HEADER ANTITUMOR PROTEIN 20-APR-25 9OA9 TITLE CRYOEM STRUCTURE OF ANTI-MHC-I MAB B1.23.2 FC DOMAINS COMPND MOL_ID: 1; COMPND 2 MOLECULE: ANTI-MHC-I MAB B1.23.2 FC DOMAINS H-CHAIN; COMPND 3 CHAIN: J, K; COMPND 4 ENGINEERED: YES; COMPND 5 OTHER_DETAILS: MAB B1.23.2 FULL-LENGTH: VH, HUMAN IGG1 CH1, FC (CH2, COMPND 6 CH3) DOMAINS, INCLUDING THE HINGE 9213-226), AND LALAPG MUTATIONS COMPND 7 (A230, A231, AND G325) SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 CELL: EXPI293F; SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PCDNA3.1 KEYWDS MHC-I, HLA, ANTI-HUMAN-MAB, H2-DD, B1.23.2, ANTI-MHC-I ANTIBODY, KEYWDS 2 ANTI-TUMOR, CANCER IMMUNOTHERAPY, ANTITUMOR PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR J.JIANG,K.NATARAJAN,D.H.MARGULIES REVDAT 1 04-FEB-26 9OA9 0 JRNL AUTH J.JIANG,K.NATARAJAN,D.H.MARGULIES JRNL TITL CRYOEM STRUCTURE OF ANTI-MHC-I B1.23.2 FC DOMAINS JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.44 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : CRYOSPARC, SERIALEM, CRYOSPARC, UCSF REMARK 3 CHIMERAX, CRYOSPARC, CRYOSPARC, 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 : REAL REMARK 3 REFINEMENT PROTOCOL : RIGID BODY FIT REMARK 3 REFINEMENT TARGET : CC REMARK 3 OVERALL ANISOTROPIC B VALUE : 92.800 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) : 3.440 REMARK 3 NUMBER OF PARTICLES : 251084 REMARK 3 CTF CORRECTION METHOD : NONE REMARK 3 REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL REMARK 3 REMARK 3 OTHER DETAILS: NULL REMARK 4 REMARK 4 9OA9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-APR-25. REMARK 100 THE DEPOSITION ID IS D_1000295033. REMARK 245 REMARK 245 EXPERIMENTAL DETAILS REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE REMARK 245 SPECIMEN TYPE : NULL REMARK 245 REMARK 245 ELECTRON MICROSCOPE SAMPLE REMARK 245 SAMPLE TYPE : PARTICLE REMARK 245 PARTICLE TYPE : POINT REMARK 245 NAME OF SAMPLE : COMPLEX OF ANTI-HUMAN-MAB REMARK 245 B1.23.2 AND MHC-I HLA-B44:05, REMARK 245 FC DOMAINS REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 1.00 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 : THE SAMPLE WAS MIXED 1:1 MOLE REMARK 245 RATIO OF ANTIBODY AND HLA-B44 AND PURIFIED. WITH CONCENTRATION REMARK 245 OF 1.0 MG/ML REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : 7154 REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : TFS KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 (6K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 700.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2000.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : 2.70 REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 5420.00 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : 105000 REMARK 245 CALIBRATED MAGNIFICATION : 60096 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: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: J, K, X, 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 GLN J 1 REMARK 465 VAL J 2 REMARK 465 GLN J 3 REMARK 465 LEU J 4 REMARK 465 GLN J 5 REMARK 465 GLN J 6 REMARK 465 SER J 7 REMARK 465 GLY J 8 REMARK 465 THR J 9 REMARK 465 VAL J 10 REMARK 465 LEU J 11 REMARK 465 ALA J 12 REMARK 465 ARG J 13 REMARK 465 PRO J 14 REMARK 465 GLY J 15 REMARK 465 SER J 16 REMARK 465 SER J 17 