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PDBsum entry 1qrk

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Top Page protein metals Protein-protein interface(s) links
Transferase PDB id
1qrk
Jmol
Contents
Protein chain
700 a.a. *
Metals
_SR ×2
Waters ×230
* Residue conservation analysis
HEADER    TRANSFERASE                             14-JUN-99   1QRK
TITLE     HUMAN FACTOR XIII WITH STRONTIUM BOUND IN THE ION SITE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PROTEIN (COAGULATION FACTOR XIII);
COMPND   3 CHAIN: A, B;
COMPND   4 FRAGMENT: FULL LENGTH DIMER;
COMPND   5 EC: 2.3.2.13;
COMPND   6 ENGINEERED: YES;
COMPND   7 OTHER_DETAILS: STRONTIUM BOUND IN THE ION SITE
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE   6 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 4932
KEYWDS    TRANSGLUTAMINASE, BLOOD COAGULATION, CALCIUM, STRONTIUM,
KEYWDS   2 TRANSFERASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    B.A.FOX,V.C.YEE,L.C.PEDERSON,I.LE TRONG,P.D.BISHOP,
AUTHOR   2 R.E.STENKAMP,D.C.TELLER
REVDAT   3   24-FEB-09 1QRK    1       VERSN
REVDAT   2   01-APR-03 1QRK    1       JRNL
REVDAT   1   02-JUL-99 1QRK    0
SPRSDE     02-JUL-99 1QRK      1BL2
JRNL        AUTH   B.A.FOX,V.C.YEE,L.C.PEDERSEN,I.LE TRONG,P.D.BISHOP,
JRNL        AUTH 2 R.E.STENKAMP,D.C.TELLER
JRNL        TITL   IDENTIFICATION OF THE CALCIUM BINDING SITE AND A
JRNL        TITL 2 NOVEL YTTERBIUM SITE IN BLOOD COAGULATION FACTOR
JRNL        TITL 3 XIII BY X-RAY CRYSTALLOGRAPHY.
JRNL        REF    J.BIOL.CHEM.                  V. 274  4917 1999
JRNL        REFN                   ISSN 0021-9258
JRNL        PMID   9988734
JRNL        DOI    10.1074/JBC.274.8.4917
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : X-PLOR 3.1
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) : 10.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 100000.000
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.1000
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 78.5
REMARK   3   NUMBER OF REFLECTIONS             : 50777
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOMLY PICKED 5% OF DATA
REMARK   3   R VALUE            (WORKING SET) : 0.183
REMARK   3   FREE R VALUE                     : 0.275
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 2558
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.005
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 6
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.50
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.65
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 55.10
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 5598
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2700
REMARK   3   BIN FREE R VALUE                    : 0.3420
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.70
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 279
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.020
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 11260
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 2
REMARK   3   SOLVENT ATOMS            : 230
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 17.60
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 33.80
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : 0.00000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.26
REMARK   3   ESD FROM SIGMAA              (A) : 0.37
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.37
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.50
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.012
REMARK   3   BOND ANGLES            (DEGREES) : 1.70
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 27.30
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.50
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : 2.850 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 4.550 ; 2.000
REMARK   3   SIDE-CHAIN BOND              (A**2) : 4.420 ; 2.000
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 6.620 ; 2.500
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  : PARHCSDX.PRO
REMARK   3  PARAMETER FILE  2  : PARAM19.SOL
REMARK   3  PARAMETER FILE  3  : PARAM19.ION
REMARK   3  PARAMETER FILE  4  : NULL
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO
REMARK   3  TOPOLOGY FILE  2   : TOPH19.ION
REMARK   3  TOPOLOGY FILE  3   : TOPH19.SOL
REMARK   3  TOPOLOGY FILE  4   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1QRK COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-JUN-99.
