HEADER VIRAL PROTEIN/IMMUNE SYSTEM 16-MAY-24 9BU6 TITLE VACCINE ELICITED FAB C968.180 WITH INFLUENZA H10 JD13 HA TRIMER COMPND MOL_ID: 1; COMPND 2 MOLECULE: FAB C968.180 HEAVY CHAIN; COMPND 3 CHAIN: A, E, I; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: FAB C968.180 LIGHT CHAIN; COMPND 7 CHAIN: B, F, J; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: HEMAGGLUTININ HA1; COMPND 11 CHAIN: C, G, K; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 4; COMPND 14 MOLECULE: HEMAGGLUTININ HA2; COMPND 15 CHAIN: D, H, L; COMPND 16 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_COMMON: HUMAN; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 13 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 15 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS; SOURCE 17 ORGANISM_TAXID: 11320; SOURCE 18 GENE: HA; SOURCE 19 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 20 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 21 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 22 MOL_ID: 4; SOURCE 23 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS; SOURCE 24 ORGANISM_TAXID: 11320; SOURCE 25 GENE: HA; SOURCE 26 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 27 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 28 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS VACCINE, VIRAL PROTEIN-IMMUNE SYSTEM COMPLEX, IMMUNE SYSTEM EXPDTA ELECTRON MICROSCOPY AUTHOR J.GORMAN,P.D.KWONG REVDAT 1 27-NOV-24 9BU6 0 JRNL AUTH J.GORMAN,P.D.KWONG JRNL TITL HUMAN VACCINATION WITH DIFFERENT GROUP 2 INFLUENZA SUBTYPES JRNL TITL 2 ALTERS EPITOPE TARGETING AND BREADTH OF HEMAGGLUTININ JRNL TITL 3 STEM-SPECIFIC B CELLS JRNL REF SCI TRANSL MED 2024 JRNL REFN ESSN 1946-6242 REMARK 2 REMARK 2 RESOLUTION. 3.65 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 : REAL REMARK 3 REFINEMENT PROTOCOL : FLEXIBLE FIT 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) : 3.650 REMARK 3 NUMBER OF PARTICLES : 81468 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 9BU6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-MAY-24. REMARK 100 THE DEPOSITION ID IS D_1000284127. 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 : VACCINE ELICITED FAB C968.180 REMARK 245 WITH INFLUENZA H10 JD13 HA REMARK 245 TRIMER REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 2.00 REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.40 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : 6067 REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 (6K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 800.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2500.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : NULL REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 5215.00 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) : 300 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: DODECAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J, REMARK 350 AND CHAINS: K, L, M, N, O, P, Q, R, S, REMARK 350 AND CHAINS: T, U 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 SER A 112 REMARK 465 SER A 113 REMARK 465 GLN C 328 REMARK 465 GLY C 329 REMARK 465 ARG C 330 REMARK 465 GLY D 1 REMARK 465 ASN D 174 REMARK 465 PRO D 175 REMARK 465 VAL D 176 REMARK 465 THR D 177 REMARK 465 GLY D 178 REMARK 465 SER D 179 REMARK 465 GLY D 180 REMARK 465 TYR D 181 REMARK 465 ILE D 182 REMARK 465 PRO D 183 REMARK 465 GLU D 184 REMARK 465 ALA D 185 REMARK 465 PRO D 186 REMARK 465 ARG D 187 REMARK 465 ASP D 188 REMARK 465 GLY D 189 REMARK 465 GLN D 190 REMARK 465 ALA D 191 REMARK 465 TYR D 192 REMARK 465 VAL D 193 REMARK 465 ARG D 194 REMARK 465 LYS D 195 REMARK 465 ASP D 196 REMARK 465 GLY D 197 REMARK 465 GLU D 198 REMARK 465 TRP D 199 REMARK 465 VAL D 200 REMARK 465 LEU D 201 REMARK 465 LEU D 202 REMARK 465 SER D 203 REMARK 465 THR D 204 REMARK 465 PHE D 205 REMARK 465 LEU D 206 REMARK 465 GLY D 207 REMARK 465 SER D 208 REMARK 465 GLY D 209 REMARK 465 LEU D 210 REMARK 465 ASN D 211 REMARK 465 ASP D 212 REMARK 465 ILE D 213 REMARK 465 PHE D 214 REMARK 465 GLU D 215 REMARK 465 ALA D 216 REMARK 465 GLN D 217 REMARK 465 LYS D 218 REMARK 465 ILE D 219 REMARK 465 GLU D 220 REMARK 465 TRP D 221 REMARK 465 HIS D 222 REMARK 465 GLU D 223 REMARK 465 GLY D 224 REMARK 465 HIS D 225 REMARK 465 HIS D 226 REMARK 465 HIS D 227 REMARK 465 HIS D 228 REMARK 465 HIS D 229 REMARK 465 HIS D 230 REMARK 465 SER E 112 REMARK 465 SER E 113 REMARK 465 GLN G 328 REMARK 465 GLY G 329 REMARK 465 ARG G 330 REMARK 465 GLY H 1 REMARK 465 ASN H 174 REMARK 465 PRO H 175 REMARK 465 VAL H 176 REMARK 465 THR H 177 REMARK 465 GLY H 178 REMARK 465 SER H 179 REMARK 465 GLY H 180 REMARK 465 TYR H 181 REMARK 465 ILE H 182 REMARK 465 PRO H 183 REMARK 465 GLU H 184 REMARK 465 ALA H 185 REMARK 465 PRO H 186 REMARK 465 ARG H 187 REMARK 465 ASP H 188 REMARK 465 GLY H 189 REMARK 465 GLN H 190 REMARK 465 ALA H 191 REMARK 465 TYR H 192 REMARK 465 VAL H 193 REMARK 465 ARG H 194 REMARK 465 LYS H 195 REMARK 465 ASP H 196 REMARK 465 GLY H 197 REMARK 465 GLU H 198 REMARK 465 TRP H 199 REMARK 465 VAL H 200 REMARK 465 LEU H 201 REMARK 465 LEU H 202 REMARK 465 SER H 203 REMARK 465 THR H 204 REMARK 465 PHE H 205 REMARK 465 LEU H 206 REMARK 465 GLY H 207 REMARK 465 SER H 208 REMARK 465 GLY H 209 REMARK 465 LEU H 210 REMARK 465 ASN H 211 REMARK 465 ASP H 212 REMARK 465 ILE H 213 REMARK 465 PHE H 214 REMARK 465 GLU H 215 REMARK 465 ALA H 216 REMARK 465 GLN H 217 REMARK 465 LYS H 218 REMARK 465 ILE H 219 REMARK 465 GLU H 220 REMARK 465 TRP H 221 REMARK 465 HIS H 222 REMARK 465 GLU H 223 REMARK 465 GLY H 224 REMARK 465 HIS H 225 REMARK 465 HIS H 226 REMARK 465 HIS H 227 REMARK 465 HIS H 228 REMARK 465 HIS H 229 REMARK 465 HIS H 230 REMARK 465 SER I 112 REMARK 465 SER I 113 