HEADER HYDROLASE 14-SEP-12 4BAM
TITLE THROMBIN IN COMPLEX WITH INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THROMBIN LIGHT CHAIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: COAGULATION FACTOR II;
COMPND 5 EC: 3.4.21.5;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: THROMBIN HEAVY CHAIN;
COMPND 8 CHAIN: B;
COMPND 9 SYNONYM: COAGULATION FACTOR II;
COMPND 10 EC: 3.4.21.5;
COMPND 11 MOL_ID: 3;
COMPND 12 MOLECULE: HIRUDIN VARIANT-1;
COMPND 13 CHAIN: D;
COMPND 14 FRAGMENT: RESIDUES 53-64;
COMPND 15 SYNONYM: HIRUDIN-1, HIRUDIN-I, LEPIRUDIN;
COMPND 16 ENGINEERED: YES;
COMPND 17 OTHER_DETAILS: SYNTHETIC C-TERMINAL PEPTIDE 53-64 (WITH SULFATO-
COMPND 18 TYR63)
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 SYNTHETIC: YES;
SOURCE 11 ORGANISM_SCIENTIFIC: HIRUDO MEDICINALIS;
SOURCE 12 ORGANISM_TAXID: 6421
KEYWDS THROMBIN INHIBITOR, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.XUE,D.MUSIL
REVDAT 5 29-JUL-20 4BAM 1 COMPND REMARK HETNAM LINK
REVDAT 5 2 1 SITE
REVDAT 4 05-JUL-17 4BAM 1 REMARK
REVDAT 3 13-MAR-13 4BAM 1 REMARK SITE
REVDAT 2 20-FEB-13 4BAM 1 JRNL
REVDAT 1 16-JAN-13 4BAM 0
JRNL AUTH J.WINQUIST,S.GESCHWINDNER,Y.XUE,L.GUSTAVSSON,D.MUSIL,
JRNL AUTH 2 J.DEINUM,U.H.DANIELSON
JRNL TITL IDENTIFICATION OF STRUCTURE-KINETIC AND
JRNL TITL 2 STRUCTURE-THERMODYNAMIC RELATIONSHIPS FOR THROMBIN
JRNL TITL 3 INHIBITORS.
JRNL REF BIOCHEMISTRY V. 52 613 2013
JRNL REFN ISSN 0006-2960
JRNL PMID 23290007
JRNL DOI 10.1021/BI301333Z
REMARK 2
REMARK 2 RESOLUTION. 1.88 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.1
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.88
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 23.11
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 28259
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.170
REMARK 3 R VALUE (WORKING SET) : 0.169
REMARK 3 FREE R VALUE : 0.195
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030
REMARK 3 FREE R VALUE TEST SET COUNT : 1422
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 : 14
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 1.88
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 1.95
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.87
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2935
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2062
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2803
REMARK 3 BIN R VALUE (WORKING SET) : 0.2038
REMARK 3 BIN FREE R VALUE : 0.2589
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.50
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 132
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 : 2329
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 49
REMARK 3 SOLVENT ATOMS : 338
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 21.88
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.85
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -4.14200
REMARK 3 B22 (A**2) : 3.26520
REMARK 3 B33 (A**2) : 0.87690
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 3.70870
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.190
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.133
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.117
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.125
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.113
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.950
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.936
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 2438 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 3299 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 850 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 62 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 346 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 2438 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : 1 ; 5.000 ; SEMIHARMONIC
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 298 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 3011 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.05
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.72
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 15.16
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4BAM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 14-SEP-12.
