HEADER MEMBRANE PROTEIN/IMMUNE SYSTEM 19-DEC-23 8XIP TITLE STRUCTURE OF PASIREOTIDE-SSTR1 G PROTEIN COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: SOMATOSTATIN RECEPTOR TYPE 1; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: SS-1-R,SS1-R,SS1R,SST1,SRIF-2; 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 ENGINEERED: YES; COMPND 16 MOL_ID: 4; COMPND 17 MOLECULE: NANOBODY NB35; COMPND 18 CHAIN: D; COMPND 19 ENGINEERED: YES; COMPND 20 MOL_ID: 5; COMPND 21 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(O) SUBUNIT COMPND 22 GAMMA-2; COMPND 23 CHAIN: G; COMPND 24 SYNONYM: G GAMMA-I; COMPND 25 ENGINEERED: YES; COMPND 26 MOL_ID: 6; COMPND 27 MOLECULE: 004-DTR-LYS-TY5-PHE-A1D5E; COMPND 28 CHAIN: E; COMPND 29 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: SSTR1; 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, SSTR1, PASIREOTIDE, MEMBRANE PROTEIN/IMMUNE SYSTEM, MEMBRANE KEYWDS 2 PROTEIN-IMMUNE SYSTEM COMPLEX 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. 3.29 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) : 3.290 REMARK 3 NUMBER OF PARTICLES : 149370 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 8XIP 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_1300043582. 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-SSTR1 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, E 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 PHE A 2 REMARK 465 PRO A 3 REMARK 465 ASN A 4 REMARK 465 GLY A 5 REMARK 465 THR A 6 REMARK 465 ALA A 7 REMARK 465 SER A 8 REMARK 465 SER A 9 REMARK 465 PRO A 10 REMARK 465 SER A 11 REMARK 465 SER A 12 REMARK 465 SER A 13 REMARK 465 PRO A 14 REMARK 465 SER A 15 REMARK 465 PRO A 16 REMARK 465 SER A 17 REMARK 465 PRO A 18 REMARK 465 GLY A 19 REMARK 465 SER A 20 REMARK 465 CYS A 21 REMARK 465 GLY A 22 REMARK 465 GLU A 23 REMARK 465 GLY A 24 REMARK 465 GLY A 25 REMARK 465 GLY A 26 REMARK 465 SER A 27 REMARK 465 ARG A 28 REMARK 465 GLY A 29 REMARK 465 PRO A 30 REMARK 465 GLY A 31 REMARK 465 ALA A 32 REMARK 465 GLY A 33 REMARK 465 ALA A 34 REMARK 465 ALA A 35 REMARK 465 ASP A 36 REMARK 465 GLY A 37 REMARK 465 MET A 38 REMARK 465 GLU A 39 REMARK 465 GLU A 40 REMARK 465 PRO A 41 REMARK 465 GLY A 42 REMARK 465 ARG A 43 REMARK 465 ASN A 44 REMARK 465 ALA A 45 REMARK 465 SER A 46 REMARK 465 GLN A 47 REMARK 465 ASN A 48 REMARK 465 GLY A 49 REMARK 465 THR A 50 REMARK 465 LEU A 51 REMARK 465 ILE A 337 REMARK 465 LEU A 338 REMARK 465 CYS A 339 REMARK 465 LEU A 340 REMARK 465 SER A 341 REMARK 465 TRP A 342 REMARK 465 MET A 343 REMARK 465 ASP A 344 REMARK 465 ASN A 345 REMARK 465 ALA A 346 REMARK 465 ALA A 347 REMARK 465 GLU A 348 REMARK 465 GLU A 349 