HEADER VIRAL PROTEIN/IMMUNE SYSTEM 01-JAN-25 9MQ3 TITLE CRYO-EM MAP OF H5 HA (A/JIANGSU/NJ210/2023) IN COMPLEX WITH MONOCLONAL TITLE 2 FAB 6G1 CAVEAT 9MQ3 COMPND MOL_ID: 1; COMPND 2 MOLECULE: 6G1 HEAVY CHAIN FAB; COMPND 3 CHAIN: H; COMPND 4 OTHER_DETAILS: 6G1 HEAVY CHAIN FAB; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: 6G1 LIGHT CHAIN FAB; COMPND 7 CHAIN: L; COMPND 8 MOL_ID: 3; COMPND 9 MOLECULE: HEMAGGLUTININ HA1; COMPND 10 CHAIN: B, A, C; COMPND 11 ENGINEERED: YES; COMPND 12 MOL_ID: 4; COMPND 13 MOLECULE: HEMAGGLUTININ HA2; COMPND 14 CHAIN: b, a, c; COMPND 15 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 MOL_ID: 2; SOURCE 5 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 6 ORGANISM_TAXID: 9606; SOURCE 7 MOL_ID: 3; SOURCE 8 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS; SOURCE 9 ORGANISM_TAXID: 11320; SOURCE 10 STRAIN: A/JIANGSU/NJ210/2023; SOURCE 11 GENE: HA; SOURCE 12 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 13 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 14 EXPRESSION_SYSTEM_CELL_LINE: HEK293; SOURCE 15 MOL_ID: 4; SOURCE 16 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS; SOURCE 17 ORGANISM_TAXID: 11320; SOURCE 18 STRAIN: A/JIANGSU/NJ210/2023; SOURCE 19 GENE: HA; SOURCE 20 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 21 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 22 EXPRESSION_SYSTEM_CELL_LINE: HEK293 KEYWDS INFLUENZA, HEMAGGLUTININ, H5, MONOCLONAL, COMPLEX, FAB COMPLEX, VIRAL KEYWDS 2 FUSION PROTEIN, VIRAL PROTEIN, VIRAL PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR A.N.LEON,P.J.M.BROUWER,A.J.RODRIGUEZ,J.HAN,A.B.WARD REVDAT 1 05-NOV-25 9MQ3 0 JRNL AUTH G.PENA ALZUA,A.N.LEON,P.J.M.BROUWER,T.YELLIN,D.BHAVSAR, JRNL AUTH 2 M.LOGANATHAN,K.BUSHFIELD,C.MARIZZI,A.J.RODRIGUEZ,J.HAN, JRNL AUTH 3 R.WEBBY,A.B.WARD,J.A.DUTY,K.FLORIAN JRNL TITL HUMAN MONOCLONAL ANTIBODIES THAT TARGET CLADE 2.3.4.4B H5N1 JRNL TITL 2 HEMAGGLUTININ JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.22 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : PHENIX, 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) : 3.220 REMARK 3 NUMBER OF PARTICLES : 123783 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 9MQ3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-JAN-25. REMARK 100 THE DEPOSITION ID IS D_1000291407. 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 : H5 HA (A/JIANGSU/NJ210/2023) IN REMARK 245 COMPLEX WITH MONOCLONAL FAB 6G1, REMARK 245 1A1 AND CR9114 REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 0.53 REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.40 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : TFS GLACIOS REMARK 245 DETECTOR TYPE : FEI FALCON I (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 800.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2000.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : NULL REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 4239.00 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : NULL REMARK 245 CALIBRATED MAGNIFICATION : NULL REMARK 245 SOURCE : FIELD EMISSION GUN REMARK 245 ACCELERATION VOLTAGE (KV) : 200 REMARK 245 IMAGING DETAILS : NULL REMARK 247 REMARK 247 ELECTRON MICROSCOPY REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION REMARK 247 OF THE STRUCTURE FACTORS. REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: OCTAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L, B, b, A, a, C, c 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 ASP L 1 REMARK 465 MET B -5 REMARK 465 GLU B -4 REMARK 465 ASN B -3 REMARK 465 ILE B -2 REMARK 465 VAL B -1 REMARK 465 LEU B 0 REMARK 465 LEU B 1 REMARK 465 LEU B 2 REMARK 465 ALA B 3 REMARK 465 ILE B 4 REMARK 465 VAL B 5 REMARK 465 ASN B 6 REMARK 465 LEU B 7 REMARK 465 VAL B 8 REMARK 465 LYS B 9 REMARK 465 SER B 10 REMARK 465 ASP B 11 REMARK 465 GLN B 12 REMARK 465 VAL B 272 REMARK 465 GLU B 273 REMARK 465 ASN B 322 REMARK 465 SER B 323 REMARK 465 PRO B 324 REMARK 465 PRO B 325 REMARK 465 ARG B 326 REMARK 465 GLU B 327 REMARK 465 LYS B 328 REMARK 465 ARG B 329 REMARK 465 ARG B 330 REMARK 465 LYS B 331 REMARK 465 ARG B 332 REMARK 465 GLY b 1 REMARK 465 ARG b 167 REMARK 465 LEU b 168 REMARK 465 LYS b 169 REMARK 465 ARG b 170 REMARK 465 GLU b 171 REMARK 465 GLU b 172 REMARK 465 ILE b 173 REMARK 465 SER 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 GLY b 213 REMARK 465 SER b 214 REMARK 465 HIS b 215 REMARK 465 HIS b 216 REMARK 465 HIS b 217 REMARK 465 HIS b 218 REMARK 465 HIS b 219 REMARK 465 HIS b 220 REMARK 465 MET A -5 