HEADER TRANSPORT PROTEIN 07-AUG-25 9PYM TITLE CRYO-EM STRUCTURE OF THE ISETHIONATE TRAP TRANSPORTER ISEQM FROM TITLE 2 OLEIDESULFOVIBRIO ALASKENSIS WITH BOUND ISETHIONATE COMPND MOL_ID: 1; COMPND 2 MOLECULE: ISETHIONATE TRAP TRANSPORTER PERMEASE PROTEIN DCTMQ; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: TRAP TRANSPORTER,FUSED DCTMQ SUBUNIT; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: MEGABODY C7HOPQ; COMPND 8 CHAIN: B; COMPND 9 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: OLEIDESULFOVIBRIO ALASKENSIS G20; SOURCE 3 ORGANISM_TAXID: 207559; SOURCE 4 GENE: DCTMQ, DDE_1274; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: HELICOBACTER PYLORI; SOURCE 9 ORGANISM_TAXID: 210; SOURCE 10 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 11 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS TRAP TRANSPORTER, MEGABODY, ISETHIONATE, TRANSPORT PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR M.C.NEWTON-VESTY,J.S.DAVIES,R.C.J.DOBSON REVDAT 1 12-NOV-25 9PYM 0 JRNL AUTH M.C.NEWTON-VESTY,M.SCALISE,S.A.JAMIESON,M.J.CURRIE, JRNL AUTH 2 H.G.BROWN,S.VALIMEHR,Z.D.TILLETT,K.R.HALL,S.QUAN, JRNL AUTH 3 J.R.ALLISON,A.E.WHITTEN,S.PANJIKAR,C.INDIVERI,E.HANSSEN, JRNL AUTH 4 P.D.MACE,R.A.NORTH,R.C.DOBSON,J.S.DAVIES JRNL TITL STRUCTURAL BASIS OF ISETHIONATE TRANSPORT BY A TRAP JRNL TITL 2 TRANSPORTER FROM A SULFATE-REDUCING BACTERIUM JRNL REF STRUCTURE 2025 JRNL REFN ISSN 0969-2126 JRNL DOI 10.1016/J.STR.2025.10.011 REMARK 2 REMARK 2 RESOLUTION. 2.98 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : CRYOSPARC, CRYOSPARC REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : NULL REMARK 3 REFINEMENT SPACE : NULL REMARK 3 REFINEMENT PROTOCOL : NULL REMARK 3 REFINEMENT TARGET : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL REMARK 3 REMARK 3 FITTING PROCEDURE : NULL REMARK 3 REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 2.980 REMARK 3 NUMBER OF PARTICLES : 83854 REMARK 3 CTF CORRECTION METHOD : PHASE FLIPPING AND AMPLITUDE REMARK 3 CORRECTION REMARK 3 REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL REMARK 3 REMARK 3 OTHER DETAILS: NULL REMARK 4 REMARK 4 9PYM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-AUG-25. REMARK 100 THE DEPOSITION ID IS D_1000298581. REMARK 245 REMARK 245 EXPERIMENTAL DETAILS REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE REMARK 245 SPECIMEN TYPE : NULL REMARK 245 REMARK 245 ELECTRON MICROSCOPE SAMPLE REMARK 245 SAMPLE TYPE : PARTICLE REMARK 245 PARTICLE TYPE : POINT REMARK 245 NAME OF SAMPLE : ISEQM COMPLEXED WITH MEGABODY REMARK 245 C7HOPQ REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 8.00 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : TFS KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 BIOQUANTUM (6K X REMARK 245 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 800.