HEADER MEMBRANE PROTEIN 26-JUN-24 9IK9 TITLE CRYO-EM STRUCTURE OF SST ANALOGS BOND SSTR1-GI COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I) SUBUNIT ALPHA-1; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: ADENYLATE CYCLASE-INHIBITING G ALPHA PROTEIN; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(T) SUBUNIT COMPND 8 BETA-1; COMPND 9 CHAIN: B; COMPND 10 SYNONYM: TRANSDUCIN BETA CHAIN 1; COMPND 11 ENGINEERED: YES; COMPND 12 MOL_ID: 3; COMPND 13 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(O) SUBUNIT COMPND 14 GAMMA-2; COMPND 15 CHAIN: C; COMPND 16 SYNONYM: G GAMMA-I; COMPND 17 ENGINEERED: YES; COMPND 18 MOL_ID: 4; COMPND 19 MOLECULE: SCFV16; COMPND 20 CHAIN: E; COMPND 21 ENGINEERED: YES; COMPND 22 MOL_ID: 5; COMPND 23 MOLECULE: SOMATOSTATIN RECEPTOR TYPE 1; COMPND 24 CHAIN: D; COMPND 25 SYNONYM: SS-1-R,SS1-R,SS1R,SST1,SRIF-2; COMPND 26 ENGINEERED: YES; COMPND 27 MOL_ID: 6; COMPND 28 MOLECULE: (4J2)(DCY)(DTY)(DTR)K(DVA)(DCY)(ALO)(NH2); COMPND 29 CHAIN: F; COMPND 30 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: GNAI1; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_COMMON: HUMAN; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 GENE: GNB1; SOURCE 13 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 15 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 17 ORGANISM_COMMON: HUMAN; SOURCE 18 ORGANISM_TAXID: 9606; SOURCE 19 GENE: GNG2; SOURCE 20 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 21 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 22 MOL_ID: 4; SOURCE 23 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT; SOURCE 24 ORGANISM_TAXID: 32630; SOURCE 25 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 26 EXPRESSION_SYSTEM_TAXID: 7111; SOURCE 27 MOL_ID: 5; SOURCE 28 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 29 ORGANISM_COMMON: HUMAN; SOURCE 30 ORGANISM_TAXID: 9606; SOURCE 31 GENE: SSTR1; SOURCE 32 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 33 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 34 MOL_ID: 6; SOURCE 35 SYNTHETIC: YES; SOURCE 36 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT; SOURCE 37 ORGANISM_TAXID: 32630 KEYWDS SSTR1, SST ANALOGS, MEMBRANE PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR T.S.WONG,Z.C.ZENG,T.T.XIONG,S.Y.GAN,Y.DU REVDAT 1 30-APR-25 9IK9 0 JRNL AUTH Z.ZENG,Q.LIAO,S.GAN,X.LI,T.XIONG,L.XU,D.LI,Y.JIANG,J.CHEN, JRNL AUTH 2 R.YE,Y.DU,T.WONG JRNL TITL STRUCTURAL INSIGHTS INTO THE BINDING MODES OF LANREOTIDE AND JRNL TITL 2 PASIREOTIDE WITH SOMATOSTATIN RECEPTOR 1 JRNL REF ACTA PHARM SIN B 2025 JRNL REFN ESSN 2211-3843 JRNL DOI 10.1016/J.APSB.2025.03.043 REMARK 2 REMARK 2 RESOLUTION. 3.37 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) : 3.370 REMARK 3 NUMBER OF PARTICLES : 217201 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 9IK9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 28-JUN-24. REMARK 100 THE DEPOSITION ID IS D_1300048985. 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 : CRYO-EM STRUCTURE OF SST REMARK 245 ANALOGS BIND SSTR1-GI COMPLEX 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 BIOQUANTUM (6K X REMARK 245 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1000.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 1400.00 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) : 5360.00 REMARK 245 ILLUMINATION MODE : OTHER REMARK 245 NOMINAL MAGNIFICATION : NULL REMARK 245 CALIBRATED MAGNIFICATION : NULL REMARK 245 SOURCE : OTHER 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 APPLY THE FOLLOWING TO CHAINS: A, B, C, E, D, 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 ILE A 56 REMARK 465 HIS A 57 REMARK 465 GLU A 58 REMARK 465 ALA A 59 REMARK 465 GLY A 60 REMARK 465 TYR A 61 REMARK 465 SER A 62 REMARK 465 GLU A 63 REMARK 465 GLU A 64 REMARK 465 GLU A 65 REMARK 465 CYS A 66 REMARK 465 LYS A 67 REMARK 465 GLN A 68 REMARK 465 TYR A 69 REMARK 465 LYS A 70 REMARK 465 ALA A 71 REMARK 465 VAL A 72 REMARK 465 VAL A 73 REMARK 465 TYR A 74 REMARK 465 SER A 75 REMARK 465 ASN A 76 REMARK 465 THR A 77 REMARK 465 ILE A 78 