HEADER VIRAL PROTEIN 29-JAN-16 5FUU TITLE ECTODOMAIN OF CLEAVED WILD TYPE JR-FL ENVDCT TRIMER IN COMPLEX WITH TITLE 2 PGT151 FAB COMPND MOL_ID: 1; COMPND 2 MOLECULE: HIV-1 ENVELOPE GLYCOPROTEIN GP160; COMPND 3 CHAIN: A, C, E; COMPND 4 FRAGMENT: GP120, RESIDUES 30-502; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES; COMPND 7 OTHER_DETAILS: GP120 OF JR-FL ENV; COMPND 8 MOL_ID: 2; COMPND 9 MOLECULE: HIV-1 ENVELOPE GLYCOPROTEIN GP160; COMPND 10 CHAIN: B, D, F; COMPND 11 FRAGMENT: GP41, RESIDUES 503-655; COMPND 12 ENGINEERED: YES; COMPND 13 OTHER_DETAILS: GP41 ECTODOMAIN OF JR-FL ENV; COMPND 14 MOL_ID: 3; COMPND 15 MOLECULE: IMMUNOGLOBULIN G PGT151; COMPND 16 CHAIN: H, M; COMPND 17 FRAGMENT: FAB HEAVY CHAIN VARIABLE REGION, RESIDUES 1-218; COMPND 18 ENGINEERED: YES; COMPND 19 OTHER_DETAILS: PGT151 CLEAVED INTO FAB; COMPND 20 MOL_ID: 4; COMPND 21 MOLECULE: IMMUNOGLOBULIN G PGT151; COMPND 22 CHAIN: L, N; COMPND 23 FRAGMENT: FAB LIGHT CHAIN VARIABLE REGION, RESIDUES 1-214; COMPND 24 ENGINEERED: YES; COMPND 25 OTHER_DETAILS: PGT151 CLEAVED INTO FAB SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 3 ORGANISM_TAXID: 11676; SOURCE 4 GENE: ENV; SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HEK293; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PHCMV3; SOURCE 11 MOL_ID: 2; SOURCE 12 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 13 ORGANISM_TAXID: 11676; SOURCE 14 GENE: ENV; SOURCE 15 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 16 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 18 EXPRESSION_SYSTEM_CELL_LINE: HEK293; SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PHCMV3; SOURCE 21 MOL_ID: 3; SOURCE 22 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 23 ORGANISM_COMMON: HUMAN; SOURCE 24 ORGANISM_TAXID: 9606; SOURCE 25 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 26 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 27 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 28 EXPRESSION_SYSTEM_CELL_LINE: HEK293; SOURCE 29 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 30 EXPRESSION_SYSTEM_PLASMID: PHCMV3; SOURCE 31 MOL_ID: 4; SOURCE 32 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 33 ORGANISM_COMMON: HUMAN; SOURCE 34 ORGANISM_TAXID: 9606; SOURCE 35 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 36 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 37 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 38 EXPRESSION_SYSTEM_CELL_LINE: HEK293; SOURCE 39 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 40 EXPRESSION_SYSTEM_PLASMID: PHCMV3 KEYWDS VIRAL PROTEIN, HIV-1, ENV, PGT151, BROADLY NEUTRALIZING ANTIBODY EXPDTA ELECTRON MICROSCOPY AUTHOR J.H.LEE,A.B.WARD JRNL AUTH J.H.LEE,G.OZOROWSKI,A.B.WARD JRNL TITL CRYO-EM STRUCTURE OF A NATIVE, FULLY GLYCOSYLATED AND JRNL TITL 2 CLEAVED HIV-1 ENVELOPE TRIMER JRNL REF SCIENCE V. 351 1043 2016 JRNL REFN ISSN 0036-8075 JRNL PMID 26941313 JRNL DOI 10.1126/SCIENCE.AAD2450 REMARK 2 REMARK 2 RESOLUTION. 4.20 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : UCSF CHIMERA, RELION REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : NULL REMARK 3 REFINEMENT SPACE : REAL REMARK 3 REFINEMENT PROTOCOL : OTHER REMARK 3 REFINEMENT TARGET : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL REMARK 3 REMARK 3 FITTING PROCEDURE : REFINEMENT PROTOCOL--EM REMARK 3 REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : 1.310 REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 4.190 REMARK 3 NUMBER OF PARTICLES : 201386 REMARK 3 CTF CORRECTION METHOD : NULL REMARK 3 REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL REMARK 3 REMARK 3 OTHER DETAILS: SUBMISSION BASED ON EXPERIMENTAL DATA FROM EMDB EMD REMARK 3 -3308. (DEPOSITION ID: 14201). REMARK 4 REMARK 4 5FUU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE. REMARK 100 THE DEPOSITION ID IS D_1290066152. 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 : JR-FL ENVDCT IN COMPLEX WITH REMARK 245 PGT151 FAB REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 3.50 REMARK 245 SAMPLE SUPPORT DETAILS : HOLEY CARBON REMARK 245 SAMPLE VITRIFICATION DETAILS : SAMPLES WERE PLUNGED INTO REMARK 245 LIQUID ETHANE USING A MANUAL REMARK 245 PLUNGER AT RT. REMARK 245 SAMPLE BUFFER : 50 MM TRIS, 150 MM NACL, 0.1% REMARK 245 DDM, 0.03 MG/ML SODIUM REMARK 245 DEOXYCHOLATE REMARK 245 PH : 7.40 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : 27-FEB-15 REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS REMARK 245 DETECTOR TYPE : GATAN K2 SUMMIT (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1200.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 3000.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : 0.00 REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : 2.70 REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 32.40 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : 22500 REMARK 245 CALIBRATED MAGNIFICATION : 22500 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, H, L, M, N, REMARK 350 AND CHAINS: G, I, J, K, 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, k, l, REMARK 350 AND CHAINS: m, n, o, p, q, r, s, t, u, v, REMARK 350 AND CHAINS: w, x, y, z, 0, 1, 2, 3, 4, REMARK 350 AND CHAINS: 5, 6, 7, 8, 9, AA, BA REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 ALA A 58 REMARK 465 LYS A 59 REMARK 465 ALA A 60 REMARK 465 TYR A 61 REMARK 465 ASP A 62 REMARK 465 THR A 63 REMARK 465 ASN A 138 REMARK 465 THR A 139 REMARK 465 THR A 140 REMARK 465 ASN A 141 REMARK 465 ASP A 142 REMARK 465 SER A 143 REMARK 465 GLU A 144 REMARK 465 GLY A 145 REMARK 465 THR A 146 REMARK 465 MET A 147 REMARK 465 GLU A 403 REMARK 465 GLY A 404 REMARK 465 SER A 405 REMARK 465 ASN A 406 REMARK 465 ASN A 407 REMARK 465 GLU A 509 REMARK 465 LYS A 510 REMARK 465 ARG A 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 ALA C 60 REMARK 465 TYR C 61 REMARK 465 ASP C 62 REMARK 465 THR C 63 REMARK 465 THR C 137 REMARK 465 ASN C 138 REMARK 465 THR C 139 REMARK 465 THR C 140 REMARK 465 ASN C 141 REMARK 465 ASP C 142 REMARK 465 SER C 143 REMARK 465 GLU C 144 REMARK 465 GLY C 145 REMARK 465 THR C 146 REMARK 465 MET C 147 REMARK 465 GLU C 148 REMARK 465 ARG C 149 REMARK 465 THR C 402 REMARK 465 GLU C 403 REMARK 465 GLY C 404 REMARK 465 SER C 405 REMARK 465 ASN C 406 REMARK 465 ASN C 407 REMARK 465 THR C 408 REMARK 465 GLN C 507 REMARK 465 ARG C 508 REMARK 465 GLU C 509 REMARK 465 LYS C 510 REMARK 465 ARG C 511 REMARK 465 GLU D 659 REMARK 465 LEU D 660 REMARK 465 LEU D 661 REMARK 465 GLU D 662 REMARK 465 LEU D 663 REMARK 465 ASP D 664 REMARK 465 LYS E 59 REMARK 465 ALA E 60 REMARK 465 TYR E 61 REMARK 465 ASP E 62 REMARK 465 THR E 63 REMARK 465 THR E 137 REMARK 465 ASN E 138 REMARK 465 THR E 139 REMARK 465 THR E 140 REMARK 465 ASN E 141 REMARK 465 ASP E 142 REMARK 465 SER E 143 REMARK 465 GLU E 144 REMARK 465 GLY E 145 REMARK 465 THR E 146 REMARK 465 MET E 147 REMARK 465 SER E 405 REMARK 465 ASN E 406 REMARK 465 ASN E 407 REMARK 465 THR E 408 REMARK 465 GLU E 409 REMARK 465 ARG E 508 REMARK 465 GLU E 509 REMARK 465 LYS E 510 REMARK 465 ARG E 511 REMARK 465 ALA H 114 REMARK 465 SER H 115 REMARK 465 THR H 116 REMARK 465 LYS H 117 REMARK 465 GLY H 118 REMARK 465 PRO H 119 REMARK 465 SER H 120 REMARK 465 VAL H 121 REMARK 465 PHE H 122 REMARK 465 PRO H 123 REMARK 465 LEU H 124 REMARK 465 ALA H 125 REMARK 465 PRO H 126 REMARK 465 SER H 127 REMARK 465 SER H 128 REMARK 465 LYS H 129 REMARK 465 SER H 130 REMARK 465 THR H 131 REMARK 465 SER H 132 REMARK 465 GLY H 133 REMARK 465 GLY H 134 REMARK 465 THR H 135 REMARK 465 ALA H 136 REMARK 465 ALA H 137 REMARK 465 LEU H 138 REMARK 465 GLY H 139 REMARK 465 CYS H 140 REMARK 465 LEU H 141 REMARK 465 VAL H 142 REMARK 465 LYS H 143 REMARK 465 ASP H 144 REMARK 465 TYR H 145 REMARK 465 PHE H 146 REMARK 465 PRO H 147 REMARK 465 GLU H 148 REMARK 465 PRO H 149 REMARK 465 VAL H 150 REMARK 465 THR H 151 REMARK 465 VAL H 152 REMARK 465 SER H 153 REMARK 465 TRP H 154 REMARK 465 ASN H 155 REMARK 465 SER H 156 REMARK 465 GLY H 157 REMARK 465 ALA H 158 REMARK 465 LEU H 159 REMARK 465 THR H 160 REMARK 465 SER H 161 REMARK 465 GLY H 162 REMARK 465 VAL H 163 REMARK 465 HIS H 164 REMARK 465 THR H 165 REMARK 465 PHE H 166 REMARK 465 PRO H 167 REMARK 465 ALA H 168 REMARK 465 VAL H 169 REMARK 465 LEU H 170 REMARK 465 GLN H 171 REMARK 465 SER H 172 REMARK 465 SER H 173 REMARK 465 GLY H 174 REMARK 465 LEU H 175 REMARK 465 TYR