HEADER MEMBRANE PROTEIN 14-MAR-25 9NR8 TITLE THE STRUCTURE OF CEREBELLAR GLUA1/A4 ATD COMPND MOL_ID: 1; COMPND 2 MOLECULE: GLUTAMATE RECEPTOR 1; COMPND 3 CHAIN: A, C; COMPND 4 SYNONYM: GLUR-1,AMPA-SELECTIVE GLUTAMATE RECEPTOR 1,GLUR-A,GLUR-K1, COMPND 5 GLUTAMATE RECEPTOR IONOTROPIC,AMPA 1; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: GLUTAMATE RECEPTOR 4; COMPND 8 CHAIN: B, D; COMPND 9 SYNONYM: GLUR-4,GLUR4,AMPA-SELECTIVE GLUTAMATE RECEPTOR 4,GLUR-D, COMPND 10 GLUTAMATE RECEPTOR IONOTROPIC,AMPA 4,GLUA4; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: 11B8 SCFV; COMPND 13 CHAIN: E, F; COMPND 14 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS; SOURCE 3 ORGANISM_COMMON: NORWAY RAT; SOURCE 4 ORGANISM_TAXID: 10116; SOURCE 5 MOL_ID: 2; SOURCE 6 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS; SOURCE 7 ORGANISM_COMMON: NORWAY RAT; SOURCE 8 ORGANISM_TAXID: 10116; SOURCE 9 MOL_ID: 3; SOURCE 10 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 11 ORGANISM_COMMON: MOUSE; SOURCE 12 ORGANISM_TAXID: 10090; SOURCE 13 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 14 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 7108 KEYWDS IGLUR, CP-AMPA RECEPTORS, MEMBRANE PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR C.F.FANG,E.GOUAUX REVDAT 1 02-JUL-25 9NR8 0 JRNL AUTH C.FANG,C.J.SPANGLER,J.PARK,N.SHELDON,L.O.TRUSSELL,E.GOUAUX JRNL TITL GATING AND NOELIN CLUSTERING OF NATIVE CA2+-PERMEABLE AMPA JRNL TITL 2 RECEPTORS JRNL REF NATURE 2025 JRNL REFN ESSN 1476-4687 JRNL DOI 10.1038/S41586-025-09289-0 REMARK 2 REMARK 2 RESOLUTION. 3.53 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : PHENIX REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : NULL REMARK 3 REFINEMENT SPACE : NULL REMARK 3 REFINEMENT PROTOCOL : NULL REMARK 3 REFINEMENT TARGET : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL REMARK 3 REMARK 3 FITTING PROCEDURE : NULL REMARK 3 REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 3.530 REMARK 3 NUMBER OF PARTICLES : 36405 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 9NR8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-MAR-25. REMARK 100 THE DEPOSITION ID IS D_1000294018. 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 : CP-AMPA RECEPTORS REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 0.10 REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 8.00 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 : FEI FALCON IV (4K 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 : OTHER 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: A, B, C, D, E, F, I, J, N, G, REMARK 350 AND CHAINS: H, K, L, M 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 ALA A 1 REMARK 465 ALA C 1 REMARK 465 SER E 118 REMARK 465 SER E 119 REMARK 465 SER E 120 REMARK 465 GLY E 121 REMARK 465 GLY E 122 REMARK 465 GLY E 123 REMARK 465 GLY E 124 REMARK 465 SER E 125 REMARK 465 GLY E 126 REMARK 465 GLY E 127 REMARK 465 GLY E 128 REMARK 465 GLY E 129 REMARK 465 SER E 130 REMARK 465 GLY E 131 REMARK 465 GLY E 132 REMARK 465 GLY E 133 REMARK 465 GLY E 134 REMARK 465 ALA E 247 REMARK 465 SER E 248 REMARK 465 ASN E 249 REMARK 465 TRP E 250 REMARK 465 SER E 251 REMARK 465 HIS E 252 REMARK 465 PRO E 253 REMARK 465 GLN E 254 REMARK 465 PHE E 255 REMARK 465 GLU E 256 REMARK 465 LYS E 257 REMARK 465 SER F 118 REMARK 465 SER F 119 REMARK 465 SER F 120 REMARK 465 GLY F 121 REMARK 465 GLY F 122 REMARK 465 GLY F 123 REMARK 465 GLY F 124 REMARK 465 SER F 125 REMARK 465 GLY F 126 REMARK 465 GLY F 127 REMARK 465 GLY F 128 REMARK 465 GLY F 129 REMARK 465 SER F 130 REMARK 465 GLY F 131 REMARK 465 GLY F 132 REMARK 465 GLY F 133 REMARK 465 GLY F 134 REMARK 465 ALA F 247 REMARK 465 SER F 248 REMARK 465 ASN F 249 REMARK 465 TRP F 250 REMARK 465 SER F 251 REMARK 465 HIS F 252 REMARK 465 PRO F 253 REMARK 465 GLN F 254 REMARK 465 PHE F 255 REMARK 465 GLU F 256 REMARK 465 LYS F 257 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 ASN A 2 CG OD1 ND2 REMARK 470 PHE A 3 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LYS A 178 CG CD CE NZ REMARK 470 ARG A 180 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 200 CG CD CE NZ REMARK 470 ARG A 262 CG CD NE CZ NH1 NH2 REMARK 470 ARG A 299 CG CD NE CZ NH1 NH2 REMARK 470 ASN A 301 CG OD1 ND2 REMARK 470 ARG B 15 CG CD NE CZ NH1 NH2 REMARK 470 GLU B 39 CG CD OE1 OE2 REMARK 470 ARG B 265 CG CD NE CZ NH1 NH2 REMARK 470 ASN C 2 CG OD1 ND2 REMARK 470 PHE C 3 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LYS C 200 CG CD CE NZ REMARK 470 ARG C 262 CG CD NE CZ NH1 NH2 REMARK 470 ARG C 299 CG CD NE CZ NH1 NH2 REMARK 470 ASN C 301 CG OD1 ND2 REMARK 470 GLU D 39 CG CD OE1 OE2 REMARK 470 LYS D 299 CG CD CE NZ REMARK 470 GLU E 1 CG CD OE1 OE2 REMARK 470 VAL E 2 CG1 CG2 REMARK 470 LYS E 3 CG CD CE NZ REMARK 470 LEU E 4 CG CD1 CD2 REMARK 470 LEU E 5 CG CD1 CD2 REMARK 470 GLU E 6 CG CD OE1 OE2 REMARK 470 SER E 7 OG REMARK 470 LEU E 11 CG CD1 CD2 REMARK 470 VAL E 12 CG1 CG2 REMARK 470 GLN E 13 CG CD