HEADER TRANSPORT PROTEIN 26-APR-25 9R1E TITLE CRYO-EM STRUCTURE OF HUMAN MATE1 IN COMPLEX WITH MPP COMPND MOL_ID: 1; COMPND 2 MOLECULE: MULTIDRUG AND TOXIN EXTRUSION PROTEIN 1; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: MATE-1,HMATE-1,SOLUTE CARRIER FAMILY 47 MEMBER 1; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: HEAVY CHAIN OF FAB; COMPND 8 CHAIN: H; COMPND 9 ENGINEERED: YES; COMPND 10 MOL_ID: 3; COMPND 11 MOLECULE: LIGHT CHAIN OF FAB; COMPND 12 CHAIN: L; COMPND 13 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: SLC47A1, MATE1; SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT; SOURCE 10 ORGANISM_TAXID: 32630; SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 13 MOL_ID: 3; SOURCE 14 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT; SOURCE 15 ORGANISM_TAXID: 32630; SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS SLC47A1, SUBSTRATE, FAB, MULTIDRUG TRANSPORTER, TRANSPORT PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR K.ROMANE,G.PETEANI,S.MUKHERJEE,J.KOWAL,L.ROSSI,J.HOU,A.KOSSIAKOFF, AUTHOR 2 T.LEMMIN,K.P.LOCHER REVDAT 1 05-NOV-25 9R1E 0 JRNL AUTH K.ROMANE,G.PETEANI,S.MUKHERJEE,J.KOWAL,L.ROSSI,J.HOU, JRNL AUTH 2 A.A.KOSSIAKOFF,T.LEMMIN,K.P.LOCHER JRNL TITL STRUCTURAL BASIS OF DRUG RECOGNITION BY HUMAN MATE1 JRNL TITL 2 TRANSPORTER. JRNL REF NAT COMMUN V. 16 9444 2025 JRNL REFN ESSN 2041-1723 JRNL PMID 41145429 JRNL DOI 10.1038/S41467-025-64490-Z REMARK 2 REMARK 2 RESOLUTION. 3.20 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : EPU, CRYOSPARC, COOT, PHENIX, 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) : 3.200 REMARK 3 NUMBER OF PARTICLES : 166048 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 9R1E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-APR-25. REMARK 100 THE DEPOSITION ID IS D_1292147357. 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 : HUMAN MULTIDRUG AND TOXIN REMARK 245 EXTRUSION PROTEIN (MATE1) IN REMARK 245 COMPLEX WITH FAB AND MPP 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 : 7.40 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : 8490 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) : 600.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2400.00 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) : 5100.00 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: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, H, L 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 GLU A 2 REMARK 465 ALA A 3 REMARK 465 PRO A 4 REMARK 465 GLU A 5 REMARK 465 GLU A 6 REMARK 465 PRO A 7 REMARK 465 ALA A 8 REMARK 465 PRO A 9 REMARK 465 VAL A 10 REMARK 465 ARG A 11 REMARK 465 GLY A 12 REMARK 465 GLY A 13 REMARK 465 PRO A 14 REMARK 465 GLU A 15 REMARK 465 ALA A 16 REMARK 465 THR A 17 REMARK 465 LEU A 18 REMARK 465 GLU A 19 REMARK 465 VAL A 20 REMARK 465 ARG A 21 REMARK 465 GLY A 22 REMARK 465 SER A 23 REMARK 