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PDBsum entry 1dug

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Transferase, blood clotting PDB id
1dug
Jmol
Contents
Protein chains
234 a.a. *
Ligands
GSH ×2
Waters ×662
* Residue conservation analysis
HEADER    TRANSFERASE, BLOOD CLOTTING             17-JAN-00   1DUG
TITLE     STRUCTURE OF THE FIBRINOGEN G CHAIN INTEGRIN BINDING AND
TITLE    2 FACTOR XIIIA CROSSLINKING SITES OBTAINED THROUGH CARRIER
TITLE    3 PROTEIN DRIVEN CRYSTALLIZATION
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CHIMERA OF GLUTATHIONE S-TRANSFERASE-SYNTHETIC
COMPND   3 LINKER-C-TERMINAL FIBRINOGEN GAMMA CHAIN;
COMPND   4 CHAIN: A, B;
COMPND   5 EC: 2.5.1.18;
COMPND   6 ENGINEERED: YES;
COMPND   7 OTHER_DETAILS: GLUTATHIONE S-TRANSFERASE (RESIDUES 1-217)
COMPND   8 BOUND TO SYNTHETIC SDP LINKER (RESIDUES 218-220) BOUND TO
COMPND   9 C-TERMINAL FIBRINOGEN GAMMA CHAIN (RESIDUES 221-234)
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: SCHISTOSOMA JAPONICUM;
SOURCE   3 ORGANISM_TAXID: 6182;
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: DH5ALPHA;
SOURCE   7 OTHER_DETAILS: EUKARYOTA; METAZOA; PLATYHELMINTHES;
SOURCE   8 TREMATODA; DIGENEA; STRIGEIDIDA; SCHISTOSOMATOIDEA;
SOURCE   9 SCHISTOSOMATIDAE; SCHISTOSOMA
KEYWDS    GAMMA CHAIN INTEGRIN FRAGMENT, CARRIER PROTEIN DRIVEN
KEYWDS   2 CRYSTALLIZATION, TRANSFERASE, BLOOD CLOTTING
EXPDTA    X-RAY DIFFRACTION
AUTHOR    S.WARE,J.P.DONAHUE,J.HAWIGER,W.F.ANDERSON
REVDAT   3   24-FEB-09 1DUG    1       VERSN
REVDAT   2   01-APR-03 1DUG    1       JRNL
REVDAT   1   02-FEB-00 1DUG    0
JRNL        AUTH   S.WARE,J.P.DONAHUE,J.HAWIGER,W.F.ANDERSON
JRNL        TITL   STRUCTURE OF THE FIBRINOGEN GAMMA-CHAIN INTEGRIN
JRNL        TITL 2 BINDING AND FACTOR XIIIA CROSS-LINKING SITES
JRNL        TITL 3 OBTAINED THROUGH CARRIER PROTEIN DRIVEN
JRNL        TITL 4 CRYSTALLIZATION.
JRNL        REF    PROTEIN SCI.                  V.   8  2663 1999
JRNL        REFN                   ISSN 0961-8368
JRNL        PMID   10631982
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    1.80 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) : 1.80
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 89.2
REMARK   3   NUMBER OF REFLECTIONS             : 57456
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE            (WORKING SET) : 0.185
REMARK   3   FREE R VALUE                     : 0.226
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : 5745
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            : 3818
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 40
REMARK   3   SOLVENT ATOMS            : 662
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL
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) : 0.007
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 1DUG COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-JAN-00.