REMARK 100 THE RCSB ID CODE IS RCSB009183.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-JUN-94
REMARK 200  TEMPERATURE           (KELVIN) : 293
REMARK 200  PH                             : 6.2
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 RU200
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IIC
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : R-AXIS
REMARK 200  DATA SCALING SOFTWARE          : R-AXIS
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 50777
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500
REMARK 200  RESOLUTION RANGE LOW       (A) : 10.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 78.5
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) : 2.50
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.65
REMARK 200  COMPLETENESS FOR SHELL     (%) : 55.1
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: PDB ENTRY 1FIE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 57.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1,2-PROPANEDIOL (24%) AND NAKPO4
REMARK 280  (100MM) PH 6.2, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 25K
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       36.16000
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 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 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     SER A     1
REMARK 465     GLU A     2
REMARK 465     THR A     3
REMARK 465     SER A     4
REMARK 465     ARG A     5
REMARK 465     THR A     6
REMARK 465     ALA A     7
REMARK 465     PHE A     8
REMARK 465     LEU A    31
REMARK 465     GLN A    32
REMARK 465     GLY A    33
REMARK 465     VAL A    34
REMARK 465     VAL A    35
REMARK 465     PRO A    36
REMARK 465     ARG A    37
REMARK 465     GLY A    38
REMARK 465     VAL A    39
REMARK 465     ASN A    40
REMARK 465     LEU A    41
REMARK 465     GLN A    42
REMARK 465     GLU A    43
REMARK 465     PHE A    44
REMARK 465     MET A   512
REMARK 465     LYS A   513
REMARK 465     SER A   514
REMARK 465     ARG A   515
REMARK 465     SER A   516
REMARK 465     ARG A   728
REMARK 465     PRO A   729
REMARK 465     SER A   730
REMARK 465     MET A   731
REMARK 465     SER B     1
REMARK 465     GLU B     2
REMARK 465     THR B     3
REMARK 465     SER B     4
REMARK 465     ARG B     5
REMARK 465     THR B     6
REMARK 465     ALA B     7
REMARK 465     PHE B     8
REMARK 465     GLY B     9
REMARK 465     PRO B    36
REMARK 465     ARG B    37
REMARK 465     GLY B    38
REMARK 465     VAL B    39
REMARK 465     ASN B    40
REMARK 465     THR B   508
REMARK 465     GLU B   509
REMARK 465     GLY B   510
REMARK 465     VAL B   511
REMARK 465     MET B   512
REMARK 465     LYS B   513
REMARK 465     SER B   514
REMARK 465     ARG B   515
REMARK 465     ARG B   728
REMARK 465     PRO B   729
REMARK 465     SER B   730
REMARK 465     MET B   731
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     GLU A  30    O
REMARK 470     VAL A 511    O
REMARK 470     ARG A 727    O
REMARK 470     VAL B  34    CG1  CG2
REMARK 470     VAL B  35    O    CG1  CG2
REMARK 470     LEU B  41    CG   CD1  CD2
REMARK 470     ASN B 507    O
REMARK 470     ARG B 727    O
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    PHE A  53       68.64   -104.47
REMARK 500    LYS A  54      -75.74    -59.67
REMARK 500    GLU A  55      117.07     -1.22
REMARK 500    MET A 136      136.75    173.84
REMARK 500    ASP A 139       80.23     13.70
