HEADER TRANSPORT PROTEIN/IMMUNE SYSTEM 24-DEC-24 9MNZ TITLE CRYO-EM STRUCTURE OF HUMAN MPC IN COMPLEX WITH UK5099 IN NANODISCS COMPND MOL_ID: 1; COMPND 2 MOLECULE: FAB_8D3_2 HEAVY CHAIN; COMPND 3 CHAIN: D; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: NANOBODY; COMPND 7 CHAIN: C; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: MITOCHONDRIAL PYRUVATE CARRIER 2; COMPND 11 CHAIN: B; COMPND 12 SYNONYM: BRAIN PROTEIN 44; COMPND 13 ENGINEERED: YES; COMPND 14 MOL_ID: 4; COMPND 15 MOLECULE: MITOCHONDRIAL PYRUVATE CARRIER 1; COMPND 16 CHAIN: A; COMPND 17 SYNONYM: BRAIN PROTEIN 44-LIKE PROTEIN; COMPND 18 ENGINEERED: YES; COMPND 19 MOL_ID: 5; COMPND 20 MOLECULE: MBP-PRA/G; COMPND 21 CHAIN: F; COMPND 22 ENGINEERED: YES; COMPND 23 MOL_ID: 6; COMPND 24 MOLECULE: FAB_8D3_2 LIGHT CHAIN; COMPND 25 CHAIN: E; COMPND 26 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: MOUSE; SOURCE 4 ORGANISM_TAXID: 10090; SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT; SOURCE 10 ORGANISM_TAXID: 32630; SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 12 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 13 MOL_ID: 3; SOURCE 14 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 15 ORGANISM_COMMON: HUMAN; SOURCE 16 ORGANISM_TAXID: 9606; SOURCE 17 GENE: MPC2, BRP44; SOURCE 18 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 19 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 20 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 21 MOL_ID: 4; SOURCE 22 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 23 ORGANISM_COMMON: HUMAN; SOURCE 24 ORGANISM_TAXID: 9606; SOURCE 25 GENE: MPC1, BRP44L, CGI-129, HSPC040, PNAS-115; SOURCE 26 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 27 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 28 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 29 MOL_ID: 5; SOURCE 30 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI; SOURCE 31 ORGANISM_TAXID: 562; SOURCE 32 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 33 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 34 MOL_ID: 6; SOURCE 35 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 36 ORGANISM_COMMON: MOUSE; SOURCE 37 ORGANISM_TAXID: 10090; SOURCE 38 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 39 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 40 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS MEMBRANE TRANSPORTER, TRANSPORT PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR J.ZHANG,Z.HE,L.FENG REVDAT 1 05-MAR-25 9MNZ 0 JRNL AUTH Z.HE,J.ZHANG,Y.XU,E.J.FINE,C.M.SUOMIVUORI,R.O.DROR,L.FENG JRNL TITL STRUCTURE OF MITOCHONDRIAL PYRUVATE CARRIER AND ITS JRNL TITL 2 INHIBITION MECHANISM JRNL REF NATURE 2025 JRNL REFN ESSN 1476-4687 JRNL DOI 10.1038/S41586-025-08667-Y REMARK 2 REMARK 2 RESOLUTION. 2.73 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) : 2.730 REMARK 3 NUMBER OF PARTICLES : 570457 REMARK 3 CTF CORRECTION METHOD : NONE REMARK 3 REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL REMARK 3 REMARK 3 OTHER DETAILS: NULL REMARK 4 REMARK 4 9MNZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-JAN-25. REMARK 100 THE DEPOSITION ID IS D_1000283722. 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 : HUMAN MPC IN NANODISCS WITH REMARK 245 UK5099 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 : TFS KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 (6K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1200.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2000.