HEADER ANTIVIRAL PROTEIN 15-MAY-24 9FCM TITLE SINGLE-DOMAIN ANTIBODY BINDING THE SARS-COV2 S2 COMPND MOL_ID: 1; COMPND 2 MOLECULE: SINGLE-DOMAIN ANTIBODY R3DC23; COMPND 3 CHAIN: A, B, C; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: SPIKE PROTEIN S2'; COMPND 7 CHAIN: D, E, F; COMPND 8 ENGINEERED: YES; COMPND 9 OTHER_DETAILS: H1159-K1211 OF THE SARS-COV-2 SPIKE GP AT THE N- COMPND 10 TERMINUS RESULT FROM 3C PROTEASE CLEAVAGE SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 3 ORGANISM_TAXID: 9844; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS SOURCE 8 2; SOURCE 9 ORGANISM_TAXID: 2697049; SOURCE 10 GENE: S, 2; SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS SINGLE DOMAIN ANITBODIES VIRAL PROTEINS SARS-COV2, ANTIVIRAL PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR I.VANN MOLLE,H.REMAUT REVDAT 1 21-MAY-25 9FCM 0 JRNL AUTH S.DE CAE,I.VAN MOLLE,L.VAN SCHIE,S.R.SHOEMAKER,J.DECKERS, JRNL AUTH 2 N.DEBEUF,S.LAMEIRE,W.NERINCKX,K.ROOSE,D.FIJALKOWSKA,S.DEVOS, JRNL AUTH 3 A.S.DE SMET,J.MARCHAN,T.VENNEMAN,K.SEEDY,L.MUJANOVIC, JRNL AUTH 4 M.BALLEGEER,M.VANHEERSWYNGHELS,C.DE WOLF,H.DEMOL, JRNL AUTH 5 J.ZUALLAERT,P.VANHAVERBEKE,G.GHASSABEH,C.LONIGRO,V.BOCKSTAL, JRNL AUTH 6 M.RINALDI,R.ABDELNABI,J.NEYTS,S.MARQUSEE,B.N.LAMBRECHT, JRNL AUTH 7 N.CALLEWAERT,H.REMAUT,X.SAELENS,B.SCHEPENS JRNL TITL ULTRAPOTENT SARS CORONAVIRUS-NEUTRALIZING SINGLE-DOMAIN JRNL TITL 2 ANTIBODIES THAT BIND A CONSERVED MEMBRANE PROXIMAL EPITOPE JRNL TITL 3 OF THE SPIKE JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 1.94 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.21_5207 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) : 1.94 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 82.64 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 78.0 REMARK 3 NUMBER OF REFLECTIONS : 39359 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.202 REMARK 3 R VALUE (WORKING SET) : 0.200 REMARK 3 FREE R VALUE : 0.247 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.980 REMARK 3 FREE R VALUE TEST SET COUNT : 1960 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 82.6400 - 4.6700 1.00 3620 181 0.1868 0.2108 REMARK 3 2 4.6700 - 3.7100 1.00 3473 185 0.1513 0.1995 REMARK 3 3 3.7100 - 3.2400 1.00 3433 191 0.1773 0.2324 REMARK 3 4 3.2400 - 2.9400 1.00 3433 186 0.2044 0.2635 REMARK 3 5 2.9400 - 2.7300 1.00 3421 167 0.2190 0.2673 REMARK 3 6 2.7300 - 2.5700 1.00 3419 188 0.2272 0.2634 REMARK 3 7 2.5700 - 2.4400 0.99 3370 156 0.2206 0.2664 REMARK 3 8 2.4400 - 2.3300 0.90 3049 160 0.2304 0.3124 REMARK 3 9 2.3300 - 2.2400 0.78 2644 141 0.2278 0.2536 REMARK 3 10 2.2400 - 2.1700 0.69 2344 131 0.2377 0.2567 REMARK 3 11 2.1700 - 2.1000 0.60 2007 111 0.2409 0.3019 REMARK 3 12 2.1000 - 2.0400 0.48 1661 85 0.2439 0.2906 REMARK 3 13 2.0400 - 1.9900 0.36 1209 60 0.2557 0.3614 REMARK 3 14 1.9900 - 1.9400 0.09 316 18 0.2904 0.3001 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) : 0.226 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.067 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 