HEADER VIRAL PROTEIN/IMMUNE SYSTEM 06-FEB-25 9N7T TITLE H5 HEMAGGLUTININ (A/JIANGSU/NJ210/2023) IN COMPLEX WITH CENTRAL STEM- TITLE 2 TARGETING FAB ST14 COMPND MOL_ID: 1; COMPND 2 MOLECULE: H5 HA1; COMPND 3 CHAIN: A, B, C; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: ST14 LIGHT CHAIN FAB; COMPND 7 CHAIN: L, F, G; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: ST14 HEAVY CHAIN FAB; COMPND 11 CHAIN: H, D, E; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 4; COMPND 14 MOLECULE: H5 HA2; COMPND 15 CHAIN: a, I, J; 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 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 7 EXPRESSION_SYSTEM_CELL_LINE: HEK293; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_TAXID: 9606; SOURCE 11 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 13 EXPRESSION_SYSTEM_CELL_LINE: HEK293; SOURCE 14 MOL_ID: 3; SOURCE 15 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 16 ORGANISM_TAXID: 9606; SOURCE 17 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 18 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 19 EXPRESSION_SYSTEM_CELL_LINE: HEK293; SOURCE 20 MOL_ID: 4; SOURCE 21 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS; SOURCE 22 ORGANISM_TAXID: 11320; SOURCE 23 STRAIN: A/JIANGSU/NJ210/2023; SOURCE 24 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 25 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 26 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 P.J.M.BROUWER,J.R.LOEFFLER,J.A.FERGUSON,A.J.RODRIGUEZ,J.HAN,A.B.WARD REVDAT 1 18-FEB-26 9N7T 0 JRNL AUTH A.FISHER,M.CORCORAN,M.CHERNYSHEV,P.J.M.BROUWER,R.GILLESPIE, JRNL AUTH 2 A.NICOLETTO,J.R.LOEFFLER,J.A.FERGUSON,A.J.RODRIGUEZ, JRNL AUTH 3 S.NARANG,M.ADORI,D.ANGELETTI,M.J.VAN GILS,X.CASTRO DOPICO, JRNL AUTH 4 M.KANEKIYO,A.B.WARD,J.HAN,G.B.KARLSSON HEDESTAM JRNL TITL INDIVIDUALIZED IG GENOTYPING COUPLED WITH HIGH THROUGHPUT JRNL TITL 2 ISOLATION OF INFLUENZA HA-SPECIFIC MONOCLONAL ANTIBODIES JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.01 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : PHENIX 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) : 3.010 REMARK 3 NUMBER OF PARTICLES : 114222 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 9N7T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-FEB-25. REMARK 100 THE DEPOSITION ID IS D_1000292623. 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 HEMAGGLUTININ REMARK 245 (A/JIANGSU/NJ210/2023) IN REMARK 245 COMPLEX WITH CENTRAL STEM- REMARK 245 TARGETING FAB ST14 REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 0.90 REMARK 245 SAMPLE SUPPORT DETAILS : 15MA 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 IV (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 700.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 1800.00 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) : 4194.00 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: 12-MERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: 12-MERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, L, H, a, B, F, D, I, C, G, REMARK 350 AND CHAINS: E, J, K, M, N, O, P, Q 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 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 SER L 2 REMARK 465 ALA L 3 REMARK 465 