HEADER CELL INVASION/IMMUNE SYSTEM 01-SEP-23 8U1P TITLE LOCAL REFINEMENT OF PLASMODIUM FALCIPARUM GAMETOCYTE SURFACE PROTEIN TITLE 2 PFS48/45 DOMAINS 1 AND 2 IN COMPLEX WITH NEUTRALIZING ANTIBODIES COMPND MOL_ID: 1; COMPND 2 MOLECULE: GAMETOCYTE SURFACE PROTEIN P45/48; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: RUPA154 FAB HEAVY CHAIN; COMPND 7 CHAIN: H; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: RUPA154 FAB LIGHT CHAIN; COMPND 11 CHAIN: L; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 4; COMPND 14 MOLECULE: RUPA58 FAB LIGHT CHAIN; COMPND 15 CHAIN: C; COMPND 16 ENGINEERED: YES; COMPND 17 MOL_ID: 5; COMPND 18 MOLECULE: RUPA58 FAB HEAVY CHAIN; COMPND 19 CHAIN: B; COMPND 20 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: PLASMODIUM FALCIPARUM 3D7; SOURCE 3 ORGANISM_TAXID: 36329; SOURCE 4 GENE: PF45/48; SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 9 ORGANISM_TAXID: 9606; SOURCE 10 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 11 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 12 MOL_ID: 3; SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 14 ORGANISM_TAXID: 9606; SOURCE 15 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 16 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 17 MOL_ID: 4; SOURCE 18 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 19 ORGANISM_TAXID: 9606; SOURCE 20 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 21 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 22 MOL_ID: 5; SOURCE 23 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 24 ORGANISM_TAXID: 9606; SOURCE 25 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 26 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS TRANSMISSION BLOCKING VACCINE, ANTIBODY, MALARIA, CELL INVASION, CELL KEYWDS 2 INVASION-IMMUNE SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR I.KUCHARSKA,S.HAILEMARIAM,D.IVANOCHKO,J.RUBINSTEIN,J.P.JULIEN REVDAT 1 12-MAR-25 8U1P 0 JRNL AUTH I.KUCHARSKA,D.IVANOCHKO,S.HAILEMARIAM,M.R.INKLAAR,K.TEELEN, JRNL AUTH 2 R.STOTER,M.VAN DE VEGTE-BOLMER,G.J.VAN GEMERT,A.SEMESI, JRNL AUTH 3 B.MCLEOD,J.RUBINSTEIN,M.M.JORE,J.P.JULIEN JRNL TITL STRUCTURAL ELUCIDATION OF FULL-LENGTH PFS48/45 IN COMPLEX JRNL TITL 2 WITH POTENT MABS ISOLATED FROM A NATURALLY EXPOSED JRNL TITL 3 INDIVIDUAL JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.30 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : CRYOSPARC, EPU, CRYOSPARC, UCSF REMARK 3 CHIMERA, CRYOSPARC, CRYOSPARC, PHENIX REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : 7ZXG REMARK 3 REFINEMENT SPACE : REAL REMARK 3 REFINEMENT PROTOCOL : FLEXIBLE FIT 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) : 3.300 REMARK 3 NUMBER OF PARTICLES : 306744 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: LOCAL REFINEMENT WAS PERFORMED WITH A MASK REMARK 3 INCLUDING DOMAINS D1 AND D2 OF PFS48/45 AND VARIABLE REGIONS OF REMARK 3 RUPA-58 AND RUPA-154 FABS REMARK 4 REMARK 4 8U1P COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-SEP-23. REMARK 100 THE DEPOSITION ID IS D_1000268511. 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 : COMPLEX OF PFS48/45, RUPA58 AND REMARK 245 RUPA154 REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 0.50 REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : SAMPLE WAS FROZEN WITH LEICA REMARK 245 AUTOMATIC PLUNGE FREEZER EM GP2 REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.00 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : 7744 REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS REMARK 245 DETECTOR TYPE : FEI FALCON IV (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 500.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2000.