HEADER TRANSFERASE 22-JUL-98 1GGU
TITLE HUMAN FACTOR XIII WITH CALCIUM BOUND IN THE ION SITE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (COAGULATION FACTOR XIII);
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: FULL LENGTH;
COMPND 5 EC: 2.3.2.13;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: CALCIUM BOUND IN THE ION SITE
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 4932
KEYWDS TRANSGLUTAMINASE, BLOOD COAGULATION, CALCIUM, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.A.FOX,V.C.YEE,L.C.PEDERSON,I.L.TRONG,P.D.BISHOP,
AUTHOR 2 R.E.STENKAMP,D.C.TELLER
REVDAT 4 24-FEB-09 1GGU 1 VERSN
REVDAT 3 01-APR-03 1GGU 1 JRNL
REVDAT 2 22-DEC-99 1GGU 4 HEADER COMPND REMARK JRNL
REVDAT 2 2 4 ATOM SOURCE SEQRES
REVDAT 1 16-SEP-99 1GGU 0
JRNL AUTH B.A.FOX,V.C.YEE,L.C.PEDERSEN,I.LE TRONG,P.D.BISHOP,
JRNL AUTH 2 R.E.STENKAMP,D.C.TELLER
JRNL TITL IDENTIFICATION OF THE CALCIUM BINDING SITE AND A
JRNL TITL 2 NOVEL YTTERBIUM SITE IN BLOOD COAGULATION FACTOR
JRNL TITL 3 XIII BY X-RAY CRYSTALLOGRAPHY.
JRNL REF J.BIOL.CHEM. V. 274 4917 1999
JRNL REFN ISSN 0021-9258
JRNL PMID 9988734
JRNL DOI 10.1074/JBC.274.8.4917
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 100000.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.1000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 91.9
REMARK 3 NUMBER OF REFLECTIONS : 96682
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 SET) : 0.227
REMARK 3 FREE R VALUE : 0.313
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4829
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.23
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 88.50
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 14639
REMARK 3 BIN R VALUE (WORKING SET) : 0.3640
REMARK 3 BIN FREE R VALUE : 0.3990
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.90
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 759
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.014
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 11294
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 2
REMARK 3 SOLVENT ATOMS : 1001
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -7.87000
REMARK 3 B22 (A**2) : 7.63000
REMARK 3 B33 (A**2) : 0.24000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 2.47000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.31
REMARK 3 ESD FROM SIGMAA (A) : 0.39
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.40
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.38
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.017
REMARK 3 BOND ANGLES (DEGREES) : 2.00
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 27.60
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.76
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.780 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.950 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.770 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 4.170 ; 2.500
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PARHCSDX.PRO
REMARK 3 PARAMETER FILE 2 : PARAM19.SOL
REMARK 3 PARAMETER FILE 3 : PARAM19.ION
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : TOPH19.ION
REMARK 3 TOPOLOGY FILE 3 : TOPH19.SOL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK 4
REMARK 4 1GGU COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-SEP-99.
REMARK 100 THE RCSB ID CODE IS RCSB008088.
