HEADER HYDROLASE 07-NOV-03 1V3X
TITLE FACTOR XA IN COMPLEX WITH THE INHIBITOR 1-[6-METHYL-4,5,6,7-
TITLE 2 TETRAHYDROTHIAZOLO(5,4-C)PYRIDIN-2-YL] CARBONYL-2-CARBAMOYL-4-(6-
TITLE 3 CHLORONAPHTH-2-YLSULPHONYL)PIPERAZINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: COAGULATION FACTOR X, HEAVY CHAIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 16-243;
COMPND 5 SYNONYM: FACTOR XA HEAVY CHAIN, ACTIVATED FACTOR XA HEAVY CHAIN;
COMPND 6 EC: 3.4.21.6;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: COAGULATION FACTOR X, LIGHT CHAIN;
COMPND 9 CHAIN: B;
COMPND 10 FRAGMENT: RESIDUES 87-138;
COMPND 11 SYNONYM: FACTOR XA LIGHT CHAIN;
COMPND 12 EC: 3.4.21.6
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 7 ORGANISM_COMMON: HUMAN;
SOURCE 8 ORGANISM_TAXID: 9606;
SOURCE 9 OTHER_DETAILS: PROTEOLYTIC CLEAVAGE PRODUCT
KEYWDS GLYCOPROTEIN, HYDROLASE, SERINE PROTEASE, PLASMA, BLOOD COAGULATION
KEYWDS 2 FACTOR, PROTEIN INHIBITOR COMPLEX, CALCIUM-BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR M.SUZUKI
REVDAT 3 25-OCT-23 1V3X 1 COMPND REMARK HETNAM LINK
REVDAT 2 24-FEB-09 1V3X 1 VERSN
REVDAT 1 07-NOV-04 1V3X 0
JRNL AUTH N.HAGINOYA,S.KOBAYASHI,S.KOMORIYA,T.YOSHINO,M.SUZUKI,
JRNL AUTH 2 T.SHIMADA,K.WATANABE,Y.HIROKAWA,T.FURUGORI,T.NAGAHARA
JRNL TITL SYNTHESIS AND CONFORMATIONAL ANALYSIS OF A NON-AMIDINE
JRNL TITL 2 FACTOR XA INHIBITOR THAT INCORPORATES
JRNL TITL 3 5-METHYL-4,5,6,7-TETRAHYDROTHIAZOLO[5,4-C]PYRIDINE AS S4
JRNL TITL 4 BINDING ELEMENT
JRNL REF J.MED.CHEM. V. 47 5167 2004
JRNL REFN ISSN 0022-2623
JRNL PMID 15456260
JRNL DOI 10.1021/JM049884D
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH K.KAMATA,H.KAWAMOTO,T.HONMA,T.IWAMA,S.H.KIM
REMARK 1 TITL STRUCTURAL BASIS FOR CHEMICAL INHIBITION OF HUMAN BLOOD
REMARK 1 TITL 2 COAGULATION FACTOR XA
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 95 6630 1998
REMARK 1 REFN ISSN 0027-8424
REMARK 1 PMID 9618463
REMARK 1 DOI 10.1073/PNAS.95.12.6630
REMARK 1 REFERENCE 2
REMARK 1 AUTH H.BRANDSTETTER,A.KUHNE,W.BODE,R.HUBER,W.VON DER SAAL,
REMARK 1 AUTH 2 K.WIRTHENSOHN,R.A.ENGH
REMARK 1 TITL X-RAY STRUCTURE OF ACTIVE SITE-INHIBITED CLOTTING FACTOR XA.
REMARK 1 TITL 2 IMPLICATIONS FOR DRUG DESIGN AND SUBSTRATE RECOGNITION
REMARK 1 REF J.BIOL.CHEM. V. 271 29988 1996
REMARK 1 REFN ISSN 0021-9258
REMARK 1 PMID 8939944
REMARK 1 DOI 10.1074/JBC.271.47.29988
REMARK 1 REFERENCE 3
REMARK 1 AUTH K.PADMANABHAN,K.P.PADMANABHAN,A.TULINSKY,C.H.PARK,W.BODE,
REMARK 1 AUTH 2 R.HUBER,D.T.BLANKENSHIP,A.D.CARDIN,W.KISIEL
REMARK 1 TITL STRUCTURE OF HUMAN DES(1-45) FACTOR XA AT 2.2 A RESOLUTION
REMARK 1 REF J.MOL.BIOL. V. 232 947 1993
REMARK 1 REFN ISSN 0022-2836
REMARK 1 PMID 8355279
REMARK 1 DOI 10.1006/JMBI.1993.1441
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.24
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 15207
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) : 0.194
REMARK 3 R VALUE (WORKING SET) : 0.192
REMARK 3 FREE R VALUE : 0.233
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.700
REMARK 3 FREE R VALUE TEST SET COUNT : 751
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 15
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.28
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1370
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.1760
REMARK 3 BIN FREE R VALUE SET COUNT : 65
REMARK 3 BIN FREE R VALUE : 0.2580
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2146
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 37
REMARK 3 SOLVENT ATOMS : 161
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 35.62
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.91
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.55000
REMARK 3 B22 (A**2) : -2.16000
REMARK 3 B33 (A**2) : 0.61000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.271
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.204
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.135
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.151
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.931
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.921
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2235 ; 0.019 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3036 ; 1.798 ; 1.964
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 283 ; 6.971 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 332 ; 0.117 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1685 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1026 ; 0.214 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 196 ; 0.172 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 6 ; 0.115 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 29 ; 0.163 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 19 ; 0.186 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1406 ; 1.582 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2243 ; 2.604 ; 2.500
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 829 ; 2.339 ; 2.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 793 ; 3.331 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL PARAMETERS FOR MASK CALCULATION
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : NULL
REMARK 3 ION PROBE RADIUS : NULL
REMARK 3 SHRINKAGE RADIUS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1V3X COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 10-NOV-03.
