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Database: PDB
Entry: 3GKY
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Original site: 3GKY 
HEADER    HORMONE                                 11-MAR-09   3GKY              
TITLE     THE STRUCTURAL BASIS OF AN ER STRESS-ASSOCIATED BOTTLENECK IN A       
TITLE    2 PROTEIN FOLDING LANDSCAPE                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INSULIN A CHAIN;                                           
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: INSULIN B CHAIN;                                           
COMPND   7 CHAIN: B, D;                                                         
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 SYNTHETIC: YES;                                                      
SOURCE   3 ORGANISM_SCIENTIFIC: SUS SCROFA;                                     
SOURCE   4 ORGANISM_COMMON: PIG;                                                
SOURCE   5 ORGANISM_TAXID: 9823;                                                
SOURCE   6 OTHER_DETAILS: BIOSYNTHETIC SEQUENCE;                                
SOURCE   7 MOL_ID: 2;                                                           
SOURCE   8 SYNTHETIC: YES;                                                      
SOURCE   9 ORGANISM_SCIENTIFIC: SUS SCROFA;                                     
SOURCE  10 ORGANISM_COMMON: PIG;                                                
SOURCE  11 ORGANISM_TAXID: 9823;                                                
SOURCE  12 OTHER_DETAILS: BIOSYNTHETIC SEQUENCE                                 
KEYWDS    PROTEIN FOLDING, ER STRESS-ASSOCIATED, TR TRANSITION RECEPTOR         
KEYWDS   2 BINDING, CARBOHYDRATE METABOLISM, CLEAVAGE ON PAIR OF BASIC          
KEYWDS   3 RESIDUES, DIABETES MELLITUS, DISEASE MUTATION, DISULFIDE BOND,       
KEYWDS   4 GLUCOSE METABOLISM, HORMONE, PHARMACEUTICAL, SECRETED                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.LIU,Z.L.WAN,Y.C.CHU,H.ALDDIN,B.KLAPROTH,M.A.WEISS                   
REVDAT   4   06-SEP-23 3GKY    1       REMARK SEQADV                            
REVDAT   3   24-JAN-18 3GKY    1       AUTHOR                                   
REVDAT   2   22-DEC-09 3GKY    1       JRNL                                     
REVDAT   1   24-MAR-09 3GKY    0                                                
JRNL        AUTH   M.LIU,Z.L.WAN,Y.C.CHU,H.ALADDIN,B.KLAPROTH,M.CHOQUETTE,      
JRNL        AUTH 2 Q.X.HUA,R.B.MACKIN,J.S.RAO,P.DE MEYTS,P.G.KATSOYANNIS,       
JRNL        AUTH 3 P.ARVAN,M.A.WEISS                                            
JRNL        TITL   CRYSTAL STRUCTURE OF A "NONFOLDABLE" INSULIN: IMPAIRED       
JRNL        TITL 2 FOLDING EFFICIENCY DESPITE NATIVE ACTIVITY.                  
JRNL        REF    J.BIOL.CHEM.                  V. 284 35259 2009              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   19850922                                                     
JRNL        DOI    10.1074/JBC.M109.046888                                      
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   E.N.BAKER,T.L.BLUJDELL,J.F.CUTFIELD,S.M.CUTFIELD,E.J.DODSON, 
REMARK   1  AUTH 2 G.G.DODSON,D.HODGKIN,N.W.ISAACS,C.D.REYNOLDS                 
REMARK   1  TITL   THE STRUCTURE OF 2ZN PIG INSULIN CRYSTAL AT 1.5 A RESOLUTION 
REMARK   1  REF    PHILOS.TRANS.R.SOC.LONDON,    V. 319   369 1988              
REMARK   1  REF  2 SER.B                                                        
REMARK   1  REFN                   ISSN 0080-4622                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   G.BENTLEY,E.DODSON,G.DODSON,D.HODGKIN,D.MERCOLA              
REMARK   1  TITL   STRUCTURE OF INSULIN IN 4-ZINC INSULIN                       
REMARK   1  REF    NATURE                        V. 261   166 1976              
REMARK   1  REFN                   ISSN 0028-0836                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   U.DEREWENDA,Z.DEREWENDA,E.DODSON,G.DODSON,C.REYNOLD,G.SMITH, 
REMARK   1  AUTH 2 C.SPARKS,D.SWENSON                                           
REMARK   1  TITL   PHENOL STABILIZES MORE HELIX IN A NEW SYMMETRICAL ZINC       
REMARK   1  TITL 2 INSULIN HEXAMER                                              
REMARK   1  REF    NATURE                        V. 338   594 1989              
REMARK   1  REFN                   ISSN 0028-0836                               
REMARK   1 REFERENCE 4                                                          
REMARK   1  AUTH   Q.X.HUA,S.NAKAGAWA,S.Q.HU,W.JIA,S.WANG,M.A.WEISS             
REMARK   1  TITL   TOWARD THE ACTIVE CONFORMATION OF INSULIN: STEREOSPECIFIC    
REMARK   1  TITL 2 MODULATION OF A STRUCTURAL SWITH IN THE B CHAIN              
REMARK   1  REF    J.BIOL.CHEM.                  V. 281 24900 2006              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 22.58                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 94.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 7299                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.209                           
REMARK   3   FREE R VALUE                     : 0.253                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 789                             
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) : 1.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.91                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 90.10                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2970                       
REMARK   3   BIN FREE R VALUE                    : 0.3110                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 133                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.022                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 810                                     
