  CB  ASN A  46     2457   1875   1495     38     83   -403       C  
ATOM    318  CG  ASN A  46      19.255  21.893  40.156  1.00 25.36           C  
ANISOU  318  CG  ASN A  46     3462   3213   2958   -111    324     17       C  
ATOM    319  OD1 ASN A  46      18.792  20.858  40.639  1.00 32.96           O  
ANISOU  319  OD1 ASN A  46     4463   3698   4361   -191    386    -65       O  
ATOM    320  ND2 ASN A  46      18.729  23.089  40.387  1.00 34.59           N  
ANISOU  320  ND2 ASN A  46     4737   3876   4526    237     42   -428       N  
ATOM    321  N   PHE A  47      21.396  22.056  36.086  1.00 10.30           N  
ANISOU  321  N   PHE A  47     1535   1221   1154   -114    188   -228       N  
ATOM    322  CA  PHE A  47      21.877  22.825  34.955  1.00  9.47           C  
ANISOU  322  CA  PHE A  47     1210   1179   1207    -74    -37    -94       C  
ATOM    323  C   PHE A  47      20.994  22.606  33.725  1.00 10.17           C  
ANISOU  323  C   PHE A  47     1376   1123   1365    -62    -87   -195       C  
ATOM    324  O   PHE A  47      20.605  23.550  33.044  1.00 10.48           O  
ANISOU  324  O   PHE A  47     1297   1126   1557     40    124     91       O  
ATOM    325  CB  PHE A  47      23.331  22.479  34.646  1.00 11.85           C  
ANISOU  325  CB  PHE A  47     1153   1618   1729   -128     56   -199       C  
ATOM    326  CG  PHE A  47      23.881  23.208  33.458  1.00 11.71           C  
ANISOU  326  CG  PHE A  47     1324   1259   1864     -5   -106   -246       C  
ATOM    327  CD1 PHE A  47      24.106  24.575  33.509  1.00 13.90           C  
ANISOU  327  CD1 PHE A  47     1859   1508   1913    -44    293    -89       C  
ATOM    328  CD2 PHE A  47      24.184  22.525  32.295  1.00 11.62           C  
ANISOU  328  CD2 PHE A  47     1264   1853   1295    133   -197    -31       C  
ATOM    329  CE1 PHE A  47      24.605  25.252  32.405  1.00 15.97           C  
ANISOU  329  CE1 PHE A  47     2274   1574   2218     53    464      4       C  
ATOM    330  CE2 PHE A  47      24.659  23.190  31.183  1.00 12.75           C  
ANISOU  330  CE2 PHE A  47     1303   1916   1625    119    109     59       C  
ATOM    331  CZ  PHE A  47      24.867  24.550  31.236  1.00 14.75           C  
ANISOU  331  CZ  PHE A  47     2130   1558   1913    113    240      8       C  
ATOM    332  N   PHE A  48      20.673  21.351  33.435  1.00  8.97           N  
ANISOU  332  N   PHE A  48     1327    785   1295   -161    120   -184       N  
ATOM    333  CA  PHE A  48      19.859  21.046  32.274  1.00 10.29           C  
ANISOU  333  CA  PHE A  48     1366   1206   1338     15     72     17       C  
ATOM    334  C   PHE A  48      18.520  21.772  32.291  1.00  9.35           C  
ANISOU  334  C   PHE A  48     1334    949   1270   -100     62    -51       C  
ATOM    335  O   PHE A  48      17.966  22.093  31.244  1.00  9.77           O  
ANISOU  335  O   PHE A  48     1216    920   1575    -16    137     10       O  
ATOM    336  CB  PHE A  48      19.683  19.537  32.122  1.00  9.95           C  
ANISOU  336  CB  PHE A  48     1401   1028   1350     58     29   -238       C  
ATOM    337  CG  PHE A  48      20.980  18.797  31.874  1.00 11.83           C  
ANISOU  337  CG  PHE A  48     1884   1602   1006    310    -54   -394       C  
ATOM    338  CD1 PHE A  48      22.082  19.459  31.344  1.00 14.44           C  
ANISOU  338  CD1 PHE A  48     1459   2280   1747    518    -60   -447       C  
ATOM    339  CD2 PHE A  48      21.119  17.466  32.241  1.00 16.64           C  
ANISOU  339  CD2 PHE A  48     2758   2392   1169    587    274     34       C  
ATOM    340  CE1 PHE A  48      23.283  18.797  31.118  1.00 15.47           C  
ANISOU  340  CE1 PHE A  48     2175   2079   1622    306    -22   -477       C  
ATOM    341  CE2 PHE A  48      22.331  16.791  32.018  1.00 13.36           C  
ANISOU  341  CE2 PHE A  48     1937   1979   1159    493    182   -282       C  
ATOM    342  CZ  PHE A  48      23.420  17.482  31.514  1.00 14.81           C  
ANISOU  342  CZ  PHE A  48     2333   1933   1360    479    125   -153       C  
ATOM    343  N   PHE A  49      17.979  21.977  33.490  1.00  9.78           N  
ANISOU  343  N   PHE A  49     1238   1056   1421    -21    322   -124       N  
ATOM    344  CA  PHE A  49      16.652  22.582  33.651  1.00 12.60           C  
ANISOU  344  CA  PHE A  49     1561   1416   1809     46    322     24       C  
ATOM    345  C   PHE A  49      16.650  24.016  33.089  1.00 13.16           C  
ANISOU  345  C   PHE A  49     1382   1299   2320    235     96   -156       C  
ATOM    346  O   PHE A  49      15.602  24.570  32.731  1.00 19.03           O  
ANISOU  346  O   PHE A  49     1733   1412   4085    212     42     51       O  
ATOM    347  CB  PHE A  49      16.298  22.576  35.146  1.00 14.74           C  
ANISOU  347  CB  PHE A  49     1816   2288   1497    -73    265   -321       C  
ATOM    348  CG  PHE A  49      14.869  22.213  35.466  1.00 18.52           C  
ANISOU  348  CG  PHE A  49     2632   2594   1810   -322    -18   -375       C  
ATOM    349  CD1 PHE A  49      13.971  21.822  34.484  1.00 17.39           C  
ANISOU  349  CD1 PHE A  49     2242   2185   2179   -216    171   -212       C  
ATOM    350  CD2 PHE A  49      14.400  22.382  36.764  1.00 17.52           C  
ANISOU  350  CD2 PHE A  49     1851   2686   2117    333    677   -301       C  
ATOM    351  CE1 PHE A  49      12.625  21.627  34.788  1.00 15.61           C  
ANISOU  351  CE1 PHE A  49     2633   1057   2240    151    249   -216       C  
ATOM    352  CE2 PHE A  49      13.042  22.243  37.067  1.00 18.80           C  
ANISOU  352  CE2 PHE A  49     1956   2654   2532     70    144    141       C  
ATOM    353  CZ  PHE A  49      12.159  21.842  36.079  1.00 17.80           C  
ANISOU  353  CZ  PHE A  49     2537   1944   2280    229    -90     -7       C  
ATOM    354  N   GLN A  50      17.835  24.586  32.934  1.00 10.64           N  
ANISOU  354  N   GLN A  50     1585    895   1560     70    225   -148       N  
ATOM    355  CA  GLN A  50      17.961  25.930  32.375  1.00 12.40           C  
ANISOU  355  CA  GLN A  50     1740   1119   1851     21      9   -156       C  
ATOM    356  C   GLN A  50      17.781  25.972  30.855  1.00 10.87           C  
ANISOU  356  C   GLN A  50     1613    888   1626    243     51     -9       C  
ATOM    357  O   GLN A  50      17.806  27.047  30.241  1.00 11.67           O  
ANISOU  357  O   GLN A  50     1661    786   1985    263    151   -103       O  
ATOM    358  CB  GLN A  50      19.303  26.548  32.776  1.00 13.91           C  
ANISOU  358  CB  GLN A  50     2006   1363   1913   -239    -78     40       C  
ATOM    359  CG  GLN A  50      19.435  26.755  34.268  1.00 17.23           C  
ANISOU  359  CG  GLN A  50     2709   1632   2203   -404   -306   -159       C  
ATOM    360  CD  GLN A  50      20.869  27.019  34.728  1.00 25.27           C  
ANISOU  360  CD  GLN A  50     3239   3001   3360   -277   -250    -26       C  
ATOM    361  OE1 GLN A  50      21.211  26.761  35.881  1.00 29.70           O  
ANISOU  361  OE1 GLN A  50     4092   3796   3395    -69    -71   -289       O  
ATOM    362  NE2 GLN A  50      21.698  27.560  33.840  1.00 22.35           N  
ANISOU  362  NE2 GLN A  50     2811   3004   2676   -628   -595   -317       N  
ATOM    363  N   SER A  51      17.563  24.800  30.251  1.00 10.92           N  
ANISOU  363  N   SER A  51     1369   1111   1666     18   -159    -55       N  
ATOM    364  CA  SER A  51      17.346  24.733  28.813  1.00  9.93           C  
ANISOU  364  CA  SER A  51     1272    898   1602     33     33     96       C  
ATOM    365  C   SER A  51      15.937  25.166  28.419  1.00  9.89           C  
ANISOU  365  C   SER A  51     1320    943   1493    120    183    219       C  
ATOM    366  O   SER A  51      15.696  25.495  27.260  1.00 13.08           O  
ANISOU  366  O   SER A  51     1812   1708   1447    200    184    520       O  
ATOM    367  CB  SER A  51      17.610  23.326  28.280  1.00 11.19           C  
ANISOU  367  CB  SER A  51     1385   1080   1785    -35     94      1       C  
ATOM    368  OG  SER A  51      16.657  22.425  28.809  1.00  9.72           O  
ANISOU  368  OG  SER A  51     1251   1070   1370    115     89    177       O  
ATOM    369  N   GLY A  52      14.991  25.061  29.348  1.00  9.59           N  
ANISOU  369  N   GLY A  52     1166    982   1493     72     87    -55       N  
ATOM    370  CA  GLY A  52      13.595  25.305  29.024  1.00  9.31           C  
ANISOU  370  CA  GLY A  52     1117    907   1511    120     95    -77       C  
ATOM    371  C   GLY A  52      12.801  24.052  28.685  1.00  9.43           C  
ANISOU  371  C   GLY A  52     1346    765   1471    144    197    112       C  
ATOM    372  O   GLY A  52      11.586  24.122  28.528  1.00 10.48           O  
ANISOU  372  O   GLY A  52     1495    724   1762    148     33     50       O  
ATOM    373  N   LEU A  53      13.484  22.922  28.497  1.00 10.35           N  
ANISOU  373  N   LEU A  53     1451    824   1656     34    136     10       N  
ATOM    374  CA  LEU A  53      12.804  21.701  28.074  1.00 12.47           C  
ANISOU  374  CA  LEU A  53     1501    975   2261    280    125   -213       C  
ATOM    375  C   LEU A  53      11.983  21.164  29.233  1.00 12.29           C  
ANISOU  375  C   LEU A  53     1329    812   2526    281    203   -260       C  
ATOM    376  O   LEU A  53      12.317  21.400  30.391  1.00 12.46           O  
ANISOU  376  O   LEU A  53     1628    606   2498    186    518     49       O  
ATOM    377  CB  LEU A  53      13.809  20.631  27.620  1.00 11.23           C  
ANISOU  377  CB  LEU A  53     1259    935   2073    220      4   -215       C  
ATOM    378  CG  LEU A  53      14.465  20.878  26.265  1.00 12.07           C  
ANISOU  378  CG  LEU A  53     1374   1456   1753    140     16   -192       C  
ATOM    379  CD1 LEU A  53      15.568  19.863  26.007  1.00 11.25           C  
ANISOU  379  CD1 LEU A  53     1137   1149   1987    410    -42   -613       C  
ATOM    380  CD2 LEU A  53      13.440  20.843  25.153  1.00 13.80           C  
ANISOU  380  CD2 LEU A  53     1558   1695   1987      0   -340      4       C  
ATOM    381  N   PRO A  54      10.906  20.431  28.920  1.00 15.81           N  
ANISOU  381  N   PRO A  54     1554   1236   3217    335    503   -164       N  
ATOM    382  CA  PRO A  54      10.085  19.815  29.946  1.00 17.62           C  
ANISOU  382  CA  PRO A  54     1933   1456   3303   -137    555   -185       C  
ATOM    383  C   PRO A  54      10.909  18.912  30.859  1.00 16.41           C  
ANISOU  383  C   PRO A  54     1546   1455   3231    -38    930   -111       C  
ATOM    384  O   PRO A  54      11.780  18.174  30.385  1.00 16.04           O  
ANISOU  384  O   PRO A  54     1880   1053   3159     -3   1197   -272       O  
ATOM    385  CB  PRO A  54       9.066  19.000  29.139  1.00 17.36           C  
ANISOU  385  CB  PRO A  54     1633   1517   3445     23    598   -572       C  
ATOM    386  CG  PRO A  54       9.022  19.634  27.802  1.00 18.02           C  
ANISOU  386  CG  PRO A  54     1305   1659   3879   -242    257   -390       C  
ATOM    387  CD  PRO A  54      10.412  20.160  27.561  1.00 16.64           C  
ANISOU  387  CD  PRO A  54     1437   1456   3429     70    424   -187       C  
ATOM    388  N   GLN A  55      10.541  18.864  32.134  1.00 19.51           N  
ANISOU  388  N   GLN A  55     2624   1458   3330   -173    670   -530       N  
ATOM    389  CA  GLN A  55      11.203  17.985  33.089  1.00 19.06           C  
ANISOU  389  CA  GLN A  55     2239   1930   3071   -181   1003   -242       C  
ATOM    390  C   GLN A  55      11.221  16.506  32.650  1.00 17.89           C  
ANISOU  390  C   GLN A  55     2006   1646   3143     50    895   -294       C  
ATOM    391  O   GLN A  55      12.268  15.854  32.748  1.00 18.99           O  
ANISOU  391  O   GLN A  55     2337   1656   3220   -150   1259    137       O  
ATOM    392  CB  GLN A  55      10.611  18.130  34.497  1.00 22.70           C  
ANISOU  392  CB  GLN A  55     2947   2338   3337     48    790   -355       C  
ATOM    393  CG  GLN A  55      11.566  17.717  35.617  1.00 27.70           C  
ANISOU  393  CG  GLN A  55     3286   3605   3634   -236    512   -530       C  
ATOM    394  CD  GLN A  55      10.950  16.720  36.578  1.00 32.87           C  
ANISOU  394  CD  GLN A  55     4631   3812   4045     33    -89    -44       C  
ATOM    395  OE1 GLN A  55      10.295  15.764  36.158  1.00 30.33           O  
ANISOU  395  OE1 GLN A  55     4486   2440   4595    171    245    245       O  
