HEADER VIRAL PROTEIN/IMMUNE SYSTEM 16-OCT-23 8ULR TITLE CRYO-EM STRUCTURE OF THE BG505 SOSIPV2 IN COMPLEX WITH BNAB 05_B08 TITLE 2 FABS 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: BG505 DS-SOSIP GLYCOPROTEIN GP41; COMPND 8 CHAIN: B, D, F; COMPND 9 ENGINEERED: YES; COMPND 10 MOL_ID: 3; COMPND 11 MOLECULE: 05_B08 FAB HEAVY CHAIN; COMPND 12 CHAIN: H, I, J; COMPND 13 ENGINEERED: YES; COMPND 14 MOL_ID: 4; COMPND 15 MOLECULE: 05_B08 LIGHT CHAIN; COMPND 16 CHAIN: L, M, N; COMPND 17 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 EXPRESSION_SYSTEM_CELL: HEK293; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 10 ORGANISM_TAXID: 11676; SOURCE 11 GENE: ENV; SOURCE 12 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 13 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 14 EXPRESSION_SYSTEM_CELL: HEK293; SOURCE 15 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 17 ORGANISM_TAXID: 9606; SOURCE 18 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 19 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 20 EXPRESSION_SYSTEM_CELL: HEK293; SOURCE 21 MOL_ID: 4; SOURCE 22 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 23 ORGANISM_TAXID: 9606; SOURCE 24 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 25 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 26 EXPRESSION_SYSTEM_CELL: HEK293 KEYWDS HIV-1, ANTIBODY, CD4-BINDING SITE, IMMUNE COMPLEX, VIRAL PROTEIN- KEYWDS 2 IMMUNE SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR A.T.DELAITSCH,P.J.BJORKMAN REVDAT 1 16-APR-25 8ULR 0 JRNL AUTH A.T.DELAITSCH,P.J.BJORKMAN JRNL TITL CRYO-EM STRUCTURE OF THE BG505 SOSIPV2 IN COMPLEX WITH BNAB JRNL TITL 2 05_B08 FABS JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.30 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : TOPAZ, SERIALEM, CRYOSPARC, UCSF REMARK 3 CHIMERAX, CRYOSPARC, CRYOSPARC, REMARK 3 CRYOSPARC, PHENIX REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : 6UDJ REMARK 3 REFINEMENT SPACE : REAL REMARK 3 REFINEMENT PROTOCOL : RIGID BODY FIT REMARK 3 REFINEMENT TARGET : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL REMARK 3 REMARK 3 FITTING PROCEDURE : NULL REMARK 3 REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 3.300 REMARK 3 NUMBER OF PARTICLES : 129686 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 8ULR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-OCT-23. REMARK 100 THE DEPOSITION ID IS D_1000277632. 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 : ANTIBODY-ANTIGEN COMPLEX OF HIV REMARK 245 -1 BG505 SOSIPV2 TRIMER WITH 05_ REMARK 245 B08 FABS REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 4.40 REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : 3S BLOT, 0 BLOT FORCE REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 8.00 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : 3667 REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 (6K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1000.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 3000.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : NULL REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 6000.00 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : 105000 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: DODECAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, H, I, J, L, REMARK 350 AND CHAINS: M, N, G, K, 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, k, l, REMARK 350 AND CHAINS: m, n 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 58 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 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 399 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 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 LEU B 520 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 ALA B 662 REMARK 465 LEU B 663 REMARK 465 ASP B 664 REMARK 465 ALA C 58 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 GLU C 185A REMARK 465 ASN C 185B REMARK 465 GLN C 185C REMARK 465 GLY C 185D REMARK 465 ASN C 185E REMARK 465 ARG C 185F REMARK 465 SER C 185G REMARK 465 ASN C 185H REMARK 465 ASN C 185I REMARK 465 SER C 185J 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 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 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 ALA D 662 REMARK 465 LEU D 663 REMARK 465 ASP D 664 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 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 399 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 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 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 ALA F 662 REMARK 465 LEU F 663 REMARK 465 ASP F 664 REMARK 465 GLN H 1 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 ARG H 210 REMARK 465 VAL H 211 REMARK 465 GLU H 212 REMARK 465 PRO H 213 REMARK 465 LYS 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 HIS H 221 REMARK 465 HIS H 222 REMARK 465 HIS H 223 REMARK 465 HIS H 224 REMARK 465 HIS H 225 REMARK 465 GLN I 1 REMARK 465 ALA I 114 REMARK 465 SER I 115 REMARK 465 THR I 116 REMARK 465 LYS I 117 REMARK 465 GLY I 118 REMARK 465 PRO I 119 REMARK 465 SER I 120 REMARK 465 VAL I 121 REMARK 465 PHE I 122 REMARK 465 PRO I 123 REMARK 465 LEU I 124 REMARK 465 ALA I 125 REMARK 465 PRO I 126 REMARK 465 SER I 127 REMARK 465 SER I 128 REMARK 465 LYS I 129 REMARK 465 SER I 130 REMARK 465 THR I 131 REMARK 465 SER I 132 REMARK 465 GLY I 133 REMARK 465 GLY I 134 REMARK 465 THR I 135 REMARK 465 ALA I 136 REMARK 465 ALA I 137 REMARK 465 LEU I 138 REMARK 465 GLY I 139 REMARK 465 CYS I 140 REMARK 465 LEU I 141 REMARK 465 VAL I 142 REMARK 465 LYS I 143 REMARK 465 ASP I 144 REMARK 465 TYR I 145 REMARK 465 PHE I 146 REMARK 465 PRO I 147 REMARK 465 GLU I 148 REMARK 465 PRO I 149 REMARK 465 VAL I 150 REMARK 465 THR I 151 REMARK 465 VAL I 152 REMARK 465 SER I 153 REMARK 465 TRP I 154 REMARK 465 ASN I 155 REMARK 465 SER I 156 REMARK 465 GLY I 157 REMARK 465 ALA I 158 REMARK 465 LEU I 159 REMARK 465 THR I 160 REMARK 465 SER I 161 REMARK 465 GLY I 162 REMARK 465 VAL I 163 REMARK 465 HIS I 164 REMARK 465 THR I 165 REMARK 465 PHE I 166 REMARK 465 PRO I 167 REMARK 465 ALA I 168 REMARK 465 VAL I 169 REMARK 465 LEU I 170 REMARK 465 GLN I 171 REMARK 465 SER I 172 REMARK 465 SER I 173 REMARK 465 GLY I 174 REMARK 465 LEU I 175 REMARK 465 TYR I 176 REMARK 465 SER I 177 REMARK 465 LEU I 178 REMARK 465 SER I 179 REMARK 465 SER I 180 REMARK 465 VAL I 181 REMARK 465 VAL I 182 REMARK 465 THR I 183 REMARK 465 VAL I 184 REMARK 465 PRO I 185 REMARK 465 SER I 186 REMARK 465 SER I 187 REMARK 465 SER I 188 REMARK 465 LEU I 189 REMARK 465 GLY I 190 REMARK 465 THR I 191 REMARK 465 GLN I 192 REMARK 465 THR I 193 REMARK 465 TYR I 194 REMARK 465 ILE I 195 REMARK 465 CYS I 196 REMARK 465 ASN I 197 REMARK 465 VAL I 198 REMARK 465 ASN I 199 REMARK 465 HIS I 200 REMARK 465 LYS I 201 REMARK 465 PRO I 202 REMARK 465 SER I 203 REMARK 465 ASN I 204 REMARK 465 THR I 205 REMARK 465 LYS I 206 REMARK 465 