HEADER HYDROLASE/HYDROLASE INHIBITOR 05-FEB-98 1TBZ
TITLE HUMAN THROMBIN WITH ACTIVE SITE N-METHYL-D PHENYLALANYL-N-[5-
TITLE 2 (AMINOIMINOMETHYL)AMINO]-1-{{BENZOTHIAZOLYL)CARBONYL] BUTYL]-L-
TITLE 3 PROLINAMIDE TRIFLUROACETATE AND EXOSITE-HIRUGEN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA-THROMBIN;
COMPND 3 CHAIN: L;
COMPND 4 EC: 3.4.21.5;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: ALPHA-THROMBIN;
COMPND 7 CHAIN: H;
COMPND 8 EC: 3.4.21.5;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: HIRUGEN;
COMPND 11 CHAIN: I
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 TISSUE: PLASMA;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 8 ORGANISM_COMMON: HUMAN;
SOURCE 9 ORGANISM_TAXID: 9606;
SOURCE 10 TISSUE: PLASMA;
SOURCE 11 MOL_ID: 3;
SOURCE 12 ORGANISM_SCIENTIFIC: HIRUDO MEDICINALIS;
SOURCE 13 ORGANISM_COMMON: MEDICINAL LEECH;
SOURCE 14 ORGANISM_TAXID: 6421
KEYWDS COMPLEX (SERINE PROTEASE-INHIBITOR), HYDROLASE-HYDROLASE INHIBITOR
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.H.MATTHEWS,R.KRISHNAN,M.J.COSTANZO,B.E.MARYANOFF,A.TULINSKY
REVDAT 4 09-AUG-23 1TBZ 1 REMARK LINK
REVDAT 3 13-JUL-11 1TBZ 1 VERSN
REVDAT 2 24-FEB-09 1TBZ 1 VERSN
REVDAT 1 27-MAY-98 1TBZ 0
JRNL AUTH J.H.MATTHEWS,R.KRISHNAN,M.J.COSTANZO,B.E.MARYANOFF,
JRNL AUTH 2 A.TULINSKY
JRNL TITL CRYSTAL STRUCTURES OF THROMBIN WITH THIAZOLE-CONTAINING
JRNL TITL 2 INHIBITORS: PROBES OF THE S1' BINDING SITE.
JRNL REF BIOPHYS.J. V. 71 2830 1996
JRNL REFN ISSN 0006-3495
JRNL PMID 8913620
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.VIJAYALAKSHMI,K.P.PADMANABHAN,K.G.MANN,A.TULINSKY
REMARK 1 TITL THE ISOMORPHOUS STRUCTURES OF PRETHROMBIN2, HIRUGEN-, AND
REMARK 1 TITL 2 PPACK-THROMBIN: CHANGES ACCOMPANYING ACTIVATION AND EXOSITE
REMARK 1 TITL 3 BINDING TO THROMBIN
REMARK 1 REF PROTEIN SCI. V. 3 2254 1994
REMARK 1 REFN ISSN 0961-8368
REMARK 1 REFERENCE 2
REMARK 1 AUTH A.TULINSKY,X.QIU
REMARK 1 TITL ACTIVE SITE AND EXOSITE BINDING OF ALPHA-THROMBIN
REMARK 1 REF BLOOD COAGULATION V. 4 305 1993
REMARK 1 REF 2 FIBRINOLYSIS
REMARK 1 REFN ISSN 0957-5235
REMARK 1 REFERENCE 3
REMARK 1 AUTH X.QIU,K.P.PADMANABHAN,V.E.CARPEROS,A.TULINSKY,T.KLINE,
REMARK 1 AUTH 2 J.M.MARAGANORE,J.W.FENTON II
REMARK 1 TITL STRUCTURE OF THE HIRULOG 3-THROMBIN COMPLEX AND NATURE OF
REMARK 1 TITL 2 THE S' SUBSITES OF SUBSTRATES AND INHIBITORS
REMARK 1 REF BIOCHEMISTRY V. 31 11689 1992
REMARK 1 REFN ISSN 0006-2960
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 7.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 75.0
REMARK 3 NUMBER OF REFLECTIONS : 13574
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.158
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
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 : 2322
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 40
REMARK 3 SOLVENT ATOMS : 123
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.00
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) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
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) : 1.100 ; 1.000
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.900 ; 1.500
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.600 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.800 ; 2.500
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1TBZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000176605.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : APR-93
REMARK 200 TEMPERATURE (KELVIN) : 298
REMARK 200 PH : 7.3