465 ARG A 24 REMARK 465 CYS A 25 REMARK 465 LEU A 26 REMARK 465 VAL A 477 REMARK 465 ASN A 478 REMARK 465 ASN A 479 REMARK 465 VAL A 480 REMARK 465 PRO A 481 REMARK 465 ARG A 482 REMARK 465 SER A 483 REMARK 465 GLY A 484 REMARK 465 ASN A 485 REMARK 465 SER A 486 REMARK 465 ALA A 487 REMARK 465 LEU A 488 REMARK 465 PRO A 489 REMARK 465 GLN A 490 REMARK 465 ASP A 491 REMARK 465 PRO A 492 REMARK 465 LEU A 493 REMARK 465 HIS A 494 REMARK 465 PRO A 495 REMARK 465 GLY A 496 REMARK 465 CYS A 497 REMARK 465 PRO A 498 REMARK 465 GLU A 499 REMARK 465 ASN A 500 REMARK 465 LEU A 501 REMARK 465 GLU A 502 REMARK 465 GLY A 503 REMARK 465 ILE A 504 REMARK 465 LEU A 505 REMARK 465 THR A 506 REMARK 465 ASN A 507 REMARK 465 ASP A 508 REMARK 465 VAL A 509 REMARK 465 GLY A 510 REMARK 465 LYS A 511 REMARK 465 THR A 512 REMARK 465 GLY A 513 REMARK 465 GLU A 514 REMARK 465 PRO A 515 REMARK 465 GLN A 516 REMARK 465 SER A 517 REMARK 465 ASP A 518 REMARK 465 GLN A 519 REMARK 465 GLN A 520 REMARK 465 MET A 521 REMARK 465 ARG A 522 REMARK 465 GLN A 523 REMARK 465 GLU A 524 REMARK 465 GLU A 525 REMARK 465 PRO A 526 REMARK 465 LEU A 527 REMARK 465 PRO A 528 REMARK 465 GLU A 529 REMARK 465 HIS A 530 REMARK 465 PRO A 531 REMARK 465 GLN A 532 REMARK 465 ASP A 533 REMARK 465 GLY A 534 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 ARG A 27 CG CD NE CZ NH1 NH2 REMARK 470 LYS H 220 CG CD CE NZ 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 136 C18 CLR A 603 1.43 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 ASN A 136 49.39 -89.28 REMARK 500 GLN A 208 -60.89 -91.37 REMARK 500 ASN A 404 40.20 -104.27 REMARK 500 VAL H 48 -50.76 -121.27 REMARK 500 SER H 53 -3.10 67.64 REMARK 500 TYR H 55 60.79 -104.37 REMARK 500 SER H 57 63.63 64.63 REMARK 500 TYR H 60 153.17 73.57 REMARK 500 ALA H 97 127.96 70.12 REMARK 500 PRO H 158 -159.85 -82.09 REMARK 500 SER H 198 62.11 62.57 REMARK 500 THR H 202 47.00 37.49 REMARK 500 SER L 31 -136.34 59.12 REMARK 500 ALA L 51 -3.15 67.09 REMARK 500 SER L 56 62.92 37.91 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 9R10 RELATED DB: PDB REMARK 900 9R10 CONTAINS THE SAME PROTEIN COMPLEXED WITH CIMETIDINE REMARK 900 RELATED ID: EMD-53506 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF HUMAN MATE1 IN COMPLEX WITH MPP DBREF 9R1E A 1 570 UNP Q96FL8 S47A1_HUMAN 1 570 DBREF 9R1E H 2 225 PDB 9R1E 9R1E 2 225 DBREF 9R1E L 1 211 PDB 9R1E 9R1E 1 211 SEQRES 1 A 570 MET GLU ALA PRO GLU GLU PRO ALA PRO VAL ARG GLY GLY SEQRES 2 A 570 PRO GLU ALA THR LEU GLU VAL ARG GLY SER ARG CYS LEU SEQRES 3 A 570 ARG LEU SER ALA PHE ARG GLU GLU LEU ARG ALA LEU LEU SEQRES 4 A 570 VAL LEU ALA GLY PRO ALA PHE LEU VAL GLN LEU MET VAL SEQRES 5 A 570 PHE LEU ILE SER PHE ILE SER SER VAL PHE CYS GLY HIS SEQRES 6 A 570 LEU GLY LYS LEU GLU LEU ASP ALA VAL THR LEU ALA ILE SEQRES 7 A 570 ALA VAL ILE ASN VAL THR GLY VAL SER VAL GLY PHE GLY SEQRES 