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Database: PDB
Entry: 1UCF
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Original site: 1UCF 
HEADER    RNA BINDING PROTEIN                     11-APR-03   1UCF              
TITLE     THE CRYSTAL STRUCTURE OF DJ-1, A PROTEIN RELATED TO MALE              
TITLE    2 FERTILITY AND PARKINSON'S DISEASE                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RNA-BINDING PROTEIN REGULATORY SUBUNIT;                    
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: DJ-1;                                                       
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: DJ-1;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PGEX-6P                                   
KEYWDS    FLAVODOXIN-LIKE ROSSMANN FOLD, RNA BINDING PROTEIN                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.HONBOU,N.N.SUZUKI,M.HORIUCHI,T.NIKI,T.TAIRA,H.ARIGA,                
AUTHOR   2 F.INAGAKI                                                            
REVDAT   2   24-FEB-09 1UCF    1       VERSN                                    
REVDAT   1   19-AUG-03 1UCF    0                                                
JRNL        AUTH   K.HONBOU,N.N.SUZUKI,M.HORIUCHI,T.NIKI,T.TAIRA,               
JRNL        AUTH 2 H.ARIGA,F.INAGAKI                                            
JRNL        TITL   THE CRYSTAL STRUCTURE OF DJ-1, A PROTEIN RELATED             
JRNL        TITL 2 TO MALE FERTILITY AND PARKINSON'S DISEASE                    
JRNL        REF    J.BIOL.CHEM.                  V. 278 31380 2003              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   12796482                                                     
JRNL        DOI    10.1074/JBC.M305878200                                       
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.95 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
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) : 1.95                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 37.52                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 128474.640                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 95.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 32766                          
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) : 0.170                           
REMARK   3   FREE R VALUE                     : 0.195                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 3277                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.003                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.95                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.07                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 87.40                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 4474                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2100                       
REMARK   3   BIN FREE R VALUE                    : 0.2480                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 10.60                        
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 532                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.011                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2718                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 321                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 13.50                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.70                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.15000                                              
REMARK   3    B22 (A**2) : 1.15000                                              
REMARK   3    B33 (A**2) : -2.30000                                             
REMARK   3    B12 (A**2) : 1.96000                                              
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) : 0.18                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.13                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.22                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.18                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.005                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.30                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.00                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.91                            
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) : 1.140 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.740 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.080 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.030 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.37                                                 
REMARK   3   BSOL        : 50.27                                                
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  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1UCF COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-APR-03.                  
