HEADER VIRAL PROTEIN/IMMUNE SYSTEM 16-AUG-24 9D7I TITLE CRYO-EM STRUCTURE OF BG505 DS-SOSIP.664 WITH 2 CH103 KN FABS BOUND COMPND MOL_ID: 1; COMPND 2 MOLECULE: SURFACE PROTEIN GP120; COMPND 3 CHAIN: A, C, E; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: TRANSMEMBRANE PROTEIN GP41; COMPND 7 CHAIN: B, D, F; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: CH103 FAB LIGHT CHAIN; COMPND 11 CHAIN: G, I; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 4; COMPND 14 MOLECULE: CH103 K75 N76 FAB HEAVY CHAIN; COMPND 15 CHAIN: H, J; COMPND 16 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 3 ORGANISM_TAXID: 11676; SOURCE 4 VARIANT: BG505; SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 9 ORGANISM_TAXID: 11676; SOURCE 10 VARIANT: BG505; SOURCE 11 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 13 MOL_ID: 3; SOURCE 14 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 15 ORGANISM_TAXID: 9606; SOURCE 16 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 18 MOL_ID: 4; SOURCE 19 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 20 ORGANISM_TAXID: 9606; SOURCE 21 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 22 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS TRIMER, ENV, BG505, CH103, VIRAL PROTEIN, VIRAL PROTEIN-IMMUNE SYSTEM KEYWDS 2 COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR R.J.PARSONS,P.ACHARYA REVDAT 1 04-JUN-25 9D7I 0 JRNL AUTH Q.LIU,R.J.PARSONS,K.WIEHE,R.J.EDWARDS,K.O.SAUNDERS,P.ZHANG, JRNL AUTH 2 H.MIAO,K.TILAHUN,J.JONES,Y.CHEN,B.HORA,W.B.WILLIAMS, JRNL AUTH 3 D.EASTERHOFF,X.HUANG,K.JANOWSKA,K.MANSOURI,B.F.HAYNES, JRNL AUTH 4 P.ACHARYA,P.LUSSO JRNL TITL ACQUISITION OF QUATERNARY TRIMER INTERACTION AS A KEY STEP JRNL TITL 2 IN THE LINEAGE MATURATION OF A BROAD AND POTENT HIV-1 JRNL TITL 3 NEUTRALIZING ANTIBODY. JRNL REF STRUCTURE 2025 JRNL REFN ISSN 0969-2126 JRNL PMID 40412376 JRNL DOI 10.1016/J.STR.2025.04.020 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH D.LIEBSCHNER,P.V.AFONINE,M.L.BAKER,G.BUNKOCZI,V.B.CHEN, REMARK 1 AUTH 2 T.I.CROLL,B.HINTZE,L.W.HUNG,S.JAIN,A.J.MCCOY,N.W.MORIARTY, REMARK 1 AUTH 3 R.D.OEFFNER,B.K.POON,M.G.PRISANT,R.J.READ,J.S.RICHARDSON, REMARK 1 AUTH 4 D.C.RICHARDSON,M.D.SAMMITO,O.V.SOBOLEV,D.H.STOCKWELL, REMARK 1 AUTH 5 T.C.TERWILLIGER,A.G.URZHUMTSEV,L.L.VIDEAU,C.J.WILLIAMS, REMARK 1 AUTH 6 P.D.ADAMS REMARK 1 TITL MACROMOLECULAR STRUCTURE DETERMINATION USING X-RAYS, REMARK 1 TITL 2 NEUTRONS AND ELECTRONS: RECENT DEVELOPMENTS IN PHENIX REMARK 1 REF ACTA CRYSTALLOGR., SECT. D: V. 75 861 2019 REMARK 1 REF 2 BIOL. CRYSTALLOGR. REMARK 1 REFN ISSN 0907-4449 REMARK 1 PMID 31588918 REMARK 1 DOI 10.1107/S2059798319011471 REMARK 2 REMARK 2 RESOLUTION. 3.68 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : PHENIX 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) : 3.680 REMARK 3 NUMBER OF PARTICLES : 73518 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 9D7I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-AUG-24. REMARK 100 THE DEPOSITION ID IS D_1000287319. REMARK 245 REMARK 245 EXPERIMENTAL DETAILS REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE REMARK 245 SPECIMEN TYPE : NULL REMARK 245 REMARK 245 ELECTRON MICROSCOPE SAMPLE REMARK 245 SAMPLE TYPE : PARTICLE REMARK 245 PARTICLE TYPE : POINT REMARK 245 NAME OF SAMPLE : BG505 HIV-1 ENV WITH 2 CH103 REMARK 245 K75 N76 FABS BOUND REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : LEICA EM GP2 REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 8.00 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : TFS KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 BIOQUANTUM (6K X REMARK 245 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1400.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 1800.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : NULL REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 5910.00 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : NULL REMARK 245 CALIBRATED MAGNIFICATION : NULL REMARK 245 SOURCE : FIELD EMISSION GUN REMARK 245 ACCELERATION VOLTAGE (KV) : 300 REMARK 245 IMAGING DETAILS : NULL REMARK 247 REMARK 247 ELECTRON MICROSCOPY REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION REMARK 247 OF THE STRUCTURE FACTORS. REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DECAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J, REMARK 350 AND CHAINS: K, L, M, N, O, P, 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 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 7 REMARK 465 PRO A 8 REMARK 465 MET A 9 REMARK 465 GLY A 10 REMARK 465 SER A 11 REMARK 465 LEU A 12 REMARK 465 GLN A 13 REMARK 465 PRO A 14 REMARK 465 LEU A 15 REMARK 465 ALA A 16 REMARK 465 THR A 17 REMARK 465 LEU A 18 REMARK 465 TYR A 19 REMARK 465 LEU A 20 REMARK 465 LEU A 21 REMARK 465 GLY A 22 REMARK 465 MET A 23 REMARK 465 LEU A 24 REMARK 465 VAL A 25 REMARK 465 ALA A 26 REMARK 465 SER A 27 REMARK 465 VAL A 28 REMARK 465 LEU A 29 REMARK 465 ALA A 30 REMARK 465 ALA A 31 REMARK 465 GLU A 32 REMARK 465 ASN A 33 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 HIS A 66 REMARK 465 ASN A 136 REMARK 465 ASN A 137 REMARK 465 ILE A 138 REMARK 465 THR A 139 REMARK 465 ASP A 140 REMARK 465 ASP A 141 REMARK 465 MET A 142 REMARK 465 ARG A 143 REMARK 465 GLU A 178 REMARK 465 ASN A 179 REMARK 465 GLN A 180 REMARK 465 GLY A 181 REMARK 465 ASN A 182 REMARK 465 ARG A 183 REMARK 465 SER A 184 REMARK 465 ASN A 185 REMARK 465 ASN A 186 REMARK 465 SER A 187 REMARK 465 ASN A 399 REMARK 465 THR A 400 REMARK 465 SER A 401 REMARK 465 VAL A 402 REMARK 465 GLN A 403 REMARK 465 GLY A 404 REMARK 465 SER A 405 REMARK 465 ASN A 406 REMARK 465 SER A 407 REMARK 465 THR A 408 REMARK 465 GLY A 409 REMARK 465 SER A 410 REMARK 465 ASN A 411 REMARK 465 VAL B 503 REMARK 465 VAL B 504 REMARK 465 GLY B 505 REMARK 465 ARG B 506 REMARK 465 ARG B 507 REMARK 465 ARG B 508 REMARK 465 ARG B 509 REMARK 465 ARG B 510 REMARK 465 ARG B 511 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 PHE B 519 REMARK 465 LEU B 520 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 ALA 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 664 REMARK 465 MET C 7 REMARK 465 PRO C 8 REMARK 465 MET C 9 REMARK 465 GLY C 10 REMARK 