HEADER VIRAL PROTEIN/IMMUNE SYSTEM 06-FEB-25 9N7V TITLE H1 HEMAGGLUTININ (A/MICHIGAN/45/2015) IN COMPLEX WITH ANCHOR-TARGETING TITLE 2 FAB ST4 COMPND MOL_ID: 1; COMPND 2 MOLECULE: ST4 HEAVY CHAIN FAB; COMPND 3 CHAIN: H; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: ST4 LIGHT CHAIN FAB; COMPND 7 CHAIN: L; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: H1 HA1; COMPND 11 CHAIN: A, C, B; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 4; COMPND 14 MOLECULE: H1 HA2; COMPND 15 CHAIN: a, c, b; COMPND 16 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 EXPRESSION_SYSTEM_CELL_LINE: HEK293; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 9 ORGANISM_TAXID: 9606; SOURCE 10 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 11 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 12 EXPRESSION_SYSTEM_CELL_LINE: HEK293; SOURCE 13 MOL_ID: 3; SOURCE 14 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS; SOURCE 15 ORGANISM_TAXID: 11320; SOURCE 16 STRAIN: A/MICHIGAN/45/2015; 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/MICHIGAN/45/2015; SOURCE 24 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 25 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 26 EXPRESSION_SYSTEM_CELL_LINE: HEK293 KEYWDS INFLUENZA, HEMAGGLUTININ, H1, 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 9N7V 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. 3.15 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) : 3.150 REMARK 3 NUMBER OF PARTICLES : 55333 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 9N7V 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_1000292634. 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 : H1 HEMAGGLUTININ REMARK 245 (A/MICHIGAN/45/2015) IN COMPLEX REMARK 245 WITH ANCHOR-TARGETING FAB ST4 REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 0.90 REMARK 245 SAMPLE SUPPORT DETAILS : 15 MA 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) : 4326.00 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, A, a, C, c, B, b, 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 GLN H 1 REMARK 465 GLY H 10 REMARK 465 VAL H 11 REMARK 465 VAL H 12 REMARK 465 ARG H 13 REMARK 465 PRO H 14 REMARK 465 GLY H 15 REMARK 465 LYS H 16 REMARK 465 ARG H 71 REMARK 465 ASP H 72 REMARK 465 ASN H 73 REMARK 465 SER H 74 REMARK 465 LYS H 75 REMARK 465 THR H 76 REMARK 465 THR H 77 REMARK 465 LEU H 78 REMARK 465 SER H 112 REMARK 465 SER H 113 REMARK 465 SER L 26A REMARK 465 SER L 26B REMARK 465 ASP L 26C REMARK 465 VAL L 26D REMARK 465 GLY L 26E REMARK 465 THR L 26F REMARK 465 MET A -6 REMARK 465 LYS A -5 REMARK 465 ALA A -4 REMARK 465 ILE A -3 REMARK 465 LEU A -2 REMARK 465 VAL A -1 REMARK 465 VAL A 0 REMARK 465 LEU A 1 REMARK 465 LEU A 2 REMARK 465 TYR A 3 REMARK 465 THR A 4 REMARK 465 PHE A 5 REMARK 465 THR A 6 REMARK 465 THR A 7 REMARK 465 ALA A 8 REMARK 465 ASN A 9 REMARK 465 ALA A 10 REMARK 465 HIS A 148 REMARK 465 ALA A 149 REMARK 465 GLY A 150 REMARK 465 ILE