HEADER VIRAL PROTEIN/IMMUNE SYSTEM 14-MAR-24 9B2C TITLE STRUCTURE OF THE PORCINE DELTACORONAVIRUS (PDCOV) RECEPTOR-BINDING TITLE 2 DOMAIN BOUND TO THE PD33 ANTIBODY FAB FRAGMENT AND THE KAPPA LIGHT TITLE 3 CHAIN NANOBODY COMPND MOL_ID: 1; COMPND 2 MOLECULE: SPIKE GLYCOPROTEIN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: RECEPTOR-BINDING DOMAIN (UNP RESIDUES 303-416); COMPND 5 SYNONYM: SPIKE PROTEIN; COMPND 6 ENGINEERED: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: PD33 FAB KAPPA LIGHT CHAIN; COMPND 9 CHAIN: L; COMPND 10 ENGINEERED: YES; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: KAPPA LIGHT CHAIN NANOBODY; COMPND 13 CHAIN: N; COMPND 14 ENGINEERED: YES; COMPND 15 MOL_ID: 4; COMPND 16 MOLECULE: PD33 FAB HEAVY CHAIN; COMPND 17 CHAIN: H; COMPND 18 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: PORCINE DELTACORONAVIRUS; SOURCE 3 ORGANISM_TAXID: 1586324; SOURCE 4 STRAIN: ILLINOIS STRAIN IL121_2014; 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: MUS SP.; SOURCE 10 ORGANISM_TAXID: 10095; SOURCE 11 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 12 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 13 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 14 MOL_ID: 3; SOURCE 15 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 16 ORGANISM_COMMON: LLAMA; SOURCE 17 ORGANISM_TAXID: 9844; 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: MUS SP.; SOURCE 23 ORGANISM_TAXID: 10095; SOURCE 24 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 25 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 26 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS SPIKE GLYCOPROTEIN, FUSION PROTEIN, STRUCTURAL GENOMICS, SEATTLE KEYWDS 2 STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE, SSGCID, VIRAL KEYWDS 3 NEUTRALIZATION, INHIBITOR, VIRAL PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR Y.J.PARK,SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE AUTHOR 2 (SSGCID),D.VEESLER REVDAT 1 13-NOV-24 9B2C 0 JRNL AUTH M.REXHEPAJ,D.ASARNOW,L.PERRUZZA,Y.J.PARK,B.GUARINO, JRNL AUTH 2 M.MCCALLUM,K.CULAP,C.SALIBA,G.LEONI,A.BALMELLI, JRNL AUTH 3 C.N.YOSHIYAMA,M.S.DICKINSON,J.QUISPE,J.T.BROWN, JRNL AUTH 4 M.A.TORTORICI,K.R.SPROUSE,A.L.TAYLOR,D.CORTI,T.N.STARR, JRNL AUTH 5 F.BENIGNI,D.VEESLER JRNL TITL ISOLATION AND ESCAPE MAPPING OF BROADLY NEUTRALIZING JRNL TITL 2 ANTIBODIES AGAINST EMERGING DELTA-CORONAVIRUSES. JRNL REF IMMUNITY 2024 JRNL REFN ISSN 1074-7613 JRNL PMID 39488210 JRNL DOI 10.1016/J.IMMUNI.2024.10.001 REMARK 2 REMARK 2 RESOLUTION. 3.00 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : LEGINON, CRYOSPARC REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : NULL REMARK 3 REFINEMENT SPACE : NULL REMARK 3 REFINEMENT PROTOCOL : NULL REMARK 3 REFINEMENT TARGET : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL REMARK 3 REMARK 3 FITTING PROCEDURE : NULL REMARK 3 REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 3.000 REMARK 3 NUMBER OF PARTICLES : 564616 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 9B2C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-MAR-24. REMARK 100 THE DEPOSITION ID IS D_1000282507. 