HEADER VIRAL PROTEIN/IMMUNE SYSTEM 14-DEC-21 7T76 TITLE HIV-1 ENVELOPE APEXGT3 IN COMPLEX WITH PG9.IGL FAB COMPND MOL_ID: 1; COMPND 2 MOLECULE: HIV ENVELOPE APEXGT3 GP120; COMPND 3 CHAIN: A, C, E; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: HIV ENVELOPE APEXGT3 GP41; COMPND 7 CHAIN: D, F, B; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: PG9.IGL FAB LIGHT CHAIN; COMPND 11 CHAIN: L; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 4; COMPND 14 MOLECULE: PG9.IGL FAB HEAVY CHAIN; COMPND 15 CHAIN: H; COMPND 16 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 3 ORGANISM_COMMON: HIV-1; SOURCE 4 ORGANISM_TAXID: 11676; SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HEK; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 11 ORGANISM_COMMON: HIV-1; SOURCE 12 ORGANISM_TAXID: 11676; SOURCE 13 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 14 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 16 EXPRESSION_SYSTEM_CELL_LINE: HEK; SOURCE 17 MOL_ID: 3; SOURCE 18 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 19 ORGANISM_COMMON: HUMAN; SOURCE 20 ORGANISM_TAXID: 9606; SOURCE 21 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 22 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 23 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 24 EXPRESSION_SYSTEM_CELL_LINE: HEK; SOURCE 25 MOL_ID: 4; SOURCE 26 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 27 ORGANISM_COMMON: HUMAN; SOURCE 28 ORGANISM_TAXID: 9606; SOURCE 29 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 30 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 31 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 32 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. 4.43 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) : 4.430 REMARK 3 NUMBER OF PARTICLES : 78573 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 7T76 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_1000259243. 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 APEXGT3 IN REMARK 245 COMPLEX WITH PG9.IGL 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) : NULL REMARK 245 MAXIMUM DEFOCUS (NM) : NULL 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: A, C, D, E, F, B, L, H, G, I, REMARK 350 AND CHAINS: J, K, M, N, O, P, Q, R, S, REMARK 350 AND CHAINS: T, U, V, W, X, Y, Z, a, b, c, REMARK 350 AND CHAINS: d, e, f, g, h, i, j 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 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 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 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 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 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 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 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 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 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 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 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 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 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 L -47 REMARK 465 LEU L -46 REMARK 465 ASN L -45 REMARK 465 SER L -44 REMARK 465 THR L -43 REMARK 465 SER L -42 REMARK 465 LEU L -41 REMARK 465 PHE L -40 REMARK 465 ARG L -39 REMARK 465 PHE L -38 REMARK 465 LEU L -37 REMARK 465 PHE L -36 REMARK 465 CYS L -35 REMARK 465 ALA L -34 REMARK 465 VAL L -33 REMARK 465 THR L -32 REMARK 465 ASP L -31 REMARK 465 PRO L -30 REMARK 465 SER L -29 REMARK 465 CYS L -28 REMARK 465 ASP L -27 REMARK 465 ARG L -26 REMARK 465 ARG L -25 REMARK 465 LEU L -24 REMARK 465 PRO L -23 REMARK 465 GLU L -22 REMARK 465 ILE L -21 REMARK 465 ASN L -20 REMARK 465 MET L -19 REMARK 465 TYR L -18 REMARK 465 ARG L -17 REMARK 465 MET L -16 REMARK 465 GLN L -15 REMARK 465 LEU L -14 REMARK 465 LEU L -13 REMARK 465 SER L -12 REMARK 465 CYS L -11 REMARK 465 ILE L -10 REMARK 465 ALA L -9 REMARK 465 LEU L -8 REMARK 465 SER L -7 REMARK 465 LEU L -6 REMARK 465 ALA L -5 REMARK 465 LEU L -4 REMARK 465 VAL L -3 REMARK 465 THR L -2 REMARK 465 ASN L -1 REMARK 465 SER L 0 REMARK 465 GLN L 1 REMARK 465 GLY L 108 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 MET H -19 REMARK 465 TYR H -18 REMARK 465 ARG H -17 REMARK 465 MET H -16 REMARK 465 GLN H -15 REMARK 465 LEU H -14 REMARK 465 LEU H -13 REMARK 465 SER H -12 REMARK 465 CYS H -11 REMARK 465 ILE H -10 REMARK 465 ALA H -9 REMARK 465 LEU H -8 REMARK 465 SER H -7 REMARK 465 LEU H -6 REMARK 465 ALA H -5 REMARK 465 LEU H -4 REMARK 465 VAL H -3 REMARK 465 THR H -2 REMARK 465 ASN H -1 REMARK 465 SER H 0 REMARK 465 GLN H 1 