HEADER MEMBRANE PROTEIN 03-JUL-24 9FYR TITLE CRYO-EM STRUCTURE OF NATIVE SV2A IN COMPLEX WITH TENT-HC, PRO- TITLE 2 MACROBODY 5 AND LEVETIRACETAM COMPND MOL_ID: 1; COMPND 2 MOLECULE: SYNAPTIC VESICLE GLYCOPROTEIN 2A; COMPND 3 CHAIN: A; COMPND 4 MOL_ID: 2; COMPND 5 MOLECULE: TETANUS TOXIN HEAVY CHAIN; COMPND 6 CHAIN: C; COMPND 7 SYNONYM: TETANUS TOXIN CHAIN H; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: PRO-MACROBODY 5,MALTOSE/MALTODEXTRIN-BINDING PERIPLASMIC COMPND 11 PROTEIN,MALTOSE/MALTODEXTRIN-BINDING PERIPLASMIC PROTEIN; COMPND 12 CHAIN: D; COMPND 13 SYNONYM: MMBP,MALTODEXTRIN-BINDING PROTEIN,MALTOSE-BINDING PROTEIN, COMPND 14 MBP; COMPND 15 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: OVIS ARIES; SOURCE 3 ORGANISM_COMMON: SHEEP; SOURCE 4 ORGANISM_TAXID: 9940; SOURCE 5 MOL_ID: 2; SOURCE 6 ORGANISM_SCIENTIFIC: CLOSTRIDIUM TETANI E88; SOURCE 7 ORGANISM_TAXID: 212717; SOURCE 8 GENE: TETX, CTC_P60; SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 83333; SOURCE 11 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 12 MOL_ID: 3; SOURCE 13 ORGANISM_SCIENTIFIC: LAMA GLAMA, ESCHERICHIA COLI K-12; SOURCE 14 ORGANISM_TAXID: 9844, 83333; SOURCE 15 GENE: MALE, B4034, JW3994; SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 83333; SOURCE 18 EXPRESSION_SYSTEM_STRAIN: MC1061 KEYWDS SYNAPTIC VESICLES, MFS TRANSPORTER, MEMBRANE PROTEIN, EPILEPSY, KEYWDS 2 LEVETIRACETAM, CLOSTRIDIAL NEUROTOXIN EXPDTA ELECTRON MICROSCOPY AUTHOR S.SCHENCK,J.D.BRUNNER REVDAT 1 21-MAY-25 9FYR 0 JRNL AUTH S.SCHENCK,T.LAEREMANS,J.STEYAERT,J.D.BRUNNER JRNL TITL STRUCTURES OF NATIVE SV2A REVEAL THE BINDING MODE FOR JRNL TITL 2 TETANUS NEUROTOXIN AND ANTI-EPILEPTIC RACETAMS. JRNL REF NAT COMMUN V. 16 4172 2025 JRNL REFN ESSN 2041-1723 JRNL PMID 40325068 JRNL DOI 10.1038/S41467-025-59545-0 REMARK 2 REMARK 2 RESOLUTION. 3.60 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : CRYOSPARC, SERIALEM, CRYOSPARC, REMARK 3 CRYOSPARC, CRYOSPARC, CRYOSPARC, REMARK 3 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 : REAL REMARK 3 REFINEMENT PROTOCOL : AB INITIO MODEL 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) : 3.600 REMARK 3 NUMBER OF PARTICLES : 158703 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 9FYR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-JUL-24. REMARK 100 THE DEPOSITION ID IS D_1292139800. 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 : SV2A BOUND TO TENT-HC, PRO REMARK 245 -MACROBODY 5 AND LEVETIRACETAM; REMARK 245 SYNAPTIC VESICLE GLYCOPROTEIN REMARK 245 2A; TENT-HC; PRO-MACROBODY 5 REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 7.00 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 : 17809 REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : JEOL CRYO ARM 300 REMARK 245 DETECTOR TYPE : GATAN K3 (6K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 800.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2500.00 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 : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : 60000 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: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, D, Z, Y 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 GLU A 2 REMARK 465 GLU A 3 REMARK 465 GLY A 4 REMARK 465 PHE A 5 REMARK 465 ARG A 6 REMARK 465 ASP A 7 REMARK 465 ARG A 8 REMARK 465 ALA A 9 REMARK 465 ALA A 10 REMARK 465 PHE A 11 REMARK 465 ILE A 12 REMARK 465 ARG A 13 REMARK 465 GLY A 14 REMARK 465 ALA A 15 REMARK 465 LYS A 16 REMARK 465 ASP A 17 REMARK 465 ILE A 18 REMARK 465 ALA A 19 REMARK 465 LYS A 20 REMARK 465 GLU A 21 REMARK 465 VAL A 22 REMARK 465 LYS A 23 REMARK 465 LYS A 24 REMARK 465 HIS A 25 REMARK 465 ALA A 26 REMARK 465 ALA A 27 REMARK 465 LYS A 28 REMARK 465 LYS A 29 REMARK 465 VAL A 30 REMARK 465 VAL A 31 REMARK 465 LYS A 32 REMARK 465 GLY A 33 REMARK 465 LEU A 34 REMARK 465 ASP A 35 REMARK 465 ARG A 36 REMARK 465 VAL A 37 REMARK 465 GLN A 38 REMARK 465 ASP A 39 REMARK 465 GLU A 40 REMARK 465 TYR A 41 REMARK 465 SER A 42 REMARK 465 ARG A 43 REMARK 465 ARG A 44 REMARK 465 SER A 45 REMARK 465 TYR A 46 REMARK 465 SER A 47 REMARK 465 ARG A 48 REMARK 465 PHE A 49 REMARK 465 GLU A 50 REMARK 465 GLU A 51 REMARK 465 GLU A 52 REMARK 465 ASP A 53 REMARK 465 ASP A 54 REMARK 465 ASP A 