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : 2.70 REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 4869.00 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : 75000 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: PENTAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, H, L, C, B, D, E 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 ASN A 28 REMARK 465 ASN A 29 REMARK 465 ASP A 30 REMARK 465 PHE A 31 REMARK 465 CYS A 32 REMARK 465 LYS A 33 REMARK 465 PRO A 34 REMARK 465 SER A 35 REMARK 465 SER A 36 REMARK 465 LEU A 37 REMARK 465 ASN A 38 REMARK 465 SER A 39 REMARK 465 GLU A 40 REMARK 465 ILE A 41 REMARK 465 PHE A 51 REMARK 465 SER A 52 REMARK 465 ASN A 53 REMARK 465 GLU A 54 REMARK 465 GLY A 55 REMARK 465 VAL A 56 REMARK 465 HIS A 57 REMARK 465 ASN A 58 REMARK 465 LEU A 59 REMARK 465 LYS A 60 REMARK 465 PRO A 61 REMARK 465 ASP A 62 REMARK 465 MET A 63 REMARK 465 ARG A 64 REMARK 465 GLU A 65 REMARK 465 ARG A 66 REMARK 465 ARG A 67 REMARK 465 SER A 68 REMARK 465 ILE A 69 REMARK 465 CYS A 158 REMARK 465 ASP A 159 REMARK 465 ASN A 160 REMARK 465 THR A 161 REMARK 465 GLU A 162 REMARK 465 LYS A 163 REMARK 465 VAL A 164 REMARK 465 ILE A 165 REMARK 465 SER A 166 REMARK 465 SER A 167 REMARK 465 ILE A 168 REMARK 465 GLU A 169 REMARK 465 GLY A 170 REMARK 465 ARG A 171 REMARK 465 SER A 172 REMARK 465 ALA A 173 REMARK 465 LYS A 289 REMARK 465 TYR A 290 REMARK 465 GLU A 291 REMARK 465 LYS A 292 REMARK 465 LYS A 293 REMARK 465 VAL A 294 REMARK 465 ILE A 295 REMARK 465 HIS A 296 REMARK 465 GLY A 297 REMARK 465 CYS A 298 REMARK 465 ASN A 299 REMARK 465 PHE A 300 REMARK 465 SER A 301 REMARK 465 SER A 302 REMARK 465 ASN A 303 REMARK 465 VAL A 304 REMARK 465 SER A 305 REMARK 465 SER A 306 REMARK 465 LYS A 307 REMARK 465 TYR A 308 REMARK 465 THR A 309 REMARK 465 PHE A 310 REMARK 465 THR A 311 REMARK 465 ASP A 312 REMARK 465 SER A 313 REMARK 465 LEU A 314 REMARK 465 ASP A 315 REMARK 465 ILE A 316 REMARK 465 SER A 317 REMARK 465 LEU A 318 REMARK 465 VAL A 319 REMARK 465 ASP A 320 REMARK 465 ASP A 321 REMARK 465 SER A 322 REMARK 465 ALA A 323 REMARK 465 HIS A 324 REMARK 465 ILE A 325 REMARK 465 SER A 326 REMARK 465 CYS A 327 REMARK 465 ASN A 328 REMARK 465 VAL A 329 REMARK 465 HIS A 330 REMARK 465 LEU A 331 REMARK 465 SER A 332 REMARK 465 GLU A 333 REMARK 465 PRO A 334 REMARK 465 LYS A 335 REMARK 465 TYR A 336 REMARK 465 ASN A 337 REMARK 465 HIS A 338 REMARK 465 LEU A 339 REMARK 465 VAL A 340 REMARK 465 GLY A 341 REMARK 465 LEU A 342 REMARK 465 ASN A 343 REMARK 465 CYS A 344 REMARK 465 PRO A 345 REMARK 465 GLY A 346 REMARK 465 ASP A 347 REMARK 465 ILE A 348 REMARK 465 ILE A 349 REMARK 465 PRO A 350 REMARK 465 ASP A 351 REMARK 465 CYS A 352 REMARK 465 PHE A 353 REMARK 465 PHE A 354 REMARK 465 GLN A 355 REMARK 465 VAL A 356 REMARK 465 TYR A 357 REMARK 465 GLN A 358 REMARK 465 PRO A 359 REMARK 465 GLU A 360 REMARK 465 ARG A 361 REMARK 465 GLU A 362 REMARK 465 GLU A 363 REMARK 465 LEU A 364 REMARK 465 GLU A 365 REMARK 465 PRO A 366 REMARK 465 SER A 367 REMARK 465 ASN A 368 REMARK 465 ILE A 369 REMARK 465 VAL A 370 REMARK 465 TYR A 371 REMARK 465 LEU A 372 REMARK 465 SER A 373 REMARK 465 SER A 374 REMARK 465 GLN A 375 REMARK 465 ILE A 376 REMARK 465 ASN A 377 REMARK 465 ILE A 378 REMARK 465 GLY A 379 REMARK 465 ASP A 380 REMARK 465 ILE A 381 REMARK 465 GLU A 382 REMARK 465 TYR A 383 REMARK 465 TYR A 384 REMARK 465 GLU A 385 REMARK 465 ASP A 386 REMARK 465 ALA A 387 REMARK 465 GLU A 388 REMARK 465 GLY A 389 REMARK 465 ASP A 390 REMARK 465 ASP A 391 REMARK 465 LYS A 392 REMARK 465 ILE A 393 REMARK 465 LYS A 394 REMARK 465 LEU A 395 REMARK 465 PHE A 396 REMARK 465 LEU A 397 REMARK 465 ILE A 398 REMARK 465 VAL A 399 REMARK 465 GLY A 400 REMARK 465 SER A 401 REMARK 465 VAL A 402 REMARK 465 PRO A 403 REMARK 465 LYS A 404 REMARK 465 THR A 405 REMARK 465 THR A 406 REMARK 465 SER A 407 REMARK 465 PHE A 408 REMARK 465 THR A 409 REMARK 465 CYS A 410 REMARK 465 ILE A 411 REMARK 465 CYS A 412 REMARK 465 LYS A 413 REMARK 465 LYS A 414 REMARK 465 ASP A 415 REMARK 465 LYS A 416 REMARK 465 LYS A 417 REMARK 465 SER A 418 REMARK 465 ALA A 419 REMARK 465 TYR A 420 REMARK 465 MET A 421 REMARK 465 THR A 422 REMARK 465 VAL A 423 REMARK 465 THR A 424 REMARK 465 ILE A 425 REMARK 465 ASP A 426 REMARK 465 SER A 427 REMARK 465 ALA A 428 REMARK 465 SER H 112 REMARK 465 SER H 113 REMARK 465 ALA H 114 REMARK 465 SER H 115 REMARK 465 THR H 116 REMARK 465 LYS H 117 REMARK 465 GLY H 118 REMARK 465 PRO H 119 REMARK 465 SER H 120 REMARK 465 VAL H 121 REMARK 465 PHE H 122 REMARK 465 PRO H 123 REMARK 465 LEU H 124 REMARK 465 ALA H 125 REMARK 465 PRO H 126 REMARK 465 SER H 127 REMARK 465 SER H 128 REMARK 465 LYS H 129 REMARK 465 SER H 130 REMARK 465 THR H 131 REMARK 465 SER H 132 REMARK 465 GLY H 133 REMARK 465 GLY H 134 REMARK 465 THR H 135 REMARK 465 ALA H 136 REMARK 465 ALA H 137 REMARK 465 LEU H 138 REMARK 465 GLY H 139 REMARK 465 CYS H 140 REMARK 