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PDBsum entry 3sf8

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Oncoprotein,unknown function PDB id
3sf8
Jmol
Contents
Protein chain
190 a.a.
Waters ×341
HEADER    ONCOPROTEIN,UNKNOWN FUNCTION            13-JUN-11   3SF8
TITLE     STRUCTURAL INSIGHTS INTO THIOL STABILIZATION OF 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 EC: 3.4.-.-;
COMPND   6 ENGINEERED: YES;
COMPND   7 MOL_ID: 2;
COMPND   8 MOLECULE: PROTEIN DJ-1;
COMPND   9 CHAIN: B;
COMPND  10 SYNONYM: ONCOGENE DJ1, PARKINSON DISEASE PROTEIN 7;
COMPND  11 EC: 3.4.-.-;
COMPND  12 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 MOL_ID: 2;
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE  10 ORGANISM_COMMON: HUMAN;
SOURCE  11 ORGANISM_TAXID: 9606;
SOURCE  12 GENE: PARK7;
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS    OXIDATIVE STRESS, REDOX REGULATION, CYSTEINE OXIDATION, PROTECTING
KEYWDS   2 DJ-1 OXIDATION, REDUCED DJ-1, CLASS I GLUTAMINE AMIDOTRANSFERASE
KEYWDS   3 FAMILY, CYTOPROTECTIVE ACTIVITY AGAINST OXIDATIVE STRESS; CYSTEINE
KEYWDS   4 SULFENIC ACID MODIFICATION, HYDROLASE, ONCOPROTEIN,UNKNOWN FUNCTION
EXPDTA    X-RAY DIFFRACTION
AUTHOR    L.PREMKUMAR,M.K.DOBACZEWSKA,S.J.RIEDL
REVDAT   2   23-NOV-11 3SF8    1       JRNL
REVDAT   1   05-OCT-11 3SF8    0
JRNL        AUTH   L.PREMKUMAR,M.K.DOBACZEWSKA,S.J.RIEDL
JRNL        TITL   IDENTIFICATION OF AN ARTIFICIAL PEPTIDE MOTIF THAT BINDS AND
JRNL        TITL 2 STABILIZES REDUCED HUMAN DJ-1.
JRNL        REF    J.STRUCT.BIOL.                V. 176   414 2011
JRNL        REFN                   ISSN 1047-8477
JRNL        PMID   21893204
JRNL        DOI    10.1016/J.JSB.2011.08.011
REMARK   2
REMARK   2 RESOLUTION.    1.56 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.5.0102
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) : 1.56
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.3
REMARK   3   NUMBER OF REFLECTIONS             : 42954
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) : 0.174
REMARK   3   R VALUE            (WORKING SET) : 0.172
REMARK   3   FREE R VALUE                     : 0.211
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 2318
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) : 1.56
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.60
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2980
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 89.54
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2500
REMARK   3   BIN FREE R VALUE SET COUNT          : 154
REMARK   3   BIN FREE R VALUE                    : 0.2840
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2777
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 0
REMARK   3   SOLVENT ATOMS            : 341
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.12
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.51000
REMARK   3    B22 (A**2) : 1.40000
REMARK   3    B33 (A**2) : -1.52000
REMARK   3    B12 (A**2) : -0.00000
REMARK   3    B13 (A**2) : -0.73000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): NULL
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.094
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.071
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.058
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.968
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.955
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2920 ; 0.013 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3964 ; 1.421 ; 1.999
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   408 ;12.185 ; 5.049
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   107 ;41.738 ;25.514
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   545 ;13.786 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    15 ;17.019 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   468 ; 0.108 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2149 ; 0.008 ; 0.021
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
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):  1922 ; 1.888 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3092 ; 3.194 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   998 ; 4.418 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   859 ; 7.041 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2920 ; 2.588 ; 3.000
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 RIDING
REMARK   3  POSITIONS
REMARK   4
REMARK   4 3SF8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-JUN-11.
REMARK 100 THE RCSB ID CODE IS RCSB066129.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 03-MAR-11
REMARK 200  TEMPERATURE           (KELVIN) : 100.0
REMARK 200  PH                             : 6.5
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 FR-E SUPERBRIGHT
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS HTC
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200  DATA SCALING SOFTWARE          : SCALA
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 47218
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.530
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.0
REMARK 200  DATA REDUNDANCY                : 4.900
REMARK 200  R MERGE                    (I) : 0.04400
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 19.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.53
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.61
REMARK 200  COMPLETENESS FOR SHELL     (%) : 82.4
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.60
REMARK 200  R MERGE FOR SHELL          (I) : 0.25200
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 4.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 1PDV
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 41.37