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 : PORCINE DELTACORONAVIRUS REMARK 245 (PDCOV) RECEPTOR-BINDING DOMAIN REMARK 245 BOUND TO THE PD33 ANTIBODY FAB REMARK 245 FRAGMENT AND THE KAPPA LIGHT REMARK 245 CHAIN NANOBODY 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 : 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 : FEI TITAN KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 (6K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 200.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 3000.00 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) : 5800.00 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: TETRAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, L, N, H, B 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 271 REMARK 465 GLY A 272 REMARK 465 ILE A 273 REMARK 465 LEU A 274 REMARK 465 PRO A 275 REMARK 465 SER A 276 REMARK 465 PRO A 277 REMARK 465 GLY A 278 REMARK 465 MET A 279 REMARK 465 PRO A 280 REMARK 465 ALA A 281 REMARK 465 LEU A 282 REMARK 465 LEU A 283 REMARK 465 SER A 284 REMARK 465 LEU A 285 REMARK 465 VAL A 286 REMARK 465 SER A 287 REMARK 465 LEU A 288 REMARK 465 LEU A 289 REMARK 465 SER A 290 REMARK 465 VAL A 291 REMARK 465 LEU A 292 REMARK 465 LEU A 293 REMARK 465 MET A 294 REMARK 465 GLY A 295 REMARK 465 CYS A 296 REMARK 465 VAL A 297 REMARK 465 ALA A 298 REMARK 465 GLU A 299 REMARK 465 THR A 300 REMARK 465 GLY A 301 REMARK 465 THR A 302 REMARK 465 PRO A 303 REMARK 465 GLU A 304 REMARK 465 LEU A 305 REMARK 465 GLU A 306 REMARK 465 LEU A 417 REMARK 465 VAL A 418 REMARK 465 PRO A 419 REMARK 465 ARG A 420 REMARK 465 GLY A 421 REMARK 465 SER A 422 REMARK 465 GLY A 423 REMARK 465 GLY A 424 REMARK 465 SER A 425 REMARK 465 HIS A 426 REMARK 465 HIS A 427 REMARK 465 HIS A 428 REMARK 465 HIS A 429 REMARK 465 HIS A 430 REMARK 465 HIS A 431 REMARK 465 HIS A 432 REMARK 465 HIS A 433 REMARK 465 ASP L 1 REMARK 465 GLU L 218 REMARK 465 CYS L 219 REMARK 465 MET N -24 REMARK 465 LYS N -23 REMARK 465 LYS N -22 REMARK 465 THR N -21 REMARK 465 ALA N -20 REMARK 465 ILE N -19 REMARK 465 ALA N -18 REMARK 465 ILE N -17 REMARK 465 ALA N -16 REMARK 465 VAL N -15 REMARK 465 ALA N -14 REMARK 465 LEU N -13 REMARK 465 ALA N -12 REMARK 465 GLY N -11 REMARK 465 PHE N -10 REMARK 465 ALA N -9 REMARK 465 THR N -8 REMARK 465 VAL N -7 REMARK 465 ALA N -6 REMARK 465 GLN N -5 REMARK 465 ALA N -4 REMARK 465 ALA N -3 REMARK 465 PRO N -2 REMARK 465 MET N -1 REMARK 465 GLY N 0 REMARK 465 SER N 1 REMARK 465 SER N 121 REMARK 465 SER N 122 REMARK 465 HIS N 123 REMARK 465 HIS N 124 REMARK 465 HIS N 125 REMARK 465 HIS N 126 REMARK 465 HIS N 127 REMARK 465 HIS N 128 REMARK 465 HIS N 129 REMARK 465 HIS N 130 REMARK 465 GLU N 131 REMARK 465 PRO N 132 REMARK 465 GLU N 133 REMARK 465 ALA N 134 REMARK 465 SER H 134 REMARK 465 LYS H 135 REMARK 465 SER H 136 REMARK 465 THR H 137 REMARK 465 SER H 138 REMARK 465 GLY H 139 REMARK 465 GLY H 140 REMARK 465 LYS H 220 REMARK 465 SER H 221 REMARK 465 CYS H 222 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 SER A 313 OG REMARK 470 ASP A 317 CG OD1 OD2 REMARK 470 ASP A 324 CG OD1 OD2 REMARK 470 SER A 325 OG REMARK 470 THR A 327 OG1 CG2 REMARK 470 ASN A 329 CG OD1 ND2 REMARK 470 THR A 332 OG1 CG2 REMARK 470 SER A 333 OG REMARK 470 VAL A 336 CG1 CG2 REMARK 470 