REMARK 465 PRO A 350 REMARK 465 VAL A 351 REMARK 465 ASP A 352 REMARK 465 TYR A 353 REMARK 465 TYR A 354 REMARK 465 ALA A 355 REMARK 465 THR A 356 REMARK 465 ALA A 357 REMARK 465 LEU A 358 REMARK 465 LYS A 359 REMARK 465 SER A 360 REMARK 465 ARG A 361 REMARK 465 ALA A 362 REMARK 465 TYR A 363 REMARK 465 SER A 364 REMARK 465 VAL A 365 REMARK 465 GLU A 366 REMARK 465 ASP A 367 REMARK 465 PHE A 368 REMARK 465 GLN A 369 REMARK 465 PRO A 370 REMARK 465 GLU A 371 REMARK 465 ASN A 372 REMARK 465 LEU A 373 REMARK 465 GLU A 374 REMARK 465 SER A 375 REMARK 465 GLY A 376 REMARK 465 GLY A 377 REMARK 465 VAL A 378 REMARK 465 PHE A 379 REMARK 465 ARG A 380 REMARK 465 ASN A 381 REMARK 465 GLY A 382 REMARK 465 THR A 383 REMARK 465 CYS A 384 REMARK 465 THR A 385 REMARK 465 SER A 386 REMARK 465 ARG A 387 REMARK 465 ILE A 388 REMARK 465 THR A 389 REMARK 465 THR A 390 REMARK 465 LEU A 391 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 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 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 SG CYS A 130 SG CYS A 208 1.29 REMARK 500 CD2 LEU C 257 CD1 LEU C 266 2.09 REMARK 500 SG CYS A 130 CB CYS A 208 2.18 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 LYS E 3 C TY5 E 4 N 0.149 REMARK 500 TY5 E 4 C PHE E 5 N 0.150 REMARK 500 PHE E 5 C D5E E 6 N 0.169 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 TRP A 123 72.23 52.67 REMARK 500 TYR A 168 59.19 -101.15 REMARK 500 ARG A 169 27.10 -150.36 REMARK 500 PRO A 171 35.07 -70.85 REMARK 500 PRO A 213 -172.28 -68.68 REMARK 500 ASP A 328 -15.05 -49.56 REMARK 500 SER B 333 -4.14 68.03 REMARK 500 GLN C 80 49.04 -87.61 REMARK 500 ASN C 124 19.32 59.46 REMARK 500 ASP C 168 31.76 -95.50 REMARK 500 LEU C 266 -60.23 -93.49 REMARK 500 ASP C 296 36.58 -98.76 REMARK 500 VAL D 50 -60.00 -108.96 REMARK 500 LYS E 3 53.53 -95.07 REMARK 500 TY5 E 4 -155.69 -131.47 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-38386 RELATED DB: EMDB REMARK 900 STRUCTURE OF PASIREOTIDE-SSTR1 G PROTEIN COMPLEX DBREF 8XIP A 1 391 UNP P30872 SSR1_HUMAN 1 391 DBREF 8XIP B 1 361 PDB 8XIP 8XIP 1 361 DBREF 8XIP C 7 345 UNP P62873 GBB1_HUMAN 2 340 DBREF 8XIP D -19 136 PDB 8XIP 8XIP -19 136 DBREF 8XIP G 1 71 UNP P59768 GBG2_HUMAN 1 71 DBREF 8XIP E 1 6 PDB 8XIP 8XIP 1 6 SEQADV 8XIP TYR A 276 UNP P30872 VAL 276 ENGINEERED MUTATION SEQADV 8XIP MET C -5 UNP P62873 INITIATING METHIONINE SEQADV 8XIP HIS C -4 UNP P62873 EXPRESSION TAG SEQADV 8XIP HIS C -3 UNP P62873 EXPRESSION TAG SEQADV 8XIP HIS C -2 UNP P62873 EXPRESSION TAG SEQADV 8XIP HIS C -1 UNP P62873 EXPRESSION TAG SEQADV 8XIP HIS C 0 UNP P62873 EXPRESSION TAG SEQADV 8XIP HIS C 1 UNP P62873 EXPRESSION TAG SEQADV 