465 LEU H 141 REMARK 465 VAL H 142 REMARK 465 LYS H 143 REMARK 465 ASP H 144 REMARK 465 TYR H 145 REMARK 465 PHE H 146 REMARK 465 PRO H 147 REMARK 465 GLU H 148 REMARK 465 PRO H 149 REMARK 465 VAL H 150 REMARK 465 THR H 151 REMARK 465 VAL H 152 REMARK 465 SER H 153 REMARK 465 TRP H 154 REMARK 465 ASN H 155 REMARK 465 SER H 156 REMARK 465 GLY H 157 REMARK 465 ALA H 158 REMARK 465 LEU H 159 REMARK 465 THR H 160 REMARK 465 SER H 161 REMARK 465 GLY H 162 REMARK 465 VAL H 163 REMARK 465 HIS H 164 REMARK 465 THR H 165 REMARK 465 PHE H 166 REMARK 465 PRO H 167 REMARK 465 ALA H 168 REMARK 465 VAL H 169 REMARK 465 LEU H 170 REMARK 465 GLN H 171 REMARK 465 SER H 172 REMARK 465 SER H 173 REMARK 465 GLY H 174 REMARK 465 LEU H 175 REMARK 465 TYR H 176 REMARK 465 SER H 177 REMARK 465 LEU H 178 REMARK 465 SER H 179 REMARK 465 SER H 180 REMARK 465 VAL H 181 REMARK 465 VAL H 182 REMARK 465 THR H 183 REMARK 465 VAL H 184 REMARK 465 PRO H 185 REMARK 465 SER H 186 REMARK 465 SER H 187 REMARK 465 SER H 188 REMARK 465 LEU H 189 REMARK 465 GLY H 190 REMARK 465 THR H 191 REMARK 465 GLN H 192 REMARK 465 THR H 193 REMARK 465 TYR H 194 REMARK 465 ILE H 195 REMARK 465 CYS H 196 REMARK 465 ASN H 197 REMARK 465 VAL H 198 REMARK 465 ASN H 199 REMARK 465 HIS H 200 REMARK 465 LYS H 201 REMARK 465 PRO H 202 REMARK 465 SER H 203 REMARK 465 ASN H 204 REMARK 465 THR H 205 REMARK 465 LYS H 206 REMARK 465 VAL H 207 REMARK 465 ASP H 208 REMARK 465 LYS H 209 REMARK 465 LYS H 210 REMARK 465 VAL H 211 REMARK 465 GLU H 212 REMARK 465 PRO H 213 REMARK 465 LYS H 214 REMARK 465 SER H 215 REMARK 465 CYS H 216 REMARK 465 LEU L 107 REMARK 465 GLY L 108 REMARK 465 GLN L 109 REMARK 465 PRO L 110 REMARK 465 LYS L 111 REMARK 465 ALA L 112 REMARK 465 ALA L 113 REMARK 465 PRO L 114 REMARK 465 SER L 115 REMARK 465 VAL L 116 REMARK 465 THR L 117 REMARK 465 LEU L 118 REMARK 465 PHE L 119 REMARK 465 PRO L 120 REMARK 465 PRO L 121 REMARK 465 SER L 122 REMARK 465 SER L 123 REMARK 465 GLU L 124 REMARK 465 GLU L 125 REMARK 465 LEU L 126 REMARK 465 GLN L 127 REMARK 465 ALA L 128 REMARK 465 ASN L 129 REMARK 465 LYS L 130 REMARK 465 ALA L 131 REMARK 465 THR L 132 REMARK 465 LEU L 133 REMARK 465 VAL L 134 REMARK 465 CYS L 135 REMARK 465 LEU L 136 REMARK 465 ILE L 137 REMARK 465 SER L 138 REMARK 465 ASP L 139 REMARK 465 PHE L 140 REMARK 465 TYR L 141 REMARK 465 PRO L 142 REMARK 465 GLY L 143 REMARK 465 ALA L 144 REMARK 465 VAL L 145 REMARK 465 THR L 146 REMARK 465 VAL L 147 REMARK 465 ALA L 148 REMARK 465 TRP L 149 REMARK 465 LYS L 150 REMARK 465 ALA L 151 REMARK 465 ASP L 152 REMARK 465 SER L 153 REMARK 465 SER L 154 REMARK 465 PRO L 155 REMARK 465 VAL L 156 REMARK 465 LYS L 157 REMARK 465 ALA L 158 REMARK 465 GLY L 159 REMARK 465 VAL L 160 REMARK 465 GLU L 161 REMARK 465 THR L 162 REMARK 465 THR L 163 REMARK 465 THR L 164 REMARK 465 PRO L 165 REMARK 465 SER L 166 REMARK 465 LYS L 167 REMARK 465 GLN L 168 REMARK 465 SER L 169 REMARK 465 ASN L 170 REMARK 465 ASN L 171 REMARK 465 LYS L 172 REMARK 465 TYR L 173 REMARK 465 ALA L 174 REMARK 465 ALA L 175 REMARK 465 SER L 176 REMARK 465 SER L 177 REMARK 465 TYR L 178 REMARK 465 LEU L 179 REMARK 465 SER L 180 REMARK 465 LEU L 181 REMARK 465 THR L 182 REMARK 465 PRO L 183 REMARK 465 GLU L 184 REMARK 465 GLN L 185 REMARK 465 TRP L 186 REMARK 465 LYS L 187 REMARK 465 SER L 188 REMARK 465 HIS L 189 REMARK 465 ARG L 190 REMARK 465 SER L 191 REMARK 465 TYR L 192 REMARK 465 SER L 193 REMARK 465 CYS L 194 REMARK 465 GLN L 195 REMARK 465 VAL L 196 REMARK 465 THR L 197 REMARK 465 HIS L 198 REMARK 465 GLU L 199 REMARK 465 GLY L 200 REMARK 465 SER L 201 REMARK 465 THR L 202 REMARK 465 VAL L 203 REMARK 465 GLU L 204 REMARK 465 LYS L 205 REMARK 465 THR L 206 REMARK 465 VAL L 207 REMARK 465 ALA L 208 REMARK 465 PRO L 209 REMARK 465 THR L 210 REMARK 465 GLU L 211 REMARK 465 CYS L 212 REMARK 465 SER L 213 REMARK 465 LYS C 107 REMARK 465 ARG C 108 REMARK 465 THR C 109 REMARK 465 VAL C 110 REMARK 465 ALA C 111 REMARK 465 ALA C 112 REMARK 465 PRO C 113 REMARK 465 SER C 114 REMARK 465 VAL C 115 REMARK 465 PHE C 116 REMARK 465 ILE C 117 REMARK 465 PHE C 118 REMARK 465 PRO C 119 REMARK 465 PRO C 120 REMARK 465 SER C 121 REMARK 465 ASP C 122 REMARK 465 GLU C 123 REMARK 465 GLN C 124 REMARK 465 LEU C 125 REMARK 465 LYS C 126 REMARK 465 SER C 127 REMARK 465 GLY C 128 REMARK 465 