55 REMARK 465 ASP A 56 REMARK 465 ASP A 57 REMARK 465 PHE A 58 REMARK 465 PRO A 59 REMARK 465 ALA A 60 REMARK 465 PRO A 61 REMARK 465 ALA A 62 REMARK 465 ASP A 63 REMARK 465 GLY A 64 REMARK 465 TYR A 65 REMARK 465 TYR A 66 REMARK 465 ARG A 67 REMARK 465 GLY A 68 REMARK 465 GLU A 69 REMARK 465 GLY A 70 REMARK 465 ALA A 71 REMARK 465 GLN A 72 REMARK 465 ASP A 73 REMARK 465 GLU A 74 REMARK 465 GLU A 75 REMARK 465 GLU A 76 REMARK 465 GLY A 77 REMARK 465 GLY A 78 REMARK 465 ALA A 79 REMARK 465 SER A 80 REMARK 465 SER A 81 REMARK 465 ASP A 82 REMARK 465 ALA A 83 REMARK 465 THR A 84 REMARK 465 GLU A 85 REMARK 465 GLY A 86 REMARK 465 HIS A 87 REMARK 465 ASP A 88 REMARK 465 GLU A 89 REMARK 465 ASP A 90 REMARK 465 ASP A 91 REMARK 465 GLU A 92 REMARK 465 ILE A 93 REMARK 465 TYR A 94 REMARK 465 GLU A 95 REMARK 465 GLY A 96 REMARK 465 GLU A 97 REMARK 465 TYR A 98 REMARK 465 GLN A 99 REMARK 465 GLY A 100 REMARK 465 ILE A 101 REMARK 465 PRO A 102 REMARK 465 ARG A 103 REMARK 465 ALA A 104 REMARK 465 GLU A 105 REMARK 465 SER A 106 REMARK 465 GLY A 107 REMARK 465 GLY A 108 REMARK 465 LYS A 109 REMARK 465 GLY A 110 REMARK 465 GLU A 111 REMARK 465 ARG A 112 REMARK 465 MET A 113 REMARK 465 ALA A 114 REMARK 465 ASP A 115 REMARK 465 GLY A 116 REMARK 465 ALA A 117 REMARK 465 PRO A 118 REMARK 465 LEU A 119 REMARK 465 ALA A 120 REMARK 465 GLY A 121 REMARK 465 VAL A 122 REMARK 465 ARG A 123 REMARK 465 GLY A 124 REMARK 465 GLY A 125 REMARK 465 LEU A 126 REMARK 465 GLY A 127 REMARK 465 ASP A 128 REMARK 465 GLY A 129 REMARK 465 GLU A 130 REMARK 465 GLY A 131 REMARK 465 PRO A 132 REMARK 465 PRO A 133 REMARK 465 GLY A 134 REMARK 465 GLY A 135 REMARK 465 ARG A 136 REMARK 465 GLY A 137 REMARK 465 GLU A 138 REMARK 465 ALA A 139 REMARK 465 GLN A 140 REMARK 465 ARG A 141 REMARK 465 ARG A 142 REMARK 465 LYS A 143 REMARK 465 GLU A 144 REMARK 465 PHE A 322 REMARK 465 GLN A 323 REMARK 465 MET A 324 REMARK 465 GLY A 325 REMARK 465 SER A 326 REMARK 465 ALA A 327 REMARK 465 TYR A 328 REMARK 465 GLN A 329 REMARK 465 HIS A 401 REMARK 465 GLN A 402 REMARK 465 GLU A 403 REMARK 465 ASP A 404 REMARK 465 GLU A 405 REMARK 465 LEU A 406 REMARK 465 ILE A 407 REMARK 465 GLU A 408 REMARK 465 ILE A 409 REMARK 465 GLN A 410 REMARK 465 SER A 411 REMARK 465 ASP A 412 REMARK 465 THR A 413 REMARK 465 GLY A 414 REMARK 465 ALA A 415 REMARK 465 TRP A 416 REMARK 465 TYR A 417 REMARK 465 GLN A 418 REMARK 465 ARG A 419 REMARK 465 TRP A 420 REMARK 465 GLY A 589 REMARK 465 THR A 590 REMARK 465 GLY A 591 REMARK 465 GLU A 592 REMARK 465 GLY A 593 REMARK 465 ALA A 594 REMARK 465 MET C 847 REMARK 465 GLY C 848 REMARK 465 LYS C 849 REMARK 465 HIS C 850 REMARK 465 HIS C 851 REMARK 465 HIS C 852 REMARK 465 HIS C 853 REMARK 465 HIS C 854 REMARK 465 HIS C 855 REMARK 465 HIS C 856 REMARK 465 HIS C 857 REMARK 465 HIS C 858 REMARK 465 HIS C 859 REMARK 465 GLY C 860 REMARK 465 SER C 861 REMARK 465 ALA C 862 REMARK 465 SER C 863 REMARK 465 LEU C 864 REMARK 465 GLU C 865 REMARK 465 VAL C 866 REMARK 465 LEU C 867 REMARK 465 PHE C 868 REMARK 465 GLN C 869 REMARK 465 GLY C 870 REMARK 465 PRO C 871 REMARK 465 SER C 872 REMARK 465 HIS C 873 REMARK 465 MET C 874 REMARK 465 GLU C 875 REMARK 465 ASP C 876 REMARK 465 ILE C 877 REMARK 465 ASP C 878 REMARK 465 VAL C 879 REMARK 465 ILE C 880 REMARK 465 LEU C 881 REMARK 465 LYS C 882 REMARK 465 LYS C 883 REMARK 465 SER C 884 REMARK 465 THR C 885 REMARK 465 ILE C 886 REMARK 465 LEU C 887 REMARK 465 ASN C 888 REMARK 465 LEU C 889 REMARK 465 ASP C 890 REMARK 465 ILE C 891 REMARK 465 ASN C 892 REMARK 465 ASN C 893 REMARK 465 ASP C 894 REMARK 465 ILE C 895 REMARK 465 ILE C 896 REMARK 465 SER C 897 REMARK 465 ASP C 898 REMARK 465 ILE C 899 REMARK 465 SER C 900 REMARK 465 GLY C 901 REMARK 465 PHE C 902 REMARK 465 ASN C 903 REMARK 465 SER C 904 REMARK 465 SER C 905 REMARK 465 VAL C 906 REMARK 465 ILE C 907 REMARK 465 THR C 908 REMARK 465 TYR C 909 REMARK 465 PRO C 910 REMARK 465 ASP C 911 REMARK 465 ALA C 912 REMARK 465 GLN C 913 REMARK 465 LEU C 914 REMARK 465 VAL C 915 REMARK 465 PRO C 916 REMARK 465 GLY C 917 REMARK 465 ILE C 918 REMARK 465 ASN C 919 REMARK 465 GLY C 920 REMARK 465 LYS C 921 REMARK 465 ALA C 922 REMARK 465 ILE C 923 REMARK 465 HIS C 924 REMARK 465 LYS C 937 REMARK 465 ALA C 938 REMARK 465 MET C 939 REMARK 465 ASP C 940 REMARK 