HEADER VIRAL PROTEIN/IMMUNE SYSTEM 16-APR-25 9O8T TITLE CRYO-EM STRUCTURE OF NI04359_D30_240 FAB IN COMPLEX WITH INFLUENZA TITLE 2 VIRUS HEMAGGLUTININ FROM A/MICHIGAN/45/2015 (H1N1) 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/MICHIGAN/45/2015(H1N1)); SOURCE 3 ORGANISM_TAXID: 1777792; SOURCE 4 GENE: HA; SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS (A/MICHIGAN/45/2015(H1N1)); SOURCE 9 ORGANISM_TAXID: 1777792; SOURCE 10 GENE: HA; SOURCE 11 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 13 MOL_ID: 3; SOURCE 14 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 15 ORGANISM_TAXID: 9606; SOURCE 16 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 18 MOL_ID: 4; SOURCE 19 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 20 ORGANISM_TAXID: 9606; SOURCE 21 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 22 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS INFLUENZA, HEMAGGLUTININ, ANTIBODY COMPLEX, VIRAL PROTEIN-IMMUNE KEYWDS 2 SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR G.JO,A.B.WARD REVDAT 1 04-FEB-26 9O8T 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. 3.12 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) : 3.120 REMARK 3 NUMBER OF PARTICLES : 84345 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 9O8T 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_1000294518. 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/MICHIGAN/ REMARK 245 45/2015 (H1N1) REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 0.67 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 : 5879 REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : TFS GLACIOS REMARK 245 DETECTOR TYPE : FEI FALCON IV (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 700.00 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) : 4487.00 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 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 -6 REMARK 465 LYS A -5 REMARK 465 ALA A -4 REMARK 465 ILE A -3 REMARK 465 LEU A -2 REMARK 465 VAL A -1 REMARK 465 VAL A 0 REMARK 465 LEU A 1 REMARK 465 LEU A 2 REMARK 465 TYR A 3 REMARK 465 THR A 4 REMARK 465 PHE A 5 REMARK 465 THR A 6 REMARK 465 THR A 7 REMARK 465 ALA A 8 REMARK 465 ASN A 9 REMARK 465 ALA A 10 REMARK 465 ILE A 326 REMARK 465 GLN A 327 REMARK 465 SER A 328 REMARK 465 ARG A 329 REMARK 465 GLY B 1 REMARK 465 LEU B 2 REMARK 465 PHE B 3 REMARK 465 GLY B 4 REMARK 465 LYS B 172 REMARK 465 ILE B 173 REMARK 465 ASP B 174 REMARK 465 GLY B 175 REMARK 465 GLY B 176 REMARK 465 TYR B 177 REMARK 465 ILE B 178 REMARK 465 PRO B 179 REMARK 465 GLU B 180 REMARK 465 ALA B 181 REMARK 465 PRO B 182 REMARK 465 ARG B 183 REMARK 465 ASP B 184 REMARK 465 GLY B 185 REMARK 465 GLN B 186 REMARK 465 ALA B 187 REMARK 465 TYR B 188 REMARK 465 VAL B 189 REMARK 465 ARG B 190 REMARK 465 LYS B 191 REMARK 465 ASP B 192 REMARK 465 GLY B 193 REMARK 465 GLU B 194 REMARK 465 TRP B 195 REMARK 465 VAL B 196 REMARK 465 LEU B 197 REMARK 465 LEU B 198 REMARK 465 SER B 199 REMARK 465 THR B 200 REMARK 465 PHE B 201 REMARK 465 LEU B 202 REMARK 465 GLY B 203 REMARK 465 SER B 204 REMARK 465 GLU B 205 REMARK 465 ASN B 206 REMARK 465 LEU B 207 REMARK 465 TYR B 208 REMARK 465 PHE B 209 REMARK 465 GLN B 210 REMARK 465 GLY B 211 REMARK 465 SER B 212 REMARK 465 HIS B 213 REMARK 465 HIS B 214 REMARK 465 HIS B 215 REMARK 465 HIS B 216 REMARK 465 HIS B 217 REMARK 465 HIS B 218 REMARK 465 GLY B 219 REMARK 465 LEU B 220 REMARK 465 ASN B 221 REMARK 465 ASP B 222 REMARK 465 ILE B 223 REMARK 465 PHE B 224 REMARK 465 GLU B 225 REMARK 465 ALA B 226 REMARK 465 GLN B 227 REMARK 465 LYS B 228 REMARK 465 ILE B 229 REMARK 465 GLU B 230 REMARK 465 TRP B 231 REMARK 465 HIS B 232 REMARK 465 GLU B 233 REMARK 465 SER H 112 REMARK 465 SER H 113 REMARK 465 ILE L 106 REMARK 465 LYS L 107 REMARK 465 MET C -6 REMARK 465 LYS C -5 REMARK 465 ALA C -4 REMARK 465 ILE C -3 REMARK 465 LEU C -2 REMARK 465 VAL C -1 REMARK 465 VAL C 0 REMARK 465 LEU C 1 REMARK 465 LEU C 2 REMARK 465 TYR C 3 REMARK 465 THR C 4 REMARK 465 PHE C 5 REMARK 465 THR C 6 REMARK 465 THR C 7 REMARK 465 ALA C 8 REMARK 465 ASN C 9 REMARK 465 ALA C 10 REMARK 465 ILE C 326 REMARK 465 GLN C 327 REMARK 465 SER C 328 REMARK 465 ARG C 329 REMARK 465 GLY E 1 REMARK 465 LEU E 2 REMARK 465 PHE E 3 REMARK 465 GLY E 4 REMARK 465 LYS E 172 REMARK 465 ILE E 173 REMARK 465 ASP E 174 REMARK 465 GLY E 175 REMARK 465 GLY E 176 REMARK 465 TYR E 177 REMARK 465 ILE E 178 REMARK 465 PRO E 179 REMARK 465 GLU E 180 REMARK 465 ALA E 181 REMARK 465 PRO E 182 REMARK 465 ARG E 183 REMARK 465 ASP E 184 REMARK 465 GLY E 185 REMARK 465 GLN E 186 REMARK 465 ALA E 187 REMARK 465 TYR E 188 REMARK 465 VAL E 189 REMARK 465 ARG E 190 REMARK 465 LYS E 191 REMARK 465 ASP E 192 REMARK 465 GLY E 193 REMARK 465 GLU E 194 REMARK 465 TRP E 195 REMARK 465 VAL E 196 REMARK 465 LEU E 197 REMARK 465 LEU E 198 REMARK 465 SER E 199 REMARK 465 THR E 200 REMARK 465 PHE E 201 REMARK 465 LEU E 202 REMARK 465 GLY E 203 REMARK 465 SER E 204 REMARK 465 GLU E 205 REMARK 465 ASN E 206 REMARK 465 LEU E 207 REMARK 465 TYR E 208 REMARK 465 PHE E 209 REMARK 465 GLN E 210 REMARK 465 GLY E 211 REMARK 465 SER E 212 REMARK 465 HIS E 213 REMARK 465 HIS E 214 REMARK 465 HIS E 215 REMARK 465 HIS E 216 REMARK 465 HIS E 217 REMARK 465 HIS E 218 REMARK 465 GLY E 219 REMARK 465 LEU E 220 REMARK 465 ASN E 221 REMARK 465 ASP E 222 REMARK 465 ILE E 223 REMARK 465 PHE E 224 REMARK 465 GLU E 225 