HEADER MEMBRANE PROTEIN/IMMUNE SYSTEM 16-NOV-24 9KMK TITLE APO MTAUT IN INWARD OPEN II STATE COMPND MOL_ID: 1; COMPND 2 MOLECULE: HEAVY CHAIN OF 9D5 FAB; COMPND 3 CHAIN: H; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: LIGHT CHAIN OF 9D5 FAB; COMPND 7 CHAIN: L; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: SODIUM- AND CHLORIDE-DEPENDENT TAURINE TRANSPORTER; COMPND 11 CHAIN: A; COMPND 12 SYNONYM: SOLUTE CARRIER FAMILY 6 MEMBER 6; COMPND 13 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE; SOURCE 4 ORGANISM_TAXID: 10090; SOURCE 5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 9 ORGANISM_COMMON: HOUSE MOUSE; SOURCE 10 ORGANISM_TAXID: 10090; SOURCE 11 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 13 MOL_ID: 3; SOURCE 14 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 15 ORGANISM_COMMON: HOUSE MOUSE; SOURCE 16 ORGANISM_TAXID: 10090; SOURCE 17 GENE: SLC6A6, TAUT; SOURCE 18 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 19 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS TRANSPORTER, TAURINE, CHLORINE, SODIUM, MEMBRANE PROTEIN/IMMUNE KEYWDS 2 SYSTEM, MEMBRANE PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR J.SHE,M.WANG,J.HE REVDAT 1 02-JUL-25 9KMK 0 JRNL AUTH J.SHE,M.WANG,J.HE JRNL TITL MOLECULAR BASIS FOR SUBSTRATE RECOGNITION AND TRANSPORT OF JRNL TITL 2 MAMMALIAN TAURINE TRANSPORTERS JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.06 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : NULL 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) : 3.060 REMARK 3 NUMBER OF PARTICLES : 150929 REMARK 3 CTF CORRECTION METHOD : NONE REMARK 3 REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL REMARK 3 REMARK 3 OTHER DETAILS: NULL REMARK 4 REMARK 4 9KMK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 19-NOV-24. REMARK 100 THE DEPOSITION ID IS D_1300052531. 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 : MTAUT IN THE INWARD-OPEN II REMARK 245 STATE 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 : NULL REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : TFS KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 (6K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1500.