REMARK 465 GLU A -4 REMARK 465 ASN A -3 REMARK 465 ILE A -2 REMARK 465 VAL A -1 REMARK 465 LEU A 0 REMARK 465 LEU A 1 REMARK 465 LEU A 2 REMARK 465 ALA A 3 REMARK 465 ILE A 4 REMARK 465 VAL A 5 REMARK 465 ASN A 6 REMARK 465 LEU A 7 REMARK 465 VAL A 8 REMARK 465 LYS A 9 REMARK 465 SER A 10 REMARK 465 ASP A 11 REMARK 465 GLN A 12 REMARK 465 VAL A 272 REMARK 465 GLU A 273 REMARK 465 ASN A 322 REMARK 465 SER A 323 REMARK 465 PRO A 324 REMARK 465 PRO A 325 REMARK 465 ARG A 326 REMARK 465 GLU A 327 REMARK 465 LYS A 328 REMARK 465 ARG A 329 REMARK 465 ARG A 330 REMARK 465 LYS A 331 REMARK 465 ARG A 332 REMARK 465 GLY a 1 REMARK 465 ARG a 167 REMARK 465 LEU a 168 REMARK 465 LYS a 169 REMARK 465 ARG a 170 REMARK 465 GLU a 171 REMARK 465 GLU a 172 REMARK 465 ILE a 173 REMARK 465 SER a 174 REMARK 465 GLY a 175 REMARK 465 VAL a 176 REMARK 465 GLY a 177 REMARK 465 TYR a 178 REMARK 465 ILE a 179 REMARK 465 PRO a 180 REMARK 465 GLU a 181 REMARK 465 ALA a 182 REMARK 465 PRO a 183 REMARK 465 ARG a 184 REMARK 465 ASP a 185 REMARK 465 GLY a 186 REMARK 465 GLN a 187 REMARK 465 ALA a 188 REMARK 465 TYR a 189 REMARK 465 VAL a 190 REMARK 465 ARG a 191 REMARK 465 LYS a 192 REMARK 465 ASP a 193 REMARK 465 GLY a 194 REMARK 465 GLU a 195 REMARK 465 TRP a 196 REMARK 465 VAL a 197 REMARK 465 LEU a 198 REMARK 465 LEU a 199 REMARK 465 SER a 200 REMARK 465 THR a 201 REMARK 465 PHE a 202 REMARK 465 LEU a 203 REMARK 465 GLY a 204 REMARK 465 SER a 205 REMARK 465 GLU a 206 REMARK 465 ASN a 207 REMARK 465 LEU a 208 REMARK 465 TYR a 209 REMARK 465 PHE a 210 REMARK 465 GLN a 211 REMARK 465 GLY a 212 REMARK 465 GLY a 213 REMARK 465 SER a 214 REMARK 465 HIS a 215 REMARK 465 HIS a 216 REMARK 465 HIS a 217 REMARK 465 HIS a 218 REMARK 465 HIS a 219 REMARK 465 HIS a 220 REMARK 465 MET C -5 REMARK 465 GLU C -4 REMARK 465 ASN C -3 REMARK 465 ILE C -2 REMARK 465 VAL C -1 REMARK 465 LEU C 0 REMARK 465 LEU C 1 REMARK 465 LEU C 2 REMARK 465 ALA C 3 REMARK 465 ILE C 4 REMARK 465 VAL C 5 REMARK 465 ASN C 6 REMARK 465 LEU C 7 REMARK 465 VAL C 8 REMARK 465 LYS C 9 REMARK 465 SER C 10 REMARK 465 ASP C 11 REMARK 465 GLN C 12 REMARK 465 VAL C 272 REMARK 465 GLU C 273 REMARK 465 ASN C 322 REMARK 465 SER C 323 REMARK 465 PRO C 324 REMARK 465 PRO C 325 REMARK 465 ARG C 326 REMARK 465 GLU C 327 REMARK 465 LYS C 328 REMARK 465 ARG C 329 REMARK 465 ARG C 330 REMARK 465 LYS C 331 REMARK 465 ARG C 332 REMARK 465 GLY c 1 REMARK 465 ARG c 167 REMARK 465 LEU c 168 REMARK 465 LYS c 169 REMARK 465 ARG c 170 REMARK 465 GLU c 171 REMARK 465 GLU c 172 REMARK 465 ILE c 173 REMARK 465 SER c 174 REMARK 465 GLY c 175 REMARK 465 VAL c 176 REMARK 465 GLY c 177 REMARK 465 TYR c 178 REMARK 465 ILE c 179 REMARK 465 PRO c 180 REMARK 465 GLU c 181 REMARK 465 ALA c 182 REMARK 465 PRO c 183 REMARK 465 ARG c 184 REMARK 465 ASP c 185 REMARK 465 GLY c 186 REMARK 465 GLN c 187 REMARK 465 ALA c 188 REMARK 465 TYR c 189 REMARK 465 VAL c 190 REMARK 465 ARG c 191 REMARK 465 LYS c 192 REMARK 465 ASP c 193 REMARK 465 GLY c 194 REMARK 465 GLU c 195 REMARK 465 TRP c 196 REMARK 465 VAL c 197 REMARK 465 LEU c 198 REMARK 465 LEU c 199 REMARK 465 SER c 200 REMARK 465 THR c 201 REMARK 465 PHE c 202 REMARK 465 LEU c 203 REMARK 465 GLY c 204 REMARK 465 SER c 205 REMARK 465 GLU c 206 REMARK 465 ASN c 207 REMARK 465 LEU c 208 REMARK 465 TYR c 209 REMARK 465 PHE c 210 REMARK 465 GLN c 211 REMARK 465 GLY c 212 REMARK 465 GLY c 213 REMARK 465 SER c 214 REMARK 465 HIS c 215 REMARK 465 HIS c 216 REMARK 465 HIS c 217 REMARK 465 HIS c 218 REMARK 465 HIS c 219 REMARK 465 HIS c 220 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 O LEU B 70 OH TYR B 258 2.08 REMARK 500 OG SER C 113 O SER C 265 2.10 REMARK 500 O VAL C 309 OG1 THR c 93 2.13 REMARK 500 OG SER A 185 OE1 GLN A 191 2.13 REMARK 500 OG SER B 101 OD1 ASP B 231 2.16 REMARK 500 O LEU A 70 OH TYR A 258 2.16 REMARK 500 O LEU a 89 OG1 THR a 93 2.17 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 CYS c 144 CA - CB - SG ANGL. DEV. = 8.6 DEGREES REMARK 500 CYS c 148 CA - CB - SG ANGL. DEV. = 6.7 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 GLU H 16 -169.50 -163.00 REMARK 500 GLN L 27 147.22 -170.02 REMARK 500 CYS B 14 115.34 -161.31 REMARK 500 ASN B 92 77.91 -111.72 REMARK 500 ASP B 240 -3.85 74.30 REMARK 500 ALA b 7 -5.19 78.28 REMARK 500 GLU b 132 72.03 -100.08 REMARK 500 SER b 163 99.27 -69.61 REMARK 500 PHE A 147 -177.41 -177.60 REMARK 500 TRP A 180 -168.65 -129.23 REMARK 500 ASN A 296 33.10 -140.51 REMARK 500 ALA a 5 -53.78 -120.00 REMARK 500 LEU a 73 -5.40 76.64 REMARK 500 ARG a 127 -126.76 49.54 REMARK 