HEADER VIRAL PROTEIN/IMMUNE SYSTEM 06-FEB-25 9N7S TITLE H1 HEMAGGLUTININ (A/CALIFORNIA/04/2009) WITH E47K MUTATION IN HA2 IN TITLE 2 COMPLEX WITH CENTRAL STEM-TARGETING FAB ST10 COMPND MOL_ID: 1; COMPND 2 MOLECULE: H1 HA2; COMPND 3 CHAIN: b, a, c; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: ST10 LIGHT CHAIN FAB; COMPND 7 CHAIN: L; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: H1 HA1; COMPND 11 CHAIN: C, A, B; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 4; COMPND 14 MOLECULE: ST10 HEAVY CHAIN FAB; COMPND 15 CHAIN: H; COMPND 16 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS; SOURCE 3 ORGANISM_TAXID: 11320; SOURCE 4 STRAIN: A/CALIFORNIA/04/2009; 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: INFLUENZA A VIRUS; SOURCE 16 ORGANISM_TAXID: 11320; SOURCE 17 STRAIN: A/CALIFORNIA/04/2009; 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: HOMO SAPIENS; SOURCE 23 ORGANISM_TAXID: 9606; 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 9N7S 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. 2.97 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) : 2.970 REMARK 3 NUMBER OF PARTICLES : 133491 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 9N7S 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_1000292624. 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/CALIFORNIA/04/2009) WITH REMARK 245 E47K MUTATION IN HA2 IN COMPLEX REMARK 245 WITH CENTRAL STEM-TARGETING FAB REMARK 245 ST10 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) : 4500.00 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: b, a, L, c, C, A, B, H, 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 ASP b 174 REMARK 465 GLY b 175 REMARK 465 SER 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 GLY b 206 REMARK 465 LEU b 207 REMARK 465 ASN b 208 REMARK 465 ASP b 209 REMARK 465 ILE b 210 REMARK 465 PHE b 211 REMARK 465 GLU b 212 REMARK 465 ALA b 213 REMARK 465 GLN b 214 REMARK 465 LYS b 215 REMARK 465 ILE b 216 REMARK 465 GLU b 217 REMARK 465 TRP b 218 REMARK 465 HIS b 219 REMARK 465 GLU b 220 REMARK 465 GLY b 221 REMARK 465 HIS b 222 REMARK 465 HIS b 223 REMARK 465 HIS b 224 REMARK 465 HIS b 225 REMARK 465 HIS b 226 REMARK 465 HIS b 227 REMARK 465 ILE a 173 REMARK 465 ASP a 174 REMARK 465 GLY a 175 REMARK 465 SER 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 GLY a 206 REMARK 465 LEU a 207 REMARK 465 ASN a 208 REMARK 465 ASP a 209 REMARK 465 ILE a 210 REMARK 465 PHE a 211 REMARK 465 GLU a 212 REMARK 465 ALA a 213 REMARK 465 GLN a 214 REMARK 465 LYS a 215 REMARK 465 ILE a 216 REMARK 465 GLU a 217 REMARK 465 TRP a 218 REMARK 465 HIS a 219 REMARK 465 GLU a 220 REMARK 465 GLY a 221 REMARK 465 HIS a 222 REMARK 465 HIS a 223 REMARK 465 HIS a 224 REMARK 465 HIS a 225 REMARK 465 HIS a 226 REMARK 465 HIS a 227 REMARK 