HEADER MEMBRANE PROTEIN 19-DEC-23 8XIR TITLE STRUCTURE OF PASIREOTIDE-SSTR3 G PROTEIN COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: SOMATOSTATIN RECEPTOR TYPE 3; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: SS-3-R,SS3-R,SS3R,SST3,SSR-28; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: G-ALPHA I; COMPND 9 CHAIN: B; COMPND 10 ENGINEERED: YES; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(T) SUBUNIT COMPND 13 BETA-1; COMPND 14 CHAIN: C; COMPND 15 SYNONYM: TRANSDUCIN BETA CHAIN 1; COMPND 16 ENGINEERED: YES; COMPND 17 MOL_ID: 4; COMPND 18 MOLECULE: NANOBODY NB35; COMPND 19 CHAIN: D; COMPND 20 ENGINEERED: YES; COMPND 21 MOL_ID: 5; COMPND 22 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(O) SUBUNIT COMPND 23 GAMMA-2; COMPND 24 CHAIN: G; COMPND 25 SYNONYM: G GAMMA-I; COMPND 26 ENGINEERED: YES; COMPND 27 MOL_ID: 6; COMPND 28 MOLECULE: PASIREOTIDE; 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: SSTR3; SOURCE 6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7111; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_COMMON: HUMAN; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 13 EXPRESSION_SYSTEM_TAXID: 7111; SOURCE 14 MOL_ID: 3; SOURCE 15 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 16 ORGANISM_COMMON: HUMAN; SOURCE 17 ORGANISM_TAXID: 9606; SOURCE 18 GENE: GNB1; SOURCE 19 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 20 EXPRESSION_SYSTEM_TAXID: 7111; SOURCE 21 MOL_ID: 4; SOURCE 22 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 23 ORGANISM_TAXID: 9844; SOURCE 24 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 25 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 26 MOL_ID: 5; SOURCE 27 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 28 ORGANISM_COMMON: HUMAN; SOURCE 29 ORGANISM_TAXID: 9606; SOURCE 30 GENE: GNG2; SOURCE 31 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 32 EXPRESSION_SYSTEM_TAXID: 7111; SOURCE 33 MOL_ID: 6; SOURCE 34 SYNTHETIC: YES; SOURCE 35 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT; SOURCE 36 ORGANISM_TAXID: 32630 KEYWDS GPCR, SSTR3, PASIREOTIDE, MEMBRANE PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR Y.WANG,Y.XU,H.E.XU,Y.ZHUANG JRNL AUTH Y.WANG,Y.XU,X.HE,W.FAN,K.WU,W.HU,X.CHENG,S.SUN,H.E.XU, JRNL AUTH 2 Y.ZHUANG JRNL TITL SELECTIVE LIGAND RECOGNITION AND ACTIVATION OF SOMATOSTATIN JRNL TITL 2 RECEPTORS SSTR1 AND SSTR3 JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.52 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) : 2.520 REMARK 3 NUMBER OF PARTICLES : 252565 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 8XIR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC. REMARK 100 THE DEPOSITION ID IS D_1300043584. 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 : PASIREOTIDE-SSTR3 G PROTEIN REMARK 245 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 : 7.50 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 REMARK 245 DETECTOR TYPE : GATAN K3 (6K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1200.