HEADER TRANSPORT PROTEIN 14-JUN-23 8T60 TITLE CRYOEM STRUCTURE OF AN INWARD-FACING MELBST AT A NA(+)-BOUND AND SUGAR TITLE 2 LOW-AFFINITY CONFORMATION COMPND MOL_ID: 1; COMPND 2 MOLECULE: MELIBIOSE PERMEASE; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: MELIBIOSE CARRIER,MELIBIOSE TRANSPORTER,MELIBIOSE/CATION COMPND 5 SYMPORTER,NA+ (LI+)/MELIBIOSE SYMPORTER,THIOMETHYLGALACTOSIDE COMPND 6 PERMEASE II; COMPND 7 ENGINEERED: YES; COMPND 8 MOL_ID: 2; COMPND 9 MOLECULE: NB725_4; COMPND 10 CHAIN: B; COMPND 11 ENGINEERED: YES; COMPND 12 MOL_ID: 3; COMPND 13 MOLECULE: NABFAB_H CHAIN; COMPND 14 CHAIN: H; COMPND 15 ENGINEERED: YES; COMPND 16 MOL_ID: 4; COMPND 17 MOLECULE: NABFAB_L CHAIN; COMPND 18 CHAIN: L; COMPND 19 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SALMONELLA ENTERICA SUBSP. ENTERICA SEROVAR SOURCE 3 TYPHIMURIUM; SOURCE 4 ORGANISM_TAXID: 90371; SOURCE 5 STRAIN: LT2; SOURCE 6 GENE: MELB, STM4299; SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT; SOURCE 11 ORGANISM_TAXID: 32630; SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 13 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 14 MOL_ID: 3; SOURCE 15 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT; SOURCE 16 ORGANISM_TAXID: 32630; SOURCE 17 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 18 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 19 MOL_ID: 4; SOURCE 20 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT; SOURCE 21 ORGANISM_TAXID: 32630; SOURCE 22 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 23 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS SUGAR TRANSPORTER; CATION-COUPLED SYMPORTER; NA(+) BINDING; PROTEIN KEYWDS 2 CONFORMATION; NANOBODIES; NABFAB; CRYOEM, MEMBRANE PROTEINS; KEYWDS 3 PROTEIN-PROTEIN INTERACTION, TRANSPORT PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR L.GUAN JRNL AUTH P.HARIHARAN,Y.SHI,S.KATSUBE,K.WILLIBAL,N.D.BURROWS, JRNL AUTH 2 P.MITCHELL,A.BAKHTIIARI,S.STANFIELD,E.PARDON,H.R.KABACK, JRNL AUTH 3 R.LIANG,J.STEYAERT,R.VINER,L.GRAN JRNL TITL MOBILE BARRIER MECHANISMS FOR NA+-COUPLED SYMPORT IN AN MFS JRNL TITL 2 SUGAR TRANSPORTER JRNL REF ELIFE 2024 JRNL REFN ESSN 2050-084X JRNL DOI 10.7554/ELIFE.92462.3 REMARK 2 REMARK 2 RESOLUTION. 3.29 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : CRYOSPARC, EPU, CRYOSPARC, UCSF REMARK 3 CHIMERAX, PHENIX, PHENIX, CRYOSPARC, REMARK 3 CRYOSPARC REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : 7L17 REMARK 3 REFINEMENT SPACE : NULL REMARK 3 REFINEMENT PROTOCOL : AB INITIO MODEL 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) : 3.290 REMARK 3 NUMBER OF PARTICLES : 296925 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 8T60 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_1000275224. 