HEADER MEMBRANE PROTEIN 01-MAY-19 6ORV TITLE NON-PEPTIDE AGONIST (TT-OAD2) BOUND TO THE GLUCAGON-LIKE PEPTIDE-1 TITLE 2 (GLP-1) RECEPTOR COMPND MOL_ID: 1; COMPND 2 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(S) SUBUNIT ALPHA COMPND 3 ISOFORMS SHORT; COMPND 4 CHAIN: AP; 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: BP; 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: GP; COMPND 17 SYNONYM: G GAMMA-I; COMPND 18 ENGINEERED: YES; COMPND 19 MOL_ID: 4; COMPND 20 MOLECULE: NANOBODY 35; COMPND 21 CHAIN: NP; COMPND 22 ENGINEERED: YES; COMPND 23 MOL_ID: 5; COMPND 24 MOLECULE: GLUCAGON-LIKE PEPTIDE 1 RECEPTOR; COMPND 25 CHAIN: RP; COMPND 26 SYNONYM: GLP-1R; 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: TRICHOPLUSIA NI; SOURCE 7 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7111; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 11 ORGANISM_COMMON: HUMAN; SOURCE 12 ORGANISM_TAXID: 9606; SOURCE 13 GENE: GNB1; SOURCE 14 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 15 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER; SOURCE 16 EXPRESSION_SYSTEM_TAXID: 7111; SOURCE 17 MOL_ID: 3; SOURCE 18 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 19 ORGANISM_COMMON: HUMAN; SOURCE 20 ORGANISM_TAXID: 9606; SOURCE 21 GENE: GNG2; SOURCE 22 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 23 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER; SOURCE 24 EXPRESSION_SYSTEM_TAXID: 7111; SOURCE 25 MOL_ID: 4; SOURCE 26 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 27 ORGANISM_COMMON: HUMAN; SOURCE 28 ORGANISM_TAXID: 9606; SOURCE 29 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 30 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 31 MOL_ID: 5; SOURCE 32 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 33 ORGANISM_COMMON: HUMAN; SOURCE 34 ORGANISM_TAXID: 9606; SOURCE 35 GENE: GLP1R; SOURCE 36 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 37 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER; SOURCE 38 EXPRESSION_SYSTEM_TAXID: 7111 KEYWDS G-COUPLED PROTEIN RECEPTOR, GPCR, NON-PEPTIDE ANGONIST, MEMBRANE KEYWDS 2 PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR M.J.BELOUSOFF,Y.L.LIANG,R.DANEV JRNL AUTH P.ZHAO,Y.L.LIANG,M.J.BELOUSOFF,G.DEGANUTTI,M.M.FLETCHER, JRNL AUTH 2 F.S.WILLARD,M.G.BELL,M.E.CHRISTE,K.W.SLOOP,A.INOUE, JRNL AUTH 3 T.T.TRUONG,L.CLYDESDALE,S.G.B.FURNESS,A.CHRISTOPOULOS, JRNL AUTH 4 M.W.WANG,L.J.MILLER,C.A.REYNOLDS,R.DANEV,P.M.SEXTON, JRNL AUTH 5 D.WOOTTEN JRNL TITL ACTIVATION OF THE GLP-1 RECEPTOR BY A NON-PEPTIDIC AGONIST. JRNL REF NATURE V. 577 432 2020 JRNL REFN ESSN 1476-4687 JRNL PMID 31915381 JRNL DOI 10.1038/S41586-019-1902-Z REMARK 2 REMARK 2 RESOLUTION. 3.00 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) : 3.000 REMARK 3 NUMBER OF PARTICLES : 85978 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 6ORV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB. REMARK 100 THE DEPOSITION ID IS D_1000241239. 