HEADER IMMUNE SYSTEM 11-JUN-24 9C7X TITLE CRYSTAL STRUCTURE OF SARS-COV-2 ANTIBODY 1H06 IN COMPLEX WITH A HR2 TITLE 2 PEPTIDE COMPND MOL_ID: 1; COMPND 2 MOLECULE: HEAVY CHAIN OF SARS-COV-2 ANTIBODY 1H06; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: LIGHT CHAIN OF SARS-COV-2 ANTIBODY 1H06; COMPND 7 CHAIN: B; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: SPIKE PROTEIN S2'; COMPND 11 CHAIN: C; COMPND 12 ENGINEERED: YES; COMPND 13 OTHER_DETAILS: ACETYLATED AT N-TERMINUS SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_TAXID: 10090; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 8 ORGANISM_TAXID: 10090; SOURCE 9 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 11 MOL_ID: 3; SOURCE 12 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS SOURCE 13 2; SOURCE 14 ORGANISM_TAXID: 2697049; SOURCE 15 GENE: S, 2; SOURCE 16 EXPRESSION_SYSTEM: SYNTHETIC CONSTRUCT; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 32630 KEYWDS ANTIBODY, HEPTAD REPEAT 2, HR2, SARS-COV-2, SPIKE, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR D.J.VAN WAZER,T.ZHOU,P.D.KWONG REVDAT 1 18-JUN-25 9C7X 0 JRNL AUTH M.SASTRY JRNL TITL SARS-COV-2 PEPTIDE IMMUNIZATION IN MICE ELICITS BROADLY JRNL TITL 2 NEUTRALIZING ANTIBODIES TARGETING CRYPTIC S2 HELICAL-STEM JRNL TITL 3 EPITOPE JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 1.96 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 : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.96 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.89 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330 REMARK 3 COMPLETENESS FOR RANGE (%) : 96.9 REMARK 3 NUMBER OF REFLECTIONS : 33251 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.175 REMARK 3 R VALUE (WORKING SET) : 0.172 REMARK 3 FREE R VALUE : 0.215 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 6.010 REMARK 3 FREE R VALUE TEST SET COUNT : 1999 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 45.8900 - 4.7200 1.00 2479 158 0.1667 0.2171 REMARK 3 2 4.7200 - 3.7500 1.00 2352 150 0.1449 0.1777 REMARK 3 3 3.7500 - 3.2700 1.00 2334 150 0.1614 0.1924 REMARK 3 4 3.2700 - 2.9700 1.00 2315 148 0.1654 0.1975 REMARK 3 5 2.9700 - 2.7600 1.00 2296 146 0.1747 0.2070 REMARK 3 6 2.7600 - 2.6000 0.99 2248 145 0.1832 0.2368 REMARK 3 7 2.6000 - 2.4700 0.97 2232 143 0.1916 0.2325 REMARK 3 8 2.4700 - 2.3600 0.97 2208 141 0.1837 0.2789 REMARK 3 9 2.3600 - 2.2700 0.96 2187 140 0.1830 0.2341 REMARK 3 10 2.2700 - 2.1900 0.96 2188 140 0.1800 0.2439 REMARK 3 11 2.1900 - 2.1200 0.94 2131 136 0.1852 0.2313 REMARK 3 12 2.1200 - 2.0600 0.94 2115 136 0.2091 0.2295 REMARK 3 13 2.0600 - 2.0100 0.93 2097 133 0.2135 0.2448 REMARK 3 14 2.0100 - 1.9600 0.91 2070 133 0.2336 0.3065 