HEADER HYDROLASE/HYDROLASE INHIBITOR 19-AUG-92 1DWB
TITLE CRYSTALLOGRAPHIC ANALYSIS AT 3.0-ANGSTROMS RESOLUTION OF THE BINDING
TITLE 2 TO HUMAN THROMBIN OF FOUR ACTIVE SITE-DIRECTED INHIBITORS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA-THROMBIN (SMALL SUBUNIT);
COMPND 3 CHAIN: L;
COMPND 4 EC: 3.4.21.5;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: ALPHA-THROMBIN (LARGE SUBUNIT);
COMPND 8 CHAIN: H;
COMPND 9 EC: 3.4.21.5;
COMPND 10 ENGINEERED: YES;
COMPND 11 MOL_ID: 3;
COMPND 12 MOLECULE: HIRUDIN IIIA;
COMPND 13 CHAIN: I;
COMPND 14 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 ORGAN: PLASMA;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 8 ORGANISM_COMMON: HUMAN;
SOURCE 9 ORGANISM_TAXID: 9606;
SOURCE 10 ORGAN: PLASMA;
SOURCE 11 MOL_ID: 3;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 ORGANISM_SCIENTIFIC: HIRUDO MEDICINALIS;
SOURCE 14 ORGANISM_COMMON: MEDICINAL LEECH;
SOURCE 15 ORGANISM_TAXID: 6421
KEYWDS SERINE PROTEINASE, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR D.W.BANNER,P.HADVARY
REVDAT 4 13-JUL-11 1DWB 1 VERSN
REVDAT 3 24-FEB-09 1DWB 1 VERSN
REVDAT 2 01-APR-03 1DWB 1 JRNL
REVDAT 1 31-JAN-94 1DWB 0
JRNL AUTH D.W.BANNER,P.HADVARY
JRNL TITL CRYSTALLOGRAPHIC ANALYSIS AT 3.0-A RESOLUTION OF THE BINDING
JRNL TITL 2 TO HUMAN THROMBIN OF FOUR ACTIVE SITE-DIRECTED INHIBITORS.
JRNL REF J.BIOL.CHEM. V. 266 20085 1991
JRNL REFN ISSN 0021-9258
JRNL PMID 1939071
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH W.BODE,D.TURK,J.STURZEBECHER
REMARK 1 TITL GEOMETRY OF BINDING OF THE BENZAMIDINE- AND ARGININE-BASED
REMARK 1 TITL 2 INHIBITORS N
REMARK 1 TITL 3 ALPHA-(2-NAPHTHYL-SULPHONYL-GLYCYL)-DL-P-
REMARK 1 TITL 4 AMIDINOPHENYLALANYL-PIPE RIDINE (NAPAP) AND
REMARK 1 TITL 5 (2R,4R)-4-METHYL-1-[N ALPHA-(3-METHYL-1,2,3,4-TETRAHYDRO-8-
REMARK 1 TITL 6 QUINOLINESULPHONYL)-L-ARGINYL]-2-PIPERIDINE CARBOXYLIC ACID
REMARK 1 TITL 7 (MQPA) TO HUMAN ALPHA-THROMBIN. X-RAY CRYSTALLOGRAPHIC
REMARK 1 TITL 8 DETERMINATION OF THE NAPAP-TRYPSIN COMPLEX AND MODELING OF
REMARK 1 TITL 9 NAPAP-THROMBIN AND MQPA-THROMBIN.
REMARK 1 REF EUR.J.BIOCHEM. V. 193 175 1990
REMARK 1 REFN ISSN 0014-2956
REMARK 1 PMID 2226434
REMARK 1 REFERENCE 2
REMARK 1 AUTH W.BODE,I.MAYR,U.BAUMANN,R.HUBER,S.R.STONE,J.HOFSTEENGE
REMARK 1 TITL THE REFINED 1.9 A CRYSTAL STRUCTURE OF HUMAN ALPHA-THROMBIN:
REMARK 1 TITL 2 INTERACTION WITH D-PHE-PRO-ARG CHLOROMETHYLKETONE AND
REMARK 1 TITL 3 SIGNIFICANCE OF THE TYR-PRO-PRO-TRP INSERTION SEGMENT.