A 334 REMARK 465 GLN A 335 REMARK 465 SER A 336 REMARK 465 ARG A 337 REMARK 465 GLY a 1 REMARK 465 LEU a 2 REMARK 465 PHE a 3 REMARK 465 GLY a 4 REMARK 465 ALA a 5 REMARK 465 ILE a 6 REMARK 465 ALA a 7 REMARK 465 GLY a 8 REMARK 465 PHE a 9 REMARK 465 ASP 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 -6 REMARK 465 LYS C -5 REMARK 465 ALA C -4 REMARK 465 ILE C -3 REMARK 465 LEU C -2 REMARK 465 VAL C -1 REMARK 465 VAL C 0 REMARK 465 LEU C 1 REMARK 465 LEU C 2 REMARK 465 TYR C 3 REMARK 465 THR C 4 REMARK 465 PHE C 5 REMARK 465 THR C 6 REMARK 465 THR C 7 REMARK 465 ALA C 8 REMARK 465 ASN C 9 REMARK 465 ALA C 10 REMARK 465 HIS C 148 REMARK 465 ALA C 149 REMARK 465 GLY C 150 REMARK 465 GLN C 335 REMARK 465 SER C 336 REMARK 465 ARG C 337 REMARK 465 GLY c 1 REMARK 465 LEU c 2 REMARK 465 PHE c 3 REMARK 465 GLY c 4 REMARK 465 ALA c 5 REMARK 465 ILE c 6 REMARK 465 ALA c 7 REMARK 465 GLY c 8 REMARK 465 PHE c 9 REMARK 465 ASP 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 465 MET B -6 REMARK 465 LYS B -5 REMARK 465 ALA B -4 REMARK 465 ILE B -3 REMARK 465 LEU B -2 REMARK 465 VAL B -1 REMARK 465 VAL B 0 REMARK 465 LEU B 1 REMARK 465 LEU B 2 REMARK 465 TYR B 3 REMARK 465 THR B 4 REMARK 465 PHE B 5 REMARK 465 THR B 6 REMARK 465 THR B 7 REMARK 465 ALA B 8 REMARK 465 ASN B 9 REMARK 465 ALA B 10 REMARK 465 ARG B 337 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 ASP 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 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 GLY A 63 OG1 THR A 92 2.12 REMARK 500 O SER L 2 OG1 THR L 26 2.12 REMARK 500 O THR A 92 OG SER A 95 2.13 REMARK 500 OG SER C 85 O SER C 119 2.13 REMARK 500 OG1 THR B 287 O ILE B 296 2.15 REMARK 500 O LEU b 89 OG1 THR b 93 2.17 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 LYS H 64 -8.87 77.07 REMARK 500 SER L 32 36.25 -98.69 REMARK 500 ASP L 50 -120.55 52.60 REMARK 500 PHE L 98 -65.31 -96.52 REMARK 500 THR A 23 30.93 -96.10 REMARK 500 LYS A 64 51.94 -90.55 REMARK 500 SER A 167 138.73 -173.61 REMARK 500 ASN A 257 65.40 60.91 REMARK 500 ASN A 304 28.50 -140.40 REMARK 500 LYS a 127 -128.42 51.84 REMARK 500 ALA a 130 79.34 -117.52 REMARK 500 SER C 131 -5.11 77.14 REMARK 500 LEU C 201 -60.68 -90.33 REMARK 500 GLN C 203 -2.01 71.47 REMARK 500 LYS c 127 -123.67 59.25 REMARK 500 SER B 131 -7.58 77.15 REMARK 500 ALA B 225 141.34 -171.78 REMARK 500 LYS b 127 -139.90 57.58 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-49100 RELATED DB: EMDB REMARK 900 H1 HEMAGGLUTININ (A/MICHIGAN/45/2015) IN COMPLEX WITH ANCHOR- REMARK 900 TARGETING FAB ST4 DBREF 9N7V H 1 113 PDB 9N7V 9N7V 1 113 DBREF 9N7V L 1 107 PDB 9N7V 9N7V 1 107 DBREF 9N7V A -6 337 PDB 9N7V 9N7V -6 337 DBREF 9N7V a 1 220 PDB 9N7V 9N7V 1 220 DBREF 9N7V C -6 337 PDB 9N7V 9N7V -6 337 DBREF 9N7V c 1 220 PDB 9N7V 9N7V 1 220 DBREF 9N7V B -6 337 PDB 9N7V 9N7V -6 337 DBREF 9N7V b 1 220 PDB 9N7V 9N7V 1 220 SEQRES 1 H 123 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY VAL VAL