REMARK 100 THE DEPOSITION ID IS D_1000006174.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-DEC-98
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 5.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.542
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA, CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15999
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 53.124
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.0
REMARK 200 DATA REDUNDANCY : 3.100
REMARK 200 R MERGE (I) : 0.04400
REMARK 200 R SYM (I) : 0.04400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.27
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.4
REMARK 200 DATA REDUNDANCY IN SHELL : 2.60
REMARK 200 R MERGE FOR SHELL (I) : 0.25900
REMARK 200 R SYM FOR SHELL (I) : 0.25900
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: RIGID BODY REFINEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: 1FAX
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.54
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG6000, SODIUM ACETATE, MALATE
REMARK 280 IMIDAZOLE, CALCIUM CHLORIDE, PH 5.00, VAPOR DIFFUSION, MACRO-
REMARK 280 SEEDING, SOAKING, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-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 28.02500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 39.39950
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.96350
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 39.39950
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 28.02500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 35.96350
REMARK 290 SMTRY3 4 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: 2760 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12390 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -51.0 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 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 37 CG CD OE1 OE2
REMARK 470 GLU A 39 CG CD OE1 OE2
REMARK 470 LYS A 62 CG CD CE NZ
REMARK 470 GLU A 74 CD OE1 OE2
REMARK 470 GLN A 75 CG CD OE1 NE2
REMARK 470 GLU A 76 CD OE1 OE2
REMARK 470 GLU A 77 CG CD OE1 OE2
REMARK 470 ARG A 93 NE CZ NH1 NH2
REMARK 470 LYS A 96 CG CD CE NZ
REMARK 470 GLU A 97 CG CD OE1 OE2
REMARK 470 LYS A 109 CG CD CE NZ
REMARK 470 LYS A 148 CG CD CE NZ
REMARK 470 ARG A 150 CG CD NE CZ NH1 NH2
REMARK 470 SER A 171 OG
REMARK 470 GLN A 187 OE1 NE2
REMARK 470 GLN A 192 OE1 NE2
REMARK 470 ARG A 202 NH1 NH2
REMARK 470 LYS A 223 CG CD CE NZ
REMARK 470 LYS A 236 CE NZ
REMARK 470 ARG A 240 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 87 CE NZ
REMARK 470 GLN B 104 CG CD OE1 NE2
REMARK 470 ARG B 113 NH1 NH2
REMARK 470 ASP B 119 OD1 OD2
REMARK 470 GLU B 138 CG CD OE1 OE2
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 GLU A 76 CG
REMARK 480 LYS A 243 OXT
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 76 CB GLU A 76 CG 0.884
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 ASP A 70 CB - CG - OD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 GLU A 76 CA - CB - CG ANGL. DEV. = -19.8 DEGREES
REMARK 500 ASP A 100 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP A 102 CB - CG - OD2 ANGL. DEV. = 6.4 DEGREES
