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PDBsum entry 1ex0

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Top Page protein ligands metals Protein-protein interface(s) links
Transferase PDB id
1ex0
Jmol
Contents
Protein chain
705 a.a. *
Ligands
PO4 ×3
PGO ×6
Metals
_CA ×2
Waters ×1306
* Residue conservation analysis
HEADER    TRANSFERASE                             28-APR-00   1EX0
TITLE     HUMAN FACTOR XIII, MUTANT W279F ZYMOGEN
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: COAGULATION FACTOR XIII A CHAIN;
COMPND   3 CHAIN: A, B;
COMPND   4 EC: 2.3.2.13;
COMPND   5 ENGINEERED: YES;
COMPND   6 MUTATION: 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;
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PD16
KEYWDS    TRANSGLUTAMINASE, BLOOD COAGULATION, MUTANT, W279F,
KEYWDS   2 OXYANION, 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 1EX0    1       VERSN
REVDAT   1   23-DEC-03 1EX0    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.    2.00 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 4.0.3.5
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.94
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.6
REMARK   3   NUMBER OF REFLECTIONS             : 117421
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL
REMARK   3   R VALUE            (WORKING SET) : 0.187
REMARK   3   FREE R VALUE                     : 0.234
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900
REMARK   3   FREE R VALUE TEST SET COUNT      : 5793
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 11417
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 47
REMARK   3   SOLVENT ATOMS            : 1306
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 16.60
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.00
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -2.84000
REMARK   3    B22 (A**2) : 3.28000
REMARK   3    B33 (A**2) : -0.43000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 2.38000
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 ; 1.500
REMARK   3    ANGLE DISTANCE                  (A) : NULL  ; 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) : 2.580 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 3.260 ; 2.000
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.570 ; 2.000
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.280 ; 2.500
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1EX0 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-MAY-00.
REMARK 100 THE RCSB ID CODE IS RCSB010981.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 17-APR-98
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 6.0
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   : 158697
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.790
REMARK 200  RESOLUTION RANGE LOW       (A) : 28.510
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : 0.04800
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 11.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.79
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.84
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : 0.40200
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 54.95
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.73
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10 - 12 % 1,2-PROPANEDIOL, 0.1 M NA
REMARK 280  -K PHOSPHATE, PH 6.0, VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 295K
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       35.32000
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 300 REMARK: THE BIOLOGICAL UNIT IS THE DIMER COMPOSED OF CHAINS
REMARK 300 A OF SUBUNIT 1 AND CHAINS B OF SUBUNIT 2. A
REMARK 300 NON-CRYSTALLOGRAPHIC TWOFOLD AXIS RELATES THE TWO
REMARK 300 DIMERS.
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: 6550 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 54930 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.0 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     SAC 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     LEU A    31
REMARK 465     GLN A    32
REMARK 465     GLY A    33
REMARK 465     VAL A    34
REMARK 465     ASN A    35
REMARK 465     LEU 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     SER 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    37