REMARK 100 THE RCSB ID CODE IS RCSB010378.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 15-MAR-97
REMARK 200  TEMPERATURE           (KELVIN) : 100.0
REMARK 200  PH                             : 4.6
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : NSLS
REMARK 200  BEAMLINE                       : X4A
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0093
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : FUJI
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 67736
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700
REMARK 200  RESOLUTION RANGE LOW       (A) : 28.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 89.2
REMARK 200  DATA REDUNDANCY                : 5.560
REMARK 200  R MERGE                    (I) : 0.05400
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) : 1.80
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.00
REMARK 200  COMPLETENESS FOR SHELL     (%) : 66.1
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.25000
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: NULL
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 65.21
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.54
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, SODIUM ACETATE, SODIUM
REMARK 280  CHLORIDE, AMMONIUM SULFATE, TRIS, REDUCED GLUTATHIONE, PH 4.6,
REMARK 280  VAPOR DIFFUSION, HANGING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z+1/2
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4
REMARK 290       7555   Y,X,-Z
REMARK 290       8555   -Y,-X,-Z+1/2
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       68.61500
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       52.89000
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       52.89000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       34.30750
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       52.89000
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       52.89000
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      102.92250
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       52.89000
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       52.89000
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       34.30750
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       52.89000
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       52.89000
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      102.92250
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       68.61500
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: 4060 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20300 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE
REMARK 500   O    PRO A   220     OE1  GLU B    24     5555     2.18
REMARK 500
REMARK 500 REMARK: NULL
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  66      106.77     84.74
REMARK 500    GLN A 203     -167.43   -120.94
REMARK 500    SER A 218      -50.28     67.58
REMARK 500    GLN A 222      111.17    166.99
REMARK 500    HIS A 223     -155.37   -113.57
REMARK 500    GLN A 230      -85.86    -71.26
REMARK 500    ALA A 231      -70.87   -176.93
REMARK 500    ASP A 233      -92.96   -164.28
REMARK 500    LYS B  10      -72.11    -71.95
REMARK 500    ASP B  59     -158.72   -137.99
REMARK 500    VAL B  62      115.63   -164.87
REMARK 500    GLN B  66      106.24     84.68
REMARK 500    ASP B 113       54.00   -102.56
REMARK 500    ASN B 143       15.99     85.02
REMARK 500    GLN B 203     -167.78   -117.12
REMARK 500    PRO B 216     -114.97    -67.14
REMARK 500    ASP B 219      -50.89   -146.81
REMARK 500    PRO B 220       75.78    -57.36
