HEADER TOXIN 29-OCT-93 1TSS 1TSS 2 COMPND TOXIC SHOCK SYNDROME TOXIN 1 1TSS 3 SOURCE STAPHYLOCOCCUS AUREUS 1TSS 4 AUTHOR G.S.PRASAD,C.A.EARHART,D.L.MURRAY,R.P.NOVICK,P.M.SCHLIVERT, 1TSS 5 AUTHOR 2 D.H.OHLENDORF 1TSS 6 REVDAT 1 15-OCT-94 1TSS 0 1TSS 7 JRNL AUTH G.S.PRASAD,C.A.EARHART,D.L.MURRAY,R.P.NOVICK, 1TSS 8 JRNL AUTH 2 P.M.SCHLIVERT,D.H.OHLENDORF 1TSS 9 JRNL TITL STRUCTURE OF TOXIC SHOCK TOXIN 1 1TSS 10 JRNL REF BIOCHEMISTRY V. 32 13761 1993 1TSS 11 JRNL REFN ASTM BICHAW US ISSN 0006-2960 0033 1TSS 12 REMARK 1 1TSS 13 REMARK 2 1TSS 14 REMARK 2 RESOLUTION. 2.5 ANGSTROMS. 1TSS 15 REMARK 3 1TSS 16 REMARK 3 REFINEMENT. 1TSS 17 REMARK 3 PROGRAM X-PLOR 1TSS 18 REMARK 3 AUTHORS BRUNGER 1TSS 19 REMARK 3 R VALUE 0.226 1TSS 20 REMARK 3 RMSD BOND DISTANCES 0.016 ANGSTROMS 1TSS 21 REMARK 3 RMSD BOND ANGLES 2.2 DEGREES 1TSS 22 REMARK 3 1TSS 23 REMARK 3 NUMBER OF REFLECTIONS 28624 1TSS 24 REMARK 3 RESOLUTION RANGE 8. - 2.5 ANGSTROMS 1TSS 25 REMARK 3 DATA CUTOFF 2. SIGMA(F) 1TSS 26 REMARK 3 PERCENT COMPLETION 98.0 1TSS 27 REMARK 3 1TSS 28 REMARK 3 NUMBER OF PROTEIN ATOMS 4677 1TSS 29 REMARK 3 NUMBER OF SOLVENT ATOMS 0 1TSS 30 REMARK 4 1TSS 31 REMARK 4 DATA WERE COLLECTED TO 2.05 ANGSTROMS RESOLUTION ON A 1TSS 32 REMARK 4 SIEMENS AREA DETECTOR. THE STRUCTURE WAS SOLVED BY THE 1TSS 33 REMARK 4 MULTIPLE ISOMORPHOUS METHOD. 1TSS 34 REMARK 5 1TSS 35 REMARK 5 THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT IS A TRIMER. RESIDUES 1TSS 36 REMARK 5 ARE NUMBERED 1 - 194 IN CHAINS *A*, *B*, AND *C*. 1TSS 37 REMARK 6 1TSS 38 REMARK 6 THE TRANSFORMATION PRESENTED ON *MTRIX 1* RECORDS BELOW 1TSS 39 REMARK 6 WILL YIELD APPROXIMATE COORDINATES FOR CHAIN *B* WHEN 1TSS 40 REMARK 6 APPLIED TO THE CHAIN *A*. 1TSS 41 REMARK 6 THE TRANSFORMATION PRESENTED ON *MTRIX 2* RECORDS BELOW 1TSS 42 REMARK 6 WILL YIELD APPROXIMATE COORDINATES FOR CHAIN *C* WHEN 1TSS 43 REMARK 6 APPLIED TO THE CHAIN *A*. 1TSS 44 REMARK 7 1TSS 45 REMARK 7 SEQUENCE ADVISORY NOTICE 1TSS 46 REMARK 7 DIFFERENCE BETWEEN SWISS-PROT AND PDB SEQUENCE. 