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2700.00 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) : 5400.00 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 APPLY THE FOLLOWING TO CHAINS: H, L, A 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 ALA A 2 REMARK 465 THR A 3 REMARK 465 LYS A 4 REMARK 465 GLU A 5 REMARK 465 LYS A 6 REMARK 465 LEU A 7 REMARK 465 GLN A 8 REMARK 465 CYS A 9 REMARK 465 LEU A 10 REMARK 465 LYS A 11 REMARK 465 ASP A 12 REMARK 465 PHE A 13 REMARK 465 HIS A 14 REMARK 465 LYS A 15 REMARK 465 ASP A 16 REMARK 465 ILE A 17 REMARK 465 LEU A 18 REMARK 465 LYS A 19 REMARK 465 PRO A 20 REMARK 465 SER A 21 REMARK 465 PRO A 22 REMARK 465 GLY A 23 REMARK 465 LYS A 24 REMARK 465 SER A 25 REMARK 465 PRO A 26 REMARK 465 GLY A 27 REMARK 465 THR A 28 REMARK 465 ARG A 29 REMARK 465 PRO A 30 REMARK 465 GLU A 31 REMARK 465 ASP A 32 REMARK 465 GLU A 33 REMARK 465 ALA A 34 REMARK 465 ASP A 35 REMARK 465 GLY A 36 REMARK 465 LYS A 37 REMARK 465 PRO A 38 REMARK 465 PRO A 39 REMARK 465 GLN A 40 REMARK 465 ARG A 41 REMARK 465 GLU A 42 REMARK 465 LYS A 43 REMARK 465 TRP A 44 REMARK 465 SER A 45 REMARK 465 SER A 46 REMARK 465 LYS A 47 REMARK 465 ILE A 48 REMARK 465 ASP A 49 REMARK 465 PHE A 50 REMARK 465 VAL A 51 REMARK 465 LEU A 52 REMARK 465 SER A 53 REMARK 465 VAL A 54 REMARK 465 ALA A 55 REMARK 465 GLY A 56 REMARK 465 HIS A 182 REMARK 465 TRP A 183 REMARK 465 VAL A 184 REMARK 465 SER A 185 REMARK 465 LEU A 186 REMARK 465 SER A 187 REMARK 465 THR A 188 REMARK 465 GLU A 584 REMARK 465 PRO A 585 REMARK 465 ASN A 586 REMARK 465 ARG A 587 REMARK 465 TRP A 588 REMARK 465 ALA A 589 REMARK 465 VAL A 590 REMARK 465 GLU A 591 REMARK 465 ARG A 592 REMARK 465 GLU A 593 REMARK 465 GLY A 594 REMARK 465 ALA A 595 REMARK 465 THR A 596 REMARK 465 PRO A 597 REMARK 465 PHE A 598 REMARK 465 HIS A 599 REMARK 465 SER A 600 REMARK 465 ARG A 601 REMARK 465 VAL A 602 REMARK 465 THR A 603 REMARK 465 LEU A 604 REMARK 465 MET A 605 REMARK 465 ASN A 606 REMARK 465 GLY A 607 REMARK 465 ALA A 608 REMARK 465 LEU A 609 REMARK 465 MET A 610 REMARK 465 LYS A 611 REMARK 465 PRO A 612 REMARK 465 SER A 613 REMARK 465 HIS A 614 REMARK 465 VAL A 615 REMARK 465 ILE A 616 REMARK 465 VAL A 617 REMARK 465 GLU A 618 REMARK 465 THR A 619 REMARK 465 MET A 620 REMARK 465 MET A 621 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 GLU H 89 48.63 -91.93 REMARK 500 GLN H 111 -164.95 -79.82 REMARK 500 SER L 31 -3.48 67.48 REMARK 500 TRP L 48 -52.87 -121.28 REMARK 500 THR L 52 -9.05 66.70 REMARK 500 SER L 53 -37.41 -130.98 REMARK 500 LEU A 61 49.13 -92.92 REMARK 500 CYS A 117 77.35 52.85 REMARK 500 ARG A 177 -30.09 -132.61 REMARK 500 THR A 242 -50.10 -122.15 REMARK 500 ASN A 321 64.12 39.21 REMARK 500 LEU A 383 74.83 53.48 REMARK 500 LEU A 422 -5.56 69.73 