HEADER TRANSPORT PROTEIN 12-JUL-24 9G3E TITLE CRYO-EM STRUCTURE OF SBMA IN THE INWARD-FACING-WIDE CONFORMATION BOUND TITLE 2 TO 2 SYBODIES COMPND MOL_ID: 1; COMPND 2 MOLECULE: PEPTIDE ANTIBIOTIC TRANSPORTER SBMA; COMPND 3 CHAIN: A, B; COMPND 4 ENGINEERED: YES; COMPND 5 OTHER_DETAILS: PROTOMER A AND B; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: SYBODY 2; COMPND 8 CHAIN: C, D; COMPND 9 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI; SOURCE 3 ORGANISM_TAXID: 562; SOURCE 4 GENE: SBMA, B0377, JW0368; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI MC1061; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 1211845; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT; SOURCE 9 ORGANISM_TAXID: 32630; SOURCE 10 EXPRESSION_SYSTEM: ESCHERICHIA COLI MC1061; SOURCE 11 EXPRESSION_SYSTEM_TAXID: 1211845 KEYWDS PEPTIDE ANTIBIOTIC TRANSPORTER SBMA, PEPTIDE UPTAKE PERMEASE (PUP) KEYWDS 2 FAMILY, TRANSMEMBRANE PROTEIN, TRANSPORT PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR C.THANGARATNARAJAH,T.W.ETTEMA,D.J.SLOTBOOM REVDAT 1 23-JUL-25 9G3E 0 JRNL AUTH C.THANGARATNARAJAH,T.W.ETTEMA,D.J.SLOTBOOM JRNL TITL CRYO-EM STRUCTURE OF THE SBMA IN THE INWARD-FACING CLOSED JRNL TITL 2 CONFORMATION BOUND TO 2 SYBODIES JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.14 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : CRYOLO, SERIALEM, CTFFIND, COOT, REMARK 3 CRYOSPARC, CRYOSPARC, CRYOSPARC, PHENIX REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : NULL REMARK 3 REFINEMENT SPACE : REAL 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) : 3.140 REMARK 3 NUMBER OF PARTICLES : 114603 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 9G3E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-JUL-24. REMARK 100 THE DEPOSITION ID IS D_1292140107. 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 : PEPTIDE ANTIBIOTIC TRANSPORTER REMARK 245 SBMA IN COMPLEX WITH SYBODY 2 REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 6.29 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 : 1585 REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : FEI TALOS ARCTICA REMARK 245 DETECTOR TYPE : GATAN K2 SUMMIT (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 800.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 1800.