HEADER HYDROLASE 04-DEC-02 1NC6
TITLE POTENT, SMALL MOLECULE INHIBITORS OF HUMAN MAST CELL TRYPTASE. ANTI-
TITLE 2 ASTHMATIC ACTION OF A DIPEPTIDE-BASED TRANSITION STATE ANALOGUE
TITLE 3 CONTAINING BENZOTHIAZOLE KETONE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRYPSINOGEN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: BETA-TRYPSIN;
COMPND 5 EC: 3.4.21.4;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: CATTLE;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PROTEIN-INHIBITOR COMPLEX, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.J.COSTANZO,S.C.YABUT,H.R.ALMOND JR.,P.ANDRADE-GORDON,T.W.CORCORAN,
AUTHOR 2 L.DE GARAVILLA,J.A.KAUFFMAN,W.M.ABRAHAM,R.RECACHA,D.CHATTOPADHYAY,
AUTHOR 3 B.E.MARYANOFF
REVDAT 3 11-OCT-17 1NC6 1 REMARK
REVDAT 2 24-FEB-09 1NC6 1 VERSN
REVDAT 1 23-SEP-03 1NC6 0
JRNL AUTH M.J.COSTANZO,S.C.YABUT,H.R.ALMOND JR.,P.ANDRADE-GORDON,
JRNL AUTH 2 T.W.CORCORAN,L.DE GARAVILLA,J.A.KAUFFMAN,W.M.ABRAHAM,
JRNL AUTH 3 R.RECACHA,D.CHATTOPADHYAY,B.E.MARYANOFF
JRNL TITL POTENT, SMALL-MOLECULE INHIBITORS OF HUMAN MAST CELL
JRNL TITL 2 TRYPTASE. ANTIASTHMATIC ACTION OF A DIPEPTIDE-BASED
JRNL TITL 3 TRANSITION-STATE ANALOGUE CONTAINING A BENZOTHIAZOLE KETONE.
JRNL REF J.MED.CHEM. V. 46 3865 2003
JRNL REFN ISSN 0022-2623
JRNL PMID 12930148
JRNL DOI 10.1021/JM030050P
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 17.90
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1231211.070
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 15186
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) : 0.175
REMARK 3 FREE R VALUE : 0.206
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1538
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.02
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.60
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2190
REMARK 3 BIN R VALUE (WORKING SET) : 0.2000
REMARK 3 BIN FREE R VALUE : 0.2360
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.20
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 249
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.015
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1629
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 37
REMARK 3 SOLVENT ATOMS : 223
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 10.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.52000
REMARK 3 B22 (A**2) : 0.52000
REMARK 3 B33 (A**2) : -1.04000
REMARK 3 B12 (A**2) : 0.03000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.18
REMARK 3 ESD FROM SIGMAA (A) : 0.12
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.22
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.16
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.011
REMARK 3 BOND ANGLES (DEGREES) : 1.500
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.80
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.090
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 0.780 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.210 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.280 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 1.850 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.42
REMARK 3 BSOL : 56.62
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : ION.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : TRY_INH.PARAM
REMARK 3 PARAMETER FILE 5 : INH5.PARAM
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 PARAMETER FILE 7 : NULL
REMARK 3 PARAMETER FILE 8 : NULL
REMARK 3 PARAMETER FILE 9 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : ION.TOP
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 5 : INH5.TOP
REMARK 3 TOPOLOGY FILE 6 : TOPHCSDX_PRO.TOP
REMARK 3 TOPOLOGY FILE 7 : TOPH19_SOL.TOP
REMARK 3 TOPOLOGY FILE 8 : SULF.TOP
REMARK 3 TOPOLOGY FILE 9 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1NC6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-DEC-02.
REMARK 100 THE DEPOSITION ID IS D_1000017762.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-MAR-00
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.75
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 : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : YALE MIRRORS
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15384
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 99.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
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) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.02
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.6
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 29.55
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.76
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MAGNESIUM CHLORIDE, PH 7.75, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 35.95667
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 71.91333
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 71.91333
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 35.95667
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 A 661 LIES ON A SPECIAL POSITION.