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 : TT-OAD2:GLP-1R:GS COMPLEX; REMARK 245 GUANINE NUCLEOTIDE-BINDING REMARK 245 PROTEIN G(S) SUBUNIT ALPHA REMARK 245 ISOFORMS SHORT, GUANINE REMARK 245 NUCLEOTIDE-BINDING PROTEIN G(I)/ REMARK 245 G(S)/G(T) SUBUNIT BETA-1, REMARK 245 GUANINE NUCLEOTIDE-BINDING REMARK 245 PROTEIN G(I)/G(S)/G(O) SUBUNIT REMARK 245 GAMMA-2, GLUCAGON-LIKE PEPTIDE REMARK 245 1 RECEPTOR; NANOBODY 35 REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 3.50 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 (6K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : NULL REMARK 245 MAXIMUM DEFOCUS (NM) : NULL 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) : 66.65 REMARK 245 ILLUMINATION MODE : SPOT SCAN 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: PENTAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: AP, BP, GP, NP, RP 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 THR A 9 REMARK 465 GLU A 10 REMARK 465 ALA A 48 REMARK 465 GLY A 49 REMARK 465 GLU A 50 REMARK 465 SER A 51 REMARK 465 GLY A 52 REMARK 465 LYS A 53 REMARK 465 ASN A 54 REMARK 465 THR A 55 REMARK 465 ILE A 56 REMARK 465 VAL A 57 REMARK 465 LYS A 58 REMARK 465 GLN A 59 REMARK 465 MET A 60 REMARK 465 ARG A 61 REMARK 465 ILE A 62 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 THR A 204 REMARK 465 SER A 250 REMARK 465 SER A 251 REMARK 465 SER A 252 REMARK 465 TYR A 253 REMARK 465 ASN A 254 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 THR A 263 REMARK 465 LEU A 296 REMARK 465 LEU A 297 REMARK 465 ALA A 298 REMARK 465 GLU A 299 REMARK 465 LYS A 300 REMARK 465 VAL A 301 REMARK 465 LEU A 302 REMARK 465 ALA A 303 REMARK 465 GLY A 304 REMARK 465 LYS A 305 REMARK 465 SER A 306 REMARK 465 LYS A 307 REMARK 465 CYS A 365 REMARK 465 ALA A 366 REMARK 465 VAL A 367 REMARK 465 ASP A 368 REMARK 465 THR A 369 REMARK 465 GLU A 370 REMARK 465 MET B -9 REMARK 465 HIS B -8 REMARK 465 HIS B -7 REMARK 465 HIS B -6 REMARK 465 HIS B -5 REMARK 465 HIS B -4 REMARK 465 HIS 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 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 SER N 127 REMARK 465 SER N 128 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 GLU N 135 REMARK 465 PRO N 136 REMARK 465 GLU N 137 REMARK 465 ALA N 138 REMARK 465 MET R -8 REMARK 465 LYS R -7 REMARK 465 THR R -6 REMARK 465 ILE R -5 REMARK 465 ILE R -4 REMARK 465 ALA R -3 REMARK 465 LEU R -2 REMARK 465 SER R -1 REMARK 465 TYR R 0 REMARK 465 ILE R 1 REMARK 465 PHE R 2 REMARK 465 CYS R 3 REMARK 465 LEU R 4 REMARK 465 VAL R 5 REMARK 465 PHE R 6 REMARK 465 ALA R 7 REMARK 465 ASP R 8 REMARK 465 TYR R 9 REMARK 465 LYS R 10 REMARK 465 ASP R 11 REMARK 465 ASP R 12 REMARK 465 ASP R 13 REMARK 465 ASP R 14 REMARK 465 LEU R 15 REMARK 465 GLU R 16 REMARK 465 VAL R 17 REMARK 465 LEU R 18 REMARK 465 PHE R 19 REMARK 465 GLN R 20 REMARK 465 GLY R 21 REMARK 465 PRO R 22 REMARK 465 ALA R 23 REMARK 465 ARG R 24 REMARK 465 PRO R 25 REMARK 465 GLN R 26 REMARK 465 GLY R 27 REMARK 465 ALA R 28 REMARK 465 THR R 29 REMARK 465 VAL R 30 REMARK 465 SER R 31 REMARK 465 LEU R 32 REMARK 465 TRP R 33 REMARK 465 GLU R 34 REMARK 465 THR R 35 REMARK 465 VAL R 36 REMARK 465 GLN R 37 REMARK 465 LYS R 38 REMARK 465 TRP R 39 REMARK 465 ARG R 40 REMARK 465 GLU R 41 REMARK 465 TYR R 42 REMARK 465 ARG R 43 REMARK 465 ARG R 44 REMARK 465 GLN R 45 REMARK 465 CYS R 46 REMARK 465 GLN R 47 REMARK 465 ARG R 48 REMARK 465 SER