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 : MELBST BOUND WITH NB725_4 REMARK 245 -NABFAB COMPLEX REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 1.00 REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.50 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : 20778 REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS REMARK 245 DETECTOR TYPE : FEI CETA (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) : 1.28 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: TETRAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 VAL A 211 REMARK 465 THR A 212 REMARK 465 ALA A 213 REMARK 465 GLY A 214 REMARK 465 ARG A 215 REMARK 465 PRO A 216 REMARK 465 HIS A 217 REMARK 465 LEU A 218 REMARK 465 GLY A 356 REMARK 465 GLU A 357 REMARK 465 PHE A 358 REMARK 465 LYS A 359 REMARK 465 LEU A 360 REMARK 465 ASN A 361 REMARK 465 TYR A 433 REMARK 465 ARG A 434 REMARK 465 LEU A 435 REMARK 465 ASN A 436 REMARK 465 GLY A 437 REMARK 465 ASP A 438 REMARK 465 MET A 439 REMARK 465 LEU A 440 REMARK 465 ARG A 441 REMARK 465 LYS A 442 REMARK 465 ILE A 443 REMARK 465 GLN A 444 REMARK 465 ILE A 445 REMARK 465 HIS A 446 REMARK 465 LEU A 447 REMARK 465 LEU A 448 REMARK 465 ASP A 449 REMARK 465 LYS A 450 REMARK 465 TYR A 451 REMARK 465 ARG A 452 REMARK 465 LYS A 453 REMARK 465 THR A 454 REMARK 465 PRO A 455 REMARK 465 PRO A 456 REMARK 465 PHE A 457 REMARK 465 VAL A 458 REMARK 465 GLU A 459 REMARK 465 GLN A 460 REMARK 465 PRO A 461 REMARK 465 ASP A 462 REMARK 465 SER A 463 REMARK 465 PRO A 464 REMARK 465 ALA A 465 REMARK 465 ILE A 466 REMARK 465 SER A 467 REMARK 465 VAL A 468 REMARK 465 VAL A 469 REMARK 465 ALA A 470 REMARK 465 THR A 471 REMARK 465 SER A 472 REMARK 465 ASP A 473 REMARK 465 VAL A 474 REMARK 465 LYS A 475 REMARK 465 ALA A 476 REMARK 465 HIS A 477 REMARK 465 HIS A 478 REMARK 465 HIS A 479 REMARK 465 HIS A 480 REMARK 465 HIS A 481 REMARK 465 HIS A 482 REMARK 465 HIS A 483 REMARK 465 HIS A 484 REMARK 465 HIS A 485 REMARK 465 HIS A 486 REMARK 465 MET B -1 REMARK 465 SER B 0 REMARK 465 GLN B 1 REMARK 465 PRO B 124 REMARK 465 HIS B 125 REMARK 465 HIS B 126 REMARK 465 HIS B 127 REMARK 465 HIS B 128 REMARK 465 HIS B 129 REMARK 465 HIS B 130 REMARK 465 HIS B 131 REMARK 465 HIS B 132 REMARK 465 GLU H -2 REMARK 465 ILE H -1 REMARK 465 SER H 0 REMARK 465 SER H 215 REMARK 465 CYS H 216 REMARK 465 ASP H 217 REMARK 465 LYS H 218 REMARK 465 THR H 219 REMARK 465 HIS H 220 REMARK 465 THR H 221 REMARK 465 SER L 0 REMARK 465 ASP L 1 REMARK 465 ILE L 2 REMARK 465 GLN L 3 REMARK 465 CYS L 214 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 LEU A 293 CG CD1 CD2 REMARK 470 TYR A 355 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ARG A 363 CG CD NE CZ NH1 NH2 REMARK 470 TYR A 369 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 TYR A 396 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 MET A 410 CG SD CE 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 VAL A 36 -60.52 -123.49 REMARK 500 SER A 40 -169.97 -72.69 REMARK 500 PHE A 95 37.14 -97.63 REMARK 500 THR A 135 70.44 52.43 REMARK 500 ARG A 139 -1.61 68.12 REMARK 500 ALA A 173 -3.08 73.25 REMARK 500 ALA A 319 61.53 60.10 REMARK 500 HIS A 322 65.05 60.24 REMARK 500 CYS A 364 -7.09 79.24 REMARK 500 PRO A 398 -7.89 -56.02 REMARK 500 THR A 406 -7.03 76.39 REMARK 500 GLN B 3 144.19 -170.97 REMARK 500 ASP B 31 -176.60 -170.68 REMARK 500 ALA B 91 -179.69 -176.15 REMARK 500 ALA H 88 -171.51 -170.90 REMARK 500 THR H 160 19.32 -140.90 REMARK 500 ALA L 13 -169.19 -161.37 REMARK 500 SER L 52 55.25 70.28 REMARK 500 PRO L 80 -8.40 -59.37 REMARK 500 ALA L 84 -169.89 -167.36 REMARK 500 SER L 93 -119.18 55.51 REMARK 500 GLN L 124 -8.43 75.80 REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NA A 501 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 55 OD1 REMARK 620 2 ASN A 58 OD1 68.3 REMARK 620 3 ASP A 59 OD1 122.8 104.2 REMARK 620 4 THR A 121 OG1 67.8 109.2 146.3 REMARK 620 N 1 2 3 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-41062 RELATED DB: EMDB REMARK 900 CRYOEM STRUCTURE OF AN INWARD-FACING MELBST AT A NA(+)-BOUND AND REMARK 900 SUGAR LOW-AFFINITY CONFORMATION DBREF 8T60 A 2 476 UNP P30878 MELB_SALTY 2 476 DBREF 8T60 B -1 132 PDB 8T60 8T60 -1 132 DBREF 8T60 H -2 221 PDB 8T60 8T60 -2 221 DBREF 8T60 L 0 214 PDB 8T60 8T60 0 214 SEQADV 8T60 MET A 5 UNP P30878 LEU 5 CONFLICT SEQADV 8T60 HIS A 477 UNP P30878 EXPRESSION TAG SEQADV 8T60 HIS A 478 UNP P30878 EXPRESSION TAG SEQADV 8T60 HIS A 479 UNP P30878 EXPRESSION TAG SEQADV 8T60 HIS A 480 UNP P30878 EXPRESSION TAG SEQADV 8T60 HIS A 481 UNP P30878 EXPRESSION TAG SEQADV 8T60 HIS A 482 UNP P30878 EXPRESSION TAG SEQADV 8T60 HIS A 483 UNP P30878 EXPRESSION TAG SEQADV 8T60 HIS A 484 UNP P30878 EXPRESSION TAG SEQADV 8T60 HIS A 485 UNP P30878 EXPRESSION TAG SEQADV 8T60 HIS A 486 UNP P30878 EXPRESSION TAG SEQRES 1 A 485 SER ILE SER MET THR THR LYS LEU SER TYR GLY PHE GLY SEQRES 2 A 485 ALA PHE GLY LYS ASP PHE ALA ILE GLY ILE VAL TYR MET SEQRES 3 A 485 TYR LEU MET TYR TYR TYR THR ASP VAL VAL GLY LEU SER SEQRES 4 A 485 VAL GLY LEU VAL GLY THR LEU PHE LEU VAL ALA ARG ILE SEQRES 5 A 485 TRP ASP ALA ILE ASN ASP PRO ILE MET GLY TRP ILE VAL SEQRES 6 A 485 ASN ALA THR ARG SER ARG TRP GLY LYS PHE LYS PRO TRP SEQRES 7 A 485 ILE LEU ILE GLY THR LEU THR ASN SER LEU VAL LEU PHE SEQRES 8 A 485 LEU LEU PHE SER ALA HIS LEU PHE GLU GLY THR ALA GLN SEQRES 9 A 485 VAL VAL PHE VAL CYS VAL THR TYR ILE LEU TRP GLY MET SEQRES 10 A 485 THR TYR THR ILE MET ASP ILE PRO PHE TRP SER LEU VAL SEQRES 11 A 485 PRO THR ILE THR LEU ASP LYS ARG GLU ARG GLU GLN LEU SEQRES 12 A 485 VAL PRO PHE PRO ARG PHE PHE ALA SER LEU ALA GLY PHE SEQRES 13 A 485 VAL THR ALA GLY ILE THR LEU PRO PHE VAL SER TYR VAL SEQRES 14 A 485 GLY GLY ALA ASP ARG GLY PHE GLY PHE GLN MET PHE THR SEQRES 15 A 485 LEU VAL LEU ILE ALA PHE PHE ILE ALA SER THR ILE VAL SEQRES 16 A 485 THR LEU ARG ASN VAL HIS GLU VAL TYR SER SER ASP ASN