HEADER MEMBRANE PROTEIN, SIGNALING PROTEIN 29-APR-21 7MLY TITLE CRYO-EM REVEALS PARTIALLY AND FULLY ASSEMBLED NATIVE GLYCINE TITLE 2 RECEPTORS,HETEROMERIC PENTAMER COMPND MOL_ID: 1; COMPND 2 MOLECULE: 3D1 FAB LIGHT CHAIN; COMPND 3 CHAIN: J, K, M, I; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: 3D1 FAB HEAVY CHAIN; COMPND 7 CHAIN: G, F, L, H; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: GLYCINE RECEPTOR ALPHA 1; COMPND 11 CHAIN: D, A, B, C; COMPND 12 MOL_ID: 4; COMPND 13 MOLECULE: GLYCINE RECEPTOR BETA; COMPND 14 CHAIN: E SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS; SOURCE 3 ORGANISM_TAXID: 10116; SOURCE 4 EXPRESSION_SYSTEM: RATTUS NORVEGICUS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 10116; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS; SOURCE 8 ORGANISM_TAXID: 10116; SOURCE 9 EXPRESSION_SYSTEM: RATTUS NORVEGICUS; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 10116; SOURCE 11 MOL_ID: 3; SOURCE 12 ORGANISM_SCIENTIFIC: SUS SCROFA; SOURCE 13 ORGANISM_COMMON: PIG; SOURCE 14 ORGANISM_TAXID: 9823; SOURCE 15 MOL_ID: 4; SOURCE 16 ORGANISM_SCIENTIFIC: SUS SCROFA; SOURCE 17 ORGANISM_COMMON: PIG; SOURCE 18 ORGANISM_TAXID: 9823 KEYWDS GLYCINE RECEPTOR, ION CHANNEL, HETEROMERIC PENTAMER, MEMBRANE KEYWDS 2 PROTEIN, SIGNALING PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR H.ZHU,E.GOUAUX JRNL AUTH H.ZHU,E.GOUAUX JRNL TITL ARCHITECTURE AND ASSEMBLY MECHANISM OF NATIVE GLYCINE JRNL TITL 2 RECEPTORS JRNL REF NATURE 2021 JRNL REFN ESSN 1476-4687 JRNL DOI 10.1038/S41586-021-04022-Z REMARK 2 REMARK 2 RESOLUTION. 2.70 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : SERIALEM, CRYOSPARC, CRYOSPARC, REMARK 3 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) : 2.700 REMARK 3 NUMBER OF PARTICLES : 527075 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 7MLY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB. REMARK 100 THE DEPOSITION ID IS D_1000256233. 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 : NATIVE HETEROMERIC GLYCINE REMARK 245 RECEPTOR BOUND WITH 3D1 FAB; REMARK 245 NATIVE HETEROMERIC GLYCINE REMARK 245 RECEPTOR; 3D1 FAB REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 0.05 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 : FEI TITAN KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 BIOQUANTUM (6K X REMARK 245 4K) REMARK 245 MINIMUM DEFOCUS (NM) : NULL REMARK 245 MAXIMUM DEFOCUS (NM) : NULL 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) : 28.20 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: TRIDECAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: J, G, K, F, M, L, I, H, D, A, REMARK 350 AND CHAINS: B, C, E, T, Z, f, l, r 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 ASP J 1 REMARK 465 LYS J 103 REMARK 465 LEU J 104 REMARK 465 GLU J 105 REMARK 465 ILE J 106 REMARK 465 LYS J 107 REMARK 465 GLN G 1 REMARK 465 SER G 117 REMARK 465 SER G 118 REMARK 465 ASP K 1 REMARK 465 LEU K 104 REMARK 465 GLU K 105 REMARK 465 ILE K 106 REMARK 465 LYS K 107 REMARK 465 GLN F 1 REMARK 465 SER F 117 REMARK 465 SER F 118 REMARK 465 ASP M 1 REMARK 465 GLU M 105 REMARK 465 ILE M 106 REMARK 465 LYS M 107 REMARK 465 GLN L 1 REMARK 465 SER L 117 REMARK 465 SER L 118 REMARK 465 ASP I 1 REMARK 465 GLU I 105 REMARK 465 ILE I 106 REMARK 465 LYS I 107 REMARK 465 GLN H 1 REMARK 465 SER H 117 REMARK 465 SER H 118 REMARK 465 MET D -27 REMARK 465 TYR D -26 REMARK 465 ARG D -25 REMARK 465 PHE D -24 REMARK 465 ASN D -23 REMARK 465 THR D -22 REMARK 465 LEU D -21 REMARK 465 ARG D -20 REMARK 465 LEU D -19 REMARK 465 TYR D -18 REMARK 465 LEU D -17 REMARK 465 TRP D -16 REMARK 465 GLU D -15 REMARK 465 THR D -14 REMARK 465 ILE D -13 REMARK 465 VAL D -12 REMARK 465 PHE D -11 REMARK 465 PHE D -10 REMARK 465 SER D -9 REMARK 465 LEU D -8 REMARK 465 ALA D -7 REMARK 465 ALA D -6 REMARK 465 SER D -5 REMARK 465 LYS D -4 REMARK 465 GLU D -3 REMARK 465 ALA D -2 REMARK 465 GLU D -1 REMARK 465 ALA D 0 REMARK 465 ALA D 1 REMARK 465 ARG D 2 REMARK 465 SER D 3 REMARK 465 ALA D 4 REMARK 465 SER D 5 REMARK 465 LYS D 6 REMARK 465 PRO D 7 REMARK 465 MET D 8 REMARK 465 GLN D 310 REMARK 465 HIS D 311 REMARK 465 LYS D 312 REMARK 465 GLU D 313 REMARK 465 LEU D 314 REMARK 465 LEU D 315 REMARK 465 ARG D 316 REMARK 465 PHE D 317 REMARK 465 ARG D 318 REMARK 465 ARG D 319 REMARK 465 LYS D 320 REMARK 465 ARG D 321 REMARK 465 ARG D 322 REMARK 465 HIS D 323 REMARK 465 HIS D 324 REMARK 465 LYS D 325 REMARK 465 SER D 326 REMARK 465 PRO D 327 REMARK 465 MET D 328 REMARK 465 LEU D 329 REMARK 465 ASN D 330 REMARK 465 LEU D 331 REMARK 465 PHE D 332 REMARK 465 GLN D 333 REMARK 465 GLU D 334 REMARK 465 ASP D 335 REMARK 465 GLU D 336 REMARK 465 ALA D 337 REMARK 465 GLY D 338 REMARK 465 GLU D 339 REMARK 465 GLY D 340 REMARK 465 ARG D 341 REMARK 465 PHE D 342 REMARK 465 ASN D 343 REMARK 465 PHE D 344 REMARK 465 SER D 345 REMARK 465 ALA D 346 REMARK 465 TYR D 347 REMARK 465 GLY D 348 REMARK 465 MET D 349 REMARK 465 GLY D 350 REMARK 465 PRO D 351 REMARK 465 ALA D 352 REMARK 465 CYS D 353 REMARK 465 LEU D 354 REMARK 465 GLN D 355 REMARK 465 ALA D 356 REMARK 465 LYS D 357 REMARK 465 ASP D 358 REMARK 465 GLY D 359 REMARK 465 ILE D 360 REMARK 465 SER D 361 REMARK 465 VAL D 362 REMARK 465 LYS D 363 REMARK 465 GLY D 364 REMARK 465 ALA D 365 REMARK 465 ASN D 366 REMARK 465 ASN D 367 REMARK 465 THR D 368 REMARK 465 THR D 369 REMARK 465 THR D 370 REMARK 465 ASN D 371 REMARK 465 PRO D 372 REMARK 465 PRO D 373 REMARK 465 PRO D 374 REMARK 465 ALA D 375 REMARK 465 PRO D 376 REMARK 465 SER D 377 REMARK 465 LYS D 378 REMARK 465 SER D 379 REMARK 465 PRO D 380 REMARK 465 GLU D 381 REMARK 465 GLU D 382 REMARK 465 MET D 383 REMARK 465 ARG D 384 REMARK 465 LYS D 385 REMARK 465 MET A -27 REMARK 465 TYR A -26 REMARK 465 ARG A -25 REMARK 465 PHE A -24 REMARK 465 ASN A -23 REMARK 465 THR A -22 REMARK 465 LEU A -21 REMARK 465 ARG A -20 REMARK 465 LEU A -19 REMARK 465 TYR A -18 REMARK 465 LEU A -17 REMARK 465 TRP A -16 REMARK 465 GLU A -15 REMARK 465 THR A -14 REMARK 465 ILE A -13 REMARK 465 VAL A -12 REMARK 465 PHE A -11 REMARK 465 PHE A -10 REMARK 465 SER A -9 REMARK 465 LEU A -8 REMARK 465 ALA A -7 REMARK 465 ALA A -6 REMARK 465 SER A -5 