HEADER VIRAL PROTEIN 02-DEC-24 9EKF TITLE CRYOEM STRUCTURE OF H5N1 A/TEXAS/37/2024 HA BOUND TO FAB 65C6 AND AN TITLE 2 AUTO GLYCAN OCCUPYING THE RECEPTOR-BINDING SITE COMPND MOL_ID: 1; COMPND 2 MOLECULE: HEMAGGLUTININ; COMPND 3 CHAIN: A, B, C; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: FAB 65C6 HEAVY CHAIN; COMPND 7 CHAIN: D, G, H; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: FAB 65C6 LIGHT CHAIN; COMPND 11 CHAIN: I, K, L; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS; SOURCE 3 ORGANISM_TAXID: 11320; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 9 ORGANISM_COMMON: HUMAN; SOURCE 10 ORGANISM_TAXID: 9606; 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: HOMO SAPIENS; SOURCE 16 ORGANISM_COMMON: HUMAN; SOURCE 17 ORGANISM_TAXID: 9606; SOURCE 18 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 19 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 20 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS H5N1, ANTIBODY, INFLUENZA, VIRAL PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR N.C.MORANO,L.SHAPIRO,P.D.KWONG REVDAT 1 18-DEC-24 9EKF 0 JRNL AUTH N.C.MORANO,Y.GUO,J.E.BECKER,Z.LI,J.YU,D.D.HO,L.SHAPIRO, JRNL AUTH 2 P.D.KWONG JRNL TITL STRUCTURE OF A ZOONOTIC H5N1 HEMAGGLUTININ REVEALS A JRNL TITL 2 RECEPTOR-BINDING SITE OCCUPIED BY AN AUTO-GLYCAN JRNL REF BIORXIV 2024 JRNL REFN ISSN 2692-8205 JRNL DOI 10.1101/2024.12.06.626699 REMARK 2 REMARK 2 RESOLUTION. 2.68 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : 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) : 2.680 REMARK 3 NUMBER OF PARTICLES : 206541 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 9EKF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-DEC-24. REMARK 100 THE DEPOSITION ID IS D_1000290490. 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 HEMAGGLUTININ FROM REMARK 245 H5N1 HA A/TEXAS/37/2024 WITH REMARK 245 ANTIBODY 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 : 7.40 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : TFS KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 (6K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 800.00 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 : 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: NONAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, G, H, I, K, L, E, REMARK 350 AND CHAINS: F, J 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 -11 REMARK 465 GLU A -10 REMARK 465 ASN A -9 REMARK 465 ILE A -8 REMARK 465 VAL A -7 REMARK 465 LEU A -6 REMARK 465 LEU A -5 REMARK 465 LEU A -4 REMARK 465 ALA A -3 REMARK 465 ILE A -2 REMARK 465 VAL A -1 REMARK 465 SER A 0 REMARK 465 LEU A 1 REMARK 465 VAL A 2 REMARK 465 LYS A 3 REMARK 465 SER A 4 REMARK 465 LEU A 328 REMARK 465 ARG A 329 REMARK 465 ARG A 330 REMARK 465 ARG A 331 REMARK 465 ARG A 332 REMARK 465 ARG A 333 REMARK 465 ARG A 334 REMARK 465 GLY A 335 REMARK 465 GLY A 506 REMARK 465 SER A 507 REMARK 465 SER A 508 REMARK 465 GLY A 509 REMARK 465 SER A 510 REMARK 465 SER A 511 REMARK 465 GLY A 512 REMARK 465 TYR A 513 REMARK 465 ILE A 514 REMARK 465 PRO A 515 REMARK 465 GLU A 516 REMARK 465 ALA A 517 REMARK 465 PRO A 518 REMARK 465 ARG A 519 REMARK 465 ASP A 520 REMARK 465 GLY A 521 REMARK 465 GLN A 522 REMARK 465 ALA A 523 REMARK 465 TYR A 524 REMARK 465 VAL A 525 REMARK 465 ARG A 526 REMARK 465 LYS A 527 REMARK 465 ASP A 528 REMARK 465 GLY A 529 REMARK 465 GLU A 530 REMARK 465 TRP A 531 REMARK 465 VAL A 532 REMARK 465 LEU A 533 REMARK 465 LEU A 534 REMARK 465 SER A 535 REMARK 465 THR A 536 REMARK 465 PHE A 537 REMARK 465 LEU A 538 REMARK 465 GLY A 539 REMARK 465 HIS A 540 REMARK 465 HIS A 541 REMARK 465 HIS A 542 REMARK 465 HIS A 543 REMARK 465 HIS A 544 REMARK 465 HIS A 545 REMARK 465 HIS A 546 REMARK 465 HIS A 547 REMARK 465 HIS A 548 REMARK 465 GLY A 549 REMARK 465 GLY A 550 REMARK 465 SER A 551 REMARK 465 GLY A 552 REMARK 465 LEU A 553 REMARK 465 ASN A 554 REMARK 465 ASP A 555 REMARK 465 ILE A 556 REMARK 465 PHE A 557 REMARK 465 GLU A 558 REMARK 465 ALA A 559 REMARK 465 GLN A 560 REMARK 465 LYS A 561 REMARK 465 ILE A 562 REMARK 465 GLU A 563 REMARK 465 TRP A 564 REMARK 465 HIS A 565 REMARK 465 GLU A 566 REMARK 465 MET B -11 REMARK 465 GLU B -10 REMARK 465 ASN B -9 REMARK 465 ILE B -8 REMARK 465 VAL B -7 REMARK 465 LEU B -6 REMARK 465 LEU B -5 REMARK 465 LEU B -4 REMARK 465 ALA B -3 REMARK 465 ILE B -2 REMARK 465 VAL B -1 REMARK 465 SER B 0 REMARK 465 LEU B 1 REMARK 465 VAL B 2 REMARK 465 LYS B 3 REMARK 465 SER B 4 REMARK 465 LEU B 336 REMARK 465 ARG B 337 REMARK 465 ARG B 338 REMARK 465 ARG B 339 REMARK 465 ARG B 340 REMARK 465 ARG B 341 REMARK 465 ARG B 342 REMARK 465 GLY B 343 REMARK 465 GLY B 514 REMARK 465 SER B 515 REMARK 465 SER B 516 REMARK 465 GLY B 517 REMARK 465 SER B 518 REMARK 465 SER B 519 REMARK 465 GLY B 520 REMARK 465 TYR B 521 REMARK 465 ILE B 522 REMARK 465 PRO B 523 REMARK 465 GLU B 524 REMARK 465 ALA B 525 REMARK 465 PRO B 526 REMARK 465 ARG B 527 REMARK 465 ASP B 528 REMARK 465 GLY B 529 REMARK 465 GLN B 530 REMARK 465 ALA B 531 REMARK 465 TYR B 532 REMARK 465 VAL B 533 REMARK 465 ARG B 534 REMARK 465 LYS B 535 REMARK 465 ASP B 536 REMARK 465 GLY B 537 REMARK 465 GLU B 538 REMARK 465 TRP B 539 REMARK 465 VAL B 540 REMARK 465 LEU B 541 REMARK 465 LEU B 542 REMARK 465 SER B 543 REMARK 465 THR B 544 REMARK 465 PHE B 545 REMARK 465 LEU B 546 REMARK 465 GLY B 547 REMARK 465 HIS B 548 REMARK 465 HIS B 549 REMARK 465 HIS B 550 REMARK 465 HIS B 551 REMARK 465 HIS B 552 REMARK 465 HIS B 553 REMARK 465 HIS B 554 REMARK 465 HIS B 555 REMARK 465 HIS B 556 REMARK 465 GLY B 557 REMARK 465 GLY B 558 REMARK 465 SER B 559 REMARK 465 GLY B 560 REMARK 465 LEU B 561 REMARK 465 ASN B 562 REMARK 465 ASP B 563 REMARK 465 ILE B 564 REMARK 465 PHE B 565 REMARK 465 GLU B 566 REMARK 465 ALA B 567 REMARK 465 GLN B 568 REMARK 465 LYS B 569 REMARK 465 ILE B 570 REMARK 465 GLU B 571 REMARK 465 TRP B 572 REMARK 465 HIS B 573 REMARK 465 GLU B 574 REMARK 465 MET C -11 REMARK 465 GLU C -10 REMARK 465 ASN C -9 REMARK 465 ILE C -8 REMARK 465 VAL C -7 REMARK 465 LEU C -6 REMARK 465 LEU C -5 REMARK 465 LEU C -4 REMARK 465 ALA C -3 REMARK 465 ILE C -2 REMARK 465 VAL C -1 REMARK 465 SER C 0 REMARK 465 LEU C 1 REMARK 465 VAL C 2 REMARK 465 LYS C 3 REMARK 465 SER C 4 REMARK 465 LEU C 336 REMARK 465 ARG C 337 REMARK 465 ARG C 338 REMARK 465 ARG C 339 REMARK 465 ARG C 340 REMARK 465 ARG C 341 REMARK 465 ARG C 342 REMARK 465 GLY C 343 REMARK 465 GLY C 514 REMARK 465 SER C 515 REMARK 465 SER C 516 REMARK 465 GLY C 517 REMARK 465 SER C 518 REMARK 465 SER C 519 REMARK 465 GLY C 520 REMARK 465 TYR C 521 REMARK 465 ILE C 522 REMARK 465 PRO C 523 REMARK 465 GLU C 524 REMARK 465 ALA C 525 REMARK 465 PRO C 526 REMARK 465 ARG C 527 REMARK 465 ASP C 528 REMARK 465 GLY C 529 REMARK 465 GLN C 530 REMARK 465 ALA C 531 REMARK 465 TYR C 532 REMARK 465 VAL C 533 REMARK 465 ARG C 534 REMARK 465 LYS C 535 REMARK 465 ASP C 536 REMARK 465 GLY C 537 REMARK 465 