465 ASP L 1 REMARK 465 LYS L 107 REMARK 465 ASP c 174 REMARK 465 GLY c 175 REMARK 465 SER 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 GLY c 206 REMARK 465 LEU c 207 REMARK 465 ASN c 208 REMARK 465 ASP c 209 REMARK 465 ILE c 210 REMARK 465 PHE c 211 REMARK 465 GLU c 212 REMARK 465 ALA c 213 REMARK 465 GLN c 214 REMARK 465 LYS c 215 REMARK 465 ILE c 216 REMARK 465 GLU c 217 REMARK 465 TRP c 218 REMARK 465 HIS c 219 REMARK 465 GLU c 220 REMARK 465 GLY c 221 REMARK 465 HIS c 222 REMARK 465 HIS c 223 REMARK 465 HIS c 224 REMARK 465 HIS c 225 REMARK 465 HIS c 226 REMARK 465 HIS c 227 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 ALA C 6 REMARK 465 THR C 7 REMARK 465 ALA C 8 REMARK 465 ASN C 9 REMARK 465 ALA C 10 REMARK 465 ILE C 323 REMARK 465 PRO C 324 REMARK 465 SER C 325 REMARK 465 ILE C 326 REMARK 465 GLN C 327 REMARK 465 SER C 328 REMARK 465 ARG C 329 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 ALA A 6 REMARK 465 THR A 7 REMARK 465 ALA A 8 REMARK 465 ASN A 9 REMARK 465 ALA A 10 REMARK 465 ILE A 323 REMARK 465 PRO A 324 REMARK 465 SER A 325 REMARK 465 ILE A 326 REMARK 465 GLN A 327 REMARK 465 SER A 328 REMARK 465 ARG A 329 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 ALA B 6 REMARK 465 THR B 7 REMARK 465 ALA B 8 REMARK 465 ASN B 9 REMARK 465 ALA B 10 REMARK 465 ASP B 11 REMARK 465 ILE B 326 REMARK 465 GLN B 327 REMARK 465 SER B 328 REMARK 465 ARG B 329 REMARK 465 GLN H 1 REMARK 465 SER H 112 REMARK 465 SER H 113 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 OG1 THR C 283 O GLY C 286 2.08 REMARK 500 OG SER b 151 O THR b 156 2.09 REMARK 500 OG1 THR L 63 OG1 THR L 74 2.12 REMARK 500 O CYS B 139 OG SER B 146 2.12 REMARK 500 OE2 GLU b 97 OG SER B 311 2.15 REMARK 500 OH TYR A 201 OE2 GLU A 246 2.15 REMARK 500 OE2 GLU a 97 OG SER A 311 2.17 REMARK 500 OG SER b 113 O LEU c 2 2.17 REMARK 500 OG SER H 65 O4 NAG E 1 2.17 REMARK 500 OG SER H 70 OG SER H 79 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 LYS b 143 66.28 61.33 REMARK 500 ALA L 51 -6.27 73.48 REMARK 500 SER L 52 87.68 -156.07 REMARK 500 THR L 53 146.69 -174.04 REMARK 500 ARG L 96 94.09 -69.51 REMARK 500 GLU c 11 -9.78 76.99 REMARK 500 GLN c 27 45.62 -140.61 REMARK 500 CYS c 137 64.98 61.35 REMARK 500 LYS c 143 61.71 62.21 REMARK 500 LEU C 13 50.55 -117.65 REMARK 500 GLN C 196 -7.13 75.29 REMARK 500 ALA C 263 -114.33 56.71 REMARK 500 ASN C 296 24.73 -141.46 REMARK 500 ILE C 297 -60.59 -91.00 REMARK 500 LEU A 61 57.87 -93.40 REMARK 500 TYR A 148 150.67 -48.80 REMARK 500 ASP A 171 18.66 -141.42 REMARK 500 GLN A 196 -6.10 74.80 REMARK 500 THR A 290 48.89 -88.79 REMARK 500 ASN A 296 18.77 -141.67 REMARK 500 GLU B 75 32.02 -97.06 REMARK 500 PRO B 99 174.63 -59.22 REMARK 500 ASP B 104 60.35 61.40 REMARK 500 ASN B 289 73.10 -100.72 REMARK 500 ASN B 296 27.99 -140.27 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-49098 RELATED DB: EMDB REMARK 900 H1 HEMAGGLUTININ (A/CALIFORNIA/04/2009) WITH E47K MUTATION IN HA2 REMARK 900 IN COMPLEX WITH CENTRAL STEM-TARGETING FAB ST10 DBREF 9N7S b 1 227 PDB 9N7S 9N7S 1 227 DBREF 9N7S a 1 227 PDB 9N7S 9N7S 1 227 DBREF 9N7S L 1 107 PDB 9N7S 9N7S 1 107 DBREF 9N7S c 1 227 PDB 9N7S 9N7S 1 227 DBREF 9N7S C -6 329 PDB 9N7S 9N7S -6 329 DBREF 9N7S A -6 329 PDB 9N7S 9N7S -6 329 DBREF 9N7S B -6 329 PDB 9N7S 9N7S -6 329 DBREF 9N7S H 1 113 PDB 9N7S 9N7S 1 113 SEQRES 1 b 227 GLY LEU PHE GLY ALA ILE ALA GLY PHE ILE GLU GLY GLY SEQRES 2 b 227 TRP THR GLY MET VAL ASP GLY TRP TYR GLY TYR HIS HIS SEQRES 3 b 227 GLN ASN GLU GLN GLY SER GLY TYR ALA ALA ASP LEU LYS SEQRES 4 b 227 SER THR GLN ASN ALA ILE ASP LYS ILE THR ASN LYS VAL SEQRES 5 b 227 ASN SER VAL ILE GLU LYS MET ASN THR GLN PHE THR ALA SEQRES 6 b 227 VAL GLY LYS GLU PHE ASN HIS LEU GLU LYS ARG ILE GLU SEQRES 7 b 227 ASN LEU ASN LYS LYS VAL ASP ASP GLY PHE LEU ASP ILE SEQRES 8 b 227 TRP THR TYR ASN ALA GLU LEU LEU VAL LEU LEU GLU ASN SEQRES 9 b 227 GLU ARG THR LEU ASP TYR HIS ASP SER ASN VAL LYS ASN SEQRES 10 b 227 LEU TYR GLU LYS VAL ARG SER GLN LEU LYS ASN ASN ALA SEQRES 11 b 227 LYS GLU ILE GLY ASN GLY CYS PHE GLU PHE TYR HIS LYS SEQRES 12 b 227 CYS ASP ASN THR CYS MET GLU SER VAL LYS ASN GLY THR SEQRES 13 b 227 TYR ASP TYR PRO LYS TYR SER GLU GLU ALA LYS LEU ASN SEQRES 14 b 227 ARG GLU GLU ILE ASP GLY SER GLY TYR ILE PRO GLU ALA SEQRES 15 b 227 PRO ARG ASP GLY GLN ALA TYR VAL ARG LYS ASP GLY GLU SEQRES 16 b 227 TRP VAL LEU LEU SER THR PHE LEU GLY SER GLY LEU ASN SEQRES 17 b 227 ASP ILE PHE GLU ALA GLN LYS ILE GLU TRP HIS GLU GLY SEQRES 18 b 227 HIS HIS HIS HIS HIS HIS SEQRES 1 a 227 GLY LEU PHE GLY ALA ILE ALA GLY PHE ILE GLU GLY GLY SEQRES 2 a 227 TRP THR GLY MET VAL ASP GLY TRP TYR GLY TYR HIS HIS SEQRES 3 a 227 GLN ASN GLU GLN GLY SER GLY TYR ALA ALA ASP LEU LYS SEQRES 4 a 227 SER THR GLN ASN ALA ILE ASP LYS ILE THR ASN LYS VAL SEQRES 5 a 227 ASN SER VAL ILE GLU LYS MET ASN THR GLN PHE THR ALA SEQRES 6 a 227 VAL GLY LYS GLU PHE ASN HIS LEU GLU LYS ARG ILE GLU SEQRES 7 a 227 ASN LEU ASN LYS LYS VAL ASP ASP GLY PHE LEU ASP ILE SEQRES 8 a 227 TRP THR TYR ASN ALA GLU LEU LEU VAL LEU LEU GLU ASN SEQRES 9 a 227 GLU ARG THR LEU ASP TYR HIS ASP SER ASN VAL LYS ASN SEQRES 10 a 227 LEU TYR GLU LYS VAL ARG SER GLN LEU LYS ASN ASN ALA SEQRES 11 a 227 LYS GLU ILE GLY ASN GLY CYS PHE GLU PHE TYR HIS LYS SEQRES 12 a 227 CYS ASP ASN THR CYS MET GLU SER VAL LYS ASN GLY THR SEQRES 13 a 227 TYR ASP TYR PRO LYS TYR SER GLU GLU ALA LYS LEU ASN SEQRES 14 a 227 ARG GLU GLU ILE ASP GLY SER GLY TYR ILE PRO GLU ALA SEQRES 15 a 227 PRO ARG ASP GLY GLN ALA TYR VAL ARG LYS ASP GLY GLU SEQRES 16 a 227 TRP VAL LEU LEU SER THR PHE LEU GLY SER GLY