HEADER TRANSFERASE/TRANSFERASE INHIBITOR 14-JUN-13 4L7O
TITLE HUMAN ARTD3 (PARP3) - CATALYTIC DOMAIN IN COMPLEX WITH INHIBITOR
TITLE 2 STO1542
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLY [ADP-RIBOSE] POLYMERASE 3;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CATALYTIC PARP DOMAIN;
COMPND 5 SYNONYM: PARP-3, HPARP-3, ADP-RIBOSYLTRANSFERASE DIPHTHERIA TOXIN-
COMPND 6 LIKE 3, ARTD3, IRT1, NAD(+) ADP-RIBOSYLTRANSFERASE 3, ADPRT-3,
COMPND 7 POLY[ADP-RIBOSE] SYNTHASE 3, PADPRT-3;
COMPND 8 EC: 2.4.2.30;
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 GENE: ADPRT3, ADPRTL3, PARP3;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3) R3 PRARE;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PNIC-BSA4
KEYWDS DIPHTHERIA TOXIN LIKE ADP-RIBOSE TRANSFERASE, TRANSFERASE, ADP-
KEYWDS 2 RIBOSYLATION, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR T.KARLBERG,A.G.THORSELL,A.E.G.LINDGREN,T.EKBLAD,S.SPJUT,
AUTHOR 2 C.D.ANDERSSON,J.WEIGELT,A.LINUSSON,M.ELOFSSON,H.SCHULER
REVDAT 2 20-SEP-23 4L7O 1 REMARK SEQADV
REVDAT 1 19-FEB-14 4L7O 0
JRNL AUTH A.E.LINDGREN,T.KARLBERG,T.EKBLAD,S.SPJUT,A.G.THORSELL,
JRNL AUTH 2 C.D.ANDERSSON,T.T.NHAN,V.HELLSTEN,J.WEIGELT,A.LINUSSON,
JRNL AUTH 3 H.SCHULER,M.ELOFSSON
JRNL TITL CHEMICAL PROBES TO STUDY ADP-RIBOSYLATION: SYNTHESIS AND
JRNL TITL 2 BIOCHEMICAL EVALUATION OF INHIBITORS OF THE HUMAN
JRNL TITL 3 ADP-RIBOSYLTRANSFERASE ARTD3/PARP3.
JRNL REF J.MED.CHEM. V. 56 9556 2013
JRNL REFN ISSN 0022-2623
JRNL PMID 24188023
JRNL DOI 10.1021/JM401394U
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.46
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 20793
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) : 0.165
REMARK 3 R VALUE (WORKING SET) : 0.163
REMARK 3 FREE R VALUE : 0.210
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1095
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1515
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.1960
REMARK 3 BIN FREE R VALUE SET COUNT : 80
REMARK 3 BIN FREE R VALUE : 0.2550
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2755
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 33
REMARK 3 SOLVENT ATOMS : 135
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.45
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.20000
REMARK 3 B22 (A**2) : -0.94000
REMARK 3 B33 (A**2) : -0.11000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.20000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.188
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.160
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.111
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.600
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.956
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.928
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2851 ; 0.019 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 1930 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3861 ; 1.677 ; 1.985
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4745 ; 0.980 ; 3.003
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 352 ; 6.318 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 127 ;40.713 ;25.276
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 492 ;14.364 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 11 ;18.257 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 422 ; 0.103 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3156 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 521 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1768 ; 1.036 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 709 ; 0.263 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2851 ; 1.876 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1083 ; 2.784 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1010 ; 4.556 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 176 A 532
REMARK 3 ORIGIN FOR THE GROUP (A): 18.5400 0.5750 11.9020
REMARK 3 T TENSOR
REMARK 3 T11: 0.0181 T22: 0.0111
REMARK 3 T33: 0.0081 T12: 0.0019
REMARK 3 T13: 0.0081 T23: 0.0008
REMARK 3 L TENSOR
REMARK 3 L11: 0.1308 L22: 0.2728
REMARK 3 L33: 0.1131 L12: -0.0092
REMARK 3 L13: -0.0201 L23: 0.0188
REMARK 3 S TENSOR
REMARK 3 S11: -0.0083 S12: -0.0091 S13: -0.0114
REMARK 3 S21: -0.0546 S22: 0.0010 S23: -0.0207
REMARK 3 S31: -0.0199 S32: 0.0009 S33: 0.0072
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4L7O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-JUN-13.