REMARK 465 GLN K 328 REMARK 465 GLY K 329 REMARK 465 ARG K 330 REMARK 465 GLY L 1 REMARK 465 ASN L 174 REMARK 465 PRO L 175 REMARK 465 VAL L 176 REMARK 465 THR L 177 REMARK 465 GLY L 178 REMARK 465 SER L 179 REMARK 465 GLY L 180 REMARK 465 TYR L 181 REMARK 465 ILE L 182 REMARK 465 PRO L 183 REMARK 465 GLU L 184 REMARK 465 ALA L 185 REMARK 465 PRO L 186 REMARK 465 ARG L 187 REMARK 465 ASP L 188 REMARK 465 GLY L 189 REMARK 465 GLN L 190 REMARK 465 ALA L 191 REMARK 465 TYR L 192 REMARK 465 VAL L 193 REMARK 465 ARG L 194 REMARK 465 LYS L 195 REMARK 465 ASP L 196 REMARK 465 GLY L 197 REMARK 465 GLU L 198 REMARK 465 TRP L 199 REMARK 465 VAL L 200 REMARK 465 LEU L 201 REMARK 465 LEU L 202 REMARK 465 SER L 203 REMARK 465 THR L 204 REMARK 465 PHE L 205 REMARK 465 LEU L 206 REMARK 465 GLY L 207 REMARK 465 SER L 208 REMARK 465 GLY L 209 REMARK 465 LEU L 210 REMARK 465 ASN L 211 REMARK 465 ASP L 212 REMARK 465 ILE L 213 REMARK 465 PHE L 214 REMARK 465 GLU L 215 REMARK 465 ALA L 216 REMARK 465 GLN L 217 REMARK 465 LYS L 218 REMARK 465 ILE L 219 REMARK 465 GLU L 220 REMARK 465 TRP L 221 REMARK 465 HIS L 222 REMARK 465 GLU L 223 REMARK 465 GLY L 224 REMARK 465 HIS L 225 REMARK 465 HIS L 226 REMARK 465 HIS L 227 REMARK 465 HIS L 228 REMARK 465 HIS L 229 REMARK 465 HIS L 230 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 OH TYR L 119 OE1 GLU L 132 1.90 REMARK 500 OD2 ASP L 37 OG SER L 40 2.09 REMARK 500 O CYS K 139 OG SER K 146 2.10 REMARK 500 OG SER F 94 NH1 ARG F 96 2.10 REMARK 500 NH1 ARG G 311 OE2 GLU H 97 2.17 REMARK 500 OD2 ASP E 100G NH1 ARG E 100L 2.17 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 THR H 32 N - CA - CB ANGL. DEV. = 16.3 DEGREES REMARK 500 CYS H 137 CA - CB - SG ANGL. DEV. = 11.6 DEGREES REMARK 500 CYS L 137 CA - CB - SG ANGL. DEV. = 7.1 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 SER A 7 -178.37 -68.33 REMARK 500 TYR A 32 132.58 67.32 REMARK 500 TYR A 33 -179.67 -69.97 REMARK 500 ALA A 88 -174.99 -171.21 REMARK 500 ASN A 100A 11.75 -140.16 REMARK 500 TRP A 100B -5.04 67.78 REMARK 500 ASN A 100C 87.44 -163.23 REMARK 500 TYR A 102 67.80 60.10 REMARK 500 SER B 51 -7.86 77.52 REMARK 500 LEU C 51 76.68 -100.94 REMARK 500 ARG C 90 -169.34 -79.90 REMARK 500 PRO C 185 173.96 -57.55 REMARK 500 ASN C 224 -138.13 54.71 REMARK 500 ALA D 5 134.35 74.97 REMARK 500 LEU D 10 -6.27 82.11 REMARK 500 ALA D 35 147.47 -171.18 REMARK 500 ARG D 127 -131.00 66.55 REMARK 500 ASN D 155 34.43 71.32 REMARK 500 SER E 7 -177.64 -68.16 REMARK 500 TYR E 32 132.87 67.18 REMARK 500 SER E 84 -4.22 76.10 REMARK 500 TRP E 100B -3.91 59.22 REMARK 500 ASN E 100C 88.86 -162.47 REMARK 500 ASP E 100H 32.39 -140.66 REMARK 500 TYR E 102 68.09 60.02 REMARK 500 GLN E 105 -32.27 -130.52 REMARK 500 PRO F 44 175.56 -59.84 REMARK 500 SER F 51 -6.29 77.69 REMARK 500 SER F 52 12.55 -151.06 REMARK 500 ALA F 55 -167.53 -61.05 REMARK 500 ARG F 61 -8.83 -58.86 REMARK 500 PRO G 185 171.81 -55.29 REMARK 500 ASN G 224 -142.24 54.07 REMARK 500 ALA H 5 125.55 74.63 REMARK 500 LEU H 10 -2.37 81.59 REMARK 500 ASN H 12 171.47 179.80 REMARK 500 ARG H 127 -132.32 62.38 REMARK 500 SER I 7 -179.61 -65.88 REMARK 500 TYR I 32 126.36 66.89 REMARK 500 SER I 84 -4.90 74.91 REMARK 500 TRP I 100B -8.17 62.25 REMARK 500 ASN I 100C 88.40 -157.82 REMARK 500 ASP I 100H 26.36 -140.94 REMARK 500 SER J 51 -8.88 78.41 REMARK 500 LEU K 51 77.77 -100.34 REMARK 500 ASN K 92 37.61 71.91 REMARK 500 PRO K 185 174.09 -57.11 REMARK 500 ASN K 224 -137.69 55.00 REMARK 500 ALA L 5 126.78 76.14 REMARK 500 LEU L 10 -4.87 81.54 REMARK 500 REMARK 500 THIS ENTRY HAS 52 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 ASN D 82 TRP D 83 148.40 REMARK 500 ASN H 82 TRP H 83 147.66 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 ARG F 53 0.15 SIDE CHAIN REMARK 500 ARG F 54 0.09 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-44901 RELATED DB: EMDB REMARK 900 VACCINE ELICITED FAB C968.180 WITH INFLUENZA H10 JD13 HA TRIMER DBREF 9BU6 A 1 113 PDB 9BU6 9BU6 1 113 DBREF 9BU6 B 1 107 PDB 9BU6 9BU6 1 107 DBREF1 9BU6 C 9 330 UNP A0A059T4A1_9INFA DBREF2 9BU6 C A0A059T4A1 16 340 DBREF1 9BU6 D 1 177 UNP A0A0B4UV34_9INFA DBREF2 9BU6 D A0A0B4UV34 341 517 DBREF 9BU6 E 1 113 PDB 9BU6 9BU6 1 113 DBREF 9BU6 F 1 107 PDB 9BU6 9BU6 1 107 DBREF1 9BU6 G 9 330 UNP A0A059T4A1_9INFA DBREF2 9BU6 G A0A059T4A1 16 340 DBREF1 9BU6 H 1 177 UNP A0A0B4UV34_9INFA DBREF2 9BU6 H A0A0B4UV34 341 517 DBREF 9BU6 I 1 113 PDB 9BU6 9BU6 1 113 DBREF 9BU6 J 1 107 PDB 9BU6 9BU6 1 107 DBREF1 9BU6 K 9 330 UNP A0A059T4A1_9INFA DBREF2 9BU6 K A0A059T4A1 16 340 DBREF1 9BU6 L 1 177 UNP A0A0B4UV34_9INFA DBREF2 9BU6 L A0A0B4UV34 341 517 SEQADV 9BU6 GLY D 178 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 SER D 179 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 GLY D 180 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 TYR D 181 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 ILE D 182 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 PRO D 183 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 GLU D 184 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 ALA D 185 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 PRO D 186 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 ARG D 187 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 ASP D 188 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 GLY D 189 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 GLN D 190 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 ALA D 191 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 TYR D 192 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 VAL D 193 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 ARG D 194 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 LYS D 195 