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 5000.00 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) : 50.00 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: HEXAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, G, F REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 MET A 1 REMARK 465 ASP A 2 REMARK 465 MET A 3 REMARK 465 LEU A 4 REMARK 465 HIS A 5 REMARK 465 PRO A 6 REMARK 465 SER A 7 REMARK 465 SER A 8 REMARK 465 VAL A 9 REMARK 465 SER A 10 REMARK 465 THR A 11 REMARK 465 THR A 12 REMARK 465 SER A 13 REMARK 465 GLU A 14 REMARK 465 PRO A 15 REMARK 465 GLU A 16 REMARK 465 ASN A 17 REMARK 465 ALA A 18 REMARK 465 SER A 19 REMARK 465 SER A 20 REMARK 465 ALA A 21 REMARK 465 TRP A 22 REMARK 465 PRO A 23 REMARK 465 PRO A 24 REMARK 465 ASP A 25 REMARK 465 ALA A 26 REMARK 465 THR A 27 REMARK 465 LEU A 28 REMARK 465 GLY A 29 REMARK 465 ASN A 30 REMARK 465 VAL A 31 REMARK 465 SER A 32 REMARK 465 ALA A 33 REMARK 465 GLY A 34 REMARK 465 PRO A 35 REMARK 465 SER A 36 REMARK 465 PRO A 37 REMARK 465 ALA A 38 REMARK 465 GLY A 39 REMARK 465 LEU A 329 REMARK 465 ARG A 330 REMARK 465 PRO A 331 REMARK 465 SER A 332 REMARK 465 ARG A 333 REMARK 465 ARG A 334 REMARK 465 VAL A 335 REMARK 465 ARG A 336 REMARK 465 SER A 337 REMARK 465 GLN A 338 REMARK 465 GLU A 339 REMARK 465 PRO A 340 REMARK 465 THR A 341 REMARK 465 VAL A 342 REMARK 465 GLY A 343 REMARK 465 PRO A 344 REMARK 465 PRO A 345 REMARK 465 GLU A 346 REMARK 465 LYS A 347 REMARK 465 THR A 348 REMARK 465 GLU A 349 REMARK 465 GLU A 350 REMARK 465 GLU A 351 REMARK 465 ASP A 352 REMARK 465 GLU A 353 REMARK 465 GLU A 354 REMARK 465 GLU A 355 REMARK 465 GLU A 356 REMARK 465 ASP A 357 REMARK 465 GLY A 358 REMARK 465 GLU A 359 REMARK 465 GLU A 360 REMARK 465 SER A 361 REMARK 465 ARG A 362 REMARK 465 GLU A 363 REMARK 465 GLY A 364 REMARK 465 GLY A 365 REMARK 465 LYS A 366 REMARK 465 GLY A 367 REMARK 465 LYS A 368 REMARK 465 GLU A 369 REMARK 465 MET A 370 REMARK 465 ASN A 371 REMARK 465 GLY A 372 REMARK 465 ARG A 373 REMARK 465 VAL A 374 REMARK 465 SER A 375 REMARK 465 GLN A 376 REMARK 465 ILE A 377 REMARK 465 THR A 378 REMARK 465 GLN A 379 REMARK 465 PRO A 380 REMARK 465 GLY A 381 REMARK 465 THR A 382 REMARK 465 SER A 383 REMARK 465 GLY A 384 REMARK 465 GLN A 385 REMARK 465 GLU A 386 REMARK 465 ARG A 387 REMARK 465 PRO A 388 REMARK 465 PRO A 389 REMARK 465 SER A 390 REMARK 465 ARG A 391 REMARK 465 VAL A 392 REMARK 465 ALA A 393 REMARK 465 SER A 394 REMARK 465 LYS A 395 REMARK 465 GLU A 396 REMARK 465 GLN A 397 REMARK 465 GLN A 398 REMARK 465 LEU A 399 REMARK 465 LEU A 400 REMARK 465 PRO A 401 REMARK 465 GLN A 402 REMARK 465 GLU A 403 REMARK 465 ALA A 404 REMARK 465 SER A 405 REMARK 465 THR A 406 REMARK 465 GLY A 407 REMARK 465 GLU A 408 REMARK 465 LYS A 409 REMARK 465 SER A 410 REMARK 465 SER A 411 REMARK 465 THR A 412 REMARK 465 MET A 413 REMARK 465 ARG A 414 REMARK 465 ILE A 415 REMARK 465 SER A 416 REMARK 465 TYR A 417 REMARK 465 LEU A 418 REMARK 465 MET B 1 REMARK 465 GLY B 2 REMARK 465 CYS B 3 REMARK 465 TYR B 56 REMARK 465 HIS B 57 REMARK 465 VAL B 58 REMARK 465 ASN B 59 REMARK 465 GLY B 60 REMARK 465 TYR B 61 REMARK 465 SER B 62 REMARK 465 GLU B 63 REMARK 465 GLU B 64 REMARK 465 GLU B 65 REMARK 465 CYS B 66 REMARK 465 LYS B 67 REMARK 465 GLN B 68 REMARK 465 TYR B 69 REMARK 465 LYS B 70 REMARK 465 ALA