HEADER VIRAL PROTEIN/IMMUNE SYSTEM 30-APR-19 6ORN TITLE MODIFIED BG505 SOSIP-BASED IMMUNOGEN RC1 IN COMPLEX WITH THE ELICITED TITLE 2 V3-GLYCAN PATCH BNAB 10-1074 COMPND MOL_ID: 1; COMPND 2 MOLECULE: RC1 VARIANT OF HIV-1 ENV GLYCOPROTEIN GP41; COMPND 3 CHAIN: C, J, Q; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: RC1 VARIANT OF HIV-1 ENV GLYCOPROTEIN GP120; COMPND 7 CHAIN: G, K, R; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: 10-1074 ANTIBODY FAB HEAVY CHAIN; COMPND 11 CHAIN: A, F, O; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 4; COMPND 14 MOLECULE: 10-1074 ANTIBODY FAB LIGHT CHAIN; COMPND 15 CHAIN: B, I, P; COMPND 16 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 3 ORGANISM_TAXID: 11676; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 7 EXPRESSION_SYSTEM_CELL: 293 6E; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 10 ORGANISM_TAXID: 11676; SOURCE 11 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 12 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 13 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 14 EXPRESSION_SYSTEM_CELL: 293 6E; SOURCE 15 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 17 ORGANISM_COMMON: HUMAN; SOURCE 18 ORGANISM_TAXID: 9606; SOURCE 19 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 20 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 21 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 22 EXPRESSION_SYSTEM_CELL: EXPI293; SOURCE 23 MOL_ID: 4; SOURCE 24 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 25 ORGANISM_COMMON: HUMAN; SOURCE 26 ORGANISM_TAXID: 9606; SOURCE 27 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 28 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 29 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 30 EXPRESSION_SYSTEM_CELL: EXPI293 KEYWDS HIV-1 BROADLY-NEUTRALIZING ANTIBODY, ENV TRIMER STRUCTURE, V3-GLYCAN KEYWDS 2 PATCH, CRYO-EM, RC1, IMMUNOGEN DESIGN, ANTIVIRAL PROTEIN-IMMUNE KEYWDS 3 SYSTEM COMPLEX, ANTIVIRAL PROTEIN, VIRAL PROTEIN-IMMUNE SYSTEM KEYWDS 4 COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR M.E.ABERNATHY,H.B.GRISTICK,P.J.BJORKMAN REVDAT 1 12-JUN-19 6ORN 0 JRNL AUTH A.ESCOLANO,H.B.GRISTICK,M.E.ABERNATHY,J.MERKENSCHLAGER, JRNL AUTH 2 R.GAUTAM,T.Y.OLIVEIRA,J.PAI,A.P.WEST JR.,C.O.BARNES, JRNL AUTH 3 A.A.COHEN,H.WANG,J.GOLIJANIN,D.YOST,J.R.KEEFFE,Z.WANG, JRNL AUTH 4 P.ZHAO,K.H.YAO,J.BAUER,L.NOGUEIRA,H.GAO,A.V.VOLL, JRNL AUTH 5 D.C.MONTEFIORI,M.S.SEAMAN,A.GAZUMYAN,M.SILVA,A.T.MCGUIRE, JRNL AUTH 6 L.STAMATATOS,D.J.IRVINE,L.WELLS,M.A.MARTIN,P.J.BJORKMAN, JRNL AUTH 7 M.C.NUSSENZWEIG JRNL TITL IMMUNIZATION EXPANDS B CELLS SPECIFIC TO HIV-1 V3 GLYCAN IN JRNL TITL 2 MICE AND MACAQUES. JRNL REF NATURE 2019 JRNL REFN ESSN 1476-4687 JRNL PMID 31142836 JRNL DOI 10.1038/S41586-019-1250-Z REMARK 2 REMARK 2 RESOLUTION. 4.05 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : RELION, EPU, GCTF, UCSF CHIMERA, REMARK 3 PHENIX, CRYOSPARC, CRYOSPARC, CRYOSPARC, REMARK 3 CRYOSPARC REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : 5T3Z REMARK 3 REFINEMENT SPACE : REAL REMARK 3 REFINEMENT PROTOCOL : RIGID BODY FIT REMARK 3 REFINEMENT TARGET : CORRELATION COEFFICIENT 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) : 4.050 REMARK 3 NUMBER OF PARTICLES : 122013 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 6ORN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-MAY-19. REMARK 100 THE DEPOSITION ID IS D_1000241079. REMARK 245 REMARK 245 EXPERIMENTAL DETAILS REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE REMARK 245 SPECIMEN TYPE : NULL REMARK 245 REMARK 245 ELECTRON MICROSCOPE SAMPLE REMARK 245 SAMPLE TYPE : PARTICLE REMARK 245 PARTICLE TYPE : POINT REMARK 245 NAME OF SAMPLE : COMPLEX OF RC1 VARIANT OF BG505 REMARK 245 SOSIP.664 TRIMER WITH THREE 10- REMARK 245 1074 FABS AND THREE CD4BS FABS; REMARK 245 RC1 VARIANT OF BG505 SOSIP.664 REMARK 245 TRIMER; 10-1074 FAB REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 0.75 REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : 0 BLOT FORCE, 3.5 SECOND BLOT REMARK 245 TIME, 3 UL SAMPLE ADDED TO REMARK 245 FRESHLY GLOW-DISCHARGED GRIDS REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 8.00 REMARK 245 SAMPLE DETAILS : FAB FRAGMENTS GENERATED BY REMARK 245 RECOMBINANT EXPRESSION AND COMPLEXED WITH THE RC1 VARIANT OF REMARK 245 BG505 SOSIP.664 TRIMER REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : 684 REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : FEI TALOS ARCTICA REMARK 245 DETECTOR TYPE : FEI FALCON III (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1000.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 3400.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : 2.70 REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 40.00 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : 73000 REMARK 245 CALIBRATED MAGNIFICATION : NULL REMARK 245 SOURCE : FIELD EMISSION GUN REMARK 245 ACCELERATION VOLTAGE (KV) : 200 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: C, G, J, K, Q, R, A, F, O, B, REMARK 350 AND CHAINS: I, P 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 C 512 REMARK 465 VAL C 513 REMARK 465 GLY C 514 REMARK 465 ILE C 515 REMARK 465 GLY C 516 REMARK 465 ALA C 517 REMARK 465 GLY C 547 REMARK 465 ILE C 548 REMARK 465 VAL C 549 REMARK 465 GLN C 550 REMARK 465 GLN C 551 REMARK 465 GLN C 552 REMARK 465 SER C 553 REMARK 465 ASN C 554 REMARK 465 LEU C 555 REMARK 465 LEU C 556 REMARK 465 ARG C 557 REMARK 465 ALA C 558 REMARK 465 PRO C 559 REMARK 465 GLU C 560 REMARK 465 PRO C 561 REMARK 465 GLN C 562 REMARK 465 GLN C 563 REMARK 465 HIS C 564 REMARK 465 LEU C 565 REMARK 465 LEU C 566 REMARK 465 LYS C 567 REMARK 465 ASP C 568 REMARK 465 THR C 569 REMARK 465 ALA G 58 REMARK 465 LYS G 59 REMARK 465 ALA G 60 REMARK 465 TYR G 61 REMARK 465 GLU G 62 REMARK 465 THR G 63 REMARK 465 GLU G 64 REMARK 465 LYS G 65 REMARK 465 ASP G 78 REMARK 465 PRO G 79 REMARK 465 ASN G 80 REMARK 465 GLU G 185A REMARK 465 ASN G 185B REMARK 465 GLN G 185C REMARK 465 GLY G 185D REMARK 465 ASN G 185E REMARK 465 ARG G 185F REMARK 465 SER G 185G REMARK 465 ASN G 185H REMARK 465 ASN G 185I REMARK 465 THR G 400 REMARK 465 SER G 401 REMARK 465 VAL G 402 REMARK 465 GLN G 403 REMARK 465 GLY G 404 REMARK 465 SER G 405 REMARK 465 ASN G 406 REMARK 465 SER G 407 REMARK 465 THR G 408 REMARK 465 GLY G 409 REMARK 465 SER G 410 REMARK 465 VAL G 506 REMARK 465 GLY G 507 REMARK 465 ARG G 508 REMARK 465 ARG G 509 REMARK 465 ARG G 510 REMARK 465 ARG G 511 REMARK 465 ARG G 512 REMARK 465 ARG G 513 REMARK 465 ALA J 512 REMARK 465 VAL J 513 REMARK 465 GLY J 514 REMARK 465 ILE J 515 REMARK 465 GLY J 516 REMARK 465 ALA J 517 REMARK 465 GLY J 547 REMARK 465 ILE J 548 REMARK 465 VAL J 549 REMARK 465 GLN J 550 REMARK 465 GLN J 551 REMARK 465 GLN J 552 REMARK 465 SER J 553 REMARK 465 ASN J 554 REMARK 465 LEU J 555 REMARK 465 LEU J 556 REMARK 465 ARG J 557 REMARK 465 ALA J 558 REMARK 465 PRO J 559 REMARK 465 GLU J 560 REMARK 465 PRO J 561 REMARK 465 GLN J 562 REMARK 465 GLN J 563 REMARK 465 HIS J 564 REMARK 465 LEU J 565 REMARK 465 LEU J 566 REMARK 465 LYS J 567 REMARK 465 ASP J 568 REMARK 465 THR J 569 REMARK 465 ALA K 58 REMARK 465 LYS K 59 REMARK 465 ALA K 60 REMARK 465 TYR K 61 REMARK 465 GLU K 62 REMARK 465 THR K 63 REMARK 465 GLU K 64 REMARK 465 LYS K 65 REMARK 465 ASP K 78 REMARK 465 PRO K 79 REMARK 465 ASN K 80 REMARK 465 GLU K 185A REMARK 465 ASN K 185B REMARK 465 GLN K 185C REMARK 465 GLY K 185D REMARK 465 ASN K 185E REMARK 465 ARG K 185F REMARK 465 SER K 185G REMARK 465 ASN K 185H REMARK 465 ASN K 185I REMARK 465 THR K 400 REMARK 465 SER K 401 REMARK 465 VAL K 402 REMARK 465 GLN K 403 REMARK 465 GLY K 404 REMARK 465 SER K 405 REMARK 465 ASN K 406 REMARK 465 SER K 407 REMARK 465 THR K 408 REMARK 465 GLY K 409 REMARK 465 SER K 410 REMARK 465 VAL K 506 REMARK 465 GLY K 507 REMARK 465 ARG K 508 REMARK 465 ARG K 509 REMARK 465 ARG K 510 REMARK 465 ARG K 511 REMARK 465 ARG K 512 REMARK 465 ARG K 513 REMARK 465 ALA Q 512 REMARK 465 VAL Q 513 REMARK 465 GLY Q 514 REMARK 465 ILE Q 515 REMARK 465 GLY Q 516 REMARK 465 ALA Q 517 REMARK 465 GLY Q 547 REMARK 465 ILE Q 548 REMARK 465 VAL Q 549 REMARK 465 GLN Q 550 REMARK 465 GLN Q 551 REMARK 465 GLN Q 552 REMARK 465 SER Q 553 REMARK 465 ASN Q 554 REMARK 465 LEU Q 555 REMARK 465 LEU Q 556 REMARK 465 ARG Q 557 REMARK 465 ALA Q 558 REMARK 465 PRO Q 559 REMARK 465 GLU Q 560 REMARK 465 PRO Q 561 REMARK 465 GLN Q 562 REMARK 465 GLN Q 563 REMARK 465 HIS Q 564 REMARK 465 LEU Q 565 REMARK 465 LEU Q 566 REMARK 465 LYS Q 567 REMARK 465 ASP Q 568 REMARK 465 THR Q 569 REMARK 465 ALA R 58 REMARK 465 LYS R 59 REMARK 465 ALA R 60 REMARK 465 TYR R 61 REMARK 465 GLU R 62 REMARK 465 THR R 63 REMARK 