HEADER VIRAL PROTEIN/IMMUNE SYSTEM 27-JUN-24 9CF5 TITLE STRUCTURE OF CD4 MIMETIC CJF-III-288 IN COMPLEX WITH BG505 SOSIP.664 TITLE 2 HIV-1ENV TRIMER AND 17B FAB COMPND MOL_ID: 1; COMPND 2 MOLECULE: ENVELOPE GLYCOPROTEIN GP120; COMPND 3 CHAIN: A, C, E; COMPND 4 ENGINEERED: YES; COMPND 5 MUTATION: YES; COMPND 6 OTHER_DETAILS: BG505 SOSIP.664 CONSTRUCT; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: ENVELOPE GLYCOPROTEIN GP41; COMPND 9 CHAIN: B, D, F; COMPND 10 FRAGMENT: RESIDUES 512-664 (509-661 UNIPROT NUMBERING); COMPND 11 ENGINEERED: YES; COMPND 12 MUTATION: YES; COMPND 13 OTHER_DETAILS: BG505 SOSIP.664 CONSTRUCT; COMPND 14 MOL_ID: 3; COMPND 15 MOLECULE: 17B FAB LIGHT CHAIN; COMPND 16 CHAIN: K, I, G; COMPND 17 ENGINEERED: YES; COMPND 18 MOL_ID: 4; COMPND 19 MOLECULE: 17B FAB HEAVY CHAIN; COMPND 20 CHAIN: L, J, H; COMPND 21 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_LINE: HEK 293 GNT1-; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 11 ORGANISM_TAXID: 11676; SOURCE 12 GENE: ENV; SOURCE 13 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 15 EXPRESSION_SYSTEM_CELL_LINE: HEK 293 GNT1-; SOURCE 16 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 17 MOL_ID: 3; SOURCE 18 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 19 ORGANISM_TAXID: 9606; SOURCE 20 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 21 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 22 EXPRESSION_SYSTEM_CELL_LINE: HEK293; SOURCE 23 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 24 MOL_ID: 4; SOURCE 25 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 26 ORGANISM_TAXID: 9606; SOURCE 27 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 28 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 29 EXPRESSION_SYSTEM_CELL_LINE: HEK293; SOURCE 30 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID KEYWDS HIV-1, FUSION, ENTRY, MEMBRANE, VIRAL PROTEIN, VIRAL PROTEIN-IMMUNE KEYWDS 2 SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR L.NIU,W.D.TOLBERT,M.PAZGIER REVDAT 1 19-NOV-25 9CF5 0 JRNL AUTH J.RICHARD,M.W.GRUNST,L.NIU,M.A.DIAZ-SALINAS,L.ZHU, JRNL AUTH 2 W.D.TOLBERT,L.MARCHITTO,F.ZHOU,C.BOURASSA,H.KIM, JRNL AUTH 3 S.L.T.BOODAPATI,D.YANG,T.J.CHIU,H.-C.CHEN,M.BENLARBI, JRNL AUTH 4 G.BEAUDOIN-BUSSIERES,S.GOTTUMUKKALA,W.LI,K.DIONNE, JRNL AUTH 5 E.BELANGER,D.CHATTERJEE,H.MEDJAHED,W.A.HENDRICKSON, JRNL AUTH 6 J.SODROSKI,Z.C.LANG,A.J.MORTON,R.K.HUANG,D.MATTHIES, JRNL AUTH 7 A.B.SMITH 3RD,P.KUMAR,W.MOTHES,J.B.MUNRO,M.PAZGIER,A.FINZI JRNL TITL THE ASYMMETRIC OPENING OF HIV-1 ENV BY A POTENT CD4 MIMETIC JRNL TITL 2 ENABLES ANTI-CORECEPTOR BINDING SITE ANTIBODIES TO MEDIATE JRNL TITL 3 ADCC JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.50 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : CRYOSPARC, SERIALEM, CRYOSPARC, UCSF REMARK 3 CHIMERAX, CRYOSPARC, PHENIX REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : 7LOK REMARK 3 REFINEMENT SPACE : NULL REMARK 3 REFINEMENT PROTOCOL : NULL REMARK 3 REFINEMENT TARGET : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL REMARK 3 REMARK 3 FITTING PROCEDURE : NULL REMARK 3 REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 3.500 REMARK 3 NUMBER OF PARTICLES : 108769 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 9CF5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-JUL-24. REMARK 100 THE DEPOSITION ID IS D_1000285380. 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 BG505 SOSIP.664 ENV REMARK 245 TRIMER WITH CJF-III-288 AND REMARK 245 THREE BOUND 17B FABS.; BG505 REMARK 245 SOSIP.664 ENV TRIMER; 17B FAB REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 1.50 REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.20 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : 9431 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) : 500.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2700.00 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) : 5420.00 REMARK 245 ILLUMINATION MODE : SPOT SCAN REMARK 245 NOMINAL MAGNIFICATION : NULL REMARK 245 CALIBRATED MAGNIFICATION : NULL REMARK 245 SOURCE : FIELD EMISSION GUN REMARK 245 ACCELERATION VOLTAGE (KV) : 300 REMARK 245 IMAGING DETAILS : NULL REMARK 247 REMARK 247 ELECTRON MICROSCOPY REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION REMARK 247 OF THE STRUCTURE FACTORS. REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DODECAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, K, L, C, D, I, J, E, F, REMARK 350 AND CHAINS: G, H, M, N, W, X, O, P, Q, REMARK 350 AND CHAINS: R, S, T, U, V 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 VAL A 127 REMARK 465 THR A 128 REMARK 465 LEU A 129 REMARK 465 GLN A 130 REMARK 465 CYS A 131 REMARK 465 THR A 132 REMARK 465 ASN A 133 REMARK 465 VAL A 134 REMARK 465 THR A 135 REMARK 465 ASN A 136 REMARK 465 ASN A 137 REMARK 465 ILE A 138 REMARK 465 THR A 139 REMARK 465 ASP A 140 REMARK 465 ASP A 141 REMARK 465 MET A 142 REMARK 465 ARG A 143 REMARK 465 GLY A 144 REMARK 465 GLU A 145 REMARK 465 LEU A 146 REMARK 465 LYS A 147 REMARK 465 ASN A 148 REMARK 465 CYS A 149 REMARK 465 SER A 150 REMARK 465 PHE A 151 REMARK 465 ASN A 152 REMARK 465 MET A 153 REMARK 465 THR A 154 REMARK 465 THR A 155 REMARK 465 GLU A 156 REMARK 465 LEU A 157 REMARK 465 ARG A 158 REMARK 465 ASP A 159 REMARK 465 LYS A 160 REMARK 465 LYS A 161 REMARK 465 GLN A 162 REMARK 465 LYS A 163 REMARK 465 VAL A 164 REMARK 465 TYR A 165 REMARK 465 SER A 166 REMARK 465 LEU A 167 REMARK 465 PHE A 168 REMARK 465 TYR A 169 REMARK 465 ARG A 170 REMARK 465 LEU A 171 REMARK 465 ASP A 172 REMARK 465 VAL A 173 REMARK 465 VAL A 174 REMARK 465 GLN A 175 REMARK 465 ILE A 176 REMARK 465 ASN A 177 REMARK 465 GLU A 178 REMARK 465 ASN A 179 REMARK 465 GLN A 180 REMARK 465 GLY A 181 REMARK 465 ASN