REMARK 500    GLU A 177        2.53    -66.42
REMARK 500    ASN A 197      109.91   -170.45
REMARK 500    TYR A 214     -152.32   -162.15
REMARK 500    ARG A 223      136.20   -173.53
REMARK 500    ALA A 268      101.96    -51.31
REMARK 500    ASP A 270       80.43     65.97
REMARK 500    GLU A 272      -74.13   -122.64
REMARK 500    VAL A 274      -71.06    -75.62
REMARK 500    SER A 278      129.43   -175.20
REMARK 500    ASN A 281       11.38    -51.13
REMARK 500    VAL A 296      -73.06    -42.95
REMARK 500    PHE A 339       74.01     74.26
REMARK 500    MET A 406       72.99     71.49
REMARK 500    SER A 437      162.32    -47.01
REMARK 500    ASP A 472       17.80    -67.90
REMARK 500    GLU A 509     -100.83    -76.24
REMARK 500    HIS A 544       42.23    -86.37
REMARK 500    GLU A 571      115.42   -167.92
REMARK 500    TYR A 594      -37.29   -135.62
REMARK 500    GLU A 600      -50.02    -28.42
REMARK 500    ASN A 613      -37.01    -31.03
REMARK 500    LYS A 621      137.34   -172.22
REMARK 500    SER A 713      -83.01   -125.74
REMARK 500    PRO B  15      171.44    -56.76
REMARK 500    LEU B  45      132.79    123.26
REMARK 500    SER B  49      159.85    179.66
REMARK 500    LEU B  52       63.50   -119.30
REMARK 500    PHE B  53       70.08    -21.59
REMARK 500    LYS B  54      -77.52    -84.59
REMARK 500    GLU B  55      122.90      6.98
REMARK 500    ARG B  56      -32.89    -32.14
REMARK 500    ASP B  58      152.99    -49.64
REMARK 500    ASN B  60      -73.75    -48.52
REMARK 500    PRO B  91      136.76    -31.77
REMARK 500    PRO B  94        7.80    -64.44
REMARK 500    ARG B 100      148.51   -176.19
REMARK 500    TYR B 108       66.13   -117.27
REMARK 500    VAL B 119       87.59     55.65
REMARK 500    MET B 136      135.70   -172.12
REMARK 500    THR B 172      172.93    -59.43
REMARK 500    VAL B 205      -53.75   -126.85
REMARK 500    TYR B 214     -154.73   -134.20
REMARK 500    ASP B 219       71.67    177.85
REMARK 500    ARG B 252       13.80    -65.94
REMARK 500    ALA B 268       93.36    -61.02
REMARK 500    ASP B 270     -111.33     70.39
REMARK 500    ASP B 271       46.03   -141.76
REMARK 500    GLU B 272      -66.35   -103.15
REMARK 500    ASN B 281       -4.13     68.83
REMARK 500    ILE B 282      -60.02   -103.06
REMARK 500    TYR B 283       63.93     66.20
REMARK 500    ALA B 284      -71.28    -36.05
REMARK 500    CYS B 314      -34.43    -38.11
REMARK 500    PHE B 339       78.23     69.59
REMARK 500    ALA B 346       -7.82     68.00
REMARK 500    SER B 362      -19.68    -44.61
REMARK 500    MET B 406       59.84     78.58
REMARK 500    GLN B 487      143.92    -32.43
REMARK 500    LYS B 504       70.74   -155.70
REMARK 500    PRO B 505      -83.58    -46.28
REMARK 500    ASP B 521      151.56    178.19
REMARK 500    ARG B 540      135.40   -177.51
REMARK 500    HIS B 544       50.12    -98.94
REMARK 500    SER B 581     -153.24   -125.90
REMARK 500    PHE B 582      142.79   -174.16
REMARK 500    GLN B 597       44.20   -146.71
REMARK 500    GLN B 601       -6.14     73.00
REMARK 500    ILE B 612       66.86   -103.73
REMARK 500    ASN B 613      -34.46    -25.67
REMARK 500    VAL B 672      -35.41   -132.89
REMARK 500    ARG B 703     -166.70   -112.00
REMARK 500    SER B 713      -93.71    -92.28
REMARK 500
REMARK 500 REMARK: NULL
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                              SR B 732  SR
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA B 457   O