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) : 100.0
REMARK 200 PH : 6.20
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: PDB ENTRY 1FIE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.20
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 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 SER A 1
REMARK 465 GLU A 2
REMARK 465 THR A 3
REMARK 465 SER A 4
REMARK 465 ARG A 5
REMARK 465 THR A 6
REMARK 465 ALA A 7
REMARK 465 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 SER B 1
REMARK 465 GLU B 2
REMARK 465 THR B 3
REMARK 465 SER B 4
REMARK 465 ARG B 5
REMARK 465 THR B 6
REMARK 465 ALA B 7
REMARK 465 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 515
REMARK 465 ARG B 728
REMARK 465 PRO B 729
REMARK 465 SER B 730
REMARK 465 MET B 731
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLU A 30 O
REMARK 470 THR A 508 O
REMARK 470 ARG A 727 O
REMARK 470 VAL B 34 CG1 CG2
REMARK 470 VAL B 35 O CG1 CG2
REMARK 470 THR B 508 O
REMARK 470 ARG B 727 O
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 158 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG A 158 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG A 174 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 GLY B 9 N - CA - C ANGL. DEV. = -17.6 DEGREES
REMARK 500 LEU B 52 N - CA - C ANGL. DEV. = -19.3 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 LEU A 45 118.78 108.39
REMARK 500 ASN A 60 -71.94 -53.03
REMARK 500 ASP A 139 -124.35 59.59
REMARK 500 PRO A 166 33.56 -76.03
REMARK 500 TYR A 167 -36.11 -145.28
REMARK 500 VAL A 193 1.44 -68.50
REMARK 500 TYR A 194 108.72 -51.73
REMARK 500 ASP A 196 37.03 -69.03
REMARK 500 TYR A 214 -151.71 -126.75
REMARK 500 ASP A 219 80.05 -165.91
REMARK 500 ASP A 270 -108.38 77.52
REMARK 500 SER A 278 125.67 -170.23
REMARK 500 ASN A 281 -14.39 55.65
REMARK 500 TYR A 285 41.66 -92.30
REMARK 500 PHE A 339 77.69 73.41
REMARK 500 THR A 365 91.23 -67.77
REMARK 500 ASN A 402 -166.84 -115.16
REMARK 500 ASN A 517 11.29 89.85
REMARK 500 HIS A 544 31.05 -99.25
REMARK 500 GLN A 601 -15.45 85.43
REMARK 500 ILE A 612 -164.38 -71.84
REMARK 500 ASN A 613 -41.05 -134.66
REMARK 500 ARG A 616 16.64 55.53
REMARK 500 PRO A 630 170.70 -52.62
REMARK 500 GLN A 640 79.24 -108.26
REMARK 500 ASN A 662 64.95 33.44
REMARK 500 ARG A 681 -51.76 -25.23
REMARK 500 PRO A 697 155.17 -46.51
REMARK 500 ARG A 703 -166.13 -109.32
REMARK 500 SER A 711 -132.78 -82.04
REMARK 500 SER A 713 -66.80 -133.39
REMARK 500 HIS A 716 35.35 75.43
REMARK 500 GLN B 32 123.52 -172.27
REMARK 500 VAL B 34 -132.19 -123.07
REMARK 500 LEU B 45 123.89 129.52
REMARK 500 PHE B 53 76.10 -111.66
