HEADER IMMUNE SYSTEM 06-NOV-25 9T5Z TITLE CRYO-EM STRUCTURE OF ALPHAM/BETA2:MEM148-FAB HEADPIECE COMPLEX TITLE 2 (WITHOUT ALPHAM I-DOMAIN) COMPND MOL_ID: 1; COMPND 2 MOLECULE: INTEGRIN ALPHA-M; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: CD11 ANTIGEN-LIKE FAMILY MEMBER B,CR-3 ALPHA CHAIN,CELL COMPND 5 SURFACE GLYCOPROTEIN MAC-1 SUBUNIT ALPHA,LEUKOCYTE ADHESION RECEPTOR COMPND 6 MO1,NEUTROPHIL ADHERENCE RECEPTOR; COMPND 7 ENGINEERED: YES; COMPND 8 MOL_ID: 2; COMPND 9 MOLECULE: INTEGRIN BETA-2; COMPND 10 CHAIN: B; COMPND 11 SYNONYM: CELL SURFACE ADHESION GLYCOPROTEINS LFA-1/CR3/P150,95 COMPND 12 SUBUNIT BETA,COMPLEMENT RECEPTOR C3 SUBUNIT BETA; COMPND 13 ENGINEERED: YES; COMPND 14 MOL_ID: 3; COMPND 15 MOLECULE: MURINE IGG1 MEM148 HEAVY CHAIN; COMPND 16 CHAIN: H; COMPND 17 ENGINEERED: YES; COMPND 18 MOL_ID: 4; COMPND 19 MOLECULE: ANTI-COLORECTAL CARCINOMA LIGHT CHAIN; COMPND 20 CHAIN: L; COMPND 21 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: ITGAM, CD11B, CR3A; SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_COMMON: HUMAN; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 GENE: ITGB2, CD18, MFI7; SOURCE 13 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 15 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 17 ORGANISM_TAXID: 10090; SOURCE 18 EXPRESSION_SYSTEM: MUS MUSCULUS; SOURCE 19 EXPRESSION_SYSTEM_TAXID: 10090; SOURCE 20 MOL_ID: 4; SOURCE 21 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 22 ORGANISM_TAXID: 10090; SOURCE 23 EXPRESSION_SYSTEM: MUS MUSCULUS; SOURCE 24 EXPRESSION_SYSTEM_TAXID: 10090 KEYWDS PHAGOCYTOSIS, INTEGRIN, OPSONISATION, IMMUNE SYSTEM EXPDTA ELECTRON MICROSCOPY AUTHOR J.LORENTZEN,G.R.ANDERSEN REVDAT 1 25-MAR-26 9T5Z 0 JRNL AUTH J.LORENTZEN,G.R.ANDERSEN JRNL TITL CRYO-EM STRUCTURE OF ALPHAM/BETA2:MEM148-FAB HEADPIECE JRNL TITL 2 COMPLEX (WITHOUT ALPHAM I-DOMAIN) JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.10 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : CRYOSPARC, EPU, RELION, 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 : FLEXIBLE FIT 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) : 3.100 REMARK 3 NUMBER OF PARTICLES : 188421 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 9T5Z COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-NOV-25. REMARK 100 THE DEPOSITION ID IS D_1292151860. 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 : HEADPIECE OF ALPHAM/BETA2 IN REMARK 245 COMPLEX WITH MEM148 FAB REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 0.15 REMARK 245 SAMPLE SUPPORT DETAILS : 25 MA CURRENT REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.50 REMARK 245 SAMPLE DETAILS : HEADPIECE OF ALPHAM/BETA2 IN REMARK 245 COMPLEX WITH MEM148 FAB-FRAGMENT FROM MOUSE IGG1 REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : TFS KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 (6K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 800.00 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 : 2.70 REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 6000.00 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : 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, B, H, L, C, D, E, F 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 GLU A 131 REMARK 465 ASP A 132 REMARK 465 SER A 133 REMARK 465 ASP A 134 REMARK 465 ILE A 135 REMARK 465 ALA A 136 REMARK 465 PHE A 137 REMARK 465 LEU A 138 REMARK 465 ILE A 139 REMARK 465 ASP A 140 REMARK 465 GLY A 141 REMARK 465 SER A 142 REMARK 465 GLY A 143 REMARK 465 SER A 144 REMARK 465 ILE A 145 REMARK 465 ILE A 146 REMARK 465 PRO A 147 REMARK 465 HIS A 148 REMARK 465 ASP A 149 REMARK 465 PHE A 150 REMARK 465 ARG A 151 REMARK 465 ARG A 152 REMARK 465 MET A 153 REMARK 465 LYS A 154 REMARK 465 GLU A 155 REMARK 465 PHE A 156 REMARK 465 VAL A 157 REMARK 465 SER A 158 REMARK 465 THR A 159 REMARK 465 VAL A 160 REMARK 465 MET A 161 REMARK 465 GLU A 162 REMARK 465 GLN A 163 REMARK 465 LEU A 164 REMARK 465 LYS A 165 REMARK 465 LYS A 166 REMARK 465 SER A 167 REMARK 465 LYS A 168 REMARK 465 THR A 169 REMARK 465 LEU A 170 REMARK 465 PHE A 171 REMARK 465 SER A 172 REMARK 465 LEU A 173 REMARK 465 MET A 174 REMARK 465 GLN A 175 REMARK 465 TYR A 176 REMARK 465 SER A 177 REMARK 465 GLU A 178 REMARK 465 GLU A 179 REMARK 465 PHE A 180 