465 GLU R 64 REMARK 465 LYS R 65 REMARK 465 ASP R 78 REMARK 465 PRO R 79 REMARK 465 ASN R 80 REMARK 465 GLU R 185A REMARK 465 ASN R 185B REMARK 465 GLN R 185C REMARK 465 GLY R 185D REMARK 465 ASN R 185E REMARK 465 ARG R 185F REMARK 465 SER R 185G REMARK 465 ASN R 185H REMARK 465 ASN R 185I REMARK 465 THR R 400 REMARK 465 SER R 401 REMARK 465 VAL R 402 REMARK 465 GLN R 403 REMARK 465 GLY R 404 REMARK 465 SER R 405 REMARK 465 ASN R 406 REMARK 465 SER R 407 REMARK 465 THR R 408 REMARK 465 GLY R 409 REMARK 465 SER R 410 REMARK 465 VAL R 506 REMARK 465 GLY R 507 REMARK 465 ARG R 508 REMARK 465 ARG R 509 REMARK 465 ARG R 510 REMARK 465 ARG R 511 REMARK 465 ARG R 512 REMARK 465 ARG R 513 REMARK 465 SER A 134 REMARK 465 THR A 135 REMARK 465 LYS A 136 REMARK 465 GLY A 137 REMARK 465 PRO A 138 REMARK 465 SER A 139 REMARK 465 VAL A 140 REMARK 465 PHE A 141 REMARK 465 PRO A 142 REMARK 465 LEU A 143 REMARK 465 ALA A 144 REMARK 465 PRO A 145 REMARK 465 SER A 146 REMARK 465 SER A 147 REMARK 465 LYS A 148 REMARK 465 SER A 149 REMARK 465 THR A 150 REMARK 465 SER A 151 REMARK 465 GLY A 152 REMARK 465 GLY A 153 REMARK 465 THR A 154 REMARK 465 ALA A 155 REMARK 465 ALA A 156 REMARK 465 LEU A 157 REMARK 465 GLY A 158 REMARK 465 CYS A 159 REMARK 465 LEU A 160 REMARK 465 VAL A 161 REMARK 465 LYS A 162 REMARK 465 ASP A 163 REMARK 465 TYR A 164 REMARK 465 PHE A 165 REMARK 465 PRO A 166 REMARK 465 GLU A 167 REMARK 465 PRO A 168 REMARK 465 VAL A 169 REMARK 465 THR A 170 REMARK 465 VAL A 171 REMARK 465 SER A 172 REMARK 465 TRP A 173 REMARK 465 ASN A 174 REMARK 465 SER A 175 REMARK 465 GLY A 176 REMARK 465 ALA A 177 REMARK 465 LEU A 178 REMARK 465 THR A 179 REMARK 465 SER A 180 REMARK 465 GLY A 181 REMARK 465 VAL A 182 REMARK 465 HIS A 183 REMARK 465 THR A 184 REMARK 465 PHE A 185 REMARK 465 PRO A 186 REMARK 465 ALA A 187 REMARK 465 VAL A 188 REMARK 465 LEU A 189 REMARK 465 GLN A 190 REMARK 465 SER A 191 REMARK 465 SER A 192 REMARK 465 GLY A 193 REMARK 465 LEU A 194 REMARK 465 TYR A 195 REMARK 465 SER A 196 REMARK 465 LEU A 197 REMARK 465 SER A 198 REMARK 465 SER A 199 REMARK 465 VAL A 200 REMARK 465 VAL A 201 REMARK 465 THR A 202 REMARK 465 VAL A 203 REMARK 465 PRO A 204 REMARK 465 SER A 205 REMARK 465 SER A 206 REMARK 465 SER A 207 REMARK 465 LEU A 208 REMARK 465 GLY A 209 REMARK 465 THR A 210 REMARK 465 GLN A 211 REMARK 465 THR A 212 REMARK 465 TYR A 213 REMARK 465 ILE A 214 REMARK 465 CYS A 215 REMARK 465 ASN A 216 REMARK 465 VAL A 217 REMARK 465 ASN A 218 REMARK 465 HIS A 219 REMARK 465 LYS A 220 REMARK 465 PRO A 221 REMARK 465 SER A 222 REMARK 465 ASN A 223 REMARK 465 THR A 224 REMARK 465 LYS A 225 REMARK 465 VAL A 226 REMARK 465 ASP A 227 REMARK 465 LYS A 228 REMARK 465 ARG A 229 REMARK 465 VAL A 230 REMARK 465 GLU A 231 REMARK 465 PRO A 232 REMARK 465 LYS A 233 REMARK 465 SER A 234 REMARK 465 CYS A 235 REMARK 465 ASP A 236 REMARK 465 LYS A 237 REMARK 465 THR A 238 REMARK 465 SER F 115 REMARK 465 THR F 116 REMARK 465 LYS F 117 REMARK 465 GLY F 118 REMARK 465 PRO F 119 REMARK 465 SER F 120 REMARK 465 VAL F 121 REMARK 465 PHE F 122 REMARK 465 PRO F 123 REMARK 465 LEU F 124 REMARK 465 ALA F 125 REMARK 465 PRO F 126 REMARK 465 SER F 127 REMARK 465 SER F 128 REMARK 465 LYS F 129 REMARK 465 SER F 130 REMARK 465 THR F 131 REMARK 465 SER F 132 REMARK 465 GLY F 133 REMARK 465 GLY F 134 REMARK 465 THR F 135 REMARK 465 ALA F 136 REMARK 465 ALA F 137 REMARK 465 LEU F 138 REMARK 465 GLY F 139 REMARK 465 CYS F 140 REMARK 465 LEU F 141 REMARK 465 VAL F 142 REMARK 465 LYS F 143 REMARK 465 ASP F 144 REMARK 465 TYR F 145 REMARK 465 PHE F 146 REMARK 465 PRO F 147 REMARK 465 GLU F 148 REMARK 465 PRO F 149 REMARK 465 VAL F 150 REMARK 465 THR F 151 REMARK 465 VAL F 152 REMARK 465 SER F 153 REMARK 465 TRP F 154 REMARK 465 ASN F 155 REMARK 465 SER F 156 REMARK 465 GLY F 157 REMARK 465 ALA F 158 REMARK 465 LEU F 159 REMARK 465 THR F 160 REMARK 465 SER F 161 REMARK 465 GLY F 162 REMARK 465 VAL F 163 REMARK 465 HIS F 164 REMARK 465 THR F 165 REMARK 465 PHE F 166 REMARK 465 PRO F 167 REMARK 465 ALA F 168 REMARK 465 VAL F 169 REMARK 465 LEU F 170 REMARK 465 GLN F 171 REMARK 465 SER F 172 REMARK 465 SER F 173 REMARK 465 GLY F 174 REMARK 465 LEU F 175 REMARK 465 TYR F 176 REMARK 465 SER F 177 REMARK 465 LEU F 178 REMARK 465 SER F 179 REMARK 465 SER F 180 REMARK 465 VAL F 181 REMARK 465 VAL F 182 REMARK 465 THR F 183 REMARK 465 VAL F 184 REMARK 465 PRO F 185 REMARK 465 SER F 186 REMARK 465 SER F 187 REMARK 465 SER F 188 REMARK 465 LEU F 189 REMARK 465 GLY F 190 REMARK 465 THR F 191 REMARK 465 GLN F 192 REMARK 465 THR F 193 REMARK 465 TYR F 194 REMARK 465 ILE F 195 REMARK 465 CYS F 196 REMARK 465 ASN F 197 REMARK 465 VAL F 198 REMARK 465 ASN F 199 REMARK 465 HIS F 200 REMARK 465 LYS F 201 REMARK 465 PRO F 202 REMARK 465 SER F 203 REMARK 465 ASN F 204 REMARK 465 THR F 205 REMARK 465 LYS F 206 REMARK 465 VAL F 207 REMARK 465 ASP F 208 REMARK 465 LYS F 209 REMARK 465 ARG F 210 REMARK 465 VAL F 211 REMARK 465 GLU F 212 REMARK 465 PRO F 213 REMARK 465 LYS F 214 REMARK 465 SER F 215 REMARK 465 CYS F 216 REMARK 465 ASP F 217 REMARK 465 LYS F 218 REMARK 465 THR F 219 REMARK 465 SER O 115 REMARK 465 THR O 116 REMARK 465 LYS O 117 REMARK 465 GLY O 118 REMARK 465 PRO O 119 REMARK 465 SER O 120 REMARK 465 VAL O 121 REMARK 465 PHE O 122 REMARK 465 PRO O 123 REMARK 465 LEU O 124 REMARK 465 ALA O 125 REMARK 465 PRO O 126 REMARK 465 SER O 127 REMARK 465 SER O 128 REMARK 465 LYS O 129 REMARK 465 SER O 130 REMARK 465 THR O 131 REMARK 465 SER O 132 REMARK 465 GLY O 133 REMARK 465 GLY O 134 REMARK 465 THR O 135 REMARK 465 ALA O 136 REMARK 465 ALA O 137 REMARK 465 LEU O 138 REMARK 465 GLY O 139 REMARK 465 CYS O 140 REMARK 465 LEU O 141 REMARK 465 VAL O 142 REMARK 465 LYS O 143 REMARK 465 ASP O 144 REMARK 465 TYR O 145 REMARK 465 PHE O 146 REMARK 465 PRO O 147 REMARK 465 GLU O 148 REMARK 465 PRO O 149 REMARK 465 VAL O 150 REMARK 465 THR O 151 REMARK 465 VAL O 152 REMARK 465 SER O 153 REMARK 465 TRP O 154 REMARK 465 ASN O 155 REMARK 465 SER O 156 REMARK 465 GLY O 157 REMARK 465 ALA O 158 REMARK 465 LEU O 159 REMARK 465 THR O 160 REMARK 465 SER O 161 REMARK 465 GLY O 162 REMARK 465 VAL O 163 REMARK 465 HIS O 164 REMARK 465 THR O 165 REMARK 465 PHE O 166 REMARK 465 PRO O 167 REMARK 465 ALA O 168 REMARK 465 VAL O 169 REMARK 465 LEU O 170 REMARK 465 GLN O 171 REMARK 465 SER O 172 REMARK 465 SER O 173 REMARK 465 GLY O 174 REMARK 465 LEU O 175 REMARK 465 TYR O 176 REMARK 465 SER O 177 REMARK 465 LEU O 178 REMARK 465 SER O 179 REMARK 465 SER O 180 REMARK 465 VAL O 181 REMARK 465 VAL O 182 REMARK 465 THR O 183 REMARK 465 VAL O 184 REMARK 465 PRO O 185 REMARK 465 SER O 186 REMARK 465 SER O 187 REMARK 465 SER O 188 REMARK 465 LEU O 189 REMARK 465 GLY O 190 REMARK 465 THR O 191 REMARK 465 GLN O 192 REMARK 465 THR O 193 REMARK 465 TYR O 194 REMARK 465 ILE O 195 REMARK 465 CYS O 196 REMARK 465 ASN O 197 REMARK 465 VAL O 198 REMARK 465 ASN O 199 REMARK 465 HIS O 200 REMARK 465 LYS O 201 REMARK 465 PRO O 202 REMARK 465 SER O 203 REMARK 465 ASN O 204 REMARK 465 THR O 205 REMARK 465 LYS O 206 REMARK 465 VAL O 207 REMARK 465 ASP O 208 REMARK 465 LYS O 209 REMARK 465 ARG O 210 REMARK 465 VAL O 211 REMARK 465 GLU O 212 REMARK 465 PRO O 213 REMARK 465 LYS O 214 REMARK 465 SER O 215 REMARK 465 CYS O 216 REMARK 465 ASP O 217 REMARK 465 LYS O 218 REMARK 465 THR O 219 REMARK 465 SER B 6 REMARK 465 TYR B 7 REMARK 465 GLN B 109 REMARK 465 PRO B 110 REMARK 465 LYS B 111 REMARK 465 ALA B 112 REMARK 465 ALA B 113 REMARK 465 PRO B 114 REMARK 465 SER B 115 REMARK 465 VAL B 116 REMARK 465 THR B 117 REMARK 465 LEU B 118 REMARK 465 PHE B 119 REMARK 465 PRO B 120 REMARK 465 PRO B 121 REMARK 465 SER B 122 REMARK 465 SER B 123 REMARK 465 GLU B 124 REMARK 465 GLU B 125 REMARK 465 LEU B 126 REMARK 465 GLN B 127 REMARK 465 ALA B 128 REMARK 465 ASN B 129 REMARK 465 LYS B 130 REMARK 465 ALA B 131 REMARK 465 THR B 132 REMARK 465 LEU B 133 REMARK 465 VAL B 134 REMARK 465 CYS B 135 REMARK 465 LEU B 136 REMARK 465 ILE B 137 REMARK 465 SER B 138 REMARK 465 ASP B 139 REMARK 465 PHE B 140 REMARK 465 TYR B 141 REMARK 465 PRO B 142 REMARK 465 GLY B 143 REMARK 465 ALA B 144 REMARK 465 VAL B 145 REMARK 465 THR B 146 REMARK 465 VAL B 147 REMARK 465 ALA B 148 REMARK 465 TRP B 149 REMARK 465 LYS B 150 REMARK 465 ALA B 151 REMARK 465 ASP B 152 REMARK 465 SER B 153 REMARK 465 SER B 154 REMARK 465 PRO B 155 REMARK 465 VAL B 156 REMARK 465 LYS B 157 REMARK 465 ALA B 158 REMARK 465 GLY B 159 REMARK 465 VAL B 160 REMARK 465 GLU B 161 REMARK 465 THR B 162 REMARK 465 THR B 163 REMARK 465 THR B 164 REMARK 465 PRO B 165 REMARK 465 SER B 166 REMARK 465 LYS B 167 REMARK 465 GLN B 168 REMARK 465 SER B 169 REMARK 465 ASN B 170 REMARK 465 ASN B 171 REMARK 465 LYS B 172 REMARK 465 