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 45% (V/V) POLYPROYLENE GLYCOL 400, 0.1
REMARK 280  M BIS-TRIS, PH 6.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280  293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,Y,-Z
REMARK 290       3555   X+1/2,Y+1/2,Z
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        0.00000
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       70.94000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       20.91550
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       70.94000
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       20.91550
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: 2760 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15280 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 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     MET B     1
REMARK 465     ASP B   189
REMARK 465     LEU B   190
REMARK 465     GLU B   191
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    CSO A 106     -110.57     76.73
REMARK 500    CYS B 106     -105.65     75.64
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS
REMARK 500    PRO A  66        22.3      L          L   OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
DBREF  3SF8 A    1   189  UNP    Q99497   PARK7_HUMAN      1    189
DBREF  3SF8 B    1   189  UNP    Q99497   PARK7_HUMAN      1    189
SEQADV 3SF8 LEU A  190  UNP  Q99497              EXPRESSION TAG
SEQADV 3SF8 GLU A  191  UNP  Q99497              EXPRESSION TAG
SEQADV 3SF8 LEU B  190  UNP  Q99497              EXPRESSION TAG
SEQADV 3SF8 GLU B  191  UNP  Q99497              EXPRESSION TAG
SEQRES   1 A  191  MET ALA SER LYS ARG ALA LEU VAL ILE LEU ALA LYS GLY
SEQRES   2 A  191  ALA GLU GLU MET GLU THR VAL ILE PRO VAL ASP VAL MET
SEQRES   3 A  191  ARG ARG ALA GLY ILE LYS VAL THR VAL ALA GLY LEU ALA
SEQRES   4 A  191  GLY LYS ASP PRO VAL GLN CYS SER ARG ASP VAL VAL ILE
SEQRES   5 A  191  CYS PRO ASP ALA SER LEU GLU ASP ALA LYS LYS GLU GLY
SEQRES   6 A  191  PRO TYR ASP VAL VAL VAL LEU PRO GLY GLY ASN LEU GLY
SEQRES   7 A  191  ALA GLN ASN LEU SER GLU SER ALA ALA VAL LYS GLU ILE
SEQRES   8 A  191  LEU LYS GLU GLN GLU ASN ARG LYS GLY LEU ILE ALA ALA
SEQRES   9 A  191  ILE CSO ALA GLY PRO THR ALA LEU LEU ALA HIS GLU ILE
SEQRES  10 A  191  GLY PHE GLY SER LYS VAL THR THR HIS PRO LEU ALA LYS
SEQRES  11 A  191  ASP LYS MET MET ASN GLY GLY HIS TYR THR TYR SER GLU
SEQRES  12 A  191  ASN ARG VAL GLU LYS ASP GLY LEU ILE LEU THR SER ARG
SEQRES  13 A  191  GLY PRO GLY THR SER PHE GLU PHE ALA LEU ALA ILE VAL
SEQRES  14 A  191  GLU ALA LEU ASN GLY LYS GLU VAL ALA ALA GLN VAL LYS
SEQRES  15 A  191  ALA PRO LEU VAL LEU LYS ASP LEU GLU
SEQRES   1 B  191  MET ALA SER LYS ARG ALA LEU VAL ILE LEU ALA LYS GLY
SEQRES   2 B  191  ALA GLU GLU MET GLU THR VAL ILE PRO VAL ASP VAL MET
SEQRES   3 B  191  ARG ARG ALA GLY ILE LYS VAL THR VAL ALA GLY LEU ALA
SEQRES   4 B  191  GLY LYS ASP PRO VAL GLN CYS SER ARG ASP VAL VAL ILE
SEQRES   5 B  191  CYS PRO ASP ALA SER LEU GLU ASP ALA LYS LYS GLU GLY
SEQRES   6 B  191  PRO TYR ASP VAL VAL VAL LEU PRO GLY GLY ASN LEU GLY
SEQRES   7 B  191  ALA GLN ASN LEU SER GLU SER ALA ALA VAL LYS GLU ILE
SEQRES   8 B  191  LEU LYS GLU GLN GLU ASN ARG LYS GLY LEU ILE ALA ALA
SEQRES   9 B  191  ILE CYS ALA GLY PRO THR ALA LEU LEU ALA HIS GLU ILE
SEQRES  10 B  191  GLY PHE GLY SER LYS VAL THR THR HIS PRO LEU ALA LYS
SEQRES  11 B  191  ASP LYS MET MET ASN GLY GLY HIS TYR THR TYR SER GLU
SEQRES  12 B  191  ASN ARG VAL GLU LYS ASP GLY LEU ILE LEU THR SER ARG
SEQRES  13 B  191  GLY PRO GLY THR SER PHE GLU PHE ALA LEU ALA ILE VAL
SEQRES  14 B  191  GLU ALA LEU ASN GLY LYS GLU VAL ALA ALA GLN VAL LYS
SEQRES  15 B  191  ALA PRO LEU VAL LEU LYS ASP LEU GLU
MODRES 3SF8 CSO A  106  CYS  S-HYDROXYCYSTEINE
HET    CSO  A 106       7
HETNAM     CSO S-HYDROXYCYSTEINE
FORMUL   1  CSO    C3 H7 N O3 S
FORMUL   3  HOH   *341(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  GLU A   84  1                                  10
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
HELIX   13  13 GLU B   15  ALA B   29  1                                  15
HELIX   14  14 LEU B   58  LYS B   63  1                                   6
HELIX   15  15 GLY B   75  SER B   85  1                                  11
HELIX   16  16 SER B   85  ARG B   98  1                                  14
HELIX   17  17 GLY B  108  HIS B  115  1                                   8
HELIX   18  18 HIS B  126  LEU B  128  5                                   3
HELIX   19  19 ALA B  129  ASN B  135  1                                   7
HELIX   20  20 GLY B  157  GLY B  159  5                                   3
HELIX   21  21 THR B  160  GLY B  174  1                                  15
HELIX   22  22 GLY B  174  ALA B  183  1                                  10
HELIX   23  23 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  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 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  CYS B  53 -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  LEU B  72
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
LINK         C   ILE A 105                 N   CSO A 106     1555   1555  1.34
LINK         C   CSO A 106                 N   ALA A 107     1555   1555  1.34
CISPEP   1 GLY A   65    PRO A   66          0        -3.75
CISPEP   2 GLY B   65    PRO B   66          0        -6.22
CRYST1  141.880   41.831   63.344  90.00 115.79  90.00 C 1 2 1       4
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      0.007048  0.000000  0.003406        0.00000
SCALE2      0.000000  0.023906  0.000000        0.00000
SCALE3      0.000000  0.000000  0.017533        0.00000
      
PROCHECK
Go to PROCHECK summary
 References