R 49 REMARK 465 LEU R 50 REMARK 465 THR R 51 REMARK 465 GLU R 52 REMARK 465 ASP R 53 REMARK 465 PRO R 54 REMARK 465 PRO R 55 REMARK 465 PRO R 56 REMARK 465 ALA R 57 REMARK 465 THR R 58 REMARK 465 ASP R 59 REMARK 465 LEU R 60 REMARK 465 PHE R 61 REMARK 465 CYS R 62 REMARK 465 ASN R 63 REMARK 465 ARG R 64 REMARK 465 THR R 65 REMARK 465 PHE R 66 REMARK 465 ASP R 67 REMARK 465 GLU R 68 REMARK 465 TYR R 69 REMARK 465 ALA R 70 REMARK 465 CYS R 71 REMARK 465 TRP R 72 REMARK 465 PRO R 73 REMARK 465 ASP R 74 REMARK 465 GLY R 75 REMARK 465 GLU R 76 REMARK 465 PRO R 77 REMARK 465 GLY R 78 REMARK 465 SER R 79 REMARK 465 PHE R 80 REMARK 465 VAL R 81 REMARK 465 ASN R 82 REMARK 465 VAL R 83 REMARK 465 SER R 84 REMARK 465 CYS R 85 REMARK 465 PRO R 86 REMARK 465 TRP R 87 REMARK 465 TYR R 88 REMARK 465 LEU R 89 REMARK 465 PRO R 90 REMARK 465 TRP R 91 REMARK 465 ALA R 92 REMARK 465 SER R 93 REMARK 465 SER R 94 REMARK 465 VAL R 95 REMARK 465 PRO R 96 REMARK 465 GLN R 97 REMARK 465 GLY R 98 REMARK 465 HIS R 99 REMARK 465 VAL R 100 REMARK 465 TYR R 101 REMARK 465 ARG R 102 REMARK 465 PHE R 103 REMARK 465 CYS R 104 REMARK 465 THR R 105 REMARK 465 ALA R 106 REMARK 465 GLU R 107 REMARK 465 GLY R 108 REMARK 465 LEU R 109 REMARK 465 TRP R 110 REMARK 465 LEU R 111 REMARK 465 GLN R 112 REMARK 465 LYS R 113 REMARK 465 ASP R 114 REMARK 465 ASN R 115 REMARK 465 SER R 116 REMARK 465 SER R 117 REMARK 465 LEU R 118 REMARK 465 PRO R 119 REMARK 465 TRP R 120 REMARK 465 ARG R 121 REMARK 465 ASP R 122 REMARK 465 LEU R 123 REMARK 465 SER R 124 REMARK 465 GLU R 125 REMARK 465 CYS R 126 REMARK 465 GLU R 127 REMARK 465 GLU R 128 REMARK 465 SER R 129 REMARK 465 LYS R 130 REMARK 465 ARG R 131 REMARK 465 GLY R 132 REMARK 465 GLU R 133 REMARK 465 ARG R 134 REMARK 465 SER R 135 REMARK 465 SER R 136 REMARK 465 ASN R 338 REMARK 465 LEU R 339 REMARK 465 MET R 340 REMARK 465 CYS R 341 REMARK 465 LYS R 342 REMARK 465 THR R 343 REMARK 465 HIS R 424 REMARK 465 LEU R 425 REMARK 465 HIS R 426 REMARK 465 ILE R 427 REMARK 465 GLN R 428 REMARK 465 ARG R 429 REMARK 465 ASP R 430 REMARK 465 SER R 431 REMARK 465 SER R 432 REMARK 465 MET R 433 REMARK 465 LYS R 434 REMARK 465 PRO R 435 REMARK 465 LEU R 436 REMARK 465 LYS R 437 REMARK 465 CYS R 438 REMARK 465 PRO R 439 REMARK 465 THR R 440 REMARK 465 SER R 441 REMARK 465 SER R 442 REMARK 465 LEU R 443 REMARK 465 SER R 444 REMARK 465 SER R 445 REMARK 465 GLY R 446 REMARK 465 ALA R 447 REMARK 465 THR R 448 REMARK 465 ALA R 449 REMARK 465 GLY R 450 REMARK 465 SER R 451 REMARK 465 SER R 452 REMARK 465 MET R 453 REMARK 465 TYR R 454 REMARK 465 THR R 455 REMARK 465 ALA R 456 REMARK 465 THR R 457 REMARK 465 CYS R 458 REMARK 465 GLN R 459 REMARK 465 ALA R 460 REMARK 465 SER R 461 REMARK 465 CYS R 462 REMARK 465 SER R 463 REMARK 465 PRO R 464 REMARK 465 ALA R 465 REMARK 465 GLY R 466 REMARK 465 LEU R 467 REMARK 465 GLU R 468 REMARK 465 VAL R 469 REMARK 465 LEU R 470 REMARK 465 PHE R 471 REMARK 465 GLN R 472 REMARK 465 GLY R 473 REMARK 465 PRO R 474 REMARK 465 HIS R 475 REMARK 465 HIS R 476 REMARK 465 HIS R 477 REMARK 465 HIS R 478 REMARK 465 HIS R 479 REMARK 465 HIS R 480 REMARK 465 HIS R 481 REMARK 465 HIS R 482 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 