REMARK 500 PRO B 91 126.79 -34.71
REMARK 500 PRO B 94 -18.82 -40.55
REMARK 500 ASP B 139 82.04 51.29
REMARK 500 ARG B 140 -47.20 73.64
REMARK 500 TYR B 214 -156.66 -139.78
REMARK 500 ASP B 219 73.34 -166.02
REMARK 500 ASP B 270 -119.80 66.09
REMARK 500 ASN B 281 1.24 59.70
REMARK 500 PHE B 339 79.94 64.60
REMARK 500 ASN B 402 -164.05 -111.50
REMARK 500 LEU B 580 76.63 51.39
REMARK 500 GLN B 601 -7.72 88.83
REMARK 500 ASN B 654 107.37 -52.51
REMARK 500 GLU B 682 135.03 -171.21
REMARK 500 ASN B 686 12.54 48.64
REMARK 500 SER B 713 -86.14 -135.33
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 B6418 DISTANCE = 5.45 ANGSTROMS
REMARK 525 HOH B6477 DISTANCE = 6.93 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 A2001 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA A 457 O
REMARK 620 2 HOH A6438 O 96.4
REMARK 620 3 HOH A6155 O 103.8 131.3
REMARK 620 4 HOH A6437 O 60.6 76.9 75.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B2002 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA B 457 O
REMARK 620 2 HOH B6135 O 81.1
REMARK 620 3 HOH B6136 O 87.6 73.3
REMARK 620 4 HOH B6293 O 152.3 101.4 67.2
REMARK 620 5 HOH B6151 O 100.5 144.8 71.6 61.6
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CAT
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: CATALYTIC TRIAD IN CHAIN A
REMARK 800 SITE_IDENTIFIER: CBT
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: CATALYTIC TRIAD IN CHAIN B
REMARK 800 SITE_IDENTIFIER: INA
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: ION BINDING SITE A - CALCIUM LIGANDS
REMARK 800 SITE_IDENTIFIER: INB
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: ION BINDING SITE B - CALCIUM LIGANDS
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 2001
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 2002
DBREF 1GGU A 1 731 UNP P00488 F13A_HUMAN 2 732
DBREF 1GGU B 1 731 UNP P00488 F13A_HUMAN 2 732
SEQADV 1GGU GLU A 567 UNP P00488 GLN 651 CONFLICT
SEQADV 1GGU GLU B 567 UNP P00488 GLN 651 CONFLICT
SEQRES 1 A 731 SER GLU THR SER ARG THR ALA PHE GLY GLY ARG ARG ALA
SEQRES 2 A 731 VAL PRO PRO ASN ASN SER ASN ALA ALA GLU ASP ASP LEU
SEQRES 3 A 731 PRO THR VAL GLU LEU GLN GLY VAL VAL PRO ARG GLY VAL
SEQRES 4 A 731 ASN LEU GLN GLU PHE LEU ASN VAL THR SER VAL HIS LEU
SEQRES 5 A 731 PHE LYS GLU ARG TRP ASP THR ASN LYS VAL ASP HIS HIS
SEQRES 6 A 731 THR ASP LYS TYR GLU ASN ASN LYS LEU ILE VAL ARG ARG
SEQRES 7 A 731 GLY GLN SER PHE TYR VAL GLN ILE ASP PHE SER ARG PRO
SEQRES 8 A 731 TYR ASP PRO ARG ARG ASP LEU PHE ARG VAL GLU TYR VAL
SEQRES 9 A 731 ILE GLY ARG TYR PRO GLN GLU ASN LYS GLY THR TYR ILE
