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PDBsum entry 1grh

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Oxidoreductase PDB id
1grh
Jmol
Contents
Protein chain
461 a.a.
Ligands
PO4
FAD
EOH
Waters ×520
HEADER    OXIDOREDUCTASE                          15-DEC-92   1GRH
TITLE     INHIBITION OF HUMAN GLUTATHIONE REDUCTASE BY THE NITROSOUREA DRUGS 1,
TITLE    2 3-BIS(2-CHLOROETHYL)-1-NITROSOUREA AND 1-(2-CHLOROETHYL)-3-(2-
TITLE    3 HYDROXYETHYL)-1-NITROSOUREA
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: GLUTATHIONE REDUCTASE;
COMPND   3 CHAIN: A;
COMPND   4 EC: 1.6.4.2;
COMPND   5 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606
KEYWDS    OXIDOREDUCTASE, FLAVOENZYME
EXPDTA    X-RAY DIFFRACTION
AUTHOR    P.A.KARPLUS,G.E.SCHULZ
REVDAT   5   27-JUL-11 1GRH    1       ATOM   DBREF  REMARK REVDAT
REVDAT   5 2                   1       SEQRES
REVDAT   4   13-JUL-11 1GRH    1       VERSN
REVDAT   3   24-FEB-09 1GRH    1       VERSN
REVDAT   2   01-APR-03 1GRH    1       JRNL
REVDAT   1   31-JAN-94 1GRH    0
JRNL        AUTH   P.A.KARPLUS,R.L.KRAUTH-SIEGEL,R.H.SCHIRMER,G.E.SCHULZ
JRNL        TITL   INHIBITION OF HUMAN GLUTATHIONE REDUCTASE BY THE NITROSOUREA
JRNL        TITL 2 DRUGS 1,3-BIS(2-CHLOROETHYL)-1-NITROSOUREA AND
JRNL        TITL 3 1-(2-CHLOROETHYL)-3-(2-HYDROXYETHYL)-1-NITROSOUREA. A
JRNL        TITL 4 CRYSTALLOGRAPHIC ANALYSIS.
JRNL        REF    EUR.J.BIOCHEM.                V. 171   193 1988
JRNL        REFN                   ISSN 0014-2956
JRNL        PMID   3338461
JRNL        DOI    10.1111/J.1432-1033.1988.TB13775.X
REMARK   2
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : NULL
REMARK   3   AUTHORS     : NULL
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : NULL
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             : NULL
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) : NULL
REMARK   3   FREE R VALUE                     : NULL
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            : 3499
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 61
REMARK   3   SOLVENT ATOMS            : 520
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) : 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: IN AN ADDITIONAL EXPERIMENT THE REDUCED
REMARK   3  ENZYME WAS REACTED WITH HECNU IN SOLUTION AND THEN CRYSTALLIZED.
REMARK   3  DATA WERE COLLECTED TO ONLY 3.0 ANGSTROM RESOLUTION. THE MODIFIED
REMARK   3  ENZYME WAS ANALYZED USING A DIFFERENCE FOURIER MAP WITHOUT
REMARK   3  REFINEMENT. THE COORDINATES OF THE RESULTING MODEL OF THE
REMARK   3  MODIFIED AMINO ACID RESIDUE CYS 58 (HECN-482) WERE INITIALLY
REMARK   3  GIVEN IN THIS ENTRY. IN ORDER TO BRING COMPLETENESS TO THE
REMARK   3  STRUCTURE, THE ENTRY HAS BEEN REMEDIATED BY MERGING THE
REMARK   3  COORDINATES OF THE ENTIRE MOLECULE FROM THE PDB ENTRY 1GRG, APART
REMARK   3  FROM THE COORDINATES OF RESIDUE 0A8 AND SUBSTITUTING IT BY THE
REMARK   3  COORDINATES OF CYS AND ETHANOL PRESENT IN THIS ENTRY.