ATOM    396  NE2 GLN A  55      11.068  16.998  37.877  1.00 30.97           N  
ANISOU  396  NE2 GLN A  55     4160   3957   3649    -54   -238    -38       N  
ATOM    397  N   PRO A  56      10.095  15.998  32.095  1.00 18.32           N  
ANISOU  397  N   PRO A  56     2041   1508   3412     97    863   -154       N  
ATOM    398  CA  PRO A  56      10.079  14.585  31.713  1.00 17.70           C  
ANISOU  398  CA  PRO A  56     1922   1354   3446   -186    663   -112       C  
ATOM    399  C   PRO A  56      11.080  14.320  30.607  1.00 14.86           C  
ANISOU  399  C   PRO A  56     1564    944   3138    163    564   -168       C  
ATOM    400  O   PRO A  56      11.708  13.266  30.567  1.00 16.63           O  
ANISOU  400  O   PRO A  56     2023    833   3460     53   1001    161       O  
ATOM    401  CB  PRO A  56       8.656  14.365  31.178  1.00 21.29           C  
ANISOU  401  CB  PRO A  56     2288   1955   3846   -185    556    -48       C  
ATOM    402  CG  PRO A  56       7.844  15.442  31.777  1.00 18.91           C  
ANISOU  402  CG  PRO A  56     2120   1665   3400    108    524   -215       C  
ATOM    403  CD  PRO A  56       8.767  16.624  31.949  1.00 19.09           C  
ANISOU  403  CD  PRO A  56     1931   1634   3688   -124    728   -410       C  
ATOM    404  N   VAL A  57      11.190  15.273  29.692  1.00 14.09           N  
ANISOU  404  N   VAL A  57     1420   1180   2750     15    608     53       N  
ATOM    405  CA  VAL A  57      12.150  15.193  28.607  1.00 12.68           C  
ANISOU  405  CA  VAL A  57     1473   1227   2118    -61     95    -70       C  
ATOM    406  C   VAL A  57      13.579  15.171  29.149  1.00 10.92           C  
ANISOU  406  C   VAL A  57     1367    987   1791    -58    103   -255       C  
ATOM    407  O   VAL A  57      14.394  14.344  28.728  1.00 10.14           O  
ANISOU  407  O   VAL A  57     1304    901   1645      6    315    -89       O  
ATOM    408  CB  VAL A  57      11.948  16.351  27.600  1.00 13.17           C  
ANISOU  408  CB  VAL A  57     1311   1416   2276   -189   -150    -28       C  
ATOM    409  CG1 VAL A  57      13.081  16.401  26.592  1.00 14.75           C  
ANISOU  409  CG1 VAL A  57     1755   1627   2220     95    -51    -42       C  
ATOM    410  CG2 VAL A  57      10.594  16.219  26.908  1.00 16.85           C  
ANISOU  410  CG2 VAL A  57     1898   1588   2916    167   -369   -164       C  
ATOM    411  N   LEU A  58      13.888  16.085  30.066  1.00 10.25           N  
ANISOU  411  N   LEU A  58     1366    915   1611   -316    195    -63       N  
ATOM    412  CA  LEU A  58      15.215  16.126  30.658  1.00  9.38           C  
ANISOU  412  CA  LEU A  58     1455    741   1368   -176    186   -376       C  
ATOM    413  C   LEU A  58      15.575  14.884  31.469  1.00  9.82           C  
ANISOU  413  C   LEU A  58     1523    934   1274    -89    462   -260       C  
ATOM    414  O   LEU A  58      16.745  14.521  31.570  1.00 10.20           O  
ANISOU  414  O   LEU A  58     1540    880   1454     17    538     84       O  
ATOM    415  CB  LEU A  58      15.413  17.400  31.479  1.00 10.88           C  
ANISOU  415  CB  LEU A  58     1623    849   1660   -266    323    -95       C  
ATOM    416  CG  LEU A  58      15.370  18.665  30.624  1.00 10.54           C  
ANISOU  416  CG  LEU A  58     1378    829   1797    -70    492    -91       C  
ATOM    417  CD1 LEU A  58      15.312  19.870  31.541  1.00 11.16           C  
ANISOU  417  CD1 LEU A  58     1752    596   1893   -193    605   -261       C  
ATOM    418  CD2 LEU A  58      16.571  18.728  29.702  1.00  9.52           C  
ANISOU  418  CD2 LEU A  58     1387    718   1512   -333    429    -71       C  
ATOM    419  N   ALA A  59      14.575  14.278  32.107  1.00 10.86           N  
ANISOU  419  N   ALA A  59     1675    950   1498   -139    374     -7       N  
ATOM    420  CA  ALA A  59      14.785  13.026  32.818  1.00 10.24           C  
ANISOU  420  CA  ALA A  59     1582    941   1367     29    759   -134       C  
ATOM    421  C   ALA A  59      15.225  11.925  31.862  1.00  9.50           C  
ANISOU  421  C   ALA A  59     1431    902   1276    -85    381    -62       C  
ATOM    422  O   ALA A  59      16.152  11.168  32.160  1.00  9.93           O  
ANISOU  422  O   ALA A  59     1619    715   1437    -92    338    -26       O  
ATOM    423  CB  ALA A  59      13.507  12.621  33.551  1.00 11.02           C  
ANISOU  423  CB  ALA A  59     1602   1011   1575     44    945     54       C  
ATOM    424  N   GLN A  60      14.572  11.854  30.709  1.00  9.26           N  
ANISOU  424  N   GLN A  60     1308    751   1459    -14    344   -337       N  
ATOM    425  CA  GLN A  60      14.960  10.893  29.689  1.00  9.30           C  
ANISOU  425  CA  GLN A  60     1279    883   1370   -101    242   -197       C  
ATOM    426  C   GLN A  60      16.373  11.184  29.180  1.00  8.55           C  
ANISOU  426  C   GLN A  60     1110    768   1367     51    214    -44       C  
ATOM    427  O   GLN A  60      17.166  10.276  28.951  1.00  9.52           O  
ANISOU  427  O   GLN A  60     1388    784   1443    140     91     11       O  
ATOM    428  CB  GLN A  60      13.971  10.916  28.536  1.00  9.86           C  
ANISOU  428  CB  GLN A  60     1346    910   1490     82     28   -158       C  
ATOM    429  CG  GLN A  60      14.294   9.917  27.440  1.00 10.61           C  
ANISOU  429  CG  GLN A  60     1574   1055   1400    -29     21    -45       C  
ATOM    430  CD  GLN A  60      13.214   9.839  26.394  1.00 13.30           C  
ANISOU  430  CD  GLN A  60     1840   1577   1637    -41      0    -11       C  
ATOM    431  OE1 GLN A  60      12.176  10.498  26.509  1.00 16.59           O  
ANISOU  431  OE1 GLN A  60     1612   2493   2197    -25   -224    181       O  
ATOM    432  NE2 GLN A  60      13.463   9.061  25.339  1.00 15.96           N  
ANISOU  432  NE2 GLN A  60     2431   1052   2579   -166    -29   -252       N  
ATOM    433  N   ILE A  61      16.684  12.463  28.985  1.00  8.20           N  
ANISOU  433  N   ILE A  61     1121    782   1210   -199    168    -72       N  
ATOM    434  CA  ILE A  61      18.019  12.836  28.532  1.00  8.29           C  
ANISOU  434  CA  ILE A  61     1129    911   1110     18    108     64       C  
ATOM    435  C   ILE A  61      19.081  12.450  29.555  1.00  8.73           C  
ANISOU  435  C   ILE A  61     1195   1063   1056      2    154   -120       C  
ATOM    436  O   ILE A  61      20.123  11.896  29.192  1.00  9.05           O  
ANISOU  436  O   ILE A  61     1262    972   1204    129    212   -141       O  
ATOM    437  CB  ILE A  61      18.107  14.327  28.159  1.00  8.11           C  
ANISOU  437  CB  ILE A  61     1148    839   1093      4    235     66       C  
ATOM    438  CG1 ILE A  61      17.310  14.576  26.878  1.00  7.89           C  
ANISOU  438  CG1 ILE A  61     1281    803    913     93    122     13       C  
ATOM    439  CG2 ILE A  61      19.557  14.766  28.010  1.00 10.36           C  
ANISOU  439  CG2 ILE A  61     1110   1336   1488   -204    215    175       C  
ATOM    440  CD1 ILE A  61      17.175  16.017  26.482  1.00  9.92           C  
ANISOU  440  CD1 ILE A  61     1589    846   1334    364    -11     52       C  
ATOM    441  N   TRP A  62      18.806  12.702  30.833  1.00  8.93           N  
ANISOU  441  N   TRP A  62     1281    973   1139   -157     36   -100       N  
ATOM    442  CA  TRP A  62      19.728  12.281  31.873  1.00  8.48           C  
ANISOU  442  CA  TRP A  62     1442    909    867   -108    254   -105       C  
ATOM    443  C   TRP A  62      20.014  10.777  31.756  1.00  9.13           C  
ANISOU  443  C   TRP A  62     1472   1037    960   -109    249    -36       C  
ATOM    444  O   TRP A  62      21.164  10.342  31.808  1.00 10.29           O  
ANISOU  444  O   TRP A  62     1493   1083   1331    -12    214     66       O  
ATOM    445  CB  TRP A  62      19.181  12.616  33.264  1.00  9.09           C  
ANISOU  445  CB  TRP A  62     1403   1254    796     50    321    -85       C  
ATOM    446  CG  TRP A  62      19.912  11.878  34.324  1.00  9.04           C  
ANISOU  446  CG  TRP A  62     1374   1053   1005   -109    295     94       C  
ATOM    447  CD1 TRP A  62      19.556  10.672  34.874  1.00 10.26           C  
ANISOU  447  CD1 TRP A  62     1810   1070   1016    -18    245     72       C  
ATOM    448  CD2 TRP A  62      21.236  12.154  34.796  1.00  9.09           C  
ANISOU  448  CD2 TRP A  62     1347   1003   1104   -109    133    -95       C  
ATOM    449  NE1 TRP A  62      20.551  10.223  35.704  1.00 12.00           N  
ANISOU  449  NE1 TRP A  62     1761   1572   1225     87     33    -10       N  
ATOM    450  CE2 TRP A  62      21.615  11.084  35.632  1.00  9.69           C  
ANISOU  450  CE2 TRP A  62     1571    917   1192    -78   -240   -149       C  
ATOM    451  CE3 TRP A  62      22.140  13.210  34.595  1.00 10.57           C  
ANISOU  451  CE3 TRP A  62     1605   1294   1116   -280    120   -222       C  
ATOM    452  CZ2 TRP A  62      22.856  11.036  36.268  1.00 12.46           C  
ANISOU  452  CZ2 TRP A  62     1826   1494   1413     46   -115    162       C  
ATOM    453  CZ3 TRP A  62      23.382  13.145  35.204  1.00 12.93           C  
ANISOU  453  CZ3 TRP A  62     2142   1395   1373   -233   -118   -161       C  
ATOM    454  CH2 TRP A  62      23.726  12.065  36.037  1.00 13.70           C  
ANISOU  454  CH2 TRP A  62     1833   2007   1364   -129    -99     35       C  
ATOM    455  N   ALA A  63      18.963   9.978  31.620  1.00 10.25           N  
ANISOU  455  N   ALA A  63     1752    986   1156   -153    212     17       N  
ATOM    456  CA  ALA A  63      19.128   8.523  31.648  1.00 11.97           C  
ANISOU  456  CA  ALA A  63     1932   1107   1509   -105    421     54       C  
ATOM    457  C   ALA A  63      19.872   8.027  30.406  1.00  9.77           C  
ANISOU  457  C   ALA A  63     1544    910   1257    -80    261    -62       C  
ATOM    458  O   ALA A  63      20.634   7.059  30.461  1.00 12.14           O  
ANISOU  458  O   ALA A  63     1652   1310   1648     85     33     16       O  
ATOM    459  CB  ALA A  63      17.778   7.856  31.751  1.00 14.11           C  
ANISOU  459  CB  ALA A  63     2114   1336   1910   -305    410     -2       C  
ATOM    460  N   LEU A  64      19.640   8.690  29.278  1.00  8.83           N  
ANISOU  460  N   LEU A  64     1230    862   1263   -239    325     52       N  
ATOM    461  CA  LEU A  64      20.375   8.360  28.059  1.00  8.41           C  
ANISOU  461  CA  LEU A  64     1137    918   1138    -39    331    -63       C  
ATOM    462  C   LEU A  64      21.861   8.669  28.227  1.00  8.90           C  
ANISOU  462  C   LEU A  64     1172    910   1301    104    188     -9       C  
ATOM    463  O   LEU A  64      22.727   7.901  27.792  1.00  9.54           O  
ANISOU  463  O   LEU A  64     1135    949   1539    -59    279   -134       O  
ATOM    464  CB  LEU A  64      19.808   9.143  26.876  1.00  9.47           C  
ANISOU  464  CB  LEU A  64     1258   1015   1323    -55    166    -81       C  
ATOM    465  CG  LEU A  64      18.518   8.601  26.259  1.00  7.96           C  
ANISOU  465  CG  LEU A  64     1099    715   1208     -8    292   -156       C  
ATOM    466  CD1 LEU A  64      17.868   9.664  25.381  1.00 10.84           C  
ANISOU  466  CD1 LEU A  64     1552   1119   1448     84     30   -196       C  
ATOM    467  CD2 LEU A  64      18.865   7.366  25.430  1.00  7.98           C  
ANISOU  467  CD2 LEU A  64     1289    785    957    147    169   -183       C  
ATOM    468  N   ALA A  65      22.147   9.825  28.823  1.00  9.45           N  
ANISOU  468  N   ALA A  65     1180   1056   1353   -156     43     11       N  
ATOM    469  CA  ALA A  65      23.514  10.344  28.868  1.00  9.66           C  
ANISOU  469  CA  ALA A  65     1150   1141   1380   -131    114    157       C  
ATOM    470  C   ALA A  65      24.367   9.712  29.962  1.00 10.66           C  
ANISOU  470  C   ALA A  65     1290   1297   1463    -38     78     27       C  
ATOM    471  O   ALA A  65      25.592   9.679  29.851  1.00 11.82           O  
ANISOU  471  O   ALA A  65     1155   1486   1850   -148    155    290       O  
ATOM    472  CB  ALA A  65      23.501  11.858  29.024  1.00 10.02           C  
ANISOU  472  CB  ALA A  65     1451   1001   1355   -110     74    100       C  
ATOM    473  N   ASP A  66      23.731   9.283  31.047  1.00  9.59           N  
ANISOU  473  N   ASP A  66     1347   1079   1218      1    -30     95       N  
ATOM    474  CA  ASP A  66      24.462   8.638  32.134  1.00 10.87           C  
ANISOU  474  CA  ASP A  66     1543   1324   1262     35    -28    182       C  