REMARK 465 ALA E 226 REMARK 465 GLN E 227 REMARK 465 LYS E 228 REMARK 465 ILE E 229 REMARK 465 GLU E 230 REMARK 465 TRP E 231 REMARK 465 HIS E 232 REMARK 465 GLU E 233 REMARK 465 SER G 112 REMARK 465 SER G 113 REMARK 465 ILE J 106 REMARK 465 LYS J 107 REMARK 465 MET D -6 REMARK 465 LYS D -5 REMARK 465 ALA D -4 REMARK 465 ILE D -3 REMARK 465 LEU D -2 REMARK 465 VAL D -1 REMARK 465 VAL D 0 REMARK 465 LEU D 1 REMARK 465 LEU D 2 REMARK 465 TYR D 3 REMARK 465 THR D 4 REMARK 465 PHE D 5 REMARK 465 THR D 6 REMARK 465 THR D 7 REMARK 465 ALA D 8 REMARK 465 ASN D 9 REMARK 465 ALA D 10 REMARK 465 ILE D 326 REMARK 465 GLN D 327 REMARK 465 SER D 328 REMARK 465 ARG D 329 REMARK 465 GLY F 1 REMARK 465 LEU F 2 REMARK 465 PHE F 3 REMARK 465 GLY F 4 REMARK 465 LYS F 172 REMARK 465 ILE F 173 REMARK 465 ASP F 174 REMARK 465 GLY F 175 REMARK 465 GLY F 176 REMARK 465 TYR F 177 REMARK 465 ILE F 178 REMARK 465 PRO F 179 REMARK 465 GLU F 180 REMARK 465 ALA F 181 REMARK 465 PRO F 182 REMARK 465 ARG F 183 REMARK 465 ASP F 184 REMARK 465 GLY F 185 REMARK 465 GLN F 186 REMARK 465 ALA F 187 REMARK 465 TYR F 188 REMARK 465 VAL F 189 REMARK 465 ARG F 190 REMARK 465 LYS F 191 REMARK 465 ASP F 192 REMARK 465 GLY F 193 REMARK 465 GLU F 194 REMARK 465 TRP F 195 REMARK 465 VAL F 196 REMARK 465 LEU F 197 REMARK 465 LEU F 198 REMARK 465 SER F 199 REMARK 465 THR F 200 REMARK 465 PHE F 201 REMARK 465 LEU F 202 REMARK 465 GLY F 203 REMARK 465 SER F 204 REMARK 465 GLU F 205 REMARK 465 ASN F 206 REMARK 465 LEU F 207 REMARK 465 TYR F 208 REMARK 465 PHE F 209 REMARK 465 GLN F 210 REMARK 465 GLY F 211 REMARK 465 SER F 212 REMARK 465 HIS F 213 REMARK 465 HIS F 214 REMARK 465 HIS F 215 REMARK 465 HIS F 216 REMARK 465 HIS F 217 REMARK 465 HIS F 218 REMARK 465 GLY F 219 REMARK 465 LEU F 220 REMARK 465 ASN F 221 REMARK 465 ASP F 222 REMARK 465 ILE F 223 REMARK 465 PHE F 224 REMARK 465 GLU F 225 REMARK 465 ALA F 226 REMARK 465 GLN F 227 REMARK 465 LYS F 228 REMARK 465 ILE F 229 REMARK 465 GLU F 230 REMARK 465 TRP F 231 REMARK 465 HIS F 232 REMARK 465 GLU F 233 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 NE2 GLN D 282 O GLY D 286 2.15 REMARK 500 NE2 GLN A 282 O GLY A 286 2.15 REMARK 500 NE2 GLN C 282 O GLY C 286 2.15 REMARK 500 O PHE I 29 NH2 ARG I 71 2.19 REMARK 500 O PHE G 29 NH2 ARG G 71 2.19 REMARK 500 O PHE H 29 NH2 ARG H 71 2.19 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 TYR H 100I CA - CB - CG ANGL. DEV. = 15.2 DEGREES REMARK 500 TYR H 100I CB - CG - CD1 ANGL. DEV. = 4.6 DEGREES REMARK 500 TYR G 100I CA - CB - CG ANGL. DEV. = 15.2 DEGREES REMARK 500 TYR G 100I CB - CG - CD1 ANGL. DEV. = 4.6 DEGREES REMARK 500 TYR I 100I CA - CB - CG ANGL. DEV. = 15.2 DEGREES REMARK 500 TYR I 100I CB - CG - CD1 ANGL. DEV. = 4.6 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 ARG A 55 -132.23 58.14 REMARK 500 PHE A 124 76.93 53.87 REMARK 500 ASN A 165 37.73 -140.61 REMARK 500 LYS A 212 74.12 -119.71 REMARK 500 CYS A 277 137.14 -170.16 REMARK 500 THR A 290 35.89 71.58 REMARK 500 PRO B 160 49.88 -80.26 REMARK 500 LYS B 161 -37.16 -130.25 REMARK 500 PHE H 29 -12.60 73.29 REMARK 500 SER L 30 -121.21 56.23 REMARK 500 ALA L 51 -9.21 72.54 REMARK 500 SER L 91 61.66 -100.87 REMARK 500 ARG C 55 -132.17 58.25 REMARK 500 PHE C 124 76.90 53.84 REMARK 500 ASN C 165 37.69 -140.64 REMARK 500 LYS C 212 74.06 -119.61 REMARK 500 CYS C 277 137.11 -170.20 REMARK 500 THR C 290 35.84 71.62 REMARK 500 PRO E 160 49.93 -80.30 REMARK 500 LYS E 161 -37.20 -130.28 REMARK 500 PHE G 29 -12.60 73.33 REMARK 500 SER J 30 -121.26 56.24 REMARK 500 ALA J 51 -9.18 72.50 REMARK 500 SER J 91 61.59 -100.75 REMARK 500 ARG D 55 -132.23 58.24 REMARK 500 PHE D 124 76.90 53.86 REMARK 500 ASN D 165 37.80 -140.71 REMARK 500 LYS D 212 74.09 -119.65 REMARK 500 CYS D 277 137.15 -170.15 REMARK 500 THR D 290 35.89 71.59 REMARK 500 PRO F 160 49.90 -80.21 REMARK 500 LYS F 161 -37.17 -130.28 REMARK 500 PHE I 29 -12.62 73.30 REMARK 500 SER K 30 -121.24 56.21 REMARK 500 ALA K 51 -9.30 72.52 REMARK 500 SER K 91 61.60 -100.80 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 55 0.08 SIDE CHAIN REMARK 500 ARG A 224 0.24 SIDE CHAIN REMARK 500 ARG H 38 0.08 SIDE CHAIN REMARK 500 ARG C 55 0.08 SIDE CHAIN REMARK 500 ARG C 224 0.24 SIDE CHAIN REMARK 500 ARG G 38 0.08 SIDE CHAIN REMARK 500 ARG D 55 0.08 SIDE CHAIN REMARK 500 ARG D 224 0.24 SIDE CHAIN REMARK 500 ARG I 38 0.08 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-70236 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF NI04359_D30_240 FAB IN COMPLEX WITH INFLUENZA REMARK 900 VIRUS HEMAGGLUTININ FROM A/MICHIGAN/45/2015 (H1N1) DBREF1 9O8T A -6 329 UNP A0A1J0CXU0_9INFA DBREF2 9O8T A A0A1J0CXU0 1 344 DBREF1 9O8T B 1 174 UNP A0A1J0CXU0_9INFA DBREF2 9O8T B A0A1J0CXU0 345 518 DBREF 9O8T H 1 113 PDB 9O8T 9O8T 1 113 DBREF 9O8T L 1 107 PDB 9O8T 9O8T 1 107 DBREF1 9O8T C -6 329 UNP A0A1J0CXU0_9INFA DBREF2 9O8T C A0A1J0CXU0 1 344 DBREF1 9O8T E 1 174 UNP A0A1J0CXU0_9INFA DBREF2 9O8T E A0A1J0CXU0 345 518 DBREF 9O8T G 1 113 PDB 9O8T 9O8T 1 113 DBREF 9O8T J 1 107 PDB 9O8T 9O8T 1 107 DBREF1 9O8T D -6 329 UNP A0A1J0CXU0_9INFA DBREF2 9O8T D A0A1J0CXU0 1 344 DBREF1 9O8T F 1 174 UNP A0A1J0CXU0_9INFA DBREF2 9O8T F A0A1J0CXU0 345 518 DBREF 9O8T I 1 113 PDB 9O8T 9O8T 1 113 DBREF 9O8T K 1 107 PDB 9O8T 9O8T 1 107 SEQADV 9O8T GLY B 175 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T GLY B 176 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T TYR