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 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 C PHE E 233 O4 NAG E 607 0.39 REMARK 500 C ASN E 234 C2 NAG E 607 0.53 REMARK 500 N GLY E 235 C1 NAG E 607 0.61 REMARK 500 CA ASN E 234 C3 NAG E 607 0.70 REMARK 500 O ASN E 234 N2 NAG E 607 0.82 REMARK 500 CB PHE E 233 O6 NAG E 607 0.93 REMARK 500 CA ASN E 234 O3 NAG E 607 0.96 REMARK 500 N GLY E 235 C2 NAG E 607 0.99 REMARK 500 CA PHE E 233 O6 NAG E 607 0.99 REMARK 500 CB ASN E 234 O7 NAG E 607 1.05 REMARK 500 CA GLY E 235 C1 NAG E 607 1.13 REMARK 500 CG ASN E 234 O7 NAG E 607 1.15 REMARK 500 C ASN E 234 C3 NAG E 607 1.17 REMARK 500 C PHE E 233 C4 NAG E 607 1.18 REMARK 500 CB PHE E 233 C6 NAG E 607 1.18 REMARK 500 O PHE E 233 O4 NAG E 607 1.22 REMARK 500 C ASN E 234 N2 NAG E 607 1.31 REMARK 500 O ASN E 234 C2 NAG E 607 1.33 REMARK 500 N ASN E 234 C4 NAG E 607 1.36 REMARK 500 CG PHE E 233 C6 NAG E 607 1.41 REMARK 500 N ASN E 234 C3 NAG E 607 1.42 REMARK 500 N ASN E 234 O4 NAG E 607 1.42 REMARK 500 O PHE E 233 C4 NAG E 607 1.49 REMARK 500 CG ASN E 234 C7 NAG E 607 1.52 REMARK 500 N GLY E 235 O5 NAG E 607 1.54 REMARK 500 CA ASN E 234 O7 NAG E 607 1.54 REMARK 500 O ASN E 234 C7 NAG E 607 1.57 REMARK 500 ND2 ASN E 234 C8 NAG E 607 1.63 REMARK 500 CA PHE E 233 O4 NAG E 607 1.63 REMARK 500 OD1 ASN E 234 O7 NAG E 607 1.69 REMARK 500 N PHE E 233 O6 NAG E 607 1.72 REMARK 500 CD2 PHE E 233 C6 NAG E 607 1.74 REMARK 500 CG ASN E 234 C8 NAG E 607 1.82 REMARK 500 CG PHE E 233 C5 NAG E 607 1.83 REMARK 500 CB ASN E 234 O3 NAG E 607 1.86 REMARK 500 N GLY E 235 C3 NAG E 607 1.88 REMARK 500 C PHE E 233 O6 NAG E 607 1.88 REMARK 500 C ASN E 234 C1 NAG E 607 1.89 REMARK 500 C ASN E 234 O3 NAG E 607 1.95 REMARK 500 CA ASN E 234 C4 NAG E 607 1.96 REMARK 500 CA GLY E 235 O5 NAG E 607 1.97 REMARK 500 CD2 PHE E 233 O5 NAG E 607 1.98 REMARK 500 C ASN E 234 C7 NAG E 607 1.98 REMARK 500 OD1 ASN E 234 C7 NAG E 607 1.98 REMARK 500 C PHE E 233 C5 NAG E 607 2.00 REMARK 500 CD2 PHE E 233 C5 NAG E 607 2.01 REMARK 500 CA ASN E 234 C2 NAG E 607 2.01 REMARK 500 CB ASN E 234 C7 NAG E 607 2.02 REMARK 500 CA GLY E 235 C2 NAG E 607 2.03 REMARK 500 C GLY E 235 C1 NAG E 607 2.03 REMARK 500 REMARK 500 THIS ENTRY HAS 57 CLOSE CONTACTS REMARK 500 REMARK 500 REMARK: NULL 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 45 CB TRP A 45 CG -0.138 REMARK 500 TRP D 610 CB TRP D 610 CG -0.109 REMARK 500 TRP E 45 CB TRP E 45 CG -0.157 REMARK 500 CYS E 205 CB CYS E 205 SG 0.124 REMARK 500 CYS F 604 CB CYS F 604 SG -0.107 REMARK 500 TRP B 610 CB TRP B 610 CG -0.111 REMARK 500 TRP B 610 NE1 TRP B 610 CE2 -0.081 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 A 217 CB - CG - CD1 ANGL. DEV. = -3.7 DEGREES REMARK 500 ARG A 500 NE - CZ - NH2 ANGL. DEV. = -4.5 DEGREES REMARK 500 ARG C 480 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES REMARK 500 ARG E 151 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES REMARK 500 CYS E 157 CA - CB - SG ANGL. DEV. = 7.2 DEGREES REMARK 500 TYR E 177 CB - CG - CD2 ANGL. DEV. = -3.9 DEGREES REMARK 500 PRO E 238 C - N - CA ANGL. DEV. = 9.2 DEGREES REMARK 500 ARG E 327 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES REMARK 500 ARG E 419 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES REMARK 500 ARG E 469 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES REMARK 500 ARG F 542 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES REMARK 500 ARG F 617 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES REMARK 500 ARG B 617 NE - CZ - NH2 ANGL. DEV. = -4.8 DEGREES REMARK 500 ARG H 19 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES REMARK 500 ARG H 83 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ASN A 136 73.08 -160.30 REMARK 500 ARG A 186 -53.18 72.02 REMARK 500 GLN A 203 133.36 179.95 REMARK 500 ALA A 204 -133.21 -164.98 REMARK 500 ASN A 234 -65.29 -93.79 REMARK 500 GLN A 258 -50.35 -138.71 REMARK 500 ASN A 262 73.87 44.26 REMARK 500 PRO A 313 81.22 -69.54 REMARK 500 ASN A 392 59.56 -143.94 REMARK 500 MET A 426 -63.37 60.49 REMARK 500 TRP A 427 -117.25 -116.61 REMARK 500 PHE C 53 -133.06 -87.63 REMARK 500 ASN C 80 70.05 -153.05 REMARK 500 ASN C 88 64.43 25.87 REMARK 500 TRP C 96 -10.31 76.76 REMARK 500 ASN C 167 -5.13 -165.72 REMARK 500 ARG C 186 154.03 70.93 REMARK 500 ALA C 187 -54.46 69.49 REMARK 500 SER C 189 1.98 -161.18 REMARK 500 GLN C 203 128.75 179.33 REMARK 500 ALA C 204 -112.47 -146.96 REMARK 500 THR C 257 -93.98 -126.69 REMARK 500 ASN C 425 79.38 -106.43 REMARK 500 CYS D 598 75.58 -106.33 REMARK 500 PRO E 79 24.97 -78.82 REMARK 500 TRP E 96 -18.11 76.92 REMARK 500 ASN E 136 52.64 -140.53 REMARK 500 THR E 