HEADER HYDROLASE 17-MAY-00 1F0R
TITLE CRYSTAL STRUCTURE OF HUMAN COAGULATION FACTOR XA COMPLEXED WITH
TITLE 2 RPR208815
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: COAGULATION FACTOR XA;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: ACTIVATED FACTOR XA, HEAVY CHAIN;
COMPND 5 EC: 3.4.21.6;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: COAGULATION FACTOR XA;
COMPND 8 CHAIN: B;
COMPND 9 FRAGMENT: FACTOR X LIGHT CHAIN;
COMPND 10 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
KEYWDS PROTEIN-INHIBITOR COMPLEX, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.MAIGNAN,J.P.GUILLOTEAU,S.POUZIEUX,Y.M.CHOI-SLEDESKI,M.R.BECKER,
AUTHOR 2 S.I.KLEIN,W.R.EWING,H.W.PAULS,A.P.SPADA,V.MIKOL
REVDAT 3 13-MAR-24 1F0R 1 COMPND SOURCE REMARK LINK
REVDAT 2 24-FEB-09 1F0R 1 VERSN
REVDAT 1 20-SEP-00 1F0R 0
JRNL AUTH S.MAIGNAN,J.P.GUILLOTEAU,S.POUZIEUX,Y.M.CHOI-SLEDESKI,
JRNL AUTH 2 M.R.BECKER,S.I.KLEIN,W.R.EWING,H.W.PAULS,A.P.SPADA,V.MIKOL
JRNL TITL CRYSTAL STRUCTURES OF HUMAN FACTOR XA COMPLEXED WITH POTENT
JRNL TITL 2 INHIBITORS.
JRNL REF J.MED.CHEM. V. 43 3226 2000
JRNL REFN ISSN 0022-2623
JRNL PMID 10966741
JRNL DOI 10.1021/JM000940U
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 98.0
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)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 16710
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.216
REMARK 3 FREE R VALUE : 0.263
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1150
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2227
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 32
REMARK 3 SOLVENT ATOMS : 170
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 27.57
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.018
REMARK 3 BOND ANGLES (DEGREES) : 1.756
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 27.98
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1F0R COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-MAY-00.
REMARK 100 THE DEPOSITION ID IS D_1000011103.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-JUL-98
REMARK 200 TEMPERATURE (KELVIN) : 95
REMARK 200 PH : 5.7
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 : MACSCIENCE
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAC SCIENCE DIP-2000
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA, CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25914
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 26.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.04600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.30
REMARK 200 R MERGE FOR SHELL (I) : 0.26700
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 (%): 32.27
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.82
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 18-22%PEG 600, 50MM MES-NAOH, PH 5.7,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 292K
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 28.25500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 38.95600
