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PDBsum entry 1g0d

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Transferase PDB id
1g0d
Jmol
Contents
Protein chain
666 a.a. *
Ligands
SO4
Waters ×383
* Residue conservation analysis
HEADER    TRANSFERASE                             06-OCT-00   1G0D
TITLE     CRYSTAL STRUCTURE OF RED SEA BREAM TRANSGLUTAMINASE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PROTEIN-GLUTAMINE GAMMA-GLUTAMYLTRANSFERASE;
COMPND   3 CHAIN: A;
COMPND   4 EC: 2.3.2.13;
COMPND   5 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: PAGRUS MAJOR;
SOURCE   3 ORGANISM_COMMON: RED SEABREAM;
SOURCE   4 ORGANISM_TAXID: 143350;
SOURCE   5 TISSUE: LIVER;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PTTNCO
KEYWDS    TISSUE TRANSGLUTAMINASE,ACYLTRANSFERASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    K.NOGUCHI,K.ISHIKAWA,K.YOKOYAMA,T.OHTSUKA,N.NIO,E.SUZUKI
REVDAT   4   24-FEB-09 1G0D    1       VERSN
REVDAT   3   01-APR-03 1G0D    1       JRNL
REVDAT   2   31-DEC-02 1G0D    1       REMARK
REVDAT   1   23-MAY-01 1G0D    0
JRNL        AUTH   K.NOGUCHI,K.ISHIKAWA,K.I.YOKOYAMA,T.OHTSUKA,N.NIO,
JRNL        AUTH 2 E.SUZUKI
JRNL        TITL   CRYSTAL STRUCTURE OF RED SEA BREAM
JRNL        TITL 2 TRANSGLUTAMINASE.
JRNL        REF    J.BIOL.CHEM.                  V. 276 12055 2001
JRNL        REFN                   ISSN 0021-9258
JRNL        PMID   11080504
JRNL        DOI    10.1074/JBC.M009862200
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   K.YOKOYAMA,Y.KIKUCHI,H.YASUEDA
REMARK   1  TITL   OVERPRODUCTION OF DNAJ IN ESCHERICHIA COLI
REMARK   1  TITL 2 IMPROVES IN VIVO SOLUBILITY OF THE RECOMBINANT
REMARK   1  TITL 3 FISH-DERIVED TRANSGLUTAMINASE
REMARK   1  REF    BIOSCI.BIOTECHNOL.BIOCHEM.    V.  62  1205 1998
REMARK   1  REFN                   ISSN 0916-8451
REMARK   1 REFERENCE 2
REMARK   1  AUTH   H.YASUEDA,K.NAKANISHI,Y.KUMAZAWA,K.NAGASE,M.MOTOKI,
REMARK   1  AUTH 2 H.MATSUI
REMARK   1  TITL   TISSUE-TYPE TRANSGLUTAMINASE FROM RED SEA BREAM
REMARK   1  TITL 2 (PAGRUS MAJOR)
REMARK   1  REF    EUR.J.BIOCHEM.                V. 232   411 1995
REMARK   1  REFN                   ISSN 0014-2956
REMARK   2
REMARK   2 RESOLUTION.    2.50 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) : 2.50
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00
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)   (%) : 86.0
REMARK   3   NUMBER OF REFLECTIONS             : 39366
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) : 0.200
REMARK   3   FREE R VALUE                     : 0.249
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : 3936
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            : 5283
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 5
REMARK   3   SOLVENT ATOMS            : 383
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 25.40
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) : 0.016
REMARK   3   BOND ANGLES            (DEGREES) : 1.99
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 28.52
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.03
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 1G0D COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 31-OCT-00.