REMARK 465 LYS A -4 REMARK 465 GLU A -3 REMARK 465 ALA A -2 REMARK 465 GLU A -1 REMARK 465 ALA A 0 REMARK 465 ALA A 1 REMARK 465 ARG A 2 REMARK 465 SER A 3 REMARK 465 ALA A 4 REMARK 465 SER A 5 REMARK 465 LYS A 6 REMARK 465 PRO A 7 REMARK 465 LYS A 312 REMARK 465 GLU A 313 REMARK 465 LEU A 314 REMARK 465 LEU A 315 REMARK 465 ARG A 316 REMARK 465 PHE A 317 REMARK 465 ARG A 318 REMARK 465 ARG A 319 REMARK 465 LYS A 320 REMARK 465 ARG A 321 REMARK 465 ARG A 322 REMARK 465 HIS A 323 REMARK 465 HIS A 324 REMARK 465 LYS A 325 REMARK 465 SER A 326 REMARK 465 PRO A 327 REMARK 465 MET A 328 REMARK 465 LEU A 329 REMARK 465 ASN A 330 REMARK 465 LEU A 331 REMARK 465 PHE A 332 REMARK 465 GLN A 333 REMARK 465 GLU A 334 REMARK 465 ASP A 335 REMARK 465 GLU A 336 REMARK 465 ALA A 337 REMARK 465 GLY A 338 REMARK 465 GLU A 339 REMARK 465 GLY A 340 REMARK 465 ARG A 341 REMARK 465 PHE A 342 REMARK 465 ASN A 343 REMARK 465 PHE A 344 REMARK 465 SER A 345 REMARK 465 ALA A 346 REMARK 465 TYR A 347 REMARK 465 GLY A 348 REMARK 465 MET A 349 REMARK 465 GLY A 350 REMARK 465 PRO A 351 REMARK 465 ALA A 352 REMARK 465 CYS A 353 REMARK 465 LEU A 354 REMARK 465 GLN A 355 REMARK 465 ALA A 356 REMARK 465 LYS A 357 REMARK 465 ASP A 358 REMARK 465 GLY A 359 REMARK 465 ILE A 360 REMARK 465 SER A 361 REMARK 465 VAL A 362 REMARK 465 LYS A 363 REMARK 465 GLY A 364 REMARK 465 ALA A 365 REMARK 465 ASN A 366 REMARK 465 ASN A 367 REMARK 465 THR A 368 REMARK 465 THR A 369 REMARK 465 THR A 370 REMARK 465 ASN A 371 REMARK 465 PRO A 372 REMARK 465 PRO A 373 REMARK 465 PRO A 374 REMARK 465 ALA A 375 REMARK 465 PRO A 376 REMARK 465 SER A 377 REMARK 465 LYS A 378 REMARK 465 SER A 379 REMARK 465 PRO A 380 REMARK 465 GLU A 381 REMARK 465 GLU A 382 REMARK 465 MET A 383 REMARK 465 MET B -27 REMARK 465 TYR B -26 REMARK 465 ARG B -25 REMARK 465 PHE B -24 REMARK 465 ASN B -23 REMARK 465 THR B -22 REMARK 465 LEU B -21 REMARK 465 ARG B -20 REMARK 465 LEU B -19 REMARK 465 TYR B -18 REMARK 465 LEU B -17 REMARK 465 TRP B -16 REMARK 465 GLU B -15 REMARK 465 THR B -14 REMARK 465 ILE B -13 REMARK 465 VAL B -12 REMARK 465 PHE B -11 REMARK 465 PHE B -10 REMARK 465 SER B -9 REMARK 465 LEU B -8 REMARK 465 ALA B -7 REMARK 465 ALA B -6 REMARK 465 SER B -5 REMARK 465 LYS B -4 REMARK 465 GLU B -3 REMARK 465 ALA B -2 REMARK 465 GLU B -1 REMARK 465 ALA B 0 REMARK 465 ALA B 1 REMARK 465 ARG B 2 REMARK 465 SER B 3 REMARK 465 ALA B 4 REMARK 465 SER B 5 REMARK 465 LYS B 6 REMARK 465 PRO B 7 REMARK 465 GLN B 310 REMARK 465 HIS B 311 REMARK 465 LYS B 312 REMARK 465 GLU B 313 REMARK 465 LEU B 314 REMARK 465 LEU B 315 REMARK 465 ARG B 316 REMARK 465 PHE B 317 REMARK 465 ARG B 318 REMARK 465 ARG B 319 REMARK 465 LYS B 320 REMARK 465 ARG B 321 REMARK 465 ARG B 322 REMARK 465 HIS B 323 REMARK 465 HIS B 324 REMARK 465 LYS B 325 REMARK 465 SER B 326 REMARK 465 PRO B 327 REMARK 465 MET B 328 REMARK 465 LEU B 329 REMARK 465 ASN B 330 REMARK 465 LEU B 331 REMARK 465 PHE B 332 REMARK 465 GLN B 333 REMARK 465 GLU B 334 REMARK 465 ASP B 335 REMARK 465 GLU B 336 REMARK 465 ALA B 337 REMARK 465 GLY B 338 REMARK 465 GLU B 339 REMARK 465 GLY B 340 REMARK 465 ARG B 341 REMARK 465 PHE B 342 REMARK 465 ASN B 343 REMARK 465 PHE B 344 REMARK 465 SER B 345 REMARK 465 ALA B 346 REMARK 465 TYR B 347 REMARK 465 GLY B 348 REMARK 465 MET B 349 REMARK 465 GLY B 350 REMARK 465 PRO B 351 REMARK 465 ALA B 352 REMARK 465 CYS B 353 REMARK 465 LEU B 354 REMARK 465 GLN B 355 REMARK 465 ALA B 356 REMARK 465 LYS B 357 REMARK 465 ASP B 358 REMARK 465 GLY B 359 REMARK 465 ILE B 360 REMARK 465 SER B 361 REMARK 465 VAL B 362 REMARK 465 LYS B 363 REMARK 465 GLY B 364 REMARK 465 ALA B 365 REMARK 465 ASN B 366 REMARK 465 ASN B 367 REMARK 465 THR B 368 REMARK 465 THR B 369 REMARK 465 THR B 370 REMARK 465 ASN B 371 REMARK 465 PRO B 372 REMARK 465 PRO B 373 REMARK 465 PRO B 374 REMARK 465 ALA B 375 REMARK 465 PRO B 376 REMARK 465 SER B 377 REMARK 465 LYS B 378 REMARK 465 SER B 379 REMARK 465 PRO B 380 REMARK 465 GLU B 381 REMARK 465 GLU B 382 REMARK 465 MET B 383 REMARK 465 ARG B 384 REMARK 465 LYS B 385 REMARK 465 MET C -27 REMARK 465 TYR C -26 REMARK 465 ARG C -25 REMARK 465 PHE C -24 REMARK 465 ASN C -23 REMARK 465 THR C -22 REMARK 465 LEU C -21 REMARK 465 ARG C -20 REMARK 465 LEU C -19 REMARK 465 TYR C -18 REMARK 465 LEU C -17 REMARK 465 TRP C -16 REMARK 465 GLU C -15 REMARK 465 THR C -14 REMARK 465 ILE C -13 REMARK 465 VAL C -12 REMARK 465 PHE C -11 REMARK 465 PHE C -10 REMARK 465 SER C -9 REMARK 465 LEU C -8 REMARK 465 ALA C -7 REMARK 465 ALA C -6 REMARK 465 SER C -5 REMARK 465 LYS C -4 REMARK 465 GLU C -3 REMARK 465 ALA C -2 REMARK 465 GLU C -1 REMARK 465 ALA C 0 REMARK 465 ALA C 1 REMARK 465 ARG C 2 REMARK 465 SER C 3 REMARK 465 ALA C 4 REMARK 465 SER C 5 REMARK 465 LYS C 6 REMARK 465 PRO C 7 REMARK 465 MET C 8 REMARK 465 ARG C 316 REMARK 465 PHE C 317 REMARK 465 ARG C 318 REMARK 465 ARG C 319 REMARK 465 LYS C 320 REMARK 465 ARG C 321 REMARK 465 ARG C 322 REMARK 465 HIS C 323 REMARK 465 HIS C 324 REMARK 465 LYS C 325 REMARK 465 SER C 326 REMARK 465 PRO C 327 REMARK 465 MET C 328 REMARK 465 LEU C 329 REMARK 465 ASN C 330 REMARK 465 LEU C 331 REMARK 465 PHE C 332 REMARK 465 GLN C 333 REMARK 465 GLU C 334 REMARK 465 ASP C 335 REMARK 465 GLU C 336 REMARK 465 ALA C 337 REMARK 465 GLY C 338 REMARK 465 GLU C 339 REMARK 465 GLY C 340 REMARK 465 ARG C 341 REMARK 465 PHE C 342 REMARK 465 ASN C 343 REMARK 465 PHE C 344 REMARK 465 SER C 345 REMARK 465 ALA C 346 REMARK 465 TYR C 347 REMARK 465 GLY C 348 REMARK 465 MET C 349 REMARK 465 GLY C 350 REMARK 465 PRO C 351 REMARK 465 ALA C 352 REMARK 465 CYS C 353 REMARK 465 LEU C 354 REMARK 465 GLN C 355 REMARK 465 ALA C 356 REMARK 465 LYS C 357 REMARK 465 ASP C 358 REMARK 465 GLY C 359 REMARK 465 ILE C 360 REMARK 465 SER C 361 REMARK 465 VAL C 362 REMARK 465 LYS C 363 REMARK 465 GLY C 364 REMARK 465 ALA C 365 REMARK 465 ASN C 366 REMARK 465 ASN C 367 REMARK 465 THR C 368 REMARK 465 THR C 369 REMARK 465 THR C 370 REMARK 465 ASN C 371 REMARK 465 PRO C 372 REMARK 465 PRO C 373 REMARK 465 PRO C 374 REMARK 465 ALA C 375 REMARK 465 PRO C 376 REMARK 465 SER C 377 REMARK 465 LYS C 378 REMARK 465 SER C 379 REMARK 465 MET E -21 REMARK 465 LYS E -20 REMARK 465 PHE E -19 REMARK 465 LEU E -18 REMARK 465 LEU E -17 REMARK 465 ALA E -16 REMARK 465 VAL E -15 REMARK 465 ALA E -14 REMARK 465 PHE E -13 REMARK 465 PHE E -12 REMARK 465 ILE E -11 REMARK 465 LEU E -10 REMARK 465 ILE E -9 REMARK 465 SER E -8 REMARK 465 LEU E -7 REMARK 465 TRP E -6 REMARK 465 VAL E -5 REMARK 465 GLU E -4 REMARK 465 GLU E -3 REMARK 465 ALA E -2 REMARK 465 TYR E -1 REMARK 465 SER E 0 REMARK 465 LYS E 1 REMARK 465 GLU E 2 REMARK 465 LYS E 3 REMARK 465 SER E 4 REMARK 465 SER E 5 REMARK 465 LYS E 6 REMARK 465 LYS E 7 REMARK 465 GLY E 8 REMARK 465 LYS E 9 REMARK 465 GLY E 10 REMARK 465 LYS E 11 REMARK 465 LYS E 12 REMARK 465 LYS E 13 REMARK 465 GLN E 14 REMARK 465 TYR E 15 REMARK 465 LEU E 16 REMARK 465 CYS E 17 REMARK 465 PRO E 18 REMARK 465 SER E 19 REMARK 465 GLN E 20 REMARK 465 GLN E 21 REMARK 465 SER E 22 REMARK 465 ALA E 23 REMARK 465 GLU E 24 REMARK 465 ASP E 25 REMARK 465 LEU E 26 REMARK 465 ALA E 27 REMARK 465 ARG E 28 REMARK 465 VAL E 29 REMARK 465 PRO E 30 REMARK 465 ALA E 31 REMARK 465 ASN E 32 REMARK 465 PRO E 335 REMARK 465 LYS E 336 REMARK 465 ARG E 337 REMARK 465 VAL E 338 REMARK 465 GLU E 339 REMARK 465 ALA E 340 REMARK 465 GLU E 341 REMARK 465 LYS E 342 REMARK 465 ALA E 343 REMARK 465 ARG E 344 REMARK 465 ILE E 345 REMARK 465 ALA E 346 REMARK 465 LYS E 347 REMARK 465 ALA E 348 REMARK 465 GLU E 349 REMARK 465 GLN E 350 REMARK 465 ALA E 351 REMARK 465 ASP E 352 REMARK 465 GLY E 353 REMARK 465 LYS E 354 REMARK 465 GLY E 355 REMARK 465 ALA E 356 REMARK 465 ASN E 357 REMARK 465 ALA E 358 REMARK 465 VAL E 359 REMARK 465 LYS E 360 REMARK 465 LYS E 361 REMARK 465 ASN E 362 REMARK 465 THR E 363 REMARK 465 VAL E 364 REMARK 465 ASN E 365 REMARK 465 GLY E 366 REMARK 465 THR E 367 REMARK 465 GLY E 368 REMARK 465 THR E 369 REMARK 465 PRO E 370 REMARK 465 VAL E 371 REMARK 465 HIS E 372 REMARK 465 ILE E 373 REMARK 465 SER E 374 REMARK 465 THR E 375 REMARK 465 LEU E 376 REMARK 465 GLN E 377 REMARK 465 VAL E 378 REMARK 465 GLY E 379 REMARK 465 GLU E 380 REMARK 465 THR E 381 REMARK 465 ARG E 382 REMARK 465 CYS E 383 REMARK 465 LYS E 384 REMARK 465 LYS E 385 REMARK 465 VAL E 386 REMARK 465 CYS E 387 REMARK 465 THR E 388 REMARK 465 SER E 389 REMARK 465 LYS E 390 REMARK 465 SER E 391 REMARK 465 ASP E 392 REMARK 465 LEU E 393 REMARK 465 ARG E 394 REMARK 465 SER E 395 REMARK 465 ASN E 396 REMARK 465 ASP E 397 REMARK 465 PHE E 398 REMARK 465 SER E 399 REMARK 465 ILE E 400 REMARK 465 VAL E 401 REMARK 465 GLY E 402 REMARK 465 SER E 403 REMARK 465 LEU E 404 REMARK 465 PRO E 405 REMARK 465 ARG E 406 REMARK 465 ASP E 407 REMARK 465 PHE E 408 REMARK 465 GLU E 409 REMARK 465 LEU E 410 REMARK 465 SER E 411 REMARK 465 ASN E 412 REMARK 465 TYR E 413 REMARK 465 ASP E 414 REMARK 465 CYS E 415 REMARK 465 TYR E 416 REMARK 465 GLY E 417 REMARK 465 LYS E 418 REMARK 465 PRO E 419 REMARK 465 ILE E 420 REMARK 465 GLU E 421 REMARK 465 VAL E 422 REMARK 465 ASN E 423 REMARK 465 ASN E 424 REMARK 465 GLY E 425 REMARK 465 LEU E 426 REMARK 465 GLY E 427 REMARK 465 LYS E 428 REMARK 465 SER E 429 REMARK 465 GLN E 430 REMARK 465 ALA E 431 REMARK 465 LYS E 432 REMARK 465 ASN E 433 REMARK 465 ASN E 434 REMARK 465 LYS E 435 REMARK 465 LYS E 436 REMARK 465 PRO E 437 REMARK 465 PRO E 438 REMARK 465 PRO E 439 REMARK 465 ALA E 440 REMARK 465 LYS E 441 REMARK 465 PRO E 442 REMARK 465 VAL E 443 REMARK 465 ILE E 444 REMARK 465 PRO E 445 REMARK 465 THR E 446 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 TYR J 92 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 TYR M 92 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 TYR I 92 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 HIS C 311 CG ND1 CD2 CE1 NE2 REMARK 470 PHE C 387 CG CD1 CD2 CE1 CE2 CZ 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 SER I 30 OH TYR I 71 2.04 REMARK 500 O LEU A 98 OG1 THR B 112 2.05 REMARK 500 O LYS D 16 OG SER D 22 2.05 REMARK 500 OG SER J 43 O GLY G 109 2.06 REMARK 500 O SER J 30 OH TYR J 71 2.07 REMARK 500 OG SER K 43 O GLY F 109 2.09 REMARK 500 O SER M 30 OH TYR M 71 2.09 REMARK 500 OD2 ASP B 25 OG SER C 11 2.10 REMARK 500 O THR C 258 OG1 THR C 262 2.10 REMARK 500 O LEU B 98 OG1 THR C 112 2.11 REMARK 500 O LYS B 16 OG SER B 22 2.13 REMARK 500 OG SER E 262 OG SER E 321 2.13 REMARK 500 O LEU D 98 OG1 THR E 135 2.13 REMARK 500 OG SER M 43 O GLY L 109 2.14 REMARK 500 O TYR K 49 OG1 THR K 53 2.14 REMARK 500 O TYR K 92 OG SER E 103 2.15 REMARK 500 O ALA B 282 OH TYR B 413 2.15 REMARK 500 O ASN B 305 OG SER B 308 2.15 REMARK 500 O TYR I 49 OG1 THR I 53 2.16 REMARK 500 OG SER I 43 O GLY H 109 2.16 REMARK 500 OE1 GLN K 6 OG1 THR K 102 2.16 REMARK 500 OG1 THR D 112 O LEU C 98 2.17 REMARK 500 ND2 ASN D 38 O5 NAG T 1 2.18 REMARK 500 OG1 THR J 13 OD2 ASP J 17 2.19 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 CYS B 198 CA - CB - SG ANGL. DEV. = 7.2 DEGREES 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 SER J 30 -167.83 -171.32 REMARK 500 ALA J 51 -6.96 74.26 REMARK 500 ARG J 61 27.01 49.58 REMARK 500 SER J 65 -175.92 -171.95 REMARK 500 ARG G 101 32.15 -96.90 REMARK 500 SER K 30 -13.35 74.70 REMARK 500 THR K 31 -16.49 -146.58 REMARK 500 ALA K 51 -7.98 75.04 REMARK 500 SER K 52 -4.79 -140.65 REMARK 500 ARG F 101 32.94 -99.86 REMARK 500 THR M 13 142.86 -170.42 REMARK 500 VAL M 29 -65.54 -101.86 REMARK 500 SER M 30 -166.40 -172.21 REMARK 500 ALA M 51 -8.54 75.41 REMARK 500 SER M 84 -175.41 -173.43 REMARK 500 ALA L 16 -167.92 -79.88 REMARK 500 PRO L 53 6.42 -69.80 REMARK 500 SER I 30 -167.86 -172.10 REMARK 500 ALA I 51 -10.28 75.02 REMARK 500 SER I 76 -50.50 -120.22 REMARK 500 ALA H 16 -169.57 -79.19 REMARK 500 PRO H 53 2.82 -69.17 REMARK 500 SER H 85 61.22 61.22 REMARK 500 SER D 22 -5.49 76.30 REMARK 500 THR D 112 -10.16 73.03 REMARK 500 THR D 113 175.18 178.14 REMARK 500 LEU D 142 34.56 -97.03 REMARK 500 LEU D 166 118.26 -161.87 REMARK 500 GLN D 186 -8.34 74.08 REMARK 500 TRP D 243 49.71 -90.88 REMARK 500 THR A 21 34.19 -96.70 REMARK 500 ASN A 46 -60.84 -93.86 REMARK 500 LEU A 90 48.45 -91.26 REMARK 500 THR A 112 -10.78 74.46 REMARK 500 THR A 113 153.15 179.51 REMARK 500 GLN A 186 -9.15 76.20 REMARK 500 SER B 9 76.91 55.35 REMARK 500 SER B 22 -5.34 75.77 REMARK 