VAL I 207 REMARK 465 ASP I 208 REMARK 465 LYS I 209 REMARK 465 ARG I 210 REMARK 465 VAL I 211 REMARK 465 GLU I 212 REMARK 465 PRO I 213 REMARK 465 LYS I 214 REMARK 465 SER I 215 REMARK 465 CYS I 216 REMARK 465 ASP I 217 REMARK 465 LYS I 218 REMARK 465 THR I 219 REMARK 465 HIS I 220 REMARK 465 HIS I 221 REMARK 465 HIS I 222 REMARK 465 HIS I 223 REMARK 465 HIS I 224 REMARK 465 HIS I 225 REMARK 465 GLN J 1 REMARK 465 ALA J 114 REMARK 465 SER J 115 REMARK 465 THR J 116 REMARK 465 LYS J 117 REMARK 465 GLY J 118 REMARK 465 PRO J 119 REMARK 465 SER J 120 REMARK 465 VAL J 121 REMARK 465 PHE J 122 REMARK 465 PRO J 123 REMARK 465 LEU J 124 REMARK 465 ALA J 125 REMARK 465 PRO J 126 REMARK 465 SER J 127 REMARK 465 SER J 128 REMARK 465 LYS J 129 REMARK 465 SER J 130 REMARK 465 THR J 131 REMARK 465 SER J 132 REMARK 465 GLY J 133 REMARK 465 GLY J 134 REMARK 465 THR J 135 REMARK 465 ALA J 136 REMARK 465 ALA J 137 REMARK 465 LEU J 138 REMARK 465 GLY J 139 REMARK 465 CYS J 140 REMARK 465 LEU J 141 REMARK 465 VAL J 142 REMARK 465 LYS J 143 REMARK 465 ASP J 144 REMARK 465 TYR J 145 REMARK 465 PHE J 146 REMARK 465 PRO J 147 REMARK 465 GLU J 148 REMARK 465 PRO J 149 REMARK 465 VAL J 150 REMARK 465 THR J 151 REMARK 465 VAL J 152 REMARK 465 SER J 153 REMARK 465 TRP J 154 REMARK 465 ASN J 155 REMARK 465 SER J 156 REMARK 465 GLY J 157 REMARK 465 ALA J 158 REMARK 465 LEU J 159 REMARK 465 THR J 160 REMARK 465 SER J 161 REMARK 465 GLY J 162 REMARK 465 VAL J 163 REMARK 465 HIS J 164 REMARK 465 THR J 165 REMARK 465 PHE J 166 REMARK 465 PRO J 167 REMARK 465 ALA J 168 REMARK 465 VAL J 169 REMARK 465 LEU J 170 REMARK 465 GLN J 171 REMARK 465 SER J 172 REMARK 465 SER J 173 REMARK 465 GLY J 174 REMARK 465 LEU J 175 REMARK 465 TYR J 176 REMARK 465 SER J 177 REMARK 465 LEU J 178 REMARK 465 SER J 179 REMARK 465 SER J 180 REMARK 465 VAL J 181 REMARK 465 VAL J 182 REMARK 465 THR J 183 REMARK 465 VAL J 184 REMARK 465 PRO J 185 REMARK 465 SER J 186 REMARK 465 SER J 187 REMARK 465 SER J 188 REMARK 465 LEU J 189 REMARK 465 GLY J 190 REMARK 465 THR J 191 REMARK 465 GLN J 192 REMARK 465 THR J 193 REMARK 465 TYR J 194 REMARK 465 ILE J 195 REMARK 465 CYS J 196 REMARK 465 ASN J 197 REMARK 465 VAL J 198 REMARK 465 ASN J 199 REMARK 465 HIS J 200 REMARK 465 LYS J 201 REMARK 465 PRO J 202 REMARK 465 SER J 203 REMARK 465 ASN J 204 REMARK 465 THR J 205 REMARK 465 LYS J 206 REMARK 465 VAL J 207 REMARK 465 ASP J 208 REMARK 465 LYS J 209 REMARK 465 ARG J 210 REMARK 465 VAL J 211 REMARK 465 GLU J 212 REMARK 465 PRO J 213 REMARK 465 LYS J 214 REMARK 465 SER J 215 REMARK 465 CYS J 216 REMARK 465 ASP J 217 REMARK 465 LYS J 218 REMARK 465 THR J 219 REMARK 465 HIS J 220 REMARK 465 HIS J 221 REMARK 465 HIS J 222 REMARK 465 HIS J 223 REMARK 465 HIS J 224 REMARK 465 HIS J 225 REMARK 465 ASP L 1 REMARK 465 SER L 2 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 465 ASP M 1 REMARK 465 SER M 2 REMARK 465 ARG M 108 REMARK 465 THR M 109 REMARK 465 VAL M 110 REMARK 465 ALA M 111 REMARK 465 ALA M 112 REMARK 465 PRO M 113 REMARK 465 SER M 114 REMARK 465 VAL M 115 REMARK 465 PHE M 116 REMARK 465 ILE M 117 REMARK 465 PHE M 118 REMARK 465 PRO M 119 REMARK 465 PRO M 120 REMARK 465 SER M 121 REMARK 465 ASP M 122 REMARK 465 GLU M 123 REMARK 465 GLN M 124 REMARK 465 LEU M 125 REMARK 465 LYS M 126 REMARK 465 SER M 127 REMARK 465 GLY M 128 REMARK 465 THR M 129 REMARK 465 ALA M 130 REMARK 465 SER M 131 REMARK 465 VAL M 132 REMARK 465 VAL M 133 REMARK 465 CYS M 134 REMARK 465 LEU M 135 REMARK 465 LEU M 136 REMARK 465 ASN M 137 REMARK 465 ASN M 138 REMARK 465 PHE M 139 REMARK 465 TYR M 140 REMARK 465 PRO M 141 REMARK 465 ARG M 142 REMARK 465 GLU M 143 REMARK 465 ALA M 144 REMARK 465 LYS M 145 REMARK 465 VAL M 146 REMARK 465 GLN M 147 REMARK 465 TRP M 148 REMARK 465 LYS M 149 REMARK 465 VAL M 150 REMARK 465 ASP M 151 REMARK 465 ASN M 152 REMARK 465 ALA M 153 REMARK 465 LEU M 154 REMARK 465 GLN M 155 REMARK 465 SER M 156 REMARK 465 GLY M 157 REMARK 465 ASN M 158 REMARK 465 SER M 159 REMARK 465 GLN M 160 REMARK 465 GLU M 161 REMARK 465 SER M 162 REMARK 465 VAL M 163 REMARK 465 THR M 164 REMARK 465 GLU M 165 REMARK 465 GLN M 166 REMARK 465 ASP M 167 REMARK 465 SER M 168 REMARK 465 LYS M 169 REMARK 465 ASP M 170 REMARK 465 SER M 171 REMARK 465 THR M 172 REMARK 465 TYR M 173 REMARK 465 SER M 174 REMARK 465 LEU M 175 REMARK 465 SER M 176 REMARK 465 SER M 177 REMARK 465 THR M 178 REMARK 465 LEU M 179 REMARK 465 THR M 180 REMARK 465 LEU M 181 REMARK 465 SER M 182 REMARK 465 LYS M 183 REMARK 465 ALA M 184 REMARK 465 ASP M 185 REMARK 465 TYR M 186 REMARK 465 GLU M 187 REMARK 465 LYS M 188 REMARK 465 HIS M 189 REMARK 465 LYS M 190 REMARK 465 VAL M 191 REMARK 465 TYR M 192 REMARK 465 ALA M 193 REMARK 465 CYS M 194 REMARK 465 GLU M 195 REMARK 465 VAL M 196 REMARK 465 THR M 197 REMARK 465 HIS M 198 REMARK 465 GLN M 199 REMARK 465 GLY M 200 REMARK 465 LEU M 201 REMARK 465 SER M 202 REMARK 465 SER M 203 REMARK 465 PRO M 204 REMARK 465 VAL M 205 REMARK 465 THR M 206 REMARK 465 LYS M 207 REMARK 465 SER M 208 REMARK 465 PHE M 209 REMARK 465 ASN M 210 REMARK 465 ARG M 211 REMARK 465 GLY M 212 REMARK 465 GLU M 213 REMARK 465 CYS M 214 REMARK 465 ASP N 1 REMARK 465 SER N 2 REMARK 465 ARG N 108 REMARK 465 THR N 109 REMARK 465 VAL N 110 REMARK 465 ALA N 111 REMARK 465 ALA N 112 REMARK 465 PRO N 113 REMARK 465 SER N 114 REMARK 465 VAL N 115 REMARK 465 PHE N 116 REMARK 465 ILE N 117 REMARK 465 PHE N 118 REMARK 465 PRO N 119 REMARK 465 PRO N 120 REMARK 465 SER N 121 REMARK 465 ASP N 122 REMARK 465 GLU N 123 REMARK 465 GLN N 124 REMARK 465 LEU N 125 REMARK 465 LYS N 126 REMARK 465 SER N 127 REMARK 465 GLY N 128 REMARK 465 THR N 129 REMARK 465 ALA N 130 REMARK 465 SER N 131 REMARK 465 VAL N 132 REMARK 465 VAL N 133 REMARK 465 CYS N 134 REMARK 465 LEU N 135 REMARK 465 LEU N 136 REMARK 465 ASN N 137 REMARK 465 ASN N 138 REMARK 465 PHE N 139 REMARK 465 TYR N 140 REMARK 465 PRO N 141 REMARK 465 ARG N 142 REMARK 465 GLU N 143 REMARK 465 ALA N 144 REMARK 465 LYS N 145 REMARK 465 VAL N 146 REMARK 465 GLN N 147 REMARK 465 TRP N 148 REMARK 465 LYS N 149 REMARK 465 VAL N 150 REMARK 465 ASP N 151 REMARK 465 ASN N 152 REMARK 465 ALA N 153 REMARK 465 LEU N 154 REMARK 465 GLN N 155 REMARK 465 SER N 156 REMARK 465 GLY N 157 REMARK 465 ASN N 158 REMARK 465 SER N 159 REMARK 465 GLN N 160 REMARK 465 GLU N 161 REMARK 465 SER N 162 REMARK 465 VAL N 163 REMARK 465 THR N 164 REMARK 465 GLU N 165 REMARK 465 GLN N 166 REMARK 465 ASP N 167 REMARK 465 SER N 168 REMARK 465 LYS N 169 REMARK 465 ASP N 170 REMARK 465 SER N 171 REMARK 465 THR N 172 REMARK 465 TYR N 173 REMARK 465 SER N 174 REMARK 465 LEU N 175 REMARK 465 SER N 176 REMARK 465 SER N 177 REMARK 465 THR N 178 REMARK 465 LEU N 179 REMARK 465 THR N 180 REMARK 465 LEU N 181 REMARK 465 SER N 182 REMARK 465 LYS N 183 REMARK 465 ALA N 184 REMARK 465 ASP N 185 REMARK 465 TYR N 186 REMARK 465 GLU N 187 REMARK 465 LYS N 188 REMARK 465 HIS N 189 REMARK 465 LYS N 190 REMARK 465 VAL N 191 REMARK 465 TYR N 192 REMARK 465 ALA