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.11400
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 38.95600
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 28.25500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 36.11400
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 300 REMARK: THE BIOLOGICAL ASEMBLY IS CONSTRUCTED FROM CHAIN A AND B
REMARK 300 LINKED THROUGH A DISLUFIDE BRIDGE
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: 2680 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13530 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 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 ARG A 245
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 SER A 252
REMARK 465 HIS A 253
REMARK 465 ALA A 254
REMARK 465 PRO A 255
REMARK 465 GLU A 256
REMARK 465 VAL A 257
REMARK 465 ILE A 258
REMARK 465 THR A 259
REMARK 465 SER A 260
REMARK 465 SER A 261
REMARK 465 PRO A 262
REMARK 465 LEU A 263
REMARK 465 LYS A 264
REMARK 465 GLU B -82
REMARK 465 GLU B -81
REMARK 465 MET B -80
REMARK 465 LYS B -79
REMARK 465 LYS B -78
REMARK 465 GLY B -77
REMARK 465 HIS B -76
REMARK 465 LEU B -75
REMARK 465 GLU B -74
REMARK 465 ARG B -73
REMARK 465 GLU B -72
REMARK 465 CYS B -71
REMARK 465 MET B -70
REMARK 465 GLU B -69
REMARK 465 GLU B -68
REMARK 465 THR B -67
REMARK 465 CYS B -66
REMARK 465 SER B -65
REMARK 465 TYR B -64
REMARK 465 GLU B -63
REMARK 465 GLU B -62
REMARK 465 ALA B -61
REMARK 465 ARG B -60
REMARK 465 GLU B -59
REMARK 465 VAL B -58
REMARK 465 PHE B -57
REMARK 465 GLU B -56
REMARK 465 ASP B -55
REMARK 465 SER B -54
REMARK 465 ASP B -53
REMARK 465 LYS B -52
REMARK 465 THR B -51
REMARK 465 ASN B -50
REMARK 465 GLU B -49
REMARK 465 PHE B -48
REMARK 465 TRP B -47
REMARK 465 ASN B -46
REMARK 465 LYS B -45
REMARK 465 TYR B -44
REMARK 465 LYS B -43
REMARK 465 ASP B -42
REMARK 465 GLY B -41
REMARK 465 ASP B -40
REMARK 465 GLN B -39
REMARK 465 CYS B -38
REMARK 465 GLU B -37
REMARK 465 THR B -36
REMARK 465 SER B -35
REMARK 465 PRO B -34
REMARK 465 CYS B -33
REMARK 465 GLN B -32
REMARK 465 ASN B -31
REMARK 465 GLN B -30
REMARK 465 GLY B -29
REMARK 465 LYS B -28
REMARK 465 CYS B -27
REMARK 465 LYS B -26
REMARK 465 ASP B -25
REMARK 465 GLY B -24
REMARK 465 LEU B -23
REMARK 465 GLY B -22
REMARK 465 GLU B -21
REMARK 465 TYR B -20
REMARK 465 THR B -19
REMARK 465 CYS B -18
REMARK 465 THR B -17
REMARK 465 CYS B -16
REMARK 465 LEU B -15
REMARK 465 GLU B -14
REMARK 465 GLY B -13
REMARK 465 PHE B -12
REMARK 465 GLU B -11
REMARK 465 GLY B -10
REMARK 465 LYS B -9
REMARK 465 ASN B -8
REMARK 465 CYS B -7
REMARK 465 GLU B -6
REMARK 465 LEU B -5
REMARK 465 PHE B -4
REMARK 465 THR B -3
REMARK 465 ARG B -2
REMARK 465 LYS B -1
REMARK 465 ARG B 51
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 39 CG CD OE1 OE2
REMARK 480 LYS A 62 CB CG CD CE NZ
REMARK 480 ARG A 63 CG CD NE CZ NH1 NH2
REMARK 480 GLU A 76 CG CD OE1 OE2
REMARK 480 GLU A 77 CG CD OE1 OE2
REMARK 480 LYS A 96 CD CE NZ
REMARK 480 GLU A 97 CG CD OE1 OE2