500 THR B 112 -8.63 73.24 REMARK 500 THR B 113 175.32 178.66 REMARK 500 LEU B 142 32.61 -98.06 REMARK 500 GLN B 186 -8.69 73.96 REMARK 500 CYS B 198 16.02 -142.65 REMARK 500 ARG C 20 -8.49 75.44 REMARK 500 SER C 22 -4.44 76.06 REMARK 500 ASP C 97 58.68 -92.67 REMARK 500 PHE C 108 -177.91 -69.55 REMARK 500 THR C 112 -8.67 73.61 REMARK 500 THR C 113 156.33 177.87 REMARK 500 LEU C 134 69.56 60.37 REMARK 500 REMARK 500 THIS ENTRY HAS 57 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-23913 RELATED DB: EMDB REMARK 900 CRYO-EM REVEALS PARTIALLY AND FULLY ASSEMBLED NATIVE GLYCINE REMARK 900 RECEPTORS,HETEROMERIC PENTAMER DBREF 7MLY J 1 107 PDB 7MLY 7MLY 1 107 DBREF 7MLY G 1 118 PDB 7MLY 7MLY 1 118 DBREF 7MLY K 1 107 PDB 7MLY 7MLY 1 107 DBREF 7MLY F 1 118 PDB 7MLY 7MLY 1 118 DBREF 7MLY M 1 107 PDB 7MLY 7MLY 1 107 DBREF 7MLY L 1 118 PDB 7MLY 7MLY 1 118 DBREF 7MLY I 1 107 PDB 7MLY 7MLY 1 107 DBREF 7MLY H 1 118 PDB 7MLY 7MLY 1 118 DBREF 7MLY D -27 419 UNP F1RQB7 F1RQB7_PIG 1 447 DBREF 7MLY A -27 419 UNP F1RQB7 F1RQB7_PIG 1 447 DBREF 7MLY B -27 419 UNP F1RQB7 F1RQB7_PIG 1 447 DBREF 7MLY C -27 419 UNP F1RQB7 F1RQB7_PIG 1 447 DBREF 7MLY E -21 475 UNP Q6KBX4 Q6KBX4_PIG 1 497 SEQRES 1 J 107 ASP ILE VAL MET THR GLN SER HIS LYS PHE MET SER THR SEQRES 2 J 107 SER VAL GLY ASP ARG VAL SER ILE THR CYS LYS ALA SER SEQRES 3 J 107 GLN ASP VAL SER THR ALA VAL ALA TRP TYR GLN GLN LYS SEQRES 4 J 107 PRO GLY GLN SER PRO LYS LEU LEU ILE TYR TRP ALA SER SEQRES 5 J 107 THR ARG HIS THR GLY VAL PRO GLY ARG PHE THR GLY SER SEQRES 6 J 107 GLY SER GLY THR ASP TYR THR LEU THR ILE SER SER VAL SEQRES 7 J 107 GLN ALA GLU ASP LEU SER LEU TYR TYR CYS GLN GLN HIS SEQRES 8 J 107 TYR SER THR PRO ARG THR PHE GLY GLY GLY THR LYS LEU SEQRES 9 J 107 GLU ILE LYS SEQRES 1 G 118 GLN VAL GLN LEU GLN GLN SER GLY ALA GLU LEU MET LYS SEQRES 2 G 118 PRO GLY ALA ALA VAL LYS ILE SER CYS LYS ALA THR GLY SEQRES 3 G 118 HIS THR ILE SER ARG TYR TRP ILE ASP TRP LEU LYS GLN SEQRES 4 G 118 ARG PRO GLY HIS GLY LEU GLU TRP ILE GLY GLU ILE LEU SEQRES 5 G 118 PRO GLY SER GLY SER THR ASN TYR ASN GLU LYS PHE LYS SEQRES 6 G 118 GLY LYS ALA THR PHE THR ALA GLU LYS SER SER ASN THR SEQRES 7 G 118 ALA TYR MET GLN LEU SER SER LEU THR SER GLU ASP SER SEQRES 8 G 118 ALA VAL TYR TYR CYS ALA MET GLY VAL ARG GLY ASN TYR SEQRES 9 G 118 PHE ASP TYR TRP GLY GLN GLY THR THR LEU THR VAL SER SEQRES 10 G 118 SER SEQRES 1 K 107 ASP ILE VAL MET THR GLN SER HIS LYS PHE MET SER THR SEQRES 2 K 107 SER VAL GLY ASP ARG VAL SER ILE THR CYS LYS ALA SER SEQRES 3 K 107 GLN ASP VAL SER THR ALA VAL ALA TRP TYR GLN GLN LYS SEQRES 4 K 107 PRO GLY GLN SER PRO LYS LEU LEU ILE TYR TRP ALA SER SEQRES 5 K 107 THR ARG HIS THR GLY VAL PRO GLY ARG PHE THR GLY SER SEQRES 6 K 107 GLY SER GLY THR ASP TYR THR LEU THR ILE SER SER VAL SEQRES 7 K 107 GLN ALA GLU ASP LEU SER LEU TYR TYR CYS GLN GLN HIS SEQRES 8 K 107 TYR SER THR PRO ARG THR PHE GLY GLY GLY THR LYS LEU SEQRES 9 K 107 GLU ILE LYS SEQRES 1 F 118 GLN VAL GLN LEU GLN GLN SER GLY ALA GLU LEU MET LYS SEQRES 2 F 118 PRO GLY ALA ALA VAL LYS ILE SER CYS LYS ALA THR GLY SEQRES 3 F 118 HIS THR ILE SER ARG TYR TRP ILE ASP TRP LEU LYS GLN SEQRES 4 F 118 ARG PRO GLY HIS GLY LEU GLU TRP ILE GLY GLU ILE LEU SEQRES 5 F 118 PRO GLY SER GLY SER THR ASN TYR ASN GLU LYS PHE LYS SEQRES 6 F 118 GLY LYS ALA THR PHE THR ALA GLU LYS SER SER ASN THR SEQRES 7 F 118 ALA TYR MET GLN LEU SER SER LEU THR SER GLU ASP SER SEQRES 8 F 118 ALA VAL TYR TYR CYS ALA MET GLY VAL ARG GLY ASN TYR SEQRES 9 F 118 PHE ASP TYR TRP GLY GLN GLY THR THR LEU THR VAL SER SEQRES 10 F 118 SER SEQRES 1 M 107 ASP ILE VAL MET THR GLN SER HIS LYS PHE MET SER THR SEQRES 2 M 107 SER VAL GLY ASP ARG VAL SER ILE THR CYS LYS ALA SER SEQRES 3 M 107 GLN ASP VAL SER THR ALA VAL ALA TRP TYR GLN GLN LYS SEQRES 4 M 107 PRO GLY GLN SER PRO LYS LEU LEU ILE TYR TRP ALA SER SEQRES 5 M 107 THR ARG HIS THR GLY VAL PRO GLY ARG PHE THR GLY SER SEQRES 6 M 107 GLY SER GLY THR ASP TYR THR LEU THR ILE SER SER VAL SEQRES 7 M 107 GLN ALA GLU ASP LEU SER LEU TYR TYR CYS GLN GLN HIS SEQRES 8 M 107 TYR SER THR PRO ARG THR PHE GLY GLY GLY THR LYS LEU SEQRES 9 M 107 GLU ILE LYS SEQRES 1 L 118 GLN VAL GLN LEU GLN GLN SER GLY ALA GLU LEU MET LYS SEQRES 2 L 118 PRO GLY ALA ALA VAL LYS ILE SER CYS LYS ALA THR GLY SEQRES 3 L 118 HIS THR ILE SER ARG TYR TRP ILE ASP TRP LEU LYS GLN SEQRES 4 L 118 ARG PRO GLY HIS GLY LEU GLU TRP ILE GLY GLU ILE LEU SEQRES 5 L 118 PRO GLY SER GLY SER THR ASN TYR ASN GLU LYS PHE LYS SEQRES 6 L 118 GLY LYS ALA THR PHE THR ALA GLU LYS SER SER ASN THR SEQRES 7 L 118 ALA TYR MET GLN LEU SER SER LEU THR SER GLU ASP SER SEQRES 8 L 118 ALA VAL TYR TYR CYS ALA MET GLY VAL ARG GLY ASN TYR SEQRES 9 L 118 PHE ASP TYR TRP GLY GLN GLY THR THR LEU THR VAL SER SEQRES 10 L 118 SER SEQRES 1 I 107 ASP ILE VAL MET THR GLN SER HIS LYS PHE MET SER THR SEQRES 2 I 107 SER VAL GLY ASP ARG VAL SER ILE THR CYS LYS ALA SER SEQRES 3 I 107 GLN ASP VAL SER THR ALA VAL ALA TRP TYR GLN GLN LYS SEQRES 4 I 107 PRO GLY GLN SER PRO LYS LEU LEU ILE TYR TRP ALA SER SEQRES 5 I 107 THR ARG HIS THR GLY VAL PRO GLY ARG PHE THR GLY SER SEQRES 6 I 107 GLY SER GLY THR ASP TYR THR LEU THR ILE SER SER VAL SEQRES 7 I 107 GLN ALA GLU ASP LEU SER LEU TYR TYR CYS GLN GLN HIS SEQRES 8 I 107 TYR SER THR PRO ARG THR PHE GLY GLY GLY THR LYS LEU SEQRES 9 I 107 GLU ILE LYS SEQRES 1 H 118 GLN VAL GLN LEU GLN GLN SER GLY ALA GLU LEU MET LYS SEQRES 2 H 118 PRO GLY ALA ALA VAL LYS ILE SER CYS LYS ALA THR GLY SEQRES 3 H 118 HIS THR ILE SER ARG TYR TRP ILE ASP TRP LEU LYS GLN SEQRES 4 H 118 ARG PRO GLY HIS GLY LEU GLU TRP ILE GLY GLU ILE LEU SEQRES 5 H 118 PRO GLY SER GLY SER THR ASN TYR ASN GLU LYS PHE LYS SEQRES 6 H 118 GLY LYS ALA THR PHE THR ALA GLU LYS SER SER ASN THR SEQRES 7 H 118 ALA TYR MET GLN LEU SER SER LEU THR SER GLU ASP SER SEQRES 8 H 118 ALA VAL TYR TYR CYS ALA MET GLY VAL ARG GLY ASN TYR SEQRES 9 H 118 PHE ASP TYR TRP GLY GLN GLY THR THR LEU THR VAL SER SEQRES 10 H 118 SER SEQRES 1 D 447 MET TYR ARG PHE ASN THR LEU ARG LEU TYR LEU TRP GLU SEQRES 2 D 447 THR ILE VAL PHE PHE SER LEU ALA ALA SER LYS GLU ALA SEQRES 3 D 447 GLU ALA ALA ARG SER ALA SER LYS PRO MET SER PRO SER SEQRES 4 D 447 ASP PHE LEU ASP