REMARK 465     GLY B    38
REMARK 465     VAL B    39
REMARK 465     ASN B    40
REMARK 465     LEU B    41
REMARK 465     MET B   512
REMARK 465     LYS B   513
REMARK 465     SER B   514
REMARK 465     ARG B   515
REMARK 465     SER B   516
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     SER A 509    OG
REMARK 470     ARG A 510    CG   CD   NE   CZ   NH1  NH2
REMARK 470     VAL B  34    CG1  CG2
REMARK 470     ASN B  35    CG   OD1  ND2
REMARK 470     LEU B  36    CG   CD1  CD2
REMARK 470     SER B 509    OG
REMARK 470     ARG B 510    CG   CD   NE   CZ   NH1  NH2
REMARK 470     SER B 511    OG
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500    ASP A  24   CB  -  CG  -  OD1 ANGL. DEV. =   6.2 DEGREES
REMARK 500    ARG A  56   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.9 DEGREES
REMARK 500    ASP A  67   CB  -  CG  -  OD1 ANGL. DEV. =   6.9 DEGREES
REMARK 500    ARG A  77   NE  -  CZ  -  NH2 ANGL. DEV. =   4.2 DEGREES
REMARK 500    ARG A  95   CD  -  NE  -  CZ  ANGL. DEV. =  30.0 DEGREES
REMARK 500    ARG A  95   NE  -  CZ  -  NH1 ANGL. DEV. =   6.3 DEGREES
REMARK 500    ARG A 100   CG  -  CD  -  NE  ANGL. DEV. =  13.2 DEGREES
REMARK 500    ARG A 100   CD  -  NE  -  CZ  ANGL. DEV. =   8.6 DEGREES
REMARK 500    ARG A 100   NE  -  CZ  -  NH2 ANGL. DEV. =   3.3 DEGREES
REMARK 500    ARG A 143   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.0 DEGREES
REMARK 500    ARG A 158   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES
REMARK 500    ARG A 158   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.4 DEGREES
REMARK 500    VAL A 193   N   -  CA  -  CB  ANGL. DEV. = -15.0 DEGREES
REMARK 500    ARG A 201   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES
REMARK 500    ARG A 223   CD  -  NE  -  CZ  ANGL. DEV. =  17.7 DEGREES
REMARK 500    ARG A 223   NE  -  CZ  -  NH1 ANGL. DEV. =   8.8 DEGREES
REMARK 500    ARG A 223   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.9 DEGREES
REMARK 500    ARG A 223   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.5 DEGREES
REMARK 500    ASP A 243   CB  -  CG  -  OD1 ANGL. DEV. =   6.0 DEGREES
REMARK 500    ARG A 244   NE  -  CZ  -  NH1 ANGL. DEV. =   4.3 DEGREES
REMARK 500    ASP A 280   CB  -  CG  -  OD2 ANGL. DEV. =   6.1 DEGREES
REMARK 500    ASP A 297   CB  -  CG  -  OD1 ANGL. DEV. =   5.8 DEGREES
REMARK 500    ARG A 303   CD  -  NE  -  CZ  ANGL. DEV. =  16.6 DEGREES
REMARK 500    ARG A 303   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.6 DEGREES
REMARK 500    ARG A 310   CD  -  NE  -  CZ  ANGL. DEV. =  31.6 DEGREES
REMARK 500    ARG A 310   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES
REMARK 500    HIS A 342   CA  -  C   -  N   ANGL. DEV. =  13.7 DEGREES
REMARK 500    HIS A 342   O   -  C   -  N   ANGL. DEV. = -11.8 DEGREES
REMARK 500    ASP A 479   CB  -  CG  -  OD1 ANGL. DEV. =   7.8 DEGREES
REMARK 500    ASP A 479   CB  -  CG  -  OD2 ANGL. DEV. =  -7.2 DEGREES
REMARK 500    ARG A 491   CD  -  NE  -  CZ  ANGL. DEV. =   8.7 DEGREES
REMARK 500    ARG A 491   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES
REMARK 500    ARG A 491   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.7 DEGREES
REMARK 500    ASN A 507   CB  -  CA  -  C   ANGL. DEV. =  12.1 DEGREES
REMARK 500    ASP A 521   CB  -  CG  -  OD1 ANGL. DEV. =   7.3 DEGREES
REMARK 500    MET A 595   CA  -  C   -  N   ANGL. DEV. =  13.0 DEGREES
REMARK 500    ARG A 611   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.4 DEGREES
REMARK 500    ARG A 611   NE  -  CZ  -  NH2 ANGL. DEV. =   4.6 DEGREES
REMARK 500    ASP A 668   CB  -  CG  -  OD1 ANGL. DEV. =   5.7 DEGREES
REMARK 500    ARG A 674   CD  -  NE  -  CZ  ANGL. DEV. =   8.4 DEGREES
REMARK 500    ASP B  24   CB  -  CG  -  OD1 ANGL. DEV. =   6.1 DEGREES
REMARK 500    ARG B  78   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES
REMARK 500    ARG B  90   CD  -  NE  -  CZ  ANGL. DEV. =  10.1 DEGREES
REMARK 500    ARG B 100   CG  -  CD  -  NE  ANGL. DEV. =  15.3 DEGREES
REMARK 500    ARG B 100   NE  -  CZ  -  NH1 ANGL. DEV. =   6.7 DEGREES
REMARK 500    ARG B 143   CD  -  NE  -  CZ  ANGL. DEV. =  19.2 DEGREES
REMARK 500    ARG B 143   NE  -  CZ  -  NH1 ANGL. DEV. =   5.5 DEGREES
REMARK 500    ARG B 143   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.8 DEGREES