REMARK 620 2 GLU B 485   OE1  81.2
REMARK 620 N                    1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CAT
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: CATALYTIC TRIAD IN CHAIN A
REMARK 800 SITE_IDENTIFIER: CBT
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: CATALYTIC TRIAD IN CHAIN B
REMARK 800 SITE_IDENTIFIER: INA
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: ION BINDING SITE A STRONTIUM LIGANDS
REMARK 800 SITE_IDENTIFIER: INB
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: ION BINDING SITE B STRONTIUM LIGANDS
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SR A 732
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SR B 732
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1GGT   RELATED DB: PDB
REMARK 900 FACTOR XIII - ZYMOGEN
REMARK 900 RELATED ID: 1FIE   RELATED DB: PDB
REMARK 900 FACTOR XIII - THROMBIN CLEAVED
REMARK 900 RELATED ID: 1GGU   RELATED DB: PDB
REMARK 900 FACTOR XIII - CALCIUM BOUND
REMARK 900 RELATED ID: 1GGY   RELATED DB: PDB
REMARK 900 FACTOR XIII - YTTERBIUM BOUND
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 RESIDUES NOT VISIBLE IN ELECTRON DENSITY MAPS:
REMARK 999 CHAIN A 1-8, 31-44, 512-516, 728-731
REMARK 999 CHAIN B 1-9, 36-40, 508-515, 728-731
DBREF  1QRK A    1   731  UNP    P00488   F13A_HUMAN       1    731
DBREF  1QRK B    1   731  UNP    P00488   F13A_HUMAN       1    731
SEQADV 1QRK GLU A  651  UNP  P00488    GLN   651 CONFLICT
SEQADV 1QRK GLU B  651  UNP  P00488    GLN   651 CONFLICT
SEQRES   1 A  731  SER GLU THR SER ARG THR ALA PHE GLY GLY ARG ARG ALA
SEQRES   2 A  731  VAL PRO PRO ASN ASN SER ASN ALA ALA GLU ASP ASP LEU
SEQRES   3 A  731  PRO THR VAL GLU LEU GLN GLY VAL VAL PRO ARG GLY VAL
SEQRES   4 A  731  ASN LEU GLN GLU PHE LEU ASN VAL THR SER VAL HIS LEU
SEQRES   5 A  731  PHE LYS GLU ARG TRP ASP THR ASN LYS VAL ASP HIS HIS
SEQRES   6 A  731  THR ASP LYS TYR GLU ASN ASN LYS LEU ILE VAL ARG ARG
SEQRES   7 A  731  GLY GLN SER PHE TYR VAL GLN ILE ASP PHE SER ARG PRO
SEQRES   8 A  731  TYR ASP PRO ARG ARG ASP LEU PHE ARG VAL GLU TYR VAL
SEQRES   9 A  731  ILE GLY ARG TYR PRO GLN GLU ASN LYS GLY THR TYR ILE
SEQRES  10 A  731  PRO VAL PRO ILE VAL SER GLU LEU GLN SER GLY LYS TRP
SEQRES  11 A  731  GLY ALA LYS ILE VAL MET ARG GLU ASP ARG SER VAL ARG
SEQRES  12 A  731  LEU SER ILE GLN SER SER PRO LYS CYS ILE VAL GLY LYS
SEQRES  13 A  731  PHE ARG MET TYR VAL ALA VAL TRP THR PRO TYR GLY VAL
SEQRES  14 A  731  LEU ARG THR SER ARG ASN PRO GLU THR ASP THR TYR ILE
SEQRES  15 A  731  LEU PHE ASN PRO TRP CYS GLU ASP ASP ALA VAL TYR LEU
SEQRES  16 A  731  ASP ASN GLU LYS GLU ARG GLU GLU TYR VAL LEU ASN ASP
SEQRES  17 A  731  ILE GLY VAL ILE PHE TYR GLY GLU VAL ASN ASP ILE LYS
SEQRES  18 A  731  THR ARG SER TRP SER TYR GLY GLN PHE GLU ASP GLY ILE
SEQRES  19 A  731  LEU ASP THR CYS LEU TYR VAL MET ASP ARG ALA GLN MET
SEQRES  20 A  731  ASP LEU SER GLY ARG GLY ASN PRO ILE LYS VAL SER ARG
SEQRES  21 A  731  VAL GLY SER ALA MET VAL ASN ALA LYS ASP ASP GLU GLY
SEQRES  22 A  731  VAL LEU VAL GLY SER TRP ASP ASN ILE TYR ALA TYR GLY
SEQRES  23 A  731  VAL PRO PRO SER ALA TRP THR GLY SER VAL ASP ILE LEU
SEQRES  24 A  731  LEU GLU TYR ARG SER SER GLU ASN PRO VAL ARG TYR GLY
SEQRES  25 A  731  GLN CYS TRP VAL PHE ALA GLY VAL PHE ASN THR PHE LEU
SEQRES  26 A  731  ARG CYS LEU GLY ILE PRO ALA ARG ILE VAL THR ASN TYR
SEQRES  27 A  731  PHE SER ALA HIS ASP ASN ASP ALA ASN LEU GLN MET ASP