B 177 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T ILE B 178 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T PRO B 179 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T GLU B 180 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T ALA B 181 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T PRO B 182 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T ARG B 183 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T ASP B 184 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T GLY B 185 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T GLN B 186 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T ALA B 187 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T TYR B 188 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T VAL B 189 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T ARG B 190 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T LYS B 191 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T ASP B 192 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T GLY B 193 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T GLU B 194 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T TRP B 195 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T VAL B 196 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T LEU B 197 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T LEU B 198 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T SER B 199 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T THR B 200 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T PHE B 201 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T LEU B 202 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T GLY B 203 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T SER B 204 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T GLU B 205 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T ASN B 206 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T LEU B 207 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T TYR B 208 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T PHE B 209 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T GLN B 210 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T GLY B 211 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T SER B 212 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T HIS B 213 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T HIS B 214 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T HIS B 215 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T HIS B 216 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T HIS B 217 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T HIS B 218 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T GLY B 219 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T LEU B 220 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T ASN B 221 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T ASP B 222 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T ILE B 223 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T PHE B 224 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T GLU B 225 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T ALA B 226 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T GLN B 227 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T LYS B 228 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T ILE B 229 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T GLU B 230 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T TRP B 231 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T HIS B 232 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T GLU B 233 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T GLY E 175 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T GLY E 176 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T TYR E 177 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T ILE E 178 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T PRO E 179 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T GLU E 180 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T ALA E 181 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T PRO E 182 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T ARG E 183 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T ASP E 184 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T GLY E 185 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T GLN E 186 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T ALA E 187 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T TYR E 188 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T VAL E 189 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T ARG E 190 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T LYS E 191 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T ASP E 192 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T GLY E 193 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T GLU E 194 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T TRP E 195 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T VAL E 196 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T LEU E 197 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T LEU E 198 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T SER E 199 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T THR E 200 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T PHE E 