ATOM    475  C   ASP A  66      24.793   7.204  31.737  1.00 12.00           C  
ANISOU  475  C   ASP A  66     1388   1310   1859     -1     23    188       C  
ATOM    476  O   ASP A  66      24.167   6.240  32.205  1.00 12.02           O  
ANISOU  476  O   ASP A  66     1457   1294   1815     78    -31    263       O  
ATOM    477  CB  ASP A  66      23.656   8.672  33.433  1.00 10.66           C  
ANISOU  477  CB  ASP A  66     1454   1328   1269    182     67    251       C  
ATOM    478  CG  ASP A  66      24.415   8.060  34.609  1.00 11.81           C  
ANISOU  478  CG  ASP A  66     1432   1549   1505     -6   -116     77       C  
ATOM    479  OD1 ASP A  66      25.653   7.907  34.508  1.00 11.15           O  
ANISOU  479  OD1 ASP A  66     1290   1241   1706   -144   -173    268       O  
ATOM    480  OD2 ASP A  66      23.769   7.708  35.621  1.00 11.88           O  
ANISOU  480  OD2 ASP A  66     1507   1512   1493    -66     23    409       O  
HETATM  481  N   MSE A  67      25.753   7.074  30.824  1.00 12.43           N  
ANISOU  481  N   MSE A  67     1680   1468   1574     98     75    149       N  
HETATM  482  CA  MSE A  67      25.984   5.827  30.110  1.00 14.73           C  
ANISOU  482  CA  MSE A  67     1972   1699   1925    301    -81     23       C  
HETATM  483  C   MSE A  67      26.307   4.659  31.028  1.00 14.09           C  
ANISOU  483  C   MSE A  67     1855   1506   1992     50      4    127       C  
HETATM  484  O   MSE A  67      26.004   3.515  30.701  1.00 16.86           O  
ANISOU  484  O   MSE A  67     2309   1657   2438    257    -32   -108       O  
HETATM  485  CB  MSE A  67      27.136   5.987  29.130  1.00 18.02           C  
ANISOU  485  CB  MSE A  67     2559   1992   2292    140    145   -122       C  
HETATM  486  CG  MSE A  67      26.817   6.842  27.944  1.00 20.03           C  
ANISOU  486  CG  MSE A  67     2465   2525   2621    294     16     37       C  
HETATM  487 SE   MSE A  67      28.259   6.672  26.674  1.00 28.30          SE  
ANISOU  487 SE   MSE A  67     3986   3478   3288    -66    344   -190      SE  
HETATM  488  CE  MSE A  67      29.635   7.612  27.666  1.00 24.48           C  
ANISOU  488  CE  MSE A  67     3366   2920   3012     35    149   -302       C  
ATOM    489  N   ASN A  68      27.039   4.930  32.102  1.00 13.01           N  
ANISOU  489  N   ASN A  68     1816   1207   1917    158    -43    199       N  
ATOM    490  CA  ASN A  68      27.420   3.855  33.025  1.00 14.11           C  
ANISOU  490  CA  ASN A  68     1779   1554   2028    137   -243    215       C  
ATOM    491  C   ASN A  68      26.485   3.722  34.223  1.00 14.20           C  
ANISOU  491  C   ASN A  68     1738   1553   2104    -85   -240    331       C  
ATOM    492  O   ASN A  68      26.726   2.910  35.120  1.00 16.89           O  
ANISOU  492  O   ASN A  68     2151   1784   2478    -47   -328    571       O  
ATOM    493  CB  ASN A  68      28.876   4.006  33.478  1.00 14.28           C  
ANISOU  493  CB  ASN A  68     1684   1533   2207    163   -143    248       C  
ATOM    494  CG  ASN A  68      29.070   5.133  34.480  1.00 13.76           C  
ANISOU  494  CG  ASN A  68     1707   1612   1908     20   -295    328       C  
ATOM    495  OD1 ASN A  68      28.259   6.062  34.571  1.00 13.80           O  
ANISOU  495  OD1 ASN A  68     1970   1285   1986    -52   -188    284       O  
ATOM    496  ND2 ASN A  68      30.205   5.110  35.165  1.00 18.08           N  
ANISOU  496  ND2 ASN A  68     1755   2179   2934    167   -428    212       N  
ATOM    497  N   ASN A  69      25.393   4.483  34.206  1.00 15.21           N  
ANISOU  497  N   ASN A  69     1973   1701   2105    -22    -46    142       N  
ATOM    498  CA  ASN A  69      24.306   4.310  35.168  1.00 14.95           C  
ANISOU  498  CA  ASN A  69     2060   1412   2207   -312    -20    179       C  
ATOM    499  C   ASN A  69      24.753   4.493  36.613  1.00 15.94           C  
ANISOU  499  C   ASN A  69     2036   1821   2199   -243    -98    290       C  
ATOM    500  O   ASN A  69      24.124   3.969  37.539  1.00 18.34           O  
ANISOU  500  O   ASN A  69     2575   1946   2445   -255     66    362       O  
ATOM    501  CB  ASN A  69      23.620   2.947  34.986  1.00 14.75           C  
ANISOU  501  CB  ASN A  69     1972   1501   2129   -425      5     13       C  
ATOM    502  CG  ASN A  69      23.106   2.748  33.583  1.00 15.33           C  
ANISOU  502  CG  ASN A  69     1689   1678   2456   -330    -45    226       C  
ATOM    503  OD1 ASN A  69      22.430   3.614  33.026  1.00 18.46           O  
ANISOU  503  OD1 ASN A  69     2133   2248   2631   -553   -473    676       O  
ATOM    504  ND2 ASN A  69      23.473   1.623  32.978  1.00 18.30           N  
ANISOU  504  ND2 ASN A  69     2761   1824   2365   -443   -276   -314       N  
ATOM    505  N   ASP A  70      25.790   5.301  36.815  1.00 15.65           N  
ANISOU  505  N   ASP A  70     2048   1725   2172   -221    -83    443       N  
ATOM    506  CA  ASP A  70      26.321   5.510  38.157  1.00 16.20           C  
ANISOU  506  CA  ASP A  70     2159   2028   1967   -193    -42    343       C  
ATOM    507  C   ASP A  70      25.784   6.730  38.887  1.00 14.67           C  
ANISOU  507  C   ASP A  70     1891   1844   1838   -169    -93    519       C  
ATOM    508  O   ASP A  70      26.127   6.957  40.042  1.00 17.17           O  
ANISOU  508  O   ASP A  70     2303   2324   1897   -153    -62    458       O  
ATOM    509  CB  ASP A  70      27.853   5.483  38.175  1.00 16.10           C  
ANISOU  509  CB  ASP A  70     2069   1914   2131   -116    -99    561       C  
ATOM    510  CG  ASP A  70      28.481   6.724  37.560  1.00 15.86           C  
ANISOU  510  CG  ASP A  70     2014   1903   2106   -244   -204    214       C  
ATOM    511  OD1 ASP A  70      27.740   7.573  37.016  1.00 13.56           O  
ANISOU  511  OD1 ASP A  70     1688   1579   1883    -44   -140    253       O  
ATOM    512  OD2 ASP A  70      29.727   6.830  37.599  1.00 17.29           O  
ANISOU  512  OD2 ASP A  70     2146   2120   2301     48   -506    541       O  
ATOM    513  N   GLY A  71      24.899   7.485  38.237  1.00 14.82           N  
ANISOU  513  N   GLY A  71     1930   1863   1836     42     81    583       N  
ATOM    514  CA  GLY A  71      24.210   8.585  38.902  1.00 14.37           C  
ANISOU  514  CA  GLY A  71     2011   1694   1755   -262    172    469       C  
ATOM    515  C   GLY A  71      24.999   9.885  38.961  1.00 13.43           C  
ANISOU  515  C   GLY A  71     1864   1668   1570   -146    -22    351       C  
ATOM    516  O   GLY A  71      24.528  10.877  39.523  1.00 13.99           O  
ANISOU  516  O   GLY A  71     2017   1828   1468   -210    188    268       O  
ATOM    517  N   ARG A  72      26.218   9.867  38.429  1.00 12.05           N  
ANISOU  517  N   ARG A  72     1741   1701   1133   -126   -140    563       N  
ATOM    518  CA  ARG A  72      27.019  11.084  38.310  1.00 13.19           C  
ANISOU  518  CA  ARG A  72     1748   1867   1395   -124    -93    155       C  
ATOM    519  C   ARG A  72      27.479  11.215  36.858  1.00 12.43           C  
ANISOU  519  C   ARG A  72     1626   1774   1320   -185    -31    273       C  
ATOM    520  O   ARG A  72      27.266  10.304  36.059  1.00 12.07           O  
ANISOU  520  O   ARG A  72     1653   1610   1321   -133   -108    305       O  
ATOM    521  CB  ARG A  72      28.234  11.028  39.243  1.00 13.82           C  
ANISOU  521  CB  ARG A  72     1933   2043   1274   -118    -44    158       C  
ATOM    522  CG  ARG A  72      29.139   9.858  38.952  1.00 15.02           C  
ANISOU  522  CG  ARG A  72     2000   2212   1492     47   -245    234       C  
ATOM    523  CD  ARG A  72      30.412   9.855  39.788  1.00 15.83           C  
ANISOU  523  CD  ARG A  72     1835   2374   1804     46    -98    261       C  
ATOM    524  NE  ARG A  72      31.217   8.681  39.453  1.00 17.72           N  
ANISOU  524  NE  ARG A  72     2116   2336   2279    239   -401    390       N  
ATOM    525  CZ  ARG A  72      32.467   8.475  39.847  1.00 19.68           C  
ANISOU  525  CZ  ARG A  72     2313   2624   2540    195   -294    254       C  
ATOM    526  NH1 ARG A  72      33.042   9.306  40.704  1.00 17.65           N  
ANISOU  526  NH1 ARG A  72     2005   2313   2388    -33   -389    412       N  
ATOM    527  NH2 ARG A  72      33.112   7.392  39.437  1.00 22.14           N  
ANISOU  527  NH2 ARG A  72     2491   2632   3287    319   -301    229       N  
HETATM  528  N   MSE A  73      28.124  12.332  36.522  1.00 11.69           N  
ANISOU  528  N   MSE A  73     1575   1678   1189     51   -148    131       N  
HETATM  529  CA  MSE A  73      28.356  12.657  35.122  1.00 12.36           C  
ANISOU  529  CA  MSE A  73     1552   1687   1456    -30     23    214       C  
HETATM  530  C   MSE A  73      29.770  13.179  34.876  1.00 10.22           C  
ANISOU  530  C   MSE A  73     1382   1315   1187    115    -44      3       C  
HETATM  531  O   MSE A  73      30.241  14.078  35.573  1.00 11.78           O  
ANISOU  531  O   MSE A  73     1564   1489   1422     33    164    179       O  
HETATM  532  CB  MSE A  73      27.318  13.681  34.672  1.00 13.13           C  
ANISOU  532  CB  MSE A  73     1493   1862   1630    -20    -82    128       C  
HETATM  533  CG  MSE A  73      27.474  14.156  33.246  1.00 12.51           C  
ANISOU  533  CG  MSE A  73     1350   1849   1554    279     95     95       C  
HETATM  534 SE   MSE A  73      25.792  14.887  32.600  1.00 18.91          SE  
ANISOU  534 SE   MSE A  73     2348   2849   1988    560     65    240      SE  
HETATM  535  CE  MSE A  73      24.926  13.252  32.034  1.00 16.29           C  
ANISOU  535  CE  MSE A  73     1687   2840   1662    480    417    174       C  
ATOM    536  N   ASP A  74      30.460  12.564  33.916  1.00 10.37           N  
ANISOU  536  N   ASP A  74     1256   1502   1182    -75    140    186       N  
ATOM    537  CA  ASP A  74      31.764  13.047  33.494  1.00 10.24           C  
ANISOU  537  CA  ASP A  74     1196   1492   1200    112     26     77       C  
ATOM    538  C   ASP A  74      31.656  13.831  32.191  1.00 10.13           C  
ANISOU  538  C   ASP A  74     1255   1319   1275    -61    -73     13       C  
ATOM    539  O   ASP A  74      30.560  14.137  31.717  1.00  9.84           O  
ANISOU  539  O   ASP A  74     1142   1233   1362    -60     -4      6       O  
ATOM    540  CB  ASP A  74      32.771  11.901  33.373  1.00 13.50           C  
ANISOU  540  CB  ASP A  74     1816   1717   1594    245   -157    188       C  
ATOM    541  CG  ASP A  74      32.413  10.906  32.285  1.00 12.21           C  
ANISOU  541  CG  ASP A  74     1440   1387   1812    196     24    123       C  
ATOM    542  OD1 ASP A  74      31.528  11.190  31.451  1.00 12.74           O  
ANISOU  542  OD1 ASP A  74     1469   1628   1742    -50     78     72       O  
ATOM    543  OD2 ASP A  74      33.066   9.842  32.227  1.00 17.16           O  
ANISOU  543  OD2 ASP A  74     2130   1717   2673    355     45    130       O  
ATOM    544  N   GLN A  75      32.798  14.204  31.636  1.00  9.85           N  
ANISOU  544  N   GLN A  75     1199   1350   1192    -70    -21     95       N  
ATOM    545  CA  GLN A  75      32.800  15.125  30.509  1.00 10.55           C  
ANISOU  545  CA  GLN A  75     1125   1505   1379   -124      6    192       C  
ATOM    546  C   GLN A  75      32.159  14.533  29.255  1.00 10.40           C  
ANISOU  546  C   GLN A  75     1158   1360   1430    -73    124     44       C  
ATOM    547  O   GLN A  75      31.437  15.225  28.538  1.00 10.83           O  
ANISOU  547  O   GLN A  75     1190   1489   1433   -139     17     96       O  
ATOM    548  CB  GLN A  75      34.226  15.568  30.218  1.00 12.16           C  
ANISOU  548  CB  GLN A  75     1169   1766   1683   -154    132    362       C  
ATOM    549  CG  GLN A  75      34.378  16.596  29.126  1.00 10.72           C  
ANISOU  549  CG  GLN A  75     1221   1548   1302    -62    161    197       C  
ATOM    550  CD  GLN A  75      35.826  16.774  28.748  1.00 11.45           C  
ANISOU  550  CD  GLN A  75     1270   1598   1479    -83    -89    193       C  
ATOM    551  OE1 GLN A  75      36.436  15.890  28.143  1.00 12.50           O  
ANISOU  551  OE1 GLN A  75     1197   1825   1725     68     70    400       O  
ATOM    552  NE2 GLN A  75      36.411  17.877  29.184  1.00 13.91           N  
ANISOU  552  NE2 GLN A  75     1606   1700   1978   -124   -302    191       N  
ATOM    553  N  AVAL A  76      32.429  13.255  29.002  0.50  9.53           N  
