HEADER VIRAL PROTEIN 16-SEP-24 9GST TITLE LN02-ML85 FAB IN COMPLEX WITH CROSSLINKED DS-SOSIP HIV-1 ENV TRIMER COMPND MOL_ID: 1; COMPND 2 MOLECULE: ENVELOPE GLYCOPROTEIN GP160; COMPND 3 CHAIN: A, C, E; COMPND 4 SYNONYM: ENV POLYPROTEIN; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: ENVELOPE GLYCOPROTEIN GP160; COMPND 8 CHAIN: B, D, F; COMPND 9 SYNONYM: ENV POLYPROTEIN; COMPND 10 ENGINEERED: YES; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: HEAVY CHAIN FAB OF ANTIBODY LN02-ML85; COMPND 13 CHAIN: H; COMPND 14 ENGINEERED: YES; COMPND 15 MOL_ID: 4; COMPND 16 MOLECULE: LIGHT CHAIN OF ANTIBODY LN02-ML85; COMPND 17 CHAIN: L; COMPND 18 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 3 ORGANISM_TAXID: 11676; SOURCE 4 GENE: ENV; SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 9 ORGANISM_TAXID: 11676; SOURCE 10 GENE: ENV; SOURCE 11 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 13 MOL_ID: 3; SOURCE 14 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 15 ORGANISM_TAXID: 9606; SOURCE 16 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 18 MOL_ID: 4; SOURCE 19 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 20 ORGANISM_TAXID: 9606; SOURCE 21 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 22 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS HIV-1, COMPLEX, ANTIBODY, FAB, ENV, VIRAL PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR B.PEDENKO,G.EFFANTIN,W.WEISSENHORN REVDAT 1 24-SEP-25 9GST 0 JRNL AUTH B.PEDENKO,G.EFFANTIN,W.WEISSENHORN,C.FENWICK JRNL TITL STRUCTURE OF LN02-ML85 FAB IN COMPLEX WITH DS-SOSIP JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.10 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : PHENIX REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : NULL REMARK 3 REFINEMENT SPACE : NULL REMARK 3 REFINEMENT PROTOCOL : NULL REMARK 3 REFINEMENT TARGET : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL REMARK 3 REMARK 3 FITTING PROCEDURE : NULL REMARK 3 REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 3.100 REMARK 3 NUMBER OF PARTICLES : 98398 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 9GST COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-SEP-24. REMARK 100 THE DEPOSITION ID IS D_1292141761. 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 HIV-1 DS-SOSIP ENV REMARK 245 TRIMER WITH LN02-ML85 FAB 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 : 7.00 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : TFS KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 BIOQUANTUM (6K X REMARK 245 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1000.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2200.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : NULL REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 5020.00 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: OCTAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, H, L, G, I, REMARK 350 AND CHAINS: J, K, M, N, O, P, Q, R, S, REMARK 350 AND CHAINS: T, U, V, W, X, Y, Z, a, b, c, REMARK 350 AND CHAINS: d, e, f, g, h, i, 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 ALA A 31 REMARK 465 GLU A 32 REMARK 465 ASN A 33 REMARK 465 LYS A 59 REMARK 465 ALA A 60 REMARK 465 TYR A 61 REMARK 465 GLU A 62 REMARK 465 THR A 63 REMARK 465 GLU A 64 REMARK 465 LYS A 65 REMARK 465 HIS A 66 REMARK 465 ASN A 67 REMARK 465 GLU A 185A REMARK 465 ASN A 185B REMARK 465 GLN A 185C REMARK 465 GLY A 185D REMARK 465 ASN A 185E REMARK 465 ARG A 185F REMARK 465 SER A 185G REMARK 465 ASN A 185H REMARK 465 ASN A 185I REMARK 465 SER A 185J REMARK 465 ASN A 185K REMARK 465 THR A 400 REMARK 465 SER A 401 REMARK 465 VAL A 402 REMARK 465 GLN A 403 REMARK 465 GLY A 404 REMARK 465 SER A 405 REMARK 465 ASN A 406 REMARK 465 SER A 407 REMARK 465 THR A 408 REMARK 465 GLY A 409 REMARK 465 SER A 410 REMARK 465 ARG A 504 REMARK 465 VAL A 505 REMARK 465 VAL A 506 REMARK 465 GLY A 507 REMARK 465 ARG A 508 REMARK 465 ARG A 509 REMARK 465 ARG A 510 REMARK 465 ARG A 511 REMARK 465 ARG A 512 REMARK 465 ARG A 513 REMARK 465 ALA B 512 REMARK 465 VAL B 513 REMARK 465 GLY B 514 REMARK 465 ILE B 515 REMARK 465 GLY B 516 REMARK 465 ALA B 517 REMARK 465 VAL B 518 REMARK 465 PHE B 519 REMARK 465 ARG B 542 REMARK 465 ASN B 543 REMARK 465 LEU B 544 REMARK 465 LEU B 545 REMARK 465 SER B 546 REMARK 465 GLY B 547 REMARK 465 ILE B 548 REMARK 465 VAL B 549 REMARK 465 GLN B 550 REMARK 465 GLN B 551 REMARK 465 GLN B 552 REMARK 465 SER B 553 REMARK 465 ASN B 554 REMARK 465 LEU B 555 REMARK 465 LEU B 556 REMARK 465 ARG B 557 REMARK 465 ALA B 558 REMARK 465 PRO B 559 REMARK 465 GLU B 560 REMARK 465 ALA B 561 REMARK 465 GLN B 562 REMARK 465 GLN B 563 REMARK 465 HIS B 564 REMARK 465 LEU B 565 REMARK 465 LEU B 566 REMARK 465 LYS B 567 REMARK 465 LEU B 661 REMARK 465 ALA B 662 REMARK 465 LEU B 663 REMARK 465 ASP B 664 REMARK 465 ASP B 665 REMARK 465 TYR B 666 REMARK 465 LYS B 667 REMARK 465 ASP B 668 REMARK 465 ASP B 669 REMARK 465 ASP B 670 REMARK 465 ASP B 671 REMARK 465 LYS B 672 REMARK 465 ALA C 31 REMARK 465 GLU C 32 REMARK 465 ASN C 33 REMARK 465 LYS C 59 REMARK 465 ALA C 60 REMARK 465 TYR C 61 REMARK 465 GLU C 62 REMARK 465 THR C 63 REMARK 465 GLU C 64 REMARK 465 LYS C 65 REMARK 465 HIS C 66 REMARK 465 ASN C 67 REMARK 465 VAL C 68 REMARK 465 TRP C 69 REMARK 465 ALA C 70 REMARK 465 THR C 71 REMARK 465 HIS C 72 REMARK 465 ASN C 184A REMARK 465 GLU C 184B REMARK 465 ASN C 184C REMARK 465 GLN C 184D REMARK 465 GLY C 184E REMARK 465 ASN C 184F REMARK 465 ARG C 184G REMARK 465 SER C 184H REMARK 465 ASN C 184I REMARK 465 ASN C 184J REMARK 465 SER C 184K REMARK 465 ASN C 184L REMARK 465 ASN C 399 REMARK 465 THR C 400 REMARK 465 SER C 401 REMARK 465 VAL C 402 REMARK 465 GLN C 403 REMARK 465 GLY C 404 REMARK 465 SER C 405 REMARK 465 ASN C 406 REMARK 465 SER C 407 REMARK 465 THR C 408 REMARK 465 GLY C 409 REMARK 465 SER C 410 REMARK 465 ARG C 504 REMARK 465 VAL C 505 REMARK 465 VAL