465 SER C 11 REMARK 465 LEU C 12 REMARK 465 GLN C 13 REMARK 465 PRO C 14 REMARK 465 LEU C 15 REMARK 465 ALA C 16 REMARK 465 THR C 17 REMARK 465 LEU C 18 REMARK 465 TYR C 19 REMARK 465 LEU C 20 REMARK 465 LEU C 21 REMARK 465 GLY C 22 REMARK 465 MET C 23 REMARK 465 LEU C 24 REMARK 465 VAL C 25 REMARK 465 ALA C 26 REMARK 465 SER C 27 REMARK 465 VAL C 28 REMARK 465 LEU C 29 REMARK 465 ALA C 30 REMARK 465 ALA C 31 REMARK 465 GLU C 32 REMARK 465 ASN C 33 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 GLU C 178 REMARK 465 ASN C 179 REMARK 465 GLN C 180 REMARK 465 GLY C 181 REMARK 465 ASN C 182 REMARK 465 ARG C 183 REMARK 465 SER C 184 REMARK 465 ASN C 185 REMARK 465 ASN C 186 REMARK 465 SER C 187 REMARK 465 ASN C 399 REMARK 465 THR C 400 REMARK 465 SER C 401 REMARK 465 VAL C 402 REMARK 465 GLN C 403 REMARK 465 GLY C 404 REMARK 465 SER C 405 REMARK 465 ASN C 406 REMARK 465 SER C 407 REMARK 465 THR C 408 REMARK 465 GLY C 409 REMARK 465 SER C 410 REMARK 465 VAL D 503 REMARK 465 VAL D 504 REMARK 465 GLY D 505 REMARK 465 ARG D 506 REMARK 465 ARG D 507 REMARK 465 ARG D 508 REMARK 465 ARG D 509 REMARK 465 ARG D 510 REMARK 465 ARG D 511 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 PHE D 519 REMARK 465 LEU D 520 REMARK 465 GLY D 547 REMARK 465 ILE D 548 REMARK 465 VAL D 549 REMARK 465 GLN D 550 REMARK 465 GLN D 551 REMARK 465 GLN D 552 REMARK 465 SER D 553 REMARK 465 ASN D 554 REMARK 465 LEU D 555 REMARK 465 LEU D 556 REMARK 465 ARG D 557 REMARK 465 ALA D 558 REMARK 465 PRO D 559 REMARK 465 GLU D 560 REMARK 465 ALA D 561 REMARK 465 GLN D 562 REMARK 465 GLN D 563 REMARK 465 HIS D 564 REMARK 465 LEU D 565 REMARK 465 LEU D 566 REMARK 465 LYS D 567 REMARK 465 LEU D 568 REMARK 465 ASP D 664 REMARK 465 MET E 7 REMARK 465 PRO E 8 REMARK 465 MET E 9 REMARK 465 GLY E 10 REMARK 465 SER E 11 REMARK 465 LEU E 12 REMARK 465 GLN E 13 REMARK 465 PRO E 14 REMARK 465 LEU E 15 REMARK 465 ALA E 16 REMARK 465 THR E 17 REMARK 465 LEU E 18 REMARK 465 TYR E 19 REMARK 465 LEU E 20 REMARK 465 LEU E 21 REMARK 465 GLY E 22 REMARK 465 MET E 23 REMARK 465 LEU E 24 REMARK 465 VAL E 25 REMARK 465 ALA E 26 REMARK 465 SER E 27 REMARK 465 VAL E 28 REMARK 465 LEU E 29 REMARK 465 ALA E 30 REMARK 465 ALA E 31 REMARK 465 GLU E 32 REMARK 465 ASN E 33 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 HIS E 66 REMARK 465 GLU E 178 REMARK 465 ASN E 179 REMARK 465 GLN E 180 REMARK 465 GLY E 181 REMARK 465 ASN E 182 REMARK 465 ARG E 183 REMARK 465 SER E 184 REMARK 465 ASN E 185 REMARK 465 ASN E 186 REMARK 465 SER E 187 REMARK 465 ASN E 399 REMARK 465 THR E 400 REMARK 465 SER E 401 REMARK 465 VAL E 402 REMARK 465 GLN E 403 REMARK 465 GLY E 404 REMARK 465 SER E 405 REMARK 465 ASN E 406 REMARK 465 SER E 407 REMARK 465 THR E 408 REMARK 465 GLY E 409 REMARK 465 SER E 410 REMARK 465 VAL F 503 REMARK 465 VAL F 504 REMARK 465 GLY F 505 REMARK 465 ARG F 506 REMARK 465 ARG F 507 REMARK 465 ARG F 508 REMARK 465 ARG F 509 REMARK 465 ARG F 510 REMARK 465 ARG F 511 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 PHE F 519 REMARK 465 LEU F 520 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 ALA F 561 REMARK 465 GLN F 562 REMARK 465 GLN F 563 REMARK 465 HIS F 564 REMARK 465 LEU F 565 REMARK 465 LEU F 566 REMARK 465 LYS F 567 REMARK 465 LEU F 568 REMARK 465 ASP F 664 REMARK 465 MET G -18 REMARK 465 GLY G -17 REMARK 465 TRP G -16 REMARK 465 SER G -15 REMARK 465 CYS G -14 REMARK 465 ILE G -13 REMARK 465 ILE G -12 REMARK 465 LEU G -11 REMARK 465 PHE G -10 REMARK 465 LEU G -9 REMARK 465 VAL G -8 REMARK 465 ALA G -7 REMARK 465 THR G -6 REMARK 465 ALA G -5 REMARK 465 THR G -4 REMARK 465 GLY G -3 REMARK 465 SER G -2 REMARK 465 TRP G -1 REMARK 465 ALA G 0 REMARK 465 SER G 1 REMARK 465 SER G 122 REMARK 465 GLU G 123 REMARK 465 GLU G 124 REMARK 465 LEU G 125 REMARK 465 GLN G 126 REMARK 465 ALA G 127 REMARK 465 ASN G 128 REMARK 465 LYS G 129 REMARK 465 ASP G 151 REMARK 465 SER G 152 REMARK 465 GLU G 183 REMARK 465 LYS G 186 REMARK 465 VAL G 206 REMARK 465 THR G 209 REMARK 465 GLU G 210 REMARK 465 CYS G 211 REMARK 465 SER G 212 REMARK 465 MET H -18 REMARK 465 GLY H -17 REMARK 465 TRP H -16 REMARK 465 SER H -15 REMARK 465 CYS H -14 REMARK 465 ILE H -13 REMARK 465 ILE H -12 REMARK 465 LEU H -11 REMARK 465 PHE H -10 REMARK 465 LEU H -9 REMARK 465 VAL H -8 REMARK 465 ALA H -7 REMARK 465 THR H -6 REMARK 465 ALA H -5 REMARK 465 THR H -4 REMARK 465 GLY H -3 REMARK 465 VAL H -2 REMARK 465 HIS H -1 REMARK 465 SER H 0 REMARK 465 GLN H 1 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 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 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 H 218 REMARK 465 MET I -18 REMARK 465 GLY I -17 REMARK 465 TRP I -16 REMARK 465 SER I -15 REMARK 465 CYS I -14 REMARK 465 ILE I -13 REMARK 465 ILE I -12 REMARK 465 LEU I -11 REMARK 465 PHE I -10 REMARK 465 LEU I -9 REMARK 465 VAL I -8 REMARK 465 ALA I -7 REMARK 465 THR I -6 REMARK 465 ALA I -5 REMARK 465 THR I -4 REMARK 465 GLY I -3 REMARK 465 SER I -2 REMARK 465 TRP I -1 REMARK 465 ALA I 0 REMARK 465 SER I 1 REMARK 465 SER I 122 REMARK 465 GLU I 123 REMARK 465 GLU I 124 REMARK 465 LEU I 125 REMARK 465 GLN I 126 REMARK 465 ALA I 127 REMARK 465 ASN I 128 REMARK 465 LYS I 129 REMARK 465 ASP I 151 REMARK 465 SER I 152 REMARK 465 GLU I 183 REMARK 465 LYS I 186 REMARK 465 VAL I 206 REMARK 465 THR I 209 REMARK 465 GLU I 210 REMARK 465 CYS I 211 REMARK 465 SER I 212 REMARK 465 MET J -18 REMARK 465 GLY J -17 REMARK 465 TRP J -16 REMARK 465 SER J -15 REMARK 465 CYS J -14 REMARK 465 ILE J -13 REMARK 465 ILE J -12 REMARK 465 LEU J -11 REMARK 465 PHE J -10 REMARK 465 LEU J -9 REMARK 465 VAL J -8 REMARK 465 ALA J -7 REMARK 465 THR J -6 REMARK 465 ALA J -5 REMARK 465 THR J -4 REMARK 465 GLY J -3 REMARK 465 VAL J -2 REMARK 465 HIS J -1 REMARK 465 SER J 0 REMARK 465 GLN J 1 REMARK 465 PHE J 122 REMARK 465 PRO J 123 REMARK 465 LEU J 124 REMARK 465 ALA J 125 REMARK 465 PRO J 126 REMARK 465 SER J 127 REMARK 465 SER J 128 REMARK 465 LYS J 129 REMARK 465 SER J 130 REMARK 465 THR J 131 REMARK 465 SER J 132 REMARK 465 GLY J 133 REMARK 465 GLY J 134 REMARK 465 THR J 135 REMARK 465 ALA J 136 REMARK 465 ALA J 137 REMARK 465 LEU J 138 REMARK 465 GLY J 139 REMARK 465 CYS J 140 