HEADER VIRAL PROTEIN/IMMUNE SYSTEM 14-DEC-21 7T73 TITLE HIV-1 ENVELOPE APEXGT2.2MUT IN COMPLEX WITH PCT64.LMCA FAB CAVEAT 7T73 NAG F 701 HAS WRONG CHIRALITY AT ATOM C1 COMPND MOL_ID: 1; COMPND 2 MOLECULE: PCT64.LMCA FAB HEAVY CHAIN; COMPND 3 CHAIN: H; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: PCT64.LMCA FAB LIGHT CHAIN; COMPND 7 CHAIN: L; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: HIV ENVELOPE APEXGT2.2MUT GP120; COMPND 11 CHAIN: A, C, E; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 4; COMPND 14 MOLECULE: HIV ENVELOPE APEXGT2.2MUT GP41; COMPND 15 CHAIN: B, D, F; COMPND 16 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 CELL_LINE: HEK; SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 7 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: HEK; SOURCE 10 MOL_ID: 2; SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 12 ORGANISM_COMMON: HUMAN; SOURCE 13 ORGANISM_TAXID: 9606; SOURCE 14 CELL_LINE: HEK; SOURCE 15 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 16 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 18 EXPRESSION_SYSTEM_CELL_LINE: HEK; SOURCE 19 MOL_ID: 3; SOURCE 20 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 21 ORGANISM_COMMON: HIV-1; SOURCE 22 ORGANISM_TAXID: 11676; SOURCE 23 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 24 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 25 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 26 EXPRESSION_SYSTEM_CELL_LINE: HEK; SOURCE 27 MOL_ID: 4; SOURCE 28 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 29 ORGANISM_COMMON: HIV-1; SOURCE 30 ORGANISM_TAXID: 11676; SOURCE 31 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 32 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 33 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 34 EXPRESSION_SYSTEM_CELL_LINE: HEK KEYWDS HIV, GERMLINE TARGETING VACCINE, VIRAL PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR Z.T.BERNDSEN JRNL AUTH J.R.WILLIS,Z.T.BERNDSEN,K.M.MA,J.M.STEICHEN,T.SCHIFNER, JRNL AUTH 2 E.LANDAIS,A.LIGUORI,O.KALYUZHNIY,J.D.ALLEN,S.BABOO, JRNL AUTH 3 O.OMORODION,J.K.DIEDRICH,X.HU,E.GEORGESON,N.PHELPS, JRNL AUTH 4 S.ESKANDARZADEH,B.GROSCHEL,M.KUBITZ,Y.ADACHI,T.M.MULLIN, JRNL AUTH 5 N.ALAVI,S.FALCONE,S.HIMANSU,A.CARFI,I.A.WILSON, JRNL AUTH 6 J.R.YATES III,J.C.PAULSON,M.CRISPIN,A.B.WARD,W.SCHIEF JRNL TITL HUMAN IMMUNOGLOBULIN REPERTOIRE ANALYSIS GUIDES DESIGN OF JRNL TITL 2 VACCINE PRIMING IMMUNOGENS TARGETING HIV V2-APEX BROADLY JRNL TITL 3 NEUTRALIZING ANTIBODY PRECURSORS JRNL REF IMMUNITY 2022 JRNL REFN ISSN 1074-7613 REMARK 2 REMARK 2 RESOLUTION. 4.00 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) : 4.000 REMARK 3 NUMBER OF PARTICLES : 238078 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 7T73 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_1000259198. 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 ENVELOPE APEXGT2.2MUT IN REMARK 245 COMPLEX WITH PCT64.LMCA 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 : 7.40 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 TALOS ARCTICA REMARK 245 DETECTOR TYPE : GATAN K2 SUMMIT (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1000.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2500.00 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) : 50.00 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) : 200 REMARK 245 IMAGING DETAILS : NULL REMARK 247 REMARK 247 ELECTRON MICROSCOPY REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION REMARK 247 OF THE STRUCTURE FACTORS. REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: OCTAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L, A, B, C, E, D, F, G, I, REMARK 350 AND CHAINS: J, K, M, N, O, P, Q, R, S, REMARK 350 AND CHAINS: T, U, V REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 SER H 112 REMARK 465 SER H 113 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 LYS 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 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 GLU L 213 REMARK 465 CYS L 214 REMARK 465 MET A 0 REMARK 465 GLY A 1 REMARK 465 ILE A 2 REMARK 465 LEU A 3 REMARK 465 PRO A 4 REMARK 465 SER A 5 REMARK 465 PRO A 6 REMARK 465 GLY A 7 REMARK 465 MET A 8 REMARK 465 PRO A 9 REMARK 465 ALA A 10 REMARK 465 LEU A 11 REMARK 465 LEU A 12 REMARK 465 SER A 13 REMARK 465 LEU A 14 REMARK 465 VAL A 15 REMARK 465 SER A 16 REMARK 465 LEU A 17 REMARK 465 LEU A 18 REMARK 465 SER A 19 REMARK 465 VAL A 20 REMARK 465 LEU A 21 REMARK 465 LEU A 22 REMARK 465 MET A 23 REMARK 465 GLY A 24 REMARK 465 CYS A 25 REMARK 465 VAL A 26 REMARK 465 ALA A 27 REMARK 465 GLU A 28 REMARK 465 THR A 29 REMARK 465 GLY A 30 REMARK 465 ALA A 31 REMARK 465 ALA A 58 REMARK 465 LYS A 59 REMARK 465 ALA A 60 REMARK 465 TYR A 61 REMARK 465 GLU A 62 REMARK 465 THR A 63 REMARK 465 GLU A 64 REMARK 465 LYS A 65 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 LYS A 502 REMARK 465 ARG A 503 REMARK 465 ARG A 504 REMARK 465 VAL A 505 REMARK 465 VAL A 506 REMARK 465 GLY A 507 REMARK 465 ARG A 508 REMARK 465 ARG A 509 REMARK 465 ARG A 510 REMARK 465 ARG A 511 REMARK 465 ARG A 512 REMARK 465 ARG A 513 REMARK 465 ALA