HEADER VIRAL PROTEIN/IMMUNE SYSTEM 16-APR-25 9O8S TITLE CRYO-EM STRUCTURE OF NI04359_D30_240 FAB IN COMPLEX WITH INFLUENZA TITLE 2 VIRUS HEMAGGLUTININ FROM A/HONG KONG/485197/2014 (H3N2) COMPND MOL_ID: 1; COMPND 2 MOLECULE: HEMAGGLUTININ HA1; COMPND 3 CHAIN: A, C, D; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: HEMAGGLUTININ HA2; COMPND 7 CHAIN: B, E, F; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: NI04359_D30_240 FAB HEAVY CHAIN; COMPND 11 CHAIN: H, G, I; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 4; COMPND 14 MOLECULE: NI04359_D30_240 FAB LIGHT CHAIN; COMPND 15 CHAIN: L, J, K; COMPND 16 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS (A/HONG SOURCE 3 KONG/485197/2014(H3N2)); SOURCE 4 ORGANISM_TAXID: 1679038; SOURCE 5 GENE: HA; SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS (A/HONG SOURCE 10 KONG/485197/2014(H3N2)); SOURCE 11 ORGANISM_TAXID: 1679038; SOURCE 12 GENE: HA; SOURCE 13 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 15 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 17 ORGANISM_TAXID: 9606; SOURCE 18 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 19 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 20 MOL_ID: 4; SOURCE 21 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 22 ORGANISM_TAXID: 9606; SOURCE 23 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 24 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS INFLUENZA, HEMAGGLUTININ, ANTIBODY COMPLEX, VIRAL PROTEIN, VIRAL KEYWDS 2 PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR G.JO,A.B.WARD REVDAT 1 04-FEB-26 9O8S 0 JRNL AUTH G.JO,A.B.WARD JRNL TITL A SINGLE AMINO ACID SUBSTITUTION IN HEMAGGLUTININ STALK JRNL TITL 2 DRIVES HETEROSUBTYPIC IMPRINTING OF CROSS-GROUP REACTIVE B JRNL TITL 3 CELLS IN CHILDREN JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.65 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : CRYOSPARC, EPU, CRYOSPARC, PHENIX, REMARK 3 CRYOSPARC, CRYOSPARC, CRYOSPARC 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) : 2.650 REMARK 3 NUMBER OF PARTICLES : 196828 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 9O8S COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-APR-25. REMARK 100 THE DEPOSITION ID IS D_1000294517. 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 : CRYO-EM STRUCTURE OF REMARK 245 NI04359_D30_240 FAB IN COMPLEX REMARK 245 WITH INFLUENZA VIRUS REMARK 245 HEMAGGLUTININ FROM A/HONG KONG/ REMARK 245 485197/2014 (H3N2) REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 0.80 REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.40 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : 2516 REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : TFS GLACIOS REMARK 245 DETECTOR TYPE : TFS FALCON 4I (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 600.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 1400.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : 2.70 REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 4509.00 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : 190000 REMARK 245 CALIBRATED MAGNIFICATION : NULL REMARK 245 SOURCE : FIELD EMISSION GUN REMARK 245 ACCELERATION VOLTAGE (KV) : 200 REMARK 245 IMAGING DETAILS : NULL REMARK 247 REMARK 247 ELECTRON MICROSCOPY REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION REMARK 247 OF THE STRUCTURE FACTORS. REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 12-MERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: 12-MERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, H, L, C, E, G, J, D, F, REMARK 350 AND CHAINS: I, K, M, N, O, P, Q, R, S, REMARK 350 AND CHAINS: T, U, V, W, X, Y, Z, a 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 -15 REMARK 465 LYS A -14 REMARK 465 THR A -13 REMARK 465 ILE A -12 REMARK 465 ILE A -11 REMARK 465 ALA A -10 REMARK 465 LEU A -9 REMARK 465 SER A -8 REMARK 465 TYR A -7 REMARK 465 ILE A -6 REMARK 465 LEU A -5 REMARK 465 CYS A -4 REMARK 465 LEU A -3 REMARK 465 VAL A -2 REMARK 465 PHE A -1 REMARK 465 ALA A 0 REMARK 465 GLN A 1 REMARK 465 LYS A 2 REMARK 465 ILE A 3 REMARK 465 PRO A 4 REMARK 465 GLY A 5 REMARK 465 ASN A 6 REMARK 465 ASP A 7 REMARK 465 ASN A 8 REMARK 465 SER A 9 REMARK 465 LYS A 326 REMARK 465 GLN A 327 REMARK 465 THR A 328 REMARK 465 ARG A 329 REMARK 465 ILE B 173 REMARK 465 LYS B 174 REMARK 465 GLY B 175 REMARK 465 VAL B 176 REMARK 465 GLY B 177 REMARK 465 TYR B 178 REMARK 465 ILE B 179 REMARK 465 PRO B 180 REMARK 465 GLU B 181 REMARK 465 ALA B 182 REMARK 465 PRO B 183 REMARK 465 ARG B 184 REMARK 465 ASP B 185 REMARK 465 GLY B 186 REMARK 465 GLN B 187 REMARK 465 ALA B 188 REMARK 465 TYR B 189 REMARK 465 VAL B 190 REMARK 465 ARG B 191 REMARK 465 LYS B 192 REMARK 465 ASP B 193 REMARK 465 GLY B 194 REMARK 465 GLU B 195 REMARK 465 TRP B 196 REMARK 465 VAL B 197 REMARK 465 LEU B 198 REMARK 465 LEU B 199 REMARK 465 SER B 200 REMARK 465 THR B 201 REMARK 465 PHE B 202 REMARK 465 LEU B 203 REMARK 465 GLY B 204 REMARK 465 SER B 205 REMARK 465 GLU B 206 REMARK 465 ASN B 207 REMARK 465 LEU B 208 REMARK 465 TYR B 209 REMARK 465 PHE B 210 REMARK 465 GLN B 211 REMARK 465 GLY B 212 REMARK 465 SER B 213 REMARK 465 ALA B 214 REMARK 465 TRP B 215 REMARK 465 SER B 216 REMARK 465 HIS B 217 REMARK 465 PRO B 218 REMARK 465 GLN B 219 REMARK 465 PHE B 220 REMARK 465 GLU B 221 REMARK 465 LYS B 222 REMARK 465 GLY B 223 REMARK 465 GLY B 224 REMARK 465 GLY B 225 REMARK 465 SER B 226 REMARK 465 GLY B 227 REMARK 465 GLY B 228 REMARK 465 GLY B 229 REMARK 465 SER B 230 REMARK 465 HIS B 231 REMARK 465 HIS B 232 REMARK 465 HIS B 233 REMARK 465 HIS B 234 REMARK 465 HIS B 235 REMARK 465 HIS B 236 REMARK 465 SER H 112 REMARK 465 SER H 113 REMARK 465 ILE L 106 REMARK 465 LYS L 107 REMARK 465 MET C -15 REMARK 465 LYS C -14 REMARK 465 THR C -13 REMARK 465 ILE C -12 REMARK 465 ILE C -11 REMARK 465 ALA C -10 REMARK 465 LEU C -9 REMARK 465 SER C -8 REMARK 465 TYR C -7 REMARK 465 ILE C -6 REMARK 465 LEU C -5 REMARK 465 CYS C -4 REMARK 465 LEU C -3 REMARK 465 VAL C -2 REMARK 465 PHE C -1 REMARK 465 ALA C 0 REMARK 465 GLN C 1 REMARK 465 LYS C 2 REMARK 465 ILE C 3 REMARK 465 PRO C 4 REMARK 465 GLY C 5 REMARK 465 ASN C 6 REMARK 465 ASP C 7 REMARK 465 ASN C 8 REMARK 465 SER C 9 REMARK 465 LYS C 326 REMARK 465 GLN C 327 REMARK 465 THR C 328 REMARK 465 ARG C 329 REMARK 465 ILE E 173 REMARK 465 LYS E 174 REMARK 465 GLY E 175 REMARK 465 VAL E 176 REMARK 465 GLY E 177 REMARK 465 TYR E 178 REMARK 465 ILE E 179 REMARK 465 PRO E 180 REMARK 465 GLU E 181 REMARK 465 ALA E 182 REMARK 465 PRO E 183 REMARK 465 ARG E 184 REMARK 465 ASP E 185 REMARK 465 GLY E 186 REMARK 