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PDBsum entry 1evu

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Top Page protein ligands metals Protein-protein interface(s) links
Transferase PDB id
1evu
Jmol
Contents
Protein chain
708 a.a. *
Ligands
PGO
Metals
_CA ×2
Waters ×1159
* Residue conservation analysis
HEADER    TRANSFERASE                             20-APR-00   1EVU
TITLE     HUMAN FACTOR XIII WITH CALCIUM BOUND IN THE ION SITE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: COAGULATION FACTOR XIII;
COMPND   3 CHAIN: A, B;
COMPND   4 EC: 2.3.2.13;
COMPND   5 ENGINEERED: YES
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;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: ZM118
KEYWDS    TRANSGLUTAMINASE, BLOOD COAGULATION, CALCIUM, TRANSFERASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    R.J.GARZON,K.P.PRATT,P.D.BISHOP,I.LE TRONG,R.E.STENKAMP,
AUTHOR   2 D.C.TELLER
REVDAT   2   24-FEB-09 1EVU    1       VERSN
REVDAT   1   10-MAY-00 1EVU    0
JRNL        AUTH   R.J.GARZON,K.P.PRATT,P.D.BISHOP,I.LE TRONG,
JRNL        AUTH 2 R.E.STENKAMP,D.C.TELLER
JRNL        TITL   TRYPTOPHAN 279 IS ESSENTIAL FOR THE
JRNL        TITL 2 TRANSGLUTAMINASE ACTIVITY OF COAGULATION FACTOR
JRNL        TITL 3 XIII: FUNCTIONAL AND STRUCTURAL CHARACTERIZATION
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   B.A.FOX,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   IDENTIFICATION OF THE CALCIUM BINDING SITE AND A
REMARK   1  TITL 2 NOVEL YTTERBIUM SITE IN BLOOD COAGULATION FACTOR
REMARK   1  TITL 3 XIII BY X-RAY CRYSTALLOGRAPHY
REMARK   1  REF    J.BIOL.CHEM.                  V. 274  4917 1999
REMARK   1  REFN                   ISSN 0021-9258
REMARK   1  DOI    10.1074/JBC.274.8.4917
REMARK   2
REMARK   2 RESOLUTION.    2.01 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.01
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.66
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 92.0
REMARK   3   NUMBER OF REFLECTIONS             : 110289
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : SAME AS 1GGU
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL
REMARK   3   R VALUE            (WORKING SET) : 0.208
REMARK   3   FREE R VALUE                     : 0.266
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 5532
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 11427
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 7
REMARK   3   SOLVENT ATOMS            : 1159
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 23.30
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 42.40
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -8.16000
REMARK   3    B22 (A**2) : 7.87000
REMARK   3    B33 (A**2) : 0.29000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 3.11000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): NULL
REMARK   3   ESU BASED ON FREE R VALUE                       (A): NULL
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA
REMARK   3    BOND LENGTH                     (A) : 0.013 ; NULL
REMARK   3    ANGLE DISTANCE                  (A) : 2.700 ; NULL
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL
REMARK   3
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL
REMARK   3
REMARK   3   NON-BONDED CONTACT RESTRAINTS.
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL
REMARK   3
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : 2.330 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 3.260 ; 2.000
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.650 ; 2.000
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.720 ; 2.500
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: THIS ENTRY IS THE FURTHER REFINEMENT
REMARK   3  OF THE 1GGU PDB COORDINATES (FOX ET AL, 1999). THE CRYSTALS OF
REMARK   3  THIS ZYMOGEN CONTAIN 90 MM CACL2 AND DIFFRACT TO 2.0 A
REMARK   3  RESOLUTION. THE CHANGES TO THE 1GGU MODEL INCLUDE EXTENSION OF
REMARK   3  THE ACTIVATION PEPTIDE OF SUBUNIT 1 TO THE N-ACETYL SER AT
REMARK   3  POSITION 1, REFITTING OF SOME RESIDUES, ADDITION AND DELETION
REMARK   3  OF WATER MOLECULES, AND INSERTION OF ALTERNATE CONFORMATIONS
REMARK   3  FOR SEVEN RESIDUES. THE PURPOSE FOR THE FURTHER REFINEMENT IS
REMARK   3  FOR COMPARISON WITH THE W279F MUTANT OF FACTOR XIII
REMARK   4
REMARK   4 1EVU COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-APR-00.