GLU C 538 REMARK 465 TRP C 539 REMARK 465 VAL C 540 REMARK 465 LEU C 541 REMARK 465 LEU C 542 REMARK 465 SER C 543 REMARK 465 THR C 544 REMARK 465 PHE C 545 REMARK 465 LEU C 546 REMARK 465 GLY C 547 REMARK 465 HIS C 548 REMARK 465 HIS C 549 REMARK 465 HIS C 550 REMARK 465 HIS C 551 REMARK 465 HIS C 552 REMARK 465 HIS C 553 REMARK 465 HIS C 554 REMARK 465 HIS C 555 REMARK 465 HIS C 556 REMARK 465 GLY C 557 REMARK 465 GLY C 558 REMARK 465 SER C 559 REMARK 465 GLY C 560 REMARK 465 LEU C 561 REMARK 465 ASN C 562 REMARK 465 ASP C 563 REMARK 465 ILE C 564 REMARK 465 PHE C 565 REMARK 465 GLU C 566 REMARK 465 ALA C 567 REMARK 465 GLN C 568 REMARK 465 LYS C 569 REMARK 465 ILE C 570 REMARK 465 GLU C 571 REMARK 465 TRP C 572 REMARK 465 HIS C 573 REMARK 465 GLU C 574 REMARK 465 GLU D 1 REMARK 465 GLY D 106 REMARK 465 THR D 107 REMARK 465 LEU D 108 REMARK 465 VAL D 109 REMARK 465 THR D 110 REMARK 465 VAL D 111 REMARK 465 SER D 112 REMARK 465 SER D 113 REMARK 465 ALA D 114 REMARK 465 SER D 115 REMARK 465 THR D 116 REMARK 465 LYS D 117 REMARK 465 GLY D 118 REMARK 465 PRO D 119 REMARK 465 SER D 120 REMARK 465 VAL D 121 REMARK 465 PHE D 122 REMARK 465 PRO D 123 REMARK 465 LEU D 124 REMARK 465 ALA D 125 REMARK 465 PRO D 126 REMARK 465 SER D 127 REMARK 465 SER D 128 REMARK 465 LYS D 129 REMARK 465 SER D 130 REMARK 465 THR D 131 REMARK 465 SER D 132 REMARK 465 GLY D 133 REMARK 465 GLY D 134 REMARK 465 THR D 135 REMARK 465 ALA D 136 REMARK 465 ALA D 137 REMARK 465 LEU D 138 REMARK 465 GLY D 139 REMARK 465 CYS D 140 REMARK 465 LEU D 141 REMARK 465 VAL D 142 REMARK 465 LYS D 143 REMARK 465 ASP D 144 REMARK 465 TYR D 145 REMARK 465 PHE D 146 REMARK 465 PRO D 147 REMARK 465 GLU D 148 REMARK 465 PRO D 149 REMARK 465 VAL D 150 REMARK 465 THR D 151 REMARK 465 VAL D 152 REMARK 465 SER D 153 REMARK 465 TRP D 154 REMARK 465 ASN D 155 REMARK 465 SER D 156 REMARK 465 GLY D 157 REMARK 465 ALA D 158 REMARK 465 LEU D 159 REMARK 465 THR D 160 REMARK 465 SER D 161 REMARK 465 GLY D 162 REMARK 465 VAL D 163 REMARK 465 HIS D 164 REMARK 465 THR D 165 REMARK 465 PHE D 166 REMARK 465 PRO D 167 REMARK 465 ALA D 168 REMARK 465 VAL D 169 REMARK 465 LEU D 170 REMARK 465 GLN D 171 REMARK 465 SER D 172 REMARK 465 SER D 173 REMARK 465 GLY D 174 REMARK 465 LEU D 175 REMARK 465 TYR D 176 REMARK 465 SER D 177 REMARK 465 LEU D 178 REMARK 465 SER D 179 REMARK 465 SER D 180 REMARK 465 VAL D 181 REMARK 465 VAL D 182 REMARK 465 THR D 183 REMARK 465 VAL D 184 REMARK 465 PRO D 185 REMARK 465 SER D 186 REMARK 465 SER D 187 REMARK 465 SER D 188 REMARK 465 LEU D 189 REMARK 465 GLY D 190 REMARK 465 THR D 191 REMARK 465 GLN D 192 REMARK 465 THR D 193 REMARK 465 TYR D 194 REMARK 465 ILE D 195 REMARK 465 CYS D 196 REMARK 465 ASN D 197 REMARK 465 VAL D 198 REMARK 465 ASN D 199 REMARK 465 HIS D 200 REMARK 465 LYS D 201 REMARK 465 PRO D 202 REMARK 465 SER D 203 REMARK 465 ASN D 204 REMARK 465 THR D 205 REMARK 465 LYS D 206 REMARK 465 VAL D 207 REMARK 465 ASP D 208 REMARK 465 LYS D 209 REMARK 465 LYS D 210 REMARK 465 VAL D 211 REMARK 465 GLU D 212 REMARK 465 SER D 213 REMARK 465 ALA D 214 REMARK 465 SER D 215 REMARK 465 CYS D 216 REMARK 465 ASP D 217 REMARK 465 LYS D 218 REMARK 465 THR D 219 REMARK 465 HIS D 220 REMARK 465 THR D 221 REMARK 465 CYS D 222 REMARK 465 PRO D 223 REMARK 465 GLU G 1 REMARK 465 GLY G 106 REMARK 465 THR G 107 REMARK 465 LEU G 108 REMARK 465 VAL G 109 REMARK 465 THR G 110 REMARK 465 VAL G 111 REMARK 465 SER G 112 REMARK 465 SER G 113 REMARK 465 ALA G 114 REMARK 465 SER G 115 REMARK 465 THR G 116 REMARK 465 LYS G 117 REMARK 465 GLY G 118 REMARK 465 PRO G 119 REMARK 465 SER G 120 REMARK 465 VAL G 121 REMARK 465 PHE G 122 REMARK 465 PRO G 123 REMARK 465 LEU G 124 REMARK 465 ALA G 125 REMARK 465 PRO G 126 REMARK 465 SER G 127 REMARK 465 SER G 128 REMARK 465 LYS G 129 REMARK 465 SER G 130 REMARK 465 THR G 131 REMARK 465 SER G 132 REMARK 465 GLY G 133 REMARK 465 GLY G 134 REMARK 465 THR G 135 REMARK 465 ALA G 136 REMARK 465 ALA G 137 REMARK 465 LEU G 138 REMARK 465 GLY G 139 REMARK 465 CYS G 140 REMARK 465 LEU G 141 REMARK 465 VAL G 142 REMARK 465 LYS G 143 REMARK 465 ASP G 144 REMARK 465 TYR G 145 REMARK 465 PHE G 146 REMARK 465 PRO G 147 REMARK 465 GLU G 148 REMARK 465 PRO G 149 REMARK 465 VAL G 150 REMARK 465 THR G 151 REMARK 465 VAL G 152 REMARK 465 SER G 153 REMARK 465 TRP G 154 REMARK 465 ASN G 155 REMARK 465 SER G 156 REMARK 465 GLY G 157 REMARK 465 ALA G 158 REMARK 465 LEU G 159 REMARK 465 THR G 160 REMARK 465 SER G 161 REMARK 465 GLY G 162 REMARK 465 VAL G 163 REMARK 465 HIS G 164 REMARK 465 THR G 165 REMARK 465 PHE G 166 REMARK 465 PRO G 167 REMARK 465 ALA G 168 REMARK 465 VAL G 169 REMARK 465 LEU G 170 REMARK 465 GLN G 171 REMARK 465 SER G 172 REMARK 465 SER G 173 REMARK 465 GLY G 174 REMARK 465 LEU G 175 REMARK 465 TYR G 176 REMARK 465 SER G 177 REMARK 465 LEU G 178 REMARK 465 SER G 179 REMARK 465 SER G 180 REMARK 465 VAL G 181 REMARK 465 VAL G 182 REMARK 465 THR G 183 REMARK 465 VAL G 184 REMARK 465 PRO G 185 REMARK 465 SER G 186 REMARK 465 SER G 187 REMARK 465 SER G 188 REMARK 465 LEU G 189 REMARK 465 GLY G 190 REMARK 465 THR G 191 REMARK 465 GLN G 192 REMARK 465 THR G 193 REMARK 465 TYR G 194 REMARK 465 ILE G 195 REMARK 465 CYS G 196 REMARK 465 ASN G 197 REMARK 465 VAL G 198 REMARK 465 ASN G 199 REMARK 465 HIS G 200 REMARK 465 LYS G 201 REMARK 465 PRO G 202 REMARK 465 SER G 203 REMARK 465 ASN G 204 REMARK 465 THR G 205 REMARK 465 LYS G 206 REMARK 465 VAL G 207 REMARK 465 ASP G 208 REMARK 465 LYS G 209 REMARK 465 LYS G 210 REMARK 465 VAL G 211 REMARK 465 GLU G 212 REMARK 465 SER G 213 REMARK 465 ALA G 214 REMARK 465 SER G 215 REMARK 465 CYS G 216 REMARK 465 ASP G 217 REMARK 465 LYS G 218 REMARK 465 THR G 219 REMARK 465 HIS G 220 REMARK 465 THR G 221 REMARK 465 CYS G 222 REMARK 465 PRO G 223 REMARK 465 GLU H 1 REMARK 465 GLY H 106 REMARK 465 THR H 107 REMARK 465 LEU H 108 REMARK 465 VAL H 109 REMARK 465 THR H 110 REMARK 465 VAL H 111 REMARK 465 SER H 112 REMARK 465 SER H 113 REMARK 465 ALA H 114 REMARK 465 SER H 115 REMARK 465 THR H 116 REMARK 465 LYS H 117 REMARK 465 GLY H 118 REMARK 465 PRO H 119 REMARK 465 SER H 120 REMARK 465 VAL H 121 REMARK 465 PHE H 122 REMARK 465 PRO H 123 REMARK 465 LEU H 124 REMARK 465 ALA H 125 REMARK 465 PRO H 126 REMARK 465 SER H 127 REMARK 465 SER H 128 REMARK 465 LYS H 129 REMARK 465 SER H 130 REMARK 465 THR H 131 REMARK 465 SER H 132 REMARK 465 GLY H 133 REMARK 465 GLY H 134 REMARK 465 THR H 135 REMARK 465 ALA H 136 REMARK 465 ALA H 137 REMARK 465 LEU H 138 REMARK 465 GLY H 139 REMARK 465 CYS H 140 REMARK 465 LEU H 141 REMARK 465 VAL H 142 REMARK 465 LYS H 143 REMARK 465 ASP H 144 REMARK 465 TYR H 145 REMARK 465 PHE H 146 REMARK 465 PRO H 147 REMARK 465 GLU H 148 REMARK 465 PRO H 149 REMARK 465 VAL H 150 REMARK 465 THR H 151 REMARK 465 VAL H 152 REMARK 465 SER H 153 REMARK 465 TRP H 154 REMARK 465 ASN H 155 REMARK 465 SER H 156 REMARK 465 GLY H 157 REMARK 465 ALA H 158 REMARK 465 LEU H 159 