HEADER BLOOD CLOTTING 26-JUN-08 2VWO
TITLE AMINOPYRROLIDINE FACTOR XA INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACTIVATED FACTOR XA HEAVY CHAIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PEPTIDASE S1 DOMAIN, RESIDUES 235-475;
COMPND 5 EC: 3.4.21.6;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: FACTOR X LIGHT CHAIN;
COMPND 10 CHAIN: L;
COMPND 11 FRAGMENT: EGF2, RESIDUES 126-180;
COMPND 12 EC: 3.4.21.6;
COMPND 13 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: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 9 ORGANISM_COMMON: HUMAN;
SOURCE 10 ORGANISM_TAXID: 9606;
SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HYDROLASE, CATION, PLASMA, CALCIUM, ZYMOGEN, PROTEASE, INHIBITOR,
KEYWDS 2 POLYMORPHISM, GLYCOPROTEIN, GAMMA-CARBOXYGLUTAMIC ACID, BLOOD
KEYWDS 3 CLOTTING, COAGULATION FACTOR, HYDROXYLATION, SERINE PROTEASE, EGF-
KEYWDS 4 LIKE DOMAIN, CLEAVAGE ON PAIR OF BASIC RESIDUES
EXPDTA X-RAY DIFFRACTION
AUTHOR K.GROEBKE-ZBINDEN,D.W.BANNER,J.M.BENZ,F.BLASCO,G.DECORET,J.HIMBER,
AUTHOR 2 B.KUHN,N.PANDAY,F.RICKLIN,P.RISCH,D.SCHLATTER,M.STAHL,R.UNGER,W.HAAP
REVDAT 2 13-DEC-23 2VWO 1 REMARK LINK
REVDAT 1 07-JUL-09 2VWO 0
JRNL AUTH K.G.ZBINDEN,L.ANSELM,D.W.BANNER,J.M.BENZ,F.BLASCO,G.DECORET,
JRNL AUTH 2 J.HIMBER,B.KUHN,N.PANDAY,F.RICKLIN,P.RISCH,D.SCHLATTER,
JRNL AUTH 3 M.STAHL,S.THOMI,R.UNGER,W.HAAP
JRNL TITL DESIGN OF NOVEL AMINOPYRROLIDINE FACTOR XA INHIBITORS FROM A
JRNL TITL 2 SCREENING HIT.
JRNL REF EUR.J.MED.CHEM. V. 44 2787 2009
JRNL REFN ISSN 0223-5234
JRNL PMID 19200624
JRNL DOI 10.1016/J.EJMECH.2008.12.025
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.4.0077
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) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.09
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 34963
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) : 0.196
REMARK 3 R VALUE (WORKING SET) : 0.194
REMARK 3 FREE R VALUE : 0.228
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1839
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.64
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2499
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2320
REMARK 3 BIN FREE R VALUE SET COUNT : 132
REMARK 3 BIN FREE R VALUE : 0.2450
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2156
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 39
REMARK 3 SOLVENT ATOMS : 221
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.85
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.14000
REMARK 3 B22 (A**2) : 0.14000
REMARK 3 B33 (A**2) : -0.28000
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): 0.099
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.099
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.061
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.712
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.955
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.937
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2304 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3108 ; 1.378 ; 1.967
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 284 ; 5.686 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 102 ;34.647 ;23.922
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 396 ;12.306 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 15 ;12.608 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 330 ; 0.090 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1750 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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 ; 0.784 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2253 ; 1.407 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 898 ; 1.893 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 855 ; 3.033 ; 4.500
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 WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2VWO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-JUN-08.
REMARK 100 THE DEPOSITION ID IS D_1290036708.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-FEB-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9787
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36802
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 6.400
REMARK 200 R MERGE (I) : 0.05000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.70
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.40
REMARK 200 R MERGE FOR SHELL (I) : 0.37000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.420
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 2VVC
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 24.70250
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 52.64050
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 52.64050
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 37.05375
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 52.64050
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 52.64050
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 12.35125
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 52.64050
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 52.64050
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 37.05375
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 52.64050
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 52.64050
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 12.35125
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 24.70250
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 1960 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15490 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, L
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 NA NA A1249 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A2059 LIES ON A SPECIAL POSITION.
