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Database: PDB
Entry: 1IRK
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Original site: 1IRK 
HEADER    TRANSFERASE (PHOSPHOTRANSFERASE)        02-JAN-95   1IRK              
TITLE     CRYSTAL STRUCTURE OF THE TYROSINE KINASE DOMAIN OF THE                
TITLE    2 HUMAN INSULIN RECEPTOR                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INSULIN RECEPTOR TYROSINE KINASE DOMAIN;                   
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606                                                 
KEYWDS    TRANSFERASE (PHOSPHOTRANSFERASE)                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.R.HUBBARD,L.WEI,L.ELLIS,W.A.HENDRICKSON                             
REVDAT   2   24-FEB-09 1IRK    1       VERSN                                    
REVDAT   1   27-FEB-95 1IRK    0                                                
JRNL        AUTH   S.R.HUBBARD,L.WEI,L.ELLIS,W.A.HENDRICKSON                    
JRNL        TITL   CRYSTAL STRUCTURE OF THE TYROSINE KINASE DOMAIN OF           
JRNL        TITL 2 THE HUMAN INSULIN RECEPTOR.                                  
JRNL        REF    NATURE                        V. 372   746 1994              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   7997262                                                      
JRNL        DOI    10.1038/372746A0                                             
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   L.WEI,S.R.HUBBARD,W.A.HENDRICKSON,L.ELLIS                    
REMARK   1  TITL   EXPRESSION, CHARACTERIZATION AND CRYSTALLIZATION             
REMARK   1  TITL 2 OF THE CATALYTIC CORE OF THE HUMAN INSULIN                   
REMARK   1  TITL 3 RECEPTOR PROTEIN TYROSINE KINASE DOMAIN                      
REMARK   1  REF    TO BE PUBLISHED                                              
REMARK   1  REFN                                                                
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   Y.EBINA,L.ELLIS,K.JARNAGIN,M.EDERY,L.GRAF,                   
REMARK   1  AUTH 2 E.CLAUSER,J.-H.OU,F.MASIARZ,Y.W.KAN,I.D.GOLDFINE,            
REMARK   1  AUTH 3 R.A.ROTH,W.J.RUTTER                                          
REMARK   1  TITL   THE HUMAN INSULIN RECEPTOR CDNA: THE STRUCTURAL              
REMARK   1  TITL 2 BASIS FOR HORMONE-ACTIVATED TRANSMEMBRANE                    
REMARK   1  TITL 3 SIGNALLING                                                   
REMARK   1  REF    CELL(CAMBRIDGE,MASS.)         V.  40   747 1985              
REMARK   1  REFN                   ISSN 0092-8674                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 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) : 2.10                           
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)   (%) : 91.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 34747                          
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) : 0.196                           
REMARK   3   FREE R VALUE                     : 0.232                           
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            : 2380                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 6                                       
REMARK   3   SOLVENT ATOMS            : 199                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.60                          
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) : 0.011                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.58                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.46                            
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) : 1.660 ; 1.000                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.720 ; 1.500                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.930 ; 1.500                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.130 ; 2.000                
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 1IRK 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   : 37359                              
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     (%) : 93.9                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> 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  <I/SIGMA(I)> 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   (%): 51.30                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.53                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       27.01500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       44.59000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       36.49500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       44.59000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       27.01500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       36.49500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 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     VAL A   978                                                      
REMARK 465     PHE A   979                                                      
REMARK 465     PRO A   980                                                      
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     PHE A 984    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU A 988    CG   CD   OE1  OE2                                  
REMARK 470     GLU A1094    CG   CD   OE1  OE2                                  
REMARK 470     GLU A1096    CG   CD   OE1  OE2                                  
REMARK 470     MET A1153    CG   SD   CE                                        
REMARK 470     THR A1154    OG1  CG2                                            
REMARK 470     ARG A1155    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP A1156    CG   OD1  OD2                                       
REMARK 470     ILE A1157    CG1  CG2  CD1                                       
REMARK 470     GLU A1159    CG   CD   OE1  OE2                                  
REMARK 470     ARG A1237    CG   CD   NE   CZ   NH1  NH2                        
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 A1131      -13.51     77.45                                   
REMARK 500    ASP A1132       41.00   -145.75                                   
REMARK 500    MET A1153       70.88   -113.07                                   
REMARK 500    ASP A1156     -148.23   -173.00                                   
REMARK 500    LYS A1168     -129.09    -93.35                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600                                                                      
REMARK 600 THE MODEL INCLUDES TWO ETHYL MERCURY GROUPS (EMC)                    
REMARK 600 WHICH ARE COVALENTLY BOUND TO CYS 1056 AND CYS 1234.                 
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EMC A 500                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EMC A 501                 
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999                                                                      
REMARK 999 RESIDUE NUMBERING IS ACCORDING TO EBINA ET AL.                       
