HEADER VIRAL PROTEIN/IMMUNE SYSTEM 23-JAN-25 9LOG TITLE CRYO-EM STRUCTURE OF SFTSV GN IN COMPLEX WITH ZS01S-65 COMPND MOL_ID: 1; COMPND 2 MOLECULE: ENVELOPMENT POLYPROTEIN; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: M POLYPROTEIN; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: HEAVY CHAIN OF 65; COMPND 8 CHAIN: B; COMPND 9 ENGINEERED: YES; COMPND 10 MOL_ID: 3; COMPND 11 MOLECULE: LIGHT CHAIN OF 65; COMPND 12 CHAIN: C; COMPND 13 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SEVERE FEVER WITH THROMBOCYTOPENIA SYNDROME SOURCE 3 VIRUS; SOURCE 4 ORGANISM_TAXID: 1003835; SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 9 ORGANISM_TAXID: 9606; SOURCE 10 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 11 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 12 MOL_ID: 3; SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 14 ORGANISM_TAXID: 9606; SOURCE 15 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 16 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS VIRAL GLYCOPROTEIN, NEUTRALIZING ANTIBODY, VIRAL PROTEIN, VIRAL KEYWDS 2 PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR J.H.BI,Y.Y.ZHANG,Q.ZHOU,D.P.LI REVDAT 1 28-JAN-26 9LOG 0 JRNL AUTH J.H.BI,Y.Y.ZHANG,Q.ZHOU,D.P.LI JRNL TITL SINGLE-DOSE THERAPEUTIC ANTIBODY PROTECTS AGAINST SFTSV IN JRNL TITL 2 MICE AND RHESUS MACAQUES JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.50 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : RELION REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : NULL REMARK 3 REFINEMENT SPACE : NULL REMARK 3 REFINEMENT PROTOCOL : NULL REMARK 3 REFINEMENT TARGET : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL REMARK 3 REMARK 3 FITTING PROCEDURE : NULL REMARK 3 REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 3.500 REMARK 3 NUMBER OF PARTICLES : 185732 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 9LOG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 28-JAN-25. REMARK 100 THE DEPOSITION ID IS D_1300056098. 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 : CRYO-EM STRUCTURE OF SFTSV GN REMARK 245 IN COMPLEX WITH 65 REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 8.00 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 : FEI TALOS ARCTICA REMARK 245 DETECTOR TYPE : GATAN K3 BIOQUANTUM (6K X REMARK 245 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1200.