HEADER VIRAL PROTEIN/IMMUNE SYSTEM 20-AUG-24 9D8Y TITLE CRYO-EM STRUCTURE OF HIV-1 BG505 SOSIP.664 ENV BOUND TO 3-SCD4, 3- TITLE 2 VRC34.01 FAB WITH ONE GP120 ROTATED COMPND MOL_ID: 1; COMPND 2 MOLECULE: ENVELOPE GLYCOPROTEIN GP160; COMPND 3 CHAIN: A, B, C; COMPND 4 SYNONYM: ENV POLYPROTEIN; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES; COMPND 7 OTHER_DETAILS: BG505 SOSIP.664 CONSTRUCT; COMPND 8 MOL_ID: 2; COMPND 9 MOLECULE: ENVELOPE GLYCOPROTEIN GP160; COMPND 10 CHAIN: D, E, F; COMPND 11 FRAGMENT: UNP RESIDUES 509-611; COMPND 12 ENGINEERED: YES; COMPND 13 MUTATION: YES; COMPND 14 OTHER_DETAILS: BG505 SOSIP.664 CONSTRUCT; COMPND 15 MOL_ID: 3; COMPND 16 MOLECULE: VRC34.01 FAB HEAVY CHAIN; COMPND 17 CHAIN: G, I, K; COMPND 18 ENGINEERED: YES; COMPND 19 MOL_ID: 4; COMPND 20 MOLECULE: VRC34.01 FAB LIGHT CHAIN; COMPND 21 CHAIN: H, J, L; COMPND 22 ENGINEERED: YES; COMPND 23 MOL_ID: 5; COMPND 24 MOLECULE: T-CELL SURFACE GLYCOPROTEIN CD4; COMPND 25 CHAIN: M, N, O; COMPND 26 FRAGMENT: RESIDUES 1-96; COMPND 27 SYNONYM: T-CELL SURFACE ANTIGEN T4/LEU-3; COMPND 28 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: MAMMALIA; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 40674; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 9 ORGANISM_TAXID: 11676; SOURCE 10 GENE: ENV; SOURCE 11 EXPRESSION_SYSTEM: MAMMALIA; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 40674; SOURCE 13 MOL_ID: 3; SOURCE 14 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 15 ORGANISM_TAXID: 9606; SOURCE 16 EXPRESSION_SYSTEM: MAMMALIA; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 40674; SOURCE 18 MOL_ID: 4; SOURCE 19 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 20 ORGANISM_TAXID: 9606; SOURCE 21 EXPRESSION_SYSTEM: MAMMALIA; SOURCE 22 EXPRESSION_SYSTEM_TAXID: 40674; SOURCE 23 MOL_ID: 5; SOURCE 24 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 25 ORGANISM_COMMON: HUMAN; SOURCE 26 ORGANISM_TAXID: 9606; SOURCE 27 GENE: CD4; SOURCE 28 EXPRESSION_SYSTEM: MAMMALIA; SOURCE 29 EXPRESSION_SYSTEM_TAXID: 40674 KEYWDS RECOMBINANT PROTEIN, HIV-1 ENV, CD4, FUSION PEPTIDE BINNING ANTIBODY KEYWDS 2 VRC34.01, VACCINE, VIRAL PROTEIN, VIRAL PROTEIN-IMMUNE SYSTEM KEYWDS 3 COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR B.THAKUR,P.ACHARYA REVDAT 1 30-APR-25 9D8Y 0 JRNL AUTH B.THAKUR,P.ACHARYA JRNL TITL CRYO-EM STRUCTURE OF HIV-1 BG505 SOSIP.664 ENV BOUND TO JRNL TITL 2 3-SCD4, 3-VRC34.01 FAB WITH ONE GP120 ROTATED JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 4.06 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : CRYOSPARC, LATITUDE, CRYOSPARC, REMARK 3 CRYOSPARC, CRYOSPARC, CRYOSPARC REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : NULL REMARK 3 REFINEMENT SPACE : REAL 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) : 4.060 REMARK 3 NUMBER OF PARTICLES : 274345 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 9D8Y COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-AUG-24. REMARK 100 THE DEPOSITION ID IS D_1000287569. 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 : HIV-1 BG505 SOSIP.664 ENV IN REMARK 245 COMPLEX WITH 3 MOLECULES OF REMARK 245 SCD4 AND 3 VRC34.01 FAB REMARK 245 FRAGMENTS; HIV-1 BG505 REMARK 245 SOSIP.664; 4-DOMAIN CD4; REMARK 245 VRC34.01 FAB REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 8.00 REMARK 245 SAMPLE DETAILS : HERE ONE OF THE GP120 PROTOMER REMARK 245 IS ROTATED OUTWARD WHILE OTHER GP120 PROMOTERS MAINTAIN REMARK 245 PREFUSION ORIENTATION REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : TFS KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 (6K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 800.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2400.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : NULL REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 5910.00 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : NULL REMARK 245 CALIBRATED MAGNIFICATION : NULL REMARK 245 SOURCE : FIELD EMISSION GUN REMARK 245 ACCELERATION VOLTAGE (KV) : 300 REMARK 245 IMAGING DETAILS : NULL REMARK 247 REMARK 247 ELECTRON MICROSCOPY REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION REMARK 247 OF THE STRUCTURE FACTORS. REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: PENTADECAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J, REMARK 350 AND CHAINS: K, L, M, N, O, P, U, Z, e REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 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 ASN A 302 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 ASN A 411 REMARK 465 THR A 461 REMARK 465 ASN A 462 REMARK 465 SER A 463 REMARK 465 ASP B 57 REMARK 465 ALA B 58 REMARK 465 LYS B 59 REMARK 465 ALA B 60 REMARK 465 TYR B 61 REMARK 465 GLU B 62 REMARK 465 THR B 63 REMARK 465 GLU B 64 REMARK 465 LYS B 65 REMARK 465 HIS B 66 REMARK 465 ASN B 67 REMARK 465 VAL B 68 REMARK 465 LEU B 116 REMARK 465 LYS B 117 REMARK 465 PRO B 118 REMARK 465 CYS B 119 REMARK 465 VAL B 120 REMARK 465 LYS B 121 REMARK 465 LEU B 122 REMARK 465 THR B 123 REMARK 465 PRO B 124 REMARK 465 LEU B 125 REMARK 465 CYS B 126 REMARK 465 VAL B 127 REMARK 465 THR B 128 REMARK 465 LEU B 129 REMARK 465 GLN B 130 REMARK 465 CYS B 131 REMARK 465 THR B 132 REMARK 465 ASN B 133 REMARK 465 VAL B 134 REMARK 465 THR B 135 REMARK 465 ASN B 136 REMARK 465 ASN B 137 REMARK 465 ILE B 138 REMARK 465 THR B 139 REMARK 465 ASP B 140 REMARK 465 ASP B 141 REMARK 465 MET B 142 REMARK 465 ARG B 143 REMARK 465 GLY B 144 REMARK 465 GLU B 145 REMARK 465 LEU B 146 REMARK 465 LYS B 147 REMARK 465 ASN B 148 REMARK 465 CYS B 149 REMARK 465 SER B 150 REMARK 465 PHE B 151 REMARK 465 ASN B 152 REMARK 465 MET B 153 REMARK 465 THR B 154 REMARK 465 THR B 155 REMARK 465 GLU B 156 REMARK 465 LEU B 157 REMARK 465 ARG B 158 REMARK 465 ASP B 159 REMARK 465 LYS B 160 REMARK 465 LYS B 161 REMARK 465 GLN B 162 REMARK 465 LYS B 163 REMARK 465 VAL B 164 REMARK 465 TYR B 165 REMARK 465 SER B 166 REMARK 465 LEU B 167 REMARK 465 PHE B 168 REMARK 465 TYR B 169 REMARK 465 ARG B 170 REMARK 465 LEU B 171 REMARK 465 ASP B 172 REMARK 465 VAL B 173 REMARK 465 VAL B 174 REMARK 465 GLN B 175 REMARK 465 ILE B 176 REMARK 465 ASN B 177 REMARK 465 GLU B 178 REMARK 465 ASN B 179 REMARK 465 GLN B 180 REMARK 465 GLY B 181 REMARK 465 ASN B 182 REMARK 465 ARG B 183 REMARK 465 SER B 184 REMARK 465 ASN B 185 REMARK 465 ASN B 186 REMARK 465 SER B 187 REMARK 465 ASN B 188 REMARK 465 LYS B 189 REMARK 465 GLU B 190 REMARK 465 TYR B 191 REMARK 465 ARG B 192 REMARK 465 LEU B 193 REMARK 465 ILE B 194 REMARK 465 ASN B 195 REMARK 465 CYS B 196 REMARK 465 ASN B 197 REMARK 465 THR B 198 REMARK 465 SER B 199 REMARK 465 ALA B 200 REMARK 465 ILE B 201 REMARK 465 THR B 202 REMARK 465 GLN B 203 REMARK 465 ALA B 204 REMARK 465 CYS B 205 REMARK 465 PRO B 206 REMARK 465 ASN B 301 REMARK 465 ASN B 302 REMARK 465 ASN B 303 REMARK 465 THR B 304 REMARK 465 ARG B 305 REMARK 465 LYS B 306 REMARK 465 SER B 307 REMARK 465 ILE B 308 REMARK 465 ARG B 309 REMARK 465 ILE B 310 REMARK 465 GLY B 311 REMARK 465 PRO B 312 REMARK 465 GLY B 313 REMARK 465 GLN B 314 REMARK 465 ALA B 315 REMARK 465 PHE B 316 REMARK 465 TYR B 317 REMARK 465 ALA B 318 REMARK 465 THR B 319 REMARK 465 GLY B 320 REMARK 465 ASP B 321 REMARK 465 ILE B 322 REMARK 465 ILE B 323 REMARK 465 GLY B 324 REMARK 465 ASP B 325 REMARK 465 ILE B 326 REMARK 465 ARG B 327 REMARK 465 THR B 400 REMARK 465 SER B 401 REMARK 465 VAL B 402 REMARK 465 GLN B 403 REMARK 