HEADER MEMBRANE PROTEIN 22-APR-23 8OUD TITLE STRUCTURE OF THE HUMAN NEUTRAL AMINO ACID TRANSPORTER ASCT2 IN COMPLEX TITLE 2 WITH NANOBODY 469 COMPND MOL_ID: 1; COMPND 2 MOLECULE: NEUTRAL AMINO ACID TRANSPORTER B(0); COMPND 3 CHAIN: A, B, C; COMPND 4 SYNONYM: ATB(0),BABOON M7 VIRUS RECEPTOR,RD114/SIMIAN TYPE D COMPND 5 RETROVIRUS RECEPTOR,SODIUM-DEPENDENT NEUTRAL AMINO ACID TRANSPORTER COMPND 6 TYPE 2,SOLUTE CARRIER FAMILY 1 MEMBER 5, ALANINE SERINE CYSTEINE COMPND 7 TRANSPORTER 2; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 2; COMPND 10 MOLECULE: NANOBODY 469; COMPND 11 CHAIN: D, E, F; COMPND 12 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: SLC1A5, ASCT2, M7V1, RDR, RDRC; SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HEK293F; SOURCE 9 EXPRESSION_SYSTEM_ORGAN: KIDNEY; SOURCE 10 MOL_ID: 2; SOURCE 11 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 12 ORGANISM_TAXID: 9844; SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 83333 KEYWDS NEUTRAL AMINOACID TRANSMEMBRANE TRANSPORTER ACTIVITY, ASCT2, COMPLEX, KEYWDS 2 NANOBODY, MEMBRANE PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR J.CANUL-TEC,N.REYES REVDAT 1 01-MAY-24 8OUD 0 JRNL AUTH S.KHARE,M.VILLALBA,J.CANUL-TEC,A.BALSEBRE,A.KUMAR,E.PARDON, JRNL AUTH 2 J.STEYAERT,C.PEREZ,N.REYES JRNL TITL RECEPTOR-RECOGNITION AND ANTIVIRAL MECHANISMS OF HUMAN JRNL TITL 2 PLACENTAL PROTEINS. JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.31 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : CRYOSPARC, EPU, CRYOSPARC, UCSF REMARK 3 CHIMERA, PHENIX, 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 : 6GCT REMARK 3 REFINEMENT SPACE : REAL REMARK 3 REFINEMENT PROTOCOL : AB INITIO MODEL REMARK 3 REFINEMENT TARGET : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE : 77.400 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) : 2.310 REMARK 3 NUMBER OF PARTICLES : 441100 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 8OUD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-APR-23. REMARK 100 THE DEPOSITION ID IS D_1292129767. REMARK 245 REMARK 245 EXPERIMENTAL DETAILS REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE REMARK 245 SPECIMEN TYPE : NULL REMARK 245 REMARK 245 ELECTRON MICROSCOPE SAMPLE REMARK 245 SAMPLE TYPE : PARTICLE REMARK 245 PARTICLE TYPE : POINT REMARK 245 NAME OF SAMPLE : COMPLEX OF HUMAN ASCT2 WITH REMARK 245 NANOBODY 69; ALANINE SERINE REMARK 245 CYSTEINE TRANSPORTER 2; REMARK 245 NANOBODY 69 REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 8.10 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 : 4344 REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS REMARK 245 DETECTOR TYPE : FEI FALCON IV (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 600.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 1500.00 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) : 5224.00 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : 130000 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: HEXAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 16230 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 62390 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -144.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F 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 VAL A 2 REMARK 465 ALA A 3 REMARK 465 ASP A 4 REMARK 465 PRO A 5 REMARK 465 PRO A 6 REMARK 465 ARG A 7 REMARK 465 ASP A 8 REMARK 465 SER A 9 REMARK 465 LYS A 10 REMARK 465 GLY A 11 REMARK 465 LEU A 12 REMARK 465 ALA A 13 REMARK 465 ALA A 14 REMARK 465 ALA A 15 REMARK 465 GLU A 16 REMARK 465 PRO A 17 REMARK 465 THR A 18 REMARK 465 ALA A 19 REMARK 465 ASN A 20 REMARK 465 GLY A 21 REMARK 465 GLY A 22 REMARK 465 LEU A 23 REMARK 465 ALA A 24 REMARK 465 LEU A 25 REMARK 465 ALA A 26 REMARK 465 SER A 27 REMARK 465 ILE A 28 REMARK 465 GLU A 29 REMARK 465 ASP A 30 REMARK 465 GLN A 31 REMARK 465 GLY A 32 REMARK 465 ALA A 33 REMARK 465 ALA A 34 REMARK 465 ALA A 35 REMARK 465 GLY A 36 REMARK 465 GLY A 37 REMARK 465 TYR A 38 REMARK 465 CYS A 39 REMARK 465 GLY A 40 REMARK 465 SER A 41 REMARK 465 