HEADER LIGASE(SYNTHETASE) 21-FEB-94 1SES 1SES 2 COMPND SERYL-TRNA SYNTHETASE (E.C.6.1.1.11) (SERINE-TRNA LIGASE) 1SES 3 COMPND 2 COMPLEXED WITH SERYL-HYDROXAMATE-AMP 1SES 4 SOURCE (THERMUS THERMOPHILUS) 1SES 5 AUTHOR S.CUSACK,H.BELRHALI 1SES 6 REVDAT 1 31-JUL-94 1SES 0 1SES 7 JRNL AUTH H.BELRHALI,A.D.YAREMCHUK,M.A.TUKALO,K.LARSEN, 1SES 8 JRNL AUTH 2 C.BERTHET-COLOMINAS,R.LEBERMAN,B.BEIJER,B.SPROAT, 1SES 9 JRNL AUTH 3 J.ALS-NIELSEN,G.GRUBEL,J.-F.LEGRAND,M.LEHMANN, 1SES 10 JRNL AUTH 4 S.CUSACK 1SES 11 JRNL TITL CRYSTAL STRUCTURES AT 2.5 ANGSTROMS RESOLUTION OF 1SES 12 JRNL TITL 2 SERYL-TRNA SYNTHETASE COMPLEXED WITH TWO 1SES 13 JRNL TITL 3 DIFFERENT ANALOGUES OF SERYL-ADENYLATE 1SES 14 JRNL REF SCIENCE V. 263 1432 1994 1SES 15 JRNL REFN ASTM SCIEAS US ISSN 0036-8075 0038 1SES 16 REMARK 1 1SES 17 REMARK 1 REFERENCE 1 1SES 18 REMARK 1 AUTH V.BIOU,A.YAREMCHUK,M.TUKALO,S.CUSACK 1SES 19 REMARK 1 TITL THE 2.9 ANGSTROMS CRYSTAL STRUCTURE OF T. 1SES 20 REMARK 1 TITL 2 THERMOPHILUS SERYL-TRNA SYNTHETASE COMPLEXED WITH 1SES 21 REMARK 1 TITL 3 TRNA-SER 1SES 22 REMARK 1 REF SCIENCE V. 263 1404 1994 1SES 23 REMARK 1 REFN ASTM SCIEAS US ISSN 0036-8075 0038 1SES 24 REMARK 1 REFERENCE 2 1SES 25 REMARK 1 AUTH M.FUJINAGA,C.BERTHET-COLOMINAS,A.D.YAREMCHUK, 1SES 26 REMARK 1 AUTH 2 M.A.TUKALO,S.CUSACK 1SES 27 REMARK 1 TITL REFINED CRYSTAL STRUCTURE OF THE SERYL-TRNA 1SES 28 REMARK 1 TITL 2 SYNTHETASE FROM THERMUS THERMOPHILUS AT 2.5 1SES 29 REMARK 1 TITL 3 ANGSTROMS RESOLUTION 1SES 30 REMARK 1 REF J.MOL.BIOL. V. 234 222 1993 1SES 31 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 0070 1SES 32 REMARK 1 REFERENCE 3 1SES 33 REMARK 1 AUTH S.PRICE,S.CUSACK,F.BOREL,C.BERTHET-COLOMINAS, 1SES 34 REMARK 1 AUTH 2 R.LEBERMAN 1SES 35 REMARK 1 TITL CRYSTALLIZATION OF THE SERYL-TRNA SYNTHETASE: 1SES 36 REMARK 1 TITL 2 TRNA-SER COMPLEX OF ESCHERICHIA COLI 1SES 37 REMARK 1 REF /FEBS$ LETT. V. 324 167 1993 1SES 38 REMARK 1 REFN ASTM FEBLAL NE ISSN 0014-5793 0165 1SES 39 REMARK 1 REFERENCE 4 1SES 40 REMARK 1 AUTH A.D.YAREMCHUK,M.A.TUKALO,I.KRIKLIVIY,N.MALCHENKO, 1SES 41 REMARK 1 AUTH 2 V.BIOU,C.BERTHET-COLOMINAS,S.CUSACK 1SES 42 REMARK 1 TITL A NEW CRYSTAL FORM OF THE COMPLEX BETWEEN 1SES 43 REMARK 1 TITL 2 SERYL-TRNA SYNTHETASE AND TRNA-SER FROM THERMUS 1SES 44 REMARK 1 TITL 3 THERMOPHILUS THAT DIFFRACTS TO 2.8 ANGSTROMS 1SES 45 REMARK 1 TITL 4 RESOLUTION 1SES 46 REMARK 1 REF /FEBS$ LETT. V. 310 157 1992 1SES 47 REMARK 1 REFN ASTM FEBLAL NE ISSN 0014-5793 0165 1SES 48 REMARK 1 REFERENCE 