HEADER VIRAL PROTEIN/IMMUNE SYSTEM 01-JAN-25 9MQ2 TITLE CRYO-EM MAP OF H5 HA (A/JIANGSU/NJ210/2023) IN COMPLEX WITH MONOCLONAL TITLE 2 FAB 12G1 COMPND MOL_ID: 1; COMPND 2 MOLECULE: HEMAGGLUTININ HA1; COMPND 3 CHAIN: A, B, C; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: 12G1 HEAVY CHAIN FAB; COMPND 7 CHAIN: H; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: 12G1 LIGHT CHAIN FAB; COMPND 11 CHAIN: L; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 4; COMPND 14 MOLECULE: HEMAGGLUTININ HA2; COMPND 15 CHAIN: a, b, c; COMPND 16 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS; SOURCE 3 ORGANISM_TAXID: 11320; SOURCE 4 STRAIN: A/JIANGSU/NJ210/2023; SOURCE 5 GENE: HA; SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HEK293; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 13 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 14 EXPRESSION_SYSTEM_CELL_LINE: HEK293; 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 EXPRESSION_SYSTEM_CELL_LINE: HEK293; SOURCE 21 MOL_ID: 4; SOURCE 22 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS; SOURCE 23 ORGANISM_TAXID: 11320; SOURCE 24 STRAIN: A/JIANGSU/NJ210/2023; SOURCE 25 GENE: HA; SOURCE 26 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 27 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 28 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 9MQ2 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. 3.06 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : PHENIX, 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) : 3.060 REMARK 3 NUMBER OF PARTICLES : 61353 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 9MQ2 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_1000291526. 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 REMARK 245 12G1 AND CR9114 REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 0.86 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 II (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) : 4485.00 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: A, B, C, H, L, a, b, c, D, E, REMARK 350 AND CHAINS: F 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 -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 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 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 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 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 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 a 1 REMARK 465 TYR a 158 REMARK 465 TYR a 159 REMARK 465 PRO a 160 REMARK 465 GLN a 161 REMARK 465 TYR a 162 REMARK 465 SER a 163 REMARK 465 GLU a 164 REMARK 465 GLU a 165 REMARK 465 ALA a 166 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 GLY b 1 REMARK 465 LEU b 2 REMARK 465 PHE b 3 REMARK 465 GLY b 4 REMARK 465 ALA b 5 REMARK 465 ILE b 6 REMARK 465 ALA b 7 REMARK 465 GLY b 8 REMARK 465 PHE b 9 REMARK 465 ILE b 10 REMARK 465 TYR b 158 REMARK 465 TYR b 159 REMARK 465 PRO b 160 REMARK 465 GLN b 161 REMARK 465 TYR b 162 REMARK 465 SER b 163 REMARK 465 GLU b 164 REMARK 465 GLU b 165 REMARK 465 ALA b 166 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 GLY c 1 REMARK 465 TYR c 158 REMARK 465 TYR c 159 REMARK 465 PRO c 160 REMARK 465 GLN c 161 REMARK 465 TYR c 162 REMARK 465 SER c 163 REMARK 465 GLU c 164 REMARK 465 GLU c 165 REMARK 465 ALA c 166 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 GLU b 103 OG1 THR b 107 2.10 REMARK 500 OG SER b 113 O LEU c 2 2.11 REMARK 500 O GLU a 103 OG1 THR a 107 2.17 REMARK 500 OD1 ASN C 150 OH TYR C 258 2.19 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 