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***  HYDROLASE(SH2 DOMAIN) 15-MAY-94 1AYD  ***

elNémo ID: 19012900002414492

Job options:

ID        	=	 19012900002414492
JOBID     	=	 HYDROLASE(SH2 DOMAIN) 15-MAY-94 1AYD
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 5
DQMIN     	=	 -5
DQMAX     	=	 5
DQSTEP    	=	 2
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


HEADER    HYDROLASE(SH2 DOMAIN)                   15-MAY-94   1AYD              
TITLE     CRYSTAL STRUCTURES OF PEPTIDE COMPLEXES OF THE AMINO-                 
TITLE    2 TERMINAL SH2 DOMAIN OF THE SYP TYROSINE PHOSPHATASE                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN-TYROSINE PHOSPHATASE SYP (N-TERMINAL SH2           
COMPND   3 DOMAIN);                                                             
COMPND   4 CHAIN: A;                                                            
COMPND   5 EC: 3.1.3.48;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE   4 ORGANISM_TAXID: 10090                                                
KEYWDS    HYDROLASE(SH2 DOMAIN)                                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.-H.LEE,J.KURIYAN                                                    
REVDAT   3   24-FEB-09 1AYD    1       VERSN                                    
REVDAT   2   01-APR-03 1AYD    1       JRNL                                     
REVDAT   1   31-AUG-94 1AYD    0                                                
JRNL        AUTH   C.H.LEE,D.KOMINOS,S.JACQUES,B.MARGOLIS,                      
JRNL        AUTH 2 J.SCHLESSINGER,S.E.SHOELSON,J.KURIYAN                        
JRNL        TITL   CRYSTAL STRUCTURES OF PEPTIDE COMPLEXES OF THE               
JRNL        TITL 2 AMINO-TERMINAL SH2 DOMAIN OF THE SYP TYROSINE                
JRNL        TITL 3 PHOSPHATASE.                                                 
JRNL        REF    STRUCTURE                     V.   2   423 1994              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   7521735                                                      
JRNL        DOI    10.1016/S0969-2126(00)00044-7                                
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   G.WAKSMAN,S.E.SHOELSON,N.PANT,D.COWBURN,J.KURIYAN            
REMARK   1  TITL   BINDING OF A HIGH AFFINITY PHOSPHOTYROSYL PEPTIDE            
REMARK   1  TITL 2 TO THE SRC SH2 DOMAIN: CRYSTAL STRUCTURES OF THE             
REMARK   1  TITL 3 COMPLEXED AND PEPTIDE-FREE FORMS                             
REMARK   1  REF    CELL(CAMBRIDGE,MASS.)         V.  72   779 1993              
REMARK   1  REFN                   ISSN 0092-8674                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   J.KURIYAN,D.COWBURN                                          
REMARK   1  TITL   STRUCTURES OF SH2 AND SH3 DOMAINS                            
REMARK   1  REF    CURR.OPIN.STRUCT.BIOL.        V.   3   828 1993              
REMARK   1  REFN                   ISSN 0959-440X                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   G.WAKSMAN,D.KOMINOS,S.R.ROBERTSON,N.PANT,                    
REMARK   1  AUTH 2 D.BALTIMORE,R.B.BIRGE,D.COWBURN,H.HANAFUSA,                  
REMARK   1  AUTH 3 B.J.MAYER,M.OVERDUIN,M.D.RESH,C.B.RIOS,L.SILVERMAN,          
REMARK   1  AUTH 4 J.KURIYAN                                                    
REMARK   1  TITL   CRYSTAL STRUCTURE OF THE PHOSPHOTYROSINE                     
REMARK   1  TITL 2 RECOGNITION DOMAIN SH2 OF V-SRC COMPLEXED WITH               
REMARK   1  TITL 3 TYROSINE-PHOSPHORYLATED PEPTIDES                             
REMARK   1  REF    NATURE                        V. 358   646 1992              
REMARK   1  REFN                   ISSN 0028-0836                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR                                               
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 6.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 6359                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.200                           
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
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           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
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            : 784                                     
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 87                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.012                           
REMARK   3   BOND ANGLES            (DEGREES) : 3.00                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
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  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1AYD COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : NULL                               
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: X-PLOR                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 62.66                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.29                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+3/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -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 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       38.05000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       31.60000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       31.60000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       57.07500            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       31.60000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       31.60000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       19.02500            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       31.60000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       31.60000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       57.07500            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       31.60000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       31.60000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       19.02500            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       38.05000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 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 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     MET A   3    CG   SD   CE                                        
REMARK 470     ARG A   4    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A   5    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER A  34    OG                                                  
REMARK 470     LYS A  35    CE   NZ                                             
REMARK 470     ASN A  37    CG   OD1  ND2                                       
REMARK 470     LYS A  55    CE   NZ                                             
REMARK 470     LYS A  91    CG   CD   CE   NZ                                   
REMARK 470     ASN A  92    CG   OD1  ND2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    HIS A   8   NE2   HIS A   8   CD2    -0.069                       
REMARK 500    HIS A  53   NE2   HIS A  53   CD2    -0.067                       
REMARK 500    HIS A  85   NE2   HIS A  85   CD2    -0.067                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    TRP A   6   CD1 -  CG  -  CD2 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    TRP A   6   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.3 DEGREES          
REMARK 500    ARG A  23   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG A  32   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500    TYR A  80   CB  -  CG  -  CD1 ANGL. DEV. =  -4.0 DEGREES          
REMARK 500    LEU A 102   CA  -  CB  -  CG  ANGL. DEV. =  15.1 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ARG A   4      -49.32   -133.69                                   
REMARK 500    ASN A  37      110.70   -168.97                                   
REMARK 500    LEU A  65       60.98   -113.92                                   
REMARK 500    TYR A  66       53.62     35.48                                   
REMARK 500    LYS A  91      -79.56     38.95                                   
REMARK 500    ASN A  92       36.80    -82.51                                   
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 331        DISTANCE =  5.31 ANGSTROMS                       
REMARK 525    HOH A 336        DISTANCE =  5.16 ANGSTROMS                       
DBREF  1AYD A    4   103  UNP    P35235   PTN11_MOUSE      4    103             
SEQRES   1 A  101  MET ARG ARG TRP PHE HIS PRO ASN ILE THR GLY VAL GLU          
SEQRES   2 A  101  ALA GLU ASN LEU LEU LEU THR ARG GLY VAL ASP GLY SER          
SEQRES   3 A  101  PHE LEU ALA ARG PRO SER LYS SER ASN PRO GLY ASP PHE          
SEQRES   4 A  101  THR LEU SER VAL ARG ARG ASN GLY ALA VAL THR HIS ILE          
SEQRES   5 A  101  LYS ILE GLN ASN THR GLY ASP TYR TYR ASP LEU TYR GLY          
SEQRES   6 A  101  GLY GLU LYS PHE ALA THR LEU ALA GLU LEU VAL GLN TYR          
SEQRES   7 A  101  TYR MET GLU HIS HIS GLY GLN LEU LYS GLU LYS ASN GLY          
SEQRES   8 A  101  ASP VAL ILE GLU LEU LYS TYR PRO LEU ASN                      
FORMUL   2  HOH   *87(H2 O)                                                     
HELIX    1   1 THR A   12  GLY A   24  1                                  13    
HELIX    2   2 THR A   73  HIS A   84  1                                  12    
HELIX    3   3 HIS A   85  GLN A   87  5                                   3    
SHEET    1   A 5 TYR A  63  ASP A  64  0                                        
SHEET    2   A 5 ALA A  50  ASN A  58 -1  N  GLN A  57   O  ASP A  64           
SHEET    3   A 5 PHE A  41  ARG A  47 -1  O  PHE A  41   N  ILE A  56           
SHEET    4   A 5 SER A  28  PRO A  33 -1  O  SER A  28   N  ARG A  46           
SHEET    5   A 5 TYR A 100  PRO A 101  1  O  TYR A 100   N  PHE A  29           
SHEET    1   B 2 LYS A  89  GLU A  90  0                                        
SHEET    2   B 2 ASP A  94  VAL A  95 -1  O  ASP A  94   N  GLU A  90           