REMARK 480 LYS A 134 CD CE NZ
REMARK 480 ARG A 150 CB CG CD NE CZ NH1 NH2
REMARK 480 LYS A 236 CD CE NZ
REMARK 480 LYS A 243 CG CD CE NZ
REMARK 480 THR A 244 CB OG1 CG2
REMARK 480 GLU B 15 CG CD OE1 OE2
REMARK 480 ARG B 25 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 O HOH A 428 O HOH A 527 0.33
REMARK 500 O LYS A 224 O HOH A 410 2.14
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 ARG A 115 -172.50 -170.94
REMARK 500 ASP A 189 164.44 176.82
REMARK 500 ALA A 221 19.42 58.40
REMARK 500 GLN B 10 -110.20 -128.15
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 301 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 70 OD1
REMARK 620 2 ASN A 72 O 79.1
REMARK 620 3 GLN A 75 O 157.3 80.0
REMARK 620 4 GLU A 80 OE1 108.4 157.9 88.3
REMARK 620 5 HOH A 451 O 76.5 93.0 96.1 69.5
REMARK 620 6 HOH A 496 O 87.7 106.1 106.5 95.1 152.4
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 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 815 A 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1EZQ RELATED DB: PDB
REMARK 900 HUMAN COAGULATION FACTOR XA WITH INHIBITOR RPR128515
REMARK 900 RELATED ID: 1F0S RELATED DB: PDB
REMARK 900 HUMAN COAGULATION FACTOR XA WITH INHIBITOR RPR208707
REMARK 900 RELATED ID: 1F0T RELATED DB: PDB
REMARK 900 BOVINE PANCREATIC TRYPSIN WITH INHIBITOR RPR131247
REMARK 900 RELATED ID: 1F0U RELATED DB: PDB
REMARK 900 BOVINE PANCREATIC TRYPSIN WITH INHIBITOR RPR128515
DBREF 1F0R A 16 264 UNP P00742 FA10_HUMAN 235 488
DBREF 1F0R B -82 51 UNP P00742 FA10_HUMAN 46 179
SEQRES 1 A 254 ILE VAL GLY GLY GLN GLU CYS LYS ASP GLY GLU CYS PRO
SEQRES 2 A 254 TRP GLN ALA LEU LEU ILE ASN GLU GLU ASN GLU GLY PHE
SEQRES 3 A 254 CYS GLY GLY THR ILE LEU SER GLU PHE TYR ILE LEU THR
SEQRES 4 A 254 ALA ALA HIS CYS LEU TYR GLN ALA LYS ARG PHE LYS VAL
SEQRES 5 A 254 ARG VAL GLY ASP ARG ASN THR GLU GLN GLU GLU GLY GLY
SEQRES 6 A 254 GLU ALA VAL HIS GLU VAL GLU VAL VAL ILE LYS HIS ASN
SEQRES 7 A 254 ARG PHE THR LYS GLU THR TYR ASP PHE ASP ILE ALA VAL
SEQRES 8 A 254 LEU ARG LEU LYS THR PRO ILE THR PHE ARG MET ASN VAL
SEQRES 9 A 254 ALA PRO ALA CYS LEU PRO GLU ARG ASP TRP ALA GLU SER
SEQRES 10 A 254 THR LEU MET THR GLN LYS THR GLY ILE VAL SER GLY PHE
SEQRES 11 A 254 GLY ARG THR HIS GLU LYS GLY ARG GLN SER THR ARG LEU
SEQRES 12 A 254 LYS MET LEU GLU VAL PRO TYR VAL ASP ARG ASN SER CYS
SEQRES 13 A 254 LYS LEU SER SER SER PHE ILE ILE THR GLN ASN MET PHE
SEQRES 14 A 254 CYS ALA GLY TYR ASP THR LYS GLN GLU ASP ALA CYS GLN
SEQRES 15 A 254 GLY ASP SER GLY GLY PRO HIS VAL THR ARG PHE LYS ASP
SEQRES 16 A 254 THR TYR PHE VAL THR GLY ILE VAL SER TRP GLY GLU GLY
SEQRES 17 A 254 CYS ALA ARG LYS GLY LYS TYR GLY ILE TYR THR LYS VAL
SEQRES 18 A 254 THR ALA PHE LEU LYS TRP ILE ASP ARG SER MET LYS THR
SEQRES 19 A 254 ARG GLY LEU PRO LYS ALA LYS SER HIS ALA PRO GLU VAL
SEQRES 20 A 254 ILE THR SER SER PRO LEU LYS
SEQRES 1 B 134 GLU GLU MET LYS LYS GLY HIS LEU GLU ARG GLU CYS MET
SEQRES 2 B 134 GLU GLU THR CYS SER TYR GLU GLU ALA ARG GLU VAL PHE