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 ASP D 196 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 GLY D 197 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 GLU D 198 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 TRP D 199 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 VAL D 200 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 LEU D 201 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 LEU D 202 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 SER D 203 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 THR D 204 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 PHE D 205 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 LEU D 206 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 GLY D 207 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 SER D 208 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 GLY D 209 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 LEU D 210 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 ASN D 211 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 ASP D 212 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 ILE D 213 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 PHE D 214 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 GLU D 215 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 ALA D 216 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 GLN D 217 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 LYS D 218 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 ILE D 219 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 GLU D 220 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 TRP D 221 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 HIS D 222 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 GLU D 223 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 GLY D 224 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 HIS D 225 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 HIS D 226 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 HIS D 227 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 HIS D 228 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 HIS D 229 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 HIS D 230 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 GLY H 178 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 SER H 179 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 GLY H 180 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 TYR H 181 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 ILE H 182 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 PRO H 183 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 GLU H 184 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 ALA H 185 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 PRO H 186 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 ARG H 187 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 ASP H 188 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 GLY H 189 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 GLN H 190 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 ALA H 191 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 TYR H 192 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 VAL H 193 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 ARG H 194 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 LYS H 195 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 ASP H 196 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 GLY H 197 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 GLU H 198 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 TRP H 199 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 VAL H 200 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 LEU H 201 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 LEU H 202 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 SER H 203 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 THR H 204 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 PHE H 205 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 LEU H 206 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 GLY H 207 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 SER H 208 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 GLY H 209 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 LEU H 210 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 ASN H 211 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 ASP H 212 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 ILE H 213 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 PHE H 214 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 GLU H 215 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 ALA H 216 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 GLN H 217 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 LYS H 218 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 ILE H 219 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 GLU H 220 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 TRP H 221 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 HIS H 222 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 GLU H 223 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 GLY H 224 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 HIS H 225 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 HIS H 226 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 HIS H 227 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 HIS H 228 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 HIS H 229 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 HIS H 230 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 GLY L 178 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 