REMARK 465 THR H 160 REMARK 465 SER H 161 REMARK 465 GLY H 162 REMARK 465 VAL H 163 REMARK 465 HIS H 164 REMARK 465 THR H 165 REMARK 465 PHE H 166 REMARK 465 PRO H 167 REMARK 465 ALA H 168 REMARK 465 VAL H 169 REMARK 465 LEU H 170 REMARK 465 GLN H 171 REMARK 465 SER H 172 REMARK 465 SER H 173 REMARK 465 GLY H 174 REMARK 465 LEU H 175 REMARK 465 TYR H 176 REMARK 465 SER H 177 REMARK 465 LEU H 178 REMARK 465 SER H 179 REMARK 465 SER H 180 REMARK 465 VAL H 181 REMARK 465 VAL H 182 REMARK 465 THR H 183 REMARK 465 VAL H 184 REMARK 465 PRO H 185 REMARK 465 SER H 186 REMARK 465 SER H 187 REMARK 465 SER H 188 REMARK 465 LEU H 189 REMARK 465 GLY H 190 REMARK 465 THR H 191 REMARK 465 GLN H 192 REMARK 465 THR H 193 REMARK 465 TYR H 194 REMARK 465 ILE H 195 REMARK 465 CYS H 196 REMARK 465 ASN H 197 REMARK 465 VAL H 198 REMARK 465 ASN H 199 REMARK 465 HIS H 200 REMARK 465 LYS H 201 REMARK 465 PRO H 202 REMARK 465 SER H 203 REMARK 465 ASN H 204 REMARK 465 THR H 205 REMARK 465 LYS H 206 REMARK 465 VAL H 207 REMARK 465 ASP H 208 REMARK 465 LYS H 209 REMARK 465 LYS H 210 REMARK 465 VAL H 211 REMARK 465 GLU H 212 REMARK 465 SER H 213 REMARK 465 ALA H 214 REMARK 465 SER H 215 REMARK 465 CYS H 216 REMARK 465 ASP H 217 REMARK 465 LYS H 218 REMARK 465 THR H 219 REMARK 465 HIS H 220 REMARK 465 THR H 221 REMARK 465 CYS H 222 REMARK 465 PRO H 223 REMARK 465 GLU I 1 REMARK 465 ARG I 108 REMARK 465 THR I 109 REMARK 465 VAL I 110 REMARK 465 ALA I 111 REMARK 465 ALA I 112 REMARK 465 PRO I 113 REMARK 465 SER I 114 REMARK 465 VAL I 115 REMARK 465 PHE I 116 REMARK 465 ILE I 117 REMARK 465 PHE I 118 REMARK 465 PRO I 119 REMARK 465 PRO I 120 REMARK 465 SER I 121 REMARK 465 ASP I 122 REMARK 465 GLU I 123 REMARK 465 GLN I 124 REMARK 465 LEU I 125 REMARK 465 LYS I 126 REMARK 465 SER I 127 REMARK 465 GLY I 128 REMARK 465 THR I 129 REMARK 465 ALA I 130 REMARK 465 SER I 131 REMARK 465 VAL I 132 REMARK 465 VAL I 133 REMARK 465 CYS I 134 REMARK 465 LEU I 135 REMARK 465 LEU I 136 REMARK 465 ASN I 137 REMARK 465 ASN I 138 REMARK 465 PHE I 139 REMARK 465 TYR I 140 REMARK 465 PRO I 141 REMARK 465 ARG I 142 REMARK 465 GLU I 143 REMARK 465 ALA I 144 REMARK 465 LYS I 145 REMARK 465 VAL I 146 REMARK 465 GLN I 147 REMARK 465 TRP I 148 REMARK 465 LYS I 149 REMARK 465 VAL I 150 REMARK 465 ASP I 151 REMARK 465 ASN I 152 REMARK 465 ALA I 153 REMARK 465 LEU I 154 REMARK 465 GLN I 155 REMARK 465 SER I 156 REMARK 465 GLY I 157 REMARK 465 ASN I 158 REMARK 465 SER I 159 REMARK 465 GLN I 160 REMARK 465 GLU I 161 REMARK 465 SER I 162 REMARK 465 VAL I 163 REMARK 465 THR I 164 REMARK 465 GLU I 165 REMARK 465 GLN I 166 REMARK 465 ASP I 167 REMARK 465 SER I 168 REMARK 465 LYS I 169 REMARK 465 ASP I 170 REMARK 465 SER I 171 REMARK 465 THR I 172 REMARK 465 TYR I 173 REMARK 465 SER I 174 REMARK 465 LEU I 175 REMARK 465 SER I 176 REMARK 465 SER I 177 REMARK 465 THR I 178 REMARK 465 LEU I 179 REMARK 465 THR I 180 REMARK 465 LEU I 181 REMARK 465 SER I 182 REMARK 465 LYS I 183 REMARK 465 ALA I 184 REMARK 465 ASP I 185 REMARK 465 TYR I 186 REMARK 465 GLU I 187 REMARK 465 LYS I 188 REMARK 465 HIS I 189 REMARK 465 LYS I 190 REMARK 465 VAL I 191 REMARK 465 TYR I 192 REMARK 465 ALA I 193 REMARK 465 CYS I 194 REMARK 465 GLU I 195 REMARK 465 VAL I 196 REMARK 465 THR I 197 REMARK 465 HIS I 198 REMARK 465 GLN I 199 REMARK 465 GLY I 200 REMARK 465 LEU I 201 REMARK 465 SER I 202 REMARK 465 SER I 203 REMARK 465 PRO I 204 REMARK 465 VAL I 205 REMARK 465 THR I 206 REMARK 465 LYS I 207 REMARK 465 SER I 208 REMARK 465 PHE I 209 REMARK 465 ASN I 210 REMARK 465 ARG I 211 REMARK 465 GLY I 212 REMARK 465 GLU I 213 REMARK 465 CYS I 214 REMARK 465 GLU K 1 REMARK 465 ARG K 108 REMARK 465 THR K 109 REMARK 465 VAL K 110 REMARK 465 ALA K 111 REMARK 465 ALA K 112 REMARK 465 PRO K 113 REMARK 465 SER K 114 REMARK 465 VAL K 115 REMARK 465 PHE K 116 REMARK 465 ILE K 117 REMARK 465 PHE K 118 REMARK 465 PRO K 119 REMARK 465 PRO K 120 REMARK 465 SER K 121 REMARK 465 ASP K 122 REMARK 465 GLU K 123 REMARK 465 GLN K 124 REMARK 465 LEU K 125 REMARK 465 LYS K 126 REMARK 465 SER K 127 REMARK 465 GLY K 128 REMARK 465 THR K 129 REMARK 465 ALA K 130 REMARK 465 SER K 131 REMARK 465 VAL K 132 REMARK 465 VAL K 133 REMARK 465 CYS K 134 REMARK 465 LEU K 135 REMARK 465 LEU K 136 REMARK 465 ASN K 137 REMARK 465 ASN K 138 REMARK 465 PHE K 139 REMARK 465 TYR K 140 REMARK 465 PRO K 141 REMARK 465 ARG K 142 REMARK 465 GLU K 143 REMARK 465 ALA K 144 REMARK 465 LYS K 145 REMARK 465 VAL K 146 REMARK 465 GLN K 147 REMARK 465 TRP K 148 REMARK 465 LYS K 149 REMARK 465 VAL K 150 REMARK 465 ASP K 151 REMARK 465 ASN K 152 REMARK 465 ALA K 153 REMARK 465 LEU K 154 REMARK 465 GLN K 155 REMARK 465 SER K 156 REMARK 465 GLY K 157 REMARK 465 ASN K 158 REMARK 465 SER K 159 REMARK 465 GLN K 160 REMARK 465 GLU K 161 REMARK 465 SER K 162 REMARK 465 VAL K 163 REMARK 465 THR K 164 REMARK 465 GLU K 165 REMARK 465 GLN K 166 REMARK 465 ASP K 167 REMARK 465 SER K 168 REMARK 465 LYS K 169 REMARK 465 ASP K 170 REMARK 465 SER K 171 REMARK 465 THR K 172 REMARK 465 TYR K 173 REMARK 465 SER K 174 REMARK 465 LEU K 175 REMARK 465 SER K 176 REMARK 465 SER K 177 REMARK 465 THR K 178 REMARK 465 LEU K 179 REMARK 465 THR K 180 REMARK 465 LEU K 181 REMARK 465 SER K 182 REMARK 465 LYS K 183 REMARK 465 ALA K 184 REMARK 465 ASP K 185 REMARK 465 TYR K 186 REMARK 465 GLU K 187 REMARK 465 LYS K 188 REMARK 465 HIS K 189 REMARK 465 LYS K 190 REMARK 465 VAL K 191 REMARK 465 TYR K 192 REMARK 465 ALA K 193 REMARK 465 CYS K 194 REMARK 465 GLU K 195 REMARK 465 VAL K 196 REMARK 465 THR K 197 REMARK 465 HIS K 198 REMARK 465 GLN K 199 REMARK 465 GLY K 200 REMARK 465 LEU K 201 REMARK 465 SER K 202 REMARK 465 SER K 203 REMARK 465 PRO K 204 REMARK 465 VAL K 205 REMARK 465 THR K 206 REMARK 465 LYS K 207 REMARK 465 SER K 208 REMARK 465 PHE K 209 REMARK 465 ASN K 210 REMARK 465 ARG K 211 REMARK 465 GLY K 212 REMARK 465 GLU K 213 REMARK 465 CYS K 214 REMARK 465 GLU L 1 REMARK 465 ARG L 108 REMARK 465 THR L 109 REMARK 465 VAL L 110 REMARK 465 ALA L 111 REMARK 465 ALA L 112 REMARK 465 PRO L 113 REMARK 465 SER L 114 REMARK 465 VAL L 115 REMARK 465 PHE L 116 REMARK 465 ILE L 117 REMARK 465 PHE L 118 REMARK 465 PRO L 119 REMARK 465 PRO L 120 REMARK 465 SER L 121 REMARK 465 ASP L 122 REMARK 465 GLU L 123 REMARK 465 GLN L 124 REMARK 465 LEU L 125 REMARK 465 LYS L 126 REMARK 465 SER L 127 REMARK 465 GLY L 128 REMARK 465 THR L 129 REMARK 465 ALA L 130 REMARK 465 SER L 131 REMARK 465 VAL L 132 REMARK 465 VAL L 133 REMARK 465 CYS L 134 REMARK 465 LEU L 135 REMARK 465 LEU L 136 REMARK 465 ASN L 137 REMARK 465 ASN L 138 REMARK 465 PHE L 139 REMARK 465 TYR L 140 REMARK 465 PRO L 141 REMARK 465 ARG L 142 REMARK 465 GLU L 143 REMARK 465 ALA L 144 REMARK 465 LYS L 145 REMARK 465 VAL L 146 REMARK 465 GLN L 147 REMARK 465 TRP L 148 REMARK 465 LYS L 149 REMARK 465 VAL L 150 REMARK 465 ASP L 151 REMARK 465 ASN L 152 REMARK 465 ALA L 153 REMARK 465 LEU L 154 REMARK 465 GLN L 155 REMARK 465 