REMARK 400
REMARK 400 COMPOUND
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, ARG 372 TO GLU
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 GLY A 246
REMARK 465 LEU A 247
REMARK 465 PRO A 248
REMARK 465 LYS A 249
REMARK 465 ALA A 250
REMARK 465 LYS A 251
REMARK 465 ARG L 86
REMARK 465 LYS L 87
REMARK 465 HIS L 101
REMARK 465 GLU L 102
REMARK 465 GLU L 103
REMARK 465 GLN L 104
REMARK 465 ASN L 105
REMARK 465 SER L 106
REMARK 465 ASP L 119
REMARK 465 ASN L 120
REMARK 465 GLY L 121
REMARK 465 ARG L 140
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 245 CA C O CB CG CD NE
REMARK 470 ARG A 245 CZ NH1 NH2
REMARK 470 ARG L 139 CA C O CB CG CD NE
REMARK 470 ARG L 139 CZ NH1 NH2
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 ASN A 92 CG OD1 ND2
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 O HOH A 2019 O HOH A 2065 2.03
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 TYR A 99 14.33 56.81
REMARK 500 ASP L 95 -4.35 70.75
REMARK 500 GLN L 98 -104.51 -129.11
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 A2016 DISTANCE = 6.37 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 NA A1249 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN A 20 OE1
REMARK 620 2 GLN A 20 OE1 101.8
REMARK 620 3 HOH A2010 O 94.1 162.0
REMARK 620 4 HOH A2010 O 163.0 92.8 73.0
REMARK 620 5 HOH A2011 O 110.5 84.2 82.4 79.4
REMARK 620 6 HOH A2011 O 85.0 109.5 79.9 81.9 157.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A1246 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 70 OD1
REMARK 620 2 ASN A 72 O 87.5
REMARK 620 3 GLN A 75 O 166.2 86.8
REMARK 620 4 GLU A 77 OE2 86.7 87.6 80.5
REMARK 620 5 GLU A 80 OE2 93.5 171.7 90.4 84.2
REMARK 620 6 HOH A2060 O 91.4 92.9 101.4 178.0 95.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A1247 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR A 185 O
REMARK 620 2 ASP A 185A O 80.9
REMARK 620 3 ARG A 222 O 166.5 86.3
REMARK 620 4 HOH A2163 O 96.1 84.1 86.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A1248 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A2038 O
REMARK 620 2 HOH A2039 O 86.0
REMARK 620 3 HOH A2103 O 96.5 177.0
REMARK 620 4 HOH A2105 O 89.2 93.8 84.5
REMARK 620 5 HOH A2106 O 177.4 96.0 81.6 92.3
REMARK 620 6 HOH A2131 O 88.8 81.6 100.2 175.1 89.8
REMARK 620 N 1 2 3 4 5
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: DSSP
REMARK 700 THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 8-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LZG A 1245
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1246
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 1247
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 1248
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 1249
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1250
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1251
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1WU1 RELATED DB: PDB
REMARK 900 FACTOR XA IN COMPLEX WITH THE INHIBITOR 4 -[(5-CHLOROINDOL-2-YL)
REMARK 900 SULFONYL]-2-(2- METHYLPROPYL)-1-[[5-(PYRIDIN-4-YL)PYRIMIDIN -2-YL]
REMARK 900 CARBONYL]PIPERAZINE
REMARK 900 RELATED ID: 2J34 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF A HUMAN FACTOR XA INHIBITOR COMPLEX