201 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T LEU E 202 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T GLY E 203 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T SER E 204 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T GLU E 205 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T ASN E 206 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T LEU E 207 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T TYR E 208 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T PHE E 209 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T GLN E 210 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T GLY E 211 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T SER E 212 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T HIS E 213 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T HIS E 214 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T HIS E 215 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T HIS E 216 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T HIS E 217 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T HIS E 218 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T GLY E 219 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T LEU E 220 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T ASN E 221 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T ASP E 222 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T ILE E 223 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T PHE E 224 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T GLU E 225 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T ALA E 226 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T GLN E 227 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T LYS E 228 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T ILE E 229 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T GLU E 230 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T TRP E 231 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T HIS E 232 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T GLU E 233 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T GLY F 175 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T GLY F 176 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T TYR F 177 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T ILE F 178 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T PRO F 179 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T GLU F 180 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T ALA F 181 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T PRO F 182 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T ARG F 183 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T ASP F 184 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T GLY F 185 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T GLN F 186 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T ALA F 187 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T TYR F 188 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T VAL F 189 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T ARG F 190 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T LYS F 191 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T ASP F 192 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T GLY F 193 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T GLU F 194 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T TRP F 195 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T VAL F 196 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T LEU F 197 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T LEU F 198 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T SER F 199 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T THR F 200 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T PHE F 201 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T LEU F 202 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T GLY F 203 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T SER F 204 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T GLU F 205 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T ASN F 206 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T LEU F 207 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T TYR F 208 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T PHE F 209 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T GLN F 210 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T GLY F 211 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T SER F 212 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T HIS F 213 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T HIS F 214 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T HIS F 215 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T HIS F 216 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T HIS F 217 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T HIS F 218 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T GLY F 219 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T LEU F 220 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T ASN F 221 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T ASP F 222 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T ILE F 223 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T PHE F 224 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T GLU F 225 