REMARK 100 THE RCSB ID CODE IS RCSB010939.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-JUN-97
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 6.2
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : SSRL
REMARK 200  BEAMLINE                       : BL9-1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 111498
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.660
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.5
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : 0.04300
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) : 2.00
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.03
REMARK 200  COMPLETENESS FOR SHELL     (%) : 76.0
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : 0.66900
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: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 55.03
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.73
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 24% 1,2-PROPANEDIOL, 100 MM SODIUM
REMARK 280  POTASSIUM PHOSPHATE BUFFER. TO INCORPORATE CALCIUM, THE
REMARK 280  CRYSTALS WERE TRANSFERRED TO 24% 1,2-PROPANEDIOL AND MES
REMARK 280  BUFFER AND SOAKED FOR 1-2 DAYS IN 90 MM CACL2, PH 6.2, VAPOR
REMARK 280  DIFFUSION, TEMPERATURE 294K
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       35.38200
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: 6010 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 53710 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 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     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   509
REMARK 465     GLY A   510
REMARK 465     VAL A   511
REMARK 465     MET A   512
REMARK 465     LYS A   513
REMARK 465     SER A   514
REMARK 465     ARG A   515
REMARK 465     ARG A   728
REMARK 465     PRO A   729
REMARK 465     SER A   730
REMARK 465     MET A   731
REMARK 465     SAC 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     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     LEU B    41
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   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     ARG A   5    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG B 515    CG   CD   NE   CZ   NH1  NH2
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   290     ND1  HIS A   716              2.09
REMARK 500   O    GLU A   272     O    HOH A  1507              2.14
REMARK 500   O    VAL A   672     O    HOH A  1332              2.17
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    ARG A  12   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.3 DEGREES
REMARK 500    ASP A  24   CB  -  CG  -  OD1 ANGL. DEV. =   5.7 DEGREES
REMARK 500    ARG A  56   NE  -  CZ  -  NH1 ANGL. DEV. =   4.6 DEGREES
REMARK 500    TYR A  69   CB  -  CG  -  CD2 ANGL. DEV. =  -4.2 DEGREES
REMARK 500    ARG A  77   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.4 DEGREES
REMARK 500    TYR A  83   CB  -  CG  -  CD2 ANGL. DEV. =  -4.3 DEGREES
REMARK 500    ASP A  87   CB  -  CG  -  OD1 ANGL. DEV. =   7.0 DEGREES
REMARK 500    ARG A 100   CD  -  NE  -  CZ  ANGL. DEV. =  19.0 DEGREES
REMARK 500    ARG A 100   NE  -  CZ  -  NH1 ANGL. DEV. =   4.4 DEGREES
REMARK 500    VAL A 104   CA  -  CB  -  CG2 ANGL. DEV. =  10.2 DEGREES
REMARK 500    ARG A 107   NE  -  CZ  -  NH1 ANGL. DEV. =   4.5 DEGREES
REMARK 500    ARG A 137   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.9 DEGREES
REMARK 500    ARG A 143   CD  -  NE  -  CZ  ANGL. DEV. =   8.9 DEGREES
REMARK 500    ARG A 143   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.1 DEGREES