SEQRES 10 A 731 PRO VAL PRO ILE VAL SER GLU LEU GLN SER GLY LYS TRP
SEQRES 11 A 731 GLY ALA LYS ILE VAL MET ARG GLU ASP ARG SER VAL ARG
SEQRES 12 A 731 LEU SER ILE GLN SER SER PRO LYS CYS ILE VAL GLY LYS
SEQRES 13 A 731 PHE ARG MET TYR VAL ALA VAL TRP THR PRO TYR GLY VAL
SEQRES 14 A 731 LEU ARG THR SER ARG ASN PRO GLU THR ASP THR TYR ILE
SEQRES 15 A 731 LEU PHE ASN PRO TRP CYS GLU ASP ASP ALA VAL TYR LEU
SEQRES 16 A 731 ASP ASN GLU LYS GLU ARG GLU GLU TYR VAL LEU ASN ASP
SEQRES 17 A 731 ILE GLY VAL ILE PHE TYR GLY GLU VAL ASN ASP ILE LYS
SEQRES 18 A 731 THR ARG SER TRP SER TYR GLY GLN PHE GLU ASP GLY ILE
SEQRES 19 A 731 LEU ASP THR CYS LEU TYR VAL MET ASP ARG ALA GLN MET
SEQRES 20 A 731 ASP LEU SER GLY ARG GLY ASN PRO ILE LYS VAL SER ARG
SEQRES 21 A 731 VAL GLY SER ALA MET VAL ASN ALA LYS ASP ASP GLU GLY
SEQRES 22 A 731 VAL LEU VAL GLY SER TRP ASP ASN ILE TYR ALA TYR GLY
SEQRES 23 A 731 VAL PRO PRO SER ALA TRP THR GLY SER VAL ASP ILE LEU
SEQRES 24 A 731 LEU GLU TYR ARG SER SER GLU ASN PRO VAL ARG TYR GLY
SEQRES 25 A 731 GLN CYS TRP VAL PHE ALA GLY VAL PHE ASN THR PHE LEU
SEQRES 26 A 731 ARG CYS LEU GLY ILE PRO ALA ARG ILE VAL THR ASN TYR
SEQRES 27 A 731 PHE SER ALA HIS ASP ASN ASP ALA ASN LEU GLN MET ASP
SEQRES 28 A 731 ILE PHE LEU GLU GLU ASP GLY ASN VAL ASN SER LYS LEU
SEQRES 29 A 731 THR LYS ASP SER VAL TRP ASN TYR HIS CYS TRP ASN GLU
SEQRES 30 A 731 ALA TRP MET THR ARG PRO ASP LEU PRO VAL GLY PHE GLY
SEQRES 31 A 731 GLY TRP GLN ALA VAL ASP SER THR PRO GLN GLU ASN SER
SEQRES 32 A 731 ASP GLY MET TYR ARG CYS GLY PRO ALA SER VAL GLN ALA
SEQRES 33 A 731 ILE LYS HIS GLY HIS VAL CYS PHE GLN PHE ASP ALA PRO
SEQRES 34 A 731 PHE VAL PHE ALA GLU VAL ASN SER ASP LEU ILE TYR ILE
SEQRES 35 A 731 THR ALA LYS LYS ASP GLY THR HIS VAL VAL GLU ASN VAL
SEQRES 36 A 731 ASP ALA THR HIS ILE GLY LYS LEU ILE VAL THR LYS GLN
SEQRES 37 A 731 ILE GLY GLY ASP GLY MET MET ASP ILE THR ASP THR TYR
SEQRES 38 A 731 LYS PHE GLN GLU GLY GLN GLU GLU GLU ARG LEU ALA LEU
SEQRES 39 A 731 GLU THR ALA LEU MET TYR GLY ALA LYS LYS PRO LEU ASN
SEQRES 40 A 731 THR GLU GLY VAL MET LYS SER ARG SER ASN VAL ASP MET
SEQRES 41 A 731 ASP PHE GLU VAL GLU ASN ALA VAL LEU GLY LYS ASP PHE
SEQRES 42 A 731 LYS LEU SER ILE THR PHE ARG ASN ASN SER HIS ASN ARG
SEQRES 43 A 731 TYR THR ILE THR ALA TYR LEU SER ALA ASN ILE THR PHE
SEQRES 44 A 731 TYR THR GLY VAL PRO LYS ALA GLU PHE LYS LYS GLU THR
SEQRES 45 A 731 PHE ASP VAL THR LEU GLU PRO LEU SER PHE LYS LYS GLU
SEQRES 46 A 731 ALA VAL LEU ILE GLN ALA GLY GLU TYR MET GLY GLN LEU
SEQRES 47 A 731 LEU GLU GLN ALA SER LEU HIS PHE PHE VAL THR ALA ARG
