HEADER VIRAL PROTEIN/IMMUNE SYSTEM 06-JAN-22 7TFO TITLE CRYO-EM STRUCTURE OF HIV-1 ENV TRIMER BG505 SOSIP.664 IN COMPLEX WITH TITLE 2 CD4BS ANTIBODY AB1573 COMPND MOL_ID: 1; COMPND 2 MOLECULE: ENVELOPE GLYCOPROTEIN BG505 SOSIP.664 - GP120; COMPND 3 CHAIN: A, B, C; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: CD4 BINDING SITE ANTIBODY AB1573 - FAB HEAVY CHAIN; COMPND 7 CHAIN: H, I, P; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: CD4 BINDING SITE ANTIBODY AB1573 - FAB LIGHT CHAIN; COMPND 11 CHAIN: J, L, Q; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 4; COMPND 14 MOLECULE: ENVELOPE GLYCOPROTEIN BG505 SOSIP.664 - GP41; COMPND 15 CHAIN: X, Y, Z; COMPND 16 FRAGMENT: UNP RESIDUES 509-661; COMPND 17 SYNONYM: ENV POLYPROTEIN; COMPND 18 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_COMMON: HUMAN; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: EXPI293F; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: MACACA MULATTA; SOURCE 11 ORGANISM_COMMON: RHESUS MONKEY; SOURCE 12 ORGANISM_TAXID: 9544; SOURCE 13 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 14 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 16 EXPRESSION_SYSTEM_CELL_LINE: EXPI293F; SOURCE 17 MOL_ID: 3; SOURCE 18 ORGANISM_SCIENTIFIC: MACACA MULATTA; SOURCE 19 ORGANISM_COMMON: RHESUS MONKEY; SOURCE 20 ORGANISM_TAXID: 9544; SOURCE 21 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 22 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 23 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 24 EXPRESSION_SYSTEM_CELL_LINE: EXPI293F; SOURCE 25 MOL_ID: 4; SOURCE 26 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 27 ORGANISM_TAXID: 11676; SOURCE 28 GENE: ENV; SOURCE 29 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 30 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 31 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 32 EXPRESSION_SYSTEM_CELL_LINE: EXPI293F KEYWDS CRYO-EM STRUCTURE OF THE TRIMERIC HIV-1 ENV ECTO-DOMAIN BG505 KEYWDS 2 SOSIP.664 IN COMPLEX WITH CD4 BINDING SITE ANTIBODY AB1573, VIRAL KEYWDS 3 PROTEIN, VIRAL PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR Z.YANG,P.J.BJORKMAN JRNL AUTH Z.YANG,K.A.DAM,M.D.BRIDGES,M.A.G.HOFFMANN,A.T.DELAITSCH, JRNL AUTH 2 H.B.GRISTICK,A.ESCOLANO,R.GAUTAM,M.A.MARTIN,M.C.NUSSENZWEIG, JRNL AUTH 3 W.L.HUBBELL,P.J.BJORKMAN JRNL TITL NEUTRALIZING ANTIBODIES INDUCED IN IMMUNIZED MACAQUES JRNL TITL 2 RECOGNIZE THE CD4-BINDING SITE ON AN OCCLUDED-OPEN HIV-1 JRNL TITL 3 ENVELOPE TRIMER JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 4.10 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : NULL REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : NULL 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) : 4.100 REMARK 3 NUMBER OF PARTICLES : 443817 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 7TFO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB. REMARK 100 THE DEPOSITION ID IS D_1000262206. 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 : BG505 SOSIP.664 IN COMPLEX WITH REMARK 245 CD4BS ANTIBODY AB1573 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 : NULL 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 : FEI TITAN KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 BIOQUANTUM (6K X REMARK 245 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1400.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 3000.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : 2.70 REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 60.00 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: DODECAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, H, I, J, L, P, Q, X, REMARK 350 AND CHAINS: Y, Z, D, E, F, G, K REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 ALA A 31 REMARK 465 GLU A 32 REMARK 465 ASN A 33 REMARK 465 ALA A 70 REMARK 465 THR A 71 REMARK 465 ASP A 148 REMARK 465 ASP A 149 REMARK 465 THR A 163 REMARK 465 GLU A 164 REMARK 465 LEU A 165 REMARK 465 ARG A 166 REMARK 465 ASP A 167 REMARK 465 LYS A 168 REMARK 465 LYS A 169 REMARK 465 GLN A 170 REMARK 465 GLU A 185A REMARK 465 ASN A 185B REMARK 465 GLN A 185C REMARK 465 GLY A 185D REMARK 465 ASN A 185E REMARK 465 ARG A 185F REMARK 465 SER A 185G REMARK 465 ASN A 185H REMARK 465 ASN A 185I REMARK 465 SER A 185J REMARK 465 ASN A 185K REMARK 465 GLU A 267 REMARK 465 GLU A 268 REMARK 465 GLY A 312 REMARK 465 PRO A 313 REMARK 465 GLY A 314 REMARK 465 ASP A 325 REMARK 465 GLY A 354 REMARK 465 ASN A 355 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 ASP A 412 REMARK 465 GLY A 459 REMARK 465 SER A 460 REMARK 465 THR A 461 REMARK 465 ASN A 462 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 31 REMARK 465 GLU B 32 REMARK 465 ASN B 33 REMARK 465 HIS B 66 REMARK 465 CYS B 74 REMARK 465 GLN B 114 REMARK 465 SER B 115 REMARK 465 LEU B 116 REMARK 465 LYS B 117 REMARK 465 PRO B 118 REMARK 465 VAL B 127 REMARK 465 THR B 128 REMARK 465 LEU B 129 REMARK 465 THR B 147 REMARK 465 ASP B 148 REMARK 465 ASP B 149 REMARK 465 MET B 150 REMARK 465 THR B 163 REMARK 465 GLU B 164 REMARK 465 LEU B 165 REMARK 465 ARG B 166 REMARK 465 ASP B 167 REMARK 465 LYS B 168 REMARK 465 LYS B 169 REMARK 465 GLN B 170 REMARK 465 LYS B 171 REMARK 465 GLU B 185A REMARK 465 ASN B 185B REMARK 465 GLN B 185C REMARK 465 GLY B 185D REMARK 465 ASN B 185E REMARK 465 ARG B 185F REMARK 465 SER B 185G REMARK 465 ASN B 185H REMARK 465 ASN B 185I REMARK 465 SER B 185J REMARK 465 ASN B 185K REMARK 465 VAL B 208 REMARK 465 SER B 209 REMARK 465 ILE B 309 REMARK 465 ARG B 310 REMARK 465 ILE B 311 REMARK 465 GLY B 312 REMARK 465 PRO B 313 REMARK 465 SER B 398 REMARK 465 ASN B 399 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 SER B 413 REMARK 465 ARG B 504 REMARK 465 VAL B 505 REMARK 465 VAL B 506 REMARK 465 GLY B 507 REMARK 465 ARG B 508 REMARK 465 ARG B 509 REMARK 465 ARG B 510 REMARK 465 ARG B 511 REMARK 465 ARG B 512 REMARK 465 ARG B 513 REMARK 465 ALA C 31 REMARK 465 GLU C 32 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 LYS C 64 REMARK 465 LYS C 65 REMARK 465 HIS C 66 REMARK 465 ASN C 67 REMARK 465 VAL C 68 REMARK 465 TRP C 69 REMARK 465 ALA C 70 REMARK 465 ASP C 148 REMARK 465 ASP C 149 REMARK 465 MET C 150 REMARK 465 THR C 163 REMARK 465 GLU C 164 REMARK 465 LEU C 165 REMARK 465 ARG C 166 REMARK 465 ASP C 167 REMARK 465 LYS C 168 REMARK 465 LYS C 169 REMARK 465 GLN C 170 REMARK 465 GLU C 185A REMARK 465 ASN C 185B REMARK 465 GLN C 185C REMARK 465 GLY C 185D REMARK 465 ASN C 185E REMARK 465 ARG C 185F REMARK 465 SER C 185G REMARK 465 ASN C 185H REMARK 465 ASN C 185I REMARK 465 SER C 185J REMARK 465 ASN C 185K REMARK 465 GLY C 312 REMARK 465 PRO C 313 REMARK 465 GLY C 314 REMARK 465 PHE C 353 REMARK 465 GLY C 354 REMARK 465 ASN C 355 REMARK 465 ILE C 397 REMARK 465 SER C 398 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 ASP C 412 REMARK 465 SER C 413 REMARK 465 GLY C 458 REMARK 465 GLY C 459 REMARK 465 SER C 460 REMARK 465 THR C 461 REMARK 465 ASN C 462 REMARK 465 SER C 463 REMARK 465 THR C 464 REMARK 465 THR C 465 REMARK 465 GLU C 466 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 H 114 REMARK 465 SER H 115 REMARK 465 THR H 116 REMARK 465 LYS H 117 REMARK 465 GLY H 118 REMARK 465 PRO H 119 REMARK 465 SER H 120 REMARK 465 VAL H 121 REMARK 465 PHE H 122 REMARK 465 PRO H 123 REMARK 465 LEU H 124 REMARK 465 ALA H 125 REMARK 465 PRO H 126 REMARK 465 SER H 127 REMARK 465 SER