ARG A 42 REMARK 465 ASP A 43 REMARK 465 GLN A 44 REMARK 465 VAL A 45 REMARK 465 ARG A 46 REMARK 465 ARG A 47 REMARK 465 CYS A 48 REMARK 465 SER A 159 REMARK 465 ALA A 160 REMARK 465 ALA A 161 REMARK 465 ILE A 162 REMARK 465 ASN A 163 REMARK 465 ALA A 164 REMARK 465 SER A 165 REMARK 465 VAL A 166 REMARK 465 GLY A 167 REMARK 465 ALA A 168 REMARK 465 ALA A 169 REMARK 465 GLY A 170 REMARK 465 SER A 171 REMARK 465 ALA A 172 REMARK 465 GLU A 173 REMARK 465 ASN A 174 REMARK 465 ALA A 175 REMARK 465 PRO A 176 REMARK 465 ASN A 212 REMARK 465 ILE A 213 REMARK 465 THR A 214 REMARK 465 GLY A 215 REMARK 465 THR A 216 REMARK 465 ARG A 217 REMARK 465 VAL A 218 REMARK 465 GLU A 490 REMARK 465 SER A 491 REMARK 465 ARG A 492 REMARK 465 SER A 493 REMARK 465 THR A 494 REMARK 465 GLU A 495 REMARK 465 PRO A 496 REMARK 465 GLU A 497 REMARK 465 LEU A 498 REMARK 465 ILE A 499 REMARK 465 GLN A 500 REMARK 465 VAL A 501 REMARK 465 LYS A 502 REMARK 465 SER A 503 REMARK 465 GLU A 504 REMARK 465 LEU A 505 REMARK 465 PRO A 506 REMARK 465 LEU A 507 REMARK 465 ASP A 508 REMARK 465 PRO A 509 REMARK 465 LEU A 510 REMARK 465 PRO A 511 REMARK 465 VAL A 512 REMARK 465 PRO A 513 REMARK 465 THR A 514 REMARK 465 GLU A 515 REMARK 465 GLU A 516 REMARK 465 GLY A 517 REMARK 465 ASN A 518 REMARK 465 PRO A 519 REMARK 465 LEU A 520 REMARK 465 LEU A 521 REMARK 465 LYS A 522 REMARK 465 HIS A 523 REMARK 465 TYR A 524 REMARK 465 ARG A 525 REMARK 465 GLY A 526 REMARK 465 PRO A 527 REMARK 465 ALA A 528 REMARK 465 GLY A 529 REMARK 465 ASP A 530 REMARK 465 ALA A 531 REMARK 465 THR A 532 REMARK 465 VAL A 533 REMARK 465 ALA A 534 REMARK 465 SER A 535 REMARK 465 GLU A 536 REMARK 465 LYS A 537 REMARK 465 GLU A 538 REMARK 465 SER A 539 REMARK 465 VAL A 540 REMARK 465 MET A 541 REMARK 465 MET B 1 REMARK 465 VAL B 2 REMARK 465 ALA B 3 REMARK 465 ASP B 4 REMARK 465 PRO B 5 REMARK 465 PRO B 6 REMARK 465 ARG B 7 REMARK 465 ASP B 8 REMARK 465 SER B 9 REMARK 465 LYS B 10 REMARK 465 GLY B 11 REMARK 465 LEU B 12 REMARK 465 ALA B 13 REMARK 465 ALA B 14 REMARK 465 ALA B 15 REMARK 465 GLU B 16 REMARK 465 PRO B 17 REMARK 465 THR B 18 REMARK 465 ALA B 19 REMARK 465 ASN B 20 REMARK 465 GLY B 21 REMARK 465 GLY B 22 REMARK 465 LEU B 23 REMARK 465 ALA B 24 REMARK 465 LEU B 25 REMARK 465 ALA B 26 REMARK 465 SER B 27 REMARK 465 ILE B 28 REMARK 465 GLU B 29 REMARK 465 ASP B 30 REMARK 465 GLN B 31 REMARK 465 GLY B 32 REMARK 465 ALA B 33 REMARK 465 ALA B 34 REMARK 465 ALA B 35 REMARK 465 GLY B 36 REMARK 465 GLY B 37 REMARK 465 TYR B 38 REMARK 465 CYS B 39 REMARK 465 GLY B 40 REMARK 465 SER B 41 REMARK 465 ARG B 42 REMARK 465 ASP B 43 REMARK 465 GLN B 44 REMARK 465 VAL B 45 REMARK 465 ARG B 46 REMARK 465 ARG B 47 REMARK 465 CYS B 48 REMARK 465 SER B 159 REMARK 465 ALA B 160 REMARK 465 ALA B 161 REMARK 465 ILE B 162 REMARK 465 ASN B 163 REMARK 465 ALA B 164 REMARK 465 SER B 165 REMARK 465 VAL B 166 REMARK 465 GLY B 167 REMARK 465 ALA B 168 REMARK 465 ALA B 169 REMARK 465 GLY B 170 REMARK 465 SER B 171 REMARK 465 ALA B 172 REMARK 465 GLU B 173 REMARK 465 ASN B 174 REMARK 465 ALA B 175 REMARK 465 PRO B 176 REMARK 465 ASN B 212 REMARK 465 ILE B 213 REMARK 465 THR B 214 REMARK 465 GLY B 215 REMARK 465 THR B 216 REMARK 465 ARG B 217 REMARK 465 VAL B 218 REMARK 465 GLU B 490 REMARK 465 SER B 491 REMARK 465 ARG B 492 REMARK 465 SER B 493 REMARK 465 THR B 494 REMARK 465 GLU B 495 REMARK 465 PRO B 496 REMARK 465 GLU B 497 REMARK 465 LEU B 498 REMARK 465 ILE B 499 REMARK 465 GLN B 500 REMARK 465 VAL B 501 REMARK 465 LYS B 502 REMARK 465 SER B 503 REMARK 465 GLU B 504 REMARK 465 LEU B 505 REMARK 465 PRO B 506 REMARK 465 LEU B 507 REMARK 465 ASP B 508 REMARK 465 PRO B 509 REMARK 465 LEU B 510 REMARK 465 PRO B 511 REMARK 465 VAL B 512 REMARK 465 PRO B 513 REMARK 465 THR B 514 REMARK 465 GLU B 515 REMARK 465 GLU B 516 REMARK 465 GLY B 517 REMARK 465 ASN B 518 REMARK 465 PRO B 519 REMARK 465 LEU B 520 REMARK 465 LEU B 521 REMARK 465 LYS B 522 REMARK 465 HIS B 523 REMARK 465 TYR B 524 REMARK 465 ARG B 525 REMARK 465 GLY B 526 REMARK 465 PRO B 527 REMARK 465 ALA B 528 REMARK 465 GLY B 529 REMARK 