500 ASN a 135 55.73 -93.10 REMARK 500 PHE C 79 31.77 -140.34 REMARK 500 LYS C 165 58.02 39.63 REMARK 500 TRP C 180 -169.18 -163.10 REMARK 500 ARG C 227 51.72 -92.28 REMARK 500 MET c 59 30.52 -94.94 REMARK 500 ARG c 127 -126.03 60.03 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-48512 RELATED DB: EMDB REMARK 900 CRYO-EM MAP OF H5 HA (A/JIANGSU/NJ210/2023) IN COMPLEX WITH REMARK 900 MONOCLONAL FAB 6G1 DBREF 9MQ3 H 1 113 PDB 9MQ3 9MQ3 1 113 DBREF 9MQ3 L 1 107 PDB 9MQ3 9MQ3 1 107 DBREF1 9MQ3 B -5 332 UNP A0A8E4ZAK5_9INFA DBREF2 9MQ3 B A0A8E4ZAK5 1 345 DBREF1 9MQ3 b 1 176 UNP A0AAX6NNL9_9INFA DBREF2 9MQ3 b A0AAX6NNL9 346 521 DBREF1 9MQ3 A -5 332 UNP A0A8E4ZAK5_9INFA DBREF2 9MQ3 A A0A8E4ZAK5 1 345 DBREF1 9MQ3 a 1 176 UNP A0AAX6NNL9_9INFA DBREF2 9MQ3 a A0AAX6NNL9 346 521 DBREF1 9MQ3 C -5 332 UNP A0A8E4ZAK5_9INFA DBREF2 9MQ3 C A0A8E4ZAK5 1 345 DBREF1 9MQ3 c 1 176 UNP A0AAX6NNL9_9INFA DBREF2 9MQ3 c A0AAX6NNL9 346 521 SEQADV 9MQ3 ASN B 6 UNP A0A8E4ZAK SER 12 CONFLICT SEQADV 9MQ3 ASP B 91 UNP A0A8E4ZAK ALA 99 CONFLICT SEQADV 9MQ3 ASP B 158 UNP A0A8E4ZAK ASN 170 CONFLICT SEQADV 9MQ3 PRO B 325 UNP A0A8E4ZAK LEU 338 CONFLICT SEQADV 9MQ3 GLY b 177 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 TYR b 178 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 ILE b 179 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 PRO b 180 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 GLU b 181 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 ALA b 182 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 PRO b 183 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 ARG b 184 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 ASP b 185 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 GLY b 186 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 GLN b 187 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 ALA b 188 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 TYR b 189 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 VAL b 190 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 ARG b 191 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 LYS b 192 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 ASP b 193 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 GLY b 194 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 GLU b 195 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 TRP b 196 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 VAL b 197 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 LEU b 198 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 LEU b 199 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 SER b 200 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 THR b 201 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 PHE b 202 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 LEU b 203 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 GLY b 204 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 SER b 205 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 GLU b 206 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 ASN b 207 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 LEU b 208 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 TYR b 209 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 PHE b 210 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 GLN b 211 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 GLY b 212 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 GLY b 213 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 SER b 214 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 HIS b 215 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 HIS b 216 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 HIS b 217 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 HIS b 218 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 HIS b 219 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 HIS b 220 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 ASN A 6 UNP A0A8E4ZAK SER 12 CONFLICT SEQADV 9MQ3 ASP A 91 UNP A0A8E4ZAK ALA 99 CONFLICT SEQADV 9MQ3 ASP A 158 UNP A0A8E4ZAK ASN 170 CONFLICT SEQADV 9MQ3 PRO A 325 UNP A0A8E4ZAK LEU 338 CONFLICT SEQADV 9MQ3 GLY a 177 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 TYR a 178 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 ILE a 179 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 PRO a 180 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 GLU a 181 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 ALA a 182 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 