SEQRES 48 A 731 ILE ASN GLU THR ARG ASP VAL LEU ALA LYS GLN LYS SER
SEQRES 49 A 731 THR VAL LEU THR ILE PRO GLU ILE ILE ILE LYS VAL ARG
SEQRES 50 A 731 GLY THR GLN VAL VAL GLY SER ASP MET THR VAL THR VAL
SEQRES 51 A 731 GLU PHE THR ASN PRO LEU LYS GLU THR LEU ARG ASN VAL
SEQRES 52 A 731 TRP VAL HIS LEU ASP GLY PRO GLY VAL THR ARG PRO MET
SEQRES 53 A 731 LYS LYS MET PHE ARG GLU ILE ARG PRO ASN SER THR VAL
SEQRES 54 A 731 GLN TRP GLU GLU VAL CYS ARG PRO TRP VAL SER GLY HIS
SEQRES 55 A 731 ARG LYS LEU ILE ALA SER MET SER SER ASP SER LEU ARG
SEQRES 56 A 731 HIS VAL TYR GLY GLU LEU ASP VAL GLN ILE GLN ARG ARG
SEQRES 57 A 731 PRO SER MET
SEQRES 1 B 731 SER GLU THR SER ARG THR ALA PHE GLY GLY ARG ARG ALA
SEQRES 2 B 731 VAL PRO PRO ASN ASN SER ASN ALA ALA GLU ASP ASP LEU
SEQRES 3 B 731 PRO THR VAL GLU LEU GLN GLY VAL VAL PRO ARG GLY VAL
SEQRES 4 B 731 ASN LEU GLN GLU PHE LEU ASN VAL THR SER VAL HIS LEU
SEQRES 5 B 731 PHE LYS GLU ARG TRP ASP THR ASN LYS VAL ASP HIS HIS
SEQRES 6 B 731 THR ASP LYS TYR GLU ASN ASN LYS LEU ILE VAL ARG ARG
SEQRES 7 B 731 GLY GLN SER PHE TYR VAL GLN ILE ASP PHE SER ARG PRO
SEQRES 8 B 731 TYR ASP PRO ARG ARG ASP LEU PHE ARG VAL GLU TYR VAL
SEQRES 9 B 731 ILE GLY ARG TYR PRO GLN GLU ASN LYS GLY THR TYR ILE
SEQRES 10 B 731 PRO VAL PRO ILE VAL SER GLU LEU GLN SER GLY LYS TRP
SEQRES 11 B 731 GLY ALA LYS ILE VAL MET ARG GLU ASP ARG SER VAL ARG
SEQRES 12 B 731 LEU SER ILE GLN SER SER PRO LYS CYS ILE VAL GLY LYS
SEQRES 13 B 731 PHE ARG MET TYR VAL ALA VAL TRP THR PRO TYR GLY VAL
SEQRES 14 B 731 LEU ARG THR SER ARG ASN PRO GLU THR ASP THR TYR ILE
SEQRES 15 B 731 LEU PHE ASN PRO TRP CYS GLU ASP ASP ALA VAL TYR LEU
SEQRES 16 B 731 ASP ASN GLU LYS GLU ARG GLU GLU TYR VAL LEU ASN ASP
SEQRES 17 B 731 ILE GLY VAL ILE PHE TYR GLY GLU VAL ASN ASP ILE LYS
SEQRES 18 B 731 THR ARG SER TRP SER TYR GLY GLN PHE GLU ASP GLY ILE
SEQRES 19 B 731 LEU ASP THR CYS LEU TYR VAL MET ASP ARG ALA GLN MET
SEQRES 20 B 731 ASP LEU SER GLY ARG GLY ASN PRO ILE LYS VAL SER ARG
SEQRES 21 B 731 VAL GLY SER ALA MET VAL ASN ALA LYS ASP ASP GLU GLY
SEQRES 22 B 731 VAL LEU VAL GLY SER TRP ASP ASN ILE TYR ALA TYR GLY
SEQRES 23 B 731 VAL PRO PRO SER ALA TRP THR GLY SER VAL ASP ILE LEU
SEQRES 24 B 731 LEU GLU TYR ARG SER SER GLU ASN PRO VAL ARG TYR GLY
SEQRES 25 B 731 GLN CYS TRP VAL PHE ALA GLY VAL PHE ASN THR PHE LEU
SEQRES 26 B 731 ARG CYS LEU GLY ILE PRO ALA ARG ILE VAL THR ASN TYR
SEQRES 27 B 731 PHE SER ALA HIS ASP ASN ASP ALA ASN LEU GLN MET ASP
SEQRES 28 B 731 ILE PHE LEU GLU GLU ASP GLY ASN VAL ASN SER LYS LEU
SEQRES 29 B 731 THR LYS ASP SER VAL TRP ASN TYR HIS CYS TRP ASN GLU
