HEADER HYDROLASE/HYDROLASE INHIBITOR 21-APR-05 1ZGI
TITLE THROMBIN IN COMPLEX WITH AN OXAZOLOPYRIDINE INHIBITOR 21
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THROMBIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: ALPHA-THROMBIN;
COMPND 5 SYNONYM: COAGULATION FACTOR II;
COMPND 6 EC: 3.4.21.5;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: HIRUDIN;
COMPND 9 CHAIN: B;
COMPND 10 FRAGMENT: HIRUGEN;
COMPND 11 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 SYNTHETIC: YES;
SOURCE 7 ORGANISM_SCIENTIFIC: HIRUDO MEDICINALIS;
SOURCE 8 ORGANISM_TAXID: 6421;
SOURCE 9 OTHER_DETAILS: THIS SEQUENCE CORRESPONDS TO THE C-TERMINUS OF
SOURCE 10 HIRUDIN.
KEYWDS THROMBIN, THROMBIN INHIBITOR COMPLEX, HYDROLASE-HYDROLASE INHIBITOR
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.Z.DENG,D.R.MCMASTERS,P.M.RABBAT,P.D.WILLIAMS,C.A.COBURN,Y.YAN,
AUTHOR 2 L.C.KUO,S.D.LEWIS,B.J.LUCAS,J.A.KRUEGER,B.STRULOVICI,J.P.VACCA,
AUTHOR 3 T.A.LYLE,C.S.BURGEY
REVDAT 3 13-JUL-11 1ZGI 1 VERSN
REVDAT 2 24-FEB-09 1ZGI 1 VERSN
REVDAT 1 27-SEP-05 1ZGI 0
JRNL AUTH J.Z.DENG,D.R.MCMASTERS,P.M.RABBAT,P.D.WILLIAMS,C.A.COBURN,
JRNL AUTH 2 Y.YAN,L.C.KUO,S.D.LEWIS,B.J.LUCAS,J.A.KRUEGER,B.STRULOVICI,
JRNL AUTH 3 J.P.VACCA,T.A.LYLE,C.S.BURGEY
JRNL TITL DEVELOPMENT OF AN OXAZOLOPYRIDINE SERIES OF DUAL
JRNL TITL 2 THROMBIN/FACTOR XA INHIBITORS VIA STRUCTURE-GUIDED LEAD
JRNL TITL 3 OPTIMIZATION.
JRNL REF BIOORG.MED.CHEM.LETT. V. 15 4411 2005
JRNL REFN ISSN 0960-894X
JRNL PMID 16137886
JRNL DOI 10.1016/J.BMCL.2005.07.022
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.0
REMARK 3 NUMBER OF REFLECTIONS : 17472
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.220
REMARK 3 FREE R VALUE : 0.264
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1719
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 : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
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 : 2331
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 32
REMARK 3 SOLVENT ATOMS : 62
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 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.80
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC
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) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; 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 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1ZGI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-APR-05.
REMARK 100 THE RCSB ID CODE IS RCSB032693.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-MAY-01
REMARK 200 TEMPERATURE (KELVIN) : 298
REMARK 200 PH : 7.3
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) : 1.54
REMARK 200 MONOCHROMATOR : YALE MIRRORS
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS II
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18364
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 4.800
REMARK 200 R MERGE (I) : 0.08800
REMARK 200 R SYM (I) : 0.08800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.40200
