HEADER MEMBRANE PROTEIN 04-JUN-24 8ZRK TITLE CRYO-EM STRUCTURE OF GPR119-GS COMPLEX WITH SMALL MOLECULE AGONIST TITLE 2 GSK-1292263 COMPND MOL_ID: 1; COMPND 2 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(S) SUBUNIT ALPHA COMPND 3 ISOFORMS SHORT; COMPND 4 CHAIN: A; COMPND 5 SYNONYM: ADENYLATE CYCLASE-STIMULATING G ALPHA PROTEIN; COMPND 6 ENGINEERED: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(T) SUBUNIT COMPND 9 BETA-1; COMPND 10 CHAIN: B; COMPND 11 SYNONYM: TRANSDUCIN BETA CHAIN 1; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 3; COMPND 14 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(O) SUBUNIT COMPND 15 GAMMA-2; COMPND 16 CHAIN: G; COMPND 17 SYNONYM: G GAMMA-I; COMPND 18 ENGINEERED: YES; COMPND 19 MOL_ID: 4; COMPND 20 MOLECULE: NANOBODY35; COMPND 21 CHAIN: N; COMPND 22 ENGINEERED: YES; COMPND 23 MOL_ID: 5; COMPND 24 MOLECULE: GLUCOSE-DEPENDENT INSULINOTROPIC RECEPTOR; COMPND 25 CHAIN: R; COMPND 26 SYNONYM: G-PROTEIN COUPLED RECEPTOR 119; COMPND 27 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: GNAS, GNAS1, GSP; 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: ESCHERICHIA COLI; SOURCE 26 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 27 MOL_ID: 5; SOURCE 28 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 29 ORGANISM_COMMON: HUMAN; SOURCE 30 ORGANISM_TAXID: 9606; SOURCE 31 GENE: GPR119; SOURCE 32 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 33 EXPRESSION_SYSTEM_TAXID: 7108 KEYWDS GPR119, GSK-1292263, MEMBRANE PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR T.S.WONG,T.T.XIONG,Z.C.ZENG,S.Y.GAN,C.QIU,Y.DU JRNL AUTH T.S.WONG,T.T.XIONG,Z.C.ZENG JRNL TITL CRYO-EM STRUCTURE OF GPR119-GS COMPLEX JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.82 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) : 2.820 REMARK 3 NUMBER OF PARTICLES : 132000 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 8ZRK 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_1300048393. 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 GPR119-GS REMARK 245 COMPLEX WITH SMALL MOLECULE REMARK 245 AGONIST GSK-1292263 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 : FEI TITAN 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) : 51.80 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: PENTAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, G, N, R 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 GLY A 2 REMARK 465 CYS A 3 REMARK 465 LEU A 4 REMARK 465 GLY A 5 REMARK 465 ASN A 6 REMARK 465 SER A 7 REMARK 465 LYS A 8 REMARK 465 LEU A 63 REMARK 465 HIS A 64 REMARK 465 VAL A 65 REMARK 465 ASN A 66 REMARK 465 GLY A 67 REMARK 465 PHE A 68 REMARK 465 ASN A 69 REMARK 465 GLY A 70 REMARK 465 GLU A 71 REMARK 465 GLY A 72 REMARK 465 GLY A 73 REMARK 465 GLU A 74 REMARK 465 GLU A 75 REMARK 465 ASP A 76 REMARK 465 PRO A 77 REMARK 465 GLN A 78 REMARK 465 ALA A 79 REMARK 465 ALA A 80 REMARK 465 ARG A 81 REMARK 465 SER A 82 REMARK 465 ASN A 83 REMARK 465 SER A 84 REMARK 465 ASP A 85 REMARK 465 GLY A 86 REMARK 465 GLU A 87 REMARK 465 LYS A 88 REMARK 465 ALA A 89 REMARK 465 THR A 90 REMARK 465 LYS A 91 REMARK 465 VAL A 92 REMARK 465 GLN A 93 REMARK 465 ASP A 94 REMARK 