LEUAP 282 31.42 -94.43 REMARK 500 ARGAP 317 50.89 -95.61 REMARK 500 ASPAP 331 139.82 -172.11 REMARK 500 THRAP 350 33.63 -96.45 REMARK 500 THRBP 34 40.09 -102.43 REMARK 500 LYSBP 127 36.39 -96.34 REMARK 500 PHEBP 292 4.97 82.16 REMARK 500 ALABP 302 -0.10 68.24 REMARK 500 ASPNP 50 149.96 -170.82 REMARK 500 ASPNP 109 31.66 -143.52 REMARK 500 TYRNP 117 50.69 -96.14 REMARK 500 LYSRP 336 51.16 -90.69 REMARK 500 PHERP 381 -35.55 -131.54 REMARK 500 CYSRP 403 -54.64 -122.07 REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue N2V RP 501 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-20179 RELATED DB: EMDB REMARK 900 NON-PEPTIDE AGONIST (TT-OAD2) BOUND TO THE GLUCAGON-LIKE PPEPTIDE-1 REMARK 900 (GLP-1) RECEPTOR DBREF 6ORVAP 1 394 UNP P63092 GNAS2_HUMAN 1 394 DBREF 6ORVBP 2 340 UNP P62873 GBB1_HUMAN 2 340 DBREF 6ORVGP 1 71 UNP P59768 GBG2_HUMAN 1 71 DBREF 6ORVNP 1 138 PDB 6ORV 6ORV 1 138 DBREF 6ORVRP 24 463 UNP P43220 GLP1R_HUMAN 24 463 SEQADV 6ORV ASNAP 54 UNP P63092 SER 54 CONFLICT SEQADV 6ORV ALAAP 226 UNP P63092 GLY 226 CONFLICT SEQADV 6ORV ALAAP 268 UNP P63092 GLU 268 CONFLICT SEQADV 6ORV LYSAP 271 UNP P63092 ASN 271 CONFLICT SEQADV 6ORV ASPAP 274 UNP P63092 LYS 274 CONFLICT SEQADV 6ORV LYSAP 280 UNP P63092 ARG 280 CONFLICT SEQADV 6ORV ASPAP 284 UNP P63092 THR 284 CONFLICT SEQADV 6ORV THRAP 285 UNP P63092 ILE 285 CONFLICT SEQADV 6ORV METBP -9 UNP P62873 EXPRESSION TAG SEQADV 6ORV HISBP -8 UNP P62873 EXPRESSION TAG SEQADV 6ORV HISBP -7 UNP P62873 EXPRESSION TAG SEQADV 6ORV HISBP -6 UNP P62873 EXPRESSION TAG SEQADV 6ORV HISBP -5 UNP P62873 EXPRESSION TAG SEQADV 6ORV HISBP -4 UNP P62873 EXPRESSION TAG SEQADV 6ORV HISBP -3 UNP P62873 EXPRESSION TAG SEQADV 6ORV GLYBP -2 UNP P62873 EXPRESSION TAG SEQADV 6ORV SERBP -1 UNP P62873 EXPRESSION TAG SEQADV 6ORV SERBP 0 UNP P62873 EXPRESSION TAG SEQADV 6ORV GLYBP 1 UNP P62873 EXPRESSION TAG SEQADV 6ORV METRP -8 UNP P43220 INITIATING METHIONINE SEQADV 6ORV LYSRP -7 UNP P43220 EXPRESSION TAG SEQADV 6ORV THRRP -6 UNP P43220 EXPRESSION TAG SEQADV 6ORV ILERP -5 UNP P43220 EXPRESSION TAG SEQADV 6ORV ILERP -4 UNP P43220 EXPRESSION TAG SEQADV 6ORV ALARP -3 UNP P43220 EXPRESSION TAG SEQADV 6ORV LEURP -2 UNP P43220 EXPRESSION TAG SEQADV 6ORV SERRP -1 UNP P43220 EXPRESSION TAG SEQADV 6ORV TYRRP 0 UNP P43220 EXPRESSION TAG SEQADV 6ORV ILERP 1 UNP P43220 EXPRESSION TAG SEQADV 6ORV PHERP 2 UNP P43220 EXPRESSION TAG SEQADV 6ORV CYSRP 3 UNP P43220 EXPRESSION TAG SEQADV 6ORV LEURP 4 UNP P43220 EXPRESSION TAG SEQADV 6ORV VALRP 5 UNP P43220 EXPRESSION TAG SEQADV 6ORV PHERP 6 UNP P43220 EXPRESSION TAG SEQADV 6ORV ALARP 7 UNP P43220 EXPRESSION TAG SEQADV 6ORV ASPRP 8 UNP P43220 EXPRESSION TAG SEQADV 6ORV TYRRP 9 UNP P43220 EXPRESSION TAG SEQADV 6ORV LYSRP 10 UNP P43220 EXPRESSION TAG SEQADV 6ORV ASPRP 11 UNP P43220 EXPRESSION TAG SEQADV 6ORV ASPRP 12 UNP P43220 EXPRESSION TAG SEQADV 6ORV ASPRP 13 UNP P43220 EXPRESSION TAG SEQADV 6ORV ASPRP 14 UNP P43220 EXPRESSION TAG SEQADV 6ORV LEURP 15 UNP P43220 EXPRESSION TAG SEQADV 6ORV GLURP 16 UNP P43220 EXPRESSION TAG SEQADV 6ORV VALRP 17 UNP P43220 EXPRESSION TAG SEQADV 6ORV LEURP 18 UNP P43220 EXPRESSION TAG SEQADV 6ORV PHERP 19 UNP P43220 EXPRESSION TAG SEQADV 6ORV GLNRP 