REMARK 100 THE RCSB ID CODE IS RCSB005673.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-MAY-01                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU ULTRAX 18                   
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : YALE MIRRORS                       
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 34488                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 100.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.2                               
REMARK 200  DATA REDUNDANCY                : 4.200                              
REMARK 200  R MERGE                    (I) : 0.07300                            
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) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.97                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.39900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR                          
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.67                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.86                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM CITRATE, HEPES, DTT, PH 7.5,      
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31                             
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                                                                      
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       24.95900            
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       49.91800            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2590 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14630 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
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     ASP A   189                                                      
REMARK 465     ASP B   189                                                      
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     LYS A  41    CG   CD   CE   NZ                                   
REMARK 470     LYS A  63    CG   CD   CE   NZ                                   
REMARK 470     GLU A  94    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  99    CG   CD   CE   NZ                                   
REMARK 470     LYS A 175    CG   CD   CE   NZ                                   
REMARK 470     LYS A 188    CG   CD   CE   NZ                                   
REMARK 470     LYS B  41    CG   CD   CE   NZ                                   
REMARK 470     GLN B  80    CG   CD   OE1  NE2                                  
REMARK 470     GLU B  90    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  99    CG   CD   CE   NZ                                   
REMARK 470     GLU B 176    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 188    CG   CD   CE   NZ                                   
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    LYS A  99       42.38     70.57                                   
REMARK 500    CYS A 106     -110.90     66.15                                   
REMARK 500    CYS B 106     -107.91     64.95                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  1UCF A    1   189  UNP    Q99497   PARK7_HUMAN      1    189             
DBREF  1UCF B    1   189  UNP    Q99497   PARK7_HUMAN      1    189             
SEQRES   1 A  189  MET ALA SER LYS ARG ALA LEU VAL ILE LEU ALA LYS GLY          
SEQRES   2 A  189  ALA GLU GLU MET GLU THR VAL ILE PRO VAL ASP VAL MET          
SEQRES   3 A  189  ARG ARG ALA GLY ILE LYS VAL THR VAL ALA GLY LEU ALA          
SEQRES   4 A  189  GLY LYS ASP PRO VAL GLN CYS SER ARG ASP VAL VAL ILE          
SEQRES   5 A  189  CYS PRO ASP ALA SER LEU GLU ASP ALA LYS LYS GLU GLY          
SEQRES   6 A  189  PRO TYR ASP VAL VAL VAL LEU PRO GLY GLY ASN LEU GLY          
SEQRES   7 A  189  ALA GLN ASN LEU SER GLU SER ALA ALA VAL LYS GLU ILE          
SEQRES   8 A  189  LEU LYS GLU GLN GLU ASN ARG LYS GLY LEU ILE ALA ALA          
SEQRES   9 A  189  ILE CYS ALA GLY PRO THR ALA LEU LEU ALA HIS GLU ILE          
SEQRES  10 A  189  GLY PHE GLY SER LYS VAL THR THR HIS PRO LEU ALA LYS          
SEQRES  11 A  189  ASP LYS MET MET ASN GLY GLY HIS TYR THR TYR SER GLU          
SEQRES  12 A  189  ASN ARG VAL GLU LYS ASP GLY LEU ILE LEU THR SER ARG          
SEQRES  13 A  189  GLY PRO GLY THR SER PHE GLU PHE ALA LEU ALA ILE VAL          
SEQRES  14 A  189  GLU ALA LEU ASN GLY LYS GLU VAL ALA ALA GLN VAL LYS          
SEQRES  15 A  189  ALA PRO LEU VAL LEU LYS ASP                                  
SEQRES   1 B  189  MET ALA SER LYS ARG ALA LEU VAL ILE LEU ALA LYS GLY          
SEQRES   2 B  189  ALA GLU GLU MET GLU THR VAL ILE PRO VAL ASP VAL MET          
SEQRES   3 B  189  ARG ARG ALA GLY ILE LYS VAL THR VAL ALA GLY LEU ALA          
SEQRES   4 B  189  GLY LYS ASP PRO VAL GLN CYS SER ARG ASP VAL VAL ILE          
SEQRES   5 B  189  CYS PRO ASP ALA SER LEU GLU ASP ALA LYS LYS GLU GLY          
