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PDBsum entry 2or3

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Top Page protein ligands Protein-protein interface(s) links
Chaperone PDB id
2or3
Jmol
Contents
Protein chain
187 a.a.
Ligands
SO4 ×2
Waters ×583
HEADER    CHAPERONE                               01-FEB-07   2OR3
TITLE     PRE-OXIDATION COMPLEX OF HUMAN DJ-1
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PROTEIN DJ-1;
COMPND   3 CHAIN: A, B;
COMPND   4 SYNONYM: ONCOGENE DJ1;
COMPND   5 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 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    CYSTEINE OXIDATION, NUCLEOPHILE ELBOW, CHAPERONE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    A.C.WITT,M.LAKSHMINARASIMHAN,M.A.WILSON
REVDAT   4   22-JUL-08 2OR3    1       JRNL
REVDAT   3   08-JUL-08 2OR3    1       JRNL
REVDAT   2   01-JUL-08 2OR3    1       JRNL   VERSN
REVDAT   1   13-FEB-07 2OR3    0
JRNL        AUTH   A.C.WITT,M.LAKSHMINARASIMHAN,B.C.REMINGTON,S.HASIM,
JRNL        AUTH 2 E.POZHARSKI,M.A.WILSON
JRNL        TITL   CYSTEINE PKA DEPRESSION BY A PROTONATED GLUTAMIC
JRNL        TITL 2 ACID IN HUMAN DJ-1.
JRNL        REF    BIOCHEMISTRY                  V.  47  7430 2008
JRNL        REFN                   ISSN 0006-2960
JRNL        PMID   18570440
JRNL        DOI    10.1021/BI800282D
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    1.20 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : SHELXL-97
REMARK   3   AUTHORS     : G.M.SHELDRICK
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.20
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 22.45
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.8
REMARK   3   CROSS-VALIDATION METHOD           : FREE R
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.136
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.182
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 5761
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 114654
REMARK   3
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : NULL
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : 0.109
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : 0.154
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : 4273
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : 86103
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS      : 2955
REMARK   3   NUCLEIC ACID ATOMS : 0
REMARK   3   HETEROGEN ATOMS    : 10
REMARK   3   SOLVENT ATOMS      : 583
REMARK   3
REMARK   3  MODEL REFINEMENT.
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : 3302.50
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : 2794.00
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : 24
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : 31968
REMARK   3   NUMBER OF RESTRAINTS                     : 40468
REMARK   3
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK   3   BOND LENGTHS                         (A) : 0.013
REMARK   3   ANGLE DISTANCES                      (A) : 0.031
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : 0.030
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : 0.069
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.077
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : 0.019
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : 0.004
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : 0.051
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : 0.115
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED: NULL
REMARK   3
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH & HUBER
REMARK   3   SPECIAL CASE: NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: AUTHORS STATE THAT THERE WERE SLIGHT
REMARK   3  MODEL CHANGES AFTER COMBINING THE TEST AND WORKING SET, SO THE
REMARK   3  FINAL R FACTOR IS LOWER THAN THE WORKING R FACTOR.
REMARK   4
REMARK   4 2OR3 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-FEB-07.
REMARK 100 THE RCSB ID CODE IS RCSB041482.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 12-MAR-06
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 6.0
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : APS
REMARK 200  BEAMLINE                       : 14-BM-C
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9
REMARK 200  MONOCHROMATOR                  : BENT GE(111)
REMARK 200  OPTICS                         : BENT CONICAL SI MIRROR
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 114729
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.200
REMARK 200  RESOLUTION RANGE LOW       (A) : 22.450
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.8
REMARK 200  DATA REDUNDANCY                : 5.300
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.06500
REMARK 200   FOR THE DATA SET  : 24.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.20
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.24
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.20
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.70200
REMARK 200   FOR SHELL         : 2.040
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 1P5F
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 47.32
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 28% PEG 4000, 200 MM AMMONIUM
REMARK 280  SULFATE, 50 MM SODIUM ACETATE, 2.5 MM EPIGALLOCATECHIN 3-
REMARK 280  GALLATE, PH 6.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280  298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X+1/2,-Y,Z+1/2
REMARK 290       3555   -X,Y+1/2,-Z+1/2
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       21.95700
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       49.41450
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       42.88300
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       49.41450
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       21.95700
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       42.88300