H 128 REMARK 465 LYS H 129 REMARK 465 SER H 130 REMARK 465 THR H 131 REMARK 465 SER H 132 REMARK 465 GLY H 133 REMARK 465 GLY H 134 REMARK 465 THR H 135 REMARK 465 ALA H 136 REMARK 465 ALA H 137 REMARK 465 LEU H 138 REMARK 465 GLY H 139 REMARK 465 CYS H 140 REMARK 465 LEU H 141 REMARK 465 VAL H 142 REMARK 465 LYS H 143 REMARK 465 ASP H 144 REMARK 465 TYR H 145 REMARK 465 PHE H 146 REMARK 465 PRO H 147 REMARK 465 GLU H 148 REMARK 465 PRO H 149 REMARK 465 VAL H 150 REMARK 465 THR H 151 REMARK 465 VAL H 152 REMARK 465 SER H 153 REMARK 465 TRP H 154 REMARK 465 ASN H 155 REMARK 465 SER H 156 REMARK 465 GLY H 157 REMARK 465 ALA H 158 REMARK 465 LEU H 159 REMARK 465 THR H 160 REMARK 465 SER H 161 REMARK 465 GLY H 162 REMARK 465 VAL H 163 REMARK 465 HIS H 164 REMARK 465 THR H 165 REMARK 465 PHE H 166 REMARK 465 PRO H 167 REMARK 465 ALA H 168 REMARK 465 VAL H 169 REMARK 465 LEU H 170 REMARK 465 GLN H 171 REMARK 465 SER H 172 REMARK 465 SER H 173 REMARK 465 GLY H 174 REMARK 465 LEU H 175 REMARK 465 TYR H 176 REMARK 465 SER H 177 REMARK 465 LEU H 178 REMARK 465 SER H 179 REMARK 465 SER H 180 REMARK 465 VAL H 181 REMARK 465 VAL H 182 REMARK 465 THR H 183 REMARK 465 VAL H 184 REMARK 465 PRO H 185 REMARK 465 SER H 186 REMARK 465 SER H 187 REMARK 465 SER H 188 REMARK 465 LEU H 189 REMARK 465 GLY H 190 REMARK 465 THR H 191 REMARK 465 GLN H 192 REMARK 465 THR H 193 REMARK 465 TYR H 194 REMARK 465 ILE H 195 REMARK 465 CYS H 196 REMARK 465 ASN H 197 REMARK 465 VAL H 198 REMARK 465 ASN H 199 REMARK 465 HIS H 200 REMARK 465 LYS H 201 REMARK 465 PRO H 202 REMARK 465 SER H 203 REMARK 465 ASN H 204 REMARK 465 THR H 205 REMARK 465 LYS H 206 REMARK 465 VAL H 207 REMARK 465 ASP H 208 REMARK 465 LYS H 209 REMARK 465 ARG H 210 REMARK 465 VAL H 211 REMARK 465 GLU H 212 REMARK 465 PRO H 213 REMARK 465 LYS H 214 REMARK 465 SER H 215 REMARK 465 CYS H 216 REMARK 465 ASP H 217 REMARK 465 LYS H 218 REMARK 465 THR H 219 REMARK 465 ALA I 114 REMARK 465 SER I 115 REMARK 465 THR I 116 REMARK 465 LYS I 117 REMARK 465 GLY I 118 REMARK 465 PRO I 119 REMARK 465 SER I 120 REMARK 465 VAL I 121 REMARK 465 PHE I 122 REMARK 465 PRO I 123 REMARK 465 LEU I 124 REMARK 465 ALA I 125 REMARK 465 PRO I 126 REMARK 465 SER I 127 REMARK 465 SER I 128 REMARK 465 LYS I 129 REMARK 465 SER I 130 REMARK 465 THR I 131 REMARK 465 SER I 132 REMARK 465 GLY I 133 REMARK 465 GLY I 134 REMARK 465 THR I 135 REMARK 465 ALA I 136 REMARK 465 ALA I 137 REMARK 465 LEU I 138 REMARK 465 GLY I 139 REMARK 465 CYS I 140 REMARK 465 LEU I 141 REMARK 465 VAL I 142 REMARK 465 LYS I 143 REMARK 465 ASP I 144 REMARK 465 TYR I 145 REMARK 465 PHE I 146 REMARK 465 PRO I 147 REMARK 465 GLU I 148 REMARK 465 PRO I 149 REMARK 465 VAL I 150 REMARK 465 THR I 151 REMARK 465 VAL I 152 REMARK 465 SER I 153 REMARK 465 TRP I 154 REMARK 465 ASN I 155 REMARK 465 SER I 156 REMARK 465 GLY I 157 REMARK 465 ALA I 158 REMARK 465 LEU I 159 REMARK 465 THR I 160 REMARK 465 SER I 161 REMARK 465 GLY I 162 REMARK 465 VAL I 163 REMARK 465 HIS I 164 REMARK 465 THR I 165 REMARK 465 PHE I 166 REMARK 465 PRO I 167 REMARK 465 ALA I 168 REMARK 465 VAL I 169 REMARK 465 LEU I 170 REMARK 465 GLN I 171 REMARK 465 SER I 172 REMARK 465 SER I 173 REMARK 465 GLY I 174 REMARK 465 LEU I 175 REMARK 465 TYR I 176 REMARK 465 SER I 177 REMARK 465 LEU I 178 REMARK 465 SER I 179 REMARK 465 SER I 180 REMARK 465 VAL I 181 REMARK 465 VAL I 182 REMARK 465 THR I 183 REMARK 465 VAL I 184 REMARK 465 PRO I 185 REMARK 465 SER I 186 REMARK 465 SER I 187 REMARK 465 SER I 188 REMARK 465 LEU I 189 REMARK 465 GLY I 190 REMARK 465 THR I 191 REMARK 465 GLN I 192 REMARK 465 THR I 193 REMARK 465 TYR I 194 REMARK 465 ILE I 195 REMARK 465 CYS I 196 REMARK 465 ASN I 197 REMARK 465 VAL I 198 REMARK 465 ASN I 199 REMARK 465 HIS I 200 REMARK 465 LYS I 201 REMARK 465 PRO I 202 REMARK 465 SER I 203 REMARK 465 ASN I 204 REMARK 465 THR I 205 REMARK 465 LYS I 206 REMARK 465 VAL I 207 REMARK 465 ASP I 208 REMARK 465 LYS I 209 REMARK 465 ARG I 210 REMARK 465 VAL I 211 REMARK 465 GLU I 212 REMARK 465 PRO I 213 REMARK 465 LYS I 214 REMARK 465 SER I 215 REMARK 465 CYS I 216 REMARK 465 ASP I 217 REMARK 465 LYS I 218 REMARK 465 THR I 219 REMARK 465 GLN J 1 REMARK 465 GLN J 109 REMARK 465 PRO J 110 REMARK 465 LYS J 111 REMARK 465 ALA J 112 REMARK 465 ALA J 113 REMARK 465 PRO J 114 REMARK 465 SER J 115 REMARK 465 VAL J 116 REMARK 465 THR J 117 REMARK 465 LEU J 118 REMARK 465 PHE J 119 REMARK 465 PRO J 120 REMARK 465 PRO J 121 REMARK 465 SER J 122 REMARK 465 SER J 123 REMARK 465 GLU J 124 REMARK 465 GLU J 125 REMARK 465 LEU J 126 REMARK 465 GLN J 127 REMARK 465 ALA J 128 REMARK 465 ASN J 129 REMARK 465 LYS J 130 REMARK 465 ALA J 131 REMARK 465 THR J 132 REMARK 465 LEU J 133 REMARK 465 VAL J 134 REMARK 465 CYS J 135 REMARK 465 LEU J 136 REMARK 465 ILE J 137 REMARK 465 SER J 138 REMARK 465 ASP J 139 REMARK 465 PHE J 140 REMARK 465 TYR J 141 REMARK 465 PRO J 142 REMARK 465 GLY J 143 REMARK 465 ALA J 144 REMARK 465 VAL J 145 REMARK 465 THR J 146 REMARK 465 VAL J 147 REMARK 465 ALA J 148 REMARK 465 TRP J 149 REMARK 465 LYS J 150 REMARK 465 ALA J 151 REMARK 465 ASP J 152 REMARK 465 SER J 153 REMARK 465 SER J 154 REMARK 465 PRO J 155 REMARK 465 VAL J 156 REMARK 465 LYS J 157 REMARK 465 ALA J 158 REMARK 465 GLY J 159 REMARK 465 VAL J 160 REMARK 465 GLU J 161 REMARK 465 THR J 162 REMARK 465 THR J 163 REMARK 465 THR J 164 REMARK 465 PRO J 165 REMARK 465 SER J 166 REMARK 465 LYS J 167 REMARK 465 GLN J 168 REMARK 465 SER J 169 REMARK 465 ASN J 170 REMARK 465 ASN J 171 REMARK 465 LYS J 172 REMARK 465 TYR J 173 REMARK 465 ALA J 174 REMARK 465 ALA J 175 REMARK 465 SER J 176 REMARK 465 SER J 177 REMARK 465 TYR J 178 REMARK 465 LEU J 179 REMARK 465 SER J 180 REMARK 465 LEU J 181 REMARK 465 THR J 182 REMARK 465 PRO J 183 REMARK 465 GLU J 184 REMARK 465 GLN J 185 REMARK 465 TRP J 186 REMARK 465 LYS J 187 REMARK 465 SER J 188 REMARK 465 HIS J 189 REMARK 465 ARG J 190 REMARK 465 SER J 191 REMARK 465 TYR J 192 REMARK 465 SER J 193 REMARK 465 CYS J 194 REMARK 465 GLN J 195 REMARK 465 VAL J 196 REMARK 465 THR J 197 REMARK 465 HIS J 198 REMARK 465 GLU J 199 REMARK 465 GLY J 200 REMARK 465 SER J 201 REMARK 465 THR J 202 REMARK 465 VAL J 203 REMARK 465 GLU J 204 REMARK 465 LYS J 205 REMARK 465 THR J 206 REMARK 465 VAL J 207 REMARK 465 ALA J 208 REMARK 465 PRO J 209 REMARK 465 THR J 210 REMARK 465 GLU J 211 REMARK 465 CYS J 212 REMARK 465 SER J 213 REMARK 465 GLN L 1 REMARK 465 GLN L 109 REMARK 465 PRO L 110 REMARK 465 LYS L 111 REMARK 465 ALA L 112 REMARK 465 ALA L 113 REMARK 465 PRO L 114 REMARK 465 SER L 115 REMARK 465 VAL L 116 REMARK 465 THR L 117 REMARK 465 LEU L 118 REMARK 465 PHE L 119 REMARK 465 PRO L 120 REMARK 465 PRO L 121 REMARK 465 SER L 122 REMARK 465 SER L 123 REMARK 465 GLU L 124 REMARK 465 GLU L 125 REMARK 465 LEU L 126 REMARK 465 GLN L 127 REMARK 465 ALA L 128 REMARK 465 ASN L 129 REMARK 465 LYS L 130 REMARK 465 ALA L 131 REMARK 465 THR L 132 REMARK 465 LEU L 133 REMARK 465 VAL L 134 REMARK 465 CYS L 135 REMARK 465 LEU L 136 REMARK 465 ILE L 137 REMARK 465 SER L 138 REMARK 465 ASP L 139 REMARK 465 PHE L 140 REMARK 465 TYR L 141 REMARK 465 PRO L 142 REMARK 465 GLY L 143 REMARK 465 ALA L 144 REMARK 465 VAL L 145 REMARK 465 THR L 146 REMARK 465 VAL L 147 REMARK 465 ALA L 148 REMARK 465 TRP L 149 REMARK 465 LYS L 150 REMARK 465 ALA L 151 REMARK 465 ASP L 152 REMARK 465 SER L 153 REMARK 465 SER L 154 REMARK 465 PRO L 