SER L 156 REMARK 465 GLY L 157 REMARK 465 ASN L 158 REMARK 465 SER L 159 REMARK 465 GLN L 160 REMARK 465 GLU L 161 REMARK 465 SER L 162 REMARK 465 VAL L 163 REMARK 465 THR L 164 REMARK 465 GLU L 165 REMARK 465 GLN L 166 REMARK 465 ASP L 167 REMARK 465 SER L 168 REMARK 465 LYS L 169 REMARK 465 ASP L 170 REMARK 465 SER L 171 REMARK 465 THR L 172 REMARK 465 TYR L 173 REMARK 465 SER L 174 REMARK 465 LEU L 175 REMARK 465 SER L 176 REMARK 465 SER L 177 REMARK 465 THR L 178 REMARK 465 LEU L 179 REMARK 465 THR L 180 REMARK 465 LEU L 181 REMARK 465 SER L 182 REMARK 465 LYS L 183 REMARK 465 ALA L 184 REMARK 465 ASP L 185 REMARK 465 TYR L 186 REMARK 465 GLU L 187 REMARK 465 LYS L 188 REMARK 465 HIS L 189 REMARK 465 LYS L 190 REMARK 465 VAL L 191 REMARK 465 TYR L 192 REMARK 465 ALA L 193 REMARK 465 CYS L 194 REMARK 465 GLU L 195 REMARK 465 VAL L 196 REMARK 465 THR L 197 REMARK 465 HIS L 198 REMARK 465 GLN L 199 REMARK 465 GLY L 200 REMARK 465 LEU L 201 REMARK 465 SER L 202 REMARK 465 SER L 203 REMARK 465 PRO L 204 REMARK 465 VAL L 205 REMARK 465 THR L 206 REMARK 465 LYS L 207 REMARK 465 SER L 208 REMARK 465 PHE L 209 REMARK 465 ASN L 210 REMARK 465 ARG L 211 REMARK 465 GLY L 212 REMARK 465 GLU L 213 REMARK 465 CYS L 214 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 ALA A 242 CB 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 OE2 GLU A 189 CZ TYR D 27 0.84 REMARK 500 OE1 GLU B 189 CZ TYR G 27 0.96 REMARK 500 OE2 GLU A 189 CE1 TYR D 27 1.13 REMARK 500 OE1 GLU B 189 CE1 TYR G 27 1.13 REMARK 500 OE2 GLU B 189 OH TYR G 27 1.24 REMARK 500 OE1 GLU A 189 OH TYR D 27 1.29 REMARK 500 CD GLU A 189 CZ TYR D 27 1.41 REMARK 500 CD GLU B 189 CZ TYR G 27 1.43 REMARK 500 OE2 GLU A 189 CE2 TYR D 27 1.58 REMARK 500 OE1 GLU B 189 CE2 TYR G 27 1.71 REMARK 500 CD GLU A 189 OH TYR D 27 1.74 REMARK 500 CD GLU B 189 OH TYR G 27 1.76 REMARK 500 CD GLU A 189 CE2 TYR D 27 1.87 REMARK 500 CD GLU B 189 CE2 TYR G 27 1.89 REMARK 500 OE1 GLU B 189 CD1 TYR G 27 1.90 REMARK 500 OE2 GLU A 189 CD1 TYR D 27 1.91 REMARK 500 OE2 GLU B 189 CZ TYR G 27 1.97 REMARK 500 OE1 GLU A 189 CZ TYR D 27 2.00 REMARK 500 OE2 GLU A 189 OH TYR D 27 2.00 REMARK 500 OE1 GLU B 189 OH TYR G 27 2.07 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 ARG A 86 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES REMARK 500 ARG B 86 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES REMARK 500 ARG C 86 NE - CZ - NH1 ANGL. DEV. = 3.4 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 LYS A 57 -118.04 58.61 REMARK 500 ASP A 92 -116.63 -123.78 REMARK 500 LYS A 196 -9.14 71.26 REMARK 500 THR A 206 -167.98 -123.14 REMARK 500 PRO A 239 2.21 -65.15 REMARK 500 ASP A 240 38.94 -140.68 REMARK 500 ARG A 461 -72.07 -82.79 REMARK 500 ASP A 479 -167.59 -121.87 REMARK 500 ASN B 14 -162.90 -129.98 REMARK 500 LYS B 57 -119.80 58.69 REMARK 500 PHE B 74 30.47 -98.46 REMARK 500 ASP B 92 -117.49 -120.33 REMARK 500 TRP B 126 79.83 -118.59 REMARK 500 GLN B 142 52.20 37.97 REMARK 500 LYS B 196 -10.61 72.17 REMARK 500 THR B 206 -168.24 -123.74 REMARK 500 PRO B 239 4.73 -65.80 REMARK 500 ARG B 469 -119.33 57.99 REMARK 500 ASP B 487 -169.03 -107.01 REMARK 500 SER B 505 81.47 -150.15 REMARK 500 GLU B 506 -39.82 -138.48 REMARK 500 CYS C 8 151.24 -49.72 REMARK 500 LYS C 57 -119.64 57.71 REMARK 500 ASP C 92 -115.11 -109.87 REMARK 500 LYS C 196 -11.14 72.37 REMARK 500 THR C 206 -169.16 -118.02 REMARK 500 PRO C 239 3.88 -65.25 REMARK 500 ASP C 240 28.53 -140.61 REMARK 500 GLU C 381 8.16 55.97 REMARK 500 ARG C 469 -123.71 59.41 REMARK 500 ALA C 472 -152.72 -114.91 REMARK 500 LYS C 473 114.19 -166.03 REMARK 500 ASP C 487 -168.50 -106.67 REMARK 500 TRP D 100G 76.59 -103.44 REMARK 500 TRP G 100G 76.47 -103.40 REMARK 500 TRP H 100G 76.52 -103.38 REMARK 500 ALA I 51 -3.53 68.34 REMARK 500 SER I 52 -32.67 -136.67 REMARK 500 ALA K 51 -3.50 68.24 REMARK 500 SER K 52 -32.58 -136.73 REMARK 500 ALA L 51 -3.59 68.35 REMARK 500 SER L 52 -32.66 -136.62 REMARK 500 REMARK 500 REMARK: NULL REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 NAG E 1 REMARK 610 NAG F 1 REMARK 610 NAG J 1 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-48120 RELATED DB: EMDB REMARK 900 CRYOEM STRUCTURE OF H5N1 A/TEXAS/37/2024 HA BOUND TO FAB 65C6 AND A REMARK 900 SELF GLYCAN OCCUPYING THE RBS DBREF 9EKF A -11 566 PDB 9EKF 9EKF -11 566 DBREF 9EKF B -11 574 PDB 9EKF 9EKF -11 574 DBREF 9EKF C -11 574 PDB 9EKF 9EKF -11 574 DBREF 9EKF D 1 223 PDB 9EKF 9EKF 1 223 DBREF 9EKF G 1 223 PDB 9EKF 9EKF 1 223 DBREF 9EKF H 1 223 PDB 9EKF 9EKF 1 223 DBREF 9EKF I 1 214 PDB 9EKF 9EKF 1 214 DBREF 9EKF K 1 214 PDB 9EKF 9EKF 1 214 DBREF 9EKF L 1 214 PDB 9EKF 9EKF 1 214 SEQRES 1 A 576 MET GLU ASN ILE VAL LEU LEU LEU ALA ILE VAL SER LEU SEQRES 2 A 576 VAL LYS SER ASP GLN ILE CYS ILE GLY TYR HIS ALA ASN SEQRES 3 A 576 ASN SER THR GLU GLN VAL ASP THR ILE MET GLU LYS ASN SEQRES 4 A 576 VAL THR VAL THR HIS ALA GLN ASP ILE LEU GLU LYS THR SEQRES 5 A 576 HIS ASN GLY LYS LEU CYS ASP LEU ASN GLY VAL LYS PRO SEQRES 6 A 576 LEU ILE LEU LYS ASP CYS SER VAL ALA GLY TRP LEU LEU SEQRES 7 A 576 GLY ASN PRO MET CYS ASP GLU PHE ILE ARG VAL PRO GLU SEQRES 8 A 576 TRP SER TYR ILE VAL GLU ARG ALA ASN PRO ALA ASN ASP SEQRES 9 A 576 LEU CYS TYR PRO GLY SER LEU ASN ASP TYR GLU GLU LEU SEQRES 10 A 576 LYS HIS MET LEU SER ARG ILE ASN HIS PHE GLU LYS ILE SEQRES 11 A 576 GLN ILE ILE PRO LYS SER SER TRP PRO ASN HIS GLU THR SEQRES 12 A 576 SER LEU GLY VAL SER ALA ALA CYS PRO TYR GLN GLY ALA SEQRES 13 A 576 PRO SER PHE PHE ARG ASN VAL VAL TRP LEU ILE LYS LYS SEQRES 14 A 576 ASN ASP ALA TYR PRO THR ILE LYS ILE SER TYR ASN ASN SEQRES 15 A 576 THR ASN ARG GLU ASP LEU LEU ILE LEU TRP GLY ILE HIS SEQRES 16 A 576 HIS SER ASN ASN ALA GLU GLU GLN THR ASN LEU TYR LYS SEQRES 17 A 576 ASN PRO ILE THR TYR ILE SER VAL GLY THR SER THR LEU SEQRES 18 A 576 ASN GLN ARG LEU ALA PRO LYS ILE ALA THR ARG SER GLN SEQRES 19 A 576 VAL ASN GLY GLN ARG GLY ARG MET ASP PHE PHE TRP THR SEQRES 20 A 576 ILE LEU LYS PRO ASP ASP ALA ILE HIS PHE GLU SER ASN SEQRES 21 A 576 GLY ASN PHE ILE ALA PRO GLU TYR ALA TYR LYS ILE VAL SEQRES 22 A 576 LYS LYS GLY ASP SER THR ILE MET LYS SER GLY VAL GLU SEQRES 23 A 576 TYR GLY HIS CYS ASN THR LYS CYS GLN THR PRO VAL GLY SEQRES 24 A 576 ALA ILE ASN SER SER MET PRO PHE HIS ASN ILE HIS PRO SEQRES 25 A 576 LEU THR ILE GLY GLU CYS PRO LYS TYR VAL LYS SER ASN SEQRES 26 A 576 LYS LEU VAL LEU ALA THR GLY LEU ARG ASN SER PRO LEU SEQRES 27 A 576 ARG ARG ARG ARG ARG ARG GLY LEU PHE GLY ALA ILE ALA SEQRES 28 A 576 GLY PHE ILE GLU GLY GLY TRP GLN GLY MET VAL ASP GLY SEQRES 29 A 576 TRP TYR GLY TYR HIS HIS SER ASN GLU GLN GLY SER GLY SEQRES 30 A 576 TYR ALA ALA ASP LYS GLU SER THR GLN LYS ALA ILE ASP SEQRES 31 A 576 GLY VAL THR ASN LYS VAL ASN SER ILE ILE ASP LYS MET SEQRES 32 A 576 ASN THR GLN PHE GLU ALA VAL GLY ARG GLU PHE ASN ASN SEQRES 33 A 576 LEU GLU ARG ARG ILE GLU ASN LEU ASN LYS LYS MET GLU SEQRES 34 A 576 ASP GLY PHE LEU ASP VAL TRP THR