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 O HOH A 640 O HOH A 640 5555 1.86
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 ASP A 71 -77.91 -132.26
REMARK 500 SER A 214 -71.86 -115.99
REMARK 500
REMARK 500 REMARK: NULL
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 CA A 448 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 70 OE1
REMARK 620 2 GLU A 80 OE2 94.0
REMARK 620 3 HOH A 535 O 83.4 87.7
REMARK 620 4 VAL A 75 O 167.6 90.8 85.4
REMARK 620 5 ASN A 72 O 95.9 169.7 96.0 80.0
REMARK 620 6 HOH A 574 O 89.5 85.0 169.5 102.3 92.4
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 448
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 450
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ABB A 300
DBREF 1NC6 A 16 245 UNP P00760 TRY1_BOVIN 21 243
SEQRES 1 A 223 ILE VAL GLY GLY TYR THR CYS GLY ALA ASN THR VAL PRO
SEQRES 2 A 223 TYR GLN VAL SER LEU ASN SER GLY TYR HIS PHE CYS GLY
SEQRES 3 A 223 GLY SER LEU ILE ASN SER GLN TRP VAL VAL SER ALA ALA
SEQRES 4 A 223 HIS CYS TYR LYS SER GLY ILE GLN VAL ARG LEU GLY GLU
SEQRES 5 A 223 ASP ASN ILE ASN VAL VAL GLU GLY ASN GLU GLN PHE ILE
SEQRES 6 A 223 SER ALA SER LYS SER ILE VAL HIS PRO SER TYR ASN SER
SEQRES 7 A 223 ASN THR LEU ASN ASN ASP ILE MET LEU ILE LYS LEU LYS
SEQRES 8 A 223 SER ALA ALA SER LEU ASN SER ARG VAL ALA SER ILE SER
SEQRES 9 A 223 LEU PRO THR SER CYS ALA SER ALA GLY THR GLN CYS LEU
SEQRES 10 A 223 ILE SER GLY TRP GLY ASN THR LYS SER SER GLY THR SER
SEQRES 11 A 223 TYR PRO ASP VAL LEU LYS CYS LEU LYS ALA PRO ILE LEU
SEQRES 12 A 223 SER ASP SER SER CYS LYS SER ALA TYR PRO GLY GLN ILE
SEQRES 13 A 223 THR SER ASN MET PHE CYS ALA GLY TYR LEU GLU GLY GLY
SEQRES 14 A 223 LYS ASP SER CYS GLN GLY ASP SER GLY GLY PRO VAL VAL
SEQRES 15 A 223 CYS SER GLY LYS LEU GLN GLY ILE VAL SER TRP GLY SER
SEQRES 16 A 223 GLY CYS ALA GLN LYS ASN LYS PRO GLY VAL TYR THR LYS
SEQRES 17 A 223 VAL CYS ASN TYR VAL SER TRP ILE LYS GLN THR ILE ALA
SEQRES 18 A 223 SER ASN
HET CA A 448 1
HET SO4 A 450 5
HET ABB A 300 31
HETNAM CA CALCIUM ION
HETNAM SO4 SULFATE ION
HETNAM ABB (2S,4R)-1-ACETYL-N-[(1S)-4-[(AMINOIMINOMETHYL)AMINO]-1-
HETNAM 2 ABB (2-BENZOTHIAZOLYLCARBONYL)BUTYL]-4-HYDROXY-2-
HETNAM 3 ABB PYRROLIDINECARBOXAMIDE
FORMUL 2 CA CA 2+
FORMUL 3 SO4 O4 S 2-
FORMUL 4 ABB C20 H26 N6 O4 S
FORMUL 5 HOH *223(H2 O)
HELIX 1 1 ALA A 55 TYR A 59 5 5
HELIX 2 2 SER A 164 TYR A 172 1 9
HELIX 3 3 TYR A 234 SER A 244 1 11
SHEET 1 A 7 TYR A 20 THR A 21 0
SHEET 2 A 7 LYS A 156 PRO A 161 -1 O CYS A 157 N TYR A 20
SHEET 3 A 7 GLN A 135 GLY A 140 -1 N ILE A 138 O LEU A 158
SHEET 4 A 7 PRO A 198 CYS A 201 -1 O VAL A 200 N LEU A 137
SHEET 5 A 7 LYS A 204 TRP A 215 -1 O LYS A 204 N CYS A 201
SHEET 6 A 7 GLY A 226 LYS A 230 -1 O VAL A 227 N TRP A 215
SHEET 7 A 7 MET A 180 ALA A 183 -1 N PHE A 181 O TYR A 228
SHEET 1 B 7 GLN A 30 ASN A 34 0
SHEET 2 B 7 HIS A 40 ASN A 48 -1 O CYS A 42 N LEU A 33
SHEET 3 B 7 TRP A 51 SER A 54 -1 O VAL A 53 N SER A 45
SHEET 4 B 7 MET A 104 LEU A 108 -1 O MET A 104 N SER A 54
SHEET 5 B 7 GLN A 81 VAL A 90 -1 N ILE A 89 O LEU A 105
SHEET 6 B 7 GLN A 64 LEU A 67 -1 N VAL A 65 O ILE A 83
SHEET 7 B 7 GLN A 30 ASN A 34 -1 N ASN A 34 O GLN A 64
SSBOND 1 CYS A 22 CYS A 157 1555 1555 2.03
SSBOND 2 CYS A 42 CYS A 58 1555 1555 2.03
SSBOND 3 CYS A 128 CYS A 232 1555 1555 2.03
SSBOND 4 CYS A 136 CYS A 201 1555 1555 2.03
SSBOND 5 CYS A 168 CYS A 182 1555 1555 2.03
SSBOND 6 CYS A 191 CYS A 220 1555 1555 2.03
LINK CA CA A 448 OE1 GLU A 70 1555 1555 2.01
LINK C ABB A 300 OG SER A 195 1555 1555 1.79
LINK CA CA A 448 OE2 GLU A 80 1555 1555 2.31
LINK CA CA A 448 O HOH A 535 1555 1555 2.19
LINK CA CA A 448 O VAL A 75 1555 1555 2.32
LINK CA CA A 448 O ASN A 72 1555 1555 2.29
LINK CA CA A 448 O HOH A 574 1555 1555 2.15
SITE 1 AC1 6 GLU A 70 ASN A 72 VAL A 75 GLU A 80
SITE 2 AC1 6 HOH A 535 HOH A 574
SITE 1 AC2 7 LYS A 87 LYS A 107 THR A 149 TYR A 151
SITE 2 AC2 7 HOH A 644 HOH A 674 HOH A 692
SITE 1 AC3 20 HIS A 57 LEU A 99 CYS A 128 SER A 130
SITE 2 AC3 20 ASP A 189 SER A 190 CYS A 191 GLN A 192
SITE 3 AC3 20 GLY A 193 ASP A 194 SER A 195 SER A 214
SITE 4 AC3 20 TRP A 215 GLY A 216 GLY A 219 GLY A 226
SITE 5 AC3 20 HOH A 503 HOH A 568 HOH A 647 HOH A 719
CRYST1 54.670 54.670 107.870 90.00 90.00 120.00 P 31 2 1 6
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 0.018292 0.010561 0.000000 0.00000
SCALE2 0.000000 0.021121 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009270 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