155 REMARK 465 VAL L 156 REMARK 465 LYS L 157 REMARK 465 ALA L 158 REMARK 465 GLY L 159 REMARK 465 VAL L 160 REMARK 465 GLU L 161 REMARK 465 THR L 162 REMARK 465 THR L 163 REMARK 465 THR L 164 REMARK 465 PRO L 165 REMARK 465 SER L 166 REMARK 465 LYS L 167 REMARK 465 GLN L 168 REMARK 465 SER L 169 REMARK 465 ASN L 170 REMARK 465 ASN L 171 REMARK 465 LYS L 172 REMARK 465 TYR L 173 REMARK 465 ALA L 174 REMARK 465 ALA L 175 REMARK 465 SER L 176 REMARK 465 SER L 177 REMARK 465 TYR L 178 REMARK 465 LEU L 179 REMARK 465 SER L 180 REMARK 465 LEU L 181 REMARK 465 THR L 182 REMARK 465 PRO L 183 REMARK 465 GLU L 184 REMARK 465 GLN L 185 REMARK 465 TRP L 186 REMARK 465 LYS L 187 REMARK 465 SER L 188 REMARK 465 HIS L 189 REMARK 465 ARG L 190 REMARK 465 SER L 191 REMARK 465 TYR L 192 REMARK 465 SER L 193 REMARK 465 CYS L 194 REMARK 465 GLN L 195 REMARK 465 VAL L 196 REMARK 465 THR L 197 REMARK 465 HIS L 198 REMARK 465 GLU L 199 REMARK 465 GLY L 200 REMARK 465 SER L 201 REMARK 465 THR L 202 REMARK 465 VAL L 203 REMARK 465 GLU L 204 REMARK 465 LYS L 205 REMARK 465 THR L 206 REMARK 465 VAL L 207 REMARK 465 ALA L 208 REMARK 465 PRO L 209 REMARK 465 THR L 210 REMARK 465 GLU L 211 REMARK 465 CYS L 212 REMARK 465 SER L 213 REMARK 465 GLN P 1 REMARK 465 SER P 74 REMARK 465 THR P 75 REMARK 465 SER P 112 REMARK 465 SER P 113 REMARK 465 ALA P 114 REMARK 465 SER P 115 REMARK 465 THR P 116 REMARK 465 LYS P 117 REMARK 465 GLY P 118 REMARK 465 PRO P 119 REMARK 465 SER P 120 REMARK 465 VAL P 121 REMARK 465 PHE P 122 REMARK 465 PRO P 123 REMARK 465 LEU P 124 REMARK 465 ALA P 125 REMARK 465 PRO P 126 REMARK 465 SER P 127 REMARK 465 SER P 128 REMARK 465 LYS P 129 REMARK 465 SER P 130 REMARK 465 THR P 131 REMARK 465 SER P 132 REMARK 465 GLY P 133 REMARK 465 GLY P 134 REMARK 465 THR P 135 REMARK 465 ALA P 136 REMARK 465 ALA P 137 REMARK 465 LEU P 138 REMARK 465 GLY P 139 REMARK 465 CYS P 140 REMARK 465 LEU P 141 REMARK 465 VAL P 142 REMARK 465 LYS P 143 REMARK 465 ASP P 144 REMARK 465 TYR P 145 REMARK 465 PHE P 146 REMARK 465 PRO P 147 REMARK 465 GLU P 148 REMARK 465 PRO P 149 REMARK 465 VAL P 150 REMARK 465 THR P 151 REMARK 465 VAL P 152 REMARK 465 SER P 153 REMARK 465 TRP P 154 REMARK 465 ASN P 155 REMARK 465 SER P 156 REMARK 465 GLY P 157 REMARK 465 ALA P 158 REMARK 465 LEU P 159 REMARK 465 THR P 160 REMARK 465 SER P 161 REMARK 465 GLY P 162 REMARK 465 VAL P 163 REMARK 465 HIS P 164 REMARK 465 THR P 165 REMARK 465 PHE P 166 REMARK 465 PRO P 167 REMARK 465 ALA P 168 REMARK 465 VAL P 169 REMARK 465 LEU P 170 REMARK 465 GLN P 171 REMARK 465 SER P 172 REMARK 465 SER P 173 REMARK 465 GLY P 174 REMARK 465 LEU P 175 REMARK 465 TYR P 176 REMARK 465 SER P 177 REMARK 465 LEU P 178 REMARK 465 SER P 179 REMARK 465 SER P 180 REMARK 465 VAL P 181 REMARK 465 VAL P 182 REMARK 465 THR P 183 REMARK 465 VAL P 184 REMARK 465 PRO P 185 REMARK 465 SER P 186 REMARK 465 SER P 187 REMARK 465 SER P 188 REMARK 465 LEU P 189 REMARK 465 GLY P 190 REMARK 465 THR P 191 REMARK 465 GLN P 192 REMARK 465 THR P 193 REMARK 465 TYR P 194 REMARK 465 ILE P 195 REMARK 465 CYS P 196 REMARK 465 ASN P 197 REMARK 465 VAL P 198 REMARK 465 ASN P 199 REMARK 465 HIS P 200 REMARK 465 LYS P 201 REMARK 465 PRO P 202 REMARK 465 SER P 203 REMARK 465 ASN P 204 REMARK 465 THR P 205 REMARK 465 LYS P 206 REMARK 465 VAL P 207 REMARK 465 ASP P 208 REMARK 465 LYS P 209 REMARK 465 ARG P 210 REMARK 465 VAL P 211 REMARK 465 GLU P 212 REMARK 465 PRO P 213 REMARK 465 LYS P 214 REMARK 465 SER P 215 REMARK 465 CYS P 216 REMARK 465 ASP P 217 REMARK 465 LYS P 218 REMARK 465 THR P 219 REMARK 465 GLN Q 1 REMARK 465 LEU Q 107 REMARK 465 GLY Q 108 REMARK 465 GLN Q 109 REMARK 465 PRO Q 110 REMARK 465 LYS Q 111 REMARK 465 ALA Q 112 REMARK 465 ALA Q 113 REMARK 465 PRO Q 114 REMARK 465 SER Q 115 REMARK 465 VAL Q 116 REMARK 465 THR Q 117 REMARK 465 LEU Q 118 REMARK 465 PHE Q 119 REMARK 465 PRO Q 120 REMARK 465 PRO Q 121 REMARK 465 SER Q 122 REMARK 465 SER Q 123 REMARK 465 GLU Q 124 REMARK 465 GLU Q 125 REMARK 465 LEU Q 126 REMARK 465 GLN Q 127 REMARK 465 ALA Q 128 REMARK 465 ASN Q 129 REMARK 465 LYS Q 130 REMARK 465 ALA Q 131 REMARK 465 THR Q 132 REMARK 465 LEU Q 133 REMARK 465 VAL Q 134 REMARK 465 CYS Q 135 REMARK 465 LEU Q 136 REMARK 465 ILE Q 137 REMARK 465 SER Q 138 REMARK 465 ASP Q 139 REMARK 465 PHE Q 140 REMARK 465 TYR Q 141 REMARK 465 PRO Q 142 REMARK 465 GLY Q 143 REMARK 465 ALA Q 144 REMARK 465 VAL Q 145 REMARK 465 THR Q 146 REMARK 465 VAL Q 147 REMARK 465 ALA Q 148 REMARK 465 TRP Q 149 REMARK 465 LYS Q 150 REMARK 465 ALA Q 151 REMARK 465 ASP Q 152 REMARK 465 SER Q 153 REMARK 465 SER Q 154 REMARK 465 PRO Q 155 REMARK 465 VAL Q 156 REMARK 465 LYS Q 157 REMARK 465 ALA Q 158 REMARK 465 GLY Q 159 REMARK 465 VAL Q 160 REMARK 465 GLU Q 161 REMARK 465 THR Q 162 REMARK 465 THR Q 163 REMARK 465 THR Q 164 REMARK 465 PRO Q 165 REMARK 465 SER Q 166 REMARK 465 LYS Q 167 REMARK 465 GLN Q 168 REMARK 465 SER Q 169 REMARK 465 ASN Q 170 REMARK 465 ASN Q 171 REMARK 465 LYS Q 172 REMARK 465 TYR Q 173 REMARK 465 ALA Q 174 REMARK 465 ALA Q 175 REMARK 465 SER Q 176 REMARK 465 SER Q 177 REMARK 465 TYR Q 178 REMARK 465 LEU Q 179 REMARK 465 SER Q 180 REMARK 465 LEU Q 181 REMARK 465 THR Q 182 REMARK 465 PRO Q 183 REMARK 465 GLU Q 184 REMARK 465 GLN Q 185 REMARK 465 TRP Q 186 REMARK 465 LYS Q 187 REMARK 465 SER Q 188 REMARK 465 HIS Q 189 REMARK 465 ARG Q 190 REMARK 465 SER Q 191 REMARK 465 TYR Q 192 REMARK 465 SER Q 193 REMARK 465 CYS Q 194 REMARK 465 GLN Q 195 REMARK 465 VAL Q 196 REMARK 465 THR Q 197 REMARK 465 HIS Q 198 REMARK 465 GLU Q 199 REMARK 465 GLY Q 200 REMARK 465 SER Q 201 REMARK 465 THR Q 202 REMARK 465 VAL Q 203 REMARK 465 GLU Q 204 REMARK 465 LYS Q 205 REMARK 465 THR Q 206 REMARK 465 VAL Q 207 REMARK 465 ALA Q 208 REMARK 465 PRO Q 209 REMARK 465 THR Q 210 REMARK 465 GLU Q 211 REMARK 465 CYS Q 212 REMARK 465 SER Q 213 REMARK 465 ALA X 512 REMARK 465 VAL X 513 REMARK 465 ASN X 543 REMARK 465 LEU X 544 REMARK 465 LEU X 545 REMARK 465 SER X 546 REMARK 465 GLY X 547 REMARK 465 ILE X 548 REMARK 465 VAL X 549 REMARK 465 GLN X 550 REMARK 465 GLN X 551 REMARK 465 GLN X 552 REMARK 465 SER X 553 REMARK 465 ASN X 554 REMARK 465 LEU X 555 REMARK 465 LEU X 556 REMARK 465 ARG X 557 REMARK 465 ALA X 558 REMARK 465 PRO X 559 REMARK 465 GLU X 560 REMARK 465 ALA X 561 REMARK 465 GLN X 562 REMARK 465 GLN X 658 REMARK 465 ASP X 659 REMARK 465 LEU X 660 REMARK 465 LEU X 661 REMARK 465 ALA X 662 REMARK 465 LEU X 663 REMARK 465 ASP X 664 REMARK 465 ALA Y 512 REMARK 465 VAL Y 513 REMARK 465 GLY Y 514 REMARK 465 ILE Y 515 REMARK 465 GLY Y 516 REMARK 465 ALA Y 517 REMARK 465 VAL Y 518 REMARK 465 PHE Y 519 REMARK 465 LEU Y 520 REMARK 465 GLY Y 521 REMARK 465 GLY Y 547 REMARK 465 ILE Y 548 REMARK 465 VAL Y 549 REMARK 465 GLN Y 550 REMARK 465 GLN Y 551 REMARK 465 GLN Y 552 REMARK 465 SER Y 553 REMARK 465 ASN Y 554 REMARK 465 LEU Y 555 REMARK 465 LEU Y 556 REMARK 465 ARG Y 557 REMARK 465 ALA Y 558 REMARK 465 PRO Y 559 REMARK 465 GLU Y 560 REMARK 465 ALA Y 561 REMARK 465 GLN Y 562 REMARK 465 LYS Y 655 REMARK 465 ASN Y 656 REMARK 465 GLU Y 657 REMARK 465 GLN Y 658 REMARK 465 ASP Y 659 REMARK 465 LEU Y 660 REMARK 465 LEU Y 661 REMARK 465 ALA Y 662 REMARK 465 LEU Y 663 REMARK 465 ASP Y 664 REMARK 465 ALA Z 512 REMARK 465 VAL Z 513 REMARK 465 GLY Z 514 REMARK 465 ILE Z 515 REMARK 465 GLY Z 516 REMARK 465 ALA Z 517 REMARK 465 VAL Z 518 REMARK 465 PHE Z 519 REMARK 465 LEU Z 520 REMARK 