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 RUH2R
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE(002)
REMARK 200 OPTICS : COLLIMATOR
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : SIEMENS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XENGEN
REMARK 200 DATA SCALING SOFTWARE : XENGEN
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15300
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 75.0
REMARK 200 DATA REDUNDANCY : 2.500
REMARK 200 R MERGE (I) : 0.05400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.40
REMARK 200 COMPLETENESS FOR SHELL (%) : 50.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: PDB ENTRY 1FPC
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M PHOSPHATE BUFFER AT PH 7.3, 27
REMARK 280 -28% PEG 8000. HANGING DROPS AND MACROSEEDING ., VAPOR DIFFUSION
REMARK 280 - HANGING DROP - MACROSEEDING
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 35.39500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.26500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 35.39500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 36.26500
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3470 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12290 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, H, I
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 400
REMARK 400 COMPOUND
REMARK 400 THROMBIN IS CLEAVED BETWEEN RESIDUES 15 AND 16. CHAIN IDENTIFIER *L*
REMARK 400 IS USED FOR RESIDUES 1H - 15 AND CHAIN IDENTIFIER *H* IS USED FOR
REMARK 400 RESIDUES 16 - 247. CHAIN IDENTIFIER *I* IS USED FOR HIRUGEN. THE
REMARK 400 INHIBITOR 00Q IS COVALENTLY CONNECTED TO SER 195 OF THE ENZYME TO
REMARK 400 FORM A HEMIKETAL.
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 THR L -7
REMARK 465 PHE L -6
REMARK 465 GLY L -5
REMARK 465 SER L -4
REMARK 465 GLY L -3
REMARK 465 GLU L -2
REMARK 465 ALA L -1
REMARK 465 ASP L 0
REMARK 465 ASP L 15
REMARK 465 GLY L 16
REMARK 465 ARG L 17
REMARK 465 THR H 146A
REMARK 465 TRP H 146B
REMARK 465 THR H 146C
REMARK 465 ALA H 146D
REMARK 465 ASN H 146E
REMARK 465 VAL H 146F
REMARK 465 GLY H 146G
REMARK 465 LYS H 146H
REMARK 465 ASN I 53
REMARK 465 GLY I 54
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 LYS L 14A CG CD CE NZ
REMARK 470 GLU I 61 CB CG CD OE1 OE2
REMARK 470 GLU I 62 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 NH1 ARG H 50 O LEU H 108 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 NH1 ARG H 75 OE1 GLU I 57 2555 1.76
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 ARG L 4 NE - CZ - NH1 ANGL. DEV. = 7.8 DEGREES
REMARK 500 GLU L 13 CB - CA - C ANGL. DEV. = -12.6 DEGREES
REMARK 500 ASP H 21 CB - CG - OD1 ANGL. DEV. = 6.8 DEGREES
REMARK 500 ASP H 21 CB - CG - OD2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 SER H 27 N - CA - CB ANGL. DEV. = -11.2 DEGREES
REMARK 500 ARG H 35 NE - CZ - NH2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 ASP H 49 CB - CG - OD1 ANGL. DEV. = -5.7 DEGREES
REMARK 500 TYR H 60A CB - CG - CD2 ANGL. DEV. = 4.5 DEGREES
REMARK 500 TYR H 60A CB - CG - CD1 ANGL. DEV. = -6.9 DEGREES
REMARK 500 ARG H 67 CD - NE - CZ ANGL. DEV. = 10.0 DEGREES
REMARK 500 ARG H 67 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 ARG H 73 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG H 73 NE - CZ - NH2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 THR H 74 CA - CB - CG2 ANGL. DEV. = 8.8 DEGREES
REMARK 500 ARG H 75 NE - CZ - NH1 ANGL. DEV. = -4.1 DEGREES
REMARK 500 ARG H 75 NE - CZ - NH2 ANGL. DEV. = 3.2 DEGREES
