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***  PHOTORECEPTOR 26-JUL-97 1AP9  ***

elNémo ID: 22013107441098703

Job options:

ID        	=	 22013107441098703
JOBID     	=	 PHOTORECEPTOR 26-JUL-97 1AP9
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    PHOTORECEPTOR                           26-JUL-97   1AP9              
TITLE     X-RAY STRUCTURE OF BACTERIORHODOPSIN FROM MICROCRYSTALS GROWN IN      
TITLE    2 LIPIDIC CUBIC PHASES                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BACTERIORHODOPSIN;                                         
COMPND   3 CHAIN: A;                                                            
COMPND   4 OTHER_DETAILS: RETINAL LINKED TO LYS 216 VIA A SCHIFF BASE           
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HALOBACTERIUM SALINARUM;                        
SOURCE   3 ORGANISM_TAXID: 2242;                                                
SOURCE   4 STRAIN: S9;                                                          
SOURCE   5 CELLULAR_LOCATION: PLASMA MEMBRANE                                   
KEYWDS    PHOTORECEPTOR, PROTON PUMP, MEMBRANE PROTEIN, RETINAL PROTEIN,        
KEYWDS   2 MICROCRYSTALS, MICROFOCUS BEAM, LIPIDIC CUBIC PHASES                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.PEBAY-PEYROULA,G.RUMMEL,J.P.ROSENBUSCH,E.M.LANDAU                   
REVDAT   3   13-JUL-11 1AP9    1       VERSN                                    
REVDAT   2   24-FEB-09 1AP9    1       VERSN                                    
REVDAT   1   16-SEP-98 1AP9    0                                                
JRNL        AUTH   E.PEBAY-PEYROULA,G.RUMMEL,J.P.ROSENBUSCH,E.M.LANDAU          
JRNL        TITL   X-RAY STRUCTURE OF BACTERIORHODOPSIN AT 2.5 ANGSTROMS FROM   
JRNL        TITL 2 MICROCRYSTALS GROWN IN LIPIDIC CUBIC PHASES.                 
JRNL        REF    SCIENCE                       V. 277  1676 1997              
JRNL        REFN                   ISSN 0036-8075                               
JRNL        PMID   9287223                                                      
JRNL        DOI    10.1126/SCIENCE.277.5332.1676                                
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   E.M.LANDAU,G.RUMMEL,S.W.COWAN-JACOB,J.P.ROSENBUSCH           
REMARK   1  TITL   CRYSTALLISATION OF A POLAR PROTEIN AND SMALL MOLECULES FROM  
REMARK   1  TITL 2 THE AQUEOUS COMPARTMENT OF LIPIDIC CUBIC PHASES              
REMARK   1  REF    J.PHYS.CHEM.B                 V. 101  1935 1997              
REMARK   1  REFN                   ISSN 1089-5647                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.35 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.8                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.35                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 5.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.500                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 10000000.000                   
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0010                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 77.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 6564                           
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 SET) : 0.258                           
REMARK   3   FREE R VALUE                     : 0.317                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 300                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.35                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.48                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 67.00                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 957                          
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3947                       
REMARK   3   BIN FREE R VALUE                    : 0.3840                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.00                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 49                           
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1694                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 20                                      
REMARK   3   SOLVENT ATOMS            : 26                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 45.50                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 75.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.40                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.62                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.51                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.76                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.008                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.49                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 20.82                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.19                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PARHCSDX.PRO                                   
REMARK   3  PARAMETER FILE  2  : PARAM19.SOL                                    
REMARK   3  PARAMETER FILE  3  : RETINAL.PAR                                    
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO                                   
REMARK   3  TOPOLOGY FILE  2   : RETINAL.TOP                                    
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1AP9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : AUG-96                             
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID13                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.688                              
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : ELLIPSOIDAL MIRROR                 
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : CCP4                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 8045                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.350                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 10.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.2                               
REMARK 200  DATA REDUNDANCY                : 2.000                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.10000                            
REMARK 200   FOR THE DATA SET  : 4.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.56                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.60                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.26600                            
REMARK 200   FOR SHELL         : 2.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: X-PLOR 3.8                                            
REMARK 200 STARTING MODEL: PDB ENTRY 2BRD                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN FROM THE PURPLE MEMBRANE WAS     
REMARK 280  DELIPIDATED AND SOLUBILIZED IN OCTYL GLUCOSIDE. PROTEIN WAS         
REMARK 280  CRYSTALLIZED FROM 60 - 70% (W/W) MONOOLEIN, 0.7 - 4.0 M NA/K -      
REMARK 280  PHOSPHATE IN A PHOSPHATE BUFFER AT PH 5.6, AT 20C AND IN THE        
REMARK 280  DARK. THE MIXTURE WAS CENTRIFUGED AT 10000G FOR 150 MN PRIOR TO     
REMARK 280  CRYSTALLISATION.                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/2                                            
REMARK 290       6555   X-Y,X,Z+1/2                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       52.08000            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       52.08000            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       52.08000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 6840 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 29080 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -56.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -0.500000 -0.866025  0.000000       30.88000            
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000       53.48573            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3 -0.500000  0.866025  0.000000      -30.88000            
REMARK 350   BIOMT2   3 -0.866025 -0.500000  0.000000       53.48573            
REMARK 350   BIOMT3   3  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     GLN A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     GLN A     3                                                      
REMARK 465     ILE A     4                                                      
REMARK 465     THR A     5                                                      
REMARK 465     GLY A     6                                                      
REMARK 465     SER A   226                                                      
REMARK 465     ARG A   227                                                      
REMARK 465     ALA A   228                                                      
REMARK 465     ILE A   229                                                      
REMARK 465     PHE A   230                                                      
REMARK 465     GLY A   231                                                      
REMARK 465     GLU A   232                                                      
REMARK 465     ALA A   233                                                      
REMARK 465     GLU A   234                                                      
REMARK 465     ALA A   235                                                      
REMARK 465     PRO A   236                                                      
REMARK 465     GLU A   237                                                      
REMARK 465     PRO A   238                                                      
REMARK 465     SER A   239                                                      
REMARK 465     ALA A   240                                                      
REMARK 465     GLY A   241                                                      
REMARK 465     ASP A   242                                                      
REMARK 465     GLY A   243                                                      
REMARK 465     ALA A   244                                                      
REMARK 465     ALA A   245                                                      
REMARK 465     ALA A   246                                                      
REMARK 465     THR A   247                                                      
REMARK 465     SER A   248                                                      
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     ARG A   7    CD   NE   CZ   NH1  NH2                             
REMARK 470     ARG A 225    O                                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LEU A  22      -53.18   -166.65                                   
REMARK 500    VAL A  34       90.28    -68.18                                   
REMARK 500    THR A  47      -24.17   -164.30                                   
REMARK 500    LEU A  66      -62.51   -152.50                                   
REMARK 500    THR A  67      101.83    -12.77                                   
REMARK 500    MET A  68      170.56    -40.73                                   
REMARK 500    VAL A  69     -148.12   -120.70                                   
REMARK 500    PRO A  70       97.78    -56.67                                   
REMARK 500    PHE A  71      107.80     62.88                                   
REMARK 500    GLN A  75      -81.16   -154.79                                   
REMARK 500    ASN A  76       99.79    -37.94                                   
REMARK 500    THR A  89      -49.50   -147.88                                   
REMARK 500    THR A 128     -147.78     60.08                                   
REMARK 500    LYS A 129       38.26   -168.29                                   
REMARK 500    VAL A 130       90.09    -45.90                                   
REMARK 500    TYR A 131      -10.18     57.79                                   
REMARK 500    PHE A 153       35.21    -94.90                                   
REMARK 500    PHE A 154      -63.21   -144.46                                   
REMARK 500    SER A 158       22.13    -77.19                                   
REMARK 500    LYS A 159      -10.96   -151.23                                   
REMARK 500    GLU A 161      -75.83    174.52                                   
REMARK 500    MET A 163       -7.29     65.81                                   
REMARK 500    VAL A 167        3.08    -58.95                                   
REMARK 500    LEU A 190       26.47    -78.92                                   
REMARK 500    ALA A 196     -105.38    -73.29                                   
REMARK 500    ILE A 198      -62.86    -90.72                                   
REMARK 500    PRO A 200     -132.71    -42.49                                   
REMARK 500    LEU A 224      -34.95   -166.34                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 413        DISTANCE =  6.50 ANGSTROMS                       
REMARK 525    HOH A 415        DISTANCE =  7.02 ANGSTROMS                       
REMARK 525    HOH A 416        DISTANCE =  6.73 ANGSTROMS                       
REMARK 525    HOH A 418        DISTANCE =  5.99 ANGSTROMS                       
REMARK 525    HOH A 419        DISTANCE =  6.97 ANGSTROMS                       
REMARK 525    HOH A 423        DISTANCE =  5.24 ANGSTROMS                       
REMARK 525    HOH A 424        DISTANCE =  6.84 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: SFF                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: SCHIFF BASE                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RET A 300                 
DBREF  1AP9 A    1   248  UNP    P02945   BACR_HALN1      14    261             
SEQRES   1 A  248  GLN ALA GLN ILE THR GLY ARG PRO GLU TRP ILE TRP LEU          
SEQRES   2 A  248  ALA LEU GLY THR ALA LEU MET GLY LEU GLY THR LEU TYR          
SEQRES   3 A  248  PHE LEU VAL LYS GLY MET GLY VAL SER ASP PRO ASP ALA          
SEQRES   4 A  248  LYS LYS PHE TYR ALA ILE THR THR LEU VAL PRO ALA ILE          
SEQRES   5 A  248  ALA PHE THR MET TYR LEU SER MET LEU LEU GLY TYR GLY          
SEQRES   6 A  248  LEU THR MET VAL PRO PHE GLY GLY GLU GLN ASN PRO ILE          
SEQRES   7 A  248  TYR TRP ALA ARG TYR ALA ASP TRP LEU PHE THR THR PRO          
SEQRES   8 A  248  LEU LEU LEU LEU ASP LEU ALA LEU LEU VAL ASP ALA ASP          
SEQRES   9 A  248  GLN GLY THR ILE LEU ALA LEU VAL GLY ALA ASP GLY ILE          
SEQRES  10 A  248  MET ILE GLY THR GLY LEU VAL GLY ALA LEU THR LYS VAL          
SEQRES  11 A  248  TYR SER TYR ARG PHE VAL TRP TRP ALA ILE SER THR ALA          
SEQRES  12 A  248  ALA MET LEU TYR ILE LEU TYR VAL LEU PHE PHE GLY PHE          
SEQRES  13 A  248  THR SER LYS ALA GLU SER MET ARG PRO GLU VAL ALA SER          
SEQRES  14 A  248  THR PHE LYS VAL LEU ARG ASN VAL THR VAL VAL LEU TRP          
SEQRES  15 A  248  SER ALA TYR PRO VAL VAL TRP LEU ILE GLY SER GLU GLY          
SEQRES  16 A  248  ALA GLY ILE VAL PRO LEU ASN ILE GLU THR LEU LEU PHE          
SEQRES  17 A  248  MET VAL LEU ASP VAL SER ALA LYS VAL GLY PHE GLY LEU          
SEQRES  18 A  248  ILE LEU LEU ARG SER ARG ALA ILE PHE GLY GLU ALA GLU          
SEQRES  19 A  248  ALA PRO GLU PRO SER ALA GLY ASP GLY ALA ALA ALA THR          
SEQRES  20 A  248  SER                                                          
HET    RET  A 300      20                                                       
HETNAM     RET RETINAL                                                          
FORMUL   2  RET    C20 H28 O                                                    
FORMUL   3  HOH   *26(H2 O)                                                     
HELIX    1  A1 TRP A   10  MET A   20  1                                  11    
HELIX    2  A2 GLY A   23  LYS A   30  1                                   8    
HELIX    3   B PRO A   37  LEU A   61  1                                  25    
HELIX    4  C1 TYR A   83  TRP A   86  1                                   4    
HELIX    5  C2 THR A   90  LEU A   93  1                                   4    
HELIX    6   D GLN A  105  ALA A  126  1                                  22    
HELIX    7   E ARG A  134  LEU A  152  1                                  19    
HELIX    8  F1 GLU A  166  SER A  169  1                                   4    
HELIX    9  F2 LYS A  172  TRP A  189  1                                  18    
HELIX   10   G ASN A  202  GLY A  220  1                                  19    
LINK         C15 RET A 300                 NZ  LYS A 216     1555   1555  1.26  
SITE     1 SFF  1 LYS A 216                                                     
SITE     1 AC1 13 TYR A  83  TRP A  86  THR A  89  THR A  90                    
SITE     2 AC1 13 MET A 118  ILE A 119  TRP A 138  SER A 141                    
SITE     3 AC1 13 MET A 145  TRP A 182  TYR A 185  ASP A 212                    
SITE     4 AC1 13 LYS A 216                                                     
CRYST1   61.760   61.760  104.160  90.00  90.00 120.00 P 63          6          
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      0.016192  0.009348  0.000000        0.00000                         
SCALE2      0.000000  0.018697  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009601        0.00000                         
ATOM      1  N   ARG A   7      22.952  32.415 -14.492  1.00 72.70           N  
ATOM      2  CA  ARG A   7      23.932  31.313 -14.764  1.00 68.93           C  
ATOM      3  C   ARG A   7      25.129  31.383 -13.807  1.00 69.45           C  
ATOM      4  O   ARG A   7      25.442  30.404 -13.132  1.00 72.71           O  
ATOM      5  CB  ARG A   7      24.389  31.361 -16.231  1.00 68.24           C  
ATOM      6  CG  ARG A   7      25.282  30.222 -16.661  1.00 73.63           C  
ATOM      7  N   PRO A   8      25.800  32.549 -13.717  1.00 66.22           N  
ATOM      8  CA  PRO A   8      26.950  32.656 -12.808  1.00 63.70           C  
ATOM      9  C   PRO A   8      26.587  32.804 -11.314  1.00 60.10           C  
ATOM     10  O   PRO A   8      27.469  33.010 -10.465  1.00 50.90           O  
ATOM     11  CB  PRO A   8      27.685  33.897 -13.335  1.00 65.28           C  
ATOM     12  CG  PRO A   8      27.167  34.076 -14.755  1.00 67.43           C  
ATOM     13  CD  PRO A   8      25.723  33.736 -14.584  1.00 66.64           C  
ATOM     14  N   GLU A   9      25.294  32.709 -10.997  1.00 54.29           N  
ATOM     15  CA  GLU A   9      24.845  32.822  -9.611  1.00 52.37           C  
ATOM     16  C   GLU A   9      24.621  31.446  -8.992  1.00 48.99           C  
ATOM     17  O   GLU A   9      24.468  31.334  -7.768  1.00 49.05           O  
ATOM     18  CB  GLU A   9      23.544  33.624  -9.496  1.00 36.01           C  
ATOM     19  CG  GLU A   9      23.366  34.760 -10.485  1.00 48.55           C  
ATOM     20  CD  GLU A   9      22.273  34.476 -11.512  1.00 57.37           C  
ATOM     21  OE1 GLU A   9      21.533  33.483 -11.351  1.00 67.47           O  
ATOM     22  OE2 GLU A   9      22.149  35.240 -12.489  1.00 55.35           O  
ATOM     23  N   TRP A  10      24.617  30.409  -9.833  1.00 42.59           N  
ATOM     24  CA  TRP A  10      24.393  29.036  -9.382  1.00 43.30           C  
ATOM     25  C   TRP A  10      25.272  28.585  -8.216  1.00 44.25           C  
ATOM     26  O   TRP A  10      24.795  27.972  -7.254  1.00 36.16           O  
ATOM     27  CB  TRP A  10      24.541  28.055 -10.546  1.00 49.17           C  
ATOM     28  CG  TRP A  10      23.412  28.096 -11.511  1.00 58.88           C  
ATOM     29  CD1 TRP A  10      22.133  28.476 -11.249  1.00 60.11           C  
ATOM     30  CD2 TRP A  10      23.465  27.806 -12.916  1.00 70.07           C  
ATOM     31  NE1 TRP A  10      21.386  28.457 -12.402  1.00 69.83           N  