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 1800.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : NULL REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 6600.00 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : NULL REMARK 245 CALIBRATED MAGNIFICATION : NULL REMARK 245 SOURCE : FIELD EMISSION GUN REMARK 245 ACCELERATION VOLTAGE (KV) : 300 REMARK 245 IMAGING DETAILS : NULL REMARK 247 REMARK 247 ELECTRON MICROSCOPY REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION REMARK 247 OF THE STRUCTURE FACTORS. 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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B 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 MET A 1 REMARK 465 SER A 2 REMARK 465 ASP A 3 REMARK 465 PRO A 4 REMARK 465 ASN A 5 REMARK 465 VAL A 6 REMARK 465 THR A 7 REMARK 465 ALA A 8 REMARK 465 THR A 9 REMARK 465 ILE A 10 REMARK 465 MET A 11 REMARK 465 ASN A 12 REMARK 465 ALA A 13 REMARK 465 GLN A 14 REMARK 465 GLY A 15 REMARK 465 GLU A 16 REMARK 465 CYS A 17 REMARK 465 SER A 18 REMARK 465 SER A 19 REMARK 465 GLY A 20 REMARK 465 SER A 21 REMARK 465 LEU A 22 REMARK 465 GLU A 23 REMARK 465 SER A 24 REMARK 465 ARG A 25 REMARK 465 PRO A 26 REMARK 465 GLY A 27 REMARK 465 ILE A 28 REMARK 465 VAL A 63 REMARK 465 TYR A 64 REMARK 465 LEU A 65 REMARK 465 HIS A 66 REMARK 465 GLU A 67 REMARK 465 GLY A 68 REMARK 465 ALA A 69 REMARK 465 ALA A 70 REMARK 465 ALA A 71 REMARK 465 ALA A 72 REMARK 465 ARG A 470 REMARK 465 GLU A 471 REMARK 465 LEU A 472 REMARK 465 SER A 473 REMARK 465 GLY A 635 REMARK 465 THR B 14 REMARK 465 LYS B 15 REMARK 465 THR B 16 REMARK 465 THR B 17 REMARK 465 THR B 18 REMARK 465 SER B 19 REMARK 465 VAL B 20 REMARK 465 ILE B 21 REMARK 465 ASP B 22 REMARK 465 THR B 23 REMARK 465 THR B 24 REMARK 465 ASN B 25 REMARK 465 ASP B 26 REMARK 465 ALA B 27 REMARK 465 GLN B 28 REMARK 465 ASN B 29 REMARK 465 LEU B 30 REMARK 465 LEU B 31 REMARK 465 THR B 32 REMARK 465 GLN B 33 REMARK 465 ALA B 34 REMARK 465 GLN B 35 REMARK 465 THR B 36 REMARK 465 ILE B 37 REMARK 465 VAL B 38 REMARK 465 ASN B 39 REMARK 465 THR B 40 REMARK 465 LEU B 41 REMARK 465 LYS B 42 REMARK 465 ASP B 43 REMARK 465 TYR B 44 REMARK 465 CYS B 45 REMARK 465 PRO B 46 REMARK 465 ILE B 47 REMARK 465 LEU B 48 REMARK 465 ILE B 49 REMARK 465 ALA B 50 REMARK 465 LYS B 51 REMARK 465 SER B 52 REMARK 465 SER B 53 REMARK 465 SER B 54 REMARK 465 SER B 55 REMARK 465 ASN B 56 REMARK 465 GLY B 57 REMARK 465 GLY B 58 REMARK 465 THR B 59 REMARK 465 ASN B 60 REMARK 465 ASN B 61 REMARK 465 ALA B 62 REMARK 465 ASN B 63 REMARK 465 THR B 64 REMARK 465 PRO B 65 REMARK 465 SER B 66 REMARK 465 TRP B 67 REMARK 465 GLN B 68 REMARK 465 THR B 69 REMARK 465 ALA B 70 REMARK 465 GLY B 71 REMARK 465 GLY B 72 REMARK 465 GLY B 73 REMARK 465 LYS B 74 REMARK 465 ASN B 75 REMARK 465 