HEADER HYDROLASE/HYDROLASE INHIBITOR 11-FEB-03 1NY2
TITLE HUMAN ALPHA THROMBIN INHIBITED BY RPPGF AND HIRUGEN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THROMBIN LIGHT CHAIN;
COMPND 3 CHAIN: 1;
COMPND 4 FRAGMENT: LIGHT CHAIN A;
COMPND 5 SYNONYM: COAGULATION FACTOR II;
COMPND 6 EC: 3.4.21.5;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: THROMBIN HEAVY CHAIN;
COMPND 9 CHAIN: 2;
COMPND 10 FRAGMENT: HEAVY CHAIN B;
COMPND 11 SYNONYM: COAGULATION FACTOR II;
COMPND 12 EC: 3.4.21.5;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: HIRUGEN;
COMPND 15 CHAIN: 3;
COMPND 16 ENGINEERED: YES;
COMPND 17 MOL_ID: 4;
COMPND 18 MOLECULE: INHIBITOR PEPTIDE RPPGF;
COMPND 19 CHAIN: 4;
COMPND 20 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 OTHER_DETAILS: ALPHA THROMBIN CATALYTIC DOMAIN;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 8 ORGANISM_COMMON: HUMAN;
SOURCE 9 ORGANISM_TAXID: 9606;
SOURCE 10 MOL_ID: 3;
SOURCE 11 SYNTHETIC: YES;
SOURCE 12 OTHER_DETAILS: CHEMICALLY SYNTHESIZED;
SOURCE 13 MOL_ID: 4;
SOURCE 14 SYNTHETIC: YES;
SOURCE 15 OTHER_DETAILS: CHEMICALLY SYNTHESIZED
KEYWDS THROMBOSIS, RETRO BINDING, HYDROLASE, HYDROLASE-HYDROLASE INHIBITOR
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR R.KRISHNAN,A.TULINSKY,A.H.SCHMAIER,A.A.HASAN,M.WARNOCK,S.SRIKANTH,
AUTHOR 2 F.MAHDI
REVDAT 8 15-NOV-23 1NY2 1 REMARK
REVDAT 7 16-AUG-23 1NY2 1 LINK
REVDAT 6 11-OCT-17 1NY2 1 REMARK
REVDAT 5 25-MAR-15 1NY2 1 DBREF
REVDAT 4 13-JUL-11 1NY2 1 VERSN
REVDAT 3 24-FEB-09 1NY2 1 VERSN
REVDAT 2 05-APR-05 1NY2 1 JRNL
REVDAT 1 04-MAR-03 1NY2 0
JRNL AUTH A.A.HASAN,M.WARNOCK,M.NIEMAN,S.SRIKANTH,F.MAHDI,R.KRISHNAN,
JRNL AUTH 2 A.TULINSKY,A.H.SCHMAIER
JRNL TITL MECHANISMS OF ARG-PRO-PRO-GLY-PHE INHIBITION OF THROMBIN.
JRNL REF AM.J.PHYSIOL.HEART V. 285 H183 2003
JRNL REF 2 CIRC.PHYSIOL.
JRNL REFN ISSN 0363-6135
JRNL PMID 12598231
JRNL DOI 10.1152/AJPHEART.00490.2002
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) : 8.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 3.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 16037
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) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.202
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 : 2503
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 51
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) : 0.020 ; NULL
REMARK 3 ANGLE DISTANCE (A) : 0.047 ; 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) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 0.057 ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1NY2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-FEB-03.