5 1SES 49 REMARK 1 AUTH A.D.YAREMCHUK,M.A.TUKALO,I.KRIKLIVIY,V.N.MEL'NIK, 1SES 50 REMARK 1 AUTH 2 C.BERTHET-COLOMINAS,S.CUSACK,R.LEBERMAN 1SES 51 REMARK 1 TITL CRYSTALLIZATION OF THE SERYL-TRNA 1SES 52 REMARK 1 TITL 2 SYNTHETASE-TRNA-SER COMPLEX FROM THERMUS 1SES 53 REMARK 1 TITL 3 THERMOPHILUS 1SES 54 REMARK 1 REF J.MOL.BIOL. V. 224 519 1992 1SES 55 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 0070 1SES 56 REMARK 1 REFERENCE 6 1SES 57 REMARK 1 AUTH S.CUSACK,M.HARTLEIN,R.LEBERMAN 1SES 58 REMARK 1 TITL SEQUENCE, STRUCTURAL AND EVOLUTIONARY 1SES 59 REMARK 1 TITL 2 RELATIONSHIPS BETWEEN CLASS 2 AMINOACYL-TRNA 1SES 60 REMARK 1 TITL 3 SYNTHETASES 1SES 61 REMARK 1 REF NUCLEIC ACIDS RES. V. 19 3489 1991 1SES 62 REMARK 1 REFN ASTM NARHAD UK ISSN 0305-1048 0389 1SES 63 REMARK 1 REFERENCE 7 1SES 64 REMARK 1 AUTH S.CUSACK,C.BERTHET-COLOMINAS,M.HARTLEIN,N.NASSAR, 1SES 65 REMARK 1 AUTH 2 R.LEBERMAN 1SES 66 REMARK 1 TITL SERYL-TRNA SYNTHETASE FROM ESCHERICHIA COLI AT 2.5 1SES 67 REMARK 1 TITL 2 ANGSTROMS RESOLUTION: A SECOND CLASS OF 1SES 68 REMARK 1 TITL 3 SYNTHETASE STRUCTURE 1SES 69 REMARK 1 REF NATURE V. 347 249 1990 1SES 70 REMARK 1 REFN ASTM NATUAS UK ISSN 0028-0836 0006 1SES 71 REMARK 1 REFERENCE 8 1SES 72 REMARK 1 AUTH M.B.GARBER,A.D.YAREMCHUK,M.A.TUKALO,S.P.EGOROVA, 1SES 73 REMARK 1 AUTH 2 C.BERTHET-COLOMINAS,R.LEBERMAN 1SES 74 REMARK 1 TITL CRYSTALS OF SERYL-TRNA SYNTHETASE FROM THERMUS 1SES 75 REMARK 1 TITL 2 THERMOPHILUS. PRELIMINARY CRYSTALLOGRAPHIC DATA 1SES 76 REMARK 1 REF J.MOL.BIOL. V. 213 631 1990 1SES 77 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 0070 1SES 78 REMARK 2 1SES 79 REMARK 2 RESOLUTION. 2.5 ANGSTROMS. 1SES 80 REMARK 3 1SES 81 REMARK 3 REFINEMENT. 1SES 82 REMARK 3 PROGRAM X-PLOR 1SES 83 REMARK 3 AUTHORS BRUNGER 1SES 84 REMARK 3 R VALUE 0.176 1SES 85 REMARK 3 RMSD BOND DISTANCES 0.016 ANGSTROMS 1SES 86 REMARK 3 RMSD BOND ANGLES 3.3 DEGREES 1SES 87 REMARK 3 1SES 88 REMARK 3 REFINEMENT. RESOLUTION RANGE: 2.5 - 8. ANGSTROMS. 1SES 89 REMARK 3 1SES 90 REMARK 3 NUMBER OF REFLECTIONS 36920 1SES 91 REMARK 3 RESOLUTION RANGE 20.0 - 2.5 ANGSTROMS 1SES 92 REMARK 3 DATA CUTOFF 2.0 SIGMA(F) 1SES 93 REMARK 3 PERCENT COMPLETION 87.0 1SES 94 REMARK 3 1SES 95 REMARK 3 NUMBER OF PROTEIN ATOMS 6746 1SES 96 REMARK 3 NUMBER OF SOLVENT ATOMS 130 1SES 97 REMARK 4 1SES 98 REMARK 4 SERYL-TRNA SYNTHETASE IS A CLASS 2 AMINOACYL-TRNA 1SES 99 REMARK 4 SYNTHETASE. SERYL-TRNA SYNTHETASE FROM THERMUS 1SES 100 REMARK 4 THERMOPHILUS IS A HOMO-DIMER WITH 421 RESIDUES PER SUBUNIT 1SES 101 REMARK 4 AND THE SUBUNITS HAVE BEEN ASSIGNED CHAIN IDENTIFIERS A AND 1SES 102 REMARK 4 B. THE STRUCTURE CONTAINS ONE SERYL-HYDROXAMATE-AMP (AHX 1SES 103 REMARK 4 422) AND ONE AMP MOLECULE (AMP 423). 