HEADER HYDROLASE/HYDROLASE INHIBITOR 23-OCT-00 1G37
TITLE CRYSTAL STRUCTURE OF HUMAN ALPHA-THROMBIN COMPLEXED WITH BCH-10556 AND
TITLE 2 EXOSITE-DIRECTED PEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA THROMBIN;
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 NONAPEPTIDE INHIBITOR;
COMPND 8 CHAIN: B;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 TISSUE: BLOOD;
SOURCE 6 OTHER_DETAILS: THROMBIN PURCHASED FROM HAEMATOLOGIC TECHNOLOGIES;
SOURCE 7 MOL_ID: 2;
SOURCE 8 SYNTHETIC: YES
KEYWDS PROTEASE, THROMBIN, INHIBITOR, BLOOD CLOTTING, HYDROLASE-HYDROLASE
KEYWDS 2 INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR B.BACHAND,M.TARAZI,Y.ST-DENIS,J.J.EDMUNDS,P.D.WINOCOUR,L.LEBLOND,
AUTHOR 2 M.A.SIDDIQUI
REVDAT 4 09-AUG-23 1G37 1 REMARK LINK
REVDAT 3 13-JUL-11 1G37 1 VERSN
REVDAT 2 24-FEB-09 1G37 1 VERSN
REVDAT 1 21-APR-01 1G37 0
JRNL AUTH B.BACHAND,M.TARAZI,Y.ST-DENIS,J.J.EDMUNDS,P.D.WINOCOUR,
JRNL AUTH 2 L.LEBLOND,M.A.SIDDIQUI
JRNL TITL POTENT AND SELECTIVE BICYCLIC LACTAM INHIBITORS OF THROMBIN.
JRNL TITL 2 PART 4: TRANSITION STATE INHIBITORS.
JRNL REF BIOORG.MED.CHEM.LETT. V. 11 287 2001
JRNL REFN ISSN 0960-894X
JRNL PMID 11212093
JRNL DOI 10.1016/S0960-894X(00)00636-3
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 23917
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 SET) : 0.198
REMARK 3 FREE R VALUE : 0.248
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2387
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 : 2323
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 40
REMARK 3 SOLVENT ATOMS : 81
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 25.00
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) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : 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) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; 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 1G37 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-NOV-00.
REMARK 100 THE DEPOSITION ID IS D_1000012176.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-APR-97
REMARK 200 TEMPERATURE (KELVIN) : 296.0
REMARK 200 PH : 6.5
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 RU300
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : MONOCHROMATOR
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IIC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24483
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.06600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.2
REMARK 200 DATA REDUNDANCY IN SHELL : 2.80
REMARK 200 R MERGE FOR SHELL (I) : 0.19600
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: ISOMORPHOUS WITH OTHER
REMARK 200 THROMBIN COMPLEXES
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: PDB ENTRY 1IHS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.56
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.71
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, SODIUM PHOSPHATE, PH 6.5,
REMARK 280 VAPOR DIFFUSION, HANGING DROP AT 296K, TEMPERATURE 296.0K
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 35.72500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.01500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 35.72500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 36.01500
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 300 REMARK: THE MOLECULE ACTS AS A MONOMER
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: 2090 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12520 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 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 TRP A 147A
REMARK 465 THR A 147B
REMARK 465 ALA A 147C
REMARK 465 ASN A 147D
REMARK 465 VAL A 147E
REMARK 465 GLY A 147F
REMARK 465 LYS A 147G
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 HD1 HIS A 91 H ARG A 93 1.32
REMARK 500
REMARK 500 REMARK: NULL
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 HH21 ARG A 75 HH21 ARG A 75 2555 1.03
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 ARG A 137 NE - CZ - NH1 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG A 137 NE - CZ - NH2 ANGL. DEV. = 3.2 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 -82.30 -126.38