CRYST1   63.200   63.200   76.100  90.00  90.00  90.00 P 43 21 2     8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.015823  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.015823  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013141        0.00000                         
ATOM      1  N   MET A   3      20.619   4.948  35.116  1.00 45.93           N  
ATOM      2  CA  MET A   3      21.882   4.950  35.804  1.00 46.07           C  
ATOM      3  C   MET A   3      23.030   4.770  34.802  1.00 51.03           C  
ATOM      4  O   MET A   3      23.460   5.802  34.270  1.00 55.91           O  
ATOM      5  CB  MET A   3      21.923   3.840  36.851  1.00 40.60           C  
ATOM      6  N   ARG A   4      23.524   3.608  34.356  1.00 56.61           N  
ATOM      7  CA  ARG A   4      24.755   3.634  33.565  1.00 57.06           C  
ATOM      8  C   ARG A   4      24.977   2.874  32.260  1.00 59.15           C  
ATOM      9  O   ARG A   4      25.442   3.453  31.273  1.00 54.90           O  
ATOM     10  CB  ARG A   4      25.881   3.263  34.515  1.00 59.15           C  
ATOM     11  N   ARG A   5      24.659   1.570  32.252  1.00 53.51           N  
ATOM     12  CA  ARG A   5      24.938   0.651  31.152  1.00 40.18           C  
ATOM     13  C   ARG A   5      24.452   0.988  29.733  1.00 36.62           C  
ATOM     14  O   ARG A   5      25.100   0.612  28.771  1.00 33.27           O  
ATOM     15  CB  ARG A   5      24.407  -0.661  31.633  1.00 43.29           C  
ATOM     16  N   TRP A   6      23.360   1.737  29.548  1.00 41.42           N  
ATOM     17  CA  TRP A   6      22.915   2.257  28.251  1.00 27.29           C  
ATOM     18  C   TRP A   6      23.794   3.406  27.720  1.00 35.75           C  
ATOM     19  O   TRP A   6      23.521   3.991  26.660  1.00 33.72           O  
ATOM     20  CB  TRP A   6      21.446   2.751  28.358  1.00 27.44           C  
ATOM     21  CG  TRP A   6      21.067   3.567  29.615  1.00 27.39           C  
ATOM     22  CD1 TRP A   6      20.295   2.998  30.601  1.00 26.31           C  
ATOM     23  CD2 TRP A   6      21.439   4.858  29.928  1.00 20.99           C  
ATOM     24  NE1 TRP A   6      20.172   3.890  31.535  1.00 21.61           N  
ATOM     25  CE2 TRP A   6      20.842   5.012  31.183  1.00 28.31           C  
ATOM     26  CE3 TRP A   6      22.178   5.900  29.362  1.00 17.07           C  
ATOM     27  CZ2 TRP A   6      20.988   6.216  31.883  1.00 28.63           C  
ATOM     28  CZ3 TRP A   6      22.323   7.098  30.061  1.00 22.84           C  
ATOM     29  CH2 TRP A   6      21.736   7.254  31.313  1.00 27.27           C  
ATOM     30  N   PHE A   7      24.800   3.861  28.479  1.00 37.95           N  
ATOM     31  CA  PHE A   7      25.708   4.922  28.053  1.00 39.46           C  
ATOM     32  C   PHE A   7      26.897   4.303  27.346  1.00 25.63           C  
ATOM     33  O   PHE A   7      27.599   3.418  27.821  1.00 27.57           O  
ATOM     34  CB  PHE A   7      26.192   5.748  29.262  1.00 39.36           C  
ATOM     35  CG  PHE A   7      27.133   6.914  28.955  1.00 37.48           C  
ATOM     36  CD1 PHE A   7      26.750   7.927  28.070  1.00 38.93           C  
ATOM     37  CD2 PHE A   7      28.391   6.964  29.571  1.00 33.45           C  
ATOM     38  CE1 PHE A   7      27.631   8.980  27.811  1.00 37.53           C  
ATOM     39  CE2 PHE A   7      29.259   8.016  29.305  1.00 29.72           C  
ATOM     40  CZ  PHE A   7      28.881   9.025  28.427  1.00 32.63           C  
ATOM     41  N   HIS A   8      27.150   4.802  26.176  1.00 27.29           N  
ATOM     42  CA  HIS A   8      28.201   4.261  25.382  1.00 34.23           C  
ATOM     43  C   HIS A   8      29.067   5.436  25.026  1.00 37.25           C  
ATOM     44  O   HIS A   8      28.713   6.216  24.150  1.00 40.40           O  
ATOM     45  CB  HIS A   8      27.611   3.634  24.148  1.00 46.77           C  
ATOM     46  CG  HIS A   8      26.879   2.318  24.385  1.00 47.48           C  
ATOM     47  ND1 HIS A   8      27.410   1.115  24.558  1.00 47.68           N  
ATOM     48  CD2 HIS A   8      25.522   2.176  24.421  1.00 46.52           C  
ATOM     49  CE1 HIS A   8      26.438   0.246  24.699  1.00 47.12           C  
ATOM     50  NE2 HIS A   8      25.312   0.903  24.613  1.00 47.78           N  
ATOM     51  N   PRO A   9      30.204   5.647  25.685  1.00 39.42           N  
ATOM     52  CA  PRO A   9      31.159   6.679  25.303  1.00 38.74           C  
ATOM     53  C   PRO A   9      31.895   6.323  24.012  1.00 54.56           C  
ATOM     54  O   PRO A   9      32.253   7.135  23.171  1.00 57.16           O  
ATOM     55  CB  PRO A   9      32.020   6.745  26.510  1.00 39.73           C  
ATOM     56  CG  PRO A   9      32.106   5.290  26.956  1.00 35.60           C  
ATOM     57  CD  PRO A   9      30.667   4.853  26.824  1.00 33.07           C  
ATOM     58  N   ASN A  10      32.019   5.012  23.875  1.00 64.88           N  
ATOM     59  CA  ASN A  10      32.780   4.290  22.886  1.00 67.77           C  
ATOM     60  C   ASN A  10      32.214   4.331  21.473  1.00 77.78           C  
ATOM     61  O   ASN A  10      32.847   3.755  20.581  1.00 92.29           O  
ATOM     62  CB  ASN A  10      32.914   2.804  23.406  1.00 61.53           C  
ATOM     63  CG  ASN A  10      31.622   2.090  23.886  1.00 40.77           C  
ATOM     64  OD1 ASN A  10      30.527   2.365  23.418  1.00 33.94           O  
ATOM     65  ND2 ASN A  10      31.587   1.222  24.883  1.00 40.51           N  
ATOM     66  N   ILE A  11      31.087   4.958  21.145  1.00 73.14           N  
ATOM     67  CA  ILE A  11      30.567   4.765  19.805  1.00 74.23           C  
ATOM     68  C   ILE A  11      30.236   6.008  18.985  1.00 72.55           C  
ATOM     69  O   ILE A  11      29.898   7.094  19.454  1.00 68.97           O  
ATOM     70  CB  ILE A  11      29.294   3.842  19.861  1.00 78.49           C  
ATOM     71  CG1 ILE A  11      28.214   4.459  20.728  1.00 85.23           C  
ATOM     72  CG2 ILE A  11      29.663   2.473  20.403  1.00 75.20           C  
ATOM     73  CD1 ILE A  11      26.900   3.665  20.673  1.00 91.10           C  
ATOM     74  N   THR A  12      30.350   5.798  17.683  1.00 73.78           N  
ATOM     75  CA  THR A  12      29.983   6.769  16.669  1.00 66.83           C  
ATOM     76  C   THR A  12      28.471   6.719  16.448  1.00 60.39           C  
ATOM     77  O   THR A  12      27.815   5.773  16.893  1.00 61.31           O  
ATOM     78  CB  THR A  12      30.752   6.403  15.384  1.00 69.89           C  
ATOM     79  OG1 THR A  12      30.581   4.997  15.135  1.00 72.46           O  
ATOM     80  CG2 THR A  12      32.227   6.733  15.518  1.00 74.80           C  
ATOM     81  N   GLY A  13      27.852   7.632  15.707  1.00 63.53           N  
ATOM     82  CA  GLY A  13      26.418   7.558  15.424  1.00 64.55           C  
ATOM     83  C   GLY A  13      26.117   6.288  14.639  1.00 63.45           C  
ATOM     84  O   GLY A  13      25.167   5.551  14.898  1.00 60.35           O  
ATOM     85  N   VAL A  14      27.008   5.987  13.704  1.00 68.04           N  
ATOM     86  CA  VAL A  14      26.905   4.801  12.877  1.00 67.80           C  
ATOM     87  C   VAL A  14      27.118   3.544  13.726  1.00 62.86           C  
ATOM     88  O   VAL A  14      26.373   2.581  13.494  1.00 60.91           O  
ATOM     89  CB  VAL A  14      27.940   4.944  11.704  1.00 71.83           C  
ATOM     90  CG1 VAL A  14      28.040   3.696  10.839  1.00 72.14           C  
ATOM     91  CG2 VAL A  14      27.442   6.024  10.757  1.00 67.97           C  
ATOM     92  N   GLU A  15      28.037   3.435  14.698  1.00 55.41           N  
ATOM     93  CA  GLU A  15      28.109   2.207  15.486  1.00 54.54           C  
ATOM     94  C   GLU A  15      26.914   2.108  16.428  1.00 56.06           C  
ATOM     95  O   GLU A  15      26.545   0.998  16.849  1.00 58.84           O  
ATOM     96  CB  GLU A  15      29.399   2.139  16.303  1.00 52.75           C  
ATOM     97  CG  GLU A  15      29.593   0.949  17.293  1.00 60.36           C  
ATOM     98  CD  GLU A  15      29.709  -0.516  16.816  1.00 57.63           C  
ATOM     99  OE1 GLU A  15      29.355  -0.844  15.686  1.00 61.30           O  
ATOM    100  OE2 GLU A  15      30.145  -1.359  17.600  1.00 50.71           O  
ATOM    101  N   ALA A  16      26.294   3.256  16.742  1.00 46.93           N  
ATOM    102  CA  ALA A  16      25.075   3.256  17.520  1.00 47.02           C  
ATOM    103  C   ALA A  16      23.948   2.652  16.676  1.00 46.87           C  
ATOM    104  O   ALA A  16      23.211   1.771  17.137  1.00 49.51           O  
ATOM    105  CB  ALA A  16      24.703   4.665  17.915  1.00 49.49           C  
ATOM    106  N   GLU A  17      23.795   3.057  15.417  1.00 47.11           N  
ATOM    107  CA  GLU A  17      22.798   2.441  14.537  1.00 48.04           C  
ATOM    108  C   GLU A  17      23.090   0.972  14.285  1.00 40.10           C  
ATOM    109  O   GLU A  17      22.161   0.184  14.201  1.00 36.77           O  
ATOM    110  CB  GLU A  17      22.760   3.133  13.212  1.00 42.10           C  
ATOM    111  CG  GLU A  17      22.080   4.447  13.368  1.00 47.81           C  
ATOM    112  CD  GLU A  17      22.510   5.406  12.285  1.00 61.05           C  
ATOM    113  OE1 GLU A  17      22.121   5.231  11.130  1.00 62.56           O  
ATOM    114  OE2 GLU A  17      23.250   6.330  12.612  1.00 72.71           O  
ATOM    115  N   ASN A  18      24.357   0.569  14.192  1.00 42.52           N  
ATOM    116  CA  ASN A  18      24.723  -0.829  14.042  1.00 49.83           C  
ATOM    117  C   ASN A  18      24.181  -1.579  15.252  1.00 47.52           C  
ATOM    118  O   ASN A  18      23.243  -2.365  15.095  1.00 47.56           O  
ATOM    119  CB  ASN A  18      26.245  -1.001  13.968  1.00 52.28           C  
ATOM    120  CG  ASN A  18      26.668  -2.466  13.940  1.00 52.26           C  
ATOM    121  OD1 ASN A  18      26.807  -3.105  14.981  1.00 54.43           O  
ATOM    122  ND2 ASN A  18      26.928  -3.064  12.790  1.00 57.34           N  