TYR B 173 REMARK 465 ALA B 174 REMARK 465 ALA B 175 REMARK 465 SER B 176 REMARK 465 SER B 177 REMARK 465 TYR B 178 REMARK 465 LEU B 179 REMARK 465 SER B 180 REMARK 465 LEU B 181 REMARK 465 THR B 182 REMARK 465 PRO B 183 REMARK 465 GLU B 184 REMARK 465 GLN B 185 REMARK 465 TRP B 186 REMARK 465 LYS B 187 REMARK 465 SER B 188 REMARK 465 HIS B 189 REMARK 465 ARG B 190 REMARK 465 SER B 191 REMARK 465 TYR B 192 REMARK 465 SER B 193 REMARK 465 CYS B 194 REMARK 465 GLN B 195 REMARK 465 VAL B 196 REMARK 465 THR B 197 REMARK 465 HIS B 198 REMARK 465 GLU B 199 REMARK 465 GLY B 200 REMARK 465 SER B 201 REMARK 465 THR B 202 REMARK 465 VAL B 203 REMARK 465 GLU B 204 REMARK 465 LYS B 205 REMARK 465 THR B 206 REMARK 465 VAL B 207 REMARK 465 ALA B 208 REMARK 465 PRO B 209 REMARK 465 THR B 210 REMARK 465 GLU B 211 REMARK 465 CYS B 212 REMARK 465 SER B 213 REMARK 465 SER I 6 REMARK 465 TYR I 7 REMARK 465 GLN I 109 REMARK 465 PRO I 110 REMARK 465 LYS I 111 REMARK 465 ALA I 112 REMARK 465 ALA I 113 REMARK 465 PRO I 114 REMARK 465 SER I 115 REMARK 465 VAL I 116 REMARK 465 THR I 117 REMARK 465 LEU I 118 REMARK 465 PHE I 119 REMARK 465 PRO I 120 REMARK 465 PRO I 121 REMARK 465 SER I 122 REMARK 465 SER I 123 REMARK 465 GLU I 124 REMARK 465 GLU I 125 REMARK 465 LEU I 126 REMARK 465 GLN I 127 REMARK 465 ALA I 128 REMARK 465 ASN I 129 REMARK 465 LYS I 130 REMARK 465 ALA I 131 REMARK 465 THR I 132 REMARK 465 LEU I 133 REMARK 465 VAL I 134 REMARK 465 CYS I 135 REMARK 465 LEU I 136 REMARK 465 ILE I 137 REMARK 465 SER I 138 REMARK 465 ASP I 139 REMARK 465 PHE I 140 REMARK 465 TYR I 141 REMARK 465 PRO I 142 REMARK 465 GLY I 143 REMARK 465 ALA I 144 REMARK 465 VAL I 145 REMARK 465 THR I 146 REMARK 465 VAL I 147 REMARK 465 ALA I 148 REMARK 465 TRP I 149 REMARK 465 LYS I 150 REMARK 465 ALA I 151 REMARK 465 ASP I 152 REMARK 465 SER I 153 REMARK 465 SER I 154 REMARK 465 PRO I 155 REMARK 465 VAL I 156 REMARK 465 LYS I 157 REMARK 465 ALA I 158 REMARK 465 GLY I 159 REMARK 465 VAL I 160 REMARK 465 GLU I 161 REMARK 465 THR I 162 REMARK 465 THR I 163 REMARK 465 THR I 164 REMARK 465 PRO I 165 REMARK 465 SER I 166 REMARK 465 LYS I 167 REMARK 465 GLN I 168 REMARK 465 SER I 169 REMARK 465 ASN I 170 REMARK 465 ASN I 171 REMARK 465 LYS I 172 REMARK 465 TYR I 173 REMARK 465 ALA I 174 REMARK 465 ALA I 175 REMARK 465 SER I 176 REMARK 465 SER I 177 REMARK 465 TYR I 178 REMARK 465 LEU I 179 REMARK 465 SER I 180 REMARK 465 LEU I 181 REMARK 465 THR I 182 REMARK 465 PRO I 183 REMARK 465 GLU I 184 REMARK 465 GLN I 185 REMARK 465 TRP I 186 REMARK 465 LYS I 187 REMARK 465 SER I 188 REMARK 465 HIS I 189 REMARK 465 ARG I 190 REMARK 465 SER I 191 REMARK 465 TYR I 192 REMARK 465 SER I 193 REMARK 465 CYS I 194 REMARK 465 GLN I 195 REMARK 465 VAL I 196 REMARK 465 THR I 197 REMARK 465 HIS I 198 REMARK 465 GLU I 199 REMARK 465 GLY I 200 REMARK 465 SER I 201 REMARK 465 THR I 202 REMARK 465 VAL I 203 REMARK 465 GLU I 204 REMARK 465 LYS I 205 REMARK 465 THR I 206 REMARK 465 VAL I 207 REMARK 465 ALA I 208 REMARK 465 PRO I 209 REMARK 465 THR I 210 REMARK 465 GLU I 211 REMARK 465 CYS I 212 REMARK 465 SER I 213 REMARK 465 SER P 6 REMARK 465 TYR P 7 REMARK 465 GLN P 109 REMARK 465 PRO P 110 REMARK 465 LYS P 111 REMARK 465 ALA P 112 REMARK 465 ALA P 113 REMARK 465 PRO P 114 REMARK 465 SER P 115 REMARK 465 VAL P 116 REMARK 465 THR P 117 REMARK 465 LEU P 118 REMARK 465 PHE P 119 REMARK 465 PRO P 120 REMARK 465 PRO P 121 REMARK 465 SER P 122 REMARK 465 SER P 123 REMARK 465 GLU P 124 REMARK 465 GLU P 125 REMARK 465 LEU P 126 REMARK 465 GLN P 127 REMARK 465 ALA P 128 REMARK 465 ASN P 129 REMARK 465 LYS P 130 REMARK 465 ALA P 131 REMARK 465 THR P 132 REMARK 465 LEU P 133 REMARK 465 VAL P 134 REMARK 465 CYS P 135 REMARK 465 LEU P 136 REMARK 465 ILE P 137 REMARK 465 SER P 138 REMARK 465 ASP P 139 REMARK 465 PHE P 140 REMARK 465 TYR P 141 REMARK 465 PRO P 142 REMARK 465 GLY P 143 REMARK 465 ALA P 144 REMARK 465 VAL P 145 REMARK 465 THR P 146 REMARK 465 VAL P 147 REMARK 465 ALA P 148 REMARK 465 TRP P 149 REMARK 465 LYS P 150 REMARK 465 ALA P 151 REMARK 465 ASP P 152 REMARK 465 SER P 153 REMARK 465 SER P 154 REMARK 465 PRO P 155 REMARK 465 VAL P 156 REMARK 465 LYS P 157 REMARK 465 ALA P 158 REMARK 465 GLY P 159 REMARK 465 VAL P 160 REMARK 465 GLU P 161 REMARK 465 THR P 162 REMARK 465 THR P 163 REMARK 465 THR P 164 REMARK 465 PRO P 165 REMARK 465 SER P 166 REMARK 465 LYS P 167 REMARK 465 GLN P 168 REMARK 465 SER P 169 REMARK 465 ASN P 170 REMARK 465 ASN P 171 REMARK 465 LYS P 172 REMARK 465 TYR P 173 REMARK 465 ALA P 174 REMARK 465 ALA P 175 REMARK 465 SER P 176 REMARK 465 SER P 177 REMARK 465 TYR P 178 REMARK 465 LEU P 179 REMARK 465 SER P 180 REMARK 465 LEU P 181 REMARK 465 THR P 182 REMARK 465 PRO P 183 REMARK 465 GLU P 184 REMARK 465 GLN P 185 REMARK 465 TRP P 186 REMARK 465 LYS P 187 REMARK 465 SER P 188 REMARK 465 HIS P 189 REMARK 465 ARG P 190 REMARK 465 SER P 191 REMARK 465 TYR P 192 REMARK 465 SER P 193 REMARK 465 CYS P 194 REMARK 465 GLN P 195 REMARK 465 VAL P 196 REMARK 465 THR P 197 REMARK 465 HIS P 198 REMARK 465 GLU P 199 REMARK 465 GLY P 200 REMARK 465 SER P 201 REMARK 465 THR P 202 REMARK 465 VAL P 203 REMARK 465 GLU P 204 REMARK 465 LYS P 205 REMARK 465 THR P 206 REMARK 465 VAL P 207 REMARK 465 ALA P 208 REMARK 465 PRO P 209 REMARK 465 THR P 210 REMARK 465 GLU P 211 REMARK 465 CYS P 212 REMARK 465 SER P 213 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 ND2 ASN K 160 O5 NAG K 604 2.15 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 ASN C 618 CB - CA - C ANGL. DEV. = -21.6 DEGREES REMARK 500 CYS G 54 CA - CB - SG ANGL. DEV. = 8.0 DEGREES REMARK 500 LEU G 154 CA - CB - CG ANGL. DEV. = 18.4 DEGREES REMARK 500 CYS G 247 CA - CB - SG ANGL. DEV. = 8.5 DEGREES REMARK 500 CYS K 54 CA - CB - SG ANGL. DEV. = 8.3 DEGREES REMARK 500 CYS K 247 CA - CB - SG ANGL. DEV. = 7.8 DEGREES REMARK 500 CYS R 54 CA - CB - SG ANGL. DEV. = 8.1 DEGREES REMARK 500 CYS R 247 CA - CB - SG ANGL. DEV. = 7.7 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 C 611 74.78 56.93 REMARK 500 SER C 612 -4.59 -53.96 REMARK 500 ASP C 624 -34.33 -130.52 REMARK 500 ALA G 48 -166.41 -162.00 REMARK 500 ALA G 55 117.27 -161.89 REMARK 500 ALA G 70 -62.77 -103.82 REMARK 500 ALA G 135 74.08 52.20 REMARK 500 ASN G 137 40.18 37.13 REMARK 500 THR G 198 -8.33 70.33 REMARK 500 PHE G 233 110.25 -160.18 REMARK 500 GLN G 258 -13.58 72.18 REMARK 500 ASN G 262 80.61 -69.77 REMARK 500 ASN G 302 74.11 59.07 REMARK 500 ASN G 392 -151.63 -93.79 REMARK 500 SER G 393 151.17 -35.29 REMARK 500 THR G 394 -177.16 -67.50 REMARK 500 GLN G 422 -61.88 -91.26 REMARK 500 THR G 461 14.76 51.81 REMARK 500 ASN G 462 25.39 -143.36 REMARK 500 THR G 465 -129.68 -151.94 REMARK 500 ASN J 611 74.76 56.90 REMARK 500 SER J 612 -4.55 -53.99 REMARK 500 ASP J 624 -34.33 -130.51 REMARK 500 THR K 50 -169.65 -128.79 REMARK 500 ALA K 55 117.02 -161.41 REMARK 500 ALA K 70 -62.33 -101.13 REMARK 500 ASN K 88 51.35 33.21 REMARK 500 TRP K 96 -4.37 67.29 REMARK 500 ALA K 135 73.99 52.06 REMARK 500 ASN K 137 39.91 36.80 REMARK 500 LEU K 154 69.18 60.72 REMARK 500 THR K 163 -168.50 -102.49 REMARK 500 GLN K 258 -10.65 72.41 REMARK 500 ALA K 266 -169.41 -127.58 REMARK 500 ILE K 277 -33.16 -39.20 REMARK 500 ARG K 298 85.88 -157.04 REMARK 500 THR K 387 36.10 39.82 REMARK 500 ASN K 392 -150.92 -92.38 REMARK 500 SER K 393 151.58 -39.69 REMARK 500 TRP K 427 17.07 59.30 REMARK 500 ASN Q 611 74.77 56.87 REMARK 500 SER Q 612 -4.56 -53.97 REMARK 500 ASP Q 624 -34.34 -130.49 REMARK 500 ALA R 55 116.12 -161.36 REMARK 500 ALA R 70 -60.49 -99.54 REMARK 500 ASN R 88 -6.00 72.42 REMARK 500 TRP R 96 -3.31 68.91 REMARK 500 LEU R 122 59.40 -97.23 REMARK 500 ALA R 135 73.92 52.75 REMARK 500 ASN R 137 39.83 36.92 REMARK 500 REMARK 500 THIS ENTRY HAS 80 RAMACHANDRAN OUTLIERS. 