HEADER SIGNALING PROTEIN 28-JUN-23 8TB7 TITLE CRYO-EM STRUCTURE OF GPR61- COMPND MOL_ID: 1; COMPND 2 MOLECULE: G-PROTEIN COUPLED RECEPTOR 61,SOLUBLE CYTOCHROME B562; COMPND 3 CHAIN: R; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: FAB24 BAK5 HEAVY CHAIN; COMPND 7 CHAIN: H; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: FAB HINGE-BINDING NANOBODY; COMPND 11 CHAIN: N; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 4; COMPND 14 MOLECULE: FAB24 BAK5 LIGHT CHAIN; COMPND 15 CHAIN: L; COMPND 16 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ESCHERICHIA COLI; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606, 562; SOURCE 5 GENE: GPR61, CYBC; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS; SOURCE 10 MOL_ID: 2; SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 12 ORGANISM_COMMON: HUMAN; SOURCE 13 ORGANISM_TAXID: 9606; SOURCE 14 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 15 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 16 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 17 MOL_ID: 3; SOURCE 18 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 19 ORGANISM_TAXID: 9844; SOURCE 20 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 21 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 22 MOL_ID: 4; SOURCE 23 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 24 ORGANISM_COMMON: HUMAN; SOURCE 25 ORGANISM_TAXID: 9606; SOURCE 26 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 27 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 28 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS GPCR, INVERSE AGONIST, MEMBRANE PROTEIN, BRIL, SIGNALING PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR J.A.LEES,J.M.DIAS,S.HAN REVDAT 1 04-OCT-23 8TB7 0 JRNL AUTH J.A.LEES,J.M.DIAS,F.RAJAMOHAN,J.P.FORTIN,R.O'CONNOR, JRNL AUTH 2 J.X.KONG,E.A.G.HUGHES,E.L.FISHER,J.B.TUTTLE,G.LOVETT, JRNL AUTH 3 B.L.KORMOS,R.J.UNWALLA,L.ZHANG,A.M.DECHERT SCHMITT,D.ZHOU, JRNL AUTH 4 M.MORAN,K.A.STEVENS,K.F.FENNELL,A.E.VARGHESE,A.MAXWELL, JRNL AUTH 5 E.E.COTE,Y.ZHANG,S.HAN JRNL TITL AN INVERSE AGONIST OF ORPHAN RECEPTOR GPR61 ACTS BY A G JRNL TITL 2 PROTEIN-COMPETITIVE ALLOSTERIC MECHANISM. JRNL REF NAT COMMUN V. 14 5938 2023 JRNL REFN ESSN 2041-1723 JRNL PMID 37741852 JRNL DOI 10.1038/S41467-023-41646-3 REMARK 2 REMARK 2 RESOLUTION. 2.94 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) : 2.940 REMARK 3 NUMBER OF PARTICLES : 170451 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 8TB7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-JUN-23. REMARK 100 THE DEPOSITION ID IS D_1000272528. 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 : GPR61-ICL3-BRIL CHIMERA IN REMARK 245 COMPLEX WITH ANTI-BRIL FAB24 REMARK 245 BAK5 AND HINGE-BINDING NANOBODY REMARK 245 BOUND TO INVERSE AGONIST REMARK 245 COMPOUND 1 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 : 7.50 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 : FEI FALCON IV (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 600.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2400.00 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) : 5000.00 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: TETRAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: R, H, N, 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 MET R 1 REMARK 465 TYR R 2 REMARK 465 PRO R 3 REMARK 465 TYR R 4 REMARK 465 ASP R 5 REMARK 465 VAL R 6 REMARK 465 PRO R 7 REMARK 465 ASP R 8 REMARK 465 TYR R 9 REMARK 465 ALA R 10 REMARK 465 GLU R 11 REMARK 465 SER R 12 REMARK 465 SER R 13 REMARK 465 PRO R 14 REMARK 465 ILE R 15 REMARK 