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Database: PDB
Entry: 1PE0
LinkDB: 1PE0
Original site: 1PE0 
HEADER    PROTEIN BINDING                         20-MAY-03   1PE0              
TITLE     CRYSTAL STRUCTURE OF THE K130R MUTANT OF HUMAN DJ-1                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DJ-1;                                                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    DJ-1, PROTEIN BINDING                                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    X.TAO,L.TONG                                                          
REVDAT   3   24-FEB-09 1PE0    1       VERSN                                    
REVDAT   2   19-AUG-03 1PE0    1       JRNL                                     
REVDAT   1   24-JUN-03 1PE0    0                                                
JRNL        AUTH   X.TAO,L.TONG                                                 
JRNL        TITL   CRYSTAL STRUCTURE OF HUMAN DJ-1, A PROTEIN                   
JRNL        TITL 2 ASSOCIATED WITH EARLY ONSET PARKINSON'S DISEASE.             
JRNL        REF    J.BIOL.CHEM.                  V. 278 31372 2003              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   12761214                                                     
JRNL        DOI    10.1074/JBC.M304221200                                       
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
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) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.54                          
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)   (%) : 92.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 36794                          
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) : 0.191                           
REMARK   3   FREE R VALUE                     : 0.231                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.600                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2790                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.004                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.76                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 80.20                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 2945                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2110                       
REMARK   3   BIN FREE R VALUE                    : 0.2490                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 7.10                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 226                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.017                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2754                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 470                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 12.20                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 18.70                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.39000                                             
REMARK   3    B22 (A**2) : 4.75000                                              
REMARK   3    B33 (A**2) : -4.36000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.54000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
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) : 0.23                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.14                            
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) : 22.80                           
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) : 1.170 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.770 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.900 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.690 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.33                                                 
REMARK   3   BSOL        : 44.45                                                
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   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1PE0 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-MAY-03.                  
REMARK 100 THE RCSB ID CODE IS RCSB019261.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-APR-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X4A                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9724                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 39841                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.8                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.06500                            
REMARK 200  R SYM                      (I) : 0.06500                            
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) : 1.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.76                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 82.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.26400                            
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: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: COMO                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.60                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG3350, 100 MM BIS-TRIS(7.0),       