163 -155.10 -144.28 REMARK 500 ASP E 185 104.53 -173.41 REMARK 500 ALA E 187 -160.91 -176.98 REMARK 500 SER E 189 -5.15 -147.84 REMARK 500 ALA E 204 -166.94 -174.21 REMARK 500 THR E 257 -90.49 -104.63 REMARK 500 PRO E 313 82.31 -69.74 REMARK 500 ASN E 392 -47.26 -148.71 REMARK 500 GLN F 650 -116.92 -89.76 REMARK 500 ASN B 625 -33.66 -131.37 REMARK 500 ASP L 27B -103.87 -119.94 REMARK 500 TYR L 32 73.29 -65.63 REMARK 500 VAL L 51 -56.24 66.84 REMARK 500 SER H 55 -19.91 -41.75 REMARK 500 LYS H 75 3.09 -68.50 REMARK 500 ALA H 96 -168.56 -71.90 REMARK 500 TYR H 100R 44.77 70.85 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 E 607 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-25735 RELATED DB: EMDB 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-25736 RELATED DB: EMDB DBREF 7T76 A 0 513 PDB 7T76 7T76 0 513 DBREF 7T76 C 0 513 PDB 7T76 7T76 0 513 DBREF 7T76 D 512 673 PDB 7T76 7T76 512 673 DBREF 7T76 E 0 513 PDB 7T76 7T76 0 513 DBREF 7T76 F 512 673 PDB 7T76 7T76 512 673 DBREF 7T76 B 512 673 PDB 7T76 7T76 512 673 DBREF 7T76 L -47 213 PDB 7T76 7T76 -47 213 DBREF 7T76 H -19 216 PDB 7T76 7T76 -19 216 SEQRES 1 A 506 MET GLY ILE LEU PRO SER PRO GLY MET PRO ALA LEU LEU SEQRES 2 A 506 SER LEU VAL SER LEU LEU SER VAL LEU LEU MET GLY CYS SEQRES 3 A 506 VAL ALA GLU THR GLY ALA GLU ASN LEU TRP VAL THR VAL SEQRES 4 A 506 TYR TYR GLY VAL PRO VAL TRP LYS ASP ALA GLU THR THR SEQRES 5 A 506 LEU PHE CYS ALA SER ASP ALA LYS ALA TYR GLU THR GLU SEQRES 6 A 506 LYS HIS ASN VAL TRP ALA THR HIS ALA CYS VAL PRO THR SEQRES 7 A 506 ASP PRO ASN PRO GLN GLU ILE HIS LEU GLU ASN VAL THR SEQRES 8 A 506 GLU GLU PHE ASN MET TRP LYS ASN ASN MET VAL GLU GLN SEQRES 9 A 506 MET HIS GLU ASP ILE ILE SER LEU TRP ASP GLN SER LEU SEQRES 10 A 506 LYS PRO CYS VAL LYS LEU THR PRO LEU CYS VAL THR LEU SEQRES 11 A 506 GLN CYS THR ASN VAL THR ASN ASN ILE THR ASP ASP MET SEQRES 12 A 506 ARG GLY GLU LEU LYS ASN CYS SER PHE ASN ALA THR THR SEQRES 13 A 506 GLU LEU ARG ASN LYS ARG VAL LYS ARG TYR SER LEU PHE SEQRES 14 A 506 TYR ARG LEU ASP ILE VAL GLN ILE ASP SER ASN ARG ALA SEQRES 15 A 506 LYS SER HIS TYR ARG LEU ILE ASN CYS ASN THR SER ALA SEQRES 16 A 506 ILE THR GLN ALA CYS PRO LYS VAL SER PHE GLU PRO ILE SEQRES 17 A 506 PRO ILE HIS TYR CYS ALA PRO ALA GLY PHE ALA ILE LEU SEQRES 18 A 506 LYS CYS LYS ASP LYS LYS PHE ASN GLY THR GLY PRO CYS SEQRES 19 A 506 PRO SER VAL SER THR VAL GLN CYS THR HIS GLY ILE LYS SEQRES 20 A 506 PRO VAL VAL SER THR GLN LEU LEU LEU ASN GLY SER LEU SEQRES 21 A 506 ALA GLU GLU GLU VAL ILE ILE ARG SER GLU ASN ILE THR SEQRES 22 A 506 ASN ASN ALA LYS ASN ILE LEU VAL GLN LEU ASN THR PRO SEQRES 23 A 506 VAL GLN ILE ASN CYS THR ARG PRO ASN ASN ASN THR VAL SEQRES 24 A 506 LYS SER ILE ARG ILE GLY PRO GLY GLN ALA PHE TYR TYR SEQRES 25 A 506 THR GLY ASP ILE ILE GLY ASP ILE ARG GLN ALA HIS CYS SEQRES 26 A 506 ASN VAL SER LYS ALA THR TRP ASN GLU THR LEU GLY LYS SEQRES 27 A 506 VAL VAL LYS GLN LEU ARG LYS HIS PHE GLY ASN ASN THR SEQRES 28 A 506 ILE ILE ARG PHE ALA GLN SER SER GLY GLY ASP LEU GLU SEQRES 29 A 506 VAL THR THR HIS SER PHE ASN CYS GLY GLY GLU PHE PHE SEQRES 30 A 506 TYR CYS ASN THR SER GLY LEU PHE ASN SER THR TRP ILE SEQRES 31 A 506 SER ASN THR SER VAL GLN GLY SER ASN SER THR GLY SER SEQRES 32 A 506 ASN ASP SER ILE THR LEU PRO CYS ARG ILE LYS GLN ILE SEQRES 33 A 506 ILE ASN MET TRP GLN ARG ILE GLY GLN ALA MET TYR ALA SEQRES 34 A 506 PRO PRO ILE GLN GLY VAL ILE ARG CYS VAL SER ASN ILE SEQRES 35 A 506 THR GLY LEU ILE LEU THR ARG ASP GLY GLY SER THR ASN SEQRES 36 A 506 SER THR THR GLU THR PHE ARG PRO GLY GLY GLY ASP MET SEQRES 37 A 506 ARG ASP ASN TRP ARG SER GLU LEU TYR LYS TYR LYS VAL SEQRES 38 A 506 VAL LYS ILE GLU PRO LEU GLY VAL ALA PRO THR ARG CYS SEQRES 39 A 506 LYS ARG ARG VAL VAL GLY ARG ARG ARG ARG ARG ARG SEQRES 1 C 506 MET GLY ILE LEU PRO SER PRO GLY MET PRO ALA LEU LEU SEQRES 2 C 506 SER LEU VAL SER LEU LEU SER VAL LEU LEU MET GLY CYS SEQRES 3 C 506 VAL ALA GLU THR GLY ALA GLU ASN LEU TRP VAL THR VAL SEQRES 4 C 506 TYR TYR GLY VAL PRO VAL TRP LYS ASP ALA GLU THR THR SEQRES 5 C 506 LEU PHE CYS ALA SER ASP ALA LYS ALA TYR GLU THR GLU SEQRES 6 C 506 LYS HIS ASN VAL TRP ALA THR HIS ALA CYS VAL PRO THR SEQRES 7 C 506 ASP PRO ASN PRO GLN GLU ILE HIS LEU GLU ASN VAL THR SEQRES 8 C 506 GLU GLU PHE ASN MET TRP LYS ASN ASN MET VAL GLU GLN SEQRES 9 C 506 MET HIS GLU ASP ILE ILE SER LEU TRP ASP GLN SER LEU SEQRES 10 C 506 LYS PRO CYS VAL LYS LEU THR PRO LEU CYS VAL THR LEU SEQRES 11 C 506 GLN CYS THR ASN VAL THR ASN ASN ILE THR ASP ASP MET SEQRES 12 C 506 ARG GLY GLU LEU LYS ASN CYS SER PHE ASN ALA THR THR SEQRES 13 C 506 GLU LEU ARG ASN LYS ARG VAL LYS ARG TYR SER