SER L 179 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 GLY L 180 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 TYR L 181 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 ILE L 182 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 PRO L 183 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 GLU L 184 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 ALA L 185 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 PRO L 186 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 ARG L 187 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 ASP L 188 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 GLY L 189 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 GLN L 190 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 ALA L 191 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 TYR L 192 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 VAL L 193 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 ARG L 194 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 LYS L 195 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 ASP L 196 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 GLY L 197 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 GLU L 198 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 TRP L 199 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 VAL L 200 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 LEU L 201 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 LEU L 202 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 SER L 203 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 THR L 204 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 PHE L 205 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 LEU L 206 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 GLY L 207 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 SER L 208 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 GLY L 209 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 LEU L 210 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 ASN L 211 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 ASP L 212 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 ILE L 213 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 PHE L 214 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 GLU L 215 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 ALA L 216 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 GLN L 217 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 LYS L 218 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 ILE L 219 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 GLU L 220 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 TRP L 221 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 HIS L 222 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 GLU L 223 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 GLY L 224 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 HIS L 225 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 HIS L 226 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 HIS L 227 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 HIS L 228 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 HIS L 229 UNP A0A0B4UV3 EXPRESSION TAG SEQADV 9BU6 HIS L 230 UNP A0A0B4UV3 EXPRESSION TAG SEQRES 1 A 131 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 A 131 PRO GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 A 131 TYR ILE PHE ILE ASP TYR TYR ILE HIS TRP VAL ARG GLN SEQRES 4 A 131 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY TRP ILE ASN SEQRES 5 A 131 PRO ASN ARG GLY GLY THR ASP TYR ALA GLN LYS PHE GLN SEQRES 6 A 131 GLY ARG VAL THR MET THR SER ASP THR SER ILE GLY THR SEQRES 7 A 131 ALA PHE LEU GLU LEU THR ARG LEU LYS SER ASP ASP THR SEQRES 8 A 131 ALA VAL TYR TYR CYS ALA ARG ASP ARG ILE TRP GLY GLY SEQRES 9 A 131 ASN TRP ASN PRO GLN LYS ASP ASP TYR GLY ASP ARG GLY SEQRES 10 A 131 GLY ASP TYR TRP GLY GLN GLY THR LEU VAL THR VAL SER SEQRES 11 A 131 SER SEQRES 1 B 108 GLU ILE VAL LEU THR GLN SER PRO GLY THR LEU SER LEU SEQRES 2 B 108 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 B 108 GLN SER PHE SER SER THR TYR LEU ALA TRP TYR GLN HIS SEQRES 4 B 108 LYS PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR GLY SER SEQRES 5 B 108 SER ARG ARG ALA THR GLY ILE PRO ASP ARG PHE SER GLY SEQRES 6 B 108 SER GLY SER GLY THR ASP PHE THR LEU THR ILE SER ARG SEQRES 7 B 108 LEU GLU PRO GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN SEQRES 8 B 108 PHE GLY SER SER PRO ARG THR PHE GLY GLN GLY THR LYS SEQRES 9 B 108 LEU GLU VAL LYS SEQRES 1 C 325 GLY LEU ASP LYS ILE CYS LEU GLY HIS HIS ALA VAL ALA SEQRES 2 C 325 ASN GLY THR ILE VAL LYS THR LEU THR ASN GLU GLN GLU SEQRES 3 C 325 GLU VAL THR ASN ALA THR GLU THR VAL GLU SER THR GLY SEQRES 4 C 325 ILE ASN ARG LEU CYS MET LYS GLY ARG LYS HIS LYS ASP SEQRES 5 C 325 LEU GLY ASN CYS HIS PRO ILE GLY MET LEU ILE GLY THR SEQRES 6 C 325 PRO ALA CYS ASP LEU HIS LEU THR GLY MET TRP ASP THR SEQRES 7 C 325 LEU ILE GLU ARG GLU ASN ALA ILE ALA TYR CYS TYR PRO SEQRES 8 C 325 GLY ALA THR VAL ASN VAL GLU ALA LEU ARG GLN LYS ILE SEQRES 9 C 325 MET GLU SER GLY GLY ILE ASN LYS ILE SER THR GLY PHE SEQRES 10 C 325 THR TYR GLY SER SER ILE ASN SER ALA GLY THR THR ARG SEQRES 11 C 325 ALA CYS MET ARG ASN GLY GLY ASN SER PHE TYR ALA GLU SEQRES 12 C 325 LEU LYS TRP LEU VAL SER LYS SER LYS GLY GLN ASN PHE SEQRES 13 C 325 PRO GLN THR THR ASN THR TYR ARG ASN THR ASP THR ALA SEQRES 14 C 325 GLU HIS LEU ILE MET TRP GLY ILE HIS HIS PRO SER SER SEQRES 15 C 325 THR GLN GLU LYS ASN ASP LEU TYR GLY THR GLN SER LEU SEQRES 16 C 325 SER ILE SER VAL GLY SER SER THR TYR ARG ASN ASN PHE SEQRES 17 C 325 VAL PRO VAL VAL GLY ALA ARG