465 GLY Z 521 REMARK 465 ALA Z 541 REMARK 465 ARG Z 542 REMARK 465 ASN Z 543 REMARK 465 LEU Z 544 REMARK 465 LEU Z 545 REMARK 465 SER Z 546 REMARK 465 GLY Z 547 REMARK 465 ILE Z 548 REMARK 465 VAL Z 549 REMARK 465 GLN Z 550 REMARK 465 GLN Z 551 REMARK 465 GLN Z 552 REMARK 465 SER Z 553 REMARK 465 ASN Z 554 REMARK 465 LEU Z 555 REMARK 465 LEU Z 556 REMARK 465 ARG Z 557 REMARK 465 ALA Z 558 REMARK 465 PRO Z 559 REMARK 465 GLU Z 560 REMARK 465 ALA Z 561 REMARK 465 GLN Z 562 REMARK 465 LEU Z 661 REMARK 465 ALA Z 662 REMARK 465 LEU Z 663 REMARK 465 ASP Z 664 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 LYS A 46 CG CD CE NZ REMARK 470 ASP A 47 CG OD1 OD2 REMARK 470 GLU A 49 CG CD OE1 OE2 REMARK 470 THR A 50 OG1 CG2 REMARK 470 THR A 51 OG1 CG2 REMARK 470 LYS A 59 CG CD CE NZ REMARK 470 GLU A 62 CG CD OE1 OE2 REMARK 470 THR A 63 OG1 CG2 REMARK 470 LYS A 64 CE NZ REMARK 470 LYS A 65 CG CD CE NZ REMARK 470 HIS A 66 CG ND1 CD2 CE1 NE2 REMARK 470 VAL A 68 CG1 CG2 REMARK 470 ASP A 78 CG OD1 OD2 REMARK 470 ASN A 136 CG OD1 ND2 REMARK 470 ASN A 137 CG OD1 ND2 REMARK 470 ILE A 138 CG1 CG2 CD1 REMARK 470 THR A 139 OG1 CG2 REMARK 470 MET A 150 CG SD CE REMARK 470 ARG A 151 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 171 CG CD CE NZ REMARK 470 ASN A 195 CG OD1 ND2 REMARK 470 CYS A 501 SG REMARK 470 LYS A 502 CG CD CE NZ REMARK 470 ARG A 503 CG CD NE CZ NH1 NH2 REMARK 470 ARG A 504 CG CD NE CZ NH1 NH2 REMARK 470 LEU B 34 CG CD1 CD2 REMARK 470 LYS B 59 CG CD CE NZ REMARK 470 VAL B 68 CG1 CG2 REMARK 470 THR B 71 OG1 CG2 REMARK 470 HIS B 72 CG ND1 CD2 CE1 NE2 REMARK 470 CYS B 126 SG REMARK 470 GLN B 130 CG CD OE1 NE2 REMARK 470 CYS B 131 SG REMARK 470 ASN B 136 CG OD1 ND2 REMARK 470 ASN B 137 CG OD1 ND2 REMARK 470 ILE B 138 CG1 CG2 CD1 REMARK 470 ARG B 151 CG CD NE CZ NH1 NH2 REMARK 470 GLU B 153 CG CD OE1 OE2 REMARK 470 GLU B 211 CG CD OE1 OE2 REMARK 470 ARG B 500 CG CD NE CZ NH1 NH2 REMARK 470 CYS B 501 SG REMARK 470 LYS B 502 CG CD CE NZ REMARK 470 ARG B 503 CG CD NE CZ NH1 NH2 REMARK 470 ASP C 57 CG OD1 OD2 REMARK 470 ASP C 78 CG OD1 OD2 REMARK 470 VAL C 120 CG1 CG2 REMARK 470 LYS C 121 CG CD CE NZ REMARK 470 THR C 123 OG1 CG2 REMARK 470 LEU C 125 CG CD1 CD2 REMARK 470 VAL C 127 CG1 CG2 REMARK 470 ASN C 136 CG OD1 ND2 REMARK 470 ASN C 137 CG OD1 ND2 REMARK 470 ILE C 138 CG1 CG2 CD1 REMARK 470 THR C 139 OG1 CG2 REMARK 470 ARG C 151 CG CD NE CZ NH1 NH2 REMARK 470 LYS C 171 CG CD CE NZ REMARK 470 LYS C 232 CG CD CE NZ REMARK 470 ASN C 392 CG OD1 ND2 REMARK 470 LYS C 421 CG CD CE NZ REMARK 470 TYR C 484 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LYS C 485 CG CD CE NZ REMARK 470 ARG C 500 NE CZ NH1 NH2 REMARK 470 LYS C 502 CG CD CE NZ REMARK 470 ARG C 503 CG CD NE CZ NH1 NH2 REMARK 470 ARG C 504 CG CD NE CZ NH1 NH2 REMARK 470 GLN H 1 CG CD OE1 NE2 REMARK 470 LYS I 61 CG CD CE NZ REMARK 470 ASP I 97 CG OD1 OD2 REMARK 470 ARG I 98 CG CD NE CZ NH1 NH2 REMARK 470 ASP J 60 CG OD1 OD2 REMARK 470 TYR J 95B CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 GLU L 29 CG CD OE1 OE2 REMARK 470 GLN P 64 CG CD OE1 NE2 REMARK 470 ASP P 72 CG OD1 OD2 REMARK 470 LEU Q 95 CG CD1 CD2 REMARK 470 TYR Q 95B CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 THR X 536 OG1 CG2 REMARK 470 THR X 538 OG1 CG2 REMARK 470 VAL X 539 CG1 CG2 REMARK 470 HIS X 564 CG ND1 CD2 CE1 NE2 REMARK 470 LYS X 567 CG CD CE NZ REMARK 470 ARG X 588 CG CD NE CZ NH1 NH2 REMARK 470 ILE X 595 CG1 CG2 CD1 REMARK 470 ASN X 616 CG OD1 ND2 REMARK 470 GLU X 647 CG CD OE1 OE2 REMARK 470 LYS X 655 CG CD CE NZ REMARK 470 GLU X 657 CG CD OE1 OE2 REMARK 470 MET Y 535 CG SD CE REMARK 470 THR Y 536 OG1 CG2 REMARK 470 GLN Y 563 CG CD OE1 NE2 REMARK 470 LYS Y 567 CG CD CE NZ REMARK 470 TRP Y 571 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP Y 571 CZ3 CH2 REMARK 470 MET Z 535 CG SD CE REMARK 470 GLU Z 647 CG CD OE1 OE2 REMARK 470 GLU Z 648 CG CD OE1 OE2 REMARK 470 LEU Z 660 CG CD1 CD2 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 SG CYS Q 23 SG CYS Q 88 1.68 REMARK 500 ND2 ASN A 262 C1 NAG G 1 1.76 REMARK 500 NE2 GLN L 38 O MET L 42 2.12 REMARK 500 ND2 ASN A 276 O5 NAG F 1 2.14 REMARK 500 OG SER A 364 O THR A 372 2.17 REMARK 500 ND2 ASN A 386 O5 NAG D 1 2.17 REMARK 500 O LEU B 369 OG1 THR B 373 2.17 REMARK 500 OG SER L 12 OG1 THR L 105 2.19 REMARK 500 O PRO J 7 OG1 THR J 102 2.19 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 HIS A 66 -135.11 50.27 REMARK 500 VAL A 68 -13.38 -49.53 REMARK 500 PRO A 79 72.71 -67.35 REMARK 500 GLU A 83 43.17 38.51 REMARK 500 THR A 90 115.40 -161.51 REMARK 500 ASN A 195 82.79 -153.21 REMARK 500 CYS A 196 -60.45 -102.91 REMARK 500 GLN A 258 -34.82 -38.89 REMARK 500 ASN A 276 108.88 -162.78 REMARK 500 ALA A 316 111.07 -160.80 REMARK 500 THR A 373 -166.72 -117.26 REMARK 500 ASN A 386 157.99 -47.63 REMARK 500 LEU B 122 -61.55 -92.00 REMARK 500 GLN B 258 8.74 53.28 REMARK 500 GLU B 268 -166.17 -127.29 REMARK 500 THR B 278 -8.56 -55.70 REMARK 500 ALA B 362 -129.57 -138.44 REMARK 500 SER B 365 23.45 -58.62 REMARK 500 ASP B 368 -167.49 -77.35 REMARK 500 TRP B 427 45.88 -91.30 REMARK 500 GLN B 428 49.63 34.54 REMARK 500 SER B 463 -3.63 67.45 REMARK 500 PRO C 43 51.97 -97.12 REMARK 500 PHE C 53 -169.80 -79.54 REMARK 500 ASN C 88 60.85 60.32 REMARK 500 LYS C 97 30.20 -95.11 REMARK 500 ASN C 195 99.68 -160.24 REMARK 500 THR C 236 -169.08 -72.77 REMARK 500 SER C 241 32.30 -142.41 REMARK 500 GLN C 258 -11.23 72.46 REMARK 500 LEU C 260 101.77 -59.73 REMARK 500 LEU C 261 -76.09 -61.51 REMARK 500 ASN C 276 103.09 -164.29 REMARK 500 PHE C 288 -76.95 -85.65 REMARK 500 ASN C 289 -41.94 -145.31 REMARK 500 SER C 334 68.72 60.38 REMARK 500 SER C 364 -173.04 73.59 REMARK 500 ASP C 368 127.98 -170.11 REMARK 500 LEU C 390 -164.13 -77.68 REMARK 500 ALA C 436 76.77 55.13 REMARK 500 SER C 447 -63.35 -122.99 REMARK 500 ARG C 456 -174.59 -68.57 REMARK 500 PHE C 468 -120.29 61.64 REMARK 500 MET C 475 -1.93 -58.72 REMARK 500 ARG C 503 -107.06 54.23 REMARK 500 VAL H 48 -57.36 -127.24 REMARK 500 ARG H 98 -7.78 -54.32 REMARK 500 CYS J 23 115.71 -160.28 REMARK 500 TYR J 30 59.90 -90.05 REMARK 500 ASN J 51 -13.41 73.93 REMARK 500 REMARK 500 THIS ENTRY HAS 80 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 NAG G 1 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 7TFN RELATED DB: PDB REMARK 900 RELATED ID: EMD-25877 RELATED DB: EMDB REMARK 900 RELATED ID: EMD-25878 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF HIV-1 ENV TRIMER BG505 SOSIP.664 IN COMPLEX REMARK 900 WITH CD4BS ANTIBODY AB1573 DBREF1 7TFO A 31 511 UNP A0A6H1VH54_9PLVG DBREF2 7TFO A A0A6H1VH54 30 508 DBREF1 7TFO B 31 511 UNP A0A6H1VH54_9PLVG DBREF2 7TFO B A0A6H1VH54 30 508 DBREF1 7TFO C 31 511 UNP A0A6H1VH54_9PLVG DBREF2 7TFO C A0A6H1VH54 30 508 DBREF 7TFO H 1 219 PDB 7TFO 7TFO 1 219 DBREF 7TFO I 1 219 PDB 7TFO 7TFO 1 219 DBREF 7TFO J 1 213 PDB 7TFO 7TFO 1 213 DBREF 7TFO L 1 213 PDB 7TFO 7TFO 1 213 DBREF 7TFO P 1 219 PDB 7TFO 7TFO 1 219 DBREF 7TFO Q 1 213 PDB 7TFO 7TFO 1 213 DBREF 7TFO X 512 664 UNP Q2N0S6 Q2N0S6_9HIV1 509 661 DBREF 7TFO Y 512 664 UNP Q2N0S6 Q2N0S6_9HIV1 509 661 DBREF 7TFO Z 512 664 UNP Q2N0S6 Q2N0S6_9HIV1 509 661 SEQADV 7TFO LYS A 64 UNP A0A6H1VH5 GLU 63 CONFLICT SEQADV 7TFO SER A 375 UNP A0A6H1VH5 TYR 373 CONFLICT SEQADV 7TFO CYS A 501 UNP A0A6H1VH5 ALA 498 CONFLICT SEQADV 7TFO ARG A 509 UNP A0A6H1VH5 GLU 506 CONFLICT SEQADV 7TFO ARG A 512 UNP A0A6H1VH5 EXPRESSION