VAL L 106 REMARK 465 LEU L 107 REMARK 465 GLY a 1 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 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 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 SER F 2 REMARK 465 ALA F 3 REMARK 465 VAL F 106 REMARK 465 LEU F 107 REMARK 465 GLY I 1 REMARK 465 GLU I 171 REMARK 465 GLU I 172 REMARK 465 ILE I 173 REMARK 465 SER I 174 REMARK 465 GLY I 175 REMARK 465 VAL I 176 REMARK 465 GLY I 177 REMARK 465 TYR I 178 REMARK 465 ILE I 179 REMARK 465 PRO I 180 REMARK 465 GLU I 181 REMARK 465 ALA I 182 REMARK 465 PRO I 183 REMARK 465 ARG I 184 REMARK 465 ASP I 185 REMARK 465 GLY I 186 REMARK 465 GLN I 187 REMARK 465 ALA I 188 REMARK 465 TYR I 189 REMARK 465 VAL I 190 REMARK 465 ARG I 191 REMARK 465 LYS I 192 REMARK 465 ASP I 193 REMARK 465 GLY I 194 REMARK 465 GLU I 195 REMARK 465 TRP I 196 REMARK 465 VAL I 197 REMARK 465 LEU I 198 REMARK 465 LEU I 199 REMARK 465 SER I 200 REMARK 465 THR I 201 REMARK 465 PHE I 202 REMARK 465 LEU I 203 REMARK 465 GLY I 204 REMARK 465 SER I 205 REMARK 465 GLU I 206 REMARK 465 ASN I 207 REMARK 465 LEU I 208 REMARK 465 TYR I 209 REMARK 465 PHE I 210 REMARK 465 GLN I 211 REMARK 465 GLY I 212 REMARK 465 GLY I 213 REMARK 465 SER I 214 REMARK 465 HIS I 215 REMARK 465 HIS I 216 REMARK 465 HIS I 217 REMARK 465 HIS I 218 REMARK 465 HIS I 219 REMARK 465 HIS I 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 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 SER G 2 REMARK 465 ALA G 3 REMARK 465 VAL G 106 REMARK 465 LEU G 107 REMARK 465 GLY J 1 REMARK 465 GLU J 171 REMARK 465 GLU J 172 REMARK 465 ILE J 173 REMARK 465 SER J 174 REMARK 465 GLY J 175 REMARK 465 VAL J 176 REMARK 465 GLY J 177 REMARK 465 TYR J 178 REMARK 465 ILE J 179 REMARK 465 PRO J 180 REMARK 465 GLU J 181 REMARK 465 ALA J 182 REMARK 465 PRO J 183 REMARK 465 ARG J 184 REMARK 465 ASP J 185 REMARK 465 GLY J 186 REMARK 465 GLN J 187 REMARK 465 ALA J 188 REMARK 465 TYR J 189 REMARK 465 VAL J 190 REMARK 465 ARG J 191 REMARK 465 LYS J 192 REMARK 465 ASP J 193 REMARK 465 GLY J 194 REMARK 465 GLU J 195 REMARK 465 TRP J 196 REMARK 465 VAL J 197 REMARK 465 LEU J 198 REMARK 465 LEU J 199 REMARK 465 SER J 200 REMARK 465 THR J 201 REMARK 465 PHE J 202 REMARK 465 LEU J 203 REMARK 465 GLY J 204 REMARK 465 SER J 205 REMARK 465 GLU J 206 REMARK 465 ASN J 207 REMARK 465 LEU J 208 REMARK 465 TYR J 209 REMARK 465 PHE J 210 REMARK 465 GLN J 211 REMARK 465 GLY J 212 REMARK 465 GLY J 213 REMARK 465 SER J 214 REMARK 465 HIS J 215 REMARK 465 HIS J 216 REMARK 465 HIS J 217 REMARK 465 HIS J 218 REMARK 465 HIS J 219 REMARK 465 HIS J 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 ASP G 27B OG SER G 90 2.13 REMARK 500 O ASP F 27B OG SER F 90 2.13 REMARK 500 O ASP L 27B OG SER L 90 2.13 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 ASP A 63 -7.47 75.34 REMARK 500 ASP A 95 -160.74 -77.48 REMARK 500 LEU A 96 108.96 -54.74 REMARK 500 ALA A 160 -62.00 -99.85 REMARK 500 TYR A 161 72.99 48.81 REMARK 500 LYS A 196 -7.82 73.83 REMARK 500 ASN L 31 57.54 -95.15 REMARK 500 VAL L 51 -65.76 68.16 REMARK 500 HIS L 95B -65.11 71.70 REMARK 500 ASN a 71 -169.74 -79.62 REMARK 500 ARG a 127 -95.09 58.80 REMARK 500 ASP B 63 -7.48 75.28 REMARK 500 ASP B 95 -160.74 -77.49 REMARK 500 LEU B 96 108.99 -54.71 