18.28 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.66 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 : 0.007 4061 REMARK 3 ANGLE : 0.945 5494 REMARK 3 CHIRALITY : 0.058 587 REMARK 3 PLANARITY : 0.009 713 REMARK 3 DIHEDRAL : 17.744 1459 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 1 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: ALL REMARK 3 ORIGIN FOR THE GROUP (A): 20.4692 17.0188 42.5052 REMARK 3 T TENSOR REMARK 3 T11: 0.0783 T22: 0.1311 REMARK 3 T33: 0.1296 T12: -0.0046 REMARK 3 T13: -0.0581 T23: 0.0081 REMARK 3 L TENSOR REMARK 3 L11: 0.4032 L22: 1.6021 REMARK 3 L33: 0.6113 L12: -0.3824 REMARK 3 L13: -0.1415 L23: 0.2995 REMARK 3 S TENSOR REMARK 3 S11: -0.0364 S12: -0.0421 S13: -0.0653 REMARK 3 S21: 0.1197 S22: -0.0118 S23: -0.1385 REMARK 3 S31: 0.0240 S32: -0.0274 S33: 0.0334 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : 2 REMARK 3 NCS GROUP : ens_1 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "A" and (resid 1 through 61 or REMARK 3 resid 67 through 107 or resid 109 through REMARK 3 113 or resid 115 through 126)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "B" and (resid 1 through 61 or REMARK 3 resid 67 through 107 or resid 109 through REMARK 3 113 or resid 115 through 126)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 3 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "C" and (resid 1 through 61 or REMARK 3 resid 67 through 107 or resid 109 through REMARK 3 113 or resid 115 through 126)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS GROUP : ens_2 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "D" and (resid 1169 through 1184 REMARK 3 or resid 1186 through 1194 or resid 1196 REMARK 3 through 1209)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "E" and (resid 1169 through 1184 REMARK 3 or resid 1186 through 1194 or resid 1196 REMARK 3 through 1209)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 3 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "F" and (resid 1169 through 1184 REMARK 3 or resid 1186 through 1194 or resid 1196 REMARK 3 through 1209)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 9FCM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-MAY-24. REMARK 100 THE DEPOSITION ID IS D_1292138535. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 23-JAN-23 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 : DIAMOND REMARK 200 BEAMLINE : I24 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.61990 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : AUTOPROC REMARK 200 DATA SCALING SOFTWARE : AUTOPROC REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39377 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.937 REMARK 200 RESOLUTION RANGE LOW (A) : 82.640 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 95.2 REMARK 200 DATA REDUNDANCY : 13.80 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 8.3000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.94 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.05 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL 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: MORDA REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 50.26 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MAGNESIUM CHLORIDE HEXAHYDRATE, REMARK 280 0.1 M SODIUM CITRATE PH 5.0, AND 15% PEG4000, VAPOR DIFFUSION, REMARK 280 SITTING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2 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,Y,-Z REMARK 290 4555 X,-Y,-Z REMARK 290 5555 X+1/2,Y+1/2,Z+1/2 REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2 REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2 REMARK 290 8555 X+1/2,-Y+1/2,-Z+1/2 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 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 45.20650 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 49.40000 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 75.38150 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 45.20650 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 49.40000 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 75.38150 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 45.20650 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 49.40000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 75.38150 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 45.20650 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 49.40000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 75.38150 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: HEXAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F 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 SER A 63 REMARK 465 MET A 64 REMARK 465 LYS A 65 REMARK 465 GLY A 66 REMARK 465 THR A 127 REMARK 465 VAL A 128 REMARK 465 SER A 129 REMARK 465 SER A 130 REMARK 465 ALA A 131 REMARK 465 ALA A 132 REMARK 465 ALA A 133 REMARK 465 TYR A 134 REMARK 465 PRO A 135 REMARK 465 TYR A 136 REMARK 465 ASP A 137 REMARK 465 VAL A 138 REMARK 465 PRO A 139 REMARK 465 ASP A 140 REMARK 465 TYR A 141 REMARK 465 GLY A 142 REMARK 465 SER A 143 REMARK 465 HIS A 144 REMARK 465 HIS A 145 REMARK 465 HIS A 146 REMARK 465 HIS A 147 REMARK 465 HIS A 148 REMARK 465 HIS A 149 REMARK 465 ASP B 62 REMARK 465 SER B 63 REMARK 465 MET B 64 REMARK 465 LYS B 65 REMARK 465 ALA B 131 REMARK 465 ALA B 132 REMARK 465 ALA B 133 REMARK 465 TYR B 134 REMARK 465 PRO B 135 REMARK 465 TYR B 136 REMARK 465 ASP B 137 REMARK 465 VAL B 138 REMARK 465 PRO B 139 REMARK 465 ASP B 140 REMARK 465 TYR B 141 REMARK 465 GLY B 142 REMARK 465 SER B 143 REMARK 465 HIS B 144 REMARK 465 HIS B 145 REMARK 465 HIS B 146 REMARK 465 HIS B 147 REMARK 465 HIS B 148 REMARK 465 HIS B 149 REMARK 465 ASP C 62 REMARK 465 SER C 63 REMARK 465 MET C 64 REMARK 465 LYS C 65 REMARK 465 ALA C 133 REMARK 465 TYR C 134 REMARK 465 PRO C 135 REMARK 465 TYR C 136 REMARK 465 ASP C 137 REMARK 465 VAL C 138 REMARK 465 PRO C 139 REMARK 465 ASP C 140 REMARK 465 TYR C 141 REMARK 465 GLY C 142 REMARK 465 SER C 143 REMARK 465 HIS C 144 REMARK 465 HIS C 145 REMARK 465 HIS C 146 REMARK 465 HIS C 147 