465 PRO R 16 REMARK 465 GLN R 17 REMARK 465 SER R 18 REMARK 465 SER R 19 REMARK 465 GLY R 20 REMARK 465 ASN R 21 REMARK 465 SER R 22 REMARK 465 SER R 23 REMARK 465 THR R 24 REMARK 465 LEU R 25 REMARK 465 GLY R 26 REMARK 465 ARG R 27 REMARK 465 VAL R 28 REMARK 465 PRO R 29 REMARK 465 GLN R 30 REMARK 465 THR R 31 REMARK 465 PRO R 32 REMARK 465 GLY R 33 REMARK 465 PRO R 34 REMARK 465 SER R 35 REMARK 465 THR R 36 REMARK 465 ALA R 37 REMARK 465 SER R 38 REMARK 465 GLY R 39 REMARK 465 VAL R 40 REMARK 465 PRO R 41 REMARK 465 GLU R 42 REMARK 465 VAL R 43 REMARK 465 GLY R 44 REMARK 465 LEU R 45 REMARK 465 ARG R 46 REMARK 465 ASP R 47 REMARK 465 VAL R 48 REMARK 465 ALA R 49 REMARK 465 SER R 50 REMARK 465 GLU R 51 REMARK 465 SER R 109 REMARK 465 SER R 110 REMARK 465 SER R 111 REMARK 465 ALA R 112 REMARK 465 LEU R 113 REMARK 465 PHE R 114 REMARK 465 ASP R 115 REMARK 465 HIS R 116 REMARK 465 ALA R 117 REMARK 465 LEU R 118 REMARK 465 PHE R 119 REMARK 465 GLY R 189 REMARK 465 ARG R 190 REMARK 465 VAL R 191 REMARK 465 SER R 192 REMARK 465 TRP R 193 REMARK 465 GLU R 194 REMARK 465 GLU R 195 REMARK 465 GLY R 196 REMARK 465 ALA R 197 REMARK 465 PRO R 198 REMARK 465 SER R 199 REMARK 465 VAL R 200 REMARK 465 PRO R 201 REMARK 465 PRO R 202 REMARK 465 GLY R 203 REMARK 465 CYS R 204 REMARK 465 SER R 205 REMARK 465 LEU R 206 REMARK 465 GLN R 207 REMARK 465 TRP R 208 REMARK 465 SER R 209 REMARK 465 HIS R 210 REMARK 465 SER R 211 REMARK 465 ALA R 212 REMARK 465 TYR R 213 REMARK 465 ARG R 355 REMARK 465 ALA R 356 REMARK 465 ARG R 357 REMARK 465 SER R 358 REMARK 465 THR R 359 REMARK 465 LEU R 360 REMARK 465 GLN R 361 REMARK 465 LEU R 393 REMARK 465 SER R 394 REMARK 465 ALA R 395 REMARK 465 GLN R 396 REMARK 465 PRO R 397 REMARK 465 ILE R 398 REMARK 465 SER R 399 REMARK 465 THR R 400 REMARK 465 GLY R 401 REMARK 465 GLU R 432 REMARK 465 LEU R 433 REMARK 465 SER R 434 REMARK 465 LYS R 435 REMARK 465 GLN R 436 REMARK 465 PHE R 437 REMARK 465 VAL R 438 REMARK 465 CYS R 439 REMARK 465 PHE R 440 REMARK 465 PHE R 441 REMARK 465 LYS R 442 REMARK 465 PRO R 443 REMARK 465 ALA R 444 REMARK 465 PRO R 445 REMARK 465 GLU R 446 REMARK 465 GLU R 447 REMARK 465 GLU R 448 REMARK 465 LEU R 449 REMARK 465 ARG R 450 REMARK 465 LEU R 451 REMARK 465 PRO R 452 REMARK 465 SER R 453 REMARK 465 ARG R 454 REMARK 465 GLU R 455 REMARK 465 GLY R 456 REMARK 465 SER R 457 REMARK 465 ILE R 458 REMARK 465 GLU R 459 REMARK 465 GLU R 460 REMARK 465 ASN R 461 REMARK 465 PHE R 462 REMARK 465 LEU R 463 REMARK 465 GLN R 464 REMARK 465 PHE R 465 REMARK 465 LEU R 466 REMARK 465 GLN R 467 REMARK 465 GLY R 468 REMARK 465 THR R 469 REMARK 465 GLY R 470 REMARK 465 CYS R 471 REMARK 465 PRO R 472 REMARK 465 SER R 473 REMARK 465 GLU R 474 REMARK 465 SER R 475 REMARK 465 TRP R 476 REMARK 465 VAL R 477 REMARK 465 SER R 478 REMARK 465 ARG R 479 REMARK 465 PRO R 480 REMARK 465 LEU R 481 REMARK 465 PRO R 482 REMARK 465 SER R 483 REMARK 465 PRO R 484 REMARK 465 LYS R 485 REMARK 465 GLN R 486 REMARK 465 GLU R 487 REMARK 465 PRO R 488 REMARK 465 PRO R 489 REMARK 465 ALA R 490 REMARK 465 VAL R 491 REMARK 465 ASP R 492 REMARK 465 PHE R 493 REMARK 465 ARG R 494 REMARK 465 ILE R 495 REMARK 465 PRO R 496 REMARK 465 GLY R 497 REMARK 465 GLN R 498 REMARK 465 ILE R 499 REMARK 465 ALA R 500 REMARK 465 GLU R 501 REMARK 465 GLU R 502 REMARK 465 THR R 503 REMARK 465 SER R 504 REMARK 465 GLU R 505 REMARK 465 PHE R 506 REMARK 465 LEU R 507 REMARK 465 GLU R 508 REMARK 465 GLN R 509 REMARK 465 GLN R 510 REMARK 465 LEU R 511 REMARK 465 THR R 512 REMARK 465 SER R 513 REMARK 465 ASP R 514 REMARK 465 ILE R 515 REMARK 465 ILE R 516 