THR A 337 OG1 CG2 REMARK 470 LYS A 338 CG CD CE NZ REMARK 470 TYR A 340 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ARG A 342 CG CD NE CZ NH1 NH2 REMARK 470 GLU A 344 CG CD OE1 OE2 REMARK 470 THR A 345 OG1 CG2 REMARK 470 MET A 348 CG SD CE REMARK 470 THR A 350 OG1 CG2 REMARK 470 THR A 353 OG1 CG2 REMARK 470 THR A 358 OG1 CG2 REMARK 470 THR A 360 OG1 CG2 REMARK 470 SER A 362 OG REMARK 470 ASP A 364 CG OD1 OD2 REMARK 470 SER A 366 OG REMARK 470 ASN A 369 CG OD1 ND2 REMARK 470 ASN A 370 CG OD1 ND2 REMARK 470 SER A 373 OG REMARK 470 SER A 375 OG REMARK 470 GLN A 376 CG CD OE1 NE2 REMARK 470 SER A 380 OG REMARK 470 THR A 381 OG1 CG2 REMARK 470 GLU A 382 CG CD OE1 OE2 REMARK 470 SER A 383 OG REMARK 470 GLU A 387 CG CD OE1 OE2 REMARK 470 THR A 407 OG1 CG2 REMARK 470 GLU A 410 CG CD OE1 OE2 REMARK 470 GLN A 412 CG CD OE1 NE2 REMARK 470 THR A 413 OG1 CG2 REMARK 470 THR A 415 OG1 CG2 REMARK 470 VAL L 3 CG1 CG2 REMARK 470 THR L 5 OG1 CG2 REMARK 470 SER L 7 OG REMARK 470 LEU L 9 CG CD1 CD2 REMARK 470 SER L 10 OG REMARK 470 THR L 14 OG1 CG2 REMARK 470 SER L 20 OG REMARK 470 SER L 22 OG REMARK 470 ARG L 24 CG CD NE CZ NH1 NH2 REMARK 470 SER L 25 OG REMARK 470 SER L 26 OG REMARK 470 SER L 28 OG REMARK 470 SER L 32 OG REMARK 470 SER L 48 OG REMARK 470 SER L 57 OG REMARK 470 ASP L 60 CG OD1 OD2 REMARK 470 SER L 61 OG REMARK 470 ASP L 65 CG OD1 OD2 REMARK 470 SER L 68 OG REMARK 470 SER L 70 OG REMARK 470 SER L 72 OG REMARK 470 THR L 74 OG1 CG2 REMARK 470 ASP L 75 CG OD1 OD2 REMARK 470 THR L 77 OG1 CG2 REMARK 470 SER L 81 OG REMARK 470 ARG L 82 CG CD NE CZ NH1 NH2 REMARK 470 GLU L 84 CG CD OE1 OE2 REMARK 470 GLU L 86 CG CD OE1 OE2 REMARK 470 LYS L 108 CG CD CE NZ REMARK 470 SER L 119 OG REMARK 470 SER L 126 OG REMARK 470 ASP L 127 CG OD1 OD2 REMARK 470 GLU L 128 CG CD OE1 OE2 REMARK 470 LYS L 131 CG CD CE NZ REMARK 470 SER L 132 OG REMARK 470 THR L 134 OG1 CG2 REMARK 470 SER L 136 OG REMARK 470 LYS L 154 CG CD CE NZ REMARK 470 ASP L 156 CG OD1 OD2 REMARK 470 ASN L 157 CG OD1 ND2 REMARK 470 SER L 161 OG REMARK 470 SER L 164 OG REMARK 470 SER L 167 OG REMARK 470 GLU L 170 CG CD OE1 OE2 REMARK 470 SER L 173 OG REMARK 470 LYS L 174 CG CD CE NZ REMARK 470 ASP L 175 CG OD1 OD2 REMARK 470 SER L 179 OG REMARK 470 SER L 181 OG REMARK 470 SER L 182 OG REMARK 470 THR L 183 OG1 CG2 REMARK 470 THR L 185 OG1 CG2 REMARK 470 SER L 187 OG REMARK 470 LYS L 188 CG CD CE NZ REMARK 470 ASP L 190 CG OD1 OD2 REMARK 470 GLU L 192 CG CD OE1 OE2 REMARK 470 LYS L 193 CG CD CE NZ REMARK 470 LYS L 195 CG CD CE NZ REMARK 470 VAL L 196 CG1 CG2 REMARK 470 SER L 207 OG REMARK 470 SER L 208 OG REMARK 470 THR L 211 OG1 CG2 REMARK 470 SER L 213 OG REMARK 470 ASN L 215 CG OD1 ND2 REMARK 470 GLN N 2 CG CD OE1 NE2 REMARK 470 VAL N 3 CG1 CG2 REMARK 470 GLN N 4 CG CD OE1 NE2 REMARK 470 GLN N 6 CG CD OE1 NE2 REMARK 470 GLU N 7 CG CD OE1 OE2 REMARK 470 SER N 8 OG REMARK 470 LEU N 12 CG CD1 CD2 REMARK 470 GLN N 14 CG CD OE1 NE2 REMARK 470 SER N 18 OG REMARK 470 LEU N 19 CG CD1 CD2 REMARK 470 SER N 22 OG REMARK 470 SER N 26 OG REMARK 470 ARG N 28 CG CD NE CZ NH1 NH2 REMARK 470 THR N 29 OG1 CG2 REMARK 470 SER N 31 OG REMARK 470 ARG N 32 CG CD NE CZ NH1 NH2 REMARK 470 SER N 36 OG REMARK 470 GLN N 40 CG CD OE1 NE2 