HEADER VIRAL PROTEIN/IMMUNE SYSTEM 17-DEC-24 9L2K TITLE THE CRYSTAL STRUCTURE OF SFTSV GN AND SD22 ANTIBODY COMPLEX 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: SD22 HEAVY CHAIN; COMPND 8 CHAIN: H; COMPND 9 ENGINEERED: YES; COMPND 10 MOL_ID: 3; COMPND 11 MOLECULE: SD22 LIGHT CHAIN; COMPND 12 CHAIN: L; COMPND 13 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SEVERE FEVER WITH THROMBOCYTOPENIA SYNDROME SOURCE 3 VIRUS; SOURCE 4 ORGANISM_COMMON: SEVERE FEVER WITH THROMBOCYTOPENIA VIRUS, SOURCE 5 HUAIYANGSHAN BANYANGVIRUS; SOURCE 6 ORGANISM_TAXID: 1003835; SOURCE 7 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 13 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 14 MOL_ID: 3; SOURCE 15 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 16 ORGANISM_TAXID: 9606; SOURCE 17 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 18 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS SD22, SFTSV, ANTIBODY, GN, SEVERE FEVER WITH THROMBOCYTOPENIA VIRUS, KEYWDS 2 VIRAL PROTEIN/IMMUNE SYSTEM, VIRAL PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR W.F.SHI,C.S.QUAN,J.X.QI REVDAT 1 18-JUN-25 9L2K 0 JRNL AUTH C.S.QUAN,J.X.QI,W.F.SHI JRNL TITL MOLECULAR MECHANISM OF POTENTLY NEUTRALIZING HUMAN JRNL TITL 2 MONOCLONAL ANTIBODIES AGAINST SEVERE FEVER WITH JRNL TITL 3 THROMBOCYTOPENIA VIRUS INFECTION JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.78 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.19.2_4158 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2 REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.78 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.94 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 40.120 REMARK 3 COMPLETENESS FOR RANGE (%) : 84.3 REMARK 3 NUMBER OF REFLECTIONS : 16920 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.306 REMARK 3 R VALUE (WORKING SET) : 0.304 REMARK 3 FREE R VALUE : 0.312 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.270 REMARK 3 FREE R VALUE TEST SET COUNT : 892 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 41.9400 - 5.0600 0.94 3226 188 0.3290 0.3303 REMARK 3 2 5.0600 - 4.0200 0.94 3138 170 0.2815 0.2656 REMARK 3 3 4.0200 - 3.5100 0.95 3200 143 0.2932 0.3309 REMARK 3 4 3.5100 - 3.1900 0.88 2886 145 0.3046 0.2897 REMARK 3 5 3.1900 - 2.9600 0.69 2304 111 0.3205 0.3340 REMARK 3 6 2.9600 - 2.7800 0.41 1353 56 0.3450 0.3174 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : NULL REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 33.155 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.90 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.003 4370 REMARK 3 ANGLE : 0.710 5914 REMARK 3 CHIRALITY : 0.045 634 REMARK 3 PLANARITY : 0.007 