H 176 REMARK 465 SER H 177 REMARK 465 LEU H 178 REMARK 465 SER H 179 REMARK 465 SER H 180 REMARK 465 VAL H 181 REMARK 465 VAL H 182 REMARK 465 THR H 183 REMARK 465 VAL H 184 REMARK 465 PRO H 185 REMARK 465 SER H 186 REMARK 465 SER H 187 REMARK 465 SER H 188 REMARK 465 LEU H 189 REMARK 465 GLY H 190 REMARK 465 THR H 191 REMARK 465 GLN H 192 REMARK 465 THR H 193 REMARK 465 TYR H 194 REMARK 465 ILE H 195 REMARK 465 CYS H 196 REMARK 465 ASN H 197 REMARK 465 VAL H 198 REMARK 465 ASN H 199 REMARK 465 HIS H 200 REMARK 465 LYS H 201 REMARK 465 PRO H 202 REMARK 465 SER H 203 REMARK 465 ASN H 204 REMARK 465 THR H 205 REMARK 465 LYS H 206 REMARK 465 VAL H 207 REMARK 465 ASP H 208 REMARK 465 LYS H 209 REMARK 465 ARG H 210 REMARK 465 VAL H 211 REMARK 465 GLU H 212 REMARK 465 PRO H 213 REMARK 465 LYS H 214 REMARK 465 SER H 215 REMARK 465 CYS H 216 REMARK 465 ASP H 217 REMARK 465 LYS H 218 REMARK 465 VAL L 110 REMARK 465 ALA L 111 REMARK 465 ALA L 112 REMARK 465 PRO L 113 REMARK 465 SER L 114 REMARK 465 VAL L 115 REMARK 465 PHE L 116 REMARK 465 ILE L 117 REMARK 465 PHE L 118 REMARK 465 PRO L 119 REMARK 465 PRO L 120 REMARK 465 SER L 121 REMARK 465 ASP L 122 REMARK 465 GLU L 123 REMARK 465 GLN L 124 REMARK 465 LEU L 125 REMARK 465 LYS L 126 REMARK 465 SER L 127 REMARK 465 GLY L 128 REMARK 465 THR L 129 REMARK 465 ALA L 130 REMARK 465 SER L 131 REMARK 465 VAL L 132 REMARK 465 VAL L 133 REMARK 465 CYS L 134 REMARK 465 LEU L 135 REMARK 465 LEU L 136 REMARK 465 ASN L 137 REMARK 465 ASN L 138 REMARK 465 PHE L 139 REMARK 465 TYR L 140 REMARK 465 PRO L 141 REMARK 465 ARG L 142 REMARK 465 GLU L 143 REMARK 465 ALA L 144 REMARK 465 LYS L 145 REMARK 465 VAL L 146 REMARK 465 GLN L 147 REMARK 465 TRP L 148 REMARK 465 LYS L 149 REMARK 465 VAL L 150 REMARK 465 ASP L 151 REMARK 465 ASN L 152 REMARK 465 ALA L 153 REMARK 465 LEU L 154 REMARK 465 GLN L 155 REMARK 465 SER L 156 REMARK 465 GLY L 157 REMARK 465 ASN L 158 REMARK 465 SER L 159 REMARK 465 GLN L 160 REMARK 465 GLU L 161 REMARK 465 SER L 162 REMARK 465 VAL L 163 REMARK 465 THR L 164 REMARK 465 GLU L 165 REMARK 465 GLN L 166 REMARK 465 ASP L 167 REMARK 465 SER L 168 REMARK 465 LYS L 169 REMARK 465 ASP L 170 REMARK 465 SER L 171 REMARK 465 THR L 172 REMARK 465 TYR L 173 REMARK 465 SER L 174 REMARK 465 LEU L 175 REMARK 465 SER L 176 REMARK 465 SER L 177 REMARK 465 THR L 178 REMARK 465 LEU L 179 REMARK 465 THR L 180 REMARK 465 LEU L 181 REMARK 465 SER L 182 REMARK 465 LYS L 183 REMARK 465 ALA L 184 REMARK 465 ASP L 185 REMARK 465 TYR L 186 REMARK 465 GLU L 187 REMARK 465 LYS L 188 REMARK 465 HIS L 189 REMARK 465 LYS L 190 REMARK 465 VAL L 191 REMARK 465 TYR L 192 REMARK 465 ALA L 193 REMARK 465 CYS L 194 REMARK 465 GLU L 195 REMARK 465 VAL L 196 REMARK 465 THR L 197 REMARK 465 HIS L 198 REMARK 465 GLN L 199 REMARK 465 GLY L 200 REMARK 465 LEU L 201 REMARK 465 SER L 202 REMARK 465 SER L 203 REMARK 465 PRO L 204 REMARK 465 VAL L 205 REMARK 465 THR L 206 REMARK 465 LYS L 207 REMARK 465 SER L 208 REMARK 465 PHE L 209 REMARK 465 ASN L 210 REMARK 465 ARG L 211 REMARK 465 GLY L 212 REMARK 465 GLU L 213 REMARK 465 CYS L 214 REMARK 465 ARG M 1 REMARK 465 SER M 115 REMARK 465 THR M 116 REMARK 465 LYS M 117 REMARK 465 GLY M 118 REMARK 465 PRO M 119 REMARK 465 SER M 120 REMARK 465 VAL M 121 REMARK 465 PHE M 122 REMARK 465 PRO M 123 REMARK 465 LEU M 124 REMARK 465 ALA M 125 REMARK 465 PRO M 126 REMARK 465 SER M 127 REMARK 465 SER M 128 REMARK 465 LYS M 129 REMARK 465 SER M 130 REMARK 465 THR M 131 REMARK 465 SER M 132 REMARK 465 GLY M 133 REMARK 465 GLY M 134 REMARK 465 THR M 135 REMARK 465 ALA M 136 REMARK 465 ALA M 137 REMARK 465 LEU M 138 REMARK 465 GLY M 139 REMARK 465 CYS M 140 REMARK 465 LEU M 141 REMARK 465 VAL M 142 REMARK 465 LYS M 143 REMARK 465 ASP M 144 REMARK 465 TYR M 145 REMARK 465 PHE M 146 REMARK 465 PRO M 147 REMARK 465 GLU M 148 REMARK 465 PRO M 149 REMARK 465 VAL M 150 REMARK 465 THR M 151 REMARK 465 VAL M 152 REMARK 465 SER M 153 REMARK 465 TRP M 154 REMARK 465 ASN M 155 REMARK 465 SER M 156 REMARK 465 GLY M 157 REMARK 465 ALA M 158 REMARK 465 LEU M 159 REMARK 465 THR M 160 REMARK 465 SER M 161 REMARK 465 GLY M 162 REMARK 465 VAL M 163 REMARK 465 HIS M 164 REMARK 465 THR M 165 REMARK 465 PHE M 166 REMARK 465 PRO M 167 REMARK 465 ALA M 168 REMARK 465 VAL M 169 REMARK 465 LEU M 170 REMARK 465 GLN M 171 REMARK 465 SER M 172 REMARK 465 SER M 173 REMARK 465 GLY M 174 REMARK 465 LEU M 175 REMARK 465 TYR M 176 REMARK 465 SER M 177 REMARK 465 LEU M 178 REMARK 465 SER M 179 REMARK 465 SER M 180 REMARK 465 VAL M 181 REMARK 465 VAL M 182 REMARK 465 THR M 183 REMARK 465 VAL M 184 REMARK 465 PRO M 185 REMARK 465 SER M 186 REMARK 465 SER M 187 REMARK 465 SER M 188 REMARK 465 LEU M 189 REMARK 465 GLY M 190 REMARK 465 THR M 191 REMARK 465 GLN M 192 REMARK 465 THR M 193 REMARK 465 TYR M 194 REMARK 465 ILE M 195 REMARK 465 CYS M 196 REMARK 465 ASN M 197 REMARK 465 VAL M 198 REMARK 465 ASN M 199 REMARK 465 HIS M 200 REMARK 465 LYS M 201 REMARK 465 PRO M 202 REMARK 465 SER M 203 REMARK 465 ASN M 204 REMARK 465 THR M 205 REMARK 465 LYS M 206 REMARK 465 VAL M 207 REMARK 465 ASP M 208 REMARK 465 LYS M 209 REMARK 465 ARG M 210 REMARK 465 VAL M 211 REMARK 465 GLU M 212 REMARK 465 PRO M 213 REMARK 465 LYS M 214 REMARK 465 SER M 215 REMARK 465 CYS M 216 REMARK 465 ASP M 217 REMARK 465 LYS M 218 REMARK 465 ASP N 1 REMARK 465 THR N 109 REMARK 465 VAL N 110 REMARK 465 ALA N 111 REMARK 465 ALA N 112 REMARK 465 PRO N 113 REMARK 465 SER N 114 REMARK 465 VAL N 115 REMARK 465 PHE N 116 REMARK 465 ILE N 117 REMARK 465 PHE N 118 REMARK 465 PRO N 119 REMARK 465 PRO N 120 REMARK 465 SER N 121 REMARK 465 ASP N 122 REMARK 465 GLU N 123 REMARK 465 GLN N 124 REMARK 465 LEU N 125 REMARK 465 LYS N 126 REMARK 465 SER N 127 REMARK 465 GLY N 128 REMARK 465 THR N 129 REMARK 465 ALA N 130 REMARK 465 SER N 131 REMARK 465 VAL N 132 REMARK 465 VAL N 133 REMARK 465 CYS N 134 REMARK 465 LEU N 135 REMARK 465 LEU N 136 REMARK 465 ASN N 137 REMARK 465 ASN N 138 REMARK 465 PHE N 139 REMARK 465 TYR N 140 REMARK 465 PRO N 141 REMARK 465 ARG N 142 REMARK 465 GLU N 143 REMARK 465 ALA N 144 REMARK 465 LYS N 145 REMARK 465 VAL N 146 REMARK 465 GLN N 147 REMARK 465 TRP N 148 REMARK 465 LYS N 149 REMARK 465 VAL N 150 REMARK 465 ASP N 151 REMARK 465 ASN N 152 REMARK 465 ALA N 153 REMARK 465 LEU N 154 REMARK 465 GLN N 155 REMARK 465 SER N 156 REMARK 465 GLY N 157 REMARK 465 ASN N 158 REMARK 465 SER N 159 REMARK 465 GLN N 160 REMARK 465 GLU N 161 REMARK 465 SER N 162 REMARK 465 VAL N 163 REMARK 465 THR N 164 REMARK 465 GLU N 165 REMARK 465 GLN N 166 REMARK 465 ASP N 167 REMARK 465 SER N 168 REMARK 465 LYS N 169 REMARK 465 ASP N 170 REMARK 465 SER N 171 REMARK 465 THR N 172 REMARK 465 TYR N 173 REMARK 465 SER N 174 REMARK 465 LEU N 175 REMARK 465 SER N 176 REMARK 465 SER N 177 REMARK 465 THR N 178 REMARK 465 LEU N 179 REMARK 465 THR N 180 REMARK 465 LEU N 181 REMARK 465 SER N 182 REMARK 465 LYS N 183 REMARK 465 ALA N 184 REMARK 465 ASP N 185 REMARK 465 TYR N 186 REMARK 465 GLU N 187 REMARK 465 LYS N 188 REMARK 465 HIS N 189 REMARK 465 LYS N 190 REMARK 465 VAL N 191 REMARK 465 TYR N 192 REMARK 465 ALA N 193 REMARK 465 CYS N 194 REMARK 465 GLU N 195 REMARK 465 VAL N 196 REMARK 465 THR N 197 REMARK 465 HIS N 198 REMARK 465 GLN N 199 REMARK 465 GLY N 200 REMARK 465 LEU N 201 REMARK 465 SER N 202 REMARK 465 SER N 203 REMARK 465 PRO N 204 REMARK 465 VAL N 205 REMARK 465 THR N 206 REMARK 465 LYS N 207 REMARK 465 SER N 208 REMARK 465 PHE N 209 REMARK 465 ASN N 210 REMARK 465 ARG N 211 REMARK 465 GLY N 212 REMARK 465 GLU N 213 REMARK 465 CYS N 214 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 NE ARG A 298 CD1 ILE A 443 1.86 REMARK 500 CA PRO E 183 CD1 TYR E 191 1.87 REMARK 500 O ALA E 336 OD1 ASN E 339 1.97 REMARK 500 ND2 ASN E 339 O5 NAG 3 1 1.98 REMARK 500 ND2 ASN C 88 O5 NAG a 1 1.98 REMARK 500 ND2 ASN B 611 C2 NAG Y 1 1.99 REMARK 500 OE1 GLU A 87 O7 NAG G 1 2.00 REMARK 500 O3 GAL Y 6 O2 MAN x 6 2.00 REMARK 500 NH1 ARG M 100C OD1 ASP M 100E 2.01 REMARK 500 CG ASN A 156 C1 NAG I 1 2.01 REMARK 500 ND2 ASN A 241 O5 NAG K 1 2.02 REMARK 500 ND2 ASN C 397 O5 NAG C 1397 2.03 REMARK 500 CG ASN C 160 C1 NAG d 1 2.03 REMARK 500 ND2 ASN E 448 O5 NAG 8 1 2.03 REMARK 500 ND2 ASN A 160 O5 NAG J 1 2.04 REMARK 500 ND2 ASN A 88 O5 NAG G 1 2.04 REMARK 500 ND2 ASN F 625 O5 NAGAA 1 2.04 REMARK 500 NH2 ARG A 444 O6 NAG Q 1 2.05 REMARK 500 OD1 ASN A 156 O7 NAG I 1 2.05 REMARK 