LYS LEU MET GLY ARG THR SER GLY TYR SEQRES 5 D 447 ASP ALA ARG ILE ARG PRO ASN PHE LYS GLY PRO PRO VAL SEQRES 6 D 447 ASN VAL SER CYS ASN ILE PHE ILE ASN SER PHE GLY SER SEQRES 7 D 447 ILE ALA GLU THR THR MET ASP TYR ARG VAL ASN ILE PHE SEQRES 8 D 447 LEU ARG GLN GLN TRP ASN ASP PRO ARG LEU ALA TYR ASN SEQRES 9 D 447 GLU TYR PRO ASP ASP SER LEU ASP LEU ASP PRO SER MET SEQRES 10 D 447 LEU ASP SER ILE TRP LYS PRO ASP LEU PHE PHE ALA ASN SEQRES 11 D 447 GLU LYS GLY ALA HIS PHE HIS GLU ILE THR THR ASP ASN SEQRES 12 D 447 LYS LEU LEU ARG ILE SER ARG ASN GLY ASN VAL LEU TYR SEQRES 13 D 447 SER ILE ARG ILE THR LEU THR LEU ALA CYS PRO MET ASP SEQRES 14 D 447 LEU LYS ASN PHE PRO MET ASP VAL GLN THR CYS ILE MET SEQRES 15 D 447 GLN LEU GLU SER PHE GLY TYR THR MET ASN ASP LEU ILE SEQRES 16 D 447 PHE GLU TRP GLN GLU GLN GLY ALA VAL GLN VAL ALA ASP SEQRES 17 D 447 GLY LEU THR LEU PRO GLN PHE ILE LEU LYS GLU GLU LYS SEQRES 18 D 447 ASP LEU ARG TYR CYS THR LYS HIS TYR ASN THR GLY LYS SEQRES 19 D 447 PHE THR CYS ILE GLU ALA ARG PHE HIS LEU GLU ARG GLN SEQRES 20 D 447 MET GLY TYR TYR LEU ILE GLN MET TYR ILE PRO SER LEU SEQRES 21 D 447 LEU ILE VAL ILE LEU SER TRP ILE SER PHE TRP ILE ASN SEQRES 22 D 447 MET ASP ALA ALA PRO ALA ARG VAL GLY LEU GLY ILE THR SEQRES 23 D 447 THR VAL LEU THR MET THR THR GLN SER SER GLY SER ARG SEQRES 24 D 447 ALA SER LEU PRO LYS VAL SER TYR VAL LYS ALA ILE ASP SEQRES 25 D 447 ILE TRP MET ALA VAL CYS LEU LEU PHE VAL PHE SER ALA SEQRES 26 D 447 LEU LEU GLU TYR ALA ALA VAL ASN PHE VAL SER ARG GLN SEQRES 27 D 447 HIS LYS GLU LEU LEU ARG PHE ARG ARG LYS ARG ARG HIS SEQRES 28 D 447 HIS LYS SER PRO MET LEU ASN LEU PHE GLN GLU ASP GLU SEQRES 29 D 447 ALA GLY GLU GLY ARG PHE ASN PHE SER ALA TYR GLY MET SEQRES 30 D 447 GLY PRO ALA CYS LEU GLN ALA LYS ASP GLY ILE SER VAL SEQRES 31 D 447 LYS GLY ALA ASN ASN THR THR THR ASN PRO PRO PRO ALA SEQRES 32 D 447 PRO SER LYS SER PRO GLU GLU MET ARG LYS LEU PHE ILE SEQRES 33 D 447 GLN ARG ALA LYS LYS ILE ASP LYS ILE SER ARG ILE GLY SEQRES 34 D 447 PHE PRO MET ALA PHE LEU ILE PHE ASN MET PHE TYR TRP SEQRES 35 D 447 ILE ILE TYR LYS ILE SEQRES 1 A 447 MET TYR ARG PHE ASN THR LEU ARG LEU TYR LEU TRP GLU SEQRES 2 A 447 THR ILE VAL PHE PHE SER LEU ALA ALA SER LYS GLU ALA SEQRES 3 A 447 GLU ALA ALA ARG SER ALA SER LYS PRO MET SER PRO SER SEQRES 4 A 447 ASP PHE LEU ASP LYS LEU MET GLY ARG THR SER GLY TYR SEQRES 5 A 447 ASP ALA ARG ILE ARG PRO ASN PHE LYS GLY PRO PRO VAL SEQRES 6 A 447 ASN VAL SER CYS ASN ILE PHE ILE ASN SER PHE GLY SER SEQRES 7 A 447 ILE ALA GLU THR THR MET ASP TYR ARG VAL ASN ILE PHE SEQRES 8 A 447 LEU ARG GLN GLN TRP ASN ASP PRO ARG LEU ALA TYR ASN SEQRES 9 A 447 GLU TYR PRO ASP ASP SER LEU ASP LEU ASP PRO SER MET SEQRES 10 A 447 LEU ASP SER ILE TRP LYS PRO ASP LEU PHE PHE ALA ASN SEQRES 11 A 447 GLU LYS GLY ALA HIS PHE HIS GLU ILE THR THR ASP ASN SEQRES 12 A 447 LYS LEU LEU ARG ILE SER ARG ASN GLY ASN VAL LEU TYR SEQRES 13 A 447 SER ILE ARG ILE THR LEU THR LEU ALA CYS PRO MET ASP SEQRES 14 A 447 LEU LYS ASN PHE PRO MET ASP VAL GLN THR CYS ILE MET SEQRES 15 A 447 GLN LEU GLU SER PHE GLY TYR THR MET ASN ASP LEU ILE SEQRES 16 A 447 PHE GLU TRP GLN GLU GLN GLY ALA VAL GLN VAL ALA ASP SEQRES 17 A 447 GLY LEU THR LEU PRO GLN PHE ILE LEU LYS GLU GLU LYS SEQRES 18 A 447 ASP LEU ARG TYR CYS THR LYS HIS TYR ASN THR GLY LYS SEQRES 19 A 447 PHE THR CYS ILE GLU ALA ARG PHE HIS LEU GLU ARG GLN SEQRES 20 A 447 MET GLY TYR TYR LEU ILE GLN MET TYR ILE PRO SER LEU SEQRES 21 A 447 LEU ILE VAL ILE LEU SER TRP ILE SER PHE TRP ILE ASN SEQRES 22 A 447 MET ASP ALA ALA PRO ALA ARG VAL GLY LEU GLY ILE THR SEQRES 23 A 447 THR VAL LEU THR MET THR THR GLN SER SER GLY SER ARG SEQRES 24 A 447 ALA SER LEU PRO LYS VAL SER TYR VAL LYS ALA ILE ASP SEQRES 25 A 447 ILE TRP MET ALA VAL CYS LEU LEU PHE VAL PHE SER ALA SEQRES 26 A 447 LEU LEU GLU TYR ALA ALA VAL ASN PHE VAL SER ARG GLN SEQRES 27 A 447 HIS LYS GLU LEU LEU ARG PHE ARG ARG LYS ARG ARG HIS SEQRES 28 A 447 HIS LYS SER PRO MET LEU ASN LEU PHE GLN GLU ASP GLU SEQRES 29 A 447 ALA GLY GLU GLY ARG PHE ASN PHE SER ALA TYR GLY MET SEQRES 30 A 447 GLY PRO ALA CYS LEU GLN ALA LYS ASP GLY ILE SER VAL SEQRES 31 A 447 LYS GLY ALA ASN ASN THR THR THR ASN PRO PRO PRO ALA SEQRES 32 A 447 PRO SER LYS SER PRO GLU GLU MET ARG LYS LEU PHE ILE SEQRES 33 A 447 GLN ARG ALA LYS LYS ILE ASP LYS ILE SER ARG ILE GLY SEQRES 34 A 447 PHE PRO MET ALA PHE LEU ILE PHE ASN MET PHE TYR TRP SEQRES 35 A 447 ILE ILE TYR LYS ILE SEQRES 1 B 447 MET TYR ARG PHE ASN THR LEU ARG LEU TYR LEU TRP GLU SEQRES 2 B 447 THR ILE VAL PHE PHE SER LEU ALA ALA SER LYS GLU ALA SEQRES 3 B 447 GLU ALA ALA ARG SER ALA SER LYS PRO MET SER PRO SER SEQRES 4 B 447 ASP PHE LEU ASP LYS LEU MET GLY ARG THR SER GLY TYR SEQRES 5 B 447 ASP ALA ARG ILE ARG PRO ASN PHE LYS GLY PRO PRO VAL SEQRES 6 B 447 ASN VAL SER CYS ASN ILE PHE ILE ASN SER PHE GLY SER SEQRES 7 B 447 ILE ALA GLU THR THR MET ASP TYR ARG VAL ASN ILE PHE SEQRES 8 B 447 LEU ARG GLN GLN TRP ASN ASP PRO ARG LEU ALA TYR ASN SEQRES 9 B 447 GLU TYR PRO ASP ASP SER LEU ASP LEU ASP PRO SER MET SEQRES 10 B 447 LEU ASP SER ILE TRP LYS PRO ASP LEU PHE PHE ALA ASN SEQRES 11 B 447 GLU LYS GLY ALA HIS PHE HIS GLU ILE THR THR ASP ASN SEQRES 12 B 447 LYS LEU LEU ARG ILE SER ARG ASN GLY ASN VAL LEU TYR SEQRES 13 B 447 SER ILE ARG ILE THR LEU THR LEU ALA CYS PRO MET ASP SEQRES 14 B 447 LEU LYS ASN PHE PRO MET ASP VAL GLN THR CYS ILE MET SEQRES 15 B 447 GLN LEU GLU SER PHE GLY TYR THR MET ASN ASP LEU ILE SEQRES 16 B 447 PHE GLU TRP GLN GLU GLN GLY ALA VAL GLN VAL ALA ASP SEQRES 17 B 447 GLY LEU THR LEU PRO GLN PHE ILE LEU LYS GLU GLU LYS SEQRES 18 B 447 ASP LEU ARG TYR CYS THR LYS HIS TYR ASN THR GLY LYS SEQRES 19 B 447 PHE THR CYS ILE GLU ALA ARG PHE HIS LEU GLU ARG GLN SEQRES 20 B 447 MET GLY TYR TYR LEU ILE GLN MET TYR ILE PRO SER LEU SEQRES 21 B 447 LEU ILE VAL ILE LEU SER TRP ILE SER PHE TRP ILE ASN SEQRES 22 B 447 MET ASP ALA ALA PRO ALA ARG VAL GLY LEU GLY ILE THR SEQRES 23 B 447 THR VAL LEU THR MET THR THR GLN SER SER GLY SER ARG SEQRES 24 B 447 ALA SER LEU PRO LYS VAL SER TYR VAL LYS ALA ILE ASP SEQRES 25 B 447 ILE TRP MET ALA VAL CYS LEU LEU PHE VAL PHE SER ALA SEQRES 26 B 447 LEU LEU