REMARK 500 ALA B 160 -62.03 -99.80 REMARK 500 TYR B 161 73.05 48.81 REMARK 500 LYS B 196 -7.91 73.93 REMARK 500 ASN F 31 57.53 -95.17 REMARK 500 VAL F 51 -65.67 68.15 REMARK 500 HIS F 95B -65.07 71.66 REMARK 500 ASN I 71 -169.75 -79.56 REMARK 500 ARG I 127 -95.08 58.82 REMARK 500 ASP C 63 -7.51 75.28 REMARK 500 ASP C 95 -160.77 -77.51 REMARK 500 LEU C 96 108.93 -54.65 REMARK 500 ALA C 160 -61.88 -99.83 REMARK 500 TYR C 161 72.99 48.78 REMARK 500 LYS C 196 -7.72 73.79 REMARK 500 ASN G 31 57.48 -95.17 REMARK 500 VAL G 51 -65.70 68.09 REMARK 500 HIS G 95B -65.05 71.68 REMARK 500 ASN J 71 -169.74 -79.57 REMARK 500 ARG J 127 -95.12 58.81 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-49099 RELATED DB: EMDB REMARK 900 H5 HEMAGGLUTININ (A/JIANGSU/NJ210/2023) IN COMPLEX WITH CENTRAL REMARK 900 STEM-TARGETING FAB ST14 DBREF 9N7T A -5 332 PDB 9N7T 9N7T -5 332 DBREF 9N7T L 2 107 PDB 9N7T 9N7T 2 107 DBREF 9N7T H 1 113 PDB 9N7T 9N7T 1 113 DBREF 9N7T a 1 220 PDB 9N7T 9N7T 1 220 DBREF 9N7T B -5 332 PDB 9N7T 9N7T -5 332 DBREF 9N7T F 2 107 PDB 9N7T 9N7T 2 107 DBREF 9N7T D 1 113 PDB 9N7T 9N7T 1 113 DBREF 9N7T I 1 220 PDB 9N7T 9N7T 1 220 DBREF 9N7T C -5 332 PDB 9N7T 9N7T -5 332 DBREF 9N7T G 2 107 PDB 9N7T 9N7T 2 107 DBREF 9N7T E 1 113 PDB 9N7T 9N7T 1 113 DBREF 9N7T J 1 220 PDB 9N7T 9N7T 1 220 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 L 110 SER ALA LEU THR GLN PRO ALA SER VAL SER GLY SER PRO SEQRES 2 L 110 GLY GLN SER ILE THR ILE SER CYS THR GLY THR SER SER SEQRES 3 L 110 ASP VAL GLY GLY TYR ASN TYR VAL SER TRP TYR GLN GLN SEQRES 4 L 110 TYR PRO GLY LYS ALA PRO LYS VAL MET ILE TYR GLU VAL SEQRES 5 L 110 THR ASN ARG PRO SER GLY VAL SER ASN ARG PHE SER GLY SEQRES 6 L 110 SER LYS SER GLY ASN THR ALA SER LEU THR ILE SER GLY SEQRES 7 L 110 LEU GLN THR GLU ASP GLU ALA ASP TYR TYR CYS SER SER SEQRES 8 L 110 TYR THR GLY THR ILE THR HIS TYR VAL PHE GLY THR GLY SEQRES 9 L 110 THR LYS VAL THR VAL LEU SEQRES 1 H 124 GLN VAL GLN VAL VAL GLU SER GLY GLY GLY LEU VAL LYS SEQRES 2 H 124 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 H 124 PHE ILE PHE SER ASP TYR TYR MET SER TRP ILE ARG GLN SEQRES 4 H 124 ALA PRO GLY LYS GLY LEU ASP TRP VAL SER SER ILE THR SEQRES 5 H 124 SER THR GLY SER VAL ILE TYR TYR GLY ASP SER VAL ARG SEQRES 6 H 124 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN SER SEQRES 7 H 124 LEU TYR LEU GLN MET ASN THR LEU ARG ALA GLU ASP THR SEQRES 8 H 124 ALA VAL TYR TYR CYS ALA ARG GLY ASN THR ILE PHE GLY SEQRES 9 H 124 ILE VAL ARG GLY TRP TYR PHE ASP LEU TRP GLY ARG GLY SEQRES 10 H 124 THR LEU VAL THR VAL SER SER 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 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 F 110 SER ALA LEU THR GLN PRO ALA SER VAL SER GLY SER PRO SEQRES 2 F 110 GLY GLN SER ILE THR ILE SER CYS THR GLY THR SER SER SEQRES 3 F 110 ASP VAL GLY GLY TYR ASN TYR VAL SER TRP TYR GLN GLN SEQRES 4 F 110 TYR PRO GLY LYS ALA PRO LYS VAL MET ILE TYR GLU VAL SEQRES 5 F 110 THR ASN ARG PRO SER GLY VAL SER ASN ARG PHE SER GLY SEQRES 6 F 110 SER LYS SER GLY ASN THR ALA SER LEU THR ILE SER GLY SEQRES 7 F 110 LEU GLN THR GLU ASP GLU ALA ASP TYR TYR CYS SER SER SEQRES 8 F 110 TYR THR GLY THR ILE THR HIS TYR VAL PHE GLY THR GLY SEQRES 9 F 110 THR LYS VAL THR VAL LEU SEQRES 1 D 124 GLN