LEU PHE SEQRES 14 C 506 TYR ARG LEU ASP ILE VAL GLN ILE ASP SER ASN ARG ALA SEQRES 15 C 506 LYS SER HIS TYR ARG LEU ILE ASN CYS ASN THR SER ALA SEQRES 16 C 506 ILE THR GLN ALA CYS PRO LYS VAL SER PHE GLU PRO ILE SEQRES 17 C 506 PRO ILE HIS TYR CYS ALA PRO ALA GLY PHE ALA ILE LEU SEQRES 18 C 506 LYS CYS LYS ASP LYS LYS PHE ASN GLY THR GLY PRO CYS SEQRES 19 C 506 PRO SER VAL SER THR VAL GLN CYS THR HIS GLY ILE LYS SEQRES 20 C 506 PRO VAL VAL SER THR GLN LEU LEU LEU ASN GLY SER LEU SEQRES 21 C 506 ALA GLU GLU GLU VAL ILE ILE ARG SER GLU ASN ILE THR SEQRES 22 C 506 ASN ASN ALA LYS ASN ILE LEU VAL GLN LEU ASN THR PRO SEQRES 23 C 506 VAL GLN ILE ASN CYS THR ARG PRO ASN ASN ASN THR VAL SEQRES 24 C 506 LYS SER ILE ARG ILE GLY PRO GLY GLN ALA PHE TYR TYR SEQRES 25 C 506 THR GLY ASP ILE ILE GLY ASP ILE ARG GLN ALA HIS CYS SEQRES 26 C 506 ASN VAL SER LYS ALA THR TRP ASN GLU THR LEU GLY LYS SEQRES 27 C 506 VAL VAL LYS GLN LEU ARG LYS HIS PHE GLY ASN ASN THR SEQRES 28 C 506 ILE ILE ARG PHE ALA GLN SER SER GLY GLY ASP LEU GLU SEQRES 29 C 506 VAL THR THR HIS SER PHE ASN CYS GLY GLY GLU PHE PHE SEQRES 30 C 506 TYR CYS ASN THR SER GLY LEU PHE ASN SER THR TRP ILE SEQRES 31 C 506 SER ASN THR SER VAL GLN GLY SER ASN SER THR GLY SER SEQRES 32 C 506 ASN ASP SER ILE THR LEU PRO CYS ARG ILE LYS GLN ILE SEQRES 33 C 506 ILE ASN MET TRP GLN ARG ILE GLY GLN ALA MET TYR ALA SEQRES 34 C 506 PRO PRO ILE GLN GLY VAL ILE ARG CYS VAL SER ASN ILE SEQRES 35 C 506 THR GLY LEU ILE LEU THR ARG ASP GLY GLY SER THR ASN SEQRES 36 C 506 SER THR THR GLU THR PHE ARG PRO GLY GLY GLY ASP MET SEQRES 37 C 506 ARG ASP ASN TRP ARG SER GLU LEU TYR LYS TYR LYS VAL SEQRES 38 C 506 VAL LYS ILE GLU PRO LEU GLY VAL ALA PRO THR ARG CYS SEQRES 39 C 506 LYS ARG 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 E 506 MET GLY ILE LEU PRO SER PRO GLY MET PRO ALA LEU LEU SEQRES 2 E 506 SER LEU VAL SER LEU LEU SER VAL LEU LEU MET GLY CYS SEQRES 3 E 506 VAL ALA GLU THR GLY ALA GLU ASN LEU TRP VAL THR VAL SEQRES 4 E 506 TYR TYR GLY VAL PRO VAL TRP LYS ASP ALA GLU THR THR SEQRES 5 E 506 LEU PHE CYS ALA SER ASP ALA LYS ALA TYR GLU THR GLU SEQRES 6 E 506 LYS HIS ASN VAL TRP ALA THR HIS ALA CYS VAL PRO THR SEQRES 7 E 506 ASP PRO ASN PRO GLN GLU ILE HIS LEU GLU ASN VAL THR SEQRES 8 E 506 GLU GLU PHE ASN MET TRP LYS ASN ASN MET VAL GLU GLN SEQRES 9 E 506 MET HIS GLU ASP ILE ILE SER LEU TRP ASP GLN SER LEU SEQRES 10 E 506 LYS PRO CYS VAL LYS LEU THR PRO LEU CYS VAL THR LEU SEQRES 11 E 506 GLN CYS THR ASN VAL THR ASN ASN ILE THR ASP ASP MET SEQRES 12 E 506 ARG GLY GLU LEU LYS ASN CYS SER PHE ASN ALA THR THR SEQRES 13 E 506 GLU LEU ARG ASN LYS ARG VAL LYS ARG TYR SER LEU PHE SEQRES 14 E 506 TYR ARG LEU ASP ILE VAL GLN ILE ASP SER ASN ARG ALA SEQRES 15 E 506 LYS SER HIS TYR ARG LEU ILE ASN CYS ASN THR SER ALA SEQRES 16 E 506 ILE THR GLN ALA CYS PRO LYS VAL SER PHE GLU PRO ILE SEQRES 17 E 506 PRO ILE HIS TYR CYS ALA PRO ALA GLY PHE ALA ILE LEU SEQRES 18 E 506 LYS CYS LYS ASP LYS LYS PHE ASN GLY THR GLY PRO CYS SEQRES 19 E 506 PRO SER VAL SER THR VAL GLN CYS THR HIS GLY ILE LYS SEQRES 20 E 506 PRO VAL VAL SER THR GLN LEU LEU LEU ASN GLY SER LEU SEQRES 21 E 506 ALA GLU GLU GLU VAL ILE ILE ARG SER GLU ASN ILE THR SEQRES 22 E 506 ASN ASN ALA LYS ASN ILE LEU VAL GLN LEU ASN THR PRO SEQRES 23 E 506 VAL GLN ILE ASN CYS THR ARG PRO ASN ASN ASN THR VAL SEQRES 24 E 506 LYS SER ILE ARG ILE GLY PRO GLY GLN ALA PHE TYR TYR SEQRES 25 E 506 THR GLY ASP ILE ILE GLY ASP ILE ARG GLN ALA HIS CYS SEQRES 26 E 506 ASN VAL SER LYS ALA THR TRP ASN GLU THR LEU GLY LYS SEQRES 27 E 506 VAL VAL LYS GLN LEU ARG LYS HIS PHE GLY ASN ASN THR SEQRES 28 E 506 ILE ILE ARG PHE ALA GLN SER SER GLY GLY ASP LEU GLU SEQRES 29 E 506 VAL THR THR HIS SER PHE ASN CYS GLY GLY GLU PHE PHE SEQRES 30 E 506 TYR CYS ASN THR SER GLY LEU PHE ASN SER THR TRP ILE SEQRES 31 E 506 SER ASN THR SER VAL GLN GLY SER ASN SER THR GLY SER SEQRES 32 E 506 ASN ASP SER ILE THR LEU PRO CYS ARG ILE LYS GLN ILE SEQRES 33 E 506 ILE ASN MET TRP GLN ARG ILE GLY GLN ALA MET TYR ALA SEQRES 34 E 506 PRO PRO ILE GLN GLY VAL ILE ARG CYS VAL SER ASN ILE SEQRES 35 E 506 THR GLY LEU ILE LEU THR ARG ASP GLY GLY SER THR ASN SEQRES 36 E 506 SER THR THR GLU THR PHE ARG PRO GLY GLY GLY ASP MET SEQRES 37 E 506 ARG ASP ASN TRP ARG SER GLU LEU TYR LYS TYR LYS VAL SEQRES 38 E 506 VAL LYS ILE GLU PRO LEU GLY VAL ALA PRO THR ARG CYS SEQRES 39 E 506 LYS ARG ARG VAL VAL GLY ARG ARG ARG ARG ARG ARG 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 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 L 264 MET LEU ASN SER THR SER LEU PHE ARG PHE LEU PHE CYS SEQRES 2 L 264 ALA VAL THR ASP PRO SER CYS ASP