REMARK 900 RELATED ID: 2BQ7 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF FACTOR XA IN COMPLEX WITH 43
REMARK 900 RELATED ID: 2W3K RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF FXA IN COMPLEX WITH 4 ,4-DISUBSTITUTED
REMARK 900 PYRROLIDINE-1,2- DICARBOXAMIDE INHIBITOR 1
REMARK 900 RELATED ID: 1XKA RELATED DB: PDB
REMARK 900 FACTOR XA COMPLEXED WITH A SYNTHETIC INHIBITOR FX-2212A,(2S) -(3'-
REMARK 900 AMIDINO-3- BIPHENYLYL)-5-(4-PYRIDYLAMINO)PENTANOIC ACID
REMARK 900 RELATED ID: 1NFW RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN COAGULATION FACTOR XA COMPLEXEDWITH
REMARK 900 RPR209685
REMARK 900 RELATED ID: 2GD4 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE ANTITHROMBIN-S195A FACTOR XA-
REMARK 900 PENTASACCHARIDE COMPLEX
REMARK 900 RELATED ID: 2VVV RELATED DB: PDB
REMARK 900 AMINOPYRROLIDINE-RELATED TRIAZOLE FACTOR XA INHIBITOR
REMARK 900 RELATED ID: 1MSX RELATED DB: PDB
REMARK 900 HUMAN FACTOR XA COMPLEXED WITH 2-[3-(15N- AMINO-15N-IMINO-13C-
REMARK 900 METHYL)PHENOXY]-6-[3 -(15N-AMINO-13C-METHYL)PHENOXY]-3,5- DIFLUORO-
REMARK 900 4-METHYLPYRIDINE (ZK-806299), BINDING MODELFROM DOUBLE REDOR NMR
REMARK 900 AND MD SIMULATIONS.
REMARK 900 RELATED ID: 1LPG RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF FXA IN COMPLEX WITH 79.
REMARK 900 RELATED ID: 2VVU RELATED DB: PDB
REMARK 900 AMINOPYRROLIDINE FACTOR XA INHIBITOR
REMARK 900 RELATED ID: 1P0S RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF BLOOD COAGULATION FACTOR XA IN COMPLEXWITH
REMARK 900 ECOTIN M84R
REMARK 900 RELATED ID: 2G00 RELATED DB: PDB
REMARK 900 FACTOR XA IN COMPLEX WITH THE INHIBITOR 3 -(6-(2'-((DIMETHYLAMINO)
REMARK 900 METHYL)-4-BIPHENYLYL )-7-OXO-3-(TRIFLUOROMETHYL)-4,5,6,7-
REMARK 900 TETRAHYDRO-1H-PYRAZOLO[3,4-C]PYRIDIN-1- YL)BENZAMIDE
REMARK 900 RELATED ID: 1MQ6 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF 3-CHLORO-N-[4-CHLORO -2-[[(5-CHLORO-2-
REMARK 900 PYRIDINYL)AMINO]CARBONYL ]-6-METHOXYPHENYL]-4-[[(4,5-DIHYDRO-2-
REMARK 900 OXAZOLYL)METHYLAMINO]METHYL]-2- THIOPHENECARBOXAMIDE COMPLEXED WITH
REMARK 900 HUMAN FACTOR XA
REMARK 900 RELATED ID: 1XKB RELATED DB: PDB
REMARK 900 FACTOR XA COMPLEXED WITH A SYNTHETIC INHIBITOR FX-2212A,(2S) -(3'-
REMARK 900 AMIDINO-3- BIPHENYLYL)-5-(4-PYRIDYLAMINO)PENTANOIC ACID
REMARK 900 RELATED ID: 1IQE RELATED DB: PDB
REMARK 900 HUMAN COAGULATION FACTOR XA COMPLEXD WITH M55590
REMARK 900 RELATED ID: 1G2M RELATED DB: PDB
REMARK 900 FACTOR XA INHIBITOR COMPLEX
REMARK 900 RELATED ID: 2VH0 RELATED DB: PDB
REMARK 900 STRUCTURE AND PROPERTY BASED DESIGN OF FACTOR XA INHIBITORS:BIARYL
REMARK 900 PYRROLIDIN-2- ONES INCORPORATING BASIC HETEROCYCLIC MOTIFS
REMARK 900 RELATED ID: 1NFY RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN COAGULATION FACTOR XA COMPLEXEDWITH
REMARK 900 RPR200095
REMARK 900 RELATED ID: 2UWL RELATED DB: PDB
REMARK 900 SELECTIVE AND DUAL ACTION ORALLY ACTIVE INHIBITORS OF THROMBIN AND
REMARK 900 FACTOR XA
REMARK 900 RELATED ID: 2BOK RELATED DB: PDB
REMARK 900 FACTOR XA - CATION
REMARK 900 RELATED ID: 1HCG RELATED DB: PDB
REMARK 900 BLOOD COAGULATION FACTOR XA
REMARK 900 RELATED ID: 1LPZ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF FXA IN COMPLEX WITH 41.
