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Database: PDB
Entry: 3SF8
LinkDB: 3SF8
Original site: 3SF8 
HEADER    ONCOPROTEIN,UNKNOWN FUNCTION            13-JUN-11   3SF8              
TITLE     STRUCTURAL INSIGHTS INTO THIOL STABILIZATION OF DJ-1                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN DJ-1;                                              
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: ONCOGENE DJ1, PARKINSON DISEASE PROTEIN 7;                  
COMPND   5 EC: 3.4.-.-;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: PROTEIN DJ-1;                                              
COMPND   9 CHAIN: B;                                                            
COMPND  10 SYNONYM: ONCOGENE DJ1, PARKINSON DISEASE PROTEIN 7;                  
COMPND  11 EC: 3.4.-.-;                                                         
COMPND  12 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;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: PARK7;                                                         
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    OXIDATIVE STRESS, REDOX REGULATION, CYSTEINE OXIDATION, PROTECTING    
KEYWDS   2 DJ-1 OXIDATION, REDUCED DJ-1, CLASS I GLUTAMINE AMIDOTRANSFERASE     
KEYWDS   3 FAMILY, CYTOPROTECTIVE ACTIVITY AGAINST OXIDATIVE STRESS; CYSTEINE   
KEYWDS   4 SULFENIC ACID MODIFICATION, HYDROLASE, ONCOPROTEIN,UNKNOWN FUNCTION  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.PREMKUMAR,M.K.DOBACZEWSKA,S.J.RIEDL                                 
REVDAT   2   23-NOV-11 3SF8    1       JRNL                                     
REVDAT   1   05-OCT-11 3SF8    0                                                
JRNL        AUTH   L.PREMKUMAR,M.K.DOBACZEWSKA,S.J.RIEDL                        
JRNL        TITL   IDENTIFICATION OF AN ARTIFICIAL PEPTIDE MOTIF THAT BINDS AND 
JRNL        TITL 2 STABILIZES REDUCED HUMAN DJ-1.                               
JRNL        REF    J.STRUCT.BIOL.                V. 176   414 2011              
JRNL        REFN                   ISSN 1047-8477                               
JRNL        PMID   21893204                                                     
JRNL        DOI    10.1016/J.JSB.2011.08.011                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.56 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0102                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.56                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 42954                          
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 + TEST SET) : 0.174                           
REMARK   3   R VALUE            (WORKING SET) : 0.172                           
REMARK   3   FREE R VALUE                     : 0.211                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2318                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.56                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.60                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2980                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 89.54                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2500                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 154                          
REMARK   3   BIN FREE R VALUE                    : 0.2840                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2777                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 341                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.12                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.51000                                             
REMARK   3    B22 (A**2) : 1.40000                                              
REMARK   3    B33 (A**2) : -1.52000                                             
REMARK   3    B12 (A**2) : -0.00000                                             
REMARK   3    B13 (A**2) : -0.73000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.094         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.071         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.058         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.968                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.955                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2920 ; 0.013 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3964 ; 1.421 ; 1.999       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   408 ;12.185 ; 5.049       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   107 ;41.738 ;25.514       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   545 ;13.786 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    15 ;17.019 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   468 ; 0.108 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2149 ; 0.008 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1922 ; 1.888 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3092 ; 3.194 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   998 ; 4.418 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   859 ; 7.041 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2920 ; 2.588 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3SF8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-JUN-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB066129.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-MAR-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 6.5                                
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 FR-E SUPERBRIGHT            
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS HTC                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 47218                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.530                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.0                               
REMARK 200  DATA REDUNDANCY                : 4.900                              