CYS A 76 57.93 -95.60 REMARK 500 ASN A 129 34.60 -99.36 REMARK 500 SER A 247 135.45 -170.97 REMARK 500 CYS B 76 53.13 -92.35 REMARK 500 ASN B 248 13.71 -140.04 REMARK 500 SER B 265 -175.84 -170.79 REMARK 500 SER B 270 143.26 -170.53 REMARK 500 THR B 318 35.55 -98.86 REMARK 500 LYS C 157 -61.14 -96.82 REMARK 500 SER H 31 10.31 -142.23 REMARK 500 LYS H 43 -131.86 61.27 REMARK 500 ALA H 88 -169.51 -166.25 REMARK 500 SER L 10 110.92 -160.10 REMARK 500 GLU L 81 -1.85 77.84 REMARK 500 ASN a 71 -169.65 -76.74 REMARK 500 LEU a 73 -168.60 -79.58 REMARK 500 ASP a 128 -12.60 84.91 REMARK 500 ALA b 130 -176.28 -170.04 REMARK 500 LEU b 133 -133.62 52.25 REMARK 500 THR b 156 33.83 -99.53 REMARK 500 ALA c 5 -3.24 82.10 REMARK 500 ASP c 19 -1.87 76.71 REMARK 500 ASN c 28 -169.16 -166.62 REMARK 500 ARG c 127 -121.30 64.56 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-48511 RELATED DB: EMDB REMARK 900 CRYO-EM MAP OF H5 HA (A/JIANGSU/NJ210/2023) IN COMPLEX WITH REMARK 900 MONOCLONAL FAB 12G1 DBREF1 9MQ2 A -5 332 UNP A0A8E4ZAK5_9INFA DBREF2 9MQ2 A A0A8E4ZAK5 1 345 DBREF1 9MQ2 B -5 332 UNP A0A8E4ZAK5_9INFA DBREF2 9MQ2 B A0A8E4ZAK5 1 345 DBREF1 9MQ2 C -5 332 UNP A0A8E4ZAK5_9INFA DBREF2 9MQ2 C A0A8E4ZAK5 1 345 DBREF 9MQ2 H 1 110 PDB 9MQ2 9MQ2 1 110 DBREF 9MQ2 L 1 106 PDB 9MQ2 9MQ2 1 106 DBREF1 9MQ2 a 1 176 UNP A0AAX6NNL9_9INFA DBREF2 9MQ2 a A0AAX6NNL9 346 521 DBREF1 9MQ2 b 1 176 UNP A0AAX6NNL9_9INFA DBREF2 9MQ2 b A0AAX6NNL9 346 521 DBREF1 9MQ2 c 1 176 UNP A0AAX6NNL9_9INFA DBREF2 9MQ2 c A0AAX6NNL9 346 521 SEQADV 9MQ2 ASN A 6 UNP A0A8E4ZAK SER 12 CONFLICT SEQADV 9MQ2 ASP A 91 UNP A0A8E4ZAK ALA 99 CONFLICT SEQADV 9MQ2 ASP A 158 UNP A0A8E4ZAK ASN 170 CONFLICT SEQADV 9MQ2 PRO A 325 UNP A0A8E4ZAK LEU 338 CONFLICT SEQADV 9MQ2 ASN B 6 UNP A0A8E4ZAK SER 12 CONFLICT SEQADV 9MQ2 ASP B 91 UNP A0A8E4ZAK ALA 99 CONFLICT SEQADV 9MQ2 ASP B 158 UNP A0A8E4ZAK ASN 170 CONFLICT SEQADV 9MQ2 PRO B 325 UNP A0A8E4ZAK LEU 338 CONFLICT SEQADV 9MQ2 ASN C 6 UNP A0A8E4ZAK SER 12 CONFLICT SEQADV 9MQ2 ASP C 91 UNP A0A8E4ZAK ALA 99 CONFLICT SEQADV 9MQ2 ASP C 158 UNP A0A8E4ZAK ASN 170 CONFLICT SEQADV 9MQ2 PRO C 325 UNP A0A8E4ZAK LEU 338 CONFLICT SEQADV 9MQ2 GLY a 177 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 TYR a 178 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 ILE a 179 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 PRO a 180 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 GLU a 181 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 ALA a 182 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 PRO a 183 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 ARG a 184 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 ASP a 185 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 GLY a 186 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 GLN a 187 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 ALA a 188 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 TYR a 189 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 VAL a 190 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 ARG a 191 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 LYS a 192 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 ASP a 193 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 GLY a 194 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 GLU a 195 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 TRP a 196 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 VAL a 197 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 LEU a 198 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 LEU