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : 2.70 REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 5000.00 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : NULL REMARK 245 CALIBRATED MAGNIFICATION : NULL REMARK 245 SOURCE : FIELD EMISSION GUN REMARK 245 ACCELERATION VOLTAGE (KV) : 300 REMARK 245 IMAGING DETAILS : NULL REMARK 247 REMARK 247 ELECTRON MICROSCOPY REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION REMARK 247 OF THE STRUCTURE FACTORS. REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, C, B, A, F, E REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 MET D -18 REMARK 465 ASP D -17 REMARK 465 TRP D -16 REMARK 465 THR D -15 REMARK 465 TRP D -14 REMARK 465 ARG D -13 REMARK 465 VAL D -12 REMARK 465 PHE D -11 REMARK 465 CYS D -10 REMARK 465 LEU D -9 REMARK 465 LEU D -8 REMARK 465 ALA D -7 REMARK 465 VAL D -6 REMARK 465 ALA D -5 REMARK 465 PRO D -4 REMARK 465 GLY D -3 REMARK 465 ALA D -2 REMARK 465 HIS D -1 REMARK 465 SER D 0 REMARK 465 THR D 126 REMARK 465 LYS D 127 REMARK 465 GLY D 128 REMARK 465 PRO D 129 REMARK 465 SER D 130 REMARK 465 VAL D 131 REMARK 465 PHE D 132 REMARK 465 PRO D 133 REMARK 465 LEU D 134 REMARK 465 ALA D 135 REMARK 465 PRO D 136 REMARK 465 SER D 137 REMARK 465 SER D 138 REMARK 465 LYS D 139 REMARK 465 SER D 140 REMARK 465 THR D 141 REMARK 465 SER D 142 REMARK 465 GLY D 143 REMARK 465 GLY D 144 REMARK 465 THR D 145 REMARK 465 ALA D 146 REMARK 465 ALA D 147 REMARK 465 LEU D 148 REMARK 465 GLY D 149 REMARK 465 CYS D 150 REMARK 465 LEU D 151 REMARK 465 VAL D 152 REMARK 465 LYS D 153 REMARK 465 ASP D 154 REMARK 465 TYR D 155 REMARK 465 PHE D 156 REMARK 465 PRO D 157 REMARK 465 GLU D 158 REMARK 465 PRO D 159 REMARK 465 VAL D 160 REMARK 465 THR D 161 REMARK 465 VAL D 162 REMARK 465 SER D 163 REMARK 465 TRP D 164 REMARK 465 ASN D 165 REMARK 465 SER D 166 REMARK 465 GLY D 167 REMARK 465 ALA D 168 REMARK 465 LEU D 169 REMARK 465 THR D 170 REMARK 465 SER D 171 REMARK 465 GLY D 172 REMARK 465 VAL D 173 REMARK 465 HIS D 174 REMARK 465 THR D 175 REMARK 465 PHE D 176 REMARK 465 PRO D 177 REMARK 465 ALA D 178 REMARK 465 VAL D 179 REMARK 465 LEU D 180 REMARK 465 GLN D 181 REMARK 465 SER D 182 REMARK 465 SER D 183 REMARK 465 GLY D 184 REMARK 465 LEU D 185 REMARK 465 TYR D 186 REMARK 465 SER D 187 REMARK 465 LEU D 188 REMARK 465 SER D 189 REMARK 465 SER D 190 REMARK 465 VAL D 191 REMARK 465 VAL D 192 REMARK 465 THR D 193 REMARK 465 VAL D 194 REMARK 465 PRO D 195 REMARK 465 SER D 196 REMARK 465 SER D 197 REMARK 465 SER D 198 REMARK 465 LEU D 199 REMARK 465 GLY D 200 REMARK 465 THR D 201 REMARK 465 GLN D 202 REMARK 465 THR D 203 REMARK 465 TYR D 204 REMARK 465 ILE D 205 REMARK 465 CYS D 206 REMARK 465 ASN D 207 REMARK 465 VAL D 208 REMARK 465 ASN D 209 REMARK 465 HIS D 210 REMARK 465 LYS D 211 REMARK 465 PRO D 212 REMARK 465 SER D 213 REMARK 465 ASN D 214 REMARK 465 THR D 215 REMARK 465 LYS D 216 REMARK 465 VAL D 217 REMARK 465 ASP D 218 REMARK 465 LYS D 219 REMARK 465 LYS D 220 REMARK 465 VAL D 221 REMARK 465 GLU D 222 REMARK 465 PRO D 223 REMARK 465 LYS D 224 REMARK 465 SER D 225 REMARK 465 CYS D 226 REMARK 465 GLY D 227 REMARK 465 SER D 228 REMARK 465 LEU D 229 REMARK 465 GLU D 230 REMARK 465 VAL D 231 REMARK 465 LEU D 232 REMARK 465 PHE D 233 REMARK 465 GLN D 234 REMARK 465 GLY D 235 REMARK 465 PRO D 236 REMARK 465 HIS D 237 REMARK 465 HIS D 238 REMARK 465 HIS D 239 REMARK 465 HIS D 240 REMARK 465 HIS D 241 REMARK 465 HIS D 242 REMARK 465 HIS D 243 REMARK 465 HIS D 244 REMARK 465 HIS D 245 REMARK 465 HIS D 246 REMARK 465 MET C -21 REMARK 465 LYS C -20 REMARK 465 TYR C -19 REMARK 465 LEU C -18 REMARK 465 LEU C -17 REMARK 465 PRO C -16 REMARK 465 THR C -15 REMARK 465 ALA C -14 REMARK 465 ALA C -13 REMARK 465 ALA C -12 REMARK 465 GLY C -11 REMARK 465 LEU C -10 REMARK 465 LEU C -9 REMARK 465 LEU C -8 REMARK 465 LEU C -7 REMARK 465 ALA C -6 REMARK 465 ALA C -5 REMARK 465 GLN C -4 REMARK 465 PRO C -3 REMARK 465 ALA C -2 REMARK 465 MET C -1 REMARK 465 ALA C 0 REMARK 465 HIS C 124 REMARK 465 HIS C 125 REMARK 465 HIS C 126 REMARK 465 HIS C 127 REMARK 465 HIS C 128 REMARK 465 HIS C 129 REMARK 465 HIS C 130 REMARK 465 MET B 1 REMARK 465 SER B 2 REMARK 465 ALA B 3 REMARK 465 ALA B 4 REMARK 465 GLY B 5 REMARK 465 HIS B 126 REMARK 465 LYS B 127 REMARK 465 MET A 1 REMARK 465 ALA A 2 REMARK 465 GLY A 3 REMARK 465 ALA A 4 REMARK 465 LEU A 5 REMARK 465 VAL A 6 REMARK 465 ARG A 7 REMARK 465 LYS A 8 REMARK 465 MET F 1 REMARK 465 LYS F 2 REMARK 465 ILE F 3 REMARK 465 GLU F 4 REMARK 465 GLU F 5 REMARK 465 GLY F 6 REMARK 465 LYS F 7 REMARK 465 LEU F 8 REMARK 465 VAL F 9 REMARK 465 ILE F 10 REMARK 465 TRP F 11 