ATOM     32  CE2 TRP A  10      22.181  28.048 -13.441  1.00 66.38           C  
ATOM     33  CE3 TRP A  10      24.477  27.370 -13.784  1.00 78.48           C  
ATOM     34  CZ2 TRP A  10      21.877  27.871 -14.798  1.00 65.14           C  
ATOM     35  CZ3 TRP A  10      24.173  27.192 -15.140  1.00 66.13           C  
ATOM     36  CH2 TRP A  10      22.885  27.444 -15.628  1.00 58.83           C  
ATOM     37  N   ILE A  11      26.558  28.880  -8.299  1.00 38.57           N  
ATOM     38  CA  ILE A  11      27.453  28.478  -7.250  1.00 40.66           C  
ATOM     39  C   ILE A  11      27.079  29.192  -5.947  1.00 40.25           C  
ATOM     40  O   ILE A  11      27.049  28.549  -4.904  1.00 44.60           O  
ATOM     41  CB  ILE A  11      28.934  28.679  -7.676  1.00 46.56           C  
ATOM     42  CG1 ILE A  11      29.878  27.906  -6.741  1.00 55.46           C  
ATOM     43  CG2 ILE A  11      29.285  30.168  -7.757  1.00 52.72           C  
ATOM     44  CD1 ILE A  11      29.591  26.413  -6.635  1.00 56.92           C  
ATOM     45  N   TRP A  12      26.689  30.473  -6.026  1.00 41.80           N  
ATOM     46  CA  TRP A  12      26.296  31.266  -4.840  1.00 40.52           C  
ATOM     47  C   TRP A  12      24.928  30.802  -4.337  1.00 43.34           C  
ATOM     48  O   TRP A  12      24.633  30.855  -3.127  1.00 44.36           O  
ATOM     49  CB  TRP A  12      26.265  32.770  -5.154  1.00 47.52           C  
ATOM     50  CG  TRP A  12      27.556  33.319  -5.779  1.00 59.28           C  
ATOM     51  CD1 TRP A  12      27.657  34.182  -6.843  1.00 52.68           C  
ATOM     52  CD2 TRP A  12      28.907  33.002  -5.399  1.00 61.42           C  
ATOM     53  NE1 TRP A  12      28.975  34.407  -7.151  1.00 50.67           N  
ATOM     54  CE2 TRP A  12      29.762  33.696  -6.283  1.00 55.76           C  
ATOM     55  CE3 TRP A  12      29.474  32.193  -4.403  1.00 57.83           C  
ATOM     56  CZ2 TRP A  12      31.153  33.606  -6.197  1.00 55.65           C  
ATOM     57  CZ3 TRP A  12      30.857  32.105  -4.320  1.00 50.34           C  
ATOM     58  CH2 TRP A  12      31.679  32.808  -5.213  1.00 45.36           C  
ATOM     59  N   LEU A  13      24.098  30.335  -5.268  1.00 37.10           N  
ATOM     60  CA  LEU A  13      22.769  29.810  -4.928  1.00 43.86           C  
ATOM     61  C   LEU A  13      22.933  28.503  -4.130  1.00 32.35           C  
ATOM     62  O   LEU A  13      22.591  28.434  -2.952  1.00 38.30           O  
ATOM     63  CB  LEU A  13      21.955  29.521  -6.211  1.00 40.57           C  
ATOM     64  CG  LEU A  13      20.880  30.470  -6.765  1.00 34.36           C  
ATOM     65  CD1 LEU A  13      21.251  31.917  -6.583  1.00 27.61           C  
ATOM     66  CD2 LEU A  13      20.640  30.171  -8.224  1.00 24.51           C  
ATOM     67  N   ALA A  14      23.525  27.498  -4.774  1.00 42.92           N  
ATOM     68  CA  ALA A  14      23.743  26.184  -4.180  1.00 40.02           C  
ATOM     69  C   ALA A  14      24.627  26.169  -2.931  1.00 41.35           C  
ATOM     70  O   ALA A  14      24.415  25.352  -2.036  1.00 43.39           O  
ATOM     71  CB  ALA A  14      24.271  25.226  -5.224  1.00 48.63           C  
ATOM     72  N   LEU A  15      25.628  27.045  -2.885  1.00 40.58           N  
ATOM     73  CA  LEU A  15      26.522  27.155  -1.718  1.00 41.74           C  
ATOM     74  C   LEU A  15      25.734  27.824  -0.595  1.00 47.68           C  
ATOM     75  O   LEU A  15      25.954  27.556   0.584  1.00 43.74           O  
ATOM     76  CB  LEU A  15      27.730  28.025  -2.049  1.00 44.70           C  
ATOM     77  CG  LEU A  15      28.840  28.145  -1.018  1.00 60.24           C  
ATOM     78  CD1 LEU A  15      29.524  26.779  -0.777  1.00 45.71           C  
ATOM     79  CD2 LEU A  15      29.832  29.181  -1.531  1.00 63.06           C  
ATOM     80  N   GLY A  16      24.817  28.708  -0.988  1.00 51.34           N  
ATOM     81  CA  GLY A  16      23.980  29.397  -0.030  1.00 50.30           C  
ATOM     82  C   GLY A  16      23.063  28.400   0.647  1.00 43.74           C  
ATOM     83  O   GLY A  16      22.760  28.528   1.834  1.00 47.65           O  
ATOM     84  N   THR A  17      22.598  27.422  -0.130  1.00 41.05           N  
ATOM     85  CA  THR A  17      21.721  26.375   0.386  1.00 41.59           C  
ATOM     86  C   THR A  17      22.559  25.414   1.229  1.00 46.74           C  
ATOM     87  O   THR A  17      22.091  24.874   2.240  1.00 37.67           O  
ATOM     88  CB  THR A  17      21.038  25.609  -0.755  1.00 52.64           C  
ATOM     89  OG1 THR A  17      21.851  25.678  -1.926  1.00 53.76           O  
ATOM     90  CG2 THR A  17      19.682  26.200  -1.062  1.00 34.97           C  
ATOM     91  N   ALA A  18      23.815  25.249   0.822  1.00 49.81           N  
ATOM     92  CA  ALA A  18      24.755  24.393   1.532  1.00 58.61           C  
ATOM     93  C   ALA A  18      25.129  25.006   2.888  1.00 67.49           C  
ATOM     94  O   ALA A  18      25.248  24.281   3.880  1.00 73.26           O  
ATOM     95  CB  ALA A  18      26.006  24.157   0.685  1.00 57.40           C  
ATOM     96  N   LEU A  19      25.296  26.332   2.939  1.00 62.32           N  
ATOM     97  CA  LEU A  19      25.645  27.007   4.201  1.00 64.91           C  
ATOM     98  C   LEU A  19      24.476  27.117   5.189  1.00 62.48           C  
ATOM     99  O   LEU A  19      24.679  27.397   6.374  1.00 62.93           O  
ATOM    100  CB  LEU A  19      26.294  28.381   3.961  1.00 58.25           C  
ATOM    101  CG  LEU A  19      27.678  28.333   3.297  1.00 44.33           C  
ATOM    102  CD1 LEU A  19      28.347  29.692   3.384  1.00 47.46           C  
ATOM    103  CD2 LEU A  19      28.537  27.277   3.958  1.00 40.55           C  
ATOM    104  N   MET A  20      23.259  26.917   4.682  1.00 61.06           N  
ATOM    105  CA  MET A  20      22.048  26.931   5.501  1.00 59.01           C  
ATOM    106  C   MET A  20      21.726  25.455   5.751  1.00 60.84           C  
ATOM    107  O   MET A  20      21.145  25.090   6.777  1.00 60.78           O  
ATOM    108  CB  MET A  20      20.896  27.606   4.758  1.00 53.88           C  
ATOM    109  CG  MET A  20      21.212  28.995   4.224  1.00 52.78           C  
ATOM    110  SD  MET A  20      21.652  30.243   5.467  1.00 79.68           S  
ATOM    111  CE  MET A  20      20.047  30.601   6.189  1.00 60.56           C  
ATOM    112  N   GLY A  21      22.086  24.620   4.775  1.00 62.14           N  
ATOM    113  CA  GLY A  21      21.905  23.183   4.894  1.00 58.21           C  
ATOM    114  C   GLY A  21      23.128  22.701   5.655  1.00 53.27           C  
ATOM    115  O   GLY A  21      24.017  22.029   5.112  1.00 44.24           O  
ATOM    116  N   LEU A  22      23.187  23.133   6.910  1.00 47.27           N  
ATOM    117  CA  LEU A  22      24.273  22.834   7.829  1.00 48.13           C  
ATOM    118  C   LEU A  22      23.758  23.236   9.204  1.00 50.17           C  
ATOM    119  O   LEU A  22      23.768  22.440  10.142  1.00 55.17           O  
ATOM    120  CB  LEU A  22      25.497  23.685   7.486  1.00 45.56           C  
ATOM    121  CG  LEU A  22      26.683  23.593   8.447  1.00 61.21           C  
ATOM    122  CD1 LEU A  22      27.639  22.478   8.001  1.00 60.51           C  
ATOM    123  CD2 LEU A  22      27.414  24.927   8.490  1.00 60.25           C  
ATOM    124  N   GLY A  23      23.291  24.480   9.301  1.00 50.91           N  
ATOM    125  CA  GLY A  23      22.762  24.994  10.553  1.00 51.71           C  
ATOM    126  C   GLY A  23      21.447  24.330  10.909  1.00 53.66           C  
ATOM    127  O   GLY A  23      21.224  23.959  12.062  1.00 50.43           O  
ATOM    128  N   THR A  24      20.575  24.176   9.915  1.00 57.55           N  
ATOM    129  CA  THR A  24      19.287  23.534  10.132  1.00 61.98           C  
ATOM    130  C   THR A  24      19.587  22.141  10.665  1.00 66.43           C  
ATOM    131  O   THR A  24      18.842  21.617  11.482  1.00 68.24           O  
ATOM    132  CB  THR A  24      18.463  23.432   8.826  1.00 60.41           C  
ATOM    133  OG1 THR A  24      18.343  24.731   8.231  1.00 61.40           O  
ATOM    134  CG2 THR A  24      17.059  22.904   9.112  1.00 58.27           C  
ATOM    135  N   LEU A  25      20.723  21.581  10.246  1.00 74.96           N  
ATOM    136  CA  LEU A  25      21.163  20.254  10.681  1.00 75.99           C  
ATOM    137  C   LEU A  25      21.829  20.293  12.057  1.00 78.20           C  
ATOM    138  O   LEU A  25      21.512  19.479  12.926  1.00 79.09           O  
ATOM    139  CB  LEU A  25      22.111  19.639   9.651  1.00 66.49           C  
ATOM    140  CG  LEU A  25      21.443  19.339   8.308  1.00 61.01           C  
ATOM    141  CD1 LEU A  25      22.462  18.825   7.299  1.00 50.67           C  
ATOM    142  CD2 LEU A  25      20.311  18.341   8.521  1.00 43.06           C  
ATOM    143  N   TYR A  26      22.748  21.237  12.252  1.00 79.95           N  
ATOM    144  CA  TYR A  26      23.443  21.386  13.529  1.00 81.64           C  
ATOM    145  C   TYR A  26      22.480  21.811  14.636  1.00 83.96           C  
ATOM    146  O   TYR A  26      22.291  21.086  15.617  1.00 85.28           O  
ATOM    147  CB  TYR A  26      24.572  22.416  13.410  1.00 85.87           C  
ATOM    148  CG  TYR A  26      25.947  21.818  13.203  1.00 94.83           C  
ATOM    149  CD1 TYR A  26      26.660  21.280  14.275  1.00 98.47           C  
ATOM    150  CD2 TYR A  26      26.548  21.805  11.940  1.00 98.66           C  
ATOM    151  CE1 TYR A  26      27.940  20.746  14.099  1.00102.56           C  
ATOM    152  CE2 TYR A  26      27.830  21.271  11.753  1.00 99.80           C  
ATOM    153  CZ  TYR A  26      28.518  20.745  12.839  1.00104.57           C  
ATOM    154  OH  TYR A  26      29.783  20.229  12.677  1.00101.42           O  
ATOM    155  N   PHE A  27      21.844  22.967  14.445  1.00 81.17           N  
ATOM    156  CA  PHE A  27      20.903  23.533  15.412  1.00 79.36           C  
ATOM    157  C   PHE A  27      19.695  22.663  15.750  1.00 83.25           C  
ATOM    158  O   PHE A  27      19.054  22.873  16.782  1.00 85.20           O  
ATOM    159  CB  PHE A  27      20.437  24.923  14.960  1.00 79.20           C  
ATOM    160  CG  PHE A  27      21.508  25.981  15.041  1.00 82.94           C  
ATOM    161  CD1 PHE A  27      22.095  26.306  16.264  1.00 82.61           C  
ATOM    162  CD2 PHE A  27      21.932  26.653  13.899  1.00 80.19           C  
ATOM    163  CE1 PHE A  27      23.088  27.283  16.342  1.00 80.32           C  
ATOM    164  CE2 PHE A  27      22.921  27.626  13.969  1.00 77.35           C  
ATOM    165  CZ  PHE A  27      23.500  27.942  15.190  1.00 77.80           C  
ATOM    166  N   LEU A  28      19.369  21.704  14.883  1.00 83.75           N  
ATOM    167  CA  LEU A  28      18.238  20.814  15.136  1.00 84.34           C  
ATOM    168  C   LEU A  28      18.579  19.747  16.173  1.00 85.94           C  
ATOM    169  O   LEU A  28      17.696  19.244  16.867  1.00 85.48           O  
ATOM    170  CB  LEU A  28      17.767  20.140  13.849  1.00 84.21           C  
ATOM    171  CG  LEU A  28      16.611  20.784  13.077  1.00 87.39           C  
ATOM    172  CD1 LEU A  28      16.322  19.965  11.830  1.00 91.43           C  
ATOM    173  CD2 LEU A  28      15.365  20.862  13.941  1.00 93.28           C  
ATOM    174  N   VAL A  29      19.863  19.414  16.278  1.00 89.77           N  
ATOM    175  CA  VAL A  29      20.327  18.403  17.221  1.00 93.79           C  
ATOM    176  C   VAL A  29      20.282  18.906  18.660  1.00 96.39           C  
ATOM    177  O   VAL A  29      19.889  18.168  19.571  1.00 96.81           O  
ATOM    178  CB  VAL A  29      21.766  17.940  16.890  1.00 95.43           C  
ATOM    179  CG1 VAL A  29      22.217  16.864  17.868  1.00 97.57           C  
ATOM    180  CG2 VAL A  29      21.835  17.411  15.465  1.00 98.66           C  
ATOM    181  N   LYS A  30      20.678  20.160  18.861  1.00 99.18           N  
ATOM    182  CA  LYS A  30      20.690  20.750  20.198  1.00103.00           C  
ATOM    183  C   LYS A  30      19.290  21.140  20.657  1.00102.77           C  
ATOM    184  O   LYS A  30      18.999  21.150  21.853  1.00 98.96           O  
ATOM    185  CB  LYS A  30      21.598  21.977  20.240  1.00105.71           C  
ATOM    186  CG  LYS A  30      21.894  22.449  21.650  1.00114.63           C  
ATOM    187  CD  LYS A  30      22.119  23.944  21.689  1.00123.52           C  
ATOM    188  CE  LYS A  30      22.506  24.411  23.083  1.00130.58           C  
ATOM    189  NZ  LYS A  30      22.733  25.887  23.139  1.00132.42           N  
ATOM    190  N   GLY A  31      18.432  21.472  19.698  1.00106.81           N  
ATOM    191  CA  GLY A  31      17.069  21.854  20.018  1.00114.62           C  
ATOM    192  C   GLY A  31      16.266  20.718  20.628  1.00118.92           C  
ATOM    193  O   GLY A  31      16.740  19.580  20.710  1.00121.38           O  
ATOM    194  N   MET A  32      15.045  21.035  21.054  1.00121.78           N  
ATOM    195  CA  MET A  32      14.128  20.071  21.666  1.00126.31           C  
ATOM    196  C   MET A  32      14.606  19.558  23.030  1.00127.19           C  
ATOM    197  O   MET A  32      14.043  18.602  23.573  1.00127.21           O  
ATOM    198  CB  MET A  32      13.859  18.894  20.718  1.00133.84           C  
ATOM    199  CG  MET A  32      13.706  19.273  19.244  1.00142.27           C  
ATOM    200  SD  MET A  32      12.719  20.759  18.974  1.00150.85           S  
ATOM    201  CE  MET A  32      11.061  20.076  19.057  1.00151.06           C  
ATOM    202  N   GLY A  33      15.649  20.189  23.572  1.00126.86           N  
ATOM    203  CA  GLY A  33      16.178  19.802  24.871  1.00123.65           C  
ATOM    204  C   GLY A  33      15.500  20.604  25.967  1.00122.48           C  
ATOM    205  O   GLY A  33      15.925  21.713  26.283  1.00122.40           O  
ATOM    206  N   VAL A  34      14.442  20.036  26.542  1.00120.74           N  
ATOM    207  CA  VAL A  34      13.665  20.695  27.590  1.00117.79           C  
ATOM    208  C   VAL A  34      14.374  20.888  28.928  1.00115.64           C  
ATOM    209  O   VAL A  34      14.321  20.027  29.807  1.00115.03           O  
ATOM    210  CB  VAL A  34      12.299  19.983  27.825  1.00120.59           C  
ATOM    211  CG1 VAL A  34      11.374  20.208  26.642  1.00118.87           C  
ATOM    212  CG2 VAL A  34      12.498  18.488  28.054  1.00122.91           C  
ATOM    213  N   SER A  35      15.043  22.030  29.065  1.00114.70           N  
ATOM    214  CA  SER A  35      15.750  22.391  30.295  1.00112.41           C  
ATOM    215  C   SER A  35      15.011  23.573  30.903  1.00112.12           C  
ATOM    216  O   SER A  35      14.763  23.621  32.108  1.00112.86           O  
ATOM    217  CB  SER A  35      17.195  22.795  29.999  1.00111.18           C  
ATOM    218  OG  SER A  35      17.808  23.349  31.151  1.00104.97           O  
ATOM    219  N   ASP A  36      14.684  24.534  30.047  1.00110.93           N  
ATOM    220  CA  ASP A  36      13.957  25.727  30.447  1.00111.67           C  
ATOM    221  C   ASP A  36      12.881  25.973  29.394  1.00109.00           C  
ATOM    222  O   ASP A  36      13.125  25.800  28.193  1.00108.17           O  
ATOM    223  CB  ASP A  36      14.896  26.937  30.525  1.00118.28           C  
ATOM    224  CG  ASP A  36      15.995  26.764  31.556  1.00123.16           C  
ATOM    225  OD1 ASP A  36      15.675  26.606  32.754  1.00124.28           O  
ATOM    226  OD2 ASP A  36      17.181  26.795  31.166  1.00126.63           O  
ATOM    227  N   PRO A  37      11.666  26.342  29.832  1.00104.03           N  
ATOM    228  CA  PRO A  37      10.543  26.612  28.928  1.00100.64           C  
ATOM    229  C   PRO A  37      10.833  27.832  28.059  1.00 97.28           C  
ATOM    230  O   PRO A  37      10.341  27.940  26.937  1.00 99.27           O  
ATOM    231  CB  PRO A  37       9.386  26.881  29.893  1.00102.68           C  
ATOM    232  CG  PRO A  37       9.771  26.109  31.124  1.00103.64           C  
ATOM    233  CD  PRO A  37      11.234  26.436  31.236  1.00104.54           C  
ATOM    234  N   ASP A  38      11.640  28.743  28.595  1.00 91.10           N  
ATOM    235  CA  ASP A  38      12.022  29.962  27.892  1.00 86.49           C  
ATOM    236  C   ASP A  38      13.099  29.692  26.846  1.00 82.01           C  
ATOM    237  O   ASP A  38      13.118  30.318  25.788  1.00 82.19           O  
ATOM    238  CB  ASP A  38      12.519  31.004  28.891  1.00 86.43           C  
ATOM    239  CG  ASP A  38      11.447  31.423  29.883  1.00 83.80           C  
ATOM    240  OD1 ASP A  38      10.298  30.931  29.790  1.00 67.51           O  
ATOM    241  OD2 ASP A  38      11.763  32.257  30.760  1.00 90.62           O  
ATOM    242  N   ALA A  39      13.994  28.759  27.156  1.00 76.39           N  
ATOM    243  CA  ALA A  39      15.071  28.389  26.250  1.00 68.72           C  
ATOM    244  C   ALA A  39      14.498  27.672  25.032  1.00 64.59           C  
ATOM    245  O   ALA A  39      15.064  27.756  23.936  1.00 57.32           O  
ATOM    246  CB  ALA A  39      16.079  27.501  26.970  1.00 70.96           C  
ATOM    247  N   LYS A  40      13.369  26.985  25.237  1.00 62.24           N  
ATOM    248  CA  LYS A  40      12.667  26.243  24.179  1.00 63.49           C  
ATOM    249  C   LYS A  40      12.175  27.127  23.031  1.00 58.46           C  
ATOM    250  O   LYS A  40      12.380  26.796  21.855  1.00 50.37           O  
ATOM    251  CB  LYS A  40      11.492  25.450  24.765  1.00 70.48           C  
ATOM    252  CG  LYS A  40      11.881  24.102  25.364  1.00 81.07           C  
ATOM    253  CD  LYS A  40      11.646  22.939  24.389  1.00 88.08           C  
ATOM    254  CE  LYS A  40      12.503  23.026  23.126  1.00 90.93           C  
ATOM    255  NZ  LYS A  40      13.970  22.968  23.405  1.00 92.17           N  
ATOM    256  N   LYS A  41      11.507  28.230  23.378  1.00 55.27           N  
ATOM    257  CA  LYS A  41      11.015  29.182  22.386  1.00 51.49           C  
ATOM    258  C   LYS A  41      12.191  29.873  21.692  1.00 47.35           C  
ATOM    259  O   LYS A  41      12.167  30.084  20.485  1.00 42.02           O  
ATOM    260  CB  LYS A  41      10.066  30.216  23.012  1.00 54.48           C  
ATOM    261  CG  LYS A  41      10.616  31.013  24.187  1.00 55.98           C  
ATOM    262  CD  LYS A  41       9.768  32.277  24.479  1.00 49.62           C  
ATOM    263  CE  LYS A  41       8.328  31.963  24.834  1.00 36.28           C  
ATOM    264  NZ  LYS A  41       8.212  31.105  26.050  1.00 36.62           N  
ATOM    265  N   PHE A  42      13.230  30.197  22.454  1.00 51.35           N  
ATOM    266  CA  PHE A  42      14.425  30.829  21.891  1.00 58.68           C  
ATOM    267  C   PHE A  42      15.081  29.918  20.844  1.00 63.26           C  
ATOM    268  O   PHE A  42      15.438  30.386  19.758  1.00 67.36           O  
ATOM    269  CB  PHE A  42      15.429  31.186  22.997  1.00 62.27           C  
ATOM    270  CG  PHE A  42      15.106  32.470  23.724  1.00 66.71           C  
ATOM    271  CD1 PHE A  42      15.291  33.701  23.103  1.00 68.71           C  
ATOM    272  CD2 PHE A  42      14.619  32.452  25.022  1.00 72.12           C  
ATOM    273  CE1 PHE A  42      14.998  34.899  23.757  1.00 69.35           C  
ATOM    274  CE2 PHE A  42      14.319  33.644  25.691  1.00 80.93           C  
ATOM    275  CZ  PHE A  42      14.511  34.873  25.052  1.00 77.21           C  
ATOM    276  N   TYR A  43      15.215  28.625  21.159  1.00 70.42           N  
ATOM    277  CA  TYR A  43      15.805  27.657  20.223  1.00 73.24           C  
ATOM    278  C   TYR A  43      14.929  27.472  18.986  1.00 71.29           C  
ATOM    279  O   TYR A  43      15.397  27.679  17.858  1.00 69.02           O  