ANISOU  553  N  AVAL A  76     1062   1291   1267    -86     90    -21       N  
ATOM    554  N  BVAL A  76      32.411  13.255  28.992  0.50  9.72           N  
ANISOU  554  N  BVAL A  76     1088   1308   1297    -88     88    -19       N  
ATOM    555  CA AVAL A  76      31.872  12.557  27.843  0.50 10.38           C  
ANISOU  555  CA AVAL A  76     1147   1336   1458     15     59    -38       C  
ATOM    556  CA BVAL A  76      31.844  12.612  27.806  0.50 10.87           C  
ANISOU  556  CA BVAL A  76     1222   1399   1506     18     49    -21       C  
ATOM    557  C  AVAL A  76      30.351  12.490  27.947  0.50  9.97           C  
ANISOU  557  C  AVAL A  76     1261   1256   1268    -19     22     20       C  
ATOM    558  C  BVAL A  76      30.330  12.470  27.931  0.50 10.18           C  
ANISOU  558  C  BVAL A  76     1299   1280   1287    -13     18     17       C  
ATOM    559  O  AVAL A  76      29.639  12.869  27.021  0.50 10.49           O  
ANISOU  559  O  AVAL A  76     1386   1307   1291     64    -72    -19       O  
ATOM    560  O  BVAL A  76      29.596  12.769  26.993  0.50 10.73           O  
ANISOU  560  O  BVAL A  76     1417   1338   1319     69    -71     37       O  
ATOM    561  CB AVAL A  76      32.445  11.123  27.723  0.50 11.33           C  
ANISOU  561  CB AVAL A  76      976   1654   1672     92    134    -55       C  
ATOM    562  CB BVAL A  76      32.481  11.234  27.525  0.50 12.35           C  
ANISOU  562  CB BVAL A  76     1096   1795   1800     92    127   -105       C  
ATOM    563  CG1AVAL A  76      31.714  10.340  26.643  0.50 12.38           C  
ANISOU  563  CG1AVAL A  76     1180   1611   1909    160     71   -140       C  
ATOM    564  CG1BVAL A  76      33.929  11.393  27.070  0.50 17.24           C  
ANISOU  564  CG1BVAL A  76     1551   2357   2642     38    124    150       C  
ATOM    565  CG2AVAL A  76      33.944  11.167  27.442  0.50 16.44           C  
ANISOU  565  CG2AVAL A  76     1331   2318   2596     64    153    190       C  
ATOM    566  CG2BVAL A  76      32.390  10.346  28.750  0.50 16.24           C  
ANISOU  566  CG2BVAL A  76     1784   1964   2420    147    -19     34       C  
ATOM    567  N   GLU A  77      29.862  12.081  29.114  1.00  9.44           N  
ANISOU  567  N   GLU A  77     1182   1100   1302     51    180    169       N  
ATOM    568  CA  GLU A  77      28.422  11.969  29.357  1.00  8.56           C  
ANISOU  568  CA  GLU A  77     1144    962   1146    -16    125    126       C  
ATOM    569  C   GLU A  77      27.749  13.333  29.247  1.00  8.88           C  
ANISOU  569  C   GLU A  77     1090   1110   1171    -33     47      2       C  
ATOM    570  O   GLU A  77      26.659  13.470  28.692  1.00  8.68           O  
ANISOU  570  O   GLU A  77     1136   1099   1064    -70    -62    -50       O  
ATOM    571  CB  GLU A  77      28.160  11.341  30.725  1.00  9.20           C  
ANISOU  571  CB  GLU A  77     1493    836   1164     65    109    289       C  
ATOM    572  CG  GLU A  77      28.599   9.891  30.821  1.00  9.57           C  
ANISOU  572  CG  GLU A  77     1323    962   1350     -5    110     53       C  
ATOM    573  CD  GLU A  77      28.408   9.323  32.215  1.00  9.83           C  
ANISOU  573  CD  GLU A  77     1451    924   1358   -211    135     42       C  
ATOM    574  OE1 GLU A  77      28.306  10.131  33.165  1.00 12.00           O  
ANISOU  574  OE1 GLU A  77     1794   1177   1588     96    224    106       O  
ATOM    575  OE2 GLU A  77      28.356   8.075  32.363  1.00 11.89           O  
ANISOU  575  OE2 GLU A  77     1606   1291   1619    -23     31    242       O  
ATOM    576  N   PHE A  78      28.422  14.358  29.749  1.00  8.47           N  
ANISOU  576  N   PHE A  78     1151    974   1091   -151     99      1       N  
ATOM    577  CA  PHE A  78      27.885  15.705  29.662  1.00  8.91           C  
ANISOU  577  CA  PHE A  78     1308   1061   1016    -71    -70     50       C  
ATOM    578  C   PHE A  78      27.717  16.161  28.204  1.00  8.47           C  
ANISOU  578  C   PHE A  78      986   1222   1009     35     13     37       C  
ATOM    579  O   PHE A  78      26.702  16.760  27.840  1.00  8.61           O  
ANISOU  579  O   PHE A  78     1029   1084   1158    167    -74     63       O  
ATOM    580  CB  PHE A  78      28.798  16.663  30.423  1.00  8.97           C  
ANISOU  580  CB  PHE A  78     1205    970   1232      0     24   -229       C  
ATOM    581  CG  PHE A  78      28.285  18.077  30.489  1.00  8.32           C  
ANISOU  581  CG  PHE A  78      920   1037   1201     12   -195    -56       C  
ATOM    582  CD1 PHE A  78      27.341  18.435  31.439  1.00 11.29           C  
ANISOU  582  CD1 PHE A  78     1033   1596   1658    207    -17   -104       C  
ATOM    583  CD2 PHE A  78      28.729  19.042  29.589  1.00 10.06           C  
ANISOU  583  CD2 PHE A  78     1217   1004   1597   -131   -299     23       C  
ATOM    584  CE1 PHE A  78      26.898  19.736  31.535  1.00 11.15           C  
ANISOU  584  CE1 PHE A  78     1184   1269   1782     94    -46   -269       C  
ATOM    585  CE2 PHE A  78      28.278  20.358  29.680  1.00 11.14           C  
ANISOU  585  CE2 PHE A  78     1496   1129   1606      0   -108     -5       C  
ATOM    586  CZ  PHE A  78      27.356  20.692  30.647  1.00 10.53           C  
ANISOU  586  CZ  PHE A  78     1267   1087   1647     45   -300   -214       C  
ATOM    587  N   SER A  79      28.694  15.830  27.365  1.00  9.56           N  
ANISOU  587  N   SER A  79     1075   1527   1028    -51     30    153       N  
ATOM    588  CA  SER A  79      28.641  16.187  25.954  1.00  9.36           C  
ANISOU  588  CA  SER A  79      831   1687   1036   -169    110    -29       C  
ATOM    589  C   SER A  79      27.434  15.525  25.294  1.00  8.61           C  
ANISOU  589  C   SER A  79     1024   1228   1018    -13    125   -112       C  
ATOM    590  O   SER A  79      26.722  16.137  24.508  1.00  9.01           O  
ANISOU  590  O   SER A  79     1169   1156   1099      1    181     40       O  
ATOM    591  CB  SER A  79      29.939  15.751  25.259  1.00  9.74           C  
ANISOU  591  CB  SER A  79      896   1630   1174     62    164    342       C  
ATOM    592  OG  SER A  79      29.859  15.940  23.854  1.00 10.87           O  
ANISOU  592  OG  SER A  79     1328   1737   1062   -153     52    212       O  
ATOM    593  N   ILE A  80      27.249  14.243  25.581  1.00  9.48           N  
ANISOU  593  N   ILE A  80     1204   1193   1203    -87    126    -74       N  
ATOM    594  CA  ILE A  80      26.092  13.524  25.088  1.00  9.28           C  
ANISOU  594  CA  ILE A  80     1162   1189   1171     26     52   -149       C  
ATOM    595  C   ILE A  80      24.770  14.194  25.490  1.00  8.24           C  
ANISOU  595  C   ILE A  80     1104   1007   1018    -16    -19   -239       C  
ATOM    596  O   ILE A  80      23.893  14.412  24.644  1.00  8.99           O  
ANISOU  596  O   ILE A  80     1123   1194   1096    -20    -12     18       O  
ATOM    597  CB  ILE A  80      26.134  12.057  25.545  1.00  8.58           C  
ANISOU  597  CB  ILE A  80     1111    891   1258   -135      6    -94       C  
ATOM    598  CG1 ILE A  80      27.303  11.337  24.859  1.00 13.00           C  
ANISOU  598  CG1 ILE A  80     1611   1382   1944    165    113     36       C  
ATOM    599  CG2 ILE A  80      24.820  11.342  25.247  1.00  8.99           C  
ANISOU  599  CG2 ILE A  80     1228   1062   1123    -66   -308   -104       C  
ATOM    600  CD1 ILE A  80      27.668   9.995  25.455  1.00 12.61           C  
ANISOU  600  CD1 ILE A  80     1610   1318   1861    269     94    -93       C  
ATOM    601  N   ALA A  81      24.654  14.571  26.763  1.00  7.82           N  
ANISOU  601  N   ALA A  81     1094    965    910    222    127    -93       N  
ATOM    602  CA  ALA A  81      23.458  15.257  27.236  1.00  7.83           C  
ANISOU  602  CA  ALA A  81     1004    986    984    152    165   -127       C  
ATOM    603  C   ALA A  81      23.243  16.574  26.498  1.00  7.54           C  
ANISOU  603  C   ALA A  81      998    953    911    124     20    107       C  
ATOM    604  O   ALA A  81      22.128  16.894  26.073  1.00  8.98           O  
ANISOU  604  O   ALA A  81     1146   1204   1059     77     47      0       O  
ATOM    605  CB  ALA A  81      23.560  15.527  28.716  1.00  8.36           C  
ANISOU  605  CB  ALA A  81     1368   1016    790     32    149     79       C  
HETATM  606  N   MSE A  82      24.329  17.318  26.289  1.00  8.95           N  
ANISOU  606  N   MSE A  82     1096   1223   1078     65     95    -11       N  
HETATM  607  CA  MSE A  82      24.216  18.608  25.623  1.00  9.51           C  
ANISOU  607  CA  MSE A  82     1258   1128   1226     73    -15    -38       C  
HETATM  608  C   MSE A  82      23.763  18.439  24.177  1.00  9.34           C  
ANISOU  608  C   MSE A  82     1198   1178   1172    -12    135     96       C  
HETATM  609  O   MSE A  82      22.938  19.215  23.683  1.00  9.44           O  
ANISOU  609  O   MSE A  82     1307   1124   1156    -90    -54    132       O  
HETATM  610  CB  MSE A  82      25.534  19.372  25.688  1.00 11.06           C  
ANISOU  610  CB  MSE A  82     1314   1506   1379   -108     13    187       C  
HETATM  611  CG  MSE A  82      25.938  19.796  27.089  1.00 11.52           C  
ANISOU  611  CG  MSE A  82     1410   1189   1775    322   -301   -300       C  
HETATM  612 SE   MSE A  82      24.688  21.043  27.905  1.00 18.26          SE  
ANISOU  612 SE   MSE A  82     2584   2014   2340    153   -233   -141      SE  
HETATM  613  CE  MSE A  82      25.244  22.663  27.013  1.00 21.01           C  
ANISOU  613  CE  MSE A  82     2774   1990   3218     24   -139     11       C  
ATOM    614  N   LYS A  83      24.256  17.398  23.514  1.00  8.82           N  
ANISOU  614  N   LYS A  83     1107   1327    914    -62    128    136       N  
ATOM    615  CA  LYS A  83      23.837  17.135  22.146  1.00  9.19           C  
ANISOU  615  CA  LYS A  83     1146   1298   1045     61     67    158       C  
ATOM    616  C   LYS A  83      22.346  16.793  22.089  1.00  7.78           C  
ANISOU  616  C   LYS A  83     1067   1028    860     61    -30     56       C  
ATOM    617  O   LYS A  83      21.611  17.284  21.238  1.00  9.43           O  
ANISOU  617  O   LYS A  83     1147   1368   1065    133     38    147       O  
ATOM    618  CB  LYS A  83      24.651  15.985  21.563  1.00 10.89           C  
ANISOU  618  CB  LYS A  83     1222   1774   1138    -83     51   -322       C  
ATOM    619  CG  LYS A  83      24.288  15.632  20.133  1.00 14.55           C  
ANISOU  619  CG  LYS A  83     1711   2504   1314    -50    -94   -340       C  
ATOM    620  CD  LYS A  83      24.724  16.707  19.163  1.00 18.39           C  
ANISOU  620  CD  LYS A  83     2407   3102   1476   -389   -179   -187       C  
ATOM    621  CE  LYS A  83      24.189  16.428  17.774  1.00 24.76           C  
ANISOU  621  CE  LYS A  83     3131   4189   2086   -280   -124   -219       C  
ATOM    622  NZ  LYS A  83      25.189  16.743  16.724  1.00 21.67           N  
ANISOU  622  NZ  LYS A  83     2715   3396   2122   -248     23     -4       N  
ATOM    623  N   LEU A  84      21.896  15.955  23.019  1.00  8.19           N  
ANISOU  623  N   LEU A  84     1017   1059   1035    146    213    136       N  
ATOM    624  CA  LEU A  84      20.490  15.559  23.062  1.00  8.42           C  
ANISOU  624  CA  LEU A  84     1046   1159    995    162     47    167       C  
ATOM    625  C   LEU A  84      19.589  16.757  23.358  1.00  6.96           C  
ANISOU  625  C   LEU A  84     1070    724    849     10    -13     31       C  
ATOM    626  O   LEU A  84      18.502  16.889  22.784  1.00  8.78           O  
ANISOU  626  O   LEU A  84     1105   1064   1166     44    -22    -32       O  
ATOM    627  CB  LEU A  84      20.268  14.444  24.088  1.00  9.42           C  
ANISOU  627  CB  LEU A  84     1210   1227   1142    190    152     42       C  
ATOM    628  CG  LEU A  84      20.919  13.102  23.748  1.00  9.12           C  
ANISOU  628  CG  LEU A  84     1128   1060   1276     53    206   -103       C  
ATOM    629  CD1 LEU A  84      20.897  12.190  24.955  1.00  9.50           C  
ANISOU  629  CD1 LEU A  84     1248    873   1486   -160     64    188       C  
ATOM    630  CD2 LEU A  84      20.234  12.444  22.565  1.00 10.67           C  
ANISOU  630  CD2 LEU A  84     1293   1325   1434     11    101   -307       C  
ATOM    631  N   ILE A  85      20.037  17.638  24.249  1.00  8.21           N  
ANISOU  631  N   ILE A  85     1170    834   1115    210     66    -84       N  