REMARK 900 RELATED ID: 2W3I RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF FXA IN COMPLEX WITH 4 ,4-DISUBSTITUTED
REMARK 900 PYRROLIDINE-1,2- DICARBOXAMIDE INHIBITOR 2
REMARK 900 RELATED ID: 1Z6E RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF FACTOR XA COMPLEXED TO RAZAXABAN
REMARK 900 RELATED ID: 2JKH RELATED DB: PDB
REMARK 900 FACTOR XA - CATION INHIBITOR COMPLEX
REMARK 900 RELATED ID: 2UWP RELATED DB: PDB
REMARK 900 FACTOR XA INHIBITOR COMPLEX
REMARK 900 RELATED ID: 1G2L RELATED DB: PDB
REMARK 900 FACTOR XA INHIBITOR COMPLEX
REMARK 900 RELATED ID: 1NFU RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN COAGULATION FACTOR XA COMPLEXEDWITH
REMARK 900 RPR132747
REMARK 900 RELATED ID: 2BQ6 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF FACTOR XA IN COMPLEX WITH 21
REMARK 900 RELATED ID: 1FAX RELATED DB: PDB
REMARK 900 COAGULATION FACTOR XA INHIBITOR COMPLEX
REMARK 900 RELATED ID: 1IQF RELATED DB: PDB
REMARK 900 HUMAN COAGULATION FACTOR XA COMPLEXD WITH M55165
REMARK 900 RELATED ID: 1NL8 RELATED DB: PDB
REMARK 900 THEORETICAL MODEL OF THE TISSUE FACTOR/ FACTOR VIIA/FACTORXA COMPLEX
REMARK 900 RELATED ID: 1IQG RELATED DB: PDB
REMARK 900 HUNMAN COAGULATION FACTOR XA COMPLEXD WITH M55159
REMARK 900 RELATED ID: 1IQH RELATED DB: PDB
REMARK 900 HUNMAN COAGULATION FACTOR XA COMPLEXD WITH M55143
REMARK 900 RELATED ID: 1LQD RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF FXA IN COMPLEX WITH 45.
REMARK 900 RELATED ID: 2UWO RELATED DB: PDB
REMARK 900 SELECTIVE AND DUAL ACTION ORALLY ACTIVE INHIBITORS OF THROMBIN AND
REMARK 900 FACTOR XA
REMARK 900 RELATED ID: 1C5M RELATED DB: PDB
REMARK 900 STRUCTURAL BASIS FOR SELECTIVITY OF A SMALL MOLECULE, S1-BINDING,
REMARK 900 SUB- MICROMOLAR INHIBITOR OF UROKINASE TYPE PLASMINOGEN ACTIVATOR
REMARK 900 RELATED ID: 1IOE RELATED DB: PDB
REMARK 900 HUNMAN COAGULATION FACTOR XA COMPLEXD WITH M55532
REMARK 900 RELATED ID: 1F0S RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN COAGULATION FACTOR XA COMPLEXED WITH
REMARK 900 RPR208707
REMARK 900 RELATED ID: 1F0R RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN COAGULATION FACTOR XA COMPLEXED WITH
REMARK 900 RPR208815
REMARK 900 RELATED ID: 2BMG RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF FACTOR XA IN COMPLEX WITH 50
REMARK 900 RELATED ID: 1MQ5 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF 3-CHLORO-N-[4-CHLORO -2-[[(4-CHLOROPHENYL)
