HEADER COMPLEX(SERINE PROTEINASE/INHIBITOR) 27-JUN-94 1HAH
TITLE THE ISOMORPHOUS STRUCTURES OF PRETHROMBIN2, HIRUGEN-AND PPACK-
TITLE 2 THROMBIN: CHANGES ACCOMPANYING ACTIVATION AND EXOSITE BINDING TO
TITLE 3 THROMBIN
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: HIRUGEN;
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 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 7 ORGANISM_COMMON: HUMAN;
SOURCE 8 ORGANISM_TAXID: 9606;
SOURCE 9 MOL_ID: 3;
SOURCE 10 ORGANISM_SCIENTIFIC: HIRUDO MEDICINALIS;
SOURCE 11 ORGANISM_COMMON: MEDICINAL LEECH;
SOURCE 12 ORGANISM_TAXID: 6421
KEYWDS COMPLEX(SERINE PROTEINASE-INHIBITOR), COMPLEX(SERINE PROTEINASE-
KEYWDS 2 INHIBITOR) COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR A.TULINSKY,J.VIJAYALAKSHMI
REVDAT 7 29-JUL-20 1HAH 1 COMPND REMARK HETNAM LINK
REVDAT 7 2 1 SITE
REVDAT 6 14-AUG-19 1HAH 1 REMARK
REVDAT 5 17-JUL-19 1HAH 1 REMARK LINK
REVDAT 4 29-NOV-17 1HAH 1 HELIX
REVDAT 3 13-JUL-11 1HAH 1 VERSN
REVDAT 2 24-FEB-09 1HAH 1 VERSN
REVDAT 1 20-DEC-94 1HAH 0
JRNL AUTH J.VIJAYALAKSHMI,K.P.PADMANABHAN,K.G.MANN,A.TULINSKY
JRNL TITL THE ISOMORPHOUS STRUCTURES OF PRETHROMBIN2, HIRUGEN-, AND
JRNL TITL 2 PPACK-THROMBIN: CHANGES ACCOMPANYING ACTIVATION AND EXOSITE
JRNL TITL 3 BINDING TO THROMBIN.
JRNL REF PROTEIN SCI. V. 3 2254 1994
JRNL REFN ISSN 0961-8368
JRNL PMID 7756983
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH T.J.RYDEL,A.TULINSKY,W.BODE,R.HUBER
REMARK 1 TITL REFINED STRUCTURE OF THE HIRUDIN-THROMBIN COMPLEX
REMARK 1 REF J.MOL.BIOL. V. 221 583 1991
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 2
REMARK 1 AUTH E.SKRZYPCZAK-JANKUN,V.E.CARPEROS,K.G.RAVICHANDRAN,
REMARK 1 AUTH 2 A.TULINSKY,M.WESTBROOK,J.M.MARAGANORE
REMARK 1 TITL STRUCTURE OF THE HIRUGEN AND HIRULOG 1 COMPLEXES OF
REMARK 1 TITL 2 ALPHA-THROMBIN
REMARK 1 REF J.MOL.BIOL. V. 221 1379 1991
REMARK 1 REFN ISSN 0022-2836
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PROLSQ
REMARK 3 AUTHORS : KONNERT,HENDRICKSON
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 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 15157
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 + TEST SET) : 0.114
REMARK 3 R VALUE (WORKING SET) : 0.114
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 FIT/AGREEMENT OF MODEL WITH ALL DATA.
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 : 2435
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 14
REMARK 3 SOLVENT ATOMS : 204
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
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 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : NULL ; NULL
REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.200 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.900 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.600 ; 2.500
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.500 ; 3.000
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1HAH 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_1000173745.
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: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.79
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.66
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 35.87500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.19500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 35.87500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 36.19500
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: 4450 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13220 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 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 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 HOH H 508 LIES ON A SPECIAL POSITION.
REMARK 375 HOH H 518 LIES ON A SPECIAL POSITION.
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 N-ACETYLHIRUDIN 53 - 64 WITH
REMARK 400 SULFATO-TYR 63.