REMARK 500    ARG A 158   CD  -  NE  -  CZ  ANGL. DEV. =   9.0 DEGREES
REMARK 500    ARG A 158   NE  -  CZ  -  NH1 ANGL. DEV. =   5.6 DEGREES
REMARK 500    ARG A 171   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.2 DEGREES
REMARK 500    ARG A 174   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES
REMARK 500    ASP A 190   CB  -  CG  -  OD1 ANGL. DEV. =   7.5 DEGREES
REMARK 500    ARG A 201   CD  -  NE  -  CZ  ANGL. DEV. =   9.3 DEGREES
REMARK 500    LYS A 221   CA  -  CB  -  CG  ANGL. DEV. =  14.0 DEGREES
REMARK 500    ARG A 223   NE  -  CZ  -  NH1 ANGL. DEV. =   5.5 DEGREES
REMARK 500    ARG A 223   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.3 DEGREES
REMARK 500    MET A 242   CG  -  SD  -  CE  ANGL. DEV. =  10.3 DEGREES
REMARK 500    ARG A 244   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES
REMARK 500    ARG A 260   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES
REMARK 500    CYS A 314   CA  -  CB  -  SG  ANGL. DEV. =   7.4 DEGREES
REMARK 500    ARG A 326   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.1 DEGREES
REMARK 500    VAL A 335   CA  -  CB  -  CG1 ANGL. DEV. =   9.2 DEGREES
REMARK 500    ASP A 357   CB  -  CG  -  OD2 ANGL. DEV. =   9.5 DEGREES
REMARK 500    ARG A 382   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES
REMARK 500    GLU A 401   CG  -  CD  -  OE1 ANGL. DEV. =  13.4 DEGREES
REMARK 500    ASP A 476   CB  -  CG  -  OD1 ANGL. DEV. =   6.3 DEGREES
REMARK 500    ASP A 479   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES
REMARK 500    ASP A 532   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES
REMARK 500    ASP A 532   CB  -  CG  -  OD2 ANGL. DEV. =  -6.5 DEGREES
REMARK 500    ARG A 540   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 DEGREES
REMARK 500    GLU A 593   OE1 -  CD  -  OE2 ANGL. DEV. =  -8.3 DEGREES
REMARK 500    TYR A 594   CB  -  CG  -  CD2 ANGL. DEV. =   3.8 DEGREES
REMARK 500    ARG A 674   CD  -  NE  -  CZ  ANGL. DEV. =   9.3 DEGREES
REMARK 500    ARG A 684   CD  -  NE  -  CZ  ANGL. DEV. =   8.8 DEGREES
REMARK 500    ARG A 703   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.6 DEGREES
REMARK 500    ARG B  11   NE  -  CZ  -  NH1 ANGL. DEV. =   4.7 DEGREES
REMARK 500    ARG B  11   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.4 DEGREES
REMARK 500    GLU B  23   OE1 -  CD  -  OE2 ANGL. DEV. =  -8.8 DEGREES
REMARK 500    GLU B  30   OE1 -  CD  -  OE2 ANGL. DEV. =  -7.5 DEGREES
REMARK 500    ARG B  56   NH1 -  CZ  -  NH2 ANGL. DEV. =   9.2 DEGREES
REMARK 500    ARG B  56   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES
REMARK 500    ARG B  56   NE  -  CZ  -  NH2 ANGL. DEV. = -12.8 DEGREES
REMARK 500    HIS B  64   CE1 -  NE2 -  CD2 ANGL. DEV. =   5.3 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS      99 ANGLE DEVIATIONS.
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    THR A   6      141.75     85.61
REMARK 500    ASP A 139     -123.77     52.65
REMARK 500    ASP A 196       52.71    -90.59
REMARK 500    TYR A 214     -154.17   -140.17
REMARK 500    ASP A 219       69.06   -164.59
REMARK 500    ASP A 270     -125.43     63.58
REMARK 500    ASN A 281       -7.74     77.04
REMARK 500    TYR A 283       37.30     70.29
REMARK 500    TRP A 292      147.54    -34.68
REMARK 500    PHE A 339       81.98     68.14
REMARK 500    PRO A 386      156.69    -46.17
REMARK 500    ASN A 402     -153.96   -120.78
REMARK 500    ASN A 517       11.86     87.27
REMARK 500    THR A 561        4.92    -68.09