465 GLY B 404 REMARK 465 SER B 405 REMARK 465 ASN B 406 REMARK 465 SER B 407 REMARK 465 THR B 408 REMARK 465 GLY B 409 REMARK 465 SER B 410 REMARK 465 ASN B 411 REMARK 465 ASP B 412 REMARK 465 GLY B 458 REMARK 465 GLY B 459 REMARK 465 SER B 460 REMARK 465 ALA C 58 REMARK 465 LYS C 59 REMARK 465 ALA C 60 REMARK 465 TYR C 61 REMARK 465 GLU C 62 REMARK 465 THR C 63 REMARK 465 GLU C 64 REMARK 465 LYS C 65 REMARK 465 HIS C 66 REMARK 465 ASN C 67 REMARK 465 VAL C 68 REMARK 465 LYS C 117 REMARK 465 PRO C 118 REMARK 465 CYS C 119 REMARK 465 VAL C 120 REMARK 465 LYS C 121 REMARK 465 LEU C 122 REMARK 465 THR C 123 REMARK 465 PRO C 124 REMARK 465 LEU C 125 REMARK 465 CYS C 126 REMARK 465 VAL C 127 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 195 REMARK 465 CYS C 196 REMARK 465 ASN C 197 REMARK 465 THR C 198 REMARK 465 SER C 199 REMARK 465 ALA C 200 REMARK 465 ILE C 201 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 ASP C 325 REMARK 465 ILE C 326 REMARK 465 ARG C 327 REMARK 465 GLN C 328 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 ILE D 548 REMARK 465 VAL D 549 REMARK 465 GLN D 550 REMARK 465 GLN D 551 REMARK 465 GLN D 552 REMARK 465 SER D 553 REMARK 465 ASN D 554 REMARK 465 LEU D 555 REMARK 465 LEU D 556 REMARK 465 ARG D 557 REMARK 465 ALA D 558 REMARK 465 PRO D 559 REMARK 465 GLU D 560 REMARK 465 ALA D 561 REMARK 465 GLN D 562 REMARK 465 GLN D 563 REMARK 465 HIS D 564 REMARK 465 LEU D 565 REMARK 465 LEU D 566 REMARK 465 LYS D 567 REMARK 465 LEU D 568 REMARK 465 ILE E 548 REMARK 465 VAL E 549 REMARK 465 GLN E 550 REMARK 465 GLN E 551 REMARK 465 GLN E 552 REMARK 465 SER E 553 REMARK 465 ASN E 554 REMARK 465 LEU E 555 REMARK 465 LEU E 556 REMARK 465 ARG E 557 REMARK 465 ALA E 558 REMARK 465 PRO E 559 REMARK 465 GLU E 560 REMARK 465 ALA E 561 REMARK 465 GLN E 562 REMARK 465 GLN E 563 REMARK 465 HIS E 564 REMARK 465 LEU E 565 REMARK 465 ILE F 548 REMARK 465 VAL F 549 REMARK 465 GLN F 550 REMARK 465 GLN F 551 REMARK 465 GLN F 552 REMARK 465 SER F 553 REMARK 465 ASN F 554 REMARK 465 LEU F 555 REMARK 465 LEU F 556 REMARK 465 ARG F 557 REMARK 465 ALA F 558 REMARK 465 PRO F 559 REMARK 465 GLU F 560 REMARK 465 ALA F 561 REMARK 465 GLN F 562 REMARK 465 GLN F 563 REMARK 465 HIS F 564 REMARK 465 LEU F 565 REMARK 465 LEU F 566 REMARK 465 LEU F 663 REMARK 465 ASP F 664 REMARK 465 VAL G 111 REMARK 465 SER G 112 REMARK 465 SER G 113 REMARK 465 ALA G 114 REMARK 465 SER G 115 REMARK 465 THR G 116 REMARK 465 LYS G 117 REMARK 465 GLY G 118 REMARK 465 PRO G 119 REMARK 465 SER G 120 REMARK 465 VAL G 121 REMARK 465 PHE G 122 REMARK 465 PRO G 123 REMARK 465 LEU G 124 REMARK 465 ALA G 125 REMARK 465 PRO G 126 REMARK 465 SER G 127 REMARK 465 SER G 128 REMARK 465 LYS G 129 REMARK 465 SER G 130 REMARK 465 THR G 131 REMARK 465 SER G 132 REMARK 465 GLY G 133 REMARK 465 GLY G 134 REMARK 465 THR G 135 REMARK 465 ALA G 136 REMARK 465 ALA G 137 REMARK 465 LEU G 138 REMARK 465 GLY G 139 REMARK 465 CYS G 140 REMARK 465 LEU G 141 REMARK 465 VAL G 142 REMARK 465 LYS G 143 REMARK 465 ASP G 144 REMARK 465 TYR G 145 REMARK 465 PHE G 146 REMARK 465 PRO G 147 REMARK 465 GLU G 148 REMARK 465 PRO G 149 REMARK 465 VAL G 150 REMARK 465 THR G 151 REMARK 465 VAL G 152 REMARK 465 SER G 153 REMARK 465 TRP G 154 REMARK 465 ASN G 155 REMARK 465 SER G 156 REMARK 465 GLY G 157 REMARK 465 ALA G 158 REMARK 465 LEU G 159 REMARK 465 THR G 160 REMARK 465 SER G 161 REMARK 465 GLY G 162 REMARK 465 VAL G 163 REMARK 465 HIS G 164 REMARK 465 THR G 165 REMARK 465 PHE G 166 REMARK 465 PRO G 167 REMARK 465 ALA G 168 REMARK 465 VAL G 169 REMARK 465 LEU G 170 REMARK 465 GLN G 171 REMARK 465 SER G 172 REMARK 465 SER G 173 REMARK 465 GLY G 174 REMARK 465 LEU G 175 REMARK 465 TYR G 176 REMARK 465 SER G 177 REMARK 465 LEU G 178 REMARK 465 SER G 179 REMARK 465 SER G 180 REMARK 465 VAL G 181 REMARK 465 VAL G 182 REMARK 465 THR G 183 REMARK 465 VAL G 184 REMARK 465 PRO G 185 REMARK 465 SER G 186 REMARK 465 SER G 187 REMARK 465 SER G 188 REMARK 465 LEU G 189 REMARK 465 GLY G 190 REMARK 465 THR G 191 REMARK 465 GLN G 192 REMARK 465 THR G 193 REMARK 465 TYR G 194 REMARK 465 ILE G 195 REMARK 465 CYS G 196 REMARK 465 ASN G 197 REMARK 465 VAL G 198 REMARK 465 ASN G 199 REMARK 465 HIS G 200 REMARK 465 LYS G 201 REMARK 465 PRO G 202 REMARK 465 SER G 203 REMARK 465 ASN G 204 REMARK 465 THR G 205 REMARK 465 LYS G 206 REMARK 465 VAL G 207 REMARK 465 ASP G 208 REMARK 465 LYS G 209 REMARK 465 LYS G 210 REMARK 465 VAL G 211 REMARK 465 GLU G 212 REMARK 465 PRO G 213 REMARK 465 LYS G 214 REMARK 465 ILE H 106 REMARK 465 LYS H 107 REMARK 465 ARG H 108 REMARK 465 THR H 109 REMARK 465 VAL H 110 REMARK 465 ALA H 111 REMARK 465 ALA H 112 REMARK 465 PRO H 113 REMARK 465 SER H 114 REMARK 465 VAL H 115 REMARK 465 PHE H 116 REMARK 465 ILE H 117 REMARK 465 PHE H 118 REMARK 465 PRO H 119 REMARK 465 PRO H 120 REMARK 465 SER H 121 REMARK 465 ASP H 122 REMARK 465 GLU H 123 REMARK 465 GLN H 124 REMARK 465 LEU H 125 REMARK 465 LYS H 126 REMARK 465 SER H 127 REMARK 465 GLY H 128 REMARK 465 THR H 129 REMARK 465 ALA H 130 REMARK 465 SER H 131 REMARK 465 VAL H 132 REMARK 465 VAL H 133 REMARK 465 CYS H 134 REMARK 465 LEU H 135 REMARK 465 LEU H 136 REMARK 465 ASN H 137 REMARK 465 ASN H 138 REMARK 465 PHE H 139 REMARK 465 TYR H 140 REMARK 465 PRO H 141 REMARK 465 ARG H 142 REMARK 465 GLU H 143 REMARK 465 ALA H 144 REMARK 465 LYS H 145 REMARK 465 VAL H 146 REMARK 465 GLN H 147 REMARK 465 TRP H 148 REMARK 465 LYS H 149 REMARK 465 VAL H 150 REMARK 465 ASP H 151 REMARK 465 ASN H 152 REMARK 465 ALA H 153 REMARK 465 LEU H 154 REMARK 465 GLN H 155 REMARK 465 SER H 156 REMARK 465 GLY H 157 REMARK 465 ASN H 158 REMARK 465 SER H 159 REMARK 465 GLN H 160 REMARK 465 GLU H 161 REMARK 465 SER H 162 REMARK 465 VAL H 163 REMARK 465 THR H 164 REMARK 465 GLU H 165 REMARK 465 GLN H 166 REMARK 465 ASP H 167 REMARK 465 SER H 168 REMARK 465 LYS H 169 REMARK 465 ASP H 170 REMARK 465 SER H 171 REMARK 465 THR H 172 REMARK 465 TYR H 173 REMARK 465 SER H 174 REMARK 465 LEU H 175 REMARK 465 SER H 176 REMARK 465 SER H 177 REMARK 465 THR H 178 REMARK 465 LEU H 179 REMARK 465 THR H 180 REMARK 465 LEU H 181 REMARK 465 SER H 182 REMARK 465 LYS H 183 REMARK 465 ALA H 184 REMARK 465 ASP H 185 REMARK 465 TYR H 186 REMARK 465 GLU H 187 REMARK 465 LYS H 188 REMARK 465 HIS H 189 REMARK 465 LYS H 190 REMARK 465 VAL H 191 REMARK 465 TYR H 192 REMARK 465 ALA H 193 REMARK 465 CYS H 194 REMARK 465 GLU H 195 REMARK 465 VAL H 196 REMARK 465 THR H 197 REMARK 465 HIS H 198 REMARK 465 GLN H 199 REMARK 465 GLY H 200 REMARK 465 LEU H 201 REMARK 465 SER H 202 REMARK 465 SER H 203 REMARK 465 PRO H 204 REMARK 465 VAL H 205 REMARK 465 THR H 206 REMARK 465 LYS H 207 REMARK 465 SER H 208 REMARK 465 PHE H 209 REMARK 465 ASN H 210 REMARK 465 ARG H 211 REMARK 465 GLY H 212 REMARK 465 VAL I 111 REMARK 465 SER I 112 REMARK 465 SER I 113 REMARK 465 ALA I 114 REMARK 465 SER I 115 REMARK 465 THR I 116 REMARK 465 LYS I 117 REMARK 465 GLY I 118 REMARK 465 PRO I 119 REMARK 465 SER I 120 REMARK 465 VAL I 121 REMARK 465 PHE I 122 REMARK 465 PRO I 123 REMARK 465 LEU I 124 REMARK 465 ALA I 125 REMARK 465 PRO I 126 REMARK 465 SER I 127 REMARK 465 SER I 128 REMARK 465 LYS I 129 REMARK 465 SER I 130 REMARK 465 THR I 131 REMARK 465 SER I 132 REMARK 465 GLY I 133 REMARK 465 GLY I 134 REMARK 465 THR I 135 REMARK 465 ALA I 136 REMARK 465 ALA I 137 REMARK 465 LEU I 138 REMARK 465 GLY I 139 REMARK 465 CYS I 140 REMARK 465 LEU I 141 REMARK 465 VAL I 142 REMARK 465 LYS