REMARK 500 ASP B 95 CB - CG - OD1 ANGL. DEV. = 7.1 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ALA A 61A 141.20 -173.57
REMARK 500 ARG A 115 -169.49 -168.88
REMARK 500 LEU B 88 -119.49 40.83
REMARK 500 GLN B 98 -111.54 -128.26
REMARK 500 GLN B 104 -129.02 46.16
REMARK 500 LYS B 122 -50.46 -132.61
REMARK 500
REMARK 500 REMARK: NULL
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 A 261 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 70 OD1
REMARK 620 2 ASN A 72 O 93.6
REMARK 620 3 GLN A 75 O 165.9 80.4
REMARK 620 4 GLU A 80 OE2 101.3 163.2 86.8
REMARK 620 5 HOH A 710 O 84.6 92.1 108.2 81.7
REMARK 620 6 HOH A 808 O 73.2 88.1 93.8 103.5 157.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 262 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR A 185 O
REMARK 620 2 ASP A 185A O 79.9
REMARK 620 3 ARG A 222 O 169.0 92.5
REMARK 620 4 LYS A 224 O 86.8 119.7 90.2
REMARK 620 5 HOH A 716 O 90.9 170.4 97.0 62.2
REMARK 620 6 HOH A 732 O 95.9 88.6 91.8 151.6 89.5
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 261
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 262
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE D76 A 700
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1XKA RELATED DB: PDB
REMARK 900 FACTOR XA COMPLEXED WITH A SYNTHETIC INHIBITOR FX-2212A
REMARK 900 RELATED ID: 1FAX RELATED DB: PDB
REMARK 900 FACTOR XA COMPLEXED WITH A SYNTHETIC INHIBITOR DX-9065
DBREF 1V3X A 16 243 UNP P00742 FA10_HUMAN 235 467
DBREF 1V3X B 87 138 UNP P00742 FA10_HUMAN 127 178
SEQRES 1 A 233 ILE VAL GLY GLY GLN GLU CYS LYS ASP GLY GLU CYS PRO
SEQRES 2 A 233 TRP GLN ALA LEU LEU ILE ASN GLU GLU ASN GLU GLY PHE
SEQRES 3 A 233 CYS GLY GLY THR ILE LEU SER GLU PHE TYR ILE LEU THR
SEQRES 4 A 233 ALA ALA HIS CYS LEU TYR GLN ALA LYS ARG PHE LYS VAL
SEQRES 5 A 233 ARG VAL GLY ASP ARG ASN THR GLU GLN GLU GLU GLY GLY
SEQRES 6 A 233 GLU ALA VAL HIS GLU VAL GLU VAL VAL ILE LYS HIS ASN
SEQRES 7 A 233 ARG PHE THR LYS GLU THR TYR ASP PHE ASP ILE ALA VAL
SEQRES 8 A 233 LEU ARG LEU LYS THR PRO ILE THR PHE ARG MET ASN VAL
SEQRES 9 A 233 ALA PRO ALA CYS LEU PRO GLU ARG ASP TRP ALA GLU SER
SEQRES 10 A 233 THR LEU MET THR GLN LYS THR GLY ILE VAL SER GLY PHE
SEQRES 11 A 233 GLY ARG THR HIS GLU LYS GLY ARG GLN SER THR ARG LEU
SEQRES 12 A 233 LYS MET LEU GLU VAL PRO TYR VAL ASP ARG ASN SER CYS
SEQRES 13 A 233 LYS LEU SER SER SER PHE ILE ILE THR GLN ASN MET PHE
SEQRES 14 A 233 CYS ALA GLY TYR ASP THR LYS GLN GLU ASP ALA CYS GLN
SEQRES 15 A 233 GLY ASP SER GLY GLY PRO HIS VAL THR ARG PHE LYS ASP
SEQRES 16 A 233 THR TYR PHE VAL THR GLY ILE VAL SER TRP GLY GLU GLY
SEQRES 17 A 233 CYS ALA ARG LYS GLY LYS TYR GLY ILE TYR THR LYS VAL
SEQRES 18 A 233 THR ALA PHE LEU LYS TRP ILE ASP ARG SER MET LYS
SEQRES 1 B 52 LYS LEU CYS SER LEU ASP ASN GLY ASP CYS ASP GLN PHE
SEQRES 2 B 52 CYS HIS GLU GLU GLN ASN SER VAL VAL CYS SER CYS ALA
SEQRES 3 B 52 ARG GLY TYR THR LEU ALA ASP ASN GLY LYS ALA CYS ILE
SEQRES 4 B 52 PRO THR GLY PRO TYR PRO CYS GLY LYS GLN THR LEU GLU
HET CA A 261 1
HET CA A 262 1
HET D76 A 700 35
HETNAM CA CALCIUM ION
HETNAM D76 (2R)-4-[(6-CHLORO-2-NAPHTHYL)SULFONYL]-1-[(5-METHYL-4,