A 182 REMARK 465 ARG A 183 REMARK 465 SER A 184 REMARK 465 ASN A 185 REMARK 465 ASN A 186 REMARK 465 SER A 187 REMARK 465 ASN A 188 REMARK 465 LYS A 189 REMARK 465 GLU A 190 REMARK 465 TYR A 191 REMARK 465 ARG A 192 REMARK 465 LEU A 193 REMARK 465 ILE A 194 REMARK 465 ASN A 303 REMARK 465 THR A 304 REMARK 465 ARG A 305 REMARK 465 LYS A 306 REMARK 465 SER A 307 REMARK 465 ILE A 308 REMARK 465 ARG A 309 REMARK 465 ILE A 310 REMARK 465 GLY A 311 REMARK 465 PRO A 312 REMARK 465 GLY A 313 REMARK 465 GLN A 314 REMARK 465 ALA A 315 REMARK 465 PHE A 316 REMARK 465 TYR A 317 REMARK 465 ALA A 318 REMARK 465 THR A 319 REMARK 465 GLY A 320 REMARK 465 ASP A 321 REMARK 465 ILE A 322 REMARK 465 ILE A 323 REMARK 465 GLY A 324 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 THR A 461 REMARK 465 ASN A 462 REMARK 465 SER A 463 REMARK 465 ARG A 504 REMARK 465 VAL A 505 REMARK 465 VAL A 506 REMARK 465 GLY A 507 REMARK 465 ARG A 508 REMARK 465 ARG A 509 REMARK 465 ARG A 510 REMARK 465 ARG A 511 REMARK 465 ARG A 512 REMARK 465 ARG A 513 REMARK 465 ALA B 512 REMARK 465 VAL B 513 REMARK 465 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 ASN B 656 REMARK 465 GLU B 657 REMARK 465 GLN B 658 REMARK 465 ASP B 659 REMARK 465 LEU B 660 REMARK 465 LEU B 661 REMARK 465 ALA B 662 REMARK 465 LEU B 663 REMARK 465 ASP B 664 REMARK 465 VAL K 110 REMARK 465 ALA K 111 REMARK 465 ALA K 112 REMARK 465 PRO K 113 REMARK 465 SER K 114 REMARK 465 VAL K 115 REMARK 465 PHE K 116 REMARK 465 ILE K 117 REMARK 465 PHE K 118 REMARK 465 PRO K 119 REMARK 465 PRO K 120 REMARK 465 SER K 121 REMARK 465 ASP K 122 REMARK 465 GLU K 123 REMARK 465 GLN K 124 REMARK 465 LEU K 125 REMARK 465 LYS K 126 REMARK 465 SER K 127 REMARK 465 GLY K 128 REMARK 465 THR K 129 REMARK 465 ALA K 130 REMARK 465 SER K 131 REMARK 465 VAL K 132 REMARK 465 VAL K 133 REMARK 465 CYS K 134 REMARK 465 LEU K 135 REMARK 465 LEU K 136 REMARK 465 ASN K 137 REMARK 465 ASN K 138 REMARK 465 PHE K 139 REMARK 465 TYR K 140 REMARK 465 PRO K 141 REMARK 465 ARG K 142 REMARK 465 GLU K 143 REMARK 465 ALA K 144 REMARK 465 LYS K 145 REMARK 465 VAL K 146 REMARK 465 GLN K 147 REMARK 465 TRP K 148 REMARK 465 LYS K 149 REMARK 465 VAL K 150 REMARK 465 ASP K 151 REMARK 465 ASN K 152 REMARK 465 ALA K 153 REMARK 465 LEU K 154 REMARK 465 GLN K 155 REMARK 465 SER K 156 REMARK 465 GLY K 157 REMARK 465 ASN K 158 REMARK 465 SER K 159 REMARK 465 GLN K 160 REMARK 465 GLU K 161 REMARK 465 SER K 162 REMARK 465 VAL K 163 REMARK 465 THR K 164 REMARK 465 GLU K 165 REMARK 465 GLN K 166 REMARK 465 ASP K 167 REMARK 465 SER K 168 REMARK 465 LYS K 169 REMARK 465 ASP K 170 REMARK 465 SER K 171 REMARK 465 THR K 172 REMARK 465 TYR K 173 REMARK 465 SER K 174 REMARK 465 LEU K 175 REMARK 465 SER K 176 REMARK 465 SER K 177 REMARK 465 THR K 178 REMARK 465 LEU K 179 REMARK 465 THR K 180 REMARK 465 LEU K 181 REMARK 465 SER K 182 REMARK 465 LYS K 183 REMARK 465 ALA K 184 REMARK 465 ASP K 185 REMARK 465 TYR K 186 REMARK 465 GLU K 187 REMARK 465 LYS K 188 REMARK 465 HIS K 189 REMARK 465 LYS K 190 REMARK 465 VAL K 191 REMARK 465 TYR K 192 REMARK 465 ALA K 193 REMARK 465 CYS K 194 REMARK 465 GLU K 195 REMARK 465 VAL K 196 REMARK 465 THR K 197 REMARK 465 HIS K 198 REMARK 465 GLN K 199 REMARK 465 GLY K 200 REMARK 465 LEU K 201 REMARK 465 SER K 202 REMARK 465 SER K 203 REMARK 465 PRO K 204 REMARK 465 VAL K 205 REMARK 465 THR K 206 REMARK 465 LYS K 207 REMARK 465 SER K 208 REMARK 465 PHE K 209 REMARK 465 ASN K 210 REMARK 465 ARG K 211 REMARK 465 GLY K 212 REMARK 465 ALA L 114 REMARK 465 SER L 115 REMARK 465 THR L 116 REMARK 465 LYS L 117 REMARK 465 GLY L 118 REMARK 465 PRO L 119 REMARK 465 SER L 120 REMARK 465 VAL L 121 REMARK 465 PHE L 122 REMARK 465 PRO L 123 REMARK 465 LEU L 124 REMARK 465 ALA L 125 REMARK 465 PRO L 126 REMARK 465 SER L 127 REMARK 465 SER L 128 REMARK 465 LYS L 129 REMARK 465 SER L 130 REMARK 465 THR L 131 REMARK 465 SER L 132 REMARK 465 GLY L 133 REMARK 465 GLY L 134 REMARK 465 THR L 135 REMARK 465 ALA L 136 REMARK 465 ALA L 137 REMARK 465 LEU L 138 REMARK 465 GLY L 139 REMARK 465 CYS L 140 REMARK 465 LEU L 141 REMARK 465 VAL L 142 REMARK 465 LYS L 143 REMARK 465 ASP L 144 REMARK 465 TYR L 145 REMARK 465 PHE L 146 REMARK 465 PRO L 147 REMARK 465 GLU L 148 REMARK 465 PRO L 149 REMARK 465 VAL L 150 REMARK 465 THR L 151 REMARK 465 VAL L 152 REMARK 465 SER L 153 REMARK 465 TRP L 154 REMARK 465 ASN L 155 REMARK 465 SER L 156 REMARK 465 GLY L 157 REMARK 465 ALA L 158 REMARK 465 LEU L 159 REMARK 465 THR L 160 REMARK 465 SER L 161 REMARK 465 GLY L 162 REMARK 465 VAL L 163 REMARK 465 HIS L 164 REMARK 465 THR L 165 REMARK 465 PHE L 166 REMARK 465 PRO L 167 REMARK 465 ALA L 168 REMARK 465 VAL L 169 REMARK 465 LEU L 170 REMARK 465 GLN L 171 REMARK 465 SER L 172 REMARK 465 SER L 173 REMARK 465 GLY L 174 REMARK 465 LEU L 175 REMARK 465 TYR L 176 REMARK 465 SER L 177 REMARK 465 LEU L 178 REMARK 465 SER L 179 REMARK 465 SER L 180 REMARK 465 VAL L 181 REMARK 465 VAL L 182 REMARK 465 THR L 183 REMARK 465 VAL L 184 REMARK 465 PRO L 185 REMARK 465 SER L 186 REMARK 465 SER L 187 REMARK 465 SER L 188 REMARK 465 LEU L 189 REMARK 465 GLY L 190 REMARK 465 THR L 191 REMARK 465 GLN L 192 REMARK 465 THR L 193 REMARK 465 TYR L 194 REMARK 465 ILE L 195 REMARK 465 CYS L 196 REMARK 465 ASN L 197 REMARK 465 VAL L 198 REMARK 465 ASN L 199 REMARK 465 HIS L 200 REMARK 465 LYS L 201 REMARK 465 PRO L 202 REMARK 465 SER L 203 REMARK 465 ASN L 204 REMARK 465 THR L 205 REMARK 465 LYS L 206 REMARK 465 VAL L 207 REMARK 465 ASP L 208 REMARK 465 LYS L 209 REMARK 465 ARG L 210 REMARK 465 VAL L 211 REMARK 465 GLU L 212 REMARK 465 PRO L 213 REMARK 465 LYS L 214 REMARK 465 SER L 215 REMARK 465 THR C 128 REMARK 465 LEU C 129 REMARK 465 GLN C 130 REMARK 465 CYS C 131 REMARK 465 THR C 132 REMARK 465 ASN C 133 