ATOM    280  CB  TYR A  43      16.024  26.284  20.881  1.00 73.64           C  
ATOM    281  CG  TYR A  43      17.197  26.224  21.837  1.00 83.33           C  
ATOM    282  CD1 TYR A  43      18.497  26.512  21.405  1.00 90.51           C  
ATOM    283  CD2 TYR A  43      17.009  25.913  23.185  1.00 87.24           C  
ATOM    284  CE1 TYR A  43      19.579  26.498  22.300  1.00 87.42           C  
ATOM    285  CE2 TYR A  43      18.084  25.898  24.087  1.00 89.21           C  
ATOM    286  CZ  TYR A  43      19.359  26.194  23.636  1.00 85.69           C  
ATOM    287  OH  TYR A  43      20.400  26.216  24.527  1.00 80.85           O  
ATOM    288  N   ALA A  44      13.660  27.114  19.211  1.00 66.50           N  
ATOM    289  CA  ALA A  44      12.680  26.863  18.146  1.00 56.63           C  
ATOM    290  C   ALA A  44      12.892  27.730  16.927  1.00 62.34           C  
ATOM    291  O   ALA A  44      13.171  27.228  15.840  1.00 57.61           O  
ATOM    292  CB  ALA A  44      11.267  27.055  18.669  1.00 42.64           C  
ATOM    293  N   ILE A  45      12.814  29.040  17.146  1.00 67.45           N  
ATOM    294  CA  ILE A  45      12.974  30.041  16.098  1.00 75.50           C  
ATOM    295  C   ILE A  45      14.315  30.002  15.384  1.00 71.20           C  
ATOM    296  O   ILE A  45      14.348  29.997  14.153  1.00 62.91           O  
ATOM    297  CB  ILE A  45      12.704  31.470  16.646  1.00 78.52           C  
ATOM    298  CG1 ILE A  45      11.194  31.687  16.795  1.00 82.46           C  
ATOM    299  CG2 ILE A  45      13.334  32.538  15.747  1.00 73.25           C  
ATOM    300  CD1 ILE A  45      10.812  33.042  17.375  1.00 88.02           C  
ATOM    301  N   THR A  46      15.411  29.964  16.139  1.00 69.86           N  
ATOM    302  CA  THR A  46      16.734  29.940  15.520  1.00 72.32           C  
ATOM    303  C   THR A  46      17.143  28.542  15.031  1.00 69.78           C  
ATOM    304  O   THR A  46      18.224  28.029  15.345  1.00 69.95           O  
ATOM    305  CB  THR A  46      17.809  30.569  16.433  1.00 67.84           C  
ATOM    306  OG1 THR A  46      17.245  31.689  17.120  1.00 68.04           O  
ATOM    307  CG2 THR A  46      18.957  31.083  15.602  1.00 61.90           C  
ATOM    308  N   THR A  47      16.249  27.961  14.235  1.00 64.40           N  
ATOM    309  CA  THR A  47      16.397  26.646  13.614  1.00 60.31           C  
ATOM    310  C   THR A  47      15.331  26.611  12.511  1.00 62.14           C  
ATOM    311  O   THR A  47      15.455  25.891  11.517  1.00 62.33           O  
ATOM    312  CB  THR A  47      16.183  25.496  14.641  1.00 58.62           C  
ATOM    313  OG1 THR A  47      17.301  25.443  15.535  1.00 68.83           O  
ATOM    314  CG2 THR A  47      16.071  24.165  13.953  1.00 55.57           C  
ATOM    315  N   LEU A  48      14.295  27.426  12.697  1.00 59.85           N  
ATOM    316  CA  LEU A  48      13.204  27.559  11.741  1.00 49.08           C  
ATOM    317  C   LEU A  48      13.579  28.636  10.714  1.00 51.43           C  
ATOM    318  O   LEU A  48      13.188  28.562   9.545  1.00 60.02           O  
ATOM    319  CB  LEU A  48      11.922  27.958  12.468  1.00 42.16           C  
ATOM    320  CG  LEU A  48      10.917  26.862  12.830  1.00 44.34           C  
ATOM    321  CD1 LEU A  48      11.583  25.696  13.526  1.00 53.77           C  
ATOM    322  CD2 LEU A  48       9.825  27.440  13.709  1.00 48.41           C  
ATOM    323  N   VAL A  49      14.342  29.631  11.168  1.00 46.20           N  
ATOM    324  CA  VAL A  49      14.809  30.743  10.340  1.00 41.24           C  
ATOM    325  C   VAL A  49      15.746  30.287   9.213  1.00 45.73           C  
ATOM    326  O   VAL A  49      15.498  30.593   8.046  1.00 49.32           O  
ATOM    327  CB  VAL A  49      15.471  31.848  11.228  1.00 47.64           C  
ATOM    328  CG1 VAL A  49      16.537  32.621  10.470  1.00 39.56           C  
ATOM    329  CG2 VAL A  49      14.396  32.806  11.740  1.00 42.93           C  
ATOM    330  N   PRO A  50      16.824  29.545   9.534  1.00 37.40           N  
ATOM    331  CA  PRO A  50      17.701  29.120   8.436  1.00 33.70           C  
ATOM    332  C   PRO A  50      17.070  28.002   7.628  1.00 45.80           C  
ATOM    333  O   PRO A  50      17.554  27.650   6.551  1.00 47.92           O  
ATOM    334  CB  PRO A  50      18.961  28.652   9.159  1.00 39.81           C  
ATOM    335  CG  PRO A  50      18.435  28.126  10.474  1.00 34.89           C  
ATOM    336  CD  PRO A  50      17.382  29.157  10.846  1.00 40.60           C  
ATOM    337  N   ALA A  51      15.978  27.461   8.160  1.00 49.25           N  
ATOM    338  CA  ALA A  51      15.235  26.388   7.517  1.00 45.94           C  
ATOM    339  C   ALA A  51      14.279  26.930   6.451  1.00 46.61           C  
ATOM    340  O   ALA A  51      14.087  26.296   5.408  1.00 38.18           O  
ATOM    341  CB  ALA A  51      14.477  25.597   8.557  1.00 54.03           C  
ATOM    342  N   ILE A  52      13.690  28.098   6.710  1.00 44.93           N  
ATOM    343  CA  ILE A  52      12.786  28.721   5.744  1.00 45.51           C  
ATOM    344  C   ILE A  52      13.616  29.299   4.590  1.00 40.98           C  
ATOM    345  O   ILE A  52      13.277  29.125   3.418  1.00 46.17           O  
ATOM    346  CB  ILE A  52      11.898  29.834   6.389  1.00 52.92           C  
ATOM    347  CG1 ILE A  52      11.043  29.253   7.532  1.00 38.34           C  
ATOM    348  CG2 ILE A  52      10.972  30.445   5.327  1.00 48.51           C  
ATOM    349  CD1 ILE A  52      10.477  30.273   8.484  1.00 22.58           C  
ATOM    350  N   ALA A  53      14.719  29.959   4.911  1.00 35.46           N  
ATOM    351  CA  ALA A  53      15.587  30.510   3.860  1.00 46.97           C  
ATOM    352  C   ALA A  53      16.234  29.383   3.025  1.00 46.42           C  
ATOM    353  O   ALA A  53      16.411  29.529   1.819  1.00 43.00           O  
ATOM    354  CB  ALA A  53      16.660  31.435   4.464  1.00 45.89           C  
ATOM    355  N   PHE A  54      16.568  28.264   3.670  1.00 44.90           N  
ATOM    356  CA  PHE A  54      17.157  27.112   2.984  1.00 50.81           C  
ATOM    357  C   PHE A  54      16.247  26.644   1.842  1.00 54.29           C  
ATOM    358  O   PHE A  54      16.715  26.342   0.741  1.00 49.44           O  
ATOM    359  CB  PHE A  54      17.366  25.951   3.965  1.00 43.09           C  
ATOM    360  CG  PHE A  54      17.699  24.636   3.296  1.00 52.63           C  
ATOM    361  CD1 PHE A  54      16.683  23.786   2.845  1.00 50.95           C  
ATOM    362  CD2 PHE A  54      19.028  24.242   3.120  1.00 55.53           C  
ATOM    363  CE1 PHE A  54      16.985  22.570   2.231  1.00 51.61           C  
ATOM    364  CE2 PHE A  54      19.342  23.022   2.507  1.00 46.71           C  
ATOM    365  CZ  PHE A  54      18.320  22.186   2.061  1.00 52.54           C  
ATOM    366  N   THR A  55      14.951  26.541   2.133  1.00 50.46           N  
ATOM    367  CA  THR A  55      13.977  26.106   1.142  1.00 51.94           C  
ATOM    368  C   THR A  55      13.931  27.122   0.024  1.00 52.40           C  
ATOM    369  O   THR A  55      13.943  26.761  -1.149  1.00 58.15           O  
ATOM    370  CB  THR A  55      12.559  25.979   1.745  1.00 55.17           C  
ATOM    371  OG1 THR A  55      12.070  27.272   2.116  1.00 51.91           O  
ATOM    372  CG2 THR A  55      12.573  25.076   2.974  1.00 59.98           C  
ATOM    373  N   MET A  56      13.925  28.397   0.418  1.00 60.83           N  
ATOM    374  CA  MET A  56      13.866  29.535  -0.507  1.00 50.72           C  
ATOM    375  C   MET A  56      15.064  29.624  -1.439  1.00 41.10           C  
ATOM    376  O   MET A  56      14.892  29.901  -2.621  1.00 28.66           O  
ATOM    377  CB  MET A  56      13.709  30.848   0.260  1.00 49.72           C  
ATOM    378  CG  MET A  56      12.586  31.695  -0.267  1.00 50.83           C  
ATOM    379  SD  MET A  56      10.967  30.939   0.008  1.00 53.91           S  
ATOM    380  CE  MET A  56      10.384  30.620  -1.687  1.00 18.76           C  
ATOM    381  N   TYR A  57      16.267  29.399  -0.902  1.00 47.39           N  
ATOM    382  CA  TYR A  57      17.491  29.419  -1.706  1.00 56.20           C  
ATOM    383  C   TYR A  57      17.429  28.263  -2.708  1.00 53.96           C  
ATOM    384  O   TYR A  57      17.843  28.402  -3.867  1.00 50.79           O  
ATOM    385  CB  TYR A  57      18.732  29.264  -0.832  1.00 56.17           C  
ATOM    386  CG  TYR A  57      18.901  30.325   0.224  1.00 59.75           C  
ATOM    387  CD1 TYR A  57      18.778  31.673  -0.086  1.00 71.67           C  
ATOM    388  CD2 TYR A  57      19.192  29.979   1.541  1.00 68.17           C  
ATOM    389  CE1 TYR A  57      18.938  32.654   0.884  1.00 76.07           C  
ATOM    390  CE2 TYR A  57      19.350  30.952   2.518  1.00 75.38           C  
ATOM    391  CZ  TYR A  57      19.221  32.283   2.180  1.00 79.06           C  
ATOM    392  OH  TYR A  57      19.364  33.247   3.141  1.00 92.97           O  
ATOM    393  N   LEU A  58      16.909  27.122  -2.252  1.00 50.29           N  
ATOM    394  CA  LEU A  58      16.753  25.951  -3.111  1.00 45.43           C  
ATOM    395  C   LEU A  58      15.683  26.276  -4.150  1.00 44.47           C  
ATOM    396  O   LEU A  58      15.540  25.559  -5.136  1.00 45.54           O  
ATOM    397  CB  LEU A  58      16.343  24.719  -2.295  1.00 47.96           C  
ATOM    398  CG  LEU A  58      17.311  23.528  -2.158  1.00 42.10           C  
ATOM    399  CD1 LEU A  58      16.773  22.531  -1.137  1.00 41.17           C  
ATOM    400  CD2 LEU A  58      17.523  22.830  -3.483  1.00 26.73           C  
ATOM    401  N   SER A  59      14.927  27.348  -3.901  1.00 37.76           N  
ATOM    402  CA  SER A  59      13.883  27.815  -4.810  1.00 45.58           C  
ATOM    403  C   SER A  59      14.569  28.569  -5.942  1.00 47.28           C  
ATOM    404  O   SER A  59      14.311  28.319  -7.120  1.00 49.82           O  
ATOM    405  CB  SER A  59      12.908  28.734  -4.073  1.00 56.44           C  
ATOM    406  OG  SER A  59      12.048  29.418  -4.960  1.00 50.18           O  
ATOM    407  N   MET A  60      15.455  29.489  -5.576  1.00 46.82           N  
ATOM    408  CA  MET A  60      16.223  30.255  -6.558  1.00 48.96           C  
ATOM    409  C   MET A  60      17.136  29.333  -7.385  1.00 47.51           C  
ATOM    410  O   MET A  60      17.385  29.589  -8.568  1.00 49.06           O  
ATOM    411  CB  MET A  60      17.069  31.308  -5.842  1.00 44.31           C  
ATOM    412  CG  MET A  60      16.238  32.294  -5.054  1.00 45.66           C  
ATOM    413  SD  MET A  60      17.232  33.539  -4.249  1.00 45.12           S  
ATOM    414  CE  MET A  60      17.397  32.775  -2.659  1.00 47.85           C  
ATOM    415  N   LEU A  61      17.626  28.266  -6.749  1.00 54.20           N  
ATOM    416  CA  LEU A  61      18.509  27.296  -7.396  1.00 53.87           C  
ATOM    417  C   LEU A  61      17.732  26.512  -8.460  1.00 57.41           C  
ATOM    418  O   LEU A  61      18.187  26.325  -9.598  1.00 55.39           O  
ATOM    419  CB  LEU A  61      19.067  26.316  -6.352  1.00 49.29           C  
ATOM    420  CG  LEU A  61      20.321  25.453  -6.600  1.00 43.80           C  
ATOM    421  CD1 LEU A  61      20.309  24.272  -5.623  1.00 31.02           C  
ATOM    422  CD2 LEU A  61      20.391  24.925  -8.018  1.00 21.32           C  
ATOM    423  N   LEU A  62      16.552  26.052  -8.083  1.00 57.98           N  
ATOM    424  CA  LEU A  62      15.749  25.280  -9.001  1.00 68.53           C  
ATOM    425  C   LEU A  62      14.658  26.061  -9.750  1.00 82.36           C  
ATOM    426  O   LEU A  62      13.451  25.866  -9.529  1.00 82.26           O  
ATOM    427  CB  LEU A  62      15.196  24.062  -8.276  1.00 66.24           C  
ATOM    428  CG  LEU A  62      16.277  23.077  -7.822  1.00 60.30           C  
ATOM    429  CD1 LEU A  62      15.684  21.991  -6.947  1.00 58.67           C  
ATOM    430  CD2 LEU A  62      16.948  22.474  -9.038  1.00 58.75           C  
ATOM    431  N   GLY A  63      15.114  26.971 -10.613  1.00 90.78           N  
ATOM    432  CA  GLY A  63      14.225  27.761 -11.447  1.00 98.56           C  
ATOM    433  C   GLY A  63      13.380  28.884 -10.877  1.00104.10           C  
ATOM    434  O   GLY A  63      13.205  29.901 -11.550  1.00107.06           O  
ATOM    435  N   TYR A  64      12.841  28.716  -9.671  1.00108.90           N  
ATOM    436  CA  TYR A  64      11.986  29.744  -9.064  1.00115.22           C  
ATOM    437  C   TYR A  64      12.620  31.133  -8.942  1.00115.84           C  
ATOM    438  O   TYR A  64      13.830  31.299  -9.127  1.00114.26           O  
ATOM    439  CB  TYR A  64      11.478  29.297  -7.697  1.00119.34           C  
ATOM    440  CG  TYR A  64      10.787  27.955  -7.683  1.00124.53           C  
ATOM    441  CD1 TYR A  64      11.523  26.775  -7.576  1.00124.74           C  
ATOM    442  CD2 TYR A  64       9.397  27.864  -7.749  1.00126.01           C  
ATOM    443  CE1 TYR A  64      10.896  25.536  -7.533  1.00126.50           C  
ATOM    444  CE2 TYR A  64       8.757  26.625  -7.705  1.00127.32           C  
ATOM    445  CZ  TYR A  64       9.515  25.465  -7.595  1.00126.25           C  
ATOM    446  OH  TYR A  64       8.893  24.239  -7.535  1.00123.87           O  
ATOM    447  N   GLY A  65      11.788  32.115  -8.594  1.00115.63           N  
ATOM    448  CA  GLY A  65      12.237  33.493  -8.475  1.00115.29           C  
ATOM    449  C   GLY A  65      12.246  34.101  -9.865  1.00117.11           C  
ATOM    450  O   GLY A  65      13.107  33.759 -10.679  1.00117.85           O  
ATOM    451  N   LEU A  66      11.289  34.981 -10.156  1.00117.87           N  
ATOM    452  CA  LEU A  66      11.212  35.588 -11.483  1.00121.21           C  
ATOM    453  C   LEU A  66      10.576  36.974 -11.570  1.00122.15           C  
ATOM    454  O   LEU A  66      11.247  37.926 -11.974  1.00124.62           O  
ATOM    455  CB  LEU A  66      10.513  34.637 -12.465  1.00125.39           C  
ATOM    456  CG  LEU A  66      10.253  35.099 -13.900  1.00128.88           C  
ATOM    457  CD1 LEU A  66      11.562  35.471 -14.600  1.00129.03           C  
ATOM    458  CD2 LEU A  66       9.523  34.002 -14.673  1.00130.12           C  
ATOM    459  N   THR A  67       9.293  37.076 -11.209  1.00123.58           N  
ATOM    460  CA  THR A  67       8.507  38.324 -11.264  1.00123.60           C  
ATOM    461  C   THR A  67       9.294  39.610 -11.477  1.00121.91           C  
ATOM    462  O   THR A  67       9.878  40.163 -10.550  1.00123.04           O  
ATOM    463  CB  THR A  67       7.584  38.483 -10.041  1.00125.60           C  
ATOM    464  OG1 THR A  67       6.868  37.260  -9.816  1.00130.39           O  
ATOM    465  CG2 THR A  67       6.574  39.580 -10.309  1.00128.08           C  
ATOM    466  N   MET A  68       9.252  40.080 -12.719  1.00122.47           N  
ATOM    467  CA  MET A  68       9.953  41.267 -13.215  1.00122.09           C  
ATOM    468  C   MET A  68      10.065  42.562 -12.406  1.00123.23           C  
ATOM    469  O   MET A  68       9.431  42.748 -11.373  1.00123.44           O  
ATOM    470  CB  MET A  68       9.426  41.611 -14.615  1.00119.03           C  
ATOM    471  CG  MET A  68       7.966  42.067 -14.664  1.00113.47           C  
ATOM    472  SD  MET A  68       6.745  40.764 -14.412  1.00104.06           S  
ATOM    473  CE  MET A  68       6.083  40.612 -16.060  1.00102.52           C  
ATOM    474  N   VAL A  69      10.903  43.449 -12.939  1.00124.56           N  
ATOM    475  CA  VAL A  69      11.209  44.781 -12.404  1.00126.16           C  
ATOM    476  C   VAL A  69      10.795  45.745 -13.552  1.00125.79           C  
ATOM    477  O   VAL A  69       9.820  45.434 -14.246  1.00124.24           O  
ATOM    478  CB  VAL A  69      12.720  44.884 -12.061  1.00130.18           C  
ATOM    479  CG1 VAL A  69      13.011  44.194 -10.769  1.00129.38           C  
ATOM    480  CG2 VAL A  69      13.566  44.303 -13.192  1.00131.93           C  
ATOM    481  N   PRO A  70      11.457  46.915 -13.748  1.00126.03           N  
ATOM    482  CA  PRO A  70      10.970  47.729 -14.870  1.00127.21           C  
ATOM    483  C   PRO A  70      10.983  46.987 -16.204  1.00129.50           C  
ATOM    484  O   PRO A  70      12.018  46.883 -16.864  1.00128.55           O  
ATOM    485  CB  PRO A  70      11.911  48.942 -14.865  1.00124.25           C  
ATOM    486  CG  PRO A  70      13.099  48.496 -14.098  1.00124.31           C  
ATOM    487  CD  PRO A  70      12.499  47.671 -13.023  1.00126.16           C  
ATOM    488  N   PHE A  71       9.815  46.461 -16.566  1.00132.64           N  
ATOM    489  CA  PHE A  71       9.608  45.699 -17.795  1.00134.94           C  
ATOM    490  C   PHE A  71      10.410  44.405 -17.883  1.00134.77           C  
ATOM    491  O   PHE A  71      11.628  44.416 -18.062  1.00135.26           O  
ATOM    492  CB  PHE A  71       9.840  46.568 -19.035  1.00137.07           C  
ATOM    493  CG  PHE A  71       8.622  47.334 -19.468  1.00137.15           C  
ATOM    494  CD1 PHE A  71       8.223  48.480 -18.786  1.00136.05           C  
ATOM    495  CD2 PHE A  71       7.862  46.897 -20.551  1.00136.98           C  
ATOM    496  CE1 PHE A  71       7.082  49.180 -19.174  1.00137.98           C  
ATOM    497  CE2 PHE A  71       6.721  47.588 -20.947  1.00138.87           C  
ATOM    498  CZ  PHE A  71       6.330  48.733 -20.258  1.00139.39           C  
ATOM    499  N   GLY A  72       9.700  43.289 -17.749  1.00134.82           N  
ATOM    500  CA  GLY A  72      10.329  41.984 -17.824  1.00136.30           C  
ATOM    501  C   GLY A  72      10.037  41.292 -19.141  1.00137.60           C  
ATOM    502  O   GLY A  72       9.236  41.781 -19.947  1.00137.34           O  
ATOM    503  N   GLY A  73      10.675  40.144 -19.355  1.00137.56           N  
ATOM    504  CA  GLY A  73      10.479  39.403 -20.587  1.00136.95           C  
ATOM    505  C   GLY A  73      11.448  39.858 -21.661  1.00135.82           C  
ATOM    506  O   GLY A  73      11.830  39.080 -22.536  1.00135.88           O  
ATOM    507  N   GLU A  74      11.828  41.131 -21.602  1.00134.64           N  
ATOM    508  CA  GLU A  74      12.766  41.698 -22.558  1.00134.74           C  
ATOM    509  C   GLU A  74      14.212  41.515 -22.096  1.00134.47           C  
ATOM    510  O   GLU A  74      15.070  41.118 -22.889  1.00134.51           O  
ATOM    511  CB  GLU A  74      12.453  43.178 -22.805  1.00134.17           C  
ATOM    512  CG  GLU A  74      11.145  43.407 -23.558  1.00134.34           C  
ATOM    513  CD  GLU A  74      10.857  44.873 -23.846  1.00133.68           C  
ATOM    514  OE1 GLU A  74      11.807  45.635 -24.124  1.00133.40           O  
ATOM    515  OE2 GLU A  74       9.669  45.261 -23.809  1.00131.75           O  
ATOM    516  N   GLN A  75      14.475  41.762 -20.812  1.00132.76           N  
ATOM    517  CA  GLN A  75      15.829  41.617 -20.280  1.00129.97           C  
ATOM    518  C   GLN A  75      15.954  41.333 -18.783  1.00127.24           C  
ATOM    519  O   GLN A  75      16.150  40.186 -18.379  1.00129.13           O  
ATOM    520  CB  GLN A  75      16.671  42.850 -20.624  1.00132.50           C  
ATOM    521  CG  GLN A  75      18.109  42.768 -20.124  1.00135.14           C  
ATOM    522  CD  GLN A  75      18.869  44.068 -20.285  1.00136.69           C  
ATOM    523  OE1 GLN A  75      18.296  45.155 -20.189  1.00138.17           O  
ATOM    524  NE2 GLN A  75      20.171  43.963 -20.518  1.00137.68           N  
ATOM    525  N   ASN A  76      15.857  42.393 -17.982  1.00123.34           N  
ATOM    526  CA  ASN A  76      16.004  42.358 -16.522  1.00120.35           C  