REMARK 465 GLN A 79 REMARK 465 SER A 80 REMARK 465 ILE A 81 REMARK 465 ILE A 82 REMARK 465 ALA A 83 REMARK 465 ILE A 84 REMARK 465 ILE A 85 REMARK 465 ARG A 86 REMARK 465 ALA A 87 REMARK 465 MET A 88 REMARK 465 GLY A 89 REMARK 465 ARG A 90 REMARK 465 LEU A 91 REMARK 465 LYS A 92 REMARK 465 ILE A 93 REMARK 465 ASP A 94 REMARK 465 PHE A 95 REMARK 465 GLY A 96 REMARK 465 ASP A 97 REMARK 465 SER A 98 REMARK 465 ALA A 99 REMARK 465 ARG A 100 REMARK 465 ALA A 101 REMARK 465 ASP A 102 REMARK 465 ASP A 103 REMARK 465 ALA A 104 REMARK 465 ARG A 105 REMARK 465 GLN A 106 REMARK 465 LEU A 107 REMARK 465 PHE A 108 REMARK 465 VAL A 109 REMARK 465 LEU A 110 REMARK 465 ALA A 111 REMARK 465 GLY A 112 REMARK 465 ALA A 113 REMARK 465 ALA A 114 REMARK 465 GLU A 115 REMARK 465 GLU A 116 REMARK 465 GLY A 117 REMARK 465 PHE A 118 REMARK 465 MET A 119 REMARK 465 THR A 120 REMARK 465 ALA A 121 REMARK 465 GLU A 122 REMARK 465 LEU A 123 REMARK 465 ALA A 124 REMARK 465 GLY A 125 REMARK 465 VAL A 126 REMARK 465 ILE A 127 REMARK 465 LYS A 128 REMARK 465 ARG A 129 REMARK 465 LEU A 130 REMARK 465 TRP A 131 REMARK 465 LYS A 132 REMARK 465 ASP A 133 REMARK 465 SER A 134 REMARK 465 GLY A 135 REMARK 465 VAL A 136 REMARK 465 GLN A 137 REMARK 465 ALA A 138 REMARK 465 CYS A 139 REMARK 465 PHE A 140 REMARK 465 ASN A 141 REMARK 465 ARG A 142 REMARK 465 SER A 143 REMARK 465 ARG A 144 REMARK 465 GLU A 145 REMARK 465 TYR A 146 REMARK 465 GLN A 147 REMARK 465 LEU A 148 REMARK 465 ASN A 149 REMARK 465 ASP A 150 REMARK 465 SER A 151 REMARK 465 ALA A 152 REMARK 465 ALA A 153 REMARK 465 TYR A 154 REMARK 465 TYR A 155 REMARK 465 LEU A 156 REMARK 465 ASN A 157 REMARK 465 ASP A 158 REMARK 465 LEU A 159 REMARK 465 ASP A 160 REMARK 465 ARG A 161 REMARK 465 ILE A 162 REMARK 465 ALA A 163 REMARK 465 GLN A 164 REMARK 465 PRO A 165 REMARK 465 ASN A 166 REMARK 465 TYR A 167 REMARK 465 ILE A 168 REMARK 465 PRO A 169 REMARK 465 THR A 170 REMARK 465 GLN A 171 REMARK 465 GLN A 172 REMARK 465 ASP A 173 REMARK 465 VAL A 174 REMARK 465 LEU A 175 REMARK 465 ARG A 176 REMARK 465 THR A 177 REMARK 465 ARG A 178 REMARK 465 VAL A 179 REMARK 465 LYS A 180 REMARK 465 THR A 181 REMARK 465 LEU A 234 REMARK 465 ALA A 235 REMARK 465 GLU A 236 REMARK 465 ASP A 237 REMARK 465 GLU A 238 REMARK 465 GLU A 239 REMARK 465 MET A 240 REMARK 465 MET B -21 REMARK 465 HIS B -20 REMARK 465 HIS B -19 REMARK 465 HIS B -18 REMARK 465 HIS B -17 REMARK 465 HIS B -16 REMARK 465 HIS B -15 REMARK 465 HIS B -14 REMARK 465 HIS B -13 REMARK 465 HIS B -12 REMARK 465 HIS B -11 REMARK 465 LEU B -10 REMARK 465 GLU B -9 REMARK 465 VAL B -8 REMARK 465 LEU B -7 REMARK 465 PHE B -6 REMARK 465 GLN B -5 REMARK 465 GLY B -4 REMARK 465 PRO B -3 REMARK 465 GLY B -2 REMARK 465 SER B -1 REMARK 465 SER B 0 REMARK 465 GLY B 1 REMARK 465 SER B 2 REMARK 465 GLU B 3 REMARK 465 LEU B 4 REMARK 465 VAL B 341 REMARK 465 SER B 342 REMARK 465 GLY B 343 REMARK 465 TRP B 344 REMARK 465 ARG B 345 REMARK 465 LEU B 346 REMARK 465 PHE B 347 REMARK 465 LYS B 348 REMARK 465 LYS B 349 REMARK 465 ILE B 350 REMARK 465 SER B 351 REMARK 465 MET C 1 REMARK 465 ALA C 2 REMARK 465 SER C 3 REMARK 465 ASN C 4 REMARK 465 ASN C 5 REMARK 465 THR C 6 REMARK 465 ALA C 7 REMARK 465 SER C 8 REMARK 465 ARG C 62 REMARK 465 GLU C 63 REMARK 465 LYS C 64 REMARK 465 LYS C 65 REMARK 465 PHE C 66 REMARK 465 PHE C 67 REMARK 465 CYS C 68 REMARK 465 ALA C 69 REMARK 465 ILE C 70 REMARK 465 LEU C 71 REMARK 465 GLY E 121A REMARK 465 GLY E 121B REMARK 465 GLY E 121C REMARK 465 GLY E 121D REMARK 465 SER E 121E REMARK 465 GLY E 121F REMARK 465 GLY E 121G REMARK 465 GLY E 121H REMARK 465 GLY E 121I REMARK 465 SER E 121J REMARK 465 GLY E 121K REMARK 465 GLY E 121L REMARK 465 GLY E 121M REMARK 465 GLY E 121N REMARK 465 SER E 236 REMARK 465 ILE E 237 REMARK 465 SER E 238 REMARK 465 CYS E 239 REMARK 465 ARG E 240 REMARK 465 SER E 241 REMARK 465 SER E 242 REMARK 465 LYS E 243 REMARK 465 SER E 244 REMARK 465 LEU E 245 REMARK 465 LEU E 246 REMARK 465 HIS E 247 REMARK 465 SER E 248 REMARK 465 ASN E 249 REMARK 465 GLY E 250 REMARK 465 ASN E 251 REMARK 465 THR E 252 REMARK 465 TYR