REMARK 465 VAL C 134 REMARK 465 THR C 135 REMARK 465 ASN C 136 REMARK 465 ASN C 137 REMARK 465 ILE C 138 REMARK 465 THR C 139 REMARK 465 ASP C 140 REMARK 465 ASP C 141 REMARK 465 MET C 142 REMARK 465 ARG C 143 REMARK 465 GLY C 144 REMARK 465 GLU C 145 REMARK 465 LEU C 146 REMARK 465 LYS C 147 REMARK 465 ASN C 148 REMARK 465 CYS C 149 REMARK 465 SER C 150 REMARK 465 PHE C 151 REMARK 465 ASN C 152 REMARK 465 MET C 153 REMARK 465 THR C 154 REMARK 465 THR C 155 REMARK 465 GLU C 156 REMARK 465 LEU C 157 REMARK 465 ARG C 158 REMARK 465 ASP C 159 REMARK 465 LYS C 160 REMARK 465 LYS C 161 REMARK 465 GLN C 162 REMARK 465 LYS C 163 REMARK 465 VAL C 164 REMARK 465 TYR C 165 REMARK 465 SER C 166 REMARK 465 LEU C 167 REMARK 465 PHE C 168 REMARK 465 TYR C 169 REMARK 465 ARG C 170 REMARK 465 LEU C 171 REMARK 465 ASP C 172 REMARK 465 VAL C 173 REMARK 465 VAL C 174 REMARK 465 GLN C 175 REMARK 465 ILE C 176 REMARK 465 ASN C 177 REMARK 465 GLU C 178 REMARK 465 ASN C 179 REMARK 465 GLN C 180 REMARK 465 GLY C 181 REMARK 465 ASN C 182 REMARK 465 ARG C 183 REMARK 465 SER C 184 REMARK 465 ASN C 185 REMARK 465 ASN C 186 REMARK 465 SER C 187 REMARK 465 ASN C 188 REMARK 465 LYS C 189 REMARK 465 GLU C 190 REMARK 465 TYR C 191 REMARK 465 ARG C 192 REMARK 465 LEU C 193 REMARK 465 ILE C 194 REMARK 465 ASN C 303 REMARK 465 THR C 304 REMARK 465 ARG C 305 REMARK 465 LYS C 306 REMARK 465 SER C 307 REMARK 465 ILE C 308 REMARK 465 ARG C 309 REMARK 465 ILE C 310 REMARK 465 GLY C 311 REMARK 465 PRO C 312 REMARK 465 GLY C 313 REMARK 465 GLN C 314 REMARK 465 ALA C 315 REMARK 465 PHE C 316 REMARK 465 TYR C 317 REMARK 465 ALA C 318 REMARK 465 THR C 319 REMARK 465 GLY C 320 REMARK 465 ASP C 321 REMARK 465 ILE C 322 REMARK 465 ILE C 323 REMARK 465 GLY C 324 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 ASN C 411 REMARK 465 SER C 460 REMARK 465 THR C 461 REMARK 465 ASN C 462 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 ARG D 542 REMARK 465 ASN D 543 REMARK 465 LEU D 544 REMARK 465 LEU D 545 REMARK 465 SER D 546 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 LEU D 660 REMARK 465 LEU D 661 REMARK 465 ALA D 662 REMARK 465 LEU D 663 REMARK 465 ASP D 664 REMARK 465 VAL I 110 REMARK 465 ALA I 111 REMARK 465 ALA I 112 REMARK 465 PRO I 113 REMARK 465 SER I 114 REMARK 465 VAL I 115 REMARK 465 PHE I 116 REMARK 465 ILE I 117 REMARK 465 PHE I 118 REMARK 465 PRO I 119 REMARK 465 PRO I 120 REMARK 465 SER I 121 REMARK 465 ASP I 122 REMARK 465 GLU I 123 REMARK 465 GLN I 124 REMARK 465 LEU I 125 REMARK 465 LYS I 126 REMARK 465 SER I 127 REMARK 465 GLY I 128 REMARK 465 THR I 129 REMARK 465 ALA I 130 REMARK 465 SER I 131 REMARK 465 VAL I 132 REMARK 465 VAL I 133 REMARK 465 CYS I 134 REMARK 465 LEU I 135 REMARK 465 LEU I 136 REMARK 465 ASN I 137 REMARK 465 ASN I 138 REMARK 465 PHE I 139 REMARK 465 TYR I 140 REMARK 465 PRO I 141 REMARK 465 ARG I 142 REMARK 465 GLU I 143 REMARK 465 ALA I 144 REMARK 465 LYS I 145 REMARK 465 VAL I 146 REMARK 465 GLN I 147 REMARK 465 TRP I 148 REMARK 465 LYS I 149 REMARK 465 VAL I 150 REMARK 465 ASP I 151 REMARK 465 ASN I 152 REMARK 465 ALA I 153 REMARK 465 LEU I 154 REMARK 465 GLN I 155 REMARK 465 SER I 156 REMARK 465 GLY I 157 REMARK 465 ASN I 158 REMARK 465 SER I 159 REMARK 465 GLN I 160 REMARK 465 GLU I 161 REMARK 465 SER I 162 REMARK 465 VAL I 163 REMARK 465 THR I 164 REMARK 465 GLU I 165 REMARK 465 GLN I 166 REMARK 465 ASP I 167 REMARK 465 SER I 168 REMARK 465 LYS I 169 REMARK 465 ASP I 170 REMARK 465 SER I 171 REMARK 465 THR I 172 REMARK 465 TYR I 173 REMARK 465 SER I 174 REMARK 465 LEU I 175 REMARK 465 SER I 176 REMARK 465 SER I 177 REMARK 465 THR I 178 REMARK 465 LEU I 179 REMARK 465 THR I 180 REMARK 465 LEU I 181 REMARK 465 SER I 182 REMARK 465 LYS I 183 REMARK 465 ALA I 184 REMARK 465 ASP I 185 REMARK 465 TYR I 186 REMARK 465 GLU I 187 REMARK 465 LYS I 188 REMARK 465 HIS I 189 REMARK 465 LYS I 190 REMARK 465 VAL I 191 REMARK 465 TYR I 192 REMARK 465 ALA I 193 REMARK 465 CYS I 194 REMARK 465 GLU I 195 REMARK 465 VAL I 196 REMARK 465 THR I 197 REMARK 465 HIS I 198 REMARK 465 GLN I 199 REMARK 465 GLY I 200 REMARK 465 LEU I 201 REMARK 465 SER I 202 REMARK 465 SER I 203 REMARK 465 PRO I 204 REMARK 465 VAL I 205 REMARK 465 THR I 206 REMARK 465 LYS I 207 REMARK 465 SER I 208 REMARK 465 PHE I 209 REMARK 465 ASN I 210 REMARK 465 ARG I 211 REMARK 465 GLY I 212 REMARK 465 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 THR E 128 REMARK 465 LEU E 129 REMARK 465 GLN E 130 REMARK 465 CYS E 131 REMARK 465 THR E 132 REMARK 465 ASN E 133 REMARK 465 VAL E 134 REMARK 465 THR E 135 REMARK 465 ASN E 136 REMARK 465 ASN E 137 REMARK 465 ILE E 138 REMARK 465 THR E 139 REMARK 465 ASP E 140 REMARK 465 ASP E 141 REMARK 465 MET E 142 REMARK 465 ARG E 143 REMARK 465 GLY E 144 REMARK 465 GLU E 145 REMARK 465 LEU E 146 REMARK 465 LYS E 147 REMARK 465 ASN E 148 REMARK 465 CYS E 149 REMARK 465 SER E 150 REMARK 465 PHE E 151 REMARK 465 ASN E 152 REMARK 465 MET E 153 REMARK 465 THR E 154 REMARK 465 THR E 155 REMARK 465 GLU E 156 REMARK 465 LEU E 157 REMARK 465 ARG E 158 REMARK 465 ASP E 159 REMARK 465 LYS E 160 REMARK 465 LYS E 161 REMARK 465 GLN E 162 REMARK 465 LYS E 163 REMARK 465 VAL E 164 REMARK 465 TYR E 165 REMARK 465 SER E 166 REMARK 465 LEU E 167 REMARK 465 PHE E 168 REMARK 465 TYR E 169 REMARK 465 ARG E 170 REMARK 465 LEU E 171 REMARK 465 ASP E 172 REMARK 465 VAL E 173 REMARK 465 VAL E 174 REMARK 465 GLN E 175 REMARK 465 ILE E 176 REMARK 465 ASN E 177 REMARK 465 GLU E 178 REMARK 465 ASN E 179 REMARK 465 GLN E 180 REMARK 465 GLY E 181 REMARK 465 ASN E 182 REMARK 465 ARG E 183 REMARK 465 SER E 184 REMARK 465 ASN E 185 REMARK 465 ASN E 186 REMARK 465 SER E 187 REMARK 465 ASN E 188 REMARK 465 LYS E 189 REMARK 465 GLU E 190 REMARK 465 TYR E 191 REMARK 465 ARG E 192 