B 512 REMARK 465 VAL B 513 REMARK 465 GLY B 514 REMARK 465 ILE B 515 REMARK 465 GLY B 516 REMARK 465 ALA B 517 REMARK 465 VAL B 518 REMARK 465 SER B 519 REMARK 465 GLY B 547 REMARK 465 ILE B 548 REMARK 465 VAL B 549 REMARK 465 GLN B 550 REMARK 465 GLN B 551 REMARK 465 GLN B 552 REMARK 465 SER B 553 REMARK 465 ASN B 554 REMARK 465 LEU B 555 REMARK 465 LEU B 556 REMARK 465 ARG B 557 REMARK 465 ALA B 558 REMARK 465 PRO B 559 REMARK 465 GLU B 560 REMARK 465 PRO B 561 REMARK 465 GLN B 562 REMARK 465 GLN B 563 REMARK 465 HIS B 564 REMARK 465 LEU B 565 REMARK 465 LEU B 566 REMARK 465 LYS B 567 REMARK 465 ASP B 568 REMARK 465 THR B 569 REMARK 465 HIS B 570 REMARK 465 TRP B 571 REMARK 465 LEU B 663 REMARK 465 ASP B 664 REMARK 465 GLY B 665 REMARK 465 THR B 666 REMARK 465 LYS B 667 REMARK 465 HIS B 668 REMARK 465 HIS B 669 REMARK 465 HIS B 670 REMARK 465 HIS B 671 REMARK 465 HIS B 672 REMARK 465 HIS B 673 REMARK 465 MET C 0 REMARK 465 GLY C 1 REMARK 465 ILE C 2 REMARK 465 LEU C 3 REMARK 465 PRO C 4 REMARK 465 SER C 5 REMARK 465 PRO C 6 REMARK 465 GLY C 7 REMARK 465 MET C 8 REMARK 465 PRO C 9 REMARK 465 ALA C 10 REMARK 465 LEU C 11 REMARK 465 LEU C 12 REMARK 465 SER C 13 REMARK 465 LEU C 14 REMARK 465 VAL C 15 REMARK 465 SER C 16 REMARK 465 LEU C 17 REMARK 465 LEU C 18 REMARK 465 SER C 19 REMARK 465 VAL C 20 REMARK 465 LEU C 21 REMARK 465 LEU C 22 REMARK 465 MET C 23 REMARK 465 GLY C 24 REMARK 465 CYS C 25 REMARK 465 VAL C 26 REMARK 465 ALA C 27 REMARK 465 GLU C 28 REMARK 465 THR C 29 REMARK 465 GLY C 30 REMARK 465 ALA C 31 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 TRP C 69 REMARK 465 ALA C 70 REMARK 465 THR C 71 REMARK 465 HIS C 72 REMARK 465 ALA C 73 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 LYS C 502 REMARK 465 ARG C 503 REMARK 465 ARG C 504 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 MET E 0 REMARK 465 GLY E 1 REMARK 465 ILE E 2 REMARK 465 LEU E 3 REMARK 465 PRO E 4 REMARK 465 SER E 5 REMARK 465 PRO E 6 REMARK 465 GLY E 7 REMARK 465 MET E 8 REMARK 465 PRO E 9 REMARK 465 ALA E 10 REMARK 465 LEU E 11 REMARK 465 LEU E 12 REMARK 465 SER E 13 REMARK 465 LEU E 14 REMARK 465 VAL E 15 REMARK 465 SER E 16 REMARK 465 LEU E 17 REMARK 465 LEU E 18 REMARK 465 SER E 19 REMARK 465 VAL E 20 REMARK 465 LEU E 21 REMARK 465 LEU E 22 REMARK 465 MET E 23 REMARK 465 GLY E 24 REMARK 465 CYS E 25 REMARK 465 VAL E 26 REMARK 465 ALA E 27 REMARK 465 GLU E 28 REMARK 465 THR E 29 REMARK 465 GLY E 30 REMARK 465 ALA E 31 REMARK 465 ALA E 58 REMARK 465 LYS E 59 REMARK 465 ALA E 60 REMARK 465 TYR E 61 REMARK 465 GLU E 62 REMARK 465 THR E 63 REMARK 465 GLU E 64 REMARK 465 LYS E 65 REMARK 465 THR E 400 REMARK 465 SER E 401 REMARK 465 VAL E 402 REMARK 465 GLN E 403 REMARK 465 GLY E 404 REMARK 465 SER E 405 REMARK 465 ASN E 406 REMARK 465 SER E 407 REMARK 465 THR E 408 REMARK 465 GLY E 409 REMARK 465 SER E 410 REMARK 465 LYS E 502 REMARK 465 ARG E 503 REMARK 465 ARG E 504 REMARK 465 VAL E 505 REMARK 465 VAL E 506 REMARK 465 GLY E 507 REMARK 465 ARG E 508 REMARK 465 ARG E 509 REMARK 465 ARG E 510 REMARK 465 ARG E 511 REMARK 465 ARG E 512 REMARK 465 ARG E 513 REMARK 465 ALA D 512 REMARK 465 VAL D 513 REMARK 465 GLY D 514 REMARK 465 ILE D 515 REMARK 465 GLY D 516 REMARK 465 ALA D 517 REMARK 465 VAL D 518 REMARK 465 SER D 519 REMARK 465 GLY D 547 REMARK 465 ILE D 548 REMARK 465 VAL D 549 REMARK 465 GLN D 550 REMARK 465 GLN D 551 REMARK 465 GLN D 552 REMARK 465 SER D 553 REMARK 465 ASN D 554 REMARK 465 LEU D 555 REMARK 465 LEU D 556 REMARK 465 ARG D 557 REMARK 465 ALA D 558 REMARK 465 PRO D 559 REMARK 465 GLU D 560 REMARK 465 PRO 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 ASP D 568 REMARK 465 THR D 569 REMARK 465 HIS D 570 REMARK 465 TRP D 571 REMARK 465 LEU D 663 REMARK 465 ASP D 664 REMARK 465 GLY D 665 REMARK 465 THR D 666 REMARK 465 LYS D 667 REMARK 465 HIS D 668 REMARK 465 HIS D 669 REMARK 465 HIS D 670 REMARK 465 HIS D 671 REMARK 465 HIS D 672 REMARK 465 HIS D 673 REMARK 465 ALA F 512 REMARK 465 VAL F 513 REMARK 465 GLY F 514 REMARK 465 ILE F 515 REMARK 465 GLY F 516 REMARK 465 ALA F 517 REMARK 465 VAL F 518 REMARK 465 SER F 519 REMARK 465 GLY F 547 REMARK 465 ILE F 548 REMARK 465 VAL F 549 REMARK 465 GLN F 550 REMARK 465 GLN F 551 REMARK 465 GLN F 552 REMARK 465 SER F 553 REMARK 465 ASN F 554 REMARK 465 LEU F 555 REMARK 465 LEU F 556 REMARK 465 ARG F 557 REMARK 465 ALA F 558 REMARK 465 PRO F 559 REMARK 465 GLU F 560 REMARK 465 PRO 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 LYS F 567 REMARK 465 ASP F 568 REMARK 465 THR F 569 REMARK 465 HIS F 570 REMARK 465 TRP F 571 REMARK 465 LEU F 663 REMARK 465 ASP F 664 REMARK 465 GLY F 665 REMARK 465 THR F 666 REMARK 465 LYS F 667 REMARK 465 HIS F 668 REMARK 465 HIS F 669 REMARK 465 HIS F 670 REMARK 465 HIS F 671 REMARK 465 HIS F 672 REMARK 465 HIS F 673 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS 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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) 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 RES CSSEQI ATM2 DEVIATION REMARK 500 TRP A 112 CB TRP A 112 CG -0.111 REMARK 500 CYS A 157 CB CYS A 157 SG 0.142 REMARK 500 