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T ALA F 226 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T GLN F 227 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T LYS F 228 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T ILE F 229 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T GLU F 230 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T TRP F 231 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T HIS F 232 UNP A0A1J0CXU EXPRESSION TAG SEQADV 9O8T GLU F 233 UNP A0A1J0CXU EXPRESSION TAG SEQRES 1 A 344 MET LYS ALA ILE LEU VAL VAL LEU LEU TYR THR PHE THR SEQRES 2 A 344 THR ALA ASN ALA ASP THR LEU CYS ILE GLY TYR HIS ALA SEQRES 3 A 344 ASN ASN SER THR ASP THR VAL ASP THR VAL LEU GLU LYS SEQRES 4 A 344 ASN VAL THR VAL THR HIS SER VAL ASN LEU LEU GLU ASP SEQRES 5 A 344 LYS HIS ASN GLY LYS LEU CYS LYS LEU ARG GLY VAL ALA SEQRES 6 A 344 PRO LEU HIS LEU GLY LYS CYS ASN ILE ALA GLY TRP ILE SEQRES 7 A 344 LEU GLY ASN PRO GLU CYS GLU SER LEU SER THR ALA SER SEQRES 8 A 344 SER TRP SER TYR ILE VAL GLU THR SER ASN SER ASP ASN SEQRES 9 A 344 GLY THR CYS TYR PRO GLY ASP PHE ILE ASN TYR GLU GLU SEQRES 10 A 344 LEU ARG GLU GLN LEU SER SER VAL SER SER PHE GLU ARG SEQRES 11 A 344 PHE GLU ILE PHE PRO LYS THR SER SER TRP PRO ASN HIS SEQRES 12 A 344 ASP SER ASN LYS GLY VAL THR ALA ALA CYS PRO HIS ALA SEQRES 13 A 344 GLY ALA LYS SER PHE TYR LYS ASN LEU ILE TRP LEU VAL SEQRES 14 A 344 LYS LYS GLY ASN SER TYR PRO LYS LEU ASN GLN SER TYR SEQRES 15 A 344 ILE ASN ASP LYS GLY LYS GLU VAL LEU VAL LEU TRP GLY SEQRES 16 A 344 ILE HIS HIS PRO SER THR THR ALA ASP GLN GLN SER LEU SEQRES 17 A 344 TYR GLN ASN ALA ASP ALA TYR VAL PHE VAL GLY THR SER SEQRES 18 A 344 ARG TYR SER LYS LYS PHE LYS PRO GLU ILE ALA THR ARG SEQRES 19 A 344 PRO LYS VAL ARG ASP GLN GLU GLY ARG MET ASN TYR TYR SEQRES 20 A 344 TRP THR LEU VAL GLU PRO GLY ASP LYS ILE THR PHE GLU SEQRES 21 A 344 ALA THR GLY ASN LEU VAL VAL PRO ARG TYR ALA PHE THR SEQRES 22 A 344 MET GLU ARG ASN ALA GLY SER GLY ILE ILE ILE SER ASP SEQRES 23 A 344 THR PRO VAL HIS ASP CYS ASN THR THR CYS GLN THR PRO SEQRES 24 A 344 GLU GLY ALA ILE ASN THR SER LEU PRO PHE GLN ASN ILE SEQRES 25 A 344 HIS PRO ILE THR ILE GLY LYS CYS PRO LYS TYR VAL LYS SEQRES 26 A 344 SER THR LYS LEU ARG LEU ALA THR GLY LEU ARG ASN VAL SEQRES 27 A 344 PRO SER ILE GLN SER ARG SEQRES 1 B 233 GLY LEU PHE GLY ALA ILE ALA GLY PHE ILE GLU GLY GLY SEQRES 2 B 233 TRP THR GLY MET VAL ASP GLY TRP TYR GLY TYR HIS HIS SEQRES 3 B 233 GLN ASN GLU GLN GLY SER GLY TYR ALA ALA ASP LEU LYS SEQRES 4 B 233 SER THR GLN ASN ALA ILE ASP LYS ILE THR ASN LYS VAL SEQRES 5 B 233 ASN SER VAL ILE GLU LYS MET ASN THR GLN PHE THR ALA SEQRES 6 B 233 VAL GLY LYS GLU PHE ASN HIS LEU GLU LYS ARG ILE GLU SEQRES 7 B 233 ASN LEU ASN LYS LYS VAL ASP ASP GLY PHE LEU ASP ILE SEQRES 8 B 233 TRP THR TYR ASN ALA GLU LEU LEU VAL LEU LEU GLU ASN SEQRES 9 B 233 GLU ARG THR LEU ASP TYR HIS ASP SER ASN VAL LYS ASN SEQRES 10 B 233 LEU TYR GLU LYS VAL ARG ASN GLN LEU LYS ASN ASN ALA SEQRES 11 B 233 LYS GLU ILE GLY ASN GLY CYS PHE GLU PHE TYR HIS LYS SEQRES 12 B 233 CYS ASP ASN THR CYS MET GLU SER VAL LYS ASN GLY THR SEQRES 13 B 233 TYR ASP TYR PRO LYS TYR SER GLU GLU ALA LYS LEU ASN SEQRES 14 B 233 ARG GLU LYS ILE ASP GLY GLY TYR ILE PRO GLU ALA PRO SEQRES 15 B 233 ARG ASP GLY GLN ALA TYR VAL ARG LYS ASP GLY GLU TRP SEQRES 16 B 233 VAL LEU LEU SER THR PHE LEU GLY SER GLU ASN LEU TYR SEQRES 17 B 233 PHE GLN GLY SER HIS HIS HIS HIS HIS HIS GLY LEU ASN SEQRES 18 B 233 ASP ILE PHE GLU ALA GLN LYS ILE GLU TRP HIS GLU 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 344 MET LYS ALA ILE LEU VAL VAL LEU LEU TYR THR PHE THR SEQRES 2 C 344 THR ALA ASN ALA ASP THR LEU CYS ILE GLY TYR HIS ALA SEQRES 3 C 344 ASN ASN SER THR ASP THR VAL ASP THR VAL LEU GLU LYS SEQRES 4 C 344 ASN VAL THR VAL THR HIS SER VAL ASN LEU LEU GLU ASP SEQRES 5 C 344 LYS HIS ASN GLY LYS LEU CYS LYS LEU ARG GLY VAL ALA SEQRES 6 C 344 PRO LEU HIS LEU GLY LYS CYS ASN ILE ALA GLY TRP ILE SEQRES 7 C 344 LEU GLY ASN PRO GLU CYS GLU SER LEU SER THR ALA SER SEQRES 8 C 344 SER TRP SER TYR ILE VAL GLU THR SER ASN SER ASP ASN SEQRES 9 C 344 GLY THR CYS TYR PRO GLY ASP PHE ILE ASN TYR GLU GLU SEQRES 10 C 344 LEU ARG GLU GLN LEU SER SER VAL SER SER PHE GLU ARG SEQRES 11 C 344 PHE GLU ILE PHE PRO LYS THR SER SER TRP PRO ASN HIS SEQRES 12 C 344 ASP SER ASN LYS GLY VAL THR ALA ALA CYS PRO HIS ALA SEQRES 13 C 344 GLY ALA LYS SER PHE TYR LYS ASN LEU ILE TRP LEU VAL SEQRES 14 C 344 LYS LYS GLY ASN SER TYR PRO LYS LEU ASN GLN SER TYR SEQRES 15 C 344 ILE ASN ASP LYS GLY LYS GLU VAL LEU VAL LEU TRP GLY SEQRES 16 C 344 ILE HIS HIS PRO SER THR THR ALA ASP GLN GLN SER LEU SEQRES 17 C 344 TYR GLN ASN ALA ASP ALA TYR VAL PHE VAL GLY THR SER SEQRES 18 C 344 ARG TYR SER LYS LYS PHE LYS PRO GLU ILE ALA THR ARG SEQRES 19 C 344 PRO LYS VAL ARG ASP GLN GLU GLY ARG MET ASN TYR TYR SEQRES 20 C 344 TRP THR LEU VAL GLU PRO GLY ASP LYS ILE THR PHE GLU SEQRES 21 C 344 ALA THR GLY ASN LEU VAL VAL PRO ARG TYR ALA PHE THR SEQRES 22 C 344 MET GLU ARG ASN ALA GLY SER GLY ILE ILE ILE SER ASP SEQRES 23 C 344 THR PRO VAL HIS ASP CYS ASN THR THR CYS GLN THR PRO SEQRES 24 C 344 GLU GLY ALA ILE ASN THR SER LEU PRO PHE GLN ASN ILE SEQRES 25 C 344 HIS PRO ILE THR ILE GLY LYS CYS PRO LYS TYR VAL LYS SEQRES 26 C 344 SER THR LYS LEU ARG LEU ALA THR GLY LEU ARG ASN VAL SEQRES 27 C 344 PRO SER ILE GLN SER ARG SEQRES 1 E 233 