OE1 NE2 REMARK 470 PRO E 14 CG CD REMARK 470 SER E 17 OG REMARK 470 LEU E 18 CG CD1 CD2 REMARK 470 LYS E 19 CG CD CE NZ REMARK 470 LEU E 20 CG CD1 CD2 REMARK 470 SER E 21 OG REMARK 470 CYS E 22 SG REMARK 470 SER E 25 OG REMARK 470 PHE E 27 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ASP E 28 CG OD1 OD2 REMARK 470 PHE E 29 CG CD1 CD2 CE1 CE2 CZ REMARK 470 SER E 30 OG REMARK 470 GLU E 31 CG CD OE1 OE2 REMARK 470 TYR E 32 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 TRP E 33 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP E 33 CZ3 CH2 REMARK 470 MET E 34 CG SD CE REMARK 470 SER E 35 OG REMARK 470 TRP E 36 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP E 36 CZ3 CH2 REMARK 470 VAL E 37 CG1 CG2 REMARK 470 ARG E 38 CG CD NE CZ NH1 NH2 REMARK 470 GLN E 39 CG CD OE1 NE2 REMARK 470 PRO E 41 CG CD REMARK 470 LYS E 43 CG CD CE NZ REMARK 470 LEU E 45 CG CD1 CD2 REMARK 470 GLU E 46 CG CD OE1 OE2 REMARK 470 TRP E 47 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP E 47 CZ3 CH2 REMARK 470 ILE E 48 CG1 CG2 CD1 REMARK 470 GLU E 50 CG CD OE1 OE2 REMARK 470 ILE E 51 CG1 CG2 CD1 REMARK 470 ASN E 52 CG OD1 ND2 REMARK 470 PRO E 53 CG CD REMARK 470 ASP E 54 CG OD1 OD2 REMARK 470 SER E 55 OG REMARK 470 SER E 56 OG REMARK 470 SER E 57 OG REMARK 470 ILE E 58 CG1 CG2 CD1 REMARK 470 ASP E 59 CG OD1 OD2 REMARK 470 TYR E 60 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 THR E 61 OG1 CG2 REMARK 470 PRO E 62 CG CD REMARK 470 SER E 63 OG REMARK 470 LEU E 64 CG CD1 CD2 REMARK 470 LYS E 65 CG CD CE NZ REMARK 470 ASP E 66 CG OD1 OD2 REMARK 470 LYS E 67 CG CD CE NZ REMARK 470 ILE E 68 CG1 CG2 CD1 REMARK 470 ILE E 69 CG1 CG2 CD1 REMARK 470 ILE E 70 CG1 CG2 CD1 REMARK 470 SER E 71 OG REMARK 470 ARG E 72 CG CD NE CZ NH1 NH2 REMARK 470 ASP E 73 CG OD1 OD2 REMARK 470 ASN E 74 CG OD1 ND2 REMARK 470 LYS E 76 CG CD CE NZ REMARK 470 LYS E 77 CG CD CE NZ REMARK 470 THR E 78 OG1 CG2 REMARK 470 LEU E 79 CG CD1 CD2 REMARK 470 TYR E 80 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LEU E 81 CG CD1 CD2 REMARK 470 GLN E 82 CG CD OE1 NE2 REMARK 470 LEU E 83 CG CD1 CD2 REMARK 470 SER E 84 OG REMARK 470 LYS E 85 CG CD CE NZ REMARK 470 VAL E 86 CG1 CG2 REMARK 470 ARG E 87 CG CD NE CZ NH1 NH2 REMARK 470 SER E 88 OG REMARK 470 GLU E 89 CG CD OE1 OE2 REMARK 470 ASP E 90 CG OD1 OD2 REMARK 470 THR E 91 OG1 CG2 REMARK 470 LEU E 93 CG CD1 CD2 REMARK 470 TYR E 94 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 TYR E 95 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 CYS E 96 SG REMARK 470 ARG E 98 CG CD NE CZ NH1 NH2 REMARK 470 PRO E 99 CG CD REMARK 470 ARG E 100 CG CD NE CZ NH1 NH2 REMARK 470 ASN E 102 CG OD1 ND2 REMARK 470 TYR E 103 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 VAL E 104 CG1 CG2 REMARK 470 VAL E 105 CG1 CG2 REMARK 470 MET E 106 CG SD CE REMARK 470 ASP E 107 CG OD1 OD2 REMARK 470 TYR E 108 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 TRP E 109 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP E 109 CZ3 CH2 REMARK 470 GLN E 111 CG CD OE1 NE2 REMARK 470 THR E 113 OG1 CG2 REMARK 470 SER E 114 OG REMARK 470 VAL E 115 CG1 CG2 REMARK 470 THR E 116 OG1 CG2 REMARK 470 VAL E 117 CG1 CG2 REMARK 470 ASN E 135 CG OD1 ND2 REMARK 470 ILE E 136 CG1 CG2 CD1 REMARK 470 VAL E 137 CG1 CG2 REMARK 470 LEU E 138 CG CD1 CD2 REMARK 470 THR E 139 OG1 CG2 REMARK 470 GLN E 140 CG CD OE1 NE2 REMARK 470 SER E 141 OG REMARK 470 PRO E 142 CG CD REMARK 470 SER E 144 OG REMARK 470 LEU E 145 CG CD1 CD2 REMARK 470 VAL E 147 CG1 CG2 REMARK 470 SER E 148 OG REMARK 470 LEU E 149 CG CD1 CD2 REMARK 470 GLN E 151 CG CD OE1 NE2 REMARK 470 ARG E 152 CG CD NE CZ NH1 NH2 REMARK 470 THR E 154 OG1 CG2 REMARK 470 ILE E 155 CG1 CG2 CD1 REMARK 470 SER E 156 OG REMARK 470 CYS E 157 SG REMARK 470 ARG E 158 CG CD NE CZ NH1 NH2 REMARK 470 SER E 160 OG REMARK 470 GLU E 161 CG CD OE1 OE2 REMARK 470 SER E 162 OG REMARK 470 VAL E 163 CG1 CG2 REMARK 470 ASP E 164 CG OD1 OD2 REMARK 470 SER E 165 OG REMARK 470 TYR E 166 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 SER E 168 OG REMARK 470 SER E 169 OG REMARK 470 PHE E 170 CG CD1 CD2 CE1 CE2 CZ REMARK 470 VAL E 171 CG1 CG2 REMARK 470 HIS E 172 CG ND1 CD2 CE1 NE2 REMARK 470 TRP E 173 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP E 173 CZ3 CH2 REMARK 470 TYR E 174 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 GLN E 175 CG CD OE1 NE2 REMARK 470 GLN E 176 CG CD OE1 NE2 REMARK 470 LYS E 177 CG CD CE NZ REMARK 470 PRO E 178 CG CD REMARK 470 GLN E 180 CG CD OE1 NE2 REMARK 470 PRO E 181 CG CD REMARK 470 PRO E 182 CG CD REMARK 470 LYS E 183 CG CD CE NZ REMARK 470 LEU E 184 CG CD1 CD2 REMARK 470 LEU E 185 CG CD1 CD2 REMARK 470 ILE E 186 CG1 CG2 CD1 REMARK 470 PHE E 187 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LEU E 188 CG CD1 CD2 REMARK 470 SER E 190 OG REMARK 470 LYS E 191 CG CD CE NZ REMARK 470 LEU E 192 CG CD1 CD2 REMARK 470 GLU E 193 CG CD OE1 OE2 REMARK 470 SER E 194 OG REMARK 470 VAL E 196 CG1 CG2 REMARK 470 PRO E 