CYS C 157 CB CYS C 157 SG 0.180 REMARK 500 TRP E 45 CB TRP E 45 CG -0.113 REMARK 500 SER E 158 CA SER E 158 CB -0.137 REMARK 500 ARG E 169 CG ARG E 169 CD -0.183 REMARK 500 SER E 174 CA SER E 174 CB -0.148 REMARK 500 GLU E 482 CD GLU E 482 OE1 -0.069 REMARK 500 CYS D 604 CB CYS D 604 SG -0.107 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 TYR H 100J CA - CB - CG ANGL. DEV. = 12.7 DEGREES REMARK 500 ARG L 61 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES REMARK 500 ARG A 327 NE - CZ - NH2 ANGL. DEV. = -4.3 DEGREES REMARK 500 ARG A 419 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES REMARK 500 ARG A 456 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES REMARK 500 ARG B 579 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES REMARK 500 ARG B 588 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES REMARK 500 TYR C 435 CB - CG - CD2 ANGL. DEV. = -3.8 DEGREES REMARK 500 PRO C 498 N - CA - CB ANGL. DEV. = -8.8 DEGREES REMARK 500 ASN E 136 CB - CA - C ANGL. DEV. = -12.8 DEGREES REMARK 500 ASN E 156 CB - CA - C ANGL. DEV. = -21.9 DEGREES REMARK 500 ARG E 169 NE - CZ - NH1 ANGL. DEV. = -5.2 DEGREES REMARK 500 SER E 174 N - CA - CB ANGL. DEV. = -10.4 DEGREES REMARK 500 ARG E 327 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES REMARK 500 TYR E 435 CB - CG - CD2 ANGL. DEV. = -4.8 DEGREES REMARK 500 ARG E 456 NE - CZ - NH2 ANGL. DEV. = -3.9 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 ALA H 23 170.44 120.38 REMARK 500 ASP H 53 0.27 -69.12 REMARK 500 SER H 74 -54.29 -122.22 REMARK 500 THR H 94 -169.55 -168.45 REMARK 500 TYS H 100E -88.26 -110.68 REMARK 500 ALA L 51 -55.31 55.66 REMARK 500 SER L 67 -89.14 -149.05 REMARK 500 SER L 93 -9.92 81.77 REMARK 500 HIS A 85 176.07 67.10 REMARK 500 TRP A 96 -20.59 73.83 REMARK 500 ALA A 189 52.61 -149.16 REMARK 500 GLN A 203 135.01 -178.03 REMARK 500 ALA A 204 -102.45 -143.90 REMARK 500 CYS A 205 57.01 35.84 REMARK 500 THR A 257 -108.70 -120.88 REMARK 500 MET A 426 -43.93 65.91 REMARK 500 TRP A 427 -127.70 -103.61 REMARK 500 THR A 465 77.41 53.58 REMARK 500 ILE B 622 -31.59 -38.78 REMARK 500 TYR B 638 -1.95 -144.65 REMARK 500 GLN B 650 -113.94 -93.36 REMARK 500 HIS C 85 120.58 -8.65 REMARK 500 TRP C 96 -18.25 74.76 REMARK 500 THR C 135 75.84 -119.06 REMARK 500 GLU C 186 57.65 35.06 REMARK 500 ASN C 187 121.45 75.77 REMARK 500 SER C 188 27.67 -64.30 REMARK 500 THR C 198 -168.50 -127.40 REMARK 500 ALA C 204 -174.89 -174.97 REMARK 500 GLN C 258 -54.37 -140.61 REMARK 500 PRO C 313 93.57 -68.15 REMARK 500 MET C 426 -139.58 -94.47 REMARK 500 TRP E 69 -61.63 -94.89 REMARK 500 LEU E 86 117.30 -14.53 REMARK 500 TRP E 96 -45.77 77.62 REMARK 500 TYR E 173 86.74 -152.41 REMARK 500 GLN E 203 130.24 179.46 REMARK 500 ALA E 204 -116.64 -154.62 REMARK 500 PRO E 313 85.69 -68.47 REMARK 500 SER D 613 -35.86 -34.33 REMARK 500 THR D 639 -89.23 -7.95 REMARK 500 GLN D 640 -35.90 -23.36 REMARK 500 ASN D 651 -88.96 60.33 REMARK 500 GLU D 654 -50.18 -127.33 REMARK 500 ILE F 622 19.33 -63.82 REMARK 500 TRP F 623 -29.81 -142.89 REMARK 500 TYR F 638 -17.17 92.66 REMARK 500 GLN F 650 -124.37 -85.94 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-25732 RELATED DB: EMDB REMARK 900 RELATED ID: EMD-25733 RELATED DB: EMDB REMARK 900 RELATED ID: EMD-25734 RELATED DB: EMDB REMARK 900 RELATED ID: EMD-25735 RELATED DB: EMDB REMARK 900 RELATED ID: EMD-25736 RELATED DB: EMDB DBREF 7T73 H 1 217 PDB 7T73 7T73 1 217 DBREF 7T73 L 1 214 PDB 7T73 7T73 1 214 DBREF 7T73 A 0 513 PDB 7T73 7T73 0 513 DBREF 7T73 B 512 673 PDB 7T73 7T73 512 673 DBREF 7T73 C 0 513 PDB 7T73 7T73 0 513 DBREF 7T73 E 0 513 PDB 7T73 7T73 0 513 DBREF 7T73 D 512 673 PDB 7T73 7T73 512 673 DBREF 7T73 F 512 673 PDB 7T73 7T73 512 673 SEQRES 1 H 238 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL LYS SEQRES 2 H 238 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 H 238 PHE THR PHE SER ASN ALA TRP MET SER TRP VAL ARG GLN SEQRES 4 H 238 ALA PRO GLY LYS GLY LEU GLU TRP VAL GLY ARG ILE LYS SEQRES 5 H 238 SER LYS THR ASP GLY GLY THR THR ASP TYR ALA ALA PRO SEQRES 6 H 238 VAL LYS GLY ARG PHE THR ILE SER ARG ASP ASP SER LYS SEQRES 7 H 238 ASN THR LEU TYR LEU GLN MET ASN SER LEU LYS THR GLU SEQRES 8 H 238 ASP THR ALA VAL TYR TYR CYS THR THR GLY VAL GLU THR SEQRES 9 H 238 TYR ASP PHE TRP SER GLY TYS ASP ASP HIS TYS TYR ASP SEQRES 10 H 238 TYR TYR PHE ARG ASP VAL TRP GLY LYS GLY THR THR VAL SEQRES 11 H 238 THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE SEQRES 12 H 238 PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR SEQRES 13 H 238 ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU SEQRES 14 H 238 PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER SEQRES 15 H 238 GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY SEQRES 16 H 238 LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SEQRES 17 H 238 SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS SEQRES 18 H 238 LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO SEQRES 19 H 238 LYS SER CYS ASP SEQRES 1 L 214 GLU ILE VAL LEU THR GLN SER PRO GLY THR LEU SER LEU SEQRES 2 L 214 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 L 214 GLN SER VAL