REMARK 280  50 MM CACL2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       38.85300            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       39.08650            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       38.85300            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       39.08650            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2660 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14600 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 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     MET A     1                                                      
REMARK 465     ASP A   189                                                      
REMARK 465     LEU A   190                                                      
REMARK 465     GLU A   191                                                      
REMARK 465     HIS A   192                                                      
REMARK 465     HIS A   193                                                      
REMARK 465     HIS A   194                                                      
REMARK 465     HIS A   195                                                      
REMARK 465     HIS A   196                                                      
REMARK 465     HIS A   197                                                      
REMARK 465     MET B   201                                                      
REMARK 465     ASP B   389                                                      
REMARK 465     LEU B   390                                                      
REMARK 465     GLU B   391                                                      
REMARK 465     HIS B   392                                                      
REMARK 465     HIS B   393                                                      
REMARK 465     HIS B   394                                                      
REMARK 465     HIS B   395                                                      
REMARK 465     HIS B   396                                                      
REMARK 465     HIS B   397                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A  4115     O    HOH A  4439              2.08            
REMARK 500   O    HOH A  4261     O    HOH A  4468              2.13            
REMARK 500   O    HOH B  4457     O    HOH B  4458              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    CYS A 106     -106.19     66.25                                   
REMARK 500    LYS B 263       10.22    -68.06                                   
REMARK 500    GLU B 264       71.19   -107.30                                   
REMARK 500    CYS B 306     -107.22     65.42                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1PDV   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN DJ-1, P 31 2 1 SPACE GROUP                
REMARK 900 RELATED ID: 1PDW   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN DJ-1, P 1 21 1 SPACE GROUP                
DBREF  1PE0 A    1   189  UNP    Q99497   PARK7_HUMAN      1    189             
DBREF  1PE0 B  201   389  UNP    Q99497   PARK7_HUMAN      1    189             
SEQADV 1PE0 ARG A  130  UNP  Q99497    LYS   130 ENGINEERED                     
SEQADV 1PE0 LEU A  190  UNP  Q99497              EXPRESSION TAG                 
SEQADV 1PE0 GLU A  191  UNP  Q99497              EXPRESSION TAG                 
SEQADV 1PE0 HIS A  192  UNP  Q99497              EXPRESSION TAG                 
SEQADV 1PE0 HIS A  193  UNP  Q99497              EXPRESSION TAG                 
SEQADV 1PE0 HIS A  194  UNP  Q99497              EXPRESSION TAG                 
SEQADV 1PE0 HIS A  195  UNP  Q99497              EXPRESSION TAG                 
SEQADV 1PE0 HIS A  196  UNP  Q99497              EXPRESSION TAG                 
SEQADV 1PE0 HIS A  197  UNP  Q99497              EXPRESSION TAG                 
SEQADV 1PE0 ARG B  330  UNP  Q99497    LYS   130 ENGINEERED                     
SEQADV 1PE0 LEU B  390  UNP  Q99497              EXPRESSION TAG                 
SEQADV 1PE0 GLU B  391  UNP  Q99497              EXPRESSION TAG                 
SEQADV 1PE0 HIS B  392  UNP  Q99497              EXPRESSION TAG                 
SEQADV 1PE0 HIS B  393  UNP  Q99497              EXPRESSION TAG                 
SEQADV 1PE0 HIS B  394  UNP  Q99497              EXPRESSION TAG                 
SEQADV 1PE0 HIS B  395  UNP  Q99497              EXPRESSION TAG                 
SEQADV 1PE0 HIS B  396  UNP  Q99497              EXPRESSION TAG                 
SEQADV 1PE0 HIS B  397  UNP  Q99497              EXPRESSION TAG                 
SEQRES   1 A  197  MET ALA SER LYS ARG ALA LEU VAL ILE LEU ALA LYS GLY          
SEQRES   2 A  197  ALA GLU GLU MET GLU THR VAL ILE PRO VAL ASP VAL MET          
SEQRES   3 A  197  ARG ARG ALA GLY ILE LYS VAL THR VAL ALA GLY LEU ALA          
SEQRES   4 A  197  GLY LYS ASP PRO VAL GLN CYS SER ARG ASP VAL VAL ILE          
SEQRES   5 A  197  CYS PRO ASP ALA SER LEU GLU ASP ALA LYS LYS GLU GLY          
SEQRES   6 A  197  PRO TYR ASP VAL VAL VAL LEU PRO GLY GLY ASN LEU GLY          