SER B 76 REMARK 465 CYS B 77 REMARK 465 ALA B 78 REMARK 465 THR B 79 REMARK 465 PHE B 80 REMARK 465 GLY B 81 REMARK 465 ALA B 82 REMARK 465 GLU B 83 REMARK 465 PHE B 84 REMARK 465 SER B 85 REMARK 465 ALA B 86 REMARK 465 ALA B 87 REMARK 465 SER B 88 REMARK 465 ASP B 89 REMARK 465 MET B 90 REMARK 465 ILE B 91 REMARK 465 ASN B 92 REMARK 465 ASN B 93 REMARK 465 ALA B 94 REMARK 465 GLN B 95 REMARK 465 LYS B 96 REMARK 465 ILE B 97 REMARK 465 VAL B 98 REMARK 465 GLN B 99 REMARK 465 GLU B 100 REMARK 465 THR B 101 REMARK 465 GLN B 102 REMARK 465 GLN B 103 REMARK 465 LEU B 104 REMARK 465 SER B 105 REMARK 465 ALA B 106 REMARK 465 ASN B 107 REMARK 465 GLN B 108 REMARK 465 PRO B 109 REMARK 465 LYS B 110 REMARK 465 ASN B 111 REMARK 465 ILE B 112 REMARK 465 THR B 113 REMARK 465 GLN B 114 REMARK 465 PRO B 115 REMARK 465 HIS B 116 REMARK 465 ASN B 117 REMARK 465 LEU B 118 REMARK 465 ASN B 119 REMARK 465 LEU B 120 REMARK 465 ASN B 121 REMARK 465 SER B 122 REMARK 465 PRO B 123 REMARK 465 SER B 124 REMARK 465 SER B 125 REMARK 465 LEU B 126 REMARK 465 THR B 127 REMARK 465 ALA B 128 REMARK 465 LEU B 129 REMARK 465 ALA B 130 REMARK 465 GLN B 131 REMARK 465 LYS B 132 REMARK 465 MET B 133 REMARK 465 LEU B 134 REMARK 465 LYS B 135 REMARK 465 ASN B 136 REMARK 465 ALA B 137 REMARK 465 GLN B 138 REMARK 465 SER B 139 REMARK 465 GLN B 140 REMARK 465 ALA B 141 REMARK 465 GLU B 142 REMARK 465 ILE B 143 REMARK 465 LEU B 144 REMARK 465 LYS B 145 REMARK 465 LEU B 146 REMARK 465 ALA B 147 REMARK 465 ASN B 148 REMARK 465 GLN B 149 REMARK 465 VAL B 150 REMARK 465 GLU B 151 REMARK 465 SER B 152 REMARK 465 ASP B 153 REMARK 465 PHE B 154 REMARK 465 ASN B 155 REMARK 465 LYS B 156 REMARK 465 LEU B 157 REMARK 465 SER B 158 REMARK 465 SER B 159 REMARK 465 GLY B 160 REMARK 465 HIS B 161 REMARK 465 LEU B 162 REMARK 465 LYS B 163 REMARK 465 ASP B 164 REMARK 465 TYR B 165 REMARK 465 ILE B 166 REMARK 465 GLY B 167 REMARK 465 LYS B 168 REMARK 465 CYS B 169 REMARK 465 ASP B 170 REMARK 465 ALA B 171 REMARK 465 SER B 172 REMARK 465 ALA B 173 REMARK 465 ILE B 174 REMARK 465 SER B 175 REMARK 465 SER B 176 REMARK 465 ALA B 177 REMARK 465 ASN B 178 REMARK 465 MET B 179 REMARK 465 THR B 180 REMARK 465 MET B 181 REMARK 465 GLN B 182 REMARK 465 ASN B 183 REMARK 465 GLN B 184 REMARK 465 LYS B 185 REMARK 465 ASN B 186 REMARK 465 ASN B 187 REMARK 465 TRP B 188 REMARK 465 GLY B 189 REMARK 465 ASN B 190 REMARK 465 GLY B 191 REMARK 465 CYS B 192 REMARK 465 ALA B 193 REMARK 465 GLY B 194 REMARK 465 VAL B 195 REMARK 465 GLU B 196 REMARK 465 GLU B 197 REMARK 465 THR B 198 REMARK 465 GLN B 199 REMARK 465 SER B 200 REMARK 465 LEU B 201 REMARK 465 LEU B 202 REMARK 465 LYS B 203 REMARK 465 THR B 204 REMARK 465 SER B 205 REMARK 465 ALA B 206 REMARK 465 ALA B 207 REMARK 465 ASP B 208 REMARK 465 PHE B 209 REMARK 465 ASN B 210 REMARK 465 ASN B 