REMARK 100 THE DEPOSITION ID IS D_1000018337.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-NOV-97
REMARK 200 TEMPERATURE (KELVIN) : 298
REMARK 200 PH : 4.6
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) : 1.5418
REMARK 200 MONOCHROMATOR : YALE MIRRORS
REMARK 200 OPTICS : YALE MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS II
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : R-AXIS
REMARK 200 DATA SCALING SOFTWARE : R-AXIS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17158
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.500
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 73.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.06800
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) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.30
REMARK 200 COMPLETENESS FOR SHELL (%) : 0.5
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: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: 1DIT
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.06
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.62
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, AMMONIUM SULPHATE, SODIUM
REMARK 280 ACETATE, PH 4.6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 25K,
REMARK 280 TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
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 39.57500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 52.48500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 39.57500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 52.48500
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 1, 2, 3, 4
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 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 PHE 4 384
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 OG SER 2 195 N ARG 4 380 2.08
REMARK 500 O PHE 1 1G N GLY 1 1D 2.10
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 2 75 NE ARG 2 75 CZ 0.080
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 1 1F N - CA - C ANGL. DEV. = -16.0 DEGREES
REMARK 500 GLY 1 1F O - C - N ANGL. DEV. = 10.6 DEGREES
REMARK 500 GLU 1 1C CA - CB - CG ANGL. DEV. = 20.1 DEGREES
REMARK 500 ASP 1 1A CB - CG - OD2 ANGL. DEV. = -6.7 DEGREES
REMARK 500 CYS 1 1 CA - CB - SG ANGL. DEV. = 6.6 DEGREES
REMARK 500 LEU 1 3 O - C - N ANGL. DEV. = 10.7 DEGREES
REMARK 500 ARG 1 4 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 SER 1 11 N - CA - CB ANGL. DEV. = 9.4 DEGREES
REMARK 500 GLU 1 13 CA - CB - CG ANGL. DEV. = 15.8 DEGREES
REMARK 500 ARG 1 14D NE - CZ - NH2 ANGL. DEV. = -5.2 DEGREES
REMARK 500 GLU 1 14E CA - CB - CG ANGL. DEV. = 14.0 DEGREES
REMARK 500 ARG 1 15 NE - CZ - NH1 ANGL. DEV. = 5.3 DEGREES
REMARK 500 ASP 2 21 CB - CG - OD2 ANGL. DEV. = -7.7 DEGREES
REMARK 500 GLN 2 30 N - CA - CB ANGL. DEV. = 11.1 DEGREES
REMARK 500 LEU 2 33 CA - CB - CG ANGL. DEV. = 15.5 DEGREES
REMARK 500 ARG 2 35 CD - NE - CZ ANGL. DEV. = -10.5 DEGREES
REMARK 500 ARG 2 35 NH1 - CZ - NH2 ANGL. DEV. = 9.2 DEGREES
REMARK 500 ARG 2 35 NE - CZ - NH1 ANGL. DEV. = -5.7 DEGREES
REMARK 500 ARG 2 35 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 LEU 2 41 CB - CA - C ANGL. DEV. = 13.3 DEGREES
REMARK 500 ASP 2 49 CB - CG - OD1 ANGL. DEV. = 12.1 DEGREES
REMARK 500 ARG 2 50 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG 2 50 NE - CZ - NH2 ANGL. DEV. = -4.7 DEGREES
REMARK 500 TYR 2 60A CB - CG - CD1 ANGL. DEV. = -4.8 DEGREES