I 143 REMARK 465 ASP I 144 REMARK 465 TYR I 145 REMARK 465 PHE I 146 REMARK 465 PRO I 147 REMARK 465 GLU I 148 REMARK 465 PRO I 149 REMARK 465 VAL I 150 REMARK 465 THR I 151 REMARK 465 VAL I 152 REMARK 465 SER I 153 REMARK 465 TRP I 154 REMARK 465 ASN I 155 REMARK 465 SER I 156 REMARK 465 GLY I 157 REMARK 465 ALA I 158 REMARK 465 LEU I 159 REMARK 465 THR I 160 REMARK 465 SER I 161 REMARK 465 GLY I 162 REMARK 465 VAL I 163 REMARK 465 HIS I 164 REMARK 465 THR I 165 REMARK 465 PHE I 166 REMARK 465 PRO I 167 REMARK 465 ALA I 168 REMARK 465 VAL I 169 REMARK 465 LEU I 170 REMARK 465 GLN I 171 REMARK 465 SER I 172 REMARK 465 SER I 173 REMARK 465 GLY I 174 REMARK 465 LEU I 175 REMARK 465 TYR I 176 REMARK 465 SER I 177 REMARK 465 LEU I 178 REMARK 465 SER I 179 REMARK 465 SER I 180 REMARK 465 VAL I 181 REMARK 465 VAL I 182 REMARK 465 THR I 183 REMARK 465 VAL I 184 REMARK 465 PRO I 185 REMARK 465 SER I 186 REMARK 465 SER I 187 REMARK 465 SER I 188 REMARK 465 LEU I 189 REMARK 465 GLY I 190 REMARK 465 THR I 191 REMARK 465 GLN I 192 REMARK 465 THR I 193 REMARK 465 TYR I 194 REMARK 465 ILE I 195 REMARK 465 CYS I 196 REMARK 465 ASN I 197 REMARK 465 VAL I 198 REMARK 465 ASN I 199 REMARK 465 HIS I 200 REMARK 465 LYS I 201 REMARK 465 PRO I 202 REMARK 465 SER I 203 REMARK 465 ASN I 204 REMARK 465 THR I 205 REMARK 465 LYS I 206 REMARK 465 VAL I 207 REMARK 465 ASP I 208 REMARK 465 LYS I 209 REMARK 465 LYS I 210 REMARK 465 VAL I 211 REMARK 465 GLU I 212 REMARK 465 PRO I 213 REMARK 465 LYS I 214 REMARK 465 ILE J 106 REMARK 465 LYS J 107 REMARK 465 ARG J 108 REMARK 465 THR J 109 REMARK 465 VAL J 110 REMARK 465 ALA J 111 REMARK 465 ALA J 112 REMARK 465 PRO J 113 REMARK 465 SER J 114 REMARK 465 VAL J 115 REMARK 465 PHE J 116 REMARK 465 ILE J 117 REMARK 465 PHE J 118 REMARK 465 PRO J 119 REMARK 465 PRO J 120 REMARK 465 SER J 121 REMARK 465 ASP J 122 REMARK 465 GLU J 123 REMARK 465 GLN J 124 REMARK 465 LEU J 125 REMARK 465 LYS J 126 REMARK 465 SER J 127 REMARK 465 GLY J 128 REMARK 465 THR J 129 REMARK 465 ALA J 130 REMARK 465 SER J 131 REMARK 465 VAL J 132 REMARK 465 VAL J 133 REMARK 465 CYS J 134 REMARK 465 LEU J 135 REMARK 465 LEU J 136 REMARK 465 ASN J 137 REMARK 465 ASN J 138 REMARK 465 PHE J 139 REMARK 465 TYR J 140 REMARK 465 PRO J 141 REMARK 465 ARG J 142 REMARK 465 GLU J 143 REMARK 465 ALA J 144 REMARK 465 LYS J 145 REMARK 465 VAL J 146 REMARK 465 GLN J 147 REMARK 465 TRP J 148 REMARK 465 LYS J 149 REMARK 465 VAL J 150 REMARK 465 ASP J 151 REMARK 465 ASN J 152 REMARK 465 ALA J 153 REMARK 465 LEU J 154 REMARK 465 GLN J 155 REMARK 465 SER J 156 REMARK 465 GLY J 157 REMARK 465 ASN J 158 REMARK 465 SER J 159 REMARK 465 GLN J 160 REMARK 465 GLU J 161 REMARK 465 SER J 162 REMARK 465 VAL J 163 REMARK 465 THR J 164 REMARK 465 GLU J 165 REMARK 465 GLN J 166 REMARK 465 ASP J 167 REMARK 465 SER J 168 REMARK 465 LYS J 169 REMARK 465 ASP J 170 REMARK 465 SER J 171 REMARK 465 THR J 172 REMARK 465 TYR J 173 REMARK 465 SER J 174 REMARK 465 LEU J 175 REMARK 465 SER J 176 REMARK 465 SER J 177 REMARK 465 THR J 178 REMARK 465 LEU J 179 REMARK 465 THR J 180 REMARK 465 LEU J 181 REMARK 465 SER J 182 REMARK 465 LYS J 183 REMARK 465 ALA J 184 REMARK 465 ASP J 185 REMARK 465 TYR J 186 REMARK 465 GLU J 187 REMARK 465 LYS J 188 REMARK 465 HIS J 189 REMARK 465 LYS J 190 REMARK 465 VAL J 191 REMARK 465 TYR J 192 REMARK 465 ALA J 193 REMARK 465 CYS J 194 REMARK 465 GLU J 195 REMARK 465 VAL J 196 REMARK 465 THR J 197 REMARK 465 HIS J 198 REMARK 465 GLN J 199 REMARK 465 GLY J 200 REMARK 465 LEU J 201 REMARK 465 SER J 202 REMARK 465 SER J 203 REMARK 465 PRO J 204 REMARK 465 VAL J 205 REMARK 465 THR J 206 REMARK 465 LYS J 207 REMARK 465 SER J 208 REMARK 465 PHE J 209 REMARK 465 ASN J 210 REMARK 465 ARG J 211 REMARK 465 GLY J 212 REMARK 465 VAL K 111 REMARK 465 SER K 112 REMARK 465 SER K 113 REMARK 465 ALA K 114 REMARK 465 SER K 115 REMARK 465 THR K 116 REMARK 465 LYS K 117 REMARK 465 GLY K 118 REMARK 465 PRO K 119 REMARK 465 SER K 120 REMARK 465 VAL K 121 REMARK 465 PHE K 122 REMARK 465 PRO K 123 REMARK 465 LEU K 124 REMARK 465 ALA K 125 REMARK 465 PRO K 126 REMARK 465 SER K 127 REMARK 465 SER K 128 REMARK 465 LYS K 129 REMARK 465 SER K 130 REMARK 465 THR K 131 REMARK 465 SER K 132 REMARK 465 GLY K 133 REMARK 465 GLY K 134 REMARK 465 THR K 135 REMARK 465 ALA K 136 REMARK 465 ALA K 137 REMARK 465 LEU K 138 REMARK 465 GLY K 139 REMARK 465 CYS K 140 REMARK 465 LEU K 141 REMARK 465 VAL K 142 REMARK 465 LYS K 143 REMARK 465 ASP K 144 REMARK 465 TYR K 145 REMARK 465 PHE K 146 REMARK 465 PRO K 147 REMARK 465 GLU K 148 REMARK 465 PRO K 149 REMARK 465 VAL K 150 REMARK 465 THR K 151 REMARK 465 VAL K 152 REMARK 465 SER K 153 REMARK 465 TRP K 154 REMARK 465 ASN K 155 REMARK 465 SER K 156 REMARK 465 GLY K 157 REMARK 465 ALA K 158 REMARK 465 LEU K 159 REMARK 465 THR K 160 REMARK 465 SER K 161 REMARK 465 GLY K 162 REMARK 465 VAL K 163 REMARK 465 HIS K 164 REMARK 465 THR K 165 REMARK 465 PHE K 166 REMARK 465 PRO K 167 REMARK 465 ALA K 168 REMARK 465 VAL K 169 REMARK 465 LEU K 170 REMARK 465 GLN K 171 REMARK 465 SER K 172 REMARK 465 SER K 173 REMARK 465 GLY K 174 REMARK 465 LEU K 175 REMARK 465 TYR K 176 REMARK 465 SER K 177 REMARK 465 LEU K 178 REMARK 465 SER K 179 REMARK 465 SER K 180 REMARK 465 VAL K 181 REMARK 465 VAL K 182 REMARK 465 THR K 183 REMARK 465 VAL K 184 REMARK 465 PRO K 185 REMARK 465 SER K 186 REMARK 465 SER K 187 REMARK 465 SER K 188 REMARK 465 LEU K 189 REMARK 465 GLY K 190 REMARK 465 THR K 191 REMARK 465 GLN K 192 REMARK 465 THR K 193 REMARK 465 TYR K 194 REMARK 465 ILE K 195 REMARK 465 CYS K 196 REMARK 465 ASN K 197 REMARK 465 VAL K 198 REMARK 465 ASN K 199 REMARK 465 HIS K 200 REMARK 465 LYS K 201 REMARK 465 PRO K 202 REMARK 465 SER K 203 REMARK 465 ASN K 204 REMARK 465 THR K 205 REMARK 465 LYS K 206 REMARK 465 VAL K 207 REMARK 465 ASP K 208 REMARK 465 LYS K 209 REMARK 465 LYS K 210 REMARK 465 VAL K 211 REMARK 465 GLU K 212 REMARK 465 PRO K 213 REMARK 465 LYS K 214 REMARK 465 ILE L 106 REMARK 465 LYS L 107 REMARK 465 ARG L 108 REMARK 465 THR L 109 REMARK 465 VAL L 110 REMARK 465 ALA L 111 REMARK 465 ALA L 112 REMARK 465 PRO L 113 REMARK 465 SER L 114 REMARK 465 VAL L 115 REMARK 465 PHE L 116 REMARK 465 ILE L 117 REMARK 465 PHE L 118 REMARK 465 PRO L 119 REMARK 465 PRO L 120 REMARK 465 SER L 121 REMARK 465 ASP L 122 REMARK 465 GLU L 123 REMARK 465 GLN L 124 REMARK 465 LEU L 125 REMARK 465 LYS L 126 REMARK 465 SER L 127 REMARK 465 GLY L 128 REMARK 465 THR L 129 REMARK 465 ALA L 130 REMARK 465 SER L 131 REMARK 465 VAL L 132 REMARK 465 VAL L 133 REMARK 465 CYS L 134 REMARK 465 LEU L 135 REMARK 465 LEU L 136 REMARK 465 ASN L 137 REMARK 465 ASN L 138 REMARK 465 PHE L 139 REMARK 465 TYR L 140 REMARK 465 PRO L 141 REMARK 465 ARG L 142 REMARK 465 GLU L 143 REMARK 465 ALA L 144 REMARK 465 LYS L 145 REMARK 465 VAL L 146 REMARK 465 GLN L 147 REMARK 465 TRP L 148 REMARK 465 LYS L 149 REMARK 465 VAL L 150 REMARK 465 ASP L 151 REMARK 465 ASN L 152 REMARK 465 ALA L 153 REMARK 465 LEU L 154 REMARK 465 GLN L 155 REMARK 465 SER L 156 REMARK 465 GLY L 157 REMARK 465 ASN L 158 REMARK 465 SER L 159 REMARK 465 GLN L 160 REMARK 465 GLU L 161 REMARK 465 SER L 162 REMARK 465 VAL L 163 REMARK 465 THR L 164 REMARK 465 GLU L 165 REMARK 465 GLN L 166 REMARK 465 ASP L 167 REMARK 465 SER L 168 REMARK 465 LYS L 169 REMARK 465 ASP L 170 REMARK 465 SER L 171 REMARK 465 THR L 172 REMARK 465 TYR L 173 REMARK 465 SER L 174 REMARK 465 LEU L 175 REMARK 465 SER L 176 REMARK 