REMARK 465 LEU J 141 REMARK 465 VAL J 142 REMARK 465 LYS J 143 REMARK 465 ASP J 144 REMARK 465 ASN J 155 REMARK 465 SER J 156 REMARK 465 GLY J 157 REMARK 465 ALA J 158 REMARK 465 LEU J 159 REMARK 465 THR J 160 REMARK 465 SER J 161 REMARK 465 GLY J 162 REMARK 465 THR J 183 REMARK 465 VAL J 184 REMARK 465 PRO J 185 REMARK 465 SER J 186 REMARK 465 SER J 187 REMARK 465 SER J 188 REMARK 465 LEU J 189 REMARK 465 GLY J 190 REMARK 465 THR J 191 REMARK 465 GLN J 192 REMARK 465 THR J 193 REMARK 465 TYR J 194 REMARK 465 ILE J 195 REMARK 465 CYS J 196 REMARK 465 ASN J 197 REMARK 465 VAL J 198 REMARK 465 ASN J 199 REMARK 465 HIS J 200 REMARK 465 LYS J 201 REMARK 465 PRO J 202 REMARK 465 SER J 203 REMARK 465 ASN J 204 REMARK 465 THR J 205 REMARK 465 LYS J 206 REMARK 465 VAL J 207 REMARK 465 ASP J 208 REMARK 465 LYS J 209 REMARK 465 LYS J 210 REMARK 465 VAL J 211 REMARK 465 GLU J 212 REMARK 465 PRO J 213 REMARK 465 LYS J 214 REMARK 465 SER J 215 REMARK 465 CYS J 216 REMARK 465 ASP J 217 REMARK 465 LYS J 218 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 LYS H 43 CG CD CE NZ REMARK 470 GLU H 148 CG CD OE1 OE2 REMARK 470 LYS J 43 CG CD CE NZ REMARK 470 GLU J 148 CG CD OE1 OE2 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 CYS A 296 CA - CB - SG ANGL. DEV. = 8.8 DEGREES REMARK 500 LEU C 122 CA - CB - CG ANGL. DEV. = 16.4 DEGREES REMARK 500 ASP D 632 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES REMARK 500 LEU E 111 CA - CB - CG ANGL. DEV. = 15.4 DEGREES REMARK 500 LEU E 111 CB - CG - CD2 ANGL. DEV. = -11.1 DEGREES REMARK 500 CYS E 218 CA - CB - SG ANGL. DEV. = 6.7 DEGREES REMARK 500 CYS E 331 CA - CB - SG ANGL. DEV. = 9.1 DEGREES REMARK 500 LEU E 349 CA - CB - CG ANGL. DEV. = 15.0 DEGREES REMARK 500 CYS E 418 CA - CB - SG ANGL. DEV. = 13.9 DEGREES REMARK 500 ILE E 453 CG1 - CB - CG2 ANGL. DEV. = -15.6 DEGREES REMARK 500 ASP E 457 CB - CG - OD2 ANGL. DEV. = 8.1 DEGREES REMARK 500 LEU F 523 CA - CB - CG ANGL. DEV. = 16.3 DEGREES REMARK 500 CYS F 598 CA - CB - SG ANGL. DEV. = 7.0 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 80 74.82 52.84 REMARK 500 PRO A 118 49.50 -86.90 REMARK 500 LEU A 122 53.63 -93.96 REMARK 500 SER A 199 -169.39 -166.01 REMARK 500 LYS A 232 57.27 -95.88 REMARK 500 GLU A 268 -35.21 -130.73 REMARK 500 ASN A 280 47.02 -93.39 REMARK 500 THR A 387 40.87 39.68 REMARK 500 TRP A 427 46.56 -93.64 REMARK 500 LEU A 483 14.56 59.78 REMARK 500 LYS A 485 50.52 -95.62 REMARK 500 LEU B 545 -63.18 -93.67 REMARK 500 ASN B 607 34.88 -97.33 REMARK 500 ASN C 80 68.80 31.72 REMARK 500 PRO C 118 57.68 -92.25 REMARK 500 ASN C 137 45.27 -145.36 REMARK 500 THR C 155 -168.60 -111.46 REMARK 500 ARG C 158 31.91 -99.35 REMARK 500 CYS C 196 47.46 -88.78 REMARK 500 GLU C 268 -55.56 -121.67 REMARK 500 ASN C 462 35.66 39.55 REMARK 500 LYS C 485 48.07 -93.35 REMARK 500 ASN D 543 40.47 -102.56 REMARK 500 VAL E 38 117.80 67.29 REMARK 500 PRO E 43 49.26 -81.88 REMARK 500 PHE E 53 -144.61 -151.12 REMARK 500 CYS E 54 71.47 73.52 REMARK 500 ALA E 55 -165.93 -75.90 REMARK 500 ALA E 73 76.83 -100.83 REMARK 500 ASN E 80 75.92 57.18 REMARK 500 GLU E 87 -153.17 -93.35 REMARK 500 ASN E 88 0.45 -58.46 REMARK 500 ASN E 136 -68.89 -121.13 REMARK 500 ASN E 137 46.34 -144.18 REMARK 500 ARG E 158 52.08 -90.05 REMARK 500 ASP E 159 -13.88 -140.17 REMARK 500 ASN E 195 49.08 -96.55 REMARK 500 PRO E 240 45.07 -90.43 REMARK 500 SER E 241 29.66 -142.92 REMARK 500 GLN E 246 -62.14 -96.24 REMARK 500 HIS E 249 -168.49 -79.49 REMARK 500 GLU E 268 -52.76 -123.85 REMARK 500 GLU E 275 -164.18 -77.52 REMARK 500 LEU E 285 124.84 -39.09 REMARK 500 ASN E 356 14.94 -141.65 REMARK 500 PHE E 382 128.48 -37.43 REMARK 500 THR E 387 43.86 39.14 REMARK 500 LEU E 454 171.96 -58.89 REMARK 500 ASP E 474 74.15 58.59 REMARK 500 LYS E 485 46.88 -89.71 REMARK 500 REMARK 500 THIS ENTRY HAS 68 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 SER B 546 GLY B 547 144.68 REMARK 500 CYS E 331 ASN E 332 -149.64 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY REMARK 500 REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 500 I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI ANGLE REMARK 500 ASP A 78 13.79 REMARK 500 SER B 546 -10.74 REMARK 500 ASP C 78 -13.10 REMARK 500 THR C 135 11.94 REMARK 500 ASP E 78 -13.18 REMARK 500 THR E 135 11.45 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 d 1 REMARK 610 NAG E 604 REMARK 610 NAG F 701 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-46606 RELATED DB: EMDB REMARK 900 BG505 HIV-1 ENV WITH TWO CH103 K75 N76 FABS BOUND DBREF 9D7I A 7 504 PDB 9D7I 9D7I 7 504 DBREF 9D7I B 503 664 PDB 9D7I 9D7I 503 664 DBREF 9D7I C 7 504 PDB 9D7I 9D7I 7 504 DBREF 9D7I D 503 664 PDB 9D7I 9D7I 503 664 DBREF 9D7I E 7 504 PDB 9D7I 9D7I 7 504 DBREF 9D7I F 503 664 PDB 9D7I 9D7I 503 664 DBREF 9D7I G -18 212 PDB 9D7I 9D7I -18 212 DBREF 9D7I H -18 218 PDB 9D7I 9D7I -18 218 DBREF 9D7I I -18 212 PDB 9D7I 9D7I -18 212 DBREF 9D7I J -18 218 PDB 9D7I 9D7I -18 218 SEQRES 1 A 496 MET PRO MET GLY SER LEU GLN PRO LEU ALA THR LEU TYR SEQRES 2 A 496 LEU LEU GLY MET LEU VAL ALA SER VAL LEU ALA ALA GLU SEQRES 3 A 496 ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO VAL TRP SEQRES 4 A 496 LYS ASP ALA GLU THR THR LEU PHE CYS ALA SER ASP ALA SEQRES 5 A 496 LYS ALA TYR GLU THR GLU LYS HIS ASN VAL TRP ALA THR SEQRES 6 A 496 HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN GLU ILE SEQRES 7 A 496 HIS LEU GLU ASN VAL THR GLU GLU PHE ASN MET TRP LYS SEQRES 8 A 496 ASN ASN MET VAL GLU GLN MET HIS THR ASP ILE ILE SER SEQRES 9 A 496 LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS LEU THR SEQRES 10 A 496 PRO LEU CYS VAL THR LEU GLN CYS THR ASN VAL THR ASN SEQRES 11 A 496 ASN ILE THR ASP ASP MET ARG GLY GLU LEU LYS ASN CYS SEQRES 12 A 496 SER PHE ASN MET THR THR GLU LEU ARG ASP LYS LYS GLN SEQRES 13 A 496 LYS VAL TYR SER LEU PHE TYR ARG LEU ASP VAL VAL GLN SEQRES 14 A 496 ILE ASN GLU ASN GLN GLY ASN ARG SER ASN ASN SER ASN SEQRES 15 A 496 LYS GLU TYR ARG LEU ILE ASN CYS ASN THR SER ALA CYS SEQRES 16 A 496 THR GLN ALA CYS PRO LYS VAL SER PHE GLU PRO ILE PRO SEQRES 17 A 496 ILE HIS TYR CYS ALA PRO ALA GLY PHE ALA ILE LEU LYS SEQRES 18 A 496 CYS LYS ASP LYS LYS PHE ASN GLY THR GLY PRO CYS PRO SEQRES 