REMARK 100 THE DEPOSITION ID IS D_1290054113.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
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 RU300
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28262
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.880
REMARK 200 RESOLUTION RANGE LOW (A) : 24.710
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 4.100
REMARK 200 R MERGE (I) : 0.03000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 32.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.88
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.93
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : 0.16000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 9.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NONE
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.92
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.51
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 34.70500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.75500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 34.70500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 35.75500
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: 3920 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13020 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.4 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, D
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 THR A 1
REMARK 465 PHE A 2
REMARK 465 GLY A 3
REMARK 465 SER A 4
REMARK 465 GLY A 5
REMARK 465 GLU A 6
REMARK 465 GLY A 35
REMARK 465 ARG A 36
REMARK 465 THR B 184A
REMARK 465 ALA B 184B
REMARK 465 ASN B 184C
REMARK 465 VAL B 184D
REMARK 465 GLY B 184E
REMARK 465 LYS B 184F
REMARK 465 GLY B 288
REMARK 465 GLU B 289
REMARK 465 ASP D 353
REMARK 465 GLY D 354
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 ASP A 34 CA C O CB CG OD1 OD2
REMARK 470 TRP B 184 CA C O CB CG CD1 CD2
REMARK 470 TRP B 184 NE1 CE2 CE3 CZ2 CZ3 CH2
REMARK 470 PHE B 287 CA C O CB CG CD1 CD2
REMARK 470 PHE B 287 CE1 CE2 CZ
REMARK 470 GLU D 361 CB CG CD OE1 OE2
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 A 15 -89.99 -127.45
REMARK 500 TYR B 83 78.87 -150.80
REMARK 500 ASN B 89 74.96 -155.20
REMARK 500 HIS B 102 -59.12 -134.39
REMARK 500 ILE B 111 -64.26 -125.62
REMARK 500 THR B 183 -83.34 -97.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A2012 DISTANCE = 6.59 ANGSTROMS
REMARK 525 HOH B2051 DISTANCE = 7.27 ANGSTROMS
REMARK 525 HOH B2106 DISTANCE = 5.87 ANGSTROMS
REMARK 525 HOH D2006 DISTANCE = 8.44 ANGSTROMS
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 B1288 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LYS B 204 O
REMARK 620 2 THR B 207 O 81.8
REMARK 620 3 PHE B 245 O 93.5 92.4
REMARK 620 4 HOH B2253 O 67.6 78.3 159.8
REMARK 620 5 HOH B2254 O 82.6 162.6 81.1 102.6
