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 <I/SIGMA(I)> 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 <I/SIGMA(I)> 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
HETATM 1 C1A SAC A 1 28.800 -20.442 52.184 1.00 57.90 C
HETATM 2 C2A SAC A 1 27.582 -20.920 52.921 1.00 56.34 C
HETATM 3 OAC SAC A 1 29.486 -19.404 52.332 1.00 53.20 O
HETATM 4 N SAC A 1 29.134 -21.312 51.223 1.00 59.29 N
HETATM 5 CA SAC A 1 28.095 -22.115 50.607 1.00 65.56 C
HETATM 6 C SAC A 1 28.033 -23.481 51.295 1.00 68.34 C
HETATM 7 O SAC A 1 28.600 -23.731 52.381 1.00 71.40 O
HETATM 8 CB SAC A 1 28.387 -22.131 49.125 1.00 63.68 C
HETATM 9 OG SAC A 1 27.634 -21.367 48.257 1.00 62.74 O
(ATOM LINES ARE NOT SHOWN.)
END