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) : 0.200 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.920 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL 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 : 0.010 3554 REMARK 3 ANGLE : 1.141 4837 REMARK 3 CHIRALITY : 0.068 553 REMARK 3 PLANARITY : 0.009 615 REMARK 3 DIHEDRAL : 6.247 486 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 13 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 17 ) REMARK 3 ORIGIN FOR THE GROUP (A): -23.2726 22.7895 -41.2559 REMARK 3 T TENSOR REMARK 3 T11: 0.3280 T22: 0.3338 REMARK 3 T33: 0.2402 T12: -0.0555 REMARK 3 T13: 0.0728 T23: -0.0279 REMARK 3 L TENSOR REMARK 3 L11: 3.6342 L22: 3.9991 REMARK 3 L33: 6.8710 L12: -1.1274 REMARK 3 L13: 1.3558 L23: -0.8063 REMARK 3 S TENSOR REMARK 3 S11: -0.5053 S12: 0.5596 S13: 0.4626 REMARK 3 S21: -0.4988 S22: 0.0564 S23: -0.3890 REMARK 3 S31: -0.1929 S32: 0.6965 S33: 0.1960 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 18 THROUGH 83 ) REMARK 3 ORIGIN FOR THE GROUP (A): -27.8625 16.6932 -32.1500 REMARK 3 T TENSOR REMARK 3 T11: 0.2354 T22: 0.1900 REMARK 3 T33: 0.2079 T12: -0.0365 REMARK 3 T13: 0.0268 T23: -0.0361 REMARK 3 L TENSOR REMARK 3 L11: 4.1778 L22: 3.8786 REMARK 3 L33: 5.0282 L12: -0.3729 REMARK 3 L13: 0.6611 L23: 0.4562 REMARK 3 S TENSOR REMARK 3 S11: -0.3915 S12: 0.1202 S13: -0.3916 REMARK 3 S21: 0.0551 S22: 0.2888 S23: 0.0124 REMARK 3 S31: 0.5688 S32: 0.0702 S33: 0.0838 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 84 THROUGH 119 ) REMARK 3 ORIGIN FOR THE GROUP (A): -28.4458 26.4374 -39.5158 REMARK 3 T TENSOR REMARK 3 T11: 0.2421 T22: 0.2906 REMARK 3 T33: 0.1933 T12: -0.0299 REMARK 3 T13: -0.0059 T23: -0.0303 REMARK 3 L TENSOR REMARK 3 L11: -0.1528 L22: 0.5944 REMARK 3 L33: 2.0425 L12: -0.2739 REMARK 3 L13: 0.1497 L23: -1.0059 REMARK 3 S TENSOR REMARK 3 S11: -0.0586 S12: -0.0402 S13: -0.0156 REMARK 3 S21: -0.1397 S22: 0.0729 S23: 0.0313 REMARK 3 S31: 0.3201 S32: -0.2584 S33: -0.0681 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 120 THROUGH 157 ) REMARK 3 ORIGIN FOR THE GROUP (A): -23.3370 53.0271 -51.9497 REMARK 3 T TENSOR REMARK 3 T11: 0.1615 T22: 0.1713 REMARK 3 T33: 0.1768 T12: 0.0045 REMARK 3 T13: 0.0050 T23: 0.0010 REMARK 3 L TENSOR REMARK 3 L11: 0.6630 L22: 1.4388 REMARK 3 L33: 1.1568 L12: -0.1225 REMARK 3 L13: 0.3300 L23: 0.4473 REMARK 3 S TENSOR REMARK 3 S11: 0.0369 S12: 0.0080 S13: 0.0972 REMARK 3 S21: -0.0585 S22: -0.0118 S23: -0.0251 REMARK 3 S31: -0.0711 S32: -0.0084 S33: -0.0101 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 158 THROUGH 184 ) REMARK 3 ORIGIN FOR THE GROUP (A): -24.7131 49.6950 -46.5308 REMARK 3 T TENSOR REMARK 3 T11: 0.1218 T22: 0.1626 REMARK 3 T33: 0.1029 T12: -0.0057 REMARK 3 T13: 0.0080 T23: -0.0112 REMARK 3 L TENSOR REMARK 3 L11: 0.6299 L22: 3.4661 REMARK 3 L33: 3.3922 L12: -1.2924 REMARK 3 L13: -0.3235 L23: 0.5099 REMARK 3 S TENSOR REMARK 3 S11: 0.0739 S12: 0.0529 S13: 0.2302 REMARK 3 S21: 0.3089 S22: -0.1314 S23: 0.4375 REMARK 3 S31: 0.2339 S32: -0.3579 S33: 0.0831 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 185 THROUGH 202 ) REMARK 3 ORIGIN FOR THE GROUP (A): -16.1754 54.9819 -53.5468 REMARK 3 T TENSOR REMARK 3 T11: 0.1298 T22: 0.2037 REMARK 3 T33: 0.1821 T12: 0.0085 REMARK 3 T13: 0.0284 T23: 0.0278 REMARK 3 L TENSOR REMARK 3 L11: 2.3362 L22: 6.7231 REMARK 3 L33: 3.2204 L12: -0.0223 REMARK 3 L13: 0.3893 L23: 0.9201 REMARK 3 S TENSOR REMARK 3 S11: -0.0201 S12: 0.1985 S13: 0.2365 REMARK 3 S21: -0.2680 S22: 0.2312 S23: -0.6666 REMARK 3 S31: -0.2525 S32: 0.1806 S33: -0.1133 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 203 THROUGH 216 ) REMARK 3 ORIGIN FOR THE GROUP (A): -20.3221 55.3347 -60.1443 REMARK 3 T TENSOR REMARK 3 T11: 0.3477 T22: 0.3304 REMARK 3 T33: 0.1985 T12: -0.0021 REMARK 3 T13: 0.0344 T23: 0.0439 REMARK 3 L TENSOR REMARK 3 L11: 1.4398 L22: 0.3368 REMARK 3 L33: 3.4334 L12: 0.5946 REMARK 3 L13: 0.7141 L23: -0.1225 REMARK 3 S TENSOR REMARK 3 S11: 0.2623 S12: 0.5933 S13: 0.2448 REMARK 3 S21: -0.8975 S22: -0.2666 S23: -0.3936 REMARK 3 S31: -0.2521 S32: -0.0350 S33: 0.0956 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 95 ) REMARK 3 ORIGIN FOR THE GROUP (A): -28.0457 34.5887 -16.7870 REMARK 3 T TENSOR REMARK 3 T11: 0.1373 T22: 0.1726 REMARK 3 T33: 0.1248 T12: 0.0129 REMARK 3 T13: -0.0030 T23: -0.0066 REMARK 3 L TENSOR REMARK 3 L11: 2.1007 L22: 3.5773 REMARK 3 L33: 1.9206 L12: 1.1855 REMARK 3 L13: -0.2919 L23: -0.4648 REMARK 3 S TENSOR REMARK 3 S11: -0.0617 S12: 0.0083 S13: 0.0662 REMARK 3 S21: -0.0251 S22: 0.0651 S23: -0.0277 REMARK 3 S31: -0.1516 S32: 0.0464 S33: -0.0203 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 96 THROUGH 118 ) REMARK 3 ORIGIN FOR THE GROUP (A): -31.6740 40.6125 -23.9538 REMARK 3 T TENSOR REMARK 3 T11: 0.2416 T22: 0.1688 REMARK 3 T33: 0.1588 T12: 0.0000 REMARK 3 T13: 0.0056 T23: -0.0360 REMARK 3 L TENSOR REMARK 3 L11: 0.4060 L22: 2.6096 REMARK 3 L33: 1.1297 L12: 0.1598 REMARK 3 L13: -0.2099 L23: -1.7357 REMARK 3 S TENSOR REMARK 3 S11: 0.0125 S12: -0.0392 S13: -0.0407 REMARK 3 S21: 0.3094 S22: 0.0554 S23: -0.1401 REMARK 3 S31: -0.2604 S32: -0.0734 S33: -0.0878 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 119 THROUGH 179 ) REMARK 3 ORIGIN FOR THE GROUP (A): -33.6020 55.1986 -44.6349 REMARK 3 T TENSOR REMARK 3 T11: 0.1376 T22: 0.1694 REMARK 3 T33: 0.2206 T12: -0.0203 REMARK 3 T13: 0.0108 T23: -0.0092 REMARK 3 L TENSOR REMARK 3 L11: 1.8809 L22: 1.8105 REMARK 3 