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Database: PDB
Entry: 1NKR
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Original site: 1NKR 
HEADER    INHIBITORY RECEPTOR                     24-JUN-98   1NKR              
TITLE     INHIBITORY RECEPTOR (P58-CL42) FOR HUMAN NATURAL KILLER               
TITLE    2 CELLS                                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: P58-CL42 KIR;                                              
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: EXTRACELLULAR DOMAIN;                                      
COMPND   5 SYNONYM: KILLER CELL INHIBITORY RECEPTOR;                            
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 CELL_LINE: BL21;                                                     
SOURCE   6 CELL: NATURAL KILLER CELLS;                                          
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3) PLYSS;                          
SOURCE  10 EXPRESSION_SYSTEM_CELLULAR_LOCATION: INCLUSION BODY;                 
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PLM1                                      
KEYWDS    INHIBITORY RECEPTOR, NATURAL KILLER CELLS, IMMUNOLOGICAL              
KEYWDS   2 RECEPTORS, IMMUNOGLOBULIN FOLD                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Q.R.FAN,L.MOSYAK,C.C.WINTER,N.WAGTMANN,E.O.LONG,D.C.WILEY             
REVDAT   2   24-FEB-09 1NKR    1       VERSN                                    
REVDAT   1   11-NOV-98 1NKR    0                                                
JRNL        AUTH   Q.R.FAN,L.MOSYAK,C.C.WINTER,N.WAGTMANN,E.O.LONG,             
JRNL        AUTH 2 D.C.WILEY                                                    
JRNL        TITL   STRUCTURE OF THE INHIBITORY RECEPTOR FOR HUMAN               
JRNL        TITL 2 NATURAL KILLER CELLS RESEMBLES HAEMATOPOIETIC                
JRNL        TITL 3 RECEPTORS.                                                   
JRNL        REF    NATURE                        V. 389    96 1997              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   9288975                                                      
JRNL        DOI    10.1038/38028                                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 6.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 24473                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.205                           
REMARK   3   R VALUE            (WORKING SET) : 0.227                           
REMARK   3   FREE R VALUE                     : 0.255                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 2427                            
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1513                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 211                                     
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 OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): NULL          
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : NULL  ; NULL                
REMARK   3    ANGLE DISTANCE                  (A) : NULL  ; NULL                
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL                
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL                
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL                
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL                
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL                
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL                
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; 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  OTHER REFINEMENT REMARKS: THE STRUCTURE WAS INITIALLY REFINED       
REMARK   3  AT 10-2.2 ANGSTROMS USING POSITIONAL REFINEMENT AND SIMULATED       
REMARK   3  ANNEALING PROTOCOLS IN X-PLOR. THE RESOLUTION WAS THEN              
REMARK   3  EXTENDED TO 1.7 ANGSTROMS. REFINEMENT AT THIS STAGE INVOLVED        
REMARK   3  SIMULATED ANNEALING FOLLOWED BY B-FACTOR REFINEMENT, WITH THE       
REMARK   3  EXTENSIVE USE OF SIMULATED ANNEALING OMIT MAPS. THE FINAL           
REMARK   3  MODEL OBTAINED FROM X-PLOR WAS AGAIN REFINED WITH REFMAC. THE       
REMARK   3  FINAL REFINEMENT STATISTICS FROM REFMAC ARE SHOWN HERE.             
REMARK   4                                                                      
REMARK   4 1NKR 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        : OCT-96                             
REMARK 200  TEMPERATURE           (KELVIN) : 90                                 
REMARK 200  PH                             : 5.4-7.7                            
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CHESS                              
REMARK 200  BEAMLINE                       : F1                                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.918                              
REMARK 200  MONOCHROMATOR                  : HORIZONTALLY BENT SI (111),        
REMARK 200                                   ASYMMETRICALLY CUT CRYSTALS        
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : PRINCETON 2K                       
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 25065                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 16.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 7.000                              
REMARK 200  R MERGE                    (I) : 0.07300                            
REMARK 200  R SYM                      (I) : 0.07300                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.76                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.23400                            
REMARK 200  R SYM FOR SHELL            (I) : 0.23400                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: MLPHARE                                               
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 40.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.80                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLIZED FROM 0.55       
REMARK 280  M (NH4)2HPO4, 50 MM SODIUM CITRATE, PH 5.4, FINAL PH 7.7.           
REMARK 280  CRYSTALS WERE HARVESTED IN 1.5 M (NH4)2HPO4, 50 MM SODIUM           
REMARK 280  CITRATE, PH 5.4, FINAL PH 7.7; THEN SOAKED IN 1.5 M (NH4)           
REMARK 280  2HPO4, 50 MM SODIUM CITRATE, PH 5.4, 25% GLYCEROL, FINAL PH         
REMARK 280  7.7, AND FLASH-COOLED WITH LIQUID NITROGEN.                         