REMARK 500    ARG B 158   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES
REMARK 500    ARG B 174   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.5 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS      90 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    ASP A 139     -120.79     44.70
REMARK 500    ASP A 196       35.19    -87.75
REMARK 500    TYR A 214     -155.59   -140.37
REMARK 500    ASP A 219       75.83   -155.46
REMARK 500    ASN A 281        4.59     56.00
REMARK 500    TYR A 285       45.63   -104.46
REMARK 500    PHE A 339       83.69     69.20
REMARK 500    ASN A 402     -161.87   -121.61
REMARK 500    LYS A 504       69.77   -157.40
REMARK 500    THR A 508       55.69   -109.40
REMARK 500    SER A 509       80.30    -60.30
REMARK 500    ASN A 517       24.84     80.59
REMARK 500    THR A 561        1.55    -69.70
REMARK 500    GLN A 601       -6.42     83.48
REMARK 500    SER A 713      -82.33   -122.16
REMARK 500    THR B   6      -67.17   -168.09
REMARK 500    ALA B   7       62.30     83.97
REMARK 500    VAL B  34       92.40   -161.67
REMARK 500    ARG B  96       -5.79   -142.36
REMARK 500    ASP B 139     -125.24     45.76
REMARK 500    VAL B 205      -57.36   -123.49
REMARK 500    ASP B 219       70.24   -153.53
REMARK 500    ASP B 270     -139.56     61.45
REMARK 500    ILE B 282      -50.94   -122.04
REMARK 500    GLN B 313     -165.69   -129.91
REMARK 500    PHE B 339       79.90     69.13
REMARK 500    ASN B 402     -153.63   -121.44
REMARK 500    LYS B 504       72.55   -152.22
REMARK 500    THR B 508       79.26   -112.51
REMARK 500    ARG B 510     -156.79     80.49
REMARK 500    GLN B 601      -11.19     87.02
REMARK 500    ARG B 616       19.10     52.82
REMARK 500    GLN B 640       78.17   -104.40
REMARK 500    SER B 713      -83.45   -124.96
REMARK 500    HIS B 716       40.15     70.70
REMARK 500    ARG B 728      -65.67    -97.73
REMARK 500    PRO B 729     -138.73    -88.70
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 SER A  509     ARG A  510                 -140.51
REMARK 500 PRO B  729     SER B  730                 -149.95
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 A1741        DISTANCE =  5.13 ANGSTROMS
REMARK 525    HOH A1830        DISTANCE =  6.30 ANGSTROMS
REMARK 525    HOH A1868        DISTANCE =  7.49 ANGSTROMS
REMARK 525    HOH A1883        DISTANCE =  6.23 ANGSTROMS
REMARK 525    HOH A1884        DISTANCE =  5.07 ANGSTROMS
REMARK 525    HOH A1888        DISTANCE =  6.90 ANGSTROMS
REMARK 525    HOH B1932        DISTANCE =  5.38 ANGSTROMS
REMARK 525    HOH B2065        DISTANCE =  5.66 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 A1320  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 436   O
REMARK 620 2 HOH A1518   O    76.6
REMARK 620 3 ALA A 457   O   151.0  77.9
REMARK 620 4 HOH A1408   O    77.7  87.5 114.6
REMARK 620 5 ASP A 438   OD1  87.8 119.1  92.8 146.0
REMARK 620 6 HOH A1646   O   102.4 176.6 103.8  89.1  63.9
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA B1321  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 438   OD1
REMARK 620 2 HOH B1536   O   117.5
REMARK 620 3 ALA B 457   O    92.9  75.6
REMARK 620 4 HOH B1417   O   142.6  91.1 118.6
REMARK 620 5 HOH B1692   O    67.8 171.0  97.2  87.5
REMARK 620 6 ASN B 436   O    87.1  76.5 148.4  76.3 111.8
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 1320
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 1321
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 1330
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 1331
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 1332
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGO A 1340
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGO A 1341
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGO A 1342
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGO B 1343
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGO B 1344
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGO B 1345
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1EVU   RELATED DB: PDB
REMARK 900 IN THE PRIMARY REFERENCE, 1EVU IS COMPARED TO THIS ENTRY TO
REMARK 900 DEMONSTRATE THAT THE CONFORMATION OF THE W279F MUTANT
REMARK 900 PROTEIN IS ESSENTIALLY IDENTICAL TO THE WILD TYPE PROTEIN.