8XIP GLY C 2 UNP P62873 EXPRESSION TAG SEQADV 8XIP SER C 3 UNP P62873 EXPRESSION TAG SEQADV 8XIP LEU C 4 UNP P62873 EXPRESSION TAG SEQADV 8XIP LEU C 5 UNP P62873 EXPRESSION TAG SEQADV 8XIP GLN C 6 UNP P62873 EXPRESSION TAG SEQRES 1 A 391 MET PHE PRO ASN GLY THR ALA SER SER PRO SER SER SER SEQRES 2 A 391 PRO SER PRO SER PRO GLY SER CYS GLY GLU GLY GLY GLY SEQRES 3 A 391 SER ARG GLY PRO GLY ALA GLY ALA ALA ASP GLY MET GLU SEQRES 4 A 391 GLU PRO GLY ARG ASN ALA SER GLN ASN GLY THR LEU SER SEQRES 5 A 391 GLU GLY GLN GLY SER ALA ILE LEU ILE SER PHE ILE TYR SEQRES 6 A 391 SER VAL VAL CYS LEU VAL GLY LEU CYS GLY ASN SER MET SEQRES 7 A 391 VAL ILE TYR VAL ILE LEU ARG TYR ALA LYS MET LYS THR SEQRES 8 A 391 ALA THR ASN ILE TYR ILE LEU ASN LEU ALA ILE ALA ASP SEQRES 9 A 391 GLU LEU LEU MET LEU SER VAL PRO PHE LEU VAL THR SER SEQRES 10 A 391 THR LEU LEU ARG HIS TRP PRO PHE GLY ALA LEU LEU CYS SEQRES 11 A 391 ARG LEU VAL LEU SER VAL ASP ALA VAL ASN MET PHE THR SEQRES 12 A 391 SER ILE TYR CYS LEU THR VAL LEU SER VAL ASP ARG TYR SEQRES 13 A 391 VAL ALA VAL VAL HIS PRO ILE LYS ALA ALA ARG TYR ARG SEQRES 14 A 391 ARG PRO THR VAL ALA LYS VAL VAL ASN LEU GLY VAL TRP SEQRES 15 A 391 VAL LEU SER LEU LEU VAL ILE LEU PRO ILE VAL VAL PHE SEQRES 16 A 391 SER ARG THR ALA ALA ASN SER ASP GLY THR VAL ALA CYS SEQRES 17 A 391 ASN MET LEU MET PRO GLU PRO ALA GLN ARG TRP LEU VAL SEQRES 18 A 391 GLY PHE VAL LEU TYR THR PHE LEU MET GLY PHE LEU LEU SEQRES 19 A 391 PRO VAL GLY ALA ILE CYS LEU CYS TYR VAL LEU ILE ILE SEQRES 20 A 391 ALA LYS MET ARG MET VAL ALA LEU LYS ALA GLY TRP GLN SEQRES 21 A 391 GLN ARG LYS ARG SER GLU ARG LYS ILE THR LEU MET VAL SEQRES 22 A 391 MET MET TYR VAL MET VAL PHE VAL ILE CYS TRP MET PRO SEQRES 23 A 391 PHE TYR VAL VAL GLN LEU VAL ASN VAL PHE ALA GLU GLN SEQRES 24 A 391 ASP ASP ALA THR VAL SER GLN LEU SER VAL ILE LEU GLY SEQRES 25 A 391 TYR ALA ASN SER CYS ALA ASN PRO ILE LEU TYR GLY PHE SEQRES 26 A 391 LEU SER ASP ASN PHE LYS ARG SER PHE GLN ARG ILE LEU SEQRES 27 A 391 CYS LEU SER TRP MET ASP ASN ALA ALA GLU GLU PRO VAL SEQRES 28 A 391 ASP TYR TYR ALA THR ALA LEU LYS SER ARG ALA TYR SER SEQRES 29 A 391 VAL GLU ASP PHE GLN PRO GLU ASN LEU GLU SER GLY GLY SEQRES 30 A 391 VAL PHE ARG ASN GLY THR CYS THR SER ARG ILE THR THR SEQRES 31 A 391 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 351 MET HIS HIS HIS HIS HIS HIS GLY SER LEU LEU GLN SER SEQRES 2 C 351 GLU LEU ASP GLN LEU ARG GLN GLU ALA GLU GLN LEU LYS SEQRES 3 C 351 ASN GLN ILE ARG ASP ALA ARG LYS ALA CYS ALA ASP ALA SEQRES 4 C 351 THR LEU SER GLN ILE THR ASN ASN ILE ASP PRO VAL GLY SEQRES 5 C 351 ARG ILE GLN MET ARG THR ARG ARG THR LEU ARG GLY HIS SEQRES 6 C 351 