REMARK 500    GLN B 222      100.82   -167.55
REMARK 500    HIS B 224       92.30     57.80
REMARK 500    LEU B 225     -148.99   -160.73
REMARK 500    GLN B 230       39.90    -82.39
REMARK 500    ALA B 231      -87.14     67.27
REMARK 500    ASP B 233      -20.80   -166.85
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 B1646        DISTANCE =  5.16 ANGSTROMS
REMARK 525    HOH A1433        DISTANCE =  5.07 ANGSTROMS
REMARK 525    HOH A1439        DISTANCE =  5.81 ANGSTROMS
REMARK 525    HOH B1813        DISTANCE =  6.87 ANGSTROMS
REMARK 525    HOH B1823        DISTANCE =  6.47 ANGSTROMS
REMARK 525    HOH B1841        DISTANCE =  6.35 ANGSTROMS
REMARK 525    HOH A1526        DISTANCE =  7.27 ANGSTROMS
REMARK 525    HOH B1876        DISTANCE =  6.14 ANGSTROMS
REMARK 525    HOH B1883        DISTANCE =  6.87 ANGSTROMS
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 1239
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GSH B 1587
DBREF  1DUG A    1   217  UNP    P08515   GT26_SCHJA       2    218
DBREF  1DUG A  221   234  UNP    P02679   FIBG_HUMAN     424    437
DBREF  1DUG B    1   217  UNP    P08515   GT26_SCHJA       2    218
DBREF  1DUG B  221   234  UNP    P02679   FIBG_HUMAN     424    437
SEQADV 1DUG SER A  218  UNP  P08515              LINKER
SEQADV 1DUG ASP A  219  UNP  P08515              LINKER
SEQADV 1DUG PRO A  220  UNP  P08515              LINKER
SEQADV 1DUG SER B  218  UNP  P08515              LINKER
SEQADV 1DUG ASP B  219  UNP  P08515              LINKER
SEQADV 1DUG PRO B  220  UNP  P08515              LINKER
SEQRES   1 A  234  SER PRO ILE LEU GLY TYR TRP LYS ILE LYS GLY LEU VAL
SEQRES   2 A  234  GLN PRO THR ARG LEU LEU LEU GLU TYR LEU GLU GLU LYS
SEQRES   3 A  234  TYR GLU GLU HIS LEU TYR GLU ARG ASP GLU GLY ASP LYS
SEQRES   4 A  234  TRP ARG ASN LYS LYS PHE GLU LEU GLY LEU GLU PHE PRO
SEQRES   5 A  234  ASN LEU PRO TYR TYR ILE ASP GLY ASP VAL LYS LEU THR
SEQRES   6 A  234  GLN SER MET ALA ILE ILE ARG TYR ILE ALA ASP LYS HIS
SEQRES   7 A  234  ASN MET LEU GLY GLY CYS PRO LYS GLU ARG ALA GLU ILE
SEQRES   8 A  234  SER MET LEU GLU GLY ALA VAL LEU ASP ILE ARG TYR GLY
SEQRES   9 A  234  VAL SER ARG ILE ALA TYR SER LYS ASP PHE GLU THR LEU
SEQRES  10 A  234  LYS VAL ASP PHE LEU SER LYS LEU PRO GLU MET LEU LYS
SEQRES  11 A  234  MET PHE GLU ASP ARG LEU CYS HIS LYS THR TYR LEU ASN
SEQRES  12 A  234  GLY ASP HIS VAL THR HIS PRO ASP PHE MET LEU TYR ASP
SEQRES  13 A  234  ALA LEU ASP VAL VAL LEU TYR MET ASP PRO MET CYS LEU
SEQRES  14 A  234  ASP ALA PHE PRO LYS LEU VAL CYS PHE LYS LYS ARG ILE
SEQRES  15 A  234  GLU ALA ILE PRO GLN ILE ASP LYS TYR LEU LYS SER SER
SEQRES  16 A  234  LYS TYR ILE ALA TRP PRO LEU GLN GLY TRP GLN ALA THR
SEQRES  17 A  234  PHE GLY GLY GLY ASP HIS PRO PRO LYS SER ASP PRO GLN
SEQRES  18 A  234  GLN HIS HIS LEU GLY GLY ALA LYS GLN ALA GLY ASP VAL
SEQRES   1 B  234  SER PRO ILE LEU GLY TYR TRP LYS ILE LYS GLY LEU VAL
SEQRES   2 B  234  GLN PRO THR ARG LEU LEU LEU GLU TYR LEU GLU GLU LYS
SEQRES   3 B  234  TYR GLU GLU HIS LEU TYR GLU ARG ASP GLU GLY ASP LYS
SEQRES   4 B  234  TRP ARG ASN LYS LYS PHE GLU LEU GLY LEU GLU PHE PRO
SEQRES   5 B  234  ASN LEU PRO TYR TYR ILE ASP GLY ASP VAL LYS LEU THR
SEQRES   6 B  234  GLN SER MET ALA ILE ILE ARG TYR ILE ALA ASP LYS HIS
SEQRES   7 B  234  ASN MET LEU GLY GLY CYS PRO LYS GLU ARG ALA GLU ILE
SEQRES   8 B  234  SER MET LEU GLU GLY ALA VAL LEU ASP ILE ARG TYR GLY
SEQRES   9 B  234  VAL SER ARG ILE ALA TYR SER LYS ASP PHE GLU THR LEU
SEQRES  10 B  234  LYS VAL ASP PHE LEU SER LYS LEU PRO GLU MET LEU LYS
SEQRES  11 B  234  MET PHE GLU ASP ARG LEU CYS HIS LYS THR TYR LEU ASN
SEQRES  12 B  234  GLY ASP HIS VAL THR HIS PRO ASP PHE MET LEU TYR ASP