ATOM    527  C   ASN A  76      15.449  41.178 -15.705  1.00116.87           C  
ATOM    528  O   ASN A  76      14.262  41.137 -15.377  1.00114.59           O  
ATOM    529  CB  ASN A  76      15.524  43.689 -15.924  1.00117.41           C  
ATOM    530  CG  ASN A  76      16.423  44.866 -16.303  1.00114.59           C  
ATOM    531  OD1 ASN A  76      17.525  44.686 -16.838  1.00109.67           O  
ATOM    532  ND2 ASN A  76      15.958  46.078 -16.015  1.00107.80           N  
ATOM    533  N   PRO A  77      16.331  40.230 -15.327  1.00115.03           N  
ATOM    534  CA  PRO A  77      16.013  39.030 -14.543  1.00116.65           C  
ATOM    535  C   PRO A  77      16.061  39.310 -13.036  1.00117.83           C  
ATOM    536  O   PRO A  77      17.031  39.895 -12.543  1.00117.80           O  
ATOM    537  CB  PRO A  77      17.112  38.064 -14.969  1.00116.95           C  
ATOM    538  CG  PRO A  77      18.293  38.970 -15.099  1.00115.04           C  
ATOM    539  CD  PRO A  77      17.736  40.201 -15.779  1.00114.16           C  
ATOM    540  N   ILE A  78      15.032  38.873 -12.307  1.00118.43           N  
ATOM    541  CA  ILE A  78      14.944  39.110 -10.861  1.00117.54           C  
ATOM    542  C   ILE A  78      14.417  37.901 -10.090  1.00117.31           C  
ATOM    543  O   ILE A  78      13.863  36.974 -10.680  1.00119.79           O  
ATOM    544  CB  ILE A  78      14.020  40.323 -10.574  1.00118.18           C  
ATOM    545  CG1 ILE A  78      14.581  41.574 -11.247  1.00122.33           C  
ATOM    546  CG2 ILE A  78      13.861  40.562  -9.078  1.00115.40           C  
ATOM    547  CD1 ILE A  78      15.900  42.075 -10.671  1.00129.04           C  
ATOM    548  N   TYR A  79      14.614  37.915  -8.770  1.00114.64           N  
ATOM    549  CA  TYR A  79      14.152  36.845  -7.881  1.00108.80           C  
ATOM    550  C   TYR A  79      13.145  37.369  -6.847  1.00105.75           C  
ATOM    551  O   TYR A  79      13.458  38.270  -6.059  1.00104.48           O  
ATOM    552  CB  TYR A  79      15.337  36.197  -7.154  1.00102.33           C  
ATOM    553  CG  TYR A  79      16.280  35.439  -8.055  1.00 98.98           C  
ATOM    554  CD1 TYR A  79      17.028  36.096  -9.029  1.00 99.67           C  
ATOM    555  CD2 TYR A  79      16.431  34.065  -7.929  1.00 96.83           C  
ATOM    556  CE1 TYR A  79      17.900  35.400  -9.852  1.00 98.62           C  
ATOM    557  CE2 TYR A  79      17.299  33.359  -8.747  1.00 96.54           C  
ATOM    558  CZ  TYR A  79      18.031  34.033  -9.705  1.00 98.94           C  
ATOM    559  OH  TYR A  79      18.899  33.337 -10.514  1.00100.09           O  
ATOM    560  N   TRP A  80      11.930  36.821  -6.873  1.00 91.94           N  
ATOM    561  CA  TRP A  80      10.894  37.227  -5.925  1.00 90.32           C  
ATOM    562  C   TRP A  80      10.925  36.328  -4.700  1.00 87.04           C  
ATOM    563  O   TRP A  80      10.371  36.667  -3.651  1.00 85.18           O  
ATOM    564  CB  TRP A  80       9.496  37.209  -6.568  1.00 89.94           C  
ATOM    565  CG  TRP A  80       8.957  35.851  -6.931  1.00 84.86           C  
ATOM    566  CD1 TRP A  80       8.881  35.316  -8.178  1.00 85.24           C  
ATOM    567  CD2 TRP A  80       8.357  34.892  -6.047  1.00 85.95           C  
ATOM    568  NE1 TRP A  80       8.266  34.089  -8.134  1.00 88.11           N  
ATOM    569  CE2 TRP A  80       7.934  33.804  -6.836  1.00 87.32           C  
ATOM    570  CE3 TRP A  80       8.129  34.849  -4.664  1.00 86.65           C  
ATOM    571  CZ2 TRP A  80       7.300  32.682  -6.290  1.00 85.00           C  
ATOM    572  CZ3 TRP A  80       7.500  33.734  -4.125  1.00 85.26           C  
ATOM    573  CH2 TRP A  80       7.092  32.668  -4.938  1.00 81.43           C  
ATOM    574  N   ALA A  81      11.555  35.165  -4.864  1.00 83.81           N  
ATOM    575  CA  ALA A  81      11.694  34.176  -3.805  1.00 76.71           C  
ATOM    576  C   ALA A  81      12.443  34.763  -2.613  1.00 75.07           C  
ATOM    577  O   ALA A  81      12.244  34.342  -1.475  1.00 76.88           O  
ATOM    578  CB  ALA A  81      12.421  32.962  -4.336  1.00 77.93           C  
ATOM    579  N   ARG A  82      13.289  35.754  -2.878  1.00 64.44           N  
ATOM    580  CA  ARG A  82      14.059  36.407  -1.828  1.00 62.18           C  
ATOM    581  C   ARG A  82      13.149  37.101  -0.799  1.00 61.72           C  
ATOM    582  O   ARG A  82      13.173  36.764   0.383  1.00 59.75           O  
ATOM    583  CB  ARG A  82      15.065  37.384  -2.445  1.00 62.45           C  
ATOM    584  CG  ARG A  82      16.045  36.722  -3.415  1.00 61.75           C  
ATOM    585  CD  ARG A  82      17.084  37.703  -3.942  1.00 60.89           C  
ATOM    586  NE  ARG A  82      17.925  37.118  -4.988  1.00 63.27           N  
ATOM    587  CZ  ARG A  82      19.159  36.652  -4.802  1.00 66.52           C  
ATOM    588  NH1 ARG A  82      19.711  36.688  -3.599  1.00 63.94           N  
ATOM    589  NH2 ARG A  82      19.863  36.179  -5.829  1.00 66.98           N  
ATOM    590  N   TYR A  83      12.323  38.042  -1.246  1.00 59.34           N  
ATOM    591  CA  TYR A  83      11.410  38.735  -0.333  1.00 61.59           C  
ATOM    592  C   TYR A  83      10.438  37.745   0.317  1.00 60.18           C  
ATOM    593  O   TYR A  83       9.962  37.960   1.437  1.00 53.28           O  
ATOM    594  CB  TYR A  83      10.633  39.832  -1.073  1.00 59.33           C  
ATOM    595  CG  TYR A  83      11.553  40.832  -1.709  1.00 59.13           C  
ATOM    596  CD1 TYR A  83      12.079  40.599  -2.979  1.00 67.81           C  
ATOM    597  CD2 TYR A  83      11.994  41.952  -1.004  1.00 58.79           C  
ATOM    598  CE1 TYR A  83      13.036  41.447  -3.531  1.00 65.96           C  
ATOM    599  CE2 TYR A  83      12.959  42.812  -1.551  1.00 60.56           C  
ATOM    600  CZ  TYR A  83      13.474  42.542  -2.812  1.00 61.01           C  
ATOM    601  OH  TYR A  83      14.461  43.308  -3.352  1.00 48.33           O  
ATOM    602  N   ALA A  84      10.179  36.644  -0.387  1.00 61.96           N  
ATOM    603  CA  ALA A  84       9.280  35.608   0.103  1.00 60.02           C  
ATOM    604  C   ALA A  84       9.839  35.001   1.388  1.00 53.25           C  
ATOM    605  O   ALA A  84       9.118  34.297   2.103  1.00 50.34           O  
ATOM    606  CB  ALA A  84       9.072  34.529  -0.963  1.00 62.29           C  
ATOM    607  N   ASP A  85      11.118  35.234   1.660  1.00 49.85           N  
ATOM    608  CA  ASP A  85      11.697  34.708   2.877  1.00 53.37           C  
ATOM    609  C   ASP A  85      12.061  35.790   3.885  1.00 51.39           C  
ATOM    610  O   ASP A  85      11.922  35.579   5.088  1.00 45.40           O  
ATOM    611  CB  ASP A  85      12.870  33.758   2.603  1.00 56.09           C  
ATOM    612  CG  ASP A  85      14.074  34.447   1.981  1.00 71.17           C  
ATOM    613  OD1 ASP A  85      14.922  34.943   2.752  1.00 72.15           O  
ATOM    614  OD2 ASP A  85      14.180  34.445   0.730  1.00 76.38           O  
ATOM    615  N   TRP A  86      12.475  36.966   3.390  1.00 54.69           N  
ATOM    616  CA  TRP A  86      12.852  38.108   4.241  1.00 50.86           C  
ATOM    617  C   TRP A  86      11.630  38.583   5.030  1.00 49.34           C  
ATOM    618  O   TRP A  86      11.747  39.077   6.153  1.00 37.20           O  
ATOM    619  CB  TRP A  86      13.427  39.257   3.391  1.00 52.29           C  
ATOM    620  CG  TRP A  86      14.759  38.920   2.724  1.00 54.85           C  
ATOM    621  CD1 TRP A  86      15.533  37.820   2.958  1.00 49.26           C  
ATOM    622  CD2 TRP A  86      15.447  39.681   1.714  1.00 51.23           C  
ATOM    623  NE1 TRP A  86      16.648  37.841   2.153  1.00 51.84           N  
ATOM    624  CE2 TRP A  86      16.622  38.972   1.381  1.00 47.17           C  
ATOM    625  CE3 TRP A  86      15.183  40.890   1.058  1.00 52.36           C  
ATOM    626  CZ2 TRP A  86      17.533  39.429   0.420  1.00 45.31           C  
ATOM    627  CZ3 TRP A  86      16.091  41.344   0.101  1.00 49.28           C  
ATOM    628  CH2 TRP A  86      17.254  40.610  -0.208  1.00 42.62           C  
ATOM    629  N   LEU A  87      10.454  38.412   4.430  1.00 52.38           N  
ATOM    630  CA  LEU A  87       9.186  38.767   5.059  1.00 52.68           C  
ATOM    631  C   LEU A  87       8.899  37.674   6.101  1.00 60.81           C  
ATOM    632  O   LEU A  87       8.194  37.904   7.090  1.00 63.11           O  
ATOM    633  CB  LEU A  87       8.087  38.773   4.002  1.00 51.35           C  
ATOM    634  CG  LEU A  87       6.648  39.112   4.369  1.00 47.81           C  
ATOM    635  CD1 LEU A  87       6.481  40.616   4.427  1.00 50.83           C  
ATOM    636  CD2 LEU A  87       5.727  38.532   3.309  1.00 43.63           C  
ATOM    637  N   PHE A  88       9.467  36.488   5.863  1.00 67.28           N  
ATOM    638  CA  PHE A  88       9.317  35.326   6.745  1.00 63.45           C  
ATOM    639  C   PHE A  88      10.617  34.943   7.461  1.00 62.49           C  
ATOM    640  O   PHE A  88      10.917  33.761   7.613  1.00 65.18           O  
ATOM    641  CB  PHE A  88       8.806  34.117   5.952  1.00 56.95           C  
ATOM    642  CG  PHE A  88       7.326  34.129   5.705  1.00 56.03           C  
ATOM    643  CD1 PHE A  88       6.464  34.820   6.550  1.00 53.59           C  
ATOM    644  CD2 PHE A  88       6.790  33.425   4.640  1.00 54.62           C  
ATOM    645  CE1 PHE A  88       5.096  34.809   6.341  1.00 38.42           C  
ATOM    646  CE2 PHE A  88       5.421  33.407   4.423  1.00 54.39           C  
ATOM    647  CZ  PHE A  88       4.575  34.102   5.280  1.00 53.38           C  
ATOM    648  N   THR A  89      11.411  35.943   7.840  1.00 54.37           N  
ATOM    649  CA  THR A  89      12.663  35.706   8.560  1.00 54.30           C  
ATOM    650  C   THR A  89      12.955  36.852   9.517  1.00 51.39           C  
ATOM    651  O   THR A  89      13.236  36.643  10.699  1.00 47.14           O  
ATOM    652  CB  THR A  89      13.860  35.545   7.621  1.00 51.48           C  
ATOM    653  OG1 THR A  89      13.729  34.322   6.888  1.00 56.30           O  
ATOM    654  CG2 THR A  89      15.151  35.520   8.423  1.00 52.38           C  
ATOM    655  N   THR A  90      12.870  38.066   8.996  1.00 54.03           N  
ATOM    656  CA  THR A  90      13.112  39.259   9.791  1.00 53.69           C  
ATOM    657  C   THR A  90      12.154  39.434  10.994  1.00 54.96           C  
ATOM    658  O   THR A  90      12.591  39.857  12.061  1.00 52.43           O  
ATOM    659  CB  THR A  90      13.056  40.517   8.912  1.00 54.34           C  
ATOM    660  OG1 THR A  90      13.893  40.352   7.758  1.00 48.30           O  
ATOM    661  CG2 THR A  90      13.521  41.717   9.698  1.00 56.83           C  
ATOM    662  N   PRO A  91      10.847  39.106  10.842  1.00 57.09           N  
ATOM    663  CA  PRO A  91       9.888  39.257  11.950  1.00 56.10           C  
ATOM    664  C   PRO A  91      10.116  38.301  13.117  1.00 55.22           C  
ATOM    665  O   PRO A  91       9.822  38.635  14.259  1.00 54.96           O  
ATOM    666  CB  PRO A  91       8.534  38.957  11.290  1.00 51.47           C  
ATOM    667  CG  PRO A  91       8.769  39.216   9.830  1.00 53.05           C  
ATOM    668  CD  PRO A  91      10.142  38.656   9.623  1.00 56.58           C  
ATOM    669  N   LEU A  92      10.592  37.098  12.810  1.00 57.17           N  
ATOM    670  CA  LEU A  92      10.850  36.081  13.826  1.00 62.52           C  
ATOM    671  C   LEU A  92      12.209  36.249  14.493  1.00 63.29           C  
ATOM    672  O   LEU A  92      12.384  35.874  15.656  1.00 56.72           O  
ATOM    673  CB  LEU A  92      10.729  34.671  13.229  1.00 68.61           C  
ATOM    674  CG  LEU A  92       9.339  34.045  13.068  1.00 69.81           C  
ATOM    675  CD1 LEU A  92       8.486  34.852  12.097  1.00 74.29           C  
ATOM    676  CD2 LEU A  92       9.500  32.608  12.581  1.00 73.33           C  
ATOM    677  N   LEU A  93      13.169  36.790  13.744  1.00 63.58           N  
ATOM    678  CA  LEU A  93      14.516  37.028  14.254  1.00 68.60           C  
ATOM    679  C   LEU A  93      14.514  38.177  15.285  1.00 72.28           C  
ATOM    680  O   LEU A  93      15.419  38.289  16.126  1.00 70.71           O  
ATOM    681  CB  LEU A  93      15.450  37.357  13.090  1.00 72.93           C  
ATOM    682  CG  LEU A  93      16.842  36.731  13.149  1.00 78.28           C  
ATOM    683  CD1 LEU A  93      16.692  35.221  13.189  1.00 80.33           C  
ATOM    684  CD2 LEU A  93      17.661  37.160  11.944  1.00 78.11           C  
ATOM    685  N   LEU A  94      13.509  39.045  15.186  1.00 70.32           N  
ATOM    686  CA  LEU A  94      13.347  40.153  16.113  1.00 69.96           C  
ATOM    687  C   LEU A  94      12.494  39.665  17.266  1.00 73.16           C  
ATOM    688  O   LEU A  94      12.472  40.264  18.335  1.00 78.43           O  
ATOM    689  CB  LEU A  94      12.673  41.346  15.435  1.00 68.13           C  
ATOM    690  CG  LEU A  94      13.592  42.494  15.009  1.00 63.67           C  
ATOM    691  CD1 LEU A  94      14.784  41.942  14.251  1.00 67.79           C  
ATOM    692  CD2 LEU A  94      12.827  43.491  14.167  1.00 54.52           C  
ATOM    693  N   LEU A  95      11.772  38.577  17.033  1.00 77.22           N  
ATOM    694  CA  LEU A  95      10.933  37.991  18.068  1.00 83.43           C  
ATOM    695  C   LEU A  95      11.850  37.253  19.048  1.00 82.39           C  
ATOM    696  O   LEU A  95      11.446  36.909  20.162  1.00 83.83           O  
ATOM    697  CB  LEU A  95       9.910  37.029  17.448  1.00 85.54           C  
ATOM    698  CG  LEU A  95       8.691  36.630  18.285  1.00 87.43           C  
ATOM    699  CD1 LEU A  95       7.984  37.872  18.826  1.00 91.69           C  
ATOM    700  CD2 LEU A  95       7.736  35.810  17.429  1.00 89.72           C  
ATOM    701  N   ASP A  96      13.091  37.028  18.624  1.00 79.61           N  
ATOM    702  CA  ASP A  96      14.070  36.349  19.458  1.00 76.54           C  
ATOM    703  C   ASP A  96      14.888  37.380  20.233  1.00 74.97           C  
ATOM    704  O   ASP A  96      15.438  37.072  21.295  1.00 75.27           O  
ATOM    705  CB  ASP A  96      14.982  35.459  18.608  1.00 76.71           C  
ATOM    706  CG  ASP A  96      15.539  34.281  19.392  1.00 78.08           C  
ATOM    707  OD1 ASP A  96      16.013  34.493  20.520  1.00 77.44           O  
ATOM    708  OD2 ASP A  96      15.498  33.141  18.888  1.00 80.13           O  
ATOM    709  N   LEU A  97      14.976  38.598  19.692  1.00 70.76           N  
ATOM    710  CA  LEU A  97      15.711  39.679  20.346  1.00 62.39           C  
ATOM    711  C   LEU A  97      14.787  40.602  21.134  1.00 56.04           C  
ATOM    712  O   LEU A  97      15.250  41.523  21.793  1.00 52.82           O  
ATOM    713  CB  LEU A  97      16.575  40.469  19.348  1.00 64.65           C  
ATOM    714  CG  LEU A  97      15.978  41.202  18.140  1.00 73.21           C  
ATOM    715  CD1 LEU A  97      15.185  42.433  18.555  1.00 72.13           C  
ATOM    716  CD2 LEU A  97      17.107  41.621  17.213  1.00 78.00           C  
ATOM    717  N   ALA A  98      13.479  40.372  21.031  1.00 56.34           N  
ATOM    718  CA  ALA A  98      12.490  41.163  21.773  1.00 55.77           C  
ATOM    719  C   ALA A  98      12.114  40.390  23.043  1.00 59.28           C  
ATOM    720  O   ALA A  98      11.674  40.978  24.044  1.00 55.03           O  
ATOM    721  CB  ALA A  98      11.265  41.422  20.929  1.00 42.28           C  
ATOM    722  N   LEU A  99      12.250  39.065  22.976  1.00 59.33           N  
ATOM    723  CA  LEU A  99      11.961  38.223  24.124  1.00 62.96           C  
ATOM    724  C   LEU A  99      13.182  38.225  25.035  1.00 65.99           C  
ATOM    725  O   LEU A  99      13.060  38.040  26.245  1.00 72.97           O  
ATOM    726  CB  LEU A  99      11.594  36.794  23.700  1.00 64.21           C  
ATOM    727  CG  LEU A  99      10.102  36.443  23.515  1.00 71.90           C  
ATOM    728  CD1 LEU A  99       9.334  36.673  24.822  1.00 63.45           C  
ATOM    729  CD2 LEU A  99       9.457  37.239  22.374  1.00 68.45           C  
ATOM    730  N   LEU A 100      14.355  38.477  24.456  1.00 66.09           N  
ATOM    731  CA  LEU A 100      15.594  38.527  25.231  1.00 63.05           C  
ATOM    732  C   LEU A 100      15.513  39.766  26.102  1.00 62.11           C  
ATOM    733  O   LEU A 100      15.761  39.705  27.305  1.00 63.17           O  
ATOM    734  CB  LEU A 100      16.821  38.622  24.315  1.00 60.71           C  
ATOM    735  CG  LEU A 100      18.136  38.011  24.820  1.00 48.66           C  
ATOM    736  CD1 LEU A 100      18.042  36.481  24.763  1.00 42.18           C  
ATOM    737  CD2 LEU A 100      19.308  38.495  23.976  1.00 42.83           C  
ATOM    738  N   VAL A 101      15.103  40.872  25.480  1.00 65.28           N  
ATOM    739  CA  VAL A 101      14.946  42.174  26.139  1.00 66.03           C  
ATOM    740  C   VAL A 101      13.687  42.187  27.023  1.00 65.20           C  
ATOM    741  O   VAL A 101      13.414  43.159  27.734  1.00 57.16           O  
ATOM    742  CB  VAL A 101      14.867  43.311  25.074  1.00 67.83           C  
ATOM    743  CG1 VAL A 101      14.844  44.691  25.728  1.00 71.49           C  
ATOM    744  CG2 VAL A 101      16.037  43.206  24.130  1.00 58.75           C  
ATOM    745  N   ASP A 102      12.921  41.100  26.963  1.00 69.00           N  
ATOM    746  CA  ASP A 102      11.703  40.953  27.759  1.00 75.86           C  
ATOM    747  C   ASP A 102      10.793  42.185  27.616  1.00 77.46           C  
ATOM    748  O   ASP A 102      10.244  42.684  28.600  1.00 77.67           O  
ATOM    749  CB  ASP A 102      12.062  40.725  29.241  1.00 81.05           C  
ATOM    750  CG  ASP A 102      13.040  39.558  29.456  1.00 84.83           C  
ATOM    751  OD1 ASP A 102      12.625  38.385  29.330  1.00 80.91           O  
ATOM    752  OD2 ASP A 102      14.219  39.815  29.789  1.00 84.07           O  
ATOM    753  N   ALA A 103      10.648  42.668  26.383  1.00 85.59           N  
ATOM    754  CA  ALA A 103       9.820  43.839  26.083  1.00 85.38           C  
ATOM    755  C   ALA A 103       8.321  43.544  26.080  1.00 87.30           C  
ATOM    756  O   ALA A 103       7.900  42.397  25.934  1.00 90.23           O  
ATOM    757  CB  ALA A 103      10.231  44.436  24.751  1.00 83.21           C  
ATOM    758  N   ASP A 104       7.518  44.595  26.227  1.00 89.59           N  
ATOM    759  CA  ASP A 104       6.059  44.477  26.242  1.00 88.78           C  
ATOM    760  C   ASP A 104       5.520  44.199  24.834  1.00 86.11           C  
ATOM    761  O   ASP A 104       6.194  44.497  23.841  1.00 84.48           O  
ATOM    762  CB  ASP A 104       5.446  45.768  26.804  1.00 92.92           C  
ATOM    763  CG  ASP A 104       3.937  45.679  26.983  1.00 97.87           C  
ATOM    764  OD1 ASP A 104       3.475  44.832  27.775  1.00100.08           O  
ATOM    765  OD2 ASP A 104       3.215  46.461  26.331  1.00 99.73           O  
ATOM    766  N   GLN A 105       4.309  43.641  24.753  1.00 81.85           N  
ATOM    767  CA  GLN A 105       3.685  43.330  23.465  1.00 77.84           C  
ATOM    768  C   GLN A 105       3.531  44.549  22.570  1.00 74.17           C  
ATOM    769  O   GLN A 105       3.308  44.411  21.367  1.00 74.46           O  
ATOM    770  CB  GLN A 105       2.316  42.675  23.649  1.00 80.67           C  
ATOM    771  CG  GLN A 105       2.365  41.223  24.116  1.00 88.01           C  
ATOM    772  CD  GLN A 105       0.994  40.556  24.121  1.00 86.25           C  
ATOM    773  OE1 GLN A 105       0.238  40.655  25.097  1.00 80.69           O  
ATOM    774  NE2 GLN A 105       0.669  39.869  23.027  1.00 81.03           N  