1TSS 47 REMARK 7 1TSS 48 REMARK 7 SWISS-PROT ENTRY NAME: TSST_STAAU 1TSS 49 REMARK 7 1TSS 50 REMARK 7 SWISS-PROT RESIDUE PDB SEQRES 1TSS 51 REMARK 7 1TSS 52 REMARK 7 NAME NUMBER NAME CHAIN SEQ/INSERT CODE 1TSS 53 REMARK 7 GLY 156 TRP A 116 1TSS 54 REMARK 7 GLY 156 TRP B 116 1TSS 55 REMARK 7 GLY 156 TRP C 116 1TSS 56 REMARK 7 1TSS 57 REMARK 7 TSST-1 IS PRODUCED AS A PRO-PEPTIDE WITH 40 AMINO ACIDS AT 1TSS 58 REMARK 7 ITS AMINO-TERMINUS. THE NUMBERING SCHEME HERE BEGINS WITH 1TSS 59 REMARK 7 THE FIRST RESIDUE OF THE MATURE PROTEIN. THE SEQUENCE IN 1TSS 60 REMARK 7 THIS ENTRY IS BASED ON THE PUBLISHED SEQUENCE 1TSS 61 REMARK 7 (BLOMSTER-HAUTAMAA, ET AL., (1986), J. BIOL. CHEM. 261, 1TSS 62 REMARK 7 15783). THE DENSITY AGREES THAT 116 IS A TRYPTOPHAN. 1TSS 63 REMARK 8 1TSS 64 REMARK 8 THE SHEETS REPRESENTED AS *BAR*, *BLB*, AND *BLC* ON THE 1TSS 65 REMARK 8 SHEET RECORDS BELOW ARE ACTUALLY FIVE-STRANDED BETA-BARRELS 1TSS 66 REMARK 8 SIMILAR TO STAPHYLOCOCCAL NUCLEASE (PROTEIN DATA BANK ENTRY 1TSS 67 REMARK 8 1SNC). THESE ARE REPRESENTED AS SIX-STRANDED SHEETS IN 1TSS 68 REMARK 8 WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE 1TSS 69 REMARK 8 TOPOLOGY OF THESE SHEETS IS (-1,-1,-2,+1,+3X) WHERE THE +3X 1TSS 70 REMARK 8 IS THE CONNECTION OF STRAND 5 BACK TO STRAND 1 IN THE 1TSS 71 REMARK 8 BARREL. 1TSS 72 REMARK 9 1TSS 73 REMARK 9 SHEETS *SML*, *SMB*, AND *SCM* ARE COMPOSED OF THREE 1TSS 74 REMARK 9 ANTI-PARALLEL STRANDS. SHEETS *LRG*, *LRB*, AND *LRC* 1TSS 75 REMARK 9 HAVE THE TOPOLOGY (+1,-3X,-1,+2X). 1TSS 76 REMARK 10 1TSS 77 REMARK 10 THE MODEL PRESENTED HERE IS NOT COMPLETELY REFINED; FURTHER 1TSS 78 REMARK 10 REFINEMENT IS IN PROGRESS. 1TSS 79 SEQRES 1 A 194 SER THR ASN ASP ASN ILE LYS ASP LEU LEU ASP TRP TYR 1TSS 80 SEQRES 2 A 194 SER SER GLY SER ASP THR PHE THR ASN SER GLU VAL LEU 1TSS 81 SEQRES 3 A 194 ASP ASN SER LEU GLY SER MET ARG ILE LYS ASN THR ASP 1TSS 82 SEQRES 4 A 194 GLY SER ILE SER LEU ILE ILE PHE PRO SER PRO TYR TYR 1TSS 83 SEQRES 5 A 194 SER PRO ALA PHE THR LYS GLY GLU LYS VAL ASP LEU ASN 1TSS 84 SEQRES 6 A 194 THR LYS ARG THR LYS LYS SER GLN HIS THR SER GLU GLY 1TSS 85 SEQRES 7 A 194 THR TYR ILE HIS PHE GLN ILE SER GLY VAL THR ASN THR 1TSS 86 SEQRES 8 A 194 GLU LYS LEU PRO THR PRO ILE GLU LEU PRO LEU LYS VAL 1TSS 87 SEQRES 9 A 194 LYS VAL HIS GLY LYS ASP