REMARK 465 VAL J 18 REMARK 465 LYS J 19 REMARK 465 MET J 20 REMARK 465 SER J 21 REMARK 465 CYS J 22 REMARK 465 LYS J 23 REMARK 465 ALA J 24 REMARK 465 SER J 25 REMARK 465 GLY J 26 REMARK 465 TYR J 27 REMARK 465 SER J 28 REMARK 465 PHE J 29 REMARK 465 THR J 30 REMARK 465 SER J 31 REMARK 465 TYR J 32 REMARK 465 TRP J 33 REMARK 465 MET J 34 REMARK 465 HIS J 35 REMARK 465 TRP J 36 REMARK 465 VAL J 37 REMARK 465 LYS J 38 REMARK 465 GLN J 39 REMARK 465 ARG J 40 REMARK 465 PRO J 41 REMARK 465 GLY J 42 REMARK 465 GLN J 43 REMARK 465 GLY J 44 REMARK 465 LEU J 45 REMARK 465 GLU J 46 REMARK 465 TRP J 47 REMARK 465 ILE J 48 REMARK 465 GLY J 49 REMARK 465 ALA J 50 REMARK 465 ILE J 51 REMARK 465 TYR J 52 REMARK 465 PRO J 53 REMARK 465 GLY J 54 REMARK 465 ASN J 55 REMARK 465 SER J 56 REMARK 465 ASP J 57 REMARK 465 ALA J 58 REMARK 465 THR J 59 REMARK 465 TYR J 60 REMARK 465 ASN J 61 REMARK 465 GLN J 62 REMARK 465 LYS J 63 REMARK 465 PHE J 64 REMARK 465 LYS J 65 REMARK 465 GLY J 66 REMARK 465 LYS J 67 REMARK 465 ALA J 68 REMARK 465 LYS J 69 REMARK 465 LEU J 70 REMARK 465 THR J 71 REMARK 465 ALA J 72 REMARK 465 VAL J 73 REMARK 465 THR J 74 REMARK 465 SER J 75 REMARK 465 ALA J 76 REMARK 465 ASN J 77 REMARK 465 THR J 78 REMARK 465 ALA J 79 REMARK 465 TYR J 80 REMARK 465 MET J 81 REMARK 465 GLU J 82 REMARK 465 LEU J 83 REMARK 465 SER J 84 REMARK 465 SER J 85 REMARK 465 LEU J 86 REMARK 465 THR J 87 REMARK 465 ASN J 88 REMARK 465 GLU J 89 REMARK 465 ASP J 90 REMARK 465 SER J 91 REMARK 465 ALA J 92 REMARK 465 VAL J 93 REMARK 465 TYR J 94 REMARK 465 TYR J 95 REMARK 465 CYS J 96 REMARK 465 THR J 97 REMARK 465 ASN J 98 REMARK 465 TYR J 99 REMARK 465 PHE J 100 REMARK 465 ASP J 101 REMARK 465 GLN J 102 REMARK 465 TRP J 103 REMARK 465 GLY J 104 REMARK 465 GLN J 105 REMARK 465 GLY J 106 REMARK 465 THR J 107 REMARK 465 THR J 108 REMARK 465 LEU J 109 REMARK 465 THR J 110 REMARK 465 VAL J 111 REMARK 465 SER J 112 REMARK 465 SER J 113 REMARK 465 ALA J 114 REMARK 465 SER J 115 REMARK 465 THR J 116 REMARK 465 LYS J 117 REMARK 465 GLY J 118 REMARK 465 PHE J 146 REMARK 465 PRO J 147 REMARK 465 GLU J 148 REMARK 465 PRO J 149 REMARK 465 ASN J 155 REMARK 465 SER J 156 REMARK 465 GLY J 157 REMARK 465 ALA J 158 REMARK 465 LEU J 159 REMARK 465 THR J 160 REMARK 465 SER J 161 REMARK 465 VAL J 198 REMARK 465 ASN J 199 REMARK 465 HIS J 200 REMARK 465 LYS J 201 REMARK 465 PRO J 202 REMARK 465 SER J 203 REMARK 465 GLU J 289 REMARK 465 GLU J 290 REMARK 465 SER J 350 REMARK 465 ARG J 351 REMARK 465 GLU J 352 REMARK 465 GLU J 353 REMARK 465 MET J 354 REMARK 465 THR J 355 REMARK 465 PRO J 383 REMARK 465 GLU J 384 REMARK 465 ASN J 385 REMARK 465 ASN J 386 REMARK 465 TYR J 387 REMARK 465 LYS J 388 REMARK 465 THR J 389 REMARK 465 THR J 390 REMARK 465 PRO J 391 REMARK 465 PRO J 392 REMARK 465 VAL J 393 REMARK 465 GLY J 416 REMARK 465 ASN J 417 REMARK 465 VAL J 418 REMARK 465 HIS J 429 REMARK 465 ASN J 430 REMARK 465 SER J 440 REMARK 465 PRO J 441 REMARK 465 GLY J 442 REMARK 465 LYS J 443 REMARK 465 GLN K 1 REMARK 465 VAL K 2 REMARK 465 GLN K 3 REMARK 465 LEU K 4 REMARK 465 GLN K 5 REMARK 465 GLN K 6 REMARK 465 SER K 7 REMARK 465 GLY K 8 REMARK 465 THR K 9 REMARK 465 VAL K 10 REMARK 465 LEU K 11 REMARK 465 ALA K 12 REMARK 465 ARG K 13 REMARK 465 PRO K 14 REMARK 465 GLY K 