HEADER LIGASE (SYNTHETASE) 29-JUN-89 2TS1 2TS1 3 COMPND TYROSYL-TRANSFER /RNA$ SYNTHETASE (E.C.6.1.1.1) 2TS1 4 SOURCE (BACILLUS $STEAROTHERMOPHILUS /NCA$ 1503) 2TS1 5 AUTHOR P.BRICK,T.N.BHAT,D.M.BLOW 2TS1 6 REVDAT 2 15-JAN-90 2TS1A 1 SPRSDE 2TS1A 1 REVDAT 1 15-OCT-89 2TS1 0 2TS1 7 SPRSDE 15-JAN-90 2TS1 1TS1 2TS1A 2 JRNL AUTH P.BRICK,T.N.BHAT,D.M.BLOW 2TS1 8 JRNL TITL STRUCTURE OF TYROSYL-T/RNA$ SYNTHETASE REFINED AT 2TS1 9 JRNL TITL 2 2.3 ANGSTROMS RESOLUTION. INTERACTION OF THE ENZYME 2TS1 10 JRNL TITL 3 WITH THE TYROSYL ADENYLATE INTERMEDIATE 2TS1 11 JRNL REF J.MOL.BIOL. V. 208 83 1989 2TS1 12 JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 070 2TS1 13 REMARK 1 2TS1 14 REMARK 1 REFERENCE 1 2TS1 15 REMARK 1 AUTH P.BRICK,D.M.BLOW 2TS1 16 REMARK 1 TITL CRYSTAL STRUCTURE OF A DELETION MUTANT OF A 2TS1 17 REMARK 1 TITL 2 TYROSYL-T/RNA$ SYNTHETASE COMPLEXED WITH TYROSINE 2TS1 18 REMARK 1 REF J.MOL.BIOL. V. 194 287 1987 2TS1 19 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 2TS1 20 REMARK 1 REFERENCE 2 2TS1 21 REMARK 1 AUTH C.MONTEILHET,D.M.BLOW,P.BRICK 2TS1 22 REMARK 1 TITL INTERACTION OF CRYSTALLINE TYROSOL-T/RNA$ 2TS1 23 REMARK 1 TITL 2 SYNTHETASE WITH ADENOSINE, ADENOSINE MONOPHOSPHATE, 2TS1 24 REMARK 1 TITL 3 ADENOSINE TRIPHOSPHATE AND PYROPHOSPHATE IN THE 2TS1 25 REMARK 1 TITL 4 PRESENCE OF TYROSINOL 2TS1 26 REMARK 1 REF J.MOL.BIOL. V. 173 477 1984 2TS1 27 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 2TS1 28 REMARK 1 REFERENCE 3 2TS1 29 REMARK 1 AUTH T.N.BHAT,D.M.BLOW,P.BRICK,J.NYBORG 2TS1 30 REMARK 1 TITL TYROSYL-T/RNA$ SYNTHETASE FORMS A 2TS1 31 REMARK 1 TITL 2 MONONUCLEOTIDE-BINDING FOLD 2TS1 32 REMARK 1 REF J.MOL.BIOL. V. 158 699 1982 2TS1 33 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 2TS1 34 REMARK 1 REFERENCE 4 2TS1 35 REMARK 1 AUTH T.N.BHAT,D.M.BLOW 2TS1 36 REMARK 1 TITL A DENSITY-*MODIFICATION METHOD FOR THE IMPROVEMENT 2TS1 37 REMARK 1 TITL 2 OF POORLY RESOLVED PROTEIN ELECTRON-*DENSITY MAPS 2TS1 38 REMARK 1 REF ACTA CRYSTALLOGR.,SECT.A V. 38 21 1982 2TS1 39 REMARK 1 REFN ASTM ACACBN DK ISSN 0567-7394 108 2TS1 40 REMARK 1 REFERENCE 5 2TS1 41 REMARK 1 AUTH