HEADER DE NOVO PROTEIN 24-FEB-25 9NH7 TITLE CRYOEM STRUCTURE OF DE NOVO VHH, VHH_FLU_01, BOUND TO INFLUENZA HA, TITLE 2 STRAIN A/USA:IOWA/1943 H1N1. COMPND MOL_ID: 1; COMPND 2 MOLECULE: VHH_FLU_01; COMPND 3 CHAIN: E, F; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: HEMAGGLUTININ HA1 CHAIN; COMPND 7 CHAIN: A, B, C; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: HEMAGGLUTININ HA2 CHAIN; COMPND 11 CHAIN: G, H, I; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT; SOURCE 3 ORGANISM_TAXID: 32630; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS (STRAIN A/USA:IOWA/1943 SOURCE 8 H1N1); SOURCE 9 ORGANISM_TAXID: 425563; SOURCE 10 STRAIN: A/USA:IOWA/1943 H1N1; SOURCE 11 GENE: HA; 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 (STRAIN A/USA:IOWA/1943 SOURCE 17 H1N1); SOURCE 18 ORGANISM_TAXID: 425563; SOURCE 19 STRAIN: A/USA:IOWA/1943 H1N1; SOURCE 20 GENE: HA; SOURCE 21 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 22 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 23 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS INFLUENZA, FLU, HA, HEMAGGLUTININ, H1N1, ANTIBODY, DE NOVO, PROTEIN KEYWDS 2 DESIGN, VHH_FLU_01, DE NOVO ANTIBODY, DE NOVO PROTEIN, RFDIFFUSION, KEYWDS 3 RFANTIBODY EXPDTA ELECTRON MICROSCOPY AUTHOR A.J.BORST,C.WEIDLE REVDAT 1 12-NOV-25 9NH7 0 JRNL AUTH N.R.BENNETT,J.L.WATSON,R.J.RAGOTTE,A.J.BORST,D.L.SEE, JRNL AUTH 2 C.WEIDLE,R.BISWAS,Y.YU,E.L.SHROCK,R.AULT,P.J.Y.LEUNG, JRNL AUTH 3 B.HUANG,I.GORESHNIK,J.TAM,K.D.CARR,B.SINGER,C.CRISWELL, JRNL AUTH 4 B.I.M.WICKY,D.VAFEADOS,M.G.SANCHEZ,H.M.KIM,S.T.TORRES, JRNL AUTH 5 S.CHAN,S.M.SUN,T.SPEAR,Y.SUN,K.O'REILLY,J.M.MARIS, JRNL AUTH 6 N.G.SGOURAKIS,R.A.MELNYK,C.C.LIU,D.BAKER JRNL TITL ATOMICALLY ACCURATE DE NOVO DESIGN OF ANTIBODIES WITH JRNL TITL 2 RFDIFFUSION JRNL REF NATURE 2025 JRNL REFN ESSN 1476-4687 JRNL DOI 10.1038/S41586-025-09721-5 REMARK 2 REMARK 2 RESOLUTION. 3.02 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : CRYOSPARC, SERIALEM, CRYOSPARC, UCSF REMARK 3 CHIMERA, CRYOSPARC, CRYOSPARC, REMARK 3 CRYOSPARC, CRYOSPARC, PHENIX, PYMOL, REMARK 3 COOT, ISOLDE, UCSF CHIMERAX REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : 8SK7 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) : 3.020 REMARK 3 NUMBER OF PARTICLES : 288441 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 9NH7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-FEB-25. REMARK 100 THE DEPOSITION ID IS D_1000293317. 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 : DE NOVO VHH, VHH_FLU_01, BOUND REMARK 245 TO INFLUENZA HA, STRAIN A/USA: REMARK 245 IOWA/1943 H1N1. REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 0.30 REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.50 REMARK 245 SAMPLE DETAILS : INFLUENZA HA, STRAIN REMARK 245 A/USA:IOWA/1943 H1N1 WAS EXPRESSED AND PURIFIED. VHH_FLU_01 WAS REMARK 245 EXPRESSED AND PURIFIED. VHH_FLU_01 WAS MIXED WITH INFLUENZA HA, REMARK 245 STRAIN A/USA:IOWA/1943 H1N1 AT A 3:1 MOLAR RATIO. REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : 16954 REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : TFS KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 (6K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 800.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 1800.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : 2.70 REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 5300.00 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : 105000 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: OCTAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, A, B, C, F, G, H, I, D, J, REMARK 350 AND CHAINS: K, L, M, N REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 MET E -2 REMARK 465 SER E -1 REMARK 465 GLY E 0 REMARK 465 GLN E 1 REMARK 465 GLY E 8 REMARK 465 GLY E 9 REMARK 465 GLY E 10 REMARK 465 LEU E 11 REMARK 465 PRO E 41 REMARK 465 GLY E 42 REMARK 465 GLN E 43 REMARK 465 ASN E 84 REMARK 465 SER E 85 REMARK 465 LEU E 86 REMARK 465 ARG E 87 REMARK 465 ALA E 88 REMARK 465 GLU E 89 REMARK 465 ASP E 90 REMARK 465 THR E 91 REMARK 465 ALA E 92 REMARK 465 LEU E 117 REMARK 465 VAL E 118 REMARK 465 THR E 119 REMARK 465 VAL E 120 REMARK 465 SER E 121 REMARK 465 GLY E 122 REMARK 465 SER E 123 REMARK 465 GLY E 124 REMARK 465 SER E 125 REMARK 465 HIS E 126 REMARK 465 HIS E 127 REMARK 465 TRP E 128 REMARK 465 GLY E 129 REMARK 465 SER E 130 REMARK 465 THR E 131 REMARK 465 HIS E 132 REMARK 465 HIS E 133 REMARK 465 HIS E 134 REMARK 465 HIS E 135 REMARK 465 HIS E 136 REMARK 465 HIS E 137 REMARK 465 MET F -2 REMARK 465 SER F -1 REMARK 465 GLY F 0 REMARK 465 GLN F 1 REMARK 465 GLY F 8 REMARK 465 GLY F 9 REMARK 465 GLY F 10 REMARK 465 LEU F 11 REMARK 465 PRO F 41 REMARK 465 GLY F 42 REMARK 465 GLN F 43 REMARK 465 ASN F 84 REMARK 465 SER F 85 REMARK 465 LEU F 86 REMARK 465 ARG F 87 REMARK 465 ALA F 88 REMARK 465 GLU F 89 REMARK 465 ASP F 90 REMARK 465 THR F 91 REMARK 465 ALA F 92 REMARK 465 LEU F 117 REMARK 465 VAL F 118 REMARK 465 THR F 119 REMARK 465 VAL F 120 REMARK 465 SER F 121 REMARK 465 GLY F 122 REMARK 465 SER F 123 REMARK 465 GLY F 124 REMARK 465 SER F 125 REMARK 465 HIS F 126 REMARK 465 HIS F 127 REMARK 465 TRP F 128 REMARK 465 GLY F 129 REMARK 465 SER F 130 REMARK 465 THR F 131 REMARK 465 HIS F 132 REMARK 465 HIS F 133 REMARK 465 HIS F 134 REMARK 465 HIS F 135 REMARK 465 HIS F 136 REMARK 465 HIS F 137 REMARK 465 SER G -4 REMARK 465 ILE G -3 REMARK 465 GLN G -2 REMARK 465 SER G -1 REMARK 465 ARG G 0 REMARK 465 GLY G 1 REMARK 465 LEU G 2 REMARK 465 PHE G 3 REMARK 465 GLY G 4 REMARK 465 ALA G 5 REMARK 465 ILE G 6 REMARK 465 ALA G 7 REMARK 465 GLY G 8 REMARK 465 ASP G 174 REMARK 465 GLY G 175 REMARK 465 SER G 176 REMARK 465 GLY G 177 REMARK 465 TYR G 178 REMARK 465 ILE G 179 REMARK 465 PRO G 180 REMARK 465 GLU G 181 REMARK 465 ALA G 182 REMARK 465 PRO G 183 REMARK 465 ARG G 184 REMARK 465 ASP G 185 REMARK 465 GLY G 186 REMARK 465 GLN G 187 REMARK 465 ALA G 188 REMARK 465 TYR G 189 REMARK 465 VAL G 190 REMARK 465 ARG G 191 REMARK 