REMARK 500 ARG A 428 -11.14 72.10 REMARK 500 SER A 464 45.87 -144.07 REMARK 500 ILE A 496 -61.47 -91.82 REMARK 500 LYS A 534 -3.65 63.24 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-62436 RELATED DB: EMDB REMARK 900 APO MTAUT IN INWARD OPEN II STATE DBREF 9KMK H 1 118 PDB 9KMK 9KMK 1 118 DBREF 9KMK L 1 108 PDB 9KMK 9KMK 1 108 DBREF 9KMK A 1 621 UNP O35316 SC6A6_MOUSE 1 621 SEQADV 9KMK VAL A 485 UNP O35316 GLY 485 CONFLICT SEQADV 9KMK ASN A 486 UNP O35316 ASP 486 CONFLICT SEQADV 9KMK ARG A 487 UNP O35316 ASN 487 CONFLICT SEQADV 9KMK PHE A 488 UNP O35316 LEU 488 CONFLICT SEQADV 9KMK SER A 489 UNP O35316 TYR 489 CONFLICT SEQADV 9KMK GLU A 490 UNP O35316 ASP 490 CONFLICT SEQADV 9KMK ASP A 491 UNP O35316 GLY 491 CONFLICT SEQADV 9KMK ARG A 493 UNP O35316 GLU 493 CONFLICT SEQRES 1 H 118 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL LYS SEQRES 2 H 118 PRO GLY GLY SER LEU LYS LEU SER CYS ALA ALA SER GLY SEQRES 3 H 118 PHE THR PHE SER SER TYR ALA MET SER TRP VAL ARG GLN SEQRES 4 H 118 SER PRO GLU LYS ARG LEU GLU TRP VAL ALA GLU ILE SER SEQRES 5 H 118 SER GLY GLY ARG TYR ILE TYR TYR SER ASP THR VAL THR SEQRES 6 H 118 GLY ARG PHE THR ILE SER ARG ASP ASN ALA ARG ASN ILE SEQRES 7 H 118 LEU HIS LEU GLU MET SER SER LEU ARG SER GLU ASP THR SEQRES 8 H 118 ALA MET TYR TYR CYS ALA ARG GLY GLU VAL ARG GLN ARG SEQRES 9 H 118 GLY PHE ASP TYR TRP GLY GLN GLY THR THR LEU THR VAL SEQRES 10 H 118 SER SEQRES 1 L 108 GLU ASN VAL LEU THR GLN SER PRO ALA ILE MET SER THR SEQRES 2 L 108 SER PRO GLY GLU LYS VAL THR MET THR CYS ARG ALA SER SEQRES 3 L 108 SER SER VAL GLY SER SER TYR LEU HIS TRP TYR GLN GLN SEQRES 4 L 108 LYS SER GLY ALA SER PRO LYS LEU TRP ILE TYR SER THR SEQRES 5 L 108 SER ASN LEU ALA SER GLY VAL PRO ALA ARG PHE SER GLY SEQRES 6 L 108 SER GLY SER GLY THR SER TYR SER LEU THR ILE SER SER SEQRES 7 L 108 VAL GLU ALA GLU ASP ALA ALA THR TYR TYR CYS GLN GLN SEQRES 8 L 108 PHE SER GLY TYR PRO LEU THR PHE GLY SER GLY THR LYS SEQRES 9 L 108 LEU GLU MET LYS SEQRES 1 A 621 MET ALA THR LYS GLU LYS LEU GLN CYS LEU LYS ASP PHE SEQRES 2 A 621 HIS LYS ASP ILE LEU LYS PRO SER PRO GLY LYS SER PRO SEQRES 3 A 621 GLY THR ARG PRO GLU ASP GLU ALA ASP GLY LYS PRO PRO SEQRES 4 A 621 GLN ARG GLU LYS TRP SER SER LYS ILE ASP PHE VAL LEU SEQRES 5 A 621 SER VAL ALA GLY GLY PHE VAL GLY LEU GLY ASN VAL TRP SEQRES 6 A 621 ARG PHE PRO TYR LEU CYS TYR LYS ASN GLY GLY GLY ALA SEQRES 7 A 621 PHE LEU ILE PRO TYR PHE ILE PHE LEU PHE GLY SER GLY SEQRES 8 A 621 LEU PRO VAL PHE PHE LEU GLU