764 REMARK 3 DIHEDRAL : 14.750 1573 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 3 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: ( CHAIN A AND RESID 21:341 ) REMARK 3 ORIGIN FOR THE GROUP (A): 39.350 0.022 68.706 REMARK 3 T TENSOR REMARK 3 T11: 0.0827 T22: 0.0876 REMARK 3 T33: 0.1051 T12: 0.1022 REMARK 3 T13: -0.0219 T23: -0.0134 REMARK 3 L TENSOR REMARK 3 L11: 0.0118 L22: 0.0329 REMARK 3 L33: 0.0082 L12: -0.0211 REMARK 3 L13: -0.0058 L23: 0.0102 REMARK 3 S TENSOR REMARK 3 S11: 0.0450 S12: 0.0274 S13: 0.0030 REMARK 3 S21: -0.0398 S22: -0.0157 S23: -0.0280 REMARK 3 S31: 0.0269 S32: 0.0280 S33: 0.1049 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: ( CHAIN H AND RESID 1:121 ) REMARK 3 ORIGIN FOR THE GROUP (A): 22.011 -4.684 31.901 REMARK 3 T TENSOR REMARK 3 T11: 0.3055 T22: 0.1724 REMARK 3 T33: 0.1325 T12: 0.1319 REMARK 3 T13: -0.0999 T23: -0.0503 REMARK 3 L TENSOR REMARK 3 L11: 0.0051 L22: 0.0020 REMARK 3 L33: 0.0061 L12: -0.0029 REMARK 3 L13: 0.0012 L23: -0.0026 REMARK 3 S TENSOR REMARK 3 S11: 0.0002 S12: 0.0019 S13: -0.0004 REMARK 3 S21: -0.0415 S22: -0.0025 S23: 0.0146 REMARK 3 S31: 0.0046 S32: 0.0072 S33: 0.0057 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: ( CHAIN L AND RESID 1:108 ) REMARK 3 ORIGIN FOR THE GROUP (A): 4.970 1.728 45.123 REMARK 3 T TENSOR REMARK 3 T11: 0.2100 T22: 0.2218 REMARK 3 T33: 0.1232 T12: 0.1516 REMARK 3 T13: -0.0747 T23: -0.0527 REMARK 3 L TENSOR REMARK 3 L11: 0.0068 L22: 0.0020 REMARK 3 L33: 0.0049 L12: -0.0023 REMARK 3 L13: -0.0012 L23: 0.0030 REMARK 3 S TENSOR REMARK 3 S11: 0.0004 S12: -0.0006 S13: -0.0051 REMARK 3 S21: -0.0035 S22: -0.0068 S23: 0.0085 REMARK 3 S31: -0.0162 S32: -0.0323 S33: -0.0087 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 9L2K COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 23-DEC-24. REMARK 100 THE DEPOSITION ID IS D_1300054807. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 14-NOV-24 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SSRF REMARK 200 BEAMLINE : BL02U1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97915 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19950 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.780 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7 REMARK 200 DATA REDUNDANCY : 5.400 REMARK 200 R MERGE (I) : 0.18600 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 12.3220 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 1.29900 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 49.12 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 4 %V/V(+/-)-2-METHY1-2,4-PENTANEDIOL, REMARK 280 0.1 M CITRIC ACID PH 3.5, 20 % W/V POLYETHYLENE GLYCOL 1,500, REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 