REMARK   4
REMARK   4 1GRH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
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        : NULL
REMARK 200  TEMPERATURE           (KELVIN) : NULL
REMARK 200  PH                             : NULL
REMARK 200  NUMBER OF CRYSTALS USED        : NULL
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : NULL
REMARK 200  RADIATION SOURCE               : NULL
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : NULL
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   : NULL
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : NULL
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) : 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: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 53.51
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: B 2
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,Z+1/2
REMARK 290       4555   -X+1/2,-Y,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        0.00000
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       59.90000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       31.60000
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       59.90000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       31.60000
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10570 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 36820 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -73.4 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 350   BIOMT1   2 -1.000000  0.000000  0.000000      163.69936
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000       72.20177
REMARK 350   BIOMT3   2  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     ALA A     1
REMARK 465     CYS A     2
REMARK 465     ARG A     3
REMARK 465     GLN A     4
REMARK 465     GLU A     5
REMARK 465     PRO A     6
REMARK 465     GLN A     7
REMARK 465     PRO A     8
REMARK 465     GLN A     9
REMARK 465     GLY A    10
REMARK 465     PRO A    11
REMARK 465     PRO A    12
REMARK 465     PRO A    13
REMARK 465     ALA A    14
REMARK 465     ALA A    15
REMARK 465     GLY A    16
REMARK 465     ALA A    17
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    HOH A   585     O    HOH A   585     2665     0.64
REMARK 500   SG   CYS A    90     SG   CYS A    90     2665     1.56
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION
REMARK 500    THR A  57   C     CYS A  58   N      -0.193
REMARK 500    CYS A  58   C     VAL A  59   N       0.172
REMARK 500    GLU A  91   CD    GLU A  91   OE2     0.072
REMARK 500    GLU A 101   CD    GLU A 101   OE2     0.073
REMARK 500    GLU A 124   CD    GLU A 124   OE1     0.079
REMARK 500    GLU A 185   CD    GLU A 185   OE1     0.084
REMARK 500    GLU A 317   CD    GLU A 317   OE1     0.071
REMARK 500    GLU A 358   CD    GLU A 358   OE2     0.075
REMARK 500    GLU A 394   CD    GLU A 394   OE1     0.067
REMARK 500    GLU A 427   CD    GLU A 427   OE1     0.075
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500    ASP A  22   CB  -  CG  -  OD1 ANGL. DEV. =  -6.3 DEGREES
REMARK 500    ASP A  22   CB  -  CG  -  OD2 ANGL. DEV. =   5.4 DEGREES
REMARK 500    GLY A  92   N   -  CA  -  C   ANGL. DEV. =  15.5 DEGREES