C 506 REMARK 465 GLY C 507 REMARK 465 ARG C 508 REMARK 465 ARG C 509 REMARK 465 ARG C 510 REMARK 465 ARG C 511 REMARK 465 ARG C 512 REMARK 465 ARG C 513 REMARK 465 ALA D 512 REMARK 465 VAL D 513 REMARK 465 GLY D 514 REMARK 465 ILE D 515 REMARK 465 GLY D 516 REMARK 465 ALA D 517 REMARK 465 VAL D 518 REMARK 465 PHE D 519 REMARK 465 LEU D 520 REMARK 465 GLY D 521 REMARK 465 GLY D 547 REMARK 465 ILE D 548 REMARK 465 VAL D 549 REMARK 465 GLN D 550 REMARK 465 GLN D 551 REMARK 465 GLN D 552 REMARK 465 SER D 553 REMARK 465 ASN D 554 REMARK 465 LEU D 555 REMARK 465 LEU D 556 REMARK 465 ARG D 557 REMARK 465 ALA D 558 REMARK 465 PRO D 559 REMARK 465 GLU D 560 REMARK 465 ALA D 561 REMARK 465 GLN D 562 REMARK 465 GLN D 563 REMARK 465 HIS D 564 REMARK 465 LEU D 565 REMARK 465 LEU D 566 REMARK 465 LYS D 567 REMARK 465 LYS D 655 REMARK 465 ASN D 656 REMARK 465 GLU D 657 REMARK 465 GLN D 658 REMARK 465 ASP D 659 REMARK 465 LEU D 660 REMARK 465 LEU D 661 REMARK 465 ALA D 662 REMARK 465 LEU D 663 REMARK 465 ASP D 664 REMARK 465 ASP D 665 REMARK 465 TYR D 666 REMARK 465 LYS D 667 REMARK 465 ASP D 668 REMARK 465 ASP D 669 REMARK 465 ASP D 670 REMARK 465 ASP D 671 REMARK 465 LYS D 672 REMARK 465 ALA E 31 REMARK 465 GLU E 32 REMARK 465 ASN E 33 REMARK 465 ALA E 58 REMARK 465 LYS E 59 REMARK 465 ALA E 60 REMARK 465 TYR E 61 REMARK 465 GLU E 62 REMARK 465 THR E 63 REMARK 465 GLU E 64 REMARK 465 LYS E 65 REMARK 465 HIS E 66 REMARK 465 ASN E 67 REMARK 465 VAL E 68 REMARK 465 TRP E 69 REMARK 465 ALA E 70 REMARK 465 THR E 71 REMARK 465 HIS E 72 REMARK 465 GLU E 185A REMARK 465 ASN E 185B REMARK 465 GLN E 185C REMARK 465 GLY E 185D REMARK 465 ASN E 185E REMARK 465 ARG E 185F REMARK 465 SER E 185G REMARK 465 ASN E 185H REMARK 465 ASN E 185I REMARK 465 SER E 185J REMARK 465 ASN E 185K REMARK 465 THR E 400 REMARK 465 SER E 401 REMARK 465 VAL E 402 REMARK 465 GLN E 403 REMARK 465 GLY E 404 REMARK 465 SER E 405 REMARK 465 ASN E 406 REMARK 465 SER E 407 REMARK 465 THR E 408 REMARK 465 GLY E 409 REMARK 465 SER E 410 REMARK 465 GLY E 458 REMARK 465 GLY E 459 REMARK 465 SER E 460 REMARK 465 THR E 461 REMARK 465 ASN E 462 REMARK 465 SER E 463 REMARK 465 ARG E 504 REMARK 465 VAL E 505 REMARK 465 VAL E 506 REMARK 465 GLY E 507 REMARK 465 ARG E 508 REMARK 465 ARG E 509 REMARK 465 ARG E 510 REMARK 465 ARG E 511 REMARK 465 ARG E 512 REMARK 465 ARG E 513 REMARK 465 ALA F 512 REMARK 465 VAL F 513 REMARK 465 GLY F 514 REMARK 465 ILE F 515 REMARK 465 GLY F 516 REMARK 465 ALA F 517 REMARK 465 VAL F 518 REMARK 465 PHE F 519 REMARK 465 LEU F 520 REMARK 465 GLY F 521 REMARK 465 GLY F 547 REMARK 465 ILE F 548 REMARK 465 VAL F 549 REMARK 465 GLN F 550 REMARK 465 GLN F 551 REMARK 465 GLN F 552 REMARK 465 SER F 553 REMARK 465 ASN F 554 REMARK 465 LEU F 555 REMARK 465 LEU F 556 REMARK 465 ARG F 557 REMARK 465 ALA F 558 REMARK 465 PRO F 559 REMARK 465 GLU F 560 REMARK 465 ALA F 561 REMARK 465 GLN F 562 REMARK 465 GLN F 563 REMARK 465 HIS F 564 REMARK 465 LEU F 565 REMARK 465 LEU F 566 REMARK 465 LYS F 567 REMARK 465 ASP F 659 REMARK 465 LEU F 660 REMARK 465 LEU F 661 REMARK 465 ALA F 662 REMARK 465 LEU F 663 REMARK 465 ASP F 664 REMARK 465 ASP F 665 REMARK 465 TYR F 666 REMARK 465 LYS F 667 REMARK 465 ASP F 668 REMARK 465 ASP F 669 REMARK 465 ASP F 670 REMARK 465 ASP F 671 REMARK 465 LYS F 672 REMARK 465 ALA H 124 REMARK 465 SER H 125 REMARK 465 THR H 126 REMARK 465 LYS H 127 REMARK 465 GLY H 128 REMARK 465 PRO H 129 REMARK 465 SER H 130 REMARK 465 VAL H 131 REMARK 465 PHE H 132 REMARK 465 PRO H 133 REMARK 465 LEU H 134 REMARK 465 ALA H 135 REMARK 465 PRO H 136 REMARK 465 SER H 137 REMARK 465 SER H 138 REMARK 465 LYS H 139 REMARK 465 SER H 140 REMARK 465 THR H 141 REMARK 465 SER H 142 REMARK 465 GLY H 143 REMARK 465 GLY H 144 REMARK 465 THR H 145 REMARK 465 ALA H 146 REMARK 465 ALA H 147 REMARK 465 LEU H 148 REMARK 465 GLY H 149 REMARK 465 CYS H 150 REMARK 465 LEU H 151 REMARK 465 VAL H 152 REMARK 465 LYS H 153 REMARK 465 ASP H 154 REMARK 465 TYR H 155 REMARK 465 PHE H 156 REMARK 465 PRO H 157 REMARK 465 GLU H 158 REMARK 465 PRO H 159 REMARK 465 VAL H 160 REMARK 465 THR H 161 REMARK 465 VAL H 162 REMARK 465 SER H 163 REMARK 465 TRP H 164 REMARK 465 ASN H 165 REMARK 465 SER H 166 REMARK 465 GLY H 167 REMARK 465 ALA H 168 REMARK 465 LEU H 169 REMARK 465 THR H 170 REMARK 465 SER H 171 REMARK 465 GLY H 172 REMARK 465 VAL H 173 REMARK 465 HIS H 174 REMARK 465 THR H 175 REMARK 465 PHE H 176 REMARK 465 PRO H 177 REMARK 465 ALA H 178 REMARK 465 VAL H 179 REMARK 465 LEU H 180 REMARK 465 GLN H 181 REMARK 465 SER H 182 REMARK 465 SER H 183 REMARK 465 GLY H 184 REMARK 465 LEU H 185 REMARK 465 TYR H 186 REMARK 465 SER H 187 REMARK 465 LEU H 188 REMARK 465 SER H 189 REMARK 465 SER H 190 REMARK 465 VAL H 191 REMARK 465 VAL H 192 REMARK 465 THR H 193 REMARK 465 VAL H 194 REMARK 465 PRO H 195 REMARK 465 SER H 196 REMARK 465 SER H 197 REMARK 465 SER H 198 REMARK 465 LEU H 199 REMARK 465 GLY H 200 REMARK 465 THR H 201 REMARK 465 GLN H 202 REMARK 465 THR H 203 REMARK 465 TYR H 204 REMARK 465 ILE H 205 REMARK 465 CYS H 206 REMARK 465 ASN H 207 REMARK 465 VAL H 208 REMARK 465 ASN H 209 REMARK 465 HIS H 210 REMARK 465 LYS H 211 REMARK 465 PRO H 212 REMARK 465 SER H 213 REMARK 465 ASN H 214 REMARK 465 THR H 215 REMARK 465 LYS H 216 REMARK 465 VAL H 217 REMARK 465 ASP H 218 REMARK 465 LYS H 219 REMARK 465 ARG H 220 REMARK 465 VAL H 221 REMARK 465 GLU H 222 REMARK 465 PRO H 223 REMARK 465 LYS H 224 REMARK 465 SER L 1 REMARK 465 GLN L 110 REMARK 465 PRO L 111 REMARK 465 LYS L 112 REMARK 465 ALA L 113 REMARK 465 ALA L 114 REMARK 465 PRO L 115 REMARK 465 SER L 116 REMARK 465 VAL L 117 REMARK 465 THR L 118 REMARK 465 LEU L 119 REMARK 465 PHE L 120 REMARK 465 PRO L 121 REMARK 465 PRO L 122 REMARK 465 SER L 123 REMARK 465 SER L 124 REMARK 465 GLU L 125 REMARK 465 GLU L 126 REMARK 465 LEU L 127 REMARK 465 GLN L 128 REMARK 465 ALA L 129 REMARK 465 ASN L 130 REMARK 465 LYS L 131 REMARK 