REMARK 500 TRP 2 60D O - C - N ANGL. DEV. = 11.1 DEGREES
REMARK 500 ASP 2 60E CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 LEU 2 65 N - CA - CB ANGL. DEV. = 13.1 DEGREES
REMARK 500 LEU 2 65 CA - CB - CG ANGL. DEV. = 20.5 DEGREES
REMARK 500 ARG 2 73 CD - NE - CZ ANGL. DEV. = -17.2 DEGREES
REMARK 500 ARG 2 73 NE - CZ - NH1 ANGL. DEV. = -11.9 DEGREES
REMARK 500 ARG 2 73 NE - CZ - NH2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ARG 2 75 CG - CD - NE ANGL. DEV. = 39.0 DEGREES
REMARK 500 ARG 2 75 CD - NE - CZ ANGL. DEV. = 42.9 DEGREES
REMARK 500 ARG 2 75 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 ARG 2 75 NE - CZ - NH2 ANGL. DEV. = -8.1 DEGREES
REMARK 500 TYR 2 76 CB - CG - CD1 ANGL. DEV. = -5.1 DEGREES
REMARK 500 GLU 2 77 CB - CG - CD ANGL. DEV. = 17.4 DEGREES
REMARK 500 ARG 2 77A CD - NE - CZ ANGL. DEV. = 20.2 DEGREES
REMARK 500 ARG 2 77A NE - CZ - NH2 ANGL. DEV. = 5.1 DEGREES
REMARK 500 HIS 2 91 CA - CB - CG ANGL. DEV. = -10.4 DEGREES
REMARK 500 ARG 2 93 CD - NE - CZ ANGL. DEV. = 11.0 DEGREES
REMARK 500 TYR 2 94 CB - CG - CD2 ANGL. DEV. = 4.1 DEGREES
REMARK 500 ASN 2 95 N - CA - CB ANGL. DEV. = 16.2 DEGREES
REMARK 500 ARG 2 97 CD - NE - CZ ANGL. DEV. = 11.0 DEGREES
REMARK 500 MET 2 106 CG - SD - CE ANGL. DEV. = -9.7 DEGREES
REMARK 500 VAL 2 112 O - C - N ANGL. DEV. = 9.6 DEGREES
REMARK 500 PHE 2 114 CB - CG - CD1 ANGL. DEV. = -4.4 DEGREES
REMARK 500 LEU 2 123 O - C - N ANGL. DEV. = 12.0 DEGREES
REMARK 500 GLY 2 136 C - N - CA ANGL. DEV. = 14.1 DEGREES
REMARK 500 ARG 2 137 CD - NE - CZ ANGL. DEV. = 12.8 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 92 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 1 1G -157.14 -145.75
REMARK 500 GLU 1 1C -104.56 -31.97
REMARK 500 ALA 1 1B -37.89 -172.60
REMARK 500 LEU 1 6 -9.83 -52.02
REMARK 500 PHE 1 7 -94.66 -123.31
REMARK 500 TYR 1 14J 37.33 -78.46
REMARK 500 ILE 1 14K -66.57 106.26
REMARK 500 SER 2 36A 129.75 -173.46
REMARK 500 CYS 2 42 -169.32 -164.93
REMARK 500 ASN 2 60G 72.87 -174.09
REMARK 500 ARG 2 77A -72.96 -21.20
REMARK 500 ARG 2 97 7.17 -47.25
REMARK 500 GLU 2 97A -78.41 -140.80
REMARK 500 ARG 2 101 71.51 67.22
REMARK 500 HIS 2 119 138.63 -177.76
REMARK 500 ASN 2 204B 10.30 -162.02
REMARK 500 SER 2 214 -85.02 -103.44
REMARK 500 ASP 2 243 -72.45 -67.22
REMARK 500 GLU 3 61 46.47 -71.96
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 2 233 0.14 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 GLU 2 192 11.02
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN 3 OF HIRUGEN
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1HDT RELATED DB: PDB
REMARK 900 STRUCTURE OF A RETRO-BINDING PEPTIDE INHIBITOR COMPLEXED WITH HUMAN-
REMARK 900 THROMBIN
REMARK 900 RELATED ID: 7KME RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN -THROMBIN INHIBITED WITH SEL2711
REMARK 900 RELATED ID: 8KME RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN -THROMBIN INHIBITED WITH SEL2770
REMARK 900 RELATED ID: 1TMU RELATED DB: PDB
REMARK 900 CHANGES IN INTERACTIONS IN COMPLEXES OF HIRUDIN DERIVATIVES AND
REMARK 900 HUMAN -THROMBIN DUE TO DIFFERENT CRYSTAL FORMS
DBREF 1NY2 1 1H 15 UNP P00734 THRB_HUMAN 328 363
DBREF 1NY2 2 16 247 UNP P00734 THRB_HUMAN 364 622
DBREF 1NY2 3 55 64 UNP P28504 HIR2_HIRME 55 64
DBREF 1NY2 4 380 384 PDB 1NY2 1NY2 380 384
SEQRES 1 1 36 THR PHE GLY SER GLY GLU ALA ASP CYS GLY LEU ARG PRO
SEQRES 2 1 36 LEU PHE GLU LYS LYS SER LEU GLU ASP LYS THR GLU ARG
