HEADER MEMBRANE PROTEIN 04-MAR-24 8YKD TITLE CRYO-EM STRUCTURE OF ADGRG2-GS COMPLEX WITH NTF NANOBODY COMPND MOL_ID: 1; COMPND 2 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(S) SUBUNIT ALPHA; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MUTATION: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(T) SUBUNIT COMPND 8 BETA-1; COMPND 9 CHAIN: B; COMPND 10 SYNONYM: TRANSDUCIN BETA CHAIN 1; COMPND 11 ENGINEERED: YES; COMPND 12 MOL_ID: 3; COMPND 13 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN SUBUNIT GAMMA; COMPND 14 CHAIN: G; COMPND 15 ENGINEERED: YES; COMPND 16 MOL_ID: 4; COMPND 17 MOLECULE: NANOBODY-35; COMPND 18 CHAIN: N; COMPND 19 ENGINEERED: YES; COMPND 20 MOL_ID: 5; COMPND 21 MOLECULE: ADHESION G-PROTEIN COUPLED RECEPTOR G2; COMPND 22 CHAIN: R; COMPND 23 SYNONYM: G-PROTEIN COUPLED RECEPTOR 64,MOUSE EPIDIDYMIS-SPECIFIC COMPND 24 PROTEIN 6,ME6; COMPND 25 ENGINEERED: YES; COMPND 26 MOL_ID: 6; COMPND 27 MOLECULE: SCFV-16; COMPND 28 CHAIN: S; COMPND 29 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SPODOPTERA; SOURCE 3 ORGANISM_TAXID: 7106; SOURCE 4 EXPRESSION_SYSTEM: BACULOVIRUS EXPRESSION VECTOR PFASTBAC1-HM; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 274590; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: SPODOPTERA; SOURCE 8 ORGANISM_TAXID: 7106; SOURCE 9 GENE: GNB1; SOURCE 10 EXPRESSION_SYSTEM: BACULOVIRUS EXPRESSION VECTOR PFASTBAC1-HM; SOURCE 11 EXPRESSION_SYSTEM_TAXID: 274590; SOURCE 12 MOL_ID: 3; SOURCE 13 ORGANISM_SCIENTIFIC: SPODOPTERA; SOURCE 14 ORGANISM_TAXID: 7106; SOURCE 15 GENE: MRHIFER1_005810; SOURCE 16 EXPRESSION_SYSTEM: BACULOVIRUS EXPRESSION VECTOR PFASTBAC1-HM; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 274590; SOURCE 18 MOL_ID: 4; SOURCE 19 ORGANISM_SCIENTIFIC: SPODOPTERA; SOURCE 20 ORGANISM_TAXID: 7106; SOURCE 21 EXPRESSION_SYSTEM: BACULOVIRUS EXPRESSION VECTOR PFASTBAC1-HM; SOURCE 22 EXPRESSION_SYSTEM_TAXID: 274590; SOURCE 23 MOL_ID: 5; SOURCE 24 ORGANISM_SCIENTIFIC: SPODOPTERA; SOURCE 25 ORGANISM_TAXID: 7106; SOURCE 26 GENE: ADGRG2, GPR64, ME6; SOURCE 27 EXPRESSION_SYSTEM: BACULOVIRUS EXPRESSION VECTOR PFASTBAC1-HM; SOURCE 28 EXPRESSION_SYSTEM_TAXID: 274590; SOURCE 29 MOL_ID: 6; SOURCE 30 ORGANISM_SCIENTIFIC: SPODOPTERA; SOURCE 31 ORGANISM_TAXID: 7106; SOURCE 32 EXPRESSION_SYSTEM: BACULOVIRUS EXPRESSION VECTOR PFASTBAC1-HM; SOURCE 33 EXPRESSION_SYSTEM_TAXID: 274590 KEYWDS GPCR, MEMBRANE PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR S.M.HUANG,G.SHENG-CHAO REVDAT 1 13-AUG-25 8YKD 0 JRNL AUTH Y.ZHENG,D.JIANG,Y.LU,C.ZHANG,S.M.HUANG,H.LIN,D.ZHANG,S.GUO, JRNL AUTH 2 J.HAN,J.CHEN,Y.HE,M.ZHANG,Y.GAO,Y.GUO,R.WEI,M.XIA,Y.QIN, JRNL AUTH 3 Z.LIU,F.YANG,S.GE,F.YI,X.YU,H.LIN,P.XIAO,J.P.SUN,S.FENG JRNL TITL DEVELOPMENT OF AN ALLOSTERIC ADHESION GPCR NANOBODY WITH JRNL TITL 2 THERAPEUTIC POTENTIAL JRNL REF NAT.CHEM.BIOL. 2025 JRNL REFN ESSN 1552-4469 JRNL DOI 10.1038/S41589-025-01896-2 REMARK 2 REMARK 2 RESOLUTION. 2.90 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : CRYOSPARC, PHENIX, CRYOSPARC 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) : 2.900 REMARK 3 NUMBER OF PARTICLES : 241188 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 8YKD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-MAR-24. REMARK 100 THE DEPOSITION ID IS D_1300045838. 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 : COMPLEX OF ADGRG2 WITH NANONODY REMARK 245 AND G PROTEIN TRIMER 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 TECNAI F30 REMARK 245 DETECTOR TYPE : GATAN K3 (6K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1200.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2200.00 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) : 6000.00 REMARK 245 ILLUMINATION MODE : OTHER 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, G, N, R, S 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 18 REMARK 465 GLY A 19 REMARK 465 CYS A 20 REMARK 465 THR A 21 REMARK 465 VAL A 91 REMARK 465 ASN A 92 REMARK 465 GLY A 93 REMARK 465 TYR A 94 REMARK 465 SER A 95 REMARK 465 GLU A 96 REMARK 465 GLU A 97 REMARK 465 GLU A 98 REMARK 465 CYS A 99 REMARK 465 LYS A 100 REMARK 465 GLN A 101 REMARK 465 TYR A 102 REMARK 465 LYS A 103 REMARK 465 ALA A 104 REMARK 465 VAL A 105 REMARK 465 VAL A 106 REMARK 465 TYR A 107 REMARK 465 SER A 108 REMARK 465 ASN A 109 REMARK 465 THR A 110 REMARK 465 ILE A 111 REMARK 465 GLN A 112 REMARK 465 SER A 113 REMARK 465 ILE A 114 REMARK 465 ILE A 115 REMARK 465 ALA A 116 REMARK 465 ILE A 117 REMARK 465 ILE A 118 REMARK 465 ARG A 119 REMARK 465 ALA A 120 REMARK 465 MET A 121 REMARK 465 GLY A 122 REMARK 465 ARG A 123 REMARK 465 LEU A 124 REMARK 465 LYS A 125 REMARK 465 ILE A 126 REMARK 465 ASP A 127 REMARK 465 PHE A 128 REMARK 465 GLY A 129 REMARK 465 ASP A 130 REMARK 465 SER A 131 REMARK 465 ALA A 132 REMARK 465 ARG A 133 REMARK 465 ALA A 134 REMARK 465 ASP A 135 REMARK 465 ASP A 136 REMARK 465 ALA A 137 REMARK 465 ARG A 138 REMARK 465 GLN A 139 REMARK 465 LEU A 140 REMARK 465 PHE A 141 REMARK 465 VAL A 142 REMARK 465 LEU A 143 REMARK 465 ALA A 144 REMARK 465 GLY A 145 REMARK 465 ALA A 146 REMARK 465 ALA A 147 REMARK 465 GLU A 148 REMARK 465 GLU A 149 REMARK 465 GLY A 150 REMARK 465 PHE A 151 REMARK 465 MET A 152 REMARK 465 THR A 153 REMARK 465 ALA A 154 REMARK 465 GLU A 155 REMARK 465 LEU A 156 REMARK 465 ALA A 157 REMARK 465 GLY A 158 REMARK 465 VAL A 159 REMARK 465 ILE A 160 REMARK 465 LYS A 161 REMARK 465 ARG A 162 REMARK 465 LEU A 163 REMARK 465 TRP A 164 REMARK 465 LYS A 165 REMARK 465 ASP A 166 REMARK 465 SER A 167 REMARK 465 GLY A 168 REMARK 465 VAL A 169 REMARK 465 GLN A 170 REMARK 465 ALA A 171 REMARK 465 CYS A 172 REMARK 465 PHE A 173 REMARK 465 ASN A 174 REMARK 465 ARG A 175 REMARK 465 SER A 176 REMARK 465 ARG A 177 REMARK 465 GLU A 178 REMARK 465 TYR A 179 REMARK 465 GLN A 180 REMARK 465 LEU A 181 REMARK 465 ASN A 182 REMARK 465 ASP A 183 REMARK 