REMARK 465 MET R 517 REMARK 465 SER R 518 REMARK 465 ASP R 519 REMARK 465 SER R 520 REMARK 465 TYR R 521 REMARK 465 LEU R 522 REMARK 465 ARG R 523 REMARK 465 PRO R 524 REMARK 465 ALA R 525 REMARK 465 ALA R 526 REMARK 465 SER R 527 REMARK 465 PRO R 528 REMARK 465 ARG R 529 REMARK 465 LEU R 530 REMARK 465 GLU R 531 REMARK 465 SER R 532 REMARK 465 GLY R 533 REMARK 465 SER R 534 REMARK 465 ASP R 535 REMARK 465 TYR R 536 REMARK 465 LYS R 537 REMARK 465 ASP R 538 REMARK 465 ASP R 539 REMARK 465 ASP R 540 REMARK 465 ASP R 541 REMARK 465 ALA R 542 REMARK 465 LYS R 543 REMARK 465 MET H -260 REMARK 465 LYS H -259 REMARK 465 LYS H -258 REMARK 465 ASN H -257 REMARK 465 ILE H -256 REMARK 465 ALA H -255 REMARK 465 PHE H -254 REMARK 465 LEU H -253 REMARK 465 LEU H -252 REMARK 465 ALA H -251 REMARK 465 SER H -250 REMARK 465 MET H -249 REMARK 465 PHE H -248 REMARK 465 VAL H -247 REMARK 465 PHE H -246 REMARK 465 SER H -245 REMARK 465 ILE H -244 REMARK 465 ALA H -243 REMARK 465 THR H -242 REMARK 465 ASN H -241 REMARK 465 ALA H -240 REMARK 465 TYR H -239 REMARK 465 ALA H -238 REMARK 465 SER H -237 REMARK 465 ASP H -236 REMARK 465 ILE H -235 REMARK 465 GLN H -234 REMARK 465 MET H -233 REMARK 465 THR H -232 REMARK 465 GLN H -231 REMARK 465 SER H -230 REMARK 465 PRO H -229 REMARK 465 SER H -228 REMARK 465 SER H -227 REMARK 465 LEU H -226 REMARK 465 SER H -225 REMARK 465 ALA H -224 REMARK 465 SER H -223 REMARK 465 VAL H -222 REMARK 465 GLY H -221 REMARK 465 ASP H -220 REMARK 465 ARG H -219 REMARK 465 VAL H -218 REMARK 465 THR H -217 REMARK 465 ILE H -216 REMARK 465 THR H -215 REMARK 465 CYS H -214 REMARK 465 ARG H -213 REMARK 465 ALA H -212 REMARK 465 SER H -211 REMARK 465 GLN H -210 REMARK 465 SER H -209 REMARK 465 VAL H -208 REMARK 465 SER H -207 REMARK 465 SER H -206 REMARK 465 ALA H -205 REMARK 465 VAL H -204 REMARK 465 ALA H -203 REMARK 465 TRP H -202 REMARK 465 TYR H -201 REMARK 465 GLN H -200 REMARK 465 GLN H -199 REMARK 465 LYS H -198 REMARK 465 PRO H -197 REMARK 465 GLY H -196 REMARK 465 LYS H -195 REMARK 465 ALA H -194 REMARK 465 PRO H -193 REMARK 465 LYS H -192 REMARK 465 LEU H -191 REMARK 465 LEU H -190 REMARK 465 ILE H -189 REMARK 465 TYR H -188 REMARK 465 SER H -187 REMARK 465 ALA H -186 REMARK 465 SER H -185 REMARK 465 SER H -184 REMARK 465 LEU H -183 REMARK 465 TYR H -182 REMARK 465 SER H -181 REMARK 465 GLY H -180 REMARK 465 VAL H -179 REMARK 465 PRO H -178 REMARK 465 SER H -177 REMARK 465 ARG H -176 REMARK 465 PHE H -175 REMARK 465 SER H -174 REMARK 465 GLY H -173 REMARK 465 SER H -172 REMARK 465 ARG H -171 REMARK 465 SER H -170 REMARK 465 GLY H -169 REMARK 465 THR H -168 REMARK 465 ASP H -167 REMARK 465 PHE H -166 REMARK 465 THR H -165 REMARK 465 LEU H -164 REMARK 465 THR H -163 REMARK 465 ILE H -162 REMARK 465 SER H -161 REMARK 465 SER H -160 REMARK 465 LEU H -159 REMARK 465 GLN H -158 REMARK 465 PRO H -157 REMARK 465 GLU H -156 REMARK 465 ASP H -155 REMARK 465 PHE H -154 REMARK 465 ALA H -153 REMARK 465 THR H -152 REMARK 465 TYR H -151 REMARK 465 TYR H -150 REMARK 465 CYS H -149 REMARK 465 GLN H -148 REMARK 465 GLN H -147 REMARK 465 TYR H -146 REMARK 465 LEU H -145 REMARK 465 TYR H -144 REMARK 465 TYR H -143 REMARK 465 SER H -142 REMARK 465 LEU H -141 REMARK 465 VAL H -140 REMARK 465 THR H -139 REMARK 465 PHE H -138 REMARK 465 GLY H -137 REMARK 465 GLN H -136 REMARK 465 GLY H -135 REMARK 465 THR H -134 REMARK 465 LYS H -133 REMARK 465 VAL H -132 REMARK 465 GLU H -131 REMARK 465 ILE H -130 REMARK 465 LYS H -129 REMARK 465 ARG H -128 REMARK 465 THR H -127 REMARK 465 VAL H -126 REMARK 465 ALA H -125 REMARK 465 ALA H -124 REMARK 