HEADER VIRAL PROTEIN/IMMUNE SYSTEM 16-OCT-23 8ULT TITLE CRYO-EM STRUCTURE OF THE BG505 SOSIPV2 IN COMPLEX WITH BNAB 04_A06 TITLE 2 FABS COMPND MOL_ID: 1; COMPND 2 MOLECULE: ENVELOPE GLYCOPROTEIN GP120; 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 GP41; COMPND 8 CHAIN: B, D, F; COMPND 9 ENGINEERED: YES; COMPND 10 MOL_ID: 3; COMPND 11 MOLECULE: 04_A06 FAB HEAVY CHAIN; COMPND 12 CHAIN: H, I, J; COMPND 13 ENGINEERED: YES; COMPND 14 MOL_ID: 4; COMPND 15 MOLECULE: 04_A06 FAB 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 8ULT 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 04_A06 FABS JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.80 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : SERIALEM, CRYOSPARC, UCSF CHIMERAX, REMARK 3 PHENIX, CRYOSPARC, CRYOSPARC, CRYOSPARC 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) : 3.800 REMARK 3 NUMBER OF PARTICLES : 19388 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 8ULT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-OCT-23. REMARK 100 THE DEPOSITION ID IS D_1000278143. 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 04_ REMARK 245 A06 FABS REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 2.50 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 : 2446 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: 12-MERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: 12-MERIC REMARK 350 SOFTWARE USED: PISA 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 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 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 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 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 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 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 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 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 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 ASP F 664 REMARK 465 SER 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 SER 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 SER 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 TYR L 1 REMARK 465 GLY L 109 REMARK 465 THR L 110 REMARK 465 VAL L 111 REMARK 465 ALA L 112 REMARK 465 ALA L 113 REMARK 465 PRO L 114 REMARK 465 SER L 115 REMARK 465 VAL L 116 REMARK 465 PHE L 117 REMARK 465 ILE L 118 REMARK 465 PHE L 119 REMARK 465 PRO L 120 REMARK 465 PRO L 121 REMARK 465 SER L 122 REMARK 465 ASP L 123 REMARK 465 GLU L 124 REMARK 465 GLN L 125 REMARK 465 LEU L 126 REMARK 465 LYS L 127 REMARK 465 SER L 128 REMARK 465 GLY L 129 REMARK 465 THR L 130 REMARK 465 ALA L 131 REMARK 465 SER L 132 REMARK 465 VAL L 133 REMARK 465 VAL L 134 REMARK 465 CYS L 135 REMARK 465 LEU L 136 REMARK 465 LEU L 137 REMARK 465 ASN L 138 REMARK 465 ASN L 139 REMARK 465 PHE L 140 REMARK 465 TYR L 141 REMARK 465 PRO L 142 REMARK 465 ARG L 143 REMARK 465 GLU L 144 REMARK 465 ALA L 145 REMARK 465 LYS L 146 REMARK 465 VAL L 147 REMARK 465 GLN L 148 REMARK 465 TRP L 149 REMARK 465 LYS L 150 REMARK 465 VAL L 151 REMARK 465 ASP L 152 REMARK 465 ASN L 153 REMARK 465 ALA L 154 REMARK 465 LEU L 155 REMARK 465 GLN L 156 REMARK 465 SER L 157 REMARK 465 GLY L 158 REMARK 465 ASN L 159 REMARK 465 SER L 160 REMARK 465 GLN L 161 REMARK 465 GLU L 162 REMARK 465 SER L 163 REMARK 465 VAL L 164 REMARK 465 THR L 165 REMARK 465 GLU L 166 REMARK 465 GLN L 167 REMARK 465 ASP L 168 REMARK 465 SER L 169 REMARK 465 LYS L 170 REMARK 465 ASP L 171 REMARK 465 SER L 172 REMARK 465 THR L 173 REMARK 465 TYR L 174 REMARK 465 SER L 175 REMARK 465 LEU L 176 REMARK 465 SER L 177 REMARK 465 SER L 178 REMARK 465 THR L 179 REMARK 465 LEU L 180 REMARK 465 THR L 181 REMARK 465 LEU L 182 REMARK 465 SER L 183 REMARK 465 LYS L 184 REMARK 465 ALA L 185 REMARK 465 ASP L 186 REMARK 465 TYR L 187 REMARK 465 GLU L 188 REMARK 465 LYS L 189 REMARK 465 HIS L 190 REMARK 465 LYS L 191 REMARK 465 VAL L 192 REMARK 465 TYR L 193 REMARK 465 ALA L 194 REMARK 465 CYS L 195 REMARK 465 GLU L 196 REMARK 465 VAL L 197 REMARK 465 THR L 198 REMARK 465 HIS L 199 REMARK 465 GLN L 200 REMARK 465 GLY L 201 REMARK 465 LEU L 202 REMARK 465 SER L 203 REMARK 465 SER L 204 REMARK 465 PRO L 205 REMARK 465 VAL L 206 REMARK 465 THR L 207 REMARK 465 LYS L 208 REMARK 465 SER L 209 REMARK 465 PHE L 210 REMARK 465 ASN L 211 REMARK 465 ARG L 212 REMARK 465 GLY L 213 REMARK 465 GLU L 214 REMARK 465 CYS L 215 REMARK 465 TYR M 1 REMARK 465 GLY M 109 REMARK 465 THR M 110 REMARK 465 VAL M 111 REMARK 465 ALA M 112 REMARK 465 ALA M 113 REMARK 465 PRO M 114 REMARK 465 SER M 115 REMARK 465 VAL M 116 REMARK 465 PHE M 117 REMARK 465 ILE M 118 REMARK 465 PHE M 119 REMARK 465 PRO M 120 REMARK 465 PRO M 121 REMARK 465 SER M 122 REMARK 465 ASP M 123 REMARK 465 GLU M 124 REMARK 465 GLN M 125 REMARK 465 LEU M 126 REMARK 465 LYS M 127 REMARK 465 SER M 128 REMARK 465 GLY M 129 REMARK 465 THR M 130 REMARK 465 ALA M 131 REMARK 465 SER M 132 REMARK 465 VAL M 