REMARK 100 THE RCSB ID CODE IS RCSB012075.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 19-FEB-98
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.0
REMARK 200  NUMBER OF CRYSTALS USED        : 2
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY
REMARK 200  BEAMLINE                       : BL-6B
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00
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   : 39366
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500
REMARK 200  RESOLUTION RANGE LOW       (A) : 100.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 86.0
REMARK 200  DATA REDUNDANCY                : 6.620
REMARK 200  R MERGE                    (I) : 0.06300
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 6.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.55
REMARK 200  COMPLETENESS FOR SHELL     (%) : 61.4
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.70
REMARK 200  R MERGE FOR SHELL          (I) : 0.16200
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   (%): 69.35
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.01
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, PEG6000, HEPES,
REMARK 280  DTT, PH 7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -Y,X-Y,Z+2/3
REMARK 290       3555   -X+Y,-X,Z+1/3
REMARK 290       4555   -X,-Y,Z+1/2
REMARK 290       5555   Y,-X+Y,Z+1/6
REMARK 290       6555   X-Y,X,Z+5/6
REMARK 290       7555   Y,X,-Z+2/3
REMARK 290       8555   X-Y,-Y,-Z
REMARK 290       9555   -X,-X+Y,-Z+1/3
REMARK 290      10555   -Y,-X,-Z+1/6
REMARK 290      11555   -X+Y,Y,-Z+1/2
REMARK 290      12555   X,X-Y,-Z+5/6
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      303.66667
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      151.83333
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      227.75000
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       75.91667
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      379.58333
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      303.66667
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000      151.83333
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       75.91667
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000      227.75000
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000      379.58333
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: MONOMERIC
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 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     1
REMARK 465     ALA A     2
REMARK 465     SER A     3
REMARK 465     TYR A     4
REMARK 465     LYS A     5
REMARK 465     GLU A   462
REMARK 465     PRO A   463
REMARK 465     SER A   464
REMARK 465     ASN A   465
REMARK 465     GLU A   466
REMARK 465     ILE A   467
REMARK 465     ALA A   468
REMARK 465     GLU A   469
REMARK 465     GLN A   470
REMARK 465     GLY A   471
REMARK 465     GLY A   569
REMARK 465     GLU A   570
REMARK 465     ASN A   571
REMARK 465     TYR A   685
REMARK 465     ARG A   686