ATOM    123  N   LEU A  19      24.658  -1.245  16.453  1.00 39.47           N  
ATOM    124  CA  LEU A  19      24.232  -1.894  17.681  1.00 46.36           C  
ATOM    125  C   LEU A  19      22.744  -2.064  17.847  1.00 45.47           C  
ATOM    126  O   LEU A  19      22.257  -3.153  18.181  1.00 47.40           O  
ATOM    127  CB  LEU A  19      24.724  -1.125  18.877  1.00 47.85           C  
ATOM    128  CG  LEU A  19      25.870  -1.742  19.622  1.00 48.67           C  
ATOM    129  CD1 LEU A  19      27.002  -2.058  18.668  1.00 48.38           C  
ATOM    130  CD2 LEU A  19      26.304  -0.772  20.714  1.00 49.18           C  
ATOM    131  N   LEU A  20      22.034  -0.969  17.598  1.00 37.52           N  
ATOM    132  CA  LEU A  20      20.590  -0.997  17.696  1.00 34.28           C  
ATOM    133  C   LEU A  20      19.905  -1.852  16.608  1.00 39.36           C  
ATOM    134  O   LEU A  20      18.920  -2.556  16.901  1.00 29.45           O  
ATOM    135  CB  LEU A  20      20.072   0.447  17.652  1.00 31.25           C  
ATOM    136  CG  LEU A  20      20.194   1.353  18.873  1.00 25.23           C  
ATOM    137  CD1 LEU A  20      20.157   2.775  18.396  1.00 28.05           C  
ATOM    138  CD2 LEU A  20      19.056   1.146  19.825  1.00 20.11           C  
ATOM    139  N   LEU A  21      20.384  -1.852  15.361  1.00 33.54           N  
ATOM    140  CA  LEU A  21      19.723  -2.612  14.329  1.00 29.86           C  
ATOM    141  C   LEU A  21      20.068  -4.068  14.351  1.00 27.06           C  
ATOM    142  O   LEU A  21      19.243  -4.854  13.867  1.00 31.85           O  
ATOM    143  CB  LEU A  21      20.072  -2.083  12.991  1.00 30.44           C  
ATOM    144  CG  LEU A  21      19.677  -0.633  12.822  1.00 32.24           C  
ATOM    145  CD1 LEU A  21      20.272  -0.220  11.510  1.00 24.67           C  
ATOM    146  CD2 LEU A  21      18.171  -0.405  12.943  1.00 29.55           C  
ATOM    147  N   THR A  22      21.233  -4.456  14.887  1.00 32.37           N  
ATOM    148  CA  THR A  22      21.589  -5.874  14.952  1.00 38.31           C  
ATOM    149  C   THR A  22      21.248  -6.480  16.300  1.00 31.85           C  
ATOM    150  O   THR A  22      20.915  -7.666  16.369  1.00 36.63           O  
ATOM    151  CB  THR A  22      23.128  -6.195  14.705  1.00 37.59           C  
ATOM    152  OG1 THR A  22      23.902  -5.592  15.744  1.00 42.95           O  
ATOM    153  CG2 THR A  22      23.596  -5.714  13.361  1.00 22.08           C  
ATOM    154  N   ARG A  23      21.404  -5.747  17.390  1.00 28.31           N  
ATOM    155  CA  ARG A  23      21.098  -6.314  18.676  1.00 27.95           C  
ATOM    156  C   ARG A  23      19.958  -5.577  19.339  1.00 21.57           C  
ATOM    157  O   ARG A  23      19.637  -5.871  20.493  1.00 25.08           O  
ATOM    158  CB  ARG A  23      22.341  -6.281  19.553  1.00 41.19           C  
ATOM    159  CG  ARG A  23      23.509  -7.089  18.992  1.00 51.34           C  
ATOM    160  CD  ARG A  23      24.507  -7.310  20.117  1.00 68.77           C  
ATOM    161  NE  ARG A  23      25.895  -7.287  19.662  1.00 83.62           N  
ATOM    162  CZ  ARG A  23      26.741  -6.270  19.923  1.00 92.99           C  
ATOM    163  NH1 ARG A  23      26.395  -5.183  20.623  1.00 97.53           N  
ATOM    164  NH2 ARG A  23      27.990  -6.339  19.474  1.00 92.69           N  
ATOM    165  N   GLY A  24      19.286  -4.644  18.677  1.00 21.39           N  
ATOM    166  CA  GLY A  24      18.139  -4.012  19.290  1.00 26.66           C  
ATOM    167  C   GLY A  24      16.842  -4.568  18.722  1.00 20.27           C  
ATOM    168  O   GLY A  24      16.795  -5.355  17.764  1.00 28.40           O  
ATOM    169  N   VAL A  25      15.791  -4.080  19.359  1.00 26.89           N  
ATOM    170  CA  VAL A  25      14.398  -4.363  19.069  1.00 24.68           C  
ATOM    171  C   VAL A  25      13.672  -2.987  19.068  1.00 31.26           C  
ATOM    172  O   VAL A  25      14.240  -2.009  19.586  1.00 29.12           O  
ATOM    173  CB  VAL A  25      14.087  -5.337  20.202  1.00 27.02           C  
ATOM    174  CG1 VAL A  25      13.057  -4.758  21.161  1.00 21.34           C  
ATOM    175  CG2 VAL A  25      13.726  -6.664  19.572  1.00 26.95           C  
ATOM    176  N   ASP A  26      12.451  -2.761  18.568  1.00 26.32           N  
ATOM    177  CA  ASP A  26      11.851  -1.434  18.701  1.00 27.55           C  
ATOM    178  C   ASP A  26      11.531  -1.062  20.134  1.00 21.80           C  
ATOM    179  O   ASP A  26      10.766  -1.701  20.862  1.00 30.92           O  
ATOM    180  CB  ASP A  26      10.551  -1.287  17.915  1.00 26.62           C  
ATOM    181  CG  ASP A  26      10.686  -1.372  16.404  1.00 27.16           C  
ATOM    182  OD1 ASP A  26      11.774  -1.143  15.883  1.00 36.08           O  
ATOM    183  OD2 ASP A  26       9.694  -1.667  15.745  1.00 27.40           O  
ATOM    184  N   GLY A  27      12.170   0.026  20.505  1.00 20.05           N  
ATOM    185  CA  GLY A  27      12.087   0.544  21.848  1.00 14.19           C  
ATOM    186  C   GLY A  27      13.460   0.557  22.501  1.00 16.05           C  
ATOM    187  O   GLY A  27      13.578   1.044  23.627  1.00 24.88           O  
ATOM    188  N   SER A  28      14.476  -0.028  21.863  1.00 25.40           N  
ATOM    189  CA  SER A  28      15.857  -0.071  22.335  1.00 23.07           C  
ATOM    190  C   SER A  28      16.500   1.301  22.250  1.00 18.24           C  
ATOM    191  O   SER A  28      16.171   2.058  21.335  1.00 26.15           O  
ATOM    192  CB  SER A  28      16.624  -1.096  21.481  1.00 25.33           C  
ATOM    193  OG  SER A  28      16.174  -2.423  21.750  1.00 18.56           O  
ATOM    194  N   PHE A  29      17.387   1.700  23.153  1.00 18.43           N  
ATOM    195  CA  PHE A  29      17.957   3.041  23.088  1.00 21.41           C  
ATOM    196  C   PHE A  29      19.242   2.966  23.851  1.00 21.89           C  
ATOM    197  O   PHE A  29      19.437   2.052  24.658  1.00 16.92           O  
ATOM    198  CB  PHE A  29      17.074   4.149  23.747  1.00 21.99           C  
ATOM    199  CG  PHE A  29      16.943   4.029  25.259  1.00 25.56           C  
ATOM    200  CD1 PHE A  29      15.930   3.206  25.773  1.00 26.12           C  
ATOM    201  CD2 PHE A  29      17.889   4.630  26.111  1.00 27.74           C  
ATOM    202  CE1 PHE A  29      15.879   2.970  27.132  1.00 14.83           C  
ATOM    203  CE2 PHE A  29      17.839   4.390  27.479  1.00 21.09           C  
ATOM    204  CZ  PHE A  29      16.835   3.559  27.978  1.00 30.22           C  
ATOM    205  N   LEU A  30      20.056   3.978  23.605  1.00 25.19           N  
ATOM    206  CA  LEU A  30      21.323   4.158  24.265  1.00 25.80           C  
ATOM    207  C   LEU A  30      21.547   5.666  24.301  1.00 30.53           C  
ATOM    208  O   LEU A  30      20.817   6.401  23.622  1.00 26.90           O  
ATOM    209  CB  LEU A  30      22.404   3.432  23.451  1.00 27.19           C  
ATOM    210  CG  LEU A  30      22.602   3.697  21.953  1.00 32.77           C  
ATOM    211  CD1 LEU A  30      23.525   4.892  21.659  1.00 23.36           C  
ATOM    212  CD2 LEU A  30      23.175   2.408  21.377  1.00 35.19           C  
ATOM    213  N   ALA A  31      22.499   6.170  25.088  1.00 34.22           N  
ATOM    214  CA  ALA A  31      22.888   7.580  24.998  1.00 38.77           C  
ATOM    215  C   ALA A  31      24.380   7.582  24.626  1.00 39.65           C  
ATOM    216  O   ALA A  31      25.162   6.680  24.959  1.00 33.41           O  
ATOM    217  CB  ALA A  31      22.731   8.330  26.337  1.00 36.15           C  
ATOM    218  N   ARG A  32      24.847   8.586  23.919  1.00 43.16           N  
ATOM    219  CA  ARG A  32      26.238   8.640  23.512  1.00 49.66           C  
ATOM    220  C   ARG A  32      26.686  10.096  23.378  1.00 56.69           C  
ATOM    221  O   ARG A  32      25.830  10.973  23.163  1.00 55.49           O  
ATOM    222  CB  ARG A  32      26.367   7.873  22.181  1.00 48.94           C  
ATOM    223  CG  ARG A  32      25.353   8.319  21.152  1.00 37.45           C  
ATOM    224  CD  ARG A  32      25.559   7.613  19.846  1.00 38.59           C  
ATOM    225  NE  ARG A  32      24.703   8.319  18.922  1.00 35.41           N  
ATOM    226  CZ  ARG A  32      25.122   9.444  18.347  1.00 41.41           C  
ATOM    227  NH1 ARG A  32      26.357   9.946  18.575  1.00 38.77           N  
ATOM    228  NH2 ARG A  32      24.229  10.137  17.636  1.00 45.08           N  
ATOM    229  N   PRO A  33      27.975  10.448  23.542  1.00 59.82           N  
ATOM    230  CA  PRO A  33      28.474  11.821  23.456  1.00 52.65           C  
ATOM    231  C   PRO A  33      28.136  12.403  22.106  1.00 46.46           C  
ATOM    232  O   PRO A  33      28.124  11.670  21.114  1.00 50.18           O  
ATOM    233  CB  PRO A  33      29.952  11.683  23.705  1.00 57.96           C  
ATOM    234  CG  PRO A  33      30.059  10.410  24.526  1.00 63.14           C  
ATOM    235  CD  PRO A  33      29.080   9.523  23.786  1.00 62.64           C  
ATOM    236  N   SER A  34      27.825  13.684  22.007  1.00 47.34           N  
ATOM    237  CA  SER A  34      27.465  14.236  20.708  1.00 56.48           C  
ATOM    238  C   SER A  34      28.641  14.679  19.841  1.00 59.79           C  
ATOM    239  O   SER A  34      29.647  15.177  20.351  1.00 56.72           O  
ATOM    240  CB  SER A  34      26.522  15.424  20.891  1.00 45.54           C  
ATOM    241  N   LYS A  35      28.547  14.457  18.524  1.00 74.47           N  
ATOM    242  CA  LYS A  35      29.490  15.017  17.553  1.00 80.85           C  
ATOM    243  C   LYS A  35      28.888  16.351  17.078  1.00 81.94           C  
ATOM    244  O   LYS A  35      29.587  17.348  16.946  1.00 69.59           O  
ATOM    245  CB  LYS A  35      29.667  14.081  16.343  1.00 82.64           C  
ATOM    246  CG  LYS A  35      30.637  14.606  15.269  1.00 83.24           C  
ATOM    247  CD  LYS A  35      30.601  13.835  13.953  1.00 73.67           C  