GLY LEU PHE GLY ALA ILE ALA GLY PHE ILE GLU GLY GLY SEQRES 2 E 233 TRP THR GLY MET VAL ASP GLY TRP TYR GLY TYR HIS HIS SEQRES 3 E 233 GLN ASN GLU GLN GLY SER GLY TYR ALA ALA ASP LEU LYS SEQRES 4 E 233 SER THR GLN ASN ALA ILE ASP LYS ILE THR ASN LYS VAL SEQRES 5 E 233 ASN SER VAL ILE GLU LYS MET ASN THR GLN PHE THR ALA SEQRES 6 E 233 VAL GLY LYS GLU PHE ASN HIS LEU GLU LYS ARG ILE GLU SEQRES 7 E 233 ASN LEU ASN LYS LYS VAL ASP ASP GLY PHE LEU ASP ILE SEQRES 8 E 233 TRP THR TYR ASN ALA GLU LEU LEU VAL LEU LEU GLU ASN SEQRES 9 E 233 GLU ARG THR LEU ASP TYR HIS ASP SER ASN VAL LYS ASN SEQRES 10 E 233 LEU TYR GLU LYS VAL ARG ASN GLN LEU LYS ASN ASN ALA SEQRES 11 E 233 LYS GLU ILE GLY ASN GLY CYS PHE GLU PHE TYR HIS LYS SEQRES 12 E 233 CYS ASP ASN THR CYS MET GLU SER VAL LYS ASN GLY THR SEQRES 13 E 233 TYR ASP TYR PRO LYS TYR SER GLU GLU ALA LYS LEU ASN SEQRES 14 E 233 ARG GLU LYS ILE ASP GLY GLY TYR ILE PRO GLU ALA PRO SEQRES 15 E 233 ARG ASP GLY GLN ALA TYR VAL ARG LYS ASP GLY GLU TRP SEQRES 16 E 233 VAL LEU LEU SER THR PHE LEU GLY SER GLU ASN LEU TYR SEQRES 17 E 233 PHE GLN GLY SER HIS HIS HIS HIS HIS HIS GLY LEU ASN SEQRES 18 E 233 ASP ILE PHE GLU ALA GLN LYS ILE GLU TRP HIS GLU 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 344 MET LYS ALA ILE LEU VAL VAL LEU LEU TYR THR PHE THR SEQRES 2 D 344 THR ALA ASN ALA ASP THR LEU CYS ILE GLY TYR HIS ALA SEQRES 3 D 344 ASN ASN SER THR ASP THR VAL ASP THR VAL LEU GLU LYS SEQRES 4 D 344 ASN VAL THR VAL THR HIS SER VAL ASN LEU LEU GLU ASP SEQRES 5 D 344 LYS HIS ASN GLY LYS LEU CYS LYS LEU ARG GLY VAL ALA SEQRES 6 D 344 PRO LEU HIS LEU GLY LYS CYS ASN ILE ALA GLY TRP ILE SEQRES 7 D 344 LEU GLY ASN PRO GLU CYS GLU SER LEU SER THR ALA SER SEQRES 8 D 344 SER TRP SER TYR ILE VAL GLU THR SER ASN SER ASP ASN SEQRES 9 D 344 GLY THR CYS TYR PRO GLY ASP PHE ILE ASN TYR GLU GLU SEQRES 10 D 344 LEU ARG GLU GLN LEU SER SER VAL SER SER PHE GLU ARG SEQRES 11 D 344 PHE GLU ILE PHE PRO LYS THR SER SER TRP PRO ASN HIS SEQRES 12 D 344 ASP SER ASN LYS GLY VAL THR ALA ALA CYS PRO HIS ALA SEQRES 13 D 344 GLY ALA LYS SER PHE TYR LYS ASN LEU ILE TRP LEU VAL SEQRES 14 D 344 LYS LYS GLY ASN SER TYR PRO LYS LEU ASN GLN SER TYR SEQRES 15 D 344 ILE ASN ASP LYS GLY LYS GLU VAL LEU VAL LEU TRP GLY SEQRES 16 D 344 ILE HIS HIS PRO SER THR THR ALA ASP GLN GLN SER LEU SEQRES 17 D 344 TYR GLN ASN ALA ASP ALA TYR VAL PHE VAL GLY THR SER SEQRES 18 D 344 ARG TYR SER LYS LYS PHE LYS PRO GLU ILE ALA THR ARG SEQRES 19 D 344 PRO LYS VAL ARG ASP GLN GLU GLY ARG MET ASN TYR TYR SEQRES 20 D 344 TRP THR LEU VAL GLU PRO GLY ASP LYS ILE THR PHE GLU SEQRES 21 D 344 ALA THR GLY ASN LEU VAL VAL PRO ARG TYR ALA PHE THR SEQRES 22 D 344 MET GLU ARG ASN ALA GLY SER GLY ILE ILE ILE SER ASP SEQRES 23 D 344 THR PRO VAL HIS ASP CYS ASN THR THR CYS GLN THR PRO SEQRES 24 D 344 GLU GLY ALA ILE ASN THR SER LEU PRO PHE GLN ASN ILE SEQRES 25 D 344 HIS PRO ILE THR ILE GLY LYS CYS PRO LYS TYR VAL LYS SEQRES 26 D 344 SER THR LYS LEU ARG LEU ALA THR GLY LEU ARG ASN VAL SEQRES 27 D 344 PRO SER ILE GLN SER ARG SEQRES 1 F 233 GLY LEU PHE GLY ALA ILE ALA GLY PHE ILE GLU GLY GLY SEQRES 2 F 233 TRP THR GLY MET VAL ASP GLY TRP TYR GLY TYR HIS HIS SEQRES 3 F 233 GLN ASN GLU GLN GLY SER GLY TYR ALA ALA ASP LEU LYS SEQRES 4 F 233 SER THR GLN ASN ALA ILE ASP LYS ILE THR ASN LYS VAL SEQRES 5 F 233 ASN SER VAL ILE GLU LYS MET ASN THR GLN PHE THR ALA SEQRES 6 F 233 VAL GLY LYS GLU PHE ASN HIS LEU GLU LYS ARG ILE GLU SEQRES 7 F 233 ASN LEU ASN LYS LYS VAL ASP ASP GLY PHE LEU ASP ILE SEQRES 8 F 233 TRP THR TYR ASN ALA GLU LEU LEU VAL LEU LEU GLU ASN SEQRES 9 F 233 GLU ARG THR LEU ASP TYR HIS ASP SER ASN VAL LYS ASN SEQRES 10 F 233 LEU TYR GLU LYS VAL ARG ASN GLN LEU LYS ASN ASN ALA SEQRES 11 F 233 LYS GLU ILE GLY ASN GLY CYS PHE GLU PHE TYR HIS LYS SEQRES 12 F 233 CYS ASP ASN THR CYS MET GLU SER VAL LYS ASN GLY THR SEQRES 13 F 233 TYR ASP TYR PRO LYS TYR SER GLU GLU ALA LYS LEU ASN SEQRES 14 F 233 ARG GLU LYS ILE ASP GLY GLY TYR ILE PRO GLU ALA PRO SEQRES 15 F 233 ARG ASP GLY GLN ALA TYR VAL ARG LYS ASP GLY GLU TRP SEQRES 16 F 233 VAL LEU LEU SER THR PHE LEU GLY SER GLU ASN LEU TYR SEQRES 17 F 233 PHE GLN GLY SER HIS HIS HIS HIS HIS HIS GLY LEU ASN SEQRES 18 F 233 ASP ILE PHE GLU ALA GLN LYS ILE GLU TRP HIS GLU 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 NAG O 1 14 HET NAG O 2 14 HET NAG A 401 14 HET NAG A 402 14 HET NAG B 301 14 HET NAG C 401 14 HET NAG C 402 14 HET NAG E 301 14 HET NAG D 401 14 HET NAG D 402 14 HET NAG F 301 14 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE 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 FORMUL 13 NAG 15(C8 H15 N O6) HELIX 1 AA1 ASN A 65 GLY A 72 1 8 HELIX 2 AA2 ASN A 104 LEU A 112 1 9 HELIX 3 AA3 PRO A 125 TRP A 127 1 6 HELIX 4 AA4 THR A 187 TYR A 195 1 9 HELIX 5 AA5 ASP B 37 LYS B 58 1 22 HELIX 6 AA6 ASN B 71 LEU B 73 5 3 HELIX 7 AA7 GLU B 74 LEU B 126 1 53 HELIX 8 AA8 ASP B 145 GLY B 155 1 11 HELIX 9 AA9 ASP B 158 LYS B 161 5 4 HELIX 10 AB1 TYR B 162 ASN B 169 1 8 HELIX 11 AB2 ASP H 61 LYS H 64 5 4 HELIX 12 AB3 GLN L 79 PHE L 83 5 5 HELIX 13 AB4 ASN C 65 GLY C 72 1 8 HELIX 14 AB5 ASN C 104 LEU C 112 1 9 HELIX 15 AB6 PRO C 125 TRP C 127 1 6 HELIX 16 AB7 THR C 187 TYR C 195 1 9 HELIX 17 AB8 ASP E 37 LYS E 58 1 22 HELIX 18 AB9 ASN E 71 LEU E 73 5 3 HELIX 19 AC1 GLU E 74 LEU E 126 1 53 HELIX 20 AC2 ASP E 145 GLY E 155 1 11 HELIX 21 AC3 ASP E 158 LYS E 161 5 4 HELIX 22 AC4 TYR E 162 