REMARK 470 LYS N 44 CG CD CE NZ REMARK 470 GLU N 45 CG CD OE1 OE2 REMARK 470 GLU N 47 CG CD OE1 OE2 REMARK 470 ARG N 54 CG CD NE CZ NH1 NH2 REMARK 470 SER N 55 OG REMARK 470 ASP N 57 CG OD1 OD2 REMARK 470 ASP N 63 CG OD1 OD2 REMARK 470 SER N 64 OG REMARK 470 GLN N 66 CG CD OE1 NE2 REMARK 470 THR N 70 OG1 CG2 REMARK 470 SER N 72 OG REMARK 470 ASP N 74 CG OD1 OD2 REMARK 470 ASP N 75 CG OD1 OD2 REMARK 470 LYS N 77 CG CD CE NZ REMARK 470 ASN N 78 CG OD1 ND2 REMARK 470 THR N 79 OG1 CG2 REMARK 470 GLN N 83 CG CD OE1 NE2 REMARK 470 ASN N 85 CG OD1 ND2 REMARK 470 SER N 86 OG REMARK 470 LYS N 88 CG CD CE NZ REMARK 470 GLU N 90 CG CD OE1 OE2 REMARK 470 ASP N 91 CG OD1 OD2 REMARK 470 THR N 92 OG1 CG2 REMARK 470 ASP N 100 CG OD1 OD2 REMARK 470 SER N 101 OG REMARK 470 ASP N 102 CG OD1 OD2 REMARK 470 THR N 103 OG1 CG2 REMARK 470 PHE N 104 CG CD1 CD2 CE1 CE2 CZ REMARK 470 SER N 106 OG REMARK 470 SER N 108 OG REMARK 470 ASP N 110 CG OD1 OD2 REMARK 470 TYR N 111 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 GLN N 114 CG CD OE1 NE2 REMARK 470 THR N 116 OG1 CG2 REMARK 470 GLN N 117 CG CD OE1 NE2 REMARK 470 THR N 119 OG1 CG2 REMARK 470 GLU H 1 CG CD OE1 OE2 REMARK 470 SER H 7 OG REMARK 470 SER H 17 OG REMARK 470 SER H 21 OG REMARK 470 SER H 25 OG REMARK 470 THR H 28 OG1 CG2 REMARK 470 ARG H 43 CG CD NE CZ NH1 NH2 REMARK 470 SER H 49 OG REMARK 470 SER H 55 OG REMARK 470 ASP H 62 CG OD1 OD2 REMARK 470 SER H 63 OG REMARK 470 SER H 71 OG REMARK 470 ASP H 73 CG OD1 OD2 REMARK 470 THR H 75 OG1 CG2 REMARK 470 LYS H 76 CG CD CE NZ REMARK 470 ASN H 77 CG OD1 ND2 REMARK 470 SER H 78 OG REMARK 470 SER H 85 OG REMARK 470 SER H 87 OG REMARK 470 ASP H 107 CG OD1 OD2 REMARK 470 GLN H 111 CG CD OE1 NE2 REMARK 470 THR H 113 OG1 CG2 REMARK 470 THR H 116 OG1 CG2 REMARK 470 SER H 118 OG REMARK 470 SER H 119 OG REMARK 470 SER H 121 OG REMARK 470 THR H 122 OG1 CG2 REMARK 470 SER H 126 OG REMARK 470 SER H 133 OG REMARK 470 THR H 141 OG1 CG2 REMARK 470 ASP H 150 CG OD1 OD2 REMARK 470 THR H 157 OG1 CG2 REMARK 470 SER H 159 OG REMARK 470 SER H 162 OG REMARK 470 THR H 166 OG1 CG2 REMARK 470 SER H 167 OG REMARK 470 SER H 178 OG REMARK 470 SER H 179 OG REMARK 470 SER H 183 OG REMARK 470 SER H 185 OG REMARK 470 SER H 186 OG REMARK 470 THR H 189 OG1 CG2 REMARK 470 SER H 192 OG REMARK 470 SER H 193 OG REMARK 470 SER H 194 OG REMARK 470 THR H 197 OG1 CG2 REMARK 470 THR H 199 OG1 CG2 REMARK 470 ASN H 203 CG OD1 ND2 REMARK 470 ASN H 205 CG OD1 ND2 REMARK 470 LYS H 207 CG CD CE NZ REMARK 470 SER H 209 OG REMARK 470 ASN H 210 CG OD1 ND2 REMARK 470 THR H 211 OG1 CG2 REMARK 470 LYS H 212 CG CD CE NZ REMARK 470 ASP H 214 CG OD1 OD2 REMARK 470 ARG H 216 CG CD NE CZ NH1 NH2 REMARK 470 GLU H 218 CG CD OE1 OE2 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS 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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) 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 RES CSSEQI ATM2 DEVIATION REMARK 500 PRO H 208 CD PRO H 208 N 0.140 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 GLN L 42 CB - CA - C ANGL. DEV. = -12.4 DEGREES REMARK 500 PRO L 64 C - N - CA ANGL. DEV. = 9.0 DEGREES REMARK 500 CYS H 202 CB - CA - C ANGL. DEV. = -13.9 