REMARK 500    GLY A  92   C   -  N   -  CA  ANGL. DEV. = -23.0 DEGREES
REMARK 500    ARG A  97   NE  -  CZ  -  NH2 ANGL. DEV. =   3.7 DEGREES
REMARK 500    ASP A 104   CB  -  CG  -  OD1 ANGL. DEV. =   7.1 DEGREES
REMARK 500    ASP A 104   CB  -  CG  -  OD2 ANGL. DEV. =  -7.0 DEGREES
REMARK 500    ASP A 135   CB  -  CG  -  OD1 ANGL. DEV. =  -5.8 DEGREES
REMARK 500    MET A 159   CB  -  CA  -  C   ANGL. DEV. = -15.1 DEGREES
REMARK 500    MET A 159   CA  -  CB  -  CG  ANGL. DEV. =  12.3 DEGREES
REMARK 500    ASP A 178   CB  -  CG  -  OD2 ANGL. DEV. =  -5.7 DEGREES
REMARK 500    ASP A 283   CB  -  CG  -  OD1 ANGL. DEV. =  -7.3 DEGREES
REMARK 500    ARG A 291   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.9 DEGREES
REMARK 500    ASP A 297   CB  -  CG  -  OD2 ANGL. DEV. =  -5.8 DEGREES
REMARK 500    ASP A 308   CB  -  CG  -  OD1 ANGL. DEV. =   7.1 DEGREES
REMARK 500    ASP A 308   CB  -  CG  -  OD2 ANGL. DEV. =  -6.4 DEGREES
REMARK 500    ASP A 309   CB  -  CG  -  OD2 ANGL. DEV. =  -7.0 DEGREES
REMARK 500    ARG A 352   NE  -  CZ  -  NH2 ANGL. DEV. =   3.5 DEGREES
REMARK 500    ASP A 359   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES
REMARK 500    ASP A 385   CB  -  CG  -  OD1 ANGL. DEV. =  -6.2 DEGREES
REMARK 500    ASP A 441   CB  -  CG  -  OD1 ANGL. DEV. =   5.4 DEGREES
REMARK 500    ASP A 459   CB  -  CG  -  OD2 ANGL. DEV. =  -5.6 DEGREES
REMARK 500    ASP A 461   CB  -  CG  -  OD2 ANGL. DEV. =  -6.8 DEGREES
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    HIS A  52     -118.77   -121.45
REMARK 500    PRO A 136      -72.27    -58.44
REMARK 500    HIS A 219     -146.80   -117.48
REMARK 500    ALA A 336       74.22     51.44
REMARK 500    ASN A 425      177.92     64.85
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS
REMARK 500    ARG A  97        15.6      L          L   OUTSIDE RANGE
REMARK 500    ASP A 309        24.8      L          L   OUTSIDE RANGE
REMARK 500    LYS A 335        23.8      L          L   OUTSIDE RANGE
REMARK 500    GLN A 445        23.5      L          L   OUTSIDE RANGE
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 646        DISTANCE =  7.27 ANGSTROMS
REMARK 525    HOH A 699        DISTANCE =  6.65 ANGSTROMS
REMARK 525    HOH A 712        DISTANCE =  5.51 ANGSTROMS
REMARK 525    HOH A 714        DISTANCE =  5.68 ANGSTROMS
REMARK 525    HOH A 751        DISTANCE =  5.10 ANGSTROMS
REMARK 525    HOH A 784        DISTANCE =  5.53 ANGSTROMS
REMARK 525    HOH A 825        DISTANCE =  5.09 ANGSTROMS
REMARK 525    HOH A 849        DISTANCE =  5.38 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 480
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A 479
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EOH A 482
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1GRG   RELATED DB: PDB
DBREF  1GRH A    1   478  UNP    P00390   GSHR_HUMAN       1    478
SEQRES   1 A  478  ALA CYS ARG GLN GLU PRO GLN PRO GLN GLY PRO PRO PRO
SEQRES   2 A  478  ALA ALA GLY ALA VAL ALA SER TYR ASP TYR LEU VAL ILE
SEQRES   3 A  478  GLY GLY GLY SER GLY GLY LEU ALA SER ALA ARG ARG ALA
SEQRES   4 A  478  ALA GLU LEU GLY ALA ARG ALA ALA VAL VAL GLU SER HIS
SEQRES   5 A  478  LYS LEU GLY GLY THR CYS VAL ASN VAL GLY CYS VAL PRO
SEQRES   6 A  478  LYS LYS VAL MET TRP ASN THR ALA VAL HIS SER GLU PHE