REMARK 500    LEU A 580       78.25     10.80
REMARK 500    GLN A 601      -14.86     81.75
REMARK 500    ARG A 616        9.20     58.43
REMARK 500    GLN A 640       77.50   -109.60
REMARK 500    ASN A 662       68.79     33.87
REMARK 500    PRO A 685      118.53    -37.61
REMARK 500    ASN A 686       -4.16     77.38
REMARK 500    ARG A 703     -156.46   -112.34
REMARK 500    SER A 713      -81.47   -116.55
REMARK 500    VAL B  34     -179.86    -69.20
REMARK 500    LEU B  45      117.52    120.01
REMARK 500    GLU B 138      115.55   -161.62
REMARK 500    ASP B 139     -125.68     58.41
REMARK 500    VAL B 205      -56.37   -120.90
REMARK 500    ASP B 219       76.83   -159.17
REMARK 500    ASP B 270     -134.32     52.05
REMARK 500    ASN B 281       -0.77     81.34
REMARK 500    PHE B 339       79.87     58.60
REMARK 500    ALA B 346       10.40     58.68
REMARK 500    PRO B 386      158.89    -48.59
REMARK 500    ASN B 402     -159.12   -118.28
REMARK 500    GLU B 453      -69.39   -100.96
REMARK 500    GLN B 484      130.12    -28.43
REMARK 500    LYS B 570       84.76   -150.95
REMARK 500    GLN B 601       -2.35     80.19
REMARK 500    ALA B 602       54.58     39.66
REMARK 500    ASN B 654      105.10    -59.18
REMARK 500    LEU B 656      171.17    -58.35
REMARK 500    SER B 713      -99.83   -110.48
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500                                 MODEL     OMEGA
REMARK 500 GLU A    2     THR A    3                 -146.51
REMARK 500 THR A    3     SER A    4                  148.96
REMARK 500 GLY A  596     GLN A  597                 -147.73
REMARK 500 GLN B   32     GLY B   33                  140.23
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500  M RES CSSEQI        ANGLE
REMARK 500    ARG A  12        -10.46
REMARK 500    ILE A 105         12.53
REMARK 500    ILE B  75         11.28
REMARK 500    ILE B 632         10.42
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 A1442        DISTANCE =  5.60 ANGSTROMS
REMARK 525    HOH A1532        DISTANCE =  5.61 ANGSTROMS
REMARK 525    HOH A1575        DISTANCE =  5.61 ANGSTROMS
REMARK 525    HOH B1676        DISTANCE =  6.65 ANGSTROMS
REMARK 525    HOH A1725        DISTANCE =  5.27 ANGSTROMS
REMARK 525    HOH B1792        DISTANCE =  5.34 ANGSTROMS
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                              CA A1201  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A1363   O
REMARK 620 2 HOH A1454   O    85.0
REMARK 620 3 HOH A1469   O   142.1 104.9
REMARK 620 4 HOH A1331   O    77.5 100.3  64.8
REMARK 620 5 ALA A 457   O    96.4  99.4 117.2 158.8
REMARK 620 6 HOH A1468   O    84.3 169.0  85.1  79.8  79.4
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA B1202  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B1309   O
REMARK 620 2 HOH B1409   O    98.8
REMARK 620 3 ALA B 457   O   152.9  99.1
REMARK 620 4 HOH B1474   O    73.8 157.8  82.0
REMARK 620 5 HOH B1512   O   125.5  78.1  78.2 123.4
REMARK 620 6 HOH B1282   O    69.0  76.1  95.9  81.7 152.3
REMARK 620 N                    1     2     3     4     5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1201
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 1202
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGO B 1203
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1GGU   RELATED DB: PDB
DBREF  1EVU A    1   731  UNP    P00488   F13A_HUMAN       1    731
DBREF  1EVU B    1   731  UNP    P00488   F13A_HUMAN       1    731
SEQADV 1EVU SAC A    1  UNP  P00488    SER     1 MODIFIED RESIDUE