LEU ALA LYS ILE TYR ALA MET HIS TRP GLY THR ASP SER SEQRES 7 C 351 ARG LEU LEU VAL SER ALA SER GLN ASP GLY LYS LEU ILE SEQRES 8 C 351 ILE TRP ASP SER TYR THR THR ASN LYS VAL HIS ALA ILE SEQRES 9 C 351 PRO LEU ARG SER SER TRP VAL MET THR CYS ALA TYR ALA SEQRES 10 C 351 PRO SER GLY ASN TYR VAL ALA CYS GLY GLY LEU ASP ASN SEQRES 11 C 351 ILE CYS SER ILE TYR ASN LEU LYS THR ARG GLU GLY ASN SEQRES 12 C 351 VAL ARG VAL SER ARG GLU LEU ALA GLY HIS THR GLY TYR SEQRES 13 C 351 LEU SER CYS CYS ARG PHE LEU ASP ASP ASN GLN ILE VAL SEQRES 14 C 351 THR SER SER GLY ASP THR THR CYS ALA LEU TRP ASP ILE SEQRES 15 C 351 GLU THR GLY GLN GLN THR THR THR PHE THR GLY HIS THR SEQRES 16 C 351 GLY ASP VAL MET SER LEU SER LEU ALA PRO ASP THR ARG SEQRES 17 C 351 LEU PHE VAL SER GLY ALA CYS ASP ALA SER ALA LYS LEU SEQRES 18 C 351 TRP ASP VAL ARG GLU GLY MET CYS ARG GLN THR PHE THR SEQRES 19 C 351 GLY HIS GLU SER ASP ILE ASN ALA ILE CYS PHE PHE PRO SEQRES 20 C 351 ASN GLY ASN ALA PHE ALA THR GLY SER ASP ASP ALA THR SEQRES 21 C 351 CYS ARG LEU PHE ASP LEU ARG ALA ASP GLN GLU LEU MET SEQRES 22 C 351 THR TYR SER HIS ASP ASN ILE ILE CYS GLY ILE THR SER SEQRES 23 C 351 VAL SER PHE SER LYS SER GLY ARG LEU LEU LEU ALA GLY SEQRES 24 C 351 TYR ASP ASP PHE ASN CYS ASN VAL TRP ASP ALA LEU LYS SEQRES 25 C 351 ALA ASP ARG ALA GLY VAL LEU ALA GLY HIS ASP ASN ARG SEQRES 26 C 351 VAL SER CYS LEU GLY VAL THR ASP ASP GLY MET ALA VAL SEQRES 27 C 351 ALA THR GLY SER TRP ASP SER PHE LEU LYS ILE TRP ASN 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 E 6 004 DTR LYS TY5 PHE D5E HET 004 E 1 10 HET DTR E 2 14 HET TY5 E 4 19 HET D5E E 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 HELIX 1 AA1 SER A 52 TYR A 86 1 35 HELIX 2 AA2 ALA A 92 ARG A 121 1 30 HELIX 3 AA3 GLY A 126 HIS A 161 1 36 HELIX 4 AA4 HIS A 161 TYR A 168 1 8 HELIX 5 AA5 THR A 172 LEU A 190 1 19 HELIX 6 AA6 LEU A 190 PHE A 195 1 6 HELIX 7 AA7 PRO A 215 ALA A 257 1 43 HELIX 8 AA8 SER A 265 PHE A 296 1 32 HELIX 9 AA9 VAL A 304 PHE A 325 1 22 HELIX 10 AB1 SER A 327 ARG A 336 1 10 HELIX 11 AB2 SER B 6 THR B 33 1 28 HELIX 12 AB3 GLY B 45 VAL B 50 1 6 HELIX 13 AB4 LYS B 210 PHE B 215 5 6 HELIX 14 AB5 ASP B 229 ASN B 231 5 3 HELIX 15 AB6 ARG B 232 TRP B 244 1 13 HELIX 16 AB7 LYS B 260 GLY B 271 1 12 HELIX 17 AB8 PHE B 279 ARG B 284 5 6 HELIX 18 AB9 ASP B 298 THR B 317 1 20 HELIX 19 AC1 GLU B 337 CYS B 358 1 22 HELIX 20 AC2 LEU C 12 CYS C 30 1 19 HELIX 21 AC3 THR C 34 THR C 39 1 6 HELIX 22 AC4 THR D 30 TYR D 34 5 5 HELIX 23 AC5 LYS D 89 THR D 93 5 5 HELIX 24 AC6 ILE G 9 ALA G 23 1 15 HELIX 25 AC7 LYS G 29 HIS G 44 1 16 SHEET 1 AA1 2 SER A 196 ALA A 200 0 SHEET 2 AA1 2 VAL A 206 MET A 210 -1 O ASN A 209 N