465 LYS G 192 REMARK 465 ASP G 193 REMARK 465 GLY G 194 REMARK 465 GLU G 195 REMARK 465 TRP G 196 REMARK 465 VAL G 197 REMARK 465 LEU G 198 REMARK 465 LEU G 199 REMARK 465 SER G 200 REMARK 465 THR G 201 REMARK 465 PHE G 202 REMARK 465 LEU G 203 REMARK 465 GLY G 204 REMARK 465 SER G 205 REMARK 465 GLY G 206 REMARK 465 LEU G 207 REMARK 465 ASN G 208 REMARK 465 ASP G 209 REMARK 465 ILE G 210 REMARK 465 PHE G 211 REMARK 465 GLU G 212 REMARK 465 ALA G 213 REMARK 465 GLN G 214 REMARK 465 LYS G 215 REMARK 465 ILE G 216 REMARK 465 GLU G 217 REMARK 465 TRP G 218 REMARK 465 HIS G 219 REMARK 465 GLU G 220 REMARK 465 GLY G 221 REMARK 465 HIS G 222 REMARK 465 HIS G 223 REMARK 465 HIS G 224 REMARK 465 HIS G 225 REMARK 465 HIS G 226 REMARK 465 HIS G 227 REMARK 465 SER H -4 REMARK 465 ILE H -3 REMARK 465 GLN H -2 REMARK 465 SER H -1 REMARK 465 ARG H 0 REMARK 465 GLY H 1 REMARK 465 LEU H 2 REMARK 465 PHE H 3 REMARK 465 GLY H 4 REMARK 465 ALA H 5 REMARK 465 ILE H 6 REMARK 465 ALA H 7 REMARK 465 GLY H 8 REMARK 465 ASP H 174 REMARK 465 GLY H 175 REMARK 465 SER H 176 REMARK 465 GLY H 177 REMARK 465 TYR H 178 REMARK 465 ILE H 179 REMARK 465 PRO H 180 REMARK 465 GLU H 181 REMARK 465 ALA H 182 REMARK 465 PRO H 183 REMARK 465 ARG H 184 REMARK 465 ASP H 185 REMARK 465 GLY H 186 REMARK 465 GLN H 187 REMARK 465 ALA H 188 REMARK 465 TYR H 189 REMARK 465 VAL H 190 REMARK 465 ARG H 191 REMARK 465 LYS H 192 REMARK 465 ASP H 193 REMARK 465 GLY H 194 REMARK 465 GLU H 195 REMARK 465 TRP H 196 REMARK 465 VAL H 197 REMARK 465 LEU H 198 REMARK 465 LEU H 199 REMARK 465 SER H 200 REMARK 465 THR H 201 REMARK 465 PHE H 202 REMARK 465 LEU H 203 REMARK 465 GLY H 204 REMARK 465 SER H 205 REMARK 465 GLY H 206 REMARK 465 LEU H 207 REMARK 465 ASN H 208 REMARK 465 ASP H 209 REMARK 465 ILE H 210 REMARK 465 PHE H 211 REMARK 465 GLU H 212 REMARK 465 ALA H 213 REMARK 465 GLN H 214 REMARK 465 LYS H 215 REMARK 465 ILE H 216 REMARK 465 GLU H 217 REMARK 465 TRP H 218 REMARK 465 HIS H 219 REMARK 465 GLU H 220 REMARK 465 GLY H 221 REMARK 465 HIS H 222 REMARK 465 HIS H 223 REMARK 465 HIS H 224 REMARK 465 HIS H 225 REMARK 465 HIS H 226 REMARK 465 HIS H 227 REMARK 465 SER I -4 REMARK 465 ILE I -3 REMARK 465 GLN I -2 REMARK 465 SER I -1 REMARK 465 ARG I 0 REMARK 465 GLY I 1 REMARK 465 LEU I 2 REMARK 465 PHE I 3 REMARK 465 GLY I 4 REMARK 465 ALA I 5 REMARK 465 ILE I 6 REMARK 465 ALA I 7 REMARK 465 GLY I 8 REMARK 465 ASP I 174 REMARK 465 GLY I 175 REMARK 465 SER I 176 REMARK 465 GLY I 177 REMARK 465 TYR I 178 REMARK 465 ILE I 179 REMARK 465 PRO I 180 REMARK 465 GLU I 181 REMARK 465 ALA I 182 REMARK 465 PRO I 183 REMARK 465 ARG I 184 REMARK 465 ASP I 185 REMARK 465 GLY I 186 REMARK 465 GLN I 187 REMARK 465 ALA I 188 REMARK 465 TYR I 189 REMARK 465 VAL I 190 REMARK 465 ARG I 191 REMARK 465 LYS I 192 REMARK 465 ASP I 193 REMARK 465 GLY I 194 REMARK 465 GLU I 195 REMARK 465 TRP I 196 REMARK 465 VAL I 197 REMARK 465 LEU I 198 REMARK 465 LEU I 199 REMARK 465 SER I 200 REMARK 465 THR I 201 REMARK 465 PHE I 202 REMARK 465 LEU I 203 REMARK 465 GLY I 204 REMARK 465 SER I 205 REMARK 465 GLY I 206 REMARK 465 LEU I 207 REMARK 465 ASN I 208 REMARK 465 ASP I 209 REMARK 465 ILE I 210 REMARK 465 PHE I 211 REMARK 465 GLU I 212 REMARK 465 ALA I 213 REMARK 465 GLN I 214 REMARK 465 LYS I 215 REMARK 465 ILE I 216 REMARK 465 GLU I 217 REMARK 465 TRP I 218 REMARK 465 HIS I 219 REMARK 465 GLU I 220 REMARK 465 GLY I 221 REMARK 465 HIS I 222 REMARK 465 HIS I 223 REMARK 465 HIS I 224 REMARK 465 HIS I 225 REMARK 465 HIS I 226 REMARK 465 HIS I 227 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 VAL E 2 CG1 CG2 REMARK 470 GLN E 3 CG CD OE1 NE2 REMARK 470 LEU E 4 CG CD1 CD2 REMARK 470 VAL E 5 CG1 CG2 REMARK 470 GLU E 6 CG CD OE1 OE2 REMARK 470 SER E 7 OG REMARK 470 VAL E 12 CG1 CG2 REMARK 470 GLN E 13 CG CD OE1 NE2 REMARK 470 PRO E 14 CG CD REMARK 470 SER E 17 OG REMARK 470 LEU E 18 CG CD1 CD2 REMARK 470 ARG E 19 CG CD NE CZ NH1 NH2 REMARK 470 LEU E 20 CG CD1 CD2 REMARK 470 SER E 21 OG REMARK 470 CYS E 22 SG REMARK 470 SER E 25 OG REMARK 470 LYS E 27 CG CD CE NZ REMARK 470 TYR E 28 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 VAL E 29 CG1 CG2 REMARK 470 ASN E 30 CG OD1 ND2 REMARK 470 LEU E 31 CG CD1 CD2 REMARK 470 MET E 32 CG SD CE REMARK 470 SER E 33 OG REMARK 470 LEU E 34 CG CD1 CD2 REMARK 470 TRP E 36 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP E 36 CZ3 CH2 REMARK 470 PHE E 37 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ARG E 38 CG CD NE CZ NH1 NH2 REMARK 470 GLN E 39 CG CD OE1 NE2 REMARK 470 LEU E 45 CG CD1 CD2 REMARK 470 GLU E 46 CG CD OE1 OE2 REMARK 470 VAL E 48 CG1 CG2 REMARK 470 ILE E 51 CG1 CG2 CD1 REMARK 470 SER E 52 OG REMARK 470 PHE E 53 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ASP E 54 CG OD1 OD2 REMARK 470 LYS E 56 CG CD CE NZ REMARK 470 LYS E 57 CG CD CE NZ REMARK 470 THR E 58 OG1 CG2 REMARK 470 TYR E 59 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 TYR E 60 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ASP E 62 CG OD1 OD2 REMARK 470 SER E 63 OG REMARK 470 VAL E 64 CG1 CG2 REMARK 470 LYS E 65 CG CD CE NZ REMARK 470 ARG E 67 CG CD NE CZ NH1 NH2 REMARK 470 PHE E 68 CG CD1 CD2 CE1 CE2 CZ REMARK 470 THR E 69 OG1 CG2 REMARK 470 ILE E 70 CG1 CG2 CD1 REMARK 470 SER E 71 OG REMARK 470 ARG E 72 CG CD NE CZ NH1 NH2 REMARK 470 ASP E 73 CG OD1 OD2 REMARK 470 ASN E 74 CG OD1 ND2 REMARK 470 SER E 75 OG REMARK 470 LYS E 76 CG CD CE NZ REMARK 470 ASN E 77 CG OD1 ND2 REMARK 470 THR E 78 OG1 CG2 REMARK 470 LEU E 79 CG CD1 CD2 REMARK 470 TYR E 80 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LEU E 81 CG CD1 CD2 REMARK 470 GLN E 82 CG CD OE1 NE2 REMARK 470 MET E 83 CG SD CE REMARK 470 VAL E 93 CG1 CG2 REMARK 470 TYR E 94 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 TYR E 95 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 CYS E 96 SG REMARK 470 SER E 99 OG REMARK 470 VAL E 100 CG1 CG2 REMARK 470 VAL E 101 CG1 CG2 REMARK 470 ASP E 102 CG OD1 OD2 REMARK 470 SER E 103 OG REMARK 470 LEU E 104 CG CD1 CD2 