133 REMARK 465 VAL M 134 REMARK 465 CYS M 135 REMARK 465 LEU M 136 REMARK 465 LEU M 137 REMARK 465 ASN M 138 REMARK 465 ASN M 139 REMARK 465 PHE M 140 REMARK 465 TYR M 141 REMARK 465 PRO M 142 REMARK 465 ARG M 143 REMARK 465 GLU M 144 REMARK 465 ALA M 145 REMARK 465 LYS M 146 REMARK 465 VAL M 147 REMARK 465 GLN M 148 REMARK 465 TRP M 149 REMARK 465 LYS M 150 REMARK 465 VAL M 151 REMARK 465 ASP M 152 REMARK 465 ASN M 153 REMARK 465 ALA M 154 REMARK 465 LEU M 155 REMARK 465 GLN M 156 REMARK 465 SER M 157 REMARK 465 GLY M 158 REMARK 465 ASN M 159 REMARK 465 SER M 160 REMARK 465 GLN M 161 REMARK 465 GLU M 162 REMARK 465 SER M 163 REMARK 465 VAL M 164 REMARK 465 THR M 165 REMARK 465 GLU M 166 REMARK 465 GLN M 167 REMARK 465 ASP M 168 REMARK 465 SER M 169 REMARK 465 LYS M 170 REMARK 465 ASP M 171 REMARK 465 SER M 172 REMARK 465 THR M 173 REMARK 465 TYR M 174 REMARK 465 SER M 175 REMARK 465 LEU M 176 REMARK 465 SER M 177 REMARK 465 SER M 178 REMARK 465 THR M 179 REMARK 465 LEU M 180 REMARK 465 THR M 181 REMARK 465 LEU M 182 REMARK 465 SER M 183 REMARK 465 LYS M 184 REMARK 465 ALA M 185 REMARK 465 ASP M 186 REMARK 465 TYR M 187 REMARK 465 GLU M 188 REMARK 465 LYS M 189 REMARK 465 HIS M 190 REMARK 465 LYS M 191 REMARK 465 VAL M 192 REMARK 465 TYR M 193 REMARK 465 ALA M 194 REMARK 465 CYS M 195 REMARK 465 GLU M 196 REMARK 465 VAL M 197 REMARK 465 THR M 198 REMARK 465 HIS M 199 REMARK 465 GLN M 200 REMARK 465 GLY M 201 REMARK 465 LEU M 202 REMARK 465 SER M 203 REMARK 465 SER M 204 REMARK 465 PRO M 205 REMARK 465 VAL M 206 REMARK 465 THR M 207 REMARK 465 LYS M 208 REMARK 465 SER M 209 REMARK 465 PHE M 210 REMARK 465 ASN M 211 REMARK 465 ARG M 212 REMARK 465 GLY M 213 REMARK 465 GLU M 214 REMARK 465 CYS M 215 REMARK 465 TYR N 1 REMARK 465 GLY N 109 REMARK 465 THR N 110 REMARK 465 VAL N 111 REMARK 465 ALA N 112 REMARK 465 ALA N 113 REMARK 465 PRO N 114 REMARK 465 SER N 115 REMARK 465 VAL N 116 REMARK 465 PHE N 117 REMARK 465 ILE N 118 REMARK 465 PHE N 119 REMARK 465 PRO N 120 REMARK 465 PRO N 121 REMARK 465 SER N 122 REMARK 465 ASP N 123 REMARK 465 GLU N 124 REMARK 465 GLN N 125 REMARK 465 LEU N 126 REMARK 465 LYS N 127 REMARK 465 SER N 128 REMARK 465 GLY N 129 REMARK 465 THR N 130 REMARK 465 ALA N 131 REMARK 465 SER N 132 REMARK 465 VAL N 133 REMARK 465 VAL N 134 REMARK 465 CYS N 135 REMARK 465 LEU N 136 REMARK 465 LEU N 137 REMARK 465 ASN N 138 REMARK 465 ASN N 139 REMARK 465 PHE N 140 REMARK 465 TYR N 141 REMARK 465 PRO N 142 REMARK 465 ARG N 143 REMARK 465 GLU N 144 REMARK 465 ALA N 145 REMARK 465 LYS N 146 REMARK 465 VAL N 147 REMARK 465 GLN N 148 REMARK 465 TRP N 149 REMARK 465 LYS N 150 REMARK 465 VAL N 151 REMARK 465 ASP N 152 REMARK 465 ASN N 153 REMARK 465 ALA N 154 REMARK 465 LEU N 155 REMARK 465 GLN N 156 REMARK 465 SER N 157 REMARK 465 GLY N 158 REMARK 465 ASN N 159 REMARK 465 SER N 160 REMARK 465 GLN N 161 REMARK 465 GLU N 162 REMARK 465 SER N 163 REMARK 465 VAL N 164 REMARK 465 THR N 165 REMARK 465 GLU N 166 REMARK 465 GLN N 167 REMARK 465 ASP N 168 REMARK 465 SER N 169 REMARK 465 LYS N 170 REMARK 465 ASP N 171 REMARK 465 SER N 172 REMARK 465 THR N 173 REMARK 465 TYR N 174 REMARK 465 SER N 175 REMARK 465 LEU N 176 REMARK 465 SER N 177 REMARK 465 SER N 178 REMARK 465 THR N 179 REMARK 465 LEU N 180 REMARK 465 THR N 181 REMARK 465 LEU N 182 REMARK 465 SER N 183 REMARK 465 LYS N 184 REMARK 465 ALA N 185 REMARK 465 ASP N 186 REMARK 465 TYR N 187 REMARK 465 GLU N 188 REMARK 465 LYS N 189 REMARK 465 HIS N 190 REMARK 465 LYS N 191 REMARK 465 VAL N 192 REMARK 465 TYR N 193 REMARK 465 ALA N 194 REMARK 465 CYS N 195 REMARK 465 GLU N 196 REMARK 465 VAL N 197 REMARK 465 THR N 198 REMARK 465 HIS N 199 REMARK 465 GLN N 200 REMARK 465 GLY N 201 REMARK 465 LEU N 202 REMARK 465 SER N 203 REMARK 465 SER N 204 REMARK 465 PRO N 205 REMARK 465 VAL N 206 REMARK 465 THR N 207 REMARK 465 LYS N 208 REMARK 465 SER N 209 REMARK 465 PHE N 210 REMARK 465 ASN N 211 REMARK 465 ARG N 212 REMARK 465 GLY N 213 REMARK 465 GLU N 214 REMARK 465 CYS N 215 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 370 CG CD OE1 OE2 REMARK 470 LEU B 566 CG CD1 CD2 REMARK 470 LYS B 567 CG CD CE NZ REMARK 470 LEU B 568 CG CD1 CD2 REMARK 470 ASP C 148 CG OD1 OD2 REMARK 470 ASP C 149 CG OD1 OD2 REMARK 470 GLU C 370 CG CD OE1 OE2 REMARK 470 LEU D 566 CG CD1 CD2 REMARK 470 LYS D 567 CG CD CE NZ REMARK 470 LEU D 568 CG CD1 CD2 REMARK 470 ASP E 148 CG OD1 OD2 REMARK 470 ASP E 149 CG OD1 OD2 REMARK 470 GLU E 370 CG CD OE1 OE2 REMARK 470 LEU F 566 CG CD1 CD2 REMARK 470 LYS F 567 CG CD CE NZ REMARK 470 LEU F 568 CG CD1 CD2 REMARK 470 ARG H 3 CG CD NE CZ NH1 NH2 REMARK 470 ARG H 32 CG CD NE CZ NH1 NH2 REMARK 470 ARG H 34 CG CD NE CZ NH1 NH2 REMARK 470 LYS H 58 CG CD CE NZ REMARK 470 ARG H 62 CG CD NE CZ NH1 NH2 REMARK 470 GLN H 64 CG CD OE1 NE2 REMARK 470 ASP H 99 CG OD1 OD2 REMARK 470 ASP H 100 CG OD1 OD2 REMARK 470 ARG I 3 CG CD NE CZ NH1 NH2 REMARK 470 ARG I 32 CG CD NE CZ NH1 NH2 REMARK 470 ARG I 34 CG CD NE CZ NH1 NH2 