B 71 REMARK 465 VAL B 72 REMARK 465 VAL B 73 REMARK 465 TYR B 74 REMARK 465 SER B 75 REMARK 465 ASN B 76 REMARK 465 THR B 77 REMARK 465 ILE B 78 REMARK 465 GLN B 79 REMARK 465 SER B 80 REMARK 465 ILE B 81 REMARK 465 ILE B 82 REMARK 465 ALA B 83 REMARK 465 ILE B 84 REMARK 465 ILE B 85 REMARK 465 ARG B 86 REMARK 465 ALA B 87 REMARK 465 MET B 88 REMARK 465 GLY B 89 REMARK 465 ARG B 90 REMARK 465 LEU B 91 REMARK 465 LYS B 92 REMARK 465 ILE B 93 REMARK 465 ASP B 94 REMARK 465 PHE B 95 REMARK 465 GLY B 96 REMARK 465 ASP B 97 REMARK 465 SER B 98 REMARK 465 ALA B 99 REMARK 465 ARG B 100 REMARK 465 ALA B 101 REMARK 465 ASP B 102 REMARK 465 ASP B 103 REMARK 465 ALA B 104 REMARK 465 ARG B 105 REMARK 465 GLN B 106 REMARK 465 LEU B 107 REMARK 465 PHE B 108 REMARK 465 VAL B 109 REMARK 465 LEU B 110 REMARK 465 ALA B 111 REMARK 465 GLY B 112 REMARK 465 ALA B 113 REMARK 465 ALA B 114 REMARK 465 GLU B 115 REMARK 465 GLU B 116 REMARK 465 GLY B 117 REMARK 465 PHE B 118 REMARK 465 MET B 119 REMARK 465 THR B 120 REMARK 465 ALA B 121 REMARK 465 GLU B 122 REMARK 465 LEU B 123 REMARK 465 ALA B 124 REMARK 465 GLY B 125 REMARK 465 VAL B 126 REMARK 465 ILE B 127 REMARK 465 LYS B 128 REMARK 465 ARG B 129 REMARK 465 LEU B 130 REMARK 465 TRP B 131 REMARK 465 LYS B 132 REMARK 465 ASP B 133 REMARK 465 SER B 134 REMARK 465 GLY B 135 REMARK 465 VAL B 136 REMARK 465 GLN B 137 REMARK 465 ALA B 138 REMARK 465 CYS B 139 REMARK 465 PHE B 140 REMARK 465 ASN B 141 REMARK 465 ARG B 142 REMARK 465 SER B 143 REMARK 465 ARG B 144 REMARK 465 GLU B 145 REMARK 465 TYR B 146 REMARK 465 GLN B 147 REMARK 465 LEU B 148 REMARK 465 ASN B 149 REMARK 465 ASP B 150 REMARK 465 SER B 151 REMARK 465 ALA B 152 REMARK 465 ALA B 153 REMARK 465 TYR B 154 REMARK 465 TYR B 155 REMARK 465 LEU B 156 REMARK 465 ASN B 157 REMARK 465 ASP B 158 REMARK 465 LEU B 159 REMARK 465 ASP B 160 REMARK 465 ARG B 161 REMARK 465 ILE B 162 REMARK 465 ALA B 163 REMARK 465 GLN B 164 REMARK 465 PRO B 165 REMARK 465 ASN B 166 REMARK 465 TYR B 167 REMARK 465 ILE B 168 REMARK 465 PRO B 169 REMARK 465 THR B 170 REMARK 465 GLN B 171 REMARK 465 GLN B 172 REMARK 465 ASP B 173 REMARK 465 VAL B 174 REMARK 465 LEU B 175 REMARK 465 ARG B 176 REMARK 465 THR B 177 REMARK 465 MET C -5 REMARK 465 HIS C -4 REMARK 465 HIS C -3 REMARK 465 HIS C -2 REMARK 465 HIS C -1 REMARK 465 HIS C 0 REMARK 465 HIS C 1 REMARK 465 GLY C 2 REMARK 465 SER C 3 REMARK 465 LEU C 4 REMARK 465 LEU C 5 REMARK 465 GLN C 6 REMARK 465 SER C 7 REMARK 465 GLU C 8 REMARK 465 LEU C 9 REMARK 465 ASP C 10 REMARK 465 GLY C 346 REMARK 465 SER C 347 REMARK 465 SER C 348 REMARK 465 GLY C 349 REMARK 465 GLY C 350 REMARK 465 GLY C 351 REMARK 465 GLY C 352 REMARK 465 SER C 353 REMARK 465 GLY C 354 REMARK 465 GLY C 355 REMARK 465 GLY C 356 REMARK 465 GLY C 357 REMARK 465 SER C 358 REMARK 465 SER C 359 REMARK 465 GLY C 360 REMARK 465 VAL C 361 REMARK 465 SER C 362 REMARK 465 GLY C 363 REMARK 465 TRP C 364 REMARK 465 ARG C 365 REMARK 465 LEU C 366 REMARK 465 PHE C 367 REMARK 465 LYS C 368 REMARK 465 LYS C 369 REMARK 465 ILE C 370 REMARK 465 SER C 371 REMARK 465 MET D -19 REMARK 465 LYS D -18 REMARK 465 TYR D -17 REMARK 465 LEU D -16 REMARK 465 LEU D -15 REMARK 