HEADER HYDROLASE 28-MAR-03 1OWE
TITLE SUBSTITUTED 2-NAPHTHAMIDINE INHIBITORS OF UROKINASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UROKINASE-TYPE PLASMINOGEN ACTIVATOR;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 179-423;
COMPND 5 SYNONYM: UPA, U-PLASMINOGEN ACTIVATOR;
COMPND 6 EC: 3.4.21.73;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: PLAU;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS
KEYWDS PLASMINOGEN ACTIVATION, HYDROLASE, SERINE PROTEASE, GLYCOPROTEIN,
KEYWDS 2 KRINGLE, EGF-LIKE DOMAIN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.D.WENDT,T.W.ROCKWAY,A.GEYER,W.MCCLELLAN,M.WEITZBERG,X.ZHAO,
AUTHOR 2 R.MANTEI,V.L.NIENABER,K.STEWART,V.KLINGHOFER,V.L.GIRANDA
REVDAT 4 11-OCT-17 1OWE 1 REMARK
REVDAT 3 24-FEB-09 1OWE 1 VERSN
REVDAT 2 20-JAN-04 1OWE 1 JRNL
REVDAT 1 30-SEP-03 1OWE 0
JRNL AUTH M.D.WENDT,T.W.ROCKWAY,A.GEYER,W.MCCLELLAN,M.WEITZBERG,
JRNL AUTH 2 X.ZHAO,R.MANTEI,V.L.NIENABER,K.STEWART,V.KLINGHOFER,
JRNL AUTH 3 V.L.GIRANDA
JRNL TITL IDENTIFICATION OF NOVEL BINDING INTERACTIONS IN THE
JRNL TITL 2 DEVELOPMENT OF POTENT, SELECTIVE 2-NAPHTHAMIDINE INHIBITORS
JRNL TITL 3 OF UROKINASE. SYNTHESIS, STRUCTURAL ANALYSIS, AND SAR OF
JRNL TITL 4 N-PHENYL AMIDE 6-SUBSTITUTION.
JRNL REF J.MED.CHEM. V. 47 303 2004
JRNL REFN ISSN 0022-2623
JRNL PMID 14711304
JRNL DOI 10.1021/JM0300072
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 98.0
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 10000000.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0010
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 77.9
REMARK 3 NUMBER OF REFLECTIONS : 25225
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) : 0.210
REMARK 3 FREE R VALUE : 0.236
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2547
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) : 1.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.70
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 39.70
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1889
REMARK 3 BIN R VALUE (WORKING SET) : 0.2380
REMARK 3 BIN FREE R VALUE : 0.2600
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.50
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 222
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.017
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1934
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) : 11.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 12.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
REMARK 3 B12 (A**2) : 0.00000
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) : 0.17
REMARK 3 ESD FROM SIGMAA (A) : 0.10
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) : 0.19
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.13
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.029
REMARK 3 BOND ANGLES (DEGREES) : 2.600
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 25.70
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.920
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) : 1.350 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.960 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 3.330 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 5.220 ; 2.500
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 : PARAM11.WAT
REMARK 3 PARAMETER FILE 2 : PARVICKI.PRO
REMARK 3 PARAMETER FILE 3 : PARAM19X.PRO
REMARK 3 PARAMETER FILE 4 : PARHCSDX.PRO
REMARK 3 PARAMETER FILE 5 : 202675.XPRM
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1OWE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-APR-03.