N 193 REMARK 465 CYS N 194 REMARK 465 GLU N 195 REMARK 465 VAL N 196 REMARK 465 THR N 197 REMARK 465 HIS N 198 REMARK 465 GLN N 199 REMARK 465 GLY N 200 REMARK 465 LEU N 201 REMARK 465 SER N 202 REMARK 465 SER N 203 REMARK 465 PRO N 204 REMARK 465 VAL N 205 REMARK 465 THR N 206 REMARK 465 LYS N 207 REMARK 465 SER N 208 REMARK 465 PHE N 209 REMARK 465 ASN N 210 REMARK 465 ARG N 211 REMARK 465 GLY N 212 REMARK 465 GLU N 213 REMARK 465 CYS N 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 ASP A 148 CG OD1 OD2 REMARK 470 ASP A 149 CG OD1 OD2 REMARK 470 GLU A 268 CG CD OE1 OE2 REMARK 470 ASP C 148 CG OD1 OD2 REMARK 470 ASP C 149 CG OD1 OD2 REMARK 470 GLU C 268 CG CD OE1 OE2 REMARK 470 ASP E 148 CG OD1 OD2 REMARK 470 ASP E 149 CG OD1 OD2 REMARK 470 GLU E 268 CG CD OE1 OE2 REMARK 470 TRP H 105 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP H 105 CZ3 CH2 REMARK 470 TRP I 105 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP I 105 CZ3 CH2 REMARK 470 TRP J 105 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP J 105 CZ3 CH2 REMARK 470 ARG L 18 CG CD NE CZ NH1 NH2 REMARK 470 ARG L 24 CG CD NE CZ NH1 NH2 REMARK 470 ARG L 63 CG CD NE CZ NH1 NH2 REMARK 470 ARG M 18 CG CD NE CZ NH1 NH2 REMARK 470 ARG M 24 CG CD NE CZ NH1 NH2 REMARK 470 ARG M 63 CG CD NE CZ NH1 NH2 REMARK 470 ARG N 18 CG CD NE CZ NH1 NH2 REMARK 470 ARG N 24 CG CD NE CZ NH1 NH2 REMARK 470 ARG N 63 CG CD NE CZ NH1 NH2 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 GLN I 6 OG1 THR I 107 2.14 REMARK 500 O TYR J 100A ND2 ASN N 34 2.19 REMARK 500 NE2 GLN N 89 O TYR N 91 2.19 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 205 CA - CB - SG ANGL. DEV. = 9.3 DEGREES REMARK 500 PRO M 59 CA - N - CD ANGL. DEV. = -8.4 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 PRO A 118 34.99 -86.30 REMARK 500 GLN A 170 114.86 -160.42 REMARK 500 THR A 387 53.52 -90.67 REMARK 500 PHE A 391 76.01 -100.83 REMARK 500 ASN A 392 44.21 -141.06 REMARK 500 GLN A 428 41.98 39.36 REMARK 500 MET B 626 147.77 -172.73 REMARK 500 LEU C 122 32.52 -97.86 REMARK 500 ASN C 137 60.03 60.14 REMARK 500 GLN C 170 114.89 -160.42 REMARK 500 HIS C 249 50.92 -91.67 REMARK 500 PHE C 391 76.35 -100.79 REMARK 500 ASN C 392 44.28 -141.15 REMARK 500 GLN C 428 40.98 39.58 REMARK 500 ARG C 500 35.98 -97.85 REMARK 500 MET D 626 147.92 -174.45 REMARK 500 PRO E 118 34.17 -86.52 REMARK 500 LEU E 122 32.52 -99.48 REMARK 500 GLN E 170 115.63 -160.06 REMARK 500 ASN E 195 61.71 -100.53 REMARK 500 THR E 387 55.46 -90.07 REMARK 500 PHE E 391 76.03 -100.56 REMARK 500 ASN E 392 44.23 -141.18 REMARK 500 ARG E 500 35.01 -96.61 REMARK 500 MET F 626 147.32 -172.20 REMARK 500 PHE H 29 46.06 -83.10 REMARK 500 PHE I 29 47.20 -81.82 REMARK 500 PHE J 29 46.62 -83.33 REMARK 500 ALA L 30 -133.60 55.47 REMARK 500 THR L 51 -7.11 65.88 REMARK 500 SER L 76 -102.45 56.45 REMARK 500 ALA L 84 -174.27 -172.38 REMARK 500 TYR L 91 -122.91 57.75 REMARK 500 ALA M 30 -134.00 55.67 REMARK 500 THR M 51 -7.75 70.05 REMARK 500 SER M 76 -102.25 56.93 REMARK 500 ALA M 84 -172.09 -170.86 REMARK 500 TYR M 91 -120.24 58.33 REMARK 500 ALA N 30 -133.41 55.57 REMARK 500 THR N 51 -7.64 69.93 REMARK 500 SER N 76 -102.65 56.30 REMARK 500 ALA N 84 -172.08 -170.33 REMARK 500 TYR N 91 -121.79 61.12 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 CYS C 119 VAL C 120 -148.86 REMARK 500 CYS C 205 PRO C 206 -145.15 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-42363 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF THE BG505 SOSIPV2 IN COMPLEX WITH BNAB 05_B08 REMARK 900 FABS DBREF 8ULR A 33 504 UNP Q2N0S6 Q2N0S6_9HIV1 32 501 DBREF 8ULR B 512 664 UNP Q2N0S5 Q2N0S5_9HIV1 509 661 DBREF 8ULR C 33 504 UNP Q2N0S6 Q2N0S6_9HIV1 32 501 DBREF 8ULR D 512 664 UNP Q2N0S5 Q2N0S5_9HIV1 509 661 DBREF 8ULR E 33 504 UNP Q2N0S6 Q2N0S6_9HIV1 32 501 DBREF 8ULR F 512 664 UNP Q2N0S5 Q2N0S5_9HIV1 509 661 DBREF 8ULR H 1 225 PDB 8ULR 8ULR 1 225 DBREF 8ULR I 1 225 PDB 8ULR 8ULR 1 225 DBREF 8ULR J 1 225 PDB 8ULR 8ULR 1 225 DBREF 8ULR L 1 214 PDB 8ULR 8ULR 1 214 DBREF 8ULR M 1 214 PDB 8ULR 8ULR 1 214 DBREF 8ULR N 1 214 PDB 8ULR 8ULR 1 214 SEQADV 8ULR ASN A 332 UNP Q2N0S6 THR 330 CONFLICT SEQADV 8ULR CYS A 501 UNP Q2N0S6 ALA 498 CONFLICT SEQADV 8ULR VAL A 505 UNP Q2N0S6 EXPRESSION TAG SEQADV 8ULR VAL A 506 UNP Q2N0S6 EXPRESSION TAG SEQADV 8ULR GLY A 507 UNP Q2N0S6 EXPRESSION TAG SEQADV 8ULR ARG A 508 UNP Q2N0S6 EXPRESSION TAG SEQADV 8ULR ARG A 509 UNP Q2N0S6 EXPRESSION TAG SEQADV 8ULR ARG A 510 UNP Q2N0S6 EXPRESSION TAG SEQADV 8ULR ARG A 511 UNP Q2N0S6 EXPRESSION TAG SEQADV 8ULR ARG A 512 UNP Q2N0S6 EXPRESSION TAG SEQADV 8ULR ARG A 513 UNP Q2N0S6 EXPRESSION TAG SEQADV 8ULR PRO B 559 UNP Q2N0S5 ILE 556 ENGINEERED MUTATION SEQADV 8ULR CYS B 605 UNP Q2N0S5 THR 602 ENGINEERED MUTATION SEQADV 8ULR ASN C 332 UNP Q2N0S6 THR 330 CONFLICT SEQADV 8ULR CYS C 501 UNP Q2N0S6 ALA 498 CONFLICT SEQADV 8ULR VAL C 505 UNP Q2N0S6 EXPRESSION TAG SEQADV 8ULR VAL C 506 UNP Q2N0S6 EXPRESSION TAG SEQADV 8ULR GLY C 507 UNP Q2N0S6 EXPRESSION TAG SEQADV 8ULR ARG C 508 UNP Q2N0S6 EXPRESSION TAG SEQADV 8ULR ARG C 509 UNP Q2N0S6 EXPRESSION TAG SEQADV 8ULR ARG C 510 UNP Q2N0S6 EXPRESSION TAG SEQADV 8ULR ARG C 511 UNP Q2N0S6 EXPRESSION TAG SEQADV 8ULR ARG C 512 UNP Q2N0S6 EXPRESSION TAG SEQADV 8ULR ARG C 513 UNP Q2N0S6 EXPRESSION TAG SEQADV 8ULR PRO D 559 UNP Q2N0S5 ILE 556 ENGINEERED MUTATION SEQADV 8ULR CYS D 605 UNP Q2N0S5 THR 602 ENGINEERED MUTATION SEQADV 8ULR ASN E 332 UNP Q2N0S6 THR 330 CONFLICT SEQADV 8ULR CYS E 501 UNP Q2N0S6 ALA 498 CONFLICT SEQADV 8ULR VAL E 505 UNP Q2N0S6 EXPRESSION TAG SEQADV 8ULR VAL E 506 UNP Q2N0S6 EXPRESSION TAG SEQADV 8ULR GLY E 507 UNP Q2N0S6 EXPRESSION TAG SEQADV 8ULR ARG E 508 UNP Q2N0S6 EXPRESSION TAG SEQADV 8ULR ARG E 509 UNP Q2N0S6 EXPRESSION TAG SEQADV 8ULR ARG E 510 UNP Q2N0S6 EXPRESSION TAG SEQADV 8ULR ARG E 511 UNP Q2N0S6 EXPRESSION TAG SEQADV 8ULR ARG E 512 UNP Q2N0S6 EXPRESSION TAG SEQADV 8ULR ARG E 513 UNP Q2N0S6 EXPRESSION TAG SEQADV 8ULR PRO F 559 UNP Q2N0S5 ILE 556 ENGINEERED MUTATION SEQADV 8ULR CYS F 605 UNP Q2N0S5 THR 602 ENGINEERED MUTATION SEQRES 1 A 479 ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO VAL TRP SEQRES 2 A 479 LYS ASP ALA GLU THR THR LEU PHE CYS ALA SER ASP ALA SEQRES 3 A 479 LYS ALA TYR GLU THR GLU LYS HIS ASN VAL TRP ALA THR SEQRES 4 A 479 HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN GLU ILE SEQRES 5 A 479 HIS LEU GLU ASN VAL THR GLU GLU PHE ASN MET TRP LYS SEQRES 6 A 479 ASN ASN MET VAL GLU GLN MET HIS THR ASP ILE ILE SER SEQRES 7 A 479 LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS LEU THR SEQRES 8 A 479 PRO LEU CYS VAL THR LEU GLN CYS THR ASN VAL THR ASN SEQRES 9 A 479 ASN ILE THR ASP ASP MET ARG GLY GLU LEU LYS ASN CYS SEQRES 10 A 479 SER PHE ASN MET THR THR GLU LEU ARG ASP LYS LYS GLN SEQRES 11 A 479 LYS VAL TYR SER LEU PHE TYR ARG LEU ASP VAL VAL GLN SEQRES 12 A 479 ILE ASN GLU ASN GLN GLY ASN ARG SER ASN ASN SER ASN SEQRES 13 A 479 LYS GLU TYR ARG LEU ILE ASN CYS ASN THR SER ALA ILE SEQRES 14 