465 ASP B 530 REMARK 465 ALA B 531 REMARK 465 THR B 532 REMARK 465 VAL B 533 REMARK 465 ALA B 534 REMARK 465 SER B 535 REMARK 465 GLU B 536 REMARK 465 LYS B 537 REMARK 465 GLU B 538 REMARK 465 SER B 539 REMARK 465 VAL B 540 REMARK 465 MET B 541 REMARK 465 MET C 1 REMARK 465 VAL C 2 REMARK 465 ALA C 3 REMARK 465 ASP C 4 REMARK 465 PRO C 5 REMARK 465 PRO C 6 REMARK 465 ARG C 7 REMARK 465 ASP C 8 REMARK 465 SER C 9 REMARK 465 LYS C 10 REMARK 465 GLY C 11 REMARK 465 LEU C 12 REMARK 465 ALA C 13 REMARK 465 ALA C 14 REMARK 465 ALA C 15 REMARK 465 GLU C 16 REMARK 465 PRO C 17 REMARK 465 THR C 18 REMARK 465 ALA C 19 REMARK 465 ASN C 20 REMARK 465 GLY C 21 REMARK 465 GLY C 22 REMARK 465 LEU C 23 REMARK 465 ALA C 24 REMARK 465 LEU C 25 REMARK 465 ALA C 26 REMARK 465 SER C 27 REMARK 465 ILE C 28 REMARK 465 GLU C 29 REMARK 465 ASP C 30 REMARK 465 GLN C 31 REMARK 465 GLY C 32 REMARK 465 ALA C 33 REMARK 465 ALA C 34 REMARK 465 ALA C 35 REMARK 465 GLY C 36 REMARK 465 GLY C 37 REMARK 465 TYR C 38 REMARK 465 CYS C 39 REMARK 465 GLY C 40 REMARK 465 SER C 41 REMARK 465 ARG C 42 REMARK 465 ASP C 43 REMARK 465 GLN C 44 REMARK 465 VAL C 45 REMARK 465 ARG C 46 REMARK 465 ARG C 47 REMARK 465 CYS C 48 REMARK 465 SER C 159 REMARK 465 ALA C 160 REMARK 465 ALA C 161 REMARK 465 ILE C 162 REMARK 465 ASN C 163 REMARK 465 ALA C 164 REMARK 465 SER C 165 REMARK 465 VAL C 166 REMARK 465 GLY C 167 REMARK 465 ALA C 168 REMARK 465 ALA C 169 REMARK 465 GLY C 170 REMARK 465 SER C 171 REMARK 465 ALA C 172 REMARK 465 GLU C 173 REMARK 465 ASN C 174 REMARK 465 ALA C 175 REMARK 465 PRO C 176 REMARK 465 ASN C 212 REMARK 465 ILE C 213 REMARK 465 THR C 214 REMARK 465 GLY C 215 REMARK 465 THR C 216 REMARK 465 ARG C 217 REMARK 465 VAL C 218 REMARK 465 GLU C 490 REMARK 465 SER C 491 REMARK 465 ARG C 492 REMARK 465 SER C 493 REMARK 465 THR C 494 REMARK 465 GLU C 495 REMARK 465 PRO C 496 REMARK 465 GLU C 497 REMARK 465 LEU C 498 REMARK 465 ILE C 499 REMARK 465 GLN C 500 REMARK 465 VAL C 501 REMARK 465 LYS C 502 REMARK 465 SER C 503 REMARK 465 GLU C 504 REMARK 465 LEU C 505 REMARK 465 PRO C 506 REMARK 465 LEU C 507 REMARK 465 ASP C 508 REMARK 465 PRO C 509 REMARK 465 LEU C 510 REMARK 465 PRO C 511 REMARK 465 VAL C 512 REMARK 465 PRO C 513 REMARK 465 THR C 514 REMARK 465 GLU C 515 REMARK 465 GLU C 516 REMARK 465 GLY C 517 REMARK 465 ASN C 518 REMARK 465 PRO C 519 REMARK 465 LEU C 520 REMARK 465 LEU C 521 REMARK 465 LYS C 522 REMARK 465 HIS C 523 REMARK 465 TYR C 524 REMARK 465 ARG C 525 REMARK 465 GLY C 526 REMARK 465 PRO C 527 REMARK 465 ALA C 528 REMARK 465 GLY C 529 REMARK 465 ASP C 530 REMARK 465 ALA C 531 REMARK 465 THR C 532 REMARK 465 VAL C 533 REMARK 465 ALA C 534 REMARK 465 SER C 535 REMARK 465 GLU C 536 REMARK 465 LYS C 537 REMARK 465 GLU C 538 REMARK 465 SER C 539 REMARK 465 VAL C 540 REMARK 465 MET C 541 REMARK 465 SER D 116 REMARK 465 HIS D 117 REMARK 465 HIS D 118 REMARK 465 HIS D 119 REMARK 465 HIS D 120 REMARK 465 HIS D 121 REMARK 465 HIS D 122 REMARK 465 GLU D 123 REMARK 465 PRO D 124 REMARK 465 GLU D 125 REMARK 465 ALA D 126 REMARK 465 SER E 116 REMARK 465 HIS E 117 REMARK 465 HIS E 118 REMARK 465 HIS E 119 REMARK 465 HIS E 120 REMARK 465 HIS E 121 REMARK 465 HIS E 122 REMARK 465 GLU E 123 REMARK 465 PRO E 124 REMARK 465 GLU E 125 REMARK 465 ALA E 126 REMARK 465 SER F 116 REMARK 465 HIS F 117 REMARK 465 HIS F 118 REMARK 465 HIS F 119 REMARK 465 HIS F 120 REMARK 465 HIS F 121 REMARK 465 HIS F 122 REMARK 465 GLU F 123 REMARK 465 PRO F 124 REMARK 465 GLU F 125 REMARK 465 ALA F 126 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 ALA A 75 53.90 -93.50 REMARK 500 LEU B 319 -50.51 -120.53 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 603 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 PHE A 135 O REMARK 620 2 THR A 138 OG1 67.9 REMARK 620 3 THR A 139 OG1 74.9 129.8 REMARK 620 4 ASN A 386 OD1 97.6 100.5 117.1 REMARK 620 5 ASP A 388 OD1 151.4 97.3 99.9 109.4 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NA A 601 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLY A 382 O REMARK 620 2 ASN A 386 O 81.9 REMARK 