E 253 REMARK 465 LEU E 254 REMARK 465 TYR E 255 REMARK 465 TRP E 256 REMARK 465 PHE E 257 REMARK 465 LEU E 258 REMARK 465 GLN E 259 REMARK 465 ARG E 260 REMARK 465 PRO E 261 REMARK 465 GLY E 262 REMARK 465 GLN E 263 REMARK 465 SER E 264 REMARK 465 PRO E 265 REMARK 465 GLN E 266 REMARK 465 LEU E 267 REMARK 465 LEU E 268 REMARK 465 ILE E 269 REMARK 465 TYR E 270 REMARK 465 ARG E 271 REMARK 465 MET E 272 REMARK 465 SER E 273 REMARK 465 ASN E 274 REMARK 465 LEU E 275 REMARK 465 ALA E 276 REMARK 465 SER E 277 REMARK 465 GLY E 278 REMARK 465 VAL E 279 REMARK 465 PRO E 280 REMARK 465 ASP E 281 REMARK 465 ARG E 282 REMARK 465 PHE E 283 REMARK 465 SER E 284 REMARK 465 GLY E 285 REMARK 465 SER E 286 REMARK 465 GLY E 287 REMARK 465 SER E 288 REMARK 465 GLY E 289 REMARK 465 THR E 290 REMARK 465 ALA E 291 REMARK 465 PHE E 292 REMARK 465 THR E 293 REMARK 465 LEU E 294 REMARK 465 THR E 295 REMARK 465 ILE E 296 REMARK 465 SER E 297 REMARK 465 ARG E 298 REMARK 465 LEU E 299 REMARK 465 GLU E 300 REMARK 465 ALA E 301 REMARK 465 GLU E 302 REMARK 465 ASP E 303 REMARK 465 VAL E 304 REMARK 465 GLY E 305 REMARK 465 VAL E 306 REMARK 465 TYR E 307 REMARK 465 TYR E 308 REMARK 465 CYS E 309 REMARK 465 MET E 310 REMARK 465 GLN E 311 REMARK 465 HIS E 312 REMARK 465 LEU E 313 REMARK 465 GLU E 314 REMARK 465 TYR E 315 REMARK 465 PRO E 316 REMARK 465 LEU E 317 REMARK 465 THR E 318 REMARK 465 PHE E 319 REMARK 465 GLY E 320 REMARK 465 ALA E 321 REMARK 465 GLY E 322 REMARK 465 THR E 323 REMARK 465 LYS E 324 REMARK 465 LEU E 325 REMARK 465 GLU E 326 REMARK 465 LEU E 327 REMARK 465 MET D 1 REMARK 465 PHE D 2 REMARK 465 PRO D 3 REMARK 465 ASN D 4 REMARK 465 GLY D 5 REMARK 465 THR D 6 REMARK 465 ALA D 7 REMARK 465 SER D 8 REMARK 465 SER D 9 REMARK 465 PRO D 10 REMARK 465 SER D 11 REMARK 465 SER D 12 REMARK 465 SER D 13 REMARK 465 PRO D 14 REMARK 465 SER D 15 REMARK 465 PRO D 16 REMARK 465 SER D 17 REMARK 465 PRO D 18 REMARK 465 GLY D 19 REMARK 465 SER D 20 REMARK 465 CYS D 21 REMARK 465 GLY D 22 REMARK 465 GLU D 23 REMARK 465 GLY D 24 REMARK 465 GLY D 25 REMARK 465 GLY D 26 REMARK 465 SER D 27 REMARK 465 ARG D 28 REMARK 465 GLY D 29 REMARK 465 PRO D 30 REMARK 465 GLY D 31 REMARK 465 ALA D 32 REMARK 465 GLY D 33 REMARK 465 ALA D 34 REMARK 465 ALA D 35 REMARK 465 ASP D 36 REMARK 465 GLY D 37 REMARK 465 MET D 38 REMARK 465 GLU D 39 REMARK 465 GLU D 40 REMARK 465 PRO D 41 REMARK 465 GLY D 42 REMARK 465 ARG D 43 REMARK 465 ASN D 44 REMARK 465 ALA D 45 REMARK 465 SER D 46 REMARK 465 GLN D 47 REMARK 465 ASN D 48 REMARK 465 GLY D 49 REMARK 465 THR D 50 REMARK 465 LEU D 51 REMARK 465 SER D 52 REMARK 465 GLU D 53 REMARK 465 GLY D 54 REMARK 465 GLN D 55 REMARK 465 GLY D 56 REMARK 465 ALA D 200 REMARK 465 ASN D 201 REMARK 465 SER D 202 REMARK 465 ASP D 203 REMARK 465 GLY D 204 REMARK 465 THR D 205 REMARK 465 VAL D 206 REMARK 465 ALA D 347 REMARK 465 GLU D 348 REMARK 465 GLU D 349 REMARK 465 PRO D 350 REMARK 465 VAL D 351 REMARK 465 ASP D 352 REMARK 465 TYR D 353 REMARK 465 TYR D 354 REMARK 465 ALA D 355 REMARK 465 THR D 356 REMARK 465 ALA D 357 REMARK 465 LEU D 358 REMARK 465 LYS D 359 REMARK 465 SER D 360 REMARK 465 ARG D 361 REMARK 465 ALA D 362 REMARK 465 TYR D 363 REMARK 465 SER D 364 REMARK 465 VAL D 365 REMARK 465 GLU D 366 REMARK 465 ASP D 367 REMARK 465 PHE D 368 REMARK 465 GLN D 369 REMARK 465 PRO D 370 REMARK 465 GLU D 371 REMARK 465 ASN D 372 REMARK 465 LEU D 373 REMARK 465 GLU D 374 REMARK 465 SER D 375 REMARK 465 GLY D 376 REMARK 465 GLY D 377 REMARK 465 VAL D 378 REMARK 465 PHE D 379 REMARK 465 ARG D 380 REMARK 465 ASN D 381 REMARK 465 GLY D 382 REMARK 465 THR D 383 REMARK 465 CYS D 384 REMARK 465 THR D 385 REMARK 465 SER D 386 REMARK 465 ARG D 387 REMARK 465 ILE D 388 REMARK 465 THR D 389 REMARK 465 THR D 390 REMARK 465 LEU D 391 REMARK 465 LEU D 392 REMARK 465 GLU D 393 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 ASP A 26 CG OD1 OD2 REMARK 470 GLU A 28 CG CD OE1 OE2 REMARK 470 GLU A 43 CG CD OE1 OE2 REMARK 470 LYS A 46 CG CD CE NZ REMARK 470 ILE A 55 CG1 CG2 CD1 REMARK 470 GLU A 186 CG CD OE1 OE2 REMARK 470 ASP A 193 CG OD1 OD2 