REMARK 620 6 HOH B2261 O 175.5 97.6 91.0 107.9 98.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B1289 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG B 263 O
REMARK 620 2 LYS B 266 O 92.0
REMARK 620 3 HOH B2277 O 155.8 67.2
REMARK 620 4 HOH B2278 O 91.7 92.7 77.7
REMARK 620 5 HOH B2291 O 100.0 81.6 89.4 167.1
REMARK 620 6 HOH B2311 O 110.6 156.9 89.7 82.4 98.3
REMARK 620 N 1 2 3 4 5
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: DSSP
REMARK 700 THE SHEETS PRESENTED AS "BB" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 6-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 7-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4BAK RELATED DB: PDB
REMARK 900 THROMBIN IN COMPLEX WITH INHIBITOR
REMARK 900 RELATED ID: 4BAM RELATED DB: PDB
REMARK 900 THROMBIN IN COMPLEX WITH INHIBITOR
REMARK 900 RELATED ID: 4BAN RELATED DB: PDB
REMARK 900 THROMBIN IN COMPLEX WITH INHIBITOR
REMARK 900 RELATED ID: 4BAO RELATED DB: PDB
REMARK 900 THROMBIN IN COMPLEX WITH INHIBITOR
REMARK 900 RELATED ID: 4BAQ RELATED DB: PDB
REMARK 900 THROMBIN IN COMPLEX WITH INHIBITOR
DBREF 4BAM A 1 36 UNP P00734 THRB_HUMAN 328 363
DBREF 4BAM B 37 289 UNP P00734 THRB_HUMAN 364 622
DBREF 4BAM D 353 364 UNP P01050 HIRV1_HIRME 53 64
SEQRES 1 A 36 THR PHE GLY SER GLY GLU ALA ASP CYS GLY LEU ARG PRO
SEQRES 2 A 36 LEU PHE GLU LYS LYS SER LEU GLU ASP LYS THR GLU ARG
SEQRES 3 A 36 GLU LEU LEU GLU SER TYR ILE ASP GLY ARG
SEQRES 1 B 259 ILE VAL GLU GLY SER ASP ALA GLU ILE GLY MET SER PRO
SEQRES 2 B 259 TRP GLN VAL MET LEU PHE ARG LYS SER PRO GLN GLU LEU
SEQRES 3 B 259 LEU CYS GLY ALA SER LEU ILE SER ASP ARG TRP VAL LEU
SEQRES 4 B 259 THR ALA ALA HIS CYS LEU LEU TYR PRO PRO TRP ASP LYS
SEQRES 5 B 259 ASN PHE THR GLU ASN ASP LEU LEU VAL ARG ILE GLY LYS
SEQRES 6 B 259 HIS SER ARG THR ARG TYR GLU ARG ASN ILE GLU LYS ILE
SEQRES 7 B 259 SER MET LEU GLU LYS ILE TYR ILE HIS PRO ARG TYR ASN
SEQRES 8 B 259 TRP ARG GLU ASN LEU ASP ARG ASP ILE ALA LEU MET LYS
SEQRES 9 B 259 LEU LYS LYS PRO VAL ALA PHE SER ASP TYR ILE HIS PRO
SEQRES 10 B 259 VAL CYS LEU PRO ASP ARG GLU THR ALA ALA SER LEU LEU
SEQRES 11 B 259 GLN ALA GLY TYR LYS GLY ARG VAL THR GLY TRP GLY ASN
SEQRES 12 B 259 LEU LYS GLU THR TRP THR ALA ASN VAL GLY LYS GLY GLN
SEQRES 13 B 259 PRO SER VAL LEU GLN VAL VAL ASN LEU PRO ILE VAL GLU
SEQRES 14 B 259 ARG PRO VAL CYS LYS ASP SER THR ARG ILE ARG ILE THR
SEQRES 15 B 259 ASP ASN MET PHE CYS ALA GLY TYR LYS PRO ASP GLU GLY
SEQRES 16 B 259 LYS ARG GLY ASP ALA CYS GLU GLY ASP SER GLY GLY PRO
SEQRES 17 B 259 PHE VAL MET LYS SER PRO PHE ASN ASN ARG TRP TYR GLN
SEQRES 18 B 259 MET GLY ILE VAL SER TRP GLY GLU GLY CYS ASP ARG ASP
SEQRES 19 B 259 GLY LYS TYR GLY PHE TYR THR HIS VAL PHE ARG LEU LYS
SEQRES 20 B 259 LYS TRP ILE GLN LYS VAL ILE ASP GLN PHE GLY GLU
SEQRES 1 D 12 ASP GLY ASP PHE GLU GLU ILE PRO GLU GLU TYS LEU
MODRES 4BAM ASN B 89 ASN GLYCOSYLATION SITE
