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PDBsum entry 16gs

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Top Page protein ligands Protein-protein interface(s) links
Transferase PDB id
16gs
Jmol
Contents
Protein chain
208 a.a. *
Ligands
SO4
MES ×2
Waters ×298
* Residue conservation analysis
HEADER    TRANSFERASE                             30-NOV-97   16GS
TITLE     GLUTATHIONE S-TRANSFERASE P1-1 APO FORM 3
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: GLUTATHIONE S-TRANSFERASE;
COMPND   3 CHAIN: A, B;
COMPND   4 SYNONYM: GSTP1-1;
COMPND   5 EC: 2.5.1.18;
COMPND   6 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 CELLULAR_LOCATION: CYTOSOL;
SOURCE   6 GENE: GSTP1;
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   9 EXPRESSION_SYSTEM_GENE: GSTP1
KEYWDS    TRANSFERASE, APOENZYME, DETOXIFICATION
EXPDTA    X-RAY DIFFRACTION
AUTHOR    A.J.OAKLEY,M.LO BELLO,G.RICCI,G.FEDERICI,M.W.PARKER
REVDAT   2   24-FEB-09 16GS    1       VERSN
REVDAT   1   13-JAN-99 16GS    0
JRNL        AUTH   A.J.OAKLEY,M.LO BELLO,G.RICCI,G.FEDERICI,M.W.PARKER
JRNL        TITL   EVIDENCE FOR AN INDUCED-FIT MECHANISM OPERATING IN
JRNL        TITL 2 PI CLASS GLUTATHIONE TRANSFERASES.
JRNL        REF    BIOCHEMISTRY                  V.  37  9912 1998
JRNL        REFN                   ISSN 0006-2960
JRNL        PMID   9665696
JRNL        DOI    10.1021/BI980323W
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : X-PLOR 3.851
REMARK   3   AUTHORS     : BRUNGER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 15.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 100000000.000
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 93.5
REMARK   3   NUMBER OF REFLECTIONS             : 34299
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) : 0.227
REMARK   3   FREE R VALUE                     : 0.263
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1705
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.006
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 10
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.90
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.97
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 75.80
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 2641
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3660
REMARK   3   BIN FREE R VALUE                    : 0.3600
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.00
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 139
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.031
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 3262
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 29
REMARK   3   SOLVENT ATOMS            : 1631
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 21.00
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 27.20
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : 0.00000
REMARK   3    B12 (A**2) : 0.00000
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) : 0.25
REMARK   3   ESD FROM SIGMAA              (A) : 0.28
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 15.00
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.29
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.28
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.007
REMARK   3   BOND ANGLES            (DEGREES) : 1.30
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.20
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.82
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) : 2.140 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 3.100 ; 2.000
REMARK   3   SIDE-CHAIN BOND              (A**2) : 3.750 ; 2.000
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 5.340 ; 2.500
REMARK   3
REMARK   3  NCS MODEL : RESTRAINTS
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.
REMARK   3  PARAMETER FILE  3  : MES.PA
REMARK   3  PARAMETER FILE  4  : SO4.PA
REMARK   3  PARAMETER FILE  5  : NULL
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO
REMARK   3  TOPOLOGY FILE  2   : MES.TO
REMARK   3  TOPOLOGY FILE  3   : WATER.