REMARK 200 R SYM FOR SHELL (I) : 0.40200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.36
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.66
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEK8K, SODIUM PHOSPHATE, PH 7.3, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 298K
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 35.46500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.99000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 35.46500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 35.99000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2130 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12450 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 ASP A 14L
REMARK 465 GLY A 14M
REMARK 465 ARG A 15
REMARK 465 THR A 146A
REMARK 465 TRP A 146B
REMARK 465 THR A 146C
REMARK 465 ALA A 146D
REMARK 465 ASN A 146E
REMARK 465 VAL A 146F
REMARK 465 GLY A 146G
REMARK 465 LYS A 146H
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 ILE A 14K CG1 CG2 CD1
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 NH2 ARG A 14D NH2 ARG A 14D 2556 2.04
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 CYS A 220 CB CYS A 220 SG 0.187
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 CYS A 42 CA - CB - SG ANGL. DEV. = 13.5 DEGREES
REMARK 500 CYS A 220 CA - CB - SG ANGL. DEV. = 10.1 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 A 7 -85.24 -131.21
REMARK 500 TYR A 60A 82.46 -156.88
REMARK 500 ASP A 60E 28.20 45.13
REMARK 500 HIS A 71 -53.09 -135.08
REMARK 500 ASN A 78 -0.06 72.22
REMARK 500 ASN A 205 19.81 56.25
REMARK 500 ASP A 243 34.01 -85.33
REMARK 500 GLN A 244 -28.60 -142.34
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 LYS A 14A 24.4 L L OUTSIDE RANGE
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 RESIDUE 382 A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF HIRUDIN
DBREF 1ZGI A 1A 246 UNP P00734 THRB_HUMAN 335 621
DBREF 1ZGI B 355 364 UNP P28511 ITHK_HIRME 55 64
SEQRES 1 A 287 ASP CYS GLY LEU ARG PRO LEU PHE GLU LYS LYS SER LEU
SEQRES 2 A 287 GLU ASP LYS THR GLU ARG GLU LEU LEU GLU SER TYR ILE
SEQRES 3 A 287 ASP GLY ARG ILE VAL GLU GLY SER ASP ALA GLU ILE GLY
SEQRES 4 A 287 MET SER PRO TRP GLN VAL MET LEU PHE ARG LYS SER PRO
SEQRES 5 A 287 GLN GLU LEU LEU CYS GLY ALA SER LEU ILE SER ASP ARG
SEQRES 6 A 287 TRP VAL LEU THR ALA ALA HIS CYS LEU LEU TYR PRO PRO
SEQRES 7 A 287 TRP ASP LYS ASN PHE THR GLU ASN ASP LEU LEU VAL ARG
SEQRES 8 A 287 ILE GLY LYS HIS SER ARG THR ARG TYR GLU ARG ASN ILE
SEQRES 9 A 287 GLU LYS ILE SER MET LEU GLU LYS ILE TYR ILE HIS PRO
SEQRES 10 A 287 ARG TYR ASN TRP ARG GLU ASN LEU ASP ARG ASP ILE ALA
SEQRES 11 A 287 LEU MET LYS LEU LYS LYS PRO VAL ALA PHE SER ASP TYR
SEQRES 12 A 287 ILE HIS PRO VAL CYS LEU PRO ASP ARG GLU THR ALA ALA
SEQRES 13 A 287 SER LEU LEU GLN ALA GLY TYR LYS GLY ARG VAL THR GLY
SEQRES 14 A 287 TRP GLY ASN LEU LYS GLU THR TRP THR ALA ASN VAL GLY
SEQRES 15 A 287 LYS GLY GLN PRO SER VAL LEU GLN VAL VAL ASN LEU PRO
SEQRES 16 A 287 ILE VAL GLU ARG PRO VAL CYS LYS ASP SER THR ARG ILE