A 479 THR GLN ALA CYS PRO LYS VAL SER PHE GLU PRO ILE PRO SEQRES 15 A 479 ILE HIS TYR CYS ALA PRO ALA GLY PHE ALA ILE LEU LYS SEQRES 16 A 479 CYS LYS ASP LYS LYS PHE ASN GLY THR GLY PRO CYS PRO SEQRES 17 A 479 SER VAL SER THR VAL GLN CYS THR HIS GLY ILE LYS PRO SEQRES 18 A 479 VAL VAL SER THR GLN LEU LEU LEU ASN GLY SER LEU ALA SEQRES 19 A 479 GLU GLU GLU VAL MET ILE ARG SER GLU ASN ILE THR ASN SEQRES 20 A 479 ASN ALA LYS ASN ILE LEU VAL GLN PHE ASN THR PRO VAL SEQRES 21 A 479 GLN ILE ASN CYS THR ARG PRO ASN ASN ASN THR ARG LYS SEQRES 22 A 479 SER ILE ARG ILE GLY PRO GLY GLN ALA PHE TYR ALA THR SEQRES 23 A 479 GLY ASP ILE ILE GLY ASP ILE ARG GLN ALA HIS CYS ASN SEQRES 24 A 479 VAL SER LYS ALA THR TRP ASN GLU THR LEU GLY LYS VAL SEQRES 25 A 479 VAL LYS GLN LEU ARG LYS HIS PHE GLY ASN ASN THR ILE SEQRES 26 A 479 ILE ARG PHE ALA ASN SER SER GLY GLY ASP LEU GLU VAL SEQRES 27 A 479 THR THR HIS SER PHE ASN CYS GLY GLY GLU PHE PHE TYR SEQRES 28 A 479 CYS ASN THR SER GLY LEU PHE ASN SER THR TRP ILE SER SEQRES 29 A 479 ASN THR SER VAL GLN GLY SER ASN SER THR GLY SER ASN SEQRES 30 A 479 ASP SER ILE THR LEU PRO CYS ARG ILE LYS GLN ILE ILE SEQRES 31 A 479 ASN MET TRP GLN ARG ILE GLY GLN ALA MET TYR ALA PRO SEQRES 32 A 479 PRO ILE GLN GLY VAL ILE ARG CYS VAL SER ASN ILE THR SEQRES 33 A 479 GLY LEU ILE LEU THR ARG ASP GLY GLY SER THR ASN SER SEQRES 34 A 479 THR THR GLU THR PHE ARG PRO GLY GLY GLY ASP MET ARG SEQRES 35 A 479 ASP ASN TRP ARG SER GLU LEU TYR LYS TYR LYS VAL VAL SEQRES 36 A 479 LYS ILE GLU PRO LEU GLY VAL ALA PRO THR ARG CYS LYS SEQRES 37 A 479 ARG ARG VAL VAL GLY ARG ARG ARG ARG ARG ARG SEQRES 1 B 153 ALA VAL GLY ILE GLY ALA VAL PHE LEU GLY PHE LEU GLY SEQRES 2 B 153 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 B 153 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 B 153 GLN GLN SER ASN LEU LEU ARG ALA PRO GLU ALA GLN GLN SEQRES 5 B 153 HIS LEU LEU LYS LEU THR VAL TRP GLY ILE LYS GLN LEU SEQRES 6 B 153 GLN ALA ARG VAL LEU ALA VAL GLU ARG TYR LEU ARG ASP SEQRES 7 B 153 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 B 153 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 B 153 ASN ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 B 153 LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE SEQRES 11 B 153 ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 B 153 LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP SEQRES 1 C 479 ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO VAL TRP SEQRES 2 C 479 LYS ASP ALA GLU THR THR LEU PHE CYS ALA SER ASP ALA SEQRES 3 C 479 LYS ALA TYR GLU THR GLU LYS HIS ASN VAL TRP ALA THR SEQRES 4 C 479 HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN GLU ILE SEQRES 5 C 479 HIS LEU GLU ASN VAL THR GLU GLU PHE ASN MET TRP LYS SEQRES 6 C 479 ASN ASN MET VAL GLU GLN MET HIS THR ASP ILE ILE SER SEQRES 7 C 479 LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS LEU THR SEQRES 8 C 479 PRO LEU CYS VAL THR LEU GLN CYS THR ASN VAL THR ASN SEQRES 9 C 479 ASN ILE THR ASP ASP MET ARG GLY GLU LEU LYS ASN CYS SEQRES 10 C 479 SER PHE ASN MET THR THR GLU LEU ARG ASP LYS LYS GLN SEQRES 11 C 479 LYS VAL TYR SER LEU PHE TYR ARG LEU ASP VAL VAL GLN SEQRES 12 C 479 ILE ASN GLU ASN GLN GLY ASN ARG SER ASN ASN SER ASN SEQRES 13 C 479 LYS GLU TYR ARG LEU ILE ASN CYS ASN THR SER ALA ILE SEQRES 14 C 479 THR GLN ALA CYS PRO LYS VAL SER PHE GLU PRO ILE PRO SEQRES 15 C 479 ILE HIS TYR CYS ALA PRO ALA GLY PHE ALA ILE LEU LYS SEQRES 16 C 479 CYS LYS ASP LYS LYS PHE ASN GLY THR GLY PRO CYS PRO SEQRES 17 C 479 SER VAL SER THR VAL GLN CYS THR HIS GLY ILE LYS PRO SEQRES 18 C 479 VAL VAL SER THR GLN LEU LEU LEU ASN GLY SER LEU ALA SEQRES 19 C 479 GLU GLU GLU VAL MET ILE ARG SER GLU ASN ILE THR ASN SEQRES 20 C 479 ASN ALA LYS ASN ILE LEU VAL GLN PHE ASN THR PRO VAL SEQRES 21 C 479 GLN ILE ASN CYS THR ARG PRO ASN ASN ASN THR ARG LYS SEQRES 22 C 479 SER ILE ARG ILE GLY PRO GLY GLN ALA PHE TYR ALA THR SEQRES 23 C 479 GLY ASP ILE ILE GLY ASP ILE ARG GLN ALA HIS CYS ASN SEQRES 24 C 479 VAL SER LYS ALA THR TRP ASN GLU THR LEU GLY LYS VAL SEQRES 25 C 479 VAL LYS GLN LEU ARG LYS HIS PHE GLY ASN ASN THR ILE SEQRES 26 C 479 ILE ARG PHE ALA ASN SER SER GLY GLY ASP LEU GLU VAL SEQRES 27 C 479 THR THR HIS SER PHE ASN CYS GLY GLY GLU PHE PHE TYR SEQRES 28 C 479 CYS ASN THR SER GLY LEU PHE ASN SER THR TRP ILE SER SEQRES 29 C 479 ASN THR SER VAL GLN GLY SER ASN SER THR GLY SER ASN SEQRES 30 C 479 ASP SER ILE THR LEU PRO CYS ARG ILE LYS GLN ILE ILE SEQRES 31 C 479 ASN MET TRP GLN ARG ILE GLY GLN ALA MET TYR ALA PRO SEQRES 32 C 479 PRO ILE GLN GLY VAL ILE ARG CYS VAL SER ASN ILE THR SEQRES 33 C 479 GLY LEU ILE LEU THR ARG ASP GLY GLY SER THR ASN SER SEQRES 34 C 479 THR THR GLU THR PHE ARG PRO GLY GLY GLY ASP MET ARG SEQRES 35 C 479 ASP ASN TRP ARG SER GLU LEU TYR LYS TYR LYS VAL VAL SEQRES 36 C 479 LYS ILE GLU PRO LEU GLY VAL ALA PRO THR ARG CYS LYS SEQRES 37 C 479 ARG ARG VAL VAL GLY ARG ARG ARG ARG ARG ARG SEQRES 1 D 153 ALA VAL GLY ILE GLY ALA VAL PHE LEU GLY PHE LEU GLY SEQRES 2 D 153 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 D 153 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 D 153 GLN GLN SER ASN LEU LEU ARG ALA PRO GLU ALA GLN GLN SEQRES 5 D 153 HIS LEU LEU LYS LEU THR VAL TRP GLY ILE LYS GLN LEU SEQRES 6 D 153 GLN ALA ARG VAL LEU ALA VAL GLU ARG TYR LEU ARG ASP SEQRES 7 D 153 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 D 153 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 D 153 ASN ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 D 153 LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE SEQRES 11 D 153 ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 D 153 LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP SEQRES 1 E 479 ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO VAL TRP SEQRES 2 E 479 LYS ASP ALA GLU THR THR LEU PHE CYS ALA SER ASP ALA SEQRES 3 E 479 LYS ALA TYR GLU THR GLU LYS HIS ASN VAL TRP ALA THR SEQRES 4 E 479 HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN GLU ILE SEQRES 5 E 479 HIS LEU GLU ASN VAL THR GLU GLU PHE ASN MET TRP LYS SEQRES 6 E 479 ASN ASN MET VAL GLU GLN MET HIS THR ASP ILE ILE SER SEQRES 7 E 479 LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS LEU THR SEQRES 8 E 479 PRO LEU CYS VAL THR LEU GLN CYS THR ASN VAL THR ASN SEQRES 9 E 479 ASN ILE THR ASP ASP MET ARG GLY GLU LEU LYS ASN CYS SEQRES 10 E 479 SER PHE ASN MET THR THR GLU LEU ARG ASP LYS LYS GLN SEQRES 11 E 479 LYS VAL TYR SER LEU PHE TYR ARG LEU ASP VAL VAL GLN SEQRES 12 E 479 ILE ASN GLU ASN GLN GLY ASN ARG SER ASN ASN SER ASN SEQRES 13 E 479 LYS GLU TYR ARG LEU ILE ASN CYS ASN THR SER ALA ILE SEQRES 14 E 479 THR GLN ALA CYS PRO LYS VAL SER PHE GLU PRO ILE PRO SEQRES 15 E 479 ILE HIS TYR CYS ALA PRO ALA GLY PHE ALA ILE LEU LYS SEQRES 16 E 479 CYS LYS ASP LYS LYS PHE ASN GLY THR GLY PRO CYS PRO SEQRES 17 E 479 SER VAL SER THR VAL GLN CYS THR HIS GLY ILE LYS PRO SEQRES 18 E 479 VAL VAL SER THR GLN LEU LEU LEU ASN GLY SER LEU ALA SEQRES 19 E 479 