19 A 496 SER VAL SER THR VAL GLN CYS THR HIS GLY ILE LYS PRO SEQRES 20 A 496 VAL VAL SER THR GLN LEU LEU LEU ASN GLY SER LEU ALA SEQRES 21 A 496 GLU GLU GLU VAL MET ILE ARG SER GLU ASN ILE THR ASN SEQRES 22 A 496 ASN ALA LYS ASN ILE LEU VAL GLN PHE ASN THR PRO VAL SEQRES 23 A 496 GLN ILE ASN CYS THR ARG PRO ASN ASN ASN THR ARG LYS SEQRES 24 A 496 SER ILE ARG ILE GLY PRO GLY GLN ALA PHE TYR ALA THR SEQRES 25 A 496 GLY ASP ILE ILE GLY ASP ILE ARG GLN ALA HIS CYS ASN SEQRES 26 A 496 VAL SER LYS ALA THR TRP ASN GLU THR LEU GLY LYS VAL SEQRES 27 A 496 VAL LYS GLN LEU ARG LYS HIS PHE GLY ASN ASN THR ILE SEQRES 28 A 496 ILE ARG PHE ALA ASN SER SER GLY GLY ASP LEU GLU VAL SEQRES 29 A 496 THR THR HIS SER PHE ASN CYS GLY GLY GLU PHE PHE TYR SEQRES 30 A 496 CYS ASN THR SER GLY LEU PHE ASN SER THR TRP ILE SER SEQRES 31 A 496 ASN THR SER VAL GLN GLY SER ASN SER THR GLY SER ASN SEQRES 32 A 496 ASP SER ILE THR LEU PRO CYS ARG ILE LYS GLN ILE ILE SEQRES 33 A 496 ASN MET TRP GLN ARG ILE GLY GLN CYS MET TYR ALA PRO SEQRES 34 A 496 PRO ILE GLN GLY VAL ILE ARG CYS VAL SER ASN ILE THR SEQRES 35 A 496 GLY LEU ILE LEU THR ARG ASP GLY GLY SER THR ASN SER SEQRES 36 A 496 THR THR GLU THR PHE ARG PRO GLY GLY GLY ASP MET ARG SEQRES 37 A 496 ASP ASN TRP ARG SER GLU LEU TYR LYS TYR LYS VAL VAL SEQRES 38 A 496 LYS ILE GLU PRO LEU GLY VAL ALA PRO THR ARG CYS LYS SEQRES 39 A 496 ARG ARG SEQRES 1 B 162 VAL VAL GLY ARG ARG ARG ARG ARG ARG ALA VAL GLY ILE SEQRES 2 B 162 GLY ALA VAL PHE LEU GLY PHE LEU GLY ALA ALA GLY SER SEQRES 3 B 162 THR MET GLY ALA ALA SER MET THR LEU THR VAL GLN ALA SEQRES 4 B 162 ARG ASN LEU LEU SER GLY ILE VAL GLN GLN GLN SER ASN SEQRES 5 B 162 LEU LEU ARG ALA PRO GLU ALA GLN GLN HIS LEU LEU LYS SEQRES 6 B 162 LEU THR VAL TRP GLY ILE LYS GLN LEU GLN ALA ARG VAL SEQRES 7 B 162 LEU ALA VAL GLU ARG TYR LEU ARG ASP GLN GLN LEU LEU SEQRES 8 B 162 GLY ILE TRP GLY CYS SER GLY LYS LEU ILE CYS CYS THR SEQRES 9 B 162 ASN VAL PRO TRP ASN SER SER TRP SER ASN ARG ASN LEU SEQRES 10 B 162 SER GLU ILE TRP ASP ASN MET THR TRP LEU GLN TRP ASP SEQRES 11 B 162 LYS GLU ILE SER ASN TYR THR GLN ILE ILE TYR GLY LEU SEQRES 12 B 162 LEU GLU GLU SER GLN ASN GLN GLN GLU LYS ASN GLU GLN SEQRES 13 B 162 ASP LEU LEU ALA LEU ASP SEQRES 1 C 496 MET PRO MET GLY SER LEU GLN PRO LEU ALA THR LEU TYR SEQRES 2 C 496 LEU LEU GLY MET LEU VAL ALA SER VAL LEU ALA ALA GLU SEQRES 3 C 496 ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO VAL TRP SEQRES 4 C 496 LYS ASP ALA GLU THR THR LEU PHE CYS ALA SER ASP ALA SEQRES 5 C 496 LYS ALA TYR GLU THR GLU LYS HIS ASN VAL TRP ALA THR SEQRES 6 C 496 HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN GLU ILE SEQRES 7 C 496 HIS LEU GLU ASN VAL THR GLU GLU PHE ASN MET TRP LYS SEQRES 8 C 496 ASN ASN MET VAL GLU GLN MET HIS THR ASP ILE ILE SER SEQRES 9 C 496 LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS LEU THR SEQRES 10 C 496 PRO LEU CYS VAL THR LEU GLN CYS THR ASN VAL THR ASN SEQRES 11 C 496 ASN ILE THR ASP ASP MET ARG GLY GLU LEU LYS ASN CYS SEQRES 12 C 496 SER PHE ASN MET THR THR GLU LEU ARG ASP LYS LYS GLN SEQRES 13 C 496 LYS VAL TYR SER LEU PHE TYR ARG LEU ASP VAL VAL GLN SEQRES 14 C 496 ILE ASN GLU ASN GLN GLY ASN ARG SER ASN ASN SER ASN SEQRES 15 C 496 LYS GLU TYR ARG LEU ILE ASN CYS ASN THR SER ALA CYS SEQRES 16 C 496 THR GLN ALA CYS PRO LYS VAL SER PHE GLU PRO ILE PRO SEQRES 17 C 496 ILE HIS TYR CYS ALA PRO ALA GLY PHE ALA ILE LEU LYS SEQRES 18 C 496 CYS LYS ASP LYS LYS PHE ASN GLY THR GLY PRO CYS PRO SEQRES 19 C 496 SER VAL SER THR VAL GLN CYS THR HIS GLY ILE LYS PRO SEQRES 20 C 496 VAL VAL SER THR GLN LEU LEU LEU ASN GLY SER LEU ALA SEQRES 21 C 496 GLU GLU GLU VAL MET ILE ARG SER GLU ASN ILE THR ASN SEQRES 22 C 496 ASN ALA LYS ASN ILE LEU VAL GLN PHE ASN THR PRO VAL SEQRES 23 C 496 GLN ILE ASN CYS THR ARG PRO ASN ASN ASN THR ARG LYS SEQRES 24 C 496 SER ILE ARG ILE GLY PRO GLY GLN ALA PHE TYR ALA THR SEQRES 25 C 496 GLY ASP ILE ILE GLY ASP ILE ARG GLN ALA HIS CYS ASN SEQRES 26 C 496 VAL SER LYS ALA THR TRP ASN GLU THR LEU GLY LYS VAL SEQRES 27 C 496 VAL LYS GLN LEU ARG LYS HIS PHE GLY ASN ASN THR ILE SEQRES 28 C 496 ILE ARG PHE ALA ASN SER SER GLY GLY ASP LEU GLU VAL SEQRES 29 C 496 THR THR HIS SER PHE ASN CYS GLY GLY GLU PHE PHE TYR SEQRES 30 C 496 CYS ASN THR SER GLY LEU PHE ASN SER THR TRP ILE SER SEQRES 31 C 496 ASN THR SER VAL GLN GLY SER ASN SER THR GLY SER ASN SEQRES 32 C 496 ASP SER ILE THR LEU PRO CYS ARG ILE LYS GLN ILE ILE SEQRES 33 C 496 ASN MET TRP GLN ARG ILE GLY GLN CYS MET TYR ALA PRO SEQRES 34 C 496 PRO ILE GLN GLY VAL ILE ARG CYS VAL SER ASN ILE THR SEQRES 35 C 496 GLY LEU ILE LEU THR ARG ASP GLY GLY SER THR ASN SER SEQRES 36 C 496 THR THR GLU THR PHE ARG PRO GLY GLY GLY ASP MET ARG SEQRES 37 C 496 ASP ASN TRP ARG SER GLU LEU TYR LYS TYR LYS VAL VAL SEQRES 38 C 496 LYS ILE GLU PRO LEU GLY VAL ALA PRO THR ARG CYS LYS SEQRES 39 C 496 ARG ARG SEQRES 1 D 162 VAL VAL GLY ARG ARG ARG ARG ARG ARG ALA VAL GLY ILE SEQRES 2 D 162 GLY ALA VAL PHE LEU GLY PHE LEU GLY ALA ALA GLY SER SEQRES 3 D 162 THR MET GLY ALA ALA SER MET THR LEU THR VAL GLN ALA SEQRES 4 D 162 ARG ASN LEU LEU SER GLY ILE VAL GLN GLN GLN SER ASN SEQRES 5 D 162 LEU LEU ARG ALA PRO GLU ALA GLN GLN HIS LEU LEU LYS SEQRES 6 D 162 LEU THR VAL TRP GLY ILE LYS GLN LEU GLN ALA ARG VAL SEQRES 7 D 162 LEU ALA VAL GLU ARG TYR LEU ARG ASP GLN GLN LEU LEU SEQRES 8 D 162 GLY ILE TRP GLY CYS SER GLY LYS LEU ILE CYS CYS THR SEQRES 9 D 162 ASN VAL PRO TRP ASN SER SER TRP SER ASN ARG ASN LEU SEQRES 10 D 162 SER GLU ILE TRP ASP ASN MET THR TRP LEU GLN TRP ASP SEQRES 11 D 162 LYS GLU ILE SER ASN TYR THR GLN ILE ILE TYR GLY LEU SEQRES 12 D 162 LEU GLU GLU SER GLN ASN GLN GLN GLU LYS ASN GLU GLN SEQRES 13 D 162 ASP LEU LEU ALA LEU ASP SEQRES 1 E 496 MET PRO MET GLY SER LEU GLN PRO LEU ALA THR LEU TYR SEQRES 2 E 496 LEU LEU GLY MET LEU VAL ALA SER VAL LEU ALA ALA GLU SEQRES 3 E 496 ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO VAL TRP SEQRES 4 E 496 LYS ASP ALA GLU THR THR LEU PHE CYS ALA SER ASP ALA SEQRES 5 E 496 LYS ALA TYR GLU THR GLU LYS HIS ASN VAL TRP ALA THR SEQRES 6 E 496 HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN GLU ILE SEQRES 7 E 496 HIS LEU GLU ASN VAL THR GLU GLU PHE ASN MET TRP