REMARK 470 LYS I 58 CG CD CE NZ REMARK 470 ARG I 62 CG CD NE CZ NH1 NH2 REMARK 470 GLN I 64 CG CD OE1 NE2 REMARK 470 ASP I 99 CG OD1 OD2 REMARK 470 ASP I 100 CG OD1 OD2 REMARK 470 ARG J 3 CG CD NE CZ NH1 NH2 REMARK 470 ARG J 32 CG CD NE CZ NH1 NH2 REMARK 470 ARG J 34 CG CD NE CZ NH1 NH2 REMARK 470 LYS J 58 CG CD CE NZ REMARK 470 ARG J 62 CG CD NE CZ NH1 NH2 REMARK 470 GLN J 64 CG CD OE1 NE2 REMARK 470 ASP J 99 CG OD1 OD2 REMARK 470 ASP J 100 CG OD1 OD2 REMARK 470 GLN L 3 CG CD OE1 NE2 REMARK 470 GLU L 24 CG CD OE1 OE2 REMARK 470 GLN M 3 CG CD OE1 NE2 REMARK 470 GLU M 24 CG CD OE1 OE2 REMARK 470 GLN N 3 CG CD OE1 NE2 REMARK 470 GLU N 24 CG CD OE1 OE2 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 OG1 THR F 627 OE1 GLN F 630 2.18 REMARK 500 OD2 ASP E 113 NH1 ARG E 429 2.18 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 A 296 CA - CB - SG ANGL. DEV. = 10.1 DEGREES REMARK 500 CYS E 296 CA - CB - SG ANGL. DEV. = 9.6 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 ASN A 88 -0.05 73.80 REMARK 500 PRO A 118 49.27 -82.76 REMARK 500 LEU A 122 50.10 -91.49 REMARK 500 PRO A 240 44.10 -82.27 REMARK 500 SER A 241 42.23 -141.76 REMARK 500 ASN A 262 19.58 58.03 REMARK 500 TRP A 427 -1.95 70.28 REMARK 500 ALA B 525 33.58 -98.01 REMARK 500 THR B 606 -168.89 -128.81 REMARK 500 SER B 612 -4.45 67.48 REMARK 500 ALA B 662 -77.00 -93.10 REMARK 500 ASN C 88 -3.67 75.58 REMARK 500 LEU C 122 52.22 -90.77 REMARK 500 ASN C 195 57.98 -97.66 REMARK 500 SER C 274 119.21 -161.38 REMARK 500 TRP C 427 -1.96 66.50 REMARK 500 ALA D 525 31.44 -96.51 REMARK 500 ALA D 662 -61.30 -90.60 REMARK 500 ASN E 94 100.79 -165.13 REMARK 500 PRO E 118 49.31 -87.22 REMARK 500 LEU E 122 52.58 -91.03 REMARK 500 ALA E 281 -44.74 -150.27 REMARK 500 PHE E 353 -111.45 -95.63 REMARK 500 PHE E 376 143.86 -170.77 REMARK 500 ALA F 525 32.55 -98.20 REMARK 500 SER F 612 -4.39 69.31 REMARK 500 GLU H 35G 59.70 -94.05 REMARK 500 LEU H 48 -61.19 -93.51 REMARK 500 LEU L 47 -61.73 -99.80 REMARK 500 ALA L 51 -5.84 76.81 REMARK 500 HIS L 52 -0.82 -144.06 REMARK 500 ASN L 77 61.75 36.20 REMARK 500 PHE L 91 -118.83 53.28 REMARK 500 ALA M 51 -13.93 72.60 REMARK 500 ASN M 77 63.85 36.00 REMARK 500 PHE M 91 -120.84 53.95 REMARK 500 ALA N 51 -7.05 76.85 REMARK 500 HIS N 52 10.50 -140.32 REMARK 500 ASN N 77 63.99 35.60 REMARK 500 PHE N 91 -120.75 52.72 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 ARG C 500 0.12 SIDE CHAIN REMARK 500 ARG E 350 0.11 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-42365 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF THE BG505 SOSIPV2 IN COMPLEX WITH BNAB 04_A06 REMARK 900 FABS DBREF 8ULT A 33 504 UNP Q2N0S6 Q2N0S6_9HIV1 32 501 DBREF 8ULT B 512 664 UNP Q2N0S5 Q2N0S5_9HIV1 509 661 DBREF 8ULT C 33 504 UNP Q2N0S6 Q2N0S6_9HIV1 32 501 DBREF 8ULT D 512 664 UNP Q2N0S5 Q2N0S5_9HIV1 509 661 DBREF 8ULT E 33 504 UNP Q2N0S6 Q2N0S6_9HIV1 32 501 DBREF 8ULT F 512 664 UNP Q2N0S5 Q2N0S5_9HIV1 509 661 DBREF 8ULT H 1 225 PDB 8ULT 8ULT 1 225 DBREF 8ULT I 1 225 PDB 8ULT 8ULT 1 225 DBREF 8ULT J 1 225 PDB 8ULT 8ULT 1 225 DBREF 8ULT L 1 215 PDB 8ULT 8ULT 1 215 DBREF 8ULT M 1 215 PDB 8ULT 8ULT 1 215 DBREF 8ULT N 1 215 PDB 8ULT 8ULT 1 215 SEQADV 8ULT ASN A 332 UNP Q2N0S6 THR 330 CONFLICT SEQADV 8ULT CYS A 501 UNP Q2N0S6 ALA 498 CONFLICT SEQADV 8ULT VAL A 505 UNP Q2N0S6 EXPRESSION TAG SEQADV 8ULT VAL A 506 UNP Q2N0S6 EXPRESSION TAG SEQADV 8ULT GLY A 507 UNP Q2N0S6 EXPRESSION TAG SEQADV 8ULT ARG A 508 UNP Q2N0S6 EXPRESSION TAG SEQADV 8ULT ARG A 509 UNP Q2N0S6 EXPRESSION TAG SEQADV 8ULT ARG A 510 UNP Q2N0S6 EXPRESSION TAG SEQADV 8ULT ARG A 511 UNP Q2N0S6 EXPRESSION TAG SEQADV 8ULT ARG A 512 UNP Q2N0S6 EXPRESSION TAG SEQADV 8ULT ARG A 513 UNP Q2N0S6 EXPRESSION TAG SEQADV 8ULT PRO B 559 UNP Q2N0S5 ILE 556 ENGINEERED MUTATION SEQADV 8ULT CYS B 605 UNP Q2N0S5 THR 602 ENGINEERED MUTATION SEQADV 8ULT ASN C 332 UNP Q2N0S6 THR 330 CONFLICT SEQADV 8ULT CYS C 501 UNP Q2N0S6 ALA 498 CONFLICT SEQADV 8ULT VAL C 505 UNP Q2N0S6 EXPRESSION TAG SEQADV 8ULT VAL C 506 UNP Q2N0S6 EXPRESSION TAG SEQADV 8ULT GLY C 507 UNP Q2N0S6 EXPRESSION TAG SEQADV 8ULT ARG C 508 UNP Q2N0S6 EXPRESSION TAG SEQADV 8ULT ARG C 509 UNP Q2N0S6 EXPRESSION TAG SEQADV 8ULT ARG C 510 UNP Q2N0S6 EXPRESSION TAG SEQADV 8ULT ARG C 511 UNP Q2N0S6 EXPRESSION TAG SEQADV 8ULT ARG C 512 UNP Q2N0S6 EXPRESSION TAG SEQADV 8ULT ARG C 513 UNP Q2N0S6 EXPRESSION TAG SEQADV 8ULT PRO D 559 UNP Q2N0S5 ILE 556 ENGINEERED MUTATION SEQADV 8ULT CYS D 605 UNP Q2N0S5 THR 602 ENGINEERED MUTATION SEQADV 8ULT ASN E 332 UNP Q2N0S6 THR 330 CONFLICT SEQADV 8ULT CYS E 501 UNP Q2N0S6 ALA 498 CONFLICT SEQADV 8ULT VAL E 505 UNP Q2N0S6 EXPRESSION TAG SEQADV 8ULT VAL E 506 UNP Q2N0S6 EXPRESSION TAG SEQADV 8ULT GLY E 507 UNP Q2N0S6 EXPRESSION TAG SEQADV 8ULT ARG E 508 UNP Q2N0S6 EXPRESSION TAG SEQADV 8ULT ARG E 509 UNP Q2N0S6 EXPRESSION TAG SEQADV 8ULT ARG E 510 UNP Q2N0S6 EXPRESSION TAG SEQADV 8ULT ARG E 511 UNP Q2N0S6 EXPRESSION TAG SEQADV 8ULT ARG E 512 UNP Q2N0S6 EXPRESSION TAG