REMARK 100 THE DEPOSITION ID IS D_1000080284.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-JUL-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97950
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21888
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 7.400
REMARK 200 R MERGE (I) : 0.12600
REMARK 200 R SYM (I) : 0.12200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.9000
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) : 2.05
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : 7.50
REMARK 200 R MERGE FOR SHELL (I) : 0.67400
REMARK 200 R SYM FOR SHELL (I) : 0.47500
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 4GV4
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.02
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.05
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.8M DL-MALIC ACID, 0.1M BIS-TRIS
REMARK 280 -PROPANE , PH 7.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 28.45900
REMARK 290 SMTRY3 2 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: MONOMERIC
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 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 GLY A 242
REMARK 465 PRO A 243
REMARK 465 THR A 244
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 ASP A 245 CG OD1 OD2
REMARK 470 GLU A 251 CD OE1 OE2
REMARK 470 ARG A 351 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 375 CG CD CE NZ
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 478 108.50 -51.06
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 1VD A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 602
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4L6Z RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH STO1168.
REMARK 900 RELATED ID: 4L70 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH ME0352.
REMARK 900 RELATED ID: 4L7L RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH ME0368.
REMARK 900 RELATED ID: 4L7N RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH STO1541.
REMARK 900 RELATED ID: 4L7P RELATED DB: PDB
REMARK 900 RELATED ID: 4L7R RELATED DB: PDB
REMARK 900 RELATED ID: 4L7U RELATED DB: PDB
DBREF 4L7O A 178 532 UNP Q9Y6F1 PARP3_HUMAN 178 532
SEQADV 4L7O SER A 176 UNP Q9Y6F1 EXPRESSION TAG
SEQADV 4L7O MET A 177 UNP Q9Y6F1 EXPRESSION TAG
SEQRES 1 A 357 SER MET LYS ARG VAL GLN PRO CYS SER LEU ASP PRO ALA
SEQRES 2 A 357 THR GLN LYS LEU ILE THR ASN ILE PHE SER LYS GLU MET
SEQRES 3 A 357 PHE LYS ASN THR MET ALA LEU MET ASP LEU ASP VAL LYS
SEQRES 4 A 357 LYS MET PRO LEU GLY LYS LEU SER LYS GLN GLN ILE ALA
SEQRES 5 A 357 ARG GLY PHE GLU ALA LEU GLU ALA LEU GLU GLU ALA LEU
SEQRES 6 A 357 LYS GLY PRO THR ASP GLY GLY GLN SER LEU GLU GLU LEU
SEQRES 7 A 357 SER SER HIS PHE TYR THR VAL ILE PRO HIS ASN PHE GLY
SEQRES 8 A 357 HIS SER GLN PRO PRO PRO ILE ASN SER PRO GLU LEU LEU
SEQRES 9 A 357 GLN ALA LYS LYS ASP MET LEU LEU VAL LEU ALA ASP ILE
SEQRES 10 A 357 GLU LEU ALA GLN ALA LEU GLN ALA VAL SER GLU GLN GLU
SEQRES 11 A 357 LYS THR VAL GLU GLU VAL PRO HIS PRO LEU ASP ARG ASP
SEQRES 12 A 357 TYR GLN LEU LEU LYS CYS GLN LEU GLN LEU LEU ASP SER
SEQRES 13 A 357 GLY ALA PRO GLU TYR LYS VAL ILE GLN THR TYR LEU GLU
SEQRES 14 A 357 GLN THR GLY SER ASN HIS ARG CYS PRO THR LEU GLN HIS
SEQRES 15 A 357 ILE TRP LYS VAL ASN GLN GLU GLY GLU GLU ASP ARG PHE
