HEADER TRANSFERASE 12-AUG-03 1Q66
TITLE CRYSTAL STRUCTURE OF TGT IN COMPLEX WITH 2-AMINO-6-AMINOMETHYL-8-
TITLE 2 PHENYLSULFANYLMETHYL-3H-QUINAZOLIN-4-ONE CRYSTALLIZED AT PH 5.5
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: QUEUINE TRNA-RIBOSYLTRANSFERASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: TRNA-GUANINE TRANSGLYCOSYLASE, GUANINE INSERTION ENZYME,
COMPND 5 TGT;
COMPND 6 EC: 2.4.2.29;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ZYMOMONAS MOBILIS;
SOURCE 3 ORGANISM_TAXID: 542;
SOURCE 4 GENE: TGT;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET9D
KEYWDS TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.BRENK,E.MEYER,K.REUTER,M.T.STUBBS,G.A.GARCIA,G.KLEBE
REVDAT 5 16-AUG-23 1Q66 1 REMARK
REVDAT 4 19-AUG-20 1Q66 1 REMARK LINK
REVDAT 3 13-JUL-11 1Q66 1 VERSN
REVDAT 2 24-FEB-09 1Q66 1 VERSN
REVDAT 1 13-APR-04 1Q66 0
JRNL AUTH R.BRENK,E.MEYER,K.REUTER,M.T.STUBBS,G.A.GARCIA,F.DIEDERICH,
JRNL AUTH 2 G.KLEBE
JRNL TITL CRYSTALLOGRAPHIC STUDY OF INHIBITORS OF TRNA-GUANINE
JRNL TITL 2 TRANSGLYCOSYLASE SUGGESTS A NEW STRUCTURE-BASED
JRNL TITL 3 PHARMACOPHORE FOR VIRTUAL SCREENING.
JRNL REF J.MOL.BIOL. V. 338 55 2004
JRNL REFN ISSN 0022-2836
JRNL PMID 15050823
JRNL DOI 10.1016/J.JMB.2004.02.019
REMARK 2
REMARK 2 RESOLUTION. 1.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 646321.680
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 92.6
REMARK 3 NUMBER OF REFLECTIONS : 38127
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) : 0.189
REMARK 3 FREE R VALUE : 0.210
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3857
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.003
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) : 1.75
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.86
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 86.80
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 5326
REMARK 3 BIN R VALUE (WORKING SET) : 0.2670
REMARK 3 BIN FREE R VALUE : 0.3070
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.90
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 586
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.013
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2845
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 23
REMARK 3 SOLVENT ATOMS : 374
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 23.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.50
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.05000
REMARK 3 B22 (A**2) : -3.51000
REMARK 3 B33 (A**2) : 2.46000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.92000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.19
REMARK 3 ESD FROM SIGMAA (A) : 0.11
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) : 0.14
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.100
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.70
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.750
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) : 1.320 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.060 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.890 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.770 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.38
REMARK 3 BSOL : 65.57
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 : DNA-RNA_REP.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : 247_FRAG_2.PARAM
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : DNA-RNA.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : 247_FRAG_2.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1Q66 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-AUG-03.