REMARK 470 VAL E 106 CG1 CG2 REMARK 470 PHE E 108 CG CD1 CD2 CE1 CE2 CZ REMARK 470 TYR E 109 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 SER E 110 OG REMARK 470 TYR E 111 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 TRP E 112 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP E 112 CZ3 CH2 REMARK 470 GLN E 114 CG CD OE1 NE2 REMARK 470 THR E 116 OG1 CG2 REMARK 470 CYS A 52 SG REMARK 470 ASP A 104 CG OD1 OD2 REMARK 470 ASP A 164 CG OD1 OD2 REMARK 470 GLU A 204 CG CD OE1 OE2 REMARK 470 GLU A 283 CG CD OE1 OE2 REMARK 470 CYS A 284 SG REMARK 470 GLU A 311 CG CD OE1 OE2 REMARK 470 CYS B 52 SG REMARK 470 GLU B 96 CG CD OE1 OE2 REMARK 470 ASP B 104 CG OD1 OD2 REMARK 470 ASP B 164 CG OD1 OD2 REMARK 470 GLU B 204 CG CD OE1 OE2 REMARK 470 GLU B 283 CG CD OE1 OE2 REMARK 470 CYS B 284 SG REMARK 470 GLU B 311 CG CD OE1 OE2 REMARK 470 CYS C 52 SG REMARK 470 GLU C 96 CG CD OE1 OE2 REMARK 470 ASP C 104 CG OD1 OD2 REMARK 470 ASP C 164 CG OD1 OD2 REMARK 470 GLU C 204 CG CD OE1 OE2 REMARK 470 GLU C 283 CG CD OE1 OE2 REMARK 470 CYS C 284 SG REMARK 470 GLU C 311 CG CD OE1 OE2 REMARK 470 GLN F 3 CG CD OE1 NE2 REMARK 470 LEU F 4 CG CD1 CD2 REMARK 470 VAL F 12 CG1 CG2 REMARK 470 GLN F 13 CG CD OE1 NE2 REMARK 470 ARG F 38 CG CD NE CZ NH1 NH2 REMARK 470 GLU F 46 CG CD OE1 OE2 REMARK 470 ASP F 62 CG OD1 OD2 REMARK 470 SER F 63 OG REMARK 470 VAL F 64 CG1 CG2 REMARK 470 ARG F 72 CG CD NE CZ NH1 NH2 REMARK 470 LYS F 76 CG CD CE NZ REMARK 470 MET F 83 CG SD CE REMARK 470 GLN F 114 CG CD OE1 NE2 REMARK 470 PHE G 9 CG CD1 CD2 CE1 CE2 CZ REMARK 470 GLU G 11 CG CD OE1 OE2 REMARK 470 GLU G 29 CG CD OE1 OE2 REMARK 470 LYS G 39 CG CD CE NZ REMARK 470 LYS G 131 CG CD CE NZ REMARK 470 GLU G 147 CG CD OE1 OE2 REMARK 470 GLU G 150 CG CD OE1 OE2 REMARK 470 LYS G 153 CG CD CE NZ REMARK 470 GLU G 164 CG CD OE1 OE2 REMARK 470 GLU G 165 CG CD OE1 OE2 REMARK 470 LYS G 167 CG CD CE NZ REMARK 470 LEU G 168 CG CD1 CD2 REMARK 470 GLU G 171 CG CD OE1 OE2 REMARK 470 LYS G 172 CG CD CE NZ REMARK 470 ILE G 173 CG1 CG2 CD1 REMARK 470 PHE H 9 CG CD1 CD2 CE1 CE2 CZ REMARK 470 GLU H 11 CG CD OE1 OE2 REMARK 470 ASP H 19 CG OD1 OD2 REMARK 470 GLU H 29 CG CD OE1 OE2 REMARK 470 LYS H 39 CG CD CE NZ REMARK 470 LYS H 131 CG CD CE NZ REMARK 470 GLU H 147 CG CD OE1 OE2 REMARK 470 GLU H 150 CG CD OE1 OE2 REMARK 470 GLU H 164 CG CD OE1 OE2 REMARK 470 GLU H 165 CG CD OE1 OE2 REMARK 470 LYS H 167 CG CD CE NZ REMARK 470 LEU H 168 CG CD1 CD2 REMARK 470 GLU H 171 CG CD OE1 OE2 REMARK 470 LYS H 172 CG CD CE NZ REMARK 470 ILE H 173 CG1 CG2 CD1 REMARK 470 PHE I 9 CG CD1 CD2 CE1 CE2 CZ REMARK 470 GLU I 11 CG CD OE1 OE2 REMARK 470 ASP I 19 CG OD1 OD2 REMARK 470 GLU I 29 CG CD OE1 OE2 REMARK 470 LYS I 131 CG CD CE NZ REMARK 470 GLU I 147 CG CD OE1 OE2 REMARK 470 GLU I 150 CG CD OE1 OE2 REMARK 470 GLU I 164 CG CD OE1 OE2 REMARK 470 GLU I 165 CG CD OE1 OE2 REMARK 470 LYS I 167 CG CD CE NZ REMARK 470 LEU I 168 CG CD1 CD2 REMARK 470 GLU I 171 CG CD OE1 OE2 REMARK 470 LYS I 172 CG CD CE NZ REMARK 470 ILE I 173 CG1 CG2 CD1 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 ND2 ASN B 33 H1 NAG B 404 1.46 REMARK 500 O ILE C 71 HD21 ASN C 156 1.54 REMARK 500 HH TYR B 154 OH TYR B 238 1.55 REMARK 500 HH TYR A 154 OH TYR A 238 1.56 REMARK 500 OD2 ASP A 11 H CYS G 144 1.56 REMARK 500 OE1 GLU C 181 HH21 ARG C 268 1.57 REMARK 500 OH TYR G 119 OE2 GLU G 132 2.10 REMARK 500 NH1 ARG A 317 OD1 ASP G 90 2.10 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 CYS C 14 CA - CB - SG ANGL. DEV. = 8.2 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 PRO E 14 49.02 -75.68 REMARK 500 TYR E 28 50.25 35.36 REMARK 500 ASP E 54 19.35 56.64 REMARK 500 GLU A 162 156.95 -48.31 REMARK 500 TYR A 167 75.94 -154.73 REMARK 500 ASN A 171 11.11 -142.70 REMARK 500 TRP A 186 -158.94 -150.22 REMARK 500 PRO A 191 175.91 -57.32 REMARK 500 ALA A 224 147.84 -174.41 REMARK 500 ASN B 21 56.67 -95.89 REMARK 500 ASN B 66 -168.36 -119.00 REMARK 500 ASN B 94 33.06 -97.25 REMARK 500 TRP B 261 -51.28 -120.81 REMARK 500 ASN B 303 36.82 -142.96 REMARK 500 ASP C 45 14.89 -141.46 REMARK 500 GLU C 96 -16.11 -140.85 REMARK 500 TRP C 133 77.32 -110.80 REMARK 500 PRO C 191 172.66 -54.70 REMARK 500 ARG C 230 12.19 59.04 REMARK 500 ILE C 330 72.23 -150.49 REMARK 500 TYR F 28 56.87 31.09 REMARK 500 VAL F 48 -54.77 -129.46 REMARK 500 ASP F 54 15.76 59.02 REMARK 500 PHE F 68 64.42 64.19 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-49405 RELATED DB: EMDB REMARK 900 CRYOEM STRUCTURE OF DE NOVO VHH, VHH_FLU_01, BOUND TO INFLUENZA HA, REMARK 900 STRAIN A/USA:IOWA/1943 H1N1. DBREF 9NH7 E -2 137 PDB 9NH7 9NH7 -2 137 DBREF 9NH7 A 11 331 UNP A4GCK8 HEMA_I43A0 18 338 DBREF 9NH7 B 11 331 UNP A4GCK8 HEMA_I43A0 18 338 DBREF 9NH7 C 11 331 UNP A4GCK8 HEMA_I43A0 18 338 DBREF 9NH7 F -2 137 PDB 9NH7 9NH7 -2 137 DBREF 9NH7 G -4 175 UNP A4GCK8 HEMA_I43A0 339 518 DBREF 9NH7 H -4 175 UNP A4GCK8 HEMA_I43A0 339 518 DBREF 9NH7 I -4 175 UNP A4GCK8 HEMA_I43A0 339 518 SEQADV 9NH7 PHE A 101 UNP A4GCK8 TYR 108 CONFLICT SEQADV 9NH7 ILE A 307 UNP A4GCK8 VAL 314 CONFLICT SEQADV 9NH7 PHE B 101 UNP A4GCK8 TYR 108 CONFLICT SEQADV 9NH7 ILE B 307 UNP A4GCK8 VAL 314 CONFLICT SEQADV 9NH7 PHE C 101 UNP A4GCK8 TYR 108 CONFLICT SEQADV 9NH7 ILE C 307 UNP A4GCK8 VAL 314 CONFLICT SEQADV 9NH7 TRP G 26 UNP A4GCK8 HIS 369 CONFLICT SEQADV 9NH7 ILE G 51 UNP A4GCK8 LYS 394 CONFLICT SEQADV 9NH7 ILE G 103 UNP A4GCK8 GLU 446 CONFLICT SEQADV 9NH7 SER G 176 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 GLY G 177 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 TYR G 178 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 ILE G 179 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 PRO G 180 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 GLU G 181 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 ALA G 182 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 PRO G 183 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 ARG G 184 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 ASP G 185 