REMARK 465 ILE F 12 REMARK 465 ASN F 13 REMARK 465 GLY F 14 REMARK 465 ASP F 15 REMARK 465 LYS F 16 REMARK 465 GLY F 17 REMARK 465 TYR F 18 REMARK 465 ASN F 19 REMARK 465 GLY F 20 REMARK 465 LEU F 21 REMARK 465 ALA F 22 REMARK 465 GLU F 23 REMARK 465 VAL F 24 REMARK 465 GLY F 25 REMARK 465 LYS F 26 REMARK 465 LYS F 27 REMARK 465 PHE F 28 REMARK 465 GLU F 29 REMARK 465 LYS F 30 REMARK 465 ASP F 31 REMARK 465 THR F 32 REMARK 465 GLY F 33 REMARK 465 ILE F 34 REMARK 465 LYS F 35 REMARK 465 VAL F 36 REMARK 465 THR F 37 REMARK 465 VAL F 38 REMARK 465 GLU F 39 REMARK 465 HIS F 40 REMARK 465 PRO F 41 REMARK 465 ASP F 42 REMARK 465 LYS F 43 REMARK 465 LEU F 44 REMARK 465 GLU F 45 REMARK 465 GLU F 46 REMARK 465 LYS F 47 REMARK 465 PHE F 48 REMARK 465 PRO F 49 REMARK 465 GLN F 50 REMARK 465 VAL F 51 REMARK 465 ALA F 52 REMARK 465 ALA F 53 REMARK 465 THR F 54 REMARK 465 GLY F 55 REMARK 465 ASP F 56 REMARK 465 GLY F 57 REMARK 465 PRO F 58 REMARK 465 ASP F 59 REMARK 465 ILE F 60 REMARK 465 ILE F 61 REMARK 465 PHE F 62 REMARK 465 TRP F 63 REMARK 465 ALA F 64 REMARK 465 HIS F 65 REMARK 465 ASP F 66 REMARK 465 ARG F 67 REMARK 465 PHE F 68 REMARK 465 GLY F 69 REMARK 465 GLY F 70 REMARK 465 TYR F 71 REMARK 465 ALA F 72 REMARK 465 GLN F 73 REMARK 465 SER F 74 REMARK 465 GLY F 75 REMARK 465 LEU F 76 REMARK 465 LEU F 77 REMARK 465 ALA F 78 REMARK 465 GLU F 79 REMARK 465 ILE F 80 REMARK 465 THR F 81 REMARK 465 PRO F 82 REMARK 465 ASP F 83 REMARK 465 LYS F 84 REMARK 465 ALA F 85 REMARK 465 PHE F 86 REMARK 465 GLN F 87 REMARK 465 ASP F 88 REMARK 465 LYS F 89 REMARK 465 LEU F 90 REMARK 465 TYR F 91 REMARK 465 PRO F 92 REMARK 465 PHE F 93 REMARK 465 THR F 94 REMARK 465 TRP F 95 REMARK 465 ASP F 96 REMARK 465 ALA F 97 REMARK 465 VAL F 98 REMARK 465 ARG F 99 REMARK 465 TYR F 100 REMARK 465 ASN F 101 REMARK 465 GLY F 102 REMARK 465 LYS F 103 REMARK 465 LEU F 104 REMARK 465 ILE F 105 REMARK 465 ALA F 106 REMARK 465 TYR F 107 REMARK 465 PRO F 108 REMARK 465 ILE F 109 REMARK 465 ALA F 110 REMARK 465 VAL F 111 REMARK 465 GLU F 112 REMARK 465 ALA F 113 REMARK 465 LEU F 114 REMARK 465 SER F 115 REMARK 465 LEU F 116 REMARK 465 ILE F 117 REMARK 465 TYR F 118 REMARK 465 ASN F 119 REMARK 465 LYS F 120 REMARK 465 ASP F 121 REMARK 465 LEU F 122 REMARK 465 LEU F 123 REMARK 465 PRO F 124 REMARK 465 ASN F 125 REMARK 465 PRO F 126 REMARK 465 PRO F 127 REMARK 465 LYS F 128 REMARK 465 THR F 129 REMARK 465 TRP F 130 REMARK 465 GLU F 131 REMARK 465 GLU F 132 REMARK 465 ILE F 133 REMARK 465 PRO F 134 REMARK 465 ALA F 135 REMARK 465 LEU F 136 REMARK 465 ASP F 137 REMARK 465 LYS F 138 REMARK 465 GLU F 139 REMARK 465 LEU F 140 REMARK 465 LYS F 141 REMARK 465 ALA F 142 REMARK 465 LYS F 143 REMARK 465 GLY F 144 REMARK 465 LYS F 145 REMARK 465 SER F 146 REMARK 465 ALA F 147 REMARK 465 LEU F 148 REMARK 465 MET F 149 REMARK 465 PHE F 150 REMARK 465 ASN F 151 REMARK 465 LEU F 152 REMARK 465 GLN F 153 REMARK 465 GLU F 154 REMARK 465 PRO F 155 REMARK 465 TYR F 156 REMARK 465 PHE F 157 REMARK 465 THR F 158 REMARK 465 TRP F 159 REMARK 465 PRO F 160 REMARK 465 LEU F 161 REMARK 465 ILE F 162 REMARK 465 ALA F 163 REMARK 465 ALA F 164 REMARK 465 ASP F 165 REMARK 465 GLY F 166 REMARK 465 GLY F 167 REMARK 465 TYR F 168 REMARK 465 ALA F 169 REMARK 465 PHE F 170 REMARK 465 LYS F 171 REMARK 465 TYR F 172 REMARK 465 GLU F 173 REMARK 465 ASN F 174 REMARK 465 GLY F 175 REMARK 465 LYS F 176 REMARK 465 TYR F 177 REMARK 465 ASP F 178 REMARK 465 ILE F 179 REMARK 465 LYS F 180 REMARK 465 ASP F 181 REMARK 465 VAL F 182 REMARK 465 GLY F 183 REMARK 465 VAL F 184 REMARK 465 ASP F 185 REMARK 465 ASN F 186 REMARK 465 ALA F 187 REMARK 465 GLY F 188 REMARK 465 ALA F 189 REMARK 465 LYS F 190 REMARK 465 ALA F 191 REMARK 465 GLY F 192 REMARK 465 LEU F 193 REMARK 465 THR F 194 REMARK 465 PHE F 195 REMARK 465 LEU F 196 REMARK 465 VAL F 197 REMARK 465 ASP F 198 REMARK 465 LEU F 199 REMARK 465 ILE F 200 REMARK 465 LYS F 201 REMARK 465 ASN F 202 REMARK 465 LYS F 203 REMARK 465 HIS F 204 REMARK 465 MET F 205 REMARK 465 ASN F 206 REMARK 465 ALA F 207 REMARK 465 ASP F 208 REMARK 465 THR F 