HEADER VIRAL PROTEIN 23-JAN-25 9LOF TITLE CRYO-EM STRUCTURE OF SFTSV GN IN COMPLEX WITH ZS01S-336 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 336; COMPND 8 CHAIN: B; COMPND 9 ENGINEERED: YES; COMPND 10 MOL_ID: 3; COMPND 11 MOLECULE: LIGHT CHAIN OF 336; 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 EXPDTA ELECTRON MICROSCOPY AUTHOR J.H.BI,Y.Y.ZHANG,Q.ZHOU,D.P.LI REVDAT 1 28-JAN-26 9LOF 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. 3.03 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : CRYOSPARC 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) : 3.030 REMARK 3 NUMBER OF PARTICLES : 164593 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 9LOF 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_1300056097. 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 336 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 ARG C 211 REMARK 465 GLY C 212 REMARK 465 GLU C 213 REMARK 465 CYS C 214 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 -61.33 -124.22 REMARK 500 SER A 115 -60.22 -96.22 REMARK 500 PRO A 187 -169.99 -76.19 REMARK 500 HIS A 234 -155.30 -150.02 REMARK 500 THR A 276 30.64 -89.02 REMARK 500 SER A 277 72.49 64.05 REMARK 500 GLU A 296 -162.93 -165.03 REMARK 500 GLU A 297 50.63 73.82 REMARK 500 ALA A 298 42.09 72.45 REMARK 500 GLU B 89 45.78 -87.70 REMARK 500 VAL B 109 123.18 -37.61 REMARK 500 LEU B 111 79.64 58.06 REMARK 500 ASP B 159 63.73 61.43 REMARK 500 SER C 30 -54.62 -28.63 REMARK 500 ALA C 51 -5.96 61.92 REMARK 500 SER C 52 -15.66 -141.92 REMARK 500 PHE C 83 76.00 -104.83 REMARK 500 LYS C 169 -64.30 -98.14 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 ILE C 29 SER C 30 -139.54 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-63247 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF SFTSV GN IN COMPLEX WITH 336 DBREF1 9LOF A 20 340 UNP A0A1S6XXK1_SFTS DBREF2 9LOF A A0A1S6XXK1 20 340 DBREF 9LOF B 1 226 PDB 9LOF 9LOF 1 226 DBREF 9LOF C 1 214 PDB 9LOF 9LOF 1 214 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 226 GLU VAL GLN LEU LEU GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 B 226 PRO GLY GLY SER LEU ARG LEU SER CYS THR ALA SER GLY SEQRES 3 B 226 PHE THR PHE SER THR GLY ASP MET SER TRP VAL ARG GLN SEQRES 4 B 226 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER THR VAL THR SEQRES 5 B 226 GLY GLY GLY VAL SER THR TYR TYR ALA ASP SER ALA LYS SEQRES 6 B 226 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR SEQRES 7 B 226 LEU TYR LEU GLN MET ASN SER LEU ARG PRO GLU ASP THR SEQRES 8 B 226 ALA VAL TYR TYR CYS ALA LYS VAL GLY PRO TRP TYR PHE SEQRES 9 B 226 TYR ASP SER SER VAL HIS LEU LEU TYR TYR PHE ASP TYR SEQRES 10 B 226 TRP SER GLN GLY THR LEU VAL THR VAL SER SER ALA SER SEQRES 11 B 226 THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER SEQRES 12 B 226 LYS SER THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU SEQRES 13 B 226 VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP SEQRES 14 B 226 ASN SER GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO SEQRES 15 B 226 ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SER SEQRES 16 B 226 VAL VAL THR VAL PRO SER SER SER LEU GLY THR GLN THR SEQRES 17 B 226 TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS SEQRES 18 B 226 VAL ASP LYS LYS VAL SEQRES 1 C 214 ASP ILE GLN MET THR GLN SER PRO SER THR LEU SER ALA SEQRES 2 C 214 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 C 214 GLN SER ILE SER SER TRP LEU ALA TRP TYR GLN GLN LYS SEQRES 4 C 214 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR LYS ALA SER SEQRES 5 C 214 SER LEU GLU SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 C 214 GLY SER GLY THR GLU PHE THR LEU THR ILE SER SER LEU SEQRES 7 C 214 GLN PRO ASP ASP PHE ALA THR TYR TYR CYS GLN GLN TYR SEQRES 8 C 214 HIS THR TYR PRO VAL ALA PHE GLY GLN GLY THR LYS VAL SEQRES 9 C 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 C 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 C 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 C 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 C 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 C 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 C 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 C 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 C 214 PHE ASN ARG GLY GLU CYS 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 97 LEU A 104 1 8 HELIX 5 AA5 SER A 160 SER A 163 5 4 HELIX 6 AA6 PRO A 168 ASP A 170 5 3 HELIX 7 AA7 PRO A 187 GLU A 201 1 15 HELIX 8 AA8 SER A 267 LYS A 275 1 9 HELIX 9 AA9 PHE A 286 GLY A 291 1 6 HELIX 10 AB1 ARG B 87 THR B 91 5 5 HELIX 11 AB2 SER B 142 LYS B 144 5 3 HELIX 12 AB3 SER B 202 LEU B 204 5 3 HELIX 13 AB4 GLN C 79 PHE C 83 5 5 HELIX 14 AB5 SER C 121 SER C 127 1 7 HELIX 15 AB6 LYS C 183 LYS C 188 1 6 SHEET 1 AA1 5 SER A 81 TYR A 83 0 SHEET 2 AA1 5 VAL A 172 ILE A 175 1 O VAL A 172 N SER A 81 SHEET 3 AA1 5 PHE A 129 PRO A 133 1 N GLU A 131 O ILE A 175 SHEET 4 AA1 5 TYR A 138 GLY A 142 -1 O VAL A 139 N ARG A 132 SHEET 5 AA1 5 VAL A 109 LYS A 111 1 N LYS A 110 O TYR A 138 SHEET 1 AA2 2 LYS A 147 ARG A 149 0 SHEET 2 AA2 2 CYS A 156 SER A 158 -1 O SER A 157 N SER A 148 SHEET 1 AA3 4 ASP A 177 CYS A 180 0 SHEET 2 AA3 4 CYS A 327 GLU A 338 -1 O TYR A 328 N ALA A 179 SHEET 3 AA3 4 GLU A 219 ASP A 231 -1 N SER A 220 O MET A 337 SHEET 4 AA3 4 ILE A 238 MET A 240 -1 O MET A 240 N ALA A 228 SHEET 1 AA4 3 LYS A 244 VAL A 248 0 SHEET 2 AA4 3 GLU A 313 SER A 317 -1 O GLU A 313 N VAL A 248 SHEET 3 AA4 3 ARG A 322 VAL A 323 -1 O VAL A 323 N VAL A 316 SHEET 1 AA5 2 PHE A 256 TYR A 259 0 SHEET 2 AA5 2 ARG A 304 LEU A 307 -1 O ARG A 304 N TYR A 259 SHEET 1 AA6 4 GLN B 3 SER B 7 0 SHEET 2 AA6 4 SER B 17 SER B 25 -1 O THR B 23 N LEU B 5 SHEET 3 AA6 4 THR B 78 ASN B 84 -1 O MET B 83 N LEU B 18 SHEET 4 AA6 4 THR B 69 ASP B 73 -1 N THR B 69 O GLN B 82 SHEET 1 AA7 6 LEU B 11 VAL B 12 0 SHEET 2 AA7 6 THR B 122 VAL B 126 1 O THR B 125 N VAL B 12 SHEET 3 AA7 6 ALA B 92 VAL B 99 -1 N ALA B 92 O VAL B 124 SHEET 4 AA7 6 MET B 34 GLN B 39 -1 N VAL B 37 O TYR B 95 SHEET 5 AA7 6 LEU B 45 VAL B 51 -1 O GLU B 46 N ARG B 38 SHEET 