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : 2.70 REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 5010.00 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : 130000 REMARK 245 CALIBRATED MAGNIFICATION : 48924 REMARK 245 SOURCE : FIELD EMISSION GUN REMARK 245 ACCELERATION VOLTAGE (KV) : 200 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: TETRAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D 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 0 REMARK 465 SER A 1 REMARK 465 GLY A 395 REMARK 465 ASP A 396 REMARK 465 LYS A 397 REMARK 465 ILE A 398 REMARK 465 GLN A 399 REMARK 465 GLU A 400 REMARK 465 VAL A 401 REMARK 465 THR A 402 REMARK 465 HIS A 403 REMARK 465 THR A 404 REMARK 465 LEU A 405 REMARK 465 SER A 406 REMARK 465 ALA A 407 REMARK 465 LEU A 408 REMARK 465 GLU A 409 REMARK 465 VAL A 410 REMARK 465 LEU A 411 REMARK 465 PHE A 412 REMARK 465 GLN A 413 REMARK 465 GLY A 414 REMARK 465 PRO A 415 REMARK 465 HIS A 416 REMARK 465 HIS A 417 REMARK 465 HIS A 418 REMARK 465 HIS A 419 REMARK 465 HIS A 420 REMARK 465 HIS A 421 REMARK 465 HIS A 422 REMARK 465 HIS A 423 REMARK 465 HIS A 424 REMARK 465 HIS A 425 REMARK 465 MET B 0 REMARK 465 SER B 1 REMARK 465 GLY B 395 REMARK 465 ASP B 396 REMARK 465 LYS B 397 REMARK 465 ILE B 398 REMARK 465 GLN B 399 REMARK 465 GLU B 400 REMARK 465 VAL B 401 REMARK 465 THR B 402 REMARK 465 HIS B 403 REMARK 465 THR B 404 REMARK 465 LEU B 405 REMARK 465 SER B 406 REMARK 465 ALA B 407 REMARK 465 LEU B 408 REMARK 465 GLU B 409 REMARK 465 VAL B 410 REMARK 465 LEU B 411 REMARK 465 PHE B 412 REMARK 465 GLN B 413 REMARK 465 GLY B 414 REMARK 465 PRO B 415 REMARK 465 HIS B 416 REMARK 465 HIS B 417 REMARK 465 HIS B 418 REMARK 465 HIS B 419 REMARK 465 HIS B 420 REMARK 465 HIS B 421 REMARK 465 HIS B 422 REMARK 465 HIS B 423 REMARK 465 HIS B 424 REMARK 465 HIS B 425 REMARK 465 MET C 1 REMARK 465 ALA C 2 REMARK 465 GLY C 3 REMARK 465 SER C 4 REMARK 465 SER C 5 REMARK 465 SER C 6 REMARK 465 GLN C 7 REMARK 465 GLY C 122 REMARK 465 ARG C 123 REMARK 465 ALA C 124 REMARK 465 GLY C 125 REMARK 465 GLU C 126 REMARK 465 GLN C 127 REMARK 465 ARG C 128 REMARK 465 LEU C 129 REMARK 465 ILE C 130 REMARK 465 SER C 131 REMARK 465 GLU C 132 REMARK 465 GLU C 133 REMARK 465 ASP C 134 REMARK 465 LEU C 135 REMARK 465 ASN C 136 REMARK 465 SER C 137 REMARK 465 ALA C 138 REMARK 465 VAL C 139 REMARK 465 ASP C 140 REMARK 465 HIS C 141 REMARK 465 HIS C 142 REMARK 465 HIS C 143 REMARK 465 HIS C 144 REMARK 465 HIS C 145 REMARK 465 HIS C 146 REMARK 465 MET D 1 REMARK 465 ALA D 2 REMARK 465 GLY D 3 REMARK 465 SER D 4 REMARK 465 SER D 5 REMARK 465 SER D 6 REMARK 465 GLY D 122 REMARK 465 ARG D 123 REMARK 465 ALA D 124 REMARK 465 GLY D 125 REMARK 465 GLU D 126 REMARK 465 GLN D 127 REMARK 465 ARG D 128 REMARK 465 LEU D 129 REMARK 465 ILE D 130 REMARK 465 SER D 131 REMARK 