211 REMARK 465 GLN B 212 REMARK 465 THR B 213 REMARK 465 PRO B 214 REMARK 465 GLN B 215 REMARK 465 ILE B 216 REMARK 465 ASN B 217 REMARK 465 GLN B 218 REMARK 465 ALA B 219 REMARK 465 GLN B 220 REMARK 465 ASN B 221 REMARK 465 LEU B 222 REMARK 465 ALA B 223 REMARK 465 ASN B 224 REMARK 465 THR B 225 REMARK 465 LEU B 226 REMARK 465 ILE B 227 REMARK 465 GLN B 228 REMARK 465 GLU B 229 REMARK 465 LEU B 230 REMARK 465 GLY B 231 REMARK 465 ASN B 232 REMARK 465 ASN B 233 REMARK 465 THR B 234 REMARK 465 TYR B 235 REMARK 465 GLU B 236 REMARK 465 GLN B 237 REMARK 465 LEU B 238 REMARK 465 SER B 239 REMARK 465 ARG B 240 REMARK 465 LEU B 241 REMARK 465 LEU B 242 REMARK 465 THR B 243 REMARK 465 ASN B 244 REMARK 465 ASP B 245 REMARK 465 ASN B 246 REMARK 465 GLY B 247 REMARK 465 THR B 248 REMARK 465 ASN B 249 REMARK 465 SER B 250 REMARK 465 LYS B 251 REMARK 465 THR B 252 REMARK 465 SER B 253 REMARK 465 ALA B 254 REMARK 465 GLN B 255 REMARK 465 ALA B 256 REMARK 465 ILE B 257 REMARK 465 ASN B 258 REMARK 465 GLN B 259 REMARK 465 ALA B 260 REMARK 465 VAL B 261 REMARK 465 ASN B 262 REMARK 465 ASN B 263 REMARK 465 LEU B 264 REMARK 465 ASN B 265 REMARK 465 GLU B 266 REMARK 465 ARG B 267 REMARK 465 ALA B 268 REMARK 465 LYS B 269 REMARK 465 THR B 270 REMARK 465 LEU B 271 REMARK 465 ALA B 272 REMARK 465 GLY B 273 REMARK 465 GLY B 274 REMARK 465 THR B 275 REMARK 465 THR B 276 REMARK 465 ASN B 277 REMARK 465 SER B 278 REMARK 465 PRO B 279 REMARK 465 ALA B 280 REMARK 465 TYR B 281 REMARK 465 GLN B 282 REMARK 465 ALA B 283 REMARK 465 THR B 284 REMARK 465 LEU B 285 REMARK 465 LEU B 286 REMARK 465 ALA B 287 REMARK 465 LEU B 288 REMARK 465 ARG B 289 REMARK 465 SER B 290 REMARK 465 VAL B 291 REMARK 465 LEU B 292 REMARK 465 GLY B 293 REMARK 465 LEU B 294 REMARK 465 TRP B 295 REMARK 465 ASN B 296 REMARK 465 SER B 297 REMARK 465 MET B 298 REMARK 465 GLY B 299 REMARK 465 TYR B 300 REMARK 465 ALA B 301 REMARK 465 VAL B 302 REMARK 465 ILE B 303 REMARK 465 CYS B 304 REMARK 465 GLY B 305 REMARK 465 GLY B 306 REMARK 465 TYR B 307 REMARK 465 THR B 308 REMARK 465 LYS B 309 REMARK 465 SER B 310 REMARK 465 PRO B 311 REMARK 465 GLY B 312 REMARK 465 GLU B 313 REMARK 465 ASN B 314 REMARK 465 ASN B 315 REMARK 465 GLN B 316 REMARK 465 LYS B 317 REMARK 465 ASP B 318 REMARK 465 PHE B 319 REMARK 465 HIS B 320 REMARK 465 TYR B 321 REMARK 465 THR B 322 REMARK 465 ASP B 323 REMARK 465 GLU B 324 REMARK 465 ASN B 325 REMARK 465 GLY B 326 REMARK 465 ASN B 327 REMARK 465 GLY B 328 REMARK 465 THR B 329 REMARK 465 THR B 330 REMARK 465 ILE B 331 REMARK 465 ASN B 332 REMARK 465 CYS B 333 REMARK 465 GLY B 334 REMARK 465 GLY B 335 REMARK 465 SER B 336 REMARK 465 THR B 337 REMARK 465 ASN B 338 REMARK 465 SER B 339 REMARK 465 ASN B 340 REMARK 465 GLY B 341 REMARK 465 THR B 342 REMARK 465 HIS B 343 REMARK 465 SER B 344 REMARK 465 TYR B 