HEADER IMMUNE SYSTEM 25-NOV-24 9EI9 TITLE CRYO-EM STRUCTURE OF 5E10 FAB IN COMPLEX WITH H3 INFLUENZA VICTORIA TITLE 2 2011 HA TRIMER COMPND MOL_ID: 1; COMPND 2 MOLECULE: HEMAGGLUTININ HA1; COMPND 3 CHAIN: B, C, G; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: HEMAGGLUTININ HA2; COMPND 7 CHAIN: E, F, I; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: 5E10 FAB HEAVY CHAIN; COMPND 11 CHAIN: A, H; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 4; COMPND 14 MOLECULE: 5E10 FAB LIGHT CHAIN; COMPND 15 CHAIN: D, J; COMPND 16 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS; SOURCE 3 ORGANISM_COMMON: A/VICTORIA/361/2011(H3N2); SOURCE 4 ORGANISM_TAXID: 1268360; SOURCE 5 GENE: HA; SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 7 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS; SOURCE 11 ORGANISM_COMMON: A/VICTORIA/361/2011(H3N2); SOURCE 12 ORGANISM_TAXID: 1268360; SOURCE 13 GENE: HA; SOURCE 14 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 15 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 16 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 17 MOL_ID: 3; SOURCE 18 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 19 ORGANISM_COMMON: MOUSE; SOURCE 20 ORGANISM_TAXID: 10090; SOURCE 21 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 22 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 23 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 24 MOL_ID: 4; SOURCE 25 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 26 ORGANISM_COMMON: MOUSE; SOURCE 27 ORGANISM_TAXID: 10090; SOURCE 28 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 29 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 30 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS HA, INFLUENZA, FLU, N-TERM, H3, IMMUNE SYSTEM EXPDTA ELECTRON MICROSCOPY AUTHOR J.GORMAN,P.D.KWONG REVDAT 1 16-JUL-25 9EI9 0 JRNL AUTH J.GORMAN,P.D.KWONG JRNL TITL THE N TERMINUS OF H3-INFLUENZA HEMAGGLUTININ AS A JRNL TITL 2 SITE-OF-VULNERABILITY TO NEUTRALIZING ANTIBODY JRNL REF STRUCTURE 2025 JRNL REFN ISSN 0969-2126 REMARK 2 REMARK 2 RESOLUTION. 3.89 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : LEGINON, CRYOSPARC, CRYOSPARC, REMARK 3 CRYOSPARC, 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) : 3.890 REMARK 3 NUMBER OF PARTICLES : 28277 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 9EI9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-NOV-24. REMARK 100 THE DEPOSITION ID IS D_1000290527. 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 : 5E10 FAB IN COMPLEX WITH H3 REMARK 245 INFLUENZA VICTORIA 2011 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 : NULL REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : TFS KRIOS REMARK 245 DETECTOR TYPE : GATAN K2 SUMMIT (4K 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) : 7051.00 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: DECAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C, E, F, G, I, A, D, H, J, REMARK 350 AND CHAINS: K, L, M, N, O, P, Q REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 GLN B 1 REMARK 465 LYS B 2 REMARK 465 ARG B 329 REMARK 465 ARG B 330 REMARK 465 ARG B 331 REMARK 465 ARG B 332 REMARK 465 ARG B 333 REMARK 465 ARG B 334 REMARK 465 GLN C 1 REMARK 465 LYS C 2 REMARK 465 LEU C 3 REMARK 465 PRO C 4 REMARK 465 ARG C 329 REMARK 465 ARG C 330 REMARK 465 ARG C 331 REMARK 465 ARG C 332 REMARK 465 ARG C 333 REMARK 465 ARG C 334 REMARK 465 ILE E 173 REMARK 465 LYS E 174 REMARK 465 GLY E 175 REMARK 465 VAL E 176 REMARK 465 SER E 177 REMARK 465 GLY E 178 REMARK 465 ARG E 179 REMARK 465 LEU E 180 REMARK 465 VAL E 181 REMARK 465 PRO E 182 REMARK 465 ARG E 183 REMARK 465 GLY E 184 REMARK 465 SER E 185 REMARK 465 PRO E 186 REMARK 465 GLY E 187 REMARK 465 SER E 188 REMARK 465 GLY E 189 REMARK 465 TYR E 190 REMARK 465 ILE E 191 REMARK 465 PRO E 192 REMARK 465 GLU E 193 REMARK 465 ALA E 194 REMARK 465 PRO E 195 REMARK 465 ARG E 196 REMARK 465 ASP E 197 REMARK 465 GLY E 198 REMARK 465 GLN E 199 REMARK 465 ALA E 200 REMARK 465 TYR E 201 REMARK 465 VAL E 202 REMARK 465 ARG E 203 REMARK 465 LYS E 204 REMARK 465 ASP E 205 REMARK 465 GLY E 206 REMARK 465 GLU E 207 REMARK 465 TRP E 208 REMARK 465 VAL E 209 REMARK 465 LEU E 210 REMARK 465 LEU E 211 REMARK 465 SER E 212 REMARK 465 THR E 213 REMARK 465 PHE E 214 REMARK 465 LEU E 215 REMARK 465 GLY E 216 REMARK 465 HIS E 217 REMARK 465 HIS E 218 REMARK 465 HIS E 219 REMARK 465 HIS E 220 REMARK 465 HIS E 221 REMARK 465 HIS E 222 REMARK 465 ILE F 173 REMARK 465 LYS F 174 REMARK 465 GLY F 175 REMARK 465 VAL F 176 REMARK 465 SER F 177 REMARK 465 GLY F 178 REMARK 465 ARG F 179 REMARK 465 LEU F 180 REMARK 465 VAL F 181 REMARK 465 PRO F 182 REMARK 465 ARG F 183 REMARK 465 GLY F 184 REMARK 465 SER F 185 REMARK 465 PRO F 186 REMARK 465 GLY F 187 REMARK 465 SER F 188 REMARK 465 GLY F 189 REMARK 465 TYR F 190 REMARK 465 ILE F 191 REMARK 465 PRO F 192 REMARK 465 GLU F 193 REMARK 465 ALA F 194 REMARK 465 PRO F 195 REMARK 465 ARG F 196 REMARK 465 ASP F 197 REMARK 465 GLY F 198 REMARK 465 GLN F 199 REMARK 465 ALA F 200 REMARK 465 TYR F 201 REMARK 465 VAL F 202 REMARK 465 ARG F 203 REMARK 465 LYS F 204 REMARK 465 ASP F 205 REMARK 465 GLY F 206 REMARK 465 GLU F 207 REMARK 465 TRP F 208 REMARK 465 VAL F 209 REMARK 465 LEU F 210 REMARK 465 LEU F 211 REMARK 465 SER F 212 REMARK 465 THR F 213 REMARK 465 PHE F 214 REMARK 465 LEU F 215 REMARK 465 GLY F 216 REMARK 465 HIS F 217 REMARK 465 HIS F 218 REMARK 465 HIS F 219 REMARK 465 HIS F 220 REMARK 465 HIS F 221 REMARK 465 HIS F 222 REMARK 465 GLN G 1 REMARK 465 LYS G 2 REMARK 465 LEU G 3 REMARK 465 PRO G 4 REMARK 465 ARG G 330 REMARK 465 ARG G 331 REMARK 465 ARG G 332 REMARK 465 ARG G 333 REMARK 465 ARG G 334 REMARK 465 GLY I 1 REMARK 465 ILE I 2 REMARK 465 ILE I 173 REMARK 465 LYS I 174 REMARK 465 GLY I 175 REMARK 465 VAL I 176 REMARK 465 SER I 177 REMARK 465 GLY I 178 REMARK 465 ARG I 179 REMARK 465 LEU I 180 REMARK 465 VAL I 181 REMARK 465 PRO I 182 REMARK 465 ARG I 183 REMARK 465 GLY I 184 REMARK 465 SER I 185 REMARK 465 PRO I 186 REMARK 465 GLY I 187 REMARK 465 SER I 188 REMARK 465 GLY I 189 REMARK 465 TYR I 190 REMARK 465 ILE I 191 REMARK 465 PRO I 192 REMARK 465 GLU I 193 REMARK 465 ALA I 194 REMARK 465 PRO I 195 REMARK 465 ARG I 196 REMARK 465 ASP I 197 REMARK 465 GLY I 198 REMARK 465 GLN I 199 REMARK 465 ALA I 200 REMARK 465 TYR I 201 REMARK 465 VAL I 202 REMARK 465 ARG I 203 REMARK 465 LYS I 204 REMARK 465 ASP I 205 REMARK 465 GLY I 206 REMARK 465 GLU I 207 REMARK 465 TRP I 208 REMARK 465 VAL I 209 REMARK 465 LEU I 210 REMARK 465 LEU I 211 REMARK 465 SER I 212 REMARK 465 THR I 213 REMARK 465 PHE I 214 REMARK 465 LEU I 215 REMARK 465 GLY I 216 REMARK 465 HIS I 217 REMARK 465 HIS I 218 REMARK 465 HIS I 219 REMARK 465 HIS I 220 REMARK 465 HIS I 221 REMARK 465 HIS I 222 REMARK 465 SER A 113 REMARK 465 ALA A 114 REMARK 465 GLN D 108 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 GLN A 