465 ALA L 132 REMARK 465 THR L 133 REMARK 465 LEU L 134 REMARK 465 VAL L 135 REMARK 465 CYS L 136 REMARK 465 LEU L 137 REMARK 465 ILE L 138 REMARK 465 SER L 139 REMARK 465 ASP L 140 REMARK 465 PHE L 141 REMARK 465 TYR L 142 REMARK 465 PRO L 143 REMARK 465 GLY L 144 REMARK 465 ALA L 145 REMARK 465 VAL L 146 REMARK 465 THR L 147 REMARK 465 VAL L 148 REMARK 465 ALA L 149 REMARK 465 TRP L 150 REMARK 465 LYS L 151 REMARK 465 ALA L 152 REMARK 465 ASP L 153 REMARK 465 SER L 154 REMARK 465 SER L 155 REMARK 465 PRO L 156 REMARK 465 VAL L 157 REMARK 465 LYS L 158 REMARK 465 ALA L 159 REMARK 465 GLY L 160 REMARK 465 VAL L 161 REMARK 465 GLU L 162 REMARK 465 THR L 163 REMARK 465 THR L 164 REMARK 465 THR L 165 REMARK 465 PRO L 166 REMARK 465 SER L 167 REMARK 465 LYS L 168 REMARK 465 GLN L 169 REMARK 465 SER L 170 REMARK 465 ASN L 171 REMARK 465 ASN L 172 REMARK 465 LYS L 173 REMARK 465 TYR L 174 REMARK 465 ALA L 175 REMARK 465 ALA L 176 REMARK 465 SER L 177 REMARK 465 SER L 178 REMARK 465 TYR L 179 REMARK 465 LEU L 180 REMARK 465 SER L 181 REMARK 465 LEU L 182 REMARK 465 THR L 183 REMARK 465 PRO L 184 REMARK 465 GLU L 185 REMARK 465 GLN L 186 REMARK 465 TRP L 187 REMARK 465 LYS L 188 REMARK 465 SER L 189 REMARK 465 HIS L 190 REMARK 465 ARG L 191 REMARK 465 SER L 192 REMARK 465 TYR L 193 REMARK 465 SER L 194 REMARK 465 CYS L 195 REMARK 465 GLN L 196 REMARK 465 VAL L 197 REMARK 465 THR L 198 REMARK 465 HIS L 199 REMARK 465 GLU L 200 REMARK 465 GLY L 201 REMARK 465 SER L 202 REMARK 465 THR L 203 REMARK 465 VAL L 204 REMARK 465 GLU L 205 REMARK 465 LYS L 206 REMARK 465 THR L 207 REMARK 465 VAL L 208 REMARK 465 ALA L 209 REMARK 465 PRO L 210 REMARK 465 THR L 211 REMARK 465 GLU L 212 REMARK 465 CYS L 213 REMARK 465 SER L 214 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 OE1 GLU C 275 NZ LYS C 282 2.16 REMARK 500 ND2 ASN A 195 O SER A 199 2.17 REMARK 500 O LEU C 369 OG1 THR C 373 2.17 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 CYS C 247 CA - CB - SG ANGL. DEV. = 7.4 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 ALA A 55 115.61 -165.62 REMARK 500 LEU A 116 44.01 -109.84 REMARK 500 PRO A 118 11.51 -65.75 REMARK 500 THR A 135 74.47 -69.36 REMARK 500 ASP A 140 -2.37 69.97 REMARK 500 ASP A 141 -39.52 -135.49 REMARK 500 MET A 150 54.09 -94.02 REMARK 500 THR A 163 -164.47 -116.11 REMARK 500 CYS A 196 42.54 -82.26 REMARK 500 ASN A 197 10.66 -150.86 REMARK 500 THR A 198 -33.45 -135.46 REMARK 500 PRO A 240 42.51 -84.65 REMARK 500 SER A 241 101.34 -160.44 REMARK 500 GLU A 268 -8.88 74.78 REMARK 500 ILE A 396 -69.62 -91.51 REMARK 500 ASN A 425 78.94 -100.59 REMARK 500 GLN A 428 9.62 55.24 REMARK 500 LEU A 483 50.62 -91.13 REMARK 500 LEU B 523 1.86 -65.51 REMARK 500 SER B 534 -36.97 -39.66 REMARK 500 THR B 536 1.30 -59.33 REMARK 500 GLN B 540 -6.73 63.99 REMARK 500 GLN B 575 45.18 -86.39 REMARK 500 LEU B 576 -40.66 -131.07 REMARK 500 SER B 613 31.02 -141.98 REMARK 500 ARG B 617 -63.01 -109.25 REMARK 500 ASN B 618 -179.44 174.32 REMARK 500 ASN B 625 25.03 -141.34 REMARK 500 GLN B 650 -13.12 70.27 REMARK 500 ASN B 651 -54.65 -124.10 REMARK 500 ALA C 55 46.19 -141.86 REMARK 500 THR C 135 23.06 45.75 REMARK 500 ASN C 137 72.91 -69.38 REMARK 500 MET C 150 41.75 -103.68 REMARK 500 GLN C 258 -9.86 73.15 REMARK 500 LEU C 259 117.72 -162.20 REMARK 500 ASN C 262 49.41 33.71 REMARK 500 GLU C 268 -7.33 72.25 REMARK 500 ASN C 301 116.32 -38.95 REMARK 500 THR C 387 54.45 -90.02 REMARK 500 LEU C 483 54.35 -94.15 REMARK 500 CYS C 501 -84.79 16.52 REMARK 500 LYS C 502 149.25 75.28 REMARK 500 SER D 615 -70.69 63.14 REMARK 500 ASN D 625 37.08 -140.13 REMARK 500 LEU D 645 46.96 -65.58 REMARK 500 LEU D 646 -26.31 -148.65 REMARK 500 SER D 649 -3.51 -56.82 REMARK 500 THR E 135 -159.60 -91.43 REMARK 500 ASN E 136 77.37 66.98 REMARK 500 REMARK 500 THIS ENTRY HAS 68 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-51554 RELATED DB: EMDB REMARK 900 LN02-ML85 FAB IN COMPLEX WITH CROSSLINKED DS-SOSIP HIV-1 ENV TRIMER DBREF1 9GST A 31 511 UNP A0A6H1VH54_9PLVG DBREF2 9GST A A0A6H1VH54 30 508 DBREF1 9GST B 512 666 UNP A0A6H1VGP3_9PLVG DBREF2 9GST B A0A6H1VGP3 508 662 DBREF1 9GST C 31 511 UNP A0A6H1VH54_9PLVG DBREF2 9GST C A0A6H1VH54 30 508 DBREF1 9GST D 512 666 UNP A0A6H1VGP3_9PLVG DBREF2 9GST D A0A6H1VGP3 508 662 DBREF1 9GST E 31 511 UNP A0A6H1VH54_9PLVG DBREF2 9GST E A0A6H1VH54 30 508 DBREF1 9GST F 512 666 UNP A0A6H1VGP3_9PLVG DBREF2 9GST F A0A6H1VGP3 508 662 DBREF 9GST H 1 224 PDB 9GST 9GST 1 224 DBREF 9GST L 1 214 PDB 9GST 9GST 1 214 SEQADV 9GST CYS A 201 UNP A0A6H1VH5 ILE 200 CONFLICT SEQADV 9GST SER A 375 UNP A0A6H1VH5 TYR 373 CONFLICT SEQADV 9GST CYS A 433 UNP A0A6H1VH5 ALA 430 CONFLICT SEQADV 9GST CYS A 501 UNP A0A6H1VH5 ALA 498 CONFLICT SEQADV 9GST ARG A 509 UNP A0A6H1VH5 GLU 506 CONFLICT SEQADV 9GST ARG A 512 UNP A0A6H1VH5 EXPRESSION TAG SEQADV 9GST ARG A 513 UNP A0A6H1VH5 EXPRESSION TAG SEQADV 9GST PRO B 559 UNP A0A6H1VGP ILE 555 CONFLICT SEQADV 9GST CYS B 605 UNP A0A6H1VGP THR 601 CONFLICT SEQADV 9GST ASP B 665 UNP A0A6H1VGP LYS 661 CONFLICT SEQADV 9GST TYR B 666 UNP A0A6H1VGP TRP 662 CONFLICT SEQADV 9GST LYS B 667 UNP A0A6H1VGP EXPRESSION TAG SEQADV 9GST ASP B 668 UNP A0A6H1VGP EXPRESSION TAG SEQADV 9GST ASP B 669 UNP A0A6H1VGP EXPRESSION TAG SEQADV 9GST ASP B 670 UNP A0A6H1VGP EXPRESSION TAG SEQADV 9GST ASP B 671 UNP A0A6H1VGP EXPRESSION TAG SEQADV 9GST LYS B 672 UNP A0A6H1VGP EXPRESSION TAG SEQADV 9GST CYS C 201 UNP A0A6H1VH5 ILE 200 CONFLICT SEQADV 9GST SER C 375 UNP A0A6H1VH5 TYR 373 CONFLICT SEQADV 9GST CYS C 433 UNP A0A6H1VH5 ALA 430 CONFLICT SEQADV 9GST CYS C 501 UNP A0A6H1VH5 ALA 498 CONFLICT SEQADV 9GST ARG C 509 UNP A0A6H1VH5 GLU 506 CONFLICT SEQADV 9GST ARG C 512 UNP A0A6H1VH5 EXPRESSION TAG SEQADV 9GST ARG C 513 UNP A0A6H1VH5 EXPRESSION TAG SEQADV 9GST PRO D 559 UNP A0A6H1VGP ILE 555 CONFLICT SEQADV 9GST CYS D 605 UNP A0A6H1VGP THR 601 CONFLICT SEQADV 9GST ASP D 665 UNP A0A6H1VGP LYS 661 CONFLICT SEQADV 