REMARK 900 1EVU IS A FURTHER REFINEMENT OF THE 1GGU ENTRY (REFERENCE
REMARK 900 1).
DBREF  1EX0 A    1   731  UNP    P00488   F13A_HUMAN       1    731
DBREF  1EX0 B    1   731  UNP    P00488   F13A_HUMAN       1    731
SEQADV 1EX0 SAC A    1  UNP  P00488    SER     1 MODIFIED RESIDUE
SEQADV 1EX0 ASN A   35  UNP  P00488    VAL    35 CONFLICT
SEQADV 1EX0 LEU A   36  UNP  P00488    PRO    36 CONFLICT
SEQADV 1EX0 PHE A  279  UNP  P00488    TRP   279 ENGINEERED
SEQADV 1EX0 SER A  509  UNP  P00488    GLU   509 CONFLICT
SEQADV 1EX0 ARG A  510  UNP  P00488    GLY   510 CONFLICT
SEQADV 1EX0 SAC B    1  UNP  P00488    SER     1 MODIFIED RESIDUE
SEQADV 1EX0 ASN B   35  UNP  P00488    VAL    35 CONFLICT
SEQADV 1EX0 LEU B   36  UNP  P00488    PRO    36 CONFLICT
SEQADV 1EX0 PHE B  279  UNP  P00488    TRP   279 ENGINEERED
SEQADV 1EX0 SER B  509  UNP  P00488    GLU   509 CONFLICT
SEQADV 1EX0 ARG B  510  UNP  P00488    GLY   510 CONFLICT
SEQADV 1EX0 SER B  511  UNP  P00488    VAL   511 CONFLICT
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 ASN LEU 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 PHE 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 SER ARG SER 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 ASN LEU 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 PHE 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 SER ARG SER 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
HET     CA  A1320       1
HET     CA  B1321       1
HET    PO4  A1330       5
HET    PO4  B1331       5
HET    PO4  B1332       5
HET    PGO  A1340       5
HET    PGO  A1341       5
HET    PGO  A1342       5
HET    PGO  B1343       5
HET    PGO  B1344       5
HET    PGO  B1345       5
HETNAM      CA CALCIUM ION
HETNAM     PO4 PHOSPHATE ION
HETNAM     PGO S-1,2-PROPANEDIOL
FORMUL   3   CA    2(CA 2+)
FORMUL   5  PO4    3(O4 P 3-)
FORMUL   8  PGO    6(C3 H8 O2)
FORMUL  14  HOH   *1306(H2 O)
HELIX    1   1 ASP A   58  HIS A   65  1                                   8
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 PRO A  288  TRP A  292  5                                   5
HELIX    9   9 SER A  295  GLU A  306  1                                  12
HELIX   10  10 GLN A  313  GLY A  329  1                                  17
HELIX   11  11 VAL A  414  GLY A  420  1                                   7
HELIX   12  12 ASP A  427  SER A  437  1                                  11
HELIX   13  13 ILE A  477  LYS A  482  1                                   6
HELIX   14  14 GLN A  487  MET A  499  1                                  13
HELIX   15  15 GLN A  590  MET A  595  1                                   6
HELIX   16  16 ASP B   58  HIS B   64  1                                   7
HELIX   17  17 GLN B  110  GLY B  114  5                                   5
HELIX   18  18 ASN B  175  THR B  178  5                                   4
HELIX   19  19 ASN B  197  VAL B  205  1                                   9