REMARK 470 GLU A 207 CG CD OE1 OE2 REMARK 470 ASP A 229 CG OD1 OD2 REMARK 470 LEU A 232 CG CD1 CD2 REMARK 470 VAL A 233 CG1 CG2 REMARK 470 LYS A 248 CG CD CE NZ REMARK 470 LYS A 257 CG CD CE NZ REMARK 470 ASP A 272 CG OD1 OD2 REMARK 470 LYS A 277 CG CD CE NZ REMARK 470 LYS A 279 CG CD CE NZ REMARK 470 LYS A 280 CG CD CE NZ REMARK 470 SER A 281 OG REMARK 470 LEU A 283 CG CD1 CD2 REMARK 470 GLU A 289 CG CD OE1 OE2 REMARK 470 GLU A 297 CG CD OE1 OE2 REMARK 470 ASP A 315 CG OD1 OD2 REMARK 470 GLU A 318 CG CD OE1 OE2 REMARK 470 THR A 327 OG1 CG2 REMARK 470 ASP A 328 CG OD1 OD2 REMARK 470 ASP A 350 CG OD1 OD2 REMARK 470 ASP B 5 CG OD1 OD2 REMARK 470 GLN B 6 CG CD OE1 NE2 REMARK 470 ARG B 8 CG CD NE CZ NH1 NH2 REMARK 470 ILE B 18 CG1 CG2 CD1 REMARK 470 ARG B 19 CG CD NE CZ NH1 NH2 REMARK 470 LYS B 23 CG CD CE NZ REMARK 470 CYS B 25 SG REMARK 470 GLN B 32 CG CD OE1 NE2 REMARK 470 ASN B 36 CG OD1 ND2 REMARK 470 ASP B 38 CG OD1 OD2 REMARK 470 GLU B 130 CG CD OE1 OE2 REMARK 470 ARG B 214 CG CD NE CZ NH1 NH2 REMARK 470 MET B 217 CG SD CE REMARK 470 ASN B 237 CG OD1 ND2 REMARK 470 ASP B 312 CG OD1 OD2 REMARK 470 ASN B 340 CG OD1 ND2 REMARK 470 GLN C 11 CG CD OE1 NE2 REMARK 470 LYS C 14 CG CD CE NZ REMARK 470 GLU C 17 CG CD OE1 OE2 REMARK 470 GLN C 18 CG CD OE1 NE2 REMARK 470 LYS C 20 CG CD CE NZ REMARK 470 ASP C 26 CG OD1 OD2 REMARK 470 ASP C 48 CG OD1 OD2 REMARK 470 GLU C 58 CG CD OE1 OE2 REMARK 470 SER E 17 OG REMARK 470 GLU E 42 CG CD OE1 OE2 REMARK 470 SER E 52 OG REMARK 470 ASP E 73 CG OD1 OD2 REMARK 470 GLU E 89 CG CD OE1 OE2 REMARK 470 SER E 121 OG REMARK 470 SER E 124 OG REMARK 470 GLU E 141 CG CD OE1 OE2 REMARK 470 MET E 180 CG SD CE REMARK 470 ASP E 189 CG OD1 OD2 REMARK 470 THR E 198 OG1 CG2 REMARK 470 GLU E 210 CG CD OE1 OE2 REMARK 470 GLU E 234 CG CD OE1 OE2 REMARK 470 PHE D 195 CG CD1 CD2 CE1 CE2 CZ REMARK 470 MET D 212 CG SD CE REMARK 470 GLN D 217 CG CD OE1 NE2 REMARK 470 ARG D 218 CG CD NE CZ NH1 NH2 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 HE2 PHE D 223 HZ2 DTR F 4 1.19 REMARK 500 OD1 ASP B 205 HG SER B 207 1.31 REMARK 500 O ALA B 287 HG CYS B 294 1.32 REMARK 500 O ARG D 264 HG SER D 265 1.37 REMARK 500 O ASP B 333 HG SER B 334 1.37 REMARK 500 OE1 GLU E 6 H GLY E 114 1.40 REMARK 500 O THR B 29 H GLN B 32 1.41 REMARK 500 O PHE E 29 HH22 ARG E 72 1.43 REMARK 500 O ASN D 319 H LEU D 322 1.44 REMARK 500 HH12 ARG E 67 OD2 ASP E 90 1.44 REMARK 500 OE1 GLN E 130 H GLY E 230 1.46 REMARK 500 O GLY E 193 HG SER E 194 1.48 REMARK 500 O SER E 133 HG SER E 134 1.49 REMARK 500 O LEU D 119 HH11 ARG D 121 1.51 REMARK 500 O LEU D 233 H GLY D 237 1.52 REMARK 500 OD1 ASN B 313 H ARG B 314 1.53 REMARK 500 O THR B 86 HG1 THR B 87 1.54 REMARK 500 O ARG A 24 H GLY A 27 1.54 REMARK 500 HG SER E 149 O LYS E 151 1.55 REMARK 500 O GLY E 56 HG1 THR E 57 1.56 REMARK 500 O PHE D 63 HG SER D 66 1.58 REMARK 500 O LEU D 311 H ALA D 314 1.59 REMARK 500 O PHE E 29 NH2 ARG E 72 2.03 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS 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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) 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 RES CSSEQI ATM2 DEVIATION REMARK 500 4J2 F 1 C DCY F 2 N 0.157 REMARK 500 DTY F 3 CG DTY F 3 CD2 0.136 REMARK 500 DTY F 3 CG DTY F 3 CD1 -0.085 REMARK 500 DTY F 3 CD1 DTY F 3 CE1 0.147 REMARK 500 DTY F 3 CZ DTY F 3 CE2 0.140 REMARK 500 DTY F 3 C DTR F 4 N 0.165 REMARK 500 DTR F 4 C LYS F 5 N 0.165 REMARK 500 LYS F 5 C DVA F 6 N 0.155 REMARK 500 DCY F 7 C ALO F 8 N 0.141 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 DTR F 4 CD1 - NE1 - CE2 ANGL. DEV. = 11.9 DEGREES REMARK 500 DTR F 4 NE1 - CE2 - CZ2 ANGL. DEV. = 6.7 DEGREES REMARK 500 DTR F 4 CE2 - CD2 - CG ANGL. DEV. = -5.1 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 ALA A 7 -69.41 -106.36 REMARK 500 GLU A 43 55.09 39.12 REMARK 500 SER A 44 -61.08 -94.89 REMARK 500 CYS A 254 7.28 -69.38 REMARK 500 SER A 263 -178.74 -68.00 REMARK 500 ASP A 328 -5.15 75.06 REMARK 500 THR A 329 67.04 -163.23 REMARK 500 ASP B 27 23.87 -140.30 REMARK 500 MET B 101 29.08 -140.02 REMARK 