465 SER L 177 REMARK 465 THR L 178 REMARK 465 LEU L 179 REMARK 465 THR L 180 REMARK 465 LEU L 181 REMARK 465 SER L 182 REMARK 465 LYS L 183 REMARK 465 ALA L 184 REMARK 465 ASP L 185 REMARK 465 TYR L 186 REMARK 465 GLU L 187 REMARK 465 LYS L 188 REMARK 465 HIS L 189 REMARK 465 LYS L 190 REMARK 465 VAL L 191 REMARK 465 TYR L 192 REMARK 465 ALA L 193 REMARK 465 CYS L 194 REMARK 465 GLU L 195 REMARK 465 VAL L 196 REMARK 465 THR L 197 REMARK 465 HIS L 198 REMARK 465 GLN L 199 REMARK 465 GLY L 200 REMARK 465 LEU L 201 REMARK 465 SER L 202 REMARK 465 SER L 203 REMARK 465 PRO L 204 REMARK 465 VAL L 205 REMARK 465 THR L 206 REMARK 465 LYS L 207 REMARK 465 SER L 208 REMARK 465 PHE L 209 REMARK 465 ASN L 210 REMARK 465 ARG L 211 REMARK 465 GLY L 212 REMARK 465 LEU N 96 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 GLU A 49 CG CD OE1 OE2 REMARK 470 ASP A 57 CG OD1 OD2 REMARK 470 GLU A 87 CG CD OE1 OE2 REMARK 470 LYS A 97 CG CD CE NZ REMARK 470 LYS A 117 CG CD CE NZ REMARK 470 ARG A 192 CG CD NE CZ NH1 NH2 REMARK 470 LEU A 193 CG CD1 CD2 REMARK 470 GLN A 203 CG CD OE1 NE2 REMARK 470 VAL A 208 CG1 CG2 REMARK 470 GLU A 211 CG CD OE1 OE2 REMARK 470 LYS A 231 CG CD CE NZ REMARK 470 LYS A 232 CG CD CE NZ REMARK 470 GLU A 267 CG CD OE1 OE2 REMARK 470 GLU A 268 CG CD OE1 OE2 REMARK 470 GLU A 269 CG CD OE1 OE2 REMARK 470 GLU A 275 CG CD OE1 OE2 REMARK 470 ILE A 358 CG1 CG2 CD1 REMARK 470 GLU A 370 CG CD OE1 OE2 REMARK 470 GLU A 381 CG CD OE1 OE2 REMARK 470 ILE A 396 CG1 CG2 CD1 REMARK 470 GLN A 440 CG CD OE1 NE2 REMARK 470 ASP A 457 CG OD1 OD2 REMARK 470 THR A 465 CG2 REMARK 470 GLU A 466 CD OE1 OE2 REMARK 470 THR A 467 OG1 CG2 REMARK 470 ASP A 474 CG OD1 OD2 REMARK 470 LYS A 502 CG CD CE NZ REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 CYS A 247 CA - CB - SG ANGL. DEV. = 10.9 DEGREES REMARK 500 CYS A 501 CA - CB - SG ANGL. DEV. = 6.7 DEGREES REMARK 500 ALA B 219 C - N - CA ANGL. DEV. = 19.6 DEGREES REMARK 500 CYS B 247 CA - CB - SG ANGL. DEV. = 9.2 DEGREES REMARK 500 CYS L 23 CA - CB - SG ANGL. DEV. = 7.8 DEGREES REMARK 500 ASP M 56 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES REMARK 500 LEU M 61 CA - CB - CG ANGL. DEV. = 13.9 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 LYS A 65 -4.22 77.04 REMARK 500 CYS A 126 64.76 60.58 REMARK 500 GLN A 258 -10.70 74.84 REMARK 500 PRO A 493 54.15 -90.94 REMARK 500 ALA B 73 52.06 -91.04 REMARK 500 GLN B 258 -67.50 60.75 REMARK 500 GLU B 268 -101.94 55.23 REMARK 500 ASN C 88 -130.97 57.23 REMARK 500 GLN C 258 -64.78 61.09 REMARK 500 GLU C 268 -129.84 58.13 REMARK 500 SER C 375 66.86 -101.94 REMARK 500 GLN C 428 -168.09 -115.38 REMARK 500 ARG C 429 -130.34 61.00 REMARK 500 GLN C 440 170.92 64.39 REMARK 500 SER D 546 -100.88 53.75 REMARK 500 SER D 599 -8.18 64.64 REMARK 500 LEU D 602 -14.04 72.75 REMARK 500 ALA E 525 51.83 -92.80 REMARK 500 MET E 530 -133.30 52.41 REMARK 500 THR E 536 54.54 -91.65 REMARK 500 SER E 599 -13.10 69.00 REMARK 500 LEU E 602 -19.07 73.36 REMARK 500 SER F 546 -138.17 60.41 REMARK 500 TRP F 571 -123.91 56.68 REMARK 500 SER F 599 -8.77 64.85 REMARK 500 LEU F 602 -20.40 73.76 REMARK 500 ASN F 656 -2.40 69.66 REMARK 500 HIS G 53 -61.02 -91.09 REMARK 500 TYR G 97 69.62 60.64 REMARK 500 VAL G 100C -52.51 -125.71 REMARK 500 ARG H 30 -138.92 62.40 REMARK 500 ALA H 51 -5.27 66.49 REMARK 500 SER H 52 -14.11 -140.29 REMARK 500 ARG J 30 -133.88 61.77 REMARK 500 ALA J 51 -3.78 64.84 REMARK 500 SER J 52 -14.31 -140.83 REMARK 500 LEU K 48 -60.97 -95.57 REMARK 500 TYR K 97 61.32 61.94 REMARK 500 VAL K 100C -50.77 -122.31 REMARK 500 ARG L 30 -137.88 60.57 REMARK 500 ALA L 51 -5.58 66.87 REMARK 500 SER L 52 -14.71 -140.33 REMARK 500 MET L 91 21.75 -140.44 REMARK 500 ASN M 32 49.77 -95.03 REMARK 500 ILE M 36 -64.67 -93.87 REMARK 500 GLN N 33 24.61 49.99 REMARK 500 ILE N 36 -61.44 -103.24 REMARK 500 LEU N 51 30.55 -95.55 REMARK 500 LYS N 75 -169.63 -118.93 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 TRP D 596 GLY D 597 -140.16 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-46653 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF HIV-1 BG505 SOSIP.664 ENV BOUND TO 3-SCD4, 3- REMARK 900 VRC34.01 FAB WITH ONE GP120 ROTATED DBREF 9D8Y A 33 503 UNP Q2N0S5 Q2N0S5_HV1 32 500 DBREF 9D8Y B 33 503 UNP Q2N0S5 Q2N0S5_HV1 32 500 DBREF 9D8Y C 33 503 UNP Q2N0S5 Q2N0S5_HV1 32 500 DBREF 9D8Y D 512 664 UNP Q2N0S6 Q2N0S6_9HIV1 509 661 DBREF 9D8Y E 512 664 UNP Q2N0S6 Q2N0S6_9HIV1 509 661 DBREF 9D8Y F 512 664 UNP Q2N0S6 Q2N0S6_9HIV1 509 661 DBREF 9D8Y G 1 214 PDB 9D8Y 9D8Y 1 214 DBREF 9D8Y H 1 212 PDB 9D8Y 9D8Y 1 212 DBREF 9D8Y I 1 214 PDB 9D8Y 9D8Y 1 214 DBREF 9D8Y J 1 212 PDB 9D8Y 9D8Y 1 212 DBREF 9D8Y K 1 214 PDB 9D8Y 9D8Y 1 214 DBREF 9D8Y L 1 212 PDB 9D8Y 9D8Y 1 212 DBREF 9D8Y M 1 96 UNP P01730 CD4_HUMAN 26 121 DBREF 9D8Y N 1 96 UNP P01730 CD4_HUMAN 26 121 DBREF 9D8Y O 1 96 UNP P01730 CD4_HUMAN 26 121 SEQADV 9D8Y ASN A 332 UNP Q2N0S5 THR 330 ENGINEERED MUTATION SEQADV 9D8Y CYS A 501 UNP Q2N0S5 ALA 498 ENGINEERED MUTATION SEQADV 9D8Y ASN B 332 UNP Q2N0S5 THR 330 ENGINEERED MUTATION SEQADV 9D8Y CYS B 501 UNP Q2N0S5 ALA 498 ENGINEERED MUTATION SEQADV 9D8Y ASN C 332 UNP Q2N0S5 THR 330 ENGINEERED MUTATION SEQADV 9D8Y CYS C 501 UNP Q2N0S5 ALA 498 ENGINEERED MUTATION SEQADV 9D8Y PRO D 559 UNP Q2N0S6 ILE 556 ENGINEERED MUTATION SEQADV 9D8Y CYS D 605 UNP Q2N0S6 THR 602 ENGINEERED MUTATION SEQADV 9D8Y PRO E 559 UNP Q2N0S6 ILE 556 ENGINEERED MUTATION SEQADV 9D8Y CYS E 605 UNP Q2N0S6 THR 602 ENGINEERED MUTATION SEQADV 9D8Y PRO F 559 UNP Q2N0S6 ILE 556 ENGINEERED MUTATION SEQADV 9D8Y CYS F 605 UNP Q2N0S6 THR 602 ENGINEERED MUTATION SEQRES 1 A 469 ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO VAL TRP SEQRES 2 A 469 LYS ASP ALA GLU THR THR LEU PHE CYS ALA SER ASP ALA SEQRES 3 A 469 LYS ALA TYR GLU THR GLU LYS HIS ASN VAL TRP ALA THR SEQRES 4 A 469 HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN GLU ILE SEQRES 5 A 469 HIS LEU GLU ASN VAL THR GLU GLU PHE ASN MET TRP LYS SEQRES 6 A 469 ASN ASN MET VAL GLU GLN MET HIS THR ASP ILE ILE SER SEQRES 7 A 469 LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS LEU THR SEQRES 8 A 469 PRO LEU CYS VAL THR LEU GLN CYS THR ASN VAL THR ASN SEQRES 9 A 469 ASN ILE THR ASP ASP MET ARG GLY GLU LEU LYS ASN CYS SEQRES 10 A 469 SER PHE ASN MET THR THR GLU LEU ARG ASP LYS LYS GLN SEQRES 11 A 469 LYS VAL TYR SER LEU PHE TYR ARG LEU ASP VAL VAL GLN SEQRES 12 A 469 ILE ASN GLU ASN GLN GLY ASN ARG SER ASN ASN SER ASN SEQRES 13 A 469 LYS GLU TYR ARG LEU ILE ASN CYS ASN THR SER ALA ILE SEQRES 14 A 469 THR GLN ALA CYS PRO LYS VAL SER PHE GLU PRO ILE PRO SEQRES 15 A 469 ILE HIS TYR CYS ALA PRO ALA GLY PHE ALA ILE LEU LYS SEQRES 16 A 469 CYS LYS ASP LYS LYS PHE ASN GLY THR GLY PRO CYS PRO SEQRES 17 A 469 SER VAL SER THR VAL GLN CYS THR HIS GLY ILE LYS PRO SEQRES 18 A 469 VAL VAL SER THR GLN LEU LEU LEU ASN GLY SER LEU ALA SEQRES 19 A 469 GLU GLU GLU VAL MET ILE ARG SER GLU ASN ILE THR ASN SEQRES 20 A 469 ASN ALA LYS ASN ILE LEU VAL GLN PHE ASN THR PRO VAL SEQRES 21 A 469 GLN ILE ASN CYS THR ARG PRO ASN ASN ASN THR ARG LYS SEQRES 22 A 469 SER ILE ARG ILE GLY PRO GLY GLN ALA PHE TYR ALA THR SEQRES 23 A 469 GLY ASP ILE ILE GLY ASP ILE ARG GLN ALA HIS CYS ASN SEQRES 24 A 469 VAL SER LYS ALA THR TRP ASN GLU THR LEU GLY LYS VAL SEQRES 25 A 469 VAL LYS GLN LEU ARG LYS HIS PHE GLY ASN ASN THR ILE SEQRES 26 A 469 ILE ARG PHE ALA ASN SER SER GLY GLY ASP LEU GLU VAL SEQRES 27 A 469 THR THR HIS SER PHE ASN CYS GLY