SER SER SER TYR LEU ALA TRP TYR GLN GLN SEQRES 4 L 214 LYS PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR GLY ALA SEQRES 5 L 214 SER SER ARG ALA THR GLY ILE PRO ASP ARG PHE SER GLY SEQRES 6 L 214 SER GLY SER GLY THR ASP PHE THR LEU THR ILE SER ARG SEQRES 7 L 214 LEU GLU PRO GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN SEQRES 8 L 214 TYR GLY SER SER PHE THR PHE GLY PRO GLY THR LYS VAL SEQRES 9 L 214 ASP ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 L 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 L 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 L 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 L 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 L 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 L 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 L 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 L 214 PHE ASN ARG GLY GLU CYS SEQRES 1 A 504 MET GLY ILE LEU PRO SER PRO GLY MET PRO ALA LEU LEU SEQRES 2 A 504 SER LEU VAL SER LEU LEU SER VAL LEU LEU MET GLY CYS SEQRES 3 A 504 VAL ALA GLU THR GLY ALA GLU ASN LEU TRP VAL THR VAL SEQRES 4 A 504 TYR TYR GLY VAL PRO VAL TRP LYS ASP ALA GLU THR THR SEQRES 5 A 504 LEU PHE CYS ALA SER ASP ALA LYS ALA TYR GLU THR GLU SEQRES 6 A 504 LYS HIS ASN VAL TRP ALA THR HIS ALA CYS VAL PRO THR SEQRES 7 A 504 ASP PRO ASN PRO GLN GLU ILE HIS LEU GLU ASN VAL THR SEQRES 8 A 504 GLU GLU PHE ASN MET TRP LYS ASN ASN MET VAL GLU GLN SEQRES 9 A 504 MET HIS GLU ASP ILE ILE SER LEU TRP ASP GLN SER LEU SEQRES 10 A 504 LYS PRO CYS VAL LYS LEU THR PRO LEU CYS VAL THR LEU SEQRES 11 A 504 GLN CYS THR ASN VAL THR ASN ASN ILE THR ASP ASP MET SEQRES 12 A 504 ARG GLY GLU LEU LYS ASN CYS SER PHE ASN ALA THR THR SEQRES 13 A 504 GLU LEU ARG ASN LYS ARG GLN LYS VAL TYR SER LEU PHE SEQRES 14 A 504 TYR ARG LEU ASP ILE VAL PRO MET GLY GLU ASN SER ALA SEQRES 15 A 504 ASN TYR ARG LEU ILE ASP CYS ASN THR SER ALA ILE THR SEQRES 16 A 504 GLN ALA CYS PRO LYS VAL SER PHE GLU PRO ILE PRO ILE SEQRES 17 A 504 HIS TYR CYS ALA PRO ALA GLY PHE ALA ILE LEU LYS CYS SEQRES 18 A 504 LYS ASP LYS LYS PHE ASN GLY THR GLY PRO CYS PRO SER SEQRES 19 A 504 VAL SER THR VAL GLN CYS THR HIS GLY ILE LYS PRO VAL SEQRES 20 A 504 VAL SER THR GLN LEU LEU LEU ASN GLY SER LEU ALA GLU SEQRES 21 A 504 GLU GLU VAL ILE ILE ARG SER GLU ASN ILE THR ASN ASN SEQRES 22 A 504 ALA LYS ASN ILE LEU VAL GLN LEU ASN THR PRO VAL GLN SEQRES 23 A 504 ILE ASN CYS THR ARG PRO ASN ASN ASN THR VAL LYS SER SEQRES 24 A 504 ILE ARG ILE GLY PRO GLY GLN ALA PHE TYR TYR THR GLY SEQRES 25 A 504 ASP ILE ILE GLY ASP ILE ARG GLN ALA HIS CYS ASN VAL SEQRES 26 A 504 SER LYS ALA THR TRP ASN GLU THR LEU GLY LYS VAL VAL SEQRES 27 A 504 LYS GLN LEU ARG LYS HIS PHE GLY ASN ASN THR ILE ILE SEQRES 28 A 504 ARG PHE ALA GLN SER SER GLY GLY ASP LEU GLU VAL THR SEQRES 29 A 504 THR HIS SER PHE ASN CYS GLY GLY GLU PHE PHE TYR CYS SEQRES 30 A 504 ASN THR SER GLY LEU PHE ASN SER THR TRP ILE SER ASN SEQRES 31 A 504 THR SER VAL GLN GLY SER ASN SER THR GLY SER ASN ASP SEQRES 32 A 504 SER ILE THR LEU PRO CYS ARG ILE LYS GLN ILE ILE ASN SEQRES 33 A 504 MET TRP GLN ARG ILE GLY GLN ALA MET TYR ALA PRO PRO SEQRES 34 A 504 ILE GLN GLY VAL ILE ARG CYS VAL SER ASN ILE THR GLY SEQRES 35 A 504 LEU ILE LEU THR ARG ASP GLY GLY SER THR ASN SER THR SEQRES 36 A 504 THR GLU THR PHE ARG PRO GLY GLY GLY ASP MET ARG ASP SEQRES 37 A 504 ASN TRP ARG SER GLU LEU TYR LYS TYR LYS VAL VAL LYS SEQRES 38 A 504 ILE GLU PRO LEU GLY VAL ALA PRO THR ARG CYS LYS ARG SEQRES 39 A 504 ARG VAL VAL GLY ARG ARG ARG ARG ARG ARG SEQRES 1 B 162 ALA VAL GLY ILE GLY ALA VAL SER LEU GLY PHE LEU GLY SEQRES 2 B 162 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 B 162 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 B 162 GLN GLN SER ASN LEU LEU ARG ALA PRO GLU PRO GLN GLN SEQRES 5 B 162 HIS LEU LEU LYS ASP THR HIS TRP GLY ILE LYS GLN LEU SEQRES 6 B 162 GLN ALA ARG VAL LEU ALA VAL GLU HIS TYR LEU ARG ASP SEQRES 7 B 162 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 B 162 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 B 162 ASN ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 B 162 LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE SEQRES 11 B 162 ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 B 162 LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP GLY THR LYS SEQRES 13 B 162 HIS HIS HIS HIS HIS HIS SEQRES 1 C 504 MET GLY ILE LEU PRO SER PRO GLY MET PRO ALA LEU LEU SEQRES 2 C 504 SER LEU VAL SER LEU LEU SER VAL LEU LEU MET GLY CYS SEQRES 3 C 504 VAL ALA GLU THR GLY ALA GLU ASN LEU TRP VAL THR VAL SEQRES 4 C 504 TYR TYR GLY VAL PRO VAL TRP LYS ASP ALA GLU THR THR SEQRES 5 C 504 LEU PHE CYS ALA SER ASP ALA LYS ALA TYR GLU THR GLU SEQRES 6 C 504 LYS HIS ASN VAL TRP ALA THR HIS ALA CYS VAL PRO THR SEQRES 7 C 504 ASP PRO ASN PRO GLN GLU ILE HIS LEU GLU ASN VAL THR SEQRES 8 C 504 GLU GLU PHE ASN MET TRP LYS ASN ASN MET VAL GLU GLN SEQRES 9 C 504 MET HIS GLU ASP ILE ILE SER LEU TRP ASP GLN SER LEU SEQRES 10 C 504 LYS PRO CYS VAL LYS LEU THR PRO LEU CYS VAL THR LEU SEQRES 11 C 504 GLN CYS THR ASN VAL THR ASN ASN ILE THR ASP ASP MET SEQRES 12 C 504 ARG GLY GLU LEU LYS ASN