500 ND2 ASN D 616 O5 NAG D 1600 2.05 REMARK 500 ND2 ASN A 355 O5 NAG A 1355 2.05 REMARK 500 ND2 ASN E 448 C2 NAG 8 1 2.05 REMARK 500 ND2 ASN C 386 O5 NAG n 1 2.05 REMARK 500 CG ASN E 301 C1 NAG 1 1 2.06 REMARK 500 CG ASN C 156 C1 NAG c 1 2.06 REMARK 500 ND2 ASN F 616 O5 NAG F 1600 2.06 REMARK 500 ND2 ASN B 625 O5 NAG B 1625 2.06 REMARK 500 CG ASN C 88 C1 NAG a 1 2.06 REMARK 500 ND2 ASN A 262 O5 NAG O 1 2.07 REMARK 500 CG ASN C 301 C1 NAG i 1 2.07 REMARK 500 CG ASN A 355 C1 NAG A 1355 2.07 REMARK 500 CB ASN A 229 O6 NAG K 1 2.08 REMARK 500 CB ASN A 401 O6 NAG A 1397 2.08 REMARK 500 ND2 ASN E 241 O5 NAG x 1 2.08 REMARK 500 CG ASN E 355 C1 NAG 4 1 2.08 REMARK 500 CG ASN A 397 C1 NAG A 1397 2.08 REMARK 500 ND2 ASN C 241 O5 NAG e 1 2.08 REMARK 500 CG ASN D 625 C1 NAG r 1 2.08 REMARK 500 ND2 ASN C 135 O5 NAG b 1 2.08 REMARK 500 ND2 ASN C 448 O5 NAG p 1 2.09 REMARK 500 ND2 ASN A 339 O5 NAG T 1 2.09 REMARK 500 ND2 ASN E 156 O5 NAG v 1 2.09 REMARK 500 CG ASN F 637 C1 NAGBA 1 2.09 REMARK 500 CE1 TYR C 173 O3 NAG c 1 2.09 REMARK 500 CD1 TYR A 173 C8 NAG I 1 2.10 REMARK 500 ND2 ASN E 362 O5 NAG 5 1 2.10 REMARK 500 CG ASN E 156 C1 NAG v 1 2.10 REMARK 500 CE1 TYR D 638 C6 FUC q 3 2.11 REMARK 500 ND2 ASN E 135 O5 NAG u 1 2.11 REMARK 500 NH2 ARG E 469 O6 NAG 5 1 2.11 REMARK 500 REMARK 500 THIS ENTRY HAS 88 CLOSE CONTACTS 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 PRO A 369 C - N - CA ANGL. DEV. = 9.3 DEGREES REMARK 500 PRO A 493 C - N - CA ANGL. DEV. = 10.0 DEGREES REMARK 500 PRO C 43 C - N - CA ANGL. DEV. = 9.1 DEGREES REMARK 500 PRO C 81 C - N - CA ANGL. DEV. = 11.2 DEGREES REMARK 500 PRO C 183 C - N - CA ANGL. DEV. = 9.6 DEGREES REMARK 500 PRO C 238 C - N - CA ANGL. DEV. = 9.6 DEGREES REMARK 500 PRO C 253 C - N - CA ANGL. DEV. = 9.6 DEGREES REMARK 500 PRO C 299 C - N - CA ANGL. DEV. = 10.7 DEGREES REMARK 500 PHE C 353 N - CA - CB ANGL. DEV. = -11.4 DEGREES REMARK 500 PRO C 369 C - N - CA ANGL. DEV. = 9.7 DEGREES REMARK 500 PRO E 238 C - N - CA ANGL. DEV. = 9.1 DEGREES REMARK 500 PRO E 369 C - N - CA ANGL. DEV. = 9.0 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 SER A 56 -169.92 -164.99 REMARK 500 ASN A 67 160.83 90.83 REMARK 500 ASN A 80 95.02 -161.83 REMARK 500 GLN A 82 63.05 63.96 REMARK 500 ARG A 151 70.30 54.09 REMARK 500 THR A 163 -62.10 -90.02 REMARK 500 ASN A 186 -125.00 49.95 REMARK 500 GLU A 211 74.19 46.33 REMARK 500 THR A 232 125.03 74.94 REMARK 500 GLN A 258 -52.14 65.02 REMARK 500 GLU A 268 -55.80 -120.32 REMARK 500 PRO A 313 105.97 -55.06 REMARK 500 GLU A 354 -124.96 44.98 REMARK 500 ASN A 392 58.38 -149.70 REMARK 500 ASN A 397 165.89 176.65 REMARK 500 ASN A 401 136.05 -39.92 REMARK 500 ASN A 425 71.64 -108.49 REMARK 500 TRP A 427 19.18 59.82 REMARK 500 ALA A 501 175.33 115.71 REMARK 500 ARG A 504 85.05 84.98 REMARK 500 PHE B 522 57.58 -68.92 REMARK 500 ALA B 532 -61.10 106.92 REMARK 500 ALA B 541 -75.99 33.09 REMARK 500 LEU B 543 151.70 -36.09 REMARK 500 LEU B 545 -155.48 158.73 REMARK 500 SER B 546 -159.61 60.69 REMARK 500 GLN B 567 179.08 91.68 REMARK 500 VAL B 570 -82.39 -39.05 REMARK 500 TRP B 571 -39.97 -38.56 REMARK 500 SER B 599 -119.91 55.02 REMARK 500 LYS B 601 137.69 67.68 REMARK 500 PRO C 43 73.82 -60.71 REMARK 500 ASP C 57 137.75 -38.69 REMARK 500 VAL C 65 -58.76 -130.87 REMARK 500 TRP C 69 -104.95 -73.14 REMARK 500 HIS C 72 58.13 -141.40 REMARK 500 ALA C 73 22.76 171.76 REMARK 500 CYS C 74 134.04 -172.59 REMARK 500 ASP C 78 46.81 -148.71 REMARK 500 ASN C 80 99.41 160.64 REMARK 500 GLU C 87 -104.99 -85.00 REMARK 500 ASN C 99 -46.58 -19.12 REMARK 500 PHE C 159 148.96 -172.33 REMARK 500 SER C 164 -115.03 55.02 REMARK 500 ILE C 165 -147.04 -94.98 REMARK 500 ASP C 167 -155.02 59.62 REMARK 500 ASP C 185 83.78 70.04 REMARK 500 ASN C 186 -122.53 58.10 REMARK 500 TYR C 191 -178.95 -170.01 REMARK 500 ILE C 194 -94.69 -14.99 REMARK 500 REMARK 500 THIS ENTRY HAS 116 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 PRO A 81 GLN A 82 30.33 REMARK 500 VAL C 65 HIS C 66 -37.56 REMARK 500 ASN E 412 THR E 413 -46.52 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 PRO A 81 -21.79 REMARK 500 THR A 499 -21.68 REMARK 500 GLN A 507 -21.78 REMARK 500 GLY B 600 22.39 REMARK 500 VAL C 65 21.24 REMARK 500 VAL D 518 -21.86 REMARK 500 SER D 528 -21.62 REMARK 500 GLY D 600 22.04 REMARK 500 VAL E 65 20.98 REMARK 500 HIS E 66 22.08 REMARK 500 CYS E 157 -21.15 REMARK 500 ASN E 412 21.00 REMARK 500 VAL F 518 -21.91 REMARK 500 GLY F 600 20.07 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-3308 RELATED DB: EMDB REMARK 999 REMARK 999 SEQUENCE REMARK 999 V31 WAS FOUND TO HAVE MUTATED TO T31 WHEN THE PLASMID WAS REMARK 999 SEQUENCED DBREF 5FUU A 31 511 UNP Q75760 Q75760_9HIV1 30 502 DBREF 5FUU B 512 664 UNP Q6BC19 Q6BC19_9HIV1 503 655 DBREF 5FUU C 31 511 UNP Q75760 Q75760_9HIV1 30 502 DBREF 5FUU D 512 664 UNP Q6BC19 Q6BC19_9HIV1 503 655 DBREF 5FUU E 31 511 UNP Q75760 Q75760_9HIV1 30 502 DBREF 5FUU F 512 664 UNP Q6BC19 Q6BC19_9HIV1 503 655 DBREF 5FUU H 1 218 PDB 5FUU 5FUU 1 218 DBREF 5FUU L 1 214 PDB 5FUU 5FUU 1 214 DBREF 5FUU M 1 218 PDB 5FUU 5FUU 1 218 DBREF 5FUU N 1 214 PDB 5FUU 5FUU 1 214 SEQADV 5FUU THR A 31 UNP Q75760 VAL 30 ENGINEERED MUTATION SEQADV 5FUU THR C 31 UNP Q75760 VAL 30 ENGINEERED MUTATION SEQADV 5FUU THR E 31 UNP Q75760 VAL 30 ENGINEERED MUTATION SEQRES 1 A 473 THR GLU LYS LEU TRP VAL THR VAL TYR TYR GLY VAL PRO SEQRES 2 A 473 VAL TRP LYS GLU ALA THR THR THR LEU PHE CYS ALA SER SEQRES 3 A 473 ASP ALA LYS ALA TYR ASP THR GLU VAL HIS ASN VAL TRP SEQRES 4 A 473 ALA THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN SEQRES 5 A 473 GLU VAL VAL LEU GLU ASN VAL THR GLU HIS PHE ASN MET SEQRES 6 A 473 TRP LYS ASN ASN MET VAL GLU GLN MET GLN GLU ASP ILE SEQRES 7 A 473 ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS SEQRES 8 A 473 LEU THR PRO LEU CYS VAL THR LEU ASN CYS LYS ASP VAL SEQRES 9 A 473 ASN ALA THR ASN THR THR ASN ASP SER GLU GLY THR MET SEQRES 10 A 473 GLU ARG GLY GLU ILE LYS ASN CYS SER PHE ASN ILE THR SEQRES 11 A 473 THR SER ILE ARG ASP GLU VAL GLN LYS GLU TYR ALA LEU SEQRES 12 A 473 PHE TYR LYS LEU ASP VAL VAL PRO ILE ASP ASN ASN ASN SEQRES 13 A 473 THR SER TYR ARG LEU ILE SER CYS ASP THR SER VAL ILE SEQRES 14 A 473 THR GLN ALA CYS PRO LYS ILE SER PHE GLU PRO ILE PRO SEQRES 15 A 473 ILE HIS TYR CYS ALA PRO ALA GLY PHE ALA ILE LEU LYS SEQRES 16 A 473 CYS ASN ASP LYS THR PHE ASN GLY LYS GLY PRO CYS LYS SEQRES 17 A 473 ASN VAL SER THR VAL GLN CYS THR HIS GLY ILE ARG PRO SEQRES 18 A 473 VAL VAL SER THR GLN LEU LEU LEU ASN GLY SER LEU ALA SEQRES 19 A 473 GLU GLU GLU VAL VAL ILE ARG SER ASP ASN PHE THR ASN SEQRES 20 A 473 ASN ALA LYS THR ILE ILE VAL GLN LEU LYS GLU SER VAL SEQRES 21 A 473 GLU ILE ASN CYS THR ARG PRO ASN ASN ASN THR ARG LYS SEQRES 22 A 473 SER ILE HIS ILE GLY PRO GLY ARG ALA PHE TYR THR THR SEQRES 23 A 473 GLY GLU ILE ILE GLY ASP ILE ARG GLN ALA HIS CYS ASN SEQRES 24 A 473 ILE SER ARG ALA LYS TRP ASN ASP THR LEU LYS GLN ILE SEQRES 25 A 473 VAL ILE LYS LEU ARG GLU GLN PHE GLU ASN LYS THR ILE SEQRES 26 A 473 VAL PHE ASN HIS SER SER GLY GLY ASP PRO GLU ILE VAL SEQRES 27 A 473 MET HIS SER PHE ASN CYS GLY GLY GLU PHE PHE TYR CYS SEQRES 28 A 473 ASN SER THR GLN LEU PHE ASN SER THR TRP ASN ASN ASN SEQRES 29 A 473 THR GLU GLY SER ASN ASN THR GLU GLY ASN THR ILE THR SEQRES 30 A 473 LEU PRO CYS ARG ILE LYS GLN ILE ILE ASN MET TRP GLN SEQRES 31 A 473 GLU VAL GLY LYS ALA MET TYR ALA PRO PRO ILE ARG GLY SEQRES 32 A 473 GLN ILE ARG CYS SER SER ASN ILE THR GLY LEU LEU LEU SEQRES 33 A 473 THR ARG ASP GLY GLY ILE ASN GLU ASN GLY THR GLU ILE SEQRES 34 A 473 PHE ARG PRO GLY GLY GLY ASP MET ARG ASP ASN TRP ARG SEQRES 35 A 473 SER GLU LEU TYR LYS TYR LYS VAL VAL LYS ILE GLU PRO SEQRES 36 A 473 LEU GLY VAL ALA PRO THR LYS ALA LYS ARG ARG VAL VAL SEQRES 37 A 473 GLN ARG GLU LYS ARG SEQRES 1 B 153 ALA VAL GLY ILE GLY ALA VAL PHE LEU GLY PHE LEU GLY SEQRES 2 B 153 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 B 153 THR VAL GLN ALA ARG LEU LEU LEU SER GLY ILE VAL GLN SEQRES 4 B 153 GLN GLN ASN ASN LEU LEU ARG ALA ILE GLU ALA GLN GLN SEQRES 5 B 153 ARG MET LEU GLN LEU THR VAL TRP GLY ILE LYS GLN LEU SEQRES 6 B 153 GLN ALA ARG VAL LEU ALA VAL GLU ARG TYR LEU GLY ASP SEQRES 7 B 153 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 B 153 ILE CYS THR THR ALA VAL PRO TRP ASN ALA SER TRP SER SEQRES 9 B 153 ASN LYS SER LEU ASP ARG ILE TRP ASN ASN MET THR TRP SEQRES 10 B 153 MET GLU TRP