C.MONTEILHET,D.M.BLOW 2TS1 42 REMARK 1 TITL BINDING OF TYROSINE, ADENOSINE TRIPHOSPHATE AND 2TS1 43 REMARK 1 TITL 2 ANALOGUES TO CRYSTALLINE TYROSYL TRANSFER /RNA$ 2TS1 44 REMARK 1 TITL 3 SYNTHETASE 2TS1 45 REMARK 1 REF J.MOL.BIOL. V. 122 407 1978 2TS1 46 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 2TS1 47 REMARK 1 REFERENCE 6 2TS1 48 REMARK 1 AUTH D.M.BLOW,C.MONTEILHET,J.R.RUBIN 2TS1 49 REMARK 1 TITL STRUCTURE OF AMINOACYL $T/RNA$ SYNTHETASES 2TS1 50 REMARK 1 REF PROC./FEBS$ MEET. V. 52 59 1978 2TS1 51 REMARK 1 REFN ASTM FEBPBY UK ISSN 0071-4402 924 2TS1 52 REMARK 1 REFERENCE 7 2TS1 53 REMARK 1 AUTH D.M.BLOW,M.J.IRWIN,J.NYBORG 2TS1 54 REMARK 1 TITL THE PEPTIDE CHAIN OF TYROSYL $T/RNA$ SYNTHETASE. 2TS1 55 REMARK 1 TITL 2 NO EVIDENCE FOR A SUPER-*SECONDARY STRUCTURE OF 2TS1 56 REMARK 1 TITL 3 FOUR ALPHA-*HELICES 2TS1 57 REMARK 1 REF BIOCHEM.BIOPHYS.RES.COMM. V. 76 728 1977 2TS1 58 REMARK 1 REFN ASTM BBRCA9 US ISSN 0006-291X 146 2TS1 59 REMARK 1 REFERENCE 8 2TS1 60 REMARK 1 AUTH M.J.IRWIN,J.NYBORG,B.R.REID,D.M.BLOW 2TS1 61 REMARK 1 TITL THE CRYSTAL STRUCTURE OF TYROSYL-TRANSFER /RNA$ 2TS1 62 REMARK 1 TITL 2 SYNTHETASE AT 2.7 ANGSTROMS RESOLUTION 2TS1 63 REMARK 1 REF J.MOL.BIOL. V. 105 577 1976 2TS1 64 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 2TS1 65 REMARK 1 REFERENCE 9 2TS1 66 REMARK 1 AUTH B.R.REID,G.L.E.KOCH,Y.BOULANGER,B.S.HARTLEY, 2TS1 67 REMARK 1 AUTH 2 D.M.BLOW 2TS1 68 REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY DIFFRACTION 2TS1 69 REMARK 1 TITL 2 STUDIES ON TYROSYL-TRANSFER /RNA$ SYNTHETASE FROM 2TS1 70 REMARK 1 TITL 3 BACILLUS $STEAROTHERMOPHILUS 2TS1 71 REMARK 1 REF J.MOL.BIOL. V. 80 199 1973 2TS1 72 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 2TS1 73 REMARK 2 2TS1 74 REMARK 2 RESOLUTION. 2.3 ANGSTROMS. 2TS1 75 REMARK 3 2TS1 76 REMARK 3 REFINEMENT. BY A MODIFIED VERSION OF THE RESTRAINED 2TS1 77 REMARK 3 LEAST-SQUARES PROCEDURE OF J. KONNERT AND W. HENDRICKSON 2TS1 78 REMARK 3 (MODIFIED VERSION OF PROGRAM *PROLSQ*). THE R VALUE IS 2TS1 79 REMARK 3 0.228 FOR 24432 REFLECTIONS. ATOMS WITH THERMAL FACTORS 2TS1 80 REMARK 3 WHICH CALCULATE LESS THAN 2.00 ARE ASSIGNED THIS VALUE. 