SEQRES 3 1 36 GLU LEU LEU GLU SER TYR ILE ASP GLY ARG
SEQRES 1 2 259 ILE VAL GLU GLY SER ASP ALA GLU ILE GLY MET SER PRO
SEQRES 2 2 259 TRP GLN VAL MET LEU PHE ARG LYS SER PRO GLN GLU LEU
SEQRES 3 2 259 LEU CYS GLY ALA SER LEU ILE SER ASP ARG TRP VAL LEU
SEQRES 4 2 259 THR ALA ALA HIS CYS LEU LEU TYR PRO PRO TRP ASP LYS
SEQRES 5 2 259 ASN PHE THR GLU ASN ASP LEU LEU VAL ARG ILE GLY LYS
SEQRES 6 2 259 HIS SER ARG THR ARG TYR GLU ARG ASN ILE GLU LYS ILE
SEQRES 7 2 259 SER MET LEU GLU LYS ILE TYR ILE HIS PRO ARG TYR ASN
SEQRES 8 2 259 TRP ARG GLU ASN LEU ASP ARG ASP ILE ALA LEU MET LYS
SEQRES 9 2 259 LEU LYS LYS PRO VAL ALA PHE SER ASP TYR ILE HIS PRO
SEQRES 10 2 259 VAL CYS LEU PRO ASP ARG GLU THR ALA ALA SER LEU LEU
SEQRES 11 2 259 GLN ALA GLY TYR LYS GLY ARG VAL THR GLY TRP GLY ASN
SEQRES 12 2 259 LEU LYS GLU THR TRP THR ALA ASN VAL GLY LYS GLY GLN
SEQRES 13 2 259 PRO SER VAL LEU GLN VAL VAL ASN LEU PRO ILE VAL GLU
SEQRES 14 2 259 ARG PRO VAL CYS LYS ASP SER THR ARG ILE ARG ILE THR
SEQRES 15 2 259 ASP ASN MET PHE CYS ALA GLY TYR LYS PRO ASP GLU GLY
SEQRES 16 2 259 LYS ARG GLY ASP ALA CYS GLU GLY ASP SER GLY GLY PRO
SEQRES 17 2 259 PHE VAL MET LYS SER PRO PHE ASN ASN ARG TRP TYR GLN
SEQRES 18 2 259 MET GLY ILE VAL SER TRP GLY GLU GLY CYS ASP ARG ASP
SEQRES 19 2 259 GLY LYS TYR GLY PHE TYR THR HIS VAL PHE ARG LEU LYS
SEQRES 20 2 259 LYS TRP ILE GLN LYS VAL ILE ASP GLN PHE GLY GLU
SEQRES 1 3 10 ASP PHE GLU GLU ILE PRO GLU GLU TYS LEU
SEQRES 1 4 5 ARG PRO PRO GLY PHE
MODRES 1NY2 TYS 3 63 TYR O-SULFO-L-TYROSINE
HET TYS 3 63 16
HETNAM TYS O-SULFO-L-TYROSINE
FORMUL 3 TYS C9 H11 N O6 S
FORMUL 5 HOH *51(H2 O)
HELIX 1 1 GLU 1 14C GLU 1 14H 1 6
HELIX 2 2 ALA 2 55 CYS 2 58 5 4
HELIX 3 3 PRO 2 60B ASP 2 60E 5 4
HELIX 4 4 THR 2 60I ASN 2 62 5 3
HELIX 5 5 ASP 2 125 LEU 2 130 1 9
HELIX 6 6 GLU 2 164 ASP 2 170 1 7
HELIX 7 7 LYS 2 185 GLY 2 186C 5 5
HELIX 8 8 LEU 2 234 GLY 2 246 1 13
SHEET 1 A 7 SER 2 20 ASP 2 21 0
SHEET 2 A 7 GLN 2 156 PRO 2 161 -1 O VAL 2 157 N SER 2 20
SHEET 3 A 7 LYS 2 135 GLY 2 140 -1 N VAL 2 138 O VAL 2 158
SHEET 4 A 7 PRO 2 198 LYS 2 202 -1 O VAL 2 200 N ARG 2 137
SHEET 5 A 7 TRP 2 207 TRP 2 215 -1 O MET 2 210 N PHE 2 199
SHEET 6 A 7 GLY 2 226 THR 2 229 -1 O PHE 2 227 N TRP 2 215
SHEET 7 A 7 MET 2 180 ALA 2 183 -1 N PHE 2 181 O TYR 2 228
SHEET 1 B 7 GLN 2 30 ARG 2 35 0
SHEET 2 B 7 GLU 2 39 LEU 2 46 -1 O GLU 2 39 N ARG 2 35
SHEET 3 B 7 TRP 2 51 THR 2 54 -1 O LEU 2 53 N SER 2 45
SHEET 4 B 7 ALA 2 104 LEU 2 108 -1 O ALA 2 104 N THR 2 54
SHEET 5 B 7 LYS 2 81 ILE 2 90 -1 N TYR 2 89 O LEU 2 105
SHEET 6 B 7 LEU 2 64 ILE 2 68 -1 N VAL 2 66 O SER 2 83
SHEET 7 B 7 GLN 2 30 ARG 2 35 -1 N MET 2 32 O ARG 2 67
SSBOND 1 CYS 1 1 CYS 2 122 1555 1555 2.09
SSBOND 2 CYS 2 42 CYS 2 58 1555 1555 2.04
SSBOND 3 CYS 2 168 CYS 2 182 1555 1555 2.14
SSBOND 4 CYS 2 191 CYS 2 220 1555 1555 2.07
LINK C GLU 3 62 N TYS 3 63 1555 1555 1.31
LINK C TYS 3 63 N LEU 3 64 1555 1555 1.33
CISPEP 1 SER 2 36A PRO 2 37 0 -5.14
SITE 1 AC1 14 PHE 2 34 LYS 2 36 LEU 2 65 ARG 2 67
SITE 2 AC1 14 ARG 2 73 THR 2 74 TYR 2 76 ILE 2 82
SITE 3 AC1 14 GLU 2 97A ASN 2 98 ASP 2 100 ARG 2 175
SITE 4 AC1 14 HOH 3 423 HOH 3 429
CRYST1 79.150 104.970 45.180 90.00 90.00 90.00 P 21 21 2 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 0.012634 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009527 0.000000 0.00000
SCALE3 0.000000 0.000000 0.022134 0.00000
(ATOM LINES ARE NOT SHOWN.)
END