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