20 UNP P43220 EXPRESSION TAG SEQADV 6ORV GLYRP 21 UNP P43220 EXPRESSION TAG SEQADV 6ORV PRORP 22 UNP P43220 EXPRESSION TAG SEQADV 6ORV ALARP 23 UNP P43220 EXPRESSION TAG SEQADV 6ORV PHERP 260 UNP P43220 LEU 260 CONFLICT SEQADV 6ORV PRORP 464 UNP P43220 EXPRESSION TAG SEQADV 6ORV ALARP 465 UNP P43220 EXPRESSION TAG SEQADV 6ORV GLYRP 466 UNP P43220 EXPRESSION TAG SEQADV 6ORV LEURP 467 UNP P43220 EXPRESSION TAG SEQADV 6ORV GLURP 468 UNP P43220 EXPRESSION TAG SEQADV 6ORV VALRP 469 UNP P43220 EXPRESSION TAG SEQADV 6ORV LEURP 470 UNP P43220 EXPRESSION TAG SEQADV 6ORV PHERP 471 UNP P43220 EXPRESSION TAG SEQADV 6ORV GLNRP 472 UNP P43220 EXPRESSION TAG SEQADV 6ORV GLYRP 473 UNP P43220 EXPRESSION TAG SEQADV 6ORV PRORP 474 UNP P43220 EXPRESSION TAG SEQADV 6ORV HISRP 475 UNP P43220 EXPRESSION TAG SEQADV 6ORV HISRP 476 UNP P43220 EXPRESSION TAG SEQADV 6ORV HISRP 477 UNP P43220 EXPRESSION TAG SEQADV 6ORV HISRP 478 UNP P43220 EXPRESSION TAG SEQADV 6ORV HISRP 479 UNP P43220 EXPRESSION TAG SEQADV 6ORV HISRP 480 UNP P43220 EXPRESSION TAG SEQADV 6ORV HISRP 481 UNP P43220 EXPRESSION TAG SEQADV 6ORV HISRP 482 UNP P43220 EXPRESSION TAG SEQRES 1AP 394 MET GLY CYS LEU GLY ASN SER LYS THR GLU ASP GLN ARG SEQRES 2AP 394 ASN GLU GLU LYS ALA GLN ARG GLU ALA ASN LYS LYS ILE SEQRES 3AP 394 GLU LYS GLN LEU GLN LYS ASP LYS GLN VAL TYR ARG ALA SEQRES 4AP 394 THR HIS ARG LEU LEU LEU LEU GLY ALA GLY GLU SER GLY SEQRES 5AP 394 LYS ASN THR ILE VAL LYS GLN MET ARG ILE LEU HIS VAL SEQRES 6AP 394 ASN GLY PHE ASN GLY GLU GLY GLY GLU GLU ASP PRO GLN SEQRES 7AP 394 ALA ALA ARG SER ASN SER ASP GLY GLU LYS ALA THR LYS SEQRES 8AP 394 VAL GLN ASP ILE LYS ASN ASN LEU LYS GLU ALA ILE GLU SEQRES 9AP 394 THR ILE VAL ALA ALA MET SER ASN LEU VAL PRO PRO VAL SEQRES 10AP 394 GLU LEU ALA ASN PRO GLU ASN GLN PHE ARG VAL ASP TYR SEQRES 11AP 394 ILE LEU SER VAL MET ASN VAL PRO ASP PHE ASP PHE PRO SEQRES 12AP 394 PRO GLU PHE TYR GLU HIS ALA LYS ALA LEU TRP GLU ASP SEQRES 13AP 394 GLU GLY VAL ARG ALA CYS TYR GLU ARG SER ASN GLU TYR SEQRES 14AP 394 GLN LEU ILE ASP CYS ALA GLN TYR PHE LEU ASP LYS ILE SEQRES 15AP 394 ASP VAL ILE LYS GLN ALA ASP TYR VAL PRO SER ASP GLN SEQRES 16AP 394 ASP LEU LEU ARG CYS ARG VAL LEU THR SER GLY ILE PHE SEQRES 17AP 394 GLU THR LYS PHE GLN VAL ASP LYS VAL ASN PHE HIS MET SEQRES 18AP 394 PHE ASP VAL GLY ALA GLN ARG ASP GLU ARG ARG LYS TRP SEQRES 19AP 394 ILE GLN CYS PHE ASN ASP VAL THR ALA ILE ILE PHE VAL SEQRES 20AP 394 VAL ALA SER SER SER TYR ASN MET VAL ILE ARG GLU ASP SEQRES 21AP 394 ASN GLN THR ASN ARG LEU GLN ALA ALA LEU LYS LEU PHE SEQRES 22AP 394 ASP SER ILE TRP ASN ASN LYS TRP LEU ARG ASP THR SER SEQRES 23AP 394 VAL ILE LEU PHE LEU ASN LYS GLN ASP LEU LEU ALA GLU SEQRES 24AP 394 LYS VAL LEU ALA GLY LYS SER LYS ILE GLU ASP TYR PHE SEQRES 25AP 394 PRO GLU PHE ALA ARG TYR THR THR PRO GLU ASP ALA THR SEQRES 26AP 394 PRO GLU PRO GLY GLU ASP PRO ARG VAL THR ARG ALA LYS SEQRES 27AP 394 TYR PHE ILE ARG ASP GLU PHE LEU ARG ILE SER THR ALA SEQRES 28AP 394 SER GLY ASP GLY ARG HIS TYR CYS TYR PRO HIS PHE THR SEQRES 29AP 394 CYS ALA VAL ASP THR GLU ASN ILE ARG ARG VAL PHE ASN SEQRES 30AP 394 ASP CYS ARG ASP ILE ILE GLN ARG MET HIS LEU ARG GLN SEQRES 31AP 394 TYR GLU LEU LEU