ASN E 169 1 8 HELIX 23 AC5 ASP G 61 LYS G 64 5 4 HELIX 24 AC6 GLN J 79 PHE J 83 5 5 HELIX 25 AC7 ASN D 65 GLY D 72 1 8 HELIX 26 AC8 ASN D 104 LEU D 112 1 9 HELIX 27 AC9 PRO D 125 TRP D 127 1 6 HELIX 28 AD1 THR D 187 TYR D 195 1 9 HELIX 29 AD2 ASP F 37 LYS F 58 1 22 HELIX 30 AD3 ASN F 71 LEU F 73 5 3 HELIX 31 AD4 GLU F 74 LEU F 126 1 53 HELIX 32 AD5 ASP F 145 GLY F 155 1 11 HELIX 33 AD6 ASP F 158 LYS F 161 5 4 HELIX 34 AD7 TYR F 162 ASN F 169 1 8 HELIX 35 AD8 ASP I 61 LYS I 64 5 4 HELIX 36 AD9 GLN K 79 PHE K 83 5 5 SHEET 1 AA1 3 THR A 12 TYR A 17 0 SHEET 2 AA1 3 TYR B 22 GLN B 27 -1 O HIS B 25 N CYS A 14 SHEET 3 AA1 3 SER B 32 ALA B 36 -1 O ALA B 35 N TYR B 24 SHEET 1 AA2 2 ASP A 24 VAL A 26 0 SHEET 2 AA2 2 VAL A 34 VAL A 36 -1 O VAL A 34 N VAL A 26 SHEET 1 AA3 2 SER A 39 ASN A 41 0 SHEET 2 AA3 2 ARG A 315 ALA A 317 -1 O LEU A 316 N VAL A 40 SHEET 1 AA4 3 LEU A 43 GLU A 44 0 SHEET 2 AA4 3 PHE A 294 GLN A 295 1 O PHE A 294 N GLU A 44 SHEET 3 AA4 3 LYS A 307 TYR A 308 1 O LYS A 307 N GLN A 295 SHEET 1 AA5 2 LEU A 51 LEU A 54 0 SHEET 2 AA5 2 VAL A 274 THR A 279 1 O CYS A 277 N LYS A 53 SHEET 1 AA6 3 LEU A 59 GLY A 62 0 SHEET 2 AA6 3 ILE A 87 GLU A 89 1 O VAL A 88 N LEU A 59 SHEET 3 AA6 3 ILE A 267 ILE A 268 1 O ILE A 268 N GLU A 89 SHEET 1 AA7 4 GLU A 119 PHE A 121 0 SHEET 2 AA7 4 ALA A 257 MET A 260 -1 O ALA A 257 N PHE A 121 SHEET 3 AA7 4 GLU A 175 HIS A 184 -1 N LEU A 177 O PHE A 258 SHEET 4 AA7 4 ARG A 229 VAL A 237 -1 O ARG A 229 N HIS A 184 SHEET 1 AA8 2 THR A 136 HIS A 141 0 SHEET 2 AA8 2 ALA A 144 SER A 146 -1 O ALA A 144 N HIS A 141 SHEET 1 AA9 2 LEU A 151 TRP A 153 0 SHEET 2 AA9 2 VAL A 252 PRO A 254 -1 O VAL A 253 N ILE A 152 SHEET 1 AB1 4 SER A 167 ILE A 169 0 SHEET 2 AB1 4 LYS A 242 ALA A 247 -1 O ILE A 243 N TYR A 168 SHEET 3 AB1 4 VAL A 202 THR A 206 -1 N PHE A 203 O GLU A 246 SHEET 4 AB1 4 TYR A 209 LYS A 211 -1 O TYR A 209 N THR A 206 SHEET 1 AB2 3 CYS A 281 GLN A 282 0 SHEET 2 AB2 3 ILE A 302 GLY A 303 -1 O ILE A 302 N GLN A 282 SHEET 3 AB2 3 THR B 64 ALA B 65 -1 O THR B 64 N GLY A 303 SHEET 1 AB3 2 ALA B 130 GLU B 132 0 SHEET 2 AB3 2 PHE B 138 PHE B 140 -1 O GLU B 139 N LYS B 131 SHEET 1 AB4 4 GLN H 3 SER H 7 0 SHEET 2 AB4 4 SER H 17 SER H 25 -1 O SER H 21 N SER H 7 SHEET 3 AB4 4 THR H 77 ASN H 82A-1 O LEU H 80 N LEU H 20 SHEET 4 AB4 4 PHE H 67 ASP H 72 -1 N ASP H 72 O THR H 77 SHEET 1 AB5 6 GLY H 10 LEU H 11 0 SHEET 2 AB5 6 THR H 107 THR H 110 1 O THR H 110 N GLY H 10 SHEET 3 AB5 6 VAL H 89 ASP H 95 -1 N TYR H 90 O THR H 107 SHEET 4 AB5 6 MET H 34 GLN H 39 -1 N GLN H 39 O VAL H 89 SHEET 5 AB5 6 LEU H 45 ILE H 51 -1 O ILE H 51 N MET H 34 SHEET 6 AB5 6 THR H 57 TYR H 59 -1 O TYR H 58 N GLY H 50 SHEET 1 AB6 4 GLY H 10 LEU H 11 0 SHEET 2 AB6 4 THR H 107 THR H 110 1 O THR H 110 N GLY H 10 SHEET 3 AB6 4 VAL H 89 ASP H 95 -1 N TYR H 90 O THR H 107 SHEET 4 AB6 4 MET H 100M TRP H 103 -1 O VAL H 102 N LYS H 94 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 TYR L 87 -1 N TYR L 86 O THR L 102 SHEET 4 AB7 6 TRP L 35 GLN L 38 -1 N GLN L 38 O THR L 85 SHEET 5 AB7 6 LYS L 45 TYR L 49 -1 O LEU L 47 N TRP L 35 SHEET 6 AB7 6 SER L 53 LEU L 54 -1 O SER L 53 N TYR L 49 SHEET 1 AB8 3 VAL L 19 ARG L 24 0 SHEET 2 AB8 3 ASP L 70 ILE L 75 -1 O PHE L 71 N CYS L 23 SHEET 3 AB8 3 PHE L 62 SER L 67 -1 N SER L 65 O THR L 72 SHEET 1 AB9 3 THR C 12 TYR C 17 0 SHEET 2 AB9 3 TYR E 22 GLN E 27 -1 O HIS E 25 N CYS C 14 SHEET 3 AB9 3 SER E 32 ALA E 36 -1 O ALA E 35 N TYR E 24 SHEET 1 AC1 2 ASP C 24 VAL C 26 0 SHEET 2 AC1 2 VAL C 34 VAL C 36 -1 O VAL C 34 N VAL C 26 SHEET 1 AC2 2 SER C 39 ASN C 41 0 SHEET 2 AC2 2 ARG C 315 ALA C 317 -1 O LEU C 316 N VAL C 40 SHEET 1 AC3 3 LEU C 43 GLU C 44 0 SHEET 2 AC3 3 PHE C 294 GLN C 295 1 O PHE C 294 N GLU C 44 SHEET 3 AC3 3 LYS C 307 TYR C 308 1 O LYS C 307 N GLN C 295 SHEET 1 AC4 2 LEU C 51 LEU C 54 0 SHEET 2 AC4 2 VAL C 274 THR C 279 1 O CYS C 277 N LYS C 53 SHEET 1 AC5 3 LEU C 59 GLY C 62 0 SHEET 2 AC5 3 ILE C 87 GLU C 89 1 O VAL C 88 N LEU C 59 SHEET 3 AC5 3 ILE C 267 ILE C 268 1 O ILE C 268 N GLU C 89 SHEET 1 AC6 4 GLU C 119 PHE C 121 0 SHEET 2 AC6 4 ALA C 257 MET C 260 -1 O ALA C 257 N PHE C 121 SHEET 3 AC6 4 GLU C 175 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 THR C 136 HIS C 141 0 SHEET 2 AC7 2 ALA C 144 SER C 146 -1 O ALA C 144 N HIS C 141 SHEET 1 AC8 2 LEU C 151 TRP C 153 0 SHEET 2 AC8 2 VAL C 252 PRO C 254 -1 O VAL C 253 N ILE C 152 SHEET 1 AC9 4 SER C 167 ILE C 169 0 SHEET 2 AC9 4 LYS C 242 ALA C 247 -1 O ILE C 243 N TYR C 168 SHEET 3 AC9 4 VAL C 202 THR C 206 -1 N PHE C 203 O GLU C 246 SHEET 4 AC9 4 TYR C 209 LYS C 211 -1 O TYR C 209 N THR C 206 SHEET 1 AD1 3 CYS C 281 GLN C 282 0 SHEET 2 AD1 3 ILE C 302 GLY C 303 -1 O ILE C 302 N GLN C 282 SHEET 3 AD1 3 THR E 64 ALA E 65 -1 O THR E 64 N GLY C 303 SHEET 1 AD2 2 ALA E 130 GLU E 132 0 SHEET 2 AD2 2 PHE E 138 PHE E 140 -1 O GLU E 139 N LYS E 131 SHEET 1 AD3 4 GLN G 3 SER G 7 0 SHEET 2 AD3 4 SER G 17 SER G 25 -1 O SER G 21 N SER G 7 SHEET 3 AD3 4 THR G 77 ASN G 82A-1 O LEU G 80 N LEU G 20 SHEET 4 AD3 4 PHE G 67 ASP G 72 -1 N ASP G 72 O THR G 77 SHEET 1 AD4 6 GLY G 10 LEU G 11 0 SHEET 2 AD4 6 THR G 107 THR G 110 1 O THR G 110 N GLY G 10 SHEET 3 AD4 6 VAL G 89 ASP G 95 -1 N TYR G 90 O THR G 107 SHEET 4 AD4 6 MET G 34 GLN G 39 -1 N GLN G 39 O VAL G 89 SHEET 5 AD4 6 LEU G 45 ILE G 51 -1 O ILE G 51 N MET G 34 SHEET 6 AD4 6 THR G 57 TYR G 59 -1 O TYR G 58 N GLY G 50 SHEET 1 AD5 4 GLY G 10 LEU G 11 0 SHEET 2 AD5 