ATOM    248  N   SER A  36      27.570  16.418  16.860  1.00 89.58           N  
ATOM    249  CA  SER A  36      26.879  17.633  16.442  1.00 96.59           C  
ATOM    250  C   SER A  36      27.099  18.849  17.344  1.00100.82           C  
ATOM    251  O   SER A  36      26.811  19.979  16.940  1.00104.48           O  
ATOM    252  CB  SER A  36      25.386  17.330  16.360  1.00 99.78           C  
ATOM    253  OG  SER A  36      24.593  18.310  15.699  1.00104.35           O  
ATOM    254  N   ASN A  37      27.512  18.640  18.593  1.00101.49           N  
ATOM    255  CA  ASN A  37      27.825  19.694  19.543  1.00 98.03           C  
ATOM    256  C   ASN A  37      28.495  18.907  20.659  1.00100.60           C  
ATOM    257  O   ASN A  37      27.843  18.038  21.249  1.00106.69           O  
ATOM    258  CB  ASN A  37      26.565  20.359  20.096  1.00 94.81           C  
ATOM    259  N   PRO A  38      29.799  19.034  20.903  1.00101.09           N  
ATOM    260  CA  PRO A  38      30.457  18.438  22.060  1.00 97.71           C  
ATOM    261  C   PRO A  38      29.887  18.959  23.365  1.00 92.84           C  
ATOM    262  O   PRO A  38      29.314  20.051  23.415  1.00 94.75           O  
ATOM    263  CB  PRO A  38      31.909  18.770  21.848  1.00100.07           C  
ATOM    264  CG  PRO A  38      32.012  18.725  20.340  1.00102.19           C  
ATOM    265  CD  PRO A  38      30.778  19.510  19.936  1.00100.80           C  
ATOM    266  N   GLY A  39      29.989  18.170  24.428  1.00 91.92           N  
ATOM    267  CA  GLY A  39      29.498  18.547  25.756  1.00 88.06           C  
ATOM    268  C   GLY A  39      28.132  17.946  26.059  1.00 77.68           C  
ATOM    269  O   GLY A  39      27.759  17.599  27.193  1.00 64.51           O  
ATOM    270  N   ASP A  40      27.394  17.951  24.962  1.00 69.90           N  
ATOM    271  CA  ASP A  40      26.092  17.371  24.882  1.00 65.82           C  
ATOM    272  C   ASP A  40      26.220  15.887  24.580  1.00 60.66           C  
ATOM    273  O   ASP A  40      27.293  15.355  24.237  1.00 46.32           O  
ATOM    274  CB  ASP A  40      25.350  18.112  23.793  1.00 65.23           C  
ATOM    275  CG  ASP A  40      24.854  19.494  24.205  1.00 67.09           C  
ATOM    276  OD1 ASP A  40      25.475  20.168  25.034  1.00 69.52           O  
ATOM    277  OD2 ASP A  40      23.817  19.894  23.679  1.00 64.48           O  
ATOM    278  N   PHE A  41      25.065  15.234  24.696  1.00 54.43           N  
ATOM    279  CA  PHE A  41      24.920  13.801  24.447  1.00 46.67           C  
ATOM    280  C   PHE A  41      23.756  13.636  23.499  1.00 38.67           C  
ATOM    281  O   PHE A  41      23.002  14.601  23.284  1.00 46.64           O  
ATOM    282  CB  PHE A  41      24.588  13.036  25.713  1.00 45.12           C  
ATOM    283  CG  PHE A  41      25.679  13.192  26.739  1.00 47.89           C  
ATOM    284  CD1 PHE A  41      26.739  12.288  26.751  1.00 39.30           C  
ATOM    285  CD2 PHE A  41      25.615  14.258  27.650  1.00 50.85           C  
ATOM    286  CE1 PHE A  41      27.752  12.453  27.686  1.00 45.83           C  
ATOM    287  CE2 PHE A  41      26.640  14.414  28.584  1.00 54.52           C  
ATOM    288  CZ  PHE A  41      27.707  13.509  28.599  1.00 50.71           C  
ATOM    289  N   THR A  42      23.575  12.447  22.940  1.00 37.40           N  
ATOM    290  CA  THR A  42      22.442  12.186  22.082  1.00 40.02           C  
ATOM    291  C   THR A  42      21.921  10.761  22.290  1.00 35.69           C  
ATOM    292  O   THR A  42      22.702   9.821  22.512  1.00 28.42           O  
ATOM    293  CB  THR A  42      22.943  12.537  20.654  1.00 38.63           C  
ATOM    294  OG1 THR A  42      21.951  12.103  19.733  1.00 51.70           O  
ATOM    295  CG2 THR A  42      24.285  11.981  20.374  1.00 35.01           C  
ATOM    296  N   LEU A  43      20.582  10.701  22.419  1.00 32.64           N  
ATOM    297  CA  LEU A  43      19.796   9.456  22.575  1.00 35.34           C  
ATOM    298  C   LEU A  43      19.561   8.832  21.203  1.00 40.67           C  
ATOM    299  O   LEU A  43      18.927   9.485  20.373  1.00 41.29           O  
ATOM    300  CB  LEU A  43      18.382   9.676  23.157  1.00 28.03           C  
ATOM    301  CG  LEU A  43      18.183  10.045  24.623  1.00 28.54           C  
ATOM    302  CD1 LEU A  43      16.769  10.474  24.889  1.00 28.35           C  
ATOM    303  CD2 LEU A  43      18.512   8.842  25.479  1.00 26.13           C  
ATOM    304  N   SER A  44      20.034   7.630  20.890  1.00 43.96           N  
ATOM    305  CA  SER A  44      19.762   6.980  19.616  1.00 30.68           C  
ATOM    306  C   SER A  44      18.730   5.948  20.031  1.00 34.60           C  
ATOM    307  O   SER A  44      18.962   5.114  20.928  1.00 32.52           O  
ATOM    308  CB  SER A  44      21.022   6.334  19.102  1.00 37.32           C  
ATOM    309  OG  SER A  44      22.069   7.298  18.938  1.00 43.07           O  
ATOM    310  N   VAL A  45      17.537   6.134  19.468  1.00 28.27           N  
ATOM    311  CA  VAL A  45      16.378   5.329  19.786  1.00 34.11           C  
ATOM    312  C   VAL A  45      15.907   4.538  18.578  1.00 33.89           C  
ATOM    313  O   VAL A  45      15.849   5.089  17.476  1.00 32.72           O  
ATOM    314  CB  VAL A  45      15.222   6.208  20.244  1.00 27.33           C  
ATOM    315  CG1 VAL A  45      14.117   5.349  20.844  1.00 32.76           C  
ATOM    316  CG2 VAL A  45      15.746   7.216  21.248  1.00 45.42           C  
ATOM    317  N   ARG A  46      15.526   3.265  18.759  1.00 38.58           N  
ATOM    318  CA  ARG A  46      15.008   2.463  17.658  1.00 36.46           C  
ATOM    319  C   ARG A  46      13.487   2.412  17.678  1.00 24.51           C  
ATOM    320  O   ARG A  46      12.860   2.092  18.705  1.00 20.31           O  
ATOM    321  CB  ARG A  46      15.573   1.028  17.724  1.00 30.04           C  
ATOM    322  CG  ARG A  46      15.064   0.272  16.514  1.00 31.33           C  
ATOM    323  CD  ARG A  46      15.726  -1.065  16.391  1.00 35.97           C  
ATOM    324  NE  ARG A  46      14.754  -1.912  15.737  1.00 42.48           N  
ATOM    325  CZ  ARG A  46      15.037  -3.105  15.233  1.00 38.16           C  
ATOM    326  NH1 ARG A  46      16.272  -3.595  15.284  1.00 40.84           N  
ATOM    327  NH2 ARG A  46      14.038  -3.823  14.703  1.00 40.22           N  
ATOM    328  N   ARG A  47      12.878   2.778  16.560  1.00 26.44           N  
ATOM    329  CA  ARG A  47      11.438   2.642  16.431  1.00 31.66           C  
ATOM    330  C   ARG A  47      11.134   2.436  14.970  1.00 29.36           C  
ATOM    331  O   ARG A  47      11.761   2.967  14.053  1.00 29.97           O  
ATOM    332  CB  ARG A  47      10.680   3.877  16.940  1.00 45.09           C  
ATOM    333  CG  ARG A  47      10.375   5.126  16.105  1.00 51.07           C  
ATOM    334  CD  ARG A  47       9.468   6.016  16.976  1.00 58.00           C  
ATOM    335  NE  ARG A  47       8.627   6.969  16.261  1.00 64.37           N  
ATOM    336  CZ  ARG A  47       9.127   7.995  15.575  1.00 71.88           C  
ATOM    337  NH1 ARG A  47      10.435   8.236  15.491  1.00 69.78           N  
ATOM    338  NH2 ARG A  47       8.288   8.792  14.930  1.00 77.28           N  
ATOM    339  N   ASN A  48      10.179   1.541  14.817  1.00 29.79           N  
ATOM    340  CA  ASN A  48       9.684   1.089  13.535  1.00 36.78           C  
ATOM    341  C   ASN A  48      10.793   0.655  12.604  1.00 34.40           C  
ATOM    342  O   ASN A  48      10.834   0.982  11.433  1.00 45.79           O  
ATOM    343  CB  ASN A  48       8.835   2.194  12.913  1.00 43.67           C  
ATOM    344  CG  ASN A  48       7.482   2.267  13.621  1.00 64.16           C  
ATOM    345  OD1 ASN A  48       7.323   2.687  14.775  1.00 68.32           O  
ATOM    346  ND2 ASN A  48       6.417   1.833  12.974  1.00 78.60           N  
ATOM    347  N   GLY A  49      11.775  -0.071  13.121  1.00 42.38           N  
ATOM    348  CA  GLY A  49      12.856  -0.610  12.318  1.00 42.53           C  
ATOM    349  C   GLY A  49      13.993   0.373  12.109  1.00 49.01           C  
ATOM    350  O   GLY A  49      15.097  -0.059  11.772  1.00 53.70           O  
ATOM    351  N   ALA A  50      13.766   1.672  12.313  1.00 52.24           N  
ATOM    352  CA  ALA A  50      14.770   2.709  12.147  1.00 54.00           C  
ATOM    353  C   ALA A  50      15.326   3.292  13.449  1.00 51.74           C  
ATOM    354  O   ALA A  50      14.818   3.035  14.547  1.00 50.02           O  
ATOM    355  CB  ALA A  50      14.153   3.826  11.345  1.00 63.88           C  
ATOM    356  N   VAL A  51      16.395   4.070  13.335  1.00 51.21           N  
ATOM    357  CA  VAL A  51      17.041   4.742  14.453  1.00 42.32           C  
ATOM    358  C   VAL A  51      16.869   6.261  14.345  1.00 44.10           C  
ATOM    359  O   VAL A  51      17.148   6.866  13.299  1.00 36.65           O  
ATOM    360  CB  VAL A  51      18.524   4.349  14.443  1.00 33.83           C  
ATOM    361  CG1 VAL A  51      19.327   5.117  15.484  1.00 26.90           C  
ATOM    362  CG2 VAL A  51      18.604   2.865  14.706  1.00 34.80           C  
ATOM    363  N   THR A  52      16.400   6.883  15.422  1.00 49.46           N  
ATOM    364  CA  THR A  52      16.283   8.328  15.573  1.00 43.75           C  
ATOM    365  C   THR A  52      17.395   8.785  16.516  1.00 45.41           C  
ATOM    366  O   THR A  52      17.771   8.059  17.440  1.00 42.45           O  
ATOM    367  CB  THR A  52      14.924   8.688  16.183  1.00 42.62           C  
ATOM    368  OG1 THR A  52      13.940   8.233  15.273  1.00 53.98           O  
ATOM    369  CG2 THR A  52      14.737  10.182  16.407  1.00 41.23           C  
ATOM    370  N   HIS A  53      17.982   9.965  16.306  1.00 45.58           N  
ATOM    371  CA  HIS A  53      18.976  10.515  17.220  1.00 39.17           C  
ATOM    372  C   HIS A  53      18.353  11.788  17.763  1.00 40.89           C  
