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PDBsum entry 4ec0

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Top Page protein ligands metals Protein-protein interface(s) links
Isomerase/isomerase inhibitor PDB id
4ec0
Jmol
Contents
Protein chain
199 a.a.
Ligands
GSH ×2
7PQ
Metals
_MG
Waters ×761
HEADER    ISOMERASE/ISOMERASE INHIBITOR           26-MAR-12   4EC0
TITLE     CRYSTAL STRUCTURE OF HH-PGDS WITH WATER DISPLACING INHIBITOR
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: HEMATOPOIETIC PROSTAGLANDIN D SYNTHASE;
COMPND   3 CHAIN: A, B;
COMPND   4 SYNONYM: H-PGDS, GST CLASS-SIGMA, GLUTATHIONE S-TRANSFERASE,
COMPND   5 GLUTATHIONE-DEPENDENT PGD SYNTHASE, GLUTATHIONE-REQUIRING
COMPND   6 PROSTAGLANDIN D SYNTHASE, PROSTAGLANDIN-H2 D-ISOMERASE;
COMPND   7 EC: 5.3.99.2, 2.5.1.18;
COMPND   8 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: GSTS, HPGDS, PGDS, PTGDS2;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS    INHIBITOR, SOLVENT REPLACEMENT, ISOMERASE-ISOMERASE INHIBITOR COMPLEX
EXPDTA    X-RAY DIFFRACTION
AUTHOR    J.E.DAY,A.THORARENSEN,J.I.TRUJILLO
REVDAT   2   02-JAN-13 4EC0    1       JRNL
REVDAT   1   16-MAY-12 4EC0    0
JRNL        AUTH   J.I.TRUJILLO,J.R.KIEFER,W.HUANG,J.E.DAY,J.MOON,G.M.JEROME,
JRNL        AUTH 2 C.P.BONO,C.M.KORNMEIER,M.L.WILLIAMS,C.KUHN,G.R.RENNIE,
JRNL        AUTH 3 T.A.WYNN,C.P.CARRON,A.THORARENSEN
JRNL        TITL   INVESTIGATION OF THE BINDING POCKET OF HUMAN HEMATOPOIETIC
JRNL        TITL 2 PROSTAGLANDIN (PG) D2 SYNTHASE (HH-PGDS): A TALE OF TWO
JRNL        TITL 3 WATERS.
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  22  3795 2012
JRNL        REFN                   ISSN 0960-894X
JRNL        PMID   22546671
JRNL        DOI    10.1016/J.BMCL.2012.04.004
REMARK   2
REMARK   2 RESOLUTION.    1.85 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : X-PLOR 98.1
REMARK   3   AUTHORS     : BRUNGER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL
REMARK   3   NUMBER OF REFLECTIONS             : 32124
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) : 0.186
REMARK   3   FREE R VALUE                     : 0.252
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL
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            : 3302
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 70
REMARK   3   SOLVENT ATOMS            : 761
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 21.48
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : NULL
REMARK   3    B22 (A**2) : NULL
REMARK   3    B33 (A**2) : NULL
REMARK   3    B12 (A**2) : NULL
REMARK   3    B13 (A**2) : NULL
REMARK   3    B23 (A**2) : NULL
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) : NULL
REMARK   3   BOND ANGLES            (DEGREES) : NULL
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) : NULL  ; NULL
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL
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  : NULL
REMARK   3  TOPOLOGY FILE  1   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 4EC0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-APR-12.
REMARK 100 THE RCSB ID CODE IS RCSB071427.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : NULL
REMARK 200  TEMPERATURE           (KELVIN) : NULL
REMARK 200  PH                             : NULL
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 MICROMAX-007
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : OSMIC MIRRORS
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL
REMARK 200  DATA SCALING SOFTWARE          : HKL
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 32926
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.850
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.5
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.08200
REMARK 200   FOR THE DATA SET  : 13.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 41.75
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOR DIFFUSION
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,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       38.85300
REMARK 290   SMTRY3   2  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 300 REMARK: BIOLOGICAL UNIT IS THE SAME AS ASYM.