620 3 ASN A 471 O 146.0 82.7 REMARK 620 4 ASP A 475 OD1 74.0 78.9 73.4 REMARK 620 5 ASP A 475 OD2 83.7 125.7 81.0 46.8 REMARK 620 6 HOH A 707 O 105.1 101.8 107.7 178.8 132.5 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NA A 602 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 THR A 384 O REMARK 620 2 SER A 425 O 128.4 REMARK 620 3 VAL A 426 O 93.0 91.9 REMARK 620 4 ALA A 428 O 99.4 129.2 103.0 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NA B 603 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 PHE B 135 O REMARK 620 2 THR B 138 OG1 65.2 REMARK 620 3 THR B 139 OG1 77.5 127.9 REMARK 620 4 ASP B 388 OD1 144.9 96.1 94.3 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NA B 601 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLY B 382 O REMARK 620 2 ASN B 386 O 89.5 REMARK 620 3 ASN B 471 O 149.8 89.9 REMARK 620 4 ASP B 475 OD1 74.4 85.8 75.5 REMARK 620 5 ASP B 475 OD2 80.7 133.5 78.0 47.7 REMARK 620 6 HOH B 715 O 103.8 116.3 103.5 157.9 110.2 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NA B 602 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 THR B 384 O REMARK 620 2 SER B 425 O 132.5 REMARK 620 3 VAL B 426 O 79.2 83.8 REMARK 620 4 ALA B 428 O 92.1 131.1 87.1 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NA C 603 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 PHE C 135 O REMARK 620 2 THR C 138 OG1 68.0 REMARK 620 3 THR C 139 OG1 76.0 131.3 REMARK 620 4 ASN C 386 OD1 94.9 95.2 120.0 REMARK 620 5 ASP C 388 OD1 156.3 98.7 101.8 106.1 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NA C 601 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLY C 382 O REMARK 620 2 ASN C 386 O 75.3 REMARK 620 3 ASN C 471 O 149.2 94.5 REMARK 620 4 ASP C 475 OD1 70.1 82.5 79.8 REMARK 620 5 ASP C 475 OD2 76.5 129.9 89.3 49.1 REMARK 620 6 HOH C 709 O 88.9 102.3 121.9 156.7 117.5 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NA C 602 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 THR C 384 O REMARK 620 2 SER C 425 O 131.8 REMARK 620 3 VAL C 426 O 84.2 87.9 REMARK 620 4 ALA C 428 O 90.8 136.9 105.2 REMARK 620 N 1 2 3 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-17189 RELATED DB: EMDB REMARK 900 STRUCTURE OF THE HUMAN NEUTRAL AMINO ACID TRANSPORTER ASCT2 IN REMARK 900 COMPLEX WITH NANOBODY 469 DBREF 8OUD A 1 541 UNP Q15758 AAAT_HUMAN 1 541 DBREF 8OUD B 1 541 UNP Q15758 AAAT_HUMAN 1 541 DBREF 8OUD C 1 541 UNP Q15758 AAAT_HUMAN 1 541 DBREF 8OUD D 1 126 PDB 8OUD 8OUD 1 126 DBREF 8OUD E 1 126 PDB 8OUD 8OUD 1 126 DBREF 8OUD F 1 126 PDB 8OUD 8OUD 1 126 SEQRES 1 A 541 MET VAL ALA ASP PRO PRO ARG ASP SER LYS GLY LEU ALA SEQRES 2 A 541 ALA ALA GLU PRO THR ALA ASN GLY GLY LEU ALA LEU ALA SEQRES 3 A 541 SER ILE GLU ASP GLN GLY ALA ALA ALA GLY GLY TYR CYS SEQRES 4 A 541 GLY SER ARG ASP GLN VAL ARG ARG CYS LEU ARG ALA ASN SEQRES 5 A 541 LEU LEU VAL LEU LEU THR VAL VAL ALA VAL VAL ALA GLY SEQRES 6 A 541 VAL ALA LEU GLY LEU GLY VAL SER GLY ALA GLY GLY ALA SEQRES 7 A 541 LEU ALA LEU GLY PRO GLU ARG LEU SER ALA PHE VAL PHE SEQRES 8 A 541 PRO GLY GLU LEU LEU LEU ARG LEU LEU ARG MET ILE ILE SEQRES 9 A 541 LEU PRO LEU VAL VAL CYS SER LEU ILE GLY GLY ALA ALA SEQRES 10 A 541 SER LEU ASP PRO GLY ALA LEU GLY ARG LEU GLY ALA TRP SEQRES 11 A 541 ALA LEU LEU PHE PHE LEU VAL THR THR LEU LEU ALA SER SEQRES 12 A 541 ALA LEU GLY VAL GLY LEU ALA LEU ALA LEU GLN PRO GLY SEQRES 13 A 541 ALA ALA SER ALA ALA ILE ASN ALA SER VAL GLY ALA ALA SEQRES 14 A 541 GLY SER ALA GLU ASN ALA PRO SER LYS GLU VAL LEU ASP SEQRES 15 A 541 SER PHE LEU ASP LEU ALA ARG ASN ILE PHE PRO SER ASN SEQRES 16 A 541 LEU VAL SER ALA ALA PHE ARG SER TYR SER THR THR TYR SEQRES 17 A 541 GLU GLU ARG ASN ILE THR GLY THR ARG VAL LYS VAL PRO SEQRES 18 A 541 VAL GLY GLN GLU VAL GLU GLY MET ASN ILE LEU GLY LEU SEQRES 19 A 541 VAL VAL PHE ALA ILE VAL PHE GLY VAL ALA LEU ARG LYS SEQRES 20 A 541 LEU GLY PRO GLU GLY GLU LEU LEU ILE ARG PHE PHE ASN SEQRES 21 A 541 SER PHE ASN GLU ALA THR MET VAL LEU VAL SER TRP ILE SEQRES 22 A 541 MET TRP TYR ALA PRO VAL GLY ILE MET PHE LEU VAL ALA SEQRES 23 A 541 GLY LYS