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PDBsum entry 3b36

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Chaperone PDB id
3b36
Jmol
Contents
Protein chain
187 a.a.
Ligands
EDO ×8
Metals
_CL
Waters ×211
HEADER    CHAPERONE                               19-OCT-07   3B36
TITLE     STRUCTURE OF M26L DJ-1
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PROTEIN DJ-1;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: ONCOGENE DJ1, PARKINSON DISEASE PROTEIN 7;
COMPND   5 ENGINEERED: YES;
COMPND   6 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: PARK7;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS    PARKINSON'S DISEASE, PFPI, THIJ, CHAPERONE, CYTOPLASM,
KEYWDS   2 DISEASE MUTATION, NUCLEUS, ONCOGENE, OXIDATION, PARKINSON
KEYWDS   3 DISEASE, PHOSPHORYLATION, POLYMORPHISM, UBL CONJUGATION
EXPDTA    X-RAY DIFFRACTION
AUTHOR    M.LAKSHMINARASIMHAN,M.T.MALDONADO,W.ZHOU,A.L.FINK,M.A.WILSON
REVDAT   3   24-FEB-09 3B36    1       VERSN
REVDAT   2   19-FEB-08 3B36    1       JRNL
REVDAT   1   15-JAN-08 3B36    0
JRNL        AUTH   M.LAKSHMINARASIMHAN,M.T.MALDONADO,W.ZHOU,A.L.FINK,
JRNL        AUTH 2 M.A.WILSON
JRNL        TITL   STRUCTURAL IMPACT OF THREE PARKINSONISM-ASSOCIATED
JRNL        TITL 2 MISSENSE MUTATIONS ON HUMAN DJ-1.
JRNL        REF    BIOCHEMISTRY                  V.  47  1381 2008
JRNL        REFN                   ISSN 0006-2960
JRNL        PMID   18181649
JRNL        DOI    10.1021/BI701189C
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    1.50 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 64.82
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9
REMARK   3   NUMBER OF REFLECTIONS             : 37433
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) : 0.166
REMARK   3   R VALUE            (WORKING SET) : 0.166
REMARK   3   FREE R VALUE                     : 0.175
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1976
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) : 1.50
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.54
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2723
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.93
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2530
REMARK   3   BIN FREE R VALUE SET COUNT          : 135
REMARK   3   BIN FREE R VALUE                    : 0.2660
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 1468
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 33
REMARK   3   SOLVENT ATOMS            : 211
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 13.11
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.14000
REMARK   3    B22 (A**2) : 0.14000
REMARK   3    B33 (A**2) : -0.20000
REMARK   3    B12 (A**2) : 0.07000
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): 0.060
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.057
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.030
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.766
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.963
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.959
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1519 ; 0.007 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2048 ; 1.165 ; 2.009
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   207 ; 5.630 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    52 ;36.425 ;25.192
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   281 ;10.745 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     8 ;16.895 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   238 ; 0.072 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1111 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   782 ; 0.208 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1055 ; 0.303 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   161 ; 0.126 ; 0.200
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):    67 ; 0.208 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    23 ; 0.102 ; 0.200
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):  1025 ; 0.631 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1598 ; 0.904 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   542 ; 1.609 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   450 ; 2.613 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.40
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 3B36 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-DEC-07.