209 REMARK 465 ASP F 210 REMARK 465 TYR F 211 REMARK 465 SER F 212 REMARK 465 ILE F 213 REMARK 465 ALA F 214 REMARK 465 GLU F 215 REMARK 465 ALA F 216 REMARK 465 ALA F 217 REMARK 465 PHE F 218 REMARK 465 ASN F 219 REMARK 465 LYS F 220 REMARK 465 GLY F 221 REMARK 465 GLU F 222 REMARK 465 THR F 223 REMARK 465 ALA F 224 REMARK 465 MET F 225 REMARK 465 THR F 226 REMARK 465 ILE F 227 REMARK 465 ASN F 228 REMARK 465 GLY F 229 REMARK 465 PRO F 230 REMARK 465 TRP F 231 REMARK 465 ALA F 232 REMARK 465 TRP F 233 REMARK 465 SER F 234 REMARK 465 ASN F 235 REMARK 465 ILE F 236 REMARK 465 ASP F 237 REMARK 465 THR F 238 REMARK 465 SER F 239 REMARK 465 LYS F 240 REMARK 465 VAL F 241 REMARK 465 ASN F 242 REMARK 465 TYR F 243 REMARK 465 GLY F 244 REMARK 465 VAL F 245 REMARK 465 THR F 246 REMARK 465 VAL F 247 REMARK 465 LEU F 248 REMARK 465 PRO F 249 REMARK 465 THR F 250 REMARK 465 PHE F 251 REMARK 465 LYS F 252 REMARK 465 GLY F 253 REMARK 465 GLN F 254 REMARK 465 PRO F 255 REMARK 465 SER F 256 REMARK 465 LYS F 257 REMARK 465 PRO F 258 REMARK 465 PHE F 259 REMARK 465 VAL F 260 REMARK 465 GLY F 261 REMARK 465 VAL F 262 REMARK 465 LEU F 263 REMARK 465 SER F 264 REMARK 465 ALA F 265 REMARK 465 GLY F 266 REMARK 465 ILE F 267 REMARK 465 ASN F 268 REMARK 465 ALA F 269 REMARK 465 ALA F 270 REMARK 465 SER F 271 REMARK 465 PRO F 272 REMARK 465 ASN F 273 REMARK 465 LYS F 274 REMARK 465 GLU F 275 REMARK 465 LEU F 276 REMARK 465 ALA F 277 REMARK 465 LYS F 278 REMARK 465 GLU F 279 REMARK 465 PHE F 280 REMARK 465 LEU F 281 REMARK 465 GLU F 282 REMARK 465 ASN F 283 REMARK 465 TYR F 284 REMARK 465 LEU F 285 REMARK 465 LEU F 286 REMARK 465 THR F 287 REMARK 465 ASP F 288 REMARK 465 GLU F 289 REMARK 465 GLY F 290 REMARK 465 LEU F 291 REMARK 465 GLU F 292 REMARK 465 ALA F 293 REMARK 465 VAL F 294 REMARK 465 ASN F 295 REMARK 465 LYS F 296 REMARK 465 ASP F 297 REMARK 465 LYS F 298 REMARK 465 PRO F 299 REMARK 465 LEU F 300 REMARK 465 GLY F 301 REMARK 465 ALA F 302 REMARK 465 VAL F 303 REMARK 465 ALA F 304 REMARK 465 LEU F 305 REMARK 465 LYS F 306 REMARK 465 SER F 307 REMARK 465 TYR F 308 REMARK 465 GLU F 309 REMARK 465 GLU F 310 REMARK 465 GLU F 311 REMARK 465 LEU F 312 REMARK 465 ALA F 313 REMARK 465 LYS F 314 REMARK 465 ASP F 315 REMARK 465 PRO F 316 REMARK 465 ARG F 317 REMARK 465 ILE F 318 REMARK 465 ALA F 319 REMARK 465 ALA F 320 REMARK 465 THR F 321 REMARK 465 MET F 322 REMARK 465 GLU F 323 REMARK 465 ASN F 324 REMARK 465 ALA F 325 REMARK 465 GLN F 326 REMARK 465 LYS F 327 REMARK 465 GLY F 328 REMARK 465 GLU F 329 REMARK 465 ILE F 330 REMARK 465 MET F 331 REMARK 465 PRO F 332 REMARK 465 ASN F 333 REMARK 465 ILE F 334 REMARK 465 PRO F 335 REMARK 465 GLN F 336 REMARK 465 MET F 337 REMARK 465 SER F 338 REMARK 465 ALA F 339 REMARK 465 PHE F 340 REMARK 465 TRP F 341 REMARK 465 TYR F 342 REMARK 465 ALA F 343 REMARK 465 VAL F 344 REMARK 465 ARG F 345 REMARK 465 THR F 346 REMARK 465 ALA F 347 REMARK 465 VAL F 348 REMARK 465 ILE F 349 REMARK 465 ASN F 350 REMARK 465 ALA F 351 REMARK 465 ALA F 352 REMARK 465 SER F 353 REMARK 465 GLY F 354 REMARK 465 ARG F 355 REMARK 465 GLN F 356 REMARK 465 THR F 357 REMARK 465 VAL F 358 REMARK 465 ASP F 359 REMARK 465 GLN F 360 REMARK 465 ALA F 361 REMARK 465 LEU F 362 REMARK 465 LYS F 409 REMARK 465 GLY F 410 REMARK 465 GLY F 411 REMARK 465 SER F 412 REMARK 465 GLY F 413 REMARK 465 GLY F 414 REMARK 465 ALA F 415 REMARK 465 GLY F 416 REMARK 465 SER F 417 REMARK 465 GLY F 418 REMARK 465 GLY F 468 REMARK 465 GLY F 469 REMARK 465 GLY F 470 REMARK 465 SER F 471 REMARK 465 GLY F 472 REMARK 465 GLY F 473 REMARK 465 GLY F 474 REMARK 465 SER F 475 REMARK 465 GLY F 476 REMARK 465 GLY F 477 REMARK 465 SER F 478 REMARK 465 ALA F 479 REMARK 465 VAL F 480 REMARK 465 THR F 481 REMARK 465 THR F 482 REMARK 465 TYR F 483 REMARK 465 LYS F 484 REMARK 465 LEU F 485 REMARK 465 VAL F 486 REMARK 465 ILE F 487 REMARK 465 ASN F 488 REMARK 465 GLY F 489 REMARK 465 LYS F 490 REMARK 465 THR F 491 REMARK 465 LEU F 492 REMARK 465 LYS F 493 REMARK 465 GLY F 494 REMARK 465 GLU F 495 REMARK 465 THR F 496 REMARK 465 THR F 497 REMARK 465 