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 GLY G 186 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 GLN G 187 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 ALA G 188 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 TYR G 189 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 VAL G 190 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 ARG G 191 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 LYS G 192 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 ASP G 193 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 GLY G 194 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 GLU G 195 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 TRP G 196 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 VAL G 197 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 LEU G 198 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 LEU G 199 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 SER G 200 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 THR G 201 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 PHE G 202 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 LEU G 203 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 GLY G 204 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 SER G 205 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 GLY G 206 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 LEU G 207 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 ASN G 208 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 ASP G 209 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 ILE G 210 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 PHE G 211 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 GLU G 212 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 ALA G 213 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 GLN G 214 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 LYS G 215 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 ILE G 216 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 GLU G 217 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 TRP G 218 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 HIS G 219 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 GLU G 220 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 GLY G 221 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 HIS G 222 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 HIS G 223 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 HIS G 224 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 HIS G 225 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 HIS G 226 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 HIS G 227 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 TRP H 26 UNP A4GCK8 HIS 369 CONFLICT SEQADV 9NH7 ILE H 51 UNP A4GCK8 LYS 394 CONFLICT SEQADV 9NH7 ILE H 103 UNP A4GCK8 GLU 446 CONFLICT SEQADV 9NH7 SER H 176 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 GLY H 177 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 TYR H 178 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 ILE H 179 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 PRO H 180 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 GLU H 181 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 ALA H 182 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 PRO H 183 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 ARG H 184 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 ASP H 185 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 GLY H 186 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 GLN H 187 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 ALA H 188 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 TYR H 189 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 VAL H 190 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 ARG H 191 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 LYS H 192 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 ASP H 193 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 GLY H 194 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 GLU H 195 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 TRP H 196 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 VAL H 197 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 LEU H 198 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 LEU H 199 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 SER H 200 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 THR H 201 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 PHE H 202 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 LEU H 203 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 GLY H 204 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 SER H 205 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 GLY H 206 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 LEU H 207 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 ASN H 208 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 ASP H 209 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 ILE H 210 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 PHE H 211 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 GLU H 212 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 ALA H 213 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 GLN H 214 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 LYS H 215 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 ILE H 216 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 GLU H 217 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 TRP H 218 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 HIS H 219 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 GLU H 220 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 GLY H 221 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 HIS H 222 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 HIS H 223 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 HIS H 224 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 