465 GLN E 187 REMARK 465 ALA E 188 REMARK 465 TYR E 189 REMARK 465 VAL E 190 REMARK 465 ARG E 191 REMARK 465 LYS E 192 REMARK 465 ASP E 193 REMARK 465 GLY E 194 REMARK 465 GLU E 195 REMARK 465 TRP E 196 REMARK 465 VAL E 197 REMARK 465 LEU E 198 REMARK 465 LEU E 199 REMARK 465 SER E 200 REMARK 465 THR E 201 REMARK 465 PHE E 202 REMARK 465 LEU E 203 REMARK 465 GLY E 204 REMARK 465 SER E 205 REMARK 465 GLU E 206 REMARK 465 ASN E 207 REMARK 465 LEU E 208 REMARK 465 TYR E 209 REMARK 465 PHE E 210 REMARK 465 GLN E 211 REMARK 465 GLY E 212 REMARK 465 SER E 213 REMARK 465 ALA E 214 REMARK 465 TRP E 215 REMARK 465 SER E 216 REMARK 465 HIS E 217 REMARK 465 PRO E 218 REMARK 465 GLN E 219 REMARK 465 PHE E 220 REMARK 465 GLU E 221 REMARK 465 LYS E 222 REMARK 465 GLY E 223 REMARK 465 GLY E 224 REMARK 465 GLY E 225 REMARK 465 SER E 226 REMARK 465 GLY E 227 REMARK 465 GLY E 228 REMARK 465 GLY E 229 REMARK 465 SER E 230 REMARK 465 HIS E 231 REMARK 465 HIS E 232 REMARK 465 HIS E 233 REMARK 465 HIS E 234 REMARK 465 HIS E 235 REMARK 465 HIS E 236 REMARK 465 SER G 112 REMARK 465 SER G 113 REMARK 465 ILE J 106 REMARK 465 LYS J 107 REMARK 465 MET D -15 REMARK 465 LYS D -14 REMARK 465 THR D -13 REMARK 465 ILE D -12 REMARK 465 ILE D -11 REMARK 465 ALA D -10 REMARK 465 LEU D -9 REMARK 465 SER D -8 REMARK 465 TYR D -7 REMARK 465 ILE D -6 REMARK 465 LEU D -5 REMARK 465 CYS D -4 REMARK 465 LEU D -3 REMARK 465 VAL D -2 REMARK 465 PHE D -1 REMARK 465 ALA D 0 REMARK 465 GLN D 1 REMARK 465 LYS D 2 REMARK 465 ILE D 3 REMARK 465 PRO D 4 REMARK 465 GLY D 5 REMARK 465 ASN D 6 REMARK 465 ASP D 7 REMARK 465 ASN D 8 REMARK 465 SER D 9 REMARK 465 LYS D 326 REMARK 465 GLN D 327 REMARK 465 THR D 328 REMARK 465 ARG D 329 REMARK 465 ILE F 173 REMARK 465 LYS F 174 REMARK 465 GLY F 175 REMARK 465 VAL F 176 REMARK 465 GLY F 177 REMARK 465 TYR F 178 REMARK 465 ILE F 179 REMARK 465 PRO F 180 REMARK 465 GLU F 181 REMARK 465 ALA F 182 REMARK 465 PRO F 183 REMARK 465 ARG F 184 REMARK 465 ASP F 185 REMARK 465 GLY F 186 REMARK 465 GLN F 187 REMARK 465 ALA F 188 REMARK 465 TYR F 189 REMARK 465 VAL F 190 REMARK 465 ARG F 191 REMARK 465 LYS F 192 REMARK 465 ASP F 193 REMARK 465 GLY F 194 REMARK 465 GLU F 195 REMARK 465 TRP F 196 REMARK 465 VAL F 197 REMARK 465 LEU F 198 REMARK 465 LEU F 199 REMARK 465 SER F 200 REMARK 465 THR F 201 REMARK 465 PHE F 202 REMARK 465 LEU F 203 REMARK 465 GLY F 204 REMARK 465 SER F 205 REMARK 465 GLU F 206 REMARK 465 ASN F 207 REMARK 465 LEU F 208 REMARK 465 TYR F 209 REMARK 465 PHE F 210 REMARK 465 GLN F 211 REMARK 465 GLY F 212 REMARK 465 SER F 213 REMARK 465 ALA F 214 REMARK 465 TRP F 215 REMARK 465 SER F 216 REMARK 465 HIS F 217 REMARK 465 PRO F 218 REMARK 465 GLN F 219 REMARK 465 PHE F 220 REMARK 465 GLU F 221 REMARK 465 LYS F 222 REMARK 465 GLY F 223 REMARK 465 GLY F 224 REMARK 465 GLY F 225 REMARK 465 SER F 226 REMARK 465 GLY F 227 REMARK 465 GLY F 228 REMARK 465 GLY F 229 REMARK 465 SER F 230 REMARK 465 HIS F 231 REMARK 465 HIS F 232 REMARK 465 HIS F 233 REMARK 465 HIS F 234 REMARK 465 HIS F 235 REMARK 465 HIS F 236 REMARK 465 SER I 112 REMARK 465 SER I 113 REMARK 465 ILE K 106 REMARK 465 LYS K 107 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 NH2 ARG A 222 C2 NAG a 2 1.33 REMARK 500 NH2 ARG A 222 N2 NAG a 2 1.36 REMARK 500 NH2 ARG C 222 N2 NAG Q 2 1.36 REMARK 500 NH1 ARG D 222 N2 NAG V 2 1.36 REMARK 500 NH2 ARG C 222 C2 NAG Q 2 1.53 REMARK 500 NH1 ARG D 222 C2 NAG V 2 1.56 REMARK 500 CZ ARG A 222 N2 NAG a 2 1.71 REMARK 500 CZ ARG C 222 N2 NAG Q 2 1.80 REMARK 500 O3 NAG O 1 O5 NAG O 2 2.10 REMARK 500 O3 NAG T 1 O5 NAG T 2 2.11 REMARK 500 O3 NAG Y 1 O5 NAG Y 2 2.11 REMARK 500 OD1 ASP H 86 OH TYR H 90 2.13 REMARK 500 OD1 ASP G 86 OH TYR G 90 2.14 REMARK 500 OD2 ASP I 72 NZ LYS I 75 2.18 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 CYS A 52 CB CYS A 52 SG 0.132 REMARK 500 CYS A 277 CB CYS A 277 SG -0.127 REMARK 500 CYS C 52 CB CYS C 52 SG 0.133 REMARK 500 CYS C 277 CB CYS C 277 SG -0.127 REMARK 500 CYS D 52 CB CYS D 52 SG 0.132 REMARK 500 CYS D 277 CB CYS D 277 SG -0.127 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 LEU A 13 CA - CB - CG ANGL. DEV. = 14.1 DEGREES REMARK 500 ASP A 188 CB - CG - OD1 ANGL. DEV. = 6.0 DEGREES REMARK 500 CYS A 277 CA - CB - SG ANGL. DEV. = 18.5 DEGREES REMARK 500 CYS B 137 CA - CB - SG ANGL. DEV. = 9.1 DEGREES REMARK 500 CYS B 144 CA - CB - SG ANGL. DEV. = 6.7 DEGREES REMARK 500 CYS L 23 CA - CB - SG ANGL. DEV. = 10.1 DEGREES REMARK 500 LEU C 13 CA - CB - CG ANGL. DEV. = 15.7 DEGREES REMARK 500 CYS C 277 CA - CB - SG ANGL. DEV. = 18.6 DEGREES REMARK 500 CYS E 137 CA - CB - SG ANGL. DEV. = 8.3 DEGREES REMARK 500 CYS E 144 CA - CB - SG ANGL. DEV. = 6.7 DEGREES REMARK 500 CYS J 23 CA - CB - SG ANGL. DEV. = 10.1 DEGREES REMARK 500 LEU D 13 CA - CB - CG ANGL. DEV. = 15.7 DEGREES REMARK 500 CYS D 277 CA - CB - SG ANGL. DEV. = 18.6 DEGREES REMARK 500 CYS F 137 CA - CB - SG ANGL. DEV. = 8.2 DEGREES REMARK 500 CYS F 144 CA - CB - SG ANGL. DEV. = 6.6 DEGREES REMARK 500 CYS K 23 CA - CB - SG ANGL. DEV. = 9.6 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 81 15.83 55.79 REMARK 500 LYS A 264 -4.20 74.52 REMARK 500 ALA B 7 -5.40 76.23 REMARK 500 PHE B 9 -8.21 73.37 REMARK 500 PHE B 63 -60.91 -97.51 REMARK 500 SER L 30 -133.64 58.79 REMARK 500 LEU L 47 -62.15 -99.65 REMARK 500 ALA L 50 -1.74 79.52 REMARK 500 ALA L 51 -6.98 79.83 REMARK 500 ASN C 81 15.80 55.84 REMARK 500 LYS C 264 -4.22 74.62 REMARK 500 ALA E 7 -5.42 76.34 REMARK 500 PHE E 9 -8.24 73.36 REMARK 500 PHE E 63 -60.85 -97.59 REMARK 500 SER J 30 -133.64 58.86 REMARK 500 LEU J 47 -62.06 -99.61 REMARK 500 ALA J 50 -1.60 79.05 REMARK 500 ALA J 51 -6.53 80.13 REMARK 500 ASN D 81 15.88 55.79 REMARK 500 LYS D 264 -4.25 74.57 REMARK 500 ALA F 7 -5.49 76.29 REMARK 500 PHE F 9 -8.24 73.36 REMARK 500 PHE F 63 -60.87 -97.54 REMARK 500 SER K 30 -133.63 58.91 REMARK 500 LEU K 47 -62.12 -99.65 REMARK 500 ALA K 50 -1.45 78.91 REMARK 500 ALA K 51 -6.53 80.07 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 ARG A 141 0.18 SIDE CHAIN REMARK 500 ARG A 142 0.14 SIDE CHAIN REMARK 500 ARG A 208 0.08 SIDE CHAIN REMARK 500 ARG A 222 0.23 SIDE CHAIN REMARK 500 ARG A 229 0.24 SIDE CHAIN REMARK 500 ARG B 32 0.12 SIDE CHAIN REMARK 500 ARG C 141 0.18 SIDE CHAIN REMARK 500 ARG C 142 0.14 SIDE CHAIN REMARK 500 ARG C 208 0.08 SIDE CHAIN REMARK 500 ARG C 229 0.25 SIDE CHAIN REMARK 500 ARG E 32 0.15 SIDE CHAIN REMARK 500 ARG D 141 0.18 SIDE CHAIN REMARK 500 ARG D 142 0.14 SIDE CHAIN REMARK 500 ARG D 208 0.08 SIDE CHAIN REMARK 500 ARG D 222 0.19 SIDE CHAIN REMARK 500 ARG D 229 0.25 SIDE CHAIN REMARK 