500 CYS B 114 -168.33 -126.42 REMARK 500 GLU B 130 -5.26 92.88 REMARK 500 ALA B 248 -1.41 70.19 REMARK 500 PHE B 292 -1.14 75.35 REMARK 500 ASN B 293 -168.50 -127.19 REMARK 500 CYS B 294 -166.71 -125.93 REMARK 500 ALA B 302 -3.96 74.00 REMARK 500 LEU B 318 146.48 -171.81 REMARK 500 MET B 325 6.25 -69.70 REMARK 500 SER B 334 41.22 70.43 REMARK 500 PRO C 49 -6.49 -57.05 REMARK 500 ASN C 59 71.09 -161.17 REMARK 500 PRO C 60 2.14 -64.78 REMARK 500 SER E 106 69.33 -156.86 REMARK 500 SER E 134 143.41 -171.41 REMARK 500 PRO E 139 153.30 -46.72 REMARK 500 GLN E 167 110.48 -161.62 REMARK 500 ARG E 179 32.61 72.11 REMARK 500 MET E 180 -10.95 72.32 REMARK 500 SER E 181 -36.18 -132.03 REMARK 500 THR E 198 -0.95 82.92 REMARK 500 GLU E 210 -1.07 78.29 REMARK 500 PRO E 224 -168.63 -72.86 REMARK 500 LYS D 88 69.26 61.60 REMARK 500 LYS D 90 -52.51 -120.19 REMARK 500 LEU D 119 -60.42 -96.69 REMARK 500 TRP D 123 79.91 -113.49 REMARK 500 PRO D 124 46.64 -79.45 REMARK 500 PHE D 232 -33.99 -144.27 REMARK 500 CYS D 242 3.67 -67.12 REMARK 500 LYS D 256 36.13 -98.85 REMARK 500 GLN D 261 -163.50 -77.86 REMARK 500 ARG D 262 122.52 -37.33 REMARK 500 SER D 265 -11.96 74.75 REMARK 500 LYS F 5 39.01 37.71 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-60651 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF SST ANALOGS BOND SSTR1-GI COMPLEX DBREF 9IK9 A 5 354 UNP P63096 GNAI1_HUMAN 5 354 DBREF 9IK9 B 2 340 UNP P62873 GBB1_HUMAN 2 340 DBREF 9IK9 C 1 71 UNP P59768 GBG2_HUMAN 1 71 DBREF 9IK9 E 2 327 PDB 9IK9 9IK9 2 327 DBREF 9IK9 D 1 391 UNP P30872 SSR1_HUMAN 1 391 DBREF 9IK9 F 1 9 PDB 9IK9 9IK9 1 9 SEQADV 9IK9 MET B -21 UNP P62873 INITIATING METHIONINE SEQADV 9IK9 HIS B -20 UNP P62873 EXPRESSION TAG SEQADV 9IK9 HIS B -19 UNP P62873 EXPRESSION TAG SEQADV 9IK9 HIS B -18 UNP P62873 EXPRESSION TAG SEQADV 9IK9 HIS B -17 UNP P62873 EXPRESSION TAG SEQADV 9IK9 HIS B -16 UNP P62873 EXPRESSION TAG SEQADV 9IK9 HIS B -15 UNP P62873 EXPRESSION TAG SEQADV 9IK9 HIS B -14 UNP P62873 EXPRESSION TAG SEQADV 9IK9 HIS B -13 UNP P62873 EXPRESSION TAG SEQADV 9IK9 HIS B -12 UNP P62873 EXPRESSION TAG SEQADV 9IK9 HIS B -11 UNP P62873 EXPRESSION TAG SEQADV 9IK9 LEU B -10 UNP P62873 EXPRESSION TAG SEQADV 9IK9 GLU B -9 UNP P62873 EXPRESSION TAG SEQADV 9IK9 VAL B -8 UNP P62873 EXPRESSION TAG SEQADV 9IK9 LEU B -7 UNP P62873 EXPRESSION TAG SEQADV 9IK9 PHE B -6 UNP P62873 EXPRESSION TAG SEQADV 9IK9 GLN B -5 UNP P62873 EXPRESSION TAG SEQADV 9IK9 GLY B -4 UNP P62873 EXPRESSION TAG SEQADV 9IK9 PRO B -3 UNP P62873 EXPRESSION TAG SEQADV 9IK9 GLY B -2 UNP P62873 EXPRESSION TAG SEQADV 9IK9 SER B -1 UNP P62873 EXPRESSION TAG SEQADV 9IK9 SER B 0 UNP P62873 EXPRESSION TAG SEQADV 9IK9 GLY B 1 UNP P62873 EXPRESSION TAG SEQADV 9IK9 VAL B 341 UNP P62873 EXPRESSION TAG SEQADV 9IK9 SER B 342 UNP P62873 EXPRESSION TAG SEQADV 9IK9 GLY B 343 UNP P62873 EXPRESSION TAG SEQADV 9IK9 TRP B 344 UNP P62873 EXPRESSION TAG SEQADV 9IK9 ARG B 345 UNP P62873 EXPRESSION TAG SEQADV 9IK9 LEU B 346 UNP P62873 EXPRESSION TAG SEQADV 9IK9 PHE B 347 UNP P62873 EXPRESSION TAG SEQADV 9IK9 LYS B 348 UNP P62873 EXPRESSION TAG SEQADV 9IK9 LYS B 349 UNP P62873 EXPRESSION TAG SEQADV 9IK9 ILE B 350 UNP P62873 EXPRESSION TAG SEQADV 9IK9 SER B 351 UNP P62873 EXPRESSION TAG SEQADV 9IK9 LEU D 392 UNP P30872 EXPRESSION TAG SEQADV 9IK9 GLU D 393 UNP P30872 EXPRESSION TAG SEQRES 1 A 350 LEU SER ALA GLU ASP LYS ALA ALA VAL GLU ARG SER LYS SEQRES 2 A 350 MET ILE ASP ARG ASN LEU ARG GLU ASP GLY GLU LYS ALA SEQRES 3 A 350 ALA ARG GLU VAL LYS LEU LEU LEU LEU GLY ALA GLY GLU SEQRES 4 A 350 SER GLY LYS SER THR ILE VAL LYS GLN MET LYS ILE ILE SEQRES 5 A 350 HIS GLU ALA GLY TYR SER GLU GLU GLU CYS LYS GLN TYR SEQRES 6 A 350 LYS ALA VAL VAL TYR SER ASN THR ILE GLN SER ILE ILE SEQRES 7 A 350 ALA ILE ILE ARG ALA MET GLY ARG LEU LYS ILE ASP PHE SEQRES 8 A 350 GLY ASP SER ALA ARG ALA ASP ASP ALA ARG GLN LEU PHE SEQRES 9 A 350 VAL LEU ALA GLY ALA ALA GLU GLU GLY PHE MET THR ALA SEQRES 10 A 350 GLU LEU ALA GLY VAL ILE LYS ARG LEU TRP LYS ASP SER SEQRES 11 A 350 GLY VAL GLN ALA CYS PHE ASN ARG SER ARG GLU TYR GLN SEQRES 12 