PRO GLN VAL ASN GLY GLN SEQRES 18 C 325 SER GLY ARG ILE ASP PHE HIS TRP THR LEU VAL GLN PRO SEQRES 19 C 325 GLY ASP ASN ILE THR PHE SER HIS ASN GLY GLY LEU ILE SEQRES 20 C 325 ALA PRO SER ARG VAL SER LYS LEU ILE GLY ARG GLY LEU SEQRES 21 C 325 GLY ILE GLN SER ASP ALA PRO ILE ASP ASN ASN CYS GLU SEQRES 22 C 325 SER LYS CYS PHE TRP ARG GLY GLY SER ILE ASN THR ARG SEQRES 23 C 325 LEU PRO PHE GLN ASN LEU SER PRO ARG THR VAL GLY GLN SEQRES 24 C 325 CYS PRO LYS TYR VAL ASN ARG ARG SER LEU MET LEU ALA SEQRES 25 C 325 THR GLY MET ARG ASN VAL PRO GLU LEU ILE GLN GLY ARG SEQRES 1 D 230 GLY LEU PHE GLY ALA ILE ALA GLY PHE LEU GLU ASN GLY SEQRES 2 D 230 TRP GLU GLY MET VAL ASP GLY TRP TYR GLY PHE ARG HIS SEQRES 3 D 230 GLN ASN ALA GLN GLY THR GLY GLN ALA ALA ASP TYR LYS SEQRES 4 D 230 SER THR GLN ALA ALA ILE ASP GLN ILE THR GLY LYS LEU SEQRES 5 D 230 ASN ARG LEU VAL GLU LYS THR ASN THR GLU PHE GLU SER SEQRES 6 D 230 ILE GLU SER GLU PHE SER GLU ILE GLU HIS GLN ILE GLY SEQRES 7 D 230 ASN VAL ILE ASN TRP THR LYS ASP SER ILE THR ASP ILE SEQRES 8 D 230 TRP THR TYR GLN ALA GLU LEU LEU VAL ALA MET GLU ASN SEQRES 9 D 230 GLN HIS THR ILE ASP MET ALA ASP SER GLU MET LEU ASN SEQRES 10 D 230 LEU TYR GLU ARG VAL ARG LYS GLN LEU ARG GLN ASN ALA SEQRES 11 D 230 GLU GLU ASP GLY LYS GLY CYS PHE GLU ILE TYR HIS ALA SEQRES 12 D 230 CYS ASP ASP SER CYS MET GLU SER ILE ARG ASN ASN THR SEQRES 13 D 230 TYR ASP HIS SER GLN TYR ARG GLU GLU ALA LEU LEU ASN SEQRES 14 D 230 ARG LEU ASN ILE ASN PRO VAL THR GLY SER GLY TYR ILE SEQRES 15 D 230 PRO GLU ALA PRO ARG ASP GLY GLN ALA TYR VAL ARG LYS SEQRES 16 D 230 ASP GLY GLU TRP VAL LEU LEU SER THR PHE LEU GLY SER SEQRES 17 D 230 GLY LEU ASN ASP ILE PHE GLU ALA GLN LYS ILE GLU TRP SEQRES 18 D 230 HIS GLU GLY HIS HIS HIS HIS HIS HIS SEQRES 1 E 131 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 E 131 PRO GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 E 131 TYR ILE PHE ILE ASP TYR TYR ILE HIS TRP VAL ARG GLN SEQRES 4 E 131 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY TRP ILE ASN SEQRES 5 E 131 PRO ASN ARG GLY GLY THR ASP TYR ALA GLN LYS PHE GLN SEQRES 6 E 131 GLY ARG VAL THR MET THR SER ASP THR SER ILE GLY THR SEQRES 7 E 131 ALA PHE LEU GLU LEU THR ARG LEU LYS SER ASP ASP THR SEQRES 8 E 131 ALA VAL TYR TYR CYS ALA ARG ASP ARG ILE TRP GLY GLY SEQRES 9 E 131 ASN TRP ASN PRO GLN LYS ASP ASP TYR GLY ASP ARG GLY SEQRES 10 E 131 GLY ASP TYR TRP GLY GLN GLY THR LEU VAL THR VAL SER SEQRES 11 E 131 SER SEQRES 1 F 108 GLU ILE VAL LEU THR GLN SER PRO GLY THR LEU SER LEU SEQRES 2 F 108 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 F 108 GLN SER PHE SER SER THR TYR LEU ALA TRP TYR GLN HIS SEQRES 4 F 108 LYS PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR GLY SER SEQRES 5 F 108 SER ARG ARG ALA THR GLY ILE PRO ASP ARG PHE SER GLY SEQRES 6 F 108 SER GLY SER GLY THR ASP PHE THR LEU THR ILE SER ARG SEQRES 7 F 108 LEU GLU PRO GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN SEQRES 8 F 108 PHE GLY SER SER PRO ARG THR PHE GLY GLN GLY THR LYS SEQRES 9 F 108 LEU GLU VAL LYS SEQRES 1 G 325 GLY LEU ASP LYS ILE CYS LEU GLY HIS HIS ALA VAL ALA SEQRES 2 G 325 ASN GLY THR ILE VAL LYS THR LEU THR ASN GLU GLN GLU SEQRES 3 G 325 GLU VAL THR ASN ALA THR GLU THR VAL GLU SER THR GLY SEQRES 4 G 325 ILE ASN ARG LEU CYS MET LYS GLY ARG LYS HIS LYS ASP SEQRES 5 G 325 LEU GLY ASN CYS HIS PRO ILE GLY MET LEU ILE GLY THR SEQRES 6 G 325 PRO ALA CYS ASP LEU HIS LEU THR GLY MET TRP ASP THR SEQRES 7 G 325 LEU ILE GLU ARG GLU ASN ALA ILE ALA TYR CYS TYR PRO SEQRES 8 G 325 GLY ALA THR VAL ASN VAL GLU ALA LEU ARG GLN LYS ILE SEQRES 9 G 325 MET GLU SER GLY GLY ILE ASN LYS ILE SER THR GLY PHE SEQRES 10 G 325 THR TYR GLY SER SER ILE ASN SER ALA GLY THR THR ARG SEQRES 11 G 325 ALA CYS MET ARG ASN GLY GLY ASN SER PHE TYR ALA GLU SEQRES 12 G 325 LEU LYS TRP LEU VAL SER LYS SER LYS GLY GLN ASN PHE SEQRES 13 G 325 PRO GLN THR THR ASN THR TYR ARG ASN THR ASP THR ALA SEQRES 14 G 325 GLU HIS LEU ILE MET TRP GLY ILE HIS HIS PRO SER SER SEQRES 15 G 325 THR GLN GLU LYS ASN ASP LEU TYR GLY THR GLN SER LEU SEQRES 16 G 325 SER ILE SER VAL GLY SER SER THR TYR ARG ASN ASN PHE SEQRES 17 G 325 VAL PRO VAL VAL GLY ALA ARG PRO GLN VAL ASN GLY GLN SEQRES 18 G 325 SER GLY ARG ILE ASP PHE HIS TRP THR LEU VAL GLN PRO SEQRES 19 G 325 GLY ASP ASN ILE THR PHE SER HIS ASN GLY GLY LEU ILE SEQRES 20 G 325 ALA PRO SER ARG VAL SER LYS LEU ILE GLY ARG GLY LEU SEQRES 21 G 325 GLY ILE GLN SER ASP ALA PRO ILE ASP ASN ASN CYS GLU SEQRES 22 G 325 SER LYS CYS PHE TRP ARG GLY GLY SER ILE ASN THR ARG SEQRES 23 G 325 LEU PRO PHE GLN ASN LEU SER PRO ARG THR VAL GLY GLN SEQRES 24 G 325 CYS PRO LYS TYR VAL ASN ARG ARG SER LEU MET LEU ALA SEQRES 25 G 325 THR GLY MET ARG ASN VAL PRO GLU LEU ILE GLN GLY ARG SEQRES 1 H 230 GLY LEU PHE GLY ALA ILE ALA GLY PHE LEU GLU ASN GLY SEQRES 2 H 230 TRP GLU GLY MET VAL ASP GLY TRP TYR GLY PHE ARG HIS SEQRES 3 H 230 GLN ASN ALA GLN GLY THR GLY GLN ALA ALA ASP TYR LYS SEQRES 4 H 230 SER THR GLN ALA ALA ILE ASP GLN ILE THR GLY LYS LEU SEQRES 5 H 230 ASN ARG LEU VAL GLU LYS THR ASN THR GLU PHE GLU SER SEQRES 6 H 230 ILE GLU SER GLU PHE SER GLU ILE GLU HIS GLN ILE GLY SEQRES 7 H 230 ASN VAL ILE ASN TRP THR LYS ASP SER ILE THR ASP ILE SEQRES 8 H 230 TRP THR TYR GLN ALA GLU LEU LEU VAL ALA MET GLU ASN SEQRES 9 H 230 GLN HIS THR ILE ASP MET ALA ASP SER GLU MET LEU ASN SEQRES 10 H 230 LEU TYR GLU ARG VAL ARG LYS GLN LEU ARG GLN ASN ALA SEQRES 11 H 230 GLU GLU ASP GLY LYS GLY CYS PHE GLU ILE TYR HIS ALA SEQRES 12 H 230 CYS ASP ASP SER CYS MET GLU SER ILE ARG ASN ASN THR SEQRES 13 H 230 TYR ASP HIS SER GLN TYR ARG GLU GLU ALA LEU LEU ASN SEQRES 14 H 230 ARG LEU ASN ILE ASN PRO VAL THR GLY SER GLY TYR ILE SEQRES 15 H 230 PRO GLU ALA PRO