GLU ARG GLU ILE ASP ASN TYR THR SER GLU SEQRES 11 B 153 ILE TYR THR LEU ILE GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 B 153 LYS ASN GLU GLN GLU LEU LEU GLU LEU ASP SEQRES 1 C 473 THR GLU LYS LEU TRP VAL THR VAL TYR TYR GLY VAL PRO SEQRES 2 C 473 VAL TRP LYS GLU ALA THR THR THR LEU PHE CYS ALA SER SEQRES 3 C 473 ASP ALA LYS ALA TYR ASP THR GLU VAL HIS ASN VAL TRP SEQRES 4 C 473 ALA THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN SEQRES 5 C 473 GLU VAL VAL LEU GLU ASN VAL THR GLU HIS PHE ASN MET SEQRES 6 C 473 TRP LYS ASN ASN MET VAL GLU GLN MET GLN GLU ASP ILE SEQRES 7 C 473 ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS SEQRES 8 C 473 LEU THR PRO LEU CYS VAL THR LEU ASN CYS LYS ASP VAL SEQRES 9 C 473 ASN ALA THR ASN THR THR ASN ASP SER GLU GLY THR MET SEQRES 10 C 473 GLU ARG GLY GLU ILE LYS ASN CYS SER PHE ASN ILE THR SEQRES 11 C 473 THR SER ILE ARG ASP GLU VAL GLN LYS GLU TYR ALA LEU SEQRES 12 C 473 PHE TYR LYS LEU ASP VAL VAL PRO ILE ASP ASN ASN ASN SEQRES 13 C 473 THR SER TYR ARG LEU ILE SER CYS ASP THR SER VAL ILE SEQRES 14 C 473 THR GLN ALA CYS PRO LYS ILE SER PHE GLU PRO ILE PRO SEQRES 15 C 473 ILE HIS TYR CYS ALA PRO ALA GLY PHE ALA ILE LEU LYS SEQRES 16 C 473 CYS ASN ASP LYS THR PHE ASN GLY LYS GLY PRO CYS LYS SEQRES 17 C 473 ASN VAL SER THR VAL GLN CYS THR HIS GLY ILE ARG PRO SEQRES 18 C 473 VAL VAL SER THR GLN LEU LEU LEU ASN GLY SER LEU ALA SEQRES 19 C 473 GLU GLU GLU VAL VAL ILE ARG SER ASP ASN PHE THR ASN SEQRES 20 C 473 ASN ALA LYS THR ILE ILE VAL GLN LEU LYS GLU SER VAL SEQRES 21 C 473 GLU ILE ASN CYS THR ARG PRO ASN ASN ASN THR ARG LYS SEQRES 22 C 473 SER ILE HIS ILE GLY PRO GLY ARG ALA PHE TYR THR THR SEQRES 23 C 473 GLY GLU ILE ILE GLY ASP ILE ARG GLN ALA HIS CYS ASN SEQRES 24 C 473 ILE SER ARG ALA LYS TRP ASN ASP THR LEU LYS GLN ILE SEQRES 25 C 473 VAL ILE LYS LEU ARG GLU GLN PHE GLU ASN LYS THR ILE SEQRES 26 C 473 VAL PHE ASN HIS SER SER GLY GLY ASP PRO GLU ILE VAL SEQRES 27 C 473 MET HIS SER PHE ASN CYS GLY GLY GLU PHE PHE TYR CYS SEQRES 28 C 473 ASN SER THR GLN LEU PHE ASN SER THR TRP ASN ASN ASN SEQRES 29 C 473 THR GLU GLY SER ASN ASN THR GLU GLY ASN THR ILE THR SEQRES 30 C 473 LEU PRO CYS ARG ILE LYS GLN ILE ILE ASN MET TRP GLN SEQRES 31 C 473 GLU VAL GLY LYS ALA MET TYR ALA PRO PRO ILE ARG GLY SEQRES 32 C 473 GLN ILE ARG CYS SER SER ASN ILE THR GLY LEU LEU LEU SEQRES 33 C 473 THR ARG ASP GLY GLY ILE ASN GLU ASN GLY THR GLU ILE SEQRES 34 C 473 PHE ARG PRO GLY GLY GLY ASP MET ARG ASP ASN TRP ARG SEQRES 35 C 473 SER GLU LEU TYR LYS TYR LYS VAL VAL LYS ILE GLU PRO SEQRES 36 C 473 LEU GLY VAL ALA PRO THR LYS ALA LYS ARG ARG VAL VAL SEQRES 37 C 473 GLN ARG GLU LYS ARG SEQRES 1 D 153 ALA VAL GLY ILE GLY ALA VAL PHE LEU GLY PHE LEU GLY SEQRES 2 D 153 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 D 153 THR VAL GLN ALA ARG LEU LEU LEU SER GLY ILE VAL GLN SEQRES 4 D 153 GLN GLN ASN ASN LEU LEU ARG ALA ILE GLU ALA GLN GLN SEQRES 5 D 153 ARG MET LEU GLN LEU THR VAL TRP GLY ILE LYS GLN LEU SEQRES 6 D 153 GLN ALA ARG VAL LEU ALA VAL GLU ARG TYR LEU GLY ASP SEQRES 7 D 153 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 D 153 ILE CYS THR THR ALA VAL PRO TRP ASN ALA SER TRP SER SEQRES 9 D 153 ASN LYS SER LEU ASP ARG ILE TRP ASN ASN MET THR TRP SEQRES 10 D 153 MET GLU TRP GLU ARG GLU ILE ASP ASN TYR THR SER GLU SEQRES 11 D 153 ILE TYR THR LEU ILE GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 D 153 LYS ASN GLU GLN GLU LEU LEU GLU LEU ASP SEQRES 1 E 473 THR GLU LYS LEU TRP VAL THR VAL TYR TYR GLY VAL PRO SEQRES 2 E 473 VAL TRP LYS GLU ALA THR THR THR LEU PHE CYS ALA SER SEQRES 3 E 473 ASP ALA LYS ALA TYR ASP THR GLU VAL HIS ASN VAL TRP SEQRES 4 E 473 ALA THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN SEQRES 5 E 473 GLU VAL VAL LEU GLU ASN VAL THR GLU HIS PHE ASN MET SEQRES 6 E 473 TRP LYS ASN ASN MET VAL GLU GLN MET GLN GLU ASP ILE SEQRES 7 E 473 ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS SEQRES 8 E 473 LEU THR PRO LEU CYS VAL THR LEU ASN CYS LYS ASP VAL SEQRES 9 E 473 ASN ALA THR ASN THR THR ASN ASP SER GLU GLY THR MET SEQRES 10 E 473 GLU ARG GLY GLU ILE LYS ASN CYS SER PHE ASN ILE THR SEQRES 11 E 473 THR SER ILE ARG ASP GLU VAL GLN LYS GLU TYR ALA LEU SEQRES 12 E 473 PHE TYR LYS LEU ASP VAL VAL PRO ILE ASP ASN ASN ASN SEQRES 13 E 473 THR SER TYR ARG LEU ILE SER CYS ASP THR SER VAL ILE SEQRES 14 E 473 THR GLN ALA CYS PRO LYS ILE SER PHE GLU PRO ILE PRO SEQRES 15 E 473 ILE HIS TYR CYS ALA PRO ALA GLY PHE ALA ILE LEU LYS SEQRES 16 E 473 CYS ASN ASP LYS THR PHE ASN GLY LYS GLY PRO CYS LYS SEQRES 17 E 473 ASN VAL SER THR VAL GLN CYS THR HIS GLY ILE ARG PRO SEQRES 18 E 473 VAL VAL SER THR GLN LEU LEU LEU ASN GLY SER LEU ALA SEQRES 19 E 473 GLU GLU GLU VAL VAL ILE ARG SER ASP ASN PHE THR ASN SEQRES 20 E 473 ASN ALA LYS THR ILE ILE VAL GLN LEU LYS GLU SER VAL SEQRES 21 E 473 GLU ILE ASN CYS THR ARG PRO ASN ASN ASN THR ARG LYS SEQRES 22 E 473 SER ILE HIS ILE GLY PRO GLY ARG ALA PHE TYR THR THR SEQRES 23 E 473 GLY GLU ILE ILE GLY ASP ILE ARG GLN ALA HIS CYS ASN SEQRES 24 E 473 ILE SER ARG ALA LYS TRP ASN ASP THR LEU LYS GLN ILE SEQRES 25 E 473 VAL ILE LYS LEU ARG GLU GLN PHE GLU ASN LYS THR ILE SEQRES 26 E 473 VAL PHE ASN HIS SER SER GLY GLY ASP PRO GLU ILE VAL SEQRES 27 E 473 MET HIS SER PHE ASN CYS GLY GLY GLU PHE PHE TYR CYS SEQRES 28 E 473 ASN SER THR GLN LEU PHE ASN SER THR TRP ASN ASN ASN SEQRES 29 E 473 THR GLU GLY SER ASN ASN THR GLU GLY ASN THR ILE THR SEQRES 30 E 473 LEU PRO CYS ARG ILE LYS GLN ILE ILE ASN MET TRP GLN SEQRES 31 E 473 GLU VAL GLY LYS ALA MET TYR ALA PRO PRO ILE ARG GLY SEQRES 32 E 473 GLN ILE ARG CYS SER SER ASN ILE THR GLY LEU LEU LEU SEQRES 33 E 473 THR ARG ASP GLY GLY ILE ASN GLU ASN GLY THR GLU ILE SEQRES 34 E 473 PHE ARG PRO GLY GLY GLY ASP MET ARG ASP ASN TRP ARG SEQRES 35 E 473 SER GLU LEU TYR LYS TYR LYS VAL VAL LYS ILE GLU PRO SEQRES 36 E 473 LEU GLY VAL ALA PRO THR LYS ALA LYS ARG ARG VAL VAL SEQRES 37 E 473 GLN ARG GLU LYS ARG SEQRES 1 F 153 ALA VAL GLY ILE GLY ALA VAL PHE LEU GLY PHE LEU GLY SEQRES 2 F 153 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 F 153 THR VAL GLN ALA ARG LEU LEU LEU SER GLY ILE VAL GLN SEQRES 4 F 153 GLN GLN ASN ASN LEU LEU ARG ALA ILE GLU ALA GLN GLN SEQRES 5 F 153 ARG MET LEU GLN LEU THR VAL TRP GLY ILE LYS GLN LEU SEQRES 6 F 153 GLN ALA ARG VAL LEU ALA VAL GLU ARG TYR LEU GLY ASP SEQRES 7 F 153 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 F 153 ILE CYS THR THR ALA VAL PRO TRP ASN ALA SER TRP SER SEQRES 9 F 153 ASN LYS SER LEU ASP ARG ILE TRP ASN ASN MET THR TRP SEQRES 10 F 153 MET GLU TRP GLU ARG GLU ILE ASP ASN TYR THR SER GLU SEQRES 11 F 153 ILE TYR THR LEU ILE GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 F 153 LYS ASN GLU GLN GLU LEU LEU GLU LEU ASP SEQRES 1 H 240 ARG VAL GLN LEU VAL GLU SER GLY GLY GLY VAL VAL GLN SEQRES 2 H 240 PRO GLY LYS SER VAL ARG LEU SER CYS VAL VAL SER ASP SEQRES 3 H 240 PHE PRO PHE SER LYS TYR PRO MET TYR TRP VAL ARG GLN SEQRES 4 H 240 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA ALA ILE SER SEQRES 5 H 240 GLY ASP ALA TRP HIS VAL VAL TYR SER ASN SER VAL GLN SEQRES 6 H 240 GLY ARG PHE LEU VAL SER ARG ASP ASN VAL LYS ASN THR SEQRES 7 H 240 LEU TYR LEU GLU MET ASN SER LEU LYS ILE GLU ASP THR SEQRES 8 H 240 ALA VAL TYR ARG CYS ALA ARG MET PHE GLN GLU SER GLY SEQRES 9 H 240 PRO PRO ARG LEU ASP ARG TRP SER GLY ARG ASN TYR TYR SEQRES 10 H 240 TYR TYR SER GLY MET ASP VAL TRP GLY GLN GLY THR THR SEQRES 11 H 240 VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL SEQRES 12 H 240 PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY SEQRES 13 H 240 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO SEQRES 14 H 240 GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SEQRES 15 H 240 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER SEQRES 16 H 240 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SEQRES 17 H 240 SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN SEQRES 18 H 240 HIS LYS PRO SER ASN THR LYS VAL ASP LYS ARG VAL GLU SEQRES 19 H 240 PRO LYS SER CYS ASP LYS SEQRES 1 L 219 ASP ILE VAL MET THR GLN THR PRO LEU SER LEU SER VAL SEQRES 2 L 219 THR PRO GLY GLN PRO ALA SER ILE SER CYS LYS SER SER SEQRES 3 L 219 GLU SER LEU ARG GLN SER ASN GLY LYS THR SER LEU TYR SEQRES 4 L 219 TRP TYR ARG GLN LYS PRO GLY GLN SER PRO GLN LEU LEU SEQRES 5 L 219 VAL PHE GLU VAL SER ASN ARG PHE SER GLY VAL SER ASP SEQRES 6 L 