SEQADV 8ULT ARG E 513 UNP Q2N0S6 EXPRESSION TAG SEQADV 8ULT PRO F 559 UNP Q2N0S5 ILE 556 ENGINEERED MUTATION SEQADV 8ULT 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 245 SER VAL ARG LEU ASP GLN SER GLY THR ALA VAL LYS LYS SEQRES 2 H 245 PRO GLY ALA SER VAL ARG VAL SER CYS ARG ALA PRO ASP SEQRES 3 H 245 SER PHE THR VAL TYR ARG PRO ARG LEU SER ALA TYR PHE SEQRES 4 H 245 ILE GLY GLU PHE ASN ILE HIS TRP LEU ARG GLN ALA PRO SEQRES 5 H 245 GLY GLN GLY LEU GLU TRP LEU GLY PHE VAL ASN ILE PHE SEQRES 6 H 245 ARG GLY ALA VAL LYS TYR SER SER ARG PHE GLN GLY ARG SEQRES 7 H 245 ILE THR ILE THR ARG ASP THR SER SER GLU THR SER TYR SEQRES 8 H 245 LEU ASP LEU GLY ALA LEU LYS ALA ASP ASP THR ALA THR SEQRES 9 H 245 TYR TYR CYS ALA TRP ASP LYS ASN VAL ASP ASP ASN PRO SEQRES 10 H 245 TRP ARG LEU ASP SER TRP GLY GLN GLY THR LEU VAL ILE SEQRES 11 H 245 VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO SEQRES 12 H 245 LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA SEQRES 13 H 245 ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO SEQRES 14 H 245 VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY SEQRES 15 H 245 VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU SEQRES 16 H 245 TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SER SEQRES 17 H 245 LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS SEQRES 18 H 245 PRO SER ASN THR LYS VAL ASP LYS ARG VAL GLU PRO LYS SEQRES 19 H 245 SER CYS ASP LYS THR HIS HIS HIS HIS HIS HIS SEQRES 1 I 245 SER VAL ARG LEU ASP GLN SER GLY THR ALA VAL LYS LYS SEQRES 2 I 245 PRO GLY ALA SER VAL ARG VAL SER CYS ARG ALA PRO ASP SEQRES 3 I 245 SER PHE THR VAL TYR ARG PRO ARG LEU SER ALA TYR PHE SEQRES 4 I 245 ILE GLY GLU PHE ASN ILE HIS TRP LEU ARG GLN ALA PRO SEQRES 5 I 245 GLY GLN GLY LEU GLU TRP LEU GLY PHE VAL ASN ILE PHE SEQRES 6 I 245 ARG GLY ALA VAL LYS TYR SER SER ARG PHE GLN GLY ARG SEQRES 7 I 245 ILE THR ILE THR ARG ASP THR SER SER GLU THR SER TYR SEQRES 8 I 245 LEU ASP LEU GLY ALA LEU LYS ALA ASP ASP THR ALA THR SEQRES 9 I 245 TYR TYR CYS ALA TRP ASP LYS ASN VAL ASP ASP ASN PRO SEQRES 10 I 245 TRP ARG LEU ASP SER TRP GLY GLN GLY THR LEU VAL ILE SEQRES 11 I 245 VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO SEQRES 12 I 245 LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA SEQRES 13 I 245 ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO SEQRES 14 I 245 VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY SEQRES 15 I 245 VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU SEQRES 16 I 245 TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SER SEQRES 17 I 245 LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS SEQRES 18 I 245 PRO SER ASN THR LYS VAL ASP LYS ARG VAL GLU PRO LYS SEQRES 19 I 245 SER CYS ASP LYS THR HIS HIS HIS HIS HIS HIS SEQRES 1 J 245 SER VAL ARG LEU ASP GLN SER GLY THR ALA VAL LYS LYS SEQRES 2 J 245 PRO GLY ALA SER VAL ARG VAL SER CYS ARG ALA PRO ASP SEQRES 3 J 245 SER PHE THR VAL TYR ARG PRO ARG LEU SER ALA TYR PHE SEQRES 4 J 245 ILE GLY GLU PHE ASN ILE HIS TRP LEU ARG GLN ALA PRO SEQRES 5 J 245 GLY GLN GLY LEU GLU TRP LEU GLY PHE VAL ASN ILE PHE SEQRES 6 J 245 ARG GLY ALA VAL LYS TYR SER SER ARG PHE GLN GLY ARG SEQRES 7 J 245 ILE THR ILE THR ARG ASP THR SER SER GLU THR SER TYR SEQRES 8 J 245 LEU ASP LEU GLY ALA LEU LYS ALA ASP ASP THR ALA THR SEQRES 9 J 245 TYR TYR CYS ALA TRP ASP LYS ASN VAL ASP ASP ASN PRO SEQRES 10 J 245 TRP ARG LEU ASP SER TRP GLY GLN GLY THR LEU VAL ILE SEQRES 11 J 245 VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO SEQRES 12 J 245 LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA SEQRES 13 J 245 ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO SEQRES 14 J 245 VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY SEQRES 15 J 245 VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU SEQRES 16 J 245 TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SER SEQRES 17 J 245 LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS SEQRES 18 J 245 PRO SER ASN THR LYS VAL ASP LYS ARG VAL GLU PRO LYS SEQRES 19 J 245 SER CYS ASP LYS THR HIS HIS HIS HIS HIS HIS SEQRES 1 L 211 TYR ILE GLN VAL THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 L 211 SER ILE GLY ASP THR ILE THR VAL ALA CYS GLU VAL SER SEQRES 3 L 211 GLN ASP VAL GLY TRP ALA VAL ASN TRP TYR HIS GLN ARG SEQRES 4 L 211 PRO GLY ARG PRO PRO TYR ASN LEU ILE TYR THR ALA HIS SEQRES 5 L 211 ASN LEU ALA PRO GLY VAL ALA SER ARG PHE ARG GLY SER SEQRES 6 L 211 ARG VAL GLY THR TYR PHE THR LEU THR ILE ASN ASN LEU SEQRES 7 L 211 LEU PRO GLU ASP VAL GLY THR TYR TYR CYS GLN VAL PHE SEQRES 8 L 211 ASP SER PHE ALA PRO GLY GLY THR ARG VAL ASP LEU ARG SEQRES 9 L 211 GLY THR VAL ALA ALA PRO SER VAL PHE ILE PHE PRO PRO SEQRES 10 L 211 SER ASP GLU GLN LEU LYS SER GLY THR ALA SER VAL VAL SEQRES 11 L 211 CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU ALA LYS VAL SEQRES 12 L 211 GLN TRP LYS VAL ASP ASN ALA LEU GLN SER GLY ASN SER SEQRES 13 L 211 GLN GLU SER VAL THR GLU GLN ASP SER