X+1/2,Y+1/2,Z REMARK 290 4555 -X+1/2,Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 32.23550 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.17300 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 32.23550 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 35.17300 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL 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, H, L, B, C 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 A 1 REMARK 465 GLY A 2 REMARK 465 TRP A 3 REMARK 465 SER A 4 REMARK 465 CYS A 5 REMARK 465 ILE A 6 REMARK 465 ILE A 7 REMARK 465 LEU A 8 REMARK 465 PHE A 9 REMARK 465 LEU A 10 REMARK 465 VAL A 11 REMARK 465 ALA A 12 REMARK 465 THR A 13 REMARK 465 ALA A 14 REMARK 465 THR A 15 REMARK 465 GLY A 16 REMARK 465 VAL A 17 REMARK 465 HIS A 18 REMARK 465 SER A 19 REMARK 465 GLY A 20 REMARK 465 HIS A 342 REMARK 465 HIS A 343 REMARK 465 HIS A 344 REMARK 465 ALA H 122 REMARK 465 SER H 123 REMARK 465 THR H 124 REMARK 465 LYS H 125 REMARK 465 GLY H 126 REMARK 465 PRO H 127 REMARK 465 SER H 128 REMARK 465 VAL H 129 REMARK 465 PHE H 130 REMARK 465 PRO H 131 REMARK 465 LEU H 132 REMARK 465 ALA H 133 REMARK 465 PRO H 134 REMARK 465 SER H 135 REMARK 465 SER H 136 REMARK 465 LYS H 137 REMARK 465 SER H 138 REMARK 465 THR H 139 REMARK 465 SER H 140 REMARK 465 GLY H 141 REMARK 465 GLY H 142 REMARK 465 THR H 143 REMARK 465 ALA H 144 REMARK 465 ALA H 145 REMARK 465 LEU H 146 REMARK 465 GLY H 147 REMARK 465 CYS H 148 REMARK 465 LEU H 149 REMARK 465 VAL H 150 REMARK 465 LYS H 151 REMARK 465 ASP H 152 REMARK 465 TYR H 153 REMARK 465 PHE H 154 REMARK 465 PRO H 155 REMARK 465 GLU H 156 REMARK 465 PRO H 157 REMARK 465 VAL H 158 REMARK 465 THR H 159 REMARK 465 VAL H 160 REMARK 465 SER H 161 REMARK 465 TRP H 162 REMARK 465 ASN H 163 REMARK 465 SER H 164 REMARK 465 GLY H 165 REMARK 465 ALA H 166 REMARK 465 LEU H 167 REMARK 465 THR H 168 REMARK 465 SER H 169 REMARK 465 GLY H 170 REMARK 465 VAL H 171 REMARK 465 HIS H 172 REMARK 465 THR H 173 REMARK 465 PHE H 174 REMARK 465 PRO H 175 REMARK 465 ALA H 176 REMARK 465 VAL H 177 REMARK 465 LEU H 178 REMARK 465 GLN H 179 REMARK 465 SER H 180 REMARK 465 SER H 181 REMARK 465 GLY H 182 REMARK 465 LEU H 183 REMARK 465 TYR H 184 REMARK 465 SER H 185 REMARK 465 LEU H 186 REMARK 465 SER H 187 REMARK 465 SER H 188 REMARK 465 VAL H 189 REMARK 465 VAL H 190 REMARK 465 THR H 191 REMARK 465 VAL H 192 REMARK 465 PRO H 193 REMARK 465 SER H 194 REMARK 465 SER H 195 REMARK 465 SER H 196 REMARK 465 LEU H 197 REMARK 465 GLY H 198 REMARK 465 THR H 199 REMARK 465 GLN H 200 REMARK 465 THR H 201 REMARK 465 TYR H 202 REMARK 465 ILE H 203 REMARK 465 CYS H 204 REMARK 465 ASN H 205 REMARK 465 VAL H 206 REMARK 