465 PRO D -14 REMARK 465 THR D -13 REMARK 465 ALA D -12 REMARK 465 ALA D -11 REMARK 465 ALA D -10 REMARK 465 GLY D -9 REMARK 465 LEU D -8 REMARK 465 LEU D -7 REMARK 465 LEU D -6 REMARK 465 LEU D -5 REMARK 465 ALA D -4 REMARK 465 ALA D -3 REMARK 465 GLN D -2 REMARK 465 PRO D -1 REMARK 465 ALA D 0 REMARK 465 MET D 1 REMARK 465 ALA D 2 REMARK 465 VAL D 128 REMARK 465 SER D 129 REMARK 465 SER D 130 REMARK 465 HIS D 131 REMARK 465 HIS D 132 REMARK 465 HIS D 133 REMARK 465 HIS D 134 REMARK 465 HIS D 135 REMARK 465 HIS D 136 REMARK 465 MET G 1 REMARK 465 ALA G 2 REMARK 465 SER G 3 REMARK 465 ASN G 4 REMARK 465 ASN G 5 REMARK 465 THR G 6 REMARK 465 ALA G 7 REMARK 465 GLU G 63 REMARK 465 LYS G 64 REMARK 465 LYS G 65 REMARK 465 PHE G 66 REMARK 465 PHE G 67 REMARK 465 CYS G 68 REMARK 465 ALA G 69 REMARK 465 ILE G 70 REMARK 465 LEU G 71 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 ASN A 280 CG OD1 ND2 REMARK 470 CYS A 283 SG REMARK 470 PRO A 284 CG CD REMARK 470 LEU A 285 CG CD1 CD2 REMARK 470 PRO A 286 CG CD REMARK 470 GLU A 287 CG CD OE1 OE2 REMARK 470 GLU A 288 CG CD OE1 OE2 REMARK 470 THR C 34 OG1 CG2 REMARK 470 SER C 36 OG REMARK 470 GLU C 135 CG CD OE1 OE2 REMARK 470 ASP C 158 CG OD1 OD2 REMARK 470 GLU C 177 CG CD OE1 OE2 REMARK 470 ARG C 202 CG CD NE CZ NH1 NH2 REMARK 470 GLU C 220 CG CD OE1 OE2 REMARK 470 GLU G 17 CG CD OE1 OE2 REMARK 470 ASP G 26 CG OD1 OD2 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 HOH A 504 O HOH B 403 2.06 REMARK 500 OH TYR B 285 OD2 ASP B 310 2.08 REMARK 500 O ALA B 41 OG SER B 44 2.12 REMARK 500 OG SER C 79 OD2 ASP C 81 2.14 REMARK 500 O ALA A 290 CD1 LEU A 294 2.16 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 TYR A 295 CE1 TYR A 295 CZ -0.121 REMARK 500 LYS F 3 C TY5 F 4 N 0.175 REMARK 500 TY5 F 4 C PHE F 5 N 0.157 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 ASN C 345 C - N - CA ANGL. DEV. = 17.6 DEGREES REMARK 500 PHE F 5 N - CA - CB ANGL. DEV. = 14.8 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 HIS A 147 64.72 -110.21 REMARK 500 CYS A 245 -4.67 75.33 REMARK 500 ARG A 249 44.52 -140.88 REMARK 500 ARG A 319 -7.12 73.11 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY REMARK 500 REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 500 I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI ANGLE REMARK 500 GLY B 359 10.60 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-38388 RELATED DB: EMDB REMARK 900 STRUCTURE OF PASIREOTIDE-SSTR3 G PROTEIN COMPLEX DBREF 8XIR A 1 418 UNP P32745 SSR3_HUMAN 1 418 DBREF 8XIR B 1 361 PDB 8XIR 8XIR 1 361 DBREF 8XIR C 7 345 UNP P62873 GBB1_HUMAN 2 340 DBREF 8XIR D -19 136 PDB 8XIR 8XIR -19 136 DBREF 8XIR G 1 71 UNP P59768 GBG2_HUMAN 1 71 DBREF 8XIR F 1 6 PDB 8XIR 8XIR 1 6 SEQADV 8XIR TYR A 262 UNP P32745 VAL 262 ENGINEERED MUTATION SEQADV 8XIR MET C -5 UNP P62873 INITIATING METHIONINE SEQADV 8XIR HIS C -4 UNP P62873 EXPRESSION TAG SEQADV 8XIR HIS C -3 UNP P62873 EXPRESSION TAG SEQADV 8XIR HIS C -2 UNP P62873 EXPRESSION TAG SEQADV 8XIR HIS C -1 UNP P62873 EXPRESSION TAG SEQADV 8XIR HIS C 0 UNP P62873 EXPRESSION TAG SEQADV 8XIR HIS C 1 UNP P62873 EXPRESSION TAG SEQADV 8XIR GLY C 2 UNP P62873 EXPRESSION