a 199 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 SER a 200 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 THR a 201 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 PHE a 202 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 LEU a 203 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 GLY a 204 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 SER a 205 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 GLU a 206 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 ASN a 207 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 LEU a 208 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 TYR a 209 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 PHE a 210 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 GLN a 211 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 GLY a 212 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 GLY a 213 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 SER a 214 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 HIS a 215 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 HIS a 216 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 HIS a 217 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 HIS a 218 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 HIS a 219 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 HIS a 220 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 GLY b 177 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 TYR b 178 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 ILE b 179 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 PRO b 180 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 GLU b 181 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 ALA b 182 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 PRO b 183 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 ARG b 184 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 ASP b 185 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 GLY b 186 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 GLN b 187 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 ALA b 188 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 TYR b 189 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 VAL b 190 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 ARG b 191 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 LYS b 192 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 ASP b 193 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 GLY b 194 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 GLU b 195 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 TRP b 196 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 VAL b 197 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 LEU b 198 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 LEU b 199 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 SER b 200 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 THR b 201 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 PHE b 202 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 LEU b 203 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 GLY b 204 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 SER b 205 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 GLU b 206 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 ASN b 207 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 LEU b 208 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 TYR b 209 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 PHE b 210 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 GLN b 211 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 GLY b 212 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 GLY b 213 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 SER b 214 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 HIS b 215 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 HIS b 216 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 HIS b 217 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 HIS b 218 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 HIS b 219 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 HIS b 220 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 GLY c 177 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 TYR c 178 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 ILE c 179 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 PRO c 180 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 GLU c 181 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 ALA c 182 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 PRO c 183 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 ARG c 184 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 ASP c 185 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 GLY c 186 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 GLN c 187 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 ALA c 188 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 TYR c 189 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 VAL c 190 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 ARG c 191 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 LYS c 192 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 ASP c 193 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 GLY c 194 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 GLU c 195 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 TRP c 196 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 VAL c 197 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 LEU c 198 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 LEU c 199 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 SER c 200 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 THR c 201 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 PHE c 202 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 LEU c 203 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 GLY c 204 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 SER c 205 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 GLU c 206 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 ASN c 207 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 LEU c 208 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 TYR c 209 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 PHE c 210 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 GLN c 211 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 GLY c 212 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 GLY c 213 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 SER c 214 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 HIS c 215 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 HIS c 216 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 HIS c 217 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 HIS c 218 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 HIS c 219 UNP A0AAX6NNL EXPRESSION TAG SEQADV 9MQ2 HIS c 220 UNP A0AAX6NNL EXPRESSION TAG 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 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 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 