HEADER HYDROLASE/HYDROLASE INHIBITOR 28-JUN-12 4FUE
TITLE CRYSTAL STRUCTURE OF THE UROKINASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UROKINASE-TYPE PLASMINOGEN ACTIVATOR;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: U-PLASMINOGEN ACTIVATOR, UPA, UROKINASE-TYPE PLASMINOGEN
COMPND 5 ACTIVATOR LONG CHAIN A, UROKINASE-TYPE PLASMINOGEN ACTIVATOR SHORT
COMPND 6 CHAIN A, UROKINASE-TYPE PLASMINOGEN ACTIVATOR CHAIN B;
COMPND 7 EC: 3.4.21.73;
COMPND 8 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: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HYDROLASE, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.N.KANG,J.A.STUCKEY,V.NIENABER,V.GIRANDA
REVDAT 1 22-AUG-12 4FUE 0
JRNL AUTH Y.N.KANG,J.A.STUCKEY,V.NIENABER,V.GIRANDA
JRNL TITL CRYSTAL STRUCTURE OF THE UROKINASE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.00 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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.67
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.1
REMARK 3 NUMBER OF REFLECTIONS : 15981
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) : 0.159
REMARK 3 R VALUE (WORKING SET) : 0.158
REMARK 3 FREE R VALUE : 0.190
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.160
REMARK 3 FREE R VALUE TEST SET COUNT : 825
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 : 8
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.14
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.08
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2904
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.1862
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2753
REMARK 3 BIN R VALUE (WORKING SET) : 0.1849
REMARK 3 BIN FREE R VALUE : 0.2094
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.20
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 151
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 : 1936
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 69
REMARK 3 SOLVENT ATOMS : 310
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 16.57
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.37
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.95700
REMARK 3 B22 (A**2) : -0.43460
REMARK 3 B33 (A**2) : -1.52240
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 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.19
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
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 : 0.947
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.933
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 2134 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 2913 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 980 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 46 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 352 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 2134 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 270 ; 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 : 2608 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.04
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.74
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 2.68
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 4FUE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-JUL-12.