465 ILE A 95 REMARK 465 LYS A 96 REMARK 465 ASN A 97 REMARK 465 ASN A 98 REMARK 465 LEU A 99 REMARK 465 LYS A 100 REMARK 465 GLU A 101 REMARK 465 ALA A 102 REMARK 465 ILE A 103 REMARK 465 GLU A 104 REMARK 465 THR A 105 REMARK 465 ILE A 106 REMARK 465 VAL A 107 REMARK 465 ALA A 108 REMARK 465 ALA A 109 REMARK 465 MET A 110 REMARK 465 SER A 111 REMARK 465 ASN A 112 REMARK 465 LEU A 113 REMARK 465 VAL A 114 REMARK 465 PRO A 115 REMARK 465 PRO A 116 REMARK 465 VAL A 117 REMARK 465 GLU A 118 REMARK 465 LEU A 119 REMARK 465 ALA A 120 REMARK 465 ASN A 121 REMARK 465 PRO A 122 REMARK 465 GLU A 123 REMARK 465 ASN A 124 REMARK 465 GLN A 125 REMARK 465 PHE A 126 REMARK 465 ARG A 127 REMARK 465 VAL A 128 REMARK 465 ASP A 129 REMARK 465 TYR A 130 REMARK 465 ILE A 131 REMARK 465 LEU A 132 REMARK 465 SER A 133 REMARK 465 VAL A 134 REMARK 465 MET A 135 REMARK 465 ASN A 136 REMARK 465 VAL A 137 REMARK 465 PRO A 138 REMARK 465 ASP A 139 REMARK 465 PHE A 140 REMARK 465 ASP A 141 REMARK 465 PHE A 142 REMARK 465 PRO A 143 REMARK 465 PRO A 144 REMARK 465 GLU A 145 REMARK 465 PHE A 146 REMARK 465 TYR A 147 REMARK 465 GLU A 148 REMARK 465 HIS A 149 REMARK 465 ALA A 150 REMARK 465 LYS A 151 REMARK 465 ALA A 152 REMARK 465 LEU A 153 REMARK 465 TRP A 154 REMARK 465 GLU A 155 REMARK 465 ASP A 156 REMARK 465 GLU A 157 REMARK 465 GLY A 158 REMARK 465 VAL A 159 REMARK 465 ARG A 160 REMARK 465 ALA A 161 REMARK 465 CYS A 162 REMARK 465 TYR A 163 REMARK 465 GLU A 164 REMARK 465 ARG A 165 REMARK 465 SER A 166 REMARK 465 ASN A 167 REMARK 465 GLU A 168 REMARK 465 TYR A 169 REMARK 465 GLN A 170 REMARK 465 LEU A 171 REMARK 465 ILE A 172 REMARK 465 ASP A 173 REMARK 465 CYS A 174 REMARK 465 ALA A 175 REMARK 465 GLN A 176 REMARK 465 TYR A 177 REMARK 465 PHE A 178 REMARK 465 LEU A 179 REMARK 465 ASP A 180 REMARK 465 LYS A 181 REMARK 465 ILE A 182 REMARK 465 ASP A 183 REMARK 465 VAL A 184 REMARK 465 ILE A 185 REMARK 465 LYS A 186 REMARK 465 GLN A 187 REMARK 465 ALA A 188 REMARK 465 ASP A 189 REMARK 465 TYR A 190 REMARK 465 VAL A 191 REMARK 465 PRO A 192 REMARK 465 SER A 193 REMARK 465 ASP A 194 REMARK 465 GLN A 195 REMARK 465 ASP A 196 REMARK 465 LEU A 197 REMARK 465 LEU A 198 REMARK 465 ARG A 199 REMARK 465 CYS A 200 REMARK 465 ARG A 201 REMARK 465 VAL A 202 REMARK 465 LEU A 203 REMARK 465 MET A 255 REMARK 465 VAL A 256 REMARK 465 ILE A 257 REMARK 465 ARG A 258 REMARK 465 GLU A 259 REMARK 465 ASP A 260 REMARK 465 ASN A 261 REMARK 465 GLN A 262 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 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 VAL B 352 REMARK 465 SER B 353 REMARK 465 GLY B 354 REMARK 465 TRP B 355 REMARK 465 ARG B 356 REMARK 465 LEU B 357 REMARK 465 PHE B 358 REMARK 465 LYS B 359 REMARK 465 LYS B 360 REMARK 465 ILE B 361 REMARK 465 SER B 362 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 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 465 MET N -22 REMARK 465 LYS N -21 REMARK 465 TYR N -20 REMARK 465 LEU N -19 REMARK 465 LEU N -18 REMARK 465 PRO N -17 REMARK 465 THR N -16 REMARK 465 ALA N -15 REMARK 465 ALA N -14 REMARK 465 ALA N -13 REMARK 465 GLY N -12 REMARK 465 LEU N -11 REMARK 465 LEU N -10 REMARK 465 LEU N -9 REMARK 465 LEU N -8 REMARK 465 ALA N -7 REMARK 465 ALA N -6 REMARK 465 GLN N -5 REMARK 465 PRO N -4 REMARK 465 ALA N -3 REMARK 465 MET N -2 REMARK 465 ALA N -1 REMARK 465 MET N 0 REMARK 465 HIS N 129 REMARK 465 HIS N 130 REMARK 465 HIS N 131 REMARK 465 HIS N 132 REMARK 465 HIS N 133 REMARK 465 HIS N 134 REMARK 465 MET R -33 REMARK 465 LYS R -32 REMARK 465 THR R -31 REMARK 465 ILE R -30 REMARK 465 ILE R -29 REMARK 465 ALA R -28 REMARK 465 LEU R -27 REMARK 465 SER R -26 REMARK 465 TYR R -25 REMARK 465 ILE R -24 REMARK 465 PHE R -23 REMARK 465 CYS R -22 REMARK 465 LEU R -21 REMARK 465 VAL R -20 REMARK 465 PHE R -19 REMARK 465 ALA R -18 REMARK 465 ASP R -17 REMARK 465 TYR R -16 REMARK 465 LYS R -15 REMARK 465 ASP R -14 REMARK 465 ASP R -13 REMARK 465 ASP R -12 REMARK 465 ASP R -11 REMARK 465 LYS R -10 REMARK 465 LEU R -9 REMARK 465 GLU R -8 REMARK 465 VAL R -7 REMARK 465 LEU R -6 REMARK 465 PHE R -5 REMARK 465 GLN R -4 REMARK 465 GLY R -3 REMARK 465 PRO R -2 REMARK 465 GLY R -1 REMARK 465 SER R 0 REMARK 465 MET R 1 REMARK 465 GLU R 2 REMARK 465 SER R 3 REMARK 465 SER R 4 REMARK 465 PHE R 5 REMARK 465 LEU R 66 REMARK 465 SER R 67 REMARK 465 SER R 68 REMARK 465 PRO R 69 REMARK 465 SER R 70 REMARK 465 ARG R 71 REMARK 465 PRO R 72 REMARK 465 THR R 73 REMARK 465 GLY R 211 REMARK 465 TYR R 212 REMARK 465 ARG R 213 REMARK 465 SER R 214 REMARK 465 PRO R 215 REMARK 465 ARG R 216 REMARK 465 THR R 217 REMARK 465 PRO R 218 REMARK 465 ALA R 294 REMARK 465 LEU R 295 REMARK 465 GLY R 296 REMARK 465 VAL R 297 REMARK 465 LYS R 298 REMARK 465 LYS R 299 REMARK 465 VAL R 300 REMARK 465 LEU R 301 REMARK 465 THR R 302 REMARK 465 SER R 303 REMARK 465 PHE R 304 REMARK 465 LEU R 305 REMARK 465 LEU R 306 REMARK 465 PHE R 307 REMARK 465 LEU R 308 REMARK 465 SER R 309 REMARK 465 ALA R 310 REMARK 465 ARG R 311 REMARK 465 ASN R 312 REMARK 465 CYS R 313 REMARK 465 GLY R 314 REMARK 465 PRO R 315 REMARK 465 GLU R 316 REMARK 465 ARG R 317 REMARK 465 PRO R 318 REMARK 465 ARG R 319 REMARK 465 GLU R 320 REMARK 465 SER R 321 REMARK 465 SER R 322 REMARK 465 CYS R 323 REMARK 465 HIS R 324 REMARK 465 ILE R 325 REMARK 465 VAL R 326 REMARK 465 THR R 327 REMARK 465 ILE R 328 REMARK 465 SER R 329 REMARK 465 SER R 330 REMARK 465 SER R 331 REMARK 465 GLU R 332 REMARK 465 PHE R 333 REMARK 465 ASP R 334 REMARK 465 GLY R 335 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 ARG A 13 CG CD NE CZ NH1 NH2 REMARK 470 ASN A 254 CG OD1 ND2 REMARK 470 HIS A 357 CG ND1 CD2 CE1 NE2 REMARK 470 SER A 366 OG REMARK 470 GLU B 3 CG CD OE1 OE2 REMARK 470 GLN B 13 CG CD OE1 NE2 REMARK 470 LYS B 15 CG CD CE NZ REMARK 470 LYS B 23 CG CD CE NZ REMARK 470 TYR B 105 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ASP B 170 CG OD1 OD2 REMARK 470 ASP B 195 CG OD1 OD2 REMARK 470 PHE B 234 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ASN B 340 CG OD1 ND2 REMARK 470 GLN N 5 CG CD OE1 NE2 REMARK 470 SER N 57 OG REMARK 470 SER N 71 OG REMARK 470 LYS N 87 CG CD CE NZ REMARK 470 CYS N 99 SG REMARK 470 ARG N 105 CG CD NE CZ NH1 NH2 REMARK 470 SER N 112 OG REMARK 470 CYS R 78 SG REMARK 470 GLN R 154 CG CD OE1 NE2 REMARK 470 SER R 219 OG REMARK 470 ASP R 220 CG OD1 OD2 REMARK 470 CYS R 251 SG REMARK 470 GLU R 253 