ARG ARG LEU PRO GLU SEQRES 3 L 264 ILE ASN MET TYR ARG MET GLN LEU LEU SER CYS ILE ALA SEQRES 4 L 264 LEU SER LEU ALA LEU VAL THR ASN SER GLN SER ALA LEU SEQRES 5 L 264 THR GLN PRO ALA SER VAL SER GLY SER PRO GLY GLN SER SEQRES 6 L 264 ILE THR ILE SER CYS THR GLY THR SER SER ASP VAL GLY SEQRES 7 L 264 GLY TYR ASN TYR VAL SER TRP TYR GLN GLN HIS PRO GLY SEQRES 8 L 264 LYS ALA PRO LYS LEU MET ILE TYR GLU VAL SER ASN ARG SEQRES 9 L 264 PRO SER GLY VAL SER ASN ARG PHE SER GLY SER LYS SER SEQRES 10 L 264 GLY ASN THR ALA SER LEU THR ILE SER GLY LEU GLN ALA SEQRES 11 L 264 GLU ASP GLU ALA ASP TYR TYR CYS SER SER TYR THR SER SEQRES 12 L 264 SER SER THR VAL VAL PHE GLY GLY GLY THR LYS LEU THR SEQRES 13 L 264 VAL LEU GLY GLN PRO LYS ALA ALA PRO SER VAL THR LEU SEQRES 14 L 264 PHE PRO PRO SER SER GLU GLU LEU GLN ALA ASN LYS ALA SEQRES 15 L 264 THR LEU VAL CYS LEU ILE SER ASP PHE TYR PRO GLY ALA SEQRES 16 L 264 VAL THR VAL ALA TRP LYS ALA ASP SER SER PRO VAL LYS SEQRES 17 L 264 ALA GLY VAL GLU THR THR THR PRO SER LYS GLN SER ASN SEQRES 18 L 264 ASN LYS TYR ALA ALA SER SER TYR LEU SER LEU THR PRO SEQRES 19 L 264 GLU GLN TRP LYS SER HIS ARG SER TYR SER CYS GLN VAL SEQRES 20 L 264 THR HIS GLU GLY SER THR VAL GLU LYS THR VAL ALA PRO SEQRES 21 L 264 THR GLU CYS SER SEQRES 1 H 260 MET TYR ARG MET GLN LEU LEU SER CYS ILE ALA LEU SER SEQRES 2 H 260 LEU ALA LEU VAL THR ASN SER GLN VAL GLN LEU VAL GLU SEQRES 3 H 260 SER GLY GLY GLY VAL VAL GLN PRO GLY ARG SER LEU ARG SEQRES 4 H 260 LEU SER CYS ALA ALA SER GLY PHE THR PHE SER SER TYR SEQRES 5 H 260 GLY MET HIS TRP VAL ARG GLN ALA PRO GLY LYS GLY LEU SEQRES 6 H 260 GLU TRP VAL ALA VAL ILE SER TYR ASP GLY SER ASN LYS SEQRES 7 H 260 TYR TYR ALA ASP SER VAL LYS GLY ARG PHE THR ILE SER SEQRES 8 H 260 ARG ASP ASN SER LYS ASN THR LEU TYR LEU GLN MET ASN SEQRES 9 H 260 SER LEU ARG ALA GLU ASP THR ALA VAL TYR TYR CYS ALA SEQRES 10 H 260 ARG GLU ALA GLY GLY PRO ASP TYR ARG ASN GLY TYS ASN SEQRES 11 H 260 TYR TYS ASP PHE TRP SER GLY TYR TYR TYR TYR TYR TYR SEQRES 12 H 260 MET ASP VAL TRP GLY LYS GLY THR THR VAL THR VAL SER SEQRES 13 H 260 SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA SEQRES 14 H 260 PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU SEQRES 15 H 260 GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR SEQRES 16 H 260 VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS SEQRES 17 H 260 THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER SEQRES 18 H 260 LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY SEQRES 19 H 260 THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER SEQRES 20 H 260 ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER CYS HET TYS H 100E 16 HET TYS H 100H 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 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 D 701 14 HET NAG D 702 14 HET NAG D 703 14 HET NAG E 601 14 HET NAG E 602 14 HET NAG E 603 14 HET NAG E 604 14 HET NAG E 605 14 HET NAG E 606 14 HET NAG E 607 14 HET NAG F 701 14 HET NAG F 702 14 HET NAG F 703 14 HET NAG B 701 14 HET NAG B 702 14 HET NAG B 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 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 NAG O 1 14 HET NAG O 2 14 HET NAG P 1 14 HET NAG P 2 14 HET NAG Q 1 14 HET NAG Q 2 14 HET NAG R 1 14 HET NAG R 2 14 HET NAG S 1 14 HET NAG S 2 14 HET BMA S 3 11 HET MAN S 4 11 HET MAN S 5 11 HET NAG T 1 14 HET NAG T 2 14 HET NAG U 1 14 HET NAG U 2 14 HET BMA U 3 11 HET MAN U 4 11 HET NAG V 1 14 HET NAG V 2 14 HET NAG W 1 14 HET NAG W 2 14 HET NAG X 1 14 HET NAG X 2 14 HET NAG Y 1 14 HET NAG Y 2 14 HET NAG Z 1 14 HET NAG Z 2 14 HET BMA Z 3 11 HET MAN Z 4 11 HET MAN Z 5 11 HET MAN Z 6 11 HET NAG a 1 14 HET NAG a 2 14 HET NAG b 1 14 HET NAG b 2 14 HET NAG c 1 14 HET NAG c 2 14 HET BMA c 3 11 HET MAN c 4 11 HET MAN c 5 11 HET NAG d 1 14 HET NAG d 2 14 HET NAG e 1 14 HET NAG e 2 14 HET NAG f 1 14 HET NAG f 2 14 HET NAG g 1 14 HET NAG g 2 14 HET NAG h 1 14 HET NAG h 2 14 HET NAG i 1 14 HET NAG i 2 14 HET BMA i 3 11 HET MAN i 4 11 HET MAN i 5 11 HET NAG j 1 14 HET NAG j 2 14 HET BMA j 3 11 HET MAN j 4 11 HET MAN j 5 11 HET MAN j 6 11 HET MAN j 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 8 TYS 2(C9 H11 N O6 S) FORMUL 9 NAG 84(C8 H15 N O6) FORMUL 47 BMA 6(C6 H12 O6) FORMUL 47 MAN 14(C6 H12 O6) HELIX 1 AA1 ASN A 99 LYS A 117 1 19 HELIX 2 AA2 LEU A 122 CYS A 126 5 5 HELIX 3 AA3 LYS A 335 ARG A 350 1 16 HELIX 4 AA4 ASP A 368 THR A 372 5 5 HELIX 5 AA5 THR A 387 PHE A 391 5 5 HELIX 6 AA6 SER A 460 THR A 464 5 5 HELIX 7 AA7 MET A 475 TYR A 484 1 10 HELIX 8 AA8 ASN C 99 LYS C 117 1 19 HELIX 9 AA9 LEU C 122 CYS C 126 5 5 HELIX 10 AB1 THR C 139 ARG