REMARK 465 LEU E 193 REMARK 465 ILE E 194 REMARK 465 ASN E 303 REMARK 465 THR E 304 REMARK 465 ARG E 305 REMARK 465 LYS E 306 REMARK 465 SER E 307 REMARK 465 ILE E 308 REMARK 465 ARG E 309 REMARK 465 ILE E 310 REMARK 465 GLY E 311 REMARK 465 PRO E 312 REMARK 465 GLY E 313 REMARK 465 GLN E 314 REMARK 465 ALA E 315 REMARK 465 PHE E 316 REMARK 465 TYR E 317 REMARK 465 ALA E 318 REMARK 465 THR E 319 REMARK 465 GLY E 320 REMARK 465 ASP E 321 REMARK 465 ILE E 322 REMARK 465 ILE E 323 REMARK 465 GLY E 324 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 ASN E 411 REMARK 465 SER E 460 REMARK 465 THR E 461 REMARK 465 ASN E 462 REMARK 465 ARG E 504 REMARK 465 VAL E 505 REMARK 465 VAL E 506 REMARK 465 GLY E 507 REMARK 465 ARG E 508 REMARK 465 ARG E 509 REMARK 465 ARG E 510 REMARK 465 ARG E 511 REMARK 465 ARG E 512 REMARK 465 ARG E 513 REMARK 465 ALA F 512 REMARK 465 VAL F 513 REMARK 465 ALA F 541 REMARK 465 ARG F 542 REMARK 465 ASN F 543 REMARK 465 LEU F 544 REMARK 465 LEU F 545 REMARK 465 SER F 546 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 GLU F 657 REMARK 465 GLN F 658 REMARK 465 ASP F 659 REMARK 465 LEU F 660 REMARK 465 LEU F 661 REMARK 465 ALA F 662 REMARK 465 LEU F 663 REMARK 465 ASP F 664 REMARK 465 VAL G 110 REMARK 465 ALA G 111 REMARK 465 ALA G 112 REMARK 465 PRO G 113 REMARK 465 SER G 114 REMARK 465 VAL G 115 REMARK 465 PHE G 116 REMARK 465 ILE G 117 REMARK 465 PHE G 118 REMARK 465 PRO G 119 REMARK 465 PRO G 120 REMARK 465 SER G 121 REMARK 465 ASP G 122 REMARK 465 GLU G 123 REMARK 465 GLN G 124 REMARK 465 LEU G 125 REMARK 465 LYS G 126 REMARK 465 SER G 127 REMARK 465 GLY G 128 REMARK 465 THR G 129 REMARK 465 ALA G 130 REMARK 465 SER G 131 REMARK 465 VAL G 132 REMARK 465 VAL G 133 REMARK 465 CYS G 134 REMARK 465 LEU G 135 REMARK 465 LEU G 136 REMARK 465 ASN G 137 REMARK 465 ASN G 138 REMARK 465 PHE G 139 REMARK 465 TYR G 140 REMARK 465 PRO G 141 REMARK 465 ARG G 142 REMARK 465 GLU G 143 REMARK 465 ALA G 144 REMARK 465 LYS G 145 REMARK 465 VAL G 146 REMARK 465 GLN G 147 REMARK 465 TRP G 148 REMARK 465 LYS G 149 REMARK 465 VAL G 150 REMARK 465 ASP G 151 REMARK 465 ASN G 152 REMARK 465 ALA G 153 REMARK 465 LEU G 154 REMARK 465 GLN G 155 REMARK 465 SER G 156 REMARK 465 GLY G 157 REMARK 465 ASN G 158 REMARK 465 SER G 159 REMARK 465 GLN G 160 REMARK 465 GLU G 161 REMARK 465 SER G 162 REMARK 465 VAL G 163 REMARK 465 THR G 164 REMARK 465 GLU G 165 REMARK 465 GLN G 166 REMARK 465 ASP G 167 REMARK 465 SER G 168 REMARK 465 LYS G 169 REMARK 465 ASP G 170 REMARK 465 SER G 171 REMARK 465 THR G 172 REMARK 465 TYR G 173 REMARK 465 SER G 174 REMARK 465 LEU G 175 REMARK 465 SER G 176 REMARK 465 SER G 177 REMARK 465 THR G 178 REMARK 465 LEU G 179 REMARK 465 THR G 180 REMARK 465 LEU G 181 REMARK 465 SER G 182 REMARK 465 LYS G 183 REMARK 465 ALA G 184 REMARK 465 ASP G 185 REMARK 465 TYR G 186 REMARK 465 GLU G 187 REMARK 465 LYS G 188 REMARK 465 HIS G 189 REMARK 465 LYS G 190 REMARK 465 VAL G 191 REMARK 465 TYR G 192 REMARK 465 ALA G 193 REMARK 465 CYS G 194 REMARK 465 GLU G 195 REMARK 465 VAL G 196 REMARK 465 THR G 197 REMARK 465 HIS G 198 REMARK 465 GLN G 199 REMARK 465 GLY G 200 REMARK 465 LEU G 201 REMARK 465 SER G 202 REMARK 465 SER G 203 REMARK 465 PRO G 204 REMARK 465 VAL G 205 REMARK 465 THR G 206 REMARK 465 LYS G 207 REMARK 465 SER G 208 REMARK 465 PHE G 209 REMARK 465 ASN G 210 REMARK 465 ARG G 211 REMARK 465 GLY G 212 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 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 ASN A 195 CG OD1 ND2 REMARK 470 THR A 465 CG2 REMARK 470 GLU B 621 CG CD OE1 OE2 REMARK 470 LYS B 655 CG CD CE NZ REMARK 470 ASP K 1 CG OD1 OD2 REMARK 470 GLU F 560 CG CD OE1 OE2 REMARK 470 GLN F 562 CG CD OE1 NE2 REMARK 470 GLN F 563 CG CD OE1 NE2 REMARK 470 GLU F 621 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 NZ LYS H 23 O THR H 75 2.19 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 CYS C 54 CA - CB - SG ANGL. DEV. = 9.5 DEGREES REMARK 500 CYS E 54 CA - CB - SG ANGL. DEV. = 8.9 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 LEU A 52 151.09 -48.67 REMARK 500 LYS A 97 52.06 -94.08 REMARK 500 GLN A 258 -7.10 75.87 REMARK 500 THR A 387 48.09 -85.63 REMARK 500 THR A 450 63.49 -100.05 REMARK 500 ASN B 543 -60.26 -95.10 REMARK 500 ASN B 607 51.90 -91.08 REMARK 500 SER B 612 4.14 -68.99 REMARK 500 TRP B 614 40.34 -109.05 REMARK 500 GLU B 621 48.72 -92.85 REMARK 500 SER K 30 -116.57 68.46 REMARK 500 ASP K 32 79.88 -101.17 REMARK 500 PRO K 40 76.18 -69.61 REMARK 500 ALA K 84 -168.96 -161.87 REMARK 500 ASN L 100G 49.66 32.79 REMARK 500 THR C 50 -169.85 -127.45 REMARK 500 THR C 236 -167.32 -79.88 REMARK 500 PRO C 240 45.11 -75.63 REMARK 500 SER C 241 29.29 -142.90 REMARK 500 GLN C 258 -8.38 71.83 REMARK 500 ASN C 280 -7.22 72.98 REMARK 500 GLN C 293 127.22 -33.89 REMARK 500 ALA C 433 -168.70 -78.52 REMARK 500 LYS C 485 49.66 -93.54 REMARK 500 LYS C 487 147.01 -171.96 REMARK 500 SER I 30 -70.20 -63.75 REMARK 500 SER I 31 29.36 -140.01 REMARK 500 PRO I 44 -178.01 -69.53 REMARK 500 ALA I 51 -6.06 72.46 REMARK 500 SER I 52 -24.38 -141.58 REMARK 500 SER I 76 -60.18 -93.43 REMARK 500 PRO I 95A 76.34 -67.91 REMARK 500 ARG I 95B 57.17 -93.31 REMARK 500 CYS E 54 -179.52 -68.94 REMARK 500 PRO E 79 49.45 -87.20 REMARK 500 CYS E 196 147.84 69.28 REMARK 500 ASN E 197 -169.71 -165.19 REMARK 500 LEU E 226 -169.59 -79.18 REMARK 500 GLN E 258 -8.54 72.63 REMARK 500 ASN E 280 -3.99 67.63 REMARK 500 ASN E 300 33.89 -99.98 REMARK 500 LEU E 454 153.36 -47.36 REMARK 500 LYS E 485 52.95 -92.54 REMARK 500 PHE F 519 -73.95 -83.60 REMARK 500 LEU F 523 30.23 -92.63 REMARK 500 ALA F 526 -132.89 50.00 REMARK 500 ALA G 51 -8.64 71.23 REMARK 500 ASN G 92 30.51 -93.22 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-45530 RELATED DB: EMDB REMARK 900 STRUCTURE OF CD4 MIMETIC CJF-III-288 IN COMPLEX WITH BG505 REMARK 900 SOSIP.664 HIV-1 ENV TRIMER AND 17B FAB DBREF 9CF5 A 33 511 UNP Q2N0S6 Q2N0S6_9HIV1 32 508 DBREF 9CF5 B 512 664 UNP Q2N0S6 Q2N0S6_9HIV1 509 661 DBREF 9CF5 K 1 212 PDB 9CF5 9CF5 1 212 DBREF 9CF5 L 1 215 PDB 9CF5 9CF5 1 215 DBREF 9CF5 C 33 511 UNP Q2N0S6 Q2N0S6_9HIV1 32 508 DBREF 9CF5 D 512 664 UNP Q2N0S6 Q2N0S6_9HIV1 509 661 DBREF 9CF5 I 1 212 PDB 9CF5 9CF5 1 212 DBREF 9CF5 J 1 215 PDB 9CF5 9CF5 1 215 DBREF 9CF5 E 33 511 UNP Q2N0S6 Q2N0S6_9HIV1 32 508 DBREF 9CF5 F 512 664 UNP Q2N0S6 Q2N0S6_9HIV1 509 661 DBREF 9CF5 G 1 212 PDB 9CF5 9CF5 1 212 DBREF 9CF5 H 1 215 PDB 9CF5 9CF5 1 215 SEQADV 9CF5 ASN A 332 UNP Q2N0S6 THR 330 ENGINEERED MUTATION SEQADV 9CF5 CYS A 501 UNP Q2N0S6 ALA 498 ENGINEERED MUTATION SEQADV 9CF5 ARG A 509 UNP Q2N0S6 GLU 506 ENGINEERED MUTATION SEQADV 9CF5 ARG A 510 UNP Q2N0S6 LYS 507 ENGINEERED MUTATION SEQADV 9CF5 ARG A 512 UNP Q2N0S6 INSERTION SEQADV 9CF5 ARG A 513 UNP Q2N0S6 INSERTION SEQADV 9CF5 PRO B 559 UNP Q2N0S6 ILE 556 ENGINEERED MUTATION SEQADV 9CF5 CYS B 605 UNP Q2N0S6 THR 602 ENGINEERED MUTATION SEQADV 9CF5 ASN C 332 UNP Q2N0S6 THR 330 ENGINEERED MUTATION SEQADV 9CF5 CYS C 501 UNP Q2N0S6 ALA 498 ENGINEERED MUTATION SEQADV 9CF5 ARG C 509 UNP Q2N0S6 GLU 506 ENGINEERED MUTATION SEQADV 9CF5 ARG C 510 UNP Q2N0S6 LYS 507 ENGINEERED MUTATION SEQADV 9CF5 ARG C 512 UNP Q2N0S6 INSERTION SEQADV 9CF5 ARG C 513 UNP Q2N0S6 INSERTION SEQADV 9CF5 PRO D 559 UNP Q2N0S6 ILE 556 ENGINEERED MUTATION SEQADV 9CF5 CYS D 605 UNP Q2N0S6 THR 602 ENGINEERED MUTATION SEQADV 9CF5 ASN E 332 UNP Q2N0S6 THR 330 ENGINEERED MUTATION SEQADV 9CF5 CYS E 501 UNP Q2N0S6 ALA 498 ENGINEERED MUTATION SEQADV 9CF5 ARG E 509 UNP Q2N0S6 GLU 506 ENGINEERED MUTATION SEQADV 9CF5 ARG E 510 UNP Q2N0S6 LYS 507 ENGINEERED MUTATION SEQADV 9CF5 ARG E 512 UNP Q2N0S6 INSERTION SEQADV 9CF5 ARG E 513 UNP Q2N0S6 INSERTION SEQADV 9CF5 PRO F 559 UNP Q2N0S6 ILE 556 ENGINEERED MUTATION SEQADV 9CF5 CYS F 605 UNP Q2N0S6 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 K 214 ASP ILE VAL MET THR GLN SER PRO ALA THR LEU SER VAL SEQRES 2 K 214 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 K 214 GLU SER VAL SER SER ASP LEU ALA TRP TYR GLN GLN LYS SEQRES 4 K 214 PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR GLY ALA SER SEQRES 5 K 214 THR ARG ALA THR GLY VAL PRO ALA ARG PHE SER GLY SER SEQRES 6 K 214 GLY SER GLY ALA GLU PHE THR LEU THR ILE SER SER LEU SEQRES 7 K 214 GLN SER GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN TYR SEQRES 8 K 214 ASN ASN TRP PRO PRO ARG TYR THR PHE GLY GLN GLY THR SEQRES 9 K 214 ARG LEU GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL SEQRES 10 K 214 PHE ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY SEQRES 11 K 214 THR ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO SEQRES 12 K 214 ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU SEQRES 13 K 214 GLN SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SEQRES 14 K 214 SER LYS ASP SER THR TYR SER LEU SER SER THR LEU THR SEQRES 15 K 214 LEU SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA SEQRES 16 K 214 CYS GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR SEQRES 17 K 214 LYS SER PHE ASN ARG GLY SEQRES 1 L 230 GLU VAL GLN LEU VAL GLU SER GLY ALA GLU VAL LYS LYS SEQRES 2 L 230 PRO GLY SER SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 L 230 ASP THR PHE ILE ARG TYR SER PHE THR TRP VAL ARG GLN SEQRES 4 L 230 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY ARG ILE ILE SEQRES 5 L 230 THR ILE LEU ASP VAL ALA HIS TYR ALA PRO HIS LEU GLN SEQRES 6 L 230 GLY ARG VAL THR ILE THR ALA ASP LYS SER THR SER THR SEQRES 7 L 230 VAL TYR LEU GLU LEU ARG ASN LEU ARG SER ASP ASP THR SEQRES 8 L 230 ALA VAL TYR PHE CYS ALA GLY VAL TYR GLU GLY GLU ALA SEQRES 9 L 230 ASP GLU GLY GLU TYR ASP ASN ASN GLY PHE LEU LYS HIS SEQRES 10 L 230 TRP GLY GLN GLY THR LEU VAL THR VAL SER SER ALA SER SEQRES 11 L 230 THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER SEQRES 12 L 230 LYS SER THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU SEQRES 13 L 230 VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP SEQRES 14 L 230 ASN SER GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO SEQRES 15 L 230 ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SER SEQRES 16 L 230 VAL VAL THR VAL PRO SER SER SER LEU GLY THR GLN THR SEQRES 17 L 230 TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS SEQRES 18 L 230 VAL ASP LYS ARG VAL GLU PRO LYS SER 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 I 214 ASP ILE VAL MET THR GLN SER PRO ALA THR LEU SER VAL SEQRES 2 I 214 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 I 214 GLU SER VAL SER SER ASP LEU ALA TRP TYR GLN GLN LYS SEQRES 4 I 214 PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR GLY ALA SER SEQRES 5 I 214 THR ARG ALA THR GLY VAL PRO ALA ARG PHE SER GLY SER SEQRES 6 I 214 GLY SER GLY ALA GLU PHE THR LEU THR ILE SER SER LEU SEQRES 7 I 214 GLN SER GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN TYR SEQRES 8 I 214 ASN ASN TRP PRO PRO ARG TYR THR PHE GLY GLN GLY THR SEQRES 9 I 214 ARG LEU GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL SEQRES 10 I 214 PHE ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY SEQRES 11 I 214 THR ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO SEQRES 12 I 214 ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU SEQRES 13 I 214 GLN SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SEQRES 14 I 214 SER LYS ASP SER THR TYR SER LEU SER SER THR LEU THR SEQRES 15 I 214 LEU SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA SEQRES 16 I 214 CYS GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR SEQRES 17 I 214 LYS SER PHE ASN ARG GLY SEQRES 1 