TAG SEQADV 7TFO ARG A 513 UNP A0A6H1VH5 EXPRESSION TAG SEQADV 7TFO LYS B 64 UNP A0A6H1VH5 GLU 63 CONFLICT SEQADV 7TFO SER B 375 UNP A0A6H1VH5 TYR 373 CONFLICT SEQADV 7TFO CYS B 501 UNP A0A6H1VH5 ALA 498 CONFLICT SEQADV 7TFO ARG B 509 UNP A0A6H1VH5 GLU 506 CONFLICT SEQADV 7TFO ARG B 512 UNP A0A6H1VH5 EXPRESSION TAG SEQADV 7TFO ARG B 513 UNP A0A6H1VH5 EXPRESSION TAG SEQADV 7TFO LYS C 64 UNP A0A6H1VH5 GLU 63 CONFLICT SEQADV 7TFO SER C 375 UNP A0A6H1VH5 TYR 373 CONFLICT SEQADV 7TFO CYS C 501 UNP A0A6H1VH5 ALA 498 CONFLICT SEQADV 7TFO ARG C 509 UNP A0A6H1VH5 GLU 506 CONFLICT SEQADV 7TFO ARG C 512 UNP A0A6H1VH5 EXPRESSION TAG SEQADV 7TFO ARG C 513 UNP A0A6H1VH5 EXPRESSION TAG SEQADV 7TFO PRO X 559 UNP Q2N0S6 ILE 556 CONFLICT SEQADV 7TFO CYS X 605 UNP Q2N0S6 THR 602 CONFLICT SEQADV 7TFO PRO Y 559 UNP Q2N0S6 ILE 556 CONFLICT SEQADV 7TFO CYS Y 605 UNP Q2N0S6 THR 602 CONFLICT SEQADV 7TFO PRO Z 559 UNP Q2N0S6 ILE 556 CONFLICT SEQADV 7TFO CYS Z 605 UNP Q2N0S6 THR 602 CONFLICT SEQRES 1 A 481 ALA GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO SEQRES 2 A 481 VAL TRP LYS ASP ALA GLU THR THR LEU PHE CYS ALA SER SEQRES 3 A 481 ASP ALA LYS ALA TYR GLU THR LYS LYS HIS ASN VAL TRP SEQRES 4 A 481 ALA THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN SEQRES 5 A 481 GLU ILE HIS LEU GLU ASN VAL THR GLU GLU PHE ASN MET SEQRES 6 A 481 TRP LYS ASN ASN MET VAL GLU GLN MET HIS THR ASP ILE SEQRES 7 A 481 ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS SEQRES 8 A 481 LEU THR PRO LEU CYS VAL THR LEU GLN CYS THR ASN VAL SEQRES 9 A 481 THR ASN ASN ILE THR ASP ASP MET ARG GLY GLU LEU LYS SEQRES 10 A 481 ASN CYS SER PHE ASN MET THR THR GLU LEU ARG ASP LYS SEQRES 11 A 481 LYS GLN LYS VAL TYR SER LEU PHE TYR ARG LEU ASP VAL SEQRES 12 A 481 VAL GLN ILE ASN GLU ASN GLN GLY ASN ARG SER ASN ASN SEQRES 13 A 481 SER ASN LYS GLU TYR ARG LEU ILE ASN CYS ASN THR SER SEQRES 14 A 481 ALA ILE THR GLN ALA CYS PRO LYS VAL SER PHE GLU PRO SEQRES 15 A 481 ILE PRO ILE HIS TYR CYS ALA PRO ALA GLY PHE ALA ILE SEQRES 16 A 481 LEU LYS CYS LYS ASP LYS LYS PHE ASN GLY THR GLY PRO SEQRES 17 A 481 CYS PRO SER VAL SER THR VAL GLN CYS THR HIS GLY ILE SEQRES 18 A 481 LYS PRO VAL VAL SER THR GLN LEU LEU LEU ASN GLY SER SEQRES 19 A 481 LEU ALA GLU GLU GLU VAL MET ILE ARG SER GLU ASN ILE SEQRES 20 A 481 THR ASN ASN ALA LYS ASN ILE LEU VAL GLN PHE ASN THR SEQRES 21 A 481 PRO VAL GLN ILE ASN CYS THR ARG PRO ASN ASN ASN THR SEQRES 22 A 481 ARG LYS SER ILE ARG ILE GLY PRO GLY GLN ALA PHE TYR SEQRES 23 A 481 ALA THR GLY ASP ILE ILE GLY ASP ILE ARG GLN ALA HIS SEQRES 24 A 481 CYS ASN VAL SER LYS ALA THR TRP ASN GLU THR LEU GLY SEQRES 25 A 481 LYS VAL VAL LYS GLN LEU ARG LYS HIS PHE GLY ASN ASN SEQRES 26 A 481 THR ILE ILE ARG PHE ALA ASN SER SER GLY GLY ASP LEU SEQRES 27 A 481 GLU VAL THR THR HIS SER PHE ASN CYS GLY GLY GLU PHE SEQRES 28 A 481 PHE TYR CYS ASN THR SER GLY LEU PHE ASN SER THR TRP SEQRES 29 A 481 ILE SER ASN THR SER VAL GLN GLY SER ASN SER THR GLY SEQRES 30 A 481 SER ASN ASP SER ILE THR LEU PRO CYS ARG ILE LYS GLN SEQRES 31 A 481 ILE ILE ASN MET TRP GLN ARG ILE GLY GLN ALA MET TYR SEQRES 32 A 481 ALA PRO PRO ILE GLN GLY VAL ILE ARG CYS VAL SER ASN SEQRES 33 A 481 ILE THR GLY LEU ILE LEU THR ARG ASP GLY GLY SER THR SEQRES 34 A 481 ASN SER THR THR GLU THR PHE ARG PRO GLY GLY GLY ASP SEQRES 35 A 481 MET ARG ASP ASN TRP ARG SER GLU LEU TYR LYS TYR LYS SEQRES 36 A 481 VAL VAL LYS ILE GLU PRO LEU GLY VAL ALA PRO THR ARG SEQRES 37 A 481 CYS LYS ARG ARG VAL VAL GLY ARG ARG ARG ARG ARG ARG SEQRES 1 B 481 ALA GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO SEQRES 2 B 481 VAL TRP LYS ASP ALA GLU THR THR LEU PHE CYS ALA SER SEQRES 3 B 481 ASP ALA LYS ALA TYR GLU THR LYS LYS HIS ASN VAL TRP SEQRES 4 B 481 ALA THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN SEQRES 5 B 481 GLU ILE HIS LEU GLU ASN VAL THR GLU GLU PHE ASN MET SEQRES 6 B 481 TRP LYS ASN ASN MET VAL GLU GLN MET HIS THR ASP ILE SEQRES 7 B 481 ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS SEQRES 8 B 481 LEU THR PRO LEU CYS VAL THR LEU GLN CYS THR ASN VAL SEQRES 9 B 481 THR ASN ASN ILE THR ASP ASP MET ARG GLY GLU LEU LYS SEQRES 10 B 481 ASN CYS SER PHE ASN MET THR THR GLU LEU ARG ASP LYS SEQRES 11 B 481 LYS GLN LYS VAL TYR SER LEU PHE TYR ARG LEU ASP VAL SEQRES 12 B 481 VAL GLN ILE ASN GLU ASN GLN GLY ASN ARG SER ASN ASN SEQRES 13 B 481 SER ASN LYS GLU TYR ARG LEU ILE ASN CYS ASN THR SER SEQRES 14 B 481 ALA ILE THR GLN ALA CYS PRO LYS VAL SER PHE GLU PRO SEQRES 15 B 481 ILE PRO ILE HIS TYR CYS ALA PRO ALA GLY PHE ALA ILE SEQRES 16 B 481 LEU LYS CYS LYS ASP LYS LYS PHE ASN GLY THR GLY PRO SEQRES 17 B 481 CYS PRO SER VAL SER THR VAL GLN CYS THR HIS GLY ILE SEQRES 18 B 481 LYS PRO VAL VAL SER THR GLN LEU LEU LEU ASN GLY SER SEQRES 19 B 481 LEU ALA GLU GLU GLU VAL MET ILE ARG SER GLU ASN ILE SEQRES 20 B 481 THR ASN ASN ALA LYS ASN ILE LEU VAL GLN PHE ASN THR SEQRES 21 B 481 PRO VAL GLN ILE ASN CYS THR ARG PRO ASN ASN ASN THR SEQRES 22 B 481 ARG LYS SER ILE ARG ILE GLY PRO GLY GLN ALA PHE TYR SEQRES 23 B 481 ALA THR GLY ASP ILE ILE GLY ASP ILE ARG GLN ALA HIS SEQRES 24 B 481 CYS ASN VAL SER LYS ALA THR TRP ASN GLU THR LEU GLY SEQRES 25 B 481 LYS VAL VAL LYS GLN LEU ARG LYS HIS PHE GLY ASN ASN SEQRES 26 B 481 THR ILE ILE ARG PHE ALA ASN SER SER GLY GLY ASP LEU SEQRES 27 B 481 GLU VAL THR THR HIS SER PHE ASN CYS GLY GLY GLU PHE SEQRES 28 B 481 PHE TYR CYS ASN THR SER GLY LEU PHE ASN SER THR TRP SEQRES 29 B 481 ILE SER ASN THR SER VAL GLN GLY SER ASN SER THR GLY SEQRES 30 B 481 SER ASN ASP SER ILE THR LEU PRO CYS ARG ILE LYS GLN SEQRES 31 B 481 ILE ILE ASN MET TRP GLN ARG ILE GLY GLN ALA MET TYR SEQRES 32 B 481 ALA PRO PRO ILE GLN GLY VAL ILE ARG CYS VAL SER ASN SEQRES 33 B 481 ILE THR GLY LEU ILE LEU THR ARG ASP GLY GLY SER THR SEQRES 34 B 481 ASN SER THR THR GLU THR PHE ARG PRO GLY GLY GLY ASP SEQRES 35 B 481 MET ARG ASP ASN TRP ARG SER GLU LEU TYR LYS TYR LYS SEQRES 36 B 481 VAL VAL LYS ILE GLU PRO LEU GLY VAL ALA PRO THR ARG SEQRES 37 B 481 CYS LYS ARG ARG VAL VAL GLY ARG ARG ARG ARG ARG ARG SEQRES 1 C 481 ALA GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO SEQRES 2 C 481 VAL TRP LYS ASP ALA GLU THR THR LEU PHE CYS ALA SER SEQRES 3 C 481 ASP ALA LYS ALA TYR GLU THR LYS LYS HIS ASN VAL TRP SEQRES 4 C 481 ALA THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN SEQRES 5 C 481 GLU ILE HIS LEU GLU ASN VAL THR GLU GLU PHE ASN MET SEQRES 6 C 481 TRP LYS ASN ASN MET VAL GLU GLN MET HIS THR ASP ILE SEQRES 7 C 481 ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS SEQRES 8 C 481 LEU THR PRO LEU CYS VAL THR LEU GLN CYS THR ASN VAL SEQRES 9 C 481 THR ASN ASN ILE THR ASP ASP MET ARG GLY GLU LEU LYS SEQRES 10 C 481 ASN CYS SER PHE ASN MET THR THR GLU LEU ARG ASP LYS SEQRES 11 C 481 LYS GLN LYS VAL TYR SER LEU PHE TYR ARG LEU ASP VAL SEQRES 12 C 481 VAL GLN ILE ASN GLU ASN GLN GLY ASN ARG SER ASN ASN SEQRES 13 C 481 SER ASN LYS GLU TYR ARG LEU ILE ASN CYS ASN THR SER SEQRES 14 C 481 ALA ILE THR GLN ALA CYS PRO LYS VAL SER PHE GLU PRO SEQRES 15 C 481 ILE PRO ILE HIS TYR CYS ALA PRO ALA GLY PHE ALA ILE SEQRES 16 C 481 LEU LYS CYS LYS ASP LYS LYS PHE ASN GLY THR GLY PRO SEQRES 17 C 481 CYS PRO SER VAL SER THR VAL GLN CYS THR HIS GLY ILE SEQRES 18 C 481 LYS PRO VAL VAL SER THR GLN LEU LEU LEU ASN GLY SER SEQRES 19 C 481 LEU ALA GLU GLU GLU VAL MET ILE ARG SER GLU ASN ILE SEQRES 20 C 481 THR ASN ASN ALA LYS