REMARK 465 ARG A 181 REMARK 465 ILE A 182 REMARK 465 HIS A 183 REMARK 465 PHE A 184 REMARK 465 THR A 185 REMARK 465 PHE A 186 REMARK 465 LYS A 187 REMARK 465 GLU A 188 REMARK 465 PHE A 189 REMARK 465 GLN A 190 REMARK 465 ASN A 191 REMARK 465 ASN A 192 REMARK 465 PRO A 193 REMARK 465 ASN A 194 REMARK 465 PRO A 195 REMARK 465 ARG A 196 REMARK 465 SER A 197 REMARK 465 LEU A 198 REMARK 465 VAL A 199 REMARK 465 LYS A 200 REMARK 465 PRO A 201 REMARK 465 ILE A 202 REMARK 465 THR A 203 REMARK 465 GLN A 204 REMARK 465 LEU A 205 REMARK 465 LEU A 206 REMARK 465 GLY A 207 REMARK 465 ARG A 208 REMARK 465 THR A 209 REMARK 465 HIS A 210 REMARK 465 THR A 211 REMARK 465 ALA A 212 REMARK 465 THR A 213 REMARK 465 GLY A 214 REMARK 465 ILE A 215 REMARK 465 ARG A 216 REMARK 465 LYS A 217 REMARK 465 VAL A 218 REMARK 465 VAL A 219 REMARK 465 ARG A 220 REMARK 465 GLU A 221 REMARK 465 LEU A 222 REMARK 465 PHE A 223 REMARK 465 ARG A 224 REMARK 465 ILE A 225 REMARK 465 THR A 226 REMARK 465 ASN A 227 REMARK 465 GLY A 228 REMARK 465 ALA A 229 REMARK 465 ARG A 230 REMARK 465 LYS A 231 REMARK 465 ASN A 232 REMARK 465 ALA A 233 REMARK 465 PHE A 234 REMARK 465 LYS A 235 REMARK 465 ILE A 236 REMARK 465 LEU A 237 REMARK 465 VAL A 238 REMARK 465 VAL A 239 REMARK 465 ILE A 240 REMARK 465 THR A 241 REMARK 465 ASP A 242 REMARK 465 GLY A 243 REMARK 465 GLU A 244 REMARK 465 LYS A 245 REMARK 465 PHE A 246 REMARK 465 GLY A 247 REMARK 465 ASP A 248 REMARK 465 PRO A 249 REMARK 465 LEU A 250 REMARK 465 GLY A 251 REMARK 465 TYR A 252 REMARK 465 GLU A 253 REMARK 465 ASP A 254 REMARK 465 VAL A 255 REMARK 465 ILE A 256 REMARK 465 PRO A 257 REMARK 465 GLU A 258 REMARK 465 ALA A 259 REMARK 465 ASP A 260 REMARK 465 ARG A 261 REMARK 465 GLU A 262 REMARK 465 GLY A 263 REMARK 465 VAL A 264 REMARK 465 ILE A 265 REMARK 465 ARG A 266 REMARK 465 TYR A 267 REMARK 465 VAL A 268 REMARK 465 ILE A 269 REMARK 465 GLY A 270 REMARK 465 VAL A 271 REMARK 465 GLY A 272 REMARK 465 ASP A 273 REMARK 465 ALA A 274 REMARK 465 PHE A 275 REMARK 465 ARG A 276 REMARK 465 SER A 277 REMARK 465 GLU A 278 REMARK 465 LYS A 279 REMARK 465 SER A 280 REMARK 465 ARG A 281 REMARK 465 GLN A 282 REMARK 465 GLU A 283 REMARK 465 LEU A 284 REMARK 465 ASN A 285 REMARK 465 THR A 286 REMARK 465 ILE A 287 REMARK 465 ALA A 288 REMARK 465 SER A 289 REMARK 465 LYS A 290 REMARK 465 PRO A 291 REMARK 465 PRO A 292 REMARK 465 ARG A 293 REMARK 465 ASP A 294 REMARK 465 HIS A 295 REMARK 465 VAL A 296 REMARK 465 PHE A 297 REMARK 465 GLN A 298 REMARK 465 VAL A 299 REMARK 465 ASN A 300 REMARK 465 ASN A 301 REMARK 465 PHE A 302 REMARK 465 GLU A 303 REMARK 465 ALA A 304 REMARK 465 LEU A 305 REMARK 465 LYS A 306 REMARK 465 THR A 307 REMARK 465 ILE A 308 REMARK 465 GLN A 309 REMARK 465 ASN A 310 REMARK 465 GLN A 311 REMARK 465 LEU A 312 REMARK 465 ARG A 313 REMARK 465 GLU A 751 REMARK 465 LYS A 752 REMARK 465 ASN A 753 REMARK 465 THR A 754 REMARK 465 GLY A 755 REMARK 465 GLY A 756 REMARK 465 LEU A 757 REMARK 465 GLU A 758 REMARK 465 VAL A 759 REMARK 465 LEU A 760 REMARK 465 PHE A 761 REMARK 465 GLN A 762 REMARK 465 GLN B 1 REMARK 465 GLU B 2 REMARK 465 CYS B 3 REMARK 465 THR B 4 REMARK 465 LYS B 5 REMARK 465 PHE B 6 REMARK 465 LYS B 7 REMARK 465 VAL B 8 REMARK 465 SER B 9 REMARK 465 SER B 10 REMARK 465 CYS B 11 REMARK 465 ARG B 12 REMARK 465 GLU B 13 REMARK 465 CYS B 14 REMARK 465 ILE B 15 REMARK 465 GLU B 16 REMARK 465 SER B 17 REMARK 465 GLY B 18 REMARK 465 PRO B 19 REMARK 465 GLY B 20 REMARK 465 CYS B 21 REMARK 465 THR B 22 REMARK 465 TRP B 23 REMARK 465 CYS B 24 REMARK 465 GLN B 25 REMARK 465 LYS B 26 REMARK 465 LEU B 27 REMARK 465 ASN B 28 REMARK 465 PHE B 29 REMARK 465 THR B 30 REMARK 465 GLY B 31 REMARK 465 PRO B 32 REMARK 465 GLY B 33 REMARK 465 ASP B 34 REMARK 465 PRO B 35 REMARK 465 ASP B 36 REMARK 465 SER B 37 REMARK 465 ILE B 38 REMARK 465 ARG B 39 REMARK 465 CYS B 40 REMARK 465 ASP B 41 REMARK 465 THR B 42 REMARK 465 ARG B 43 REMARK 465 PRO B 44 REMARK 465 GLN B 45 REMARK 465 LEU B 46 REMARK 465 LEU B 47 REMARK 465 MET B 48 REMARK 465 ARG B 49 REMARK 465 GLY B 50 REMARK 465 CYS B 51 REMARK 465 ALA B 52 REMARK 465 ALA B 53 REMARK 465 ASP B 54 REMARK 465 ASP B 55 REMARK 465 ILE B 56 REMARK 465 MET B 57 REMARK 465 ASP B 58 REMARK 465 PRO B 59 REMARK 465 GLU B 424 REMARK 465 CYS B 425 REMARK 465 