J 230 GLU VAL GLN LEU VAL GLU SER GLY ALA GLU VAL LYS LYS SEQRES 2 J 230 PRO GLY SER SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 J 230 ASP THR PHE ILE ARG TYR SER PHE THR TRP VAL ARG GLN SEQRES 4 J 230 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY ARG ILE ILE SEQRES 5 J 230 THR ILE LEU ASP VAL ALA HIS TYR ALA PRO HIS LEU GLN SEQRES 6 J 230 GLY ARG VAL THR ILE THR ALA ASP LYS SER THR SER THR SEQRES 7 J 230 VAL TYR LEU GLU LEU ARG ASN LEU ARG SER ASP ASP THR SEQRES 8 J 230 ALA VAL TYR PHE CYS ALA GLY VAL TYR GLU GLY GLU ALA SEQRES 9 J 230 ASP GLU GLY GLU TYR ASP ASN ASN GLY PHE LEU LYS HIS SEQRES 10 J 230 TRP GLY GLN GLY THR LEU VAL THR VAL SER SER ALA SER SEQRES 11 J 230 THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER SEQRES 12 J 230 LYS SER THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU SEQRES 13 J 230 VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP SEQRES 14 J 230 ASN SER GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO SEQRES 15 J 230 ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SER SEQRES 16 J 230 VAL VAL THR VAL PRO SER SER SER LEU GLY THR GLN THR SEQRES 17 J 230 TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS SEQRES 18 J 230 VAL ASP LYS ARG VAL GLU PRO LYS SER 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 G 214 ASP ILE VAL MET THR GLN SER PRO ALA THR LEU SER VAL SEQRES 2 G 214 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 G 214 GLU SER VAL SER SER ASP LEU ALA TRP TYR GLN GLN LYS SEQRES 4 G 214 PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR GLY ALA SER SEQRES 5 G 214 THR ARG ALA THR GLY VAL PRO ALA ARG PHE SER GLY SER SEQRES 6 G 214 GLY SER GLY ALA GLU PHE THR LEU THR ILE SER SER LEU SEQRES 7 G 214 GLN SER GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN TYR SEQRES 8 G 214 ASN ASN TRP PRO PRO ARG TYR THR PHE GLY GLN GLY THR SEQRES 9 G 214 ARG LEU GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL SEQRES 10 G 214 PHE ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY SEQRES 11 G 214 THR ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO SEQRES 12 G 214 ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU SEQRES 13 G 214 GLN SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SEQRES 14 G 214 SER LYS ASP SER THR TYR SER LEU SER SER THR LEU THR SEQRES 15 G 214 LEU SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA SEQRES 16 G 214 CYS GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR SEQRES 17 G 214 LYS SER PHE ASN ARG GLY SEQRES 1 H 230 GLU VAL GLN LEU VAL GLU SER GLY ALA GLU VAL LYS LYS SEQRES 2 H 230 PRO GLY SER SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 H 230 ASP THR PHE ILE ARG TYR SER PHE THR TRP VAL ARG GLN SEQRES 4 H 230 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY ARG ILE ILE SEQRES 5 H 230 THR ILE LEU ASP VAL ALA HIS TYR ALA PRO HIS LEU GLN SEQRES 6 H 230 GLY ARG VAL THR ILE THR ALA ASP LYS SER THR SER THR SEQRES 7 H 230 VAL TYR LEU GLU LEU ARG ASN LEU ARG SER ASP ASP THR SEQRES 8 H 230 ALA VAL TYR PHE CYS ALA GLY VAL TYR GLU GLY GLU ALA SEQRES 9 H 230 ASP GLU GLY GLU TYR ASP ASN ASN GLY PHE LEU LYS HIS SEQRES 10 H 230 TRP GLY GLN GLY THR LEU VAL THR VAL SER SER ALA SER SEQRES 11 H 230 THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER SEQRES 12 H 230 LYS SER THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU SEQRES 13 H 230 VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP SEQRES 14 H 230 ASN SER GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO SEQRES 15 H 230 ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SER SEQRES 16 H 230 VAL VAL THR VAL PRO SER SER SER LEU GLY THR GLN THR SEQRES 17 H 230 TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS SEQRES 18 H 230 VAL ASP LYS ARG VAL GLU PRO LYS SER HET NAG M 1 14 HET NAG M 2 14 HET NAG N 1 14 HET NAG N 2 14 HET BMA N 3 11 HET MAN N 4 11 HET MAN N 5 11 HET MAN N 6 11 HET NAG W 1 14 HET NAG W 2 14 HET NAG X 1 14 HET NAG X 2 14 HET NAG O 1 14 HET NAG O 2 14 HET BMA O 3 11 HET MAN O 4 11 HET MAN O 5 11 HET MAN O 6 11 HET MAN O 7 11 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 MAN S 4 11 HET MAN S 5 11 HET MAN S 6 11 HET MAN S 7 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 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 Y26 A 608 37 HET NAG B 701 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 Y26 C 609 37 HET NAG D 701 14 HET NAG D 702 14 HET NAG E 601 14 HET NAG E 602 14 HET NAG E 603 14 HET NAG E 604 14 HET NAG E 605 14 HET NAG E 606 14 HET NAG E 607 14 HET NAG E 608 14 HET Y26 E 609 37 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BMA BETA-D-MANNOPYRANOSE HETNAM MAN ALPHA-D-MANNOPYRANOSE HETNAM Y26 PROPYL (2R,3S)-2-(CARBAMIMIDAMIDOMETHYL)-3-[2-(4- HETNAM 2 Y26 CHLORO-3-FLUOROANILINO)(OXO)ACETAMIDO]-6- HETNAM 3 Y26 [(METHYLAMINO)METHYL]-2,3-DIHYDRO-1H-INDOLE-1- HETNAM 4 Y26 CARBOXYLATE HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA- HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO- HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE FORMUL 13 NAG 50(C8 H15 N O6) FORMUL 14 BMA 3(C6 H12 O6) FORMUL 14 MAN 11(C6 H12 O6) FORMUL 32 Y26 3(C24 H29 CL F N7 O4) HELIX 1 AA1 GLU A 64 CYS A 74 1 11 HELIX 2 AA2 ASN A 99 LEU A 116 1 18 HELIX 3 AA3 LYS A 335 GLY A 354 1 20 HELIX 4 AA4 ASP A 368 THR A 373 1 6 HELIX 5 AA5 ASN A 386 PHE A 391 5 6 HELIX 6 AA6 MET A 475 LEU A 483 1 9 HELIX 7 AA7 ILE B 515 GLY B 521 1 7 HELIX 8 AA8 PHE B 522 GLY B 524 5 3 HELIX 9 AA9 THR B 529 THR B 536 1 8 HELIX 10 AB1 THR B 538 LEU B 544 1 7 HELIX 11 AB2 GLU B 560 LYS B 567 1 8 HELIX 12 AB3 VAL B 570 TRP B 596 1 27 HELIX 13 AB4 LEU B 619 TRP B 623 5 5 HELIX 14 AB5 THR B 627 ILE B 635 1 9 HELIX 15 AB6 TYR B 638 LYS B 655 1 18 HELIX 16 AB7 ARG L 83 THR L 87 5 5 HELIX 17 AB8 GLU C 64 CYS