SEQRES  28 A  731  ILE PHE LEU GLU GLU ASP GLY ASN VAL ASN SER LYS LEU
SEQRES  29 A  731  THR LYS ASP SER VAL TRP ASN TYR HIS CYS TRP ASN GLU
SEQRES  30 A  731  ALA TRP MET THR ARG PRO ASP LEU PRO VAL GLY PHE GLY
SEQRES  31 A  731  GLY TRP GLN ALA VAL ASP SER THR PRO GLN GLU ASN SER
SEQRES  32 A  731  ASP GLY MET TYR ARG CYS GLY PRO ALA SER VAL GLN ALA
SEQRES  33 A  731  ILE LYS HIS GLY HIS VAL CYS PHE GLN PHE ASP ALA PRO
SEQRES  34 A  731  PHE VAL PHE ALA GLU VAL ASN SER ASP LEU ILE TYR ILE
SEQRES  35 A  731  THR ALA LYS LYS ASP GLY THR HIS VAL VAL GLU ASN VAL
SEQRES  36 A  731  ASP ALA THR HIS ILE GLY LYS LEU ILE VAL THR LYS GLN
SEQRES  37 A  731  ILE GLY GLY ASP GLY MET MET ASP ILE THR ASP THR TYR
SEQRES  38 A  731  LYS PHE GLN GLU GLY GLN GLU GLU GLU ARG LEU ALA LEU
SEQRES  39 A  731  GLU THR ALA LEU MET TYR GLY ALA LYS LYS PRO LEU ASN
SEQRES  40 A  731  THR GLU GLY VAL MET LYS SER ARG SER ASN VAL ASP MET
SEQRES  41 A  731  ASP PHE GLU VAL GLU ASN ALA VAL LEU GLY LYS ASP PHE
SEQRES  42 A  731  LYS LEU SER ILE THR PHE ARG ASN ASN SER HIS ASN ARG
SEQRES  43 A  731  TYR THR ILE THR ALA TYR LEU SER ALA ASN ILE THR PHE
SEQRES  44 A  731  TYR THR GLY VAL PRO LYS ALA GLU PHE LYS LYS GLU THR
SEQRES  45 A  731  PHE ASP VAL THR LEU GLU PRO LEU SER PHE LYS LYS GLU
SEQRES  46 A  731  ALA VAL LEU ILE GLN ALA GLY GLU TYR MET GLY GLN LEU
SEQRES  47 A  731  LEU GLU GLN ALA SER LEU HIS PHE PHE VAL THR ALA ARG
SEQRES  48 A  731  ILE ASN GLU THR ARG ASP VAL LEU ALA LYS GLN LYS SER
SEQRES  49 A  731  THR VAL LEU THR ILE PRO GLU ILE ILE ILE LYS VAL ARG
SEQRES  50 A  731  GLY THR GLN VAL VAL GLY SER ASP MET THR VAL THR VAL
SEQRES  51 A  731  GLU PHE THR ASN PRO LEU LYS GLU THR LEU ARG ASN VAL
SEQRES  52 A  731  TRP VAL HIS LEU ASP GLY PRO GLY VAL THR ARG PRO MET
SEQRES  53 A  731  LYS LYS MET PHE ARG GLU ILE ARG PRO ASN SER THR VAL
SEQRES  54 A  731  GLN TRP GLU GLU VAL CYS ARG PRO TRP VAL SER GLY HIS
SEQRES  55 A  731  ARG LYS LEU ILE ALA SER MET SER SER ASP SER LEU ARG
SEQRES  56 A  731  HIS VAL TYR GLY GLU LEU ASP VAL GLN ILE GLN ARG ARG
SEQRES  57 A  731  PRO SER MET
SEQRES   1 B  731  SER GLU THR SER ARG THR ALA PHE GLY GLY ARG ARG ALA
SEQRES   2 B  731  VAL PRO PRO ASN ASN SER ASN ALA ALA GLU ASP ASP LEU
SEQRES   3 B  731  PRO THR VAL GLU LEU GLN GLY VAL VAL PRO ARG GLY VAL
SEQRES   4 B  731  ASN LEU GLN GLU PHE LEU ASN VAL THR SER VAL HIS LEU
SEQRES   5 B  731  PHE LYS GLU ARG TRP ASP THR ASN LYS VAL ASP HIS HIS
SEQRES   6 B  731  THR ASP LYS TYR GLU ASN ASN LYS LEU ILE VAL ARG ARG
SEQRES   7 B  731  GLY GLN SER PHE TYR VAL GLN ILE ASP PHE SER ARG PRO
SEQRES   8 B  731  TYR ASP PRO ARG ARG ASP LEU PHE ARG VAL GLU TYR VAL
SEQRES   9 B  731  ILE GLY ARG TYR PRO GLN GLU ASN LYS GLY THR TYR ILE
SEQRES  10 B  731  PRO VAL PRO ILE VAL SER GLU LEU GLN SER GLY LYS TRP
SEQRES  11 B  731  GLY ALA LYS ILE VAL MET ARG GLU ASP ARG SER VAL ARG
SEQRES  12 B  731  LEU SER ILE GLN SER SER PRO LYS CYS ILE VAL GLY LYS
SEQRES  13 B  731  PHE ARG MET TYR VAL ALA VAL TRP THR PRO TYR GLY VAL
SEQRES  14 B  731  LEU ARG THR SER ARG ASN PRO GLU THR ASP THR TYR ILE
SEQRES  15 B  731  LEU PHE ASN PRO TRP CYS GLU ASP ASP ALA VAL TYR LEU
SEQRES  16 B  731  ASP ASN GLU LYS GLU ARG GLU GLU TYR VAL LEU ASN ASP
SEQRES  17 B  731  ILE GLY VAL ILE PHE TYR GLY GLU VAL ASN ASP ILE LYS
SEQRES  18 B  731  THR ARG SER TRP SER TYR GLY GLN PHE GLU ASP GLY ILE
SEQRES  19 B  731  LEU ASP THR CYS LEU TYR VAL MET ASP ARG ALA GLN MET
SEQRES  20 B  731  ASP LEU SER GLY ARG GLY ASN PRO ILE LYS VAL SER ARG