ARG ASP GLY GLN ALA TYR VAL ARG LYS SEQRES 16 H 230 ASP GLY GLU TRP VAL LEU LEU SER THR PHE LEU GLY SER SEQRES 17 H 230 GLY LEU ASN ASP ILE PHE GLU ALA GLN LYS ILE GLU TRP SEQRES 18 H 230 HIS GLU GLY HIS HIS HIS HIS HIS HIS SEQRES 1 I 131 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 I 131 PRO GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 I 131 TYR ILE PHE ILE ASP TYR TYR ILE HIS TRP VAL ARG GLN SEQRES 4 I 131 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY TRP ILE ASN SEQRES 5 I 131 PRO ASN ARG GLY GLY THR ASP TYR ALA GLN LYS PHE GLN SEQRES 6 I 131 GLY ARG VAL THR MET THR SER ASP THR SER ILE GLY THR SEQRES 7 I 131 ALA PHE LEU GLU LEU THR ARG LEU LYS SER ASP ASP THR SEQRES 8 I 131 ALA VAL TYR TYR CYS ALA ARG ASP ARG ILE TRP GLY GLY SEQRES 9 I 131 ASN TRP ASN PRO GLN LYS ASP ASP TYR GLY ASP ARG GLY SEQRES 10 I 131 GLY ASP TYR TRP GLY GLN GLY THR LEU VAL THR VAL SER SEQRES 11 I 131 SER SEQRES 1 J 108 GLU ILE VAL LEU THR GLN SER PRO GLY THR LEU SER LEU SEQRES 2 J 108 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 J 108 GLN SER PHE SER SER THR TYR LEU ALA TRP TYR GLN HIS SEQRES 4 J 108 LYS PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR GLY SER SEQRES 5 J 108 SER ARG ARG ALA THR GLY ILE PRO ASP ARG PHE SER GLY SEQRES 6 J 108 SER GLY SER GLY THR ASP PHE THR LEU THR ILE SER ARG SEQRES 7 J 108 LEU GLU PRO GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN SEQRES 8 J 108 PHE GLY SER SER PRO ARG THR PHE GLY GLN GLY THR LYS SEQRES 9 J 108 LEU GLU VAL LYS SEQRES 1 K 325 GLY LEU ASP LYS ILE CYS LEU GLY HIS HIS ALA VAL ALA SEQRES 2 K 325 ASN GLY THR ILE VAL LYS THR LEU THR ASN GLU GLN GLU SEQRES 3 K 325 GLU VAL THR ASN ALA THR GLU THR VAL GLU SER THR GLY SEQRES 4 K 325 ILE ASN ARG LEU CYS MET LYS GLY ARG LYS HIS LYS ASP SEQRES 5 K 325 LEU GLY ASN CYS HIS PRO ILE GLY MET LEU ILE GLY THR SEQRES 6 K 325 PRO ALA CYS ASP LEU HIS LEU THR GLY MET TRP ASP THR SEQRES 7 K 325 LEU ILE GLU ARG GLU ASN ALA ILE ALA TYR CYS TYR PRO SEQRES 8 K 325 GLY ALA THR VAL ASN VAL GLU ALA LEU ARG GLN LYS ILE SEQRES 9 K 325 MET GLU SER GLY GLY ILE ASN LYS ILE SER THR GLY PHE SEQRES 10 K 325 THR TYR GLY SER SER ILE ASN SER ALA GLY THR THR ARG SEQRES 11 K 325 ALA CYS MET ARG ASN GLY GLY ASN SER PHE TYR ALA GLU SEQRES 12 K 325 LEU LYS TRP LEU VAL SER LYS SER LYS GLY GLN ASN PHE SEQRES 13 K 325 PRO GLN THR THR ASN THR TYR ARG ASN THR ASP THR ALA SEQRES 14 K 325 GLU HIS LEU ILE MET TRP GLY ILE HIS HIS PRO SER SER SEQRES 15 K 325 THR GLN GLU LYS ASN ASP LEU TYR GLY THR GLN SER LEU SEQRES 16 K 325 SER ILE SER VAL GLY SER SER THR TYR ARG ASN ASN PHE SEQRES 17 K 325 VAL PRO VAL VAL GLY ALA ARG PRO GLN VAL ASN GLY GLN SEQRES 18 K 325 SER GLY ARG ILE ASP PHE HIS TRP THR LEU VAL GLN PRO SEQRES 19 K 325 GLY ASP ASN ILE THR PHE SER HIS ASN GLY GLY LEU ILE SEQRES 20 K 325 ALA PRO SER ARG VAL SER LYS LEU ILE GLY ARG GLY LEU SEQRES 21 K 325 GLY ILE GLN SER ASP ALA PRO ILE ASP ASN ASN CYS GLU SEQRES 22 K 325 SER LYS CYS PHE TRP ARG GLY GLY SER ILE ASN THR ARG SEQRES 23 K 325 LEU PRO PHE GLN ASN LEU SER PRO ARG THR VAL GLY GLN SEQRES 24 K 325 CYS PRO LYS TYR VAL ASN ARG ARG SER LEU MET LEU ALA SEQRES 25 K 325 THR GLY MET ARG ASN VAL PRO GLU LEU ILE GLN GLY ARG SEQRES 1 L 230 GLY LEU PHE GLY ALA ILE ALA GLY PHE LEU GLU ASN GLY SEQRES 2 L 230 TRP GLU GLY MET VAL ASP GLY TRP TYR GLY PHE ARG HIS SEQRES 3 L 230 GLN ASN ALA GLN GLY THR GLY GLN ALA ALA ASP TYR LYS SEQRES 4 L 230 SER THR GLN ALA ALA ILE ASP GLN ILE THR GLY LYS LEU SEQRES 5 L 230 ASN ARG LEU VAL GLU LYS THR ASN THR GLU PHE GLU SER SEQRES 6 L 230 ILE GLU SER GLU PHE SER GLU ILE GLU HIS GLN ILE GLY SEQRES 7 L 230 ASN VAL ILE ASN TRP THR LYS ASP SER ILE THR ASP ILE SEQRES 8 L 230 TRP THR TYR GLN ALA GLU LEU LEU VAL ALA MET GLU ASN SEQRES 9 L 230 GLN HIS THR ILE ASP MET ALA ASP SER GLU MET LEU ASN SEQRES 10 L 230 LEU TYR GLU ARG VAL ARG LYS GLN LEU ARG GLN ASN ALA SEQRES 11 L 230 GLU GLU ASP GLY LYS GLY CYS PHE GLU ILE TYR HIS ALA SEQRES 12 L 230 CYS ASP ASP SER CYS MET GLU SER ILE ARG ASN ASN THR SEQRES 13 L 230 TYR ASP HIS SER GLN TYR ARG GLU GLU ALA LEU LEU ASN SEQRES 14 L 230 ARG LEU ASN ILE ASN PRO VAL THR GLY SER GLY TYR ILE SEQRES 15 L 230 PRO GLU ALA PRO ARG ASP GLY GLN ALA TYR VAL ARG LYS SEQRES 16 L 230 ASP GLY GLU TRP VAL LEU LEU SER THR PHE LEU GLY SER SEQRES 17 L 230 GLY LEU ASN ASP ILE PHE GLU ALA GLN LYS ILE GLU TRP SEQRES 18 L 230 HIS GLU GLY HIS HIS HIS HIS HIS HIS 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 BMA O 3 11 HET NAG P 1 14 HET NAG P 2 14 HET NAG Q 1 14 HET NAG Q 2 14 HET NAG R 1 14 HET NAG R 2 14 HET BMA R 3 11 HET NAG S 1 14 HET NAG S 2 14 HET NAG T 1 14 HET NAG T 2 14 HET NAG U 1 14 HET NAG U 2 14 HET BMA U 3 11 HET NAG D 301 14 HET NAG H 301 14 HET NAG L 301 14 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BMA BETA-D-MANNOPYRANOSE 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 BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE FORMUL 13 NAG 21(C8 H15 N O6) FORMUL 15 BMA 3(C6 H12 O6) HELIX 1 AA1 GLN A 61 GLN A 64 5 4 HELIX 2 AA2 ASN A 100C ASP A 100G 5 5 HELIX 3 AA3 GLU B 79 PHE B 83 5 5 HELIX 4 AA4 HIS C 65 GLY C 72 1 8 HELIX 5 AA5 THR C 73 ASP C 77 5 5 HELIX 6 AA6 ASN C 104 SER C 115 1 12 HELIX 7 AA7 SER C 187 TYR C 195 1 9 HELIX 8 AA8 ASP D 37 GLY D 50 1 14 HELIX 9 AA9 LYS D 51 VAL D 56 5 6 HELIX 10 AB1 GLU D 74 ARG D 127 1 54 HELIX 11 AB2 ASP D 145 ASN D 155 1 11 HELIX 12 AB3 ASP D 158 GLN D 161 5 4 HELIX 13 AB4 TYR D 162 LEU D 171 1 10 HELIX 14 AB5 ASN E 100C ASP E 100G 5 5 HELIX 15 AB6 GLU F 79 PHE F 83 5 5 HELIX 16 AB7 HIS G 65 GLY G 72 1 8 HELIX 17 AB8 THR G 73 ASP G 77 5 5 HELIX 18 AB9 ASN G 104 SER G 115 1 12 HELIX 19 AC1 SER G 187 TYR G 195 1 9 HELIX 20 AC2 ASP H 37 THR H 49 1 13 HELIX 21 AC3 GLY H 50 LYS H 51 5 