LEU ASN SEQRES 17 a 227 ASP ILE PHE GLU ALA GLN LYS ILE GLU TRP HIS GLU GLY SEQRES 18 a 227 HIS HIS HIS HIS HIS HIS SEQRES 1 L 113 ASP ILE VAL LEU THR GLN SER PRO ASP SER LEU ALA VAL SEQRES 2 L 113 SER LEU GLY GLU ARG ALA SER ILE ASN CYS ARG SER SER SEQRES 3 L 113 GLN SER LEU LEU ASN ARG SER ASN ASN LYS ASN PHE LEU SEQRES 4 L 113 ALA TRP TYR GLN GLN THR PRO GLY GLN PRO PRO LYS LEU SEQRES 5 L 113 LEU ILE TYR TRP ALA SER THR ARG GLU SER GLY VAL PRO SEQRES 6 L 113 ASP ARG PHE THR GLY SER GLY SER GLY ALA ASP PHE THR SEQRES 7 L 113 LEU THR ILE SER SER LEU GLN ALA GLU ASP VAL ALA VAL SEQRES 8 L 113 TYR TYR CYS GLN GLN TYR TYR THR THR PRO ARG THR PHE SEQRES 9 L 113 GLY GLN GLY THR LYS VAL GLU ILE LYS SEQRES 1 c 227 GLY LEU PHE GLY ALA ILE ALA GLY PHE ILE GLU GLY GLY SEQRES 2 c 227 TRP THR GLY MET VAL ASP GLY TRP TYR GLY TYR HIS HIS SEQRES 3 c 227 GLN ASN GLU GLN GLY SER GLY TYR ALA ALA ASP LEU LYS SEQRES 4 c 227 SER THR GLN ASN ALA ILE ASP LYS ILE THR ASN LYS VAL SEQRES 5 c 227 ASN SER VAL ILE GLU LYS MET ASN THR GLN PHE THR ALA SEQRES 6 c 227 VAL GLY LYS GLU PHE ASN HIS LEU GLU LYS ARG ILE GLU SEQRES 7 c 227 ASN LEU ASN LYS LYS VAL ASP ASP GLY PHE LEU ASP ILE SEQRES 8 c 227 TRP THR TYR ASN ALA GLU LEU LEU VAL LEU LEU GLU ASN SEQRES 9 c 227 GLU ARG THR LEU ASP TYR HIS ASP SER ASN VAL LYS ASN SEQRES 10 c 227 LEU TYR GLU LYS VAL ARG SER GLN LEU LYS ASN ASN ALA SEQRES 11 c 227 LYS GLU ILE GLY ASN GLY CYS PHE GLU PHE TYR HIS LYS SEQRES 12 c 227 CYS ASP ASN THR CYS MET GLU SER VAL LYS ASN GLY THR SEQRES 13 c 227 TYR ASP TYR PRO LYS TYR SER GLU GLU ALA LYS LEU ASN SEQRES 14 c 227 ARG GLU GLU ILE ASP GLY SER GLY TYR ILE PRO GLU ALA SEQRES 15 c 227 PRO ARG ASP GLY GLN ALA TYR VAL ARG LYS ASP GLY GLU SEQRES 16 c 227 TRP VAL LEU LEU SER THR PHE LEU GLY SER GLY LEU ASN SEQRES 17 c 227 ASP ILE PHE GLU ALA GLN LYS ILE GLU TRP HIS GLU GLY SEQRES 18 c 227 HIS HIS HIS HIS HIS HIS SEQRES 1 C 344 MET LYS ALA ILE LEU VAL VAL LEU LEU TYR THR PHE ALA 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 PRO SER SER ASP ASN SEQRES 9 C 344 GLY THR CYS TYR PRO GLY ASP PHE ILE ASP 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 SER LYS 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 SER ALA ASP GLN GLN SER LEU SEQRES 17 C 344 TYR GLN ASN ALA ASP THR TYR VAL PHE VAL GLY SER SER SEQRES 18 C 344 ARG TYR SER LYS LYS PHE LYS PRO GLU ILE ALA ILE 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 ALA 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 LYS 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 ILE SEQRES 27 C 344 PRO SER ILE GLN SER ARG SEQRES 1 A 344 MET LYS ALA ILE LEU VAL VAL LEU LEU TYR THR PHE ALA 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 PRO SER SER ASP ASN SEQRES 9 A 344 GLY THR CYS TYR PRO GLY ASP PHE ILE ASP 