SEQADV 1EVU SAC B    1  UNP  P00488    SER     1 MODIFIED RESIDUE
SEQRES   1 A  731  SAC 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  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  SAC 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  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
MODRES 1EVU SAC A    1  SER  N-ACETYL-SERINE
HET    SAC  A   1       9
HET     CA  A1201       1
HET     CA  B1202       1
HET    PGO  B1203       5
HETNAM     SAC N-ACETYL-SERINE
HETNAM      CA CALCIUM ION
HETNAM     PGO S-1,2-PROPANEDIOL
FORMUL   1  SAC    C5 H9 N O4
FORMUL   3   CA    2(CA 2+)
FORMUL   5  PGO    C3 H8 O2
FORMUL   6  HOH   *1159(H2 O)
HELIX    1   1 ASP A   58  HIS A   64  1                                   7
HELIX    2   2 GLN A  110  GLY A  114  5                                   5
HELIX    3   3 ASN A  175  THR A  178  5                                   4
HELIX    4   4 ASN A  197  VAL A  205  1                                   9
HELIX    5   5 GLY A  233  ALA A  245  1                                  13
HELIX    6   6 ASP A  248  ARG A  252  5                                   5
HELIX    7   7 ASN A  254  ASN A  267  1                                  14
HELIX    8   8 SER A  295  GLU A  306  1                                  12
HELIX    9   9 GLN A  313  GLY A  329  1                                  17
HELIX   10  10 VAL A  414  GLY A  420  1                                   7
HELIX   11  11 ASP A  427  SER A  437  1                                  11
HELIX   12  12 ILE A  477  LYS A  482  1                                   6
HELIX   13  13 GLN A  487  TYR A  500  1                                  14
HELIX   14  14 GLN A  590  TYR A  594  5                                   5
HELIX   15  15 ASP B   58  HIS B   64  1                                   7
HELIX   16  16 GLN B  110  GLY B  114  5                                   5
HELIX   17  17 ASN B  175  THR B  178  5                                   4
HELIX   18  18 ASN B  197  VAL B  205  1                                   9
HELIX   19  19 GLY B  233  ALA B  245  1                                  13
HELIX   20  20 ASP B  248  ARG B  252  5                                   5
HELIX   21  21 ASN B  254  ASN B  267  1                                  14
HELIX   22  22 PRO B  288  TRP B  292  5                                   5
HELIX   23  23 SER B  295  GLU B  306  1                                  12
HELIX   24  24 GLN B  313  GLY B  329  1                                  17
HELIX   25  25 VAL B  414  GLY B  420  1                                   7
HELIX   26  26 ASP B  427  SER B  437  1                                  11
HELIX   27  27 ILE B  477  LYS B  482  1                                   6
HELIX   28  28 GLN B  487  MET B  499  1                                  13
HELIX   29  29 GLN B  590  TYR B  594  5                                   5
SHEET    1   A 5 VAL A  47  HIS A  51  0
SHEET    2   A 5 PHE A  82  PHE A  88 -1  N  GLN A  85   O  HIS A  51
SHEET    3   A 5 SER A 141  GLN A 147 -1  N  VAL A 142   O  ILE A  86
SHEET    4   A 5 GLY A 131  GLU A 138 -1  O  GLY A 131   N  GLN A 147
SHEET    5   A 5 ILE A 121  VAL A 122  1  N  VAL A 122   O  ALA A 132
SHEET    1   B 4 TYR A 116  VAL A 119  0
SHEET    2   B 4 PHE A  99  VAL A 104 -1  O  VAL A 101   N  VAL A 119
SHEET    3   B 4 GLY A 155  THR A 165 -1  N  ARG A 158   O  VAL A 104
SHEET    4   B 4 GLY A 168  ARG A 171 -1  O  GLY A 168   N  THR A 165
SHEET    1   C 5 TYR A 116  VAL A 119  0
SHEET    2   C 5 PHE A  99  VAL A 104 -1  O  VAL A 101   N  VAL A 119