C 151 5 5 HELIX 11 AB2 LYS C 335 PHE C 353 1 19 HELIX 12 AB3 ASP C 368 THR C 373 1 6 HELIX 13 AB4 ASN C 425 ARG C 429 5 5 HELIX 14 AB5 SER C 460 THR C 464 5 5 HELIX 15 AB6 ASP C 474 ASN C 478 5 5 HELIX 16 AB7 TRP C 479 TYR C 484 1 6 HELIX 17 AB8 GLY D 531 MET D 535 5 5 HELIX 18 AB9 THR D 536 ALA D 541 1 6 HELIX 19 AC1 ARG D 542 LEU D 544 5 3 HELIX 20 AC2 ILE D 573 TRP D 596 1 24 HELIX 21 AC3 ASN D 618 ASN D 625 1 8 HELIX 22 AC4 THR D 627 ILE D 635 1 9 HELIX 23 AC5 TYR D 638 ASP D 659 1 22 HELIX 24 AC6 ASN E 99 LYS E 117 1 19 HELIX 25 AC7 LEU E 122 CYS E 126 5 5 HELIX 26 AC8 THR E 139 ARG E 151 5 5 HELIX 27 AC9 LYS E 335 LYS E 351 1 17 HELIX 28 AD1 ASP E 368 THR E 373 1 6 HELIX 29 AD2 ARG E 476 TYR E 484 1 9 HELIX 30 AD3 THR F 529 SER F 534 1 6 HELIX 31 AD4 THR F 536 ASN F 543 1 8 HELIX 32 AD5 ILE F 573 TRP F 596 1 24 HELIX 33 AD6 ASN F 611 SER F 615 5 5 HELIX 34 AD7 ASN F 618 ASN F 625 1 8 HELIX 35 AD8 THR F 627 SER F 636 1 10 HELIX 36 AD9 TYR F 638 GLN F 650 1 13 HELIX 37 AE1 GLN F 650 LEU F 661 1 12 HELIX 38 AE2 GLY B 531 MET B 535 5 5 HELIX 39 AE3 THR B 536 ASN B 543 1 8 HELIX 40 AE4 ILE B 573 TRP B 596 1 24 HELIX 41 AE5 ASN B 611 SER B 615 5 5 HELIX 42 AE6 ASN B 618 ASP B 624 1 7 HELIX 43 AE7 THR B 627 ILE B 635 1 9 HELIX 44 AE8 TYR B 638 GLN B 650 1 13 HELIX 45 AE9 GLN B 650 GLN B 658 1 9 HELIX 46 AF1 ASP B 659 LEU B 663 5 5 HELIX 47 AF2 GLN L 79 GLU L 83 5 5 HELIX 48 AF3 THR H 28 TYR H 32 5 5 HELIX 49 AF4 ASP H 61 LYS H 64 5 4 HELIX 50 AF5 ARG H 83 THR H 87 5 5 HELIX 51 AF6 ASP H 100I GLY H 100M 5 5 SHEET 1 AA1 3 LEU A 494 VAL A 496 0 SHEET 2 AA1 3 TRP A 35 TYR A 40 -1 N TYR A 39 O GLY A 495 SHEET 3 AA1 3 ILE B 603 PRO B 609 -1 O VAL B 608 N VAL A 36 SHEET 1 AA2 5 TRP A 45 ASP A 47 0 SHEET 2 AA2 5 TYR A 486 ILE A 491 -1 O LYS A 490 N LYS A 46 SHEET 3 AA2 5 PHE A 223 CYS A 228 -1 N LEU A 226 O LYS A 487 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 LEU A 86 -1 N LEU A 86 O VAL A 242 SHEET 1 AA3 3 PHE A 53 ALA A 55 0 SHEET 2 AA3 3 ILE A 215 CYS A 218 -1 O HIS A 216 N ALA A 55 SHEET 3 AA3 3 CYS A 247 ILE A 251 -1 O THR A 248 N TYR A 217 SHEET 1 AA4 2 GLU A 91 GLU A 92 0 SHEET 2 AA4 2 PRO A 238 CYS A 239 -1 O CYS A 239 N GLU A 91 SHEET 1 AA5 3 GLN A 130 ASN A 133 0 SHEET 2 AA5 3 LEU A 154 THR A 162 -1 O ASN A 156 N THR A 132 SHEET 3 AA5 3 ARG A 169 TYR A 177 -1 O VAL A 170 N ALA A 161 SHEET 1 AA6 2 ILE A 181 VAL A 182 0 SHEET 2 AA6 2 ARG A 192 LEU A 193 -1 O ARG A 192 N VAL A 182 SHEET 1 AA7 2 ILE A 201 THR A 202 0 SHEET 2 AA7 2 ALA A 433 MET A 434 1 O ALA A 433 N THR A 202 SHEET 1 AA812 LEU A 259 LEU A 261 0 SHEET 2 AA812 ILE A 271 ARG A 273 0 SHEET 3 AA812 ILE A 284 GLY A 312 -1 O LEU A 285 N ARG A 273 SHEET 4 AA812 GLN A 315 ILE A 322 -1 O GLY A 321 N THR A 303 SHEET 5 AA812 HIS A 330 SER A 334 -1 O HIS A 330 N THR A 297 SHEET 6 AA812 ILE A 359 PHE A 361 0 SHEET 7 AA812 HIS A 374 CYS A 378 0 SHEET 8 AA812 GLU A 381 CYS A 385 -1 O CYS A 385 N HIS A 374 SHEET 9 AA812 SER A 393 TRP A 395 -1 O TRP A 395 N ILE A 359 SHEET 10 AA812 SER A 413 LYS A 421 -1 O ARG A 419 N TYR A 384 SHEET 11 AA812 GLY A 441 ARG A 456 -1 O LEU A 454 N ILE A 284 SHEET 12 AA812 GLU A 466 PRO A 470 -1 O ARG A 469 N THR A 455 SHEET 1 AA9 3 LEU C 494 THR C 499 0 SHEET 2 AA9 3 TRP C 35 TYR C 40 -1 N TYR C 39 O GLY C 495 SHEET 3 AA9 3 ILE D 603 PRO D 609 -1 O VAL D 608 N VAL C 36 SHEET 1 AB1 5 TRP C 45 ASP C 47 0 SHEET 2 AB1 5 TYR C 486 ILE C 491 -1 O LYS C 490 N LYS C 46 SHEET 3 AB1 5 PHE C 223 CYS C 228 -1 N LEU C 226 O LYS C 487 SHEET 4 AB1 5 VAL C 242 VAL C 245 -1 O SER C 243 N LYS C 227 SHEET 5 AB1 5 ILE C 84 HIS C 85 -1 N ILE C 84 O THR C 244 SHEET 1 AB2 2 GLU C 91 ASN C 94 0 SHEET 2 AB2 2 THR C 236 CYS C 239 -1 O GLY C 237 N PHE C 93 SHEET 1 AB3 5 ARG C 169 TYR C 177 0 SHEET 2 AB3 5 LEU C 154 THR C 162 -1 N PHE C 159 O ARG C 172 SHEET 3 AB3 5 LEU C 129 THR C 132 -1 N GLN C 130 O SER C 158 SHEET 4 AB3 5 HIS C 190 LEU C 193 -1 O TYR C 191 N LEU C 129 SHEET 5 AB3 5 ILE C 181 ASP C 185 -1 N VAL C 182 O ARG C 192 SHEET 1 AB4 2 ILE C 215 CYS C 218 0 SHEET 2 AB4 2 CYS C 247 ILE C 251 -1 O THR C 248 N TYR C 217 SHEET 1 AB511 LEU C 259 LEU C 261 0 SHEET 2 AB511 ILE C 271 ARG C 273 0 SHEET 3 AB511 ILE C 284 ARG C 298 -1 O LEU C 285 N ARG C 273 SHEET 4 AB511 HIS C 330 SER C 334 -1 O ASN C 332 N ASN C 295 SHEET 5 AB511 ILE C 359 PHE C 361 0 SHEET 6 AB511 HIS C 374 CYS C 378 0 SHEET 7 AB511 GLU C 381 CYS C 385 -1 O CYS C 385 N HIS C 374 SHEET 8 AB511 SER C 393 TRP C 395 -1 O TRP C 395 N ILE C 359 SHEET 9 AB511 SER C 413 ILE C 420 -1 O ARG C 419 N TYR C 384 SHEET 10 AB511 ILE C 443 ARG C 456 -1 O LEU C 452 N VAL C 286 SHEET 11 AB511 THR C 467 PRO C 470 -1 O ARG C 469 N THR