VAL GLN VAL VAL GLU SER GLY GLY GLY LEU VAL LYS SEQRES 2 D 124 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 D 124 PHE ILE PHE SER ASP TYR TYR MET SER TRP ILE ARG GLN SEQRES 4 D 124 ALA PRO GLY LYS GLY LEU ASP TRP VAL SER SER ILE THR SEQRES 5 D 124 SER THR GLY SER VAL ILE TYR TYR GLY ASP SER VAL ARG SEQRES 6 D 124 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN SER SEQRES 7 D 124 LEU TYR LEU GLN MET ASN THR LEU ARG ALA GLU ASP THR SEQRES 8 D 124 ALA VAL TYR TYR CYS ALA ARG GLY ASN THR ILE PHE GLY SEQRES 9 D 124 ILE VAL ARG GLY TRP TYR PHE ASP LEU TRP GLY ARG GLY SEQRES 10 D 124 THR LEU VAL THR VAL SER SER SEQRES 1 I 220 GLY LEU PHE GLY ALA ILE ALA GLY PHE ILE GLU GLY GLY SEQRES 2 I 220 TRP GLN GLY MET VAL ASP GLY TRP TYR GLY TYR HIS HIS SEQRES 3 I 220 SER ASN GLU GLN GLY SER GLY TYR ALA ALA ASP LYS GLU SEQRES 4 I 220 SER THR GLN LYS ALA ILE ASP GLY VAL THR ASN LYS VAL SEQRES 5 I 220 ASN SER ILE ILE ASP LYS MET ASN THR GLN PHE GLU ALA SEQRES 6 I 220 VAL GLY ARG GLU PHE ASN ASN LEU GLU ARG ARG ILE GLU SEQRES 7 I 220 ASN LEU ASN LYS LYS MET GLU ASP GLY PHE LEU ASP VAL SEQRES 8 I 220 TRP THR TYR ASN ALA GLU LEU LEU VAL LEU MET GLU ASN SEQRES 9 I 220 GLU ARG THR LEU ASP PHE HIS ASP SER ASN VAL LYS ASN SEQRES 10 I 220 LEU TYR ASP LYS VAL ARG LEU GLN LEU ARG ASP ASN ALA SEQRES 11 I 220 LYS GLU LEU GLY ASN GLY CYS PHE GLU PHE TYR HIS LYS SEQRES 12 I 220 CYS ASP ASN GLU CYS MET GLU SER VAL ARG ASN GLY THR SEQRES 13 I 220 TYR TYR TYR PRO GLN TYR SER GLU GLU ALA ARG LEU LYS SEQRES 14 I 220 ARG GLU GLU ILE SER GLY VAL GLY TYR ILE PRO GLU ALA SEQRES 15 I 220 PRO ARG ASP GLY GLN ALA TYR VAL ARG LYS ASP GLY GLU SEQRES 16 I 220 TRP VAL LEU LEU SER THR PHE LEU GLY SER GLU ASN LEU SEQRES 17 I 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 G 110 SER ALA LEU THR GLN PRO ALA SER VAL SER GLY SER PRO SEQRES 2 G 110 GLY GLN SER ILE THR ILE SER CYS THR GLY THR SER SER SEQRES 3 G 110 ASP VAL GLY GLY TYR ASN TYR VAL SER TRP TYR GLN GLN SEQRES 4 G 110 TYR PRO GLY LYS ALA PRO LYS VAL MET ILE TYR GLU VAL SEQRES 5 G 110 THR ASN ARG PRO SER GLY VAL SER ASN ARG PHE SER GLY SEQRES 6 G 110 SER LYS SER GLY ASN THR ALA SER LEU THR ILE SER GLY SEQRES 7 G 110 LEU GLN THR GLU ASP GLU ALA ASP TYR TYR CYS SER SER SEQRES 8 G 110 TYR THR GLY THR ILE THR HIS TYR VAL PHE GLY THR GLY SEQRES 9 G 110 THR LYS VAL THR VAL LEU SEQRES 1 E 124 GLN VAL GLN VAL VAL GLU SER GLY GLY GLY LEU VAL LYS SEQRES 2 E 124 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 E 124 PHE ILE PHE SER ASP TYR TYR MET SER TRP ILE ARG GLN SEQRES 4 E 124 ALA PRO GLY LYS GLY LEU ASP TRP VAL SER SER ILE THR SEQRES 5 E 124 SER THR GLY SER VAL ILE TYR TYR GLY ASP SER VAL ARG SEQRES 6 E 124 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN SER SEQRES 7 E 124 LEU TYR LEU GLN MET ASN THR LEU ARG ALA GLU ASP THR SEQRES 8 E 124 ALA VAL TYR TYR CYS ALA ARG GLY ASN THR ILE PHE GLY SEQRES 9 E 124 ILE VAL ARG GLY TRP TYR PHE ASP LEU TRP GLY ARG GLY SEQRES 10 E 124 THR LEU VAL THR VAL SER SER SEQRES 1 J 220 GLY LEU PHE GLY ALA ILE ALA GLY PHE ILE GLU GLY GLY SEQRES 2 J 220 TRP GLN GLY MET VAL ASP GLY TRP TYR GLY TYR HIS HIS SEQRES 3 J 220 SER ASN GLU GLN GLY SER GLY TYR ALA ALA ASP LYS GLU SEQRES 4 J 220 SER THR GLN LYS ALA ILE ASP GLY VAL THR ASN LYS VAL SEQRES 5 J 