1 CG CD OE1 NE2 REMARK 470 VAL A 2 CG1 CG2 REMARK 470 THR A 3 OG1 CG2 REMARK 470 LEU A 4 CG CD1 CD2 REMARK 470 LYS A 5 CG CD CE NZ REMARK 470 GLU A 6 CG CD OE1 OE2 REMARK 470 SER A 7 OG REMARK 470 PRO A 9 CG CD REMARK 470 ILE A 11 CG1 CG2 CD1 REMARK 470 LEU A 12 CG CD1 CD2 REMARK 470 GLN A 13 CG CD OE1 NE2 REMARK 470 PRO A 14 CG CD REMARK 470 SER A 15 OG REMARK 470 GLN A 16 CG CD OE1 NE2 REMARK 470 THR A 17 OG1 CG2 REMARK 470 LEU A 18 CG CD1 CD2 REMARK 470 SER A 19 OG REMARK 470 LEU A 20 CG CD1 CD2 REMARK 470 THR A 21 OG1 CG2 REMARK 470 CYS A 22 SG REMARK 470 SER A 23 OG REMARK 470 PHE A 24 CG CD1 CD2 CE1 CE2 CZ REMARK 470 SER A 25 OG REMARK 470 PHE A 27 CG CD1 CD2 CE1 CE2 CZ REMARK 470 SER A 28 OG REMARK 470 LEU A 29 CG CD1 CD2 REMARK 470 SER A 30 OG REMARK 470 THR A 31 OG1 CG2 REMARK 470 PHE A 32 CG CD1 CD2 CE1 CE2 CZ REMARK 470 MET A 34 CG SD CE REMARK 470 VAL A 35A CG1 CG2 REMARK 470 TRP A 36 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP A 36 CZ3 CH2 REMARK 470 ILE A 37 CG1 CG2 CD1 REMARK 470 ARG A 38 CG CD NE CZ NH1 NH2 REMARK 470 GLN A 39 CG CD OE1 NE2 REMARK 470 PRO A 40 CG CD REMARK 470 SER A 41 OG REMARK 470 LYS A 43 CG CD CE NZ REMARK 470 LEU A 45 CG CD1 CD2 REMARK 470 GLU A 46 CG CD OE1 OE2 REMARK 470 TRP A 47 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP A 47 CZ3 CH2 REMARK 470 LEU A 48 CG CD1 CD2 REMARK 470 HIS A 50 CG ND1 CD2 CE1 NE2 REMARK 470 ILE A 51 CG1 CG2 CD1 REMARK 470 TRP A 52 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP A 52 CZ3 CH2 REMARK 470 TRP A 53 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP A 53 CZ3 CH2 REMARK 470 ASP A 54 CG OD1 OD2 REMARK 470 ASN A 55 CG OD1 ND2 REMARK 470 ASP A 56 CG OD1 OD2 REMARK 470 GLU A 57 CG CD OE1 OE2 REMARK 470 TYR A 58 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 CYS A 59 SG REMARK 470 ASN A 60 CG OD1 ND2 REMARK 470 PRO A 61 CG CD REMARK 470 LEU A 63 CG CD1 CD2 REMARK 470 LYS A 64 CG CD CE NZ REMARK 470 SER A 65 OG REMARK 470 ARG A 66 CG CD NE CZ NH1 NH2 REMARK 470 LEU A 67 CG CD1 CD2 REMARK 470 THR A 68 OG1 CG2 REMARK 470 ILE A 69 CG1 CG2 CD1 REMARK 470 SER A 70 OG REMARK 470 LYS A 71 CG CD CE NZ REMARK 470 ASP A 72 CG OD1 OD2 REMARK 470 THR A 73 OG1 CG2 REMARK 470 SER A 74 OG REMARK 470 LYS A 75 CG CD CE NZ REMARK 470 ASN A 76 CG OD1 ND2 REMARK 470 HIS A 77 CG ND1 CD2 CE1 NE2 REMARK 470 ILE A 78 CG1 CG2 CD1 REMARK 470 PHE A 79 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LEU A 80 CG CD1 CD2 REMARK 470 LYS A 81 CG CD CE NZ REMARK 470 ILE A 82 CG1 CG2 CD1 REMARK 470 ASN A 82B CG OD1 ND2 REMARK 470 VAL A 82C CG1 CG2 REMARK 470 ASP A 83 CG OD1 OD2 REMARK 470 THR A 84 OG1 CG2 REMARK 470 ASP A 86 CG OD1 OD2 REMARK 470 THR A 87 OG1 CG2 REMARK 470 THR A 89 OG1 CG2 REMARK 470 TYR A 90 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 TYR A 91 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 CYS A 92 SG REMARK 470 ARG A 94 CG CD NE CZ NH1 NH2 REMARK 470 ILE A 95 CG1 CG2 CD1 REMARK 470 PHE A 96 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ASN A 98 CG OD1 ND2 REMARK 470 TYR A 99 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ASP A 100B CG OD1 OD2 REMARK 470 MET A 100D CG SD CE REMARK 470 ASP A 101 CG OD1 OD2 REMARK 470 TYR A 102 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 TRP A 103 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP A 103 CZ3 CH2 REMARK 470 GLN A 105 CG CD OE1 NE2 REMARK 470 THR A 107 OG1 CG2 REMARK 470 SER A 108 OG REMARK 470 VAL A 109 CG1 CG2 REMARK 470 THR A 110 OG1 CG2 REMARK 470 VAL A 111 CG1 CG2 REMARK 470 SER A 112 OG REMARK 470 GLN D 1 CG CD OE1 NE2 REMARK 470 VAL D 3 CG1 CG2 REMARK 470 VAL D 4 CG1 CG2 REMARK 470 THR D 5 OG1 CG2 REMARK 470 GLN D 6 CG CD OE1 NE2 REMARK 470 GLU D 7 CG CD OE1 OE2 REMARK 470 SER D 8 OG REMARK 470 LEU D 11 CG CD1 CD2 REMARK 470 THR D 12 OG1 CG2 REMARK 470 THR D 13 OG1 CG2 REMARK 470 SER D 14 OG REMARK 470 PRO D 15 CG CD REMARK 470 THR D 18 OG1 CG2 REMARK 470 VAL D 19 CG1 CG2 REMARK 470 ILE D 20 CG1 CG2 CD1 REMARK 470 LEU D 21 CG CD1 CD2 REMARK 470 THR D 22 OG1 CG2 REMARK 470 CYS D 23 SG REMARK 470 ARG D 24 CG CD NE CZ NH1 NH2 REMARK 470 SER D 25 OG REMARK 470 SER D 26 OG REMARK 470 THR D 27 OG1 CG2 REMARK 470 VAL D 27C CG1 CG2 REMARK 470 THR D 28 OG1 CG2 REMARK 470 THR D 29 OG1 CG2 REMARK 470 SER D 30 OG REMARK 470 ASN D 31 CG OD1 ND2 REMARK 470 TYR D 32 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ASN D 34 CG OD1 ND2 REMARK 470 TRP D 35 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP D 35 CZ3 CH2 REMARK 470 VAL D 36 CG1 CG2 REMARK 470 GLN D 37 CG CD OE1 NE2 REMARK 470 LYS D 38 CG CD CE NZ REMARK 470 LYS D 39 CG CD CE NZ REMARK 470 PRO D 40 CG CD REMARK 470 ASP D 41 CG OD1 OD2 REMARK 470 HIS D 42 CG ND1 CD2 CE1 NE2 REMARK 470 LEU D 43 CG CD1 CD2 REMARK 470 PHE D 44 CG CD1 CD2 CE1 CE2 CZ REMARK 470 THR D 45 OG1 CG2 REMARK 470 LEU D 47 CG CD1 CD2 REMARK 470 ILE D 48 CG1 CG2 CD1 REMARK 470 THR D 51 OG1 CG2 REMARK 470 SER D 52 OG REMARK 470 ASN D 53 CG OD1 ND2 REMARK 470 ARG D 54 CG CD NE CZ NH1 NH2 REMARK 470 VAL D 55 CG1 CG2 REMARK 470 SER D 56 OG REMARK 470 VAL D 58 CG1 CG2 REMARK 470 PRO D 59 CG CD REMARK 470 VAL D 60 CG1 CG2 REMARK 470 ARG D 61 CG CD NE CZ NH1 NH2 REMARK 470 PHE D 62 CG CD1 CD2 CE1 CE2 CZ REMARK 470 SER D 63 OG REMARK 470 SER D 65 OG REMARK 470 LEU D 66 CG CD1 CD2 REMARK 470 ILE D 67 CG1 CG2 CD1 REMARK 470 ASP D 69 CG OD1 OD2 REMARK 470 LYS D 70 CG CD CE NZ REMARK 470 LEU D 73 CG CD1 CD2 REMARK 470 THR D 74 OG1 CG2 REMARK 470 ILE D 75 CG1 CG2 CD1 REMARK 470 THR D 76 OG1 CG2 REMARK 470 GLN D 79 CG CD OE1 NE2 REMARK 470 THR D 80 OG1 CG2 REMARK 470 GLU D 81 CG CD OE1 OE2 REMARK 470 ASP D 82 CG OD1 OD2 REMARK 470 ASP D 83 CG OD1 OD2 REMARK 470 MET D 85 CG SD CE REMARK 470 TYR D 86 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 PHE D 87 CG CD1 CD2 CE1 CE2 CZ REMARK 470 CYS D 88 SG REMARK 470 LEU D 90 CG CD1 CD2 REMARK 470 TRP D 91 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP D 91 CZ3 CH2 REMARK 470 PHE D 92 CG CD1 CD2 CE1 CE2 CZ REMARK 470 SER D 93 OG REMARK 470 THR D 94 OG1 CG2 REMARK 470 HIS D 95 CG ND1 CD2 CE1 NE2 REMARK 470 TYR D 96 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 VAL D 97 CG1 CG2 REMARK 470 PHE D 98 CG CD1 CD2 CE1 CE2 CZ REMARK 470 THR D 102 OG1 CG2 REMARK 470 LYS D 103 CG CD CE NZ REMARK 470 VAL D 104 CG1 CG2 REMARK 470 THR D 105 OG1 CG2 REMARK 470 VAL D 106 CG1 CG2 REMARK 470 LEU D 106A CG CD1 CD2 REMARK 470 SER D 107 OG REMARK 470 GLN H 1 CG CD OE1 NE2 REMARK 470 VAL H 2 CG1 CG2 REMARK 470 THR H 3 OG1 CG2 REMARK 470 LEU H 4 CG CD1 CD2 REMARK 470 LYS H 5 CG CD CE NZ REMARK 470 GLU H 6 CG CD OE1 OE2 REMARK 470 SER H 7 OG REMARK 470 PRO H 9 CG CD REMARK 470 ILE H 11 CG1 CG2 CD1 REMARK 470 LEU H 12 CG CD1 CD2 REMARK 470 GLN H 13 CG CD OE1 NE2 REMARK 470 PRO H 14 CG CD REMARK 470 SER H 15 OG REMARK 470 GLN H 16 CG CD OE1 NE2 REMARK 470 THR H 17 OG1 CG2 REMARK 470 LEU H 18 CG CD1 CD2 REMARK 470 SER H 19 OG REMARK 470 LEU