REMARK 200  R MERGE                    (I) : 0.04400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.53                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.61                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 82.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.25200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 1PDV                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 41.37                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 45% (V/V) POLYPROYLENE GLYCOL 400, 0.1   
REMARK 280  M BIS-TRIS, PH 6.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE      
REMARK 280  293K                                                                
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       70.94000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       20.91550            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       70.94000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       20.91550            
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: 2760 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15280 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     MET B     1                                                      
REMARK 465     ASP B   189                                                      
REMARK 465     LEU B   190                                                      
REMARK 465     GLU B   191                                                      
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    CSO A 106     -110.57     76.73                                   
REMARK 500    CYS B 106     -105.65     75.64                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    PRO A  66        22.3      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  3SF8 A    1   189  UNP    Q99497   PARK7_HUMAN      1    189             
DBREF  3SF8 B    1   189  UNP    Q99497   PARK7_HUMAN      1    189             
SEQADV 3SF8 LEU A  190  UNP  Q99497              EXPRESSION TAG                 
SEQADV 3SF8 GLU A  191  UNP  Q99497              EXPRESSION TAG                 
SEQADV 3SF8 LEU B  190  UNP  Q99497              EXPRESSION TAG                 
SEQADV 3SF8 GLU B  191  UNP  Q99497              EXPRESSION TAG                 
SEQRES   1 A  191  MET ALA SER LYS ARG ALA LEU VAL ILE LEU ALA LYS GLY          
SEQRES   2 A  191  ALA GLU GLU MET GLU THR VAL ILE PRO VAL ASP VAL MET          
SEQRES   3 A  191  ARG ARG ALA GLY ILE LYS VAL THR VAL ALA GLY LEU ALA          
SEQRES   4 A  191  GLY LYS ASP PRO VAL GLN CYS SER ARG ASP VAL VAL ILE          
SEQRES   5 A  191  CYS PRO ASP ALA SER LEU GLU ASP ALA LYS LYS GLU GLY          
SEQRES   6 A  191  PRO TYR ASP VAL VAL VAL LEU PRO GLY GLY ASN LEU GLY          
SEQRES   7 A  191  ALA GLN ASN LEU SER GLU SER ALA ALA VAL LYS GLU ILE          
SEQRES   8 A  191  LEU LYS GLU GLN GLU ASN ARG LYS GLY LEU ILE ALA ALA          
SEQRES   9 A  191  ILE CSO ALA GLY PRO THR ALA LEU LEU ALA HIS GLU ILE          
SEQRES  10 A  191  GLY PHE GLY SER LYS VAL THR THR HIS PRO LEU ALA LYS          
SEQRES  11 A  191  ASP LYS MET MET ASN GLY GLY HIS TYR THR TYR SER GLU          
SEQRES  12 A  191  ASN ARG VAL GLU LYS ASP GLY LEU ILE LEU THR SER ARG          
SEQRES  13 A  191  GLY PRO GLY THR SER PHE GLU PHE ALA LEU ALA ILE VAL          
SEQRES  14 A  191  GLU ALA LEU ASN GLY LYS GLU VAL ALA ALA GLN VAL LYS          
SEQRES  15 A  191  ALA PRO LEU VAL LEU LYS ASP LEU GLU                          
SEQRES   1 B  191  MET ALA SER LYS ARG ALA LEU VAL ILE LEU ALA LYS GLY          
SEQRES   2 B  191  ALA GLU GLU MET GLU THR VAL ILE PRO VAL ASP VAL MET          
SEQRES   3 B  191  ARG ARG ALA GLY ILE LYS VAL THR VAL ALA GLY LEU ALA          
SEQRES   4 B  191  GLY LYS ASP PRO VAL GLN CYS SER ARG ASP VAL VAL ILE          
SEQRES   5 B  191  CYS PRO ASP ALA SER LEU GLU ASP ALA LYS LYS GLU GLY          
SEQRES   6 B  191  PRO TYR ASP VAL VAL VAL LEU PRO GLY GLY ASN LEU GLY          
SEQRES   7 B  191  ALA GLN ASN LEU SER GLU SER ALA ALA VAL LYS GLU ILE          
SEQRES   8 B  191  LEU LYS GLU GLN GLU ASN ARG LYS GLY LEU ILE ALA ALA          
SEQRES   9 B  191  ILE CYS ALA GLY PRO THR ALA LEU LEU ALA HIS GLU ILE          
SEQRES  10 B  191  GLY PHE GLY SER LYS VAL THR THR HIS PRO LEU ALA LYS          
SEQRES  11 B  191  ASP LYS MET MET ASN GLY GLY HIS TYR THR TYR SER GLU          
SEQRES  12 B  191  ASN ARG VAL GLU LYS ASP GLY LEU ILE LEU THR SER ARG          
SEQRES  13 B  191  GLY PRO GLY THR SER PHE GLU PHE ALA LEU ALA ILE VAL          
SEQRES  14 B  191  GLU ALA LEU ASN GLY LYS GLU VAL ALA ALA GLN VAL LYS          
SEQRES  15 B  191  ALA PRO LEU VAL LEU LYS ASP LEU GLU                          
MODRES 3SF8 CSO A  106  CYS  S-HYDROXYCYSTEINE                                  
HET    CSO  A 106       7                                                       
HETNAM     CSO S-HYDROXYCYSTEINE                                                
FORMUL   1  CSO    C3 H7 N O3 S                                                 
FORMUL   3  HOH   *341(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  GLU A   84  1                                  10    
HELIX    5   5 SER A   85  ARG A   98  1                                  14    
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 GLY B  108  HIS B  115  1                                   8    
HELIX   18  18 HIS B  126  LEU B  128  5                                   3    
HELIX   19  19 ALA B  129  ASN B  135  1                                   7    
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           
LINK         C   ILE A 105                 N   CSO A 106     1555   1555  1.34  
LINK         C   CSO A 106                 N   ALA A 107     1555   1555  1.34  
CISPEP   1 GLY A   65    PRO A   66          0        -3.75                     
CISPEP   2 GLY B   65    PRO B   66          0        -6.22                     
CRYST1  141.880   41.831   63.344  90.00 115.79  90.00 C 1 2 1       4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.007048  0.000000  0.003406        0.00000                         
SCALE2      0.000000  0.023906  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017533        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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