465 SER A 184 REMARK 465 ALA A 185 REMARK 465 ALA A 186 REMARK 465 TYR A 187 REMARK 465 TYR A 188 REMARK 465 LEU A 189 REMARK 465 ASN A 190 REMARK 465 ASP A 191 REMARK 465 LEU A 192 REMARK 465 ASP A 193 REMARK 465 ARG A 194 REMARK 465 ILE A 195 REMARK 465 ALA A 196 REMARK 465 GLN A 197 REMARK 465 PRO A 198 REMARK 465 ASN A 199 REMARK 465 TYR A 200 REMARK 465 ILE A 201 REMARK 465 PRO A 202 REMARK 465 THR A 203 REMARK 465 GLN A 204 REMARK 465 GLN A 205 REMARK 465 ASP A 206 REMARK 465 VAL A 207 REMARK 465 LEU A 208 REMARK 465 ARG A 209 REMARK 465 THR A 210 REMARK 465 ARG A 211 REMARK 465 VAL A 212 REMARK 465 LYS A 213 REMARK 465 THR A 214 REMARK 465 MET B -17 REMARK 465 HIS B -16 REMARK 465 HIS B -15 REMARK 465 HIS B -14 REMARK 465 HIS B -13 REMARK 465 HIS B -12 REMARK 465 HIS B -11 REMARK 465 LEU B -10 REMARK 465 GLU B -9 REMARK 465 VAL B -8 REMARK 465 LEU B -7 REMARK 465 PHE B -6 REMARK 465 GLN B -5 REMARK 465 GLY B -4 REMARK 465 PRO B -3 REMARK 465 GLY B -2 REMARK 465 SER B -1 REMARK 465 SER B 0 REMARK 465 GLY B 1 REMARK 465 SER B 2 REMARK 465 GLU B 3 REMARK 465 MET G -36 REMARK 465 TRP G -35 REMARK 465 ARG G -34 REMARK 465 GLU G -33 REMARK 465 LEU G -32 REMARK 465 PRO G -31 REMARK 465 LEU G -30 REMARK 465 GLY G -29 REMARK 465 LEU G -28 REMARK 465 GLY G -27 REMARK 465 GLU G -26 REMARK 465 LEU G -25 REMARK 465 HIS G -24 REMARK 465 LYS G -23 REMARK 465 ASP G -22 REMARK 465 HIS G -21 REMARK 465 GLN G -20 REMARK 465 ALA G -19 REMARK 465 SER G -18 REMARK 465 ARG G -17 REMARK 465 LYS G -16 REMARK 465 LEU G -15 REMARK 465 GLU G -14 REMARK 465 PRO G -13 REMARK 465 GLU G -12 REMARK 465 LEU G -11 REMARK 465 TRP G -10 REMARK 465 SER G -9 REMARK 465 VAL G -8 REMARK 465 SER G -7 REMARK 465 GLU G -6 REMARK 465 ASN G -5 REMARK 465 PRO G -4 REMARK 465 PRO G -3 REMARK 465 SER G -2 REMARK 465 THR G -1 REMARK 465 SER G 0 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 465 SER N 128 REMARK 465 MET R 14 REMARK 465 LYS R 15 REMARK 465 THR R 16 REMARK 465 ILE R 17 REMARK 465 ILE R 18 REMARK 465 ALA R 19 REMARK 465 LEU R 20 REMARK 465 SER R 21 REMARK 465 TYR R 22 REMARK 465 ILE R 23 REMARK 465 PHE R 24 REMARK 465 CYS R 25 REMARK 465 LEU R 26 REMARK 465 VAL R 27 REMARK 465 PHE R 28 REMARK 465 ALA R 29 REMARK 465 ASP R 30 REMARK 465 TYR R 31 REMARK 465 LYS R 32 REMARK 465 ASP R 33 REMARK 465 ASP R 34 REMARK 465 ASP R 35 REMARK 465 ASP R 36 REMARK 465 LYS R 37 REMARK 465 LEU R 38 REMARK 465 LYS R 39 REMARK 465 GLU R 40 REMARK 465 ASN R 41 REMARK 465 GLY R 42 REMARK 465 ASN R 43 REMARK 465 SER R 44 REMARK 465 SER R 45 REMARK 465 LEU R 46 REMARK 465 LEU R 47 REMARK 465 SER R 48 REMARK 465 PRO R 49 REMARK 465 SER R 50 REMARK 465 ALA R 51 REMARK 465 GLU R 52 REMARK 465 SER R 53 REMARK 465 SER R 54 REMARK 465 LEU R 55 REMARK 465 VAL R 56 REMARK 465 SER R 57 REMARK 465 LEU R 58 REMARK 465 ILE R 59 REMARK 465 PRO R 60 REMARK 465 TYR R 61 REMARK 465 SER R 62 REMARK 465 ASN R 63 REMARK 465 GLY R 64 REMARK 465 THR R 65 REMARK 465 PRO R 66 REMARK 465 ASP R 67 REMARK 465 ALA R 68 REMARK 465 ALA R 69 REMARK 465 SER R 70 REMARK 465 GLU R 71 REMARK 465 VAL R 72 REMARK 465 LEU R 73 REMARK 465 SER R 74 REMARK 465 THR R 75 REMARK 465 LEU R 76 REMARK 465 ASN R 77 REMARK 465 LYS R 78 REMARK 465 THR R 79 REMARK 465 GLU R 80 REMARK 465 LYS R 81 REMARK 465 SER R 82 REMARK 465 LYS R 83 REMARK 465 ILE R 84 REMARK 465 THR R 85 REMARK 465 ILE R 86 REMARK 465 VAL R 87 REMARK 465 LYS R 88 REMARK 465 THR R 89 REMARK 465 PHE R 90 REMARK 465 ASN R 91 REMARK 465 ALA R 92 REMARK 465 SER R 93 REMARK 465 GLY R 94 REMARK 465 VAL R 95 REMARK 465 LYS R 96 REMARK 465 SER R 97 REMARK 465 GLN R 98 REMARK 465 ARG R 99 REMARK 465 ASN R 100 REMARK 465 ILE R 101 REMARK 465 CYS R 102 REMARK 465 ASN R 103 REMARK 465 LEU R 104 REMARK 465 SER R 105 REMARK 465 SER R 106 REMARK 465 LEU R 107 REMARK 465 CYS R 108 REMARK 465 ASN R 109 REMARK 465 ASP R 110 REMARK 465 SER R 111 REMARK 465 VAL R 112 REMARK 465 PHE R 113 REMARK 465 PHE R 114 REMARK 465 ARG R 115 REMARK 465 GLY R 116 REMARK 465 GLU R 117 REMARK 465 ILE R 118 REMARK 465 VAL R 119 REMARK 465 PHE R 120 REMARK 465 GLN R 121 REMARK 465 HIS R 122 REMARK 465 ASP R 123 REMARK 465 GLU R 124 REMARK 465 ASP R 125 REMARK 465 HIS R 126 REMARK 465 ASN R 127 REMARK 465 VAL R 128 REMARK 465 THR R 129 REMARK 465 GLN R 130 REMARK 465 ASN R 131 REMARK 465 GLN R 132 REMARK 465 ASP R 133 REMARK 465 THR R 134 REMARK 465 ALA R 135 REMARK 465 ASN R 136 REMARK 465 GLY R 137 REMARK 465 THR R 138 REMARK 465 PHE R 139 REMARK 465 ALA R 140 REMARK 465 GLY R 141 REMARK 465 VAL R 142 REMARK 465 LEU R 143 REMARK 465 SER R 144 REMARK 465 LEU R 145 REMARK 465 SER R 146 REMARK 465 GLU R 147 REMARK 465 LEU R 148 REMARK 465 LYS R 149 REMARK 465 ARG R 150 REMARK 465 SER R 151 REMARK 465 GLU R 152 REMARK 465 LEU R 153 REMARK 465 ASN R 154 REMARK 465 LYS R 155 REMARK 465 THR R 156 REMARK 465 LEU R 157 REMARK 465 GLN R 158 REMARK 465 THR R 159 REMARK 465 LEU R 160 REMARK 465 SER R 161 REMARK 465 GLU R 162 REMARK 465 THR R 163 REMARK 465 TYR R 164 REMARK 465 PHE R 165 REMARK 465 ILE R 166 REMARK 465 VAL R 167 REMARK 465 CYS R 168 REMARK 465 ALA R 169 REMARK 465 THR R 170 REMARK 465 ALA R 171 REMARK 465 GLU R 172 REMARK 465 ALA R 173 REMARK 465 GLN R 174 REMARK 465 SER R 175 REMARK 465 THR R 176 REMARK 465 VAL R 177 REMARK 465 ASN R 178 REMARK 465 CYS R 179 REMARK 465 THR R 180 REMARK 465 PHE R 181 REMARK 465 THR R 182 REMARK 465 VAL R 183 REMARK 465 LYS R 184 REMARK 465 LEU R 185 REMARK 465 ASN R 186 REMARK 465 GLU R 187 REMARK 465 THR R 188 REMARK 465 MET R 189 REMARK 465 ASN R 190 REMARK 465 VAL R 191 REMARK 465 CYS R 192 REMARK 465 ALA R 193 REMARK 465 MET R 194 REMARK 465 MET R 195 REMARK 465 VAL R 196 REMARK 465 THR R 197 REMARK 465 PHE R 198 REMARK 465 GLN R 199 REMARK 465 THR R 200 REMARK 465 VAL R 201 REMARK 465 GLN R 202 REMARK 465 ILE R 203 REMARK 465 ARG R 204 REMARK 465 PRO R 205 REMARK 465 MET R 206 REMARK 465 