ATOM    373  O   HIS A  53      17.818  12.588  16.992  1.00 48.66           O  
ATOM    374  CB  HIS A  53      20.223  10.830  16.484  1.00 36.35           C  
ATOM    375  CG  HIS A  53      20.866   9.557  15.965  1.00 36.63           C  
ATOM    376  ND1 HIS A  53      21.718   8.757  16.605  1.00 36.48           N  
ATOM    377  CD2 HIS A  53      20.678   9.057  14.699  1.00 29.18           C  
ATOM    378  CE1 HIS A  53      22.056   7.796  15.777  1.00 33.33           C  
ATOM    379  NE2 HIS A  53      21.426   7.988  14.639  1.00 33.38           N  
ATOM    380  N   ILE A  54      18.304  11.948  19.087  1.00 40.31           N  
ATOM    381  CA  ILE A  54      17.671  13.060  19.777  1.00 31.58           C  
ATOM    382  C   ILE A  54      18.790  13.712  20.586  1.00 32.31           C  
ATOM    383  O   ILE A  54      19.650  13.051  21.174  1.00 27.88           O  
ATOM    384  CB  ILE A  54      16.555  12.517  20.674  1.00 33.83           C  
ATOM    385  CG1 ILE A  54      15.544  11.771  19.834  1.00 31.41           C  
ATOM    386  CG2 ILE A  54      15.855  13.663  21.404  1.00 32.10           C  
ATOM    387  CD1 ILE A  54      14.468  11.124  20.728  1.00 40.95           C  
ATOM    388  N   LYS A  55      18.796  15.029  20.574  1.00 38.57           N  
ATOM    389  CA  LYS A  55      19.879  15.821  21.111  1.00 42.24           C  
ATOM    390  C   LYS A  55      19.494  16.202  22.505  1.00 37.67           C  
ATOM    391  O   LYS A  55      18.346  16.612  22.746  1.00 34.59           O  
ATOM    392  CB  LYS A  55      20.097  17.093  20.289  1.00 54.08           C  
ATOM    393  CG  LYS A  55      20.722  16.841  18.918  1.00 60.49           C  
ATOM    394  CD  LYS A  55      20.944  18.140  18.159  1.00 66.67           C  
ATOM    395  N   ILE A  56      20.486  15.986  23.379  1.00 31.57           N  
ATOM    396  CA  ILE A  56      20.345  16.272  24.793  1.00 29.60           C  
ATOM    397  C   ILE A  56      21.279  17.463  24.967  1.00 28.43           C  
ATOM    398  O   ILE A  56      22.456  17.431  24.594  1.00 28.38           O  
ATOM    399  CB  ILE A  56      20.807  15.064  25.676  1.00 26.62           C  
ATOM    400  CG1 ILE A  56      20.000  13.781  25.438  1.00 26.03           C  
ATOM    401  CG2 ILE A  56      20.555  15.441  27.116  1.00 24.75           C  
ATOM    402  CD1 ILE A  56      20.494  12.511  26.152  1.00 18.97           C  
ATOM    403  N   GLN A  57      20.706  18.510  25.540  1.00 30.36           N  
ATOM    404  CA  GLN A  57      21.404  19.734  25.879  1.00 30.87           C  
ATOM    405  C   GLN A  57      21.932  19.707  27.314  1.00 28.08           C  
ATOM    406  O   GLN A  57      21.209  19.391  28.263  1.00 26.71           O  
ATOM    407  CB  GLN A  57      20.481  20.916  25.751  1.00 26.64           C  
ATOM    408  CG  GLN A  57      21.198  22.237  26.011  1.00 35.98           C  
ATOM    409  CD  GLN A  57      20.304  23.461  25.912  1.00 28.00           C  
ATOM    410  OE1 GLN A  57      20.715  24.459  25.333  1.00 38.56           O  
ATOM    411  NE2 GLN A  57      19.115  23.476  26.495  1.00 26.40           N  
ATOM    412  N   ASN A  58      23.175  20.134  27.446  1.00 20.66           N  
ATOM    413  CA  ASN A  58      23.788  20.267  28.732  1.00 23.68           C  
ATOM    414  C   ASN A  58      24.262  21.715  28.723  1.00 29.46           C  
ATOM    415  O   ASN A  58      25.214  22.073  28.019  1.00 26.46           O  
ATOM    416  CB  ASN A  58      24.953  19.315  28.849  1.00 20.43           C  
ATOM    417  CG  ASN A  58      25.823  19.574  30.067  1.00 31.94           C  
ATOM    418  OD1 ASN A  58      25.475  20.339  30.982  1.00 35.22           O  
ATOM    419  ND2 ASN A  58      26.993  18.941  30.115  1.00 39.40           N  
ATOM    420  N   THR A  59      23.536  22.537  29.492  1.00 24.41           N  
ATOM    421  CA  THR A  59      23.810  23.948  29.636  1.00 23.29           C  
ATOM    422  C   THR A  59      24.804  24.176  30.746  1.00 26.41           C  
ATOM    423  O   THR A  59      24.987  25.297  31.217  1.00 35.62           O  
ATOM    424  CB  THR A  59      22.568  24.757  30.019  1.00 24.70           C  
ATOM    425  OG1 THR A  59      22.187  24.312  31.319  1.00 23.45           O  
ATOM    426  CG2 THR A  59      21.428  24.615  29.038  1.00 28.54           C  
ATOM    427  N   GLY A  60      25.299  23.129  31.364  1.00 27.68           N  
ATOM    428  CA  GLY A  60      26.180  23.308  32.496  1.00 24.04           C  
ATOM    429  C   GLY A  60      25.331  23.644  33.707  1.00 26.22           C  
ATOM    430  O   GLY A  60      25.889  23.679  34.811  1.00 34.29           O  
ATOM    431  N   ASP A  61      24.021  23.904  33.587  1.00 20.13           N  
ATOM    432  CA  ASP A  61      23.211  24.163  34.765  1.00 21.26           C  
ATOM    433  C   ASP A  61      22.123  23.148  34.962  1.00 17.71           C  
ATOM    434  O   ASP A  61      21.478  23.174  36.004  1.00 15.52           O  
ATOM    435  CB  ASP A  61      22.542  25.517  34.696  1.00 31.80           C  
ATOM    436  CG  ASP A  61      23.361  26.717  35.160  1.00 35.79           C  
ATOM    437  OD1 ASP A  61      23.292  27.036  36.344  1.00 61.07           O  
ATOM    438  OD2 ASP A  61      24.008  27.372  34.351  1.00 29.07           O  
ATOM    439  N   TYR A  62      21.808  22.409  33.892  1.00 23.73           N  
ATOM    440  CA  TYR A  62      20.830  21.320  33.887  1.00 20.60           C  
ATOM    441  C   TYR A  62      20.967  20.622  32.537  1.00 23.16           C  
ATOM    442  O   TYR A  62      21.706  21.059  31.648  1.00 19.55           O  
ATOM    443  CB  TYR A  62      19.402  21.852  34.037  1.00 22.17           C  
ATOM    444  CG  TYR A  62      19.032  22.841  32.924  1.00 26.73           C  
ATOM    445  CD1 TYR A  62      18.542  22.381  31.700  1.00 23.12           C  
ATOM    446  CD2 TYR A  62      19.184  24.212  33.121  1.00 24.72           C  
ATOM    447  CE1 TYR A  62      18.212  23.264  30.689  1.00 22.16           C  
ATOM    448  CE2 TYR A  62      18.849  25.107  32.115  1.00 21.87           C  
ATOM    449  CZ  TYR A  62      18.368  24.617  30.913  1.00 23.72           C  
ATOM    450  OH  TYR A  62      18.014  25.480  29.908  1.00 22.13           O  
ATOM    451  N   TYR A  63      20.224  19.547  32.341  1.00 28.09           N  
ATOM    452  CA  TYR A  63      20.148  18.806  31.095  1.00 19.96           C  
ATOM    453  C   TYR A  63      18.708  18.916  30.658  1.00 24.14           C  
ATOM    454  O   TYR A  63      17.829  18.915  31.542  1.00 19.76           O  
ATOM    455  CB  TYR A  63      20.378  17.319  31.275  1.00 21.99           C  
ATOM    456  CG  TYR A  63      21.810  17.013  31.539  1.00 13.13           C  
ATOM    457  CD1 TYR A  63      22.335  17.219  32.813  1.00 16.11           C  
ATOM    458  CD2 TYR A  63      22.595  16.543  30.480  1.00 21.29           C  
ATOM    459  CE1 TYR A  63      23.697  16.957  33.012  1.00 23.57           C  
ATOM    460  CE2 TYR A  63      23.948  16.271  30.682  1.00 18.93           C  
ATOM    461  CZ  TYR A  63      24.485  16.488  31.951  1.00 23.36           C  
ATOM    462  OH  TYR A  63      25.829  16.270  32.162  1.00 30.76           O  
ATOM    463  N   ASP A  64      18.455  19.042  29.351  1.00 23.56           N  
ATOM    464  CA  ASP A  64      17.104  18.844  28.860  1.00 15.82           C  
ATOM    465  C   ASP A  64      17.160  18.391  27.414  1.00 19.03           C  
ATOM    466  O   ASP A  64      18.229  17.999  26.912  1.00 23.61           O  
ATOM    467  CB  ASP A  64      16.271  20.101  28.998  1.00 14.15           C  
ATOM    468  CG  ASP A  64      16.546  21.287  28.104  1.00 25.44           C  
ATOM    469  OD1 ASP A  64      17.518  21.337  27.345  1.00 29.02           O  
ATOM    470  OD2 ASP A  64      15.714  22.176  28.188  1.00 27.30           O  
ATOM    471  N   LEU A  65      16.008  18.390  26.752  1.00 29.67           N  
ATOM    472  CA  LEU A  65      15.933  18.041  25.346  1.00 34.56           C  
ATOM    473  C   LEU A  65      15.510  19.333  24.650  1.00 46.20           C  
ATOM    474  O   LEU A  65      14.422  19.381  24.064  1.00 55.13           O  
ATOM    475  CB  LEU A  65      14.897  16.947  25.163  1.00 23.61           C  
ATOM    476  CG  LEU A  65      15.086  15.700  26.002  1.00 25.22           C  
ATOM    477  CD1 LEU A  65      13.883  14.856  25.815  1.00 15.74           C  
ATOM    478  CD2 LEU A  65      16.378  14.979  25.636  1.00 18.83           C  
ATOM    479  N   TYR A  66      16.366  20.389  24.782  1.00 46.23           N  
ATOM    480  CA  TYR A  66      16.130  21.765  24.322  1.00 34.55           C  
ATOM    481  C   TYR A  66      14.663  22.161  24.469  1.00 31.41           C  
ATOM    482  O   TYR A  66      13.960  22.561  23.553  1.00 39.91           O  
ATOM    483  CB  TYR A  66      16.524  21.913  22.893  1.00 27.11           C  
ATOM    484  CG  TYR A  66      17.998  21.726  22.702  1.00 31.10           C  
ATOM    485  CD1 TYR A  66      18.515  20.459  22.472  1.00 31.34           C  
ATOM    486  CD2 TYR A  66      18.829  22.852  22.734  1.00 30.19           C  
ATOM    487  CE1 TYR A  66      19.892  20.314  22.278  1.00 38.56           C  
ATOM    488  CE2 TYR A  66      20.205  22.717  22.539  1.00 25.60           C  
ATOM    489  CZ  TYR A  66      20.725  21.443  22.315  1.00 36.81           C  
ATOM    490  OH  TYR A  66      22.088  21.280  22.199  1.00 45.54           O  
ATOM    491  N   GLY A  67      14.194  21.980  25.680  1.00 26.81           N  
ATOM    492  CA  GLY A  67      12.819  22.208  26.021  1.00 23.55           C  
ATOM    493  C   GLY A  67      12.476  21.081  26.969  1.00 26.75           C  
ATOM    494  O   GLY A  67      13.261  20.153  27.202  1.00 31.66           O  
ATOM    495  N   GLY A  68      11.323  21.127  27.569  1.00 24.73           N  
ATOM    496  CA  GLY A  68      10.909  20.066  28.454  1.00 31.58           C  
ATOM    497  C   GLY A  68      11.457  20.229  29.834  1.00 33.29           C  
ATOM    498  O   GLY A  68      12.010  21.258  30.226  1.00 35.80           O  