220 ASN SER ILE ILE ASP LYS MET ASN THR GLN PHE GLU ALA SEQRES 6 J 220 VAL GLY ARG GLU PHE ASN ASN LEU GLU ARG ARG ILE GLU SEQRES 7 J 220 ASN LEU ASN LYS LYS MET GLU ASP GLY PHE LEU ASP VAL SEQRES 8 J 220 TRP THR TYR ASN ALA GLU LEU LEU VAL LEU MET GLU ASN SEQRES 9 J 220 GLU ARG THR LEU ASP PHE HIS ASP SER ASN VAL LYS ASN SEQRES 10 J 220 LEU TYR ASP LYS VAL ARG LEU GLN LEU ARG ASP ASN ALA SEQRES 11 J 220 LYS GLU LEU GLY ASN GLY CYS PHE GLU PHE TYR HIS LYS SEQRES 12 J 220 CYS ASP ASN GLU CYS MET GLU SER VAL ARG ASN GLY THR SEQRES 13 J 220 TYR TYR TYR PRO GLN TYR SER GLU GLU ALA ARG LEU LYS SEQRES 14 J 220 ARG GLU GLU ILE SER GLY VAL GLY TYR ILE PRO GLU ALA SEQRES 15 J 220 PRO ARG ASP GLY GLN ALA TYR VAL ARG LYS ASP GLY GLU SEQRES 16 J 220 TRP VAL LEU LEU SER THR PHE LEU GLY SER GLU ASN LEU SEQRES 17 J 220 TYR PHE GLN GLY GLY SER HIS HIS HIS HIS HIS HIS HET NAG K 1 14 HET NAG K 2 14 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 P 1 14 HET NAG P 2 14 HET NAG Q 1 14 HET NAG Q 2 14 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 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 21(C8 H15 N O6) HELIX 1 AA1 SER A 65 GLY A 72 1 8 HELIX 2 AA2 ASN A 73 ILE A 80 5 8 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 GLN L 79 GLU L 83 5 5 HELIX 7 AA7 ILE H 28 TYR H 32 5 5 HELIX 8 AA8 ARG H 83 THR H 87 5 5 HELIX 9 AA9 ASP a 37 LYS a 58 1 22 HELIX 10 AB1 GLU a 74 ARG a 127 1 54 HELIX 11 AB2 ASP a 145 GLY a 155 1 11 HELIX 12 AB3 TYR a 158 ARG a 170 1 13 HELIX 13 AB4 SER B 65 GLY B 72 1 8 HELIX 14 AB5 ASN B 73 ILE B 80 5 8 HELIX 15 AB6 ASP B 104 SER B 113 1 10 HELIX 16 AB7 PRO B 125 TRP B 127 5 5 HELIX 17 AB8 ASN B 187 TYR B 195 1 9 HELIX 18 AB9 GLN F 79 GLU F 83 5 5 HELIX 19 AC1 ILE D 28 TYR D 32 5 5 HELIX 20 AC2 ARG D 83 THR D 87 5 5 HELIX 21 AC3 ASP I 37 LYS I 58 1 22 HELIX 22 AC4 GLU I 74 ARG I 127 1 54 HELIX 23 AC5 ASP I 145 GLY I 155 1 11 HELIX 24 AC6 TYR I 158 ARG I 170 1 13 HELIX 25 AC7 SER C 65 GLY C 72 1 8 HELIX 26 AC8 ASN C 73 ILE C 80 5 8 HELIX 27 AC9 ASP C 104 SER C 113 1 10 HELIX 28 AD1 PRO C 125 TRP C 127 5 5 HELIX 29 AD2 ASN C 187 TYR C 195 1 9 HELIX 30 AD3 GLN G 79 GLU G 83 5 5 HELIX 31 AD4 ILE E 28 TYR E 32 5 5 HELIX 32 AD5 ARG E 83 THR E 87 5 5 HELIX 33 AD6 ASP J 37 LYS J 58 1 22 HELIX 34 AD7 GLU J 74 ARG J 127 1 54 HELIX 35 AD8 ASP J 145 GLY J 155 1 11 HELIX 36 AD9 TYR J 158 ARG J 170 1 13 SHEET 1 AA1 3 GLN A 12 CYS A 14 0 SHEET 2 AA1 3 CYS a 137 PHE a 140 -1 O PHE a 138 N ILE A 13 SHEET 3 AA1 3 ALA a 130 GLU a 132 -1 N LYS a 131 O GLU a 139 SHEET 1 AA2 3 GLY A 16 TYR A 17 0 SHEET 2 AA2 3 TYR a 22 ASN a 28 -1 O GLY a 23 N GLY A 16 SHEET 3 AA2 3 GLY a 31 ALA a 36 -1 O ALA a 35 N TYR a 24 SHEET 1 AA3 2 GLN A 25 VAL A 26 0 SHEET 2 AA3 2 VAL A 34 THR A 35 -1 O VAL A 34 N VAL A 26 SHEET 1 AA4 2 ALA A 39 ASP A 41 0 SHEET 2 AA4 2 VAL A 315 ALA A 317 -1 O LEU A 316 N GLN A 40 SHEET 1 AA5 3 LEU A 43 GLU A 44 0 SHEET 2 AA5 3 PHE A 294 HIS A 295 1 O PHE A 294 N GLU A 44 SHEET 3 AA5 3 LYS A 307 TYR A 308 1 O LYS A 307 N HIS A 295 SHEET 1 AA6 2 LEU A 51 LEU A 54 0 SHEET 2 AA6 2 TYR A 274 THR A 279 1 O CYS A 277 N ASP A 53 SHEET 1 AA7 3 LEU A 59 ILE A 60 0 SHEET 2 AA7 3 ILE A 87 GLU A 89 1 O VAL A 88 N LEU A 59 SHEET 3 AA7 3 ILE A 267 LYS A 269 1 O MET A 268 N ILE A 87 