219 ARG PHE VAL GLY SER GLY SER GLY THR ASP PHE THR LEU SEQRES 7 L 219 ARG ILE SER ARG VAL GLU ALA GLU ASP VAL GLY PHE TYR SEQRES 8 L 219 TYR CYS MET GLN SER LYS ASP PHE PRO LEU THR PHE GLY SEQRES 9 L 219 GLY GLY THR LYS VAL ASP LEU LYS ARG THR VAL ALA ALA SEQRES 10 L 219 PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU SEQRES 11 L 219 LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN SEQRES 12 L 219 PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP SEQRES 13 L 219 ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL THR SEQRES 14 L 219 GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER SER SEQRES 15 L 219 THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS SEQRES 16 L 219 VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER SEQRES 17 L 219 PRO VAL THR LYS SER PHE ASN ARG GLY GLU CYS SEQRES 1 M 240 ARG VAL GLN LEU VAL GLU SER GLY GLY GLY VAL VAL GLN SEQRES 2 M 240 PRO GLY LYS SER VAL ARG LEU SER CYS VAL VAL SER ASP SEQRES 3 M 240 PHE PRO PHE SER LYS TYR PRO MET TYR TRP VAL ARG GLN SEQRES 4 M 240 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA ALA ILE SER SEQRES 5 M 240 GLY ASP ALA TRP HIS VAL VAL TYR SER ASN SER VAL GLN SEQRES 6 M 240 GLY ARG PHE LEU VAL SER ARG ASP ASN VAL LYS ASN THR SEQRES 7 M 240 LEU TYR LEU GLU MET ASN SER LEU LYS ILE GLU ASP THR SEQRES 8 M 240 ALA VAL TYR ARG CYS ALA ARG MET PHE GLN GLU SER GLY SEQRES 9 M 240 PRO PRO ARG LEU ASP ARG TRP SER GLY ARG ASN TYR TYR SEQRES 10 M 240 TYR TYR SER GLY MET ASP VAL TRP GLY GLN GLY THR THR SEQRES 11 M 240 VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL SEQRES 12 M 240 PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY SEQRES 13 M 240 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO SEQRES 14 M 240 GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SEQRES 15 M 240 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER SEQRES 16 M 240 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SEQRES 17 M 240 SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN SEQRES 18 M 240 HIS LYS PRO SER ASN THR LYS VAL ASP LYS ARG VAL GLU SEQRES 19 M 240 PRO LYS SER CYS ASP LYS SEQRES 1 N 219 ASP ILE VAL MET THR GLN THR PRO LEU SER LEU SER VAL SEQRES 2 N 219 THR PRO GLY GLN PRO ALA SER ILE SER CYS LYS SER SER SEQRES 3 N 219 GLU SER LEU ARG GLN SER ASN GLY LYS THR SER LEU TYR SEQRES 4 N 219 TRP TYR ARG GLN LYS PRO GLY GLN SER PRO GLN LEU LEU SEQRES 5 N 219 VAL PHE GLU VAL SER ASN ARG PHE SER GLY VAL SER ASP SEQRES 6 N 219 ARG PHE VAL GLY SER GLY SER GLY THR ASP PHE THR LEU SEQRES 7 N 219 ARG ILE SER ARG VAL GLU ALA GLU ASP VAL GLY PHE TYR SEQRES 8 N 219 TYR CYS MET GLN SER LYS ASP PHE PRO LEU THR PHE GLY SEQRES 9 N 219 GLY GLY THR LYS VAL ASP LEU LYS ARG THR VAL ALA ALA SEQRES 10 N 219 PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU SEQRES 11 N 219 LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN SEQRES 12 N 219 PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP SEQRES 13 N 219 ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL THR SEQRES 14 N 219 GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER SER SEQRES 15 N 219 THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS SEQRES 16 N 219 VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER SEQRES 17 N 219 PRO VAL THR LYS SER PHE ASN ARG GLY GLU CYS MODRES 5FUU ASN A 88 ASN GLYCOSYLATION SITE MODRES 5FUU ASN A 135 ASN GLYCOSYLATION SITE MODRES 5FUU ASN A 156 ASN GLYCOSYLATION SITE MODRES 5FUU ASN A 160 ASN GLYCOSYLATION SITE MODRES 5FUU ASN A 241 ASN GLYCOSYLATION SITE MODRES 5FUU ASN A 262 ASN GLYCOSYLATION SITE MODRES 5FUU ASN A 276 ASN GLYCOSYLATION SITE MODRES 5FUU ASN A 295 ASN GLYCOSYLATION SITE MODRES 5FUU ASN A 301 ASN GLYCOSYLATION SITE MODRES 5FUU ASN A 332 ASN GLYCOSYLATION SITE MODRES 5FUU ASN A 339 ASN GLYCOSYLATION SITE MODRES 5FUU ASN A 355 ASN GLYCOSYLATION SITE MODRES 5FUU ASN A 362 ASN GLYCOSYLATION SITE MODRES 5FUU ASN A 386 ASN GLYCOSYLATION SITE MODRES 5FUU ASN A 392 ASN GLYCOSYLATION SITE MODRES 5FUU ASN A 397 ASN GLYCOSYLATION SITE MODRES 5FUU ASN A 448 ASN GLYCOSYLATION SITE MODRES 5FUU ASN B 611 ASN GLYCOSYLATION SITE MODRES 5FUU ASN B 616 ASN GLYCOSYLATION SITE MODRES 5FUU ASN B 625 ASN GLYCOSYLATION SITE MODRES 5FUU ASN B 637 ASN GLYCOSYLATION SITE MODRES 5FUU ASN C 88 ASN GLYCOSYLATION SITE MODRES 5FUU ASN C 135 ASN GLYCOSYLATION SITE MODRES 5FUU ASN C 156 ASN GLYCOSYLATION SITE MODRES 5FUU ASN C 160 ASN GLYCOSYLATION SITE MODRES 5FUU ASN C 241 ASN GLYCOSYLATION SITE MODRES 5FUU ASN C 262 ASN GLYCOSYLATION SITE MODRES 5FUU ASN C 276 ASN GLYCOSYLATION SITE MODRES 5FUU ASN C 295 ASN GLYCOSYLATION SITE MODRES 5FUU ASN C 301 ASN GLYCOSYLATION SITE MODRES 5FUU ASN C 332 ASN GLYCOSYLATION SITE MODRES 5FUU ASN C 339 ASN GLYCOSYLATION SITE MODRES 5FUU ASN C 355 ASN GLYCOSYLATION SITE MODRES 5FUU ASN C 362 ASN GLYCOSYLATION SITE MODRES 5FUU ASN C 386 ASN GLYCOSYLATION SITE MODRES 5FUU ASN C 392 ASN GLYCOSYLATION SITE MODRES 5FUU ASN C 397 ASN GLYCOSYLATION SITE MODRES 5FUU ASN C 448 ASN GLYCOSYLATION SITE MODRES 5FUU ASN D 611 ASN GLYCOSYLATION SITE MODRES 5FUU ASN D 616 ASN GLYCOSYLATION SITE MODRES 5FUU ASN D 625 ASN GLYCOSYLATION SITE MODRES 5FUU ASN D 637 ASN GLYCOSYLATION SITE MODRES 5FUU ASN E 88 ASN GLYCOSYLATION SITE MODRES 5FUU ASN E 135 ASN GLYCOSYLATION SITE MODRES 5FUU ASN E 156 ASN GLYCOSYLATION SITE MODRES 5FUU ASN E 160 ASN GLYCOSYLATION SITE MODRES 5FUU ASN E 187 ASN GLYCOSYLATION SITE MODRES 5FUU ASN E 241 ASN GLYCOSYLATION SITE MODRES 5FUU ASN E 262 ASN GLYCOSYLATION SITE MODRES 5FUU ASN E 276 ASN GLYCOSYLATION SITE MODRES 5FUU ASN E 295 ASN GLYCOSYLATION SITE MODRES 5FUU ASN E 301 ASN GLYCOSYLATION SITE MODRES 5FUU ASN E 332 ASN GLYCOSYLATION SITE MODRES 5FUU ASN E 339 ASN GLYCOSYLATION SITE MODRES 5FUU ASN E 355 ASN GLYCOSYLATION SITE MODRES 5FUU ASN E 362 ASN GLYCOSYLATION SITE MODRES 5FUU ASN E 386 ASN GLYCOSYLATION SITE MODRES 5FUU ASN E 392 ASN GLYCOSYLATION SITE MODRES 5FUU ASN E 397 ASN GLYCOSYLATION SITE MODRES 5FUU ASN E 448 ASN GLYCOSYLATION SITE MODRES 5FUU ASN F 611 ASN GLYCOSYLATION SITE MODRES 5FUU ASN F 616 ASN GLYCOSYLATION SITE MODRES 5FUU ASN F 625 ASN GLYCOSYLATION SITE MODRES 5FUU ASN F 637 ASN GLYCOSYLATION SITE HET NAG A1135 14 HET NAG A1355 14 HET NAG A1397 14 HET NAG B1600 14 HET NAG B1625 14 HET NAG C1397 14 HET NAG D1600 14 HET NAG E1187 14 HET NAG E1397 14 HET NAG F1600 14 HET NAG G 1 14 HET NAG G 2 14 HET NAG I 1 14 HET NAG I 2 14 HET BMA I 3 11 HET NAG J 1 14 HET NAG J 2 14 HET BMA J 3 11 HET NAG K 1 14 HET NAG K 2 14 HET BMA K 3 11 HET NAG O 1 14 HET NAG O 2 14 HET BMA O 3 11 HET MAN O 4 11 HET MAN O 5 11 HET MAN O 6 11 HET MAN O 7 11 HET NAG P 1 14 HET NAG P 2 14 HET BMA P 3 11 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 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 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 BMA W 3 11 HET NAG X 1 14 HET NAG X 2 14 HET NAG Y 1 14 HET NAG Y 2 14 HET BMA Y 3 11 HET MAN Y 4 11 HET NAG Y 5 14 HET GAL Y 6 11 HET NAG Y 7 14 HET GAL Y 8 11 HET MAN Y 9 11 HET NAG Y 10 14 HET FUC Y 11 10 HET NAG Z 1 14 HET NAG Z 2 14 HET BMA Z 3 11 HET MAN Z 4 11 HET NAG Z 5 14 HET GAL Z 6 11 HET NAG Z 7 14 HET GAL Z 8 11 HET MAN Z 9 11 HET NAG Z 10 14 HET GAL Z 11 11 HET NAG Z 12 14 HET FUC Z 13 10 HET NAG a 1 14 HET NAG a 2 14 HET BMA a 3 11 HET NAG b 1 14 HET NAG b 2 14 HET NAG c 1 14 HET NAG c 2 14 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 BMA e 3 11 HET MAN e 4 11 HET MAN e 5 11 HET NAG f 1 14 HET NAG f 2 14 HET BMA f 3 11 HET MAN f 4 11 HET MAN f 5 11 HET MAN f 6 11 HET MAN f 7 11 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 NAG i 1 14 HET NAG i 2 14 HET BMA i 3 11 HET NAG j 1 14 HET NAG j 2 14 HET BMA j 3 11 HET NAG k 1 14 HET NAG k 2 14 HET NAG l 1 14 HET NAG l 2 14 HET NAG m 1 14 HET NAG m 2 14 HET BMA m 3 11 HET NAG n 1 14 HET NAG n 2 14 HET BMA n 3 11 HET NAG o 1 14 HET NAG o 2 14 HET NAG p 1 14 HET NAG p 2 14 HET BMA p 3 11 HET MAN p 4 11 HET MAN p 5 11 HET MAN p 6 11 HET MAN p 7 11 HET MAN p 8 11 HET NAG q 1 14 HET NAG q 2 14 HET FUC q 3 10 HET NAG r 1 14 HET NAG r 2 14 HET NAG s 1 14 HET NAG s 2 14 HET NAG t 1 14 HET NAG t 2 14 HET BMA t 3 11 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 MAN x 4 11 HET MAN x 5 11 HET MAN x 6 11 HET NAG y 1 14 HET NAG y 2 14 HET BMA y 3 11 HET MAN y 4 11 HET MAN y 5 11 HET MAN y 6 11 HET MAN y 7 11 HET NAG z 1 14 HET NAG z 2 14 HET NAG 0 1 14 HET NAG 