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 SER LYS 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 SER ALA ASP GLN GLN SER LEU SEQRES 17 A 344 TYR GLN ASN ALA ASP THR TYR VAL PHE VAL GLY SER SER SEQRES 18 A 344 ARG TYR SER LYS LYS PHE LYS PRO GLU ILE ALA ILE 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 ALA 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 LYS 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 ILE SEQRES 27 A 344 PRO SER ILE GLN SER ARG SEQRES 1 B 344 MET LYS ALA ILE LEU VAL VAL LEU LEU TYR THR PHE ALA 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 PRO SER SER ASP ASN SEQRES 9 B 344 GLY THR CYS TYR PRO GLY ASP PHE ILE ASP 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 SER LYS 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 SER ALA ASP GLN GLN SER LEU SEQRES 17 B 344 TYR GLN ASN ALA ASP THR TYR VAL PHE VAL GLY SER SER SEQRES 18 B 344 ARG TYR SER LYS LYS PHE LYS PRO GLU ILE ALA ILE 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 ALA 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 LYS 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 ILE SEQRES 27 B 344 PRO SER ILE GLN SER ARG SEQRES 1 H 126 GLN VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 H 126 PRO SER GLY THR LEU SER LEU THR CYS ALA VAL SER GLY SEQRES 3 H 126 GLY SER ILE SER SER ASN ASN TRP TRP THR TRP VAL ARG SEQRES 4 H 126 GLN SER PRO GLY LYS GLY LEU GLU TRP MET GLY GLU ILE SEQRES 5 H 126 PHE HIS SER GLY SER THR SER TYR ASN PRO SER LEU ASN SEQRES 6 H 126 SER ARG VAL THR MET SER VAL ASP LYS SER LYS ASN GLN SEQRES 7 H 126 PHE SER LEU ARG LEU ASN SER LEU THR ALA ALA ASP THR SEQRES 8 H 126 ALA VAL TYR TYR CYS ALA ARG LEU GLN GLN ILE MET ILE SEQRES 9 H 126 TYR GLY LEU ILE ARG GLY GLY ALA MET ASP VAL TRP GLY SEQRES 10 H 126 GLN GLY THR THR VAL THR VAL SER SER HET NAG D 1 14 HET FUC D 2 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 NAG c 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 A 401 14 HET NAG A 402 14 HET NAG A 403 14 HET NAG A 404 14 HET NAG A 405 14 HET NAG B 401 14 HET NAG B 402 14 HET NAG B 403 14 HET NAG B 404 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 20(C8 H15 N O6) FORMUL 9 FUC 2(C6 H12 O5) HELIX 1 AA1 ASP b 37 LYS b 58 1 22 HELIX 2 AA2 GLU b 74 LEU b 126 1 53 HELIX 3 AA3 ASP b 145 ASN b 154 1 10 HELIX 4 AA4 TYR b 162 ILE b 173 1 12 HELIX 5 AA5 ASP a 37 LYS a 58 1 22 HELIX 6 AA6 GLU a 74 LEU a 126 1 53 HELIX 7 AA7 ASP a 145 GLY a 155 1 11 HELIX 8 AA8 TYR a 162 GLU a 172 1 11 HELIX 9 AA9 ASP c 37 LYS c 58 1 22 HELIX 10 AB1 LYS c 75 LEU c 126 1 52 HELIX 11 AB2 ASP c 145 GLY c 155 1 11 HELIX 12 AB3 ASP c 158 GLU c 172 1 15 HELIX 13 AB4 ASN C 65 GLY C 72 1 8 HELIX 14 AB5 ASN C 73 GLU C 77 5 5 HELIX 15 AB6 ASP C 104 LEU C 112 1 9 HELIX 16 AB7 THR C 187 TYR C 195 1 9 HELIX 17 AB8 ASN A 65 GLY A 72 1 8 