LYS SEQRES 8 E 496 ASN ASN MET VAL GLU GLN MET HIS THR ASP ILE ILE SER SEQRES 9 E 496 LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS LEU THR SEQRES 10 E 496 PRO LEU CYS VAL THR LEU GLN CYS THR ASN VAL THR ASN SEQRES 11 E 496 ASN ILE THR ASP ASP MET ARG GLY GLU LEU LYS ASN CYS SEQRES 12 E 496 SER PHE ASN MET THR THR GLU LEU ARG ASP LYS LYS GLN SEQRES 13 E 496 LYS VAL TYR SER LEU PHE TYR ARG LEU ASP VAL VAL GLN SEQRES 14 E 496 ILE ASN GLU ASN GLN GLY ASN ARG SER ASN ASN SER ASN SEQRES 15 E 496 LYS GLU TYR ARG LEU ILE ASN CYS ASN THR SER ALA CYS SEQRES 16 E 496 THR GLN ALA CYS PRO LYS VAL SER PHE GLU PRO ILE PRO SEQRES 17 E 496 ILE HIS TYR CYS ALA PRO ALA GLY PHE ALA ILE LEU LYS SEQRES 18 E 496 CYS LYS ASP LYS LYS PHE ASN GLY THR GLY PRO CYS PRO SEQRES 19 E 496 SER VAL SER THR VAL GLN CYS THR HIS GLY ILE LYS PRO SEQRES 20 E 496 VAL VAL SER THR GLN LEU LEU LEU ASN GLY SER LEU ALA SEQRES 21 E 496 GLU GLU GLU VAL MET ILE ARG SER GLU ASN ILE THR ASN SEQRES 22 E 496 ASN ALA LYS ASN ILE LEU VAL GLN PHE ASN THR PRO VAL SEQRES 23 E 496 GLN ILE ASN CYS THR ARG PRO ASN ASN ASN THR ARG LYS SEQRES 24 E 496 SER ILE ARG ILE GLY PRO GLY GLN ALA PHE TYR ALA THR SEQRES 25 E 496 GLY ASP ILE ILE GLY ASP ILE ARG GLN ALA HIS CYS ASN SEQRES 26 E 496 VAL SER LYS ALA THR TRP ASN GLU THR LEU GLY LYS VAL SEQRES 27 E 496 VAL LYS GLN LEU ARG LYS HIS PHE GLY ASN ASN THR ILE SEQRES 28 E 496 ILE ARG PHE ALA ASN SER SER GLY GLY ASP LEU GLU VAL SEQRES 29 E 496 THR THR HIS SER PHE ASN CYS GLY GLY GLU PHE PHE TYR SEQRES 30 E 496 CYS ASN THR SER GLY LEU PHE ASN SER THR TRP ILE SER SEQRES 31 E 496 ASN THR SER VAL GLN GLY SER ASN SER THR GLY SER ASN SEQRES 32 E 496 ASP SER ILE THR LEU PRO CYS ARG ILE LYS GLN ILE ILE SEQRES 33 E 496 ASN MET TRP GLN ARG ILE GLY GLN CYS MET TYR ALA PRO SEQRES 34 E 496 PRO ILE GLN GLY VAL ILE ARG CYS VAL SER ASN ILE THR SEQRES 35 E 496 GLY LEU ILE LEU THR ARG ASP GLY GLY SER THR ASN SER SEQRES 36 E 496 THR THR GLU THR PHE ARG PRO GLY GLY GLY ASP MET ARG SEQRES 37 E 496 ASP ASN TRP ARG SER GLU LEU TYR LYS TYR LYS VAL VAL SEQRES 38 E 496 LYS ILE GLU PRO LEU GLY VAL ALA PRO THR ARG CYS LYS SEQRES 39 E 496 ARG ARG SEQRES 1 F 162 VAL VAL GLY ARG ARG ARG ARG ARG ARG ALA VAL GLY ILE SEQRES 2 F 162 GLY ALA VAL PHE LEU GLY PHE LEU GLY ALA ALA GLY SER SEQRES 3 F 162 THR MET GLY ALA ALA SER MET THR LEU THR VAL GLN ALA SEQRES 4 F 162 ARG ASN LEU LEU SER GLY ILE VAL GLN GLN GLN SER ASN SEQRES 5 F 162 LEU LEU ARG ALA PRO GLU ALA GLN GLN HIS LEU LEU LYS SEQRES 6 F 162 LEU THR VAL TRP GLY ILE LYS GLN LEU GLN ALA ARG VAL SEQRES 7 F 162 LEU ALA VAL GLU ARG TYR LEU ARG ASP GLN GLN LEU LEU SEQRES 8 F 162 GLY ILE TRP GLY CYS SER GLY LYS LEU ILE CYS CYS THR SEQRES 9 F 162 ASN VAL PRO TRP ASN SER SER TRP SER ASN ARG ASN LEU SEQRES 10 F 162 SER GLU ILE TRP ASP ASN MET THR TRP LEU GLN TRP ASP SEQRES 11 F 162 LYS GLU ILE SER ASN TYR THR GLN ILE ILE TYR GLY LEU SEQRES 12 F 162 LEU GLU GLU SER GLN ASN GLN GLN GLU LYS ASN GLU GLN SEQRES 13 F 162 ASP LEU LEU ALA LEU ASP SEQRES 1 G 229 MET GLY TRP SER CYS ILE ILE LEU PHE LEU VAL ALA THR SEQRES 2 G 229 ALA THR GLY SER TRP ALA SER TYR GLU LEU THR GLN PRO SEQRES 3 G 229 PRO SER VAL SER VAL SER PRO GLY GLN THR ALA THR ILE SEQRES 4 G 229 THR CYS SER GLY ALA SER THR ASN VAL CYS TRP TYR GLN SEQRES 5 G 229 VAL LYS PRO GLY GLN SER PRO GLU VAL VAL ILE PHE GLU SEQRES 6 G 229 ASN TYR LYS ARG PRO SER GLY ILE PRO ASP ARG PHE SER SEQRES 7 G 229 GLY SER LYS SER GLY SER THR ALA THR LEU THR ILE ARG SEQRES 8 G 229 GLY THR GLN ALA ILE ASP GLU ALA ASP TYR TYR CYS GLN SEQRES 9 G 229 VAL TRP ASP SER PHE SER THR PHE VAL PHE GLY SER GLY SEQRES 10 G 229 THR GLN VAL THR VAL LEU GLY GLN PRO LYS ALA ASN PRO SEQRES 11 G 229 THR VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN SEQRES 12 G 229 ALA ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE SEQRES 13 G 229 TYR PRO GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER SEQRES 14 G 229 SER PRO VAL LYS ALA GLY VAL GLU THR THR THR PRO SER SEQRES 15 G 229 LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SEQRES 16 G 229 SER LEU THR PRO GLU GLN TRP LYS SER HIS ARG SER TYR SEQRES 17 G 229 SER CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS SEQRES 18 G 229 THR VAL ALA PRO THR GLU CYS SER SEQRES 1 H 245 MET GLY TRP SER CYS ILE ILE LEU PHE LEU VAL ALA THR SEQRES 2 H 245 ALA THR GLY VAL HIS SER GLN VAL GLN LEU GLN GLU SER SEQRES 3 H 245 GLY PRO GLY VAL VAL LYS SER SER GLU THR LEU SER LEU SEQRES 4 H 245 THR CYS THR VAL SER GLY GLY SER MET GLY GLY THR TYR SEQRES 5 H 245 TRP SER TRP LEU ARG LEU SER PRO GLY LYS GLY LEU GLU SEQRES 6 H 245 TRP ILE GLY TYR ILE PHE HIS THR GLY GLU THR ASN TYR SEQRES 7 H 245 SER PRO SER LEU LYS GLY ARG VAL SER ILE SER VAL ASP SEQRES 8 H 245 THR SER LYS ASN GLN PHE SER LEU ARG LEU ARG SER VAL SEQRES 9 H 245 THR ALA ALA ASP THR ALA VAL TYR PHE CYS ALA SER LEU SEQRES 10 H 245 PRO ARG GLY GLN LEU VAL ASN ALA TYR PHE ARG ASN TRP SEQRES 11 H 245 GLY ARG GLY SER LEU VAL SER VAL THR ALA ALA SER THR SEQRES 12 H 245 LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SEQRES 13 H 245 SER THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL SEQRES 14 H 245 LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SEQRES 15 H 245 SER GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA SEQRES 16 H 245 VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL SEQRES 17 H 245 VAL THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR SEQRES 18 H 245 ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL SEQRES 19 H 245 ASP LYS LYS VAL GLU PRO LYS SER CYS ASP LYS SEQRES 1 I 229 MET GLY TRP SER CYS ILE ILE LEU PHE LEU VAL ALA THR SEQRES 2 I 229 ALA THR GLY SER TRP ALA SER TYR GLU LEU THR GLN PRO SEQRES 3 I 229 PRO SER VAL SER VAL SER PRO GLY GLN THR ALA THR ILE SEQRES 4 I 229 THR CYS SER GLY ALA SER THR ASN VAL CYS TRP TYR GLN SEQRES 5 I 229 VAL LYS PRO GLY GLN SER PRO GLU VAL VAL ILE PHE GLU SEQRES 6 I 229 ASN TYR LYS ARG PRO SER GLY ILE PRO ASP ARG PHE SER SEQRES 7 I 229 GLY SER LYS SER GLY SER THR ALA THR LEU THR ILE ARG SEQRES 8 I 229 GLY THR GLN ALA ILE ASP GLU ALA ASP TYR TYR CYS GLN SEQRES 9 I 229 VAL TRP ASP SER PHE SER THR PHE VAL PHE GLY SER GLY SEQRES 10 I 229 THR GLN VAL THR VAL LEU GLY GLN PRO LYS