0 2 14 HET NAG 1 1 14 HET NAG 1 2 14 HET NAG 2 1 14 HET NAG 2 2 14 HET BMA 2 3 11 HET NAG 3 1 14 HET NAG 3 2 14 HET NAG 4 1 14 HET NAG 4 2 14 HET NAG 5 1 14 HET NAG 5 2 14 HET NAG 6 1 14 HET NAG 6 2 14 HET BMA 6 3 11 HET MAN 6 4 11 HET NAG 7 1 14 HET NAG 7 2 14 HET BMA 7 3 11 HET NAG 8 1 14 HET NAG 8 2 14 HET BMA 8 3 11 HET MAN 8 4 11 HET MAN 8 5 11 HET MAN 8 6 11 HET MAN 8 7 11 HET MAN 8 8 11 HET NAG 9 1 14 HET NAG 9 2 14 HET BMA 9 3 11 HET MAN 9 4 11 HET NAG 9 5 14 HET GAL 9 6 11 HET NAG 9 7 14 HET GAL 9 8 11 HET MAN 9 9 11 HET NAG 9 10 14 HET FUC 9 11 10 HET NAG AA 1 14 HET NAG AA 2 14 HET NAG BA 1 14 HET NAG BA 2 14 HET BMA BA 3 11 HET MAN BA 4 11 HET NAG BA 5 14 HET GAL BA 6 11 HET NAG BA 7 14 HET GAL BA 8 11 HET MAN BA 9 11 HET NAG BA 10 14 HET NAG BA 11 14 HET FUC BA 12 10 HETNAM NAG N-ACETYL-D-GLUCOSAMINE HETNAM BMA BETA-D-MANNOSE HETNAM MAN ALPHA-D-MANNOSE HETNAM GAL BETA-D-GALACTOSE HETNAM FUC ALPHA-L-FUCOSE FORMUL 11 NAG 132(C8 H15 N O6) FORMUL 22 BMA 31(C6 H12 O6) FORMUL 25 MAN 36(C6 H12 O6) FORMUL 35 GAL 9(C6 H12 O6) FORMUL 35 FUC 5(C6 H12 O5) HELIX 1 1 ALA A 70 CYS A 74 5 5 HELIX 2 2 ASN A 99 LYS A 117 1 19 HELIX 3 3 LEU A 122 CYS A 126 5 5 HELIX 4 4 ARG A 335 PHE A 353 1 19 HELIX 5 5 ASP A 368 MET A 373 1 6 HELIX 6 6 SER A 387 PHE A 391 5 5 HELIX 7 7 ASN A 425 GLU A 429 5 5 HELIX 8 8 MET A 475 TYR A 484 1 10 HELIX 9 9 LEU B 523 SER B 528 5 6 HELIX 10 10 THR B 529 ALA B 541 1 13 HELIX 11 11 GLY B 547 LEU B 566 1 20 HELIX 12 12 THR B 569 TRP B 596 1 28 HELIX 13 13 SER B 618 ASN B 624 1 7 HELIX 14 14 THR B 627 GLU B 634 1 8 HELIX 15 15 ILE B 635 ASN B 651 1 17 HELIX 16 16 ASN B 651 LEU B 663 1 13 HELIX 17 17 TRP C 96 ASN C 98 5 3 HELIX 18 18 ASN C 99 SER C 115 1 17 HELIX 19 19 THR C 123 VAL C 127 5 5 HELIX 20 20 TYR C 177 LEU C 179 5 3 HELIX 21 21 SER C 195 SER C 199 5 5 HELIX 22 22 ARG C 335 PHE C 353 1 19 HELIX 23 23 ASP C 368 MET C 373 1 6 HELIX 24 24 SER C 387 PHE C 391 5 5 HELIX 25 25 ASN C 425 GLU C 429 5 5 HELIX 26 26 MET C 475 SER C 481 1 7 HELIX 27 27 LEU D 523 SER D 528 5 6 HELIX 28 28 THR D 529 SER D 534 1 6 HELIX 29 29 THR D 536 ARG D 542 1 7 HELIX 30 30 LEU D 555 ARG D 564 1 10 HELIX 31 31 VAL D 570 GLY D 597 1 28 HELIX 32 32 SER D 618 ASN D 625 1 8 HELIX 33 33 THR D 627 ASP D 636 1 10 HELIX 34 34 TYR D 638 GLU D 657 1 20 HELIX 35 35 TRP E 69 ALA E 73 5 5 HELIX 36 36 ASN E 98 LYS E 117 1 20 HELIX 37 37 ALA E 336 PHE E 353 1 18 HELIX 38 38 ASP E 368 MET E 373 1 6 HELIX 39 39 SER E 387 ASN E 392 1 6 HELIX 40 40 ASN E 425 GLU E 429 5 5 HELIX 41 41 ILE E 460 GLY E 464 5 5 HELIX 42 42 MET E 475 TYR E 484 1 10 HELIX 43 43 THR F 529 SER F 534 1 6 HELIX 44 44 THR F 536 ARG F 542 1 7 HELIX 45 45 ASN F 553 LEU F 566 1 14 HELIX 46 46 THR F 569 TRP F 596 1 28 HELIX 47 47 SER F 618 TRP F 623 1 6 HELIX 48 48 THR F 627 ASP F 636 1 10 HELIX 49 49 TYR F 638 GLN F 652 1 15 HELIX 50 50 LYS F 655 GLU F 662 1 8 HELIX 51 51 LYS H 83 THR H 87 5 5 HELIX 52 52 GLU L 79 VAL L 83 5 5 HELIX 53 53 PRO M 28 TYR M 32 5 5 HELIX 54 54 LYS M 83 THR M 87 5 5 SHEET 1 AA 3 LEU A 494 ALA A 497 0 SHEET 2 AA 3 TRP A 35 TYR A 40 -1 O THR A 37 N ALA A 497 SHEET 3 AA 3 ILE B 603 PRO B 609 -1 O CYS B 604 N VAL A 38 SHEET 1 AB 5 TRP A 45 GLU A 47 0 SHEET 2 AB 5 TYR A 486 ILE A 491 -1 O LYS A 490 N LYS A 46 SHEET 3 AB 5 PHE A 223 CYS A 228 -1 O ALA A 224 N VAL A 489 SHEET 4 AB 5 VAL A 242 VAL A 245 -1 O SER A 243 N LYS A 227 SHEET 5 AB 5 GLU A 83 VAL A 85 -1 O VAL A 84 N THR A 244 SHEET 1 AC 3 VAL A 75 PRO A 76 0 SHEET 2 AC 3 PHE A 53 SER A 56 1 O CYS A 54 N VAL A 75 SHEET 3 AC 3 HIS A 216 CYS A 218 -1 O HIS A 216 N ALA A 55 SHEET 1 AD 2 GLU A 91 ASN A 94 0 SHEET 2 AD 2 LYS A 236 CYS A 239 -1 O GLY A 237 N PHE A 93 SHEET 1 AE 5 LYS A 171 TYR A 177 0 SHEET 2 AE 5 ILE A 154 ASN A 160 -1 O LYS A 155 N PHE A 176 SHEET 3 AE 5 LEU A 129 ASP A 133 -1 O ASN A 130 N SER A 158 SHEET 4 AE 5 SER A 190 LEU A 193 -1 O TYR A 191 N LEU A 129 SHEET 5 AE 5 VAL A 181 ILE A 184 -1 O VAL A 182 N ARG A 192 SHEET 1 AF 3 VAL A 200 GLN A 203 0 SHEET 2 AF 3 LYS A 432 TYR A 435 1 O ALA A 433 N THR A 202 SHEET 3 AF 3 ILE A 423 ILE A 424 -1 O ILE A 424 N MET A 434 SHEET 1 AG10 SER A 256 THR A 257 0 SHEET 2 AG10 HIS A 374 CYS A 378 -1 O SER A 375 N THR A 257 SHEET 3 AG10 GLU A 381 CYS A 385 1 O GLU A 381 N CYS A 378 SHEET 4 AG10 THR A 413 ILE A 420 1 O ARG A 419 N TYR A 384 SHEET 5 AG10 HIS A 330 SER A 334 -1 O CYS A 331 N LEU A 416 SHEET 6 AG10 ILE A 284 ARG A 298 -1 O GLU A 293 N SER A 334 SHEET 7 AG10 ILE A 443 ARG A 456 -1 O ILE A 443 N ARG A 298 SHEET 8 AG10 THR A 465 PRO A 470 -1 O ARG A 469 N THR A 455 SHEET 9 AG10 THR A 358 PHE A 361 1 O THR A 358 N GLU A 466 SHEET 10 AG10 SER A 393 TRP A 395 -1 O SER A 393 N PHE A 361 SHEET 1 AH 7 SER A 256 THR A 257 0 SHEET 2 AH 7 HIS A 374 CYS A 378 -1 O SER A 375 N THR A 257 SHEET 3 AH 7 GLU A 381 CYS A 385 1 O GLU A 381 N CYS A 378 SHEET 4 AH 7 THR A 413 ILE A 420 1 O ARG A 419 N TYR A 384 SHEET 5 AH 7 HIS A 330 SER A 334 -1 O CYS A 331 N LEU A 416 SHEET 6 AH 7 ILE A 284 ARG A 298 -1 O GLU A 293 N SER A 334 SHEET 7 AH 7 VAL A 271 SER A 274 -1 O VAL A 271 N GLN A 287 SHEET 1 AI 2 LEU A 259 LEU A 261 0 SHEET 2 AI 2 ILE A 443 ARG A 456 1 N THR A 450 O LEU A 260 SHEET 1 AJ 8 SER A 256 THR A 257 0 SHEET 2 AJ 8 HIS A 374 CYS A 378 -1 O SER A 375 N THR A 257 SHEET 3 AJ 8 GLU A 381 CYS A 385 1 O GLU A 381 N CYS A 378 SHEET 4 AJ 8 THR A 413 ILE A 420 1 O ARG A 419 N TYR A 384 SHEET 5 AJ 8 HIS A 330 SER A 334 -1 O CYS A 331 N LEU A 416 SHEET 6 AJ 8 ILE A 284 ARG A 298 -1 O GLU A 293 N SER A 334 SHEET 7 AJ 8 ILE A 443 ARG A 456 -1 O ILE A 443 N ARG A 298 SHEET 8 AJ 8 LEU A 259 LEU A 261 1 O LEU A 260 N THR A 450 SHEET 1 AK 2 ASN A 301 GLY A 312 0 SHEET 2 AK 2 ARG A 315 ILE A 323 -1 O ARG A 315 N GLY A 312 SHEET 1 CA 3 LEU C 494 THR C 499 0 SHEET 2 CA 3 TRP C 35 TYR C 40 -1 O TRP C 35 N THR C 499 SHEET 3 CA 3 ILE D 603 PRO D 609 -1 O CYS D 604 N VAL C 38 SHEET 1 CB 5 TRP C 45 GLU C 47 0 SHEET 2 CB 5 TYR C 486 ILE C 491 -1 O LYS C 490 N LYS C 46 SHEET 3 CB 5 PHE C 223 CYS C 228 -1 O ALA C 224 N VAL C 489 SHEET 4 CB 5 VAL C 242 VAL C 245 -1 O SER C 243 N LYS C 227 SHEET 5 CB 5 GLU C 83 VAL C 85 -1 O VAL C 84 N THR C 244 SHEET 1 CC 2 PHE C 53 ALA C 55 0 SHEET 2 CC 2 HIS C 216 CYS C 218 -1 O HIS C 216 N ALA C 55 SHEET 1 CD 2 GLU C 91 ASN C 94 0 SHEET 2 CD 2 LYS C 236 CYS C 239 -1 O GLY C 237 N PHE C 93 SHEET 1 CE 3 LEU C 129 ASN C 130 0 SHEET 2 CE 3 SER C 190 LEU C 193 -1 O TYR C 191 N LEU C 129 SHEET 3 CE 3 VAL C 181 PRO C 183 -1 O VAL C 182 N ARG C 192 SHEET 1 CF 2 LYS C 155 CYS C 157 0 SHEET 2 CF 2 ALA C 174 PHE C 176 -1 O ALA C 174 N CYS C 157 SHEET 1 CG 3 THR C 202 GLN C 203 0 SHEET 2 CG 3 MET C 434 TYR C 435 1 N TYR C 435 O THR C 202 SHEET 3 CG 3 ILE C 423 ILE C 424 -1 O ILE C 424 N MET C 434 SHEET 1 CH 2 LEU C 260 LEU C 261 0 SHEET 2 CH 2 CYS C 445 ARG C 456 1 N THR C 450 O LEU C 260 SHEET 1 CI 2 VAL C 271 ARG C 273 0 SHEET 2 CI 2 ILE C 284 CYS C 296 -1 O ILE C 285 N ARG C 273 SHEET 1 CJ 9 HIS C 374 CYS C 378 0 SHEET 2 CJ 9 GLU C 381 CYS C 385 -1 O GLU C 381 N CYS C 378 SHEET 3 CJ 9 THR C 413 LYS C 421 -1 O ARG C 419 N TYR C 384 SHEET 4 CJ 9 HIS C 330 SER C 334 -1 O CYS C 331 N LEU C 416 SHEET 5 CJ 9 ILE C 284 CYS C 296 -1 O ASN C 295 N ASN C 332 SHEET 6 CJ 9 CYS C 445 ARG C 456 -1 O CYS C 445 N CYS C 296 SHEET 7 CJ 9 THR C 465 PRO C 470 -1 O ARG C 469 N THR C 455 SHEET 8 CJ 9 THR C 358 PHE C 361 1 O THR C 358 N GLU C 466 SHEET 9 CJ 9 SER C 393 TRP C 395 -1 O SER C 393 N PHE C 361 SHEET 1 CK 6 HIS C 374 CYS C 378 0 SHEET 2 CK 6 GLU C 381 CYS C 385 -1 O GLU C 381 N CYS C 378 SHEET 3 CK 6 THR C 413 LYS C 421 -1 O ARG C 419 N TYR C 384 SHEET 4 CK 6 HIS C 330 SER C 334 -1 O CYS C 331 N LEU C 416 SHEET 5 CK 6 ILE C 284 CYS C 296 -1 O ASN C 295 N ASN C 332 SHEET 6 CK 6 VAL C 271 ARG C 273 -1 O VAL C 271 N GLN C 287 SHEET 1 CL 2 ASN C 301 HIS C 308 0 SHEET 2 CL 2 ALA C 316 ILE C 323 -1 O PHE C 317 N ILE C 307 SHEET 1 DA 3 VAL D 513 ILE D 515 0 SHEET 2 DA 3 ASN H 100K TYR H 100N-1 O TYR H 100M N GLY D 514 SHEET 3 DA 3 ARG H 100C LEU H 100D-1 O ARG H 100C N TYR H 100L SHEET 1 EA 3 LEU E 494 THR E 499 0 SHEET 2 EA 3 TRP E 35 TYR E 40 -1 O TRP E 35 N THR E 499 SHEET 3 EA 3 ILE F 603 PRO F 609 -1 O CYS F 604 N VAL E 38 SHEET 1 EB 5 TRP E 45 GLU E 47 0 SHEET 2 EB 5 TYR E 486 ILE E 491 -1 O LYS E 490 N LYS E 46 SHEET 3 EB 5 PHE E 223 CYS E 228 -1 O ALA E 224 N VAL E 489 SHEET 4 EB 5 VAL E 242 VAL E 245 -1 O SER E 243 N LYS E 227 SHEET 5 EB 5 VAL