465 ASN H 207 REMARK 465 HIS H 208 REMARK 465 LYS H 209 REMARK 465 PRO H 210 REMARK 465 SER H 211 REMARK 465 ASN H 212 REMARK 465 THR H 213 REMARK 465 LYS H 214 REMARK 465 VAL H 215 REMARK 465 ASP H 216 REMARK 465 LYS H 217 REMARK 465 ARG H 218 REMARK 465 VAL H 219 REMARK 465 GLU H 220 REMARK 465 PRO H 221 REMARK 465 LYS H 222 REMARK 465 SER H 223 REMARK 465 THR L 109 REMARK 465 VAL L 110 REMARK 465 ALA L 111 REMARK 465 ALA L 112 REMARK 465 PRO L 113 REMARK 465 SER L 114 REMARK 465 VAL L 115 REMARK 465 PHE L 116 REMARK 465 ILE L 117 REMARK 465 PHE L 118 REMARK 465 PRO L 119 REMARK 465 PRO L 120 REMARK 465 SER L 121 REMARK 465 ASP L 122 REMARK 465 GLU L 123 REMARK 465 GLN L 124 REMARK 465 LEU L 125 REMARK 465 LYS L 126 REMARK 465 SER L 127 REMARK 465 GLY L 128 REMARK 465 THR L 129 REMARK 465 ALA L 130 REMARK 465 SER L 131 REMARK 465 VAL L 132 REMARK 465 VAL L 133 REMARK 465 CYS L 134 REMARK 465 LEU L 135 REMARK 465 LEU L 136 REMARK 465 ASN L 137 REMARK 465 ASN L 138 REMARK 465 PHE L 139 REMARK 465 TYR L 140 REMARK 465 PRO L 141 REMARK 465 ARG L 142 REMARK 465 GLU L 143 REMARK 465 ALA L 144 REMARK 465 LYS L 145 REMARK 465 VAL L 146 REMARK 465 GLN L 147 REMARK 465 TRP L 148 REMARK 465 LYS L 149 REMARK 465 VAL L 150 REMARK 465 ASP L 151 REMARK 465 ASN L 152 REMARK 465 ALA L 153 REMARK 465 LEU L 154 REMARK 465 GLN L 155 REMARK 465 SER L 156 REMARK 465 GLY L 157 REMARK 465 ASN L 158 REMARK 465 SER L 159 REMARK 465 GLN L 160 REMARK 465 GLU L 161 REMARK 465 SER L 162 REMARK 465 VAL L 163 REMARK 465 THR L 164 REMARK 465 GLU L 165 REMARK 465 GLN L 166 REMARK 465 ASP L 167 REMARK 465 SER L 168 REMARK 465 LYS L 169 REMARK 465 ASP L 170 REMARK 465 SER L 171 REMARK 465 THR L 172 REMARK 465 TYR L 173 REMARK 465 SER L 174 REMARK 465 LEU L 175 REMARK 465 SER L 176 REMARK 465 SER L 177 REMARK 465 THR L 178 REMARK 465 LEU L 179 REMARK 465 THR L 180 REMARK 465 LEU L 181 REMARK 465 SER L 182 REMARK 465 LYS L 183 REMARK 465 ALA L 184 REMARK 465 ASP L 185 REMARK 465 TYR L 186 REMARK 465 GLU L 187 REMARK 465 LYS L 188 REMARK 465 HIS L 189 REMARK 465 LYS L 190 REMARK 465 VAL L 191 REMARK 465 TYR L 192 REMARK 465 ALA L 193 REMARK 465 CYS L 194 REMARK 465 GLU L 195 REMARK 465 VAL L 196 REMARK 465 THR L 197 REMARK 465 HIS L 198 REMARK 465 GLN L 199 REMARK 465 GLY L 200 REMARK 465 LEU L 201 REMARK 465 SER L 202 REMARK 465 SER L 203 REMARK 465 PRO L 204 REMARK 465 VAL L 205 REMARK 465 THR L 206 REMARK 465 LYS L 207 REMARK 465 SER L 208 REMARK 465 PHE L 209 REMARK 465 ASN L 210 REMARK 465 ARG L 211 REMARK 465 GLY L 212 REMARK 465 GLU L 213 REMARK 465 CYS L 214 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 GLU A 115 CG CD OE1 OE2 REMARK 470 ARG A 242 CG CD NE CZ NH1 NH2 REMARK 