465 GLU D 132 REMARK 465 GLU D 133 REMARK 465 ASP D 134 REMARK 465 LEU D 135 REMARK 465 ASN D 136 REMARK 465 SER D 137 REMARK 465 ALA D 138 REMARK 465 VAL D 139 REMARK 465 ASP D 140 REMARK 465 HIS D 141 REMARK 465 HIS D 142 REMARK 465 HIS D 143 REMARK 465 HIS D 144 REMARK 465 HIS D 145 REMARK 465 HIS D 146 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 PRO A 7 -170.91 -67.12 REMARK 500 SER A 48 -168.85 -78.48 REMARK 500 TRP A 83 34.03 -99.74 REMARK 500 ASP A 288 49.49 -93.20 REMARK 500 PHE B 5 -60.26 -91.06 REMARK 500 PRO B 7 -169.75 -69.99 REMARK 500 TRP B 27 -60.40 -91.06 REMARK 500 TRP B 83 31.12 -94.49 REMARK 500 ILE B 235 -63.49 66.54 REMARK 500 TYR B 241 73.94 -102.83 REMARK 500 ASP B 288 32.25 -96.38 REMARK 500 ASP B 289 -157.64 57.19 REMARK 500 ASP C 58 -169.87 -79.85 REMARK 500 ALA D 20 149.10 67.54 REMARK 500 ASN D 80 155.92 -48.12 REMARK 500 ALA D 81 -1.18 81.52 REMARK 500 REMARK 500 REMARK: NULL REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 PGT A 501 REMARK 610 PGT B 501 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-50996 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF SBMA IN THE INWARD-FACING-WIDE CONFORMATION REMARK 900 BOUND TO 2 SYBODIES REMARK 900 RELATED ID: 9G3D RELATED DB: PDB REMARK 900 RELATED ID: 9G3F RELATED DB: PDB REMARK 900 RELATED ID: 9G3G RELATED DB: PDB REMARK 900 RELATED ID: EMD-50994 RELATED DB: EMDB REMARK 900 RELATED ID: EMD-50998 RELATED DB: EMDB REMARK 900 RELATED ID: EMD-50997 RELATED DB: EMDB DBREF 9G3E A 2 406 UNP P0AFY6 SBMA_ECOLI 2 406 DBREF 9G3E B 2 406 UNP P0AFY6 SBMA_ECOLI 2 406 DBREF 9G3E C 1 146 PDB 9G3E 9G3E 1 146 DBREF 9G3E D 1 146 PDB 9G3E 9G3E 1 146 SEQADV 9G3E MET A 0 UNP P0AFY6 INITIATING METHIONINE SEQADV 9G3E SER A 1 UNP P0AFY6 EXPRESSION TAG SEQADV 9G3E ALA A 407 UNP P0AFY6 EXPRESSION TAG SEQADV 9G3E LEU A 408 UNP P0AFY6 EXPRESSION TAG SEQADV 9G3E GLU A 409 UNP P0AFY6 EXPRESSION TAG SEQADV 9G3E VAL A 410 UNP P0AFY6 EXPRESSION TAG SEQADV 9G3E LEU A 411 UNP P0AFY6 EXPRESSION TAG SEQADV 9G3E PHE A 412 UNP P0AFY6 EXPRESSION TAG SEQADV 9G3E GLN A 413 UNP P0AFY6 EXPRESSION TAG SEQADV 9G3E GLY A 414 UNP P0AFY6 EXPRESSION TAG SEQADV 9G3E PRO A 415 UNP P0AFY6 EXPRESSION TAG SEQADV 9G3E HIS A 416 UNP P0AFY6 EXPRESSION TAG SEQADV 9G3E HIS A 417 UNP P0AFY6 EXPRESSION TAG SEQADV 9G3E HIS A 418 UNP P0AFY6 EXPRESSION TAG SEQADV 9G3E HIS A 419 UNP P0AFY6 EXPRESSION TAG SEQADV 9G3E HIS A 420 UNP P0AFY6 EXPRESSION TAG SEQADV 9G3E HIS A 421 UNP P0AFY6 EXPRESSION TAG SEQADV 9G3E HIS A 422 UNP P0AFY6 EXPRESSION TAG SEQADV 9G3E HIS A 423 UNP P0AFY6 