REMARK 100 THE DEPOSITION ID IS D_1000018735.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-JUN-97
REMARK 200 TEMPERATURE (KELVIN) : 160
REMARK 200 PH : NULL
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
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
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 : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30696
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 19.180
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
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) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 36.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.96
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 27.58000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 41.15000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 26.50000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 41.15000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.58000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 26.50000
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: 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 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 CYS A 133 SG
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 SER A 230 CA SER A 230 CB 0.104
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 GLU A 63 CB - CG - CD ANGL. DEV. = 19.4 DEGREES
REMARK 500 GLU A 63 OE1 - CD - OE2 ANGL. DEV. = -16.2 DEGREES
REMARK 500 GLU A 63 CG - CD - OE1 ANGL. DEV. = 12.2 DEGREES
REMARK 500 CYS A 180 CA - CB - SG ANGL. DEV. = -12.0 DEGREES
REMARK 500 TYR A 186 O - C - N ANGL. DEV. = -10.3 DEGREES
REMARK 500 ASP A 205 CB - CG - OD1 ANGL. DEV. = 7.1 DEGREES
REMARK 500 ARG A 255 CG - CD - NE ANGL. DEV. = 13.3 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 VAL A 32 -67.01 -109.36
REMARK 500 SER A 51 -147.45 -143.77
REMARK 500 PRO A 60 20.19 -79.01
REMARK 500 TYR A 185 -107.39 -85.42
REMARK 500 SER A 230 -64.82 -122.60
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 SO4 A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 675 A 1001
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1FV9 RELATED DB: PDB
REMARK 900 RELATED ID: 1OWD RELATED DB: PDB
REMARK 900 RELATED ID: 1OWH RELATED DB: PDB
REMARK 900 RELATED ID: 1OWI RELATED DB: PDB
REMARK 900 RELATED ID: 1OWJ RELATED DB: PDB
REMARK 900 RELATED ID: 1OWK RELATED DB: PDB
DBREF 1OWE A 1 258 UNP P00749 UROK_HUMAN 179 423
SEQADV 1OWE GLN A 156 UNP P00749 ASN 322 CONFLICT
SEQRES 1 A 245 ILE ILE GLY GLY GLU PHE THR THR ILE GLU ASN GLN PRO
SEQRES 2 A 245 TRP PHE ALA ALA ILE TYR ARG ARG HIS ARG GLY GLY SER
SEQRES 3 A 245 VAL THR TYR VAL CYS GLY GLY SER LEU MET SER PRO CYS
SEQRES 4 A 245 TRP VAL ILE SER ALA THR HIS CYS PHE ILE ASP TYR PRO
SEQRES 5 A 245 LYS LYS GLU ASP TYR ILE VAL TYR LEU GLY ARG SER ARG
SEQRES 6 A 245 LEU ASN SER ASN THR GLN GLY GLU MET LYS PHE GLU VAL
SEQRES 7 A 245 GLU ASN LEU ILE LEU HIS LYS ASP TYR SER ALA ASP THR