197 CG CD REMARK 470 ARG E 199 CG CD NE CZ NH1 NH2 REMARK 470 PHE E 200 CG CD1 CD2 CE1 CE2 CZ REMARK 470 SER E 201 OG REMARK 470 SER E 203 OG REMARK 470 SER E 205 OG REMARK 470 ARG E 206 CG CD NE CZ NH1 NH2 REMARK 470 THR E 207 OG1 CG2 REMARK 470 ASP E 208 CG OD1 OD2 REMARK 470 PHE E 209 CG CD1 CD2 CE1 CE2 CZ REMARK 470 THR E 210 OG1 CG2 REMARK 470 LEU E 211 CG CD1 CD2 REMARK 470 THR E 212 OG1 CG2 REMARK 470 ILE E 213 CG1 CG2 CD1 REMARK 470 ASP E 214 CG OD1 OD2 REMARK 470 PRO E 215 CG CD REMARK 470 VAL E 216 CG1 CG2 REMARK 470 GLU E 217 CG CD OE1 OE2 REMARK 470 ASP E 219 CG OD1 OD2 REMARK 470 ASP E 220 CG OD1 OD2 REMARK 470 THR E 223 OG1 CG2 REMARK 470 TYR E 224 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 TYR E 225 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 CYS E 226 SG REMARK 470 GLN E 227 CG CD OE1 NE2 REMARK 470 GLN E 228 CG CD OE1 NE2 REMARK 470 THR E 229 OG1 CG2 REMARK 470 ASN E 230 CG OD1 ND2 REMARK 470 GLU E 231 CG CD OE1 OE2 REMARK 470 ASP E 232 CG OD1 OD2 REMARK 470 PRO E 233 CG CD REMARK 470 TYR E 234 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 THR E 235 OG1 CG2 REMARK 470 PHE E 236 CG CD1 CD2 CE1 CE2 CZ REMARK 470 THR E 240 OG1 CG2 REMARK 470 LYS E 241 CG CD CE NZ REMARK 470 LEU E 242 CG CD1 CD2 REMARK 470 GLU E 243 CG CD OE1 OE2 REMARK 470 ILE E 244 CG1 CG2 CD1 REMARK 470 LYS E 245 CG CD CE NZ REMARK 470 ARG E 246 CG CD NE CZ NH1 NH2 REMARK 470 GLU F 1 CG CD OE1 OE2 REMARK 470 VAL F 2 CG1 CG2 REMARK 470 LYS F 3 CG CD CE NZ REMARK 470 LEU F 4 CG CD1 CD2 REMARK 470 LEU F 5 CG CD1 CD2 REMARK 470 GLU F 6 CG CD OE1 OE2 REMARK 470 SER F 7 OG REMARK 470 LEU F 11 CG CD1 CD2 REMARK 470 VAL F 12 CG1 CG2 REMARK 470 GLN F 13 CG CD OE1 NE2 REMARK 470 PRO F 14 CG CD REMARK 470 SER F 17 OG REMARK 470 LEU F 18 CG CD1 CD2 REMARK 470 LYS F 19 CG CD CE NZ REMARK 470 LEU F 20 CG CD1 CD2 REMARK 470 SER F 21 OG REMARK 470 CYS F 22 SG REMARK 470 SER F 25 OG REMARK 470 PHE F 27 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ASP F 28 CG OD1 OD2 REMARK 470 PHE F 29 CG CD1 CD2 CE1 CE2 CZ REMARK 470 SER F 30 OG REMARK 470 GLU F 31 CG CD OE1 OE2 REMARK 470 TYR F 32 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 TRP F 33 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP F 33 CZ3 CH2 REMARK 470 MET F 34 CG SD CE REMARK 470 SER F 35 OG REMARK 470 TRP F 36 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP F 36 CZ3 CH2 REMARK 470 VAL F 37 CG1 CG2 REMARK 470 ARG F 38 CG CD NE CZ NH1 NH2 REMARK 470 GLN F 39 CG CD OE1 NE2 REMARK 470 PRO F 41 CG CD REMARK 470 LYS F 43 CG CD CE NZ REMARK 470 LEU F 45 CG CD1 CD2 REMARK 470 GLU F 46 CG CD OE1 OE2 REMARK 470 TRP F 47 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP F 47 CZ3 CH2 REMARK 470 ILE F 48 CG1 CG2 CD1 REMARK 470 GLU F 50 CG CD OE1 OE2 REMARK 470 ILE F 51 CG1 CG2 CD1 REMARK 470 ASN F 52 CG OD1 ND2 REMARK 470 PRO F 53 CG CD REMARK 470 ASP F 54 CG OD1 OD2 REMARK 470 SER F 55 OG REMARK 470 SER F 56 OG REMARK 470 SER F 57 OG REMARK 470 ILE F 58 CG1 CG2 CD1 REMARK 470 ASP F 59 CG OD1 OD2 REMARK 470 TYR F 60 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 THR F 61 OG1 CG2 REMARK 470 PRO F 62 CG CD REMARK 470 SER F 63 OG REMARK 470 LEU F 64 CG CD1 CD2 REMARK 470 LYS F 65 CG CD CE NZ REMARK 470 ASP F 66 CG OD1 OD2 REMARK 470 LYS F 67 CG CD CE NZ REMARK 470 ILE F 68 CG1 CG2 CD1 REMARK 470 ILE F 69 CG1 CG2 CD1 REMARK 470 ILE F 70 CG1 CG2 CD1 REMARK 470 SER F 71 OG REMARK 470 ARG F 72 CG CD NE CZ NH1 NH2 REMARK 470 ASP F 73 CG OD1 OD2 REMARK 470 ASN F 74 CG OD1 ND2 REMARK 470 LYS F 76 CG CD CE NZ REMARK 470 LYS F 77 CG CD CE NZ REMARK 470 THR F 78 OG1 CG2 REMARK 470 LEU F 79 CG CD1 CD2 REMARK 470 TYR F 80 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LEU F 81 CG CD1 CD2 REMARK 470 GLN F 82 CG CD OE1 NE2 REMARK 470 LEU F 83 CG CD1 CD2 REMARK 470 SER F 84 OG REMARK 470 LYS F 85 CG CD CE NZ REMARK 470 VAL F 86 CG1 CG2 REMARK 470 ARG F 87 CG CD NE CZ NH1 NH2 REMARK 470 SER F 88 OG REMARK 470 GLU F 89 CG CD OE1 OE2 REMARK 470 ASP F 90 CG OD1 OD2 REMARK 470 THR F 91 OG1 CG2 REMARK 470 LEU F 93 CG CD1 CD2 REMARK 470 TYR F 94 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 TYR F 95 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 CYS F 96 SG REMARK 470 ARG F 98 CG CD NE CZ NH1 NH2 REMARK 470 PRO F 99 CG CD REMARK 470 ARG F 100 CG CD NE CZ NH1 NH2 REMARK 470 ASN F 102 CG OD1 ND2 REMARK 470 TYR F 103 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 VAL F 104 CG1 CG2 REMARK 470 VAL F 105 CG1 CG2 REMARK 470 MET F 106 CG SD CE REMARK 470 ASP F 107 CG OD1 OD2 REMARK 470 TYR F 108 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 TRP F 109 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP F 109 CZ3 CH2 REMARK 470 GLN F 111 CG CD OE1 NE2 REMARK 470 THR F 113 OG1 CG2 REMARK 470 SER F 114 OG REMARK 470 VAL F 115 CG1 CG2 REMARK 470 THR F 116 OG1 CG2 REMARK 470 VAL F 117 CG1 CG2 REMARK 470 ASN F 135 CG OD1 ND2 REMARK 470 ILE F 136 CG1 CG2 CD1 REMARK 470 VAL F 137 CG1 CG2 REMARK 470 LEU