SHEET    3   C 5 GLY A 155  THR A 165 -1  N  ARG A 158   O  VAL A 104
SHEET    4   C 5 THR A 180  LEU A 183 -1  O  THR A 180   N  PHE A 157
SHEET    5   C 5 LEU A  74  ARG A  77  1  O  LEU A  74   N  TYR A 181
SHEET    1   D 2 ILE A 209  GLU A 216  0
SHEET    2   D 2 ASP A 219  SER A 226 -1  N  ASP A 219   O  GLU A 216
SHEET    1   E 2 LEU A 275  GLY A 277  0
SHEET    2   E 2 VAL A 309  GLY A 312  1  O  VAL A 309   N  VAL A 276
SHEET    1   F 6 GLY A 405  SER A 413  0
SHEET    2   F 6 GLY A 391  ASN A 402 -1  N  ALA A 394   O  ALA A 412
SHEET    3   F 6 TRP A 370  MET A 380 -1  N  ASN A 376   O  VAL A 395
SHEET    4   F 6 ALA A 332  SER A 340 -1  O  ARG A 333   N  GLU A 377
SHEET    5   F 6 LEU A 463  LYS A 467 -1  O  LEU A 463   N  TYR A 338
SHEET    6   F 6 MET A 474  ASP A 476 -1  N  MET A 475   O  THR A 466
SHEET    1   G 3 GLN A 349  LEU A 354  0
SHEET    2   G 3 ASP A 438  ALA A 444  1  O  ASP A 438   N  MET A 350
SHEET    3   G 3 HIS A 450  ASP A 456 -1  O  VAL A 451   N  THR A 443
SHEET    1   H 3 VAL A 518  VAL A 524  0
SHEET    2   H 3 PHE A 533  ASN A 541 -1  N  SER A 536   O  GLU A 523
SHEET    3   H 3 SER A 581  ILE A 589 -1  N  SER A 581   O  ASN A 541
SHEET    1   I 4 PRO A 564  LEU A 577  0
SHEET    2   I 4 TYR A 547  THR A 558 -1  O  TYR A 547   N  LEU A 577
SHEET    3   I 4 SER A 603  ILE A 612 -1  O  SER A 603   N  THR A 558
SHEET    4   I 4 VAL A 618  VAL A 626 -1  O  LEU A 619   N  ALA A 610
SHEET    1   J 3 ILE A 633  GLY A 638  0
SHEET    2   J 3 MET A 646  THR A 653 -1  N  THR A 647   O  ARG A 637
SHEET    3   J 3 THR A 688  CYS A 695 -1  N  VAL A 689   O  PHE A 652
SHEET    1   K 4 MET A 676  ILE A 683  0
SHEET    2   K 4 LEU A 660  ASP A 668 -1  O  LEU A 660   N  ILE A 683
SHEET    3   K 4 LEU A 705  SER A 710 -1  N  ILE A 706   O  ASP A 668
SHEET    4   K 4 VAL A 717  LEU A 721 -1  O  VAL A 717   N  MET A 709
SHEET    1   L 2 GLY A 701  HIS A 702  0
SHEET    2   L 2 GLN A 724  ILE A 725 -1  O  ILE A 725   N  GLY A 701
SHEET    1   M 9 VAL B  47  HIS B  51  0
SHEET    2   M 9 SER B  81  PHE B  88 -1  O  GLN B  85   N  HIS B  51
SHEET    3   M 9 SER B 141  GLN B 147 -1  N  VAL B 142   O  ILE B  86
SHEET    4   M 9 GLY B 131  GLU B 138 -1  O  GLY B 131   N  GLN B 147
SHEET    5   M 9 TYR B 116  VAL B 122  1  O  PRO B 120   N  ALA B 132
SHEET    6   M 9 PHE B  99  VAL B 104 -1  O  PHE B  99   N  ILE B 121
SHEET    7   M 9 GLY B 155  THR B 165 -1  N  ARG B 158   O  VAL B 104
SHEET    8   M 9 GLY B 168  ARG B 171 -1  O  GLY B 168   N  THR B 165
SHEET    9   M 9 VAL B  29  LEU B  31 -1  N  GLU B  30   O  VAL B 169
SHEET    1   N 9 VAL B  47  HIS B  51  0
SHEET    2   N 9 SER B  81  PHE B  88 -1  O  GLN B  85   N  HIS B  51
SHEET    3   N 9 SER B 141  GLN B 147 -1  N  VAL B 142   O  ILE B  86
SHEET    4   N 9 GLY B 131  GLU B 138 -1  O  GLY B 131   N  GLN B 147
SHEET    5   N 9 TYR B 116  VAL B 122  1  O  PRO B 120   N  ALA B 132
SHEET    6   N 9 PHE B  99  VAL B 104 -1  O  PHE B  99   N  ILE B 121
SHEET    7   N 9 GLY B 155  THR B 165 -1  N  ARG B 158   O  VAL B 104
SHEET    8   N 9 THR B 180  LEU B 183 -1  O  THR B 180   N  PHE B 157
SHEET    9   N 9 LEU B  74  ARG B  77  1  O  LEU B  74   N  TYR B 181
SHEET    1   O 2 ILE B 209  GLU B 216  0
SHEET    2   O 2 ASP B 219  SER B 226 -1  N  ASP B 219   O  GLU B 216
SHEET    1   P 2 LEU B 275  GLY B 277  0
SHEET    2   P 2 VAL B 309  GLY B 312  1  O  VAL B 309   N  VAL B 276
SHEET    1   Q 6 MET B 406  SER B 413  0
SHEET    2   Q 6 GLY B 391  GLU B 401 -1  N  ALA B 394   O  ALA B 412