500 ARG F 32 0.12 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-70235 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF NI04359_D30_240 FAB IN COMPLEX WITH INFLUENZA REMARK 900 VIRUS HEMAGGLUTININ FROM A/HONG KONG/485197/2014 (H3N2) DBREF1 9O8S A -15 329 UNP A0A0K0YAS1_9INFA DBREF2 9O8S A A0A0K0YAS1 1 345 DBREF1 9O8S B 1 176 UNP A0A0K0YAS1_9INFA DBREF2 9O8S B A0A0K0YAS1 346 521 DBREF 9O8S H 1 113 PDB 9O8S 9O8S 1 113 DBREF 9O8S L 1 107 PDB 9O8S 9O8S 1 107 DBREF1 9O8S C -15 329 UNP A0A0K0YAS1_9INFA DBREF2 9O8S C A0A0K0YAS1 1 345 DBREF1 9O8S E 1 176 UNP A0A0K0YAS1_9INFA DBREF2 9O8S E A0A0K0YAS1 346 521 DBREF 9O8S G 1 113 PDB 9O8S 9O8S 1 113 DBREF 9O8S J 1 107 PDB 9O8S 9O8S 1 107 DBREF1 9O8S D -15 329 UNP A0A0K0YAS1_9INFA DBREF2 9O8S D A0A0K0YAS1 1 345 DBREF1 9O8S F 1 176 UNP A0A0K0YAS1_9INFA DBREF2 9O8S F A0A0K0YAS1 346 521 DBREF 9O8S I 1 113 PDB 9O8S 9O8S 1 113 DBREF 9O8S K 1 107 PDB 9O8S 9O8S 1 107 SEQADV 9O8S GLY B 177 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S TYR B 178 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S ILE B 179 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S PRO B 180 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S GLU B 181 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S ALA B 182 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S PRO B 183 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S ARG B 184 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S ASP B 185 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S GLY B 186 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S GLN B 187 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S ALA B 188 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S TYR B 189 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S VAL B 190 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S ARG B 191 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S LYS B 192 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S ASP B 193 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S GLY B 194 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S GLU B 195 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S TRP B 196 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S VAL B 197 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S LEU B 198 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S LEU B 199 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S SER B 200 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S THR B 201 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S PHE B 202 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S LEU B 203 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S GLY B 204 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S SER B 205 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S GLU B 206 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S ASN B 207 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S LEU B 208 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S TYR B 209 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S PHE B 210 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S GLN B 211 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S GLY B 212 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S SER B 213 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S ALA B 214 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S TRP B 215 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S SER B 216 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S HIS B 217 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S PRO B 218 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S GLN B 219 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S PHE B 220 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S GLU B 221 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S LYS B 222 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S GLY B 223 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S GLY B 224 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S GLY B 225 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S SER B 226 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S GLY B 227 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S GLY B 228 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S GLY B 229 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S SER B 230 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S HIS B 231 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S HIS B 232 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S HIS B 233 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S HIS B 234 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S HIS B 235 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S HIS B 236 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S GLY E 177 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S TYR E 178 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S ILE E 179 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S PRO E 180 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S GLU E 181 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S ALA E 182 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S PRO E 183 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S ARG E 184 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S ASP E 185 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S GLY E 186 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S GLN E 187 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S ALA E 188 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S TYR E 189 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S VAL E 190 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S ARG E 191 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S LYS E 192 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S ASP E 193 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S GLY E 194 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S GLU E 195 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S TRP E 196 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S VAL E 197 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S LEU E 198 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S LEU E 199 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S SER E 200 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S THR E 201 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S PHE E 202 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S LEU E 203 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S