ILE VAL GLU MET GLU ASP VAL GLY LEU LEU PHE SEQRES 24 A 541 ALA ARG LEU GLY LYS TYR ILE LEU CYS CYS LEU LEU GLY SEQRES 25 A 541 HIS ALA ILE HIS GLY LEU LEU VAL LEU PRO LEU ILE TYR SEQRES 26 A 541 PHE LEU PHE THR ARG LYS ASN PRO TYR ARG PHE LEU TRP SEQRES 27 A 541 GLY ILE VAL THR PRO LEU ALA THR ALA PHE GLY THR SER SEQRES 28 A 541 SER SER SER ALA THR LEU PRO LEU MET MET LYS CYS VAL SEQRES 29 A 541 GLU GLU ASN ASN GLY VAL ALA LYS HIS ILE SER ARG PHE SEQRES 30 A 541 ILE LEU PRO ILE GLY ALA THR VAL ASN MET ASP GLY ALA SEQRES 31 A 541 ALA LEU PHE GLN CYS VAL ALA ALA VAL PHE ILE ALA GLN SEQRES 32 A 541 LEU SER GLN GLN SER LEU ASP PHE VAL LYS ILE ILE THR SEQRES 33 A 541 ILE LEU VAL THR ALA THR ALA SER SER VAL GLY ALA ALA SEQRES 34 A 541 GLY ILE PRO ALA GLY GLY VAL LEU THR LEU ALA ILE ILE SEQRES 35 A 541 LEU GLU ALA VAL ASN LEU PRO VAL ASP HIS ILE SER LEU SEQRES 36 A 541 ILE LEU ALA VAL ASP TRP LEU VAL ASP ARG SER CYS THR SEQRES 37 A 541 VAL LEU ASN VAL GLU GLY ASP ALA LEU GLY ALA GLY LEU SEQRES 38 A 541 LEU GLN ASN TYR VAL ASP ARG THR GLU SER ARG SER THR SEQRES 39 A 541 GLU PRO GLU LEU ILE GLN VAL LYS SER GLU LEU PRO LEU SEQRES 40 A 541 ASP PRO LEU PRO VAL PRO THR GLU GLU GLY ASN PRO LEU SEQRES 41 A 541 LEU LYS HIS TYR ARG GLY PRO ALA GLY ASP ALA THR VAL SEQRES 42 A 541 ALA SER GLU LYS GLU SER VAL MET SEQRES 1 B 541 MET VAL ALA ASP PRO PRO ARG ASP SER LYS GLY LEU ALA SEQRES 2 B 541 ALA ALA GLU PRO THR ALA ASN GLY GLY LEU ALA LEU ALA SEQRES 3 B 541 SER ILE GLU ASP GLN GLY ALA ALA ALA GLY GLY TYR CYS SEQRES 4 B 541 GLY SER ARG ASP GLN VAL ARG ARG CYS LEU ARG ALA ASN SEQRES 5 B 541 LEU LEU VAL LEU LEU THR VAL VAL ALA VAL VAL ALA GLY SEQRES 6 B 541 VAL ALA LEU GLY LEU GLY VAL SER GLY ALA GLY GLY ALA SEQRES 7 B 541 LEU ALA LEU GLY PRO GLU ARG LEU SER ALA PHE VAL PHE SEQRES 8 B 541 PRO GLY GLU LEU LEU LEU ARG LEU LEU ARG MET ILE ILE SEQRES 9 B 541 LEU PRO LEU VAL VAL CYS SER LEU ILE GLY GLY ALA ALA SEQRES 10 B 541 SER LEU ASP PRO GLY ALA LEU GLY ARG LEU GLY ALA TRP SEQRES 11 B 541 ALA LEU LEU PHE PHE LEU VAL THR THR LEU LEU ALA SER SEQRES 12 B 541 ALA LEU GLY VAL GLY LEU ALA LEU ALA LEU GLN PRO GLY SEQRES 13 B 541 ALA ALA SER ALA ALA ILE ASN ALA SER VAL GLY ALA ALA SEQRES 14 B 541 GLY SER ALA GLU ASN ALA PRO SER LYS GLU VAL LEU ASP SEQRES 15 B 541 SER PHE LEU ASP LEU ALA ARG ASN ILE PHE PRO SER ASN SEQRES 16 B 541 LEU VAL SER ALA ALA PHE ARG SER TYR SER THR THR TYR SEQRES 17 B 541 GLU GLU ARG ASN ILE THR GLY THR ARG VAL LYS VAL PRO SEQRES 18 B 541 VAL GLY GLN GLU VAL GLU GLY MET ASN ILE LEU GLY LEU SEQRES 19 B 541 VAL VAL PHE ALA ILE VAL PHE GLY VAL ALA LEU ARG LYS SEQRES 20 B 541 LEU GLY PRO GLU GLY GLU LEU LEU ILE ARG PHE PHE ASN SEQRES 21 B 541 SER PHE ASN GLU ALA THR MET VAL LEU VAL SER TRP ILE SEQRES 22 B 541 MET TRP TYR ALA PRO VAL GLY ILE MET PHE LEU VAL ALA SEQRES 23 B 541 GLY LYS ILE VAL GLU MET GLU ASP VAL GLY LEU LEU PHE SEQRES 24 B 541 ALA ARG LEU GLY LYS TYR ILE LEU CYS CYS LEU LEU GLY SEQRES 25 B 541 HIS ALA ILE HIS GLY LEU LEU VAL LEU PRO LEU ILE TYR SEQRES 26 B 541 PHE LEU PHE THR ARG LYS ASN PRO TYR ARG PHE LEU TRP SEQRES 27 B 541 GLY ILE VAL THR PRO LEU ALA THR ALA PHE GLY THR SER SEQRES 28 B 541 SER SER SER ALA THR LEU PRO LEU MET MET LYS CYS VAL SEQRES 29 B 541 GLU GLU ASN ASN GLY VAL ALA LYS HIS ILE SER ARG PHE SEQRES 30 B 541 ILE LEU PRO ILE GLY ALA THR VAL ASN MET ASP GLY ALA SEQRES 31 B 541 ALA LEU PHE GLN CYS VAL ALA ALA VAL PHE ILE ALA GLN SEQRES 32 B 541 LEU SER GLN GLN SER LEU ASP PHE VAL LYS ILE ILE THR SEQRES 33 B 541 ILE LEU VAL THR ALA THR ALA SER SER VAL GLY ALA ALA SEQRES 34 B 541 GLY ILE PRO ALA GLY GLY VAL LEU THR LEU ALA ILE ILE SEQRES 35 B 541 LEU GLU ALA VAL ASN LEU PRO VAL ASP HIS ILE SER LEU SEQRES 36 B 541 ILE LEU ALA VAL ASP TRP LEU VAL ASP ARG SER CYS THR SEQRES 37 B 541 VAL LEU ASN VAL GLU GLY ASP ALA LEU GLY ALA GLY LEU SEQRES 38 B 541 LEU GLN ASN TYR VAL ASP ARG THR GLU SER ARG SER THR SEQRES 39 B 541 GLU PRO GLU LEU ILE GLN VAL LYS SER GLU LEU PRO LEU SEQRES 40 B 541 ASP PRO LEU PRO VAL PRO THR GLU GLU GLY ASN PRO LEU SEQRES 41 B 541 LEU LYS HIS TYR ARG GLY