CYS SER PHE ASN ALA THR THR SEQRES 13 C 504 GLU LEU ARG ASN LYS ARG GLN LYS VAL TYR SER LEU PHE SEQRES 14 C 504 TYR ARG LEU ASP ILE VAL PRO MET GLY GLU ASN SER ALA SEQRES 15 C 504 ASN TYR ARG LEU ILE ASP CYS ASN THR SER ALA ILE THR SEQRES 16 C 504 GLN ALA CYS PRO LYS VAL SER PHE GLU PRO ILE PRO ILE SEQRES 17 C 504 HIS TYR CYS ALA PRO ALA GLY PHE ALA ILE LEU LYS CYS SEQRES 18 C 504 LYS ASP LYS LYS PHE ASN GLY THR GLY PRO CYS PRO SER SEQRES 19 C 504 VAL SER THR VAL GLN CYS THR HIS GLY ILE LYS PRO VAL SEQRES 20 C 504 VAL SER THR GLN LEU LEU LEU ASN GLY SER LEU ALA GLU SEQRES 21 C 504 GLU GLU VAL ILE ILE ARG SER GLU ASN ILE THR ASN ASN SEQRES 22 C 504 ALA LYS ASN ILE LEU VAL GLN LEU ASN THR PRO VAL GLN SEQRES 23 C 504 ILE ASN CYS THR ARG PRO ASN ASN ASN THR VAL LYS SER SEQRES 24 C 504 ILE ARG ILE GLY PRO GLY GLN ALA PHE TYR TYR THR GLY SEQRES 25 C 504 ASP ILE ILE GLY ASP ILE ARG GLN ALA HIS CYS ASN VAL SEQRES 26 C 504 SER LYS ALA THR TRP ASN GLU THR LEU GLY LYS VAL VAL SEQRES 27 C 504 LYS GLN LEU ARG LYS HIS PHE GLY ASN ASN THR ILE ILE SEQRES 28 C 504 ARG PHE ALA GLN SER SER GLY GLY ASP LEU GLU VAL THR SEQRES 29 C 504 THR HIS SER PHE ASN CYS GLY GLY GLU PHE PHE TYR CYS SEQRES 30 C 504 ASN THR SER GLY LEU PHE ASN SER THR TRP ILE SER ASN SEQRES 31 C 504 THR SER VAL GLN GLY SER ASN SER THR GLY SER ASN ASP SEQRES 32 C 504 SER ILE THR LEU PRO CYS ARG ILE LYS GLN ILE ILE ASN SEQRES 33 C 504 MET TRP GLN ARG ILE GLY GLN ALA MET TYR ALA PRO PRO SEQRES 34 C 504 ILE GLN GLY VAL ILE ARG CYS VAL SER ASN ILE THR GLY SEQRES 35 C 504 LEU ILE LEU THR ARG ASP GLY GLY SER THR ASN SER THR SEQRES 36 C 504 THR GLU THR PHE ARG PRO GLY GLY GLY ASP MET ARG ASP SEQRES 37 C 504 ASN TRP ARG SER GLU LEU TYR LYS TYR LYS VAL VAL LYS SEQRES 38 C 504 ILE GLU PRO LEU GLY VAL ALA PRO THR ARG CYS LYS ARG SEQRES 39 C 504 ARG VAL VAL GLY ARG ARG ARG ARG ARG ARG SEQRES 1 E 504 MET GLY ILE LEU PRO SER PRO GLY MET PRO ALA LEU LEU SEQRES 2 E 504 SER LEU VAL SER LEU LEU SER VAL LEU LEU MET GLY CYS SEQRES 3 E 504 VAL ALA GLU THR GLY ALA GLU ASN LEU TRP VAL THR VAL SEQRES 4 E 504 TYR TYR GLY VAL PRO VAL TRP LYS ASP ALA GLU THR THR SEQRES 5 E 504 LEU PHE CYS ALA SER ASP ALA LYS ALA TYR GLU THR GLU SEQRES 6 E 504 LYS HIS ASN VAL TRP ALA THR HIS ALA CYS VAL PRO THR SEQRES 7 E 504 ASP PRO ASN PRO GLN GLU ILE HIS LEU GLU ASN VAL THR SEQRES 8 E 504 GLU GLU PHE ASN MET TRP LYS ASN ASN MET VAL GLU GLN SEQRES 9 E 504 MET HIS GLU ASP ILE ILE SER LEU TRP ASP GLN SER LEU SEQRES 10 E 504 LYS PRO CYS VAL LYS LEU THR PRO LEU CYS VAL THR LEU SEQRES 11 E 504 GLN CYS THR ASN VAL THR ASN ASN ILE THR ASP ASP MET SEQRES 12 E 504 ARG GLY GLU LEU LYS ASN CYS SER PHE ASN ALA THR THR SEQRES 13 E 504 GLU LEU ARG ASN LYS ARG GLN LYS VAL TYR SER LEU PHE SEQRES 14 E 504 TYR ARG LEU ASP ILE VAL PRO MET GLY GLU ASN SER ALA SEQRES 15 E 504 ASN TYR ARG LEU ILE ASP CYS ASN THR SER ALA ILE THR SEQRES 16 E 504 GLN ALA CYS PRO LYS VAL SER PHE GLU PRO ILE PRO ILE SEQRES 17 E 504 HIS TYR CYS ALA PRO ALA GLY PHE ALA ILE LEU LYS CYS SEQRES 18 E 504 LYS ASP LYS LYS PHE ASN GLY THR GLY PRO CYS PRO SER SEQRES 19 E 504 VAL SER THR VAL GLN CYS THR HIS GLY ILE LYS PRO VAL SEQRES 20 E 504 VAL SER THR GLN LEU LEU LEU ASN GLY SER LEU ALA GLU SEQRES 21 E 504 GLU GLU VAL ILE ILE ARG SER GLU ASN ILE THR ASN ASN SEQRES 22 E 504 ALA LYS ASN ILE LEU VAL GLN LEU ASN THR PRO VAL GLN SEQRES 23 E 504 ILE ASN CYS THR ARG PRO ASN ASN ASN THR VAL LYS SER SEQRES 24 E 504 ILE ARG ILE GLY PRO GLY GLN ALA PHE TYR TYR THR GLY SEQRES 25 E 504 ASP ILE ILE GLY ASP ILE ARG GLN ALA HIS CYS ASN VAL SEQRES 26 E 504 SER LYS ALA THR TRP ASN GLU THR LEU GLY LYS VAL VAL SEQRES 27 E 504 LYS GLN LEU ARG LYS HIS PHE GLY ASN ASN THR ILE ILE SEQRES 28 E 504 ARG PHE ALA GLN SER SER GLY GLY ASP LEU GLU VAL THR SEQRES 29 E 504 THR HIS SER PHE ASN CYS GLY GLY GLU PHE PHE TYR CYS SEQRES 30 E 504 ASN THR SER GLY LEU PHE ASN SER THR TRP ILE SER ASN SEQRES 31 E 504 THR SER VAL GLN GLY SER ASN SER THR GLY SER ASN ASP SEQRES 32 E 504 SER ILE THR LEU PRO CYS ARG ILE LYS GLN ILE ILE ASN SEQRES 33 E 504 MET TRP GLN ARG ILE GLY GLN ALA MET TYR ALA PRO PRO SEQRES 34 E 504 ILE GLN GLY VAL ILE ARG CYS VAL SER ASN ILE THR GLY SEQRES 35 E 504 LEU ILE LEU THR ARG ASP GLY GLY SER THR ASN SER THR SEQRES 36 E 504 THR GLU THR PHE ARG PRO GLY GLY GLY ASP MET ARG ASP SEQRES 37 E 504 ASN TRP ARG SER GLU LEU TYR LYS TYR LYS VAL VAL LYS SEQRES 38 E 504 ILE GLU PRO LEU GLY VAL ALA PRO THR ARG CYS LYS ARG SEQRES 39 E 504 ARG VAL VAL GLY ARG ARG ARG ARG ARG ARG SEQRES 1 D 162 ALA VAL GLY ILE GLY ALA VAL SER LEU GLY PHE LEU GLY SEQRES 2 D 162 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 D 162 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 D 162 GLN GLN SER ASN LEU LEU ARG ALA PRO GLU PRO GLN GLN SEQRES 5 D 162 HIS LEU LEU LYS ASP THR HIS TRP GLY ILE LYS GLN LEU SEQRES 6 D 162 GLN ALA ARG VAL LEU ALA VAL GLU HIS TYR LEU ARG ASP SEQRES 7 D 162 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 D 162 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 D 162 ASN ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 D 162 LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE SEQRES 11 D 