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Database: PDB
Entry: 4BTE
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Original site: 4BTE 
HEADER    HYDROLASE                               14-JUN-13   4BTE              
TITLE     DJ-1 CU(I) COMPLEX                                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN DJ-1;                                              
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: DJ-1, ONCOGENE DJ1, PARKINSON DISEASE PROTEIN 7;            
COMPND   5 EC: 3.4.-.-;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_VECTOR: PET28A                                     
KEYWDS    HYDROLASE, COPPER CHAPERONE, PARKINSON'S DISEASE, SUPEROXIDE          
KEYWDS   2 DISMUTASE ACTIVATION, MULTI-FUNCTIONAL                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.R.A.PUNO,M.ODELL,P.C.E.MOODY                                        
REVDAT   2   25-DEC-13 4BTE    1       JRNL                                     
REVDAT   1   06-NOV-13 4BTE    0                                                
JRNL        AUTH   M.R.PUNO,N.A.PATEL,S.G.MOLLER,C.V.ROBINSON,P.C.E.MOODY,      
JRNL        AUTH 2 M.ODELL                                                      
JRNL        TITL   STRUCTURE OF CU(I)-BOUND DJ-1 REVEALS A BISCYSTEINATE METAL  
JRNL        TITL 2 BINDING SITE AT THE HOMODIMER INTERFACE: INSIGHTS INTO       
JRNL        TITL 3 MUTATIONAL INACTIVATION OF DJ-1 IN PARKINSONISM.             
JRNL        REF    J.AM.CHEM.SOC.                V. 135 15974 2013              
JRNL        REFN                   ISSN 0002-7863                               
JRNL        PMID   24144264                                                     
JRNL        DOI    10.1021/JA406010M                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.38 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0029                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,                      
REMARK   3                 STEINER,NICHOLLS,WINN,LONG,VAGIN                     
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.38                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 26.64                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 89.60                          
REMARK   3   NUMBER OF REFLECTIONS             : 43643                          
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) : 0.11996                         
REMARK   3   R VALUE            (WORKING SET) : 0.11841                         
REMARK   3   FREE R VALUE                     : 0.14981                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.1                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 2343                            
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) : 1.378                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.414                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 818                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 22.91                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.278                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 47                           
REMARK   3   BIN FREE R VALUE                    : 0.420                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1391                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 1                                       
REMARK   3   SOLVENT ATOMS            : 218                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 17.955                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.11                                                 
REMARK   3    B22 (A**2) : 0.11                                                 
REMARK   3    B33 (A**2) : -0.36                                                
REMARK   3    B12 (A**2) : 0.11                                                 
REMARK   3    B13 (A**2) : 0.00                                                 
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.040         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.042         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.021         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.127         
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.980                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.971                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1412 ; 0.025 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  1437 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1911 ; 2.183 ; 1.996       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  3321 ; 1.044 ; 3.001       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   192 ; 6.044 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    51 ;33.136 ;25.490       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   258 ;15.107 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     7 ;18.439 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   228 ; 0.148 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1594 ; 0.010 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   271 ; 0.001 ; 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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ANISOTROPIC THERMAL FACTOR RESTRAINTS.   COUNT   RMS    WEIGHT      
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2848 ; 6.706 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):    92 ;55.546 ; 5.000       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  2955 ;13.341 ; 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 : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
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          
REMARK   3   RIDING POSITIONS.  U VALUES HAVE BEEN REFINED INDIVIDUALLY         
REMARK   4                                                                      
REMARK   4 4BTE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-JUN-13.                  
REMARK 100 THE PDBE ID CODE IS EBI-57306.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-JUL-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I03                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.3772                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL (PILATUS)                    
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS                            
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 46017                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.38                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 26.20                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 89.5                               
REMARK 200  DATA REDUNDANCY                : 28.9                               
REMARK 200  R MERGE                    (I) : 0.08                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 34.80                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.38                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.40                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 15.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.8                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.44                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.10                               
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 1PDV                                       
REMARK 200                                                                      
REMARK 200 REMARK: CU ANOMALOUS OPTIMISED                                       
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.14                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       25.11800            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       50.23600            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  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        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       50.23600            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       25.11800            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2890 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14900 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.8 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      -25.11800            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375 CU   CU1 A1189   LIES ON A SPECIAL POSITION.                         
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 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   NH2  ARG A     5     O    GLU A    64              2.20            
REMARK 500   SG   CYS A   106     O    HOH A  2100              1.96            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU A  96   CD    GLU A  96   OE1     0.109                       
REMARK 500    GLU A 176   CG    GLU A 176   CD      0.107                       
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    ARG A   5   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    ARG A 145   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 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     -102.81     74.03                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CU1 A1189  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  53   SG                                                     
REMARK 620 2 CYS A  53   SG  154.4                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 A1189                 
DBREF  4BTE A    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                                  
HET    CU1  A1189       1                                                       
HETNAM     CU1 COPPER (I) ION                                                   
FORMUL   2  CU1    CU 1+                                                        
FORMUL   3  HOH   *218(H2 O)                                                    
HELIX    1   1 GLU A   15  ALA A   29  1                                  15    
HELIX    2   2 LEU A   58  LYS A   63  1                                   6    
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  MET A  134  1                                   6    
HELIX    8   8 GLY A  157  GLY A  159  5                                   3    
HELIX    9   9 THR A  160  GLY A  174  1                                  15    
HELIX   10  10 GLY A  174  ALA A  183  1                                  10    
HELIX   11  11 PRO A  184  VAL A  186  5                                   3    
SHEET    1  AA 7 ALA A  56  SER A  57  0                                        
SHEET    2  AA 7 LYS A  32  GLY A  37  1  N  GLY A  37   O  ALA A  56           
SHEET    3  AA 7 ARG A   5  LEU A  10  1  O  ALA A   6   N  THR A  34           
SHEET    4  AA 7 VAL A  69  LEU A  72  1  O  VAL A  69   N  LEU A   7           
SHEET    5  AA 7 LEU A 101  ILE A 105  1  O  LEU A 101   N  VAL A  70           
SHEET    6  AA 7 ILE A 152  SER A 155  1  O  LEU A 153   N  ALA A 104           
SHEET    7  AA 7 VAL A 146  ASP A 149 -1  O  GLU A 147   N  THR A 154           
SHEET    1  AB 2 VAL A  44  GLN A  45  0                                        
SHEET    2  AB 2 VAL A  51  ILE A  52 -1  O  ILE A  52   N  VAL A  44           
SHEET    1  AC 2 LYS A 122  VAL A 123  0                                        
SHEET    2  AC 2 THR A 140  TYR A 141  1  O  THR A 140   N  VAL A 123           
LINK        CU   CU1 A1189                 SG  CYS A  53     1555   1555  1.92  
LINK        CU   CU1 A1189                 SG  CYS A  53     1555   5554  1.84  
CISPEP   1 GLY A   65    PRO A   66          0         3.00                     
SITE     1 AC1  1 CYS A  53                                                     
CRYST1   75.257   75.257   75.354  90.00  90.00 120.00 P 31 2 1      6          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.013288  0.007672  0.000000        0.00000                         
SCALE2      0.000000  0.015343  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013271        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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