ARG SEQRES 2 H 123 PRO GLY LYS SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 H 123 PHE THR LEU SER ASN HIS ALA LEU HIS TRP VAL ARG GLN SEQRES 4 H 123 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA ALA ILE SER SEQRES 5 H 123 TYR ASP GLY SER ILE LYS TYR TYR ALA ASP SER VAL LYS SEQRES 6 H 123 ASP ARG PHE THR ILE SER ARG ASP ASN SER LYS THR THR SEQRES 7 H 123 LEU TYR MET GLN MET ASP SER LEU ARG PRO GLU ASP THR SEQRES 8 H 123 ALA VAL TYR TYR CYS ALA ARG GLY GLY TRP LEU ARG PHE SEQRES 9 H 123 VAL PHE LEU TRP HIS PHE ASP LEU TRP GLY ARG GLY THR SEQRES 10 H 123 LEU VAL THR VAL SER SER SEQRES 1 L 109 GLN SER ALA LEU THR GLN PRO ALA SER VAL SER GLY SER SEQRES 2 L 109 PRO GLY GLN SER ILE THR ILE SER CYS THR ALA THR SER SEQRES 3 L 109 SER ASP VAL GLY THR TYR ASN SER VAL SER TRP TYR GLN SEQRES 4 L 109 HIS TYR PRO GLY LYS ALA PRO LYS LEU ILE LEU PHE ASP SEQRES 5 L 109 VAL ASN ASN ARG PRO SER GLY VAL SER ASN ARG PHE SER SEQRES 6 L 109 GLY SER LYS SER GLY LYS THR ALA SER LEU THR ILE SER SEQRES 7 L 109 GLY LEU GLN ALA GLU ASP GLU ALA ASP TYR TYR CYS SER SEQRES 8 L 109 SER ASN THR GLY ARG SER THR MET PHE GLY GLY GLY THR SEQRES 9 L 109 LYS LEU THR VAL LEU SEQRES 1 A 344 MET LYS ALA ILE LEU VAL VAL LEU LEU TYR THR PHE THR SEQRES 2 A 344 THR ALA ASN ALA ASP THR LEU CYS ILE GLY TYR HIS ALA SEQRES 3 A 344 ASN ASN SER THR ASP THR VAL ASP THR VAL LEU GLU LYS SEQRES 4 A 344 ASN VAL THR VAL THR HIS SER VAL ASN LEU LEU GLU ASP SEQRES 5 A 344 LYS HIS ASN GLY LYS LEU CYS LYS LEU ARG GLY VAL ALA SEQRES 6 A 344 PRO LEU HIS LEU GLY LYS CYS ASN ILE ALA GLY TRP ILE SEQRES 7 A 344 LEU GLY ASN PRO GLU CYS GLU SER LEU SER THR ALA SER SEQRES 8 A 344 SER TRP SER TYR ILE VAL GLU THR SER ASN SER ASP ASN SEQRES 9 A 344 GLY THR CYS TYR PRO GLY ASP PHE ILE ASN TYR GLU GLU SEQRES 10 A 344 LEU ARG GLU GLN LEU SER SER VAL SER SER PHE GLU ARG SEQRES 11 A 344 PHE GLU ILE PHE PRO LYS THR SER SER TRP PRO ASN HIS SEQRES 12 A 344 ASP SER ASN LYS GLY VAL THR ALA ALA CYS PRO HIS ALA SEQRES 13 A 344 GLY ALA LYS SER PHE TYR LYS ASN LEU ILE TRP LEU VAL SEQRES 14 A 344 LYS LYS GLY ASN SER TYR PRO LYS LEU ASN GLN SER TYR SEQRES 15 A 344 ILE ASN ASP LYS GLY LYS GLU VAL LEU VAL LEU TRP GLY SEQRES 16 A 344 ILE HIS HIS PRO SER THR THR ALA ASP GLN GLN SER LEU SEQRES 17 A 344 TYR GLN ASN ALA ASP ALA TYR VAL PHE VAL GLY THR SER SEQRES 18 A 344 ARG TYR SER LYS LYS PHE LYS PRO GLU ILE ALA THR ARG SEQRES 19 A 344 PRO LYS VAL ARG ASP GLN GLU GLY ARG MET ASN TYR TYR SEQRES 20 A 344 TRP THR LEU VAL GLU PRO GLY ASP LYS ILE THR PHE GLU SEQRES 21 A 344 ALA THR GLY ASN LEU VAL VAL PRO ARG TYR ALA PHE THR SEQRES 22 A 344 MET GLU ARG ASN ALA GLY SER GLY ILE ILE ILE SER ASP SEQRES 23 A 344 THR PRO VAL HIS ASP CYS ASN THR THR CYS GLN THR PRO SEQRES 24 A 344 GLU GLY ALA ILE ASN THR SER LEU PRO PHE GLN ASN ILE SEQRES 25 A 344 HIS PRO ILE THR ILE GLY LYS CYS PRO LYS TYR VAL LYS SEQRES 26 A 344 SER THR LYS LEU ARG LEU ALA THR GLY LEU ARG ASN VAL SEQRES 27 A 344 PRO SER ILE