GLY E 204 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S SER E 205 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S GLU E 206 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S ASN E 207 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S LEU E 208 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S TYR E 209 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S PHE E 210 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S GLN E 211 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S GLY E 212 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S SER E 213 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S ALA E 214 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S TRP E 215 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S SER E 216 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S HIS E 217 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S PRO E 218 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S GLN E 219 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S PHE E 220 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S GLU E 221 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S LYS E 222 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S GLY E 223 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S GLY E 224 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S GLY E 225 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S SER E 226 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S GLY E 227 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S GLY E 228 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S GLY E 229 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S SER E 230 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S HIS E 231 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S HIS E 232 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S HIS E 233 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S HIS E 234 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S HIS E 235 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S HIS E 236 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S GLY F 177 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S TYR F 178 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S ILE F 179 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S PRO F 180 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S GLU F 181 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S ALA F 182 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S PRO F 183 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S ARG F 184 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S ASP F 185 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S GLY F 186 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S GLN F 187 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S ALA F 188 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S TYR F 189 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S VAL F 190 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S ARG F 191 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S LYS F 192 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S ASP F 193 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S GLY F 194 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S GLU F 195 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S TRP F 196 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S VAL F 197 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S LEU F 198 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S LEU F 199 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S SER F 200 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S THR F 201 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S PHE F 202 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S LEU F 203 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S GLY F 204 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S SER F 205 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S GLU F 206 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S ASN F 207 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S LEU F 208 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S TYR F 209 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S PHE F 210 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S GLN F 211 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S GLY F 212 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S SER F 213 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S ALA F 214 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S TRP F 215 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S SER F 216 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S HIS F 217 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S PRO F 218 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S GLN F 219 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S PHE F 220 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S GLU F 221 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S LYS F 222 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S GLY F 223 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S GLY F 224 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S GLY F 225 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S SER F 226 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S GLY F 227 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S GLY F 228 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S GLY F 229 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S SER F 230 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S HIS F 231 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S HIS F 232 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S HIS F 233 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S HIS F 234 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S HIS F 235 UNP A0A0K0YAS EXPRESSION TAG SEQADV 9O8S HIS F 236 UNP A0A0K0YAS EXPRESSION TAG SEQRES 1 A 345 MET LYS THR ILE ILE ALA LEU SER TYR ILE LEU CYS LEU SEQRES 2 A 345 VAL PHE ALA GLN LYS ILE PRO GLY ASN ASP ASN SER THR SEQRES 3 A 345 ALA THR LEU CYS LEU GLY HIS HIS ALA VAL PRO ASN GLY SEQRES 4 A 345 THR ILE VAL LYS THR ILE THR ASN ASP ARG ILE GLU VAL SEQRES 5 A 345 THR ASN ALA THR GLU LEU VAL GLN ASN SER SER ILE GLY SEQRES 6 A 345 GLU ILE CYS ASP SER PRO HIS GLN ILE LEU ASP GLY GLU SEQRES 7 A 345 ASN CYS THR LEU ILE ASP ALA LEU LEU GLY ASP PRO GLN SEQRES 8 A 345 CYS ASP GLY PHE GLN ASN LYS LYS TRP ASP LEU PHE VAL SEQRES 9 A 345 GLU ARG