ALA ASN PRO SEQRES 11 I 229 THR VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN SEQRES 12 I 229 ALA ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE SEQRES 13 I 229 TYR PRO GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER SEQRES 14 I 229 SER PRO VAL LYS ALA GLY VAL GLU THR THR THR PRO SER SEQRES 15 I 229 LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SEQRES 16 I 229 SER LEU THR PRO GLU GLN TRP LYS SER HIS ARG SER TYR SEQRES 17 I 229 SER CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS SEQRES 18 I 229 THR VAL ALA PRO THR GLU CYS SER SEQRES 1 J 245 MET GLY TRP SER CYS ILE ILE LEU PHE LEU VAL ALA THR SEQRES 2 J 245 ALA THR GLY VAL HIS SER GLN VAL GLN LEU GLN GLU SER SEQRES 3 J 245 GLY PRO GLY VAL VAL LYS SER SER GLU THR LEU SER LEU SEQRES 4 J 245 THR CYS THR VAL SER GLY GLY SER MET GLY GLY THR TYR SEQRES 5 J 245 TRP SER TRP LEU ARG LEU SER PRO GLY LYS GLY LEU GLU SEQRES 6 J 245 TRP ILE GLY TYR ILE PHE HIS THR GLY GLU THR ASN TYR SEQRES 7 J 245 SER PRO SER LEU LYS GLY ARG VAL SER ILE SER VAL ASP SEQRES 8 J 245 THR SER LYS ASN GLN PHE SER LEU ARG LEU ARG SER VAL SEQRES 9 J 245 THR ALA ALA ASP THR ALA VAL TYR PHE CYS ALA SER LEU SEQRES 10 J 245 PRO ARG GLY GLN LEU VAL ASN ALA TYR PHE ARG ASN TRP SEQRES 11 J 245 GLY ARG GLY SER LEU VAL SER VAL THR ALA ALA SER THR SEQRES 12 J 245 LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SEQRES 13 J 245 SER THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL SEQRES 14 J 245 LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SEQRES 15 J 245 SER GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA SEQRES 16 J 245 VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL SEQRES 17 J 245 VAL THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR SEQRES 18 J 245 ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL SEQRES 19 J 245 ASP LYS LYS VAL GLU PRO LYS SER CYS ASP LYS HET NAG K 1 14 HET NAG K 2 14 HET NAG L 1 14 HET NAG L 2 14 HET BMA L 3 11 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 BMA O 3 11 HET NAG P 1 14 HET NAG P 2 14 HET NAG Q 1 14 HET NAG Q 2 14 HET NAG R 1 14 HET NAG R 2 14 HET BMA R 3 11 HET NAG S 1 14 HET NAG S 2 14 HET BMA S 3 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 NAG W 1 14 HET NAG W 2 14 HET NAG X 1 14 HET NAG X 2 14 HET BMA X 3 11 HET NAG Y 1 14 HET NAG Y 2 14 HET NAG Z 1 14 HET NAG Z 2 14 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 NAG d 1 14 HET NAG d 2 14 HET BMA d 3 11 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 BMA g 3 11 HET NAG h 1 14 HET NAG h 2 14 HET BMA h 3 11 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 B 701 14 HET NAG C 601 14 HET NAG C 602 14 HET NAG C 603 14 HET NAG C 604 14 HET NAG C 605 14 HET NAG C 606 14 HET NAG C 607 14 HET NAG D 701 14 HET NAG D 702 14 HET NAG E 601 14 HET NAG E 602 14 HET NAG E 603 14 HET NAG E 604 14 HET NAG E 605 14 HET NAG E 606 14 HET NAG E 607 14 HET NAG E 608 14 HET NAG E 609 14 HET NAG F 701 14 HET NAG F 702 14 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BMA BETA-D-MANNOPYRANOSE HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA- HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO- HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE FORMUL 11 NAG 78(C8 H15 N O6) FORMUL 12 BMA 10(C6 H12 O6) HELIX 1 AA1 ASN A 99 LEU A 116 1 18 HELIX 2 AA2 TYR A 169 LEU A 171 5 3 HELIX 3 AA3 SER A 334 GLY A 354 1 21 HELIX 4 AA4 ASP A 368 THR A 373 1 6 HELIX 5 AA5 MET A 475 SER A 481 1 7 HELIX 6 AA6 GLY B 531 THR B 536 5 6 HELIX 7 AA7 LEU B 537 ASN B 543 1 7 HELIX 8 AA8 THR B 569 TRP B 596 1 28 HELIX 9 AA9 THR B 627 ASP B 632 5 6 HELIX 10 AB1 TYR B 638 ALA B 662 1 25 HELIX 11 AB2 ASN C 99 LEU C 116 1 18 HELIX 12 AB3 LYS C 335 ARG C 350 1 16 HELIX 13 AB4 ASP C 368 THR C 373 1 6 HELIX 14 AB5 MET C 475 SER C 481 1 7 HELIX 15 AB6 THR D 529 SER D 534 1 6 HELIX 16 AB7 LEU D 537 ASN D 543 1 7 HELIX 17 AB8 GLY D 572 TRP D 596 1 25 HELIX 18 AB9 ASN D 618 ILE D 622 5 5 HELIX 19 AC1 THR D 627 SER D 636 1 10 HELIX 20 AC2 TYR D 638 GLU D 654 1 17 HELIX 21 AC3 ASN E 98 LEU E 116 1 19 HELIX 22 AC4 SER E 334 ARG E 350 1 17 HELIX 23 AC5 ASP E 368 THR E 373 1 6 HELIX 24 AC6 ASP E 474 TRP E 479 5 6 HELIX 25 AC7 THR F 529 SER F 534 1 6 HELIX 26 AC8 GLY F 572 TRP F 596 1 25 HELIX 27 AC9 ASN F 618 TRP F 623 1 6 HELIX 28 AD1 THR F 627 GLU F 634 1 8 HELIX 29 AD2 TYR F 638 LEU F 646 1 9 HELIX 30 AD3 GLN G 79 GLU G 83 5 5 HELIX 31 AD4 THR H 83 THR H 87 5 5 HELIX 32 AD5 GLN I 79 GLU I 83 5 5 HELIX 33 AD6 PRO J 61 LYS J 64 5 4 HELIX 34 AD7 THR J 83 THR J 87 5 5 SHEET 1 AA1 3 GLY A 495 THR A 499 0 SHEET 2 AA1 3 TRP A 35 TYR A 39 -1 N TYR A 39 O GLY A 495 SHEET 3 AA1 3 ILE B 603 PRO B 609 -1 O THR B 606 N VAL A 36 SHEET 1 AA2 5 TRP A 45 LYS A 46 0 SHEET 2 AA2 5 VAL A 488 ILE A 491 -1 O LYS A 490 N LYS A 46 SHEET 3 AA2 5 PHE A 223 CYS A 228 -1 N ALA A 224 O VAL A 489 SHEET 4 AA2 5 VAL A 242 VAL A 245 -1 O SER A 243 N LYS A 227 SHEET 5 AA2 5 ILE A 84 LEU A 86 -1 N LEU A 86 O VAL A 242 SHEET 1 AA3 2 PHE A 53 ALA A 55 0 SHEET 2 AA3 2 HIS A 216 CYS A 218 -1 O CYS A 218 N PHE A 53 SHEET 1 AA4 2 GLU A 92 ASN A 94 0 SHEET 2 AA4 2 THR A 236 PRO A 238 -1 O GLY A 237 N PHE A 93 SHEET 1 AA5 3 GLN A 130 ASN A 133 0 SHEET 2 AA5 3 LYS A 147 THR A 154 -1 O ASN A 148 N THR A 132 SHEET 3 AA5 3 LYS A 161 PHE A 168 -1 O SER A 166 N CYS A 149 SHEET 1 AA6 2 VAL A 173 GLN A 175 0 SHEET 2 AA6 2 TYR A 191 LEU A 193 -1 O ARG A 192 N VAL A 174 SHEET 1 AA7 3 THR A 202 GLN A 203 0 SHEET 2 AA7 3 MET A 434 TYR A 435 1 O TYR A 435 N THR A 202 SHEET 3 AA7 3 ILE A 423 ILE A 424 -1 N ILE A 424 O MET A 434 SHEET 1 AA8 4 MET A 271 ARG A 273 0 SHEET 2 AA8 4 LEU A 285 THR A 297 -1 O LEU A 285 N ARG A 273 SHEET 3 AA8 4 ALA A 329 VAL A 333 -1 O ASN A 332 N ASN A 295 SHEET 4 AA8 4 PRO A 417 CYS A 418 -1 O CYS A 418 N ALA A 329 SHEET 1 AA9 3 MET A 271 ARG A 273 0 SHEET 2 AA9 3 LEU A 285 THR A 297 -1 O LEU A 285 N ARG A 273 SHEET 3 AA9 3 ARG A 444 LEU A 452 -1 O SER A 447 N ILE A 294 SHEET 1 AB1 2 ARG A 304 ARG A 308 0 SHEET 2 AB1 2 ALA A 316 THR A 320 -1 O ALA A 319 N LYS A 305 SHEET 1 AB2 4 SER A 393 TRP A 395 0 SHEET 2 AB2 4 ILE A 358 PHE A 361 -1 N ILE A 359 O TRP A 395 SHEET 3 AB2 4 THR A 465 PRO A 470 1 O GLU A 466 N ILE A 358 SHEET 4 AB2 4 