C 455 SHEET 1 AB6 2 ASN C 301 GLY C 312 0 SHEET 2 AB6 2 GLN C 315 ILE C 323 -1 O GLN C 315 N ILE C 309 SHEET 1 AB7 2 ILE C 423 ILE C 424 0 SHEET 2 AB7 2 MET C 434 TYR C 435 -1 O MET C 434 N ILE C 424 SHEET 1 AB8 3 LEU E 494 VAL E 496 0 SHEET 2 AB8 3 TRP E 35 TYR E 40 -1 N TYR E 39 O GLY E 495 SHEET 3 AB8 3 ILE F 603 PRO F 609 -1 O VAL F 608 N VAL E 36 SHEET 1 AB9 4 TRP E 45 ASP E 47 0 SHEET 2 AB9 4 TYR E 486 ILE E 491 -1 O LYS E 490 N LYS E 46 SHEET 3 AB9 4 PHE E 223 CYS E 228 -1 N LEU E 226 O LYS E 487 SHEET 4 AB9 4 VAL E 242 VAL E 245 -1 O VAL E 245 N ILE E 225 SHEET 1 AC1 3 VAL E 75 PRO E 76 0 SHEET 2 AC1 3 PHE E 53 SER E 56 1 N CYS E 54 O VAL E 75 SHEET 3 AC1 3 HIS E 216 CYS E 218 -1 O HIS E 216 N ALA E 55 SHEET 1 AC2 2 GLU E 91 GLU E 92 0 SHEET 2 AC2 2 PRO E 238 CYS E 239 -1 O CYS E 239 N GLU E 91 SHEET 1 AC3 7 ILE E 181 GLN E 183 0 SHEET 2 AC3 7 HIS E 190 LEU E 193 -1 O ARG E 192 N VAL E 182 SHEET 3 AC3 7 LEU E 129 ASN E 133 -1 N LEU E 129 O TYR E 191 SHEET 4 AC3 7 LEU E 154 THR E 162 -1 O SER E 158 N GLN E 130 SHEET 5 AC3 7 LYS E 168 TYR E 177 -1 O ARG E 172 N PHE E 159 SHEET 6 AC3 7 TYS H 100E TYS H 100H 1 O TYS H 100H N ARG E 169 SHEET 7 AC3 7 ASP H 100 ARG H 100B-1 N ARG H 100B O TYS H 100E SHEET 1 AC4 3 ILE E 201 THR E 202 0 SHEET 2 AC4 3 ALA E 433 TYR E 435 1 O ALA E 433 N THR E 202 SHEET 3 AC4 3 ILE E 423 ILE E 424 -1 N ILE E 424 O MET E 434 SHEET 1 AC511 LEU E 259 LEU E 261 0 SHEET 2 AC511 ILE E 271 ARG E 273 0 SHEET 3 AC511 ILE E 284 GLY E 312 -1 O LEU E 285 N ARG E 273 SHEET 4 AC511 GLN E 315 ILE E 323 -1 O GLN E 315 N ILE E 309 SHEET 5 AC511 ALA E 329 SER E 334 -1 O ASN E 332 N ASN E 295 SHEET 6 AC511 ILE E 359 PHE E 361 0 SHEET 7 AC511 HIS E 374 CYS E 378 0 SHEET 8 AC511 GLU E 381 CYS E 385 -1 O CYS E 385 N HIS E 374 SHEET 9 AC511 SER E 413 LYS E 421 -1 O ARG E 419 N TYR E 384 SHEET 10 AC511 GLY E 441 ARG E 456 -1 O LEU E 454 N ILE E 284 SHEET 11 AC511 GLU E 466 PRO E 470 -1 O ARG E 469 N THR E 455 SHEET 1 AC6 6 SER L 9 GLY L 13 0 SHEET 2 AC6 6 VAL L 33 GLN L 38 0 SHEET 3 AC6 6 LYS L 45 ILE L 48 -1 O MET L 47 N TRP L 35 SHEET 4 AC6 6 ASP L 85 TYR L 91 -1 O ASP L 85 N GLN L 38 SHEET 5 AC6 6 VAL L 96 PHE L 98 -1 O VAL L 97 N SER L 90 SHEET 6 AC6 6 THR L 102 VAL L 106 -1 O THR L 102 N TYR L 86 SHEET 1 AC7 3 SER L 18 THR L 24 0 SHEET 2 AC7 3 THR L 70 SER L 76 -1 O ALA L 71 N CYS L 23 SHEET 3 AC7 3 PHE L 62 SER L 67 -1 N SER L 65 O SER L 72 SHEET 1 AC8 4 GLN H 3 SER H 7 0 SHEET 2 AC8 4 LEU H 18 SER H 25 -1 O ALA H 23 N VAL H 5 SHEET 3 AC8 4 THR H 77 MET H 82 -1 O MET H 82 N LEU H 18 SHEET 4 AC8 4 PHE H 67 ASP H 72 -1 N SER H 70 O TYR H 79 SHEET 1 AC9 7 VAL H 11 VAL H 12 0 SHEET 2 AC9 7 MET H 34 GLN H 39 0 SHEET 3 AC9 7 GLU H 46 ILE H 51 -1 O GLU H 46 N ARG H 38 SHEET 4 AC9 7 LYS H 57 TYR H 59 -1 O TYR H 58 N VAL H 50 SHEET 5 AC9 7 ALA H 88 GLY H 98 -1 O TYR H 91 N VAL H 37 SHEET 6 AC9 7 TYR H 100O TRP H 103 -1 O TYR H 100O N GLY H 98 SHEET 7 AC9 7 THR H 107 VAL H 111 -1 O THR H 107 N TYR H 90 SSBOND 1 CYS A 54 CYS A 74 1555 1555 2.21 SSBOND 2 CYS A 119 CYS A 205 1555 1555 2.07 SSBOND 3 CYS A 126 CYS A 196 1555 1555 2.06 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 2.04 SSBOND 7 CYS A 296 CYS A 331 1555 1555 2.03 SSBOND 8 CYS A 378 CYS A 445 1555 1555 2.01 SSBOND 9 CYS A 385 CYS A 418 1555 1555 2.02 SSBOND 10 CYS A 501 CYS B 605 1555 1555 2.03 SSBOND 11 CYS C 54 CYS C 74 1555 1555 2.10 SSBOND 12 CYS C 119 CYS C 205 1555 1555 2.09 SSBOND 13 CYS C 126 CYS C 196 1555 1555 2.04 SSBOND 14 CYS C 218 CYS C 247 1555 1555 2.03 SSBOND 15 CYS C 228 CYS C 239 1555 1555 2.03 SSBOND 16 CYS C 296 CYS C 331 1555 1555 2.02 SSBOND 17 CYS C 378 CYS C 445 1555 1555 2.02 SSBOND 18 CYS C 385 CYS C 418 1555 1555 2.03 SSBOND 19 CYS C 501 CYS D 605 1555 1555 2.04 SSBOND 20 CYS D 598 CYS D 604 1555 1555 2.02 SSBOND 21 CYS E 54 CYS E 74 1555 1555 2.15 SSBOND 22 CYS E 119 CYS E 205 1555 1555 2.20 SSBOND 23 CYS E 126 CYS E 196 1555 1555 2.05 SSBOND 24 CYS E 131 CYS E 157 1555 1555 2.01 SSBOND 25 CYS E 218 CYS E 247 1555 1555 2.03 SSBOND 26 CYS E 228 CYS E 239 1555 1555 2.13 SSBOND 27 CYS E 296 CYS E 331 1555 1555 2.03 SSBOND 28 CYS E 378 CYS E 445 1555 1555 2.02 SSBOND 29 CYS E 385 CYS E 418 1555 1555 2.03 SSBOND 30 CYS E 501 CYS F 605 1555 1555 2.03 SSBOND 31 CYS F 598 CYS F 604 1555 1555 2.03 SSBOND 32 CYS B 598 CYS B 604 1555 1555 2.02 SSBOND 33 CYS L 23 CYS L 88 1555 1555 2.02 SSBOND 34 CYS H 22 CYS H 92 1555 1555 2.03 LINK ND2 ASN A 88 C1 NAG A 601 1555 1555 1.52 LINK ND2 ASN A 133 C1 NAG A 605 1555 1555 1.53 LINK ND2 ASN A 137 C1 NAG A 602 1555 1555 1.52 LINK ND2 ASN A 156 C1 NAG G 1 1555 1555 1.51 LINK ND2 ASN A 160 C1 NAG I 1 1555 1555 1.52 LINK