SEQRES 17 A 485 GLY VAL THR ALA GLY ARG PRO HIS LEU THR LEU LYS THR SEQRES 18 A 485 ILE VAL GLY LEU ILE TYR LYS ASN ASP GLN LEU SER CYS SEQRES 19 A 485 LEU LEU GLY MET ALA LEU ALA TYR ASN ILE ALA SER ASN SEQRES 20 A 485 ILE ILE ASN GLY PHE ALA ILE TYR TYR PHE THR TYR VAL SEQRES 21 A 485 ILE GLY ASP ALA ASP LEU PHE PRO TYR TYR LEU SER TYR SEQRES 22 A 485 ALA GLY ALA ALA ASN LEU LEU THR LEU ILE VAL PHE PRO SEQRES 23 A 485 ARG LEU VAL LYS MET LEU SER ARG ARG ILE LEU TRP ALA SEQRES 24 A 485 GLY ALA SER VAL MET PRO VAL LEU SER CYS ALA GLY LEU SEQRES 25 A 485 PHE ALA MET ALA LEU ALA ASP ILE HIS ASN ALA ALA LEU SEQRES 26 A 485 ILE VAL ALA ALA GLY ILE PHE LEU ASN ILE GLY THR ALA SEQRES 27 A 485 LEU PHE TRP VAL LEU GLN VAL ILE MET VAL ALA ASP THR SEQRES 28 A 485 VAL ASP TYR GLY GLU PHE LYS LEU ASN ILE ARG CYS GLU SEQRES 29 A 485 SER ILE ALA TYR SER VAL GLN THR MET VAL VAL LYS GLY SEQRES 30 A 485 GLY SER ALA PHE ALA ALA PHE PHE ILE ALA LEU VAL LEU SEQRES 31 A 485 GLY LEU ILE GLY TYR THR PRO ASN VAL ALA GLN SER ALA SEQRES 32 A 485 GLN THR LEU GLN GLY MET GLN PHE ILE MET ILE VAL LEU SEQRES 33 A 485 PRO VAL LEU PHE PHE MET MET THR LEU VAL LEU TYR PHE SEQRES 34 A 485 ARG TYR TYR ARG LEU ASN GLY ASP MET LEU ARG LYS ILE SEQRES 35 A 485 GLN ILE HIS LEU LEU ASP LYS TYR ARG LYS THR PRO PRO SEQRES 36 A 485 PHE VAL GLU GLN PRO ASP SER PRO ALA ILE SER VAL VAL SEQRES 37 A 485 ALA THR SER ASP VAL LYS ALA HIS HIS HIS HIS HIS HIS SEQRES 38 A 485 HIS HIS HIS HIS SEQRES 1 B 134 MET SER GLN ARG GLN LEU VAL GLU SER GLY GLY GLY LEU SEQRES 2 B 134 VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA VAL SEQRES 3 B 134 SER GLY ILE ILE PHE ARG ASP ASN ALA MET GLY TRP TYR SEQRES 4 B 134 ARG GLN ALA PRO GLY LYS GLU ARG GLU TRP VAL ALA THR SEQRES 5 B 134 ILE THR ASP LEU GLY TYR THR ALA TYR ALA ASP SER VAL SEQRES 6 B 134 LYS GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASP SEQRES 7 B 134 THR VAL TYR LEU GLN MET ASN SER LEU GLU PRO GLU ASP SEQRES 8 B 134 THR ALA VAL TYR TYR CYS HIS LEU PRO GLY THR ALA ALA SEQRES 9 B 134 GLY ASP TYR TRP GLY LYS GLY THR PRO VAL THR VAL SER SEQRES 10 B 134 SER LEU GLU VAL LEU PHE GLN GLY PRO HIS HIS HIS HIS SEQRES 11 B 134 HIS HIS HIS HIS SEQRES 1 H 239 GLU ILE SER GLU VAL GLN LEU VAL GLU SER GLY GLY GLY SEQRES 2 H 239 LEU VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA SEQRES 3 H 239 ALA SER GLY PHE ASN PHE SER TYR TYR SER ILE HIS TRP SEQRES 4 H 239 VAL ARG GLN ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA SEQRES 5 H 239 TYR ILE SER SER SER SER SER TYR THR SER TYR ALA ASP SEQRES 6 H 239 SER VAL LYS GLY ARG PHE THR ILE SER ALA ASP THR SER SEQRES 7 H 239 LYS ASN THR ALA TYR LEU GLN MET ASN SER LEU ARG ALA SEQRES 8 H 239 GLU ASP THR ALA VAL TYR TYR CYS ALA ARG GLY TYR GLN SEQRES 9 H 239 TYR TRP GLN TYR HIS ALA SER TRP TYR TRP ASN GLY GLY SEQRES 10 H 239 LEU ASP TYR TRP GLY GLN GLY THR LEU VAL THR VAL SER SEQRES 