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Database: PDB
Entry: 4ZGG
LinkDB: 4ZGG
Original site: 4ZGG 
HEADER    CHAPERONE                               22-APR-15   4ZGG              
TITLE     CRYSTAL STRUCTURE OF A DJ-1 (PARK7) FROM HOMO SAPIENS AT 1.23 A       
TITLE    2 RESOLUTION                                                           
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                                                      
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 EXPRESSION_SYSTEM_STRAIN: PB1;                                       
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: SPEEDET                                   
KEYWDS    PARKINSON DISEASE, STRUCTURAL GENOMICS, JOINT CENTER FOR STRUCTURAL   
KEYWDS   2 GENOMICS, JCSG, PROTEIN STRUCTURE INITIATIVE, PARTNERSHIP FOR        
KEYWDS   3 NUCLEAR RECEPTOR SIGNALING CODE BIOLOGY, NHRS, PARTNERSHIP FOR T-    
KEYWDS   4 CELL BIOLOGY, TCELL, PSI-BIOLOGY, CHAPERONE                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG),PARTNERSHIP FOR NUCLEAR   
AUTHOR   2 RECEPTOR SIGNALING CODE BIOLOGY (NHRS),PARTNERSHIP FOR T-CELL        
AUTHOR   3 BIOLOGY (TCELL)                                                      
REVDAT   4   01-FEB-23 4ZGG    1       REMARK SEQADV                            
REVDAT   3   22-NOV-17 4ZGG    1       SOURCE AUTHOR REMARK                     
REVDAT   2   27-MAY-15 4ZGG    1       KEYWDS AUTHOR JRNL                       
REVDAT   1   20-MAY-15 4ZGG    0                                                
JRNL        AUTH   JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG),                 
JRNL        AUTH 2 PARTNERSHIP FOR NUCLEAR RECEPTOR SIGNALING CODE BIOLOGY      
JRNL        AUTH 3 (NHRS),PARTNERSHIP FOR T-CELL BIOLOGY (TCELL)                
JRNL        TITL   CRYSTAL STRUCTURE OF A DJ-1 (PARK7) FROM HOMO SAPIENS AT     
JRNL        TITL 2 1.23 A RESOLUTION                                            
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.23 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0103                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES                
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.23                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.80                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 69700                          
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) : 0.117                           
REMARK   3   R VALUE            (WORKING SET) : 0.116                           
REMARK   3   FREE R VALUE                     : 0.134                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3374                            
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) : 1.23                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.26                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4272                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 85.71                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2870                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 192                          
REMARK   3   BIN FREE R VALUE                    : 0.2930                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1396                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 40                                      
REMARK   3   SOLVENT ATOMS            : 198                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 17.44                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.20000                                              
REMARK   3    B22 (A**2) : 0.20000                                              
REMARK   3    B33 (A**2) : -0.64000                                             
REMARK   3    B12 (A**2) : 0.10000                                              
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): 0.027         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.027         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.017         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.931         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.982                         
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):  1557 ; 0.016 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  1631 ; 0.003 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2100 ; 1.697 ; 2.009       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  3785 ; 1.091 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   219 ; 6.157 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    55 ;36.157 ;25.455       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   298 ;11.474 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     8 ;19.353 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   246 ; 0.104 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1745 ; 0.009 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   297 ; 0.004 ; 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):   801 ; 2.064 ; 2.409       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   800 ; 1.992 ; 2.402       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1009 ; 2.034 ; 4.542       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  3187 ; 2.717 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   129 ;30.129 ; 5.000       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  3237 ; 8.773 ; 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: 1. A MET-INHIBITION PROTOCOL WAS USED     
REMARK   3  FOR SELENOMETHIONINE INCORPORATION DURING PROTEIN EXPRESSION.       