ATOM    775  N   GLY A 106       3.656  45.734  23.163  1.00 69.36           N  
ATOM    776  CA  GLY A 106       3.534  46.971  22.415  1.00 65.72           C  
ATOM    777  C   GLY A 106       4.614  47.158  21.362  1.00 65.52           C  
ATOM    778  O   GLY A 106       4.325  47.161  20.160  1.00 67.87           O  
ATOM    779  N   THR A 107       5.864  47.283  21.801  1.00 60.09           N  
ATOM    780  CA  THR A 107       6.971  47.489  20.873  1.00 58.02           C  
ATOM    781  C   THR A 107       7.228  46.287  19.955  1.00 53.71           C  
ATOM    782  O   THR A 107       7.846  46.425  18.904  1.00 52.04           O  
ATOM    783  CB  THR A 107       8.258  47.862  21.620  1.00 59.89           C  
ATOM    784  OG1 THR A 107       9.244  48.319  20.684  1.00 64.31           O  
ATOM    785  CG2 THR A 107       8.791  46.662  22.380  1.00 64.67           C  
ATOM    786  N   ILE A 108       6.764  45.112  20.363  1.00 51.65           N  
ATOM    787  CA  ILE A 108       6.930  43.904  19.566  1.00 51.48           C  
ATOM    788  C   ILE A 108       5.996  43.983  18.359  1.00 54.19           C  
ATOM    789  O   ILE A 108       6.407  43.725  17.223  1.00 49.44           O  
ATOM    790  CB  ILE A 108       6.627  42.628  20.411  1.00 46.49           C  
ATOM    791  CG1 ILE A 108       7.708  42.444  21.475  1.00 37.92           C  
ATOM    792  CG2 ILE A 108       6.535  41.379  19.527  1.00 51.65           C  
ATOM    793  CD1 ILE A 108       7.549  41.181  22.276  1.00 39.42           C  
ATOM    794  N   LEU A 109       4.756  44.394  18.615  1.00 55.69           N  
ATOM    795  CA  LEU A 109       3.739  44.519  17.577  1.00 58.66           C  
ATOM    796  C   LEU A 109       4.160  45.483  16.468  1.00 59.41           C  
ATOM    797  O   LEU A 109       4.140  45.125  15.291  1.00 61.07           O  
ATOM    798  CB  LEU A 109       2.423  44.988  18.195  1.00 57.40           C  
ATOM    799  CG  LEU A 109       1.124  44.678  17.450  1.00 60.56           C  
ATOM    800  CD1 LEU A 109      -0.051  44.948  18.380  1.00 66.75           C  
ATOM    801  CD2 LEU A 109       1.005  45.488  16.174  1.00 56.96           C  
ATOM    802  N   ALA A 110       4.510  46.712  16.840  1.00 59.65           N  
ATOM    803  CA  ALA A 110       4.930  47.713  15.861  1.00 56.62           C  
ATOM    804  C   ALA A 110       6.079  47.140  15.051  1.00 54.93           C  
ATOM    805  O   ALA A 110       6.129  47.291  13.842  1.00 60.57           O  
ATOM    806  CB  ALA A 110       5.366  48.994  16.562  1.00 64.38           C  
ATOM    807  N   LEU A 111       6.951  46.410  15.737  1.00 57.77           N  
ATOM    808  CA  LEU A 111       8.122  45.771  15.150  1.00 67.06           C  
ATOM    809  C   LEU A 111       7.799  44.730  14.050  1.00 66.16           C  
ATOM    810  O   LEU A 111       8.611  44.507  13.143  1.00 64.29           O  
ATOM    811  CB  LEU A 111       8.957  45.184  16.299  1.00 78.08           C  
ATOM    812  CG  LEU A 111      10.149  44.239  16.194  1.00 79.28           C  
ATOM    813  CD1 LEU A 111      11.189  44.623  17.247  1.00 76.40           C  
ATOM    814  CD2 LEU A 111       9.665  42.809  16.405  1.00 81.79           C  
ATOM    815  N   VAL A 112       6.617  44.111  14.119  1.00 57.79           N  
ATOM    816  CA  VAL A 112       6.204  43.137  13.105  1.00 49.88           C  
ATOM    817  C   VAL A 112       5.570  43.901  11.936  1.00 51.15           C  
ATOM    818  O   VAL A 112       5.879  43.646  10.764  1.00 50.08           O  
ATOM    819  CB  VAL A 112       5.159  42.119  13.649  1.00 40.50           C  
ATOM    820  CG1 VAL A 112       5.255  40.801  12.887  1.00 31.87           C  
ATOM    821  CG2 VAL A 112       5.352  41.886  15.117  1.00 55.05           C  
ATOM    822  N   GLY A 113       4.681  44.840  12.267  1.00 53.57           N  
ATOM    823  CA  GLY A 113       4.018  45.651  11.258  1.00 48.24           C  
ATOM    824  C   GLY A 113       4.983  46.581  10.543  1.00 42.58           C  
ATOM    825  O   GLY A 113       4.722  47.000   9.420  1.00 34.94           O  
ATOM    826  N   ALA A 114       6.096  46.898  11.210  1.00 39.98           N  
ATOM    827  CA  ALA A 114       7.145  47.772  10.684  1.00 40.22           C  
ATOM    828  C   ALA A 114       7.928  47.014   9.607  1.00 48.98           C  
ATOM    829  O   ALA A 114       8.110  47.514   8.491  1.00 47.10           O  
ATOM    830  CB  ALA A 114       8.076  48.197  11.819  1.00 30.83           C  
ATOM    831  N   ASP A 115       8.392  45.809   9.952  1.00 54.31           N  
ATOM    832  CA  ASP A 115       9.126  44.961   9.015  1.00 54.89           C  
ATOM    833  C   ASP A 115       8.207  44.473   7.895  1.00 57.30           C  
ATOM    834  O   ASP A 115       8.605  44.449   6.725  1.00 51.74           O  
ATOM    835  CB  ASP A 115       9.730  43.752   9.725  1.00 64.60           C  
ATOM    836  CG  ASP A 115      10.532  42.877   8.784  1.00 71.36           C  
ATOM    837  OD1 ASP A 115      11.453  43.401   8.118  1.00 71.33           O  
ATOM    838  OD2 ASP A 115      10.228  41.674   8.694  1.00 80.43           O  
ATOM    839  N   GLY A 116       6.988  44.069   8.262  1.00 54.66           N  
ATOM    840  CA  GLY A 116       6.030  43.602   7.275  1.00 56.85           C  
ATOM    841  C   GLY A 116       5.960  44.581   6.115  1.00 56.95           C  
ATOM    842  O   GLY A 116       6.092  44.209   4.946  1.00 57.20           O  
ATOM    843  N   ILE A 117       5.841  45.858   6.455  1.00 50.28           N  
ATOM    844  CA  ILE A 117       5.767  46.895   5.448  1.00 43.52           C  
ATOM    845  C   ILE A 117       7.132  47.100   4.797  1.00 38.20           C  
ATOM    846  O   ILE A 117       7.208  47.362   3.591  1.00 33.41           O  
ATOM    847  CB  ILE A 117       5.204  48.210   6.053  1.00 44.99           C  
ATOM    848  CG1 ILE A 117       3.760  47.970   6.501  1.00 48.54           C  
ATOM    849  CG2 ILE A 117       5.255  49.363   5.035  1.00 44.95           C  
ATOM    850  CD1 ILE A 117       2.853  47.406   5.375  1.00 53.14           C  
ATOM    851  N   MET A 118       8.201  46.894   5.570  1.00 25.33           N  
ATOM    852  CA  MET A 118       9.576  47.071   5.062  1.00 28.76           C  
ATOM    853  C   MET A 118       9.918  46.165   3.865  1.00 28.01           C  
ATOM    854  O   MET A 118      10.523  46.608   2.884  1.00 36.14           O  
ATOM    855  CB  MET A 118      10.572  46.831   6.189  1.00 39.12           C  
ATOM    856  CG  MET A 118      12.025  46.957   5.805  1.00 40.58           C  
ATOM    857  SD  MET A 118      12.996  46.341   7.185  1.00 48.87           S  
ATOM    858  CE  MET A 118      14.643  46.508   6.532  1.00 52.28           C  
ATOM    859  N   ILE A 119       9.526  44.891   3.974  1.00 40.21           N  
ATOM    860  CA  ILE A 119       9.750  43.886   2.933  1.00 37.05           C  
ATOM    861  C   ILE A 119       8.545  43.823   1.974  1.00 38.75           C  
ATOM    862  O   ILE A 119       8.647  43.393   0.825  1.00 27.19           O  
ATOM    863  CB  ILE A 119      10.092  42.532   3.569  1.00 44.05           C  
ATOM    864  CG1 ILE A 119      11.327  42.711   4.461  1.00 46.41           C  
ATOM    865  CG2 ILE A 119      10.347  41.468   2.507  1.00 40.05           C  
ATOM    866  CD1 ILE A 119      12.493  43.445   3.793  1.00 42.62           C  
ATOM    867  N   GLY A 120       7.406  44.303   2.450  1.00 39.74           N  
ATOM    868  CA  GLY A 120       6.244  44.369   1.597  1.00 43.35           C  
ATOM    869  C   GLY A 120       6.593  45.457   0.595  1.00 42.04           C  
ATOM    870  O   GLY A 120       6.703  45.195  -0.601  1.00 55.64           O  
ATOM    871  N   THR A 121       6.882  46.654   1.099  1.00 41.29           N  
ATOM    872  CA  THR A 121       7.242  47.785   0.245  1.00 48.78           C  
ATOM    873  C   THR A 121       8.461  47.508  -0.661  1.00 48.04           C  
ATOM    874  O   THR A 121       8.555  48.037  -1.770  1.00 41.49           O  
ATOM    875  CB  THR A 121       7.507  49.067   1.078  1.00 51.67           C  
ATOM    876  OG1 THR A 121       6.365  49.367   1.890  1.00 56.15           O  
ATOM    877  CG2 THR A 121       7.761  50.241   0.163  1.00 61.61           C  
ATOM    878  N   GLY A 122       9.392  46.689  -0.188  1.00 42.88           N  
ATOM    879  CA  GLY A 122      10.566  46.385  -0.990  1.00 44.45           C  
ATOM    880  C   GLY A 122      10.218  45.436  -2.125  1.00 49.85           C  
ATOM    881  O   GLY A 122      10.669  45.600  -3.272  1.00 42.42           O  
ATOM    882  N   LEU A 123       9.419  44.425  -1.782  1.00 50.31           N  
ATOM    883  CA  LEU A 123       8.966  43.410  -2.728  1.00 53.82           C  
ATOM    884  C   LEU A 123       8.258  44.108  -3.875  1.00 47.44           C  
ATOM    885  O   LEU A 123       8.552  43.857  -5.037  1.00 57.85           O  
ATOM    886  CB  LEU A 123       8.013  42.430  -2.026  1.00 60.45           C  
ATOM    887  CG  LEU A 123       7.200  41.407  -2.836  1.00 68.70           C  
ATOM    888  CD1 LEU A 123       8.116  40.484  -3.675  1.00 62.04           C  
ATOM    889  CD2 LEU A 123       6.336  40.598  -1.863  1.00 70.18           C  
ATOM    890  N   VAL A 124       7.341  45.001  -3.529  1.00 42.12           N  
ATOM    891  CA  VAL A 124       6.592  45.767  -4.512  1.00 33.91           C  
ATOM    892  C   VAL A 124       7.561  46.583  -5.368  1.00 40.20           C  
ATOM    893  O   VAL A 124       7.452  46.619  -6.603  1.00 41.15           O  
ATOM    894  CB  VAL A 124       5.616  46.716  -3.797  1.00 23.77           C  
ATOM    895  CG1 VAL A 124       5.171  47.854  -4.719  1.00 35.74           C  
ATOM    896  CG2 VAL A 124       4.422  45.929  -3.311  1.00 29.00           C  
ATOM    897  N   GLY A 125       8.518  47.218  -4.691  1.00 50.82           N  
ATOM    898  CA  GLY A 125       9.512  48.042  -5.360  1.00 48.87           C  
ATOM    899  C   GLY A 125      10.180  47.286  -6.478  1.00 50.63           C  
ATOM    900  O   GLY A 125      10.318  47.816  -7.576  1.00 54.45           O  
ATOM    901  N   ALA A 126      10.532  46.031  -6.197  1.00 46.99           N  
ATOM    902  CA  ALA A 126      11.181  45.134  -7.153  1.00 50.58           C  
ATOM    903  C   ALA A 126      10.243  44.658  -8.271  1.00 55.43           C  
ATOM    904  O   ALA A 126      10.680  44.472  -9.407  1.00 41.37           O  
ATOM    905  CB  ALA A 126      11.761  43.943  -6.424  1.00 39.73           C  
ATOM    906  N   LEU A 127       8.960  44.485  -7.934  1.00 61.87           N  
ATOM    907  CA  LEU A 127       7.935  44.025  -8.862  1.00 70.41           C  
ATOM    908  C   LEU A 127       7.467  45.005  -9.911  1.00 82.73           C  
ATOM    909  O   LEU A 127       6.583  45.822  -9.675  1.00 80.04           O  
ATOM    910  CB  LEU A 127       6.754  43.451  -8.103  1.00 70.31           C  
ATOM    911  CG  LEU A 127       6.875  41.937  -7.976  1.00 77.44           C  
ATOM    912  CD1 LEU A 127       8.230  41.547  -7.363  1.00 81.29           C  
ATOM    913  CD2 LEU A 127       5.702  41.371  -7.186  1.00 77.08           C  
ATOM    914  N   THR A 128       8.019  44.828 -11.109  1.00 99.42           N  
ATOM    915  CA  THR A 128       7.745  45.671 -12.273  1.00109.05           C  
ATOM    916  C   THR A 128       8.157  47.111 -11.916  1.00112.47           C  
ATOM    917  O   THR A 128       9.131  47.313 -11.182  1.00113.56           O  
ATOM    918  CB  THR A 128       6.274  45.551 -12.751  1.00109.61           C  
ATOM    919  OG1 THR A 128       5.807  44.212 -12.530  1.00109.90           O  
ATOM    920  CG2 THR A 128       6.186  45.828 -14.249  1.00109.83           C  
ATOM    921  N   LYS A 129       7.466  48.102 -12.459  1.00116.84           N  
ATOM    922  CA  LYS A 129       7.769  49.502 -12.171  1.00122.49           C  
ATOM    923  C   LYS A 129       6.603  50.296 -12.727  1.00124.93           C  
ATOM    924  O   LYS A 129       6.776  51.381 -13.295  1.00125.16           O  
ATOM    925  CB  LYS A 129       9.073  49.932 -12.851  1.00125.56           C  
ATOM    926  CG  LYS A 129      10.162  50.434 -11.906  1.00127.19           C  
ATOM    927  CD  LYS A 129      10.468  51.914 -12.119  1.00128.39           C  
ATOM    928  CE  LYS A 129      11.904  52.136 -12.570  1.00128.42           C  
ATOM    929  NZ  LYS A 129      12.250  53.590 -12.618  1.00125.60           N  
ATOM    930  N   VAL A 130       5.412  49.718 -12.563  1.00125.16           N  
ATOM    931  CA  VAL A 130       4.146  50.281 -13.037  1.00124.80           C  
ATOM    932  C   VAL A 130       3.918  51.768 -12.752  1.00123.38           C  
ATOM    933  O   VAL A 130       3.384  52.139 -11.708  1.00124.88           O  
ATOM    934  CB  VAL A 130       2.954  49.444 -12.514  1.00126.02           C  
ATOM    935  CG1 VAL A 130       3.001  48.059 -13.136  1.00126.70           C  
ATOM    936  CG2 VAL A 130       3.005  49.327 -11.001  1.00129.71           C  
ATOM    937  N   TYR A 131       4.350  52.604 -13.698  1.00121.62           N  
ATOM    938  CA  TYR A 131       4.222  54.059 -13.629  1.00118.64           C  
ATOM    939  C   TYR A 131       4.880  54.691 -12.401  1.00113.59           C  
ATOM    940  O   TYR A 131       5.013  55.909 -12.311  1.00110.74           O  
ATOM    941  CB  TYR A 131       2.743  54.462 -13.709  1.00125.53           C  
ATOM    942  CG  TYR A 131       2.530  55.958 -13.703  1.00133.10           C  
ATOM    943  CD1 TYR A 131       2.786  56.721 -14.842  1.00138.44           C  
ATOM    944  CD2 TYR A 131       2.108  56.615 -12.548  1.00136.04           C  
ATOM    945  CE1 TYR A 131       2.640  58.108 -14.827  1.00142.67           C  
ATOM    946  CE2 TYR A 131       1.960  57.999 -12.523  1.00140.03           C  
ATOM    947  CZ  TYR A 131       2.223  58.738 -13.664  1.00142.43           C  
ATOM    948  OH  TYR A 131       2.081  60.107 -13.637  1.00143.62           O  
ATOM    949  N   SER A 132       5.290  53.846 -11.463  1.00110.51           N  
ATOM    950  CA  SER A 132       5.926  54.280 -10.231  1.00105.52           C  
ATOM    951  C   SER A 132       7.431  54.071 -10.275  1.00107.47           C  
ATOM    952  O   SER A 132       7.923  53.168 -10.952  1.00111.15           O  
ATOM    953  CB  SER A 132       5.330  53.519  -9.040  1.00 98.52           C  
ATOM    954  OG  SER A 132       4.720  52.298  -9.440  1.00 76.85           O  
ATOM    955  N   TYR A 133       8.158  54.926  -9.568  1.00120.08           N  
ATOM    956  CA  TYR A 133       9.604  54.814  -9.508  1.00120.08           C  
ATOM    957  C   TYR A 133       9.906  53.746  -8.465  1.00120.08           C  
ATOM    958  O   TYR A 133       9.255  53.687  -7.423  1.00120.08           O  
ATOM    959  CB  TYR A 133      10.233  56.151  -9.102  1.00120.08           C  
ATOM    960  CG  TYR A 133       9.814  57.313  -9.978  1.00120.08           C  
ATOM    961  CD1 TYR A 133       8.629  58.007  -9.728  1.00120.08           C  
ATOM    962  CD2 TYR A 133      10.586  57.702 -11.071  1.00120.08           C  
ATOM    963  CE1 TYR A 133       8.222  59.055 -10.546  1.00120.08           C  
ATOM    964  CE2 TYR A 133      10.186  58.750 -11.895  1.00120.08           C  
ATOM    965  CZ  TYR A 133       9.004  59.420 -11.626  1.00120.08           C  
ATOM    966  OH  TYR A 133       8.607  60.456 -12.435  1.00120.08           O  
ATOM    967  N   ARG A 134      10.857  52.873  -8.770  1.00120.08           N  
ATOM    968  CA  ARG A 134      11.232  51.811  -7.846  1.00120.08           C  
ATOM    969  C   ARG A 134      12.102  52.354  -6.716  1.00120.08           C  
ATOM    970  O   ARG A 134      12.514  51.615  -5.816  1.00120.08           O  
ATOM    971  CB  ARG A 134      11.949  50.686  -8.586  1.00120.08           C  
ATOM    972  CG  ARG A 134      13.339  51.029  -9.092  1.00120.08           C  
ATOM    973  CD  ARG A 134      13.937  49.823  -9.768  1.00120.08           C  
ATOM    974  NE  ARG A 134      13.536  48.611  -9.063  1.00120.08           N  
ATOM    975  CZ  ARG A 134      13.773  47.379  -9.490  1.00120.08           C  
ATOM    976  NH1 ARG A 134      14.426  47.181 -10.625  1.00120.08           N  
ATOM    977  NH2 ARG A 134      13.339  46.346  -8.788  1.00120.08           N  
ATOM    978  N   PHE A 135      12.413  53.643  -6.798  1.00 88.12           N  
ATOM    979  CA  PHE A 135      13.200  54.309  -5.774  1.00 79.08           C  
ATOM    980  C   PHE A 135      12.239  54.876  -4.727  1.00 80.80           C  
ATOM    981  O   PHE A 135      12.638  55.187  -3.601  1.00 82.14           O  
ATOM    982  CB  PHE A 135      14.077  55.394  -6.397  1.00 65.06           C  
ATOM    983  CG  PHE A 135      15.161  54.852  -7.280  1.00 67.28           C  
ATOM    984  CD1 PHE A 135      16.206  54.101  -6.737  1.00 72.41           C  
ATOM    985  CD2 PHE A 135      15.134  55.067  -8.651  1.00 63.52           C  
ATOM    986  CE1 PHE A 135      17.205  53.573  -7.550  1.00 59.35           C  
ATOM    987  CE2 PHE A 135      16.122  54.548  -9.472  1.00 63.72           C  
ATOM    988  CZ  PHE A 135      17.163  53.799  -8.925  1.00 67.43           C  
ATOM    989  N   VAL A 136      10.961  54.958  -5.100  1.00 77.33           N  
ATOM    990  CA  VAL A 136       9.912  55.439  -4.204  1.00 71.10           C  
ATOM    991  C   VAL A 136       9.800  54.438  -3.063  1.00 62.42           C  
ATOM    992  O   VAL A 136       9.981  54.798  -1.896  1.00 59.33           O  
ATOM    993  CB  VAL A 136       8.533  55.514  -4.915  1.00 73.50           C  
ATOM    994  CG1 VAL A 136       7.452  55.986  -3.945  1.00 73.64           C  
ATOM    995  CG2 VAL A 136       8.604  56.446  -6.095  1.00 86.03           C  
ATOM    996  N   TRP A 137       9.521  53.181  -3.425  1.00 55.02           N  
ATOM    997  CA  TRP A 137       9.376  52.095  -2.458  1.00 43.51           C  
ATOM    998  C   TRP A 137      10.691  51.844  -1.725  1.00 50.14           C  
ATOM    999  O   TRP A 137      10.683  51.591  -0.517  1.00 56.31           O  
ATOM   1000  CB  TRP A 137       8.916  50.804  -3.137  1.00 26.56           C  
ATOM   1001  CG  TRP A 137       7.723  50.973  -4.015  1.00 37.56           C  
ATOM   1002  CD1 TRP A 137       7.694  50.855  -5.368  1.00 31.50           C  
ATOM   1003  CD2 TRP A 137       6.390  51.347  -3.616  1.00 32.13           C  
ATOM   1004  NE1 TRP A 137       6.432  51.144  -5.845  1.00 31.14           N  
ATOM   1005  CE2 TRP A 137       5.615  51.455  -4.789  1.00 32.65           C  
ATOM   1006  CE3 TRP A 137       5.781  51.612  -2.384  1.00 37.29           C  
ATOM   1007  CZ2 TRP A 137       4.260  51.819  -4.769  1.00 24.85           C  
ATOM   1008  CZ3 TRP A 137       4.426  51.973  -2.366  1.00 25.53           C  
ATOM   1009  CH2 TRP A 137       3.687  52.075  -3.554  1.00 22.35           C  
ATOM   1010  N   TRP A 138      11.818  51.927  -2.437  1.00 42.83           N  
ATOM   1011  CA  TRP A 138      13.110  51.707  -1.787  1.00 47.38           C  
ATOM   1012  C   TRP A 138      13.231  52.697  -0.621  1.00 51.03           C  
ATOM   1013  O   TRP A 138      13.737  52.346   0.449  1.00 61.45           O  
ATOM   1014  CB  TRP A 138      14.283  51.849  -2.774  1.00 42.76           C  
ATOM   1015  CG  TRP A 138      15.633  51.641  -2.129  1.00 49.66           C  
ATOM   1016  CD1 TRP A 138      16.336  50.467  -2.042  1.00 47.45           C  
ATOM   1017  CD2 TRP A 138      16.407  52.621  -1.424  1.00 57.54           C  
ATOM   1018  NE1 TRP A 138      17.488  50.654  -1.321  1.00 39.50           N  
ATOM   1019  CE2 TRP A 138      17.555  51.966  -0.923  1.00 58.40           C  
ATOM   1020  CE3 TRP A 138      16.234  53.991  -1.155  1.00 54.09           C  
ATOM   1021  CZ2 TRP A 138      18.529  52.633  -0.164  1.00 65.75           C  