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 11                                      
REMARK   3   SOLVENT ATOMS            : 125                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 27.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 39.20                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.62000                                             
REMARK   3    B22 (A**2) : -1.62000                                             
REMARK   3    B33 (A**2) : 3.24000                                              
REMARK   3    B12 (A**2) : 1.10000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.21                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.12                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.200                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 20.80                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.600                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
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  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : 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 3GKY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-MAR-09.                  
REMARK 100 THE DEPOSITION ID IS D_1000051990.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-FEB-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.1                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CHESS                              
REMARK 200  BEAMLINE                       : F2                                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.948                              
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 7299                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 22.580                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 390252.                            
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.3                               
REMARK 200  DATA REDUNDANCY                : 6.400                              
REMARK 200  R MERGE                    (I) : 0.04800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.91                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.18200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 7.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: 1TRZ                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 33.53                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.85                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.02 M TRIS, 0.05 M SODIUM CITRATE, 5%   
REMARK 280  ACETONE, 0.03% PHENOL, 0.01% ZINC ACETATE, PH 8.1, VAPOR            
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 298K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   X+2/3,Y+1/3,Z+1/3                                       
REMARK 290       5555   -Y+2/3,X-Y+1/3,Z+1/3                                    
REMARK 290       6555   -X+Y+2/3,-X+1/3,Z+1/3                                   
REMARK 290       7555   X+1/3,Y+2/3,Z+2/3                                       
REMARK 290       8555   -Y+1/3,X-Y+2/3,Z+2/3                                    
REMARK 290       9555   -X+Y+1/3,-X+2/3,Z+2/3                                   
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       39.11250            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       22.58161            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       12.23733            
REMARK 290   SMTRY1   5 -0.500000 -0.866025  0.000000       39.11250            
REMARK 290   SMTRY2   5  0.866025 -0.500000  0.000000       22.58161            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       12.23733            
REMARK 290   SMTRY1   6 -0.500000  0.866025  0.000000       39.11250            
REMARK 290   SMTRY2   6 -0.866025 -0.500000  0.000000       22.58161            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       12.23733            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       45.16322            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       24.47467            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       45.16322            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       24.47467            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       45.16322            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       24.47467            
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: DODECAMERIC                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DODECAMERIC                
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 19390 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 13360 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -314.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -0.500000 -0.866025  0.000000       39.11250            
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000       67.74484            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3 -0.500000  0.866025  0.000000      -39.11250            
REMARK 350   BIOMT2   3 -0.866025 -0.500000  0.000000       67.74484            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375 ZN    ZN B  31  LIES ON A SPECIAL POSITION.                          
REMARK 375 CL    CL B  32  LIES ON A SPECIAL POSITION.                          
REMARK 375 ZN    ZN D  31  LIES ON A SPECIAL POSITION.                          
REMARK 375 CL    CL D  32  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH D  36  LIES ON A SPECIAL POSITION.                          