GLU TYR ALA ALA VAL ASN PHE VAL SER ARG GLN SEQRES 27 B 447 HIS LYS GLU LEU LEU ARG PHE ARG ARG LYS ARG ARG HIS SEQRES 28 B 447 HIS LYS SER PRO MET LEU ASN LEU PHE GLN GLU ASP GLU SEQRES 29 B 447 ALA GLY GLU GLY ARG PHE ASN PHE SER ALA TYR GLY MET SEQRES 30 B 447 GLY PRO ALA CYS LEU GLN ALA LYS ASP GLY ILE SER VAL SEQRES 31 B 447 LYS GLY ALA ASN ASN THR THR THR ASN PRO PRO PRO ALA SEQRES 32 B 447 PRO SER LYS SER PRO GLU GLU MET ARG LYS LEU PHE ILE SEQRES 33 B 447 GLN ARG ALA LYS LYS ILE ASP LYS ILE SER ARG ILE GLY SEQRES 34 B 447 PHE PRO MET ALA PHE LEU ILE PHE ASN MET PHE TYR TRP SEQRES 35 B 447 ILE ILE TYR LYS ILE SEQRES 1 C 447 MET TYR ARG PHE ASN THR LEU ARG LEU TYR LEU TRP GLU SEQRES 2 C 447 THR ILE VAL PHE PHE SER LEU ALA ALA SER LYS GLU ALA SEQRES 3 C 447 GLU ALA ALA ARG SER ALA SER LYS PRO MET SER PRO SER SEQRES 4 C 447 ASP PHE LEU ASP LYS LEU MET GLY ARG THR SER GLY TYR SEQRES 5 C 447 ASP ALA ARG ILE ARG PRO ASN PHE LYS GLY PRO PRO VAL SEQRES 6 C 447 ASN VAL SER CYS ASN ILE PHE ILE ASN SER PHE GLY SER SEQRES 7 C 447 ILE ALA GLU THR THR MET ASP TYR ARG VAL ASN ILE PHE SEQRES 8 C 447 LEU ARG GLN GLN TRP ASN ASP PRO ARG LEU ALA TYR ASN SEQRES 9 C 447 GLU TYR PRO ASP ASP SER LEU ASP LEU ASP PRO SER MET SEQRES 10 C 447 LEU ASP SER ILE TRP LYS PRO ASP LEU PHE PHE ALA ASN SEQRES 11 C 447 GLU LYS GLY ALA HIS PHE HIS GLU ILE THR THR ASP ASN SEQRES 12 C 447 LYS LEU LEU ARG ILE SER ARG ASN GLY ASN VAL LEU TYR SEQRES 13 C 447 SER ILE ARG ILE THR LEU THR LEU ALA CYS PRO MET ASP SEQRES 14 C 447 LEU LYS ASN PHE PRO MET ASP VAL GLN THR CYS ILE MET SEQRES 15 C 447 GLN LEU GLU SER PHE GLY TYR THR MET ASN ASP LEU ILE SEQRES 16 C 447 PHE GLU TRP GLN GLU GLN GLY ALA VAL GLN VAL ALA ASP SEQRES 17 C 447 GLY LEU THR LEU PRO GLN PHE ILE LEU LYS GLU GLU LYS SEQRES 18 C 447 ASP LEU ARG TYR CYS THR LYS HIS TYR ASN THR GLY LYS SEQRES 19 C 447 PHE THR CYS ILE GLU ALA ARG PHE HIS LEU GLU ARG GLN SEQRES 20 C 447 MET GLY TYR TYR LEU ILE GLN MET TYR ILE PRO SER LEU SEQRES 21 C 447 LEU ILE VAL ILE LEU SER TRP ILE SER PHE TRP ILE ASN SEQRES 22 C 447 MET ASP ALA ALA PRO ALA ARG VAL GLY LEU GLY ILE THR SEQRES 23 C 447 THR VAL LEU THR MET THR THR GLN SER SER GLY SER ARG SEQRES 24 C 447 ALA SER LEU PRO LYS VAL SER TYR VAL LYS ALA ILE ASP SEQRES 25 C 447 ILE TRP MET ALA VAL CYS LEU LEU PHE VAL PHE SER ALA SEQRES 26 C 447 LEU LEU GLU TYR ALA ALA VAL ASN PHE VAL SER ARG GLN SEQRES 27 C 447 HIS LYS GLU LEU LEU ARG PHE ARG ARG LYS ARG ARG HIS SEQRES 28 C 447 HIS LYS SER PRO MET LEU ASN LEU PHE GLN GLU ASP GLU SEQRES 29 C 447 ALA GLY GLU GLY ARG PHE ASN PHE SER ALA TYR GLY MET SEQRES 30 C 447 GLY PRO ALA CYS LEU GLN ALA LYS ASP GLY ILE SER VAL SEQRES 31 C 447 LYS GLY ALA ASN ASN THR THR THR ASN PRO PRO PRO ALA SEQRES 32 C 447 PRO SER LYS SER PRO GLU GLU MET ARG LYS LEU PHE ILE SEQRES 33 C 447 GLN ARG ALA LYS LYS ILE ASP LYS ILE SER ARG ILE GLY SEQRES 34 C 447 PHE PRO MET ALA PHE LEU ILE PHE ASN MET PHE TYR TRP SEQRES 35 C 447 ILE ILE TYR LYS ILE SEQRES 1 E 497 MET LYS PHE LEU LEU ALA VAL ALA PHE PHE ILE LEU ILE SEQRES 2 E 497 SER LEU TRP VAL GLU GLU ALA TYR SER LYS GLU LYS SER SEQRES 3 E 497 SER LYS LYS GLY LYS GLY LYS LYS LYS GLN TYR LEU CYS SEQRES 4 E 497 PRO SER GLN GLN SER ALA GLU ASP LEU ALA ARG VAL PRO SEQRES 5 E 497 ALA ASN SER THR SER ASN ILE LEU ASN ARG LEU LEU VAL SEQRES 6 E 497 SER TYR ASP PRO ARG ILE ARG PRO ASN PHE LYS GLY ILE SEQRES 7 E 497 PRO VAL ASP VAL VAL VAL ASN ILE PHE ILE ASN SER PHE SEQRES 8 E 497 GLY SER ILE GLN GLU THR THR MET ASP TYR ARG VAL ASN SEQRES 9 E 497 ILE PHE LEU ARG GLN LYS TRP ASN ASP PRO ARG LEU LYS SEQRES 10 E 497 LEU PRO SER ASP PHE ARG GLY SER ASP ALA LEU THR VAL SEQRES 11 E 497 ASP PRO THR MET TYR LYS CYS LEU TRP LYS PRO ASP LEU SEQRES 12 E 497 PHE PHE ALA ASN GLU LYS SER ALA ASN PHE HIS ASP VAL SEQRES 13 E 497 THR GLN GLU ASN ILE LEU LEU PHE ILE PHE ARG ASP GLY SEQRES 14 E 497 ASP VAL LEU VAL SER MET ARG LEU SER ILE THR LEU SER SEQRES 15 E 497 CYS PRO LEU ASP LEU THR LEU PHE PRO MET ASP THR GLN SEQRES 16 E 497 ARG CYS LYS MET GLN LEU GLU SER PHE GLY TYR THR THR SEQRES 17 E 497 ASP ASP LEU ARG PHE ILE TRP GLN SER GLY ASP PRO VAL SEQRES 18 E 497 GLN LEU GLU LYS ILE ALA LEU PRO GLN PHE ASP ILE LYS SEQRES 19 E 497 LYS GLU ASP ILE GLU TYR GLY ASN CYS THR LYS TYR TYR SEQRES 20 E 497 LYS GLY THR GLY TYR TYR THR CYS VAL GLU VAL ILE PHE SEQRES 21 E 497 THR LEU ARG ARG GLN VAL GLY PHE TYR MET MET GLY VAL SEQRES 22 E 497 TYR ALA PRO THR LEU LEU ILE VAL VAL LEU SER TRP LEU SEQRES 23 E 497 SER PHE TRP ILE ASN PRO ASP ALA SER ALA ALA ARG VAL SEQRES 24 E 497 PRO LEU GLY ILE PHE SER VAL LEU SER LEU ALA SER GLU SEQRES 25 E 497 CYS THR THR LEU ALA ALA GLU LEU PRO LYS VAL SER TYR SEQRES 26 E 497 VAL LYS ALA LEU ASP VAL TRP LEU ILE ALA CYS LEU LEU SEQRES 27 E 497 PHE GLY PHE ALA SER LEU VAL GLU TYR ALA VAL VAL GLN SEQRES 28 E 497 VAL MET LEU ASN ASN PRO LYS ARG VAL GLU ALA GLU LYS SEQRES 29 E 497 ALA ARG ILE ALA LYS ALA GLU GLN ALA ASP GLY LYS GLY SEQRES 30 E 497 ALA ASN ALA VAL LYS LYS ASN THR VAL ASN GLY THR GLY SEQRES 31 E 497 THR PRO VAL HIS ILE SER THR LEU GLN VAL GLY GLU THR SEQRES 32 E 497 ARG CYS LYS LYS VAL CYS THR SER LYS SER ASP LEU ARG SEQRES 33 E 497 SER ASN ASP PHE SER ILE VAL GLY SER LEU PRO ARG ASP SEQRES 34 E 497 PHE GLU LEU SER ASN TYR ASP CYS TYR GLY LYS PRO ILE SEQRES 35 E 497 GLU VAL ASN ASN GLY LEU GLY LYS SER GLN ALA LYS ASN SEQRES 36 E 497 ASN LYS LYS PRO PRO PRO ALA LYS PRO VAL ILE PRO THR SEQRES 37 E 497 ALA ALA LYS ARG ILE ASP LEU TYR ALA ARG ALA LEU PHE SEQRES 38 E 497 PRO PHE CYS PHE LEU PHE PHE ASN VAL ILE TYR TRP SER SEQRES 39 E 497 ILE TYR LEU HET HP6 D 501 23 HET HP6 D 502 23 HET DD9 D 503 29 HET LNK D 504 17 HET MYS D 505 47 HET D10 D 506 32 HET LNK D 507 17 HET NBU D 508 14 HET NBU D 509 14 HET GLY A 501 5 HET GLY A 502 5 HET D12 A 503 38 HET HP6 A 504 23 HET HP6 A 505 23 HET LNK A 506 17 HET OCT A 507 26 HET OCT A 508 26 HET LNK A 509 17 HET HEX A 510 20 HET OCT A 511 26 HET DD9 A 512 29 HET GLY B 501 5 HET HP6 B 502 23 HET DD9 B 503 29 HET LNK B 504 17 HET HEX B 505 20 HET LNK B 506 17 HET NBU B 507 14 HET NBU B 508 14 HET NBU B 509 14 HET HP6 B 510 23 HET GLY C 501 5 HET D12 C 502 38 HET LNK C 503 17 HET OCT C 504 26 HET