ATOM   1022  CZ3 TRP A 138      17.199  54.651  -0.404  1.00 51.59           C  
ATOM   1023  CH2 TRP A 138      18.334  53.970   0.085  1.00 59.72           C  
ATOM   1024  N   ALA A 139      12.704  53.907  -0.816  1.00 48.64           N  
ATOM   1025  CA  ALA A 139      12.716  54.948   0.219  1.00 49.28           C  
ATOM   1026  C   ALA A 139      11.756  54.616   1.377  1.00 49.90           C  
ATOM   1027  O   ALA A 139      12.092  54.794   2.554  1.00 44.78           O  
ATOM   1028  CB  ALA A 139      12.337  56.294  -0.390  1.00 46.23           C  
ATOM   1029  N   ILE A 140      10.558  54.148   1.034  1.00 48.84           N  
ATOM   1030  CA  ILE A 140       9.563  53.804   2.037  1.00 56.33           C  
ATOM   1031  C   ILE A 140      10.063  52.636   2.882  1.00 63.17           C  
ATOM   1032  O   ILE A 140       9.821  52.582   4.091  1.00 72.46           O  
ATOM   1033  CB  ILE A 140       8.209  53.458   1.384  1.00 61.59           C  
ATOM   1034  CG1 ILE A 140       7.625  54.705   0.706  1.00 69.76           C  
ATOM   1035  CG2 ILE A 140       7.239  52.913   2.422  1.00 66.00           C  
ATOM   1036  CD1 ILE A 140       6.288  54.477  -0.012  1.00 71.35           C  
ATOM   1037  N   SER A 141      10.793  51.724   2.247  1.00 60.25           N  
ATOM   1038  CA  SER A 141      11.340  50.562   2.941  1.00 59.00           C  
ATOM   1039  C   SER A 141      12.571  50.918   3.774  1.00 63.26           C  
ATOM   1040  O   SER A 141      12.893  50.228   4.746  1.00 58.62           O  
ATOM   1041  CB  SER A 141      11.660  49.459   1.942  1.00 55.12           C  
ATOM   1042  OG  SER A 141      10.460  48.987   1.364  1.00 46.61           O  
ATOM   1043  N   THR A 142      13.270  51.979   3.373  1.00 61.34           N  
ATOM   1044  CA  THR A 142      14.431  52.436   4.117  1.00 60.06           C  
ATOM   1045  C   THR A 142      13.939  53.184   5.352  1.00 58.36           C  
ATOM   1046  O   THR A 142      14.486  53.013   6.448  1.00 54.98           O  
ATOM   1047  CB  THR A 142      15.312  53.366   3.294  1.00 60.33           C  
ATOM   1048  OG1 THR A 142      15.855  52.646   2.182  1.00 67.43           O  
ATOM   1049  CG2 THR A 142      16.451  53.911   4.159  1.00 59.66           C  
ATOM   1050  N   ALA A 143      12.916  54.021   5.169  1.00 54.19           N  
ATOM   1051  CA  ALA A 143      12.353  54.772   6.286  1.00 57.09           C  
ATOM   1052  C   ALA A 143      11.736  53.774   7.259  1.00 51.96           C  
ATOM   1053  O   ALA A 143      11.699  54.006   8.464  1.00 56.78           O  
ATOM   1054  CB  ALA A 143      11.308  55.778   5.805  1.00 56.53           C  
ATOM   1055  N   ALA A 144      11.282  52.646   6.725  1.00 49.40           N  
ATOM   1056  CA  ALA A 144      10.695  51.593   7.544  1.00 47.74           C  
ATOM   1057  C   ALA A 144      11.790  50.902   8.364  1.00 43.63           C  
ATOM   1058  O   ALA A 144      11.559  50.471   9.493  1.00 45.05           O  
ATOM   1059  CB  ALA A 144       9.971  50.574   6.654  1.00 57.61           C  
ATOM   1060  N   MET A 145      12.987  50.824   7.789  1.00 46.86           N  
ATOM   1061  CA  MET A 145      14.128  50.189   8.443  1.00 44.86           C  
ATOM   1062  C   MET A 145      14.800  51.072   9.507  1.00 45.68           C  
ATOM   1063  O   MET A 145      15.155  50.583  10.585  1.00 39.06           O  
ATOM   1064  CB  MET A 145      15.139  49.721   7.403  1.00 47.19           C  
ATOM   1065  CG  MET A 145      16.286  48.928   7.963  1.00 55.35           C  
ATOM   1066  SD  MET A 145      17.559  48.749   6.717  1.00 71.57           S  
ATOM   1067  CE  MET A 145      18.656  50.136   7.123  1.00 56.05           C  
ATOM   1068  N   LEU A 146      14.968  52.362   9.212  1.00 45.85           N  
ATOM   1069  CA  LEU A 146      15.571  53.289  10.174  1.00 48.30           C  
ATOM   1070  C   LEU A 146      14.745  53.289  11.456  1.00 49.45           C  
ATOM   1071  O   LEU A 146      15.289  53.394  12.550  1.00 49.13           O  
ATOM   1072  CB  LEU A 146      15.633  54.711   9.593  1.00 57.53           C  
ATOM   1073  CG  LEU A 146      16.261  55.900  10.359  1.00 63.72           C  
ATOM   1074  CD1 LEU A 146      15.371  56.372  11.520  1.00 55.27           C  
ATOM   1075  CD2 LEU A 146      17.670  55.552  10.847  1.00 65.17           C  
ATOM   1076  N   TYR A 147      13.428  53.196  11.298  1.00 50.16           N  
ATOM   1077  CA  TYR A 147      12.485  53.163  12.414  1.00 55.83           C  
ATOM   1078  C   TYR A 147      12.883  52.088  13.443  1.00 51.38           C  
ATOM   1079  O   TYR A 147      12.906  52.342  14.653  1.00 41.11           O  
ATOM   1080  CB  TYR A 147      11.069  52.888  11.869  1.00 59.36           C  
ATOM   1081  CG  TYR A 147       9.990  52.865  12.916  1.00 61.45           C  
ATOM   1082  CD1 TYR A 147       9.439  54.055  13.402  1.00 67.62           C  
ATOM   1083  CD2 TYR A 147       9.566  51.661  13.471  1.00 60.45           C  
ATOM   1084  CE1 TYR A 147       8.494  54.050  14.430  1.00 71.59           C  
ATOM   1085  CE2 TYR A 147       8.619  51.639  14.507  1.00 72.40           C  
ATOM   1086  CZ  TYR A 147       8.092  52.839  14.983  1.00 73.06           C  
ATOM   1087  OH  TYR A 147       7.200  52.825  16.026  1.00 68.44           O  
ATOM   1088  N   ILE A 148      13.218  50.902  12.930  1.00 57.00           N  
ATOM   1089  CA  ILE A 148      13.617  49.749  13.735  1.00 52.59           C  
ATOM   1090  C   ILE A 148      14.936  50.000  14.418  1.00 51.28           C  
ATOM   1091  O   ILE A 148      15.153  49.515  15.527  1.00 48.67           O  
ATOM   1092  CB  ILE A 148      13.821  48.485  12.872  1.00 48.68           C  
ATOM   1093  CG1 ILE A 148      12.606  48.236  11.995  1.00 45.12           C  
ATOM   1094  CG2 ILE A 148      14.108  47.281  13.755  1.00 47.63           C  
ATOM   1095  CD1 ILE A 148      12.964  48.172  10.569  1.00 45.19           C  
ATOM   1096  N   LEU A 149      15.838  50.687  13.716  1.00 50.58           N  
ATOM   1097  CA  LEU A 149      17.159  51.001  14.260  1.00 56.98           C  
ATOM   1098  C   LEU A 149      16.996  51.988  15.409  1.00 59.11           C  
ATOM   1099  O   LEU A 149      17.735  51.939  16.390  1.00 55.15           O  
ATOM   1100  CB  LEU A 149      18.083  51.575  13.177  1.00 52.32           C  
ATOM   1101  CG  LEU A 149      18.332  50.768  11.886  1.00 54.91           C  
ATOM   1102  CD1 LEU A 149      19.469  51.441  11.124  1.00 47.81           C  
ATOM   1103  CD2 LEU A 149      18.660  49.273  12.146  1.00 34.22           C  
ATOM   1104  N   TYR A 150      15.983  52.845  15.295  1.00 64.91           N  
ATOM   1105  CA  TYR A 150      15.667  53.831  16.324  1.00 71.26           C  
ATOM   1106  C   TYR A 150      15.183  53.032  17.528  1.00 75.58           C  
ATOM   1107  O   TYR A 150      15.786  53.082  18.595  1.00 78.59           O  
ATOM   1108  CB  TYR A 150      14.553  54.757  15.840  1.00 68.67           C  
ATOM   1109  CG  TYR A 150      14.501  56.093  16.529  1.00 70.09           C  
ATOM   1110  CD1 TYR A 150      15.495  57.040  16.323  1.00 80.53           C  
ATOM   1111  CD2 TYR A 150      13.457  56.416  17.382  1.00 76.67           C  
ATOM   1112  CE1 TYR A 150      15.454  58.282  16.958  1.00 87.52           C  
ATOM   1113  CE2 TYR A 150      13.405  57.651  18.023  1.00 83.80           C  
ATOM   1114  CZ  TYR A 150      14.406  58.578  17.810  1.00 85.64           C  
ATOM   1115  OH  TYR A 150      14.373  59.785  18.477  1.00 88.87           O  
ATOM   1116  N   VAL A 151      14.140  52.231  17.319  1.00 78.07           N  
ATOM   1117  CA  VAL A 151      13.571  51.393  18.373  1.00 78.49           C  
ATOM   1118  C   VAL A 151      14.589  50.394  18.934  1.00 79.24           C  
ATOM   1119  O   VAL A 151      14.587  50.106  20.128  1.00 79.32           O  
ATOM   1120  CB  VAL A 151      12.312  50.630  17.872  1.00 75.35           C  
ATOM   1121  CG1 VAL A 151      11.773  49.708  18.960  1.00 75.45           C  
ATOM   1122  CG2 VAL A 151      11.238  51.612  17.454  1.00 73.02           C  
ATOM   1123  N   LEU A 152      15.471  49.891  18.077  1.00 81.48           N  
ATOM   1124  CA  LEU A 152      16.473  48.931  18.508  1.00 88.81           C  
ATOM   1125  C   LEU A 152      17.512  49.560  19.428  1.00 96.71           C  
ATOM   1126  O   LEU A 152      17.699  49.085  20.548  1.00100.34           O  
ATOM   1127  CB  LEU A 152      17.146  48.263  17.308  1.00 90.28           C  
ATOM   1128  CG  LEU A 152      17.122  46.730  17.287  1.00 92.17           C  
ATOM   1129  CD1 LEU A 152      15.689  46.231  17.323  1.00 93.83           C  
ATOM   1130  CD2 LEU A 152      17.827  46.202  16.048  1.00 91.40           C  
ATOM   1131  N   PHE A 153      18.186  50.621  18.981  1.00103.17           N  
ATOM   1132  CA  PHE A 153      19.190  51.250  19.840  1.00109.81           C  
ATOM   1133  C   PHE A 153      18.712  52.446  20.667  1.00111.00           C  
ATOM   1134  O   PHE A 153      19.469  53.386  20.929  1.00112.38           O  
ATOM   1135  CB  PHE A 153      20.510  51.545  19.092  1.00115.60           C  
ATOM   1136  CG  PHE A 153      20.353  52.316  17.807  1.00122.08           C  
ATOM   1137  CD1 PHE A 153      19.893  53.632  17.808  1.00123.97           C  
ATOM   1138  CD2 PHE A 153      20.722  51.739  16.595  1.00124.28           C  
ATOM   1139  CE1 PHE A 153      19.803  54.363  16.619  1.00125.48           C  
ATOM   1140  CE2 PHE A 153      20.637  52.461  15.404  1.00128.71           C  
ATOM   1141  CZ  PHE A 153      20.176  53.778  15.416  1.00127.67           C  
ATOM   1142  N   PHE A 154      17.460  52.372  21.111  1.00112.63           N  
ATOM   1143  CA  PHE A 154      16.842  53.406  21.938  1.00117.10           C  
ATOM   1144  C   PHE A 154      15.908  52.735  22.939  1.00119.95           C  
ATOM   1145  O   PHE A 154      16.123  52.806  24.150  1.00119.76           O  
ATOM   1146  CB  PHE A 154      16.036  54.405  21.090  1.00118.98           C  
ATOM   1147  CG  PHE A 154      16.852  55.538  20.529  1.00121.77           C  
ATOM   1148  CD1 PHE A 154      17.488  55.417  19.299  1.00123.65           C  
ATOM   1149  CD2 PHE A 154      16.971  56.734  21.227  1.00124.95           C  
ATOM   1150  CE1 PHE A 154      18.233  56.468  18.773  1.00124.84           C  
ATOM   1151  CE2 PHE A 154      17.716  57.794  20.710  1.00126.42           C  
ATOM   1152  CZ  PHE A 154      18.346  57.659  19.478  1.00127.02           C  
ATOM   1153  N   GLY A 155      14.876  52.074  22.416  1.00123.05           N  
ATOM   1154  CA  GLY A 155      13.900  51.398  23.254  1.00126.63           C  
ATOM   1155  C   GLY A 155      14.424  50.144  23.926  1.00129.22           C  
ATOM   1156  O   GLY A 155      14.097  49.874  25.081  1.00131.30           O  
ATOM   1157  N   PHE A 156      15.223  49.370  23.199  1.00129.85           N  
ATOM   1158  CA  PHE A 156      15.796  48.139  23.735  1.00130.83           C  
ATOM   1159  C   PHE A 156      16.893  48.444  24.753  1.00129.53           C  
ATOM   1160  O   PHE A 156      16.964  47.809  25.802  1.00129.67           O  
ATOM   1161  CB  PHE A 156      16.358  47.266  22.603  1.00134.25           C  
ATOM   1162  CG  PHE A 156      15.302  46.623  21.739  1.00133.53           C  
ATOM   1163  CD1 PHE A 156      14.397  47.394  21.020  1.00133.96           C  
ATOM   1164  CD2 PHE A 156      15.215  45.240  21.649  1.00134.39           C  
ATOM   1165  CE1 PHE A 156      13.421  46.798  20.224  1.00134.83           C  
ATOM   1166  CE2 PHE A 156      14.243  44.632  20.857  1.00134.98           C  
ATOM   1167  CZ  PHE A 156      13.343  45.413  20.143  1.00134.63           C  
ATOM   1168  N   THR A 157      17.728  49.432  24.441  1.00143.83           N  
ATOM   1169  CA  THR A 157      18.830  49.837  25.314  1.00144.89           C  
ATOM   1170  C   THR A 157      18.326  50.388  26.647  1.00145.06           C  
ATOM   1171  O   THR A 157      18.928  50.152  27.695  1.00146.38           O  
ATOM   1172  CB  THR A 157      19.709  50.919  24.648  1.00145.52           C  
ATOM   1173  OG1 THR A 157      19.001  52.166  24.617  1.00147.91           O  
ATOM   1174  CG2 THR A 157      20.064  50.518  23.230  1.00142.94           C  
ATOM   1175  N   SER A 158      17.226  51.133  26.594  1.00144.40           N  
ATOM   1176  CA  SER A 158      16.625  51.722  27.785  1.00144.18           C  
ATOM   1177  C   SER A 158      15.844  50.675  28.585  1.00144.08           C  
ATOM   1178  O   SER A 158      14.947  50.997  29.368  1.00144.15           O  
ATOM   1179  CB  SER A 158      15.709  52.880  27.382  1.00145.57           C  
ATOM   1180  OG  SER A 158      16.421  53.852  26.635  1.00146.21           O  
ATOM   1181  N   LYS A 159      16.202  49.411  28.367  1.00143.48           N  
ATOM   1182  CA  LYS A 159      15.592  48.260  29.033  1.00141.86           C  
ATOM   1183  C   LYS A 159      16.615  47.129  29.135  1.00142.52           C  
ATOM   1184  O   LYS A 159      16.386  46.129  29.813  1.00142.58           O  
ATOM   1185  CB  LYS A 159      14.377  47.770  28.235  1.00137.96           C  
ATOM   1186  CG  LYS A 159      13.048  48.384  28.642  1.00130.82           C  
ATOM   1187  CD  LYS A 159      12.509  47.739  29.914  1.00127.12           C  
ATOM   1188  CE  LYS A 159      11.106  48.244  30.242  1.00120.34           C  
ATOM   1189  NZ  LYS A 159      10.482  47.580  31.422  1.00108.72           N  
ATOM   1190  N   ALA A 160      17.744  47.291  28.427  1.00142.89           N  
ATOM   1191  CA  ALA A 160      18.817  46.303  28.417  1.00143.31           C  
ATOM   1192  C   ALA A 160      19.638  46.326  29.707  1.00144.98           C  
ATOM   1193  O   ALA A 160      20.399  47.266  29.961  1.00144.98           O  
ATOM   1194  CB  ALA A 160      19.729  46.536  27.220  1.00142.81           C  
ATOM   1195  N   GLU A 161      19.482  45.269  30.502  1.00146.01           N  
ATOM   1196  CA  GLU A 161      20.167  45.097  31.785  1.00146.81           C  
ATOM   1197  C   GLU A 161      19.582  43.827  32.396  1.00147.67           C  
ATOM   1198  O   GLU A 161      20.214  42.767  32.386  1.00149.10           O  
ATOM   1199  CB  GLU A 161      19.896  46.291  32.708  1.00145.78           C  
ATOM   1200  CG  GLU A 161      21.141  47.025  33.167  1.00146.27           C  
ATOM   1201  CD  GLU A 161      21.983  46.202  34.117  1.00148.26           C  
ATOM   1202  OE1 GLU A 161      21.566  46.041  35.285  1.00150.41           O  
ATOM   1203  OE2 GLU A 161      23.056  45.716  33.696  1.00148.93           O  
ATOM   1204  N   SER A 162      18.364  43.956  32.914  1.00136.87           N  
ATOM   1205  CA  SER A 162      17.612  42.855  33.509  1.00137.72           C  
ATOM   1206  C   SER A 162      18.305  42.027  34.590  1.00135.19           C  
ATOM   1207  O   SER A 162      18.065  40.821  34.694  1.00137.18           O  
ATOM   1208  CB  SER A 162      17.083  41.930  32.407  1.00142.06           C  
ATOM   1209  OG  SER A 162      16.260  42.638  31.497  1.00147.32           O  
ATOM   1210  N   MET A 163      19.159  42.665  35.387  1.00130.94           N  
ATOM   1211  CA  MET A 163      19.868  41.986  36.478  1.00129.06           C  
ATOM   1212  C   MET A 163      20.866  40.920  35.991  1.00127.62           C  
ATOM   1213  O   MET A 163      21.635  40.365  36.782  1.00126.87           O  
ATOM   1214  CB  MET A 163      18.842  41.366  37.449  1.00126.80           C  
ATOM   1215  CG  MET A 163      19.379  40.967  38.816  1.00121.73           C  
ATOM   1216  SD  MET A 163      19.808  42.375  39.840  1.00116.15           S  
ATOM   1217  CE  MET A 163      21.562  42.511  39.510  1.00119.50           C  
ATOM   1218  N   ARG A 164      20.851  40.646  34.688  1.00124.27           N  
ATOM   1219  CA  ARG A 164      21.744  39.659  34.089  1.00122.98           C  
ATOM   1220  C   ARG A 164      22.650  40.352  33.077  1.00123.98           C  
ATOM   1221  O   ARG A 164      22.190  40.801  32.024  1.00121.18           O  
ATOM   1222  CB  ARG A 164      20.938  38.561  33.395  1.00122.65           C  
ATOM   1223  CG  ARG A 164      19.937  37.870  34.296  1.00123.22           C  
ATOM   1224  CD  ARG A 164      20.637  37.098  35.392  1.00124.44           C  
ATOM   1225  NE  ARG A 164      19.798  36.974  36.580  1.00125.45           N  
ATOM   1226  CZ  ARG A 164      19.785  35.918  37.384  1.00127.22           C  
ATOM   1227  NH1 ARG A 164      20.562  34.871  37.134  1.00125.74           N  
ATOM   1228  NH2 ARG A 164      19.023  35.930  38.468  1.00130.07           N  
ATOM   1229  N   PRO A 165      23.959  40.433  33.379  1.00125.13           N  
ATOM   1230  CA  PRO A 165      24.937  41.077  32.496  1.00125.02           C  
ATOM   1231  C   PRO A 165      25.031  40.408  31.133  1.00123.87           C  
ATOM   1232  O   PRO A 165      25.264  41.077  30.131  1.00124.96           O  
ATOM   1233  CB  PRO A 165      26.241  40.946  33.282  1.00124.89           C  
ATOM   1234  CG  PRO A 165      26.048  39.673  34.047  1.00124.39           C  
ATOM   1235  CD  PRO A 165      24.629  39.817  34.540  1.00125.60           C  
ATOM   1236  N   GLU A 166      24.820  39.094  31.104  1.00123.77           N  
ATOM   1237  CA  GLU A 166      24.878  38.322  29.863  1.00122.32           C  
ATOM   1238  C   GLU A 166      23.760  38.728  28.901  1.00118.75           C  
ATOM   1239  O   GLU A 166      24.026  39.298  27.844  1.00116.56           O  
ATOM   1240  CB  GLU A 166      24.789  36.816  30.149  1.00119.91           C  
ATOM   1241  CG  GLU A 166      25.788  36.287  31.181  1.00117.55           C  
ATOM   1242  CD  GLU A 166      25.271  36.336  32.614  1.00114.90           C  
ATOM   1243  OE1 GLU A 166      24.057  36.548  32.821  1.00114.46           O  
ATOM   1244  OE2 GLU A 166      26.084  36.145  33.539  1.00113.24           O  
ATOM   1245  N   VAL A 167      22.514  38.485  29.302  1.00113.42           N  
ATOM   1246  CA  VAL A 167      21.347  38.812  28.484  1.00106.52           C  
ATOM   1247  C   VAL A 167      21.264  40.303  28.143  1.00 99.60           C  
ATOM   1248  O   VAL A 167      20.315  40.746  27.496  1.00101.52           O  
ATOM   1249  CB  VAL A 167      20.031  38.368  29.183  1.00111.11           C  
ATOM   1250  CG1 VAL A 167      19.636  39.354  30.272  1.00115.81           C  
ATOM   1251  CG2 VAL A 167      18.917  38.215  28.174  1.00114.58           C  
ATOM   1252  N   ALA A 168      22.270  41.063  28.570  1.00 94.65           N  
ATOM   1253  CA  ALA A 168      22.330  42.498  28.322  1.00 88.93           C  
ATOM   1254  C   ALA A 168      23.572  42.909  27.530  1.00 85.17           C  
ATOM   1255  O   ALA A 168      23.548  43.916  26.817  1.00 82.31           O  
ATOM   1256  CB  ALA A 168      22.271  43.255  29.636  1.00 85.95           C  
ATOM   1257  N   SER A 169      24.661  42.158  27.687  1.00 82.62           N  
ATOM   1258  CA  SER A 169      25.898  42.449  26.967  1.00 84.30           C  
ATOM   1259  C   SER A 169      26.071  41.497  25.786  1.00 90.04           C  
ATOM   1260  O   SER A 169      26.743  41.827  24.804  1.00 92.02           O  
ATOM   1261  CB  SER A 169      27.123  42.422  27.899  1.00 74.90           C  
ATOM   1262  OG  SER A 169      27.281  41.184  28.570  1.00 56.36           O  
ATOM   1263  N   THR A 170      25.462  40.317  25.885  1.00 98.04           N  
ATOM   1264  CA  THR A 170      25.520  39.335  24.804  1.00100.28           C  
ATOM   1265  C   THR A 170      24.389  39.661  23.823  1.00102.18           C  
ATOM   1266  O   THR A 170      24.118  38.909  22.880  1.00100.36           O  
ATOM   1267  CB  THR A 170      25.391  37.878  25.324  1.00103.98           C  
ATOM   1268  OG1 THR A 170      24.102  37.681  25.919  1.00107.71           O  
ATOM   1269  CG2 THR A 170      26.482  37.578  26.352  1.00101.53           C  
