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PDBsum entry 1fie

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Top Page protein Protein-protein interface(s) links
Transferase PDB id
1fie
Jmol
Contents
Protein chain
705 a.a. *
Waters ×557
* Residue conservation analysis
HEADER    TRANSFERASE                             24-AUG-96   1FIE
TITLE     RECOMBINANT HUMAN COAGULATION FACTOR XIII
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: COAGULATION FACTOR XIII;
COMPND   3 CHAIN: A, B;
COMPND   4 FRAGMENT: A-SUBUNIT (THROMBIN-CLEAVED);
COMPND   5 EC: 2.3.2.13;
COMPND   6 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 ORGAN: PLACENTA;
SOURCE   6 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE   7 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 4932
KEYWDS    TRANSFERASE, ACYLTRANSFERASE, BLOOD COAGULATION
EXPDTA    X-RAY DIFFRACTION
AUTHOR    V.C.YEE,D.C.TELLER
REVDAT   2   24-FEB-09 1FIE    1       VERSN
REVDAT   1   12-FEB-97 1FIE    0
JRNL        AUTH   V.C.YEE,L.C.PEDERSEN,P.D.BISHOP,R.E.STENKAMP,
JRNL        AUTH 2 D.C.TELLER
JRNL        TITL   STRUCTURAL EVIDENCE THAT THE ACTIVATION PEPTIDE IS
JRNL        TITL 2 NOT RELEASED UPON THROMBIN CLEAVAGE OF FACTOR XIII.
JRNL        REF    THROMB.RES.                   V.  78   389 1995
JRNL        REFN                   ISSN 0049-3848
JRNL        PMID   7660355
JRNL        DOI    10.1016/0049-3848(95)00072-Y
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   L.C.PEDERSEN,V.C.YEE,P.D.BISHOP,I.LE TRONG,
REMARK   1  AUTH 2 D.C.TELLER,R.E.STENKAMP
REMARK   1  TITL   TRANSGLUTAMINASE FACTOR XIII USES PROTEINASE-LIKE
REMARK   1  TITL 2 CATALYTIC TRIAD TO CROSSLINK MACROMOLECULES
REMARK   1  REF    PROTEIN SCI.                  V.   3  1131 1994
REMARK   1  REFN                   ISSN 0961-8368
REMARK   1 REFERENCE 2
REMARK   1  AUTH   V.C.YEE,L.C.PEDERSEN,I.LE TRONG,P.D.BISHOP,
REMARK   1  AUTH 2 R.E.STENKAMP,D.C.TELLER
REMARK   1  TITL   THREE-DIMENSIONAL STRUCTURE OF A TRANSGLUTAMINASE:
REMARK   1  TITL 2 HUMAN BLOOD COAGULATION FACTOR XIII
REMARK   1  REF    PROC.NATL.ACAD.SCI.USA        V.  91  7296 1994
REMARK   1  REFN                   ISSN 0027-8424
REMARK   1 REFERENCE 3
REMARK   1  AUTH   P.D.BISHOP,D.C.TELLER,R.A.SMITH,G.W.LASSER,
REMARK   1  AUTH 2 T.GILBERT,R.L.SEALE
REMARK   1  TITL   EXPRESSION, PURIFICATION, AND CHARACTERIZATION OF
REMARK   1  TITL 2 HUMAN FACTOR XIII IN SACCHAROMYCES CEREVISIAE
REMARK   1  REF    BIOCHEMISTRY                  V.  29  1861 1990
REMARK   1  REFN                   ISSN 0006-2960
REMARK   2
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : X-PLOR
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)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 77.0
REMARK   3   NUMBER OF REFLECTIONS             : 49681
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL
REMARK   3   R VALUE            (WORKING SET) : 0.182
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            : 11372
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 0
REMARK   3   SOLVENT ATOMS            : 557
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.90
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) : 0.011
REMARK   3   BOND ANGLES            (DEGREES) : 1.92
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 25.21
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.46
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  ; 1.500
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; 2.000
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; 2.000
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; 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  : NULL
REMARK   3  TOPOLOGY FILE  1   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1FIE COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
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        : 01-AUG-94
REMARK 200  TEMPERATURE           (KELVIN) : NULL
REMARK 200  PH                             : 6.
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : NULL
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : NULL
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
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : R-AXIS
REMARK 200  DATA SCALING SOFTWARE          : R-AXIS
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 50732
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 77.7
REMARK 200  DATA REDUNDANCY                : 1.900
REMARK 200  R MERGE                    (I) : 0.06500
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: X-PLOR
REMARK 200 STARTING MODEL: NULL
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): 2.87
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.