GLN SER ARG SEQRES 1 a 220 GLY LEU PHE GLY ALA ILE ALA GLY PHE ILE GLU GLY GLY SEQRES 2 a 220 TRP THR GLY MET VAL ASP GLY TRP TYR GLY TYR HIS HIS SEQRES 3 a 220 GLN ASN GLU GLN GLY SER GLY TYR ALA ALA ASP LEU LYS SEQRES 4 a 220 SER THR GLN ASN ALA ILE ASP LYS ILE THR ASN LYS VAL SEQRES 5 a 220 ASN SER VAL ILE GLU LYS MET ASN THR GLN PHE THR ALA SEQRES 6 a 220 VAL GLY LYS GLU PHE ASN HIS LEU GLU LYS ARG ILE GLU SEQRES 7 a 220 ASN LEU ASN LYS LYS VAL ASP ASP GLY PHE LEU ASP ILE SEQRES 8 a 220 TRP THR TYR ASN ALA GLU LEU LEU VAL LEU LEU GLU ASN SEQRES 9 a 220 GLU ARG THR LEU ASP TYR HIS ASP SER ASN VAL LYS ASN SEQRES 10 a 220 LEU TYR GLU LYS VAL ARG ASN GLN LEU LYS ASN ASN ALA SEQRES 11 a 220 LYS GLU ILE GLY ASN GLY CYS PHE GLU PHE TYR HIS LYS SEQRES 12 a 220 CYS ASP ASN THR CYS MET GLU SER VAL LYS ASN GLY THR SEQRES 13 a 220 TYR ASP TYR PRO LYS TYR SER GLU GLU ALA LYS LEU ASN SEQRES 14 a 220 ARG GLU LYS ILE ASP 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 344 MET LYS ALA ILE LEU VAL VAL LEU LEU TYR THR PHE THR SEQRES 2 C 344 THR ALA ASN ALA ASP THR LEU CYS ILE GLY TYR HIS ALA SEQRES 3 C 344 ASN ASN SER THR ASP THR VAL ASP THR VAL LEU GLU LYS SEQRES 4 C 344 ASN VAL THR VAL THR HIS SER VAL ASN LEU LEU GLU ASP SEQRES 5 C 344 LYS HIS ASN GLY LYS LEU CYS LYS LEU ARG GLY VAL ALA SEQRES 6 C 344 PRO LEU HIS LEU GLY LYS CYS ASN ILE ALA GLY TRP ILE SEQRES 7 C 344 LEU GLY ASN PRO GLU CYS GLU SER LEU SER THR ALA SER SEQRES 8 C 344 SER TRP SER TYR ILE VAL GLU THR SER ASN SER ASP ASN SEQRES 9 C 344 GLY THR CYS TYR PRO GLY ASP PHE ILE ASN TYR GLU GLU SEQRES 10 C 344 LEU ARG GLU GLN LEU SER SER VAL SER SER PHE GLU ARG SEQRES 11 C 344 PHE GLU ILE PHE PRO LYS THR SER SER TRP PRO ASN HIS SEQRES 12 C 344 ASP SER ASN LYS GLY VAL THR ALA ALA CYS PRO HIS ALA SEQRES 13 C 344 GLY ALA LYS SER PHE TYR LYS ASN LEU ILE TRP LEU VAL SEQRES 14 C 344 LYS LYS GLY ASN SER TYR PRO LYS LEU ASN GLN SER TYR SEQRES 15 C 344 ILE ASN ASP LYS GLY LYS GLU VAL LEU VAL LEU TRP GLY SEQRES 16 C 344 ILE HIS HIS PRO SER THR THR ALA ASP GLN GLN SER LEU SEQRES 17 C 344 TYR GLN ASN ALA ASP ALA TYR VAL PHE VAL GLY THR SER SEQRES 18 C 344 ARG TYR SER LYS LYS PHE LYS PRO GLU ILE ALA THR ARG SEQRES 19 C 344 PRO LYS VAL ARG ASP GLN GLU GLY ARG MET ASN TYR TYR SEQRES 20 C 344 TRP THR LEU VAL GLU PRO GLY ASP LYS ILE THR PHE GLU SEQRES 21 C 344 ALA THR GLY ASN LEU VAL VAL PRO ARG TYR ALA PHE THR SEQRES 22 C 344 MET GLU ARG ASN ALA GLY SER GLY ILE ILE ILE SER ASP SEQRES 23 C 344 THR PRO VAL HIS ASP CYS ASN THR THR CYS GLN THR PRO SEQRES 24 C 344 GLU GLY ALA ILE ASN THR SER LEU PRO PHE GLN ASN ILE SEQRES 25 C 344 HIS PRO ILE THR ILE GLY LYS CYS PRO LYS TYR VAL LYS SEQRES 26 C 344 SER THR LYS LEU ARG LEU ALA THR GLY LEU ARG ASN VAL SEQRES 27 C 344 PRO SER ILE GLN SER ARG SEQRES 1 c 220 GLY LEU PHE GLY ALA ILE ALA GLY PHE ILE GLU GLY GLY SEQRES 2 c 220 TRP THR GLY MET VAL ASP GLY TRP TYR GLY TYR HIS HIS SEQRES 3 c 220 GLN ASN GLU GLN GLY SER GLY TYR ALA ALA ASP