HEADER HYDROLASE 03-AUG-09 3IIT
TITLE FACTOR XA IN COMPLEX WITH A CIS-1,2-DIAMINOCYCLOHEXANE DERIVATIVE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACTIVATED FACTOR XA HEAVY CHAIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: COAGULATION FACTOR X HEAVY CHAIN, FACTOR X HEAVY CHAIN;
COMPND 5 EC: 3.4.21.6;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: FACTOR X LIGHT CHAIN;
COMPND 8 CHAIN: B;
COMPND 9 FRAGMENT: UNP RESIDUES 125-178;
COMPND 10 SYNONYM: COAGULATION FACTOR X LIGHT CHAIN;
COMPND 11 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, BLOOD
KEYWDS 3 COAGULATION, CLEAVAGE ON PAIR OF BASIC RESIDUES, DISULFIDE BOND,
KEYWDS 4 EGF-LIKE DOMAIN, GAMMA-CARBOXYGLUTAMIC ACID, HYDROXYLATION,
KEYWDS 5 PROTEASE, SECRETED, ZYMOGEN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.SUZUKI
REVDAT 2 01-NOV-23 3IIT 1 REMARK LINK
REVDAT 1 04-AUG-10 3IIT 0
JRNL AUTH K.YOSHIKAWA,S.KOBAYASHI,Y.NAKAMOTO,N.HAGINOYA,S.KOMORIYA,
JRNL AUTH 2 T.YOSHINO,T.NAGATA,A.MOCHIZUKI,K.WATANABE,M.SUZUKI,H.KANNO,
JRNL AUTH 3 T.OHTA
JRNL TITL DESIGN, SYNTHESIS, AND SAR OF CIS-1,2-DIAMINOCYCLOHEXANE
JRNL TITL 2 DERIVATIVES AS POTENT FACTOR XA INHIBITORS. PART II:
JRNL TITL 3 EXPLORATION OF 6-6 FUSED RINGS AS ALTERNATIVE S1 MOIETIES.
JRNL REF BIOORG.MED.CHEM. V. 17 8221 2009
JRNL REFN ISSN 0968-0896
JRNL PMID 19900814
JRNL DOI 10.1016/J.BMC.2009.10.024
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0066
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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.2
REMARK 3 NUMBER OF REFLECTIONS : 26348
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) : 0.203
REMARK 3 R VALUE (WORKING SET) : 0.202
REMARK 3 FREE R VALUE : 0.233
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1375
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) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.86
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1918
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 85.37
REMARK 3 BIN R VALUE (WORKING SET) : 0.3100
REMARK 3 BIN FREE R VALUE SET COUNT : 90
REMARK 3 BIN FREE R VALUE : 0.3400
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2172
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 34
REMARK 3 SOLVENT ATOMS : 192
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.39
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.54000
REMARK 3 B22 (A**2) : -0.83000
REMARK 3 B33 (A**2) : 0.29000
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): 0.141
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.130
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.089
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.904
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.941
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.932
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2260 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3068 ; 1.538 ; 1.961
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 285 ; 6.308 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 94 ;31.192 ;23.936
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 357 ;12.871 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 12 ;21.283 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 335 ; 0.107 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1714 ; 0.007 ; 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): 1417 ; 1.101 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2268 ; 2.003 ; 2.300
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 843 ; 3.189 ; 4.500
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 800 ; 4.555 ; 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 PARAMETERS FOR MASK CACLULATION
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: RIGID BODY REFINEMENT
REMARK 4
REMARK 4 3IIT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-AUG-09.