PRO a 183 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 ARG a 184 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 ASP a 185 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 GLY a 186 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 GLN a 187 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 ALA a 188 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 TYR a 189 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 VAL a 190 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 ARG a 191 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 LYS a 192 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 ASP a 193 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 GLY a 194 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 GLU a 195 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 TRP a 196 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 VAL a 197 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 LEU a 198 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 LEU a 199 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 SER a 200 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 THR a 201 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 PHE a 202 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 LEU a 203 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 GLY a 204 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 SER a 205 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 GLU a 206 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 ASN a 207 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 LEU a 208 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 TYR a 209 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 PHE a 210 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 GLN a 211 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 GLY a 212 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 GLY a 213 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 SER a 214 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 HIS a 215 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 HIS a 216 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 HIS a 217 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 HIS a 218 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 HIS a 219 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 HIS a 220 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 ASN C 6 UNP A0A8E4ZAK SER 12 CONFLICT SEQADV 9MQ3 ASP C 91 UNP A0A8E4ZAK ALA 99 CONFLICT SEQADV 9MQ3 ASP C 158 UNP A0A8E4ZAK ASN 170 CONFLICT SEQADV 9MQ3 PRO C 325 UNP A0A8E4ZAK LEU 338 CONFLICT SEQADV 9MQ3 GLY c 177 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 TYR c 178 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 ILE c 179 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 PRO c 180 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 GLU c 181 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 ALA c 182 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 PRO c 183 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 ARG c 184 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 ASP c 185 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 GLY c 186 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 GLN c 187 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 ALA c 188 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 TYR c 189 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 VAL c 190 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 ARG c 191 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 LYS c 192 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 ASP c 193 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 GLY c 194 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 GLU c 195 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 TRP c 196 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 VAL c 197 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 LEU c 198 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 LEU c 199 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 SER c 200 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 THR c 201 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 PHE c 202 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 LEU c 203 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 GLY c 204 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 SER c 205 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 GLU c 206 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 