ARG B 426 REMARK 465 CYS B 427 REMARK 465 ARG B 428 REMARK 465 ASP B 429 REMARK 465 GLN B 430 REMARK 465 SER B 431 REMARK 465 ARG B 432 REMARK 465 ASP B 433 REMARK 465 ARG B 434 REMARK 465 SER B 435 REMARK 465 LEU B 436 REMARK 465 CYS B 437 REMARK 465 HIS B 438 REMARK 465 GLY B 439 REMARK 465 LYS B 440 REMARK 465 GLY B 441 REMARK 465 PHE B 442 REMARK 465 LEU B 443 REMARK 465 GLU B 444 REMARK 465 CYS B 445 REMARK 465 GLY B 446 REMARK 465 ILE B 447 REMARK 465 CYS B 448 REMARK 465 ARG B 449 REMARK 465 CYS B 450 REMARK 465 ASP B 451 REMARK 465 THR B 452 REMARK 465 GLY B 453 REMARK 465 TYR B 454 REMARK 465 ILE B 455 REMARK 465 GLY B 456 REMARK 465 LYS B 457 REMARK 465 ASN B 458 REMARK 465 CYS B 459 REMARK 465 GLU B 460 REMARK 465 PRO B 461 REMARK 465 ALA B 462 REMARK 465 ALA B 463 REMARK 465 LEU B 464 REMARK 465 GLN B 465 REMARK 465 THR B 466 REMARK 465 LEU B 467 REMARK 465 PHE B 468 REMARK 465 GLN B 469 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 THR A 682 CG2 REMARK 470 THR A 692 CG2 REMARK 470 THR A 694 CG2 REMARK 470 THR A 697 CG2 REMARK 470 THR A 724 CG2 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 CYS A 638 CB CYS A 638 SG 0.183 REMARK 500 CYS A 695 CB CYS A 695 SG -0.101 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 PRO A 83 C - N - CD ANGL. DEV. = -13.2 DEGREES REMARK 500 ASP A 380 CB - CG - OD1 ANGL. DEV. = 8.4 DEGREES REMARK 500 CYS A 638 CA - CB - SG ANGL. DEV. = 13.2 DEGREES REMARK 500 CYS A 695 CA - CB - SG ANGL. DEV. = 18.9 DEGREES REMARK 500 CYS A 705 CA - CB - SG ANGL. DEV. = 17.9 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 SER A 28 33.25 -140.06 REMARK 500 PRO A 83 90.15 30.17 REMARK 500 THR A 92 49.11 -97.11 REMARK 500 LEU A 125 52.27 -90.69 REMARK 500 ARG A 126 -126.24 55.57 REMARK 500 ILE A 316 -73.33 70.34 REMARK 500 PHE A 317 146.34 70.01 REMARK 500 GLU A 320 -143.35 63.57 REMARK 500 THR A 322 44.90 33.32 REMARK 500 ASN A 375 -66.53 -125.13 REMARK 500 MET A 376 -171.88 177.89 REMARK 500 ASP A 380 -17.58 75.89 REMARK 500 ILE A 413 -59.73 -125.21 REMARK 500 GLN A 469 -74.69 67.62 REMARK 500 ALA A 526 75.62 -160.39 REMARK 500 ALA A 616 -5.59 73.93 REMARK 500 PHE A 620 49.58 -86.42 REMARK 500 ASN A 623 32.28 -99.81 REMARK 500 GLU A 631 159.48 65.09 REMARK 500 VAL A 710 -56.62 -127.54 REMARK 500 VAL B 150 -68.17 -126.98 REMARK 500 THR B 153 54.34 -96.30 REMARK 500 ASN B 167 77.03 -156.24 REMARK 500 ASN B 171 -6.64 69.64 REMARK 500 LYS B 172 41.74 -104.66 REMARK 500 LYS B 174 -158.26 -149.31 REMARK 500 HIS B 265 21.04 -140.63 REMARK 500 SER B 343 -175.94 58.53 REMARK 500 LEU B 347 118.80 -160.58 REMARK 500 ASN B 372 61.63 62.26 REMARK 500 TYR H 42 40.63 -96.05 REMARK 500 ASP H 100 9.34 59.14 REMARK 500 ALA H 102 -132.14 45.75 REMARK 500 PRO H 192 31.66 -82.55 REMARK 500 ALA L 51 -7.61 74.66 REMARK 500 LYS L 52 -38.61 -130.10 REMARK 500 ASP L 82 55.86 -93.30 REMARK 500 ALA L 130 109.06 -161.12 REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 MN B2001 MN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLU A 320 OE1 REMARK 620 2 SER B 114 OG 106.7 REMARK 620 3 SER B 116 OG 84.4 102.4 REMARK 620 4 GLU B 212 OE2 99.1 94.3 161.3 REMARK 620 5 HOH B2101 O 93.4 159.7 81.5 79.9 REMARK 620 6 HOH B2102 O 167.2 81.6 84.3 89.8 79.0 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A1203 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 449 OD1 REMARK 620 2 ASP A 451 OD1 73.7 REMARK 620 3 ASN A 453 OD1 93.5 74.3 REMARK 620 4 SER A 455 O 71.3 140.1 89.1 REMARK 620 5 ASP A 457 OD1 118.8 134.4 139.9 80.5 REMARK 620 6 ASP A 457 OD2 94.2 81.4 151.3 119.6 55.4 REMARK 620 7 HOH A1303 O 167.9 96.5 76.7 115.0 73.0 91.2 REMARK 620 N 1 2 3 4 5 6 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A1202 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 513 OD1 REMARK 620 2 ASN A 515 OD1 92.7 REMARK 620 3 ASP A 517 OD1 73.1 75.9 REMARK 620 4 LEU A 519 O 85.7 172.2 96.4 REMARK 620 5 ASP A 521 OD1 150.8 100.6 135.2 84.2 REMARK 620 6 ASP A 521 OD2 105.8 86.1 161.8 101.7 50.2 REMARK 620 7 HOH A1302 O 137.4 99.8 70.8 76.6 65.8 115.6 REMARK 620 N 1 2 3 4 5 6 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A1201 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 576 OD1 REMARK 620 2 THR A 578 OG1 86.7 REMARK 620 3 ASP A 580 OD1 83.0 70.5 REMARK 620 