15 REMARK 465 SER K 16 REMARK 465 SER K 17 REMARK 465 VAL K 18 REMARK 465 LYS K 19 REMARK 465 MET K 20 REMARK 465 SER K 21 REMARK 465 CYS K 22 REMARK 465 LYS K 23 REMARK 465 ALA K 24 REMARK 465 SER K 25 REMARK 465 GLY K 26 REMARK 465 TYR K 27 REMARK 465 SER K 28 REMARK 465 PHE K 29 REMARK 465 THR K 30 REMARK 465 SER K 31 REMARK 465 TYR K 32 REMARK 465 TRP K 33 REMARK 465 MET K 34 REMARK 465 HIS K 35 REMARK 465 TRP K 36 REMARK 465 VAL K 37 REMARK 465 LYS K 38 REMARK 465 GLN K 39 REMARK 465 ARG K 40 REMARK 465 PRO K 41 REMARK 465 GLY K 42 REMARK 465 GLN K 43 REMARK 465 GLY K 44 REMARK 465 LEU K 45 REMARK 465 GLU K 46 REMARK 465 TRP K 47 REMARK 465 ILE K 48 REMARK 465 GLY K 49 REMARK 465 ALA K 50 REMARK 465 ILE K 51 REMARK 465 TYR K 52 REMARK 465 PRO K 53 REMARK 465 GLY K 54 REMARK 465 ASN K 55 REMARK 465 SER K 56 REMARK 465 ASP K 57 REMARK 465 ALA K 58 REMARK 465 THR K 59 REMARK 465 TYR K 60 REMARK 465 ASN K 61 REMARK 465 GLN K 62 REMARK 465 LYS K 63 REMARK 465 PHE K 64 REMARK 465 LYS K 65 REMARK 465 GLY K 66 REMARK 465 LYS K 67 REMARK 465 ALA K 68 REMARK 465 LYS K 69 REMARK 465 LEU K 70 REMARK 465 THR K 71 REMARK 465 ALA K 72 REMARK 465 VAL K 73 REMARK 465 THR K 74 REMARK 465 SER K 75 REMARK 465 ALA K 76 REMARK 465 ASN K 77 REMARK 465 THR K 78 REMARK 465 ALA K 79 REMARK 465 TYR K 80 REMARK 465 MET K 81 REMARK 465 GLU K 82 REMARK 465 LEU K 83 REMARK 465 SER K 84 REMARK 465 SER K 85 REMARK 465 LEU K 86 REMARK 465 THR K 87 REMARK 465 ASN K 88 REMARK 465 GLU K 89 REMARK 465 ASP K 90 REMARK 465 SER K 91 REMARK 465 ALA K 92 REMARK 465 VAL K 93 REMARK 465 TYR K 94 REMARK 465 TYR K 95 REMARK 465 CYS K 96 REMARK 465 THR K 97 REMARK 465 ASN K 98 REMARK 465 TYR K 99 REMARK 465 PHE K 100 REMARK 465 ASP K 101 REMARK 465 GLN K 102 REMARK 465 TRP K 103 REMARK 465 GLY K 104 REMARK 465 GLN K 105 REMARK 465 GLY K 106 REMARK 465 THR K 107 REMARK 465 THR K 108 REMARK 465 LEU K 109 REMARK 465 THR K 110 REMARK 465 VAL K 111 REMARK 465 SER K 112 REMARK 465 SER K 113 REMARK 465 ALA K 114 REMARK 465 SER K 115 REMARK 465 THR K 116 REMARK 465 LYS K 117 REMARK 465 GLY K 118 REMARK 465 PRO K 119 REMARK 465 SER K 120 REMARK 465 VAL K 121 REMARK 465 PHE K 122 REMARK 465 PRO K 123 REMARK 465 LEU K 124 REMARK 465 ALA K 125 REMARK 465 PRO K 126 REMARK 465 PHE K 146 REMARK 465 PRO K 147 REMARK 465 LYS K 201 REMARK 465 PRO K 202 REMARK 465 SER K 203 REMARK 465 ASN K 204 REMARK 465 GLY K 277 REMARK 465 VAL K 278 REMARK 465 GLU K 279 REMARK 465 VAL K 280 REMARK 465 HIS K 281 REMARK 465 LYS K 313 REMARK 465 GLU K 314 REMARK 465 TYR K 315 REMARK 465 ARG K 351 REMARK 465 GLU K 352 REMARK 465 GLU K 353 REMARK 465 MET K 354 REMARK 465 THR K 355 REMARK 465 ASN K 380 REMARK 465 GLY K 381 REMARK 465 GLN K 382 REMARK 465 PRO K 383 REMARK 465 GLU K 384 REMARK 465 ASN K 385 REMARK 465 ASN K 386 REMARK 465 TYR K 387 REMARK 465 LYS K 388 REMARK 465 THR K 389 REMARK 465 THR K 390 REMARK 465 PRO K 391 REMARK 465 PRO K 392 REMARK 465 VAL K 393 REMARK 465 LEU K 394 REMARK 465 ASP K 395 REMARK 465 SER K 396 REMARK 465 ASP K 397 REMARK 465 GLY K 398 REMARK 465 SER K 399 REMARK 465 SER K 436 REMARK 465 LEU K 437 REMARK 465 SER K 438 REMARK 465 LEU K 439 REMARK 465 SER K 440 REMARK 465 PRO K 441 REMARK 465 GLY K 442 REMARK 465 LYS K 443 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 