9GST TYR D 666 UNP A0A6H1VGP TRP 662 CONFLICT SEQADV 9GST LYS D 667 UNP A0A6H1VGP EXPRESSION TAG SEQADV 9GST ASP D 668 UNP A0A6H1VGP EXPRESSION TAG SEQADV 9GST ASP D 669 UNP A0A6H1VGP EXPRESSION TAG SEQADV 9GST ASP D 670 UNP A0A6H1VGP EXPRESSION TAG SEQADV 9GST ASP D 671 UNP A0A6H1VGP EXPRESSION TAG SEQADV 9GST LYS D 672 UNP A0A6H1VGP EXPRESSION TAG SEQADV 9GST CYS E 201 UNP A0A6H1VH5 ILE 200 CONFLICT SEQADV 9GST SER E 375 UNP A0A6H1VH5 TYR 373 CONFLICT SEQADV 9GST CYS E 433 UNP A0A6H1VH5 ALA 430 CONFLICT SEQADV 9GST CYS E 501 UNP A0A6H1VH5 ALA 498 CONFLICT SEQADV 9GST ARG E 509 UNP A0A6H1VH5 GLU 506 CONFLICT SEQADV 9GST ARG E 512 UNP A0A6H1VH5 EXPRESSION TAG SEQADV 9GST ARG E 513 UNP A0A6H1VH5 EXPRESSION TAG SEQADV 9GST PRO F 559 UNP A0A6H1VGP ILE 555 CONFLICT SEQADV 9GST CYS F 605 UNP A0A6H1VGP THR 601 CONFLICT SEQADV 9GST ASP F 665 UNP A0A6H1VGP LYS 661 CONFLICT SEQADV 9GST TYR F 666 UNP A0A6H1VGP TRP 662 CONFLICT SEQADV 9GST LYS F 667 UNP A0A6H1VGP EXPRESSION TAG SEQADV 9GST ASP F 668 UNP A0A6H1VGP EXPRESSION TAG SEQADV 9GST ASP F 669 UNP A0A6H1VGP EXPRESSION TAG SEQADV 9GST ASP F 670 UNP A0A6H1VGP EXPRESSION TAG SEQADV 9GST ASP F 671 UNP A0A6H1VGP EXPRESSION TAG SEQADV 9GST LYS F 672 UNP A0A6H1VGP EXPRESSION TAG SEQRES 1 A 481 ALA GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO SEQRES 2 A 481 VAL TRP LYS ASP ALA GLU THR THR LEU PHE CYS ALA SER SEQRES 3 A 481 ASP ALA LYS ALA TYR GLU THR GLU LYS HIS ASN VAL TRP SEQRES 4 A 481 ALA THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN SEQRES 5 A 481 GLU ILE HIS LEU GLU ASN VAL THR GLU GLU PHE ASN MET SEQRES 6 A 481 TRP LYS ASN ASN MET VAL GLU GLN MET HIS THR ASP ILE SEQRES 7 A 481 ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS SEQRES 8 A 481 LEU THR PRO LEU CYS VAL THR LEU GLN CYS THR ASN VAL SEQRES 9 A 481 THR ASN ASN ILE THR ASP ASP MET ARG GLY GLU LEU LYS SEQRES 10 A 481 ASN CYS SER PHE ASN MET THR THR GLU LEU ARG ASP LYS SEQRES 11 A 481 LYS GLN LYS VAL TYR SER LEU PHE TYR ARG LEU ASP VAL SEQRES 12 A 481 VAL GLN ILE ASN GLU ASN GLN GLY ASN ARG SER ASN ASN SEQRES 13 A 481 SER ASN LYS GLU TYR ARG LEU ILE ASN CYS ASN THR SER SEQRES 14 A 481 ALA CYS THR GLN ALA CYS PRO LYS VAL SER PHE GLU PRO SEQRES 15 A 481 ILE PRO ILE HIS TYR CYS ALA PRO ALA GLY PHE ALA ILE SEQRES 16 A 481 LEU LYS CYS LYS ASP LYS LYS PHE ASN GLY THR GLY PRO SEQRES 17 A 481 CYS PRO SER VAL SER THR VAL GLN CYS THR HIS GLY ILE SEQRES 18 A 481 LYS PRO VAL VAL SER THR GLN LEU LEU LEU ASN GLY SER SEQRES 19 A 481 LEU ALA GLU GLU GLU VAL MET ILE ARG SER GLU ASN ILE SEQRES 20 A 481 THR ASN ASN ALA LYS ASN ILE LEU VAL GLN PHE ASN THR SEQRES 21 A 481 PRO VAL GLN ILE ASN CYS THR ARG PRO ASN ASN ASN THR SEQRES 22 A 481 ARG LYS SER ILE ARG ILE GLY PRO GLY GLN ALA PHE TYR SEQRES 23 A 481 ALA THR GLY ASP ILE ILE GLY ASP ILE ARG GLN ALA HIS SEQRES 24 A 481 CYS ASN VAL SER LYS ALA THR TRP ASN GLU THR LEU GLY SEQRES 25 A 481 LYS VAL VAL LYS GLN LEU ARG LYS HIS PHE GLY ASN ASN SEQRES 26 A 481 THR ILE ILE ARG PHE ALA ASN SER SER GLY GLY ASP LEU SEQRES 27 A 481 GLU VAL THR THR HIS SER PHE ASN CYS GLY GLY GLU PHE SEQRES 28 A 481 PHE TYR CYS ASN THR SER GLY LEU PHE ASN SER THR TRP SEQRES 29 A 481 ILE SER ASN THR SER VAL GLN GLY SER ASN SER THR GLY SEQRES 30 A 481 SER ASN ASP SER ILE THR LEU PRO CYS ARG ILE LYS GLN SEQRES 31 A 481 ILE ILE ASN MET TRP GLN ARG ILE GLY GLN CYS MET TYR SEQRES 32 A 481 ALA PRO PRO ILE GLN GLY VAL ILE ARG CYS VAL SER ASN SEQRES 33 A 481 ILE THR GLY LEU ILE LEU THR ARG ASP GLY GLY SER THR SEQRES 34 A 481 ASN SER THR THR GLU THR PHE ARG PRO GLY GLY GLY ASP SEQRES 35 A 481 MET ARG ASP ASN TRP ARG SER GLU LEU TYR LYS TYR LYS SEQRES 36 A 481 VAL VAL LYS ILE GLU PRO LEU GLY VAL ALA PRO THR ARG SEQRES 37 A 481 CYS LYS ARG ARG VAL VAL GLY ARG ARG ARG ARG ARG ARG SEQRES 1 B 161 ALA VAL GLY ILE GLY ALA VAL PHE LEU GLY PHE LEU GLY SEQRES 2 B 161 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 B 161 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 B 161 GLN GLN SER ASN LEU LEU ARG ALA PRO GLU ALA GLN GLN SEQRES 5 B 161 HIS LEU LEU LYS LEU THR VAL TRP GLY ILE LYS GLN LEU SEQRES 6 B 161 GLN ALA ARG VAL LEU ALA VAL GLU ARG TYR LEU ARG ASP SEQRES 7 B 161 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 B 161 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 B 161 ASN ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 B 161 LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE SEQRES 11 B 161 ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 B 161 LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP ASP TYR LYS SEQRES 13 B 161 ASP ASP ASP ASP LYS SEQRES 1 C 481 ALA GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO SEQRES 2 C 481 VAL TRP LYS ASP ALA GLU THR THR LEU PHE CYS ALA SER SEQRES 3 C 481 ASP ALA LYS ALA TYR GLU THR GLU LYS HIS ASN VAL TRP SEQRES 4 C 481 ALA THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN SEQRES 5 C 481 GLU ILE HIS LEU GLU ASN VAL THR GLU GLU PHE ASN MET SEQRES 6 C 481 TRP LYS ASN ASN MET VAL GLU GLN MET HIS THR ASP ILE SEQRES 7 C 481 ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS SEQRES 8 C 481 LEU THR PRO LEU CYS VAL THR LEU GLN CYS THR ASN VAL SEQRES 9 C 481 THR ASN ASN ILE THR ASP ASP MET ARG GLY GLU LEU LYS SEQRES 10 C 481 ASN CYS SER PHE ASN MET THR THR GLU LEU ARG ASP LYS SEQRES 11 C 481 LYS GLN LYS VAL TYR SER LEU PHE TYR ARG LEU ASP VAL SEQRES 12 C 481 VAL GLN ILE ASN GLU ASN GLN GLY ASN ARG SER ASN ASN SEQRES 13 C 481 SER ASN LYS GLU TYR ARG LEU ILE ASN CYS ASN THR SER SEQRES 14 C 481 ALA CYS THR GLN ALA CYS PRO LYS VAL SER PHE GLU PRO SEQRES 15 C 481 ILE PRO ILE HIS TYR CYS ALA PRO ALA GLY PHE ALA ILE SEQRES 16 C 481 LEU LYS CYS LYS ASP LYS LYS PHE ASN GLY THR GLY PRO SEQRES 17 C 481 CYS PRO SER VAL SER THR VAL GLN CYS THR HIS GLY ILE SEQRES 18 C 481 LYS PRO VAL VAL SER THR GLN LEU LEU LEU ASN GLY SER SEQRES 19 C 481 LEU ALA GLU GLU GLU VAL MET ILE ARG SER GLU ASN ILE SEQRES 20 C 481 