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 LEU G 261 ASN G 262 -147.30 REMARK 500 ARG K 298 PRO K 299 -149.97 REMARK 500 ASN K 392 SER K 393 -149.87 REMARK 500 LEU R 261 ASN R 262 -134.34 REMARK 500 ASN R 386 THR R 387 -127.74 REMARK 500 THR R 387 SER R 388 147.07 REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG C 703 bound REMARK 800 to ASN C 611 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG C 702 bound REMARK 800 to ASN C 618 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG C 701 bound REMARK 800 to ASN C 637 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG G 601 bound REMARK 800 to ASN G 88 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG G 602 bound REMARK 800 to ASN G 160 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG G 603 bound REMARK 800 to ASN G 197 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG G 604 bound REMARK 800 to ASN G 234 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG G REMARK 800 605 through MAN G 610 bound to ASN G 262 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG G REMARK 800 611 through BMA G 613 bound to ASN G 276 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG G 614 bound REMARK 800 to ASN G 295 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG G 615 bound REMARK 800 to ASN G 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG G REMARK 800 616 through MAN G 622 bound to ASN G 332 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG G 623 bound REMARK 800 to ASN G 339 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG G 624 bound REMARK 800 to ASN G 355 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG G REMARK 800 625 through BMA G 627 bound to ASN G 386 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG G 628 bound REMARK 800 to ASN G 392 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG G REMARK 800 629 through NAG G 630 bound to ASN G 448 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG J 701 bound REMARK 800 to ASN J 611 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG J 702 bound REMARK 800 to ASN J 618 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG J 703 bound REMARK 800 to ASN J 637 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG K REMARK 800 602 through NAG K 603 bound to ASN K 88 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG K REMARK 800 604 through NAG K 605 bound to ASN K 160 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG K REMARK 800 606 through NAG K 607 bound to ASN K 197 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG K 608 bound REMARK 800 to ASN K 234 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG K REMARK 800 609 through MAN K 615 bound to ASN K 262 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG K REMARK 800 616 through BMA K 618 bound to ASN K 276 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG K 619 bound REMARK 800 to ASN K 295 REMARK 800 REMARK 800 SITE_IDENTIFIER: AF1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG K 620 bound REMARK 800 to ASN K 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: AF2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG K REMARK 800 621 through MAN K 626 bound to ASN K 332 REMARK 800 REMARK 800 SITE_IDENTIFIER: AF3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG K 627 bound REMARK 800 to ASN K 339 REMARK 800 REMARK 800 SITE_IDENTIFIER: AF4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG K 628 bound REMARK 800 to ASN K 355 REMARK 800 REMARK 800 SITE_IDENTIFIER: AF5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG K REMARK 800 629 through NAG K 630 bound to ASN K 386 REMARK 800 REMARK 800 SITE_IDENTIFIER: AF6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG K 631 bound REMARK 800 to ASN K 392 REMARK 800 REMARK 800 SITE_IDENTIFIER: AF7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG K 601 bound REMARK 800 to ASN K 448 REMARK 800 REMARK 800 SITE_IDENTIFIER: AF8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG Q 701 bound REMARK 800 to ASN Q 611 REMARK 800 REMARK 800 SITE_IDENTIFIER: AF9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG Q 702 bound REMARK 800 to ASN Q 618 REMARK 800 REMARK 800 SITE_IDENTIFIER: AG1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG Q 703 bound REMARK 800 to ASN Q 637 REMARK 800 REMARK 800 SITE_IDENTIFIER: AG2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG R REMARK 800 601 through NAG R 602 bound to ASN R 88 REMARK 800 REMARK 800 SITE_IDENTIFIER: AG3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG R REMARK 800 603 through NAG R 604 bound to ASN R 160 REMARK 800 REMARK 800 SITE_IDENTIFIER: AG4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG R REMARK 800 605 through NAG R 606 bound to ASN R 197 REMARK 800 REMARK 800 SITE_IDENTIFIER: AG5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG R 607 bound REMARK 800 to ASN R 234 REMARK 800 REMARK 800 SITE_IDENTIFIER: AG6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG R REMARK 800 608 through MAN R 613 bound to ASN R 262 REMARK 800 REMARK 800 SITE_IDENTIFIER: AG7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG R REMARK 800 614 through NAG R 615 bound to ASN R 276 REMARK 800 REMARK 800 SITE_IDENTIFIER: AG8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG R 616 bound REMARK 800 to ASN R 295 REMARK 800 REMARK 800 SITE_IDENTIFIER: AG9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG R REMARK 800 617 through NAG R 618 bound to ASN R 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: AH1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG R REMARK 800 619 through MAN R 624 bound to ASN R 332 REMARK 800 REMARK 800 SITE_IDENTIFIER: AH2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG R 625 bound REMARK 800 to ASN R 339 REMARK 800 REMARK 800 SITE_IDENTIFIER: AH3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG R 626 bound REMARK 800 to ASN R 355 REMARK 800 REMARK 800 SITE_IDENTIFIER: AH4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG R REMARK 800 627 through NAG R 628 bound to ASN R 386 REMARK 800 REMARK 800 SITE_IDENTIFIER: AH5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG R 629 bound REMARK 800 to ASN R 392 REMARK 800 REMARK 800 SITE_IDENTIFIER: AH6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG R REMARK 800 630 through NAG R 631 bound to ASN R 448 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-20175 RELATED DB: EMDB REMARK 900 MODIFIED BG505 SOSIP-BASED IMMUNOGEN RC1 IN COMPLEX WITH THE REMARK 900 ELICITED V3-GLYCAN PATCH BNAB 10-1074 DBREF 6ORN C 512 664 PDB 6ORN 6ORN 512 664 DBREF 6ORN G 31 513 PDB 6ORN 6ORN 31 513 DBREF 6ORN J 512 664 PDB 6ORN 6ORN 512 664 DBREF 6ORN K 31 513 PDB 6ORN 6ORN 31 513 DBREF 6ORN Q 512 664 PDB 6ORN 6ORN 512 664 DBREF 6ORN R 31 513 PDB 6ORN 6ORN 31 513 DBREF 6ORN A 1 238 PDB 6ORN 6ORN 1 238 DBREF 6ORN F 1 219 PDB 6ORN 6ORN 1 219 DBREF 6ORN O 1 219 PDB 6ORN 6ORN 1 219 DBREF 6ORN B 6 213 PDB 6ORN 6ORN 6 213 DBREF 6ORN I 6 213 PDB 6ORN 6ORN 6 213 DBREF 6ORN P 6 213 PDB 6ORN 6ORN 6 213 SEQRES 1 C 153 ALA VAL GLY ILE GLY ALA VAL SER LEU GLY PHE LEU GLY SEQRES 2 C 153 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 C 153 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 C 153 GLN GLN SER ASN LEU LEU ARG ALA PRO GLU PRO GLN GLN SEQRES 5 C 153 HIS LEU LEU LYS ASP THR HIS TRP GLY ILE LYS GLN LEU SEQRES 6 C 153 GLN ALA ARG VAL LEU ALA VAL GLU HIS TYR LEU ARG ASP SEQRES 7 C 153 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 C 153 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 C 153 ASN ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 C 153 LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE SEQRES 11 C 153 ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 C 153 LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP SEQRES 1 G 481 ALA GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO SEQRES 2 G 481 VAL TRP LYS ASP ALA GLU THR THR LEU PHE CYS ALA SER SEQRES 3 G 481 ASP ALA LYS ALA TYR GLU THR GLU LYS HIS ASN VAL TRP SEQRES 4 G 481 ALA THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN SEQRES 5 G 481 GLU ILE HIS LEU GLU ASN VAL THR GLU GLU PHE ASN MET SEQRES 6 G 481 TRP LYS ASN ASN MET VAL GLU GLN MET HIS GLU ASP ILE SEQRES 7 G 481 ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS SEQRES 8 G 481 LEU THR PRO LEU CYS VAL THR LEU GLN CYS THR ASN TYR SEQRES 9 G 481 ALA PRO ASN LEU LEU SER ASN MET ARG GLY GLU LEU LYS SEQRES 10 G 481 GLN CYS SER PHE ASN MET THR THR GLU LEU ARG ASP LYS SEQRES 11 G 481 LYS GLN LYS VAL TYR SER LEU PHE TYR ARG LEU ASP VAL SEQRES 12 G 481 VAL GLN ILE ASN GLU ASN GLN GLY ASN ARG SER ASN ASN SEQRES 13 G 481 SER ASN LYS GLU TYR ARG LEU ILE ASN CYS ASN THR SER SEQRES 14 G 481 ALA ILE THR GLN ALA CYS PRO LYS VAL SER PHE GLU PRO SEQRES 15 G 481 ILE PRO ILE HIS TYR CYS ALA PRO ALA GLY PHE ALA ILE SEQRES 16 G 481 LEU LYS CYS LYS ASP LYS LYS PHE ASN GLY THR GLY PRO SEQRES 17 G 481 CYS PRO SER VAL SER THR VAL GLN CYS THR HIS GLY ILE SEQRES 18 G 481 LYS PRO VAL VAL SER THR GLN LEU LEU LEU ASN GLY SER SEQRES 19 G 481 LEU ALA GLU GLU GLU VAL ILE ILE ARG SER GLU ASN ILE SEQRES 20 G 481 THR ASN ASN ALA LYS ASN ILE LEU VAL GLN LEU ASN THR SEQRES 21 G 481 PRO VAL GLN ILE ASN CYS THR ARG PRO ASN ASN ASN THR SEQRES 22 G 481 VAL LYS SER ILE ARG ILE GLY PRO GLY GLN ALA PHE TYR SEQRES 23 G 481 TYR PHE GLY ASP ILE ILE GLY ASP ILE ARG MET ALA HIS SEQRES 24 G 481 CYS ASN VAL SER LYS ALA THR TRP ASN GLU THR LEU GLY SEQRES 25 G 481 LYS VAL VAL LYS GLN LEU ARG LYS HIS PHE GLY ASN ASN SEQRES 26 G 481 THR ILE ILE ARG PHE ALA GLN SER SER GLY GLY ASP LEU SEQRES 27 G 481 GLU VAL THR THR HIS SER PHE ASN CYS GLY GLY GLU PHE SEQRES 28 G 481 PHE TYR