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Database: PDB
Entry: 2OR3
LinkDB: 2OR3
Original site: 2OR3 
HEADER    CHAPERONE                               01-FEB-07   2OR3              
TITLE     PRE-OXIDATION COMPLEX OF HUMAN DJ-1                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN DJ-1;                                              
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: ONCOGENE DJ1;                                               
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: PARK7;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET15B                                    
KEYWDS    CYSTEINE OXIDATION, NUCLEOPHILE ELBOW, CHAPERONE                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.C.WITT,M.LAKSHMINARASIMHAN,M.A.WILSON                               
REVDAT   4   22-JUL-08 2OR3    1       JRNL                                     
REVDAT   3   08-JUL-08 2OR3    1       JRNL                                     
REVDAT   2   01-JUL-08 2OR3    1       JRNL   VERSN                             
REVDAT   1   13-FEB-07 2OR3    0                                                
JRNL        AUTH   A.C.WITT,M.LAKSHMINARASIMHAN,B.C.REMINGTON,S.HASIM,          
JRNL        AUTH 2 E.POZHARSKI,M.A.WILSON                                       
JRNL        TITL   CYSTEINE PKA DEPRESSION BY A PROTONATED GLUTAMIC             
JRNL        TITL 2 ACID IN HUMAN DJ-1.                                          
JRNL        REF    BIOCHEMISTRY                  V.  47  7430 2008              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   18570440                                                     
JRNL        DOI    10.1021/BI800282D                                            
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : SHELXL-97                                            
REMARK   3   AUTHORS     : G.M.SHELDRICK                                        
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 22.45                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.8                           
REMARK   3   CROSS-VALIDATION METHOD           : FREE R                         
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).                         
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL                   
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.136                  
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.182                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.000                  
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 5761                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 114654                 
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).                     
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : NULL                   
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : 0.109                  
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : 0.154                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 5.000                  
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : 4273                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : 86103                  
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS      : 2955                                          
REMARK   3   NUCLEIC ACID ATOMS : 0                                             
REMARK   3   HETEROGEN ATOMS    : 10                                            
REMARK   3   SOLVENT ATOMS      : 583                                           
REMARK   3                                                                      
REMARK   3  MODEL REFINEMENT.                                                   
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : 3302.50                 
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : 2794.00                 
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : 24                      
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : 31968                   
REMARK   3   NUMBER OF RESTRAINTS                     : 40468                   
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.                        
REMARK   3   BOND LENGTHS                         (A) : 0.013                   
REMARK   3   ANGLE DISTANCES                      (A) : 0.031                   
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000                   
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : 0.030                   
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : 0.069                   
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.077                   
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : 0.019                   
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : 0.004                   
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : 0.051                   
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : 0.115                   
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED: NULL                                                  
REMARK   3                                                                      
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH & HUBER                        
REMARK   3   SPECIAL CASE: NULL                                                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: AUTHORS STATE THAT THERE WERE SLIGHT      
REMARK   3  MODEL CHANGES AFTER COMBINING THE TEST AND WORKING SET, SO THE      
REMARK   3  FINAL R FACTOR IS LOWER THAN THE WORKING R FACTOR.                  