GLY GLU PHE PHE TYR SEQRES 28 A 469 CYS ASN THR SER GLY LEU PHE ASN SER THR TRP ILE SER SEQRES 29 A 469 ASN THR SER VAL GLN GLY SER ASN SER THR GLY SER ASN SEQRES 30 A 469 ASP SER ILE THR LEU PRO CYS ARG ILE LYS GLN ILE ILE SEQRES 31 A 469 ASN MET TRP GLN ARG ILE GLY GLN ALA MET TYR ALA PRO SEQRES 32 A 469 PRO ILE GLN GLY VAL ILE ARG CYS VAL SER ASN ILE THR SEQRES 33 A 469 GLY LEU ILE LEU THR ARG ASP GLY GLY SER THR ASN SER SEQRES 34 A 469 THR THR GLU THR PHE ARG PRO GLY GLY GLY ASP MET ARG SEQRES 35 A 469 ASP ASN TRP ARG SER GLU LEU TYR LYS TYR LYS VAL VAL SEQRES 36 A 469 LYS ILE GLU PRO LEU GLY VAL ALA PRO THR ARG CYS LYS SEQRES 37 A 469 ARG SEQRES 1 B 469 ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO VAL TRP SEQRES 2 B 469 LYS ASP ALA GLU THR THR LEU PHE CYS ALA SER ASP ALA SEQRES 3 B 469 LYS ALA TYR GLU THR GLU LYS HIS ASN VAL TRP ALA THR SEQRES 4 B 469 HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN GLU ILE SEQRES 5 B 469 HIS LEU GLU ASN VAL THR GLU GLU PHE ASN MET TRP LYS SEQRES 6 B 469 ASN ASN MET VAL GLU GLN MET HIS THR ASP ILE ILE SER SEQRES 7 B 469 LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS LEU THR SEQRES 8 B 469 PRO LEU CYS VAL THR LEU GLN CYS THR ASN VAL THR ASN SEQRES 9 B 469 ASN ILE THR ASP ASP MET ARG GLY GLU LEU LYS ASN CYS SEQRES 10 B 469 SER PHE ASN MET THR THR GLU LEU ARG ASP LYS LYS GLN SEQRES 11 B 469 LYS VAL TYR SER LEU PHE TYR ARG LEU ASP VAL VAL GLN SEQRES 12 B 469 ILE ASN GLU ASN GLN GLY ASN ARG SER ASN ASN SER ASN SEQRES 13 B 469 LYS GLU TYR ARG LEU ILE ASN CYS ASN THR SER ALA ILE SEQRES 14 B 469 THR GLN ALA CYS PRO LYS VAL SER PHE GLU PRO ILE PRO SEQRES 15 B 469 ILE HIS TYR CYS ALA PRO ALA GLY PHE ALA ILE LEU LYS SEQRES 16 B 469 CYS LYS ASP LYS LYS PHE ASN GLY THR GLY PRO CYS PRO SEQRES 17 B 469 SER VAL SER THR VAL GLN CYS THR HIS GLY ILE LYS PRO SEQRES 18 B 469 VAL VAL SER THR GLN LEU LEU LEU ASN GLY SER LEU ALA SEQRES 19 B 469 GLU GLU GLU VAL MET ILE ARG SER GLU ASN ILE THR ASN SEQRES 20 B 469 ASN ALA LYS ASN ILE LEU VAL GLN PHE ASN THR PRO VAL SEQRES 21 B 469 GLN ILE ASN CYS THR ARG PRO ASN ASN ASN THR ARG LYS SEQRES 22 B 469 SER ILE ARG ILE GLY PRO GLY GLN ALA PHE TYR ALA THR SEQRES 23 B 469 GLY ASP ILE ILE GLY ASP ILE ARG GLN ALA HIS CYS ASN SEQRES 24 B 469 VAL SER LYS ALA THR TRP ASN GLU THR LEU GLY LYS VAL SEQRES 25 B 469 VAL LYS GLN LEU ARG LYS HIS PHE GLY ASN ASN THR ILE SEQRES 26 B 469 ILE ARG PHE ALA ASN SER SER GLY GLY ASP LEU GLU VAL SEQRES 27 B 469 THR THR HIS SER PHE ASN CYS GLY GLY GLU PHE PHE TYR SEQRES 28 B 469 CYS ASN THR SER GLY LEU PHE ASN SER THR TRP ILE SER SEQRES 29 B 469 ASN THR SER VAL GLN GLY SER ASN SER THR GLY SER ASN SEQRES 30 B 469 ASP SER ILE THR LEU PRO CYS ARG ILE LYS GLN ILE ILE SEQRES 31 B 469 ASN MET TRP GLN ARG ILE GLY GLN ALA MET TYR ALA PRO SEQRES 32 B 469 PRO ILE GLN GLY VAL ILE ARG CYS VAL SER ASN ILE THR SEQRES 33 B 469 GLY LEU ILE LEU THR ARG ASP GLY GLY SER THR ASN SER SEQRES 34 B 469 THR THR GLU THR PHE ARG PRO GLY GLY GLY ASP MET ARG SEQRES 35 B 469 ASP ASN TRP ARG SER GLU LEU TYR LYS TYR LYS VAL VAL SEQRES 36 B 469 LYS ILE GLU PRO LEU GLY VAL ALA PRO THR ARG CYS LYS SEQRES 37 B 469 ARG SEQRES 1 C 469 ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO VAL TRP SEQRES 2 C 469 LYS ASP ALA GLU THR THR LEU PHE CYS ALA SER ASP ALA SEQRES 3 C 469 LYS ALA TYR GLU THR GLU LYS HIS ASN VAL TRP ALA THR SEQRES 4 C 469 HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN GLU ILE SEQRES 5 C 469 HIS LEU GLU ASN VAL THR GLU GLU PHE ASN MET TRP LYS SEQRES 6 C 469 ASN ASN MET VAL GLU GLN MET HIS THR ASP ILE ILE SER SEQRES 7 C 469 LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS LEU THR SEQRES 8 C 469 PRO LEU CYS VAL THR LEU GLN CYS THR ASN VAL THR ASN SEQRES 9 C 469 ASN ILE THR ASP ASP MET ARG GLY GLU LEU LYS ASN CYS SEQRES 10 C 469 SER PHE ASN MET THR THR GLU LEU ARG ASP LYS LYS GLN SEQRES 11 C 469 LYS VAL TYR SER LEU PHE TYR ARG LEU ASP VAL VAL GLN SEQRES 12 C 469 ILE ASN GLU ASN GLN GLY ASN ARG SER ASN ASN SER ASN SEQRES 13 C 469 LYS GLU TYR ARG LEU ILE ASN CYS ASN THR SER ALA ILE SEQRES 14 C 469 THR GLN ALA CYS PRO LYS VAL SER PHE GLU PRO ILE PRO SEQRES 15 C 469 ILE HIS TYR CYS ALA PRO ALA GLY PHE ALA ILE LEU LYS SEQRES 16 C 469 CYS LYS ASP LYS LYS PHE ASN GLY THR GLY PRO CYS PRO SEQRES 17 C 469 SER VAL SER THR VAL GLN CYS THR HIS GLY ILE LYS PRO SEQRES 18 C 469 VAL VAL SER THR GLN LEU LEU LEU ASN GLY SER LEU ALA SEQRES 19 C 469 GLU GLU GLU VAL MET ILE ARG SER GLU ASN ILE THR ASN SEQRES 20 C 469 ASN ALA LYS ASN ILE LEU VAL GLN PHE ASN THR PRO VAL SEQRES 21 C 469 GLN ILE ASN CYS THR ARG PRO ASN ASN ASN THR ARG LYS SEQRES 22 C 469 SER ILE ARG ILE GLY PRO GLY GLN ALA PHE TYR ALA THR SEQRES 23 C 469 GLY ASP ILE ILE GLY ASP ILE ARG GLN ALA HIS CYS ASN SEQRES 24 C 469 VAL SER LYS ALA THR TRP ASN GLU THR LEU GLY LYS VAL SEQRES 25 C 469 VAL LYS GLN LEU ARG LYS HIS PHE GLY ASN ASN THR ILE SEQRES 26 C 469 ILE ARG PHE ALA ASN SER SER GLY GLY ASP LEU GLU VAL SEQRES 27 C 469 THR THR HIS SER PHE ASN CYS GLY GLY GLU PHE PHE TYR SEQRES 28 C 469 CYS ASN THR SER GLY LEU PHE ASN SER THR TRP ILE SER SEQRES 29 C 469 ASN THR SER VAL GLN GLY SER ASN SER THR GLY SER ASN SEQRES 30 C 469 ASP SER ILE THR LEU PRO CYS ARG ILE LYS GLN ILE ILE SEQRES 31 C 469 ASN MET TRP GLN ARG ILE GLY GLN ALA MET TYR ALA PRO SEQRES 32 C 469 PRO ILE GLN GLY VAL ILE ARG CYS VAL SER ASN ILE THR SEQRES 33 C 469 GLY LEU ILE LEU THR ARG ASP GLY GLY SER THR ASN SER SEQRES 34 C 469 THR THR GLU THR PHE ARG PRO GLY GLY GLY ASP MET ARG SEQRES 35 C 469 ASP ASN TRP ARG SER GLU LEU TYR LYS TYR LYS VAL VAL SEQRES 36 C 469 LYS ILE GLU PRO LEU GLY VAL ALA PRO THR ARG CYS LYS SEQRES 37 C 469 ARG SEQRES 1 D 153 ALA VAL GLY ILE GLY ALA VAL PHE LEU GLY PHE LEU GLY SEQRES 2 D 153 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 D 153 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 D 153 GLN GLN SER ASN LEU LEU ARG ALA PRO GLU ALA GLN GLN SEQRES 5 D 153 HIS LEU LEU LYS LEU THR VAL TRP GLY ILE LYS GLN LEU SEQRES 6 D 153 GLN ALA ARG VAL LEU ALA VAL GLU ARG TYR LEU ARG ASP SEQRES 7 D 153 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 D 153 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 D 153 ASN ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 D 153 LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE SEQRES 11 D 153 ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 D 153 LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP SEQRES 1 E 153 ALA VAL GLY ILE GLY ALA VAL PHE LEU GLY PHE LEU GLY SEQRES 2 E 153 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 E 153 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 E 153 GLN GLN SER ASN LEU LEU ARG ALA PRO GLU ALA GLN GLN SEQRES 5 E 153 HIS LEU LEU LYS LEU THR VAL TRP GLY ILE LYS GLN LEU SEQRES 6 E 153 GLN ALA ARG VAL LEU ALA VAL GLU ARG TYR LEU ARG ASP SEQRES 7 E 153 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 E 153 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 E 153 ASN ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 E 153 LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE SEQRES 11 E 153 ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 E 153 LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP 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 223 GLN GLU VAL LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 G 223 PRO GLY ALA SER VAL LYS VAL SER CYS ARG ALA PHE GLY SEQRES 3 G 223 TYR THR PHE THR GLY ASN ALA LEU HIS TRP