REMARK 100 THE RCSB ID CODE IS RCSB045020.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 10-SEP-07
REMARK 200  TEMPERATURE           (KELVIN) : 110.0
REMARK 200  PH                             : 7.50
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU MICROMAX-007
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.542
REMARK 200  MONOCHROMATOR                  : OSMIC BLUE CONFOCAL MIRRORS
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV++
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 39440
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.500
REMARK 200  RESOLUTION RANGE LOW       (A) : 64.820
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9
REMARK 200  DATA REDUNDANCY                : 9.800
REMARK 200  R MERGE                    (I) : 0.06900
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 36.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.55
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9
REMARK 200  DATA REDUNDANCY IN SHELL       : 8.90
REMARK 200  R MERGE FOR SHELL          (I) : 0.16000
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 13.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 1P5F
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 59.18
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.01
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 3000, 100 MM HEPES, 200 MM
REMARK 280  NACL, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K,
REMARK 280  PH 7.50
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       25.08800
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       50.17600
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       50.17600
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       25.08800
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5290 ANGSTROM**2
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       25.08800
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     GLY A    -2
REMARK 465     SER A    -1
REMARK 465     HIS A     0
REMARK 465     MET A     1
REMARK 465     ASP A   189
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     -112.06     73.70
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 CL A 190
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 191
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 192
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 193
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 194
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 195
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 196
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 197
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 198
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2RK3   RELATED DB: PDB
REMARK 900 STRUCTURE OF A104T DJ-1
REMARK 900 RELATED ID: 2RK4   RELATED DB: PDB
REMARK 900 STRUCTURE OF M26I DJ-1
REMARK 900 RELATED ID: 2RK6   RELATED DB: PDB
REMARK 900 STRUCTURE OF E163K DJ-1
DBREF  3B36 A    1   189  UNP    Q99497   PARK7_HUMAN      1    189
SEQADV 3B36 GLY A   -2  UNP  Q99497              EXPRESSION TAG
SEQADV 3B36 SER A   -1  UNP  Q99497              EXPRESSION TAG
SEQADV 3B36 HIS A    0  UNP  Q99497              EXPRESSION TAG
SEQADV 3B36 LEU A   26  UNP  Q99497    MET    26 ENGINEERED
SEQRES   1 A  192  GLY SER HIS MET ALA SER LYS ARG ALA LEU VAL ILE LEU
SEQRES   2 A  192  ALA LYS GLY ALA GLU GLU MET GLU THR VAL ILE PRO VAL
SEQRES   3 A  192  ASP VAL LEU ARG ARG ALA GLY ILE LYS VAL THR VAL ALA
SEQRES   4 A  192  GLY LEU ALA GLY LYS ASP PRO VAL GLN CYS SER ARG ASP
SEQRES   5 A  192  VAL VAL ILE CYS PRO ASP ALA SER LEU GLU ASP ALA LYS
SEQRES   6 A  192  LYS GLU GLY PRO TYR ASP VAL VAL VAL LEU PRO GLY GLY
SEQRES   7 A  192  ASN LEU GLY ALA GLN ASN LEU SER GLU SER ALA ALA VAL
SEQRES   8 A  192  LYS GLU ILE LEU LYS GLU GLN GLU ASN ARG LYS GLY LEU