PRO ALA GLY ASP ALA THR VAL SEQRES 42 B 541 ALA SER GLU LYS GLU SER VAL MET SEQRES 1 C 541 MET VAL ALA ASP PRO PRO ARG ASP SER LYS GLY LEU ALA SEQRES 2 C 541 ALA ALA GLU PRO THR ALA ASN GLY GLY LEU ALA LEU ALA SEQRES 3 C 541 SER ILE GLU ASP GLN GLY ALA ALA ALA GLY GLY TYR CYS SEQRES 4 C 541 GLY SER ARG ASP GLN VAL ARG ARG CYS LEU ARG ALA ASN SEQRES 5 C 541 LEU LEU VAL LEU LEU THR VAL VAL ALA VAL VAL ALA GLY SEQRES 6 C 541 VAL ALA LEU GLY LEU GLY VAL SER GLY ALA GLY GLY ALA SEQRES 7 C 541 LEU ALA LEU GLY PRO GLU ARG LEU SER ALA PHE VAL PHE SEQRES 8 C 541 PRO GLY GLU LEU LEU LEU ARG LEU LEU ARG MET ILE ILE SEQRES 9 C 541 LEU PRO LEU VAL VAL CYS SER LEU ILE GLY GLY ALA ALA SEQRES 10 C 541 SER LEU ASP PRO GLY ALA LEU GLY ARG LEU GLY ALA TRP SEQRES 11 C 541 ALA LEU LEU PHE PHE LEU VAL THR THR LEU LEU ALA SER SEQRES 12 C 541 ALA LEU GLY VAL GLY LEU ALA LEU ALA LEU GLN PRO GLY SEQRES 13 C 541 ALA ALA SER ALA ALA ILE ASN ALA SER VAL GLY ALA ALA SEQRES 14 C 541 GLY SER ALA GLU ASN ALA PRO SER LYS GLU VAL LEU ASP SEQRES 15 C 541 SER PHE LEU ASP LEU ALA ARG ASN ILE PHE PRO SER ASN SEQRES 16 C 541 LEU VAL SER ALA ALA PHE ARG SER TYR SER THR THR TYR SEQRES 17 C 541 GLU GLU ARG ASN ILE THR GLY THR ARG VAL LYS VAL PRO SEQRES 18 C 541 VAL GLY GLN GLU VAL GLU GLY MET ASN ILE LEU GLY LEU SEQRES 19 C 541 VAL VAL PHE ALA ILE VAL PHE GLY VAL ALA LEU ARG LYS SEQRES 20 C 541 LEU GLY PRO GLU GLY GLU LEU LEU ILE ARG PHE PHE ASN SEQRES 21 C 541 SER PHE ASN GLU ALA THR MET VAL LEU VAL SER TRP ILE SEQRES 22 C 541 MET TRP TYR ALA PRO VAL GLY ILE MET PHE LEU VAL ALA SEQRES 23 C 541 GLY LYS ILE VAL GLU MET GLU ASP VAL GLY LEU LEU PHE SEQRES 24 C 541 ALA ARG LEU GLY LYS TYR ILE LEU CYS CYS LEU LEU GLY SEQRES 25 C 541 HIS ALA ILE HIS GLY LEU LEU VAL LEU PRO LEU ILE TYR SEQRES 26 C 541 PHE LEU PHE THR ARG LYS ASN PRO TYR ARG PHE LEU TRP SEQRES 27 C 541 GLY ILE VAL THR PRO LEU ALA THR ALA PHE GLY THR SER SEQRES 28 C 541 SER SER SER ALA THR LEU PRO LEU MET MET LYS CYS VAL SEQRES 29 C 541 GLU GLU ASN ASN GLY VAL ALA LYS HIS ILE SER ARG PHE SEQRES 30 C 541 ILE LEU PRO ILE GLY ALA THR VAL ASN MET ASP GLY ALA SEQRES 31 C 541 ALA LEU PHE GLN CYS VAL ALA ALA VAL PHE ILE ALA GLN SEQRES 32 C 541 LEU SER GLN GLN SER LEU ASP PHE VAL LYS ILE ILE THR SEQRES 33 C 541 ILE LEU VAL THR ALA THR ALA SER SER VAL GLY ALA ALA SEQRES 34 C 541 GLY ILE PRO ALA GLY GLY VAL LEU THR LEU ALA ILE ILE SEQRES 35 C 541 LEU GLU ALA VAL ASN LEU PRO VAL ASP HIS ILE SER LEU SEQRES 36 C 541 ILE LEU ALA VAL ASP TRP LEU VAL ASP ARG SER CYS THR SEQRES 37 C 541 VAL LEU ASN VAL GLU GLY ASP ALA LEU GLY ALA GLY LEU SEQRES 38 C 541 LEU GLN ASN TYR VAL ASP ARG THR GLU SER ARG SER THR SEQRES 39 C 541 GLU PRO GLU LEU ILE GLN VAL LYS SER GLU LEU PRO LEU SEQRES 40 C 541 ASP PRO LEU PRO VAL PRO THR GLU GLU GLY ASN PRO LEU SEQRES 41 C 541 LEU LYS HIS TYR ARG GLY PRO ALA GLY ASP ALA THR VAL SEQRES 42 C 541 ALA SER GLU LYS GLU SER VAL MET SEQRES 1 D 126 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 D 126 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 D 126 SER ILE PHE ARG LEU ASP ALA MET GLY TRP TYR ARG GLN SEQRES 4 D 126 ALA PRO GLY LYS GLN ARG GLU LEU VAL ALA VAL ILE ARG SEQRES 5 D 126 SER GLY GLY SER THR ASP TYR GLY ASP SER VAL LYS GLY SEQRES 6 D 126 ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR VAL SEQRES 7 D 126 TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR ALA SEQRES 8 D 126 VAL TYR TYR CYS ASN ALA VAL GLN ILE LEU LYS THR ILE SEQRES 9 D 126 TYR TRP GLY GLN GLY THR GLN VAL THR VAL SER SER HIS SEQRES 10 D 126 HIS HIS HIS HIS HIS GLU PRO GLU ALA SEQRES 1 E 126 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 E 126 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 E 126 SER ILE PHE ARG LEU ASP ALA MET GLY TRP TYR ARG GLN SEQRES 4 E 126 ALA PRO GLY LYS GLN ARG GLU LEU VAL ALA VAL ILE ARG SEQRES 5 E 126 SER GLY GLY SER THR ASP TYR GLY ASP SER VAL LYS GLY SEQRES 6 E 126 ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR VAL SEQRES 7 E 126 TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR ALA SEQRES 8 E 126 VAL TYR TYR CYS ASN ALA