REMARK 500 TYR H 76 CB - CG - CD1 ANGL. DEV. = -5.5 DEGREES
REMARK 500 GLU H 77 CB - CG - CD ANGL. DEV. = 17.6 DEGREES
REMARK 500 ARG H 77A CD - NE - CZ ANGL. DEV. = -11.1 DEGREES
REMARK 500 ARG H 77A NE - CZ - NH1 ANGL. DEV. = -5.8 DEGREES
REMARK 500 ARG H 77A NE - CZ - NH2 ANGL. DEV. = 11.2 DEGREES
REMARK 500 ARG H 77A CA - C - N ANGL. DEV. = 17.3 DEGREES
REMARK 500 ASN H 78 C - N - CA ANGL. DEV. = -15.9 DEGREES
REMARK 500 GLU H 80 CG - CD - OE1 ANGL. DEV. = -12.8 DEGREES
REMARK 500 TYR H 94 CB - CG - CD2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 TYR H 94 CB - CG - CD1 ANGL. DEV. = 4.9 DEGREES
REMARK 500 ARG H 97 NH1 - CZ - NH2 ANGL. DEV. = 7.0 DEGREES
REMARK 500 ARG H 97 NE - CZ - NH2 ANGL. DEV. = -7.1 DEGREES
REMARK 500 GLU H 97A CA - CB - CG ANGL. DEV. = 16.0 DEGREES
REMARK 500 ARG H 101 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG H 101 NE - CZ - NH2 ANGL. DEV. = -7.5 DEGREES
REMARK 500 ASP H 102 CB - CG - OD2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 ASP H 116 CB - CG - OD1 ANGL. DEV. = 6.8 DEGREES
REMARK 500 TYR H 117 CB - CG - CD2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 ARG H 126 CD - NE - CZ ANGL. DEV. = -9.0 DEGREES
REMARK 500 VAL H 154 N - CA - CB ANGL. DEV. = -13.6 DEGREES
REMARK 500 VAL H 154 CA - CB - CG1 ANGL. DEV. = 9.1 DEGREES
REMARK 500 ARG H 173 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 ILE H 176 CA - CB - CG2 ANGL. DEV. = 13.6 DEGREES
REMARK 500 TYR H 184A CB - CG - CD1 ANGL. DEV. = -4.9 DEGREES
REMARK 500 LYS H 186D N - CA - CB ANGL. DEV. = 10.9 DEGREES
REMARK 500 ASP H 189 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 GLU H 192 OE1 - CD - OE2 ANGL. DEV. = -12.2 DEGREES
REMARK 500 GLU H 192 CG - CD - OE1 ANGL. DEV. = 12.5 DEGREES
REMARK 500 ARG H 206 CD - NE - CZ ANGL. DEV. = 8.5 DEGREES
REMARK 500 ARG H 206 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG H 206 NE - CZ - NH2 ANGL. DEV. = -4.9 DEGREES
REMARK 500 ARG H 221A NE - CZ - NH2 ANGL. DEV. = 5.2 DEGREES
REMARK 500 ASP H 243 CB - CG - OD1 ANGL. DEV. = 6.3 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 PHE L 7 -83.64 -130.72
REMARK 500 TYR H 60A 77.14 -153.61
REMARK 500 ASN H 60G 74.25 -155.48
REMARK 500 HIS H 71 -52.55 -131.01
REMARK 500 ILE H 79 -60.06 -100.60
REMARK 500 GLU H 97A -64.64 -128.64
REMARK 500 LEU H 130 71.82 -67.71
REMARK 500 GLU H 186B -32.19 -24.77
REMARK 500 SER H 195 139.45 -37.89
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG L 14D 0.11 SIDE CHAIN
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 NA H 1 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG H 221A O
REMARK 620 2 LYS H 224 O 114.1
REMARK 620 3 HOH H 731 O 89.0 130.1
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA H 2 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LYS H 169 O
REMARK 620 2 THR H 172 O 80.0
REMARK 620 3 PHE H 204A O 92.3 85.2
REMARK 620 4 HOH H 627 O 64.3 79.0 153.6
REMARK 620 N 1 2 3
REMARK 630
REMARK 630 MOLECULE TYPE: PEPTIDE-LIKE THROMBIN INHIBITOR
REMARK 630 MOLECULE NAME: D-PHENYLALANYL-N-{(1S)-1-[(S)-1,3-BENZOTHIAZOL-2-
REMARK 630 YL(HYDROXY)METHYL]-4-CARBAMIMIDAMIDOBUTYL}-L-PROLINAMIDE
REMARK 630 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 630 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 630
REMARK 630 M RES C SSSEQI
REMARK 630 00Q H 343
REMARK 630 SOURCE: NULL
REMARK 630 TAXONOMY: NULL
REMARK 630 SUBCOMP: DPN PRO THZ
REMARK 630 DETAILS: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CAT
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE.