L33: 4.7507 L12: -0.2442 REMARK 3 L13: 1.1837 L23: -0.2639 REMARK 3 S TENSOR REMARK 3 S11: 0.1172 S12: 0.1358 S13: -0.0779 REMARK 3 S21: -0.0417 S22: 0.0048 S23: 0.2248 REMARK 3 S31: 0.2459 S32: -0.2338 S33: -0.0447 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 180 THROUGH 219 ) REMARK 3 ORIGIN FOR THE GROUP (A): -38.9490 60.7877 -50.6532 REMARK 3 T TENSOR REMARK 3 T11: 0.1678 T22: 0.2319 REMARK 3 T33: 0.3026 T12: 0.0287 REMARK 3 T13: -0.0257 T23: 0.0089 REMARK 3 L TENSOR REMARK 3 L11: 4.2001 L22: 2.8167 REMARK 3 L33: 8.2373 L12: -0.6033 REMARK 3 L13: 2.9148 L23: -0.0388 REMARK 3 S TENSOR REMARK 3 S11: 0.0213 S12: 0.4495 S13: 0.1912 REMARK 3 S21: -0.2410 S22: -0.2253 S23: 0.4600 REMARK 3 S31: -0.3645 S32: -0.1230 S33: 0.1813 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 1179 THROUGH 1188 ) REMARK 3 ORIGIN FOR THE GROUP (A): -22.6030 17.7140 -15.1344 REMARK 3 T TENSOR REMARK 3 T11: 0.2956 T22: 0.2180 REMARK 3 T33: 0.3090 T12: 0.1093 REMARK 3 T13: -0.0182 T23: 0.0104 REMARK 3 L TENSOR REMARK 3 L11: 8.9623 L22: 8.2218 REMARK 3 L33: 8.7323 L12: 3.2146 REMARK 3 L13: -0.2598 L23: -2.6619 REMARK 3 S TENSOR REMARK 3 S11: -0.3181 S12: -0.3044 S13: -0.7078 REMARK 3 S21: 0.2208 S22: 0.2267 S23: -0.9008 REMARK 3 S31: 0.7245 S32: 0.7327 S33: 0.0852 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 1189 THROUGH 1197 ) REMARK 3 ORIGIN FOR THE GROUP (A): -12.7853 30.3165 -18.5185 REMARK 3 T TENSOR REMARK 3 T11: 0.3993 T22: 0.5003 REMARK 3 T33: 0.8728 T12: -0.0579 REMARK 3 T13: 0.0722 T23: -0.0019 REMARK 3 L TENSOR REMARK 3 L11: 5.9792 L22: 8.4099 REMARK 3 L33: 6.4345 L12: -2.0365 REMARK 3 L13: 1.3982 L23: -0.4587 REMARK 3 S TENSOR REMARK 3 S11: 0.6948 S12: -0.1848 S13: 0.3526 REMARK 3 S21: 0.2679 S22: -0.2307 S23: -1.7822 REMARK 3 S31: 0.0515 S32: 0.7847 S33: -0.4790 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 9C7X COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-JUN-24. REMARK 100 THE DEPOSITION ID IS D_1000283147. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 05-OCT-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 : NSLS-II REMARK 200 BEAMLINE : 17-ID-2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1 REMARK 200 MONOCHROMATOR : HORIZONTAL DOUBLE CRYSTAL REMARK 200 MONOCHROMATOR (DCM) REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33382 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950 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 (%) : 97.2 REMARK 200 DATA REDUNDANCY : 5.700 REMARK 200 R MERGE (I) : 0.11000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 6.9000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.98 REMARK 200 COMPLETENESS FOR SHELL (%) : 93.7 REMARK 200 DATA REDUNDANCY IN SHELL : 5.60 REMARK 