REMARK   3  THE OCCUPANCY OF THE SE ATOMS IN THE MSE RESIDUES WAS REDUCED TO    
REMARK   3  0.75 FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL S-MET          
REMARK   3  INCORPORATION. 2. THE SAD PHASES WERE USED AS RESTRAINTS DURING     
REMARK   3  REFINEMENT. 3. HYDROGENS HAVE BEEN ADDED IN THE RIDING              
REMARK   3  POSITIONS. 4. EDO MODELED WAS PRESENT IN CRYO CONDITION.            
REMARK   4                                                                      
REMARK   4 4ZGG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-APR-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000209222.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-DEC-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL14-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL SI(111)             
REMARK 200  OPTICS                         : VERTICAL FOCUSING MIRROR; DOUBLE   
REMARK 200                                   CRYSTAL SI(111) MONOCHROMATOR      
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 325 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA 3.3.20                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 69760                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.230                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.796                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.3                               
REMARK 200  DATA REDUNDANCY                : 6.900                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.11500                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.1000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.23                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.26                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 86.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.80400                            
REMARK 200  R SYM FOR SHELL            (I) : 0.80400                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.13                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.01                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 5.00% POLYETHYLENE GLYCOL 6000, 0.1M     
REMARK 280  TRIS PH 8.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K        
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       24.96567            
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       49.93133            
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       49.93133            
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       24.96567            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: MONOMERIC                         
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                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6200 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15820 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 30.0 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 -0.500000  0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.866025  0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
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  59   CD    GLU A  59   OE2    -0.106                       
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     -102.14     76.74                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 206                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 207                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 208                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 209                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 210                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: JCSG-399795   RELATED DB: TARGETTRACK                    
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE CONSTRUCT WAS EXPRESSED WITH A PURIFICATION TAG                  
REMARK 999 MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV PROTEASE LEAVING   
REMARK 999 ONLY A GLYCINE (0) FOLLOWED BY THE TARGET SEQUENCE.                  
DBREF  4ZGG A    1   189  UNP    Q99497   PARK7_HUMAN      1    189             
SEQADV 4ZGG GLY A    0  UNP  Q99497              EXPRESSION TAG                 
SEQRES   1 A  190  GLY MSE ALA SER LYS ARG ALA LEU VAL ILE LEU ALA LYS          
SEQRES   2 A  190  GLY ALA GLU GLU MSE GLU THR VAL ILE PRO VAL ASP VAL          
SEQRES   3 A  190  MSE ARG ARG ALA GLY ILE LYS VAL THR VAL ALA GLY LEU          
SEQRES   4 A  190  ALA GLY LYS ASP PRO VAL GLN CYS SER ARG ASP VAL VAL          
SEQRES   5 A  190  ILE CYS PRO ASP ALA SER LEU GLU ASP ALA LYS LYS GLU          
SEQRES   6 A  190  GLY PRO TYR ASP VAL VAL VAL LEU PRO GLY GLY ASN LEU          
SEQRES   7 A  190  GLY ALA GLN ASN LEU SER GLU SER ALA ALA VAL LYS GLU          
SEQRES   8 A  190  ILE LEU LYS GLU GLN GLU ASN ARG LYS GLY LEU ILE ALA          
SEQRES   9 A  190  ALA ILE CYS ALA GLY PRO THR ALA LEU LEU ALA HIS GLU          
SEQRES  10 A  190  ILE GLY PHE GLY SER LYS VAL THR THR HIS PRO LEU ALA          
SEQRES  11 A  190  LYS ASP LYS MSE MSE ASN GLY GLY HIS TYR THR TYR SER          
