HEADER ANTIVIRAL PROTEIN 15-MAY-24 9FC2 TITLE THE CRYSTAL STRUCTURE OF THE SARS-COV-2 RECEPTOR BINDING DOMAIN IN TITLE 2 COMPLEX WITH THE NEUTRALIZING NANOBODY 4. COMPND MOL_ID: 1; COMPND 2 MOLECULE: SPIKE PROTEIN S1; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: NANOBODY 4; COMPND 7 CHAIN: B; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS SOURCE 3 2; SOURCE 4 ORGANISM_TAXID: 2697049; SOURCE 5 GENE: S, 2; SOURCE 6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: CHO LEC. 3.2.8.1; SOURCE 9 EXPRESSION_SYSTEM_TISSUE: OVARY; SOURCE 10 EXPRESSION_SYSTEM_CELL: EPITHELIAL; SOURCE 11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PBJ5-GS; SOURCE 13 MOL_ID: 2; SOURCE 14 ORGANISM_SCIENTIFIC: CAMELUS DROMEDARIUS; SOURCE 15 ORGANISM_TAXID: 9838; SOURCE 16 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 18 EXPRESSION_SYSTEM_CELL_LINE: HEK293F; SOURCE 19 EXPRESSION_SYSTEM_ATCC_NUMBER: CRL-1573; SOURCE 20 EXPRESSION_SYSTEM_ORGAN: KIDNEY; SOURCE 21 EXPRESSION_SYSTEM_TISSUE: EMBRYO; SOURCE 22 EXPRESSION_SYSTEM_CELL: EPITHELIAL; SOURCE 23 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 24 EXPRESSION_SYSTEM_PLASMID: FLAG-MCS-PCDNA3.1 KEYWDS CORONAVIRUS, COVID-19, RBD, SARS-COV-2, SPIKE, NANOBODIES, KEYWDS 2 NEUTRALIZATION, VIRAL PROTEIN, ANTIVIRAL PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR J.M.CASASNOVAS,L.A.FERNANDEZ,K.SILVA REVDAT 1 11-JUN-25 9FC2 0 JRNL AUTH L.CERDAN,K.SILVA,D.RODRIGUEZ-MARTIN,P.PEREZ,M.A.NORIEGA, JRNL AUTH 2 A.ESTEBAN MARTIN,A.GUTIERREZ-ADAN,Y.MARGOLLES,J.A.CORBERA, JRNL AUTH 3 M.A.MARTIN-ACEBES,J.GARCIA-ARRIAZA,J.FERNANDEZ-RECIO, JRNL AUTH 4 L.A.FERNANDEZ,J.M.CASASNOVAS JRNL TITL INTEGRATING IMMUNE LIBRARY PROBING WITH STRUCTURE-BASED JRNL TITL 2 COMPUTATIONAL DESIGN TO DEVELOP POTENT NEUTRALIZING JRNL TITL 3 NANOBODIES AGAINST EMERGING SARS-COV-2 VARIANTS. JRNL REF MABS V. 17 99595 2025 JRNL REFN ESSN 1942-0870 JRNL PMID 40329514 JRNL DOI 10.1080/19420862.2025.2499595 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH J.M.CASASNOVAS,Y.MARGOLLES,M.A.NORIEGA,M.GUZMAN,R.ARRANZ, REMARK 1 AUTH 2 R.MELERO,M.CASANOVA,J.A.CORBERA,N.JIMENEZ-DE-OYA, REMARK 1 AUTH 3 P.GASTAMINZA,U.GARAIGORTA,J.C.SAIZ,M.A.MARTIN-ACEBES, REMARK 1 AUTH 4 L.A.FERNANDEZ REMARK 1 TITL NANOBODIES PROTECTING FROM LETHAL SARS-COV-2 INFECTION REMARK 1 TITL 2 TARGET RECEPTOR BINDING EPITOPES PRESERVED IN VIRUS VARIANTS REMARK 1 TITL 3 OTHER THAN OMICRON. REMARK 1 REF FRONT IMMUNOL V. 13 63831 2022 REMARK 1 REFN ESSN 1664-3224 REMARK 1 PMID 35547740 REMARK 1 DOI 10.1038/S41586-021-04017-W REMARK 2 REMARK 2 RESOLUTION. 