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PDBsum entry 2r1u

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Protein binding PDB id
2r1u
Jmol
Contents
Protein chain
187 a.a.
Waters ×416
HEADER    PROTEIN BINDING                         23-AUG-07   2R1U
TITLE     DJ-1 ACTIVATION BY CATECHOL QUINONE MODIFICATION
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PROTEIN DJ-1;
COMPND   3 CHAIN: A, B;
COMPND   4 SYNONYM: ONCOGENE DJ1, PARKINSON DISEASE PROTEIN 7;
COMPND   5 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 GENE: PARK7;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: B834;
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: VECTOR;
SOURCE   8 EXPRESSION_SYSTEM_VECTOR: PET
KEYWDS    DJ-1, CATECHOL QUINONE, ISOPEPTIDASE, CHAPERONE, CYTOPLASM,
KEYWDS   2 DISEASE MUTATION, NUCLEUS, ONCOGENE, OXIDATION, PARKINSON
KEYWDS   3 DISEASE, PHOSPHORYLATION, POLYMORPHISM, UBL CONJUGATION,
KEYWDS   4 PROTEIN BINDING
EXPDTA    X-RAY DIFFRACTION
AUTHOR    ZHONGTAO Z.,YUE F.
REVDAT   2   24-FEB-09 2R1U    1       VERSN
REVDAT   1   26-AUG-08 2R1U    0
JRNL        AUTH   ZHONGTAO Z.,YUE F.
JRNL        TITL   DJ-1 ACTIVATION BY CATECHOL QUINONE MODIFICATION
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    1.50 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK   3               : READ,RICE,SIMONSON,WARREN
REMARK   3
REMARK   3  REFINEMENT TARGET : NULL
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 24.68
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 93.3
REMARK   3   NUMBER OF REFLECTIONS             : 71845
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL
REMARK   3   R VALUE            (WORKING SET) : 0.185
REMARK   3   FREE R VALUE                     : 0.195
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.400
REMARK   3   FREE R VALUE TEST SET COUNT      : 7230
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : NULL
REMARK   3   BIN FREE R VALUE                    : NULL
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2752
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 0
REMARK   3   SOLVENT ATOMS            : 416
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 17.05
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.94300
REMARK   3    B22 (A**2) : -0.94300
REMARK   3    B33 (A**2) : 1.88600
REMARK   3    B12 (A**2) : -0.87400
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL
REMARK   3   ESD FROM SIGMAA              (A) : NULL
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.005
REMARK   3   BOND ANGLES            (DEGREES) : 1.32
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : 0.946 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.512 ; 2.000
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.037 ; 2.000
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.010 ; 2.500
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : NULL
REMARK   3   KSOL        : NULL
REMARK   3   BSOL        : 63.55
REMARK   3
REMARK   3  NCS MODEL : NULL
REMARK   3
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM
REMARK   3  PARAMETER FILE  2  : DNA-RNA_REP.PARAM
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM
REMARK   3  PARAMETER FILE  4  : ION.PARAM
REMARK   3  PARAMETER FILE  5  : NULL
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP
REMARK   3  TOPOLOGY FILE  2   : DNA-RNA.TOP
REMARK   3  TOPOLOGY FILE  3   : WATER.TOP
REMARK   3  TOPOLOGY FILE  4   : ION.TOP
REMARK   3  TOPOLOGY FILE  5   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 2R1U COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-SEP-07.