E 84 VAL E 85 -1 O VAL E 84 N THR E 244 SHEET 1 EC 2 PHE E 53 ALA E 55 0 SHEET 2 EC 2 HIS E 216 CYS E 218 -1 O HIS E 216 N ALA E 55 SHEET 1 ED 2 GLU E 91 ASN E 94 0 SHEET 2 ED 2 LYS E 236 CYS E 239 -1 O GLY E 237 N PHE E 93 SHEET 1 EE 4 VAL E 120 LYS E 121 0 SHEET 2 EE 4 VAL E 200 GLN E 203 -1 O GLN E 203 N VAL E 120 SHEET 3 EE 4 LYS E 432 TYR E 435 1 O ALA E 433 N THR E 202 SHEET 4 EE 4 ILE E 423 ILE E 424 -1 O ILE E 424 N MET E 434 SHEET 1 EF 3 LEU E 129 ASN E 130 0 SHEET 2 EF 3 SER E 190 LEU E 193 -1 O TYR E 191 N LEU E 129 SHEET 3 EF 3 VAL E 181 PRO E 183 -1 O VAL E 182 N ARG E 192 SHEET 1 EG 2 ILE E 154 THR E 162 0 SHEET 2 EG 2 VAL E 169 TYR E 177 -1 O GLN E 170 N ILE E 161 SHEET 1 EH 2 LEU E 259 LEU E 261 0 SHEET 2 EH 2 ILE E 443 ARG E 456 1 N THR E 450 O LEU E 260 SHEET 1 EI 2 VAL E 271 SER E 274 0 SHEET 2 EI 2 ILE E 284 ARG E 298 -1 O ILE E 285 N ARG E 273 SHEET 1 EJ 9 HIS E 374 ASN E 377 0 SHEET 2 EJ 9 PHE E 382 CYS E 385 1 O PHE E 383 N PHE E 376 SHEET 3 EJ 9 ILE E 414 ILE E 420 -1 O ARG E 419 N TYR E 384 SHEET 4 EJ 9 HIS E 330 ILE E 333 1 O CYS E 331 N LEU E 416 SHEET 5 EJ 9 ILE E 284 ARG E 298 1 O ASN E 295 N ASN E 332 SHEET 6 EJ 9 ILE E 443 ARG E 456 -1 O ILE E 443 N ARG E 298 SHEET 7 EJ 9 GLU E 466 ARG E 469 -1 O ARG E 469 N THR E 455 SHEET 8 EJ 9 ILE E 359 PHE E 361 1 O VAL E 360 N PHE E 468 SHEET 9 EJ 9 THR E 394 TRP E 395 -1 O TRP E 395 N ILE E 359 SHEET 1 EK 6 HIS E 374 ASN E 377 0 SHEET 2 EK 6 PHE E 382 CYS E 385 1 O PHE E 383 N PHE E 376 SHEET 3 EK 6 ILE E 414 ILE E 420 -1 O ARG E 419 N TYR E 384 SHEET 4 EK 6 HIS E 330 ILE E 333 1 O CYS E 331 N LEU E 416 SHEET 5 EK 6 ILE E 284 ARG E 298 1 O ASN E 295 N ASN E 332 SHEET 6 EK 6 VAL E 271 SER E 274 -1 O VAL E 271 N GLN E 287 SHEET 1 EL 2 ASN E 302 GLY E 312 0 SHEET 2 EL 2 ARG E 315 ILE E 322 -1 O ARG E 315 N ILE E 309 SHEET 1 FA 2 VAL F 513 ILE F 515 0 SHEET 2 FA 2 TYR M 100L TYR M 100N-1 O TYR M 100M N GLY F 514 SHEET 1 HA 4 GLN H 3 SER H 7 0 SHEET 2 HA 4 VAL H 18 SER H 25 -1 O SER H 21 N SER H 7 SHEET 3 HA 4 THR H 77 MET H 82 -1 O LEU H 78 N CYS H 22 SHEET 4 HA 4 PHE H 67 ASP H 72 -1 O LEU H 68 N GLU H 81 SHEET 1 HB 4 GLY H 10 VAL H 12 0 SHEET 2 HB 4 THR H 107 VAL H 111 -1 O THR H 108 N GLY H 10 SHEET 3 HB 4 ALA H 88 MET H 95 -1 O ALA H 88 N VAL H 109 SHEET 4 HB 4 MET H 100R TRP H 103 -1 N ASP H 101 O ARG H 94 SHEET 1 HC 6 GLY H 10 VAL H 12 0 SHEET 2 HC 6 THR H 107 VAL H 111 -1 O THR H 108 N GLY H 10 SHEET 3 HC 6 ALA H 88 MET H 95 -1 O ALA H 88 N VAL H 109 SHEET 4 HC 6 MET H 34 GLN H 39 -1 O TYR H 35 N ALA H 93 SHEET 5 HC 6 LEU H 45 ILE H 51 -1 O GLU H 46 N ARG H 38 SHEET 6 HC 6 VAL H 57 TYR H 59 -1 O VAL H 58 N ALA H 50 SHEET 1 HD 2 MET H 100R TRP H 103 0 SHEET 2 HD 2 ALA H 88 MET H 95 -1 O ARG H 94 N ASP H 101 SHEET 1 LA 4 MET L 4 GLN L 6 0 SHEET 2 LA 4 ALA L 19 SER L 25 -1 O LYS L 24 N THR L 5 SHEET 3 LA 4 ASP L 70 ILE L 75 -1 O PHE L 71 N CYS L 23 SHEET 4 LA 4 PHE L 62 SER L 67 -1 O VAL L 63 N ARG L 74 SHEET 1 LB 4 SER L 10 VAL L 13 0 SHEET 2 LB 4 THR L 102 LEU L 106 1 O LYS L 103 N LEU L 11 SHEET 3 LB 4 GLY L 84 GLN L 90 -1 O GLY L 84 N VAL L 104 SHEET 4 LB 4 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90 SHEET 1 LC 6 SER L 10 VAL L 13 0 SHEET 2 LC 6 THR L 102 LEU L 106 1 O LYS L 103 N LEU L 11 SHEET 3 LC 6 GLY L 84 GLN L 90 -1 O GLY L 84 N VAL L 104 SHEET 4 LC 6 LEU L 33 GLN L 38 -1 O TYR L 34 N MET L 89 SHEET 5 LC 6 GLN L 45 GLU L 50 -1 O GLN L 45 N ARG L 37 SHEET 6 LC 6 ASN L 53 ARG L 54 -1 O ASN L 53 N PHE L 49 SHEET 1 LD 2 THR L 97 PHE L 98 0 SHEET 2 LD 2 GLY L 84 GLN L 90 -1 O GLN L 90 N THR L 97 SHEET 1 MA 4 LEU M 4 SER M 7 0 SHEET 2 MA 4 VAL M 18 VAL M 24 -1 O SER M 21 N SER M 7 SHEET 3 MA 4 THR M 77 MET M 82 -1 O LEU M 78 N CYS M 22 SHEET 4 MA 4 PHE M 67 ASP M 72 -1 O LEU M 68 N GLU M 81 SHEET 1 MB 4 GLY M 10 VAL M 12 0 SHEET 2 MB 4 THR M 107 VAL M 111 -1 O THR M 108 N GLY M 10 SHEET 3 MB 4 ALA M 88 MET M 95 -1 O ALA M 88 N VAL M 109 SHEET 4 MB 4 MET M 100R TRP M 103 -1 N ASP M 101 O ARG M 94 SHEET 1 MC 6 GLY M 10 VAL M 12 0 SHEET 2 MC 6 THR M 107 VAL M 111 -1 O THR M 108 N GLY M 10 SHEET 3 MC 6 ALA M 88 MET M 95 -1 O ALA M 88 N VAL M 109 SHEET 4 MC 6 MET M 34 GLN M 39 -1 O TYR M 35 N ALA M 93 SHEET 5 MC 6 LEU M 45 ILE M 51 -1 O GLU M 46 N ARG M 38 SHEET 6 MC 6 VAL M 57 TYR M 59 -1 O VAL M 58 N ALA M 50 SHEET 1 MD 2 MET M 100R TRP M 103 0 SHEET 2 MD 2 ALA M 88 MET M 95 -1 O ARG M 94 N ASP M 101 SHEET 1 NA 4 MET N 4 THR N 7 0 SHEET 2 NA 4 ALA N 19 SER N 25 -1 O SER N 22 N THR N 7 SHEET 3 NA 4 ASP N 70 ILE N 75 -1 O PHE N 71 N CYS N 23 SHEET 4 NA 4 PHE N 62 GLY N 66 -1 O VAL N 63 N ARG N 74 SHEET 1 NB 4 SER N 10 SER N 12 0 SHEET 2 NB 4 THR N 102 ASP N 105 1 O LYS N 103 N LEU N 11 SHEET 3 NB 4 GLY N 84 GLN N 90 -1 O GLY N 84 N VAL N 104 SHEET 4 NB 4 THR N 97 PHE N 98 -1 O THR N 97 N GLN N 90 SHEET 1 NC 6 SER N 10 SER N 12 0 SHEET 2 NC 6 THR N 102 ASP N 105 1 O LYS N 103 N LEU N 11 SHEET 3 NC 6 GLY N 84 GLN N 90 -1 O GLY N 84 N VAL N 104 SHEET 4 NC 6 LEU N 33 GLN N 38 -1 O TYR N 34 N MET N 89 SHEET 5 NC 6 GLN N 45 PHE N 49 -1 O GLN N 45 N ARG N 37 SHEET 6 NC 6 ASN N 53 ARG N 54 -1 O ASN N 53 N PHE N 49 SHEET 1 ND 2 THR N 97 PHE N 98 0 SHEET 2 ND 2 GLY N 84 GLN N 90 -1 O GLN N 90 N THR N 97 SHEET 1 NE 2 ARG N 27C GLN N 27D 0 SHEET 2 NE 2 LYS N 30 THR N 31 -1 O LYS N 30 N GLN N 27D SSBOND 1 CYS A 54 CYS A 74 1555 1555 2.02 SSBOND 2 CYS A 119 CYS A 205 1555 1555 2.03 SSBOND 3 CYS A 126 CYS A 196 1555 1555 2.03 SSBOND 4 CYS A 131 CYS A 157 1555 1555 2.02 SSBOND 5 CYS A 218 CYS A 247 1555 1555 2.03 SSBOND 6 CYS A 228 CYS A 239 1555 1555 2.03 SSBOND 7 CYS A 296 CYS A 331 1555 1555 2.03 SSBOND 8 CYS A 378 CYS A 445 1555 1555 2.02 SSBOND 9 CYS A 385 CYS A 418 1555 1555 2.02 SSBOND 10 CYS B 598 CYS B 604 1555 1555 2.03 SSBOND 11 CYS C 54 CYS C 74 1555 1555 2.03 SSBOND 12 CYS C 119 CYS C 205 1555 1555 2.03 SSBOND 13 CYS C 126 CYS C 196 1555 1555 2.03 SSBOND 14 CYS C 131 CYS C 157 1555 1555 2.02 SSBOND 15 CYS C 218 CYS C 247 1555 1555 2.03 SSBOND 16 CYS C 228 CYS C 239 1555 1555 2.03 SSBOND 17 CYS C 296 CYS C 331 1555 1555 2.03 SSBOND 18 CYS C 378 CYS C 445 1555 1555 2.03 SSBOND 19 CYS C 385 CYS C 418 1555 1555 2.03 SSBOND 20 CYS D 598 CYS D 604 1555 1555 2.02 SSBOND 21 CYS E 54 CYS E 74 1555 1555 2.03 SSBOND 22 CYS E 119 CYS E 205 1555 1555 2.03 SSBOND 23 CYS E 126 CYS E 196 1555 1555 2.02 SSBOND 24 CYS E 131 CYS E 157 1555 1555 2.03 SSBOND 25 CYS E 218 CYS E 247 1555 1555 2.03 SSBOND 26 CYS E 228 CYS E 239 1555 1555 2.03 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 2.02 SSBOND 30 CYS F 598 CYS F 604 1555 1555 2.03 SSBOND 31 CYS H 22 CYS H 92 1555 1555 2.03 SSBOND 32 CYS L 23 CYS L 88 1555 1555 2.03 SSBOND 33 CYS M 22 CYS M 92 1555 1555 2.03 SSBOND 34 CYS N 23 CYS N 88 1555 1555 2.03 LINK ND2 ASN A 88 C1 NAG G 1 1555 1555 1.45 LINK ND2 ASN A 135 C1 NAG A1135 1555 1555 1.44 LINK ND2 ASN A 156 C1 NAG I 1 1555 1555 1.38 LINK ND2 ASN A 160 C1 NAG J 1 1555 1555 1.45 LINK ND2 ASN A 241 C1 NAG K 1 1555 1555 1.44 LINK ND2 ASN A 262 C1 NAG O 1 1555 1555 1.36 LINK ND2 ASN A 276 C1 NAG P 1 1555 1555 1.40 LINK ND2 ASN A 295 C1 NAG Q 1 1555 1555 1.42 LINK ND2 ASN A 301 C1 NAG R 1 1555 1555 1.43 LINK ND2 ASN A 332 C1 NAG S 1 1555 1555 1.43 LINK ND2 ASN A 339 C1 NAG T 1 1555 1555 1.40 LINK ND2 ASN A 355 C1 NAG A1355 1555 1555 1.39 LINK ND2 ASN A 362 C1 NAG U 1 1555 1555 1.39 LINK ND2 ASN A 386 C1 NAG V 1 1555 1555 1.42 LINK ND2 ASN A 392 C1 NAG W 1 1555 1555 1.45 LINK ND2 ASN A 397 C1 NAG A1397 1555 1555 1.42 LINK ND2 ASN A 448 C1 NAG X 1 1555 1555 1.43 LINK ND2 ASN B 611 C1 NAG Y 1 1555 1555 1.43 LINK ND2 ASN B 616 C1 NAG B1600 1555 1555 1.47 LINK ND2 ASN B 625 C1 NAG B1625 1555 1555 1.42 LINK ND2 ASN B 637 C1 NAG Z 1 1555 1555 1.44 LINK ND2 ASN C 88 C1 NAG a 1 1555 1555 1.51 LINK ND2 ASN C 135 C1 NAG b 1 1555 1555 1.41 LINK ND2 ASN C 156 C1 NAG c 1 1555 1555 1.55 LINK ND2 ASN C 160 C1 NAG d 1 1555 1555 1.42 LINK ND2 ASN C 241 C1 NAG e 1 1555 1555 1.46 LINK ND2 ASN C 262 C1 NAG f 1 1555 1555 1.43 LINK ND2 ASN C 276 C1 NAG g 1 1555 1555 1.43 LINK ND2 ASN C 295 C1 NAG h 1 1555 1555 1.41 LINK ND2 ASN C 301 C1 NAG i 1 1555 1555 1.51 LINK ND2 ASN C 332 C1 NAG j 1 1555 1555 1.41 LINK ND2 ASN C 339 C1 NAG k 1 1555 1555 1.43 LINK ND2 ASN C 355 C1 NAG l 1 1555 1555 1.43 LINK ND2 ASN C 362 C1 NAG m 1 1555 1555 1.44 LINK ND2 ASN C 386 C1 NAG n 1 1555 1555 1.38 LINK ND2 ASN C 392 C1 NAG o 1 1555 1555 1.45 LINK ND2 ASN C 397 C1 NAG C1397 1555 1555 1.41 LINK