LEU A 454 ASP A 457 -1 N THR A 455 O ARG A 469 SHEET 1 AB3 3 HIS A 374 CYS A 378 0 SHEET 2 AB3 3 GLU A 381 CYS A 385 -1 O GLU A 381 N CYS A 378 SHEET 3 AB3 3 ILE A 420 LYS A 421 -1 O LYS A 421 N PHE A 382 SHEET 1 AB4 2 TRP C 35 TYR C 40 0 SHEET 2 AB4 2 LEU C 494 THR C 499 -1 O GLY C 495 N TYR C 39 SHEET 1 AB5 5 TRP C 45 ASP C 47 0 SHEET 2 AB5 5 TYR C 486 ILE C 491 -1 O LYS C 490 N LYS C 46 SHEET 3 AB5 5 PHE C 223 CYS C 228 -1 N LEU C 226 O LYS C 487 SHEET 4 AB5 5 VAL C 242 VAL C 245 -1 O SER C 243 N LYS C 227 SHEET 5 AB5 5 GLU C 83 HIS C 85 -1 N ILE C 84 O THR C 244 SHEET 1 AB6 3 VAL C 75 PRO C 76 0 SHEET 2 AB6 3 CYS C 54 SER C 56 1 N SER C 56 O VAL C 75 SHEET 3 AB6 3 HIS C 216 TYR C 217 -1 O HIS C 216 N ALA C 55 SHEET 1 AB7 2 GLU C 91 ASN C 94 0 SHEET 2 AB7 2 THR C 236 CYS C 239 -1 O GLY C 237 N PHE C 93 SHEET 1 AB8 5 SER C 166 TYR C 169 0 SHEET 2 AB8 5 LEU C 146 CYS C 149 -1 N LYS C 147 O PHE C 168 SHEET 3 AB8 5 LEU C 129 ASN C 133 -1 N THR C 132 O ASN C 148 SHEET 4 AB8 5 GLU C 190 LEU C 193 -1 O TYR C 191 N LEU C 129 SHEET 5 AB8 5 VAL C 173 GLN C 175 -1 N VAL C 174 O ARG C 192 SHEET 1 AB9 2 ASN C 152 THR C 154 0 SHEET 2 AB9 2 LYS C 161 LYS C 163 -1 O GLN C 162 N MET C 153 SHEET 1 AC1 3 THR C 202 GLN C 203 0 SHEET 2 AC1 3 MET C 434 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 AC2 7 LEU C 259 LEU C 261 0 SHEET 2 AC2 7 ILE C 443 ASP C 457 -1 O GLY C 451 N LEU C 260 SHEET 3 AC2 7 ILE C 284 ARG C 298 -1 N PHE C 288 O THR C 450 SHEET 4 AC2 7 ALA C 329 SER C 334 -1 O ASN C 332 N ASN C 295 SHEET 5 AC2 7 SER C 413 LYS C 421 -1 O ILE C 414 N VAL C 333 SHEET 6 AC2 7 PHE C 382 CYS C 385 -1 N TYR C 384 O ARG C 419 SHEET 7 AC2 7 HIS C 374 ASN C 377 -1 N HIS C 374 O CYS C 385 SHEET 1 AC3 6 MET C 271 ARG C 273 0 SHEET 2 AC3 6 ILE C 284 ARG C 298 -1 O LEU C 285 N ARG C 273 SHEET 3 AC3 6 ILE C 443 ASP C 457 -1 O THR C 450 N PHE C 288 SHEET 4 AC3 6 THR C 465 PRO C 470 -1 O ARG C 469 N THR C 455 SHEET 5 AC3 6 ILE C 358 PHE C 361 1 N ARG C 360 O PHE C 468 SHEET 6 AC3 6 SER C 393 TRP C 395 -1 O SER C 393 N PHE C 361 SHEET 1 AC4 2 ARG C 304 ARG C 308 0 SHEET 2 AC4 2 ALA C 316 THR C 320 -1 O PHE C 317 N ILE C 307 SHEET 1 AC5 2 TYR E 39 TYR E 40 0 SHEET 2 AC5 2 LEU E 494 GLY E 495 -1 O GLY E 495 N TYR E 39 SHEET 1 AC6 5 LYS E 46 ASP E 47 0 SHEET 2 AC6 5 TYR E 486 LYS E 490 -1 O LYS E 490 N LYS E 46 SHEET 3 AC6 5 PHE E 223 LYS E 227 -1 N LEU E 226 O LYS E 487 SHEET 4 AC6 5 SER E 243 VAL E 245 -1 O SER E 243 N LYS E 227 SHEET 5 AC6 5 ILE E 84 HIS E 85 -1 N ILE E 84 O THR E 244 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 5 LYS E 161 TYR E 169 0 SHEET 2 AC8 5 LEU E 146 THR E 154 -1 N LYS E 147 O PHE E 168 SHEET 3 AC8 5 LEU E 129 ASN E 133 -1 N THR E 132 O ASN E 148 SHEET 4 AC8 5 GLU E 190 LEU E 193 -1 O TYR E 191 N LEU E 129 SHEET 5 AC8 5 VAL E 173 GLN E 175 -1 N VAL E 174 O ARG E 192 SHEET 1 AC9 4 LEU E 259 LEU E 261 0 SHEET 2 AC9 4 GLY E 441 LEU E 452 -1 O THR E 450 N LEU E 260 SHEET 3 AC9 4 VAL E 292 ASN E 302 -1 N ILE E 294 O SER E 447 SHEET 4 AC9 4 CYS E 331 VAL E 333 -1 O ASN E 332 N ASN E 295 SHEET 1 AD1 2 MET E 271 ILE E 272 0 SHEET 2 AD1 2 VAL E 286 GLN E 287 -1 O GLN E 287 N MET E 271 SHEET 1 AD2 2 ILE E 307 GLY E 312 0 SHEET 2 AD2 2 GLN E 315 PHE E 317 -1 O PHE E 317 N ILE E 307 SHEET 1 AD3 4 THR E 394 TRP E 395 0 SHEET 2 AD3 4 ILE E 358 PHE E 361 -1 N ILE E 359 O TRP E 395 SHEET 3 AD3 4 THR E 465 ARG E 469 1 O PHE E 468 N ARG E 360 SHEET 4 AD3 4 THR E 455 ASP E 457 -1 N ASP E 457 O THR E 467 SHEET 1 AD4 2 PHE E 383 CYS E 385 0 SHEET 2 AD4 2 CYS E 418 ILE E 420 -1 O ARG E 419 N TYR E 384 SHEET 1 AD5 2 ILE E 423 ILE E 424 0 SHEET 2 AD5 2 MET E 434 TYR E 435 -1 O MET E 434 N ILE E 424 SHEET 1 AD6 5 SER G 9 VAL G 13 0 SHEET 2 AD6 5 THR G 102 VAL G 106 1 O GLN G 103 N VAL G 11 SHEET 3 AD6 5 ASP G 85 TRP G 91 -1 N TYR G 86 O THR G 102 SHEET 4 AD6 5 VAL G 33 VAL G 38 -1 N TYR G 36 O TYR G 87 SHEET 5 AD6 5 GLU G 45 ILE G 48 -1 O GLU G 45 N GLN G 37 SHEET 1 AD7 4 SER G 9 VAL G 13 0 SHEET 2 AD7 4 THR G 102 VAL G 106 1 O GLN G 103 N VAL G 11 SHEET 3 AD7 4 ASP G 85 TRP G 91 -1 N TYR G 86 O THR G 102 SHEET 4 AD7 4 PHE G 96 PHE G 98 -1 O VAL G 97 N VAL G 90 SHEET 1 AD8 3 ALA G 19 CYS G 23 0 SHEET 2 AD8 3 THR G 70 ILE G 75 -1 O ALA G 71 N CYS G 23 SHEET 3 AD8 3 PHE G 62 SER G 67 -1 N SER G 63 O THR G 74 SHEET 1 AD9 4 THR G 114 PHE G 118 0 SHEET 2 AD9 4 THR G 131 PHE G 139 -1 O SER G 137 N THR G 114 SHEET 3 AD9 4 TYR G 172 SER G 179 -1 O LEU G 178 N LEU G 132 SHEET 4 AD9 4 VAL G 159 THR G 161 -1 N GLU G 160 O TYR G 177 SHEET 1 AE1 3 THR G 145 LYS G 149 0 SHEET 2 AE1 3 SER G 192 HIS G 197 -1 O SER G 192 N LYS G 149 SHEET 3 AE1 3 SER G 200 LYS G 204 -1 O SER G 200 N HIS G 197 SHEET 1 AE2 4 GLN H 3 SER H 7 0 SHEET 2 AE2 4 LEU H 18 SER H 25 -1 O THR H 23 N GLN H 5 SHEET 3 AE2 4 GLN H 77 LEU H 82 -1 O PHE H 78 N CYS H 22 SHEET 4 AE2 4 VAL H 67 ASP H 72 -1 N SER H 70 O SER H 79 SHEET 1 AE3 6 VAL H 11 LYS H 13 0 SHEET 2 AE3 6 SER H 107 THR H 112 1 O SER H 110 N VAL H 12 SHEET 3 AE3 6 ALA H 88 PRO H 96 -1 N ALA H 88 O VAL H 109 SHEET 4 AE3 6 THR H 32 SER H 40 -1 N LEU H 37 O PHE H 91 SHEET 5 AE3 6 GLY H 44 ILE H 51 -1 O GLU H 46 N ARG H 38 SHEET 6 AE3 6 THR H 57 TYR H 59 -1 O ASN H 58 N TYR H 50 SHEET 1 AE4 2 VAL H 169 LEU H 170 0 SHEET 2 AE4 2 TYR H 176 SER H 177 -1 O SER H 177 N VAL H 169 SHEET 1 AE5 5 SER I 9 VAL I 13 0 SHEET 2 AE5 5 THR I 102 VAL I 106 1 O GLN I 103 N VAL I 11 SHEET 3 AE5 5 ASP I 85 TRP I 91 -1 N TYR I 86 O THR I 102 SHEET 4 AE5 5 CYS I 34 VAL I 38 -1 N TYR I 36 O TYR I 87 SHEET 5 AE5 5 GLU I 45 ILE I 48 -1 O ILE I 48 N TRP I 35 SHEET 1 AE6 4 SER I 9 VAL I 13 0 SHEET 2 AE6 4 THR I 102 VAL I 106 1 O GLN I 103 N VAL I 11 SHEET 3 AE6 4 ASP I 85 TRP I 91 -1 N TYR I 86 O THR I 102 SHEET 4 AE6 4 PHE I 96 PHE I 98 -1 O VAL I 97 N VAL I 90 SHEET 1 AE7 3 ALA I 19 CYS I 23 0 SHEET 2 AE7 3 THR I 70 ILE I 75 -1 O ALA I 71 N CYS I 23 SHEET 3 AE7 3 PHE I 62 SER I 67 -1 N SER I 65 O THR I 72 SHEET 1 AE8 4 THR I 114 PHE I 118 0 SHEET 2 AE8 4 THR I 131 PHE I 139 -1 O SER I 137 N THR I 114 SHEET 3 AE8 4 TYR I 172 SER I 179 -1 O TYR I 172 N PHE I 139 SHEET 4 AE8 4 VAL I 159 THR I 161 -1 N GLU I 160 O TYR I 177 SHEET 1 AE9 3 VAL I 144 LYS I 149 0 SHEET 2 AE9 3 SER I 192 HIS I 197 -1 O GLN I 194 N