HEADER HYDROLASE/HYDROLASE INHIBITOR 09-SEP-96 1HXF
TITLE HUMAN THROMBIN COMPLEX WITH HIRUDIN VARIANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THROMBIN;
COMPND 3 CHAIN: L;
COMPND 4 SYNONYM: FACTOR IIA;
COMPND 5 EC: 3.4.21.5;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: THROMBIN;
COMPND 8 CHAIN: H;
COMPND 9 SYNONYM: FACTOR IIA;
COMPND 10 EC: 3.4.21.5;
COMPND 11 MOL_ID: 3;
COMPND 12 MOLECULE: HIRUDIN VARIANT;
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: BLOOD;
SOURCE 6 TISSUE: BLOOD;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 9 ORGANISM_COMMON: HUMAN;
SOURCE 10 ORGANISM_TAXID: 9606;
SOURCE 11 ORGAN: BLOOD;
SOURCE 12 TISSUE: BLOOD;
SOURCE 13 MOL_ID: 3;
SOURCE 14 ORGANISM_SCIENTIFIC: HIRUDO MEDICINALIS;
SOURCE 15 ORGANISM_COMMON: MEDICINAL LEECH;
SOURCE 16 ORGANISM_TAXID: 6421
KEYWDS COMPLEX (SERINE PROTEASE INHIBITOR), SULFATATION, MULTIGENE FAMILY,
KEYWDS 2 BLOOD COAGULATION, PLASMA, CALCIUM-BINDING, GLYCOPROTEIN,
KEYWDS 3 DUPLICATION, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR A.TULINSKY,E.ZHANG
REVDAT 3 13-JUL-11 1HXF 1 VERSN
REVDAT 2 24-FEB-09 1HXF 1 VERSN
REVDAT 1 27-JAN-97 1HXF 0
JRNL AUTH E.ZHANG,A.TULINSKY
JRNL TITL THE MOLECULAR ENVIRONMENT OF THE NA+ BINDING SITE OF
JRNL TITL 2 THROMBIN.
JRNL REF BIOPHYS.CHEM. V. 63 185 1997
JRNL REFN ISSN 0301-4622
JRNL PMID 9108691
JRNL DOI 10.1016/S0301-4622(96)02227-2
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH E.DI CERA,E.R.GUINTO,A.VINDIGNI,Q.D.DANG,Y.M.AYALA,M.WUYI,
REMARK 1 AUTH 2 A.TULINSKY
REMARK 1 TITL THE NA+ BINDING SITE OF THROMBIN
REMARK 1 REF J.BIOL.CHEM. V. 270 22089 1995
REMARK 1 REFN ISSN 0021-9258
REMARK 1 REFERENCE 2
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 3
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 2
REMARK 2 RESOLUTION. 2.10 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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 7.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 3.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 13281
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) : 0.151
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 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 : 2309
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 138
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.00
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) : 0.20
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) : 0.014 ; 0.018
REMARK 3 ANGLE DISTANCE (A) : 0.049 ; 0.038
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.061 ; 0.058
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : 0.033 ; 0.040
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : 0.181 ; 0.150
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : 0.230 ; 0.500
REMARK 3 MULTIPLE TORSION (A) : 0.300 ; 0.500
REMARK 3 H-BOND (X...Y) (A) : 0.260 ; 0.500
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) : 4.000 ; 3.000
REMARK 3 STAGGERED (DEGREES) : 22.900; 15.000
REMARK 3 TRANSVERSE (DEGREES) : 29.000; 20.000
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.700 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.500 ; 2.500
REMARK 3 SIDE-CHAIN BOND (A**2) : 3.000 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 4.000 ; 3.500
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1HXF 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 : 20-FEB-96
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
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 : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : SIEMENS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XENGEN
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15885
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 70.0
REMARK 200 DATA REDUNDANCY : 2.000
REMARK 200 R MERGE (I) : 0.04800
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 (%): 49.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.62
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 35.33000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.23500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 35.33000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 36.23500
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: 3230 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12750 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 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 473 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 1A - 14K AND CHAIN
REMARK 400 INDICATOR *H* IS USED FOR RESIDUES 16 - 244. CHAIN
REMARK 400 INDICATOR *I* IS USED FOR HIRUDIN 55 -64.
REMARK 400 RESIDUES 1 - 7 AND 34 - 36 OF CHAIN L ARE NOT IN ATOM LIST.
REMARK 400 THE LAST THREE C-TERMINAL RESIDUES ARE NOT IN ATOM LIST.