LEU LYS SEQRES 4 c 220 SER THR GLN ASN ALA ILE ASP LYS ILE THR ASN LYS VAL SEQRES 5 c 220 ASN SER VAL ILE GLU LYS MET ASN THR GLN PHE THR ALA SEQRES 6 c 220 VAL GLY LYS GLU PHE ASN HIS LEU GLU LYS ARG ILE GLU SEQRES 7 c 220 ASN LEU ASN LYS LYS VAL ASP ASP GLY PHE LEU ASP ILE SEQRES 8 c 220 TRP THR TYR ASN ALA GLU LEU LEU VAL LEU LEU GLU ASN SEQRES 9 c 220 GLU ARG THR LEU ASP TYR HIS ASP SER ASN VAL LYS ASN SEQRES 10 c 220 LEU TYR GLU LYS VAL ARG ASN GLN LEU LYS ASN ASN ALA SEQRES 11 c 220 LYS GLU ILE GLY ASN GLY CYS PHE GLU PHE TYR HIS LYS SEQRES 12 c 220 CYS ASP ASN THR CYS MET GLU SER VAL LYS ASN GLY THR SEQRES 13 c 220 TYR ASP TYR PRO LYS TYR SER GLU GLU ALA LYS LEU ASN SEQRES 14 c 220 ARG GLU LYS ILE ASP 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 SEQRES 1 B 344 MET LYS ALA ILE LEU VAL VAL LEU LEU TYR THR PHE THR SEQRES 2 B 344 THR ALA ASN ALA ASP THR LEU CYS ILE GLY TYR HIS ALA SEQRES 3 B 344 ASN ASN SER THR ASP THR VAL ASP THR VAL LEU GLU LYS SEQRES 4 B 344 ASN VAL THR VAL THR HIS SER VAL ASN LEU LEU GLU ASP SEQRES 5 B 344 LYS HIS ASN GLY LYS LEU CYS LYS LEU ARG GLY VAL ALA SEQRES 6 B 344 PRO LEU HIS LEU GLY LYS CYS ASN ILE ALA GLY TRP ILE SEQRES 7 B 344 LEU GLY ASN PRO GLU CYS GLU SER LEU SER THR ALA SER SEQRES 8 B 344 SER TRP SER TYR ILE VAL GLU THR SER ASN SER ASP ASN SEQRES 9 B 344 GLY THR CYS TYR PRO GLY ASP PHE ILE ASN TYR GLU GLU SEQRES 10 B 344 LEU ARG GLU GLN LEU SER SER VAL SER SER PHE GLU ARG SEQRES 11 B 344 PHE GLU ILE PHE PRO LYS THR SER SER TRP PRO ASN HIS SEQRES 12 B 344 ASP SER ASN LYS GLY VAL THR ALA ALA CYS PRO HIS ALA SEQRES 13 B 344 GLY ALA LYS SER PHE TYR LYS ASN LEU ILE TRP LEU VAL SEQRES 14 B 344 LYS LYS GLY ASN SER TYR PRO LYS LEU ASN GLN SER TYR SEQRES 15 B 344 ILE ASN ASP LYS GLY LYS GLU VAL LEU VAL LEU TRP GLY SEQRES 16 B 344 ILE HIS HIS PRO SER THR THR ALA ASP GLN GLN SER LEU SEQRES 17 B 344 TYR GLN ASN ALA ASP ALA TYR VAL PHE VAL GLY THR SER SEQRES 18 B 344 ARG TYR SER LYS LYS PHE LYS PRO GLU ILE ALA THR ARG SEQRES 19 B 344 PRO LYS VAL ARG ASP GLN GLU GLY ARG MET ASN TYR TYR SEQRES 20 B 344 TRP THR LEU VAL GLU PRO GLY ASP LYS ILE THR PHE GLU SEQRES 21 B 344 ALA THR GLY ASN LEU VAL VAL PRO ARG TYR ALA PHE THR SEQRES 22 B 344 MET GLU ARG ASN ALA GLY SER GLY ILE ILE ILE SER ASP SEQRES 23 B 344 THR PRO VAL HIS ASP CYS ASN THR THR CYS GLN THR PRO SEQRES 24 B 344 GLU GLY ALA ILE ASN THR SER LEU PRO PHE GLN ASN ILE SEQRES 25 B 344 HIS PRO ILE THR ILE GLY LYS CYS PRO LYS TYR VAL LYS SEQRES 26 B 344 SER THR LYS LEU ARG LEU ALA THR GLY LEU ARG ASN VAL SEQRES 27 B 344 PRO SER ILE GLN SER ARG SEQRES 1 b 220 GLY LEU PHE GLY ALA ILE ALA GLY PHE ILE GLU GLY GLY SEQRES 2 b 220 TRP THR GLY MET VAL ASP GLY TRP TYR GLY TYR HIS HIS SEQRES 3 b 220 GLN ASN GLU GLN GLY SER GLY TYR ALA ALA ASP LEU LYS SEQRES 4 b 220 SER THR GLN ASN ALA ILE ASP LYS ILE THR ASN LYS VAL SEQRES 5 b 220 ASN SER VAL ILE GLU LYS MET ASN THR GLN PHE THR ALA SEQRES 6 b 220 VAL GLY LYS GLU PHE ASN HIS LEU GLU