470 THR A 299 OG1 CG2 REMARK 470 LYS A 303 CG CD CE NZ REMARK 470 ARG H 16 CG CD NE CZ NH1 NH2 REMARK 470 THR H 28 CG2 REMARK 470 TYR H 59 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LYS H 84 CD CE NZ REMARK 470 ARG L 24 CD NE CZ NH1 NH2 REMARK 470 ARG L 27 CD NE CZ NH1 NH2 REMARK 470 LYS L 39 CG CD CE NZ REMARK 470 ARG L 42 CG CD NE CZ NH1 NH2 REMARK 470 LYS L 103 CG CD CE NZ REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 SER A 22 -82.45 56.68 REMARK 500 SER A 46 -49.78 171.94 REMARK 500 ARG A 75 -9.70 72.66 REMARK 500 GLU A 218 -14.60 74.07 REMARK 500 HIS A 235 -169.85 -121.94 REMARK 500 CYS A 281 -167.92 -104.01 REMARK 500 THR A 299 -65.89 -91.64 REMARK 500 SER A 300 -65.18 -120.56 REMARK 500 GLU A 301 -159.86 42.18 REMARK 500 VAL H 48 -60.38 -106.50 REMARK 500 THR L 30 -114.60 44.59 REMARK 500 ALA L 51 -8.75 72.13 REMARK 500 SER L 52 -5.69 -144.98 REMARK 500 ALA L 84 -176.15 -170.00 REMARK 500 REMARK 500 REMARK: NULL DBREF1 9L2K A 19 338 UNP A0A1S6K8S9_SFTS DBREF2 9L2K A A0A1S6K8S9 18 337 DBREF 9L2K H 1 223 PDB 9L2K 9L2K 1 223 DBREF 9L2K L 1 214 PDB 9L2K 9L2K 1 214 SEQADV 9L2K MET A 1 UNP A0A1S6K8S INITIATING METHIONINE SEQADV 9L2K GLY A 2 UNP A0A1S6K8S EXPRESSION TAG SEQADV 9L2K TRP A 3 UNP A0A1S6K8S EXPRESSION TAG SEQADV 9L2K SER A 4 UNP A0A1S6K8S EXPRESSION TAG SEQADV 9L2K CYS A 5 UNP A0A1S6K8S EXPRESSION TAG SEQADV 9L2K ILE A 6 UNP A0A1S6K8S EXPRESSION TAG SEQADV 9L2K ILE A 7 UNP A0A1S6K8S EXPRESSION TAG SEQADV 9L2K LEU A 8 UNP A0A1S6K8S EXPRESSION TAG SEQADV 9L2K PHE A 9 UNP A0A1S6K8S EXPRESSION TAG SEQADV 9L2K LEU A 10 UNP A0A1S6K8S EXPRESSION TAG SEQADV 9L2K VAL A 11 UNP A0A1S6K8S EXPRESSION TAG SEQADV 9L2K ALA A 12 UNP A0A1S6K8S EXPRESSION TAG SEQADV 9L2K THR A 13 UNP A0A1S6K8S EXPRESSION TAG SEQADV 9L2K ALA A 14 UNP A0A1S6K8S EXPRESSION TAG SEQADV 9L2K THR A 15 UNP A0A1S6K8S EXPRESSION TAG SEQADV 9L2K GLY A 16 UNP A0A1S6K8S EXPRESSION TAG SEQADV 9L2K VAL A 17 UNP A0A1S6K8S EXPRESSION TAG SEQADV 9L2K HIS A 18 UNP A0A1S6K8S EXPRESSION TAG SEQADV 9L2K HIS A 339 UNP A0A1S6K8S EXPRESSION TAG SEQADV 9L2K HIS A 340 UNP A0A1S6K8S EXPRESSION TAG SEQADV 9L2K HIS A 341 UNP A0A1S6K8S EXPRESSION TAG SEQADV 9L2K HIS A 342 UNP A0A1S6K8S EXPRESSION TAG SEQADV 9L2K HIS A 343 UNP A0A1S6K8S EXPRESSION TAG SEQADV 9L2K HIS A 344 UNP A0A1S6K8S EXPRESSION TAG SEQRES 1 A 344 MET GLY TRP SER CYS ILE ILE LEU PHE LEU VAL ALA THR SEQRES 2 A 344 ALA THR GLY VAL HIS SER GLY ASP SER GLY PRO ILE ILE SEQRES 3 A 344 CYS ALA GLY PRO ILE HIS SER ASN LYS SER ALA GLY ILE SEQRES 4 A 344 PRO HIS LEU LEU GLY TYR SER GLU LYS ILE CYS GLN ILE SEQRES 5 A 344 ASP ARG LEU ILE HIS VAL SER SER TRP LEU ARG ASN HIS SEQRES 6 A 344 SER GLN PHE GLN GLY TYR VAL GLY GLN ARG GLY