THR C 129 REMARK 465 ALA C 130 REMARK 465 SER C 131 REMARK 465 VAL C 132 REMARK 465 VAL C 133 REMARK 465 CYS C 134 REMARK 465 LEU C 135 REMARK 465 LEU C 136 REMARK 465 ASN C 137 REMARK 465 ASN C 138 REMARK 465 PHE C 139 REMARK 465 TYR C 140 REMARK 465 PRO C 141 REMARK 465 ARG C 142 REMARK 465 GLU C 143 REMARK 465 ALA C 144 REMARK 465 LYS C 145 REMARK 465 VAL C 146 REMARK 465 GLN C 147 REMARK 465 TRP C 148 REMARK 465 LYS C 149 REMARK 465 VAL C 150 REMARK 465 ASP C 151 REMARK 465 ASN C 152 REMARK 465 ALA C 153 REMARK 465 LEU C 154 REMARK 465 GLN C 155 REMARK 465 SER C 156 REMARK 465 GLY C 157 REMARK 465 ASN C 158 REMARK 465 SER C 159 REMARK 465 GLN C 160 REMARK 465 GLU C 161 REMARK 465 SER C 162 REMARK 465 VAL C 163 REMARK 465 THR C 164 REMARK 465 GLU C 165 REMARK 465 GLN C 166 REMARK 465 ASP C 167 REMARK 465 SER C 168 REMARK 465 LYS C 169 REMARK 465 ASP C 170 REMARK 465 SER C 171 REMARK 465 THR C 172 REMARK 465 TYR C 173 REMARK 465 SER C 174 REMARK 465 LEU C 175 REMARK 465 SER C 176 REMARK 465 SER C 177 REMARK 465 THR C 178 REMARK 465 LEU C 179 REMARK 465 THR C 180 REMARK 465 LEU C 181 REMARK 465 SER C 182 REMARK 465 LYS C 183 REMARK 465 ALA C 184 REMARK 465 ASP C 185 REMARK 465 TYR C 186 REMARK 465 GLU C 187 REMARK 465 LYS C 188 REMARK 465 HIS C 189 REMARK 465 LYS C 190 REMARK 465 VAL C 191 REMARK 465 TYR C 192 REMARK 465 ALA C 193 REMARK 465 CYS C 194 REMARK 465 GLU C 195 REMARK 465 VAL C 196 REMARK 465 THR C 197 REMARK 465 HIS C 198 REMARK 465 GLN C 199 REMARK 465 GLY C 200 REMARK 465 LEU C 201 REMARK 465 SER C 202 REMARK 465 SER C 203 REMARK 465 PRO C 204 REMARK 465 VAL C 205 REMARK 465 THR C 206 REMARK 465 LYS C 207 REMARK 465 SER C 208 REMARK 465 PHE C 209 REMARK 465 ASN C 210 REMARK 465 ARG C 211 REMARK 465 GLY C 212 REMARK 465 GLU C 213 REMARK 465 CYS C 214 REMARK 465 GLN B 1 REMARK 465 SER B 112 REMARK 465 SER B 113 REMARK 465 ALA B 114 REMARK 465 SER B 115 REMARK 465 THR B 116 REMARK 465 LYS B 117 REMARK 465 GLY B 118 REMARK 465 PRO B 119 REMARK 465 SER B 120 REMARK 465 VAL B 121 REMARK 465 PHE B 122 REMARK 465 PRO B 123 REMARK 465 LEU B 124 REMARK 465 ALA B 125 REMARK 465 PRO B 126 REMARK 465 SER B 127 REMARK 465 SER B 128 REMARK 465 LYS B 129 REMARK 465 SER B 130 REMARK 465 THR B 131 REMARK 465 SER B 132 REMARK 465 GLY B 133 REMARK 465 GLY B 134 REMARK 465 THR B 135 REMARK 465 ALA B 136 REMARK 465 ALA B 137 REMARK 465 LEU B 138 REMARK 465 GLY B 139 REMARK 465 CYS B 140 REMARK 465 LEU B 141 REMARK 465 VAL B 142 REMARK 465 LYS B 143 REMARK 465 ASP B 144 REMARK 465 TYR B 145 REMARK 465 PHE B 146 REMARK 465 PRO B 147 REMARK 465 GLU B 148 REMARK 465 PRO B 149 REMARK 465 VAL B 150 REMARK 465 THR B 151 REMARK 465 VAL B 152 REMARK 465 SER B 153 REMARK 465 TRP B 154 REMARK 465 ASN B 155 REMARK 465 SER B 156 REMARK 465 GLY B 157 REMARK 465 ALA B 158 REMARK 465 LEU B 159 REMARK 465 THR B 160 REMARK 465 SER B 161 REMARK 465 GLY B 162 REMARK 465 VAL B 163 REMARK 465 HIS B 164 REMARK 465 THR B 165 REMARK 465 PHE B 166 REMARK 465 PRO B 167 REMARK 465 ALA B 168 REMARK 465 VAL B 169 REMARK 465 LEU B 170 REMARK 465 GLN B 171 REMARK 465 SER B 172 REMARK 465 SER B 173 REMARK 465 GLY B 174 REMARK 465 LEU B 175 REMARK 465 TYR B 176 REMARK 465 SER B 177 REMARK 465 LEU B 178 REMARK 465 SER B 179 REMARK 465 SER B 180 REMARK 465 VAL B 181 REMARK 465 VAL B 182 REMARK 465 THR B 183 REMARK 465 VAL B 184 REMARK 465 PRO B 185 REMARK 465 SER B 186 REMARK 465 SER B 187 REMARK 465 SER B 188 REMARK 465 LEU B 189 REMARK 465 GLY B 190 REMARK 465 THR B 191 REMARK 465 GLN B 192 REMARK 465 THR B 193 REMARK 465 TYR B 194 REMARK 465 ILE B 195 REMARK 465 CYS B 196 REMARK 465 ASN B 197 REMARK 465 VAL B 198 REMARK 465 ASN B 199 REMARK 465 HIS B 200 REMARK 465 LYS B 201 REMARK 465 PRO B 202 REMARK 465 SER B 203 REMARK 465 ASN B 204 REMARK 465 THR B 205 REMARK 465 LYS B 206 REMARK 465 VAL B 207 REMARK 465 ASP B 208 REMARK 465 LYS B 209 REMARK 465 LYS B 210 REMARK 465 VAL B 211 REMARK 465 GLU B 212 REMARK 465 PRO B 213 REMARK 465 LYS B 214 REMARK 465 SER B 215 REMARK 465 CYS B 216 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 SER A 42 OG REMARK 470 PHE A 44 CG CD1 CD2 CE1 CE2 CZ REMARK 470 CYS A 49 SG REMARK 470 ASN A 50 CG OD1 ND2 REMARK 470 PHE A 70 CG CD1 CD2 CE1 CE2 CZ REMARK 470 CYS A 71 SG REMARK 470 ASP A 109 CG OD1 OD2 REMARK 470 GLU A 125 CG CD