8 A 570 LEU SER SER ALA CYS ASP THR LEU ILE SER GLN THR TYR SEQRES 9 A 570 GLY SER GLN ASN LEU LYS HIS VAL GLY VAL ILE LEU GLN SEQRES 10 A 570 ARG SER ALA LEU VAL LEU LEU LEU CYS CYS PHE PRO CYS SEQRES 11 A 570 TRP ALA LEU PHE LEU ASN THR GLN HIS ILE LEU LEU LEU SEQRES 12 A 570 PHE ARG GLN ASP PRO ASP VAL SER ARG LEU THR GLN THR SEQRES 13 A 570 TYR VAL THR ILE PHE ILE PRO ALA LEU PRO ALA THR PHE SEQRES 14 A 570 LEU TYR MET LEU GLN VAL LYS TYR LEU LEU ASN GLN GLY SEQRES 15 A 570 ILE VAL LEU PRO GLN ILE VAL THR GLY VAL ALA ALA ASN SEQRES 16 A 570 LEU VAL ASN ALA LEU ALA ASN TYR LEU PHE LEU HIS GLN SEQRES 17 A 570 LEU HIS LEU GLY VAL ILE GLY SER ALA LEU ALA ASN LEU SEQRES 18 A 570 ILE SER GLN TYR THR LEU ALA LEU LEU LEU PHE LEU TYR SEQRES 19 A 570 ILE LEU GLY LYS LYS LEU HIS GLN ALA THR TRP GLY GLY SEQRES 20 A 570 TRP SER LEU GLU CYS LEU GLN ASP TRP ALA SER PHE LEU SEQRES 21 A 570 ARG LEU ALA ILE PRO SER MET LEU MET LEU CYS MET GLU SEQRES 22 A 570 TRP TRP ALA TYR GLU VAL GLY SER PHE LEU SER GLY ILE SEQRES 23 A 570 LEU GLY MET VAL GLU LEU GLY ALA GLN SER ILE VAL TYR SEQRES 24 A 570 GLU LEU ALA ILE ILE VAL TYR MET VAL PRO ALA GLY PHE SEQRES 25 A 570 SER VAL ALA ALA SER VAL ARG VAL GLY ASN ALA LEU GLY SEQRES 26 A 570 ALA GLY ASP MET GLU GLN ALA ARG LYS SER SER THR VAL SEQRES 27 A 570 SER LEU LEU ILE THR VAL LEU PHE ALA VAL ALA PHE SER SEQRES 28 A 570 VAL LEU LEU LEU SER CYS LYS ASP HIS VAL GLY TYR ILE SEQRES 29 A 570 PHE THR THR ASP ARG ASP ILE ILE ASN LEU VAL ALA GLN SEQRES 30 A 570 VAL VAL PRO ILE TYR ALA VAL SER HIS LEU PHE GLU ALA SEQRES 31 A 570 LEU ALA CYS THR SER GLY GLY VAL LEU ARG GLY SER GLY SEQRES 32 A 570 ASN GLN LYS VAL GLY ALA ILE VAL ASN THR ILE GLY TYR SEQRES 33 A 570 TYR VAL VAL GLY LEU PRO ILE GLY ILE ALA LEU MET PHE SEQRES 34 A 570 ALA THR THR LEU GLY VAL MET GLY LEU TRP SER GLY ILE SEQRES 35 A 570 ILE ILE CYS THR VAL PHE GLN ALA VAL CYS PHE LEU GLY SEQRES 36 A 570 PHE ILE ILE GLN LEU ASN TRP LYS LYS ALA CYS GLN GLN SEQRES 37 A 570 ALA GLN VAL HIS ALA ASN LEU LYS VAL ASN ASN VAL PRO SEQRES 38 A 570 ARG SER GLY ASN SER ALA LEU PRO GLN ASP PRO LEU HIS SEQRES 39 A 570 PRO GLY CYS PRO GLU ASN LEU GLU GLY ILE LEU THR ASN SEQRES 40 A 570 ASP VAL GLY LYS THR GLY GLU PRO GLN SER ASP GLN GLN SEQRES 41 A 570 MET ARG GLN GLU GLU PRO LEU PRO GLU HIS PRO GLN ASP SEQRES 42 A 570 GLY ALA LYS LEU SER ARG LYS GLN LEU VAL LEU ARG ARG SEQRES 43 A 570 GLY LEU LEU LEU LEU GLY VAL PHE LEU ILE LEU LEU VAL SEQRES 44 A 570 GLY ILE LEU VAL ARG PHE TYR VAL ARG ILE GLN SEQRES 1 H 227 VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN PRO SEQRES 2 H 227 GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY PHE SEQRES 3 H 227 ASN PHE SER TYR SER TYR ILE HIS TRP VAL ARG GLN ALA SEQRES 4 H 227 PRO GLY LYS GLY LEU GLU TRP VAL ALA SER ILE SER SER SEQRES 5 H 227 TYR TYR GLY SER THR TYR TYR ALA ASP SER VAL LYS GLY SEQRES 6 H 227 ARG PHE