SEQRES  21 B  731  VAL GLY SER ALA MET VAL ASN ALA LYS ASP ASP GLU GLY
SEQRES  22 B  731  VAL LEU VAL GLY SER TRP ASP ASN ILE TYR ALA TYR GLY
SEQRES  23 B  731  VAL PRO PRO SER ALA TRP THR GLY SER VAL ASP ILE LEU
SEQRES  24 B  731  LEU GLU TYR ARG SER SER GLU ASN PRO VAL ARG TYR GLY
SEQRES  25 B  731  GLN CYS TRP VAL PHE ALA GLY VAL PHE ASN THR PHE LEU
SEQRES  26 B  731  ARG CYS LEU GLY ILE PRO ALA ARG ILE VAL THR ASN TYR
SEQRES  27 B  731  PHE SER ALA HIS ASP ASN ASP ALA ASN LEU GLN MET ASP
SEQRES  28 B  731  ILE PHE LEU GLU GLU ASP GLY ASN VAL ASN SER LYS LEU
SEQRES  29 B  731  THR LYS ASP SER VAL TRP ASN TYR HIS CYS TRP ASN GLU
SEQRES  30 B  731  ALA TRP MET THR ARG PRO ASP LEU PRO VAL GLY PHE GLY
SEQRES  31 B  731  GLY TRP GLN ALA VAL ASP SER THR PRO GLN GLU ASN SER
SEQRES  32 B  731  ASP GLY MET TYR ARG CYS GLY PRO ALA SER VAL GLN ALA
SEQRES  33 B  731  ILE LYS HIS GLY HIS VAL CYS PHE GLN PHE ASP ALA PRO
SEQRES  34 B  731  PHE VAL PHE ALA GLU VAL ASN SER ASP LEU ILE TYR ILE
SEQRES  35 B  731  THR ALA LYS LYS ASP GLY THR HIS VAL VAL GLU ASN VAL
SEQRES  36 B  731  ASP ALA THR HIS ILE GLY LYS LEU ILE VAL THR LYS GLN
SEQRES  37 B  731  ILE GLY GLY ASP GLY MET MET ASP ILE THR ASP THR TYR
SEQRES  38 B  731  LYS PHE GLN GLU GLY GLN GLU GLU GLU ARG LEU ALA LEU
SEQRES  39 B  731  GLU THR ALA LEU MET TYR GLY ALA LYS LYS PRO LEU ASN
SEQRES  40 B  731  THR GLU GLY VAL MET LYS SER ARG SER ASN VAL ASP MET
SEQRES  41 B  731  ASP PHE GLU VAL GLU ASN ALA VAL LEU GLY LYS ASP PHE
SEQRES  42 B  731  LYS LEU SER ILE THR PHE ARG ASN ASN SER HIS ASN ARG
SEQRES  43 B  731  TYR THR ILE THR ALA TYR LEU SER ALA ASN ILE THR PHE
SEQRES  44 B  731  TYR THR GLY VAL PRO LYS ALA GLU PHE LYS LYS GLU THR
SEQRES  45 B  731  PHE ASP VAL THR LEU GLU PRO LEU SER PHE LYS LYS GLU
SEQRES  46 B  731  ALA VAL LEU ILE GLN ALA GLY GLU TYR MET GLY GLN LEU
SEQRES  47 B  731  LEU GLU GLN ALA SER LEU HIS PHE PHE VAL THR ALA ARG
SEQRES  48 B  731  ILE ASN GLU THR ARG ASP VAL LEU ALA LYS GLN LYS SER
SEQRES  49 B  731  THR VAL LEU THR ILE PRO GLU ILE ILE ILE LYS VAL ARG
SEQRES  50 B  731  GLY THR GLN VAL VAL GLY SER ASP MET THR VAL THR VAL
SEQRES  51 B  731  GLU PHE THR ASN PRO LEU LYS GLU THR LEU ARG ASN VAL
SEQRES  52 B  731  TRP VAL HIS LEU ASP GLY PRO GLY VAL THR ARG PRO MET
SEQRES  53 B  731  LYS LYS MET PHE ARG GLU ILE ARG PRO ASN SER THR VAL
SEQRES  54 B  731  GLN TRP GLU GLU VAL CYS ARG PRO TRP VAL SER GLY HIS
SEQRES  55 B  731  ARG LYS LEU ILE ALA SER MET SER SER ASP SER LEU ARG
SEQRES  56 B  731  HIS VAL TYR GLY GLU LEU ASP VAL GLN ILE GLN ARG ARG
SEQRES  57 B  731  PRO SER MET
HET     SR  A 732       1
HET     SR  B 732       1
HETNAM      SR STRONTIUM ION
FORMUL   3   SR    2(SR 2+)
FORMUL   5  HOH   *230(H2 O)
HELIX    1   1 THR A   59  HIS A   64  1                                   6
HELIX    2   2 PRO A  176  THR A  178  5                                   3
HELIX    3   3 GLU A  198  LEU A  206  1                                   9
HELIX    4   4 ILE A  234  ARG A  244  1                                  11
HELIX    5   5 LEU A  249  GLY A  251  5                                   3
HELIX    6   6 PRO A  255  VAL A  266  1                                  12
HELIX    7   7 VAL A  296  SER A  305  1                                  10
HELIX    8   8 CYS A  314  LEU A  328  1                                  15
HELIX    9   9 VAL A  414  HIS A  419  1                                   6
HELIX   10  10 ALA A  428  ASN A  436  1                                   9