465 ILE C 941 REMARK 465 GLU C 942 REMARK 465 TYR C 943 REMARK 465 ASN C 944 REMARK 465 ASP C 945 REMARK 465 MET C 946 REMARK 465 PHE C 947 REMARK 465 ASN C 948 REMARK 465 ASN C 949 REMARK 465 MET C 980 REMARK 465 LYS C 981 REMARK 465 LYS C 982 REMARK 465 HIS C 983 REMARK 465 SER C 984 REMARK 465 LEU C 985 REMARK 465 SER C 986 REMARK 465 ILE C 987 REMARK 465 GLY C 988 REMARK 465 SER C 989 REMARK 465 GLY C 990 REMARK 465 LYS C 1005 REMARK 465 ASP C 1006 REMARK 465 SER C 1007 REMARK 465 ALA C 1008 REMARK 465 GLY C 1009 REMARK 465 GLU C 1010 REMARK 465 VAL C 1011 REMARK 465 GLY C 1062 REMARK 465 ALA C 1063 REMARK 465 ILE C 1064 REMARK 465 ARG C 1065 REMARK 465 GLU C 1066 REMARK 465 ASP C 1067 REMARK 465 ASN C 1068 REMARK 465 ASN C 1069 REMARK 465 PRO C 1182 REMARK 465 ASN C 1183 REMARK 465 ASN C 1184 REMARK 465 GLU C 1185 REMARK 465 ILE C 1186 REMARK 465 ASP C 1187 REMARK 465 GLY D 1 REMARK 465 PRO D 2 REMARK 465 SER D 3 REMARK 465 VAL D 125 REMARK 465 PRO D 126 REMARK 465 PRO D 127 REMARK 465 LEU D 128 REMARK 465 VAL D 129 REMARK 465 ILE D 130 REMARK 465 TRP D 131 REMARK 465 ILE D 132 REMARK 465 ASN D 133 REMARK 465 GLY D 134 REMARK 465 ASP D 135 REMARK 465 LYS D 136 REMARK 465 GLY D 137 REMARK 465 TYR D 138 REMARK 465 ASN D 139 REMARK 465 GLY D 140 REMARK 465 LEU D 141 REMARK 465 ALA D 142 REMARK 465 GLU D 143 REMARK 465 VAL D 144 REMARK 465 GLY D 145 REMARK 465 LYS D 146 REMARK 465 LYS D 147 REMARK 465 PHE D 148 REMARK 465 GLU D 149 REMARK 465 LYS D 150 REMARK 465 ASP D 151 REMARK 465 THR D 152 REMARK 465 GLY D 153 REMARK 465 ILE D 154 REMARK 465 LYS D 155 REMARK 465 VAL D 156 REMARK 465 THR D 157 REMARK 465 VAL D 158 REMARK 465 GLU D 159 REMARK 465 HIS D 160 REMARK 465 PRO D 161 REMARK 465 ASP D 162 REMARK 465 LYS D 163 REMARK 465 LEU D 164 REMARK 465 GLU D 165 REMARK 465 GLU D 166 REMARK 465 LYS D 167 REMARK 465 PHE D 168 REMARK 465 PRO D 169 REMARK 465 GLN D 170 REMARK 465 VAL D 171 REMARK 465 ALA D 172 REMARK 465 ALA D 173 REMARK 465 THR D 174 REMARK 465 GLY D 175 REMARK 465 ASP D 176 REMARK 465 GLY D 177 REMARK 465 PRO D 178 REMARK 465 ASP D 179 REMARK 465 ILE D 180 REMARK 465 ILE D 181 REMARK 465 PHE D 182 REMARK 465 TRP D 183 REMARK 465 ALA D 184 REMARK 465 HIS D 185 REMARK 465 ASP D 186 REMARK 465 ARG D 187 REMARK 465 PHE D 188 REMARK 465 GLY D 189 REMARK 465 GLY D 190 REMARK 465 TYR D 191 REMARK 465 ALA D 192 REMARK 465 GLN D 193 REMARK 465 SER D 194 REMARK 465 GLY D 195 REMARK 465 LEU D 196 REMARK 465 LEU D 197 REMARK 465 ALA D 198 REMARK 465 GLU D 199 REMARK 465 ILE D 200 REMARK 465 THR D 201 REMARK 465 PRO D 202 REMARK 465 ASP D 203 REMARK 465 LYS D 204 REMARK 465 ALA D 205 REMARK 465 PHE D 206 REMARK 465 GLN D 207 REMARK 465 ASP D 208 REMARK 465 LYS D 209 REMARK 465 LEU D 210 REMARK 465 TYR D 211 REMARK 465 PRO D 212 REMARK 465 PHE D 213 REMARK 465 THR D 214 REMARK 465 TRP D 215 REMARK 465 ASP D 216 REMARK 465 ALA D 217 REMARK 465 VAL D 218 REMARK 465 ARG D 219 REMARK 465 TYR D 220 REMARK 465 ASN D 221 REMARK 465 GLY D 222 REMARK 465 LYS D 223 REMARK 465 LEU D 224 REMARK 465 ILE D 225 REMARK 465 ALA D 226 REMARK 465 TYR D 227 REMARK 465 PRO D 228 REMARK 465 ILE D 229 REMARK 465 ALA D 230 REMARK 465 VAL D 231 REMARK 465 GLU D 232 REMARK 465 ALA D 233 REMARK 465 LEU D 234 REMARK 465 SER D 235 REMARK 465 LEU D 236 REMARK 465 ILE D 237 REMARK 465 TYR D 238 REMARK 465 ASN D 239 REMARK 465 LYS D 240 REMARK 465 ASP D 241 REMARK 465 LEU D 242 REMARK 465 LEU D 243 REMARK 465 PRO D 244 REMARK 465 ASN D 245 REMARK 465 PRO D 246 REMARK 465 PRO D 247 REMARK 465 LYS D 248 REMARK 465 THR D 249 REMARK 465 TRP D 250 REMARK 465 GLU D 251 REMARK 465 GLU D 252 REMARK 465 ILE D 253 REMARK 465 PRO D 254 REMARK 465 ALA D 255 REMARK 465 LEU D 256 REMARK 465 ASP D 257 REMARK 465 LYS D 258 REMARK 465 GLU D 259 REMARK 465 LEU D 260 REMARK 465 LYS D 261 REMARK 465 ALA D 262 REMARK 465 LYS D 263 REMARK 465 GLY D 264 REMARK 465 LYS D 265 REMARK 465 SER D 266 REMARK 465 ALA D 267 REMARK 465 LEU D 268 REMARK 465 MET D 269 REMARK 465 PHE D 270 REMARK 465 ASN D 271 REMARK 465 LEU D 272 REMARK 465 GLN D 273 REMARK 465 GLU D 274 REMARK 465 PRO D 275 REMARK 465 TYR D 276 REMARK 465 PHE D 277 REMARK 465 THR D 278 REMARK 465 TRP D 279 REMARK 465 PRO D 280 REMARK 465 LEU D 281 REMARK 465 ILE D 282 REMARK 465 ALA D 283 