465 PRO H -123 REMARK 465 SER H -122 REMARK 465 VAL H -121 REMARK 465 PHE H -120 REMARK 465 ILE H -119 REMARK 465 PHE H -118 REMARK 465 PRO H -117 REMARK 465 PRO H -116 REMARK 465 SER H -115 REMARK 465 ASP H -114 REMARK 465 SER H -113 REMARK 465 GLN H -112 REMARK 465 LEU H -111 REMARK 465 LYS H -110 REMARK 465 SER H -109 REMARK 465 GLY H -108 REMARK 465 THR H -107 REMARK 465 ALA H -106 REMARK 465 SER H -105 REMARK 465 VAL H -104 REMARK 465 VAL H -103 REMARK 465 CYS H -102 REMARK 465 LEU H -101 REMARK 465 LEU H -100 REMARK 465 ASN H -99 REMARK 465 ASN H -98 REMARK 465 PHE H -97 REMARK 465 TYR H -96 REMARK 465 PRO H -95 REMARK 465 ARG H -94 REMARK 465 GLU H -93 REMARK 465 ALA H -92 REMARK 465 LYS H -91 REMARK 465 VAL H -90 REMARK 465 GLN H -89 REMARK 465 TRP H -88 REMARK 465 LYS H -87 REMARK 465 VAL H -86 REMARK 465 ASP H -85 REMARK 465 ASN H -84 REMARK 465 ALA H -83 REMARK 465 LEU H -82 REMARK 465 GLN H -81 REMARK 465 SER H -80 REMARK 465 GLY H -79 REMARK 465 ASN H -78 REMARK 465 SER H -77 REMARK 465 GLN H -76 REMARK 465 GLU H -75 REMARK 465 SER H -74 REMARK 465 VAL H -73 REMARK 465 THR H -72 REMARK 465 GLU H -71 REMARK 465 GLN H -70 REMARK 465 ASP H -69 REMARK 465 SER H -68 REMARK 465 LYS H -67 REMARK 465 ASP H -66 REMARK 465 SER H -65 REMARK 465 THR H -64 REMARK 465 TYR H -63 REMARK 465 SER H -62 REMARK 465 LEU H -61 REMARK 465 SER H -60 REMARK 465 SER H -59 REMARK 465 THR H -58 REMARK 465 LEU H -57 REMARK 465 THR H -56 REMARK 465 LEU H -55 REMARK 465 SER H -54 REMARK 465 LYS H -53 REMARK 465 ALA H -52 REMARK 465 ASP H -51 REMARK 465 TYR H -50 REMARK 465 GLU H -49 REMARK 465 LYS H -48 REMARK 465 HIS H -47 REMARK 465 LYS H -46 REMARK 465 VAL H -45 REMARK 465 TYR H -44 REMARK 465 ALA H -43 REMARK 465 CYS H -42 REMARK 465 GLU H -41 REMARK 465 VAL H -40 REMARK 465 THR H -39 REMARK 465 HIS H -38 REMARK 465 GLN H -37 REMARK 465 GLY H -36 REMARK 465 LEU H -35 REMARK 465 SER H -34 REMARK 465 SER H -33 REMARK 465 PRO H -32 REMARK 465 VAL H -31 REMARK 465 THR H -30 REMARK 465 LYS H -29 REMARK 465 SER H -28 REMARK 465 PHE H -27 REMARK 465 ASN H -26 REMARK 465 ARG H -25 REMARK 465 GLY H -24 REMARK 465 GLU H -23 REMARK 465 MET H -22 REMARK 465 LYS H -21 REMARK 465 LYS H -20 REMARK 465 ASN H -19 REMARK 465 ILE H -18 REMARK 465 ALA H -17 REMARK 465 PHE H -16 REMARK 465 LEU H -15 REMARK 465 LEU H -14 REMARK 465 ALA H -13 REMARK 465 SER H -12 REMARK 465 MET H -11 REMARK 465 PHE H -10 REMARK 465 VAL H -9 REMARK 465 PHE H -8 REMARK 465 SER H -7 REMARK 465 ILE H -6 REMARK 465 ALA H -5 REMARK 465 THR H -4 REMARK 465 ASN H -3 REMARK 465 ALA H -2 REMARK 465 TYR H -1 REMARK 465 ALA H 0 REMARK 465 GLU H 1 REMARK 465 ILE H 2 REMARK 465 SER H 3 REMARK 465 THR H 145 REMARK 465 SER H 146 REMARK 465 GLY H 147 REMARK 465 SER H 229 REMARK 465 GLY N -1 REMARK 465 SER N 0 REMARK 465 PRO N 41 REMARK 465 GLY N 42 REMARK 465 SER N 120 REMARK 465 MET L 1 REMARK 465 GLY 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 LYS R 362 CB CG CD CE NZ REMARK 470 GLU R 363 CB CG CD OE1 OE2 REMARK 470 VAL R 364 CB CG1 CG2 REMARK 470 LYS H 223 CG CD CE NZ REMARK 470 LYS N 76 CG CD CE NZ REMARK 470 LYS L 40 CG CD CE NZ REMARK 470 LYS L 43 CG CD CE NZ 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 O TRP R 254 HD21 ASN R 258 1.51 REMARK 500 HE22 GLN H 85 OD1 ASN H 87 1.56 REMARK 500 HD22 ASN R 69 OD2 ASP R 95 1.59 REMARK 500 O PRO L 9 OG1 THR L 104 2.16 REMARK 500 NH1 ARG R 281 OD1 ASP R 320 2.18 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 LEU R 216 -2.89 73.75 REMARK 500 GLU R 363 -47.92 85.01 REMARK 500 VAL R 364 109.81 -58.41 REMARK 500 ASP H 158 65.19 