ASN ILE LEU VAL GLN PHE ASN THR SEQRES 21 C 481 PRO VAL GLN ILE ASN CYS THR ARG PRO ASN ASN ASN THR SEQRES 22 C 481 ARG LYS SER ILE ARG ILE GLY PRO GLY GLN ALA PHE TYR SEQRES 23 C 481 ALA THR GLY ASP ILE ILE GLY ASP ILE ARG GLN ALA HIS SEQRES 24 C 481 CYS ASN VAL SER LYS ALA THR TRP ASN GLU THR LEU GLY SEQRES 25 C 481 LYS VAL VAL LYS GLN LEU ARG LYS HIS PHE GLY ASN ASN SEQRES 26 C 481 THR ILE ILE ARG PHE ALA ASN SER SER GLY GLY ASP LEU SEQRES 27 C 481 GLU VAL THR THR HIS SER PHE ASN CYS GLY GLY GLU PHE SEQRES 28 C 481 PHE TYR CYS ASN THR SER GLY LEU PHE ASN SER THR TRP SEQRES 29 C 481 ILE SER ASN THR SER VAL GLN GLY SER ASN SER THR GLY SEQRES 30 C 481 SER ASN ASP SER ILE THR LEU PRO CYS ARG ILE LYS GLN SEQRES 31 C 481 ILE ILE ASN MET TRP GLN ARG ILE GLY GLN ALA MET TYR SEQRES 32 C 481 ALA PRO PRO ILE GLN GLY VAL ILE ARG CYS VAL SER ASN SEQRES 33 C 481 ILE THR GLY LEU ILE LEU THR ARG ASP GLY GLY SER THR SEQRES 34 C 481 ASN SER THR THR GLU THR PHE ARG PRO GLY GLY GLY ASP SEQRES 35 C 481 MET ARG ASP ASN TRP ARG SER GLU LEU TYR LYS TYR LYS SEQRES 36 C 481 VAL VAL LYS ILE GLU PRO LEU GLY VAL ALA PRO THR ARG SEQRES 37 C 481 CYS LYS ARG ARG VAL VAL GLY ARG ARG ARG ARG ARG ARG SEQRES 1 H 228 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 H 228 PRO GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 H 228 PHE THR PHE GLY ARG TYR SER PHE THR TRP VAL ARG GLN SEQRES 4 H 228 ALA PRO GLY GLN GLY LEU GLU TRP VAL GLY VAL ILE VAL SEQRES 5 H 228 PRO LEU VAL GLY VAL THR ASN SER ALA LYS LYS PHE GLN SEQRES 6 H 228 GLY ARG VAL THR ILE THR ALA ASP THR SER THR ASN THR SEQRES 7 H 228 VAL TYR MET ASP LEU SER SER LEU ARG SER GLU ASP THR SEQRES 8 H 228 ALA VAL TYR TYR CYS ALA ARG VAL GLY ASP ARG PHE GLY SEQRES 9 H 228 SER GLY TYR ALA MET ASP VAL TRP GLY ARG GLY ALA LEU SEQRES 10 H 228 VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL SEQRES 11 H 228 PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY SEQRES 12 H 228 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO SEQRES 13 H 228 GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SEQRES 14 H 228 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER SEQRES 15 H 228 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SEQRES 16 H 228 SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN SEQRES 17 H 228 HIS LYS PRO SER ASN THR LYS VAL ASP LYS ARG VAL GLU SEQRES 18 H 228 PRO LYS SER CYS ASP LYS THR SEQRES 1 I 228 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 I 228 PRO GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 I 228 PHE THR PHE GLY ARG TYR SER PHE THR TRP VAL ARG GLN SEQRES 4 I 228 ALA PRO GLY GLN GLY LEU GLU TRP VAL GLY VAL ILE VAL SEQRES 5 I 228 PRO LEU VAL GLY VAL THR ASN SER ALA LYS LYS PHE GLN SEQRES 6 I 228 GLY ARG VAL THR ILE THR ALA ASP THR SER THR ASN THR SEQRES 7 I 228 VAL TYR MET ASP LEU SER SER LEU ARG SER GLU ASP THR SEQRES 8 I 228 ALA VAL TYR TYR CYS ALA ARG VAL GLY ASP ARG PHE GLY SEQRES 9 I 228 SER GLY TYR ALA MET ASP VAL TRP GLY ARG GLY ALA LEU SEQRES 10 I 228 VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL SEQRES 11 I 228 PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY SEQRES 12 I 228 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO SEQRES 13 I 228 GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SEQRES 14 I 228 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER SEQRES 15 I 228 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SEQRES 16 I 228 SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN SEQRES 17 I 228 HIS LYS PRO SER ASN THR LYS VAL ASP LYS ARG VAL GLU SEQRES 18 I 228 PRO LYS SER CYS ASP LYS THR SEQRES 1 J 216 GLN SER ALA LEU THR GLN PRO PRO SER VAL SER GLY ALA SEQRES 2 J 216 PRO GLY GLU ARG VAL THR ILE SER CYS SER GLY SER GLY SEQRES 3 J 216 SER ASN PHE GLU TYR SER PHE VAL TYR TRP TYR GLN GLN SEQRES 4 J 216 VAL PRO GLY MET ALA PRO LYS LEU LEU ILE TYR ASP ASN SEQRES 5 J 216 TYR LYS ARG PRO SER GLY VAL SER ASP ARG PHE SER GLY SEQRES 6 J 216 SER ARG SER GLY THR SER ALA SER LEU THR ILE THR GLY SEQRES 7 J 216 LEU GLN THR GLU ASP GLU SER ASP TYR TYR CYS GLN SER SEQRES 8 J 216 TYR ASP SER SER LEU THR TYR TRP VAL PHE GLY GLY GLY SEQRES 9 J 216 THR ARG LEU THR VAL LEU GLY GLN PRO LYS ALA ALA PRO SEQRES 10 J 216 SER VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN SEQRES 11 J 216 ALA ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE SEQRES 12 J 216 TYR PRO GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER SEQRES 13 J 216 SER PRO VAL LYS ALA GLY VAL GLU THR THR THR PRO SER SEQRES 14 J 216 LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SEQRES 15 J 216 SER LEU THR PRO GLU GLN TRP LYS SER HIS ARG SER TYR SEQRES 16 J 216 SER CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS SEQRES 17 J 216 THR VAL ALA PRO THR GLU CYS SER SEQRES 1 L 216 GLN SER ALA LEU THR GLN PRO PRO SER VAL SER GLY ALA SEQRES 2 L 216 PRO GLY GLU ARG VAL THR ILE SER CYS SER GLY SER GLY SEQRES 3 L 216 SER ASN PHE GLU TYR SER PHE VAL TYR TRP TYR GLN GLN SEQRES 4 L 216 VAL PRO GLY MET ALA PRO LYS LEU LEU ILE TYR ASP ASN SEQRES 5 L 216 TYR LYS ARG PRO SER GLY VAL SER ASP ARG PHE SER GLY SEQRES 6 L 216 SER ARG SER GLY THR SER ALA SER LEU THR ILE THR GLY SEQRES 7 L 216 LEU GLN THR GLU ASP GLU SER ASP TYR TYR CYS GLN SER SEQRES 8 L 216 TYR ASP SER SER LEU THR TYR TRP VAL PHE GLY GLY GLY SEQRES 9 L 216 THR ARG LEU THR VAL LEU GLY GLN PRO LYS ALA ALA PRO SEQRES 10 L 216 SER VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN SEQRES 11 L 216 ALA ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE SEQRES 12 L 216 TYR PRO GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER SEQRES 13 L 216 SER PRO VAL LYS ALA GLY VAL GLU THR THR THR PRO SER SEQRES 14 L 216 LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SEQRES 15 L 216 SER LEU THR PRO GLU GLN TRP LYS SER HIS ARG SER TYR SEQRES 16 L 216 SER CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS SEQRES 17 L 216 THR VAL ALA PRO THR GLU CYS SER SEQRES 1 P 228 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 P 228 PRO GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 P 228 PHE THR PHE GLY ARG TYR SER PHE THR TRP VAL ARG GLN SEQRES 4 P 228 ALA PRO GLY GLN GLY LEU GLU TRP VAL GLY VAL ILE VAL SEQRES 5 P 228 PRO LEU VAL GLY VAL THR ASN SER ALA LYS LYS PHE GLN SEQRES 6 P 228 GLY ARG VAL THR ILE THR ALA ASP THR SER THR ASN THR SEQRES 7 P 228 VAL TYR MET ASP LEU SER SER LEU ARG SER GLU ASP THR SEQRES 8 P 228 ALA VAL TYR TYR CYS ALA ARG VAL GLY ASP ARG PHE GLY SEQRES 9 P 228 SER GLY TYR ALA MET ASP VAL TRP GLY ARG GLY ALA LEU SEQRES 10 P 228 VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL SEQRES 11 P 228 PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY SEQRES 12 P 228 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO SEQRES 13 P 228 GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SEQRES 14 P 228 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER SEQRES 15 P 228 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SEQRES 16 P 228 SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN SEQRES 17 P 228 HIS LYS PRO SER ASN THR LYS VAL ASP LYS ARG VAL GLU SEQRES 18 P 228 PRO LYS SER CYS ASP LYS THR SEQRES 1 Q 216 GLN SER ALA LEU THR GLN PRO PRO SER VAL SER GLY ALA SEQRES 2 Q 216 PRO GLY GLU ARG VAL THR ILE SER CYS SER GLY SER GLY SEQRES 3 Q 216 SER ASN PHE GLU TYR SER PHE VAL TYR TRP TYR GLN GLN SEQRES 4 Q 216 VAL PRO GLY MET ALA PRO LYS