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 ASN A 346 76.06 -118.94 REMARK 500 ASP A 359 -60.02 -145.43 REMARK 500 VAL A 395 -51.83 -157.86 REMARK 500 LEU L 29 32.93 -97.68 REMARK 500 TYR L 54 -117.83 -103.73 REMARK 500 LYS L 55 86.28 -56.46 REMARK 500 VAL L 56 -60.44 67.19 REMARK 500 PRO L 64 -3.46 -47.46 REMARK 500 ALA L 85 -58.78 70.85 REMARK 500 ARG L 113 -158.22 -144.19 REMARK 500 ASN L 143 88.34 37.92 REMARK 500 SER L 161 -113.16 -96.98 REMARK 500 LEU L 186 -142.63 -118.40 REMARK 500 ARG N 53 -165.62 -101.76 REMARK 500 SER H 30 13.72 -67.45 REMARK 500 TYR H 105 -147.71 72.36 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 ARG L 51 0.11 SIDE CHAIN REMARK 500 ARG L 79 0.12 SIDE CHAIN REMARK 500 ARG L 113 0.15 SIDE CHAIN REMARK 500 ARG N 73 0.30 SIDE CHAIN REMARK 500 ARG H 72 0.09 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY REMARK 500 REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 500 I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI ANGLE REMARK 500 SER H 30 -10.53 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-44103 RELATED DB: EMDB REMARK 900 STRUCTURE OF THE PORCINE DELTACORONAVIRUS (PDCOV) RECEPTOR-BINDING REMARK 900 DOMAIN BOUND TO THE PD33 ANTIBODY FAB FRAGMENT AND THE KAPPA LIGHT REMARK 900 CHAIN NANOBODY DBREF1 9B2C A 303 416 UNP A0A1S6L971_9NIDO DBREF2 9B2C A A0A1S6L971 303 416 DBREF 9B2C L 1 219 PDB 9B2C 9B2C 1 219 DBREF 9B2C N -24 134 PDB 9B2C 9B2C -24 134 DBREF 9B2C H 1 222 PDB 9B2C 9B2C 1 222 SEQADV 9B2C MET A 271 UNP A0A1S6L97 EXPRESSION TAG SEQADV 9B2C GLY A 272 UNP A0A1S6L97 EXPRESSION TAG SEQADV 9B2C ILE A 273 UNP A0A1S6L97 EXPRESSION TAG SEQADV 9B2C LEU A 274 UNP A0A1S6L97 EXPRESSION TAG SEQADV 9B2C PRO A 275 UNP A0A1S6L97 EXPRESSION TAG SEQADV 9B2C SER A 276 UNP A0A1S6L97 EXPRESSION TAG SEQADV 9B2C PRO A 277 UNP A0A1S6L97 EXPRESSION TAG SEQADV 9B2C GLY A 278 UNP A0A1S6L97 EXPRESSION TAG SEQADV 9B2C MET A 279 UNP A0A1S6L97 EXPRESSION TAG SEQADV 9B2C PRO A 280 UNP A0A1S6L97 EXPRESSION TAG SEQADV 9B2C ALA A 281 UNP A0A1S6L97 EXPRESSION TAG SEQADV 9B2C LEU A 282 UNP A0A1S6L97 EXPRESSION TAG SEQADV 9B2C LEU A 283 UNP A0A1S6L97 EXPRESSION TAG SEQADV 9B2C SER A 284 UNP A0A1S6L97 EXPRESSION TAG SEQADV 9B2C LEU A 285 UNP A0A1S6L97 EXPRESSION TAG SEQADV 9B2C VAL A 286 UNP A0A1S6L97 EXPRESSION TAG SEQADV 9B2C SER A 287 UNP A0A1S6L97 EXPRESSION TAG SEQADV 9B2C LEU A 288 UNP A0A1S6L97 EXPRESSION TAG SEQADV 9B2C LEU A 289 UNP A0A1S6L97 EXPRESSION TAG SEQADV 9B2C SER A 290 UNP A0A1S6L97 EXPRESSION TAG SEQADV 9B2C VAL A 291 UNP A0A1S6L97 EXPRESSION TAG SEQADV 9B2C LEU A 292 UNP A0A1S6L97 EXPRESSION TAG SEQADV 9B2C LEU A 293 UNP A0A1S6L97 EXPRESSION TAG SEQADV 9B2C MET A 294 UNP A0A1S6L97 EXPRESSION TAG SEQADV 9B2C GLY A 295 UNP A0A1S6L97 EXPRESSION TAG SEQADV 9B2C CYS A 296 UNP A0A1S6L97 EXPRESSION TAG SEQADV 9B2C VAL A 297 UNP A0A1S6L97 EXPRESSION TAG SEQADV 9B2C ALA A 298 UNP A0A1S6L97 EXPRESSION TAG SEQADV 9B2C GLU A 299 UNP A0A1S6L97 EXPRESSION TAG SEQADV 9B2C THR A 300 UNP A0A1S6L97 EXPRESSION TAG SEQADV 9B2C GLY A 301 UNP A0A1S6L97 EXPRESSION TAG SEQADV 9B2C THR A 302 UNP A0A1S6L97 EXPRESSION TAG SEQADV 9B2C LEU A 417 UNP A0A1S6L97 EXPRESSION TAG SEQADV 9B2C VAL A 418 UNP A0A1S6L97 EXPRESSION TAG SEQADV 9B2C