C 74 1 11 HELIX 18 AB9 ASN C 99 LEU C 116 1 18 HELIX 19 AC1 LYS C 335 PHE C 353 1 19 HELIX 20 AC2 ASP C 368 THR C 373 1 6 HELIX 21 AC3 ARG C 476 SER C 481 1 6 HELIX 22 AC4 LEU D 523 GLY D 527 5 5 HELIX 23 AC5 THR D 529 THR D 538 1 10 HELIX 24 AC6 HIS D 564 GLY D 597 1 34 HELIX 25 AC7 SER D 620 ASN D 625 1 6 HELIX 26 AC8 THR D 627 ILE D 635 1 9 HELIX 27 AC9 TYR D 638 ASP D 659 1 22 HELIX 28 AD1 ARG J 83 THR J 87 5 5 HELIX 29 AD2 GLU E 64 CYS E 74 1 11 HELIX 30 AD3 ASN E 99 LEU E 116 1 18 HELIX 31 AD4 LYS E 335 PHE E 353 1 19 HELIX 32 AD5 MET E 475 TRP E 479 5 5 HELIX 33 AD6 GLY F 516 GLY F 521 1 6 HELIX 34 AD7 ALA F 533 GLN F 540 1 8 HELIX 35 AD8 ALA F 561 TRP F 596 1 36 HELIX 36 AD9 ASN F 618 ASN F 625 1 8 HELIX 37 AE1 THR F 627 SER F 636 1 10 HELIX 38 AE2 TYR F 638 SER F 649 1 12 HELIX 39 AE3 GLN F 650 GLU F 654 5 5 HELIX 40 AE4 GLN G 79 PHE G 83 5 5 HELIX 41 AE5 ARG H 83 THR H 87 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 TRP A 35 O THR A 499 SHEET 3 AA1 3 ILE B 603 PRO B 609 -1 O THR B 606 N VAL A 36 SHEET 1 AA2 3 TRP A 45 ASP A 47 0 SHEET 2 AA2 3 LYS A 487 ILE A 491 -1 O LYS A 490 N LYS A 46 SHEET 3 AA2 3 PHE A 223 LEU A 226 -1 N LEU A 226 O LYS A 487 SHEET 1 AA3 3 VAL A 75 PRO A 76 0 SHEET 2 AA3 3 PHE A 53 SER A 56 1 N SER A 56 O VAL A 75 SHEET 3 AA3 3 ILE A 215 CYS A 218 -1 O HIS A 216 N ALA A 55 SHEET 1 AA4 2 GLU A 83 LEU A 86 0 SHEET 2 AA4 2 VAL A 242 VAL A 245 -1 O THR A 244 N ILE A 84 SHEET 1 AA5 2 VAL A 120 LYS A 121 0 SHEET 2 AA5 2 ILE A 201 THR A 202 -1 O ILE A 201 N LYS A 121 SHEET 1 AA6 3 SER A 256 THR A 257 0 SHEET 2 AA6 3 SER A 375 CYS A 378 -1 O SER A 375 N THR A 257 SHEET 3 AA6 3 GLU A 381 PHE A 383 -1 O PHE A 383 N PHE A 376 SHEET 1 AA7 4 MET A 271 ARG A 273 0 SHEET 2 AA7 4 ILE A 284 GLN A 287 -1 O LEU A 285 N ARG A 273 SHEET 3 AA7 4 LEU A 452 ARG A 456 -1 O LEU A 454 N ILE A 284 SHEET 4 AA7 4 PHE A 468 PRO A 470 -1 O ARG A 469 N THR A 455 SHEET 1 AA8 4 SER A 413 CYS A 418 0 SHEET 2 AA8 4 ALA A 329 SER A 334 -1 N CYS A 331 O LEU A 416 SHEET 3 AA8 4 VAL A 292 ARG A 298 -1 N THR A 297 O HIS A 330 SHEET 4 AA8 4 ILE A 443 ILE A 449 -1 O SER A 447 N ILE A 294 SHEET 1 AA9 2 ILE A 423 ILE A 424 0 SHEET 2 AA9 2 ALA A 433 MET A 434 -1 O ALA A 433 N ILE A 424 SHEET 1 AB1 2 LEU K 33 GLN K 38 0 SHEET 2 AB1 2 VAL K 85 GLN K 90 -1 O TYR K 87 N TYR K 36 SHEET 1 AB2 2 GLN L 3 GLU L 6 0 SHEET 2 AB2 2 CYS L 22 SER L 25 -1 O LYS L 23 N VAL L 5 SHEET 1 AB3 5 VAL L 56 ALA L 57 0 SHEET 2 AB3 5 ARG L 50 ILE L 52 -1 N ILE L 52 O VAL L 56 SHEET 3 AB3 5 SER L 33 GLN L 39 -1 N PHE L 34 O ILE L 51 SHEET 4 AB3 5 VAL L 89 VAL L 95 -1 O PHE L 91 N VAL L 37 SHEET 5 AB3 5 THR L 107 LEU L 108 -1 O THR L 107 N TYR L 90 SHEET 1 AB4 2 VAL L 67 ASP L 72 0 SHEET 2 AB4 2 THR L 77 LEU L 82 -1 O GLU L 81 N THR L 68 SHEET 1 AB5 3 VAL C 496 ALA C 497 0 SHEET 2 AB5 3 TRP C 35 TYR C 39 -1 N THR C 37 O ALA C 497 SHEET 3 AB5 3 ILE D 603 PRO D 609 -1 O CYS D 604 N VAL C 38 SHEET 1 AB6 3 VAL C 44 ASP C 47 0 SHEET 2 AB6 3 LYS C 487 GLU C 492 -1 O GLU C 492 N VAL C 44 SHEET 3 AB6 3 PHE C 223 LEU C 226 -1 N ALA C 224 O VAL C 489 SHEET 1 AB7 2 PHE C 53 ALA C 55 0 SHEET 2 AB7 2 HIS C 216 CYS C 218 -1 O HIS C 216 N ALA C 55 SHEET 1 AB8 2 ILE C 84 HIS C 85 0 SHEET 2 AB8 2 SER C 243 THR C 244 -1 O THR C 244 N ILE C 84 SHEET 1 AB9 2 GLU C 92 PHE C 93 0 SHEET 2 AB9 2 GLY C 237 PRO C 238 -1 O GLY C 237 N PHE C 93 SHEET 1 AC1 4 LEU C 259 LEU C 261 0 SHEET 2 AC1 4 ILE C 449 LEU C 454 -1 O THR C 450 N LEU C 260 SHEET 3 AC1 4 ILE C 284 GLN C 287 -1 N ILE C 284 O LEU C 454 SHEET 4 AC1 4 ILE C 272 ARG C 273 -1 N ARG C 273 O LEU C 285 SHEET 1 AC2 6 HIS C 374 CYS C 378 0 SHEET 2 AC2 6 GLU C 381 CYS C 385 -1 O GLU C 381 N CYS C 378 SHEET 3 AC2 6 SER C 413 LYS C 421 -1 O ARG C 419 N TYR C 384 SHEET 4 AC2 6 GLN C 328 SER C 334 -1 N ALA C 329 O CYS C 418 SHEET 5 AC2 6 ILE C 294 ARG C 298 -1 N THR C 297 O HIS C 330 SHEET 6 AC2 6 ILE C 443 SER C 447 -1 O SER C 447 N ILE C 294 SHEET 1 AC3 3 THR C 394 TRP C 395 0 SHEET 2 AC3 3 ILE C 359 PHE C 361 -1 N ILE C 359 O TRP C 395 SHEET 3 AC3 3 GLU C 466 PHE C 468 1 O GLU C 466 N ARG C 360 SHEET 1 AC4 3 THR I 20 ARG I 24 0 SHEET 2 AC4 3 GLU I 70 THR I 74 -1 O LEU I 73 N LEU I 21 SHEET 3 AC4 3 SER I 63 SER I 67 -1 N SER I 63 O THR I 74 SHEET 1 AC5 4 THR I 53 ARG I 54 0 SHEET 2 AC5 4 ARG I 45 TYR I 49 -1 N TYR I 49 O THR I 53 SHEET 3 AC5 4 LEU I 33 GLN I 38 -1 N TRP I 35 O LEU I 47 SHEET 4 AC5 4 VAL I 85 GLN I 90 -1 O GLN I 89 N ALA I 34 SHEET 1 AC6 4 LEU J 4 GLU J 6 0 SHEET 2 AC6 4 SER J 17 ALA J 24 -1 O LYS J 23 N VAL J 5 SHEET 3 AC6 4 THR J 77 ARG J 82A-1 O LEU J 80 N VAL J 20 SHEET 4 AC6 4 VAL J 67 ASP J 72 -1 N ASP J 72 O THR J 77 SHEET 1 AC7 5 VAL J 56 TYR J 59 0 SHEET 2 AC7 5 LEU J 45 ILE J 52 -1 N ILE J 52 O VAL J 56 SHEET 3 AC7 5 SER J 33 GLN J 39 -1 N ARG J 38 O GLU J 46 SHEET 4 AC7 5 ALA J 88 VAL J 95 -1 O VAL J 89 N GLN J 39 SHEET 5 AC7 5 HIS J 102 TRP J 103 -1 O HIS J 102 N GLY J 94 SHEET 1 AC8 5 VAL J 56 TYR J 59 0 SHEET 2 AC8 5 LEU J 45 ILE J 52 -1 N ILE J 52 O VAL J 56 SHEET 3 AC8 5 SER J 33 GLN J 39 -1 N ARG J 38 O GLU J 46 SHEET 4 AC8 5 ALA J 88 VAL J 95 -1 O VAL J 89 N GLN J 39 SHEET 5 AC8 5 THR J 107 VAL J 109 -1 O VAL J 109 N ALA J 88 SHEET 1 AC9 3 ALA E 497 THR E 499 0 SHEET 2 AC9 3 TRP E 35 THR E 37 -1 N TRP E 35 O THR E 499 SHEET 3 AC9 3 CYS F 605 PRO F 609 -1 O VAL F 608 N VAL E 36 SHEET 1 AD1 3 TRP E 45 ASP E 47 0 SHEET 2 AD1 3 VAL E 488 ILE E 491 -1 O LYS E 490 N LYS E 46 SHEET 3 AD1 3 PHE E 223 ILE E 225 -1 N ALA E 224 O VAL E 489 SHEET 1 AD2 2 PHE E 53 ALA E 55 0 SHEET 2 AD2 2 HIS E 216 CYS E 218 -1 O CYS E 218 N PHE E 53 SHEET 1 AD3 2 ILE E 84 LEU E 86 0 SHEET 2 AD3 2 VAL E 242 THR E 244 -1 O VAL E 242 N LEU E 86 SHEET 1 AD4 2 GLU E 91 ASN E 94 0 SHEET 2 AD4 2 THR E 236 CYS E 239 -1 N CYS E 239 O GLU E 91 SHEET 1 AD5 