CYS ASN THR SER GLY LEU PHE ASN SER THR TRP SEQRES 29 G 481 ILE SER ASN THR SER VAL GLN GLY SER ASN SER THR GLY SEQRES 30 G 481 SER ASN ASP SER ILE VAL LEU PRO CYS ARG ILE LYS GLN SEQRES 31 G 481 ILE ILE ASN MET TRP GLN ARG ILE GLY GLN ALA MET TYR SEQRES 32 G 481 ALA PRO PRO ILE GLN GLY VAL ILE ARG CYS VAL SER ASN SEQRES 33 G 481 ILE THR GLY LEU ILE LEU THR ARG ASP GLY GLY SER THR SEQRES 34 G 481 ASN SER THR THR GLU THR PHE ARG PRO GLY GLY GLY ASP SEQRES 35 G 481 MET ARG ASP ASN TRP ARG SER GLU LEU TYR LYS TYR LYS SEQRES 36 G 481 VAL VAL LYS ILE GLU PRO LEU GLY VAL ALA PRO THR ARG SEQRES 37 G 481 CYS LYS ARG ARG VAL VAL GLY ARG ARG ARG ARG ARG ARG SEQRES 1 J 153 ALA VAL GLY ILE GLY ALA VAL SER LEU GLY PHE LEU GLY SEQRES 2 J 153 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 J 153 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 J 153 GLN GLN SER ASN LEU LEU ARG ALA PRO GLU PRO GLN GLN SEQRES 5 J 153 HIS LEU LEU LYS ASP THR HIS TRP GLY ILE LYS GLN LEU SEQRES 6 J 153 GLN ALA ARG VAL LEU ALA VAL GLU HIS TYR LEU ARG ASP SEQRES 7 J 153 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 J 153 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 J 153 ASN ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 J 153 LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE SEQRES 11 J 153 ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 J 153 LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP SEQRES 1 K 481 ALA GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO SEQRES 2 K 481 VAL TRP LYS ASP ALA GLU THR THR LEU PHE CYS ALA SER SEQRES 3 K 481 ASP ALA LYS ALA TYR GLU THR GLU LYS HIS ASN VAL TRP SEQRES 4 K 481 ALA THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN SEQRES 5 K 481 GLU ILE HIS LEU GLU ASN VAL THR GLU GLU PHE ASN MET SEQRES 6 K 481 TRP LYS ASN ASN MET VAL GLU GLN MET HIS GLU ASP ILE SEQRES 7 K 481 ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS SEQRES 8 K 481 LEU THR PRO LEU CYS VAL THR LEU GLN CYS THR ASN TYR SEQRES 9 K 481 ALA PRO ASN LEU LEU SER ASN MET ARG GLY GLU LEU LYS SEQRES 10 K 481 GLN CYS SER PHE ASN MET THR THR GLU LEU ARG ASP LYS SEQRES 11 K 481 LYS GLN LYS VAL TYR SER LEU PHE TYR ARG LEU ASP VAL SEQRES 12 K 481 VAL GLN ILE ASN GLU ASN GLN GLY ASN ARG SER ASN ASN SEQRES 13 K 481 SER ASN LYS GLU TYR ARG LEU ILE ASN CYS ASN THR SER SEQRES 14 K 481 ALA ILE THR GLN ALA CYS PRO LYS VAL SER PHE GLU PRO SEQRES 15 K 481 ILE PRO ILE HIS TYR CYS ALA PRO ALA GLY PHE ALA ILE SEQRES 16 K 481 LEU LYS CYS LYS ASP LYS LYS PHE ASN GLY THR GLY PRO SEQRES 17 K 481 CYS PRO SER VAL SER THR VAL GLN CYS THR HIS GLY ILE SEQRES 18 K 481 LYS PRO VAL VAL SER THR GLN LEU LEU LEU ASN GLY SER SEQRES 19 K 481 LEU ALA GLU GLU GLU VAL ILE ILE ARG SER GLU ASN ILE SEQRES 20 K 481 THR ASN ASN ALA LYS ASN ILE LEU VAL GLN LEU ASN THR SEQRES 21 K 481 PRO VAL GLN ILE ASN CYS THR ARG PRO ASN ASN ASN THR SEQRES 22 K 481 VAL LYS SER ILE ARG ILE GLY PRO GLY GLN ALA PHE TYR SEQRES 23 K 481 TYR PHE GLY ASP ILE ILE GLY ASP ILE ARG MET ALA HIS SEQRES 24 K 481 CYS ASN VAL SER LYS ALA THR TRP ASN GLU THR LEU GLY SEQRES 25 K 481 LYS VAL VAL LYS GLN LEU ARG LYS HIS PHE GLY ASN ASN SEQRES 26 K 481 THR ILE ILE ARG PHE ALA GLN SER SER GLY GLY ASP LEU SEQRES 27 K 481 GLU VAL THR THR HIS SER PHE ASN CYS GLY GLY GLU PHE SEQRES 28 K 481 PHE TYR CYS ASN THR SER GLY LEU PHE ASN SER THR TRP SEQRES 29 K 481 ILE SER ASN THR SER VAL GLN GLY SER ASN SER THR GLY SEQRES 30 K 481 SER ASN ASP SER ILE VAL LEU PRO CYS ARG ILE LYS GLN SEQRES 31 K 481 ILE ILE ASN MET TRP GLN ARG ILE GLY GLN ALA MET TYR SEQRES 32 K 481 ALA PRO PRO ILE GLN GLY VAL ILE ARG CYS VAL SER ASN SEQRES 33 K 481 ILE THR GLY LEU ILE LEU THR ARG ASP GLY GLY SER THR SEQRES 34 K 481 ASN SER THR THR GLU THR PHE ARG PRO GLY GLY GLY ASP SEQRES 35 K 481 MET ARG ASP ASN TRP ARG SER GLU LEU TYR LYS TYR LYS SEQRES 36 K 481 VAL VAL LYS ILE GLU PRO LEU GLY VAL ALA PRO THR ARG SEQRES 37 K 481 CYS LYS ARG ARG VAL VAL GLY ARG ARG ARG ARG ARG ARG SEQRES 1 Q 153 ALA VAL GLY ILE GLY ALA VAL SER LEU GLY PHE LEU GLY SEQRES 2 Q 153 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 Q 153 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 Q 153 GLN GLN SER ASN LEU LEU ARG ALA PRO GLU PRO GLN GLN SEQRES 5 Q 153 HIS LEU LEU LYS ASP THR HIS TRP GLY ILE LYS GLN LEU SEQRES 6 Q 153 GLN ALA ARG VAL LEU ALA VAL GLU HIS TYR LEU ARG ASP SEQRES 7 Q 153 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 Q 153 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 Q 153 ASN ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 Q 153 LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE SEQRES 11 Q 153 ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 Q 153 LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP SEQRES 1 R 481 ALA GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO SEQRES 2 R 481 VAL TRP LYS ASP ALA GLU THR THR LEU PHE CYS ALA SER SEQRES 3 R 481 ASP ALA LYS ALA TYR GLU THR GLU LYS HIS ASN VAL TRP SEQRES 4 R 481 ALA THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN SEQRES 5 R 481 GLU ILE HIS LEU GLU ASN VAL THR GLU GLU PHE ASN MET SEQRES 6 R 481 TRP LYS ASN ASN MET VAL GLU GLN MET HIS GLU ASP ILE SEQRES 7 R 481 ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS SEQRES 8 R 481 LEU THR PRO LEU CYS VAL THR LEU GLN CYS THR ASN TYR SEQRES 9 R 481 ALA PRO ASN LEU LEU SER ASN MET ARG GLY GLU LEU LYS SEQRES 10 R 481 GLN CYS SER PHE ASN MET THR THR GLU LEU ARG ASP LYS SEQRES 11 R 481 LYS GLN LYS VAL TYR SER LEU PHE TYR ARG LEU ASP VAL SEQRES 12 R 481 VAL GLN ILE ASN GLU ASN GLN GLY ASN ARG SER ASN ASN SEQRES 13 R 481 SER ASN LYS GLU TYR ARG LEU ILE ASN CYS ASN THR SER SEQRES 14 R 481 ALA ILE THR GLN ALA CYS PRO LYS VAL SER PHE GLU PRO SEQRES 15 R 481 ILE PRO ILE HIS TYR CYS ALA PRO ALA GLY PHE ALA ILE SEQRES 16 R 481 LEU LYS CYS LYS ASP LYS LYS PHE ASN GLY THR GLY PRO SEQRES 17 R 481 CYS PRO SER VAL SER THR VAL GLN CYS THR HIS GLY ILE SEQRES 18 R 481 LYS PRO VAL VAL SER THR GLN LEU LEU LEU ASN GLY SER SEQRES 19 R 481 LEU ALA GLU GLU GLU VAL ILE ILE ARG SER GLU ASN ILE SEQRES 20 R 481 THR ASN ASN ALA LYS ASN ILE LEU VAL GLN LEU ASN THR SEQRES 21 R 481 PRO VAL GLN ILE ASN CYS THR ARG PRO ASN ASN ASN THR SEQRES 22 R 481 VAL LYS SER ILE ARG ILE GLY PRO GLY GLN ALA PHE TYR SEQRES 23 R 481 TYR PHE GLY ASP ILE ILE GLY ASP ILE ARG MET ALA HIS SEQRES 24 R 481 CYS ASN VAL SER LYS ALA THR TRP ASN GLU THR LEU GLY SEQRES 25 R 481 LYS VAL VAL LYS GLN LEU ARG LYS HIS PHE GLY ASN ASN SEQRES 26 R 481 THR ILE ILE ARG PHE ALA GLN SER SER GLY GLY ASP LEU SEQRES 27 R 481 GLU VAL THR THR HIS SER PHE ASN CYS GLY GLY GLU PHE SEQRES 28 R 481 PHE TYR CYS ASN THR SER GLY LEU PHE ASN SER THR TRP SEQRES 29 R 481 ILE SER ASN THR SER VAL GLN GLY SER ASN SER THR GLY SEQRES 30 R 481 SER ASN ASP SER ILE VAL LEU PRO CYS ARG ILE LYS GLN SEQRES 31 R 481 ILE ILE ASN MET TRP GLN ARG ILE GLY GLN ALA MET TYR SEQRES 32 R 481 ALA PRO PRO ILE GLN GLY VAL ILE ARG CYS VAL SER ASN SEQRES 33 R 481 ILE THR GLY LEU ILE LEU THR ARG ASP GLY GLY SER THR SEQRES 34 R 481 ASN SER THR THR GLU THR PHE ARG PRO GLY GLY GLY ASP SEQRES 35 R 481 MET ARG ASP ASN TRP ARG SER GLU LEU TYR LYS TYR LYS SEQRES 36 R 481 VAL VAL LYS ILE GLU PRO LEU GLY VAL ALA PRO THR ARG SEQRES 37 R 481 CYS LYS ARG ARG VAL VAL GLY ARG ARG ARG ARG ARG ARG SEQRES 1 A 238 GLN VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 A 238 PRO SER GLU THR LEU SER VAL THR CYS SER VAL SER GLY SEQRES 3 A 238 ASP SER MET ASN ASN TYR TYR TRP THR TRP ILE ARG GLN SEQRES 4 A 238 SER PRO GLY LYS GLY LEU GLU TRP ILE GLY TYR ILE SER SEQRES 5 A 238 ASP ARG GLU SER ALA THR TYR ASN PRO SER LEU ASN SER SEQRES 6 A 238 ARG VAL VAL ILE SER ARG ASP THR SER LYS ASN GLN LEU SEQRES 7 A 238 SER LEU LYS LEU ASN SER VAL THR PRO ALA ASP THR ALA SEQRES 8 A 238 VAL TYR TYR CYS ALA THR ALA ARG ARG GLY GLN ARG ILE SEQRES 9 A 238 TYR GLY VAL VAL SER PHE GLY GLU PHE PHE TYR TYR TYR SEQRES 10 A 238 SER MET ASP VAL TRP GLY LYS GLY THR THR VAL THR VAL SEQRES 11 A 238 SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU SEQRES 12 A 238 ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA SEQRES 13 A 238 LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL SEQRES 14 A 238 THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL SEQRES 15 A 238 HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SEQRES 16 A 238 SER LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU SEQRES 17 A 238 GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SEQRES 18 A 238 SER ASN THR LYS VAL ASP LYS ARG VAL GLU PRO LYS SER SEQRES 19 A 238 CYS ASP LYS THR SEQRES 1 F 238 GLN VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 F 238 PRO SER GLU THR LEU SER VAL THR CYS SER VAL SER GLY SEQRES 3 F 238 ASP SER MET ASN ASN