SEQRES 1BP 350 MET HIS HIS HIS HIS HIS HIS GLY SER SER GLY SER GLU SEQRES 2BP 350 LEU ASP GLN LEU ARG GLN GLU ALA GLU GLN LEU LYS ASN SEQRES 3BP 350 GLN ILE ARG ASP ALA ARG LYS ALA CYS ALA ASP ALA THR SEQRES 4BP 350 LEU SER GLN ILE THR ASN ASN ILE ASP PRO VAL GLY ARG SEQRES 5BP 350 ILE GLN MET ARG THR ARG ARG THR LEU ARG GLY HIS LEU SEQRES 6BP 350 ALA LYS ILE TYR ALA MET HIS TRP GLY THR ASP SER ARG SEQRES 7BP 350 LEU LEU VAL SER ALA SER GLN ASP GLY LYS LEU ILE ILE SEQRES 8BP 350 TRP ASP SER TYR THR THR ASN LYS VAL HIS ALA ILE PRO SEQRES 9BP 350 LEU ARG SER SER TRP VAL MET THR CYS ALA TYR ALA PRO SEQRES 10BP 350 SER GLY ASN TYR VAL ALA CYS GLY GLY LEU ASP ASN ILE SEQRES 11BP 350 CYS SER ILE TYR ASN LEU LYS THR ARG GLU GLY ASN VAL SEQRES 12BP 350 ARG VAL SER ARG GLU LEU ALA GLY HIS THR GLY TYR LEU SEQRES 13BP 350 SER CYS CYS ARG PHE LEU ASP ASP ASN GLN ILE VAL THR SEQRES 14BP 350 SER SER GLY ASP THR THR CYS ALA LEU TRP ASP ILE GLU SEQRES 15BP 350 THR GLY GLN GLN THR THR THR PHE THR GLY HIS THR GLY SEQRES 16BP 350 ASP VAL MET SER LEU SER LEU ALA PRO ASP THR ARG LEU SEQRES 17BP 350 PHE VAL SER GLY ALA CYS ASP ALA SER ALA LYS LEU TRP SEQRES 18BP 350 ASP VAL ARG GLU GLY MET CYS ARG GLN THR PHE THR GLY SEQRES 19BP 350 HIS GLU SER ASP ILE ASN ALA ILE CYS PHE PHE PRO ASN SEQRES 20BP 350 GLY ASN ALA PHE ALA THR GLY SER ASP ASP ALA THR CYS SEQRES 21BP 350 ARG LEU PHE ASP LEU ARG ALA ASP GLN GLU LEU MET THR SEQRES 22BP 350 TYR SER HIS ASP ASN ILE ILE CYS GLY ILE THR SER VAL SEQRES 23BP 350 SER PHE SER LYS SER GLY ARG LEU LEU LEU ALA GLY TYR SEQRES 24BP 350 ASP ASP PHE ASN CYS ASN VAL TRP ASP ALA LEU LYS ALA SEQRES 25BP 350 ASP ARG ALA GLY VAL LEU ALA GLY HIS ASP ASN ARG VAL SEQRES 26BP 350 SER CYS LEU GLY VAL THR ASP ASP GLY MET ALA VAL ALA SEQRES 27BP 350 THR GLY SER TRP ASP SER PHE LEU LYS ILE TRP ASN SEQRES 1GP 71 MET ALA SER ASN ASN THR ALA SER ILE ALA GLN ALA ARG SEQRES 2GP 71 LYS LEU VAL GLU GLN LEU LYS MET GLU ALA ASN ILE ASP SEQRES 3GP 71 ARG ILE LYS VAL SER LYS ALA ALA ALA ASP LEU MET ALA SEQRES 4GP 71 TYR CYS GLU ALA HIS ALA LYS GLU ASP PRO LEU LEU THR SEQRES 5GP 71 PRO VAL PRO ALA SER GLU ASN PRO PHE ARG GLU LYS LYS SEQRES 6GP 71 PHE PHE CYS ALA ILE LEU SEQRES 1NP 138 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2NP 138 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3NP 138 PHE THR PHE SER ASN TYR LYS MET ASN TRP VAL ARG GLN SEQRES 4NP 138 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER ASP ILE SER SEQRES 5NP 138 GLN SER GLY ALA SER ILE SER TYR THR GLY SER VAL LYS SEQRES 6NP 138 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR SEQRES 7NP 138 LEU TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR SEQRES 8NP 138 ALA VAL TYR TYR CYS ALA ARG CYS PRO ALA PRO PHE THR SEQRES 9NP 138 ARG ASP CYS PHE ASP VAL THR SER THR THR TYR ALA TYR SEQRES 10NP 138 ARG GLY GLN GLY THR GLN VAL THR VAL SER SER HIS HIS SEQRES 11NP 138 HIS HIS HIS HIS GLU PRO GLU ALA SEQRES 1RP 491 MET LYS THR ILE ILE ALA LEU SER TYR ILE PHE CYS LEU SEQRES 2RP 491 VAL PHE ALA ASP TYR LYS ASP ASP ASP ASP LEU GLU VAL SEQRES 3RP 491 LEU PHE GLN GLY PRO ALA ARG PRO GLN GLY ALA THR VAL SEQRES 4RP 491 SER LEU TRP GLU THR VAL GLN LYS TRP ARG GLU TYR ARG SEQRES 