REMARK 900 AMINO]CARBONYL]PHENYL]- 4-[(4-METHYL-1-PIPERAZINYL)METHYL]-2-
REMARK 900 THIOPHENECARBOXAMIDE COMPLEXED WITHHUMAN FACTOR XA
REMARK 900 RELATED ID: 1IQN RELATED DB: PDB
REMARK 900 HUMAN COAGULATION FACTOR XA COMPLEXD WITH M55192
REMARK 900 RELATED ID: 2BQW RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF FACTOR XA IN COMPLEX WITH COMPOUND 45
REMARK 900 RELATED ID: 1IQM RELATED DB: PDB
REMARK 900 HUNMAN COAGULATION FACTOR XA COMPLEXD WITH M54471
REMARK 900 RELATED ID: 1EZQ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN COAGULATION FACTOR XA COMPLEXED WITH
REMARK 900 RPR128515
REMARK 900 RELATED ID: 2VWL RELATED DB: PDB
REMARK 900 AMINOPYRROLIDINE FACTOR XA INHIBITOR
REMARK 900 RELATED ID: 2VH6 RELATED DB: PDB
REMARK 900 STRUCTURE AND PROPERTY BASED DESIGN OF FACTOR XA INHIBITORS:
REMARK 900 PYRROLIDIN-2-ONES WITH BIARYL P4 MOTIFS
REMARK 900 RELATED ID: 1FJS RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE INHIBITOR ZK-807834 (CI-1031)COMPLEXED
REMARK 900 WITH FACTOR XA
REMARK 900 RELATED ID: 1LPK RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF FXA IN COMPLEX WITH 125.
REMARK 900 RELATED ID: 2J4I RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF A HUMAN FACTOR XA INHIBITOR COMPLEX
REMARK 900 RELATED ID: 1NFX RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN COAGULATION FACTOR XA COMPLEXEDWITH
REMARK 900 RPR208944
REMARK 900 RELATED ID: 2VWN RELATED DB: PDB
REMARK 900 AMINOPYRROLIDINE FACTOR XA INHIBITOR
REMARK 900 RELATED ID: 2J94 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF A HUMAN FACTOR XA INHIBITOR COMPLEX
REMARK 900 RELATED ID: 1IQJ RELATED DB: PDB
REMARK 900 HUNMAN COAGULATION FACTOR XA COMPLEXD WITH M55124
REMARK 900 RELATED ID: 2CJI RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF A HUMAN FACTOR XA INHIBITOR COMPLEX
REMARK 900 RELATED ID: 2J95 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF A HUMAN FACTOR XA INHIBITOR COMPLEX
REMARK 900 RELATED ID: 2BOH RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF FACTOR XA IN COMPLEX WITH 1
REMARK 900 RELATED ID: 2J38 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF A HUMAN FACTOR XA INHIBITOR COMPLEX
REMARK 900 RELATED ID: 2W26 RELATED DB: PDB
REMARK 900 FATOR XA IN COMPLEX WITH BAY59-7939
REMARK 900 RELATED ID: 2VVC RELATED DB: PDB
REMARK 900 AMINOPYRROLIDINE FACTOR XA INHIBITOR