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2200.00 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) : 5000.00 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: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 ASP A 20 REMARK 465 SER A 21 REMARK 465 GLY A 22 REMARK 465 VAL B 225 REMARK 465 SER C 217 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 A 303 CA - CB - SG ANGL. DEV. = 6.9 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 ILE A 25 -63.31 -124.08 REMARK 500 SER A 32 -61.23 -103.14 REMARK 500 PRO A 39 -167.49 -74.00 REMARK 500 PRO A 120 -169.79 -74.35 REMARK 500 PRO A 122 -176.58 -69.93 REMARK 500 PHE A 202 79.60 -113.54 REMARK 500 SER A 220 -169.98 -103.27 REMARK 500 THR A 276 -52.58 -121.39 REMARK 500 ASN B 103 36.24 -92.30 REMARK 500 TRP B 104 49.86 -78.72 REMARK 500 TYR B 112 58.57 -97.73 REMARK 500 ASP B 158 60.97 60.36 REMARK 500 GLN C 16 -169.49 -128.05 REMARK 500 ALA C 31 30.39 -90.55 REMARK 500 ASN C 53 -10.21 71.39 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-63248 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF SFTSV GN IN COMPLEX WITH 65 DBREF1 9LOG A 20 340 UNP A0A1S6XXK1_SFTS DBREF2 9LOG A A0A1S6XXK1 20 340 DBREF 9LOG B 1 225 PDB 9LOG 9LOG 1 225 DBREF 9LOG C 1 217 PDB 9LOG 9LOG 1 217 SEQRES 1 A 321 ASP SER GLY PRO ILE ILE CYS ALA GLY PRO ILE HIS SER SEQRES 2 A 321 ASN LYS SER ALA GLY ILE PRO HIS LEU LEU GLY TYR SER SEQRES 3 A 321 GLU LYS ILE CYS GLN ILE ASP ARG LEU ILE HIS VAL SER SEQRES 4 A 321 SER TRP LEU ARG ASN HIS SER GLN PHE GLN GLY TYR VAL SEQRES 5 A 321 GLY GLN ARG GLY GLY ARG SER GLN VAL SER TYR TYR PRO SEQRES 6 A 321 ALA GLU ASN SER TYR SER ARG TRP SER GLY LEU LEU SER SEQRES 7 A 321 PRO CYS ASP ALA ASP TRP LEU GLY MET LEU VAL VAL LYS SEQRES 8 A 321 LYS ALA LYS GLY SER ASP MET ILE VAL PRO GLY PRO SER SEQRES 9 A 321 TYR LYS GLY LYS VAL PHE PHE GLU ARG PRO THR PHE ASP SEQRES 10 A 321 GLY TYR VAL GLY TRP GLY CYS GLY SER GLY LYS SER ARG SEQRES 11 A 321 THR GLU SER GLY GLU LEU CYS SER SER ASP SER GLY THR SEQRES 12 A 321 SER SER GLY LEU LEU PRO SER ASP ARG VAL LEU TRP ILE SEQRES 13 A 321 GLY ASP VAL ALA CYS GLN PRO MET THR PRO ILE PRO GLU SEQRES 14 A 321 GLU THR PHE LEU GLU LEU LYS SER PHE SER GLN SER GLU SEQRES 15 A 321 PHE PRO ASP ILE CYS LYS ILE ASP GLY ILE VAL PHE ASN SEQRES 16 A 321 GLN CYS GLU GLY GLU SER LEU PRO GLN PRO PHE ASP VAL SEQRES 17 A 321 ALA TRP MET ASP VAL GLY HIS SER HIS LYS ILE ILE MET SEQRES 18 A 321 ARG GLU HIS LYS THR LYS TRP VAL GLN GLU SER SER SER SEQRES 19 A 321 LYS ASP PHE VAL CYS TYR LYS GLU GLY THR GLY PRO CYS SEQRES 20 A 321 SER GLU SER GLU GLU LYS ALA CYS LYS THR SER GLY SER SEQRES 21 A 321 CYS ARG GLY ASP MET GLN PHE CYS LYS VAL ALA GLY CYS SEQRES 22 A 321 GLU HIS GLY GLU GLU ALA SER GLU ALA LYS CYS ARG CYS SEQRES 23 A 321 SER LEU VAL HIS LYS PRO GLY GLU VAL VAL VAL SER TYR SEQRES 24 A 321 GLY GLY MET ARG VAL ARG PRO LYS CYS TYR GLY PHE SER SEQRES 25 A 321 ARG MET