H 20 CG CD1 CD2 REMARK 470 THR H 21 OG1 CG2 REMARK 470 CYS H 22 SG REMARK 470 SER H 23 OG REMARK 470 PHE H 24 CG CD1 CD2 CE1 CE2 CZ REMARK 470 SER H 25 OG REMARK 470 PHE H 27 CG CD1 CD2 CE1 CE2 CZ REMARK 470 SER H 28 OG REMARK 470 LEU H 29 CG CD1 CD2 REMARK 470 SER H 30 OG REMARK 470 THR H 31 OG1 CG2 REMARK 470 PHE H 32 CG CD1 CD2 CE1 CE2 CZ REMARK 470 MET H 34 CG SD CE REMARK 470 VAL H 35A CG1 CG2 REMARK 470 TRP H 36 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP H 36 CZ3 CH2 REMARK 470 ILE H 37 CG1 CG2 CD1 REMARK 470 ARG H 38 CG CD NE CZ NH1 NH2 REMARK 470 GLN H 39 CG CD OE1 NE2 REMARK 470 PRO H 40 CG CD REMARK 470 SER H 41 OG REMARK 470 LYS H 43 CG CD CE NZ REMARK 470 LEU H 45 CG CD1 CD2 REMARK 470 GLU H 46 CG CD OE1 OE2 REMARK 470 TRP H 47 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP H 47 CZ3 CH2 REMARK 470 LEU H 48 CG CD1 CD2 REMARK 470 HIS H 50 CG ND1 CD2 CE1 NE2 REMARK 470 ILE H 51 CG1 CG2 CD1 REMARK 470 TRP H 52 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP H 52 CZ3 CH2 REMARK 470 TRP H 53 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP H 53 CZ3 CH2 REMARK 470 ASP H 54 CG OD1 OD2 REMARK 470 ASN H 55 CG OD1 ND2 REMARK 470 ASP H 56 CG OD1 OD2 REMARK 470 GLU H 57 CG CD OE1 OE2 REMARK 470 TYR H 58 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 CYS H 59 SG REMARK 470 ASN H 60 CG OD1 ND2 REMARK 470 PRO H 61 CG CD REMARK 470 LEU H 63 CG CD1 CD2 REMARK 470 LYS H 64 CG CD CE NZ REMARK 470 SER H 65 OG REMARK 470 ARG H 66 CG CD NE CZ NH1 NH2 REMARK 470 LEU H 67 CG CD1 CD2 REMARK 470 THR H 68 OG1 CG2 REMARK 470 ILE H 69 CG1 CG2 CD1 REMARK 470 SER H 70 OG REMARK 470 LYS H 71 CG CD CE NZ REMARK 470 ASP H 72 CG OD1 OD2 REMARK 470 THR H 73 OG1 CG2 REMARK 470 SER H 74 OG REMARK 470 LYS H 75 CG CD CE NZ REMARK 470 ASN H 76 CG OD1 ND2 REMARK 470 HIS H 77 CG ND1 CD2 CE1 NE2 REMARK 470 ILE H 78 CG1 CG2 CD1 REMARK 470 PHE H 79 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LEU H 80 CG CD1 CD2 REMARK 470 LYS H 81 CG CD CE NZ REMARK 470 ILE H 82 CG1 CG2 CD1 REMARK 470 ASN H 82B CG OD1 ND2 REMARK 470 VAL H 82C CG1 CG2 REMARK 470 ASP H 83 CG OD1 OD2 REMARK 470 THR H 84 OG1 CG2 REMARK 470 ASP H 86 CG OD1 OD2 REMARK 470 THR H 87 OG1 CG2 REMARK 470 THR H 89 OG1 CG2 REMARK 470 TYR H 90 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 TYR H 91 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 CYS H 92 SG REMARK 470 ARG H 94 CG CD NE CZ NH1 NH2 REMARK 470 ILE H 95 CG1 CG2 CD1 REMARK 470 PHE H 96 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ASN H 98 CG OD1 ND2 REMARK 470 TYR H 99 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ASP H 100B CG OD1 OD2 REMARK 470 MET H 100D CG SD CE REMARK 470 ASP H 101 CG OD1 OD2 REMARK 470 TYR H 102 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 TRP H 103 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP H 103 CZ3 CH2 REMARK 470 GLN H 105 CG CD OE1 NE2 REMARK 470 THR H 107 OG1 CG2 REMARK 470 SER H 108 OG REMARK 470 VAL H 109 CG1 CG2 REMARK 470 THR H 110 OG1 CG2 REMARK 470 VAL H 111 CG1 CG2 REMARK 470 SER H 112 OG REMARK 470 SER H 113 OG REMARK 470 GLN J 1 CG CD OE1 NE2 REMARK 470 VAL J 3 CG1 CG2 REMARK 470 VAL J 4 CG1 CG2 REMARK 470 THR J 5 OG1 CG2 REMARK 470 GLN J 6 CG CD OE1 NE2 REMARK 470 GLU J 7 CG CD OE1 OE2 REMARK 470 SER J 8 OG REMARK 470 LEU J 11 CG CD1 CD2 REMARK 470 THR J 12 OG1 CG2 REMARK 470 THR J 13 OG1 CG2 REMARK 470 SER J 14 OG REMARK 470 PRO J 15 CG CD REMARK 470 THR J 18 OG1 CG2 REMARK 470 VAL J 19 CG1 CG2 REMARK 470 ILE J 20 CG1 CG2 CD1 REMARK 470 LEU J 21 CG CD1 CD2 REMARK 470 THR J 22 OG1 CG2 REMARK 470 CYS J 23 SG REMARK 470 ARG J 24 CG CD NE CZ NH1 NH2 REMARK 470 SER J 25 OG REMARK 470 SER J 26 OG REMARK 470 THR J 27 OG1 CG2 REMARK 470 VAL J 27C CG1 CG2 REMARK 470 THR J 28 OG1 CG2 REMARK 470 THR J 29 OG1 CG2 REMARK 470 SER J 30 OG REMARK 470 ASN J 31 CG OD1 ND2 REMARK 470 TYR J 32 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ASN J 34 CG OD1 ND2 REMARK 470 TRP J 35 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP J 35 CZ3 CH2 REMARK 470 VAL J 36 CG1 CG2 REMARK 470 GLN J 37 CG CD OE1 NE2 REMARK 470 LYS J 38 CG CD CE NZ REMARK 470 LYS J 39 CG CD CE NZ REMARK 470 PRO J 40 CG CD REMARK 470 ASP J 41 CG OD1 OD2 REMARK 470 HIS J 42 CG ND1 CD2 CE1 NE2 REMARK 470 LEU J 43 CG CD1 CD2 REMARK 470 PHE J 44 CG CD1 CD2 CE1 CE2 CZ REMARK 470 THR J 45 OG1 CG2 REMARK 470 LEU J 47 CG CD1 CD2 REMARK 470 ILE J 48 CG1 CG2 CD1 REMARK 470 THR J 51 OG1 CG2 REMARK 470 SER J 52 OG REMARK 470 ASN J 53 CG OD1 ND2 REMARK 470 ARG J 54 CG CD NE CZ NH1 NH2 REMARK 470 VAL J 55 CG1 CG2 REMARK 470 SER J 56 OG REMARK 470 VAL J 58 CG1 CG2 REMARK 470 PRO J 59 CG CD REMARK 470 VAL J 60 CG1 CG2 REMARK 470 ARG J 61 CG CD NE CZ NH1 NH2 REMARK 470 PHE J 62 CG CD1 CD2 CE1 CE2 CZ REMARK 470 SER J 63 OG REMARK 470 SER J 65 OG REMARK 470 LEU J 66 CG CD1 CD2 REMARK 470 ILE J 67 CG1 CG2 CD1 REMARK 470 ASP J 69 CG OD1 OD2 REMARK 470 LYS J 70 CG CD CE NZ REMARK 470 LEU J 73 CG CD1 CD2 REMARK 470 THR J 74 OG1 CG2 REMARK 470 ILE J 75 CG1 CG2 CD1 REMARK 470 THR J 76 OG1 CG2 REMARK 470 GLN J 79 CG CD OE1 NE2 REMARK 470 THR J 80 OG1 CG2 REMARK 470 GLU J 81 CG CD OE1 OE2 REMARK 470 ASP J 82 CG OD1 OD2 REMARK 470 ASP J 83 CG OD1 OD2 REMARK 470 MET J 85 CG SD CE REMARK 470 TYR J 86 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 PHE J 87 CG CD1 CD2 CE1 CE2 CZ REMARK 470 CYS J 88 SG REMARK 470 LEU J 90 CG CD1 CD2 REMARK 470 TRP J 91 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP J 91 CZ3 CH2 REMARK 470 PHE J 92 CG CD1 CD2 CE1 CE2 CZ REMARK 470 SER J 93 OG REMARK 470 THR J 94 OG1 CG2 REMARK 470 HIS J 95 CG ND1 CD2 CE1 NE2 REMARK 470 TYR J 96 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 VAL J 97 CG1 CG2 REMARK 470 PHE J 98 CG CD1 CD2 CE1 CE2 CZ REMARK 470 THR J 102 OG1 CG2 REMARK 470 LYS J 103 CG CD CE NZ REMARK 470 VAL J 104 CG1 CG2 REMARK 470 THR J 105 OG1 CG2 REMARK 470 VAL J 106 CG1 CG2 REMARK 470 LEU J 106A CG CD1 CD2 REMARK 470 SER J 107 OG REMARK 470 GLN J 108 CG CD OE1 NE2 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 ASP B 101 CB - CG - OD1 ANGL. DEV. = 7.0 DEGREES REMARK 500 ASP B 291 CB - CG - OD1 ANGL. DEV. = 5.8 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 ASP B 53 51.79 -95.20 REMARK 500 ASN B 81 46.20 34.05 REMARK 500 LEU B 86 116.43 -161.04 REMARK 500 GLU B 325 -94.26 67.53 REMARK 500 THR C 28 -169.72 -125.94 REMARK 500 ASP C 53 56.17 -98.76 REMARK 500 SER C 124 39.31 -98.27 REMARK 500 SER C 137 44.33 -92.69 REMARK 500 ARG C 141 79.83 -110.86 REMARK 500 ARG C 142 -16.47 67.24 REMARK 500 SER C 143 -27.59 -143.65 REMARK 500 ASN C 158 74.08 -69.35 REMARK 500 ALA C 196 18.73 59.35 REMARK 500 VAL C 323 73.21 52.37 REMARK 500 PRO C 324 -119.18 0.35 REMARK 500 GLN C 327 -172.63 59.59 REMARK 500 ASN E 28 -167.23 -120.82 REMARK 500 LYS E 39 -10.69 71.76 REMARK 500 HIS E 142 170.38 64.89 REMARK 500 ARG E 170 -156.89 -126.35 REMARK 500 PHE F 3 -137.26 57.99 REMARK 500 PHE F 