REMARK 1 REF EMBO J. V. 8 3467 1989
REMARK 1 REFN ISSN 0261-4189
REMARK 1 PMID 2583108
REMARK 1 REFERENCE 3
REMARK 1 AUTH W.BODE,D.TURK,A.KARSHIKOV
REMARK 1 TITL THE REFINED 1.9-A X-RAY CRYSTAL STRUCTURE OF D-PHE-PRO-ARG
REMARK 1 TITL 2 CHLOROMETHYLKETONE-INHIBITED HUMAN ALPHA-THROMBIN: STRUCTURE
REMARK 1 TITL 3 ANALYSIS, OVERALL STRUCTURE, ELECTROSTATIC PROPERTIES,
REMARK 1 TITL 4 DETAILED ACTIVE-SITE GEOMETRY, AND STRUCTURE-FUNCTION
REMARK 1 TITL 5 RELATIONSHIPS.
REMARK 1 REF PROTEIN SCI. V. 1 426 1992
REMARK 1 REFN ISSN 0961-8368
REMARK 1 PMID 1304349
REMARK 1 REFERENCE 4
REMARK 1 AUTH T.J.RYDEL,K.G.RAVICHANDRAN,A.TULINSKY,W.BODE,R.HUBER,
REMARK 1 AUTH 2 C.ROITSCH,J.W.FENTON
REMARK 1 TITL THE STRUCTURE OF A COMPLEX OF RECOMBINANT HIRUDIN AND HUMAN
REMARK 1 TITL 2 ALPHA-THROMBIN.
REMARK 1 REF SCIENCE V. 249 277 1990
REMARK 1 REFN ISSN 0036-8075
REMARK 1 PMID 2374926
REMARK 1 REFERENCE 5
REMARK 1 AUTH M.T.STUBBS,H.OSCHKINAT,I.MAYR,R.HUBER,H.ANGLIKER,S.R.STONE,
REMARK 1 AUTH 2 W.BODE
REMARK 1 TITL THE INTERACTION OF THROMBIN WITH FIBRINOGEN. A STRUCTURAL
REMARK 1 TITL 2 BASIS FOR ITS SPECIFICITY.
REMARK 1 REF EUR.J.BIOCHEM. V. 206 187 1992
REMARK 1 REFN ISSN 0014-2956
REMARK 1 PMID 1587268
REMARK 1 REFERENCE 6
REMARK 1 AUTH M.G.GRUTTER,J.P.PRIESTLE,J.RAHUEL,H.GROSSENBACHER,W.BODE,
REMARK 1 AUTH 2 J.HOFSTEENGE,S.R.STONE
REMARK 1 TITL CRYSTAL STRUCTURE OF THE THROMBIN-HIRUDIN COMPLEX: A NOVEL
REMARK 1 TITL 2 MODE OF SERINE PROTEASE INHIBITION.
REMARK 1 REF EMBO J. V. 9 2361 1990
REMARK 1 REFN ISSN 0261-4189
REMARK 1 PMID 2369893
REMARK 2
REMARK 2 RESOLUTION. 3.16 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : TNT
REMARK 3 AUTHORS : TRONRUD,TEN EYCK,MATTHEWS
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.16
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : NULL
REMARK 3
REMARK 3 USING DATA ABOVE SIGMA CUTOFF.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : 0.151
REMARK 3 R VALUE (WORKING SET) : NULL
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
REMARK 3 USING ALL DATA, NO SIGMA CUTOFF.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2358
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 9
REMARK 3 SOLVENT ATOMS : 50
REMARK 3
REMARK 3 WILSON B VALUE (FROM FCALC, A**2) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. RMS WEIGHT COUNT
REMARK 3 BOND LENGTHS (A) : 0.015 ; NULL ; NULL
REMARK 3 BOND ANGLES (DEGREES) : 1.930 ; NULL ; NULL
REMARK 3 TORSION ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 TRIGONAL CARBON PLANES (A) : NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES (A) : NULL ; NULL ; NULL
REMARK 3 ISOTROPIC THERMAL FACTORS (A**2) : NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS (A) : NULL ; NULL ; NULL
REMARK 3
REMARK 3 INCORRECT CHIRAL-CENTERS (COUNT) : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 RESTRAINT LIBRARIES.
REMARK 3 STEREOCHEMISTRY : NULL
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 PROLINES ARE TOO FLAT AS A BAD DICTIONARY WAS USED.