162 ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 D 162 LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP GLY THR LYS SEQRES 13 D 162 HIS HIS HIS HIS HIS HIS SEQRES 1 F 162 ALA VAL GLY ILE GLY ALA VAL SER LEU GLY PHE LEU GLY SEQRES 2 F 162 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 F 162 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 F 162 GLN GLN SER ASN LEU LEU ARG ALA PRO GLU PRO GLN GLN SEQRES 5 F 162 HIS LEU LEU LYS ASP THR HIS TRP GLY ILE LYS GLN LEU SEQRES 6 F 162 GLN ALA ARG VAL LEU ALA VAL GLU HIS TYR LEU ARG ASP SEQRES 7 F 162 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 F 162 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 F 162 ASN ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 F 162 LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE SEQRES 11 F 162 ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 F 162 LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP GLY THR LYS SEQRES 13 F 162 HIS HIS HIS HIS HIS HIS HET TYS H 100E 16 HET TYS H 100I 16 HET NAG A 601 14 HET NAG A 602 14 HET NAG A 603 14 HET NAG A 604 14 HET NAG A 605 14 HET NAG A 606 14 HET NAG A 607 14 HET NAG A 608 14 HET NAG A 609 14 HET NAG A 610 14 HET NAG A 611 14 HET NAG B 701 14 HET NAG B 702 14 HET NAG B 703 14 HET NAG C 601 14 HET NAG C 602 14 HET NAG C 603 14 HET NAG C 604 14 HET NAG C 605 14 HET NAG C 606 14 HET NAG C 607 14 HET NAG C 608 14 HET NAG C 609 14 HET NAG C 610 14 HET NAG E1001 14 HET NAG E1002 14 HET NAG E1003 14 HET NAG E1004 14 HET NAG E1005 14 HET NAG E1006 14 HET NAG E1007 14 HET NAG D 701 14 HET NAG D 702 14 HET NAG D 703 14 HET NAG F 701 14 HET NAG F 702 14 HET NAG F 703 14 HET NAG G 1 14 HET NAG G 2 14 HET NAG I 1 14 HET NAG I 2 14 HET NAG J 1 14 HET NAG J 2 14 HET BMA J 3 11 HET MAN J 4 11 HET NAG K 1 14 HET NAG K 2 14 HET NAG M 1 14 HET NAG M 2 14 HET NAG N 1 14 HET NAG N 2 14 HET BMA N 3 11 HET NAG O 1 14 HET NAG O 2 14 HET NAG P 1 14 HET NAG P 2 14 HET BMA P 3 11 HET MAN P 4 11 HET NAG Q 1 14 HET NAG Q 2 14 HET NAG R 1 14 HET NAG R 2 14 HET BMA R 3 11 HET NAG S 1 14 HET NAG S 2 14 HET BMA S 3 11 HET MAN S 4 11 HET NAG T 1 14 HET NAG T 2 14 HET NAG U 1 14 HET NAG U 2 14 HET NAG V 1 14 HET NAG V 2 14 HET BMA V 3 11 HET MAN V 4 11 HET MAN V 5 11 HET MAN V 6 11 HET MAN V 7 11 HETNAM TYS O-SULFO-L-TYROSINE HETNAM NAG N-ACETYL-D-GLUCOSAMINE HETNAM BMA BETA-D-MANNOSE HETNAM MAN ALPHA-D-MANNOSE FORMUL 1 TYS 2(C9 H11 N O6 S) FORMUL 9 NAG 65(C8 H15 N O6) FORMUL 48 BMA 6(C6 H12 O6) FORMUL 48 MAN 7(C6 H12 O6) HELIX 1 AA1 THR H 28 ALA H 32 5 5 HELIX 2 AA2 ALA H 61 LYS H 64 5 4 HELIX 3 AA3 LYS H 83 THR H 87 5 5 HELIX 4 AA4 SER L 29 SER L 31 5 3 HELIX 5 AA5 GLU L 79 PHE L 83 5 5 HELIX 6 AA6 ASN A 98 LYS A 117 1 20 HELIX 7 AA7 LEU A 122 CYS A 126 5 5 HELIX 8 AA8 THR A 139 ARG A 151 5 5 HELIX 9 AA9 LYS A 335 ARG A 350 1 16 HELIX 10 AB1 ASP A 368 THR A 372 5 5 HELIX 11 AB2 ARG A 476 SER A 481 1 6 HELIX 12 AB3 LEU B 523 SER B 528 5 6 HELIX 13 AB4 THR B 529 SER B 534 1 6 HELIX 14 AB5 THR B 536 ARG B 542 1 7 HELIX 15 AB6 ILE B 573 TRP B 596 1 24 HELIX 16 AB7 ASN B 611 SER B 615 5 5 HELIX 17 AB8 THR B 627 LYS B 633 1 7 HELIX 18 AB9 TYR B 638 GLN B 650 1 13 HELIX 19 AC1 GLN B 650 LEU B 660 1 11 HELIX 20 AC2 ASN C 99 SER C 115 1 17 HELIX 21 AC3 LEU C 122 CYS C 126 5 5 HELIX 22 AC4 THR C 139 ARG C 151 5 5 HELIX 23 AC5 LYS C 335 ARG C 350 1 16 HELIX 24 AC6 ASP C 368 THR C 373 1 6 HELIX 25 AC7 SER C 460 THR C 464 5 5 HELIX 26 AC8 MET C 475 SER C 481 1 7 HELIX 27 AC9 GLU C 482 TYR C 484 5 3 HELIX 28 AD1 ASN E 98 LEU E 116 1 19 HELIX 29 AD2 LEU E 122 CYS E 126 5 5 HELIX 30 AD3 THR E 139 ARG E 151 5 5 HELIX 31 AD4 THR E 341 PHE E 353 1 13 HELIX 32 AD5 ASP E 368 THR E 372 5 5 HELIX 33 AD6 ARG E 476 TYR E 484 1 9 HELIX 34 AD7 THR D 529 SER D 534 1 6 HELIX 35 AD8 MET D 535 LEU D 537 5 3 HELIX 36 AD9 THR D 538 ASN D 543 1 6 HELIX 37 AE1 ILE D 573 TRP D 596 1 24 HELIX 38 AE2 ASN D 611 SER D 615 5 5 HELIX 39 AE3 ASN D 618 ASN D 625 1 8 HELIX 40 AE4 THR D 627 ILE D 635 1 9 HELIX 41 AE5 THR D 639 GLN D 650 1 12 HELIX 42 AE6 ASN D 651 GLN D 653 5 3 HELIX 43 AE7 GLU D 654 LEU D 660 1 7 HELIX 44 AE8 LEU F 523 SER F 528 5 6 HELIX 45 AE9 THR F 529 SER F 534 1 6 HELIX 46 AF1 THR F 536 ARG F 542 1 7 HELIX 47 AF2 ILE F 573 TRP F 596 1 24 HELIX 48 AF3 SER F 620 ASN F 625 1 6 HELIX 49 AF4 THR F 627 SER F 636 1 10 HELIX 50 AF5 TYR F 638 GLN F 650 1 13 HELIX 51 AF6 GLN F 650 LEU F 660 1 11 SHEET 1 AA1 4 VAL H 5 GLU H 6 0 SHEET 2 AA1 4 SER H 17 ALA H 23 -1 O ALA H 23 N VAL H 5 SHEET 3 AA1 4 LEU H 78 ASN H 82A-1 O LEU H 80 N LEU H 20 SHEET 4 AA1 4 ILE H 69 ARG H 71 -1 N SER H 70 O TYR H 79 SHEET 1 AA2 6 MET H 34 GLN H 39 0 SHEET 2 AA2 6 GLU H 46 ILE H 51 -1 O GLU H 46 N ARG H 38 SHEET 3 AA2 6 THR H 57 TYR H 59 -1 O ASP H 58 N ARG H 50 SHEET 4 AA2 6 VAL H 89 PHE H 100A-1 O TYR H 91 N VAL H 37 SHEET 5 AA2 6 TYR H 100J TRP H 103 -1 O TYR H 100M N THR H 98 SHEET 6 AA2 6 THR H 107 THR H 108 -1 O THR H 107 N TYR H 90 SHEET 1 AA3 7 THR L 10 SER L 12 0 SHEET 2 AA3 7 LEU L 33 GLN L 38 0 SHEET 3 AA3 7 ARG L 45 TYR L 49 -1 O LEU L 47 N TRP L 35 SHEET 4 AA3 7 SER L 53 ARG L 54 -1 O SER L 53 N TYR L 49 SHEET 5 AA3 7 VAL L 85 TYR L 91 -1 O