REMARK 465 HIS C 148 REMARK 465 HIS C 149 REMARK 465 GLY D 1157 REMARK 465 PRO D 1158 REMARK 465 HIS D 1159 REMARK 465 THR D 1160 REMARK 465 SER D 1161 REMARK 465 PRO D 1162 REMARK 465 ASP D 1163 REMARK 465 VAL D 1164 REMARK 465 ASP D 1165 REMARK 465 LEU D 1166 REMARK 465 GLY E 1157 REMARK 465 PRO E 1158 REMARK 465 HIS E 1159 REMARK 465 THR E 1160 REMARK 465 SER E 1161 REMARK 465 PRO E 1162 REMARK 465 ASP E 1163 REMARK 465 VAL E 1164 REMARK 465 ASP E 1165 REMARK 465 ILE E 1210 REMARK 465 LYS E 1211 REMARK 465 GLY F 1157 REMARK 465 PRO F 1158 REMARK 465 HIS F 1159 REMARK 465 THR F 1160 REMARK 465 SER F 1161 REMARK 465 PRO F 1162 REMARK 465 ASP F 1163 REMARK 465 VAL F 1164 REMARK 465 ASP F 1165 REMARK 465 LEU F 1166 REMARK 465 GLY F 1167 REMARK 465 ASP F 1168 REMARK 465 ILE F 1210 REMARK 465 LYS F 1211 REMARK 480 REMARK 480 ZERO OCCUPANCY ATOM REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 480 M RES C SSEQI ATOMS REMARK 480 GLN A 5 CD REMARK 480 ARG A 27 CG CZ REMARK 480 GLN B 1 CD REMARK 480 LEU B 18 CD2 REMARK 480 GLN B 39 NE2 REMARK 480 GLN B 122 CD REMARK 480 LYS C 43 N REMARK 480 GLU C 44 CD REMARK 480 GLU C 89 CD REMARK 480 ASN D 1178 CG REMARK 480 GLU D 1188 CD REMARK 480 TYR D 1206 CB CG CZ REMARK 480 GLU D 1207 CD REMARK 480 ARG E 1185 CZ REMARK 480 LYS E 1191 CD REMARK 480 GLU F 1188 CD REMARK 480 GLU F 1202 CD 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 NH1 ARG C 45 O HOH C 201 2.10 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 SER A 85 71.35 45.80 REMARK 500 LYS B 103 30.49 -99.90 REMARK 500 ILE D1169 -54.55 73.13 REMARK 500 REMARK 500 REMARK: NULL DBREF 9FCM A 1 149 PDB 9FCM 9FCM 1 149 DBREF 9FCM B 1 149 PDB 9FCM 9FCM 1 149 DBREF 9FCM C 1 149 PDB 9FCM 9FCM 1 149 DBREF 9FCM D 1159 1211 UNP P0DTC2 SPIKE_SARS2 1159 1211 DBREF 9FCM E 1159 1211 UNP P0DTC2 SPIKE_SARS2 1159 1211 DBREF 9FCM F 1159 1211 UNP P0DTC2 SPIKE_SARS2 1159 1211 SEQADV 9FCM GLY D 1157 UNP P0DTC2 EXPRESSION TAG SEQADV 9FCM PRO D 1158 UNP P0DTC2 EXPRESSION TAG SEQADV 9FCM GLY E 1157 UNP P0DTC2 EXPRESSION TAG SEQADV 9FCM PRO E 1158 UNP P0DTC2 EXPRESSION TAG SEQADV 9FCM GLY F 1157 UNP P0DTC2 EXPRESSION TAG SEQADV 9FCM PRO F 1158 UNP P0DTC2 EXPRESSION TAG SEQRES 1 A 149 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 A 149 ALA GLY ASP SER LEU THR LEU SER CYS ALA VAL SER GLY SEQRES 3 A 149 ARG ILE PHE SER THR TYR THR MET GLY TRP PHE ARG GLN SEQRES 4 A 149 ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA ALA VAL ARG SEQRES 5 A 149 TRP GLY ALA GLY THR ILE TYR TYR ALA ASP SER MET LYS SEQRES 6 A 149 GLY ARG PHE THR ILE SER ARG ASP SER ALA LYS ASN THR SEQRES 7 A 149 VAL ASP LEU GLN MET ASN SER THR LYS PRO GLU ASP THR SEQRES 8 A 149 ALA VAL TYR TYR CYS GLY ALA ALA TYR VAL SER LYS ALA SEQRES 9 A 149 ASN TYR GLY SER LEU TRP TYR GLN ASP SER ARG ARG TYR SEQRES 10 A 149 ASP TYR TRP GLY GLN GLY THR GLN VAL THR VAL SER SER SEQRES 11 A 149 ALA ALA ALA TYR PRO TYR ASP VAL PRO ASP TYR GLY SER SEQRES 12 A 149 HIS HIS HIS HIS HIS HIS SEQRES 1 B 149 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 