SER LYS ALA TYR SER ASN CYS TYR PRO TYR ASP SEQRES 10 A 345 VAL PRO ASP TYR ALA SER LEU ARG SER LEU VAL ALA THR SEQRES 11 A 345 SER GLY THR LEU GLU PHE ASN ASN GLU SER PHE ASN TRP SEQRES 12 A 345 THR GLY VAL THR GLN ASN GLY THR SER SER ALA CYS ILE SEQRES 13 A 345 ARG ARG SER SER SER SER PHE PHE SER ARG LEU ASN TRP SEQRES 14 A 345 LEU THR HIS LEU ASN TYR THR TYR PRO ALA LEU ASN VAL SEQRES 15 A 345 THR MET PRO ASN ASN GLU GLN PHE ASP LYS LEU TYR ILE SEQRES 16 A 345 TRP GLY VAL HIS HIS PRO GLY THR ASP LYS ASP GLN ILE SEQRES 17 A 345 PHE LEU TYR ALA GLN SER SER GLY ARG ILE THR VAL SER SEQRES 18 A 345 THR LYS ARG SER GLN GLN ALA VAL ILE PRO ASN ILE GLY SEQRES 19 A 345 SER ARG PRO ARG ILE ARG ASP ILE PRO SER ARG ILE SER SEQRES 20 A 345 ILE TYR TRP THR ILE VAL LYS PRO GLY ASP ILE LEU LEU SEQRES 21 A 345 ILE ASN SER THR GLY ASN LEU ILE ALA PRO ARG GLY TYR SEQRES 22 A 345 PHE LYS ILE ARG SER GLY LYS SER SER ILE MET ARG SER SEQRES 23 A 345 ASP ALA PRO ILE GLY LYS CYS LYS SER GLU CYS ILE THR SEQRES 24 A 345 PRO ASN GLY SER ILE PRO ASN ASP LYS PRO PHE GLN ASN SEQRES 25 A 345 VAL ASN ARG ILE THR TYR GLY ALA CYS PRO ARG TYR VAL SEQRES 26 A 345 LYS HIS SER THR LEU LYS LEU ALA THR GLY MET ARG ASN SEQRES 27 A 345 VAL PRO GLU LYS GLN THR ARG SEQRES 1 B 236 GLY ILE PHE GLY ALA ILE ALA GLY PHE ILE GLU ASN GLY SEQRES 2 B 236 TRP GLU GLY MET VAL ASP GLY TRP TYR GLY PHE ARG HIS SEQRES 3 B 236 GLN ASN SER GLU GLY ARG GLY GLN ALA ALA ASP LEU LYS SEQRES 4 B 236 SER THR GLN ALA ALA ILE ASP GLN ILE ASN GLY LYS LEU SEQRES 5 B 236 ASN ARG LEU ILE GLY LYS THR ASN GLU LYS PHE HIS GLN SEQRES 6 B 236 ILE GLU LYS GLU PHE SER GLU VAL GLU GLY ARG ILE GLN SEQRES 7 B 236 ASP LEU GLU LYS TYR VAL GLU ASP THR LYS ILE ASP LEU SEQRES 8 B 236 TRP SER TYR ASN ALA GLU LEU LEU VAL ALA LEU GLU ASN SEQRES 9 B 236 GLN HIS THR ILE ASP LEU THR ASP SER GLU MET ASN LYS SEQRES 10 B 236 LEU PHE GLU LYS THR LYS LYS GLN LEU ARG GLU ASN ALA SEQRES 11 B 236 GLU ASP MET GLY ASN GLY CYS PHE LYS ILE TYR HIS LYS SEQRES 12 B 236 CYS ASP ASN ALA CYS ILE GLY SER ILE ARG ASN GLY THR SEQRES 13 B 236 TYR ASP HIS ASN VAL TYR ARG ASP GLU ALA LEU ASN ASN SEQRES 14 B 236 ARG PHE GLN ILE LYS GLY VAL GLY TYR ILE PRO GLU ALA SEQRES 15 B 236 PRO ARG ASP GLY GLN ALA TYR VAL ARG LYS ASP GLY GLU SEQRES 16 B 236 TRP VAL LEU LEU SER THR PHE LEU GLY SER GLU ASN LEU SEQRES 17 B 236 TYR PHE GLN GLY SER ALA TRP SER HIS PRO GLN PHE GLU SEQRES 18 B 236 LYS GLY GLY GLY SER GLY GLY GLY SER HIS HIS HIS HIS SEQRES 19 B 236 HIS HIS SEQRES 1 H 130 ASP VAL GLN LEU LEU GLU SER GLY GLY GLY LEU VAL HIS SEQRES 2 H 130 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 H 130 PHE THR PHE SER SER TYR GLY MET ASN TRP VAL ARG GLN SEQRES 4 H 130 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER GLY ILE SER SEQRES 5 H 130 GLY SER GLY GLY THR THR TYR TYR ALA ASP SER VAL LYS SEQRES 6 H 130 GLY ARG PHE THR VAL SER ARG ASP ASN SER LYS ASN THR SEQRES 7 H 130 LEU PHE LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 H 130 ALA VAL TYR TYR CYS ALA LYS ASP ARG GLY CYS ARG SER SEQRES 9 H 130 SER ASN CYS TYR ILE VAL GLY TYR TYR TYR TYR GLY MET SEQRES 10 H 130 ASP VAL TRP GLY GLN GLY THR THR VAL THR VAL SER SER SEQRES 1 L 107 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 L 107 SER VAL GLY ASP ARG VAL THR PHE THR CYS ARG ALA SER SEQRES 3 L 107 GLN SER ILE SER SER TYR LEU ASN TRP TYR GLN GLN LYS SEQRES 4 L 107 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR ALA ALA SER SEQRES 5 L 107 SER LEU GLN ASN GLU VAL PRO SER ARG PHE SER GLY SER SEQRES 6 L 107 GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 L 107 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN SER SEQRES 8 L 107 SER SER THR PRO LEU THR PHE GLY GLY GLY THR THR VAL SEQRES 9 L 107 GLU ILE LYS SEQRES 1 C 345 MET LYS THR ILE ILE ALA LEU SER TYR ILE LEU CYS LEU SEQRES 2 C 345 VAL PHE ALA GLN LYS ILE PRO GLY ASN ASP ASN SER THR SEQRES 3 C 345 ALA THR LEU CYS LEU GLY HIS HIS ALA VAL PRO ASN GLY SEQRES 4 C 345 THR ILE VAL LYS THR ILE THR ASN ASP ARG ILE GLU VAL SEQRES 5 C 345 THR ASN ALA THR GLU LEU VAL GLN ASN SER SER ILE GLY SEQRES 6 C 345 GLU ILE CYS ASP SER PRO HIS GLN ILE LEU ASP GLY GLU SEQRES 7 C 345 ASN CYS THR LEU ILE ASP ALA LEU LEU GLY ASP PRO GLN SEQRES 8 C 345 CYS ASP GLY PHE GLN ASN LYS LYS TRP ASP LEU PHE VAL SEQRES 9 C 345 GLU ARG SER LYS ALA TYR SER ASN CYS TYR PRO TYR ASP SEQRES 10 C 345 VAL PRO ASP TYR ALA SER LEU ARG SER LEU VAL ALA THR SEQRES 11 C 345 SER GLY THR LEU GLU PHE ASN ASN GLU SER PHE ASN TRP SEQRES 12 C 345 THR GLY VAL THR GLN ASN GLY THR SER SER ALA CYS ILE SEQRES 13 C 345 ARG ARG SER SER SER SER PHE PHE SER ARG LEU ASN TRP SEQRES 14 C 345 LEU THR HIS LEU ASN TYR THR TYR PRO ALA LEU ASN VAL SEQRES 15 C 345 THR MET PRO ASN ASN GLU GLN PHE ASP LYS LEU TYR ILE SEQRES 16 C 345 TRP GLY VAL HIS HIS PRO GLY THR ASP LYS ASP GLN ILE SEQRES 17 C 345 PHE LEU TYR ALA GLN SER SER GLY ARG ILE THR VAL SER SEQRES 18 C 345 THR LYS ARG SER GLN GLN ALA VAL ILE PRO ASN ILE GLY SEQRES 19 C 345 SER ARG PRO ARG ILE ARG ASP ILE PRO SER ARG ILE SER SEQRES 20 C 345 ILE TYR TRP THR ILE VAL LYS PRO GLY ASP ILE LEU LEU SEQRES 21 C 345 ILE ASN SER THR GLY ASN LEU ILE ALA PRO ARG GLY TYR SEQRES 22 C 345 PHE LYS ILE ARG SER GLY LYS SER SER ILE MET ARG SER SEQRES 23 C 345 ASP ALA PRO ILE GLY LYS CYS LYS SER GLU CYS ILE THR SEQRES 24 C 345 PRO ASN GLY SER ILE PRO ASN ASP LYS PRO PHE GLN ASN SEQRES 25 C 345 VAL ASN ARG ILE THR TYR GLY ALA CYS PRO ARG TYR VAL SEQRES 26 C 345 LYS HIS SER THR LEU LYS LEU ALA THR GLY MET ARG ASN SEQRES 27 C 345 VAL PRO GLU LYS GLN THR ARG SEQRES 1 E 236 GLY ILE PHE GLY ALA ILE ALA GLY PHE ILE GLU ASN GLY SEQRES 2 E 236 TRP GLU GLY MET VAL ASP GLY TRP TYR GLY PHE ARG HIS SEQRES 3 E 236 GLN ASN SER GLU GLY ARG GLY GLN ALA ALA ASP LEU LYS SEQRES 4 E 236 SER THR GLN ALA ALA ILE ASP GLN ILE ASN GLY LYS LEU SEQRES 5 E 236 ASN ARG LEU ILE GLY LYS THR ASN GLU LYS PHE HIS GLN SEQRES 6 E 236 ILE GLU LYS GLU PHE SER GLU VAL GLU GLY ARG ILE GLN SEQRES 7 E 236 ASP LEU GLU LYS TYR VAL GLU ASP THR LYS ILE ASP LEU SEQRES 8 E 236 TRP SER TYR ASN ALA GLU LEU LEU VAL ALA LEU GLU ASN SEQRES 9 E 236 GLN HIS THR ILE ASP LEU THR ASP SER GLU MET ASN LYS SEQRES 10 E 236 LEU PHE GLU LYS THR LYS LYS GLN LEU ARG GLU ASN ALA SEQRES 11 E 236 GLU ASP MET GLY ASN GLY CYS PHE LYS ILE TYR HIS LYS SEQRES 12 E 236 CYS ASP ASN ALA CYS ILE GLY SER ILE ARG ASN GLY THR SEQRES 13 E 236 TYR ASP HIS ASN VAL TYR ARG ASP GLU ALA LEU ASN ASN SEQRES 14 E 236 ARG PHE GLN ILE LYS GLY VAL GLY TYR ILE PRO GLU ALA SEQRES 15 E 236 PRO ARG ASP GLY GLN ALA TYR VAL ARG LYS ASP GLY GLU SEQRES 16 E 236 TRP VAL LEU