THR ASN ASN ALA LYS ASN ILE LEU VAL GLN PHE ASN THR SEQRES 21 C 481 PRO VAL GLN ILE ASN CYS THR ARG PRO ASN ASN ASN THR SEQRES 22 C 481 ARG LYS SER ILE ARG ILE GLY PRO GLY GLN ALA PHE TYR SEQRES 23 C 481 ALA THR GLY ASP ILE ILE GLY ASP ILE ARG GLN ALA HIS SEQRES 24 C 481 CYS ASN VAL SER LYS ALA THR TRP ASN GLU THR LEU GLY SEQRES 25 C 481 LYS VAL VAL LYS GLN LEU ARG LYS HIS PHE GLY ASN ASN SEQRES 26 C 481 THR ILE ILE ARG PHE ALA ASN SER SER GLY GLY ASP LEU SEQRES 27 C 481 GLU VAL THR THR HIS SER PHE ASN CYS GLY GLY GLU PHE SEQRES 28 C 481 PHE TYR CYS ASN THR SER GLY LEU PHE ASN SER THR TRP SEQRES 29 C 481 ILE SER ASN THR SER VAL GLN GLY SER ASN SER THR GLY SEQRES 30 C 481 SER ASN ASP SER ILE THR LEU PRO CYS ARG ILE LYS GLN SEQRES 31 C 481 ILE ILE ASN MET TRP GLN ARG ILE GLY GLN CYS MET TYR SEQRES 32 C 481 ALA PRO PRO ILE GLN GLY VAL ILE ARG CYS VAL SER ASN SEQRES 33 C 481 ILE THR GLY LEU ILE LEU THR ARG ASP GLY GLY SER THR SEQRES 34 C 481 ASN SER THR THR GLU THR PHE ARG PRO GLY GLY GLY ASP SEQRES 35 C 481 MET ARG ASP ASN TRP ARG SER GLU LEU TYR LYS TYR LYS SEQRES 36 C 481 VAL VAL LYS ILE GLU PRO LEU GLY VAL ALA PRO THR ARG SEQRES 37 C 481 CYS LYS ARG ARG VAL VAL GLY ARG ARG ARG ARG ARG ARG SEQRES 1 D 161 ALA VAL GLY ILE GLY ALA VAL PHE LEU GLY PHE LEU GLY SEQRES 2 D 161 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 D 161 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 D 161 GLN GLN SER ASN LEU LEU ARG ALA PRO GLU ALA GLN GLN SEQRES 5 D 161 HIS LEU LEU LYS LEU THR VAL TRP GLY ILE LYS GLN LEU SEQRES 6 D 161 GLN ALA ARG VAL LEU ALA VAL GLU ARG TYR LEU ARG ASP SEQRES 7 D 161 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 D 161 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 D 161 ASN ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 D 161 LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE SEQRES 11 D 161 ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 D 161 LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP ASP TYR LYS SEQRES 13 D 161 ASP ASP ASP ASP LYS SEQRES 1 E 481 ALA GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO SEQRES 2 E 481 VAL TRP LYS ASP ALA GLU THR THR LEU PHE CYS ALA SER SEQRES 3 E 481 ASP ALA LYS ALA TYR GLU THR GLU LYS HIS ASN VAL TRP SEQRES 4 E 481 ALA THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN SEQRES 5 E 481 GLU ILE HIS LEU GLU ASN VAL THR GLU GLU PHE ASN MET SEQRES 6 E 481 TRP LYS ASN ASN MET VAL GLU GLN MET HIS THR ASP ILE SEQRES 7 E 481 ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS SEQRES 8 E 481 LEU THR PRO LEU CYS VAL THR LEU GLN CYS THR ASN VAL SEQRES 9 E 481 THR ASN ASN ILE THR ASP ASP MET ARG GLY GLU LEU LYS SEQRES 10 E 481 ASN CYS SER PHE ASN MET THR THR GLU LEU ARG ASP LYS SEQRES 11 E 481 LYS GLN LYS VAL TYR SER LEU PHE TYR ARG LEU ASP VAL SEQRES 12 E 481 VAL GLN ILE ASN GLU ASN GLN GLY ASN ARG SER ASN ASN SEQRES 13 E 481 SER ASN LYS GLU TYR ARG LEU ILE ASN CYS ASN THR SER SEQRES 14 E 481 ALA CYS THR GLN ALA CYS PRO LYS VAL SER PHE GLU PRO SEQRES 15 E 481 ILE PRO ILE HIS TYR CYS ALA PRO ALA GLY PHE ALA ILE SEQRES 16 E 481 LEU LYS CYS LYS ASP LYS LYS PHE ASN GLY THR GLY PRO SEQRES 17 E 481 CYS PRO SER VAL SER THR VAL GLN CYS THR HIS GLY ILE SEQRES 18 E 481 LYS PRO VAL VAL SER THR GLN LEU LEU LEU ASN GLY SER SEQRES 19 E 481 LEU ALA GLU GLU GLU VAL MET ILE ARG SER GLU ASN ILE SEQRES 20 E 481 THR ASN ASN ALA LYS ASN ILE LEU VAL GLN PHE ASN THR SEQRES 21 E 481 PRO VAL GLN ILE ASN CYS THR ARG PRO ASN ASN ASN THR SEQRES 22 E 481 ARG LYS SER ILE ARG ILE GLY PRO GLY GLN ALA PHE TYR SEQRES 23 E 481 ALA THR GLY ASP ILE ILE GLY ASP ILE ARG GLN ALA HIS SEQRES 24 E 481 CYS ASN VAL SER LYS ALA THR TRP ASN GLU THR LEU GLY SEQRES 25 E 481 LYS VAL VAL LYS GLN LEU ARG LYS HIS PHE GLY ASN ASN SEQRES 26 E 481 THR ILE ILE ARG PHE ALA ASN SER SER GLY GLY ASP LEU SEQRES 27 E 481 GLU VAL THR THR HIS SER PHE ASN CYS GLY GLY GLU PHE SEQRES 28 E 481 PHE TYR CYS ASN THR SER GLY LEU PHE ASN SER THR TRP SEQRES 29 E 481 ILE SER ASN THR SER VAL GLN GLY SER ASN SER THR GLY SEQRES 30 E 481 SER ASN ASP SER ILE THR LEU PRO CYS ARG ILE LYS GLN SEQRES 31 E 481 ILE ILE ASN MET TRP GLN ARG ILE GLY GLN CYS MET TYR SEQRES 32 E 481 ALA PRO PRO ILE GLN GLY VAL ILE ARG CYS VAL SER ASN SEQRES 33 E 481 ILE THR GLY LEU ILE LEU THR ARG ASP GLY GLY SER THR SEQRES 34 E 481 ASN SER THR THR GLU THR PHE ARG PRO GLY GLY GLY ASP SEQRES 35 E 481 MET ARG ASP ASN TRP ARG SER GLU LEU TYR LYS TYR LYS SEQRES 36 E 481 VAL VAL LYS ILE GLU PRO LEU GLY VAL ALA PRO THR ARG SEQRES 37 E 481 CYS LYS ARG ARG VAL VAL GLY ARG ARG ARG ARG ARG ARG SEQRES 1 F 161 ALA VAL GLY ILE GLY ALA VAL PHE LEU GLY PHE LEU GLY SEQRES 2 F 161 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 F 161 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 F 161 GLN GLN SER ASN LEU LEU ARG ALA PRO GLU ALA GLN GLN SEQRES 5 F 161 HIS LEU LEU LYS LEU THR VAL TRP GLY ILE LYS GLN LEU SEQRES 6 F 161 GLN ALA ARG VAL LEU ALA VAL GLU ARG TYR LEU ARG ASP SEQRES 7 F 161 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 F 161 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 F 161 ASN ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 F 161 LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE SEQRES 11 F 161 ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 F 161 LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP ASP TYR LYS SEQRES 13 F 161 ASP ASP ASP ASP LYS SEQRES 1 H 224 GLN ALA PRO LEU PRO GLU SER GLY PRO GLY VAL VAL ARG SEQRES 2 H 224 PRO THR GLY THR LEU SER LEU THR CYS THR ALA ALA TYR SEQRES 3 H 224 GLY SER ILE SER ARG HIS PHE TRP GLY TRP VAL ARG GLN SEQRES 4 H 224 SER PRO GLN GLY THR LEU GLU TRP ILE ALA HIS MET HIS SEQRES 5 H 224 HIS LEU GLY VAL LYS TYR VAL ASN PRO SER LEU LYS ASN SEQRES 6 H 224 ARG VAL SER ILE SER MET ASP THR SER LYS ASN GLN MET SEQRES 7 H 224 SER LEU THR LEU LYS THR VAL THR ALA THR ASP ALA ALA SEQRES 8 H 224 LYS TYR HIS CYS VAL ARG MET GLY ALA ARG