GLU GLU GLU VAL MET ILE ARG SER GLU ASN ILE THR ASN SEQRES 20 E 479 ASN ALA LYS ASN ILE LEU VAL GLN PHE ASN THR PRO VAL SEQRES 21 E 479 GLN ILE ASN CYS THR ARG PRO ASN ASN ASN THR ARG LYS SEQRES 22 E 479 SER ILE ARG ILE GLY PRO GLY GLN ALA PHE TYR ALA THR SEQRES 23 E 479 GLY ASP ILE ILE GLY ASP ILE ARG GLN ALA HIS CYS ASN SEQRES 24 E 479 VAL SER LYS ALA THR TRP ASN GLU THR LEU GLY LYS VAL SEQRES 25 E 479 VAL LYS GLN LEU ARG LYS HIS PHE GLY ASN ASN THR ILE SEQRES 26 E 479 ILE ARG PHE ALA ASN SER SER GLY GLY ASP LEU GLU VAL SEQRES 27 E 479 THR THR HIS SER PHE ASN CYS GLY GLY GLU PHE PHE TYR SEQRES 28 E 479 CYS ASN THR SER GLY LEU PHE ASN SER THR TRP ILE SER SEQRES 29 E 479 ASN THR SER VAL GLN GLY SER ASN SER THR GLY SER ASN SEQRES 30 E 479 ASP SER ILE THR LEU PRO CYS ARG ILE LYS GLN ILE ILE SEQRES 31 E 479 ASN MET TRP GLN ARG ILE GLY GLN ALA MET TYR ALA PRO SEQRES 32 E 479 PRO ILE GLN GLY VAL ILE ARG CYS VAL SER ASN ILE THR SEQRES 33 E 479 GLY LEU ILE LEU THR ARG ASP GLY GLY SER THR ASN SER SEQRES 34 E 479 THR THR GLU THR PHE ARG PRO GLY GLY GLY ASP MET ARG SEQRES 35 E 479 ASP ASN TRP ARG SER GLU LEU TYR LYS TYR LYS VAL VAL SEQRES 36 E 479 LYS ILE GLU PRO LEU GLY VAL ALA PRO THR ARG CYS LYS SEQRES 37 E 479 ARG ARG VAL VAL GLY ARG ARG ARG ARG ARG ARG SEQRES 1 F 153 ALA VAL GLY ILE GLY ALA VAL PHE LEU GLY PHE LEU GLY SEQRES 2 F 153 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 F 153 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 F 153 GLN GLN SER ASN LEU LEU ARG ALA PRO GLU ALA GLN GLN SEQRES 5 F 153 HIS LEU LEU LYS LEU THR VAL TRP GLY ILE LYS GLN LEU SEQRES 6 F 153 GLN ALA ARG VAL LEU ALA VAL GLU ARG TYR LEU ARG ASP SEQRES 7 F 153 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 F 153 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 F 153 ASN ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 F 153 LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE SEQRES 11 F 153 ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 F 153 LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP SEQRES 1 H 232 GLN VAL ARG LEU MET GLN SER GLY ASP GLU VAL LYS LYS SEQRES 2 H 232 PRO GLY ALA SER VAL ARG LEU SER CYS LYS ALA ASP GLY SEQRES 3 H 232 TYR GLU PHE SER ASP TYR PHE LEU HIS TRP VAL ARG GLN SEQRES 4 H 232 ALA PRO GLY GLN GLY LEU GLU TRP LEU GLY PHE ILE ARG SEQRES 5 H 232 PRO ARG LEU GLY SER VAL ASN TYR SER LYS ARG PHE GLN SEQRES 6 H 232 GLY ARG ILE THR MET THR ARG ASP MET SER ILE ASN THR SEQRES 7 H 232 VAL TYR MET GLU LEU ARG SER LEU THR SER ASP ASP THR SEQRES 8 H 232 ALA GLN TYR TYR CYS ALA ARG MET TYR ASP THR ASP SER SEQRES 9 H 232 TYR LYS PHE ASP SER TRP GLY TRP GLY THR VAL VAL ILE SEQRES 10 H 232 VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO SEQRES 11 H 232 LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA SEQRES 12 H 232 ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO SEQRES 13 H 232 VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY SEQRES 14 H 232 VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU SEQRES 15 H 232 TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SER SEQRES 16 H 232 LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS SEQRES 17 H 232 PRO SER ASN THR LYS VAL ASP LYS ARG VAL GLU PRO LYS SEQRES 18 H 232 SER CYS ASP LYS THR HIS HIS HIS HIS HIS HIS SEQRES 1 I 232 GLN VAL ARG LEU MET GLN SER GLY ASP GLU VAL LYS LYS SEQRES 2 I 232 PRO GLY ALA SER VAL ARG LEU SER CYS LYS ALA ASP GLY SEQRES 3 I 232 TYR GLU PHE SER ASP TYR PHE LEU HIS TRP VAL ARG GLN SEQRES 4 I 232 ALA PRO GLY GLN GLY LEU GLU TRP LEU GLY PHE ILE ARG SEQRES 5 I 232 PRO ARG LEU GLY SER VAL ASN TYR SER LYS ARG PHE GLN SEQRES 6 I 232 GLY ARG ILE THR MET THR ARG ASP MET SER ILE ASN THR SEQRES 7 I 232 VAL TYR MET GLU LEU ARG SER LEU THR SER ASP ASP THR SEQRES 8 I 232 ALA GLN TYR TYR CYS ALA ARG MET TYR ASP THR ASP SER SEQRES 9 I 232 TYR LYS PHE ASP SER TRP GLY TRP GLY THR VAL VAL ILE SEQRES 10 I 232 VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO SEQRES 11 I 232 LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA SEQRES 12 I 232 ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO SEQRES 13 I 232 VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY SEQRES 14 I 232 VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU SEQRES 15 I 232 TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SER SEQRES 16 I 232 LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS SEQRES 17 I 232 PRO SER ASN THR LYS VAL ASP LYS ARG VAL GLU PRO LYS SEQRES 18 I 232 SER CYS ASP LYS THR HIS HIS HIS HIS HIS HIS SEQRES 1 J 232 GLN VAL ARG LEU MET GLN SER GLY ASP GLU VAL LYS LYS SEQRES 2 J 232 PRO GLY ALA SER VAL ARG LEU SER CYS LYS ALA ASP GLY SEQRES 3 J 232 TYR GLU PHE SER ASP TYR PHE LEU HIS TRP VAL ARG GLN SEQRES 4 J 232 ALA PRO GLY GLN GLY LEU GLU TRP LEU GLY PHE ILE ARG SEQRES 5 J 232 PRO ARG LEU GLY SER VAL ASN TYR SER LYS ARG PHE GLN SEQRES 6 J 232 GLY ARG ILE THR MET THR ARG ASP MET SER ILE ASN THR SEQRES 7 J 232 VAL TYR MET GLU LEU ARG SER LEU THR SER ASP ASP THR SEQRES 8 J 232 ALA GLN TYR TYR CYS ALA ARG MET TYR ASP THR ASP SER SEQRES 9 J 232 TYR LYS PHE ASP SER TRP GLY TRP GLY THR VAL VAL ILE SEQRES 10 J 232 VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO SEQRES 11 J 232 LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA SEQRES 12 J 232 ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO SEQRES 13 J 232 VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY SEQRES 14 J 232 VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU SEQRES 15 J 232 TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SER SEQRES 16 J 232 LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS SEQRES 17 J 232 PRO SER ASN THR LYS VAL ASP LYS ARG VAL GLU PRO LYS SEQRES 18 J 232 SER CYS ASP LYS THR HIS HIS HIS HIS HIS HIS SEQRES 1 L 210 ASP SER PRO MET THR GLN SER PRO SER SER LEU SER ILE SEQRES 2 L 210 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG SER SER SEQRES 3 L 210 GLN TYR ALA ALA HIS ASN VAL ASN TRP TYR GLN GLN ARG SEQRES 4 L 210 SER GLY LYS PRO PRO LYS LEU LEU ILE TYR ASP THR SER SEQRES 5 L 210 LYS LEU GLN ALA GLY VAL PRO SER ARG PHE ARG GLY GLY SEQRES 6 L 210 GLY PHE GLY THR GLU PHE THR PHE THR ILE SER SER LEU SEQRES 7 L 210 GLN PRO GLU ASP VAL ALA THR TYR TYR CYS GLN HIS TYR SEQRES 8 L 210 GLU PHE PHE GLY GLN GLY THR ARG LEU GLU ILE THR ARG SEQRES 9 L 210 THR VAL ALA ALA PRO SER VAL PHE ILE PHE PRO PRO SER SEQRES 10 L 210 ASP GLU GLN LEU LYS SER GLY THR ALA SER VAL VAL CYS SEQRES 11 L 210 LEU LEU ASN ASN PHE TYR PRO ARG GLU ALA LYS VAL GLN SEQRES 12 L 210 TRP LYS VAL ASP ASN ALA LEU GLN SER GLY ASN SER GLN SEQRES 13 L 210 GLU SER VAL THR GLU GLN ASP SER LYS ASP SER THR TYR SEQRES 14 L 210 SER LEU SER SER THR LEU THR LEU SER LYS ALA ASP TYR SEQRES 15 L 210 GLU LYS HIS LYS VAL TYR ALA CYS GLU VAL THR HIS GLN SEQRES 16 L 210 GLY LEU SER SER PRO VAL THR LYS SER PHE ASN ARG GLY SEQRES 17 L 210 GLU CYS SEQRES 1 M 210 ASP SER PRO MET THR GLN SER PRO SER SER LEU SER ILE SEQRES 2 M 210 