345 REMARK 465 ASN B 346 REMARK 465 GLY B 347 REMARK 465 THR B 348 REMARK 465 ASN B 349 REMARK 465 THR B 350 REMARK 465 LEU B 351 REMARK 465 LYS B 352 REMARK 465 ALA B 353 REMARK 465 ASP B 354 REMARK 465 LYS B 355 REMARK 465 ASN B 356 REMARK 465 VAL B 357 REMARK 465 SER B 358 REMARK 465 LEU B 359 REMARK 465 SER B 360 REMARK 465 ILE B 361 REMARK 465 GLU B 362 REMARK 465 GLN B 363 REMARK 465 TYR B 364 REMARK 465 GLU B 365 REMARK 465 LYS B 366 REMARK 465 ILE B 367 REMARK 465 HIS B 368 REMARK 465 GLU B 369 REMARK 465 ALA B 370 REMARK 465 TYR B 371 REMARK 465 GLN B 372 REMARK 465 ILE B 373 REMARK 465 LEU B 374 REMARK 465 SER B 375 REMARK 465 LYS B 376 REMARK 465 ALA B 377 REMARK 465 LEU B 378 REMARK 465 LYS B 379 REMARK 465 GLN B 380 REMARK 465 ALA B 381 REMARK 465 GLY B 382 REMARK 465 LEU B 383 REMARK 465 ALA B 384 REMARK 465 PRO B 385 REMARK 465 LEU B 386 REMARK 465 ASN B 387 REMARK 465 SER B 388 REMARK 465 LYS B 389 REMARK 465 GLY B 390 REMARK 465 GLU B 391 REMARK 465 LYS B 392 REMARK 465 LEU B 393 REMARK 465 GLU B 394 REMARK 465 ALA B 395 REMARK 465 HIS B 396 REMARK 465 VAL B 397 REMARK 465 THR B 398 REMARK 465 THR B 399 REMARK 465 SER B 400 REMARK 465 LYS B 401 REMARK 465 TYR B 402 REMARK 465 ALA B 403 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 O GLN A 257 HG1 THR A 261 1.58 REMARK 500 O VAL A 327 H GLY A 331 1.58 REMARK 500 O ILE A 49 HG1 THR A 53 1.59 REMARK 500 OD1 ASN A 418 H LYS A 420 1.60 REMARK 500 OG SER A 322 O4 8X3 A 702 1.95 REMARK 500 NH1 ARG A 80 OD1 ASP A 264 2.13 REMARK 500 OG SER B 406 O MET B 471 2.16 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 ILE A 319 -60.58 -108.40 REMARK 500 ARG A 415 145.41 -171.78 REMARK 500 CYS A 466 -37.19 -133.85 REMARK 500 PRO A 627 -6.17 -59.21 REMARK 500 MET A 631 37.63 -99.45 REMARK 500 PHE A 633 -60.49 -90.81 REMARK 500 ALA B 444 45.76 70.59 REMARK 500 THR B 479 26.91 -142.63 REMARK 500 REMARK 500 REMARK: NULL REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 PTY A 703 REMARK 610 PTY A 704 REMARK 610 PTY A 705 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 NA A 701 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ALA A 317 O REMARK 620 2 SER A 320 O 87.0 REMARK 620 3 GLY A 359 O 118.6 101.6 REMARK 620 4 ILE A 362 O 90.4 168.2 89.7 REMARK 620 5 PRO A 364 O 137.6 102.8 99.9 71.6 REMARK 620 N 1 2 3 4 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-72036 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF THE ISETHIONATE TRAP TRANSPORTER ISEQM FROM REMARK 900 OLEIDESULFOVIBRIO ALASKENSIS WITH BOUND ISETHIONATE DBREF 9PYM A 1 635 UNP Q312S1 DCTMQ_OLEA2 1 635 DBREF 9PYM B 1 515 PDB 9PYM 9PYM 1 515 SEQRES 1 A 635 MET SER ASP PRO ASN VAL THR ALA THR ILE MET ASN ALA SEQRES 2 A 635 GLN GLY GLU CYS SER SER GLY SER LEU GLU SER ARG PRO SEQRES 3 A 635 GLY ILE LEU GLY TRP LEU ASP ALA ASN