SEQRES 30 B 731 ALA TRP MET THR ARG PRO ASP LEU PRO VAL GLY PHE GLY
SEQRES 31 B 731 GLY TRP GLN ALA VAL ASP SER THR PRO GLN GLU ASN SER
SEQRES 32 B 731 ASP GLY MET TYR ARG CYS GLY PRO ALA SER VAL GLN ALA
SEQRES 33 B 731 ILE LYS HIS GLY HIS VAL CYS PHE GLN PHE ASP ALA PRO
SEQRES 34 B 731 PHE VAL PHE ALA GLU VAL ASN SER ASP LEU ILE TYR ILE
SEQRES 35 B 731 THR ALA LYS LYS ASP GLY THR HIS VAL VAL GLU ASN VAL
SEQRES 36 B 731 ASP ALA THR HIS ILE GLY LYS LEU ILE VAL THR LYS GLN
SEQRES 37 B 731 ILE GLY GLY ASP GLY MET MET ASP ILE THR ASP THR TYR
SEQRES 38 B 731 LYS PHE GLN GLU GLY GLN GLU GLU GLU ARG LEU ALA LEU
SEQRES 39 B 731 GLU THR ALA LEU MET TYR GLY ALA LYS LYS PRO LEU ASN
SEQRES 40 B 731 THR GLU GLY VAL MET LYS SER ARG SER ASN VAL ASP MET
SEQRES 41 B 731 ASP PHE GLU VAL GLU ASN ALA VAL LEU GLY LYS ASP PHE
SEQRES 42 B 731 LYS LEU SER ILE THR PHE ARG ASN ASN SER HIS ASN ARG
SEQRES 43 B 731 TYR THR ILE THR ALA TYR LEU SER ALA ASN ILE THR PHE
SEQRES 44 B 731 TYR THR GLY VAL PRO LYS ALA GLU PHE LYS LYS GLU THR
SEQRES 45 B 731 PHE ASP VAL THR LEU GLU PRO LEU SER PHE LYS LYS GLU
SEQRES 46 B 731 ALA VAL LEU ILE GLN ALA GLY GLU TYR MET GLY GLN LEU
SEQRES 47 B 731 LEU GLU GLN ALA SER LEU HIS PHE PHE VAL THR ALA ARG
SEQRES 48 B 731 ILE ASN GLU THR ARG ASP VAL LEU ALA LYS GLN LYS SER
SEQRES 49 B 731 THR VAL LEU THR ILE PRO GLU ILE ILE ILE LYS VAL ARG
SEQRES 50 B 731 GLY THR GLN VAL VAL GLY SER ASP MET THR VAL THR VAL
SEQRES 51 B 731 GLU PHE THR ASN PRO LEU LYS GLU THR LEU ARG ASN VAL
SEQRES 52 B 731 TRP VAL HIS LEU ASP GLY PRO GLY VAL THR ARG PRO MET
SEQRES 53 B 731 LYS LYS MET PHE ARG GLU ILE ARG PRO ASN SER THR VAL
SEQRES 54 B 731 GLN TRP GLU GLU VAL CYS ARG PRO TRP VAL SER GLY HIS
SEQRES 55 B 731 ARG LYS LEU ILE ALA SER MET SER SER ASP SER LEU ARG
SEQRES 56 B 731 HIS VAL TYR GLY GLU LEU ASP VAL GLN ILE GLN ARG ARG
SEQRES 57 B 731 PRO SER MET
HET CA A2001 1
HET CA B2002 1
HETNAM CA CALCIUM ION
FORMUL 3 CA 2(CA 2+)
FORMUL 5 HOH *1001(H2 O)
HELIX 1 1 THR A 59 ASP A 63 1 5
HELIX 2 2 GLU A 111 LYS A 113 5 3
HELIX 3 3 PRO A 176 THR A 178 5 3
HELIX 4 4 GLU A 198 TYR A 204 1 7
HELIX 5 5 ILE A 234 ARG A 244 1 11
HELIX 6 6 LEU A 249 GLY A 251 5 3
HELIX 7 7 PRO A 255 VAL A 266 1 12
HELIX 8 8 PRO A 289 ALA A 291 5 3
HELIX 9 9 SER A 295 SER A 305 1 11
HELIX 10 10 CYS A 314 LEU A 328 1 15
HELIX 11 11 VAL A 414 HIS A 419 1 6
HELIX 12 12 ALA A 428 ASN A 436 1 9
HELIX 13 13 THR A 478 TYR A 481 1 4
HELIX 14 14 GLU A 488 MET A 499 1 12
HELIX 15 15 ALA A 591 GLU A 593 5 3
HELIX 16 16 THR B 59 ASP B 63 1 5
HELIX 17 17 GLU B 111 LYS B 113 5 3
HELIX 18 18 PRO B 176 THR B 178 5 3