F 138 CG CD1 CD2 REMARK 470 THR F 139 OG1 CG2 REMARK 470 GLN F 140 CG CD OE1 NE2 REMARK 470 SER F 141 OG REMARK 470 PRO F 142 CG CD REMARK 470 SER F 144 OG REMARK 470 LEU F 145 CG CD1 CD2 REMARK 470 VAL F 147 CG1 CG2 REMARK 470 SER F 148 OG REMARK 470 LEU F 149 CG CD1 CD2 REMARK 470 GLN F 151 CG CD OE1 NE2 REMARK 470 ARG F 152 CG CD NE CZ NH1 NH2 REMARK 470 THR F 154 OG1 CG2 REMARK 470 ILE F 155 CG1 CG2 CD1 REMARK 470 SER F 156 OG REMARK 470 CYS F 157 SG REMARK 470 ARG F 158 CG CD NE CZ NH1 NH2 REMARK 470 SER F 160 OG REMARK 470 GLU F 161 CG CD OE1 OE2 REMARK 470 SER F 162 OG REMARK 470 VAL F 163 CG1 CG2 REMARK 470 ASP F 164 CG OD1 OD2 REMARK 470 SER F 165 OG REMARK 470 TYR F 166 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 SER F 168 OG REMARK 470 SER F 169 OG REMARK 470 PHE F 170 CG CD1 CD2 CE1 CE2 CZ REMARK 470 VAL F 171 CG1 CG2 REMARK 470 HIS F 172 CG ND1 CD2 CE1 NE2 REMARK 470 TRP F 173 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP F 173 CZ3 CH2 REMARK 470 TYR F 174 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 GLN F 175 CG CD OE1 NE2 REMARK 470 GLN F 176 CG CD OE1 NE2 REMARK 470 LYS F 177 CG CD CE NZ REMARK 470 PRO F 178 CG CD REMARK 470 GLN F 180 CG CD OE1 NE2 REMARK 470 PRO F 181 CG CD REMARK 470 PRO F 182 CG CD REMARK 470 LYS F 183 CG CD CE NZ REMARK 470 LEU F 184 CG CD1 CD2 REMARK 470 LEU F 185 CG CD1 CD2 REMARK 470 ILE F 186 CG1 CG2 CD1 REMARK 470 PHE F 187 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LEU F 188 CG CD1 CD2 REMARK 470 SER F 190 OG REMARK 470 LYS F 191 CG CD CE NZ REMARK 470 LEU F 192 CG CD1 CD2 REMARK 470 GLU F 193 CG CD OE1 OE2 REMARK 470 SER F 194 OG REMARK 470 VAL F 196 CG1 CG2 REMARK 470 PRO F 197 CG CD REMARK 470 ARG F 199 CG CD NE CZ NH1 NH2 REMARK 470 PHE F 200 CG CD1 CD2 CE1 CE2 CZ REMARK 470 SER F 201 OG REMARK 470 SER F 203 OG REMARK 470 SER F 205 OG REMARK 470 ARG F 206 CG CD NE CZ NH1 NH2 REMARK 470 THR F 207 OG1 CG2 REMARK 470 ASP F 208 CG OD1 OD2 REMARK 470 PHE F 209 CG CD1 CD2 CE1 CE2 CZ REMARK 470 THR F 210 OG1 CG2 REMARK 470 LEU F 211 CG CD1 CD2 REMARK 470 THR F 212 OG1 CG2 REMARK 470 ILE F 213 CG1 CG2 CD1 REMARK 470 ASP F 214 CG OD1 OD2 REMARK 470 PRO F 215 CG CD REMARK 470 VAL F 216 CG1 CG2 REMARK 470 GLU F 217 CG CD OE1 OE2 REMARK 470 ASP F 219 CG OD1 OD2 REMARK 470 ASP F 220 CG OD1 OD2 REMARK 470 THR F 223 OG1 CG2 REMARK 470 TYR F 224 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 TYR F 225 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 CYS F 226 SG REMARK 470 GLN F 227 CG CD OE1 NE2 REMARK 470 GLN F 228 CG CD OE1 NE2 REMARK 470 THR F 229 OG1 CG2 REMARK 470 ASN F 230 CG OD1 ND2 REMARK 470 GLU F 231 CG CD OE1 OE2 REMARK 470 ASP F 232 CG OD1 OD2 REMARK 470 PRO F 233 CG CD REMARK 470 TYR F 234 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 THR F 235 OG1 CG2 REMARK 470 PHE F 236 CG CD1 CD2 CE1 CE2 CZ REMARK 470 THR F 240 OG1 CG2 REMARK 470 LYS F 241 CG CD CE NZ REMARK 470 LEU F 242 CG CD1 CD2 REMARK 470 GLU F 243 CG CD OE1 OE2 REMARK 470 ILE F 244 CG1 CG2 CD1 REMARK 470 LYS F 245 CG CD CE NZ REMARK 470 ARG F 246 CG CD NE CZ NH1 NH2 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 OD2 ASP D 141 OE2 GLU D 194 1.79 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 ASP B 139 CB - CG - OD2 ANGL. DEV. = 6.3 DEGREES REMARK 500 ASP D 139 CB - CG - OD1 ANGL. DEV. = 6.8 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 SER A 47 175.06 179.47 REMARK 500 ASP A 134 46.29 -87.79 REMARK 500 TYR A 240 48.22 -88.99 REMARK 500 THR A 261 -152.25 56.45 REMARK 500 LYS A 266 71.84 59.65 REMARK 500 ARG A 267 70.44 65.19 REMARK 500 VAL A 311 72.67 50.16 REMARK 500 HIS A 355 -2.63 65.59 REMARK 500 LYS A 369 -132.34 58.50 REMARK 500 ALA B 40 80.86 -151.05 REMARK 500 GLU B 52 84.88 64.02 REMARK 500 THR B 53 73.62 65.49 REMARK 500 ALA B 54 94.37 -66.24 REMARK 500 SER B 108 -134.10 52.38 REMARK 500 GLN B 109 -117.02 61.39 REMARK 500 PHE B 110 30.89 -99.82 REMARK 500 ASN B 351 61.49 60.57 REMARK 500 LYS B 375 -142.18 58.99 REMARK 500 ASP C 134 45.29 -87.98 REMARK 500 LEU C 222 49.45 -91.57 REMARK 500 ASP C 256 30.80 -98.45 REMARK 500 ARG C 258 -49.41 70.92 REMARK 500 ASP C 259 81.86 58.79 REMARK 500 THR C 261 45.07 -83.80 REMARK 500 ARG C 262 -157.32 55.34 REMARK 500 TRP C 265 -71.80 -107.17 REMARK 500 LYS C 266 -117.93 41.01 REMARK 500 ALA C 310 35.86 -98.85 REMARK 500 GLN C 325 -9.07 -143.19 REMARK 500 HIS C 355 12.30 55.68 REMARK 500 LYS C 369 -137.83 58.38 REMARK 500 ALA D 40 78.54 -157.97 REMARK 500 GLU D 52 76.71 60.89 REMARK 500 THR D 53 71.02 57.21 REMARK 500 SER D 108 -134.83 57.27 REMARK 500 GLN D 109 -106.22 59.16 REMARK 500 ASN D 248 58.42 -92.47 REMARK 500 ASN D 307 53.83 -92.68 REMARK 500 ASP D 344 -169.44 -118.11 REMARK 500 ASN D 351 57.40 30.50 REMARK 500 LYS D 375 -140.43 59.13 REMARK 500 ALA E 189 17.88 57.70 REMARK 500 ALA F 189 19.06 56.88 REMARK 500 REMARK 500 REMARK: NULL REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 NAG H 1 REMARK 610 NAG M 1 REMARK 610 NAG A 401 