REMARK 3
REMARK 3 ASN H 60G IS GLYCOSYLATED. THE SUGAR ELECTRON DENSITY IS
REMARK 3 WEAK AND NO COORDINATES ARE PRESENT FOR THE SUGAR.
REMARK 4
REMARK 4 1DWB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : NULL
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
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) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 68.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.87
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 66.25000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 45.40000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 45.40000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 99.37500
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 45.40000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 45.40000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 33.12500
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 45.40000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 45.40000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 99.37500
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 45.40000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 45.40000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 33.12500
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 66.25000
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: 3640 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13570 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 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
REMARK 400 INDICATOR *L* IS USED FOR RESIDUES 1H - 15 AND CHAIN
REMARK 400 INDICATOR *H* IS USED FOR RESIDUES 16 - 247. CHAIN
REMARK 400 INDICATOR *I* IS USED FOR A C-TERMINAL HIRUDIN PEPTIDE
REMARK 400 ((DES-AMINO ASP55)HIRUDIN(55-65)). THE RESIDUES OF
REMARK 400 CHAIN I ARE NUMBERED FROM 1 - 11. IT BINDS IN THE
REMARK 400 ANION-BINDING EXOSITE.
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 1H
REMARK 465 PHE L 1G
REMARK 465 GLY L 1F
REMARK 465 SER L 1E
REMARK 465 GLY L 1D
REMARK 465 GLY L 14M
REMARK 465 ARG L 14N
REMARK 465 GLU H 247
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 L 1C CG CD OE1 OE2
REMARK 470 ARG H 77A CG CD NE CZ NH1 NH2
REMARK 470 ASN H 78 CG OD1
REMARK 470 LYS H 81 CG CD CE NZ
REMARK 470 ARG H 93 CG CD NE CZ NH1 NH2
REMARK 470 ARG H 97 CG CD NE CZ NH1 NH2
REMARK 470 GLU H 127 CG CD OE1 OE2
REMARK 470 LYS H 149E CG CD CE NZ
REMARK 470 LYS H 169 CG CD CE NZ
REMARK 470 ARG H 173 CG CD NE CZ NH1 NH2
REMARK 470 GLY H 246 CA C O
REMARK 470 ASP I 1 N
REMARK 470 GLU I 8 CG CD OE1 OE2
REMARK 470 GLN I 11 CA C O CB CG CD OE1
REMARK 470 GLN I 11 NE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU L 14E CD GLU L 14E OE1 0.071
REMARK 500 GLU H 18 CD GLU H 18 OE2 0.073
REMARK 500 GLU H 39 CD GLU H 39 OE2 0.070
REMARK 500 GLU H 86 CD GLU H 86 OE2 0.069
REMARK 500 GLU H 97A CD GLU H 97A OE1 0.070
REMARK 500 GLU H 186B CD GLU H 186B OE2 0.076
REMARK 500 GLU I 4 CD GLU I 4 OE2 0.075
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP L 14L CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ASP L 14L CB - CG - OD2 ANGL. DEV. = -6.7 DEGREES
REMARK 500 ASP H 49 N - CA - CB ANGL. DEV. = -11.2 DEGREES
REMARK 500 ASP H 49 CB - CG - OD2 ANGL. DEV. = -6.7 DEGREES
REMARK 500 ASP H 60E CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP H 60E CB - CG - OD2 ANGL. DEV. = -7.1 DEGREES
REMARK 500 ARG H 101 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ASP H 102 CB - CG - OD2 ANGL. DEV. = -5.7 DEGREES