61.40 REMARK 500 SER H 201 53.31 34.69 REMARK 500 THR H 205 29.41 49.63 REMARK 500 ARG N 27 -133.20 61.65 REMARK 500 SER N 54 16.91 57.40 REMARK 500 ALA N 58 117.41 -160.88 REMARK 500 ASP N 73 -129.61 53.27 REMARK 500 ALA N 75 -3.39 71.13 REMARK 500 ASN N 83 -158.27 -139.36 REMARK 500 SER N 84 89.56 -65.25 REMARK 500 PRO N 87 40.82 -80.62 REMARK 500 SER N 99 0.65 -69.66 REMARK 500 THR L 21 118.60 -160.34 REMARK 500 GLN L 28 -169.61 -124.59 REMARK 500 SER L 51 -179.28 57.37 REMARK 500 SER L 77 -13.92 -48.36 REMARK 500 ALA L 85 -169.69 -166.05 REMARK 500 GLN L 90 140.66 -170.70 REMARK 500 PRO L 143 -166.63 -71.53 REMARK 500 ASN L 154 61.45 62.20 REMARK 500 GLN L 201 46.12 -81.63 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-41145 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF GPR61- DBREF 8TB7 R 11 242 UNP Q9BZJ8 GPR61_HUMAN 2 233 DBREF 8TB7 R 248 352 UNP P0ABE7 C562_ECOLX 23 127 DBREF 8TB7 R 365 532 UNP Q9BZJ8 GPR61_HUMAN 284 451 DBREF 8TB7 H -260 229 PDB 8TB7 8TB7 -260 229 DBREF 8TB7 N -1 120 PDB 8TB7 8TB7 -1 120 DBREF 8TB7 L 1 214 PDB 8TB7 8TB7 1 214 SEQADV 8TB7 MET R 1 UNP Q9BZJ8 EXPRESSION TAG SEQADV 8TB7 TYR R 2 UNP Q9BZJ8 EXPRESSION TAG SEQADV 8TB7 PRO R 3 UNP Q9BZJ8 EXPRESSION TAG SEQADV 8TB7 TYR R 4 UNP Q9BZJ8 EXPRESSION TAG SEQADV 8TB7 ASP R 5 UNP Q9BZJ8 EXPRESSION TAG SEQADV 8TB7 VAL R 6 UNP Q9BZJ8 EXPRESSION TAG SEQADV 8TB7 PRO R 7 UNP Q9BZJ8 EXPRESSION TAG SEQADV 8TB7 ASP R 8 UNP Q9BZJ8 EXPRESSION TAG SEQADV 8TB7 TYR R 9 UNP Q9BZJ8 EXPRESSION TAG SEQADV 8TB7 ALA R 10 UNP Q9BZJ8 EXPRESSION TAG SEQADV 8TB7 ALA R 243 UNP Q9BZJ8 LINKER SEQADV 8TB7 ARG R 244 UNP Q9BZJ8 LINKER SEQADV 8TB7 ARG R 245 UNP Q9BZJ8 LINKER SEQADV 8TB7 GLN R 246 UNP Q9BZJ8 LINKER SEQADV 8TB7 LEU R 247 UNP Q9BZJ8 LINKER SEQADV 8TB7 TRP R 254 UNP P0ABE7 MET 29 CONFLICT SEQADV 8TB7 ILE R 349 UNP P0ABE7 HIS 124 CONFLICT SEQADV 8TB7 LEU R 353 UNP P0ABE7 LINKER SEQADV 8TB7 GLU R 354 UNP P0ABE7 LINKER SEQADV 8TB7 ARG R 355 UNP P0ABE7 LINKER SEQADV 8TB7 ALA R 356 UNP P0ABE7 LINKER SEQADV 8TB7 ARG R 357 UNP P0ABE7 LINKER SEQADV 8TB7 SER R 358 UNP P0ABE7 LINKER SEQADV 8TB7 THR R 359 UNP P0ABE7 LINKER SEQADV 8TB7 LEU R 360 UNP P0ABE7 LINKER SEQADV 8TB7 GLN R 361 UNP P0ABE7 LINKER SEQADV 8TB7 LYS R 362 UNP P0ABE7 LINKER SEQADV 8TB7 GLU R 363 UNP P0ABE7 LINKER SEQADV 8TB7 VAL R 364 UNP P0ABE7 LINKER SEQADV 8TB7 GLY R 533 UNP Q9BZJ8 EXPRESSION TAG SEQADV 8TB7 SER R 534 UNP Q9BZJ8 EXPRESSION TAG SEQADV 8TB7 ASP R 535 UNP Q9BZJ8 EXPRESSION TAG SEQADV 8TB7 TYR R 536 UNP Q9BZJ8 EXPRESSION TAG SEQADV 8TB7 LYS R 537 UNP Q9BZJ8 EXPRESSION TAG SEQADV 8TB7 ASP R 538 UNP Q9BZJ8 EXPRESSION TAG SEQADV 8TB7 ASP R 539 UNP Q9BZJ8 EXPRESSION TAG SEQADV 8TB7 ASP R 540 UNP Q9BZJ8 EXPRESSION TAG SEQADV 8TB7 ASP R 541 UNP Q9BZJ8 EXPRESSION TAG SEQADV 8TB7 ALA R 542 UNP Q9BZJ8 EXPRESSION TAG SEQADV 8TB7 LYS R 543 UNP Q9BZJ8 EXPRESSION TAG SEQRES 1 R 543 MET TYR PRO TYR ASP VAL PRO ASP TYR ALA GLU SER SER SEQRES 2 R 543 PRO ILE PRO GLN SER SER GLY ASN SER SER THR LEU GLY SEQRES 3 R 543 ARG VAL PRO GLN THR PRO GLY PRO SER THR ALA SER GLY SEQRES 4 R 543 VAL PRO GLU VAL GLY LEU ARG ASP VAL ALA SER GLU SER SEQRES 5 R 543 VAL ALA LEU PHE PHE MET LEU LEU LEU ASP LEU THR ALA SEQRES 6 R 543 VAL ALA GLY ASN ALA ALA VAL MET ALA VAL ILE ALA LYS SEQRES 7 R 543 THR PRO ALA LEU ARG LYS PHE VAL PHE VAL PHE HIS LEU SEQRES 8 R 543 CYS LEU VAL ASP LEU LEU ALA ALA LEU THR LEU MET PRO SEQRES 9 R 543 LEU ALA MET LEU SER SER SER ALA LEU PHE ASP HIS ALA SEQRES 10 R 543 LEU PHE GLY GLU VAL ALA CYS ARG LEU TYR LEU PHE LEU SEQRES 11 R 543 SER VAL CYS PHE VAL SER LEU ALA ILE LEU SER VAL SER