1SES 104 REMARK 5 1SES 105 REMARK 5 THE NON-CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATION TO GO FROM 1SES 106 REMARK 5 MONOMER 1 TO MONOMER 2 IS GIVEN ON *MTRIX* RECORDS BELOW. 1SES 107 REMARK 5 IT WILL YIELD APPROXIMATE COORDINATES FOR CHAIN B WHEN 1SES 108 REMARK 5 APPLIED TO CHAIN A. IT IS BASED ON SIMULTANEOUS 1SES 109 REMARK 5 SUPERPOSITION OF THE C-ALPHAS OF RESIDUES 100 - 258 AND 1SES 110 REMARK 5 270 - 419. 1SES 111 REMARK 6 1SES 112 REMARK 6 RESIDUES WITH NO ELECTRON DENSITY OR B GREATER THAN 90 1SES 113 REMARK 6 HAVE OCCUPANCY 0.0. 1SES 114 REMARK 7 1SES 115 REMARK 7 THE SEQUENCE IS REPORTED IN REFERENCE 2. 1SES 116 REMARK 8 1SES 117 REMARK 8 PDB ADVISORY NOTICE: 1SES 118 REMARK 8 ARG 82 A AND VAL 111 B HAVE A CLOSE PACKING INTERACTION OF 1SES 119 REMARK 8 1.96 ANGSTROMS. ARG 16 B AND GLU 50 A HAVE A PACKING 1SES 120 REMARK 8 INTERACTION OF 2.10 ANGSTROMS. 1SES 121 REMARK 9 1SES 122 REMARK 9 HET GROUP AHX IS 1SES 123 REMARK 9 1-SERYL-HYDROXAMATE-ADENOSINE MONOPHOSPHATE. 1SES 124 SEQRES 1 A 421 MET VAL ASP LEU LYS ARG LEU ARG GLN GLU PRO GLU VAL 1SES 125 SEQRES 2 A 421 PHE HIS ARG ALA ILE ARG GLU LYS GLY VAL ALA LEU ASP 1SES 126 SEQRES 3 A 421 LEU GLU ALA LEU LEU ALA LEU ASP ARG GLU VAL GLN GLU 1SES 127 SEQRES 4 A 421 LEU LYS LYS ARG LEU GLN GLU VAL GLN THR GLU ARG ASN 1SES 128 SEQRES 5 A 421 GLN VAL ALA LYS ARG VAL PRO LYS ALA PRO PRO GLU GLU 1SES 129 SEQRES 6 A 421 LYS GLU ALA LEU ILE ALA ARG GLY LYS ALA LEU GLY GLU 1SES 130 SEQRES 7 A 421 GLU ALA LYS ARG LEU GLU GLU ALA LEU ARG GLU LYS GLU 1SES 131 SEQRES 8 A 421 ALA ARG LEU GLU ALA LEU LEU LEU GLN VAL PRO LEU PRO 1SES 132 SEQRES 9 A 421 PRO TRP PRO GLY ALA PRO VAL GLY GLY GLU GLU ALA ASN 1SES 133 SEQRES 10 A 421 ARG GLU ILE LYS ARG VAL GLY GLY PRO PRO GLU PHE SER 1SES 134 SEQRES 11 A 421 PHE PRO PRO LEU ASP HIS VAL ALA LEU MET GLU LYS ASN 1SES 135 SEQRES 12 A 421 GLY TRP TRP GLU PRO ARG ILE SER GLN VAL SER GLY SER 1SES 136 SEQRES 13 A 421 ARG SER TYR ALA LEU LYS GLY ASP LEU ALA LEU TYR GLU 1SES 137 SEQRES 14 A 421 LEU ALA LEU LEU ARG PHE ALA MET ASP PHE MET ALA ARG 1SES 138 SEQRES 15 A 421 ARG GLY PHE LEU PRO MET THR LEU PRO SER TYR ALA ARG 1SES 139 SEQRES 16 A 421 GLU LYS ALA PHE LEU GLY THR GLY HIS PHE PRO ALA TYR 1SES 140 SEQRES 17 A 421 ARG ASP GLN