H 122 GLN VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 H 122 PRO SER GLU THR LEU SER LEU THR CYS THR VAL SER GLY SEQRES 3 H 122 ASP SER ILE SER SER TYR TYR TRP SER TRP ILE ARG GLN SEQRES 4 H 122 PRO PRO GLY LYS GLY LEU GLU TRP ILE GLY TYR VAL HIS SEQRES 5 H 122 TYR SER GLY ASN THR ASN TYR ASN PRO SER LEU LYS SER SEQRES 6 H 122 ARG VAL THR ILE SER VAL ASP THR SER LYS ASN GLN PHE SEQRES 7 H 122 SER LEU LYS LEU SER SER VAL THR ALA ALA ASP THR ALA SEQRES 8 H 122 VAL TYR TYR CYS ALA ARG THR THR MET SER ARG GLY PRO SEQRES 9 H 122 SER LEU TYR TYR TYR TYR GLY LEU ASP VAL TRP GLY GLN SEQRES 10 H 122 GLY THR THR VAL THR SEQRES 1 L 111 ASP ILE VAL MET THR GLN SER PRO LEU SER LEU PRO VAL SEQRES 2 L 111 THR PRO GLY GLU PRO ALA SER ILE SER CYS ARG SER SER SEQRES 3 L 111 GLN SER LEU LEU HIS SER TYR GLY TYR ILE TYR LEU ASP SEQRES 4 L 111 TRP TYR LEU GLN LYS PRO GLY GLN SER PRO GLN LEU LEU SEQRES 5 L 111 ILE TYR LEU GLY SER ASP ARG ALA SER GLY ILE PRO ASP SEQRES 6 L 111 ARG PHE SER GLY SER GLY ALA GLY THR ASP PHE THR LEU SEQRES 7 L 111 LYS ILE SER ARG VAL GLU ALA GLU ASP VAL GLY VAL TYR SEQRES 8 L 111 TYR CYS MET GLN ALA LEU GLN THR PRO ILE THR PHE GLY SEQRES 9 L 111 GLN GLY THR ARG LEU GLU ILE 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 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 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 D 1 14 HET NAG D 2 14 HET FUC D 3 10 HET NAG E 1 14 HET NAG E 2 14 HET FUC E 3 10 HET NAG F 1 14 HET NAG F 2 14 HET FUC F 3 10 HET NAG A 401 14 HET NAG A 402 14 HET NAG A 403 14 HET NAG B 401 14 HET NAG B 402 14 HET NAG B 403 14 HET NAG C 401 14 HET NAG C 402 14 HET NAG C 403 14 HET NAG a 301 14 HET NAG c 301 14 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM FUC ALPHA-L-FUCOPYRANOSE 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 FORMUL 9 NAG 17(C8 H15 N O6) FORMUL 9 FUC 3(C6 H12 O5) HELIX 1 AA1 SER A 65 GLY A 72 1 8 HELIX 2 AA2 CYS A 76 ILE A 80 5 5 HELIX 3 AA3 ASP A 104 SER A 113 1 10 HELIX 4 AA4 PRO A 125 TRP A 127 5 5 HELIX 5 AA5 ASN A 187 TYR A 195 1 9 HELIX 6 AA6 SER B 65 GLY B 72 1 8 HELIX 7 AA7 CYS B 76 ILE B 80 5 5 HELIX 8 AA8 ASP B 104 SER B 113 1 10 HELIX 9 AA9 PRO B 125 TRP B 127 5 5 HELIX 10 AB1 ASN B 187 TYR B 195 1 9 HELIX 11 AB2 SER C 65 GLY C 72 1 8 HELIX 12 AB3 ASP C 104 SER C 113 1 10 HELIX 13 AB4 PRO C 125 TRP C 127 5 5 HELIX 14 AB5 ASN C 187 TYR C 195 1 9 HELIX 15 AB6 ASP a 37 MET a 59 1 23 HELIX 16 AB7 GLU a 74 ARG a 127 1 54 HELIX 17 AB8 ASP a 145 GLY a 155 1 11 HELIX 18 AB9 ASP b 37 MET b 59 1 23 HELIX 19 AC1 GLU b 74 ASP b 120 1 47 HELIX 20 AC2 ASP b 120 GLN b 125 1 6 HELIX 21 AC3 ASP b 145 GLY b 155 1 11 HELIX 22 AC4 ASP c 37 MET c 59 1 23 HELIX 23 AC5 GLU c 74 GLU c 103 1 30 HELIX 24 AC6 ASN c 104 ARG c 127 1 24 HELIX 25 AC7 ASP c 145 GLY c 155 1 11 SHEET 1 AA1 3 CYS A 14 ILE A 15 0 SHEET 2 AA1 3 TYR a 24 SER a 27 -1 O HIS a 25 N CYS A 14 SHEET 3 AA1 3 SER a 32 ALA a 35 -1 O ALA a 35 N TYR a 24 SHEET 1 AA2 2 GLU 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 GLN A 40 ASP A 41 0 SHEET 2 AA3 2 VAL A 315 LEU A 316 -1 O LEU A 316 N GLN A 40 SHEET 1 AA4 3 LEU A 43 GLU A 44 0 SHEET 2 AA4 3 PHE A 294 HIS 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 HIS A 295 SHEET 1 AA5 2 LEU A 51 LEU A 54 0 SHEET 2 AA5 2 TYR A 274 THR A 279 1 O CYS A 277 N ASP A 53 SHEET 1 AA6 3 LEU A 59 ILE A 60 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 LYS A 269 1 O MET A 268 N ILE A 87 SHEET 1 AA7 5 GLY A 100 LEU A 102 0 SHEET 2 AA7 5 ARG A 229 LEU A 237 1 O PHE A 232 N SER A 101 SHEET 3 AA7 5 LEU A 176 HIS A 184 -1 N LEU