4 THR G 107 THR G 110 1 O THR G 110 N GLY G 10 SHEET 3 AD5 4 VAL G 89 ASP G 95 -1 N TYR G 90 O THR G 107 SHEET 4 AD5 4 MET G 100M TRP G 103 -1 O VAL G 102 N LYS G 94 SHEET 1 AD6 6 SER J 10 SER J 12 0 SHEET 2 AD6 6 THR J 102 GLU J 105 1 O THR J 103 N LEU J 11 SHEET 3 AD6 6 THR J 85 TYR J 87 -1 N TYR J 86 O THR J 102 SHEET 4 AD6 6 TRP J 35 GLN J 38 -1 N GLN J 38 O THR J 85 SHEET 5 AD6 6 LYS J 45 TYR J 49 -1 O LEU J 47 N TRP J 35 SHEET 6 AD6 6 SER J 53 LEU J 54 -1 O SER J 53 N TYR J 49 SHEET 1 AD7 3 VAL J 19 ARG J 24 0 SHEET 2 AD7 3 ASP J 70 ILE J 75 -1 O PHE J 71 N CYS J 23 SHEET 3 AD7 3 PHE J 62 SER J 67 -1 N SER J 65 O THR J 72 SHEET 1 AD8 3 THR D 12 TYR D 17 0 SHEET 2 AD8 3 TYR F 22 GLN F 27 -1 O HIS F 25 N CYS D 14 SHEET 3 AD8 3 SER F 32 ALA F 36 -1 O ALA F 35 N TYR F 24 SHEET 1 AD9 2 ASP D 24 VAL D 26 0 SHEET 2 AD9 2 VAL D 34 VAL D 36 -1 O VAL D 34 N VAL D 26 SHEET 1 AE1 2 SER D 39 ASN D 41 0 SHEET 2 AE1 2 ARG D 315 ALA D 317 -1 O LEU D 316 N VAL D 40 SHEET 1 AE2 3 LEU D 43 GLU D 44 0 SHEET 2 AE2 3 PHE D 294 GLN D 295 1 O PHE D 294 N GLU D 44 SHEET 3 AE2 3 LYS D 307 TYR D 308 1 O LYS D 307 N GLN D 295 SHEET 1 AE3 2 LEU D 51 LEU D 54 0 SHEET 2 AE3 2 VAL D 274 THR D 279 1 O CYS D 277 N LYS D 53 SHEET 1 AE4 3 LEU D 59 GLY D 62 0 SHEET 2 AE4 3 ILE D 87 GLU D 89 1 O VAL D 88 N LEU D 59 SHEET 3 AE4 3 ILE D 267 ILE D 268 1 O ILE D 268 N GLU D 89 SHEET 1 AE5 4 GLU D 119 PHE D 121 0 SHEET 2 AE5 4 ALA D 257 MET D 260 -1 O ALA D 257 N PHE D 121 SHEET 3 AE5 4 GLU D 175 HIS D 184 -1 N LEU D 177 O PHE D 258 SHEET 4 AE5 4 ARG D 229 VAL D 237 -1 O ARG D 229 N HIS D 184 SHEET 1 AE6 2 THR D 136 HIS D 141 0 SHEET 2 AE6 2 ALA D 144 SER D 146 -1 O ALA D 144 N HIS D 141 SHEET 1 AE7 2 LEU D 151 TRP D 153 0 SHEET 2 AE7 2 VAL D 252 PRO D 254 -1 O VAL D 253 N ILE D 152 SHEET 1 AE8 4 SER D 167 ILE D 169 0 SHEET 2 AE8 4 LYS D 242 ALA D 247 -1 O ILE D 243 N TYR D 168 SHEET 3 AE8 4 VAL D 202 THR D 206 -1 N PHE D 203 O GLU D 246 SHEET 4 AE8 4 TYR D 209 LYS D 211 -1 O TYR D 209 N THR D 206 SHEET 1 AE9 3 CYS D 281 GLN D 282 0 SHEET 2 AE9 3 ILE D 302 GLY D 303 -1 O ILE D 302 N GLN D 282 SHEET 3 AE9 3 THR F 64 ALA F 65 -1 O THR F 64 N GLY D 303 SHEET 1 AF1 2 ALA F 130 GLU F 132 0 SHEET 2 AF1 2 PHE F 138 PHE F 140 -1 O GLU F 139 N LYS F 131 SHEET 1 AF2 4 GLN I 3 SER I 7 0 SHEET 2 AF2 4 SER I 17 SER I 25 -1 O SER I 21 N SER I 7 SHEET 3 AF2 4 THR I 77 ASN I 82A-1 O LEU I 80 N LEU I 20 SHEET 4 AF2 4 PHE I 67 ASP I 72 -1 N ASP I 72 O THR I 77 SHEET 1 AF3 6 GLY I 10 LEU I 11 0 SHEET 2 AF3 6 THR I 107 THR I 110 1 O THR I 110 N GLY I 10 SHEET 3 AF3 6 VAL I 89 ASP I 95 -1 N TYR I 90 O THR I 107 SHEET 4 AF3 6 MET I 34 GLN I 39 -1 N GLN I 39 O VAL I 89 SHEET 5 AF3 6 LEU I 45 ILE I 51 -1 O ILE I 51 N MET I 34 SHEET 6 AF3 6 THR I 57 TYR I 59 -1 O TYR I 58 N GLY I 50 SHEET 1 AF4 4 GLY I 10 LEU I 11 0 SHEET 2 AF4 4 THR I 107 THR I 110 1 O THR I 110 N GLY I 10 SHEET 3 AF4 4 VAL I 89 ASP I 95 -1 N TYR I 90 O THR I 107 SHEET 4 AF4 4 MET I 100M TRP I 103 -1 O VAL I 102 N LYS I 94 SHEET 1 AF5 6 SER K 10 SER K 12 0 SHEET 2 AF5 6 THR K 102 GLU K 105 1 O THR K 103 N LEU K 11 SHEET 3 AF5 6 THR K 85 TYR K 87 -1 N TYR K 86 O THR K 102 SHEET 4 AF5 6 TRP K 35 GLN K 38 -1 N GLN K 38 O THR K 85 SHEET 5 AF5 6 LYS K 45 TYR K 49 -1 O LEU K 47 N TRP K 35 SHEET 6 AF5 6 SER K 53 LEU K 54 -1 O SER K 53 N TYR K 49 SHEET 1 AF6 3 VAL K 19 ARG K 24 0 SHEET 2 AF6 3 ASP K 70 ILE K 75 -1 O PHE K 71 N CYS K 23 SHEET 3 AF6 3 PHE K 62 SER K 67 -1 N SER K 65 O THR K 72 SSBOND 1 CYS A 14 CYS B 137 1555 1555 2.02 SSBOND 2 CYS A 52 CYS A 277 1555 1555 2.03 SSBOND 3 CYS A 64 CYS A 76 1555 1555 2.03 SSBOND 4 CYS A 97 CYS A 139 1555 1555 2.02 SSBOND 5 CYS A 281 CYS A 305 1555 1555 2.03 SSBOND 6 CYS B 144 CYS B 148 1555 1555 2.02 SSBOND 7 CYS H 22 CYS H 92 1555 1555 2.03 SSBOND 8 CYS H 98 CYS H 100C 1555 1555 2.02 SSBOND 9 CYS L 23 CYS L 88 1555 1555 2.03 SSBOND 10 CYS C 14 CYS E 137 1555 1555 2.02 SSBOND 11 CYS C 52 CYS C 277 1555 1555 2.03 SSBOND 12 CYS C 64 CYS C 76 1555 1555 2.03 SSBOND 13 CYS C 97 CYS C 139 1555 1555 2.02 SSBOND 14 CYS C 281 CYS C 305 1555 1555 2.03 SSBOND 15 CYS E 144 CYS E 148 1555 1555 2.02 SSBOND 16 CYS G 22 CYS G 92 1555 1555 2.03 SSBOND 17 CYS G 98 CYS G 100C 1555 1555 2.02 SSBOND 18 CYS J 23 CYS J 88 1555 1555 2.03 SSBOND 19 CYS D 14 CYS F 137 1555 1555 2.02 SSBOND 20 CYS D 52 CYS D 277 1555 1555 2.03 SSBOND 21 CYS D 64 CYS D 76 1555 1555 2.03 SSBOND 22 CYS D 97 CYS D 139 1555 1555 2.02 SSBOND 23 CYS D 281 CYS D 305 1555 1555 2.03 SSBOND 24 CYS F 144 CYS F 148 1555 1555 2.02 SSBOND 25 CYS I 22 CYS I 92 1555 1555 2.03 SSBOND 26 CYS I 98 CYS I 100C 1555 1555 2.02 SSBOND 27 CYS K 23 CYS K 88 1555 1555 2.03 LINK ND2 ASN A 33 C1 NAG A 401 1555 1555 1.44 LINK ND2 ASN A 94 C1 NAG M 1 1555 1555 1.43 LINK ND2 ASN A 278 C1 NAG A 402 1555 1555 1.45 LINK ND2 ASN B 154 C1 NAG B 301 1555 1555 1.44 LINK ND2 ASN C 33 C1 NAG C 401 1555 1555 1.44 LINK ND2 ASN C 94 C1 NAG N 1 1555 1555 1.43 LINK ND2 ASN C 278 C1 NAG C 402 1555 1555 1.46 LINK ND2 ASN E 154 C1 NAG E 301 1555 1555 1.44 LINK ND2 ASN D 33 C1 NAG D 401 1555 1555 1.44 LINK ND2 ASN D 94 C1 NAG O 1 1555 1555 1.43 LINK ND2 ASN D 278 C1 NAG D 402 1555 1555 1.45 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 O4 NAG O 1 C1 NAG O 2 1555 1555 1.44 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 1.000000 0.000000 0.000000 0.00000 SCALE2 0.000000 1.000000 0.000000 0.00000 SCALE3 0.000000 0.000000 1.000000 0.00000