TYR ASN ALA GLU LEU SEQRES 35 A 576 LEU VAL LEU MET GLU ASN GLU ARG THR LEU ASP PHE HIS SEQRES 36 A 576 ASP SER ASN VAL LYS ASN LEU TYR ASP LYS VAL ARG LEU SEQRES 37 A 576 GLN LEU ARG ASP ASN ALA LYS GLU LEU GLY ASN GLY CYS SEQRES 38 A 576 PHE GLU PHE TYR HIS LYS CYS ASP ASN GLU CYS MET GLU SEQRES 39 A 576 SER VAL ARG ASN GLY THR TYR ASP TYR PRO GLN TYR SER SEQRES 40 A 576 GLU GLU ALA ARG LEU LYS ARG GLU GLY SER SER GLY SER SEQRES 41 A 576 SER GLY TYR ILE PRO GLU ALA PRO ARG ASP GLY GLN ALA SEQRES 42 A 576 TYR VAL ARG LYS ASP GLY GLU TRP VAL LEU LEU SER THR SEQRES 43 A 576 PHE LEU GLY HIS HIS HIS HIS HIS HIS HIS HIS HIS GLY SEQRES 44 A 576 GLY SER GLY LEU ASN ASP ILE PHE GLU ALA GLN LYS ILE SEQRES 45 A 576 GLU TRP HIS GLU SEQRES 1 B 576 MET GLU ASN ILE VAL LEU LEU LEU ALA ILE VAL SER LEU SEQRES 2 B 576 VAL LYS SER ASP GLN ILE CYS ILE GLY TYR HIS ALA ASN SEQRES 3 B 576 ASN SER THR GLU GLN VAL ASP THR ILE MET GLU LYS ASN SEQRES 4 B 576 VAL THR VAL THR HIS ALA GLN ASP ILE LEU GLU LYS THR SEQRES 5 B 576 HIS ASN GLY LYS LEU CYS ASP LEU ASN GLY VAL LYS PRO SEQRES 6 B 576 LEU ILE LEU LYS ASP CYS SER VAL ALA GLY TRP LEU LEU SEQRES 7 B 576 GLY ASN PRO MET CYS ASP GLU PHE ILE ARG VAL PRO GLU SEQRES 8 B 576 TRP SER TYR ILE VAL GLU ARG ALA ASN PRO ALA ASN ASP SEQRES 9 B 576 LEU CYS TYR PRO GLY SER LEU ASN ASP TYR GLU GLU LEU SEQRES 10 B 576 LYS HIS MET LEU SER ARG ILE ASN HIS PHE GLU LYS ILE SEQRES 11 B 576 GLN ILE ILE PRO LYS SER SER TRP PRO ASN HIS GLU THR SEQRES 12 B 576 SER LEU GLY VAL SER ALA ALA CYS PRO TYR GLN GLY ALA SEQRES 13 B 576 PRO SER PHE PHE ARG ASN VAL VAL TRP LEU ILE LYS LYS SEQRES 14 B 576 ASN ASP ALA TYR PRO THR ILE LYS ILE SER TYR ASN ASN SEQRES 15 B 576 THR ASN ARG GLU ASP LEU LEU ILE LEU TRP GLY ILE HIS SEQRES 16 B 576 HIS SER ASN ASN ALA GLU GLU GLN THR ASN LEU TYR LYS SEQRES 17 B 576 ASN PRO ILE THR TYR ILE SER VAL GLY THR SER THR LEU SEQRES 18 B 576 ASN GLN ARG LEU ALA PRO LYS ILE ALA THR ARG SER GLN SEQRES 19 B 576 VAL ASN GLY GLN ARG GLY ARG MET ASP PHE PHE TRP THR SEQRES 20 B 576 ILE LEU LYS PRO ASP ASP ALA ILE HIS PHE GLU SER ASN SEQRES 21 B 576 GLY ASN PHE ILE ALA PRO GLU TYR ALA TYR LYS ILE VAL SEQRES 22 B 576 LYS LYS GLY ASP SER THR ILE MET LYS SER GLY VAL GLU SEQRES 23 B 576 TYR GLY HIS CYS ASN THR LYS CYS GLN THR PRO VAL GLY SEQRES 24 B 576 ALA ILE ASN SER SER MET PRO PHE HIS ASN ILE HIS PRO SEQRES 25 B 576 LEU THR ILE GLY GLU CYS PRO LYS TYR VAL LYS SER ASN SEQRES 26 B 576 LYS LEU VAL LEU ALA THR GLY LEU ARG ASN SER PRO LEU SEQRES 27 B 576 ARG ARG ARG ARG ARG ARG GLY LEU PHE GLY ALA ILE ALA SEQRES 28 B 576 GLY PHE ILE GLU GLY GLY TRP GLN GLY MET VAL ASP GLY SEQRES 29 B 576 TRP TYR GLY TYR HIS HIS SER ASN GLU GLN GLY SER GLY SEQRES 30 B 576 TYR ALA ALA ASP LYS GLU SER THR GLN LYS ALA ILE ASP SEQRES 31 B 576 GLY VAL THR ASN LYS VAL ASN SER ILE ILE ASP LYS MET SEQRES 32 B 576 ASN THR GLN PHE GLU ALA VAL GLY ARG GLU PHE ASN ASN SEQRES 33 B 576 LEU GLU ARG ARG ILE GLU ASN LEU ASN LYS LYS MET GLU SEQRES 34 B 576 ASP GLY PHE LEU ASP VAL TRP THR TYR ASN ALA GLU LEU SEQRES 35 B 576 LEU VAL LEU MET GLU ASN GLU ARG THR LEU ASP PHE HIS SEQRES 36 B 576 ASP SER ASN VAL LYS ASN LEU TYR ASP LYS VAL ARG LEU SEQRES 37 B 576 GLN LEU ARG ASP ASN ALA LYS GLU LEU GLY ASN GLY CYS SEQRES 38 B 576 PHE GLU PHE TYR HIS LYS CYS ASP ASN GLU CYS MET GLU SEQRES 39 B 576 SER VAL ARG ASN GLY THR TYR ASP TYR PRO GLN TYR SER SEQRES 40 B 576 GLU GLU ALA ARG LEU LYS ARG GLU GLY SER SER GLY SER SEQRES 41 B 576 SER GLY TYR ILE PRO GLU ALA PRO ARG ASP GLY GLN ALA SEQRES 42 B 576 TYR VAL ARG LYS ASP GLY GLU TRP VAL LEU LEU SER THR SEQRES 43 B 576 PHE LEU GLY HIS HIS HIS HIS HIS HIS HIS HIS HIS GLY SEQRES 44 B 576 GLY SER GLY LEU ASN ASP ILE PHE GLU ALA GLN LYS ILE SEQRES 45 B 576 GLU TRP HIS GLU SEQRES 1 C 576 MET GLU ASN ILE VAL LEU LEU LEU ALA ILE VAL SER LEU SEQRES 2 C 576 VAL LYS SER ASP GLN ILE CYS ILE GLY TYR HIS ALA ASN SEQRES 3 C 576 ASN SER THR GLU GLN VAL ASP THR ILE MET GLU LYS ASN SEQRES 4 C 576 VAL THR VAL THR HIS ALA GLN ASP ILE LEU GLU LYS THR SEQRES 5 C 576 HIS ASN GLY LYS LEU CYS ASP LEU ASN GLY VAL LYS PRO SEQRES 6 C 576 LEU ILE LEU LYS ASP CYS SER VAL ALA GLY TRP LEU LEU SEQRES 7 C 576 GLY ASN PRO MET CYS ASP GLU PHE ILE ARG VAL PRO GLU SEQRES 8 C 576 TRP SER TYR ILE VAL GLU ARG ALA ASN PRO ALA ASN ASP SEQRES 9 C 576 LEU CYS TYR PRO GLY SER LEU ASN ASP TYR GLU GLU LEU SEQRES 10 C 576 LYS HIS MET LEU SER ARG ILE ASN HIS PHE GLU LYS ILE SEQRES 11 C 576 GLN ILE ILE PRO LYS SER SER TRP PRO ASN HIS GLU THR SEQRES 12 C 576 SER LEU GLY VAL SER ALA ALA CYS PRO TYR GLN GLY ALA SEQRES 13 C 576 PRO SER PHE PHE ARG ASN VAL VAL TRP LEU ILE LYS LYS SEQRES 14 C 576 ASN ASP ALA TYR PRO THR ILE LYS ILE SER TYR ASN ASN SEQRES 15 C 576 THR ASN ARG GLU ASP LEU LEU ILE LEU TRP GLY ILE HIS SEQRES 16 C 576 HIS SER ASN ASN ALA GLU GLU GLN THR ASN LEU TYR LYS SEQRES 17 C 576 ASN PRO ILE THR TYR ILE SER VAL GLY THR SER THR LEU SEQRES 18 C 576 ASN GLN ARG LEU ALA PRO LYS ILE ALA THR ARG SER GLN SEQRES 19 C 576 VAL ASN GLY GLN ARG GLY ARG MET ASP PHE PHE TRP THR SEQRES 20 C 576 ILE LEU LYS PRO ASP ASP ALA ILE HIS PHE GLU SER ASN SEQRES 21 C 576 GLY ASN PHE ILE ALA PRO GLU TYR ALA TYR LYS ILE VAL SEQRES 22 C 576 LYS LYS GLY ASP SER THR ILE MET LYS SER GLY VAL GLU SEQRES 23 C 576 TYR GLY HIS CYS ASN THR LYS CYS GLN THR PRO VAL GLY SEQRES 24 C 576 ALA ILE ASN SER SER MET PRO PHE HIS ASN ILE HIS PRO SEQRES 25 C 576 LEU THR ILE GLY GLU CYS PRO LYS TYR VAL LYS SER ASN SEQRES 26 C 576 LYS LEU VAL LEU ALA THR GLY LEU ARG ASN SER PRO LEU SEQRES 27 C 576 ARG ARG ARG ARG ARG ARG GLY LEU PHE GLY ALA ILE ALA SEQRES 28 C 576 GLY PHE ILE GLU GLY GLY TRP GLN GLY MET VAL ASP GLY SEQRES 29 C 576 TRP TYR GLY TYR HIS HIS SER ASN GLU GLN GLY SER GLY SEQRES 30 C 576 TYR ALA ALA ASP LYS GLU SER THR GLN LYS ALA ILE ASP SEQRES 31 C 576 GLY VAL THR ASN LYS VAL ASN SER ILE ILE ASP LYS MET SEQRES 32 C 576 ASN THR GLN PHE GLU ALA VAL GLY ARG GLU PHE ASN ASN SEQRES 33 C 576 LEU GLU ARG ARG ILE GLU ASN LEU ASN LYS LYS MET GLU SEQRES 34 C 576 ASP GLY PHE LEU ASP VAL TRP THR TYR ASN ALA GLU LEU SEQRES 35 C 576 LEU VAL LEU MET GLU ASN GLU ARG THR LEU ASP PHE HIS SEQRES 36 C 576 ASP SER ASN VAL LYS ASN LEU TYR ASP LYS VAL ARG LEU SEQRES 37 C 576 GLN LEU ARG ASP ASN ALA LYS GLU LEU GLY ASN GLY CYS SEQRES 38 C 576 PHE GLU PHE TYR HIS LYS CYS ASP ASN GLU CYS MET GLU SEQRES 39 C 576 SER VAL ARG ASN GLY THR TYR ASP TYR PRO GLN TYR SER SEQRES 40 C 576 GLU GLU ALA ARG LEU LYS ARG GLU GLY SER SER GLY SER SEQRES 41 C 576 SER GLY TYR ILE PRO GLU ALA PRO ARG ASP GLY GLN ALA SEQRES 42 C 576 TYR VAL ARG LYS ASP GLY GLU TRP VAL LEU LEU SER THR SEQRES 43 C 576 PHE LEU GLY HIS HIS HIS HIS HIS HIS HIS HIS HIS GLY SEQRES 44 C 576 GLY SER GLY LEU ASN ASP ILE PHE GLU ALA GLN LYS ILE SEQRES 45 C 576 GLU TRP HIS GLU SEQRES 1 D 237 GLU VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 D 237 PRO GLY GLU SER LEU ARG ILE SER CYS LYS GLY PHE ALA SEQRES 3 D 237 TYR