PHE GLU LYS PRO SEQRES 4 A 635 PHE LEU VAL ALA GLY MET LEU ALA ILE ILE PHE ILE ILE SEQRES 5 A 635 THR PHE GLN THR LEU TYR ARG TYR ILE GLY VAL TYR LEU SEQRES 6 A 635 HIS GLU GLY ALA ALA ALA ALA VAL TRP THR GLU GLU MET SEQRES 7 A 635 ALA ARG PHE ILE PHE ILE TRP ILE SER TYR LEU ALA VAL SEQRES 8 A 635 PRO VAL ALA ILE LYS ASN ARG SER SER ILE ARG VAL ASP SEQRES 9 A 635 ILE ILE PHE ASP ARG LEU PRO VAL ARG PHE GLN ASN ILE SEQRES 10 A 635 SER TRP ILE ILE VAL ASP VAL CYS PHE LEU THR LEU ALA SEQRES 11 A 635 ALA THR VAL LEU TRP GLN SER LEU ASP LEU ILE LYS MET SEQRES 12 A 635 GLN LEU THR TYR PRO GLN THR SER PRO ALA LEU GLN LEU SEQRES 13 A 635 PRO TYR TYR ILE PRO TYR LEU VAL LEU PRO VAL SER PHE SEQRES 14 A 635 GLY LEU MET ALA VAL ARG LEU LEU GLN ASP LEU ALA GLY SEQRES 15 A 635 GLN VAL ARG ILE CYS GLY ALA ALA ASP THR VAL ILE GLY SEQRES 16 A 635 LEU ILE LEU CYS ALA VAL LEU ALA ALA PRO LEU PHE ILE SEQRES 17 A 635 ALA ASP TYR ILE ASP PRO LEU PRO VAL LEU PHE GLY TYR SEQRES 18 A 635 PHE ALA LEU PHE LEU VAL VAL GLY VAL PRO ILE ALA ILE SEQRES 19 A 635 GLY LEU GLY LEU ALA ALA LEU ALA THR ILE VAL ALA ALA SEQRES 20 A 635 GLY SER LEU PRO ILE ASP TYR VAL ALA GLN ILE ALA PHE SEQRES 21 A 635 THR SER ILE ASP SER PHE PRO ILE MET ALA ILE PRO PHE SEQRES 22 A 635 PHE ILE ALA ALA GLY VAL PHE MET GLY ALA GLY GLY LEU SEQRES 23 A 635 SER ARG ARG LEU LEU ASN LEU ALA ASP GLU MET LEU GLY SEQRES 24 A 635 ALA LEU PRO GLY GLY MET ALA LEU ALA THR ILE GLY THR SEQRES 25 A 635 CYS MET PHE PHE ALA ALA ILE SER GLY SER GLY PRO ALA SEQRES 26 A 635 THR VAL ALA ALA ILE GLY SER LEU THR ILE PRO ALA MET SEQRES 27 A 635 VAL GLU ARG GLY TYR CYS LYS TYR PHE SER ALA ALA ILE SEQRES 28 A 635 VAL ALA ALA ALA GLY ALA ILE GLY VAL MET ILE PRO PRO SEQRES 29 A 635 SER ASN PRO PHE VAL VAL TYR GLY VAL SER ALA GLN ALA SEQRES 30 A 635 SER ILE GLY LYS LEU PHE MET GLY GLY ILE VAL PRO GLY SEQRES 31 A 635 LEU LEU THR GLY LEU ALA LEU MET ALA TYR SER TYR TRP SEQRES 32 A 635 TYR SER LYS LYS ARG GLY TRP LYS GLY GLU VAL ARG ASP SEQRES 33 A 635 ARG ASN LEU LYS THR PHE MET HIS ALA VAL TRP GLU ALA SEQRES 34 A 635 LYS TRP ALA LEU MET VAL PRO VAL ILE VAL LEU GLY GLY SEQRES 35 A 635 ILE TYR GLY GLY ILE MET THR PRO THR GLU ALA ALA ALA SEQRES 36 A 635 LEU ALA ALA PHE TYR GLY LEU ILE ILE GLY CYS PHE VAL SEQRES 37 A 635 HIS ARG GLU LEU SER CYS GLY SER PHE TYR ASP CYS VAL SEQRES 38 A 635 VAL GLU ALA ALA GLY THR SER ALA MET VAL ILE VAL LEU SEQRES 39 A 635 MET SER MET ALA THR ILE PHE GLY ASN ILE MET THR ILE SEQRES 40 A 635 GLU GLU VAL PRO THR THR ILE ALA GLN ALA MET LEU GLY SEQRES 41 A 635 LEU THR THR ASP LYS ILE ALA ILE LEU LEU MET ILE ASN SEQRES 42 A 635 VAL LEU LEU LEU ILE ILE GLY THR PHE MET GLU ALA LEU SEQRES 43 A 635 ALA ALA ILE VAL ILE LEU THR PRO ILE LEU LEU PRO ILE SEQRES 44 A 635 VAL LEU LYS VAL GLY VAL ASP PRO VAL HIS PHE GLY ILE SEQRES 45 A 635 ILE