HIS H 225 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 HIS H 226 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 HIS H 227 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 TRP I 26 UNP A4GCK8 HIS 369 CONFLICT SEQADV 9NH7 ILE I 51 UNP A4GCK8 LYS 394 CONFLICT SEQADV 9NH7 ILE I 103 UNP A4GCK8 GLU 446 CONFLICT SEQADV 9NH7 SER I 176 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 GLY I 177 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 TYR I 178 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 ILE I 179 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 PRO I 180 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 GLU I 181 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 ALA I 182 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 PRO I 183 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 ARG I 184 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 ASP I 185 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 GLY I 186 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 GLN I 187 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 ALA I 188 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 TYR I 189 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 VAL I 190 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 ARG I 191 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 LYS I 192 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 ASP I 193 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 GLY I 194 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 GLU I 195 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 TRP I 196 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 VAL I 197 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 LEU I 198 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 LEU I 199 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 SER I 200 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 THR I 201 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 PHE I 202 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 LEU I 203 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 GLY I 204 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 SER I 205 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 GLY I 206 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 LEU I 207 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 ASN I 208 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 ASP I 209 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 ILE I 210 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 PHE I 211 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 GLU I 212 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 ALA I 213 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 GLN I 214 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 LYS I 215 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 ILE I 216 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 GLU I 217 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 TRP I 218 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 HIS I 219 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 GLU I 220 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 GLY I 221 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 HIS I 222 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 HIS I 223 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 HIS I 224 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 HIS I 225 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 HIS I 226 UNP A4GCK8 EXPRESSION TAG SEQADV 9NH7 HIS I 227 UNP A4GCK8 EXPRESSION TAG SEQRES 1 E 140 MET SER GLY GLN VAL GLN LEU VAL GLU SER GLY GLY GLY SEQRES 2 E 140 LEU VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA SEQRES 3 E 140 ALA SER GLY LYS TYR VAL ASN LEU MET SER LEU GLY TRP SEQRES 4 E 140 PHE ARG GLN ALA PRO GLY GLN GLY LEU GLU ALA VAL ALA SEQRES 5 E 140 ALA ILE SER PHE ASP GLY LYS LYS THR TYR TYR ALA ASP SEQRES 6 E 140 SER VAL LYS GLY ARG PHE THR ILE SER ARG ASP ASN SER SEQRES 7 E 140 LYS ASN THR LEU TYR LEU GLN MET ASN SER LEU ARG ALA SEQRES 8 E 140 GLU ASP THR ALA VAL TYR TYR CYS ALA ALA SER VAL VAL SEQRES 9 E 140 ASP SER LEU GLY VAL GLY PHE TYR SER TYR TRP GLY GLN SEQRES 10 E 140 GLY THR LEU VAL THR VAL SER GLY SER GLY SER HIS HIS SEQRES 11 E 140 TRP GLY SER THR HIS HIS HIS HIS HIS HIS SEQRES 1 A 321 ASP THR ILE CYS ILE GLY TYR HIS ALA ASN ASN SER THR SEQRES 2 A 321 ASP THR VAL ASP THR VAL LEU GLU LYS ASN VAL THR VAL SEQRES 3 A 321 THR HIS SER VAL ASN LEU LEU GLU ASP SER HIS ASN GLY SEQRES 4 A 321 LYS LEU CYS ARG LEU LYS GLY ILE ALA PRO LEU GLN LEU SEQRES 5 A 321 GLY LYS CYS ASN ILE ALA GLY TRP ILE LEU GLY ASN PRO SEQRES 6 A 321 GLU CYS GLU SER LEU LEU SER GLU ARG SER TRP SER TYR SEQRES 7 A 321 ILE VAL GLU THR PRO ASN SER GLU ASN GLY THR CYS PHE SEQRES 8 A 321 PRO GLY ASP PHE ILE ASP TYR GLU GLU LEU ARG GLU GLN SEQRES 9 A 321 LEU SER SER VAL SER SER PHE GLU ARG PHE GLU ILE PHE SEQRES 10 A 321 SER LYS GLU SER SER TRP PRO LYS HIS THR THR GLY GLY SEQRES 11 A 321 VAL THR ALA ALA CYS SER HIS ALA GLY LYS SER SER PHE SEQRES 12 A 321 TYR ARG ASN LEU LEU TRP LEU THR GLU LYS ASP GLY SER SEQRES 13 A 321 TYR PRO ASN LEU ASN ASN SER TYR VAL ASN LYS LYS GLY SEQRES 14 A 321 LYS GLU VAL LEU VAL LEU TRP GLY VAL HIS HIS PRO SER SEQRES 15 A 321 ASN ILE LYS ASP GLN GLN THR LEU TYR GLN LYS GLU ASN SEQRES 16 A 321 ALA TYR VAL SER VAL VAL SER SER ASN TYR ASN ARG ARG SEQRES 17 A 321 PHE THR PRO GLU ILE ALA GLU ARG PRO LYS VAL ARG GLY SEQRES 18 A 321 GLN ALA GLY ARG ILE ASN TYR TYR TRP THR LEU LEU LYS SEQRES 19 A 321 PRO GLY ASP THR ILE MET PHE GLU ALA ASN GLY ASN LEU SEQRES 20 A 321 ILE ALA PRO TRP TYR ALA PHE ALA LEU SER ARG GLY PHE SEQRES 21 A 321 GLY SER GLY ILE ILE THR SER ASN ALA SER MET HIS GLU SEQRES 22 A 321 CYS ASP THR LYS CYS GLN THR PRO GLN GLY ALA ILE ASN SEQRES 23 A 321 SER SER LEU PRO PHE GLN ASN ILE HIS PRO ILE THR ILE SEQRES 24 A 321 GLY GLU CYS PRO LYS TYR VAL ARG SER THR LYS LEU ARG SEQRES 25 