SEQRES 12 R 543 ALA ILE ASN VAL GLU ARG TYR TYR TYR VAL VAL HIS PRO SEQRES 13 R 543 MET ARG TYR GLU VAL ARG MET THR LEU GLY LEU VAL ALA SEQRES 14 R 543 SER VAL LEU VAL GLY VAL TRP VAL LYS ALA LEU ALA MET SEQRES 15 R 543 ALA SER VAL PRO VAL LEU GLY ARG VAL SER TRP GLU GLU SEQRES 16 R 543 GLY ALA PRO SER VAL PRO PRO GLY CYS SER LEU GLN TRP SEQRES 17 R 543 SER HIS SER ALA TYR CYS GLN LEU PHE VAL VAL VAL PHE SEQRES 18 R 543 ALA VAL LEU TYR PHE LEU LEU PRO LEU LEU LEU ILE LEU SEQRES 19 R 543 VAL VAL TYR CYS SER MET PHE ARG ALA ARG ARG GLN LEU SEQRES 20 R 543 ALA ASP LEU GLU ASP ASN TRP GLU THR LEU ASN ASP ASN SEQRES 21 R 543 LEU LYS VAL ILE GLU LYS ALA ASP ASN ALA ALA GLN VAL SEQRES 22 R 543 LYS ASP ALA LEU THR LYS MET ARG ALA ALA ALA LEU ASP SEQRES 23 R 543 ALA GLN LYS ALA THR PRO PRO LYS LEU GLU ASP LYS SER SEQRES 24 R 543 PRO ASP SER PRO GLU MET LYS ASP PHE ARG HIS GLY PHE SEQRES 25 R 543 ASP ILE LEU VAL GLY GLN ILE ASP ASP ALA LEU LYS LEU SEQRES 26 R 543 ALA ASN GLU GLY LYS VAL LYS GLU ALA GLN ALA ALA ALA SEQRES 27 R 543 GLU GLN LEU LYS THR THR ARG ASN ALA TYR ILE GLN LYS SEQRES 28 R 543 TYR LEU GLU ARG ALA ARG SER THR LEU GLN LYS GLU VAL SEQRES 29 R 543 LYS ALA ALA VAL VAL LEU LEU ALA VAL GLY GLY GLN PHE SEQRES 30 R 543 LEU LEU CYS TRP LEU PRO TYR PHE SER PHE HIS LEU TYR SEQRES 31 R 543 VAL ALA LEU SER ALA GLN PRO ILE SER THR GLY GLN VAL SEQRES 32 R 543 GLU SER VAL VAL THR TRP ILE GLY TYR PHE CYS PHE THR SEQRES 33 R 543 SER ASN PRO PHE PHE TYR GLY CYS LEU ASN ARG GLN ILE SEQRES 34 R 543 ARG GLY GLU LEU SER LYS GLN PHE VAL CYS PHE PHE LYS SEQRES 35 R 543 PRO ALA PRO GLU GLU GLU LEU ARG LEU PRO SER ARG GLU SEQRES 36 R 543 GLY SER ILE GLU GLU ASN PHE LEU GLN PHE LEU GLN GLY SEQRES 37 R 543 THR GLY CYS PRO SER GLU SER TRP VAL SER ARG PRO LEU SEQRES 38 R 543 PRO SER PRO LYS GLN GLU PRO PRO ALA VAL ASP PHE ARG SEQRES 39 R 543 ILE PRO GLY GLN ILE ALA GLU GLU THR SER GLU PHE LEU SEQRES 40 R 543 GLU GLN GLN LEU THR SER ASP ILE ILE MET SER ASP SER SEQRES 41 R 543 TYR LEU ARG PRO ALA ALA SER PRO ARG LEU GLU SER GLY SEQRES 42 R 543 SER ASP TYR LYS ASP ASP ASP ASP ALA LYS SEQRES 1 H 490 MET LYS LYS ASN ILE ALA PHE LEU LEU ALA SER MET PHE SEQRES 2 H 490 VAL PHE SER ILE ALA THR ASN ALA TYR ALA SER ASP ILE SEQRES 3 H 490 GLN MET THR GLN SER PRO SER SER LEU SER ALA SER VAL SEQRES 4 H 490 GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER GLN SER SEQRES 5 H 490 VAL SER SER ALA VAL ALA TRP TYR GLN GLN LYS PRO GLY SEQRES 6 H 490 LYS ALA PRO LYS LEU LEU ILE TYR SER ALA SER SER LEU SEQRES 7 H 490 TYR SER GLY VAL PRO SER ARG PHE SER GLY SER ARG SER SEQRES 8 H 490 GLY THR ASP PHE THR LEU THR ILE SER SER LEU GLN PRO SEQRES 9 H 490 GLU ASP PHE ALA THR TYR TYR CYS GLN GLN TYR LEU TYR SEQRES 10 H 490 TYR SER LEU VAL THR PHE GLY GLN GLY THR LYS VAL GLU SEQRES 11 H 490 ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE PHE SEQRES 12 H 490 PRO PRO SER ASP SER GLN LEU LYS SER GLY THR ALA SER SEQRES 13 H 490 VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU ALA SEQRES 14 H 490 LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER GLY SEQRES 15 H 490 ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS ASP SEQRES 16 H 490 SER THR TYR SER LEU SER SER THR LEU THR LEU SER LYS SEQRES 17 H 490 ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU VAL SEQRES 18 H 490 THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER PHE SEQRES 19 H 490 ASN ARG GLY GLU MET LYS LYS ASN ILE ALA PHE LEU LEU SEQRES 20 H 490 ALA SER MET PHE VAL PHE SER ILE ALA THR ASN ALA TYR SEQRES 21 H 490 ALA GLU ILE SER GLU VAL GLN LEU VAL GLU SER GLY GLY SEQRES 22 H 