LNK C 505 17 HET NBU C 506 14 HET NBU C 507 14 HET NBU C 508 14 HET NBU C 509 14 HET HEX C 510 20 HET GLY E 501 5 HET HP6 E 502 23 HET HP6 E 503 23 HET HP6 E 504 23 HET LNK E 505 17 HET UND E 506 35 HET LNK E 507 17 HET NAG T 1 14 HET NAG T 2 14 HET BMA T 3 11 HET MAN T 4 11 HET MAN T 5 11 HET NAG Z 1 14 HET NAG Z 2 14 HET BMA Z 3 11 HET MAN Z 4 11 HET MAN Z 5 11 HET NAG f 1 14 HET NAG f 2 14 HET BMA f 3 11 HET MAN f 4 11 HET NAG l 1 14 HET NAG l 2 14 HET BMA l 3 11 HET MAN l 4 11 HET NAG r 1 14 HET NAG r 2 14 HET BMA r 3 11 HETNAM HP6 HEPTANE HETNAM DD9 NONANE HETNAM LNK PENTANE HETNAM MYS PENTADECANE HETNAM D10 DECANE HETNAM NBU N-BUTANE HETNAM GLY GLYCINE HETNAM D12 DODECANE HETNAM OCT N-OCTANE HETNAM HEX HEXANE HETNAM UND UNDECANE HETNAM NAG N-ACETYL-D-GLUCOSAMINE HETNAM BMA BETA-D-MANNOSE HETNAM MAN ALPHA-D-MANNOSE HETSYN UND LIPID FRAGMENT FORMUL 14 HP6 9(C7 H16) FORMUL 16 DD9 3(C9 H20) FORMUL 17 LNK 10(C5 H12) FORMUL 18 MYS C15 H32 FORMUL 19 D10 C10 H22 FORMUL 21 NBU 9(C4 H10) FORMUL 23 GLY 5(C2 H5 N O2) FORMUL 25 D12 2(C12 H26) FORMUL 29 OCT 4(C8 H18) FORMUL 32 HEX 3(C6 H14) FORMUL 60 UND C11 H24 FORMUL 62 NAG 10(C8 H15 N O6) FORMUL 62 BMA 5(C6 H12 O6) FORMUL 62 MAN 6(C6 H12 O6) HELIX 1 AA1 GLN J 79 LEU J 83 5 5 HELIX 2 AA2 ASN G 61 LYS G 65 5 5 HELIX 3 AA3 THR F 87 SER F 91 5 5 HELIX 4 AA4 GLN M 79 LEU M 83 5 5 HELIX 5 AA5 GLU L 62 LYS L 65 5 4 HELIX 6 AA6 THR L 87 SER L 91 5 5 HELIX 7 AA7 TRP I 50 SER I 52 5 3 HELIX 8 AA8 GLU H 62 LYS H 65 5 4 HELIX 9 AA9 THR H 87 SER H 91 5 5 HELIX 10 AB1 ASP D 12 MET D 18 1 7 HELIX 11 AB2 ASP D 70 ALA D 74 5 5 HELIX 12 AB3 ASP D 86 SER D 92 5 7 HELIX 13 AB4 ASN D 144 MET D 147 5 4 HELIX 14 AB5 MET D 220 MET D 227 1 8 HELIX 15 AB6 MET D 227 TRP D 239 1 13 HELIX 16 AB7 ILE D 240 ILE D 244 5 5 HELIX 17 AB8 ALA D 248 ARG D 271 1 24 HELIX 18 AB9 ILE D 283 SER D 308 1 26 HELIX 19 AC1 PHE D 387 ILE D 415 1 29 HELIX 20 AC2 SER A 9 MET A 18 1 10 HELIX 21 AC3 PRO A 71 ALA A 74 5 4 HELIX 22 AC4 MET A 220 MET A 227 1 8 HELIX 23 AC5 MET A 227 ILE A 240 1 14 HELIX 24 AC6 SER A 241 TRP A 243 5 3 HELIX 25 AC7 ALA A 248 SER A 270 1 23 HELIX 26 AC8 ILE A 283 ARG A 309 1 27 HELIX 27 AC9 LYS A 385 LYS A 418 1 34 HELIX 28 AD1 SER B 9 MET B 18 1 10 HELIX 29 AD2 PRO B 71 ALA B 74 5 4 HELIX 30 AD3 ASP B 86 ASP B 91 5 6 HELIX 31 AD4 ASN B 144 MET B 147 5 4 HELIX 32 AD5 TYR B 222 MET B 227 1 6 HELIX 33 AD6 MET B 227 SER B 238 1 12 HELIX 34 AD7 TRP B 239 TRP B 243 5 5 HELIX 35 AD8 ALA B 248 GLY B 269 1 22 HELIX 36 AD9 ILE B 283 ARG B 309 1 27 HELIX 37 AE1 PHE B 387 ILE B 397 1 11 HELIX 38 AE2 ILE B 397 LYS B 418 1 22 HELIX 39 AE3 SER C 11 MET C 18 1 8 HELIX 40 AE4 ASP C 70 ALA C 74 5 5 HELIX 41 AE5 ASP C 86 ASP C 91 5 6 HELIX 42 AE6 ASN C 144 MET C 147 5 4 HELIX 43 AE7 MET C 220 MET C 227 1 8 HELIX 44 AE8 MET C 227 SER C 238 1 12 HELIX 45 AE9 TRP C 239 PHE C 242 5 4 HELIX 46 AF1 ALA C 248 SER C 273 1 26 HELIX 47 AF2 ILE C 283 LEU C 314 1 32 HELIX 48 AF3 PRO C 380 ARG C 384 5 5 HELIX 49 AF4 PHE C 387 TYR C 417 1 31 HELIX 50 AF5 SER E 35 VAL E 43 1 9 HELIX 51 AF6 PRO E 92 LYS E 95 5 4 HELIX 52 AF7 ASP E 109 LEU E 116 5 8 HELIX 53 AF8 VAL E 244 MET E 249 1 6 HELIX 54 AF9 VAL E 251 TRP E 263 1 13 HELIX 55 AG1 LEU E 264 TRP E 267 5 4 HELIX 56 AG2 ALA E 272 ALA E 296 1 25 HELIX 57 AG3 LYS E 305 ASN E 333 1 29 HELIX 58 AG4 ALA E 448 ALA E 457 1 10 HELIX 59 AG5 LEU E 458 LEU E 475 1 18 SHEET 1 AA1 2 MET J 4 GLN J 6 0 SHEET 2 AA1 2 CYS J 23 ALA J 25 -1 O LYS J 24 N THR J 5 SHEET 1 AA2 3 VAL J 19 SER J 20 0 SHEET 2 AA2 3 ASP J 70 ILE J 75 -1 O ILE J 75 N VAL J 19 SHEET 3 AA2 3 THR J 63 SER J 67 -1 N THR J 63 O THR J 74 SHEET 1 AA3 4 THR J 53 ARG J 54 0 SHEET 2 AA3 4 LYS J 45 TYR J 49 -1 N TYR J 49 O THR J 53 SHEET 3 AA3 4 VAL J 33 GLN J 38 -1 N GLN J 37 O LYS J 45 SHEET 4 AA3 4 LEU J 85 GLN J 90 -1 O GLN J 89 N ALA J 34 SHEET 1 AA4 4 LEU G 4 GLN G 6 0 SHEET 2 AA4 4 VAL G 18 ALA G 24 -1 O LYS G 23 N GLN G 5 SHEET 3 AA4 4 THR G 78 LEU G 83 -1 O MET G 81 N ILE G 20 SHEET 4 AA4 4 ALA G 68 GLU G 73 -1 N THR G 71 O TYR G 80 SHEET 1 AA5 4 TRP G 47 ILE G 51 0 SHEET 2 AA5 4 ILE G 34 GLN G 39 -1 N TRP G 36 O ILE G 48 SHEET 3 AA5 4 ALA G 92 TYR G 95 -1 O VAL G 93 N GLN G 39 SHEET 4 AA5 4 THR G 112 LEU G 114 -1 O THR G 112 N TYR G 94 SHEET 1 AA6 4 THR K 5 GLN K 6 0 SHEET 2 AA6 4 VAL K 19 LYS K 24 -1 O LYS K 24 N THR K 5 SHEET 3 AA6 4 TYR K 71 ILE K 75 -1 O LEU K 73 N ILE K 21 SHEET 4 AA6 4 PHE K 62 GLY K 66 -1 N THR K 63 O THR K 74 SHEET 1 AA7 4 THR K 53 ARG K 54 0 SHEET 2 AA7 4 LYS K 45 TYR K 49 -1 N TYR K 49 O THR K 53 SHEET 3 AA7 4 ALA K 34 GLN K 38 -1 N GLN K 37 O LYS K 45 SHEET 4 AA7 4 LEU K 85 GLN K 89 -1 O TYR K 87 N TYR K 36 SHEET 1 AA8 4 LEU F 4 GLN F 6 0 SHEET 2 AA8 4 VAL F 18 ALA F 24 -1 O LYS F 23 N GLN F 5 SHEET 3 AA8 4 THR F 78 LEU F 83 -1 O MET F 81 N ILE F 20 SHEET 4 AA8 4 ALA F 68 GLU F 73 -1 N THR F 71 O TYR F 80 SHEET 1 AA9 6 GLU F 10 LEU F 11 0 SHEET 2 AA9 6 THR F 112 THR F 115 1 O THR F 113 N GLU F 10 SHEET 3 AA9 6 ALA F 92 TYR F 95 -1 N ALA F 92 O LEU F 114 SHEET 4 AA9 6 ILE F 34 GLN F 39 -1 N GLN F 39 O VAL F 93 SHEET 5 AA9 6 LEU F 45 LEU F 52 -1 O ILE F 48 N TRP F 36 SHEET 6 AA9 6 SER F 57 THR F 58 -1 O SER F 57 N LEU F 52 SHEET 1 AB1 2 THR M 5 GLN M 6 0 SHEET 2 AB1 2 CYS M 23 LYS M 24 -1 O LYS M 24 N THR M 5 SHEET 1 AB2 4 THR M 53 ARG M 54 0 SHEET 2 AB2 4 LYS M 45 TYR M 49 -1 N TYR M 49 O THR M 53 SHEET 3 AB2 4 ALA M 34 GLN M 38 -1 N TRP M 35 O LEU M 47 SHEET 4 AB2 4 LEU M 85 GLN M 89 -1 O GLN M 89 N ALA M 34 SHEET 1 AB3 2 PHE M 62 SER M 67 0 SHEET 2 AB3 2 ASP M 70 ILE M 75 -1 O THR M 74 N THR M 63 SHEET 1 AB4 4 LEU L 4 GLN L 6 0 SHEET 2 AB4 4 VAL L 18 ALA L 24 -1 O LYS L 23 N GLN L 5 SHEET 3 AB4 4 THR L 78 LEU L 83 -1 O MET L 81 N ILE L 20 SHEET 4 AB4 4 ALA L 68 PHE L 70 -1 N THR L 69 O GLN L 82 SHEET 1 AB5 6 GLU L 10 LEU L 11 0 SHEET 2 AB5 6 THR L 112 THR L 115 1 O THR L 113 N GLU L 10 SHEET 3 AB5 6 ALA L 92 TYR L 95 -1 N ALA L 92 O LEU L 114 SHEET 4 AB5 6 ILE L 34 GLN L 39 -1 N GLN L 39 O VAL L 93 SHEET 5 AB5 6 TRP L 47 ILE L 51 -1 O ILE L 51 N ILE L 34 SHEET 6 AB5 6 THR L 58 TYR L 60 -1 O ASN L 59 N GLU L 50 SHEET 1 AB6 3 VAL I 19 THR I 22 0 SHEET 2 AB6 3 THR I 72 ILE I 75 -1 O LEU I 73 N ILE I 21 SHEET 3 AB6 3 THR I 63 