SER SER THR TYR PHE TRP ILE SER TRP VAL ARG GLN SEQRES 4 D 237 MET PRO GLY LYS GLY LEU GLU TRP MET GLY ARG ILE ASP SEQRES 5 D 237 PRO THR ASP SER TYR ILE ASN TYR SER PRO SER PHE GLN SEQRES 6 D 237 GLY HIS VAL THR ILE SER VAL ASP ARG SER ILE SER THR SEQRES 7 D 237 VAL TYR LEU GLN TRP SER SER LEU LYS ALA SER ASP THR SEQRES 8 D 237 ALA MET TYR TYR CYS ALA TYR HIS ARG ARG GLY HIS PHE SEQRES 9 D 237 TYR GLY SER GLY SER ALA TRP ASP TRP PHE GLU SER TRP SEQRES 10 D 237 GLY GLN GLY THR LEU VAL THR VAL SER SER ALA SER THR SEQRES 11 D 237 LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SEQRES 12 D 237 SER THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL SEQRES 13 D 237 LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SEQRES 14 D 237 SER GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA SEQRES 15 D 237 VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL SEQRES 16 D 237 VAL THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR SEQRES 17 D 237 ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL SEQRES 18 D 237 ASP LYS LYS VAL GLU SER ALA SER CYS ASP LYS THR HIS SEQRES 19 D 237 THR CYS PRO SEQRES 1 G 237 GLU VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 G 237 PRO GLY GLU SER LEU ARG ILE SER CYS LYS GLY PHE ALA SEQRES 3 G 237 TYR SER SER THR TYR PHE TRP ILE SER TRP VAL ARG GLN SEQRES 4 G 237 MET PRO GLY LYS GLY LEU GLU TRP MET GLY ARG ILE ASP SEQRES 5 G 237 PRO THR ASP SER TYR ILE ASN TYR SER PRO SER PHE GLN SEQRES 6 G 237 GLY HIS VAL THR ILE SER VAL ASP ARG SER ILE SER THR SEQRES 7 G 237 VAL TYR LEU GLN TRP SER SER LEU LYS ALA SER ASP THR SEQRES 8 G 237 ALA MET TYR TYR CYS ALA TYR HIS ARG ARG GLY HIS PHE SEQRES 9 G 237 TYR GLY SER GLY SER ALA TRP ASP TRP PHE GLU SER TRP SEQRES 10 G 237 GLY GLN GLY THR LEU VAL THR VAL SER SER ALA SER THR SEQRES 11 G 237 LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SEQRES 12 G 237 SER THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL SEQRES 13 G 237 LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SEQRES 14 G 237 SER GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA SEQRES 15 G 237 VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL SEQRES 16 G 237 VAL THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR SEQRES 17 G 237 ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL SEQRES 18 G 237 ASP LYS LYS VAL GLU SER ALA SER CYS ASP LYS THR HIS SEQRES 19 G 237 THR CYS PRO SEQRES 1 H 237 GLU VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 H 237 PRO GLY GLU SER LEU ARG ILE SER CYS LYS GLY PHE ALA SEQRES 3 H 237 TYR SER SER THR TYR PHE TRP ILE SER TRP VAL ARG GLN SEQRES 4 H 237 MET PRO GLY LYS GLY LEU GLU TRP MET GLY ARG ILE ASP SEQRES 5 H 237 PRO THR ASP SER TYR ILE ASN TYR SER PRO SER PHE GLN SEQRES 6 H 237 GLY HIS VAL THR ILE SER VAL ASP ARG SER ILE SER THR SEQRES 7 H 237 VAL TYR LEU GLN TRP SER SER LEU LYS ALA SER ASP THR SEQRES 8 H 237 ALA MET TYR TYR CYS ALA TYR HIS ARG ARG GLY HIS PHE SEQRES 9 H 237 TYR GLY SER GLY SER ALA TRP ASP TRP PHE GLU SER TRP SEQRES 10 H 237 GLY GLN GLY THR LEU VAL THR VAL SER SER ALA SER THR SEQRES 11 H 237 LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SEQRES 12 H 237 SER THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL SEQRES 13 H 237 LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SEQRES 14 H 237 SER GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA SEQRES 15 H 237 VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL SEQRES 16 H 237 VAL THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR SEQRES 17 H 237 ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL SEQRES 18 H 237 ASP LYS LYS VAL GLU SER ALA SER CYS ASP LYS THR HIS SEQRES 19 H 237 THR CYS PRO SEQRES 1 I 214 GLU ILE VAL LEU THR GLN SER PRO LEU THR LEU SER VAL SEQRES 2 I 214 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 I 214 GLN SER VAL SER SER ASN LEU ALA TRP TYR GLN GLN MET SEQRES 4 I 214 PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR GLY ALA SER SEQRES 5 I 214 THR ARG ALA THR GLY ILE PRO ALA ARG LEU SER GLY SER SEQRES 6 I 214 ALA SER GLY THR GLU PHE THR LEU THR ILE SER SER LEU SEQRES 7 I 214 GLN SER GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN TYR SEQRES 8 I 214 ASN ASN TRP PRO TYR THR PHE GLY GLN GLY THR LYS LEU SEQRES 9 I 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 I 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 I 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 I 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 I 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 I 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 I 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 I 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 I 214 PHE ASN ARG GLY GLU CYS SEQRES 1 K 214 GLU ILE VAL LEU THR GLN SER PRO LEU THR LEU SER VAL SEQRES 2 K 214 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 K 214 GLN SER VAL SER SER ASN LEU ALA TRP TYR GLN GLN MET SEQRES 4 K 214 PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR GLY ALA SER SEQRES 5 K 214 THR ARG ALA THR GLY ILE PRO ALA ARG LEU SER GLY SER SEQRES 6 K 214 ALA SER GLY THR GLU PHE THR LEU THR ILE SER SER LEU SEQRES 7 K 214 GLN SER GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN TYR SEQRES 8 K 214 ASN ASN TRP PRO TYR THR PHE GLY GLN GLY THR LYS LEU SEQRES 9 K 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 K 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 K 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 K 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 K 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 K 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 K 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 K 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 K 214 PHE ASN ARG GLY GLU CYS SEQRES 1 L 214 GLU ILE VAL LEU THR GLN SER PRO LEU THR LEU SER VAL SEQRES 2 L 214 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 L 214 GLN SER VAL SER SER ASN LEU ALA TRP TYR GLN GLN MET SEQRES 4 L 214 PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR GLY ALA SER SEQRES 5 L 214 THR ARG ALA THR GLY ILE PRO ALA ARG LEU SER GLY SER SEQRES 6 L 214 ALA SER GLY THR GLU PHE THR LEU THR ILE SER SER LEU SEQRES 7 L 214 GLN SER GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN TYR SEQRES 8 L 214 ASN ASN TRP PRO TYR THR PHE GLY GLN GLY THR LYS LEU SEQRES 9 L 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 L 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 L 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 L 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 L 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 L 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 L 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 L 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 L 214 PHE ASN ARG GLY GLU CYS HET NAG E 1 14 HET NAG E 2 14 HET BMA E 3 11 HET MAN E 4 11 HET NAG E 5 14 HET GAL E 