LYS ASP SER THR SEQRES 14 L 211 TYR SER LEU SER SER THR LEU THR LEU SER LYS ALA ASP SEQRES 15 L 211 TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU VAL THR HIS SEQRES 16 L 211 GLN GLY LEU SER SER PRO VAL THR LYS SER PHE ASN ARG SEQRES 17 L 211 GLY GLU CYS SEQRES 1 M 211 TYR ILE GLN VAL THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 M 211 SER ILE GLY ASP THR ILE THR VAL ALA CYS GLU VAL SER SEQRES 3 M 211 GLN ASP VAL GLY TRP ALA VAL ASN TRP TYR HIS GLN ARG SEQRES 4 M 211 PRO GLY ARG PRO PRO TYR ASN LEU ILE TYR THR ALA HIS SEQRES 5 M 211 ASN LEU ALA PRO GLY VAL ALA SER ARG PHE ARG GLY SER SEQRES 6 M 211 ARG VAL GLY THR TYR PHE THR LEU THR ILE ASN ASN LEU SEQRES 7 M 211 LEU PRO GLU ASP VAL GLY THR TYR TYR CYS GLN VAL PHE SEQRES 8 M 211 ASP SER PHE ALA PRO GLY GLY THR ARG VAL ASP LEU ARG SEQRES 9 M 211 GLY THR VAL ALA ALA PRO SER VAL PHE ILE PHE PRO PRO SEQRES 10 M 211 SER ASP GLU GLN LEU LYS SER GLY THR ALA SER VAL VAL SEQRES 11 M 211 CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU ALA LYS VAL SEQRES 12 M 211 GLN TRP LYS VAL ASP ASN ALA LEU GLN SER GLY ASN SER SEQRES 13 M 211 GLN GLU SER VAL THR GLU GLN ASP SER LYS ASP SER THR SEQRES 14 M 211 TYR SER LEU SER SER THR LEU THR LEU SER LYS ALA ASP SEQRES 15 M 211 TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU VAL THR HIS SEQRES 16 M 211 GLN GLY LEU SER SER PRO VAL THR LYS SER PHE ASN ARG SEQRES 17 M 211 GLY GLU CYS SEQRES 1 N 211 TYR ILE GLN VAL THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 N 211 SER ILE GLY ASP THR ILE THR VAL ALA CYS GLU VAL SER SEQRES 3 N 211 GLN ASP VAL GLY TRP ALA VAL ASN TRP TYR HIS GLN ARG SEQRES 4 N 211 PRO GLY ARG PRO PRO TYR ASN LEU ILE TYR THR ALA HIS SEQRES 5 N 211 ASN LEU ALA PRO GLY VAL ALA SER ARG PHE ARG GLY SER SEQRES 6 N 211 ARG VAL GLY THR TYR PHE THR LEU THR ILE ASN ASN LEU SEQRES 7 N 211 LEU PRO GLU ASP VAL GLY THR TYR TYR CYS GLN VAL PHE SEQRES 8 N 211 ASP SER PHE ALA PRO GLY GLY THR ARG VAL ASP LEU ARG SEQRES 9 N 211 GLY THR VAL ALA ALA PRO SER VAL PHE ILE PHE PRO PRO SEQRES 10 N 211 SER ASP GLU GLN LEU LYS SER GLY THR ALA SER VAL VAL SEQRES 11 N 211 CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU ALA LYS VAL SEQRES 12 N 211 GLN TRP LYS VAL ASP ASN ALA LEU GLN SER GLY ASN SER SEQRES 13 N 211 GLN GLU SER VAL THR GLU GLN ASP SER LYS ASP SER THR SEQRES 14 N 211 TYR SER LEU SER SER THR LEU THR LEU SER LYS ALA ASP SEQRES 15 N 211 TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU VAL THR HIS SEQRES 16 N 211 GLN GLY LEU SER SER PRO VAL THR LYS SER PHE ASN ARG SEQRES 17 N 211 GLY GLU CYS HET NAG G 1 14 HET NAG G 2 14 HET BMA G 3 11 HET NAG K 1 14 HET NAG K 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 NAG R 1 14 HET NAG R 2 14 HET NAG S 1 14 HET NAG S 2 14 HET BMA S 3 11 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 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 BMA d 3 11 HET NAG e 1 14 HET NAG e 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 A 606 14 HET NAG A 607 14 HET NAG A 608 14 HET NAG A 609 14 HET NAG A 610 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 C 608 14 HET NAG C 609 14 HET NAG C 610 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 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BMA BETA-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 FORMUL 13 NAG 67(C8 H15 N O6) FORMUL 13 BMA 3(C6 H12 O6) HELIX 1 AA1 ALA A 70 CYS A 74 5 5 HELIX 2 AA2 ASN A 98 SER A 115 1 18 HELIX 3 AA3 LEU A 122 CYS A 126 5 5 HELIX 4 AA4 THR A 147 ARG A 151 5 5 HELIX 5 AA5 ASN A 195 ASN A 197 5 3 HELIX 6 AA6 LYS A 335 ARG A 350 1 16 HELIX 7 AA7 ASP A 368 THR A 373 1 6 HELIX 8 AA8 ASN A 425 ARG A 429 5 5 HELIX 9 AA9 ASP A 474 SER A 481 1 8 HELIX 10 AB1 THR B 529 THR B 536 1 8 HELIX 11 AB2 THR B 536 ASN B 543 1 8 HELIX 12 AB3 THR B 569 TRP B 596 1 28 HELIX 13 AB4 ASN B 618 ASN B 625 1 8 HELIX 14 AB5 THR B 627 GLU B 634 1 8 HELIX 15 AB6 TYR B 638 LEU B 663 1 26 HELIX 16 AB7 ASN C 98 SER C 115 1 18 HELIX 17 AB8 THR C 147 ARG C 151 5 5 HELIX 18 AB9 LYS C 335 ARG C 350 1 16 HELIX 19 AC1 ASP C 368 THR C 373 1 6 HELIX 20 AC2 ASN C 425 ARG C 429 5 5 HELIX 21 AC3 ASP C 474 SER C 481 1 8 HELIX 22 AC4 THR D 529 THR D 536 1 8 HELIX 23 AC5 THR D 536 ARG D 542 1 7 HELIX 24 AC6 THR D 569 TRP D 596 1 28 HELIX 25 AC7 ASN D 618 ASN D 625 1 8 HELIX 26 AC8 THR D 627 GLU D 634 1 8 HELIX 27 AC9 TYR D 638 LEU D 663 1 26 HELIX 28 AD1 ALA E 70 CYS E 74 5 5 HELIX 29 AD2 ASN E 98 SER E 115 1 18 HELIX 30 AD3 THR E 147 ARG E 151 5 5 HELIX 31 AD4 ASN E 195 THR E 198 5 4 HELIX 32 AD5 LYS E 335 PHE E 353 1 19 HELIX 33 AD6 ASP E 368 THR E 373 1 6 HELIX 34 AD7 ASN E 425 ARG E 429 5 5 HELIX 35 AD8 ASP E 474 SER E 481 1 8 HELIX 36 AD9 THR F 529 THR F 536 1 8 HELIX 37 AE1 THR F 536 ARG F 542 1 7 HELIX 38 AE2 THR F 569 TRP F 596 1 28 HELIX 39 AE3 ASN F 618 ASN F 625 1 8 HELIX 40 AE4 THR F 627 GLU F 634 1 8 HELIX 41 AE5 ILE F 635 ASN F 637 5 3 HELIX 42 AE6 TYR F 638 LEU F 663 1 26 HELIX 43 AE7 LYS H 83 THR H 87 5 5 HELIX 44 AE8 LYS I 83 