200 R MERGE FOR SHELL (I) : 0.99100 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: PHENIX REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 47.53 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 88 MM TRIS (PH 7.0), 31% PEG REMARK 280 MONOMETHYL ETHER 2000, VAPOR DIFFUSION, HANGING DROP, REMARK 280 TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 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+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 29.99150 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 71.24900 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 29.99150 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 71.24900 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 5910 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 20150 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -37.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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 340 O HOH C 1212 2.04 REMARK 500 O HOH B 423 O HOH B 435 2.09 REMARK 500 O HOH A 372 O HOH A 404 2.15 REMARK 500 NH1 ARG B 66 O HOH B 301 2.15 REMARK 500 O HOH A 388 O HOH A 451 2.16 REMARK 500 NZ LYS B 204 O HOH B 302 2.16 REMARK 500 O HOH A 363 O HOH A 397 2.16 REMARK 500 O HOH B 369 O HOH B 464 2.17 REMARK 500 O HOH A 451 O HOH C 1213 2.17 REMARK 500 OD2 ASP B 17 O HOH B 303 2.17 REMARK 500 O HOH A 364 O HOH A 378 2.18 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 430 O HOH B 377 1554 2.07 REMARK 500 O HOH A 425 O HOH B 378 4554 2.14 REMARK 500 O HOH A 435 O HOH B 395 1554 2.19 REMARK 500 REMARK 500 REMARK: NULL 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 195 CA - CB - SG ANGL. DEV. = 7.3 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 ARG A 43 -84.32 -137.61 REMARK 500 ILE B 29 50.27 -118.72 REMARK 500 VAL B 56 -53.20 76.73 REMARK 500 SER B 61 -123.46 47.82 REMARK 500 ARG B 82 105.62 -161.61 REMARK 500 REMARK 500 REMARK: NULL DBREF 9C7X A 1 216 PDB 9C7X 9C7X 1 216 DBREF 9C7X B 1 219 PDB 9C7X 9C7X 1 219 DBREF 9C7X C 1179 1197 UNP P0DTC2 SPIKE_SARS2 1179 1197 SEQADV 9C7X ACE C 1178 UNP P0DTC2 ACETYLATION SEQRES 1 A 216 GLU VAL GLN LEU GLN GLN SER GLY PRO GLU LEU VAL LYS SEQRES 2 A 216 PRO GLY ALA SER VAL LYS ILE SER CYS LYS ALA SER GLY SEQRES 3 A 216 TYR THR PHE THR ASP TYR TYR MET SER TRP VAL LYS GLN SEQRES 4 A 216 SER HIS GLY ARG SER LEU GLU TRP ILE GLY ASP ILE ASN SEQRES 5 A 216 PRO ASN ASN GLY GLY ILE THR TYR ASN GLN ASN PHE LYS SEQRES 6 A 216 GLY LYS ALA THR LEU THR VAL ASP LYS SER SER SER THR SEQRES 7 A 216 ALA TYR MET GLU LEU ARG SER LEU THR SER GLU ASP SER SEQRES 8 A 216 ALA VAL TYR TYR CYS ALA ARG THR PHE ALA TYR TRP GLY SEQRES 9 A 216 LEU GLY THR LEU VAL THR VAL SER ALA ALA SER THR THR SEQRES 