SER PRO LEU LYS TYR TRP PRO 1TSS 88 SEQRES 10 A 194 LYS PHE ASP LYS LYS GLN LEU ALA ILE SER THR LEU ASP 1TSS 89 SEQRES 11 A 194 PHE GLU ILE ARG HIS GLN LEU THR GLN ILE HIS GLY LEU 1TSS 90 SEQRES 12 A 194 TYR ARG SER SER ASP LYS THR GLY GLY TYR TRP LYS ILE 1TSS 91 SEQRES 13 A 194 THR MET ASN ASP GLY SER THR TYR GLN SER ASP LEU SER 1TSS 92 SEQRES 14 A 194 LYS LYS PHE GLU TYR ASN THR GLU LYS PRO PRO ILE ASN 1TSS 93 SEQRES 15 A 194 ILE ASP GLU ILE LYS THR ILE GLU ALA GLU ILE ASN 1TSS 94 SEQRES 1 B 194 SER THR ASN ASP ASN ILE LYS ASP LEU LEU ASP TRP TYR 1TSS 95 SEQRES 2 B 194 SER SER GLY SER ASP THR PHE THR ASN SER GLU VAL LEU 1TSS 96 SEQRES 3 B 194 ASP ASN SER LEU GLY SER MET ARG ILE LYS ASN THR ASP 1TSS 97 SEQRES 4 B 194 GLY SER ILE SER LEU ILE ILE PHE PRO SER PRO TYR TYR 1TSS 98 SEQRES 5 B 194 SER PRO ALA PHE THR LYS GLY GLU LYS VAL ASP LEU ASN 1TSS 99 SEQRES 6 B 194 THR LYS ARG THR LYS LYS SER GLN HIS THR SER GLU GLY 1TSS 100 SEQRES 7 B 194 THR TYR ILE HIS PHE GLN ILE SER GLY VAL THR ASN THR 1TSS 101 SEQRES 8 B 194 GLU LYS LEU PRO THR PRO ILE GLU LEU PRO LEU LYS VAL 1TSS 102 SEQRES 9 B 194 LYS VAL HIS GLY LYS ASP SER PRO LEU LYS TYR TRP PRO 1TSS 103 SEQRES 10 B 194 LYS PHE ASP LYS LYS GLN LEU ALA ILE SER THR LEU ASP 1TSS 104 SEQRES 11 B 194 PHE GLU ILE ARG HIS GLN LEU THR GLN ILE HIS GLY LEU 1TSS 105 SEQRES 12 B 194 TYR ARG SER SER ASP LYS THR GLY GLY TYR TRP LYS ILE 1TSS 106 SEQRES 13 B 194 THR MET ASN ASP GLY SER THR TYR GLN SER ASP LEU SER 1TSS 107 SEQRES 14 B 194 LYS LYS PHE GLU TYR ASN THR GLU LYS PRO PRO ILE ASN 1TSS 108 SEQRES 15 B 194 ILE ASP GLU ILE LYS THR ILE GLU ALA GLU ILE ASN 1TSS 109 SEQRES 1 C 194 SER THR ASN ASP ASN ILE LYS ASP LEU LEU ASP TRP TYR 1TSS 110 SEQRES 2 C 194 SER SER GLY SER ASP THR PHE THR ASN SER GLU VAL LEU 1TSS 111 SEQRES 3 C 194 ASP ASN SER LEU GLY SER MET ARG ILE LYS ASN THR ASP 1TSS 112 SEQRES 4 C 194 GLY SER ILE SER LEU ILE ILE PHE PRO SER PRO TYR TYR 1TSS 113 SEQRES 5 C 194 SER PRO ALA PHE THR LYS GLY GLU LYS VAL ASP LEU ASN 1TSS 114 SEQRES 6 C 194 THR LYS ARG THR LYS LYS SER GLN HIS THR SER GLU GLY 1TSS 115 SEQRES 7 C 194 THR TYR ILE HIS PHE GLN ILE SER GLY VAL THR ASN THR 1TSS 116 SEQRES 8 C 194 