REMARK 900 RELATED ID: 1IQI RELATED DB: PDB
REMARK 900 HUNMAN COAGULATION FACTOR XA COMPLEXD WITH M55125
REMARK 900 RELATED ID: 2VWM RELATED DB: PDB
REMARK 900 AMINOPYRROLIDINE FACTOR XA INHIBITOR
REMARK 900 RELATED ID: 1KYE RELATED DB: PDB
REMARK 900 FACTOR XA IN COMPLEX WITH (R)-2-(3- ADAMANTAN-1-YL-UREIDO)-3-(3-
REMARK 900 CARBAMIMIDOYL- PHENYL)-N-PHENETHYL-PROPIONAMIDE
REMARK 900 RELATED ID: 1IQK RELATED DB: PDB
REMARK 900 HUNMAN COAGULATION FACTOR XA COMPLEXD WITH M55113
REMARK 900 RELATED ID: 1V3X RELATED DB: PDB
REMARK 900 FACTOR XA IN COMPLEX WITH THE INHIBITOR 1 -[6-METHYL-4,5,6,7-
REMARK 900 TETRAHYDROTHIAZOLO(5, 4-C)PYRIDIN-2-YL] CARBONYL-2-CARBAMOYL-4 -(6-
REMARK 900 CHLORONAPHTH-2-YLSULPHONYL)PIPERAZINE
REMARK 900 RELATED ID: 2FZZ RELATED DB: PDB
REMARK 900 FACTOR XA IN COMPLEX WITH THE INHIBITOR 1 -(3-AMINO-1,2-
REMARK 900 BENZISOXAZOL-5-YL)-6-(2 '-(((3R)-3-HYDROXY-1-PYRROLIDINYL)METHYL)-4
REMARK 900 -BIPHENYLYL)-3-(TRIFLUOROMETHYL)-1,4,5,6- TETRAHYDRO-7H-PYRAZOLO[3,
REMARK 900 4-C]PYRIDIN-7- ONE
REMARK 900 RELATED ID: 2J2U RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF A HUMAN FACTOR XA INHIBITOR COMPLEX
REMARK 900 RELATED ID: 1KSN RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN COAGULATION FACTOR XA COMPLEXEDWITH
REMARK 900 FXV673
REMARK 900 RELATED ID: 1IQL RELATED DB: PDB
REMARK 900 HUNMAN COAGULATION FACTOR XA COMPLEXD WITH M54476
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 ARG-GLU MUTANT.THE RESIDUE NUMBERING IN THE CATALYTIC
REMARK 999 DOMAIN FOLLOWS THAT OF CHYMOTRYPSINOGEN
DBREF 2VWO A 16 251 UNP P00742 FA10_HUMAN 235 475
DBREF 2VWO L 86 140 UNP P00742 FA10_HUMAN 126 180
SEQADV 2VWO GLU A 150 UNP P00742 ARG 372 ENGINEERED MUTATION
SEQRES 1 A 241 ILE VAL GLY GLY GLN GLU CYS LYS ASP GLY GLU CYS PRO
SEQRES 2 A 241 TRP GLN ALA LEU LEU ILE ASN GLU GLU ASN GLU GLY PHE
SEQRES 3 A 241 CYS GLY GLY THR ILE LEU SER GLU PHE TYR ILE LEU THR
SEQRES 4 A 241 ALA ALA HIS CYS LEU TYR GLN ALA LYS ARG PHE LYS VAL
SEQRES 5 A 241 ARG VAL GLY ASP ARG ASN THR GLU GLN GLU GLU GLY GLY
SEQRES 6 A 241 GLU ALA VAL HIS GLU VAL GLU VAL VAL ILE LYS HIS ASN
SEQRES 7 A 241 ARG PHE THR LYS GLU THR TYR ASP PHE ASP ILE ALA VAL
SEQRES 8 A 241 LEU ARG LEU LYS THR PRO ILE THR PHE ARG MET ASN VAL
SEQRES 9 A 241 ALA PRO ALA CYS LEU PRO GLU ARG ASP TRP ALA GLU SER
SEQRES 10 A 241 THR LEU MET THR GLN LYS THR GLY ILE VAL SER GLY PHE