PRO A 419 UNP A0A1S6L97 EXPRESSION TAG SEQADV 9B2C ARG A 420 UNP A0A1S6L97 EXPRESSION TAG SEQADV 9B2C GLY A 421 UNP A0A1S6L97 EXPRESSION TAG SEQADV 9B2C SER A 422 UNP A0A1S6L97 EXPRESSION TAG SEQADV 9B2C GLY A 423 UNP A0A1S6L97 EXPRESSION TAG SEQADV 9B2C GLY A 424 UNP A0A1S6L97 EXPRESSION TAG SEQADV 9B2C SER A 425 UNP A0A1S6L97 EXPRESSION TAG SEQADV 9B2C HIS A 426 UNP A0A1S6L97 EXPRESSION TAG SEQADV 9B2C HIS A 427 UNP A0A1S6L97 EXPRESSION TAG SEQADV 9B2C HIS A 428 UNP A0A1S6L97 EXPRESSION TAG SEQADV 9B2C HIS A 429 UNP A0A1S6L97 EXPRESSION TAG SEQADV 9B2C HIS A 430 UNP A0A1S6L97 EXPRESSION TAG SEQADV 9B2C HIS A 431 UNP A0A1S6L97 EXPRESSION TAG SEQADV 9B2C HIS A 432 UNP A0A1S6L97 EXPRESSION TAG SEQADV 9B2C HIS A 433 UNP A0A1S6L97 EXPRESSION TAG SEQRES 1 A 163 MET GLY ILE LEU PRO SER PRO GLY MET PRO ALA LEU LEU SEQRES 2 A 163 SER LEU VAL SER LEU LEU SER VAL LEU LEU MET GLY CYS SEQRES 3 A 163 VAL ALA GLU THR GLY THR PRO GLU LEU GLU VAL VAL GLN SEQRES 4 A 163 LEU ASN ILE SER ALA HIS MET ASP PHE GLY GLU ALA ARG SEQRES 5 A 163 LEU ASP SER VAL THR ILE ASN GLY ASN THR SER TYR CYS SEQRES 6 A 163 VAL THR LYS PRO TYR PHE ARG LEU GLU THR ASN PHE MET SEQRES 7 A 163 CYS THR GLY CYS THR MET ASN LEU ARG THR ASP THR CYS SEQRES 8 A 163 SER PHE ASP LEU SER ALA VAL ASN ASN GLY MET SER PHE SEQRES 9 A 163 SER GLN PHE CYS LEU SER THR GLU SER GLY ALA CYS GLU SEQRES 10 A 163 MET LYS ILE ILE VAL THR TYR VAL TRP ASN TYR LEU LEU SEQRES 11 A 163 ARG GLN ARG LEU TYR VAL THR ALA VAL GLU GLY GLN THR SEQRES 12 A 163 HIS THR GLY LEU VAL PRO ARG GLY SER GLY GLY SER HIS SEQRES 13 A 163 HIS HIS HIS HIS HIS HIS HIS SEQRES 1 L 219 ASP ILE VAL MET THR GLN SER PRO LEU SER LEU PRO VAL SEQRES 2 L 219 THR LEU GLY GLN PRO ALA SER ILE SER CYS ARG SER SER SEQRES 3 L 219 GLN SER LEU VAL TYR SER ASP GLY ASN THR PHE LEU ASN SEQRES 4 L 219 TRP PHE GLN GLN ARG PRO GLY GLN SER PRO ARG ARG LEU SEQRES 5 L 219 ILE TYR LYS VAL SER ASN ARG ASP SER GLY VAL PRO ASP SEQRES 6 L 219 ARG PHE SER GLY SER GLY SER GLY THR ASP PHE THR LEU SEQRES 7 L 219 ARG ILE SER ARG VAL GLU ALA GLU ASP VAL GLY PHE TYR SEQRES 8 L 219 TYR CYS MET GLN GLY THR HIS TRP PRO PRO THR PHE GLY SEQRES 9 L 219 PRO GLY THR LYS VAL GLU ILE LYS ARG THR VAL ALA ALA SEQRES 10 L 219 PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU SEQRES 11 L 219 LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN SEQRES 12 L 219 PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP SEQRES 13 L 219 ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL THR SEQRES 14 L 219 GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER SER SEQRES 15 L 219 THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS SEQRES 16 L 219 VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER SEQRES 17 L 219 PRO VAL THR LYS SER PHE ASN ARG GLY GLU CYS SEQRES 1 N 159 MET LYS LYS THR ALA ILE ALA ILE ALA VAL ALA LEU ALA SEQRES 2 N 159 GLY PHE ALA THR VAL ALA GLN ALA ALA PRO MET GLY SER SEQRES 3 N 159 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 4 N 159 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 5 N 159 ARG THR ILE SER ARG TYR ALA MET SER TRP PHE ARG GLN SEQRES 6 N 159 ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA VAL ALA ARG SEQRES 7 N 159 ARG SER