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 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: 3220 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14770 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -50.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 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 465     MET B     1
REMARK 465     ASP B   189
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   NH1 -  CZ  -  NH2 ANGL. DEV. =   7.5 DEGREES
REMARK 500    ARG A   5   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.9 DEGREES
REMARK 500    ARG A  48   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.0 DEGREES
REMARK 500    LYS A  89   CD  -  CE  -  NZ  ANGL. DEV. =  16.6 DEGREES
REMARK 500    ASP A 131   CB  -  CG  -  OD2 ANGL. DEV. =  -5.9 DEGREES
REMARK 500    GLU A 143   OE1 -  CD  -  OE2 ANGL. DEV. =  15.5 DEGREES
REMARK 500    ARG A 145   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES
REMARK 500    LYS A 188   CA  -  CB  -  CG  ANGL. DEV. =  18.4 DEGREES
REMARK 500    GLU B  94   OE1 -  CD  -  OE2 ANGL. DEV. =  -7.3 DEGREES
REMARK 500    GLU B  96   OE1 -  CD  -  OE2 ANGL. DEV. =   8.0 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     -107.43     72.50
REMARK 500    CYS B 106     -106.42     72.03
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH B 645        DISTANCE =  7.24 ANGSTROMS
REMARK 525    HOH A 797        DISTANCE =  5.91 ANGSTROMS
REMARK 525    HOH A 830        DISTANCE =  6.76 ANGSTROMS
REMARK 525    HOH B 837        DISTANCE =  6.72 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 600
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 601
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1P5F   RELATED DB: PDB
REMARK 900 RELATED ID: 1SOA   RELATED DB: PDB
DBREF  2OR3 A    1   189  UNP    Q99497   PARK7_HUMAN      1    189
DBREF  2OR3 B    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
SEQRES   1 B  189  MET ALA SER LYS ARG ALA LEU VAL ILE LEU ALA LYS GLY
SEQRES   2 B  189  ALA GLU GLU MET GLU THR VAL ILE PRO VAL ASP VAL MET
SEQRES   3 B  189  ARG ARG ALA GLY ILE LYS VAL THR VAL ALA GLY LEU ALA
SEQRES   4 B  189  GLY LYS ASP PRO VAL GLN CYS SER ARG ASP VAL VAL ILE
SEQRES   5 B  189  CYS PRO ASP ALA SER LEU GLU ASP ALA LYS LYS GLU GLY
SEQRES   6 B  189  PRO TYR ASP VAL VAL VAL LEU PRO GLY GLY ASN LEU GLY
SEQRES   7 B  189  ALA GLN ASN LEU SER GLU SER ALA ALA VAL LYS GLU ILE
SEQRES   8 B  189  LEU LYS GLU GLN GLU ASN ARG LYS GLY LEU ILE ALA ALA
SEQRES   9 B  189  ILE CYS ALA GLY PRO THR ALA LEU LEU ALA HIS GLU ILE
SEQRES  10 B  189  GLY PHE GLY SER LYS VAL THR THR HIS PRO LEU ALA LYS
SEQRES  11 B  189  ASP LYS MET MET ASN GLY GLY HIS TYR THR TYR SER GLU
SEQRES  12 B  189  ASN ARG VAL GLU LYS ASP GLY LEU ILE LEU THR SER ARG
SEQRES  13 B  189  GLY PRO GLY THR SER PHE GLU PHE ALA LEU ALA ILE VAL
SEQRES  14 B  189  GLU ALA LEU ASN GLY LYS GLU VAL ALA ALA GLN VAL LYS
SEQRES  15 B  189  ALA PRO LEU VAL LEU LYS ASP
HET    SO4  A 600       5
HET    SO4  B 601       5
HETNAM     SO4 SULFATE ION
FORMUL   3  SO4    2(O4 S 2-)
FORMUL   5  HOH   *583(H2 O)
HELIX    1   1 GLU A   15  ALA A   29  1                                  15
HELIX    2   2 LEU A   58  GLU A   64  1                                   7
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  ASN A  135  1                                   7
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
HELIX   12  12 GLU B   15  ALA B   29  1                                  15
HELIX   13  13 LEU B   58  GLU B   64  1                                   7
HELIX   14  14 GLY B   75  GLU B   84  1                                  10
HELIX   15  15 SER B   85  ARG B   98  1                                  14
HELIX   16  16 PRO B  109  HIS B  115  1                                   7
HELIX   17  17 HIS B  126  LEU B  128  5                                   3
HELIX   18  18 ALA B  129  ASN B  135  1                                   7
HELIX   19  19 GLY B  157  GLY B  159  5                                   3
HELIX   20  20 THR B  160  GLY B  174  1                                  15
HELIX   21  21 GLY B  174  ALA B  183  1                                  10
HELIX   22  22 PRO B  184  VAL B  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  ALA A   6   O  THR A  34
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  VAL A  70
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 4 VAL A  44  GLN A  45  0
SHEET    2   B 4 VAL A  51  CYS A  53 -1  O  ILE A  52   N  VAL A  44
SHEET    3   B 4 VAL B  51  ILE B  52 -1  O  VAL B  51   N  CYS A  53
SHEET    4   B 4 VAL B  44  GLN B  45 -1  N  VAL B  44   O  ILE B  52
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
SHEET    1   D 7 ALA B  56  SER B  57  0
SHEET    2   D 7 LYS B  32  GLY B  37  1  N  GLY B  37   O  ALA B  56
SHEET    3   D 7 ARG B   5  LEU B  10  1  N  LEU B  10   O  ALA B  36
SHEET    4   D 7 VAL B  69  LEU B  72  1  O  VAL B  71   N  LEU B   7
SHEET    5   D 7 LEU B 101  ILE B 105  1  O  ALA B 103   N  VAL B  70
SHEET    6   D 7 ILE B 152  SER B 155  1  O  LEU B 153   N  ILE B 102
SHEET    7   D 7 VAL B 146  ASP B 149 -1  N  GLU B 147   O  THR B 154
SHEET    1   E 2 LYS B 122  VAL B 123  0
SHEET    2   E 2 THR B 140  TYR B 141  1  O  THR B 140   N  VAL B 123
CISPEP   1 GLY A   65    PRO A   66          0         0.52
CISPEP   2 GLY B   65    PRO B   66          0         1.98
SITE     1 AC1  6 GLU A  15  ARG A  48  GLY A  75  ASN A  76
SITE     2 AC1  6 HOH A 639  HOH A 719
SITE     1 AC2  5 ARG B  48  GLY B  75  ASN B  76  HOH B 634
SITE     2 AC2  5 HOH B 806
CRYST1   43.914   85.766   98.829  90.00  90.00  90.00 P 21 21 21    8
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.022772  0.000000  0.000000        0.00000
SCALE2      0.000000  0.011660  0.000000        0.00000
SCALE3      0.000000  0.000000  0.010118        0.00000
      
PROCHECK
Go to PROCHECK summary
 References