GLU R 207 REMARK 465 GLN R 208 REMARK 465 CYS R 209 REMARK 465 CYS R 210 REMARK 465 CYS R 211 REMARK 465 SER R 212 REMARK 465 PRO R 213 REMARK 465 ARG R 214 REMARK 465 THR R 215 REMARK 465 PRO R 216 REMARK 465 CYS R 217 REMARK 465 PRO R 218 REMARK 465 SER R 219 REMARK 465 SER R 220 REMARK 465 PRO R 221 REMARK 465 GLU R 222 REMARK 465 GLU R 223 REMARK 465 LEU R 224 REMARK 465 GLU R 225 REMARK 465 LYS R 226 REMARK 465 LEU R 227 REMARK 465 GLN R 228 REMARK 465 CYS R 229 REMARK 465 GLU R 230 REMARK 465 LEU R 231 REMARK 465 GLN R 232 REMARK 465 ASP R 233 REMARK 465 PRO R 234 REMARK 465 ILE R 235 REMARK 465 VAL R 236 REMARK 465 CYS R 237 REMARK 465 LEU R 238 REMARK 465 ALA R 239 REMARK 465 ASP R 240 REMARK 465 GLN R 241 REMARK 465 PRO R 242 REMARK 465 HIS R 243 REMARK 465 GLY R 244 REMARK 465 PRO R 245 REMARK 465 PRO R 246 REMARK 465 LEU R 247 REMARK 465 SER R 248 REMARK 465 SER R 249 REMARK 465 SER R 250 REMARK 465 SER R 251 REMARK 465 LYS R 252 REMARK 465 PRO R 253 REMARK 465 VAL R 254 REMARK 465 VAL R 255 REMARK 465 PRO R 256 REMARK 465 GLN R 257 REMARK 465 ALA R 258 REMARK 465 THR R 259 REMARK 465 ILE R 260 REMARK 465 ILE R 261 REMARK 465 SER R 262 REMARK 465 HIS R 263 REMARK 465 VAL R 264 REMARK 465 ALA R 265 REMARK 465 SER R 266 REMARK 465 ASP R 267 REMARK 465 PHE R 268 REMARK 465 SER R 269 REMARK 465 LEU R 270 REMARK 465 ALA R 271 REMARK 465 GLU R 272 REMARK 465 PRO R 273 REMARK 465 LEU R 274 REMARK 465 ASP R 275 REMARK 465 HIS R 276 REMARK 465 ALA R 277 REMARK 465 LEU R 278 REMARK 465 MET R 279 REMARK 465 THR R 280 REMARK 465 PRO R 281 REMARK 465 SER R 282 REMARK 465 THR R 283 REMARK 465 PRO R 284 REMARK 465 SER R 285 REMARK 465 LEU R 286 REMARK 465 THR R 287 REMARK 465 GLN R 288 REMARK 465 GLU R 289 REMARK 465 SER R 290 REMARK 465 ASN R 291 REMARK 465 LEU R 292 REMARK 465 PRO R 293 REMARK 465 SER R 294 REMARK 465 PRO R 295 REMARK 465 GLN R 296 REMARK 465 PRO R 297 REMARK 465 THR R 298 REMARK 465 ILE R 299 REMARK 465 PRO R 300 REMARK 465 LEU R 301 REMARK 465 ALA R 302 REMARK 465 SER R 303 REMARK 465 SER R 304 REMARK 465 PRO R 305 REMARK 465 ALA R 306 REMARK 465 THR R 307 REMARK 465 ASP R 308 REMARK 465 LEU R 309 REMARK 465 PRO R 310 REMARK 465 VAL R 311 REMARK 465 GLN R 312 REMARK 465 SER R 313 REMARK 465 VAL R 314 REMARK 465 VAL R 315 REMARK 465 VAL R 316 REMARK 465 SER R 317 REMARK 465 SER R 318 REMARK 465 LEU R 319 REMARK 465 PRO R 320 REMARK 465 GLN R 321 REMARK 465 THR R 322 REMARK 465 ASP R 323 REMARK 465 LEU R 324 REMARK 465 SER R 325 REMARK 465 HIS R 326 REMARK 465 THR R 327 REMARK 465 LEU R 328 REMARK 465 SER R 329 REMARK 465 PRO R 330 REMARK 465 VAL R 331 REMARK 465 GLN R 332 REMARK 465 SER R 333 REMARK 465 SER R 334 REMARK 465 ILE R 335 REMARK 465 PRO R 336 REMARK 465 SER R 337 REMARK 465 PRO R 338 REMARK 465 THR R 339 REMARK 465 THR R 340 REMARK 465 PRO R 341 REMARK 465 ALA R 342 REMARK 465 PRO R 343 REMARK 465 SER R 344 REMARK 465 VAL R 345 REMARK 465 PRO R 346 REMARK 465 THR R 347 REMARK 465 GLU R 348 REMARK 465 LEU R 349 REMARK 465 VAL R 350 REMARK 465 THR R 351 REMARK 465 ILE R 352 REMARK 465 SER R 353 REMARK 465 THR R 354 REMARK 465 PRO R 355 REMARK 465 PRO R 356 REMARK 465 GLY R 357 REMARK 465 GLU R 358 REMARK 465 THR R 359 REMARK 465 VAL R 360 REMARK 465 VAL R 361 REMARK 465 ASN R 362 REMARK 465 THR R 363 REMARK 465 SER R 364 REMARK 465 THR R 365 REMARK 465 VAL R 366 REMARK 465 SER R 367 REMARK 465 ASP R 368 REMARK 465 LEU R 369 REMARK 465 GLU R 370 REMARK 465 ALA R 371 REMARK 465 GLN R 372 REMARK 465 VAL R 373 REMARK 465 SER R 374 REMARK 465 GLN R 375 REMARK 465 MET R 376 REMARK 465 GLU R 377 REMARK 465 LYS R 378 REMARK 465 ALA R 379 REMARK 465 LEU R 380 REMARK 465 SER R 381 REMARK 465 LEU R 382 REMARK 465 GLY R 383 REMARK 465 SER R 384 REMARK 465 LEU R 385 REMARK 465 GLU R 386 REMARK 465 PRO R 387 REMARK 465 ASN R 388 REMARK 465 LEU R 389 REMARK 465 ALA R 390 REMARK 465 GLY R 391 REMARK 465 GLU R 392 REMARK 465 MET R 393 REMARK 465 VAL R 394 REMARK 465 ASN R 395 REMARK 465 ARG R 396 REMARK 465 VAL R 397 REMARK 465 SER R 398 REMARK 465 LYS R 399 REMARK 465 LEU R 400 REMARK 465 LEU R 401 REMARK 465 HIS R 402 REMARK 465 SER R 403 REMARK 465 PRO R 404 REMARK 465 PRO R 405 REMARK 465 ALA R 406 REMARK 465 LEU R 407 REMARK 465 LEU R 408 REMARK 465 ALA R 409 REMARK 465 PRO R 410 REMARK 465 LEU R 411 REMARK 465 ALA R 412 REMARK 465 GLN R 413 REMARK 465 ARG R 414 REMARK 465 LEU R 415 REMARK 465 LEU R 416 REMARK 465 LYS R 417 REMARK 465 VAL R 418 REMARK 465 VAL R 419 REMARK 465 ASP R 420 REMARK 465 ALA R 421 REMARK 465 ILE R 422 REMARK 465 GLY R 423 REMARK 465 LEU R 424 REMARK 465 GLN R 425 REMARK 465 LEU R 426 REMARK 465 ASN R 427 REMARK 465 PHE R 428 REMARK 465 SER R 429 REMARK 465 SER R 430 REMARK 465 THR R 431 REMARK 465 THR R 432 REMARK 465 ILE R 433 REMARK 465 SER R 434 REMARK 465 LEU R 435 REMARK 465 THR R 436 REMARK 465 SER R 437 REMARK 465 PRO R 438 REMARK 465 SER R 439 REMARK 465 LEU R 440 REMARK 465 ALA R 441 REMARK 465 LEU R 442 REMARK 465 ALA R 443 REMARK 465 VAL R 444 REMARK 465 ILE R 445 REMARK 465 ARG R 446 REMARK 465 VAL R 447 REMARK 465 ASN R 448 REMARK 465 ALA R 449 REMARK 465 SER R 450 REMARK 465 ASN R 451 REMARK 465 PHE R 452 REMARK 465 ASN R 453 REMARK 465 THR R 454 REMARK 465 THR R 455 REMARK 465 THR R 456 REMARK 465 PHE R 457 REMARK 465 ALA R 458 REMARK 465 ALA R 459 REMARK 465 GLN R 460 REMARK 465 ASP R 461 REMARK 465 PRO R 462 REMARK 465 THR R 463 REMARK 465 ASN R 464 REMARK 465 LEU R 465 REMARK 465 GLN R 466 REMARK 465 VAL R 467 REMARK 465 SER R 468 REMARK 465 LEU R 469 REMARK 465 GLU R 470 REMARK 465 THR R 471 REMARK 465 PRO R 472 REMARK 465 PRO R 473 REMARK 465 PRO R 474 REMARK 465 GLU R 475 REMARK 465 ASN R 476 REMARK 465 SER R 477 REMARK 465 ILE R 478 REMARK 465 GLY R 479 REMARK 465 ALA R 480 REMARK 465 ILE R 481 REMARK 465 THR R 482 REMARK 465 LEU R 483 REMARK 465 PRO R 484 REMARK 465 SER R 485 REMARK 465 SER R 486 REMARK 465 