REMARK 999 (REFERENCE 2).                                                       
DBREF  1IRK A  978  1283  UNP    P06213   INSR_HUMAN    1005   1310             
SEQADV 1IRK SER A  981  UNP  P06213    CYS  1008 CONFLICT                       
SEQADV 1IRK PHE A  984  UNP  P06213    TYR  1011 CONFLICT                       
SEQRES   1 A  306  VAL PHE PRO SER SER VAL PHE VAL PRO ASP GLU TRP GLU          
SEQRES   2 A  306  VAL SER ARG GLU LYS ILE THR LEU LEU ARG GLU LEU GLY          
SEQRES   3 A  306  GLN GLY SER PHE GLY MET VAL TYR GLU GLY ASN ALA ARG          
SEQRES   4 A  306  ASP ILE ILE LYS GLY GLU ALA GLU THR ARG VAL ALA VAL          
SEQRES   5 A  306  LYS THR VAL ASN GLU SER ALA SER LEU ARG GLU ARG ILE          
SEQRES   6 A  306  GLU PHE LEU ASN GLU ALA SER VAL MET LYS GLY PHE THR          
SEQRES   7 A  306  CYS HIS HIS VAL VAL ARG LEU LEU GLY VAL VAL SER LYS          
SEQRES   8 A  306  GLY GLN PRO THR LEU VAL VAL MET GLU LEU MET ALA HIS          
SEQRES   9 A  306  GLY ASP LEU LYS SER TYR LEU ARG SER LEU ARG PRO GLU          
SEQRES  10 A  306  ALA GLU ASN ASN PRO GLY ARG PRO PRO PRO THR LEU GLN          
SEQRES  11 A  306  GLU MET ILE GLN MET ALA ALA GLU ILE ALA ASP GLY MET          
SEQRES  12 A  306  ALA TYR LEU ASN ALA LYS LYS PHE VAL HIS ARG ASP LEU          
SEQRES  13 A  306  ALA ALA ARG ASN CYS MET VAL ALA HIS ASP PHE THR VAL          
SEQRES  14 A  306  LYS ILE GLY ASP PHE GLY MET THR ARG ASP ILE TYR GLU          
SEQRES  15 A  306  THR ASP TYR TYR ARG LYS GLY GLY LYS GLY LEU LEU PRO          
SEQRES  16 A  306  VAL ARG TRP MET ALA PRO GLU SER LEU LYS ASP GLY VAL          
SEQRES  17 A  306  PHE THR THR SER SER ASP MET TRP SER PHE GLY VAL VAL          
SEQRES  18 A  306  LEU TRP GLU ILE THR SER LEU ALA GLU GLN PRO TYR GLN          
SEQRES  19 A  306  GLY LEU SER ASN GLU GLN VAL LEU LYS PHE VAL MET ASP          
SEQRES  20 A  306  GLY GLY TYR LEU ASP GLN PRO ASP ASN CYS PRO GLU ARG          
SEQRES  21 A  306  VAL THR ASP LEU MET ARG MET CYS TRP GLN PHE ASN PRO          
SEQRES  22 A  306  LYS MET ARG PRO THR PHE LEU GLU ILE VAL ASN LEU LEU          
SEQRES  23 A  306  LYS ASP ASP LEU HIS PRO SER PHE PRO GLU VAL SER PHE          
SEQRES  24 A  306  PHE HIS SER GLU GLU ASN LYS                                  
HET    EMC  A 500       3                                                       
HET    EMC  A 501       3                                                       
HETNAM     EMC ETHYL MERCURY ION                                                
FORMUL   2  EMC    2(C2 H5 HG 1+)                                               
FORMUL   4  HOH   *199(H2 O)                                                    
HELIX    1   C LEU A 1038  MET A 1051  1                                  14    
HELIX    2   D LEU A 1084  SER A 1090  1                                   7    
HELIX    3   E LEU A 1106  ALA A 1125  1                                  20    
HELIX    4  EF PRO A 1178  ASP A 1183  1                                   6    
HELIX    5   F THR A 1188  SER A 1204  1                                  17    
HELIX    6   G ASN A 1215  MET A 1223  1                                   9    
HELIX    7   H GLU A 1236  CYS A 1245  1                                  10    
HELIX    8   I PHE A 1256  LEU A 1263  1                                   8    
HELIX    9   J PHE A 1271  VAL A 1274  1                                   4    
SHEET    1   A 5 LEU A1062  VAL A1066  0                                        
SHEET    2   A 5 LEU A1073  GLU A1077 -1  N  VAL A1075   O  LEU A1063           
SHEET    3   A 5 GLU A1022  LYS A1030 -1  N  LYS A1030   O  VAL A1074           
SHEET    4   A 5 MET A1009  ILE A1019 -1  N  ALA A1015   O  THR A1025           
SHEET    5   A 5 ILE A 996  GLN A1004 -1  N  ARG A1000   O  GLU A1012           
SHEET    1   B 2 CYS A1138  VAL A1140  0                                        
SHEET    2   B 2 VAL A1146  ILE A1148 -1  N  LYS A1147   O  MET A1139           
SHEET    1   C 2 TYR A1163  ARG A1164  0                                        
SHEET    2   C 2 LEU A1170  LEU A1171 -1  N  LEU A1171   O  TYR A1163           
LINK        HG   EMC A 500                 SG  CYS A1056     1555   1555  2.38  
LINK        HG   EMC A 501                 SG  CYS A1234     1555   1555  2.37  
CISPEP   1 GLN A 1070    PRO A 1071          0        -0.47                     
SITE     1 AC1  3 CYS A1056  PHE A1276  SER A1279                               
SITE     1 AC2  2 MET A1109  CYS A1234                                          
CRYST1   54.030   72.990   89.180  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.018508  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013701  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011213        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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