MET ALA THR MET GLU VAL ASN SEQRES 1 B 225 GLN VAL GLN LEU VAL GLN SER GLY ALA GLY MET LYS LYS SEQRES 2 B 225 PRO GLY SER SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 B 225 GLY SER PHE SER GLY TYR SER PHE ASN TRP VAL ARG GLN SEQRES 4 B 225 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY GLY ILE VAL SEQRES 5 B 225 PRO ILE PHE GLY THR ALA VAL TYR ALA GLN LYS PHE ARG SEQRES 6 B 225 GLY ARG VAL ALA ILE THR ALA ASP GLU SER THR THR THR SEQRES 7 B 225 ALA TYR MET GLU LEU SER SER LEU ARG TYR GLU ASP THR SEQRES 8 B 225 ALA VAL TYR TYR CYS ALA ARG ASP PRO GLY SER ASN TRP SEQRES 9 B 225 ALA ALA GLY ASP ILE ARG ASP TYR TYR PHE ASP TYR TRP SEQRES 10 B 225 GLY GLN GLY THR LEU VAL THR VAL SER SER ALA SER THR SEQRES 11 B 225 LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SEQRES 12 B 225 SER THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL SEQRES 13 B 225 LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SEQRES 14 B 225 SER GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA SEQRES 15 B 225 VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL SEQRES 16 B 225 VAL THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR SEQRES 17 B 225 ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL SEQRES 18 B 225 ASP LYS LYS VAL SEQRES 1 C 217 GLN SER VAL LEU THR GLN PRO PRO SER VAL SER GLY ALA SEQRES 2 C 217 PRO GLY GLN ARG VAL THR LEU SER CYS THR GLY SER SER SEQRES 3 C 217 SER ASN ILE GLY ALA ASP TYR ASP VAL HIS TRP TYR GLN SEQRES 4 C 217 GLN LEU PRO GLY ALA ALA PRO LYS LEU LEU ILE TYR GLY SEQRES 5 C 217 ASN ILE ASN ARG PRO SER GLY VAL PRO ALA ARG PHE SER SEQRES 6 C 217 GLY SER LYS SER GLY THR SER ALA SER LEU ALA ILE THR SEQRES 7 C 217 GLY LEU GLN ALA ASP ASP GLU ALA ASP TYR TYR CYS GLN SEQRES 8 C 217 SER TYR ASP SER ARG LEU SER ALA TYR VAL PHE GLY THR SEQRES 9 C 217 GLY THR LYS VAL THR VAL LEU GLY GLN PRO LYS ALA ASN SEQRES 10 C 217 PRO THR VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU SEQRES 11 C 217 GLN ALA ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP SEQRES 12 C 217 PHE TYR PRO GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SEQRES 13 C 217 SER SER PRO VAL LYS ALA GLY VAL GLU THR THR THR PRO SEQRES 14 C 217 SER LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR SEQRES 15 C 217 LEU SER LEU THR PRO GLU GLN TRP LYS SER HIS ARG SER SEQRES 16 C 217 TYR SER CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU SEQRES 17 C 217 LYS THR VAL ALA PRO THR GLU CYS SER HET NAG D 1 14 HET NAG D 2 14 HET NAG E 1 14 HET NAG E 2 14 HET MAN E 3 11 HET MAN E 4 11 HET MAN E 5 11 HET MAN E 6 11 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM MAN