10 A 216 ALA PRO SER VAL TYR PRO LEU ALA PRO VAL CYS GLY GLY SEQRES 11 A 216 THR THR GLY SER SER VAL THR LEU GLY CYS LEU VAL LYS SEQRES 12 A 216 GLY TYR PHE PRO GLU PRO VAL THR LEU THR TRP ASN SER SEQRES 13 A 216 GLY SER LEU SER SER GLY VAL HIS THR PHE PRO ALA LEU SEQRES 14 A 216 LEU GLN SER GLY LEU TYR THR LEU SER SER SER VAL THR SEQRES 15 A 216 VAL THR SER ASN THR TRP PRO SER GLN THR ILE THR CYS SEQRES 16 A 216 ASN VAL ALA HIS PRO ALA SER SER THR LYS VAL ASP LYS SEQRES 17 A 216 LYS ILE GLU PRO ARG VAL PRO ALA SEQRES 1 B 219 ASP VAL LEU MET THR GLN THR PRO LEU SER LEU PRO VAL SEQRES 2 B 219 SER LEU GLY ASP GLN ALA SER ILE SER CYS ARG SER SER SEQRES 3 B 219 GLN SER ILE VAL HIS SER SER GLY ASN THR TYR LEU GLN SEQRES 4 B 219 TRP TYR LEU GLN LYS PRO GLY GLN SER PRO LYS LEU LEU SEQRES 5 B 219 ILE PHE LYS VAL SER ASN ARG PHE SER GLY VAL PRO ASP SEQRES 6 B 219 ARG PHE SER GLY SER GLY SER GLY THR ASP PHE THR LEU SEQRES 7 B 219 LYS ILE SER ARG VAL GLU ALA GLU ASP LEU GLY VAL TYR SEQRES 8 B 219 TYR CYS PHE GLN VAL SER HIS VAL PRO TYR THR PHE GLY SEQRES 9 B 219 GLY GLY THR LYS LEU GLU ILE LYS ARG THR ASP ALA ALA SEQRES 10 B 219 PRO THR VAL SER ILE PHE PRO PRO SER SER GLU GLN LEU SEQRES 11 B 219 THR SER GLY GLY ALA SER VAL VAL CYS PHE LEU ASN ASN SEQRES 12 B 219 PHE TYR PRO LYS ASP ILE ASN VAL LYS TRP LYS ILE ASP SEQRES 13 B 219 GLY SER GLU ARG GLN ASN GLY VAL LEU ASN SER TRP THR SEQRES 14 B 219 ASP GLN ASP SER LYS ASP SER THR TYR SER MET SER SER SEQRES 15 B 219 THR LEU THR LEU THR LYS ASP GLU TYR GLU ARG HIS ASN SEQRES 16 B 219 SER TYR THR CYS GLU ALA THR HIS LYS THR SER THR SER SEQRES 17 B 219 PRO ILE VAL LYS SER PHE ASN ARG ASN GLU CYS SEQRES 1 C 20 ACE ILE GLN LYS GLU ILE ASP ARG LEU ASN GLU VAL ALA SEQRES 2 C 20 LYS ASN LEU ASN GLU SER LEU HET ACE C1178 3 HETNAM ACE ACETYL GROUP FORMUL 3 ACE C2 H4 O FORMUL 4 HOH *344(H2 O) HELIX 1 AA1 THR A 28 TYR A 32 5 5 HELIX 2 AA2 GLN A 62 LYS A 65 5 4 HELIX 3 AA3 LYS A 74 SER A 76 5 3 HELIX 4 AA4 THR A 87 SER A 91 5 5 HELIX 5 AA5 SER A 156 SER A 158 5 3 HELIX 6 AA6 PRO A 200 SER A 203 5 4 HELIX 7 AA7 GLU B 84 LEU B 88 5 5 HELIX 8 AA8 SER B 126 THR B 131 1 6 HELIX 9 AA9 LYS B 188 HIS B 194 1 7 HELIX 10 AB1 ILE C 1179 ARG C 1185 1 7 HELIX 11 AB2 LEU C 1186 VAL C 1189 5 4 SHEET 1 AA1 4 GLN A 3 GLN A 6 0 SHEET 2 AA1 4 VAL A 18 SER A 25 -1 O LYS A 23 N GLN A 5 SHEET 3 AA1 4 THR A 78 LEU A 83 -1 O MET A 81 N ILE A 20 SHEET 4 AA1 4 ALA A 68 ASP A 73 -1 N THR A 71 O TYR A 80 SHEET 1 AA2 6 GLU A 10 VAL A 12 0 SHEET 2 AA2 6 THR A 107 VAL A 111 1 O LEU A 108 N GLU A 10 SHEET 3 AA2 6 ALA A 92 ARG A 98 -1 N ALA A 92 O VAL A 109 SHEET 4 AA2 6 MET A 34 GLN A 39 -1 N VAL A 37 O TYR A 95 SHEET 5 AA2 6 LEU A 45 ILE A 51 -1 O GLU A 46 N LYS A 38 SHEET 6 AA2 6 