EXPRESSION TAG SEQADV 9G3E HIS A 424 UNP P0AFY6 EXPRESSION TAG SEQADV 9G3E HIS A 425 UNP P0AFY6 EXPRESSION TAG SEQADV 9G3E MET B 0 UNP P0AFY6 INITIATING METHIONINE SEQADV 9G3E SER B 1 UNP P0AFY6 EXPRESSION TAG SEQADV 9G3E ALA B 407 UNP P0AFY6 EXPRESSION TAG SEQADV 9G3E LEU B 408 UNP P0AFY6 EXPRESSION TAG SEQADV 9G3E GLU B 409 UNP P0AFY6 EXPRESSION TAG SEQADV 9G3E VAL B 410 UNP P0AFY6 EXPRESSION TAG SEQADV 9G3E LEU B 411 UNP P0AFY6 EXPRESSION TAG SEQADV 9G3E PHE B 412 UNP P0AFY6 EXPRESSION TAG SEQADV 9G3E GLN B 413 UNP P0AFY6 EXPRESSION TAG SEQADV 9G3E GLY B 414 UNP P0AFY6 EXPRESSION TAG SEQADV 9G3E PRO B 415 UNP P0AFY6 EXPRESSION TAG SEQADV 9G3E HIS B 416 UNP P0AFY6 EXPRESSION TAG SEQADV 9G3E HIS B 417 UNP P0AFY6 EXPRESSION TAG SEQADV 9G3E HIS B 418 UNP P0AFY6 EXPRESSION TAG SEQADV 9G3E HIS B 419 UNP P0AFY6 EXPRESSION TAG SEQADV 9G3E HIS B 420 UNP P0AFY6 EXPRESSION TAG SEQADV 9G3E HIS B 421 UNP P0AFY6 EXPRESSION TAG SEQADV 9G3E HIS B 422 UNP P0AFY6 EXPRESSION TAG SEQADV 9G3E HIS B 423 UNP P0AFY6 EXPRESSION TAG SEQADV 9G3E HIS B 424 UNP P0AFY6 EXPRESSION TAG SEQADV 9G3E HIS B 425 UNP P0AFY6 EXPRESSION TAG SEQRES 1 A 426 MET SER PHE LYS SER PHE PHE PRO LYS PRO GLY THR PHE SEQRES 2 A 426 PHE LEU SER ALA PHE VAL TRP ALA LEU ILE ALA VAL ILE SEQRES 3 A 426 PHE TRP GLN ALA GLY GLY GLY ASP TRP VAL ALA ARG ILE SEQRES 4 A 426 THR GLY ALA SER GLY GLN ILE PRO ILE SER ALA ALA ARG SEQRES 5 A 426 PHE TRP SER LEU ASP PHE LEU ILE PHE TYR ALA TYR TYR SEQRES 6 A 426 ILE VAL CYS VAL GLY LEU PHE ALA LEU PHE TRP PHE ILE SEQRES 7 A 426 TYR SER PRO HIS ARG TRP GLN TYR TRP SER ILE LEU GLY SEQRES 8 A 426 THR ALA LEU ILE ILE PHE VAL THR TRP PHE LEU VAL GLU SEQRES 9 A 426 VAL GLY VAL ALA VAL ASN ALA TRP TYR ALA PRO PHE TYR SEQRES 10 A 426 ASP LEU ILE GLN THR ALA LEU SER SER PRO HIS LYS VAL SEQRES 11 A 426 THR ILE GLU GLN PHE TYR ARG GLU VAL GLY VAL PHE LEU SEQRES 12 A 426 GLY ILE ALA LEU ILE ALA VAL VAL ILE SER VAL LEU ASN SEQRES 13 A 426 ASN PHE PHE VAL SER HIS TYR VAL PHE ARG TRP ARG THR SEQRES 14 A 426 ALA MET ASN GLU TYR TYR MET ALA ASN TRP GLN GLN LEU SEQRES 15 A 426 ARG HIS ILE GLU GLY ALA ALA GLN ARG VAL GLN GLU ASP SEQRES 16 A 426 THR MET ARG PHE ALA SER THR LEU GLU ASN MET GLY VAL SEQRES 17 A 426 SER PHE ILE ASN ALA ILE MET THR LEU ILE ALA PHE LEU SEQRES 18 A 426 PRO VAL LEU VAL THR LEU SER ALA HIS VAL PRO GLU LEU SEQRES 19 A 426 PRO ILE ILE GLY HIS ILE PRO TYR GLY LEU VAL ILE ALA SEQRES 20 A 426 ALA ILE VAL TRP SER LEU MET GLY THR GLY LEU LEU ALA SEQRES 21 A 426 VAL VAL GLY ILE LYS LEU PRO GLY LEU GLU PHE LYS ASN SEQRES 22 A 426 GLN