REMARK 465 ALA D 284 REMARK 465 ASP D 285 REMARK 465 GLY D 286 REMARK 465 GLY D 287 REMARK 465 TYR D 288 REMARK 465 ALA D 289 REMARK 465 PHE D 290 REMARK 465 LYS D 291 REMARK 465 TYR D 292 REMARK 465 GLU D 293 REMARK 465 ASN D 294 REMARK 465 GLY D 295 REMARK 465 LYS D 296 REMARK 465 TYR D 297 REMARK 465 ASP D 298 REMARK 465 ILE D 299 REMARK 465 LYS D 300 REMARK 465 ASP D 301 REMARK 465 VAL D 302 REMARK 465 GLY D 303 REMARK 465 VAL D 304 REMARK 465 ASP D 305 REMARK 465 ASN D 306 REMARK 465 ALA D 307 REMARK 465 GLY D 308 REMARK 465 ALA D 309 REMARK 465 LYS D 310 REMARK 465 ALA D 311 REMARK 465 GLY D 312 REMARK 465 LEU D 313 REMARK 465 THR D 314 REMARK 465 PHE D 315 REMARK 465 LEU D 316 REMARK 465 VAL D 317 REMARK 465 ASP D 318 REMARK 465 LEU D 319 REMARK 465 ILE D 320 REMARK 465 LYS D 321 REMARK 465 ASN D 322 REMARK 465 LYS D 323 REMARK 465 HIS D 324 REMARK 465 MET D 325 REMARK 465 ASN D 326 REMARK 465 ALA D 327 REMARK 465 ASP D 328 REMARK 465 THR D 329 REMARK 465 ASP D 330 REMARK 465 TYR D 331 REMARK 465 SER D 332 REMARK 465 ILE D 333 REMARK 465 ALA D 334 REMARK 465 GLU D 335 REMARK 465 ALA D 336 REMARK 465 ALA D 337 REMARK 465 PHE D 338 REMARK 465 ASN D 339 REMARK 465 LYS D 340 REMARK 465 GLY D 341 REMARK 465 GLU D 342 REMARK 465 THR D 343 REMARK 465 ALA D 344 REMARK 465 MET D 345 REMARK 465 THR D 346 REMARK 465 ILE D 347 REMARK 465 ASN D 348 REMARK 465 GLY D 349 REMARK 465 PRO D 350 REMARK 465 TRP D 351 REMARK 465 ALA D 352 REMARK 465 TRP D 353 REMARK 465 SER D 354 REMARK 465 ASN D 355 REMARK 465 ILE D 356 REMARK 465 ASP D 357 REMARK 465 THR D 358 REMARK 465 SER D 359 REMARK 465 LYS D 360 REMARK 465 VAL D 361 REMARK 465 ASN D 362 REMARK 465 TYR D 363 REMARK 465 GLY D 364 REMARK 465 VAL D 365 REMARK 465 THR D 366 REMARK 465 VAL D 367 REMARK 465 LEU D 368 REMARK 465 PRO D 369 REMARK 465 THR D 370 REMARK 465 PHE D 371 REMARK 465 LYS D 372 REMARK 465 GLY D 373 REMARK 465 GLN D 374 REMARK 465 PRO D 375 REMARK 465 SER D 376 REMARK 465 LYS D 377 REMARK 465 PRO D 378 REMARK 465 PHE D 379 REMARK 465 VAL D 380 REMARK 465 GLY D 381 REMARK 465 VAL D 382 REMARK 465 LEU D 383 REMARK 465 SER D 384 REMARK 465 ALA D 385 REMARK 465 GLY D 386 REMARK 465 ILE D 387 REMARK 465 ASN D 388 REMARK 465 ALA D 389 REMARK 465 ALA D 390 REMARK 465 SER D 391 REMARK 465 PRO D 392 REMARK 465 ASN D 393 REMARK 465 LYS D 394 REMARK 465 GLU D 395 REMARK 465 LEU D 396 REMARK 465 ALA D 397 REMARK 465 LYS D 398 REMARK 465 GLU D 399 REMARK 465 PHE D 400 REMARK 465 LEU D 401 REMARK 465 GLU D 402 REMARK 465 ASN D 403 REMARK 465 TYR D 404 REMARK 465 LEU D 405 REMARK 465 LEU D 406 REMARK 465 THR D 407 REMARK 465 ASP D 408 REMARK 465 GLU D 409 REMARK 465 GLY D 410 REMARK 465 LEU D 411 REMARK 465 GLU D 412 REMARK 465 ALA D 413 REMARK 465 VAL D 414 REMARK 465 ASN D 415 REMARK 465 LYS D 416 REMARK 465 ASP D 417 REMARK 465 LYS D 418 REMARK 465 PRO D 419 REMARK 465 LEU D 420 REMARK 465 GLY D 421 REMARK 465 ALA D 422 REMARK 465 VAL D 423 REMARK 465 ALA D 424 REMARK 465 LEU D 425 REMARK 465 LYS D 426 REMARK 465 SER D 427 REMARK 465 TYR D 428 REMARK 465 GLU D 429 REMARK 465 GLU D 430 REMARK 465 GLU D 431 REMARK 465 LEU D 432 REMARK 465 ALA D 433 REMARK 465 LYS D 434 REMARK 465 ASP D 435 REMARK 465 PRO D 436 REMARK 465 ARG D 437 REMARK 465 ILE D 438 REMARK 465 ALA D 439 REMARK 465 ALA D 440 REMARK 465 THR D 441 REMARK 465 MET D 442 REMARK 465 GLU D 443 REMARK 465 ASN D 444 REMARK 465 ALA D 445 REMARK 465 GLN D 446 REMARK 465 LYS D 447 REMARK 465 GLY D 448 REMARK 465 GLU D 449 REMARK 465 ILE D 450 REMARK 465 MET D 451 REMARK 465 PRO D 452 REMARK 465 ASN D 453 REMARK 465 ILE D 454 REMARK 465 PRO D 455 REMARK 465 GLN D 456 REMARK 465 MET D 457 REMARK 465 SER D 458 REMARK 465 ALA D 459 REMARK 465 PHE D 460 REMARK 465 TRP D 461 REMARK 465 TYR D 462 REMARK 465 ALA D 463 REMARK 465 VAL D 464 REMARK 465 ARG D 465 REMARK 465 THR D 466 REMARK 465 ALA D 467 REMARK 465 VAL D 468 REMARK 465 ILE D 469 REMARK 465 ASN D 470 REMARK 465 ALA D 471 REMARK 465 ALA D 472 REMARK 465 SER D 473 REMARK 465 GLY D 474 REMARK 465 ARG D 475 REMARK 465 GLN D 476 REMARK 465 THR D 477 REMARK 465 VAL D 478 REMARK 465 ASP D 479 REMARK 465 GLU D 480 REMARK 465 ALA D 481 REMARK 465 LEU D 482 REMARK 465 LYS D 483 REMARK 465 ASP D 484 REMARK 465 ALA D 485 REMARK 465 GLN D 486 REMARK 