VAL GLN ILE LEU LYS THR ILE SEQRES 9 E 126 TYR TRP GLY GLN GLY THR GLN VAL THR VAL SER SER HIS SEQRES 10 E 126 HIS HIS HIS HIS HIS GLU PRO GLU ALA SEQRES 1 F 126 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 F 126 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 F 126 SER ILE PHE ARG LEU ASP ALA MET GLY TRP TYR ARG GLN SEQRES 4 F 126 ALA PRO GLY LYS GLN ARG GLU LEU VAL ALA VAL ILE ARG SEQRES 5 F 126 SER GLY GLY SER THR ASP TYR GLY ASP SER VAL LYS GLY SEQRES 6 F 126 ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR VAL SEQRES 7 F 126 TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR ALA SEQRES 8 F 126 VAL TYR TYR CYS ASN ALA VAL GLN ILE LEU LYS THR ILE SEQRES 9 F 126 TYR TRP GLY GLN GLY THR GLN VAL THR VAL SER SER HIS SEQRES 10 F 126 HIS HIS HIS HIS HIS GLU PRO GLU ALA HET NA A 601 1 HET NA A 602 1 HET NA A 603 1 HET ALA A 604 6 HET Y01 A 605 35 HET NA B 601 1 HET NA B 602 1 HET NA B 603 1 HET ALA B 604 6 HET Y01 B 605 35 HET NA C 601 1 HET NA C 602 1 HET NA C 603 1 HET ALA C 604 6 HET Y01 C 605 35 HETNAM NA SODIUM ION HETNAM ALA ALANINE HETNAM Y01 CHOLESTEROL HEMISUCCINATE FORMUL 7 NA 9(NA 1+) FORMUL 10 ALA 3(C3 H7 N O2) FORMUL 11 Y01 3(C31 H50 O4) FORMUL 22 HOH *93(H2 O) HELIX 1 AA1 ASN A 52 ALA A 75 1 24 HELIX 2 AA2 GLY A 76 SER A 118 1 43 HELIX 3 AA3 ASP A 120 GLN A 154 1 35 HELIX 4 AA4 GLU A 179 PHE A 192 1 14 HELIX 5 AA5 ASN A 195 ALA A 200 1 6 HELIX 6 AA6 ASN A 230 GLY A 249 1 20 HELIX 7 AA7 GLY A 252 MET A 292 1 41 HELIX 8 AA8 ASP A 294 LEU A 319 1 26 HELIX 9 AA9 LEU A 319 ARG A 330 1 12 HELIX 10 AB1 ASN A 332 ILE A 340 1 9 HELIX 11 AB2 ILE A 340 SER A 351 1 12 HELIX 12 AB3 THR A 356 GLY A 369 1 14 HELIX 13 AB4 ALA A 371 ASN A 386 1 16 HELIX 14 AB5 MET A 387 SER A 405 1 19 HELIX 15 AB6 ASP A 410 ALA A 428 1 19 HELIX 16 AB7 GLY A 435 VAL A 446 1 12 HELIX 17 AB8 PRO A 449 ASP A 451 5 3 HELIX 18 AB9 HIS A 452 LEU A 457 1 6 HELIX 19 AC1 VAL A 459 THR A 489 1 31 HELIX 20 AC2 ASN B 52 ALA B 75 1 24 HELIX 21 AC3 GLY B 77 GLY B 82 1 6 HELIX 22 AC4 GLY B 82 VAL B 90 1 9 HELIX 23 AC5 VAL B 90 SER B 118 1 29 HELIX 24 AC6 ASP B 120 LEU B 153 1 34 HELIX 25 AC7 GLU B 179 PHE B 192 1 14 HELIX 26 AC8 ASN B 195 ALA B 200 1 6 HELIX 27 AC9 ASN B 230 GLY B 249 1 20 HELIX 28 AD1 GLY B 252 MET B 292 1 41 HELIX 29 AD2 ASP B 294 LEU B 319 1 26 HELIX 30 AD3 LEU B 319 ARG B 330 1 12 HELIX 31 AD4 ASN B 332 GLY B 339 1 8 HELIX 32 AD5 ILE B 340 SER B 351 1 12 HELIX 33 AD6 SER B 352 ASN B 367 1 16 HELIX 34 AD7 ALA B 371 ASN B 386 1 16 HELIX 35 AD8 MET B 387 SER B 405 1 19 HELIX 36 AD9 ASP B 410 ALA B 428 1 19 HELIX 37 AE1 GLY B 435 VAL B 446 1 12 HELIX 38 AE2 HIS B 452 LEU B 457 1 6 HELIX 39 AE3 VAL B 459 THR B 489 1 31 HELIX 40 AE4 ASN C 52 ALA C 75 1 24 HELIX 41 AE5 GLY C 77 VAL C 90 1 14 HELIX 42 AE6 VAL C 90 SER C 118 1 29 HELIX 43 AE7 ASP C 120 GLN C 154 1 35 HELIX 44 AE8 GLU C 179 PHE C 192 1 14 HELIX 45 AE9 ASN C 195 ALA C 200 1 6 HELIX 46 AF1 ASN C 230 GLY C 249 1 20 HELIX 47 AF2 GLY C 252 MET C 292 1 41 HELIX 48 AF3 ASP C 294 LEU C 319 1 26 HELIX 49 AF4 LEU C 319 ARG C 330 1 12 HELIX 50 AF5 ASN C 332 ILE C 340 1 9 HELIX 51 AF6 ILE C 340 SER C 351 1 12 HELIX 52 AF7 SER C 352 ASN C 367 1 16 HELIX 53 AF8 ALA C 371 ASN C 386 1 16 HELIX 54 AF9 MET C 387 SER C 405 1 19 HELIX 55 AG1 ASP C 410 ALA C 428 1 19 HELIX 56 AG2 GLY C 435 VAL C 446 1 12 HELIX 57 AG3 HIS C 452 LEU C 457 1 6 HELIX 58 AG4 VAL C 459 ARG C 488 1 30 HELIX 59 AG5 LYS D 86 THR D 90 5 5 HELIX 60 AG6 LYS E 86 THR E 90 5 5 HELIX 61 AG7 LYS F 86 THR F 90 5 5 SHEET 1 AA1 2 ARG A 202 GLU A 209 0 SHEET 2 AA1 2 VAL A 220 GLU A 227 -1 O VAL A 226 N SER A 203 SHEET 1 AA2 2 ARG B 202 GLU B 209 0 SHEET 2 AA2 2 VAL B 220 GLU B 227 -1 O VAL B 226 N SER B 203 SHEET 1 AA3 2 ARG C 202 GLU C 209 0 SHEET 2 AA3 2 VAL C 220 GLU C 227 -1 O VAL C 226 N SER C 203 SHEET 1 AA4 4 VAL D 2 SER D 7 0 SHEET 2 AA4 4 LEU D 18 GLY D 26 -1 O ALA D 23 N VAL D 5 SHEET 3 AA4 4 THR D 77 MET D 82 -1 O VAL D 78 N CYS D 22 SHEET 4 AA4 4 PHE D 67 ASP D 72 -1 N THR D 68 O GLN D 81 SHEET 1 AA5 6 GLY D 10 VAL D 12 0 SHEET 2 AA5 6 THR D 110 VAL D 114 1 O THR D 113 N