A 321 MET VAL THR GLY LEU ARG ASN ILE PRO SEQRES 1 B 321 ASP THR ILE CYS ILE GLY TYR HIS ALA ASN ASN SER THR SEQRES 2 B 321 ASP THR VAL ASP THR VAL LEU GLU LYS ASN VAL THR VAL SEQRES 3 B 321 THR HIS SER VAL ASN LEU LEU GLU ASP SER HIS ASN GLY SEQRES 4 B 321 LYS LEU CYS ARG LEU LYS GLY ILE ALA PRO LEU GLN LEU SEQRES 5 B 321 GLY LYS CYS ASN ILE ALA GLY TRP ILE LEU GLY ASN PRO SEQRES 6 B 321 GLU CYS GLU SER LEU LEU SER GLU ARG SER TRP SER TYR SEQRES 7 B 321 ILE VAL GLU THR PRO ASN SER GLU ASN GLY THR CYS PHE SEQRES 8 B 321 PRO GLY ASP PHE ILE ASP TYR GLU GLU LEU ARG GLU GLN SEQRES 9 B 321 LEU SER SER VAL SER SER PHE GLU ARG PHE GLU ILE PHE SEQRES 10 B 321 SER LYS GLU SER SER TRP PRO LYS HIS THR THR GLY GLY SEQRES 11 B 321 VAL THR ALA ALA CYS SER HIS ALA GLY LYS SER SER PHE SEQRES 12 B 321 TYR ARG ASN LEU LEU TRP LEU THR GLU LYS ASP GLY SER SEQRES 13 B 321 TYR PRO ASN LEU ASN ASN SER TYR VAL ASN LYS LYS GLY SEQRES 14 B 321 LYS GLU VAL LEU VAL LEU TRP GLY VAL HIS HIS PRO SER SEQRES 15 B 321 ASN ILE LYS ASP GLN GLN THR LEU TYR GLN LYS GLU ASN SEQRES 16 B 321 ALA TYR VAL SER VAL VAL SER SER ASN TYR ASN ARG ARG SEQRES 17 B 321 PHE THR PRO GLU ILE ALA GLU ARG PRO LYS VAL ARG GLY SEQRES 18 B 321 GLN ALA GLY ARG ILE ASN TYR TYR TRP THR LEU LEU LYS SEQRES 19 B 321 PRO GLY ASP THR ILE MET PHE GLU ALA ASN GLY ASN LEU SEQRES 20 B 321 ILE ALA PRO TRP TYR ALA PHE ALA LEU SER ARG GLY PHE SEQRES 21 B 321 GLY SER GLY ILE ILE THR SER ASN ALA SER MET HIS GLU SEQRES 22 B 321 CYS ASP THR LYS CYS GLN THR PRO GLN GLY ALA ILE ASN SEQRES 23 B 321 SER SER LEU PRO PHE GLN ASN ILE HIS PRO ILE THR ILE SEQRES 24 B 321 GLY GLU CYS PRO LYS TYR VAL ARG SER THR LYS LEU ARG SEQRES 25 B 321 MET VAL THR GLY LEU ARG ASN ILE PRO SEQRES 1 C 321 ASP THR ILE CYS ILE GLY TYR HIS ALA ASN ASN SER THR SEQRES 2 C 321 ASP THR VAL ASP THR VAL LEU GLU LYS ASN VAL THR VAL SEQRES 3 C 321 THR HIS SER VAL ASN LEU LEU GLU ASP SER HIS ASN GLY SEQRES 4 C 321 LYS LEU CYS ARG LEU LYS GLY ILE ALA PRO LEU GLN LEU SEQRES 5 C 321 GLY LYS CYS ASN ILE ALA GLY TRP ILE LEU GLY ASN PRO SEQRES 6 C 321 GLU CYS GLU SER LEU LEU SER GLU ARG SER TRP SER TYR SEQRES 7 C 321 ILE VAL GLU THR PRO ASN SER GLU ASN GLY THR CYS PHE SEQRES 8 C 321 PRO GLY ASP PHE ILE ASP TYR GLU GLU LEU ARG GLU GLN SEQRES 9 C 321 LEU SER SER VAL SER SER PHE GLU ARG PHE GLU ILE PHE SEQRES 10 C 321 SER LYS GLU SER SER TRP PRO LYS HIS THR THR GLY GLY SEQRES 11 C 321 VAL THR ALA ALA CYS SER HIS ALA GLY LYS SER SER PHE SEQRES 12 C 321 TYR ARG ASN LEU LEU TRP LEU THR GLU LYS ASP GLY SER SEQRES 13 C 321 TYR PRO ASN LEU ASN ASN SER TYR VAL ASN LYS LYS GLY SEQRES 14 C 321 LYS GLU VAL LEU VAL LEU TRP GLY VAL HIS HIS PRO SER SEQRES 15 C 321 ASN ILE LYS ASP GLN GLN THR LEU TYR GLN LYS GLU ASN SEQRES 16 C 321 ALA TYR VAL SER VAL VAL SER SER ASN TYR ASN ARG ARG SEQRES 17 C 321 PHE THR PRO GLU ILE ALA GLU ARG PRO LYS VAL ARG GLY SEQRES 18 C 321 GLN ALA GLY ARG ILE ASN TYR TYR TRP THR LEU LEU LYS SEQRES 19 C 321 PRO GLY ASP THR ILE MET PHE GLU ALA ASN GLY ASN LEU SEQRES 20 C 321 ILE ALA PRO TRP TYR ALA PHE ALA LEU SER ARG GLY PHE SEQRES 21 C 321 GLY SER GLY ILE ILE THR SER ASN ALA SER MET HIS GLU SEQRES 22 C 321 CYS ASP THR LYS CYS GLN THR PRO GLN GLY ALA ILE ASN SEQRES 23 C 321 SER SER LEU PRO PHE GLN ASN ILE HIS PRO ILE THR ILE SEQRES 24 C 321 GLY GLU CYS PRO LYS TYR VAL ARG SER THR LYS LEU ARG SEQRES 25 C 321 MET VAL THR GLY LEU ARG ASN ILE PRO SEQRES 1 F 140 MET SER GLY GLN VAL GLN LEU VAL GLU SER GLY GLY GLY SEQRES 2 F 140 LEU VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA SEQRES 3 F 140 ALA SER GLY LYS TYR VAL ASN LEU MET SER LEU GLY TRP SEQRES 4 F 140 PHE ARG GLN ALA PRO GLY GLN GLY LEU GLU ALA VAL ALA SEQRES 5 F 140 ALA ILE SER PHE ASP GLY LYS LYS THR TYR TYR ALA ASP SEQRES 6 F 140 SER VAL LYS GLY ARG PHE THR ILE SER ARG ASP ASN SER SEQRES 7 F 140 LYS ASN THR LEU TYR LEU GLN MET ASN SER LEU ARG ALA SEQRES 8 F 140 GLU ASP THR ALA VAL TYR TYR CYS ALA ALA SER VAL VAL SEQRES 9 F 140 ASP SER LEU GLY VAL GLY PHE TYR SER TYR TRP GLY GLN SEQRES 10 F 140 GLY THR LEU VAL THR VAL SER GLY SER GLY SER HIS HIS SEQRES 11 F 140 TRP GLY SER THR HIS HIS HIS HIS HIS HIS SEQRES 1 G 232 SER ILE GLN SER ARG GLY LEU PHE GLY ALA ILE ALA GLY SEQRES 2 G 232 PHE ILE GLU GLY GLY TRP THR GLY MET ILE ASP GLY TRP SEQRES 3 G 232 TYR GLY TYR HIS TRP GLN ASN GLU GLN GLY SER GLY TYR SEQRES 4 G 232 ALA ALA ASP GLN LYS SER THR GLN ASN ALA ILE ASN GLY SEQRES 5 G 232 ILE THR ASN ILE VAL ASN SER VAL ILE GLU LYS MET ASN SEQRES 6 G 232 THR GLN PHE THR ALA VAL GLY LYS GLU PHE ASN ASN LEU SEQRES 7 G 232 GLU LYS ARG MET GLU ASN LEU ASN LYS LYS VAL ASP ASP SEQRES 8 G 232 GLY PHE LEU ASP ILE TRP THR TYR ASN ALA GLU LEU LEU SEQRES 9 G 232 VAL LEU LEU ILE ASN GLU ARG THR LEU ASP PHE HIS ASP SEQRES 10 G 232 SER ASN VAL LYS ASN LEU TYR GLU LYS VAL LYS ASN GLN SEQRES 11 G 232 LEU ARG ASN ASN ALA LYS GLU ILE GLY ASN GLY CYS PHE SEQRES 12 G 232 GLU PHE TYR HIS LYS CYS ASN ASN GLU CYS MET GLU SER SEQRES 13 G 232 VAL LYS ASN GLY THR TYR ASP TYR PRO LYS TYR SER GLU SEQRES 14 G 232 GLU SER LYS LEU ASN ARG GLU LYS ILE ASP GLY SER GLY SEQRES 15 G 232 TYR ILE PRO GLU ALA PRO ARG ASP GLY GLN ALA TYR VAL SEQRES 16 G 232 ARG LYS ASP GLY GLU TRP VAL LEU LEU SER THR PHE LEU SEQRES 17 G 232 GLY SER GLY LEU ASN ASP ILE PHE GLU ALA GLN LYS ILE SEQRES 18 G 232 GLU TRP HIS GLU GLY HIS HIS HIS HIS HIS HIS SEQRES 1 H 232 SER ILE GLN SER ARG GLY LEU PHE GLY ALA ILE ALA GLY SEQRES 2 H 232 PHE ILE GLU GLY GLY TRP THR GLY MET ILE ASP GLY TRP SEQRES 3 H 232 TYR GLY TYR HIS TRP GLN ASN GLU GLN GLY SER GLY TYR SEQRES 4 H 232 ALA ALA ASP GLN LYS SER THR GLN ASN ALA ILE ASN GLY SEQRES 5 H 232 ILE THR ASN ILE VAL ASN SER VAL ILE GLU LYS MET ASN SEQRES 6 H 232 THR GLN PHE THR ALA VAL GLY LYS GLU PHE ASN ASN LEU SEQRES 7 H 232 GLU LYS ARG MET GLU ASN LEU ASN LYS LYS VAL ASP ASP SEQRES 8 H 232 GLY PHE LEU ASP ILE TRP THR TYR ASN ALA GLU LEU LEU SEQRES 9 H 232 VAL LEU LEU ILE ASN GLU ARG THR LEU ASP PHE HIS ASP SEQRES 10 H 232 SER ASN VAL LYS ASN LEU TYR GLU LYS VAL LYS