2TS1 81 REMARK 3 THIS IS THE LOWEST VALUE ALLOWED BY THE REFINEMENT 2TS1 82 REMARK 3 PROGRAM. 2TS1 83 REMARK 3 2TS1 84 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES (THE VALUES OF 2TS1 85 REMARK 3 SIGMA, IN PARENTHESES, ARE THE INPUT ESTIMATED 2TS1 86 REMARK 3 STANDARD DEVIATIONS THAT DETERMINE THE RELATIVE 2TS1 87 REMARK 3 WEIGHTS OF THE CORRESPONDING RESTRAINTS) 2TS1 88 REMARK 3 DISTANCE RESTRAINTS (ANGSTROMS) 2TS1 89 REMARK 3 BOND DISTANCE 0.018(0.03) 2TS1 90 REMARK 3 ANGLE DISTANCE 0.044(0.04) 2TS1 91 REMARK 3 PLANAR 1-4 DISTANCE 0.047(0.05) 2TS1 92 REMARK 3 PLANE RESTRAINT (ANGSTROMS) 0.013(0.02) 2TS1 93 REMARK 3 CHIRAL-CENTER RESTRAINT (ANGSTROMS**3) 0.140(0.15) 2TS1 94 REMARK 3 NON-BONDED CONTACT RESTRAINTS (ANGSTROMS) 2TS1 95 REMARK 3 SINGLE TORSION CONTACT 0.19(0.30) 2TS1 96 REMARK 3 MULTIPLE TORSION CONTACT 0.27(0.30) 2TS1 97 REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINT (DEGREES) 2TS1 98 REMARK 3 STAGGERED 9.7(15.0) 2TS1 99 REMARK 3 TRANSVERSE 29.8(45.0) 2TS1 100 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS (ANGSTROMS**2) 2TS1 101 REMARK 3 MAIN-CHAIN BOND 2.68(1.75) 2TS1 102 REMARK 3 MAIN-CHAIN ANGLE 3.76(2.25) 2TS1 103 REMARK 3 SIDE-CHAIN BOND 3.87(2.00) 2TS1 104 REMARK 3 SIDE-CHAIN ANGLE 5.40(2.50) 2TS1 105 REMARK 4 2TS1 106 REMARK 4 THE ASYMMETRIC UNIT OF THE CRYSTAL CONTAINS ONE SUBUNIT 2TS1 107 REMARK 4 OF THE DIMERIC MOLECULE. THE FOLLOWING TRANSFORMATION, 2TS1 108 REMARK 4 WHEN APPLIED TO THE COORDINATES IN THIS FILE, YIELDS THE 2TS1 109 REMARK 4 COORDINATES OF THE OTHER SUBUNIT OF THE MOLECULAR DIMER. 2TS1 110 REMARK 4 THIS TRANSFORMATION CORRESPONDS TO A TWO-FOLD ROTATION 2TS1 111 REMARK 4 ABOUT THE CRYSTALLOGRAPHIC DYAD AXIS ALONG (1 1 0). 2TS1 112 REMARK 4 2TS1 113 REMARK 4 -0.500000 0.866025 0.000000 0.00000 2TS1 114 REMARK 4 0.866025 0.500000 0.000000 0.00000 2TS1 115 REMARK 4 0.000000 0.000000 -1.000000 0.00000 2TS1 116 REMARK 5 2TS1 117 REMARK 5 THE C-TERMINAL RESIDUES 322-419 HAVE EXTREMELY WEAK 2TS1 118 REMARK 5 ELECTRON DENSITY IN THE FINAL MAP AND ARE NOT INCLUDED IN 2TS1 119 REMARK 5 THE MODEL. RESIDUES 212-213 HAVE NO SIGNIFICANT ELECTRON 2TS1 120 REMARK 5 DENSITY AND ARE NOT INCLUDED IN THE MODEL. 