ALPHA-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 MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE FORMUL 4 NAG 4(C8 H15 N O6) FORMUL 5 MAN 4(C6 H12 O6) HELIX 1 AA1 GLY A 43 ARG A 53 1 11 HELIX 2 AA2 LEU A 54 SER A 65 1 12 HELIX 3 AA3 GLY A 75 VAL A 80 5 6 HELIX 4 AA4 SER A 88 TRP A 92 5 5 HELIX 5 AA5 SER A 97 ASP A 102 1 6 HELIX 6 AA6 SER A 160 SER A 163 5 4 HELIX 7 AA7 PRO A 187 PHE A 202 1 16 HELIX 8 AA8 SER A 267 SER A 277 1 11 HELIX 9 AA9 ASP A 283 ALA A 290 1 8 HELIX 10 AB1 GLN B 62 ARG B 65 5 4 HELIX 11 AB2 ARG B 87 THR B 91 5 5 HELIX 12 AB3 SER B 170 ALA B 172 5 3 HELIX 13 AB4 SER B 201 LEU B 203 5 3 HELIX 14 AB5 SER C 126 ALA C 132 1 7 HELIX 15 AB6 THR C 186 HIS C 193 1 8 HELIX 16 AB7 ALA C 212 CYS C 216 5 5 SHEET 1 AA1 2 TYR A 70 GLN A 73 0 SHEET 2 AA1 2 LEU A 166 PRO A 168 1 O LEU A 167 N GLN A 73 SHEET 1 AA2 5 SER A 81 TYR A 83 0 SHEET 2 AA2 5 VAL A 172 ILE A 175 1 O TRP A 174 N SER A 81 SHEET 3 AA2 5 PHE A 129 PRO A 133 1 N PHE A 129 O LEU A 173 SHEET 4 AA2 5 TYR A 138 TRP A 141 -1 O TRP A 141 N PHE A 130 SHEET 5 AA2 5 VAL A 109 LYS A 111 1 N LYS A 110 O TYR A 138 SHEET 1 AA3 2 LYS A 147 ARG A 149 0 SHEET 2 AA3 2 CYS A 156 SER A 158 -1 O SER A 157 N SER A 148 SHEET 1 AA4 4 ASP A 177 CYS A 180 0 SHEET 2 AA4 4 CYS A 327 ALA A 335 -1 O PHE A 330 N ASP A 177 SHEET 3 AA4 4 GLN A 223 ASP A 231 -1 N VAL A 227 O SER A 331 SHEET 4 AA4 4 LYS A 237 MET A 240 -1 O MET A 240 N ALA A 228 SHEET 1 AA5 2 LYS A 207 ILE A 208 0 SHEET 2 AA5 2 ILE A 211 VAL A 212 -1 O ILE A 211 N ILE A 208 SHEET 1 AA6 3 LYS A 244 VAL A 248 0 SHEET 2 AA6 3 GLU A 313 TYR A 318 -1 O SER A 317 N LYS A 244 SHEET 3 AA6 3 MET A 321 VAL A 323 -1 O MET A 321 N TYR A 318 SHEET 1 AA7 2 PHE A 256 TYR A 259 0 SHEET 2 AA7 2 ARG A 304 LEU A 307 -1 O ARG A 304 N TYR A 259 SHEET 1 AA8 4 GLN B 3 GLN B 6 0 SHEET 2 AA8 4 SER B 17 SER B 25 -1 O LYS B 23 N VAL B 5 SHEET 3 AA8 4 THR B 78 SER B 84 -1 O ALA B 79 N CYS B 22 SHEET 4 AA8 4 VAL B 68 ASP B 73 -1 N ASP B 73 O THR B 78 SHEET 1 AA9 6 MET B 11 LYS B 12 0 SHEET 2 AA9 6 THR B 121 VAL B 125 1 O THR B 124 N LYS B 12 SHEET 3 AA9 6 ALA B 92 ASP B 99 -1 N TYR B 94 O THR B 121 SHEET 4 AA9 6 SER B 33 GLN B 39 -1 N VAL B 37 O TYR B 95 SHEET 5 AA9 6 LEU B 45 ILE B 51 -1 O GLY B 49 N TRP B 36 SHEET 6 AA9 6 VAL B 59 TYR B 60 -1 O VAL B 59 N GLY B 50 SHEET 1 AB1 4 SER B 134 LEU B 138 0 SHEET 2 AB1 4 THR B 149 TYR B 159 -1 O LEU B 155 N PHE B 136 SHEET 3 AB1 4 TYR B 190 PRO B 199 -1 O TYR B 190 N TYR B 159 SHEET 4 AB1 4 VAL B 177 THR B 179 -1 N HIS B 178 O VAL B 195 SHEET 1 AB2 4 THR B 145 SER B 146 0 SHEET 2 AB2 4 THR B 149 TYR B 159 -1 O THR B 149 N SER B 146 SHEET 3 AB2 4 TYR B 190 PRO B 199 -1 O TYR