REMARK 465     SER A   687
REMARK 465     LEU A   688
REMARK 465     ILE A   689
REMARK 465     THR A   690
REMARK 465     GLY A   691
REMARK 465     LEU A   692
REMARK 465     HIS A   693
REMARK 465     THR A   694
REMARK 465     ASP A   695
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   OG   SER A   298     OE1  GLU A   393              2.10
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    GLU A 238   N   -  CA  -  C   ANGL. DEV. =  16.8 DEGREES
REMARK 500    PRO A 239   C   -  N   -  CA  ANGL. DEV. = -10.8 DEGREES
REMARK 500    LEU A 361   N   -  CA  -  C   ANGL. DEV. =  17.9 DEGREES
REMARK 500    SER A 362   N   -  CA  -  C   ANGL. DEV. = -16.6 DEGREES
REMARK 500    LEU A 509   CA  -  CB  -  CG  ANGL. DEV. =  15.5 DEGREES
REMARK 500    VAL A 619   CB  -  CA  -  C   ANGL. DEV. = -12.6 DEGREES
REMARK 500    LEU A 622   CA  -  CB  -  CG  ANGL. DEV. =  14.0 DEGREES
REMARK 500    LEU A 628   CA  -  CB  -  CG  ANGL. DEV. =  14.9 DEGREES
REMARK 500    VAL A 676   CB  -  CA  -  C   ANGL. DEV. = -11.4 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    ASP A  10      135.18   -171.53
REMARK 500    ASP A  28      144.80   -172.73
REMARK 500    ASP A  48      -91.52   -153.39
REMARK 500    PRO A  52      -76.96     -4.27
REMARK 500    GLU A  75     -148.14   -173.35
REMARK 500    HIS A  76       78.69    -15.03
REMARK 500    ALA A  78     -149.49    -62.82
REMARK 500    ALA A  89      -96.79   -104.55
REMARK 500    GLN A  90      -91.48   -116.78
REMARK 500    GLU A 123      149.85   -178.69
REMARK 500    ASP A 147      100.60   -163.53
REMARK 500    VAL A 155      -53.38   -129.41
REMARK 500    TYR A 169       75.25   -151.92
REMARK 500    TYR A 183       -2.23     69.98
REMARK 500    ASN A 224      -51.83   -142.68
REMARK 500    GLU A 238      -52.38    -18.63
REMARK 500    PRO A 239       93.87    -68.70
REMARK 500    TYR A 240       52.84    -90.82
REMARK 500    ASP A 242       52.92   -112.43
REMARK 500    VAL A 264       85.31     58.59
REMARK 500    PRO A 266      133.80    -39.04
REMARK 500    ALA A 297       68.99     64.16
REMARK 500    ASP A 326       72.62   -113.16
REMARK 500    SER A 327     -151.45     55.68
REMARK 500    ARG A 341       79.72   -107.49
REMARK 500    GLU A 360      -76.65    -21.22
REMARK 500    LEU A 361       32.48    -91.89
REMARK 500    ASP A 363      103.59    -42.14
REMARK 500    HIS A 416      -39.05    160.04
REMARK 500    ALA A 417     -151.45     15.86
REMARK 500    SER A 418      142.63     30.67
REMARK 500    GLN A 481       74.95     50.60
REMARK 500    GLU A 497       52.31   -101.78
REMARK 500    ASN A 516       32.25    -81.56
REMARK 500    ARG A 520      -94.25   -120.61
REMARK 500    GLU A 522       82.93    -67.65
REMARK 500    CYS A 523       30.36    -79.31
REMARK 500    GLN A 524      135.75    133.90
REMARK 500    LYS A 526      131.00   -179.11
REMARK 500    HIS A 535       35.61     39.89
REMARK 500    SER A 554     -168.70   -107.88
REMARK 500    PRO A 612       34.73    -82.17