1.21 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.20.1_4487 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) : 1.21 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.29 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360 REMARK 3 COMPLETENESS FOR RANGE (%) : 97.2 REMARK 3 NUMBER OF REFLECTIONS : 103164 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.153 REMARK 3 R VALUE (WORKING SET) : 0.153 REMARK 3 FREE R VALUE : 0.170 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030 REMARK 3 FREE R VALUE TEST SET COUNT : 5193 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 42.2900 - 3.7600 1.00 3450 176 0.1495 0.1526 REMARK 3 2 3.7600 - 2.9800 1.00 3404 187 0.1589 0.1623 REMARK 3 3 2.9800 - 2.6100 1.00 3382 176 0.1618 0.1793 REMARK 3 4 2.6100 - 2.3700 1.00 3391 165 0.1629 0.1733 REMARK 3 5 2.3700 - 2.2000 1.00 3401 159 0.1545 0.1564 REMARK 3 6 2.2000 - 2.0700 1.00 3362 179 0.1472 0.1627 REMARK 3 7 2.0700 - 1.9700 1.00 3360 188 0.1391 0.1567 REMARK 3 8 1.9700 - 1.8800 1.00 3354 170 0.1486 0.1719 REMARK 3 9 1.8800 - 1.8100 1.00 3353 186 0.1461 0.1751 REMARK 3 10 1.8100 - 1.7500 1.00 3355 166 0.1422 0.1739 REMARK 3 11 1.7500 - 1.6900 1.00 3372 181 0.1412 0.1706 REMARK 3 12 1.6900 - 1.6400 1.00 3340 195 0.1368 0.1746 REMARK 3 13 1.6400 - 1.6000 1.00 3342 186 0.1357 0.1680 REMARK 3 14 1.6000 - 1.5600 1.00 3343 193 0.1321 0.1751 REMARK 3 15 1.5600 - 1.5300 1.00 3349 185 0.1380 0.1552 REMARK 3 16 1.5300 - 1.4900 1.00 3349 171 0.1473 0.1663 REMARK 3 17 1.4900 - 1.4600 1.00 3330 184 0.1411 0.1830 REMARK 3 18 1.4600 - 1.4400 1.00 3367 173 0.1465 0.1713 REMARK 3 19 1.4400 - 1.4100 1.00 3348 182 0.1476 0.1766 REMARK 3 20 1.4100 - 1.3900 1.00 3391 178 0.1436 0.1936 REMARK 3 21 1.3900 - 1.3600 1.00 3337 150 0.1524 0.2114 REMARK 3 22 1.3600 - 1.3400 1.00 3333 177 0.1539 0.1782 REMARK 3 23 1.3400 - 1.3200 1.00 3325 211 0.1467 0.1898 REMARK 3 24 1.3200 - 1.3000 1.00 3375 145 0.1572 0.2055 REMARK 3 25 1.3000 - 1.2900 1.00 3322 180 0.1634 0.1831 REMARK 3 26 1.2900 - 1.2700 1.00 3369 166 0.1780 0.2100 REMARK 3 27 1.2700 - 1.2600 1.00 951 69 0.1871 0.2604 REMARK 3 28 1.2500 - 1.2400 0.96 2913 157 0.2067 0.2571 REMARK 3 29 1.2400 - 1.2200 1.00 3367 177 0.2109 0.2910 REMARK 3 30 1.2200 - 1.2100 1.00 3336 181 0.2167 0.2517 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.10 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) : 0.123 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.811 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 14.87 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.71 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 : 0.012 2679 REMARK 3 ANGLE : 1.216 3670 REMARK 3 CHIRALITY : 0.102 397 REMARK 3 PLANARITY : 0.013 486 REMARK 3 DIHEDRAL : 6.968 403 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL 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 9FC2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 20-MAY-24. REMARK 100 THE DEPOSITION ID IS D_1292133195. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 14-JUL-23 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 4.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ALBA REMARK 200 BEAMLINE : XALOC REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97926 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 103166 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.210 REMARK 200 RESOLUTION RANGE LOW (A) : 48.832 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.2 REMARK 200 DATA REDUNDANCY : 9.890 REMARK 200 R MERGE (I) : 0.04400 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 22.2450 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.21 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.23 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 8.33 REMARK 200 R MERGE FOR SHELL (I) : 0.81400 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.212 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: MONOCLINIC REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 44.50 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.21 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 22,5 % PEG 8000, 100MM NAAC PH 4.5, REMARK 280 200MM NACL, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z+1/3 REMARK 290 3555 -X+Y,-X,Z+2/3 REMARK 290 4555 -X,-Y,Z+1/2 REMARK 290 5555 Y,-X+Y,Z+5/6 REMARK 290 6555 X-Y,X,Z+1/6 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 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 21.45000 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 42.90000 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 32.17500 REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 53.62500 REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 10.72500 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: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 2910 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 14630 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 1.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B 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 GLY A 330 REMARK 465 SER A 331 REMARK 465 ILE A 332 REMARK 465 LYS A 528 REMARK 465 LYS A 529 REMARK 465 SER A 530 REMARK 465 THR A 531 REMARK 465 ASN A 532 REMARK 465 LEU A 533 REMARK 465 VAL A 534 REMARK 465 PRO A 535 REMARK 465 ARG A 536 REMARK 465 ALA B 121 REMARK 465 LEU B 122 REMARK 465 VAL B 123 REMARK 465 PRO B 124 REMARK 465 ARG B 125 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 O HOH A 890 O HOH A 902 1.88 REMARK 500 O HOH B 322 O HOH B 404 1.90 REMARK 500 O HOH B 384 O HOH B 391 1.93 REMARK 500 O HOH A 862 