HELIX   20  20 GLY B  233  ALA B  245  1                                  13
HELIX   21  21 ASP B  248  ARG B  252  5                                   5
HELIX   22  22 ASN B  254  MET B  265  1                                  12
HELIX   23  23 PRO B  288  TRP B  292  5                                   5
HELIX   24  24 SER B  295  GLU B  306  1                                  12
HELIX   25  25 GLN B  313  GLY B  329  1                                  17
HELIX   26  26 VAL B  414  GLY B  420  1                                   7
HELIX   27  27 ASP B  427  SER B  437  1                                  11
HELIX   28  28 ILE B  477  LYS B  482  1                                   6
HELIX   29  29 GLN B  487  TYR B  500  1                                  14
HELIX   30  30 GLN B  590  TYR B  594  5                                   5
SHEET    1   A 5 VAL A  47  HIS A  51  0
SHEET    2   A 5 SER A  81  PHE A  88 -1  O  GLN A  85   N  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 MET A 406  SER A 413  0
SHEET    2   F 6 GLY A 391  GLU A 401 -1  O  ALA A 394   N  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  O  SER A 581   N  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  N  LEU A 619   O  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 THR A 673  ILE A 683  0
SHEET    2   K 4 LEU A 660  GLY A 669 -1  O  LEU A 660   N  ILE A 683
SHEET    3   K 4 GLY A 701  SER A 710 -1  O  ILE A 706   N  ASP A 668
SHEET    4   K 4 VAL A 717  ILE A 725 -1  O  VAL A 717   N  MET A 709
SHEET    1   L 5 TYR B 116  VAL B 119  0
SHEET    2   L 5 LEU B  98  VAL B 104 -1  O  VAL B 101   N  VAL B 119
SHEET    3   L 5 GLY B 155  THR B 165 -1  N  ARG B 158   O  VAL B 104
SHEET    4   L 5 GLY B 168  ARG B 171 -1  O  GLY B 168   N  THR B 165
SHEET    5   L 5 VAL B  29  LEU B  31 -1  N  GLU B  30   O  VAL B 169
SHEET    1   M 5 TYR B 116  VAL B 119  0
SHEET    2   M 5 LEU B  98  VAL B 104 -1  O  VAL B 101   N  VAL B 119
SHEET    3   M 5 GLY B 155  THR B 165 -1  N  ARG B 158   O  VAL B 104
SHEET    4   M 5 THR B 180  LEU B 183 -1  O  THR B 180   N  PHE B 157
SHEET    5   M 5 LEU B  74  ARG B  77  1  O  LEU B  74   N  TYR B 181
SHEET    1   N 5 VAL B  47  HIS B  51  0
SHEET    2   N 5 PHE B  82  PHE B  88 -1  N  GLN B  85   O  HIS B  51
SHEET    3   N 5 SER B 141  GLN B 147 -1  O  VAL B 142   N  ILE B  86
SHEET    4   N 5 GLY B 131  GLU B 138 -1  O  GLY B 131   N  GLN B 147
SHEET    5   N 5 ILE B 121  VAL B 122  1  N  VAL B 122   O  ALA B 132
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  O  ARG B 333   N  GLU B 377
SHEET    5   Q 6 LEU B 463  LYS B 467 -1  O  LEU B 463   N  TYR B 338
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 PRO B 564  LEU B 577  0
SHEET    2   T 4 TYR B 547  THR B 558 -1  O  TYR B 547   N  LEU B 577
SHEET    3   T 4 SER B 603  ILE B 612 -1  O  SER B 603   N  THR B 558
SHEET    4   T 4 VAL B 618  VAL B 626 -1  N  LEU B 619   O  ALA B 610
SHEET    1   U 3 ILE B 633  ARG B 637  0