MET VAL VAL ASN LEU ALA ILE GLY PHE VAL THR PRO SEQRES 46 A 635 PRO VAL GLY VAL ASN LEU PHE VAL ALA SER GLY VAL ALA SEQRES 47 A 635 ASN ALA LYS ILE GLU GLN LEU SER LYS VAL VAL LEU PRO SEQRES 48 A 635 LEU ILE ALA LEU MET LEU ALA VAL LEU LEU ILE THR THR SEQRES 49 A 635 TYR VAL PRO ALA ILE PRO MET PHE PHE ALA GLY SEQRES 1 B 515 GLN VAL SER LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 B 515 THR LYS THR THR THR SER VAL ILE ASP THR THR ASN ASP SEQRES 3 B 515 ALA GLN ASN LEU LEU THR GLN ALA GLN THR ILE VAL ASN SEQRES 4 B 515 THR LEU LYS ASP TYR CYS PRO ILE LEU ILE ALA LYS SER SEQRES 5 B 515 SER SER SER ASN GLY GLY THR ASN ASN ALA ASN THR PRO SEQRES 6 B 515 SER TRP GLN THR ALA GLY GLY GLY LYS ASN SER CYS ALA SEQRES 7 B 515 THR PHE GLY ALA GLU PHE SER ALA ALA SER ASP MET ILE SEQRES 8 B 515 ASN ASN ALA GLN LYS ILE VAL GLN GLU THR GLN GLN LEU SEQRES 9 B 515 SER ALA ASN GLN PRO LYS ASN ILE THR GLN PRO HIS ASN SEQRES 10 B 515 LEU ASN LEU ASN SER PRO SER SER LEU THR ALA LEU ALA SEQRES 11 B 515 GLN LYS MET LEU LYS ASN ALA GLN SER GLN ALA GLU ILE SEQRES 12 B 515 LEU LYS LEU ALA ASN GLN VAL GLU SER ASP PHE ASN LYS SEQRES 13 B 515 LEU SER SER GLY HIS LEU LYS ASP TYR ILE GLY LYS CYS SEQRES 14 B 515 ASP ALA SER ALA ILE SER SER ALA ASN MET THR MET GLN SEQRES 15 B 515 ASN GLN LYS ASN ASN TRP GLY ASN GLY CYS ALA GLY VAL SEQRES 16 B 515 GLU GLU THR GLN SER LEU LEU LYS THR SER ALA ALA ASP SEQRES 17 B 515 PHE ASN ASN GLN THR PRO GLN ILE ASN GLN ALA GLN ASN SEQRES 18 B 515 LEU ALA ASN THR LEU ILE GLN GLU LEU GLY ASN ASN THR SEQRES 19 B 515 TYR GLU GLN LEU SER ARG LEU LEU THR ASN ASP ASN GLY SEQRES 20 B 515 THR ASN SER LYS THR SER ALA GLN ALA ILE ASN GLN ALA SEQRES 21 B 515 VAL ASN ASN LEU ASN GLU ARG ALA LYS THR LEU ALA GLY SEQRES 22 B 515 GLY THR THR ASN SER PRO ALA TYR GLN ALA THR LEU LEU SEQRES 23 B 515 ALA LEU ARG SER VAL LEU GLY LEU TRP ASN SER MET GLY SEQRES 24 B 515 TYR ALA VAL ILE CYS GLY GLY TYR THR LYS SER PRO GLY SEQRES 25 B 515 GLU ASN ASN GLN LYS ASP PHE HIS TYR THR ASP GLU ASN SEQRES 26 B 515 GLY ASN GLY THR THR ILE ASN CYS GLY GLY SER THR ASN SEQRES 27 B 515 SER ASN GLY THR HIS SER TYR ASN GLY THR ASN THR LEU SEQRES 28 B 515 LYS ALA ASP LYS ASN VAL SER LEU SER ILE GLU GLN TYR SEQRES 29 B 515 GLU LYS ILE HIS GLU ALA TYR GLN ILE LEU SER LYS ALA SEQRES 30 B 515 LEU LYS GLN ALA GLY LEU ALA PRO LEU ASN SER LYS GLY SEQRES 31 B 515 GLU LYS LEU GLU ALA HIS VAL THR THR SER LYS TYR ALA SEQRES 32 B 515 GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY ASN SEQRES 33 B 515 ILE PHE LEU TRP ALA ASN MET GLY TRP TYR ARG GLN ALA SEQRES 34 B 515 PRO GLY LYS GLU ARG GLU PHE VAL ALA SER ILE SER LEU SEQRES 35 B 515 GLY ALA ASN THR ASN TYR ALA ASP SER VAL LYS GLY ARG SEQRES 36 B 515 PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR VAL TYR SEQRES 37 B 515 LEU GLN MET ASN SER