ATOM    632  CA  ILE A  85      19.263  18.837  24.542  1.00  8.58           C  
ANISOU  632  CA  ILE A  85     1259    960   1038    208     24    -25       C  
ATOM    633  C   ILE A  85      19.096  19.719  23.305  1.00  8.84           C  
ANISOU  633  C   ILE A  85     1169    889   1299     39   -158      1       C  
ATOM    634  O   ILE A  85      17.992  20.162  22.990  1.00  9.55           O  
ANISOU  634  O   ILE A  85     1169   1111   1347    206    -64    103       O  
ATOM    635  CB  ILE A  85      19.874  19.632  25.701  1.00  8.50           C  
ANISOU  635  CB  ILE A  85     1235    796   1199    120    -16     -6       C  
ATOM    636  CG1 ILE A  85      19.683  18.875  27.019  1.00  8.98           C  
ANISOU  636  CG1 ILE A  85     1340   1266    804     -5     57    102       C  
ATOM    637  CG2 ILE A  85      19.304  21.049  25.754  1.00 10.35           C  
ANISOU  637  CG2 ILE A  85     1621    802   1509    242   -105    127       C  
ATOM    638  CD1 ILE A  85      20.479  19.453  28.184  1.00 10.18           C  
ANISOU  638  CD1 ILE A  85     1559   1295   1011     39    203   -138       C  
ATOM    639  N   LYS A  86      20.180  19.909  22.562  1.00  9.18           N  
ANISOU  639  N   LYS A  86     1570    897   1019    -68      0    118       N  
ATOM    640  CA  LYS A  86      20.110  20.707  21.340  1.00 11.24           C  
ANISOU  640  CA  LYS A  86     1619   1363   1286    -46     -5    159       C  
ATOM    641  C   LYS A  86      19.166  20.083  20.324  1.00 11.17           C  
ANISOU  641  C   LYS A  86     1580   1372   1291     62    -60    121       C  
ATOM    642  O   LYS A  86      18.327  20.766  19.730  1.00 11.63           O  
ANISOU  642  O   LYS A  86     1704   1355   1360    -14   -329    117       O  
ATOM    643  CB  LYS A  86      21.495  20.921  20.729  1.00 12.89           C  
ANISOU  643  CB  LYS A  86     1736   1713   1445   -292    -94    204       C  
ATOM    644  CG  LYS A  86      21.463  21.795  19.482  1.00 16.32           C  
ANISOU  644  CG  LYS A  86     2243   2229   1726   -260     42    580       C  
ATOM    645  CD  LYS A  86      22.842  22.311  19.117  1.00 21.19           C  
ANISOU  645  CD  LYS A  86     2417   3070   2562   -440    259    355       C  
ATOM    646  CE  LYS A  86      23.619  21.289  18.304  1.00 26.52           C  
ANISOU  646  CE  LYS A  86     3039   3748   3290   -327    237    161       C  
ATOM    647  NZ  LYS A  86      24.714  21.927  17.507  1.00 27.57           N  
ANISOU  647  NZ  LYS A  86     2839   4279   3355   -428    335    122       N  
ATOM    648  N   LEU A  87      19.292  18.777  20.128  1.00 11.25           N  
ANISOU  648  N   LEU A  87     1487   1624   1161    -87     -2    -15       N  
ATOM    649  CA  LEU A  87      18.395  18.086  19.209  1.00 10.43           C  
ANISOU  649  CA  LEU A  87     1422   1431   1109     49    -35    -47       C  
ATOM    650  C   LEU A  87      16.931  18.250  19.614  1.00 10.31           C  
ANISOU  650  C   LEU A  87     1322   1468   1128    144    -56     -5       C  
ATOM    651  O   LEU A  87      16.074  18.538  18.776  1.00 11.23           O  
ANISOU  651  O   LEU A  87     1338   1571   1356    248   -160    120       O  
ATOM    652  CB  LEU A  87      18.750  16.603  19.118  1.00 11.78           C  
ANISOU  652  CB  LEU A  87     1660   1499   1314    158     43   -306       C  
ATOM    653  CG  LEU A  87      20.041  16.252  18.379  1.00 12.77           C  
ANISOU  653  CG  LEU A  87     1742   1787   1321    207    120     51       C  
ATOM    654  CD1 LEU A  87      20.338  14.772  18.591  1.00 14.20           C  
ANISOU  654  CD1 LEU A  87     1912   1774   1707    527    -55   -147       C  
ATOM    655  CD2 LEU A  87      19.903  16.583  16.878  1.00 15.57           C  
ANISOU  655  CD2 LEU A  87     2164   2346   1402    242    -73    210       C  
ATOM    656  N   LYS A  88      16.644  18.087  20.901  1.00 10.15           N  
ANISOU  656  N   LYS A  88     1235   1282   1338    107     10    220       N  
ATOM    657  CA  LYS A  88      15.262  18.223  21.358  1.00 10.60           C  
ANISOU  657  CA  LYS A  88     1305   1420   1302    221    130    139       C  
ATOM    658  C   LYS A  88      14.749  19.659  21.171  1.00 11.74           C  
ANISOU  658  C   LYS A  88     1442   1391   1625    112    -42    257       C  
ATOM    659  O   LYS A  88      13.605  19.871  20.771  1.00 12.97           O  
ANISOU  659  O   LYS A  88     1421   1667   1840    246    -87    179       O  
ATOM    660  CB  LYS A  88      15.129  17.786  22.821  1.00 12.17           C  
ANISOU  660  CB  LYS A  88     1749   1643   1231    131    146    280       C  
ATOM    661  CG  LYS A  88      13.690  17.627  23.313  1.00 20.65           C  
ANISOU  661  CG  LYS A  88     2616   3025   2202   -267    125    155       C  
ATOM    662  CD  LYS A  88      12.854  16.751  22.389  1.00 20.33           C  
ANISOU  662  CD  LYS A  88     2677   2742   2303   -276    222     46       C  
ATOM    663  CE  LYS A  88      11.667  16.127  23.109  1.00 27.64           C  
ANISOU  663  CE  LYS A  88     3429   3607   3463   -296     12    122       C  
ATOM    664  NZ  LYS A  88      10.475  16.013  22.225  1.00 30.37           N  
ANISOU  664  NZ  LYS A  88     3662   4085   3790    -32   -218     15       N  
ATOM    665  N   LEU A  89      15.584  20.646  21.478  1.00 11.20           N  
ANISOU  665  N   LEU A  89     1390   1161   1705    322     26    135       N  
ATOM    666  CA  LEU A  89      15.205  22.037  21.235  1.00 12.80           C  
ANISOU  666  CA  LEU A  89     1660   1368   1835    362   -123    141       C  
ATOM    667  C   LEU A  89      14.904  22.322  19.759  1.00 13.57           C  
ANISOU  667  C   LEU A  89     1653   1628   1873    275   -148    198       C  
ATOM    668  O   LEU A  89      14.108  23.205  19.431  1.00 15.49           O  
ANISOU  668  O   LEU A  89     1852   1823   2209    416   -327     99       O  
ATOM    669  CB  LEU A  89      16.283  22.984  21.751  1.00 13.56           C  
ANISOU  669  CB  LEU A  89     1729   1402   2019    294     -6     88       C  
ATOM    670  CG  LEU A  89      16.392  23.128  23.271  1.00 13.56           C  
ANISOU  670  CG  LEU A  89     1733   1585   1833    556    -33    198       C  
ATOM    671  CD1 LEU A  89      17.678  23.852  23.633  1.00 16.11           C  
ANISOU  671  CD1 LEU A  89     2160   2021   1938    373   -207   -265       C  
ATOM    672  CD2 LEU A  89      15.170  23.869  23.820  1.00 14.02           C  
ANISOU  672  CD2 LEU A  89     2049   1278   2000    442    -16    -91       C  
ATOM    673  N   GLN A  90      15.611  21.634  18.874  1.00 12.16           N  
ANISOU  673  N   GLN A  90     1571   1332   1717    176    -99    295       N  
ATOM    674  CA  GLN A  90      15.404  21.771  17.440  1.00 12.47           C  
ANISOU  674  CA  GLN A  90     1607   1378   1753     84   -261    213       C  
ATOM    675  C   GLN A  90      14.174  21.003  16.961  1.00 12.59           C  
ANISOU  675  C   GLN A  90     1661   1448   1672     -7   -298    282       C  
ATOM    676  O   GLN A  90      13.825  21.062  15.790  1.00 14.34           O  
ANISOU  676  O   GLN A  90     1876   1638   1931   -102   -483    480       O  
ATOM    677  CB  GLN A  90      16.648  21.311  16.674  1.00 12.02           C  
ANISOU  677  CB  GLN A  90     1474   1331   1761    -35   -260    313       C  
ATOM    678  CG  GLN A  90      17.827  22.275  16.790  1.00 11.55           C  
ANISOU  678  CG  GLN A  90     1594   1362   1429   -227   -195    300       C  
ATOM    679  CD  GLN A  90      19.073  21.768  16.081  1.00 16.38           C  
ANISOU  679  CD  GLN A  90     1929   2135   2159     37    -82    207       C  
ATOM    680  OE1 GLN A  90      19.296  20.561  15.976  1.00 21.12           O  
ANISOU  680  OE1 GLN A  90     2286   2777   2960   -227    136    277       O  
ATOM    681  NE2 GLN A  90      19.941  22.689  15.693  1.00 21.94           N  
ANISOU  681  NE2 GLN A  90     2527   2884   2923   -319    -41    380       N  
ATOM    682  N   GLY A  91      13.573  20.219  17.856  1.00 13.94           N  
ANISOU  682  N   GLY A  91     1609   1771   1914   -113   -312    361       N  
ATOM    683  CA  GLY A  91      12.329  19.510  17.541  1.00 14.49           C  
ANISOU  683  CA  GLY A  91     1597   1812   2094    -97   -233    222       C  
ATOM    684  C   GLY A  91      12.478  18.059  17.115  1.00 12.76           C  
ANISOU  684  C   GLY A  91     1316   1635   1894   -108   -174    253       C  
ATOM    685  O   GLY A  91      11.505  17.426  16.703  1.00 14.69           O  
ANISOU  685  O   GLY A  91     1731   1606   2244   -162   -358    304       O  
ATOM    686  N   TYR A  92      13.684  17.510  17.237  1.00 13.43           N  
ANISOU  686  N   TYR A  92     1594   1556   1952   -102   -122    408       N  
ATOM    687  CA  TYR A  92      13.865  16.074  17.046  1.00 13.60           C  
ANISOU  687  CA  TYR A  92     1478   1613   2075   -132   -214    234       C  
ATOM    688  C   TYR A  92      13.243  15.285  18.187  1.00 14.35           C  
ANISOU  688  C   TYR A  92     1603   1863   1985   -183   -113    196       C  
ATOM    689  O   TYR A  92      13.164  15.757  19.317  1.00 15.83           O  
ANISOU  689  O   TYR A  92     2157   1827   2030   -518   -197    121       O  
ATOM    690  CB  TYR A  92      15.342  15.720  16.923  1.00 13.70           C  
ANISOU  690  CB  TYR A  92     1502   1583   2119     11    -90    408       C  
ATOM    691  CG  TYR A  92      15.987  16.277  15.679  1.00 14.39           C  
ANISOU  691  CG  TYR A  92     1787   1962   1715    -21   -331    243       C  
ATOM    692  CD1 TYR A  92      16.561  17.543  15.678  1.00 14.48           C  
ANISOU  692  CD1 TYR A  92     1788   1843   1868    138   -488    556       C  
ATOM    693  CD2 TYR A  92      15.985  15.553  14.492  1.00 14.95           C  
ANISOU  693  CD2 TYR A  92     2432   1710   1538    -76    -57    469       C  
ATOM    694  CE1 TYR A  92      17.132  18.069  14.525  1.00 14.61           C  
ANISOU  694  CE1 TYR A  92     1855   2159   1535    232   -148    223       C  
ATOM    695  CE2 TYR A  92      16.529  16.080  13.328  1.00 16.60           C  
ANISOU  695  CE2 TYR A  92     2621   2046   1639      1     -5    190       C  
ATOM    696  CZ  TYR A  92      17.116  17.324  13.357  1.00 14.07           C  
ANISOU  696  CZ  TYR A  92     1923   1746   1674   -107     51    170       C  
ATOM    697  OH  TYR A  92      17.662  17.838  12.209  1.00 18.22           O  
ANISOU  697  OH  TYR A  92     2668   2259   1994    121    219    339       O  
ATOM    698  N   GLN A  93      12.808  14.068  17.890  1.00 14.02           N  
ANISOU  698  N   GLN A  93     1827   1461   2039    -79    -99    313       N  
ATOM    699  CA  GLN A  93      12.400  13.150  18.947  1.00 15.20           C  
ANISOU  699  CA  GLN A  93     1829   1928   2018    -84   -315    407       C  
ATOM    700  C   GLN A  93      13.627  12.470  19.545  1.00 12.67           C  
ANISOU  700  C   GLN A  93     1319   1723   1769   -149   -156    185       C  
ATOM    701  O   GLN A  93      14.580  12.151  18.828  1.00 16.53           O  
ANISOU  701  O   GLN A  93     1857   2335   2089    151    -28    379       O  
ATOM    702  CB  GLN A  93      11.437  12.103  18.391  1.00 17.39           C  
ANISOU  702  CB  GLN A  93     2217   1942   2449   -268   -291    496       C  
ATOM    703  CG  GLN A  93      10.121  12.674  17.870  1.00 24.53           C  
ANISOU  703  CG  GLN A  93     2712   3265   3343   -104   -416    365       C  
ATOM    704  CD  GLN A  93       9.403  13.538  18.893  1.00 32.82           C  
ANISOU  704  CD  GLN A  93     4098   3973   4397     84   -112    114       C  
ATOM    705  OE1 GLN A  93       9.224  13.142  20.049  1.00 38.23           O  
ANISOU  705  OE1 GLN A  93     4695   5128   4701    192   -116     60       O  
ATOM    706  NE2 GLN A  93       8.961  14.717  18.463  1.00 37.57           N  
ANISOU  706  NE2 GLN A  93     4820   4455   4997    236   -285    195       N  
ATOM    707  N   LEU A  94      13.578  12.200  20.846  1.00 11.92           N  
ANISOU  707  N   LEU A  94     1417   1236   1874    -90   -111    239       N  
ATOM    708  CA  LEU A  94      14.665  11.486  21.500  1.00 12.43           C  
ANISOU  708  CA  LEU A  94     1486   1344   1890    110    -58     -1       C  
ATOM    709  C   LEU A  94      14.616  10.009  21.138  1.00 12.70           C  
ANISOU  709  C   LEU A  94     1619   1256   1947     78    -52     44       C  
ATOM    710  O   LEU A  94      13.538   9.431  21.003  1.00 13.32           O  