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       36.56500
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4400 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 54100 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     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     GLU A    30
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     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     ARG B    37
REMARK 465     GLY B    38
REMARK 465     VAL B    39
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     ASP A  24    CG   OD1  OD2
REMARK 470     VAL A  29    O
REMARK 470     ARG A 727    O
REMARK 470     VAL B  34    CG1  CG2
REMARK 470     VAL B  35    CG1  CG2
REMARK 470     PRO B  36    O
REMARK 470     ASN B  40    CG   OD1  ND2
REMARK 470     LEU B  41    N    CG   CD1  CD2
REMARK 470     GLN B  42    CG   CD   OE1  NE2
REMARK 470     ARG B 727    O
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    THR A 365   N   -  CA  -  C   ANGL. DEV. = -19.1 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    LEU A  45      110.35    128.41
REMARK 500    ASN A  60      -73.13    -48.10
REMARK 500    PRO A  94       17.93    -59.82
REMARK 500    ASP A 139       82.00     40.14
REMARK 500    PRO A 166       21.86    -70.70
REMARK 500    TYR A 167      -56.00   -140.41
REMARK 500    VAL A 205      -46.45   -134.77
REMARK 500    TYR A 214     -156.15   -144.33
REMARK 500    ILE A 256      -70.46    -49.46
REMARK 500    ALA A 268       93.26    -47.75
REMARK 500    ASP A 270       87.59     61.93
REMARK 500    GLU A 272      -78.12    -91.17
REMARK 500    ASN A 281       11.10    -60.70
REMARK 500    ILE A 282      -62.62    -98.09
REMARK 500    TYR A 283       48.44     72.17
REMARK 500    ALA A 284      -20.63    -38.42
REMARK 500    TYR A 285       18.98   -147.94
REMARK 500    TRP A 292      133.22    -39.15
REMARK 500    TYR A 311      122.86     65.28
REMARK 500    PHE A 339       77.73     72.42
REMARK 500    THR A 365       68.46   -175.17
REMARK 500    ASN A 402     -151.51   -117.84
REMARK 500    GLN A 425      157.19    -39.15
REMARK 500    PHE A 426       71.92     81.87
REMARK 500    ASP A 427       27.89     37.34
REMARK 500    LYS A 446       -2.86    -54.21
REMARK 500    TYR A 500       47.61    -96.75
REMARK 500    GLU A 509      -69.59     62.87
REMARK 500    VAL A 511     -136.21    164.24
REMARK 500    SER A 514       -6.76    -53.86
REMARK 500    ARG A 515       -2.92     57.83
REMARK 500    ASP A 521      149.41   -173.31
REMARK 500    LEU A 529      124.99    -35.20
REMARK 500    LYS A 531     -164.26   -101.96
REMARK 500    MET A 595      -29.96    -39.34
REMARK 500    LEU A 598      144.21    -38.81
REMARK 500    GLU A 600      -41.10    -25.62
REMARK 500    ASN A 613      -38.76    -37.92
REMARK 500    ARG A 616       43.78     33.20
REMARK 500    ASN A 654       99.27    -63.69
REMARK 500    LYS A 657       43.29    -84.72
REMARK 500    PRO A 685      108.60    -46.42
REMARK 500    ASN A 686       24.83     82.69
REMARK 500    ARG A 703     -169.70   -120.39
REMARK 500    SER A 713      -91.16   -103.49
REMARK 500    HIS A 716       41.03     79.16
REMARK 500    VAL B  35      -67.82    -23.58
REMARK 500    PRO B  91      147.48    -37.33
REMARK 500    PRO B  94        4.63    -56.18
REMARK 500    ARG B  95      -77.00   -109.53
REMARK 500    MET B 136      131.68   -174.24
REMARK 500    ARG B 140      -10.80     70.90
REMARK 500    ARG B 174      107.30    -43.20
REMARK 500    GLU B 189      -33.05    -38.68
REMARK 500    TYR B 214     -146.20   -133.46
REMARK 500    ASP B 219       55.68   -164.37
REMARK 500    ARG B 252        4.07    -58.44
REMARK 500    LYS B 269       59.41    -90.30
REMARK 500    ASP B 270      127.04     64.92
REMARK 500    ASP B 271      -32.36     57.77
REMARK 500    GLU B 272      -91.23    -84.44
REMARK 500    TYR B 283       66.25     71.67
REMARK 500    TYR B 285       50.42   -108.41
REMARK 500    TYR B 311      113.22     81.81
REMARK 500    GLN B 313     -166.67   -127.48
REMARK 500    PHE B 339       85.84     67.85
REMARK 500    ALA B 341       74.56   -101.20
REMARK 500    ASP B 357       13.35    -66.78
REMARK 500    TRP B 375     -158.07   -114.47
REMARK 500    GLN B 400      144.42   -170.77
REMARK 500    PHE B 426       67.57     91.50
REMARK 500    LYS B 446      -17.56    -39.58
REMARK 500    GLU B 453      -71.77    -74.13
REMARK 500    ALA B 457        4.86    -69.56
REMARK 500    GLU B 509     -164.89     51.70
REMARK 500    MET B 512       16.48   -165.56
REMARK 500    LYS B 513      168.77    171.50
REMARK 500    SER B 514      -20.56   -145.26
REMARK 500    ARG B 515       11.80     53.17
REMARK 500    ASP B 521      148.98   -179.41
REMARK 500    LYS B 569      118.26   -174.07
REMARK 500    GLN B 597        2.07   -156.31
REMARK 500    ILE B 612       32.46    -79.60
REMARK 500    ASN B 613      -77.39     31.85
REMARK 500    GLU B 614      -75.60    -54.51
REMARK 500    ARG B 616       62.72    -43.05
REMARK 500    GLU B 631      176.55    -58.27
REMARK 500    GLN B 640       45.42    -86.03
REMARK 500    VAL B 672      -53.00   -134.33
REMARK 500    SER B 713      -86.78    -98.02
REMARK 500    HIS B 716       36.18     79.78
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 945        DISTANCE =  5.11 ANGSTROMS
REMARK 525    HOH B 978        DISTANCE =  6.89 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CAT
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE, CATALYTIC TRIAD.