TAG SEQADV 8XIR SER C 3 UNP P62873 EXPRESSION TAG SEQADV 8XIR LEU C 4 UNP P62873 EXPRESSION TAG SEQADV 8XIR LEU C 5 UNP P62873 EXPRESSION TAG SEQADV 8XIR GLN C 6 UNP P62873 EXPRESSION TAG SEQADV 8XIR GLY C 346 UNP P62873 EXPRESSION TAG SEQADV 8XIR SER C 347 UNP P62873 EXPRESSION TAG SEQADV 8XIR SER C 348 UNP P62873 EXPRESSION TAG SEQADV 8XIR GLY C 349 UNP P62873 EXPRESSION TAG SEQADV 8XIR GLY C 350 UNP P62873 EXPRESSION TAG SEQADV 8XIR GLY C 351 UNP P62873 EXPRESSION TAG SEQADV 8XIR GLY C 352 UNP P62873 EXPRESSION TAG SEQADV 8XIR SER C 353 UNP P62873 EXPRESSION TAG SEQADV 8XIR GLY C 354 UNP P62873 EXPRESSION TAG SEQADV 8XIR GLY C 355 UNP P62873 EXPRESSION TAG SEQADV 8XIR GLY C 356 UNP P62873 EXPRESSION TAG SEQADV 8XIR GLY C 357 UNP P62873 EXPRESSION TAG SEQADV 8XIR SER C 358 UNP P62873 EXPRESSION TAG SEQADV 8XIR SER C 359 UNP P62873 EXPRESSION TAG SEQADV 8XIR GLY C 360 UNP P62873 EXPRESSION TAG SEQADV 8XIR VAL C 361 UNP P62873 EXPRESSION TAG SEQADV 8XIR SER C 362 UNP P62873 EXPRESSION TAG SEQADV 8XIR GLY C 363 UNP P62873 EXPRESSION TAG SEQADV 8XIR TRP C 364 UNP P62873 EXPRESSION TAG SEQADV 8XIR ARG C 365 UNP P62873 EXPRESSION TAG SEQADV 8XIR LEU C 366 UNP P62873 EXPRESSION TAG SEQADV 8XIR PHE C 367 UNP P62873 EXPRESSION TAG SEQADV 8XIR LYS C 368 UNP P62873 EXPRESSION TAG SEQADV 8XIR LYS C 369 UNP P62873 EXPRESSION TAG SEQADV 8XIR ILE C 370 UNP P62873 EXPRESSION TAG SEQADV 8XIR SER C 371 UNP P62873 EXPRESSION TAG SEQRES 1 A 418 MET ASP MET LEU HIS PRO SER SER VAL SER THR THR SER SEQRES 2 A 418 GLU PRO GLU ASN ALA SER SER ALA TRP PRO PRO ASP ALA SEQRES 3 A 418 THR LEU GLY ASN VAL SER ALA GLY PRO SER PRO ALA GLY SEQRES 4 A 418 LEU ALA VAL SER GLY VAL LEU ILE PRO LEU VAL TYR LEU SEQRES 5 A 418 VAL VAL CYS VAL VAL GLY LEU LEU GLY ASN SER LEU VAL SEQRES 6 A 418 ILE TYR VAL VAL LEU ARG HIS THR ALA SER PRO SER VAL SEQRES 7 A 418 THR ASN VAL TYR ILE LEU ASN LEU ALA LEU ALA ASP GLU SEQRES 8 A 418 LEU PHE MET LEU GLY LEU PRO PHE LEU ALA ALA GLN ASN SEQRES 9 A 418 ALA LEU SER TYR TRP PRO PHE GLY SER LEU MET CYS ARG SEQRES 10 A 418 LEU VAL MET ALA VAL ASP GLY ILE ASN GLN PHE THR SER SEQRES 11 A 418 ILE PHE CYS LEU THR VAL MET SER VAL ASP ARG TYR LEU SEQRES 12 A 418 ALA VAL VAL HIS PRO THR ARG SER ALA ARG TRP ARG THR SEQRES 13 A 418 ALA PRO VAL ALA ARG THR VAL SER ALA ALA VAL TRP VAL SEQRES 14 A 418 ALA SER ALA VAL VAL VAL LEU PRO VAL VAL VAL PHE SER SEQRES 15 A 418 GLY VAL PRO ARG GLY MET SER THR CYS HIS MET GLN TRP SEQRES 16 A 418 PRO GLU PRO ALA ALA ALA TRP ARG ALA GLY PHE ILE ILE SEQRES 17 A 418 TYR THR ALA ALA LEU GLY PHE PHE GLY PRO LEU LEU VAL SEQRES 18 A 418 ILE CYS LEU CYS TYR LEU LEU ILE VAL VAL LYS VAL ARG SEQRES 19 A 418 SER ALA GLY ARG ARG VAL TRP ALA PRO SER CYS GLN ARG SEQRES 20 A 418 ARG ARG ARG SER GLU ARG ARG VAL THR ARG MET VAL VAL SEQRES 21 A 418 ALA TYR VAL ALA LEU PHE VAL LEU CYS TRP MET PRO PHE SEQRES 22 A 418 TYR VAL LEU ASN ILE VAL ASN VAL VAL CYS PRO LEU PRO SEQRES 23 A 418 GLU GLU PRO ALA PHE PHE GLY LEU TYR PHE LEU VAL VAL SEQRES 24 A 418 ALA LEU PRO TYR ALA ASN SER CYS ALA ASN PRO ILE LEU SEQRES 25 A 418 TYR GLY PHE LEU SER TYR ARG PHE LYS GLN GLY PHE ARG SEQRES 26 A 418 ARG VAL LEU LEU ARG PRO SER