SEQRES 16 A 357 GLN ALA HIS SER LYS LEU GLY ASN ARG LYS LEU LEU TRP
SEQRES 17 A 357 HIS GLY THR ASN MET ALA VAL VAL ALA ALA ILE LEU THR
SEQRES 18 A 357 SER GLY LEU ARG ILE MET PRO HIS SER GLY GLY ARG VAL
SEQRES 19 A 357 GLY LYS GLY ILE TYR PHE ALA SER GLU ASN SER LYS SER
SEQRES 20 A 357 ALA GLY TYR VAL ILE GLY MET LYS CYS GLY ALA HIS HIS
SEQRES 21 A 357 VAL GLY TYR MET PHE LEU GLY GLU VAL ALA LEU GLY ARG
SEQRES 22 A 357 GLU HIS HIS ILE ASN THR ASP ASN PRO SER LEU LYS SER
SEQRES 23 A 357 PRO PRO PRO GLY PHE ASP SER VAL ILE ALA ARG GLY HIS
SEQRES 24 A 357 THR GLU PRO ASP PRO THR GLN ASP THR GLU LEU GLU LEU
SEQRES 25 A 357 ASP GLY GLN GLN VAL VAL VAL PRO GLN GLY GLN PRO VAL
SEQRES 26 A 357 PRO CYS PRO GLU PHE SER SER SER THR PHE SER GLN SER
SEQRES 27 A 357 GLU TYR LEU ILE TYR GLN GLU SER GLN CYS ARG LEU ARG
SEQRES 28 A 357 TYR LEU LEU GLU VAL HIS
HET 1VD A 601 29
HET DMS A 602 4
HETNAM 1VD N-{(1S)-1-[4-(1H-IMIDAZOL-1-YL)PHENYL]ETHYL}-3-(4-OXO-
HETNAM 2 1VD 3,4-DIHYDROQUINAZOLIN-2-YL)PROPANAMIDE
HETNAM DMS DIMETHYL SULFOXIDE
FORMUL 2 1VD C22 H21 N5 O2
FORMUL 3 DMS C2 H6 O S
FORMUL 4 HOH *135(H2 O)
HELIX 1 1 ASP A 186 PHE A 197 1 12
HELIX 2 2 SER A 198 MET A 209 1 12
HELIX 3 3 PRO A 217 LEU A 221 5 5
HELIX 4 4 SER A 222 LYS A 241 1 20
HELIX 5 5 SER A 249 ILE A 261 1 13
HELIX 6 6 SER A 275 GLN A 299 1 25
HELIX 7 7 SER A 302 VAL A 308 1 7
HELIX 8 8 HIS A 313 LEU A 322 1 10
HELIX 9 9 GLU A 335 GLY A 347 1 13
HELIX 10 10 GLU A 366 HIS A 373 1 8
HELIX 11 11 SER A 374 LEU A 376 5 3
HELIX 12 12 ASN A 387 ALA A 389 5 3
HELIX 13 13 VAL A 390 GLY A 398 1 9
HELIX 14 14 GLU A 418 GLY A 424 1 7
HELIX 15 15 PRO A 479 ASP A 482 5 4
HELIX 16 16 PRO A 503 SER A 506 5 4
HELIX 17 17 GLN A 519 SER A 521 5 3
SHEET 1 A 2 ARG A 179 VAL A 180 0
SHEET 2 A 2 GLU A 310 VAL A 311 1 O VAL A 311 N ARG A 179
SHEET 1 B 5 GLN A 325 LEU A 328 0
SHEET 2 B 5 THR A 354 ASN A 362 -1 O LYS A 360 N GLN A 327
SHEET 3 B 5 CYS A 523 HIS A 532 -1 O LEU A 528 N TRP A 359
SHEET 4 B 5 HIS A 434 ALA A 445 -1 N GLU A 443 O ARG A 524
SHEET 5 B 5 ARG A 379 GLY A 385 -1 N HIS A 384 O PHE A 440
SHEET 1 C 5 GLN A 325 LEU A 328 0
SHEET 2 C 5 THR A 354 ASN A 362 -1 O LYS A 360 N GLN A 327
SHEET 3 C 5 CYS A 523 HIS A 532 -1 O LEU A 528 N TRP A 359
SHEET 4 C 5 HIS A 434 ALA A 445 -1 N GLU A 443 O ARG A 524
SHEET 5 C 5 MET A 429 CYS A 431 -1 N CYS A 431 O HIS A 434
SHEET 1 D 4 ILE A 413 PHE A 415 0
SHEET 2 D 4 GLU A 514 ILE A 517 -1 O ILE A 517 N ILE A 413
SHEET 3 D 4 SER A 468 ALA A 471 -1 N VAL A 469 O LEU A 516
SHEET 4 D 4 GLU A 449 ILE A 452 1 N HIS A 450 O ILE A 470
SHEET 1 E 2 THR A 475 PRO A 477 0
SHEET 2 E 2 PRO A 499 PRO A 501 -1 O VAL A 500 N GLU A 476
SHEET 1 F 2 THR A 483 LEU A 487 0
SHEET 2 F 2 GLN A 490 VAL A 494 -1 O VAL A 494 N THR A 483
SITE 1 AC1 13 ASP A 284 LEU A 287 ASP A 291 HIS A 384
SITE 2 AC1 13 GLY A 385 THR A 386 ARG A 400 MET A 402
SITE 3 AC1 13 TYR A 414 SER A 422 TYR A 425 GLU A 514
SITE 4 AC1 13 DMS A 602
SITE 1 AC2 4 GLY A 398 LEU A 399 ARG A 400 1VD A 601
CRYST1 54.519 56.918 56.840 90.00 112.43 90.00 P 1 21 1 2
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 0.018342 0.000000 0.007572 0.00000
SCALE2 0.000000 0.017569 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019034 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