SEQRES 8 A 245 LEU ALA HIS HIS ASN ASP ILE ALA LEU LEU LYS ILE ARG
SEQRES 9 A 245 SER LYS GLU GLY ARG CYS ALA GLN PRO SER ARG THR ILE
SEQRES 10 A 245 GLN THR ILE CYS LEU PRO SER MET TYR ASN ASP PRO GLN
SEQRES 11 A 245 PHE GLY THR SER CYS GLU ILE THR GLY PHE GLY LYS GLU
SEQRES 12 A 245 GLN SER THR ASP TYR LEU TYR PRO GLU GLN LEU LYS MET
SEQRES 13 A 245 THR VAL VAL LYS LEU ILE SER HIS ARG GLU CYS GLN GLN
SEQRES 14 A 245 PRO HIS TYR TYR GLY SER GLU VAL THR THR LYS MET LEU
SEQRES 15 A 245 CYS ALA ALA ASP PRO GLN TRP LYS THR ASP SER CYS GLN
SEQRES 16 A 245 GLY ASP SER GLY GLY PRO LEU VAL CYS SER LEU GLN GLY
SEQRES 17 A 245 ARG MET THR LEU THR GLY ILE VAL SER TRP GLY ARG GLY
SEQRES 18 A 245 CYS ALA LEU LYS ASP LYS PRO GLY VAL TYR THR ARG VAL
SEQRES 19 A 245 SER HIS PHE LEU PRO TRP ILE ARG SER HIS THR
HET SO4 A 301 5
HET SO4 A 302 5
HET SO4 A 303 5
HET 675 A1001 22
HETNAM SO4 SULFATE ION
HETNAM 675 6-[(Z)-AMINO(IMINO)METHYL]-N-PHENYL-2-NAPHTHAMIDE
HETSYN 675 6-(N-PHENYLCARBAMYL)-2-NAPHTHALENECARBOXAMIDINE
FORMUL 2 SO4 3(O4 S 2-)
FORMUL 5 675 C18 H15 N3 O
FORMUL 6 HOH *223(H2 O)
HELIX 1 1 THR A 8 GLN A 12 5 5
HELIX 2 2 ALA A 52 PHE A 56 5 5
HELIX 3 3 LYS A 61 GLU A 63 5 3
HELIX 4 4 SER A 176 GLN A 181 1 6
HELIX 5 5 TYR A 186 VAL A 190 5 5
HELIX 6 6 PHE A 250 THR A 258 1 9
SHEET 1 A 8 GLU A 5 PHE A 6 0
SHEET 2 A 8 LYS A 168 ILE A 175 -1 O MET A 169 N GLU A 5
SHEET 3 A 8 SER A 146 GLY A 151 -1 N CYS A 147 O VAL A 172
SHEET 4 A 8 PRO A 214 LEU A 219 -1 O PRO A 214 N THR A 150
SHEET 5 A 8 ARG A 222 TRP A 231 -1 O ARG A 222 N LEU A 219
SHEET 6 A 8 GLY A 242 ARG A 246 -1 N VAL A 243 O TRP A 231
SHEET 7 A 8 MET A 194 ALA A 198 -1 N LEU A 195 O TYR A 244
SHEET 8 A 8 LYS A 168 ILE A 175 -1 N LYS A 173 O ALA A 198
SHEET 1 B 7 PHE A 15 ARG A 21 0
SHEET 2 B 7 VAL A 29 SER A 43 -1 O THR A 30 N ARG A 20
SHEET 3 B 7 TRP A 48 SER A 51 -1 O TRP A 48 N MET A 41
SHEET 4 B 7 ALA A 111 ARG A 116 -1 O ALA A 111 N SER A 51
SHEET 5 B 7 MET A 86 LEU A 95 -1 O GLU A 89 N ARG A 116
SHEET 6 B 7 TYR A 67 LEU A 71 -1 O VAL A 69 N PHE A 88
SHEET 7 B 7 PHE A 15 ARG A 21 -1 O ALA A 17 N TYR A 70
SHEET 1 C 2 SER A 100 ALA A 101 0
SHEET 2 C 2 HIS A 106 HIS A 107 -1 N HIS A 107 O SER A 100
SSBOND 1 CYS A 34 CYS A 55 1555 1555 2.28
SSBOND 2 CYS A 147 CYS A 217 1555 1555 2.19
SSBOND 3 CYS A 180 CYS A 196 1555 1555 2.17
SSBOND 4 CYS A 207 CYS A 235 1555 1555 2.24
SITE 1 AC1 6 LYS A 61 HIS A 107 THR A 191 LYS A 193
SITE 2 AC1 6 MET A 194 HOH A1028
SITE 1 AC2 8 VAL A 32 CYS A 34 HIS A 54 GLN A 208
SITE 2 AC2 8 GLY A 209 SER A 211 675 A1001 HOH A1150
SITE 1 AC3 3 TYR A 138 ARG A 246 HIS A 249
SITE 1 AC4 11 HIS A 54 HIS A 106 ASP A 205 SER A 206
SITE 2 AC4 11 GLN A 208 SER A 211 TRP A 231 GLY A 234
SITE 3 AC4 11 GLY A 242 SO4 A 302 HOH A1024
CRYST1 55.160 53.000 82.300 90.00 90.00 90.00 P 21 21 21 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 0.018129 0.000000 0.000000 0.00000
SCALE2 0.000000 0.018868 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012151 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