CG CD OE1 OE2 REMARK 470 HIS R 255 CG ND1 CD2 CE1 NE2 REMARK 470 LYS R 284 CG CD CE NZ REMARK 470 ARG R 287 CG CD NE CZ NH1 NH2 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 CYS B 121 CA - CB - SG ANGL. DEV. = 6.7 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 SER A 251 53.45 -91.73 REMARK 500 SER A 252 23.28 -143.95 REMARK 500 ARG A 317 56.95 -96.68 REMARK 500 THR B 34 58.83 -96.22 REMARK 500 THR B 87 9.15 81.18 REMARK 500 ASN B 119 34.27 71.47 REMARK 500 ASN B 155 20.34 -142.24 REMARK 500 THR B 164 9.78 80.53 REMARK 500 ALA B 206 31.45 72.60 REMARK 500 ALA B 248 30.65 74.55 REMARK 500 SER B 334 6.81 83.09 REMARK 500 VAL N 48 -61.56 -106.48 REMARK 500 ALA N 92 -175.41 -171.62 REMARK 500 ASP N 109 44.35 -140.66 REMARK 500 TYR N 117 36.20 -98.77 REMARK 500 VAL R 160 -51.62 -125.94 REMARK 500 HIS R 255 75.53 -101.18 REMARK 500 ALA R 280 -69.51 -121.78 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-60399 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF GPR119-GS COMPLEX WITH SMALL MOLECULE AGONIST REMARK 900 GSK-1292263 DBREF 8ZRK A 1 394 UNP P63092 GNAS2_HUMAN 1 394 DBREF 8ZRK B 2 340 UNP P62873 GBB1_HUMAN 2 340 DBREF 8ZRK G 1 71 UNP P59768 GBG2_HUMAN 1 71 DBREF 8ZRK N -22 134 PDB 8ZRK 8ZRK -22 134 DBREF 8ZRK R 1 335 UNP Q8TDV5 GP119_HUMAN 1 335 SEQADV 8ZRK ASN A 54 UNP P63092 SER 54 CONFLICT SEQADV 8ZRK ALA A 226 UNP P63092 GLY 226 CONFLICT SEQADV 8ZRK ALA A 268 UNP P63092 GLU 268 CONFLICT SEQADV 8ZRK LYS A 271 UNP P63092 ASN 271 CONFLICT SEQADV 8ZRK ASP A 274 UNP P63092 LYS 274 CONFLICT SEQADV 8ZRK LYS A 280 UNP P63092 ARG 280 CONFLICT SEQADV 8ZRK ASP A 284 UNP P63092 THR 284 CONFLICT SEQADV 8ZRK THR A 285 UNP P63092 ILE 285 CONFLICT SEQADV 8ZRK SER A 366 UNP P63092 ALA 366 CONFLICT SEQADV 8ZRK MET B -21 UNP P62873 INITIATING METHIONINE SEQADV 8ZRK HIS B -20 UNP P62873 EXPRESSION TAG SEQADV 8ZRK HIS B -19 UNP P62873 EXPRESSION TAG SEQADV 8ZRK HIS B -18 UNP P62873 EXPRESSION TAG SEQADV 8ZRK HIS B -17 UNP P62873 EXPRESSION TAG SEQADV 8ZRK HIS B -16 UNP P62873 EXPRESSION TAG SEQADV 8ZRK HIS B -15 UNP P62873 EXPRESSION TAG SEQADV 8ZRK HIS B -14 UNP P62873 EXPRESSION TAG SEQADV 8ZRK HIS B -13 UNP P62873 EXPRESSION TAG SEQADV 8ZRK HIS B -12 UNP P62873 EXPRESSION TAG SEQADV 8ZRK HIS B -11 UNP P62873 EXPRESSION TAG SEQADV 8ZRK LEU B -10 UNP P62873 EXPRESSION TAG SEQADV 8ZRK GLU B -9 UNP P62873 EXPRESSION TAG SEQADV 8ZRK VAL B -8 UNP P62873 EXPRESSION TAG SEQADV 8ZRK LEU B -7 UNP P62873 EXPRESSION TAG SEQADV 8ZRK PHE B -6 UNP P62873 EXPRESSION TAG SEQADV 8ZRK GLN B -5 UNP P62873 EXPRESSION TAG SEQADV 8ZRK GLY B -4 UNP P62873 EXPRESSION TAG SEQADV 8ZRK PRO B -3 UNP P62873 EXPRESSION TAG SEQADV 8ZRK GLY B -2 UNP P62873 EXPRESSION TAG SEQADV 8ZRK SER B -1 UNP P62873 EXPRESSION TAG SEQADV 8ZRK SER B 0 UNP P62873 EXPRESSION TAG SEQADV 8ZRK GLY B 1 UNP P62873 EXPRESSION TAG SEQADV 8ZRK VAL B 341 UNP P62873 EXPRESSION TAG SEQADV 8ZRK SER B 342 UNP P62873 EXPRESSION TAG SEQADV 8ZRK GLY B 343 UNP P62873 EXPRESSION TAG SEQADV 8ZRK TRP B 344 UNP P62873 EXPRESSION TAG SEQADV 8ZRK ARG B 345 UNP P62873 EXPRESSION TAG SEQADV 8ZRK LEU B 346 UNP P62873 EXPRESSION TAG SEQADV 8ZRK PHE B 347 UNP P62873 EXPRESSION TAG SEQADV 