9 -11.41 71.56 REMARK 500 GLU F 11 -104.04 59.32 REMARK 500 THR F 156 52.77 -93.07 REMARK 500 CYS G 30 -159.48 -144.25 REMARK 500 ASN G 31 127.10 -32.41 REMARK 500 ASN G 63 48.39 39.99 REMARK 500 PHE G 79 31.82 -98.66 REMARK 500 THR G 128 -164.69 -80.00 REMARK 500 ASN G 145 144.35 68.29 REMARK 500 ALA G 163 127.62 -39.73 REMARK 500 GLN G 327 -161.37 50.02 REMARK 500 ALA I 7 -167.44 -124.95 REMARK 500 PHE I 9 -75.38 61.37 REMARK 500 GLU I 11 66.31 61.22 REMARK 500 ASN I 12 148.80 77.48 REMARK 500 LEU I 52 48.95 -90.62 REMARK 500 HIS I 142 73.21 59.04 REMARK 500 LYS I 143 128.46 -36.89 REMARK 500 THR I 156 54.21 -92.36 REMARK 500 PHE I 171 -147.04 62.07 REMARK 500 ASP A 54 32.97 -97.53 REMARK 500 THR D 51 -7.96 70.64 REMARK 500 SER D 93 -8.83 71.28 REMARK 500 SER H 41 67.14 60.99 REMARK 500 LEU H 48 -62.58 -94.05 REMARK 500 ALA J 2 65.78 60.39 REMARK 500 THR J 51 -12.89 73.07 REMARK 500 SER J 93 -8.57 71.39 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 CYS G 30 ASN G 31 -146.18 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-48079 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF 5E10 FAB IN COMPLEX WITH H3 INFLUENZA VICTORIA REMARK 900 2011 HA TRIMER DBREF 9EI9 B 1 329 UNP L0HR89 L0HR89_9INFA 17 345 DBREF 9EI9 C 1 329 UNP L0HR89 L0HR89_9INFA 17 345 DBREF 9EI9 E 1 176 UNP L0HR89 L0HR89_9INFA 346 521 DBREF 9EI9 F 1 176 UNP L0HR89 L0HR89_9INFA 346 521 DBREF 9EI9 G 1 329 UNP L0HR89 L0HR89_9INFA 17 345 DBREF 9EI9 I 1 176 UNP L0HR89 L0HR89_9INFA 346 521 DBREF 9EI9 A 1 114 PDB 9EI9 9EI9 1 114 DBREF 9EI9 D 1 108 PDB 9EI9 9EI9 1 108 DBREF 9EI9 H 1 114 PDB 9EI9 9EI9 1 114 DBREF 9EI9 J 1 108 PDB 9EI9 9EI9 1 108 SEQADV 9EI9 CYS B 30 UNP L0HR89 THR 46 CONFLICT SEQADV 9EI9 ARG B 330 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 ARG B 331 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 ARG B 332 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 ARG B 333 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 ARG B 334 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 CYS C 30 UNP L0HR89 THR 46 CONFLICT SEQADV 9EI9 ARG C 330 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 ARG C 331 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 ARG C 332 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 ARG C 333 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 ARG C 334 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 CYS E 47 UNP L0HR89 GLN 392 CONFLICT SEQADV 9EI9 SER E 177 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 GLY E 178 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 ARG E 179 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 LEU E 180 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 VAL E 181 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 PRO E 182 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 ARG E 183 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 GLY E 184 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 SER E 185 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 PRO E 186 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 GLY E 187 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 SER E 188 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 GLY E 189 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 TYR E 190 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 ILE E 191 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 PRO E 192 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 GLU E 193 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 ALA E 194 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 PRO E 195 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 ARG E 196 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 ASP E 197 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 GLY E 198 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 GLN E 199 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 ALA E 200 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 TYR E 201 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 VAL E 202 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 ARG E 203 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 LYS E 204 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 ASP E 205 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 GLY E 206 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 GLU E 207 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 TRP E 208 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 VAL E 209 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 LEU E 210 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 LEU E 211 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 SER E 212 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 THR E 213 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 PHE E 214 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 LEU E 215 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 GLY E 216 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 HIS E 217 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 HIS E 218 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 HIS E 219 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 HIS E 220 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 HIS E 221 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 HIS E 222 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 CYS F 47 UNP L0HR89 GLN 392 CONFLICT SEQADV 9EI9 SER F 177 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 GLY F 178 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 ARG F 179 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 LEU F 180 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 VAL F 181 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 PRO F 182 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 ARG F 183 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 GLY F 184 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 SER F 185 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 PRO F 186 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 GLY F 187 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 SER F 188 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 GLY F 189 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 TYR F 190 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 ILE F 191 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 PRO F 192 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 GLU F 193 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 ALA F 194 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 PRO F 195 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 ARG F 196 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 ASP F 197 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 GLY F 198 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 GLN F 199 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 