LEU R 487 REMARK 465 MET R 488 REMARK 465 ASN R 489 REMARK 465 ASN R 490 REMARK 465 LEU R 491 REMARK 465 PRO R 492 REMARK 465 ALA R 493 REMARK 465 ASN R 494 REMARK 465 ASP R 495 REMARK 465 VAL R 496 REMARK 465 GLU R 497 REMARK 465 LEU R 498 REMARK 465 ALA R 499 REMARK 465 SER R 500 REMARK 465 ARG R 501 REMARK 465 ILE R 502 REMARK 465 GLN R 503 REMARK 465 PHE R 504 REMARK 465 ASN R 505 REMARK 465 PHE R 506 REMARK 465 PHE R 507 REMARK 465 GLU R 508 REMARK 465 THR R 509 REMARK 465 PRO R 510 REMARK 465 ALA R 511 REMARK 465 LEU R 512 REMARK 465 PHE R 513 REMARK 465 GLN R 514 REMARK 465 ASP R 515 REMARK 465 PRO R 516 REMARK 465 SER R 517 REMARK 465 LEU R 518 REMARK 465 GLU R 519 REMARK 465 ASN R 520 REMARK 465 LEU R 521 REMARK 465 THR R 522 REMARK 465 LEU R 523 REMARK 465 ILE R 524 REMARK 465 SER R 525 REMARK 465 TYR R 526 REMARK 465 VAL R 527 REMARK 465 ILE R 528 REMARK 465 SER R 529 REMARK 465 SER R 530 REMARK 465 SER R 531 REMARK 465 VAL R 532 REMARK 465 THR R 533 REMARK 465 ASN R 534 REMARK 465 MET R 535 REMARK 465 THR R 536 REMARK 465 ILE R 537 REMARK 465 LYS R 538 REMARK 465 ASN R 539 REMARK 465 LEU R 540 REMARK 465 THR R 541 REMARK 465 ARG R 542 REMARK 465 ASN R 543 REMARK 465 VAL R 544 REMARK 465 THR R 545 REMARK 465 VAL R 546 REMARK 465 ALA R 547 REMARK 465 LEU R 548 REMARK 465 LYS R 549 REMARK 465 HIS R 550 REMARK 465 ILE R 551 REMARK 465 ASN R 552 REMARK 465 PRO R 553 REMARK 465 SER R 554 REMARK 465 PRO R 555 REMARK 465 ASP R 556 REMARK 465 ASP R 557 REMARK 465 LEU R 558 REMARK 465 THR R 559 REMARK 465 VAL R 560 REMARK 465 LYS R 561 REMARK 465 CYS R 562 REMARK 465 VAL R 563 REMARK 465 PHE R 564 REMARK 465 TRP R 565 REMARK 465 ASP R 566 REMARK 465 LEU R 567 REMARK 465 GLY R 568 REMARK 465 ARG R 569 REMARK 465 ASN R 570 REMARK 465 GLY R 571 REMARK 465 GLY R 572 REMARK 465 LYS R 573 REMARK 465 GLY R 574 REMARK 465 GLY R 575 REMARK 465 TRP R 576 REMARK 465 SER R 577 REMARK 465 SER R 578 REMARK 465 ASP R 579 REMARK 465 GLY R 580 REMARK 465 CYS R 581 REMARK 465 SER R 582 REMARK 465 VAL R 583 REMARK 465 LYS R 584 REMARK 465 ASP R 585 REMARK 465 LYS R 586 REMARK 465 ARG R 587 REMARK 465 MET R 588 REMARK 465 ASN R 589 REMARK 465 GLU R 590 REMARK 465 THR R 591 REMARK 465 ILE R 592 REMARK 465 CYS R 593 REMARK 465 THR R 594 REMARK 465 CYS R 595 REMARK 465 SER R 596 REMARK 465 ALA R 597 REMARK 465 LEU R 598 REMARK 465 ALA R 599 REMARK 465 SER R 600 REMARK 465 PHE R 601 REMARK 465 GLY R 602 REMARK 465 ILE R 603 REMARK 465 LEU R 604 REMARK 465 LEU R 605 REMARK 465 ASP R 606 REMARK 465 LEU R 607 REMARK 465 SER R 608 REMARK 465 ARG R 609 REMARK 465 THR R 610 REMARK 465 SER R 611 REMARK 465 LEU R 612 REMARK 465 PRO R 613 REMARK 465 PRO R 614 REMARK 465 SER R 615 REMARK 465 GLN R 616 REMARK 465 MET R 617 REMARK 465 MET R 618 REMARK 465 GLY R 756 REMARK 465 SER R 757 REMARK 465 TYR R 758 REMARK 465 GLY R 759 REMARK 465 LYS R 760 REMARK 465 PHE R 761 REMARK 465 PRO R 762 REMARK 465 ASN R 763 REMARK 465 GLY R 764 REMARK 465 THR R 765 REMARK 465 PRO R 766 REMARK 465 ASP R 767 REMARK 465 ASP R 768 REMARK 465 LYS R 811 REMARK 465 GLN R 812 REMARK 465 LEU R 813 REMARK 465 GLY R 814 REMARK 465 ALA R 815 REMARK 465 GLN R 816 REMARK 465 ARG R 817 REMARK 465 LYS R 818 REMARK 465 THR R 819 REMARK 465 SER R 820 REMARK 465 ILE R 821 REMARK 465 GLN R 822 REMARK 465 ARG R 884 REMARK 465 TYR R 885 REMARK 465 LEU R 886 REMARK 465 CYS R 887 REMARK 465 CYS R 888 REMARK 465 GLY R 889 REMARK 465 LYS R 890 REMARK 465 LEU R 891 REMARK 465 PHE R 892 REMARK 465 TRP R 893 REMARK 465 PHE R 894 REMARK 465 PRO R 895 REMARK 465 GLU R 896 REMARK 465 LYS R 897 REMARK 465 GLY R 898 REMARK 465 ALA R 899 REMARK 465 ILE R 900 REMARK 465 LEU R 901 REMARK 465 THR R 902 REMARK 465 ASP R 903 REMARK 465 THR R 904 REMARK 465 SER R 905 REMARK 465 VAL R 906 REMARK 465 LYS R 907 REMARK 465 ARG R 908 REMARK 465 ASN R 909 REMARK 465 ASP R 910 REMARK 465 LEU R 911 REMARK 465 SER R 912 REMARK 465 ILE R 913 REMARK 465 ILE R 914 REMARK 465 SER R 915 REMARK 465 GLY R 916 REMARK 465 ASP S 1 REMARK 465 GLY S 122 REMARK 465 GLY S 123 REMARK 465 GLY S 124 REMARK 465 GLY S 125 REMARK 465 SER S 126 REMARK 465 GLY S 127 REMARK 465 GLY S 128 REMARK 465 GLY S 129 REMARK 465 GLY S 130 REMARK 465 SER S 131 REMARK 465 GLY S 132 REMARK 465 GLY S 133 REMARK 465 GLY S 134 REMARK 465 LYS S 248 REMARK 465 GLY S 249 REMARK 465 SER S 250 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 LYS A 38 CG CD CE NZ REMARK 470 ASP A 59 CG OD1 OD2 REMARK 470 LYS A 68 CG CD CE NZ REMARK 470 GLN A 69 CG CD OE1 NE2 REMARK 470 ARG A 71 CG CD NE CZ NH1 NH2 REMARK 470 ILE A 72 CG1 CG2 CD1 REMARK 470 TYR A 73 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 GLU A 219 CG CD OE1 OE2 REMARK 470 LYS A 226 CG CD CE NZ REMARK 470 ASP A 250 CG OD1 OD2 REMARK 470 ASN A 264 CG OD1 ND2 REMARK 470 ARG A 280 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 305 CG CD CE NZ REMARK 470 LYS A 307 CG CD CE NZ REMARK 470 ARG A 317 CG CD NE CZ NH1 NH2 REMARK 470 GLU A 322 CG CD OE1 OE2 REMARK 470 ASP A 323 CG OD1 OD2 REMARK 470 GLU A 330 CG CD OE1 OE2 REMARK 470 ASP A 354 CG OD1 OD2 REMARK 470 ARG A 356 CG CD NE CZ NH1 NH2 REMARK 470 ASP B 5 CG OD1 OD2 REMARK 470 GLN B 6 CG CD OE1 NE2 REMARK 470 ARG B 8 CG CD NE CZ NH1 NH2 REMARK 470 LYS B 23 CG CD CE NZ REMARK 470 ASP B 38 CG OD1 OD2 REMARK 470 ARG B 42 CG CD NE CZ NH1 NH2 REMARK 470 ASP B 153 CG OD1 OD2 REMARK 470 ARG B 197 CG CD NE CZ NH1 NH2 REMARK 470 ARG B 214 CG CD NE CZ NH1 NH2 REMARK 470 LYS N 43 CG CD CE NZ REMARK 470 LYS N 76 CG CD CE NZ REMARK 470 ARG N 105 CG CD NE CZ NH1 NH2 REMARK 470 ASP N 109 CG OD1 OD2 REMARK 470 PHE R 622 CG CD1 CD2 CE1 CE2 CZ REMARK 470 GLU R 646 CG CD OE1 OE2 REMARK 470 LYS R 647 CG CD CE NZ REMARK 470 ARG R 650 CG CD NE CZ NH1 NH2 REMARK 470 TRP R 676 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP R 676 CZ3 CH2 REMARK 470 TYR R 680 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ASN