4 LEU A 582 O 83.5 168.0 114.9 REMARK 620 5 ASP A 584 OD1 128.6 84.3 138.9 96.4 REMARK 620 6 ASP A 584 OD2 79.6 85.5 151.0 85.9 49.3 REMARK 620 7 HOH A1301 O 145.8 76.4 63.4 115.6 79.6 127.3 REMARK 620 N 1 2 3 4 5 6 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA B2002 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 SER B 116 O REMARK 620 2 ASP B 119 OD1 80.4 REMARK 620 3 ASP B 120 OD2 89.0 70.2 REMARK 620 4 ASP B 242 OD2 85.8 145.7 78.3 REMARK 620 5 HOH B2103 O 163.6 111.4 84.8 78.1 REMARK 620 6 HOH B2104 O 86.9 88.0 158.2 122.6 104.4 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA B2003 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP B 151 OD2 REMARK 620 2 ASN B 207 OD1 98.2 REMARK 620 3 ASP B 209 O 161.4 75.5 REMARK 620 4 ASP B 209 OD1 88.4 91.9 74.4 REMARK 620 5 PRO B 211 O 90.1 170.6 97.8 92.7 REMARK 620 6 GLU B 212 OE1 99.6 88.4 97.8 171.8 85.9 REMARK 620 N 1 2 3 4 5 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-55599 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF ALPHAM/BETA2:MEM148-FAB HEADPIECE COMPLEX REMARK 900 (WITHOUT ALPHAM I-DOMAIN) DBREF 9T5Z A 1 755 UNP P11215 ITAM_HUMAN 17 771 DBREF 9T5Z B 1 463 UNP P05107 ITB2_HUMAN 23 485 DBREF 9T5Z H 1 218 PDB 9T5Z 9T5Z 1 218 DBREF 9T5Z L 1 214 PDB 9T5Z 9T5Z 1 214 SEQADV 9T5Z ARG A 224 UNP P11215 ASN 240 ENGINEERED MUTATION SEQADV 9T5Z THR A 485 UNP P11215 ALA 501 ENGINEERED MUTATION SEQADV 9T5Z ARG A 680 UNP P11215 ASN 696 ENGINEERED MUTATION SEQADV 9T5Z THR A 754 UNP P11215 CYS 770 ENGINEERED MUTATION SEQADV 9T5Z GLY A 756 UNP P11215 EXPRESSION TAG SEQADV 9T5Z LEU A 757 UNP P11215 EXPRESSION TAG SEQADV 9T5Z GLU A 758 UNP P11215 EXPRESSION TAG SEQADV 9T5Z VAL A 759 UNP P11215 EXPRESSION TAG SEQADV 9T5Z LEU A 760 UNP P11215 EXPRESSION TAG SEQADV 9T5Z PHE A 761 UNP P11215 EXPRESSION TAG SEQADV 9T5Z GLN A 762 UNP P11215 EXPRESSION TAG SEQADV 9T5Z PRO B 461 UNP P05107 CYS 483 ENGINEERED MUTATION SEQADV 9T5Z ALA B 462 UNP P05107 GLN 484 ENGINEERED MUTATION SEQADV 9T5Z ALA B 463 UNP P05107 THR 485 ENGINEERED MUTATION SEQADV 9T5Z LEU B 464 UNP P05107 EXPRESSION TAG SEQADV 9T5Z GLN B 465 UNP P05107 EXPRESSION TAG SEQADV 9T5Z THR B 466 UNP P05107 EXPRESSION TAG SEQADV 9T5Z LEU B 467 UNP P05107 EXPRESSION TAG SEQADV 9T5Z PHE B 468 UNP P05107 EXPRESSION TAG SEQADV 9T5Z GLN B 469 UNP P05107 EXPRESSION TAG SEQRES 1 A 762 PHE ASN LEU ASP THR GLU ASN ALA MET THR PHE GLN GLU SEQRES 2 A 762 ASN ALA ARG GLY PHE GLY GLN SER VAL VAL GLN LEU GLN SEQRES 3 A 762 GLY SER ARG VAL VAL VAL GLY ALA PRO GLN GLU ILE VAL SEQRES 4 A 762 ALA ALA ASN GLN ARG GLY SER LEU TYR GLN CYS ASP TYR SEQRES 5 A 762 SER THR GLY SER CYS GLU PRO ILE ARG LEU GLN VAL PRO SEQRES 6 A 762 VAL GLU ALA VAL ASN MET SER LEU GLY LEU SER LEU ALA SEQRES 7 A 762 ALA THR THR SER PRO PRO GLN LEU LEU ALA CYS GLY PRO SEQRES 8 A 762 THR VAL HIS GLN THR CYS SER GLU ASN THR TYR VAL LYS SEQRES 9 A 762 GLY LEU CYS PHE LEU PHE GLY SER ASN LEU ARG GLN GLN SEQRES 10 A 762 PRO GLN LYS PHE PRO GLU ALA LEU ARG GLY CYS PRO GLN SEQRES 11 A 762 GLU ASP SER ASP ILE ALA PHE LEU ILE ASP GLY SER GLY SEQRES 12 A 762 SER ILE ILE PRO HIS ASP PHE ARG ARG MET LYS GLU PHE SEQRES 13 A 762 VAL SER THR VAL MET GLU GLN LEU LYS LYS SER LYS THR SEQRES 14 A 762 LEU PHE SER LEU MET GLN TYR SER GLU GLU PHE ARG ILE SEQRES 15 A 762 HIS PHE THR PHE LYS GLU PHE GLN ASN ASN PRO ASN PRO SEQRES 16 A 762 ARG SER LEU VAL LYS PRO ILE THR GLN LEU LEU GLY ARG SEQRES 17 A 762 THR HIS THR ALA THR GLY ILE ARG LYS VAL VAL ARG GLU SEQRES 18 A 762 LEU PHE ARG ILE THR ASN GLY ALA ARG LYS ASN ALA PHE SEQRES 19 A 762 LYS ILE LEU VAL VAL ILE THR ASP GLY GLU LYS PHE GLY SEQRES 20 A 762 ASP PRO LEU GLY TYR GLU ASP VAL ILE PRO GLU ALA ASP SEQRES 21 A 762 ARG GLU GLY VAL ILE ARG TYR VAL ILE GLY VAL GLY ASP SEQRES 22 A 762 ALA PHE ARG SER GLU LYS SER ARG GLN GLU LEU ASN THR SEQRES 23 A 762 ILE ALA SER LYS PRO PRO ARG ASP HIS VAL PHE GLN VAL SEQRES 24 A 762 ASN ASN PHE GLU ALA LEU LYS THR ILE GLN ASN GLN LEU SEQRES 25 A 762 ARG GLU LYS ILE PHE ALA ILE GLU GLY THR GLN THR GLY SEQRES 26 A 762 SER SER SER SER PHE GLU HIS GLU MET SER GLN GLU GLY SEQRES 27 A 762 PHE SER ALA ALA ILE THR SER ASN GLY PRO LEU LEU SER SEQRES 28 A 762 THR VAL GLY SER TYR ASP TRP ALA GLY GLY VAL PHE LEU SEQRES 29 A 762 TYR THR SER LYS GLU LYS