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 00Q H 343
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA H 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA H 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN I OF HIRUGEN
DBREF 1TBZ L -7 17 UNP P00734 THRB_HUMAN 328 363
DBREF 1TBZ H 16 247 UNP P00734 THRB_HUMAN 364 622
DBREF 1TBZ I 53 64 UNP P09945 ITH3_HIRME 60 71
SEQRES 1 L 36 THR PHE GLY SER GLY GLU ALA ASP CYS GLY LEU ARG PRO
SEQRES 2 L 36 LEU PHE GLU LYS LYS SER LEU GLU ASP LYS THR GLU ARG
SEQRES 3 L 36 GLU LEU LEU GLU SER TYR ILE ASP GLY ARG
SEQRES 1 H 259 ILE VAL GLU GLY SER ASP ALA GLU ILE GLY MET SER PRO
SEQRES 2 H 259 TRP GLN VAL MET LEU PHE ARG LYS SER PRO GLN GLU LEU
SEQRES 3 H 259 LEU CYS GLY ALA SER LEU ILE SER ASP ARG TRP VAL LEU
SEQRES 4 H 259 THR ALA ALA HIS CYS LEU LEU TYR PRO PRO TRP ASP LYS
SEQRES 5 H 259 ASN PHE THR GLU ASN ASP LEU LEU VAL ARG ILE GLY LYS
SEQRES 6 H 259 HIS SER ARG THR ARG TYR GLU ARG ASN ILE GLU LYS ILE
SEQRES 7 H 259 SER MET LEU GLU LYS ILE TYR ILE HIS PRO ARG TYR ASN
SEQRES 8 H 259 TRP ARG GLU ASN LEU ASP ARG ASP ILE ALA LEU MET LYS
SEQRES 9 H 259 LEU LYS LYS PRO VAL ALA PHE SER ASP TYR ILE HIS PRO
SEQRES 10 H 259 VAL CYS LEU PRO ASP ARG GLU THR ALA ALA SER LEU LEU
SEQRES 11 H 259 GLN ALA GLY TYR LYS GLY ARG VAL THR GLY TRP GLY ASN
SEQRES 12 H 259 LEU LYS GLU THR TRP THR ALA ASN VAL GLY LYS GLY GLN
SEQRES 13 H 259 PRO SER VAL LEU GLN VAL VAL ASN LEU PRO ILE VAL GLU
SEQRES 14 H 259 ARG PRO VAL CYS LYS ASP SER THR ARG ILE ARG ILE THR
SEQRES 15 H 259 ASP ASN MET PHE CYS ALA GLY TYR LYS PRO ASP GLU GLY
SEQRES 16 H 259 LYS ARG GLY ASP ALA CYS GLU GLY ASP SER GLY GLY PRO
SEQRES 17 H 259 PHE VAL MET LYS SER PRO PHE ASN ASN ARG TRP TYR GLN
SEQRES 18 H 259 MET GLY ILE VAL SER TRP GLY GLU GLY CYS ASP ARG ASP
SEQRES 19 H 259 GLY LYS TYR GLY PHE TYR THR HIS VAL PHE ARG LEU LYS
SEQRES 20 H 259 LYS TRP ILE GLN LYS VAL ILE ASP GLN PHE GLY GLU
SEQRES 1 I 12 ASN GLY ASP PHE GLU GLU ILE PRO GLU GLU TYS LEU
MODRES 1TBZ TYS I 63 TYR O-SULFO-L-TYROSINE
HET TYS I 63 16
HET 00Q H 343 38
HET NA H 1 1
HET NA H 2 1
HETNAM TYS O-SULFO-L-TYROSINE
HETNAM 00Q D-PHENYLALANYL-N-{(1S)-1-[(S)-1,3-BENZOTHIAZOL-2-
HETNAM 2 00Q YL(HYDROXY)METHYL]-4-CARBAMIMIDAMIDOBUTYL}-L-
HETNAM 3 00Q PROLINAMIDE