R 681 CG OD1 ND2 REMARK 470 ARG R 683 CG CD NE CZ NH1 NH2 REMARK 470 GLU R 707 CG CD OE1 OE2 REMARK 470 LYS R 717 CG CD CE NZ REMARK 470 ARG R 724 CG CD NE CZ NH1 NH2 REMARK 470 LYS R 725 CG CD CE NZ REMARK 470 LYS R 808 CG CD CE NZ REMARK 470 LYS R 809 CG CD CE NZ REMARK 470 LYS R 810 CG CD CE NZ REMARK 470 ASP R 823 CG OD1 OD2 REMARK 470 LEU R 824 CG CD1 CD2 REMARK 470 ARG R 825 CG CD NE CZ NH1 NH2 REMARK 470 TRP R 845 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP R 845 CZ3 CH2 REMARK 470 VAL R 850 CG1 CG2 REMARK 470 TYR R 854 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 GLU R 876 CG CD OE1 OE2 REMARK 470 LYS R 880 CG CD CE NZ REMARK 470 ARG R 883 CG CD NE CZ NH1 NH2 REMARK 470 SER S 121 OG REMARK 470 SER S 136 OG REMARK 470 GLU S 153 CG CD OE1 OE2 REMARK 470 GLU S 234 CG CD OE1 OE2 REMARK 470 TYR S 235 CG CD1 CD2 CE1 CE2 CZ OH 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 PHE A 248 53.43 -92.35 REMARK 500 THR A 284 -0.14 74.86 REMARK 500 PRO A 313 44.75 -85.94 REMARK 500 THR A 350 47.09 -92.45 REMARK 500 PRO B 107 45.09 -82.00 REMARK 500 LEU B 152 -71.79 -81.29 REMARK 500 ASP B 153 89.81 -151.79 REMARK 500 ASP B 154 -9.15 65.96 REMARK 500 ASN B 155 -2.35 -147.02 REMARK 500 ASP B 163 30.09 -94.13 REMARK 500 PRO B 194 42.50 -80.18 REMARK 500 HIS G 44 48.46 -92.27 REMARK 500 ASP G 48 86.55 -158.56 REMARK 500 LYS N 43 20.88 -144.46 REMARK 500 SER N 57 36.81 -143.02 REMARK 500 ASN N 74 46.91 -90.92 REMARK 500 ASP N 106 79.47 -102.85 REMARK 500 ASP N 109 45.15 36.15 REMARK 500 TYR N 117 57.36 -95.45 REMARK 500 VAL R 716 -62.97 -90.81 REMARK 500 SER R 749 98.52 -162.62 REMARK 500 ASN R 775 -7.52 70.76 REMARK 500 CYS R 872 -53.86 -122.49 REMARK 500 ALA S 92 165.37 175.49 REMARK 500 LEU S 188 -60.54 -108.38 REMARK 500 MET S 192 -54.50 74.28 REMARK 500 SER S 193 4.25 -152.31 REMARK 500 SER S 208 43.61 -140.32 REMARK 500 LEU S 245 73.14 -100.36 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-39365 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF ADGRG2-GS COMPLEX WITH NTF NANOBODY DBREF 8YKD A 18 213 PDB 8YKD 8YKD 18 213 DBREF 8YKD A 214 394 UNP P63091 GNAS_CANLF 204 394 DBREF 8YKD B 2 340 UNP P62871 GBB1_BOVIN 2 340 DBREF1 8YKD G -9 71 UNP A0A7J7XNR4_RHIFE DBREF2 8YKD G A0A7J7XNR4 19 99 DBREF 8YKD N 1 128 PDB 8YKD 8YKD 1 128 DBREF 8YKD R 38 891 UNP Q8CJ12 AGRG2_MOUSE 38 891 DBREF 8YKD S 1 250 PDB 8YKD 8YKD 1 250 SEQADV 8YKD ALA A 236 UNP P63091 GLY 226 CONFLICT SEQADV 8YKD ASP A 259 UNP P63091 ALA 249 CONFLICT SEQADV 8YKD ASP A 262 UNP P63091 SER 252 CONFLICT SEQADV 8YKD A UNP P63091 ASN 254 DELETION SEQADV 8YKD A UNP P63091 MET 255 DELETION SEQADV 8YKD A UNP P63091 VAL 256 DELETION SEQADV 8YKD A UNP P63091 ILE 257 DELETION SEQADV 8YKD A UNP P63091 ARG 258 DELETION SEQADV 8YKD A UNP P63091 GLU 259 DELETION SEQADV 8YKD A UNP P63091 ASP 260 DELETION SEQADV 8YKD A UNP P63091 ASN 261 DELETION SEQADV 8YKD A UNP P63091 GLN 262 DELETION SEQADV 8YKD A UNP P63091 THR 263 DELETION SEQADV 8YKD ASP A 272 UNP P63091 LEU 272 CONFLICT SEQADV 8YKD SER A 366 UNP P63091 ALA 366 CONFLICT SEQADV 8YKD ALA A 372 UNP P63091 ILE 372 CONFLICT SEQADV 8YKD ILE A 375 UNP P63091 VAL 375 CONFLICT SEQADV 8YKD MET B -17 UNP P62871 INITIATING METHIONINE SEQADV 8YKD HIS B -16 UNP P62871 EXPRESSION TAG SEQADV 8YKD HIS B -15 UNP P62871 EXPRESSION TAG SEQADV 8YKD HIS B -14 UNP P62871 EXPRESSION TAG SEQADV 8YKD HIS B -13 UNP P62871 EXPRESSION TAG SEQADV 8YKD HIS B -12 UNP P62871 EXPRESSION TAG SEQADV 8YKD HIS B -11 UNP P62871 EXPRESSION TAG SEQADV 8YKD LEU B -10 UNP P62871 EXPRESSION TAG SEQADV 8YKD GLU B -9 UNP P62871 EXPRESSION TAG SEQADV 8YKD VAL B -8 UNP P62871 EXPRESSION TAG SEQADV 8YKD LEU B -7 UNP P62871 EXPRESSION TAG SEQADV 8YKD PHE B -6 UNP P62871 EXPRESSION TAG SEQADV 8YKD GLN B -5 UNP P62871 EXPRESSION TAG SEQADV 8YKD GLY B -4 UNP P62871 EXPRESSION TAG SEQADV 8YKD PRO B -3 UNP P62871 EXPRESSION TAG SEQADV 8YKD GLY B -2 UNP P62871 EXPRESSION TAG SEQADV 8YKD SER B -1 UNP P62871 EXPRESSION TAG SEQADV 8YKD SER B 0 UNP P62871 EXPRESSION TAG SEQADV 8YKD GLY B 1 UNP P62871 EXPRESSION TAG SEQADV 8YKD MET G -36 UNP A0A7J7XNR INITIATING METHIONINE SEQADV 8YKD TRP G -35 UNP A0A7J7XNR EXPRESSION TAG SEQADV 8YKD ARG G -34 UNP A0A7J7XNR EXPRESSION TAG SEQADV 8YKD GLU G -33 UNP A0A7J7XNR EXPRESSION TAG SEQADV 8YKD LEU G -32 UNP A0A7J7XNR EXPRESSION TAG SEQADV 8YKD PRO G -31 UNP A0A7J7XNR EXPRESSION TAG SEQADV 8YKD LEU G -30 UNP A0A7J7XNR EXPRESSION TAG SEQADV 8YKD GLY G -29 UNP A0A7J7XNR EXPRESSION TAG SEQADV 8YKD LEU G -28 UNP A0A7J7XNR EXPRESSION TAG SEQADV 8YKD GLY G -27 UNP A0A7J7XNR EXPRESSION TAG SEQADV 8YKD GLU G -26 UNP A0A7J7XNR EXPRESSION TAG SEQADV 8YKD LEU G -25 UNP A0A7J7XNR EXPRESSION TAG SEQADV 8YKD HIS G -24 UNP A0A7J7XNR EXPRESSION TAG SEQADV 8YKD LYS G -23 UNP A0A7J7XNR EXPRESSION TAG SEQADV 8YKD ASP G -22 UNP A0A7J7XNR EXPRESSION TAG SEQADV 8YKD HIS G -21 UNP A0A7J7XNR EXPRESSION TAG SEQADV 8YKD GLN G -20 UNP A0A7J7XNR EXPRESSION TAG SEQADV 8YKD ALA G -19 UNP A0A7J7XNR EXPRESSION TAG SEQADV 8YKD SER G -18 UNP A0A7J7XNR EXPRESSION TAG SEQADV 8YKD ARG G -17 UNP A0A7J7XNR EXPRESSION TAG SEQADV 8YKD LYS G -16 UNP A0A7J7XNR EXPRESSION TAG SEQADV 8YKD LEU G -15 UNP A0A7J7XNR EXPRESSION TAG SEQADV 8YKD GLU G -14 UNP A0A7J7XNR EXPRESSION TAG SEQADV 8YKD PRO G -13 UNP A0A7J7XNR EXPRESSION TAG SEQADV 8YKD GLU G -12 UNP A0A7J7XNR EXPRESSION TAG SEQADV 8YKD LEU G -11 UNP A0A7J7XNR EXPRESSION TAG SEQADV 8YKD TRP G -10 UNP A0A7J7XNR EXPRESSION TAG SEQADV 8YKD MET R 14 UNP Q8CJ12 INITIATING METHIONINE SEQADV 8YKD LYS R 15 UNP Q8CJ12 EXPRESSION TAG SEQADV 8YKD THR R 16 UNP Q8CJ12 EXPRESSION TAG SEQADV 8YKD ILE R 17 UNP Q8CJ12 EXPRESSION TAG SEQADV 8YKD ILE R 18 UNP Q8CJ12 EXPRESSION TAG SEQADV 8YKD ALA R 19 UNP Q8CJ12 EXPRESSION TAG SEQADV 8YKD LEU R 20 UNP Q8CJ12 EXPRESSION TAG SEQADV 8YKD SER R 21 UNP Q8CJ12 EXPRESSION TAG SEQADV 8YKD TYR R 22 UNP Q8CJ12 EXPRESSION