ILE A 58 TYR A 60 -1 O THR A 59 N ASP A 50 SHEET 1 AA3 4 GLU A 10 VAL A 12 0 SHEET 2 AA3 4 THR A 107 VAL A 111 1 O LEU A 108 N GLU A 10 SHEET 3 AA3 4 ALA A 92 ARG A 98 -1 N ALA A 92 O VAL A 109 SHEET 4 AA3 4 TYR A 102 TRP A 103 -1 O TYR A 102 N ARG A 98 SHEET 1 AA4 4 SER A 120 LEU A 124 0 SHEET 2 AA4 4 SER A 135 TYR A 145 -1 O LYS A 143 N SER A 120 SHEET 3 AA4 4 LEU A 174 THR A 184 -1 O TYR A 175 N TYR A 145 SHEET 4 AA4 4 VAL A 163 THR A 165 -1 N HIS A 164 O SER A 180 SHEET 1 AA5 4 SER A 120 LEU A 124 0 SHEET 2 AA5 4 SER A 135 TYR A 145 -1 O LYS A 143 N SER A 120 SHEET 3 AA5 4 LEU A 174 THR A 184 -1 O TYR A 175 N TYR A 145 SHEET 4 AA5 4 LEU A 169 GLN A 171 -1 N LEU A 169 O THR A 176 SHEET 1 AA6 3 THR A 151 TRP A 154 0 SHEET 2 AA6 3 THR A 194 HIS A 199 -1 O ASN A 196 N THR A 153 SHEET 3 AA6 3 THR A 204 LYS A 209 -1 O VAL A 206 N VAL A 197 SHEET 1 AA7 4 MET B 4 THR B 7 0 SHEET 2 AA7 4 ALA B 19 SER B 25 -1 O ARG B 24 N THR B 5 SHEET 3 AA7 4 ASP B 75 ILE B 80 -1 O ILE B 80 N ALA B 19 SHEET 4 AA7 4 PHE B 67 SER B 72 -1 N SER B 68 O LYS B 79 SHEET 1 AA8 6 SER B 10 VAL B 13 0 SHEET 2 AA8 6 THR B 107 ILE B 111 1 O LYS B 108 N LEU B 11 SHEET 3 AA8 6 GLY B 89 GLN B 95 -1 N GLY B 89 O LEU B 109 SHEET 4 AA8 6 LEU B 38 GLN B 43 -1 N GLN B 39 O PHE B 94 SHEET 5 AA8 6 LYS B 50 PHE B 54 -1 O LEU B 52 N TRP B 40 SHEET 6 AA8 6 ASN B 58 ARG B 59 -1 O ASN B 58 N PHE B 54 SHEET 1 AA9 4 SER B 10 VAL B 13 0 SHEET 2 AA9 4 THR B 107 ILE B 111 1 O LYS B 108 N LEU B 11 SHEET 3 AA9 4 GLY B 89 GLN B 95 -1 N GLY B 89 O LEU B 109 SHEET 4 AA9 4 THR B 102 PHE B 103 -1 O THR B 102 N GLN B 95 SHEET 1 AB1 4 THR B 119 PHE B 123 0 SHEET 2 AB1 4 GLY B 134 PHE B 144 -1 O VAL B 138 N PHE B 123 SHEET 3 AB1 4 TYR B 178 THR B 187 -1 O MET B 180 N LEU B 141 SHEET 4 AB1 4 VAL B 164 TRP B 168 -1 N LEU B 165 O THR B 183 SHEET 1 AB2 4 SER B 158 ARG B 160 0 SHEET 2 AB2 4 ASN B 150 ILE B 155 -1 N ILE B 155 O SER B 158 SHEET 3 AB2 4 SER B 196 THR B 202 -1 O GLU B 200 N LYS B 152 SHEET 4 AB2 4 ILE B 210 ASN B 215 -1 O ILE B 210 N ALA B 201 SSBOND 1 CYS A 22 CYS A 96 1555 1555 2.07 SSBOND 2 CYS A 128 CYS B 219 1555 1555 2.04 SSBOND 3 CYS A 140 CYS A 195 1555 1555 2.07 SSBOND 4 CYS B 23 CYS B 93 1555 1555 2.14 SSBOND 5 CYS B 139 CYS B 199 1555 1555 2.05 LINK C ACE C1178 N ILE C1179 1555 1555 1.33 CISPEP 1 PHE A 146 PRO A 147 0 -9.10 CISPEP 2 GLU A 148 PRO A 149 0 4.05 CISPEP 3 TRP A 188 PRO A 189 0 6.96 CISPEP 4 THR B 7 PRO B 8 0 -3.25 CISPEP 5 VAL B 99 PRO B 100 0 0.20 CISPEP 6 TYR B 145 PRO B 146 0 1.55 CRYST1 59.983 142.498 54.262 90.00 90.00 90.00 P 21 21 2 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 0.016671 0.000000 0.000000 0.00000 SCALE2 0.000000 0.007018 0.000000 0.00000 SCALE3 0.000000 0.000000 0.018429 0.00000