THR I 87 5 5 HELIX 45 AE9 LYS J 83 THR J 87 5 5 HELIX 46 AF1 LEU L 79 VAL L 83 5 5 HELIX 47 AF2 LEU M 79 VAL M 83 5 5 HELIX 48 AF3 LEU 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 CYS A 54 O VAL A 75 SHEET 3 AA3 3 HIS A 216 CYS A 218 -1 O HIS A 216 N ALA A 55 SHEET 1 AA4 2 GLU A 91 ASN A 94 0 SHEET 2 AA4 2 THR A 236 CYS A 239 -1 O CYS A 239 N GLU A 91 SHEET 1 AA5 5 LYS A 169 TYR A 177 0 SHEET 2 AA5 5 LEU A 154 THR A 162 -1 N CYS A 157 O SER A 174 SHEET 3 AA5 5 LEU A 129 ASN A 133 -1 N THR A 132 O ASN A 156 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 3 SER A 199 GLN A 203 0 SHEET 2 AA6 3 GLY A 431 TYR A 435 1 O ALA A 433 N THR A 202 SHEET 3 AA6 3 ILE A 423 ILE A 424 -1 N ILE A 424 O MET A 434 SHEET 1 AA7 7 LEU A 259 LEU A 261 0 SHEET 2 AA7 7 ARG A 444 ARG A 456 -1 O THR A 450 N LEU A 260 SHEET 3 AA7 7 ILE A 284 THR A 297 -1 N ILE A 284 O LEU A 454 SHEET 4 AA7 7 HIS A 330 SER A 334 -1 O ASN A 332 N ASN A 295 SHEET 5 AA7 7 SER A 413 LYS A 421 -1 O ILE A 414 N VAL A 333 SHEET 6 AA7 7 GLU A 381 CYS A 385 -1 N TYR A 384 O ARG A 419 SHEET 7 AA7 7 HIS A 374 CYS A 378 -1 N HIS A 374 O CYS A 385 SHEET 1 AA8 6 MET A 271 ARG A 273 0 SHEET 2 AA8 6 ILE A 284 THR A 297 -1 O LEU A 285 N ARG A 273 SHEET 3 AA8 6 ARG A 444 ARG A 456 -1 O LEU A 454 N ILE A 284 SHEET 4 AA8 6 THR A 465 PRO A 470 -1 O ARG A 469 N THR A 455 SHEET 5 AA8 6 ILE A 358 PHE A 361 1 N ILE A 358 O GLU A 466 SHEET 6 AA8 6 THR A 394 TRP A 395 -1 O TRP A 395 N ILE A 359 SHEET 1 AA9 2 ARG A 304 GLY A 312 0 SHEET 2 AA9 2 GLN A 315 THR A 320 -1 O PHE A 317 N ILE A 309 SHEET 1 AB1 3 LEU C 494 THR C 499 0 SHEET 2 AB1 3 TRP C 35 TYR C 40 -1 N TRP C 35 O THR C 499 SHEET 3 AB1 3 ILE D 603 PRO D 609 -1 O CYS D 604 N VAL C 38 SHEET 1 AB2 5 TRP C 45 ASP C 47 0 SHEET 2 AB2 5 TYR C 486 ILE C 491 -1 O LYS C 490 N LYS C 46 SHEET 3 AB2 5 PHE C 223 CYS C 228 -1 N ALA C 224 O VAL C 489 SHEET 4 AB2 5 VAL C 242 VAL C 245 -1 O SER C 243 N LYS C 227 SHEET 5 AB2 5 GLU C 83 LEU C 86 -1 N ILE C 84 O THR C 244 SHEET 1 AB3 3 VAL C 75 PRO C 76 0 SHEET 2 AB3 3 PHE C 53 SER C 56 1 N CYS C 54 O VAL C 75 SHEET 3 AB3 3 HIS C 216 CYS C 218 -1 O HIS C 216 N ALA C 55 SHEET 1 AB4 2 GLU C 91 ASN C 94 0 SHEET 2 AB4 2 THR C 236 CYS C 239 -1 O CYS C 239 N GLU C 91 SHEET 1 AB5 5 LYS C 169 TYR C 177 0 SHEET 2 AB5 5 LEU C 154 THR C 162 -1 N MET C 161 O GLN C 170 SHEET 3 AB5 5 LEU C 129 ASN C 133 -1 N THR C 132 O ASN C 156 SHEET 4 AB5 5 LYS C 189 LEU C 193 -1 O TYR C 191 N LEU C 129 SHEET 5 AB5 5 VAL C 181 GLN C 183 -1 N VAL C 182 O ARG C 192 SHEET 1 AB6 3 ALA C 200 GLN C 203 0 SHEET 2 AB6 3 GLN C 432 TYR C 435 1 O ALA C 433 N ALA C 200 SHEET 3 AB6 3 ILE C 423 ILE C 424 -1 N ILE C 424 O MET C 434 SHEET 1 AB7 7 LEU C 259 LEU C 261 0 SHEET 2 AB7 7 GLY C 441 ARG C 456 -1 O GLY C 451 N LEU C 260 SHEET 3 AB7 7 ILE C 284 ASN C 302 -1 N CYS C 296 O CYS C 445 SHEET 4 AB7 7 HIS C 330 SER C 334 -1 O ASN C 332 N ASN C 295 SHEET 5 AB7 7 SER C 413 LYS C 421 -1 O ILE C 414 N VAL C 333 SHEET 6 AB7 7 GLU C 381 CYS C 385 -1 N TYR C 384 O ARG C 419 SHEET 7 AB7 7 HIS C 374 CYS C 378 -1 N CYS C 378 O GLU C 381 SHEET 1 AB8 6 MET C 271 ARG C 273 0 SHEET 2 AB8 6 ILE C 284 ASN C 302 -1 O LEU C 285 N ARG C 273 SHEET 3 AB8 6 GLY C 441 ARG C 456 -1 O CYS C 445 N CYS C 296 SHEET 4 AB8 6 THR C 465 PRO C 470 -1 O ARG C 469 N THR C 455 SHEET 5 AB8 6 ILE C 358 PHE C 361 1 N ARG C 360 O PHE C 468 SHEET 6 AB8 6 THR C 394 TRP C 395 -1 O TRP C 395 N ILE C 359 SHEET 1 AB9 2 ARG C 304 GLY C 312 0 SHEET 2 AB9 2 GLN C 315 THR C 320 -1 O PHE C 317 N ILE C 309 SHEET 1 AC1 3 LEU E 494 THR E 499 0 SHEET 2 AC1 3 TRP E 35 TYR E 40 -1 N TRP E 35 O THR E 499 SHEET 3 AC1 3 ILE F 603 PRO F 609 -1 O CYS F 604 N VAL E 38 SHEET 1 AC2 5 TRP E 45 ASP E 47 0 SHEET 2 AC2 5 TYR E 486 ILE E 491 -1 O LYS E 490 N LYS E 46 SHEET 3 AC2 5 PHE E 223 CYS E 228 -1 N ALA E 224 O VAL E 489 SHEET 4 AC2 5 VAL E 242 VAL E 245 -1 O SER E 243 N LYS E 227 SHEET 5 AC2 5 GLU E 83 LEU E 86 -1 N ILE E 84 O THR E 244 SHEET 1 AC3 3 VAL E 75 PRO E 76 0 SHEET 2 AC3 3 PHE E 53 SER E 56 1 N CYS E 54 O VAL E 75 SHEET 3 AC3 3 HIS E 216 CYS E 218 -1 O HIS E 216 N ALA E 55 SHEET 1 AC4 2 GLU E 91 ASN E 94 0 SHEET 2 AC4 2 THR E 236 CYS E 239 -1 O CYS E 239 N GLU E 91 SHEET 1 AC5 5 LYS E 169 TYR E 177 0 SHEET 2 AC5 5 LEU E 154 THR E 162 -1 N MET E 161 O GLN E 170 SHEET 3 AC5 5 LEU E 129 ASN E 133 -1 N THR E 132 O ASN E 156 SHEET 4 AC5 5 LYS E 189 LEU E 193 -1 O TYR E 191 N LEU E 129 SHEET 5 AC5 5 VAL E 181 GLN E 183 -1 N VAL E 182 O ARG E 192 SHEET 1 AC6 3 ALA E 200 GLN E 203 0 SHEET 2 AC6 3 GLN E 432 TYR E 435 1 O ALA E 433 N THR E 202 SHEET 3 AC6 3 ILE E 423 ILE E 424 -1 N ILE E 424 O MET E 434 SHEET 1 AC7 7 LEU E 259 LEU E 261 0 SHEET 2 AC7 7 ARG E 444 ARG E 456 -1 O THR E 450 N LEU E 260 SHEET 3 AC7 7 ILE E 284 THR E 297 -1 N ILE E 284 O LEU E 454 SHEET 4 AC7 7 HIS E 330 SER E 334 -1 O ASN E 332 N ASN E 295 SHEET 5 AC7 7 SER E 413 LYS E 421 -1 O ILE E 414 N VAL E 333 SHEET 6 AC7 7 GLU E 381 CYS E 385 -1 N TYR E 384 O ARG E 419 SHEET 