TAG SEQADV 8YKD ILE R 23 UNP Q8CJ12 EXPRESSION TAG SEQADV 8YKD PHE R 24 UNP Q8CJ12 EXPRESSION TAG SEQADV 8YKD CYS R 25 UNP Q8CJ12 EXPRESSION TAG SEQADV 8YKD LEU R 26 UNP Q8CJ12 EXPRESSION TAG SEQADV 8YKD VAL R 27 UNP Q8CJ12 EXPRESSION TAG SEQADV 8YKD PHE R 28 UNP Q8CJ12 EXPRESSION TAG SEQADV 8YKD ALA R 29 UNP Q8CJ12 EXPRESSION TAG SEQADV 8YKD ASP R 30 UNP Q8CJ12 EXPRESSION TAG SEQADV 8YKD TYR R 31 UNP Q8CJ12 EXPRESSION TAG SEQADV 8YKD LYS R 32 UNP Q8CJ12 EXPRESSION TAG SEQADV 8YKD ASP R 33 UNP Q8CJ12 EXPRESSION TAG SEQADV 8YKD ASP R 34 UNP Q8CJ12 EXPRESSION TAG SEQADV 8YKD ASP R 35 UNP Q8CJ12 EXPRESSION TAG SEQADV 8YKD ASP R 36 UNP Q8CJ12 EXPRESSION TAG SEQADV 8YKD LYS R 37 UNP Q8CJ12 EXPRESSION TAG SEQADV 8YKD ALA R 597 UNP Q8CJ12 HIS 597 ENGINEERED MUTATION SEQADV 8YKD ALA R 599 UNP Q8CJ12 THR 599 ENGINEERED MUTATION SEQADV 8YKD PHE R 892 UNP Q8CJ12 EXPRESSION TAG SEQADV 8YKD TRP R 893 UNP Q8CJ12 EXPRESSION TAG SEQADV 8YKD PHE R 894 UNP Q8CJ12 EXPRESSION TAG SEQADV 8YKD PRO R 895 UNP Q8CJ12 EXPRESSION TAG SEQADV 8YKD GLU R 896 UNP Q8CJ12 EXPRESSION TAG SEQADV 8YKD LYS R 897 UNP Q8CJ12 EXPRESSION TAG SEQADV 8YKD GLY R 898 UNP Q8CJ12 EXPRESSION TAG SEQADV 8YKD ALA R 899 UNP Q8CJ12 EXPRESSION TAG SEQADV 8YKD ILE R 900 UNP Q8CJ12 EXPRESSION TAG SEQADV 8YKD LEU R 901 UNP Q8CJ12 EXPRESSION TAG SEQADV 8YKD THR R 902 UNP Q8CJ12 EXPRESSION TAG SEQADV 8YKD ASP R 903 UNP Q8CJ12 EXPRESSION TAG SEQADV 8YKD THR R 904 UNP Q8CJ12 EXPRESSION TAG SEQADV 8YKD SER R 905 UNP Q8CJ12 EXPRESSION TAG SEQADV 8YKD VAL R 906 UNP Q8CJ12 EXPRESSION TAG SEQADV 8YKD LYS R 907 UNP Q8CJ12 EXPRESSION TAG SEQADV 8YKD ARG R 908 UNP Q8CJ12 EXPRESSION TAG SEQADV 8YKD ASN R 909 UNP Q8CJ12 EXPRESSION TAG SEQADV 8YKD ASP R 910 UNP Q8CJ12 EXPRESSION TAG SEQADV 8YKD LEU R 911 UNP Q8CJ12 EXPRESSION TAG SEQADV 8YKD SER R 912 UNP Q8CJ12 EXPRESSION TAG SEQADV 8YKD ILE R 913 UNP Q8CJ12 EXPRESSION TAG SEQADV 8YKD ILE R 914 UNP Q8CJ12 EXPRESSION TAG SEQADV 8YKD SER R 915 UNP Q8CJ12 EXPRESSION TAG SEQADV 8YKD GLY R 916 UNP Q8CJ12 EXPRESSION TAG SEQRES 1 A 361 MET GLY CYS THR LEU SER ALA GLU ASP LYS ALA ALA VAL SEQRES 2 A 361 GLU ARG SER LYS MET ILE GLU LYS GLN LEU GLN LYS ASP SEQRES 3 A 361 LYS GLN VAL TYR ARG ALA THR HIS ARG LEU LEU LEU LEU SEQRES 4 A 361 GLY ALA ASP ASN SER GLY LYS SER THR ILE VAL LYS GLN SEQRES 5 A 361 MET ARG ILE TYR HIS VAL ASN GLY TYR SER GLU GLU GLU SEQRES 6 A 361 CYS LYS GLN TYR LYS ALA VAL VAL TYR SER ASN THR ILE SEQRES 7 A 361 GLN SER ILE ILE ALA ILE ILE ARG ALA MET GLY ARG LEU SEQRES 8 A 361 LYS ILE ASP PHE GLY ASP SER ALA ARG ALA ASP ASP ALA SEQRES 9 A 361 ARG GLN LEU PHE VAL LEU ALA GLY ALA ALA GLU GLU GLY SEQRES 10 A 361 PHE MET THR ALA GLU LEU ALA GLY VAL ILE LYS ARG LEU SEQRES 11 A 361 TRP LYS ASP SER GLY VAL GLN ALA CYS PHE ASN ARG SER SEQRES 12 A 361 ARG GLU TYR GLN LEU ASN ASP SER ALA ALA TYR TYR LEU SEQRES 13 A 361 ASN ASP LEU ASP ARG ILE ALA GLN PRO ASN TYR ILE PRO SEQRES 14 A 361 THR GLN GLN ASP VAL LEU ARG THR ARG VAL LYS THR SER SEQRES 15 A 361 GLY ILE PHE GLU THR LYS PHE GLN VAL ASP LYS VAL ASN SEQRES 16 A 361 PHE HIS MET PHE ASP VAL GLY ALA GLN ARG ASP GLU ARG SEQRES 17 A 361 ARG LYS TRP ILE GLN CYS PHE ASN ASP VAL THR ALA ILE SEQRES 18 A 361 ILE PHE VAL VAL ASP SER SER ASP TYR ASN ARG LEU GLN SEQRES 19 A 361 GLU ALA LEU ASN ASP PHE LYS SER ILE TRP ASN ASN ARG SEQRES 20 A 361 TRP LEU ARG THR ILE SER VAL ILE LEU PHE LEU ASN LYS SEQRES 21 A 361 GLN ASP LEU LEU ALA GLU LYS VAL LEU ALA GLY LYS SER SEQRES 22 A 361 LYS ILE GLU ASP TYR PHE PRO GLU PHE ALA ARG TYR THR SEQRES 23 A 361 THR PRO GLU ASP ALA THR PRO GLU PRO GLY GLU ASP PRO SEQRES 24 A 361 ARG VAL THR ARG ALA LYS TYR PHE ILE ARG ASP GLU PHE SEQRES 25 A 361 LEU ARG ILE SER THR ALA SER GLY ASP GLY ARG HIS TYR SEQRES 26 A 361 CYS TYR PRO HIS PHE THR CYS SER VAL ASP THR GLU ASN SEQRES 27 A 361 ALA ARG ARG ILE PHE ASN ASP CYS ARG ASP ILE ILE GLN SEQRES 28 A 361 ARG MET HIS LEU ARG GLN TYR GLU LEU LEU SEQRES 1 B 358 MET HIS HIS HIS HIS HIS HIS LEU GLU VAL LEU PHE GLN SEQRES 2 B 358 GLY PRO GLY SER SER GLY SER GLU LEU ASP GLN LEU ARG SEQRES 3 B 358 GLN GLU ALA GLU GLN LEU LYS ASN GLN ILE ARG ASP ALA SEQRES 4 B 358 ARG LYS ALA CYS ALA ASP ALA THR LEU SER GLN ILE THR SEQRES 5 B 358 ASN ASN ILE ASP PRO VAL GLY ARG ILE GLN MET ARG THR SEQRES 6 B 358 ARG ARG THR LEU ARG GLY HIS LEU ALA LYS ILE TYR ALA SEQRES 7 B 358 MET HIS TRP GLY THR ASP SER ARG LEU LEU VAL SER ALA SEQRES 8 B 358 SER GLN ASP GLY LYS LEU ILE ILE TRP ASP SER TYR THR SEQRES 9 B 358 THR ASN LYS VAL HIS ALA ILE PRO LEU ARG SER SER TRP SEQRES 10 B 358 VAL MET THR CYS ALA TYR ALA PRO SER GLY ASN TYR VAL SEQRES 11 B 358 ALA CYS GLY GLY LEU ASP ASN ILE CYS SER ILE TYR ASN SEQRES 12 B 358 LEU LYS THR ARG GLU GLY ASN VAL ARG VAL SER ARG GLU SEQRES 13 B 358 LEU ALA GLY HIS THR GLY TYR LEU SER CYS CYS ARG PHE SEQRES 14 B 358 LEU ASP ASP ASN GLN ILE VAL THR SER SER GLY ASP THR SEQRES 15 B 358 THR CYS ALA LEU TRP ASP ILE GLU THR GLY GLN GLN THR SEQRES 16 B 358 THR THR PHE THR GLY HIS THR GLY ASP VAL MET SER LEU SEQRES 17 B 358 SER LEU ALA PRO ASP THR ARG LEU PHE VAL SER GLY ALA SEQRES 18 B 358 CYS ASP ALA SER ALA LYS LEU TRP ASP VAL ARG GLU GLY SEQRES 19 B 358 MET CYS ARG GLN THR PHE THR GLY HIS GLU SER ASP ILE SEQRES 20 B 358 ASN ALA ILE CYS PHE PHE PRO ASN GLY ASN ALA PHE ALA SEQRES 21 B 358 THR GLY SER ASP ASP ALA THR CYS ARG LEU PHE ASP LEU SEQRES 22 B 358 ARG ALA ASP GLN GLU LEU MET THR TYR SER HIS ASP ASN SEQRES 23 B 358 ILE ILE CYS GLY ILE THR SER VAL SER PHE SER LYS SER SEQRES 24 B 358 GLY ARG LEU LEU LEU ALA GLY TYR ASP ASP PHE ASN CYS SEQRES 25 B 358 ASN VAL TRP ASP ALA LEU LYS ALA ASP ARG ALA GLY VAL SEQRES 26 B 358 LEU ALA GLY HIS ASP ASN ARG VAL SER CYS LEU GLY VAL SEQRES 27 B 358 THR ASP ASP GLY MET ALA VAL ALA THR GLY SER TRP ASP SEQRES 28 B 358 SER PHE LEU LYS ILE TRP ASN SEQRES 1 G 108 MET TRP ARG GLU LEU PRO LEU GLY LEU GLY GLU LEU HIS SEQRES 2 G 108 LYS ASP