2TS1 121 REMARK 6 2TS1 122 REMARK 6 A NUMBER OF SIDE CHAIN ATOMS HAVE BEEN OMITTED FROM THE 2TS1 123 REMARK 6 MODEL BECAUSE THEY HAVE NO ELECTRON DENSITY IN THE FINAL 2TS1 124 REMARK 6 MAP. SEE THE *FTNOTE* RECORDS BELOW FOR SPECIFIC DETAILS. 2TS1 125 REMARK 7 2TS1 126 REMARK 7 THE 29 WATER MOLECULES WITH RESIDUE NUMBERS GREATER 2TS1 127 REMARK 7 THAN 500 PROBABLY REPRESENT DISORDERED PROTEIN. 2TS1 128 REMARK 7 THE R VALUE CALCULATED WITHOUT THESE 29 WATER MOLECULES 2TS1 129 REMARK 7 IS 0.234 THE R VALUE OBTAINED WHEN ALL WATER MOLECULES 2TS1 130 REMARK 7 ARE OMITTED FROM THE MODEL IS 0.262. 2TS1 131 REMARK 8 2TS1A 3 REMARK 8 CORRECTION. INSERT SPRSDE RECORD. 15-JAN-90. 2TS1A 4 SEQRES 1 419 MET ASP LEU LEU ALA GLU LEU GLN TRP ARG GLY LEU VAL 2TS1 132 SEQRES 2 419 ASN GLN THR THR ASP GLU ASP GLY LEU ARG LYS LEU LEU 2TS1 133 SEQRES 3 419 ASN GLU GLU ARG VAL THR LEU TYR CYS GLY PHE ASP PRO 2TS1 134 SEQRES 4 419 THR ALA ASP SER LEU HIS ILE GLY HIS LEU ALA THR ILE 2TS1 135 SEQRES 5 419 LEU THR MET ARG ARG PHE GLN GLN ALA GLY HIS ARG PRO 2TS1 136 SEQRES 6 419 ILE ALA LEU VAL GLY GLY ALA THR GLY LEU ILE GLY ASP 2TS1 137 SEQRES 7 419 PRO SER GLY LYS LYS SER GLU ARG THR LEU ASN ALA LYS 2TS1 138 SEQRES 8 419 GLU THR VAL GLU ALA TRP SER ALA ARG ILE LYS GLU GLN 2TS1 139 SEQRES 9 419 LEU GLY ARG PHE LEU ASP PHE GLU ALA ASP GLY ASN PRO 2TS1 140 SEQRES 10 419 ALA LYS ILE LYS ASN ASN TYR ASP TRP ILE GLY PRO LEU 2TS1 141 SEQRES 11 419 ASP VAL ILE THR PHE LEU ARG ASP VAL GLY LYS HIS PHE 2TS1 142 SEQRES 12 419 SER VAL ASN TYR MET MET ALA LYS GLU SER VAL GLN SER 2TS1 143 SEQRES 13 419 ARG ILE GLU THR GLY ILE SER PHE THR GLU PHE SER TYR 2TS1 144 SEQRES 14 419 MET MET LEU GLN ALA TYR ASP PHE LEU ARG LEU TYR GLU 2TS1 145 SEQRES 15 419 THR GLU GLY CYS ARG LEU GLN ILE GLY GLY SER ASP GLN 2TS1 146 SEQRES 16 419 TRP GLY ASN ILE THR ALA GLY LEU GLU LEU ILE ARG LYS 2TS1 147 SEQRES 17 419 THR LYS GLY GLU ALA ARG ALA PHE GLY LEU THR ILE PRO 2TS1 148 SEQRES 18 419 LEU VAL THR LYS ALA ASP GLY THR LYS PHE GLY LYS THR 2TS1 149 SEQRES 19 419 GLU SER GLY THR