MODRES 4BAM TYS D 363 TYR O-SULFO-L-TYROSINE
HET TYS D 363 16
HET NAG B 901 14
HET MM9 B1287 35
HET NA B1288 1
HET NA B1289 1
HETNAM TYS O-SULFO-L-TYROSINE
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM MM9 (2S)-N-[(4-CARBAMIMIDOYLPHENYL)METHYL]-1-[(2R)-2-
HETNAM 2 MM9 CYCLOHEXYL-2-[[2-(DIMETHYLAMINO)-2-OXIDANYLIDENE-
HETNAM 3 MM9 ETHYL]AMINO]ETHANOYL]AZETIDINE-2-CARBOXAMIDE
HETNAM NA SODIUM ION
FORMUL 3 TYS C9 H11 N O6 S
FORMUL 4 NAG C8 H15 N O6
FORMUL 5 MM9 C24 H36 N6 O3
FORMUL 6 NA 2(NA 1+)
FORMUL 8 HOH *338(H2 O)
HELIX 1 1 PHE A 15 SER A 19 5 5
HELIX 2 2 THR A 24 TYR A 32 1 9
HELIX 3 3 ALA B 77 CYS B 80 5 4
HELIX 4 4 PRO B 84 ASP B 87 5 4
HELIX 5 5 THR B 91 ASN B 93 5 3
HELIX 6 6 ASP B 158 LEU B 166 1 9
HELIX 7 7 GLU B 199 SER B 206 1 8
HELIX 8 8 LYS B 221 GLY B 225 5 5
HELIX 9 9 LEU B 276 GLN B 286 1 11
HELIX 10 10 PRO D 360 LEU D 364 5 5
SHEET 1 BA 7 SER B 41 ASP B 42 0
SHEET 2 BA 7 GLN B 191 PRO B 196 -1 O VAL B 192 N SER B 41
SHEET 3 BA 7 LYS B 171 GLY B 176 -1 O GLY B 172 N LEU B 195
SHEET 4 BA 7 PRO B 238 LYS B 242 -1 O PRO B 238 N THR B 175
SHEET 5 BA 7 TRP B 249 TRP B 257 -1 O TYR B 250 N MET B 241
SHEET 6 BA 7 GLY B 268 HIS B 272 -1 O PHE B 269 N SER B 256
SHEET 7 BA 7 MET B 215 ALA B 218 -1 O PHE B 216 N TYR B 270
SHEET 1 BB 7 GLN B 51 ARG B 56 0
SHEET 2 BB 7 GLU B 61 LEU B 68 -1 O GLU B 61 N ARG B 56
SHEET 3 BB 7 TRP B 73 THR B 76 -1 O LEU B 75 N SER B 67
SHEET 4 BB 7 ALA B 137 LEU B 141 -1 O ALA B 137 N THR B 76
SHEET 5 BB 7 LYS B 113 ILE B 122 -1 N GLU B 118 O LYS B 140
SHEET 6 BB 7 LEU B 95 ILE B 99 -1 O LEU B 95 N LEU B 117
SHEET 7 BB 7 GLN B 51 ARG B 56 -1 O MET B 53 N ARG B 98
SHEET 1 BC 2 LEU B 82 TYR B 83 0
SHEET 2 BC 2 LYS B 88 ASN B 89 -1 O LYS B 88 N TYR B 83
SSBOND 1 CYS A 9 CYS B 155 1555 1555 2.04
SSBOND 2 CYS B 64 CYS B 80 1555 1555 2.03
SSBOND 3 CYS B 203 CYS B 217 1555 1555 2.02
SSBOND 4 CYS B 231 CYS B 261 1555 1555 2.04
LINK ND2 ASN B 89 C1 NAG B 901 1555 1555 1.45
LINK C GLU D 362 N TYS D 363 1555 1555 1.35
LINK C TYS D 363 N LEU D 364 1555 1555 1.37
LINK O LYS B 204 NA NA B1288 1555 1555 2.38
LINK O THR B 207 NA NA B1288 1555 1555 2.32
LINK O PHE B 245 NA NA B1288 4546 1555 2.60
LINK O ARG B 263 NA NA B1289 1555 1555 2.36
LINK O LYS B 266 NA NA B1289 1555 1555 2.38
LINK NA NA B1288 O HOH B2253 1555 1555 2.71
LINK NA NA B1288 O HOH B2254 1555 1555 2.39
LINK NA NA B1288 O HOH B2261 1555 1555 2.23
LINK NA NA B1289 O HOH B2277 1555 1555 2.63
LINK NA NA B1289 O HOH B2278 1555 1555 2.85
LINK NA NA B1289 O HOH B2291 1555 1555 2.33
LINK NA NA B1289 O HOH B2311 1555 1555 2.42
CISPEP 1 SER B 58 PRO B 59 0 -4.90
CRYST1 69.410 71.510 72.160 90.00 100.34 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 0.014407 0.000000 0.002629 0.00000
SCALE2 0.000000 0.013984 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014087 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