VAL ILE ILE GLY GLN TYR SEQRES 9 A 621 THR SER GLU GLY GLY ILE THR CYS TRP GLU LYS ILE CYS SEQRES 10 A 621 PRO LEU PHE SER GLY ILE GLY TYR ALA SER ILE VAL ILE SEQRES 11 A 621 VAL SER LEU LEU ASN VAL TYR TYR ILE VAL ILE LEU ALA SEQRES 12 A 621 TRP ALA THR TYR TYR LEU PHE HIS SER PHE GLN LYS ASP SEQRES 13 A 621 LEU PRO TRP ALA HIS CYS ASN HIS SER TRP ASN THR PRO SEQRES 14 A 621 GLN CYS MET GLU ASP THR LEU ARG ARG ASN GLU SER HIS SEQRES 15 A 621 TRP VAL SER LEU SER THR ALA ASN PHE THR SER PRO VAL SEQRES 16 A 621 ILE GLU PHE TRP GLU ARG ASN VAL LEU SER LEU SER SER SEQRES 17 A 621 GLY ILE ASP ASN PRO GLY SER LEU LYS TRP ASP LEU ALA SEQRES 18 A 621 LEU CYS LEU LEU LEU VAL TRP LEU VAL CYS PHE PHE CYS SEQRES 19 A 621 ILE TRP LYS GLY VAL ARG SER THR GLY LYS VAL VAL TYR SEQRES 20 A 621 PHE THR ALA THR PHE PRO PHE ALA MET LEU LEU VAL LEU SEQRES 21 A 621 LEU VAL ARG GLY LEU THR LEU PRO GLY ALA GLY GLU GLY SEQRES 22 A 621 ILE LYS PHE TYR LEU TYR PRO ASP ILE SER ARG LEU GLY SEQRES 23 A 621 ASP PRO GLN VAL TRP ILE ASP ALA GLY THR GLN ILE PHE SEQRES 24 A 621 PHE SER TYR ALA ILE CYS LEU GLY ALA MET THR SER LEU SEQRES 25 A 621 GLY SER TYR ASN LYS TYR LYS TYR ASN SER TYR ARG ASP SEQRES 26 A 621 CYS MET LEU LEU GLY CYS LEU ASN SER GLY THR SER PHE SEQRES 27 A 621 VAL SER GLY PHE ALA ILE PHE SER ILE LEU GLY PHE MET SEQRES 28 A 621 ALA GLN GLU GLN GLY VAL ASP ILE ALA ASP VAL ALA GLU SEQRES 29 A 621 SER GLY PRO GLY LEU ALA PHE ILE ALA TYR PRO LYS ALA SEQRES 30 A 621 VAL THR MET MET PRO LEU PRO THR PHE TRP SER ILE LEU SEQRES 31 A 621 PHE PHE ILE MET LEU LEU LEU LEU GLY LEU ASP SER GLN SEQRES 32 A 621 PHE VAL GLU VAL GLU GLY GLN ILE THR SER LEU VAL ASP SEQRES 33 A 621 LEU TYR PRO SER PHE LEU ARG LYS GLY TYR ARG ARG GLU SEQRES 34 A 621 ILE PHE ILE ALA ILE LEU CYS SER ILE SER TYR LEU LEU SEQRES 35 A 621 GLY LEU THR MET VAL THR GLU GLY GLY MET TYR VAL PHE SEQRES 36 A 621 GLN LEU PHE ASP TYR TYR ALA ALA SER GLY VAL CYS LEU SEQRES 37 A 621 LEU TRP VAL ALA PHE PHE GLU CYS PHE VAL ILE ALA TRP SEQRES 38 A 621 ILE TYR GLY VAL ASN ARG PHE SER GLU ASP ILE ARG ASP SEQRES 39 A 621 MET ILE GLY TYR ARG PRO GLY PRO TRP MET LYS TYR SER SEQRES 40 A 621 TRP ALA VAL ILE THR PRO ALA LEU CYS VAL GLY CYS PHE SEQRES 41 A 621 VAL PHE SER LEU VAL LYS TYR VAL PRO LEU THR TYR ASN SEQRES 42 A 621 LYS VAL TYR ARG TYR PRO ASP TRP ALA ILE GLY LEU GLY SEQRES 43 A 621 TRP GLY LEU ALA LEU SER SER MET LEU CYS ILE PRO LEU SEQRES 44 A 621 VAL ILE VAL ILE LEU LEU CYS ARG THR GLU GLY PRO LEU SEQRES 45 A 621 ARG