GLU LYS LEU PRO THR PRO ILE GLU LEU PRO LEU LYS VAL 1TSS 117 SEQRES 9 C 194 LYS VAL HIS GLY LYS ASP SER PRO LEU LYS TYR TRP PRO 1TSS 118 SEQRES 10 C 194 LYS PHE ASP LYS LYS GLN LEU ALA ILE SER THR LEU ASP 1TSS 119 SEQRES 11 C 194 PHE GLU ILE ARG HIS GLN LEU THR GLN ILE HIS GLY LEU 1TSS 120 SEQRES 12 C 194 TYR ARG SER SER ASP LYS THR GLY GLY TYR TRP LYS ILE 1TSS 121 SEQRES 13 C 194 THR MET ASN ASP GLY SER THR TYR GLN SER ASP LEU SER 1TSS 122 SEQRES 14 C 194 LYS LYS PHE GLU TYR ASN THR GLU LYS PRO PRO ILE ASN 1TSS 123 SEQRES 15 C 194 ILE ASP GLU ILE LYS THR ILE GLU ALA GLU ILE ASN 1TSS 124 FTNOTE 1 1TSS 125 FTNOTE 1 DENSITY FOR THE FOLLOWING SIDE CHAIN RESIDUES WERE WEAK: 1TSS 126 FTNOTE 1 THR A 75, SER A 76, GLU A 77, THR B 75, SER B 76, GLU B 77, 1TSS 127 FTNOTE 1 THR C 75, SER C 76, AND GLU C 77. THEREFORE, THE 1TSS 128 FTNOTE 1 OCCUPANCIES OF THESE SIDE CHAIN ATOMS WERE SET TO 0.00. 1TSS 129 HELIX 1 HA ASN A 3 SER A 15 4 SUBUNIT A HELIX 1 1TSS 130 HELIX 2 HB ALA A 125 HIS A 141 4 SUBUNIT A HELIX 2 1TSS 131 HELIX 3 HC ARG A 145 LYS A 149 3 SUBUNIT A HELIX 3 1TSS 132 HELIX 4 HD GLU A 173 GLU A 177 3 SUBUNIT A HELIX 4 1TSS 133 HELIX 5 HAA ASN B 3 SER B 15 4 SUBUNIT B HELIX 1 1TSS 134 HELIX 6 HBA ALA B 125 HIS B 141 4 SUBUNIT B HELIX 2 1TSS 135 HELIX 7 HCA ARG B 145 LYS B 149 3 SUBUNIT B HELIX 3 1TSS 136 HELIX 8 HDA GLU B 173 GLU B 177 3 SUBUNIT B HELIX 4 1TSS 137 HELIX 9 HAB ASN C 3 SER C 15 4 SUBUNIT C HELIX 1 1TSS 138 HELIX 10 HBB ALA C 125 HIS C 141 4 SUBUNIT C HELIX 2 1TSS 139 HELIX 11 HCB ARG C 145 LYS C 149 3 SUBUNIT C HELIX 3 1TSS 140 HELIX 12 HDB GLU C 173 GLU C 177 3 SUBUNIT C HELIX 4 1TSS 141 SHEET 1 BAR 6 ASP A 18 SER A 29 0 1TSS 142 SHEET 2 BAR 6 GLY A 31 ASN A 37 -1 N ARG A 34 O ASP A 27 1TSS 143 SHEET 3 BAR 6 SER A 41 PHE A 47 -1 N SER A 43 O ILE A 35 1TSS 144 SHEET 4 BAR 6 THR A 79 THR A 89 -1 N HIS A 82 O ILE A 42 1TSS 145 SHEET 5 BAR 6 GLU A 60 THR A 75 -1 N LYS A 70 O PHE A 83 1TSS 146 SHEET 6 BAR 6 ASP A 18 SER A 29 1 N PHE A 20 O LEU A 64 1TSS 147 SHEET 1 SML 3 GLU A 92 LEU A 100 0 1TSS 148 SHEET 2 SML 3 PRO A 117 LEU A 124 -1 N PHE A 119 O ILE A 98 1TSS 149 SHEET 3 SML 3 ILE A 181 ILE A 183 -1 N ILE A 181 O LEU A 124 