B 149 ALA GLY ASP SER LEU THR LEU SER CYS ALA VAL SER GLY SEQRES 3 B 149 ARG ILE PHE SER THR TYR THR MET GLY TRP PHE ARG GLN SEQRES 4 B 149 ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA ALA VAL ARG SEQRES 5 B 149 TRP GLY ALA GLY THR ILE TYR TYR ALA ASP SER MET LYS SEQRES 6 B 149 GLY ARG PHE THR ILE SER ARG ASP SER ALA LYS ASN THR SEQRES 7 B 149 VAL ASP LEU GLN MET ASN SER THR LYS PRO GLU ASP THR SEQRES 8 B 149 ALA VAL TYR TYR CYS GLY ALA ALA TYR VAL SER LYS ALA SEQRES 9 B 149 ASN TYR GLY SER LEU TRP TYR GLN ASP SER ARG ARG TYR SEQRES 10 B 149 ASP TYR TRP GLY GLN GLY THR GLN VAL THR VAL SER SER SEQRES 11 B 149 ALA ALA ALA TYR PRO TYR ASP VAL PRO ASP TYR GLY SER SEQRES 12 B 149 HIS HIS HIS HIS HIS HIS SEQRES 1 C 149 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 C 149 ALA GLY ASP SER LEU THR LEU SER CYS ALA VAL SER GLY SEQRES 3 C 149 ARG ILE PHE SER THR TYR THR MET GLY TRP PHE ARG GLN SEQRES 4 C 149 ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA ALA VAL ARG SEQRES 5 C 149 TRP GLY ALA GLY THR ILE TYR TYR ALA ASP SER MET LYS SEQRES 6 C 149 GLY ARG PHE THR ILE SER ARG ASP SER ALA LYS ASN THR SEQRES 7 C 149 VAL ASP LEU GLN MET ASN SER THR LYS PRO GLU ASP THR SEQRES 8 C 149 ALA VAL TYR TYR CYS GLY ALA ALA TYR VAL SER LYS ALA SEQRES 9 C 149 ASN TYR GLY SER LEU TRP TYR GLN ASP SER ARG ARG TYR SEQRES 10 C 149 ASP TYR TRP GLY GLN GLY THR GLN VAL THR VAL SER SER SEQRES 11 C 149 ALA ALA ALA TYR PRO TYR ASP VAL PRO ASP TYR GLY SER SEQRES 12 C 149 HIS HIS HIS HIS HIS HIS SEQRES 1 D 55 GLY PRO HIS THR SER PRO ASP VAL ASP LEU GLY ASP ILE SEQRES 2 D 55 SER GLY ILE ASN ALA SER VAL VAL ASN ILE GLN LYS GLU SEQRES 3 D 55 ILE ASP ARG LEU ASN GLU VAL ALA LYS ASN LEU ASN GLU SEQRES 4 D 55 SER LEU ILE ASP LEU GLN GLU LEU GLY LYS TYR GLU GLN SEQRES 5 D 55 TYR ILE LYS SEQRES 1 E 55 GLY PRO HIS THR SER PRO ASP VAL ASP LEU GLY ASP ILE SEQRES 2 E 55 SER GLY ILE ASN ALA SER VAL VAL ASN ILE GLN LYS GLU SEQRES 3 E 55 ILE ASP ARG LEU ASN GLU VAL ALA LYS ASN LEU ASN GLU SEQRES 4 E 55 SER LEU ILE ASP LEU GLN GLU LEU GLY LYS TYR GLU GLN SEQRES 5 E 55 TYR ILE LYS SEQRES 1 F 55 GLY PRO HIS THR SER PRO ASP VAL ASP LEU GLY ASP ILE SEQRES 2 F 55 SER GLY ILE ASN ALA SER VAL VAL ASN ILE GLN LYS GLU SEQRES 3 F 55 ILE ASP ARG LEU ASN GLU VAL ALA LYS ASN LEU ASN GLU SEQRES 4 F 55 SER LEU ILE ASP LEU GLN GLU LEU GLY LYS TYR GLU GLN SEQRES 5 F 55 TYR ILE LYS HET CL A 201 1 HETNAM CL CHLORIDE ION FORMUL 7 CL CL 1- FORMUL 8 HOH *277(H2 O) HELIX 1 AA1 LYS A 87 THR A 91 5 5 HELIX 2 AA2 LYS A 103 GLY A 107 5 5 HELIX 3 AA3 LEU A 109 TYR A 117 5 9 HELIX 4 AA4 LYS B 87 THR B 91 5 5 HELIX 5 AA5 LYS B 103 GLY B 107 5 5 HELIX 6 AA6 LEU B 109 TYR B 117 5 9 HELIX 7 AA7 LYS C 87 THR C 91 5 5 HELIX 8 AA8 LYS C 103 GLY C 107 5 5 HELIX 9 AA9 LEU C 109 TYR C 117 5 9 HELIX 10 AB1 SER D 1170 LYS D 1205 1 36 HELIX 11 AB2 GLY E 1167 LYS E 1205 1 39 HELIX 12 AB3 SER F 1170 GLY F 1204 1 35 HELIX 13 AB4 LYS F 1205 GLU F 1207 5 3 SHEET 1 AA1 4 VAL A 2 SER A 7 0 SHEET 2 AA1 4 LEU A 18 GLY A 26 -1 O ALA A 23 N GLN A 5 SHEET 3 AA1 4 THR