A 176 O LEU A 237 SHEET 4 AA7 5 TYR A 256 LYS A 262A-1 O TYR A 258 N LEU A 177 SHEET 5 AA7 5 ILE A 115 LEU A 122 -1 N ILE A 121 O ALA A 257 SHEET 1 AA8 5 GLY A 100 LEU A 102 0 SHEET 2 AA8 5 ARG A 229 LEU A 237 1 O PHE A 232 N SER A 101 SHEET 3 AA8 5 LEU A 176 HIS A 184 -1 N LEU A 176 O LEU A 237 SHEET 4 AA8 5 PHE A 251 PRO A 254 -1 O ILE A 252 N GLY A 181 SHEET 5 AA8 5 VAL A 151 TRP A 153 -1 N VAL A 152 O ALA A 253 SHEET 1 AA9 2 SER A 136 TYR A 141 0 SHEET 2 AA9 2 ALA A 144 SER A 146 -1 O ALA A 144 N TYR A 141 SHEET 1 AB1 4 ILE A 164 ASN A 169 0 SHEET 2 AB1 4 ALA A 242 SER A 247 -1 O PHE A 245 N ILE A 166 SHEET 3 AB1 4 ILE A 202 GLY A 205 -1 N GLY A 205 O HIS A 244 SHEET 4 AB1 4 ASN A 210 LEU A 213 -1 O GLN A 211 N VAL A 204 SHEET 1 AB2 2 CYS A 281 GLN A 282 0 SHEET 2 AB2 2 ILE A 302 GLY A 303 -1 O ILE A 302 N GLN A 282 SHEET 1 AB3 2 CYS B 14 ILE B 15 0 SHEET 2 AB3 2 TYR b 24 HIS b 25 -1 O HIS b 25 N CYS B 14 SHEET 1 AB4 2 GLN B 25 VAL B 26 0 SHEET 2 AB4 2 VAL B 34 THR B 35 -1 O VAL B 34 N VAL B 26 SHEET 1 AB5 2 ALA B 39 ASP B 41 0 SHEET 2 AB5 2 VAL B 315 ALA B 317 -1 O LEU B 316 N GLN B 40 SHEET 1 AB6 3 LEU B 43 GLU B 44 0 SHEET 2 AB6 3 PHE B 294 HIS B 295 1 O PHE B 294 N GLU B 44 SHEET 3 AB6 3 LYS B 307 TYR B 308 1 O LYS B 307 N HIS B 295 SHEET 1 AB7 2 LEU B 51 LEU B 54 0 SHEET 2 AB7 2 TYR B 274 THR B 279 1 O CYS B 277 N ASP B 53 SHEET 1 AB8 3 LEU B 59 LEU B 61 0 SHEET 2 AB8 3 ILE B 87 GLU B 89 1 O VAL B 88 N LEU B 59 SHEET 3 AB8 3 ILE B 267 LYS B 269 1 O MET B 268 N ILE B 87 SHEET 1 AB9 5 GLY B 100 LEU B 102 0 SHEET 2 AB9 5 ARG B 229 LEU B 237 1 O MET B 230 N SER B 101 SHEET 3 AB9 5 ASP B 175 HIS B 184 -1 N LEU B 176 O LEU B 237 SHEET 4 AB9 5 TYR B 256 LYS B 262 -1 O ILE B 260 N ASP B 175 SHEET 5 AB9 5 HIS B 117 LEU B 122 -1 N ILE B 121 O ALA B 257 SHEET 1 AC1 5 GLY B 100 LEU B 102 0 SHEET 2 AC1 5 ARG B 229 LEU B 237 1 O MET B 230 N SER B 101 SHEET 3 AC1 5 ASP B 175 HIS B 184 -1 N LEU B 176 O LEU B 237 SHEET 4 AC1 5 PHE B 251 PRO B 254 -1 O ILE B 252 N GLY B 181 SHEET 5 AC1 5 VAL B 151 TRP B 153 -1 N VAL B 152 O ALA B 253 SHEET 1 AC2 2 SER B 136 TYR B 141 0 SHEET 2 AC2 2 ALA B 144 SER B 146 -1 O ALA B 144 N TYR B 141 SHEET 1 AC3 5 ASN B 210 LEU B 213 0 SHEET 2 AC3 5 ILE B 202 GLY B 205 -1 N VAL B 204 O GLN B 211 SHEET 3 AC3 5 ALA B 242 SER B 247 -1 O GLU B 246 N SER B 203 SHEET 4 AC3 5 ILE B 164 ASN B 169 -1 N ILE B 166 O PHE B 245 SHEET 5 AC3 5 LEU H 100C TYR H 100D-1 O TYR H 100D N SER B 167 SHEET 1 AC4 2 CYS B 281 GLN B 282 0 SHEET 2 AC4 2 ILE B 302 GLY B 303 -1 O ILE B 302 N GLN B 282 SHEET 1 AC5 2 GLN C 25 VAL C 26 0 SHEET 2 AC5 2 VAL C 34 THR C 35 -1 O VAL C 34 N VAL C 26 SHEET 1 AC6 2 GLN C 40 ASP C 41 0 SHEET 2 AC6 2 VAL C 315 LEU C 316 -1 O LEU C 316 N GLN C 40 SHEET 1 AC7 2 LEU C 51 LEU C 54 0 SHEET 2 AC7 2 TYR C 274 THR C 279 1 O CYS C 277 N ASP C 53 SHEET 1 AC8 2 LEU C 59 LEU C 61 0 SHEET 2 AC8 2 ILE C 87 GLU C 89 1 O VAL C 88 N LEU C 61 SHEET 1 AC9 5 GLY C 100 LEU C 102 0 SHEET 2 AC9 5 ARG C 229 LEU C 237 1 O PHE C 232 N SER C 101 SHEET 3 AC9 5 LEU C 176 HIS C 184 -1 N LEU C 176 O LEU C 237 SHEET 4 AC9 5 TYR C 256 LYS C 262A-1 O TYR C 258 N LEU C 177 SHEET 5 AC9 5 ILE C 115 LEU C 122 -1 N GLU C 119 O LYS C 259 SHEET 1 AD1 5 GLY C 100 LEU C 102 0 SHEET 2 AD1 5 ARG C 229 LEU C 237 1 O PHE C 232 N SER C 101 SHEET 3 AD1 5 LEU C 176 HIS C 184 -1 N LEU C 176 O LEU C 237 SHEET 4 AD1 5 PHE C 251 PRO C 254 -1 O ILE C 252 N GLY C 181 SHEET 5 AD1 5 VAL C 151 TRP C 153 -1 N VAL C 152 O ALA C 253 SHEET 1 AD2 2 SER C 136 TYR C 141 0 SHEET 2 AD2 2 ALA C 144 SER C 146 -1 O ALA C 144 N TYR C 141 SHEET 1 AD3 4 