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Database: PDB
Entry: 5SY9
LinkDB: 5SY9
Original site: 5SY9 
HEADER    PROTEIN BINDING                         10-AUG-16   5SY9              
TITLE     ATOMIC RESOLUTION STRUCTURE OF E15Q MUTANT HUMAN DJ-1                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN DEGLYCASE DJ-1;                                    
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: DJ-1,ONCOGENE DJ1,PARKINSON DISEASE PROTEIN 7;              
COMPND   5 EC: 3.1.2.-,3.5.1.-;                                                 
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: 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: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET15B                                    
KEYWDS    DJ-1/PFPI SUPERFAMILY OXIDATIVE STRESS NUCLEOPHILE ELBOW, PROTEIN     
KEYWDS   2 BINDING                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.A.WILSON,J.LIN                                                      
REVDAT   6   04-OCT-23 5SY9    1       REMARK                                   
REVDAT   5   25-DEC-19 5SY9    1       REMARK                                   
REVDAT   4   13-SEP-17 5SY9    1       REMARK                                   
REVDAT   3   01-FEB-17 5SY9    1       JRNL                                     
REVDAT   2   04-JAN-17 5SY9    1       JRNL                                     
REVDAT   1   28-DEC-16 5SY9    0                                                
JRNL        AUTH   J.LIN,E.POZHARSKI,M.A.WILSON                                 
JRNL        TITL   SHORT CARBOXYLIC ACID-CARBOXYLATE HYDROGEN BONDS CAN HAVE    
JRNL        TITL 2 FULLY LOCALIZED PROTONS.                                     
JRNL        REF    BIOCHEMISTRY                  V.  56   391 2017              
JRNL        REFN                   ISSN 1520-4995                               
JRNL        PMID   27989121                                                     
JRNL        DOI    10.1021/ACS.BIOCHEM.6B00906                                  
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0151                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 37.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 88556                          
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) : 0.118                           
REMARK   3   R VALUE            (WORKING SET) : 0.118                           
REMARK   3   FREE R VALUE                     : 0.137                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2751                            
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) : 1.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.13                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 5770                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 87.55                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2870                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 174                          
REMARK   3   BIN FREE R VALUE                    : 0.3220                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1385                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 20                                      
REMARK   3   SOLVENT ATOMS            : 308                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 13.23                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.35000                                              
REMARK   3    B22 (A**2) : -0.44000                                             
REMARK   3    B33 (A**2) : 0.10000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.022         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.023         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.015         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.749         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.984                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.976                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1690 ; 0.014 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  1741 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2306 ; 1.821 ; 2.013       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  4062 ; 1.046 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   246 ; 6.327 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    62 ;42.483 ;26.129       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   324 ;11.549 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     7 ;17.445 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   266 ; 0.117 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1965 ; 0.010 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   322 ; 0.003 ; 0.020       
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):   873 ; 0.852 ; 0.932       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   872 ; 0.809 ; 0.929       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1119 ; 1.214 ; 1.411       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  1120 ; 1.229 ; 1.413       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   817 ; 1.392 ; 1.220       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):   817 ; 1.393 ; 1.220       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  1173 ; 1.572 ; 1.690       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  2198 ; 8.630 ;17.461       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  1981 ; 5.384 ;14.005       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  3431 ; 2.126 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):    42 ;49.608 ; 5.000       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  3658 ;13.182 ; 5.000       
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 : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.30                                          
REMARK   3   ION PROBE RADIUS   : 1.00                                          
REMARK   3   SHRINKAGE RADIUS   : 1.00                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 5SY9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-AUG-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000223326.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-FEB-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL9-2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.88                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : RH COATED COLLIMATING MIRROR, K    
REMARK 200                                   -B FOCUSING MIRRORS                
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 91327                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 37.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1                               
REMARK 200  DATA REDUNDANCY                : 5.100                              
REMARK 200  R MERGE                    (I) : 0.07000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.12                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 85.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.06600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.400                              
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: 1P5F                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.52                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.83                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25-28% PEG 4000, 0.1 M TRIS HCL, 0.1 M   
REMARK 280  SODIUM CITRATE, PH 8.5, VAPOR DIFFUSION, SITTING DROP,              
REMARK 280  TEMPERATURE 298K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   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       21.75600            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       21.75600            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       43.13800            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       60.98150            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       43.13800            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       60.98150            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       21.75600            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       43.13800            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       60.98150            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       21.75600            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       43.13800            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       60.98150            
REMARK 290   SMTRY3   8  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 300 THE ASSEMBLY REPRESENTED IN THIS ENTRY HAS REGULAR                   
REMARK 300 CYCLIC POINT SYMMETRY (SCHOENFLIES SYMBOL = C2).                     