ASN c 207 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 LEU c 208 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 TYR c 209 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 PHE c 210 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 GLN c 211 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 GLY c 212 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 GLY c 213 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 SER c 214 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 HIS c 215 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 HIS c 216 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 HIS c 217 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 HIS c 218 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 HIS c 219 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ3 HIS c 220 UNP A0AAX6NNL EXPRESSION TAG SEQRES 1 H 125 GLN VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 H 125 PRO SER GLU THR LEU SER LEU THR CYS THR VAL SER GLY SEQRES 3 H 125 GLY SER ILE SER SER TYR TYR TRP SER TRP ILE ARG GLN SEQRES 4 H 125 PRO PRO GLY LYS GLY LEU GLU TRP ILE GLY TYR ILE TYR SEQRES 5 H 125 TYR SER GLY SER THR ASN TYR ASN PRO SER LEU LYS SER SEQRES 6 H 125 ARG VAL THR ILE SER VAL ASP THR ALA LYS ASN GLN PHE SEQRES 7 H 125 SER LEU ASN LEU ASN SER VAL THR ALA ALA ASP THR ALA SEQRES 8 H 125 VAL TYR TYR CYS ALA ARG ASP LEU ARG GLU TRP SER GLY SEQRES 9 H 125 ALA LEU ASN TYR TYR TYR GLY MET ASP VAL TRP GLY GLN SEQRES 10 H 125 GLY THR PRO VAL THR VAL SER SER SEQRES 1 L 112 ASP ILE VAL MET THR GLN SER PRO LEU SER LEU PRO VAL SEQRES 2 L 112 THR PRO GLY GLU PRO ALA SER MET SER CYS ARG SER SER SEQRES 3 L 112 GLN SER LEU LEU HIS SER TYR GLY SER ASN TYR LEU ASP SEQRES 4 L 112 TRP TYR LEU GLN LYS PRO GLY GLN SER PRO GLN LEU LEU SEQRES 5 L 112 ILE TYR LEU GLY SER TYR ARG ALA SER GLY VAL SER ASP SEQRES 6 L 112 ARG PHE SER GLY SER GLY SER GLY THR ASN PHE THR LEU SEQRES 7 L 112 LYS ILE SER ARG VAL GLU ALA GLU ASP VAL GLY VAL TYR SEQRES 8 L 112 TYR CYS MET GLN ALA LEU GLN THR PRO PHE THR PHE GLY SEQRES 9 L 112 PRO GLY THR LYS VAL ASP ILE LYS SEQRES 1 B 345 MET GLU ASN ILE VAL LEU LEU LEU ALA ILE VAL ASN LEU SEQRES 2 B 345 VAL LYS SER ASP GLN ILE CYS ILE GLY TYR HIS ALA ASN SEQRES 3 B 345 ASN SER THR GLU GLN VAL ASP THR ILE MET GLU LYS ASN SEQRES 4 B 345 VAL THR VAL THR HIS ALA GLN ASP ILE LEU GLU LYS THR SEQRES 5 B 345 HIS ASN GLY LYS LEU CYS ASP LEU ASN GLY VAL LYS PRO SEQRES 6 B 345 LEU ILE LEU LYS ASP CYS SER VAL ALA GLY TRP LEU LEU SEQRES 7 B 345 GLY ASN PRO MET CYS ASP GLU PHE ILE ARG VAL PRO GLU SEQRES 8 B 345 TRP SER TYR ILE VAL GLU ARG ASP ASN PRO ALA ASN ASP SEQRES 9 B 345 LEU CYS TYR PRO GLY SER LEU ASN ASP TYR GLU GLU LEU SEQRES 10 B 345 LYS HIS LEU LEU SER ARG ILE ASN HIS PHE GLU LYS ILE SEQRES 11 B 345 LEU ILE ILE PRO LYS SER SER TRP PRO ASN HIS GLU THR SEQRES 12 B 345 SER LEU GLY VAL SER ALA ALA CYS PRO TYR GLN GLY ALA SEQRES 13 B 345 PRO SER PHE PHE ARG ASN VAL VAL TRP LEU ILE LYS LYS SEQRES 14 B 345 ASP ASP ALA TYR PRO THR ILE LYS ILE SER TYR ASN ASN SEQRES 15 B 345 THR ASN ARG GLU ASP LEU LEU ILE LEU TRP GLY ILE HIS SEQRES 16 B 345 HIS SER ASN ASN ALA GLU GLU GLN THR ASN LEU TYR LYS SEQRES 17 B 345 ASN PRO THR THR TYR ILE SER VAL GLY THR SER THR LEU SEQRES 18 B 345 ASN GLN ARG LEU VAL PRO LYS ILE ALA THR ARG SER GLN SEQRES 19 B 345 VAL ASN GLY GLN ARG GLY ARG MET ASP PHE PHE TRP THR SEQRES 20 B 345 ILE LEU LYS PRO ASP ASP ALA ILE HIS PHE GLU SER ASN SEQRES 21 B 345 GLY ASN PHE ILE ALA PRO GLU TYR ALA TYR LYS ILE VAL SEQRES 22 B 345 LYS LYS GLY ASP SER THR ILE MET LYS SER GLY VAL GLU SEQRES 23 B 345 TYR GLY HIS CYS ASN THR LYS CYS GLN THR PRO VAL GLY SEQRES 24 B 345 ALA ILE ASN SER SER MET PRO PHE HIS ASN ILE HIS PRO SEQRES 25 B 345 LEU THR ILE GLY GLU CYS PRO LYS TYR VAL LYS SER ASN SEQRES 26 B 345 LYS LEU VAL LEU ALA THR GLY LEU ARG ASN SER PRO PRO SEQRES 27 B 345 ARG GLU LYS ARG ARG LYS ARG SEQRES 1 b 220 GLY LEU PHE GLY ALA ILE ALA GLY PHE ILE GLU GLY GLY SEQRES 2 b 220 TRP GLN GLY MET VAL ASP GLY TRP TYR GLY TYR HIS HIS SEQRES 3 b 220 SER ASN GLU GLN GLY SER GLY TYR ALA ALA ASP LYS GLU SEQRES 4 b 220 SER THR GLN LYS ALA ILE ASP GLY VAL THR ASN LYS VAL SEQRES 5 b 220 ASN SER ILE ILE ASP LYS MET ASN THR GLN PHE GLU ALA SEQRES 6 b 220 VAL GLY ARG GLU PHE ASN ASN LEU GLU ARG ARG ILE GLU SEQRES 7 b 220 ASN LEU ASN LYS LYS MET GLU ASP GLY PHE LEU ASP VAL SEQRES 8 b 220 TRP THR TYR ASN ALA GLU LEU LEU VAL LEU MET GLU ASN SEQRES 9 b 220 GLU ARG THR LEU ASP PHE HIS ASP SER ASN VAL LYS ASN SEQRES 10 b 220 