GLY ARG SEQRES 7 A 344 SER GLN VAL SER TYR TYR PRO ALA GLU ASN SER TYR SER SEQRES 8 A 344 ARG TRP SER GLY LEU LEU SER PRO CYS ASP ALA ASP TRP SEQRES 9 A 344 LEU GLY MET LEU VAL VAL LYS LYS ALA ARG GLU SER ASP SEQRES 10 A 344 MET ILE VAL PRO GLY PRO SER TYR LYS GLY LYS VAL PHE SEQRES 11 A 344 PHE GLU ARG PRO THR PHE ASP GLY TYR VAL GLY TRP GLY SEQRES 12 A 344 CYS GLY SER GLY LYS SER ARG THR GLU SER GLY GLU LEU SEQRES 13 A 344 CYS SER SER ASP SER GLY THR SER SER GLY LEU LEU PRO SEQRES 14 A 344 SER ASP ARG VAL LEU TRP ILE GLY ASP VAL ALA CYS GLN SEQRES 15 A 344 LEU MET THR PRO ILE PRO GLU GLU THR PHE LEU GLU LEU SEQRES 16 A 344 LYS SER PHE SER GLN SER GLU PHE PRO ASP ILE CYS LYS SEQRES 17 A 344 ILE ASP GLY ILE VAL PHE ASN GLN CYS GLU GLY GLU SER SEQRES 18 A 344 LEU PRO GLN PRO PHE ASP VAL ALA TRP MET ASP VAL GLY SEQRES 19 A 344 HIS SER HIS LYS ILE ILE MET ARG GLU HIS LYS THR LYS SEQRES 20 A 344 TRP VAL GLN GLU SER SER SER LYS ASP PHE VAL CYS TYR SEQRES 21 A 344 LYS GLU GLY THR GLY PRO CYS SER GLU SER GLU GLU LYS SEQRES 22 A 344 ALA CYS LYS THR SER GLY SER CYS ARG GLY ASP MET GLN SEQRES 23 A 344 PHE CYS LYS VAL ALA GLY CYS GLU HIS GLY GLU GLU THR SEQRES 24 A 344 SER GLU ALA LYS CYS ARG CYS SER LEU VAL HIS LYS PRO SEQRES 25 A 344 GLY GLU VAL VAL VAL SER TYR GLY GLY MET ARG VAL ARG SEQRES 26 A 344 PRO LYS CYS TYR GLY PHE SER ARG MET MET ALA THR LEU SEQRES 27 A 344 HIS HIS HIS HIS HIS HIS SEQRES 1 H 223 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY VAL VAL GLN SEQRES 2 H 223 PRO GLY ARG SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 H 223 PHE THR PHE SER GLY PHE GLY MET HIS TRP VAL ARG GLN SEQRES 4 H 223 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA LEU ILE SER SEQRES 5 H 223 TYR ASP GLY SER ASP THR TYR TYR SER ASP SER VAL LYS SEQRES 6 H 223 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR SEQRES 7 H 223 LEU TYR LEU GLN LEU LYS SER LEU ARG PRO ASP ASP THR SEQRES 8 H 223 ALA VAL TYR TYR CYS VAL GLY ASP ARG ASP TYR PHE GLY SEQRES 9 H 223 SER GLY PHE PHE ASP HIS TRP GLY GLN GLY THR LEU VAL SEQRES 10 H 223 THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE SEQRES 11 H 223 PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR SEQRES 12 H 223 ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU SEQRES 13 H 223 PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER SEQRES 14 H 223 GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY SEQRES 15 H 223 LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SEQRES 16 H 223 SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS SEQRES 17 H 223 LYS PRO SER ASN THR LYS VAL ASP LYS ARG VAL GLU PRO SEQRES 18 H 223 LYS SER SEQRES 1 L 214 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 