7 AC7 7 HIS E 374 CYS E 378 -1 N CYS E 378 O GLU E 381 SHEET 1 AC8 6 MET E 271 ARG E 273 0 SHEET 2 AC8 6 ILE E 284 THR E 297 -1 O LEU E 285 N ARG E 273 SHEET 3 AC8 6 ARG E 444 ARG E 456 -1 O LEU E 454 N ILE E 284 SHEET 4 AC8 6 THR E 465 PRO E 470 -1 O ARG E 469 N THR E 455 SHEET 5 AC8 6 ILE E 358 PHE E 361 1 N ARG E 360 O PHE E 468 SHEET 6 AC8 6 THR E 394 TRP E 395 -1 O TRP E 395 N ILE E 359 SHEET 1 AC9 2 ARG E 304 GLY E 312 0 SHEET 2 AC9 2 GLN E 315 THR E 320 -1 O PHE E 317 N ILE E 309 SHEET 1 AD1 4 ASP H 5 GLN H 6 0 SHEET 2 AD1 4 SER H 17 ARG H 23 -1 O ARG H 23 N ASP H 5 SHEET 3 AD1 4 THR H 77 GLY H 82A-1 O SER H 78 N CYS H 22 SHEET 4 AD1 4 ILE H 67 ASP H 72 -1 N THR H 70 O TYR H 79 SHEET 1 AD2 6 ALA H 10 LYS H 12 0 SHEET 2 AD2 6 THR H 107 VAL H 111 1 O ILE H 110 N LYS H 12 SHEET 3 AD2 6 ALA H 88 ASP H 95 -1 N TYR H 90 O THR H 107 SHEET 4 AD2 6 ASN H 35I GLN H 39 -1 N LEU H 37 O TYR H 91 SHEET 5 AD2 6 LEU H 45 ASN H 52 -1 O GLY H 49 N TRP H 36 SHEET 6 AD2 6 VAL H 57 TYR H 59 -1 O LYS H 58 N PHE H 50 SHEET 1 AD3 4 ALA H 10 LYS H 12 0 SHEET 2 AD3 4 THR H 107 VAL H 111 1 O ILE H 110 N LYS H 12 SHEET 3 AD3 4 ALA H 88 ASP H 95 -1 N TYR H 90 O THR H 107 SHEET 4 AD3 4 LEU H 100E TRP H 103 -1 O SER H 102 N TRP H 94 SHEET 1 AD4 2 THR H 29 ARG H 32 0 SHEET 2 AD4 2 ALA H 35B ILE H 35E-1 O PHE H 35D N VAL H 30 SHEET 1 AD5 4 ASP I 5 GLN I 6 0 SHEET 2 AD5 4 SER I 17 ARG I 23 -1 O ARG I 23 N ASP I 5 SHEET 3 AD5 4 THR I 77 GLY I 82A-1 O SER I 78 N CYS I 22 SHEET 4 AD5 4 ILE I 67 ASP I 72 -1 N THR I 70 O TYR I 79 SHEET 1 AD6 6 ALA I 10 LYS I 12 0 SHEET 2 AD6 6 THR I 107 VAL I 111 1 O ILE I 110 N LYS I 12 SHEET 3 AD6 6 ALA I 88 ASP I 95 -1 N TYR I 90 O THR I 107 SHEET 4 AD6 6 ASN I 35I GLN I 39 -1 N LEU I 37 O TYR I 91 SHEET 5 AD6 6 LEU I 45 ASN I 52 -1 O GLY I 49 N TRP I 36 SHEET 6 AD6 6 VAL I 57 TYR I 59 -1 O LYS I 58 N PHE I 50 SHEET 1 AD7 4 ALA I 10 LYS I 12 0 SHEET 2 AD7 4 THR I 107 VAL I 111 1 O ILE I 110 N LYS I 12 SHEET 3 AD7 4 ALA I 88 ASP I 95 -1 N TYR I 90 O THR I 107 SHEET 4 AD7 4 SER I 102 TRP I 103 -1 O SER I 102 N TRP I 94 SHEET 1 AD8 2 THR I 29 ARG I 32 0 SHEET 2 AD8 2 ALA I 35B ILE I 35E-1 O PHE I 35D N VAL I 30 SHEET 1 AD9 4 ASP J 5 GLN J 6 0 SHEET 2 AD9 4 SER J 17 ARG J 23 -1 O ARG J 23 N ASP J 5 SHEET 3 AD9 4 THR J 77 GLY J 82A-1 O SER J 78 N CYS J 22 SHEET 4 AD9 4 ILE J 67 ASP J 72 -1 N THR J 70 O TYR J 79 SHEET 1 AE1 6 ALA J 10 LYS J 12 0 SHEET 2 AE1 6 THR J 107 VAL J 111 1 O ILE J 110 N LYS J 12 SHEET 3 AE1 6 ALA J 88 ASP J 95 -1 N TYR J 90 O THR J 107 SHEET 4 AE1 6 ASN J 35I GLN J 39 -1 N LEU J 37 O TYR J 91 SHEET 5 AE1 6 LEU J 45 ASN J 52 -1 O GLY J 49 N TRP J 36 SHEET 6 AE1 6 VAL J 57 TYR J 59 -1 O LYS J 58 N PHE J 50 SHEET 1 AE2 4 ALA J 10 LYS J 12 0 SHEET 2 AE2 4 THR J 107 VAL J 111 1 O ILE J 110 N LYS J 12 SHEET 3 AE2 4 ALA J 88 ASP J 95 -1 N TYR J 90 O THR J 107 SHEET 4 AE2 4 SER J 102 TRP J 103 -1 O SER J 102 N TRP J 94 SHEET 1 AE3 2 THR J 29 ARG J 32 0 SHEET 2 AE3 2 ALA J 35B ILE J 35E-1 O PHE J 35D N VAL J 30 SHEET 1 AE4 4 VAL L 4 SER L 7 0 SHEET 2 AE4 4 ILE L 19 VAL L 25 -1 O GLU L 24 N THR L 5 SHEET 3 AE4 4 TYR L 70 ILE L 75 -1 O ILE L 75 N ILE L 19 SHEET 4 AE4 4 PHE L 62 VAL L 67 -1 N VAL L 67 O TYR L 70 SHEET 1 AE5 6 SER L 10 ALA L 13 0 SHEET 2 AE5 6 THR L 103 LEU L 107 1 O ARG L 104 N LEU L 11 SHEET 3 AE5 6 GLY L 84 VAL L 90 -1 N GLY L 84 O VAL L 105 SHEET 4 AE5 6 ASN L 34 GLN L 38 -1 N ASN L 34 O GLN L 89 SHEET 5 AE5 6 TYR L 45 TYR L 49 -1 O ILE L 48 N TRP L 35 SHEET 6 AE5 6 ASN L 53 LEU L 54 -1 O ASN L 53 N TYR L 49 SHEET 1 AE6 4 SER L 10 ALA L 13 0 SHEET 2 AE6 4 THR L 103 LEU L 107 1 O ARG L 104 N LEU L 11 SHEET 3 AE6 4 GLY L 84 VAL L 90 -1 N GLY L 84 O VAL L 105 SHEET 4 AE6 4 SER L 97 PHE L 98 -1 O SER L 97 N VAL L 90 SHEET 1 AE7 4 VAL M 4 SER M 7 0 SHEET 2 AE7 4 ILE M 19 VAL M 25 -1 O GLU M 24 N THR M 5 SHEET 3 AE7 4 TYR M 70 ILE M 75 -1 O ILE M 75 N ILE M 19 SHEET 4 AE7 4 PHE M 62 VAL M 67 -1 N ARG M 63 O THR M 74 SHEET 1 AE8 6 SER M 10 ALA M 13 0 SHEET 2 AE8 6 THR M 103 LEU M 107 1 O ARG M 104 N LEU M 11 SHEET 3 AE8 6 GLY M 84 VAL M 90 -1 N GLY M 84 O VAL M 105 SHEET 4 AE8 6 ASN M 34 GLN M 38 -1 N ASN M 34 O GLN M 89 SHEET 5 AE8 6 TYR M 45 TYR M 49 -1 O ILE M 48 N TRP M 35 SHEET 6 AE8 6 ASN M 53 LEU M 54 -1 O ASN M 53 N TYR M 49 SHEET 1 AE9 4 SER M 10 ALA M 13 0 SHEET 2 AE9 4 THR M 103 LEU M 107 1 O ARG M 104 N LEU M 11 SHEET 3 AE9 4 GLY M 84 VAL M 90 -1 N GLY M 84 O VAL M 105 SHEET 4 AE9 4 SER M 97 PHE M 98 -1 O SER M 97 N VAL M 90 SHEET 1 AF1 4 VAL N 4 SER N 7 0 SHEET 2 AF1 4 ILE N 19 VAL N 25 -1 O GLU N 24 N THR N 5 SHEET 3 AF1 4 TYR N 70 ILE N 75 -1 O ILE N 75 N ILE N 19 SHEET 4 AF1 4 PHE N 62 VAL N 67 -1 N ARG N 63 O THR N 74 SHEET 1 AF2 6 SER N 10 ALA N 13 0 SHEET 2 AF2 6 THR N 103 LEU N 107 1 O ARG N 104 N LEU N 11 SHEET 3 AF2 6 GLY N 84 VAL N 90 -1 N GLY N 84 O VAL N 105 SHEET 4 AF2 6 ASN N 34 GLN N 38 -1 N ASN N 34 O GLN N 89 SHEET 5 AF2 6 TYR N 45 TYR N 49 -1 O LEU N 47 N TRP N 35 SHEET 6 AF2 6 ASN N 53 LEU N 54 -1 O ASN N 53 