1TSS 150 SHEET 1 LRG 5 LYS A 109 SER A 111 0 1TSS 151 SHEET 2 LRG 5 PRO A 101 HIS A 107 -1 N VAL A 106 O LYS A 109 1TSS 152 SHEET 3 LRG 5 GLU A 185 ASN A 194 1 N ILE A 193 O LYS A 105 1TSS 153 SHEET 4 LRG 5 GLY A 151 ASN A 159 -1 N THR A 157 O THR A 188 1TSS 154 SHEET 5 LRG 5 SER A 162 LEU A 168 -1 N SER A 166 O TRP A 154 1TSS 155 SHEET 1 BLB 6 ASP B 18 SER B 29 0 1TSS 156 SHEET 2 BLB 6 GLY B 31 ASN B 37 -1 N ARG B 34 O ASP B 27 1TSS 157 SHEET 3 BLB 6 SER B 41 PHE B 47 -1 N SER B 43 O ILE B 35 1TSS 158 SHEET 4 BLB 6 THR B 79 THR B 89 -1 N HIS B 82 O ILE B 42 1TSS 159 SHEET 5 BLB 6 GLU B 60 THR B 75 -1 N LYS B 70 O PHE B 83 1TSS 160 SHEET 6 BLB 6 ASP B 18 SER B 29 1 N PHE B 20 O LEU B 64 1TSS 161 SHEET 1 SMB 3 GLU B 92 LEU B 100 0 1TSS 162 SHEET 2 SMB 3 PRO B 117 LEU B 124 -1 N PHE B 119 O ILE B 98 1TSS 163 SHEET 3 SMB 3 ILE B 181 ILE B 183 -1 N ILE B 181 O LEU B 124 1TSS 164 SHEET 1 LRB 5 LYS B 109 SER B 111 0 1TSS 165 SHEET 2 LRB 5 PRO B 101 HIS B 107 -1 N VAL B 106 O LYS B 109 1TSS 166 SHEET 3 LRB 5 GLU B 185 ASN B 194 1 N ILE B 193 O LYS B 105 1TSS 167 SHEET 4 LRB 5 GLY B 151 ASN B 159 -1 N THR B 157 O THR B 188 1TSS 168 SHEET 5 LRB 5 SER B 162 LEU B 168 -1 N SER B 166 O TRP B 154 1TSS 169 SHEET 1 BLC 6 ASP C 18 SER C 29 0 1TSS 170 SHEET 2 BLC 6 GLY C 31 ASN C 37 -1 N ARG C 34 O ASP C 27 1TSS 171 SHEET 3 BLC 6 SER C 41 PHE C 47 -1 N SER C 43 O ILE C 35 1TSS 172 SHEET 4 BLC 6 THR C 79 THR C 89 -1 N HIS C 82 O ILE C 42 1TSS 173 SHEET 5 BLC 6 GLU C 60 THR C 75 -1 N LYS C 70 O PHE C 83 1TSS 174 SHEET 6 BLC 6 ASP C 18 SER C 29 1 N PHE C 20 O LEU C 64 1TSS 175 SHEET 1 SMC 3 GLU C 92 LEU C 100 0 1TSS 176 SHEET 2 SMC 3 PRO C 117 LEU C 124 -1 N PHE C 119 O ILE C 98 1TSS 177 SHEET 3 SMC 3 ILE C 181 ILE C 183 -1 N ILE C 181 O LEU C 124 1TSS 178 SHEET 1 LRC 5 LYS C 109 SER C 111 0 1TSS 179 SHEET 2 LRC 5 PRO C 101 HIS C 107 -1 N VAL C 106 O LYS C 109 1TSS 180 SHEET 3 LRC 5 GLU C 185 ASN C 194 1 N ILE C 193 O LYS C 105 1TSS 181 SHEET 4 LRC 5 GLY C 151 ASN C 159 -1 N THR C 157 O THR C 188 1TSS 182 SHEET 5 LRC 5 SER C 162 LEU C 168 -1 N SER C 166 O TRP C 154 1TSS 183 TURN 1 TA1 SER A 29 SER A 32 SUBUNIT A LOOP 1 1TSS 184 TURN 2 TA2 ASN A 37 GLY A 