LEU TYR ASP LYS VAL ARG LEU GLN LEU ARG ASP ASN ALA SEQRES 11 b 220 LYS GLU LEU GLY ASN GLY CYS PHE GLU PHE TYR HIS LYS SEQRES 12 b 220 CYS ASP ASN GLU CYS MET GLU SER VAL ARG ASN GLY THR SEQRES 13 b 220 TYR TYR TYR PRO GLN TYR SER GLU GLU ALA ARG LEU LYS SEQRES 14 b 220 ARG GLU GLU ILE SER GLY VAL GLY TYR ILE PRO GLU ALA SEQRES 15 b 220 PRO ARG ASP GLY GLN ALA TYR VAL ARG LYS ASP GLY GLU SEQRES 16 b 220 TRP VAL LEU LEU SER THR PHE LEU GLY SER GLU ASN LEU SEQRES 17 b 220 TYR PHE GLN GLY GLY SER HIS HIS HIS HIS HIS HIS SEQRES 1 A 345 MET GLU ASN ILE VAL LEU LEU LEU ALA ILE VAL ASN LEU SEQRES 2 A 345 VAL LYS SER ASP GLN ILE CYS ILE GLY TYR HIS ALA ASN SEQRES 3 A 345 ASN SER THR GLU GLN VAL ASP THR ILE MET GLU LYS ASN SEQRES 4 A 345 VAL THR VAL THR HIS ALA GLN ASP ILE LEU GLU LYS THR SEQRES 5 A 345 HIS ASN GLY LYS LEU CYS ASP LEU ASN GLY VAL LYS PRO SEQRES 6 A 345 LEU ILE LEU LYS ASP CYS SER VAL ALA GLY TRP LEU LEU SEQRES 7 A 345 GLY ASN PRO MET CYS ASP GLU PHE ILE ARG VAL PRO GLU SEQRES 8 A 345 TRP SER TYR ILE VAL GLU ARG ASP ASN PRO ALA ASN ASP SEQRES 9 A 345 LEU CYS TYR PRO GLY SER LEU ASN ASP TYR GLU GLU LEU SEQRES 10 A 345 LYS HIS LEU LEU SER ARG ILE ASN HIS PHE GLU LYS ILE SEQRES 11 A 345 LEU ILE ILE PRO LYS SER SER TRP PRO ASN HIS GLU THR SEQRES 12 A 345 SER LEU GLY VAL SER ALA ALA CYS PRO TYR GLN GLY ALA SEQRES 13 A 345 PRO SER PHE PHE ARG ASN VAL VAL TRP LEU ILE LYS LYS SEQRES 14 A 345 ASP ASP ALA TYR PRO THR ILE LYS ILE SER TYR ASN ASN SEQRES 15 A 345 THR ASN ARG GLU ASP LEU LEU ILE LEU TRP GLY ILE HIS SEQRES 16 A 345 HIS SER ASN ASN ALA GLU GLU GLN THR ASN LEU TYR LYS SEQRES 17 A 345 ASN PRO THR THR TYR ILE SER VAL GLY THR SER THR LEU SEQRES 18 A 345 ASN GLN ARG LEU VAL PRO LYS ILE ALA THR ARG SER GLN SEQRES 19 A 345 VAL ASN GLY GLN ARG GLY ARG MET ASP PHE PHE TRP THR SEQRES 20 A 345 ILE LEU LYS PRO ASP ASP ALA ILE HIS PHE GLU SER ASN SEQRES 21 A 345 GLY ASN PHE ILE ALA PRO GLU TYR ALA TYR LYS ILE VAL SEQRES 22 A 345 LYS LYS GLY ASP SER THR ILE MET LYS SER GLY VAL GLU SEQRES 23 A 345 TYR GLY HIS CYS ASN THR LYS CYS GLN THR PRO VAL GLY SEQRES 24 A 345 ALA ILE ASN SER SER MET PRO PHE HIS ASN ILE HIS PRO SEQRES 25 A 345 LEU THR ILE GLY GLU CYS PRO LYS TYR VAL LYS SER ASN SEQRES 26 A 345 LYS LEU VAL LEU ALA THR GLY LEU ARG ASN SER PRO PRO SEQRES 27 A 345 ARG GLU LYS ARG ARG LYS ARG SEQRES 1 a 220 GLY LEU PHE GLY ALA ILE ALA GLY PHE ILE GLU GLY GLY SEQRES 2 a 220 TRP GLN GLY MET VAL ASP GLY TRP TYR GLY TYR HIS HIS SEQRES 3 a 220 SER ASN GLU GLN GLY SER GLY TYR ALA ALA ASP LYS GLU SEQRES 4 a 220 SER THR GLN LYS ALA ILE ASP GLY VAL THR ASN LYS VAL SEQRES 5 a 220 ASN SER ILE ILE ASP LYS MET ASN THR GLN PHE GLU ALA SEQRES 6 a 220 VAL GLY ARG GLU PHE ASN ASN LEU GLU ARG ARG ILE GLU SEQRES 7 a 220 ASN LEU ASN LYS LYS MET GLU ASP GLY PHE LEU ASP VAL SEQRES 8 a 220 TRP THR TYR ASN ALA GLU LEU LEU VAL LEU MET GLU ASN SEQRES 9 a 220 GLU ARG THR LEU ASP PHE HIS ASP SER ASN VAL LYS ASN SEQRES 10 a 220 LEU TYR ASP LYS VAL ARG LEU GLN LEU ARG ASP ASN ALA SEQRES 11 a 220 LYS GLU LEU GLY ASN GLY CYS PHE GLU PHE TYR HIS LYS SEQRES 12 a 220 CYS ASP ASN GLU CYS MET GLU SER VAL ARG ASN GLY THR SEQRES 13 a 220 TYR TYR TYR PRO GLN TYR SER GLU GLU ALA ARG LEU LYS SEQRES 14 a 220 ARG GLU GLU ILE SER GLY VAL GLY TYR ILE PRO GLU ALA SEQRES 15 a 220 PRO ARG ASP GLY GLN ALA TYR VAL ARG LYS ASP GLY GLU SEQRES 16 a 220 TRP VAL LEU LEU SER THR PHE LEU GLY SER GLU ASN LEU SEQRES 17 a 220 TYR PHE GLN GLY GLY SER HIS HIS HIS HIS HIS HIS SEQRES 1 C 345 MET GLU ASN ILE VAL LEU LEU LEU ALA ILE VAL ASN LEU SEQRES 2 C 345 VAL LYS SER ASP GLN ILE CYS ILE GLY TYR HIS ALA ASN SEQRES 3 C 345 ASN SER THR GLU GLN VAL ASP THR ILE MET GLU LYS ASN SEQRES 4 C 345 VAL THR VAL THR HIS ALA GLN ASP ILE LEU GLU LYS THR SEQRES 5 C 345 HIS ASN GLY LYS LEU CYS ASP LEU ASN GLY VAL LYS PRO SEQRES 6 C 345 LEU ILE LEU LYS ASP CYS SER VAL ALA GLY TRP LEU LEU SEQRES 7 C 345 GLY ASN PRO MET CYS ASP GLU PHE ILE ARG VAL PRO GLU SEQRES 8 C 345 TRP SER TYR ILE VAL GLU ARG ASP ASN PRO ALA ASN ASP SEQRES 9 C 345 LEU CYS TYR PRO GLY SER LEU ASN ASP TYR GLU GLU LEU SEQRES 10 C 345 LYS HIS LEU LEU SER ARG ILE ASN HIS PHE GLU LYS ILE SEQRES 11 C 345 LEU ILE ILE PRO LYS SER SER TRP PRO ASN HIS GLU THR SEQRES 12 C 345 SER LEU GLY VAL SER ALA ALA CYS PRO TYR GLN GLY ALA SEQRES 13 C 345 PRO SER PHE PHE ARG ASN VAL VAL TRP LEU ILE LYS LYS SEQRES 14 C 345 ASP ASP ALA TYR PRO THR ILE LYS ILE SER TYR ASN ASN SEQRES 15 C 345 THR ASN ARG GLU ASP LEU LEU ILE LEU TRP GLY ILE HIS SEQRES 16 C 345 HIS SER ASN ASN ALA GLU GLU GLN THR ASN LEU TYR LYS