OE1 OE2 REMARK 470 GLU A 127 CG CD OE1 OE2 REMARK 470 GLU A 139 CG CD OE1 OE2 REMARK 470 SER A 148 OG REMARK 470 LYS A 150 CG CD CE NZ REMARK 470 ASP A 151 CG OD1 OD2 REMARK 470 LYS A 181 CG CD CE NZ REMARK 470 ASN A 185 CG OD1 ND2 REMARK 470 ASP A 194 CG OD1 OD2 REMARK 470 LYS A 201 CG CD CE NZ REMARK 470 SER A 206 OG REMARK 470 ASN A 207 CG OD1 ND2 REMARK 470 ASP A 219 CG OD1 OD2 REMARK 470 GLU A 221 CG CD OE1 OE2 REMARK 470 CYS A 227 SG REMARK 470 LEU A 229 CG CD1 CD2 REMARK 470 ASN A 231 CG OD1 ND2 REMARK 470 LYS A 232 CG CD CE NZ REMARK 470 LYS A 241 CG CD CE NZ REMARK 470 LEU A 243 CG CD1 CD2 REMARK 470 LYS A 245 CG CD CE NZ REMARK 470 LYS A 248 CG CD CE NZ REMARK 470 HIS A 252 CG ND1 CD2 CE1 NE2 REMARK 470 LYS A 253 CG CD CE NZ REMARK 470 PHE A 262 CG CD1 CD2 CE1 CE2 CZ REMARK 470 TYR A 263 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LYS A 267 CG CD CE NZ REMARK 470 CYS A 275 SG REMARK 470 LYS A 278 CG CD CE NZ REMARK 470 GLN H 1 CG CD OE1 NE2 REMARK 470 VAL H 2 CG1 CG2 REMARK 470 GLN H 3 CG CD OE1 NE2 REMARK 470 LEU H 4 CG CD1 CD2 REMARK 470 GLU H 10 CG CD OE1 OE2 REMARK 470 VAL H 11 CG1 CG2 REMARK 470 ARG H 12 CG CD NE CZ NH1 NH2 REMARK 470 LYS H 13 CG CD CE NZ REMARK 470 PRO H 14 CG CD REMARK 470 SER H 17 OG REMARK 470 VAL H 18 CG1 CG2 REMARK 470 LYS H 19 CG CD CE NZ REMARK 470 SER H 21 OG REMARK 470 ARG H 23 CG CD NE CZ NH1 NH2 REMARK 470 SER H 25 OG REMARK 470 TYR H 27 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 THR H 28 OG1 CG2 REMARK 470 THR H 30 OG1 CG2 REMARK 470 ASP H 31 CG OD1 OD2 REMARK 470 VAL H 37 CG1 CG2 REMARK 470 ARG H 38 CG CD NE CZ NH1 NH2 REMARK 470 GLU H 43 CG CD OE1 OE2 REMARK 470 GLU H 46 CG CD OE1 OE2 REMARK 470 SER H 50 OG REMARK 470 LYS H 53 CG CD CE NZ REMARK 470 SER H 54 OG REMARK 470 THR H 57 OG1 CG2 REMARK 470 SER H 58 OG REMARK 470 VAL H 67 CG1 CG2 REMARK 470 THR H 68 OG1 CG2 REMARK 470 GLU H 72 CG CD OE1 OE2 REMARK 470 THR H 73 OG1 CG2 REMARK 470 SER H 74 OG REMARK 470 VAL H 75 CG1 CG2 REMARK 470 THR H 77 OG1 CG2 REMARK 470 ASP H 81 CG OD1 OD2 REMARK 470 SER H 82A OG REMARK 470 LEU H 82C CG CD1 CD2 REMARK 470 ARG H 83 CG CD NE CZ NH1 NH2 REMARK 470 SER H 84 OG REMARK 470 ASP H 85 CG OD1 OD2 REMARK 470 ARG H 94 CG CD NE CZ NH1 NH2 REMARK 470 ASP H 101 CG OD1 OD2 REMARK 470 GLN H 105 CG CD OE1 NE2 REMARK 470 THR H 107 OG1 CG2 REMARK 470 THR H 108 OG1 CG2 REMARK 470 GLU L 3 CG CD OE1 OE2 REMARK 470 GLN L 6 CG CD OE1 NE2 REMARK 470 PRO L 8 CG CD REMARK 470 SER L 9 OG REMARK 470 SER L 11 OG REMARK 470 LYS L 16 CG CD CE NZ REMARK 470 ARG L 19 CG CD NE CZ NH1 NH2 REMARK 470 THR L 69 OG1 CG2 REMARK 470 ARG L 76 CG CD NE CZ NH1 NH2 REMARK 470 GLU L 78 CG CD OE1 OE2 REMARK 470 GLU L 82 CG CD OE1 OE2 REMARK 470 ASP L 91 CG OD1 OD2 REMARK 470 SER L 93 OG REMARK 470 SER L 94 OG REMARK 470 HIS L 95A CG ND1 CD2 CE1 NE2 REMARK 470 TYR L 96 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ARG L 100 CG CD NE CZ NH1 NH2 REMARK 470 ILE C 2 CG1 CG2 CD1 REMARK 470 GLN C 3 CG CD OE1 NE2 REMARK 470 THR C 5 OG1 CG2 REMARK 470 SER C 7 OG REMARK 470 PRO C 8 CG CD REMARK 470 SER C 9 OG REMARK 470 SER C 10 OG REMARK 470 LEU C 11 CG CD1 CD2 REMARK 470 SER C 12 OG REMARK 470 SER C 14 OG REMARK 470 VAL C 15 CG1 CG2 REMARK 470 ASP C 17 CG OD1 OD2 REMARK 470 SER C 60 OG REMARK 470 ARG C 61 CG CD NE CZ NH1 NH2 REMARK 470 SER C 63 OG REMARK 470 SER C 65 OG REMARK 470 THR C 72 OG1 CG2 REMARK 470 THR C 74 OG1 CG2 REMARK 470 THR C 76 OG1 CG2 REMARK 470 SER C 77 OG REMARK 470 GLN C 79 CG CD OE1 NE2 REMARK 470 GLU C 81 CG CD OE1 OE2 REMARK 470 ASP C 82 CG OD1 OD2 REMARK 470 GLN C 89 CG CD OE1 NE2 REMARK 470 GLN C 90 CG CD OE1 NE2 REMARK 470 ARG C 103 CG CD NE CZ NH1 NH2 REMARK 470 GLU C 105 CG CD OE1 OE2 REMARK 470 ILE C 106 CG1 CG2 CD1 REMARK 470 GLN B 6 CG CD OE1 NE2 REMARK 470 SER B 7 OG REMARK 470 PRO B 9 CG CD REMARK 470 GLU B 10 CG CD OE1 OE2 REMARK 470 LYS B 12 CG CD CE NZ REMARK 470 LYS B 13 CG CD CE NZ REMARK 470 PRO B 14 CG CD REMARK 470 SER B 17 OG REMARK 470 LYS B 19 CG CD CE NZ REMARK 470 SER B 21 OG REMARK 470 LEU B 37 CG CD1 CD2 REMARK 470 PRO B 41 CG CD REMARK 470 GLN B 43 CG CD OE1 NE2 REMARK 470 ASN B 53 CG OD1 ND2 REMARK 470 SER B 54 OG REMARK 470 GLN B 61 CG CD OE1 NE2 REMARK 470 THR B 68 OG1 CG2 REMARK 470 THR B 70 OG1 CG2 REMARK 470 ARG B 71 CG CD NE CZ NH1 NH2 REMARK 470 ASP B 72 CG