2 HELIX 22 AC4 LEU H 52 VAL H 56 5 5 HELIX 23 AC5 GLU H 74 ARG H 127 1 54 HELIX 24 AC6 ASP H 145 ASN H 155 1 11 HELIX 25 AC7 ASP H 158 GLN H 161 5 4 HELIX 26 AC8 TYR H 162 LEU H 171 1 10 HELIX 27 AC9 ASN I 100C ASP I 100G 5 5 HELIX 28 AD1 GLU J 79 PHE J 83 5 5 HELIX 29 AD2 HIS K 65 LEU K 70 1 6 HELIX 30 AD3 THR K 73 ASP K 77 5 5 HELIX 31 AD4 ASN K 104 SER K 115 1 12 HELIX 32 AD5 SER K 187 TYR K 195 1 9 HELIX 33 AD6 LYS L 39 GLY L 50 1 12 HELIX 34 AD7 LYS L 51 VAL L 56 5 6 HELIX 35 AD8 GLU L 74 ARG L 127 1 54 HELIX 36 AD9 ASP L 145 ASN L 155 1 11 HELIX 37 AE1 ASP L 158 GLN L 161 5 4 HELIX 38 AE2 TYR L 162 LEU L 171 1 10 SHEET 1 AA1 4 GLN A 3 GLN A 6 0 SHEET 2 AA1 4 VAL A 18 SER A 25 -1 O LYS A 23 N VAL A 5 SHEET 3 AA1 4 THR A 77 LEU A 82 -1 O LEU A 82 N VAL A 18 SHEET 4 AA1 4 VAL A 67 ASP A 72 -1 N THR A 68 O GLU A 81 SHEET 1 AA2 6 GLU A 10 VAL A 11 0 SHEET 2 AA2 6 THR A 107 THR A 110 1 O LEU A 108 N GLU A 10 SHEET 3 AA2 6 ALA A 88 TYR A 90 -1 N TYR A 90 O THR A 107 SHEET 4 AA2 6 ILE A 34 GLN A 39 -1 N GLN A 39 O VAL A 89 SHEET 5 AA2 6 GLU A 46 ILE A 51 -1 O MET A 48 N TRP A 36 SHEET 6 AA2 6 THR A 57 TYR A 59 -1 O ASP A 58 N TRP A 50 SHEET 1 AA3 4 LEU B 4 GLN B 6 0 SHEET 2 AA3 4 ALA B 19 ALA B 25 -1 O ARG B 24 N THR B 5 SHEET 3 AA3 4 ASP B 70 ILE B 75 -1 O PHE B 71 N CYS B 23 SHEET 4 AA3 4 PHE B 62 SER B 67 -1 N SER B 63 O THR B 74 SHEET 1 AA4 4 ARG B 53 ARG B 54 0 SHEET 2 AA4 4 ARG B 45 TYR B 49 -1 N TYR B 49 O ARG B 53 SHEET 3 AA4 4 ALA B 34 HIS B 38 -1 N TRP B 35 O LEU B 47 SHEET 4 AA4 4 VAL B 85 GLN B 89 -1 O VAL B 85 N HIS B 38 SHEET 1 AA5 5 GLY D 33 ALA D 36 0 SHEET 2 AA5 5 TYR D 22 GLN D 27 -1 N PHE D 24 O ALA D 35 SHEET 3 AA5 5 LYS C 12 HIS C 17 -1 N CYS C 14 O ARG D 25 SHEET 4 AA5 5 CYS D 137 ILE D 140 -1 O PHE D 138 N ILE C 13 SHEET 5 AA5 5 ALA D 130 GLU D 132 -1 N GLU D 131 O GLU D 139 SHEET 1 AA6 2 THR C 24 VAL C 26 0 SHEET 2 AA6 2 GLU C 34 VAL C 36 -1 O GLU C 34 N VAL C 26 SHEET 1 AA7 2 ALA C 39 GLU C 41 0 SHEET 2 AA7 2 MET C 315 ALA C 317 -1 O LEU C 316 N THR C 40 SHEET 1 AA8 3 VAL C 43 GLU C 44 0 SHEET 2 AA8 3 PHE C 294 GLN C 295 1 O PHE C 294 N GLU C 44 SHEET 3 AA8 3 LYS C 307 TYR C 308 1 O LYS C 307 N GLN C 295 SHEET 1 AA9 2 LEU C 51 CYS C 52 0 SHEET 2 AA9 2 ILE C 274 ASP C 275 1 O ASP C 275 N LEU C 51 SHEET 1 AB1 3 HIS C 58 ASP C 60 0 SHEET 2 AB1 3 THR C 86 GLU C 89 1 O ILE C 88 N LYS C 59 SHEET 3 AB1 3 LEU C 266 GLN C 269 1 O ILE C 268 N LEU C 87 SHEET 1 AB2 3 GLY C 82 MET C 83 0 SHEET 2 AB2 3 GLY C 117 SER C 122 -1 O ILE C 118 N GLY C 82 SHEET 3 AB2 3 ARG C 256 LEU C 260 -1 O LYS C 259 N ASN C 119 SHEET 1 AB3 5 GLY C 100 THR C 102 0 SHEET 2 AB3 5 ARG C 229 VAL C 237 1 O PHE C 232 N ALA C 101 SHEET 3 AB3 5 HIS C 176 HIS C 184 -1 N HIS C 176 O VAL C 237 SHEET 4 AB3 5 LEU C 251 PRO C 254 -1 O ILE C 252 N GLY C 181 SHEET 5 AB3 5 LEU C 151 TRP C 153 -1 N LYS C 152 O ALA C 253 SHEET 1 AB4 2 ILE C 130 ASN C 131 0 SHEET 2 AB4 2 VAL C 155 SER C 156 -1 O VAL C 155 N ASN C 131 SHEET 1 AB5 2 THR C 136 ARG C 141 0 SHEET 2 AB5 2 GLY C 144 SER C 146 -1 O GLY C 144 N ARG C 141 SHEET 1 AB6 4 THR C 164 ARG C 169 0 SHEET 2 AB6 4 ASN C 242 HIS C 247 -1 O PHE C 245 N ASN C 166 SHEET 3 AB6 4 ILE C 202 SER C 206 -1 N SER C 203 O SER C 246 SHEET 4 AB6 4 ARG C 210 PHE C 213 -1 O ASN C 211 N VAL C 204 SHEET 1 AB7 3 GLY C 286 ILE C 288 0 SHEET 2 AB7 3 CYS C 281 TRP C 283 -1 N TRP C 283 O GLY C 286 SHEET 3 AB7 3 THR C 301 GLY C 303 -1 O VAL C 302 N PHE C 282 SHEET 1 AB8 4 VAL E 5 GLN E 6 0 SHEET 2 AB8 4 VAL E 20 LYS E 23 -1 O LYS E 23 N VAL E 5 SHEET 3 AB8 4 THR E 77 LEU E 80 -1 O ALA E 78 N CYS E 22 SHEET 4 AB8 4 MET E 69 ASP E 72 -1 N THR E 70 O PHE E 79 SHEET 1 AB9 6 GLU E 10 VAL E 11 0 SHEET 2 AB9 6 THR E 107 THR E 110 1 O LEU E 108 N GLU E 10 SHEET 3 AB9 6 ALA E 88 TYR E 90 -1 N ALA E 88 O VAL E 109 SHEET 4 AB9 6 ILE E 34 GLN E 39 -1 N GLN E 39 O VAL E 89 SHEET 5 AB9 6 GLU E 46 ILE E 51 -1 O MET E 48 N TRP E 36 SHEET 6 AB9 6 THR E 57 TYR E 59 -1 O ASP E 58 N TRP E 50 SHEET 1 AC1 5 GLU E 10 VAL E 11 0 SHEET 2 AC1 5 THR E 107 THR E 110 1 O LEU E 108 N GLU E 10 SHEET 3 AC1 5 ALA E 88 TYR E 90 -1 N ALA E 88 O VAL E 109 SHEET 4 AC1 5 ILE E 34 GLN E 39 -1 N GLN E 39 O VAL E 89 SHEET 5 AC1 5 ALA E 93 ARG E 94 -1 O ALA E 93 N HIS E 35 SHEET 1 AC2 4 LEU F 4 GLN F 6 0 SHEET 2 AC2 4 ALA F 19 ALA F 25 -1 O ARG F 24 N THR F 5 SHEET 3 AC2 4 ASP F 70 ILE F 75 -1 O PHE F 71 N CYS F 23 SHEET 4 AC2 4 PHE F 62 SER F 67 -1 N SER F 63 O THR F 74 SHEET 1 AC3 4 ARG F 53 ARG F 54 0 SHEET 2 AC3 4 ARG F 45 TYR F 49 -1 N TYR F 49 O ARG F 53 SHEET 3 AC3 4 ALA F 34 HIS F 38 -1 N TRP F 35 O LEU F 47 SHEET 4 AC3 4 VAL F 85 GLN F 89 -1 O VAL F 85 N HIS F 38 SHEET 1 AC4 5 THR H 32 ALA H 36 0 SHEET 2 AC4 5 TYR H 22 GLN H 27 -1 N PHE H 24 O ALA H 35 SHEET 3 AC4 5 LYS G 12 HIS G 17 -1 N CYS G 14 O ARG H 25 SHEET 4 AC4 5 CYS H 137 ILE H 140 -1 O PHE H 138 N ILE G 13 SHEET 5 AC4 5 ALA H 130 GLU H 132 -1 N GLU H 131 O GLU H 139 SHEET 1 AC5 2 THR G 24 VAL G 26 0 SHEET 2 AC5 2 GLU G 34 VAL G 36 -1 O GLU G 34 N VAL G 26 SHEET 1 AC6 2 ALA G 39 THR G 40 0 SHEET 2 AC6 2 LEU G 316 ALA G 317 -1 O LEU G 316 N THR G 40 SHEET 1 AC7 3 VAL G 43 GLU G 44 0 SHEET 2 AC7 3 PHE G 294 GLN G 295 1 O PHE G 294 N GLU G 44 SHEET 3 AC7 3 LYS G 307 TYR G 308 1 O LYS G 307 N GLN G 295 SHEET 1 AC8 2 LEU G 51 CYS G 52 0 SHEET 2 AC8 2 ILE G 274 ASP G 275 1 O ASP G 275 N LEU G 51 SHEET 1 AC9 3 HIS G 58 ASP G 60 0 SHEET 2 AC9 3 THR G 86 GLU G 89 1 O ILE G 88 N LYS G 59 SHEET 3 AC9 3 LEU G 266 GLN G 269 1 O ILE G 268 N LEU G 87 SHEET 1 AD1 3 GLY G 82 MET G 83 0 SHEET 2 AD1 3 GLY G 117 SER G 122 -1 O ILE G 118 N GLY G 82 SHEET 3 AD1 3 ARG G 256 LEU G 260 -1 O LYS G 259 N ASN G 119 SHEET 1 AD2 5 GLY G 100 THR G 102 0 SHEET 2 AD2 5 ARG G 229 VAL G 237 1 O PHE G 232 N ALA G 101 SHEET 3 AD2 5 HIS