SEQRES 17 C 345 ASN PRO THR THR TYR ILE SER VAL GLY THR SER THR LEU SEQRES 18 C 345 ASN GLN ARG LEU VAL PRO LYS ILE ALA THR ARG SER GLN SEQRES 19 C 345 VAL ASN GLY GLN ARG GLY ARG MET ASP PHE PHE TRP THR SEQRES 20 C 345 ILE LEU LYS PRO ASP ASP ALA ILE HIS PHE GLU SER ASN SEQRES 21 C 345 GLY ASN PHE ILE ALA PRO GLU TYR ALA TYR LYS ILE VAL SEQRES 22 C 345 LYS LYS GLY ASP SER THR ILE MET LYS SER GLY VAL GLU SEQRES 23 C 345 TYR GLY HIS CYS ASN THR LYS CYS GLN THR PRO VAL GLY SEQRES 24 C 345 ALA ILE ASN SER SER MET PRO PHE HIS ASN ILE HIS PRO SEQRES 25 C 345 LEU THR ILE GLY GLU CYS PRO LYS TYR VAL LYS SER ASN SEQRES 26 C 345 LYS LEU VAL LEU ALA THR GLY LEU ARG ASN SER PRO PRO SEQRES 27 C 345 ARG GLU LYS ARG ARG LYS ARG SEQRES 1 c 220 GLY LEU PHE GLY ALA ILE ALA GLY PHE ILE GLU GLY GLY SEQRES 2 c 220 TRP GLN GLY MET VAL ASP GLY TRP TYR GLY TYR HIS HIS SEQRES 3 c 220 SER ASN GLU GLN GLY SER GLY TYR ALA ALA ASP LYS GLU SEQRES 4 c 220 SER THR GLN LYS ALA ILE ASP GLY VAL THR ASN LYS VAL SEQRES 5 c 220 ASN SER ILE ILE ASP LYS MET ASN THR GLN PHE GLU ALA SEQRES 6 c 220 VAL GLY ARG GLU PHE ASN ASN LEU GLU ARG ARG ILE GLU SEQRES 7 c 220 ASN LEU ASN LYS LYS MET GLU ASP GLY PHE LEU ASP VAL SEQRES 8 c 220 TRP THR TYR ASN ALA GLU LEU LEU VAL LEU MET GLU ASN SEQRES 9 c 220 GLU ARG THR LEU ASP PHE HIS ASP SER ASN VAL LYS ASN SEQRES 10 c 220 LEU TYR ASP LYS VAL ARG LEU GLN LEU ARG ASP ASN ALA SEQRES 11 c 220 LYS GLU LEU GLY ASN GLY CYS PHE GLU PHE TYR HIS LYS SEQRES 12 c 220 CYS ASP ASN GLU CYS MET GLU SER VAL ARG ASN GLY THR SEQRES 13 c 220 TYR TYR TYR PRO GLN TYR SER GLU GLU ALA ARG LEU LYS SEQRES 14 c 220 ARG GLU GLU ILE SER GLY VAL GLY TYR ILE PRO GLU ALA SEQRES 15 c 220 PRO ARG ASP GLY GLN ALA TYR VAL ARG LYS ASP GLY GLU SEQRES 16 c 220 TRP VAL LEU LEU SER THR PHE LEU GLY SER GLU ASN LEU SEQRES 17 c 220 TYR PHE GLN GLY GLY SER HIS HIS HIS HIS HIS HIS HET NAG B 401 14 HET NAG B 402 14 HET NAG B 403 14 HET NAG B 404 14 HET NAG b 301 14 HET NAG A 401 14 HET NAG A 402 14 HET NAG A 403 14 HET NAG A 404 14 HET NAG a 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 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 9 NAG 15(C8 H15 N O6) HELIX 1 AA1 PRO H 61 LYS H 64 5 4 HELIX 2 AA2 THR H 83 THR H 87 5 5 HELIX 3 AA3 HIS L 27D SER L 30 5 5 HELIX 4 AA4 GLU L 79 VAL L 83 5 5 HELIX 5 AA5 SER B 65 LEU B 71 1 7 HELIX 6 AA6 ASP B 104 SER B 113 1 10 HELIX 7 AA7 PRO B 125 TRP B 127 5 5 HELIX 8 AA8 ASN B 187 TYR B 195 1 9 HELIX 9 AA9 ASP b 37 MET b 59 1 23 HELIX 10 AB1 GLU b 74 GLN b 125 1 52 HELIX 11 AB2 ASP b 145 GLY b 155 1 11 HELIX 12 AB3 TYR b 158 SER b 163 1 6 HELIX 13 AB4 SER A 65 LEU A 71 1 7 HELIX 14 AB5 ASP A 104 LEU A 112 1 9 HELIX 15 AB6 PRO A 125 TRP A 127 5 5 HELIX 16 AB7 ASN A 187 TYR A 195 1 9 HELIX 17 AB8 ASP a 37 MET a 59 1 23 HELIX 18 AB9 GLU a 74 ARG a 127 1 54 HELIX 19 AC1 ASP a 145 GLY a 155 1 11 HELIX 20 AC2 SER C 65 LEU C 71 1 7 HELIX 21 AC3 ASN C 73 ASP C 77 5 5 HELIX 22 AC4 ASP C 104 SER C 113 1 10 HELIX 23 AC5 ASN C 187 TYR C 195 1 9 HELIX 24 AC6 ASP c 37 MET c 59 1 23 HELIX 25 AC7 GLU c 74 GLN c 125 1 52 HELIX 26 AC8 LEU c 126 ASP c 128 5 3 HELIX 27 AC9 ASP c 145 GLY c 155 1 11 SHEET 1 AA1 4 GLN H 3 GLU H 6 0 SHEET 2 AA1 4 THR H 21 SER H 25 -1 O SER H 25 N GLN H 3 SHEET 3 AA1 4 GLN H 77 SER H 79 -1 O PHE H 78 N CYS H 22 SHEET 4 AA1 4 VAL H 71 ASP H 72 -1 N ASP H 72 O GLN H 77 SHEET 1 AA2 2 LEU H 11 VAL H 12 0 SHEET 2 AA2 2 THR H 110 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 1 AA3 5 THR H 57 TYR H 59 0 SHEET 2 AA3 5 GLU H 46 ILE H 51 -1 N TYR H 50 O ASN H 58 SHEET 3 AA3 5 TYR H 33 GLN H 39 -1 N TRP H 34 O ILE H 51 SHEET 4 AA3 5 VAL H 89 ASP H 95 -1 O TYR H 91 N ILE H 37 SHEET 5 AA3 5 THR H 107 PRO H 108 -1 O THR H 107 N TYR H 90 SHEET 1 AA4 4 THR L 5 GLN L 6 0 SHEET 2 AA4 4 ALA L 19 ARG L 24 -1 O ARG L 24 N THR L 5 SHEET 3 AA4 4 ASN L 70 ILE L 75 -1 O PHE L 71 N CYS L 23 SHEET 4 AA4 4 PHE L 62 SER L 65 -1 N SER L 65 O THR L 72 SHEET 1 AA5 6 PRO L 12 VAL L 13 0 SHEET 2 AA5 6 THR L 102 ILE L 106 1 O ASP L 105 N VAL L 13 SHEET 3 AA5 6 GLY L 84 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AA5 6 LEU L 33 GLN L 38 -1 N TYR L 36 O TYR L 87 SHEET 5 AA5 6 GLN L 45 TYR L 49 -1 O GLN L 45 N LEU L 37 SHEET 6 AA5 6 TYR L 53 ARG L 54 -1 O TYR L 53 N TYR L 49 SHEET 1 AA6 2 GLU B 24 VAL B 26 0 SHEET 2 AA6 2 VAL B 34 VAL B 36 -1 O VAL B 34 N VAL B 26 SHEET 1 AA7 3 LEU B 43 GLU B 44 0 SHEET 2 AA7 3 PHE B 294 HIS B 295 1 O PHE B 294 N GLU B 44 SHEET 3 AA7 3 LYS B 307 TYR B 308 1 O LYS B 307 N HIS B 295 SHEET 1 AA8 2 ASP B 53 LEU B 54 0 SHEET 2 AA8 2 ASN B 278 