SEQRES 17 A 287 ARG ILE THR ASP ASN MET PHE CYS ALA GLY TYR LYS PRO
SEQRES 18 A 287 ASP GLU GLY LYS ARG GLY ASP ALA CYS GLU GLY ASP SER
SEQRES 19 A 287 GLY GLY PRO PHE VAL MET LYS SER PRO PHE ASN ASN ARG
SEQRES 20 A 287 TRP TYR GLN MET GLY ILE VAL SER TRP GLY GLU GLY CYS
SEQRES 21 A 287 ASP ARG ASP GLY LYS TYR GLY PHE TYR THR HIS VAL PHE
SEQRES 22 A 287 ARG LEU LYS LYS TRP ILE GLN LYS VAL ILE ASP GLN PHE
SEQRES 23 A 287 GLY
SEQRES 1 B 10 ASP PHE GLU GLU ILE PRO GLU GLU TYS LEU
MODRES 1ZGI TYS B 363 TYR O-SULFO-L-TYROSINE
HET TYS B 363 16
HET 382 A1001 32
HETNAM TYS O-SULFO-L-TYROSINE
HETNAM 382 (R)-2-(2-(1H-1,2,4-TRIAZOL-1-YL)BENZYL)-N-(2,2-
HETNAM 2 382 DIFLUORO-2-(PIPERIDIN-2-YL)ETHYL)OXAZOLO[4,5-
HETNAM 3 382 C]PYRIDIN-4-AMINE
HETSYN 382 N-{2,2-DIFLUORO-2-[(2R)-PIPERIDIN-2-YL]ETHYL}-2-[2-(1H-
HETSYN 2 382 1,2,4-TRIAZOL-1-YL)BENZYL][1,3]OXAZOLO[4,5-C]PYRIDIN-
HETSYN 3 382 4-AMINE
FORMUL 2 TYS C9 H11 N O6 S
FORMUL 3 382 C22 H23 F2 N7 O
FORMUL 4 HOH *62(H2 O)
HELIX 1 1 PHE A 7 SER A 11 5 5
HELIX 2 2 THR A 14B TYR A 14J 1 9
HELIX 3 3 ALA A 55 CYS A 58 5 4
HELIX 4 4 PRO A 60B ASP A 60E 5 4
HELIX 5 5 THR A 60I ASN A 62 5 3
HELIX 6 6 ASP A 125 LEU A 130 1 9
HELIX 7 7 GLU A 164 SER A 171 1 8
HELIX 8 8 LEU A 234 GLY A 246 1 13
SHEET 1 A 8 SER A 20 ASP A 21 0
SHEET 2 A 8 GLN A 156 VAL A 163 -1 O VAL A 157 N SER A 20
SHEET 3 A 8 MET A 180 ALA A 183 -1 O CYS A 182 N VAL A 163
SHEET 4 A 8 GLY A 226 HIS A 230 -1 O TYR A 228 N PHE A 181
SHEET 5 A 8 TRP A 207 TRP A 215 -1 N TRP A 215 O PHE A 227
SHEET 6 A 8 PRO A 198 LYS A 202 -1 N MET A 201 O TYR A 208
SHEET 7 A 8 LYS A 135 GLY A 140 -1 N ARG A 137 O VAL A 200
SHEET 8 A 8 GLN A 156 VAL A 163 -1 O LEU A 160 N GLY A 136
SHEET 1 B 7 LYS A 81 SER A 83 0
SHEET 2 B 7 LEU A 64 ILE A 68 -1 N ILE A 68 O LYS A 81
SHEET 3 B 7 GLN A 30 ARG A 35 -1 N PHE A 34 O LEU A 65
SHEET 4 B 7 GLU A 39 LEU A 46 -1 O GLU A 39 N ARG A 35
SHEET 5 B 7 TRP A 51 THR A 54 -1 O LEU A 53 N SER A 45
SHEET 6 B 7 ALA A 104 LEU A 108 -1 O MET A 106 N VAL A 52
SHEET 7 B 7 LEU A 85 ILE A 90 -1 N GLU A 86 O LYS A 107
SHEET 1 C 2 LEU A 60 TYR A 60A 0
SHEET 2 C 2 LYS A 60F ASN A 60G-1 O LYS A 60F N TYR A 60A
SSBOND 1 CYS A 1 CYS A 122 1555 1555 1.86
SSBOND 2 CYS A 42 CYS A 58 1555 1555 1.82
SSBOND 3 CYS A 168 CYS A 182 1555 1555 1.87
SSBOND 4 CYS A 191 CYS A 220 1555 1555 1.81
LINK C GLU B 362 N TYS B 363 1555 1555 1.33
LINK C TYS B 363 N LEU B 364 1555 1555 1.33
CISPEP 1 SER A 36A PRO A 37 0 -0.49
SITE 1 AC1 15 HIS A 57 TYR A 60A GLU A 97A ASN A 98
SITE 2 AC1 15 LEU A 99 ASP A 189 ALA A 190 GLU A 192
SITE 3 AC1 15 SER A 195 VAL A 213 TRP A 215 GLY A 216
SITE 4 AC1 15 GLU A 217 GLY A 219 HOH A1033
SITE 1 AC2 12 PHE A 34 LYS A 36 GLN A 38 LEU A 65
SITE 2 AC2 12 ARG A 67 ARG A 73 THR A 74 ARG A 75
SITE 3 AC2 12 TYR A 76 GLU A 80 LYS A 81 ILE A 82
CRYST1 70.930 71.980 73.070 90.00 100.85 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 0.014098 0.000000 0.002702 0.00000
SCALE2 0.000000 0.013893 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013935 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