11 H 239 SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA SEQRES 12 H 239 PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU SEQRES 13 H 239 GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR SEQRES 14 H 239 VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS SEQRES 15 H 239 THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER SEQRES 16 H 239 LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY SEQRES 17 H 239 THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER SEQRES 18 H 239 ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER CYS SEQRES 19 H 239 ASP LYS THR HIS THR SEQRES 1 L 215 SER ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER SEQRES 2 L 215 ALA SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SEQRES 3 L 215 SER GLN SER VAL SER SER ALA VAL ALA TRP TYR GLN GLN SEQRES 4 L 215 LYS PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR SER ALA SEQRES 5 L 215 SER SER LEU TYR SER GLY VAL PRO SER ARG PHE SER GLY SEQRES 6 L 215 SER ARG SER GLY THR ASP PHE THR LEU THR ILE SER SER SEQRES 7 L 215 LEU GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN SEQRES 8 L 215 SER SER SER SER LEU ILE THR PHE GLY GLN GLY THR LYS SEQRES 9 L 215 VAL GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 L 215 ILE PHE PRO PRO SER ASP SER GLN LEU LYS SER GLY THR SEQRES 11 L 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 L 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 L 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 L 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 L 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 L 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 L 215 SER PHE ASN ARG GLY GLU CYS HET NA A 501 1 HETNAM NA SODIUM ION FORMUL 5 NA NA 1+ HELIX 1 AA1 SER A 4 VAL A 36 1 33 HELIX 2 AA2 VAL A 41 ASN A 58 1 18 HELIX 3 AA3 ASN A 58 THR A 69 1 12 HELIX 4 AA4 PHE A 76 PHE A 95 1 20 HELIX 5 AA5 SER A 96 PHE A 100 5 5 HELIX 6 AA6 GLY A 102 ILE A 134 1 33 HELIX 7 AA7 GLU A 140 VAL A 145 1 6 HELIX 8 AA8 VAL A 145 GLY A 171 1 27 HELIX 9 AA9 GLY A 176 ASN A 200 1 25 HELIX 10 AB1 LEU A 220 ASN A 230 1 11 HELIX 11 AB2 ASN A 230 VAL A 261 1 32 HELIX 12 AB3 LEU A 267 SER A 273 1 7 HELIX 13 AB4 TYR A 274 VAL A 285 1 12 HELIX 14 AB5 VAL A 285 LEU A 293 1 9 HELIX 15 AB6 SER A 294 ALA A 317 1 24 HELIX 16 AB7 ASN A 323 TYR A 355 1 33 HELIX 17 AB8 GLU A 365 GLY A 395 1 31 HELIX 18 AB9 LEU A 407 LEU A 417 1 11 HELIX 19 AC1 LEU A 417 TYR A 432 1 16 HELIX 20 AC2 ASP B 61 LYS B 64 5 4 HELIX 21 AC3 GLU B 86 THR B 90 5 5 HELIX 22 AC4 ASP H 61 LYS H 64 5 4 HELIX 23 AC5 ARG H 83 THR H 87 5 5 HELIX 24 AC6 LYS L 183 GLU L 187 1 5 SHEET 1 AA1 4 GLN B 3 GLU B 6 0 SHEET 2 AA1 4 SER B 17 SER B 25 -1 O ALA B 23 N VAL B 5 SHEET 3 AA1 4 THR B 77 ASN B 83 -1 O MET B 82 N LEU B 18 SHEET 4 AA1 4 THR B 68 ASP B 72 -1 N ASP B 72 O THR B 77 SHEET 1 AA2 5 THR B 57 TYR B 59 0 SHEET 2 AA2 5 