SEQRES   9 A  192  ILE ALA ALA ILE CYS ALA GLY PRO THR ALA LEU LEU ALA
SEQRES  10 A  192  HIS GLU ILE GLY PHE GLY SER LYS VAL THR THR HIS PRO
SEQRES  11 A  192  LEU ALA LYS ASP LYS MET MET ASN GLY GLY HIS TYR THR
SEQRES  12 A  192  TYR SER GLU ASN ARG VAL GLU LYS ASP GLY LEU ILE LEU
SEQRES  13 A  192  THR SER ARG GLY PRO GLY THR SER PHE GLU PHE ALA LEU
SEQRES  14 A  192  ALA ILE VAL GLU ALA LEU ASN GLY LYS GLU VAL ALA ALA
SEQRES  15 A  192  GLN VAL LYS ALA PRO LEU VAL LEU LYS ASP
HET     CL  A 190       1
HET    EDO  A 191       4
HET    EDO  A 192       4
HET    EDO  A 193       4
HET    EDO  A 194       4
HET    EDO  A 195       4
HET    EDO  A 196       4
HET    EDO  A 197       4
HET    EDO  A 198       4
HETNAM      CL CHLORIDE ION
HETNAM     EDO 1,2-ETHANEDIOL
HETSYN     EDO ETHYLENE GLYCOL
FORMUL   2   CL    CL 1-
FORMUL   3  EDO    8(C2 H6 O2)
FORMUL  11  HOH   *211(H2 O)
HELIX    1   1 GLU A   15  ALA A   29  1                                  15
HELIX    2   2 LEU A   58  LYS A   62  1                                   5
HELIX    3   3 LYS A   63  GLY A   65  5                                   3
HELIX    4   4 GLY A   75  SER A   85  1                                  11
HELIX    5   5 SER A   85  ARG A   98  1                                  14
HELIX    6   6 PRO A  109  HIS A  115  1                                   7
HELIX    7   7 HIS A  126  LEU A  128  5                                   3
HELIX    8   8 ALA A  129  MET A  134  1                                   6
HELIX    9   9 GLY A  157  GLY A  159  5                                   3
HELIX   10  10 THR A  160  GLY A  174  1                                  15
HELIX   11  11 GLY A  174  ALA A  183  1                                  10
HELIX   12  12 PRO A  184  VAL A  186  5                                   3
SHEET    1   A 7 ALA A  56  SER A  57  0
SHEET    2   A 7 LYS A  32  GLY A  37  1  N  GLY A  37   O  ALA A  56
SHEET    3   A 7 ARG A   5  LEU A  10  1  N  LEU A  10   O  ALA A  36
SHEET    4   A 7 VAL A  69  LEU A  72  1  O  VAL A  71   N  LEU A   7
SHEET    5   A 7 LEU A 101  ILE A 105  1  O  ALA A 103   N  LEU A  72
SHEET    6   A 7 ILE A 152  SER A 155  1  O  LEU A 153   N  ILE A 102
SHEET    7   A 7 VAL A 146  ASP A 149 -1  N  GLU A 147   O  THR A 154
SHEET    1   B 2 VAL A  44  GLN A  45  0
SHEET    2   B 2 VAL A  51  ILE A  52 -1  O  ILE A  52   N  VAL A  44
SHEET    1   C 2 LYS A 122  VAL A 123  0
SHEET    2   C 2 THR A 140  TYR A 141  1  O  THR A 140   N  VAL A 123
CISPEP   1 GLY A   65    PRO A   66          0         0.30
SITE     1 AC1  5 ARG A  48  GLY A  75  ASN A  76  GLY A 120
SITE     2 AC1  5 EDO A 194
SITE     1 AC2  9 ASN A  76  ALA A 107  HIS A 126  LEU A 128
SITE     2 AC2  9 EDO A 194  EDO A 195  HOH A 226  HOH A 314
SITE     3 AC2  9 HOH A 373
SITE     1 AC3  8 LYS A  12  GLN A  45  LYS A 122  GLU A 147
SITE     2 AC3  8 LYS A 148  ASP A 149  EDO A 197  HOH A 377
SITE     1 AC4  9 LEU A 166  ALA A 178  ALA A 179  LYS A 182
SITE     2 AC4  9 HOH A 251  HOH A 308  HOH A 313  HOH A 346
SITE     3 AC4  9 HOH A 357
SITE     1 AC5  7 GLU A  15  ARG A  28  HIS A 126  PRO A 184
SITE     2 AC5  7  CL A 190  EDO A 191  HOH A 226
SITE     1 AC6  6 ASN A  76  LYS A 132  EDO A 191  HOH A 240
SITE     2 AC6  6 HOH A 373  HOH A 382
SITE     1 AC7  5 PRO A  66  TYR A  67  GLU A  94  GLN A  95
SITE     2 AC7  5 HOH A 341
SITE     1 AC8  6 GLN A  45  ASP A  49  SER A 142  ASN A 144
SITE     2 AC8  6 GLU A 147  EDO A 192
SITE     1 AC9  5 GLN A  80  GLU A  96  LYS A 132  HOH A 368
SITE     2 AC9  5 HOH A 382
CRYST1   74.818   74.818   75.264  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      0.013366  0.007717  0.000000        0.00000
SCALE2      0.000000  0.015433  0.000000        0.00000
SCALE3      0.000000  0.000000  0.013287        0.00000
      
PROCHECK
Go to PROCHECK summary
 References