REMARK 500 TYR A 60A 80.73 -153.48
REMARK 500 ASN A 60G 83.19 -159.68
REMARK 500 HIS A 71 -55.13 -128.53
REMARK 500 SER A 115 -168.66 -161.48
REMARK 500 GLU B 362 33.27 -73.78
REMARK 500 TYR B 363 -30.37 -145.03
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 110 A 900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF THROMBIN NONAPEPTIDE
REMARK 800 INHIBITOR
DBREF 1G37 A 1B 245 UNP P00734 THRB_HUMAN 334 620
DBREF 1G37 B 356 364 PDB 1G37 1G37 356 364
SEQRES 1 A 287 ALA ASP CYS GLY LEU ARG PRO LEU PHE GLU LYS LYS SER
SEQRES 2 A 287 LEU GLU ASP LYS THR GLU ARG GLU LEU LEU GLU SER TYR
SEQRES 3 A 287 ILE ASP GLY ARG ILE VAL GLU GLY SER ASP ALA GLU ILE
SEQRES 4 A 287 GLY MET SER PRO TRP GLN VAL MET LEU PHE ARG LYS SER
SEQRES 5 A 287 PRO GLN GLU LEU LEU CYS GLY ALA SER LEU ILE SER ASP
SEQRES 6 A 287 ARG TRP VAL LEU THR ALA ALA HIS CYS LEU LEU TYR PRO
SEQRES 7 A 287 PRO TRP ASP LYS ASN PHE THR GLU ASN ASP LEU LEU VAL
SEQRES 8 A 287 ARG ILE GLY LYS HIS SER ARG THR ARG TYR GLU ARG ASN
SEQRES 9 A 287 ILE GLU LYS ILE SER MET LEU GLU LYS ILE TYR ILE HIS
SEQRES 10 A 287 PRO ARG TYR ASN TRP ARG GLU ASN LEU ASP ARG ASP ILE
SEQRES 11 A 287 ALA LEU MET LYS LEU LYS LYS PRO VAL ALA PHE SER ASP
SEQRES 12 A 287 TYR ILE HIS PRO VAL CYS LEU PRO ASP ARG GLU THR ALA
SEQRES 13 A 287 ALA SER LEU LEU GLN ALA GLY TYR LYS GLY ARG VAL THR
SEQRES 14 A 287 GLY TRP GLY ASN LEU LYS GLU THR TRP THR ALA ASN VAL
SEQRES 15 A 287 GLY LYS GLY GLN PRO SER VAL LEU GLN VAL VAL ASN LEU
SEQRES 16 A 287 PRO ILE VAL GLU ARG PRO VAL CYS LYS ASP SER THR ARG
SEQRES 17 A 287 ILE ARG ILE THR ASP ASN MET PHE CYS ALA GLY TYR LYS
SEQRES 18 A 287 PRO ASP GLU GLY LYS ARG GLY ASP ALA CYS GLU GLY ASP
SEQRES 19 A 287 SER GLY GLY PRO PHE VAL MET LYS SER PRO PHE ASN ASN
SEQRES 20 A 287 ARG TRP TYR GLN MET GLY ILE VAL SER TRP GLY GLU GLY
SEQRES 21 A 287 CYS ASP ARG ASP GLY LYS TYR GLY PHE TYR THR HIS VAL
SEQRES 22 A 287 PHE ARG LEU LYS LYS TRP ILE GLN LYS VAL ILE ASP GLN
SEQRES 23 A 287 PHE
SEQRES 1 B 9 PHE GLU ALA ILE PRO ALA GLU TYR LEU
HET 110 A 900 43
HETNAM 110 3-(4-AMINO-CYCLOHEXYL)-2-HYDROXY-3-[(4-OXO-2-
HETNAM 2 110 PHENYLMETHANESULFONYL-1,2,3,4-TETRAHYDRO-PYRROLO[1,2-
HETNAM 3 110 A]PYRAZINE-6-CARBONYL)-AMINO]-PROPIONIC ACID BUTYL
HETNAM 4 110 ESTER
HETSYN 110 BCH-10556
FORMUL 3 110 C28 H38 N4 O7 S
FORMUL 4 HOH *81(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 ASP A 170 1 7
HELIX 8 8 LYS A 185 GLY A 186C 5 5
HELIX 9 9 LEU A 234 PHE A 245 1 12
SHEET 1 A 7 SER A 20 ASP A 21 0
SHEET 2 A 7 GLN A 156 PRO A 161 -1 N VAL A 157 O SER A 20
SHEET 3 A 7 LYS A 135 GLY A 140 -1 N GLY A 136 O LEU A 160
SHEET 4 A 7 PRO A 198 LYS A 202 -1 O PRO A 198 N THR A 139
SHEET 5 A 7 TRP A 207 TRP A 215 -1 N TYR A 208 O MET A 201
SHEET 6 A 7 GLY A 226 HIS A 230 -1 N PHE A 227 O TRP A 215
SHEET 7 A 7 MET A 180 ALA A 183 -1 O PHE A 181 N TYR A 228
SHEET 1 B 7 GLN A 30 ARG A 35 0
SHEET 2 B 7 GLU A 39 LEU A 46 -1 O GLU A 39 N ARG A 35
SHEET 3 B 7 TRP A 51 THR A 54 -1 N LEU A 53 O SER A 45
SHEET 4 B 7 ALA A 104 LEU A 108 -1 O ALA A 104 N THR A 54
SHEET 5 B 7 LYS A 81 ILE A 90 -1 N GLU A 86 O LYS A 107
SHEET 6 B 7 LEU A 64 ILE A 68 -1 O LEU A 64 N LEU A 85
SHEET 7 B 7 GLN A 30 ARG A 35 -1 N MET A 32 O ARG A 67
SSBOND 1 CYS A 1 CYS A 122 1555 1555 2.00
SSBOND 2 CYS A 42 CYS A 58 1555 1555 2.04
SSBOND 3 CYS A 168 CYS A 182 1555 1555 2.01
SSBOND 4 CYS A 191 CYS A 220 1555 1555 2.05
LINK OG SER A 195 C3 110 A 900 1555 1555 1.44
CISPEP 1 SER A 36A PRO A 37 0 -0.96
SITE 1 AC1 21 LEU A 40 LEU A 41 HIS A 57 TYR A 60A
SITE 2 AC1 21 TRP A 60D GLU A 97A ASN A 98 ILE A 174
SITE 3 AC1 21 ASP A 189 ALA A 190 CYS A 191 GLU A 192
SITE 4 AC1 21 GLY A 193 ASP A 194 SER A 195 SER A 214
SITE 5 AC1 21 TRP A 215 GLY A 216 GLY A 219 HOH A 423
SITE 6 AC1 21 HOH A 478
SITE 1 AC2 8 PHE A 34 LYS A 36 GLN A 38 ARG A 67
SITE 2 AC2 8 ARG A 73 THR A 74 ARG A 75 TYR A 76
CRYST1 71.450 72.030 73.150 90.00 100.71 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 0.013996 0.000000 0.002647 0.00000
SCALE2 0.000000 0.013883 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013913 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