GLU B 46 ILE B 51 -1 N THR B 50 O ALA B 58 SHEET 3 AA2 5 MET B 34 GLN B 39 -1 N TRP B 36 O VAL B 48 SHEET 4 AA2 5 ALA B 91 HIS B 96 -1 O VAL B 92 N GLN B 39 SHEET 5 AA2 5 THR B 110 VAL B 112 -1 O VAL B 112 N ALA B 91 SHEET 1 AA3 4 GLN H 3 SER H 7 0 SHEET 2 AA3 4 LEU H 18 SER H 25 -1 O ALA H 23 N VAL H 5 SHEET 3 AA3 4 THR H 77 MET H 82 -1 O LEU H 80 N LEU H 20 SHEET 4 AA3 4 PHE H 67 ASP H 72 -1 N THR H 68 O GLN H 81 SHEET 1 AA4 6 GLY H 10 VAL H 12 0 SHEET 2 AA4 6 THR H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AA4 6 ALA H 88 ARG H 94 -1 N TYR H 90 O THR H 107 SHEET 4 AA4 6 SER H 33 GLN H 39 -1 N HIS H 35 O ALA H 93 SHEET 5 AA4 6 LEU H 45 SER H 52 -1 O GLU H 46 N ARG H 38 SHEET 6 AA4 6 THR H 57 TYR H 59 -1 O SER H 58 N TYR H 50 SHEET 1 AA5 4 VAL H 121 LEU H 124 0 SHEET 2 AA5 4 THR H 135 VAL H 142 -1 O LEU H 141 N PHE H 122 SHEET 3 AA5 4 TYR H 176 PRO H 185 -1 O LEU H 178 N VAL H 142 SHEET 4 AA5 4 HIS H 164 THR H 165 -1 N HIS H 164 O VAL H 181 SHEET 1 AA6 4 VAL H 121 LEU H 124 0 SHEET 2 AA6 4 THR H 135 VAL H 142 -1 O LEU H 141 N PHE H 122 SHEET 3 AA6 4 TYR H 176 PRO H 185 -1 O LEU H 178 N VAL H 142 SHEET 4 AA6 4 VAL H 169 LEU H 170 -1 N VAL H 169 O SER H 177 SHEET 1 AA7 3 THR H 151 TRP H 154 0 SHEET 2 AA7 3 TYR H 194 HIS H 200 -1 O ASN H 199 N THR H 151 SHEET 3 AA7 3 THR H 205 LYS H 206 -1 O THR H 205 N HIS H 200 SHEET 1 AA8 3 THR H 151 TRP H 154 0 SHEET 2 AA8 3 TYR H 194 HIS H 200 -1 O ASN H 199 N THR H 151 SHEET 3 AA8 3 LYS H 209 VAL H 211 -1 O LYS H 209 N CYS H 196 SHEET 1 AA9 2 SER L 10 ALA L 13 0 SHEET 2 AA9 2 LYS L 103 ILE L 106 1 O GLU L 105 N LEU L 11 SHEET 1 AB1 3 VAL L 19 CYS L 23 0 SHEET 2 AB1 3 PHE L 71 ILE L 75 -1 O LEU L 73 N ILE L 21 SHEET 3 AB1 3 PHE L 62 SER L 65 -1 N SER L 63 O THR L 74 SHEET 1 AB2 3 LYS L 45 ILE L 48 0 SHEET 2 AB2 3 TRP L 35 GLN L 38 -1 N GLN L 37 O LYS L 45 SHEET 3 AB2 3 THR L 85 TYR L 87 -1 O THR L 85 N GLN L 38 SHEET 1 AB3 2 GLN L 89 GLN L 90 0 SHEET 2 AB3 2 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90 SHEET 1 AB4 4 SER L 114 PHE L 118 0 SHEET 2 AB4 4 THR L 129 ASN L 137 -1 O LEU L 135 N PHE L 116 SHEET 3 AB4 4 SER L 174 SER L 182 -1 O LEU L 181 N ALA L 130 SHEET 4 AB4 4 SER L 159 VAL L 163 -1 N SER L 162 O SER L 176 SHEET 1 AB5 4 ALA L 153 LEU L 154 0 SHEET 2 AB5 4 ALA L 144 VAL L 150 -1 N VAL L 150 O ALA L 153 SHEET 3 AB5 4 VAL L 191 HIS L 198 -1 O THR L 197 N LYS L 145 SHEET 4 AB5 4 VAL L 205 ASN L 210 -1 O PHE L 209 N TYR L 192 SSBOND 1 CYS B 22 CYS B 95 1555 1555 2.03 SSBOND 2 CYS H 22 CYS H 92 1555 1555 2.04 SSBOND 3 CYS H 140 CYS H 196 1555 1555 2.03 SSBOND 4 CYS L 23 CYS L 88 1555 1555 2.03 SSBOND 5 CYS L 134 CYS L 194 1555 1555 2.03 LINK OD1 ASP A 55 NA NA A 501 1555 1555 2.66 LINK OD1 ASN A 58 NA NA A 501 1555 1555 2.80 LINK OD1 ASP A 59 NA NA A 501 1555 1555 2.11 LINK OG1 THR A 121 NA NA A 501 1555 1555 2.17 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