REMARK 100 THE DEPOSITION ID IS D_1000019965.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-JUL-01
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 5.50
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) : 1.54
REMARK 200 MONOCHROMATOR : YALE MIRROR
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 : 38581
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.9
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04300
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) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.83
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.5
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.21300
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: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1PUD
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.89
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, TRIS, DMSO, DTT, PH 5.50,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K
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 45.70000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 32.54500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 45.70000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 32.54500
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4670 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26430 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL
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 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 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 MET A 1
REMARK 465 VAL A 2
REMARK 465 GLU A 3
REMARK 465 ALA A 4
REMARK 465 THR A 5
REMARK 465 ALA A 6
REMARK 465 GLN A 7
REMARK 465 GLU A 8
REMARK 465 THR A 9
REMARK 465 ASP A 10
REMARK 465 SER A 112
REMARK 465 SER A 113
REMARK 465 LEU A 114
REMARK 465 ASP A 129
REMARK 465 GLY A 130
REMARK 465 ARG A 286
REMARK 465 SER A 287
REMARK 465 GLY A 288
REMARK 465 ALA A 383
REMARK 465 ARG A 384
REMARK 465 ASN A 385
REMARK 465 SER A 386
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 GLN A 107 CG CD OE1 NE2
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 ASN A 70 CG OD1 ND2
REMARK 480 SER A 110 OG
REMARK 480 LYS A 116 CA CB CG CD CE NZ
REMARK 480 LYS A 125 CG CD CE NZ
REMARK 480 HIS A 127 CA CB
REMARK 480 ARG A 132 CB CG CD NE CZ NH1 NH2
REMARK 480 ARG A 167 NE CZ NH1 NH2
REMARK 480 LYS A 264 CG CD CE NZ
REMARK 480 LEU A 283 CA C O CB
REMARK 480 ARG A 289 CB CG CD NE CZ NH1 NH2
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 C13 KMB A 900 O HOH A 1384 1.34
REMARK 500 C13 KMB A 900 O HOH A 1384 1.44
REMARK 500 C12 KMB A 900 O HOH A 1384 1.74
REMARK 500 C12 KMB A 900 O HOH A 1384 1.85
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 ALA A 48 61.20 -113.19
REMARK 500 LYS A 52 114.61 -29.68
REMARK 500 MET A 109 41.82 -89.63
REMARK 500 SER A 110 -34.41 -158.94
REMARK 500 GLN A 203 -168.56 -125.13
REMARK 500 SER A 205 -132.26 55.11
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 A1215 DISTANCE = 7.13 ANGSTROMS
REMARK 525 HOH A1240 DISTANCE = 7.30 ANGSTROMS
REMARK 525 HOH A1299 DISTANCE = 6.82 ANGSTROMS