REMARK 500 ASP H 170 CB - CG - OD2 ANGL. DEV. = -5.7 DEGREES
REMARK 500 ASP H 178 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP H 178 CB - CG - OD2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 ASP H 189 CB - CG - OD1 ANGL. DEV. = -6.5 DEGREES
REMARK 500 ASP H 189 CB - CG - OD2 ANGL. DEV. = 6.4 DEGREES
REMARK 500 ASP H 194 CB - CG - OD1 ANGL. DEV. = -5.8 DEGREES
REMARK 500 ASP H 243 CB - CG - OD2 ANGL. DEV. = -5.4 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 -87.59 -126.42
REMARK 500 SER H 48 166.10 175.36
REMARK 500 ASP H 49 -22.82 -36.70
REMARK 500 ARG H 50 -0.47 -146.85
REMARK 500 HIS H 57 -5.36 -51.74
REMARK 500 TYR H 60A 82.23 -155.91
REMARK 500 PRO H 60C -22.00 -35.29
REMARK 500 ASN H 60G 72.57 -154.95
REMARK 500 HIS H 71 -57.42 -123.55
REMARK 500 ASN H 149B -6.77 62.57
REMARK 500 VAL H 149C 71.63 -105.63
REMARK 500 SER H 214 -73.31 -104.45
REMARK 500 GLN H 244 6.57 -58.34
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 GLU L 1C 24.7 L L OUTSIDE RANGE
REMARK 500 ASP L 1A 24.0 L L OUTSIDE RANGE
REMARK 500 ARG H 93 24.9 L L OUTSIDE RANGE
REMARK 500 GLU H 97A 24.6 L L OUTSIDE RANGE
REMARK 500 GLU H 186B 24.4 L L OUTSIDE RANGE
REMARK 500 PHE H 232 24.0 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: ACT
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: CATALYTIC SITE
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BEN H 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN I OF HIRUDIN IIIA
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1DWC RELATED DB: PDB
REMARK 900 RELATED ID: 1DWD RELATED DB: PDB
REMARK 900 RELATED ID: 1DWE RELATED DB: PDB
DBREF 1DWB L 1H 14N UNP P00734 THRB_HUMAN 328 363
DBREF 1DWB H 16 247 UNP P00734 THRB_HUMAN 364 622
DBREF 1DWB I 1 11 UNP P28508 ITHH_HIRME 55 65
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 11 ASP PHE GLU GLU ILE PRO GLU GLU TYR LEU GLN
HET BEN H 1 9
HETNAM BEN BENZAMIDINE
FORMUL 4 BEN C7 H8 N2
FORMUL 5 HOH *50(H2 O)
HELIX 1 1 PHE L 7 SER L 11 5 5
HELIX 2 2 THR L 14B SER L 14I 1 8
HELIX 3 3 ALA H 55 CYS H 58 5 4
HELIX 4 4 PRO H 60B ASP H 60E 5 4
HELIX 5 5 ASP H 125 LEU H 130 1 9
HELIX 6 6 GLU H 164 ASP H 170 1 7
HELIX 7 7 LYS H 185 GLY H 186C 5 5
HELIX 8 8 LEU H 234 ASP H 243 1 10
HELIX 9 9 PRO I 6 LEU I 10 5 5
SHEET 1 A 7 GLN H 30 ARG H 35 0
SHEET 2 A 7 GLU H 39 SER H 48 -1 O GLU H 39 N ARG H 35
SHEET 3 A 7 TRP H 51 THR H 54 -1 O TRP H 51 N ILE H 47
SHEET 4 A 7 ALA H 104 LEU H 108 -1 O ALA H 104 N THR H 54
SHEET 5 A 7 LYS H 81 ILE H 90 -1 N GLU H 86 O LYS H 107
SHEET 6 A 7 LEU H 64 ILE H 68 -1 O LEU H 64 N LEU H 85
SHEET 7 A 7 GLN H 30 ARG H 35 -1 N MET H 32 O ARG H 67
SSBOND 1 CYS L 1 CYS H 122 1555 1555 2.01
SSBOND 2 CYS H 42 CYS H 58 1555 1555 2.06
SSBOND 3 CYS H 168 CYS H 182 1555 1555 2.03
SSBOND 4 CYS H 191 CYS H 220 1555 1555 2.04
CISPEP 1 SER H 36A PRO H 37 0 0.80
SITE 1 ACT 3 HIS H 57 ASP H 102 SER H 195
SITE 1 AC1 7 ASP H 189 ALA H 190 SER H 195 TRP H 215
SITE 2 AC1 7 GLY H 219 GLY H 226 HOH H 325
SITE 1 AC2 17 LYS H 36 GLN H 38 ARG H 67 ARG H 73
SITE 2 AC2 17 THR H 74 ARG H 75 TYR H 76 ILE H 82
SITE 3 AC2 17 MET H 84 LYS H 236 GLN H 239 HOH H 339
SITE 4 AC2 17 HOH I 298 HOH I 299 HOH I 301 HOH I 303
SITE 5 AC2 17 HOH I 304
CRYST1 90.800 90.800 132.500 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 0.011013 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011013 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007547 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