LEU J 124 CG CD1 CD2 REMARK 470 SER J 127 OG REMARK 470 SER J 128 OG REMARK 470 LYS J 129 CG CD CE NZ REMARK 470 VAL J 142 CG1 CG2 REMARK 470 LYS J 143 CG CD CE NZ REMARK 470 ASP J 144 CG OD1 OD2 REMARK 470 TYR J 145 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 VAL J 163 CG1 CG2 REMARK 470 VAL J 169 CG1 CG2 REMARK 470 LEU J 170 CG CD1 CD2 REMARK 470 GLN J 171 CG CD OE1 NE2 REMARK 470 SER J 173 OG REMARK 470 TYR J 176 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 THR J 183 OG1 CG2 REMARK 470 SER J 187 OG REMARK 470 SER J 188 OG REMARK 470 GLN J 192 CG CD OE1 NE2 REMARK 470 ILE J 195 CG1 CG2 CD1 REMARK 470 ASN J 204 CG OD1 ND2 REMARK 470 LYS J 206 CG CD CE NZ REMARK 470 LYS J 209 CG CD CE NZ REMARK 470 LYS J 210 CG CD CE NZ REMARK 470 VAL J 211 CG1 CG2 REMARK 470 GLU J 212 CG CD OE1 OE2 REMARK 470 CYS J 216 SG REMARK 470 LYS J 218 CG CD CE NZ REMARK 470 HIS J 220 CG ND1 CD2 CE1 NE2 REMARK 470 GLU J 229 CG CD OE1 OE2 REMARK 470 VAL J 236 CG1 CG2 REMARK 470 PHE J 239 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LYS J 242 CG CD CE NZ REMARK 470 MET J 248 CG SD CE REMARK 470 ILE J 249 CG1 CG2 CD1 REMARK 470 ARG J 251 CG CD NE CZ NH1 NH2 REMARK 470 VAL J 255 CG1 CG2 REMARK 470 THR J 256 OG1 CG2 REMARK 470 VAL J 258 CG1 CG2 REMARK 470 VAL J 259 CG1 CG2 REMARK 470 VAL J 260 CG1 CG2 REMARK 470 ASP J 261 CG OD1 OD2 REMARK 470 SER J 263 OG REMARK 470 HIS J 264 CG ND1 CD2 CE1 NE2 REMARK 470 ASP J 266 CG OD1 OD2 REMARK 470 GLU J 268 CG CD OE1 OE2 REMARK 470 ASN J 272 CG OD1 ND2 REMARK 470 TYR J 292 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 TYR J 296 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ARG J 297 CG CD NE CZ NH1 NH2 REMARK 470 VAL J 298 CG1 CG2 REMARK 470 VAL J 299 CG1 CG2 REMARK 470 SER J 300 OG REMARK 470 VAL J 301 CG1 CG2 REMARK 470 LEU J 305 CG CD1 CD2 REMARK 470 HIS J 306 CG ND1 CD2 CE1 NE2 REMARK 470 ASP J 308 CG OD1 OD2 REMARK 470 LYS J 313 CG CD CE NZ REMARK 470 GLU J 314 CG CD OE1 OE2 REMARK 470 LYS J 322 CG CD CE NZ REMARK 470 LEU J 324 CG CD1 CD2 REMARK 470 THR J 331 OG1 CG2 REMARK 470 SER J 333 OG REMARK 470 LYS J 334 CG CD CE NZ REMARK 470 LYS J 336 CG CD CE NZ REMARK 470 GLN J 338 CG CD OE1 NE2 REMARK 470 ARG J 340 CG CD NE CZ NH1 NH2 REMARK 470 GLU J 341 CG CD OE1 OE2 REMARK 470 LYS J 356 CG CD CE NZ REMARK 470 ASN J 357 CG OD1 ND2 REMARK 470 GLN J 358 CG CD OE1 NE2 REMARK 470 LYS J 366 CG CD CE NZ REMARK 470 PHE J 368 CG CD1 CD2 CE1 CE2 CZ REMARK 470 TYR J 369 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 SER J 371 OG REMARK 470 GLU J 376 CG CD OE1 OE2 REMARK 470 GLU J 378 CG CD OE1 OE2 REMARK 470 ASN J 380 CG OD1 ND2 REMARK 470 GLN J 382 CG CD OE1 NE2 REMARK 470 ASP J 395 CG OD1 OD2 REMARK 470 LEU J 406 CG CD1 CD2 REMARK 470 VAL J 408 CG1 CG2 REMARK 470 LYS J 410 CG CD CE NZ REMARK 470 GLN J 414 CG CD OE1 NE2 REMARK 470 SER J 422 OG REMARK 470 VAL J 423 CG1 CG2 REMARK 470 MET J 424 CG SD CE REMARK 470 HIS J 425 CG ND1 CD2 CE1 NE2 REMARK 470 GLU J 426 CG CD OE1 OE2 REMARK 470 LEU J 428 CG CD1 CD2 REMARK 470 HIS J 431 CG ND1 CD2 CE1 NE2 REMARK 470 TYR J 432 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 THR J 433 OG1 CG2 REMARK 470 GLN J 434 CG CD OE1 NE2 REMARK 470 LYS J 435 CG CD CE NZ REMARK 470 SER J 438 OG REMARK 470 LYS K 