ATOM   1270  N   PHE A 171      23.731  40.788  24.096  1.00101.27           N  
ATOM   1271  CA  PHE A 171      22.638  41.342  23.297  1.00 99.82           C  
ATOM   1272  C   PHE A 171      23.232  42.539  22.546  1.00 99.16           C  
ATOM   1273  O   PHE A 171      22.789  42.897  21.457  1.00 99.53           O  
ATOM   1274  CB  PHE A 171      21.491  41.795  24.214  1.00100.38           C  
ATOM   1275  CG  PHE A 171      20.443  42.628  23.524  1.00101.30           C  
ATOM   1276  CD1 PHE A 171      19.739  42.129  22.429  1.00102.06           C  
ATOM   1277  CD2 PHE A 171      20.183  43.931  23.946  1.00 97.72           C  
ATOM   1278  CE1 PHE A 171      18.796  42.918  21.765  1.00100.37           C  
ATOM   1279  CE2 PHE A 171      19.241  44.727  23.287  1.00 92.77           C  
ATOM   1280  CZ  PHE A 171      18.549  44.221  22.195  1.00 93.90           C  
ATOM   1281  N   LYS A 172      24.238  43.153  23.156  1.00 95.97           N  
ATOM   1282  CA  LYS A 172      24.946  44.283  22.572  1.00 96.49           C  
ATOM   1283  C   LYS A 172      25.684  43.759  21.338  1.00 98.58           C  
ATOM   1284  O   LYS A 172      25.681  44.404  20.288  1.00102.95           O  
ATOM   1285  CB  LYS A 172      25.935  44.832  23.605  1.00 98.56           C  
ATOM   1286  CG  LYS A 172      26.799  46.012  23.194  1.00 93.53           C  
ATOM   1287  CD  LYS A 172      27.656  46.410  24.394  1.00 95.95           C  
ATOM   1288  CE  LYS A 172      28.802  47.342  24.029  1.00 99.50           C  
ATOM   1289  NZ  LYS A 172      29.734  47.552  25.187  1.00 93.24           N  
ATOM   1290  N   VAL A 173      26.279  42.568  21.467  1.00 93.73           N  
ATOM   1291  CA  VAL A 173      27.008  41.925  20.371  1.00 85.54           C  
ATOM   1292  C   VAL A 173      26.030  41.548  19.256  1.00 80.55           C  
ATOM   1293  O   VAL A 173      26.416  41.400  18.094  1.00 73.59           O  
ATOM   1294  CB  VAL A 173      27.787  40.668  20.867  1.00 88.19           C  
ATOM   1295  CG1 VAL A 173      26.838  39.654  21.478  1.00 87.90           C  
ATOM   1296  CG2 VAL A 173      28.587  40.037  19.726  1.00 90.78           C  
ATOM   1297  N   LEU A 174      24.758  41.420  19.630  1.00 77.32           N  
ATOM   1298  CA  LEU A 174      23.685  41.092  18.701  1.00 76.05           C  
ATOM   1299  C   LEU A 174      23.340  42.369  17.946  1.00 79.16           C  
ATOM   1300  O   LEU A 174      23.146  42.356  16.731  1.00 83.19           O  
ATOM   1301  CB  LEU A 174      22.455  40.620  19.471  1.00 72.69           C  
ATOM   1302  CG  LEU A 174      21.561  39.605  18.768  1.00 76.37           C  
ATOM   1303  CD1 LEU A 174      22.212  38.227  18.824  1.00 73.44           C  
ATOM   1304  CD2 LEU A 174      20.204  39.570  19.448  1.00 85.26           C  
ATOM   1305  N   ARG A 175      23.286  43.474  18.687  1.00 86.29           N  
ATOM   1306  CA  ARG A 175      22.977  44.788  18.133  1.00 83.43           C  
ATOM   1307  C   ARG A 175      24.034  45.205  17.114  1.00 76.78           C  
ATOM   1308  O   ARG A 175      23.718  45.843  16.116  1.00 80.23           O  
ATOM   1309  CB  ARG A 175      22.886  45.826  19.256  1.00 86.89           C  
ATOM   1310  CG  ARG A 175      22.365  47.189  18.821  1.00 89.25           C  
ATOM   1311  CD  ARG A 175      22.424  48.182  19.967  1.00 92.43           C  
ATOM   1312  NE  ARG A 175      21.682  47.706  21.129  1.00101.56           N  
ATOM   1313  CZ  ARG A 175      22.007  47.980  22.388  1.00108.74           C  
ATOM   1314  NH1 ARG A 175      23.068  48.733  22.655  1.00112.85           N  
ATOM   1315  NH2 ARG A 175      21.267  47.509  23.382  1.00107.26           N  
ATOM   1316  N   ASN A 176      25.287  44.842  17.370  1.00 67.53           N  
ATOM   1317  CA  ASN A 176      26.378  45.166  16.450  1.00 72.26           C  
ATOM   1318  C   ASN A 176      26.204  44.343  15.178  1.00 72.73           C  
ATOM   1319  O   ASN A 176      26.279  44.865  14.065  1.00 74.19           O  
ATOM   1320  CB  ASN A 176      27.728  44.843  17.089  1.00 70.50           C  
ATOM   1321  CG  ASN A 176      27.907  45.518  18.422  1.00 68.65           C  
ATOM   1322  OD1 ASN A 176      27.029  46.253  18.881  1.00 73.70           O  
ATOM   1323  ND2 ASN A 176      29.043  45.268  19.064  1.00 74.58           N  
ATOM   1324  N   VAL A 177      25.971  43.048  15.369  1.00 78.00           N  
ATOM   1325  CA  VAL A 177      25.750  42.119  14.276  1.00 75.93           C  
ATOM   1326  C   VAL A 177      24.595  42.628  13.424  1.00 80.34           C  
ATOM   1327  O   VAL A 177      24.777  42.875  12.239  1.00 86.83           O  
ATOM   1328  CB  VAL A 177      25.394  40.717  14.817  1.00 83.83           C  
ATOM   1329  CG1 VAL A 177      24.869  39.819  13.697  1.00 83.94           C  
ATOM   1330  CG2 VAL A 177      26.614  40.093  15.471  1.00 81.12           C  
ATOM   1331  N   THR A 178      23.442  42.861  14.053  1.00 78.19           N  
ATOM   1332  CA  THR A 178      22.251  43.328  13.348  1.00 69.84           C  
ATOM   1333  C   THR A 178      22.376  44.690  12.676  1.00 62.84           C  
ATOM   1334  O   THR A 178      22.094  44.804  11.484  1.00 58.41           O  
ATOM   1335  CB  THR A 178      21.000  43.310  14.258  1.00 70.80           C  
ATOM   1336  OG1 THR A 178      20.798  41.984  14.763  1.00 72.44           O  
ATOM   1337  CG2 THR A 178      19.758  43.713  13.472  1.00 77.10           C  
ATOM   1338  N   VAL A 179      22.808  45.708  13.421  1.00 64.67           N  
ATOM   1339  CA  VAL A 179      22.945  47.067  12.872  1.00 67.82           C  
ATOM   1340  C   VAL A 179      23.827  47.167  11.627  1.00 68.49           C  
ATOM   1341  O   VAL A 179      23.407  47.750  10.623  1.00 68.16           O  
ATOM   1342  CB  VAL A 179      23.409  48.096  13.947  1.00 69.76           C  
ATOM   1343  CG1 VAL A 179      23.879  49.408  13.292  1.00 64.74           C  
ATOM   1344  CG2 VAL A 179      22.257  48.380  14.917  1.00 67.45           C  
ATOM   1345  N   VAL A 180      25.033  46.605  11.682  1.00 63.22           N  
ATOM   1346  CA  VAL A 180      25.922  46.640  10.518  1.00 60.18           C  
ATOM   1347  C   VAL A 180      25.334  45.767   9.407  1.00 55.61           C  
ATOM   1348  O   VAL A 180      25.370  46.133   8.234  1.00 49.22           O  
ATOM   1349  CB  VAL A 180      27.355  46.157  10.865  1.00 61.65           C  
ATOM   1350  CG1 VAL A 180      27.772  46.691  12.230  1.00 59.85           C  
ATOM   1351  CG2 VAL A 180      27.457  44.646  10.820  1.00 50.87           C  
ATOM   1352  N   LEU A 181      24.725  44.654   9.821  1.00 54.49           N  
ATOM   1353  CA  LEU A 181      24.093  43.673   8.943  1.00 53.06           C  
ATOM   1354  C   LEU A 181      22.988  44.251   8.073  1.00 58.35           C  
ATOM   1355  O   LEU A 181      23.036  44.102   6.847  1.00 54.90           O  
ATOM   1356  CB  LEU A 181      23.506  42.526   9.777  1.00 43.68           C  
ATOM   1357  CG  LEU A 181      24.099  41.130   9.621  1.00 43.06           C  
ATOM   1358  CD1 LEU A 181      23.782  40.602   8.236  1.00 48.40           C  
ATOM   1359  CD2 LEU A 181      25.590  41.176   9.853  1.00 40.76           C  
ATOM   1360  N   TRP A 182      21.991  44.873   8.717  1.00 61.35           N  
ATOM   1361  CA  TRP A 182      20.834  45.467   8.032  1.00 56.28           C  
ATOM   1362  C   TRP A 182      21.130  46.757   7.278  1.00 55.68           C  
ATOM   1363  O   TRP A 182      20.482  47.050   6.278  1.00 55.20           O  
ATOM   1364  CB  TRP A 182      19.666  45.679   8.995  1.00 58.59           C  
ATOM   1365  CG  TRP A 182      18.966  44.422   9.420  1.00 66.29           C  
ATOM   1366  CD1 TRP A 182      19.402  43.141   9.257  1.00 77.83           C  
ATOM   1367  CD2 TRP A 182      17.727  44.335  10.129  1.00 73.24           C  
ATOM   1368  NE1 TRP A 182      18.519  42.258   9.831  1.00 71.09           N  
ATOM   1369  CE2 TRP A 182      17.480  42.965  10.375  1.00 73.20           C  
ATOM   1370  CE3 TRP A 182      16.799  45.282  10.586  1.00 80.47           C  
ATOM   1371  CZ2 TRP A 182      16.344  42.517  11.058  1.00 74.46           C  
ATOM   1372  CZ3 TRP A 182      15.666  44.835  11.268  1.00 80.10           C  
ATOM   1373  CH2 TRP A 182      15.452  43.466  11.496  1.00 76.55           C  
ATOM   1374  N   SER A 183      22.076  47.548   7.772  1.00 40.39           N  
ATOM   1375  CA  SER A 183      22.471  48.771   7.070  1.00 48.56           C  
ATOM   1376  C   SER A 183      22.939  48.369   5.662  1.00 51.28           C  
ATOM   1377  O   SER A 183      22.904  49.167   4.730  1.00 60.78           O  
ATOM   1378  CB  SER A 183      23.645  49.459   7.814  1.00 60.05           C  
ATOM   1379  OG  SER A 183      24.341  50.421   7.013  1.00 42.05           O  
ATOM   1380  N   ALA A 184      23.338  47.109   5.524  1.00 46.21           N  
ATOM   1381  CA  ALA A 184      23.863  46.576   4.281  1.00 44.67           C  
ATOM   1382  C   ALA A 184      22.887  46.433   3.140  1.00 47.41           C  
ATOM   1383  O   ALA A 184      23.098  47.021   2.076  1.00 49.31           O  
ATOM   1384  CB  ALA A 184      24.558  45.244   4.542  1.00 50.78           C  
ATOM   1385  N   TYR A 185      21.827  45.653   3.366  1.00 43.65           N  
ATOM   1386  CA  TYR A 185      20.805  45.375   2.350  1.00 39.62           C  
ATOM   1387  C   TYR A 185      20.438  46.564   1.469  1.00 41.94           C  
ATOM   1388  O   TYR A 185      20.665  46.520   0.262  1.00 46.04           O  
ATOM   1389  CB  TYR A 185      19.552  44.741   2.972  1.00 37.75           C  
ATOM   1390  CG  TYR A 185      19.790  43.379   3.591  1.00 33.43           C  
ATOM   1391  CD1 TYR A 185      20.313  43.260   4.876  1.00 45.24           C  
ATOM   1392  CD2 TYR A 185      19.550  42.210   2.871  1.00 39.26           C  
ATOM   1393  CE1 TYR A 185      20.599  42.017   5.426  1.00 44.93           C  
ATOM   1394  CE2 TYR A 185      19.837  40.959   3.412  1.00 30.22           C  
ATOM   1395  CZ  TYR A 185      20.367  40.873   4.689  1.00 40.10           C  
ATOM   1396  OH  TYR A 185      20.713  39.651   5.218  1.00 47.86           O  
ATOM   1397  N   PRO A 186      19.969  47.678   2.068  1.00 43.35           N  
ATOM   1398  CA  PRO A 186      19.587  48.878   1.308  1.00 43.65           C  
ATOM   1399  C   PRO A 186      20.596  49.412   0.302  1.00 49.02           C  
ATOM   1400  O   PRO A 186      20.227  49.702  -0.830  1.00 54.01           O  
ATOM   1401  CB  PRO A 186      19.282  49.907   2.401  1.00 50.38           C  
ATOM   1402  CG  PRO A 186      20.013  49.388   3.605  1.00 48.91           C  
ATOM   1403  CD  PRO A 186      19.790  47.909   3.509  1.00 29.91           C  
ATOM   1404  N   VAL A 187      21.860  49.540   0.705  1.00 56.41           N  
ATOM   1405  CA  VAL A 187      22.904  50.061  -0.192  1.00 55.33           C  
ATOM   1406  C   VAL A 187      23.220  49.072  -1.325  1.00 53.77           C  
ATOM   1407  O   VAL A 187      23.768  49.451  -2.362  1.00 41.81           O  
ATOM   1408  CB  VAL A 187      24.233  50.368   0.578  1.00 52.20           C  
ATOM   1409  CG1 VAL A 187      25.161  51.211  -0.294  1.00 51.47           C  
ATOM   1410  CG2 VAL A 187      23.961  51.067   1.918  1.00 33.78           C  
ATOM   1411  N   VAL A 188      22.860  47.806  -1.101  1.00 48.31           N  
ATOM   1412  CA  VAL A 188      23.094  46.709  -2.045  1.00 57.17           C  
ATOM   1413  C   VAL A 188      22.040  46.705  -3.154  1.00 62.59           C  
ATOM   1414  O   VAL A 188      22.235  46.126  -4.233  1.00 59.80           O  
ATOM   1415  CB  VAL A 188      23.094  45.336  -1.285  1.00 60.15           C  
ATOM   1416  CG1 VAL A 188      23.213  44.176  -2.246  1.00 70.65           C  
ATOM   1417  CG2 VAL A 188      24.251  45.278  -0.286  1.00 59.05           C  
ATOM   1418  N   TRP A 189      20.962  47.438  -2.905  1.00 68.27           N  
ATOM   1419  CA  TRP A 189      19.835  47.532  -3.828  1.00 62.36           C  
ATOM   1420  C   TRP A 189      19.971  48.537  -4.966  1.00 50.83           C  
ATOM   1421  O   TRP A 189      19.902  48.162  -6.136  1.00 47.02           O  
ATOM   1422  CB  TRP A 189      18.550  47.822  -3.044  1.00 63.21           C  
ATOM   1423  CG  TRP A 189      17.441  46.904  -3.387  1.00 57.92           C  
ATOM   1424  CD1 TRP A 189      17.354  45.586  -3.076  1.00 52.87           C  
ATOM   1425  CD2 TRP A 189      16.253  47.228  -4.122  1.00 54.55           C  
ATOM   1426  NE1 TRP A 189      16.187  45.059  -3.571  1.00 50.96           N  
ATOM   1427  CE2 TRP A 189      15.490  46.046  -4.220  1.00 56.17           C  
ATOM   1428  CE3 TRP A 189      15.754  48.405  -4.705  1.00 51.42           C  
ATOM   1429  CZ2 TRP A 189      14.253  46.000  -4.873  1.00 54.39           C  
ATOM   1430  CZ3 TRP A 189      14.523  48.362  -5.351  1.00 50.49           C  
ATOM   1431  CH2 TRP A 189      13.787  47.164  -5.429  1.00 45.12           C  
ATOM   1432  N   LEU A 190      20.155  49.808  -4.629  1.00 48.19           N  
ATOM   1433  CA  LEU A 190      20.247  50.835  -5.659  1.00 62.12           C  
ATOM   1434  C   LEU A 190      21.572  50.998  -6.419  1.00 66.75           C  
ATOM   1435  O   LEU A 190      21.856  52.066  -6.958  1.00 69.33           O  
ATOM   1436  CB  LEU A 190      19.749  52.182  -5.115  1.00 71.01           C  
ATOM   1437  CG  LEU A 190      20.590  53.074  -4.206  1.00 66.66           C  
ATOM   1438  CD1 LEU A 190      19.728  54.254  -3.758  1.00 56.52           C  
ATOM   1439  CD2 LEU A 190      21.095  52.293  -3.010  1.00 77.06           C  
ATOM   1440  N   ILE A 191      22.354  49.926  -6.514  1.00 75.53           N  
ATOM   1441  CA  ILE A 191      23.632  49.980  -7.228  1.00 79.50           C  
ATOM   1442  C   ILE A 191      23.786  48.888  -8.291  1.00 82.54           C  
ATOM   1443  O   ILE A 191      24.796  48.837  -8.993  1.00 84.54           O  
ATOM   1444  CB  ILE A 191      24.862  49.944  -6.263  1.00 75.27           C  
ATOM   1445  CG1 ILE A 191      24.890  48.644  -5.462  1.00 76.30           C  
ATOM   1446  CG2 ILE A 191      24.840  51.142  -5.325  1.00 83.59           C  
ATOM   1447  CD1 ILE A 191      26.096  48.514  -4.581  1.00 72.89           C  
ATOM   1448  N   GLY A 192      22.788  48.020  -8.418  1.00 84.98           N  
ATOM   1449  CA  GLY A 192      22.871  46.969  -9.417  1.00 88.51           C  
ATOM   1450  C   GLY A 192      21.668  46.049  -9.518  1.00 89.75           C  
ATOM   1451  O   GLY A 192      20.905  46.104 -10.484  1.00 87.84           O  
ATOM   1452  N   SER A 193      21.512  45.190  -8.518  1.00 89.42           N  
ATOM   1453  CA  SER A 193      20.421  44.226  -8.474  1.00 95.96           C  
ATOM   1454  C   SER A 193      19.072  44.745  -8.964  1.00 95.75           C  
ATOM   1455  O   SER A 193      18.562  44.310 -10.002  1.00 97.33           O  
ATOM   1456  CB  SER A 193      20.273  43.662  -7.053  1.00101.56           C  
ATOM   1457  OG  SER A 193      20.246  44.695  -6.080  1.00103.85           O  
ATOM   1458  N   GLU A 194      18.516  45.702  -8.230  1.00 92.86           N  
ATOM   1459  CA  GLU A 194      17.211  46.242  -8.563  1.00 89.56           C  
ATOM   1460  C   GLU A 194      17.156  47.760  -8.419  1.00 85.13           C  
ATOM   1461  O   GLU A 194      16.120  48.324  -8.060  1.00 84.41           O  
ATOM   1462  CB  GLU A 194      16.158  45.588  -7.667  1.00 94.48           C  
ATOM   1463  CG  GLU A 194      16.506  44.166  -7.248  1.00 93.41           C  
ATOM   1464  CD  GLU A 194      15.293  43.329  -6.947  1.00 97.59           C  
ATOM   1465  OE1 GLU A 194      14.381  43.296  -7.796  1.00101.26           O  
ATOM   1466  OE2 GLU A 194      15.256  42.696  -5.873  1.00101.36           O  
ATOM   1467  N   GLY A 195      18.274  48.418  -8.699  1.00 79.96           N  
ATOM   1468  CA  GLY A 195      18.315  49.864  -8.603  1.00 81.89           C  
ATOM   1469  C   GLY A 195      18.933  50.473  -9.843  1.00 83.01           C  
ATOM   1470  O   GLY A 195      18.263  50.673 -10.863  1.00 81.02           O  
ATOM   1471  N   ALA A 196      20.223  50.779  -9.745  1.00 80.20           N  
ATOM   1472  CA  ALA A 196      20.959  51.352 -10.853  1.00 70.78           C  
ATOM   1473  C   ALA A 196      21.192  50.257 -11.887  1.00 73.32           C  
ATOM   1474  O   ALA A 196      20.269  49.836 -12.575  1.00 78.33           O  
ATOM   1475  CB  ALA A 196      22.274  51.915 -10.360  1.00 65.97           C  
ATOM   1476  N   GLY A 197      22.423  49.768 -11.953  1.00 80.07           N  
ATOM   1477  CA  GLY A 197      22.776  48.728 -12.899  1.00 85.19           C  
ATOM   1478  C   GLY A 197      24.283  48.709 -13.060  1.00 93.86           C  
ATOM   1479  O   GLY A 197      24.797  48.651 -14.177  1.00 96.44           O  
ATOM   1480  N   ILE A 198      24.992  48.814 -11.937  1.00 95.26           N  
ATOM   1481  CA  ILE A 198      26.450  48.809 -11.939  1.00 98.01           C  
ATOM   1482  C   ILE A 198      26.921  47.369 -11.784  1.00 97.98           C  
ATOM   1483  O   ILE A 198      27.574  46.817 -12.671  1.00101.08           O  
ATOM   1484  CB  ILE A 198      27.019  49.684 -10.797  1.00102.14           C  
ATOM   1485  CG1 ILE A 198      26.306  51.045 -10.782  1.00106.06           C  
ATOM   1486  CG2 ILE A 198      28.529  49.874 -10.981  1.00 99.84           C  
ATOM   1487  CD1 ILE A 198      26.672  51.933  -9.613  1.00110.28           C  
ATOM   1488  N   VAL A 199      26.583  46.769 -10.648  1.00 95.00           N  
ATOM   1489  CA  VAL A 199      26.931  45.382 -10.371  1.00 94.05           C  
ATOM   1490  C   VAL A 199      25.652  44.592 -10.651  1.00 97.14           C  
ATOM   1491  O   VAL A 199      24.758  44.533  -9.810  1.00100.96           O  
ATOM   1492  CB  VAL A 199      27.406  45.207  -8.897  1.00 89.11           C  
ATOM   1493  CG1 VAL A 199      27.297  43.769  -8.456  1.00 78.68           C  
ATOM   1494  CG2 VAL A 199      28.849  45.667  -8.757  1.00 85.01           C  
ATOM   1495  N   PRO A 200      25.539  44.017 -11.865  1.00 98.80           N  
ATOM   1496  CA  PRO A 200      24.414  43.222 -12.377  1.00 99.99           C  
ATOM   1497  C   PRO A 200      23.782  42.200 -11.431  1.00 99.23           C  
ATOM   1498  O   PRO A 200      23.442  42.519 -10.294  1.00101.71           O  
ATOM   1499  CB  PRO A 200      25.010  42.560 -13.617  1.00103.57           C  
ATOM   1500  CG  PRO A 200      25.915  43.635 -14.133  1.00104.04           C  
ATOM   1501  CD  PRO A 200      26.622  44.070 -12.867  1.00102.32           C  
ATOM   1502  N   LEU A 201      23.574  40.986 -11.925  1.00 93.65           N  
ATOM   1503  CA  LEU A 201      22.955  39.941 -11.123  1.00 83.98           C  
ATOM   1504  C   LEU A 201      23.993  39.043 -10.464  1.00 81.60           C  
ATOM   1505  O   LEU A 201      23.904  38.743  -9.273  1.00 84.35           O  
ATOM   1506  CB  LEU A 201      22.003  39.118 -12.001  1.00 82.04           C  
ATOM   1507  CG  LEU A 201      21.160  37.981 -11.417  1.00 76.72           C  
ATOM   1508  CD1 LEU A 201      20.443  38.433 -10.162  1.00 75.21           C  
ATOM   1509  CD2 LEU A 201      20.161  37.509 -12.468  1.00 68.76           C  
ATOM   1510  N   ASN A 202      24.998  38.663 -11.243  1.00 68.65           N  
ATOM   1511  CA  ASN A 202      26.069  37.783 -10.796  1.00 68.14           C  
ATOM   1512  C   ASN A 202      26.645  38.114  -9.420  1.00 66.21           C  
ATOM   1513  O   ASN A 202      26.494  37.347  -8.476  1.00 65.97           O  
ATOM   1514  CB  ASN A 202      27.182  37.776 -11.845  1.00 70.08           C  
ATOM   1515  CG  ASN A 202      28.165  36.659 -11.641  1.00 65.81           C  
ATOM   1516  OD1 ASN A 202      29.301  36.725 -12.107  1.00 68.16           O  