ATOM    499  N   GLU A  69      11.265  19.163  30.570  1.00 33.27           N  
ATOM    500  CA  GLU A  69      11.669  19.147  31.956  1.00 35.35           C  
ATOM    501  C   GLU A  69      13.193  19.192  32.046  1.00 30.25           C  
ATOM    502  O   GLU A  69      13.909  18.691  31.175  1.00 21.28           O  
ATOM    503  CB  GLU A  69      11.083  17.894  32.562  1.00 34.57           C  
ATOM    504  CG  GLU A  69      10.812  18.000  34.037  1.00 46.60           C  
ATOM    505  CD  GLU A  69       9.641  18.867  34.449  1.00 55.16           C  
ATOM    506  OE1 GLU A  69       8.705  19.077  33.669  1.00 54.52           O  
ATOM    507  OE2 GLU A  69       9.678  19.319  35.593  1.00 68.74           O  
ATOM    508  N   LYS A  70      13.671  19.858  33.089  1.00 23.23           N  
ATOM    509  CA  LYS A  70      15.092  20.059  33.309  1.00 24.79           C  
ATOM    510  C   LYS A  70      15.557  19.053  34.352  1.00 28.60           C  
ATOM    511  O   LYS A  70      14.825  18.759  35.312  1.00 31.29           O  
ATOM    512  CB  LYS A  70      15.332  21.469  33.818  1.00 24.89           C  
ATOM    513  CG  LYS A  70      15.190  22.603  32.822  1.00 25.23           C  
ATOM    514  CD  LYS A  70      15.255  23.939  33.570  1.00 27.35           C  
ATOM    515  CE  LYS A  70      15.272  25.133  32.618  1.00 32.66           C  
ATOM    516  NZ  LYS A  70      14.170  25.079  31.666  1.00 23.55           N  
ATOM    517  N   PHE A  71      16.777  18.520  34.204  1.00 33.32           N  
ATOM    518  CA  PHE A  71      17.347  17.505  35.116  1.00 27.36           C  
ATOM    519  C   PHE A  71      18.778  17.840  35.579  1.00 20.66           C  
ATOM    520  O   PHE A  71      19.515  18.535  34.873  1.00 23.08           O  
ATOM    521  CB  PHE A  71      17.356  16.157  34.406  1.00 23.25           C  
ATOM    522  CG  PHE A  71      15.984  15.821  33.844  1.00 24.80           C  
ATOM    523  CD1 PHE A  71      15.031  15.250  34.681  1.00 14.65           C  
ATOM    524  CD2 PHE A  71      15.688  16.100  32.498  1.00 27.07           C  
ATOM    525  CE1 PHE A  71      13.772  14.955  34.175  1.00 21.37           C  
ATOM    526  CE2 PHE A  71      14.423  15.799  31.988  1.00 24.36           C  
ATOM    527  CZ  PHE A  71      13.466  15.226  32.832  1.00 23.13           C  
ATOM    528  N   ALA A  72      19.196  17.499  36.792  1.00 21.08           N  
ATOM    529  CA  ALA A  72      20.574  17.726  37.198  1.00 16.75           C  
ATOM    530  C   ALA A  72      21.529  16.767  36.531  1.00 19.64           C  
ATOM    531  O   ALA A  72      22.665  17.158  36.295  1.00 26.77           O  
ATOM    532  CB  ALA A  72      20.752  17.572  38.698  1.00 19.72           C  
ATOM    533  N   THR A  73      21.092  15.549  36.167  1.00 22.20           N  
ATOM    534  CA  THR A  73      21.955  14.512  35.618  1.00 25.85           C  
ATOM    535  C   THR A  73      21.333  13.814  34.437  1.00 25.01           C  
ATOM    536  O   THR A  73      20.117  13.737  34.263  1.00 31.09           O  
ATOM    537  CB  THR A  73      22.293  13.418  36.666  1.00 28.09           C  
ATOM    538  OG1 THR A  73      21.047  13.035  37.270  1.00 36.15           O  
ATOM    539  CG2 THR A  73      23.299  13.889  37.719  1.00 32.02           C  
ATOM    540  N   LEU A  74      22.208  13.268  33.625  1.00 21.04           N  
ATOM    541  CA  LEU A  74      21.845  12.564  32.442  1.00 19.34           C  
ATOM    542  C   LEU A  74      20.962  11.382  32.829  1.00 26.15           C  
ATOM    543  O   LEU A  74      19.852  11.182  32.320  1.00 25.08           O  
ATOM    544  CB  LEU A  74      23.184  12.189  31.784  1.00 19.93           C  
ATOM    545  CG  LEU A  74      23.271  11.372  30.498  1.00 30.40           C  
ATOM    546  CD1 LEU A  74      22.323  11.935  29.453  1.00 36.91           C  
ATOM    547  CD2 LEU A  74      24.699  11.422  29.970  1.00 30.69           C  
ATOM    548  N   ALA A  75      21.429  10.628  33.818  1.00 26.28           N  
ATOM    549  CA  ALA A  75      20.722   9.445  34.275  1.00 27.12           C  
ATOM    550  C   ALA A  75      19.314   9.733  34.805  1.00 19.27           C  
ATOM    551  O   ALA A  75      18.404   8.890  34.732  1.00 28.62           O  
ATOM    552  CB  ALA A  75      21.597   8.774  35.345  1.00 16.27           C  
ATOM    553  N   GLU A  76      19.113  10.944  35.308  1.00 20.83           N  
ATOM    554  CA  GLU A  76      17.815  11.378  35.777  1.00 14.96           C  
ATOM    555  C   GLU A  76      16.882  11.735  34.626  1.00 18.70           C  
ATOM    556  O   GLU A  76      15.648  11.541  34.682  1.00 21.48           O  
ATOM    557  CB  GLU A  76      18.059  12.546  36.689  1.00 26.90           C  
ATOM    558  CG  GLU A  76      16.881  13.472  36.899  1.00 38.14           C  
ATOM    559  CD  GLU A  76      17.057  14.559  37.933  1.00 40.71           C  
ATOM    560  OE1 GLU A  76      18.018  15.314  37.921  1.00 25.06           O  
ATOM    561  OE2 GLU A  76      16.186  14.630  38.779  1.00 50.53           O  
ATOM    562  N   LEU A  77      17.489  12.287  33.568  1.00 16.34           N  
ATOM    563  CA  LEU A  77      16.769  12.617  32.366  1.00 23.05           C  
ATOM    564  C   LEU A  77      16.242  11.303  31.781  1.00 34.52           C  
ATOM    565  O   LEU A  77      15.019  11.169  31.571  1.00 34.30           O  
ATOM    566  CB  LEU A  77      17.702  13.344  31.341  1.00 19.35           C  
ATOM    567  CG  LEU A  77      17.077  13.710  29.973  1.00 20.94           C  
ATOM    568  CD1 LEU A  77      17.516  15.079  29.554  1.00  9.11           C  
ATOM    569  CD2 LEU A  77      17.478  12.684  28.910  1.00 16.42           C  
ATOM    570  N   VAL A  78      17.152  10.313  31.572  1.00 34.10           N  
ATOM    571  CA  VAL A  78      16.748   9.058  30.964  1.00 28.76           C  
ATOM    572  C   VAL A  78      15.750   8.360  31.844  1.00 28.58           C  
ATOM    573  O   VAL A  78      14.711   7.942  31.322  1.00 32.95           O  
ATOM    574  CB  VAL A  78      17.937   8.141  30.709  1.00 25.91           C  
ATOM    575  CG1 VAL A  78      17.476   6.846  30.033  1.00 28.33           C  
ATOM    576  CG2 VAL A  78      18.843   8.785  29.683  1.00 17.18           C  
ATOM    577  N   GLN A  79      15.935   8.323  33.167  1.00 35.36           N  
ATOM    578  CA  GLN A  79      14.939   7.673  34.011  1.00 30.13           C  
ATOM    579  C   GLN A  79      13.567   8.345  33.901  1.00 31.82           C  
ATOM    580  O   GLN A  79      12.556   7.640  33.824  1.00 31.05           O  
ATOM    581  CB  GLN A  79      15.396   7.693  35.438  1.00 30.82           C  
ATOM    582  CG  GLN A  79      14.577   6.761  36.335  1.00 51.50           C  
ATOM    583  CD  GLN A  79      14.862   6.948  37.824  1.00 65.52           C  
ATOM    584  OE1 GLN A  79      16.014   6.961  38.280  1.00 72.04           O  
ATOM    585  NE2 GLN A  79      13.846   7.106  38.671  1.00 73.32           N  
ATOM    586  N   TYR A  80      13.468   9.670  33.799  1.00 32.02           N  
ATOM    587  CA  TYR A  80      12.167  10.301  33.733  1.00 29.29           C  
ATOM    588  C   TYR A  80      11.437   9.860  32.476  1.00 33.35           C  
ATOM    589  O   TYR A  80      10.259   9.485  32.510  1.00 32.40           O  
ATOM    590  CB  TYR A  80      12.351  11.818  33.762  1.00 27.35           C  
ATOM    591  CG  TYR A  80      11.070  12.640  33.609  1.00 25.66           C  
ATOM    592  CD1 TYR A  80      10.680  12.965  32.313  1.00 25.35           C  
ATOM    593  CD2 TYR A  80      10.282  13.031  34.705  1.00 23.36           C  
ATOM    594  CE1 TYR A  80       9.510  13.659  32.068  1.00 25.65           C  
ATOM    595  CE2 TYR A  80       9.100  13.737  34.468  1.00 28.35           C  
ATOM    596  CZ  TYR A  80       8.723  14.040  33.137  1.00 30.21           C  
ATOM    597  OH  TYR A  80       7.547  14.694  32.799  1.00 34.61           O  
ATOM    598  N   TYR A  81      12.133   9.871  31.346  1.00 30.08           N  
ATOM    599  CA  TYR A  81      11.501   9.489  30.101  1.00 24.44           C  
ATOM    600  C   TYR A  81      11.178   7.998  29.995  1.00 29.75           C  
ATOM    601  O   TYR A  81      10.252   7.630  29.275  1.00 33.37           O  
ATOM    602  CB  TYR A  81      12.411   9.953  28.964  1.00 19.42           C  
ATOM    603  CG  TYR A  81      12.259  11.450  28.825  1.00 27.20           C  
ATOM    604  CD1 TYR A  81      11.004  11.978  28.471  1.00 28.99           C  
ATOM    605  CD2 TYR A  81      13.343  12.295  29.084  1.00 21.02           C  
ATOM    606  CE1 TYR A  81      10.824  13.356  28.367  1.00 33.87           C  
ATOM    607  CE2 TYR A  81      13.157  13.678  28.990  1.00 30.54           C  
ATOM    608  CZ  TYR A  81      11.908  14.200  28.623  1.00 32.74           C  
ATOM    609  OH  TYR A  81      11.727  15.555  28.432  1.00 36.36           O  
ATOM    610  N   MET A  82      11.906   7.112  30.678  1.00 33.85           N  
ATOM    611  CA  MET A  82      11.566   5.696  30.731  1.00 26.07           C  
ATOM    612  C   MET A  82      10.288   5.526  31.528  1.00 30.73           C  
ATOM    613  O   MET A  82       9.365   4.786  31.178  1.00 33.39           O  
ATOM    614  CB  MET A  82      12.674   4.912  31.405  1.00 22.11           C  
ATOM    615  CG  MET A  82      13.709   4.640  30.377  1.00 19.80           C  
ATOM    616  SD  MET A  82      15.067   3.696  31.073  1.00 31.49           S  
ATOM    617  CE  MET A  82      14.343   2.089  30.911  1.00 27.48           C  
ATOM    618  N   GLU A  83      10.230   6.251  32.642  1.00 29.42           N  
ATOM    619  CA  GLU A  83       9.063   6.197  33.484  1.00 28.79           C  
ATOM    620  C   GLU A  83       7.888   6.952  32.940  1.00 29.10           C  
ATOM    621  O   GLU A  83       6.749   6.627  33.260  1.00 38.22           O  
ATOM    622  CB  GLU A  83       9.358   6.756  34.821  1.00 27.32           C  
ATOM    623  CG  GLU A  83      10.354   5.883  35.542  1.00 33.56           C  