ALA F 200 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 TYR F 201 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 VAL F 202 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 ARG F 203 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 LYS F 204 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 ASP F 205 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 GLY F 206 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 GLU F 207 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 TRP F 208 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 VAL F 209 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 LEU F 210 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 LEU F 211 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 SER F 212 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 THR F 213 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 PHE F 214 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 LEU F 215 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 GLY F 216 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 HIS F 217 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 HIS F 218 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 HIS F 219 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 HIS F 220 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 HIS F 221 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 HIS F 222 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 CYS G 30 UNP L0HR89 THR 46 CONFLICT SEQADV 9EI9 ARG G 330 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 ARG G 331 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 ARG G 332 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 ARG G 333 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 ARG G 334 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 CYS I 47 UNP L0HR89 GLN 392 CONFLICT SEQADV 9EI9 SER I 177 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 GLY I 178 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 ARG I 179 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 LEU I 180 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 VAL I 181 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 PRO I 182 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 ARG I 183 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 GLY I 184 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 SER I 185 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 PRO I 186 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 GLY I 187 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 SER I 188 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 GLY I 189 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 TYR I 190 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 ILE I 191 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 PRO I 192 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 GLU I 193 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 ALA I 194 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 PRO I 195 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 ARG I 196 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 ASP I 197 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 GLY I 198 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 GLN I 199 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 ALA I 200 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 TYR I 201 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 VAL I 202 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 ARG I 203 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 LYS I 204 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 ASP I 205 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 GLY I 206 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 GLU I 207 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 TRP I 208 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 VAL I 209 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 LEU I 210 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 LEU I 211 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 SER I 212 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 THR I 213 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 PHE I 214 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 LEU I 215 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 GLY I 216 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 HIS I 217 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 HIS I 218 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 HIS I 219 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 HIS I 220 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 HIS I 221 UNP L0HR89 EXPRESSION TAG SEQADV 9EI9 HIS I 222 UNP L0HR89 EXPRESSION TAG SEQRES 1 B 334 GLN LYS LEU PRO GLY ASN ASP ASN SER THR ALA THR LEU SEQRES 2 B 334 CYS LEU GLY HIS HIS ALA VAL PRO ASN GLY THR ILE VAL SEQRES 3 B 334 LYS THR ILE CYS ASN ASP GLN ILE GLU VAL THR ASN ALA SEQRES 4 B 334 THR GLU LEU VAL GLN ASN SER SER ILE GLY GLU ILE CYS SEQRES 5 B 334 ASP SER PRO HIS GLN ILE LEU ASP GLY GLU ASN CYS THR SEQRES 6 B 334 LEU ILE ASP ALA LEU LEU GLY ASP PRO GLN CYS ASP GLY SEQRES 7 B 334 PHE GLN ASN LYS LYS TRP ASP LEU PHE VAL GLU ARG SER SEQRES 8 B 334 LYS ALA TYR SER ASN CYS TYR PRO TYR ASP VAL PRO ASP SEQRES 9 B 334 TYR ALA SER LEU ARG SER LEU VAL ALA SER SER GLY THR SEQRES 10 B 334 LEU GLU PHE ASN ASN GLU SER PHE ASN TRP THR GLY VAL SEQRES 11 B 334 THR GLN ASN GLY THR SER SER ALA CYS ILE ARG ARG SER SEQRES 12 B 334 ASN ASN SER PHE PHE SER ARG LEU ASN TRP LEU THR GLN SEQRES 13 B 334 LEU ASN PHE LYS TYR PRO ALA LEU ASN VAL THR MET PRO SEQRES 14 B 334 ASN ASN GLU GLN PHE ASP LYS LEU TYR ILE TRP GLY VAL SEQRES 15 B 334 HIS HIS PRO VAL THR ASP LYS ASP GLN ILE PHE LEU TYR SEQRES 16 B 334 ALA GLN SER SER GLY ARG ILE THR VAL SER THR LYS ARG SEQRES 17 B 334 SER GLN GLN ALA VAL ILE PRO ASN ILE GLY TYR ARG PRO SEQRES 18 B 334 ARG ILE ARG ASN ILE PRO SER ARG ILE SER ILE TYR TRP SEQRES 19 B 334 THR ILE VAL LYS PRO GLY ASP ILE LEU LEU ILE ASN SER SEQRES 20 B 334 THR GLY ASN LEU ILE ALA PRO ARG GLY TYR PHE LYS ILE SEQRES 21 B 334 ARG SER GLY LYS SER SER ILE MET ARG SER ASP ALA PRO SEQRES 22 B 334 ILE GLY LYS CYS ASN SER GLU CYS ILE THR PRO ASN GLY SEQRES 23 B 334 SER ILE PRO ASN ASP LYS PRO PHE GLN ASN VAL ASN ARG SEQRES 24 B 334 ILE THR TYR GLY ALA CYS PRO ARG TYR VAL LYS GLN SER SEQRES 25 B 334 THR LEU LYS LEU ALA THR GLY MET ARG ASN VAL PRO GLU SEQRES 26 B 334 LYS GLN THR ARG ARG ARG ARG ARG ARG SEQRES 1 C 334 GLN LYS LEU PRO GLY ASN ASP ASN SER THR ALA THR LEU SEQRES 2 C 334 CYS LEU GLY HIS HIS ALA VAL PRO ASN GLY THR ILE VAL SEQRES 3 C 334 LYS THR ILE CYS ASN ASP GLN ILE GLU VAL THR ASN ALA SEQRES 4 C 334 THR GLU LEU VAL GLN ASN SER SER ILE GLY GLU ILE CYS SEQRES 5 C 334 ASP SER PRO HIS GLN ILE LEU ASP GLY GLU ASN CYS THR SEQRES 6 C 334 LEU ILE ASP ALA LEU LEU GLY