ND2 ASN C 448 C1 NAG p 1 1555 1555 1.44 LINK ND2 ASN D 611 C1 NAG q 1 1555 1555 1.43 LINK ND2 ASN D 616 C1 NAG D1600 1555 1555 1.41 LINK ND2 ASN D 625 C1 NAG r 1 1555 1555 1.43 LINK ND2 ASN D 637 C1 NAG s 1 1555 1555 1.43 LINK ND2 ASN E 88 C1 NAG t 1 1555 1555 1.48 LINK ND2 ASN E 135 C1 NAG u 1 1555 1555 1.49 LINK ND2 ASN E 156 C1 NAG v 1 1555 1555 1.40 LINK ND2 ASN E 160 C1 NAG w 1 1555 1555 1.38 LINK ND2 ASN E 187 C1 NAG E1187 1555 1555 1.45 LINK ND2 ASN E 241 C1 NAG x 1 1555 1555 1.35 LINK ND2 ASN E 262 C1 NAG y 1 1555 1555 1.41 LINK ND2 ASN E 276 C1 NAG z 1 1555 1555 1.32 LINK ND2 ASN E 295 C1 NAG 0 1 1555 1555 1.43 LINK ND2 ASN E 301 C1 NAG 1 1 1555 1555 1.47 LINK ND2 ASN E 332 C1 NAG 2 1 1555 1555 1.45 LINK ND2 ASN E 339 C1 NAG 3 1 1555 1555 1.39 LINK ND2 ASN E 355 C1 NAG 4 1 1555 1555 1.42 LINK ND2 ASN E 362 C1 NAG 5 1 1555 1555 1.50 LINK ND2 ASN E 386 C1 NAG 6 1 1555 1555 1.43 LINK ND2 ASN E 392 C1 NAG 7 1 1555 1555 1.44 LINK ND2 ASN E 397 C1 NAG E1397 1555 1555 1.42 LINK ND2 ASN E 448 C1 NAG 8 1 1555 1555 1.46 LINK ND2 ASN F 611 C1 NAG 9 1 1555 1555 1.44 LINK ND2 ASN F 616 C1 NAG F1600 1555 1555 1.41 LINK ND2 ASN F 625 C1 NAGAA 1 1555 1555 1.45 LINK ND2 ASN F 637 C1 NAGBA 1 1555 1555 1.37 LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.39 LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.39 LINK O4 NAG I 2 C1 BMA I 3 1555 1555 1.41 LINK O4 NAG J 1 C1 NAG J 2 1555 1555 1.39 LINK O4 NAG J 2 C1 BMA J 3 1555 1555 1.41 LINK O4 NAG K 1 C1 NAG K 2 1555 1555 1.39 LINK O4 NAG K 2 C1 BMA K 3 1555 1555 1.40 LINK O4 NAG O 1 C1 NAG O 2 1555 1555 1.44 LINK O4 NAG O 2 C1 BMA O 3 1555 1555 1.44 LINK O3 BMA O 3 C1 MAN O 4 1555 1555 1.44 LINK O6 BMA O 3 C1 MAN O 6 1555 1555 1.44 LINK O2 MAN O 4 C1 MAN O 5 1555 1555 1.44 LINK O3 MAN O 6 C1 MAN O 7 1555 1555 1.39 LINK O4 NAG P 1 C1 NAG P 2 1555 1555 1.39 LINK O4 NAG P 2 C1 BMA P 3 1555 1555 1.41 LINK O4 NAG Q 1 C1 NAG Q 2 1555 1555 1.39 LINK O4 NAG R 1 C1 NAG R 2 1555 1555 1.39 LINK O4 NAG S 1 C1 NAG S 2 1555 1555 1.39 LINK O4 NAG S 2 C1 BMA S 3 1555 1555 1.41 LINK O4 NAG T 1 C1 NAG T 2 1555 1555 1.39 LINK O4 NAG U 1 C1 NAG U 2 1555 1555 1.39 LINK O4 NAG U 2 C1 BMA U 3 1555 1555 1.41 LINK O4 NAG V 1 C1 NAG V 2 1555 1555 1.39 LINK O4 NAG V 2 C1 BMA V 3 1555 1555 1.41 LINK O4 NAG W 1 C1 NAG W 2 1555 1555 1.39 LINK O4 NAG W 2 C1 BMA W 3 1555 1555 1.41 LINK O4 NAG X 1 C1 NAG X 2 1555 1555 1.39 LINK O4 NAG Y 1 C1 NAG Y 2 1555 1555 1.47 LINK O6 NAG Y 1 C1 FUC Y 11 1555 1555 1.48 LINK O4 NAG Y 2 C1 BMA Y 3 1555 1555 1.47 LINK O6 BMA Y 3 C1 MAN Y 4 1555 1555 1.46 LINK O3 BMA Y 3 C1 MAN Y 9 1555 1555 1.47 LINK O2 MAN Y 4 C1 NAG Y 5 1555 1555 1.47 LINK O6 MAN Y 4 C1 NAG Y 7 1555 1555 1.47 LINK O4 NAG Y 5 C1 GAL Y 6 1555 1555 1.47 LINK O4 NAG Y 7 C1 GAL Y 8 1555 1555 1.47 LINK O2 MAN Y 9 C1 NAG Y 10 1555 1555 1.47 LINK O4 NAG Z 1 C1 NAG Z 2 1555 1555 1.47 LINK O6 NAG Z 1 C1 FUC Z 13 1555 1555 1.48 LINK O4 NAG Z 2 C1 BMA Z 3 1555 1555 1.47 LINK O3 BMA Z 3 C1 MAN Z 4 1555 1555 1.47 LINK O6 BMA Z 3 C1 MAN Z 9 1555 1555 1.46 LINK O2 MAN Z 4 C1 NAG Z 5 1555 1555 1.47 LINK O4 MAN Z 4 C1 NAG Z 7 1555 1555 1.47 LINK O4 NAG Z 5 C1 GAL Z 6 1555 1555 1.47 LINK O4 NAG Z 7 C1 GAL Z 8 1555 1555 1.47 LINK O2 MAN Z 9 C1 NAG Z 10 1555 1555 1.47 LINK O6 MAN Z 9 C1 NAG Z 12 1555 1555 1.47 LINK O4 NAG Z 10 C1 GAL Z 11 1555 1555 1.47 LINK O4 NAG a 1 C1 NAG a 2 1555 1555 1.39 LINK O4 NAG a 2 C1 BMA a 3 1555 1555 1.41 LINK O4 NAG b 1 C1 NAG b 2 1555 1555 1.39 LINK O4 NAG c 1 C1 NAG c 2 1555 1555 1.39 LINK O4 NAG d 1 C1 NAG d 2 1555 1555 1.39 LINK O4 NAG d 2 C1 BMA d 3 1555 1555 1.41 LINK O4 NAG e 1 C1 NAG e 2 1555 1555 1.39 LINK O4 NAG e 2 C1 BMA e 3 1555 1555 1.40 LINK O3 BMA e 3 C1 MAN e 4 1555 1555 1.40 LINK O6 BMA e 3 C1 MAN e 5 1555 1555 1.40 LINK O4 NAG f 1 C1 NAG f 2 1555 1555 1.44 LINK O4 NAG f 2 C1 BMA f 3 1555 1555 1.44 LINK O3 BMA f 3 C1 MAN f 4 1555 1555 1.44 LINK O6 BMA f 3 C1 MAN f 6 1555 1555 1.44 LINK O2 MAN f 4 C1 MAN f 5 1555 1555 1.44 LINK O3 MAN f 6 C1 MAN f 7 1555 1555 1.39 LINK O4 NAG g 1 C1 NAG g 2 1555 1555 1.39 LINK O4 NAG g 2 C1 BMA g 3 1555 1555 1.41 LINK O4 NAG h 1 C1 NAG h 2 1555 1555 1.39 LINK O4 NAG i 1 C1 NAG i 2 1555 1555 1.39 LINK O4 NAG i 2 C1 BMA i 3 1555 1555 1.41 LINK O4 NAG j 1 C1 NAG j 2 1555 1555 1.39 LINK O4 NAG j 2 C1 BMA j 3 1555 1555 1.41 LINK O4 NAG k 1 C1 NAG k 2 1555 1555 1.39 LINK O4 NAG l 1 C1 NAG l 2 1555 1555 1.39 LINK O4 NAG m 1 C1 NAG m 2 1555 1555 1.39 LINK O4 NAG m 2 C1 BMA m 3 1555 1555 1.41 LINK O4 NAG n 1 C1 NAG n 2 1555 1555 1.39 LINK O4 NAG n 2 C1 BMA n 3 1555 1555 1.41 LINK O4 NAG o 1 C1 NAG o 2 1555 1555 1.39 LINK O4 NAG p 1 C1 NAG p 2 1555 1555 1.39 LINK O4 NAG p 2 C1 BMA p 3 1555 1555 1.41 LINK O3 BMA p 3 C1 MAN p 4 1555 1555 1.40 LINK O6 BMA p 3 C1 MAN p 6 1555 1555 1.41 LINK O2 MAN p 4 C1 MAN p 5 1555 1555 1.41 LINK O3 MAN p 6 C1 MAN p 7 1555 1555 1.41 LINK O6 MAN p 6 C1 MAN p 8 1555 1555 1.40 LINK O4 NAG q 1 C1 NAG q 2 1555 1555 1.47 LINK O6 NAG q 1 C1 FUC q 3 1555 1555 1.48 LINK O4 NAG r 1 C1 NAG r 2 1555 1555 1.39 LINK O4 NAG s 1 C1 NAG s 2 1555 1555 1.47 LINK O4 NAG t 1 C1 NAG t 2 1555 1555 1.39 LINK O4 NAG t 2 C1 BMA t 3 1555 1555 1.41 LINK O4 NAG u 1 C1 NAG u 2 1555 1555 1.39 LINK O4 NAG v 1 C1 NAG v 2 1555 1555 1.39 LINK O4 NAG v 2 C1 BMA v 3 1555 1555 1.41 LINK O4 NAG w 1 C1 NAG w 2 1555 1555 1.39 LINK O4 NAG x 1 C1 NAG x 2 1555 1555 1.39 LINK O4 NAG x 2 C1 BMA x 3 1555 1555 1.40 LINK O3 BMA x 3 C1 MAN x 4 1555 1555 1.41 LINK O6 BMA x 3 C1 MAN x 6 1555 1555 1.40 LINK O2 MAN x 4 C1 MAN x 5 1555 1555 1.41 LINK O4 NAG y 1 C1 NAG y 2 1555 1555 1.44 LINK O4 NAG y 2 C1 BMA y 3 1555 1555 1.44 LINK O3 BMA y 3 C1 MAN y 4 1555 1555 1.44 LINK O6 BMA y 3 C1 MAN y 6 1555 1555 1.44 LINK O2 MAN y 4 C1 MAN y 5 1555 1555 1.44 LINK O3 MAN y 6 C1 MAN y 7 1555 1555 1.39 LINK O4 NAG z 1 C1 NAG z 2 1555 1555 1.39 LINK O4 NAG 0 1 C1 NAG 0 2 1555 1555 1.39 LINK O4 NAG 1 1 C1 NAG 1 2 1555 1555 1.39 LINK O4 NAG 2 1 C1 NAG 2 2 1555 1555 1.39 LINK O4 NAG 2 2 C1 BMA 2 3 1555 1555 1.41 LINK O4 NAG 3 1 C1 NAG 3 2 1555 1555 1.39 LINK O4 NAG 4 1 C1 NAG 4 2 1555 1555 1.39 LINK O4 NAG 5 1 C1 NAG 5 2 1555 1555 1.39 LINK O4 NAG 6 1 C1 NAG 6 2 1555 1555 1.39 LINK O4 NAG 6 2 C1 BMA 6 3 1555 1555 1.41 LINK O6 BMA 6 3 C1 MAN 6 4 1555 1555 1.40 LINK O4 NAG 7 1 C1 NAG 7 2 1555 1555 1.39 LINK O4 NAG 7 2 C1 BMA 7 3 1555 1555 1.41 LINK O4 NAG 8 1 C1 NAG 8 2 1555 1555 1.39 LINK O4 NAG 8 2 C1 BMA 8 3 1555 1555 1.41 LINK O3 BMA 8 3 C1 MAN 8 4 1555 1555 1.40 LINK O6 BMA 8 3 C1 MAN 8 6 1555 1555 1.41 LINK O2 MAN 8 4 C1 MAN 8 5 1555 1555 1.41 LINK O3 MAN 8 6 C1 MAN 8 7 1555 1555 1.41 LINK O6 MAN 8 6 C1 MAN 8 8 1555 1555 1.31 LINK O4 NAG 9 1 C1 NAG 9 2 1555 1555 1.47 LINK O6 NAG 9 1 C1 FUC 9 11 1555 1555 1.48 LINK O4 NAG 9 2 C1 BMA 9 3 1555 1555 1.47 LINK O6 BMA 9 3 C1 MAN 9 4 1555 1555 1.46 LINK O3 BMA 9 3 C1 MAN 9 9 1555 1555 1.47 LINK O2 MAN 9 4 C1 NAG 9 5 1555 1555 1.47 LINK O6 MAN 9 4 C1 NAG 9 7 1555 1555 1.47 LINK O4 NAG 9 5 C1 GAL 9 6 1555 1555 1.47 LINK O4 NAG 9 7 C1 GAL 9 8 1555 1555 1.47 LINK O2 MAN 9 9 C1 NAG 9 10 1555 1555 1.47 LINK O4 NAGAA 1 C1 NAGAA 2 1555 1555 1.39 LINK O4 NAGBA 1 C1 NAGBA 2 1555 1555 1.47 LINK O6 NAGBA 1 C1 FUCBA 12 1555 1555 1.48 LINK O4 NAGBA 2 C1 BMABA 3 1555 1555 1.47 LINK O3 BMABA 3 C1 MANBA 4 1555 1555 1.46 LINK O6 BMABA 3 C1 MANBA 9 1555 1555 1.46 LINK O2 MANBA 4 C1 NAGBA 5 1555 1555 1.47 LINK O4 MANBA 4 C1 NAGBA 7 1555 1555 1.47 LINK O4 NAGBA 5 C1 GALBA 6 1555 1555 1.47 LINK O4 NAGBA 7 C1 GALBA 8 1555 1555 1.47 LINK O2 MANBA 9 C1 NAGBA 10 1555 1555 1.47 LINK O6 MANBA 9 C1 NAGBA 11 1555 1555 1.47 CISPEP 1 THR A 499 LYS A 500 0 14.53 CISPEP 2 GLN A 507 ARG A 508 0 0.70 CISPEP 3 GLY B 600 LYS B 601 0 -13.03 CISPEP 4 HIS C 66 ASN C 67 0 0.91 CISPEP 5 VAL C 68 TRP C 69 0 -2.30 CISPEP 6 VAL D 518 PHE D 519 0 -2.07 CISPEP 7 SER D 528 THR D 529 0 21.91 CISPEP 8 GLY D 600 LYS D 601 0 -16.21 CISPEP 9 VAL E 65 HIS E 66 0 -0.91 CISPEP 10 HIS E 66 ASN E 67 0 -22.24 CISPEP 11 ASP E 78 PRO E 79 0 -19.26 CISPEP 12 THR E 123 PRO E 124 0 1.24 CISPEP 13 VAL E 134 ASN E 135 0 -0.23 CISPEP 14 CYS E 157 SER E 158 0 26.62 CISPEP 15 ASN E 355 LYS E 357 0 -8.51 CISPEP 16 VAL F 518 PHE F 519 0 -10.04 CISPEP 17 GLN F 552 ASN F 553 0 7.74 CISPEP 18 GLY F 600 LYS F 601 0 -17.47 CISPEP 19 ARG H 1 VAL H 2 0 25.56 CISPEP 20 PHE L 94 PRO L 95 0 -1.28 CISPEP 21 THR N 7 PRO N 8 0 -2.26 CISPEP 22 PHE N 94 PRO N 95 0 -0.96 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