ARG VAL GLU ALA ALA TYR ARG LYS GLU LEU VAL TYR SEQRES 23 A 426 GLY GLU ASP ASP ALA THR ARG ALA THR PRO PRO THR VAL SEQRES 24 A 426 ARG GLU LEU PHE SER ALA VAL ARG LYS ASN TYR PHE ARG SEQRES 25 A 426 LEU TYR PHE HIS TYR MET TYR PHE ASN ILE ALA ARG ILE SEQRES 26 A 426 LEU TYR LEU GLN VAL ASP ASN VAL PHE GLY LEU PHE LEU SEQRES 27 A 426 LEU PHE PRO SER ILE VAL ALA GLY THR ILE THR LEU GLY SEQRES 28 A 426 LEU MET THR GLN ILE THR ASN VAL PHE GLY GLN VAL ARG SEQRES 29 A 426 GLY ALA PHE GLN TYR LEU ILE ASN SER TRP THR THR LEU SEQRES 30 A 426 VAL GLU LEU MET SER ILE TYR LYS ARG LEU ARG SER PHE SEQRES 31 A 426 GLU HIS GLU LEU ASP GLY ASP LYS ILE GLN GLU VAL THR SEQRES 32 A 426 HIS THR LEU SER ALA LEU GLU VAL LEU PHE GLN GLY PRO SEQRES 33 A 426 HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS SEQRES 1 B 426 MET SER PHE LYS SER PHE PHE PRO LYS PRO GLY THR PHE SEQRES 2 B 426 PHE LEU SER ALA PHE VAL TRP ALA LEU ILE ALA VAL ILE SEQRES 3 B 426 PHE TRP GLN ALA GLY GLY GLY ASP TRP VAL ALA ARG ILE SEQRES 4 B 426 THR GLY ALA SER GLY GLN ILE PRO ILE SER ALA ALA ARG SEQRES 5 B 426 PHE TRP SER LEU ASP PHE LEU ILE PHE TYR ALA TYR TYR SEQRES 6 B 426 ILE VAL CYS VAL GLY LEU PHE ALA LEU PHE TRP PHE ILE SEQRES 7 B 426 TYR SER PRO HIS ARG TRP GLN TYR TRP SER ILE LEU GLY SEQRES 8 B 426 THR ALA LEU ILE ILE PHE VAL THR TRP PHE LEU VAL GLU SEQRES 9 B 426 VAL GLY VAL ALA VAL ASN ALA TRP TYR ALA PRO PHE TYR SEQRES 10 B 426 ASP LEU ILE GLN THR ALA LEU SER SER PRO HIS LYS VAL SEQRES 11 B 426 THR ILE GLU GLN PHE TYR ARG GLU VAL GLY VAL PHE LEU SEQRES 12 B 426 GLY ILE ALA LEU ILE ALA VAL VAL ILE SER VAL LEU ASN SEQRES 13 B 426 ASN PHE PHE VAL SER HIS TYR VAL PHE ARG TRP ARG THR SEQRES 14 B 426 ALA MET ASN GLU TYR TYR MET ALA ASN TRP GLN GLN LEU SEQRES 15 B 426 ARG HIS ILE GLU GLY ALA ALA GLN ARG VAL GLN GLU ASP SEQRES 16 B 426 THR MET ARG PHE ALA SER THR LEU GLU ASN MET GLY VAL SEQRES 17 B 426 SER PHE ILE ASN ALA ILE MET THR LEU ILE ALA PHE LEU SEQRES 18 B 426 PRO VAL LEU VAL THR LEU SER ALA HIS VAL PRO GLU LEU SEQRES 19 B 426 PRO ILE ILE GLY HIS ILE PRO TYR GLY LEU VAL ILE ALA SEQRES 20 B 426 ALA ILE VAL TRP SER LEU MET GLY THR GLY LEU LEU ALA SEQRES 21 B 426 VAL VAL GLY ILE LYS LEU PRO GLY LEU GLU PHE LYS ASN SEQRES 22 B 426 GLN ARG VAL GLU ALA ALA TYR ARG LYS GLU LEU VAL TYR SEQRES 23 B 426 GLY GLU ASP ASP ALA THR ARG ALA THR PRO PRO THR VAL SEQRES 24 B 426 ARG GLU LEU PHE SER ALA VAL ARG LYS ASN TYR PHE ARG SEQRES 25 B 426 LEU TYR PHE HIS TYR MET TYR PHE ASN ILE ALA ARG ILE SEQRES 26 B 426 LEU TYR LEU GLN VAL ASP ASN VAL PHE GLY LEU PHE LEU