A 350 LEU ASN ASP SER ALA ALA TYR TYR LEU ASN ASP LEU ASP SEQRES 13 A 350 ARG ILE ALA GLN PRO ASN TYR ILE PRO THR GLN GLN ASP SEQRES 14 A 350 VAL LEU ARG THR ARG VAL LYS THR THR GLY ILE VAL GLU SEQRES 15 A 350 THR HIS PHE THR PHE LYS ASP LEU HIS PHE LYS MET PHE SEQRES 16 A 350 ASP VAL GLY GLY GLN ARG SER GLU ARG LYS LYS TRP ILE SEQRES 17 A 350 HIS CYS PHE GLU GLY VAL THR ALA ILE ILE PHE CYS VAL SEQRES 18 A 350 ALA LEU SER ASP TYR ASP LEU VAL LEU ALA GLU ASP GLU SEQRES 19 A 350 GLU MET ASN ARG MET HIS GLU SER MET LYS LEU PHE ASP SEQRES 20 A 350 SER ILE CYS ASN ASN LYS TRP PHE THR ASP THR SER ILE SEQRES 21 A 350 ILE LEU PHE LEU ASN LYS LYS ASP LEU PHE GLU GLU LYS SEQRES 22 A 350 ILE LYS LYS SER PRO LEU THR ILE CYS TYR PRO GLU TYR SEQRES 23 A 350 ALA GLY SER ASN THR TYR GLU GLU ALA ALA ALA TYR ILE SEQRES 24 A 350 GLN CYS GLN PHE GLU ASP LEU ASN LYS ARG LYS ASP THR SEQRES 25 A 350 LYS GLU ILE TYR THR HIS PHE THR CYS ALA THR ASP THR SEQRES 26 A 350 LYS ASN VAL GLN PHE VAL PHE ASP ALA VAL THR ASP VAL SEQRES 27 A 350 ILE ILE LYS ASN ASN LEU LYS ASP CYS GLY LEU PHE SEQRES 1 B 373 MET HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS LEU GLU SEQRES 2 B 373 VAL LEU PHE GLN GLY PRO GLY SER SER GLY SER GLU LEU SEQRES 3 B 373 ASP GLN LEU ARG GLN GLU ALA GLU GLN LEU LYS ASN GLN SEQRES 4 B 373 ILE ARG ASP ALA ARG LYS ALA CYS ALA ASP ALA THR LEU SEQRES 5 B 373 SER GLN ILE THR ASN ASN ILE ASP PRO VAL GLY ARG ILE SEQRES 6 B 373 GLN MET ARG THR ARG ARG THR LEU ARG GLY HIS LEU ALA SEQRES 7 B 373 LYS ILE TYR ALA MET HIS TRP GLY THR ASP SER ARG LEU SEQRES 8 B 373 LEU VAL SER ALA SER GLN ASP GLY LYS LEU ILE ILE TRP SEQRES 9 B 373 ASP SER TYR THR THR ASN LYS VAL HIS ALA ILE PRO LEU SEQRES 10 B 373 ARG SER SER TRP VAL MET THR CYS ALA TYR ALA PRO SER SEQRES 11 B 373 GLY ASN TYR VAL ALA CYS GLY GLY LEU ASP ASN ILE CYS SEQRES 12 B 373 SER ILE TYR ASN LEU LYS THR ARG GLU GLY ASN VAL ARG SEQRES 13 B 373 VAL SER ARG GLU LEU ALA GLY HIS THR GLY TYR LEU SER SEQRES 14 B 373 CYS CYS ARG PHE LEU ASP ASP ASN GLN ILE VAL THR SER SEQRES 15 B 373 SER GLY ASP THR THR CYS ALA LEU TRP ASP ILE GLU THR SEQRES 16 B 373 GLY GLN GLN THR THR THR PHE THR GLY HIS THR GLY ASP SEQRES 17 B 373 VAL MET SER LEU SER LEU ALA PRO ASP THR ARG LEU PHE SEQRES 18 B 373 VAL SER GLY ALA CYS ASP ALA SER ALA LYS LEU TRP ASP SEQRES 19 B 373 VAL ARG GLU GLY MET CYS ARG GLN THR PHE THR GLY HIS SEQRES 20 B 373 GLU SER ASP ILE ASN ALA ILE CYS PHE PHE PRO ASN GLY SEQRES 21 B 373 ASN ALA PHE ALA THR GLY SER ASP ASP ALA THR CYS ARG SEQRES 22 B 373 LEU PHE ASP LEU ARG ALA ASP GLN GLU LEU MET THR TYR SEQRES 23 B 373 SER HIS ASP ASN ILE ILE CYS GLY ILE THR SER VAL SER SEQRES 24 B 373 PHE SER LYS SER GLY ARG LEU LEU LEU ALA GLY TYR ASP SEQRES 25 B 373 ASP PHE ASN CYS ASN VAL TRP ASP ALA LEU LYS ALA ASP SEQRES 26 B 373 ARG ALA GLY VAL LEU ALA GLY HIS ASP ASN ARG VAL SER SEQRES 27 B 373 CYS LEU GLY VAL THR ASP ASP GLY MET ALA VAL ALA THR SEQRES 28 B 373 GLY SER TRP ASP SER PHE LEU LYS ILE TRP ASN VAL SER SEQRES 29 B 373 GLY TRP ARG LEU PHE LYS LYS ILE SER SEQRES 1 C 71 MET ALA SER ASN ASN THR ALA SER ILE ALA GLN ALA ARG SEQRES 2 C 71 LYS LEU VAL GLU GLN LEU LYS MET GLU ALA ASN ILE ASP SEQRES 3 C 71 ARG ILE LYS VAL SER LYS ALA ALA ALA ASP LEU MET ALA SEQRES 4 C 71 TYR CYS GLU ALA HIS ALA LYS GLU ASP PRO LEU LEU THR SEQRES 5 C 71 PRO VAL PRO ALA SER GLU ASN PRO PHE ARG GLU LYS LYS SEQRES 6 C 71 PHE PHE CYS ALA ILE LEU SEQRES 1 E 338 VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN PRO SEQRES 2 E 338 GLY GLY SER ARG LYS LEU SER CYS SER ALA SER GLY PHE SEQRES 3 E 338 ALA PHE SER SER PHE GLY MET HIS TRP VAL ARG GLN ALA SEQRES 4 E 338 PRO GLU LYS GLY LEU GLU TRP VAL ALA TYR ILE SER SER SEQRES 5 E 338 GLY SER GLY THR ILE TYR TYR ALA ASP THR VAL LYS GLY SEQRES 6 E 338 ARG PHE THR ILE SER ARG ASP ASP PRO LYS ASN THR LEU SEQRES 7 E 338 PHE LEU GLN MET THR SER LEU ARG SER GLU ASP THR ALA SEQRES 8 E 338 MET TYR TYR CYS VAL ARG SER ILE TYR TYR TYR GLY SER SEQRES 9 E 338 SER PRO PHE ASP PHE TRP GLY GLN GLY THR THR LEU THR SEQRES 10 E 338 VAL SER SER GLY GLY GLY GLY SER GLY GLY GLY GLY