ASP PRO GLN CYS ASP GLY SEQRES 7 C 334 PHE GLN ASN LYS LYS TRP ASP LEU PHE VAL GLU ARG SER SEQRES 8 C 334 LYS ALA TYR SER ASN CYS TYR PRO TYR ASP VAL PRO ASP SEQRES 9 C 334 TYR ALA SER LEU ARG SER LEU VAL ALA SER SER GLY THR SEQRES 10 C 334 LEU GLU PHE ASN ASN GLU SER PHE ASN TRP THR GLY VAL SEQRES 11 C 334 THR GLN ASN GLY THR SER SER ALA CYS ILE ARG ARG SER SEQRES 12 C 334 ASN ASN SER PHE PHE SER ARG LEU ASN TRP LEU THR GLN SEQRES 13 C 334 LEU ASN PHE LYS TYR PRO ALA LEU ASN VAL THR MET PRO SEQRES 14 C 334 ASN ASN GLU GLN PHE ASP LYS LEU TYR ILE TRP GLY VAL SEQRES 15 C 334 HIS HIS PRO VAL THR ASP LYS ASP GLN ILE PHE LEU TYR SEQRES 16 C 334 ALA GLN SER SER GLY ARG ILE THR VAL SER THR LYS ARG SEQRES 17 C 334 SER GLN GLN ALA VAL ILE PRO ASN ILE GLY TYR ARG PRO SEQRES 18 C 334 ARG ILE ARG ASN ILE PRO SER ARG ILE SER ILE TYR TRP SEQRES 19 C 334 THR ILE VAL LYS PRO GLY ASP ILE LEU LEU ILE ASN SER SEQRES 20 C 334 THR GLY ASN LEU ILE ALA PRO ARG GLY TYR PHE LYS ILE SEQRES 21 C 334 ARG SER GLY LYS SER SER ILE MET ARG SER ASP ALA PRO SEQRES 22 C 334 ILE GLY LYS CYS ASN SER GLU CYS ILE THR PRO ASN GLY SEQRES 23 C 334 SER ILE PRO ASN ASP LYS PRO PHE GLN ASN VAL ASN ARG SEQRES 24 C 334 ILE THR TYR GLY ALA CYS PRO ARG TYR VAL LYS GLN SER SEQRES 25 C 334 THR LEU LYS LEU ALA THR GLY MET ARG ASN VAL PRO GLU SEQRES 26 C 334 LYS GLN THR ARG ARG ARG ARG ARG ARG SEQRES 1 E 222 GLY ILE PHE GLY ALA ILE ALA GLY PHE ILE GLU ASN GLY SEQRES 2 E 222 TRP GLU GLY MET VAL ASP GLY TRP TYR GLY PHE ARG HIS SEQRES 3 E 222 GLN ASN SER GLU GLY ARG GLY GLN ALA ALA ASP LEU LYS SEQRES 4 E 222 SER THR GLN ALA ALA ILE ASP CYS ILE ASN GLY LYS LEU SEQRES 5 E 222 ASN ARG LEU ILE GLY LYS THR ASN GLU LYS PHE HIS GLN SEQRES 6 E 222 ILE GLU LYS GLU PHE SER GLU VAL GLU GLY ARG ILE GLN SEQRES 7 E 222 ASP LEU GLU LYS TYR VAL GLU ASP THR LYS ILE ASP LEU SEQRES 8 E 222 TRP SER TYR ASN ALA GLU LEU LEU VAL ALA LEU GLU ASN SEQRES 9 E 222 GLN HIS THR ILE ASP LEU THR ASP SER GLU MET ASN LYS SEQRES 10 E 222 LEU PHE GLU LYS THR LYS LYS GLN LEU ARG GLU ASN ALA SEQRES 11 E 222 GLU ASP MET GLY ASN GLY CYS PHE LYS ILE TYR HIS LYS SEQRES 12 E 222 CYS ASP ASN ALA CYS ILE GLY SER ILE ARG ASN GLY THR SEQRES 13 E 222 TYR ASP HIS ASP VAL TYR ARG ASP GLU ALA LEU ASN ASN SEQRES 14 E 222 ARG PHE GLN ILE LYS GLY VAL SER GLY ARG LEU VAL PRO SEQRES 15 E 222 ARG GLY SER PRO GLY SER GLY TYR ILE PRO GLU ALA PRO SEQRES 16 E 222 ARG ASP GLY GLN ALA TYR VAL ARG LYS ASP GLY GLU TRP SEQRES 17 E 222 VAL LEU LEU SER THR PHE LEU GLY HIS HIS HIS HIS HIS SEQRES 18 E 222 HIS SEQRES 1 F 222 GLY ILE PHE GLY ALA ILE ALA GLY PHE ILE GLU ASN GLY SEQRES 2 F 222 TRP GLU GLY MET VAL ASP GLY TRP TYR GLY PHE ARG HIS SEQRES 3 F 222 GLN ASN SER GLU GLY ARG GLY GLN ALA ALA ASP LEU LYS SEQRES 4 F 222 SER THR GLN ALA ALA ILE ASP CYS ILE ASN GLY LYS LEU SEQRES 5 F 222 ASN ARG LEU ILE GLY LYS THR ASN GLU LYS PHE HIS GLN SEQRES 6 F 222 ILE GLU LYS GLU PHE SER GLU VAL GLU GLY ARG ILE GLN SEQRES 7 F 222 ASP LEU GLU LYS TYR VAL GLU ASP THR LYS ILE ASP LEU SEQRES 8 F 222 TRP SER TYR ASN ALA GLU LEU LEU VAL ALA LEU GLU ASN SEQRES 9 F 222 GLN HIS THR ILE ASP LEU THR ASP SER GLU MET ASN LYS SEQRES 10 F 222 LEU PHE GLU LYS THR LYS LYS GLN LEU ARG GLU ASN ALA SEQRES 11 F 222 GLU ASP MET GLY ASN GLY CYS PHE LYS ILE TYR HIS LYS SEQRES 12 F 222 CYS ASP ASN ALA CYS ILE GLY SER ILE ARG ASN GLY THR SEQRES 13 F 222 TYR ASP HIS ASP VAL TYR ARG ASP GLU ALA LEU ASN ASN SEQRES 14 F 222 ARG PHE GLN ILE LYS GLY VAL SER GLY ARG LEU VAL PRO SEQRES 15 F 222 ARG GLY SER PRO GLY SER GLY TYR ILE PRO GLU ALA PRO SEQRES 16 F 222 ARG ASP GLY GLN ALA TYR VAL ARG LYS ASP GLY GLU TRP SEQRES 17 F 222 VAL LEU LEU SER THR PHE LEU GLY HIS HIS HIS HIS HIS SEQRES 18 F 222 HIS SEQRES 1 G 334 GLN LYS LEU PRO GLY ASN ASP ASN SER THR ALA THR LEU SEQRES 2 G 334 CYS LEU GLY HIS HIS ALA VAL PRO ASN GLY THR ILE VAL SEQRES 3 G 334 LYS THR ILE CYS ASN ASP GLN ILE GLU VAL THR ASN ALA SEQRES 4 G 334 THR GLU LEU VAL GLN ASN SER SER ILE GLY GLU ILE CYS SEQRES 5 G 334 ASP SER PRO HIS GLN ILE LEU ASP GLY GLU ASN CYS THR SEQRES 6 G 334 LEU ILE ASP ALA LEU LEU GLY ASP PRO GLN CYS ASP GLY SEQRES 7 G 334 PHE GLN ASN LYS LYS TRP ASP LEU PHE VAL GLU ARG SER SEQRES 8 G 334 LYS ALA TYR SER ASN CYS TYR PRO TYR ASP VAL PRO ASP SEQRES 9 G 334 TYR ALA SER LEU ARG SER LEU VAL ALA SER SER GLY THR SEQRES 10 G 334 LEU GLU PHE ASN ASN GLU SER PHE ASN TRP THR GLY VAL SEQRES 11 G 334 THR GLN ASN GLY THR SER SER ALA CYS ILE ARG ARG SER SEQRES 12 G 334 ASN ASN SER PHE PHE SER ARG LEU ASN TRP LEU THR GLN SEQRES 13 G 334 LEU ASN PHE LYS TYR PRO ALA LEU ASN VAL THR MET PRO SEQRES 14 G 334 ASN ASN GLU GLN PHE ASP LYS LEU TYR ILE TRP GLY VAL SEQRES 15 G 334 HIS HIS PRO VAL THR ASP LYS ASP GLN ILE PHE LEU TYR SEQRES 16 G 334 ALA GLN SER SER GLY ARG ILE THR VAL SER THR LYS ARG SEQRES 17 G 334 SER GLN GLN ALA VAL ILE PRO ASN ILE GLY TYR ARG PRO SEQRES 18 G 334 ARG ILE ARG ASN ILE PRO SER ARG ILE SER ILE TYR TRP SEQRES 19 G 334 THR ILE VAL LYS PRO GLY ASP ILE LEU LEU ILE ASN SER SEQRES 20 G 334 THR GLY ASN LEU ILE ALA PRO ARG GLY TYR PHE LYS ILE SEQRES 21 G 334 ARG SER GLY LYS SER SER ILE MET ARG SER ASP ALA PRO SEQRES 22 G 334 ILE GLY LYS CYS ASN SER GLU CYS ILE THR PRO ASN GLY SEQRES 23 G 334 SER ILE PRO ASN ASP LYS PRO PHE GLN ASN VAL ASN ARG SEQRES 24 G 334 ILE THR TYR GLY ALA CYS PRO ARG TYR VAL LYS GLN SER SEQRES 25 G 334 THR LEU LYS LEU ALA THR GLY MET ARG ASN VAL PRO GLU SEQRES 26 G 334 LYS GLN THR ARG ARG ARG ARG ARG ARG SEQRES 1 I 222 GLY ILE PHE GLY ALA ILE ALA GLY PHE ILE GLU ASN GLY SEQRES 2 I 222 TRP GLU GLY MET VAL ASP GLY TRP TYR GLY PHE ARG HIS SEQRES 3 I 222 GLN ASN SER GLU GLY ARG GLY GLN ALA ALA ASP LEU LYS SEQRES 4 I 222 SER THR GLN ALA ALA ILE ASP CYS ILE ASN GLY LYS LEU SEQRES 5 I 222 ASN ARG LEU ILE GLY LYS THR ASN GLU LYS PHE HIS GLN SEQRES 6 I 222 ILE GLU LYS GLU PHE SER GLU VAL GLU GLY ARG ILE GLN SEQRES 7 I 222 ASP LEU GLU LYS TYR VAL GLU ASP THR LYS ILE ASP LEU SEQRES 8 I 222 TRP SER TYR ASN ALA GLU LEU LEU VAL ALA LEU GLU ASN SEQRES 9 I 222 GLN HIS THR ILE ASP LEU THR ASP SER GLU MET ASN LYS SEQRES 10 I 222 LEU PHE GLU LYS THR LYS LYS GLN LEU ARG GLU ASN ALA SEQRES 11 I 222 GLU ASP MET GLY ASN GLY CYS PHE LYS ILE TYR HIS LYS SEQRES 12 I 222 CYS ASP ASN ALA CYS ILE GLY SER ILE ARG ASN GLY THR SEQRES 13 I 222 TYR ASP HIS ASP VAL TYR ARG ASP GLU ALA LEU ASN ASN SEQRES 14 I 222 ARG PHE GLN ILE LYS GLY VAL SER GLY ARG LEU VAL PRO SEQRES 15 I 222 ARG GLY SER PRO GLY SER GLY TYR ILE PRO GLU ALA PRO SEQRES 16 I 222 ARG ASP GLY GLN ALA TYR VAL ARG LYS ASP GLY GLU TRP SEQRES 17 I 222 VAL LEU LEU SER THR PHE LEU GLY HIS HIS HIS HIS HIS SEQRES 18 I 222 HIS SEQRES 1 A 123 GLN VAL THR LEU LYS GLU SER GLY PRO GLY ILE LEU GLN SEQRES 2 A 123 PRO SER GLN THR LEU SER LEU THR CYS SER PHE SER GLY SEQRES 3 A 123 PHE SER LEU SER THR PHE GLY MET GLY VAL GLY TRP ILE SEQRES 4 A 123 ARG GLN PRO SER GLY LYS GLY LEU GLU TRP LEU ALA HIS SEQRES 5 A 123 ILE TRP TRP ASP ASN