SER THR PHE ILE ASN MET THR SEQRES 30 A 762 ARG VAL ASP SER ASP MET ASN ASP ALA TYR LEU GLY TYR SEQRES 31 A 762 ALA ALA ALA ILE ILE LEU ARG ASN ARG VAL GLN SER LEU SEQRES 32 A 762 VAL LEU GLY ALA PRO ARG TYR GLN HIS ILE GLY LEU VAL SEQRES 33 A 762 ALA MET PHE ARG GLN ASN THR GLY MET TRP GLU SER ASN SEQRES 34 A 762 ALA ASN VAL LYS GLY THR GLN ILE GLY ALA TYR PHE GLY SEQRES 35 A 762 ALA SER LEU CYS SER VAL ASP VAL ASP SER ASN GLY SER SEQRES 36 A 762 THR ASP LEU VAL LEU ILE GLY ALA PRO HIS TYR TYR GLU SEQRES 37 A 762 GLN THR ARG GLY GLY GLN VAL SER VAL CYS PRO LEU PRO SEQRES 38 A 762 ARG GLY ARG THR ARG TRP GLN CYS ASP ALA VAL LEU TYR SEQRES 39 A 762 GLY GLU GLN GLY GLN PRO TRP GLY ARG PHE GLY ALA ALA SEQRES 40 A 762 LEU THR VAL LEU GLY ASP VAL ASN GLY ASP LYS LEU THR SEQRES 41 A 762 ASP VAL ALA ILE GLY ALA PRO GLY GLU GLU ASP ASN ARG SEQRES 42 A 762 GLY ALA VAL TYR LEU PHE HIS GLY THR SER GLY SER GLY SEQRES 43 A 762 ILE SER PRO SER HIS SER GLN ARG ILE ALA GLY SER LYS SEQRES 44 A 762 LEU SER PRO ARG LEU GLN TYR PHE GLY GLN SER LEU SER SEQRES 45 A 762 GLY GLY GLN ASP LEU THR MET ASP GLY LEU VAL ASP LEU SEQRES 46 A 762 THR VAL GLY ALA GLN GLY HIS VAL LEU LEU LEU ARG SER SEQRES 47 A 762 GLN PRO VAL LEU ARG VAL LYS ALA ILE MET GLU PHE ASN SEQRES 48 A 762 PRO ARG GLU VAL ALA ARG ASN VAL PHE GLU CYS ASN ASP SEQRES 49 A 762 GLN VAL VAL LYS GLY LYS GLU ALA GLY GLU VAL ARG VAL SEQRES 50 A 762 CYS LEU HIS VAL GLN LYS SER THR ARG ASP ARG LEU ARG SEQRES 51 A 762 GLU GLY GLN ILE GLN SER VAL VAL THR TYR ASP LEU ALA SEQRES 52 A 762 LEU ASP SER GLY ARG PRO HIS SER ARG ALA VAL PHE ASN SEQRES 53 A 762 GLU THR LYS ARG SER THR ARG ARG GLN THR GLN VAL LEU SEQRES 54 A 762 GLY LEU THR GLN THR CYS GLU THR LEU LYS LEU GLN LEU SEQRES 55 A 762 PRO ASN CYS ILE GLU ASP PRO VAL SER PRO ILE VAL LEU SEQRES 56 A 762 ARG LEU ASN PHE SER LEU VAL GLY THR PRO LEU SER ALA SEQRES 57 A 762 PHE GLY ASN LEU ARG PRO VAL LEU ALA GLU ASP ALA GLN SEQRES 58 A 762 ARG LEU PHE THR ALA LEU PHE PRO PHE GLU LYS ASN THR SEQRES 59 A 762 GLY GLY LEU GLU VAL LEU PHE GLN SEQRES 1 B 469 GLN GLU CYS THR LYS PHE LYS VAL SER SER CYS ARG GLU SEQRES 2 B 469 CYS ILE GLU SER GLY PRO GLY CYS THR TRP CYS GLN LYS SEQRES 3 B 469 LEU ASN PHE THR GLY PRO GLY ASP PRO ASP SER ILE ARG SEQRES 4 B 469 CYS ASP THR ARG PRO GLN LEU LEU MET ARG GLY CYS ALA SEQRES 5 B 469 ALA ASP ASP ILE MET ASP PRO THR SER LEU ALA GLU THR SEQRES 6 B 469 GLN GLU ASP HIS ASN GLY GLY GLN LYS GLN LEU SER PRO SEQRES 7 B 469 GLN LYS VAL THR LEU TYR LEU ARG PRO GLY GLN ALA ALA SEQRES 8 B 469 ALA PHE ASN VAL THR PHE ARG ARG ALA LYS GLY TYR PRO SEQRES 9 B 469 ILE ASP LEU TYR TYR LEU MET ASP LEU SER TYR SER MET SEQRES 10 B 469 LEU ASP ASP LEU ARG ASN VAL LYS LYS LEU GLY GLY ASP SEQRES 11 B 469 LEU LEU ARG ALA LEU ASN GLU ILE THR GLU SER GLY ARG SEQRES 12 B 469 ILE GLY PHE GLY SER PHE VAL ASP LYS THR VAL LEU PRO SEQRES 13 B 469 PHE VAL ASN THR HIS PRO ASP LYS LEU ARG ASN PRO CYS SEQRES 14 B 469 PRO ASN LYS GLU LYS GLU CYS GLN PRO PRO PHE ALA PHE SEQRES 15 B 469 ARG HIS VAL LEU LYS LEU THR ASN ASN SER ASN GLN PHE SEQRES 16 B 469 GLN THR GLU VAL GLY LYS GLN LEU ILE SER GLY ASN LEU SEQRES 17 B 469 ASP ALA PRO GLU GLY GLY LEU ASP ALA MET MET GLN VAL SEQRES 18 B 469 ALA ALA CYS PRO GLU GLU ILE GLY TRP ARG ASN VAL THR SEQRES 19 B 469 ARG LEU LEU VAL PHE ALA THR ASP ASP GLY PHE HIS PHE SEQRES 20 B 469 ALA GLY ASP GLY LYS LEU GLY ALA ILE LEU THR PRO ASN SEQRES 21 B 469 ASP GLY ARG CYS HIS LEU GLU ASP ASN LEU TYR LYS ARG SEQRES 22 B 469 SER ASN GLU PHE ASP TYR PRO SER VAL GLY GLN LEU ALA SEQRES 23 B 469 HIS LYS LEU ALA GLU ASN ASN ILE GLN PRO ILE PHE ALA SEQRES 24 B 469 VAL THR SER ARG MET VAL LYS THR TYR GLU LYS LEU THR SEQRES 25 B 469 GLU ILE ILE PRO LYS SER ALA VAL GLY GLU LEU SER GLU SEQRES 26 B 469 ASP SER SER ASN VAL VAL HIS LEU ILE LYS ASN ALA TYR SEQRES 27 B 469 ASN LYS LEU SER SER ARG VAL PHE LEU ASP HIS ASN ALA SEQRES 28 B 469 LEU PRO ASP THR LEU LYS VAL THR TYR ASP SER PHE CYS SEQRES 29 B 469 SER ASN GLY VAL THR HIS ARG ASN GLN PRO ARG GLY ASP SEQRES 30 B 469 CYS ASP GLY VAL GLN ILE ASN VAL PRO ILE THR PHE GLN SEQRES 31 B 469 VAL LYS VAL THR ALA THR GLU CYS ILE GLN GLU GLN SER SEQRES 32 B 469 PHE VAL ILE ARG ALA LEU GLY PHE THR ASP ILE VAL THR SEQRES 33 B 469 VAL GLN VAL LEU PRO GLN CYS GLU CYS