VAL TRP ALA ILE ALA GLU THR ASP LEU TYR 1SES 141 SEQRES 18 A 421 LEU THR GLY THR ALA GLU VAL VAL LEU ASN ALA LEU HIS 1SES 142 SEQRES 19 A 421 SER GLY GLU ILE LEU PRO TYR GLU ALA LEU PRO LEU ARG 1SES 143 SEQRES 20 A 421 TYR ALA GLY TYR ALA PRO ALA PHE ARG SER GLU ALA GLY 1SES 144 SEQRES 21 A 421 SER PHE GLY LYS ASP VAL ARG GLY LEU MET ARG VAL HIS 1SES 145 SEQRES 22 A 421 GLN PHE HIS LYS VAL GLU GLN TYR VAL LEU THR GLU ALA 1SES 146 SEQRES 23 A 421 SER LEU GLU ALA SER ASP ARG ALA PHE GLN GLU LEU LEU 1SES 147 SEQRES 24 A 421 GLU ASN ALA GLU GLU ILE LEU ARG LEU LEU GLU LEU PRO 1SES 148 SEQRES 25 A 421 TYR ARG LEU VAL GLU VAL ALA THR GLY ASP MET GLY PRO 1SES 149 SEQRES 26 A 421 GLY LYS TRP ARG GLN VAL ASP ILE GLU VAL TYR LEU PRO 1SES 150 SEQRES 27 A 421 SER GLU GLY ARG TYR ARG GLU THR HIS SER CYS SER ALA 1SES 151 SEQRES 28 A 421 LEU LEU ASP TRP GLN ALA ARG ARG ALA ASN LEU ARG TYR 1SES 152 SEQRES 29 A 421 ARG ASP PRO GLU GLY ARG VAL ARG TYR ALA TYR THR LEU 1SES 153 SEQRES 30 A 421 ASN ASN THR ALA LEU ALA THR PRO ARG ILE LEU ALA MET 1SES 154 SEQRES 31 A 421 LEU LEU GLU ASN HIS GLN LEU GLN ASP GLY ARG VAL ARG 1SES 155 SEQRES 32 A 421 VAL PRO GLN ALA LEU ILE PRO TYR MET GLY LYS GLU VAL 1SES 156 SEQRES 33 A 421 LEU GLU PRO CYS GLY 1SES 157 SEQRES 1 B 421 MET VAL ASP LEU LYS ARG LEU ARG GLN GLU PRO GLU VAL 1SES 158 SEQRES 2 B 421 PHE HIS ARG ALA ILE ARG GLU LYS GLY VAL ALA LEU ASP 1SES 159 SEQRES 3 B 421 LEU GLU ALA LEU LEU ALA LEU ASP ARG GLU VAL GLN GLU 1SES 160 SEQRES 4 B 421 LEU LYS LYS ARG LEU GLN GLU VAL GLN THR GLU ARG ASN 1SES 161 SEQRES 5 B 421 GLN VAL ALA LYS ARG VAL PRO LYS ALA PRO PRO GLU GLU 1SES 162 SEQRES 6 B 421 LYS GLU ALA LEU ILE ALA ARG GLY LYS ALA LEU GLY GLU 1SES 163 SEQRES 7 B 421 GLU ALA LYS ARG LEU GLU GLU ALA LEU ARG GLU LYS GLU 1SES 164 SEQRES 8 B 421 ALA ARG LEU GLU ALA LEU LEU LEU GLN VAL PRO LEU PRO 1SES 165 SEQRES 9 B 421 PRO TRP PRO GLY ALA PRO VAL GLY GLY GLU GLU ALA ASN 1SES 166 SEQRES 10 B 421 ARG GLU ILE LYS ARG VAL GLY GLY PRO PRO GLU PHE SER 1SES 167 SEQRES 11 B 421 PHE PRO PRO LEU ASP HIS VAL ALA LEU MET GLU LYS ASN 1SES 168 SEQRES 12 B 421 GLY TRP TRP GLU PRO ARG ILE SER GLN VAL SER GLY SER 1SES 169 SEQRES 13 B 421 ARG SER TYR ALA LEU LYS GLY ASP LEU ALA LEU TYR GLU 1SES 170 SEQRES 14 B 421 LEU ALA LEU LEU ARG PHE ALA MET ASP PHE MET ALA ARG 1SES 171 SEQRES 15 B 421 ARG GLY PHE LEU PRO MET THR LEU PRO SER TYR ALA ARG 1SES 172 SEQRES 16 B 421 GLU LYS ALA PHE LEU GLY THR GLY HIS PHE PRO ALA TYR 1SES 173 SEQRES 17 B 421 ARG ASP