LEU SER THR PHE LEU GLY SER GLU ASN LEU SEQRES 17 E 236 TYR PHE GLN GLY SER ALA TRP SER HIS PRO GLN PHE GLU SEQRES 18 E 236 LYS GLY GLY GLY SER GLY GLY GLY SER HIS HIS HIS HIS SEQRES 19 E 236 HIS HIS SEQRES 1 G 130 ASP VAL GLN LEU LEU GLU SER GLY GLY GLY LEU VAL HIS SEQRES 2 G 130 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 G 130 PHE THR PHE SER SER TYR GLY MET ASN TRP VAL ARG GLN SEQRES 4 G 130 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER GLY ILE SER SEQRES 5 G 130 GLY SER GLY GLY THR THR TYR TYR ALA ASP SER VAL LYS SEQRES 6 G 130 GLY ARG PHE THR VAL SER ARG ASP ASN SER LYS ASN THR SEQRES 7 G 130 LEU PHE LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 G 130 ALA VAL TYR TYR CYS ALA LYS ASP ARG GLY CYS ARG SER SEQRES 9 G 130 SER ASN CYS TYR ILE VAL GLY TYR TYR TYR TYR GLY MET SEQRES 10 G 130 ASP VAL TRP GLY GLN GLY THR THR VAL THR VAL SER SER SEQRES 1 J 107 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 J 107 SER VAL GLY ASP ARG VAL THR PHE THR CYS ARG ALA SER SEQRES 3 J 107 GLN SER ILE SER SER TYR LEU ASN TRP TYR GLN GLN LYS SEQRES 4 J 107 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR ALA ALA SER SEQRES 5 J 107 SER LEU GLN ASN GLU VAL PRO SER ARG PHE SER GLY SER SEQRES 6 J 107 GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 J 107 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN SER SEQRES 8 J 107 SER SER THR PRO LEU THR PHE GLY GLY GLY THR THR VAL SEQRES 9 J 107 GLU ILE LYS SEQRES 1 D 345 MET LYS THR ILE ILE ALA LEU SER TYR ILE LEU CYS LEU SEQRES 2 D 345 VAL PHE ALA GLN LYS ILE PRO GLY ASN ASP ASN SER THR SEQRES 3 D 345 ALA THR LEU CYS LEU GLY HIS HIS ALA VAL PRO ASN GLY SEQRES 4 D 345 THR ILE VAL LYS THR ILE THR ASN ASP ARG ILE GLU VAL SEQRES 5 D 345 THR ASN ALA THR GLU LEU VAL GLN ASN SER SER ILE GLY SEQRES 6 D 345 GLU ILE CYS ASP SER PRO HIS GLN ILE LEU ASP GLY GLU SEQRES 7 D 345 ASN CYS THR LEU ILE ASP ALA LEU LEU GLY ASP PRO GLN SEQRES 8 D 345 CYS ASP GLY PHE GLN ASN LYS LYS TRP ASP LEU PHE VAL SEQRES 9 D 345 GLU ARG SER LYS ALA TYR SER ASN CYS TYR PRO TYR ASP SEQRES 10 D 345 VAL PRO ASP TYR ALA SER LEU ARG SER LEU VAL ALA THR SEQRES 11 D 345 SER GLY THR LEU GLU PHE ASN ASN GLU SER PHE ASN TRP SEQRES 12 D 345 THR GLY VAL THR GLN ASN GLY THR SER SER ALA CYS ILE SEQRES 13 D 345 ARG ARG SER SER SER SER PHE PHE SER ARG LEU ASN TRP SEQRES 14 D 345 LEU THR HIS LEU ASN TYR THR TYR PRO ALA LEU ASN VAL SEQRES 15 D 345 THR MET PRO ASN ASN GLU GLN PHE ASP LYS LEU TYR ILE SEQRES 16 D 345 TRP GLY VAL HIS HIS PRO GLY THR ASP LYS ASP GLN ILE SEQRES 17 D 345 PHE LEU TYR ALA GLN SER SER GLY ARG ILE THR VAL SER SEQRES 18 D 345 THR LYS ARG SER GLN GLN ALA VAL ILE PRO ASN ILE GLY SEQRES 19 D 345 SER ARG PRO ARG ILE ARG ASP ILE PRO SER ARG ILE SER SEQRES 20 D 345 ILE TYR TRP THR ILE VAL LYS PRO GLY ASP ILE LEU LEU SEQRES 21 D 345 ILE ASN SER THR GLY ASN LEU ILE ALA PRO ARG GLY TYR SEQRES 22 D 345 PHE LYS ILE ARG SER GLY LYS SER SER ILE MET ARG SER SEQRES 23 D 345 ASP ALA PRO ILE GLY LYS CYS LYS SER GLU CYS ILE THR SEQRES 24 D 345 PRO ASN GLY SER ILE PRO ASN ASP LYS PRO PHE GLN ASN SEQRES 25 D 345 VAL ASN ARG ILE THR TYR GLY ALA CYS PRO ARG TYR VAL SEQRES 26 D 345 LYS HIS SER THR LEU LYS LEU ALA THR GLY MET ARG ASN SEQRES 27 D 345 VAL PRO GLU LYS GLN THR ARG SEQRES 1 F 236 GLY ILE PHE GLY ALA ILE ALA GLY PHE ILE GLU ASN GLY SEQRES 2 F 236 TRP GLU GLY MET VAL ASP GLY TRP TYR GLY PHE ARG HIS SEQRES 3 F 236 GLN ASN SER GLU GLY ARG GLY GLN ALA ALA ASP LEU LYS SEQRES 4 F 236 SER THR GLN ALA ALA ILE ASP GLN ILE ASN GLY LYS LEU SEQRES 5 F 236 ASN ARG LEU ILE GLY LYS THR ASN GLU LYS PHE HIS GLN SEQRES 6 F 236 ILE GLU LYS GLU PHE SER GLU VAL GLU GLY ARG ILE GLN SEQRES 7 F 236 ASP LEU GLU LYS TYR VAL GLU ASP THR LYS ILE ASP LEU SEQRES 8 F 236 TRP SER TYR ASN ALA GLU LEU LEU VAL ALA LEU GLU ASN SEQRES 9 F 236 GLN HIS THR ILE ASP LEU THR ASP SER GLU MET ASN LYS SEQRES 10 F 236 LEU PHE GLU LYS THR LYS LYS GLN LEU ARG GLU ASN ALA SEQRES 11 F 236 GLU ASP MET GLY ASN GLY CYS PHE LYS ILE TYR HIS LYS SEQRES 12 F 236 CYS ASP ASN ALA CYS ILE GLY SER ILE ARG ASN GLY THR SEQRES 13 F 236 TYR ASP HIS ASN VAL TYR ARG ASP GLU ALA LEU ASN ASN SEQRES 14 F 236 ARG PHE GLN ILE LYS GLY VAL GLY TYR ILE PRO GLU ALA SEQRES 15 F 236 PRO ARG ASP GLY GLN ALA TYR VAL ARG LYS ASP GLY GLU SEQRES 16 F 236 TRP VAL LEU LEU SER THR PHE LEU GLY SER GLU ASN LEU SEQRES 17 F 236 TYR PHE GLN GLY SER ALA TRP SER HIS PRO GLN PHE GLU SEQRES 18 F 236 LYS GLY GLY GLY SER GLY GLY GLY SER HIS HIS HIS HIS SEQRES 19 F 236 HIS HIS SEQRES 1 I 130 ASP VAL GLN LEU LEU GLU SER GLY GLY GLY LEU VAL HIS SEQRES 2 I 130 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 I 130 PHE THR PHE SER SER TYR GLY MET ASN TRP VAL ARG GLN SEQRES 4 I 130 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER GLY ILE SER SEQRES 5 I 130 GLY SER GLY GLY THR THR TYR TYR ALA ASP SER VAL LYS SEQRES 6 I 130 GLY ARG PHE THR VAL SER ARG ASP ASN SER LYS ASN THR SEQRES 7 I 130 LEU PHE LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 I 130 ALA VAL TYR TYR CYS ALA LYS ASP ARG GLY CYS ARG SER SEQRES 9 I 130 SER ASN CYS TYR ILE VAL GLY TYR TYR TYR TYR GLY MET SEQRES 10 I 130 ASP VAL TRP GLY GLN GLY THR THR VAL THR VAL SER SER SEQRES 1 K 107 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 K 107 SER VAL GLY ASP ARG VAL THR PHE THR CYS ARG ALA SER SEQRES 3 K 107 GLN SER ILE SER SER TYR LEU ASN TRP TYR GLN GLN LYS SEQRES 4 K 107 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR ALA ALA SER SEQRES 5 K 107 SER LEU GLN ASN GLU VAL PRO SER ARG PHE SER GLY SER SEQRES 6 K 107 GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 K 107 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN SER SEQRES 8 K 107 SER SER THR PRO LEU THR PHE GLY GLY GLY THR THR VAL SEQRES 9 K 107 GLU ILE LYS HET NAG M 1 14 HET NAG M 2 14 HET NAG N 1 14 HET NAG N 2 14 HET FUC N 3 10 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 NAG Q 1 14 HET NAG Q 2 14 HET BMA Q 3 11 HET NAG R 1 14 HET NAG R 2 14 HET NAG S 1 14 HET NAG S 2 14 HET FUC S 3 10 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 NAG X 1 14 HET NAG X 2 14 HET FUC X 3 10 HET NAG Y 1 14 HET NAG Y 2 14 HET NAG Z 1 14 HET NAG Z 2 14 HET BMA Z 3 11 HET NAG a 1 14 HET NAG a 2 14 HET BMA a 3 11 HET NAG A 401 14 HET NAG A 402 14 HET NAG A 403 14 HET NAG A 404 14 HET NAG A 405 14 HET NAG B 301 14 HET NAG C 401 14 HET NAG C 402 14 HET NAG C 403 14 HET NAG C 404 14 HET NAG C 405 14 HET NAG E 301 14 HET NAG D 401 14 HET NAG D 402 14 HET NAG D 403 14 HET NAG D 404 14 HET NAG D 405 14 HET NAG F 301 14 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM FUC