ARG CYS ARG ASP SEQRES 34 B 469 GLN SER ARG ASP ARG SER LEU CYS HIS GLY LYS GLY PHE SEQRES 35 B 469 LEU GLU CYS GLY ILE CYS ARG CYS ASP THR GLY TYR ILE SEQRES 36 B 469 GLY LYS ASN CYS GLU PRO ALA ALA LEU GLN THR LEU PHE SEQRES 37 B 469 GLN SEQRES 1 H 218 GLU VAL GLN LEU GLN GLU SER GLY PRO SER LEU VAL LYS SEQRES 2 H 218 PRO SER GLN THR LEU SER LEU THR CYS SER VAL THR GLY SEQRES 3 H 218 ASP SER ILE THR SER GLY TYR TRP ASN TRP ILE ARG LYS SEQRES 4 H 218 PHE PRO TYR ASN LYS LEU GLU TYR MET GLY TYR ILE SER SEQRES 5 H 218 TYR SER GLY SER THR TYR TYR ASN PRO SER LEU GLU SER SEQRES 6 H 218 ARG VAL SER ILE THR ARG ASP THR SER LYS ASN GLN TYR SEQRES 7 H 218 TYR LEU GLN LEU HIS SER VAL THR THR GLU ASP THR ALA SEQRES 8 H 218 THR TYR HIS CYS ALA ARG GLU ARG ASP TYR ALA PHE ASP SEQRES 9 H 218 PHE TRP GLY GLN GLY THR THR LEU THR VAL SER SER ALA SEQRES 10 H 218 LYS THR THR PRO PRO SER VAL TYR PRO LEU ALA PRO GLY SEQRES 11 H 218 SER ALA ALA GLN THR ASN SER MET VAL THR LEU GLY CYS SEQRES 12 H 218 LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL THR VAL THR SEQRES 13 H 218 TRP ASN SER GLY SER LEU SER SER GLY VAL HIS THR PHE SEQRES 14 H 218 PRO ALA VAL LEU GLN SER ASP LEU TYR THR LEU SER SER SEQRES 15 H 218 SER VAL THR VAL PRO SER SER PRO ARG PRO SER GLU THR SEQRES 16 H 218 VAL THR CYS ASN VAL ALA HIS PRO ALA SER SER THR LYS SEQRES 17 H 218 VAL ASP LYS LYS ILE VAL PRO ARG ASP CYS SEQRES 1 L 214 ASP ILE LYS MET THR GLN SER PRO SER PRO MET TYR ALA SEQRES 2 L 214 SER LEU GLY GLU ARG VAL THR VAL THR CYS LYS ALA SER SEQRES 3 L 214 GLN ASP ILE ASN ASN TYR LEU SER TRP PHE GLN GLN LYS SEQRES 4 L 214 PRO GLY LYS SER PRO LYS THR LEU ILE TYR ARG ALA LYS SEQRES 5 L 214 ARG LEU VAL ASP GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 L 214 GLY SER GLY GLN ASP TYR SER LEU THR ILE SER SER LEU SEQRES 7 L 214 GLU TYR GLU ASP MET GLY ILE TYR TYR CYS LEU GLN TYR SEQRES 8 L 214 ASP GLU PHE PRO LEU THR PHE GLY ALA GLY THR LYS LEU SEQRES 9 L 214 GLU LEU LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE SEQRES 10 L 214 PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA SEQRES 11 L 214 SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP SEQRES 12 L 214 ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN SEQRES 13 L 214 ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS SEQRES 14 L 214 ASP SER THR TYR SER MET SER SER THR LEU THR LEU THR SEQRES 15 L 214 LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU SEQRES 16 L 214 ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER SEQRES 17 L 214 PHE ASN ARG ASN GLU CYS HET NAG C 1 26 HET NAG C 2 26 HET BMA C 3 21 HET NAG D 1 26 HET NAG D 2 26 HET BMA D 3 19 HET MAN D 4 21 HET MAN D 5 21 HET NAG E 1 26 HET NAG E 2 26 HET BMA E 3 19 HET MAN E 4 21 HET MAN E 5 21 HET NAG F 1 14 HET NAG F 2 14 HET CA A1201 1 HET CA A1202 1 HET CA A1203 1 HET MN B2001 1 HET CA B2002 1 HET CA B2003 1 HET NAG B2004 27 HET NAG B2005 27 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BMA BETA-D-MANNOPYRANOSE HETNAM MAN ALPHA-D-MANNOPYRANOSE HETNAM CA CALCIUM ION HETNAM MN MANGANESE (II) ION 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 HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE FORMUL 5 NAG 10(C8 H15 N O6) FORMUL 5 BMA 3(C6 H12 O6) FORMUL 6 MAN 4(C6 H12 O6) FORMUL 9 CA 5(CA 2+) FORMUL 12 MN MN 2+ FORMUL 17 HOH *7(H2 O) HELIX 1 AA1 GLY A 354 ALA A 359 1 6 HELIX 2 AA2 ARG A 409 ILE A 413 5 5 HELIX 3 AA3 GLY A 528 ARG A 533 1 6 HELIX 4 AA4 SER B 114 ASP B 119 5 6 HELIX 5 AA5 ASP B 120 THR B 139 1 20 HELIX 6 AA6 ASN B 191 GLN B 202 1 12 HELIX 7 AA7 GLY B 213 ALA B 223 1 11 HELIX 8 AA8 CYS B 224 GLY B 229 1 6 HELIX 9 AA9 GLY B 249 ALA B 255 5 7 HELIX 10 AB1 TYR B 271 PHE B 277 5 7 HELIX 11 AB2 SER B 281 ASN B 293 1 13 HELIX 12 AB3 MET B 304 GLU B 313 1 10 HELIX 13 AB4 SER B 327 ASN B 339 1 13 HELIX 14 AB5 THR H 86 THR H 90 5 5 HELIX 15 AB6 PRO H 203 SER H 206 5 4 HELIX 16 AB7 SER L 121 SER L 127 1 7 HELIX 17 AB8 LYS L 183 HIS L 189 1 7 HELIX 18 AB9 ASN L 212 CYS L 214 5 3 SHEET 1 AA1 4 MET A 9 PHE A 11 0 SHEET 2 AA1 4 HIS A 592 ARG A 597 -1 O LEU A 595 N MET A 9 SHEET 3 AA1 4 ASP A 584 ALA A 589 -1 N VAL A 587 O LEU A 594 SHEET 4 AA1 4 LEU A 571 GLY A 573 -1 N SER A 572 O THR A 586 SHEET 1 AA2 4 SER A 21 GLN A 24 0 SHEET 2 AA2 4 ARG A 29 GLY A 33 -1 O VAL A 