6 AA7 6 THR B 58 TYR B 60 -1 O TYR B 59 N THR B 50 SHEET 1 AA8 4 LEU B 11 VAL B 12 0 SHEET 2 AA8 4 THR B 122 VAL B 126 1 O THR B 125 N VAL B 12 SHEET 3 AA8 4 ALA B 92 VAL B 99 -1 N ALA B 92 O VAL B 124 SHEET 4 AA8 4 PHE B 115 TYR B 117 -1 O TYR B 117 N LYS B 98 SHEET 1 AA9 4 SER B 135 LEU B 139 0 SHEET 2 AA9 4 THR B 150 TYR B 160 -1 O LYS B 158 N SER B 135 SHEET 3 AA9 4 TYR B 191 PRO B 200 -1 O TYR B 191 N TYR B 160 SHEET 4 AA9 4 VAL B 178 THR B 180 -1 N HIS B 179 O VAL B 196 SHEET 1 AB1 4 THR B 146 SER B 147 0 SHEET 2 AB1 4 THR B 150 TYR B 160 -1 O THR B 150 N SER B 147 SHEET 3 AB1 4 TYR B 191 PRO B 200 -1 O TYR B 191 N TYR B 160 SHEET 4 AB1 4 VAL B 184 LEU B 185 -1 N VAL B 184 O SER B 192 SHEET 1 AB2 3 THR B 166 TRP B 169 0 SHEET 2 AB2 3 ILE B 210 HIS B 215 -1 O ASN B 212 N SER B 168 SHEET 3 AB2 3 THR B 220 LYS B 225 -1 O VAL B 222 N VAL B 213 SHEET 1 AB3 4 THR C 5 SER C 7 0 SHEET 2 AB3 4 THR C 20 ARG C 24 -1 O ARG C 24 N THR C 5 SHEET 3 AB3 4 PHE C 71 ILE C 75 -1 O PHE C 71 N CYS C 23 SHEET 4 AB3 4 PHE C 62 SER C 65 -1 N SER C 63 O THR C 74 SHEET 1 AB4 6 THR C 10 SER C 12 0 SHEET 2 AB4 6 THR C 102 GLU C 105 1 O GLU C 105 N LEU C 11 SHEET 3 AB4 6 THR C 85 GLN C 90 -1 N TYR C 86 O THR C 102 SHEET 4 AB4 6 LEU C 33 GLN C 38 -1 N GLN C 38 O THR C 85 SHEET 5 AB4 6 LYS C 45 TYR C 49 -1 O LYS C 45 N GLN C 37 SHEET 6 AB4 6 SER C 53 LEU C 54 -1 O SER C 53 N TYR C 49 SHEET 1 AB5 4 THR C 10 SER C 12 0 SHEET 2 AB5 4 THR C 102 GLU C 105 1 O GLU C 105 N LEU C 11 SHEET 3 AB5 4 THR C 85 GLN C 90 -1 N TYR C 86 O THR C 102 SHEET 4 AB5 4 ALA C 97 PHE C 98 -1 O ALA C 97 N GLN C 90 SHEET 1 AB6 4 SER C 114 PHE C 118 0 SHEET 2 AB6 4 THR C 129 PHE C 139 -1 O VAL C 133 N PHE C 118 SHEET 3 AB6 4 TYR C 173 SER C 182 -1 O TYR C 173 N PHE C 139 SHEET 4 AB6 4 SER C 159 VAL C 163 -1 N SER C 162 O SER C 176 SHEET 1 AB7 4 ALA C 153 LEU C 154 0 SHEET 2 AB7 4 ALA C 144 VAL C 150 -1 N VAL C 150 O ALA C 153 SHEET 3 AB7 4 TYR C 192 HIS C 198 -1 O GLU C 195 N GLN C 147 SHEET 4 AB7 4 VAL C 205 PHE C 209 -1 O LYS C 207 N CYS C 194 SSBOND 1 CYS A 26 CYS A 49 1555 1555 2.03 SSBOND 2 CYS A 143 CYS A 156 1555 1555 2.04 SSBOND 3 CYS A 180 CYS A 327 1555 1555 2.03 SSBOND 4 CYS A 206 CYS A 216 1555 1555 2.03 SSBOND 5 CYS A 258 CYS A 305 1555 1555 2.03 SSBOND 6 CYS A 266 CYS A 303 1555 1555 2.03 SSBOND 7 CYS A 274 CYS A 305 1555 1555 2.04 SSBOND 8 CYS A 287 CYS A 292 1555 1555 2.03 SSBOND 9 CYS B 22 CYS B 96 1555 1555 2.04 SSBOND 10 CYS B 155 CYS B 211 1555 1555 2.03 SSBOND 11 CYS C 23 CYS C 88 1555 1555 2.03 SSBOND 12 CYS C 134 CYS C 194 1555 1555 2.03 LINK ND2 ASN A 33 C1 NAG D 1 1555 1555 1.44 LINK ND2 ASN A 63 C1 NAG E 1 1555 1555 1.43 LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.44 LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.43 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 -3.07 CISPEP 2 PHE B 161 PRO B 162 0 -5.64 CISPEP 3 GLU B 163 PRO B 164 0 -0.57 CISPEP 4 SER C 7 PRO C 8 0 -10.32 CISPEP 5 TYR C 94 PRO C 95 0 0.91 CISPEP 6 TYR C 140 PRO C 141 0 1.68 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