THR F 498 REMARK 465 LYS F 499 REMARK 465 ALA F 500 REMARK 465 VAL F 501 REMARK 465 ASP F 502 REMARK 465 ALA F 503 REMARK 465 GLU F 504 REMARK 465 THR F 505 REMARK 465 ALA F 506 REMARK 465 GLU F 507 REMARK 465 LYS F 508 REMARK 465 ALA F 509 REMARK 465 PHE F 510 REMARK 465 LYS F 511 REMARK 465 GLN F 512 REMARK 465 TYR F 513 REMARK 465 ALA F 514 REMARK 465 ASN F 515 REMARK 465 ASP F 516 REMARK 465 ASN F 517 REMARK 465 GLY F 518 REMARK 465 VAL F 519 REMARK 465 ASP F 520 REMARK 465 GLY F 521 REMARK 465 VAL F 522 REMARK 465 TRP F 523 REMARK 465 THR F 524 REMARK 465 TYR F 525 REMARK 465 ASP F 526 REMARK 465 ASP F 527 REMARK 465 ALA F 528 REMARK 465 THR F 529 REMARK 465 LYS F 530 REMARK 465 THR F 531 REMARK 465 PHE F 532 REMARK 465 THR F 533 REMARK 465 VAL F 534 REMARK 465 THR F 535 REMARK 465 GLU F 536 REMARK 465 GLY F 537 REMARK 465 SER F 538 REMARK 465 GLY F 539 REMARK 465 HIS F 540 REMARK 465 HIS F 541 REMARK 465 HIS F 542 REMARK 465 HIS F 543 REMARK 465 HIS F 544 REMARK 465 HIS F 545 REMARK 465 MET E -19 REMARK 465 VAL E -18 REMARK 465 LEU E -17 REMARK 465 GLN E -16 REMARK 465 THR E -15 REMARK 465 GLN E -14 REMARK 465 VAL E -13 REMARK 465 PHE E -12 REMARK 465 ILE E -11 REMARK 465 SER E -10 REMARK 465 LEU E -9 REMARK 465 LEU E -8 REMARK 465 LEU E -7 REMARK 465 TRP E -6 REMARK 465 ILE E -5 REMARK 465 SER E -4 REMARK 465 GLY E -3 REMARK 465 ALA E -2 REMARK 465 TYR E -1 REMARK 465 GLY E 0 REMARK 465 ARG E 113 REMARK 465 THR E 114 REMARK 465 VAL E 115 REMARK 465 ALA E 116 REMARK 465 ALA E 117 REMARK 465 PRO E 118 REMARK 465 SER E 119 REMARK 465 VAL E 120 REMARK 465 PHE E 121 REMARK 465 ILE E 122 REMARK 465 PHE E 123 REMARK 465 PRO E 124 REMARK 465 PRO E 125 REMARK 465 SER E 126 REMARK 465 ASP E 127 REMARK 465 GLU E 128 REMARK 465 GLN E 129 REMARK 465 LEU E 130 REMARK 465 LYS E 131 REMARK 465 SER E 132 REMARK 465 GLY E 133 REMARK 465 THR E 134 REMARK 465 ALA E 135 REMARK 465 SER E 136 REMARK 465 VAL E 137 REMARK 465 VAL E 138 REMARK 465 CYS E 139 REMARK 465 LEU E 140 REMARK 465 LEU E 141 REMARK 465 ASN E 142 REMARK 465 ASN E 143 REMARK 465 PHE E 144 REMARK 465 TYR E 145 REMARK 465 PRO E 146 REMARK 465 ARG E 147 REMARK 465 GLU E 148 REMARK 465 ALA E 149 REMARK 465 LYS E 150 REMARK 465 VAL E 151 REMARK 465 GLN E 152 REMARK 465 TRP E 153 REMARK 465 LYS E 154 REMARK 465 VAL E 155 REMARK 465 ASP E 156 REMARK 465 ASN E 157 REMARK 465 ALA E 158 REMARK 465 LEU E 159 REMARK 465 GLN E 160 REMARK 465 SER E 161 REMARK 465 GLY E 162 REMARK 465 ASN E 163 REMARK 465 SER E 164 REMARK 465 GLN E 165 REMARK 465 GLU E 166 REMARK 465 SER E 167 REMARK 465 VAL E 168 REMARK 465 THR E 169 REMARK 465 GLU E 170 REMARK 465 GLN E 171 REMARK 465 ASP E 172 REMARK 465 SER E 173 REMARK 465 LYS E 174 REMARK 465 ASP E 175 REMARK 465 SER E 176 REMARK 465 THR E 177 REMARK 465 TYR E 178 REMARK 465 SER E 179 REMARK 465 LEU E 180 REMARK 465 SER E 181 REMARK 465 SER E 182 REMARK 465 THR E 183 REMARK 465 LEU E 184 REMARK 465 THR E 185 REMARK 465 LEU E 186 REMARK 465 SER E 187 REMARK 465 LYS E 188 REMARK 465 ALA E 189 REMARK 465 ASP E 190 REMARK 465 TYR E 191 REMARK 465 GLU E 192 REMARK 465 LYS E 193 REMARK 465 HIS E 194 REMARK 465 LYS E 195 REMARK 465 VAL E 196 REMARK 465 TYR E 197 REMARK 465 ALA E 198 REMARK 465 CYS E 199 REMARK 465 GLU E 200 REMARK 465 VAL E 201 REMARK 465 THR E 202 REMARK 465 HIS E 203 REMARK 465 GLN E 204 REMARK 465 GLY E 205 REMARK 465 LEU E 206 REMARK 465 SER E 207 REMARK 465 SER E 208 REMARK 465 PRO E 209 REMARK 465 VAL E 210 REMARK 465 THR E 211 REMARK 465 LYS E 212 REMARK 465 SER E 213 REMARK 465 PHE E 214 REMARK 465 ASN E 215 REMARK 465 ARG E 216 REMARK 465 GLY E 217 REMARK 465 GLU E 218 REMARK 465 CYS E 219 REMARK 465 TRP E 220 REMARK 465 SER E 221 REMARK 465 HIS E 222 REMARK 465 PRO E 223 REMARK 465 GLN E 224 REMARK 465 PHE E 225 REMARK 465 GLU E 226 REMARK 465 LYS E 227 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 PRO D 14 170.07 -59.30 REMARK 500 LYS D 16 -163.21 -75.90 REMARK 500 SER D 25 145.75 -173.32 REMARK 500 PHE D 29 43.61 -81.42 REMARK 500 GLU D 42 -31.28 -139.74 REMARK 500 MET D 43 2.97 -62.31 