31 N VAL A 23 SHEET 3 AA2 4 LEU A 47 ASP A 51 -1 O CYS A 50 N VAL A 30 SHEET 4 AA2 4 CYS A 57 PRO A 59 -1 O GLU A 58 N GLN A 49 SHEET 1 AA3 2 ILE A 38 ALA A 40 0 SHEET 2 AA3 2 GLN A 43 ARG A 44 -1 O GLN A 43 N VAL A 39 SHEET 1 AA4 4 SER A 76 THR A 80 0 SHEET 2 AA4 4 GLN A 85 THR A 96 -1 O CYS A 89 N SER A 76 SHEET 3 AA4 4 THR A 101 PHE A 110 -1 O TYR A 102 N GLN A 95 SHEET 4 AA4 4 GLN A 119 LYS A 120 -1 O GLN A 119 N LEU A 109 SHEET 1 AA5 4 ALA A 342 ILE A 343 0 SHEET 2 AA5 4 PRO A 348 SER A 351 -1 O LEU A 349 N ALA A 342 SHEET 3 AA5 4 VAL A 362 TYR A 365 -1 O PHE A 363 N LEU A 350 SHEET 4 AA5 4 SER A 371 ILE A 374 -1 O THR A 372 N LEU A 364 SHEET 1 AA6 4 ALA A 391 LEU A 396 0 SHEET 2 AA6 4 GLN A 401 ALA A 407 -1 O SER A 402 N ILE A 395 SHEET 3 AA6 4 LEU A 415 ASN A 422 -1 O PHE A 419 N LEU A 403 SHEET 4 AA6 4 MET A 425 LYS A 433 -1 O ALA A 430 N MET A 418 SHEET 1 AA7 4 LEU A 445 VAL A 448 0 SHEET 2 AA7 4 LEU A 458 TYR A 467 -1 O LEU A 460 N CYS A 446 SHEET 3 AA7 4 GLY A 472 PRO A 479 -1 O CYS A 478 N VAL A 459 SHEET 4 AA7 4 ALA A 491 LEU A 493 -1 O LEU A 493 N VAL A 475 SHEET 1 AA8 4 LEU A 508 GLY A 512 0 SHEET 2 AA8 4 ASP A 521 GLY A 525 -1 O ALA A 523 N THR A 509 SHEET 3 AA8 4 ALA A 535 PHE A 539 -1 O TYR A 537 N ILE A 524 SHEET 4 AA8 4 GLN A 553 ALA A 556 -1 O GLN A 553 N LEU A 538 SHEET 1 AA9 2 GLY A 541 THR A 542 0 SHEET 2 AA9 2 GLY A 546 ILE A 547 -1 O GLY A 546 N THR A 542 SHEET 1 AB1 4 THR A 694 LEU A 698 0 SHEET 2 AB1 4 VAL A 635 LYS A 643 -1 N VAL A 637 O GLU A 696 SHEET 3 AB1 4 VAL A 601 GLU A 609 -1 N LYS A 605 O HIS A 640 SHEET 4 AB1 4 VAL A 735 LEU A 736 1 O VAL A 735 N LEU A 602 SHEET 1 AB2 3 GLY A 629 LYS A 630 0 SHEET 2 AB2 3 LEU A 700 PRO A 703 -1 O LEU A 702 N LYS A 630 SHEET 3 AB2 3 VAL A 674 PHE A 675 -1 N VAL A 674 O GLN A 701 SHEET 1 AB3 4 ARG A 683 LEU A 689 0 SHEET 2 AB3 4 SER A 656 LEU A 664 -1 N SER A 656 O LEU A 689 SHEET 3 AB3 4 ILE A 713 GLY A 723 -1 O ASN A 718 N ASP A 661 SHEET 4 AB3 4 PHE A 744 PHE A 748 -1 O ALA A 746 N LEU A 715 SHEET 1 AB4 6 LEU B 62 GLN B 66 0 SHEET 2 AB4 6 LYS B 80 TYR B 84 -1 O LYS B 80 N GLN B 66 SHEET 3 AB4 6 ILE B 414 LEU B 420 1 O GLN B 418 N VAL B 81 SHEET 4 AB4 6 GLN B 402 ALA B 408 -1 N PHE B 404 O VAL B 417 SHEET 5 AB4 6 ARG B 344 HIS B 349 -1 N ASP B 348 O ARG B 407 SHEET 6 AB4 6 GLY B 376 ASP B 379 -1 O CYS B 378 N VAL B 345 SHEET 1 AB5 5 LEU B 76 SER B 77 0 SHEET 2 AB5 5 ALA B 90 PHE B 97 -1 O THR B 96 N SER B 77 SHEET 3 AB5 5 ILE B 387 ALA B 395 -1 O ILE B 387 N PHE B 97 SHEET 4 AB5 5 LEU B 356 PHE B 363 -1 N ASP B 361 O GLN B 390 SHEET 5 AB5 5 THR B 369 GLN B 373 -1 O GLN B 373 N TYR B 360 SHEET 1 AB6 6 ARG B 183 THR B 189 0 SHEET 2 AB6 6 GLY B 142 PHE B 149 -1 N PHE B 146 O LEU B 186 SHEET 3 AB6 6 ILE B 105 ASP B 112 1 N TYR B 109 O GLY B 147 SHEET 4 AB6 6 THR B 234 THR B 241 1 O LEU B 236 N TYR B 108 SHEET 5 AB6 6 ILE B 294 VAL B 300 1 O GLN B 295 N LEU B 237 SHEET 6 AB6 6 VAL B 320 GLU B 322 1 O GLY B 321 N PHE B 298 SHEET 1 AB7 4 GLN H 3 SER H 7 0 SHEET 2 AB7 4 LEU H 18 THR H 25 -1 O THR H 25 N GLN H 3 SHEET 3 AB7 4 GLN H 77 LEU H 82 -1 O TYR H 78 N CYS H 22 SHEET 4 AB7 4 VAL H 67 ASP H 72 -1 N THR H 70 O TYR H 79 SHEET 1 AB8 6 LEU H 11 VAL H 12 0 SHEET 2 AB8 6 THR H 110 VAL H 114 1 O THR H 113 N VAL H 12 SHEET 3 AB8 6 ALA H 91 GLU H 98 -1 N TYR H 93 O THR H 110 SHEET 4 AB8 6 TYR H 33 PHE H 40 -1 N ASN H 35 O ALA H 96 SHEET 5 AB8 6 LYS H 44 ILE H 51 -1 O ILE H 51 N TRP H 34 SHEET 6 AB8 6 THR H 57 TYR H 59 -1 O TYR H 58 N TYR H 50 SHEET 1 AB9 4 SER H 123 LEU H 127 0 SHEET 2 AB9 4 MET H 138 TYR H 148 -1 O LEU H 144 N TYR H 125 SHEET 3 AB9 4 LEU H 177 PRO H 187 -1 O VAL H 184 N LEU H 141 SHEET 4 AB9 4 VAL H 166 THR H 168 -1 N HIS H 167 O SER H 183 SHEET 1 AC1 4 SER H 123 LEU H 127 0 SHEET 2 AC1 4 MET H 138 TYR H 148 -1 O LEU H 144 N TYR H 125 SHEET 3 AC1 4 LEU H 177 PRO H 187 -1 O VAL H 184 N LEU H 141 SHEET 4 AC1 4 VAL H 172 GLN H 174 -1 N GLN H 174 O LEU H 177 SHEET 1 AC2 3 THR H 154 TRP H 157 0 SHEET 2 AC2 3 THR H 197 HIS H 202 -1 O ASN H 199 N THR H 156 SHEET 3 AC2 3 THR H 207 LYS H 212 -1 O VAL H 209 N VAL H 200 SHEET 1 AC3 4 MET L 4 SER L 7 0 SHEET 2 AC3 4 VAL L 19 ALA L 25 -1 O LYS L 24 N THR L 5 SHEET 3 AC3 4 ASP L 70 ILE L 75 -1 O TYR L 71 N CYS L 23 SHEET 4 AC3 4 PHE L 62 SER L 67 -1 N SER L 65 O SER L 72 SHEET 