GLN L 89 N ALA L 34 SHEET 6 AA3 7 PHE L 96 PHE L 98 -1 O THR L 97 N GLN L 90 SHEET 7 AA3 7 THR L 102 ASP L 105 -1 O THR L 102 N TYR L 86 SHEET 1 AA4 3 ALA L 19 ARG L 24 0 SHEET 2 AA4 3 ASP L 70 ILE L 75 -1 O LEU L 73 N LEU L 21 SHEET 3 AA4 3 PHE L 62 GLY L 66 -1 N SER L 63 O THR L 74 SHEET 1 AA5 2 TRP A 35 TYR A 40 0 SHEET 2 AA5 2 LEU A 494 THR A 499 -1 O THR A 499 N TRP A 35 SHEET 1 AA6 5 TRP A 45 ASP A 47 0 SHEET 2 AA6 5 TYR A 486 ILE A 491 -1 O LYS A 490 N LYS A 46 SHEET 3 AA6 5 PHE A 223 CYS A 228 -1 N LEU A 226 O LYS A 487 SHEET 4 AA6 5 VAL A 242 VAL A 245 -1 O SER A 243 N LYS A 227 SHEET 5 AA6 5 LEU A 86 GLU A 87 -1 N GLU A 87 O VAL A 242 SHEET 1 AA7 3 VAL A 75 PRO A 76 0 SHEET 2 AA7 3 PHE A 53 SER A 56 1 N CYS A 54 O VAL A 75 SHEET 3 AA7 3 HIS A 216 CYS A 218 -1 O CYS A 218 N PHE A 53 SHEET 1 AA8 2 GLU A 91 GLU A 92 0 SHEET 2 AA8 2 PRO A 238 CYS A 239 -1 O CYS A 239 N GLU A 91 SHEET 1 AA9 3 GLN A 130 THR A 132 0 SHEET 2 AA9 3 LEU A 154 PHE A 159 -1 O SER A 158 N GLN A 130 SHEET 3 AA9 3 VAL A 172 TYR A 177 -1 O PHE A 176 N LYS A 155 SHEET 1 AB1 2 ILE A 181 PRO A 183 0 SHEET 2 AB1 2 TYR A 191 LEU A 193 -1 O ARG A 192 N VAL A 182 SHEET 1 AB210 LEU A 259 LEU A 261 0 SHEET 2 AB210 ILE A 271 ARG A 273 0 SHEET 3 AB210 ILE A 284 GLY A 312 -1 O LEU A 285 N ARG A 273 SHEET 4 AB210 GLN A 315 ILE A 323 -1 O GLN A 315 N ILE A 309 SHEET 5 AB210 HIS A 330 SER A 334 -1 O ASN A 332 N ASN A 295 SHEET 6 AB210 ILE A 359 PHE A 361 0 SHEET 7 AB210 SER A 393 TRP A 395 -1 O TRP A 395 N ILE A 359 SHEET 8 AB210 SER A 413 PRO A 417 -1 O LEU A 416 N CYS A 331 SHEET 9 AB210 GLY A 441 ARG A 456 -1 O CYS A 445 N CYS A 296 SHEET 10 AB210 GLU A 466 PRO A 470 -1 O ARG A 469 N THR A 455 SHEET 1 AB3 2 HIS A 374 CYS A 378 0 SHEET 2 AB3 2 GLU A 381 CYS A 385 -1 O CYS A 385 N HIS A 374 SHEET 1 AB4 2 ILE A 423 ILE A 424 0 SHEET 2 AB4 2 MET A 434 TYR A 435 -1 O MET A 434 N ILE A 424 SHEET 1 AB5 3 LEU C 494 THR C 499 0 SHEET 2 AB5 3 TRP C 35 TYR C 40 -1 N TYR C 39 O GLY C 495 SHEET 3 AB5 3 ILE D 603 PRO D 609 -1 O CYS D 604 N VAL C 38 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 ILE C 84 GLU C 87 -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 SER C 56 O VAL C 75 SHEET 3 AB7 3 HIS C 216 CYS C 218 -1 O HIS C 216 N ALA C 55 SHEET 1 AB8 3 GLN C 130 ASN C 133 0 SHEET 2 AB8 3 LEU C 154 THR C 162 -1 O SER C 158 N GLN C 130 SHEET 3 AB8 3 ARG C 169 TYR C 177 -1 O VAL C 172 N PHE C 159 SHEET 1 AB9 2 ILE C 181 PRO C 183 0 SHEET 2 AB9 2 TYR C 191 LEU C 193 -1 O ARG C 192 N VAL C 182 SHEET 1 AC1 3 ILE C 201 THR C 202 0 SHEET 2 AC1 3 ALA C 433 TYR C 435 1 O TYR C 435 N THR C 202 SHEET 3 AC1 3 ILE C 423 ILE C 424 -1 N ILE C 424 O MET C 434 SHEET 1 AC211 LEU C 259 LEU C 261 0 SHEET 2 AC211 ILE C 271 SER C 274 0 SHEET 3 AC211 ASN C 283 ARG C 298 -1 O LEU C 285 N ARG C 273 SHEET 4 AC211 HIS C 330 SER C 334 -1 O HIS C 330 N THR C 297 SHEET 5 AC211 ILE C 359 PHE C 361 0 SHEET 6 AC211 HIS C 374 CYS C 378 0 SHEET 7 AC211 GLU C 381 CYS C 385 -1 O PHE C 383 N PHE C 376 SHEET 8 AC211 SER C 393 TRP C 395 -1 O SER C 393 N PHE C 361 SHEET 9 AC211 SER C 413 LYS C 421 -1 O ARG C 419 N TYR C 384 SHEET 10 AC211 ILE C 443 ARG C 456 -1 O LEU C 454 N ILE C 284 SHEET 11 AC211 THR C 467 PRO C 470 -1 O ARG C 469 N THR C 455 SHEET 1 AC3 2 VAL C 304 GLY C 312 0 SHEET 2 AC3 2 GLN C 315 THR C 320 -1 O GLN C 315 N ILE C 309 SHEET 1 AC4 2 TRP E 35 TYR E 40 0 SHEET 2 AC4 2 LEU E 494 THR E 499 -1 O THR E 499 N TRP E 35 SHEET 1 AC5 4 TRP E 45 ASP E 47 0 SHEET 2 AC5 4 TYR E 486 ILE E 491 -1 O LYS E 490 N LYS E 46 SHEET 3 AC5 4 PHE E 223 CYS E 228 -1 N LEU E 226 O LYS E 487 SHEET 4 AC5 4 VAL E 242 VAL E 245 -1 O SER E 243 N LYS E 227 SHEET 1 AC6 3 VAL E 75 PRO E 76 0 SHEET 2 AC6 3 PHE E 53 SER E 56 1 N CYS E 54 O VAL E 75 SHEET 3 AC6 3 HIS E 216 CYS E 218 -1 O HIS E 216 N ALA E 55 SHEET 1 AC7 2 GLU E 91 GLU E 92 0 SHEET 2 AC7 2 PRO E 238 CYS E 239 -1 O CYS E 239 N GLU E 91 SHEET 1 AC8 3 GLN E 130 ASN E 133 0 SHEET 2 AC8 3 LEU E 154 SER E 158 -1 O ASN E 156 N THR E 132 SHEET 3 AC8 3 SER E 174 TYR E 177 -1 O SER E 174 N CYS E 157 SHEET 1 AC9 2 ASN E 160 THR E 162 0 SHEET 2 AC9 2 ARG E 169 LYS E 171 -1 O GLN E 170 N ALA E 161 SHEET 1 AD1 2 ILE E 181 PRO E 183 0 SHEET 2 AD1 2 TYR E 191 LEU E 193 -1 O ARG E 192 N VAL E 182 SHEET 1 AD212 LEU E 259 LEU E 261 0 SHEET 2 AD212 ILE E 271 SER E 274 0 SHEET 3 AD212 ILE E 284 GLY E 312 -1 O LEU E 285 N ARG E 273 SHEET 4 AD212 GLN E 315 ILE E 323 -1 O ASP E 321A N THR E 303 SHEET 5 AD212 ALA E 329 SER E 334 -1 O ASN E 332 N ASN E 295 SHEET 6 AD212 ILE E 359 PHE E 361 0 SHEET 7 AD212 HIS E 374 CYS E 378 0 SHEET 8 AD212 GLU E 381 CYS E 385 -1 O CYS E 385 N HIS E 374 SHEET 9 AD212 THR E 394 TRP E 395 -1 O TRP E 395 N ILE E 359 SHEET 10 AD212 SER E 413 ILE E 420 -1 O ARG E 419 N TYR E 384 SHEET 11 AD212 GLY E 441 ARG E 456 -1 O LEU E 454 N ILE E 284 SHEET 12 AD212 GLU E 466 PRO E 470 -1 O ARG E 469 N THR E 455 SHEET 1 AD3 2 ILE E 423 ILE E 424 0 SHEET 2 AD3 2 MET E 434 TYR E 435 -1 O MET E 434 N ILE E 424 SSBOND 1 CYS H 22 CYS H 92 1555 1555 2.02 SSBOND 2 CYS L 23 CYS L 88 1555 1555 2.03 SSBOND 3 CYS A 54 CYS A 74 1555 1555 2.19 SSBOND 4 CYS A 119 CYS A 205 1555 1555 2.05 SSBOND 