L 214 SER ILE GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 L 214 ARG HIS ILE THR ASN HIS LEU ASN TRP TYR GLN HIS LYS SEQRES 4 L 214 PRO GLY ARG ALA PRO LYS LEU LEU ILE TYR GLU ALA SER SEQRES 5 L 214 ASN LEU GLN ALA GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 L 214 GLY SER GLY THR ASP PHE THR PHE THR ILE SER SER LEU SEQRES 7 L 214 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN TYR SEQRES 8 L 214 ASP ASN LEU PRO PRO ALA PHE GLY GLY GLY THR LYS VAL SEQRES 9 L 214 ASP ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 L 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 L 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 L 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 L 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 L 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 L 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 L 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 L 214 PHE ASN ARG GLY GLU CYS HET NAG B 1 14 HET NAG B 2 14 HET BMA B 3 11 HET NAG C 1 14 HET NAG C 2 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 4 NAG 4(C8 H15 N O6) FORMUL 4 BMA C6 H12 O6 HELIX 1 AA1 SER A 46 ARG A 54 1 9 HELIX 2 AA2 LEU A 55 SER A 66 1 12 HELIX 3 AA3 GLY A 77 VAL A 81 5 5 HELIX 4 AA4 SER A 89 TRP A 93 5 5 HELIX 5 AA5 SER A 98 LEU A 105 1 8 HELIX 6 AA6 SER A 161 SER A 164 5 4 HELIX 7 AA7 PRO A 169 ASP A 171 5 3 HELIX 8 AA8 PRO A 188 PHE A 203 1 16 HELIX 9 AA9 SER A 253 LYS A 255 5 3 HELIX 10 AB1 SER A 268 GLY A 279 1 12 HELIX 11 AB2 ASP A 284 LYS A 289 1 6 HELIX 12 AB3 THR H 28 PHE H 32 5 5 HELIX 13 AB4 ASP H 62 LYS H 65 5 4 HELIX 14 AB5 ARG H 87 THR H 91 5 5 HELIX 15 AB6 GLN L 79 PHE L 83 5 5 SHEET 1 AA1 2 TYR A 71 VAL A 72 0 SHEET 2 AA1 2 LEU A 167 LEU A 168 1 O LEU A 168 N TYR A 71 SHEET 1 AA2 5 SER A 82 TYR A 84 0 SHEET 2 AA2 5 VAL A 173 ILE A 176 1 O TRP A 175 N SER A 82 SHEET 3 AA2 5 PHE A 130 THR A 135 1 N GLU A 132 O ILE A 176 SHEET 4 AA2 5 GLY A 138 GLY A 143 -1 O GLY A 138 N THR A 135 SHEET 5 AA2 5 VAL A 110 LYS A 112 1 N LYS A 111 O TYR A 139 SHEET 1 AA3 2 LYS A 148 ARG A 150 0 SHEET 2 AA3 2 CYS A 157 SER A 159 -1 O SER A 158 N SER A 149 SHEET 1 AA4 4 ASP A 178 CYS A 181 0 SHEET 2 AA4 4 CYS A 328 LEU A 338 -1 O TYR A 329 N ALA A 180 SHEET 3 AA4 4 ILE A 206 ILE A 209 -1 N CYS A 207 O THR A 337 SHEET 4 AA4 4 ILE A 212 VAL A 213 -1 O ILE A 212 N ILE A 209 SHEET 1 AA5 4 ASP A 178 CYS A 181 0 SHEET 2 AA5 4 CYS A 328 LEU A 338 -1 O TYR A 329 N ALA A 180 SHEET 3 AA5 4 GLN A 224 ASP A 232 -1 N ASP A 232 O CYS A 328 SHEET 4 AA5 4 ILE A 239 MET A 241 -1 O MET A 241 N ALA A 229 SHEET 1 AA6 3 LYS A 245 VAL A 249 0 SHEET 2 AA6 3 GLU A 314 TYR A 319 -1 O SER A 318 N LYS A 245 SHEET 3 AA6 3 MET A 322 