ARG ARG VAL ARG SER GLN SEQRES 27 A 418 GLU PRO THR VAL GLY PRO PRO GLU LYS THR GLU GLU GLU SEQRES 28 A 418 ASP GLU GLU GLU GLU ASP GLY GLU GLU SER ARG GLU GLY SEQRES 29 A 418 GLY LYS GLY LYS GLU MET ASN GLY ARG VAL SER GLN ILE SEQRES 30 A 418 THR GLN PRO GLY THR SER GLY GLN GLU ARG PRO PRO SER SEQRES 31 A 418 ARG VAL ALA SER LYS GLU GLN GLN LEU LEU PRO GLN GLU SEQRES 32 A 418 ALA SER THR GLY GLU LYS SER SER THR MET ARG ILE SER SEQRES 33 A 418 TYR LEU SEQRES 1 B 361 MET GLY CYS THR LEU SER ALA GLU ASP LYS ALA ALA VAL SEQRES 2 B 361 GLU ARG SER LYS MET ILE GLU LYS GLN LEU GLN LYS ASP SEQRES 3 B 361 LYS GLN VAL TYR ARG ALA THR HIS ARG LEU LEU LEU LEU SEQRES 4 B 361 GLY ALA ASP ASN SER GLY LYS SER THR ILE VAL LYS GLN SEQRES 5 B 361 MET ARG ILE TYR HIS VAL ASN GLY TYR SER GLU GLU GLU SEQRES 6 B 361 CYS LYS GLN TYR LYS ALA VAL VAL TYR SER ASN THR ILE SEQRES 7 B 361 GLN SER ILE ILE ALA ILE ILE ARG ALA MET GLY ARG LEU SEQRES 8 B 361 LYS ILE ASP PHE GLY ASP SER ALA ARG ALA ASP ASP ALA SEQRES 9 B 361 ARG GLN LEU PHE VAL LEU ALA GLY ALA ALA GLU GLU GLY SEQRES 10 B 361 PHE MET THR ALA GLU LEU ALA GLY VAL ILE LYS ARG LEU SEQRES 11 B 361 TRP LYS ASP SER GLY VAL GLN ALA CYS PHE ASN ARG SER SEQRES 12 B 361 ARG GLU TYR GLN LEU ASN ASP SER ALA ALA TYR TYR LEU SEQRES 13 B 361 ASN ASP LEU ASP ARG ILE ALA GLN PRO ASN TYR ILE PRO SEQRES 14 B 361 THR GLN GLN ASP VAL LEU ARG THR ARG VAL LYS THR SER SEQRES 15 B 361 GLY ILE PHE GLU THR LYS PHE GLN VAL ASP LYS VAL ASN SEQRES 16 B 361 PHE HIS MET PHE ASP VAL GLY ALA GLN ARG ASP GLU ARG SEQRES 17 B 361 ARG LYS TRP ILE GLN CYS PHE ASN ASP VAL THR ALA ILE SEQRES 18 B 361 ILE PHE VAL VAL ASP SER SER ASP TYR ASN ARG LEU GLN SEQRES 19 B 361 GLU ALA LEU ASN ASP PHE LYS SER ILE TRP ASN ASN ARG SEQRES 20 B 361 TRP LEU ARG THR ILE SER VAL ILE LEU PHE LEU ASN LYS SEQRES 21 B 361 GLN ASP LEU LEU ALA GLU LYS VAL LEU ALA GLY LYS SER SEQRES 22 B 361 LYS ILE GLU ASP TYR PHE PRO GLU PHE ALA ARG TYR THR SEQRES 23 B 361 THR PRO GLU ASP ALA THR PRO GLU PRO GLY GLU ASP PRO SEQRES 24 B 361 ARG VAL THR ARG ALA LYS TYR PHE ILE ARG ASP GLU PHE SEQRES 25 B 361 LEU ARG ILE SER THR ALA SER GLY ASP GLY ARG HIS TYR SEQRES 26 B 361 CYS TYR PRO HIS PHE THR CYS SER VAL ASP THR GLU ASN SEQRES 27 B 361 ALA ARG ARG ILE PHE ASN ASP VAL THR ASP ILE ILE ILE SEQRES 28 B 361 LYS MET ASN LEU ARG ASP CYS GLY LEU PHE SEQRES 1 C 377 MET HIS HIS HIS HIS HIS HIS GLY SER LEU LEU GLN SER SEQRES 2 C 377 GLU LEU ASP GLN LEU ARG GLN GLU ALA GLU GLN LEU LYS SEQRES 3 C 377 ASN GLN ILE ARG ASP ALA ARG LYS ALA CYS ALA ASP ALA SEQRES 4 C 377 THR LEU SER GLN ILE THR ASN ASN ILE ASP PRO VAL GLY SEQRES 5 C 377 ARG ILE GLN MET ARG THR ARG ARG THR LEU ARG GLY HIS SEQRES 6 C 377 LEU ALA LYS ILE TYR ALA MET HIS TRP GLY THR ASP SER SEQRES 7 C 377 ARG LEU LEU VAL SER ALA SER GLN ASP GLY LYS LEU ILE SEQRES 8 C 377 ILE TRP ASP SER TYR THR THR ASN LYS VAL HIS ALA ILE SEQRES 9 C 377 PRO LEU ARG SER SER TRP VAL MET THR CYS ALA TYR ALA SEQRES 10 C 377 PRO SER GLY ASN TYR VAL ALA CYS GLY GLY LEU ASP ASN SEQRES 11 C 377 ILE CYS SER ILE TYR ASN LEU LYS THR ARG GLU GLY ASN SEQRES 12 C 377 VAL ARG VAL SER ARG GLU LEU ALA GLY HIS THR GLY TYR SEQRES 13 C 377 LEU SER