HELIX   11  11 THR A  478  TYR A  481  1                                   4
HELIX   12  12 GLU A  488  TYR A  500  1                                  13
HELIX   13  13 ALA A  591  GLU A  593  5                                   3
HELIX   14  14 MET A  595  GLN A  597  5                                   3
HELIX   15  15 THR B   59  ASP B   63  1                                   5
HELIX   16  16 GLU B  111  LYS B  113  5                                   3
HELIX   17  17 PRO B  176  THR B  178  5                                   3
HELIX   18  18 GLU B  198  TYR B  204  1                                   7
HELIX   19  19 ILE B  234  ARG B  244  1                                  11
HELIX   20  20 LEU B  249  GLY B  251  5                                   3
HELIX   21  21 PRO B  255  VAL B  266  1                                  12
HELIX   22  22 SER B  295  SER B  305  1                                  11
HELIX   23  23 CYS B  314  LEU B  328  1                                  15
HELIX   24  24 VAL B  414  LYS B  418  1                                   5
HELIX   25  25 ALA B  428  VAL B  435  1                                   8
HELIX   26  26 THR B  478  TYR B  481  1                                   4
HELIX   27  27 GLU B  488  TYR B  500  1                                  13
HELIX   28  28 ALA B  591  GLN B  597  5                                   7
SHEET    1   A 3 LEU A  74  ARG A  77  0
SHEET    2   A 3 THR A 180  LEU A 183  1  N  TYR A 181   O  LEU A  74
SHEET    3   A 3 GLY A 155  PHE A 157 -1  N  PHE A 157   O  THR A 180
SHEET    1   B 4 VAL A  47  LEU A  52  0
SHEET    2   B 4 PHE A  82  PHE A  88 -1  N  ASP A  87   O  THR A  48
SHEET    3   B 4 SER A 141  GLN A 147 -1  N  ILE A 146   O  PHE A  82
SHEET    4   B 4 GLY A 131  GLU A 138 -1  N  GLU A 138   O  SER A 141
SHEET    1   C 4 TYR A 116  VAL A 119  0
SHEET    2   C 4 PHE A  99  VAL A 104 -1  N  TYR A 103   O  ILE A 117
SHEET    3   C 4 ARG A 158  THR A 165 -1  N  ALA A 162   O  ARG A 100
SHEET    4   C 4 GLY A 168  ARG A 171 -1  N  LEU A 170   O  VAL A 163
SHEET    1   D 2 GLY A 210  GLU A 216  0
SHEET    2   D 2 ASP A 219  TRP A 225 -1  N  TRP A 225   O  GLY A 210
SHEET    1   E 5 MET A 474  ASP A 476  0
SHEET    2   E 5 LEU A 463  LYS A 467 -1  N  THR A 466   O  MET A 475
SHEET    3   E 5 ALA A 332  TYR A 338 -1  N  TYR A 338   O  LEU A 463
SHEET    4   E 5 TYR A 372  MET A 380 -1  N  GLU A 377   O  ARG A 333
SHEET    5   E 5 GLY A 391  VAL A 395 -1  N  VAL A 395   O  ASN A 376
SHEET    1   F 3 GLN A 349  LEU A 354  0
SHEET    2   F 3 ASP A 438  LYS A 445  1  N  ASP A 438   O  MET A 350
SHEET    3   F 3 THR A 449  ASP A 456 -1  N  ASP A 456   O  LEU A 439
SHEET    1   G 3 VAL A 518  VAL A 524  0
SHEET    2   G 3 PHE A 533  ASN A 541 -1  N  ARG A 540   O  ASP A 519
SHEET    3   G 3 SER A 581  ILE A 589 -1  N  ILE A 589   O  PHE A 533
SHEET    1   H 4 ASP A 617  VAL A 626  0
SHEET    2   H 4 SER A 603  ILE A 612 -1  N  ILE A 612   O  ASP A 617
SHEET    3   H 4 TYR A 547  THR A 558 -1  N  THR A 558   O  SER A 603
SHEET    4   H 4 ALA A 566  LEU A 577 -1  N  LEU A 577   O  TYR A 547
SHEET    1   I 3 ILE A 633  GLY A 638  0
SHEET    2   I 3 ASP A 645  GLU A 651 -1  N  GLU A 651   O  ILE A 633
SHEET    3   I 3 TRP A 691  ARG A 696 -1  N  CYS A 695   O  MET A 646
SHEET    1   J 4 MET A 676  PHE A 680  0
SHEET    2   J 4 VAL A 663  ASP A 668 -1  N  LEU A 667   O  MET A 676
SHEET    3   J 4 LEU A 705  SER A 710 -1  N  SER A 710   O  TRP A 664