SEQRES 11 A 241 GLY ARG THR HIS GLU LYS GLY GLU GLN SER THR ARG LEU
SEQRES 12 A 241 LYS MET LEU GLU VAL PRO TYR VAL ASP ARG ASN SER CYS
SEQRES 13 A 241 LYS LEU SER SER SER PHE ILE ILE THR GLN ASN MET PHE
SEQRES 14 A 241 CYS ALA GLY TYR ASP THR LYS GLN GLU ASP ALA CYS GLN
SEQRES 15 A 241 GLY ASP SER GLY GLY PRO HIS VAL THR ARG PHE LYS ASP
SEQRES 16 A 241 THR TYR PHE VAL THR GLY ILE VAL SER TRP GLY GLU GLY
SEQRES 17 A 241 CYS ALA ARG LYS GLY LYS TYR GLY ILE TYR THR LYS VAL
SEQRES 18 A 241 THR ALA PHE LEU LYS TRP ILE ASP ARG SER MET LYS THR
SEQRES 19 A 241 ARG GLY LEU PRO LYS ALA LYS
SEQRES 1 L 55 ARG LYS LEU CYS SER LEU ASP ASN GLY ASP CYS ASP GLN
SEQRES 2 L 55 PHE CYS HIS GLU GLU GLN ASN SER VAL VAL CYS SER CYS
SEQRES 3 L 55 ALA ARG GLY TYR THR LEU ALA ASP ASN GLY LYS ALA CYS
SEQRES 4 L 55 ILE PRO THR GLY PRO TYR PRO CYS GLY LYS GLN THR LEU
SEQRES 5 L 55 GLU ARG ARG
HET LZG A1245 33
HET CA A1246 1
HET NA A1247 1
HET NA A1248 1
HET NA A1249 1
HET CL A1250 1
HET CL A1251 1
HETNAM LZG 5-CHLORO-THIOPHENE-2-CARBOXYLIC ACID ((3S,4S)-4-FLUORO-
HETNAM 2 LZG 1-{[2-FLUORO-4-(2-OXO-2H-PYRIDIN-1-YL)-
HETNAM 3 LZG PHENYLCARBAMOYL]-METHYL}-PYRROLIDIN-3-YL)-AMIDE
HETNAM CA CALCIUM ION
HETNAM NA SODIUM ION
HETNAM CL CHLORIDE ION
FORMUL 3 LZG C22 H19 CL F2 N4 O3 S
FORMUL 4 CA CA 2+
FORMUL 5 NA 3(NA 1+)
FORMUL 8 CL 2(CL 1-)
FORMUL 10 HOH *221(H2 O)
HELIX 1 1 ALA A 55 ALA A 61A 5 8
HELIX 2 2 GLU A 124A LEU A 131A 1 9
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 LEU L 91 CYS L 96 5 6
SHEET 1 AA 9 GLN A 20 GLU A 21 0
SHEET 2 AA 9 LYS A 156 VAL A 163 -1 O MET A 157 N GLN A 20
SHEET 3 AA 9 MET A 180 ALA A 183 -1 O CYS A 182 N VAL A 163
SHEET 4 AA 9 GLY A 226 LYS A 230 -1 O GLY A 226 N ALA A 183
SHEET 5 AA 9 THR A 206 TRP A 215 -1 O ILE A 212 N THR A 229
SHEET 6 AA 9 PRO A 198 PHE A 203 -1 O HIS A 199 N THR A 210
SHEET 7 AA 9 THR A 135 GLY A 140 -1 O ILE A 137 N VAL A 200
SHEET 8 AA 9 LYS A 156 VAL A 163 1 O LYS A 156 N GLY A 140
SHEET 9 AA 9 GLN A 20 GLU A 21 -1 O GLN A 20 N MET A 157
SHEET 1 AB 7 ALA A 81 HIS A 83 0
SHEET 2 AB 7 LYS A 65 VAL A 68 -1 O VAL A 66 N HIS A 83
SHEET 3 AB 7 GLN A 30 ILE A 34 -1 O LEU A 32 N ARG A 67
SHEET 4 AB 7 GLY A 40 ILE A 46 -1 N PHE A 41 O LEU A 33
SHEET 5 AB 7 TYR A 51 THR A 54 -1 O LEU A 53 N THR A 45
SHEET 6 AB 7 ALA A 104 LEU A 108 -1 O ALA A 104 N THR A 54
SHEET 7 AB 7 VAL A 85 LYS A 90 -1 N GLU A 86 O ARG A 107
SHEET 1 LA 2 TYR L 115 LEU L 117 0