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: 4200 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18550 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.0 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     HIS A     0
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  36      -18.35    -49.56
REMARK 500    SER A  44        5.61    -63.10
REMARK 500    GLN A  63      106.09     76.63
REMARK 500    GLN B1063      104.88     72.57
REMARK 500    GLU B1106      127.35    -12.77
REMARK 500    GLU B1113        0.71    -68.90
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 A 448        DISTANCE =  5.07 ANGSTROMS
REMARK 525    HOH A 564        DISTANCE =  6.05 ANGSTROMS
REMARK 525    HOH A 632        DISTANCE =  5.30 ANGSTROMS
REMARK 525    HOH A 655        DISTANCE =  7.24 ANGSTROMS
REMARK 525    HOH A 666        DISTANCE =  6.92 ANGSTROMS
REMARK 525    HOH A 682        DISTANCE =  6.49 ANGSTROMS
REMARK 525    HOH A 688        DISTANCE =  6.92 ANGSTROMS
REMARK 525    HOH B1610        DISTANCE =  8.13 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG A 202  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B1437   O
REMARK 620 2 HOH A 459   O   179.4
REMARK 620 3 HOH A 412   O    89.2  90.7
REMARK 620 4 HOH B1372   O    92.3  87.1  91.9
REMARK 620 5 HOH A 423   O    92.4  88.2  83.5 173.4
REMARK 620 6 HOH B1384   O    85.3  94.9 167.9  99.1  85.9
REMARK 620 N                    1     2     3     4     5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GSH A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 7PQ A 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GSH B 1201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4EE0   RELATED DB: PDB
REMARK 900 RELATED ID: 4EDY   RELATED DB: PDB
REMARK 900 RELATED ID: 4EDZ   RELATED DB: PDB
DBREF  4EC0 A    1   199  UNP    O60760   HPGDS_HUMAN      1    199
DBREF  4EC0 B 1001  1199  UNP    O60760   HPGDS_HUMAN      1    199
SEQADV 4EC0 HIS A    0  UNP  O60760              EXPRESSION TAG
SEQADV 4EC0 HIS B 1000  UNP  O60760              EXPRESSION TAG
SEQRES   1 A  200  HIS MET PRO ASN TYR LYS LEU THR TYR PHE ASN MET ARG
SEQRES   2 A  200  GLY ARG ALA GLU ILE ILE ARG TYR ILE PHE ALA TYR LEU
SEQRES   3 A  200  ASP ILE GLN TYR GLU ASP HIS ARG ILE GLU GLN ALA ASP
SEQRES   4 A  200  TRP PRO GLU ILE LYS SER THR LEU PRO PHE GLY LYS ILE
SEQRES   5 A  200  PRO ILE LEU GLU VAL ASP GLY LEU THR LEU HIS GLN SER
SEQRES   6 A  200  LEU ALA ILE ALA ARG TYR LEU THR LYS ASN THR ASP LEU
SEQRES   7 A  200  ALA GLY ASN THR GLU MET GLU GLN CYS HIS VAL ASP ALA
SEQRES   8 A  200  ILE VAL ASP THR LEU ASP ASP PHE MET SER CYS PHE PRO
SEQRES   9 A  200  TRP ALA GLU LYS LYS GLN ASP VAL LYS GLU GLN MET PHE
SEQRES  10 A  200  ASN GLU LEU LEU THR TYR ASN ALA PRO HIS LEU MET GLN
SEQRES  11 A  200  ASP LEU ASP THR TYR LEU GLY GLY ARG GLU TRP LEU ILE
SEQRES  12 A  200  GLY ASN SER VAL THR TRP ALA ASP PHE TYR TRP GLU ILE
SEQRES  13 A  200  CYS SER THR THR LEU LEU VAL PHE LYS PRO ASP LEU LEU
SEQRES  14 A  200  ASP ASN HIS PRO ARG LEU VAL THR LEU ARG LYS LYS VAL
SEQRES  15 A  200  GLN ALA ILE PRO ALA VAL ALA ASN TRP ILE LYS ARG ARG
SEQRES  16 A  200  PRO GLN THR LYS LEU
SEQRES   1 B  200  HIS MET PRO ASN TYR LYS LEU THR TYR PHE ASN MET ARG
SEQRES   2 B  200  GLY ARG ALA GLU ILE ILE ARG TYR ILE PHE ALA TYR LEU
SEQRES   3 B  200  ASP ILE GLN TYR GLU ASP HIS ARG ILE GLU GLN ALA ASP
SEQRES   4 B  200  TRP PRO GLU ILE LYS SER THR LEU PRO PHE GLY LYS ILE
SEQRES   5 B  200  PRO ILE LEU GLU VAL ASP GLY LEU THR LEU HIS GLN SER
SEQRES   6 B  200  LEU ALA ILE ALA ARG TYR LEU THR LYS ASN THR ASP LEU
SEQRES   7 B  200  ALA GLY ASN THR GLU MET GLU GLN CYS HIS VAL ASP ALA
SEQRES   8 B  200  ILE VAL ASP THR LEU ASP ASP PHE MET SER CYS PHE PRO
SEQRES   9 B  200  TRP ALA GLU LYS LYS GLN ASP VAL LYS GLU GLN MET PHE
SEQRES  10 B  200  ASN GLU LEU LEU THR TYR ASN ALA PRO HIS LEU MET GLN
SEQRES  11 B  200  ASP LEU ASP THR TYR LEU GLY GLY ARG GLU TRP LEU ILE
SEQRES  12 B  200  GLY ASN SER VAL THR TRP ALA ASP PHE TYR TRP GLU ILE
SEQRES  13 B  200  CYS SER THR THR LEU LEU VAL PHE LYS PRO ASP LEU LEU
SEQRES  14 B  200  ASP ASN HIS PRO ARG LEU VAL THR LEU ARG LYS LYS VAL