SEQRES  12 A  190  GLU ASN ARG VAL GLU LYS ASP GLY LEU ILE LEU THR SER          
SEQRES  13 A  190  ARG GLY PRO GLY THR SER PHE GLU PHE ALA LEU ALA ILE          
SEQRES  14 A  190  VAL GLU ALA LEU ASN GLY LYS GLU VAL ALA ALA GLN VAL          
SEQRES  15 A  190  LYS ALA PRO LEU VAL LEU LYS ASP                              
MODRES 4ZGG MSE A    1  MET  MODIFIED RESIDUE                                   
MODRES 4ZGG MSE A   17  MET  MODIFIED RESIDUE                                   
MODRES 4ZGG MSE A   26  MET  MODIFIED RESIDUE                                   
MODRES 4ZGG MSE A  133  MET  MODIFIED RESIDUE                                   
MODRES 4ZGG MSE A  134  MET  MODIFIED RESIDUE                                   
HET    MSE  A   1       8                                                       
HET    MSE  A  17       8                                                       
HET    MSE  A  26       8                                                       
HET    MSE  A 133       8                                                       
HET    MSE  A 134       8                                                       
HET    EDO  A 201       4                                                       
HET    EDO  A 202       4                                                       
HET    EDO  A 203       4                                                       
HET    EDO  A 204       4                                                       
HET    EDO  A 205       4                                                       
HET    EDO  A 206       4                                                       
HET    EDO  A 207       4                                                       
HET    EDO  A 208       4                                                       
HET    EDO  A 209       4                                                       
HET    EDO  A 210       4                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   1  MSE    5(C5 H11 N O2 SE)                                            
FORMUL   2  EDO    10(C2 H6 O2)                                                 
FORMUL  12  HOH   *198(H2 O)                                                    
HELIX    1 AA1 GLU 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 PRO A  109  HIS A  115  1                                   7    
HELIX    7 AA7 HIS A  126  LEU A  128  5                                   3    
HELIX    8 AA8 ALA A  129  MSE A  134  1                                   6    
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  VAL A   8   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  VAL A  70           
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           
LINK         C   GLY A   0                 N   MSE A   1     1555   1555  1.34  
LINK         C   MSE A   1                 N  AALA A   2     1555   1555  1.33  
LINK         C   MSE A   1                 N  BALA A   2     1555   1555  1.34  
LINK         C   GLU A  16                 N   MSE A  17     1555   1555  1.32  
LINK         C   MSE A  17                 N   GLU A  18     1555   1555  1.33  
LINK         C   VAL A  25                 N   MSE A  26     1555   1555  1.34  
LINK         C   MSE A  26                 N   ARG A  27     1555   1555  1.32  
LINK         C   LYS A 132                 N   MSE A 133     1555   1555  1.33  
LINK         C   MSE A 133                 N   MSE A 134     1555   1555  1.34  
LINK         C   MSE A 134                 N   ASN A 135     1555   1555  1.33  
CISPEP   1 GLY A   65    PRO A   66          0         4.06                     
SITE     1 AC1  7 LYS A  12  GLN A  45  LYS A 122  GLU A 147                    
SITE     2 AC1  7 LYS A 148  ASP A 149  HOH A 316                               
SITE     1 AC2  3 ASN A  76  HOH A 382  HOH A 497                               
SITE     1 AC3  6 ARG A  28  HIS A 126  PRO A 158  PRO A 184                    
SITE     2 AC3  6 HOH A 313  HOH A 382                                          
SITE     1 AC4  6 PRO A  66  TYR A  67  GLU A  94  GLN A  95                    
SITE     2 AC4  6 HOH A 311  HOH A 314                                          
SITE     1 AC5  4 GLN A  80  ASN A  81  GLU A  84  LYS A  99                    
SITE     1 AC6  4 GLN A  80  GLU A  96  LYS A 132  HOH A 490                    
SITE     1 AC7  6 LYS A 175  ALA A 178  ALA A 179  HOH A 312                    
SITE     2 AC7  6 HOH A 335  HOH A 479                                          
SITE     1 AC8  3 LYS A 175  GLU A 176  ALA A 179                               
SITE     1 AC9  3 CYS A  53  PRO A  54  ASP A  55                               
SITE     1 AD1  4 VAL A  33  THR A  34  HOH A 360  HOH A 378                    
CRYST1   75.002   75.002   74.897  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      0.013333  0.007698  0.000000        0.00000                         
SCALE2      0.000000  0.015396  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013352        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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