B 190 N TYR B 159 SHEET 4 AB2 4 VAL B 183 LEU B 184 -1 N VAL B 183 O SER B 191 SHEET 1 AB3 3 THR B 165 TRP B 168 0 SHEET 2 AB3 3 CYS B 210 HIS B 214 -1 O ASN B 211 N SER B 167 SHEET 3 AB3 3 THR B 219 LYS B 223 -1 O THR B 219 N HIS B 214 SHEET 1 AB4 5 SER C 9 VAL C 10 0 SHEET 2 AB4 5 THR C 106 VAL C 108 1 O LYS C 107 N VAL C 10 SHEET 3 AB4 5 ASP C 87 ASP C 94 -1 N TYR C 88 O THR C 106 SHEET 4 AB4 5 HIS C 36 GLN C 40 -1 N GLN C 40 O ASP C 87 SHEET 5 AB4 5 LYS C 47 ILE C 50 -1 O LYS C 47 N GLN C 39 SHEET 1 AB5 4 SER C 9 VAL C 10 0 SHEET 2 AB5 4 THR C 106 VAL C 108 1 O LYS C 107 N VAL C 10 SHEET 3 AB5 4 ASP C 87 ASP C 94 -1 N TYR C 88 O THR C 106 SHEET 4 AB5 4 ALA C 99 VAL C 101 -1 O VAL C 101 N SER C 92 SHEET 1 AB6 3 ARG C 17 THR C 23 0 SHEET 2 AB6 3 SER C 72 THR C 78 -1 O ILE C 77 N VAL C 18 SHEET 3 AB6 3 PHE C 64 SER C 69 -1 N SER C 67 O SER C 74 SHEET 1 AB7 4 THR C 119 PHE C 123 0 SHEET 2 AB7 4 ALA C 135 PHE C 144 -1 O SER C 142 N THR C 119 SHEET 3 AB7 4 TYR C 177 LEU C 185 -1 O ALA C 179 N ILE C 141 SHEET 4 AB7 4 VAL C 164 THR C 166 -1 N GLU C 165 O TYR C 182 SHEET 1 AB8 4 THR C 119 PHE C 123 0 SHEET 2 AB8 4 ALA C 135 PHE C 144 -1 O SER C 142 N THR C 119 SHEET 3 AB8 4 TYR C 177 LEU C 185 -1 O ALA C 179 N ILE C 141 SHEET 4 AB8 4 SER C 170 LYS C 171 -1 N SER C 170 O ALA C 178 SHEET 1 AB9 4 SER C 158 VAL C 160 0 SHEET 2 AB9 4 VAL C 149 ALA C 155 -1 N ALA C 155 O SER C 158 SHEET 3 AB9 4 TYR C 196 HIS C 202 -1 O GLN C 199 N ALA C 152 SHEET 4 AB9 4 SER C 205 VAL C 211 -1 O VAL C 207 N VAL C 200 SSBOND 1 CYS A 26 CYS A 49 1555 1555 2.04 SSBOND 2 CYS A 143 CYS A 156 1555 1555 2.02 SSBOND 3 CYS A 180 CYS A 327 1555 1555 2.02 SSBOND 4 CYS A 206 CYS A 216 1555 1555 2.02 SSBOND 5 CYS A 258 CYS A 305 1555 1555 2.03 SSBOND 6 CYS A 266 CYS A 303 1555 1555 2.04 SSBOND 7 CYS A 274 CYS A 280 1555 1555 2.03 SSBOND 8 CYS A 287 CYS A 292 1555 1555 2.03 SSBOND 9 CYS B 22 CYS B 96 1555 1555 2.03 SSBOND 10 CYS B 154 CYS B 210 1555 1555 2.03 SSBOND 11 CYS C 22 CYS C 90 1555 1555 2.04 SSBOND 12 CYS C 139 CYS C 198 1555 1555 2.04 LINK ND2 ASN A 33 C1 NAG D 1 1555 1555 1.45 LINK ND2 ASN A 63 C1 NAG E 1 1555 1555 1.44 LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.43 LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.42 LINK O4 NAG E 2 C1 MAN E 3 1555 1555 1.44 LINK O6 MAN E 3 C1 MAN E 4 1555 1555 1.44 LINK O3 MAN E 3 C1 MAN E 6 1555 1555 1.43 LINK O3 MAN E 4 C1 MAN E 5 1555 1555 1.44 CISPEP 1 TYR A 83 PRO A 84 0 -8.81 CISPEP 2 GLY A 295 GLU A 296 0 6.47 CISPEP 3 PHE B 160 PRO B 161 0 -7.68 CISPEP 4 GLU B 162 PRO B 163 0 -4.21 CISPEP 5 TYR C 145 PRO C 146 0 -2.24 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