ASN GLN SEQRES 11 H 232 LEU ARG ASN ASN ALA LYS GLU ILE GLY ASN GLY CYS PHE SEQRES 12 H 232 GLU PHE TYR HIS LYS CYS ASN ASN GLU CYS MET GLU SER SEQRES 13 H 232 VAL LYS ASN GLY THR TYR ASP TYR PRO LYS TYR SER GLU SEQRES 14 H 232 GLU SER LYS LEU ASN ARG GLU LYS ILE ASP GLY SER GLY SEQRES 15 H 232 TYR ILE PRO GLU ALA PRO ARG ASP GLY GLN ALA TYR VAL SEQRES 16 H 232 ARG LYS ASP GLY GLU TRP VAL LEU LEU SER THR PHE LEU SEQRES 17 H 232 GLY SER GLY LEU ASN ASP ILE PHE GLU ALA GLN LYS ILE SEQRES 18 H 232 GLU TRP HIS GLU GLY HIS HIS HIS HIS HIS HIS SEQRES 1 I 232 SER ILE GLN SER ARG GLY LEU PHE GLY ALA ILE ALA GLY SEQRES 2 I 232 PHE ILE GLU GLY GLY TRP THR GLY MET ILE ASP GLY TRP SEQRES 3 I 232 TYR GLY TYR HIS TRP GLN ASN GLU GLN GLY SER GLY TYR SEQRES 4 I 232 ALA ALA ASP GLN LYS SER THR GLN ASN ALA ILE ASN GLY SEQRES 5 I 232 ILE THR ASN ILE VAL ASN SER VAL ILE GLU LYS MET ASN SEQRES 6 I 232 THR GLN PHE THR ALA VAL GLY LYS GLU PHE ASN ASN LEU SEQRES 7 I 232 GLU LYS ARG MET GLU ASN LEU ASN LYS LYS VAL ASP ASP SEQRES 8 I 232 GLY PHE LEU ASP ILE TRP THR TYR ASN ALA GLU LEU LEU SEQRES 9 I 232 VAL LEU LEU ILE ASN GLU ARG THR LEU ASP PHE HIS ASP SEQRES 10 I 232 SER ASN VAL LYS ASN LEU TYR GLU LYS VAL LYS ASN GLN SEQRES 11 I 232 LEU ARG ASN ASN ALA LYS GLU ILE GLY ASN GLY CYS PHE SEQRES 12 I 232 GLU PHE TYR HIS LYS CYS ASN ASN GLU CYS MET GLU SER SEQRES 13 I 232 VAL LYS ASN GLY THR TYR ASP TYR PRO LYS TYR SER GLU SEQRES 14 I 232 GLU SER LYS LEU ASN ARG GLU LYS ILE ASP GLY SER GLY SEQRES 15 I 232 TYR ILE PRO GLU ALA PRO ARG ASP GLY GLN ALA TYR VAL SEQRES 16 I 232 ARG LYS ASP GLY GLU TRP VAL LEU LEU SER THR PHE LEU SEQRES 17 I 232 GLY SER GLY LEU ASN ASP ILE PHE GLU ALA GLN LYS ILE SEQRES 18 I 232 GLU TRP HIS GLU GLY HIS HIS HIS HIS HIS HIS HET NAG D 1 27 HET NAG D 2 27 HET BMA D 3 22 HET NAG J 1 27 HET NAG J 2 28 HET NAG K 1 27 HET NAG K 2 27 HET BMA K 3 22 HET NAG L 1 27 HET NAG L 2 27 HET BMA L 3 22 HET NAG M 1 27 HET NAG M 2 27 HET BMA M 3 22 HET NAG N 1 27 HET NAG N 2 27 HET BMA N 3 22 HET NAG A 401 28 HET NAG A 402 28 HET NAG A 403 28 HET NAG A 404 28 HET NAG B 401 28 HET NAG B 402 28 HET NAG B 403 28 HET NAG B 404 28 HET NAG C 401 28 HET NAG C 402 28 HET NAG C 403 28 HET NAG C 404 28 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 9 NAG 24(C8 H15 N O6) FORMUL 9 BMA 5(C6 H12 O6) HELIX 1 AA1 TYR E 28 MET E 32 5 5 HELIX 2 AA2 PHE E 53 LYS E 56 5 4 HELIX 3 AA3 ASN E 74 LYS E 76 5 3 HELIX 4 AA4 GLY E 105 TYR E 109 5 5 HELIX 5 AA5 ASN A 66 GLY A 73 1 8 HELIX 6 AA6 ASN A 74 GLU A 83 5 10 HELIX 7 AA7 ASP A 107 SER A 116 1 10 HELIX 8 AA8 ASN A 193 GLN A 202 1 10 HELIX 9 AA9 ASN B 66 GLY B 73 1 8 HELIX 10 AB1 ASN B 74 GLU B 83 5 10 HELIX 11 AB2 ASP B 107 SER B 116 1 10 HELIX 12 AB3 ASN B 193 GLN B 202 1 10 HELIX 13 AB4 ASN C 66 GLY C 73 1 8 HELIX 14 AB5 ASN C 74 GLU C 83 5 10 HELIX 15 AB6 ASP C 107 SER C 116 1 10 HELIX 16 AB7 ASN C 193 GLN C 202 1 10 HELIX 17 AB8 TYR F 28 MET F 32 5 5 HELIX 18 AB9 PHE F 53 LYS F 56 5 4 HELIX 19 AC1 ASN F 74 LYS F 76 5 3 HELIX 20 AC2 GLY F 105 TYR F 109 5 5 HELIX 21 AC3 ASP G 37 MET G 59 1 23 HELIX 22 AC4 GLU G 74 LEU G 126 1 53 HELIX 23 AC5 ASN G 145 GLY G 155 1 11 HELIX 24 AC6 TYR G 159 GLU G 171 1 13 HELIX 25 AC7 ASP H 37 MET H 59 1 23 HELIX 26 AC8 GLU H 74 ARG H 127 1 54 HELIX 27 AC9 ASN H 145 GLY H 155 1 11 HELIX 28 AD1 TYR H 159 GLU H 164 1 6 HELIX 29 AD2 GLU H 165 LYS H 172 1 8 HELIX 30 AD3 ASP I 37 MET I 59 1 23 HELIX 31 AD4 GLU I 74 ARG I 127 1 54 HELIX 32 AD5 ASN I 145 ASN I 154 1 10 HELIX 33 AD6 ASP I 158 ARG I 170 1 13 HELIX 34 AD7 GLU I 171 ILE I 173 5 3 SHEET 1 AA1 4 GLN E 3 SER E 7 0 SHEET 2 AA1 4 LEU E 20 SER E 25 -1 O ALA E 23 N VAL E 5 SHEET 3 AA1 4 THR E 78 LEU E 81 -1 O LEU E 79 N CYS E 22 SHEET 4 AA1 4 SER E 71 ARG E 72 -1 N SER E 71 O TYR E 80 SHEET 1 AA2 5 THR E 58 TYR E 60 0 SHEET 2 AA2 5 GLU E 46 ILE E 51 -1 N ALA E 50 O TYR E 59 SHEET 3 AA2 5 SER E 33 ARG E 38 -1 N TRP E 36 O ALA E 49 SHEET 4 AA2 5 TYR E 94 SER E 99 -1 O TYR E 95 N PHE E 37 SHEET 5 AA2 5 TYR E 111 TRP E 112 -1 O TYR E 111 N ALA E 98 SHEET 1 AA3 5 GLY G 31 ALA G 36 0 SHEET 2 AA3 5 TYR G 22 ASN G 28 -1 N ASN G 28 O GLY G 31 SHEET 3 AA3 5 THR A 12 TYR A 17 -1 N THR A 12 O GLN G 27 SHEET 4 AA3 5 CYS G 137 PHE G 140 -1 O PHE G 138 N ILE A 13 SHEET 5 AA3 5 ALA G 130 GLU G 132 -1 N LYS G 131 O GLU G 139 SHEET 1 AA4 2 THR A 25 VAL A 26 0 SHEET 2 AA4 2 VAL A 34 THR A 35 -1 O VAL A 34 N VAL A 26 SHEET 1 AA5 2 SER A 39 ASN A 41 0 SHEET 2 AA5 2 ARG A 322 VAL A 324 -1 O MET A 323 N VAL A 40 SHEET 1 AA6 3 LEU A 43 GLU A 44 0 SHEET 2 AA6 3 PHE A 301 GLN A 302 1 O PHE A 301 N GLU A 44 SHEET 3 AA6 3 LYS A 314 TYR A 315 1 O LYS A 314 N GLN A 302 SHEET 1 AA7 2 LEU A 51 LEU A 54 0 SHEET 2 AA7 2 MET A 281 THR A 286 1 O CYS A 284 N ARG A 53 SHEET 1 AA8 3 LEU A 60 GLN A 61 0 SHEET 2 AA8 3 ILE A 89 GLU A 91 1 O VAL A 90 N LEU A 60 SHEET 3 AA8 3 ILE A 274 THR A 276 1 O ILE A 275 N GLU A 91 SHEET 1 AA9 4 VAL A 118 GLU A 125 0 SHEET 2 AA9 4 TYR A 262 ARG A 268 -1 O SER A 267 N SER A 119 SHEET 3 AA9 4 GLU A 181 HIS A 190 -1 N GLU A 181 O LEU A 266 SHEET 4 AA9 4 ARG A 235 LEU A 243 -1 O ARG A 235 N HIS A 190 SHEET 1 AB1 3 THR A 137 THR A 138 0 SHEET 2 AB1 3 LEU A 157 THR A 161 -1 O THR A 161 N THR A 137 SHEET 3 AB1 3 ILE A 258 PRO A 260 -1 O ALA A 259 N LEU A 158 SHEET 1 AB2 2 THR A 142 HIS A 147 0 SHEET 2 AB2 2 LYS A 150 SER A 152 -1 O LYS A 150 N HIS A 147 SHEET 1 AB3 4 SER A 173 VAL A 175 0 SHEET 2 AB3 4 THR A 248 ALA A 253 -1 O ILE A 249 N TYR A 174 SHEET 3 AB3 4 VAL A 208 VAL A 211 -1 N VAL A 211 O MET A 250 SHEET 4 AB3 4 ASN A 216 PHE A 219 -1 O PHE A 219 N VAL A 208 SHEET 1 AB4 3 ALA A 294 ILE A 295 0 SHEET 2 AB4 3 CYS A 288 GLN A 289 -1 N CYS A 288 O ILE A 295 SHEET 3 AB4 3 ILE A 309 GLY A 310 -1 O ILE A 309 N GLN A 289 SHEET 1 AB5 5 GLY H 31 ALA H 36 0 SHEET 2 AB5 5 TYR H 22 ASN H 28 -1 N TYR H 24 O ALA H 35 SHEET 3 AB5 5 THR B 12 TYR B 17 -1 N CYS B 14 O HIS H 25 SHEET 4 AB5 5 PHE H 138 PHE H 140 -1 O PHE H 138 N ILE B 13 SHEET 5 AB5 5 ALA H 130 GLU H 132 -1 N LYS H 131 O GLU H 139 SHEET 1 AB6 