ATOM    624  CD  GLU A  83      10.693   6.351  36.948  1.00 43.80           C  
ATOM    625  OE1 GLU A  83      10.095   7.319  37.448  1.00 51.79           O  
ATOM    626  OE2 GLU A  83      11.567   5.714  37.535  1.00 47.15           O  
ATOM    627  N   HIS A  84       8.106   7.961  32.117  1.00 32.64           N  
ATOM    628  CA  HIS A  84       7.012   8.785  31.663  1.00 35.20           C  
ATOM    629  C   HIS A  84       6.901   8.631  30.187  1.00 33.75           C  
ATOM    630  O   HIS A  84       7.380   9.449  29.401  1.00 34.81           O  
ATOM    631  CB  HIS A  84       7.276  10.233  32.020  1.00 37.77           C  
ATOM    632  CG  HIS A  84       7.291  10.462  33.515  1.00 41.84           C  
ATOM    633  ND1 HIS A  84       8.312  10.252  34.355  1.00 37.43           N  
ATOM    634  CD2 HIS A  84       6.213  10.948  34.219  1.00 36.41           C  
ATOM    635  CE1 HIS A  84       7.898  10.603  35.550  1.00 43.69           C  
ATOM    636  NE2 HIS A  84       6.645  11.018  35.456  1.00 48.26           N  
ATOM    637  N   HIS A  85       6.160   7.605  29.814  1.00 49.33           N  
ATOM    638  CA  HIS A  85       6.053   7.237  28.419  1.00 52.87           C  
ATOM    639  C   HIS A  85       5.542   8.211  27.375  1.00 48.23           C  
ATOM    640  O   HIS A  85       6.191   8.297  26.322  1.00 57.52           O  
ATOM    641  CB  HIS A  85       5.261   5.937  28.360  1.00 63.37           C  
ATOM    642  CG  HIS A  85       6.311   4.852  28.552  1.00 70.90           C  
ATOM    643  ND1 HIS A  85       7.339   4.587  27.741  1.00 69.35           N  
ATOM    644  CD2 HIS A  85       6.408   4.034  29.643  1.00 71.20           C  
ATOM    645  CE1 HIS A  85       8.061   3.653  28.292  1.00 69.90           C  
ATOM    646  NE2 HIS A  85       7.490   3.334  29.429  1.00 77.60           N  
ATOM    647  N   GLY A  86       4.510   9.034  27.606  1.00 29.03           N  
ATOM    648  CA  GLY A  86       4.095   9.921  26.523  1.00 36.67           C  
ATOM    649  C   GLY A  86       4.980  11.149  26.275  1.00 41.08           C  
ATOM    650  O   GLY A  86       4.899  11.777  25.215  1.00 46.21           O  
ATOM    651  N   GLN A  87       5.903  11.490  27.178  1.00 39.04           N  
ATOM    652  CA  GLN A  87       6.537  12.799  27.140  1.00 34.28           C  
ATOM    653  C   GLN A  87       7.727  13.057  26.245  1.00 38.82           C  
ATOM    654  O   GLN A  87       8.141  14.225  26.143  1.00 43.37           O  
ATOM    655  CB  GLN A  87       6.930  13.196  28.546  1.00 37.41           C  
ATOM    656  CG  GLN A  87       5.770  13.620  29.424  1.00 52.38           C  
ATOM    657  CD  GLN A  87       4.861  12.483  29.847  1.00 71.48           C  
ATOM    658  OE1 GLN A  87       3.721  12.670  30.251  1.00 82.86           O  
ATOM    659  NE2 GLN A  87       5.281  11.232  29.820  1.00 78.02           N  
ATOM    660  N   LEU A  88       8.333  12.046  25.613  1.00 33.33           N  
ATOM    661  CA  LEU A  88       9.482  12.306  24.777  1.00 27.31           C  
ATOM    662  C   LEU A  88       8.853  12.265  23.423  1.00 33.80           C  
ATOM    663  O   LEU A  88       8.163  11.309  23.092  1.00 34.45           O  
ATOM    664  CB  LEU A  88      10.504  11.224  24.960  1.00 26.34           C  
ATOM    665  CG  LEU A  88      11.695  11.096  24.036  1.00 33.74           C  
ATOM    666  CD1 LEU A  88      12.530  12.328  24.099  1.00 38.74           C  
ATOM    667  CD2 LEU A  88      12.595   9.975  24.499  1.00 31.87           C  
ATOM    668  N   LYS A  89       8.974  13.354  22.677  1.00 46.74           N  
ATOM    669  CA  LYS A  89       8.379  13.443  21.356  1.00 53.33           C  
ATOM    670  C   LYS A  89       9.455  13.995  20.463  1.00 66.58           C  
ATOM    671  O   LYS A  89      10.089  14.965  20.890  1.00 84.13           O  
ATOM    672  CB  LYS A  89       7.205  14.398  21.350  1.00 42.30           C  
ATOM    673  CG  LYS A  89       6.097  13.942  22.252  1.00 41.47           C  
ATOM    674  CD  LYS A  89       5.219  15.113  22.528  1.00 49.41           C  
ATOM    675  CE  LYS A  89       4.035  14.701  23.381  1.00 63.20           C  
ATOM    676  NZ  LYS A  89       3.171  15.854  23.615  1.00 75.55           N  
ATOM    677  N   GLU A  90       9.787  13.441  19.303  1.00 73.15           N  
ATOM    678  CA  GLU A  90      10.771  14.124  18.492  1.00 80.36           C  
ATOM    679  C   GLU A  90      10.025  14.874  17.401  1.00 85.51           C  
ATOM    680  O   GLU A  90       8.973  14.449  16.903  1.00 85.10           O  
ATOM    681  CB  GLU A  90      11.783  13.117  17.909  1.00 78.06           C  
ATOM    682  CG  GLU A  90      11.774  12.730  16.432  1.00 81.81           C  
ATOM    683  CD  GLU A  90      11.008  11.471  16.030  1.00 86.99           C  
ATOM    684  OE1 GLU A  90       9.940  11.189  16.576  1.00 81.60           O  
ATOM    685  OE2 GLU A  90      11.498  10.772  15.141  1.00 89.77           O  
ATOM    686  N   LYS A  91      10.546  16.079  17.168  1.00 96.89           N  
ATOM    687  CA  LYS A  91      10.159  17.010  16.114  1.00102.23           C  
ATOM    688  C   LYS A  91       8.683  17.142  15.767  1.00102.92           C  
ATOM    689  O   LYS A  91       8.002  18.030  16.287  1.00 98.64           O  
ATOM    690  CB  LYS A  91      10.924  16.651  14.833  1.00102.82           C  
ATOM    691  N   ASN A  92       8.131  16.209  14.987  1.00102.99           N  
ATOM    692  CA  ASN A  92       6.756  16.295  14.524  1.00104.31           C  
ATOM    693  C   ASN A  92       5.712  15.802  15.529  1.00104.15           C  
ATOM    694  O   ASN A  92       4.685  15.215  15.171  1.00106.61           O  
ATOM    695  CB  ASN A  92       6.658  15.505  13.235  1.00101.05           C  
ATOM    696  N   GLY A  93       5.965  16.074  16.814  1.00102.04           N  
ATOM    697  CA  GLY A  93       5.121  15.649  17.921  1.00 95.28           C  
ATOM    698  C   GLY A  93       5.050  14.139  18.049  1.00 90.38           C  
ATOM    699  O   GLY A  93       4.199  13.604  18.767  1.00 93.37           O  
ATOM    700  N   ASP A  94       5.978  13.434  17.400  1.00 85.62           N  
ATOM    701  CA  ASP A  94       5.927  11.990  17.353  1.00 80.14           C  
ATOM    702  C   ASP A  94       6.493  11.461  18.651  1.00 70.28           C  
ATOM    703  O   ASP A  94       7.681  11.670  18.937  1.00 72.31           O  
ATOM    704  CB  ASP A  94       6.760  11.450  16.192  1.00 86.91           C  
ATOM    705  CG  ASP A  94       6.475  11.998  14.801  1.00 92.61           C  
ATOM    706  OD1 ASP A  94       5.325  11.960  14.349  1.00 90.69           O  
ATOM    707  OD2 ASP A  94       7.434  12.447  14.171  1.00 94.88           O  
ATOM    708  N   VAL A  95       5.622  10.864  19.461  1.00 50.85           N  
ATOM    709  CA  VAL A  95       6.046  10.252  20.712  1.00 53.65           C  
ATOM    710  C   VAL A  95       6.995   9.105  20.410  1.00 50.48           C  
ATOM    711  O   VAL A  95       6.759   8.317  19.485  1.00 51.74           O  
ATOM    712  CB  VAL A  95       4.824   9.726  21.499  1.00 54.36           C  
ATOM    713  CG1 VAL A  95       5.169   8.866  22.718  1.00 50.59           C  
ATOM    714  CG2 VAL A  95       4.094  10.962  21.989  1.00 61.11           C  
ATOM    715  N   ILE A  96       8.086   9.055  21.171  1.00 46.38           N  
ATOM    716  CA  ILE A  96       9.051   7.982  21.078  1.00 42.87           C  
ATOM    717  C   ILE A  96       9.185   7.434  22.477  1.00 41.69           C  
ATOM    718  O   ILE A  96       9.315   8.142  23.480  1.00 53.15           O  
ATOM    719  CB  ILE A  96      10.443   8.386  20.683  1.00 38.58           C  
ATOM    720  CG1 ILE A  96      10.478   9.464  19.642  1.00 45.46           C  
ATOM    721  CG2 ILE A  96      11.076   7.124  20.127  1.00 50.92           C  
ATOM    722  CD1 ILE A  96      11.879   9.654  19.064  1.00 51.59           C  
ATOM    723  N   GLU A  97       9.090   6.122  22.500  1.00 40.40           N  
ATOM    724  CA  GLU A  97       9.195   5.355  23.706  1.00 36.91           C  
ATOM    725  C   GLU A  97      10.659   4.975  23.931  1.00 35.04           C  
ATOM    726  O   GLU A  97      11.378   4.482  23.042  1.00 29.64           O  
ATOM    727  CB  GLU A  97       8.344   4.137  23.537  1.00 47.92           C  
ATOM    728  CG  GLU A  97       6.852   4.334  23.416  1.00 62.80           C  
ATOM    729  CD  GLU A  97       6.245   4.658  24.764  1.00 73.71           C  
ATOM    730  OE1 GLU A  97       6.359   5.815  25.164  1.00 83.11           O  
ATOM    731  OE2 GLU A  97       5.681   3.765  25.409  1.00 74.07           O  
ATOM    732  N   LEU A  98      11.110   5.254  25.131  1.00 32.02           N  
ATOM    733  CA  LEU A  98      12.432   4.901  25.578  1.00 33.66           C  
ATOM    734  C   LEU A  98      12.175   3.619  26.343  1.00 31.97           C  
ATOM    735  O   LEU A  98      12.019   3.621  27.562  1.00 24.66           O  
ATOM    736  CB  LEU A  98      12.956   6.008  26.484  1.00 31.19           C  
ATOM    737  CG  LEU A  98      14.295   6.605  26.144  1.00 30.45           C  
ATOM    738  CD1 LEU A  98      14.306   6.971  24.700  1.00 15.43           C  
ATOM    739  CD2 LEU A  98      14.566   7.829  26.993  1.00 28.65           C  
ATOM    740  N   LYS A  99      12.091   2.482  25.659  1.00 28.18           N  
ATOM    741  CA  LYS A  99      11.776   1.265  26.379  1.00 25.86           C  
ATOM    742  C   LYS A  99      12.856   0.326  26.930  1.00 17.55           C  
ATOM    743  O   LYS A  99      12.838  -0.018  28.110  1.00 17.41           O  
ATOM    744  CB  LYS A  99      10.802   0.486  25.492  1.00 20.16           C  
ATOM    745  CG  LYS A  99       9.441   1.072  25.735  1.00 23.29           C  
ATOM    746  CD  LYS A  99       8.310   0.166  25.340  1.00 23.03           C  
ATOM    747  CE  LYS A  99       8.073   0.288  23.859  1.00 33.18           C  
ATOM    748  NZ  LYS A  99       6.958  -0.563  23.487  1.00 42.50           N  