HELIX 18 AB9 ASP A 104 LEU A 112 1 9 HELIX 19 AC1 THR A 187 GLN A 196 1 10 HELIX 20 AC2 ASN B 65 LEU B 71 1 7 HELIX 21 AC3 ASN B 73 GLU B 77 5 5 HELIX 22 AC4 ASP B 104 LEU B 112 1 9 HELIX 23 AC5 THR B 187 TYR B 195 1 9 HELIX 24 AC6 PRO H 61 ASN H 64 5 4 HELIX 25 AC7 THR H 83 THR H 87 5 5 SHEET 1 AA1 5 GLY b 33 TYR b 34 0 SHEET 2 AA1 5 TYR b 22 HIS b 26 -1 N HIS b 26 O GLY b 33 SHEET 3 AA1 5 LEU B 13 TYR B 17 -1 O CYS B 14 N HIS b 25 SHEET 4 AA1 5 CYS b 137 PHE b 140 -1 N PHE b 138 O LEU B 13 SHEET 5 AA1 5 ALA b 130 LYS b 131 -1 N LYS b 131 O GLU b 139 SHEET 1 AA2 4 THR b 64 ALA b 65 0 SHEET 2 AA2 4 ILE B 302 GLY B 303 -1 O GLY B 303 N THR b 64 SHEET 3 AA2 4 CYS B 281 GLN B 282 -1 N GLN B 282 O ILE B 302 SHEET 4 AA2 4 ALA B 287 ILE B 288 -1 O ILE B 288 N CYS B 281 SHEET 1 AA3 5 GLY a 31 ALA a 36 0 SHEET 2 AA3 5 TYR a 22 ASN a 28 -1 N ASN a 28 O GLY a 31 SHEET 3 AA3 5 THR A 12 TYR A 17 -1 O THR A 12 N GLN a 27 SHEET 4 AA3 5 PHE a 138 PHE a 140 -1 N PHE a 138 O LEU A 13 SHEET 5 AA3 5 ALA a 130 LYS a 131 -1 N LYS a 131 O GLU a 139 SHEET 1 AA4 4 PHE a 63 ALA a 65 0 SHEET 2 AA4 4 ILE A 302 LYS A 304 -1 O GLY A 303 N THR a 64 SHEET 3 AA4 4 CYS A 281 GLN A 282 -1 N GLN A 282 O ILE A 302 SHEET 4 AA4 4 ALA A 287 ILE A 288 -1 O ILE A 288 N CYS A 281 SHEET 1 AA5 4 LEU L 4 THR L 5 0 SHEET 2 AA5 4 ALA L 19 SER L 25 -1 O ARG L 24 N THR L 5 SHEET 3 AA5 4 ASP L 70 ILE L 75 -1 O LEU L 73 N ILE L 21 SHEET 4 AA5 4 PHE L 62 SER L 67 -1 N SER L 65 O THR L 72 SHEET 1 AA6 5 SER L 10 ALA L 12 0 SHEET 2 AA6 5 THR L 102 GLU L 105 1 O GLU L 105 N LEU L 11 SHEET 3 AA6 5 VAL L 85 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AA6 5 LEU L 33 GLN L 38 -1 N ALA L 34 O GLN L 89 SHEET 5 AA6 5 LYS L 45 TYR L 49 -1 O LYS L 45 N GLN L 37 SHEET 1 AA7 2 LEU L 27C ASN L 27D 0 SHEET 2 AA7 2 LYS L 30 ASN L 31 -1 O LYS L 30 N ASN L 27D SHEET 1 AA8 3 GLY c 33 ALA c 36 0 SHEET 2 AA8 3 TYR c 22 HIS c 26 -1 N HIS c 26 O GLY c 33 SHEET 3 AA8 3 LEU C 13 TYR C 17 -1 O GLY C 16 N GLY c 23 SHEET 1 AA9 4 THR c 64 ALA c 65 0 SHEET 2 AA9 4 ILE C 302 GLY C 303 -1 O GLY C 303 N THR c 64 SHEET 3 AA9 4 CYS C 281 GLN C 282 -1 N GLN C 282 O ILE C 302 SHEET 4 AA9 4 ALA C 287 ILE C 288 -1 O ILE C 288 N CYS C 281 SHEET 1 AB1 2 ASP C 24 VAL C 26 0 SHEET 2 AB1 2 VAL C 34 VAL C 36 -1 O VAL C 34 N VAL C 26 SHEET 1 AB2 2 VAL C 40 ASN C 41 0 SHEET 2 AB2 2 ARG C 315 LEU C 316 -1 O LEU C 316 N VAL C 40 SHEET 1 AB3 3 LEU C 43 GLU C 44 0 SHEET 2 AB3 3 PHE C 294 GLN C 295 1 O PHE C 294 N GLU C 44 SHEET 3 AB3 3 LYS C 307 TYR C 308 1 O LYS C 307 N GLN C 295 SHEET 1 AB4 2 LEU C 51 LEU C 54 0 SHEET 2 AB4 2 VAL C 274 THR C 279 1 O CYS C 277 N LYS C 53 SHEET 1 AB5 3 LEU C 59 LEU C 61 0 SHEET 2 AB5 3 ILE C 87 GLU C 89 1 O VAL C 88 N LEU C 59 SHEET 3 AB5 3 ILE C 267 ILE C 269 1 O ILE C 268 N GLU C 89 SHEET 1 AB6 4 VAL C 115 