5 CYS A 126 CYS A 196 1555 1555 2.03 SSBOND 6 CYS A 131 CYS A 157 1555 1555 2.17 SSBOND 7 CYS A 218 CYS A 247 1555 1555 2.03 SSBOND 8 CYS A 228 CYS A 239 1555 1555 2.05 SSBOND 9 CYS A 296 CYS A 331 1555 1555 2.03 SSBOND 10 CYS A 378 CYS A 445 1555 1555 2.02 SSBOND 11 CYS A 385 CYS A 418 1555 1555 2.03 SSBOND 12 CYS A 501 CYS B 605 1555 1555 2.04 SSBOND 13 CYS B 598 CYS B 604 1555 1555 2.02 SSBOND 14 CYS C 119 CYS C 205 1555 1555 2.18 SSBOND 15 CYS C 126 CYS C 196 1555 1555 2.03 SSBOND 16 CYS C 131 CYS C 157 1555 1555 2.23 SSBOND 17 CYS C 218 CYS C 247 1555 1555 2.03 SSBOND 18 CYS C 228 CYS C 239 1555 1555 2.03 SSBOND 19 CYS C 296 CYS C 331 1555 1555 2.03 SSBOND 20 CYS C 378 CYS C 445 1555 1555 2.02 SSBOND 21 CYS C 385 CYS C 418 1555 1555 2.03 SSBOND 22 CYS C 501 CYS D 605 1555 1555 2.03 SSBOND 23 CYS E 54 CYS E 74 1555 1555 2.14 SSBOND 24 CYS E 119 CYS E 205 1555 1555 2.06 SSBOND 25 CYS E 126 CYS E 196 1555 1555 2.03 SSBOND 26 CYS E 131 CYS E 157 1555 1555 2.02 SSBOND 27 CYS E 218 CYS E 247 1555 1555 2.03 SSBOND 28 CYS E 228 CYS E 239 1555 1555 2.10 SSBOND 29 CYS E 296 CYS E 331 1555 1555 2.03 SSBOND 30 CYS E 378 CYS E 445 1555 1555 2.03 SSBOND 31 CYS E 385 CYS E 418 1555 1555 2.02 SSBOND 32 CYS E 501 CYS F 605 1555 1555 2.04 SSBOND 33 CYS D 598 CYS D 604 1555 1555 2.02 SSBOND 34 CYS F 598 CYS F 604 1555 1555 2.02 LINK C GLY H 100D N TYS H 100E 1555 1555 1.35 LINK C TYS H 100E N ASP H 100F 1555 1555 1.36 LINK C HIS H 100H N TYS H 100I 1555 1555 1.33 LINK C TYS H 100I N TYR H 100J 1555 1555 1.37 LINK ND2 ASN A 88 C1 NAG A 606 1555 1555 1.52 LINK ND2 ASN A 133 C1 NAG A 601 1555 1555 1.53 LINK ND2 ASN A 137 C1 NAG A 604 1555 1555 1.52 LINK ND2 ASN A 156 C1 NAG I 1 1555 1555 1.52 LINK ND2 ASN A 160 C1 NAG G 1 1555 1555 1.51 LINK ND2 ASN A 197 C1 NAG A 610 1555 1555 1.53 LINK ND2 ASN A 262 C1 NAG J 1 1555 1555 1.50 LINK ND2 ASN A 276 C1 NAG A 603 1555 1555 1.53 LINK ND2 ASN A 295 C1 NAG A 609 1555 1555 1.52 LINK ND2 ASN A 301 C1 NAG A 602 1555 1555 1.53 LINK ND2 ASN A 332 C1 NAG A 607 1555 1555 1.52 LINK ND2 ASN A 339 C1 NAG A 611 1555 1555 1.52 LINK ND2 ASN A 355 C1 NAG A 608 1555 1555 1.53 LINK ND2 ASN A 386 C1 NAG K 1 1555 1555 1.53 LINK ND2 ASN A 392 C1 NAG A 605 1555 1555 1.53 LINK ND2 ASN A 448 C1 NAG M 1 1555 1555 1.53 LINK ND2 ASN B 611 C1 NAG B 702 1555 1555 1.41 LINK ND2 ASN B 618 C1 NAG B 703 1555 1555 1.44 LINK ND2 ASN B 637 C1 NAG B 701 1555 1555 1.43 LINK ND2 ASN C 88 C1 NAG C 609 1555 1555 1.52 LINK ND2 ASN C 133 C1 NAG C 602 1555 1555 1.53 LINK ND2 ASN C 156 C1 NAG O 1 1555 1555 1.52 LINK ND2 ASN C 160 C1 NAG N 1 1555 1555 1.43 LINK ND2 ASN C 197 C1 NAG C 601 1555 1555 1.53 LINK ND2 ASN C 262 C1 NAG P 1 1555 1555 1.51 LINK ND2 ASN C 276 C1 NAG C 607 1555 1555 1.52 LINK ND2 ASN C 295 C1 NAG C 605 1555 1555 1.52 LINK ND2 ASN C 301 C1 NAG C 603 1555 1555 1.52 LINK ND2 ASN C 332 C1 NAG C 604 1555 1555 1.50 LINK ND2 ASN C 339 C1 NAG C 610 1555 1555 1.53 LINK ND2 ASN C 386 C1 NAG Q 1 1555 1555 1.53 LINK ND2 ASN C 392 C1 NAG C 608 1555 1555 1.52 LINK ND2 ASN C 448 C1 NAG C 606 1555 1555 1.53 LINK ND2 ASN E 88 C1 NAG E1006 1555 1555 1.52 LINK ND2 ASN E 156 C1 NAG R 1 1555 1555 1.42 LINK ND2 ASN E 160 C1 NAG V 1 1555 1555 1.43 LINK ND2 ASN E 197 C1 NAG E1001 1555 1555 1.51 LINK ND2 ASN E 262 C1 NAG S 1 1555 1555 1.51 LINK ND2 ASN E 276 C1 NAG E1004 1555 1555 1.53 LINK ND2 ASN E 301 C1 NAG E1002 1555 1555 1.53 LINK ND2 ASN E 332 C1 NAG T 1 1555 1555 1.50 LINK ND2 ASN E 339 C1 NAG E1007 1555 1555 1.52 LINK ND2 ASN E 386 C1 NAG U 1 1555 1555 1.52 LINK ND2 ASN E 392 C1 NAG E1005 1555 1555 1.53 LINK ND2 ASN E 448 C1 NAG E1003 1555 1555 1.53 LINK ND2 ASN D 611 C1 NAG D 701 1555 1555 1.43 LINK ND2 ASN D 618 C1 NAG D 702 1555 1555 1.43 LINK ND2 ASN D 637 C1 NAG D 703 1555 1555 1.43 LINK ND2 ASN F 611 C1 NAG F 701 1555 1555 1.48 LINK OG SER F 613 C1 NAG F 701 1555 1555 1.52 LINK ND2 ASN F 618 C1 NAG F 702 1555 1555 1.44 LINK ND2 ASN F 637 C1 NAG F 703 1555 1555 1.43 LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.51 LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.51 LINK O4 NAG J 1 C1 NAG J 2 1555 1555 1.50 LINK O4 NAG J 2 C1 BMA J 3 1555 1555 1.52 LINK O3 BMA J 3 C1 MAN J 4 1555 1555 1.53 LINK O4 NAG K 1 C1 NAG K 2 1555 1555 1.52 LINK O4 NAG M 1 C1 NAG M 2 1555 1555 1.52 LINK O4 NAG N 1 C1 NAG N 2 1555 1555 1.43 LINK O4 NAG N 2 C1 BMA N 3 1555 1555 1.44 LINK O4 NAG O 1 C1 NAG O 2 1555 1555 1.50 LINK O4 NAG P 1 C1 NAG P 2 1555 1555 1.50 LINK O4 NAG P 2 C1 BMA P 3 1555 1555 1.52 LINK O3 BMA P 3 C1 MAN P 4 1555 1555 1.53 LINK O4 NAG Q 1 C1 NAG Q 2 1555 1555 1.51 LINK O4 NAG R 1 C1 NAG R 2 1555 1555 1.45 LINK O4 NAG R 2 C1 BMA R 3 1555 1555 1.46 LINK O4 NAG S 1 C1 NAG S 2 1555 1555 1.50 LINK O4 NAG S 2 C1 BMA S 3 1555 1555 1.52 LINK O3 BMA S 3 C1 MAN S 4 1555 1555 1.52 LINK O4 NAG T 1 C1 NAG T 2 1555 1555 1.51 LINK O4 NAG U 1 C1 NAG U 2 1555 1555 1.51 LINK O4 NAG V 1 C1 NAG V 2 1555 1555 1.44 LINK O4 NAG V 2 C1 BMA V 3 1555 1555 1.44 LINK O6 BMA V 3 C1 MAN V 4 1555 1555 1.44 LINK O3 BMA V 3 C1 MAN V 7 1555 1555 1.44 LINK O3 MAN V 4 C1 MAN V 5 1555 1555 1.44 LINK O6 MAN V 4 C1 MAN V 6 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