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 H 148A
REMARK 465 ALA H 148B
REMARK 465 ASN H 148C
REMARK 465 VAL H 148D
REMARK 465 GLY H 148E
REMARK 465 LYS H 148F
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 O HOH H 434 O HOH H 434 2555 1.85
REMARK 500
REMARK 500 REMARK: NULL
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 ARG L 15 CZ ARG L 15 NH1 0.079
REMARK 500 GLY H 219 N GLY H 219 CA 0.093
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 GLY L 1F CA - C - O ANGL. DEV. = -12.1 DEGREES
REMARK 500 ASP L 1A CB - CG - OD1 ANGL. DEV. = -8.8 DEGREES
REMARK 500 ASP L 1A CB - CG - OD2 ANGL. DEV. = 7.4 DEGREES
REMARK 500 ARG L 4 NH1 - CZ - NH2 ANGL. DEV. = -6.7 DEGREES
REMARK 500 ARG L 4 NE - CZ - NH2 ANGL. DEV. = 3.9 DEGREES
REMARK 500 ARG L 14D CD - NE - CZ ANGL. DEV. = 10.6 DEGREES
REMARK 500 ARG L 14D NE - CZ - NH2 ANGL. DEV. = 5.3 DEGREES
REMARK 500 GLU L 14H OE1 - CD - OE2 ANGL. DEV. = 9.1 DEGREES
REMARK 500 ASP L 14L C - N - CA ANGL. DEV. = 15.1 DEGREES
REMARK 500 ARG L 15 C - N - CA ANGL. DEV. = 24.5 DEGREES
REMARK 500 ARG L 15 CD - NE - CZ ANGL. DEV. = 19.9 DEGREES
REMARK 500 ARG L 15 NE - CZ - NH1 ANGL. DEV. = 14.9 DEGREES
REMARK 500 ARG L 15 NE - CZ - NH2 ANGL. DEV. = -10.4 DEGREES
REMARK 500 GLU H 18 CG - CD - OE2 ANGL. DEV. = -12.5 DEGREES
REMARK 500 SER H 20 N - CA - CB ANGL. DEV. = 10.4 DEGREES
REMARK 500 ASP H 21 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP H 21 CB - CG - OD2 ANGL. DEV. = -10.2 DEGREES
REMARK 500 SER H 27 N - CA - CB ANGL. DEV. = 13.0 DEGREES
REMARK 500 LEU H 33 CB - CA - C ANGL. DEV. = 11.6 DEGREES
REMARK 500 LEU H 33 CB - CG - CD2 ANGL. DEV. = -14.3 DEGREES
REMARK 500 ARG H 35 NE - CZ - NH2 ANGL. DEV. = -7.0 DEGREES
REMARK 500 ASP H 49 CB - CG - OD2 ANGL. DEV. = -7.0 DEGREES
REMARK 500 ARG H 50 NE - CZ - NH2 ANGL. DEV. = -7.8 DEGREES
REMARK 500 TYR H 60A CB - CG - CD2 ANGL. DEV. = 3.8 DEGREES
REMARK 500 TYR H 60A CB - CG - CD1 ANGL. DEV. = -5.9 DEGREES
REMARK 500 ASP H 60E CB - CG - OD1 ANGL. DEV. = -5.5 DEGREES
REMARK 500 PHE H 60H CB - CG - CD1 ANGL. DEV. = -4.5 DEGREES
REMARK 500 THR H 60I CA - CB - CG2 ANGL. DEV. = 9.9 DEGREES
REMARK 500 GLU H 61 OE1 - CD - OE2 ANGL. DEV. = 10.5 DEGREES
REMARK 500 ARG H 67 C - N - CA ANGL. DEV. = 15.8 DEGREES
REMARK 500 ARG H 73 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG H 75 CG - CD - NE ANGL. DEV. = 19.3 DEGREES
REMARK 500 ARG H 75 CD - NE - CZ ANGL. DEV. = 25.3 DEGREES
REMARK 500 ARG H 75 NE - CZ - NH1 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG H 75 NE - CZ - NH2 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG H 75 NE - CZ - NH2 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG H 77A NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG H 77A NE - CZ - NH2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 GLU H 80 CG - CD - OE2 ANGL. DEV. = -12.5 DEGREES
REMARK 500 MET H 84 CA - CB - CG ANGL. DEV. = -10.4 DEGREES
REMARK 500 TYR H 94 CB - CG - CD2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ARG H 97 NE - CZ - NH1 ANGL. DEV. = 6.3 DEGREES
REMARK 500 ARG H 97 NE - CZ - NH2 ANGL. DEV. = -7.8 DEGREES
REMARK 500 ASP H 100 CB - CG - OD2 ANGL. DEV. = -8.5 DEGREES
REMARK 500 ARG H 101 NE - CZ - NH1 ANGL. DEV. = 8.0 DEGREES
REMARK 500 ARG H 101 NE - CZ - NH2 ANGL. DEV. = -7.2 DEGREES
REMARK 500 ASP H 102 CB - CG - OD2 ANGL. DEV. = -7.5 DEGREES
REMARK 500 ALA H 113 O - C - N ANGL. DEV. = 10.2 DEGREES
REMARK 500 GLU H 127 CA - CB - CG ANGL. DEV. = 13.3 DEGREES
REMARK 500 TYR H 134 CB - CG - CD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 71 ANGLE DEVIATIONS.