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 -6
REMARK 465 PHE L -5
REMARK 465 GLY L -4
REMARK 465 SER L -3
REMARK 465 GLY L -2
REMARK 465 GLU L -1
REMARK 465 ALA 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 PHE H 245
REMARK 465 GLY H 246
REMARK 465 GLU H 247
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 NZ LYS H 169 O HOH H 422 2.08
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 1A CB - CG - OD1 ANGL. DEV. = -9.1 DEGREES
REMARK 500 ASP L 1A CB - CG - OD2 ANGL. DEV. = 7.0 DEGREES
REMARK 500 ASP L 14 CB - CG - OD1 ANGL. DEV. = -6.9 DEGREES
REMARK 500 ASP L 14 CB - CG - OD2 ANGL. DEV. = 8.0 DEGREES
REMARK 500 ARG H 35 NH1 - CZ - NH2 ANGL. DEV. = 6.7 DEGREES
REMARK 500 ARG H 35 NE - CZ - NH2 ANGL. DEV. = -6.8 DEGREES
REMARK 500 CYS H 42 CA - CB - SG ANGL. DEV. = 10.8 DEGREES
REMARK 500 ARG H 50 NE - CZ - NH1 ANGL. DEV. = -3.4 DEGREES
REMARK 500 TYR H 60A CB - CG - CD1 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ARG H 67 NH1 - CZ - NH2 ANGL. DEV. = -7.1 DEGREES
REMARK 500 ARG H 67 NE - CZ - NH1 ANGL. DEV. = 7.3 DEGREES
REMARK 500 TYR H 76 CB - CG - CD1 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ARG H 77A NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 GLU H 80 CA - CB - CG ANGL. DEV. = 13.9 DEGREES
REMARK 500 SER H 83 N - CA - CB ANGL. DEV. = 9.1 DEGREES
REMARK 500 ARG H 93 NE - CZ - NH2 ANGL. DEV. = 4.3 DEGREES
REMARK 500 TYR H 94 CB - CG - CD2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 ARG H 97 NE - CZ - NH1 ANGL. DEV. = 4.8 DEGREES
REMARK 500 ARG H 97 NE - CZ - NH2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 ARG H 101 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ASP H 102 CB - CG - OD1 ANGL. DEV. = -7.5 DEGREES
REMARK 500 LYS H 109 CA - CB - CG ANGL. DEV. = 21.4 DEGREES
REMARK 500 LYS H 110 CA - CB - CG ANGL. DEV. = 14.2 DEGREES
REMARK 500 PHE H 114 CB - CG - CD2 ANGL. DEV. = 4.5 DEGREES
REMARK 500 PHE H 114 CB - CG - CD1 ANGL. DEV. = -6.2 DEGREES
REMARK 500 TYR H 117 CB - CG - CD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 TYR H 117 CB - CG - CD1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ALA H 132 CA - C - O ANGL. DEV. = -13.3 DEGREES
REMARK 500 ALA H 132 O - C - N ANGL. DEV. = 13.2 DEGREES
REMARK 500 TYR H 134 CG - CD1 - CE1 ANGL. DEV. = 5.3 DEGREES
REMARK 500 ARG H 137 NE - CZ - NH1 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG H 137 NE - CZ - NH2 ANGL. DEV. = 3.5 DEGREES
REMARK 500 GLU H 164 CG - CD - OE2 ANGL. DEV. = 12.3 DEGREES
REMARK 500 ARG H 165 NE - CZ - NH1 ANGL. DEV. = 8.6 DEGREES
REMARK 500 ARG H 173 NE - CZ - NH2 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ARG H 175 NE - CZ - NH2 ANGL. DEV. = 4.4 DEGREES
REMARK 500 ASP H 178 CB - CG - OD2 ANGL. DEV. = -7.4 DEGREES
REMARK 500 TYR H 184A CB - CG - CD2 ANGL. DEV. = 5.1 DEGREES
REMARK 500 TYR H 184A CB - CG - CD1 ANGL. DEV. = -4.8 DEGREES
REMARK 500 ARG H 206 NE - CZ - NH1 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ASP H 221 CB - CG - OD1 ANGL. DEV. = 8.8 DEGREES
REMARK 500 ARG H 221A NE - CZ - NH1 ANGL. DEV. = -5.9 DEGREES
REMARK 500 TYR H 225 CB - CG - CD1 ANGL. DEV. = -4.1 DEGREES