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-49725 RELATED DB: EMDB REMARK 900 THE STRUCTURE OF GLUA1/A4 LBD-TMD IN NOELIN-AMPAR COMPLEX DBREF 9NR8 A 1 373 UNP P19490 GRIA1_RAT 19 391 DBREF 9NR8 B 2 379 UNP P19493 GRIA4_RAT 22 399 DBREF 9NR8 C 1 373 UNP P19490 GRIA1_RAT 19 391 DBREF 9NR8 D 2 379 UNP P19493 GRIA4_RAT 22 399 DBREF 9NR8 E 1 257 PDB 9NR8 9NR8 1 257 DBREF 9NR8 F 1 257 PDB 9NR8 9NR8 1 257 SEQRES 1 A 373 ALA ASN PHE PRO ASN ASN ILE GLN ILE GLY GLY LEU PHE SEQRES 2 A 373 PRO ASN GLN GLN SER GLN GLU HIS ALA ALA PHE ARG PHE SEQRES 3 A 373 ALA LEU SER GLN LEU THR GLU PRO PRO LYS LEU LEU PRO SEQRES 4 A 373 GLN ILE ASP ILE VAL ASN ILE SER ASP SER PHE GLU MET SEQRES 5 A 373 THR TYR ARG PHE CYS SER GLN PHE SER LYS GLY VAL TYR SEQRES 6 A 373 ALA ILE PHE GLY PHE TYR GLU ARG ARG THR VAL ASN MET SEQRES 7 A 373 LEU THR SER PHE CYS GLY ALA LEU HIS VAL CYS PHE ILE SEQRES 8 A 373 THR PRO SER PHE PRO VAL ASP THR SER ASN GLN PHE VAL SEQRES 9 A 373 LEU GLN LEU ARG PRO GLU LEU GLN GLU ALA LEU ILE SER SEQRES 10 A 373 ILE ILE ASP HIS TYR LYS TRP GLN THR PHE VAL TYR ILE SEQRES 11 A 373 TYR ASP ALA ASP ARG GLY LEU SER VAL LEU GLN ARG VAL SEQRES 12 A 373 LEU ASP THR ALA ALA GLU LYS ASN TRP GLN VAL THR ALA SEQRES 13 A 373 VAL ASN ILE LEU THR THR THR GLU GLU GLY TYR ARG MET SEQRES 14 A 373 LEU PHE GLN ASP LEU GLU LYS LYS LYS GLU ARG LEU VAL SEQRES 15 A 373 VAL VAL ASP CYS GLU SER GLU ARG LEU ASN ALA ILE LEU SEQRES 16 A 373 GLY GLN ILE VAL LYS LEU GLU LYS ASN GLY ILE GLY TYR SEQRES 17 A 373 HIS TYR ILE LEU ALA ASN LEU GLY PHE MET ASP ILE ASP SEQRES 18 A 373 LEU ASN LYS PHE LYS GLU SER GLY ALA ASN VAL THR GLY SEQRES 19 A 373 PHE GLN LEU VAL ASN TYR THR ASP THR ILE PRO ALA ARG SEQRES 20 A 373 ILE MET GLN GLN TRP ARG THR SER ASP SER ARG ASP HIS SEQRES 21 A 373 THR ARG VAL ASP TRP LYS ARG PRO LYS TYR THR SER ALA SEQRES 22 A 373 LEU THR TYR ASP GLY VAL LYS VAL MET ALA GLU ALA PHE SEQRES 23 A 373 GLN SER LEU ARG ARG GLN ARG ILE ASP ILE SER ARG ARG SEQRES 24 A 373 GLY ASN ALA GLY ASP CYS LEU ALA ASN PRO ALA VAL PRO SEQRES 25 A 373 TRP GLY GLN GLY ILE ASP ILE GLN ARG ALA LEU GLN GLN SEQRES 26 A 373 VAL ARG PHE GLU GLY LEU THR GLY ASN VAL GLN PHE ASN SEQRES 27 A 373 GLU LYS GLY ARG ARG THR ASN TYR THR LEU HIS VAL ILE SEQRES 28 A 373 GLU MET LYS HIS ASP GLY ILE ARG LYS ILE GLY TYR TRP SEQRES 29 A 373 ASN GLU ASP ASP LYS PHE VAL PRO ALA SEQRES 1 B 378 ALA PHE PRO SER SER VAL GLN ILE GLY GLY LEU PHE ILE SEQRES 2 B 378 ARG ASN THR ASP GLN GLU TYR THR ALA PHE ARG LEU ALA SEQRES 3 B 378 ILE PHE LEU HIS ASN THR SER PRO ASN ALA SER GLU ALA SEQRES 4 B 378 PRO PHE ASN LEU VAL PRO HIS VAL ASP ASN ILE GLU THR SEQRES 5 B 378 ALA ASN SER PHE ALA VAL THR ASN ALA PHE CYS SER GLN SEQRES 6 B 378 TYR SER ARG GLY VAL PHE ALA ILE PHE GLY LEU TYR ASP SEQRES 7 B 378 LYS ARG SER VAL HIS THR LEU THR SER PHE CYS SER ALA SEQRES 8 B 378 LEU HIS ILE SER LEU ILE THR PRO SER PHE PRO THR GLU SEQRES 9 B 378 GLY GLU SER GLN PHE VAL LEU GLN LEU ARG PRO SER LEU SEQRES 10 B 378 ARG GLY ALA LEU LEU SER LEU LEU ASP HIS TYR GLU TRP SEQRES 11 B 378 ASN CYS PHE VAL PHE LEU TYR ASP THR ASP ARG GLY TYR SEQRES 12 B 378 SER ILE LEU GLN ALA ILE MET GLU LYS ALA GLY GLN ASN SEQRES 13 B 378 GLY TRP HIS VAL SER ALA ILE CYS VAL GLU ASN PHE ASN SEQRES 14 B 378 ASP VAL SER TYR ARG GLN LEU LEU GLU GLU LEU ASP ARG SEQRES 15 B 378 ARG GLN GLU LYS LYS PHE VAL ILE ASP CYS GLU ILE GLU SEQRES 16 B 378 ARG LEU GLN ASN ILE LEU GLU GLN ILE VAL SER VAL GLY SEQRES 17 B 378 LYS HIS VAL LYS GLY TYR HIS TYR ILE ILE ALA ASN LEU SEQRES 18 B 378 GLY PHE LYS ASP ILE SER LEU GLU ARG PHE ILE HIS GLY SEQRES 19 B 378 GLY ALA ASN VAL THR GLY PHE GLN LEU VAL ASP PHE ASN SEQRES 20 B 378 THR PRO MET VAL THR LYS LEU MET ASP ARG TRP LYS LYS SEQRES 21 B 378 LEU ASP GLN ARG GLU TYR PRO GLY SER GLU THR PRO PRO SEQRES 22 B 378 LYS TYR THR SER ALA LEU THR TYR ASP GLY VAL LEU VAL SEQRES 23 B 378 MET ALA GLU THR PHE ARG SER LEU ARG ARG GLN LYS ILE SEQRES 24 B 378 ASP ILE SER ARG ARG GLY ASN ALA GLY ASP CYS LEU ALA SEQRES 25 B 378 ASN PRO ALA ALA PRO TRP GLY GLN GLY ILE ASP MET GLU SEQRES 26 B 378 ARG THR LEU LYS GLN VAL ARG ILE GLN GLY LEU THR GLY SEQRES 27 B 378 ASN VAL GLN PHE ASP HIS TYR GLY ARG ARG VAL ASN TYR SEQRES 28 B 378 THR MET ASP VAL PHE GLU LEU LYS SER THR GLY PRO ARG SEQRES 29 B 378 LYS VAL GLY TYR TRP ASN ASP MET ASP LYS LEU VAL LEU SEQRES 30 B 378 ILE SEQRES 1 C 373 ALA ASN PHE PRO ASN ASN ILE GLN ILE GLY GLY LEU PHE SEQRES 2 C 373 PRO ASN GLN GLN SER GLN GLU HIS ALA ALA PHE ARG PHE SEQRES 3 C 373 ALA LEU SER GLN LEU THR GLU PRO PRO LYS LEU LEU PRO SEQRES 4 C 373 GLN ILE ASP ILE VAL ASN ILE SER ASP SER PHE GLU MET SEQRES 5 C 373 THR TYR ARG PHE CYS SER GLN PHE SER LYS GLY VAL TYR SEQRES 6 C 373 ALA ILE PHE GLY PHE TYR GLU ARG ARG THR VAL ASN MET SEQRES 7 C 373 LEU THR SER PHE CYS GLY ALA LEU HIS VAL CYS PHE ILE SEQRES 8 C 373 THR PRO SER PHE PRO VAL ASP THR SER ASN GLN PHE VAL SEQRES 9 C 373 LEU GLN LEU ARG PRO GLU LEU GLN GLU ALA LEU ILE SER SEQRES 10 C 373 ILE ILE