GLY ASP GLY ALA PHE TYR ALA ASP SER VAL GLN SEQRES 8 N 159 GLY ARG PHE THR VAL SER ARG ASP ASP ALA LYS ASN THR SEQRES 9 N 159 VAL TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR SEQRES 10 N 159 ALA VAL TYR TYR CYS ALA ILE ASP SER ASP THR PHE TYR SEQRES 11 N 159 SER GLY SER TYR ASP TYR TRP GLY GLN GLY THR GLN VAL SEQRES 12 N 159 THR VAL SER SER HIS HIS HIS HIS HIS HIS HIS HIS GLU SEQRES 13 N 159 PRO GLU ALA SEQRES 1 H 222 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 H 222 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 H 222 PHE THR PHE SER HIS TYR THR MET ASN TRP VAL ARG GLN SEQRES 4 H 222 ALA PRO GLY ARG GLY LEU GLU TRP VAL SER SER ILE THR SEQRES 5 H 222 THR SER SER ASN PHE ILE TYR TYR ALA ASP SER VAL LYS SEQRES 6 H 222 GLY ARG PHE THR ILE SER ARG ASP ASN THR LYS ASN SER SEQRES 7 H 222 LEU TYR LEU GLN MET ASN SER LEU SER ALA GLU ASP THR SEQRES 8 H 222 ALA VAL TYR PHE CYS ALA ARG GLY GLY TRP GLU LEU SER SEQRES 9 H 222 TYR PHE ASP PHE TRP GLY GLN GLY THR LEU VAL THR VAL SEQRES 10 H 222 SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU SEQRES 11 H 222 ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA SEQRES 12 H 222 LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL SEQRES 13 H 222 THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL SEQRES 14 H 222 HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SEQRES 15 H 222 SER LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU SEQRES 16 H 222 GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SEQRES 17 H 222 SER ASN THR LYS VAL ASP LYS ARG VAL GLU PRO LYS SER SEQRES 18 H 222 CYS HET NAG B 1 14 HET NAG B 2 14 HET BMA B 3 11 HET NAG A 501 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 5 NAG 3(C8 H15 N O6) FORMUL 5 BMA C6 H12 O6 HELIX 1 AA1 ASP A 364 ASN A 370 1 7 HELIX 2 AA2 SER L 126 LYS L 131 1 6 HELIX 3 AA3 LYS L 188 GLU L 192 1 5 HELIX 4 AA4 ASP N 63 GLN N 66 5 4 HELIX 5 AA5 LYS N 88 THR N 92 5 5 HELIX 6 AA6 THR H 28 TYR H 32 5 5 HELIX 7 AA7 ASP H 62 LYS H 65 5 4 HELIX 8 AA8 SER H 87 THR H 91 5 5 HELIX 9 AA9 GLY H 100 SER H 104 5 5 HELIX 10 AB1 SER H 162 ALA H 164 5 3 HELIX 11 AB2 LYS H 207 ASN H 210 5 4 SHEET 1 AA1 3 GLU A 320 ILE A 328 0 SHEET 2 AA1 3 VAL A 308 ASP A 317 -1 N ASN A 311 O THR A 327 SHEET 3 AA1 3 LEU A 343 ASN A 346 1 O GLU A 344 N LEU A 310 SHEET 1 AA2 3 GLU A 320 ILE A 328 0 SHEET 2 AA2 3 VAL A 308 ASP A 317 -1 N ASN A 311 O THR A 327 SHEET 3 AA2 3 CYS A 349 THR A 350 1 O THR A 350 N MET A 316 SHEET 1 AA3 5 SER A 333 CYS A 335 0 SHEET 2 AA3 5 SER A 373 SER A 380 -1 O LEU A 379 N TYR A 334 SHEET 3 AA3 5 ASN A 397 THR A 415 -1 O HIS A 414 N PHE A 374 SHEET 4 AA3 5 CYS A 386 THR A 393 -1 N CYS A 386 O VAL A 406 SHEET 5 AA3 5 THR A 353 THR A 358 -1 N ASN A 355 O ILE A 391 SHEET 1 AA4 4 MET L 4 THR L 5 0 SHEET 2 AA4 4 ALA L 19 SER L 25 -1 O ARG L 24 N THR L 5 SHEET 3 AA4 4 PHE L 76 ILE L 80 -1 O LEU L 78 N ILE L 21 SHEET 4 AA4 4 PHE L 67 GLY L 71 -1 N SER L 68 O ARG L 79 SHEET 1 AA5 5 SER L 10 VAL L 13 0 SHEET 2 AA5 5 THR L 107 ILE L 111 1 O GLU L 110 N VAL L 13 SHEET 3 AA5 5 GLY L 89 GLN L 95 -1 N GLY L 89 O VAL L 109 SHEET 4 AA5 5 LEU L 38 GLN L 43 -1 N GLN L 43 O PHE L 90 SHEET 5 AA5 5 ARG L 50 ILE L 53 -1 O LEU L 52 N TRP L 40 SHEET 1 