THR ILE SER ALA ASP THR SER LYS ASN THR ALA SEQRES 7 H 227 TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR ALA SEQRES 8 H 227 VAL TYR TYR CYS ALA ARG TRP ALA ASN THR SER SER TYR SEQRES 9 H 227 GLY TRP ARG PHE TRP SER ASN GLY LEU ASP TYR TRP GLY SEQRES 10 H 227 GLN GLY THR LEU VAL THR VAL SER SER ALA SER THR LYS SEQRES 11 H 227 GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER SEQRES 12 H 227 THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS SEQRES 13 H 227 ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER SEQRES 14 H 227 GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL SEQRES 15 H 227 LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL SEQRES 16 H 227 THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE SEQRES 17 H 227 CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP SEQRES 18 H 227 LYS LYS VAL GLU PRO LYS SEQRES 1 L 211 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 L 211 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 L 211 GLN SER VAL SER SER ALA VAL ALA TRP TYR GLN GLN LYS SEQRES 4 L 211 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR SER ALA SER SEQRES 5 L 211 SER LEU TYR SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 L 211 ARG SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 L 211 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN SER SEQRES 8 L 211 TYR TRP TRP PRO LEU THR PHE GLY GLN GLY THR LYS VAL SEQRES 9 L 211 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 L 211 PHE PRO PRO SER ASP SER GLN LEU LYS SER GLY THR ALA SEQRES 11 L 211 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 L 211 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 L 211 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 L 211 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 L 211 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 L 211 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 L 211 PHE ASN ARG HET WRF A 601 13 HET CLR A 602 28 HET CLR A 603 28 HET CLR A 604 28 HET CLR A 605 28 HET CLR A 606 28 HET CLR A 607 28 HET CLR A 608 28 HET CLR A 609 28 HET CLR H 301 28 HETNAM WRF 1-METHYL-4-PHENYLPYRIDIN-1-IUM HETNAM CLR CHOLESTEROL FORMUL 4 WRF C12 H12 N 1+ FORMUL 5 CLR 9(C27 H46 O) FORMUL 14 HOH *5(H2 O) HELIX 1 AA1 ARG A 27 PHE A 62 1 36 HELIX 2 AA2 CYS A 63 LEU A 66 5 4 HELIX 3 AA3 LYS A 68 GLY A 85 1 18 HELIX 4 AA4 GLY A 85 SER A 93 1 9 HELIX 5 AA5 ALA A 95 SER A 106 1 12 HELIX 6 AA6 GLN A 107 LYS A 110 5 4 HELIX 7 AA7 HIS A 111 ASN A 136 1 26 HELIX 8 AA8 ASN A 136 PHE A 144 1 9 HELIX 9 AA9 ASP A 147 PHE A 161 1 15 HELIX 10 AB1 PRO A 163 ASN A 180 1 18 HELIX 11 AB2 VAL A 184 HIS A 207 1 24 HELIX 12 AB3 GLY A 212 LYS A 238 1 27 HELIX 13 AB4 SER A 249 GLN A 254 5 6 HELIX 14 AB5 ASP A 255 GLY A 288 1 34 HELIX 15 AB6 GLY A 288 ALA A 326 1 39 HELIX 16 AB7 ASP A 328 CYS A 357 1 30 HELIX 17 AB8 CYS A 357 THR A 366 1 10 HELIX 18 AB9 