MET SER ASP SEQRES 9 H 224 ILE ALA PHE PHE SER PHE GLY ASP TRP GLY PRO GLY SER SEQRES 10 H 224 LEU VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER SEQRES 11 H 224 VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY SEQRES 12 H 224 GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE SEQRES 13 H 224 PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU SEQRES 14 H 224 THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SEQRES 15 H 224 SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SEQRES 16 H 224 SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL SEQRES 17 H 224 ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS ARG VAL SEQRES 18 H 224 GLU PRO LYS SEQRES 1 L 214 SER TYR VAL LEU GLY GLN SER SER SER MET SER VAL ALA SEQRES 2 L 214 PRO GLY GLN THR ALA LYS ILE SER CYS TRP GLY TYR TYR SEQRES 3 L 214 MET GLY THR LYS PRO VAL ASN TRP TYR GLN LEU LYS PRO SEQRES 4 L 214 GLY ARG ALA PRO SER LEU ILE ILE SER TYR ASP ASP GLU SEQRES 5 L 214 ARG ALA SER GLY THR PRO ALA ARG PHE SER GLY SER HIS SEQRES 6 L 214 SER GLY SER THR ALA THR LEU THR ILE SER ASN VAL VAL SEQRES 7 L 214 PRO ALA ASP GLU ALA ASP TYR PHE CYS GLN VAL TRP ASP SEQRES 8 L 214 SER TYR TYR GLU GLU ILE TYR PHE GLY GLY GLY THR ALA SEQRES 9 L 214 LEU THR VAL LEU GLY GLN PRO LYS ALA ALA PRO SER VAL SEQRES 10 L 214 THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN ALA ASN SEQRES 11 L 214 LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE TYR PRO SEQRES 12 L 214 GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER SER PRO SEQRES 13 L 214 VAL LYS ALA GLY VAL GLU THR THR THR PRO SER LYS GLN SEQRES 14 L 214 SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SER LEU SEQRES 15 L 214 THR PRO GLU GLN TRP LYS SER HIS ARG SER TYR SER CYS SEQRES 16 L 214 GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS THR VAL SEQRES 17 L 214 ALA PRO THR GLU CYS SER HET NAG G 1 14 HET NAG G 2 14 HET NAG I 1 14 HET NAG I 2 14 HET NAG J 1 14 HET NAG J 2 14 HET NAG K 1 14 HET NAG K 2 14 HET NAG M 1 14 HET NAG M 2 14 HET NAG N 1 14 HET NAG N 2 14 HET NAG O 1 14 HET NAG O 2 14 HET NAG P 1 14 HET NAG P 2 14 HET NAG Q 1 14 HET NAG Q 2 14 HET BMA Q 3 11 HET MAN Q 4 11 HET MAN Q 5 11 HET NAG R 1 14 HET NAG R 2 14 HET NAG S 1 14 HET NAG S 2 14 HET NAG T 1 14 HET NAG T 2 14 HET NAG U 1 14 HET NAG U 2 14 HET NAG V 1 14 HET NAG V 2 14 HET NAG W 1 14 HET NAG W 2 14 HET NAG X 1 14 HET NAG X 2 14 HET NAG Y 1 14 HET NAG Y 2 14 HET NAG Z 1 14 HET NAG Z 2 14 HET NAG a 1 14 HET NAG a 2 14 HET BMA a 3 11 HET MAN a 4 11 HET MAN a 5 11 HET NAG b 1 14 HET NAG b 2 14 HET NAG c 1 14 HET NAG c 2 14 HET NAG d 1 14 HET NAG d 2 14 HET NAG e 1 14 HET NAG e 2 14 HET NAG f 1 14 HET NAG f 2 14 HET BMA f 3 11 HET MAN f 4 11 HET NAG g 1 14 HET NAG g 2 14 HET NAG h 1 14 HET NAG h 2 14 HET NAG i 1 14 HET NAG i 2 14 HET NAG j 1 14 HET NAG j 2 14 HET NAG A 601 14 HET NAG A 602 14 HET NAG A 603 14 HET NAG A 604 14 HET NAG A 605 14 HET NAG B 701 14 HET NAG B 702 14 HET NAG B 703 14 HET NAG B 704 14 HET NAG C 601 14 HET NAG C 602 14 HET NAG C 603 14 HET NAG C 604 14 HET NAG C 605 14 HET NAG C 606 14 HET NAG C 607 14 HET NAG D 701 14 HET NAG D 702 14 HET NAG E 601 14 HET NAG E 602 14 HET NAG E 603 14 HET NAG E 604 14 HET NAG E 605 14 HET NAG E 606 14 HET NAG E 607 14 HET NAG E 608 14 HET NAG E 609 14 HET NAG F 701 14 HET NAG F 702 14 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BMA BETA-D-MANNOPYRANOSE HETNAM MAN ALPHA-D-MANNOPYRANOSE HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA- HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO- HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE FORMUL 9 NAG 85(C8 H15 N O6) FORMUL 17 BMA 3(C6 H12 O6) FORMUL 17 MAN 5(C6 H12 O6) HELIX 1 AA1 ASN A 98 LEU A 116 1 19 HELIX 2 AA2 LYS A 335 ARG A 350 1 16 HELIX 3 AA3 LYS A 351 PHE A 353 5 3 HELIX 4 AA4 ASP A 368 THR A 373 1 6 HELIX 5 AA5 ASN A 425 ARG A 429 5 5 HELIX 6 AA6 ARG A 476 SER A 481 1 6 HELIX 7 AA7 PHE B 522 GLY B 527 5 6 HELIX 8 AA8 THR B 529 LEU B 537 1 9 HELIX 9 AA9 VAL B 570 GLY B 597 1 28 HELIX 10 AB1 THR B 627 SER B 636 1 10 HELIX 11 AB2 TYR B 638 SER B 649 1 12 HELIX 12 AB3 ASN B 651 LEU B 660 1 10 HELIX 13 AB4 ASN C 99 SER C 115 1 17 HELIX 14 AB5 LYS C 335 GLY C 354 1 20 HELIX 15 AB6 ASP C 368 THR C 373 1 6 HELIX 16 AB7 MET C 475 SER C 481 1 7 HELIX 17 AB8 LEU D 523 GLY D 527 5 5 HELIX 18 AB9 THR D 529 SER D 534 1 6 HELIX 19 AC1 THR D 536 ASN D 543 1 8 HELIX 20 AC2 THR D 569 TRP D 596 1 28 HELIX 21 AC3 SER D 620 ASN D 625 1 6 HELIX 22 AC4 THR D 627 SER D 636 1 10 HELIX 23 AC5 TYR D 638 TYR D 643 1 6 HELIX 24 AC6 GLY D 644 LEU D 646 5 3 HELIX 25 AC7 GLU D 647 GLN D 652 1 6 HELIX 26 AC8 ASN E 98 SER E 115 1 18 HELIX 27 AC9 ASN E 195 THR E 198 5 4 HELIX 28 AD1 LYS E 335 GLY E 354 1 20 HELIX 29 AD2 ASP E 368 THR E 373 1 6 HELIX 30 AD3 ASN E 425 ARG E 429 5 5 HELIX 31 AD4 MET E 475 SER E 481 1 7 HELIX 32 AD5 ALA F 532 THR F 536 5 5 HELIX 33 AD6 THR F 538 ASN F 543 1 6 HELIX 34 AD7 THR F 569 TRP F 596 1 28 HELIX 35 AD8 SER F 620 ASN F 625 1 6 HELIX 36 AD9 THR F 627 SER F 636 1 10 HELIX 37 AE1 THR F 639 SER F 649 1 11 HELIX 38 AE2 GLN F 650 GLN F 658 1 9 HELIX 39 AE3 PRO H 61 ASN H 65 5 5 HELIX 40 AE4 THR H 86 ALA H 90 5 5 HELIX 41 AE5 VAL L 78 GLU L 82 5 5 SHEET 1 AA1 6 ILE A 84 LEU A 86 0 SHEET 2 AA1 6 VAL A 242 VAL A 245 -1 O THR A 244 N ILE A 84 SHEET 3 AA1 6 PHE A 223 CYS A 228 -1 N ILE A 225 O VAL A 245 SHEET 4 AA1 6 TYR A 486 THR A 499 -1 O LYS A 487 N LEU A 226 SHEET 5 AA1 6 TRP A 35 ASP A 47 -1 N TYR A 39 O GLY A 495 SHEET 6 AA1 6 ILE B 603 PRO B 609 -1 O CYS B 604 N VAL A 38 SHEET 1 AA2 2 GLU A 91 ASN A 94 0 SHEET 2 AA2 2 THR A 236 CYS A 239 -1 O GLY A 237 N PHE A 93 SHEET 1 AA3 5 LYS A 169 TYR A 177 0 SHEET 2 AA3 5 LEU A 154 THR A 162 -1 N CYS A 157 O SER A 174 SHEET 3 AA3 5 LEU A 129 ASN A 133 -1 N GLN A 130 O SER A 158 SHEET 4 AA3 5 GLU A 190 LEU A 193 -1 O TYR A 191 N LEU A 129 SHEET 5 AA3 5 VAL A 181 GLN A 183 -1 N VAL A 182 O ARG A 