OD1 OD2 REMARK 470 THR B 73 OG1 CG2 REMARK 470 SER B 74 OG REMARK 470 ILE B 75 CG1 CG2 CD1 REMARK 470 SER B 76 OG REMARK 470 THR B 77 OG1 CG2 REMARK 470 GLU B 81 CG CD OE1 OE2 REMARK 470 ARG B 82A CG CD NE CZ NH1 NH2 REMARK 470 ARG B 83 CG CD NE CZ NH1 NH2 REMARK 470 SER B 84 OG REMARK 470 ARG B 94 CG CD NE CZ NH1 NH2 REMARK 470 ASP B 101 CG OD1 OD2 REMARK 470 LEU B 108 CG CD1 CD2 REMARK 470 THR B 110 OG1 CG2 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 ND2 ASN A 190 O5 NAG D 1 2.18 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 LYS A 89 -10.76 75.29 REMARK 500 ASN A 204 -150.96 46.82 REMARK 500 ASN A 231 -132.05 56.06 REMARK 500 PHE A 235 -2.22 65.13 REMARK 500 GLU A 240 71.46 61.10 REMARK 500 LYS A 241 -110.12 56.33 REMARK 500 PHE A 262 -2.41 70.44 REMARK 500 ASN A 279 -7.28 71.03 REMARK 500 THR H 30 -2.33 70.59 REMARK 500 THR H 73 -3.11 66.52 REMARK 500 TYR H 100D 147.66 80.31 REMARK 500 ASP L 50 -4.00 63.88 REMARK 500 ILE L 57 146.68 -174.40 REMARK 500 SER C 30 -129.53 59.71 REMARK 500 LYS C 42 -128.61 50.81 REMARK 500 PHE C 83 108.31 -58.04 REMARK 500 ALA C 84 -179.83 -173.88 REMARK 500 ARG C 93 148.50 70.38 REMARK 500 SER B 100A -111.14 64.07 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-41821 RELATED DB: EMDB REMARK 900 RELATED ID: EMD-41822 RELATED DB: EMDB REMARK 900 LOCAL REFINEMENT OF PLASMODIUM FALCIPARUM GAMETOCYTE SURFACE REMARK 900 PROTEIN PFS48/45 DOMAINS 1 AND 2 IN COMPLEX WITH NEUTRALIZING REMARK 900 ANTIBODIES REMARK 900 RELATED ID: 8U70 RELATED DB: PDB DBREF 8U1P A 28 428 UNP Q8I6T1 P4548_PLAF7 28 428 DBREF 8U1P H 1 216 PDB 8U1P 8U1P 1 216 DBREF 8U1P L 2 213 PDB 8U1P 8U1P 2 213 DBREF 8U1P C 2 214 PDB 8U1P 8U1P 2 214 DBREF 8U1P B 1 216 PDB 8U1P 8U1P 1 216 SEQADV 8U1P TYR A 308 UNP Q8I6T1 HIS 308 CONFLICT SEQADV 8U1P ARG A 361 UNP Q8I6T1 SER 361 CONFLICT SEQADV 8U1P SER A 373 UNP Q8I6T1 ASP 373 CONFLICT SEQADV 8U1P LEU A 397 UNP Q8I6T1 GLY 397 CONFLICT SEQADV 8U1P VAL A 402 UNP Q8I6T1 ILE 402 CONFLICT SEQRES 1 A 401 ASN ASN ASP PHE CYS LYS PRO SER SER LEU ASN SER GLU SEQRES 2 A 401 ILE SER GLY PHE ILE GLY TYR LYS CYS ASN PHE SER ASN SEQRES 3 A 401 GLU GLY VAL HIS ASN LEU LYS PRO ASP MET ARG GLU ARG SEQRES 4 A 401 ARG SER ILE PHE CYS THR ILE HIS SER TYR PHE ILE TYR SEQRES 5 A 401 ASP LYS ILE ARG LEU ILE ILE PRO LYS LYS SER SER SER SEQRES 6 A 401 PRO GLU PHE LYS ILE LEU PRO GLU LYS CYS PHE GLN LYS SEQRES 7 A 401 VAL TYR THR ASP TYR GLU ASN ARG VAL GLU THR ASP ILE SEQRES 8 A 401 SER GLU LEU GLY LEU ILE GLU TYR GLU ILE GLU GLU ASN SEQRES 9 A 401 ASP THR ASN PRO ASN TYR ASN GLU ARG THR ILE THR ILE SEQRES 10 A 401 SER PRO PHE SER PRO LYS ASP ILE GLU PHE PHE CYS PHE SEQRES 11 A 401 CYS ASP ASN THR GLU LYS VAL ILE SER SER ILE GLU GLY SEQRES 12 A 401 ARG SER ALA MET VAL HIS VAL ARG VAL LEU LYS TYR PRO SEQRES 13 A 401 HIS ASN ILE LEU PHE THR ASN LEU THR ASN ASP LEU PHE SEQRES 14 A 401 THR TYR LEU PRO LYS THR TYR ASN GLU SER ASN PHE VAL SEQRES 15 A 401 SER ASN VAL LEU GLU VAL GLU LEU ASN ASP GLY GLU LEU SEQRES 16 A 401 PHE VAL LEU ALA CYS GLU LEU ILE ASN LYS LYS CYS PHE SEQRES 17 A 401 GLN GLU GLY LYS GLU LYS ALA LEU TYR LYS SER ASN LYS SEQRES 18 A 401 ILE ILE TYR HIS LYS ASN LEU THR ILE PHE LYS ALA PRO SEQRES 19 A 401 PHE TYR VAL THR SER LYS ASP VAL ASN THR GLU CYS THR SEQRES 20 A 401 CYS LYS PHE LYS ASN ASN ASN TYR LYS ILE VAL LEU LYS SEQRES 21 A 401 PRO LYS TYR GLU LYS LYS VAL ILE HIS GLY CYS ASN PHE SEQRES 22 A 401 SER SER ASN VAL SER SER LYS TYR THR PHE THR ASP SER SEQRES 23 A 401 LEU ASP ILE SER LEU VAL ASP ASP SER ALA HIS ILE SER SEQRES 24 A 401 CYS ASN VAL HIS LEU SER GLU PRO LYS TYR ASN HIS LEU SEQRES 25 A 401 VAL GLY LEU ASN CYS PRO GLY ASP ILE ILE PRO ASP CYS SEQRES 26 A 401 PHE PHE GLN VAL TYR GLN PRO GLU ARG GLU GLU LEU GLU SEQRES 27 A 401 PRO SER ASN ILE VAL TYR LEU SER SER GLN ILE ASN ILE SEQRES 28 A 401 GLY ASP ILE GLU TYR TYR GLU ASP ALA GLU GLY ASP ASP SEQRES 29 A 401 LYS ILE LYS LEU PHE LEU ILE VAL GLY SER VAL PRO LYS SEQRES 30 A 401 THR THR SER PHE THR CYS ILE CYS LYS LYS ASP LYS LYS SEQRES 31 A 401 SER ALA TYR MET THR VAL THR ILE ASP SER ALA SEQRES 1 H 226 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL ARG LYS SEQRES 2 H 226 PRO GLY ALA SER VAL LYS VAL SER CYS ARG THR SER GLY SEQRES 3 H 226 TYR THR PHE THR ASP TYR TYR MET HIS TRP VAL ARG GLN SEQRES 4 H 226 ALA PRO GLY