CYS CYS ARG PHE LEU ASP ASP ASN GLN ILE VAL SEQRES 14 C 377 THR SER SER GLY ASP THR THR CYS ALA LEU TRP ASP ILE SEQRES 15 C 377 GLU THR GLY GLN GLN THR THR THR PHE THR GLY HIS THR SEQRES 16 C 377 GLY ASP VAL MET SER LEU SER LEU ALA PRO ASP THR ARG SEQRES 17 C 377 LEU PHE VAL SER GLY ALA CYS ASP ALA SER ALA LYS LEU SEQRES 18 C 377 TRP ASP VAL ARG GLU GLY MET CYS ARG GLN THR PHE THR SEQRES 19 C 377 GLY HIS GLU SER ASP ILE ASN ALA ILE CYS PHE PHE PRO SEQRES 20 C 377 ASN GLY ASN ALA PHE ALA THR GLY SER ASP ASP ALA THR SEQRES 21 C 377 CYS ARG LEU PHE ASP LEU ARG ALA ASP GLN GLU LEU MET SEQRES 22 C 377 THR TYR SER HIS ASP ASN ILE ILE CYS GLY ILE THR SER SEQRES 23 C 377 VAL SER PHE SER LYS SER GLY ARG LEU LEU LEU ALA GLY SEQRES 24 C 377 TYR ASP ASP PHE ASN CYS ASN VAL TRP ASP ALA LEU LYS SEQRES 25 C 377 ALA ASP ARG ALA GLY VAL LEU ALA GLY HIS ASP ASN ARG SEQRES 26 C 377 VAL SER CYS LEU GLY VAL THR ASP ASP GLY MET ALA VAL SEQRES 27 C 377 ALA THR GLY SER TRP ASP SER PHE LEU LYS ILE TRP ASN SEQRES 28 C 377 GLY SER SER GLY GLY GLY GLY SER GLY GLY GLY GLY SER SEQRES 29 C 377 SER GLY VAL SER GLY TRP ARG LEU PHE LYS LYS ILE SER SEQRES 1 D 156 MET LYS TYR LEU LEU PRO THR ALA ALA ALA GLY LEU LEU SEQRES 2 D 156 LEU LEU ALA ALA GLN PRO ALA MET ALA GLN VAL GLN LEU SEQRES 3 D 156 GLN GLU SER GLY GLY GLY LEU VAL GLN PRO GLY GLY SER SEQRES 4 D 156 LEU ARG LEU SER CYS ALA ALA SER GLY PHE THR PHE SER SEQRES 5 D 156 ASN TYR LYS MET ASN TRP VAL ARG GLN ALA PRO GLY LYS SEQRES 6 D 156 GLY LEU GLU TRP VAL SER ASP ILE SER GLN SER GLY ALA SEQRES 7 D 156 SER ILE SER TYR THR GLY SER VAL LYS GLY ARG PHE THR SEQRES 8 D 156 ILE SER ARG ASP ASN ALA LYS ASN THR LEU TYR LEU GLN SEQRES 9 D 156 MET ASN SER LEU LYS PRO GLU ASP THR ALA VAL TYR TYR SEQRES 10 D 156 CYS ALA ARG CYS PRO ALA PRO PHE THR ARG ASP CYS PHE SEQRES 11 D 156 ASP VAL THR SER THR THR TYR ALA TYR ARG GLY GLN GLY SEQRES 12 D 156 THR GLN VAL THR VAL SER SER HIS HIS HIS HIS HIS HIS SEQRES 1 G 71 MET ALA SER ASN ASN THR ALA SER ILE ALA GLN ALA ARG SEQRES 2 G 71 LYS LEU VAL GLU GLN LEU LYS MET GLU ALA ASN ILE ASP SEQRES 3 G 71 ARG ILE LYS VAL SER LYS ALA ALA ALA ASP LEU MET ALA SEQRES 4 G 71 TYR CYS GLU ALA HIS ALA LYS GLU ASP PRO LEU LEU THR SEQRES 5 G 71 PRO VAL PRO ALA SER GLU ASN PRO PHE ARG GLU LYS LYS SEQRES 6 G 71 PHE PHE CYS ALA ILE LEU SEQRES 1 F 6 004 DTR LYS TY5 PHE D5E HET 004 F 1 10 HET DTR F 2 14 HET TY5 F 4 19 HET D5E F 6 14 HETNAM 004 (2S)-AMINO(PHENYL)ETHANOIC ACID HETNAM DTR D-TRYPTOPHAN HETNAM TY5 O-BENZYL-L-TYROSINE HETSYN 004 L-PHENYLGLYCINE FORMUL 6 004 C8 H9 N O2 FORMUL 6 DTR C11 H12 N2 O2 FORMUL 6 TY5 C16 H17 N O3 FORMUL 6 D5E FORMUL 7 HOH *12(H2 O) HELIX 1 AA1 LEU A 40 HIS A 72 1 33 HELIX 2 AA2 SER A 77 SER A 107 1 31 HELIX 3 AA3 GLY A 112 HIS A 147 1 36 HELIX 4 AA4 HIS A 147 ARG A 155 1 9 HELIX 5 AA5 THR A 156 PHE A 181 1 26 HELIX 6 AA6 TRP A 202 ARG A 239 1 38 HELIX 7 AA7 TRP A 241 SER A 244 5 4 HELIX 8 AA8 CYS A 245 ARG A 250 1 6 HELIX 9 AA9 ARG A 250 ASN A 277 1 28 HELIX 10 AB1 ASN A 277 VAL A 282 1 6 HELIX 11 AB2 GLU A 288 GLY A 314 1 27 HELIX 12 AB3 PHE A 320 LEU A 328 1 9 HELIX 13 AB4 SER B 6 THR B 33 1 28 HELIX 14 AB5 GLY B 45 LYS B 51 1 7 HELIX 15 AB6 LYS B 