192 SHEET 1 AA4 3 THR A 202 GLN A 203 0 SHEET 2 AA4 3 MET A 434 TYR A 435 1 O TYR A 435 N THR A 202 SHEET 3 AA4 3 ILE A 423 ILE A 424 -1 N ILE A 424 O MET A 434 SHEET 1 AA5 7 LEU A 259 LEU A 261 0 SHEET 2 AA5 7 ILE A 443 ARG A 456 -1 O THR A 450 N LEU A 260 SHEET 3 AA5 7 ILE A 284 ARG A 298 -1 N VAL A 292 O ILE A 449 SHEET 4 AA5 7 ALA A 329 SER A 334 -1 O HIS A 330 N THR A 297 SHEET 5 AA5 7 SER A 413 LYS A 421 -1 O ILE A 414 N VAL A 333 SHEET 6 AA5 7 GLU A 381 CYS A 385 -1 N TYR A 384 O ARG A 419 SHEET 7 AA5 7 HIS A 374 CYS A 378 -1 N HIS A 374 O CYS A 385 SHEET 1 AA6 6 MET A 271 SER A 274 0 SHEET 2 AA6 6 ILE A 284 ARG A 298 -1 O LEU A 285 N ARG A 273 SHEET 3 AA6 6 ILE A 443 ARG A 456 -1 O ILE A 449 N VAL A 292 SHEET 4 AA6 6 THR A 465 PRO A 470 -1 O ARG A 469 N THR A 455 SHEET 5 AA6 6 ILE A 358 PHE A 361 1 N ARG A 360 O GLU A 466 SHEET 6 AA6 6 SER A 393 TRP A 395 -1 O TRP A 395 N ILE A 359 SHEET 1 AA7 2 ILE A 307 GLY A 312 0 SHEET 2 AA7 2 GLN A 315 PHE A 317 -1 O PHE A 317 N ILE A 307 SHEET 1 AA8 3 LEU C 494 THR C 499 0 SHEET 2 AA8 3 TRP C 35 TYR C 40 -1 N TYR C 39 O GLY C 495 SHEET 3 AA8 3 ILE D 603 PRO D 609 -1 O CYS D 604 N VAL C 38 SHEET 1 AA9 5 TRP C 45 ASP C 47 0 SHEET 2 AA9 5 TYR C 486 ILE C 491 -1 O LYS C 490 N LYS C 46 SHEET 3 AA9 5 PHE C 223 CYS C 228 -1 N LEU C 226 O LYS C 487 SHEET 4 AA9 5 VAL C 242 VAL C 245 -1 O SER C 243 N LYS C 227 SHEET 5 AA9 5 GLU C 83 LEU C 86 -1 N ILE C 84 O THR C 244 SHEET 1 AB1 2 GLU C 91 ASN C 94 0 SHEET 2 AB1 2 THR C 236 CYS C 239 -1 O GLY C 237 N PHE C 93 SHEET 1 AB2 5 LYS C 169 TYR C 177 0 SHEET 2 AB2 5 LEU C 154 THR C 162 -1 N CYS C 157 O SER C 174 SHEET 3 AB2 5 LEU C 129 ASN C 133 -1 N GLN C 130 O SER C 158 SHEET 4 AB2 5 GLU C 190 LEU C 193 -1 O TYR C 191 N LEU C 129 SHEET 5 AB2 5 VAL C 181 GLN C 183 -1 N VAL C 182 O ARG C 192 SHEET 1 AB3 3 THR C 202 GLN C 203 0 SHEET 2 AB3 3 MET C 434 TYR C 435 1 O TYR C 435 N THR C 202 SHEET 3 AB3 3 ILE C 423 ILE C 424 -1 N ILE C 424 O MET C 434 SHEET 1 AB4 6 MET C 271 ARG C 273 0 SHEET 2 AB4 6 ILE C 284 ARG C 298 -1 O LEU C 285 N ARG C 273 SHEET 3 AB4 6 ALA C 329 SER C 334 -1 O HIS C 330 N THR C 297 SHEET 4 AB4 6 SER C 413 LYS C 421 -1 O LEU C 416 N CYS C 331 SHEET 5 AB4 6 GLU C 381 CYS C 385 -1 N TYR C 384 O ARG C 419 SHEET 6 AB4 6 HIS C 374 CYS C 378 -1 N HIS C 374 O CYS C 385 SHEET 1 AB5 6 MET C 271 ARG C 273 0 SHEET 2 AB5 6 ILE C 284 ARG C 298 -1 O LEU C 285 N ARG C 273 SHEET 3 AB5 6 ILE C 443 ARG C 456 -1 O LEU C 452 N VAL C 286 SHEET 4 AB5 6 THR C 465 PRO C 470 -1 O ARG C 469 N THR C 455 SHEET 5 AB5 6 ILE C 358 PHE C 361 1 N ARG C 360 O PHE C 468 SHEET 6 AB5 6 SER C 393 TRP C 395 -1 O SER C 393 N PHE C 361 SHEET 1 AB6 2 ARG C 304 GLY C 312 0 SHEET 2 AB6 2 GLN C 315 THR C 320 -1 O ALA C 319 N LYS C 305 SHEET 1 AB7 5 TRP E 35 ASP E 47 0 SHEET 2 AB7 5 TYR E 486 THR E 499 -1 O LYS E 490 N LYS E 46 SHEET 3 AB7 5 PHE E 223 CYS E 228 -1 N LEU E 226 O LYS E 487 SHEET 4 AB7 5 VAL E 242 VAL E 245 -1 O SER E 243 N LYS E 227 SHEET 5 AB7 5 ILE E 84 LEU E 86 -1 N ILE E 84 O THR E 244 SHEET 1 AB8 3 VAL E 75 PRO E 76 0 SHEET 2 AB8 3 PHE E 53 SER E 56 1 N SER E 56 O VAL E 75 SHEET 3 AB8 3 TYR E 217 CYS E 218 -1 O CYS E 218 N PHE E 53 SHEET 1 AB9 2 GLU E 91 ASN E 94 0 SHEET 2 AB9 2 THR E 236 CYS E 239 -1 O GLY E 237 N PHE E 93 SHEET 1 AC1 5 LYS E 169 TYR E 177 0 SHEET 2 AC1 5 LEU E 154 THR E 162 -1 N CYS E 157 O SER E 174 SHEET 3 AC1 5 LEU E 129 ASN E 133 -1 N GLN E 130 O SER E 158 SHEET 4 AC1 5 GLU E 190 LEU E 193 -1 O TYR E 191 N LEU E 129 SHEET 5 AC1 5 VAL E 181 GLN E 183 -1 N VAL E 182 O ARG E 192 SHEET 1 AC2 3 THR E 202 GLN E 203 0 SHEET 2 AC2 3 MET E 434 TYR E 435 1 O TYR E 435 N THR E 202 SHEET 3 AC2 3 ILE E 423 ILE E 424 -1 N ILE E 424 O MET E 434 SHEET 1 AC3 7 LEU E 259 LEU E 261 0 SHEET 2 AC3 7 ILE E 443 ASP E 457 -1 O THR E 450 N LEU E 260 SHEET 3 AC3 7 VAL E 292 ARG E 298 -1 N VAL E 292 O ILE E 449 SHEET 4 AC3 7 HIS E 330 SER E 334 -1 O ASN E 332 N ASN E 295 SHEET 5 AC3 7 SER E 413 LYS E 421 -1 O LEU E 416 N CYS E 331 SHEET 6 AC3 7 GLU E 381 CYS E 385 -1 N PHE E 382 O LYS E 421 SHEET 7 AC3 7 HIS E 374 CYS E 378 -1 N HIS E 374 O CYS E 385 SHEET 1 AC4 6 MET E 271 SER E 274 0 SHEET 2 AC4 6 ILE E 284 GLN E 287 -1 O LEU E 285 N ARG E 273 SHEET 3 AC4 6 ILE E 443 ASP E 457 -1 O LEU E 452 N VAL E 286 SHEET 4 AC4 6 THR E 465 PRO E 470 -1 O ARG E 469 N THR E 455 SHEET 5 AC4 6 ILE E 358 PHE E 361 1 N ARG E 360 O PHE E 468 SHEET 6 AC4 6 SER E 393 TRP E 395 -1 O TRP E 395 N ILE E 359 SHEET 1 AC5 2 ASN E 302 GLY E 312 0 SHEET 2 AC5 2 GLN E 315 ILE E 322 -1 O PHE E 317 N ILE E 307 SHEET 1 AC6 6 VAL H 11 VAL H 12 0 SHEET 2 AC6 6 SER H 117 VAL H 121 1 O THR H 120 N VAL H 12 SHEET 3 AC6 6 ALA H 91 MET H 102 -1 N TYR H 93 O SER H 117 SHEET 4 AC6 6 TRP H 34 GLN H 39 -1 N VAL H 37 O HIS H 94 SHEET 5 AC6 6 LEU H 45 MET H 51 -1 O GLU H 46 N ARG H 38 SHEET 6 AC6 6 LYS H 57 VAL H 59 -1 O TYR H 58 N HIS H 50 SHEET 1 AC7 4 VAL H 11 VAL H 12 0 SHEET 2 AC7 4 SER H 117 VAL H 121 1 O THR H 120 N VAL H 12 SHEET 3 AC7 4 ALA H 91 MET H 102 -1 N TYR H 93 O SER H 117 SHEET 4 AC7 4 ALA H 106 TRP H 113 -1 O SER H 109 N GLY H 99 SHEET 1 AC8 3 LEU H 18 THR H 23 0 SHEET 2 AC8 3 GLN H 77 LEU H 82 -1 O LEU H 82 N LEU H 18 SHEET 3 AC8 3 VAL H 67 ASP H 72 -1 N ASP H 72 O GLN H 77 SHEET 1 AC9 4 GLY L 5 GLN L 6 0 SHEET 2 AC9 4 ALA L 18 TRP L 23 -1 O TRP L 23 N GLY L 5 SHEET 3 AC9 4 THR L 69 ILE L 74 -1 O LEU L 72 N ILE L 20 SHEET 4 AC9 4 PHE L 61 SER L 66 -1 N SER L 66 O THR L 69 SHEET 1 AD1 6 MET L 10 VAL L 12 0 SHEET 2 AD1 6 THR L 103 VAL L 107 1 O THR L 106 N VAL L 12 SHEET 3 AD1 6 ALA L 83 ASP L 91 -1 N ALA L 83 O LEU L 105 SHEET 4 AD1 6 ASN L 33 LEU L 37 -1 N LEU L 37 O ASP L 84 SHEET 5 AD1 6 SER L 44 SER L 48 -1 O ILE L 46 N TRP L 34 SHEET 6 AD1 6 GLU L 52 ARG L 53 -1 O GLU L 52 N SER L 48 SHEET 1 AD2 4 MET L 10 VAL L 12 0 SHEET 2 AD2 4 THR L 103 VAL L 107 1 O THR L 106 N VAL L 12 SHEET 3 AD2 4 ALA L 83 ASP L 91 -1 N ALA L 83 O LEU L 105 SHEET 4 AD2 4 GLU