465 THR D 487 REMARK 465 PRO D 488 REMARK 465 GLY D 489 REMARK 465 ALA D 490 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 ASN A 498 28.36 -142.18 REMARK 500 TYR A 535 116.45 -162.18 REMARK 500 TYR C 969 53.18 -90.41 REMARK 500 ASN C 998 33.97 -98.82 REMARK 500 ALA C1028 -168.67 -79.91 REMARK 500 SER C1043 -174.82 -173.98 REMARK 500 PHE C1113 145.37 -172.32 REMARK 500 TYR C1166 -178.30 -173.18 REMARK 500 ASP C1214 49.32 39.88 REMARK 500 ASN C1220 -4.57 75.00 REMARK 500 ALA D 95 -178.51 -172.94 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-50889 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF NATIVE SV2A IN COMPLEX WITH TENT-HC AND PRO- REMARK 900 MACROBODY 5 REMARK 900 RELATED ID: 9FYQ RELATED DB: PDB REMARK 900 CRYO-EM STRUCTURE OF NATIVE SV2A IN COMPLEX WITH TENT-HC AND PRO- REMARK 900 MACROBODY 5 REMARK 900 RELATED ID: EMD-50890 RELATED DB: EMDB REMARK 900 FOCUSED REFINEMENT ON TENT AND GANGLIOSIDES REMARK 900 RELATED ID: EMD-50891 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF NATIVE SV2A IN COMPLEX WITH TENT-HC, PRO- REMARK 900 MACROBODY 5 AND LEVETIRACETAM DBREF1 9FYR A 1 742 UNP A0A836APF1_SHEEP DBREF2 9FYR A A0A836APF1 1 742 DBREF 9FYR C 875 1315 UNP P04958 TETX_CLOTE 875 1315 DBREF 9FYR D 1 127 PDB 9FYR 9FYR 1 127 DBREF 9FYR D 128 487 UNP P0AEX9 MALE_ECOLI 33 392 SEQADV 9FYR MET C 847 UNP P04958 INITIATING METHIONINE SEQADV 9FYR GLY C 848 UNP P04958 EXPRESSION TAG SEQADV 9FYR LYS C 849 UNP P04958 EXPRESSION TAG SEQADV 9FYR HIS C 850 UNP P04958 EXPRESSION TAG SEQADV 9FYR HIS C 851 UNP P04958 EXPRESSION TAG SEQADV 9FYR HIS C 852 UNP P04958 EXPRESSION TAG SEQADV 9FYR HIS C 853 UNP P04958 EXPRESSION TAG SEQADV 9FYR HIS C 854 UNP P04958 EXPRESSION TAG SEQADV 9FYR HIS C 855 UNP P04958 EXPRESSION TAG SEQADV 9FYR HIS C 856 UNP P04958 EXPRESSION TAG SEQADV 9FYR HIS C 857 UNP P04958 EXPRESSION TAG SEQADV 9FYR HIS C 858 UNP P04958 EXPRESSION TAG SEQADV 9FYR HIS C 859 UNP P04958 EXPRESSION TAG SEQADV 9FYR GLY C 860 UNP P04958 EXPRESSION TAG SEQADV 9FYR SER C 861 UNP P04958 EXPRESSION TAG SEQADV 9FYR ALA C 862 UNP P04958 EXPRESSION TAG SEQADV 9FYR SER C 863 UNP P04958 EXPRESSION TAG SEQADV 9FYR LEU C 864 UNP P04958 EXPRESSION TAG SEQADV 9FYR GLU C 865 UNP P04958 EXPRESSION TAG SEQADV 9FYR VAL C 866 UNP P04958 EXPRESSION TAG SEQADV 9FYR LEU C 867 UNP P04958 EXPRESSION TAG SEQADV 9FYR PHE C 868 UNP P04958 EXPRESSION TAG SEQADV 9FYR GLN C 869 UNP P04958 EXPRESSION TAG SEQADV 9FYR GLY C 870 UNP P04958 EXPRESSION TAG SEQADV 9FYR PRO C 871 UNP P04958 EXPRESSION TAG SEQADV 9FYR SER C 872 UNP P04958 EXPRESSION TAG SEQADV 9FYR HIS C 873 UNP P04958 EXPRESSION TAG SEQADV 9FYR MET C 874 UNP P04958 EXPRESSION TAG SEQADV 9FYR PRO D 488 UNP P0AEX9 EXPRESSION TAG SEQADV 9FYR GLY D 489 UNP P0AEX9 EXPRESSION TAG SEQADV 9FYR ALA D 490 UNP P0AEX9 EXPRESSION TAG SEQRES 1 A 742 MET GLU GLU GLY PHE ARG ASP ARG ALA ALA PHE ILE ARG SEQRES 2 A 742 GLY ALA LYS ASP ILE ALA LYS GLU VAL LYS LYS HIS ALA SEQRES 3 A 742 ALA LYS LYS VAL VAL LYS GLY LEU ASP ARG VAL GLN ASP SEQRES 4 A 742 GLU TYR SER ARG ARG SER TYR SER ARG PHE GLU GLU GLU SEQRES 5 A 742 ASP ASP ASP ASP ASP PHE PRO ALA PRO ALA ASP GLY TYR SEQRES 6 A 742 TYR ARG GLY GLU GLY ALA GLN ASP GLU GLU GLU GLY GLY SEQRES 7 A 742 ALA SER SER ASP ALA THR GLU GLY HIS ASP GLU ASP ASP SEQRES 8 A 742 GLU ILE TYR GLU GLY GLU TYR GLN GLY ILE PRO ARG ALA SEQRES 9 A 742 GLU SER GLY GLY LYS GLY GLU ARG MET ALA ASP GLY ALA SEQRES 10 A 742 PRO LEU ALA GLY VAL ARG GLY GLY LEU GLY ASP GLY GLU SEQRES 11 A 742 GLY PRO PRO GLY GLY ARG GLY GLU ALA GLN ARG ARG LYS SEQRES 12 A 742 GLU ARG GLU GLU LEU ALA GLN GLN TYR GLU ALA ILE LEU SEQRES 13 A 742 ARG GLU CYS GLY HIS GLY ARG PHE GLN TRP THR LEU TYR SEQRES 14 A 742 PHE VAL LEU GLY LEU ALA LEU MET ALA ASP GLY VAL GLU SEQRES 15 A 742 VAL PHE VAL VAL GLY PHE VAL LEU PRO SER ALA GLU LYS SEQRES 16 A 742 ASP MET CYS LEU SER ASP SER ASN LYS GLY MET LEU GLY SEQRES 17 A 742 LEU ILE VAL TYR LEU GLY MET MET VAL GLY ALA PHE LEU SEQRES 18 A 742 TRP GLY GLY LEU ALA ASP ARG LEU GLY ARG ARG GLN CYS SEQRES 19 A 742 LEU LEU ILE SER LEU SER VAL ASN SER VAL PHE ALA PHE SEQRES 20 A 742 PHE SER SER PHE VAL GLN GLY TYR GLY THR PHE LEU PHE SEQRES 21 A 742 CYS ARG LEU LEU SER GLY VAL GLY ILE GLY GLY SER ILE SEQRES 22 A 742 PRO ILE VAL PHE