HEADER TRANSPORT PROTEIN/IMMUNE SYSTEM 08-DEC-23 8XCD TITLE MACACA FASCICULARIS NTCP IN COMPLEX WITH YN69083 FAB COMPND MOL_ID: 1; COMPND 2 MOLECULE: SOLUTE CARRIER FAMILY 10 MEMBER A1; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: YN69083 FAB HEAVY CHAIN; COMPND 7 CHAIN: H; COMPND 8 MOL_ID: 3; COMPND 9 MOLECULE: YN69083 FAB LIGHT CHAIN; COMPND 10 CHAIN: L SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MACACA FASCICULARIS; SOURCE 3 ORGANISM_COMMON: CRAB-EATING MACAQUE; SOURCE 4 ORGANISM_TAXID: 9541; SOURCE 5 GENE: SLC10A1; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 10 ORGANISM_TAXID: 10090; SOURCE 11 MOL_ID: 3; SOURCE 12 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 13 ORGANISM_TAXID: 10090 KEYWDS TRANSPORTER, TRANSPORT PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR J.H.PARK,N.ISHIMOTO,S.Y.PARK REVDAT 1 13-NOV-24 8XCD 0 JRNL AUTH K.SHIONOYA,J.H.PARK,T.EKIMOTO,J.S.TAKEUCHI,J.MIFUNE, JRNL AUTH 2 T.MORITA,N.ISHIMOTO,H.UMEZAWA,K.YAMAMOTO,C.KOBAYASHI, JRNL AUTH 3 A.KUSUNOKI,N.NOMURA,S.IWATA,M.MURAMATSU,J.R.H.TAME, JRNL AUTH 4 M.IKEGUCHI,S.Y.PARK,K.WATASHI JRNL TITL STRUCTURAL BASIS FOR HEPATITIS B VIRUS RESTRICTION BY A JRNL TITL 2 VIRAL RECEPTOR HOMOLOGUE JRNL REF NAT COMMUN V. 15 9241 2024 JRNL REFN ESSN 2041-1723 JRNL DOI 10.1038/S41467-024-53533-6 REMARK 2 REMARK 2 RESOLUTION. 3.49 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : CRYOSPARC, EPU, CRYOSPARC, UCSF REMARK 3 CHIMERAX, COOT, CRYOSPARC, CRYOSPARC, REMARK 3 CRYOSPARC, CRYOSPARC, PHENIX REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : 7FCI 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) : 3.490 REMARK 3 NUMBER OF PARTICLES : 226937 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 8XCD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-DEC-23. REMARK 100 THE DEPOSITION ID IS D_1300043186. 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 : MACACA FASCICULARIS NTCP IN REMARK 245 COMPLEX WITH YN69083 FAB REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 4.80 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 : NULL REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 BIOQUANTUM (6K X REMARK 245 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 800.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2000.00 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) : 7405.70 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : NULL REMARK 245 CALIBRATED MAGNIFICATION : NULL REMARK 245 SOURCE : FIELD EMISSION GUN REMARK 245 ACCELERATION VOLTAGE (KV) : 300 REMARK 245 IMAGING DETAILS : NULL REMARK 247 REMARK 247 ELECTRON MICROSCOPY REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION REMARK 247 OF THE STRUCTURE FACTORS. REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, H, L REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 GLY A -1 REMARK 465 PRO A 0 REMARK 465 MET A 1 REMARK 465 GLU A 2 REMARK 465 ALA A 3 REMARK 465 HIS A 4 REMARK 465 ASN A 5 REMARK 465 ALA A 6 REMARK 465 SER A 7 REMARK 465 ALA A 8 REMARK 465 PRO A 9 REMARK 465 PHE A 10 REMARK 465 ASN A 11 REMARK 465 PHE A 12 REMARK 465 THR A 13 REMARK 465 LEU A 14 REMARK 465 PRO A 15 REMARK 465 PRO A 16 REMARK 465 ASN A 17 REMARK 465 PHE A 18 REMARK 465 GLY A 19 REMARK 465 LYS A 20 REMARK 465 LYS A 311 REMARK 465 THR A 312 REMARK 465 PRO A 313 REMARK 465 LYS A 314 REMARK 465 ASP A 315 REMARK 465 LYS A 316 REMARK 465 THR A 317 REMARK 465 LYS A 318 REMARK 465 MET A 319 REMARK 465 ILE A 320 REMARK 465 TYR A 321 REMARK 465 THR A 322 REMARK 465 ALA A 323 REMARK 465 ALA A 324 REMARK 465 THR A 325 REMARK 465 THR A 326 REMARK 465 GLU A 327 REMARK 465 GLU A 328 REMARK 465 THR A 329 REMARK 465 ILE A 330 REMARK 465 PRO A 331 REMARK 465 ALA A 332 REMARK 465 ALA A 333 REMARK 465 LEU A 334 REMARK 465 GLY A 335 REMARK 465 ASN A 336 REMARK 465 GLY A 337 REMARK 465 THR A 338 REMARK 465 TYR A 339 REMARK 465 LYS A 340 REMARK 465 GLY A 341 REMARK 465 GLU A 342 REMARK 465 ASP A 343 REMARK 465 CYS A 344 REMARK 465 SER A 345 REMARK 465 PRO A 346 REMARK 465 CYS A 347 REMARK 465 THR A 348 REMARK 465 ALA A 349 REMARK 465 GLY H 225 REMARK 465 CYS H 226 REMARK 465 LYS H 227 REMARK 465 PRO H 228 REMARK 465 CYS H 229 REMARK 465 ILE H 230 REMARK 465 CYS H 231 REMARK 465 THR H 232 REMARK 465 VAL H 233 REMARK 465 PRO H 234 REMARK 465 GLU H 235 REMARK 465 VAL H 236 REMARK 465 SER H 237 REMARK 465 SER H 238 REMARK 465 VAL H 239 REMARK 465 PHE H 240 REMARK 465 ILE H 241 REMARK 465 PHE H 242 REMARK 465 PRO H 243 REMARK 465 PRO H 244 REMARK 465 LYS H 245 REMARK 465 PRO H 246 REMARK 465 LYS H 247 REMARK 465 ASP H 248 REMARK 465 VAL H 249 REMARK 465 LEU H 250 REMARK 465 THR H 251 REMARK 465 ILE H 252 REMARK 465 THR H 253 REMARK 465 LEU H 254 REMARK 465 THR H 255 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 OG1 THR H 28 OD1 ASN H 31 2.16 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 PRO H 127 CA - N - CD ANGL. DEV. = -16.0 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 LYS A 57 71.89 52.47 REMARK 500 ASN A 86 -176.03 -69.01 REMARK 500 PRO A 165 2.53 -67.54 REMARK 500 PRO A 181 45.50 -83.06 REMARK 500 TYR A 186 -63.76 63.54 REMARK 500 ASN A 247 -166.31 -78.98 REMARK 500 SER H 77 19.64 54.67 REMARK 500 SER H 117 98.07 -69.12 REMARK 500 SER H 121 -62.27 -90.23 REMARK 500 THR L 50 -10.53 71.35 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-38240 RELATED DB: EMDB REMARK 900 MACACA FASCICULARIS NTCP IN COMPLEX WITH YN69083 FAB DBREF 8XCD A 1 349 UNP G7PAR4 G7PAR4_MACFA 1 349 DBREF 8XCD H 1 255 PDB 