REMARK 100 THE RCSB ID CODE IS RCSB073367.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 160
REMARK 200 PH : 4.8-6.0
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) : 1.5418
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 : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15981
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 27.670
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.2
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.83
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.15 M LI2SO4, 20% POLYETHYLENE GLYCOL
REMARK 280 MW 4000 IN SUCCINATE BUFFER, PH 4.8-6.0, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 298.0K
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 27.35000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 40.12500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 26.70000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 40.12500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.35000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 26.70000
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 ARG A 209 CG CD NE CZ NH1 NH2
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 SER A 43 -158.78 -147.41
REMARK 500 TYR A 172 -109.94 -88.41
REMARK 500 SER A 217 -62.06 -120.18
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 A 678 DISTANCE = 5.61 ANGSTROMS
REMARK 525 HOH A 697 DISTANCE = 6.30 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 7UP A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SIN 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 SO4 A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 308
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 309
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4FU7 RELATED DB: PDB
REMARK 900 RELATED ID: 4FU8 RELATED DB: PDB
REMARK 900 RELATED ID: 4FU9 RELATED DB: PDB
REMARK 900 RELATED ID: 4FUB RELATED DB: PDB
REMARK 900 RELATED ID: 4FUC RELATED DB: PDB
REMARK 900 RELATED ID: 4FUD RELATED DB: PDB
REMARK 900 RELATED ID: 4FUF RELATED DB: PDB
REMARK 900 RELATED ID: 4FUG RELATED DB: PDB
REMARK 900 RELATED ID: 4FUH RELATED DB: PDB
REMARK 900 RELATED ID: 4FUI RELATED DB: PDB
REMARK 900 RELATED ID: 4FUJ RELATED DB: PDB
DBREF 4FUE A 1 246 UNP P00749 UROK_HUMAN 179 424
SEQADV 4FUE ALA A 121 UNP P00749 CYS 299 ENGINEERED MUTATION
SEQADV 4FUE GLN A 144 UNP P00749 ASN 322 ENGINEERED MUTATION
SEQRES 1 A 246 ILE ILE GLY GLY GLU PHE THR THR ILE GLU ASN GLN PRO
SEQRES 2 A 246 TRP PHE ALA ALA ILE TYR ARG ARG HIS ARG GLY GLY SER
SEQRES 3 A 246 VAL THR TYR VAL CYS GLY GLY SER LEU ILE SER PRO CYS
SEQRES 4 A 246 TRP VAL ILE SER ALA THR HIS CYS PHE ILE ASP TYR PRO
SEQRES 5 A 246 LYS LYS GLU ASP TYR ILE VAL TYR LEU GLY ARG SER ARG
SEQRES 6 A 246 LEU ASN SER ASN THR GLN GLY GLU MET LYS PHE GLU VAL
SEQRES 7 A 246 GLU ASN LEU ILE LEU HIS LYS ASP TYR SER ALA ASP THR
SEQRES 8 A 246 LEU ALA HIS HIS ASN ASP ILE ALA LEU LEU LYS ILE ARG
SEQRES 9 A 246 SER LYS GLU GLY ARG CYS ALA GLN PRO SER ARG THR ILE
SEQRES 10 A 246 GLN THR ILE ALA LEU PRO SER MET TYR ASN ASP PRO GLN
SEQRES 11 A 246 PHE GLY THR SER CYS GLU ILE THR GLY PHE GLY LYS GLU
SEQRES 12 A 246 GLN SER THR ASP TYR LEU TYR PRO GLU GLN LEU LYS MET
SEQRES 13 A 246 THR VAL VAL LYS LEU ILE SER HIS ARG GLU CYS GLN GLN
SEQRES 14 A 246 PRO HIS TYR TYR GLY SER GLU VAL THR THR LYS MET LEU