ASP HIS TYR LYS TRP GLN THR PHE VAL TYR ILE SEQRES 11 C 373 TYR ASP ALA ASP ARG GLY LEU SER VAL LEU GLN ARG VAL SEQRES 12 C 373 LEU ASP THR ALA ALA GLU LYS ASN TRP GLN VAL THR ALA SEQRES 13 C 373 VAL ASN ILE LEU THR THR THR GLU GLU GLY TYR ARG MET SEQRES 14 C 373 LEU PHE GLN ASP LEU GLU LYS LYS LYS GLU ARG LEU VAL SEQRES 15 C 373 VAL VAL ASP CYS GLU SER GLU ARG LEU ASN ALA ILE LEU SEQRES 16 C 373 GLY GLN ILE VAL LYS LEU GLU LYS ASN GLY ILE GLY TYR SEQRES 17 C 373 HIS TYR ILE LEU ALA ASN LEU GLY PHE MET ASP ILE ASP SEQRES 18 C 373 LEU ASN LYS PHE LYS GLU SER GLY ALA ASN VAL THR GLY SEQRES 19 C 373 PHE GLN LEU VAL ASN TYR THR ASP THR ILE PRO ALA ARG SEQRES 20 C 373 ILE MET GLN GLN TRP ARG THR SER ASP SER ARG ASP HIS SEQRES 21 C 373 THR ARG VAL ASP TRP LYS ARG PRO LYS TYR THR SER ALA SEQRES 22 C 373 LEU THR TYR ASP GLY VAL LYS VAL MET ALA GLU ALA PHE SEQRES 23 C 373 GLN SER LEU ARG ARG GLN ARG ILE ASP ILE SER ARG ARG SEQRES 24 C 373 GLY ASN ALA GLY ASP CYS LEU ALA ASN PRO ALA VAL PRO SEQRES 25 C 373 TRP GLY GLN GLY ILE ASP ILE GLN ARG ALA LEU GLN GLN SEQRES 26 C 373 VAL ARG PHE GLU GLY LEU THR GLY ASN VAL GLN PHE ASN SEQRES 27 C 373 GLU LYS GLY ARG ARG THR ASN TYR THR LEU HIS VAL ILE SEQRES 28 C 373 GLU MET LYS HIS ASP GLY ILE ARG LYS ILE GLY TYR TRP SEQRES 29 C 373 ASN GLU ASP ASP LYS PHE VAL PRO ALA SEQRES 1 D 378 ALA PHE PRO SER SER VAL GLN ILE GLY GLY LEU PHE ILE SEQRES 2 D 378 ARG ASN THR ASP GLN GLU TYR THR ALA PHE ARG LEU ALA SEQRES 3 D 378 ILE PHE LEU HIS ASN THR SER PRO ASN ALA SER GLU ALA SEQRES 4 D 378 PRO PHE ASN LEU VAL PRO HIS VAL ASP ASN ILE GLU THR SEQRES 5 D 378 ALA ASN SER PHE ALA VAL THR ASN ALA PHE CYS SER GLN SEQRES 6 D 378 TYR SER ARG GLY VAL PHE ALA ILE PHE GLY LEU TYR ASP SEQRES 7 D 378 LYS ARG SER VAL HIS THR LEU THR SER PHE CYS SER ALA SEQRES 8 D 378 LEU HIS ILE SER LEU ILE THR PRO SER PHE PRO THR GLU SEQRES 9 D 378 GLY GLU SER GLN PHE VAL LEU GLN LEU ARG PRO SER LEU SEQRES 10 D 378 ARG GLY ALA LEU LEU SER LEU LEU ASP HIS TYR GLU TRP SEQRES 11 D 378 ASN CYS PHE VAL PHE LEU TYR ASP THR ASP ARG GLY TYR SEQRES 12 D 378 SER ILE LEU GLN ALA ILE MET GLU LYS ALA GLY GLN ASN SEQRES 13 D 378 GLY TRP HIS VAL SER ALA ILE CYS VAL GLU ASN PHE ASN SEQRES 14 D 378 ASP VAL SER TYR ARG GLN LEU LEU GLU GLU LEU ASP ARG SEQRES 15 D 378 ARG GLN GLU LYS LYS PHE VAL ILE ASP CYS GLU ILE GLU SEQRES 16 D 378 ARG LEU GLN ASN ILE LEU GLU GLN ILE VAL SER VAL GLY SEQRES 17 D 378 LYS HIS VAL LYS GLY TYR HIS TYR ILE ILE ALA ASN LEU SEQRES 18 D 378 GLY PHE LYS ASP ILE SER LEU GLU ARG PHE ILE HIS GLY SEQRES 19 D 378 GLY ALA ASN VAL THR GLY PHE GLN LEU VAL ASP PHE ASN SEQRES 20 D 378 THR PRO MET VAL THR LYS LEU MET ASP ARG TRP LYS LYS SEQRES 21 D 378 LEU ASP GLN ARG GLU TYR PRO GLY SER GLU THR PRO PRO SEQRES 22 D 378 LYS TYR THR SER ALA LEU THR TYR ASP GLY VAL LEU VAL SEQRES 23 D 378 MET ALA GLU THR PHE ARG SER LEU ARG ARG GLN LYS ILE SEQRES 24 D 378 ASP ILE SER ARG ARG GLY ASN ALA GLY ASP CYS LEU ALA SEQRES 25 D 378 ASN PRO ALA ALA PRO TRP GLY GLN GLY ILE ASP MET GLU SEQRES 26 D 378 ARG THR LEU LYS GLN VAL ARG ILE GLN GLY LEU THR GLY SEQRES 27 D 378 ASN VAL GLN PHE ASP HIS TYR GLY ARG ARG VAL ASN TYR SEQRES 28 D 378 THR MET ASP VAL PHE GLU LEU LYS SER THR GLY PRO ARG SEQRES 29 D 378 LYS VAL GLY TYR TRP ASN ASP MET ASP LYS LEU VAL LEU SEQRES 30 D 378 ILE SEQRES 1 E 257 GLU VAL LYS LEU LEU GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 E 257 PRO GLY GLY SER LEU LYS LEU SER CYS ALA ALA SER GLY SEQRES 3 E 257 PHE ASP PHE SER GLU TYR TRP MET SER TRP VAL ARG GLN SEQRES 4 E 257 ALA PRO GLY LYS GLY LEU GLU TRP ILE GLY GLU ILE ASN SEQRES 5 E 257 PRO ASP SER SER SER ILE ASP TYR THR PRO SER LEU LYS SEQRES 6 E 257 ASP LYS ILE ILE ILE SER ARG ASP ASN ALA LYS LYS THR SEQRES 7 E 257 LEU TYR LEU GLN LEU SER LYS VAL ARG SER GLU ASP THR SEQRES 8 E 257 ALA LEU TYR TYR CYS ALA ARG PRO ARG GLY ASN TYR VAL SEQRES 9 E 257 VAL MET ASP TYR TRP GLY GLN GLY THR SER VAL THR VAL SEQRES 10 E 257 SER SER SER GLY GLY GLY GLY SER GLY GLY GLY GLY SER SEQRES 11 E 257 GLY GLY GLY GLY ASN ILE VAL LEU THR GLN SER PRO ALA SEQRES 12 E 257 SER LEU ALA VAL SER LEU GLY GLN ARG ALA THR ILE SER SEQRES 13 E 257 CYS ARG ALA SER GLU SER VAL ASP SER TYR GLY SER SER SEQRES 14 E 257 PHE VAL HIS TRP TYR GLN GLN LYS PRO GLY GLN PRO PRO SEQRES 15 E 257 LYS LEU LEU ILE PHE LEU ALA SER LYS LEU GLU SER GLY SEQRES 16 E 257 VAL PRO ALA ARG PHE SER GLY SER GLY SER ARG THR ASP SEQRES 17 E 257 PHE THR LEU THR ILE ASP PRO VAL GLU ALA ASP ASP ALA SEQRES 18 E 257 ALA THR TYR TYR CYS GLN GLN THR ASN GLU ASP PRO TYR SEQRES 19 E 257 THR PHE GLY GLY GLY THR LYS LEU GLU ILE LYS ARG ALA SEQRES 20 E 257 SER ASN TRP SER HIS PRO GLN PHE GLU LYS SEQRES 1 F 257 GLU VAL LYS LEU LEU GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 F 257 PRO GLY GLY SER LEU LYS LEU SER CYS ALA ALA SER GLY SEQRES 3 F 257 PHE ASP PHE SER GLU TYR TRP MET SER TRP VAL ARG GLN SEQRES 4 F 257 ALA PRO GLY LYS GLY LEU GLU TRP ILE GLY GLU ILE ASN SEQRES 5 F 257 PRO ASP SER SER