ANISOU  710  O   LEU A  94     1823   1187   2051     78   -127   -200       O  
ATOM    711  CB  LEU A  94      14.590  11.644  23.020  1.00 11.96           C  
ANISOU  711  CB  LEU A  94     1820   1098   1625     98   -156     94       C  
ATOM    712  CG  LEU A  94      14.824  13.051  23.582  1.00 11.12           C  
ANISOU  712  CG  LEU A  94     1655    963   1607     32      7    -95       C  
ATOM    713  CD1 LEU A  94      14.500  13.074  25.067  1.00 14.58           C  
ANISOU  713  CD1 LEU A  94     2075   1808   1656     61    210   -508       C  
ATOM    714  CD2 LEU A  94      16.258  13.477  23.339  1.00 14.15           C  
ANISOU  714  CD2 LEU A  94     1914   1509   1950   -140    -21     -6       C  
ATOM    715  N   PRO A  95      15.787   9.367  21.079  1.00 13.13           N  
ANISOU  715  N   PRO A  95     1481   1248   2257     68   -106    -66       N  
ATOM    716  CA  PRO A  95      15.852   7.932  20.816  1.00 14.70           C  
ANISOU  716  CA  PRO A  95     1858   1380   2346    193     11   -275       C  
ATOM    717  C   PRO A  95      15.511   7.094  22.051  1.00 14.97           C  
ANISOU  717  C   PRO A  95     1846   1573   2268    284    -51   -237       C  
ATOM    718  O   PRO A  95      15.589   7.576  23.175  1.00 15.48           O  
ANISOU  718  O   PRO A  95     2013   1661   2205    268   -189   -252       O  
ATOM    719  CB  PRO A  95      17.315   7.731  20.414  1.00 14.66           C  
ANISOU  719  CB  PRO A  95     1861   1491   2218    171     40   -209       C  
ATOM    720  CG  PRO A  95      18.051   8.769  21.205  1.00 14.76           C  
ANISOU  720  CG  PRO A  95     1942   1599   2064    262     72   -417       C  
ATOM    721  CD  PRO A  95      17.127   9.970  21.230  1.00 14.13           C  
ANISOU  721  CD  PRO A  95     1700   1333   2334     96    -55    -88       C  
ATOM    722  N   SER A  96      15.145   5.832  21.842  1.00 14.10           N  
ANISOU  722  N   SER A  96     1703   1358   2295    147     35   -181       N  
ATOM    723  CA  SER A  96      14.781   4.952  22.952  1.00 16.25           C  
ANISOU  723  CA  SER A  96     1824   2020   2328    119    128   -109       C  
ATOM    724  C   SER A  96      16.009   4.406  23.676  1.00 16.51           C  
ANISOU  724  C   SER A  96     2067   2051   2156    173    128     46       C  
ATOM    725  O   SER A  96      15.893   3.777  24.731  1.00 19.22           O  
ANISOU  725  O   SER A  96     2392   2686   2223    317     78    -60       O  
ATOM    726  CB  SER A  96      13.910   3.795  22.456  1.00 16.61           C  
ANISOU  726  CB  SER A  96     2324   1748   2237    298    -51   -393       C  
ATOM    727  OG  SER A  96      14.640   2.941  21.590  1.00 19.75           O  
ANISOU  727  OG  SER A  96     2685   2221   2596   -295    301   -420       O  
ATOM    728  N   ALA A  97      17.141   4.457  22.986  1.00 14.46           N  
ANISOU  728  N   ALA A  97     1824   1626   2043    172    178   -151       N  
ATOM    729  CA  ALA A  97      18.425   4.075  23.555  1.00 14.07           C  
ANISOU  729  CA  ALA A  97     1873   1211   2262    207    224   -259       C  
ATOM    730  C   ALA A  97      19.485   4.964  22.921  1.00 11.49           C  
ANISOU  730  C   ALA A  97     1375   1208   1781     36     93   -273       C  
ATOM    731  O   ALA A  97      19.251   5.598  21.877  1.00 13.03           O  
ANISOU  731  O   ALA A  97     1533   1350   2067      3    -59   -214       O  
ATOM    732  CB  ALA A  97      18.724   2.598  23.269  1.00 16.81           C  
ANISOU  732  CB  ALA A  97     2123   1657   2605     80     72   -402       C  
ATOM    733  N   LEU A  98      20.623   5.082  23.592  1.00 12.84           N  
ANISOU  733  N   LEU A  98     1581   1411   1884     66     91   -373       N  
ATOM    734  CA  LEU A  98      21.686   5.958  23.118  1.00 13.71           C  
ANISOU  734  CA  LEU A  98     1664   1762   1782      4    122   -306       C  
ATOM    735  C   LEU A  98      22.245   5.458  21.781  1.00 13.54           C  
ANISOU  735  C   LEU A  98     1700   1579   1865     99    188   -287       C  
ATOM    736  O   LEU A  98      22.663   4.307  21.682  1.00 14.31           O  
ANISOU  736  O   LEU A  98     1888   1371   2177    194    159   -490       O  
ATOM    737  CB  LEU A  98      22.796   6.002  24.160  1.00 16.98           C  
ANISOU  737  CB  LEU A  98     2010   2370   2069   -190    -24   -341       C  
ATOM    738  CG  LEU A  98      23.825   7.104  23.942  1.00 19.03           C  
ANISOU  738  CG  LEU A  98     2372   2563   2294   -345    276     90       C  
ATOM    739  CD1 LEU A  98      23.139   8.469  23.925  1.00 18.78           C  
ANISOU  739  CD1 LEU A  98     2908   1965   2261   -639    110    117       C  
ATOM    740  CD2 LEU A  98      24.874   7.033  25.029  1.00 24.52           C  
ANISOU  740  CD2 LEU A  98     2688   3602   3023   -202   -184   -340       C  
ATOM    741  N   PRO A  99      22.156   6.278  20.723  1.00 12.12           N  
ANISOU  741  N   PRO A  99     1669   1112   1823     94    -11   -582       N  
ATOM    742  CA  PRO A  99      22.744   5.851  19.453  1.00 12.10           C  
ANISOU  742  CA  PRO A  99     1531   1330   1734    168    120   -335       C  
ATOM    743  C   PRO A  99      24.241   5.579  19.599  1.00 13.11           C  
ANISOU  743  C   PRO A  99     1506   1645   1831     94    -98   -449       C  
ATOM    744  O   PRO A  99      24.975   6.409  20.141  1.00 12.81           O  
ANISOU  744  O   PRO A  99     1511   1593   1763   -147    -19   -518       O  
ATOM    745  CB  PRO A  99      22.519   7.059  18.544  1.00 14.28           C  
ANISOU  745  CB  PRO A  99     1823   1536   2066    136    -11   -241       C  
ATOM    746  CG  PRO A  99      21.302   7.725  19.112  1.00 13.57           C  
ANISOU  746  CG  PRO A  99     1729   1538   1887    268   -106   -463       C  
ATOM    747  CD  PRO A  99      21.446   7.564  20.599  1.00 13.37           C  
ANISOU  747  CD  PRO A  99     1664   1410   2003    239    -13   -210       C  
ATOM    748  N   PRO A 100      24.698   4.405  19.136  1.00 12.91           N  
ANISOU  748  N   PRO A 100     1588   1371   1944     27   -241   -579       N  
ATOM    749  CA  PRO A 100      26.120   4.062  19.253  1.00 12.72           C  
ANISOU  749  CA  PRO A 100     1574   1489   1767    167    -85   -637       C  
ATOM    750  C   PRO A 100      27.054   5.124  18.663  1.00 13.67           C  
ANISOU  750  C   PRO A 100     1578   1719   1894    310   -108   -502       C  
ATOM    751  O   PRO A 100      28.107   5.403  19.241  1.00 15.75           O  
ANISOU  751  O   PRO A 100     1729   2111   2143    184   -297   -629       O  
ATOM    752  CB  PRO A 100      26.217   2.745  18.470  1.00 13.90           C  
ANISOU  752  CB  PRO A 100     1783   1374   2123    269   -231   -381       C  
ATOM    753  CG  PRO A 100      24.882   2.110  18.697  1.00 15.66           C  
ANISOU  753  CG  PRO A 100     1914   1565   2468     70   -269   -665       C  
ATOM    754  CD  PRO A 100      23.889   3.259  18.677  1.00 14.67           C  
ANISOU  754  CD  PRO A 100     1953   1422   2197     28   -133   -426       C  
ATOM    755  N   VAL A 101      26.617   5.813  17.613  1.00 13.56           N  
ANISOU  755  N   VAL A 101     1730   1559   1861    141    164   -488       N  
ATOM    756  CA  VAL A 101      27.459   6.845  16.994  1.00 13.88           C  
ANISOU  756  CA  VAL A 101     1647   1849   1775     25    178   -519       C  
ATOM    757  C   VAL A 101      27.746   8.019  17.944  1.00 15.60           C  
ANISOU  757  C   VAL A 101     1786   2088   2053   -135    281   -631       C  
ATOM    758  O   VAL A 101      28.720   8.750  17.760  1.00 17.62           O  
ANISOU  758  O   VAL A 101     1917   2494   2283   -175    421   -642       O  
ATOM    759  CB  VAL A 101      26.855   7.361  15.680  1.00 17.08           C  
ANISOU  759  CB  VAL A 101     1968   2161   2359    -20    151   -284       C  
ATOM    760  CG1 VAL A 101      25.588   8.159  15.944  1.00 16.22           C  
ANISOU  760  CG1 VAL A 101     1773   2062   2325     51   -101   -284       C  
ATOM    761  CG2 VAL A 101      27.885   8.183  14.908  1.00 19.95           C  
ANISOU  761  CG2 VAL A 101     2443   3092   2042    -43    421   -148       C  
HETATM  762  N   MSE A 102      26.934   8.166  18.989  1.00 15.31           N  
ANISOU  762  N   MSE A 102     1904   1885   2025   -274    132   -630       N  
HETATM  763  CA  MSE A 102      27.103   9.275  19.921  1.00 17.96           C  
ANISOU  763  CA  MSE A 102     2105   2177   2540   -209     66   -399       C  
HETATM  764  C   MSE A 102      28.199   9.006  20.933  1.00 18.22           C  
ANISOU  764  C   MSE A 102     2209   2377   2335   -268     61   -486       C  
HETATM  765  O   MSE A 102      28.581   9.905  21.692  1.00 20.16           O  
ANISOU  765  O   MSE A 102     2533   2529   2597   -395     -4   -670       O  
HETATM  766  CB  MSE A 102      25.809   9.505  20.679  1.00 18.38           C  
ANISOU  766  CB  MSE A 102     2249   2083   2650   -182    451   -610       C  
HETATM  767  CG  MSE A 102      24.751  10.214  19.902  1.00 22.08           C  
ANISOU  767  CG  MSE A 102     2730   2967   2689   -131    186     34       C  
HETATM  768 SE   MSE A 102      23.496  11.056  21.135  1.00 26.76          SE  
ANISOU  768 SE   MSE A 102     3015   3686   3464    666    809   1080      SE  
HETATM  769  CE  MSE A 102      24.429  12.699  21.439  1.00 24.07           C  
ANISOU  769  CE  MSE A 102     3409   3454   2279   1227    386   -742       C  
ATOM    770  N   LYS A 103      28.518   7.729  21.108  1.00 20.00           N  
ANISOU  770  N   LYS A 103     2512   2537   2550   -204   -120   -409       N  
ATOM    771  CA  LYS A 103      29.493   7.308  22.105  1.00 23.64           C  
ANISOU  771  CA  LYS A 103     2921   3212   2849   -270   -140   -147       C  
ATOM    772  C   LYS A 103      30.910   7.412  21.566  1.00 26.17           C  
ANISOU  772  C   LYS A 103     3153   3729   3061   -114   -128    -52       C  
ATOM    773  O   LYS A 103      31.875   7.349  22.328  1.00 29.04           O  
ANISOU  773  O   LYS A 103     3436   4061   3536   -207   -276     37       O  
ATOM    774  CB  LYS A 103      29.207   5.876  22.561  1.00 24.35           C  
ANISOU  774  CB  LYS A 103     3156   3261   2833   -213   -177     45       C  
ATOM    775  CG  LYS A 103      27.797   5.674  23.097  1.00 28.86           C  
ANISOU  775  CG  LYS A 103     3726   3923   3314   -137     85   -193       C  
ATOM    776  CD  LYS A 103      27.396   4.208  23.087  1.00 34.18           C  
ANISOU  776  CD  LYS A 103     4793   4262   3930   -127    -33    140       C  
ATOM    777  CE  LYS A 103      25.902   4.055  22.848  1.00 35.62           C  
ANISOU  777  CE  LYS A 103     4731   4586   4215    -63    164    -36       C  
ATOM    778  NZ  LYS A 103      25.390   2.726  23.297  1.00 39.01           N  
ANISOU  778  NZ  LYS A 103     5042   4627   5152    -35    127     54       N  
TER     779      LYS A 103                                                      
HETATM  780 CA    CA A 201      27.866   8.410  34.792  1.00 11.60          CA  
ANISOU  780 CA    CA A 201     1420   1430   1558     -6   -102    309      CA  
HETATM  781  S   SO4 A 301      23.628  21.630  13.932  1.00 29.31           S  
ANISOU  781  S   SO4 A 301     3867   3128   4142    -99     38   1088       S  
HETATM  782  O1  SO4 A 301      23.870  21.206  12.558  1.00 34.87           O  
ANISOU  782  O1  SO4 A 301     4859   4089   4299    263    -46    122       O  
HETATM  783  O2  SO4 A 301      22.197  21.851  14.123  1.00 32.63           O  
ANISOU  783  O2  SO4 A 301     3691   4221   4485    266     58    363       O  
HETATM  784  O3  SO4 A 301      24.090  20.583  14.845  1.00 33.44           O  
ANISOU  784  O3  SO4 A 301     4491   3934   4278    249   -244    787       O  
HETATM  785  O4  SO4 A 301      24.329  22.888  14.190  1.00 34.29           O  
ANISOU  785  O4  SO4 A 301     4496   3830   4701   -279   -120    295       O  
HETATM  786  O   HOH A 401      35.370  14.246  33.067  1.00 12.68           O  
ANISOU  786  O   HOH A 401     1158   2179   1477     78   -141    -47       O  
HETATM  787  O   HOH A 402      31.596  17.989  27.647  1.00 12.00           O  
ANISOU  787  O   HOH A 402     1299   1632   1626   -274     27    214       O  
HETATM  788  O   HOH A 403      30.159   8.591  35.498  1.00 14.53           O  
ANISOU  788  O   HOH A 403     1646   1816   2057    -39   -266    172       O  
HETATM  789  O   HOH A 404      38.600  18.642  26.446  1.00 14.13           O  