40 SUBUNIT A LOOP 2 1TSS 185 TURN 3 TA3 THR A 57 GLU A 60 SUBUNIT A LOOP 3 1TSS 186 TURN 4 TA4 THR A 75 GLY A 78 SUBUNIT A LOOP 4 1TSS 187 TURN 5 TA5 VAL A 106 LYS A 109 SUBUNIT A LOOP 5 1TSS 188 TURN 6 TA6 GLY A 142 ARG A 145 SUBUNIT A LOOP 6 1TSS 189 TURN 7 TA7 MET A 158 GLY A 161 SUBUNIT A LOOP 7 1TSS 190 TURN 8 TA8 ASP A 167 LYS A 170 SUBUNIT A LOOP 8 1TSS 191 TURN 9 TA9 ASN A 182 ILE A 186 SUBUNIT A LOOP 9 1TSS 192 TURN 10 TB1 SER B 29 SER B 32 SUBUNIT B LOOP 1 1TSS 193 TURN 11 TB2 ASN B 37 GLY B 40 SUBUNIT B LOOP 2 1TSS 194 TURN 12 TB3 THR B 57 GLU B 60 SUBUNIT B LOOP 3 1TSS 195 TURN 13 TB4 THR B 75 GLY B 78 SUBUNIT B LOOP 4 1TSS 196 TURN 14 TB5 VAL B 106 LYS B 109 SUBUNIT B LOOP 5 1TSS 197 TURN 15 TB6 GLY B 142 ARG B 145 SUBUNIT B LOOP 6 1TSS 198 TURN 16 TB7 MET B 158 GLY B 161 SUBUNIT B LOOP 7 1TSS 199 TURN 17 TB8 ASP B 167 LYS B 170 SUBUNIT B LOOP 8 1TSS 200 TURN 18 TB9 ASN B 182 ILE B 186 SUBUNIT B LOOP 9 1TSS 201 TURN 19 TC1 SER C 29 SER C 32 SUBUNIT C LOOP 1 1TSS 202 TURN 20 TC2 ASN C 37 GLY C 40 SUBUNIT C LOOP 2 1TSS 203 TURN 21 TC3 THR C 57 GLU C 60 SUBUNIT C LOOP 3 1TSS 204 TURN 22 TC4 THR C 75 GLY C 78 SUBUNIT C LOOP 4 1TSS 205 TURN 23 TC5 VAL C 106 LYS C 109 SUBUNIT C LOOP 5 1TSS 206 TURN 24 TC6 GLY C 142 ARG C 145 SUBUNIT C LOOP 6 1TSS 207 TURN 25 TC7 MET C 158 GLY C 161 SUBUNIT C LOOP 7 1TSS 208 TURN 26 TC8 ASP C 167 LYS C 170 SUBUNIT C LOOP 8 1TSS 209 TURN 27 TC9 ASN C 182 ILE C 186 SUBUNIT C LOOP 9 1TSS 210 CRYST1 108.730 177.520 97.560 90.00 90.00 90.00 C 2 2 21 24 1TSS 211 ORIGX1 1.000000 0.000000 0.000000 0.00000 1TSS 212 ORIGX2 0.000000 1.000000 0.000000 0.00000 1TSS 213 ORIGX3 0.000000 0.000000 1.000000 0.00000 1TSS 214 SCALE1 0.009197 0.000000 0.000000 0.00000 1TSS 215 SCALE2 0.000000 0.005633 0.000000 0.00000 1TSS 216 SCALE3 0.000000 0.000000 0.010250 0.00000 1TSS 217 MTRIX1 1 0.471061 -0.882058 0.008625 80.06139 1 1TSS 218 MTRIX2 1 -0.881675 -0.471115 -0.026420 134.73271 1 1TSS 219 MTRIX3 1 0.027363 0.004849 -0.999614 79.96400 1 1TSS 220 MTRIX1 2 -0.569126 -0.822138 0.012066 79.11937 1 1TSS 221 MTRIX2 2 -0.822062 0.568639 -0.029715 42.83922 1 1TSS 222 MTRIX3 2 0.017577 -0.029006 -0.998885 64.86639 1 1TSS 223