SER ILE ASP TYR THR PRO SER LEU LYS SEQRES 6 F 257 ASP LYS ILE ILE ILE SER ARG ASP ASN ALA LYS LYS THR SEQRES 7 F 257 LEU TYR LEU GLN LEU SER LYS VAL ARG SER GLU ASP THR SEQRES 8 F 257 ALA LEU TYR TYR CYS ALA ARG PRO ARG GLY ASN TYR VAL SEQRES 9 F 257 VAL MET ASP TYR TRP GLY GLN GLY THR SER VAL THR VAL SEQRES 10 F 257 SER SER SER GLY GLY GLY GLY SER GLY GLY GLY GLY SER SEQRES 11 F 257 GLY GLY GLY GLY ASN ILE VAL LEU THR GLN SER PRO ALA SEQRES 12 F 257 SER LEU ALA VAL SER LEU GLY GLN ARG ALA THR ILE SER SEQRES 13 F 257 CYS ARG ALA SER GLU SER VAL ASP SER TYR GLY SER SER SEQRES 14 F 257 PHE VAL HIS TRP TYR GLN GLN LYS PRO GLY GLN PRO PRO SEQRES 15 F 257 LYS LEU LEU ILE PHE LEU ALA SER LYS LEU GLU SER GLY SEQRES 16 F 257 VAL PRO ALA ARG PHE SER GLY SER GLY SER ARG THR ASP SEQRES 17 F 257 PHE THR LEU THR ILE ASP PRO VAL GLU ALA ASP ASP ALA SEQRES 18 F 257 ALA THR TYR TYR CYS GLN GLN THR ASN GLU ASP PRO TYR SEQRES 19 F 257 THR PHE GLY GLY GLY THR LYS LEU GLU ILE LYS ARG ALA SEQRES 20 F 257 SER ASN TRP SER HIS PRO GLN PHE GLU LYS HET NAG I 1 14 HET NAG I 2 14 HET BMA I 3 11 HET NAG J 1 14 HET NAG J 2 14 HET BMA J 3 11 HET NAG N 1 14 HET NAG N 2 14 HET NAG G 1 14 HET NAG G 2 14 HET NAG H 1 14 HET NAG H 2 14 HET NAG K 1 14 HET NAG K 2 14 HET NAG L 1 14 HET NAG L 2 14 HET NAG M 1 14 HET NAG M 2 14 HET NAG A 401 14 HET NAG B 401 14 HET NAG C 401 14 HET NAG D 401 14 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BMA BETA-D-MANNOPYRANOSE 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 BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE FORMUL 7 NAG 20(C8 H15 N O6) FORMUL 7 BMA 2(C6 H12 O6) HELIX 1 AA1 SER A 18 GLN A 30 1 13 HELIX 2 AA2 ASP A 48 GLY A 63 1 16 HELIX 3 AA3 THR A 75 HIS A 87 1 13 HELIX 4 AA4 GLU A 113 TYR A 122 1 10 HELIX 5 AA5 ALA A 133 GLY A 136 5 4 HELIX 6 AA6 LEU A 137 ASN A 151 1 15 HELIX 7 AA7 THR A 163 GLU A 175 1 13 HELIX 8 AA8 GLU A 187 LEU A 201 1 15 HELIX 9 AA9 ASN A 223 GLU A 227 5 5 HELIX 10 AB1 ASP A 242 THR A 254 1 13 HELIX 11 AB2 LYS A 269 GLN A 292 1 24 HELIX 12 AB3 GLN A 315 LEU A 323 1 9 HELIX 13 AB4 THR B 17 THR B 33 1 17 HELIX 14 AB5 ASN B 55 GLY B 70 1 16 HELIX 15 AB6 ASP B 79 ARG B 81 5 3 HELIX 16 AB7 SER B 82 LEU B 93 1 12 HELIX 17 AB8 LEU B 118 TYR B 129 1 12 HELIX 18 AB9 TYR B 144 GLY B 158 1 15 HELIX 19 AC1 ASN B 170 ARG B 184 1 15 HELIX 20 AC2 GLU B 194 GLY B 209 1 16 HELIX 21 AC3 GLU B 230 GLY B 236 1 7 HELIX 22 AC4 THR B 249 LYS B 261 1 13 HELIX 23 AC5 LYS B 275 GLN B 298 1 24 HELIX 24 AC6 GLN B 321 LYS B 330 1 10 HELIX 25 AC7 SER C 18 GLN C 30 1 13 HELIX 26 AC8 ASP C 48 GLY C 63 1 16 HELIX 27 AC9 THR C 75 LEU C 86 1 12 HELIX 28 AD1 GLU C 113 TYR C 122 1 10 HELIX 29 AD2 ALA C 133 GLY C 136 5 4 HELIX 30 AD3 LEU C 137 ASN C 151 1 15 HELIX 31 AD4 THR C 163 LYS C 176 1 14 HELIX 32 AD5 GLU C 187 GLU C 202 1 16 HELIX 33 AD6 ASN C 223 GLU C 227 5 5 HELIX 34 AD7 ASP C 242 SER C 255 1 14 HELIX 35 AD8 LYS C 269 GLN C 292 1 24 HELIX 36 AD9 GLN C 315 GLN C 324 1 10 HELIX 37 AE1 THR D 17 THR D 33 1 17 HELIX 38 AE2 ASN D 36 ALA D 40 5 5 HELIX 39 AE3 ASN D 55 GLY D 70 1 16 HELIX 40 AE4 ASP D 79 ARG D 81 5 3 HELIX 41 AE5 SER D 82 SER D 91 1 10 HELIX 42 AE6 LEU D 118 TYR D 129 1 12 HELIX 43 AE7 TYR D 144 GLY D 158 1 15 HELIX 44 AE8 ASN D 170 ARG D 184 1 15 HELIX 45 AE9 GLU D 194 GLY D 209 1 16 HELIX 46 AF1 GLU D 230 GLY D 236 1 7 HELIX 47 AF2 THR D 249 LEU D 262 1 14 HELIX 48 AF3 LYS D 275 GLN D 298 1 24 HELIX 49 AF4 GLN D 321 LYS D 330 1 10 HELIX 50 AF5 GLU E 217 ALA E 221 5 5 HELIX 51 AF6 GLU F 217 ALA F 221 5 5 SHEET 1 AA1 5 LYS A 36 ILE A 43 0 SHEET 2 AA1 5 ASN A 6 PHE A 13 1 N ILE A 9 O LEU A 38 SHEET 3 AA1 5 ALA A 66 GLY A 69 1 O PHE A 68 N GLY A 10 SHEET 4 AA1 5 CYS A 89 THR A 92 1 O ILE A 91 N ILE A 67 SHEET 5 AA1 5 VAL A 104 GLN A 106 1 O LEU A 105 N THR A 92 SHEET 1 AA2 4 GLN A 153 ASN A 158 0 SHEET 2 AA2 4 THR A 126 TYR A 131 1 N TYR A 129 O VAL A 157 SHEET 3 AA2 4 LEU A 181 ASP A 185 1 O VAL A 183 N ILE A 130 SHEET 4 AA2 4 HIS A 209 LEU A 212 1 O ILE A 211 N VAL A 184 SHEET 1 AA3 4 VAL A 232 GLN A 236 0 SHEET 2 AA3 4 LEU A 348 MET A 353 -1 O ILE A 351 N GLY A 234 SHEET 3 AA3 4 LYS A 360 ASN A 365 -1 O GLY A 362 N VAL A 350 SHEET 4 AA3 4 LYS A 369 PRO A 372 -1 O LYS A 369 N ASN A 365 SHEET 1 AA4 2 GLN A 336 PHE A 337 0 SHEET 2 AA4 2 ARG A 343 THR A 344 -1 O THR A 344 N GLN A 336 SHEET 1 AA5 5 VAL B 48 ASN B 50 0 SHEET 2 AA5 5 GLY B 10 PHE B 13 1 N PHE B 13 O ASP B 49 SHEET 3 AA5 5 ALA B 73 PHE B 75 1 O PHE B 75 N LEU B 12 SHEET 4 AA5 5 SER B 96 THR B 99 1 O SER B 96 N ILE B 74 SHEET 5 AA5 5 VAL B 111 GLN B 113 1 O LEU B 112 N THR B 99 SHEET 1 AA6 8 HIS B 160 CYS B 165 0 SHEET 2 AA6 8 CYS B 133 TYR B 138 1 N PHE B 136 O ILE B 164 SHEET 3 AA6 8 LYS B 188 ASP B 192 1 O LYS B 188 N VAL B 135 SHEET 4 AA6 8 HIS B 216 ILE B 219 1 O HIS B 216 N PHE B 189 SHEET 5 AA6 8 ASN B 238 GLN B 243 1 O ASN B 238 N TYR B 217 SHEET 6 AA6 8 THR B 353 LEU B 359 -1 O ASP B 355 N GLN B 243 SHEET 7 AA6 8 ARG B 365 ASN B 371 -1 O GLY B 368 N VAL B 356 SHEET 8 AA6 