A 78 MET A 83 -1 O MET A 83 N LEU A 18 SHEET 4 AA1 4 PHE A 68 ASP A 73 -1 N THR A 69 O GLN A 82 SHEET 1 AA2 5 ILE A 58 TYR A 60 0 SHEET 2 AA2 5 GLU A 46 ARG A 52 -1 N ALA A 50 O TYR A 59 SHEET 3 AA2 5 THR A 33 GLN A 39 -1 N TRP A 36 O ALA A 49 SHEET 4 AA2 5 ALA A 92 ALA A 99 -1 O TYR A 95 N PHE A 37 SHEET 5 AA2 5 TYR A 119 TRP A 120 -1 O TYR A 119 N ALA A 98 SHEET 1 AA3 5 ILE A 58 TYR A 60 0 SHEET 2 AA3 5 GLU A 46 ARG A 52 -1 N ALA A 50 O TYR A 59 SHEET 3 AA3 5 THR A 33 GLN A 39 -1 N TRP A 36 O ALA A 49 SHEET 4 AA3 5 ALA A 92 ALA A 99 -1 O TYR A 95 N PHE A 37 SHEET 5 AA3 5 THR A 124 VAL A 126 -1 O VAL A 126 N ALA A 92 SHEET 1 AA4 4 VAL B 2 SER B 7 0 SHEET 2 AA4 4 LEU B 18 GLY B 26 -1 O SER B 25 N GLN B 3 SHEET 3 AA4 4 THR B 78 MET B 83 -1 O MET B 83 N LEU B 18 SHEET 4 AA4 4 PHE B 68 ASP B 73 -1 N THR B 69 O GLN B 82 SHEET 1 AA5 6 GLY B 10 GLN B 13 0 SHEET 2 AA5 6 THR B 124 SER B 129 1 O GLN B 125 N GLY B 10 SHEET 3 AA5 6 ALA B 92 ALA B 99 -1 N TYR B 94 O THR B 124 SHEET 4 AA5 6 THR B 33 GLN B 39 -1 N PHE B 37 O TYR B 95 SHEET 5 AA5 6 GLU B 46 ARG B 52 -1 O ALA B 49 N TRP B 36 SHEET 6 AA5 6 ILE B 58 TYR B 60 -1 O TYR B 59 N ALA B 50 SHEET 1 AA6 4 GLY B 10 GLN B 13 0 SHEET 2 AA6 4 THR B 124 SER B 129 1 O GLN B 125 N GLY B 10 SHEET 3 AA6 4 ALA B 92 ALA B 99 -1 N TYR B 94 O THR B 124 SHEET 4 AA6 4 TYR B 119 TRP B 120 -1 O TYR B 119 N ALA B 98 SHEET 1 AA7 4 VAL C 2 SER C 7 0 SHEET 2 AA7 4 LEU C 18 GLY C 26 -1 O ALA C 23 N GLN C 5 SHEET 3 AA7 4 THR C 78 MET C 83 -1 O MET C 83 N LEU C 18 SHEET 4 AA7 4 PHE C 68 ASP C 73 -1 N SER C 71 O ASP C 80 SHEET 1 AA8 6 GLY C 10 GLN C 13 0 SHEET 2 AA8 6 THR C 124 SER C 129 1 O SER C 129 N VAL C 12 SHEET 3 AA8 6 ALA C 92 ALA C 99 -1 N TYR C 94 O THR C 124 SHEET 4 AA8 6 THR C 33 GLN C 39 -1 N PHE C 37 O TYR C 95 SHEET 5 AA8 6 GLU C 46 ARG C 52 -1 O GLU C 46 N ARG C 38 SHEET 6 AA8 6 ILE C 58 TYR C 60 -1 O TYR C 59 N ALA C 50 SHEET 1 AA9 4 GLY C 10 GLN C 13 0 SHEET 2 AA9 4 THR C 124 SER C 129 1 O SER C 129 N VAL C 12 SHEET 3 AA9 4 ALA C 92 ALA C 99 -1 N TYR C 94 O THR C 124 SHEET 4 AA9 4 TYR C 119 TRP C 120 -1 O TYR C 119 N ALA C 98 SSBOND 1 CYS A 22 CYS A 96 1555 1555 2.04 SSBOND 2 CYS B 22 CYS B 96 1555 1555 2.06 SSBOND 3 CYS C 22 CYS C 96 1555 1555 2.06 CRYST1 90.413 98.800 150.763 90.00 90.00 90.00 I 2 2 2 24 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 0.011060 0.000000 0.000000 0.00000 SCALE2 0.000000 0.010121 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006633 0.00000 MTRIX1 1 -0.362535 0.877123 0.314998 0.35738 1 MTRIX2 1 -0.154892 0.276584 -0.948425 55.51302 1 MTRIX3 1 -0.919009 -0.392627 0.035588 66.76134 1 MTRIX1 2 -0.172318 -0.203621 -0.963766 67.62739 1 MTRIX2 2 0.930213 0.288230 -0.227215 1.32064 1 MTRIX3 2 0.324052 -0.935661 0.139743 44.64378 1 MTRIX1 3 -0.342594 0.904595 0.253649 2.08007 1 MTRIX2 3 -0.143730 0.216343 -0.965680 57.19321 1 MTRIX3 3 -0.928424 -0.367293 0.055900 66.00695 1 MTRIX1 4 -0.244183 -0.184622 -0.951992 69.39691 1 MTRIX2 4 0.916608 0.276518 -0.288733 4.67723 1 MTRIX3 4 0.316550 -0.943108 0.101705 47.48251 1