2 ASP B 24 VAL B 26 0 SHEET 2 AB6 2 VAL B 34 VAL B 36 -1 O VAL B 34 N VAL B 26 SHEET 1 AB7 2 SER B 39 ASN B 41 0 SHEET 2 AB7 2 ARG B 322 VAL B 324 -1 O MET B 323 N VAL B 40 SHEET 1 AB8 3 LEU B 43 GLU B 44 0 SHEET 2 AB8 3 PHE B 301 GLN B 302 1 O PHE B 301 N GLU B 44 SHEET 3 AB8 3 LYS B 314 TYR B 315 1 O LYS B 314 N GLN B 302 SHEET 1 AB9 2 LEU B 51 LEU B 54 0 SHEET 2 AB9 2 MET B 281 THR B 286 1 O CYS B 284 N ARG B 53 SHEET 1 AC1 3 LEU B 60 GLN B 61 0 SHEET 2 AC1 3 ILE B 89 GLU B 91 1 O VAL B 90 N LEU B 60 SHEET 3 AC1 3 ILE B 274 THR B 276 1 O ILE B 275 N GLU B 91 SHEET 1 AC2 6 VAL B 118 GLU B 125 0 SHEET 2 AC2 6 TYR B 262 ARG B 268 -1 O SER B 267 N SER B 119 SHEET 3 AC2 6 GLU B 181 HIS B 190 -1 N LEU B 183 O PHE B 264 SHEET 4 AC2 6 LEU B 257 PRO B 260 -1 O ILE B 258 N GLY B 187 SHEET 5 AC2 6 LEU B 157 THR B 161 -1 N LEU B 158 O ALA B 259 SHEET 6 AC2 6 THR B 137 THR B 138 -1 N THR B 137 O THR B 161 SHEET 1 AC3 4 VAL B 118 GLU B 125 0 SHEET 2 AC3 4 TYR B 262 ARG B 268 -1 O SER B 267 N SER B 119 SHEET 3 AC3 4 GLU B 181 HIS B 190 -1 N LEU B 183 O PHE B 264 SHEET 4 AC3 4 ARG B 235 LEU B 243 -1 O ARG B 235 N HIS B 190 SHEET 1 AC4 2 THR B 142 HIS B 147 0 SHEET 2 AC4 2 LYS B 150 SER B 152 -1 O LYS B 150 N HIS B 147 SHEET 1 AC5 4 SER B 173 VAL B 175 0 SHEET 2 AC5 4 THR B 248 ALA B 253 -1 O ILE B 249 N TYR B 174 SHEET 3 AC5 4 VAL B 208 SER B 212 -1 N SER B 209 O GLU B 252 SHEET 4 AC5 4 ASN B 216 PHE B 219 -1 O PHE B 219 N VAL B 208 SHEET 1 AC6 4 ALA B 294 ILE B 295 0 SHEET 2 AC6 4 CYS B 288 GLN B 289 -1 N CYS B 288 O ILE B 295 SHEET 3 AC6 4 ILE B 309 CYS B 312 -1 O ILE B 309 N GLN B 289 SHEET 4 AC6 4 GLN H 62 THR H 64 -1 O GLN H 62 N CYS B 312 SHEET 1 AC7 5 GLY I 31 ALA I 36 0 SHEET 2 AC7 5 TYR I 22 ASN I 28 -1 N TYR I 24 O ALA I 35 SHEET 3 AC7 5 THR C 12 TYR C 17 -1 N THR C 12 O GLN I 27 SHEET 4 AC7 5 CYS I 137 PHE I 140 -1 O PHE I 138 N ILE C 13 SHEET 5 AC7 5 ALA I 130 GLU I 132 -1 N LYS I 131 O GLU I 139 SHEET 1 AC8 2 THR C 25 VAL C 26 0 SHEET 2 AC8 2 VAL C 34 THR C 35 -1 O VAL C 34 N VAL C 26 SHEET 1 AC9 2 SER C 39 ASN C 41 0 SHEET 2 AC9 2 ARG C 322 VAL C 324 -1 O MET C 323 N VAL C 40 SHEET 1 AD1 3 LEU C 43 GLU C 44 0 SHEET 2 AD1 3 PHE C 301 GLN C 302 1 O PHE C 301 N GLU C 44 SHEET 3 AD1 3 LYS C 314 TYR C 315 1 O LYS C 314 N GLN C 302 SHEET 1 AD2 2 LEU C 51 LEU C 54 0 SHEET 2 AD2 2 MET C 281 THR C 286 1 O CYS C 284 N ARG C 53 SHEET 1 AD3 3 LEU C 60 GLN C 61 0 SHEET 2 AD3 3 ILE C 89 GLU C 91 1 O VAL C 90 N LEU C 60 SHEET 3 AD3 3 ILE C 274 THR C 276 1 O ILE C 275 N GLU C 91 SHEET 1 AD4 4 VAL C 118 GLU C 125 0 SHEET 2 AD4 4 TYR C 262 ARG C 268 -1 O SER C 267 N SER C 120 SHEET 3 AD4 4 GLU C 181 HIS C 190 -1 N GLU C 181 O LEU C 266 SHEET 4 AD4 4 ARG C 235 LEU C 243 -1 O ARG C 235 N HIS C 190 SHEET 1 AD5 4 VAL C 118 GLU C 125 0 SHEET 2 AD5 4 TYR C 262 ARG C 268 -1 O SER C 267 N SER C 120 SHEET 3 AD5 4 GLU C 181 HIS C 190 -1 N GLU C 181 O LEU C 266 SHEET 4 AD5 4 LEU C 257 ILE C 258 -1 O ILE C 258 N GLY C 187 SHEET 1 AD6 2 THR C 137 THR C 138 0 SHEET 2 AD6 2 LEU C 160 THR C 161 -1 O THR C 161 N THR C 137 SHEET 1 AD7 2 THR C 142 HIS C 147 0 SHEET 2 AD7 2 LYS C 150 SER C 152 -1 O LYS C 150 N HIS C 147 SHEET 1 AD8 4 LEU C 170 VAL C 175 0 SHEET 2 AD8 4 THR C 248 ALA C 253 -1 O PHE C 251 N ASN C 172 SHEET 3 AD8 4 VAL C 208 SER C 212 -1 N SER C 209 O GLU C 252 SHEET 4 AD8 4 ASN C 216 PHE C 219 -1 O PHE C 219 N VAL C 208 SHEET 1 AD9 3 CYS C 288 GLN C 289 0 SHEET 2 AD9 3 ILE C 309 CYS C 312 -1 O ILE C 309 N GLN C 289 SHEET 3 AD9 3 GLN I 62 PHE I 63 -1 O GLN I 62 N CYS C 312 SHEET 1 AE1 4 GLN F 3 SER F 7 0 SHEET 2 AE1 4 LEU F 20 SER F 25 -1 O ALA F 23 N VAL F 5 SHEET 3 AE1 4 THR F 78 LEU F 81 -1 O LEU F 79 N CYS F 22 SHEET 4 AE1 4 ILE F 70 ARG F 72 -1 N SER F 71 O TYR F 80 SHEET 1 AE2 5 THR F 58 TYR F 60 0 SHEET 2 AE2 5 GLU F 46 ILE F 51 -1 N ALA F 50 O TYR F 59 SHEET 3 AE2 5 SER F 33 ARG F 38 -1 N TRP F 36 O ALA F 49 SHEET 4 AE2 5 TYR F 94 SER F 99 -1 O TYR F 95 N PHE F 37 SHEET 5 AE2 5 TYR F 111 TRP F 112 -1 O TYR F 111 N ALA F 98 SSBOND 1 CYS A 14 CYS G 137 1555 1555 2.04 SSBOND 2 CYS A 65 CYS A 77 1555 1555 2.03 SSBOND 3 CYS A 100 CYS A 145 1555 1555 2.03 SSBOND 4 CYS A 288 CYS A 312 1555 1555 2.03 SSBOND 5 CYS B 14 CYS H 137 1555 1555 2.03 SSBOND 6 CYS B 65 CYS B 77 1555 1555 2.04 SSBOND 7 CYS B 100 CYS B 145 1555 1555 2.03 SSBOND 8 CYS B 288 CYS B 312 1555 1555 2.03 SSBOND 9 CYS C 14 CYS I 137 1555 1555 2.04 SSBOND 10 CYS C 65 CYS C 77 1555 1555 2.04 SSBOND 11 CYS C 100 CYS C 145 1555 1555 2.03 SSBOND 12 CYS C 288 CYS C 312 1555 1555 2.02 SSBOND 13 CYS F 22 CYS F 96 1555 1555 2.04 SSBOND 14 CYS G 144 CYS G 148 1555 1555 2.03 SSBOND 15 CYS H 144 CYS H 148 1555 1555 2.03 SSBOND 16 CYS I 144 CYS I 148 1555 1555 2.03 LINK ND2 ASN A 21 C1 NAG A 402 1555 1555 1.44 LINK ND2 ASN A 33 C1 NAG A 404 1555 1555 1.45 LINK ND2 ASN A 97 C1 NAG D 1 1555 1555 1.44 LINK ND2 ASN A 171 C1 NAG A 401 1555 1555 1.44 LINK ND2 ASN A 278 C1 NAG A 403 1555 1555 1.44 LINK ND2 ASN A 296 C1 NAG J 1 1555 1555 1.45 LINK ND2 ASN B 21 C1 NAG B 402 1555 1555 1.44 LINK ND2 ASN B 33 C1 NAG B 404 1555 1555 1.50 LINK ND2 ASN B 97 C1 NAG K 1 1555 1555 1.44 LINK ND2 ASN B 171 C1 NAG B 401 1555 1555 1.44 LINK ND2 ASN B 278 C1 NAG B 403 1555 1555 1.44 LINK ND2 ASN B 296 C1 NAG L 1 1555 1555 1.45 LINK ND2 ASN C 21 C1 NAG C 402 1555 1555 1.44 LINK ND2 ASN C 33 C1 NAG C 404 1555 1555 1.44 LINK ND2 ASN C 97 C1 NAG M 1 1555 1555 1.43 LINK ND2 ASN C 171 C1 NAG C 401 1555 1555 1.45 LINK ND2 ASN C 278 C1 NAG C 403 1555 1555 1.44 LINK ND2 ASN C 296 C1 NAG N 1 1555 1555 1.44 LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.45 LINK O4 NAG D 2 C1 BMA D 3 1555 1555 1.44 LINK O4 NAG J 1 C1 NAG J 2 1555 1555 1.43 LINK O4 NAG K 1 C1 NAG K 2 1555 1555 1.45 LINK O4 NAG K 2 C1 BMA K 3 1555 1555 1.44 LINK O4 NAG L 1 C1 NAG L 2 1555 1555 1.45 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 M 2 C1 BMA M 3 1555 1555 1.44 LINK O4 NAG N 1 C1 NAG N 2 1555 1555 1.43 LINK O4 NAG N 2 C1 BMA N 3 1555 1555 1.43 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