REMARK 500    LEU A 627      -64.95   -105.32
REMARK 500    ALA A 630      127.28    -32.86
REMARK 500    SER A 642       19.93     58.86
REMARK 500    PRO A 653      154.27    -42.57
REMARK 500    ASP A 672       54.74     71.90
REMARK 500    LYS A 683       85.05    122.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500  M RES CSSEQI        RMS     TYPE
REMARK 500    TYR A 163         0.08    SIDE_CHAIN
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 911        DISTANCE =  7.00 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 696
DBREF  1G0D A    1   695  UNP    P52181   TGM2_PAGMA       1    695
SEQRES   1 A  695  MET ALA SER TYR LYS GLY LEU ILE VAL ASP VAL ASN GLY
SEQRES   2 A  695  ARG SER HIS GLU ASN ASN LEU ALA HIS ARG THR ARG GLU
SEQRES   3 A  695  ILE ASP ARG GLU ARG LEU ILE VAL ARG ARG GLY GLN PRO
SEQRES   4 A  695  PHE SER ILE THR LEU GLN CYS SER ASP SER LEU PRO PRO
SEQRES   5 A  695  LYS HIS HIS LEU GLU LEU VAL LEU HIS LEU GLY LYS ARG
SEQRES   6 A  695  ASP GLU VAL VAL ILE LYS VAL GLN LYS GLU HIS GLY ALA
SEQRES   7 A  695  ARG ASP LYS TRP TRP PHE ASN GLN GLN GLY ALA GLN ASP
SEQRES   8 A  695  GLU ILE LEU LEU THR LEU HIS SER PRO ALA ASN ALA VAL
SEQRES   9 A  695  ILE GLY HIS TYR ARG LEU ALA VAL LEU VAL MET SER PRO
SEQRES  10 A  695  ASP GLY HIS ILE VAL GLU ARG ALA ASP LYS ILE SER PHE
SEQRES  11 A  695  HIS MET LEU PHE ASN PRO TRP CYS ARG ASP ASP MET VAL
SEQRES  12 A  695  TYR LEU PRO ASP GLU SER LYS LEU GLN GLU TYR VAL MET
SEQRES  13 A  695  ASN GLU ASP GLY VAL ILE TYR MET GLY THR TRP ASP TYR
SEQRES  14 A  695  ILE ARG SER ILE PRO TRP ASN TYR GLY GLN PHE GLU ASP
SEQRES  15 A  695  TYR VAL MET ASP ILE CYS PHE GLU VAL LEU ASP ASN SER
SEQRES  16 A  695  PRO ALA ALA LEU LYS ASN SER GLU MET ASP ILE GLU HIS
SEQRES  17 A  695  ARG SER ASP PRO VAL TYR VAL GLY ARG THR ILE THR ALA
SEQRES  18 A  695  MET VAL ASN SER ASN GLY ASP ARG GLY VAL LEU THR GLY
SEQRES  19 A  695  ARG TRP GLU GLU PRO TYR THR ASP GLY VAL ALA PRO TYR
SEQRES  20 A  695  ARG TRP THR GLY SER VAL PRO ILE LEU GLN GLN TRP SER
SEQRES  21 A  695  LYS ALA GLY VAL ARG PRO VAL LYS TYR GLY GLN CYS TRP
SEQRES  22 A  695  VAL PHE ALA ALA VAL ALA CYS THR VAL LEU ARG CYS LEU
SEQRES  23 A  695  GLY ILE PRO THR ARG PRO ILE THR ASN PHE ALA SER ALA
SEQRES  24 A  695  HIS ASP VAL ASP GLY ASN LEU SER VAL ASP PHE LEU LEU
SEQRES  25 A  695  ASN GLU ARG LEU GLU SER LEU ASP SER ARG GLN ARG SER
SEQRES  26 A  695  ASP SER SER TRP ASN PHE HIS CYS TRP VAL GLU SER TRP
SEQRES  27 A  695  MET SER ARG GLU ASP LEU PRO GLU GLY ASN ASP GLY TRP
SEQRES  28 A  695  GLN VAL LEU ASP PRO THR PRO GLN GLU LEU SER ASP GLY
SEQRES  29 A  695  GLU PHE CYS CYS GLY PRO CYS PRO VAL ALA ALA ILE LYS
SEQRES  30 A  695  GLU GLY ASN LEU GLY VAL LYS TYR ASP ALA PRO PHE VAL
SEQRES  31 A  695  PHE ALA GLU VAL ASN ALA ASP THR ILE TYR TRP ILE VAL
SEQRES  32 A  695  GLN LYS ASP GLY GLN ARG ARG LYS ILE THR GLU ASP HIS
SEQRES  33 A  695  ALA SER VAL GLY LYS ASN ILE SER THR LYS SER VAL TYR
SEQRES  34 A  695  GLY ASN HIS ARG GLU ASP VAL THR LEU HIS TYR LYS TYR