LYS ARG ILE GLU SEQRES 7 b 220 ASN LEU ASN LYS LYS VAL ASP ASP GLY PHE LEU ASP ILE SEQRES 8 b 220 TRP THR TYR ASN ALA GLU LEU LEU VAL LEU LEU GLU ASN SEQRES 9 b 220 GLU ARG THR LEU ASP TYR HIS ASP SER ASN VAL LYS ASN SEQRES 10 b 220 LEU TYR GLU LYS VAL ARG ASN GLN LEU LYS ASN ASN ALA SEQRES 11 b 220 LYS GLU ILE GLY ASN GLY CYS PHE GLU PHE TYR HIS LYS SEQRES 12 b 220 CYS ASP ASN THR CYS MET GLU SER VAL LYS ASN GLY THR SEQRES 13 b 220 TYR ASP TYR PRO LYS TYR SER GLU GLU ALA LYS LEU ASN SEQRES 14 b 220 ARG GLU LYS ILE ASP 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 HET NAG D 1 14 HET NAG D 2 14 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 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 405 14 HET NAG c 301 14 HET NAG B 401 14 HET NAG B 402 14 HET NAG B 403 14 HET NAG B 404 14 HET NAG B 405 14 HET NAG B 406 14 HET NAG b 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 24(C8 H15 N O6) FORMUL 10 FUC C6 H12 O5 HELIX 1 AA1 ASN A 66 ILE A 71 1 6 HELIX 2 AA2 ASN A 107 SER A 116 1 10 HELIX 3 AA3 THR A 194 TYR A 202 1 9 HELIX 4 AA4 ASP a 37 LYS a 58 1 22 HELIX 5 AA5 ASN a 71 LEU a 73 5 3 HELIX 6 AA6 GLU a 74 LYS a 127 1 54 HELIX 7 AA7 ASP a 145 GLY a 155 1 11 HELIX 8 AA8 ASP a 158 ARG a 170 1 13 HELIX 9 AA9 ASN C 66 GLY C 73 1 8 HELIX 10 AB1 ASN C 107 SER C 116 1 10 HELIX 11 AB2 THR C 194 GLN C 203 1 10 HELIX 12 AB3 ASP c 37 LYS c 58 1 22 HELIX 13 AB4 GLU c 74 LYS c 127 1 54 HELIX 14 AB5 ASP c 145 GLY c 155 1 11 HELIX 15 AB6 ASP c 158 ILE c 173 1 16 HELIX 16 AB7 ASN B 66 ILE B 71 1 6 HELIX 17 AB8 ASN B 74 GLU B 78 5 5 HELIX 18 AB9 ASN B 107 LEU B 115 1 9 HELIX 19 AC1 THR B 194 TYR B 202 1 9 HELIX 20 AC2 ASP b 37 LYS b 58 1 22 HELIX 21 AC3 GLU b 74 LYS b 127 1 54 HELIX 22 AC4 ASP b 145 GLY b 155 1 11 HELIX 23 AC5 ASP b 158 GLU b 171 1 14 SHEET 1 AA1 2 GLU H 6 SER H 7 0 SHEET 2 AA1 2 SER H 21 CYS H 22 -1 O SER H 21 N SER H 7 SHEET 1 AA2 3 LEU H 45 ALA H 50 0 SHEET 2 AA2 3 LEU H 34 GLN H 39 -1 N TRP H 36 O VAL H 48 SHEET 3 AA2 3 VAL H 89 TYR H 90 -1 O VAL H 89 N GLN H 39 SHEET 1 AA3 3 LEU H 45 ALA H 50 0 SHEET 2 AA3 3 LEU H 34 GLN H 39 -1 N TRP H 36 O VAL H 48 SHEET 3 AA3 3 ALA H 93 ARG H 94 -1 O ALA H 93 N HIS H 35 SHEET 1 AA4 5 SER L 12 GLY L 13 0 SHEET 2 AA4 5 THR L 102 VAL L 106 1 O THR L 105 N GLY L 13 SHEET 3 AA4 5 ALA L 84 SER L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AA4 5 VAL L 33 HIS L 38 -1 N SER L 34 O SER L 89 SHEET 5 AA4 5 LYS L 45 LEU L 48 -1 O LEU L 48 N TRP L 35 SHEET 1 AA5 3 THR L 20 THR L 24 0 SHEET 2 AA5 3 THR L 70 THR L 74 -1 O ALA L 71 N CYS L 23 SHEET 3 AA5 3 SER L 63 SER L 67 -1 N SER L 67 O THR L 70 SHEET 1 AA6 5 GLY a 33 ALA a 36 0 SHEET 2 AA6 5 TYR a 22 HIS a 26 -1 N TYR a 24 O ALA a 35 SHEET 3 AA6 5 THR A 12 TYR A 17 -1 N GLY A 16 O GLY a 23 SHEET 4 AA6 5 CYS a 137 PHE a 140 -1 O PHE a 138 N LEU A 13 SHEET 5 AA6 5 ALA a 130 GLY a 134 -1 N LYS a 131 O GLU a 139 SHEET 1 AA7 2 ASP A 24 VAL A 26 0 SHEET 2 AA7 2 VAL A 34 VAL A 36 -1 O VAL A 34 N VAL A 26 