SHEET    4   J 4 ARG A 715  LEU A 721 -1  N  LEU A 721   O  LEU A 705
SHEET    1   K 4 VAL B  29  LEU B  31  0
SHEET    2   K 4 GLY B 168  ARG B 171 -1  N  VAL B 169   O  GLU B  30
SHEET    3   K 4 ARG B 158  THR B 165 -1  N  THR B 165   O  GLY B 168
SHEET    4   K 4 PHE B  99  VAL B 104 -1  N  VAL B 104   O  ARG B 158
SHEET    1   L 3 LEU B  74  ARG B  77  0
SHEET    2   L 3 THR B 180  LEU B 183  1  N  TYR B 181   O  LEU B  74
SHEET    3   L 3 GLY B 155  PHE B 157 -1  N  PHE B 157   O  THR B 180
SHEET    1   M 4 VAL B  47  HIS B  51  0
SHEET    2   M 4 PHE B  82  PHE B  88 -1  N  ASP B  87   O  THR B  48
SHEET    3   M 4 SER B 141  GLN B 147 -1  N  ILE B 146   O  PHE B  82
SHEET    4   M 4 GLY B 131  GLU B 138 -1  N  GLU B 138   O  SER B 141
SHEET    1   N 2 ILE B 209  GLU B 216  0
SHEET    2   N 2 ASP B 219  SER B 226 -1  N  TRP B 225   O  GLY B 210
SHEET    1   O 5 MET B 474  ASP B 476  0
SHEET    2   O 5 LEU B 463  LYS B 467 -1  N  THR B 466   O  MET B 475
SHEET    3   O 5 ALA B 332  TYR B 338 -1  N  TYR B 338   O  LEU B 463
SHEET    4   O 5 TYR B 372  MET B 380 -1  N  GLU B 377   O  ARG B 333
SHEET    5   O 5 GLY B 391  VAL B 395 -1  N  VAL B 395   O  ASN B 376
SHEET    1   P 3 GLN B 349  LEU B 354  0
SHEET    2   P 3 ASP B 438  ALA B 444  1  N  ASP B 438   O  MET B 350
SHEET    3   P 3 HIS B 450  ASP B 456 -1  N  ASP B 456   O  LEU B 439
SHEET    1   Q 3 MET B 520  VAL B 524  0
SHEET    2   Q 3 PHE B 533  PHE B 539 -1  N  THR B 538   O  ASP B 521
SHEET    3   Q 3 LYS B 583  ILE B 589 -1  N  ILE B 589   O  PHE B 533
SHEET    1   R 4 ASP B 617  VAL B 626  0
SHEET    2   R 4 SER B 603  ILE B 612 -1  N  ILE B 612   O  ASP B 617
SHEET    3   R 4 TYR B 547  THR B 558 -1  N  THR B 558   O  SER B 603
SHEET    4   R 4 ALA B 566  LEU B 577 -1  N  LEU B 577   O  TYR B 547
SHEET    1   S 3 ILE B 633  GLY B 638  0
SHEET    2   S 3 ASP B 645  THR B 653 -1  N  GLU B 651   O  ILE B 633
SHEET    3   S 3 THR B 688  ARG B 696 -1  N  CYS B 695   O  MET B 646
SHEET    1   T 4 MET B 676  PHE B 680  0
SHEET    2   T 4 VAL B 663  ASP B 668 -1  N  LEU B 667   O  MET B 676
SHEET    3   T 4 GLY B 701  SER B 710 -1  N  SER B 710   O  TRP B 664
SHEET    4   T 4 ARG B 715  ILE B 725 -1  N  ILE B 725   O  GLY B 701
LINK         O   ALA A 457                SR    SR A 732     1555   1555  2.55
LINK         O   ALA B 457                SR    SR B 732     1555   1555  2.75
LINK        SR    SR B 732                 OE1 GLU B 485     1555   1555  2.93
CISPEP   1 ARG A  310    TYR A  311          0         0.27
CISPEP   2 GLY A  410    PRO A  411          0         0.82
CISPEP   3 GLN A  425    PHE A  426          0        -0.99
CISPEP   4 ARG B  310    TYR B  311          0         0.80
CISPEP   5 GLY B  410    PRO B  411          0         0.25
CISPEP   6 GLN B  425    PHE B  426          0         0.77
SITE     1 CAT  3 CYS A 314  HIS A 373  ASP A 396
SITE     1 CBT  3 CYS B 314  HIS B 373  ASP B 396
SITE     1 INA  4 ALA A 457  ASN A 436  GLU A 485  GLU A 490
SITE     1 INB  4 ALA B 457  ASN B 436  GLU B 485  GLU B 490
SITE     1 AC1  2 ALA A 457  GLU A 485
SITE     1 AC2  3 ASN B 436  ALA B 457  GLU B 485
CRYST1  101.900   72.320  135.030  90.00 105.90  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      0.009814  0.000000  0.002795        0.00000
SCALE2      0.000000  0.013827  0.000000        0.00000
SCALE3      0.000000  0.000000  0.007700        0.00000
      
PROCHECK
Go to PROCHECK summary
 References