SER TYR PHE SER GLU PHE LEU ALA GLN SEQRES 23 A 742 GLU LYS ARG GLY GLU HIS LEU SER TRP LEU CYS MET PHE SEQRES 24 A 742 TRP MET ILE GLY GLY VAL TYR ALA ALA ALA MET ALA TRP SEQRES 25 A 742 ALA ILE ILE PRO HIS TYR GLY TRP SER PHE GLN MET GLY SEQRES 26 A 742 SER ALA TYR GLN PHE HIS SER TRP ARG VAL PHE VAL LEU SEQRES 27 A 742 VAL CYS ALA PHE PRO SER VAL PHE ALA ILE GLY ALA LEU SEQRES 28 A 742 THR THR GLN PRO GLU SER PRO ARG PHE PHE LEU GLU ASN SEQRES 29 A 742 GLY LYS HIS ASP GLU ALA TRP MET VAL LEU LYS GLN VAL SEQRES 30 A 742 HIS ASP THR ASN MET ARG ALA LYS GLY HIS PRO GLU ARG SEQRES 31 A 742 VAL PHE SER VAL THR HIS ILE LYS THR ILE HIS GLN GLU SEQRES 32 A 742 ASP GLU LEU ILE GLU ILE GLN SER ASP THR GLY ALA TRP SEQRES 33 A 742 TYR GLN ARG TRP GLY VAL ARG ALA LEU SER LEU GLY GLY SEQRES 34 A 742 GLN VAL TRP GLY ASN PHE LEU SER CYS PHE GLY PRO GLU SEQRES 35 A 742 TYR ARG ARG ILE THR LEU MET MET MET GLY VAL TRP PHE SEQRES 36 A 742 THR MET SER PHE SER TYR TYR GLY LEU THR VAL TRP PHE SEQRES 37 A 742 PRO ASP MET ILE ARG HIS LEU GLN ALA VAL ASP TYR ALA SEQRES 38 A 742 ALA ARG THR LYS VAL PHE PRO GLY GLU ARG VAL GLU HIS SEQRES 39 A 742 VAL THR PHE ASN PHE THR LEU GLU ASN GLN ILE HIS ARG SEQRES 40 A 742 GLY GLY GLN TYR PHE ASN ASP LYS PHE ILE GLY LEU ARG SEQRES 41 A 742 LEU LYS SER VAL SER PHE GLU ASP SER LEU PHE GLU GLU SEQRES 42 A 742 CYS TYR PHE GLU ASP VAL THR SER SER ASN THR PHE PHE SEQRES 43 A 742 ARG ASN CYS THR PHE ILE ASN THR VAL PHE TYR ASN THR SEQRES 44 A 742 ASP LEU PHE GLU TYR LYS PHE VAL ASN SER ARG LEU VAL SEQRES 45 A 742 ASN SER THR PHE LEU HIS ASN LYS GLU GLY CYS PRO LEU SEQRES 46 A 742 ASP VAL THR GLY THR GLY GLU GLY ALA TYR MET VAL TYR SEQRES 47 A 742 PHE VAL SER PHE LEU GLY THR LEU ALA VAL LEU PRO GLY SEQRES 48 A 742 ASN ILE VAL SER ALA LEU LEU MET ASP LYS ILE GLY ARG SEQRES 49 A 742 LEU ARG MET LEU ALA GLY SER SER VAL MET SER CYS VAL SEQRES 50 A 742 SER CYS PHE PHE LEU SER PHE GLY ASN SER GLU SER ALA SEQRES 51 A 742 MET ILE ALA LEU LEU CYS LEU PHE GLY GLY VAL SER ILE SEQRES 52 A 742 ALA SER TRP ASN ALA LEU ASP VAL LEU THR VAL GLU LEU SEQRES 53 A 742 TYR PRO SER ASP LYS ARG THR THR ALA PHE GLY PHE LEU SEQRES 54 A 742 ASN ALA LEU CYS LYS LEU ALA ALA VAL LEU GLY ILE SER SEQRES 55 A 742 ILE PHE THR SER PHE VAL GLY ILE THR LYS ALA ALA PRO SEQRES 56 A 742 ILE LEU PHE ALA SER ALA ALA LEU ALA LEU GLY SER SER SEQRES 57 A 742 LEU ALA LEU LYS LEU PRO GLU THR ARG GLY GLN VAL LEU SEQRES 58 A 742 GLN SEQRES 1 C 469 MET GLY LYS HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS SEQRES 2 C 469 GLY SER ALA SER LEU GLU VAL LEU PHE GLN GLY PRO SER SEQRES 3 C 469 HIS MET GLU ASP ILE ASP VAL ILE LEU LYS LYS SER THR SEQRES 4 C 469 ILE LEU ASN LEU ASP ILE ASN ASN ASP ILE ILE SER ASP SEQRES 5 C 469 ILE SER GLY PHE ASN SER SER VAL ILE THR TYR PRO ASP SEQRES 6 C 469 ALA GLN LEU VAL PRO GLY ILE ASN GLY LYS ALA ILE HIS SEQRES 7 C 469 LEU VAL ASN ASN GLU SER SER GLU VAL ILE VAL HIS LYS SEQRES 8 C 469 ALA MET ASP ILE GLU TYR ASN ASP MET PHE ASN ASN PHE SEQRES 9 C 469 THR VAL SER PHE TRP LEU ARG VAL PRO LYS VAL SER ALA SEQRES 10 C 469 SER HIS LEU GLU GLN TYR GLY THR ASN GLU TYR SER ILE SEQRES 11 C 469 ILE SER SER MET LYS LYS HIS SER LEU SER ILE GLY SER SEQRES 12 C 469 GLY TRP SER VAL SER LEU LYS GLY ASN ASN LEU ILE TRP SEQRES 13 C 469 THR LEU LYS ASP SER ALA GLY GLU VAL ARG GLN ILE THR SEQRES 14 C 469 PHE ARG ASP LEU PRO ASP LYS PHE ASN ALA TYR LEU ALA SEQRES 15 C 469 ASN LYS TRP VAL PHE ILE THR ILE THR ASN ASP ARG LEU SEQRES 16 C 469 SER SER ALA ASN LEU TYR ILE ASN GLY VAL LEU MET GLY SEQRES 17 C 469 SER ALA GLU ILE THR GLY LEU GLY ALA ILE ARG GLU ASP SEQRES 18 C 469 ASN ASN ILE THR LEU LYS LEU ASP ARG CYS ASN ASN ASN SEQRES 19 C 469 ASN GLN TYR VAL SER ILE ASP LYS PHE ARG ILE PHE CYS SEQRES 20 C 469 LYS ALA LEU ASN PRO LYS GLU ILE GLU LYS LEU TYR THR SEQRES 21 C 469 SER TYR LEU SER ILE THR PHE LEU ARG ASP PHE TRP GLY SEQRES 22 C 469 ASN PRO LEU ARG TYR ASP THR GLU TYR TYR LEU ILE PRO SEQRES 23 C 469 VAL ALA SER SER SER LYS ASP VAL GLN LEU LYS ASN ILE SEQRES 24 C 469 THR ASP TYR MET TYR LEU THR ASN ALA PRO SER TYR THR SEQRES 25 C 469 ASN GLY LYS LEU ASN ILE TYR TYR ARG ARG LEU TYR ASN SEQRES 26 C 469 GLY LEU LYS PHE ILE ILE LYS ARG TYR THR PRO ASN ASN SEQRES 27 C 469 GLU ILE ASP SER PHE VAL LYS SER GLY ASP PHE