SHEET    3   Q 6 TRP B 370  MET B 380 -1  O  ASN B 376   N  VAL B 395
SHEET    4   Q 6 ALA B 332  SER B 340 -1  N  ARG B 333   O  GLU B 377
SHEET    5   Q 6 ILE B 464  LYS B 467 -1  N  VAL B 465   O  THR B 336
SHEET    6   Q 6 MET B 474  ASP B 476 -1  N  MET B 475   O  THR B 466
SHEET    1   R 3 GLN B 349  LEU B 354  0
SHEET    2   R 3 ASP B 438  ALA B 444  1  O  ASP B 438   N  MET B 350
SHEET    3   R 3 HIS B 450  ASP B 456 -1  O  VAL B 451   N  THR B 443
SHEET    1   S 3 VAL B 518  VAL B 524  0
SHEET    2   S 3 PHE B 533  ASN B 541 -1  N  SER B 536   O  GLU B 523
SHEET    3   S 3 SER B 581  ILE B 589 -1  O  SER B 581   N  ASN B 541
SHEET    1   T 4 VAL B 618  VAL B 626  0
SHEET    2   T 4 SER B 603  ILE B 612 -1  N  LEU B 604   O  THR B 625
SHEET    3   T 4 TYR B 547  THR B 558 -1  O  THR B 550   N  ARG B 611
SHEET    4   T 4 PRO B 564  LYS B 569 -1  N  LYS B 565   O  ILE B 557
SHEET    1   U 4 VAL B 618  VAL B 626  0
SHEET    2   U 4 SER B 603  ILE B 612 -1  N  LEU B 604   O  THR B 625
SHEET    3   U 4 TYR B 547  THR B 558 -1  O  THR B 550   N  ARG B 611
SHEET    4   U 4 THR B 572  LEU B 577 -1  O  PHE B 573   N  ALA B 551
SHEET    1   V 3 ILE B 633  ARG B 637  0
SHEET    2   V 3 MET B 646  THR B 653 -1  N  THR B 647   O  ARG B 637
SHEET    3   V 3 THR B 688  CYS B 695 -1  N  VAL B 689   O  PHE B 652
SHEET    1   W 4 THR B 673  ILE B 683  0
SHEET    2   W 4 LEU B 660  GLY B 669 -1  N  LEU B 660   O  ILE B 683
SHEET    3   W 4 GLY B 701  SER B 710 -1  N  ILE B 706   O  ASP B 668
SHEET    4   W 4 VAL B 717  ILE B 725 -1  O  VAL B 717   N  MET B 709
LINK         C   SAC A   1                 N   GLU A   2     1555   1555  1.32
LINK        CA    CA A1201                 O   HOH A1363     1555   1555  2.68
LINK        CA    CA A1201                 O   HOH A1454     1555   1555  2.65
LINK        CA    CA A1201                 O   HOH A1469     1555   1555  2.62
LINK        CA    CA A1201                 O   HOH A1331     1555   1555  2.80
LINK        CA    CA A1201                 O   ALA A 457     1555   1555  2.61
LINK        CA    CA A1201                 O   HOH A1468     1555   1555  2.76
LINK        CA    CA B1202                 O   HOH B1309     1555   1555  2.73
LINK        CA    CA B1202                 O   HOH B1409     1555   1555  2.58
LINK        CA    CA B1202                 O   ALA B 457     1555   1555  2.48
LINK        CA    CA B1202                 O   HOH B1474     1555   1555  2.79
LINK        CA    CA B1202                 O   HOH B1512     1555   1555  3.17
LINK        CA    CA B1202                 O   HOH B1282     1555   1555  2.64
CISPEP   1 ARG A  310    TYR A  311          0         7.17
CISPEP   2 GLY A  410    PRO A  411          0         2.65
CISPEP   3 GLN A  425    PHE A  426          0        -0.87
CISPEP   4 ARG B  310    TYR B  311          0        -1.11
CISPEP   5 GLY B  410    PRO B  411          0         5.81
CISPEP   6 GLN B  425    PHE B  426          0        13.06
SITE     1 AC1  6 ALA A 457  HOH A1331  HOH A1363  HOH A1454
SITE     2 AC1  6 HOH A1468  HOH A1469
SITE     1 AC2  5 ALA B 457  HOH B1282  HOH B1309  HOH B1409
SITE     2 AC2  5 HOH B1474
SITE     1 AC3  7 ASP A 404  ARG A 408  HOH A1214  ASP B 404
SITE     2 AC3  7 TYR B 407  ARG B 408  HOH B1223
CRYST1  100.172   70.764  133.822  90.00 106.11  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      0.009983  0.000000  0.002883        0.00000
SCALE2      0.000000  0.014131  0.000000        0.00000
SCALE3      0.000000  0.000000  0.007778        0.00000
      
PROCHECK
Go to PROCHECK summary
 References