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PDBsum entry 1ucf

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Top Page protein Protein-protein interface(s) links
RNA binding protein PDB id
1ucf
Jmol
Contents
Protein chain
188 a.a. *
Waters ×321
* Residue conservation analysis
HEADER    RNA BINDING PROTEIN                     11-APR-03   1UCF
TITLE     THE CRYSTAL STRUCTURE OF DJ-1, A PROTEIN RELATED TO MALE
TITLE    2 FERTILITY AND PARKINSON'S DISEASE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: RNA-BINDING PROTEIN REGULATORY SUBUNIT;
COMPND   3 CHAIN: A, B;
COMPND   4 SYNONYM: DJ-1;
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: DJ-1;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PGEX-6P
KEYWDS    FLAVODOXIN-LIKE ROSSMANN FOLD, RNA BINDING PROTEIN
EXPDTA    X-RAY DIFFRACTION
AUTHOR    K.HONBOU,N.N.SUZUKI,M.HORIUCHI,T.NIKI,T.TAIRA,H.ARIGA,
AUTHOR   2 F.INAGAKI
REVDAT   2   24-FEB-09 1UCF    1       VERSN
REVDAT   1   19-AUG-03 1UCF    0
JRNL        AUTH   K.HONBOU,N.N.SUZUKI,M.HORIUCHI,T.NIKI,T.TAIRA,
JRNL        AUTH 2 H.ARIGA,F.INAGAKI
JRNL        TITL   THE CRYSTAL STRUCTURE OF DJ-1, A PROTEIN RELATED
JRNL        TITL 2 TO MALE FERTILITY AND PARKINSON'S DISEASE
JRNL        REF    J.BIOL.CHEM.                  V. 278 31380 2003
JRNL        REFN                   ISSN 0021-9258
JRNL        PMID   12796482
JRNL        DOI    10.1074/JBC.M305878200
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    1.95 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS 1.0
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 : ENGH & HUBER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 37.52
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 128474.640
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 95.3
REMARK   3   NUMBER OF REFLECTIONS             : 32766
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 SET) : 0.170
REMARK   3   FREE R VALUE                     : 0.195
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 3277
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.003
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 6
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.95
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.07
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 87.40
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 4474
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2100
REMARK   3   BIN FREE R VALUE                    : 0.2480
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 10.60
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 532
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.011
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2718
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 0
REMARK   3   SOLVENT ATOMS            : 321
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 13.50
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.70
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 1.15000
REMARK   3    B22 (A**2) : 1.15000
REMARK   3    B33 (A**2) : -2.30000
REMARK   3    B12 (A**2) : 1.96000
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) : 0.18
REMARK   3   ESD FROM SIGMAA              (A) : 0.13
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.22
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.18
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.005
REMARK   3   BOND ANGLES            (DEGREES) : 1.30
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.00
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.91
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.140 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.740 ; 2.000
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.080 ; 2.000
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.030 ; 2.500
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : FLAT MODEL
REMARK   3   KSOL        : 0.37
REMARK   3   BSOL        : 50.27
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  : WATER_REP.PARAM
REMARK   3  PARAMETER FILE  3  : NULL
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP
REMARK   3  TOPOLOGY FILE  3   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1UCF COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-APR-03.
REMARK 100 THE RCSB ID CODE IS RCSB005673.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 16-MAY-01
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.5
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 ULTRAX 18
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : YALE 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 : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 34488
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900
REMARK 200  RESOLUTION RANGE LOW       (A) : 100.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.2
REMARK 200  DATA REDUNDANCY                : 4.200
REMARK 200  R MERGE                    (I) : 0.07300
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.97
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.8
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : 0.39900
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR
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   (%): 56.67
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.86
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM CITRATE, HEPES, DTT, PH 7.5,
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
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       24.95900
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       49.91800
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: 2590 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14630 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 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     ASP A   189
REMARK 465     ASP B   189
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     LYS A  41    CG   CD   CE   NZ
REMARK 470     LYS A  63    CG   CD   CE   NZ
REMARK 470     GLU A  94    CG   CD   OE1  OE2
REMARK 470     LYS A  99    CG   CD   CE   NZ
REMARK 470     LYS A 175    CG   CD   CE   NZ
REMARK 470     LYS A 188    CG   CD   CE   NZ
REMARK 470     LYS B  41    CG   CD   CE   NZ
REMARK 470     GLN B  80    CG   CD   OE1  NE2
REMARK 470     GLU B  90    CG   CD   OE1  OE2
REMARK 470     LYS B  99    CG   CD   CE   NZ
REMARK 470     GLU B 176    CG   CD   OE1  OE2
REMARK 470     LYS B 188    CG   CD   CE   NZ
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    LYS A  99       42.38     70.57
REMARK 500    CYS A 106     -110.90     66.15
REMARK 500    CYS B 106     -107.91     64.95
REMARK 500
REMARK 500 REMARK: NULL
DBREF  1UCF A    1   189  UNP    Q99497   PARK7_HUMAN      1    189
DBREF  1UCF 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
FORMUL   3  HOH   *321(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  LYS A   99  1                                  15
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 PRO B  109  HIS B  115  1                                   7
HELIX   18  18 HIS B  126  LEU B  128  5                                   3
HELIX   19  19 ALA B  129  MET B  134  1                                   6
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
CISPEP   1 GLY A   65    PRO A   66          0         0.25
CISPEP   2 GLY B   65    PRO B   66          0         0.25
CRYST1   75.039   75.039   74.877  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      0.013326  0.007694  0.000000        0.00000
SCALE2      0.000000  0.015388  0.000000        0.00000
SCALE3      0.000000  0.000000  0.013355        0.00000
      
PROCHECK
Go to PROCHECK summary
 References

 

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