1 AC4 5 MET L 11 TYR L 12 0 SHEET 2 AC4 5 THR L 102 GLU L 105 1 O GLU L 105 N MET L 11 SHEET 3 AC4 5 ILE L 85 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AC4 5 LEU L 33 GLN L 38 -1 N PHE L 36 O TYR L 87 SHEET 5 AC4 5 LYS L 45 TYR L 49 -1 O ILE L 48 N TRP L 35 SHEET 1 AC5 4 THR L 114 PHE L 118 0 SHEET 2 AC5 4 GLY L 129 PHE L 139 -1 O VAL L 133 N PHE L 118 SHEET 3 AC5 4 TYR L 173 THR L 182 -1 O LEU L 181 N ALA L 130 SHEET 4 AC5 4 VAL L 159 TRP L 163 -1 N SER L 162 O SER L 176 SHEET 1 AC6 4 SER L 153 ARG L 155 0 SHEET 2 AC6 4 ASN L 145 ILE L 150 -1 N ILE L 150 O SER L 153 SHEET 3 AC6 4 SER L 191 HIS L 198 -1 O THR L 193 N LYS L 149 SHEET 4 AC6 4 SER L 201 ASN L 210 -1 O LYS L 207 N CYS L 194 SSBOND 1 CYS A 50 CYS A 57 1555 1555 2.03 SSBOND 2 CYS A 89 CYS A 107 1555 1555 2.03 SSBOND 3 CYS A 97 CYS A 128 1555 1555 2.04 SSBOND 4 CYS A 478 CYS A 489 1555 1555 2.04 SSBOND 5 CYS A 622 CYS A 705 1555 1555 2.03 SSBOND 6 CYS A 638 CYS A 695 1555 1555 2.07 SSBOND 7 CYS B 169 CYS B 176 1555 1555 2.03 SSBOND 8 CYS B 224 CYS B 264 1555 1555 2.03 SSBOND 9 CYS B 364 CYS B 378 1555 1555 2.03 SSBOND 10 CYS B 398 CYS B 423 1555 1555 2.03 SSBOND 11 CYS H 22 CYS H 95 1555 1555 2.04 SSBOND 12 CYS H 143 CYS H 198 1555 1555 2.03 SSBOND 13 CYS H 218 CYS L 214 1555 1555 2.03 SSBOND 14 CYS L 23 CYS L 88 1555 1555 2.04 SSBOND 15 CYS L 134 CYS L 194 1555 1555 2.04 LINK ND2 ASN A 70 C1 NAG D 1 1555 1555 1.44 LINK ND2 ASN A 375 C1 NAG E 1 1555 1555 1.43 LINK ND2 ASN A 718 C1 NAG C 1 1555 1555 1.46 LINK ND2 ASN B 94 C1 NAG F 1 1555 1555 1.55 LINK ND2 ASN B 190 C1 NAG B2004 1555 1555 1.44 LINK ND2 ASN B 232 C1 NAG B2005 1555 1555 1.44 LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.45 LINK O4 NAG C 2 C1 BMA C 3 1555 1555 1.45 LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.44 LINK O4 NAG D 2 C1 BMA D 3 1555 1555 1.44 LINK O3 BMA D 3 C1 MAN D 4 1555 1555 1.45 LINK O6 BMA D 3 C1 MAN D 5 1555 1555 1.45 LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.44 LINK O4 NAG E 2 C1 BMA E 3 1555 1555 1.45 LINK O3 BMA E 3 C1 MAN E 4 1555 1555 1.46 LINK O6 BMA E 3 C1 MAN E 5 1555 1555 1.44 LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.39 LINK OE1 GLU A 320 MN MN B2001 1555 1555 2.07 LINK OD1 ASP A 449 CA CA A1203 1555 1555 2.29 LINK OD1 ASP A 451 CA CA A1203 1555 1555 2.27 LINK OD1 ASN A 453 CA CA A1203 1555 1555 2.32 LINK O SER A 455 CA CA A1203 1555 1555 2.27 LINK OD1 ASP A 457 CA CA A1203 1555 1555 2.29 LINK OD2 ASP A 457 CA CA A1203 1555 1555 2.41 LINK OD1 ASP A 513 CA CA A1202 1555 1555 3.11 LINK OD1 ASN A 515 CA CA A1202 1555 1555 2.28 LINK OD1 ASP A 517 CA CA A1202 1555 1555 2.34 LINK O LEU A 519 CA CA A1202 1555 1555 2.23 LINK OD1 ASP A 521 CA CA A1202 1555 1555 2.54 LINK OD2 ASP A 521 CA CA A1202 1555 1555 2.59 LINK OD1 ASP A 576 CA CA A1201 1555 1555 2.38 LINK OG1 THR A 578 CA CA A1201 1555 1555 2.22 LINK OD1 ASP A 580 CA CA A1201 1555 1555 2.37 LINK O LEU A 582 CA CA A1201 1555 1555 2.20 LINK OD1 ASP A 584 CA CA A1201 1555 1555 2.78 LINK OD2 ASP A 584 CA CA A1201 1555 1555 2.33 LINK CA CA A1201 O HOH A1301 1555 1555 2.29 LINK CA CA A1202 O HOH A1302 1555 1555 2.26 LINK CA CA A1203 O HOH A1303 1555 1555 2.29 LINK OG SER B 114 MN MN B2001 1555 1555 2.07 LINK OG SER B 116 MN MN B2001 1555 1555 2.02 LINK O SER B 116 CA CA B2002 1555 1555 2.25 LINK OD1 ASP B 119 CA CA B2002 1555 1555 2.28 LINK OD2 ASP B 120 CA CA B2002 1555 1555 2.32 LINK OD2 ASP B 151 CA CA B2003 1555 1555 2.25 LINK OD1 ASN B 207 CA CA B2003 1555 1555 2.20 LINK O ASP B 209 CA CA B2003 1555 1555 2.28 LINK OD1 ASP B 209 CA CA B2003 1555 1555 2.27 LINK O PRO B 211 CA CA B2003 1555 1555 2.21 LINK OE2 GLU B 212 MN MN B2001 1555 1555 2.02 LINK OE1 GLU B 212 CA CA B2003 1555 1555 2.29 LINK OD2 ASP B 242 CA CA B2002 1555 1555 2.25 LINK MN MN B2001 O HOH B2101 1555 1555 2.15 LINK MN MN B2001 O HOH B2102 1555 1555 2.09 LINK CA CA B2002 O HOH B2103 1555 1555 2.24 LINK CA CA B2002 O HOH B2104 1555 1555 2.28 CISPEP 1 SER B 77 PRO B 78 0 -2.04 CISPEP 2 PHE H 149 PRO H 150 0 -9.82 CISPEP 3 GLU H 151 PRO H 152 0 -8.71 CISPEP 4 ARG H 191 PRO H 192 0 -11.03 CISPEP 5 SER L 7 PRO L 8 0 -10.56 CISPEP 6 SER L 9 PRO L 10 0 -8.12 CISPEP 7 PHE L 94 PRO L 95 0 1.07 CISPEP 8 TYR L 140 PRO L 141 0 0.55 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