REMARK 525 HOH A1304 DISTANCE = 7.06 ANGSTROMS
REMARK 525 HOH A1309 DISTANCE = 6.68 ANGSTROMS
REMARK 525 HOH A1319 DISTANCE = 6.56 ANGSTROMS
REMARK 525 HOH A1335 DISTANCE = 7.32 ANGSTROMS
REMARK 525 HOH A1336 DISTANCE = 8.43 ANGSTROMS
REMARK 525 HOH A1338 DISTANCE = 6.44 ANGSTROMS
REMARK 525 HOH A1345 DISTANCE = 7.30 ANGSTROMS
REMARK 525 HOH A1346 DISTANCE = 7.21 ANGSTROMS
REMARK 525 HOH A1372 DISTANCE = 9.77 ANGSTROMS
REMARK 525 HOH A1387 DISTANCE = 9.18 ANGSTROMS
REMARK 615
REMARK 615 ZERO OCCUPANCY ATOM
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 615 M RES C SSEQI
REMARK 615 KMB A 900
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 ZN A 400 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 318 SG
REMARK 620 2 CYS A 320 SG 105.1
REMARK 620 3 CYS A 323 SG 113.2 117.3
REMARK 620 4 HIS A 349 ND1 106.0 114.8 100.1
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE KMB A 900
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1PUD RELATED DB: PDB
REMARK 900 TRNA-GUANINE TRANSGLYCOSYLASE
REMARK 900 RELATED ID: 1Q4W RELATED DB: PDB
REMARK 900 CORE STRUCTURE OF 2-AMINO-6-AMINOMETHYL-8-PHENYLSULFANYLMETHYL-3H-
REMARK 900 QUINAZOLIN-4-ONE IN COMPLEX WITH TGT, CRYSTALLIZED AT PH 8.5
REMARK 900 RELATED ID: 1Q63 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF TGT IN COMPLEX WITH 2,6-DIAMINO-8-(1H-IMIDAZOL-
REMARK 900 2-YLSULFANYLMETHYL)-3H-QUINAZOLINE-4-ONE CRYSTALLIZED AT PH 5.5
REMARK 900 RELATED ID: 1Q65 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF TGT IN COMPLEX WITH 2,6-DIAMINO-8-(2-
REMARK 900 DIMETHYLAMINOETHYLSULFANYLMETHYL)-3H-QUINAZOLIN-4-ONE CRYSTALLIZED
REMARK 900 AT PH 5.5
DBREF 1Q66 A 1 386 UNP P28720 TGT_ZYMMO 0 385
SEQRES 1 A 386 MET VAL GLU ALA THR ALA GLN GLU THR ASP ARG PRO ARG
SEQRES 2 A 386 PHE SER PHE SER ILE ALA ALA ARG GLU GLY LYS ALA ARG
SEQRES 3 A 386 THR GLY THR ILE GLU MET LYS ARG GLY VAL ILE ARG THR
SEQRES 4 A 386 PRO ALA PHE MET PRO VAL GLY THR ALA ALA THR VAL LYS
SEQRES 5 A 386 ALA LEU LYS PRO GLU THR VAL ARG ALA THR GLY ALA ASP
SEQRES 6 A 386 ILE ILE LEU GLY ASN THR TYR HIS LEU MET LEU ARG PRO
SEQRES 7 A 386 GLY ALA GLU ARG ILE ALA LYS LEU GLY GLY LEU HIS SER
SEQRES 8 A 386 PHE MET GLY TRP ASP ARG PRO ILE LEU THR ASP SER GLY
SEQRES 9 A 386 GLY TYR GLN VAL MET SER LEU SER SER LEU THR LYS GLN
SEQRES 10 A 386 SER GLU GLU GLY VAL THR PHE LYS SER HIS LEU ASP GLY
SEQRES 11 A 386 SER ARG HIS MET LEU SER PRO GLU ARG SER ILE GLU ILE
SEQRES 12 A 386 GLN HIS LEU LEU GLY SER ASP ILE VAL MET ALA PHE ASP
SEQRES 13 A 386 GLU CYS THR PRO TYR PRO ALA THR PRO SER ARG ALA ALA
SEQRES 14 A 386 SER SER MET GLU ARG SER MET ARG TRP ALA LYS ARG SER
SEQRES 15 A 386 ARG ASP ALA PHE ASP SER ARG LYS GLU GLN ALA GLU ASN
SEQRES 16 A 386 ALA ALA LEU PHE GLY ILE GLN GLN GLY SER VAL PHE GLU
SEQRES 17 A 386 ASN LEU ARG GLN GLN SER ALA ASP ALA LEU ALA GLU ILE
SEQRES 18 A 386 GLY PHE ASP GLY TYR ALA VAL GLY GLY LEU ALA VAL GLY
SEQRES 19 A 386 GLU GLY GLN ASP GLU MET PHE ARG VAL LEU ASP PHE SER
SEQRES 20 A 386 VAL PRO MET LEU PRO ASP ASP LYS PRO HIS TYR LEU MET