ALPHA-L-FUCOPYRANOSE 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 FUC ALPHA-L-FUCOSE; 6-DEOXY-ALPHA-L-GALACTOPYRANOSE; L- HETSYN 2 FUC FUCOSE; FUCOSE HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE FORMUL 13 NAG 48(C8 H15 N O6) FORMUL 14 FUC 3(C6 H12 O5) FORMUL 16 BMA 6(C6 H12 O6) HELIX 1 AA1 THR A 65 LEU A 71 1 7 HELIX 2 AA2 ASP A 104 GLY A 116 1 13 HELIX 3 AA3 THR A 187 TYR A 195 1 9 HELIX 4 AA4 ASP B 37 ILE B 56 1 20 HELIX 5 AA5 GLY B 75 LEU B 126 1 52 HELIX 6 AA6 ASP B 145 ASN B 154 1 10 HELIX 7 AA7 TYR B 162 PHE B 171 1 10 HELIX 8 AA8 THR C 65 LEU C 71 1 7 HELIX 9 AA9 ASP C 104 GLY C 116 1 13 HELIX 10 AB1 THR C 187 TYR C 195 1 9 HELIX 11 AB2 ASP E 37 ILE E 56 1 20 HELIX 12 AB3 GLY E 75 LEU E 126 1 52 HELIX 13 AB4 ASP E 145 ASN E 154 1 10 HELIX 14 AB5 TYR E 162 PHE E 171 1 10 HELIX 15 AB6 THR D 65 LEU D 71 1 7 HELIX 16 AB7 ASP D 104 GLY D 116 1 13 HELIX 17 AB8 THR D 187 TYR D 195 1 9 HELIX 18 AB9 ASP F 37 ILE F 56 1 20 HELIX 19 AC1 GLY F 75 LEU F 126 1 52 HELIX 20 AC2 ASP F 145 ASN F 154 1 10 HELIX 21 AC3 TYR F 162 PHE F 171 1 10 SHEET 1 AA1 5 GLY B 33 ALA B 36 0 SHEET 2 AA1 5 TYR B 22 GLN B 27 -1 N HIS B 26 O GLY B 33 SHEET 3 AA1 5 ALA A 11 HIS A 17 -1 N THR A 12 O GLN B 27 SHEET 4 AA1 5 PHE B 138 ILE B 140 -1 O PHE B 138 N LEU A 13 SHEET 5 AA1 5 ALA B 130 ASP B 132 -1 N GLU B 131 O LYS B 139 SHEET 1 AA2 2 THR A 24 VAL A 26 0 SHEET 2 AA2 2 ILE A 34 VAL A 36 -1 O VAL A 36 N THR A 24 SHEET 1 AA3 2 ALA A 39 GLU A 41 0 SHEET 2 AA3 2 LYS A 315 ALA A 317 -1 O LEU A 316 N THR A 40 SHEET 1 AA4 3 VAL A 43 GLN A 44 0 SHEET 2 AA4 3 PHE A 294 GLN A 295 1 O PHE A 294 N GLN A 44 SHEET 3 AA4 3 ARG A 307 TYR A 308 1 O ARG A 307 N GLN A 295 SHEET 1 AA5 2 ILE A 51 CYS A 52 0 SHEET 2 AA5 2 ILE A 274 GLY A 275 1 O GLY A 275 N ILE A 51 SHEET 1 AA6 3 ILE A 58 ASP A 60 0 SHEET 2 AA6 3 LEU A 86 GLU A 89 1 O LEU A 86 N LEU A 59 SHEET 3 AA6 3 SER A 266 ARG A 269 1 O MET A 268 N GLU A 89 SHEET 1 AA7 5 PHE A 120 ASN A 122 0 SHEET 2 AA7 5 GLY A 256 LYS A 259 -1 O TYR A 257 N ASN A 121 SHEET 3 AA7 5 LYS A 176 HIS A 184 -1 N LEU A 177 O PHE A 258 SHEET 4 AA7 5 LEU A 251 PRO A 254 -1 O ILE A 252 N GLY A 181 SHEET 5 AA7 5 LEU A 151 TRP A 153 -1 N ASN A 152 O ALA A 253 SHEET 1 AA8 4 PHE A 120 ASN A 122 0 SHEET 2 AA8 4 GLY A 256 LYS A 259 -1 O TYR A 257 N ASN A 121 SHEET 3 AA8 4 LYS A 176 HIS A 184 -1 N LEU A 177 O PHE A 258 SHEET 4 AA8 4 ARG A 229 VAL A 237 -1 O ARG A 229 N HIS A 184 SHEET 1 AA9 2 VAL A 130 THR A 131 0 SHEET 2 AA9 2 THR A 155 HIS A 156 -1 O THR A 155 N THR A 131 SHEET 1 AB1 2 ILE A 140 ARG A 141 0 SHEET 2 AB1 2 SER A 144 SER A 145 -1 O SER A 144 N ARG A 141 SHEET 1 AB2 4 LEU A 164 PRO A 169 0 SHEET 2 AB2 4 ILE A 242 SER A 247 -1 O LEU A 243 N MET A 168 SHEET 3 AB2 4 ILE A 202 THR A 206 -1 N THR A 203 O ASN A 246 SHEET 4 AB2 4 GLN A 210 VAL A 213 -1 O GLN A 211 N VAL A 204 SHEET 1 AB3 2 GLY A 303 ALA A 304 0 SHEET 2 AB3 2 GLU B 61 LYS B 62 -1 O LYS B 62 N GLY A 303 SHEET 1 AB4 3 ARG H 19 CYS H 22 0 SHEET 2 AB4 3 THR H 77 MET H 82 -1 O LEU H 80 N LEU H 20 SHEET 3 AB4 3 PHE H 67 ASP H 72 -1 N THR H 68 O GLN H 81 SHEET 1 AB5 5 THR H 57 TYR H 59 0 SHEET 2 AB5 5 LEU H 45 ILE H 51 -1 N GLY H 50 O TYR H 58 SHEET 3 AB5 5 MET H 34 GLN H 39 -1 N ARG H 38 O GLU H 46 SHEET 4 AB5 5 VAL H 89 LYS H 94 -1 O ALA H 93 N ASN H 35 SHEET 5 AB5 5 THR H 107 THR H 108 -1 O THR H 107 N TYR H 90 SHEET 1 AB6 4 MET L 4 GLN L 6 0 SHEET 2 AB6 4 VAL L 19 ALA L 25 -1 O ARG L 24 N THR L 5 SHEET 3 AB6 4 ASP L 70 ILE L 75 -1 O ILE L 75 N VAL L 19 SHEET 4 AB6 4 PHE L 62 SER L 67 -1 N SER L 65 O THR L 72 SHEET 1 AB7 6 SER L 10 SER L 12 0 SHEET 2 AB7 6 THR L 102 GLU L 105 1 O THR L 103 N LEU L 11 SHEET 3 AB7 6 THR L 85 GLN L 89 -1 N TYR L 86 O THR L 102 SHEET 4 AB7 6 ASN L 34 GLN L 38 -1 N TYR L 36 O TYR L 87 SHEET 5 AB7 6 LYS L 45 TYR L 49 -1 O LYS L 45 N GLN L 37 SHEET 6 AB7 6 SER L 53 LEU L 54 -1 O SER L 53 N TYR L 49 SHEET 1 AB8 5 GLY E 33 ALA E 36 0 SHEET 2 AB8 5 TYR E 22 GLN E 27 -1 N HIS E 26 O GLY E 33 SHEET 3 AB8 5 ALA C 11 HIS C 17 -1 N CYS C 14 O ARG E 25 SHEET 4 AB8 5 PHE E 138 ILE E 140 -1 O PHE E 138 N LEU C 13 SHEET 5 AB8 5 ALA E 130 ASP E 132 -1 N GLU E 131 O LYS E 139 SHEET 1 AB9 2 THR C 24 VAL C 26 0 SHEET 2 AB9 2 ILE C 34 VAL C 36 -1 O VAL C 36 N THR C 24 SHEET 1 AC1 2 ALA C 39 GLU C 41 0 SHEET 2 AC1 2 LYS C 315 ALA C 317 -1 O LEU C 316 N THR C 40 SHEET 1 AC2 3 VAL C 43 GLN C 44 0 SHEET 2 AC2 3 PHE C 294 GLN C 295 1 O PHE C 294 N GLN C 44 SHEET 3 AC2 3 ARG C 307 TYR C 308 1 O ARG C 307 N GLN C 295 SHEET 1 AC3 2 ILE C 51 CYS C 52 0 SHEET 2 AC3 2 ILE C 274 GLY C 275 1 O GLY C 275 N ILE C 51 SHEET 1 AC4 3 ILE C 58 ASP C 60 0 SHEET 2 AC4 3 LEU C 86 GLU C 89 1 O LEU C 86 N LEU C 59 SHEET 3 AC4 3 SER C 266 ARG C 269 1 O MET C 268 N GLU C 89 SHEET 1 AC5 5 PHE C 120 ASN C 122 0 SHEET 2 AC5 5 GLY C 256 LYS C 259 -1 O TYR C 257 N ASN C 121 SHEET 3 AC5 5 LYS C 176 HIS C 184 -1 N LEU C 177 O PHE C 258 SHEET 4 AC5 5 LEU C 251 PRO C 254 -1 O ILE C 252 N GLY C 181 SHEET 5 AC5 5 LEU C 151 TRP C 153 -1 N ASN C 152 O ALA C 253 SHEET 1 AC6 4 PHE C 120 ASN C 122 0 SHEET 2 AC6 4 GLY C 256 LYS C 259 -1 O TYR C 257 N ASN C 121 SHEET 3 AC6 4 LYS C 176 HIS C 184 -1 N LEU C 177 O PHE C 258 SHEET 4 AC6 4 ARG C 229 VAL C 237 -1 O ARG C 229 N HIS C 184 SHEET 1 AC7 2 VAL C 130 THR C 131 0 SHEET 2 AC7 2 THR C 155 HIS C 156 -1 O THR C 155 N THR C 131 SHEET 1 AC8 2 ILE C 140 ARG C 141 0 SHEET 2 AC8 2 SER C 144 SER C 145 -1 O SER C 144 N ARG C 141 SHEET 1 AC9 4 LEU C 164 PRO C 169 0 SHEET 2 AC9 4 ILE C 242 SER C 247 -1 O LEU C 243 N MET C 168 SHEET 3 AC9 4 ILE C 202 THR C 206 -1 N THR C 203 O ASN C 246 SHEET 4 AC9 4 GLN C 210 VAL C 213 -1 O GLN C 211 N VAL C 204 SHEET 1 AD1 2 GLY C 303 ALA C 304 0 SHEET 2 AD1 2 GLU E 61 LYS E 62 -1 O LYS E 62 N GLY C 303 SHEET 1 AD2 3 ARG G 19 CYS G 22 0 SHEET 2 AD2 3 THR G 77 MET G 82 -1 O LEU G 80 N LEU G 20 SHEET 3 AD2 3 PHE G 67 ASP G 72 -1 N THR G 68 O GLN G 81 SHEET 1 AD3 5 THR G 57 TYR G 59 0 SHEET 2 AD3 5 LEU G 45 ILE G 51 -1 N GLY G 50 O TYR G 58 SHEET 3 AD3 5 MET G 34 GLN G 39 -1 N ARG G 38 O GLU G 46 SHEET 4 AD3 5 VAL G 89 LYS G 94 -1 O ALA G 93 N ASN G 35 SHEET 5 AD3 5 THR G 107 THR G 108 -1 O THR G 107 N TYR G 90 SHEET 1 AD4 4 MET J 4 GLN J 6 0 SHEET 2 AD4 4 VAL J 19 ALA J 25 -1 O ARG J 24 N THR J 5 SHEET 3 AD4 4 ASP J 70 ILE J 75 -1 O ILE J 75 N VAL J 19 SHEET 4 AD4 4 PHE J 62 SER J 67 -1 N SER J 65 O THR J 72 SHEET 1 AD5 6 SER J 10 SER J 12 0 SHEET 2 AD5 6 THR J 102 GLU J 105 1 O THR J 103 N LEU J 11 SHEET 3 AD5 6 THR J 85 GLN J 89 -1 N TYR J 86 O THR J 102 SHEET 4 AD5 6 ASN J 34 GLN J 38 -1 N TYR J 36 O TYR J 87 SHEET 5 AD5 6 LYS J 45 TYR J 49 -1 O LYS J 