HELIX 19 19 GLU B 198 LEU B 206 1 9
HELIX 20 20 ILE B 234 ARG B 244 1 11
HELIX 21 21 LEU B 249 GLY B 251 5 3
HELIX 22 22 PRO B 255 VAL B 266 1 12
HELIX 23 23 VAL B 296 SER B 305 1 10
HELIX 24 24 CYS B 314 LEU B 328 1 15
HELIX 25 25 VAL B 414 LYS B 418 1 5
HELIX 26 26 ALA B 428 ASN B 436 1 9
HELIX 27 27 THR B 478 TYR B 481 1 4
HELIX 28 28 GLU B 488 MET B 499 1 12
HELIX 29 29 ALA B 591 GLU B 593 5 3
HELIX 30 30 MET B 595 GLN B 597 5 3
SHEET 1 A 3 LEU A 74 ARG A 77 0
SHEET 2 A 3 THR A 180 LEU A 183 1 N TYR A 181 O LEU A 74
SHEET 3 A 3 GLY A 155 PHE A 157 -1 N PHE A 157 O THR A 180
SHEET 1 B 4 VAL A 47 LEU A 52 0
SHEET 2 B 4 PHE A 82 PHE A 88 -1 N ASP A 87 O THR A 48
SHEET 3 B 4 SER A 141 GLN A 147 -1 N ILE A 146 O PHE A 82
SHEET 4 B 4 GLY A 131 GLU A 138 -1 N GLU A 138 O SER A 141
SHEET 1 C 4 TYR A 116 VAL A 119 0
SHEET 2 C 4 PHE A 99 VAL A 104 -1 N TYR A 103 O ILE A 117
SHEET 3 C 4 ARG A 158 TRP A 164 -1 N ALA A 162 O ARG A 100
SHEET 4 C 4 VAL A 169 ARG A 171 -1 N LEU A 170 O VAL A 163
SHEET 1 D 2 ILE A 209 GLU A 216 0
SHEET 2 D 2 ASP A 219 SER A 226 -1 N TRP A 225 O GLY A 210
SHEET 1 E 5 MET A 474 ASP A 476 0
SHEET 2 E 5 LEU A 463 LYS A 467 -1 N THR A 466 O MET A 475
SHEET 3 E 5 ALA A 332 TYR A 338 -1 N TYR A 338 O LEU A 463
SHEET 4 E 5 TYR A 372 MET A 380 -1 N GLU A 377 O ARG A 333
SHEET 5 E 5 GLY A 391 VAL A 395 -1 N VAL A 395 O ASN A 376
SHEET 1 F 3 GLN A 349 LEU A 354 0
SHEET 2 F 3 ASP A 438 ALA A 444 1 N ASP A 438 O MET A 350
SHEET 3 F 3 HIS A 450 ASP A 456 -1 N ASP A 456 O LEU A 439
SHEET 1 G 3 VAL A 518 VAL A 524 0
SHEET 2 G 3 PHE A 533 ASN A 541 -1 N ARG A 540 O ASP A 519
SHEET 3 G 3 SER A 581 ILE A 589 -1 N ILE A 589 O PHE A 533
SHEET 1 H 4 VAL A 618 VAL A 626 0
SHEET 2 H 4 SER A 603 ARG A 611 -1 N ALA A 610 O LEU A 619
SHEET 3 H 4 TYR A 547 THR A 558 -1 N THR A 558 O SER A 603
SHEET 4 H 4 ALA A 566 LEU A 577 -1 N LEU A 577 O TYR A 547
SHEET 1 I 3 ILE A 632 GLY A 638 0
SHEET 2 I 3 ASP A 645 THR A 653 -1 N GLU A 651 O ILE A 633
SHEET 3 I 3 THR A 688 ARG A 696 -1 N CYS A 695 O MET A 646
SHEET 1 J 4 MET A 676 PHE A 680 0
SHEET 2 J 4 VAL A 663 ASP A 668 -1 N LEU A 667 O MET A 676
SHEET 3 J 4 LEU A 705 SER A 710 -1 N SER A 710 O TRP A 664
SHEET 4 J 4 ARG A 715 LEU A 721 -1 N LEU A 721 O LEU A 705
SHEET 1 K 3 LEU B 74 ARG B 77 0
SHEET 2 K 3 THR B 180 LEU B 183 1 N TYR B 181 O LEU B 74
SHEET 3 K 3 GLY B 155 PHE B 157 -1 N PHE B 157 O THR B 180
SHEET 1 L 4 VAL B 47 LEU B 52 0
SHEET 2 L 4 PHE B 82 PHE B 88 -1 N ASP B 87 O THR B 48
SHEET 3 L 4 SER B 141 GLN B 147 -1 N ILE B 146 O PHE B 82
SHEET 4 L 4 GLY B 131 GLU B 138 -1 N GLU B 138 O SER B 141
SHEET 1 M 4 TYR B 116 PRO B 120 0