SEQRES   7 A  197  ALA GLN ASN LEU SER GLU SER ALA ALA VAL LYS GLU ILE          
SEQRES   8 A  197  LEU LYS GLU GLN GLU ASN ARG LYS GLY LEU ILE ALA ALA          
SEQRES   9 A  197  ILE CYS ALA GLY PRO THR ALA LEU LEU ALA HIS GLU ILE          
SEQRES  10 A  197  GLY PHE GLY SER LYS VAL THR THR HIS PRO LEU ALA ARG          
SEQRES  11 A  197  ASP LYS MET MET ASN GLY GLY HIS TYR THR TYR SER GLU          
SEQRES  12 A  197  ASN ARG VAL GLU LYS ASP GLY LEU ILE LEU THR SER ARG          
SEQRES  13 A  197  GLY PRO GLY THR SER PHE GLU PHE ALA LEU ALA ILE VAL          
SEQRES  14 A  197  GLU ALA LEU ASN GLY LYS GLU VAL ALA ALA GLN VAL LYS          
SEQRES  15 A  197  ALA PRO LEU VAL LEU LYS ASP LEU GLU HIS HIS HIS HIS          
SEQRES  16 A  197  HIS HIS                                                      
SEQRES   1 B  197  MET ALA SER LYS ARG ALA LEU VAL ILE LEU ALA LYS GLY          
SEQRES   2 B  197  ALA GLU GLU MET GLU THR VAL ILE PRO VAL ASP VAL MET          
SEQRES   3 B  197  ARG ARG ALA GLY ILE LYS VAL THR VAL ALA GLY LEU ALA          
SEQRES   4 B  197  GLY LYS ASP PRO VAL GLN CYS SER ARG ASP VAL VAL ILE          
SEQRES   5 B  197  CYS PRO ASP ALA SER LEU GLU ASP ALA LYS LYS GLU GLY          
SEQRES   6 B  197  PRO TYR ASP VAL VAL VAL LEU PRO GLY GLY ASN LEU GLY          
SEQRES   7 B  197  ALA GLN ASN LEU SER GLU SER ALA ALA VAL LYS GLU ILE          
SEQRES   8 B  197  LEU LYS GLU GLN GLU ASN ARG LYS GLY LEU ILE ALA ALA          
SEQRES   9 B  197  ILE CYS ALA GLY PRO THR ALA LEU LEU ALA HIS GLU ILE          
SEQRES  10 B  197  GLY PHE GLY SER LYS VAL THR THR HIS PRO LEU ALA ARG          
SEQRES  11 B  197  ASP LYS MET MET ASN GLY GLY HIS TYR THR TYR SER GLU          
SEQRES  12 B  197  ASN ARG VAL GLU LYS ASP GLY LEU ILE LEU THR SER ARG          
SEQRES  13 B  197  GLY PRO GLY THR SER PHE GLU PHE ALA LEU ALA ILE VAL          
SEQRES  14 B  197  GLU ALA LEU ASN GLY LYS GLU VAL ALA ALA GLN VAL LYS          
SEQRES  15 B  197  ALA PRO LEU VAL LEU LYS ASP LEU GLU HIS HIS HIS HIS          
SEQRES  16 B  197  HIS HIS                                                      
FORMUL   3  HOH   *470(H2 O)                                                    
HELIX    1   1 GLU A   15  ALA A   29  1                                  15    
HELIX    2   2 LEU A   58  GLU A   64  1                                   7    
HELIX    3   3 GLY A   75  GLU A   84  1                                  10    
HELIX    4   4 SER A   85  ARG A   98  1                                  14    
HELIX    5   5 PRO A  109  HIS A  115  1                                   7    
HELIX    6   6 HIS A  126  LEU A  128  5                                   3    
HELIX    7   7 ALA A  129  MET A  134  1                                   6    
HELIX    8   8 GLY A  157  GLY A  159  5                                   3    
HELIX    9   9 THR A  160  GLY A  174  1                                  15    
HELIX   10  10 GLY A  174  ALA A  183  1                                  10    
HELIX   11  11 PRO A  184  VAL A  186  5                                   3    
HELIX   12  12 GLU B  215  ALA B  229  1                                  15    
HELIX   13  13 LEU B  258  LYS B  263  1                                   6    
HELIX   14  14 GLY B  275  SER B  285  1                                  11    
HELIX   15  15 SER B  285  ARG B  298  1                                  14    
HELIX   16  16 GLY B  308  HIS B  315  1                                   8    
HELIX   17  17 HIS B  326  LEU B  328  5                                   3    
HELIX   18  18 ALA B  329  MET B  334  1                                   6    
HELIX   19  19 GLY B  357  GLY B  359  5                                   3    
HELIX   20  20 THR B  360  GLY B  374  1                                  15    
HELIX   21  21 GLY B  374  ALA B  383  1                                  10    
HELIX   22  22 PRO B  384  VAL B  386  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 251  CYS B 253 -1  O  CYS B 253   N  VAL A  51           
SHEET    4   B 4 VAL B 244  GLN B 245 -1  N  VAL B 244   O  ILE B 252           
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 256  SER B 257  0                                        
SHEET    2   D 7 LYS B 232  GLY B 237  1  N  GLY B 237   O  ALA B 256           
SHEET    3   D 7 ARG B 205  LEU B 210  1  N  LEU B 210   O  ALA B 236           
SHEET    4   D 7 VAL B 269  LEU B 272  1  O  VAL B 271   N  LEU B 207           
SHEET    5   D 7 LEU B 301  ILE B 305  1  O  ALA B 303   N  LEU B 272           
SHEET    6   D 7 ILE B 352  SER B 355  1  O  LEU B 353   N  ILE B 302           
SHEET    7   D 7 VAL B 346  ASP B 349 -1  N  GLU B 347   O  THR B 354           
SHEET    1   E 2 LYS B 322  VAL B 323  0                                        
SHEET    2   E 2 THR B 340  TYR B 341  1  O  THR B 340   N  VAL B 323           
CRYST1   77.706   78.173   63.819  90.00 108.88  90.00 C 1 2 1       8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.012869  0.000000  0.004401        0.00000                         
SCALE2      0.000000  0.012792  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016560        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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