REMARK 500 VAL D 48 -52.35 -124.35 REMARK 500 ARG D 87 -169.43 -115.76 REMARK 500 ALA D 92 -175.65 -174.29 REMARK 500 MET D 110 130.77 -36.56 REMARK 500 SER C 7 148.37 -178.67 REMARK 500 LEU C 101 -61.16 -121.60 REMARK 500 ALA B 36 70.60 -101.11 REMARK 500 PRO B 38 16.87 -66.77 REMARK 500 ARG B 39 29.81 -140.03 REMARK 500 THR B 40 -168.52 -118.64 REMARK 500 PRO B 63 118.34 -38.42 REMARK 500 ARG B 113 0.03 -58.19 REMARK 500 HIS A 26 -38.43 -37.43 REMARK 500 PRO A 48 37.11 -78.04 REMARK 500 GLU A 111 24.78 -142.34 REMARK 500 THR F 374 -176.30 -68.12 REMARK 500 ASP F 388 74.12 -165.53 REMARK 500 ASN F 434 -178.93 -64.84 REMARK 500 SER E 9 -50.32 -126.84 REMARK 500 GLN E 27 -168.75 -166.82 REMARK 500 TYR E 38 52.63 -115.36 REMARK 500 ALA E 57 -9.05 66.31 REMARK 500 SER E 58 -2.04 -142.68 REMARK 500 ASP E 66 3.36 -66.85 REMARK 500 ASP E 88 71.12 -107.85 REMARK 500 ALA E 90 -169.16 -179.52 REMARK 500 TYR E 97 38.05 -149.13 REMARK 500 LEU E 98 -63.72 -93.12 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-48444 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF HUMAN MPC IN COMPLEX WITH UK5099 IN NANODISCS DBREF 9MNZ D -18 246 PDB 9MNZ 9MNZ -18 246 DBREF 9MNZ C -21 130 PDB 9MNZ 9MNZ -21 130 DBREF 9MNZ B 1 127 UNP O95563 MPC2_HUMAN 1 127 DBREF 9MNZ A 1 109 UNP Q9Y5U8 MPC1_HUMAN 1 109 DBREF 9MNZ F 1 545 PDB 9MNZ 9MNZ 1 545 DBREF 9MNZ E -19 227 PDB 9MNZ 9MNZ -19 227 SEQADV 9MNZ LEU A 110 UNP Q9Y5U8 EXPRESSION TAG SEQADV 9MNZ GLU A 111 UNP Q9Y5U8 EXPRESSION TAG SEQADV 9MNZ VAL A 112 UNP Q9Y5U8 EXPRESSION TAG SEQADV 9MNZ LEU A 113 UNP Q9Y5U8 EXPRESSION TAG SEQADV 9MNZ PHE A 114 UNP Q9Y5U8 EXPRESSION TAG SEQADV 9MNZ GLN A 115 UNP Q9Y5U8 EXPRESSION TAG SEQRES 1 D 265 MET ASP TRP THR TRP ARG VAL PHE CYS LEU LEU ALA VAL SEQRES 2 D 265 ALA PRO GLY ALA HIS SER ASP VAL GLN LEU VAL GLU SER SEQRES 3 D 265 GLY GLY GLY LEU VAL GLN PRO GLY LYS SER LEU ARG LEU SEQRES 4 D 265 SER CYS ALA ALA SER GLY PHE THR PHE SER ASN PHE GLY SEQRES 5 D 265 MET HIS TRP VAL ARG GLN ALA PRO GLU MET GLY LEU GLU SEQRES 6 D 265 TRP VAL ALA TYR ILE SER SER GLY SER THR THR LYS TYR SEQRES 7 D 265 TYR GLY ASP THR VAL LYS GLY ARG PHE THR ILE SER ARG SEQRES 8 D 265 ASP ASN PRO LYS ASN THR LEU TYR LEU GLN MET ASN SER SEQRES 9 D 265 LEU ARG SER GLU ASP THR ALA MET TYR TYR CYS ALA ARG SEQRES 10 D 265 ARG PRO LEU TYR ASP GLY ASP TYR GLY TYR PRO MET ASP SEQRES 11 D 265 TYR TRP GLY GLN GLY THR SER VAL THR VAL SER SER ALA SEQRES 12 D 265 SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SEQRES 13 D 265 SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY CYS SEQRES 14 D 265 LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER SEQRES 15 D 265 TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR PHE SEQRES 16 D 265 PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SEQRES 17 D 265 SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR GLN SEQRES 18 D 265 THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR SEQRES 19 D 265 LYS VAL ASP LYS LYS VAL GLU PRO LYS SER CYS GLY SER SEQRES 20 D 265 LEU GLU VAL LEU PHE GLN GLY PRO HIS HIS HIS HIS HIS SEQRES 21 D 265 HIS HIS HIS HIS HIS SEQRES 1 C 152 MET LYS TYR LEU LEU PRO THR ALA ALA ALA GLY LEU LEU SEQRES 2 C 152 LEU LEU ALA ALA GLN PRO ALA MET ALA GLN VAL GLN LEU SEQRES 3 C 152 GLN GLU SER GLY GLY GLY LEU VAL GLN ALA GLY GLY SER SEQRES 4 C 152 LEU ARG LEU SER CYS ALA ALA SER GLY THR ILE PHE TYR SEQRES 5 C 152 TYR GLY THR MET GLY TRP TYR ARG GLN ALA PRO GLY LYS SEQRES 6 C 152 GLU ARG GLU LEU VAL ALA SER ILE ASN ARG GLY GLY ASN SEQRES 7 C 152 THR ASN TYR ALA ASP SER VAL LYS GLY ARG PHE THR ILE SEQRES 8 C 152 SER ARG ASP ASN ALA LYS ASN THR VAL TYR LEU GLN MET SEQRES 9 C 152 ASN SER LEU LYS PRO GLU ASP THR ALA VAL TYR TYR CYS SEQRES 10 C 152 ALA VAL LYS SER GLY LEU ILE TYR ALA HIS ARG TYR TRP SEQRES 11 C 152 GLY GLN GLY THR GLN VAL THR VAL SER SER LEU GLU HIS SEQRES 12 C 152 HIS HIS HIS HIS HIS HIS HIS HIS HIS SEQRES 1 B 127 MET SER ALA ALA GLY ALA ARG GLY LEU ARG ALA THR TYR SEQRES 2 B 127 HIS ARG LEU LEU ASP LYS VAL GLU LEU MET LEU PRO GLU SEQRES 3 B 127 LYS LEU ARG PRO LEU TYR