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    ASN B   3       56.77   -117.28                                   
REMARK 500    LYS B  29       35.26    -78.70                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 31                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 32                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPH C 100                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 31                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 32                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1TRZ   RELATED DB: PDB                                   
REMARK 900 TR STATE INSULIN CRYSTAL STRUCTURE                                   
DBREF  3GKY A    1    21  UNP    P01315   INS_PIG         88    108             
DBREF  3GKY B    1    30  UNP    P01315   INS_PIG         25     54             
DBREF  3GKY C    1    21  UNP    P01315   INS_PIG         88    108             
DBREF  3GKY D    1    30  UNP    P01315   INS_PIG         25     54             
SEQADV 3GKY HIS A    8  UNP  P01315    THR    95 CONFLICT                       
SEQADV 3GKY VAL A   16  UNP  P01315    LEU   103 CONFLICT                       
SEQADV 3GKY HIS C    8  UNP  P01315    THR    95 CONFLICT                       
SEQADV 3GKY VAL C   16  UNP  P01315    LEU   103 CONFLICT                       
SEQRES   1 A   21  GLY ILE VAL GLU GLN CYS CYS HIS SER ILE CYS SER LEU          
SEQRES   2 A   21  TYR GLN VAL GLU ASN TYR CYS ASN                              
SEQRES   1 B   30  PHE VAL ASN GLN HIS LEU CYS GLY SER HIS LEU VAL GLU          
SEQRES   2 B   30  ALA LEU TYR LEU VAL CYS GLY GLU ARG GLY PHE PHE TYR          
SEQRES   3 B   30  THR PRO LYS ALA                                              
SEQRES   1 C   21  GLY ILE VAL GLU GLN CYS CYS HIS SER ILE CYS SER LEU          
SEQRES   2 C   21  TYR GLN VAL GLU ASN TYR CYS ASN                              
SEQRES   1 D   30  PHE VAL ASN GLN HIS LEU CYS GLY SER HIS LEU VAL GLU          
SEQRES   2 D   30  ALA LEU TYR LEU VAL CYS GLY GLU ARG GLY PHE PHE TYR          
SEQRES   3 D   30  THR PRO LYS ALA                                              
HET     ZN  B  31       1                                                       
HET     CL  B  32       1                                                       
HET    IPH  C 100       7                                                       
HET     ZN  D  31       1                                                       
HET     CL  D  32       1                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM      CL CHLORIDE ION                                                     
HETNAM     IPH PHENOL                                                           
FORMUL   5   ZN    2(ZN 2+)                                                     
FORMUL   6   CL    2(CL 1-)                                                     
FORMUL   7  IPH    C6 H6 O                                                      
FORMUL  10  HOH   *125(H2 O)                                                    
HELIX    1   1 GLY A    1  CYS A    7  1                                   7    
HELIX    2   2 SER A   12  ASN A   18  1                                   7    
HELIX    3   3 GLY B    8  GLY B   20  1                                  13    
HELIX    4   4 GLU B   21  GLY B   23  5                                   3    
HELIX    5   5 GLY C    1  CYS C    7  1                                   7    
HELIX    6   6 SER C   12  ASN C   18  1                                   7    
HELIX    7   7 ASN D    3  GLY D   20  1                                  18    
HELIX    8   8 GLU D   21  GLY D   23  5                                   3    
SHEET    1   A 2 PHE B  24  TYR B  26  0                                        
SHEET    2   A 2 PHE D  24  TYR D  26 -1  O  PHE D  24   N  TYR B  26           
SSBOND   1 CYS A    6    CYS A   11                          1555   1555  2.04  
SSBOND   2 CYS A    7    CYS B    7                          1555   1555  2.03  
SSBOND   3 CYS A   20    CYS B   19                          1555   1555  2.03  
SSBOND   4 CYS C    6    CYS C   11                          1555   1555  2.02  
SSBOND   5 CYS C    7    CYS D    7                          1555   1555  2.04  
SSBOND   6 CYS C   20    CYS D   19                          1555   1555  2.03  
LINK         NE2 HIS B  10                ZN    ZN B  31     1555   1555  2.08  
LINK         NE2 HIS D  10                ZN    ZN D  31     1555   1555  2.07  
SITE     1 AC1  2 HIS B  10   CL B  32                                          
SITE     1 AC2  2  ZN B  31  HOH B  89                                          
SITE     1 AC3  8 CYS C   6  SER C   9  ILE C  10  CYS C  11                    
SITE     2 AC3  8 HOH C  51  HIS D   5  HIS D  10  LEU D  11                    
SITE     1 AC4  2 HIS D  10   CL D  32                                          
SITE     1 AC5  2 HIS D  10   ZN D  31                                          
CRYST1   78.225   78.225   36.712  90.00  90.00 120.00 H 3          18          
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      0.012784  0.007381  0.000000        0.00000                         
SCALE2      0.000000  0.014761  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.027239        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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