O HOH A 867 1.95 REMARK 500 ND2 ASN B 72 O HOH B 301 2.01 REMARK 500 O HOH A 897 O HOH B 395 2.04 REMARK 500 O HOH A 824 O HOH A 907 2.09 REMARK 500 O HOH A 707 O HOH A 910 2.10 REMARK 500 O HOH A 840 O HOH A 918 2.12 REMARK 500 O HOH A 834 O HOH A 904 2.15 REMARK 500 O HOH A 706 O HOH A 918 2.15 REMARK 500 O HOH B 382 O HOH B 400 2.17 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 O HOH A 850 O HOH A 881 5554 2.08 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 ALA A 352 43.34 -109.71 REMARK 500 ASN A 422 -53.93 -125.05 REMARK 500 ASN A 487 19.64 57.25 REMARK 500 ASN B 75 52.00 35.17 REMARK 500 ALA B 90 170.15 176.35 REMARK 500 REMARK 500 REMARK: NULL DBREF 9FC2 A 332 534 UNP P0DTC2 SPIKE_SARS2 332 534 DBREF 9FC2 B 1 125 PDB 9FC2 9FC2 1 125 SEQADV 9FC2 GLY A 330 UNP P0DTC2 EXPRESSION TAG SEQADV 9FC2 SER A 331 UNP P0DTC2 EXPRESSION TAG SEQADV 9FC2 PRO A 535 UNP P0DTC2 EXPRESSION TAG SEQADV 9FC2 ARG A 536 UNP P0DTC2 EXPRESSION TAG SEQRES 1 A 207 GLY SER ILE THR ASN LEU CYS PRO PHE GLY GLU VAL PHE SEQRES 2 A 207 ASN ALA THR ARG PHE ALA SER VAL TYR ALA TRP ASN ARG SEQRES 3 A 207 LYS ARG ILE SER ASN CYS VAL ALA ASP TYR SER VAL LEU SEQRES 4 A 207 TYR ASN SER ALA SER PHE SER THR PHE LYS CYS TYR GLY SEQRES 5 A 207 VAL SER PRO THR LYS LEU ASN ASP LEU CYS PHE THR ASN SEQRES 6 A 207 VAL TYR ALA ASP SER PHE VAL ILE ARG GLY ASP GLU VAL SEQRES 7 A 207 ARG GLN ILE ALA PRO GLY GLN THR GLY LYS ILE ALA ASP SEQRES 8 A 207 TYR ASN TYR LYS LEU PRO ASP ASP PHE THR GLY CYS VAL SEQRES 9 A 207 ILE ALA TRP ASN SER ASN ASN LEU ASP SER LYS VAL GLY SEQRES 10 A 207 GLY ASN TYR ASN TYR LEU TYR ARG LEU PHE ARG LYS SER SEQRES 11 A 207 ASN LEU LYS PRO PHE GLU ARG ASP ILE SER THR GLU ILE SEQRES 12 A 207 TYR GLN ALA GLY SER THR PRO CYS ASN GLY VAL GLU GLY SEQRES 13 A 207 PHE ASN CYS TYR PHE PRO LEU GLN SER TYR GLY PHE GLN SEQRES 14 A 207 PRO THR ASN GLY VAL GLY TYR GLN PRO TYR ARG VAL VAL SEQRES 15 A 207 VAL LEU SER PHE GLU LEU LEU HIS ALA PRO ALA THR VAL SEQRES 16 A 207 CYS GLY PRO LYS LYS SER THR ASN LEU VAL PRO ARG SEQRES 1 B 125 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY SER VAL GLN SEQRES 2 B 125 ALA GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 B 125 ASP THR GLY ARG THR CYS ASN LEU VAL TRP TYR ARG GLN SEQRES 4 B 125 ALA PRO GLY LYS GLU LEU GLU PHE VAL SER SER ILE SER SEQRES 5 B 125 ASP GLY SER THR ASN TYR ALA GLY SER VAL LYS GLY ARG SEQRES 6 B 125 PHE THR ILE SER GLN ASP ASN ALA LYS ASN THR VAL TYR SEQRES 7 B 125 LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR ALA VAL SEQRES 8 B 125 TYR TYR CYS ALA ALA THR ILE SER ARG THR GLY SER LEU SEQRES 9 B 125 TRP CYS GLU GLU TYR TRP GLY GLN GLY THR GLN VAL THR SEQRES 10 B 125 VAL SER SER ALA LEU VAL PRO ARG HET NAG A 601 