VAL ARG ILE LYS TYR LEU ILE THR PRO ARG GLU PRO SEQRES 46 A 621 ASN ARG TRP ALA VAL GLU ARG GLU GLY ALA THR PRO PHE SEQRES 47 A 621 HIS SER ARG VAL THR LEU MET ASN GLY ALA LEU MET LYS SEQRES 48 A 621 PRO SER HIS VAL ILE VAL GLU THR MET MET HET CL A1001 1 HETNAM CL CHLORIDE ION FORMUL 4 CL CL 1- HELIX 1 AA1 ARG H 87 THR H 91 5 5 HELIX 2 AA2 GLU L 80 ALA L 84 5 5 HELIX 3 AA3 TRP A 65 ASN A 74 1 10 HELIX 4 AA4 GLY A 76 SER A 90 1 15 HELIX 5 AA5 SER A 90 THR A 105 1 16 HELIX 6 AA6 GLY A 108 TRP A 113 5 6 HELIX 7 AA7 CYS A 117 PHE A 120 5 4 HELIX 8 AA8 SER A 121 HIS A 151 1 31 HELIX 9 AA9 SER A 193 ASN A 202 1 10 HELIX 10 AB1 LYS A 217 TRP A 236 1 20 HELIX 11 AB2 GLY A 243 THR A 266 1 24 HELIX 12 AB3 GLY A 269 TYR A 279 1 11 HELIX 13 AB4 ASP A 281 GLY A 286 5 6 HELIX 14 AB5 ASP A 287 LEU A 312 1 26 HELIX 15 AB6 ASN A 321 GLN A 355 1 35 HELIX 16 AB7 ILE A 372 THR A 379 1 8 HELIX 17 AB8 LEU A 383 TYR A 418 1 36 HELIX 18 AB9 ARG A 428 LEU A 444 1 17 HELIX 19 AC1 GLY A 450 ALA A 462 1 13 HELIX 20 AC2 GLY A 465 ILE A 482 1 18 HELIX 21 AC3 GLY A 484 ILE A 496 1 13 HELIX 22 AC4 GLY A 501 VAL A 510 1 10 HELIX 23 AC5 VAL A 510 LYS A 526 1 17 HELIX 24 AC6 PRO A 539 LEU A 555 1 17 HELIX 25 AC7 LEU A 555 THR A 568 1 14 HELIX 26 AC8 PRO A 571 THR A 581 1 11 SHEET 1 AA1 4 GLN H 3 SER H 7 0 SHEET 2 AA1 4 LYS H 19 SER H 25 -1 O ALA H 23 N VAL H 5 SHEET 3 AA1 4 ILE H 78 MET H 83 -1 O LEU H 79 N CYS H 22 SHEET 4 AA1 4 PHE H 68 ASP H 73 -1 N SER H 71 O HIS H 80 SHEET 1 AA2 6 LEU H 11 VAL H 12 0 SHEET 2 AA2 6 PHE H 106 VAL H 117 1 O THR H 116 N VAL H 12 SHEET 3 AA2 6 ALA H 92 GLY H 99 -1 N ARG H 98 O TYR H 108 SHEET 4 AA2 6 MET H 34 GLN H 39 -1 N VAL H 37 O TYR H 95 SHEET 5 AA2 6 LEU H 45 ILE H 51 -1 O VAL H 48 N TRP H 36 SHEET 6 AA2 6 ILE H 58 TYR H 60 -1 O TYR H 59 N GLU H 50 SHEET 1 AA3 3 LEU L 4 GLN L 6 0 SHEET 2 AA3 3 VAL L 19 VAL L 29 -1 O ARG L 24 N THR L 5 SHEET 3 AA3 3 PHE L 63 ILE L 76 -1 O GLY L 69 N VAL L 29 SHEET 1 AA4 2 ILE L 10 SER L 12 0 SHEET 2 AA4 2 LYS L 104 GLU L 106 1 O GLU L 106 N MET L 11 SHEET 1 AA5 4 ASN L 54 LEU L 55 0 SHEET 2 AA5 4 PRO L 45 TYR L 50 -1 N TYR L 50 O ASN L 54 SHEET 3 AA5 4 LEU L 34 GLN L 39 -1 N TRP L 36 O ILE L 49 SHEET 4 AA5 4 THR L 86 GLN L 91 -1 O GLN L 90 N HIS L 35 SHEET 1 AA6 2 THR A 531 TYR A 532 0 SHEET 2 AA6 2 TYR A 536 ARG A 537 -1 O TYR A 536 N TYR A 532 SSBOND 1 CYS H 22 CYS H 96 1555 1555 2.03 SSBOND 2 CYS L 23 CYS L 89 1555 1555 2.03 SSBOND 3 CYS A 162 CYS A 171 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