8 LEU B 376 LEU B 378 -1 O VAL B 377 N TYR B 369 SHEET 1 AA7 3 ILE B 334 GLY B 336 0 SHEET 2 AA7 3 GLY B 339 PHE B 343 -1 O GLY B 339 N GLY B 336 SHEET 3 AA7 3 ARG B 349 VAL B 350 -1 O VAL B 350 N GLN B 342 SHEET 1 AA8 5 LYS C 36 ILE C 43 0 SHEET 2 AA8 5 ASN C 6 PHE C 13 1 N ILE C 9 O LEU C 38 SHEET 3 AA8 5 ALA C 66 GLY C 69 1 O PHE C 68 N LEU C 12 SHEET 4 AA8 5 CYS C 89 THR C 92 1 O ILE C 91 N ILE C 67 SHEET 5 AA8 5 VAL C 104 GLN C 106 1 O LEU C 105 N THR C 92 SHEET 1 AA9 8 GLN C 153 ASN C 158 0 SHEET 2 AA9 8 THR C 126 TYR C 131 1 N PHE C 127 O GLN C 153 SHEET 3 AA9 8 LEU C 181 ASP C 185 1 O VAL C 183 N VAL C 128 SHEET 4 AA9 8 HIS C 209 LEU C 212 1 O ILE C 211 N VAL C 184 SHEET 5 AA9 8 VAL C 232 GLN C 236 1 O THR C 233 N TYR C 210 SHEET 6 AA9 8 THR C 347 MET C 353 -1 O ILE C 351 N GLY C 234 SHEET 7 AA9 8 LYS C 360 ASN C 365 -1 O ILE C 361 N VAL C 350 SHEET 8 AA9 8 LYS C 369 PRO C 372 -1 O VAL C 371 N TYR C 363 SHEET 1 AB1 2 GLU C 329 GLY C 330 0 SHEET 2 AB1 2 GLY C 333 ASN C 334 -1 O GLY C 333 N GLY C 330 SHEET 1 AB2 2 GLN C 336 PHE C 337 0 SHEET 2 AB2 2 ARG C 343 THR C 344 -1 O THR C 344 N GLN C 336 SHEET 1 AB3 2 SER D 6 VAL D 7 0 SHEET 2 AB3 2 ASN D 43 LEU D 44 1 O ASN D 43 N VAL D 7 SHEET 1 AB4 4 GLY D 10 GLY D 11 0 SHEET 2 AB4 4 ALA D 73 PHE D 75 1 O ALA D 73 N GLY D 10 SHEET 3 AB4 4 SER D 96 THR D 99 1 O ILE D 98 N ILE D 74 SHEET 4 AB4 4 VAL D 111 GLN D 113 1 O LEU D 112 N LEU D 97 SHEET 1 AB5 8 HIS D 160 CYS D 165 0 SHEET 2 AB5 8 CYS D 133 TYR D 138 1 N PHE D 136 O ILE D 164 SHEET 3 AB5 8 LYS D 188 ASP D 192 1 O LYS D 188 N VAL D 135 SHEET 4 AB5 8 HIS D 216 ILE D 219 1 O ILE D 218 N ILE D 191 SHEET 5 AB5 8 ASN D 238 GLN D 243 1 O ASN D 238 N TYR D 217 SHEET 6 AB5 8 MET D 354 LYS D 360 -1 O ASP D 355 N GLN D 243 SHEET 7 AB5 8 GLY D 363 TRP D 370 -1 O GLY D 368 N VAL D 356 SHEET 8 AB5 8 LEU D 376 LEU D 378 -1 O VAL D 377 N TYR D 369 SHEET 1 AB6 2 ILE D 334 GLY D 336 0 SHEET 2 AB6 2 GLY D 339 VAL D 341 -1 O VAL D 341 N ILE D 334 SHEET 1 AB7 4 LYS E 3 LEU E 5 0 SHEET 2 AB7 4 LEU E 20 SER E 25 -1 O ALA E 23 N LEU E 5 SHEET 3 AB7 4 THR E 78 LEU E 83 -1 O LEU E 79 N CYS E 22 SHEET 4 AB7 4 ILE E 68 ASP E 73 -1 N SER E 71 O TYR E 80 SHEET 1 AB8 3 LEU E 45 GLU E 50 0 SHEET 2 AB8 3 SER E 35 GLN E 39 -1 N ARG E 38 O GLU E 46 SHEET 3 AB8 3 LEU E 93 ALA E 97 -1 O ALA E 97 N SER E 35 SHEET 1 AB9 3 LEU E 138 SER E 141 0 SHEET 2 AB9 3 ALA E 153 ALA E 159 -1 O SER E 156 N SER E 141 SHEET 3 AB9 3 ASP E 208 ILE E 213 -1 O ILE E 213 N ALA E 153 SHEET 1 AC1 6 SER E 144 VAL E 147 0 SHEET 2 AC1 6 THR E 240 ILE E 244 1 O GLU E 243 N LEU E 145 SHEET 3 AC1 6 ALA E 222 GLN E 228 -1 N ALA E 222 O LEU E 242 SHEET 4 AC1 6 VAL E 171 GLN E 176 -1 N HIS E 172 O GLN E 227 SHEET 5 AC1 6 LYS E 183 PHE E 187 -1 O ILE E 186 N TRP E 173 SHEET 6 AC1 6 LYS E 191 LEU E 192 -1 O LYS E 191 N PHE E 187 SHEET 1 AC2 4 LYS F 3 GLU F 6 0 SHEET 2 AC2 4 LEU F 20 SER F 25 -1 O ALA F 23 N LEU F 5 SHEET 3 AC2 4 THR F 78 LEU F 83 -1 O LEU F 79 N CYS F 22 SHEET 4 AC2 4 ILE F 68 ASP F 73 -1 N SER F 71 O TYR F 80 SHEET 1 AC3 3 LEU F 45 GLU F 50 0 SHEET 2 AC3 3 SER F 35 GLN F 39 -1 N ARG F 38 O GLU F 46 SHEET 3 AC3 3 LEU F 93 ALA F 97 -1 O ALA F 97 N SER F 35 SHEET 1 AC4 3 LEU F 138 SER F 141 0 SHEET 2 AC4 3 ALA F 153 ALA F 159 -1 O SER F 156 N SER F 141 SHEET 3 AC4 3 PHE F 209 ILE F 213 -1 O ILE F 213 N ALA F 153 SHEET 1 AC5 6 SER F 144 VAL F 147 0 SHEET 2 AC5 6 THR F 240 ILE F 244 1 O GLU F 243 N LEU F 145 SHEET 3 AC5 6 THR F 223 GLN F 228 -1 N TYR F 224 O THR F 240 SHEET 4 AC5 6 VAL F 171 GLN F 176 -1 N TYR F 174 O TYR F 225 SHEET 5 AC5 6 LYS F 183 PHE F 187 -1 O ILE F 186 N TRP F 173 SHEET 6 AC5 6 LYS F 191 LEU F 192 -1 O LYS F 191 N PHE F 187 SSBOND 1 CYS A 57 CYS A 305 1555 1555 2.03 SSBOND 2 CYS B 64 CYS B 311 1555 1555 2.03 SSBOND 3 CYS C 57 CYS C 305 1555 1555 2.03 SSBOND 4 CYS D 64 CYS D 311 1555 1555 2.03 LINK ND2 ASN A 45 C1 NAG I 1 1555 1555 1.45 LINK ND2 ASN A 231 C1 NAG K 1 1555 1555 1.44 LINK ND2 ASN B 238 C1 NAG B 401 1555 1555 1.44 LINK ND2 ASN B 351 C1 NAG G 1 1555 1555 1.44 LINK ND2 ASN C 45 C1 NAG J 1 1555 1555 1.45 LINK ND2 ASN C 231 C1 NAG L 1 1555 1555 1.44 LINK ND2 ASN C 239 C1 NAG C 401 1555 1555 1.44 LINK ND2 ASN D 238 C1 NAG D 401 1555 1555 1.44 LINK ND2 ASN D 351 C1 NAG N 1 1555 1555 1.44 LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.45 LINK O4 NAG I 2 C1 BMA I 3 1555 1555 1.45 LINK O4 NAG J 1 C1 NAG J 2 1555 1555 1.45 LINK O4 NAG J 2 C1 BMA J 3 1555 1555 1.45 LINK O4 NAG N 1 C1 NAG N 2 1555 1555 1.45 LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.45 LINK O4 NAG H 1 C1 NAG H 2 1555 1555 1.44 LINK O4 NAG K 1 C1 NAG K 2 1555 1555 1.45 LINK O4 NAG L 1 C1 NAG L 2 1555 1555 1.45 LINK O4 NAG M 1 C1 NAG M 2 1555 1555 1.44 CISPEP 1 SER E 141 PRO E 142 0 -4.23 CISPEP 2 ASP E 214 PRO E 215 0 1.66 CISPEP 3 ASP E 232 PRO E 233 0 0.19 CISPEP 4 SER F 141 PRO F 142 0 -3.36 CISPEP 5 ASP F 214 PRO F 215 0 2.83 CISPEP 6 ASP F 232 PRO F 233 0 0.39 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