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: 4600 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15440 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 16.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      -21.75600            
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     GLY A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     ASP A   189                                                      
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   526     O    HOH A   589              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   530     O    HOH A   530     3554     1.91            
REMARK 500   O    HOH A   518     O    HOH A   518     3554     1.94            
REMARK 500   CG2  THR A   140     O    HOH A   506     6445     2.14            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    LYS A  89   CD  -  CE  -  NZ  ANGL. DEV. =  27.1 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    CSD A 106     -106.22     73.19                                   
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 A 605        DISTANCE =  6.04 ANGSTROMS                       
REMARK 525    HOH A 606        DISTANCE =  6.51 ANGSTROMS                       
REMARK 525    HOH A 607        DISTANCE =  6.87 ANGSTROMS                       
REMARK 525    HOH A 608        DISTANCE =  6.91 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 204                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 205                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5SY6   RELATED DB: PDB                                   
REMARK 900 5SY6 IS WILD-TYPE DJ-1                                               
REMARK 900 RELATED ID: 5SYA   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5SY4   RELATED DB: PDB                                   
DBREF  5SY9 A    1   189  UNP    Q99497   PARK7_HUMAN      1    189             
SEQADV 5SY9 GLY A   -2  UNP  Q99497              EXPRESSION TAG                 
SEQADV 5SY9 SER A   -1  UNP  Q99497              EXPRESSION TAG                 
SEQADV 5SY9 HIS A    0  UNP  Q99497              EXPRESSION TAG                 
SEQADV 5SY9 GLN A   15  UNP  Q99497    GLU    15 ENGINEERED MUTATION            
SEQRES   1 A  192  GLY SER HIS MET ALA SER LYS ARG ALA LEU VAL ILE LEU          
SEQRES   2 A  192  ALA LYS GLY ALA GLN GLU MET GLU THR VAL ILE PRO VAL          
SEQRES   3 A  192  ASP VAL MET ARG ARG ALA GLY ILE LYS VAL THR VAL ALA          
SEQRES   4 A  192  GLY LEU ALA GLY LYS ASP PRO VAL GLN CYS SER ARG ASP          
SEQRES   5 A  192  VAL VAL ILE CYS PRO ASP ALA SER LEU GLU ASP ALA LYS          
SEQRES   6 A  192  LYS GLU GLY PRO TYR ASP VAL VAL VAL LEU PRO GLY GLY          
SEQRES   7 A  192  ASN LEU GLY ALA GLN ASN LEU SER GLU SER ALA ALA VAL          
SEQRES   8 A  192  LYS GLU ILE LEU LYS GLU GLN GLU ASN ARG LYS GLY LEU          
SEQRES   9 A  192  ILE ALA ALA ILE CSD ALA GLY PRO THR ALA LEU LEU ALA          
SEQRES  10 A  192  HIS GLU ILE GLY PHE GLY SER LYS VAL THR THR HIS PRO          
SEQRES  11 A  192  LEU ALA LYS ASP LYS MET MET ASN GLY GLY HIS TYR THR          
SEQRES  12 A  192  TYR SER GLU ASN ARG VAL GLU LYS ASP GLY LEU ILE LEU          
SEQRES  13 A  192  THR SER ARG GLY PRO GLY THR SER PHE GLU PHE ALA LEU          
SEQRES  14 A  192  ALA ILE VAL GLU ALA LEU ASN GLY LYS GLU VAL ALA ALA          
SEQRES  15 A  192  GLN VAL LYS ALA PRO LEU VAL LEU LYS ASP                      
MODRES 5SY9 CSD A  106  CYS  MODIFIED RESIDUE                                   
HET    CSD  A 106       8                                                       
HET    EDO  A 201       8                                                       
HET    EDO  A 202       8                                                       
HET    EDO  A 203       8                                                       
HET    EDO  A 204       4                                                       