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       15.59000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       31.18000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       23.38500            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       38.97500            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000        7.79500            
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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     0                                                      
REMARK 465     HIS A     1                                                      
REMARK 465     GLU A     2                                                      
REMARK 465     GLY A     3                                                      
REMARK 465     VAL A     4                                                      
REMARK 465     HIS A     5                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    ALA A   145     O    HOH A   292              2.01            
REMARK 500   CE   LYS A     7     O    HOH A   364              2.11            
REMARK 500   O    HOH A   275     O    HOH A   387              2.14            
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    CYS A 177   CA  -  CB  -  SG  ANGL. DEV. =  10.1 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    ASP A  57       73.78     42.24                                   
REMARK 500    VAL A 156       62.93   -100.02                                   
REMARK 500    ASN A 157       84.12     50.14                                   
REMARK 500    THR A 170      -56.87   -127.55                                   
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 399        DISTANCE =  5.07 ANGSTROMS                       
DBREF  1NKR A    1   200  UNP    P43626   KI2L1_HUMAN     22    221             
SEQRES   1 A  201  MET HIS GLU GLY VAL HIS ARG LYS PRO SER LEU LEU ALA          
SEQRES   2 A  201  HIS PRO GLY PRO LEU VAL LYS SER GLU GLU THR VAL ILE          
SEQRES   3 A  201  LEU GLN CYS TRP SER ASP VAL MET PHE GLU HIS PHE LEU          
SEQRES   4 A  201  LEU HIS ARG GLU GLY MET PHE ASN ASP THR LEU ARG LEU          
SEQRES   5 A  201  ILE GLY GLU HIS HIS ASP GLY VAL SER LYS ALA ASN PHE          
SEQRES   6 A  201  SER ILE SER ARG MET THR GLN ASP LEU ALA GLY THR TYR          
SEQRES   7 A  201  ARG CYS TYR GLY SER VAL THR HIS SER PRO TYR GLN VAL          
SEQRES   8 A  201  SER ALA PRO SER ASP PRO LEU ASP ILE VAL ILE ILE GLY          
SEQRES   9 A  201  LEU TYR GLU LYS PRO SER LEU SER ALA GLN PRO GLY PRO          
SEQRES  10 A  201  THR VAL LEU ALA GLY GLU ASN VAL THR LEU SER CYS SER          
SEQRES  11 A  201  SER ARG SER SER TYR ASP MET TYR HIS LEU SER ARG GLU          
SEQRES  12 A  201  GLY GLU ALA HIS GLU ARG ARG LEU PRO ALA GLY PRO LYS          
SEQRES  13 A  201  VAL ASN GLY THR PHE GLN ALA ASP PHE PRO LEU GLY PRO          
SEQRES  14 A  201  ALA THR HIS GLY GLY THR TYR ARG CYS PHE GLY SER PHE          
SEQRES  15 A  201  HIS ASP SER PRO TYR GLU TRP SER LYS SER SER ASP PRO          
SEQRES  16 A  201  LEU LEU VAL SER VAL THR                                      
FORMUL   2  HOH   *211(H2 O)                                                    
HELIX    1   1 GLN A   71  LEU A   73  5                                   3    
HELIX    2   2 THR A   84  SER A   86  5                                   3    
SHEET    1   A 4 SER A   9  HIS A  13  0                                        
SHEET    2   A 4 VAL A  24  SER A  30 -1  N  TRP A  29   O  SER A   9           
SHEET    3   A 4 VAL A  59  ILE A  66 -1  N  ILE A  66   O  VAL A  24           
SHEET    4   A 4 GLU A  54  HIS A  56 -1  N  HIS A  56   O  VAL A  59           
SHEET    1   B 2 LEU A  17  LYS A  19  0                                        
SHEET    2   B 2 VAL A 100  ILE A 102  1  N  VAL A 100   O  VAL A  18           
SHEET    1   C 4 ASP A  47  ILE A  52  0                                        
SHEET    2   C 4 HIS A  36  GLY A  43 -1  N  ARG A  41   O  ASP A  47           
SHEET    3   C 4 GLY A  75  SER A  82 -1  N  SER A  82   O  HIS A  36           
SHEET    4   C 4 LEU A  97  ILE A  99 -1  N  ILE A  99   O  GLY A  75           
SHEET    1   D 3 SER A 109  GLN A 113  0                                        
SHEET    2   D 3 ASN A 123  SER A 130 -1  N  SER A 129   O  SER A 109           
SHEET    3   D 3 PHE A 160  PRO A 168 -1  N  GLY A 167   O  VAL A 124           
SHEET    1   E 2 THR A 117  LEU A 119  0                                        
SHEET    2   E 2 SER A 198  THR A 200  1  N  SER A 198   O  VAL A 118           
SHEET    1   F 4 ARG A 148  PRO A 151  0                                        
SHEET    2   F 4 MET A 136  ARG A 141 -1  N  LEU A 139   O  ARG A 148           
SHEET    3   F 4 GLY A 173  SER A 180 -1  N  SER A 180   O  MET A 136           
SHEET    4   F 4 LEU A 195  VAL A 197 -1  N  VAL A 197   O  GLY A 173           
SSBOND   1 CYS A   28    CYS A   79                          1555   1555  2.04  
SSBOND   2 CYS A  128    CYS A  177                          1555   1555  2.06  
CISPEP   1 HIS A   13    PRO A   14          0         0.02                     
CISPEP   2 GLN A  113    PRO A  114          0        -0.32                     
CRYST1   92.360   92.360   46.770  90.00  90.00 120.00 P 61          6          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.010827  0.006251  0.000000        0.00000                         
SCALE2      0.000000  0.012502  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.021381        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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