HETNAM 2 D76 5,6,7-TETRAHYDRO[1,3]THIAZOLO[5,4-C]PYRIDIN-2-YL)
HETNAM 3 D76 CARBONYL]PIPERAZ INE-2-CARBOXAMIDE
HETSYN D76 1-[6-METHYL-4,5,6,7-TETRAHYDROTHIAZOLO(5,4-C)PYRIDIN-2-
HETSYN 2 D76 YL] CARBONYL-2-CARBAMOYL-4-(6-CHLORONAPHTH-2-
HETSYN 3 D76 YLSULPHONYL)PIPERAZINE
FORMUL 3 CA 2(CA 2+)
FORMUL 5 D76 C23 H24 CL N5 O4 S2
FORMUL 6 HOH *161(H2 O)
HELIX 1 1 ALA A 55 GLN A 61 5 7
HELIX 2 2 GLU A 124A THR A 131 1 8
HELIX 3 3 ASP A 164 SER A 172 1 9
HELIX 4 4 PHE A 234 MET A 242 1 9
HELIX 5 5 LYS B 87 CYS B 96 5 10
SHEET 1 A 8 GLN A 20 GLU A 21 0
SHEET 2 A 8 LYS A 156 VAL A 163 -1 O MET A 157 N GLN A 20
SHEET 3 A 8 MET A 180 ALA A 183 -1 O CYS A 182 N VAL A 163
SHEET 4 A 8 GLY A 226 LYS A 230 -1 O TYR A 228 N PHE A 181
SHEET 5 A 8 THR A 206 TRP A 215 -1 N ILE A 212 O THR A 229
SHEET 6 A 8 PRO A 198 PHE A 203 -1 N PHE A 203 O THR A 206
SHEET 7 A 8 THR A 135 GLY A 140 -1 N ILE A 137 O VAL A 200
SHEET 8 A 8 LYS A 156 VAL A 163 -1 O VAL A 160 N GLY A 136
SHEET 1 B 7 GLN A 30 ASN A 35 0
SHEET 2 B 7 GLY A 40 ILE A 46 -1 O CYS A 42 N LEU A 33
SHEET 3 B 7 TYR A 51 THR A 54 -1 O LEU A 53 N THR A 45
SHEET 4 B 7 ALA A 104 LEU A 108 -1 O ALA A 104 N THR A 54
SHEET 5 B 7 ALA A 81 LYS A 90 -1 N ILE A 89 O VAL A 105
SHEET 6 B 7 PHE A 64 VAL A 68 -1 N VAL A 66 O HIS A 83
SHEET 7 B 7 GLN A 30 ASN A 35 -1 N ILE A 34 O LYS A 65
SHEET 1 C 2 PHE B 99 GLU B 103 0
SHEET 2 C 2 SER B 106 SER B 110 -1 O VAL B 108 N HIS B 101
SHEET 1 D 2 TYR B 115 LEU B 117 0
SHEET 2 D 2 CYS B 124 PRO B 126 -1 O ILE B 125 N THR B 116
SSBOND 1 CYS A 22 CYS A 27 1555 1555 1.99
SSBOND 2 CYS A 42 CYS A 58 1555 1555 1.99
SSBOND 3 CYS A 122 CYS B 132 1555 1555 2.05
SSBOND 4 CYS A 168 CYS A 182 1555 1555 1.95
SSBOND 5 CYS A 191 CYS A 220 1555 1555 2.00
SSBOND 6 CYS B 89 CYS B 100 1555 1555 2.06
SSBOND 7 CYS B 96 CYS B 109 1555 1555 1.95
SSBOND 8 CYS B 111 CYS B 124 1555 1555 2.04
LINK OD1 ASP A 70 CA CA A 261 1555 1555 2.24
LINK O ASN A 72 CA CA A 261 1555 1555 2.35
LINK O GLN A 75 CA CA A 261 1555 1555 2.29
LINK OE2 GLU A 80 CA CA A 261 1555 1555 2.44
LINK O TYR A 185 CA CA A 262 1555 1555 2.38
LINK O ASP A 185A CA CA A 262 1555 1555 2.63
LINK O ARG A 222 CA CA A 262 1555 1555 2.35
LINK O LYS A 224 CA CA A 262 1555 1555 2.29
LINK CA CA A 261 O HOH A 710 1555 1555 2.45
LINK CA CA A 261 O HOH A 808 1555 1555 2.65
LINK CA CA A 262 O HOH A 716 1555 1555 2.90
LINK CA CA A 262 O HOH A 732 1555 1555 2.64
SITE 1 AC1 6 ASP A 70 ASN A 72 GLN A 75 GLU A 80
SITE 2 AC1 6 HOH A 710 HOH A 808
SITE 1 AC2 6 TYR A 185 ASP A 185A ARG A 222 LYS A 224
SITE 2 AC2 6 HOH A 716 HOH A 732
SITE 1 AC3 20 GLU A 97 THR A 98 TYR A 99 PHE A 174
SITE 2 AC3 20 ASP A 189 ALA A 190 CYS A 191 GLN A 192
SITE 3 AC3 20 SER A 195 VAL A 213 TRP A 215 GLY A 216
SITE 4 AC3 20 GLU A 217 GLY A 218 CYS A 220 GLY A 226
SITE 5 AC3 20 ILE A 227 TYR A 228 HOH A 750 HOH A 794
CRYST1 56.050 71.927 78.799 90.00 90.00 90.00 P 21 21 21 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 0.017841 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013903 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012690 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