ANISOU  789  O   HOH A 404     1497   2522   1349    157   -260     32       O  
HETATM  790  O   HOH A 405      37.221  19.087  23.163  1.00 15.49           O  
ANISOU  790  O   HOH A 405     1409   2519   1955   -135   -188    390       O  
HETATM  791  O   HOH A 406      35.939  20.434  30.527  1.00 14.29           O  
ANISOU  791  O   HOH A 406     1878   1880   1669   -107     10   -201       O  
HETATM  792  O   HOH A 407      20.943   5.904  32.922  1.00 16.78           O  
ANISOU  792  O   HOH A 407     2320   1804   2250   -212    -47    186       O  
HETATM  793  O   HOH A 408      31.431  13.999  22.586  1.00 15.11           O  
ANISOU  793  O   HOH A 408     1534   2281   1925   -111    -79   -100       O  
HETATM  794  O   HOH A 409      24.585  16.121   6.926  1.00 20.37           O  
ANISOU  794  O   HOH A 409     2770   2511   2456     13    216   -394       O  
HETATM  795  O   HOH A 410      22.705   5.153  27.831  1.00 16.10           O  
ANISOU  795  O   HOH A 410     2363   1241   2511    -69    334     92       O  
HETATM  796  O   HOH A 411      32.242   7.809  33.872  1.00 22.27           O  
ANISOU  796  O   HOH A 411     2971   2522   2967    449    316    105       O  
HETATM  797  O   HOH A 412      36.800  18.944  20.455  1.00 17.35           O  
ANISOU  797  O   HOH A 412     1863   3195   1533   -450    221    425       O  
HETATM  798  O   HOH A 413      18.456  20.310  12.425  1.00 19.97           O  
ANISOU  798  O   HOH A 413     3152   1857   2578     -7    110    404       O  
HETATM  799  O   HOH A 414      14.646  14.448  36.695  1.00 17.69           O  
ANISOU  799  O   HOH A 414     2266   1994   2461    150    -80   -536       O  
HETATM  800  O   HOH A 415      25.565  12.098  41.931  1.00 18.33           O  
ANISOU  800  O   HOH A 415     2863   2479   1619    -50   -276    461       O  
HETATM  801  O   HOH A 416      30.508   6.674  31.649  1.00 21.18           O  
ANISOU  801  O   HOH A 416     2617   2223   3205    989    241    -61       O  
HETATM  802  O   HOH A 417      39.247  18.387  29.134  1.00 19.27           O  
ANISOU  802  O   HOH A 417     1822   3334   2165   -102   -337     54       O  
HETATM  803  O   HOH A 418      36.929  16.494  32.831  1.00 18.66           O  
ANISOU  803  O   HOH A 418     2158   3230   1700   -472    241     25       O  
HETATM  804  O   HOH A 419      20.583   3.957  26.467  1.00 17.79           O  
ANISOU  804  O   HOH A 419     1884   1186   3688   -141   -325     20       O  
HETATM  805  O   HOH A 420      16.963  18.323  34.326  1.00 18.85           O  
ANISOU  805  O   HOH A 420     2415   1387   3358   -240   -791    -55       O  
HETATM  806  O   HOH A 421      14.385   5.861   8.303  1.00 23.44           O  
ANISOU  806  O   HOH A 421     2975   2248   3682    321   -835   -723       O  
HETATM  807  O   HOH A 422       9.197  23.541  27.220  1.00 16.95           O  
ANISOU  807  O   HOH A 422     1898   1886   2656   -154    -42   -355       O  
HETATM  808  O   HOH A 423      13.966  23.096  31.791  1.00 21.89           O  
ANISOU  808  O   HOH A 423     3322   2321   2673   1192  -1745   -893       O  
HETATM  809  O   HOH A 424      11.106  12.668  22.276  1.00 22.72           O  
ANISOU  809  O   HOH A 424     1905   3547   3180    -44    187    371       O  
HETATM  810  O   HOH A 425      27.958   9.517  11.040  1.00 18.23           O  
ANISOU  810  O   HOH A 425     2767   2089   2068    -34    388    -13       O  
HETATM  811  O   HOH A 426      21.818  10.954  39.827  1.00 17.25           O  
ANISOU  811  O   HOH A 426     1995   2181   2377    120    -34    611       O  
HETATM  812  O   HOH A 427      34.868  11.984  30.274  1.00 22.43           O  
ANISOU  812  O   HOH A 427     2064   3155   3301    287    155    396       O  
HETATM  813  O   HOH A 428      32.164   8.033  30.115  1.00 27.50           O  
ANISOU  813  O   HOH A 428     4178   3097   3172   -338    369   -322       O  
HETATM  814  O   HOH A 429      38.946  16.139  43.986  1.00 20.72           O  
ANISOU  814  O   HOH A 429     2547   3168   2154   -128   -142     92       O  
HETATM  815  O   HOH A 430      12.925  13.162  15.119  1.00 24.59           O  
ANISOU  815  O   HOH A 430     4047   2344   2952     13   -146    -61       O  
HETATM  816  O   HOH A 431      30.267  18.528  42.190  1.00 22.19           O  
ANISOU  816  O   HOH A 431     2518   3350   2562   -103    113    -89       O  
HETATM  817  O   HOH A 432      38.615  21.502  23.242  1.00 22.15           O  
ANISOU  817  O   HOH A 432     2361   3031   3022   -264   -670    687       O  
HETATM  818  O   HOH A 433      24.169  10.549  12.936  1.00 21.40           O  
ANISOU  818  O   HOH A 433     3405   2484   2242    393    968   -120       O  
HETATM  819  O   HOH A 434      16.366  15.447  34.631  1.00 22.70           O  
ANISOU  819  O   HOH A 434     4614   2045   1964   -324   -707     56       O  
HETATM  820  O   HOH A 435      35.014  11.192  23.906  1.00 28.34           O  
ANISOU  820  O   HOH A 435     2843   3983   3942    677    150   -153       O  
HETATM  821  O   HOH A 436      34.113  16.512  13.840  1.00 28.55           O  
ANISOU  821  O   HOH A 436     3712   4593   2542    244    694   -130       O  
HETATM  822  O   HOH A 437      14.203  11.878  37.583  1.00 19.59           O  
ANISOU  822  O   HOH A 437     4054   2038   1350   -194     15   -394       O  
HETATM  823  O   HOH A 438      29.306  18.457  44.787  1.00 21.84           O  
ANISOU  823  O   HOH A 438     2299   3569   2428   -215    518   -100       O  
HETATM  824  O   HOH A 439      20.704   8.766  41.123  1.00 19.38           O  
ANISOU  824  O   HOH A 439     2453   2664   2245   -321     37    427       O  
HETATM  825  O   HOH A 440      31.244  15.824  41.830  1.00 19.19           O  
ANISOU  825  O   HOH A 440     1920   3280   2088   -226     70   -258       O  
HETATM  826  O   HOH A 441      17.857  28.312  27.558  1.00 27.40           O  
ANISOU  826  O   HOH A 441     4480   2233   3699    165    471    952       O  
HETATM  827  O   HOH A 442      29.835  11.163  18.105  1.00 20.98           O  
ANISOU  827  O   HOH A 442     1989   2580   3402   -169   -295    300       O  
HETATM  828  O   HOH A 443      23.012  17.392  14.739  1.00 24.25           O  
ANISOU  828  O   HOH A 443     3901   2524   2786    365     -7     -6       O  
HETATM  829  O   HOH A 444      19.045  25.697  37.604  1.00 21.93           O  
ANISOU  829  O   HOH A 444     2651   2894   2784    385    -64   -305       O  
HETATM  830  O   HOH A 445      27.990  18.490   8.409  1.00 22.10           O  
ANISOU  830  O   HOH A 445     2933   2894   2570      3    287    253       O  
HETATM  831  O   HOH A 446      38.679  20.908  19.562  1.00 27.06           O  
ANISOU  831  O   HOH A 446     2750   3169   4362   -223    138    771       O  
HETATM  832  O   HOH A 447      19.748  16.222  11.242  1.00 25.15           O  
ANISOU  832  O   HOH A 447     3504   2381   3670    476    779    753       O  
HETATM  833  O   HOH A 448      33.018   9.686  23.370  1.00 33.28           O  
ANISOU  833  O   HOH A 448     4380   4303   3961    263   -185    205       O  
HETATM  834  O   HOH A 449      19.601   4.537  29.860  1.00 20.73           O  
ANISOU  834  O   HOH A 449     2755   2121   3000   -559    679   -412       O  
HETATM  835  O   HOH A 450      28.889  14.799  12.636  1.00 24.68           O  
ANISOU  835  O   HOH A 450     3175   3398   2801   -423    338    455       O  
HETATM  836  O   HOH A 451      24.026  22.924  38.564  1.00 24.42           O  
ANISOU  836  O   HOH A 451     3757   2607   2911   -349   -235   -650       O  
HETATM  837  O   HOH A 452      28.216  12.167  43.102  1.00 30.00           O  
ANISOU  837  O   HOH A 452     3549   4286   3562   -301    455    346       O  
HETATM  838  O   HOH A 453      25.435  21.152  21.219  1.00 27.04           O  
ANISOU  838  O   HOH A 453     2708   3928   3637    226   -379    444       O  
HETATM  839  O   HOH A 454      26.219  23.682  19.637  1.00 29.92           O  
ANISOU  839  O   HOH A 454     3764   3987   3614   -190      0   -126       O  
HETATM  840  O   HOH A 455      36.999  12.142  32.673  1.00 27.59           O  
ANISOU  840  O   HOH A 455     3036   3024   4420    765    763   -221       O  
HETATM  841  O   HOH A 456      27.044  16.298  14.072  1.00 24.86           O  
ANISOU  841  O   HOH A 456     2921   4072   2451   -304    240    -29       O  
HETATM  842  O   HOH A 457      21.398   6.593  35.211  1.00 21.69           O  
ANISOU  842  O   HOH A 457     1999   2627   3612    109    456    749       O  
HETATM  843  O   HOH A 458      34.371  13.524  42.153  1.00 27.77           O  
ANISOU  843  O   HOH A 458     3778   3932   2841   -606   -162    480       O  
HETATM  844  O   HOH A 459      22.497  17.114   7.937  1.00 29.38           O  
ANISOU  844  O   HOH A 459     3520   3254   4387    595    254   -306       O  
HETATM  845  O   HOH A 460      20.000  10.436   5.932  1.00 21.39           O  
ANISOU  845  O   HOH A 460     2504   2599   3024   -397    469   -483       O  
HETATM  846  O   HOH A 461      23.078  13.647  42.784  1.00 27.06           O  
ANISOU  846  O   HOH A 461     3901   3684   2695    241    625    785       O  
HETATM  847  O   HOH A 462      37.038  13.263  29.031  1.00 21.57           O  
ANISOU  847  O   HOH A 462     2393   2763   3037    386    423    877       O  
HETATM  848  O   HOH A 463      13.558   2.819  26.224  1.00 23.88           O  
ANISOU  848  O   HOH A 463     2832   2905   3336   -441    175    561       O  
HETATM  849  O   HOH A 464       7.638  17.157  36.159  1.00 26.94           O  
ANISOU  849  O   HOH A 464     3189   2415   4631    228    677    848       O  
HETATM  850  O   HOH A 465      21.846  19.578  16.073  1.00 27.56           O  
ANISOU  850  O   HOH A 465     3478   2872   4121    124    311    288       O  
HETATM  851  O   HOH A 466      36.977  15.165  45.748  1.00 24.43           O  
ANISOU  851  O   HOH A 466     3018   3484   2778     43   -416    119       O  
HETATM  852  O   HOH A 467      26.516   7.209  11.427  1.00 24.73           O  
ANISOU  852  O   HOH A 467     3086   2682   3628   -548    381   -565       O  
HETATM  853  O   HOH A 468      11.707  14.508   8.332  1.00 43.55           O  
ANISOU  853  O   HOH A 468     5865   5350   5331     -5    163   -282       O  
HETATM  854  O   HOH A 469      37.854  21.555  34.642  1.00 28.62           O  
ANISOU  854  O   HOH A 469     3511   4385   2976     96   -680   -664       O  
HETATM  855  O   HOH A 470      37.028  23.243  24.787  1.00 26.08           O  
ANISOU  855  O   HOH A 470     2408   3774   3727   -315   -261    379       O  
HETATM  856  O   HOH A 471      11.680   9.149  22.927  1.00 29.40           O  
ANISOU  856  O   HOH A 471     3750   4049   3372   -765   -255   -134       O  
HETATM  857  O   HOH A 472      30.025  13.359  41.439  1.00 19.71           O  
ANISOU  857  O   HOH A 472     2258   3146   2084     23    136    -48       O  
HETATM  858  O   HOH A 473      32.349  11.833  41.950  1.00 18.43           O  
ANISOU  858  O   HOH A 473     2314   2711   1978    108    -16    290       O  
HETATM  859  O   HOH A 474      30.005  16.155  45.763  1.00 26.04           O  
ANISOU  859  O   HOH A 474     3602   3407   2881      9   -339   -215       O  
HETATM  860  O   HOH A 475      30.375  20.594  46.171  1.00 27.42           O  
ANISOU  860  O   HOH A 475     4044   3330   3041   -363    322   -171       O  
HETATM  861  O   HOH A 476      21.884  16.750  10.045  1.00 25.14           O  
ANISOU  861  O   HOH A 476     3165   2118   4268    372    143    360       O  
HETATM  862  O   HOH A 477      35.534  16.875  47.490  1.00 28.40           O  
ANISOU  862  O   HOH A 477     3018   4637   3132   -296    169    -48       O  
HETATM  863  O   HOH A 478       8.239  22.781  24.643  1.00 22.22           O  
ANISOU  863  O   HOH A 478     4086   2005   2348   -210    730   -388       O  
HETATM  864  O   HOH A 479      25.921   9.144  41.942  1.00 25.61           O  
ANISOU  864  O   HOH A 479     3818   3087   2823    303   -764     40       O  
HETATM  865  O   HOH A 480      30.752  11.277  22.486  1.00 26.09           O  
ANISOU  865  O   HOH A 480     2465   3584   3864    -18   -454   -340       O  
HETATM  866  O   HOH A 481      35.689   9.972  33.210  1.00 29.86           O  
ANISOU  866  O   HOH A 481     2657   3866   4823    560   -130    136       O  
HETATM  867  O   HOH A 482      34.596  13.920  44.664  1.00 34.88           O  
ANISOU  867  O   HOH A 482     4771   4486   3993     -7   -219   -146       O  