REMARK   3  TOPOLOGY FILE  4   : SO4.TO
REMARK   3  TOPOLOGY FILE  5   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK   4
REMARK   4 16GS COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 25-AUG-97
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 5.8
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 RUH2R
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : GRAPHITE(002)
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 96823
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900
REMARK 200  RESOLUTION RANGE LOW       (A) : 14.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.1
REMARK 200  DATA REDUNDANCY                : 2.800
REMARK 200  R MERGE                    (I) : 0.05300
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 17.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.91
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.98
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.5
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : 0.32900
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 2.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR 3.851
REMARK 200 STARTING MODEL: PDB ENTRY 5GSS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 51.42
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.53
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 5.8
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       38.76850
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       44.89850
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       38.76850
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       44.89850
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: 2850 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17960 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 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     0
REMARK 465     PRO A     1
REMARK 465     MET B     0
REMARK 465     PRO B     1
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    GLN A  64      114.89     84.56
REMARK 500    THR A 141     -104.84   -110.30
REMARK 500    PRO A 187      -70.11    -34.39
REMARK 500    GLN B  64      116.02     84.60
REMARK 500    THR B 141     -105.01   -109.25
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 289        DISTANCE =  5.37 ANGSTROMS
REMARK 525    HOH A 328        DISTANCE =  6.26 ANGSTROMS
REMARK 525    HOH A 332        DISTANCE =  5.18 ANGSTROMS
REMARK 525    HOH B 335        DISTANCE =  7.85 ANGSTROMS
REMARK 525    HOH B 348        DISTANCE =  5.34 ANGSTROMS
REMARK 525    HOH A 365        DISTANCE =  6.03 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 210
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES A 211
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES B 210
DBREF  16GS A    1   209  UNP    P09211   GSTP1_HUMAN      1    209
DBREF  16GS B    1   209  UNP    P09211   GSTP1_HUMAN      1    209
SEQRES   1 A  210  MET PRO PRO TYR THR VAL VAL TYR PHE PRO VAL ARG GLY
SEQRES   2 A  210  ARG CYS ALA ALA LEU ARG MET LEU LEU ALA ASP GLN GLY
SEQRES   3 A  210  GLN SER TRP LYS GLU GLU VAL VAL THR VAL GLU THR TRP
SEQRES   4 A  210  GLN GLU GLY SER LEU LYS ALA SER CYS LEU TYR GLY GLN
SEQRES   5 A  210  LEU PRO LYS PHE GLN ASP GLY ASP LEU THR LEU TYR GLN
SEQRES   6 A  210  SER ASN THR ILE LEU ARG HIS LEU GLY ARG THR LEU GLY
SEQRES   7 A  210  LEU TYR GLY LYS ASP GLN GLN GLU ALA ALA LEU VAL ASP
SEQRES   8 A  210  MET VAL ASN ASP GLY VAL GLU ASP LEU ARG CYS LYS TYR
SEQRES   9 A  210  ILE SER LEU ILE TYR THR ASN TYR GLU ALA GLY LYS ASP
SEQRES  10 A  210  ASP TYR VAL LYS ALA LEU PRO GLY GLN LEU LYS PRO PHE
SEQRES  11 A  210  GLU THR LEU LEU SER GLN ASN GLN GLY GLY LYS THR PHE
SEQRES  12 A  210  ILE VAL GLY ASP GLN ILE SER PHE ALA ASP TYR ASN LEU
SEQRES  13 A  210  LEU ASP LEU LEU LEU ILE HIS GLU VAL LEU ALA PRO GLY
SEQRES  14 A  210  CYS LEU ASP ALA PHE PRO LEU LEU SER ALA TYR VAL GLY
SEQRES  15 A  210  ARG LEU SER ALA ARG PRO LYS LEU LYS ALA PHE LEU ALA
SEQRES  16 A  210  SER PRO GLU TYR VAL ASN LEU PRO ILE ASN GLY ASN GLY
SEQRES  17 A  210  LYS GLN
SEQRES   1 B  210  MET PRO PRO TYR THR VAL VAL TYR PHE PRO VAL ARG GLY
SEQRES   2 B  210  ARG CYS ALA ALA LEU ARG MET LEU LEU ALA ASP GLN GLY
SEQRES   3 B  210  GLN SER TRP LYS GLU GLU VAL VAL THR VAL GLU THR TRP
SEQRES   4 B  210  GLN GLU GLY SER LEU LYS ALA SER CYS LEU TYR GLY GLN