THR B 279 1 O THR B 279 N ASP B 53 SHEET 1 AA9 3 LEU B 59 ILE B 60 0 SHEET 2 AA9 3 TYR B 86 VAL B 88 1 O VAL B 88 N LEU B 59 SHEET 3 AA9 3 THR B 266 MET B 268 1 O MET B 268 N ILE B 87 SHEET 1 AB1 2 GLU B 119 ILE B 121 0 SHEET 2 AB1 2 ALA B 257 LYS B 259 -1 O LYS B 259 N GLU B 119 SHEET 1 AB2 2 PRO B 140 TYR B 141 0 SHEET 2 AB2 2 ALA B 144 PRO B 145 -1 O ALA B 144 N TYR B 141 SHEET 1 AB3 4 VAL B 151 TRP B 153 0 SHEET 2 AB3 4 PHE B 251 PRO B 254 -1 O ALA B 253 N VAL B 152 SHEET 3 AB3 4 LEU B 176 HIS B 184 -1 N GLY B 181 O ILE B 252 SHEET 4 AB3 4 ARG B 229 LEU B 237 -1 O LEU B 237 N LEU B 176 SHEET 1 AB4 4 ILE B 164 ASN B 169 0 SHEET 2 AB4 4 ALA B 242 SER B 247 -1 O PHE B 245 N ILE B 166 SHEET 3 AB4 4 ILE B 202 GLY B 205 -1 N SER B 203 O GLU B 246 SHEET 4 AB4 4 ASN B 210 LEU B 213 -1 O GLN B 211 N VAL B 204 SHEET 1 AB5 2 ALA b 130 GLU b 132 0 SHEET 2 AB5 2 PHE b 138 PHE b 140 -1 O GLU b 139 N LYS b 131 SHEET 1 AB6 3 CYS A 14 TYR A 17 0 SHEET 2 AB6 3 TYR a 22 SER a 27 -1 O HIS a 25 N CYS A 14 SHEET 3 AB6 3 SER a 32 ALA a 36 -1 O GLY a 33 N HIS a 26 SHEET 1 AB7 2 GLN A 25 VAL A 26 0 SHEET 2 AB7 2 VAL A 34 THR A 35 -1 O VAL A 34 N VAL A 26 SHEET 1 AB8 3 LEU A 43 GLU A 44 0 SHEET 2 AB8 3 PHE A 294 HIS A 295 1 O PHE A 294 N GLU A 44 SHEET 3 AB8 3 LYS A 307 TYR A 308 1 O LYS A 307 N HIS A 295 SHEET 1 AB9 2 LEU A 59 ILE A 60 0 SHEET 2 AB9 2 ILE A 87 VAL A 88 1 O VAL A 88 N LEU A 59 SHEET 1 AC1 4 HIS A 117 ILE A 121 0 SHEET 2 AC1 4 ALA A 257 LYS A 262 -1 O ALA A 257 N ILE A 121 SHEET 3 AC1 4 LEU A 176 HIS A 184 -1 N LEU A 177 O TYR A 258 SHEET 4 AC1 4 ARG A 229 LEU A 237 -1 O PHE A 233 N TRP A 180 SHEET 1 AC2 2 HIS A 130 GLU A 131 0 SHEET 2 AC2 2 ILE A 155 LYS A 156 -1 O ILE A 155 N GLU A 131 SHEET 1 AC3 2 VAL A 151 TRP A 153 0 SHEET 2 AC3 2 ILE A 252 PRO A 254 -1 O ALA A 253 N VAL A 152 SHEET 1 AC4 2 ALA a 130 GLU a 132 0 SHEET 2 AC4 2 PHE a 138 PHE a 140 -1 O GLU a 139 N LYS a 131 SHEET 1 AC5 2 CYS C 14 TYR C 17 0 SHEET 2 AC5 2 TYR c 22 HIS c 25 -1 O HIS c 25 N CYS C 14 SHEET 1 AC6 2 GLN C 25 VAL C 26 0 SHEET 2 AC6 2 VAL C 34 THR C 35 -1 O VAL C 34 N VAL C 26 SHEET 1 AC7 2 ASP C 53 LEU C 54 0 SHEET 2 AC7 2 ASN C 278 THR C 279 1 O THR C 279 N ASP C 53 SHEET 1 AC8 5 GLY C 100 LEU C 102 0 SHEET 2 AC8 5 ARG C 229 TRP C 234 1 O MET C 230 N SER C 101 SHEET 3 AC8 5 LEU C 179 HIS C 184 -1 N TRP C 180 O PHE C 233 SHEET 4 AC8 5 PHE C 251 PRO C 254 -1 O ILE C 252 N GLY C 181 SHEET 5 AC8 5 VAL C 151 TRP C 153 -1 N VAL C 152 O ALA C 253 SHEET 1 AC9 2 ILE C 115 ILE C 121 0 SHEET 2 AC9 2 ALA C 257 LYS C 262A-1 O ALA C 257 N ILE C 121 SHEET 1 AD1 2 PRO C 140 TYR C 141 0 SHEET 2 AD1 2 ALA C 144 PRO C 145 -1 O ALA C 144 N TYR C 141 SHEET 1 AD2 4 ILE C 166 ASN C 169 0 SHEET 2 AD2 4 ALA C 242 SER C 247 -1 O PHE C 245 N ILE C 166 SHEET 3 AD2 4 ILE C 202 THR C 206 -1 N SER C 203 O GLU C 246 SHEET 4 AD2 4 LEU C 209 LEU C 213 -1 O LEU C 209 N THR C 206 SHEET 1 AD3 3 ALA C 287 ILE C 288 0 SHEET 2 AD3 3 CYS C 281 GLN C 282 -1 N CYS C 281 O ILE C 288 SHEET 3 AD3 3 ILE C 302 GLY C 303 -1 O ILE C 302 N GLN C 282 SHEET 1 AD4 2 PHE C 294 HIS C 295 0 SHEET 2 AD4 2 LYS C 307 TYR C 308 1 O LYS C 307 N HIS C 295 SHEET 1 AD5 2 ALA c 130 GLU c 132 0 SHEET 2 AD5 2 PHE c 138 PHE c 140 -1 O GLU c 139 N LYS c 131 SSBOND 1 CYS H 22 CYS H 92 1555 1555 2.03 SSBOND 2 CYS L 23 CYS L 88 1555 1555 2.03 SSBOND 3 CYS B 52 CYS B 277 1555 1555 2.03 SSBOND 4 CYS B 64 CYS B 76 1555 1555 2.02 SSBOND 5 CYS B 97 CYS B 139 1555 1555 2.02 SSBOND 6 CYS B 281 CYS B 305 1555 1555 2.02 SSBOND 7 CYS b 144 CYS b 148 1555 1555 2.03 SSBOND 8 CYS A 64 CYS A 76 1555 1555 2.03 SSBOND 9 CYS A 97 CYS A 139 1555 1555 2.03 SSBOND 10 CYS A 281 CYS A 305 1555 1555 2.03 SSBOND 11 CYS a 144 CYS a 148 1555 1555 2.03 SSBOND 12 CYS C 52 CYS C 277 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 c 144 CYS c 148 1555 1555 2.05 LINK ND2 ASN B 21 C1 NAG B 403 1555 1555 1.44 LINK ND2 ASN B 33 C1 NAG B 402 1555 1555 1.44 LINK ND2 ASN B 169 C1 NAG B 401 1555 1555 1.44 LINK ND2 ASN B 289 C1 NAG B 404 1555 1555 1.44 LINK ND2 ASN b 154 C1 NAG b 301 1555 1555 1.44 LINK ND2 ASN A 21 C1 NAG A 404 1555 1555 1.44 LINK ND2 ASN A 33 C1 NAG A 402 1555 1555 1.44 LINK ND2 ASN A 169 C1 NAG A 401 1555 1555 1.44 LINK ND2 ASN A 289 C1 NAG A 403 1555 1555 1.45 LINK ND2 ASN a 154 C1 NAG a 301 1555 1555 1.45 LINK ND2 ASN C 21 C1 NAG C 403 1555 1555 1.44 LINK ND2 ASN C 33 C1 NAG C 402 1555 1555 1.44 LINK ND2 ASN C 169 C1 NAG C 401 1555 1555 1.44 LINK ND2 ASN C 289 C1 NAG C 404 1555 1555 1.45 LINK ND2 ASN c 154 C1 NAG c 301 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