HETATM  868  O   HOH A 483      11.008  12.909  25.461  1.00 28.74           O  
ANISOU  868  O   HOH A 483     3461   2625   4830    131     53   -365       O  
HETATM  869  O   HOH A 484      30.024  10.314  12.512  1.00 27.88           O  
ANISOU  869  O   HOH A 484     4009   4261   2320    -83    233   -542       O  
HETATM  870  O   HOH A 485      13.855   2.464  19.335  1.00 27.51           O  
ANISOU  870  O   HOH A 485     3543   3993   2917   -389    330   -460       O  
HETATM  871  O   HOH A 486      29.895   2.948  19.653  1.00 42.10           O  
ANISOU  871  O   HOH A 486     4853   5557   5585     48   -286      0       O  
HETATM  872  O   HOH A 487      31.000   4.297  30.740  1.00 34.59           O  
ANISOU  872  O   HOH A 487     4956   3724   4461    393    304    256       O  
HETATM  873  O   HOH A 488      31.125  20.917  41.491  1.00 36.45           O  
ANISOU  873  O   HOH A 488     3604   4880   5365   -215    261    265       O  
HETATM  874  O   HOH A 489      39.046  11.886  37.750  1.00 27.96           O  
ANISOU  874  O   HOH A 489     2644   3427   4550    178    304   -175       O  
HETATM  875  O   HOH A 490      26.663   4.876  10.051  1.00 30.48           O  
ANISOU  875  O   HOH A 490     3178   4174   4226   -170    407   -240       O  
HETATM  876  O   HOH A 491      19.770  28.957  29.422  1.00 28.84           O  
ANISOU  876  O   HOH A 491     4010   2584   4362    -20    184   -196       O  
HETATM  877  O   HOH A 492      22.423   5.048  39.539  1.00 30.15           O  
ANISOU  877  O   HOH A 492     3645   3948   3862     16    326    313       O  
HETATM  878  O   HOH A 493      12.197   7.253   7.776  1.00 31.67           O  
ANISOU  878  O   HOH A 493     3707   4058   4269     -6    -19    135       O  
HETATM  879  O   HOH A 494      10.448  16.736  19.749  1.00 28.41           O  
ANISOU  879  O   HOH A 494     3442   3980   3372   -333    228     45       O  
HETATM  880  O   HOH A 495      31.858  14.978  44.277  1.00 32.59           O  
ANISOU  880  O   HOH A 495     4597   4761   3022    395   -180    207       O  
HETATM  881  O   HOH A 497      36.341  20.024  33.082  1.00 31.53           O  
ANISOU  881  O   HOH A 497     3826   5177   2975    194   -244    742       O  
HETATM  882  O   HOH A 498      25.768   1.558  28.292  1.00 31.37           O  
ANISOU  882  O   HOH A 498     2923   4462   4533   -193    359    222       O  
HETATM  883  O   HOH A 499       5.895  17.173  33.971  1.00 25.58           O  
ANISOU  883  O   HOH A 499     3421   2255   4042    -13    764   -320       O  
HETATM  884  O   HOH A 500      32.748  14.055  20.195  1.00 27.53           O  
ANISOU  884  O   HOH A 500     3191   3927   3339    270    360   -139       O  
HETATM  885  O   HOH A 501      39.611  22.654  20.914  1.00 28.05           O  
ANISOU  885  O   HOH A 501     3191   3772   3695   -391     11    566       O  
HETATM  886  O   HOH A 502      26.385  20.251   6.887  1.00 23.56           O  
ANISOU  886  O   HOH A 502     2648   3406   2898   -193    195   -138       O  
HETATM  887  O   HOH A 503      21.252  20.124  12.169  1.00 27.88           O  
ANISOU  887  O   HOH A 503     3919   3632   3040   -184    197    -52       O  
HETATM  888  O   HOH A 504      22.285   3.574  30.148  1.00 30.83           O  
ANISOU  888  O   HOH A 504     4924   3631   3158    539    269    657       O  
HETATM  889  O   HOH A 505      32.681  27.663  23.913  1.00 40.32           O  
ANISOU  889  O   HOH A 505     5440   4644   5236   -203    166    167       O  
HETATM  890  O   HOH A 506      27.510   1.919  37.441  1.00 38.12           O  
ANISOU  890  O   HOH A 506     5443   3983   5054    139   -647    424       O  
HETATM  891  O   HOH A 507      37.892  22.345  14.938  1.00 36.03           O  
ANISOU  891  O   HOH A 507     4460   4499   4732    214   -248    209       O  
HETATM  892  O   HOH A 508      26.541  18.610  44.038  1.00 26.43           O  
ANISOU  892  O   HOH A 508     3594   3918   2530    -11   -128   -186       O  
HETATM  893  O   HOH A 510      33.819  25.023  19.475  1.00 29.68           O  
ANISOU  893  O   HOH A 510     4017   3653   3605   -493    -29    410       O  
HETATM  894  O   HOH A 511      10.405  19.518  36.901  1.00 24.19           O  
ANISOU  894  O   HOH A 511     3278   2086   3827    -23    618    275       O  
HETATM  895  O   HOH A 513      38.761  21.900  26.489  1.00 29.59           O  
ANISOU  895  O   HOH A 513     3388   4027   3828    542   -351    299       O  
HETATM  896  O   HOH A 514      40.679  19.758  16.690  1.00 40.28           O  
ANISOU  896  O   HOH A 514     4999   4793   5513   -246   -585    147       O  
HETATM  897  O   HOH A 516      27.005  18.408  12.446  1.00 45.60           O  
ANISOU  897  O   HOH A 516     5508   5893   5923    105   -252     23       O  
HETATM  898  O   HOH A 517      28.664  24.035  17.927  1.00 52.01           O  
ANISOU  898  O   HOH A 517     6378   6208   7173      0     76     21       O  
HETATM  899  O   HOH A 518      37.116  22.824  17.671  1.00 37.37           O  
ANISOU  899  O   HOH A 518     4848   4756   4593    -95    234    291       O  
HETATM  900  O   HOH A 519       3.780  15.838  34.361  1.00 31.11           O  
ANISOU  900  O   HOH A 519     4526   3132   4159    163   -638     27       O  
HETATM  901  O   HOH A 520      10.036  20.560  23.810  1.00 31.92           O  
ANISOU  901  O   HOH A 520     3563   4805   3759   -251   -197   -107       O  
HETATM  902  O   HOH A 521       6.888  15.961  27.445  1.00 22.17           O  
ANISOU  902  O   HOH A 521     2431   2606   3386    555     28    -89       O  
HETATM  903  O   HOH A 522      24.252  20.669  46.049  1.00 26.52           O  
ANISOU  903  O   HOH A 522     3342   4169   2562   -262    551   1004       O  
HETATM  904  O   HOH A 524      24.795   3.430  26.508  1.00 35.19           O  
ANISOU  904  O   HOH A 524     4619   4665   4085      8    256    518       O  
HETATM  905  O   HOH A 525      31.398   4.763  38.605  1.00 32.22           O  
ANISOU  905  O   HOH A 525     4173   3450   4619    661   -702   -151       O  
HETATM  906  O   HOH A 528      22.521   1.766  22.291  1.00 31.84           O  
ANISOU  906  O   HOH A 528     4553   2839   4702    406    556    308       O  
HETATM  907  O   HOH A 529      29.404  21.353  14.717  1.00 32.87           O  
ANISOU  907  O   HOH A 529     4375   4800   3313     71   -609    500       O  
HETATM  908  O   HOH A 530      23.488  22.385  41.620  1.00 39.00           O  
ANISOU  908  O   HOH A 530     5674   4906   4237    127     46   -590       O  
HETATM  909  O   HOH A 531      31.044  12.265  24.549  1.00 37.68           O  
ANISOU  909  O   HOH A 531     4677   4990   4650    141     46   -232       O  
HETATM  910  O   HOH A 532      32.241   3.018  34.550  1.00 32.92           O  
ANISOU  910  O   HOH A 532     3734   3691   5082    338   -180   -245       O  
HETATM  911  O   HOH A 533      10.271  15.454  15.296  1.00 31.49           O  
ANISOU  911  O   HOH A 533     3726   3914   4325   -379   -863   -322       O  
HETATM  912  O   HOH A 534      28.308  14.008  45.989  1.00 48.76           O  
ANISOU  912  O   HOH A 534     6131   6214   6179    -69     48     98       O  
HETATM  913  O   HOH A 535      32.196  10.354  44.216  1.00 34.65           O  
ANISOU  913  O   HOH A 535     4507   4469   4188   -161      7    359       O  
HETATM  914  O   HOH A 536      28.665  13.163  48.622  1.00 40.01           O  
ANISOU  914  O   HOH A 536     5295   4456   5449   -172    102   -402       O  
HETATM  915  O   HOH A 537      32.433   7.656  44.196  1.00 34.97           O  
ANISOU  915  O   HOH A 537     4654   4626   4006   -162    351    541       O  
HETATM  916  O   HOH A 538      36.394  11.582  43.612  1.00 50.86           O  
ANISOU  916  O   HOH A 538     6548   6194   6582    138   -115     52       O  
HETATM  917  O   HOH A 539      33.624   9.043  20.486  1.00 32.38           O  
ANISOU  917  O   HOH A 539     4614   4585   3101   -218    216    -57       O  
HETATM  918  O   HOH A 540      15.675  12.209   0.841  1.00 30.14           O  
ANISOU  918  O   HOH A 540     4047   3152   4252   -404    -35    455       O  
CONECT  475  481                                                                
CONECT  479  780                                                                
CONECT  481  475  482                                                           
CONECT  482  481  483  485                                                      
CONECT  483  482  484  489                                                      
CONECT  484  483                                                                
CONECT  485  482  486                                                           
CONECT  486  485  487                                                           
CONECT  487  486  488                                                           
CONECT  488  487                                                                
CONECT  489  483                                                                
CONECT  495  780                                                                
CONECT  511  780                                                                
CONECT  519  528                                                                
CONECT  520  780                                                                
CONECT  528  519  529                                                           
CONECT  529  528  530  532                                                      
CONECT  530  529  531  536                                                      
CONECT  531  530                                                                
CONECT  532  529  533                                                           
CONECT  533  532  534                                                           
CONECT  534  533  535                                                           
CONECT  535  534                                                                
CONECT  536  530                                                                
CONECT  574  780                                                                
CONECT  575  780                                                                
CONECT  603  606                                                                
CONECT  606  603  607                                                           
CONECT  607  606  608  610                                                      
CONECT  608  607  609  614                                                      
CONECT  609  608                                                                
CONECT  610  607  611                                                           
CONECT  611  610  612                                                           
CONECT  612  611  613                                                           
CONECT  613  612                                                                
CONECT  614  608                                                                
CONECT  757  762                                                                
CONECT  762  757  763                                                           
CONECT  763  762  764  766                                                      
CONECT  764  763  765  770                                                      
CONECT  765  764                                                                
CONECT  766  763  767                                                           
CONECT  767  766  768                                                           
CONECT  768  767  769                                                           
CONECT  769  768                                                                
CONECT  770  764                                                                
CONECT  780  479  495  511  520                                                 
CONECT  780  574  575  788                                                      
CONECT  781  782  783  784  785                                                 
CONECT  782  781                                                                
CONECT  783  781                                                                
CONECT  784  781                                                                
CONECT  785  781                                                                
CONECT  788  780                                                                
MASTER      301    0    6    6    2    0    4    6  910    1   54   10          
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.