ND2 ASN A 197 C1 NAG J 1 1555 1555 1.53 LINK ND2 ASN A 234 C1 NAG K 1 1555 1555 1.54 LINK ND2 ASN A 262 C1 NAG S 1 1555 1555 1.43 LINK ND2 ASN A 276 C1 NAG A 604 1555 1555 1.53 LINK ND2 ASN A 295 C1 NAG M 1 1555 1555 1.51 LINK ND2 ASN A 301 C1 NAG N 1 1555 1555 1.52 LINK ND2 ASN A 332 C1 NAG O 1 1555 1555 1.51 LINK ND2 ASN A 355 C1 NAG A 603 1555 1555 1.53 LINK ND2 ASN A 386 C1 NAG P 1 1555 1555 1.52 LINK ND2 ASN A 392 C1 NAG Q 1 1555 1555 1.52 LINK ND2 ASN A 448 C1 NAG R 1 1555 1555 1.53 LINK ND2 ASN C 88 C1 NAG C 607 1555 1555 1.47 LINK ND2 ASN C 133 C1 NAG C 601 1555 1555 1.51 LINK ND2 ASN C 156 C1 NAG a 1 1555 1555 1.45 LINK ND2 ASN C 160 C1 NAG Z 1 1555 1555 1.42 LINK ND2 ASN C 197 C1 NAG T 1 1555 1555 1.51 LINK ND2 ASN C 234 C1 NAG C 605 1555 1555 1.46 LINK ND2 ASN C 262 C1 NAG U 1 1555 1555 1.44 LINK ND2 ASN C 276 C1 NAG C 604 1555 1555 1.45 LINK ND2 ASN C 295 C1 NAG C 602 1555 1555 1.51 LINK ND2 ASN C 301 C1 NAG C 606 1555 1555 1.46 LINK ND2 ASN C 332 C1 NAG V 1 1555 1555 1.50 LINK ND2 ASN C 355 C1 NAG C 603 1555 1555 1.52 LINK ND2 ASN C 386 C1 NAG W 1 1555 1555 1.53 LINK ND2 ASN C 392 C1 NAG X 1 1555 1555 1.52 LINK ND2 ASN C 448 C1 NAG Y 1 1555 1555 1.52 LINK ND2 ASN D 611 C1 NAG D 701 1555 1555 1.52 LINK ND2 ASN D 618 C1 NAG D 702 1555 1555 1.52 LINK ND2 ASN D 637 C1 NAG D 703 1555 1555 1.52 LINK ND2 ASN E 88 C1 NAG E 606 1555 1555 1.52 LINK ND2 ASN E 133 C1 NAG E 601 1555 1555 1.53 LINK ND2 ASN E 156 C1 NAG j 1 1555 1555 1.43 LINK ND2 ASN E 160 C1 NAG i 1 1555 1555 1.43 LINK ND2 ASN E 197 C1 NAG b 1 1555 1555 1.52 LINK ND2 ASN E 262 C1 NAG c 1 1555 1555 1.43 LINK ND2 ASN E 276 C1 NAG E 602 1555 1555 1.53 LINK ND2 ASN E 295 C1 NAG E 603 1555 1555 1.52 LINK ND2 ASN E 301 C1 NAG d 1 1555 1555 1.53 LINK ND2 ASN E 332 C1 NAG e 1 1555 1555 1.52 LINK ND2 ASN E 355 C1 NAG E 604 1555 1555 1.52 LINK ND2 ASN E 386 C1 NAG f 1 1555 1555 1.53 LINK ND2 ASN E 392 C1 NAG g 1 1555 1555 1.52 LINK ND2 ASN E 448 C1 NAG h 1 1555 1555 1.52 LINK ND2 ASN E 462 C1 NAG E 605 1555 1555 1.53 LINK ND2 ASN F 611 C1 NAG F 701 1555 1555 1.51 LINK ND2 ASN F 618 C1 NAG F 702 1555 1555 1.52 LINK ND2 ASN F 637 C1 NAG F 703 1555 1555 1.52 LINK ND2 ASN B 611 C1 NAG B 701 1555 1555 1.52 LINK ND2 ASN B 618 C1 NAG B 702 1555 1555 1.52 LINK ND2 ASN B 637 C1 NAG B 703 1555 1555 1.53 LINK C GLY H 100D N TYS H 100E 1555 1555 1.34 LINK C TYS H 100E N ASN H 100F 1555 1555 1.34 LINK C TYR H 100G N TYS H 100H 1555 1555 1.33 LINK C TYS H 100H N ASP H 100I 1555 1555 1.33 LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.50 LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.52 LINK O4 NAG J 1 C1 NAG J 2 1555 1555 1.52 LINK O4 NAG K 1 C1 NAG K 2 1555 1555 1.52 LINK O4 NAG M 1 C1 NAG M 2 1555 1555 1.51 LINK O4 NAG N 1 C1 NAG N 2 1555 1555 1.53 LINK O4 NAG O 1 C1 NAG O 2 1555 1555 1.51 LINK O4 NAG P 1 C1 NAG P 2 1555 1555 1.51 LINK O4 NAG Q 1 C1 NAG Q 2 1555 1555 1.52 LINK O4 NAG R 1 C1 NAG R 2 1555 1555 1.54 LINK O4 NAG S 1 C1 NAG S 2 1555 1555 1.44 LINK O4 NAG S 2 C1 BMA S 3 1555 1555 1.44 LINK O3 BMA S 3 C1 MAN S 4 1555 1555 1.44 LINK O6 BMA S 3 C1 MAN S 5 1555 1555 1.44 LINK O4 NAG T 1 C1 NAG T 2 1555 1555 1.51 LINK O4 NAG U 1 C1 NAG U 2 1555 1555 1.43 LINK O4 NAG U 2 C1 BMA U 3 1555 1555 1.44 LINK O3 BMA U 3 C1 MAN U 4 1555 1555 1.44 LINK O4 NAG V 1 C1 NAG V 2 1555 1555 1.51 LINK O4 NAG W 1 C1 NAG W 2 1555 1555 1.50 LINK O4 NAG X 1 C1 NAG X 2 1555 1555 1.52 LINK O4 NAG Y 1 C1 NAG Y 2 1555 1555 1.52 LINK O4 NAG Z 1 C1 NAG Z 2 1555 1555 1.43 LINK O4 NAG Z 2 C1 BMA Z 3 1555 1555 1.44 LINK O6 BMA Z 3 C1 MAN Z 4 1555 1555 1.43 LINK O3 BMA Z 3 C1 MAN Z 6 1555 1555 1.44 LINK O6 MAN Z 4 C1 MAN Z 5 1555 1555 1.44 LINK O4 NAG a 1 C1 NAG a 2 1555 1555 1.44 LINK O4 NAG b 1 C1 NAG b 2 1555 1555 1.51 LINK O4 NAG c 1 C1 NAG c 2 1555 1555 1.44 LINK O4 NAG c 2 C1 BMA c 3 1555 1555 1.44 LINK O3 BMA c 3 C1 MAN c 4 1555 1555 1.43 LINK O6 BMA c 3 C1 MAN c 5 1555 1555 1.44 LINK O4 NAG d 1 C1 NAG d 2 1555 1555 1.51 LINK O4 NAG e 1 C1 NAG e 2 1555 1555 1.53 LINK O4 NAG f 1 C1 NAG f 2 1555 1555 1.51 LINK O4 NAG g 1 C1 NAG g 2 1555 1555 1.53 LINK O4 NAG h 1 C1 NAG h 2 1555 1555 1.51 LINK O4 NAG i 1 C1 NAG i 2 1555 1555 1.44 LINK O4 NAG i 2 C1 BMA i 3 1555 1555 1.44 LINK O3 BMA i 3 C1 MAN i 4 1555 1555 1.44 LINK O6 BMA i 3 C1 MAN i 5 1555 1555 1.44 LINK O4 NAG j 1 C1 NAG j 2 1555 1555 1.44 LINK O4 NAG j 2 C1 BMA j 3 1555 1555 1.44 LINK O6 BMA j 3 C1 MAN j 4 1555 1555 1.44 LINK O3 BMA j 3 C1 MAN j 7 1555 1555 1.44 LINK O3 MAN j 4 C1 MAN j 5 1555 1555 1.44 LINK O6 MAN j 4 C1 MAN j 6 1555 1555 1.44 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 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