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG SER SER SEQRES 3 M 210 GLN TYR ALA ALA HIS ASN VAL ASN TRP TYR GLN GLN ARG SEQRES 4 M 210 SER GLY LYS PRO PRO LYS LEU LEU ILE TYR ASP THR SER SEQRES 5 M 210 LYS LEU GLN ALA GLY VAL PRO SER ARG PHE ARG GLY GLY SEQRES 6 M 210 GLY PHE GLY THR GLU PHE THR PHE THR ILE SER SER LEU SEQRES 7 M 210 GLN PRO GLU ASP VAL ALA THR TYR TYR CYS GLN HIS TYR SEQRES 8 M 210 GLU PHE PHE GLY GLN GLY THR ARG LEU GLU ILE THR ARG SEQRES 9 M 210 THR VAL ALA ALA PRO SER VAL PHE ILE PHE PRO PRO SER SEQRES 10 M 210 ASP GLU GLN LEU LYS SER GLY THR ALA SER VAL VAL CYS SEQRES 11 M 210 LEU LEU ASN ASN PHE TYR PRO ARG GLU ALA LYS VAL GLN SEQRES 12 M 210 TRP LYS VAL ASP ASN ALA LEU GLN SER GLY ASN SER GLN SEQRES 13 M 210 GLU SER VAL THR GLU GLN ASP SER LYS ASP SER THR TYR SEQRES 14 M 210 SER LEU SER SER THR LEU THR LEU SER LYS ALA ASP TYR SEQRES 15 M 210 GLU LYS HIS LYS VAL TYR ALA CYS GLU VAL THR HIS GLN SEQRES 16 M 210 GLY LEU SER SER PRO VAL THR LYS SER PHE ASN ARG GLY SEQRES 17 M 210 GLU CYS SEQRES 1 N 210 ASP SER PRO MET THR GLN SER PRO SER SER LEU SER ILE SEQRES 2 N 210 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG SER SER SEQRES 3 N 210 GLN TYR ALA ALA HIS ASN VAL ASN TRP TYR GLN GLN ARG SEQRES 4 N 210 SER GLY LYS PRO PRO LYS LEU LEU ILE TYR ASP THR SER SEQRES 5 N 210 LYS LEU GLN ALA GLY VAL PRO SER ARG PHE ARG GLY GLY SEQRES 6 N 210 GLY PHE GLY THR GLU PHE THR PHE THR ILE SER SER LEU SEQRES 7 N 210 GLN PRO GLU ASP VAL ALA THR TYR TYR CYS GLN HIS TYR SEQRES 8 N 210 GLU PHE PHE GLY GLN GLY THR ARG LEU GLU ILE THR ARG SEQRES 9 N 210 THR VAL ALA ALA PRO SER VAL PHE ILE PHE PRO PRO SER SEQRES 10 N 210 ASP GLU GLN LEU LYS SER GLY THR ALA SER VAL VAL CYS SEQRES 11 N 210 LEU LEU ASN ASN PHE TYR PRO ARG GLU ALA LYS VAL GLN SEQRES 12 N 210 TRP LYS VAL ASP ASN ALA LEU GLN SER GLY ASN SER GLN SEQRES 13 N 210 GLU SER VAL THR GLU GLN ASP SER LYS ASP SER THR TYR SEQRES 14 N 210 SER LEU SER SER THR LEU THR LEU SER LYS ALA ASP TYR SEQRES 15 N 210 GLU LYS HIS LYS VAL TYR ALA CYS GLU VAL THR HIS GLN SEQRES 16 N 210 GLY LEU SER SER PRO VAL THR LYS SER PHE ASN ARG GLY SEQRES 17 N 210 GLU CYS HET NAG G 1 14 HET NAG G 2 14 HET NAG K 1 14 HET NAG K 2 14 HET NAG O 1 14 HET NAG O 2 14 HET BMA O 3 11 HET NAG P 1 14 HET NAG P 2 14 HET BMA P 3 11 HET MAN P 4 11 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 MAN Q 6 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 BMA T 3 11 HET MAN T 4 11 HET MAN T 5 11 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 BMA X 3 11 HET NAG Y 1 14 HET NAG Y 2 14 HET BMA Y 3 11 HET MAN Y 4 11 HET NAG Z 1 14 HET NAG Z 2 14 HET BMA Z 3 11 HET MAN Z 4 11 HET MAN Z 5 11 HET MAN Z 6 11 HET NAG a 1 14 HET NAG a 2 14 HET NAG b 1 14 HET NAG b 2 14 HET NAG c 1 14 HET NAG c 2 14 HET BMA c 3 11 HET MAN c 4 11 HET MAN c 5 11 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 NAG g 1 14 HET NAG g 2 14 HET NAG h 1 14 HET NAG h 2 14 HET BMA h 3 11 HET MAN h 4 11 HET NAG i 1 14 HET NAG i 2 14 HET BMA i 3 11 HET MAN i 4 11 HET NAG j 1 14 HET NAG j 2 14 HET BMA j 3 11 HET MAN j 4 11 HET MAN j 5 11 HET NAG k 1 14 HET NAG k 2 14 HET NAG l 1 14 HET NAG l 2 14 HET NAG m 1 14 HET NAG m 2 14 HET BMA m 3 11 HET MAN m 4 11 HET MAN m 5 11 HET NAG n 1 14 HET NAG n 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 C 601 14 HET NAG C 602 14 HET NAG C 603 14 HET NAG C 604 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 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 13 NAG 70(C8 H15 N O6) FORMUL 15 BMA 13(C6 H12 O6) FORMUL 16 MAN 18(C6 H12 O6) HELIX 1 AA1 ASN A 99 LYS A 117 1 19 HELIX 2 AA2 LEU A 122 CYS A 126 5 5 HELIX 3 AA3 THR A 147 ARG A 151 5 5 HELIX 4 AA4 ASN A 195 ASN A 197 5 3 HELIX 5 AA5 LYS A 335 GLY A 354 1 20 HELIX 6 AA6 ASP A 368 THR A 373 1 6 HELIX 7 AA7 ASN A 425 ARG A 429 5 5 HELIX 8 AA8 ASP A 474 SER A 481 1 8 HELIX 9 AA9 THR B 529 THR B 536 1 8 HELIX 10 AB1 ALA B 541 LEU B 545 5 5 HELIX 11 AB2 THR B 569 TRP B 596 1 28 HELIX 12 AB3 ASN B 618 ASN B 625 1 8 HELIX 13 AB4 THR B 627 SER B 636 1 10 HELIX 14 AB5 TYR B 638 LEU B 661 1 24 HELIX 15 AB6 ASN C 99 LYS C 117 1 19 HELIX 16 AB7 LEU C 122 CYS C 126 5 5 HELIX 17 AB8 THR C 147 ARG C 151 5 5 HELIX 18 AB9 ASN C 195 ASN C 197 5 3 HELIX 19 AC1 LYS C 335 GLY C 354 1 20 HELIX 20 AC2 ASP C 368 THR C 373 1 6 HELIX 21 AC3 ASN C 425 ARG C 429 5 5 HELIX 22 AC4 ASP C 474 SER C 481 1 8 HELIX 23 AC5 THR D 529 THR D 536 1 8 HELIX 24 AC6 ALA D 541 LEU D 545 5 5 HELIX 25 AC7 THR D 569 TRP D 596 1 28 HELIX 26 AC8 ASN D 618 ASN D 625 1 8 HELIX 27 AC9 THR D 627 GLU D 634 1 8 HELIX 28 AD1 ILE D 635 LEU D 661 1 27 HELIX 29 AD2 ASN E 99 LEU E 116 1 18 HELIX 30 AD3 LEU E 122 CYS E 126 5 5 HELIX 31 AD4 THR E 147 ARG E 151 5 5 HELIX 32 AD5 ASN E 195 ASN E 197 5 3 HELIX 33 AD6 LYS E 335 GLY E 354 1 20 HELIX 34 AD7 ASP E 368 THR E 373 1 6 HELIX 35 AD8 ASN E 425 ARG E 429 5 5 HELIX 36 AD9 ASP E 474 SER E 481 1 8 HELIX 37 AE1 THR F 529 THR F 536 1 8 HELIX 38 AE2 ALA F 541 LEU F 545 5 5 HELIX 39 AE3 THR F 569 TRP F 596 1 28 HELIX 40 AE4 ASN F 618 ASN F 625 1 8 HELIX 41 AE5 THR F 627 SER F 636 1 10 HELIX 42 AE6 TYR F 638 LEU F 661 1 24 HELIX 43 AE7 THR H 83 THR H 87 5 5 HELIX 44 AE8 THR I 83 THR I 87 5 5 HELIX 45 AE9 THR J 83 THR J 87 5 5 HELIX 46 AF1 GLN L 79 VAL L 83 5 5 HELIX 47 AF2 GLN M 79 VAL M 83 5 5 HELIX 48 AF3 GLN N 79 VAL N 83 5 5 SHEET 1 AA1 3 LEU A 494 THR A 499 0 SHEET 2 AA1 3 TRP A 35 TYR A 40 -1 N TYR A 39 O GLY A 495 SHEET 3 AA1 3 ILE B 603 PRO B 609 -1 O CYS B 604 N VAL A 38 SHEET 1 AA2 5 TRP A 45 ASP A 47 0 SHEET 2 AA2 5 TYR A 486 ILE A 491 -1 O LYS A 490 N LYS A 46 SHEET 3 AA2 5 PHE A 223 CYS A 228 -1 N ALA A 224 O VAL A 489 SHEET 4 AA2 5 VAL A 242 VAL A 245 -1 O SER A 243 N LYS A 227 SHEET 5 AA2 5 GLU A 83 HIS A 85 -1 N ILE A 84 O THR A 244 SHEET 1 AA3 3 VAL A 75 PRO A 76 0 SHEET 2 AA3 3 PHE A 53 SER A 56 1 N SER A 56 O VAL A 75 SHEET 3 AA3 3 HIS A 216 CYS A 218 -1 O CYS A 218 N PHE A 53 SHEET 1 AA4 2 GLU A 91 ASN A 94 0 SHEET 2 AA4 2 THR A 236 CYS A 239 -1 O GLY A 237 N PHE A 93 SHEET 1 AA5 5 LYS A 169 TYR A 177 0 SHEET 2 AA5 5 LEU A 154 THR A 162 -1 N MET A 161 O GLN A 170 SHEET 3 AA5 5 LEU A 129 ASN A 133 -1 N GLN A 130 O SER A 158 SHEET 4 AA5 5 LYS A 189 LEU A 193 -1 O TYR A 191 N LEU A 129 SHEET 5 AA5 5 VAL A 181 GLN A 183 -1 N VAL A 182 O ARG A 192 SHEET 1 AA6 7 LEU A 259 LEU A 261 0 SHEET 2 AA6 7 GLY A 441 ARG A 456 -1 O THR A 450 N LEU A 260 SHEET 3 AA6 7 ILE A 284 ASN A 302 -1 N PHE A 288 O THR A 450 SHEET 4 AA6 7 HIS A 330 SER A 334 -1 O ASN A 332 N ASN A 295 SHEET 5 AA6 7 SER A 413 LYS A 421 -1 O ILE A 414 N VAL A 333 SHEET 6 AA6 7 GLU A 381 CYS A 385 -1 N TYR A 384 O ARG A 419 SHEET 7 AA6 7 HIS A 374 CYS A 378 -1 N HIS A 374 O CYS A 385 SHEET 1 AA7 6 MET A 271 ARG A 273 0 SHEET 2 AA7 6 ILE A 284 ASN A 302 -1 O LEU A 285 N ARG A 273 SHEET 3 AA7 6 GLY A 441 ARG A 456 -1 O THR A 450 N PHE A 288 SHEET 4 AA7 6 GLU A 466 PRO A 470 -1 O ARG A 469 N THR A 455 SHEET 5 AA7 6 ILE A 359 PHE A 361 1 N ARG A 360 O GLU A 466 SHEET 6 AA7 6 SER A 393 TRP A 395 -1 O SER A 393 N PHE A 361 SHEET 1 AA8 2 ARG A 304 ARG A 310 0 SHEET 2 AA8 2 ALA A 316 THR A 320 -1 O ALA A 319 N LYS A 305 SHEET 1 AA9 3 LEU C 494 THR C 499 0 SHEET 2 AA9 3 TRP C 35 TYR C 40 -1 N TYR C 39 O GLY C 495 SHEET 3 AA9 3 ILE D 603 PRO D 609 -1 O CYS D 604 N VAL C 38 SHEET 1 AB1 5 TRP C 45 ASP C 47 0 SHEET 2 AB1 5 TYR C 486 ILE C 491 -1 O LYS C 490 N LYS C 46 SHEET 3 AB1 5 PHE C 223 CYS C 228 -1 N ALA C 224 O VAL C 489 SHEET 4 AB1 5 VAL C 242 VAL C 245 -1 O SER C 243 N LYS C 227 SHEET 5 AB1 5 GLU C 83 HIS C 85 -1 N ILE C 84 O THR C 244 SHEET 1 AB2 3 VAL C 75 PRO C 76 0 SHEET 2 AB2 3 PHE C 53 SER C 56 1 N SER C 56 O VAL C 75 SHEET 3 AB2 3 HIS C 216 CYS C 218 -1 O CYS C 218 N PHE C 53 SHEET 1 AB3 2 GLU C 91 ASN C 94 0 SHEET 2 AB3 2 THR C 236 CYS C 239 -1 O GLY C 237 N PHE C 93 SHEET 1 AB4 5 LYS C 169 TYR C 177 0 SHEET 2 AB4 5 LEU C 154 THR C 162 -1 N MET C 161 O GLN C 170 SHEET 3 AB4 5 LEU C 129 ASN C 133 -1 N GLN C 130 O SER C 158 SHEET 4 AB4 5 LYS C 189 LEU C 193 -1 O TYR C 191 N LEU C 129 SHEET 5 AB4 5 VAL C 181 GLN C 183 -1 N VAL C 182 O ARG C 192 SHEET 1 AB5 7 LEU C 259 LEU C 261 0 SHEET 2 AB5 7 GLY C 441 ARG C 456 -1 O THR C 450 N LEU C 260 SHEET 3 AB5 7 ILE C 284 ASN C 302 -1 N PHE C 288 O THR C 450 SHEET 4 AB5 7 HIS C 330 SER C 334 -1 O ASN C 332 N ASN C 295 SHEET 5 AB5 7 SER C 413 LYS C 421 -1 O ILE C 414 N VAL C 333 SHEET 6 AB5 7 GLU C 381 CYS C 385 -1 N TYR C 384 O ARG C 419 SHEET 7 AB5 7 HIS C 374 CYS C 378 -1 N HIS C 374 O CYS C 385 SHEET 1 AB6 6 MET C 271 ARG C 273 0 SHEET 2 AB6 6 ILE C 284 ASN C 302 -1 O LEU C 285 N ARG C 273 SHEET 3 AB6 6 GLY C 441 ARG C 456 -1 O THR C 450 N PHE C 288 SHEET 4 AB6 6 GLU C 466 PRO C 470 -1 O ARG C 469 N THR C 455 SHEET 5 AB6 6 ILE C 359 PHE C 361 1 N ARG C 360 O GLU C 466 SHEET 6 AB6 6 SER C 393 TRP C 395 -1 O SER C 393 N PHE C 361 SHEET 1 AB7 2 ARG C 304 ARG C 310 0 SHEET 2 AB7 2 ALA C 316 THR C 320 -1 O ALA C 319 N LYS C 305 SHEET 1 AB8 3 LEU E 494 THR E 499 0 SHEET 2 AB8 3 TRP E 35 TYR E 40 -1 N TYR E 39 O GLY E 495 SHEET 3 AB8 3 ILE F 603 CYS F 605 -1 O CYS F 604 N VAL E 38 SHEET 1 AB9 5 TRP E 45 ASP E 47 0 SHEET 2 AB9 5 TYR E 486 ILE E 491 -1 O LYS E 490 N LYS E 46 SHEET 3 AB9 5 PHE E 223 CYS E 228 -1 N ALA E 224 O VAL E 489 SHEET 4 AB9 5 VAL E 242 VAL E 245 -1 O SER E 243 N LYS E 227 SHEET 5 AB9 5 GLU E 83 HIS E 85 -1 N ILE E 84 O THR E 244 SHEET 1 AC1 3 VAL E 75 PRO E 76 0 SHEET 2 AC1 3 PHE E 53 SER E 56 1 N SER E 56 O VAL E 75 SHEET 3 AC1 3 HIS E 216 CYS E 218 -1 O CYS E 218 N PHE E 53 SHEET 1 AC2 2 GLU E 91 ASN E 94 0 SHEET 2 AC2 2 THR E 236 CYS E 239 -1 O GLY E 237 N PHE E 93 SHEET 1 AC3 5 LYS E 171 TYR E 177 0 SHEET 2 AC3 5 LEU E 154 ASN E 160 -1 N PHE E 159 O VAL E 172 SHEET 3 AC3 5 LEU E 129 ASN E 133 -1 N GLN E 130 O SER E 158 SHEET 4 AC3 5 LYS E 189 LEU E 193 -1 O TYR E 191 N LEU E 129 SHEET 5 AC3 5 VAL E 181 GLN E 183 -1 N VAL E 182 O ARG E 192 SHEET 1 AC4 7 LEU E 259 LEU E 261 0 SHEET 2 AC4 7 GLY E 441 ARG E 456 -1 O THR E 450 N LEU E 260 SHEET 3 AC4 7 ILE E 284 ASN E 302 -1 N PHE E 288 O THR E 450 SHEET 4 AC4 7 HIS E 330 SER E 334 -1 O ASN E 332 N ASN E 295 SHEET 5 AC4 7 SER E 413 LYS E 421 -1 O ILE E 414 N VAL E 333 SHEET 6 AC4 7 GLU E 381 CYS E 385 -1 N TYR E 384 O ARG E 419 SHEET 7 AC4 7 HIS E 374 CYS E 378 -1 N HIS E 374 O CYS E 385 SHEET 1 AC5 6 MET E 271 ARG E 273 0 SHEET 2 AC5 6 ILE E 284 ASN E 302 -1 O LEU E 285 N ARG E 273 SHEET 3 AC5 6 GLY E 441 ARG E 456 -1 O THR E 450 N PHE E 288 SHEET 4 AC5 6 GLU E 466 PRO E 470 -1 O ARG E 469 N THR E 455 SHEET 5 AC5 6 ILE E 359 PHE E 361 1 N ARG E 360 O GLU E 466 SHEET 6 AC5 6 SER E 393 TRP E 395 -1 O SER E 393 N PHE E 361 SHEET 1 AC6 2 ARG E 304 ARG E 310 0 SHEET 2 AC6 2 ALA E 316 THR E 320 -1 O ALA E 319 N LYS E 305 SHEET 1 AC7 4 ARG H 3 GLN H 6 0 SHEET 2 AC7 4 VAL H 18 ASP H 25 -1 O LYS H 23 N MET H 5 SHEET 3 AC7 4 THR H 77 LEU H 82 -1 O LEU H 82 N VAL H 18 SHEET 4 AC7 4 ILE H 67 ASP H 72 -1 N THR H 68 O GLU H 81 SHEET 1 AC8 6 GLU H 10 LYS H 12 0 SHEET 2 AC8 6 THR H 107 VAL H 111 1 O ILE H 110 N LYS H 12 SHEET 3 AC8 6 ALA H 88 MET H 95 -1 N TYR H 90 O THR H 107 SHEET 4 AC8 6 LEU H 34 GLN H 39 -1 N VAL H 37 O TYR H 91 SHEET 5 AC8 6 LEU H 45 ILE H 51 -1 O LEU H 48 N TRP H 36 SHEET 6 AC8 6 VAL H 57 TYR H 59 -1 O ASN H 58 N PHE H 50 SHEET 1 AC9 4 GLU H 10 LYS H 12 0 SHEET 2 AC9 4 THR H 107 VAL H 111 1 O ILE H 110 N LYS H 12 SHEET 3 AC9 4 ALA H 88 MET H 95 -1 N TYR H 90 O THR H 107 SHEET 4 AC9 4 PHE H 100C TRP H 103 -1 O ASP H 101 N ARG H 94 SHEET 1 AD1 4 ARG I 3 GLN I 6 0 SHEET 2 AD1 4 VAL I 18 ASP I 25 -1 O LYS I 23 N MET I 5 SHEET 3 AD1 4 THR I 77 LEU I 82 -1 O LEU I 82 N VAL I 18 SHEET 4 AD1 4 ILE I 67 ASP I 72 -1 N THR I 68 O GLU I 81 SHEET 1 AD2 6 GLU I 10 LYS I 12 0 SHEET 2 AD2 6 THR I 107 VAL I 111 1 O ILE I 110 N LYS I 12 SHEET 3 AD2 6 ALA I 88 MET I 95 -1 N TYR I 90 O THR I 107 SHEET 4 AD2 6 LEU I 34 GLN I 39 -1 N VAL I 37 O TYR I 91 SHEET 5 AD2 6 LEU I 45 ILE I 51 -1 O LEU I 48 N TRP I 36 SHEET 6 AD2 6 VAL I 57 TYR I 59 -1 O ASN I 58 N PHE I 50 SHEET 1 AD3 4 GLU I 10 LYS I 12 0 SHEET 2 AD3 4 THR I 107 VAL I 111 1 O ILE I 110 N LYS I 12 SHEET 3 AD3 4 ALA I 88 MET I 95 -1 N TYR I 90 O THR I 107 SHEET 4 AD3 4 PHE I 100C TRP I 103 -1 O ASP I 101 N ARG I 94 SHEET 1 AD4 4 ARG J 3 GLN J 6 0 SHEET 2 AD4 4 VAL J 18 ASP J 25 -1 O ASP J 25 N ARG J 3 SHEET 3 AD4 4 THR J 77 LEU J 82 -1 O LEU J 82 N VAL J 18 SHEET 4 AD4 4 ILE J 67 ASP J 72 -1 N THR J 68 O GLU J 81 SHEET 1 AD5 6 GLU J 10 LYS J 12 0 SHEET 2 AD5 6 THR J 107 VAL J 111 1 O ILE J 110 N LYS J 12 SHEET 3 AD5 6 ALA J 88 MET J 95 -1 N TYR J 90 O THR J 107 SHEET 4 AD5 6 LEU J 34 GLN J 39 -1 N VAL J 37 O TYR J 91 SHEET 5 AD5 6 LEU J 45 ILE J 51 -1 O LEU J 48 N TRP J 36 SHEET 6 AD5 6 VAL J 57 TYR J 59 -1 O ASN J 58 N PHE J 50 SHEET 1 AD6 4 GLU J 10 LYS J 12 0 SHEET 2 AD6 4 THR J 107 VAL J 111 1 O ILE J 110 N LYS J 12 SHEET 3 AD6 4 ALA J 88 MET J 95 -1 N TYR J 90 O THR J 107 SHEET 4 AD6 4 PHE J 100C TRP J 103 -1 O ASP J 101 N ARG J 94 SHEET 1 AD7 6 SER L 10 ILE L 13 0 SHEET 2 AD7 6 THR L 102 ILE L 106 1 O GLU L 105 N ILE L 13 SHEET 3 AD7 6 THR L 85 HIS L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AD7 6 ASN L 34 GLN L 38 -1 N GLN L 38 O THR L 85 SHEET 5 AD7 6 LYS L 45 TYR L 49 -1 O LYS L 45 N GLN L 37 SHEET 6 AD7 6 LYS L 53 LEU L 54 -1 O LYS L 53 N TYR L 49 SHEET 1 AD8 4 SER L 10 ILE L 13 0 SHEET 2 AD8 4 THR L 102 ILE L 106 1 O GLU L 105 N ILE L 13 SHEET 3 AD8 4 THR L 85 HIS L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AD8 4 PHE L 97 PHE L 98 -1 O PHE L 97 N HIS L 90 SHEET 1 AD9 3 THR L 20 THR L 22 0 SHEET 2 AD9 3 THR L 72 THR L 74 -1 O PHE L 73 N ILE L 21 SHEET 3 AD9 3 ARG L 63 GLY L 65 -1 N ARG L 63 O THR L 74 SHEET 1 AE1 6 SER M 10 ILE M 13 0 SHEET 2 AE1 6 THR M 102 ILE M 106 1 O GLU M 105 N ILE M 13 SHEET 3 AE1 6 THR M 85 HIS M 90 -1 N TYR M 86 O THR M 102 SHEET 4 AE1 6 ASN M 34 GLN M 38 -1 N GLN M 38 O THR M 85 SHEET 5 AE1 6 LYS M 45 TYR M 49 -1 O LYS M 45 N GLN M 37 SHEET 6 AE1 6 LYS M 53 LEU M 54 -1 O LYS M 53 N TYR M 49 SHEET 1 AE2 4 SER M 