VAL A 324 -1 O MET A 322 N TYR A 319 SHEET 1 AA7 4 GLY A 265 PRO A 266 0 SHEET 2 AA7 4 PHE A 257 LYS A 261 -1 N LYS A 261 O GLY A 265 SHEET 3 AA7 4 ARG A 305 LEU A 308 -1 O ARG A 305 N TYR A 260 SHEET 4 AA7 4 ARG A 282 GLY A 283 1 N ARG A 282 O CYS A 306 SHEET 1 AA8 4 GLN H 3 SER H 7 0 SHEET 2 AA8 4 ARG H 19 SER H 25 -1 O SER H 21 N SER H 7 SHEET 3 AA8 4 THR H 78 GLN H 82 -1 O LEU H 79 N CYS H 22 SHEET 4 AA8 4 THR H 69 ASP H 73 -1 N THR H 69 O GLN H 82 SHEET 1 AA9 6 GLY H 10 VAL H 12 0 SHEET 2 AA9 6 THR H 115 VAL H 119 1 O THR H 118 N VAL H 12 SHEET 3 AA9 6 ALA H 92 GLY H 98 -1 N TYR H 94 O THR H 115 SHEET 4 AA9 6 MET H 34 GLN H 39 -1 N VAL H 37 O TYR H 95 SHEET 5 AA9 6 LEU H 45 ILE H 51 -1 O VAL H 48 N TRP H 36 SHEET 6 AA9 6 THR H 58 TYR H 60 -1 O TYR H 59 N LEU H 50 SHEET 1 AB1 4 GLY H 10 VAL H 12 0 SHEET 2 AB1 4 THR H 115 VAL H 119 1 O THR H 118 N VAL H 12 SHEET 3 AB1 4 ALA H 92 GLY H 98 -1 N TYR H 94 O THR H 115 SHEET 4 AB1 4 HIS H 110 TRP H 111 -1 O HIS H 110 N GLY H 98 SHEET 1 AB2 4 THR L 5 SER L 7 0 SHEET 2 AB2 4 VAL L 19 ARG L 24 -1 O THR L 22 N SER L 7 SHEET 3 AB2 4 ASP L 70 ILE L 75 -1 O PHE L 73 N ILE L 21 SHEET 4 AB2 4 PHE L 62 GLY L 66 -1 N SER L 65 O THR L 72 SHEET 1 AB3 6 SER L 10 SER L 12 0 SHEET 2 AB3 6 THR L 102 ASP L 105 1 O ASP L 105 N LEU L 11 SHEET 3 AB3 6 THR L 85 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AB3 6 LEU L 33 HIS L 38 -1 N HIS L 38 O THR L 85 SHEET 5 AB3 6 LYS L 45 TYR L 49 -1 O LYS L 45 N GLN L 37 SHEET 6 AB3 6 ASN L 53 LEU L 54 -1 O ASN L 53 N TYR L 49 SHEET 1 AB4 4 SER L 10 SER L 12 0 SHEET 2 AB4 4 THR L 102 ASP L 105 1 O ASP L 105 N LEU L 11 SHEET 3 AB4 4 THR L 85 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AB4 4 ALA L 97 PHE L 98 -1 O ALA L 97 N GLN L 90 SSBOND 1 CYS A 27 CYS A 50 1555 1555 2.03 SSBOND 2 CYS A 144 CYS A 157 1555 1555 2.03 SSBOND 3 CYS A 181 CYS A 328 1555 1555 2.03 SSBOND 4 CYS A 207 CYS A 217 1555 1555 2.03 SSBOND 5 CYS A 259 CYS A 306 1555 1555 2.03 SSBOND 6 CYS A 267 CYS A 304 1555 1555 2.04 SSBOND 7 CYS A 275 CYS A 281 1555 1555 2.03 SSBOND 8 CYS A 288 CYS A 293 1555 1555 2.03 SSBOND 9 CYS H 22 CYS H 96 1555 1555 2.04 SSBOND 10 CYS L 23 CYS L 88 1555 1555 2.04 LINK ND2 ASN A 34 C1 NAG C 1 1555 1555 1.45 LINK ND2 ASN A 64 C1 NAG B 1 1555 1555 1.43 LINK O4 NAG B 1 C1 NAG B 2 1555 1555 1.45 LINK O4 NAG B 2 C1 BMA B 3 1555 1555 1.44 LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.39 CISPEP 1 TYR A 84 PRO A 85 0 0.77 CISPEP 2 SER L 7 PRO L 8 0 -4.53 CRYST1 64.471 70.346 177.469 90.00 90.18 90.00 C 1 2 1 4 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 0.015511 0.000000 0.000048 0.00000 SCALE2 0.000000 0.014215 0.000000 0.00000 SCALE3 0.000000 0.000000 0.005635 0.00000