L 96 PHE L 99 -1 O GLU L 96 N ASP L 91 SSBOND 1 CYS A 54 CYS A 74 1555 1555 2.03 SSBOND 2 CYS A 119 CYS A 205 1555 1555 2.03 SSBOND 3 CYS A 126 CYS A 196 1555 1555 2.03 SSBOND 4 CYS A 131 CYS A 157 1555 1555 2.03 SSBOND 5 CYS A 201 CYS A 433 1555 1555 2.03 SSBOND 6 CYS A 218 CYS A 247 1555 1555 2.03 SSBOND 7 CYS A 228 CYS A 239 1555 1555 2.03 SSBOND 8 CYS A 296 CYS A 331 1555 1555 2.03 SSBOND 9 CYS A 378 CYS A 445 1555 1555 2.03 SSBOND 10 CYS A 385 CYS A 418 1555 1555 2.03 SSBOND 11 CYS A 501 CYS B 605 1555 1555 2.03 SSBOND 12 CYS B 598 CYS B 604 1555 1555 2.03 SSBOND 13 CYS C 54 CYS C 74 1555 1555 2.04 SSBOND 14 CYS C 119 CYS C 205 1555 1555 2.03 SSBOND 15 CYS C 126 CYS C 196 1555 1555 2.03 SSBOND 16 CYS C 131 CYS C 157 1555 1555 2.03 SSBOND 17 CYS C 201 CYS C 433 1555 1555 2.04 SSBOND 18 CYS C 218 CYS C 247 1555 1555 2.04 SSBOND 19 CYS C 228 CYS C 239 1555 1555 2.03 SSBOND 20 CYS C 296 CYS C 331 1555 1555 2.03 SSBOND 21 CYS C 378 CYS C 445 1555 1555 2.03 SSBOND 22 CYS C 385 CYS C 418 1555 1555 2.03 SSBOND 23 CYS C 501 CYS D 605 1555 1555 2.03 SSBOND 24 CYS D 598 CYS D 604 1555 1555 2.02 SSBOND 25 CYS E 54 CYS E 74 1555 1555 2.03 SSBOND 26 CYS E 119 CYS E 205 1555 1555 2.03 SSBOND 27 CYS E 126 CYS E 196 1555 1555 2.03 SSBOND 28 CYS E 131 CYS E 157 1555 1555 2.03 SSBOND 29 CYS E 201 CYS E 433 1555 1555 2.03 SSBOND 30 CYS E 218 CYS E 247 1555 1555 2.03 SSBOND 31 CYS E 228 CYS E 239 1555 1555 2.03 SSBOND 32 CYS E 296 CYS E 331 1555 1555 2.03 SSBOND 33 CYS E 378 CYS E 445 1555 1555 2.03 SSBOND 34 CYS E 385 CYS E 418 1555 1555 2.03 SSBOND 35 CYS E 501 CYS F 605 1555 1555 2.03 SSBOND 36 CYS F 598 CYS F 604 1555 1555 2.03 SSBOND 37 CYS H 22 CYS H 95 1555 1555 2.03 SSBOND 38 CYS L 22 CYS L 87 1555 1555 2.04 LINK ND2 ASN A 88 C1 NAG G 1 1555 1555 1.43 LINK ND2 ASN A 133 C1 NAG A 604 1555 1555 1.44 LINK ND2 ASN A 137 C1 NAG A 605 1555 1555 1.45 LINK ND2 ASN A 156 C1 NAG O 1 1555 1555 1.43 LINK ND2 ASN A 160 C1 NAG P 1 1555 1555 1.44 LINK ND2 ASN A 197 C1 NAG T 1 1555 1555 1.43 LINK ND2 ASN A 234 C1 NAG I 1 1555 1555 1.44 LINK ND2 ASN A 262 C1 NAG Q 1 1555 1555 1.43 LINK ND2 ASN A 276 C1 NAG R 1 1555 1555 1.43 LINK ND2 ASN A 295 C1 NAG J 1 1555 1555 1.44 LINK ND2 ASN A 301 C1 NAG K 1 1555 1555 1.43 LINK ND2 ASN A 332 C1 NAG M 1 1555 1555 1.44 LINK ND2 ASN A 339 C1 NAG A 601 1555 1555 1.44 LINK ND2 ASN A 363 C1 NAG A 602 1555 1555 1.44 LINK ND2 ASN A 386 C1 NAG S 1 1555 1555 1.43 LINK ND2 ASN A 392 C1 NAG A 603 1555 1555 1.44 LINK ND2 ASN A 448 C1 NAG N 1 1555 1555 1.43 LINK ND2 ASN B 611 C1 NAG B 701 1555 1555 1.44 LINK ND2 ASN B 618 C1 NAG B 704 1555 1555 1.43 LINK ND2 ASN B 625 C1 NAG B 703 1555 1555 1.44 LINK ND2 ASN B 637 C1 NAG B 702 1555 1555 1.44 LINK ND2 ASN C 88 C1 NAG C 601 1555 1555 1.45 LINK ND2 ASN C 133 C1 NAG C 603 1555 1555 1.43 LINK ND2 ASN C 156 C1 NAG V 1 1555 1555 1.43 LINK ND2 ASN C 160 C1 NAG W 1 1555 1555 1.43 LINK ND2 ASN C 197 C1 NAG U 1 1555 1555 1.43 LINK ND2 ASN C 234 C1 NAG C 604 1555 1555 1.44 LINK ND2 ASN C 262 C1 NAG a 1 1555 1555 1.44 LINK ND2 ASN C 276 C1 NAG X 1 1555 1555 1.43 LINK ND2 ASN C 295 C1 NAG C 605 1555 1555 1.43 LINK ND2 ASN C 301 C1 NAG b 1 1555 1555 1.44 LINK ND2 ASN C 332 C1 NAG c 1 1555 1555 1.43 LINK ND2 ASN C 339 C1 NAG C 607 1555 1555 1.44 LINK ND2 ASN C 363 C1 NAG C 602 1555 1555 1.43 LINK ND2 ASN C 386 C1 NAG Y 1 1555 1555 1.43 LINK ND2 ASN C 392 C1 NAG C 606 1555 1555 1.44 LINK ND2 ASN C 448 C1 NAG Z 1 1555 1555 1.43 LINK ND2 ASN D 611 C1 NAG D 701 1555 1555 1.45 LINK ND2 ASN D 637 C1 NAG D 702 1555 1555 1.44 LINK ND2 ASN E 88 C1 NAG E 601 1555 1555 1.44 LINK ND2 ASN E 133 C1 NAG E 608 1555 1555 1.44 LINK ND2 ASN E 156 C1 NAG d 1 1555 1555 1.44 LINK ND2 ASN E 160 C1 NAG j 1 1555 1555 1.43 LINK ND2 ASN E 197 C1 NAG E 602 1555 1555 1.44 LINK ND2 ASN E 234 C1 NAG E 603 1555 1555 1.44 LINK ND2 ASN E 262 C1 NAG f 1 1555 1555 1.43 LINK ND2 ASN E 276 C1 NAG g 1 1555 1555 1.44 LINK ND2 ASN E 295 C1 NAG E 609 1555 1555 1.44 LINK ND2 ASN E 301 C1 NAG E 604 1555 1555 1.44 LINK ND2 ASN E 332 C1 NAG h 1 1555 1555 1.44 LINK ND2 ASN E 355 C1 NAG E 605 1555 1555 1.44 LINK ND2 ASN E 363 C1 NAG E 606 1555 1555 1.44 LINK ND2 ASN E 386 C1 NAG i 1 1555 1555 1.43 LINK ND2 ASN E 392 C1 NAG E 607 1555 1555 1.44 LINK ND2 ASN E 448 C1 NAG e 1 1555 1555 1.43 LINK ND2 ASN F 611 C1 NAG F 701 1555 1555 1.44 LINK ND2 ASN F 637 C1 NAG F 702 1555 1555 1.43 LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.43 LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.44 LINK O4 NAG J 1 C1 NAG J 2 1555 1555 1.45 LINK O4 NAG K 1 C1 NAG K 2 1555 1555 1.44 LINK O4 NAG M 1 C1 NAG M 2 1555 1555 1.44 LINK O4 NAG N 1 C1 NAG N 2 1555 1555 1.44 LINK O4 NAG O 1 C1 NAG O 2 1555 1555 1.45 LINK O4 NAG P 1 C1 NAG P 2 1555 1555 1.44 LINK O4 NAG Q 1 C1 NAG Q 2 1555 1555 1.44 LINK O4 NAG Q 2 C1 BMA Q 3 1555 1555 1.44 LINK O3 BMA Q 3 C1 MAN Q 4 1555 1555 1.44 LINK O2 MAN Q 4 C1 MAN Q 5 1555 1555 1.45 LINK O4 NAG R 1 C1 NAG R 2 1555 1555 1.44 LINK O4 NAG S 1 C1 NAG S 2 1555 1555 1.44 LINK O4 NAG T 1 C1 NAG T 2 1555 1555 1.43 LINK O4 NAG U 1 C1 NAG U 2 1555 1555 1.45 LINK O4 NAG V 1 C1 NAG V 2 1555 1555 1.44 LINK O4 NAG W 1 C1 NAG W 2 1555 1555 1.44 LINK O4 NAG X 1 C1 NAG X 2 1555 1555 1.44 LINK O4 NAG Y 1 C1 NAG Y 2 1555 1555 1.44 LINK O4 NAG Z 1 C1 NAG Z 2 1555 1555 1.44 LINK O4 NAG a 1 C1 NAG a 2 1555 1555 1.44 LINK O4 NAG a 2 C1 BMA a 3 1555 1555 1.44 LINK O3 BMA a 3 C1 MAN a 4 1555 1555 1.44 LINK O6 BMA a 3 C1 MAN a 5 1555 1555 1.44 LINK O4 NAG b 1 C1 NAG b 2 1555 1555 1.44 LINK O4 NAG c 1 C1 NAG c 2 1555 1555 1.44 LINK O4 NAG d 1 C1 NAG d 2 1555 1555 1.44 LINK O4 NAG e 1 C1 NAG e 2 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 1.44 LINK O3 BMA f 3 C1 MAN f 4 1555 1555 1.45 LINK O4 NAG g 1 C1 NAG g 2 1555 1555 1.45 LINK O4 NAG h 1 C1 NAG h 2 1555 1555 1.44 LINK O4 NAG i 1 C1 NAG i 2 1555 1555 1.44 LINK O4 NAG j 1 C1 NAG j 2 1555 1555 1.44 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