SEQRES   7 A  478  MET HIS ASP HIS ALA ASP TYR GLY PHE PRO SER CYS GLU
SEQRES   8 A  478  GLY LYS PHE ASN TRP ARG VAL ILE LYS GLU LYS ARG ASP
SEQRES   9 A  478  ALA TYR VAL SER ARG LEU ASN ALA ILE TYR GLN ASN ASN
SEQRES  10 A  478  LEU THR LYS SER HIS ILE GLU ILE ILE ARG GLY HIS ALA
SEQRES  11 A  478  ALA PHE THR SER ASP PRO LYS PRO THR ILE GLU VAL SER
SEQRES  12 A  478  GLY LYS LYS TYR THR ALA PRO HIS ILE LEU ILE ALA THR
SEQRES  13 A  478  GLY GLY MET PRO SER THR PRO HIS GLU SER GLN ILE PRO
SEQRES  14 A  478  GLY ALA SER LEU GLY ILE THR SER ASP GLY PHE PHE GLN
SEQRES  15 A  478  LEU GLU GLU LEU PRO GLY ARG SER VAL ILE VAL GLY ALA
SEQRES  16 A  478  GLY TYR ILE ALA VAL GLU MET ALA GLY ILE LEU SER ALA
SEQRES  17 A  478  LEU GLY SER LYS THR SER LEU MET ILE ARG HIS ASP LYS
SEQRES  18 A  478  VAL LEU ARG SER PHE ASP SER MET ILE SER THR ASN CYS
SEQRES  19 A  478  THR GLU GLU LEU GLU ASN ALA GLY VAL GLU VAL LEU LYS
SEQRES  20 A  478  PHE SER GLN VAL LYS GLU VAL LYS LYS THR LEU SER GLY
SEQRES  21 A  478  LEU GLU VAL SER MET VAL THR ALA VAL PRO GLY ARG LEU
SEQRES  22 A  478  PRO VAL MET THR MET ILE PRO ASP VAL ASP CYS LEU LEU
SEQRES  23 A  478  TRP ALA ILE GLY ARG VAL PRO ASN THR LYS ASP LEU SER
SEQRES  24 A  478  LEU ASN LYS LEU GLY ILE GLN THR ASP ASP LYS GLY HIS
SEQRES  25 A  478  ILE ILE VAL ASP GLU PHE GLN ASN THR ASN VAL LYS GLY
SEQRES  26 A  478  ILE TYR ALA VAL GLY ASP VAL CYS GLY LYS ALA LEU LEU
SEQRES  27 A  478  THR PRO VAL ALA ILE ALA ALA GLY ARG LYS LEU ALA HIS
SEQRES  28 A  478  ARG LEU PHE GLU TYR LYS GLU ASP SER LYS LEU ASP TYR
SEQRES  29 A  478  ASN ASN ILE PRO THR VAL VAL PHE SER HIS PRO PRO ILE
SEQRES  30 A  478  GLY THR VAL GLY LEU THR GLU ASP GLU ALA ILE HIS LYS
SEQRES  31 A  478  TYR GLY ILE GLU ASN VAL LYS THR TYR SER THR SER PHE
SEQRES  32 A  478  THR PRO MET TYR HIS ALA VAL THR LYS ARG LYS THR LYS
SEQRES  33 A  478  CYS VAL MET LYS MET VAL CYS ALA ASN LYS GLU GLU LYS
SEQRES  34 A  478  VAL VAL GLY ILE HIS MET GLN GLY LEU GLY CYS ASP GLU
SEQRES  35 A  478  MET LEU GLN GLY PHE ALA VAL ALA VAL LYS MET GLY ALA
SEQRES  36 A  478  THR LYS ALA ASP PHE ASP ASN THR VAL ALA ILE HIS PRO
SEQRES  37 A  478  THR SER SER GLU GLU LEU VAL THR LEU ARG
HET    PO4  A 480       5
HET    FAD  A 479      53
HET    EOH  A 482       3
HETNAM     PO4 PHOSPHATE ION
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE
HETNAM     EOH ETHANOL
FORMUL   2  PO4    O4 P 3-
FORMUL   3  FAD    C27 H33 N9 O15 P2
FORMUL   4  EOH    C2 H6 O
FORMUL   5  HOH   *520(H2 O)
HELIX    1   1 GLY A   29  LEU A   42  1                                  14
HELIX    2   2 GLY A   55  VAL A   61  1                                   7
HELIX    3   3 GLY A   62  HIS A   80  1                                  19
HELIX    4   4 ASP A   81  GLY A   86  5                                   6
HELIX    5   5 ASN A   95  SER A  121  1                                  27
HELIX    6   6 GLY A  170  GLY A  174  5                                   5
HELIX    7   7 THR A  176  PHE A  181  1                                   6
HELIX    8   8 GLY A  196  LEU A  209  1                                  14
HELIX    9   9 ASP A  227  ALA A  241  1                                  15
HELIX   10  10 SER A  299  LEU A  303  5                                   5