TYR TYR TRP THR TRP ILE ARG GLN SEQRES 4 F 238 SER PRO GLY LYS GLY LEU GLU TRP ILE GLY TYR ILE SER SEQRES 5 F 238 ASP ARG GLU SER ALA THR TYR ASN PRO SER LEU ASN SER SEQRES 6 F 238 ARG VAL VAL ILE SER ARG ASP THR SER LYS ASN GLN LEU SEQRES 7 F 238 SER LEU LYS LEU ASN SER VAL THR PRO ALA ASP THR ALA SEQRES 8 F 238 VAL TYR TYR CYS ALA THR ALA ARG ARG GLY GLN ARG ILE SEQRES 9 F 238 TYR GLY VAL VAL SER PHE GLY GLU PHE PHE TYR TYR TYR SEQRES 10 F 238 SER MET ASP VAL TRP GLY LYS GLY THR THR VAL THR VAL SEQRES 11 F 238 SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU SEQRES 12 F 238 ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA SEQRES 13 F 238 LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL SEQRES 14 F 238 THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL SEQRES 15 F 238 HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SEQRES 16 F 238 SER LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU SEQRES 17 F 238 GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SEQRES 18 F 238 SER ASN THR LYS VAL ASP LYS ARG VAL GLU PRO LYS SER SEQRES 19 F 238 CYS ASP LYS THR SEQRES 1 O 238 GLN VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 O 238 PRO SER GLU THR LEU SER VAL THR CYS SER VAL SER GLY SEQRES 3 O 238 ASP SER MET ASN ASN TYR TYR TRP THR TRP ILE ARG GLN SEQRES 4 O 238 SER PRO GLY LYS GLY LEU GLU TRP ILE GLY TYR ILE SER SEQRES 5 O 238 ASP ARG GLU SER ALA THR TYR ASN PRO SER LEU ASN SER SEQRES 6 O 238 ARG VAL VAL ILE SER ARG ASP THR SER LYS ASN GLN LEU SEQRES 7 O 238 SER LEU LYS LEU ASN SER VAL THR PRO ALA ASP THR ALA SEQRES 8 O 238 VAL TYR TYR CYS ALA THR ALA ARG ARG GLY GLN ARG ILE SEQRES 9 O 238 TYR GLY VAL VAL SER PHE GLY GLU PHE PHE TYR TYR TYR SEQRES 10 O 238 SER MET ASP VAL TRP GLY LYS GLY THR THR VAL THR VAL SEQRES 11 O 238 SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU SEQRES 12 O 238 ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA SEQRES 13 O 238 LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL SEQRES 14 O 238 THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL SEQRES 15 O 238 HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SEQRES 16 O 238 SER LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU SEQRES 17 O 238 GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SEQRES 18 O 238 SER ASN THR LYS VAL ASP LYS ARG VAL GLU PRO LYS SER SEQRES 19 O 238 CYS ASP LYS THR SEQRES 1 B 214 SER TYR VAL ARG PRO LEU SER VAL ALA LEU GLY GLU THR SEQRES 2 B 214 ALA ARG ILE SER CYS GLY ARG GLN ALA LEU GLY SER ARG SEQRES 3 B 214 ALA VAL GLN TRP TYR GLN HIS ARG PRO GLY GLN ALA PRO SEQRES 4 B 214 ILE LEU LEU ILE TYR ASN ASN GLN ASP ARG PRO SER GLY SEQRES 5 B 214 ILE PRO GLU ARG PHE SER GLY THR PRO ASP ILE ASN PHE SEQRES 6 B 214 GLY THR ARG ALA THR LEU THR ILE SER GLY VAL GLU ALA SEQRES 7 B 214 GLY ASP GLU ALA ASP TYR TYR CYS HIS MET TRP ASP SER SEQRES 8 B 214 ARG SER GLY PHE SER TRP SER PHE GLY GLY ALA THR ARG SEQRES 9 B 214 LEU THR VAL LEU GLY GLN PRO LYS ALA ALA PRO SER VAL SEQRES 10 B 214 THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN ALA ASN SEQRES 11 B 214 LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE TYR PRO SEQRES 12 B 214 GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER SER PRO SEQRES 13 B 214 VAL LYS ALA GLY VAL GLU THR THR THR PRO SER LYS GLN SEQRES 14 B 214 SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SER LEU SEQRES 15 B 214 THR PRO GLU GLN TRP LYS SER HIS ARG SER TYR SER CYS SEQRES 16 B 214 GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS THR VAL SEQRES 17 B 214 ALA PRO THR GLU CYS SER SEQRES 1 I 214 SER TYR VAL ARG PRO LEU SER VAL ALA LEU GLY GLU THR SEQRES 2 I 214 ALA ARG ILE SER CYS GLY ARG GLN ALA LEU GLY SER ARG SEQRES 3 I 214 ALA VAL GLN TRP TYR GLN HIS ARG PRO GLY GLN ALA PRO SEQRES 4 I 214 ILE LEU LEU ILE TYR ASN ASN GLN ASP ARG PRO SER GLY SEQRES 5 I 214 ILE PRO GLU ARG PHE SER GLY THR PRO ASP ILE ASN PHE SEQRES 6 I 214 GLY THR ARG ALA THR LEU THR ILE SER GLY VAL GLU ALA SEQRES 7 I 214 GLY ASP GLU ALA ASP TYR TYR CYS HIS MET TRP ASP SER SEQRES 8 I 214 ARG SER GLY PHE SER TRP SER PHE GLY GLY ALA THR ARG SEQRES 9 I 214 LEU THR VAL LEU GLY GLN PRO LYS ALA ALA PRO SER VAL SEQRES 10 I 214 THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN ALA ASN SEQRES 11 I 214 LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE TYR PRO SEQRES 12 I 214 GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER SER PRO SEQRES 13 I 214 VAL LYS ALA GLY VAL GLU THR THR THR PRO SER LYS GLN SEQRES 14 I 214 SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SER LEU SEQRES 15 I 214 THR PRO GLU GLN TRP LYS SER HIS ARG SER TYR SER CYS SEQRES 16 I 214 GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS THR VAL SEQRES 17 I 214 ALA PRO THR GLU CYS SER SEQRES 1 P 214 SER TYR VAL ARG PRO LEU SER VAL ALA LEU GLY GLU THR SEQRES 2 P 214 ALA ARG ILE SER CYS GLY ARG GLN ALA LEU GLY SER ARG SEQRES 3 P 214 ALA VAL GLN TRP TYR GLN HIS ARG PRO GLY GLN ALA PRO SEQRES 4 P 214 ILE LEU LEU ILE TYR ASN ASN GLN ASP ARG PRO SER GLY SEQRES 5 P 214 ILE PRO GLU ARG PHE SER GLY THR PRO ASP ILE ASN PHE SEQRES 6 P 214 GLY THR ARG ALA THR LEU THR ILE SER GLY VAL GLU ALA SEQRES 7 P 214 GLY ASP GLU ALA ASP TYR TYR CYS HIS MET TRP ASP SER SEQRES 8 P 214 ARG SER GLY PHE SER TRP SER PHE GLY GLY ALA THR ARG SEQRES 9 P 214 LEU THR VAL LEU GLY GLN PRO LYS ALA ALA PRO SER VAL SEQRES 10 P 214 THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN ALA ASN SEQRES 11 P 214 LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE TYR PRO SEQRES 12 P 214 GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER SER PRO SEQRES 13 P 214 VAL LYS ALA GLY VAL GLU THR THR THR PRO SER LYS GLN SEQRES 14 P 214 SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SER LEU SEQRES 15 P 214 THR PRO GLU GLN TRP LYS SER HIS ARG SER TYR SER CYS SEQRES 16 P 214 GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS THR VAL SEQRES 17 P 214 ALA PRO THR GLU CYS SER HET NAG C 701 14 HET NAG C 702 14 HET NAG C 703 14 HET NAG G 601 14 HET NAG G 602 14 HET NAG G 603 14 HET NAG G 604 14 HET NAG G 605 14 HET NAG G 606 14 HET BMA G 607 11 HET MAN G 608 11 HET MAN G 609 11 HET MAN G 610 11 HET NAG G 611 14 HET NAG G 612 14 HET BMA G 613 11 HET NAG G 614 14 HET NAG G 615 14 HET NAG G 616 14 HET NAG G 617 14 HET BMA G 618 11 HET MAN G 619 11 HET MAN G 620 11 HET MAN G 621 11 HET MAN G 622 11 HET NAG G 623 14 HET NAG G 624 14 HET NAG G 625 14 HET NAG G 626 14 HET BMA G 627 11 HET NAG G 628 14 HET NAG G 629 14 HET NAG G 630 14 HET NAG J 701 14 HET NAG J 702 14 HET NAG J 703 14 HET NAG K 601 14 HET NAG K 602 14 HET NAG K 603 14 HET NAG K 604 14 HET NAG K 605 14 HET NAG K 606 14 HET NAG K 607 14 HET NAG K 608 14 HET NAG K 609 14 HET NAG K 610 14 HET BMA K 611 11 HET MAN K 612 11 HET MAN K 613 11 HET MAN K 614 11 HET MAN K 615 11 HET NAG K 616 14 HET NAG K 617 14 HET BMA K 618 11 HET NAG K 619 14 HET NAG K 620 14 HET NAG K 621 14 HET NAG K 622 14 HET BMA K 623 11 HET MAN K 624 11 HET MAN K 625 11 HET MAN K 626 11 HET NAG K 627 14 HET NAG K 628 14 HET NAG K 629 14 HET NAG K 630 14 HET NAG K 631 14 HET NAG Q 701 14 HET NAG Q 702 14 HET NAG Q 703 14 HET NAG R 601 14 HET NAG R 602 14 HET NAG R 603 14 HET NAG R 604 14 HET NAG R 605 14 HET NAG R 606 14 HET NAG R 607 14 HET NAG R 608 14 HET NAG R 609 14 HET BMA R 610 11 HET MAN R 611 11 HET MAN R 612 11 HET MAN R 613 11 HET NAG R 614 14 HET NAG R 615 14 HET NAG R 616 14 HET NAG R 617 14 HET NAG R 618 14 HET NAG R 619 14 HET NAG R 620 14 HET BMA R 621 11 HET MAN R 622 11 HET MAN R 623 11 HET MAN R 624 11 HET NAG R 625 14 HET NAG R 626 14 HET NAG R 627 14 HET NAG R 628 14 HET NAG R 629 14 HET NAG R 630 14 HET NAG R 631 14 HETNAM NAG N-ACETYL-D-GLUCOSAMINE HETNAM BMA BETA-D-MANNOSE HETNAM MAN ALPHA-D-MANNOSE FORMUL 13 NAG 72(C8 H15 N O6) FORMUL 20 BMA 9(C6 H12 O6) FORMUL 20 MAN 20(C6 H12 O6) HELIX 1 AA1 THR C 529 SER C 534 1 6 HELIX 2 AA2 LEU C 537 ASN C 543 1 7 HELIX 3 AA3 ILE C 573 TRP C 596 1 24 HELIX 4 AA4 THR C 627 SER C 636 1 10 HELIX 5 AA5 TYR C 638 ALA C 662 1 25 HELIX 6 AA6 ASN G 99 SER G 115 1 17 HELIX 7 AA7 TYR G 177 LEU G 179 5 3 HELIX 8 AA8 LYS G 335 ARG G 350 1 16 HELIX 9 AA9 LYS G 351 PHE G 353 5 3 HELIX 10 AB1 ASP G 368 THR G 373 1 6 HELIX 11 AB2 THR G 387 PHE G 391 5 5 HELIX 12 AB3 ASN G 425 ARG G 429 5 5 HELIX 13 AB4 ARG G 476 SER G 481 1 6 HELIX 14 AB5 THR J 529 SER J 534 1 6 HELIX 15 AB6 LEU J 537 ASN J 543 1 7 HELIX 16 AB7 ILE J 573 TRP J 596 1 24 HELIX 17 AB8 THR J 627 SER J 636 1 10 HELIX 18 AB9 TYR J 638 ALA J 662 1 25 HELIX 19 AC1 ASN K 99 SER K 115 1 17 HELIX 20 AC2 TYR K 177 LEU K 179 5 3 HELIX 21 AC3 LYS K 335 ARG K 350 1 16 HELIX 22 AC4 LYS K 351 PHE K 353 5 3 HELIX 23 AC5 ASP K 368 THR K 373 1 6 HELIX 24 AC6 THR K 387 PHE K 391 5 5 HELIX 