SEQRES   5 B  210  LEU PRO LYS PHE GLN ASP GLY ASP LEU THR LEU TYR GLN
SEQRES   6 B  210  SER ASN THR ILE LEU ARG HIS LEU GLY ARG THR LEU GLY
SEQRES   7 B  210  LEU TYR GLY LYS ASP GLN GLN GLU ALA ALA LEU VAL ASP
SEQRES   8 B  210  MET VAL ASN ASP GLY VAL GLU ASP LEU ARG CYS LYS TYR
SEQRES   9 B  210  ILE SER LEU ILE TYR THR ASN TYR GLU ALA GLY LYS ASP
SEQRES  10 B  210  ASP TYR VAL LYS ALA LEU PRO GLY GLN LEU LYS PRO PHE
SEQRES  11 B  210  GLU THR LEU LEU SER GLN ASN GLN GLY GLY LYS THR PHE
SEQRES  12 B  210  ILE VAL GLY ASP GLN ILE SER PHE ALA ASP TYR ASN LEU
SEQRES  13 B  210  LEU ASP LEU LEU LEU ILE HIS GLU VAL LEU ALA PRO GLY
SEQRES  14 B  210  CYS LEU ASP ALA PHE PRO LEU LEU SER ALA TYR VAL GLY
SEQRES  15 B  210  ARG LEU SER ALA ARG PRO LYS LEU LYS ALA PHE LEU ALA
SEQRES  16 B  210  SER PRO GLU TYR VAL ASN LEU PRO ILE ASN GLY ASN GLY
SEQRES  17 B  210  LYS GLN
HET    SO4  A 210       5
HET    MES  A 211      12
HET    MES  B 210      12
HETNAM     SO4 SULFATE ION
HETNAM     MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID
FORMUL   3  SO4    O4 S 2-
FORMUL   4  MES    2(C6 H13 N O4 S)
FORMUL   6  HOH   *298(H2 O)
HELIX    1   1 GLY A   12  ASP A   23  5                                  12
HELIX    2   2 VAL A   35  GLN A   39  1                                   5
HELIX    3   3 SER A   42  SER A   46  1                                   5
HELIX    4   4 SER A   65  LEU A   76  1                                  12
HELIX    5   5 GLN A   83  TYR A  108  1                                  26
HELIX    6   6 TYR A  111  GLN A  135  1                                  25
HELIX    7   7 GLN A  137  GLY A  139  5                                   3
HELIX    8   8 PHE A  150  LEU A  165  1                                  16
HELIX    9   9 PRO A  174  SER A  184  1                                  11
HELIX   10  10 PRO A  187  ALA A  194  1                                   8
HELIX   11  11 PRO A  196  VAL A  199  1                                   4
HELIX   12  12 GLY B   12  ASP B   23  5                                  12
HELIX   13  13 VAL B   35  GLN B   39  1                                   5
HELIX   14  14 SER B   42  SER B   46  1                                   5
HELIX   15  15 SER B   65  LEU B   76  1                                  12
HELIX   16  16 GLN B   83  TYR B  108  1                                  26
HELIX   17  17 TYR B  111  GLN B  135  1                                  25
HELIX   18  18 GLN B  137  GLY B  139  5                                   3
HELIX   19  19 PHE B  150  LEU B  165  1                                  16
HELIX   20  20 PRO B  174  SER B  184  1                                  11
HELIX   21  21 PRO B  187  ALA B  194  1                                   8
HELIX   22  22 PRO B  196  VAL B  199  1                                   4
SHEET    1   A 4 TRP A  28  VAL A  33  0
SHEET    2   A 4 TYR A   3  PHE A   8  1  N  TYR A   3   O  LYS A  29
SHEET    3   A 4 LYS A  54  ASP A  57 -1  N  GLN A  56   O  THR A   4
SHEET    4   A 4 LEU A  60  TYR A  63 -1  N  LEU A  62   O  PHE A  55
SHEET    1   B 4 TRP B  28  VAL B  33  0
SHEET    2   B 4 TYR B   3  PHE B   8  1  N  TYR B   3   O  LYS B  29
SHEET    3   B 4 LYS B  54  ASP B  57 -1  N  GLN B  56   O  THR B   4
SHEET    4   B 4 LEU B  60  TYR B  63 -1  N  LEU B  62   O  PHE B  55
CISPEP   1 LEU A   52    PRO A   53          0        -0.01
CISPEP   2 LEU B   52    PRO B   53          0         0.67
SITE     1 AC1 12 ASN A  66  ARG A  70  ASP A  94  GLU A  97
SITE     2 AC1 12 HOH A 267  HOH A 269  HOH A 293  ASN B  66
SITE     3 AC1 12 ARG B  70  ASP B  94  GLU B  97  HOH B 211
SITE     1 AC2  6 ALA A  22  TRP A  28  GLU A  30  GLU A 197
SITE     2 AC2  6 ASP B 171  HOH B 335
SITE     1 AC3  5 ASP A 171  ALA B  22  TRP B  28  GLU B  30
SITE     2 AC3  5 GLU B 197
CRYST1   77.537   89.797   68.673  90.00  97.79  90.00 C 1 2 1       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      0.012897  0.000000  0.001764        0.00000
SCALE2      0.000000  0.011136  0.000000        0.00000
SCALE3      0.000000  0.000000  0.014697        0.00000
MTRIX1   1  0.939833  0.129827  0.316003       -5.89306    1
MTRIX2   1  0.128491 -0.991391  0.025155       21.18149    1
MTRIX3   1  0.316549  0.016962 -0.948424       27.19538    1
      
PROCHECK
Go to PROCHECK summary
 References