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 1G -130.16 172.89
REMARK 500 GLU L 1C -105.55 -106.22
REMARK 500 ALA L 1B -53.49 -156.58
REMARK 500 PHE L 7 -66.19 -128.58
REMARK 500 TYR L 14J 32.74 -93.90
REMARK 500 ASP L 14L 132.07 45.08
REMARK 500 SER H 48 -167.15 -160.78
REMARK 500 TYR H 60A 80.24 -157.20
REMARK 500 HIS H 71 -62.84 -126.11
REMARK 500 ILE H 79 -62.52 -120.73
REMARK 500 LYS H 87 146.92 -173.14
REMARK 500 LYS H 186D 133.19 -176.39
REMARK 500 SER H 195 151.75 -49.28
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 0.23 SIDE CHAIN
REMARK 500 ARG L 15 0.13 SIDE CHAIN
REMARK 500 ARG H 50 0.20 SIDE CHAIN
REMARK 500 ARG H 101 0.10 SIDE CHAIN
REMARK 500 ASP H 102 0.08 SIDE CHAIN
REMARK 500 ARG H 173 0.14 SIDE CHAIN
REMARK 500 ARG H 187 0.12 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 PRO L 5 -10.35
REMARK 500 ILE H 16 -11.74
REMARK 500 LEU H 160 -10.51
REMARK 500 GLY H 188 -11.67
REMARK 500
REMARK 500 REMARK: NULL
REMARK 700
REMARK 700 SHEET
REMARK 700 THE SHEET PRESENTED AS *B1* ON SHEET RECORDS BELOW IS
REMARK 700 ACTUALLY A SIX-STRANDED BETA-BARREL. THIS IS REPRESENTED
REMARK 700 BY A SEVEN-STRANDED SHEET IN WHICH THE FIRST AND LAST
REMARK 700 STRANDS ARE IDENTICAL. THE SHEET PRESENTED AS *B2* ON
REMARK 700 SHEET RECORDS BELOW IS ACTUALLY A SEVEN-STRANDED
REMARK 700 BETA-BARREL. THIS IS REPRESENTED BY AN EIGHT-STRANDED
REMARK 700 SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CAT
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 PEPTIDE ASP I 55 - LEU I 64 AT THE EXOSITE OF THROMBIN IS
REMARK 999 HIRUGEN MOLECULE, WHICH IS PART OF HIRUDIN 53 - 65.
DBREF 1HAH L 1 15 UNP P00734 THRB_HUMAN 328 363
DBREF 1HAH H 16 247 UNP P00734 THRB_HUMAN 364 622
DBREF 1HAH I 55 64 PDB 1HAH 1HAH 55 64
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 10 ASP PHE GLU GLU ILE PRO GLU GLU TYS LEU
MODRES 1HAH ASN H 60G ASN GLYCOSYLATION SITE
MODRES 1HAH TYS I 63 TYR O-SULFO-L-TYROSINE
HET TYS I 63 16
HET NAG H 400 14
HETNAM TYS O-SULFO-L-TYROSINE
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
FORMUL 3 TYS C9 H11 N O6 S
FORMUL 4 NAG C8 H15 N O6
FORMUL 5 HOH *204(H2 O)
HELIX 1 H1 THR L 14B GLU L 14H 1 7
HELIX 2 H2 ASP H 125 LEU H 130 1 9
HELIX 3 H3 GLU H 164 ASP H 170 1 7
HELIX 4 H4 HIS H 230 GLN H 244 1 15
SHEET 1 B1 7 TRP H 29 LYS H 36 0
SHEET 2 B1 7 LEU H 41 ILE H 47 -1
SHEET 3 B1 7 ARG H 50 ALA H 55 -1
SHEET 4 B1 7 ARG H 101 LYS H 109 -1
SHEET 5 B1 7 GLU H 80 PRO H 92 -1
SHEET 6 B1 7 ASP H 63 GLY H 69 -1
SHEET 7 B1 7 TRP H 29 LYS H 36 -1
SHEET 1 B2 8 GLY H 133 TRP H 141 0
SHEET 2 B2 8 LEU H 155 ILE H 162 -1
SHEET 3 B2 8 ASN H 179 LYS H 185 -1
SHEET 4 B2 8 TYR H 225 THR H 229 -1
SHEET 5 B2 8 ILE H 212 GLY H 219 -1
SHEET 6 B2 8 ARG H 206 GLN H 209 -1
SHEET 7 B2 8 GLY H 196 SER H 203 -1
SHEET 8 B2 8 GLY H 133 TRP H 141 -1
SSBOND 1 CYS L 1 CYS H 122 1555 1555 2.05
SSBOND 2 CYS H 42 CYS H 58 1555 1555 2.03
SSBOND 3 CYS H 168 CYS H 182 1555 1555 2.00
SSBOND 4 CYS H 191 CYS H 220 1555 1555 2.04
LINK ND2 ASN H 60G C1 NAG H 400 1555 1555 1.47
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
CISPEP 1 SER H 36A PRO H 37 0 -3.32
SITE 1 CAT 3 HIS H 57 ASP H 102 SER H 195
CRYST1 71.750 72.390 73.520 90.00 101.26 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 0.013937 0.000000 0.002775 0.00000
SCALE2 0.000000 0.013814 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013869 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