ASP GLU TYR CYS ASN PRO ALA LEU SEQRES 6 A 123 LYS SER ARG LEU THR ILE SER LYS ASP THR SER LYS ASN SEQRES 7 A 123 HIS ILE PHE LEU LYS ILE ALA ASN VAL ASP THR ALA ASP SEQRES 8 A 123 THR ALA THR TYR TYR CYS ALA ARG ILE PHE ALA ASN TYR SEQRES 9 A 123 GLY GLY ASP ALA MET ASP TYR TRP GLY GLN GLY THR SER SEQRES 10 A 123 VAL THR VAL SER SER ALA SEQRES 1 D 111 GLN ALA VAL VAL THR GLN GLU SER ALA LEU THR THR SER SEQRES 2 D 111 PRO GLY GLY THR VAL ILE LEU THR CYS ARG SER SER THR SEQRES 3 D 111 GLY ALA VAL THR THR SER ASN TYR ALA ASN TRP VAL GLN SEQRES 4 D 111 LYS LYS PRO ASP HIS LEU PHE THR GLY LEU ILE GLY GLY SEQRES 5 D 111 THR SER ASN ARG VAL SER GLY VAL PRO VAL ARG PHE SER SEQRES 6 D 111 GLY SER LEU ILE GLY ASP LYS ALA ALA LEU THR ILE THR SEQRES 7 D 111 GLY ALA GLN THR GLU ASP ASP ALA MET TYR PHE CYS ALA SEQRES 8 D 111 LEU TRP PHE SER THR HIS TYR VAL PHE GLY GLY GLY THR SEQRES 9 D 111 LYS VAL THR VAL LEU SER GLN SEQRES 1 H 123 GLN VAL THR LEU LYS GLU SER GLY PRO GLY ILE LEU GLN SEQRES 2 H 123 PRO SER GLN THR LEU SER LEU THR CYS SER PHE SER GLY SEQRES 3 H 123 PHE SER LEU SER THR PHE GLY MET GLY VAL GLY TRP ILE SEQRES 4 H 123 ARG GLN PRO SER GLY LYS GLY LEU GLU TRP LEU ALA HIS SEQRES 5 H 123 ILE TRP TRP ASP ASN ASP GLU TYR CYS ASN PRO ALA LEU SEQRES 6 H 123 LYS SER ARG LEU THR ILE SER LYS ASP THR SER LYS ASN SEQRES 7 H 123 HIS ILE PHE LEU LYS ILE ALA ASN VAL ASP THR ALA ASP SEQRES 8 H 123 THR ALA THR TYR TYR CYS ALA ARG ILE PHE ALA ASN TYR SEQRES 9 H 123 GLY GLY ASP ALA MET ASP TYR TRP GLY GLN GLY THR SER SEQRES 10 H 123 VAL THR VAL SER SER ALA SEQRES 1 J 111 GLN ALA VAL VAL THR GLN GLU SER ALA LEU THR THR SER SEQRES 2 J 111 PRO GLY GLY THR VAL ILE LEU THR CYS ARG SER SER THR SEQRES 3 J 111 GLY ALA VAL THR THR SER ASN TYR ALA ASN TRP VAL GLN SEQRES 4 J 111 LYS LYS PRO ASP HIS LEU PHE THR GLY LEU ILE GLY GLY SEQRES 5 J 111 THR SER ASN ARG VAL SER GLY VAL PRO VAL ARG PHE SER SEQRES 6 J 111 GLY SER LEU ILE GLY ASP LYS ALA ALA LEU THR ILE THR SEQRES 7 J 111 GLY ALA GLN THR GLU ASP ASP ALA MET TYR PHE CYS ALA SEQRES 8 J 111 LEU TRP PHE SER THR HIS TYR VAL PHE GLY GLY GLY THR SEQRES 9 J 111 LYS VAL THR VAL LEU SER GLN HET NAG K 1 14 HET NAG K 2 14 HET NAG L 1 14 HET NAG L 2 14 HET BMA L 3 11 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 BMA Q 3 11 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 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 406 14 HET NAG E 301 14 HET NAG F 301 14 HET NAG G 401 14 HET NAG G 402 14 HET NAG G 403 14 HET NAG G 404 14 HET NAG G 405 14 HET NAG G 406 14 HET NAG I 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 11 NAG 34(C8 H15 N O6) FORMUL 12 BMA 3(C6 H12 O6) HELIX 1 AA1 THR B 65 GLY B 72 1 8 HELIX 2 AA2 CYS B 76 GLN B 80 5 5 HELIX 3 AA3 ASP B 104 GLY B 116 1 13 HELIX 4 AA4 THR B 187 ALA B 196 1 10 HELIX 5 AA5 THR C 65 GLY C 72 1 8 HELIX 6 AA6 ASP C 73 ASP C 77 5 5 HELIX 7 AA7 ASP C 104 GLY C 116 1 13 HELIX 8 AA8 THR C 187 ALA C 196 1 10 HELIX 9 AA9 SER E 40 ILE E 56 1 17 HELIX 10 AB1 GLY E 75 LEU E 126 1 52 HELIX 11 AB2 ASP E 145 GLY E 155 1 11 HELIX 12 AB3 TYR E 162 ASN E 169 1 8 HELIX 13 AB4 LYS F 39 ILE F 56 1 18 HELIX 14 AB5 GLY F 75 GLN F 125 1 51 HELIX 15 AB6 ASP F 145 GLY F 155 1 11 HELIX 16 AB7 TYR F 162 GLN F 172 1 11 HELIX 17 AB8 THR G 65 GLY G 72 1 8 HELIX 18 AB9 ASP G 73 GLN G 80 5 8 HELIX 19 AC1 ASP G 104 GLY G 116 1 13 HELIX 20 AC2 THR G 187 ALA G 196 1 10 HELIX 21 AC3 LYS I 39 LEU I 52 1 14 HELIX 22 AC4 GLY I 75 LEU I 126 1 52 HELIX 23 AC5 ASN I 146 GLY I 155 1 10 HELIX 24 AC6 TYR I 162 LEU I 167 1 6 HELIX 25 AC7 PRO A 61 LYS A 64 5 4 HELIX 26 AC8 ASP A 83 THR A 87 5 5 HELIX 27 AC9 THR D 28 TYR D 32 5 5 HELIX 28 AD1 PRO H 61 LYS H 64 5 4 HELIX 29 AD2 ASP H 83 THR H 87 5 5 HELIX 30 AD3 THR J 28 TYR J 32 5 5 HELIX 31 AD4 GLN J 79 ASP J 83 5 5 SHEET 1 AA1 2 CYS B 14 LEU B 15 0 SHEET 2 AA1 2 PHE E 24 ARG E 25 -1 O ARG E 25 N CYS B 14 SHEET 1 AA2 2 THR B 24 VAL B 26 0 SHEET 2 AA2 2 ILE B 34 VAL B 36 -1 O VAL B 36 N THR B 24 SHEET 1 AA3 2 ALA B 39 GLU B 41 0 SHEET 2 AA3 2 LYS B 315 ALA B 317 -1 O LEU B 316 N THR B 40 SHEET 1 AA4 3 VAL B 43 GLN B 44 0 SHEET 2 AA4 3 PHE B 294 GLN B 295 1 O PHE B 294 N GLN B 44 SHEET 3 AA4 3 ARG B 307 TYR B 308 1 O ARG B 307 N GLN B 295 SHEET 1 AA5 2 ILE B 51 CYS B 52 0 SHEET 2 AA5 2 ILE B 274 GLY B 275 1 O GLY B 275 N ILE B 51 SHEET 1 AA6 3 ILE B 58 LEU B 59 0 SHEET 2 AA6 3 LEU B 86 GLU B 89 1 O VAL B 88 N LEU B 59 SHEET 3 AA6 3 SER B 266 ARG B 269 1 O SER B 266 N PHE B 87 SHEET 1 AA7 4 PHE B 120 ASN B 122 0 SHEET 2 AA7 4 GLY B 256 LYS B 259 -1 O TYR B 257 N ASN B 121 SHEET 3 AA7 4 LYS B 176 HIS B 184 -1 N LEU B 177 O PHE B 258 SHEET 4 AA7 4 ARG B 229 VAL B 237 -1 O ARG B 229 N HIS B 184 SHEET 1 AA8 2 SER B 136 ILE B 140 0 SHEET 2 AA8 2 ASN B 145 SER B 146 -1 O SER B 146 N SER B 136 SHEET 1 AA9 2 LEU B 151 TRP B 153 0 SHEET 2 AA9 2 ILE B 252 PRO B 254 -1 O ALA B 253 N ASN B 152 SHEET 1 AB1 4 LEU B 164 PRO B 169 0 SHEET 2 AB1 4 ILE B 242 SER B 247 -1 O SER B 247 N LEU B 164 SHEET 3 AB1 4 ILE B 202 SER B 205 -1 N THR B 203 O ASN B 246 SHEET 4 AB1 4 GLN B 210 VAL B 213 -1 O GLN B 211 N VAL B 204 SHEET 1 AB2 2 GLY B 303 ALA B 304 0 SHEET 2 AB2 2 GLU E 61 LYS E 62 -1 O LYS E 62 N GLY B 303 SHEET 1 AB3 3 GLY C 16 HIS C 17 0 SHEET 2 AB3 3 TYR F 22 ASN F 28 -1 O GLY F 23 N GLY C 16 SHEET 3 AB3 3 GLY F 31 ALA F 36 -1 O GLY F 31 N ASN F 28 SHEET 1 AB4 2 THR C 24 VAL C 26 0 SHEET 2 AB4 2 ILE C 34 VAL C 36 -1 O VAL C 36 N THR C 24 SHEET 1 AB5 2 ALA C 39 GLU C 41 0 SHEET 2 AB5 2 LYS C 315 ALA C 317 -1 O LEU C 316 N THR C 40 SHEET 1 AB6 3 VAL C 43 GLN C 44 0 SHEET 2 AB6 3 PHE C 294 GLN C 295 1 O PHE C 294 N GLN C 44 SHEET 3 AB6 3 ARG C 307 TYR C 308 1 O ARG C 307 N GLN C 295 SHEET 1 AB7 2 ILE C 51 CYS C 52 0 SHEET 2 AB7 2 ILE C 274 GLY C 275 1 O GLY C 275 N ILE C 51 SHEET 1 AB8 3 ILE C 58 LEU C 59 0 SHEET 2 AB8 3 LEU C 86 GLU C 89 1 O VAL C 88 N LEU C 59 SHEET 3 AB8 3 SER C 266 ARG C 269 1 O MET C 268 N PHE C 87 SHEET 1 AB9 4 PHE C 120 ASN C 122 0 SHEET 2 AB9 4 GLY C 256 LYS C 259 -1 O TYR C 257 N ASN C 121 SHEET 3 AB9 4 LYS C 176 HIS C 184 -1 N LEU C 177 O PHE C 258 SHEET 4 AB9 4 ARG C 229 VAL C 237 -1 O THR C 235 N TYR C 178 SHEET 1 AC1 2 LEU C 151 TRP C 153 0 SHEET 2 AC1 2 ILE C 252 PRO C 254 -1 O ALA C 253 N ASN C 152 SHEET 1 AC2 4 LEU C 164 PRO C 169 0 SHEET 2 AC2 4 ILE C 242 SER C 247 -1 O LEU C 243 N MET C 168 SHEET 3 AC2 4 ILE C 202 SER C 205 -1 N THR C 203 O ASN C 246 SHEET 4 AC2 4 GLN C 210 VAL C 213 -1 O GLN C 211 N VAL C 204 SHEET 1 AC3 2 GLY C 303 ALA C 304 0 SHEET 2 AC3 2 GLU F 61 LYS F 62 -1 O LYS F 62 N GLY C 303 SHEET 1 AC4 2 ALA E 130 ASP E 132 0 SHEET 2 AC4 2 PHE E 138 ILE E 140 -1 O LYS E 139 N GLU E 131 SHEET 1 AC5 3 CYS G 14 HIS G 17 0 SHEET 2 AC5 3 TYR I 22 ASN I 28 -1 O ARG I 25 N CYS G 14 SHEET 3 AC5 3 GLY I 31 ALA I 36 -1 O ALA I 35 N PHE I 24 SHEET 1 AC6 2 THR G 24 ILE G 25 0 SHEET 2 AC6 2 GLU G 35 VAL G 36 -1 O VAL G 36 N THR G 24 SHEET 1 AC7 2 ALA G 39 GLU G 41 0 SHEET 2 AC7 2 LYS