HETNAM NA SODIUM ION
HETSYN 00Q RWJ-30353
FORMUL 3 TYS C9 H11 N O6 S
FORMUL 4 00Q C27 H35 N7 O3 S
FORMUL 5 NA 2(NA 1+)
FORMUL 7 HOH *123(H2 O)
HELIX 1 H1 ALA H 55 LEU H 60 1 6
HELIX 2 H2 GLU H 164 SER H 171 1 8
HELIX 3 H3 ASP H 125 LEU H 129C 1 8
HELIX 4 H4 VAL H 231 GLN H 244 1 14
SHEET 1 B1 7 PRO H 28 ARG H 35 0
SHEET 2 B1 7 CYS H 42 ASP H 49 -1
SHEET 3 B1 7 ARG H 50 ALA H 56 -1
SHEET 4 B1 7 ARG H 101 LYS H 110 -1
SHEET 5 B1 7 LYS H 81 PRO H 92 -1
SHEET 6 B1 7 ASP H 63 GLY H 69 -1
SHEET 7 B1 7 PRO H 28 ARG H 35 -1
SHEET 1 B2 7 GLY H 133 TRP H 141 0
SHEET 2 B2 7 LEU H 155 ILE H 162 -1
SHEET 3 B2 7 ASN H 179 PRO H 186 -1
SHEET 4 B2 7 GLY H 223 THR H 229 -1
SHEET 5 B2 7 ILE H 212 GLU H 217 -1
SHEET 6 B2 7 GLY H 193 MET H 201 -1
SHEET 7 B2 7 GLY H 133 TRP H 141 -1
SSBOND 1 CYS L 1 CYS H 122 1555 1555 2.03
SSBOND 2 CYS H 42 CYS H 58 1555 1555 2.10
SSBOND 3 CYS H 168 CYS H 182 1555 1555 2.06
SSBOND 4 CYS H 191 CYS H 220 1555 1555 2.04
LINK OG SER H 195 CY 00Q H 343 1555 1555 1.68
LINK C GLU I 62 N TYS I 63 1555 1555 1.34
LINK C TYS I 63 N LEU I 64 1555 1555 1.32
LINK NA NA H 1 O ARG H 221A 1555 1555 2.15
LINK NA NA H 1 O LYS H 224 1555 1555 2.08
LINK NA NA H 1 O HOH H 731 1555 1555 3.02
LINK NA NA H 2 O LYS H 169 1555 1555 2.59
LINK NA NA H 2 O THR H 172 1555 1555 2.28
LINK NA NA H 2 O PHE H 204A 1555 4546 2.56
LINK NA NA H 2 O HOH H 627 1555 1555 2.93
CISPEP 1 SER H 36A PRO H 37 0 -3.47
SITE 1 CAT 3 HIS H 57 ASP H 102 SER H 195
SITE 1 AC1 18 HIS H 57 TYR H 60A TRP H 60D LYS H 60F
SITE 2 AC1 18 GLU H 97A ASP H 189 ALA H 190 CYS H 191
SITE 3 AC1 18 GLU H 192 GLY H 193 ASP H 194 SER H 195
SITE 4 AC1 18 SER H 214 TRP H 215 GLY H 216 GLY H 219
SITE 5 AC1 18 GLY H 226 HOH H 400
SITE 1 AC2 3 ARG H 221A LYS H 224 HOH H 731
SITE 1 AC3 4 LYS H 169 THR H 172 PHE H 204A HOH H 627
SITE 1 AC4 14 PHE H 34 LYS H 36 GLN H 38 ARG H 73
SITE 2 AC4 14 THR H 74 ARG H 75 TYR H 76 LYS H 81
SITE 3 AC4 14 ILE H 82 SER H 153 HOH H 417 HOH H 453
SITE 4 AC4 14 HOH H 521 HOH I 660
CRYST1 70.790 72.530 73.120 90.00 101.00 90.00 C 1 2 1 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.014126 0.000000 0.002746 0.00000
SCALE2 0.000000 0.013787 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013932 0.00000
(ATOM LINES ARE NOT SHOWN.)
END