10 ILE M 13 0 SHEET 2 AE2 4 THR M 102 ILE M 106 1 O GLU M 105 N ILE M 13 SHEET 3 AE2 4 THR M 85 HIS M 90 -1 N TYR M 86 O THR M 102 SHEET 4 AE2 4 PHE M 97 PHE M 98 -1 O PHE M 97 N HIS M 90 SHEET 1 AE3 3 THR M 20 THR M 22 0 SHEET 2 AE3 3 THR M 72 THR M 74 -1 O PHE M 73 N ILE M 21 SHEET 3 AE3 3 ARG M 63 GLY M 65 -1 N ARG M 63 O THR M 74 SHEET 1 AE4 6 SER N 10 ILE N 13 0 SHEET 2 AE4 6 THR N 102 ILE N 106 1 O GLU N 105 N ILE N 13 SHEET 3 AE4 6 THR N 85 HIS N 90 -1 N TYR N 86 O THR N 102 SHEET 4 AE4 6 ASN N 34 GLN N 38 -1 N GLN N 38 O THR N 85 SHEET 5 AE4 6 LYS N 45 TYR N 49 -1 O LYS N 45 N GLN N 37 SHEET 6 AE4 6 LYS N 53 LEU N 54 -1 O LYS N 53 N TYR N 49 SHEET 1 AE5 4 SER N 10 ILE N 13 0 SHEET 2 AE5 4 THR N 102 ILE N 106 1 O GLU N 105 N ILE N 13 SHEET 3 AE5 4 THR N 85 HIS N 90 -1 N TYR N 86 O THR N 102 SHEET 4 AE5 4 PHE N 97 PHE N 98 -1 O PHE N 97 N HIS N 90 SHEET 1 AE6 3 THR N 20 THR N 22 0 SHEET 2 AE6 3 THR N 72 THR N 74 -1 O PHE N 73 N ILE N 21 SHEET 3 AE6 3 ARG N 63 GLY N 65 -1 N ARG N 63 O THR N 74 SSBOND 1 CYS A 54 CYS A 74 1555 1555 2.03 SSBOND 2 CYS A 119 CYS A 205 1555 1555 2.04 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 218 CYS A 247 1555 1555 2.03 SSBOND 6 CYS A 228 CYS A 239 1555 1555 2.03 SSBOND 7 CYS A 378 CYS A 445 1555 1555 2.03 SSBOND 8 CYS A 385 CYS A 418 1555 1555 2.03 SSBOND 9 CYS A 501 CYS B 605 1555 1555 2.03 SSBOND 10 CYS B 598 CYS B 604 1555 1555 2.03 SSBOND 11 CYS C 54 CYS C 74 1555 1555 2.03 SSBOND 12 CYS C 119 CYS C 205 1555 1555 2.03 SSBOND 13 CYS C 126 CYS C 196 1555 1555 2.03 SSBOND 14 CYS C 131 CYS C 157 1555 1555 2.03 SSBOND 15 CYS C 218 CYS C 247 1555 1555 2.03 SSBOND 16 CYS C 228 CYS C 239 1555 1555 2.03 SSBOND 17 CYS C 378 CYS C 445 1555 1555 2.03 SSBOND 18 CYS C 385 CYS C 418 1555 1555 2.03 SSBOND 19 CYS C 501 CYS D 605 1555 1555 2.03 SSBOND 20 CYS D 598 CYS D 604 1555 1555 2.03 SSBOND 21 CYS E 54 CYS E 74 1555 1555 2.03 SSBOND 22 CYS E 119 CYS E 205 1555 1555 2.04 SSBOND 23 CYS E 126 CYS E 196 1555 1555 2.03 SSBOND 24 CYS E 131 CYS E 157 1555 1555 2.03 SSBOND 25 CYS E 218 CYS E 247 1555 1555 2.03 SSBOND 26 CYS E 228 CYS E 239 1555 1555 2.03 SSBOND 27 CYS E 378 CYS E 445 1555 1555 2.03 SSBOND 28 CYS E 385 CYS E 418 1555 1555 2.03 SSBOND 29 CYS E 501 CYS F 605 1555 1555 2.03 SSBOND 30 CYS F 598 CYS F 604 1555 1555 2.03 SSBOND 31 CYS H 22 CYS H 92 1555 1555 2.03 SSBOND 32 CYS I 22 CYS I 92 1555 1555 2.03 SSBOND 33 CYS J 22 CYS J 92 1555 1555 2.03 SSBOND 34 CYS L 23 CYS L 88 1555 1555 2.03 SSBOND 35 CYS M 23 CYS M 88 1555 1555 2.03 SSBOND 36 CYS N 23 CYS N 88 1555 1555 2.03 LINK ND2 ASN A 133 C1 NAG A 601 1555 1555 1.44 LINK ND2 ASN A 156 C1 NAG G 1 1555 1555 1.44 LINK ND2 ASN A 160 C1 NAG K 1 1555 1555 1.44 LINK ND2 ASN A 197 C1 NAG O 1 1555 1555 1.44 LINK ND2 ASN A 234 C1 NAG P 1 1555 1555 1.44 LINK ND2 ASN A 262 C1 NAG Q 1 1555 1555 1.44 LINK ND2 ASN A 276 C1 NAG A 602 1555 1555 1.44 LINK ND2 ASN A 295 C1 NAG R 1 1555 1555 1.44 LINK ND2 ASN A 301 C1 NAG A 603 1555 1555 1.44 LINK ND2 ASN A 332 C1 NAG S 1 1555 1555 1.43 LINK ND2 ASN A 355 C1 NAG A 604 1555 1555 1.44 LINK ND2 ASN A 363 C1 NAG T 1 1555 1555 1.44 LINK ND2 ASN A 386 C1 NAG U 1 1555 1555 1.43 LINK ND2 ASN A 448 C1 NAG A 605 1555 1555 1.44 LINK ND2 ASN C 133 C1 NAG C 601 1555 1555 1.44 LINK ND2 ASN C 156 C1 NAG V 1 1555 1555 1.44 LINK ND2 ASN C 160 C1 NAG W 1 1555 1555 1.44 LINK ND2 ASN C 197 C1 NAG X 1 1555 1555 1.44 LINK ND2 ASN C 234 C1 NAG Y 1 1555 1555 1.44 LINK ND2 ASN C 262 C1 NAG Z 1 1555 1555 1.44 LINK ND2 ASN C 276 C1 NAG C 602 1555 1555 1.44 LINK ND2 ASN C 295 C1 NAG a 1 1555 1555 1.44 LINK ND2 ASN C 301 C1 NAG C 603 1555 1555 1.44 LINK ND2 ASN C 332 C1 NAG b 1 1555 1555 1.44 LINK ND2 ASN C 355 C1 NAG C 604 1555 1555 1.44 LINK ND2 ASN C 363 C1 NAG c 1 1555 1555 1.44 LINK ND2 ASN C 386 C1 NAG d 1 1555 1555 1.43 LINK ND2 ASN C 448 C1 NAG e 1 1555 1555 1.44 LINK ND2 ASN E 133 C1 NAG E 601 1555 1555 1.44 LINK ND2 ASN E 156 C1 NAG f 1 1555 1555 1.44 LINK ND2 ASN E 160 C1 NAG g 1 1555 1555 1.44 LINK ND2 ASN E 197 C1 NAG h 1 1555 1555 1.44 LINK ND2 ASN E 234 C1 NAG i 1 1555 1555 1.44 LINK ND2 ASN E 262 C1 NAG j 1 1555 1555 1.44 LINK ND2 ASN E 276 C1 NAG E 602 1555 1555 1.44 LINK ND2 ASN E 295 C1 NAG k 1 1555 1555 1.44 LINK ND2 ASN E 301 C1 NAG E 603 1555 1555 1.44 LINK ND2 ASN E 332 C1 NAG l 1 1555 1555 1.44 LINK ND2 ASN E 355 C1 NAG E 604 1555 1555 1.44 LINK ND2 ASN E 363 C1 NAG m 1 1555 1555 1.44 LINK ND2 ASN E 386 C1 NAG n 1 1555 1555 1.43 LINK ND2 ASN E 448 C1 NAG E 605 1555 1555 1.44 LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.45 LINK O4 NAG K 1 C1 NAG K 2 1555 1555 1.45 LINK O4 NAG O 1 C1 NAG O 2 1555 1555 1.45 LINK O4 NAG O 2 C1 BMA O 3 1555 1555 1.44 LINK O4 NAG P 1 C1 NAG P 2 1555 1555 1.45 LINK O4 NAG P 2 C1 BMA P 3 1555 1555 1.44 LINK O6 BMA P 3 C1 MAN P 4 1555 1555 1.45 LINK O4 NAG Q 1 C1 NAG Q 2 1555 1555 1.45 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 O6 BMA Q 3 C1 MAN Q 6 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 1.47 LINK O4 NAG S 1 C1 NAG S 2 1555 1555 1.44 LINK O4 NAG T 1 C1 NAG T 2 1555 1555 1.44 LINK O4 NAG T 2 C1 BMA T 3 1555 1555 1.44 LINK O3 BMA T 3 C1 MAN T 4 1555 1555 1.44 LINK O6 BMA T 3 C1 MAN T 5 1555 1555 1.44 LINK O4 NAG U 1 C1 NAG U 2 1555 1555 1.44 LINK O4 NAG V 1 C1 NAG V 2 1555 1555 1.45 LINK O4 NAG W 1 C1 NAG W 2 1555 1555 1.45 LINK O4 NAG X 1 C1 NAG X 2 1555 1555 1.45 LINK O4 NAG X 2 C1 BMA X 3 1555 1555 1.44 LINK O4 NAG Y 1 C1 NAG Y 2 1555 1555 1.45 LINK O4 NAG Y 2 C1 BMA Y 3 1555 1555 1.44 LINK O6 BMA Y 3 C1 MAN Y 4 1555 1555 1.44 LINK O4 NAG Z 1 C1 NAG Z 2 1555 1555 1.45 LINK O4 NAG Z 2 C1 BMA Z 3 1555 1555 1.44 LINK O3 BMA Z 3 C1 MAN Z 4 1555 1555 1.45 LINK O6 BMA Z 3 C1 MAN Z 6 1555 1555 1.44 LINK O2 MAN Z 4 C1 MAN Z 5 1555 1555 1.45 LINK O4 NAG a 1 C1 NAG a 2 1555 1555 1.45 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 c 2 C1 BMA c 3 1555 1555 1.44 LINK O3 BMA c 3 C1 MAN c 4 1555 1555 1.44 LINK O6 BMA c 3 C1 MAN c 5 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 1.45 LINK O4 NAG f 1 C1 NAG f 2 1555 1555 1.45 LINK O4 NAG f 2 C1 BMA f 3 1555 1555 1.44 LINK O4 NAG g 1 C1 NAG g 2 1555 1555 1.45 LINK O4 NAG h 1 C1 NAG h 2 1555 1555 1.45 LINK O4 NAG h 2 C1 BMA h 3 1555 1555 1.44 LINK O6 BMA h 3 C1 MAN h 4 1555 1555 1.44 LINK O4 NAG i 1 C1 NAG i 2 1555 1555 1.45 LINK O4 NAG i 2 C1 BMA i 3 1555 1555 1.44 LINK O6 BMA i 3 C1 MAN i 4 1555 1555 1.45 LINK O4 NAG j 1 C1 NAG j 2 1555 1555 1.45 LINK O4 NAG j 2 C1 BMA j 3 1555 1555 1.44 LINK O3 BMA j 3 C1 MAN j 4 1555 1555 1.44 LINK O2 MAN j 4 C1 MAN j 5 1555 1555 1.44 LINK O4 NAG k 1 C1 NAG k 2 1555 1555 1.45 LINK O4 NAG l 1 C1 NAG l 2 1555 1555 1.44 LINK O4 NAG m 1 C1 NAG m 2 1555 1555 1.44 LINK O4 NAG m 2 C1 BMA m 3 1555 1555 1.44 LINK O3 BMA m 3 C1 MAN m 4 1555 1555 1.44 LINK O6 BMA m 3 C1 MAN m 5 1555 1555 1.44 LINK O4 NAG n 1 C1 NAG n 2 1555 1555 1.44 CISPEP 1 SER L 7 PRO L 8 0 -1.43 CISPEP 2 SER M 7 PRO M 8 0 -1.31 CISPEP 3 SER N 7 PRO N 8 0 -0.69 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