SEQRES  35 A  695  PRO GLU GLY SER GLN LYS GLU ARG GLU VAL TYR LYS LYS
SEQRES  36 A  695  ALA GLY ARG ARG VAL THR GLU PRO SER ASN GLU ILE ALA
SEQRES  37 A  695  GLU GLN GLY ARG LEU GLN LEU SER ILE LYS HIS ALA GLN
SEQRES  38 A  695  PRO VAL PHE GLY THR ASP PHE ASP VAL ILE VAL GLU VAL
SEQRES  39 A  695  LYS ASN GLU GLY GLY ARG ASP ALA HIS ALA GLN LEU THR
SEQRES  40 A  695  MET LEU ALA MET ALA VAL THR TYR ASN SER LEU ARG ARG
SEQRES  41 A  695  GLY GLU CYS GLN ARG LYS THR ILE SER VAL THR VAL PRO
SEQRES  42 A  695  ALA HIS LYS ALA HIS LYS GLU VAL MET ARG LEU HIS TYR
SEQRES  43 A  695  ASP ASP TYR VAL ARG CYS VAL SER GLU HIS HIS LEU ILE
SEQRES  44 A  695  ARG VAL LYS ALA LEU LEU ASP ALA PRO GLY GLU ASN GLY
SEQRES  45 A  695  PRO ILE MET THR VAL ALA ASN ILE PRO LEU SER THR PRO
SEQRES  46 A  695  GLU LEU LEU VAL GLN VAL PRO GLY LYS ALA VAL VAL TRP
SEQRES  47 A  695  GLU PRO LEU THR ALA TYR VAL SER PHE THR ASN PRO LEU
SEQRES  48 A  695  PRO VAL PRO LEU LYS GLY GLY VAL PHE THR LEU GLU GLY
SEQRES  49 A  695  ALA GLY LEU LEU SER ALA THR GLN ILE HIS VAL ASN GLY
SEQRES  50 A  695  ALA VAL ALA PRO SER GLY LYS VAL SER VAL LYS LEU SER
SEQRES  51 A  695  PHE SER PRO MET ARG THR GLY VAL ARG LYS LEU LEU VAL
SEQRES  52 A  695  ASP PHE ASP SER ASP ARG LEU LYS ASP VAL LYS GLY VAL
SEQRES  53 A  695  THR THR VAL VAL VAL HIS LYS LYS TYR ARG SER LEU ILE
SEQRES  54 A  695  THR GLY LEU HIS THR ASP
HET    SO4  A 696       5
HETNAM     SO4 SULFATE ION
FORMUL   2  SO4    O4 S 2-
FORMUL   3  HOH   *383(H2 O)
HELIX    1   1 ARG A   14  HIS A   22  1                                   9
HELIX    2   2 ASP A  147  VAL A  155  1                                   9
HELIX    3   3 TYR A  183  ASN A  194  1                                  12
HELIX    4   4 SER A  195  ASN A  201  1                                   7
HELIX    5   5 ASN A  201  ARG A  209  1                                   9
HELIX    6   6 ASP A  211  ASN A  224  1                                  14
HELIX    7   7 ALA A  245  TRP A  249  5                                   5
HELIX    8   8 SER A  252  ALA A  262  1                                  11
HELIX    9   9 GLN A  271  GLY A  287  1                                  17
HELIX   10  10 ALA A  299  ASP A  303  5                                   5
HELIX   11  11 VAL A  373  GLU A  378  1                                   6
HELIX   12  12 ASP A  386  ALA A  396  1                                  11
HELIX   13  13 VAL A  436  LYS A  441  1                                   6
HELIX   14  14 SER A  446  GLY A  457  1                                  12
HELIX   15  15 HIS A  545  VAL A  550  1                                   6
SHEET    1   A 4 ILE A   8  ASN A  12  0
SHEET    2   A 4 PHE A  40  CYS A  46 -1  N  THR A  43   O  ASN A  12
SHEET    3   A 4 GLU A  92  HIS A  98 -1  N  ILE A  93   O  LEU A  44
SHEET    4   A 4 TRP A  83  ALA A  89 -1  O  TRP A  83   N  HIS A  98
SHEET    1   B 4 VAL A  68  VAL A  72  0
SHEET    2   B 4 HIS A  55  LEU A  62 -1  O  LEU A  58   N  VAL A  72