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 HIS A 184 O ARG A 229 SHEET 4 AA8 5 TYR A 256 ILE A 260 -1 O TYR A 258 N LEU A 177 SHEET 5 AA8 5 PHE A 118 LEU A 122 -1 N ILE A 121 O ALA A 257 SHEET 1 AA9 5 GLY A 100 LEU A 102 0 SHEET 2 AA9 5 ARG A 229 LEU A 237 1 O PHE A 232 N SER A 101 SHEET 3 AA9 5 LEU A 176 HIS A 184 -1 N HIS A 184 O ARG A 229 SHEET 4 AA9 5 PHE A 251 PRO A 254 -1 O ILE A 252 N GLY A 181 SHEET 5 AA9 5 VAL A 151 TRP A 153 -1 N VAL A 152 O ALA A 253 SHEET 1 AB1 2 HIS A 130 GLU A 131 0 SHEET 2 AB1 2 ILE A 155 LYS A 156 -1 O ILE A 155 N GLU A 131 SHEET 1 AB2 2 SER A 136 TYR A 141 0 SHEET 2 AB2 2 ALA A 144 SER A 146 -1 O ALA A 144 N TYR A 141 SHEET 1 AB3 4 ILE A 164 ASN A 169 0 SHEET 2 AB3 4 ALA A 242 SER A 247 -1 O PHE A 245 N ILE A 166 SHEET 3 AB3 4 ILE A 202 GLY A 205 -1 N SER A 203 O GLU A 246 SHEET 4 AB3 4 ASN A 210 LEU A 213 -1 O GLN A 211 N VAL A 204 SHEET 1 AB4 3 ALA A 287 ILE A 288 0 SHEET 2 AB4 3 CYS A 281 GLN A 282 -1 N CYS A 281 O ILE A 288 SHEET 3 AB4 3 ILE A 302 GLY A 303 -1 O ILE A 302 N GLN A 282 SHEET 1 AB5 3 ILE L 19 THR L 24 0 SHEET 2 AB5 3 THR L 70 ILE L 75 -1 O ILE L 75 N ILE L 19 SHEET 3 AB5 3 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74 SHEET 1 AB6 4 LYS L 45 ILE L 48 0 SHEET 2 AB6 4 SER L 34 GLN L 38 -1 N GLN L 37 O LYS L 45 SHEET 3 AB6 4 ASP L 85 THR L 92 -1 O TYR L 87 N TYR L 36 SHEET 4 AB6 4 HIS L 95B PHE L 98 -1 O VAL L 97 N SER L 90 SHEET 1 AB7 4 GLN H 3 SER H 7 0 SHEET 2 AB7 4 LEU H 18 SER H 25 -1 O SER H 21 N SER H 7 SHEET 3 AB7 4 SER H 77 MET H 82 -1 O LEU H 80 N LEU H 20 SHEET 4 AB7 4 PHE H 67 ASP H 72 -1 N THR H 68 O GLN H 81 SHEET 1 AB8 6 LEU H 11 VAL H 12 0 SHEET 2 AB8 6 THR H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AB8 6 ALA H 88 ILE H 98 -1 N TYR H 90 O THR H 107 SHEET 4 AB8 6 MET H 34 GLN H 39 -1 N ILE H 37 O TYR H 91 SHEET 5 AB8 6 LEU H 45 ILE H 51 -1 O ASP H 46 N ARG H 38 SHEET 6 AB8 6 ILE H 57 TYR H 59 -1 O TYR H 58 N SER H 50 SHEET 1 AB9 4 LEU H 11 VAL H 12 0 SHEET 2 AB9 4 THR H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AB9 4 ALA H 88 ILE H 98 -1 N TYR H 90 O THR H 107 SHEET 4 AB9 4 ILE H 100A TRP H 103 -1 O TYR H 100F N ASN H 96 SHEET 1 AC1 3 GLN B 12 CYS B 14 0 SHEET 2 AC1 3 CYS I 137 PHE I 140 -1 O PHE I 138 N ILE B 13 SHEET 3 AC1 3 ALA I 130 GLU I 132 -1 N LYS I 131 O GLU I 139 SHEET 1 AC2 3 GLY B 16 TYR B 17 0 SHEET 2 AC2 3 TYR I 22 ASN I 28 -1 O GLY I 23 N GLY B 16 SHEET 3 AC2 3 GLY I 31 ALA I 36 -1 O ALA I 35 N TYR I 24 SHEET 1 AC3 2 GLN B 25 VAL B 26 0 SHEET 2 AC3 2 VAL B 34 THR B 35 -1 O VAL B 34 N VAL B 26 SHEET 1 AC4 2 ALA B 39 ASP B 41 0 SHEET 2 AC4 2 VAL B 315 ALA B 317 -1 O LEU B 316 N GLN B 40 SHEET 1 AC5 3 LEU B 43 GLU B 44 0 SHEET 2 AC5 3 PHE B 294 HIS B 295 1 O PHE B 294 N GLU B 44 SHEET 3 AC5 3 LYS B 307 TYR B 308 1 O LYS B 307 N HIS B 295 SHEET 1 AC6 2 LEU B 51 LEU B 54 0 SHEET 2 AC6 2 TYR B 274 THR B 279 1 O CYS B 277 N ASP B 53 SHEET 1 AC7 3 LEU B 59 ILE B 60 0 SHEET 2 AC7 3 ILE B 87 GLU B 89 1 O VAL B 88 N LEU B 59 SHEET 3 AC7 3 ILE B 267 LYS B 269 1 O MET B 268 N ILE B 87 SHEET 1 AC8 5 GLY B 100 LEU B 102 0 SHEET 2 AC8 5 ARG B 229 LEU B 237 1 O PHE B 232 N SER B 101 SHEET 3 AC8 5 LEU B 176 HIS B 184 -1 N HIS B 184 O ARG B 229 SHEET 4 AC8 5 TYR B 256 ILE B 260 -1 O TYR B 258 N LEU B 177 SHEET 5 AC8 5 PHE B 118 