GLU C 122 0 SHEET 2 AB6 4 TYR C 256 ARG C 262 -1 O ALA C 257 N PHE C 121 SHEET 3 AB6 4 GLU C 175 HIS C 184 -1 N LEU C 177 O PHE C 258 SHEET 4 AB6 4 ARG C 229 VAL C 237 -1 O ARG C 229 N HIS C 184 SHEET 1 AB7 2 THR C 136 HIS C 141 0 SHEET 2 AB7 2 ALA C 144 SER C 146 -1 O SER C 146 N THR C 136 SHEET 1 AB8 2 LEU C 151 TRP C 153 0 SHEET 2 AB8 2 VAL C 252 PRO C 254 -1 O VAL C 253 N ILE C 152 SHEET 1 AB9 4 LEU C 164 LYS C 166 0 SHEET 2 AB9 4 ILE C 243 ALA C 247 -1 O PHE C 245 N LYS C 166 SHEET 3 AB9 4 VAL C 202 SER C 206 -1 N GLY C 205 O THR C 244 SHEET 4 AB9 4 SER C 210 PHE C 213 -1 O PHE C 213 N VAL C 202 SHEET 1 AC1 2 ASP A 24 VAL A 26 0 SHEET 2 AC1 2 VAL A 34 VAL A 36 -1 O VAL A 34 N VAL A 26 SHEET 1 AC2 2 SER A 39 ASN A 41 0 SHEET 2 AC2 2 ARG A 315 ALA A 317 -1 O LEU A 316 N VAL A 40 SHEET 1 AC3 3 LEU A 43 GLU A 44 0 SHEET 2 AC3 3 PHE A 294 GLN A 295 1 O PHE A 294 N GLU A 44 SHEET 3 AC3 3 LYS A 307 TYR A 308 1 O LYS A 307 N GLN A 295 SHEET 1 AC4 2 LEU A 51 LEU A 54 0 SHEET 2 AC4 2 VAL A 274 THR A 279 1 O CYS A 277 N LYS A 53 SHEET 1 AC5 3 LEU A 59 LEU A 61 0 SHEET 2 AC5 3 ILE A 87 GLU A 89 1 O VAL A 88 N LEU A 59 SHEET 3 AC5 3 ILE A 267 ILE A 269 1 O ILE A 268 N ILE A 87 SHEET 1 AC6 5 VAL A 115 GLU A 122 0 SHEET 2 AC6 5 TYR A 256 ARG A 262 -1 O ALA A 259 N GLU A 119 SHEET 3 AC6 5 GLU A 175 HIS A 184 -1 N LEU A 177 O PHE A 258 SHEET 4 AC6 5 LEU A 251 PRO A 254 -1 O VAL A 252 N GLY A 181 SHEET 5 AC6 5 LEU A 151 TRP A 153 -1 N ILE A 152 O VAL A 253 SHEET 1 AC7 4 VAL A 115 GLU A 122 0 SHEET 2 AC7 4 TYR A 256 ARG A 262 -1 O ALA A 259 N GLU A 119 SHEET 3 AC7 4 GLU A 175 HIS A 184 -1 N LEU A 177 O PHE A 258 SHEET 4 AC7 4 ARG A 229 VAL A 237 -1 O VAL A 237 N VAL A 176 SHEET 1 AC8 2 THR A 136 PRO A 140 0 SHEET 2 AC8 2 LYS A 145 SER A 146 -1 O SER A 146 N THR A 136 SHEET 1 AC9 4 LEU A 164 ILE A 169 0 SHEET 2 AC9 4 LYS A 242 ALA A 247 -1 O PHE A 245 N LYS A 166 SHEET 3 AC9 4 VAL A 202 SER A 206 -1 N PHE A 203 O GLU A 246 SHEET 4 AC9 4 SER A 210 PHE A 213 -1 O LYS A 211 N VAL A 204 SHEET 1 AD1 2 ASP B 24 VAL B 26 0 SHEET 2 AD1 2 VAL B 34 VAL B 36 -1 O VAL B 36 N ASP B 24 SHEET 1 AD2 2 SER B 39 ASN B 41 0 SHEET 2 AD2 2 ARG B 315 ALA B 317 -1 O LEU B 316 N VAL B 40 SHEET 1 AD3 3 LEU B 43 GLU B 44 0 SHEET 2 AD3 3 PHE B 294 GLN B 295 1 O PHE B 294 N GLU B 44 SHEET 3 AD3 3 LYS B 307 TYR B 308 1 O LYS B 307 N GLN B 295 SHEET 1 AD4 3 LEU B 59 HIS B 60 0 SHEET 2 AD4 3 ILE B 87 GLU B 89 1 O VAL B 88 N LEU B 59 SHEET 3 AD4 3 ILE B 267 ILE B 269 1 O ILE B 268 N ILE B 87 SHEET 1 AD5 5 GLU B 119 GLU B 122 0 SHEET 2 AD5 5 TYR B 256 MET B 260 -1 O ALA B 257 N PHE B 121 SHEET 3 AD5 5 GLU B 175 HIS B 184 -1 N LEU B 177 O PHE B 258 SHEET 4 AD5 5 LEU B 251 PRO B 254 -1 O VAL B 252 N GLY B 181 SHEET 5 AD5 5 LEU B 151 TRP B 153 -1 N ILE B 152 O VAL B 253 SHEET 1 AD6 4 GLU B 119 GLU