SHEET 1 AA8 2 SER A 39 ASN A 41 0 SHEET 2 AA8 2 ARG A 323 ALA A 325 -1 O LEU A 324 N VAL A 40 SHEET 1 AA9 3 LEU A 43 GLU A 44 0 SHEET 2 AA9 3 PHE A 302 GLN A 303 1 O PHE A 302 N GLU A 44 SHEET 3 AA9 3 LYS A 315 TYR A 316 1 O LYS A 315 N GLN A 303 SHEET 1 AB1 2 LEU A 51 LEU A 54 0 SHEET 2 AB1 2 VAL A 282 THR A 287 1 O CYS A 285 N LYS A 53 SHEET 1 AB2 2 LEU A 60 GLY A 63 0 SHEET 2 AB2 2 ILE A 89 GLU A 91 1 O VAL A 90 N LEU A 60 SHEET 1 AB3 3 VAL A 118 PHE A 124 0 SHEET 2 AB3 3 ALA A 264 ARG A 269 -1 O ALA A 264 N PHE A 124 SHEET 3 AB3 3 GLU A 182 LEU A 184 -1 N LEU A 184 O PHE A 265 SHEET 1 AB4 2 LEU A 158 TRP A 160 0 SHEET 2 AB4 2 VAL A 259 PRO A 261 -1 O VAL A 260 N ILE A 159 SHEET 1 AB5 2 LEU A 186 HIS A 191 0 SHEET 2 AB5 2 ARG A 236 TRP A 241 -1 O ARG A 236 N HIS A 191 SHEET 1 AB6 3 SER A 217 PHE A 220 0 SHEET 2 AB6 3 VAL A 209 GLY A 212 -1 N VAL A 209 O PHE A 220 SHEET 3 AB6 3 THR A 251 ALA A 254 -1 O GLU A 253 N PHE A 210 SHEET 1 AB7 4 GLY A 294 ILE A 296 0 SHEET 2 AB7 4 CYS A 289 THR A 291 -1 N CYS A 289 O ILE A 296 SHEET 3 AB7 4 ILE A 310 GLY A 311 -1 O ILE A 310 N GLN A 290 SHEET 4 AB7 4 THR a 64 ALA a 65 -1 O THR a 64 N GLY A 311 SHEET 1 AB8 3 GLY C 16 TYR C 17 0 SHEET 2 AB8 3 TYR c 22 HIS c 25 -1 O GLY c 23 N GLY C 16 SHEET 3 AB8 3 TYR c 34 ALA c 36 -1 O ALA c 35 N TYR c 24 SHEET 1 AB9 2 THR C 25 VAL C 26 0 SHEET 2 AB9 2 VAL C 34 THR C 35 -1 O VAL C 34 N VAL C 26 SHEET 1 AC1 2 SER C 39 ASN C 41 0 SHEET 2 AC1 2 ARG C 323 ALA C 325 -1 O LEU C 324 N VAL C 40 SHEET 1 AC2 2 LEU C 51 LEU C 54 0 SHEET 2 AC2 2 VAL C 282 THR C 287 1 O HIS C 283 N LEU C 51 SHEET 1 AC3 3 LEU C 60 HIS C 61 0 SHEET 2 AC3 3 ILE C 89 GLU C 91 1 O VAL C 90 N LEU C 60 SHEET 3 AC3 3 ILE C 275 ILE C 277 1 O ILE C 276 N GLU C 91 SHEET 1 AC4 2 HIS C 136 ASP C 137 0 SHEET 2 AC4 2 VAL C 162 LYS C 163 -1 O VAL C 162 N ASP C 137 SHEET 1 AC5 2 LEU C 158 ILE C 159 0 SHEET 2 AC5 2 VAL C 260 PRO C 261 -1 O VAL C 260 N ILE C 159 SHEET 1 AC6 4 GLN C 173 ILE C 176 0 SHEET 2 AC6 4 LYS C 249 ALA C 254 -1 O PHE C 252 N GLN C 173 SHEET 3 AC6 4 VAL C 209 THR C 213 -1 N PHE C 210 O GLU C 253 SHEET 4 AC6 4 LYS C 219 PHE C 220 -1 O PHE C 220 N VAL C 209 SHEET 1 AC7 3 ARG C 236 VAL C 244 0 SHEET 2 AC7 3 GLU C 182 HIS C 191 -1 N HIS C 191 O ARG C 236 SHEET 3 AC7 3 PHE C 265 MET C 267 -1 O MET C 267 N GLU C 182 SHEET 1 AC8 2 CYS C 289 GLN C 290 0 SHEET 2 AC8 2 ALA C 295 ILE C 296 -1 O ILE C 296 N CYS C 289 SHEET 1 AC9 2 PHE C 302 GLN C 303 0 SHEET 2 AC9 2 LYS C 315 TYR C 316 1 O LYS C 315 N GLN C 303 SHEET 1 AD1 2 ALA c 130 GLU c 132 0 SHEET 2 AD1 2 PHE c 138 PHE c 140 -1 O GLU c 139 N LYS c 131 SHEET 1 AD2 5 SER b 32 ALA b 35 0 SHEET 2 AD2 5 TYR b 22 GLN b 27 -1 N HIS b 26 O GLY b 33 SHEET 3 AD2 5 LEU B 13 TYR B 17 -1 N CYS B 14 O HIS b 25 SHEET 4 AD2 5 CYS b 137 PHE b 140 -1 O PHE b 138 N LEU B 13 SHEET 5 AD2 5 ALA b 130 ILE b 133 -1 N ILE b 133 O CYS b 137 SHEET 1 AD3 2 THR B 25 ASP B 27 0 SHEET 2 AD3 2 LYS B 32 THR B 35 -1 O VAL B 34 N VAL B 26 SHEET 1 