ILE C 164 ASN C 169 0 SHEET 2 AD3 4 ALA C 242 SER C 247 -1 O PHE C 245 N ILE C 166 SHEET 3 AD3 4 ILE C 202 THR C 206 -1 N SER C 203 O GLU C 246 SHEET 4 AD3 4 LEU C 209 LEU C 213 -1 O LEU C 213 N ILE C 202 SHEET 1 AD4 3 ALA C 287 ILE C 288 0 SHEET 2 AD4 3 CYS C 281 GLN C 282 -1 N CYS C 281 O ILE C 288 SHEET 3 AD4 3 ILE C 302 GLY C 303 -1 O ILE C 302 N GLN C 282 SHEET 1 AD5 2 PHE C 294 HIS C 295 0 SHEET 2 AD5 2 LYS C 307 TYR C 308 1 O LYS C 307 N HIS C 295 SHEET 1 AD6 3 GLN H 3 SER H 7 0 SHEET 2 AD6 3 LEU H 20 SER H 25 -1 O THR H 23 N GLN H 5 SHEET 3 AD6 3 GLN H 77 LEU H 80 -1 O PHE H 78 N CYS H 22 SHEET 1 AD7 5 THR H 57 TYR H 59 0 SHEET 2 AD7 5 GLU H 46 VAL H 51 -1 N TYR H 50 O ASN H 58 SHEET 3 AD7 5 TRP H 34 GLN H 39 -1 N ARG H 38 O GLU H 46 SHEET 4 AD7 5 ALA H 88 ARG H 94 -1 O VAL H 89 N GLN H 39 SHEET 5 AD7 5 VAL H 102 TRP H 103 -1 O VAL H 102 N ARG H 94 SHEET 1 AD8 5 THR H 57 TYR H 59 0 SHEET 2 AD8 5 GLU H 46 VAL H 51 -1 N TYR H 50 O ASN H 58 SHEET 3 AD8 5 TRP H 34 GLN H 39 -1 N ARG H 38 O GLU H 46 SHEET 4 AD8 5 ALA H 88 ARG H 94 -1 O VAL H 89 N GLN H 39 SHEET 5 AD8 5 THR H 107 VAL H 109 -1 O THR H 107 N TYR H 90 SHEET 1 AD9 4 MET L 4 GLN L 6 0 SHEET 2 AD9 4 ALA L 19 SER L 25 -1 O ARG L 24 N THR L 5 SHEET 3 AD9 4 ASP L 70 ILE L 75 -1 O PHE L 71 N CYS L 23 SHEET 4 AD9 4 PHE L 62 ALA L 67 -1 N SER L 65 O THR L 72 SHEET 1 AE1 5 ASP L 53 ARG L 54 0 SHEET 2 AE1 5 PRO L 44 TYR L 49 -1 N TYR L 49 O ASP L 53 SHEET 3 AE1 5 LEU L 33 GLN L 38 -1 N LEU L 37 O GLN L 45 SHEET 4 AE1 5 VAL L 85 GLN L 90 -1 O MET L 89 N ASP L 34 SHEET 5 AE1 5 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90 SHEET 1 AE2 2 ALA a 130 GLU a 132 0 SHEET 2 AE2 2 PHE a 138 PHE a 140 -1 O GLU a 139 N LYS a 131 SHEET 1 AE3 2 HIS c 26 SER c 27 0 SHEET 2 AE3 2 SER c 32 GLY c 33 -1 O GLY c 33 N HIS c 26 SHEET 1 AE4 2 ALA c 130 GLU c 132 0 SHEET 2 AE4 2 PHE c 138 PHE c 140 -1 O GLU c 139 N LYS c 131 SSBOND 1 CYS A 52 CYS A 277 1555 1555 2.03 SSBOND 2 CYS A 64 CYS A 76 1555 1555 2.03 SSBOND 3 CYS A 97 CYS A 139 1555 1555 2.03 SSBOND 4 CYS A 281 CYS A 305 1555 1555 2.03 SSBOND 5 CYS B 52 CYS B 277 1555 1555 2.03 SSBOND 6 CYS B 64 CYS B 76 1555 1555 2.03 SSBOND 7 CYS B 97 CYS B 139 1555 1555 2.03 SSBOND 8 CYS B 281 CYS B 305 1555 1555 2.03 SSBOND 9 CYS C 52 CYS C 277 1555 1555 2.03 SSBOND 10 CYS C 64 CYS C 76 1555 1555 2.03 SSBOND 11 CYS C 97 CYS C 139 1555 1555 2.03 SSBOND 12 CYS C 281 CYS C 305 1555 1555 2.03 SSBOND 13 CYS H 22 CYS H 92 1555 1555 2.03 SSBOND 14 CYS L 23 CYS L 88 1555 1555 2.03 SSBOND 15 CYS a 144 CYS a 148 1555 1555 2.04 SSBOND 16 CYS b 144 CYS b 148 1555 1555 2.03 LINK ND2 ASN A 21 C1 NAG A 401 1555 1555 1.45 LINK ND2 ASN A 33 C1 NAG A 402 1555 1555 1.44 LINK ND2 ASN A 169 C1 NAG D 1 1555 1555 1.44 LINK ND2 ASN A 289 C1 NAG A 403 1555 1555 1.44 LINK ND2 ASN B 21 C1 NAG B 402 1555 1555 1.44 LINK ND2 ASN B 33 C1 NAG B 403 1555 1555 1.44 LINK ND2 ASN B 169 C1 NAG E 1 1555 1555 1.44 LINK ND2 ASN B 289 C1 NAG B 401 1555 1555 1.44 LINK ND2 ASN C 21 C1 NAG C 402 1555 1555 1.44 LINK ND2 ASN C 33 C1 NAG C 403 1555 1555 1.44 LINK ND2 ASN C 169 C1 NAG F 1 1555 1555 1.43 LINK ND2 ASN C 289 C1 NAG C 401 1555 1555 1.45 LINK ND2 ASN a 154 C1 NAG a 301 1555 1555 1.45 LINK ND2 ASN c 154 C1 NAG c 301 1555 1555 1.44 LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.44 LINK O6 NAG D 1 C1 FUC D 3 1555 1555 1.45 LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.44 LINK O6 NAG E 1 C1 FUC E 3 1555 1555 1.44 LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.44 LINK O6 NAG F 1 C1 FUC F 3 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