ATOM   1517  ND2 ASN A 202      27.730  35.611 -10.957  1.00 66.60           N  
ATOM   1518  N   ILE A 203      27.304  39.259  -9.308  1.00 67.53           N  
ATOM   1519  CA  ILE A 203      27.907  39.668  -8.044  1.00 70.71           C  
ATOM   1520  C   ILE A 203      26.858  39.882  -6.949  1.00 66.93           C  
ATOM   1521  O   ILE A 203      27.040  39.434  -5.815  1.00 66.58           O  
ATOM   1522  CB  ILE A 203      28.788  40.946  -8.235  1.00 71.90           C  
ATOM   1523  CG1 ILE A 203      30.016  40.630  -9.103  1.00 75.52           C  
ATOM   1524  CG2 ILE A 203      29.229  41.513  -6.900  1.00 73.50           C  
ATOM   1525  CD1 ILE A 203      31.020  39.656  -8.471  1.00 68.96           C  
ATOM   1526  N   GLU A 204      25.741  40.514  -7.305  1.00 64.86           N  
ATOM   1527  CA  GLU A 204      24.663  40.787  -6.349  1.00 63.75           C  
ATOM   1528  C   GLU A 204      24.208  39.536  -5.606  1.00 66.91           C  
ATOM   1529  O   GLU A 204      23.822  39.614  -4.433  1.00 64.11           O  
ATOM   1530  CB  GLU A 204      23.456  41.423  -7.055  1.00 61.97           C  
ATOM   1531  CG  GLU A 204      23.650  42.880  -7.500  1.00 56.43           C  
ATOM   1532  CD  GLU A 204      23.667  43.896  -6.353  1.00 54.37           C  
ATOM   1533  OE1 GLU A 204      23.712  43.493  -5.164  1.00 51.08           O  
ATOM   1534  OE2 GLU A 204      23.646  45.111  -6.655  1.00 50.79           O  
ATOM   1535  N   THR A 205      24.262  38.396  -6.305  1.00 61.48           N  
ATOM   1536  CA  THR A 205      23.862  37.092  -5.769  1.00 54.80           C  
ATOM   1537  C   THR A 205      24.814  36.564  -4.708  1.00 51.75           C  
ATOM   1538  O   THR A 205      24.391  35.876  -3.777  1.00 49.50           O  
ATOM   1539  CB  THR A 205      23.696  36.057  -6.891  1.00 53.53           C  
ATOM   1540  OG1 THR A 205      22.549  36.403  -7.676  1.00 61.73           O  
ATOM   1541  CG2 THR A 205      23.510  34.666  -6.319  1.00 50.65           C  
ATOM   1542  N   LEU A 206      26.099  36.845  -4.859  1.00 48.40           N  
ATOM   1543  CA  LEU A 206      27.034  36.414  -3.832  1.00 50.63           C  
ATOM   1544  C   LEU A 206      26.800  37.339  -2.640  1.00 52.66           C  
ATOM   1545  O   LEU A 206      26.415  36.879  -1.556  1.00 46.49           O  
ATOM   1546  CB  LEU A 206      28.493  36.495  -4.316  1.00 49.98           C  
ATOM   1547  CG  LEU A 206      29.606  36.477  -3.253  1.00 51.08           C  
ATOM   1548  CD1 LEU A 206      29.315  35.504  -2.111  1.00 39.56           C  
ATOM   1549  CD2 LEU A 206      30.926  36.146  -3.922  1.00 58.30           C  
ATOM   1550  N   LEU A 207      26.982  38.638  -2.892  1.00 55.01           N  
ATOM   1551  CA  LEU A 207      26.820  39.714  -1.908  1.00 58.47           C  
ATOM   1552  C   LEU A 207      25.647  39.481  -0.963  1.00 57.18           C  
ATOM   1553  O   LEU A 207      25.808  39.489   0.273  1.00 53.90           O  
ATOM   1554  CB  LEU A 207      26.616  41.043  -2.638  1.00 57.96           C  
ATOM   1555  CG  LEU A 207      27.821  41.937  -2.909  1.00 61.32           C  
ATOM   1556  CD1 LEU A 207      29.097  41.126  -3.127  1.00 47.01           C  
ATOM   1557  CD2 LEU A 207      27.484  42.828  -4.095  1.00 57.25           C  
ATOM   1558  N   PHE A 208      24.473  39.281  -1.563  1.00 50.99           N  
ATOM   1559  CA  PHE A 208      23.268  39.026  -0.810  1.00 47.38           C  
ATOM   1560  C   PHE A 208      23.405  37.772   0.051  1.00 46.11           C  
ATOM   1561  O   PHE A 208      23.005  37.804   1.215  1.00 48.58           O  
ATOM   1562  CB  PHE A 208      22.056  38.935  -1.738  1.00 48.33           C  
ATOM   1563  CG  PHE A 208      21.266  40.220  -1.836  1.00 49.06           C  
ATOM   1564  CD1 PHE A 208      21.317  41.166  -0.815  1.00 56.01           C  
ATOM   1565  CD2 PHE A 208      20.453  40.472  -2.930  1.00 55.29           C  
ATOM   1566  CE1 PHE A 208      20.567  42.338  -0.887  1.00 52.06           C  
ATOM   1567  CE2 PHE A 208      19.699  41.645  -3.009  1.00 54.67           C  
ATOM   1568  CZ  PHE A 208      19.760  42.579  -1.982  1.00 52.72           C  
ATOM   1569  N   MET A 209      24.028  36.708  -0.475  1.00 42.40           N  
ATOM   1570  CA  MET A 209      24.195  35.485   0.319  1.00 48.14           C  
ATOM   1571  C   MET A 209      25.174  35.616   1.502  1.00 49.93           C  
ATOM   1572  O   MET A 209      24.925  35.031   2.563  1.00 53.63           O  
ATOM   1573  CB  MET A 209      24.549  34.270  -0.541  1.00 53.17           C  
ATOM   1574  CG  MET A 209      24.349  32.934   0.193  1.00 47.18           C  
ATOM   1575  SD  MET A 209      25.820  31.870   0.259  1.00 48.24           S  
ATOM   1576  CE  MET A 209      26.590  32.479   1.725  1.00 44.71           C  
ATOM   1577  N   VAL A 210      26.263  36.377   1.331  1.00 49.03           N  
ATOM   1578  CA  VAL A 210      27.245  36.614   2.409  1.00 42.76           C  
ATOM   1579  C   VAL A 210      26.481  37.216   3.582  1.00 42.50           C  
ATOM   1580  O   VAL A 210      26.581  36.758   4.720  1.00 35.05           O  
ATOM   1581  CB  VAL A 210      28.335  37.660   1.996  1.00 46.38           C  
ATOM   1582  CG1 VAL A 210      29.359  37.864   3.125  1.00 44.07           C  
ATOM   1583  CG2 VAL A 210      29.036  37.230   0.730  1.00 51.33           C  
ATOM   1584  N   LEU A 211      25.700  38.247   3.280  1.00 44.96           N  
ATOM   1585  CA  LEU A 211      24.901  38.906   4.288  1.00 52.86           C  
ATOM   1586  C   LEU A 211      23.956  37.908   4.933  1.00 53.58           C  
ATOM   1587  O   LEU A 211      23.828  37.892   6.149  1.00 66.58           O  
ATOM   1588  CB  LEU A 211      24.106  40.077   3.683  1.00 57.28           C  
ATOM   1589  CG  LEU A 211      24.725  41.493   3.564  1.00 60.04           C  
ATOM   1590  CD1 LEU A 211      25.083  42.032   4.944  1.00 49.23           C  
ATOM   1591  CD2 LEU A 211      25.942  41.517   2.632  1.00 43.04           C  
ATOM   1592  N   ASP A 212      23.352  37.026   4.140  1.00 50.60           N  
ATOM   1593  CA  ASP A 212      22.408  36.052   4.694  1.00 52.61           C  
ATOM   1594  C   ASP A 212      22.955  34.963   5.626  1.00 52.45           C  
ATOM   1595  O   ASP A 212      22.391  34.746   6.701  1.00 66.55           O  
ATOM   1596  CB  ASP A 212      21.548  35.436   3.593  1.00 40.94           C  
ATOM   1597  CG  ASP A 212      20.445  36.352   3.151  1.00 49.67           C  
ATOM   1598  OD1 ASP A 212      20.753  37.489   2.744  1.00 57.43           O  
ATOM   1599  OD2 ASP A 212      19.264  35.950   3.218  1.00 56.68           O  
ATOM   1600  N   VAL A 213      24.025  34.275   5.222  1.00 50.52           N  
ATOM   1601  CA  VAL A 213      24.613  33.212   6.042  1.00 51.92           C  
ATOM   1602  C   VAL A 213      25.063  33.737   7.399  1.00 50.66           C  
ATOM   1603  O   VAL A 213      24.899  33.071   8.427  1.00 55.98           O  
ATOM   1604  CB  VAL A 213      25.829  32.555   5.342  1.00 52.84           C  
ATOM   1605  CG1 VAL A 213      26.868  33.607   4.945  1.00 48.87           C  
ATOM   1606  CG2 VAL A 213      26.472  31.528   6.255  1.00 53.84           C  
ATOM   1607  N   SER A 214      25.627  34.943   7.375  1.00 48.33           N  
ATOM   1608  CA  SER A 214      26.133  35.631   8.555  1.00 46.27           C  
ATOM   1609  C   SER A 214      24.969  36.150   9.379  1.00 41.17           C  
ATOM   1610  O   SER A 214      25.006  36.098  10.602  1.00 47.38           O  
ATOM   1611  CB  SER A 214      27.021  36.797   8.106  1.00 53.95           C  
ATOM   1612  OG  SER A 214      27.662  37.440   9.190  1.00 71.42           O  
ATOM   1613  N   ALA A 215      23.931  36.624   8.691  1.00 43.76           N  
ATOM   1614  CA  ALA A 215      22.716  37.177   9.306  1.00 44.22           C  
ATOM   1615  C   ALA A 215      21.837  36.187  10.083  1.00 47.78           C  
ATOM   1616  O   ALA A 215      21.133  36.580  11.021  1.00 49.56           O  
ATOM   1617  CB  ALA A 215      21.864  37.872   8.243  1.00 31.17           C  
ATOM   1618  N   LYS A 216      21.873  34.914   9.700  1.00 47.06           N  
ATOM   1619  CA  LYS A 216      21.042  33.914  10.361  1.00 48.41           C  
ATOM   1620  C   LYS A 216      21.828  32.877  11.166  1.00 50.81           C  
ATOM   1621  O   LYS A 216      21.721  32.817  12.390  1.00 49.55           O  
ATOM   1622  CB  LYS A 216      20.154  33.228   9.321  1.00 46.97           C  
ATOM   1623  CG  LYS A 216      19.418  34.204   8.417  1.00 38.78           C  
ATOM   1624  CD  LYS A 216      18.863  33.494   7.225  1.00 37.87           C  
ATOM   1625  CE  LYS A 216      18.675  34.444   6.063  1.00 44.21           C  
ATOM   1626  NZ  LYS A 216      17.510  35.342   6.204  1.00 46.71           N  
ATOM   1627  N   VAL A 217      22.589  32.031  10.481  1.00 53.23           N  
ATOM   1628  CA  VAL A 217      23.375  31.021  11.176  1.00 54.60           C  
ATOM   1629  C   VAL A 217      24.330  31.744  12.137  1.00 55.17           C  
ATOM   1630  O   VAL A 217      24.375  31.407  13.313  1.00 51.77           O  
ATOM   1631  CB  VAL A 217      24.139  30.101  10.176  1.00 54.62           C  
ATOM   1632  CG1 VAL A 217      24.941  29.036  10.910  1.00 35.97           C  
ATOM   1633  CG2 VAL A 217      23.153  29.429   9.239  1.00 56.58           C  
ATOM   1634  N   GLY A 218      25.022  32.781  11.647  1.00 57.51           N  
ATOM   1635  CA  GLY A 218      25.950  33.557  12.471  1.00 50.94           C  
ATOM   1636  C   GLY A 218      25.247  34.215  13.647  1.00 51.10           C  
ATOM   1637  O   GLY A 218      25.784  34.298  14.753  1.00 44.69           O  
ATOM   1638  N   PHE A 219      24.033  34.693  13.392  1.00 53.68           N  
ATOM   1639  CA  PHE A 219      23.197  35.304  14.419  1.00 57.55           C  
ATOM   1640  C   PHE A 219      22.855  34.188  15.405  1.00 59.06           C  
ATOM   1641  O   PHE A 219      22.985  34.356  16.617  1.00 64.40           O  
ATOM   1642  CB  PHE A 219      21.907  35.862  13.791  1.00 55.75           C  
ATOM   1643  CG  PHE A 219      20.870  36.286  14.795  1.00 53.61           C  
ATOM   1644  CD1 PHE A 219      20.918  37.549  15.382  1.00 63.77           C  
ATOM   1645  CD2 PHE A 219      19.837  35.428  15.149  1.00 52.48           C  
ATOM   1646  CE1 PHE A 219      19.946  37.946  16.312  1.00 60.51           C  
ATOM   1647  CE2 PHE A 219      18.864  35.819  16.074  1.00 52.53           C  
ATOM   1648  CZ  PHE A 219      18.918  37.078  16.655  1.00 51.41           C  
ATOM   1649  N   GLY A 220      22.429  33.046  14.864  1.00 55.10           N  
ATOM   1650  CA  GLY A 220      22.086  31.903  15.691  1.00 45.23           C  
ATOM   1651  C   GLY A 220      23.304  31.349  16.396  1.00 39.55           C  
ATOM   1652  O   GLY A 220      23.192  30.850  17.515  1.00 29.67           O  
ATOM   1653  N   LEU A 221      24.460  31.449  15.731  1.00 42.13           N  
ATOM   1654  CA  LEU A 221      25.746  31.004  16.265  1.00 46.46           C  
ATOM   1655  C   LEU A 221      26.193  31.943  17.415  1.00 50.78           C  
ATOM   1656  O   LEU A 221      27.292  31.799  17.954  1.00 54.67           O  
ATOM   1657  CB  LEU A 221      26.795  30.931  15.147  1.00 41.50           C  
ATOM   1658  CG  LEU A 221      27.762  29.730  15.085  1.00 49.16           C  
ATOM   1659  CD1 LEU A 221      27.029  28.396  14.922  1.00 41.91           C  
ATOM   1660  CD2 LEU A 221      28.722  29.917  13.923  1.00 45.33           C  
ATOM   1661  N   ILE A 222      25.341  32.919  17.750  1.00 49.08           N  
ATOM   1662  CA  ILE A 222      25.567  33.832  18.872  1.00 47.11           C  
ATOM   1663  C   ILE A 222      24.660  33.278  19.955  1.00 44.74           C  
ATOM   1664  O   ILE A 222      25.083  32.998  21.063  1.00 46.00           O  
ATOM   1665  CB  ILE A 222      25.043  35.277  18.632  1.00 46.17           C  
ATOM   1666  CG1 ILE A 222      25.647  35.896  17.376  1.00 55.51           C  
ATOM   1667  CG2 ILE A 222      25.361  36.146  19.843  1.00 36.33           C  
ATOM   1668  CD1 ILE A 222      25.210  37.320  17.157  1.00 47.10           C  
ATOM   1669  N   LEU A 223      23.389  33.142  19.598  1.00 50.76           N  
ATOM   1670  CA  LEU A 223      22.338  32.641  20.482  1.00 55.81           C  
ATOM   1671  C   LEU A 223      22.392  31.104  20.569  1.00 57.79           C  
ATOM   1672  O   LEU A 223      21.509  30.391  20.082  1.00 63.27           O  
ATOM   1673  CB  LEU A 223      20.990  33.126  19.935  1.00 57.20           C  
ATOM   1674  CG  LEU A 223      19.873  33.634  20.844  1.00 45.95           C  
ATOM   1675  CD1 LEU A 223      20.420  34.440  22.006  1.00 38.22           C  
ATOM   1676  CD2 LEU A 223      18.948  34.475  19.983  1.00 42.24           C  
ATOM   1677  N   LEU A 224      23.440  30.617  21.223  1.00 60.47           N  
ATOM   1678  CA  LEU A 224      23.705  29.186  21.393  1.00 63.45           C  
ATOM   1679  C   LEU A 224      24.778  29.080  22.468  1.00 65.00           C  
ATOM   1680  O   LEU A 224      24.820  28.129  23.260  1.00 66.01           O  
ATOM   1681  CB  LEU A 224      24.273  28.619  20.085  1.00 60.76           C  
ATOM   1682  CG  LEU A 224      25.095  27.330  20.144  1.00 60.29           C  
ATOM   1683  CD1 LEU A 224      24.209  26.140  20.442  1.00 65.34           C  
ATOM   1684  CD2 LEU A 224      25.794  27.136  18.807  1.00 64.28           C  
ATOM   1685  N   ARG A 225      25.660  30.076  22.429  1.00 67.56           N  
ATOM   1686  CA  ARG A 225      26.800  30.255  23.317  1.00 66.79           C  
ATOM   1687  C   ARG A 225      26.387  30.333  24.786  1.00 63.17           C  
ATOM   1688  CB  ARG A 225      27.496  31.546  22.894  1.00 60.83           C  
ATOM   1689  CG  ARG A 225      28.744  31.919  23.627  1.00 58.74           C  
ATOM   1690  CD  ARG A 225      29.287  33.178  22.976  1.00 68.23           C  
ATOM   1691  NE  ARG A 225      30.580  33.577  23.523  1.00 74.95           N  
ATOM   1692  CZ  ARG A 225      31.010  34.832  23.566  1.00 74.76           C  
ATOM   1693  NH1 ARG A 225      30.245  35.813  23.092  1.00 61.92           N  
ATOM   1694  NH2 ARG A 225      32.197  35.102  24.090  1.00 72.26           N  
TER    1695      ARG A 225                                                      
HETATM 1696  C1  RET A 300      15.395  45.535   1.178  1.00 46.46           C  
HETATM 1697  C2  RET A 300      14.615  46.311   0.122  1.00 39.25           C  
HETATM 1698  C3  RET A 300      15.207  47.677  -0.063  1.00 50.30           C  
HETATM 1699  C4  RET A 300      15.206  48.501   1.215  1.00 38.90           C  
HETATM 1700  C5  RET A 300      15.623  47.710   2.421  1.00 42.36           C  
HETATM 1701  C6  RET A 300      15.723  46.344   2.461  1.00 46.89           C  
HETATM 1702  C7  RET A 300      16.124  45.612   3.672  1.00 47.42           C  
HETATM 1703  C8  RET A 300      16.236  44.315   4.007  1.00 55.46           C  
HETATM 1704  C9  RET A 300      16.642  43.582   5.190  1.00 63.31           C  
HETATM 1705  C10 RET A 300      16.578  42.205   5.116  1.00 65.50           C  
HETATM 1706  C11 RET A 300      16.854  41.174   6.082  1.00 59.15           C  
HETATM 1707  C12 RET A 300      16.960  39.885   5.722  1.00 50.48           C  
HETATM 1708  C13 RET A 300      17.254  38.799   6.581  1.00 41.76           C  
HETATM 1709  C14 RET A 300      17.451  37.672   5.893  1.00 35.78           C  
HETATM 1710  C15 RET A 300      17.862  36.517   6.510  1.00 44.02           C  
HETATM 1711  C16 RET A 300      14.512  44.341   1.317  1.00 54.55           C  
HETATM 1712  C17 RET A 300      16.751  45.113   0.559  1.00 54.77           C  
HETATM 1713  C18 RET A 300      15.869  48.746   3.480  1.00 35.81           C  
HETATM 1714  C19 RET A 300      17.152  44.354   6.377  1.00 55.96           C  
HETATM 1715  C20 RET A 300      17.409  38.991   8.072  1.00 38.37           C  
HETATM 1716  O   HOH A 400      18.909  36.773  -0.205  1.00 64.03           O  
HETATM 1717  O   HOH A 401      21.493  32.109  -1.202  1.00 46.53           O  
HETATM 1718  O   HOH A 402      20.126  34.248  -2.874  1.00 59.35           O  
HETATM 1719  O   HOH A 403      19.214  39.685  11.721  1.00 42.50           O  
HETATM 1720  O   HOH A 404      15.199  42.014  35.433  1.00 43.36           O  
HETATM 1721  O   HOH A 405      21.968  36.815  23.426  1.00 54.56           O  
HETATM 1722  O   HOH A 406      21.215  45.817 -12.931  1.00 46.33           O  
HETATM 1723  O   HOH A 407      23.840  48.826 -16.394  1.00 50.76           O  
HETATM 1724  O   HOH A 408      18.429  29.041 -11.172  1.00 51.53           O  
HETATM 1725  O   HOH A 409      15.089  36.484  28.808  1.00 51.13           O  
HETATM 1726  O   HOH A 410      31.094  49.266  22.771  1.00 46.29           O  
HETATM 1727  O   HOH A 411      11.299  46.169  10.682  1.00 26.80           O  
HETATM 1728  O   HOH A 412       9.072  19.003  22.281  1.00 65.05           O  
HETATM 1729  O   HOH A 413      29.576  46.836  -3.670  1.00 50.83           O  
HETATM 1730  O   HOH A 414      27.362  28.043   9.584  1.00 60.17           O  
HETATM 1731  O   HOH A 415       9.057  60.489   7.917  1.00 63.18           O  
HETATM 1732  O   HOH A 416      27.337  21.092  20.075  1.00 45.88           O  
HETATM 1733  O   HOH A 417      19.456  52.827 -15.331  1.00 56.08           O  
HETATM 1734  O   HOH A 418      18.550  56.585  -9.961  1.00 51.66           O  
HETATM 1735  O   HOH A 419       2.581  36.648   1.584  1.00 22.60           O  
HETATM 1736  O   HOH A 420      12.994  20.788   6.754  1.00 69.37           O  
HETATM 1737  O   HOH A 421      20.548  24.755 -12.592  1.00 44.95           O  
HETATM 1738  O   HOH A 422      21.774  20.637  -0.211  1.00 45.21           O  
HETATM 1739  O   HOH A 423      25.302  17.481   9.461  1.00 72.24           O  
HETATM 1740  O   HOH A 424      28.061  21.809  -6.608  1.00 52.02           O  
HETATM 1741  O   HOH A 425      11.494  22.979  10.690  1.00 49.31           O  
CONECT 1626 1710                                                                
CONECT 1696 1697 1701 1711 1712                                                 
CONECT 1697 1696 1698                                                           
CONECT 1698 1697 1699                                                           
CONECT 1699 1698 1700                                                           
CONECT 1700 1699 1701 1713                                                      
CONECT 1701 1696 1700 1702                                                      
CONECT 1702 1701 1703                                                           
CONECT 1703 1702 1704                                                           
CONECT 1704 1703 1705 1714                                                      
CONECT 1705 1704 1706                                                           
CONECT 1706 1705 1707                                                           
CONECT 1707 1706 1708                                                           
CONECT 1708 1707 1709 1715                                                      
CONECT 1709 1708 1710                                                           
CONECT 1710 1626 1709                                                           
CONECT 1711 1696                                                                
CONECT 1712 1696                                                                
CONECT 1713 1700                                                                
CONECT 1714 1704                                                                
CONECT 1715 1708                                                                
MASTER      351    0    1   10    0    0    5    6 1740    1   21   20          
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.