ATOM    749  N   TYR A 100      13.863  -0.070  26.166  1.00 22.53           N  
ATOM    750  CA  TYR A 100      14.730  -1.188  26.481  1.00 18.50           C  
ATOM    751  C   TYR A 100      16.152  -0.683  26.366  1.00 23.12           C  
ATOM    752  O   TYR A 100      16.631  -0.444  25.246  1.00 23.93           O  
ATOM    753  CB  TYR A 100      14.434  -2.309  25.433  1.00  7.36           C  
ATOM    754  CG  TYR A 100      12.961  -2.710  25.308  1.00 10.39           C  
ATOM    755  CD1 TYR A 100      12.251  -3.090  26.442  1.00 15.75           C  
ATOM    756  CD2 TYR A 100      12.323  -2.701  24.083  1.00 10.35           C  
ATOM    757  CE1 TYR A 100      10.918  -3.463  26.359  1.00 10.15           C  
ATOM    758  CE2 TYR A 100      10.992  -3.064  23.992  1.00 12.60           C  
ATOM    759  CZ  TYR A 100      10.303  -3.444  25.133  1.00 13.80           C  
ATOM    760  OH  TYR A 100       8.972  -3.837  25.083  1.00 23.70           O  
ATOM    761  N   PRO A 101      16.899  -0.431  27.414  1.00 18.01           N  
ATOM    762  CA  PRO A 101      18.282  -0.015  27.251  1.00 24.19           C  
ATOM    763  C   PRO A 101      19.176  -1.028  26.513  1.00 28.91           C  
ATOM    764  O   PRO A 101      19.062  -2.249  26.663  1.00 26.67           O  
ATOM    765  CB  PRO A 101      18.669   0.310  28.666  1.00 23.12           C  
ATOM    766  CG  PRO A 101      17.660  -0.329  29.581  1.00 26.30           C  
ATOM    767  CD  PRO A 101      16.390  -0.359  28.763  1.00 22.30           C  
ATOM    768  N   LEU A 102      19.986  -0.518  25.599  1.00 31.03           N  
ATOM    769  CA  LEU A 102      20.867  -1.310  24.762  1.00 36.17           C  
ATOM    770  C   LEU A 102      22.166  -1.230  25.557  1.00 34.08           C  
ATOM    771  O   LEU A 102      22.857  -0.226  25.435  1.00 32.91           O  
ATOM    772  CB  LEU A 102      20.958  -0.604  23.384  1.00 39.43           C  
ATOM    773  CG  LEU A 102      21.577  -1.091  22.038  1.00 42.09           C  
ATOM    774  CD1 LEU A 102      22.916  -1.764  22.294  1.00 46.47           C  
ATOM    775  CD2 LEU A 102      20.662  -2.078  21.354  1.00 34.62           C  
ATOM    776  N   ASN A 103      22.467  -2.241  26.364  1.00 36.31           N  
ATOM    777  CA  ASN A 103      23.640  -2.302  27.227  1.00 34.72           C  
ATOM    778  C   ASN A 103      24.830  -2.917  26.478  1.00 29.10           C  
ATOM    779  O   ASN A 103      24.631  -3.961  25.813  1.00 58.40           O  
ATOM    780  CB  ASN A 103      23.327  -3.143  28.437  1.00 32.28           C  
ATOM    781  CG  ASN A 103      22.284  -2.547  29.347  1.00 42.57           C  
ATOM    782  OD1 ASN A 103      22.030  -1.335  29.476  1.00 48.11           O  
ATOM    783  ND2 ASN A 103      21.634  -3.445  30.058  1.00 46.83           N  
ATOM    784  OXT ASN A 103      25.925  -2.327  26.533  1.00 51.76           O  
TER     785      ASN A 103                                                      
HETATM  786  O   HOH A 301      23.864  19.584  35.896  1.00 30.03           O  
HETATM  787  O   HOH A 302      10.839   3.502  20.416  1.00 30.13           O  
HETATM  788  O   HOH A 303      24.898  13.723  34.371  1.00 22.19           O  
HETATM  789  O   HOH A 304      17.773  -3.262  23.775  1.00 33.58           O  
HETATM  790  O   HOH A 305      19.325  -5.602  23.360  1.00 26.25           O  
HETATM  791  O   HOH A 306       9.515  17.031  29.655  1.00 47.75           O  
HETATM  792  O   HOH A 307      13.624  17.769  28.699  1.00 23.13           O  
HETATM  793  O   HOH A 308      13.504  23.358  29.760  1.00 28.78           O  
HETATM  794  O   HOH A 309      11.876  25.301  28.353  1.00 34.91           O  
HETATM  795  O   HOH A 310       3.399   9.918  31.272  1.00 40.38           O  
HETATM  796  O   HOH A 311       7.894  -1.588  20.592  1.00 44.04           O  
HETATM  797  O   HOH A 312       8.124   1.174  17.077  1.00 34.18           O  
HETATM  798  O   HOH A 313      13.767  11.854  38.080  1.00 67.67           O  
HETATM  799  O   HOH A 314      32.317   2.889  16.448  1.00 42.80           O  
HETATM  800  O   HOH A 315      10.247  -6.917  18.913  1.00 25.60           O  
HETATM  801  O   HOH A 316      11.594  23.512  31.741  1.00 29.84           O  
HETATM  802  O   HOH A 317      12.432  16.203  21.850  1.00 42.14           O  
HETATM  803  O   HOH A 318      29.179  -4.439  18.119  1.00 61.54           O  
HETATM  804  O   HOH A 319      17.894   3.567  10.836  1.00 39.00           O  
HETATM  805  O   HOH A 320      11.388   9.863  37.097  1.00 27.34           O  
HETATM  806  O   HOH A 321      18.529   6.045  34.627  1.00 38.51           O  
HETATM  807  O   HOH A 322       9.885  16.236  25.210  1.00 44.66           O  
HETATM  808  O   HOH A 323      23.506  24.501  25.092  1.00 67.73           O  
HETATM  809  O   HOH A 324       9.498   7.117  26.715  1.00 40.05           O  
HETATM  810  O   HOH A 325      27.879  -0.069  27.675  1.00 52.16           O  
HETATM  811  O   HOH A 326      24.611  -5.702  23.558  1.00 39.89           O  
HETATM  812  O   HOH A 327      16.913  24.653  27.624  1.00 45.71           O  
HETATM  813  O   HOH A 328       8.632   1.600  20.365  1.00 36.83           O  
HETATM  814  O   HOH A 329      18.838   3.102  33.992  1.00 45.48           O  
HETATM  815  O   HOH A 330      11.247  17.974  23.467  1.00 44.71           O  
HETATM  816  O   HOH A 331      23.097  11.123  41.781  1.00 47.51           O  
HETATM  817  O   HOH A 332      17.495   2.717  37.690  1.00 75.89           O  
HETATM  818  O   HOH A 333      16.760  27.385  26.205  1.00 55.64           O  
HETATM  819  O   HOH A 334      16.769   3.997  35.375  1.00 59.08           O  
HETATM  820  O   HOH A 335      28.228  -9.834  22.394  1.00 48.08           O  
HETATM  821  O   HOH A 336      32.411   5.938  30.345  1.00 41.56           O  
HETATM  822  O   HOH A 337      15.304   6.239  40.948  1.00 53.03           O  
HETATM  823  O   HOH A 338      29.013   8.571  13.096  1.00 62.02           O  
HETATM  824  O   HOH A 339      16.191  25.528  24.224  1.00 42.30           O  
HETATM  825  O   HOH A 340      14.570  17.411  20.799  1.00 51.99           O  
HETATM  826  O   HOH A 341      23.945  14.247  17.010  1.00 60.07           O  
HETATM  827  O   HOH A 342      28.753  16.026  30.483  1.00 40.17           O  
HETATM  828  O   HOH A 343      19.351   6.974  11.433  1.00 64.90           O  
HETATM  829  O   HOH A 344      13.047   5.624  14.339  1.00 48.15           O  
HETATM  830  O   HOH A 345      13.637  -1.443  31.713  1.00 55.47           O  
HETATM  831  O   HOH A 346      26.302  13.177  16.663  1.00 31.43           O  
HETATM  832  O   HOH A 347      29.212  25.810  32.769  1.00 58.98           O  
HETATM  833  O   HOH A 348       8.494   5.688  12.736  1.00 60.27           O  
HETATM  834  O   HOH A 349      19.813  14.682  16.039  1.00 43.61           O  
HETATM  835  O   HOH A 350      10.825   1.844  34.237  1.00 48.01           O  
HETATM  836  O   HOH A 351      27.531  -5.248  23.319  1.00 61.54           O  
HETATM  837  O   HOH A 352      28.247  -2.515  23.319  1.00 55.36           O  
HETATM  838  O   HOH A 353      26.857  27.991  34.144  1.00 59.79           O  
HETATM  839  O   HOH A 354      15.556   9.940  38.613  1.00 32.47           O  
HETATM  840  O   HOH A 355      11.415   6.405  12.366  1.00 67.99           O  
HETATM  841  O   HOH A 356      24.099  28.787  29.870  1.00 55.88           O  
HETATM  842  O   HOH A 357      10.656  26.975  30.955  1.00 45.53           O  
HETATM  843  O   HOH A 358      16.207  -0.831  32.618  1.00 46.79           O  
HETATM  844  O   HOH A 359      14.227  27.478  29.431  1.00 37.50           O  
HETATM  845  O   HOH A 360      31.567  14.899  22.701  1.00 45.98           O  
HETATM  846  O   HOH A 361      26.664  20.490  36.043  1.00 43.75           O  
HETATM  847  O   HOH A 362      22.263   0.691  34.376  1.00 62.76           O  
HETATM  848  O   HOH A 363      23.222  -7.429  29.429  1.00 36.08           O  
HETATM  849  O   HOH A 364      21.828  -8.406  31.420  1.00 62.16           O  
HETATM  850  O   HOH A 365       2.743   5.629  25.472  1.00 51.75           O  
HETATM  851  O   HOH A 366      10.538  -0.397  29.758  1.00 45.06           O  
HETATM  852  O   HOH A 367       3.713  14.581  34.681  1.00 87.34           O  
HETATM  853  O   HOH A 368       8.742  22.311  32.289  1.00 67.93           O  
HETATM  854  O   HOH A 369      23.249  16.396  20.777  1.00 42.52           O  
HETATM  855  O   HOH A 370      16.424  25.414  21.498  1.00 66.68           O  
HETATM  856  O   HOH A 371      24.875  26.281  27.050  1.00 79.12           O  
HETATM  857  O   HOH A 372       4.535  17.938  25.500  1.00 49.73           O  
HETATM  858  O   HOH A 373       7.301  17.934  27.180  1.00 70.91           O  
HETATM  859  O   HOH A 374      29.113  21.967  29.947  1.00 54.33           O  
HETATM  860  O   HOH A 375       6.946  18.792  38.695  1.00 51.40           O  
HETATM  861  O   HOH A 376      11.842  17.613  19.194  1.00 44.63           O  
HETATM  862  O   HOH A 377      21.734  11.779  12.701  1.00 63.86           O  
HETATM  863  O   HOH A 378      28.203  23.609  27.874  1.00 43.98           O  
HETATM  864  O   HOH A 379      29.918  15.423  24.768  1.00 52.80           O  
HETATM  865  O   HOH A 380      24.187  10.914  13.448  1.00 50.81           O  
HETATM  866  O   HOH A 381      24.759   8.644  12.163  1.00 52.52           O  
HETATM  867  O   HOH A 382       5.771   3.624  18.444  1.00 68.44           O  
HETATM  868  O   HOH A 383       2.928  11.768  15.975  1.00 59.62           O  
HETATM  869  O   HOH A 384      20.288  22.237  38.188  1.00 73.83           O  
HETATM  870  O   HOH A 385      29.818   9.820  15.408  1.00 73.91           O  
HETATM  871  O   HOH A 386      12.115  -3.702  30.769  1.00 52.71           O  
HETATM  872  O   HOH A 387      27.101  25.978  36.081  1.00125.76           O  
MASTER      333    0    0    3    7    0    0    6  871    1    0    8          
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.