AD4 2 VAL B 40 ASN B 41 0 SHEET 2 AD4 2 ARG B 323 LEU B 324 -1 O LEU B 324 N VAL B 40 SHEET 1 AD5 3 LEU B 43 GLU B 44 0 SHEET 2 AD5 3 PHE B 302 GLN B 303 1 O PHE B 302 N GLU B 44 SHEET 3 AD5 3 LYS B 315 TYR B 316 1 O LYS B 315 N GLN B 303 SHEET 1 AD6 2 LEU B 51 LEU B 54 0 SHEET 2 AD6 2 VAL B 282 THR B 287 1 O CYS B 285 N LYS B 53 SHEET 1 AD7 3 LEU B 60 GLY B 63 0 SHEET 2 AD7 3 ILE B 89 GLU B 91 1 O VAL B 90 N LEU B 62 SHEET 3 AD7 3 ILE B 275 ILE B 277 1 O ILE B 276 N GLU B 91 SHEET 1 AD8 4 VAL B 118 PHE B 124 0 SHEET 2 AD8 4 ALA B 264 ARG B 269 -1 O ALA B 264 N PHE B 124 SHEET 3 AD8 4 GLU B 182 HIS B 191 -1 N LEU B 184 O PHE B 265 SHEET 4 AD8 4 ARG B 236 VAL B 244 -1 O ARG B 236 N HIS B 191 SHEET 1 AD9 2 LEU B 158 TRP B 160 0 SHEET 2 AD9 2 VAL B 259 PRO B 261 -1 O VAL B 260 N ILE B 159 SHEET 1 AE1 4 LEU B 171 ILE B 176 0 SHEET 2 AE1 4 LYS B 249 ALA B 254 -1 O PHE B 252 N GLN B 173 SHEET 3 AE1 4 VAL B 209 GLY B 212 -1 N PHE B 210 O GLU B 253 SHEET 4 AE1 4 SER B 217 PHE B 220 -1 O PHE B 220 N VAL B 209 SHEET 1 AE2 2 THR B 309 ILE B 310 0 SHEET 2 AE2 2 ALA b 65 VAL b 66 -1 O VAL b 66 N THR B 309 SSBOND 1 CYS H 22 CYS H 92 1555 1555 2.04 SSBOND 2 CYS L 23 CYS L 88 1555 1555 2.03 SSBOND 3 CYS A 14 CYS a 137 1555 1555 2.04 SSBOND 4 CYS A 65 CYS A 77 1555 1555 2.03 SSBOND 5 CYS A 100 CYS A 146 1555 1555 2.03 SSBOND 6 CYS a 144 CYS a 148 1555 1555 2.03 SSBOND 7 CYS C 14 CYS c 137 1555 1555 2.03 SSBOND 8 CYS C 65 CYS C 77 1555 1555 2.02 SSBOND 9 CYS C 100 CYS C 146 1555 1555 2.03 SSBOND 10 CYS C 289 CYS C 313 1555 1555 2.02 SSBOND 11 CYS c 144 CYS c 148 1555 1555 2.03 SSBOND 12 CYS B 14 CYS b 137 1555 1555 2.03 SSBOND 13 CYS B 65 CYS B 77 1555 1555 2.03 SSBOND 14 CYS B 100 CYS B 146 1555 1555 2.02 SSBOND 15 CYS b 144 CYS b 148 1555 1555 2.03 LINK ND2 ASN A 21 C1 NAG E 1 1555 1555 1.45 LINK ND2 ASN A 33 C1 NAG A 401 1555 1555 1.44 LINK ND2 ASN A 97 C1 NAG D 1 1555 1555 1.43 LINK ND2 ASN A 172 C1 NAG A 403 1555 1555 1.44 LINK ND2 ASN A 286 C1 NAG A 402 1555 1555 1.44 LINK ND2 ASN A 297 C1 NAG A 404 1555 1555 1.45 LINK ND2 ASN a 154 C1 NAG a 301 1555 1555 1.44 LINK ND2 ASN C 21 C1 NAG C 401 1555 1555 1.45 LINK ND2 ASN C 33 C1 NAG C 402 1555 1555 1.44 LINK ND2 ASN C 97 C1 NAG F 1 1555 1555 1.43 LINK ND2 ASN C 172 C1 NAG C 405 1555 1555 1.45 LINK ND2 ASN C 286 C1 NAG C 403 1555 1555 1.44 LINK ND2 ASN C 297 C1 NAG C 404 1555 1555 1.44 LINK ND2 ASN c 154 C1 NAG c 301 1555 1555 1.44 LINK ND2 ASN B 21 C1 NAG B 401 1555 1555 1.44 LINK ND2 ASN B 33 C1 NAG B 402 1555 1555 1.44 LINK ND2 ASN B 97 C1 NAG B 406 1555 1555 1.43 LINK ND2 ASN B 172 C1 NAG B 405 1555 1555 1.44 LINK ND2 ASN B 286 C1 NAG B 403 1555 1555 1.44 LINK ND2 ASN B 297 C1 NAG B 404 1555 1555 1.44 LINK ND2 ASN b 154 C1 NAG b 301 1555 1555 1.44 LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.44 LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.45 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 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