SHEET    2   U 3 MET B 646  THR B 653 -1  N  THR B 647   O  ARG B 637
SHEET    3   U 3 THR B 688  CYS B 695 -1  N  VAL B 689   O  PHE B 652
SHEET    1   V 4 THR B 673  ILE B 683  0
SHEET    2   V 4 LEU B 660  GLY B 669 -1  O  LEU B 660   N  ILE B 683
SHEET    3   V 4 GLY B 701  SER B 710 -1  O  ILE B 706   N  ASP B 668
SHEET    4   V 4 VAL B 717  ILE B 725 -1  O  VAL B 717   N  MET B 709
LINK        CA    CA A1320                 O   ASN A 436     1555   1555  2.85
LINK        CA    CA A1320                 O   HOH A1518     1555   1555  2.79
LINK        CA    CA A1320                 O   ALA A 457     1555   1555  2.84
LINK        CA    CA A1320                 O   HOH A1408     1555   1555  3.10
LINK        CA    CA A1320                 OD1 ASP A 438     1555   1555  2.91
LINK        CA    CA A1320                 O   HOH A1646     1555   1555  2.77
LINK        CA    CA B1321                 OD1 ASP B 438     1555   1555  2.74
LINK        CA    CA B1321                 O   HOH B1536     1555   1555  2.91
LINK        CA    CA B1321                 O   ALA B 457     1555   1555  2.85
LINK        CA    CA B1321                 O   HOH B1417     1555   1555  2.99
LINK        CA    CA B1321                 O   HOH B1692     1555   1555  2.77
LINK        CA    CA B1321                 O   ASN B 436     1555   1555  2.95
CISPEP   1 ARG A  310    TYR A  311          0         5.84
CISPEP   2 GLY A  410    PRO A  411          0         9.09
CISPEP   3 GLN A  425    PHE A  426          0        -0.63
CISPEP   4 ARG B  310    TYR B  311          0         4.39
CISPEP   5 GLY B  410    PRO B  411          0        12.24
CISPEP   6 GLN B  425    PHE B  426          0         8.60
SITE     1 AC1  5 ASN A 436  ASP A 438  ALA A 457  HOH A1518
SITE     2 AC1  5 HOH A1646
SITE     1 AC2  7 ASN B 436  SER B 437  ASP B 438  ALA B 457
SITE     2 AC2  7 HOH B1417  HOH B1536  HOH B1692
SITE     1 AC3  7 ASP A 456  THR A 458  HIS A 459  LYS A 462
SITE     2 AC3  7 LYS A 621  HOH A1473  HOH A1550
SITE     1 AC4  9 ASP B 456  THR B 458  HIS B 459  LYS B 462
SITE     2 AC4  9 LYS B 621  HOH B1372  HOH B1595  HOH B1664
SITE     3 AC4  9 HOH B1867
SITE     1 AC5  3 ASN B 517  SER B 543  HIS B 544
SITE     1 AC6  8 ARG A 260  ASP A 404  TYR A 407  ARG A 408
SITE     2 AC6  8 HOH A1376  HOH A1386  ASP B 404  ARG B 408
SITE     1 AC7  6 GLN A  85  MET A 136  GLU A 138  SER A 141
SITE     2 AC7  6 VAL A 142  ARG A 143
SITE     1 AC8  2 TYR A 500  PHE B 424
SITE     1 AC9  4 GLU B 525  LYS B 534  HOH B1760  HOH B1964
SITE     1 BC1  4 LYS B 565  GLY B 596  GLN B 597  HOH B2068
SITE     1 BC2  6 GLU B 571  GLU B 585  ALA B 586  VAL B 587
SITE     2 BC2  6 HOH B1438  HOH B1732
CRYST1  100.540   70.640  133.380  90.00 106.08  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      0.009946  0.000000  0.002867        0.00000
SCALE2      0.000000  0.014156  0.000000        0.00000
SCALE3      0.000000  0.000000  0.007803        0.00000
      
PROCHECK
Go to PROCHECK summary
 References