490 GLY LEU VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS SEQRES 23 H 490 ALA ALA SER GLY PHE ASN VAL ARG SER PHE SER ILE HIS SEQRES 24 H 490 TRP VAL ARG GLN ALA PRO GLY LYS GLY LEU GLU TRP VAL SEQRES 25 H 490 ALA TYR ILE SER SER SER SER GLY SER THR SER TYR ALA SEQRES 26 H 490 ASP SER VAL LYS GLY ARG PHE THR ILE SER ALA ASP THR SEQRES 27 H 490 SER LYS ASN THR ALA TYR LEU GLN MET ASN SER LEU ARG SEQRES 28 H 490 ALA GLU ASP THR ALA VAL TYR TYR CYS ALA ARG TRP GLY SEQRES 29 H 490 TYR TRP PRO GLY GLU PRO TRP TRP LYS ALA PHE ASP TYR SEQRES 30 H 490 TRP GLY GLN GLY THR LEU VAL THR VAL SER SER ALA SER SEQRES 31 H 490 THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER SEQRES 32 H 490 LYS SER THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU SEQRES 33 H 490 VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP SEQRES 34 H 490 ASN SER GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO SEQRES 35 H 490 ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SER SEQRES 36 H 490 VAL VAL THR VAL PRO SER SER SER LEU GLY THR GLN THR SEQRES 37 H 490 TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS SEQRES 38 H 490 VAL ASP LYS LYS VAL GLU PRO LYS SER SEQRES 1 N 122 GLY SER GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU SEQRES 2 N 122 VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SEQRES 3 N 122 SER GLY ARG THR ILE SER ARG TYR ALA MET SER TRP PHE SEQRES 4 N 122 ARG GLN ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA VAL SEQRES 5 N 122 ALA ARG ARG SER GLY ASP GLY ALA PHE TYR ALA ASP SER SEQRES 6 N 122 VAL GLN GLY ARG PHE THR VAL SER ARG ASP ASP ALA LYS SEQRES 7 N 122 THR VAL TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP SEQRES 8 N 122 THR ALA VAL TYR TYR CYS ALA ILE ASP SER ASP THR PHE SEQRES 9 N 122 TYR SER GLY SER TYR ASP TYR TRP GLY GLN GLY THR GLN SEQRES 10 N 122 VAL THR VAL SER SER SEQRES 1 L 214 MET ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER SEQRES 2 L 214 ALA SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SEQRES 3 L 214 SER GLN SER VAL SER SER ALA VAL ALA TRP TYR GLN GLN SEQRES 4 L 214 LYS PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR SER ALA SEQRES 5 L 214 SER SER LEU TYR SER GLY VAL PRO SER ARG PHE SER GLY SEQRES 6 L 214 SER ARG SER GLY THR ASP PHE THR LEU THR ILE SER SER SEQRES 7 L 214 LEU GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN SEQRES 8 L 214 TYR LEU TYR TYR SER LEU VAL THR PHE GLY GLN GLY THR SEQRES 9 L 214 LYS VAL GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL SEQRES 10 L 214 PHE ILE PHE PRO PRO SER ASP SER GLN LEU LYS SER GLY SEQRES 11 L 214 THR ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO SEQRES 12 L 214 ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU SEQRES 13 L 214 GLN SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SEQRES 14 L 214 SER LYS ASP SER THR TYR SER LEU SER SER THR LEU THR SEQRES 15 L 214 LEU SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA SEQRES 16 L 214 CYS GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR SEQRES 17 L 214 LYS SER PHE ASN ARG GLY HET ZOB R 601 62 HETNAM ZOB 6-{[(3,5-DIFLUOROPYRIDIN-4-YL)METHYL]AMINO}-N-(4- HETNAM 2 ZOB ETHOXY-6-METHYLPYRIMIDIN-2-YL)-2-METHOXY-N-(2- HETNAM 3 ZOB METHOXYETHYL)PYRIDINE-3-SULFONAMIDE FORMUL 5 ZOB C22 H26 F2 N6 O5 S FORMUL 6 HOH *(H2 O) HELIX 1 AA1 ALA R 54 LYS R 78 1 25 HELIX 2 AA2 PHE R 85 LEU R 108 1 24 HELIX 3 AA3 ARG R 125 HIS R 155 1 31 HELIX 4 AA4 PRO R 156 GLU R 160 5 5 HELIX 5 AA5 THR R 164 VAL R 185 1 22 HELIX 6 AA6 PRO R 186 LEU R 188 5 3 HELIX 7 AA7 LEU R 216 LYS R 266 1 51 HELIX 8 AA8 ASN R 269 GLN R 288 