5RP 491 ARG GLN CYS GLN ARG SER LEU THR GLU ASP PRO PRO PRO SEQRES 6RP 491 ALA THR ASP LEU PHE CYS ASN ARG THR PHE ASP GLU TYR SEQRES 7RP 491 ALA CYS TRP PRO ASP GLY GLU PRO GLY SER PHE VAL ASN SEQRES 8RP 491 VAL SER CYS PRO TRP TYR LEU PRO TRP ALA SER SER VAL SEQRES 9RP 491 PRO GLN GLY HIS VAL TYR ARG PHE CYS THR ALA GLU GLY SEQRES 10RP 491 LEU TRP LEU GLN LYS ASP ASN SER SER LEU PRO TRP ARG SEQRES 11RP 491 ASP LEU SER GLU CYS GLU GLU SER LYS ARG GLY GLU ARG SEQRES 12RP 491 SER SER PRO GLU GLU GLN LEU LEU PHE LEU TYR ILE ILE SEQRES 13RP 491 TYR THR VAL GLY TYR ALA LEU SER PHE SER ALA LEU VAL SEQRES 14RP 491 ILE ALA SER ALA ILE LEU LEU GLY PHE ARG HIS LEU HIS SEQRES 15RP 491 CYS THR ARG ASN TYR ILE HIS LEU ASN LEU PHE ALA SER SEQRES 16RP 491 PHE ILE LEU ARG ALA LEU SER VAL PHE ILE LYS ASP ALA SEQRES 17RP 491 ALA LEU LYS TRP MET TYR SER THR ALA ALA GLN GLN HIS SEQRES 18RP 491 GLN TRP ASP GLY LEU LEU SER TYR GLN ASP SER LEU SER SEQRES 19RP 491 CYS ARG LEU VAL PHE LEU LEU MET GLN TYR CYS VAL ALA SEQRES 20RP 491 ALA ASN TYR TYR TRP LEU LEU VAL GLU GLY VAL TYR LEU SEQRES 21RP 491 TYR THR LEU LEU ALA PHE SER VAL PHE SER GLU GLN TRP SEQRES 22RP 491 ILE PHE ARG LEU TYR VAL SER ILE GLY TRP GLY VAL PRO SEQRES 23RP 491 LEU LEU PHE VAL VAL PRO TRP GLY ILE VAL LYS TYR LEU SEQRES 24RP 491 TYR GLU ASP GLU GLY CYS TRP THR ARG ASN SER ASN MET SEQRES 25RP 491 ASN TYR TRP LEU ILE ILE ARG LEU PRO ILE LEU PHE ALA SEQRES 26RP 491 ILE GLY VAL ASN PHE LEU ILE PHE VAL ARG VAL ILE CYS SEQRES 27RP 491 ILE VAL VAL SER LYS LEU LYS ALA ASN LEU MET CYS LYS SEQRES 28RP 491 THR ASP ILE LYS CYS ARG LEU ALA LYS SER THR LEU THR SEQRES 29RP 491 LEU ILE PRO LEU LEU GLY THR HIS GLU VAL ILE PHE ALA SEQRES 30RP 491 PHE VAL MET ASP GLU HIS ALA ARG GLY THR LEU ARG PHE SEQRES 31RP 491 ILE LYS LEU PHE THR GLU LEU SER PHE THR SER PHE GLN SEQRES 32RP 491 GLY LEU MET VAL ALA ILE LEU TYR CYS PHE VAL ASN ASN SEQRES 33RP 491 GLU VAL GLN LEU GLU PHE ARG LYS SER TRP GLU ARG TRP SEQRES 34RP 491 ARG LEU GLU HIS LEU HIS ILE GLN ARG ASP SER SER MET SEQRES 35RP 491 LYS PRO LEU LYS CYS PRO THR SER SER LEU SER SER GLY SEQRES 36RP 491 ALA THR ALA GLY SER SER MET TYR THR ALA THR CYS GLN SEQRES 37RP 491 ALA SER CYS SER PRO ALA GLY LEU GLU VAL LEU PHE GLN SEQRES 38RP 491 GLY PRO HIS HIS HIS HIS HIS HIS HIS HIS HET N2V RP 501 61 FORMUL 6 N2V HELIX 1 AA1 ALAAP 18 LYSAP 25 1 8 HELIX 2 AA2 LYSAP 28 ARGAP 38 1 11 HELIX 3 AA3 TRPAP 234 ASPAP 240 5 7 HELIX 4 AA4 LEUAP 266 ASNAP 279 1 14 HELIX 5 AA5 PHEAP 312 ALAAP 316 5 5 HELIX 6 AA6 ASPAP 331 ARGAP 336 1 6 HELIX 7 AA7 ALAAP 337 THRAP 350 1 14 HELIX 8 AA8 ILEAP 372 TYRAP 391 1 20 HELIX 9 AA9 LEUBP 4 ALABP 24 1 21 HELIX 10 AB1 THRBP 29 THRBP 34 1 6 HELIX 11 AB2 ALAGP 7 GLUGP 22 1 16 HELIX 12 AB3 LYSGP 29 HISGP 44 1 16 HELIX 13 AB4 ALAGP 45 ASPGP 48 5 4 HELIX 14 AB5 THRNP 28 TYRNP 32 5 5 HELIX 15 AB6 LYSNP 87 THRNP 91 5 5 HELIX 16 AB7 GLURP 138 PHERP 169 1 32 HELIX 17 AB8 ARGRP 170 HISRP 173 5 4 HELIX 18 AB9 ARGRP 176 THRRP 207 1 32 HELIX 19 AC1 TRPRP 214 ASPRP 222 1 9 HELIX 20 AC2 SERRP 223 ALARP 239 1 17 HELIX 21 AC3 GLURP 247 ALARP 256 1 10 HELIX 22 AC4 GLNRP 263 GLYRP 273 1 11 HELIX 23 AC5 VALRP 276 PHERP 280 5 5 HELIX 24 AC6 VALRP 281 TYRRP 291 1 11 HELIX 