ILE TRP LEU ASP LYS GLU LYS THR SER 2TS1 150 SEQRES 20 419 PRO TYR GLU PHE TYR GLN PHE TRP ILE ASN THR ASP ASP 2TS1 151 SEQRES 21 419 ARG ASP VAL ILE ARG TYR LEU LYS TYR PHE THR PHE LEU 2TS1 152 SEQRES 22 419 SER LYS GLU GLU ILE GLU ALA LEU GLU GLN GLU LEU ARG 2TS1 153 SEQRES 23 419 GLU ALA PRO GLU LYS ARG ALA ALA GLN LYS THR LEU ALA 2TS1 154 SEQRES 24 419 GLU GLU VAL THR LYS LEU VAL HIS GLY GLU GLU ALA LEU 2TS1 155 SEQRES 25 419 ARG GLN ALA ILE ARG ILE SER GLU ALA LEU PHE SER GLY 2TS1 156 SEQRES 26 419 ASP ILE ALA ASN LEU THR ALA ALA GLU ILE GLU GLN GLY 2TS1 157 SEQRES 27 419 PHE LYS ASP VAL PRO SER PHE VAL HIS GLU GLY GLY ASP 2TS1 158 SEQRES 28 419 VAL PRO LEU VAL GLU LEU LEU VAL SER ALA GLY ILE SER 2TS1 159 SEQRES 29 419 PRO SER LYS ARG GLN ALA ARG GLU ASP ILE GLN ASN GLY 2TS1 160 SEQRES 30 419 ALA ILE TYR VAL ASN GLY GLU ARG LEU GLN ASP VAL GLY 2TS1 161 SEQRES 31 419 ALA ILE LEU THR ALA GLU HIS ARG LEU GLU GLY ARG PHE 2TS1 162 SEQRES 32 419 THR VAL ILE ARG ARG GLY LYS LYS LYS TYR TYR LEU ILE 2TS1 163 SEQRES 33 419 ARG TYR ALA 2TS1 164 FTNOTE 1 2TS1 165 FTNOTE 1 MET 1 - SIDE CHAIN OMITTED. 2TS1 166 FTNOTE 2 2TS1 167 FTNOTE 2 ASP 20 - SIDE CHAIN BEYOND CB OMITTED. 2TS1 168 FTNOTE 3 2TS1 169 FTNOTE 3 ARG 30 - SIDE CHAIN BEYOND CB OMITTED. 2TS1 170 FTNOTE 4 2TS1 171 FTNOTE 4 ARG 86 - SIDE CHAIN BEYOND CB OMITTED. 2TS1 172 FTNOTE 5 2TS1 173 FTNOTE 5 LYS 91 - SIDE CHAIN BEYOND CG OMITTED. 2TS1 174 FTNOTE 6 2TS1 175 FTNOTE 6 GLU 92 - SIDE CHAIN BEYOND CB OMITTED. 2TS1 176 FTNOTE 7 2TS1 177 FTNOTE 7 GLU 103 - SIDE CHAIN BEYOND CB OMITTED. 2TS1 178 FTNOTE 8 2TS1 179 FTNOTE 8 GLU 112 - SIDE CHAIN BEYOND CB OMITTED. 2TS1 180 FTNOTE 9 2TS1 181 FTNOTE 9 ILE 158 - SIDE CHAIN BEYOND CB OMITTED. 2TS1 182 FTNOTE 10 2TS1 183 FTNOTE 10 GLU 159 - SIDE CHAIN BEYOND CB OMITTED. 2TS1 184 FTNOTE 11 2TS1 185 FTNOTE 11 THR 160 - SIDE CHAIN BEYOND CB OMITTED. 2TS1 186 FTNOTE 12 2TS1 187 FTNOTE 12 ARG 214 - SIDE CHAIN BEYOND CB OMITTED. 2TS1 188 FTNOTE 13 2TS1 189 FTNOTE 13 LYS 230 - SIDE CHAIN BEYOND CG OMITTED. 2TS1 190 FTNOTE 14 2TS1 191 FTNOTE 14 LYS 233 - SIDE CHAIN BEYOND CB OMITTED. 