SEQRES  15 B  200  GLN ALA ILE PRO ALA VAL ALA ASN TRP ILE LYS ARG ARG
SEQRES  16 B  200  PRO GLN THR LYS LEU
HET    GSH  A 201      20
HET     MG  A 202       1
HET    7PQ  A 203      29
HET    GSH  B1201      20
HETNAM     GSH GLUTATHIONE
HETNAM      MG MAGNESIUM ION
HETNAM     7PQ 4-[2-(AMINOMETHYL)NAPHTHALEN-1-YL]-N-[2-(MORPHOLIN-4-
HETNAM   2 7PQ  YL)ETHYL]BENZAMIDE
FORMUL   3  GSH    2(C10 H17 N3 O6 S)
FORMUL   4   MG    MG 2+
FORMUL   5  7PQ    C24 H27 N3 O2
FORMUL   7  HOH   *761(H2 O)
HELIX    1   1 ALA A   15  ASP A   26  1                                  12
HELIX    2   2 ASP A   38  LYS A   43  1                                   6
HELIX    3   3 SER A   44  LEU A   46  5                                   3
HELIX    4   4 GLN A   63  LYS A   73  1                                  11
HELIX    5   5 THR A   81  CYS A  101  1                                  21
HELIX    6   6 LYS A  108  TYR A  122  1                                  15
HELIX    7   7 TYR A  122  GLY A  136  1                                  15
HELIX    8   8 THR A  147  LYS A  164  1                                  18
HELIX    9   9 HIS A  171  ALA A  183  1                                  13
HELIX   10  10 ILE A  184  ARG A  194  1                                  11
HELIX   11  11 ALA B 1015  LEU B 1025  1                                  11
HELIX   12  12 GLU B 1035  ALA B 1037  5                                   3
HELIX   13  13 ASP B 1038  THR B 1045  1                                   8
HELIX   14  14 GLN B 1063  LYS B 1073  1                                  11
HELIX   15  15 THR B 1081  SER B 1100  1                                  20
HELIX   16  16 LYS B 1108  ASN B 1123  1                                  16
HELIX   17  17 ASN B 1123  GLY B 1136  1                                  14
HELIX   18  18 THR B 1147  LYS B 1164  1                                  18
HELIX   19  19 HIS B 1171  ILE B 1184  1                                  14
HELIX   20  20 ILE B 1184  ARG B 1194  1                                  11
SHEET    1   A 4 GLU A  30  ARG A  33  0
SHEET    2   A 4 TYR A   4  TYR A   8  1  N  TYR A   4   O  GLU A  30
SHEET    3   A 4 ILE A  53  VAL A  56 -1  O  GLU A  55   N  LYS A   5
SHEET    4   A 4 LEU A  59  HIS A  62 -1  O  LEU A  59   N  VAL A  56
SHEET    1   B 4 GLU B1030  ILE B1034  0
SHEET    2   B 4 TYR B1004  PHE B1009  1  N  LEU B1006   O  GLU B1030
SHEET    3   B 4 ILE B1053  VAL B1056 -1  O  GLU B1055   N  LYS B1005
SHEET    4   B 4 LEU B1059  HIS B1062 -1  O  LEU B1059   N  VAL B1056
LINK        MG    MG A 202                 O   HOH B1437     1555   1555  2.26
LINK        MG    MG A 202                 O   HOH A 459     1555   1555  2.28
LINK        MG    MG A 202                 O   HOH A 412     1555   1555  2.30
LINK        MG    MG A 202                 O   HOH B1372     1555   1555  2.34
LINK        MG    MG A 202                 O   HOH A 423     1555   1555  2.36
LINK        MG    MG A 202                 O   HOH B1384     1555   1555  2.39
CISPEP   1 ILE A   51    PRO A   52          0         0.80
CISPEP   2 ILE B 1051    PRO B 1052          0         0.76
SITE     1 AC1 17 TYR A   8  ARG A  14  TRP A  39  LYS A  43
SITE     2 AC1 17 LYS A  50  ILE A  51  PRO A  52  GLN A  63
SITE     3 AC1 17 SER A  64  7PQ A 203  HOH A 301  HOH A 402
SITE     4 AC1 17 HOH A 464  HOH A 472  HOH A 652  HOH A 684
SITE     5 AC1 17 ASP B1097
SITE     1 AC2  6 HOH A 412  HOH A 423  HOH A 459  HOH B1372
SITE     2 AC2  6 HOH B1384  HOH B1437
SITE     1 AC3 11 TYR A   8  GLY A  13  ARG A  14  ASP A  96
SITE     2 AC3 11 MET A  99  TRP A 104  TYR A 152  THR A 159
SITE     3 AC3 11 LEU A 199  GSH A 201  HOH A 461
SITE     1 AC4 15 ASP A  97  TYR B1008  ARG B1014  TRP B1039
SITE     2 AC4 15 LYS B1043  LYS B1050  ILE B1051  GLN B1063
SITE     3 AC4 15 SER B1064  HOH B1309  HOH B1353  HOH B1404
SITE     4 AC4 15 HOH B1430  HOH B1438  HOH B1649
CRYST1   48.740   77.706   52.449  90.00  91.56  90.00 P 1 21 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      0.020517  0.000000  0.000559        0.00000
SCALE2      0.000000  0.012869  0.000000        0.00000
SCALE3      0.000000  0.000000  0.019073        0.00000
      
PROCHECK
Go to PROCHECK summary
 References