SEQRES   6 B  189  PRO TYR ASP VAL VAL VAL LEU PRO GLY GLY ASN LEU GLY          
SEQRES   7 B  189  ALA GLN ASN LEU SER GLU SER ALA ALA VAL LYS GLU ILE          
SEQRES   8 B  189  LEU LYS GLU GLN GLU ASN ARG LYS GLY LEU ILE ALA ALA          
SEQRES   9 B  189  ILE CYS ALA GLY PRO THR ALA LEU LEU ALA HIS GLU ILE          
SEQRES  10 B  189  GLY PHE GLY SER LYS VAL THR THR HIS PRO LEU ALA LYS          
SEQRES  11 B  189  ASP LYS MET MET ASN GLY GLY HIS TYR THR TYR SER GLU          
SEQRES  12 B  189  ASN ARG VAL GLU LYS ASP GLY LEU ILE LEU THR SER ARG          
SEQRES  13 B  189  GLY PRO GLY THR SER PHE GLU PHE ALA LEU ALA ILE VAL          
SEQRES  14 B  189  GLU ALA LEU ASN GLY LYS GLU VAL ALA ALA GLN VAL LYS          
SEQRES  15 B  189  ALA PRO LEU VAL LEU LYS ASP                                  
FORMUL   3  HOH   *321(H2 O)                                                    
HELIX    1   1 GLU A   15  ALA A   29  1                                  15    
HELIX    2   2 LEU A   58  LYS A   62  1                                   5    
HELIX    3   3 LYS A   63  GLY A   65  5                                   3    
HELIX    4   4 GLY A   75  SER A   85  1                                  11    
HELIX    5   5 SER A   85  LYS A   99  1                                  15    
HELIX    6   6 PRO A  109  HIS A  115  1                                   7    
HELIX    7   7 HIS A  126  LEU A  128  5                                   3    
HELIX    8   8 ALA A  129  MET A  134  1                                   6    
HELIX    9   9 GLY A  157  GLY A  159  5                                   3    
HELIX   10  10 THR A  160  GLY A  174  1                                  15    
HELIX   11  11 GLY A  174  ALA A  183  1                                  10    
HELIX   12  12 PRO A  184  VAL A  186  5                                   3    
HELIX   13  13 GLU B   15  ALA B   29  1                                  15    
HELIX   14  14 LEU B   58  LYS B   63  1                                   6    
HELIX   15  15 GLY B   75  SER B   85  1                                  11    
HELIX   16  16 SER B   85  ARG B   98  1                                  14    
HELIX   17  17 PRO B  109  HIS B  115  1                                   7    
HELIX   18  18 HIS B  126  LEU B  128  5                                   3    
HELIX   19  19 ALA B  129  MET B  134  1                                   6    
HELIX   20  20 GLY B  157  GLY B  159  5                                   3    
HELIX   21  21 THR B  160  GLY B  174  1                                  15    
HELIX   22  22 GLY B  174  ALA B  183  1                                  10    
HELIX   23  23 PRO B  184  VAL B  186  5                                   3    
SHEET    1   A 7 ALA A  56  SER A  57  0                                        
SHEET    2   A 7 LYS A  32  GLY A  37  1  N  GLY A  37   O  ALA A  56           
SHEET    3   A 7 ARG A   5  LEU A  10  1  N  LEU A  10   O  ALA A  36           
SHEET    4   A 7 VAL A  69  LEU A  72  1  O  VAL A  71   N  LEU A   7           
SHEET    5   A 7 LEU A 101  ILE A 105  1  O  ALA A 103   N  LEU A  72           
SHEET    6   A 7 ILE A 152  SER A 155  1  O  LEU A 153   N  ILE A 102           
SHEET    7   A 7 VAL A 146  ASP A 149 -1  N  GLU A 147   O  THR A 154           
SHEET    1   B 4 VAL A  44  GLN A  45  0                                        
SHEET    2   B 4 VAL A  51  CYS A  53 -1  O  ILE A  52   N  VAL A  44           
SHEET    3   B 4 VAL B  51  CYS B  53 -1  O  VAL B  51   N  CYS A  53           
SHEET    4   B 4 VAL B  44  GLN B  45 -1  N  VAL B  44   O  ILE B  52           
SHEET    1   C 2 LYS A 122  VAL A 123  0                                        
SHEET    2   C 2 THR A 140  TYR A 141  1  O  THR A 140   N  VAL A 123           
SHEET    1   D 7 ALA B  56  SER B  57  0                                        
SHEET    2   D 7 LYS B  32  GLY B  37  1  N  GLY B  37   O  ALA B  56           
SHEET    3   D 7 ARG B   5  LEU B  10  1  N  LEU B  10   O  ALA B  36           
SHEET    4   D 7 VAL B  69  LEU B  72  1  O  VAL B  71   N  LEU B   7           
SHEET    5   D 7 LEU B 101  ILE B 105  1  O  ALA B 103   N  LEU B  72           
SHEET    6   D 7 ILE B 152  SER B 155  1  O  LEU B 153   N  ILE B 102           
SHEET    7   D 7 VAL B 146  ASP B 149 -1  N  GLU B 147   O  THR B 154           
SHEET    1   E 2 LYS B 122  VAL B 123  0                                        
SHEET    2   E 2 THR B 140  TYR B 141  1  O  THR B 140   N  VAL B 123           
CISPEP   1 GLY A   65    PRO A   66          0         0.25                     
CISPEP   2 GLY B   65    PRO B   66          0         0.25                     
CRYST1   75.039   75.039   74.877  90.00  90.00 120.00 P 31          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      0.013326  0.007694  0.000000        0.00000                         
SCALE2      0.000000  0.015388  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013355        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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