REMARK 100 THE DEPOSITION ID IS D_1000054464.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JUN-01
REMARK 200 TEMPERATURE (KELVIN) : 100
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 RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.542
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : MONOCHROMATOR
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IIC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : PROCESS
REMARK 200 DATA SCALING SOFTWARE : PROCESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28857
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 79.240
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.5
REMARK 200 DATA REDUNDANCY : 2.660
REMARK 200 R MERGE (I) : 0.04840
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) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86
REMARK 200 COMPLETENESS FOR SHELL (%) : 78.3
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.26600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.260
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: REFMAC 5.5.0066
REMARK 200 STARTING MODEL: 1FAX
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.31
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.58
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 5.00, VAPOR DIFFUSION, TEMPERATURE
REMARK 280 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 28.02750
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 39.61900
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.08950
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 39.61900
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 28.02750
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 36.08950
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: 1860 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12690 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 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 GLN A 75 OE1 NE2
REMARK 470 GLU A 76 CD OE1 OE2
REMARK 470 GLU A 77 CG CD OE1 OE2
REMARK 470 ASN A 92 OD1 ND2
REMARK 470 ARG A 93 NE CZ NH1 NH2
REMARK 470 LYS A 96 CD CE NZ
REMARK 470 GLU A 97 CG CD OE1 OE2
REMARK 470 ARG A 115 NE CZ NH1 NH2
REMARK 470 LYS A 134 CD CE NZ
REMARK 470 LYS A 148 CD CE NZ
REMARK 470 ARG A 150 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 187 OE1 NE2
REMARK 470 LYS A 223 CG CD CE NZ
REMARK 470 LYS A 236 CD CE NZ
REMARK 470 ARG B 86 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 87 CG CD CE NZ
REMARK 470 GLN B 104 CG CD OE1 NE2
REMARK 470 GLU B 138 CG CD OE1 OE2
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 OH TYR A 60 NZ LYS A 90 2.06
REMARK 500 O HOH A 376 O HOH B 160 2.09
REMARK 500 OH TYR A 185 O HOH A 368 2.16
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 SER A 48 -177.31 -170.95
REMARK 500 ARG A 115 -176.27 -174.86
REMARK 500 ASP A 164 132.36 -37.57
REMARK 500 ASP A 205 14.02 57.50
REMARK 500 SER A 214 -65.74 -121.08
REMARK 500 LEU B 88 -128.53 52.75
REMARK 500 GLN B 98 -110.58 -130.94
REMARK 500 GLN B 104 -132.62 41.05
REMARK 500 ASN B 105 42.12 -108.06
REMARK 500 LYS B 122 -50.46 -129.91
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 D14 A 700
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 HOH A 15 O
REMARK 620 2 ASP A 70 OD1 81.5
REMARK 620 3 ASN A 72 O 90.6 88.7
REMARK 620 4 GLN A 75 O 105.0 170.4 84.2
REMARK 620 5 GLU A 80 OE2 84.7 106.7 163.0 81.3
REMARK 620 6 HOH A 321 O 156.7 75.2 88.9 98.2 101.9
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 82.2
REMARK 620 3 ARG A 222 O 168.0 86.9
REMARK 620 4 LYS A 224 O 89.3 120.3 92.0
REMARK 620 5 HOH A 267 O 93.1 174.0 98.1 63.1