SEQRES 27 B 426 LEU PHE PRO SER ILE VAL ALA GLY THR ILE THR LEU GLY SEQRES 28 B 426 LEU MET THR GLN ILE THR ASN VAL PHE GLY GLN VAL ARG SEQRES 29 B 426 GLY ALA PHE GLN TYR LEU ILE ASN SER TRP THR THR LEU SEQRES 30 B 426 VAL GLU LEU MET SER ILE TYR LYS ARG LEU ARG SER PHE SEQRES 31 B 426 GLU HIS GLU LEU ASP GLY ASP LYS ILE GLN GLU VAL THR SEQRES 32 B 426 HIS THR LEU SER ALA LEU GLU VAL LEU PHE GLN GLY PRO SEQRES 33 B 426 HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS SEQRES 1 C 146 MET ALA GLY SER SER SER GLN VAL GLN LEU VAL GLU SER SEQRES 2 C 146 GLY GLY GLY LEU VAL GLN ALA GLY GLY SER LEU ARG LEU SEQRES 3 C 146 SER CYS ALA ALA SER GLY PHE PRO VAL ILE ALA ASN VAL SEQRES 4 C 146 MET TYR TRP TYR ARG GLN ALA PRO GLY LYS GLU ARG GLU SEQRES 5 C 146 TRP VAL ALA ALA ILE ASP SER SER GLY GLU TYR ALA TYR SEQRES 6 C 146 TYR ALA ASP SER VAL LYS GLY ARG PHE THR ILE SER ARG SEQRES 7 C 146 ASP ASN ALA LYS ASN THR VAL TYR LEU GLN MET ASN SER SEQRES 8 C 146 LEU LYS PRO GLU ASP THR ALA VAL TYR TYR CYS TYR VAL SEQRES 9 C 146 LYS VAL GLY SER HIS TYR TRP GLY GLN GLY THR GLN VAL SEQRES 10 C 146 THR VAL SER ALA GLY ARG ALA GLY GLU GLN ARG LEU ILE SEQRES 11 C 146 SER GLU GLU ASP LEU ASN SER ALA VAL ASP HIS HIS HIS SEQRES 12 C 146 HIS HIS HIS SEQRES 1 D 146 MET ALA GLY SER SER SER GLN VAL GLN LEU VAL GLU SER SEQRES 2 D 146 GLY GLY GLY LEU VAL GLN ALA GLY GLY SER LEU ARG LEU SEQRES 3 D 146 SER CYS ALA ALA SER GLY PHE PRO VAL ILE ALA ASN VAL SEQRES 4 D 146 MET TYR TRP TYR ARG GLN ALA PRO GLY LYS GLU ARG GLU SEQRES 5 D 146 TRP VAL ALA ALA ILE ASP SER SER GLY GLU TYR ALA TYR SEQRES 6 D 146 TYR ALA ASP SER VAL LYS GLY ARG PHE THR ILE SER ARG SEQRES 7 D 146 ASP ASN ALA LYS ASN THR VAL TYR LEU GLN MET ASN SER SEQRES 8 D 146 LEU LYS PRO GLU ASP THR ALA VAL TYR TYR CYS TYR VAL SEQRES 9 D 146 LYS VAL GLY SER HIS TYR TRP GLY GLN GLY THR GLN VAL SEQRES 10 D 146 THR VAL SER ALA GLY ARG ALA GLY GLU GLN ARG LEU ILE SEQRES 11 D 146 SER GLU GLU ASP LEU ASN SER ALA VAL ASP HIS HIS HIS SEQRES 12 D 146 HIS HIS HIS HET PGT A 501 45 HET PGT B 501 45 HETNAM PGT (1S)-2-{[{[(2R)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY) HETNAM 2 PGT PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL STEARATE HETSYN PGT PHOSPHATIDYLGLYCEROL; 1-PALMITOYL-2-OLEOYL-SN-GLYCERO- HETSYN 2 PGT 3-[PHOSPHO-RAC-(1-GLYCEROL)](SODIUM SALT) FORMUL 5 PGT 2(C40 H79 O10 P) HELIX 1 AA1 LYS A 8 ALA A 29 1 22 HELIX 2 AA2 GLY A 30 GLY A 40 1 11 HELIX 3 AA3 SER A 48 TRP A 53 5 6 HELIX 4 AA4 SER A 54 SER A 79 1 26 HELIX 5 AA5 TRP A 83 ILE A 88 1 6 HELIX 6 AA6 ILE A 88 SER A 