14 HET EDO A 602 10 HET ACT B 201 4 HET EDO B 202 10 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM EDO 1,2-ETHANEDIOL HETNAM ACT ACETATE ION 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 EDO ETHYLENE GLYCOL FORMUL 3 NAG C8 H15 N O6 FORMUL 4 EDO 2(C2 H6 O2) FORMUL 5 ACT C2 H3 O2 1- FORMUL 7 HOH *364(H2 O) HELIX 1 AA1 PRO A 337 ASN A 343 1 7 HELIX 2 AA2 SER A 349 TRP A 353 5 5 HELIX 3 AA3 ASP A 364 SER A 371 1 8 HELIX 4 AA4 SER A 383 ASP A 389 5 7 HELIX 5 AA5 ASP A 405 ILE A 410 5 6 HELIX 6 AA6 GLY A 416 ASN A 422 1 7 HELIX 7 AA7 SER A 438 SER A 443 1 6 HELIX 8 AA8 GLY A 502 TYR A 505 5 4 HELIX 9 AA9 LYS B 85 THR B 89 5 5 SHEET 1 AA1 5 ASN A 354 ILE A 358 0 SHEET 2 AA1 5 ASN A 394 ARG A 403 -1 O VAL A 395 N ILE A 358 SHEET 3 AA1 5 PRO A 507 GLU A 516 -1 O VAL A 512 N ASP A 398 SHEET 4 AA1 5 GLY A 431 ASN A 437 -1 N CYS A 432 O LEU A 513 SHEET 5 AA1 5 THR A 376 TYR A 380 -1 N TYR A 380 O GLY A 431 SHEET 1 AA2 3 CYS A 361 VAL A 362 0 SHEET 2 AA2 3 VAL A 524 CYS A 525 1 O CYS A 525 N CYS A 361 SHEET 3 AA2 3 CYS A 391 PHE A 392 -1 N PHE A 392 O VAL A 524 SHEET 1 AA3 2 LEU A 452 ARG A 454 0 SHEET 2 AA3 2 LEU A 492 SER A 494 -1 O GLN A 493 N TYR A 453 SHEET 1 AA4 2 TYR A 473 GLN A 474 0 SHEET 2 AA4 2 CYS A 488 TYR A 489 -1 O TYR A 489 N TYR A 473 SHEET 1 AA5 7 VAL A 483 GLU A 484 0 SHEET 2 AA5 7 SER B 55 ALA B 59 1 O TYR B 58 N GLU A 484 SHEET 3 AA5 7 GLU B 46 SER B 52 -1 N VAL B 48 O ALA B 59 SHEET 4 AA5 7 THR B 28 GLN B 39 -1 N TRP B 36 O SER B 49 SHEET 5 AA5 7 ALA B 90 ARG B 100 -1 O ALA B 95 N VAL B 35 SHEET 6 AA5 7 THR B 114 SER B 119 -1 O THR B 114 N TYR B 92 SHEET 7 AA5 7 GLY B 10 GLN B 13 1 N VAL B 12 O THR B 117 SHEET 1 AA6 6 VAL A 483 GLU A 484 0 SHEET 2 AA6 6 SER B 55 ALA B 59 1 O TYR B 58 N GLU A 484 SHEET 3 AA6 6 GLU B 46 SER B 52 -1 N VAL B 48 O ALA B 59 SHEET 4 AA6 6 THR B 28 GLN B 39 -1 N TRP B 36 O SER B 49 SHEET 5 AA6 6 ALA B 90 ARG B 100 -1 O ALA B 95 N VAL B 35 SHEET 6 AA6 6 GLU B 107 TRP B 110 -1 O GLU B 107 N ILE B 98 SHEET 1 AA7 4 VAL B 2 SER B 7 0 SHEET 2 AA7 4 LEU B 18 GLY B 26 -1 O ALA B 23 N VAL B 5 SHEET 3 AA7 4 THR B 76 MET B 81 -1 O MET B 81 N LEU B 18 SHEET 4 AA7 4 PHE B 66 GLN B 70 -1 N THR B 67 O GLN B 80 SSBOND 1 CYS A 336 CYS A 361 1555 1555 2.05 SSBOND 2 CYS A 379 CYS A 432 1555 1555 2.07 SSBOND 3 CYS A 391 CYS A 525 1555 1555 2.05 SSBOND 4 CYS A 480 CYS A 488 1555 1555 2.05 SSBOND 5 CYS B 22 CYS B 94 1555 1555 2.07 SSBOND 6 CYS B 32 CYS B 106 1555 1555 2.02 LINK ND2 ASN A 343 C1 NAG A 601 1555 1555 1.43 CRYST1 97.664 97.664 64.350 90.00 90.00 120.00 P 61 6 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 0.010239 0.005912 0.000000 0.00000 SCALE2 0.000000 0.011823 0.000000 0.00000 SCALE3 0.000000 0.000000 0.015540 0.00000