210 ASN B 216 5 7 HELIX 16 AB7 ARG B 232 ASN B 246 1 15 HELIX 17 AB8 LYS B 260 GLY B 271 1 12 HELIX 18 AB9 PHE B 279 TYR B 285 5 7 HELIX 19 AC1 ASP B 298 SER B 319 1 22 HELIX 20 AC2 GLU B 337 CYS B 358 1 22 HELIX 21 AC3 ARG C 13 ALA C 31 1 19 HELIX 22 AC4 THR C 34 THR C 39 1 6 HELIX 23 AC5 THR D 30 TYR D 34 5 5 HELIX 24 AC6 LYS D 89 THR D 93 5 5 HELIX 25 AC7 ILE G 9 ALA G 23 1 15 HELIX 26 AC8 LYS G 29 HIS G 44 1 16 SHEET 1 AA1 6 ILE B 184 VAL B 191 0 SHEET 2 AA1 6 VAL B 194 VAL B 201 -1 O MET B 198 N THR B 187 SHEET 3 AA1 6 HIS B 34 GLY B 40 1 N HIS B 34 O ASN B 195 SHEET 4 AA1 6 ALA B 220 ASP B 226 1 O ILE B 222 N LEU B 39 SHEET 5 AA1 6 SER B 253 ASN B 259 1 O ILE B 255 N ILE B 221 SHEET 6 AA1 6 CYS B 326 HIS B 329 1 O HIS B 329 N LEU B 258 SHEET 1 AA2 4 ARG C 51 ARG C 57 0 SHEET 2 AA2 4 PHE C 340 ASN C 345 -1 O ILE C 343 N ARG C 53 SHEET 3 AA2 4 VAL C 332 SER C 336 -1 N THR C 334 O LYS C 342 SHEET 4 AA2 4 VAL C 320 VAL C 325 -1 N GLY C 324 O ALA C 333 SHEET 1 AA3 4 ILE C 63 TRP C 68 0 SHEET 2 AA3 4 LEU C 74 SER C 79 -1 O ALA C 78 N TYR C 64 SHEET 3 AA3 4 LYS C 83 ASP C 88 -1 O TRP C 87 N LEU C 75 SHEET 4 AA3 4 LYS C 94 PRO C 99 -1 O ILE C 98 N LEU C 84 SHEET 1 AA4 4 VAL C 105 TYR C 110 0 SHEET 2 AA4 4 TYR C 116 GLY C 121 -1 O ALA C 118 N ALA C 109 SHEET 3 AA4 4 SER C 127 ASN C 130 -1 O TYR C 129 N VAL C 117 SHEET 4 AA4 4 ARG C 139 ARG C 142 -1 O ARG C 142 N ILE C 128 SHEET 1 AA5 4 LEU C 151 CYS C 153 0 SHEET 2 AA5 4 GLN C 161 SER C 166 -1 O SER C 165 N CYS C 153 SHEET 3 AA5 4 CYS C 171 ASP C 175 -1 O TRP C 174 N ILE C 162 SHEET 4 AA5 4 GLN C 181 PHE C 185 -1 O THR C 182 N LEU C 173 SHEET 1 AA6 4 VAL C 192 LEU C 197 0 SHEET 2 AA6 4 LEU C 203 ALA C 208 -1 O GLY C 207 N SER C 194 SHEET 3 AA6 4 SER C 212 ASP C 217 -1 O LYS C 214 N SER C 206 SHEET 4 AA6 4 CYS C 223 THR C 228 -1 O PHE C 227 N ALA C 213 SHEET 1 AA7 4 ILE C 234 PHE C 239 0 SHEET 2 AA7 4 ALA C 245 SER C 250 -1 O ALA C 247 N CYS C 238 SHEET 3 AA7 4 THR C 254 ASP C 259 -1 O PHE C 258 N PHE C 246 SHEET 4 AA7 4 GLN C 264 SER C 270 -1 O TYR C 269 N CYS C 255 SHEET 1 AA8 4 ILE C 278 PHE C 283 0 SHEET 2 AA8 4 LEU C 289 TYR C 294 -1 O LEU C 291 N SER C 282 SHEET 3 AA8 4 ASN C 298 ASP C 303 -1 O ASN C 300 N ALA C 292 SHEET 4 AA8 4 ARG C 309 ALA C 314 -1 O ALA C 310 N VAL C 301 SHEET 1 AA9 4 GLN D 5 SER D 9 0 SHEET 2 AA9 4 LEU D 20 SER D 27 -1 O ALA D 25 N GLN D 7 SHEET 3 AA9 4 THR D 80 MET D 85 -1 O MET D 85 N LEU D 20 SHEET 4 AA9 4 PHE D 70 ASP D 75 -1 N THR D 71 O GLN D 84 SHEET 1 AB1 5 ILE D 60 TYR D 62 0 SHEET 2 AB1 5 LEU D 47 ILE D 53 -1 N ASP D 52 O SER D 61 SHEET 3 AB1 5 MET D 36 GLN D 41 -1 N ARG D 40 O GLU D 48 SHEET 4 AB1 5 ALA D 94 ARG D 100 -1 O VAL D 95 N GLN D 41 SHEET 5 AB1 5 THR D 124 VAL D 126 -1 O THR D 124 N TYR D 96 SSBOND 1 CYS A 116 CYS A 191 1555 1555 2.03 SSBOND 2 CYS C 126 CYS C 154 1555 1555 2.03 LINK C 004 F 1 N DTR F 2 1555 1555 1.44 LINK N 004 F 1 C D5E F 6 1555 1555 1.51 LINK C DTR F 2 N LYS F 3 1555 1555 1.46 LINK C LYS F 3 N TY5 F 4 1555 1555 1.51 LINK C TY5 F 4 N PHE F 5 1555 1555 1.49 LINK C PHE F 5 N D5E F 6 1555 1555 1.47 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 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