8ZRK LYS B 348 UNP P62873 EXPRESSION TAG SEQADV 8ZRK LYS B 349 UNP P62873 EXPRESSION TAG SEQADV 8ZRK ILE B 350 UNP P62873 EXPRESSION TAG SEQADV 8ZRK SER B 351 UNP P62873 EXPRESSION TAG SEQADV 8ZRK VAL B 352 UNP P62873 EXPRESSION TAG SEQADV 8ZRK SER B 353 UNP P62873 EXPRESSION TAG SEQADV 8ZRK GLY B 354 UNP P62873 EXPRESSION TAG SEQADV 8ZRK TRP B 355 UNP P62873 EXPRESSION TAG SEQADV 8ZRK ARG B 356 UNP P62873 EXPRESSION TAG SEQADV 8ZRK LEU B 357 UNP P62873 EXPRESSION TAG SEQADV 8ZRK PHE B 358 UNP P62873 EXPRESSION TAG SEQADV 8ZRK LYS B 359 UNP P62873 EXPRESSION TAG SEQADV 8ZRK LYS B 360 UNP P62873 EXPRESSION TAG SEQADV 8ZRK ILE B 361 UNP P62873 EXPRESSION TAG SEQADV 8ZRK SER B 362 UNP P62873 EXPRESSION TAG SEQADV 8ZRK MET R -33 UNP Q8TDV5 INITIATING METHIONINE SEQADV 8ZRK LYS R -32 UNP Q8TDV5 EXPRESSION TAG SEQADV 8ZRK THR R -31 UNP Q8TDV5 EXPRESSION TAG SEQADV 8ZRK ILE R -30 UNP Q8TDV5 EXPRESSION TAG SEQADV 8ZRK ILE R -29 UNP Q8TDV5 EXPRESSION TAG SEQADV 8ZRK ALA R -28 UNP Q8TDV5 EXPRESSION TAG SEQADV 8ZRK LEU R -27 UNP Q8TDV5 EXPRESSION TAG SEQADV 8ZRK SER R -26 UNP Q8TDV5 EXPRESSION TAG SEQADV 8ZRK TYR R -25 UNP Q8TDV5 EXPRESSION TAG SEQADV 8ZRK ILE R -24 UNP Q8TDV5 EXPRESSION TAG SEQADV 8ZRK PHE R -23 UNP Q8TDV5 EXPRESSION TAG SEQADV 8ZRK CYS R -22 UNP Q8TDV5 EXPRESSION TAG SEQADV 8ZRK LEU R -21 UNP Q8TDV5 EXPRESSION TAG SEQADV 8ZRK VAL R -20 UNP Q8TDV5 EXPRESSION TAG SEQADV 8ZRK PHE R -19 UNP Q8TDV5 EXPRESSION TAG SEQADV 8ZRK ALA R -18 UNP Q8TDV5 EXPRESSION TAG SEQADV 8ZRK ASP R -17 UNP Q8TDV5 EXPRESSION TAG SEQADV 8ZRK TYR R -16 UNP Q8TDV5 EXPRESSION TAG SEQADV 8ZRK LYS R -15 UNP Q8TDV5 EXPRESSION TAG SEQADV 8ZRK ASP R -14 UNP Q8TDV5 EXPRESSION TAG SEQADV 8ZRK ASP R -13 UNP Q8TDV5 EXPRESSION TAG SEQADV 8ZRK ASP R -12 UNP Q8TDV5 EXPRESSION TAG SEQADV 8ZRK ASP R -11 UNP Q8TDV5 EXPRESSION TAG SEQADV 8ZRK LYS R -10 UNP Q8TDV5 EXPRESSION TAG SEQADV 8ZRK LEU R -9 UNP Q8TDV5 EXPRESSION TAG SEQADV 8ZRK GLU R -8 UNP Q8TDV5 EXPRESSION TAG SEQADV 8ZRK VAL R -7 UNP Q8TDV5 EXPRESSION TAG SEQADV 8ZRK LEU R -6 UNP Q8TDV5 EXPRESSION TAG SEQADV 8ZRK PHE R -5 UNP Q8TDV5 EXPRESSION TAG SEQADV 8ZRK GLN R -4 UNP Q8TDV5 EXPRESSION TAG SEQADV 8ZRK GLY R -3 UNP Q8TDV5 EXPRESSION TAG SEQADV 8ZRK PRO R -2 UNP Q8TDV5 EXPRESSION TAG SEQADV 8ZRK GLY R -1 UNP Q8TDV5 EXPRESSION TAG SEQADV 8ZRK SER R 0 UNP Q8TDV5 EXPRESSION TAG SEQRES 1 A 394 MET GLY CYS LEU GLY ASN SER LYS THR GLU ASP GLN ARG SEQRES 2 A 394 ASN GLU GLU LYS ALA GLN ARG GLU ALA ASN LYS LYS ILE SEQRES 3 A 394 GLU LYS GLN LEU GLN LYS ASP LYS GLN VAL TYR ARG ALA SEQRES 4 A 394 THR HIS ARG LEU LEU LEU LEU GLY ALA GLY GLU SER GLY SEQRES 5 A 394 LYS ASN THR ILE VAL LYS GLN MET ARG ILE LEU HIS VAL SEQRES 6 A 394 ASN GLY PHE ASN GLY GLU GLY GLY GLU GLU ASP PRO GLN SEQRES 7 A 394 ALA ALA ARG SER ASN SER ASP GLY GLU LYS ALA THR LYS SEQRES 8 A 394 VAL GLN ASP ILE LYS ASN ASN LEU LYS GLU ALA ILE GLU SEQRES 9 A 394 THR ILE VAL ALA ALA MET SER ASN LEU VAL PRO PRO VAL SEQRES 10 A 394 GLU LEU ALA ASN PRO GLU ASN GLN PHE ARG VAL ASP TYR SEQRES 11 A 394 ILE LEU SER VAL MET ASN VAL PRO ASP PHE ASP PHE PRO SEQRES 12 A 394 PRO GLU PHE TYR GLU HIS ALA LYS ALA LEU TRP GLU ASP SEQRES 13 A 394 GLU GLY VAL ARG ALA CYS