ARG A 197 SHEET 1 AA2 6 ILE B 184 VAL B 191 0 SHEET 2 AA2 6 VAL B 194 VAL B 201 -1 O PHE B 196 N PHE B 189 SHEET 3 AA2 6 HIS B 34 LEU B 39 1 N LEU B 36 O PHE B 199 SHEET 4 AA2 6 ALA B 220 ASP B 226 1 O ILE B 222 N LEU B 39 SHEET 5 AA2 6 VAL B 254 ASN B 259 1 O ILE B 255 N ILE B 221 SHEET 6 AA2 6 CYS B 326 PHE B 330 1 O HIS B 329 N LEU B 258 SHEET 1 AA3 4 ARG C 51 ARG C 57 0 SHEET 2 AA3 4 PHE C 340 ASN C 345 -1 O LEU C 341 N LEU C 56 SHEET 3 AA3 4 VAL C 332 SER C 336 -1 N VAL C 332 O TRP C 344 SHEET 4 AA3 4 VAL C 320 VAL C 325 -1 N CYS C 322 O GLY C 335 SHEET 1 AA4 4 ILE C 63 TRP C 68 0 SHEET 2 AA4 4 LEU C 74 SER C 79 -1 O ALA C 78 N ALA C 65 SHEET 3 AA4 4 LYS C 83 ASP C 88 -1 O TRP C 87 N LEU C 75 SHEET 4 AA4 4 ASN C 93 PRO C 99 -1 O ILE C 98 N LEU C 84 SHEET 1 AA5 4 VAL C 105 CYS C 108 0 SHEET 2 AA5 4 TYR C 116 GLY C 121 -1 O GLY C 120 N MET C 106 SHEET 3 AA5 4 SER C 127 ASN C 130 -1 O TYR C 129 N VAL C 117 SHEET 4 AA5 4 VAL C 140 ARG C 142 -1 O ARG C 142 N ILE C 128 SHEET 1 AA6 4 CYS C 153 PHE C 156 0 SHEET 2 AA6 4 GLN C 161 SER C 165 -1 O VAL C 163 N ARG C 155 SHEET 3 AA6 4 THR C 170 ASP C 175 -1 O TRP C 174 N ILE C 162 SHEET 4 AA6 4 GLN C 181 THR C 186 -1 O THR C 183 N LEU C 173 SHEET 1 AA7 4 VAL C 192 LEU C 197 0 SHEET 2 AA7 4 LEU C 203 ALA C 208 -1 O GLY C 207 N MET C 193 SHEET 3 AA7 4 ALA C 213 ASP C 217 -1 O TRP C 216 N PHE C 204 SHEET 4 AA7 4 CYS C 223 PHE C 227 -1 O PHE C 227 N ALA C 213 SHEET 1 AA8 4 ILE C 234 PHE C 239 0 SHEET 2 AA8 4 ALA C 245 SER C 250 -1 O GLY C 249 N ASN C 235 SHEET 3 AA8 4 CYS C 255 ASP C 259 -1 O PHE C 258 N PHE C 246 SHEET 4 AA8 4 GLN C 264 TYR C 269 -1 O LEU C 266 N LEU C 257 SHEET 1 AA9 4 ILE C 278 PHE C 283 0 SHEET 2 AA9 4 LEU C 289 TYR C 294 -1 O GLY C 293 N THR C 279 SHEET 3 AA9 4 ASN C 298 ASP C 303 -1 O ASN C 298 N TYR C 294 SHEET 4 AA9 4 ARG C 309 LEU C 313 -1 O GLY C 311 N VAL C 301 SHEET 1 AB1 4 GLN D 5 SER D 9 0 SHEET 2 AB1 4 SER D 19 SER D 27 -1 O ALA D 25 N GLN D 7 SHEET 3 AB1 4 THR D 80 ASN D 86 -1 O MET D 85 N LEU D 20 SHEET 4 AB1 4 PHE D 70 ASP D 75 -1 N ASP D 75 O THR D 80 SHEET 1 AB2 5 ILE D 60 TYR D 62 0 SHEET 2 AB2 5 LEU D 47 ILE D 53 -1 N ASP D 52 O SER D 61 SHEET 3 AB2 5 MET D 36 GLN D 41 -1 N MET D 36 O ILE D 53 SHEET 4 AB2 5 ALA D 94 ARG D 100 -1 O VAL D 95 N GLN D 41 SHEET 5 AB2 5 THR D 124 VAL D 126 -1 O THR D 124 N TYR D 96 SSBOND 1 CYS C 126 CYS C 154 1555 1555 2.03 LINK C 004 E 1 N DTR E 2 1555 1555 1.42 LINK N 004 E 1 C D5E E 6 1555 1555 1.50 LINK C DTR E 2 N LYS E 3 1555 1555 1.46 LINK C LYS E 3 N TY5 E 4 1555 1555 1.49 LINK C TY5 E 4 N PHE E 5 1555 1555 1.49 LINK C PHE E 5 N D5E E 6 1555 1555 1.51 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