REMARK 500 ARG H 233 NE - CZ - NH1 ANGL. DEV. = 11.4 DEGREES
REMARK 500 ARG H 233 NE - CZ - NH2 ANGL. DEV. = -9.1 DEGREES
REMARK 500 ASP H 243 CB - CG - OD1 ANGL. DEV. = 8.2 DEGREES
REMARK 500 ASP I 55 CB - CG - OD1 ANGL. DEV. = 7.0 DEGREES
REMARK 500 TYR I 63 CB - CA - C ANGL. DEV. = 16.4 DEGREES
REMARK 500 TYR I 63 CB - CG - CD2 ANGL. DEV. = -4.9 DEGREES
REMARK 500 TYR I 63 CB - CG - CD1 ANGL. DEV. = 7.5 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 51 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 7 -88.03 -123.46
REMARK 500 TYR L 14J 48.72 -91.64
REMARK 500 GLU H 18 32.89 72.62
REMARK 500 ASN H 60G 82.02 -151.37
REMARK 500 HIS H 71 -57.46 -135.20
REMARK 500 ASN H 78 -12.94 75.83
REMARK 500 GLU H 97A -62.28 -106.25
REMARK 500 ASP H 102 82.99 -67.61
REMARK 500 SER H 115 -169.04 -170.40
REMARK 500 ARG H 126 -37.85 -38.87
REMARK 500 SER H 195 151.24 -40.63
REMARK 500 SER H 214 -71.72 -110.92
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 TYR I 63 0.13 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 THR H 54 11.00
REMARK 500 PHE H 60H -11.19
REMARK 500 VAL H 157 -11.23
REMARK 500 THR H 172 -10.38
REMARK 500 MET H 210 11.36
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: ACT
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 CHAIN I OF HIRUDIN VARIANT
DBREF 1HXF L -6 17 UNP P00734 THRB_HUMAN 328 363
DBREF 1HXF H 16 247 UNP P00734 THRB_HUMAN 364 622
DBREF 1HXF I 55 64 UNP P01050 ITH1_HIRME 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 GLY GLU TYR LEU
FORMUL 4 HOH *138(H2 O)
HELIX 1 1 GLU L 8 LYS L 10 5 3
HELIX 2 2 GLU L 14C SER L 14I 1 7
HELIX 3 3 ALA H 56 CYS H 58 5 3
HELIX 4 4 PRO H 60B TRP H 60D 5 3
HELIX 5 5 GLU H 61 ASP H 63 5 3
HELIX 6 6 ARG H 126 LEU H 129C 1 7
HELIX 7 7 ARG H 165 SER H 171 1 7
HELIX 8 8 PHE H 232 ASP H 243 5 12
SHEET 1 A 4 LYS H 81 MET H 84 0
SHEET 2 A 4 LEU H 64 ILE H 68 -1 N ILE H 68 O LYS H 81
SHEET 3 A 4 GLN H 30 ARG H 35 -1 N PHE H 34 O LEU H 65
SHEET 4 A 4 GLU H 39 SER H 45 -1 N ALA H 44 O VAL H 31
SHEET 1 B 3 TRP H 51 THR H 54 0
SHEET 2 B 3 ALA H 104 LEU H 108 -1 N MET H 106 O VAL H 52
SHEET 3 B 3 LEU H 85 ILE H 90 -1 N TYR H 89 O LEU H 105
SHEET 1 C 2 LYS H 135 GLY H 140 0
SHEET 2 C 2 GLN H 156 PRO H 161 -1 N LEU H 160 O GLY H 136
SHEET 1 D 4 MET H 180 ALA H 183 0
SHEET 2 D 4 GLY H 226 HIS H 230 -1 N TYR H 228 O PHE H 181
SHEET 3 D 4 TRP H 207 TRP H 215 -1 N TRP H 215 O PHE H 227
SHEET 4 D 4 PRO H 198 LYS H 202 -1 N MET H 201 O TYR H 208
SSBOND 1 CYS L 1 CYS H 122 1555 1555 2.01
SSBOND 2 CYS H 42 CYS H 58 1555 1555 2.00
SSBOND 3 CYS H 168 CYS H 182 1555 1555 2.01
SSBOND 4 CYS H 191 CYS H 220 1555 1555 2.05
CISPEP 1 SER H 36A PRO H 37 0 -1.11
SITE 1 ACT 3 HIS H 57 ASP H 102 SER H 195
SITE 1 AC1 13 PHE H 34 LYS H 36 GLN H 38 ARG H 73
SITE 2 AC1 13 THR H 74 ARG H 75 TYR H 76 ILE H 82
SITE 3 AC1 13 MET H 84 SER H 153 HOH H 454 HOH I 423
SITE 4 AC1 13 HOH I 528
CRYST1 70.660 72.470 73.090 90.00 100.75 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 0.014152 0.000000 0.002687 0.00000
SCALE2 0.000000 0.013799 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013926 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