TYR GLU ARG SER ASN GLU TYR SEQRES 14 A 394 GLN LEU ILE ASP CYS ALA GLN TYR PHE LEU ASP LYS ILE SEQRES 15 A 394 ASP VAL ILE LYS GLN ALA ASP TYR VAL PRO SER ASP GLN SEQRES 16 A 394 ASP LEU LEU ARG CYS ARG VAL LEU THR SER GLY ILE PHE SEQRES 17 A 394 GLU THR LYS PHE GLN VAL ASP LYS VAL ASN PHE HIS MET SEQRES 18 A 394 PHE ASP VAL GLY ALA GLN ARG ASP GLU ARG ARG LYS TRP SEQRES 19 A 394 ILE GLN CYS PHE ASN ASP VAL THR ALA ILE ILE PHE VAL SEQRES 20 A 394 VAL ALA SER SER SER TYR ASN MET VAL ILE ARG GLU ASP SEQRES 21 A 394 ASN GLN THR ASN ARG LEU GLN ALA ALA LEU LYS LEU PHE SEQRES 22 A 394 ASP SER ILE TRP ASN ASN LYS TRP LEU ARG ASP THR SER SEQRES 23 A 394 VAL ILE LEU PHE LEU ASN LYS GLN ASP LEU LEU ALA GLU SEQRES 24 A 394 LYS VAL LEU ALA GLY LYS SER LYS ILE GLU ASP TYR PHE SEQRES 25 A 394 PRO GLU PHE ALA ARG TYR THR THR PRO GLU ASP ALA THR SEQRES 26 A 394 PRO GLU PRO GLY GLU ASP PRO ARG VAL THR ARG ALA LYS SEQRES 27 A 394 TYR PHE ILE ARG ASP GLU PHE LEU ARG ILE SER THR ALA SEQRES 28 A 394 SER GLY ASP GLY ARG HIS TYR CYS TYR PRO HIS PHE THR SEQRES 29 A 394 CYS SER VAL ASP THR GLU ASN ILE ARG ARG VAL PHE ASN SEQRES 30 A 394 ASP CYS ARG ASP ILE ILE GLN ARG MET HIS LEU ARG GLN SEQRES 31 A 394 TYR GLU LEU LEU SEQRES 1 B 384 MET HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS LEU GLU SEQRES 2 B 384 VAL LEU PHE GLN GLY PRO GLY SER SER GLY SER GLU LEU SEQRES 3 B 384 ASP GLN LEU ARG GLN GLU ALA GLU GLN LEU LYS ASN GLN SEQRES 4 B 384 ILE ARG ASP ALA ARG LYS ALA CYS ALA ASP ALA THR LEU SEQRES 5 B 384 SER GLN ILE THR ASN ASN ILE ASP PRO VAL GLY ARG ILE SEQRES 6 B 384 GLN MET ARG THR ARG ARG THR LEU ARG GLY HIS LEU ALA SEQRES 7 B 384 LYS ILE TYR ALA MET HIS TRP GLY THR ASP SER ARG LEU SEQRES 8 B 384 LEU VAL SER ALA SER GLN ASP GLY LYS LEU ILE ILE TRP SEQRES 9 B 384 ASP SER TYR THR THR ASN LYS VAL HIS ALA ILE PRO LEU SEQRES 10 B 384 ARG SER SER TRP VAL MET THR CYS ALA TYR ALA PRO SER SEQRES 11 B 384 GLY ASN TYR VAL ALA CYS GLY GLY LEU ASP ASN ILE CYS SEQRES 12 B 384 SER ILE TYR ASN LEU LYS THR ARG GLU GLY ASN VAL ARG SEQRES 13 B 384 VAL SER ARG GLU LEU ALA GLY HIS THR GLY TYR LEU SER SEQRES 14 B 384 CYS CYS ARG PHE LEU ASP ASP ASN GLN ILE VAL THR SER SEQRES 15 B 384 SER GLY ASP THR THR CYS ALA LEU TRP ASP ILE GLU THR SEQRES 16 B 384 GLY GLN GLN THR THR THR PHE THR GLY HIS THR GLY ASP SEQRES 17 B 384 VAL MET SER LEU SER LEU ALA PRO ASP THR ARG LEU PHE SEQRES 18 B 384 VAL SER GLY ALA CYS ASP ALA SER ALA LYS LEU TRP ASP SEQRES 19 B 384 VAL ARG GLU GLY MET CYS ARG GLN THR PHE THR GLY HIS SEQRES 20 B 384 GLU SER ASP ILE ASN ALA ILE CYS PHE PHE PRO ASN GLY SEQRES 21 B 384 ASN ALA PHE ALA THR GLY SER ASP ASP ALA THR CYS ARG SEQRES 22 B 384 LEU PHE ASP LEU ARG ALA ASP GLN GLU LEU MET THR TYR SEQRES 23 B 384 SER HIS ASP ASN ILE ILE CYS GLY ILE THR SER VAL SER SEQRES 24 B 384 PHE SER LYS SER GLY ARG LEU LEU LEU ALA GLY TYR ASP SEQRES 25 B 384 ASP PHE ASN CYS ASN VAL TRP ASP ALA LEU LYS ALA ASP SEQRES 26 B 384 ARG ALA GLY VAL LEU ALA GLY HIS ASP ASN ARG VAL SER SEQRES 27 B 384 CYS LEU GLY VAL THR ASP ASP GLY MET ALA VAL ALA THR SEQRES 28 B 384 GLY SER TRP ASP SER PHE LEU LYS ILE TRP ASN VAL SER SEQRES 29 B 384 GLY TRP ARG LEU PHE LYS LYS ILE SER VAL