ALA I 147 SHEET 3 AE9 3 GLU I 203 LYS I 204 -1 O LYS I 204 N CYS I 193 SHEET 1 AF1 4 GLN J 3 SER J 7 0 SHEET 2 AF1 4 LEU J 18 SER J 25 -1 O THR J 23 N GLN J 5 SHEET 3 AF1 4 GLN J 77 LEU J 82 -1 O PHE J 78 N CYS J 22 SHEET 4 AF1 4 VAL J 67 ASP J 72 -1 N SER J 70 O SER J 79 SHEET 1 AF2 6 VAL J 11 LYS J 13 0 SHEET 2 AF2 6 SER J 107 THR J 112 1 O SER J 110 N VAL J 12 SHEET 3 AF2 6 ALA J 88 PRO J 96 -1 N ALA J 88 O VAL J 109 SHEET 4 AF2 6 THR J 32 SER J 40 -1 N SER J 35 O ALA J 93 SHEET 5 AF2 6 GLY J 44 ILE J 51 -1 O ILE J 51 N TRP J 34 SHEET 6 AF2 6 THR J 57 TYR J 59 -1 O ASN J 58 N TYR J 50 SHEET 1 AF3 2 VAL J 169 LEU J 170 0 SHEET 2 AF3 2 TYR J 176 SER J 177 -1 O SER J 177 N VAL J 169 SSBOND 1 CYS A 54 CYS A 74 1555 1555 2.03 SSBOND 2 CYS A 119 CYS A 205 1555 1555 2.04 SSBOND 3 CYS A 126 CYS A 196 1555 1555 2.03 SSBOND 4 CYS A 131 CYS A 149 1555 1555 2.03 SSBOND 5 CYS A 201 CYS A 433 1555 1555 2.03 SSBOND 6 CYS A 218 CYS A 247 1555 1555 2.03 SSBOND 7 CYS A 296 CYS A 331 1555 1555 2.05 SSBOND 8 CYS A 378 CYS A 445 1555 1555 2.03 SSBOND 9 CYS A 385 CYS A 418 1555 1555 2.03 SSBOND 10 CYS C 119 CYS C 205 1555 1555 2.04 SSBOND 11 CYS C 126 CYS C 196 1555 1555 2.03 SSBOND 12 CYS C 131 CYS C 149 1555 1555 2.03 SSBOND 13 CYS C 201 CYS C 433 1555 1555 2.03 SSBOND 14 CYS C 296 CYS C 331 1555 1555 2.04 SSBOND 15 CYS C 331 CYS C 418 1555 1555 2.04 SSBOND 16 CYS C 378 CYS C 445 1555 1555 2.03 SSBOND 17 CYS C 385 CYS C 418 1555 1555 2.03 SSBOND 18 CYS C 501 CYS D 605 1555 1555 2.03 SSBOND 19 CYS D 598 CYS D 604 1555 1555 2.03 SSBOND 20 CYS E 54 CYS E 247 1555 1555 2.05 SSBOND 21 CYS E 119 CYS E 205 1555 1555 2.03 SSBOND 22 CYS E 126 CYS E 196 1555 1555 2.03 SSBOND 23 CYS E 131 CYS E 149 1555 1555 2.03 SSBOND 24 CYS E 201 CYS E 433 1555 1555 2.03 SSBOND 25 CYS E 296 CYS E 331 1555 1555 2.03 SSBOND 26 CYS E 331 CYS E 385 1555 1555 2.05 SSBOND 27 CYS E 331 CYS E 418 1555 1555 2.09 SSBOND 28 CYS E 378 CYS E 445 1555 1555 2.03 SSBOND 29 CYS E 385 CYS E 418 1555 1555 2.02 SSBOND 30 CYS F 598 CYS F 604 1555 1555 2.03 SSBOND 31 CYS G 23 CYS G 88 1555 1555 2.03 SSBOND 32 CYS G 134 CYS G 193 1555 1555 2.03 SSBOND 33 CYS H 22 CYS H 92 1555 1555 2.03 SSBOND 34 CYS I 23 CYS I 88 1555 1555 2.04 SSBOND 35 CYS I 134 CYS I 193 1555 1555 2.03 SSBOND 36 CYS J 22 CYS J 92 1555 1555 2.03 LINK ND2 ASN A 88 C1 NAG A 601 1555 1555 1.44 LINK ND2 ASN A 133 C1 NAG K 1 1555 1555 1.44 LINK ND2 ASN A 148 C1 NAG L 1 1555 1555 1.44 LINK ND2 ASN A 152 C1 NAG M 1 1555 1555 1.44 LINK ND2 ASN A 197 C1 NAG N 1 1555 1555 1.44 LINK ND2 ASN A 234 C1 NAG A 602 1555 1555 1.44 LINK ND2 ASN A 262 C1 NAG O 1 1555 1555 1.44 LINK ND2 ASN A 276 C1 NAG A 603 1555 1555 1.45 LINK ND2 ASN A 295 C1 NAG A 604 1555 1555 1.44 LINK ND2 ASN A 301 C1 NAG A 605 1555 1555 1.44 LINK ND2 ASN A 332 C1 NAG A 606 1555 1555 1.45 LINK ND2 ASN A 355 C1 NAG A 607 1555 1555 1.44 LINK ND2 ASN A 363 C1 NAG P 1 1555 1555 1.44 LINK ND2 ASN A 386 C1 NAG Q 1 1555 1555 1.44 LINK ND2 ASN A 392 C1 NAG A 608 1555 1555 1.44 LINK ND2 ASN A 448 C1 NAG A 609 1555 1555 1.46 LINK ND2 ASN B 637 C1 NAG B 701 1555 1555 1.44 LINK ND2 ASN C 88 C1 NAG Z 1 1555 1555 1.44 LINK ND2 ASN C 133 C1 NAG C 606 1555 1555 1.44 LINK ND2 ASN C 137 C1 NAG C 607 1555 1555 1.46 LINK ND2 ASN C 148 C1 NAG Y 1 1555 1555 1.44 LINK ND2 ASN C 152 C1 NAG W 1 1555 1555 1.45 LINK ND2 ASN C 234 C1 NAG C 605 1555 1555 1.44 LINK ND2 ASN C 262 C1 NAG X 1 1555 1555 1.44 LINK ND2 ASN C 276 C1 NAG V 1 1555 1555 1.44 LINK ND2 ASN C 295 C1 NAG U 1 1555 1555 1.44 LINK ND2 ASN C 301 C1 NAG C 601 1555 1555 1.44 LINK ND2 ASN C 332 C1 NAG T 1 1555 1555 1.44 LINK ND2 ASN C 355 C1 NAG C 604 1555 1555 1.44 LINK ND2 ASN C 363 C1 NAG S 1 1555 1555 1.44 LINK ND2 ASN C 386 C1 NAG R 1 1555 1555 1.44 LINK ND2 ASN C 392 C1 NAG C 603 1555 1555 1.44 LINK ND2 ASN C 448 C1 NAG C 602 1555 1555 1.45 LINK ND2 ASN D 611 C1 NAG D 701 1555 1555 1.44 LINK ND2 ASN D 637 C1 NAG D 702 1555 1555 1.44 LINK ND2 ASN E 88 C1 NAG a 1 1555 1555 1.44 LINK ND2 ASN E 133 C1 NAG E 601 1555 1555 1.44 LINK ND2 ASN E 137 C1 NAG E 602 1555 1555 1.44 LINK ND2 ASN E 148 C1 NAG b 1 1555 1555 1.44 LINK ND2 ASN E 152 C1 NAG E 603 1555 1555 1.44 LINK ND2 ASN E 234 C1 NAG E 605 1555 1555 1.44 LINK ND2 ASN E 262 C1 NAG c 1 1555 1555 1.44 LINK ND2 ASN E 295 C1 NAG e 1 1555 1555 1.44 LINK ND2 ASN E 301 C1 NAG E 606 1555 1555 1.44 LINK ND2 ASN E 332 C1 NAG f 1 1555 1555 1.43 LINK ND2 ASN E 355 C1 NAG E 607 1555 1555 1.44 LINK ND2 ASN E 363 C1 NAG g 1 1555 1555 1.44 LINK ND2 ASN E 386 C1 NAG h 1 1555 1555 1.44 LINK ND2 ASN E 392 C1 NAG E 608 1555 1555 1.44 LINK ND2 ASN E 448 C1 NAG E 609 1555 1555 1.45 LINK ND2 ASN F 637 C1 NAG F 702 1555 1555 1.44 LINK O4 NAG K 1 C1 NAG K 2 1555 1555 1.45 LINK O4 NAG L 1 C1 NAG L 2 1555 1555 1.45 LINK O4 NAG L 2 C1 BMA L 3 1555 1555 1.45 LINK O4 NAG M 1 C1 NAG M 2 1555 1555 1.44 LINK O4 NAG N 1 C1 NAG N 2 1555 1555 1.44 LINK O4 NAG O 1 C1 NAG O 2 1555 1555 1.44 LINK O4 NAG O 2 C1 BMA O 3 1555 1555 1.45 LINK O4 NAG P 1 C1 NAG P 2 1555 1555 1.45 LINK O4 NAG Q 1 C1 NAG Q 2 1555 1555 1.44 LINK O4 NAG R 1 C1 NAG R 2 1555 1555 1.44 LINK O4 NAG R 2 C1 BMA R 3 1555 1555 1.45 LINK O4 NAG S 1 C1 NAG S 2 1555 1555 1.44 LINK O4 NAG S 2 C1 BMA S 3 1555 1555 1.45 LINK O4 NAG T 1 C1 NAG T 2 1555 1555 1.44 LINK O4 NAG U 1 C1 NAG U 2 1555 1555 1.44 LINK O4 NAG V 1 C1 NAG V 2 1555 1555 1.45 LINK O4 NAG V 2 C1 BMA V 3 1555 1555 1.44 LINK O4 NAG W 1 C1 NAG W 2 1555 1555 1.45 LINK O4 NAG X 1 C1 NAG X 2 1555 1555 1.44 LINK O4 NAG X 2 C1 BMA X 3 1555 1555 1.44 LINK O4 NAG Y 1 C1 NAG Y 2 1555 1555 1.44 LINK O4 NAG Z 1 C1 NAG Z 2 1555 1555 1.44 LINK O4 NAG a 1 C1 NAG a 2 1555 1555 1.45 LINK O4 NAG b 1 C1 NAG b 2 1555 1555 1.44 LINK O4 NAG c 1 C1 NAG c 2 1555 1555 1.44 LINK O4 NAG c 2 C1 BMA c 3 1555 1555 1.45 LINK O4 NAG d 1 C1 NAG d 2 1555 1555 1.44 LINK O4 NAG d 2 C1 BMA d 3 1555 1555 1.45 LINK O4 NAG e 1 C1 NAG e 2 1555 1555 1.44 LINK O4 NAG f 1 C1 NAG f 2 1555 1555 1.44 LINK O4 NAG g 1 C1 NAG g 2 1555 1555 1.44 LINK O4 NAG g 2 C1 BMA g 3 1555 1555 1.45 LINK O4 NAG h 1 C1 NAG h 2 1555 1555 1.44 LINK O4 NAG h 2 C1 BMA h 3 1555 1555 1.46 CISPEP 1 TYR G 140 PRO G 141 0 0.74 CISPEP 2 TYR I 140 PRO I 141 0 -2.97 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