LEU LYS GLN GLU ASP THR ALA VAL SEQRES 38 B 515 TYR TYR CYS ALA VAL TRP ALA ARG TYR PRO SER THR TYR SEQRES 39 B 515 TYR LEU GLY ARG GLY TYR ASP TYR LEU TYR TRP GLY GLN SEQRES 40 B 515 GLY THR GLN VAL THR VAL SER SER HET NA A 701 1 HET 8X3 A 702 12 HET PTY A 703 49 HET PTY A 704 61 HET PTY A 705 85 HETNAM NA SODIUM ION HETNAM 8X3 2-HYDROXYETHYLSULFONIC ACID HETNAM PTY PHOSPHATIDYLETHANOLAMINE HETSYN 8X3 2-OXIDANYLETHANESULFONIC ACID FORMUL 3 NA NA 1+ FORMUL 4 8X3 C2 H6 O4 S FORMUL 5 PTY 3(C40 H80 N O8 P) HELIX 1 AA1 LEU A 29 PHE A 36 1 8 HELIX 2 AA2 GLU A 37 GLY A 62 1 26 HELIX 3 AA3 TRP A 74 ASN A 97 1 24 HELIX 4 AA4 PRO A 111 TYR A 147 1 37 HELIX 5 AA5 ILE A 160 TYR A 162 5 3 HELIX 6 AA6 LEU A 163 GLY A 188 1 26 HELIX 7 AA7 GLY A 188 ALA A 209 1 22 HELIX 8 AA8 ASP A 213 GLY A 229 1 17 HELIX 9 AA9 PRO A 231 ALA A 247 1 17 HELIX 10 AB1 ASP A 253 SER A 262 1 10 HELIX 11 AB2 PHE A 266 ILE A 268 5 3 HELIX 12 AB3 MET A 269 ALA A 283 1 15 HELIX 13 AB4 LEU A 286 GLY A 299 1 14 HELIX 14 AB5 GLY A 303 ALA A 318 1 16 HELIX 15 AB6 SER A 322 GLY A 342 1 21 HELIX 16 AB7 CYS A 344 ALA A 357 1 14 HELIX 17 AB8 ALA A 357 ILE A 362 1 6 HELIX 18 AB9 SER A 365 ALA A 375 1 11 HELIX 19 AC1 SER A 378 GLY A 386 1 9 HELIX 20 AC2 GLY A 386 GLY A 409 1 24 HELIX 21 AC3 ASN A 418 ALA A 429 1 12 HELIX 22 AC4 ALA A 429 GLY A 445 1 17 HELIX 23 AC5 THR A 449 PHE A 467 1 19 HELIX 24 AC6 GLY A 475 GLU A 508 1 34 HELIX 25 AC7 GLU A 509 THR A 522 1 14 HELIX 26 AC8 ASP A 524 THR A 541 1 18 HELIX 27 AC9 GLU A 544 VAL A 563 1 20 HELIX 28 AD1 ASP A 566 ILE A 580 1 15 HELIX 29 AD2 GLY A 581 THR A 584 5 4 HELIX 30 AD3 ASN A 590 ASN A 599 1 10 HELIX 31 AD4 LYS A 601 VAL A 626 1 26 SHEET 1 AA1 4 SER B 3 SER B 7 0 SHEET 2 AA1 4 LEU B 409 SER B 414 -1 O SER B 410 N SER B 7 SHEET 3 AA1 4 THR B 466 GLN B 470 -1 O VAL B 467 N CYS B 411 SHEET 4 AA1 4 THR B 457 ASP B 461 -1 N THR B 457 O GLN B 470 SHEET 1 AA2 5 THR B 446 TYR B 448 0 SHEET 2 AA2 5 ALA B 438 ILE B 440 -1 N SER B 439 O ASN B 447 SHEET 3 AA2 5 ASN B 422 GLN B 428 -1 N TRP B 425 O ALA B 438 SHEET 4 AA2 5 VAL B 481 TRP B 487 -1 O TYR B 483 N TYR B 426 SHEET 5 AA2 5 TYR B 504 TRP B 505 -1 O TYR B 504 N VAL B 486 SHEET 1 AA3 2 THR B 493 TYR B 494 0 SHEET 2 AA3 2 GLY B 499 TYR B 500 -1 O TYR B 500 N THR B 493 SSBOND 1 CYS B 411 CYS B 484 1555 1555 2.03 LINK O ALA A 317 NA NA A 701 1555 1555 2.05 LINK O SER A 320 NA NA A 701 1555 1555 2.47 LINK O GLY A 359 NA NA A 701 1555 1555 2.05 LINK O ILE A 362 NA NA A 701 1555 1555 2.48 LINK O PRO A 364 NA NA A 701 1555 1555 2.24 CISPEP 1 PRO A 363 PRO A 364 0 3.71 CISPEP 2 PRO A 585 PRO A 586 0 2.25 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 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 1.000000 0.000000 0.000000 0.00000 SCALE2 0.000000 1.000000 0.000000 0.00000 SCALE3 0.000000 0.000000 1.000000 0.00000