129 CG CD CE NZ REMARK 470 SER K 130 OG REMARK 470 THR K 135 OG1 CG2 REMARK 470 LEU K 141 CG CD1 CD2 REMARK 470 LYS K 143 CG CD CE NZ REMARK 470 TYR K 145 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 GLU K 148 CG CD OE1 OE2 REMARK 470 VAL K 150 CG1 CG2 REMARK 470 THR K 151 OG1 CG2 REMARK 470 TRP K 154 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP K 154 CZ3 CH2 REMARK 470 THR K 160 OG1 CG2 REMARK 470 SER K 161 OG REMARK 470 VAL K 163 CG1 CG2 REMARK 470 PHE K 166 CG CD1 CD2 CE1 CE2 CZ REMARK 470 VAL K 169 CG1 CG2 REMARK 470 LEU K 170 CG CD1 CD2 REMARK 470 SER K 173 OG REMARK 470 LEU K 175 CG CD1 CD2 REMARK 470 TYR K 176 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LEU K 189 CG CD1 CD2 REMARK 470 THR K 191 OG1 CG2 REMARK 470 ASN K 199 CG OD1 ND2 REMARK 470 HIS K 200 CG ND1 CD2 CE1 NE2 REMARK 470 LYS K 206 CG CD CE NZ REMARK 470 ASP K 208 CG OD1 OD2 REMARK 470 LYS K 210 CG CD CE NZ REMARK 470 GLU K 212 CG CD OE1 OE2 REMARK 470 LYS K 214 CG CD CE NZ REMARK 470 CYS K 216 SG REMARK 470 ASP K 217 CG OD1 OD2 REMARK 470 LYS K 218 CG CD CE NZ REMARK 470 HIS K 220 CG ND1 CD2 CE1 NE2 REMARK 470 THR K 221 OG1 CG2 REMARK 470 LEU K 238 CG CD1 CD2 REMARK 470 PHE K 239 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LYS K 242 CG CD CE NZ REMARK 470 ASP K 245 CG OD1 OD2 REMARK 470 THR K 246 OG1 CG2 REMARK 470 MET K 248 CG SD CE REMARK 470 ILE K 249 CG1 CG2 CD1 REMARK 470 SER K 250 OG REMARK 470 ARG K 251 CG CD NE CZ NH1 NH2 REMARK 470 GLU K 254 CG CD OE1 OE2 REMARK 470 VAL K 255 CG1 CG2 REMARK 470 THR K 256 OG1 CG2 REMARK 470 HIS K 264 CG ND1 CD2 CE1 NE2 REMARK 470 GLU K 265 CG CD OE1 OE2 REMARK 470 ASP K 266 CG OD1 OD2 REMARK 470 GLU K 268 CG CD OE1 OE2 REMARK 470 LYS K 270 CG CD CE NZ REMARK 470 ASN K 272 CG OD1 ND2 REMARK 470 TYR K 274 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ASN K 282 CG OD1 ND2 REMARK 470 LYS K 284 CG CD CE NZ REMARK 470 THR K 285 OG1 CG2 REMARK 470 LYS K 286 CG CD CE NZ REMARK 470 GLU K 289 CG CD OE1 OE2 REMARK 470 GLU K 290 CG CD OE1 OE2 REMARK 470 GLN K 291 CG CD OE1 NE2 REMARK 470 TYR K 292 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 THR K 295 OG1 CG2 REMARK 470 TYR K 296 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ARG K 297 CG CD NE CZ NH1 NH2 REMARK 470 LEU K 305 CG CD1 CD2 REMARK 470 HIS K 306 CG ND1 CD2 CE1 NE2 REMARK 470 GLN K 307 CG CD OE1 NE2 REMARK 470 ASP K 308 CG OD1 OD2 REMARK 470 TRP K 309 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP K 309 CZ3 CH2 REMARK 470 LEU K 310 CG CD1 CD2 REMARK 470 ILE K 332 CG1 CG2 CD1 REMARK 470 SER K 333 OG REMARK 470 LYS K 334 CG CD CE NZ REMARK 470 GLN K 338 CG CD OE1 NE2 REMARK 470 ARG K 340 CG CD NE CZ NH1 NH2 REMARK 470 GLU K 341 CG CD OE1 OE2 REMARK 470 GLN K 343 CG CD OE1 NE2 REMARK 470 LYS K 356 CG CD CE NZ REMARK 470 GLN K 358 CG CD OE1 NE2 REMARK 470 LYS K 366 CG CD CE NZ REMARK 470 ILE K 373 CG1 CG2 CD1 REMARK 470 VAL K 375 CG1 CG2 REMARK 470 GLU K 376 CG CD OE1 OE2 REMARK 470 PHE K 400 CG CD1 CD2 CE1 CE2 CZ REMARK 470 PHE K 401 CG CD1 CD2 CE1 CE2 CZ REMARK 470 TYR K 403 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LEU K 406 CG CD1 CD2 REMARK 470 THR K 407 OG1 CG2 REMARK 470 SER K 411 OG REMARK 470 ARG K 412 CG CD NE CZ NH1 NH2 REMARK 470 TRP K 413 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP K 413 CZ3 CH2 REMARK 470 GLN K 414 CG CD OE1 NE2 REMARK 470 GLN K 415 CG CD OE1 NE2 REMARK 470 VAL K 418 CG1 CG2 REMARK 470 PHE K 419 CG CD1 CD2 CE1 CE2 CZ REMARK 470 SER K 420 OG REMARK 470 LEU K 428 CG CD1 CD2 REMARK 470 HIS K 429 CG ND1 CD2 CE1 NE2 REMARK 470 ASN K 430 CG OD1 ND2 REMARK 470 HIS K 431 CG ND1 CD2 CE1 NE2 REMARK 470 TYR K 432 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 THR K 433 OG1 CG2 REMARK 470 GLN K 434 CG CD OE1 NE2 REMARK 470 LYS K 435 CG CD CE NZ 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 O4 NAG X 2 C2 MAN X 3 2.16 REMARK 500 O4 NAG X 2 O5 MAN X 3 2.16 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 J 127 -158.97 -161.35 REMARK 500 SER J 128 31.07 -94.10 REMARK 500 LYS J 129 -157.55 -144.88 REMARK 500 HIS J 164 -155.57 -150.37 REMARK 500 SER J 172 -128.54 54.42 REMARK 500 LEU J 178 145.90 -171.88 REMARK 500 PRO J 213 -178.16 -69.33 REMARK 500 ASP J 217 -64.26 -95.21 REMARK 500 LYS J 218 -152.14 -163.96 REMARK 500 THR J 219 54.24 73.90 REMARK 500 PRO J 223 -139.03 -75.04 REMARK 500 ALA J 227 -7.37 -154.48 REMARK 500 GLU J 229 115.10 -160.81 REMARK 500 ALA J 230 -66.21 -161.98 REMARK 500 ALA J 231 69.83 36.33 REMARK 500 ILE J 249 101.65 53.94 REMARK 500 THR J 252 156.06 65.77 REMARK 500 CYS J 257 48.41 -74.03 REMARK 500 SER J 263 139.03 -38.15 REMARK 500 HIS J 264 -113.50 79.00 REMARK 500 GLU J 265 -123.57 -86.31 REMARK 500 GLU J 268 19.23 -158.37 REMARK 500 ASP J 276 44.89 -81.68 REMARK 500 VAL J 278 -58.30 -132.96 REMARK 500 ASN J 282 45.61 -141.43 REMARK 500 LEU J 310 27.42 -142.97 REMARK 500 GLU J 314 89.87 -47.54 REMARK 500 LYS J 322 41.82 -102.62 REMARK 500 SER J 333 -149.55 -127.94 REMARK 500 LYS J 334 155.78 172.19 REMARK 500 GLN J 338 144.90 -170.20 REMARK 500 PRO J 370 96.44 23.03 REMARK 500 SER J 379 96.37 -163.88 REMARK 500 ASP J 395 -150.48 68.96 REMARK 500 SER J 422 23.97 -140.62 REMARK 500 ALA J 427 -167.94 -162.12 REMARK 500 TYR J 432 115.22 -161.62 REMARK 500 LYS J 435 151.25 67.58 REMARK 500 LYS K 129 -85.53 39.99 REMARK 500 SER K 132 -171.66 55.28 REMARK 500 TRP K 154 -161.66 -163.88 REMARK 500 ASN K 155 -167.99 -74.10 REMARK 500 ALA K 168 -167.07 -114.71 REMARK 500 VAL K 169 154.97 72.75 REMARK 500 LEU K 170 70.07 56.48 REMARK 500 GLN K 171 68.78 61.60 REMARK 500 SER K 172 -167.87 -72.57 REMARK 500 SER K 173 -123.22 72.00 REMARK 500 TYR K 176 154.10 68.85 REMARK 500 LEU K 178 -65.90 -101.49 REMARK 500 REMARK 500 THIS ENTRY HAS 82 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-46601 RELATED DB: EMDB REMARK 900 PDB-ID 9D73 REMARK 900 RELATED ID: EMD-46602 RELATED DB: EMDB REMARK 900 PDB-ID 9D74 REMARK 900 RELATED ID: EMD-70276 RELATED DB: EMDB REMARK 900 CRYOEM STRUCTURE OF ANTI-MHC-I MAB B1.23.2 FC DOMAINS DBREF 9OA9 J 1 443 PDB 9OA9 9OA9 1 443 DBREF 9OA9 K 1 443 PDB 9OA9 9OA9 1 443 SEQRES 1 J 443 GLN VAL GLN LEU GLN GLN SER GLY THR VAL LEU ALA ARG SEQRES 2 J 443 PRO GLY SER SER VAL LYS MET SER CYS LYS ALA SER GLY SEQRES 3 J 443 TYR SER PHE THR SER TYR TRP MET HIS TRP VAL LYS GLN SEQRES 4 J 443 ARG PRO GLY GLN GLY LEU GLU TRP ILE GLY ALA ILE TYR SEQRES 5 J 443 PRO GLY ASN SER ASP ALA THR TYR ASN GLN LYS PHE LYS SEQRES 6 J 443 GLY LYS ALA LYS LEU THR ALA VAL THR SER ALA ASN THR SEQRES 7 J 443 ALA TYR MET GLU LEU