REMARK 800 SITE_IDENTIFIER: CBT
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE, CATALYTIC TRIAD.
DBREF  1FIE A    1   731  UNP    P00488   F13A_HUMAN      31    761
DBREF  1FIE B    1   731  UNP    P00488   F13A_HUMAN      31    761
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 ILE
SEQRES  51 A  731  GLN 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 ILE
SEQRES  51 B  731  GLN 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
FORMUL   3  HOH   *557(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 SER A  295  SER A  305  1                                  11
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 ILE A  477  THR A  480  5                                   4
HELIX   12  12 GLU A  488  TYR A  500  1                                  13
HELIX   13  13 ALA A  591  TYR A  594  1                                   4
HELIX   14  14 THR B   59  HIS B   64  1                                   6
HELIX   15  15 GLU B  111  LYS B  113  5                                   3
HELIX   16  16 PRO B  176  THR B  178  5                                   3
HELIX   17  17 GLU B  198  TYR B  204  1                                   7
HELIX   18  18 ILE B  234  ARG B  244  1                                  11
HELIX   19  19 PRO B  255  ALA B  264  1                                  10
HELIX   20  20 SER B  295  SER B  305  1                                  11
HELIX   21  21 CYS B  314  CYS B  327  1                                  14
HELIX   22  22 VAL B  414  HIS B  419  1                                   6
HELIX   23  23 ALA B  428  ASN B  436  1                                   9
HELIX   24  24 THR B  478  TYR B  481  1                                   4
HELIX   25  25 GLU B  488  TYR B  500  1                                  13
HELIX   26  26 ARG B  515  ASN B  517  5                                   3
HELIX   27  27 ALA B  591  GLU B  593  5                                   3
HELIX   28  28 MET B  595  GLN B  597  5                                   3
HELIX   29  29 ASN B  613  THR B  615  5                                   3
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  ILE A 146 -1  N  ILE A 146   O  PHE A  82
SHEET    4   B 4 ILE A 134  ARG A 137 -1  N  MET A 136   O  ARG A 143
SHEET    1   C 4 TYR A 116  PRO A 120  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  TRP A 164 -1  N  ALA A 162   O  ARG A 100
SHEET    4   C 4 VAL A 169  ARG A 171 -1  N  LEU A 170   O  VAL A 163
SHEET    1   D 2 ILE A 209  GLU A 216  0
SHEET    2   D 2 ASP A 219  SER A 226 -1  N  TRP A 225   O  GLY A 210
SHEET    1   E 4 LEU A 463  VAL A 465  0
SHEET    2   E 4 ALA A 332  TYR A 338 -1  N  TYR A 338   O  LEU A 463
SHEET    3   E 4 TYR A 372  MET A 380 -1  N  GLU A 377   O  ARG A 333
SHEET    4   E 4 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 PHE A 582  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  ILE A 557 -1  N  THR A 550   O  ARG A 611
SHEET    4   H 4 ALA A 566  LEU A 577 -1  N  LEU A 577   O  TYR A 547
SHEET    1   I 2 SER A 554  THR A 558  0
SHEET    2   I 2 SER A 603  PHE A 607 -1  N  PHE A 607   O  SER A 554
SHEET    1   J 3 ILE A 633  GLY A 638  0
SHEET    2   J 3 ASP A 645  THR A 653 -1  N  GLN A 651   O  ILE A 633