6 ASN E 377 CYS E 378 0 SHEET 2 AD5 6 GLU E 381 TYR E 384 -1 O GLU E 381 N CYS E 378 SHEET 3 AD5 6 SER E 413 LYS E 421 -1 O ARG E 419 N TYR E 384 SHEET 4 AD5 6 GLN E 328 SER E 334 -1 N ALA E 329 O CYS E 418 SHEET 5 AD5 6 ILE E 294 ARG E 298 -1 N THR E 297 O HIS E 330 SHEET 6 AD5 6 ILE E 443 SER E 447 -1 O SER E 447 N ILE E 294 SHEET 1 AD6 3 SER E 393 TRP E 395 0 SHEET 2 AD6 3 ILE E 359 PHE E 361 -1 N ILE E 359 O TRP E 395 SHEET 3 AD6 3 GLU E 466 THR E 467 1 O GLU E 466 N ARG E 360 SHEET 1 AD7 5 THR G 53 ARG G 54 0 SHEET 2 AD7 5 ARG G 45 TYR G 49 -1 N TYR G 49 O THR G 53 SHEET 3 AD7 5 ALA G 34 GLN G 37 -1 N TRP G 35 O ILE G 48 SHEET 4 AD7 5 TYR G 87 GLN G 90 -1 O TYR G 87 N TYR G 36 SHEET 5 AD7 5 THR G 97 PHE G 98 -1 O THR G 97 N GLN G 90 SHEET 1 AD8 2 SER G 65 SER G 67 0 SHEET 2 AD8 2 GLU G 70 THR G 72 -1 O THR G 72 N SER G 65 SHEET 1 AD9 4 GLN H 3 LEU H 4 0 SHEET 2 AD9 4 CYS H 22 SER H 25 -1 O SER H 25 N GLN H 3 SHEET 3 AD9 4 THR H 77 VAL H 78 -1 O VAL H 78 N CYS H 22 SHEET 4 AD9 4 ALA H 71 ASP H 72 -1 N ASP H 72 O THR H 77 SHEET 1 AE1 4 VAL H 56 TYR H 59 0 SHEET 2 AE1 4 LEU H 45 ILE H 52 -1 N ARG H 50 O HIS H 58 SHEET 3 AE1 4 SER H 33 GLN H 39 -1 N ARG H 38 O GLU H 46 SHEET 4 AE1 4 VAL H 89 VAL H 95 -1 O ALA H 93 N THR H 35 SHEET 1 AE2 2 VAL H 67 THR H 68 0 SHEET 2 AE2 2 GLU H 81 LEU H 82 -1 O GLU H 81 N THR H 68 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 218 CYS A 247 1555 1555 2.04 SSBOND 5 CYS A 228 CYS A 239 1555 1555 2.03 SSBOND 6 CYS A 296 CYS A 331 1555 1555 2.03 SSBOND 7 CYS A 378 CYS A 445 1555 1555 2.03 SSBOND 8 CYS A 385 CYS A 418 1555 1555 2.03 SSBOND 9 CYS A 501 CYS B 605 1555 1555 2.03 SSBOND 10 CYS B 598 CYS B 604 1555 1555 2.03 SSBOND 11 CYS K 23 CYS K 88 1555 1555 2.03 SSBOND 12 CYS L 22 CYS L 92 1555 1555 2.03 SSBOND 13 CYS C 54 CYS C 74 1555 1555 2.03 SSBOND 14 CYS C 119 CYS C 205 1555 1555 2.03 SSBOND 15 CYS C 126 CYS C 196 1555 1555 2.03 SSBOND 16 CYS C 218 CYS C 247 1555 1555 2.03 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 2.05 SSBOND 21 CYS C 501 CYS D 605 1555 1555 2.04 SSBOND 22 CYS D 598 CYS D 604 1555 1555 2.03 SSBOND 23 CYS I 23 CYS I 88 1555 1555 2.03 SSBOND 24 CYS J 22 CYS J 92 1555 1555 2.03 SSBOND 25 CYS E 54 CYS E 74 1555 1555 2.03 SSBOND 26 CYS E 119 CYS E 205 1555 1555 2.03 SSBOND 27 CYS E 126 CYS E 196 1555 1555 2.03 SSBOND 28 CYS E 218 CYS E 247 1555 1555 2.03 SSBOND 29 CYS E 228 CYS E 239 1555 1555 2.03 SSBOND 30 CYS E 296 CYS E 331 1555 1555 2.03 SSBOND 31 CYS E 378 CYS E 445 1555 1555 2.03 SSBOND 32 CYS E 385 CYS E 418 1555 1555 2.02 SSBOND 33 CYS E 501 CYS F 605 1555 1555 2.03 SSBOND 34 CYS F 598 CYS F 604 1555 1555 2.03 SSBOND 35 CYS G 23 CYS G 88 1555 1555 2.03 SSBOND 36 CYS H 22 CYS H 92 1555 1555 2.03 LINK ND2 ASN A 234 C1 NAG M 1 1555 1555 1.44 LINK ND2 ASN A 262 C1 NAG N 1 1555 1555 1.43 LINK ND2 ASN A 276 C1 NAG W 1 1555 1555 1.44 LINK ND2 ASN A 295 C1 NAG A 601 1555 1555 1.44 LINK ND2 ASN A 332 C1 NAG A 602 1555 1555 1.44 LINK ND2 ASN A 339 C1 NAG A 603 1555 1555 1.44 LINK ND2 ASN A 355 C1 NAG A 604 1555 1555 1.47 LINK ND2 ASN A 363 C1 NAG A 605 1555 1555 1.44 LINK ND2 ASN A 386 C1 NAG X 1 1555 1555 1.44 LINK ND2 ASN A 392 C1 NAG A 606 1555 1555 1.45 LINK ND2 ASN A 448 C1 NAG A 607 1555 1555 1.44 LINK ND2 ASN B 637 C1 NAG B 701 1555 1555 1.44 LINK ND2 ASN C 88 C1 NAG C 601 1555 1555 1.44 LINK ND2 ASN C 234 C1 NAG C 602 1555 1555 1.44 LINK ND2 ASN C 262 C1 NAG O 1 1555 1555 1.44 LINK ND2 ASN C 276 C1 NAG P 1 1555 1555 1.44 LINK ND2 ASN C 295 C1 NAG C 603 1555 1555 1.44 LINK ND2 ASN C 332 C1 NAG C 604 1555 1555 1.44 LINK ND2 ASN C 339 C1 NAG Q 1 1555 1555 1.44 LINK ND2 ASN C 355 C1 NAG C 605 1555 1555 1.44 LINK ND2 ASN C 363 C1 NAG C 606 1555 1555 1.44 LINK ND2 ASN C 386 C1 NAG R 1 1555 1555 1.44 LINK ND2 ASN C 392 C1 NAG C 607 1555 1555 1.45 LINK ND2 ASN C 448 C1 NAG C 608 1555 1555 1.44 LINK ND2 ASN D 618 C1 NAG D 701 1555 1555 1.44 LINK ND2 ASN D 637 C1 NAG D 702 1555 1555 1.44 LINK ND2 ASN E 88 C1 NAG E 601 1555 1555 1.44 LINK ND2 ASN E 234 C1 NAG E 602 1555 1555 1.44 LINK ND2 ASN E 262 C1 NAG S 1 1555 1555 1.44 LINK ND2 ASN E 276 C1 NAG T 1 1555 1555 1.44 LINK ND2 ASN E 295 C1 NAG E 603 1555 1555 1.44 LINK ND2 ASN E 332 C1 NAG E 604 1555 1555 1.44 LINK ND2 ASN E 339 C1 NAG U 1 1555 1555 1.44 LINK ND2 ASN E 355 C1 NAG E 605 1555 1555 1.45 LINK ND2 ASN E 363 C1 NAG E 606 1555 1555 1.44 LINK ND2 ASN E 386 C1 NAG V 1 1555 1555 1.44 LINK ND2 ASN E 392 C1 NAG E 607 1555 1555 1.44 LINK ND2 ASN E 448 C1 NAG E 608 1555 1555 1.44 LINK O4 NAG M 1 C1 NAG M 2 1555 1555 1.44 LINK O4 NAG N 1 C1 NAG N 2 1555 1555 1.44 LINK O4 NAG N 2 C1 BMA N 3 1555 1555 1.44 LINK O3 BMA N 3 C1 MAN N 4 1555 1555 1.44 LINK O6 BMA N 3 C1 MAN N 6 1555 1555 1.45 LINK O2 MAN N 4 C1 MAN N 5 1555 1555 1.44 LINK O4 NAG W 1 C1 NAG W 2 1555 1555 1.44 LINK O4 NAG X 1 C1 NAG X 2 1555 1555 1.44 LINK O4 NAG O 1 C1 NAG O 2 1555 1555 1.44 LINK O4 NAG O 2 C1 BMA O 3 1555 1555 1.44 LINK O3 BMA O 3 C1 MAN O 4 1555 1555 1.44 LINK O6 BMA O 3 C1 MAN O 6 1555 1555 1.44 LINK O2 MAN O 4 C1 MAN O 5 1555 1555 1.44 LINK O3 MAN O 6 C1 MAN O 7 1555 1555 1.45 LINK O4 NAG P 1 C1 NAG P 2 1555 1555 1.45 LINK O4 NAG Q 1 C1 NAG Q 2 1555 1555 1.44 LINK O4 NAG R 1 C1 NAG R 2 1555 1555 1.44 LINK O4 NAG S 1 C1 NAG S 2 1555 1555 1.44 LINK O4 NAG S 2 C1 BMA S 3 1555 1555 1.44 LINK O3 BMA S 3 C1 MAN S 4 1555 1555 1.44 LINK O6 BMA S 3 C1 MAN S 6 1555 1555 1.45 LINK O2 MAN S 4 C1 MAN S 5 1555 1555 1.44 LINK O3 MAN S 6 C1 MAN S 7 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 1.45 LINK O4 NAG V 1 C1 NAG V 2 1555 1555 1.45 CISPEP 1 TRP K 94 PRO K 95 0 6.77 CISPEP 2 SER I 7 PRO I 8 0 -0.76 CISPEP 3 TRP I 94 PRO I 95 0 5.52 CISPEP 4 SER G 7 PRO G 8 0 -4.17 CISPEP 5 TRP G 94 PRO G 95 0 2.65 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