ASN HIS PRO ALA GLY PRO ARG SEQRES 4 B 127 THR VAL PHE PHE TRP ALA PRO ILE MET LYS TRP GLY LEU SEQRES 5 B 127 VAL CYS ALA GLY LEU ALA ASP MET ALA ARG PRO ALA GLU SEQRES 6 B 127 LYS LEU SER THR ALA GLN SER ALA VAL LEU MET ALA THR SEQRES 7 B 127 GLY PHE ILE TRP SER ARG TYR SER LEU VAL ILE ILE PRO SEQRES 8 B 127 LYS ASN TRP SER LEU PHE ALA VAL ASN PHE PHE VAL GLY SEQRES 9 B 127 ALA ALA GLY ALA SER GLN LEU PHE ARG ILE TRP ARG TYR SEQRES 10 B 127 ASN GLN GLU LEU LYS ALA LYS ALA HIS LYS SEQRES 1 A 115 MET ALA GLY ALA LEU VAL ARG LYS ALA ALA ASP TYR VAL SEQRES 2 A 115 ARG SER LYS ASP PHE ARG ASP TYR LEU MET SER THR HIS SEQRES 3 A 115 PHE TRP GLY PRO VAL ALA ASN TRP GLY LEU PRO ILE ALA SEQRES 4 A 115 ALA ILE ASN ASP MET LYS LYS SER PRO GLU ILE ILE SER SEQRES 5 A 115 GLY ARG MET THR PHE ALA LEU CYS CYS TYR SER LEU THR SEQRES 6 A 115 PHE MET ARG PHE ALA TYR LYS VAL GLN PRO ARG ASN TRP SEQRES 7 A 115 LEU LEU PHE ALA CYS HIS ALA THR ASN GLU VAL ALA GLN SEQRES 8 A 115 LEU ILE GLN GLY GLY ARG LEU ILE LYS HIS GLU MET THR SEQRES 9 A 115 LYS THR ALA SER ALA LEU GLU VAL LEU PHE GLN SEQRES 1 F 545 MET LYS ILE GLU GLU GLY LYS LEU VAL ILE TRP ILE ASN SEQRES 2 F 545 GLY ASP LYS GLY TYR ASN GLY LEU ALA GLU VAL GLY LYS SEQRES 3 F 545 LYS PHE GLU LYS ASP THR GLY ILE LYS VAL THR VAL GLU SEQRES 4 F 545 HIS PRO ASP LYS LEU GLU GLU LYS PHE PRO GLN VAL ALA SEQRES 5 F 545 ALA THR GLY ASP GLY PRO ASP ILE ILE PHE TRP ALA HIS SEQRES 6 F 545 ASP ARG PHE GLY GLY TYR ALA GLN SER GLY LEU LEU ALA SEQRES 7 F 545 GLU ILE THR PRO ASP LYS ALA PHE GLN ASP LYS LEU TYR SEQRES 8 F 545 PRO PHE THR TRP ASP ALA VAL ARG TYR ASN GLY LYS LEU SEQRES 9 F 545 ILE ALA TYR PRO ILE ALA VAL GLU ALA LEU SER LEU ILE SEQRES 10 F 545 TYR ASN LYS ASP LEU LEU PRO ASN PRO PRO LYS THR TRP SEQRES 11 F 545 GLU GLU ILE PRO ALA LEU ASP LYS GLU LEU LYS ALA LYS SEQRES 12 F 545 GLY LYS SER ALA LEU MET PHE ASN LEU GLN GLU PRO TYR SEQRES 13 F 545 PHE THR TRP PRO LEU ILE ALA ALA ASP GLY GLY TYR ALA SEQRES 14 F 545 PHE LYS TYR GLU ASN GLY LYS TYR ASP ILE LYS ASP VAL SEQRES 15 F 545 GLY VAL ASP ASN ALA GLY ALA LYS ALA GLY LEU THR PHE SEQRES 16 F 545 LEU VAL ASP LEU ILE LYS ASN LYS HIS MET ASN ALA ASP SEQRES 17 F 545 THR ASP TYR SER ILE ALA GLU ALA ALA PHE ASN LYS GLY SEQRES 18 F 545 GLU THR ALA MET THR ILE ASN GLY PRO TRP ALA TRP SER SEQRES 19 F 545 ASN ILE ASP THR SER LYS VAL ASN TYR GLY VAL THR VAL SEQRES 20 F 545 LEU PRO THR PHE LYS GLY GLN PRO SER LYS PRO PHE VAL SEQRES 21 F 545 GLY VAL LEU SER ALA GLY ILE ASN ALA ALA SER PRO ASN SEQRES 22 F 545 LYS GLU LEU ALA LYS GLU PHE LEU GLU ASN TYR LEU LEU SEQRES 23 F 545 THR ASP GLU GLY LEU GLU ALA VAL ASN LYS ASP LYS PRO SEQRES 24 F 545 LEU GLY ALA VAL ALA LEU LYS SER TYR GLU GLU GLU LEU SEQRES 25 F 545 ALA LYS ASP PRO ARG ILE ALA ALA THR MET GLU ASN ALA SEQRES 26 F 545 GLN LYS GLY GLU ILE MET PRO ASN ILE PRO GLN MET SER SEQRES 27 F 545 ALA PHE TRP TYR ALA VAL ARG THR ALA VAL ILE ASN ALA SEQRES 28 F 545 ALA SER GLY ARG GLN THR VAL ASP GLN ALA LEU ALA PHE SEQRES 29 F 545 ALA GLN ILE LEU ILE MET PRO ASN LEU THR GLU GLU GLN SEQRES 30 F 545 ARG ASN GLY PHE ILE GLN SER LEU LYS ASP ASP PRO SER SEQRES 31 F 545 VAL SER LYS GLU ILE LEU ALA GLU ALA LYS LYS LEU ASN SEQRES 32 F 545 GLU HIS GLN ALA PRO LYS GLY GLY SER GLY GLY ALA GLY SEQRES 33 F 545 SER GLY ASP GLN GLN SER ALA PHE TYR GLU ILE LEU ASN SEQRES 34 F 545 MET PRO ASN LEU ASN GLU ALA GLN ARG ASN GLY PHE ILE SEQRES 35 F 545 GLN SER LEU LYS ASP ASP PRO SER GLN SER THR ASN VAL SEQRES 36 F 545 LEU GLY GLU ALA LYS LYS LEU ASN GLU SER GLN ALA GLY SEQRES 37 F 545 GLY GLY SER GLY GLY GLY SER GLY GLY SER ALA VAL THR SEQRES 38 F 545 THR TYR LYS LEU VAL ILE ASN GLY LYS THR LEU LYS GLY SEQRES 39 F 545 GLU THR THR THR LYS ALA VAL ASP ALA GLU THR ALA GLU SEQRES 40 F 545 LYS ALA PHE LYS GLN TYR ALA ASN ASP ASN GLY VAL ASP SEQRES 41 F 545 GLY VAL TRP THR TYR ASP ASP ALA THR LYS THR PHE THR SEQRES 42 F 545 VAL THR GLU GLY SER GLY HIS HIS HIS HIS HIS HIS SEQRES 1 E 247 MET VAL LEU GLN THR GLN VAL PHE ILE SER LEU LEU LEU SEQRES 2 E 247 TRP ILE SER GLY ALA TYR GLY ASN ILE MET LEU THR GLN SEQRES 3 