6 11 HET SIA E 7 20 HET NAG F 1 14 HET NAG F 2 14 HET BMA F 3 11 HET MAN F 4 11 HET NAG F 5 14 HET GAL F 6 11 HET SIA F 7 20 HET NAG J 1 14 HET NAG J 2 14 HET BMA J 3 11 HET MAN J 4 11 HET NAG J 5 14 HET GAL J 6 11 HET SIA J 7 20 HET NAG A 601 14 HET NAG A 602 14 HET NAG A 603 14 HET NAG A 604 14 HET NAG B 601 14 HET NAG B 602 14 HET NAG B 603 14 HET NAG B 604 14 HET NAG C 601 14 HET NAG C 602 14 HET NAG C 603 14 HET NAG C 604 14 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BMA BETA-D-MANNOPYRANOSE HETNAM MAN ALPHA-D-MANNOPYRANOSE HETNAM GAL BETA-D-GALACTOPYRANOSE HETNAM SIA N-ACETYL-ALPHA-NEURAMINIC ACID 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 HETSYN GAL BETA-D-GALACTOSE; D-GALACTOSE; GALACTOSE HETSYN SIA N-ACETYLNEURAMINIC ACID; SIALIC ACID; ALPHA-SIALIC HETSYN 2 SIA ACID; O-SIALIC ACID FORMUL 10 NAG 21(C8 H15 N O6) FORMUL 10 BMA 3(C6 H12 O6) FORMUL 10 MAN 3(C6 H12 O6) FORMUL 10 GAL 3(C6 H12 O6) FORMUL 10 SIA 3(C11 H19 N O9) HELIX 1 AA1 SER A 60 GLY A 67 1 8 HELIX 2 AA2 ASN A 68 ILE A 75 5 8 HELIX 3 AA3 ASP A 101 SER A 110 1 10 HELIX 4 AA4 PRO A 122 TRP A 126 5 5 HELIX 5 AA5 ASN A 187 TYR A 195 1 9 HELIX 6 AA6 SER A 374 MET A 393 1 20 HELIX 7 AA7 GLU A 408 LEU A 460 1 53 HELIX 8 AA8 ASP A 479 GLY A 489 1 11 HELIX 9 AA9 ASP A 492 LYS A 503 1 12 HELIX 10 AB1 SER B 60 GLY B 67 1 8 HELIX 11 AB2 ASN B 68 ILE B 75 5 8 HELIX 12 AB3 ASP B 101 SER B 110 1 10 HELIX 13 AB4 PRO B 122 TRP B 126 5 5 HELIX 14 AB5 ASN B 187 LYS B 196 1 10 HELIX 15 AB6 SER B 382 MET B 401 1 20 HELIX 16 AB7 GLU B 416 ARG B 469 1 54 HELIX 17 AB8 ASP B 487 GLY B 497 1 11 HELIX 18 AB9 ASP B 500 TYR B 504 5 5 HELIX 19 AC1 GLU B 506 ARG B 512 1 7 HELIX 20 AC2 SER C 60 GLY C 67 1 8 HELIX 21 AC3 ASN C 68 ILE C 75 5 8 HELIX 22 AC4 ASP C 101 SER C 110 1 10 HELIX 23 AC5 PRO C 122 TRP C 126 5 5 HELIX 24 AC6 ASN C 187 TYR C 195 1 9 HELIX 25 AC7 SER C 382 MET C 401 1 20 HELIX 26 AC8 GLU C 416 ARG C 469 1 54 HELIX 27 AC9 ASP C 487 ARG C 495 1 9 HELIX 28 AD1 ASP C 500 ARG C 512 1 13 HELIX 29 AD2 LYS D 83 THR D 87 5 5 HELIX 30 AD3 LYS G 83 THR G 87 5 5 HELIX 31 AD4 LYS H 83 THR H 87 5 5 SHEET 1 AA1 2 GLN A 6 TYR A 11 0 SHEET 2 AA1 2 TYR A 356 SER A 361 -1 O GLY A 357 N GLY A 10 SHEET 1 AA2 2 GLU A 18 VAL A 20 0 SHEET 2 AA2 2 VAL A 28 VAL A 30 -1 O VAL A 28 N VAL A 20 SHEET 1 AA3 2 ALA A 33 ASP A 35 0 SHEET 2 AA3 2 VAL A 316 ALA A 318 -1 O LEU A 317 N GLN A 34 SHEET 1 AA4 3 LEU A 37 GLU A 38 0 SHEET 2 AA4 3 PHE A 295 HIS A 296 1 O PHE A 295 N GLU A 38 SHEET 3 AA4 3 LYS A 308 TYR A 309 1 O LYS A 308 N HIS A 296 SHEET 1 AA5 2 LEU A 45 LEU A 48 0 SHEET 2 AA5 2 TYR A 275 THR A 280 1 O GLY A 276 N LEU A 45 SHEET 1 AA6 3 LEU A 54 ILE A 55 0 SHEET 2 AA6 3 ILE A 83 GLU A 85 1 O VAL A 84 N LEU A 54 SHEET 3 AA6 3 ILE A 268 LYS A 270 1 O MET A 269 N ILE A 83 SHEET 1 AA7 5 GLY A 97 LEU A 99 0 SHEET 2 AA7 5 ARG A 229 LEU A 237 1 O PHE A 232 N SER A 98 SHEET 3 AA7 5 LEU A 176 HIS A 184 -1 N HIS A 184 O ARG A 229 SHEET 4 AA7 5 TYR A 256 LYS A 263 -1 O TYR A 258 N LEU A 177 SHEET 5 AA7 5 ILE A 112 GLN A 119 -1 N GLU A 116 O LYS A 259 SHEET 1 AA8 5 GLY A 97 LEU A 99 0 SHEET 2 AA8 5 ARG A 229 LEU A 237 1 O PHE A 232 N SER A 98 SHEET 3 AA8 5 LEU A 176 HIS A 184 -1 N HIS A 184 O ARG A 229 SHEET 4 AA8 5 PHE A 251 PRO A 254 -1 O ILE A 252 N GLY A 181 SHEET 5 AA8 5 VAL A 151 TRP A 153 -1 N VAL A 152 O ALA A 253 SHEET 1 AA9 2 SER A 136 TYR A 141 0 SHEET 2 AA9 2 ALA A 144 SER A 146 -1 O ALA A 144 N TYR A 141 SHEET 1 AB1 6 ASN A 210 LEU A 213 0 SHEET 2 AB1 6 ILE A 202 GLY A 205 -1 N VAL A 204 O GLN A 211 SHEET 3 AB1 6 PHE A 245 SER A 247 -1 O GLU A 246 N SER A 203 SHEET 4 AB1 6 ILE A 164 ASN A 169 -1 N ILE A 164 O SER A 247 SHEET 5 AB1 6 HIS H 99 TYR H 100A 1 O PHE H 100 N ASN A 169 SHEET 6 AB1 6 SER H 100E ALA H 100F-1 O SER H 100E N TYR H 100A SHEET 1 AB2 3 GLY A 287 ALA A 288 0 SHEET 2 AB2 3 CYS A 282 THR A 284 -1 N THR A 284 O GLY A 287 SHEET 3 AB2 3 ILE A 303 GLY A 304 -1 O ILE A 303 N GLN A 283 SHEET 1 AB3 3 GLN B 6 TYR B 11 0 SHEET 2 AB3 3 TYR B 364 ASN B 370 -1 O SER B 369 N GLN B 6 SHEET 3 AB3 3 GLY B 373 GLY B 375 -1 O GLY B 373 N ASN B 370 SHEET 1 AB4 2 GLU B 18 VAL B 20 0 SHEET 2 AB4 2 VAL B 28 VAL B 30 -1 O VAL B 28 N VAL B 20 SHEET 1 AB5 2 ALA B 33 ASP B 35 0 SHEET 2 AB5 2 VAL B 324 ALA B 326 -1 O LEU B 325 N GLN B 34 SHEET 1 AB6 3 LEU B 37 GLU B 38 0 SHEET 2 AB6 3 PHE B 303 HIS B 304 1 O PHE B 303 N GLU B 38 SHEET 3 AB6 3 LYS B 316 TYR B 317 1 O LYS B 316 N HIS B 304 SHEET 1 AB7 2 LEU B 45 LEU B 48 0 SHEET 2 AB7 2 TYR B 283 THR B 288 1 O GLY B 284 N LEU B 45 SHEET 1 AB8 3 LEU B 54 ILE B 55 0 SHEET 2 AB8 3 ILE B 83 GLU B 85 1 O VAL B 84 N LEU B 54 SHEET 3 AB8 3 ILE B 276 LYS B 278 1 O MET B 277 N ILE B 83 SHEET 1 AB9 5 GLY B 97 LEU B 99 0 SHEET 2 AB9 5 ARG B 229 LEU B 237 1 O PHE B 232 N SER B 98 SHEET 3 AB9 5 LEU B 176 HIS B 184 -1 N HIS B 184 O ARG B 229 SHEET 4 AB9 5 TYR B 264 LYS B 271 -1 O TYR B 266 N LEU B 177 SHEET 5 AB9 5 ILE B 112 GLN B 119 -1 N GLU B 116 O LYS B 267 SHEET 1 AC1 5 GLY B 97 LEU B 99 0 SHEET 2 AC1 5 ARG B 229 LEU B 237 1 O PHE B 232 N SER B 98 SHEET 3 AC1 5 LEU B 176 HIS B 184 -1 N HIS B 184 O ARG B 229 SHEET 4 AC1 5 PHE B 259 PRO B 262 -1 O ILE B 260 N GLY B 181 SHEET 5 AC1 5 VAL B 151 TRP B 153 -1 N VAL B 152 O ALA B 261 SHEET 1 AC2 2 SER B 136 TYR B 141 0 SHEET 2 AC2 2 ALA B 144 SER B 146 -1 O ALA B 144 N TYR B 141 SHEET 1 AC3 6 ASN B 210 LEU B 213 0 SHEET 2 AC3 6 ILE B 202 GLY B 205 -1 N VAL B 204 O GLN B 211 SHEET 3 AC3 6 ALA B 242 SER B 247 -1 O GLU B 246 N SER B 203 SHEET 4 AC3 6 ILE B 164 ASN B 169 -1 N ILE B 166 O PHE B 245 SHEET 5 AC3 6 HIS D 99 TYR D 100A 1 O PHE D 100 N ASN B 169 SHEET 6 AC3 6 SER D 100E ALA D 100F-1 O SER D 100E N TYR D 100A SHEET 1 AC4 3 GLY B 295 ALA B 296 0 SHEET 2 AC4 3 CYS B 290 THR B 292 -1 N THR B 292 O GLY B 295 SHEET 3 AC4 3 ILE B 311 GLY B 312 -1 O ILE B 311 N GLN B 291 SHEET 1 AC5 3 GLN C 6 TYR C 11 0 SHEET 2 AC5 3 TYR C 364 SER C 369 -1 O GLY C 365 N GLY C 10 SHEET 3 AC5 3 TYR C 376 ALA C 378 -1 O ALA C 377 N TYR C 366 SHEET 1 AC6 2 GLN C 19 VAL C 20 0 SHEET 2 AC6 2 VAL C 28 THR C 29 -1 O VAL C 28 N VAL C 20 SHEET 1 AC7 2 ALA C 33 ASP C 35 0 SHEET 2 AC7 2 VAL C 324 ALA C 326 -1 O LEU C 325 N GLN C 34 SHEET 1 AC8 3 LEU C 37 GLU C 38 0 SHEET 2 AC8 3 PHE C 303 HIS C 304 1 O PHE C 303 N GLU C 38 SHEET 3 AC8 3 LYS C 316 TYR C 317 1 O LYS C 316 N HIS C 304 SHEET 1 AC9 2 LEU C 45 LEU C 48 0 SHEET 2 AC9 2 TYR C 283 THR C 288 1 O GLY C 284 N LEU C 45 SHEET 1 AD1 3 LEU C 54 ILE C 55 0 SHEET 2 AD1 3 ILE C 83 GLU C 85 1 O VAL C 84 N LEU C 54 SHEET 3 AD1 3 ILE C 276 LYS C 278 1 O MET C 277 N ILE C 83 SHEET 1 AD2 5 GLY C 97 LEU C 99 0 SHEET 2 AD2 5 ARG C 229 LEU C 237 1 O PHE C 232 N SER C 98 SHEET 3 AD2 5 LEU C 176 HIS C 184 -1 N HIS C 184 O ARG C 229 SHEET 4 AD2 5 TYR C 264 LYS C 271 -1 O TYR C 266 N LEU C 177 SHEET 5 AD2 5 ILE C 112 GLN C 119 -1 N GLU C 116 O LYS C 267 SHEET 1 AD3 5 GLY C 97 LEU C 99 0 SHEET 2 AD3 5 ARG C 229 LEU C 237 1 O PHE C 232 N SER C 98 SHEET 3 