ASP A 368 SER A 402 1 35 HELIX 19 AC1 ASN A 404 VAL A 418 1 15 HELIX 20 AC2 GLY A 420 THR A 431 1 12 HELIX 21 AC3 GLY A 434 GLN A 459 1 26 HELIX 22 AC4 ASN A 461 ALA A 473 1 13 HELIX 23 AC5 SER A 538 VAL A 567 1 30 HELIX 24 AC6 ARG H 84 THR H 88 5 5 HELIX 25 AC7 TYR H 102 TRP H 107 1 6 HELIX 26 AC8 SER H 167 ALA H 169 5 3 HELIX 27 AC9 SER H 198 GLN H 203 5 6 HELIX 28 AD1 SER L 121 GLY L 128 1 8 HELIX 29 AD2 LYS L 183 GLU L 187 1 5 SHEET 1 AA1 2 GLN H 3 LEU H 4 0 SHEET 2 AA1 2 ALA H 24 SER H 25 -1 O SER H 25 N GLN H 3 SHEET 1 AA2 5 LEU H 11 VAL H 12 0 SHEET 2 AA2 5 THR H 118 VAL H 122 1 O THR H 121 N VAL H 12 SHEET 3 AA2 5 ALA H 89 ARG H 95 -1 N ALA H 89 O VAL H 120 SHEET 4 AA2 5 ILE H 34 GLN H 39 -1 N VAL H 37 O TYR H 92 SHEET 5 AA2 5 LEU H 45 ILE H 51 -1 O GLU H 46 N ARG H 38 SHEET 1 AA3 3 SER H 17 SER H 21 0 SHEET 2 AA3 3 THR H 78 ASN H 83A-1 O MET H 83 N LEU H 18 SHEET 3 AA3 3 PHE H 68 ASP H 73 -1 N THR H 69 O GLN H 82 SHEET 1 AA4 4 SER H 131 LEU H 135 0 SHEET 2 AA4 4 ALA H 147 TYR H 156 -1 O LEU H 152 N PHE H 133 SHEET 3 AA4 4 TYR H 187 VAL H 195 -1 O VAL H 193 N LEU H 149 SHEET 4 AA4 4 VAL H 174 THR H 176 -1 N HIS H 175 O VAL H 192 SHEET 1 AA5 4 SER H 131 LEU H 135 0 SHEET 2 AA5 4 ALA H 147 TYR H 156 -1 O LEU H 152 N PHE H 133 SHEET 3 AA5 4 TYR H 187 VAL H 195 -1 O VAL H 193 N LEU H 149 SHEET 4 AA5 4 VAL H 180 LEU H 181 -1 N VAL H 180 O SER H 188 SHEET 1 AA6 3 THR H 162 TRP H 165 0 SHEET 2 AA6 3 TYR H 205 ASN H 210 -1 O ASN H 208 N SER H 164 SHEET 3 AA6 3 ASP H 219 VAL H 222 -1 O VAL H 222 N TYR H 205 SHEET 1 AA7 4 THR L 5 GLN L 6 0 SHEET 2 AA7 4 VAL L 19 ARG L 24 -1 O ARG L 24 N THR L 5 SHEET 3 AA7 4 ASP L 70 ILE L 75 -1 O ILE L 75 N VAL L 19 SHEET 4 AA7 4 PHE L 62 ARG L 66 -1 N SER L 63 O THR L 74 SHEET 1 AA8 6 SER L 10 ALA L 13 0 SHEET 2 AA8 6 THR L 102 ILE L 106 1 O GLU L 105 N LEU L 11 SHEET 3 AA8 6 THR L 85 TYR L 87 -1 N TYR L 86 O THR L 102 SHEET 4 AA8 6 TRP L 35 GLN L 38 -1 N GLN L 38 O THR L 85 SHEET 5 AA8 6 LYS L 45 TYR L 49 -1 O LEU L 47 N TRP L 35 SHEET 6 AA8 6 SER L 53 LEU L 54 -1 O SER L 53 N TYR L 49 SHEET 1 AA9 4 SER L 114 PHE L 118 0 SHEET 2 AA9 4 THR L 129 PHE L 139 -1 O VAL L 133 N PHE L 118 SHEET 3 AA9 4 TYR L 173 SER L 182 -1 O LEU L 175 N LEU L 136 SHEET 4 AA9 4 SER L 159 VAL L 163 -1 N SER L 162 O SER L 176 SHEET 1 AB1 4 ALA L 153 LEU L 154 0 SHEET 2 AB1 4 LYS L 145 VAL L 150 -1 N VAL L 150 O ALA L 153 SHEET 3 AB1 4 VAL L 191 THR L 197 -1 O GLU L 195 N GLN L 147 SHEET 4 AB1 4 VAL L 205 ASN L 210 -1 O LYS L 207 N CYS L 194 SSBOND 1 CYS H 22 CYS H 93 1555 1555 2.03 SSBOND 2 CYS H 151 CYS H 207 1555 1555 2.03 SSBOND 3 CYS L 23 CYS L 88 1555 1555 2.03 SSBOND 4 CYS L 134 CYS L 194 1555 1555 2.03 LINK C21 CLR A 605 C21 CLR A 607 1555 1555 1.49 CISPEP 1 PHE H 157 PRO H 158 0 3.47 CISPEP 2 TRP L 94 PRO L 95 0 1.18 CISPEP 3 TYR L 140 PRO L 141 0 -0.18 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