G 176 HIS G 184 -1 N HIS G 176 O VAL G 237 SHEET 4 AD2 5 LEU G 251 PRO G 254 -1 O ILE G 252 N GLY G 181 SHEET 5 AD2 5 LEU G 151 TRP G 153 -1 N LYS G 152 O ALA G 253 SHEET 1 AD3 2 ILE G 130 ASN G 131 0 SHEET 2 AD3 2 VAL G 155 SER G 156 -1 O VAL G 155 N ASN G 131 SHEET 1 AD4 2 THR G 136 ARG G 141 0 SHEET 2 AD4 2 GLY G 144 SER G 146 -1 O GLY G 144 N ARG G 141 SHEET 1 AD5 4 THR G 164 ARG G 169 0 SHEET 2 AD5 4 ASN G 242 HIS G 247 -1 O PHE G 245 N ASN G 166 SHEET 3 AD5 4 ILE G 202 SER G 206 -1 N GLY G 205 O THR G 244 SHEET 4 AD5 4 ARG G 210 PHE G 213 -1 O ASN G 211 N VAL G 204 SHEET 1 AD6 3 GLY G 286 ILE G 288 0 SHEET 2 AD6 3 CYS G 281 TRP G 283 -1 N TRP G 283 O GLY G 286 SHEET 3 AD6 3 THR G 301 GLY G 303 -1 O VAL G 302 N PHE G 282 SHEET 1 AD7 4 VAL I 5 GLN I 6 0 SHEET 2 AD7 4 VAL I 18 LYS I 23 -1 O LYS I 23 N VAL I 5 SHEET 3 AD7 4 THR I 77 LEU I 82 -1 O ALA I 78 N CYS I 22 SHEET 4 AD7 4 MET I 69 ASP I 72 -1 N THR I 70 O PHE I 79 SHEET 1 AD8 6 GLU I 10 VAL I 11 0 SHEET 2 AD8 6 THR I 107 THR I 110 1 O THR I 110 N GLU I 10 SHEET 3 AD8 6 ALA I 88 TYR I 90 -1 N TYR I 90 O THR I 107 SHEET 4 AD8 6 ILE I 34 GLN I 39 -1 N GLN I 39 O VAL I 89 SHEET 5 AD8 6 GLU I 46 ILE I 51 -1 O MET I 48 N TRP I 36 SHEET 6 AD8 6 THR I 57 TYR I 59 -1 O ASP I 58 N TRP I 50 SHEET 1 AD9 4 LEU J 4 GLN J 6 0 SHEET 2 AD9 4 ALA J 19 ALA J 25 -1 O ARG J 24 N THR J 5 SHEET 3 AD9 4 ASP J 70 ILE J 75 -1 O PHE J 71 N CYS J 23 SHEET 4 AD9 4 PHE J 62 SER J 67 -1 N SER J 63 O THR J 74 SHEET 1 AE1 4 ARG J 53 ARG J 54 0 SHEET 2 AE1 4 ARG J 45 TYR J 49 -1 N TYR J 49 O ARG J 53 SHEET 3 AE1 4 ALA J 34 HIS J 38 -1 N TRP J 35 O LEU J 47 SHEET 4 AE1 4 VAL J 85 GLN J 89 -1 O VAL J 85 N HIS J 38 SHEET 1 AE2 5 THR L 32 ALA L 36 0 SHEET 2 AE2 5 TYR L 22 GLN L 27 -1 N PHE L 24 O ALA L 35 SHEET 3 AE2 5 LYS K 12 HIS K 17 -1 N CYS K 14 O ARG L 25 SHEET 4 AE2 5 CYS L 137 ILE L 140 -1 O PHE L 138 N ILE K 13 SHEET 5 AE2 5 ALA L 130 GLU L 132 -1 N GLU L 131 O GLU L 139 SHEET 1 AE3 2 THR K 24 VAL K 26 0 SHEET 2 AE3 2 GLU K 34 VAL K 36 -1 O GLU K 34 N VAL K 26 SHEET 1 AE4 2 ALA K 39 THR K 40 0 SHEET 2 AE4 2 LEU K 316 ALA K 317 -1 O LEU K 316 N THR K 40 SHEET 1 AE5 3 VAL K 43 GLU K 44 0 SHEET 2 AE5 3 PHE K 294 GLN K 295 1 O PHE K 294 N GLU K 44 SHEET 3 AE5 3 LYS K 307 TYR K 308 1 O LYS K 307 N GLN K 295 SHEET 1 AE6 2 LEU K 51 CYS K 52 0 SHEET 2 AE6 2 ILE K 274 ASP K 275 1 O ASP K 275 N LEU K 51 SHEET 1 AE7 3 HIS K 58 ASP K 60 0 SHEET 2 AE7 3 THR K 86 GLU K 89 1 O ILE K 88 N LYS K 59 SHEET 3 AE7 3 LEU K 266 GLN K 269 1 O ILE K 268 N LEU K 87 SHEET 1 AE8 3 GLY K 82 MET K 83 0 SHEET 2 AE8 3 GLY K 117 SER K 122 -1 O ILE K 118 N GLY K 82 SHEET 3 AE8 3 ARG K 256 LEU K 260 -1 O VAL K 257 N ILE K 121 SHEET 1 AE9 5 GLY K 100 THR K 102 0 SHEET 2 AE9 5 ARG K 229 VAL K 237 1 O PHE K 232 N ALA K 101 SHEET 3 AE9 5 HIS K 176 HIS K 184 -1 N HIS K 176 O VAL K 237 SHEET 4 AE9 5 LEU K 251 PRO K 254 -1 O ILE K 252 N GLY K 181 SHEET 5 AE9 5 LEU K 151 TRP K 153 -1 N LYS K 152 O ALA K 253 SHEET 1 AF1 2 ILE K 130 ASN K 131 0 SHEET 2 AF1 2 VAL K 155 SER K 156 -1 O VAL K 155 N ASN K 131 SHEET 1 AF2 2 THR K 136 ARG K 141 0 SHEET 2 AF2 2 GLY K 144 SER K 146 -1 O SER K 146 N THR K 136 SHEET 1 AF3 4 THR K 164 ARG K 169 0 SHEET 2 AF3 4 ASN K 242 HIS K 247 -1 O PHE K 245 N ASN K 166 SHEET 3 AF3 4 ILE K 202 SER K 206 -1 N SER K 203 O SER K 246 SHEET 4 AF3 4 ARG K 210 PHE K 213 -1 O ASN K 211 N VAL K 204 SHEET 1 AF4 3 GLY K 286 ILE K 288 0 SHEET 2 AF4 3 CYS K 281 TRP K 283 -1 N TRP K 283 O GLY K 286 SHEET 3 AF4 3 VAL K 302 GLY K 303 -1 O VAL K 302 N PHE K 282 SSBOND 1 CYS A 22 CYS A 92 1555 1555 2.03 SSBOND 2 CYS B 23 CYS B 88 1555 1555 2.04 SSBOND 3 CYS C 14 CYS D 137 1555 1555 2.03 SSBOND 4 CYS C 52 CYS C 277 1555 1555 2.03 SSBOND 5 CYS C 64 CYS C 76 1555 1555 2.03 SSBOND 6 CYS C 97 CYS C 139 1555 1555 2.03 SSBOND 7 CYS C 281 CYS C 305 1555 1555 2.03 SSBOND 8 CYS D 144 CYS D 148 1555 1555 2.03 SSBOND 9 CYS E 22 CYS E 92 1555 1555 2.03 SSBOND 10 CYS F 23 CYS F 88 1555 1555 2.04 SSBOND 11 CYS G 14 CYS H 137 1555 1555 2.04 SSBOND 12 CYS G 52 CYS G 277 1555 1555 2.03 SSBOND 13 CYS G 64 CYS G 76 1555 1555 2.04 SSBOND 14 CYS G 97 CYS G 139 1555 1555 2.03 SSBOND 15 CYS G 281 CYS G 305 1555 1555 2.03 SSBOND 16 CYS H 144 CYS H 148 1555 1555 2.03 SSBOND 17 CYS I 22 CYS I 92 1555 1555 2.03 SSBOND 18 CYS J 23 CYS J 88 1555 1555 2.04 SSBOND 19 CYS K 14 CYS L 137 1555 1555 2.04 SSBOND 20 CYS K 52 CYS K 277 1555 1555 2.03 SSBOND 21 CYS K 64 CYS K 76 1555 1555 2.03 SSBOND 22 CYS K 97 CYS K 139 1555 1555 2.03 SSBOND 23 CYS K 281 CYS K 305 1555 1555 2.03 SSBOND 24 CYS L 144 CYS L 148 1555 1555 2.03 LINK ND2 ASN C 38 C1 NAG M 1 1555 1555 1.44 LINK ND2 ASN C 242 C1 NAG N 1 1555 1555 1.44 LINK ND2 ASN D 82 C1 NAG O 1 1555 1555 1.45 LINK ND2 ASN D 154 C1 NAG D 301 1555 1555 1.44 LINK ND2 ASN G 38 C1 NAG P 1 1555 1555 1.44 LINK ND2 ASN G 242 C1 NAG Q 1 1555 1555 1.44 LINK ND2 ASN H 82 C1 NAG R 1 1555 1555 1.46 LINK ND2 ASN H 154 C1 NAG H 301 1555 1555 1.44 LINK ND2 ASN K 38 C1 NAG S 1 1555 1555 1.44 LINK ND2 ASN K 242 C1 NAG T 1 1555 1555 1.44 LINK ND2 ASN L 82 C1 NAG U 1 1555 1555 1.44 LINK ND2 ASN L 154 C1 NAG L 301 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 1.45 LINK O4 NAG O 1 C1 NAG O 2 1555 1555 1.45 LINK O4 NAG O 2 C1 BMA O 3 1555 1555 1.45 LINK O4 NAG P 1 C1 NAG P 2 1555 1555 1.45 LINK O4 NAG Q 1 C1 NAG Q 2 1555 1555 1.45 LINK O4 NAG R 1 C1 NAG R 2 1555 1555 1.45 LINK O4 NAG R 2 C1 BMA R 3 1555 1555 1.45 LINK O4 NAG S 1 C1 NAG S 2 1555 1555 1.45 LINK O4 NAG T 1 C1 NAG T 2 1555 1555 1.45 LINK O4 NAG U 1 C1 NAG U 2 1555 1555 1.45 LINK O4 NAG U 2 C1 BMA U 3 1555 1555 1.45 CISPEP 1 SER B 94 PRO B 95 0 0.78 CISPEP 2 SER F 94 PRO F 95 0 1.31 CISPEP 3 SER J 94 PRO J 95 0 0.92 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