SER GLY TRP SEQRES 30 B 384 ARG LEU PHE LYS LYS ILE SER 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 N 157 MET LYS TYR LEU LEU PRO THR ALA ALA ALA GLY LEU LEU SEQRES 2 N 157 LEU LEU ALA ALA GLN PRO ALA MET ALA MET GLN VAL GLN SEQRES 3 N 157 LEU GLN GLU SER GLY GLY GLY LEU VAL GLN PRO GLY GLY SEQRES 4 N 157 SER LEU ARG LEU SER CYS ALA ALA SER GLY PHE THR PHE SEQRES 5 N 157 SER ASN TYR LYS MET ASN TRP VAL ARG GLN ALA PRO GLY SEQRES 6 N 157 LYS GLY LEU GLU TRP VAL SER ASP ILE SER GLN SER GLY SEQRES 7 N 157 ALA SER ILE SER TYR THR GLY SER VAL LYS GLY ARG PHE SEQRES 8 N 157 THR ILE SER ARG ASP ASN ALA LYS ASN THR LEU TYR LEU SEQRES 9 N 157 GLN MET ASN SER LEU LYS PRO GLU ASP THR ALA VAL TYR SEQRES 10 N 157 TYR CYS ALA ARG CYS PRO ALA PRO PHE THR ARG ASP CYS SEQRES 11 N 157 PHE ASP VAL THR SER THR THR TYR ALA TYR ARG GLY GLN SEQRES 12 N 157 GLY THR GLN VAL THR VAL SER SER HIS HIS HIS HIS HIS SEQRES 13 N 157 HIS SEQRES 1 R 369 MET LYS THR ILE ILE ALA LEU SER TYR ILE PHE CYS LEU SEQRES 2 R 369 VAL PHE ALA ASP TYR LYS ASP ASP ASP ASP LYS LEU GLU SEQRES 3 R 369 VAL LEU PHE GLN GLY PRO GLY SER MET GLU SER SER PHE SEQRES 4 R 369 SER PHE GLY VAL ILE LEU ALA VAL LEU ALA SER LEU ILE SEQRES 5 R 369 ILE ALA THR ASN THR LEU VAL ALA VAL ALA VAL LEU LEU SEQRES 6 R 369 LEU ILE HIS LYS ASN ASP GLY VAL SER LEU CYS PHE THR SEQRES 7 R 369 LEU ASN LEU ALA VAL ALA ASP THR LEU ILE GLY VAL ALA SEQRES 8 R 369 ILE SER GLY LEU LEU THR ASP GLN LEU SER SER PRO SER SEQRES 9 R 369 ARG PRO THR GLN LYS THR LEU CYS SER LEU ARG MET ALA SEQRES 10 R 369 PHE VAL THR SER SER ALA ALA ALA SER VAL LEU THR VAL SEQRES 11 R 369 MET LEU ILE THR PHE ASP ARG TYR LEU ALA ILE LYS GLN SEQRES 12 R 369 PRO PHE ARG TYR LEU LYS ILE MET SER GLY PHE VAL ALA SEQRES 13 R 369 GLY ALA CYS ILE ALA GLY LEU TRP LEU VAL SER TYR LEU SEQRES 14 R 369 ILE GLY PHE LEU PRO LEU GLY ILE PRO MET PHE GLN GLN SEQRES 15 R 369 THR ALA TYR LYS GLY GLN CYS SER PHE PHE ALA VAL PHE SEQRES 16 R 369 HIS PRO HIS PHE VAL LEU THR LEU SER CYS VAL GLY PHE SEQRES 17 R 369 PHE PRO ALA MET LEU LEU PHE VAL PHE PHE TYR CYS ASP SEQRES 18 R 369 MET LEU LYS ILE ALA SER MET HIS SER GLN GLN ILE ARG SEQRES 19 R 369 LYS MET GLU HIS ALA GLY ALA MET ALA GLY GLY TYR ARG SEQRES 20 R 369 SER PRO ARG THR PRO SER ASP PHE LYS ALA LEU ARG THR SEQRES 21 R 369 VAL SER VAL LEU ILE GLY SER PHE ALA LEU SER TRP THR SEQRES 22 R 369 PRO PHE LEU ILE THR GLY ILE VAL GLN VAL ALA CYS GLN SEQRES 23 R 369 GLU CYS HIS LEU TYR LEU VAL LEU GLU ARG TYR LEU TRP SEQRES 24 R 369 LEU LEU GLY VAL GLY ASN SER LEU LEU ASN PRO LEU ILE SEQRES 25 R 369 TYR ALA TYR TRP GLN LYS GLU VAL ARG LEU GLN LEU TYR SEQRES 26 R 369 HIS MET ALA LEU GLY VAL LYS LYS VAL LEU THR SER PHE SEQRES 27 R 369 LEU LEU PHE LEU SER ALA ARG ASN CYS GLY PRO GLU ARG SEQRES 28 R 369 PRO ARG GLU SER SER CYS HIS ILE VAL THR ILE SER SER SEQRES 29 R 369 SER GLU PHE ASP GLY HET D8Y R 401 60 FORMUL 6 D8Y HELIX 1 AA1 THR A 9 ALA A 39 1 31 HELIX 2 AA2 GLY A 52 ILE A 62 1 11 HELIX 3 AA3 LYS A 233 ASN A 239 5 7 HELIX 4 AA4 ASN A 264 ASN A 279 1 16 HELIX 5 AA5 LYS A 293 ALA A 303 1 11 HELIX 6 AA6 LYS A 307 TYR A 311 5 5 HELIX 7 AA7 PHE A 312 TYR A 318 5 7 HELIX 8 AA8 ASP A 331 THR A 350 1 20 HELIX 9 