LEU LEU ILE TYR ASP ASN SEQRES 5 Q 216 TYR LYS ARG PRO SER GLY VAL SER ASP ARG PHE SER GLY SEQRES 6 Q 216 SER ARG SER GLY THR SER ALA SER LEU THR ILE THR GLY SEQRES 7 Q 216 LEU GLN THR GLU ASP GLU SER ASP TYR TYR CYS GLN SER SEQRES 8 Q 216 TYR ASP SER SER LEU THR TYR TRP VAL PHE GLY GLY GLY SEQRES 9 Q 216 THR ARG LEU THR VAL LEU GLY GLN PRO LYS ALA ALA PRO SEQRES 10 Q 216 SER VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN SEQRES 11 Q 216 ALA ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE SEQRES 12 Q 216 TYR PRO GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER SEQRES 13 Q 216 SER PRO VAL LYS ALA GLY VAL GLU THR THR THR PRO SER SEQRES 14 Q 216 LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SEQRES 15 Q 216 SER LEU THR PRO GLU GLN TRP LYS SER HIS ARG SER TYR SEQRES 16 Q 216 SER CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS SEQRES 17 Q 216 THR VAL ALA PRO THR GLU CYS SER SEQRES 1 X 153 ALA VAL GLY ILE GLY ALA VAL PHE LEU GLY PHE LEU GLY SEQRES 2 X 153 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 X 153 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 X 153 GLN GLN SER ASN LEU LEU ARG ALA PRO GLU ALA GLN GLN SEQRES 5 X 153 HIS LEU LEU LYS LEU THR VAL TRP GLY ILE LYS GLN LEU SEQRES 6 X 153 GLN ALA ARG VAL LEU ALA VAL GLU ARG TYR LEU ARG ASP SEQRES 7 X 153 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 X 153 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 X 153 ASN ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 X 153 LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE SEQRES 11 X 153 ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 X 153 LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP SEQRES 1 Y 153 ALA VAL GLY ILE GLY ALA VAL PHE LEU GLY PHE LEU GLY SEQRES 2 Y 153 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 Y 153 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 Y 153 GLN GLN SER ASN LEU LEU ARG ALA PRO GLU ALA GLN GLN SEQRES 5 Y 153 HIS LEU LEU LYS LEU THR VAL TRP GLY ILE LYS GLN LEU SEQRES 6 Y 153 GLN ALA ARG VAL LEU ALA VAL GLU ARG TYR LEU ARG ASP SEQRES 7 Y 153 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 Y 153 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 Y 153 ASN ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 Y 153 LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE SEQRES 11 Y 153 ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 Y 153 LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP SEQRES 1 Z 153 ALA VAL GLY ILE GLY ALA VAL PHE LEU GLY PHE LEU GLY SEQRES 2 Z 153 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 Z 153 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 Z 153 GLN GLN SER ASN LEU LEU ARG ALA PRO GLU ALA GLN GLN SEQRES 5 Z 153 HIS LEU LEU LYS LEU THR VAL TRP GLY ILE LYS GLN LEU SEQRES 6 Z 153 GLN ALA ARG VAL LEU ALA VAL GLU ARG TYR LEU ARG ASP SEQRES 7 Z 153 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 Z 153 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 Z 153 ASN ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 Z 153 LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE SEQRES 11 Z 153 ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 Z 153 LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP HET NAG A 601 14 HET NAG B 601 14 HET NAG B 602 14 HET NAG C 601 14 HET NAG C 602 14 HET NAG D 1 14 HET NAG D 2 14 HET NAG E 1 14 HET NAG E 2 14 HET BMA E 3 11 HET NAG F 1 14 HET NAG F 2 14 HET BMA F 3 11 HET NAG G 1 14 HET NAG G 2 14 HET BMA G 3 11 HET MAN G 4 11 HET MAN G 5 11 HET NAG K 1 14 HET NAG K 2 14 HET BMA K 3 11 HETNAM NAG N-ACETYL-D-GLUCOSAMINE HETNAM BMA BETA-D-MANNOSE HETNAM MAN ALPHA-D-MANNOSE FORMUL 13 NAG 15(C8 H15 N O6) FORMUL 19 BMA 4(C6 H12 O6) FORMUL 21 MAN 2(C6 H12 O6) HELIX 1 AA1 ASP A 57 THR A 63 1 7 HELIX 2 AA2 ASN A 98 LEU A 116 1 19 HELIX 3 AA3 SER A 334 PHE A 353 1 20 HELIX 4 AA4 ARG A 476 SER A 481 1 6 HELIX 5 AA5 GLU A 482 TYR A 484 5 3 HELIX 6 AA6 ASP B 57 TYR B 61 5 5 HELIX 7 AA7 ASN B 99 ASP B 113 1 15 HELIX 8 AA8 ILE B 194 SER B 199 1 6 HELIX 9 AA9 LYS B 335 GLY B 354 1 20 HELIX 10 AB1 ASP B 368 THR B 373 1 6 HELIX 11 AB2 MET B 475 ARG B 480 1 6 HELIX 12 AB3 MET C 100 SER C 115 1 16 HELIX 13 AB4 LEU C 122 CYS C 126 5 5 HELIX 14 AB5 TYR C 177 LEU C 179 5 3 HELIX 15 AB6 SER C 334 ARG C 350 1 17 HELIX 16 AB7 ASP C 368 THR C 373 1 6 HELIX 17 AB8 ASN C 425 ARG C 429 5 5 HELIX 18 AB9 ASP C 474 LEU C 483 1 10 HELIX 19 AC1 ARG H 83 THR H 87 5 5 HELIX 20 AC2 LYS I 61 GLN I 64 5 4 HELIX 21 AC3 ARG I 83 THR I 87 5 5 HELIX 22 AC4 GLN J 79 GLU J 83 5 5 HELIX 23 AC5 GLY L 27 SER L 31 5 7 HELIX 24 AC6 ARG P 83 THR P 87 5 5 HELIX 25 AC7 ASP P 97 SER P 100A 5 5 HELIX 26 AC8 SER Q 27A TYR Q 30 5 5 HELIX 27 AC9 GLN Q 79 GLU Q 83 5 5 HELIX 28 AD1 ILE X 515 PHE X 522 1 8 HELIX 29 AD2 THR X 529 ALA X 541 1 13 HELIX 30 AD3 HIS X 564 TRP X 596 1 33 HELIX 31 AD4 SER X 620 ASP X 624 5 5 HELIX 32 AD5 THR X 627 SER X 636 1 10 HELIX 33 AD6 TYR X 638 ASN X 656 1 19 HELIX 34 AD7 THR Y 529 THR Y 536 1 8 HELIX 35 AD8 GLN Y 540 LEU Y 545 5 6 HELIX 36 AD9 HIS Y 564 TRP Y 596 1 33 HELIX 37 AE1 ASN Y 618 TRP Y 623 1 6 HELIX 38 AE2 THR Y 627 SER Y 636 1 10 HELIX 39 AE3 ASN Y 637 GLU Y 654 1 18 HELIX 40 AE4 THR Z 529 GLN Z 540 1 12 HELIX 41 AE5 HIS Z 564 TRP Z 596 1 33 HELIX 42 AE6 ASN Z 618 ASN Z 625 1 8 HELIX 43 AE7 GLN Z 630 ILE Z 635 1 6 HELIX 44 AE8 TYR Z 638 LEU Z 660 1 23 SHEET 1 AA1 3 VAL A 496 ALA A 497 0 SHEET 2 AA1 3 TRP A 35 TYR A 39 -1 N THR A 37 O ALA A 497 SHEET 3 AA1 3 ILE X 603 PRO X 609 -1 O CYS X 604 N VAL A 38 SHEET 1 AA2 5 TRP A 45 ASP A 47 0 SHEET 2 AA2 5 TYR A 486 ILE A 491 -1 O LYS A 490 N LYS A 46 SHEET 3 AA2 5 PHE A 223 CYS A 228 -1 N ALA A 224 O VAL A 489 SHEET 4 AA2 5 VAL A 242 VAL A 245 -1 O SER A 243 N LYS A 227 SHEET 5 AA2 5 ILE A 84 HIS A 85 -1 N ILE A 84 O THR A 244 SHEET 1 AA3 2 PHE A 53 ALA A 55 0 SHEET 2 AA3 2 HIS A 216 CYS A 218 -1 O HIS A 216 N ALA A 55 SHEET 1 AA4 2 GLU A 91 PHE A 93 0 SHEET 2 AA4 2 GLY A 237 CYS A 239 -1 N CYS A 239 O GLU A 91 SHEET 1 AA5 2 LEU A 154 PHE A 159 0 SHEET 2 AA5 2 VAL A 172 TYR A 177 -1 O SER A 174 N CYS A 157 SHEET 1 AA6 2 VAL A 181 GLN A 183 0 SHEET 2 AA6 2 TYR A 191 LEU A 193 -1 O ARG A 192 N VAL A 182 SHEET 1 AA7 3 ALA A 200 GLN A 203 0 SHEET 2 AA7 3 GLN A 432 TYR A 435 1 O ALA A 433 N THR A 202 SHEET 3 AA7 3 ILE A 423 ILE A 424 -1 N ILE A 424 O MET A 434 SHEET 1 AA810 LEU A 259 LEU A 261 0 SHEET 2 AA810 MET A 271 ARG A 273 0 SHEET 3 AA810 ILE A 284 ILE A 307 -1 O LEU A 285 N ARG A 273 SHEET 4 AA810 PHE A 317 ILE A 323 -1 O GLY A 321 N THR A 303 SHEET 5 AA810 HIS A 330 VAL A 333 -1 O ASN A 332 N ASN A 295 SHEET 6 AA810 HIS A 374 CYS A 378 0 SHEET 7 AA810 GLU A 381 CYS A 385 -1 O CYS A 385 N HIS A 374 SHEET 8 AA810 ILE A 414 LYS A 421 -1 O ARG A 419 N TYR A 384 SHEET 9 AA810 GLY A 441 ARG A 456 -1 O THR A 450 N PHE A 288 SHEET 10 AA810 PHE A 468 PRO A 470 -1 O ARG A 469 N THR A 455 SHEET 1 AA9 2 ILE A 359 PHE A 361 0 SHEET 2 AA9 2 SER A 393 TRP A 395 -1 O TRP A 395 N ILE A 359 SHEET 1 AB1 3 GLY B 495 THR B 499 0 SHEET 2 AB1 3 TRP B 35 TYR B 39 -1 N TRP B 35 O THR B 499 SHEET 3 AB1 3 CYS Y 604 PRO Y 609 -1 O VAL Y 608 N VAL B 36 SHEET 1 AB2 5 TRP B 45 ASP B 47 0 SHEET 2 AB2 5 TYR B 486 ILE B 491 -1 O LYS B 490 N LYS B 46 SHEET 3 AB2 5 PHE B 223 CYS B 228 -1 N ALA B 224 O VAL B 489 SHEET 4 AB2 5 VAL B 242 VAL B 245 -1 O VAL B 245 N ILE B 225 SHEET 5 AB2 5 GLU B 83 HIS B 85 -1 N ILE B 