SHEET    3   J 3 THR A 688  ARG A 696 -1  N  CYS A 695   O  MET A 646
SHEET    1   K 4 MET A 676  PHE A 680  0
SHEET    2   K 4 VAL A 663  ASP A 668 -1  N  LEU A 667   O  MET A 676
SHEET    3   K 4 LEU A 705  SER A 710 -1  N  SER A 710   O  TRP A 664
SHEET    4   K 4 ARG A 715  LEU A 721 -1  N  LEU A 721   O  LEU A 705
SHEET    1   L 5 VAL B  29  LEU B  31  0
SHEET    2   L 5 GLY B 168  ARG B 171 -1  N  VAL B 169   O  GLU B  30
SHEET    3   L 5 ARG B 158  THR B 165 -1  N  THR B 165   O  GLY B 168
SHEET    4   L 5 PHE B  99  VAL B 104 -1  N  VAL B 104   O  ARG B 158
SHEET    5   L 5 TYR B 116  PRO B 120 -1  N  VAL B 119   O  VAL B 101
SHEET    1   M 3 LEU B  74  ARG B  77  0
SHEET    2   M 3 THR B 180  LEU B 183  1  N  TYR B 181   O  LEU B  74
SHEET    3   M 3 GLY B 155  PHE B 157 -1  N  PHE B 157   O  THR B 180
SHEET    1   N 4 VAL B  47  LEU B  52  0
SHEET    2   N 4 PHE B  82  PHE B  88 -1  N  ASP B  87   O  THR B  48
SHEET    3   N 4 SER B 141  GLN B 147 -1  N  ILE B 146   O  PHE B  82
SHEET    4   N 4 GLY B 131  MET B 136 -1  N  MET B 136   O  ARG B 143
SHEET    1   O 2 ILE B 209  GLU B 216  0
SHEET    2   O 2 ASP B 219  SER B 226 -1  N  TRP B 225   O  GLY B 210
SHEET    1   P 5 MET B 474  ASP B 476  0
SHEET    2   P 5 LEU B 463  LYS B 467 -1  N  THR B 466   O  MET B 475
SHEET    3   P 5 ALA B 332  TYR B 338 -1  N  TYR B 338   O  LEU B 463
SHEET    4   P 5 TYR B 372  MET B 380 -1  N  GLU B 377   O  ARG B 333
SHEET    5   P 5 GLY B 391  VAL B 395 -1  N  VAL B 395   O  ASN B 376
SHEET    1   Q 3 GLN B 349  LEU B 354  0
SHEET    2   Q 3 ASP B 438  LYS B 445  1  N  ASP B 438   O  MET B 350
SHEET    3   Q 3 THR B 449  VAL B 452 -1  N  VAL B 451   O  THR B 443
SHEET    1   R 3 VAL B 518  VAL B 524  0
SHEET    2   R 3 PHE B 533  ASN B 541 -1  N  ARG B 540   O  ASP B 519
SHEET    3   R 3 LYS B 584  ILE B 589 -1  N  ILE B 589   O  PHE B 533
SHEET    1   S 4 VAL B 618  VAL B 626  0
SHEET    2   S 4 SER B 603  ARG B 611 -1  N  ALA B 610   O  LEU B 619
SHEET    3   S 4 ALA B 551  THR B 558 -1  N  THR B 558   O  SER B 603
SHEET    4   S 4 ALA B 566  PHE B 573 -1  N  PHE B 573   O  ALA B 551
SHEET    1   T 3 ILE B 633  GLY B 638  0
SHEET    2   T 3 ASP B 645  THR B 653 -1  N  GLN B 651   O  ILE B 633
SHEET    3   T 3 THR B 688  ARG B 696 -1  N  CYS B 695   O  MET B 646
SHEET    1   U 4 MET B 676  PHE B 680  0
SHEET    2   U 4 VAL B 663  ASP B 668 -1  N  LEU B 667   O  MET B 676
SHEET    3   U 4 GLY B 701  SER B 710 -1  N  SER B 710   O  TRP B 664
SHEET    4   U 4 ARG B 715  ILE B 725 -1  N  ILE B 725   O  GLY B 701
SHEET    1   V 2 LEU A 275  GLY A 277  0
SHEET    2   V 2 VAL A 309  GLY A 312  1  N  VAL A 309   O  VAL A 276
SHEET    1   W 2 LEU B 275  GLY B 277  0
SHEET    2   W 2 VAL B 309  GLY B 312  1  N  VAL B 309   O  VAL B 276
CISPEP   1 GLY A  410    PRO A  411          0         0.20
CISPEP   2 GLY B  410    PRO B  411          0        -0.29
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
CRYST1  101.100   73.130  134.700  90.00 106.40  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      0.009891  0.000000  0.002911        0.00000
SCALE2      0.000000  0.013674  0.000000        0.00000
SCALE3      0.000000  0.000000  0.007739        0.00000
      
PROCHECK
Go to PROCHECK summary
 References