SHEET 2 LA 2 CYS L 124 PRO L 126 -1 O ILE L 125 N THR L 116
SSBOND 1 CYS A 22 CYS A 27 1555 1555 2.05
SSBOND 2 CYS A 42 CYS A 58 1555 1555 2.08
SSBOND 3 CYS A 122 CYS L 132 1555 1555 2.03
SSBOND 4 CYS A 168 CYS A 182 1555 1555 2.03
SSBOND 5 CYS A 191 CYS A 220 1555 1555 2.05
SSBOND 6 CYS L 89 CYS L 100 1555 1555 2.03
SSBOND 7 CYS L 96 CYS L 109 1555 1555 2.04
SSBOND 8 CYS L 111 CYS L 124 1555 1555 2.03
LINK OE1 GLN A 20 NA NA A1249 8665 1555 2.27
LINK OE1 GLN A 20 NA NA A1249 1555 1555 2.30
LINK OD1 ASP A 70 CA CA A1246 1555 1555 2.26
LINK O ASN A 72 CA CA A1246 1555 1555 2.26
LINK O GLN A 75 CA CA A1246 1555 1555 2.26
LINK OE2 GLU A 77 CA CA A1246 1555 1555 2.31
LINK OE2 GLU A 80 CA CA A1246 1555 1555 2.28
LINK O TYR A 185 NA NA A1247 1555 1555 2.28
LINK O ASP A 185A NA NA A1247 1555 1555 2.50
LINK O ARG A 222 NA NA A1247 1555 1555 2.27
LINK CA CA A1246 O HOH A2060 1555 1555 2.02
LINK NA NA A1247 O HOH A2163 1555 1555 2.40
LINK NA NA A1248 O HOH A2038 1555 1555 2.06
LINK NA NA A1248 O HOH A2039 1555 1555 2.15
LINK NA NA A1248 O HOH A2103 1555 1555 2.31
LINK NA NA A1248 O HOH A2105 1555 1555 1.95
LINK NA NA A1248 O HOH A2106 1555 1555 2.11
LINK NA NA A1248 O HOH A2131 1555 1555 2.22
LINK NA NA A1249 O HOH A2010 1555 8665 2.24
LINK NA NA A1249 O HOH A2010 1555 1555 2.26
LINK NA NA A1249 O HOH A2011 1555 8665 2.00
LINK NA NA A1249 O HOH A2011 1555 1555 2.00
SITE 1 AC1 23 GLU A 97 THR A 98 TYR A 99 ASN A 166
SITE 2 AC1 23 LYS A 169 PHE A 174 ASP A 189 ALA A 190
SITE 3 AC1 23 GLN A 192 VAL A 213 TRP A 215 GLY A 216
SITE 4 AC1 23 GLY A 218 CYS A 220 GLY A 226 ILE A 227
SITE 5 AC1 23 TYR A 228 CL A1250 HOH A2141 HOH A2143
SITE 6 AC1 23 HOH A2172 HOH A2208 HOH A2209
SITE 1 AC2 6 ASP A 70 ASN A 72 GLN A 75 GLU A 77
SITE 2 AC2 6 GLU A 80 HOH A2060
SITE 1 AC3 6 TYR A 185 ASP A 185A ARG A 222 LYS A 224
SITE 2 AC3 6 HOH A2163 HOH A2188
SITE 1 AC4 6 HOH A2038 HOH A2039 HOH A2103 HOH A2105
SITE 2 AC4 6 HOH A2106 HOH A2131
SITE 1 AC5 3 GLN A 20 HOH A2010 HOH A2011
SITE 1 AC6 4 ASN A 166 GLY A 218 LZG A1245 HOH A2184
SITE 1 AC7 4 GLN A 61 LYS A 96 THR A 177 GLN A 178
CRYST1 105.281 105.281 49.405 90.00 90.00 90.00 P 43 21 2 8
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 0.009498 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009498 0.000000 0.00000
SCALE3 0.000000 0.000000 0.020241 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