25 AC7 ASN K 425 ARG K 429 5 5 HELIX 26 AC8 ARG K 476 SER K 481 1 6 HELIX 27 AC9 THR Q 529 SER Q 534 1 6 HELIX 28 AD1 LEU Q 537 ASN Q 543 1 7 HELIX 29 AD2 ILE Q 573 TRP Q 596 1 24 HELIX 30 AD3 THR Q 627 SER Q 636 1 10 HELIX 31 AD4 TYR Q 638 ALA Q 662 1 25 HELIX 32 AD5 ASN R 99 SER R 115 1 17 HELIX 33 AD6 TYR R 177 LEU R 179 5 3 HELIX 34 AD7 LYS R 335 ARG R 350 1 16 HELIX 35 AD8 LYS R 351 PHE R 353 5 3 HELIX 36 AD9 ASP R 368 THR R 373 1 6 HELIX 37 AE1 THR R 387 PHE R 391 5 5 HELIX 38 AE2 ASN R 425 ARG R 429 5 5 HELIX 39 AE3 ARG R 476 SER R 481 1 6 SHEET 1 AA1 2 TRP G 35 TYR G 40 0 SHEET 2 AA1 2 LEU G 494 THR G 499 -1 O THR G 499 N TRP G 35 SHEET 1 AA2 5 TRP G 45 LYS G 46 0 SHEET 2 AA2 5 LYS G 487 ILE G 491 -1 O LYS G 490 N LYS G 46 SHEET 3 AA2 5 PHE G 223 CYS G 228 -1 N LEU G 226 O LYS G 487 SHEET 4 AA2 5 VAL G 242 VAL G 245 -1 O VAL G 245 N ILE G 225 SHEET 5 AA2 5 ILE G 84 HIS G 85 -1 N ILE G 84 O THR G 244 SHEET 1 AA3 2 GLU G 91 ASN G 94 0 SHEET 2 AA3 2 THR G 236 CYS G 239 -1 O GLY G 237 N PHE G 93 SHEET 1 AA4 5 LYS G 169 PHE G 176 0 SHEET 2 AA4 5 LYS G 155 THR G 162 -1 N LYS G 155 O PHE G 176 SHEET 3 AA4 5 LEU G 129 ASN G 133 -1 N THR G 132 O GLN G 156 SHEET 4 AA4 5 LYS G 189 LEU G 193 -1 O TYR G 191 N LEU G 129 SHEET 5 AA4 5 VAL G 181 GLN G 183 -1 N VAL G 182 O ARG G 192 SHEET 1 AA5 2 SER G 199 GLN G 203 0 SHEET 2 AA5 2 GLY G 431 TYR G 435 1 O TYR G 435 N THR G 202 SHEET 1 AA6 4 ILE G 271 ARG G 273 0 SHEET 2 AA6 4 ILE G 284 GLN G 287 -1 O LEU G 285 N ARG G 273 SHEET 3 AA6 4 ILE G 453 ARG G 456 -1 O LEU G 454 N ILE G 284 SHEET 4 AA6 4 PHE G 468 PRO G 470 -1 O ARG G 469 N THR G 455 SHEET 1 AA7 5 TYR G 384 CYS G 385 0 SHEET 2 AA7 5 SER G 413 ARG G 419 -1 O ARG G 419 N TYR G 384 SHEET 3 AA7 5 HIS G 330 SER G 334 -1 N VAL G 333 O ILE G 414 SHEET 4 AA7 5 VAL G 292 ARG G 298 -1 N ASN G 295 O ASN G 332 SHEET 5 AA7 5 ILE G 443 ILE G 449 -1 O CYS G 445 N CYS G 296 SHEET 1 AA8 2 VAL G 304 ILE G 307 0 SHEET 2 AA8 2 PHE G 317 PHE G 320 -1 O PHE G 317 N ILE G 307 SHEET 1 AA9 2 ASN G 377 CYS G 378 0 SHEET 2 AA9 2 GLU G 381 PHE G 382 -1 O GLU G 381 N CYS G 378 SHEET 1 AB1 2 TRP K 35 TYR K 40 0 SHEET 2 AB1 2 LEU K 494 THR K 499 -1 O THR K 499 N TRP K 35 SHEET 1 AB2 5 TRP K 45 LYS K 46 0 SHEET 2 AB2 5 LYS K 487 ILE K 491 -1 O LYS K 490 N LYS K 46 SHEET 3 AB2 5 PHE K 223 CYS K 228 -1 N LEU K 226 O LYS K 487 SHEET 4 AB2 5 VAL K 242 VAL K 245 -1 O VAL K 245 N ILE K 225 SHEET 5 AB2 5 ILE K 84 HIS K 85 -1 N ILE K 84 O THR K 244 SHEET 1 AB3 2 GLU K 91 ASN K 94 0 SHEET 2 AB3 2 THR K 236 CYS K 239 -1 O CYS K 239 N GLU K 91 SHEET 1 AB4 5 LYS K 169 PHE K 176 0 SHEET 2 AB4 5 LYS K 155 THR K 162 -1 N LYS K 155 O PHE K 176 SHEET 3 AB4 5 LEU K 129 ASN K 133 -1 N THR K 132 O GLN K 156 SHEET 4 AB4 5 LYS K 189 LEU K 193 -1 O TYR K 191 N LEU K 129 SHEET 5 AB4 5 VAL K 181 GLN K 183 -1 N VAL K 182 O ARG K 192 SHEET 1 AB5 2 ALA K 200 GLN K 203 0 SHEET 2 AB5 2 GLN K 432 TYR K 435 1 O ALA K 433 N THR K 202 SHEET 1 AB6 4 LEU K 259 LEU K 261 0 SHEET 2 AB6 4 ILE K 443 ARG K 456 -1 O THR K 450 N LEU K 260 SHEET 3 AB6 4 THR K 465 ARG K 469 -1 O ARG K 469 N THR K 455 SHEET 4 AB6 4 ILE K 358 PHE K 361 1 N ILE K 358 O GLU K 466 SHEET 1 AB7 8 ILE K 271 ARG K 273 0 SHEET 2 AB7 8 ILE K 284 GLN K 287 -1 O LEU K 285 N ARG K 273 SHEET 3 AB7 8 ILE K 443 ARG K 456 -1 O LEU K 454 N ILE K 284 SHEET 4 AB7 8 VAL K 292 ARG K 298 -1 N VAL K 292 O ILE K 449 SHEET 5 AB7 8 HIS K 330 SER K 334 -1 O ASN K 332 N ASN K 295 SHEET 6 AB7 8 SER K 413 ILE K 420 -1 O ILE K 414 N VAL K 333 SHEET 7 AB7 8 GLU K 381 CYS K 385 -1 N TYR K 384 O ARG K 419 SHEET 8 AB7 8 HIS K 374 CYS K 378 -1 N HIS K 374 O CYS K 385 SHEET 1 AB8 2 ASN K 302 ILE K 307 0 SHEET 2 AB8 2 PHE K 317 ILE K 322 -1 O PHE K 317 N ILE K 307 SHEET 1 AB9 2 TRP R 35 TYR R 40 0 SHEET 2 AB9 2 LEU R 494 THR R 499 -1 O GLY R 495 N TYR R 39 SHEET 1 AC1 5 TRP R 45 LYS R 46 0 SHEET 2 AC1 5 LYS R 487 ILE R 491 -1 O LYS R 490 N LYS R 46 SHEET 3 AC1 5 PHE R 223 CYS R 228 -1 N LEU R 226 O LYS R 487 SHEET 4 AC1 5 VAL R 242 VAL R 245 -1 O VAL R 245 N ILE R 225 SHEET 5 AC1 5 ILE R 84 HIS R 85 -1 N ILE R 84 O THR R 244 SHEET 1 AC2 2 GLU R 91 ASN R 94 0 SHEET 2 AC2 2 THR R 236 CYS R 239 -1 O GLY R 237 N PHE R 93 SHEET 1 AC3 5 LYS R 169 PHE R 176 0 SHEET 2 AC3 5 LYS R 155 THR R 162 -1 N LYS R 155 O PHE R 176 SHEET 3 AC3 5 LEU R 129 ASN R 133 -1 N THR R 132 O GLN R 156 SHEET 4 AC3 5 LYS R 189 LEU R 193 -1 O TYR R 191 N LEU R 129 SHEET 5 AC3 5 VAL R 181 GLN R 183 -1 N VAL R 182 O ARG R 192 SHEET 1 AC4 2 ALA R 200 GLN R 203 0 SHEET 2 AC4 2 GLN R 432 TYR R 435 1 O TYR R 435 N THR R 202 SHEET 1 AC5 3 ILE R 271 ARG R 273 0 SHEET 2 AC5 3 ILE R 284 GLN R 287 -1 O LEU R 285 N ARG R 273 SHEET 3 AC5 3 ILE R 453 LEU R 454 -1 O LEU R 454 N ILE R 284 SHEET 1 AC6 6 HIS R 374 CYS R 378 0 SHEET 2 AC6 6 GLU R 381 CYS R 385 -1 O CYS R 385 N HIS R 374 SHEET 3 AC6 6 SER R 413 ILE R 420 -1 O ARG R 419 N TYR R 384 SHEET 4 AC6 6 HIS R 330 SER R 334 -1 N VAL R 333 O ILE R 414 SHEET 5 AC6 6 VAL R 292 ARG R 298 -1 N ASN R 295 O ASN R 332 SHEET 6 AC6 6 ILE R 443 ILE R 449 -1 O CYS R 445 N CYS R 296 SHEET 1 AC7 2 ASN R 302 ILE R 307 0 SHEET 2 AC7 2 PHE R 317 ILE R 322 -1 O GLY R 321 N THR R 303 SHEET 1 AC8 2 ARG R 360 PHE R 361 0 SHEET 2 AC8 2 THR R 467 PHE R 468 1 O PHE R 468 N ARG R 360 SHEET 1 AC9 4 GLN A 3 SER A 7 0 SHEET 2 AC9 4 THR A 21 SER A 25 -1 O SER A 23 N GLN A 5 SHEET 3 AC9 4 GLN A 77 LEU A 82 -1 O LEU A 78 N CYS A 22 SHEET 4 AC9 4 VAL A 67 ASP A 72 -1 N SER A 70 O SER A 79 SHEET 1 AD1 6 LEU A 11 VAL A 12 0 SHEET 2 AD1 6 THR A 126 VAL A 130 1 O THR A 129 N VAL A 12 SHEET 3 AD1 6 ALA A 88 ILE A 100A-1 N TYR A 90 O THR A 126 SHEET 4 AD1 6 TYR A 33 GLN A 39 -1 N TYR A 33 O ALA A 95 SHEET 5 AD1 6 LEU A 45 ILE A 51 -1 O GLU A 46 N ARG A 38 SHEET 6 AD1 6 THR A 58 TYR A 59 -1 O THR A 58 N TYR A 50 SHEET 1 AD2 4 LEU A 11 VAL A 12 0 SHEET 2 AD2 4 THR A 126 VAL A 130 1 O THR A 129 N VAL A 12 SHEET 3 AD2 4 ALA A 88 ILE A 100A-1 N TYR A 90 O THR A 126 SHEET 4 AD2 4 PHE A 100J SER A 100O-1 O SER A 100O N ARG A 96 SHEET 1 AD3 4 GLN F 3 SER F 7 0 SHEET 2 AD3 4 THR F 21 SER F 25 -1 O SER F 23 N GLN F 5 SHEET 3 AD3 4 GLN F 77 LEU F 82 -1 O LEU F 78 N CYS F 22 SHEET 4 AD3 4 VAL F 67 ASP F 72 -1 N SER F 70 O SER F 79 SHEET 1 AD4 6 LEU F 11 VAL F 12 0 SHEET 2 AD4 6 THR F 107 VAL F 111 1 O THR F 110 N VAL F 12 SHEET 3 AD4 6 ALA F 88 ILE F 100A-1 N TYR F 90 O THR F 107 SHEET 4 AD4 6 TYR F 33 GLN F 39 -1 N TYR F 33 O ALA F 95 SHEET 5 AD4 6 LEU F 45 ILE F 51 -1 O GLU F 46 N ARG F 38 SHEET 6 AD4 6 THR F 58 TYR F 59 -1 O THR F 58 N TYR F 50 SHEET 1 AD5 4 LEU F 11 VAL F 12 0 SHEET 2 AD5 4 THR F 107 VAL F 111 1 O THR F 110 N VAL F 12 SHEET 3 AD5 4 ALA F 88 ILE F 100A-1 N TYR F 90 O THR F 107 SHEET 4 AD5 4 PHE F 100J SER F 100O-1 O SER F 100O N ARG F 96 SHEET 1 AD6 4 GLN O 3 SER O 7 0 SHEET 2 AD6 4 THR O 21 SER O 25 -1 O SER O 23 N GLN O 5 SHEET 3 AD6 4 GLN O 77 LEU O 82 -1 O LEU O 78 N CYS O 22 SHEET 4 AD6 4 VAL O 67 ASP O 72 -1 N SER O 70 O SER O 79 SHEET 1 AD7 6 LEU O 11 VAL O 12 0 SHEET 2 AD7 6 THR O 107 VAL O 111 1 O THR O 110 N VAL O 12 SHEET 3 AD7 6 ALA O 88 ILE O 100A-1 N TYR O 90 O THR O 107 SHEET 4 AD7 6 TYR O 33 GLN O 39 -1 N TYR O 33 O ALA O 95 SHEET 5 AD7 6 LEU O 45 ILE O 51 -1 O GLU O 46 N ARG O 38 SHEET 6 AD7 6 THR O 58 TYR O 59 -1 O THR O 58 N TYR O 50 SHEET 1 AD8 4 LEU O 11 VAL O 12 0 SHEET 2 AD8 4 THR O 107 VAL O 111 1 O THR O 110 N VAL O 12 SHEET 3 AD8 4 ALA O 88 ILE O 100A-1 N TYR O 90 O THR O 107 SHEET 4 AD8 4 PHE O 100J SER O 100O-1 O SER O 100O N ARG O 96 SHEET 1 AD9 5 ARG B 9 LEU B 11 0 SHEET 2 AD9 5 THR B 102 LEU B 104 1 O ARG B 103 N ARG B 9 SHEET 3 AD9 5 ASP B 85 HIS B 89 -1 N TYR B 86 O THR B 102 SHEET 4 AD9 5 GLN B 34 HIS B 38 -1 N GLN B 34 O HIS B 89 SHEET 5 AD9 5 ILE B 45 TYR B 49 -1 O LEU B 47 N TRP B 35 SHEET 1 AE1 3 ALA B 19 SER B 22 0 SHEET 2 AE1 3 THR B 72 ILE B 75 -1 O LEU B 73 N ILE B 21 SHEET 3 AE1 3 PHE B 62 SER B 63 -1 N SER B 63 O THR B 74 SHEET 1 AE2 5 ARG I 9 LEU I 11 0 SHEET 2 AE2 5 THR I 102 LEU I 104 1 O ARG I 103 N ARG I 9 SHEET 3 AE2 5 ASP I 85 HIS I 89 -1 N TYR I 86 O THR I 102 SHEET 4 AE2 5 GLN I 34 HIS I 38 -1 N GLN I 34 O HIS I 89 SHEET 5 AE2 5 ILE I 45 TYR I 49 -1 O LEU I 47 N TRP I 35 SHEET 1 AE3 3 ALA I 19 SER I 22 0 SHEET 2 AE3 3 THR I 72 ILE I 75 -1 O LEU I 73 N ILE I 21 SHEET 3 AE3 3 PHE I 62 SER I 63 -1 N SER I 63 O THR I 74 SHEET 1 AE4 5 ARG P 9 LEU P 11 0 SHEET 2 AE4 5 THR P 102 LEU P 104 1 O ARG P 103 N ARG P 9 SHEET 3 AE4 5 ASP P 85 HIS P 89 -1 N TYR P 86 O THR P 102 SHEET 4 AE4 5 GLN P 34 HIS P 38 -1 N GLN P 34 O HIS P 89 SHEET 5 AE4 5 ILE P 45 TYR P 49 -1 O LEU P 47 N TRP P 35 SHEET 1 AE5 3 ALA P 19 SER P 22 0 SHEET 2 AE5 3 THR P 72 ILE P 75 -1 O LEU P 73 N ILE P 21 SHEET 3 AE5 3 PHE P 62 SER P 63 -1 N SER P 63 O THR P 74 SSBOND 1 CYS C 598 