45 N GLN J 37 SHEET 6 AD5 6 SER J 53 LEU J 54 -1 O SER J 53 N TYR J 49 SHEET 1 AD6 5 GLY F 33 ALA F 36 0 SHEET 2 AD6 5 TYR F 22 GLN F 27 -1 N HIS F 26 O GLY F 33 SHEET 3 AD6 5 ALA D 11 HIS D 17 -1 N CYS D 14 O ARG F 25 SHEET 4 AD6 5 PHE F 138 ILE F 140 -1 O PHE F 138 N LEU D 13 SHEET 5 AD6 5 ALA F 130 ASP F 132 -1 N GLU F 131 O LYS F 139 SHEET 1 AD7 2 THR D 24 VAL D 26 0 SHEET 2 AD7 2 ILE D 34 VAL D 36 -1 O VAL D 36 N THR D 24 SHEET 1 AD8 2 ALA D 39 GLU D 41 0 SHEET 2 AD8 2 LYS D 315 ALA D 317 -1 O LEU D 316 N THR D 40 SHEET 1 AD9 3 VAL D 43 GLN D 44 0 SHEET 2 AD9 3 PHE D 294 GLN D 295 1 O PHE D 294 N GLN D 44 SHEET 3 AD9 3 ARG D 307 TYR D 308 1 O ARG D 307 N GLN D 295 SHEET 1 AE1 2 ILE D 51 CYS D 52 0 SHEET 2 AE1 2 ILE D 274 GLY D 275 1 O GLY D 275 N ILE D 51 SHEET 1 AE2 3 ILE D 58 ASP D 60 0 SHEET 2 AE2 3 LEU D 86 GLU D 89 1 O LEU D 86 N LEU D 59 SHEET 3 AE2 3 SER D 266 ARG D 269 1 O MET D 268 N GLU D 89 SHEET 1 AE3 5 PHE D 120 ASN D 122 0 SHEET 2 AE3 5 GLY D 256 LYS D 259 -1 O TYR D 257 N ASN D 121 SHEET 3 AE3 5 LYS D 176 HIS D 184 -1 N LEU D 177 O PHE D 258 SHEET 4 AE3 5 LEU D 251 PRO D 254 -1 O ILE D 252 N GLY D 181 SHEET 5 AE3 5 LEU D 151 TRP D 153 -1 N ASN D 152 O ALA D 253 SHEET 1 AE4 4 PHE D 120 ASN D 122 0 SHEET 2 AE4 4 GLY D 256 LYS D 259 -1 O TYR D 257 N ASN D 121 SHEET 3 AE4 4 LYS D 176 HIS D 184 -1 N LEU D 177 O PHE D 258 SHEET 4 AE4 4 ARG D 229 VAL D 237 -1 O ARG D 229 N HIS D 184 SHEET 1 AE5 2 VAL D 130 THR D 131 0 SHEET 2 AE5 2 THR D 155 HIS D 156 -1 O THR D 155 N THR D 131 SHEET 1 AE6 2 ILE D 140 ARG D 141 0 SHEET 2 AE6 2 SER D 144 SER D 145 -1 O SER D 144 N ARG D 141 SHEET 1 AE7 4 LEU D 164 PRO D 169 0 SHEET 2 AE7 4 ILE D 242 SER D 247 -1 O LEU D 243 N MET D 168 SHEET 3 AE7 4 ILE D 202 THR D 206 -1 N THR D 203 O ASN D 246 SHEET 4 AE7 4 GLN D 210 VAL D 213 -1 O GLN D 211 N VAL D 204 SHEET 1 AE8 2 GLY D 303 ALA D 304 0 SHEET 2 AE8 2 GLU F 61 LYS F 62 -1 O LYS F 62 N GLY D 303 SHEET 1 AE9 3 ARG I 19 CYS I 22 0 SHEET 2 AE9 3 THR I 77 MET I 82 -1 O LEU I 80 N LEU I 20 SHEET 3 AE9 3 PHE I 67 ASP I 72 -1 N THR I 68 O GLN I 81 SHEET 1 AF1 5 THR I 57 TYR I 59 0 SHEET 2 AF1 5 LEU I 45 ILE I 51 -1 N GLY I 50 O TYR I 58 SHEET 3 AF1 5 MET I 34 GLN I 39 -1 N ARG I 38 O GLU I 46 SHEET 4 AF1 5 VAL I 89 LYS I 94 -1 O ALA I 93 N ASN I 35 SHEET 5 AF1 5 THR I 107 THR I 108 -1 O THR I 107 N TYR I 90 SHEET 1 AF2 4 MET K 4 GLN K 6 0 SHEET 2 AF2 4 VAL K 19 ALA K 25 -1 O ARG K 24 N THR K 5 SHEET 3 AF2 4 ASP K 70 ILE K 75 -1 O ILE K 75 N VAL K 19 SHEET 4 AF2 4 PHE K 62 SER K 67 -1 N SER K 65 O THR K 72 SHEET 1 AF3 6 SER K 10 SER K 12 0 SHEET 2 AF3 6 THR K 102 GLU K 105 1 O THR K 103 N LEU K 11 SHEET 3 AF3 6 THR K 85 GLN K 89 -1 N TYR K 86 O THR K 102 SHEET 4 AF3 6 ASN K 34 GLN K 38 -1 N TYR K 36 O TYR K 87 SHEET 5 AF3 6 LYS K 45 TYR K 49 -1 O LYS K 45 N GLN K 37 SHEET 6 AF3 6 SER K 53 LEU K 54 -1 O SER K 53 N TYR K 49 SSBOND 1 CYS A 14 CYS B 137 1555 1555 2.05 SSBOND 2 CYS A 52 CYS A 277 1555 1555 2.06 SSBOND 3 CYS A 64 CYS A 76 1555 1555 2.03 SSBOND 4 CYS A 97 CYS A 139 1555 1555 2.03 SSBOND 5 CYS A 281 CYS A 305 1555 1555 2.03 SSBOND 6 CYS B 144 CYS B 148 1555 1555 2.05 SSBOND 7 CYS H 22 CYS H 92 1555 1555 2.04 SSBOND 8 CYS H 98 CYS H 100C 1555 1555 2.03 SSBOND 9 CYS L 23 CYS L 88 1555 1555 2.04 SSBOND 10 CYS C 14 CYS E 137 1555 1555 2.05 SSBOND 11 CYS C 52 CYS C 277 1555 1555 2.06 SSBOND 12 CYS C 64 CYS C 76 1555 1555 2.03 SSBOND 13 CYS C 97 CYS C 139 1555 1555 2.03 SSBOND 14 CYS C 281 CYS C 305 1555 1555 2.03 SSBOND 15 CYS E 144 CYS E 148 1555 1555 2.05 SSBOND 16 CYS G 22 CYS G 92 1555 1555 2.04 SSBOND 17 CYS G 98 CYS G 100C 1555 1555 2.03 SSBOND 18 CYS J 23 CYS J 88 1555 1555 2.04 SSBOND 19 CYS D 14 CYS F 137 1555 1555 2.04 SSBOND 20 CYS D 52 CYS D 277 1555 1555 2.06 SSBOND 21 CYS D 64 CYS D 76 1555 1555 2.03 SSBOND 22 CYS D 97 CYS D 139 1555 1555 2.03 SSBOND 23 CYS D 281 CYS D 305 1555 1555 2.03 SSBOND 24 CYS F 144 CYS F 148 1555 1555 2.05 SSBOND 25 CYS I 22 CYS I 92 1555 1555 2.04 SSBOND 26 CYS I 98 CYS I 100C 1555 1555 2.03 SSBOND 27 CYS K 23 CYS K 88 1555 1555 2.04 LINK ND2 ASN A 22 C1 NAG A 401 1555 1555 1.44 LINK ND2 ASN A 38 C1 NAG M 1 1555 1555 1.44 LINK ND2 ASN A 45 C1 NAG A 405 1555 1555 1.46 LINK ND2 ASN A 63 C1 NAG N 1 1555 1555 1.44 LINK ND2 ASN A 126 C1 NAG A 404 1555 1555 1.44 LINK ND2 ASN A 133 C1 NAG A 402 1555 1555 1.44 LINK ND2 ASN A 158 C1 NAG A 403 1555 1555 1.44 LINK ND2 ASN A 165 C1 NAG Q 1 1555 1555 1.44 LINK ND2 ASN A 246 C1 NAG O 1 1555 1555 1.45 LINK ND2 ASN A 285 C1 NAG P 1 1555 1555 1.44 LINK ND2 ASN B 154 C1 NAG B 301 1555 1555 1.44 LINK ND2 ASN C 22 C1 NAG C 401 1555 1555 1.44 LINK ND2 ASN C 38 C1 NAG R 1 1555 1555 1.44 LINK ND2 ASN C 45 C1 NAG C 405 1555 1555 1.46 LINK ND2 ASN C 63 C1 NAG S 1 1555 1555 1.44 LINK ND2 ASN C 126 C1 NAG C 404 1555 1555 1.44 LINK ND2 ASN C 133 C1 NAG C 402 1555 1555 1.44 LINK ND2 ASN C 158 C1 NAG C 403 1555 1555 1.44 LINK ND2 ASN C 165 C1 NAG V 1 1555 1555 1.45 LINK ND2 ASN C 246 C1 NAG T 1 1555 1555 1.45 LINK ND2 ASN C 285 C1 NAG U 1 1555 1555 1.44 LINK ND2 ASN E 154 C1 NAG E 301 1555 1555 1.44 LINK ND2 ASN D 22 C1 NAG D 401 1555 1555 1.44 LINK ND2 ASN D 38 C1 NAG W 1 1555 1555 1.44 LINK ND2 ASN D 45 C1 NAG D 405 1555 1555 1.46 LINK ND2 ASN D 63 C1 NAG X 1 1555 1555 1.44 LINK ND2 ASN D 126 C1 NAG D 404 1555 1555 1.44 LINK ND2 ASN D 133 C1 NAG D 402 1555 1555 1.44 LINK ND2 ASN D 158 C1 NAG D 403 1555 1555 1.44 LINK ND2 ASN D 165 C1 NAG a 1 1555 1555 1.45 LINK ND2 ASN D 246 C1 NAG Y 1 1555 1555 1.45 LINK ND2 ASN D 285 C1 NAG Z 1 1555 1555 1.44 LINK ND2 ASN F 154 C1 NAG F 301 1555 1555 1.44 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 O6 NAG N 1 C1 FUC N 3 1555 1555 1.46 LINK O4 NAG O 1 C1 NAG O 2 1555 1555 1.45 LINK O4 NAG P 1 C1 NAG P 2 1555 1555 1.44 LINK O4 NAG P 2 C1 BMA P 3 1555 1555 1.46 LINK O4 NAG Q 1 C1 NAG Q 2 1555 1555 1.45 LINK O4 NAG Q 2 C1 BMA Q 3 1555 1555 1.45 LINK O4 NAG R 1 C1 NAG R 2 1555 1555 1.44 LINK O4 NAG S 1 C1 NAG S 2 1555 1555 1.44 LINK O6 NAG S 1 C1 FUC S 3 1555 1555 1.46 LINK O4 NAG T 1 C1 NAG T 2 1555 1555 1.45 LINK O4 NAG U 1 C1 NAG U 2 1555 1555 1.44 LINK O4 NAG U 2 C1 BMA U 3 1555 1555 1.46 LINK O4 NAG V 1 C1 NAG V 2 1555 1555 1.47 LINK O4 NAG V 2 C1 BMA V 3 1555 1555 1.45 LINK O4 NAG W 1 C1 NAG W 2 1555 1555 1.44 LINK O4 NAG X 1 C1 NAG X 2 1555 1555 1.44 LINK O6 NAG X 1 C1 FUC X 3 1555 1555 1.46 LINK O4 NAG Y 1 C1 NAG Y 2 1555 1555 1.45 LINK O4 NAG Z 1 C1 NAG Z 2 1555 1555 1.44 LINK O4 NAG Z 2 C1 BMA Z 3 1555 1555 1.45 LINK O4 NAG a 1 C1 NAG a 2 1555 1555 1.45 LINK O4 NAG a 2 C1 BMA a 3 1555 1555 1.45 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