VAL ARG GLN SEQRES 4 G 223 ALA PRO GLY GLN GLY LEU GLU TRP LEU GLY TRP ILE ASN SEQRES 5 G 223 PRO HIS SER GLY ASP THR THR THR SER GLN LYS PHE GLN SEQRES 6 G 223 GLY ARG VAL TYR MET THR ARG ASP LYS SER ILE ASN THR SEQRES 7 G 223 ALA PHE LEU ASP VAL THR ARG LEU THR SER ASP ASP THR SEQRES 8 G 223 GLY ILE TYR TYR CYS ALA ARG ASP LYS TYR TYR GLY ASN SEQRES 9 G 223 GLU ALA VAL GLY MET ASP VAL TRP GLY GLN GLY THR SER SEQRES 10 G 223 VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL SEQRES 11 G 223 PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY SEQRES 12 G 223 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO SEQRES 13 G 223 GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SEQRES 14 G 223 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER SEQRES 15 G 223 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SEQRES 16 G 223 SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN SEQRES 17 G 223 HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU SEQRES 18 G 223 PRO LYS SEQRES 1 H 212 ASP ILE GLN LEU THR GLN SER PRO SER PHE LEU SER ALA SEQRES 2 H 212 SER VAL GLY ASP LYS VAL THR ILE THR CYS ARG ALA SER SEQRES 3 H 212 GLN GLY VAL ARG ASN GLU LEU ALA TRP TYR GLN GLN LYS SEQRES 4 H 212 PRO GLY LYS ALA PRO ASN LEU LEU ILE TYR TYR ALA SER SEQRES 5 H 212 THR LEU GLN SER GLY VAL PRO SER ARG PHE SER ALA THR SEQRES 6 H 212 GLY SER GLY THR HIS PHE THR LEU THR VAL SER SER LEU SEQRES 7 H 212 GLN PRO GLU ASP PHE ALA THR TYR PHE CYS GLN HIS MET SEQRES 8 H 212 SER SER TYR PRO LEU THR PHE GLY GLY GLY THR LYS VAL SEQRES 9 H 212 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 H 212 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 H 212 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 H 212 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 H 212 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 H 212 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 H 212 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 H 212 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 H 212 PHE ASN ARG GLY SEQRES 1 I 223 GLN GLU VAL LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 I 223 PRO GLY ALA SER VAL LYS VAL SER CYS ARG ALA PHE GLY SEQRES 3 I 223 TYR THR PHE THR GLY ASN ALA LEU HIS TRP VAL ARG GLN SEQRES 4 I 223 ALA PRO GLY GLN GLY LEU GLU TRP LEU GLY TRP ILE ASN SEQRES 5 I 223 PRO HIS SER GLY ASP THR THR THR SER GLN LYS PHE GLN SEQRES 6 I 223 GLY ARG VAL TYR MET THR ARG ASP LYS SER ILE ASN THR SEQRES 7 I 223 ALA PHE LEU ASP VAL THR ARG LEU THR SER ASP ASP THR SEQRES 8 I 223 GLY ILE TYR TYR CYS ALA ARG ASP LYS TYR TYR GLY ASN SEQRES 9 I 223 GLU ALA VAL GLY MET ASP VAL TRP GLY GLN GLY THR SER SEQRES 10 I 223 VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL SEQRES 11 I 223 PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY SEQRES 12 I 223 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO SEQRES 13 I 223 GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SEQRES 14 I 223 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER SEQRES 15 I 223 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SEQRES 16 I 223 SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN SEQRES 17 I 223 HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU SEQRES 18 I 223 PRO LYS SEQRES 1 J 212 ASP ILE GLN LEU THR GLN SER PRO SER PHE LEU SER ALA SEQRES 2 J 212 SER VAL GLY ASP LYS VAL THR ILE THR CYS ARG ALA SER SEQRES 3 J 212 GLN GLY VAL ARG ASN GLU LEU ALA TRP TYR GLN GLN LYS SEQRES 4 J 212 PRO GLY LYS ALA PRO ASN LEU LEU ILE TYR TYR ALA SER SEQRES 5 J 212 THR LEU GLN SER GLY VAL PRO SER ARG PHE SER ALA THR SEQRES 6 J 212 GLY SER GLY THR HIS PHE THR LEU THR VAL SER SER LEU SEQRES 7 J 212 GLN PRO GLU ASP PHE ALA THR TYR PHE CYS GLN HIS MET SEQRES 8 J 212 SER SER TYR PRO LEU THR PHE GLY GLY GLY THR LYS VAL SEQRES 9 J 212 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 J 212 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 J 212 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 J 212 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 J 212 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 J 212 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 J 212 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 J 212 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 J 212 PHE ASN ARG GLY SEQRES 1 K 223 GLN GLU VAL LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 K 223 PRO GLY ALA SER VAL LYS VAL SER CYS ARG ALA PHE GLY SEQRES 3 K 223 TYR THR PHE THR GLY ASN ALA LEU HIS TRP VAL ARG GLN SEQRES 4 K 223 ALA PRO GLY GLN GLY LEU GLU TRP LEU GLY TRP ILE ASN SEQRES 5 K 223 PRO HIS SER GLY ASP THR THR THR SER GLN LYS PHE GLN SEQRES 6 K 223 GLY ARG VAL TYR MET THR ARG ASP LYS SER ILE ASN THR SEQRES 7 K 223 ALA PHE LEU ASP VAL THR ARG LEU THR SER ASP ASP THR SEQRES 8 K 223 GLY ILE TYR TYR CYS ALA ARG ASP LYS TYR TYR GLY ASN SEQRES 9 K 223 GLU ALA VAL GLY MET ASP VAL TRP GLY GLN GLY THR SER SEQRES 10 K 223 VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL SEQRES 11 K 223 PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY SEQRES 12 K 223 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO SEQRES 13 K 223 GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SEQRES 14 K 223 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER SEQRES 15 K 223 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SEQRES 16 K 223 SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN SEQRES 17 K 223 HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU SEQRES 18 K 223 PRO LYS SEQRES 1 L 212 ASP ILE GLN LEU THR GLN SER PRO SER PHE LEU SER ALA SEQRES 2 L 212 SER VAL GLY ASP LYS VAL THR ILE THR CYS ARG ALA SER SEQRES 3 L 212 GLN GLY VAL ARG ASN GLU LEU ALA TRP TYR GLN GLN LYS SEQRES 4 L 212 PRO GLY LYS ALA PRO ASN LEU LEU ILE TYR TYR ALA SER SEQRES 5 L 212 THR LEU GLN SER GLY VAL PRO SER ARG PHE SER ALA THR SEQRES 6 L 212 GLY SER GLY THR HIS PHE THR LEU THR VAL SER SER LEU SEQRES 7 L 212 GLN PRO GLU ASP PHE ALA THR TYR PHE CYS GLN HIS MET SEQRES 8 L 212 SER SER TYR PRO LEU THR PHE GLY GLY GLY THR LYS VAL SEQRES 9 L 212 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 L 212 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 L 212 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 L 212 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 L 212 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 L 212 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 L 212 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 L 212 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 L 212 PHE ASN ARG GLY SEQRES 1 M 96 LYS LYS VAL VAL LEU GLY LYS LYS GLY ASP THR VAL GLU SEQRES 2 M 96 LEU THR CYS THR ALA SER GLN LYS LYS SER ILE GLN PHE SEQRES 3 M 96 HIS TRP LYS ASN SER ASN GLN ILE LYS ILE LEU GLY ASN SEQRES 4 M 96 GLN GLY SER PHE LEU THR LYS GLY PRO SER LYS LEU ASN SEQRES 5 M 96 ASP ARG ALA ASP SER ARG ARG SER LEU TRP ASP GLN GLY SEQRES 6 M 96 ASN PHE PRO LEU ILE ILE LYS ASN LEU LYS ILE GLU ASP SEQRES 7 M 96 SER ASP THR TYR ILE CYS GLU VAL GLU ASP GLN LYS GLU SEQRES 8 M 96 GLU VAL GLN LEU LEU SEQRES 1 N 96 LYS LYS VAL VAL LEU GLY LYS LYS GLY ASP THR VAL GLU SEQRES 2 N 96 LEU THR CYS THR ALA SER GLN LYS LYS SER ILE GLN PHE SEQRES 3 N 96 HIS TRP LYS ASN SER ASN GLN ILE LYS ILE LEU GLY ASN SEQRES 4 N 96 GLN GLY SER PHE LEU THR LYS GLY PRO SER LYS LEU ASN SEQRES 5 N 96 ASP ARG ALA ASP SER ARG ARG SER LEU TRP ASP GLN GLY SEQRES 6 N 96 ASN PHE PRO LEU ILE ILE LYS ASN