E 247 SER PRO SER SER LEU ALA VAL SER ALA GLY GLU ARG VAL SEQRES 4 E 247 THR MET SER CYS LYS SER THR GLN SER ILE LEU TYR ASN SEQRES 5 E 247 SER ASN GLN LYS THR TYR LEU ALA TRP TYR GLN GLN LYS SEQRES 6 E 247 PRO GLY GLN SER PRO LYS LEU LEU ILE TYR TRP ALA SER SEQRES 7 E 247 THR ARG ALA SER GLY VAL PRO ASP ARG PHE THR GLY SER SEQRES 8 E 247 GLY SER GLY THR ASP PHE THR LEU THR ILE ASN SER VAL SEQRES 9 E 247 GLN PRO GLU ASP LEU ALA VAL TYR TYR CYS HIS GLN TYR SEQRES 10 E 247 LEU SER ALA TRP THR PHE GLY GLY GLY THR LYS LEU GLU SEQRES 11 E 247 ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE PHE SEQRES 12 E 247 PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SER SEQRES 13 E 247 VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU ALA SEQRES 14 E 247 LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER GLY SEQRES 15 E 247 ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS ASP SEQRES 16 E 247 SER THR TYR SER LEU SER SER THR LEU THR LEU SER LYS SEQRES 17 E 247 ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU VAL SEQRES 18 E 247 THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER PHE SEQRES 19 E 247 ASN ARG GLY GLU CYS TRP SER HIS PRO GLN PHE GLU LYS HET I2R A 201 22 HETNAM I2R (E)-2-CYANO-3-(1-PHENYLINDOL-3-YL)PROP-2-ENOIC ACID HETSYN I2R UK-5099 FORMUL 7 I2R C18 H12 N2 O2 HELIX 1 AA1 ASN D 74 LYS D 76 5 3 HELIX 2 AA2 LYS C 86 THR C 90 5 5 HELIX 3 AA3 ARG B 7 LEU B 24 1 18 HELIX 4 AA4 PRO B 25 LYS B 27 5 3 HELIX 5 AA5 LEU B 28 ASN B 33 1 6 HELIX 6 AA6 PHE B 43 ASP B 59 1 17 HELIX 7 AA7 PRO B 63 LEU B 67 5 5 HELIX 8 AA8 SER B 68 ILE B 89 1 22 HELIX 9 AA9 ASN B 93 ALA B 125 1 33 HELIX 10 AB1 ALA A 10 SER A 15 1 6 HELIX 11 AB2 LYS A 16 MET A 23 1 8 HELIX 12 AB3 SER A 24 GLY A 29 1 6 HELIX 13 AB4 GLY A 29 TRP A 34 1 6 HELIX 14 AB5 GLY A 35 MET A 44 1 10 HELIX 15 AB6 SER A 52 TYR A 71 1 20 HELIX 16 AB7 ASN A 77 ALA A 107 1 31 HELIX 17 AB8 PHE F 364 MET F 370 1 7 HELIX 18 AB9 THR F 374 ASP F 387 1 14 HELIX 19 AC1 LYS F 393 ASN F 403 1 11 HELIX 20 AC2 GLN F 420 MET F 430 1 11 HELIX 21 AC3 ASN F 434 ASP F 448 1 15 HELIX 22 AC4 GLN F 451 GLU F 464 1 14 SHEET 1 AA1 4 VAL D 5 SER D 7 0 SHEET 2 AA1 4 SER D 17 ALA D 23 -1 O ALA D 23 N VAL D 5 SHEET 3 AA1 4 THR D 78 ASN D 84 -1 O LEU D 79 N CYS D 22 SHEET 4 AA1 4 PHE D 68 ARG D 72 -1 N THR D 69 O GLN D 82 SHEET 1 AA2 6 LEU D 11 VAL D 12 0 SHEET 2 AA2 6 THR D 117 VAL D 121 1 O THR D 120 N VAL D 12 SHEET 3 AA2 6 ALA D 92 ARG D 99 -1 N ALA D 92 O VAL D 119 SHEET 4 AA2 6 GLY D 33 ALA D 40 -1 N VAL D 37 O TYR D 95 SHEET 5 AA2 6 GLY D 44 ILE D 51 -1 O GLU D 46 N ARG D 38 SHEET 6 AA2 6 LYS D 58 TYR D 60 -1 O TYR D 59 N TYR D 50 SHEET 1 AA3 4 GLN C 3 SER C 7 0 SHEET 2 AA3 4 LEU C 18 SER C 25 -1 O SER C 25 N GLN C 3 SHEET 3 AA3 4 THR C 77 MET C 82 -1 O LEU C 80 N LEU C 20 SHEET 4 AA3 4 THR C 68 ASP C 72 -1 N THR C 68 O GLN C 81 SHEET 1 AA4 6 GLY C 10 GLN C 13 0 SHEET 2 AA4 6 GLN C 113 SER C 117 1 O SER C 117 N VAL C 12 SHEET 3 AA4 6 ALA C 91 SER C 99 -1 N ALA C 91 O VAL C 114 SHEET 4 AA4 6 TYR C 31 GLN C 39 -1 N GLY C 32 O LYS C 98 SHEET 5 AA4 6 GLU C 46 ILE C 51 -1 O ILE C 51 N MET C 34 SHEET 6 AA4 6 THR C 57 TYR C 59 -1 O ASN C 58 N SER C 50 SHEET 1 AA5 4 GLY C 10 GLN C 13 0 SHEET 2 AA5 4 GLN C 113 SER C 117 1 O SER C 117 N VAL C 12 SHEET 3 AA5 4 ALA C 91 SER C 99 -1 N ALA C 91 O VAL C 114 SHEET 4 AA5 4 HIS C 105 TYR C 107 -1 O TYR C 107 N VAL C 97 SHEET 1 AA6 4 LEU E 4 GLN E 6 0 SHEET 2 AA6 4 VAL E 19 SER E 25 -1 O LYS E 24 N THR E 5 SHEET 3 AA6 4 ASP E 76 ILE E 81 -1 O PHE E 77 N CYS E 23 SHEET 4 AA6 4 THR E 69 SER E 73 -1 N SER E 71 O THR E 78 SHEET 1 AA7 6 SER E 10 LEU E 11 0 SHEET 2 AA7 6 THR E 107 LEU E 109 1 O LYS E 108 N LEU E 11 SHEET 3 AA7 6 ALA E 90 GLN E 96 -1 N ALA E 90 O LEU E 109 SHEET 4 AA7 6 LEU E 39 GLN E 44 -1 N ALA E 40 O HIS E 95 SHEET 5 AA7 6 LYS E 51 TYR E 55 -1 O LYS E 51 N GLN E 43 SHEET 6 AA7 6 THR E 59 ARG E 60 -1 O THR E 59 N TYR E 55 SSBOND 1 CYS D 22 CYS D 96 1555 1555 2.04 SSBOND 2 CYS C 22 CYS C 95 1555 1555 2.03 SSBOND 3 CYS E 23 CYS E 94 1555 1555 2.04 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