AA6 4 SER L 10 VAL L 13 0 SHEET 2 AA6 4 THR L 107 ILE L 111 1 O GLU L 110 N VAL L 13 SHEET 3 AA6 4 GLY L 89 GLN L 95 -1 N GLY L 89 O VAL L 109 SHEET 4 AA6 4 THR L 102 PHE L 103 -1 O THR L 102 N GLN L 95 SHEET 1 AA7 4 SER L 119 PHE L 123 0 SHEET 2 AA7 4 THR L 134 PHE L 144 -1 O VAL L 138 N PHE L 123 SHEET 3 AA7 4 TYR L 178 SER L 187 -1 O LEU L 180 N LEU L 141 SHEET 4 AA7 4 SER L 164 VAL L 168 -1 N SER L 167 O SER L 181 SHEET 1 AA8 4 ALA L 158 LEU L 159 0 SHEET 2 AA8 4 LYS L 150 VAL L 155 -1 N VAL L 155 O ALA L 158 SHEET 3 AA8 4 VAL L 196 THR L 202 -1 O GLU L 200 N GLN L 152 SHEET 4 AA8 4 VAL L 210 ASN L 215 -1 O LYS L 212 N CYS L 199 SHEET 1 AA9 4 GLN N 4 GLN N 6 0 SHEET 2 AA9 4 LEU N 19 SER N 26 -1 O ALA N 24 N GLN N 6 SHEET 3 AA9 4 THR N 79 MET N 84 -1 O LEU N 82 N LEU N 21 SHEET 4 AA9 4 PHE N 69 ASP N 74 -1 N THR N 70 O GLN N 83 SHEET 1 AB1 5 ALA N 59 TYR N 61 0 SHEET 2 AB1 5 ARG N 46 ALA N 52 -1 N VAL N 51 O PHE N 60 SHEET 3 AB1 5 MET N 35 GLN N 40 -1 N ARG N 39 O GLU N 47 SHEET 4 AB1 5 ALA N 93 ILE N 99 -1 O TYR N 96 N PHE N 38 SHEET 5 AB1 5 THR N 116 VAL N 118 -1 O THR N 116 N TYR N 95 SHEET 1 AB2 4 GLN H 3 SER H 7 0 SHEET 2 AB2 4 LEU H 18 SER H 25 -1 O ALA H 23 N VAL H 5 SHEET 3 AB2 4 SER H 78 MET H 83 -1 O MET H 83 N LEU H 18 SHEET 4 AB2 4 PHE H 68 ASP H 73 -1 N SER H 71 O TYR H 80 SHEET 1 AB3 6 LEU H 11 VAL H 12 0 SHEET 2 AB3 6 THR H 113 VAL H 117 1 O THR H 116 N VAL H 12 SHEET 3 AB3 6 ALA H 92 GLY H 99 -1 N TYR H 94 O THR H 113 SHEET 4 AB3 6 THR H 33 GLN H 39 -1 N VAL H 37 O PHE H 95 SHEET 5 AB3 6 LEU H 45 ILE H 51 -1 O VAL H 48 N TRP H 36 SHEET 6 AB3 6 ILE H 58 TYR H 60 -1 O TYR H 59 N SER H 50 SHEET 1 AB4 4 LEU H 11 VAL H 12 0 SHEET 2 AB4 4 THR H 113 VAL H 117 1 O THR H 116 N VAL H 12 SHEET 3 AB4 4 ALA H 92 GLY H 99 -1 N TYR H 94 O THR H 113 SHEET 4 AB4 4 PHE H 108 TRP H 109 -1 O PHE H 108 N ARG H 98 SHEET 1 AB5 4 SER H 126 LEU H 130 0 SHEET 2 AB5 4 ALA H 142 TYR H 151 -1 O LEU H 147 N PHE H 128 SHEET 3 AB5 4 TYR H 182 VAL H 190 -1 O LEU H 184 N VAL H 148 SHEET 4 AB5 4 VAL H 169 THR H 171 -1 N HIS H 170 O VAL H 187 SHEET 1 AB6 4 SER H 126 LEU H 130 0 SHEET 2 AB6 4 ALA H 142 TYR H 151 -1 O LEU H 147 N PHE H 128 SHEET 3 AB6 4 TYR H 182 VAL H 190 -1 O LEU H 184 N VAL H 148 SHEET 4 AB6 4 VAL H 175 LEU H 176 -1 N VAL H 175 O SER H 183 SHEET 1 AB7 3 THR H 157 TRP H 160 0 SHEET 2 AB7 3 TYR H 200 HIS H 206 -1 O ASN H 203 N SER H 159 SHEET 3 AB7 3 THR H 211 VAL H 217 -1 O VAL H 213 N VAL H 204 SSBOND 1 CYS A 335 CYS A 378 1555 1555 2.13 SSBOND 2 CYS A 349 CYS A 352 1555 1555 2.00 SSBOND 3 CYS A 361 CYS A 386 1555 1555 2.02 SSBOND 4 CYS L 23 CYS L 93 1555 1555 2.02 SSBOND 5 CYS L 139 CYS L 199 1555 1555 2.03 SSBOND 6 CYS N 23 CYS N 97 1555 1555 2.03 SSBOND 7 CYS H 22 CYS H 96 1555 1555 2.05 SSBOND 8 CYS H 146 CYS H 202 1555 1555 2.02 LINK ND2 ASN A 311 C1 NAG B 1 1555 1555 1.45 LINK ND2 ASN A 331 C1 NAG A 501 1555 1555 1.43 LINK O4 NAG B 1 C1 NAG B 2 1555 1555 1.39 LINK O4 NAG B 2 C1 BMA B 3 1555 1555 1.39 CISPEP 1 TRP L 99 PRO L 100 0 -1.95 CISPEP 2 TYR L 145 PRO L 146 0 1.52 CISPEP 3 PHE H 152 PRO H 153 0 -7.18 CISPEP 4 GLU H 154 PRO H 155 0 -6.17 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 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