LEU B 122 -1 N ILE B 121 O ALA B 257 SHEET 1 AC9 5 GLY B 100 LEU B 102 0 SHEET 2 AC9 5 ARG B 229 LEU B 237 1 O PHE B 232 N SER B 101 SHEET 3 AC9 5 LEU B 176 HIS B 184 -1 N HIS B 184 O ARG B 229 SHEET 4 AC9 5 PHE B 251 PRO B 254 -1 O ILE B 252 N GLY B 181 SHEET 5 AC9 5 VAL B 151 TRP B 153 -1 N VAL B 152 O ALA B 253 SHEET 1 AD1 2 HIS B 130 GLU B 131 0 SHEET 2 AD1 2 ILE B 155 LYS B 156 -1 O ILE B 155 N GLU B 131 SHEET 1 AD2 2 SER B 136 TYR B 141 0 SHEET 2 AD2 2 ALA B 144 SER B 146 -1 O ALA B 144 N TYR B 141 SHEET 1 AD3 4 ILE B 164 ASN B 169 0 SHEET 2 AD3 4 ALA B 242 SER B 247 -1 O PHE B 245 N ILE B 166 SHEET 3 AD3 4 ILE B 202 GLY B 205 -1 N SER B 203 O GLU B 246 SHEET 4 AD3 4 ASN B 210 LEU B 213 -1 O GLN B 211 N VAL B 204 SHEET 1 AD4 3 ALA B 287 ILE B 288 0 SHEET 2 AD4 3 CYS B 281 GLN B 282 -1 N CYS B 281 O ILE B 288 SHEET 3 AD4 3 ILE B 302 GLY B 303 -1 O ILE B 302 N GLN B 282 SHEET 1 AD5 3 ILE F 19 THR F 24 0 SHEET 2 AD5 3 THR F 70 ILE F 75 -1 O ILE F 75 N ILE F 19 SHEET 3 AD5 3 PHE F 62 SER F 67 -1 N SER F 63 O THR F 74 SHEET 1 AD6 4 LYS F 45 ILE F 48 0 SHEET 2 AD6 4 SER F 34 GLN F 38 -1 N GLN F 37 O LYS F 45 SHEET 3 AD6 4 ASP F 85 THR F 92 -1 O TYR F 87 N TYR F 36 SHEET 4 AD6 4 HIS F 95B PHE F 98 -1 O VAL F 97 N SER F 90 SHEET 1 AD7 4 GLN D 3 SER D 7 0 SHEET 2 AD7 4 LEU D 18 SER D 25 -1 O SER D 21 N SER D 7 SHEET 3 AD7 4 SER D 77 MET D 82 -1 O LEU D 80 N LEU D 20 SHEET 4 AD7 4 PHE D 67 ASP D 72 -1 N THR D 68 O GLN D 81 SHEET 1 AD8 6 LEU D 11 VAL D 12 0 SHEET 2 AD8 6 THR D 107 VAL D 111 1 O THR D 110 N VAL D 12 SHEET 3 AD8 6 ALA D 88 ILE D 98 -1 N TYR D 90 O THR D 107 SHEET 4 AD8 6 MET D 34 GLN D 39 -1 N ILE D 37 O TYR D 91 SHEET 5 AD8 6 LEU D 45 ILE D 51 -1 O ASP D 46 N ARG D 38 SHEET 6 AD8 6 ILE D 57 TYR D 59 -1 O TYR D 58 N SER D 50 SHEET 1 AD9 4 LEU D 11 VAL D 12 0 SHEET 2 AD9 4 THR D 107 VAL D 111 1 O THR D 110 N VAL D 12 SHEET 3 AD9 4 ALA D 88 ILE D 98 -1 N TYR D 90 O THR D 107 SHEET 4 AD9 4 ILE D 100A TRP D 103 -1 O TYR D 100F N ASN D 96 SHEET 1 AE1 5 GLY J 31 ALA J 36 0 SHEET 2 AE1 5 TYR J 22 ASN J 28 -1 N TYR J 24 O ALA J 35 SHEET 3 AE1 5 GLN C 12 TYR C 17 -1 N GLN C 12 O SER J 27 SHEET 4 AE1 5 CYS J 137 PHE J 140 -1 O PHE J 138 N ILE C 13 SHEET 5 AE1 5 ALA J 130 GLU J 132 -1 N LYS J 131 O GLU J 139 SHEET 1 AE2 2 GLN C 25 VAL C 26 0 SHEET 2 AE2 2 VAL C 34 THR C 35 -1 O VAL C 34 N VAL C 26 SHEET 1 AE3 2 ALA C 39 ASP C 41 0 SHEET 2 AE3 2 VAL C 315 ALA C 317 -1 O LEU C 316 N GLN C 40 SHEET 1 AE4 3 LEU C 43 GLU C 44 0 SHEET 2 AE4 3 PHE C 294 HIS C 295 1 O PHE C 294 N GLU C 44 SHEET 3 AE4 3 LYS C 307 TYR C 308 1 O LYS C 307 N HIS C 295 SHEET 1 AE5 2 LEU C 51 LEU C 54 0 SHEET 2 AE5 2 TYR C 274 THR C 279 1 O CYS C 277 N ASP C 53 SHEET 1 AE6 3 LEU C 59 ILE C 60 0 SHEET 2 AE6 3 ILE C 87 GLU C 89 1 O VAL C 88 N LEU C 59 SHEET 3 AE6 3 ILE C 267 LYS C 269 1 O MET C 268 N ILE C 87 SHEET 1 AE7 5 GLY C 100 LEU C 102 0 SHEET 2 AE7 5 ARG C 229 LEU C 237 1 O PHE C 232 N SER C 101 SHEET 3 AE7 5 LEU C 176 HIS C 184 -1 N HIS C 184 O ARG C 229 SHEET 4 AE7 5 TYR C 256 ILE C 260 -1 O TYR C 258 N LEU C 177 SHEET 5 AE7 5 PHE C 118 LEU C 122 -1 N ILE C 121 O ALA C 257 SHEET 1 AE8 5 GLY C 100 LEU C 102 0 SHEET 2 AE8 5 ARG C 229 LEU C 237 1 O PHE C 232 N SER C 101 SHEET 3 AE8 5 LEU C 176 HIS C 184 -1 N HIS C 184 O ARG C 229 