G 315 ALA G 317 -1 O LEU G 316 N THR G 40 SHEET 1 AC8 3 VAL G 43 GLN G 44 0 SHEET 2 AC8 3 PHE G 294 GLN G 295 1 O PHE G 294 N GLN G 44 SHEET 3 AC8 3 ARG G 307 TYR G 308 1 O ARG G 307 N GLN G 295 SHEET 1 AC9 2 ILE G 51 CYS G 52 0 SHEET 2 AC9 2 ILE G 274 GLY G 275 1 O GLY G 275 N ILE G 51 SHEET 1 AD1 3 ILE G 58 LEU G 59 0 SHEET 2 AD1 3 LEU G 86 GLU G 89 1 O VAL G 88 N LEU G 59 SHEET 3 AD1 3 ILE G 267 ARG G 269 1 O MET G 268 N GLU G 89 SHEET 1 AD2 5 TYR G 100 ASP G 101 0 SHEET 2 AD2 5 ARG G 229 VAL G 237 1 O ILE G 230 N ASP G 101 SHEET 3 AD2 5 LYS G 176 HIS G 184 -1 N VAL G 182 O SER G 231 SHEET 4 AD2 5 GLY G 256 LYS G 259 -1 O PHE G 258 N LEU G 177 SHEET 5 AD2 5 PHE G 120 ASN G 122 -1 N ASN G 121 O TYR G 257 SHEET 1 AD3 5 TYR G 100 ASP G 101 0 SHEET 2 AD3 5 ARG G 229 VAL G 237 1 O ILE G 230 N ASP G 101 SHEET 3 AD3 5 LYS G 176 HIS G 184 -1 N VAL G 182 O SER G 231 SHEET 4 AD3 5 LEU G 251 ALA G 253 -1 O ILE G 252 N GLY G 181 SHEET 5 AD3 5 ASN G 152 TRP G 153 -1 N ASN G 152 O ALA G 253 SHEET 1 AD4 4 LEU G 164 PRO G 169 0 SHEET 2 AD4 4 ILE G 242 SER G 247 -1 O LEU G 243 N MET G 168 SHEET 3 AD4 4 ILE G 202 SER G 205 -1 N THR G 203 O ASN G 246 SHEET 4 AD4 4 GLN G 210 VAL G 213 -1 O GLN G 211 N VAL G 204 SHEET 1 AD5 2 GLY G 303 CYS G 305 0 SHEET 2 AD5 2 ASN I 60 LYS I 62 -1 O LYS I 62 N GLY G 303 SHEET 1 AD6 4 THR A 3 SER A 7 0 SHEET 2 AD6 4 LEU A 18 SER A 25 -1 O SER A 23 N LYS A 5 SHEET 3 AD6 4 HIS A 77 ILE A 82 -1 O ILE A 82 N LEU A 18 SHEET 4 AD6 4 LEU A 67 ASP A 72 -1 N THR A 68 O LYS A 81 SHEET 1 AD7 6 ILE A 11 LEU A 12 0 SHEET 2 AD7 6 THR A 107 VAL A 111 1 O THR A 110 N LEU A 12 SHEET 3 AD7 6 ALA A 88 ASN A 98 -1 N TYR A 90 O THR A 107 SHEET 4 AD7 6 MET A 34 GLN A 39 -1 N GLN A 39 O THR A 89 SHEET 5 AD7 6 GLU A 46 ILE A 51 -1 O LEU A 48 N TRP A 36 SHEET 6 AD7 6 GLU A 57 CYS A 59 -1 O TYR A 58 N HIS A 50 SHEET 1 AD8 4 ILE A 11 LEU A 12 0 SHEET 2 AD8 4 THR A 107 VAL A 111 1 O THR A 110 N LEU A 12 SHEET 3 AD8 4 ALA A 88 ASN A 98 -1 N TYR A 90 O THR A 107 SHEET 4 AD8 4 GLY A 100A ALA A 100C-1 O ALA A 100C N PHE A 96 SHEET 1 AD9 4 VAL D 4 THR D 5 0 SHEET 2 AD9 4 THR D 18 SER D 25 -1 O ARG D 24 N THR D 5 SHEET 3 AD9 4 LYS D 70 THR D 76 -1 O LEU D 73 N LEU D 21 SHEET 4 AD9 4 PHE D 62 ILE D 67 -1 N SER D 63 O THR D 74 SHEET 1 AE1 6 ALA D 9 THR D 13 0 SHEET 2 AE1 6 THR D 102 VAL D 106 1 O LYS D 103 N LEU D 11 SHEET 3 AE1 6 ALA D 84 TRP D 91 -1 N TYR D 86 O THR D 102 SHEET 4 AE1 6 ASN D 34 LYS D 38 -1 N ASN D 34 O ALA D 89 SHEET 5 AE1 6 PHE D 44 GLY D 49 -1 O LEU D 47 N TRP D 35 SHEET 6 AE1 6 ASN D 53 ARG D 54 -1 O ASN D 53 N GLY D 49 SHEET 1 AE2 4 ALA D 9 THR D 13 0 SHEET 2 AE2 4 THR D 102 VAL D 106 1 O LYS D 103 N LEU D 11 SHEET 3 AE2 4 ALA D 84 TRP D 91 -1 N TYR D 86 O THR D 102 SHEET 4 AE2 4 TYR D 96 PHE D 98 -1 O VAL D 97 N LEU D 90 SHEET 1 AE3 4 THR H 3 SER H 7 0 SHEET 2 AE3 4 THR H 17 SER H 25 -1 O SER H 23 N LYS H 5 SHEET 3 AE3 4 HIS H 77 ALA H 82A-1 O ILE H 78 N CYS H 22 SHEET 4 AE3 4 LEU H 67 ASP H 72 -1 N THR H 68 O LYS H 81 SHEET 1 AE4 6 ILE H 11 LEU H 12 0 SHEET 2 AE4 6 THR H 107 VAL H 111 1 O THR H 110 N LEU H 12 SHEET 3 AE4 6 ALA H 88 ASN H 98 -1 N TYR H 90 O THR H 107 SHEET 4 AE4 6 MET H 34 GLN H 39 -1 N GLN H 39 O THR H 89 SHEET 5 AE4 6 GLU H 46 TRP H 52 -1 O ALA H 49 N TRP H 36 SHEET 6 AE4 6 GLU H 57 CYS H 59 -1 O TYR H 58 N HIS H 50 SHEET 1 AE5 4 ILE H 11 LEU H 12 0 SHEET 2 AE5 4 THR H 107 VAL H 111 1 O THR H 110 N LEU H 12 SHEET 3 AE5 4 ALA H 88 ASN H 98 -1 N TYR H 90 O THR H 107 SHEET 4 AE5 4 GLY H 100A TRP H 103 -1 O ALA H 100C N PHE H 96 SHEET 1 AE6 4 VAL J 4 THR J 5 0 SHEET 2 AE6 4 VAL J 19 SER J 25 -1 O ARG J 24 N THR J 5 SHEET 3 AE6 4 LYS J 70 ILE J 75 -1 O LEU J 73 N LEU J 21 SHEET 4 AE6 4 PHE J 62 ILE J 67 -1 N SER J 63 O THR J 74 SHEET 1 AE7 6 ALA J 9 THR J 13 0 SHEET 2 AE7 6 THR J 102 VAL J 106 1 O LYS J 103 N LEU J 11 SHEET 3 AE7 6 ALA J 84 TRP J 91 -1 N TYR J 86 O THR J 102 SHEET 4 AE7 6 ASN J 34 LYS J 38 -1 N LYS J 38 O MET J 85 SHEET 5 AE7 6 PHE J 44 GLY J 49 -1 O LEU J 47 N TRP J 35 SHEET 6 AE7 6 ASN J 53 ARG J 54 -1 O ASN J 53 N GLY J 49 SHEET 1 AE8 4 ALA J 9 THR J 13 0 SHEET 2 AE8 4 THR J 102 VAL J 106 1 O LYS J 103 N LEU J 11 SHEET 3 AE8 4 ALA J 84 TRP J 91 -1 N TYR J 86 O THR J 102 SHEET 4 AE8 4 TYR J 96 PHE J 98 -1 O VAL J 97 N LEU J 90 SSBOND 1 CYS B 14 CYS E 137 1555 1555 2.03 SSBOND 2 CYS B 30 CYS F 47 1555 1555 2.03 SSBOND 3 CYS B 52 CYS B 277 1555 1555 2.03 SSBOND 4 CYS B 64 CYS B 76 1555 1555 2.03 SSBOND 5 CYS B 97 CYS B 139 1555 1555 2.03 SSBOND 6 CYS B 281 CYS B 305 1555 1555 2.03 SSBOND 7 CYS C 14 CYS F 137 1555 1555 2.03 SSBOND 8 CYS C 30 CYS I 47 1555 1555 2.03 SSBOND 9 CYS C 52 CYS C 277 1555 1555 2.03 SSBOND 10 CYS C 64 CYS C 76 1555 1555 2.03 SSBOND 11 CYS C 97 CYS C 139 1555 1555 2.03 SSBOND 12 CYS C 281 CYS C 305 1555 1555 2.03 SSBOND 13 CYS E 47 CYS G 30 1555 1555 2.04 SSBOND 14 CYS E 144 CYS E 148 1555 1555 2.03 SSBOND 15 CYS F 144 CYS F 148 1555 1555 2.02 SSBOND 16 CYS G 14 CYS I 137 1555 1555 2.03 SSBOND 17 CYS G 52 CYS G 277 1555 1555 2.03 SSBOND 18 CYS G 64 CYS G 76 1555 1555 2.03 SSBOND 19 CYS G 97 CYS G 139 1555 1555 2.03 SSBOND 20 CYS G 281 CYS G 305 1555 1555 2.03 SSBOND 21 CYS I 144 CYS I 148 1555 1555 2.03 LINK ND2 ASN B 8 C1 NAG M 1 1555 1555 1.45 LINK ND2 ASN B 22 C1 NAG B 403 1555 1555 1.44 LINK ND2 ASN B 38 C1 NAG B 404 1555 1555 1.46 LINK ND2 ASN B 63 C1 NAG B 405 1555 1555 1.44 LINK ND2 ASN B 133 C1 NAG B 402 1555 1555 1.44 LINK ND2 ASN B 165 C1 NAG L 1 1555 1555 1.44 LINK ND2 ASN B 246 C1 NAG K 1 1555 1555 1.45 LINK ND2 ASN B 285 C1 NAG B 401 1555 1555 1.44 LINK ND2 ASN C 22 C1 NAG C 403 1555 1555 1.44 LINK ND2 ASN C 38 C1 NAG C 404 1555 1555 1.45 LINK ND2 ASN C 63 C1 NAG C 405 1555 1555 1.44 LINK ND2 ASN C 126 C1 NAG C 406 1555 1555 1.45 LINK ND2 ASN C 133 C1 NAG C 402 1555 1555 1.44 LINK ND2 ASN C 165 C1 NAG O 1 1555 1555 1.44 LINK ND2 ASN C 246 C1 NAG N 1 1555 1555 1.45 LINK ND2 ASN C 285 C1 NAG C 401 1555 1555 1.44 LINK ND2 ASN E 154 C1 NAG E 301 1555 1555 1.46 LINK ND2 ASN F 154 C1 NAG F 301 1555 1555 1.46 LINK ND2 ASN G 22 C1 NAG G 403 1555 1555 1.44 LINK ND2 ASN G 38 C1 NAG G 404 1555 1555 1.44 LINK ND2 ASN G 63 C1 NAG G 405 1555 1555 1.44 LINK ND2 ASN G 126 C1 NAG G 406 1555 1555 1.44 LINK ND2 ASN G 133 C1 NAG G 402 1555 1555 1.44 LINK ND2 ASN G 165 C1 NAG Q 1 1555 1555 1.44 LINK ND2 ASN G 246 C1 NAG P 1 1555 1555 1.45 LINK ND2 ASN G 285 C1 NAG G 401 1555 1555 1.44 LINK ND2 ASN I 154 C1 NAG I 301 1555 1555 1.45 LINK O4 NAG K 1 C1 NAG K 2 1555 1555 1.44 LINK O4 NAG L 1 C1 NAG L 2 1555 1555 1.44 LINK O4 NAG L 2 C1 BMA L 3 1555 1555 1.45 LINK O4 NAG M 1 C1 NAG M 2 1555 1555 1.44 LINK O4 NAG N 1 C1 NAG N 2 1555 1555 1.44 LINK O4 NAG O 1 C1 NAG O 2 1555 1555 1.44 LINK O4 NAG O 2 C1 BMA O 3 1555 1555 1.45 LINK O4 NAG P 1 C1 NAG P 2 1555 1555 1.44 LINK O4 NAG Q 1 C1 NAG Q 2 1555 1555 1.44 LINK O4 NAG Q 2 C1 BMA Q 3 1555 1555 1.44 CISPEP 1 TYR F 141 HIS F 142 0 7.19 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