84 O THR B 244 SHEET 1 AB3 2 GLU B 91 ASN B 94 0 SHEET 2 AB3 2 THR B 236 CYS B 239 -1 O CYS B 239 N GLU B 91 SHEET 1 AB4 3 CYS B 131 ASN B 133 0 SHEET 2 AB4 3 LYS B 155 SER B 158 -1 O ASN B 156 N THR B 132 SHEET 3 AB4 3 TYR B 173 PHE B 176 -1 O SER B 174 N CYS B 157 SHEET 1 AB5 2 VAL B 181 GLN B 183 0 SHEET 2 AB5 2 TYR B 191 LEU B 193 -1 O ARG B 192 N VAL B 182 SHEET 1 AB6 7 LEU B 259 LEU B 261 0 SHEET 2 AB6 7 ILE B 272 ARG B 273 0 SHEET 3 AB6 7 ILE B 284 GLN B 287 -1 O LEU B 285 N ARG B 273 SHEET 4 AB6 7 ILE B 358 PHE B 361 0 SHEET 5 AB6 7 THR B 394 TRP B 395 -1 O TRP B 395 N ILE B 359 SHEET 6 AB6 7 ILE B 449 ARG B 456 -1 O LEU B 454 N ILE B 284 SHEET 7 AB6 7 THR B 465 PRO B 470 -1 O ARG B 469 N THR B 455 SHEET 1 AB7 2 ILE B 294 THR B 297 0 SHEET 2 AB7 2 HIS B 330 VAL B 333 -1 O ASN B 332 N ASN B 295 SHEET 1 AB8 2 HIS B 374 CYS B 378 0 SHEET 2 AB8 2 GLU B 381 CYS B 385 -1 O CYS B 385 N HIS B 374 SHEET 1 AB9 2 LEU C 34 VAL C 38 0 SHEET 2 AB9 2 VAL C 496 ARG C 500 -1 O THR C 499 N TRP C 35 SHEET 1 AC1 2 TRP C 45 ASP C 47 0 SHEET 2 AC1 2 VAL C 489 ILE C 491 -1 O LYS C 490 N LYS C 46 SHEET 1 AC2 2 ILE C 84 HIS C 85 0 SHEET 2 AC2 2 SER C 243 THR C 244 -1 O THR C 244 N ILE C 84 SHEET 1 AC3 3 GLN C 130 ASN C 133 0 SHEET 2 AC3 3 LYS C 155 PHE C 159 -1 O ASN C 156 N THR C 132 SHEET 3 AC3 3 VAL C 172 PHE C 176 -1 O SER C 174 N CYS C 157 SHEET 1 AC4 2 VAL C 181 VAL C 182 0 SHEET 2 AC4 2 ARG C 192 LEU C 193 -1 O ARG C 192 N VAL C 182 SHEET 1 AC5 4 LEU C 259 LEU C 260 0 SHEET 2 AC5 4 GLY C 451 LEU C 454 -1 O GLY C 451 N LEU C 260 SHEET 3 AC5 4 ILE C 284 GLN C 287 -1 N ILE C 284 O LEU C 454 SHEET 4 AC5 4 MET C 271 ARG C 273 -1 N ARG C 273 O LEU C 285 SHEET 1 AC6 3 CYS C 331 ASN C 332 0 SHEET 2 AC6 3 ASN C 295 ASN C 302 -1 N ASN C 295 O ASN C 332 SHEET 3 AC6 3 GLY C 441 CYS C 445 -1 O GLY C 441 N ASN C 302 SHEET 1 AC7 3 PHE C 376 CYS C 378 0 SHEET 2 AC7 3 GLU C 381 TYR C 384 -1 O GLU C 381 N CYS C 378 SHEET 3 AC7 3 ARG C 419 ILE C 420 -1 O ARG C 419 N TYR C 384 SHEET 1 AC8 4 VAL H 5 GLN H 6 0 SHEET 2 AC8 4 SER H 17 LYS H 23 -1 O LYS H 23 N VAL H 5 SHEET 3 AC8 4 THR H 77 SER H 82A-1 O MET H 80 N VAL H 20 SHEET 4 AC8 4 VAL H 67 ASP H 72 -1 N THR H 68 O ASP H 81 SHEET 1 AC9 6 GLU H 10 LYS H 12 0 SHEET 2 AC9 6 ALA H 107 VAL H 111 1 O THR H 110 N LYS H 12 SHEET 3 AC9 6 ALA H 88 VAL H 95 -1 N TYR H 90 O ALA H 107 SHEET 4 AC9 6 SER H 33 GLN H 39 -1 N VAL H 37 O TYR H 91 SHEET 5 AC9 6 GLU H 46 VAL H 52 -1 O GLU H 46 N ARG H 38 SHEET 6 AC9 6 VAL H 56 SER H 59 -1 O VAL H 56 N VAL H 52 SHEET 1 AD1 4 GLN I 3 GLN I 6 0 SHEET 2 AD1 4 VAL I 18 SER I 25 -1 O SER I 25 N GLN I 3 SHEET 3 AD1 4 THR I 77 LEU I 82 -1 O VAL I 78 N CYS I 22 SHEET 4 AD1 4 VAL I 67 ASP I 72 -1 N THR I 70 O TYR I 79 SHEET 1 AD2 7 GLU I 10 LYS I 12 0 SHEET 2 AD2 7 SER I 33 GLN I 39 0 SHEET 3 AD2 7 LEU I 45 VAL I 52 -1 O GLY I 49 N TRP I 36 SHEET 4 AD2 7 VAL I 56 SER I 59 -1 O ASN I 58 N VAL I 50 SHEET 5 AD2 7 ALA I 88 VAL I 95 -1 O TYR I 91 N VAL I 37 SHEET 6 AD2 7 MET I 100E TRP I 103 -1 O ASP I 101 N ARG I 94 SHEET 7 AD2 7 ALA I 107 VAL I 111 -1 O ALA I 107 N TYR I 90 SHEET 1 AD3 4 LEU J 4 THR J 5 0 SHEET 2 AD3 4 VAL J 19 GLY J 25 -1 O SER J 24 N THR J 5 SHEET 3 AD3 4 SER J 70 ILE J 75 -1 O ALA J 71 N CYS J 23 SHEET 4 AD3 4 SER J 63 ARG J 66 -1 N SER J 65 O SER J 72 SHEET 1 AD4 2 SER J 9 GLY J 13 0 SHEET 2 AD4 2 ARG J 103 VAL J 106 1 O THR J 105 N GLY J 13 SHEET 1 AD5 4 PRO J 44 ILE J 48 0 SHEET 2 AD5 4 PHE J 32 GLN J 38 -1 N GLN J 37 O LYS J 45 SHEET 3 AD5 4 ASP J 85 TYR J 91 -1 O GLN J 89 N TYR J 34 SHEET 4 AD5 4 VAL J 97 PHE J 98 -1 O VAL J 97 N SER J 90 SHEET 1 AD6 4 ALA L 3 THR L 5 0 SHEET 2 AD6 4 VAL L 19 SER L 26 -1 O SER L 24 N THR L 5 SHEET 3 AD6 4 SER L 70 ILE L 75 -1 O ALA L 71 N CYS L 23 SHEET 4 AD6 4 PHE L 62 SER L 67 -1 N SER L 67 O SER L 70 SHEET 1 AD7 5 SER L 9 GLY L 13 0 SHEET 2 AD7 5 THR L 102 VAL L 106 1 O ARG L 103 N VAL L 11 SHEET 3 AD7 5 ASP L 85 GLN L 89 -1 N TYR L 86 O THR L 102 SHEET 4 AD7 5 TYR L 34 GLN L 38 -1 N TYR L 34 O GLN L 89 SHEET 5 AD7 5 PRO L 44 ILE L 48 -1 O LYS L 45 N GLN L 37 SHEET 1 AD8 4 GLN P 3 GLN P 6 0 SHEET 2 AD8 4 VAL P 18 SER P 25 -1 O SER P 25 N GLN P 3 SHEET 3 AD8 4 THR P 77 LEU P 82 -1 O LEU P 82 N VAL P 18 SHEET 4 AD8 4 THR P 68 ASP P 72 -1 N THR P 70 O TYR P 79 SHEET 1 AD9 7 GLU P 10 VAL P 11 0 SHEET 2 AD9 7 SER P 33 GLN P 39 0 SHEET 3 AD9 7 LEU P 45 ILE P 51 -1 O ILE P 51 N PHE P 34 SHEET 4 AD9 7 THR P 57 SER P 59 -1 O ASN P 58 N VAL P 50 SHEET 5 AD9 7 ALA P 88 VAL P 95 -1 O VAL P 95 N SER P 33 SHEET 6 AD9 7 MET P 100E TRP P 103 -1 O VAL P 102 N ARG P 94 SHEET 7 AD9 7 ALA P 107 THR P 110 -1 O ALA P 107 N TYR P 90 SHEET 1 AE1 5 SER Q 9 SER Q 12 0 SHEET 2 AE1 5 THR Q 102 THR Q 105 1 O ARG Q 103 N VAL Q 11 SHEET 3 AE1 5 SER Q 84 TYR Q 87 -1 N TYR Q 86 O THR Q 102 SHEET 4 AE1 5 TRP Q 35 GLN Q 38 -1 N TYR Q 36 O TYR Q 87 SHEET 5 AE1 5 LYS Q 45 ILE Q 48 -1 O LYS Q 45 N GLN Q 37 SHEET 1 AE2 3 VAL Q 19 CYS Q 23 0 SHEET 2 AE2 3 SER Q 70 ILE Q 75 -1 O ALA Q 71 N CYS Q 23 SHEET 3 AE2 3 SER Q 63 SER Q 67 -1 N SER Q 67 O SER Q 70 SHEET 1 AE3 2 GLN Q 89 ASP Q 92 0 SHEET 2 AE3 2 TYR Q 95B PHE Q 98 -1 O TYR Q 95B N ASP Q 92 SSBOND 1 CYS A 54 CYS A 74 1555 1555 2.03 SSBOND 2 CYS A 119 CYS A 205 1555 1555 2.03 SSBOND 3 CYS A 126 CYS A 196 1555 1555 2.03 SSBOND 4 CYS A 131 CYS A 157 1555 1555 2.03 SSBOND 5 CYS A 218 CYS A 247 1555 1555 2.03 SSBOND 6 CYS A 228 CYS A 239 1555 1555 2.03 SSBOND 7 CYS A 296 CYS A 331 1555 1555 2.04 SSBOND 8 CYS A 378 CYS A 445 1555 1555 2.03 SSBOND 9 CYS A 385 CYS A 418 1555 1555 2.03 SSBOND 10 CYS B 119 CYS B 205 1555 1555 2.03 SSBOND 11 CYS B 218 CYS B 247 1555 1555 2.03 SSBOND 12 CYS B 228 CYS B 239 1555 1555 2.03 SSBOND 13 CYS B 296 CYS B 331 1555 1555 2.03 SSBOND 14 CYS B 331 CYS B 418 1555 1555 2.03 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 C 126 CYS C 196 1555 1555 2.03 SSBOND 18 CYS C 131 CYS C 157 1555 1555 2.03 SSBOND 19 CYS C 228 CYS C 239 1555 1555 2.03 SSBOND 20 CYS C 296 CYS C 331 1555 1555 2.03 SSBOND 21 CYS C 378 CYS C 445 1555 1555 2.03 SSBOND 22 CYS C 385 CYS C 418 1555 1555 2.04 SSBOND 23 CYS H 22 CYS H 92 1555 1555 2.03 SSBOND 24 CYS I 22 CYS I 92 1555 1555 2.03 SSBOND 25 CYS J 23 CYS J 88 1555 1555 2.03 SSBOND 26 CYS L 23 CYS L 88 1555 1555 2.03 SSBOND 27 CYS P 22 CYS P 92 1555 1555 2.03 SSBOND 28 CYS X 598 CYS X 604 1555 1555 2.03 SSBOND 29 CYS Y 598 CYS Y 604 1555 1555 2.03 SSBOND 30 CYS Z 598 CYS Z 604 1555 1555 2.03 LINK ND2 ASN A 197 C1 NAG A 601 1555 1555 1.44 LINK ND2 ASN A 276 C1 NAG F 1 1555 1555 1.51 LINK ND2 ASN A 363 C1 NAG E 1 1555 1555 1.44 LINK ND2 ASN A 386 C1 NAG D 1 1555 1555 1.43 LINK ND2 ASN B 276 C1 NAG B 601 1555 1555 1.44 LINK ND2 ASN B 363 C1 NAG B 602 1555 1555 1.44 LINK ND2 ASN C 197 C1 NAG C 601 1555 1555 1.43 LINK ND2 ASN C 276 C1 NAG K 1 1555 1555 1.42 LINK ND2 ASN C 363 C1 NAG C 602 1555 1555 1.44 LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.44 LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.44 LINK O4 NAG E 2 C1 BMA E 3 1555 1555 1.44 LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.44 LINK O4 NAG F 2 C1 BMA F 3 1555 1555 1.44 LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.45 LINK O4 NAG G 2 C1 BMA G 3 1555 1555 1.44 LINK O3 BMA G 3 C1 MAN G 4 1555 1555 1.44 LINK O6 BMA G 3 C1 MAN G 5 1555 1555 1.44 LINK O4 NAG K 1 C1 NAG K 2 1555 1555 1.44 LINK O4 NAG K 2 C1 BMA K 3 1555 1555 1.44 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