SHEET 2 M 4 LEU B 98 VAL B 104 -1 N TYR B 103 O ILE B 117
SHEET 3 M 4 ARG B 158 TRP B 164 -1 N TRP B 164 O LEU B 98
SHEET 4 M 4 VAL B 169 ARG B 171 -1 N LEU B 170 O VAL B 163
SHEET 1 N 2 ILE B 209 GLU B 216 0
SHEET 2 N 2 ASP B 219 SER B 226 -1 N TRP B 225 O GLY B 210
SHEET 1 O 5 MET B 474 ASP B 476 0
SHEET 2 O 5 LEU B 463 LYS B 467 -1 N THR B 466 O MET B 475
SHEET 3 O 5 ALA B 332 TYR B 338 -1 N TYR B 338 O LEU B 463
SHEET 4 O 5 TYR B 372 MET B 380 -1 N GLU B 377 O ARG B 333
SHEET 5 O 5 GLY B 391 VAL B 395 -1 N VAL B 395 O ASN B 376
SHEET 1 P 3 GLN B 349 LEU B 354 0
SHEET 2 P 3 ASP B 438 ALA B 444 1 N ASP B 438 O MET B 350
SHEET 3 P 3 HIS B 450 ASP B 456 -1 N ASP B 456 O LEU B 439
SHEET 1 Q 3 VAL B 518 VAL B 524 0
SHEET 2 Q 3 PHE B 533 ASN B 541 -1 N ARG B 540 O ASP B 519
SHEET 3 Q 3 SER B 581 ILE B 589 -1 N ILE B 589 O PHE B 533
SHEET 1 R 4 VAL B 618 VAL B 626 0
SHEET 2 R 4 SER B 603 ILE B 612 -1 N ALA B 610 O LEU B 619
SHEET 3 R 4 TYR B 547 THR B 558 -1 N THR B 558 O SER B 603
SHEET 4 R 4 ALA B 566 LEU B 577 -1 N LEU B 577 O TYR B 547
SHEET 1 S 3 ILE B 633 GLY B 638 0
SHEET 2 S 3 ASP B 645 THR B 653 -1 N GLU B 651 O ILE B 633
SHEET 3 S 3 THR B 688 ARG B 696 -1 N CYS B 695 O MET B 646
SHEET 1 T 4 MET B 676 PHE B 680 0
SHEET 2 T 4 VAL B 663 ASP B 668 -1 N LEU B 667 O MET B 676
SHEET 3 T 4 GLY B 701 SER B 710 -1 N SER B 710 O TRP B 664
SHEET 4 T 4 VAL B 717 ILE B 725 -1 N ILE B 725 O GLY B 701
LINK O ALA A 457 CA CA A2001 1555 1555 2.77
LINK O ALA B 457 CA CA B2002 1555 1555 2.54
LINK CA CA A2001 O HOH A6438 1555 1555 2.14
LINK CA CA A2001 O HOH A6155 1555 1555 2.26
LINK CA CA A2001 O HOH A6437 1555 1555 2.89
LINK CA CA B2002 O HOH B6135 1555 1555 2.52
LINK CA CA B2002 O HOH B6136 1555 1555 2.65
LINK CA CA B2002 O HOH B6293 1555 1555 2.83
LINK CA CA B2002 O HOH B6151 1555 1555 2.90
CISPEP 1 ARG A 310 TYR A 311 0 0.41
CISPEP 2 GLY A 410 PRO A 411 0 0.26
CISPEP 3 GLN A 425 PHE A 426 0 0.20
CISPEP 4 ARG B 310 TYR B 311 0 -1.02
CISPEP 5 GLY B 410 PRO B 411 0 0.37
CISPEP 6 GLN B 425 PHE B 426 0 1.53
SITE 1 CAT 3 CYS A 314 HIS A 373 ASP A 396
SITE 1 CBT 3 CYS B 314 HIS B 373 ASP B 396
SITE 1 INA 4 ALA A 457 ASN A 436 GLU A 485 GLU A 490
SITE 1 INB 4 ALA B 457 ASN B 436 GLU B 485 GLU B 490
SITE 1 AC1 4 ALA A 457 HOH A6155 HOH A6437 HOH A6438
SITE 1 AC2 5 ALA B 457 HOH B6135 HOH B6136 HOH B6151
SITE 2 AC2 5 HOH B6293
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
MTRIX1 1 -0.970600 -0.200870 -0.132640 56.42603 1
MTRIX2 1 -0.202620 0.384350 0.900680 -16.31962 1
MTRIX3 1 -0.129940 0.901070 -0.413750 37.77760 1
(ATOM LINES ARE NOT SHOWN.)
END