GLY D 10 SHEET 3 AA5 6 ALA D 91 GLN D 99 -1 N TYR D 93 O THR D 110 SHEET 4 AA5 6 ALA D 33 GLN D 39 -1 N ALA D 33 O VAL D 98 SHEET 5 AA5 6 GLU D 46 ARG D 52 -1 O ILE D 51 N MET D 34 SHEET 6 AA5 6 THR D 57 TYR D 59 -1 O ASP D 58 N VAL D 50 SHEET 1 AA6 4 GLY D 10 VAL D 12 0 SHEET 2 AA6 4 THR D 110 VAL D 114 1 O THR D 113 N GLY D 10 SHEET 3 AA6 4 ALA D 91 GLN D 99 -1 N TYR D 93 O THR D 110 SHEET 4 AA6 4 THR D 103 TRP D 106 -1 O THR D 103 N GLN D 99 SHEET 1 AA7 4 VAL E 2 SER E 7 0 SHEET 2 AA7 4 LEU E 18 GLY E 26 -1 O ALA E 23 N VAL E 5 SHEET 3 AA7 4 THR E 77 MET E 82 -1 O MET E 82 N LEU E 18 SHEET 4 AA7 4 PHE E 67 ASP E 72 -1 N THR E 68 O GLN E 81 SHEET 1 AA8 6 GLY E 10 VAL E 12 0 SHEET 2 AA8 6 THR E 110 VAL E 114 1 O THR E 113 N GLY E 10 SHEET 3 AA8 6 ALA E 91 GLN E 99 -1 N TYR E 93 O THR E 110 SHEET 4 AA8 6 ALA E 33 GLN E 39 -1 N TYR E 37 O TYR E 94 SHEET 5 AA8 6 GLU E 46 ARG E 52 -1 O ILE E 51 N MET E 34 SHEET 6 AA8 6 THR E 57 TYR E 59 -1 O ASP E 58 N VAL E 50 SHEET 1 AA9 4 GLY E 10 VAL E 12 0 SHEET 2 AA9 4 THR E 110 VAL E 114 1 O THR E 113 N GLY E 10 SHEET 3 AA9 4 ALA E 91 GLN E 99 -1 N TYR E 93 O THR E 110 SHEET 4 AA9 4 THR E 103 TRP E 106 -1 O THR E 103 N GLN E 99 SHEET 1 AB1 4 VAL F 2 SER F 7 0 SHEET 2 AB1 4 LEU F 18 GLY F 26 -1 O ALA F 23 N VAL F 5 SHEET 3 AB1 4 THR F 77 MET F 82 -1 O VAL F 78 N CYS F 22 SHEET 4 AB1 4 PHE F 67 ASP F 72 -1 N ASP F 72 O THR F 77 SHEET 1 AB2 6 GLY F 10 VAL F 12 0 SHEET 2 AB2 6 THR F 110 VAL F 114 1 O THR F 113 N GLY F 10 SHEET 3 AB2 6 ALA F 91 GLN F 99 -1 N TYR F 93 O THR F 110 SHEET 4 AB2 6 ALA F 33 GLN F 39 -1 N TYR F 37 O TYR F 94 SHEET 5 AB2 6 GLU F 46 ARG F 52 -1 O GLU F 46 N ARG F 38 SHEET 6 AB2 6 THR F 57 TYR F 59 -1 O ASP F 58 N VAL F 50 SHEET 1 AB3 4 GLY F 10 VAL F 12 0 SHEET 2 AB3 4 THR F 110 VAL F 114 1 O THR F 113 N GLY F 10 SHEET 3 AB3 4 ALA F 91 GLN F 99 -1 N TYR F 93 O THR F 110 SHEET 4 AB3 4 THR F 103 TRP F 106 -1 O THR F 103 N GLN F 99 SSBOND 1 CYS D 22 CYS D 95 1555 1555 2.04 SSBOND 2 CYS E 22 CYS E 95 1555 1555 2.04 SSBOND 3 CYS F 22 CYS F 95 1555 1555 2.04 LINK O PHE A 135 NA NA A 603 1555 1555 2.69 LINK OG1 THR A 138 NA NA A 603 1555 1555 2.71 LINK OG1 THR A 139 NA NA A 603 1555 1555 2.23 LINK O GLY A 382 NA NA A 601 1555 1555 2.26 LINK O THR A 384 NA NA A 602 1555 1555 2.49 LINK O ASN A 386 NA NA A 601 1555 1555 2.54 LINK OD1 ASN A 386 NA NA A 603 1555 1555 1.99 LINK OD1 ASP A 388 NA NA A 603 1555 1555 1.94 LINK O SER A 425 NA NA A 602 1555 1555 2.34 LINK O VAL A 426 NA NA A 602 1555 1555 2.55 LINK O ALA A 428 NA NA A 602 1555 1555 2.33 LINK O ASN A 471 NA NA A 601 1555 1555 2.44 LINK OD1 ASP A 475 NA NA A 601 1555 1555 3.01 LINK OD2 ASP A 475 NA NA A 601 1555 1555 2.21 LINK NA NA A 601 O HOH A 707 1555 1555 2.14 LINK O PHE B 135 NA NA B 603 1555 1555 2.67 LINK OG1 THR B 138 NA NA B 603 1555 1555 2.87 LINK OG1 THR B 139 NA NA B 603 1555 1555 2.18 LINK O GLY B 382 NA NA B 601 1555 1555 2.41 LINK O THR B 384 NA NA B 602 1555 1555 2.64 LINK O ASN B 386 NA NA B 601 1555 1555 2.21 LINK OD1 ASP B 388 NA NA B 603 1555 1555 1.97 LINK O SER B 425 NA NA B 602 1555 1555 2.13 LINK O VAL B 426 NA NA B 602 1555 1555 3.01 LINK O ALA B 428 NA NA B 602 1555 1555 2.46 LINK O ASN B 471 NA NA B 601 1555 1555 2.32 LINK OD1 ASP B 475 NA NA B 601 1555 1555 2.88 LINK OD2 ASP B 475 NA NA B 601 1555 1555 2.45 LINK NA NA B 601 O HOH B 715 1555 1555 2.18 LINK O PHE C 135 NA NA C 603 1555 1555 2.66 LINK OG1 THR C 138 NA NA C 603 1555 1555 2.78 LINK OG1 THR C 139 NA NA C 603 1555 1555 2.17 LINK O GLY C 382 NA NA C 601 1555 1555 2.74 LINK O THR C 384 NA NA C 602 1555 1555 2.72 LINK O ASN C 386 NA NA C 601 1555 1555 2.47 LINK OD1 ASN C 386 NA NA C 603 1555 1555 2.01 LINK OD1 ASP C 388 NA NA C 603 1555 1555 1.94 LINK O SER C 425 NA NA C 602 1555 1555 2.26 LINK O VAL C 426 NA NA C 602 1555 1555 2.74 LINK O ALA C 428 NA NA C 602 1555 1555 2.37 LINK O ASN C 471 NA NA C 601 1555 1555 2.12 LINK OD1 ASP C 475 NA NA C 601 1555 1555 2.87 LINK OD2 ASP C 475 NA NA C 601 1555 1555 2.18 LINK NA NA C 601 O HOH C 709 1555 1555 2.22 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