REMARK   4                                                                      
REMARK   4 2OR3 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-FEB-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB041482.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-MAR-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 14-BM-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9                                
REMARK 200  MONOCHROMATOR                  : BENT GE(111)                       
REMARK 200  OPTICS                         : BENT CONICAL SI MIRROR             
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 114729                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 22.450                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.8                               
REMARK 200  DATA REDUNDANCY                : 5.300                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.06500                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 24.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.24                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.20                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.70200                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.040                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1P5F                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.32                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 28% PEG 4000, 200 MM AMMONIUM            
REMARK 280  SULFATE, 50 MM SODIUM ACETATE, 2.5 MM EPIGALLOCATECHIN 3-           
REMARK 280  GALLATE, PH 6.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE         
REMARK 280  298K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       21.95700            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       49.41450            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       42.88300            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       49.41450            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       21.95700            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       42.88300            
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: 3220 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14770 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -50.0 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     MET B     1                                                      
REMARK 465     ASP B   189                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A   5   NH1 -  CZ  -  NH2 ANGL. DEV. =   7.5 DEGREES          
REMARK 500    ARG A   5   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.9 DEGREES          
REMARK 500    ARG A  48   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500    LYS A  89   CD  -  CE  -  NZ  ANGL. DEV. =  16.6 DEGREES          
REMARK 500    ASP A 131   CB  -  CG  -  OD2 ANGL. DEV. =  -5.9 DEGREES          
REMARK 500    GLU A 143   OE1 -  CD  -  OE2 ANGL. DEV. =  15.5 DEGREES          
REMARK 500    ARG A 145   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500    LYS A 188   CA  -  CB  -  CG  ANGL. DEV. =  18.4 DEGREES          
REMARK 500    GLU B  94   OE1 -  CD  -  OE2 ANGL. DEV. =  -7.3 DEGREES          
REMARK 500    GLU B  96   OE1 -  CD  -  OE2 ANGL. DEV. =   8.0 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    CYS A 106     -107.43     72.50                                   
REMARK 500    CYS B 106     -106.42     72.03                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B 645        DISTANCE =  7.24 ANGSTROMS                       
REMARK 525    HOH A 797        DISTANCE =  5.91 ANGSTROMS                       
REMARK 525    HOH A 830        DISTANCE =  6.76 ANGSTROMS                       
REMARK 525    HOH B 837        DISTANCE =  6.72 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 600                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 601                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1P5F   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1SOA   RELATED DB: PDB                                   
DBREF  2OR3 A    1   189  UNP    Q99497   PARK7_HUMAN      1    189             
DBREF  2OR3 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                                  
HET    SO4  A 600       5                                                       
HET    SO4  B 601       5                                                       
HETNAM     SO4 SULFATE ION                                                      
FORMUL   3  SO4    2(O4 S 2-)                                                   
FORMUL   5  HOH   *583(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  SER A   85  1                                  11    
HELIX    4   4 SER A   85  ARG A   98  1                                  14    
HELIX    5   5 GLY A  108  HIS A  115  1                                   8    
HELIX    6   6 HIS A  126  LEU A  128  5                                   3    
HELIX    7   7 ALA A  129  ASN A  135  1                                   7    
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   15  ALA B   29  1                                  15    
HELIX   13  13 LEU B   58  GLU B   64  1                                   7    
HELIX   14  14 GLY B   75  GLU B   84  1                                  10    
HELIX   15  15 SER B   85  ARG B   98  1                                  14    
HELIX   16  16 PRO B  109  HIS B  115  1                                   7    
HELIX   17  17 HIS B  126  LEU B  128  5                                   3    
HELIX   18  18 ALA B  129  ASN B  135  1                                   7    
HELIX   19  19 GLY B  157  GLY B  159  5                                   3    
HELIX   20  20 THR B  160  GLY B  174  1                                  15    
HELIX   21  21 GLY B  174  ALA B  183  1                                  10    
HELIX   22  22 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  ALA A   6   O  THR A  34           
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  VAL A  70           
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  ILE B  52 -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  VAL B  70           
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         0.52                     
CISPEP   2 GLY B   65    PRO B   66          0         1.98                     
SITE     1 AC1  6 GLU A  15  ARG A  48  GLY A  75  ASN A  76                    
SITE     2 AC1  6 HOH A 639  HOH A 719                                          
SITE     1 AC2  5 ARG B  48  GLY B  75  ASN B  76  HOH B 634                    
SITE     2 AC2  5 HOH B 806                                                     
CRYST1   43.914   85.766   98.829  90.00  90.00  90.00 P 21 21 21    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      0.022772  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011660  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010118        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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