N TYR N 49 SHEET 1 AF3 4 SER N 10 ALA N 13 0 SHEET 2 AF3 4 THR N 103 LEU N 107 1 O ARG N 104 N LEU N 11 SHEET 3 AF3 4 GLY N 84 VAL N 90 -1 N GLY N 84 O VAL N 105 SHEET 4 AF3 4 SER N 97 PHE N 98 -1 O SER N 97 N VAL N 90 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 218 CYS A 247 1555 1555 2.04 SSBOND 6 CYS A 228 CYS A 239 1555 1555 2.03 SSBOND 7 CYS A 296 CYS A 331 1555 1555 2.05 SSBOND 8 CYS A 378 CYS A 445 1555 1555 2.03 SSBOND 9 CYS A 385 CYS A 418 1555 1555 2.03 SSBOND 10 CYS A 501 CYS B 605 1555 1555 2.03 SSBOND 11 CYS B 598 CYS B 604 1555 1555 2.03 SSBOND 12 CYS C 54 CYS C 74 1555 1555 2.03 SSBOND 13 CYS C 119 CYS C 205 1555 1555 2.03 SSBOND 14 CYS C 126 CYS C 196 1555 1555 2.03 SSBOND 15 CYS C 131 CYS C 157 1555 1555 2.03 SSBOND 16 CYS C 218 CYS C 247 1555 1555 2.04 SSBOND 17 CYS C 228 CYS C 239 1555 1555 2.03 SSBOND 18 CYS C 296 CYS C 331 1555 1555 2.03 SSBOND 19 CYS C 378 CYS C 445 1555 1555 2.03 SSBOND 20 CYS C 385 CYS C 418 1555 1555 2.03 SSBOND 21 CYS C 501 CYS D 605 1555 1555 2.03 SSBOND 22 CYS D 598 CYS D 604 1555 1555 2.04 SSBOND 23 CYS E 54 CYS E 74 1555 1555 2.03 SSBOND 24 CYS E 119 CYS E 205 1555 1555 2.03 SSBOND 25 CYS E 126 CYS E 196 1555 1555 2.03 SSBOND 26 CYS E 131 CYS E 157 1555 1555 2.03 SSBOND 27 CYS E 218 CYS E 247 1555 1555 2.04 SSBOND 28 CYS E 228 CYS E 239 1555 1555 2.03 SSBOND 29 CYS E 296 CYS E 331 1555 1555 2.05 SSBOND 30 CYS E 378 CYS E 445 1555 1555 2.03 SSBOND 31 CYS E 385 CYS E 418 1555 1555 2.03 SSBOND 32 CYS E 501 CYS F 605 1555 1555 2.03 SSBOND 33 CYS F 598 CYS F 604 1555 1555 2.03 SSBOND 34 CYS H 22 CYS H 92 1555 1555 2.03 SSBOND 35 CYS I 22 CYS I 92 1555 1555 2.03 SSBOND 36 CYS J 22 CYS J 92 1555 1555 2.03 SSBOND 37 CYS L 23 CYS L 88 1555 1555 2.03 SSBOND 38 CYS M 23 CYS M 88 1555 1555 2.03 SSBOND 39 CYS N 23 CYS N 88 1555 1555 2.03 LINK ND2 ASN A 88 C1 NAG A 601 1555 1555 1.45 LINK ND2 ASN A 133 C1 NAG A 602 1555 1555 1.44 LINK ND2 ASN A 156 C1 NAG A 603 1555 1555 1.44 LINK ND2 ASN A 160 C1 NAG A 604 1555 1555 1.44 LINK ND2 ASN A 197 C1 NAG A 605 1555 1555 1.44 LINK ND2 ASN A 234 C1 NAG A 610 1555 1555 1.45 LINK ND2 ASN A 262 C1 NAG G 1 1555 1555 1.45 LINK ND2 ASN A 276 C1 NAG R 1 1555 1555 1.44 LINK ND2 ASN A 295 C1 NAG K 1 1555 1555 1.45 LINK ND2 ASN A 301 C1 NAG A 606 1555 1555 1.44 LINK ND2 ASN A 332 C1 NAG O 1 1555 1555 1.44 LINK ND2 ASN A 339 C1 NAG A 607 1555 1555 1.44 LINK ND2 ASN A 363 C1 NAG P 1 1555 1555 1.44 LINK ND2 ASN A 386 C1 NAG Q 1 1555 1555 1.44 LINK ND2 ASN A 392 C1 NAG A 608 1555 1555 1.44 LINK ND2 ASN A 448 C1 NAG A 609 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 602 1555 1555 1.45 LINK ND2 ASN C 156 C1 NAG C 603 1555 1555 1.44 LINK ND2 ASN C 160 C1 NAG C 604 1555 1555 1.44 LINK ND2 ASN C 197 C1 NAG C 605 1555 1555 1.44 LINK ND2 ASN C 234 C1 NAG C 610 1555 1555 1.44 LINK ND2 ASN C 262 C1 NAG S 1 1555 1555 1.44 LINK ND2 ASN C 276 C1 NAG X 1 1555 1555 1.44 LINK ND2 ASN C 295 C1 NAG T 1 1555 1555 1.44 LINK ND2 ASN C 301 C1 NAG C 606 1555 1555 1.44 LINK ND2 ASN C 332 C1 NAG U 1 1555 1555 1.44 LINK ND2 ASN C 339 C1 NAG C 607 1555 1555 1.44 LINK ND2 ASN C 363 C1 NAG V 1 1555 1555 1.44 LINK ND2 ASN C 386 C1 NAG W 1 1555 1555 1.44 LINK ND2 ASN C 392 C1 NAG C 608 1555 1555 1.44 LINK ND2 ASN C 448 C1 NAG C 609 1555 1555 1.44 LINK ND2 ASN E 88 C1 NAG E 601 1555 1555 1.45 LINK ND2 ASN E 133 C1 NAG E 602 1555 1555 1.44 LINK ND2 ASN E 156 C1 NAG E 603 1555 1555 1.44 LINK ND2 ASN E 160 C1 NAG E 604 1555 1555 1.44 LINK ND2 ASN E 197 C1 NAG E 605 1555 1555 1.44 LINK ND2 ASN E 234 C1 NAG E 606 1555 1555 1.45 LINK ND2 ASN E 262 C1 NAG d 1 1555 1555 1.44 LINK ND2 ASN E 276 C1 NAG e 1 1555 1555 1.44 LINK ND2 ASN E 295 C1 NAG Y 1 1555 1555 1.43 LINK ND2 ASN E 301 C1 NAG E 607 1555 1555 1.44 LINK ND2 ASN E 332 C1 NAG Z 1 1555 1555 1.44 LINK ND2 ASN E 339 C1 NAG E 608 1555 1555 1.44 LINK ND2 ASN E 363 C1 NAG a 1 1555 1555 1.44 LINK ND2 ASN E 386 C1 NAG b 1 1555 1555 1.43 LINK ND2 ASN E 392 C1 NAG E 609 1555 1555 1.44 LINK ND2 ASN E 448 C1 NAG c 1 1555 1555 1.44 LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.44 LINK O4 NAG G 2 C1 BMA G 3 1555 1555 1.44 LINK O4 NAG K 1 C1 NAG K 2 1555 1555 1.44 LINK O4 NAG O 1 C1 NAG O 2 1555 1555 1.44 LINK O4 NAG P 1 C1 NAG P 2 1555 1555 1.44 LINK O4 NAG Q 1 C1 NAG Q 2 1555 1555 1.45 LINK O4 NAG R 1 C1 NAG R 2 1555 1555 1.43 LINK O4 NAG S 1 C1 NAG S 2 1555 1555 1.44 LINK O4 NAG S 2 C1 BMA S 3 1555 1555 1.44 LINK O4 NAG T 1 C1 NAG T 2 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 1.44 LINK O4 NAG W 1 C1 NAG W 2 1555 1555 1.44 LINK O4 NAG X 1 C1 NAG X 2 1555 1555 1.45 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 b 1 C1 NAG b 2 1555 1555 1.44 LINK O4 NAG c 1 C1 NAG c 2 1555 1555 1.46 LINK O4 NAG d 1 C1 NAG d 2 1555 1555 1.44 LINK O4 NAG d 2 C1 BMA d 3 1555 1555 1.44 LINK O4 NAG e 1 C1 NAG e 2 1555 1555 1.39 CISPEP 1 SER L 7 PRO L 8 0 -2.59 CISPEP 2 SER M 7 PRO M 8 0 -0.14 CISPEP 3 SER N 7 PRO N 8 0 -2.00 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