HELIX   11  11 GLY A  330  GLY A  334  5                                   5
HELIX   12  12 LEU A  338  GLU A  355  1                                  18
HELIX   13  13 THR A  383  GLY A  392  1                                  10
HELIX   14  14 PRO A  405  THR A  411  5                                   7
HELIX   15  15 GLY A  439  MET A  453  1                                  15
HELIX   16  16 THR A  456  ASN A  462  1                                   7
HELIX   17  17 SER A  470  THR A  476  5                                   7
SHEET    1  AA 4 ALA A  19  SER A  20  0
SHEET    2  AA 4 LYS A 145  THR A 148  1  O  LYS A 146   N  ALA A  19
SHEET    3  AA 4 THR A 139  VAL A 142 -1  O  ILE A 140   N  TYR A 147
SHEET    4  AA 4 ALA A 131  PHE A 132 -1  O  ALA A 131   N  GLU A 141
SHEET    1  AB 5 GLU A 124  ARG A 127  0
SHEET    2  AB 5 ALA A  46  GLU A  50  1  O  ALA A  46   N  GLU A 124
SHEET    3  AB 5 TYR A  23  ILE A  26  1  O  TYR A  23   N  ALA A  47
SHEET    4  AB 5 ILE A 152  ILE A 154  1  O  LEU A 153   N  ILE A  26
SHEET    5  AB 5 ILE A 326  ALA A 328  1  O  TYR A 327   N  ILE A 154
SHEET    1  AC 2 GLY A 158  PRO A 160  0
SHEET    2  AC 2 ARG A 291  PRO A 293 -1  O  VAL A 292   N  MET A 159
SHEET    1  AD 4 GLU A 244  LEU A 246  0
SHEET    2  AD 4 LYS A 212  MET A 216  1  O  THR A 213   N  GLU A 244
SHEET    3  AD 4 ARG A 189  VAL A 193  1  O  SER A 190   N  SER A 214
SHEET    4  AD 4 CYS A 284  TRP A 287  1  O  CYS A 284   N  VAL A 191
SHEET    1  AE 3 SER A 249  THR A 257  0
SHEET    2  AE 3 GLY A 260  THR A 267 -1  O  GLY A 260   N  THR A 257
SHEET    3  AE 3 VAL A 275  VAL A 282 -1  O  VAL A 275   N  THR A 267
SHEET    1  AF 5 THR A 369  VAL A 371  0
SHEET    2  AF 5 ILE A 377  GLY A 381 -1  O  ILE A 377   N  VAL A 371
SHEET    3  AF 5 LYS A 429  GLN A 436 -1  O  ILE A 433   N  VAL A 380
SHEET    4  AF 5 CYS A 417  ALA A 424 -1  O  VAL A 418   N  GLN A 436
SHEET    5  AF 5 VAL A 396  PHE A 403 -1  O  LYS A 397   N  CYS A 423
LINK         SG  CYS A  58                 C2  EOH A 482     1555   1555  1.81
CISPEP   1 HIS A  374    PRO A  375          0        -1.76
CISPEP   2 HIS A  467    PRO A  468          0        -3.89
SITE     1 AC1  5 HIS A 219  ARG A 224  HOH A 505  HOH A 575
SITE     2 AC1  5 HOH A 600
SITE     1 AC2 38 GLY A  27  GLY A  29  SER A  30  GLY A  31
SITE     2 AC2 38 GLU A  50  SER A  51  HIS A  52  GLY A  56
SITE     3 AC2 38 THR A  57  CYS A  58  VAL A  61  GLY A  62
SITE     4 AC2 38 CYS A  63  LYS A  66  GLY A 128  HIS A 129
SITE     5 AC2 38 ALA A 130  ALA A 155  THR A 156  GLY A 157
SITE     6 AC2 38 TYR A 197  ARG A 291  GLY A 330  ASP A 331
SITE     7 AC2 38 LEU A 337  LEU A 338  THR A 339  PRO A 340
SITE     8 AC2 38 HIS A 467  PRO A 468  HOH A 488  HOH A 490
SITE     9 AC2 38 HOH A 496  HOH A 501  HOH A 540  HOH A 810
SITE    10 AC2 38 HOH A 847  HOH A1006
SITE     1 AC3  3 CYS A  58  VAL A  59  TYR A 114
CRYST1  119.800   84.500   63.200  90.00  90.00  58.70 B 2           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      0.008347 -0.005075  0.000000        0.00000
SCALE2      0.000000  0.013850  0.000000        0.00000
SCALE3      0.000000  0.000000  0.015823        0.00000
      
PROCHECK
Go to PROCHECK summary
 References