REMARK 620 6 HOH A 283 O 94.2 84.3 89.5 155.4 92.3
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 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 D14 A 700
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2EI6 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH STRUCTURALLY RELATED INHIBITOR
REMARK 900 RELATED ID: 2EI7 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH STRUCTURALLY RELATED INHIBITOR
REMARK 900 RELATED ID: 2EI8 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH STRUCTURALLY RELATED INHIBITOR
REMARK 900 RELATED ID: 1V3X RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH STRUCTURALLY RELATED INHIBITOR
REMARK 900 RELATED ID: 1WU1 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH STRUCTURALLY RELATED INHIBITOR
REMARK 900 RELATED ID: 2D1J RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH STRUCTURALLY RELATED INHIBITOR
DBREF 3IIT A 16 243 UNP P00742 FA10_HUMAN 235 467
DBREF 3IIT B 85 138 UNP P00742 FA10_HUMAN 125 178
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 54 THR ARG LYS LEU CYS SER LEU ASP ASN GLY ASP CYS ASP
SEQRES 2 B 54 GLN PHE CYS HIS GLU GLU GLN ASN SER VAL VAL CYS SER
SEQRES 3 B 54 CYS ALA ARG GLY TYR THR LEU ALA ASP ASN GLY LYS ALA
SEQRES 4 B 54 CYS ILE PRO THR GLY PRO TYR PRO CYS GLY LYS GLN THR
SEQRES 5 B 54 LEU GLU
HET CA A 261 1
HET CA A 262 1
HET D14 A 700 32
HETNAM CA CALCIUM ION
HETNAM D14 7-CHLORO-N-[(1S,2R,4S)-4-(DIMETHYLCARBAMOYL)-2-{[(5-
HETNAM 2 D14 METHYL-5,6-DIHYDRO-4H-PYRROLO[3,4-D][1,3]THIAZOL-2-
HETNAM 3 D14 YL)CARBONYL]AMINO}CYCLOHEXYL]ISOQUINOLINE-3-
HETNAM 4 D14 CARBOXAMIDE
FORMUL 3 CA 2(CA 2+)
FORMUL 5 D14 C26 H29 CL N6 O3 S
FORMUL 6 HOH *192(H2 O)
HELIX 1 1 ALA A 55 ALA A 61A 5 8
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 TRP A 215 O ILE A 227
SHEET 6 A 8 PRO A 198 PHE A 203 -1 N HIS A 199 O THR A 210
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 ILE A 34 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 GLU A 86 O ARG A 107
SHEET 6 B 7 LYS A 65 VAL A 68 -1 N VAL A 66 O HIS A 83
SHEET 7 B 7 GLN A 30 ILE A 34 -1 N LEU A 32 O ARG A 67
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 2.03
SSBOND 2 CYS A 42 CYS A 58 1555 1555 2.02
SSBOND 3 CYS A 122 CYS B 132 1555 1555 2.03
SSBOND 4 CYS A 168 CYS A 182 1555 1555 1.93
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 1.99
SSBOND 8 CYS B 111 CYS B 124 1555 1555 2.03
LINK O HOH A 15 CA CA A 261 1555 1555 2.49
LINK OD1 ASP A 70 CA CA A 261 1555 1555 2.22
LINK O ASN A 72 CA CA A 261 1555 1555 2.46
LINK O GLN A 75 CA CA A 261 1555 1555 2.25
LINK OE2 GLU A 80 CA CA A 261 1555 1555 2.39
LINK O TYR A 185 CA CA A 262 1555 1555 2.22
LINK O ASP A 185A CA CA A 262 1555 1555 2.56
LINK O ARG A 222 CA CA A 262 1555 1555 2.35
LINK O LYS A 224 CA CA A 262 1555 1555 2.31
LINK CA CA A 261 O HOH A 321 1555 1555 2.57
LINK CA CA A 262 O HOH A 267 1555 1555 2.97
LINK CA CA A 262 O HOH A 283 1555 1555 2.37
SITE 1 AC1 6 HOH A 15 ASP A 70 ASN A 72 GLN A 75
SITE 2 AC1 6 GLU A 80 HOH A 321
SITE 1 AC2 6 TYR A 185 ASP A 185A ARG A 222 LYS A 224
SITE 2 AC2 6 HOH A 267 HOH A 283
SITE 1 AC3 20 THR A 98 PHE A 174 ASP A 189 ALA A 190
SITE 2 AC3 20 GLN A 192 SER A 195 VAL A 213 TRP A 215
SITE 3 AC3 20 GLY A 216 GLU A 217 GLY A 218 CYS A 220
SITE 4 AC3 20 GLY A 226 ILE A 227 TYR A 228 HOH A 287
SITE 5 AC3 20 HOH A 306 HOH A 370 HOH A 372 HOH A 379
CRYST1 56.055 72.179 79.238 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 0.017840 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013854 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012620 0.00000
(ATOM LINES ARE NOT SHOWN.)
END