GLN VAL TRP ALA ILE ALA GLU THR ASP LEU TYR 1SES 174 SEQRES 18 B 421 LEU THR GLY THR ALA GLU VAL VAL LEU ASN ALA LEU HIS 1SES 175 SEQRES 19 B 421 SER GLY GLU ILE LEU PRO TYR GLU ALA LEU PRO LEU ARG 1SES 176 SEQRES 20 B 421 TYR ALA GLY TYR ALA PRO ALA PHE ARG SER GLU ALA GLY 1SES 177 SEQRES 21 B 421 SER PHE GLY LYS ASP VAL ARG GLY LEU MET ARG VAL HIS 1SES 178 SEQRES 22 B 421 GLN PHE HIS LYS VAL GLU GLN TYR VAL LEU THR GLU ALA 1SES 179 SEQRES 23 B 421 SER LEU GLU ALA SER ASP ARG ALA PHE GLN GLU LEU LEU 1SES 180 SEQRES 24 B 421 GLU ASN ALA GLU GLU ILE LEU ARG LEU LEU GLU LEU PRO 1SES 181 SEQRES 25 B 421 TYR ARG LEU VAL GLU VAL ALA THR GLY ASP MET GLY PRO 1SES 182 SEQRES 26 B 421 GLY LYS TRP ARG GLN VAL ASP ILE GLU VAL TYR LEU PRO 1SES 183 SEQRES 27 B 421 SER GLU GLY ARG TYR ARG GLU THR HIS SER CYS SER ALA 1SES 184 SEQRES 28 B 421 LEU LEU ASP TRP GLN ALA ARG ARG ALA ASN LEU ARG TYR 1SES 185 SEQRES 29 B 421 ARG ASP PRO GLU GLY ARG VAL ARG TYR ALA TYR THR LEU 1SES 186 SEQRES 30 B 421 ASN ASN THR ALA LEU ALA THR PRO ARG ILE LEU ALA MET 1SES 187 SEQRES 31 B 421 LEU LEU GLU ASN HIS GLN LEU GLN ASP GLY ARG VAL ARG 1SES 188 SEQRES 32 B 421 VAL PRO GLN ALA LEU ILE PRO TYR MET GLY LYS GLU VAL 1SES 189 SEQRES 33 B 421 LEU GLU PRO CYS GLY 1SES 190 FTNOTE 1 1SES 191 FTNOTE 1 VAL A 58 - PRO A 59 OMEGA = 210.31 1SES 192 FTNOTE 1 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 1SES 193 FTNOTE 2 1SES 194 FTNOTE 2 CIS PROLINE - PRO A 206 1SES 195 FTNOTE 3 1SES 196 FTNOTE 3 CIS PROLINE - PRO A 245 1SES 197 FTNOTE 4 1SES 198 FTNOTE 4 CIS PROLINE - PRO A 385 1SES 199 FTNOTE 5 1SES 200 FTNOTE 5 CIS PROLINE - PRO B 206 1SES 201 FTNOTE 6 1SES 202 FTNOTE 6 CIS PROLINE - PRO B 245 1SES 203 FTNOTE 7 1SES 204 FTNOTE 7 CIS PROLINE - PRO B 385 1SES 205 HET AHX 422 30 SEE REMARK 9 1SES 206 HET AMP 423 23 ADENOSINE MONOPHOSPHATE 1SES 207 FORMUL 3 AHX C13 H21 N7 O9 P1 + 1SES 208 FORMUL 4 AMP C10 H14 N5 O7 P1 1SES 209 FORMUL 5 HOH *130(H2 O1) 1SES 210 CRYST1 85.100 125.200 62.400 90.00 108.80 90.00 P 21 4 1SES 211 ORIGX1 1.000000 0.000000 0.000000 0.00000 1SES 212 ORIGX2 0.000000 1.000000 0.000000 0.00000 1SES 213 ORIGX3 0.000000 0.000000 1.000000 0.00000 1SES 214 SCALE1 0.011751 0.000000 0.004000 0.00000 1SES 215 SCALE2 0.000000 0.007987 0.000000 0.00000 1SES 216 SCALE3 0.000000 0.000000 0.016929 0.00000 1SES 217 MTRIX1 1 0.660990 -0.489960 0.568360 -14.19824 1 1SES 218 MTRIX2 1 -0.491770 -0.854930 -0.165070 31.00661 1 1SES 219 MTRIX3 1 0.566790 -0.170390 -0.806050 68.28316 1 1SES 220