SEQRES 3 B 134 GLU ASP SER ASP LYS THR ASN GLU PHE TRP ASN LYS TYR
SEQRES 4 B 134 LYS ASP GLY ASP GLN CYS GLU THR SER PRO CYS GLN ASN
SEQRES 5 B 134 GLN GLY LYS CYS LYS ASP GLY LEU GLY GLU TYR THR CYS
SEQRES 6 B 134 THR CYS LEU GLU GLY PHE GLU GLY LYS ASN CYS GLU LEU
SEQRES 7 B 134 PHE THR ARG LYS LEU CYS SER LEU ASP ASN GLY ASP CYS
SEQRES 8 B 134 ASP GLN PHE CYS HIS GLU GLU GLN ASN SER VAL VAL CYS
SEQRES 9 B 134 SER CYS ALA ARG GLY TYR THR LEU ALA ASP ASN GLY LYS
SEQRES 10 B 134 ALA CYS ILE PRO THR GLY PRO TYR PRO CYS GLY LYS GLN
SEQRES 11 B 134 THR LEU GLU ARG
HET CA A 301 1
HET 815 A 401 31
HETNAM CA CALCIUM ION
HETNAM 815 THIENO[3,2-B]PYRIDINE-2-SULFONIC ACID [1-(1-AMINO-
HETNAM 2 815 ISOQUINOLIN-7-YLMETHYL)-2-OXO-PYRROLDIN-3-YL]-AMIDE
HETSYN 815 RPR208815
FORMUL 3 CA CA 2+
FORMUL 4 815 C21 H19 N5 O3 S2
FORMUL 5 HOH *170(H2 O)
HELIX 1 1 ALA A 55 GLN A 61 5 7
HELIX 2 3 ASP A 164 SER A 172 1 9
HELIX 3 4 PHE A 234 THR A 244 1 11
HELIX 4 5 LEU B 3 CYS B 8 5 6
SHEET 1 A 7 GLN A 20 GLU A 21 0
SHEET 2 A 7 LYS A 156 PRO A 161 -1 N MET A 157 O GLN A 20
SHEET 3 A 7 THR A 135 GLY A 140 -1 O GLY A 136 N VAL A 160
SHEET 4 A 7 PRO A 198 PHE A 203 -1 O PRO A 198 N SER A 139
SHEET 5 A 7 THR A 206 TRP A 215 -1 O THR A 206 N PHE A 203
SHEET 6 A 7 GLY A 226 LYS A 230 -1 N ILE A 227 O TRP A 215
SHEET 7 A 7 MET A 180 ALA A 183 -1 O PHE A 181 N TYR A 228
SHEET 1 B 7 GLN A 30 ASN A 35 0
SHEET 2 B 7 GLY A 40 ILE A 46 -1 N PHE A 41 O LEU A 33
SHEET 3 B 7 TYR A 51 THR A 54 -1 N LEU A 53 O 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 GLU A 86 O ARG A 107
SHEET 6 B 7 PHE A 64 VAL A 68 -1 O PHE A 64 N VAL A 85
SHEET 7 B 7 GLN A 30 ASN A 35 -1 O LEU A 32 N ARG A 67
SHEET 1 C 2 PHE B 11 GLU B 15 0
SHEET 2 C 2 SER B 18 SER B 22 -1 N SER B 18 O GLU B 15
SHEET 1 D 2 TYR B 27 LEU B 29 0
SHEET 2 D 2 CYS B 36 PRO B 38 -1 N ILE B 37 O THR B 28
SSBOND 1 CYS A 22 CYS A 27 1555 1555 2.03
SSBOND 2 CYS A 42 CYS A 58 1555 1555 2.02
SSBOND 3 CYS A 122 CYS B 44 1555 1555 2.03
SSBOND 4 CYS A 168 CYS A 182 1555 1555 2.00
SSBOND 5 CYS A 191 CYS A 220 1555 1555 2.04
SSBOND 6 CYS B 1 CYS B 12 1555 1555 2.06
SSBOND 7 CYS B 8 CYS B 21 1555 1555 2.03
SSBOND 8 CYS B 23 CYS B 36 1555 1555 2.03
LINK OD1 ASP A 70 CA CA A 301 1555 1555 2.55
LINK O ASN A 72 CA CA A 301 1555 1555 2.54
LINK O GLN A 75 CA CA A 301 1555 1555 2.57
LINK OE1 GLU A 80 CA CA A 301 1555 1555 2.50
LINK CA CA A 301 O HOH A 451 1555 1555 2.78
LINK CA CA A 301 O HOH A 496 1555 1555 2.70
SITE 1 AC1 6 ASP A 70 ASN A 72 GLN A 75 GLU A 80
SITE 2 AC1 6 HOH A 451 HOH A 496
SITE 1 AC2 12 GLU A 97 TYR A 99 PHE A 174 ASP A 189
SITE 2 AC2 12 ALA A 190 SER A 195 VAL A 213 TRP A 215
SITE 3 AC2 12 GLY A 216 GLU A 217 GLY A 219 HOH A 530
CRYST1 56.510 72.228 77.912 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 0.017696 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013845 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012835 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