SEQRES 21 A 386 GLY VAL GLY LYS PRO ASP ASP ILE VAL GLY ALA VAL GLU
SEQRES 22 A 386 ARG GLY ILE ASP MET PHE ASP CYS VAL LEU PRO THR ARG
SEQRES 23 A 386 SER GLY ARG ASN GLY GLN ALA PHE THR TRP ASP GLY PRO
SEQRES 24 A 386 ILE ASN ILE ARG ASN ALA ARG PHE SER GLU ASP LEU LYS
SEQRES 25 A 386 PRO LEU ASP SER GLU CYS HIS CYS ALA VAL CYS GLN LYS
SEQRES 26 A 386 TRP SER ARG ALA TYR ILE HIS HIS LEU ILE ARG ALA GLY
SEQRES 27 A 386 GLU ILE LEU GLY ALA MET LEU MET THR GLU HIS ASN ILE
SEQRES 28 A 386 ALA PHE TYR GLN GLN LEU MET GLN LYS ILE ARG ASP SER
SEQRES 29 A 386 ILE SER GLU GLY ARG PHE SER GLN PHE ALA GLN ASP PHE
SEQRES 30 A 386 ARG ALA ARG TYR PHE ALA ARG ASN SER
HET ZN A 400 1
HET KMB A 900 44
HETNAM ZN ZINC ION
HETNAM KMB 2-AMINO-6-AMINOMETHYL-8-PHENYLSULFANYLMETHYL-3H-
HETNAM 2 KMB QUINAZOLIN-4-ONE
FORMUL 2 ZN ZN 2+
FORMUL 3 KMB C16 H16 N4 O S
FORMUL 4 HOH *374(H2 O)
HELIX 1 1 LYS A 55 THR A 62 1 8
HELIX 2 2 ASN A 70 ARG A 77 1 8
HELIX 3 3 GLY A 79 LEU A 86 1 8
HELIX 4 4 GLY A 88 GLY A 94 1 7
HELIX 5 5 GLY A 104 MET A 109 1 6
HELIX 6 6 SER A 136 GLY A 148 1 13
HELIX 7 7 THR A 164 SER A 188 1 25
HELIX 8 8 ARG A 189 ALA A 196 1 8
HELIX 9 9 PHE A 207 GLY A 222 1 16
HELIX 10 10 GLY A 236 VAL A 248 1 13
HELIX 11 11 PRO A 249 LEU A 251 5 3
HELIX 12 12 LYS A 264 GLU A 273 1 10
HELIX 13 13 ASN A 304 SER A 308 5 5
HELIX 14 14 CYS A 320 TRP A 326 1 7
HELIX 15 15 SER A 327 GLY A 338 1 12
HELIX 16 16 GLU A 339 GLU A 367 1 29
HELIX 17 17 ARG A 369 PHE A 382 1 14
SHEET 1 A 3 PHE A 14 GLU A 22 0
SHEET 2 A 3 ALA A 25 MET A 32 -1 O GLU A 31 N SER A 15
SHEET 3 A 3 GLY A 35 THR A 39 -1 O ILE A 37 N ILE A 30
SHEET 1 B 9 ALA A 41 GLY A 46 0
SHEET 2 B 9 ILE A 67 GLY A 69 1 O LEU A 68 N GLY A 46
SHEET 3 B 9 ILE A 99 THR A 101 1 O LEU A 100 N GLY A 69
SHEET 4 B 9 ILE A 151 MET A 153 1 O ILE A 151 N THR A 101
SHEET 5 B 9 ALA A 197 GLN A 202 1 O ALA A 197 N VAL A 152
SHEET 6 B 9 GLY A 225 VAL A 228 1 O ALA A 227 N GLN A 202
SHEET 7 B 9 HIS A 257 LEU A 259 1 O TYR A 258 N VAL A 228
SHEET 8 B 9 MET A 278 CYS A 281 1 O MET A 278 N LEU A 259
SHEET 9 B 9 ALA A 41 GLY A 46 1 N MET A 43 O PHE A 279
SHEET 1 C 3 LYS A 116 SER A 118 0
SHEET 2 C 3 GLY A 121 LYS A 125 -1 O GLY A 121 N SER A 118
SHEET 3 C 3 ARG A 132 LEU A 135 -1 O LEU A 135 N VAL A 122
SHEET 1 D 2 GLN A 292 ALA A 293 0
SHEET 2 D 2 ILE A 300 ASN A 301 -1 O ILE A 300 N ALA A 293
LINK SG CYS A 318 ZN ZN A 400 1555 1555 2.32
LINK SG CYS A 320 ZN ZN A 400 1555 1555 2.29
LINK SG CYS A 323 ZN ZN A 400 1555 1555 2.29
LINK ND1 HIS A 349 ZN ZN A 400 1555 1555 2.16
CISPEP 1 THR A 39 PRO A 40 0 -0.13
CISPEP 2 ARG A 77 PRO A 78 0 0.28
CISPEP 3 TYR A 161 PRO A 162 0 -0.02
SITE 1 AC1 4 CYS A 318 CYS A 320 CYS A 323 HIS A 349
SITE 1 AC2 10 ASP A 102 TYR A 106 ASP A 156 ILE A 201
SITE 2 AC2 10 GLN A 203 GLY A 229 GLY A 230 LEU A 231
SITE 3 AC2 10 ALA A 232 MET A 260
CRYST1 91.400 65.090 69.850 90.00 95.85 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 0.010941 0.000000 0.001121 0.00000
SCALE2 0.000000 0.015363 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014391 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