SEQRES 15 A 246 CYS ALA ALA ASP PRO GLN TRP LYS THR ASP SER CYS GLN
SEQRES 16 A 246 GLY ASP SER GLY GLY PRO LEU VAL CYS SER LEU GLN GLY
SEQRES 17 A 246 ARG MET THR LEU THR GLY ILE VAL SER TRP GLY ARG GLY
SEQRES 18 A 246 CYS ALA LEU LYS ASP LYS PRO GLY VAL TYR THR ARG VAL
SEQRES 19 A 246 SER HIS PHE LEU PRO TRP ILE ARG SER HIS THR LYS
HET 7UP A 301 44
HET SIN A 302 8
HET SO4 A 303 5
HET SO4 A 304 5
HET GOL A 305 6
HET GOL A 306 6
HET GOL A 307 6
HET ACT A 308 4
HET ACT A 309 4
HETNAM 7UP 6-(1,2,3,4-TETRAHYDROISOQUINOLIN-6-YLETHYNYL)
HETNAM 2 7UP NAPHTHALENE-2-CARBOXIMIDAMIDE
HETNAM SIN SUCCINIC ACID
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
HETNAM ACT ACETATE ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 7UP C22 H19 N3
FORMUL 3 SIN C4 H6 O4
FORMUL 4 SO4 2(O4 S 2-)
FORMUL 6 GOL 3(C3 H8 O3)
FORMUL 9 ACT 2(C2 H3 O2 1-)
FORMUL 11 HOH *310(H2 O)
HELIX 1 1 THR A 8 GLN A 12 5 5
HELIX 2 2 ALA A 44 PHE A 48 5 5
HELIX 3 3 LYS A 53 GLU A 55 5 3
HELIX 4 4 SER A 163 GLN A 168 1 6
HELIX 5 5 TYR A 173 VAL A 177 5 5
HELIX 6 6 PHE A 237 LYS A 246 1 10
SHEET 1 A 8 GLU A 5 PHE A 6 0
SHEET 2 A 8 LYS A 155 ILE A 162 -1 O MET A 156 N GLU A 5
SHEET 3 A 8 MET A 181 ALA A 185 -1 O CYS A 183 N ILE A 162
SHEET 4 A 8 GLY A 229 ARG A 233 -1 O TYR A 231 N LEU A 182
SHEET 5 A 8 ARG A 209 TRP A 218 -1 N TRP A 218 O VAL A 230
SHEET 6 A 8 PRO A 201 LEU A 206 -1 N LEU A 206 O ARG A 209
SHEET 7 A 8 SER A 134 GLY A 139 -1 N GLU A 136 O VAL A 203
SHEET 8 A 8 LYS A 155 ILE A 162 -1 O VAL A 159 N CYS A 135
SHEET 1 B 7 PHE A 15 ARG A 21 0
SHEET 2 B 7 VAL A 27 SER A 37 -1 O VAL A 30 N ILE A 18
SHEET 3 B 7 TRP A 40 SER A 43 -1 O ILE A 42 N SER A 34
SHEET 4 B 7 ALA A 99 ARG A 104 -1 O LEU A 101 N VAL A 41
SHEET 5 B 7 MET A 74 LEU A 83 -1 N ILE A 82 O LEU A 100
SHEET 6 B 7 TYR A 57 LEU A 61 -1 N VAL A 59 O PHE A 76
SHEET 7 B 7 PHE A 15 ARG A 21 -1 N TYR A 19 O ILE A 58
SHEET 1 C 2 SER A 88 ALA A 89 0
SHEET 2 C 2 HIS A 94 HIS A 95 -1 O HIS A 95 N SER A 88
SSBOND 1 CYS A 31 CYS A 47 1555 1555 2.04
SSBOND 2 CYS A 39 CYS A 110 1555 1555 2.03
SSBOND 3 CYS A 135 CYS A 204 1555 1555 2.04
SSBOND 4 CYS A 167 CYS A 183 1555 1555 2.03
SSBOND 5 CYS A 194 CYS A 222 1555 1555 2.04
SITE 1 AC1 10 HIS A 46 ASP A 50 ASP A 192 SER A 193
SITE 2 AC1 10 GLN A 195 SER A 198 TRP A 218 GLY A 221
SITE 3 AC1 10 GLY A 229 SIN A 302
SITE 1 AC2 8 VAL A 30 HIS A 46 CYS A 47 GLN A 195
SITE 2 AC2 8 GLY A 196 SER A 198 7UP A 301 HOH A 686
SITE 1 AC3 9 ARG A 23 LYS A 53 HIS A 95 THR A 178
SITE 2 AC3 9 LYS A 180 MET A 181 HOH A 425 HOH A 516
SITE 3 AC3 9 HOH A 598
SITE 1 AC4 4 TYR A 126 ARG A 233 HIS A 236 HOH A 633
SITE 1 AC5 7 THR A 28 TYR A 29 TYR A 150 HOH A 408
SITE 2 AC5 7 HOH A 422 HOH A 423 HOH A 663
SITE 1 AC6 8 VAL A 27 TYR A 60 ARG A 63 LEU A 66
SITE 2 AC6 8 ASN A 67 HOH A 489 HOH A 571 HOH A 661
SITE 1 AC7 5 ARG A 20 HIS A 22 ARG A 23 TYR A 51
SITE 2 AC7 5 HOH A 664
SITE 1 AC8 5 THR A 178 THR A 179 HOH A 485 HOH A 515
SITE 2 AC8 5 HOH A 583
SITE 1 AC9 5 PRO A 52 LEU A 81 THR A 91 HOH A 483
SITE 2 AC9 5 HOH A 521
CRYST1 54.700 53.400 80.250 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 0.018282 0.000000 0.000000 0.00000
SCALE2 0.000000 0.018727 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012461 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