SER SER LEU THR ASN GLU ASP SER SEQRES 8 J 443 ALA VAL TYR TYR CYS THR ASN TYR PHE ASP GLN TRP GLY SEQRES 9 J 443 GLN GLY THR THR LEU THR VAL SER SER ALA SER THR LYS SEQRES 10 J 443 GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER SEQRES 11 J 443 THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS SEQRES 12 J 443 ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER SEQRES 13 J 443 GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL SEQRES 14 J 443 LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL SEQRES 15 J 443 THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE SEQRES 16 J 443 CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP SEQRES 17 J 443 LYS LYS VAL GLU PRO LYS SER CYS ASP LYS THR HIS THR SEQRES 18 J 443 CYS PRO PRO CYS PRO ALA PRO GLU ALA ALA GLY GLY PRO SEQRES 19 J 443 SER VAL PHE LEU PHE PRO PRO LYS PRO LYS ASP THR LEU SEQRES 20 J 443 MET ILE SER ARG THR PRO GLU VAL THR CYS VAL VAL VAL SEQRES 21 J 443 ASP VAL SER HIS GLU ASP PRO GLU VAL LYS PHE ASN TRP SEQRES 22 J 443 TYR VAL ASP GLY VAL GLU VAL HIS ASN ALA LYS THR LYS SEQRES 23 J 443 PRO ARG GLU GLU GLN TYR ASN SER THR TYR ARG VAL VAL SEQRES 24 J 443 SER VAL LEU THR VAL LEU HIS GLN ASP TRP LEU ASN GLY SEQRES 25 J 443 LYS GLU TYR LYS CYS LYS VAL SER ASN LYS ALA LEU GLY SEQRES 26 J 443 ALA PRO ILE GLU LYS THR ILE SER LYS ALA LYS GLY GLN SEQRES 27 J 443 PRO ARG GLU PRO GLN VAL TYR THR LEU PRO PRO SER ARG SEQRES 28 J 443 GLU GLU MET THR LYS ASN GLN VAL SER LEU THR CYS LEU SEQRES 29 J 443 VAL LYS GLY PHE TYR PRO SER ASP ILE ALA VAL GLU TRP SEQRES 30 J 443 GLU SER ASN GLY GLN PRO GLU ASN ASN TYR LYS THR THR SEQRES 31 J 443 PRO PRO VAL LEU ASP SER ASP GLY SER PHE PHE LEU TYR SEQRES 32 J 443 SER LYS LEU THR VAL ASP LYS SER ARG TRP GLN GLN GLY SEQRES 33 J 443 ASN VAL PHE SER CYS SER VAL MET HIS GLU ALA LEU HIS SEQRES 34 J 443 ASN HIS TYR THR GLN LYS SER LEU SER LEU SER PRO GLY SEQRES 35 J 443 LYS SEQRES 1 K 443 GLN VAL GLN LEU GLN GLN SER GLY THR VAL LEU ALA ARG SEQRES 2 K 443 PRO GLY SER SER VAL LYS MET SER CYS LYS ALA SER GLY SEQRES 3 K 443 TYR SER PHE THR SER TYR TRP MET HIS TRP VAL LYS GLN SEQRES 4 K 443 ARG PRO GLY GLN GLY LEU GLU TRP ILE GLY ALA ILE TYR SEQRES 5 K 443 PRO GLY ASN SER ASP ALA THR TYR ASN GLN LYS PHE LYS SEQRES 6 K 443 GLY LYS ALA LYS LEU THR ALA VAL THR SER ALA ASN THR SEQRES 7 K 443 ALA TYR MET GLU LEU SER SER LEU THR ASN GLU ASP SER SEQRES 8 K 443 ALA VAL TYR TYR CYS THR ASN TYR PHE ASP GLN TRP GLY SEQRES 9 K 443 GLN GLY THR THR LEU THR VAL SER SER ALA SER THR LYS SEQRES 10 K 443 GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER SEQRES 11 K 443 THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS SEQRES 12 K 443 ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER SEQRES 13 K 443 GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL SEQRES 14 K 443 LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL SEQRES 15 K 443 THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE SEQRES 16 K 443 CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP SEQRES 17 K 443 LYS LYS VAL GLU PRO LYS SER CYS ASP LYS THR HIS THR SEQRES 18 K 443 CYS PRO PRO CYS PRO ALA PRO GLU ALA ALA GLY GLY PRO SEQRES 19 K 443 SER VAL PHE LEU PHE PRO PRO LYS PRO LYS ASP THR LEU SEQRES 20 K 443 MET ILE SER ARG THR PRO