SER SEQRES 11 E 338 GLY GLY GLY GLY SER ASP ILE VAL MET THR GLN ALA THR SEQRES 12 E 338 SER SER VAL PRO VAL THR PRO GLY GLU SER VAL SER ILE SEQRES 13 E 338 SER CYS ARG SER SER LYS SER LEU LEU HIS SER ASN GLY SEQRES 14 E 338 ASN THR TYR LEU TYR TRP PHE LEU GLN ARG PRO GLY GLN SEQRES 15 E 338 SER PRO GLN LEU LEU ILE TYR ARG MET SER ASN LEU ALA SEQRES 16 E 338 SER GLY VAL PRO ASP ARG PHE SER GLY SER GLY SER GLY SEQRES 17 E 338 THR ALA PHE THR LEU THR ILE SER ARG LEU GLU ALA GLU SEQRES 18 E 338 ASP VAL GLY VAL TYR TYR CYS MET GLN HIS LEU GLU TYR SEQRES 19 E 338 PRO LEU THR PHE GLY ALA GLY THR LYS LEU GLU LEU SER SEQRES 20 E 338 ILE SER CYS ARG SER SER LYS SER LEU LEU HIS SER ASN SEQRES 21 E 338 GLY ASN THR TYR LEU TYR TRP PHE LEU GLN ARG PRO GLY SEQRES 22 E 338 GLN SER PRO GLN LEU LEU ILE TYR ARG MET SER ASN LEU SEQRES 23 E 338 ALA SER GLY VAL PRO ASP ARG PHE SER GLY SER GLY SER SEQRES 24 E 338 GLY THR ALA PHE THR LEU THR ILE SER ARG LEU GLU ALA SEQRES 25 E 338 GLU ASP VAL GLY VAL TYR TYR CYS MET GLN HIS LEU GLU SEQRES 26 E 338 TYR PRO LEU THR PHE GLY ALA GLY THR LYS LEU GLU LEU SEQRES 1 D 393 MET PHE PRO ASN GLY THR ALA SER SER PRO SER SER SER SEQRES 2 D 393 PRO SER PRO SER PRO GLY SER CYS GLY GLU GLY GLY GLY SEQRES 3 D 393 SER ARG GLY PRO GLY ALA GLY ALA ALA ASP GLY MET GLU SEQRES 4 D 393 GLU PRO GLY ARG ASN ALA SER GLN ASN GLY THR LEU SER SEQRES 5 D 393 GLU GLY GLN GLY SER ALA ILE LEU ILE SER PHE ILE TYR SEQRES 6 D 393 SER VAL VAL CYS LEU VAL GLY LEU CYS GLY ASN SER MET SEQRES 7 D 393 VAL ILE TYR VAL ILE LEU ARG TYR ALA LYS MET LYS THR SEQRES 8 D 393 ALA THR ASN ILE TYR ILE LEU ASN LEU ALA ILE ALA ASP SEQRES 9 D 393 GLU LEU LEU MET LEU SER VAL PRO PHE LEU VAL THR SER SEQRES 10 D 393 THR LEU LEU ARG HIS TRP PRO PHE GLY ALA LEU LEU CYS SEQRES 11 D 393 ARG LEU VAL LEU SER VAL ASP ALA VAL ASN MET PHE THR SEQRES 12 D 393 SER ILE TYR CYS LEU THR VAL LEU SER VAL ASP ARG TYR SEQRES 13 D 393 VAL ALA VAL VAL HIS PRO ILE LYS ALA ALA ARG TYR ARG SEQRES 14 D 393 ARG PRO THR VAL ALA LYS VAL VAL ASN LEU GLY VAL TRP SEQRES 15 D 393 VAL LEU SER LEU LEU VAL ILE LEU PRO ILE VAL VAL PHE SEQRES 16 D 393 SER ARG THR ALA ALA ASN SER ASP GLY THR VAL ALA CYS SEQRES 17 D 393 ASN MET LEU MET PRO GLU PRO ALA GLN ARG TRP LEU VAL SEQRES 18 D 393 GLY PHE VAL LEU TYR THR PHE LEU MET GLY PHE LEU LEU SEQRES 19 D 393 PRO VAL GLY ALA ILE CYS LEU CYS TYR VAL LEU ILE ILE SEQRES 20 D 393 ALA LYS MET ARG MET VAL ALA LEU LYS ALA GLY TRP GLN SEQRES 21 D 393 GLN ARG LYS ARG SER GLU ARG LYS ILE THR LEU MET VAL SEQRES 22 D 393 MET MET VAL VAL MET VAL PHE VAL ILE CYS TRP MET PRO SEQRES 23 D 393 PHE TYR VAL VAL GLN LEU VAL ASN VAL PHE ALA GLU GLN SEQRES 24 D 393 ASP ASP ALA THR VAL SER GLN LEU SER VAL ILE LEU GLY SEQRES 25 D 393 TYR ALA ASN SER CYS ALA ASN PRO ILE LEU TYR GLY PHE SEQRES 26 D 393 LEU SER ASP ASN PHE LYS ARG SER PHE GLN ARG ILE LEU SEQRES 27 D 393 CYS LEU SER TRP MET ASP ASN ALA ALA GLU GLU PRO VAL SEQRES 28 D 393 ASP TYR TYR ALA THR ALA LEU LYS SER ARG ALA TYR SER SEQRES 29 D 393 VAL GLU ASP PHE GLN PRO GLU ASN LEU GLU SER GLY GLY SEQRES 30 D 393 VAL PHE ARG ASN GLY THR CYS THR SER ARG ILE THR THR SEQRES 31 D 393 LEU LEU GLU SEQRES 1 F 9 4J2 DCY DTY DTR LYS DVA DCY ALO NH2 HET 4J2 F 1 28 HET DCY F 2 10 HET DTY F 3 21 HET DTR F 4 24 HET DVA F 6 16 HET DCY F 7 10 HET ALO F 8 14 HET NH2 F 9 3 HETNAM 4J2 (2R)-2-AMINO-3-(NAPHTHALEN-2-YL)PROPANOIC ACID HETNAM DCY D-CYSTEINE HETNAM DTY D-TYROSINE HETNAM DTR D-TRYPTOPHAN HETNAM DVA D-VALINE HETNAM ALO ALLO-THREONINE HETNAM NH2 AMINO GROUP FORMUL 6 4J2 C13 H13 N O2 FORMUL 6 DCY 2(C3 H7 N O2 S) FORMUL 6 DTY C9 H11 N O3 FORMUL 6 DTR C11 H12 N2 O2 FORMUL 6 DVA C5 H11 N O2 FORMUL 6 ALO C4 H9 N O3 FORMUL 6 NH2 H2 N HELIX 1 AA1 ARG A 15 ASP A 26 1 12 HELIX 2 AA2 ILE A 212 GLU A 216 5 5 HELIX 3 AA3 SER A 228 LEU A 232 5 5 HELIX 4 AA4 ARG A 242 CYS A 254 1 13 HELIX 5 AA5 LEU A 273 SER A 281 1 9 HELIX 6 AA6 PRO A 282 CYS A 286 5 5 HELIX 7 AA7 THR A 295 GLU A 308 1 14 HELIX 8 AA8 LYS A 330 LEU A 348 1 19 HELIX 9 AA9 LEU B 7 CYS B 25 1 19 HELIX 10 AB1 THR B 29 ILE B 37 5 9 HELIX 11 AB2 ARG C 13 ASN C 24 