HIS GLN ALA SER ARG LYS LEU GLU PRO GLU LEU SEQRES 3 G 108 TRP SER VAL SER GLU ASN PRO PRO SER THR SER MET ALA SEQRES 4 G 108 SER ASN ASN THR ALA SER ILE ALA GLN ALA ARG LYS LEU SEQRES 5 G 108 VAL GLU GLN LEU LYS MET GLU ALA ASN ILE ASP ARG ILE SEQRES 6 G 108 LYS VAL SER LYS ALA ALA ALA ASP LEU MET ALA TYR CYS SEQRES 7 G 108 GLU ALA HIS ALA LYS GLU ASP PRO LEU LEU THR PRO VAL SEQRES 8 G 108 PRO ALA SER GLU ASN PRO PHE ARG GLU LYS LYS PHE PHE SEQRES 9 G 108 CYS ALA ILE LEU SEQRES 1 N 128 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 N 128 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 N 128 PHE THR PHE SER ASN TYR LYS MET ASN TRP VAL ARG GLN SEQRES 4 N 128 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER ASP ILE SER SEQRES 5 N 128 GLN SER GLY ALA SER ILE SER TYR THR GLY SER VAL LYS SEQRES 6 N 128 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR SEQRES 7 N 128 LEU TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR SEQRES 8 N 128 ALA VAL TYR TYR CYS ALA ARG CYS PRO ALA PRO PHE THR SEQRES 9 N 128 ARG ASP CYS PHE ASP VAL THR SER THR THR TYR ALA TYR SEQRES 10 N 128 ARG GLY GLN GLY THR GLN VAL THR VAL SER SER SEQRES 1 R 903 MET LYS THR ILE ILE ALA LEU SER TYR ILE PHE CYS LEU SEQRES 2 R 903 VAL PHE ALA ASP TYR LYS ASP ASP ASP ASP LYS LEU LYS SEQRES 3 R 903 GLU ASN GLY ASN SER SER LEU LEU SER PRO SER ALA GLU SEQRES 4 R 903 SER SER LEU VAL SER LEU ILE PRO TYR SER ASN GLY THR SEQRES 5 R 903 PRO ASP ALA ALA SER GLU VAL LEU SER THR LEU ASN LYS SEQRES 6 R 903 THR GLU LYS SER LYS ILE THR ILE VAL LYS THR PHE ASN SEQRES 7 R 903 ALA SER GLY VAL LYS SER GLN ARG ASN ILE CYS ASN LEU SEQRES 8 R 903 SER SER LEU CYS ASN ASP SER VAL PHE PHE ARG GLY GLU SEQRES 9 R 903 ILE VAL PHE GLN HIS ASP GLU ASP HIS ASN VAL THR GLN SEQRES 10 R 903 ASN GLN ASP THR ALA ASN GLY THR PHE ALA GLY VAL LEU SEQRES 11 R 903 SER LEU SER GLU LEU LYS ARG SER GLU LEU ASN LYS THR SEQRES 12 R 903 LEU GLN THR LEU SER GLU THR TYR PHE ILE VAL CYS ALA SEQRES 13 R 903 THR ALA GLU ALA GLN SER THR VAL ASN CYS THR PHE THR SEQRES 14 R 903 VAL LYS LEU ASN GLU THR MET ASN VAL CYS ALA MET MET SEQRES 15 R 903 VAL THR PHE GLN THR VAL GLN ILE ARG PRO MET GLU GLN SEQRES 16 R 903 CYS CYS CYS SER PRO ARG THR PRO CYS PRO SER SER PRO SEQRES 17 R 903 GLU GLU LEU GLU LYS LEU GLN CYS GLU LEU GLN ASP PRO SEQRES 18 R 903 ILE VAL CYS LEU ALA ASP GLN PRO HIS GLY PRO PRO LEU SEQRES 19 R 903 SER SER SER SER LYS PRO VAL VAL PRO GLN ALA THR ILE SEQRES 20 R 903 ILE SER HIS VAL ALA SER ASP PHE SER LEU ALA GLU PRO SEQRES 21 R 903 LEU ASP HIS ALA LEU MET THR PRO SER THR PRO SER LEU SEQRES 22 R 903 THR GLN GLU SER ASN LEU PRO SER PRO GLN PRO THR ILE SEQRES 23 R 903 PRO LEU ALA SER SER PRO ALA THR ASP LEU PRO VAL GLN SEQRES 24 R 903 SER VAL VAL VAL SER SER LEU PRO GLN THR ASP LEU SER SEQRES 25 R 903 HIS THR LEU SER PRO VAL GLN SER SER ILE PRO SER PRO SEQRES 26 R 903 THR THR PRO ALA PRO SER VAL PRO THR GLU LEU VAL THR SEQRES 27 R 903 ILE SER THR PRO PRO GLY GLU THR VAL VAL ASN THR SER SEQRES 28 R 903 THR VAL SER ASP LEU GLU ALA GLN VAL SER GLN MET GLU SEQRES 29 R 903 LYS ALA LEU SER LEU GLY SER LEU GLU PRO ASN LEU ALA SEQRES 30 R 903 GLY GLU MET VAL ASN ARG VAL SER LYS LEU LEU HIS SER SEQRES 31 R 903 PRO PRO ALA LEU LEU ALA PRO LEU ALA GLN ARG LEU LEU SEQRES 32 R 903 LYS VAL VAL ASP ALA ILE GLY LEU GLN LEU ASN PHE SER SEQRES 33 R 903 SER THR THR ILE SER LEU THR SER PRO SER LEU ALA LEU SEQRES 34 R 903 ALA VAL ILE ARG VAL ASN ALA SER ASN PHE ASN THR THR SEQRES 35 R 903 THR PHE ALA ALA GLN ASP PRO THR ASN LEU GLN VAL SER SEQRES 36 R 903 LEU GLU THR PRO PRO PRO GLU ASN SER ILE GLY ALA ILE SEQRES 37 R 903 THR LEU PRO SER SER LEU MET ASN ASN LEU PRO ALA ASN SEQRES 38 R 903 ASP VAL GLU LEU ALA SER ARG ILE GLN PHE ASN PHE PHE SEQRES 39 R 903 GLU THR PRO ALA LEU PHE GLN ASP PRO SER LEU GLU ASN SEQRES 40 R 903 LEU THR LEU ILE SER TYR VAL ILE SER SER SER VAL THR SEQRES 41 R 903 ASN MET THR ILE LYS ASN LEU THR ARG ASN VAL THR VAL SEQRES 42 R 903 ALA LEU LYS HIS ILE ASN PRO SER PRO ASP ASP LEU THR SEQRES 43 R 903 VAL LYS CYS VAL PHE TRP ASP LEU GLY ARG ASN GLY GLY SEQRES 44 R 903 LYS GLY GLY TRP SER SER ASP GLY CYS SER VAL LYS ASP SEQRES 45 R 903 LYS ARG MET ASN GLU THR ILE CYS THR CYS SER ALA LEU SEQRES 46 R 903 ALA SER PHE GLY ILE LEU LEU ASP LEU SER ARG THR SER SEQRES 47 R 903 LEU PRO PRO SER GLN MET MET ALA LEU THR PHE ILE THR SEQRES 48 R 903 TYR ILE GLY CYS GLY LEU SER SER ILE PHE LEU SER VAL SEQRES 49 R 903 THR LEU VAL THR TYR ILE ALA PHE GLU LYS ILE ARG ARG SEQRES 50 R 903 ASP TYR PRO SER LYS ILE LEU ILE GLN LEU CYS ALA ALA SEQRES 51 R 903 LEU LEU LEU LEU ASN LEU ILE PHE LEU LEU ASP SER TRP SEQRES 52 R 903 ILE ALA LEU TYR ASN THR ARG GLY PHE CYS ILE ALA VAL SEQRES 53 R 903 ALA VAL PHE LEU HIS TYR PHE LEU LEU VAL SER PHE THR SEQRES 54 R 903 TRP MET GLY LEU GLU ALA PHE HIS MET TYR LEU ALA LEU SEQRES 55 R 903 VAL LYS VAL PHE ASN THR TYR ILE ARG LYS TYR ILE LEU SEQRES 56 R 903 LYS PHE CYS ILE VAL GLY TRP GLY ILE PRO ALA VAL VAL SEQRES 57 R 903 VAL SER ILE VAL LEU THR ILE SER PRO ASP ASN TYR GLY SEQRES 58 R 903 ILE GLY SER TYR GLY LYS PHE PRO ASN GLY THR PRO ASP SEQRES 59 R 903 ASP PHE CYS TRP ILE ASN SER ASN VAL VAL PHE TYR ILE SEQRES 60 R 903 THR VAL VAL GLY TYR PHE CYS VAL ILE PHE LEU LEU ASN SEQRES 61 R 903 VAL SER MET PHE ILE VAL VAL LEU VAL GLN LEU CYS ARG SEQRES 62 R 903 ILE LYS LYS LYS LYS GLN LEU GLY ALA GLN ARG LYS THR SEQRES 63 R 903 SER ILE GLN ASP LEU ARG SER ILE ALA GLY LEU THR PHE SEQRES 64 R 903 LEU LEU GLY ILE THR TRP GLY PHE ALA PHE PHE ALA TRP SEQRES 65 R 903 GLY PRO VAL ASN VAL THR PHE MET TYR LEU PHE ALA ILE SEQRES 66 R 903 PHE ASN THR LEU GLN GLY PHE PHE ILE PHE ILE PHE TYR SEQRES 67 R 903 CYS ALA ALA LYS GLU ASN VAL ARG LYS GLN TRP ARG ARG SEQRES 68 R 903 TYR LEU CYS CYS GLY LYS LEU PHE TRP PHE PRO GLU LYS SEQRES 69 R 903 GLY ALA ILE LEU THR ASP THR SER VAL LYS ARG ASN ASP SEQRES 70 R 903 LEU SER ILE ILE SER GLY