2TS1 192 FTNOTE 15 2TS1 193 FTNOTE 15 GLU 235 - SIDE CHAIN BEYOND CB OMITTED. 2TS1 194 FTNOTE 16 2TS1 195 FTNOTE 16 SER 236 - SIDE CHAIN BEYOND CB OMITTED. 2TS1 196 FTNOTE 17 2TS1 197 FTNOTE 17 GLU 276 - SIDE CHAIN BEYOND CG OMITTED. 2TS1 198 FTNOTE 18 2TS1 199 FTNOTE 18 GLU 284 - SIDE CHAIN BEYOND CB OMITTED. 2TS1 200 FTNOTE 19 2TS1 201 FTNOTE 19 GLU 287 - SIDE CHAIN BEYOND CG OMITTED. 2TS1 202 FTNOTE 20 2TS1 203 FTNOTE 20 GLU 290 - SIDE CHAIN BEYOND CB OMITTED. 2TS1 204 FTNOTE 21 2TS1 205 FTNOTE 21 LYS 291 - SIDE CHAIN BEYOND CG OMITTED. 2TS1 206 FTNOTE 22 2TS1 207 FTNOTE 22 LYS 296 - SIDE CHAIN BEYOND CG OMITTED. 2TS1 208 FTNOTE 23 2TS1 209 FTNOTE 23 GLU 310 - SIDE CHAIN BEYOND CB OMITTED. 2TS1 210 FTNOTE 24 2TS1 211 FTNOTE 24 SER 319 - SIDE CHAIN BEYOND CB OMITTED. 2TS1 212 FORMUL 2 HOH *110(H2 O1) 2TS1 213 HELIX 1 H1 ASP 2 ARG 10 1 2TS1 214 HELIX 2 H2 GLU 19 GLU 28 1 2TS1 215 HELIX 3 H3 LEU 49 GLN 60 1 2TS1 216 HELIX 4 H4 THR 73 LEU 75 5 2TS1 217 HELIX 5 H5 LYS 91 LEU 105 1 2TS1 218 HELIX 6 H6 TYR 124 ILE 127 1 2TS1 219 HELIX 7 H7 VAL 132 ASP 138 1 2TS1 220 HELIX 8 H GLY 140 HIS 142 5 2TS1 221 HELIX 9 H8 VAL 145 MET 149 1 2TS1 222 HELIX 10 H9 GLU 152 GLN 155 1 2TS1 223 HELIX 11 H10 PHE 164 GLU 184 1 2TS1 224 HELIX 12 H11 TRP 196 LYS 210 1 2TS1 225 HELIX 13 H1* PRO 248 ILE 256 1 2TS1 226 HELIX 14 H2* VAL 263 PHE 270 1 2TS1 227 HELIX 15 H3* LYS 275 GLU 287 1 2TS1 228 HELIX 16 H4* ALA 293 VAL 306 1 2TS1 229 HELIX 17 H5* GLU 309 ILE 318 1 2TS1 230 SHEET 1 S1 6 GLN 15 THR 16 0 2TS1 231 SHEET 2 S1 6 PHE 216 ILE 220 -1 N THR 219 O GLN 15 2TS1 232 SHEET 3 S1 6 ARG 187 GLY 192 1 O GLN 189 N LEU 218 2TS1 233 SHEET 4 S1 6 THR 32 PHE 37 1 N TYR 34 O LEU 188 2TS1 234 SHEET 5 S1 6 ARG 64 VAL 69 1 O ILE 66 N CYS 35 2TS1 235 SHEET 6 S1 6 LYS 119 ASN 122 1 N LYS 121 O ALA 67 2TS1 236 CRYST1 64.460 64.460 237.600 90.00 90.00 120.00 P 31 2 1 6 2TS1 237 ORIGX1 1.000000 0.000000 0.000000 0.00000 2TS1 238 ORIGX2 0.000000 1.000000 0.000000 0.00000 2TS1 239 ORIGX3 0.000000 0.000000 1.000000 0.00000 2TS1 240 SCALE1 0.015513 0.008957 0.000000 0.00000 2TS1 241 SCALE2 0.000000 0.017913 0.000000 0.00000 2TS1 242 SCALE3 0.000000 0.000000 0.004209 0.00000 2TS1 243