1 12 HELIX 12 AB3 LYS C 29 HIS C 44 1 16 HELIX 13 AB4 ALA E 28 PHE E 32 5 5 HELIX 14 AB5 ALA D 58 TYR D 86 1 29 HELIX 15 AB6 THR D 91 LEU D 109 1 19 HELIX 16 AB7 SER D 110 LEU D 120 1 11 HELIX 17 AB8 GLY D 126 VAL D 160 1 35 HELIX 18 AB9 ILE D 163 ARG D 167 5 5 HELIX 19 AC1 ARG D 170 VAL D 194 1 25 HELIX 20 AC2 PRO D 215 ALA D 238 1 24 HELIX 21 AC3 CYS D 240 LYS D 256 1 17 HELIX 22 AC4 SER D 265 THR D 270 1 6 HELIX 23 AC5 MET D 278 GLU D 298 1 21 HELIX 24 AC6 ASP D 301 TYR D 313 1 13 HELIX 25 AC7 ASN D 319 GLY D 324 1 6 HELIX 26 AC8 SER D 327 ALA D 346 1 20 SHEET 1 AA1 3 GLU A 33 LEU A 36 0 SHEET 2 AA1 3 LEU A 194 MET A 198 1 O LYS A 197 N LEU A 36 SHEET 3 AA1 3 PHE A 189 PHE A 191 -1 N PHE A 189 O PHE A 196 SHEET 1 AA2 2 CYS A 224 ALA A 226 0 SHEET 2 AA2 2 PHE A 267 ASN A 269 1 O ASN A 269 N VAL A 225 SHEET 1 AA3 4 ARG B 49 LEU B 51 0 SHEET 2 AA3 4 LEU B 336 TRP B 339 -1 O LEU B 336 N LEU B 51 SHEET 3 AA3 4 VAL B 327 SER B 331 -1 N THR B 329 O LYS B 337 SHEET 4 AA3 4 VAL B 315 LEU B 318 -1 N CYS B 317 O GLY B 330 SHEET 1 AA4 4 ILE B 58 TRP B 63 0 SHEET 2 AA4 4 LEU B 69 SER B 74 -1 O ALA B 73 N TYR B 59 SHEET 3 AA4 4 LYS B 78 ASP B 83 -1 O LYS B 78 N SER B 74 SHEET 4 AA4 4 LYS B 89 PRO B 94 -1 O ILE B 93 N LEU B 79 SHEET 1 AA5 4 VAL B 100 TYR B 105 0 SHEET 2 AA5 4 TYR B 111 GLY B 116 -1 O GLY B 115 N MET B 101 SHEET 3 AA5 4 ILE B 123 ASN B 125 -1 O TYR B 124 N VAL B 112 SHEET 4 AA5 4 ARG B 134 ARG B 137 -1 O ARG B 137 N ILE B 123 SHEET 1 AA6 4 LEU B 146 PHE B 151 0 SHEET 2 AA6 4 ILE B 157 SER B 161 -1 O VAL B 158 N ARG B 150 SHEET 3 AA6 4 THR B 165 LEU B 168 -1 O THR B 165 N SER B 161 SHEET 4 AA6 4 THR B 178 PHE B 180 -1 O PHE B 180 N CYS B 166 SHEET 1 AA7 3 VAL B 200 ALA B 203 0 SHEET 2 AA7 3 SER B 207 LEU B 210 -1 O SER B 207 N ALA B 203 SHEET 3 AA7 3 GLN B 220 PHE B 222 -1 O GLN B 220 N LEU B 210 SHEET 1 AA8 4 ILE B 229 PHE B 234 0 SHEET 2 AA8 4 ALA B 240 SER B 245 -1 O ALA B 242 N CYS B 233 SHEET 3 AA8 4 CYS B 250 ASP B 254 -1 O PHE B 253 N PHE B 241 SHEET 4 AA8 4 GLN B 259 TYR B 264 -1 O TYR B 264 N CYS B 250 SHEET 1 AA9 3 SER B 275 SER B 277 0 SHEET 2 AA9 3 LEU B 285 GLY B 288 -1 O GLY B 288 N SER B 275 SHEET 3 AA9 3 CYS B 294 TRP B 297 -1 O ASN B 295 N ALA B 287 SHEET 1 AB1 4 GLN E 3 SER E 7 0 SHEET 2 AB1 4 ARG E 18 SER E 25 -1 O SER E 21 N SER E 7 SHEET 3 AB1 4 THR E 78 MET E 83 -1 O LEU E 81 N LEU E 20 SHEET 4 AB1 4 PHE E 68 ASP E 73 -1 N ASP E 73 O THR E 78 SHEET 1 AB2 6 GLY E 10 LEU E 11 0 SHEET 2 AB2 6 THR E 115 THR E 118 1 O THR E 118 N GLY E 10 SHEET 3 AB2 6 ALA E 92 CYS E 96 -1 N ALA E 92 O LEU E 117 SHEET 4 AB2 6 MET E 34 GLN E 39 -1 N GLN E 39 O MET E 93 SHEET 5 AB2 6 LEU E 45 ILE E 51 -1 O ILE E 51 N MET E 34 SHEET 6 AB2 6 ILE E 58 TYR E 60 -1 O TYR E 59 N TYR E 50 SHEET 1 AB3 4 MET E 128 THR E 129 0 SHEET 2 AB3 4 SER E 146 SER E 149 -1 O ARG E 148 N THR E 129 SHEET 3 AB3 4 ALA E 199 THR E 203 -1 O PHE E 200 N CYS E 147 SHEET 4 AB3 4 SER E 192 SER E 196 -1 N SER E 194 O THR E 201 SHEET 1 AB4 4 ASN E 182 LEU E 183 0 SHEET 2 AB4 4 ILE E 177 TYR E 178 -1 N TYR E 178 O ASN E 182 SHEET 3 AB4 4 LEU E 162 TRP E 164 -1 O TRP E 164 N ILE E 177 SHEET 4 AB4 4 CYS E 217 GLN E 219 -1 O MET E 218 N TYR E 163 SHEET 1 AB5 2 GLY E 213 TYR E 215 0 SHEET 2 AB5 2 THR E 231 LEU E 233 -1 O LEU E 233 N GLY E 213 SHEET 1 AB6 2 SER D 196 ARG D 197 0 SHEET 2 AB6 2 ASN D 209 MET D 210 -1 O ASN D 209 N ARG D 197 SSBOND 1 CYS E 22 CYS E 96 1555 1555 2.04 SSBOND 2 CYS E 147 CYS E 217 1555 1555 2.04 SSBOND 3 CYS D 130 CYS D 208 1555 1555 2.03 SSBOND 4 DCY F 2 DCY F 7 1555 1555 2.12 LINK C 4J2 F 1 N DCY F 2 1555 1555 1.49 LINK C DCY F 2 N DTY F 3 1555 1555 1.47 LINK C DTY F 3 N DTR F 4 1555 1555 1.50 LINK C DTR F 4 N LYS F 5 1555 1555 1.50 LINK C LYS F 5 N DVA F 6 1555 1555 1.49 LINK C DVA F 6 N DCY F 7 1555 1555 1.47 LINK C DCY F 7 N ALO F 8 1555 1555 1.48 LINK C ALO F 8 N NH2 F 9 1555 1555 1.44 CISPEP 1 TYR E 223 PRO E 224 0 3.07 CISPEP 2 GLU D 214 PRO D 215 0 -1.52 CISPEP 3 DTY F 3 DTR F 4 0 1.45 CISPEP 4 DTR F 4 LYS F 5 0 -1.00 CISPEP 5 LYS F 5 DVA F 6 0 -2.23 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