B 122 0 SHEET 2 AD6 4 TYR B 256 MET B 260 -1 O ALA B 257 N PHE B 121 SHEET 3 AD6 4 GLU B 175 HIS B 184 -1 N LEU B 177 O PHE B 258 SHEET 4 AD6 4 ARG B 229 VAL B 237 -1 O VAL B 237 N VAL B 176 SHEET 1 AD7 4 LEU B 164 LYS B 166 0 SHEET 2 AD7 4 PHE B 245 ALA B 247 -1 O PHE B 245 N LYS B 166 SHEET 3 AD7 4 VAL B 202 GLY B 205 -1 N PHE B 203 O GLU B 246 SHEET 4 AD7 4 SER B 210 PHE B 213 -1 O LYS B 211 N VAL B 204 SHEET 1 AD8 4 GLN H 3 SER H 7 0 SHEET 2 AD8 4 THR H 17 SER H 25 -1 O ALA H 23 N GLN H 5 SHEET 3 AD8 4 GLN H 77 ASN H 82A-1 O LEU H 80 N LEU H 20 SHEET 4 AD8 4 MET H 69 ASP H 72 -1 N ASP H 72 O GLN H 77 SHEET 1 AD9 5 THR H 57 TYR H 59 0 SHEET 2 AD9 5 GLY H 44 PHE H 52 -1 N GLU H 50 O SER H 58 SHEET 3 AD9 5 TRP H 34 SER H 40 -1 N TRP H 35 O ILE H 51 SHEET 4 AD9 5 ALA H 88 ILE H 100 -1 O TYR H 91 N VAL H 37 SHEET 5 AD9 5 LEU H 100C TRP H 103 -1 O ALA H 100H N GLN H 96 SHEET 1 AE1 5 THR H 57 TYR H 59 0 SHEET 2 AE1 5 GLY H 44 PHE H 52 -1 N GLU H 50 O SER H 58 SHEET 3 AE1 5 TRP H 34 SER H 40 -1 N TRP H 35 O ILE H 51 SHEET 4 AE1 5 ALA H 88 ILE H 100 -1 O TYR H 91 N VAL H 37 SHEET 5 AE1 5 THR H 107 VAL H 109 -1 O THR H 107 N TYR H 90 SSBOND 1 CYS b 144 CYS b 148 1555 1555 2.05 SSBOND 2 CYS a 144 CYS a 148 1555 1555 2.03 SSBOND 3 CYS L 23 CYS L 88 1555 1555 2.04 SSBOND 4 CYS c 137 CYS C 14 1555 1555 2.04 SSBOND 5 CYS c 144 CYS c 148 1555 1555 2.03 SSBOND 6 CYS C 64 CYS C 76 1555 1555 2.03 SSBOND 7 CYS C 97 CYS C 139 1555 1555 2.03 SSBOND 8 CYS C 281 CYS C 305 1555 1555 2.03 SSBOND 9 CYS A 52 CYS A 277 1555 1555 2.03 SSBOND 10 CYS A 64 CYS A 76 1555 1555 2.03 SSBOND 11 CYS A 97 CYS A 139 1555 1555 2.03 SSBOND 12 CYS B 52 CYS B 277 1555 1555 2.06 SSBOND 13 CYS B 64 CYS B 76 1555 1555 2.03 SSBOND 14 CYS B 97 CYS B 139 1555 1555 2.03 SSBOND 15 CYS B 281 CYS B 305 1555 1555 2.03 SSBOND 16 CYS H 22 CYS H 92 1555 1555 2.03 LINK ND2 ASN b 154 C1 NAG D 1 1555 1555 1.44 LINK ND2 ASN a 154 C1 NAG E 1 1555 1555 1.44 LINK ND2 ASN c 154 C1 NAG c 301 1555 1555 1.44 LINK ND2 ASN C 21 C1 NAG C 404 1555 1555 1.45 LINK ND2 ASN C 33 C1 NAG C 401 1555 1555 1.44 LINK ND2 ASN C 94 C1 NAG C 402 1555 1555 1.44 LINK ND2 ASN C 278 C1 NAG C 403 1555 1555 1.44 LINK ND2 ASN C 289 C1 NAG C 405 1555 1555 1.44 LINK ND2 ASN A 21 C1 NAG A 401 1555 1555 1.44 LINK ND2 ASN A 33 C1 NAG A 402 1555 1555 1.44 LINK ND2 ASN A 94 C1 NAG A 404 1555 1555 1.44 LINK ND2 ASN A 278 C1 NAG A 403 1555 1555 1.44 LINK ND2 ASN A 289 C1 NAG A 405 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 94 C1 NAG F 1 1555 1555 1.43 LINK ND2 ASN B 278 C1 NAG B 401 1555 1555 1.44 LINK ND2 ASN B 289 C1 NAG B 404 1555 1555 1.45 LINK O6 NAG D 1 C1 FUC D 2 1555 1555 1.44 LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.47 LINK O6 NAG E 1 C1 FUC E 3 1555 1555 1.45 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