SEQRES  13 B  234  ALA LEU ASP VAL VAL LEU TYR MET ASP PRO MET CYS LEU
SEQRES  14 B  234  ASP ALA PHE PRO LYS LEU VAL CYS PHE LYS LYS ARG ILE
SEQRES  15 B  234  GLU ALA ILE PRO GLN ILE ASP LYS TYR LEU LYS SER SER
SEQRES  16 B  234  LYS TYR ILE ALA TRP PRO LEU GLN GLY TRP GLN ALA THR
SEQRES  17 B  234  PHE GLY GLY GLY ASP HIS PRO PRO LYS SER ASP PRO GLN
SEQRES  18 B  234  GLN HIS HIS LEU GLY GLY ALA LYS GLN ALA GLY ASP VAL
HET    GSH  A1239      20
HET    GSH  B1587      20
HETNAM     GSH GLUTATHIONE
FORMUL   3  GSH    2(C10 H17 N3 O6 S)
FORMUL   5  HOH   *662(H2 O)
HELIX    1   1 LYS A   10  LEU A   12  5                                   3
HELIX    2   2 VAL A   13  GLU A   24  1                                  12
HELIX    3   3 GLU A   36  LYS A   44  1                                   9
HELIX    4   4 GLN A   66  HIS A   78  1                                  13
HELIX    5   5 CYS A   84  TYR A  110  1                                  27
HELIX    6   6 ASP A  113  LEU A  136  1                                  24
HELIX    7   7 THR A  148  ASP A  165  1                                  18
HELIX    8   8 PHE A  172  ILE A  185  1                                  14
HELIX    9   9 ILE A  185  LYS A  193  1                                   9
HELIX   10  10 LYS B   10  LEU B   12  5                                   3
HELIX   11  11 VAL B   13  LEU B   23  1                                  11
HELIX   12  12 GLU B   36  LYS B   44  1                                   9
HELIX   13  13 GLN B   66  HIS B   78  1                                  13
HELIX   14  14 CYS B   84  TYR B  110  1                                  27
HELIX   15  15 ASP B  113  LEU B  136  1                                  24
HELIX   16  16 THR B  148  ASP B  165  1                                  18
HELIX   17  17 PHE B  172  ILE B  185  1                                  14
HELIX   18  18 ILE B  185  LYS B  193  1                                   9
SHEET    1   A 4 GLU A  28  TYR A  32  0
SHEET    2   A 4 ILE A   3  TRP A   7  1  N  LEU A   4   O  GLU A  28
SHEET    3   A 4 TYR A  56  ILE A  58 -1  O  TYR A  56   N  GLY A   5
SHEET    4   A 4 LYS A  63  THR A  65 -1  N  LEU A  64   O  TYR A  57
SHEET    1   B 4 GLU B  28  TYR B  32  0
SHEET    2   B 4 ILE B   3  TRP B   7  1  N  LEU B   4   O  GLU B  28
SHEET    3   B 4 TYR B  56  ASP B  59 -1  O  TYR B  56   N  GLY B   5
SHEET    4   B 4 VAL B  62  THR B  65 -1  O  VAL B  62   N  ASP B  59
CISPEP   1 LEU A   54    PRO A   55          0        -0.19
CISPEP   2 TRP A  200    PRO A  201          0         0.77
CISPEP   3 LEU B   54    PRO B   55          0         0.47
CISPEP   4 TRP B  200    PRO B  201          0        -0.60
SITE     1 AC1 20 TYR A   6  TRP A   7  LEU A  12  TRP A  40
SITE     2 AC1 20 LYS A  44  ASN A  53  LEU A  54  PRO A  55
SITE     3 AC1 20 GLN A  66  SER A  67  HOH A1243  HOH A1244
SITE     4 AC1 20 HOH A1258  HOH A1352  HOH A1363  HOH A1529
SITE     5 AC1 20 HOH A1545  ASP B 100  HOH B1689  HOH B1711
SITE     1 AC2 19 ASP A 100  HOH A1249  TYR B   6  TRP B   7
SITE     2 AC2 19 LEU B  12  TRP B  40  LYS B  44  ASN B  53
SITE     3 AC2 19 LEU B  54  PRO B  55  GLN B  66  SER B  67
SITE     4 AC2 19 HOH B1588  HOH B1590  HOH B1605  HOH B1728
SITE     5 AC2 19 HOH B1829  HOH B1833  HOH B1840
CRYST1  105.780  105.780  137.230  90.00  90.00  90.00 P 41 21 2    16
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      0.009454  0.000000  0.000000        0.00000
SCALE2      0.000000  0.009454  0.000000        0.00000
SCALE3      0.000000  0.000000  0.007287        0.00000
      
PROCHECK
Go to PROCHECK summary
 References