LEU LYS ILE GLU ASP SEQRES 7 N 96 SER ASP THR TYR ILE CYS GLU VAL GLU ASP GLN LYS GLU SEQRES 8 N 96 GLU VAL GLN LEU LEU SEQRES 1 O 96 LYS LYS VAL VAL LEU GLY LYS LYS GLY ASP THR VAL GLU SEQRES 2 O 96 LEU THR CYS THR ALA SER GLN LYS LYS SER ILE GLN PHE SEQRES 3 O 96 HIS TRP LYS ASN SER ASN GLN ILE LYS ILE LEU GLY ASN SEQRES 4 O 96 GLN GLY SER PHE LEU THR LYS GLY PRO SER LYS LEU ASN SEQRES 5 O 96 ASP ARG ALA ASP SER ARG ARG SER LEU TRP ASP GLN GLY SEQRES 6 O 96 ASN PHE PRO LEU ILE ILE LYS ASN LEU LYS ILE GLU ASP SEQRES 7 O 96 SER ASP THR TYR ILE CYS GLU VAL GLU ASP GLN LYS GLU SEQRES 8 O 96 GLU VAL GLN LEU LEU HET NAG P 1 14 HET NAG P 2 14 HET BMA P 3 11 HET MAN P 4 11 HET MAN P 5 11 HET NAG U 1 14 HET NAG U 2 14 HET BMA U 3 11 HET MAN U 4 11 HET MAN U 5 11 HET NAG Z 1 14 HET NAG Z 2 14 HET BMA Z 3 11 HET MAN Z 4 11 HET MAN Z 5 11 HET NAG e 1 14 HET NAG e 2 14 HET NAG E 701 14 HET NAG F 701 14 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BMA BETA-D-MANNOPYRANOSE HETNAM MAN ALPHA-D-MANNOPYRANOSE HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA- HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO- HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE FORMUL 16 NAG 10(C8 H15 N O6) FORMUL 16 BMA 3(C6 H12 O6) FORMUL 16 MAN 6(C6 H12 O6) HELIX 1 AA1 HIS A 66 HIS A 72 1 7 HELIX 2 AA2 ASN A 99 LEU A 116 1 18 HELIX 3 AA3 LYS A 335 ARG A 350 1 16 HELIX 4 AA4 LYS A 351 PHE A 353 5 3 HELIX 5 AA5 ASP A 368 THR A 373 1 6 HELIX 6 AA6 ASP A 474 ARG A 480 1 7 HELIX 7 AA7 MET B 100 SER B 115 1 16 HELIX 8 AA8 LYS B 335 PHE B 353 1 19 HELIX 9 AA9 ASP B 368 THR B 373 1 6 HELIX 10 AB1 ASP B 474 SER B 481 1 8 HELIX 11 AB2 ALA C 70 CYS C 74 5 5 HELIX 12 AB3 MET C 100 GLN C 114 1 15 HELIX 13 AB4 LYS C 335 GLY C 354 1 20 HELIX 14 AB5 ASP C 368 THR C 373 1 6 HELIX 15 AB6 ARG C 476 ARG C 480 5 5 HELIX 16 AB7 THR D 536 ASN D 543 1 8 HELIX 17 AB8 ILE D 573 TRP D 596 1 24 HELIX 18 AB9 ASN D 618 ASN D 625 1 8 HELIX 19 AC1 THR D 627 ILE D 635 1 9 HELIX 20 AC2 TYR D 638 GLN D 650 1 13 HELIX 21 AC3 GLU D 657 ALA D 662 1 6 HELIX 22 AC4 LYS E 567 TRP E 596 1 30 HELIX 23 AC5 ASN E 618 TRP E 623 1 6 HELIX 24 AC6 THR E 627 SER E 636 1 10 HELIX 25 AC7 TYR E 638 SER E 649 1 12 HELIX 26 AC8 GLN E 650 LYS E 655 1 6 HELIX 27 AC9 GLU E 657 ALA E 662 1 6 HELIX 28 AD1 THR F 536 ARG F 542 1 7 HELIX 29 AD2 ILE F 573 TRP F 596 1 24 HELIX 30 AD3 THR F 627 SER F 636 1 10 HELIX 31 AD4 TYR F 638 GLU F 654 1 17 HELIX 32 AD5 ASN F 656 ALA F 662 1 7 HELIX 33 AD6 THR G 28 ASN G 32 5 5 HELIX 34 AD7 THR I 28 ASN I 32 5 5 HELIX 35 AD8 GLN I 61 GLN I 64 5 4 HELIX 36 AD9 GLN J 79 PHE J 83 5 5 HELIX 37 AE1 THR K 28 ASN K 32 5 5 HELIX 38 AE2 THR K 83 THR K 87 5 5 HELIX 39 AE3 SER M 60 GLN M 64 5 5 HELIX 40 AE4 LEU N 51 ASP N 53 5 3 HELIX 41 AE5 ARG O 59 GLN O 64 5 6 HELIX 42 AE6 LYS O 75 SER O 79 5 5 SHEET 1 AA1 3 LEU A 494 THR A 499 0 SHEET 2 AA1 3 TRP A 35 TYR A 40 -1 N TYR A 39 O GLY A 495 SHEET 3 AA1 3 CYS D 604 PRO D 609 -1 O THR D 606 N VAL A 36 SHEET 1 AA2 5 TRP A 45 ASP A 47 0 SHEET 2 AA2 5 TYR A 486 ILE A 491 -1 O LYS A 490 N LYS A 46 SHEET 3 AA2 5 PHE A 223 CYS A 228 -1 N ALA A 224 O VAL A 489 SHEET 4 AA2 5 VAL A 242 VAL A 245 -1 O VAL A 245 N ILE A 225 SHEET 5 AA2 5 GLU A 83 HIS A 85 -1 N ILE A 84 O THR A 244 SHEET 1 AA3 2 GLU A 91 ASN A 94 0 SHEET 2 AA3 2 THR A 236 CYS A 239 -1 O GLY A 237 N PHE A 93 SHEET 1 AA4 4 THR A 198 THR A 202 0 SHEET 2 AA4 4 VAL A 120 PRO A 124 -1 N THR A 123 O SER A 199 SHEET 3 AA4 4 GLN A 432 MET A 434 -1 O GLN A 432 N LEU A 122 SHEET 4 AA4 4 ILE A 423 ASN A 425 -1 N ILE A 424 O ALA A 433 SHEET 1 AA5 7 LEU A 260 LEU A 261 0 SHEET 2 AA5 7 VAL A 446 ASP A 457 -1 O THR A 450 N LEU A 260 SHEET 3 AA5 7 ILE A 284 THR A 297 -1 N VAL A 292 O ILE A 449 SHEET 4 AA5 7 ALA A 329 SER A 334 -1 O ASN A 332 N ASN A 295 SHEET 5 AA5 7 SER A 413 ILE A 420 -1 O ILE A 414 N VAL A 333 SHEET 6 AA5 7 GLU A 381 CYS A 385 -1 N TYR A 384 O ARG A 419 SHEET 7 AA5 7 HIS A 374 CYS A 378 -1 N HIS A 374 O CYS A 385 SHEET 1 AA6 6 MET A 271 ARG A 273 0 SHEET 2 AA6 6 ILE A 284 THR A 297 -1 O GLN A 287 N MET A 271 SHEET 3 AA6 6 VAL A 446 ASP A 457 -1 O ILE A 449 N VAL A 292 SHEET 4 AA6 6 GLU A 466 PRO A 470 -1 O THR A 467 N ASP A 457 SHEET 5 AA6 6 ILE A 359 PHE A 361 1 N ARG A 360 O PHE A 468 SHEET 6 AA6 6 THR A 394 TRP A 395 -1 O TRP A 395 N ILE A 359 SHEET 1 AA7 3 LEU B 494 THR B 499 0 SHEET 2 AA7 3 TRP B 35 TYR B 40 -1 N TYR B 39 O GLY B 495 SHEET 3 AA7 3 ILE E 603 PRO E 609 -1 O CYS E 604 N VAL B 38 SHEET 1 AA8 5 TRP B 45 ASP B 47 0 SHEET 2 AA8 5 TYR B 486 ILE B 491 -1 O LYS B 490 N LYS B 46 SHEET 3 AA8 5 PHE B 223 CYS B 228 -1 N ALA B 224 O VAL B 489 SHEET 4 AA8 5 VAL B 242 VAL B 245 -1 O SER B 243 N LYS B 227 SHEET 5 AA8 5 GLU B 83 LEU B 86 -1 N ILE B 84 O THR B 244 SHEET 1 AA9 3 VAL B 75 PRO B 76 0 SHEET 2 AA9 3 PHE B 53 SER B 56 1 N CYS B 54 O VAL B 75 SHEET 3 AA9 3 HIS B 216 CYS B 218 -1 O CYS B 218 N PHE B 53 SHEET 1 AB1 2 GLU B 91 PHE B 93 0 SHEET 2 AB1 2 GLY B 237 CYS B 239 -1 O GLY B 237 N PHE B 93 SHEET 1 AB2 4 LEU B 259 LEU B 261 0 SHEET 2 AB2 4 ILE B 443 THR B 455 -1 O GLY B 451 N LEU B 260 SHEET 3 AB2 4 ILE B 284 ARG B 298 -1 N VAL B 292 O ILE B 449 SHEET 4 AB2 4 MET B 271 ARG B 273 -1 N ARG B 273 O LEU B 285 SHEET 1 AB3 5 LEU B 259 LEU B 261 0 SHEET 2 AB3 5 ILE B 443 THR B 455 -1 O GLY B 451 N LEU B 260 SHEET 3 AB3 5 THR B 465 PRO B 470 -1 O ARG B 469 N THR B 455 SHEET 4 AB3 5 ILE B 358 PHE B 361 1 N ARG B 360 O GLU B 466 SHEET 5 AB3 5 SER B 393 TRP B 395 -1 O SER B 393 N PHE B 361 SHEET 1 AB4 3 HIS B 374 CYS B 378 0 SHEET 2 AB4 3 GLU B 381 CYS B 385 -1 O CYS B 385 N HIS B 374 SHEET 3 AB4 3 CYS B 418 ILE B 420 -1 O ARG B 419 N TYR B 384 SHEET 1 AB5 3 LEU C 494 THR C 499 0 SHEET 2 AB5 3 TRP C 35 TYR C 40 -1 N THR C 37 O ALA C 497 SHEET 3 AB5 3 ILE F 603 PRO F 609 -1 O VAL F 608 N VAL C 36 SHEET 1 AB6 5 TRP C 45 ASP C 47 0 SHEET 2 AB6 5 TYR C 486 ILE C 491 -1 O LYS C 490 N LYS C 46 SHEET 3 AB6 5 PHE C 223 CYS C 228 -1 N LEU C 226 O LYS C 487 SHEET 4 AB6 5 VAL C 242 VAL C 245 -1 O SER C 243 N LYS C 227 SHEET 5 AB6 5 GLU C 83 LEU C 86 -1 N ILE C 84 O THR C 244 SHEET 1 AB7 3 VAL C 75 PRO C 76 0 SHEET 2 AB7 3 PHE C 53 SER C 56 1 N CYS C 54 O VAL C 75 SHEET 3 AB7 3 HIS C 216 CYS C 218 -1 O CYS C 218 N PHE C 53 SHEET 1 AB8 2 GLU C 91 ASN C 94 0 SHEET 2 AB8 2 THR C 236 CYS C 239 -1 O GLY C 237 N PHE C 93 SHEET 1 AB9 7 LEU C 259 LEU C 261 0 SHEET 2 AB9 7 ILE C 443 ARG C 456 -1 O GLY C 451 N LEU C 260 SHEET 3 AB9 7 ILE C 284 ARG C 298 -1 N VAL C 292 O ILE C 449 SHEET 4 AB9 7 HIS C 330 SER C 334 -1 O HIS C 330 N THR C 297 SHEET 5 AB9 7 SER C 413 ILE C 420 -1 O LEU C 416 N CYS C 331 SHEET 6 AB9 7 GLU C 381 CYS C 385 -1 N TYR C 384 O ARG C 419 SHEET 7 AB9 7 HIS C 374 CYS C 378 -1 N HIS C 374 O CYS C 385 SHEET 1 AC1 6 MET C 271 ARG C 273 0 SHEET 2 AC1 6 ILE C 284 ARG C 298 -1 O LEU C 285 N ARG C 273 SHEET 3 AC1 6 ILE C 443 ARG C 456 -1 O ILE C 449 N VAL C 292 SHEET 4 AC1 6 THR C 465 PRO C 470 -1 O ARG C 469 N THR C 455 SHEET 5 AC1 6 ILE C 358 PHE C 361 1 N ILE C 358 O GLU C 466 SHEET 6 AC1 6 SER C 393 TRP C 395 -1 O TRP C 395 N ILE C 359 SHEET 1 AC2 2 ILE C 423 ILE C 424 0 SHEET 2 AC2 2 MET C 434 TYR C 435 -1 O MET C 434 N ILE C 424 SHEET 1 AC3 4 VAL G 3 GLN G 6 0 SHEET 2 AC3 4 SER G 17 PHE G 25 -1 O ARG G 23 N VAL G 5 SHEET 3 AC3 4 THR G 77 THR G 82A-1 O LEU G 80 N VAL G 20 SHEET 4 AC3 4 VAL G 67 ASP G 72 -1 N TYR G 68 O ASP G 81 SHEET 1 AC4 6 GLU G 10 VAL G 11 0 SHEET 2 AC4 6 THR G 107 THR G 110 1 O SER G 108 N GLU G 10 SHEET 