GLU GLY LEU GLU TRP MET GLY SER ILE ASN SEQRES 5 H 226 PRO LYS SER GLY GLY THR SER TYR ALA GLU ARG PHE GLN SEQRES 6 H 226 GLY ARG VAL THR MET THR MET GLU THR SER VAL SER THR SEQRES 7 H 226 ALA TYR LEU ASP LEU SER SER LEU ARG SER ASP ASP THR SEQRES 8 H 226 ALA VAL TYR TYR CYS ALA ARG LEU LEU TYR SER ARG ALA SEQRES 9 H 226 VAL TYR TYR TYR GLY MET ASP VAL TRP GLY GLN GLY THR SEQRES 10 H 226 THR VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER SEQRES 11 H 226 VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY SEQRES 12 H 226 GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE SEQRES 13 H 226 PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU SEQRES 14 H 226 THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SEQRES 15 H 226 SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SEQRES 16 H 226 SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL SEQRES 17 H 226 ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL SEQRES 18 H 226 GLU PRO LYS SER CYS SEQRES 1 L 213 TYR GLU LEU THR GLN PRO PRO SER VAL SER VAL ALA PRO SEQRES 2 L 213 GLY LYS THR ALA ARG ILE THR CYS GLY GLY LYS ASP LEU SEQRES 3 L 213 GLY SER LYS SER VAL HIS TRP TYR GLN GLN LYS PRO GLY SEQRES 4 L 213 GLN ALA PRO VAL LEU VAL ILE TYR TYR ASP ASN ILE ARG SEQRES 5 L 213 PRO SER GLY ILE PRO GLU ARG PHE SER GLY SER ASN SER SEQRES 6 L 213 GLY ASN THR ALA THR LEU THR ILE SER ARG VAL GLU ALA SEQRES 7 L 213 GLY ASP GLU ALA ASP TYR TYR CYS GLN VAL TRP ASP SER SEQRES 8 L 213 SER SER ASP HIS TYR VAL PHE GLY ARG GLY ALA LYS VAL SEQRES 9 L 213 THR VAL LEU GLY GLN PRO LYS ALA ALA PRO SER VAL THR SEQRES 10 L 213 LEU PHE PRO PRO SER SER GLU GLU LEU GLN ALA ASN LYS SEQRES 11 L 213 ALA THR LEU VAL CYS LEU ILE SER ASP PHE TYR PRO GLY SEQRES 12 L 213 ALA VAL THR VAL ALA TRP LYS ALA ASP SER SER PRO VAL SEQRES 13 L 213 LYS ALA GLY VAL GLU THR THR THR PRO SER LYS GLN SER SEQRES 14 L 213 ASN ASN LYS TYR ALA ALA SER SER TYR LEU SER LEU THR SEQRES 15 L 213 PRO GLU GLN TRP LYS SER HIS ARG SER TYR SER CYS GLN SEQRES 16 L 213 VAL THR HIS GLU GLY SER THR VAL GLU LYS THR VAL ALA SEQRES 17 L 213 PRO THR GLU CYS SER SEQRES 1 C 213 ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SER SEQRES 2 C 213 VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER GLN SEQRES 3 C 213 ILE ILE SER THR TYR LEU ASN TRP TYR GLN HIS LYS PRO SEQRES 4 C 213 GLY LYS ALA PRO LYS LEU LEU ILE LYS SER ALA SER THR SEQRES 5 C 213 LEU GLN SER GLY VAL PRO SER ARG PHE SER GLY SER GLY SEQRES 6 C 213 SER GLY THR ASP PHE THR LEU THR ILE THR SER LEU GLN SEQRES 7 C 213 PRO GLU ASP PHE ALA THR PHE TYR CYS GLN GLN SER TYR SEQRES 8 C 213 ARG ASP PRO ILE THR PHE GLY GLN GLY THR ARG LEU GLU SEQRES 9 C 213 ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE PHE SEQRES 10 C 213 PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SER SEQRES 11 C 213 VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU ALA SEQRES 12 C 213 LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER GLY SEQRES 13 C 213 ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS ASP SEQRES 14 C 213 SER THR TYR SER LEU SER SER THR LEU THR LEU SER LYS SEQRES 15 C 213 ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU VAL SEQRES 16 C 213 THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER PHE SEQRES 17 C 213 ASN ARG GLY GLU CYS SEQRES 1 B 227 GLN VAL GLN LEU VAL GLN SER GLY PRO GLU ALA LYS LYS SEQRES 2 B 227 PRO GLY ALA SER VAL LYS VAL SER CYS GLN ALA SER GLY SEQRES 3 B 227 TYR PRO PHE SER GLY TYR TYR MET HIS TRP LEU ARG GLN SEQRES 4 B 227 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY TRP MET ASN SEQRES 5 B 227 PRO ASN SER GLY GLY THR LYS TYR ALA GLN ARG PHE GLN SEQRES 6 B 227 GLY ARG VAL THR MET THR ARG ASP THR SER ILE SER THR SEQRES 7 B 227 ALA HIS MET GLU LEU ARG GLY LEU ARG SER ASP ASP THR SEQRES 8 B 227 ALA VAL TYR TYR CYS ALA ARG ASP TYR CYS THR GLY SER SEQRES 9 B 227 SER CYS TYR ARG THR ASP TYR ASP TYR TRP GLY GLN GLY SEQRES 10 B 227 THR LEU VAL THR VAL SER SER ALA SER THR LYS GLY PRO SEQRES 11 B 227 SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER SEQRES 12 B 227 GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR SEQRES 13 B 227 PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA SEQRES 14 B 227 LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SEQRES 15 B 227 SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL SEQRES 16 B 227 PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN SEQRES 17 B 227 VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS SEQRES 18 B 227 VAL GLU PRO LYS SER CYS HET NAG D 1 14 HET NAG D 2 14 HET NAG E 1 14 HET NAG E 2 14 HET NAG A 501 14 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA- HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO- HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE FORMUL 6 NAG 5(C8 H15 N O6) HELIX 1 AA1 SER A 119 LEU A 121 5 3 HELIX 2 AA2 ARG H 83 THR H 87 5 5 SHEET 1 AA1 4 LYS A 48 CYS A 49 0 SHEET 2 AA1 4 LYS A 81 PRO A 87 1 O ILE A 85 N CYS A 49 SHEET 3 AA1 4 TYR A 137 THR A 143 -1 O ASN A 138 N ILE A 86 SHEET 4 AA1 4 GLU A 127 ASN A 131 -1 N GLU A 129 O THR A 141 SHEET 1 AA2 3 CYS A 71 SER A 75 0 SHEET 2 AA2 3 VAL A 175 VAL A 179 1 O HIS A 176 N ILE A 73 SHEET 3 AA2 3 ILE A 152 CYS A 156 -1 N ILE A 152 O VAL A 179 SHEET 1 AA3 2 LYS A 105 TYR A 107 0 SHEET 2 AA3 2 GLU A 115 ASP A 117 -1 O THR A 116 N VAL A 106 SHEET 1 AA4 4 ILE A 186 THR A 189 0 SHEET 2 AA4 4 LEU A 222 LEU A 225 1 O LEU A 222 N LEU A 187 SHEET 3 AA4 4 LEU A 255 LYS A 259 -1 O PHE A 258 N PHE A 223 SHEET 4 AA4 4 ILE A 249 HIS A 252 -1 N ILE A 250 O ILE A 257 SHEET 1 AA5 3 VAL A 212 GLU A 216 0 SHEET 2 AA5 3 LYS A 283 LYS A 287 1 O VAL A 285 N LEU A 213 SHEET 3 AA5 3 THR A 271 CYS A 273 -1 N THR A 271 O LEU A 286 SHEET 1 AA6 2 LYS A 276 PHE A 277 0 SHEET 2 AA6 2 ASN A 280 ASN A 281 -1 O ASN A 280 N PHE A 277 SHEET 1 AA7 4 LEU H 4 GLN H 6 0 SHEET 2 AA7 4 SER H 17 THR H 24 -1 O ARG H 23 N VAL H 5 SHEET 3 AA7 4 THR H 77 SER H 82A-1 O ALA H 78 N CYS H 22 SHEET 4 AA7 4 VAL H 67 MET H 71 -1 N THR H 68 O ASP H 81 SHEET 1 AA8 6 GLU H 10 VAL H 11 0 SHEET 2 AA8 6 THR H 107 THR H 110 1 O THR H 108 N GLU H 10 SHEET 3 AA8 6 ALA H 88 LEU H 96 -1 N TYR H 90 O THR H 107 SHEET 4 AA8 6 TYR H 32 GLN H 39 -1 N TYR H 33 O LEU H 95 SHEET 5 AA8 6 LEU H 45 ILE H 51 -1 O MET H 48 N TRP H 36 SHEET 6 AA8 6 SER H 58 TYR H 59 -1 O SER H 58 N SER H 50 SHEET 1 AA9 4 GLU H 10 VAL H 11 0 SHEET 2 AA9 4 THR H 107 THR H 110 1 O THR H 108 N GLU H 10 SHEET 3 AA9 4 ALA H 88 LEU H 96 -1 N TYR H 90 O THR H 107 SHEET 4 AA9 4 VAL H 102 TRP H 103 -1 O VAL H 102 N ARG H 94 SHEET 1 AB1 5 SER L 9 SER L 11 0 SHEET 2 AB1 5 LYS L 103 THR L 105 1 O LYS L 103 N VAL L 10 SHEET 3 AB1 5 ALA L 83 ASP L 91 -1 N ALA L 83 O VAL L 104 SHEET 4 AB1 5 VAL L 32 GLN L 37 -1 N GLN L 37 O ASP L 84 SHEET 5 AB1 5 VAL L 44 ILE L 47 -1 O VAL L 44 N GLN L 36 SHEET 1 AB2 4 SER L 9 SER L 11 0 SHEET 2 AB2 4 LYS L 103 THR L 105 1 O LYS L 103 N VAL L 10 SHEET 3 AB2 4 ALA L 83 ASP L 91 -1 N ALA L 83 O VAL L 104 SHEET 4 AB2 4 HIS L 95A PHE L 98 -1 O VAL L 97 N VAL L 89 SHEET 1 AB3 3 ALA L 18 GLY L 23 0 SHEET 2 AB3 3 THR L 69 ILE L 74 -1 O ALA L 70 N CYS L 22 SHEET 3 AB3 3 SER L 64 SER L 66 -1 N SER L 64 O THR L 71 SHEET 1 AB4 2 SER C 10 SER C 12 0 SHEET 2 AB4 2 ARG C 103 GLU C 105 1 O GLU C 105 N LEU C 11 SHEET 1 AB5 4 THR C 53 LEU C 54 0 SHEET 2 AB5 4 PRO C 44 LYS C 49 -1 N LYS C 49 O THR C 53 SHEET 3 AB5 4 LEU C 33 HIS C 38 -1 N GLN C 37 O LYS C 45 SHEET 4 AB5 4 THR C 85 GLN C 90 -1 O THR C 85 N HIS C 38 SHEET 1 AB6 2 PHE C 62 SER C 67 0 SHEET 2 AB6 2 ASP C 70 ILE C 75 -1 O THR C 72 N SER C 65 SHEET 1 AB7 4 GLN B 3 GLN B 6 0 SHEET 2 AB7 4 VAL B 18 SER B 25 -1 O GLN B 23 N VAL B 5 SHEET 3 AB7 4 THR B 77 LEU B 82 -1 O ALA B 78 N CYS B 22 SHEET 4 AB7 4 VAL B 67 ASP B 72 -1 N THR B 68 O GLU B 81 SHEET 1 AB8 5 THR B 57 TYR B 59 0 SHEET 2 AB8 5 LEU B 45 MET B 51 -1 N TRP B 50 O LYS B 58 SHEET 3 AB8 5 MET B 34 GLN B 39 -1 N TRP B 36 O MET B 48 SHEET 4 AB8 5 ALA B 88 ARG B 94 -1 O VAL B 89 N GLN B 39 SHEET 5 AB8 5 THR B 107 VAL B 109 -1 O VAL B 109 N ALA B 88 SSBOND 1 CYS A 102 CYS A 156 1555 1555 2.03 SSBOND 2 CYS A 234 CYS A 273 1555 1555 2.03 SSBOND 3 CYS H 22 CYS H 92 1555 1555 2.03 SSBOND 4 CYS L 22 CYS L 87 1555 1555 2.03 SSBOND 5 CYS C 23 CYS C 88 1555 1555 2.03 SSBOND 6 CYS B 22 CYS B 92 1555 1555 2.03 SSBOND 7 CYS B 97 CYS B 100B 1555 1555 2.03 LINK ND2 ASN A 131 C1 NAG A 501 1555 1555 1.50 LINK ND2 ASN A 190 C1 NAG D 1 1555 1555 1.46 LINK ND2 ASN A 204 C1 NAG E 1 1555 1555 1.47 LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.46 LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.45 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