SEQRES 1 S 250 ASP VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 S 250 PRO GLY GLY SER ARG LYS LEU SER CYS SER ALA SER GLY SEQRES 3 S 250 PHE ALA PHE SER SER PHE GLY MET HIS TRP VAL ARG GLN SEQRES 4 S 250 ALA PRO GLU LYS GLY LEU GLU TRP VAL ALA TYR ILE SER SEQRES 5 S 250 SER GLY SER GLY THR ILE TYR TYR ALA ASP THR VAL LYS SEQRES 6 S 250 GLY ARG PHE THR ILE SER ARG ASP ASP PRO LYS ASN THR SEQRES 7 S 250 LEU PHE LEU GLN MET THR SER LEU ARG SER GLU ASP THR SEQRES 8 S 250 ALA MET TYR TYR CYS VAL ARG SER ILE TYR TYR TYR GLY SEQRES 9 S 250 SER SER PRO PHE ASP PHE TRP GLY GLN GLY THR THR LEU SEQRES 10 S 250 THR VAL SER SER GLY GLY GLY GLY SER GLY GLY GLY GLY SEQRES 11 S 250 SER GLY GLY GLY SER SER ASP ILE VAL MET THR GLN ALA SEQRES 12 S 250 THR SER SER VAL PRO VAL THR PRO GLY GLU SER VAL SER SEQRES 13 S 250 ILE SER CYS ARG SER SER LYS SER LEU LEU HIS SER ASN SEQRES 14 S 250 GLY ASN THR TYR LEU TYR TRP PHE LEU GLN ARG PRO GLY SEQRES 15 S 250 GLN SER PRO GLN LEU LEU ILE TYR ARG MET SER ASN LEU SEQRES 16 S 250 ALA SER GLY VAL PRO ASP ARG PHE SER GLY SER GLY SER SEQRES 17 S 250 GLY THR ALA PHE THR LEU THR ILE SER ARG LEU GLU ALA SEQRES 18 S 250 GLU ASP VAL GLY VAL TYR TYR CYS MET GLN HIS LEU GLU SEQRES 19 S 250 TYR PRO LEU THR PHE GLY ALA GLY THR LYS LEU GLU LEU SEQRES 20 S 250 LYS GLY SER HET AND R1001 21 HETNAM AND 3-BETA-HYDROXY-5-ANDROSTEN-17-ONE FORMUL 7 AND C19 H28 O2 HELIX 1 AA1 SER A 23 THR A 50 1 28 HELIX 2 AA2 GLY A 62 HIS A 74 1 13 HELIX 3 AA3 TRP A 244 ASN A 249 5 6 HELIX 4 AA4 ARG A 265 ASN A 279 1 15 HELIX 5 AA5 LYS A 293 GLY A 304 1 12 HELIX 6 AA6 LYS A 307 PHE A 312 1 6 HELIX 7 AA7 ASP A 331 THR A 350 1 20 HELIX 8 AA8 GLU A 370 TYR A 391 1 22 HELIX 9 AA9 ASP B 5 ALA B 26 1 22 HELIX 10 AB1 THR B 29 THR B 34 1 6 HELIX 11 AB2 ILE G 9 ASN G 24 1 16 HELIX 12 AB3 LYS G 29 HIS G 44 1 16 HELIX 13 AB4 THR N 28 TYR N 32 5 5 HELIX 14 AB5 GLY N 62 LYS N 65 5 4 HELIX 15 AB6 LEU R 620 PHE R 645 1 26 HELIX 16 AB7 GLU R 646 ARG R 649 5 4 HELIX 17 AB8 ASP R 651 ILE R 677 1 27 HELIX 18 AB9 THR R 682 LEU R 713 1 32 HELIX 19 AC1 LYS R 725 SER R 749 1 25 HELIX 20 AC2 PRO R 750 TYR R 753 5 4 HELIX 21 AC3 VAL R 782 LYS R 809 1 28 HELIX 22 AC4 LEU R 824 GLY R 835 1 12 HELIX 23 AC5 ILE R 836 GLY R 839 5 4 HELIX 24 AC6 PHE R 840 TRP R 845 1 6 HELIX 25 AC7 ASN R 849 PHE R 859 1 11 HELIX 26 AC8 LEU R 862 CYS R 872 1 11 HELIX 27 AC9 LYS R 875 TRP R 882 1 8 HELIX 28 AD1 ASP S 62 LYS S 65 5 4 HELIX 29 AD2 ARG S 87 THR S 91 5 5 HELIX 30 AD3 GLU S 220 VAL S 224 5 5 SHEET 1 AA1 6 ILE A 217 VAL A 224 0 SHEET 2 AA1 6 VAL A 227 VAL A 234 -1 O MET A 231 N THR A 220 SHEET 3 AA1 6 ARG A 52 LEU A 55 1 N LEU A 55 O PHE A 232 SHEET 4 AA1 6 ALA A 253 ASP A 259 1 O ILE A 255 N LEU A 54 SHEET 5 AA1 6 SER A 286 ASN A 292 1 O ILE A 288 N ILE A 254 SHEET 6 AA1 6 CYS A 359 PHE A 363 1 O HIS A 362 N LEU A 291 SHEET 1 AA2 4 THR B 47 ARG B 52 0 SHEET 2 AA2 4 PHE B 335 TRP B 339 -1 O ILE B 338 N ARG B 48 SHEET 3 AA2 4 VAL B 327 GLY B 330 -1 N VAL B 327 O TRP B 339 SHEET 4 AA2 4 CYS B 317 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 ALA B 60 SHEET 3 AA3 4 LYS B 78 ASP B 83 -1 O TRP B 82 N LEU B 70 SHEET 4 AA3 4 LYS B 89 PRO B 94 -1 O ILE B 93 N LEU B 79 SHEET 1 AA4 4 VAL B 100 TYR B 105 0 SHEET 2 AA4 4 TYR B 111 GLY B 116 -1 O GLY B 115 N THR B 102 SHEET 3 AA4 4 ILE B 120 ASN B 125 -1 O TYR B 124 N VAL B 112 SHEET 4 AA4 4 ARG B 134 ALA B 140 -1 O SER B 136 N ILE B 123 SHEET 1 AA5 4 LEU B 146 PHE B 151 0 SHEET 2 AA5 4 GLN B 156 SER B 161 -1 O SER B 160 N CYS B 148 SHEET 3 AA5 4 THR B 165 ASP B 170 -1 O TRP B 169 N ILE B 157 SHEET 4 AA5 4 GLN B 176 THR B 181 -1 O PHE B 180 N CYS B 166 SHEET 1 AA6 4 VAL B 187 LEU B 192 0 SHEET 2 AA6 4 LEU B 198 ALA B 203 -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 ALA B 231 SHEET 3 AA7 4 CYS B 250 ASP B 254 -1 O PHE B 253 N PHE B 241 SHEET 4 AA7 4 GLU B 260 TYR B 264 -1 O TYR B 264 N CYS B 250 SHEET 1 AA8 4 ILE B 273 SER B 277 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 GLU N 6 0 SHEET 2 AA9 4 LEU N 18 SER N 25 -1 O ALA N 23 N GLN N 5 SHEET 3 AA9 4 THR N 78 MET N 83 -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 LEU N 11 VAL N 12 0 SHEET 2 AB1 6 THR N 122 VAL N 126 1 O THR N 125 N VAL N 12 SHEET 3 AB1 6 ALA N 92 ARG N 98 -1 N ALA N 92 O VAL N 124 SHEET 4 AB1 6 MET N 34 GLN N 39 -1 N VAL N 37 O TYR N 95 SHEET 5 AB1 6 LEU N 45 ILE N 51 -1 O VAL N 48 N TRP N 36 SHEET 6 AB1 6 SER N 59 TYR N 60 -1 O SER N 59 N ASP N 50 SHEET 1 AB2 4 GLN S 3 SER S 7 0 SHEET 2 AB2 4 LYS S 19 SER S 25 -1 O SER S 21 N SER S 7 SHEET 3 AB2 4 THR S 78 MET S 83 -1 O LEU S 81 N LEU S 20 SHEET 4 AB2 4 PHE S 68 ASP S 73 -1 N THR S 69 O GLN S 82 SHEET 1 AB3 6 LEU S 11 VAL S 12 0 SHEET 2 AB3 6 THR S 115 VAL S 119 1 O THR S 118 N VAL S 12 SHEET 3 AB3 6 ALA S 92 ARG S 98 -1 N ALA S 92 O LEU S 117 SHEET 4 AB3 6 MET S 34 GLN S 39 -1 N VAL S 37 O TYR S 95 SHEET 5 AB3 6 LEU S 45 ILE S 51 -1 O VAL S 48 N TRP S 36 SHEET 6 AB3 6 ILE S 58 TYR S 60 -1 O TYR S 59 N TYR S 50 SHEET 1 AB4 4 LEU S 11 VAL S 12 0 SHEET 2 AB4 4 THR S 115 VAL S 119 1 O THR S 118 N VAL S 12 SHEET 3 AB4 4 ALA S 92 ARG S 98 -1 N ALA S 92 O LEU S 117 SHEET 4 AB4 4 PHE S 110 TRP S 111 -1 O PHE S 110 N ARG S 98 SHEET 1 AB5 4 MET S 140 THR S 141 0 SHEET 2 AB5 4 VAL S 155 SER S 161 -1 O ARG S 160 N THR S 141 SHEET 3 AB5 4 ALA S 211 ILE S 216 -1 O PHE S 212 N CYS S 159 SHEET 4 AB5 4 PHE S 203 GLY S 207 -1 N SER S 204 O THR S 215 SHEET 1 AB6 5 ASN S 194 LEU S 195 0 SHEET 2 AB6 5 PRO S 185 TYR S 190 -1 N TYR S 190 O ASN S 194 SHEET 3 AB6 5 TRP S 176 GLN S 179 -1 N TRP S 176 O ILE S 189 SHEET 4 AB6 5 VAL S 226 TYR S 228 -1 O VAL S 226 N GLN S 179 SHEET 5 AB6 5 THR S 243 LYS S 244 -1 O THR S 243 N TYR S 227 SSBOND 1 CYS N 22 CYS N 96 1555 1555 2.03 SSBOND 2 CYS N 99 CYS N 107 1555 1555 2.01 SSBOND 3 CYS R 686 CYS R 770 1555 1555 2.04 SSBOND 4 CYS S 22 CYS S 96 1555 1555 2.03 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