HET    EDO  A 205       4                                                       
HETNAM     CSD 3-SULFINOALANINE                                                 
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     CSD S-CYSTEINESULFINIC ACID; S-SULFINOCYSTEINE                       
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   1  CSD    C3 H7 N O4 S                                                 
FORMUL   2  EDO    5(C2 H6 O2)                                                  
FORMUL   7  HOH   *308(H2 O)                                                    
HELIX    1 AA1 GLN A   15  ALA A   29  1                                  15    
HELIX    2 AA2 LEU A   58  LYS A   62  1                                   5    
HELIX    3 AA3 LYS A   63  GLY A   65  5                                   3    
HELIX    4 AA4 GLY A   75  SER A   85  1                                  11    
HELIX    5 AA5 SER A   85  ARG A   98  1                                  14    
HELIX    6 AA6 GLY A  108  HIS A  115  1                                   8    
HELIX    7 AA7 HIS A  126  LEU A  128  5                                   3    
HELIX    8 AA8 ALA A  129  ASN A  135  1                                   7    
HELIX    9 AA9 GLY A  157  GLY A  159  5                                   3    
HELIX   10 AB1 THR A  160  GLY A  174  1                                  15    
HELIX   11 AB2 GLY A  174  ALA A  183  1                                  10    
HELIX   12 AB3 PRO A  184  VAL A  186  5                                   3    
SHEET    1 AA1 7 ALA A  56  SER A  57  0                                        
SHEET    2 AA1 7 LYS A  32  GLY A  37  1  N  GLY A  37   O  ALA A  56           
SHEET    3 AA1 7 ARG A   5  LEU A  10  1  N  LEU A  10   O  ALA A  36           
SHEET    4 AA1 7 VAL A  69  LEU A  72  1  O  VAL A  71   N  LEU A   7           
SHEET    5 AA1 7 LEU A 101  ILE A 105  1  O  ALA A 103   N  LEU A  72           
SHEET    6 AA1 7 ILE A 152  SER A 155  1  O  LEU A 153   N  ILE A 102           
SHEET    7 AA1 7 VAL A 146  ASP A 149 -1  N  GLU A 147   O  THR A 154           
SHEET    1 AA2 2 VAL A  44  GLN A  45  0                                        
SHEET    2 AA2 2 VAL A  51  ILE A  52 -1  O  ILE A  52   N  VAL A  44           
SHEET    1 AA3 2 LYS A 122  VAL A 123  0                                        
SHEET    2 AA3 2 THR A 140  TYR A 141  1  O  THR A 140   N  VAL A 123           
SSBOND   1 CYS A   53    CYS A   53                          1555   3554  2.73  
LINK         C   ILE A 105                 N   CSD A 106     1555   1555  1.35  
LINK         C   CSD A 106                 N   ALA A 107     1555   1555  1.40  
CISPEP   1 GLY A   65    PRO A   66          0        16.89                     
CISPEP   2 GLY A   65    PRO A   66          0       -11.48                     
SITE     1 AC1  8 GLY A  65  PRO A  66  TYR A  67  ILE A  91                    
SITE     2 AC1  8 GLU A  94  GLN A  95  HOH A 318  HOH A 326                    
SITE     1 AC2 10 GLY A 137  HIS A 138  TYR A 139  THR A 140                    
SITE     2 AC2 10 LYS A 148  GLU A 170  ALA A 171  HOH A 310                    
SITE     3 AC2 10 HOH A 390  HOH A 491                                          
SITE     1 AC3  9 ARG A  28  CSD A 106  HIS A 126  PRO A 158                    
SITE     2 AC3  9 PRO A 184  EDO A 205  HOH A 301  HOH A 371                    
SITE     3 AC3  9 HOH A 414                                                     
SITE     1 AC4  4 GLU A 116  PHE A 119  HOH A 321  HOH A 354                    
SITE     1 AC5  3 ASN A  76  EDO A 203  HOH A 454                               
CRYST1   86.276  121.963   43.512  90.00  90.00  90.00 C 2 2 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      0.011591  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008199  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.022982        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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