SHEET 4 AE8 5 PHE C 251 PRO C 254 -1 O ILE C 252 N GLY C 181 SHEET 5 AE8 5 VAL C 151 TRP C 153 -1 N VAL C 152 O ALA C 253 SHEET 1 AE9 2 HIS C 130 GLU C 131 0 SHEET 2 AE9 2 ILE C 155 LYS C 156 -1 O ILE C 155 N GLU C 131 SHEET 1 AF1 2 SER C 136 TYR C 141 0 SHEET 2 AF1 2 ALA C 144 SER C 146 -1 O ALA C 144 N TYR C 141 SHEET 1 AF2 4 ILE C 164 ASN C 169 0 SHEET 2 AF2 4 ALA C 242 SER C 247 -1 O PHE C 245 N ILE C 166 SHEET 3 AF2 4 ILE C 202 GLY C 205 -1 N SER C 203 O GLU C 246 SHEET 4 AF2 4 ASN C 210 LEU C 213 -1 O GLN C 211 N VAL C 204 SHEET 1 AF3 3 ALA C 287 ILE C 288 0 SHEET 2 AF3 3 CYS C 281 GLN C 282 -1 N CYS C 281 O ILE C 288 SHEET 3 AF3 3 ILE C 302 GLY C 303 -1 O ILE C 302 N GLN C 282 SHEET 1 AF4 3 ILE G 19 THR G 24 0 SHEET 2 AF4 3 THR G 70 ILE G 75 -1 O ILE G 75 N ILE G 19 SHEET 3 AF4 3 PHE G 62 SER G 67 -1 N SER G 63 O THR G 74 SHEET 1 AF5 4 LYS G 45 ILE G 48 0 SHEET 2 AF5 4 SER G 34 GLN G 38 -1 N GLN G 37 O LYS G 45 SHEET 3 AF5 4 ASP G 85 THR G 92 -1 O TYR G 87 N TYR G 36 SHEET 4 AF5 4 HIS G 95B PHE G 98 -1 O VAL G 97 N SER G 90 SHEET 1 AF6 4 GLN E 3 SER E 7 0 SHEET 2 AF6 4 LEU E 18 SER E 25 -1 O SER E 21 N SER E 7 SHEET 3 AF6 4 SER E 77 MET E 82 -1 O LEU E 80 N LEU E 20 SHEET 4 AF6 4 PHE E 67 ASP E 72 -1 N THR E 68 O GLN E 81 SHEET 1 AF7 6 LEU E 11 VAL E 12 0 SHEET 2 AF7 6 THR E 107 VAL E 111 1 O THR E 110 N VAL E 12 SHEET 3 AF7 6 ALA E 88 ILE E 98 -1 N TYR E 90 O THR E 107 SHEET 4 AF7 6 MET E 34 GLN E 39 -1 N ILE E 37 O TYR E 91 SHEET 5 AF7 6 LEU E 45 ILE E 51 -1 O ASP E 46 N ARG E 38 SHEET 6 AF7 6 ILE E 57 TYR E 59 -1 O TYR E 58 N SER E 50 SHEET 1 AF8 4 LEU E 11 VAL E 12 0 SHEET 2 AF8 4 THR E 107 VAL E 111 1 O THR E 110 N VAL E 12 SHEET 3 AF8 4 ALA E 88 ILE E 98 -1 N TYR E 90 O THR E 107 SHEET 4 AF8 4 ILE E 100A TRP E 103 -1 O TYR E 100F N ASN E 96 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 L 23 CYS L 88 1555 1555 2.03 SSBOND 6 CYS H 22 CYS H 92 1555 1555 2.03 SSBOND 7 CYS a 144 CYS a 148 1555 1555 2.03 SSBOND 8 CYS B 52 CYS B 277 1555 1555 2.03 SSBOND 9 CYS B 64 CYS B 76 1555 1555 2.03 SSBOND 10 CYS B 97 CYS B 139 1555 1555 2.03 SSBOND 11 CYS B 281 CYS B 305 1555 1555 2.03 SSBOND 12 CYS F 23 CYS F 88 1555 1555 2.03 SSBOND 13 CYS D 22 CYS D 92 1555 1555 2.03 SSBOND 14 CYS I 144 CYS I 148 1555 1555 2.03 SSBOND 15 CYS C 52 CYS C 277 1555 1555 2.03 SSBOND 16 CYS C 64 CYS C 76 1555 1555 2.03 SSBOND 17 CYS C 97 CYS C 139 1555 1555 2.03 SSBOND 18 CYS C 281 CYS C 305 1555 1555 2.03 SSBOND 19 CYS G 23 CYS G 88 1555 1555 2.03 SSBOND 20 CYS E 22 CYS E 92 1555 1555 2.03 SSBOND 21 CYS J 144 CYS J 148 1555 1555 2.03 LINK ND2 ASN A 21 C1 NAG A 403 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 K 1 1555 1555 1.44 LINK ND2 ASN a 154 C1 NAG M 1 1555 1555 1.44 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 N 1 1555 1555 1.44 LINK ND2 ASN I 154 C1 NAG O 1 1555 1555 1.44 LINK ND2 ASN C 21 C1 NAG C 403 1555 1555 1.44 LINK ND2 ASN C 33 C1 NAG C 402 1555 1555 1.45 LINK ND2 ASN C 169 C1 NAG C 401 1555 1555 1.44 LINK ND2 ASN C 289 C1 NAG P 1 1555 1555 1.44 LINK ND2 ASN J 154 C1 NAG Q 1 1555 1555 1.44 LINK O4 NAG K 1 C1 NAG K 2 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 LINK O4 NAG P 1 C1 NAG P 2 1555 1555 1.44 LINK O4 NAG Q 1 C1 NAG Q 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