GLU VAL THR CYS VAL VAL VAL SEQRES 21 K 443 ASP VAL SER HIS GLU ASP PRO GLU VAL LYS PHE ASN TRP SEQRES 22 K 443 TYR VAL ASP GLY VAL GLU VAL HIS ASN ALA LYS THR LYS SEQRES 23 K 443 PRO ARG GLU GLU GLN TYR ASN SER THR TYR ARG VAL VAL SEQRES 24 K 443 SER VAL LEU THR VAL LEU HIS GLN ASP TRP LEU ASN GLY SEQRES 25 K 443 LYS GLU TYR LYS CYS LYS VAL SER ASN LYS ALA LEU GLY SEQRES 26 K 443 ALA PRO ILE GLU LYS THR ILE SER LYS ALA LYS GLY GLN SEQRES 27 K 443 PRO ARG GLU PRO GLN VAL TYR THR LEU PRO PRO SER ARG SEQRES 28 K 443 GLU GLU MET THR LYS ASN GLN VAL SER LEU THR CYS LEU SEQRES 29 K 443 VAL LYS GLY PHE TYR PRO SER ASP ILE ALA VAL GLU TRP SEQRES 30 K 443 GLU SER ASN GLY GLN PRO GLU ASN ASN TYR LYS THR THR SEQRES 31 K 443 PRO PRO VAL LEU ASP SER ASP GLY SER PHE PHE LEU TYR SEQRES 32 K 443 SER LYS LEU THR VAL ASP LYS SER ARG TRP GLN GLN GLY SEQRES 33 K 443 ASN VAL PHE SER CYS SER VAL MET HIS GLU ALA LEU HIS SEQRES 34 K 443 ASN HIS TYR THR GLN LYS SER LEU SER LEU SER PRO GLY SEQRES 35 K 443 LYS HET NAG X 1 14 HET NAG X 2 14 HET MAN X 3 11 HET MAN X 4 11 HET NAG X 5 14 HET GAL X 6 11 HET NAG Y 1 14 HET NAG Y 2 14 HET MAN Y 3 11 HET MAN Y 4 11 HET NAG Y 5 14 HET GAL Y 6 11 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM MAN ALPHA-D-MANNOPYRANOSE HETNAM GAL BETA-D-GALACTOPYRANOSE 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 MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE HETSYN GAL BETA-D-GALACTOSE; D-GALACTOSE; GALACTOSE FORMUL 3 NAG 6(C8 H15 N O6) FORMUL 3 MAN 4(C6 H12 O6) FORMUL 3 GAL 2(C6 H12 O6) HELIX 1 AA1 SER J 186 THR J 191 1 6 HELIX 2 AA2 LYS J 410 GLN J 415 1 6 HELIX 3 AA3 LYS K 242 LEU K 247 5 6 SHEET 1 AA1 2 SER J 235 PHE J 239 0 SHEET 2 AA1 2 THR J 256 VAL J 260 -1 O THR J 256 N PHE J 239 SHEET 1 AA2 2 ALA J 283 LYS J 286 0 SHEET 2 AA2 2 VAL J 299 LEU J 302 -1 O VAL J 301 N LYS J 284 SHEET 1 AA3 2 TYR J 315 CYS J 317 0 SHEET 2 AA3 2 LYS J 330 ILE J 332 -1 O ILE J 332 N TYR J 315 SHEET 1 AA4 3 GLN J 343 LEU J 347 0 SHEET 2 AA4 3 GLN J 358 PHE J 368 -1 O THR J 362 N LEU J 347 SHEET 3 AA4 3 PHE J 400 ASP J 409 -1 O VAL J 408 N VAL J 359 SHEET 1 AA5 2 CYS K 317 VAL K 319 0 SHEET 2 AA5 2 ILE K 328 LYS K 330 -1 O LYS K 330 N CYS K 317 SHEET 1 AA6 3 GLN K 343 LEU K 347 0 SHEET 2 AA6 3 LEU K 361 LYS K 366 -1 O THR K 362 N LEU K 347 SHEET 3 AA6 3 LEU K 402 LEU K 406 -1 O LEU K 402 N VAL K 365 SHEET 1 AA7 2 ALA K 374 GLU K 376 0 SHEET 2 AA7 2 SER K 422 MET K 424 -1 O SER K 422 N GLU K 376 SSBOND 1 CYS J 140 CYS J 196 1555 1555 2.03 SSBOND 2 CYS J 222 CYS K 225 1555 1555 2.17 SSBOND 3 CYS J 225 CYS K 222 1555 1555 2.13 SSBOND 4 CYS J 257 CYS J 317 1555 1555 2.03 SSBOND 5 CYS K 257 CYS K 317 1555 1555 2.03 SSBOND 6 CYS K 363 CYS K 421 1555 1555 2.03 LINK ND2 ASN J 293 C1 NAG X 1 1555 1555 1.49 LINK ND2 ASN K 293 C1 NAG Y 1 1555 1555 1.48 LINK O4 NAG X 1 C1 NAG X 2 1555 1555 1.44 LINK O4 NAG X 2 C1 MAN X 3 1555 1555 1.40 LINK O3 MAN X 3 C1 MAN X 4 1555 1555 1.45 LINK O2 MAN X 4 C1 NAG X 5 1555 1555 1.45 LINK O4 NAG X 5 C1 GAL X 6 1555 1555 1.45 LINK O4 NAG Y 1 C1 NAG Y 2 1555 1555 1.44 LINK O4 NAG Y 2 C1 MAN Y 3 1555 1555 1.44 LINK O4 MAN Y 3 C1 MAN Y 4 1555 1555 1.44 LINK O2 MAN Y 4 C1 NAG Y 5 1555 1555 1.44 LINK O4 NAG Y 5 C1 GAL Y 6 1555 1555 1.45 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