8XCD 8XCD 1 255 DBREF 8XCD L 1 213 PDB 8XCD 8XCD 1 213 SEQADV 8XCD GLY A -1 UNP G7PAR4 EXPRESSION TAG SEQADV 8XCD PRO A 0 UNP G7PAR4 EXPRESSION TAG SEQRES 1 A 351 GLY PRO MET GLU ALA HIS ASN ALA SER ALA PRO PHE ASN SEQRES 2 A 351 PHE THR LEU PRO PRO ASN PHE GLY LYS ARG PRO THR ASP SEQRES 3 A 351 LEU ALA LEU SER ILE ILE LEU VAL PHE MET LEU PHE PHE SEQRES 4 A 351 VAL MET LEU SER LEU GLY CYS THR MET GLU PHE SER LYS SEQRES 5 A 351 ILE LYS ALA HIS LEU TRP LYS PRO LYS GLY LEU ALA ILE SEQRES 6 A 351 ALA LEU VAL ALA GLN TYR GLY ILE MET PRO LEU THR ALA SEQRES 7 A 351 PHE VAL LEU GLY LYS VAL PHE GLN LEU ASN ASN ILE GLU SEQRES 8 A 351 ALA LEU ALA ILE LEU VAL CYS GLY CYS SER PRO GLY GLY SEQRES 9 A 351 ASN LEU SER ASN VAL PHE SER LEU ALA MET LYS GLY ASP SEQRES 10 A 351 MET ASN LEU SER ILE VAL MET THR THR CYS SER THR PHE SEQRES 11 A 351 CYS ALA LEU GLY MET MET PRO LEU LEU LEU TYR LEU TYR SEQRES 12 A 351 THR ARG GLY ILE TYR ASP GLY ASP LEU LYS ASP LYS VAL SEQRES 13 A 351 PRO TYR GLY ARG ILE ILE LEU SER LEU VAL PRO VAL LEU SEQRES 14 A 351 ILE PRO CYS THR ILE GLY ILE VAL LEU LYS SER LYS ARG SEQRES 15 A 351 PRO GLN TYR MET ARG TYR VAL ILE LYS GLY GLY MET ILE SEQRES 16 A 351 ILE ILE LEU LEU CYS SER VAL ALA VAL THR VAL LEU SER SEQRES 17 A 351 ALA ILE ASN VAL GLY LYS SER ILE MET PHE ALA MET THR SEQRES 18 A 351 PRO LEU LEU ILE ALA THR SER SER LEU MET PRO PHE ILE SEQRES 19 A 351 GLY PHE LEU LEU GLY TYR VAL LEU SER ALA LEU PHE CYS SEQRES 20 A 351 LEU ASN GLY ARG CYS ARG ARG THR VAL SER MET GLU THR SEQRES 21 A 351 GLY CYS GLN ASN VAL GLN LEU CYS SER THR ILE LEU ASN SEQRES 22 A 351 VAL ALA PHE PRO PRO GLU VAL ILE GLY PRO LEU PHE PHE SEQRES 23 A 351 PHE PRO LEU LEU TYR MET ILE PHE GLN LEU GLY GLU GLY SEQRES 24 A 351 LEU LEU LEU ILE ALA MET PHE ARG CYS TYR GLU LYS PHE SEQRES 25 A 351 LYS THR PRO LYS ASP LYS THR LYS MET ILE TYR THR ALA SEQRES 26 A 351 ALA THR THR GLU GLU THR ILE PRO ALA ALA LEU GLY ASN SEQRES 27 A 351 GLY THR TYR LYS GLY GLU ASP CYS SER PRO CYS THR ALA SEQRES 1 H 255 GLU VAL GLN LEU GLN GLN PRO GLY ALA GLU LEU VAL LYS SEQRES 2 H 255 PRO GLY ALA SER VAL LYS LEU SER CYS LYS THR SER GLY SEQRES 3 H 255 TYR THR PHE THR ASN TYR TRP MET LYS TRP VAL LYS GLN SEQRES 4 H 255 ARG PRO GLY GLN GLY LEU GLU TRP ILE GLY GLU ILE ASN SEQRES 5 H 255 PRO SER ASN GLY GLY THR ASN TYR ASN GLY LYS PHE LYS SEQRES 6 H 255 SER LYS ALA SER LEU THR VAL ASP LYS SER SER SER THR SEQRES 7 H 255 ALA TYR MET GLN LEU SER SER LEU THR SER GLU ASP SER SEQRES 8 H 255 ALA VAL TYR TYR CYS THR ILE LEU VAL TYR ASP ALA TYR SEQRES 9 H 255 TYR VAL PHE ALA MET ASP TYR TRP GLY LEU GLY THR SER SEQRES 10 H 255 VAL THR VAL SER SER ALA LYS THR THR PRO PRO SER VAL SEQRES 11 H 255 TYR PRO LEU ALA PRO GLY SER ALA ALA GLN THR ASN SER SEQRES 12 H 255 MET VAL THR LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO SEQRES 13 H 255 GLU PRO VAL THR VAL THR TRP ASN SER GLY SER LEU SER SEQRES 14 H 255 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER ASP SEQRES 15 H 255 LEU TYR THR LEU SER SER SER VAL THR VAL PRO SER SER SEQRES 16 H 255 THR TRP PRO SER GLU THR VAL THR CYS ASN VAL ALA HIS SEQRES 17 H 255 PRO ALA SER SER THR LYS VAL ASP LYS LYS ILE VAL PRO SEQRES 18 H 255 ARG ASP CYS GLY CYS LYS PRO CYS ILE CYS THR VAL PRO SEQRES 19 H 255 GLU VAL SER SER VAL PHE ILE PHE PRO PRO LYS PRO LYS SEQRES 20 H 255 ASP VAL LEU THR ILE THR LEU THR SEQRES 1 L 213 ASP ILE VAL MET THR GLN SER PRO ALA ILE MET SER ALA SEQRES 2 L 213 SER PRO GLY GLN LYS VAL THR ILE THR CYS SER ALA SER SEQRES 3 L 213 SER SER VAL ASN TYR MET HIS TRP TYR GLN GLN LYS LEU SEQRES 4 L 213 GLY SER SER PRO LYS LEU TRP ILE TYR ASP THR SER LYS SEQRES 5 L 213 LEU ALA LEU GLY VAL PRO ALA ARG PHE SER GLY SER GLY SEQRES 6 L 213 SER GLY THR SER TYR SER LEU THR ILE SER SER MET GLU SEQRES 7 L 213 ALA GLU ASP ALA ALA SER TYR PHE CYS HIS GLN TRP SER SEQRES 8 L 213 SER TYR PRO ARG THR PHE GLY GLY GLY THR LYS LEU GLU SEQRES 9 L 213 ILE LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE PHE SEQRES 10 L 213 PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA SER SEQRES 11 L 213 VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP ILE SEQRES 12 L 213 ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN ASN SEQRES 13 L 213 GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS ASP SEQRES 14 L 213 SER THR TYR SER MET SER SER THR LEU THR LEU THR LYS SEQRES 15 L 213 ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU ALA SEQRES 16 L 213 THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER PHE SEQRES 17 L 213 ASN ARG ASN GLU CYS HET TCH A 401 35 HET TCH A 402 35 HETNAM TCH TAUROCHOLIC ACID FORMUL 4 TCH 2(C26 H45 N O7 S) HELIX 1 AA1 ARG A 21 GLY A 43 1 23 HELIX 2 AA2 CYS A 44 MET A 46 5 3 HELIX 3 AA3 GLU A 47 TRP A 56 1 10 HELIX 4 AA4 LYS A 59 ILE A 71 1 13 HELIX 5 AA5 ILE A 71 PHE A 83 1 13 HELIX 6 AA6 ASN A 86 SER A 99 1 14 HELIX 7 AA7 ASN A 103 ALA A 111 1 9 HELIX 8 AA8 ASP A 115 THR A 142 1 28 HELIX 9 AA9 PRO A 155 ILE A 160 1 6 HELIX 10 AB1 LEU A 163 ARG A 180 1 18 HELIX 11 AB2 TYR A 186 PHE A 216 1 31 HELIX 12 AB3 THR A 219 CYS A 245 1 27 HELIX 13 AB4 GLY A 248 THR A 258 1 11 HELIX 14 AB5 VAL A 263 PHE A 274 1 12 HELIX 15 AB6 PRO A 275 GLY A 280 1 6 HELIX 16 AB7 PRO A 281 PHE A 283 5 3 HELIX 17 AB8 PHE A 284 PHE A 310 1 27 HELIX 18 AB9 THR H 87 SER H 91 5 5 HELIX 19 AC1 SER H 195 GLU H 200 1 6 HELIX 20 AC2 GLU L 78 ALA L 82 5 5 HELIX 21 AC3 SER L 120 GLY L 127 1 8 HELIX 22 AC4 LYS L 182 HIS L 188 1 7 SHEET 1 AA1 4 GLN H 3 GLN H 5 0 SHEET 2 AA1 4 VAL H 18 SER H 25 -1 O LYS H 23 N GLN H 5 SHEET 3 