25 AC7 ILERP 309 ASNRP 320 1 12 HELIX 26 AC8 ILERP 323 LEURP 335 1 13 HELIX 27 AC9 ARGRP 348 GLYRP 361 1 14 HELIX 28 AD1 THRRP 362 PHERP 367 1 6 HELIX 29 AD2 ILERP 382 PHERP 390 1 9 HELIX 30 AD3 PHERP 393 LEURP 401 1 9 HELIX 31 AD4 ASNRP 406 LEURP 411 1 6 HELIX 32 AD5 TRPRP 417 LEURP 422 1 6 SHEET 1 AA1 6 ILEAP 207 VALAP 214 0 SHEET 2 AA1 6 VALAP 217 VALAP 224 -1 O PHEAP 219 N PHEAP 212 SHEET 3 AA1 6 HISAP 41 LEUAP 46 1 N HISAP 41 O HISAP 220 SHEET 4 AA1 6 ALAAP 243 VALAP 248 1 O ILEAP 245 N LEUAP 44 SHEET 5 AA1 6 SERAP 286 LEUAP 291 1 O PHEAP 290 N VALAP 248 SHEET 6 AA1 6 CYSAP 359 PHEAP 363 1 O HISAP 362 N LEUAP 289 SHEET 1 AA2 3 ARGBP 46 THRBP 47 0 SHEET 2 AA2 3 PHEBP 335 ASNBP 340 -1 O ASNBP 340 N ARGBP 46 SHEET 3 AA2 3 LEUBP 51 ARGBP 52 -1 N LEUBP 51 O LEUBP 336 SHEET 1 AA3 4 ARGBP 46 THRBP 47 0 SHEET 2 AA3 4 PHEBP 335 ASNBP 340 -1 O ASNBP 340 N ARGBP 46 SHEET 3 AA3 4 VALBP 327 THRBP 329 -1 N VALBP 327 O TRPBP 339 SHEET 4 AA3 4 GLYBP 319 VALBP 320 -1 N GLYBP 319 O ALABP 328 SHEET 1 AA4 4 ILEBP 58 TRPBP 63 0 SHEET 2 AA4 4 LEUBP 69 SERBP 74 -1 O ALABP 73 N ALABP 60 SHEET 3 AA4 4 LYSBP 78 ASPBP 83 -1 O TRPBP 82 N LEUBP 70 SHEET 4 AA4 4 ASNBP 88 PROBP 94 -1 O VALBP 90 N ILEBP 81 SHEET 1 AA5 4 VALBP 100 TYRBP 105 0 SHEET 2 AA5 4 TYRBP 111 GLYBP 116 -1 O ALABP 113 N ALABP 104 SHEET 3 AA5 4 CYSBP 121 ASNBP 125 -1 O TYRBP 124 N VALBP 112 SHEET 4 AA5 4 ARGBP 134 LEUBP 139 -1 O SERBP 136 N ILEBP 123 SHEET 1 AA6 4 LEUBP 146 PHEBP 151 0 SHEET 2 AA6 4 ILEBP 157 SERBP 161 -1 O VALBP 158 N ARGBP 150 SHEET 3 AA6 4 CYSBP 166 TRPBP 169 -1 O TRPBP 169 N ILEBP 157 SHEET 4 AA6 4 GLNBP 176 PHEBP 180 -1 O THRBP 178 N LEUBP 168 SHEET 1 AA7 4 VALBP 187 LEUBP 192 0 SHEET 2 AA7 4 LEUBP 198 ALABP 203 -1 O GLYBP 202 N METBP 188 SHEET 3 AA7 4 ALABP 208 ASPBP 212 -1 O TRPBP 211 N PHEBP 199 SHEET 4 AA7 4 CYSBP 218 PHEBP 222 -1 O ARGBP 219 N LEUBP 210 SHEET 1 AA8 4 ILEBP 229 PHEBP 234 0 SHEET 2 AA8 4 ALABP 240 SERBP 245 -1 O ALABP 242 N CYSBP 233 SHEET 3 AA8 4 CYSBP 250 ASPBP 254 -1 O PHEBP 253 N PHEBP 241 SHEET 4 AA8 4 METBP 262 TYRBP 264 -1 O TYRBP 264 N CYSBP 250 SHEET 1 AA9 4 ILEBP 273 PHEBP 278 0 SHEET 2 AA9 4 LEUBP 284 TYRBP 289 -1 O GLYBP 288 N SERBP 275 SHEET 3 AA9 4 CYSBP 294 ASPBP 298 -1 O TRPBP 297 N LEUBP 285 SHEET 4 AA9 4 ARGBP 304 LEUBP 308 -1 O ALABP 305 N VALBP 296 SHEET 1 AB1 2 GLNNP 3 GLUNP 6 0 SHEET 2 AB1 2 CYSNP 22 SERNP 25 -1 O SERNP 25 N GLNNP 3 SHEET 1 AB2 6 GLYNP 10 LEUNP 11 0 SHEET 2 AB2 6 THRNP 122 THRNP 125 1 O THRNP 125 N GLYNP 10 SHEET 3 AB2 6 ALANP 92 TYRNP 95 -1 N TYRNP 94 O THRNP 122 SHEET 4 AB2 6 METNP 34 GLNNP 39 -1 N VALNP 37 O TYRNP 95 SHEET 5 AB2 6 LEUNP 45 ILENP 51 -1 O GLUNP 46 N ARGNP 38 SHEET 6 AB2 6 ILENP 58 TYRNP 60 -1 O SERNP 59 N ASPNP 50 SHEET 1 AB3 3 ARGNP 19 LEUNP 20 0 SHEET 2 AB3 3 THRNP 78 METNP 83 -1 O LEUNP 81 N LEUNP 20 SHEET 3 AB3 3 PHENP 68 ASPNP 73 -1 N SERNP 71 O TYRNP 80 SSBOND 1 CYSNP 22 CYSNP 96 1555 1555 2.03 SSBOND 2 CYSNP 99 CYSNP 107 1555 1555 2.02 SSBOND 3 CYSRP 226 CYSRP 296 1555 1555 2.05 SITE 1 AC1 12 TYRRP 145 TYRRP 148 VALRP 194 LYSRP 197 SITE 2 AC1 12 ALARP 200 LEURP 201 TRPRP 203 METRP 204 SITE 3 AC1 12 LEURP 217 TYRRP 220 PHERP 230 TRPRP 297 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