SHEET    3   B 4 GLY A 106  MET A 115 -1  N  ARG A 109   O  HIS A  61
SHEET    4   B 4 ILE A 121  ARG A 124 -1  N  VAL A 122   O  VAL A 114
SHEET    1   C 5 VAL A  68  VAL A  72  0
SHEET    2   C 5 HIS A  55  LEU A  62 -1  O  LEU A  58   N  VAL A  72
SHEET    3   C 5 GLY A 106  MET A 115 -1  N  ARG A 109   O  HIS A  61
SHEET    4   C 5 ILE A 128  LEU A 133 -1  O  ILE A 128   N  LEU A 110
SHEET    5   C 5 ILE A  33  ARG A  35  1  N  VAL A  34   O  HIS A 131
SHEET    1   D 2 ASP A 159  THR A 166  0
SHEET    2   D 2 TYR A 169  ASN A 176 -1  O  TYR A 169   N  THR A 166
SHEET    1   E 2 LEU A 232  GLY A 234  0
SHEET    2   E 2 VAL A 267  GLY A 270  1  O  VAL A 267   N  THR A 233
SHEET    1   F 6 CYS A 368  PRO A 372  0
SHEET    2   F 6 GLY A 350  ASP A 355 -1  N  VAL A 353   O  CYS A 371
SHEET    3   F 6 TRP A 329  MET A 339 -1  O  VAL A 335   N  LEU A 354
SHEET    4   F 6 THR A 290  SER A 298 -1  O  ARG A 291   N  GLU A 336
SHEET    5   F 6 SER A 424  LYS A 426 -1  O  SER A 424   N  THR A 294
SHEET    6   F 6 ARG A 433  ASP A 435 -1  N  GLU A 434   O  THR A 425
SHEET    1   G 3 SER A 307  LEU A 312  0
SHEET    2   G 3 ASP A 397  VAL A 403  1  O  ASP A 397   N  VAL A 308
SHEET    3   G 3 ARG A 409  LYS A 411 -1  N  ARG A 410   O  ILE A 402
SHEET    1   H 5 THR A 413  GLU A 414  0
SHEET    2   H 5 ILE A 574  PRO A 581  1  N  MET A 575   O  THR A 413
SHEET    3   H 5 LEU A 558  ASP A 566 -1  O  ILE A 559   N  ILE A 580
SHEET    4   H 5 ALA A 502  VAL A 513 -1  O  GLN A 505   N  ASP A 566
SHEET    5   H 5 ARG A 525  VAL A 532 -1  O  LYS A 526   N  MET A 508
SHEET    1   I 3 LEU A 473  HIS A 479  0
SHEET    2   I 3 PHE A 488  ASN A 496 -1  O  ILE A 491   N  LYS A 478
SHEET    3   I 3 ALA A 537  LEU A 544 -1  O  HIS A 538   N  VAL A 494
SHEET    1   J 3 LEU A 588  GLN A 590  0
SHEET    2   J 3 LEU A 601  THR A 608 -1  N  TYR A 604   O  GLN A 590
SHEET    3   J 3 LYS A 644  PHE A 651 -1  N  VAL A 645   O  PHE A 607
SHEET    1   K 5 ALA A 595  VAL A 596  0
SHEET    2   K 5 VAL A 673  HIS A 682  1  O  VAL A 680   N  ALA A 595
SHEET    3   K 5 GLY A 657  ASP A 666 -1  O  GLY A 657   N  VAL A 681
SHEET    4   K 5 VAL A 619  GLY A 624 -1  N  VAL A 619   O  ASP A 666
SHEET    5   K 5 LEU A 628  HIS A 634 -1  O  LEU A 628   N  GLY A 624
SHEET    1   L 2 LEU A 615  LYS A 616  0
SHEET    2   L 2 ALA A 638  VAL A 639 -1  N  VAL A 639   O  LEU A 615
CISPEP   1 LYS A  268    TYR A  269          0         2.70
CISPEP   2 GLY A  369    PRO A  370          0         1.96
CISPEP   3 LYS A  384    TYR A  385          0         0.13
SITE     1 AC1  7 LYS A 150  ARG A 291  TRP A 351  GLU A 434
SITE     2 AC1  7 HIS A 439  HOH A 845  HOH A 931
CRYST1   97.800   97.800  455.500  90.00  90.00 120.00 P 65 2 2     12
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      0.010225  0.005903  0.000000        0.00000
SCALE2      0.000000  0.011807  0.000000        0.00000
SCALE3      0.000000  0.000000  0.002195        0.00000
      
PROCHECK
Go to PROCHECK summary
 References