3 AC4 6 GLY G 88 ASP G 95 -1 N GLY G 88 O VAL G 109 SHEET 4 AC4 6 LEU G 34 GLN G 39 -1 N HIS G 35 O ALA G 93 SHEET 5 AC4 6 LEU G 45 ILE G 51 -1 O GLU G 46 N ARG G 38 SHEET 6 AC4 6 THR G 57 THR G 59 -1 O THR G 58 N TRP G 50 SHEET 1 AC5 4 GLU G 10 VAL G 11 0 SHEET 2 AC5 4 THR G 107 THR G 110 1 O SER G 108 N GLU G 10 SHEET 3 AC5 4 GLY G 88 ASP G 95 -1 N GLY G 88 O VAL G 109 SHEET 4 AC5 4 MET G 100E TRP G 103 -1 O VAL G 102 N ARG G 94 SHEET 1 AC6 4 LEU H 4 SER H 7 0 SHEET 2 AC6 4 VAL H 19 ALA H 25 -1 O ARG H 24 N THR H 5 SHEET 3 AC6 4 HIS H 70 VAL H 75 -1 O PHE H 71 N CYS H 23 SHEET 4 AC6 4 PHE H 62 SER H 67 -1 N THR H 65 O THR H 72 SHEET 1 AC7 6 PHE H 10 SER H 12 0 SHEET 2 AC7 6 THR H 102 GLU H 105 1 O LYS H 103 N LEU H 11 SHEET 3 AC7 6 THR H 85 GLN H 89 -1 N TYR H 86 O THR H 102 SHEET 4 AC7 6 ALA H 34 GLN H 38 -1 N GLN H 38 O THR H 85 SHEET 5 AC7 6 ASN H 45 TYR H 49 -1 O ASN H 45 N GLN H 37 SHEET 6 AC7 6 THR H 53 LEU H 54 -1 O THR H 53 N TYR H 49 SHEET 1 AC8 4 VAL I 3 GLN I 6 0 SHEET 2 AC8 4 SER I 17 PHE I 25 -1 O ARG I 23 N VAL I 5 SHEET 3 AC8 4 THR I 77 THR I 82A-1 O VAL I 82 N VAL I 18 SHEET 4 AC8 4 VAL I 67 ASP I 72 -1 N TYR I 68 O ASP I 81 SHEET 1 AC9 6 GLU I 10 VAL I 11 0 SHEET 2 AC9 6 THR I 107 THR I 110 1 O SER I 108 N GLU I 10 SHEET 3 AC9 6 GLY I 88 ASP I 95 -1 N GLY I 88 O VAL I 109 SHEET 4 AC9 6 LEU I 34 GLN I 39 -1 N GLN I 39 O ILE I 89 SHEET 5 AC9 6 GLU I 46 ILE I 51 -1 O GLU I 46 N ARG I 38 SHEET 6 AC9 6 THR I 57 THR I 59 -1 O THR I 58 N TRP I 50 SHEET 1 AD1 4 GLU I 10 VAL I 11 0 SHEET 2 AD1 4 THR I 107 THR I 110 1 O SER I 108 N GLU I 10 SHEET 3 AD1 4 GLY I 88 ASP I 95 -1 N GLY I 88 O VAL I 109 SHEET 4 AD1 4 MET I 100E TRP I 103 -1 O VAL I 102 N ARG I 94 SHEET 1 AD2 4 LEU J 4 SER J 7 0 SHEET 2 AD2 4 VAL J 19 ALA J 25 -1 O THR J 22 N SER J 7 SHEET 3 AD2 4 HIS J 70 VAL J 75 -1 O PHE J 71 N CYS J 23 SHEET 4 AD2 4 PHE J 62 SER J 67 -1 N SER J 63 O THR J 74 SHEET 1 AD3 2 PHE J 10 SER J 12 0 SHEET 2 AD3 2 LYS J 103 GLU J 105 1 O GLU J 105 N LEU J 11 SHEET 1 AD4 4 THR J 53 LEU J 54 0 SHEET 2 AD4 4 ASN J 45 TYR J 49 -1 N TYR J 49 O THR J 53 SHEET 3 AD4 4 LEU J 33 GLN J 38 -1 N GLN J 37 O ASN J 45 SHEET 4 AD4 4 THR J 85 HIS J 90 -1 O THR J 85 N GLN J 38 SHEET 1 AD5 4 VAL K 3 GLN K 6 0 SHEET 2 AD5 4 SER K 17 PHE K 25 -1 O ARG K 23 N VAL K 5 SHEET 3 AD5 4 THR K 77 THR K 82A-1 O VAL K 82 N VAL K 18 SHEET 4 AD5 4 VAL K 67 ASP K 72 -1 N TYR K 68 O ASP K 81 SHEET 1 AD6 6 GLU K 10 VAL K 11 0 SHEET 2 AD6 6 THR K 107 THR K 110 1 O THR K 110 N GLU K 10 SHEET 3 AD6 6 GLY K 88 ASP K 95 -1 N GLY K 88 O VAL K 109 SHEET 4 AD6 6 LEU K 34 GLN K 39 -1 N HIS K 35 O ALA K 93 SHEET 5 AD6 6 LEU K 45 ILE K 51 -1 O GLU K 46 N ARG K 38 SHEET 6 AD6 6 THR K 57 THR K 59 -1 O THR K 58 N TRP K 50 SHEET 1 AD7 4 GLU K 10 VAL K 11 0 SHEET 2 AD7 4 THR K 107 THR K 110 1 O THR K 110 N GLU K 10 SHEET 3 AD7 4 GLY K 88 ASP K 95 -1 N GLY K 88 O VAL K 109 SHEET 4 AD7 4 MET K 100E TRP K 103 -1 O VAL K 102 N ARG K 94 SHEET 1 AD8 4 LEU L 4 SER L 7 0 SHEET 2 AD8 4 VAL L 19 ALA L 25 -1 O ARG L 24 N THR L 5 SHEET 3 AD8 4 HIS L 70 VAL L 75 -1 O PHE L 71 N CYS L 23 SHEET 4 AD8 4 PHE L 62 SER L 67 -1 N THR L 65 O THR L 72 SHEET 1 AD9 6 PHE L 10 SER L 12 0 SHEET 2 AD9 6 THR L 102 GLU L 105 1 O LYS L 103 N LEU L 11 SHEET 3 AD9 6 THR L 85 HIS L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AD9 6 LEU L 33 GLN L 38 -1 N GLN L 38 O THR L 85 SHEET 5 AD9 6 ASN L 45 TYR L 49 -1 O LEU L 47 N TRP L 35 SHEET 6 AD9 6 THR L 53 LEU L 54 -1 O THR L 53 N TYR L 49 SHEET 1 AE1 6 LYS M 2 LEU M 5 0 SHEET 2 AE1 6 LYS M 90 LEU M 96 1 O GLN M 94 N VAL M 4 SHEET 3 AE1 6 ASP M 80 GLU M 85 -1 N TYR M 82 O VAL M 93 SHEET 4 AE1 6 HIS M 27 LYS M 29 -1 N LYS M 29 O ILE M 83 SHEET 5 AE1 6 LYS M 35 ASN M 39 -1 O ILE M 36 N TRP M 28 SHEET 6 AE1 6 LEU M 44 LYS M 46 -1 O THR M 45 N GLY M 38 SHEET 1 AE2 3 THR M 11 THR M 17 0 SHEET 2 AE2 3 ASN M 66 LYS M 72 -1 O ILE M 71 N VAL M 12 SHEET 3 AE2 3 ALA M 55 ASP M 56 -1 N ASP M 56 O ILE M 70 SHEET 1 AE3 4 LYS N 2 VAL N 3 0 SHEET 2 AE3 4 LYS N 90 GLN N 94 1 O GLN N 94 N LYS N 2 SHEET 3 AE3 4 TYR N 82 VAL N 86 -1 N TYR N 82 O VAL N 93 SHEET 4 AE3 4 PHE N 26 ASN N 30 -1 N HIS N 27 O GLU N 85 SHEET 1 AE4 3 VAL N 12 LEU N 14 0 SHEET 2 AE4 3 LEU N 69 ILE N 71 -1 O ILE N 71 N VAL N 12 SHEET 3 AE4 3 ALA N 55 ASP N 56 -1 N ASP N 56 O ILE N 70 SHEET 1 AE5 2 LEU N 37 ASN N 39 0 SHEET 2 AE5 2 LEU N 44 LYS N 46 -1 O THR N 45 N GLY N 38 SHEET 1 AE6 6 LYS O 2 LEU O 5 0 SHEET 2 AE6 6 GLN O 89 LEU O 96 1 O GLN O 94 N LYS O 2 SHEET 3 AE6 6 ASP O 80 VAL O 86 -1 N TYR O 82 O VAL O 93 SHEET 4 AE6 6 PHE O 26 LYS O 29 -1 N LYS O 29 O ILE O 83 SHEET 5 AE6 6 LYS O 35 ASN O 39 -1 O ILE O 36 N TRP O 28 SHEET 6 AE6 6 LEU O 44 LYS O 46 -1 O THR O 45 N GLY O 38 SHEET 1 AE7 3 VAL O 12 THR O 17 0 SHEET 2 AE7 3 ASN O 66 ILE O 71 -1 O PHE O 67 N CYS O 16 SHEET 3 AE7 3 ALA O 55 ASP O 56 -1 N ASP O 56 O ILE O 70 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 2.05 SSBOND 5 CYS A 228 CYS A 239 1555 1555 2.03 SSBOND 6 CYS A 296 CYS A 331 1555 1555 2.04 SSBOND 7 CYS A 378 CYS A 445 1555 1555 2.04 SSBOND 8 CYS A 385 CYS A 418 1555 1555 2.02 SSBOND 9 CYS A 501 CYS D 605 1555 1555 2.04 SSBOND 10 CYS B 54 CYS B 74 1555 1555 2.03 SSBOND 11 CYS B 218 CYS B 247 1555 1555 2.05 SSBOND 12 CYS B 228 CYS B 239 1555 1555 2.03 SSBOND 13 CYS B 296 CYS B 331 1555 1555 2.04 SSBOND 14 CYS B 296 CYS B 445 1555 1555 2.04 SSBOND 15 CYS B 378 CYS B 445 1555 1555 2.03 SSBOND 16 CYS B 385 CYS B 418 1555 1555 2.03 SSBOND 17 CYS B 501 CYS E 605 1555 1555 2.03 SSBOND 18 CYS C 54 CYS C 74 1555 1555 2.03 SSBOND 19 CYS C 218 CYS C 247 1555 1555 2.03 SSBOND 20 CYS C 228 CYS C 239 1555 1555 2.03 SSBOND 21 CYS C 296 CYS C 378 1555 1555 2.05 SSBOND 22 CYS C 296 CYS C 445 1555 1555 2.03 SSBOND 23 CYS C 378 CYS C 445 1555 1555 2.03 SSBOND 24 CYS C 385 CYS C 418 1555 1555 2.04 SSBOND 25 CYS C 501 CYS F 605 1555 1555 2.04 SSBOND 26 CYS D 598 CYS D 604 1555 1555 2.03 SSBOND 27 CYS E 598 CYS E 604 1555 1555 2.03 SSBOND 28 CYS F 598 CYS F 604 1555 1555 2.04 SSBOND 29 CYS G 22 CYS G 92 1555 1555 2.03 SSBOND 30 CYS H 23 CYS H 88 1555 1555 2.04 SSBOND 31 CYS I 22 CYS I 92 1555 1555 2.03 SSBOND 32 CYS J 23 CYS J 88 1555 1555 2.04 SSBOND 33 CYS K 22 CYS K 92 1555 1555 2.03 SSBOND 34 CYS L 23 CYS L 88 1555 1555 2.05 SSBOND 35 CYS M 16 CYS M 84 1555 1555 2.04 SSBOND 36 CYS N 16 CYS N 84 1555 1555 2.03 SSBOND 37 CYS O 16 CYS O 84 1555 1555 2.03 LINK ND2 ASN A 88 C1 NAG P 1 1555 1555 1.44 LINK ND2 ASN B 88 C1 NAG U 1 1555 1555 1.43 LINK ND2 ASN C 88 C1 NAG Z 1 1555 1555 1.44 LINK ND2 ASN D 611 C1 NAG e 1 1555 1555 1.46 LINK ND2 ASN E 611 C1 NAG E 701 1555 1555 1.44 LINK ND2 ASN F 611 C1 NAG F 701 1555 1555 1.44 LINK O4 NAG P 1 C1 NAG P 2 1555 1555 1.45 LINK O4 NAG P 2 C1 BMA P 3 1555 1555 1.44 LINK O3 BMA P 3 C1 MAN P 4 1555 1555 1.45 LINK O6 BMA P 3 C1 MAN P 5 1555 1555 1.44 LINK O4 NAG U 1 C1 NAG U 2 1555 1555 1.45 LINK O4 NAG U 2 C1 BMA U 3 1555 1555 1.45 LINK O3 BMA U 3 C1 MAN U 4 1555 1555 1.45 LINK O6 BMA U 3 C1 MAN U 5 1555 1555 1.45 LINK O4 NAG Z 1 C1 NAG Z 2 1555 1555 1.45 LINK O4 NAG Z 2 C1 BMA Z 3 1555 1555 1.47 LINK O3 BMA Z 3 C1 MAN Z 4 1555 1555 1.45 LINK O6 BMA Z 3 C1 MAN Z 5 1555 1555 1.44 LINK O4 NAG e 1 C1 NAG e 2 1555 1555 1.45 CISPEP 1 SER H 7 PRO H 8 0 -3.45 CISPEP 2 TYR H 94 PRO H 95 0 -6.28 CISPEP 3 SER J 7 PRO J 8 0 -3.30 CISPEP 4 TYR J 94 PRO J 95 0 -7.95 CISPEP 5 SER L 7 PRO L 8 0 -2.19 CISPEP 6 TYR L 94 PRO L 95 0 -7.18 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