REMARK 100 THE RCSB ID CODE IS RCSB044319.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 22-JUN-07
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : APS
REMARK 200  BEAMLINE                       : 19-BM
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                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : NULL
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200  DATA SCALING SOFTWARE          : NULL
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 71845
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.500
REMARK 200  RESOLUTION RANGE LOW       (A) : 500.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.3
REMARK 200  DATA REDUNDANCY                : 6.500
REMARK 200  R MERGE                    (I) : 0.04000
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 40.0000
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) : NULL
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.50
REMARK 200  R MERGE FOR SHELL          (I) : 0.04000
REMARK 200  R SYM FOR SHELL            (I) : 0.04000
REMARK 200   FOR SHELL         : 40.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 61.01
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.15
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 29%PEG4K, PH 6.5, VAPOR DIFFUSION,
REMARK 280  HANGING DROP, TEMPERATURE 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31
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
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       25.01500
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       50.03000
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: 2800 ANGSTROM**2
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 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     -108.62     64.91
REMARK 500    CYS B 106     -107.78     65.54
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1J42   RELATED DB: PDB
REMARK 900 RELATED ID: 2R1T   RELATED DB: PDB
REMARK 900 RELATED ID: 2R1V   RELATED DB: PDB
DBREF  2R1U A    2   188  UNP    Q99497   PARK7_HUMAN      2    188
DBREF  2R1U B    2   188  UNP    Q99497   PARK7_HUMAN      2    188
SEQRES   1 A  187  ALA SER LYS ARG ALA LEU VAL ILE LEU ALA LYS GLY ALA
SEQRES   2 A  187  GLU GLU MET GLU THR VAL ILE PRO VAL ASP VAL MET ARG
SEQRES   3 A  187  ARG ALA GLY ILE LYS VAL THR VAL ALA GLY LEU ALA GLY
SEQRES   4 A  187  LYS ASP PRO VAL GLN CYS SER ARG ASP VAL VAL ILE CYS
SEQRES   5 A  187  PRO ASP ALA SER LEU GLU ASP ALA LYS LYS GLU GLY PRO
SEQRES   6 A  187  TYR ASP VAL VAL VAL LEU PRO GLY GLY ASN LEU GLY ALA
SEQRES   7 A  187  GLN ASN LEU SER GLU SER ALA ALA VAL LYS GLU ILE LEU
SEQRES   8 A  187  LYS GLU GLN GLU ASN ARG LYS GLY LEU ILE ALA ALA ILE
SEQRES   9 A  187  CYS ALA GLY PRO THR ALA LEU LEU ALA HIS GLU ILE GLY
SEQRES  10 A  187  PHE GLY SER LYS VAL THR THR HIS PRO LEU ALA LYS ASP
SEQRES  11 A  187  LYS MET MET ASN GLY GLY HIS TYR THR TYR SER GLU ASN
SEQRES  12 A  187  ARG VAL GLU LYS ASP GLY LEU ILE LEU THR SER ARG GLY
SEQRES  13 A  187  PRO GLY THR SER PHE GLU PHE ALA LEU ALA ILE VAL GLU
SEQRES  14 A  187  ALA LEU ASN GLY LYS GLU VAL ALA ALA GLN VAL LYS ALA
SEQRES  15 A  187  PRO LEU VAL LEU LYS
SEQRES   1 B  187  ALA SER LYS ARG ALA LEU VAL ILE LEU ALA LYS GLY ALA
SEQRES   2 B  187  GLU GLU MET GLU THR VAL ILE PRO VAL ASP VAL MET ARG
SEQRES   3 B  187  ARG ALA GLY ILE LYS VAL THR VAL ALA GLY LEU ALA GLY
SEQRES   4 B  187  LYS ASP PRO VAL GLN CYS SER ARG ASP VAL VAL ILE CYS
SEQRES   5 B  187  PRO ASP ALA SER LEU GLU ASP ALA LYS LYS GLU GLY PRO
SEQRES   6 B  187  TYR ASP VAL VAL VAL LEU PRO GLY GLY ASN LEU GLY ALA
SEQRES   7 B  187  GLN ASN LEU SER GLU SER ALA ALA VAL LYS GLU ILE LEU
SEQRES   8 B  187  LYS GLU GLN GLU ASN ARG LYS GLY LEU ILE ALA ALA ILE
SEQRES   9 B  187  CYS ALA GLY PRO THR ALA LEU LEU ALA HIS GLU ILE GLY
SEQRES  10 B  187  PHE GLY SER LYS VAL THR THR HIS PRO LEU ALA LYS ASP
SEQRES  11 B  187  LYS MET MET ASN GLY GLY HIS TYR THR TYR SER GLU ASN
SEQRES  12 B  187  ARG VAL GLU LYS ASP GLY LEU ILE LEU THR SER ARG GLY
SEQRES  13 B  187  PRO GLY THR SER PHE GLU PHE ALA LEU ALA ILE VAL GLU
SEQRES  14 B  187  ALA LEU ASN GLY LYS GLU VAL ALA ALA GLN VAL LYS ALA
SEQRES  15 B  187  PRO LEU VAL LEU LYS
FORMUL   3  HOH   *416(H2 O)
HELIX    1   1 GLU A   15  ALA A   29  1                                  15
HELIX    2   2 LEU A   58  LYS A   63  1                                   6
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 PRO A  109  HIS A  115  1                                   7
HELIX    6   6 HIS A  126  LEU A  128  5                                   3
HELIX    7   7 ALA A  129  MET A  134  1                                   6
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  LYS B   63  1                                   6
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  MET B  134  1                                   6
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  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  CYS B  53   N  VAL A  51
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
CISPEP   1 GLY A   65    PRO A   66          0        -0.13
CISPEP   2 GLY B   65    PRO B   66          0        -0.03
CRYST1   75.688   75.688   75.045  90.00  90.00 120.00 P 31          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      0.013212  0.007628  0.000000        0.00000
SCALE2      0.000000  0.015256  0.000000        0.00000
SCALE3      0.000000  0.000000  0.013325        0.00000
      
PROCHECK
Go to PROCHECK summary
 References