SER I 65 -1 N THR I 63 O THR I 74 SHEET 1 AB7 4 LYS I 45 LEU I 46 0 SHEET 2 AB7 4 VAL I 33 GLN I 38 -1 N GLN I 37 O LYS I 45 SHEET 3 AB7 4 LEU I 85 GLN I 90 -1 O GLN I 89 N ALA I 34 SHEET 4 AB7 4 THR I 102 LYS I 103 -1 O THR I 102 N TYR I 86 SHEET 1 AB8 2 ILE I 48 TYR I 49 0 SHEET 2 AB8 2 THR I 53 ARG I 54 -1 O THR I 53 N TYR I 49 SHEET 1 AB9 4 GLN H 3 GLN H 6 0 SHEET 2 AB9 4 ALA H 17 THR H 25 -1 O LYS H 23 N GLN H 5 SHEET 3 AB9 4 THR H 78 SER H 84 -1 O MET H 81 N ILE H 20 SHEET 4 AB9 4 ALA H 68 PHE H 70 -1 N THR H 69 O GLN H 82 SHEET 1 AC1 6 GLU H 10 LEU H 11 0 SHEET 2 AC1 6 THR H 112 THR H 115 1 O THR H 113 N GLU H 10 SHEET 3 AC1 6 ALA H 92 TYR H 95 -1 N TYR H 94 O THR H 112 SHEET 4 AC1 6 ILE H 34 GLN H 39 -1 N LEU H 37 O TYR H 95 SHEET 5 AC1 6 LEU H 45 ILE H 51 -1 O GLU H 46 N LYS H 38 SHEET 6 AC1 6 THR H 58 TYR H 60 -1 O ASN H 59 N GLU H 50 SHEET 1 AC2 7 VAL D 37 SER D 47 0 SHEET 2 AC2 7 TYR D 58 GLN D 67 -1 O ASN D 61 N ASN D 46 SHEET 3 AC2 7 ALA D 106 PHE D 108 0 SHEET 4 AC2 7 LYS D 116 ILE D 120 0 SHEET 5 AC2 7 VAL D 126 LEU D 136 -1 O LEU D 127 N ARG D 119 SHEET 6 AC2 7 LEU D 166 TRP D 170 1 O ILE D 167 N VAL D 39 SHEET 7 AC2 7 VAL D 176 VAL D 178 1 O GLN D 177 N ILE D 45 SHEET 1 AC3 6 LEU D 98 PHE D 100 0 SHEET 2 AC3 6 VAL D 149 CYS D 152 0 SHEET 3 AC3 6 GLN D 155 SER D 158 -1 O GLU D 157 N PHE D 99 SHEET 4 AC3 6 PHE D 187 LEU D 189 0 SHEET 5 AC3 6 ASP D 194 TYR D 197 0 SHEET 6 AC3 6 CYS D 209 ARG D 218 -1 O ARG D 213 N ASP D 194 SHEET 1 AC4 2 LYS D 200 TYR D 202 0 SHEET 2 AC4 2 GLY D 205 PHE D 207 -1 O GLY D 205 N TYR D 202 SHEET 1 AC5 8 VAL A 37 ILE A 45 0 SHEET 2 AC5 8 GLY A 49 ALA A 52 0 SHEET 3 AC5 8 ASP A 57 ASN A 69 -1 O ASP A 57 N ALA A 52 SHEET 4 AC5 8 ALA A 106 PHE A 108 0 SHEET 5 AC5 8 LYS A 116 ILE A 120 0 SHEET 6 AC5 8 ASN A 125 LEU A 134 -1 O SER A 129 N LEU A 117 SHEET 7 AC5 8 LEU A 166 TRP A 170 1 O ILE A 167 N VAL A 39 SHEET 8 AC5 8 VAL A 176 VAL A 178 1 O GLN A 177 N ILE A 45 SHEET 1 AC6 5 LEU A 98 PHE A 100 0 SHEET 2 AC6 5 VAL A 149 SER A 158 -1 O GLU A 157 N PHE A 99 SHEET 3 AC6 5 PHE A 187 LEU A 189 0 SHEET 4 AC6 5 LEU A 195 ARG A 196 0 SHEET 5 AC6 5 GLU A 211 ARG A 218 -1 O GLU A 211 N ARG A 196 SHEET 1 AC7 2 LYS A 200 HIS A 201 0 SHEET 2 AC7 2 LYS A 206 PHE A 207 -1 O PHE A 207 N LYS A 200 SHEET 1 AC8 7 VAL B 37 SER B 47 0 SHEET 2 AC8 7 ASP B 57 ASN B 69 -1 O GLN B 67 N SER B 40 SHEET 3 AC8 7 ALA B 106 PHE B 108 0 SHEET 4 AC8 7 LYS B 116 ILE B 120 0 SHEET 5 AC8 7 ASN B 125 ALA B 137 -1 O LEU B 127 N ARG B 119 SHEET 6 AC8 7 LEU B 166 TRP B 170 1 O GLU B 169 N VAL B 39 SHEET 7 AC8 7 VAL B 176 VAL B 178 1 O GLN B 177 N ILE B 45 SHEET 1 AC9 3 LEU B 98 PHE B 100 0 SHEET 2 AC9 3 GLN B 155 SER B 158 -1 O GLU B 157 N PHE B 99 SHEET 3 AC9 3 CYS B 209 GLU B 211 -1 O ILE B 210 N LEU B 156 SHEET 1 AD1 3 VAL B 149 CYS B 152 0 SHEET 2 AD1 3 PHE B 214 ARG B 218 -1 O PHE B 214 N CYS B 152 SHEET 3 AD1 3 PHE B 187 LEU B 189 -1 N ILE B 188 O GLU B 217 SHEET 1 AD2 2 LYS B 200 TYR B 202 0 SHEET 2 AD2 2 GLY B 205 PHE B 207 -1 O PHE B 207 N LYS B 200 SHEET 1 AD3 8 VAL C 37 ALA C 52 0 SHEET 2 AD3 8 ASP C 57 GLN C 67 -1 O GLN C 67 N SER C 40 SHEET 3 AD3 8 ASP C 84 LEU C 85 0 SHEET 4 AD3 8 LYS C 116 ILE C 120 -1 O LEU C 118 N LEU C 85 SHEET 5 AD3 8 VAL C 126 ILE C 132 -1 O LEU C 127 N ARG C 119 SHEET 6 AD3 8 THR C 135 ALA C 137 -1 O LEU C 136 N TYR C 58 SHEET 7 AD3 8 LEU C 166 TRP C 170 1 O ILE C 167 N VAL C 39 SHEET 8 AD3 8 VAL C 176 VAL C 178 1 O GLN C 177 N ILE C 45 SHEET 1 AD4 4 LEU C 98 PHE C 100 0 SHEET 2 AD4 4 VAL C 149 SER C 158 -1 O GLU C 157 N PHE C 99 SHEET 3 AD4 4 CYS C 209 ARG C 218 -1 O ILE C 210 N LEU C 156 SHEET 4 AD4 4 PHE C 187 TYR C 197 -1 N ASP C 194 O ARG C 213 SHEET 1 AD5 2 LYS C 200 TYR C 202 0 SHEET 2 AD5 2 GLY C 205 PHE C 207 -1 O PHE C 207 N LYS C 200 SHEET 1 AD6 5 PHE E 142 ILE E 143 0 SHEET 2 AD6 5 ASP E 148 SER E 160 -1 O LEU E 150 N PHE E 142 SHEET 3 AD6 5 ASP E 78 ASN E 90 -1 N VAL E 81 O ILE E 157 SHEET 4 AD6 5 VAL E 58 GLN E 73 -1 N ASN E 63 O ARG E 86 SHEET 5 AD6 5 LEU E 189 TRP E 193 1 O ARG E 190 N VAL E 60 SHEET 1 AD7 3 LEU E 121 PHE E 123 0 SHEET 2 AD7 3 LEU E 179 SER E 181 -1 O GLU E 180 N PHE E 122 SHEET 3 AD7 3 CYS E 233 VAL E 234 -1 O VAL E 234 N LEU E 179 SHEET 1 AD8 2 THR E 172 CYS E 175 0 SHEET 2 AD8 2 PHE E 238 ARG E 241 -1 O LEU E 240 N GLN E 173 SHEET 1 AD9 2 LYS E 223 TYR E 225 0 SHEET 2 AD9 2 GLY E 229 TYR E 231 -1 O TYR E 231 N LYS E 223 SSBOND 1 CYS J 23 CYS J 88 1555 1555 2.03 SSBOND 2 CYS G 22 CYS G 96 1555 1555 2.03 SSBOND 3 CYS K 23 CYS K 88 1555 1555 2.03 SSBOND 4 CYS F 22 CYS F 96 1555 1555 2.03 SSBOND 5 CYS M 23 CYS M 88 1555 1555 2.03 SSBOND 6 CYS L 22 CYS L 96 1555 1555 2.03 SSBOND 7 CYS I 23 CYS I 88 1555 1555 2.03 SSBOND 8 CYS H 22 CYS H 96 1555 1555 2.03 SSBOND 9 CYS D 138 CYS D 152 1555 1555 2.03 SSBOND 10 CYS D 198 CYS D 209 1555 1555 2.04 SSBOND 11 CYS A 138 CYS A 152 1555 1555 2.03 SSBOND 12 CYS A 198 CYS A 209 1555 1555 2.03 SSBOND 13 CYS B 138 CYS B 152 1555 1555 2.03 SSBOND 14 CYS B 198 CYS B 209 1555 1555 2.03 SSBOND 15 CYS C 138 CYS C 152 1555 1555 2.03 SSBOND 16 CYS C 198 CYS C 209 1555 1555 2.04 SSBOND 17 CYS E 161 CYS E 175 1555 1555 2.04 SSBOND 18 CYS E 221 CYS E 233 1555 1555 2.04 LINK ND2 ASN D 38 C1 NAG T 1 1555 1555 1.44 LINK ND2 ASN A 38 C1 NAG Z 1 1555 1555 1.44 LINK ND2 ASN B 38 C1 NAG f 1 1555 1555 1.44 LINK ND2 ASN C 38 C1 NAG l 1 1555 1555 1.45 LINK ND2 ASN E 220 C1 NAG r 1 1555 1555 1.46 LINK O4 NAG T 1 C1 NAG T 2 1555 1555 1.44 LINK O4 NAG T 2 C1 BMA T 3 1555 1555 1.44 LINK O3 BMA T 3 C1 MAN T 4 1555 1555 1.45 LINK O2 MAN T 4 C1 MAN T 5 1555 1555 1.44 LINK O4 NAG Z 1 C1 NAG Z 2 1555 1555 1.45 LINK O4 NAG Z 2 C1 BMA Z 3 1555 1555 1.45 LINK O3 BMA Z 3 C1 MAN Z 4 1555 1555 1.44 LINK O6 BMA Z 3 C1 MAN Z 5 1555 1555 1.45 LINK O4 NAG f 1 C1 NAG f 2 1555 1555 1.44 LINK O4 NAG f 2 C1 BMA f 3 1555 1555 1.45 LINK O6 BMA f 3 C1 MAN f 4 1555 1555 1.44 LINK O4 NAG l 1 C1 NAG l 2 1555 1555 1.44 LINK O4 NAG l 2 C1 BMA l 3 1555 1555 1.45 LINK O6 BMA l 3 C1 MAN l 4 1555 1555 1.44 LINK O4 NAG r 1 C1 NAG r 2 1555 1555 1.44 LINK O4 NAG r 2 C1 BMA r 3 1555 1555 1.45 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 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