ILE LYS SEQRES 28 C 469 LEU TYR VAL SER TYR ASN ASN ASN GLU HIS ILE VAL GLY SEQRES 29 C 469 TYR PRO LYS ASP GLY ASN ALA PHE ASN ASN LEU ASP ARG SEQRES 30 C 469 ILE LEU ARG VAL GLY TYR ASN ALA PRO GLY ILE PRO LEU SEQRES 31 C 469 TYR LYS LYS MET GLU ALA VAL LYS LEU ARG ASP LEU LYS SEQRES 32 C 469 THR TYR SER VAL GLN LEU LYS LEU TYR ASP ASP LYS ASN SEQRES 33 C 469 ALA SER LEU GLY LEU VAL GLY THR HIS ASN GLY GLN ILE SEQRES 34 C 469 GLY ASN ASP PRO ASN ARG ASP ILE LEU ILE ALA SER ASN SEQRES 35 C 469 TRP TYR PHE ASN HIS LEU LYS ASP LYS ILE LEU GLY CYS SEQRES 36 C 469 ASP TRP TYR PHE VAL PRO THR ASP GLU GLY TRP THR ASN SEQRES 37 C 469 ASP SEQRES 1 D 490 GLY PRO SER GLN VAL GLN LEU VAL GLU SER GLY GLY GLY SEQRES 2 D 490 LEU VAL GLN ALA GLY GLY SER LEU ARG LEU SER CYS ALA SEQRES 3 D 490 ALA SER GLY ARG THR PHE SER ARG PHE ILE MET GLY TRP SEQRES 4 D 490 PHE ARG GLN ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA SEQRES 5 D 490 ALA VAL GLY LYS SER GLY ASP THR THR TYR TYR ALA ASP SEQRES 6 D 490 SER MET SER GLY ARG PHE ALA ILE SER ARG ASP ASN ALA SEQRES 7 D 490 LYS ASN THR VAL TYR LEU GLN MET ILE SER LEU LYS PRO SEQRES 8 D 490 GLU ASP THR ALA VAL TYR TYR CYS ALA ALA ASP SER SER SEQRES 9 D 490 TYR PHE TYR HIS THR HIS GLU SER GLU TYR ASP TYR TRP SEQRES 10 D 490 GLY GLN GLY THR GLN VAL THR VAL PRO PRO LEU VAL ILE SEQRES 11 D 490 TRP ILE ASN GLY ASP LYS GLY TYR ASN GLY LEU ALA GLU SEQRES 12 D 490 VAL GLY LYS LYS PHE GLU LYS ASP THR GLY ILE LYS VAL SEQRES 13 D 490 THR VAL GLU HIS PRO ASP LYS LEU GLU GLU LYS PHE PRO SEQRES 14 D 490 GLN VAL ALA ALA THR GLY ASP GLY PRO ASP ILE ILE PHE SEQRES 15 D 490 TRP ALA HIS ASP ARG PHE GLY GLY TYR ALA GLN SER GLY SEQRES 16 D 490 LEU LEU ALA GLU ILE THR PRO ASP LYS ALA PHE GLN ASP SEQRES 17 D 490 LYS LEU TYR PRO PHE THR TRP ASP ALA VAL ARG TYR ASN SEQRES 18 D 490 GLY LYS LEU ILE ALA TYR PRO ILE ALA VAL GLU ALA LEU SEQRES 19 D 490 SER LEU ILE TYR ASN LYS ASP LEU LEU PRO ASN PRO PRO SEQRES 20 D 490 LYS THR TRP GLU GLU ILE PRO ALA LEU ASP LYS GLU LEU SEQRES 21 D 490 LYS ALA LYS GLY LYS SER ALA LEU MET PHE ASN LEU GLN SEQRES 22 D 490 GLU PRO TYR PHE THR TRP PRO LEU ILE ALA ALA ASP GLY SEQRES 23 D 490 GLY TYR ALA PHE LYS TYR GLU ASN GLY LYS TYR ASP ILE SEQRES 24 D 490 LYS ASP VAL GLY VAL ASP ASN ALA GLY ALA LYS ALA GLY SEQRES 25 D 490 LEU THR PHE LEU VAL ASP LEU ILE LYS ASN LYS HIS MET SEQRES 26 D 490 ASN ALA ASP THR ASP TYR SER ILE ALA GLU ALA ALA PHE SEQRES 27 D 490 ASN LYS GLY GLU THR ALA MET THR ILE ASN GLY PRO TRP SEQRES 28 D 490 ALA TRP SER ASN ILE ASP THR SER LYS VAL ASN TYR GLY SEQRES 29 D 490 VAL THR VAL LEU PRO THR PHE LYS GLY GLN PRO SER LYS SEQRES 30 D 490 PRO PHE VAL GLY VAL LEU SER ALA GLY ILE ASN ALA ALA SEQRES 31 D 490 SER PRO ASN LYS GLU LEU ALA LYS GLU PHE LEU GLU ASN SEQRES 32 D 490 TYR LEU LEU THR ASP GLU GLY LEU GLU ALA VAL ASN LYS SEQRES 33 D 490 ASP LYS PRO LEU GLY ALA VAL ALA LEU LYS SER TYR GLU SEQRES 34 D 490 GLU GLU LEU ALA LYS ASP PRO ARG ILE ALA ALA THR MET SEQRES 35 D 490 GLU ASN ALA GLN LYS GLY GLU ILE MET PRO ASN ILE PRO SEQRES 36 D 490 GLN MET SER ALA PHE TRP TYR ALA VAL ARG THR ALA VAL SEQRES 37 D 490 ILE ASN ALA ALA SER GLY ARG GLN THR VAL ASP GLU ALA SEQRES 38 D 490 LEU LYS ASP ALA GLN THR PRO GLY ALA HET NAG Z 1 14 HET NAG Z 2 14 HET FUC Z 3 10 HET NAG Y 1 14 HET NAG Y 2 14 HET NAG A 801 14 HET 6UZ A 802 76 HET UKX A 803 26 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM FUC ALPHA-L-FUCOPYRANOSE HETNAM 6UZ OMEGA-UNDECYLENYL-BETA-D-MALTOPYRANOSIDE HETNAM UKX (2S)-2-(2-OXIDANYLIDENEPYRROLIDIN-1-YL)BUTANAMIDE HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA- HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO- HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE HETSYN FUC ALPHA-L-FUCOSE; 6-DEOXY-ALPHA-L-GALACTOPYRANOSE; L- HETSYN 2 FUC FUCOSE; FUCOSE HETSYN 6UZ (2~{R},3~{S},4~{S},5~{R},6~{R})-2-(HYDROXYMETHYL)-6- HETSYN 2 6UZ [(2~{R},3~{S},4~{R},5~{R},6~{R})-2-(HYDROXYMETHYL)-4, HETSYN 3 6UZ 5-BIS(OXIDANYL )-6-UNDEC-10-ENOXY-OXAN-3-YL]OXY-OXANE- HETSYN 4 6UZ 3,4,5-TRIOL HETSYN UKX LEVETIRACETAM FORMUL 4 NAG 5(C8 H15 N O6) FORMUL 4 FUC C6 H12 O5 FORMUL 7 6UZ C23 H42 O11 FORMUL 8 UKX C8 H14 N2 O2 HELIX 1 AA1 ARG A 145 GLY A 160 1 16 HELIX 2 AA2 GLY A 162 VAL A 183 1 22 HELIX 3 AA3 PHE A 184 MET A 197 1 14 HELIX 4 AA4 