AA1 4 THR H 78 LEU H 83 -1 O MET H 81 N LEU H 20 SHEET 4 AA1 4 THR H 71 ASP H 73 -1 N THR H 71 O TYR H 80 SHEET 1 AA2 6 ALA H 9 VAL H 12 0 SHEET 2 AA2 6 THR H 116 VAL H 120 1 O SER H 117 N GLU H 10 SHEET 3 AA2 6 ALA H 92 ASP H 102 -1 N TYR H 94 O THR H 116 SHEET 4 AA2 6 LYS H 35 GLN H 39 -1 N LYS H 35 O THR H 97 SHEET 5 AA2 6 LEU H 45 ILE H 51 -1 O GLU H 46 N LYS H 38 SHEET 6 AA2 6 THR H 58 TYR H 60 -1 O ASN H 59 N GLU H 50 SHEET 1 AA3 4 ALA H 9 VAL H 12 0 SHEET 2 AA3 4 THR H 116 VAL H 120 1 O SER H 117 N GLU H 10 SHEET 3 AA3 4 ALA H 92 ASP H 102 -1 N TYR H 94 O THR H 116 SHEET 4 AA3 4 PHE H 107 TRP H 112 -1 O MET H 109 N VAL H 100 SHEET 1 AA4 4 SER H 129 LEU H 133 0 SHEET 2 AA4 4 MET H 144 TYR H 154 -1 O LEU H 150 N TYR H 131 SHEET 3 AA4 4 SER H 188 PRO H 193 -1 O VAL H 192 N VAL H 145 SHEET 4 AA4 4 HIS H 173 THR H 174 -1 N HIS H 173 O SER H 189 SHEET 1 AA5 4 SER H 129 LEU H 133 0 SHEET 2 AA5 4 MET H 144 TYR H 154 -1 O LEU H 150 N TYR H 131 SHEET 3 AA5 4 LEU H 183 LEU H 186 -1 O LEU H 186 N VAL H 151 SHEET 4 AA5 4 VAL H 178 GLN H 180 -1 N GLN H 180 O LEU H 183 SHEET 1 AA6 3 THR H 160 VAL H 161 0 SHEET 2 AA6 3 VAL H 206 HIS H 208 -1 O ALA H 207 N THR H 160 SHEET 3 AA6 3 THR H 213 VAL H 215 -1 O THR H 213 N HIS H 208 SHEET 1 AA7 4 MET L 4 SER L 7 0 SHEET 2 AA7 4 VAL L 19 ALA L 25 -1 O THR L 22 N SER L 7 SHEET 3 AA7 4 TYR L 70 ILE L 74 -1 O TYR L 70 N CYS L 23 SHEET 4 AA7 4 PHE L 61 SER L 64 -1 N SER L 62 O THR L 73 SHEET 1 AA8 6 ILE L 10 MET L 11 0 SHEET 2 AA8 6 THR L 101 LEU L 103 1 O LYS L 102 N MET L 11 SHEET 3 AA8 6 SER L 84 GLN L 89 -1 N TYR L 85 O THR L 101 SHEET 4 AA8 6 HIS L 33 GLN L 37 -1 N HIS L 33 O HIS L 88 SHEET 5 AA8 6 LYS L 44 TYR L 48 -1 O ILE L 47 N TRP L 34 SHEET 6 AA8 6 LYS L 52 LEU L 53 -1 O LYS L 52 N TYR L 48 SHEET 1 AA9 4 ILE L 10 MET L 11 0 SHEET 2 AA9 4 THR L 101 LEU L 103 1 O LYS L 102 N MET L 11 SHEET 3 AA9 4 SER L 84 GLN L 89 -1 N TYR L 85 O THR L 101 SHEET 4 AA9 4 THR L 96 PHE L 97 -1 O THR L 96 N GLN L 89 SHEET 1 AB1 3 SER L 115 PHE L 117 0 SHEET 2 AB1 3 GLY L 128 PHE L 138 -1 O PHE L 134 N SER L 115 SHEET 3 AB1 3 TYR L 172 THR L 181 -1 O MET L 174 N LEU L 135 SHEET 1 AB2 4 SER L 152 GLU L 153 0 SHEET 2 AB2 4 ASN L 144 ILE L 149 -1 N ILE L 149 O SER L 152 SHEET 3 AB2 4 SER L 190 THR L 196 -1 O GLU L 194 N LYS L 146 SHEET 4 AB2 4 ILE L 204 ASN L 209 -1 O LYS L 206 N CYS L 193 SSBOND 1 CYS H 22 CYS H 96 1555 1555 2.04 SSBOND 2 CYS H 149 CYS H 204 1555 1555 2.03 SSBOND 3 CYS L 23 CYS L 87 1555 1555 2.04 SSBOND 4 CYS L 133 CYS L 193 1555 1555 2.03 CISPEP 1 PHE H 155 PRO H 156 0 -1.15 CISPEP 2 GLU H 157 PRO H 158 0 0.90 CISPEP 3 SER L 7 PRO L 8 0 -3.32 CISPEP 4 TYR L 93 PRO L 94 0 -2.54 CISPEP 5 TYR L 139 PRO L 140 0 0.96 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