1 20 HELIX 9 AA9 SER R 302 ALA R 326 1 25 HELIX 10 AB1 VAL R 331 ILE R 349 1 19 HELIX 11 AB2 LYS R 365 ALA R 392 1 28 HELIX 12 AB3 VAL R 403 CYS R 424 1 22 HELIX 13 AB4 ARG H 90 THR H 94 5 5 HELIX 14 AB5 GLY H 107 LYS H 112 1 6 HELIX 15 AB6 SER H 202 GLN H 206 5 5 HELIX 16 AB7 ARG N 53 ASP N 56 5 4 HELIX 17 AB8 GLN L 80 PHE L 84 5 5 HELIX 18 AB9 SER L 123 GLY L 130 1 8 HELIX 19 AC1 SER L 184 GLU L 189 1 6 SHEET 1 AA1 4 GLN H 6 SER H 10 0 SHEET 2 AA1 4 LEU H 21 SER H 28 -1 O ALA H 26 N VAL H 8 SHEET 3 AA1 4 THR H 81 MET H 86 -1 O MET H 86 N LEU H 21 SHEET 4 AA1 4 PHE H 71 ASP H 76 -1 N THR H 72 O GLN H 85 SHEET 1 AA2 6 LEU H 14 VAL H 15 0 SHEET 2 AA2 6 THR H 121 VAL H 125 1 O THR H 124 N VAL H 15 SHEET 3 AA2 6 ALA H 95 TRP H 102 -1 N TYR H 97 O THR H 121 SHEET 4 AA2 6 SER H 36 GLN H 42 -1 N SER H 36 O TRP H 102 SHEET 5 AA2 6 LEU H 48 SER H 55 -1 O VAL H 51 N TRP H 39 SHEET 6 AA2 6 SER H 60 TYR H 63 -1 O SER H 60 N SER H 55 SHEET 1 AA3 4 LEU H 14 VAL H 15 0 SHEET 2 AA3 4 THR H 121 VAL H 125 1 O THR H 124 N VAL H 15 SHEET 3 AA3 4 ALA H 95 TRP H 102 -1 N TYR H 97 O THR H 121 SHEET 4 AA3 4 TYR H 116 TRP H 117 -1 O TYR H 116 N ARG H 101 SHEET 1 AA4 4 SER H 134 LEU H 138 0 SHEET 2 AA4 4 THR H 149 TYR H 159 -1 O LEU H 155 N PHE H 136 SHEET 3 AA4 4 TYR H 190 PRO H 199 -1 O LEU H 192 N VAL H 156 SHEET 4 AA4 4 HIS H 178 THR H 179 -1 N HIS H 178 O VAL H 195 SHEET 1 AA5 4 SER H 134 LEU H 138 0 SHEET 2 AA5 4 THR H 149 TYR H 159 -1 O LEU H 155 N PHE H 136 SHEET 3 AA5 4 TYR H 190 PRO H 199 -1 O LEU H 192 N VAL H 156 SHEET 4 AA5 4 VAL H 183 LEU H 184 -1 N VAL H 183 O SER H 191 SHEET 1 AA6 3 VAL H 164 TRP H 168 0 SHEET 2 AA6 3 TYR H 208 HIS H 214 -1 O ASN H 211 N SER H 167 SHEET 3 AA6 3 THR H 219 VAL H 225 -1 O THR H 219 N HIS H 214 SHEET 1 AA7 4 LEU N 4 SER N 7 0 SHEET 2 AA7 4 LEU N 20 ALA N 24 -1 O SER N 21 N SER N 7 SHEET 3 AA7 4 THR N 77 GLN N 81 -1 O LEU N 80 N LEU N 20 SHEET 4 AA7 4 THR N 69 SER N 71 -1 N THR N 69 O GLN N 81 SHEET 1 AA8 6 GLY N 10 VAL N 12 0 SHEET 2 AA8 6 THR N 114 VAL N 118 1 O THR N 117 N GLY N 10 SHEET 3 AA8 6 ALA N 91 ASP N 98 -1 N TYR N 93 O THR N 114 SHEET 4 AA8 6 ALA N 33 ARG N 38 -1 N ALA N 33 O ASP N 98 SHEET 5 AA8 6 GLU N 46 ALA N 51 -1 O GLU N 46 N ARG N 38 SHEET 6 AA8 6 ALA N 58 TYR N 60 -1 O PHE N 59 N VAL N 50 SHEET 1 AA9 4 MET L 5 GLN L 7 0 SHEET 2 AA9 4 THR L 21 ALA L 26 -1 O ARG L 25 N THR L 6 SHEET 3 AA9 4 ASP L 71 ILE L 76 -1 O PHE L 72 N CYS L 24 SHEET 4 AA9 4 PHE L 63 SER L 68 -1 N SER L 64 O THR L 75 SHEET 1 AB1 5 SER L 11 ALA L 14 0 SHEET 2 AB1 5 THR L 104 ILE L 108 1 O GLU L 107 N LEU L 12 SHEET 3 AB1 5 THR L 86 TYR L 88 -1 N TYR L 87 O THR L 104 SHEET 4 AB1 5 TRP L 36 GLN L 39 -1 N GLN L 39 O THR L 86 SHEET 5 AB1 5 LYS L 46 ILE L 49 -1 O LYS L 46 N GLN L 38 SHEET 1 AB2 2 GLN L 90 TYR L 92 0 SHEET 2 AB2 2 VAL L 98 PHE L 100 -1 O THR L 99 N GLN L 91 SHEET 1 AB3 4 SER L 116 PHE L 120 0 SHEET 2 AB3 4 ALA L 132 PHE L 141 -1 O VAL L 135 N PHE L 120 SHEET 3 AB3 4 TYR L 175 LEU L 183 -1 O LEU L 177 N LEU L 138 SHEET 4 AB3 4 SER L 161 VAL L 165 -1 N GLN L 162 O THR L 180 SHEET 1 AB4 3 ALA L 146 VAL L 152 0 SHEET 2 AB4 3 VAL L 193 HIS L 200 -1 O GLU L 197 N GLN L 149 SHEET 3 AB4 3 VAL L 207 ASN L 212 -1 O VAL L 207 N VAL L 198 SSBOND 1 CYS R 380 CYS R 414 1555 1555 2.02 SSBOND 2 CYS H 25 CYS H 99 1555 1555 2.03 SSBOND 3 CYS H 154 CYS H 210 1555 1555 2.03 SSBOND 4 CYS N 22 CYS N 95 1555 1555 2.04 SSBOND 5 CYS L 24 CYS L 89 1555 1555 2.04 SSBOND 6 CYS L 136 CYS L 196 1555 1555 2.04 CISPEP 1 TRP H 105 PRO H 106 0 -2.37 CISPEP 2 TYR L 142 PRO L 143 0 -1.56 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