SER A 200 GLY A 230 1 31 HELIX 5 AA5 ARG A 231 SER A 249 1 19 HELIX 6 AA6 GLY A 254 GLY A 271 1 18 HELIX 7 AA7 SER A 272 GLU A 282 1 11 HELIX 8 AA8 ARG A 289 LEU A 296 1 8 HELIX 9 AA9 CYS A 297 ILE A 315 1 19 HELIX 10 AB1 HIS A 331 ALA A 341 1 11 HELIX 11 AB2 ALA A 341 THR A 352 1 12 HELIX 12 AB3 SER A 357 ASN A 364 1 8 HELIX 13 AB4 LYS A 366 ARG A 383 1 18 HELIX 14 AB5 VAL A 422 CYS A 438 1 17 HELIX 15 AB6 TYR A 443 ARG A 483 1 41 HELIX 16 AB7 PHE A 562 TYR A 564 5 3 HELIX 17 AB8 MET A 596 VAL A 608 1 13 HELIX 18 AB9 VAL A 608 GLY A 623 1 16 HELIX 19 AC1 GLY A 623 CYS A 639 1 17 HELIX 20 AC2 PHE A 640 SER A 643 5 4 HELIX 21 AC3 SER A 647 TYR A 677 1 31 HELIX 22 AC4 LYS A 681 SER A 706 1 26 HELIX 23 AC5 LYS A 712 LYS A 732 1 21 HELIX 24 AC6 SER C 962 TYR C 969 1 8 HELIX 25 AC7 ASN C 1097 LEU C 1109 1 13 HELIX 26 AC8 ASN C 1288 HIS C 1293 5 6 SHEET 1 AA1 6 LYS A 485 PRO A 488 0 SHEET 2 AA1 6 LEU A 501 ARG A 507 1 O ILE A 505 N PHE A 487 SHEET 3 AA1 6 ARG A 520 GLU A 527 1 O GLU A 527 N HIS A 506 SHEET 4 AA1 6 TYR A 535 SER A 542 1 O SER A 542 N SER A 523 SHEET 5 AA1 6 PHE A 545 ARG A 547 0 SHEET 6 AA1 6 PHE A 566 VAL A 567 1 O VAL A 567 N PHE A 546 SHEET 1 AA2 6 THR A 496 PHE A 497 0 SHEET 2 AA2 6 LYS A 515 ILE A 517 1 O ILE A 517 N PHE A 497 SHEET 3 AA2 6 TYR A 535 SER A 542 1 O TYR A 535 N PHE A 516 SHEET 4 AA2 6 ARG A 520 GLU A 527 1 N SER A 523 O SER A 542 SHEET 5 AA2 6 VAL A 555 THR A 559 0 SHEET 6 AA2 6 THR A 575 LEU A 577 1 O LEU A 577 N ASN A 558 SHEET 1 AA312 ILE C1164 ARG C1167 0 SHEET 2 AA312 SER C1156 ASN C1159 -1 N TYR C1157 O TYR C1166 SHEET 3 AA312 ARG A 491 GLU A 493 1 N ARG A 491 O SER C1156 SHEET 4 AA312 GLN A 510 PHE A 512 1 O GLN A 510 N VAL A 492 SHEET 5 AA312 PHE A 531 GLU A 532 1 O GLU A 532 N TYR A 511 SHEET 6 AA312 THR A 550 ILE A 552 1 O THR A 550 N PHE A 531 SHEET 7 AA312 ARG A 570 VAL A 572 1 O ARG A 570 N PHE A 551 SHEET 8 AA312 THR D 61 TYR D 63 1 O TYR D 63 N LEU A 571 SHEET 9 AA312 GLU D 49 VAL D 54 -1 N ALA D 53 O TYR D 62 SHEET 10 AA312 ILE D 36 GLN D 42 -1 N ARG D 41 O GLU D 49 SHEET 11 AA312 ALA D 95 ASP D 102 -1 O ASP D 102 N ILE D 36 SHEET 12 AA312 THR D 121 VAL D 123 -1 O VAL D 123 N ALA D 95 SHEET 1 AA4 5 LEU C1052 ALA C1056 0 SHEET 2 AA4 5 ALA C1044 ILE C1048 -1 N ALA C1044 O ALA C1056 SHEET 3 AA4 5 VAL C1032 ASN C1038 -1 N THR C1035 O TYR C1047 SHEET 4 AA4 5 THR C 951 ARG C 957 -1 N PHE C 954 O ILE C1034 SHEET 5 AA4 5 SER C1085 PHE C1092 -1 O ASP C1087 N TRP C 955 SHEET 1 AA5 5 ILE C1014 ARG C1017 0 SHEET 2 AA5 5 ASN C 999 THR C1003 -1 N TRP C1002 O ILE C1014 SHEET 3 AA5 5 SER C 992 LYS C 996 -1 N LYS C 996 O ASN C 999 SHEET 4 AA5 5 TYR C 974 SER C 978 -1 N ILE C 977 O VAL C 993 SHEET 5 AA5 5 THR C1071 ASP C1075 -1 O THR C1071 N SER C 978 SHEET 1 AA6 2 LEU C1130 PRO C1132 0 SHEET 2 AA6 2 TRP C1303 PHE C1305 -1 O TYR C1304 N ILE C1131 SHEET 1 AA7 2 LYS C1138 LEU C1142 0 SHEET 2 AA7 2 MET C1149 ASN C1153 -1 O THR C1152 N ASP C1139 SHEET 1 AA8 4 LYS C1174 ARG C1179 0 SHEET 2 AA8 4 ASP C1194 SER C1201 -1 O SER C1201 N LYS C1174 SHEET 3 AA8 4 GLU C1206 PRO C1212 -1 O HIS C1207 N VAL C1200 SHEET 4 AA8 4 ARG C1226 VAL C1227 -1 O ARG C1226 N GLY C1210 SHEET 1 AA9 9 ALA C1217 PHE C1218 0 SHEET 2 AA9 9 ASP C1222 ILE C1224 -1 O ASP C1222 N PHE C1218 SHEET 3 AA9 9 ARG C1281 ALA C1286 -1 O ALA C1286 N ARG C1223 SHEET 4 AA9 9 SER C1264 GLY C1273 -1 N GLY C1269 O ILE C1285 SHEET 5 AA9 9 GLN C1254 TYR C1258 -1 N LEU C1255 O VAL C1268 SHEET 6 AA9 9 MET C1240 VAL C1243 -1 N VAL C1243 O GLN C1254 SHEET 7 AA9 9 ASP C1194 SER C1201 -1 N ILE C1196 O MET C1240 SHEET 8 AA9 9 GLU C1206 PRO C1212 -1 O HIS C1207 N VAL C1200 SHEET 9 AA9 9 LEU C1236 TYR C1237 -1 O TYR C1237 N TYR C1211 SHEET 1 AB1 4 VAL D 8 SER D 10 0 SHEET 2 AB1 4 SER D 20 ALA D 26 -1 O SER D 24 N SER D 10 SHEET 3 AB1 4 THR D 81 ILE D 87 -1 O VAL D 82 N CYS D 25 SHEET 4 AB1 4 PHE D 71 ASP D 76 -1 N SER D 74 O TYR D 83 SSBOND 1 CYS A 198 CYS A 583 1555 1555 2.03 SSBOND 2 CYS D 25 CYS D 99 1555 1555 2.03 LINK ND2 ASN A 498 C1 NAG A 801 1555 1555 1.44 LINK ND2 ASN A 548 C1 NAG Y 1 1555 1555 1.44 LINK ND2 ASN A 573 C1 NAG Z 1 1555 1555 1.44 LINK O4 NAG Z 1 C1 NAG Z 2 1555 1555 1.44 LINK O6 NAG Z 1 C1 FUC Z 3 1555 1555 1.44 LINK O4 NAG Y 1 C1 NAG Y 2 1555 1555 1.44 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