CYS C 604 1555 1555 2.03 SSBOND 2 CYS C 605 CYS G 501 1555 1555 2.03 SSBOND 3 CYS G 54 CYS G 74 1555 1555 2.03 SSBOND 4 CYS G 119 CYS G 205 1555 1555 2.03 SSBOND 5 CYS G 126 CYS G 196 1555 1555 2.03 SSBOND 6 CYS G 131 CYS G 157 1555 1555 2.03 SSBOND 7 CYS G 218 CYS G 247 1555 1555 2.05 SSBOND 8 CYS G 228 CYS G 239 1555 1555 2.03 SSBOND 9 CYS G 296 CYS G 331 1555 1555 2.03 SSBOND 10 CYS G 378 CYS G 445 1555 1555 2.02 SSBOND 11 CYS G 385 CYS G 418 1555 1555 2.03 SSBOND 12 CYS J 598 CYS J 604 1555 1555 2.03 SSBOND 13 CYS J 605 CYS K 501 1555 1555 2.03 SSBOND 14 CYS K 54 CYS K 74 1555 1555 2.03 SSBOND 15 CYS K 119 CYS K 205 1555 1555 2.03 SSBOND 16 CYS K 126 CYS K 196 1555 1555 2.03 SSBOND 17 CYS K 131 CYS K 157 1555 1555 2.03 SSBOND 18 CYS K 218 CYS K 247 1555 1555 2.06 SSBOND 19 CYS K 228 CYS K 239 1555 1555 2.03 SSBOND 20 CYS K 296 CYS K 331 1555 1555 2.03 SSBOND 21 CYS K 378 CYS K 445 1555 1555 2.02 SSBOND 22 CYS K 385 CYS K 418 1555 1555 2.03 SSBOND 23 CYS Q 598 CYS Q 604 1555 1555 2.03 SSBOND 24 CYS Q 605 CYS R 501 1555 1555 2.03 SSBOND 25 CYS R 54 CYS R 74 1555 1555 2.03 SSBOND 26 CYS R 119 CYS R 205 1555 1555 2.03 SSBOND 27 CYS R 126 CYS R 196 1555 1555 2.03 SSBOND 28 CYS R 131 CYS R 157 1555 1555 2.03 SSBOND 29 CYS R 218 CYS R 247 1555 1555 2.06 SSBOND 30 CYS R 228 CYS R 239 1555 1555 2.03 SSBOND 31 CYS R 296 CYS R 331 1555 1555 2.03 SSBOND 32 CYS R 378 CYS R 445 1555 1555 2.03 SSBOND 33 CYS R 385 CYS R 418 1555 1555 2.03 SSBOND 34 CYS A 22 CYS A 92 1555 1555 2.03 SSBOND 35 CYS F 22 CYS F 92 1555 1555 2.03 SSBOND 36 CYS O 22 CYS O 92 1555 1555 2.03 SSBOND 37 CYS B 23 CYS B 88 1555 1555 2.03 SSBOND 38 CYS I 23 CYS I 88 1555 1555 2.03 SSBOND 39 CYS P 23 CYS P 88 1555 1555 2.03 LINK ND2 ASN C 611 C1 NAG C 703 1555 1555 1.43 LINK ND2 ASN C 618 C1 NAG C 702 1555 1555 1.40 LINK ND2 ASN C 637 C1 NAG C 701 1555 1555 1.45 LINK ND2 ASN G 88 C1 NAG G 601 1555 1555 1.44 LINK ND2 ASN G 160 C1 NAG G 602 1555 1555 1.44 LINK ND2 ASN G 197 C1 NAG G 603 1555 1555 1.45 LINK ND2 ASN G 234 C1 NAG G 604 1555 1555 1.44 LINK ND2 ASN G 262 C1 NAG G 605 1555 1555 1.46 LINK ND2 ASN G 276 C1 NAG G 611 1555 1555 1.44 LINK ND2 ASN G 295 C1 NAG G 614 1555 1555 1.44 LINK ND2 ASN G 301 C1 NAG G 615 1555 1555 1.44 LINK ND2 ASN G 332 C1 NAG G 616 1555 1555 1.43 LINK ND2 ASN G 339 C1 NAG G 623 1555 1555 1.43 LINK ND2 ASN G 355 C1 NAG G 624 1555 1555 1.44 LINK ND2 ASN G 386 C1 NAG G 625 1555 1555 1.44 LINK ND2 ASN G 392 C1 NAG G 628 1555 1555 1.44 LINK ND2 ASN G 448 C1 NAG G 629 1555 1555 1.43 LINK ND2 ASN J 611 C1 NAG J 701 1555 1555 1.44 LINK ND2 ASN J 618 C1 NAG J 702 1555 1555 1.46 LINK ND2 ASN J 637 C1 NAG J 703 1555 1555 1.45 LINK ND2 ASN K 88 C1 NAG K 602 1555 1555 1.44 LINK ND2 ASN K 160 C1 NAG K 604 1555 1555 1.43 LINK ND2 ASN K 197 C1 NAG K 606 1555 1555 1.44 LINK ND2 ASN K 234 C1 NAG K 608 1555 1555 1.44 LINK ND2 ASN K 262 C1 NAG K 609 1555 1555 1.45 LINK ND2 ASN K 276 C1 NAG K 616 1555 1555 1.44 LINK ND2 ASN K 295 C1 NAG K 619 1555 1555 1.44 LINK ND2 ASN K 301 C1 NAG K 620 1555 1555 1.43 LINK ND2 ASN K 332 C1 NAG K 621 1555 1555 1.43 LINK ND2 ASN K 339 C1 NAG K 627 1555 1555 1.43 LINK ND2 ASN K 355 C1 NAG K 628 1555 1555 1.45 LINK ND2 ASN K 386 C1 NAG K 629 1555 1555 1.45 LINK ND2 ASN K 392 C1 NAG K 631 1555 1555 1.44 LINK ND2 ASN K 448 C1 NAG K 601 1555 1555 1.44 LINK ND2 ASN Q 611 C1 NAG Q 701 1555 1555 1.44 LINK ND2 ASN Q 618 C1 NAG Q 702 1555 1555 1.46 LINK ND2 ASN Q 637 C1 NAG Q 703 1555 1555 1.45 LINK ND2 ASN R 88 C1 NAG R 601 1555 1555 1.44 LINK ND2 ASN R 160 C1 NAG R 603 1555 1555 1.43 LINK ND2 ASN R 197 C1 NAG R 605 1555 1555 1.44 LINK ND2 ASN R 234 C1 NAG R 607 1555 1555 1.43 LINK ND2 ASN R 262 C1 NAG R 608 1555 1555 1.44 LINK ND2 ASN R 276 C1 NAG R 614 1555 1555 1.45 LINK ND2 ASN R 295 C1 NAG R 616 1555 1555 1.45 LINK ND2 ASN R 301 C1 NAG R 617 1555 1555 1.44 LINK ND2 ASN R 332 C1 NAG R 619 1555 1555 1.43 LINK ND2 ASN R 339 C1 NAG R 625 1555 1555 1.43 LINK ND2 ASN R 355 C1 NAG R 626 1555 1555 1.45 LINK ND2 ASN R 386 C1 NAG R 627 1555 1555 1.45 LINK ND2 ASN R 392 C1 NAG R 629 1555 1555 1.43 LINK ND2 ASN R 448 C1 NAG R 630 1555 1555 1.42 LINK O4 NAG G 605 C1 NAG G 606 1555 1555 1.45 LINK O4 NAG G 606 C1 BMA G 607 1555 1555 1.44 LINK O3 BMA G 607 C1 MAN G 609 1555 1555 1.44 LINK O6 BMA G 607 C1 MAN G 608 1555 1555 1.44 LINK O2 MAN G 609 C1 MAN G 610 1555 1555 1.43 LINK O4 NAG G 611 C1 NAG G 612 1555 1555 1.45 LINK O4 NAG G 612 C1 BMA G 613 1555 1555 1.45 LINK O4 NAG G 616 C1 NAG G 617 1555 1555 1.44 LINK O4 NAG G 617 C1 BMA G 618 1555 1555 1.43 LINK O3 BMA G 618 C1 MAN G 621 1555 1555 1.44 LINK O6 BMA G 618 C1 MAN G 619 1555 1555 1.45 LINK O3 MAN G 619 C1 MAN G 620 1555 1555 1.44 LINK O2 MAN G 621 C1 MAN G 622 1555 1555 1.45 LINK O4 NAG G 625 C1 NAG G 626 1555 1555 1.43 LINK O4 NAG G 626 C1 BMA G 627 1555 1555 1.45 LINK O4 NAG G 629 C1 NAG G 630 1555 1555 1.43 LINK O4 NAG K 602 C1 NAG K 603 1555 1555 1.45 LINK O4 NAG K 604 C1 NAG K 605 1555 1555 1.43 LINK O4 NAG K 606 C1 NAG K 607 1555 1555 1.45 LINK O4 NAG K 609 C1 NAG K 610 1555 1555 1.44 LINK O4 NAG K 610 C1 BMA K 611 1555 1555 1.44 LINK O3 BMA K 611 C1 MAN K 614 1555 1555 1.44 LINK O6 BMA K 611 C1 MAN K 612 1555 1555 1.44 LINK O3 MAN K 612 C1 MAN K 613 1555 1555 1.44 LINK O2 MAN K 614 C1 MAN K 615 1555 1555 1.44 LINK O4 NAG K 616 C1 NAG K 617 1555 1555 1.44 LINK O4 NAG K 617 C1 BMA K 618 1555 1555 1.44 LINK O4 NAG K 621 C1 NAG K 622 1555 1555 1.44 LINK O4 NAG K 622 C1 BMA K 623 1555 1555 1.44 LINK O3 BMA K 623 C1 MAN K 624 1555 1555 1.44 LINK O6 BMA K 623 C1 MAN K 626 1555 1555 1.46 LINK O2 MAN K 624 C1 MAN K 625 1555 1555 1.45 LINK O4 NAG K 629 C1 NAG K 630 1555 1555 1.44 LINK O4 NAG R 601 C1 NAG R 602 1555 1555 1.45 LINK O4 NAG R 603 C1 NAG R 604 1555 1555 1.46 LINK O4 NAG R 605 C1 NAG R 606 1555 1555 1.45 LINK O4 NAG R 608 C1 NAG R 609 1555 1555 1.45 LINK O4 NAG R 609 C1 BMA R 610 1555 1555 1.44 LINK O3 BMA R 610 C1 MAN R 612 1555 1555 1.44 LINK O6 BMA R 610 C1 MAN R 611 1555 1555 1.44 LINK O2 MAN R 612 C1 MAN R 613 1555 1555 1.45 LINK O4 NAG R 614 C1 NAG R 615 1555 1555 1.45 LINK O4 NAG R 617 C1 NAG R 618 1555 1555 1.46 LINK O4 NAG R 619 C1 NAG R 620 1555 1555 1.44 LINK O4 NAG R 620 C1 BMA R 621 1555 1555 1.46 LINK O3 BMA R 621 C1 MAN R 622 1555 1555 1.46 LINK O6 BMA R 621 C1 MAN R 623 1555 1555 1.43 LINK O6 MAN R 623 C1 MAN R 624 1555 1555 1.44 LINK O4 NAG R 627 C1 NAG R 628 1555 1555 1.44 LINK O4 NAG R 630 C1 NAG R 631 1555 1555 1.44 SITE 1 AC1 2 ASN C 611 SER C 613 SITE 1 AC2 1 ASN C 618 SITE 1 AC3 1 ASN C 637 SITE 1 AC4 3 SER C 528 GLU G 87 ASN G 88 SITE 1 AC5 2 THR G 128 ASN G 160 SITE 1 AC6 2 ARG G 192 ASN G 197 SITE 1 AC7 2 ASN G 234 THR G 236 SITE 1 AC8 5 GLU G 211 LEU G 261 ASN G 262 SER G 447 SITE 2 AC8 5 NAG G 629 SITE 1 AC9 2 ASN G 276 THR G 278 SITE 1 AD1 2 ASN G 295 SER G 334 SITE 1 AD2 1 ASN G 301 SITE 1 AD3 13 ARG A 100 ILE A 100A TYR A 100B GLY A 100C SITE 2 AD3 13 VAL A 100D VAL A 100E SER B 30 ASN B 50 SITE 3 AD3 13 GLN B 52 ASP B 66A ILE B 66B HIS G 330 SITE 4 AD3 13 ASN G 332 SITE 1 AD4 1 ASN G 339 SITE 1 AD5 1 ASN G 355 SITE 1 AD6 1 ASN G 386 SITE 1 AD7 2 SER G 388 ASN G 392 SITE 1 AD8 3 PRO G 291 ASN G 448 NAG G 605 SITE 1 AD9 2 ASN J 611 SER J 613 SITE 1 AE1 1 ASN J 618 SITE 1 AE2 1 ASN J 637 SITE 1 AE3 2 GLU K 87 ASN K 88 SITE 1 AE4 4 GLN K 130 SER K 158 PHE K 159 ASN K 160 SITE 1 AE5 2 ARG K 192 ASN K 197 SITE 1 AE6 2 ASN K 234 GLU K 275 SITE 1 AE7 3 ASN K 262 VAL K 446 NAG K 601 SITE 1 AE8 1 ASN K 276 SITE 1 AE9 1 ASN K 295 SITE 1 AF1 1 ASN K 301 SITE 1 AF2 13 ARG F 100 ILE F 100A TYR F 100B GLY F 100C SITE 2 AF2 13 VAL F 100D VAL F 100E SER I 30 ASN I 50 SITE 3 AF2 13 GLN I 52 ASP I 66A ILE I 66B HIS K 330 SITE 4 AF2 13 ASN K 332 SITE 1 AF3 1 ASN K 339 SITE 1 AF4 1 ASN K 355 SITE 1 AF5 2 ASN K 386 SER K 388 SITE 1 AF6 2 SER K 388 ASN K 392 SITE 1 AF7 2 ASN K 448 NAG K 609 SITE 1 AF8 2 ASN Q 611 SER Q 613 SITE 1 AF9 1 ASN Q 618 SITE 1 AG1 1 ASN Q 637 SITE 1 AG2 2 GLU R 87 ASN R 88 SITE 1 AG3 3 SER R 158 PHE R 159 ASN R 160 SITE 1 AG4 3 VAL R 182 ARG R 192 ASN R 197 SITE 1 AG5 3 ASN R 234 SER R 274 GLU R 275 SITE 1 AG6 5 ASN R 262 ASN R 377 VAL R 446 SER R 447 SITE 2 AG6 5 NAG R 630 SITE 1 AG7 3 ASN R 276 THR R 278 ASN R 279 SITE 1 AG8 3 GLN R 293 ILE R 294 ASN R 295 SITE 1 AG9 1 ASN R 301 SITE 1 AH1 11 ARG O 100 ILE O 100A GLY O 100C VAL O 100D SITE 2 AH1 11 VAL O 100E SER P 30 ASN P 50 GLN P 52 SITE 3 AH1 11 ASP P 66A HIS R 330 ASN R 332 SITE 1 AH2 1 ASN R 339 SITE 1 AH3 1 ASN R 355 SITE 1 AH4 2 ASN R 386 SER R 388 SITE 1 AH5 2 SER R 388 ASN R 392 SITE 1 AH6 3 PRO R 291 ASN R 448 NAG R 608 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 0.003348 0.000000 0.000000 0.00000 SCALE2 0.000000 0.003348 0.000000 0.00000 SCALE3 0.000000 0.000000 0.003348 0.00000