125 1 38 HELIX 7 AA7 THR A 130 ASN A 177 1 48 HELIX 8 AA8 ASN A 177 ARG A 182 1 6 HELIX 9 AA9 GLY A 186 SER A 227 1 42 HELIX 10 AB1 ALA A 228 VAL A 230 5 3 HELIX 11 AB2 TYR A 241 VAL A 261 1 21 HELIX 12 AB3 LYS A 264 GLY A 286 1 23 HELIX 13 AB4 THR A 294 LEU A 337 1 44 HELIX 14 AB5 LEU A 338 GLY A 345 1 8 HELIX 15 AB6 THR A 348 ASP A 394 1 47 HELIX 16 AB7 LYS B 8 ALA B 29 1 22 HELIX 17 AB8 GLY B 30 GLY B 40 1 11 HELIX 18 AB9 SER B 48 TRP B 53 5 6 HELIX 19 AC1 SER B 54 SER B 79 1 26 HELIX 20 AC2 TRP B 83 SER B 125 1 43 HELIX 21 AC3 THR B 130 ASN B 177 1 48 HELIX 22 AC4 ASN B 177 ARG B 182 1 6 HELIX 23 AC5 GLY B 186 SER B 227 1 42 HELIX 24 AC6 ALA B 228 VAL B 230 5 3 HELIX 25 AC7 TYR B 241 ILE B 263 1 23 HELIX 26 AC8 ILE B 263 VAL B 284 1 22 HELIX 27 AC9 ASP B 288 ARG B 292 5 5 HELIX 28 AD1 THR B 294 LEU B 337 1 44 HELIX 29 AD2 LEU B 338 GLY B 345 1 8 HELIX 30 AD3 THR B 348 ASP B 394 1 47 HELIX 31 AD4 LYS D 93 THR D 97 5 5 SHEET 1 AA1 4 VAL C 11 GLY C 14 0 SHEET 2 AA1 4 SER C 23 ALA C 29 -1 O ALA C 29 N VAL C 11 SHEET 3 AA1 4 THR C 84 ASN C 90 -1 O MET C 89 N LEU C 24 SHEET 4 AA1 4 PHE C 74 ASP C 79 -1 N THR C 75 O GLN C 88 SHEET 1 AA2 6 LEU C 17 GLN C 19 0 SHEET 2 AA2 6 THR C 115 SER C 120 1 O SER C 120 N VAL C 18 SHEET 3 AA2 6 ALA C 98 LYS C 105 -1 N TYR C 100 O THR C 115 SHEET 4 AA2 6 MET C 40 GLN C 45 -1 N GLN C 45 O VAL C 99 SHEET 5 AA2 6 ARG C 51 ILE C 57 -1 O GLU C 52 N ARG C 44 SHEET 6 AA2 6 ALA C 64 TYR C 66 -1 O TYR C 65 N ALA C 56 SHEET 1 AA3 4 LEU C 17 GLN C 19 0 SHEET 2 AA3 4 THR C 115 SER C 120 1 O SER C 120 N VAL C 18 SHEET 3 AA3 4 ALA C 98 LYS C 105 -1 N TYR C 100 O THR C 115 SHEET 4 AA3 4 HIS C 109 TRP C 111 -1 O TYR C 110 N VAL C 104 SHEET 1 AA4 4 VAL D 11 GLY D 14 0 SHEET 2 AA4 4 LEU D 24 ALA D 29 -1 O SER D 27 N SER D 13 SHEET 3 AA4 4 THR D 84 MET D 89 -1 O MET D 89 N LEU D 24 SHEET 4 AA4 4 PHE D 74 ARG D 78 -1 N THR D 75 O GLN D 88 SHEET 1 AA5 6 LEU D 17 VAL D 18 0 SHEET 2 AA5 6 THR D 115 VAL D 119 1 O THR D 118 N VAL D 18 SHEET 3 AA5 6 ALA D 98 LYS D 105 -1 N ALA D 98 O VAL D 117 SHEET 4 AA5 6 MET D 40 GLN D 45 -1 N GLN D 45 O VAL D 99 SHEET 5 AA5 6 ARG D 51 ILE D 57 -1 O GLU D 52 N ARG D 44 SHEET 6 AA5 6 ALA D 64 TYR D 66 -1 O TYR D 65 N ALA D 56 SHEET 1 AA6 4 LEU D 17 VAL D 18 0 SHEET 2 AA6 4 THR D 115 VAL D 119 1 O THR D 118 N VAL D 18 SHEET 3 AA6 4 ALA D 98 LYS D 105 -1 N ALA D 98 O VAL D 117 SHEET 4 AA6 4 HIS D 109 TRP D 111 -1 O TYR D 110 N VAL D 104 SSBOND 1 CYS C 28 CYS C 102 1555 1555 2.03 SSBOND 2 CYS D 28 CYS D 102 1555 1555 2.03 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