AD3 5 LEU C 176 HIS C 184 -1 N HIS C 184 O ARG C 229 SHEET 4 AD3 5 PHE C 259 PRO C 262 -1 O ILE C 260 N GLY C 181 SHEET 5 AD3 5 VAL C 151 TRP C 153 -1 N VAL C 152 O ALA C 261 SHEET 1 AD4 2 SER C 136 TYR C 141 0 SHEET 2 AD4 2 ALA C 144 SER C 146 -1 O ALA C 144 N TYR C 141 SHEET 1 AD5 6 ASN C 210 LEU C 213 0 SHEET 2 AD5 6 ILE C 202 GLY C 205 -1 N VAL C 204 O GLN C 211 SHEET 3 AD5 6 PHE C 245 SER C 247 -1 O GLU C 246 N SER C 203 SHEET 4 AD5 6 ILE C 164 ASN C 169 -1 N ILE C 166 O PHE C 245 SHEET 5 AD5 6 HIS G 99 TYR G 100A 1 O PHE G 100 N SER C 167 SHEET 6 AD5 6 SER G 100E ALA G 100F-1 O SER G 100E N TYR G 100A SHEET 1 AD6 3 GLY C 295 ALA C 296 0 SHEET 2 AD6 3 CYS C 290 THR C 292 -1 N THR C 292 O GLY C 295 SHEET 3 AD6 3 ILE C 311 GLY C 312 -1 O ILE C 311 N GLN C 291 SHEET 1 AD7 4 VAL D 5 GLN D 6 0 SHEET 2 AD7 4 LEU D 18 LYS D 23 -1 O LYS D 23 N VAL D 5 SHEET 3 AD7 4 THR D 77 TRP D 82 -1 O VAL D 78 N CYS D 22 SHEET 4 AD7 4 VAL D 67 ASP D 72 -1 N ASP D 72 O THR D 77 SHEET 1 AD8 5 TYR D 56 TYR D 59 0 SHEET 2 AD8 5 LEU D 45 ASP D 52 -1 N ARG D 50 O ASN D 58 SHEET 3 AD8 5 PHE D 32 GLN D 39 -1 N ARG D 38 O GLU D 46 SHEET 4 AD8 5 MET D 89 ARG D 96 -1 O ALA D 93 N SER D 35 SHEET 5 AD8 5 SER D 102 TRP D 103 -1 O SER D 102 N TYR D 94 SHEET 1 AD9 4 VAL G 5 GLN G 6 0 SHEET 2 AD9 4 LEU G 18 LYS G 23 -1 O LYS G 23 N VAL G 5 SHEET 3 AD9 4 THR G 77 TRP G 82 -1 O VAL G 78 N CYS G 22 SHEET 4 AD9 4 VAL G 67 ASP G 72 -1 N ASP G 72 O THR G 77 SHEET 1 AE1 5 TYR G 56 TYR G 59 0 SHEET 2 AE1 5 LEU G 45 ASP G 52 -1 N ARG G 50 O ASN G 58 SHEET 3 AE1 5 PHE G 32 GLN G 39 -1 N ARG G 38 O GLU G 46 SHEET 4 AE1 5 MET G 89 ARG G 96 -1 O ALA G 93 N SER G 35 SHEET 5 AE1 5 SER G 102 TRP G 103 -1 O SER G 102 N TYR G 94 SHEET 1 AE2 4 VAL H 5 GLN H 6 0 SHEET 2 AE2 4 LEU H 18 LYS H 23 -1 O LYS H 23 N VAL H 5 SHEET 3 AE2 4 THR H 77 TRP H 82 -1 O VAL H 78 N CYS H 22 SHEET 4 AE2 4 VAL H 67 ASP H 72 -1 N ASP H 72 O THR H 77 SHEET 1 AE3 5 TYR H 56 TYR H 59 0 SHEET 2 AE3 5 LEU H 45 ASP H 52 -1 N ARG H 50 O ASN H 58 SHEET 3 AE3 5 PHE H 32 GLN H 39 -1 N ARG H 38 O GLU H 46 SHEET 4 AE3 5 MET H 89 ARG H 96 -1 O ALA H 93 N SER H 35 SHEET 5 AE3 5 SER H 102 TRP H 103 -1 O SER H 102 N TYR H 94 SHEET 1 AE4 4 THR I 5 SER I 7 0 SHEET 2 AE4 4 ALA I 19 ARG I 24 -1 O ARG I 24 N THR I 5 SHEET 3 AE4 4 GLU I 70 ILE I 75 -1 O LEU I 73 N LEU I 21 SHEET 4 AE4 4 LEU I 62 SER I 67 -1 N SER I 67 O GLU I 70 SHEET 1 AE5 6 THR I 10 VAL I 13 0 SHEET 2 AE5 6 THR I 102 ILE I 106 1 O GLU I 105 N LEU I 11 SHEET 3 AE5 6 VAL I 85 GLN I 90 -1 N TYR I 86 O THR I 102 SHEET 4 AE5 6 LEU I 33 GLN I 38 -1 N ALA I 34 O GLN I 89 SHEET 5 AE5 6 ARG I 45 TYR I 49 -1 O LEU I 47 N TRP I 35 SHEET 6 AE5 6 THR I 53 ARG I 54 -1 O THR I 53 N TYR I 49 SHEET 1 AE6 4 THR I 10 VAL I 13 0 SHEET 2 AE6 4 THR I 102 ILE I 106 1 O GLU I 105 N LEU I 11 SHEET 3 AE6 4 VAL I 85 GLN I 90 -1 N TYR I 86 O THR I 102 SHEET 4 AE6 4 THR I 97 PHE I 98 -1 O THR I 97 N GLN I 90 SHEET 1 AE7 4 THR K 5 SER K 7 0 SHEET 2 AE7 4 ALA K 19 ARG K 24 -1 O ARG K 24 N THR K 5 SHEET 3 AE7 4 GLU K 70 ILE K 75 -1 O LEU K 73 N LEU K 21 SHEET 4 AE7 4 LEU K 62 SER K 67 -1 N SER K 67 O GLU K 70 SHEET 1 AE8 6 THR K 10 VAL K 13 0 SHEET 2 AE8 6 THR K 102 ILE K 106 1 O GLU K 105 N LEU K 11 SHEET 3 AE8 6 VAL K 85 GLN K 90 -1 N TYR K 86 O THR K 102 SHEET 4 AE8 6 LEU K 33 GLN K 38 -1 N ALA K 34 O GLN K 89 SHEET 5 AE8 6 ARG K 45 TYR K 49 -1 O LEU K 47 N TRP K 35 SHEET 6 AE8 6 THR K 53 ARG K 54 -1 O THR K 53 N TYR K 49 SHEET 1 AE9 4 THR K 10 VAL K 13 0 SHEET 2 AE9 4 THR K 102 ILE K 106 1 O GLU K 105 N LEU K 11 SHEET 3 AE9 4 VAL K 85 GLN K 90 -1 N TYR K 86 O THR K 102 SHEET 4 AE9 4 THR K 97 PHE K 98 -1 O THR K 97 N GLN K 90 SHEET 1 AF1 4 THR L 5 SER L 7 0 SHEET 2 AF1 4 ALA L 19 ARG L 24 -1 O ARG L 24 N THR L 5 SHEET 3 AF1 4 GLU L 70 ILE L 75 -1 O LEU L 73 N LEU L 21 SHEET 4 AF1 4 LEU L 62 SER L 67 -1 N SER L 67 O GLU L 70 SHEET 1 AF2 6 THR L 10 VAL L 13 0 SHEET 2 AF2 6 THR L 102 ILE L 106 1 O GLU L 105 N LEU L 11 SHEET 3 AF2 6 VAL L 85 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AF2 6 LEU L 33 GLN L 38 -1 N ALA L 34 O GLN L 89 SHEET 5 AF2 6 ARG L 45 TYR L 49 -1 O LEU L 47 N TRP L 35 SHEET 6 AF2 6 THR L 53 ARG L 54 -1 O THR L 53 N TYR L 49 SHEET 1 AF3 4 THR L 10 VAL L 13 0 SHEET 2 AF3 4 THR L 102 ILE L 106 1 O GLU L 105 N LEU L 11 SHEET 3 AF3 4 VAL L 85 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AF3 4 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90 SSBOND 1 CYS A 8 CYS A 471 1555 1555 2.03 SSBOND 2 CYS A 46 CYS A 278 1555 1555 2.03 SSBOND 3 CYS A 59 CYS A 71 1555 1555 2.03 SSBOND 4 CYS A 282 CYS A 306 1555 1555 2.03 SSBOND 5 CYS A 478 CYS A 482 1555 1555 2.04 SSBOND 6 CYS B 8 CYS B 479 1555 1555 2.03 SSBOND 7 CYS B 46 CYS B 286 1555 1555 2.03 SSBOND 8 CYS B 59 CYS B 71 1555 1555 2.03 SSBOND 9 CYS B 290 CYS B 314 1555 1555 2.03 SSBOND 10 CYS B 486 CYS B 490 1555 1555 2.03 SSBOND 11 CYS C 8 CYS C 479 1555 1555 2.03 SSBOND 12 CYS C 46 CYS C 286 1555 1555 2.03 SSBOND 13 CYS C 59 CYS C 71 1555 1555 2.03 SSBOND 14 CYS C 290 CYS C 314 1555 1555 2.03 SSBOND 15 CYS C 486 CYS C 490 1555 1555 2.03 SSBOND 16 CYS D 22 CYS D 92 1555 1555 2.03 SSBOND 17 CYS G 22 CYS G 92 1555 1555 2.03 SSBOND 18 CYS H 22 CYS H 92 1555 1555 2.03 SSBOND 19 CYS I 23 CYS I 88 1555 1555 2.03 SSBOND 20 CYS K 23 CYS K 88 1555 1555 2.04 SSBOND 21 CYS L 23 CYS L 88 1555 1555 2.03 LINK ND2 ASN A 14 C1 NAG A 603 1555 1555 1.46 LINK ND2 ASN A 27 C1 NAG A 601 1555 1555 1.45 LINK ND2 ASN A 290 C1 NAG A 602 1555 1555 1.45 LINK ND2 ASN A 488 C1 NAG A 604 1555 1555 1.43 LINK ND2 ASN B 14 C1 NAG B 603 1555 1555 1.47 LINK ND2 ASN B 27 C1 NAG B 601 1555 1555 1.45 LINK ND2 ASN B 298 C1 NAG B 602 1555 1555 1.45 LINK ND2 ASN B 496 C1 NAG B 604 1555 1555 1.44 LINK ND2 ASN C 14 C1 NAG C 603 1555 1555 1.45 LINK ND2 ASN C 27 C1 NAG C 601 1555 1555 1.45 LINK ND2 ASN C 298 C1 NAG C 602 1555 1555 1.45 LINK ND2 ASN C 496 C1 NAG C 604 1555 1555 1.44 LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.43 LINK O4 NAG E 2 C1 BMA E 3 1555 1555 1.45 LINK O3 BMA E 3 C1 MAN E 4 1555 1555 1.45 LINK O2 MAN E 4 C1 NAG E 5 1555 1555 1.44 LINK O4 NAG E 5 C1 GAL E 6 1555 1555 1.44 LINK O3 GAL E 6 C2 SIA E 7 1555 1555 1.44 LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.44 LINK O4 NAG F 2 C1 BMA F 3 1555 1555 1.45 LINK O3 BMA F 3 C1 MAN F 4 1555 1555 1.45 LINK O2 MAN F 4 C1 NAG F 5 1555 1555 1.44 LINK O4 NAG F 5 C1 GAL F 6 1555 1555 1.44 LINK O3 GAL F 6 C2 SIA F 7 1555 1555 1.44 LINK O4 NAG J 1 C1 NAG J 2 1555 1555 1.43 LINK O4 NAG J 2 C1 BMA J 3 1555 1555 1.45 LINK O3 BMA J 3 C1 MAN J 4 1555 1555 1.45 LINK O2 MAN J 4 C1 NAG J 5 1555 1555 1.44 LINK O4 NAG J 5 C1 GAL J 6 1555 1555 1.44 LINK O3 GAL J 6 C2 SIA J 7 1555 1555 1.44 CISPEP 1 SER I 7 PRO I 8 0 -5.21 CISPEP 2 TRP I 94 PRO I 95 0 9.88 CISPEP 3 SER K 7 PRO K 8 0 -5.22 CISPEP 4 TRP K 94 PRO K 95 0 9.94 CISPEP 5 SER L 7 PRO L 8 0 -5.22 CISPEP 6 TRP L 94 PRO L 95 0 9.89 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