AA9 GLU A 370 TYR A 391 1 22 HELIX 10 AB1 LEU B 4 ALA B 26 1 23 HELIX 11 AB2 THR B 29 THR B 34 1 6 HELIX 12 AB3 ALA G 7 ASN G 24 1 18 HELIX 13 AB4 LYS G 29 HIS G 44 1 16 HELIX 14 AB5 ALA G 45 ASP G 48 5 4 HELIX 15 AB6 THR N 28 TYR N 32 5 5 HELIX 16 AB7 GLY N 62 LYS N 65 5 4 HELIX 17 AB8 LYS N 87 THR N 91 5 5 HELIX 18 AB9 PHE R 7 ASN R 36 1 30 HELIX 19 AC1 SER R 40 LEU R 61 1 22 HELIX 20 AC2 LYS R 75 GLN R 109 1 35 HELIX 21 AC3 GLN R 109 MET R 117 1 9 HELIX 22 AC4 SER R 118 LEU R 139 1 22 HELIX 23 AC5 SER R 156 PHE R 161 1 6 HELIX 24 AC6 HIS R 162 GLY R 173 1 12 HELIX 25 AC7 GLY R 173 GLY R 210 1 38 HELIX 26 AC8 LYS R 222 LEU R 236 1 15 HELIX 27 AC9 TRP R 238 CYS R 251 1 14 HELIX 28 AD1 TRP R 265 ALA R 280 1 16 HELIX 29 AD2 GLN R 283 MET R 293 1 11 SHEET 1 AA1 6 ILE A 207 VAL A 214 0 SHEET 2 AA1 6 VAL A 217 VAL A 224 -1 O ASP A 223 N PHE A 208 SHEET 3 AA1 6 THR A 40 LEU A 46 1 N LEU A 43 O HIS A 220 SHEET 4 AA1 6 ALA A 243 ALA A 249 1 O ILE A 245 N LEU A 44 SHEET 5 AA1 6 SER A 286 ASN A 292 1 O ILE A 288 N ILE A 244 SHEET 6 AA1 6 CYS A 359 PHE A 363 1 O TYR A 360 N VAL A 287 SHEET 1 AA2 4 THR B 47 LEU B 51 0 SHEET 2 AA2 4 LEU B 336 TRP B 339 -1 O ILE B 338 N ARG B 48 SHEET 3 AA2 4 VAL B 327 THR B 329 -1 N VAL B 327 O TRP B 339 SHEET 4 AA2 4 GLY B 319 VAL B 320 -1 N GLY B 319 O ALA B 328 SHEET 1 AA3 4 ILE B 58 TRP B 63 0 SHEET 2 AA3 4 LEU B 69 SER B 74 -1 O ALA B 73 N TYR B 59 SHEET 3 AA3 4 LYS B 78 ASP B 83 -1 O TRP B 82 N LEU B 70 SHEET 4 AA3 4 HIS B 91 PRO B 94 -1 O ILE B 93 N LEU B 79 SHEET 1 AA4 4 ALA B 104 TYR B 105 0 SHEET 2 AA4 4 TYR B 111 ALA B 113 -1 O ALA B 113 N ALA B 104 SHEET 3 AA4 4 CYS B 121 ASN B 125 -1 O TYR B 124 N VAL B 112 SHEET 4 AA4 4 ARG B 134 LEU B 139 -1 O SER B 136 N ILE B 123 SHEET 1 AA5 4 LEU B 146 ASP B 153 0 SHEET 2 AA5 4 GLN B 156 SER B 161 -1 O GLN B 156 N LEU B 152 SHEET 3 AA5 4 CYS B 166 ASP B 170 -1 O TRP B 169 N ILE B 157 SHEET 4 AA5 4 GLN B 175 PHE B 180 -1 O THR B 177 N LEU B 168 SHEET 1 AA6 4 SER B 191 LEU B 192 0 SHEET 2 AA6 4 LEU B 198 GLY B 202 -1 O VAL B 200 N SER B 191 SHEET 3 AA6 4 SER B 207 ASP B 212 -1 O TRP B 211 N PHE B 199 SHEET 4 AA6 4 MET B 217 THR B 223 -1 O PHE B 222 N ALA B 208 SHEET 1 AA7 4 ILE B 229 PHE B 234 0 SHEET 2 AA7 4 ALA B 240 SER B 245 -1 O GLY B 244 N ASN B 230 SHEET 3 AA7 4 CYS B 250 ASP B 254 -1 O PHE B 253 N PHE B 241 SHEET 4 AA7 4 GLN B 259 TYR B 264 -1 O LEU B 261 N LEU B 252 SHEET 1 AA8 4 ILE B 273 PHE B 278 0 SHEET 2 AA8 4 LEU B 284 TYR B 289 -1 O GLY B 288 N THR B 274 SHEET 3 AA8 4 CYS B 294 ASP B 298 -1 O TRP B 297 N LEU B 285 SHEET 4 AA8 4 ARG B 304 LEU B 308 -1 O ALA B 305 N VAL B 296 SHEET 1 AA9 4 GLN N 3 SER N 7 0 SHEET 2 AA9 4 SER N 17 SER N 25 -1 O SER N 21 N SER N 7 SHEET 3 AA9 4 THR N 78 ASN N 84 -1 O MET N 83 N LEU N 18 SHEET 4 AA9 4 THR N 69 ASP N 73 -1 N THR N 69 O GLN N 82 SHEET 1 AB1 6 GLY N 10 VAL N 12 0 SHEET 2 AB1 6 THR N 122 VAL N 126 1 O GLN N 123 N GLY N 10 SHEET 3 AB1 6 ALA N 92 TYR N 95 -1 N TYR N 94 O THR N 122 SHEET 4 AB1 6 MET N 34 GLN N 39 -1 N VAL N 37 O TYR N 95 SHEET 5 AB1 6 GLU N 46 ILE N 51 -1 O GLU N 46 N ARG N 38 SHEET 6 AB1 6 SER N 59 TYR N 60 -1 O SER N 59 N ASP N 50 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