HEADER VIRAL PROTEIN 28-APR-23 8OWV TITLE H6 AND F2 NANOBODIES BOUND TO SARS-COV-2 SPIKE RBD COMPND MOL_ID: 1; COMPND 2 MOLECULE: SPIKE GLYCOPROTEIN; COMPND 3 CHAIN: EEE; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: F2; COMPND 7 CHAIN: BBB; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: H6; COMPND 11 CHAIN: FFF; COMPND 12 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 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 9 ORGANISM_TAXID: 9844; SOURCE 10 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 11 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 12 MOL_ID: 3; SOURCE 13 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 14 ORGANISM_TAXID: 9844; SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 16 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS NANOBODY, COMPLEX, RECEPTOR BINDING DOMAIN, SARS-COV-2, VIRAL PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR H.MIKOLAJEK,J.H.NAISMITH,R.J.OWENS JRNL AUTH K.A.S.CORNISH,H.MIKOLAJEK,J.H.NAISMITH,R.J.OWENS JRNL TITL TRIMERIC NANOBODIES POTENTLY NEUTRALIZE OMICRON VARIANTS OF JRNL TITL 2 SARS-COV-2 JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 1.73 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0267 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 REFINEMENT TARGET : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.73 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 59.44 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 3 NUMBER OF REFLECTIONS : 53238 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE REMARK 3 FREE R VALUE TEST SET SELECTION : NULL REMARK 3 R VALUE (WORKING + TEST SET) : NULL REMARK 3 R VALUE (WORKING SET) : 0.197 REMARK 3 FREE R VALUE : 0.223 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.927 REMARK 3 FREE R VALUE TEST SET COUNT : 2623 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.73 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.78 REMARK 3 REFLECTION IN BIN (WORKING SET) : 3700 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.79 REMARK 3 BIN R VALUE (WORKING SET) : 0.4270 REMARK 3 BIN FREE R VALUE SET COUNT : 157 REMARK 3 BIN FREE R VALUE : 0.4350 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3512 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 32 REMARK 3 SOLVENT ATOMS : 216 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.51 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.96300 REMARK 3 B22 (A**2) : -0.01600 REMARK 3 B33 (A**2) : -0.94800 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.113 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.107 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.116 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.878 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.965 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.954 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3669 ; 0.006 ; 0.012 REMARK 3 BOND LENGTHS OTHERS (A): 3289 ; 0.001 ; 0.018 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4999 ; 1.403 ; 1.656 REMARK 3 BOND ANGLES OTHERS (DEGREES): 7563 ; 1.263 ; 1.581 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 458 ; 7.303 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 195 ;31.388 ;21.487 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 547 ;13.143 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 25 ;18.145 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 465 ; 0.060 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4240 ; 0.006 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 940 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 559 ; 0.186 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 60 ; 0.169 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1768 ; 0.169 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 203 ; 0.153 ; 0.200 REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1805 ; 1.007 ; 1.379 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1804 ; 1.006 ; 1.378 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2254 ; 1.582 ; 2.060 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2255 ; 1.581 ; 2.060 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1864 ; 1.715 ; 1.594 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1865 ; 1.716 ; 1.596 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2739 ; 2.525 ; 2.307 REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2740 ; 2.524 ; 2.310 REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 11 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : NULL NULL NULL NULL REMARK 3 ORIGIN FOR THE GROUP (A): 53.6390 -3.7590 -41.2070 REMARK 3 T TENSOR REMARK 3 T11: 0.2987 T22: 0.3531 REMARK 3 T33: 0.3400 T12: 0.1456 REMARK 3 T13: 0.0012 T23: 0.0482 REMARK 3 L TENSOR REMARK 3 L11: 6.0941 L22: 4.4320 REMARK 3 L33: 2.1494 L12: 3.1142 REMARK 3 L13: -2.0147 L23: -0.8029 REMARK 3 S TENSOR REMARK 3 S11: -0.1107 S12: -0.6775 S13: -0.2847 REMARK 3 S21: 0.1657 S22: -0.0853 S23: -0.4361 REMARK 3 S31: 0.4480 S32: 0.8179 S33: 0.1960 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : NULL NULL NULL NULL REMARK 3 ORIGIN FOR THE GROUP (A): 51.9460 12.3330 -39.0350 REMARK 3 T TENSOR REMARK 3 T11: 0.3661 T22: 0.2388 REMARK 3 T33: 0.4432 T12: -0.0644 REMARK 3 T13: 0.0466 T23: -0.0728 REMARK 3 L TENSOR REMARK 3 L11: 6.8336 L22: 11.0137 REMARK 3 L33: 4.6669 L12: 1.1889 REMARK 3 L13: 3.0734 L23: 5.5001 REMARK 3 S TENSOR REMARK 3 S11: -0.2391 S12: -0.2811 S13: 0.5896 REMARK 3 S21: 0.0772 S22: 0.2893 S23: -0.0873 REMARK 3 S31: -0.2331 S32: 0.2314 S33: -0.0502 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : NULL NULL NULL NULL REMARK 3 ORIGIN FOR THE GROUP (A): 45.2480 2.1640 -49.5500 REMARK 3 T TENSOR REMARK 3 T11: 0.2025 T22: 0.1281 REMARK 3 T33: 0.2593 T12: -0.0140 REMARK 3 T13: 0.0304 T23: 0.0291 REMARK 3 L TENSOR REMARK 3 L11: 6.2869 L22: 3.7692 REMARK 3 L33: 2.0239 L12: 2.7501 REMARK 3 L13: -1.0865 L23: 0.0327 REMARK 3 S TENSOR REMARK 3 S11: -0.1155 S12: 0.7466 S13: 0.4223 REMARK 3 S21: -0.2248 S22: 0.1179 S23: 0.2067 REMARK 3 S31: 0.0068 S32: -0.0355 S33: -0.0025 REMARK 3 REMARK 3 TLS GROUP : 4 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : NULL NULL NULL NULL REMARK 3 ORIGIN FOR THE GROUP (A): 50.4150 2.1020 -43.0450 REMARK 3 T TENSOR REMARK 3 T11: 0.1977 T22: 0.1246 REMARK 3 T33: 0.2646 T12: 0.0044 REMARK 3 T13: -0.0040 T23: -0.0095 REMARK 3 L TENSOR REMARK 3 L11: 4.7854 L22: 1.0200 REMARK 3 L33: 2.7933 L12: -0.0506 REMARK 3 L13: -1.8542 L23: 0.4495 REMARK 3 S TENSOR REMARK 3 S11: -0.0640 S12: -0.1049 S13: 0.1011 REMARK 3 S21: -0.0319 S22: 0.0828 S23: -0.3474 REMARK 3 S31: 0.0967 S32: 0.5035 S33: -0.0188 REMARK 3 REMARK 3 TLS GROUP : 5 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : NULL NULL NULL NULL REMARK 3 ORIGIN FOR THE GROUP (A): 15.3020 0.6160 -34.5440 REMARK 3 T TENSOR REMARK 3 T11: 0.2264 T22: 0.2087 REMARK 3 T33: 0.3120 T12: -0.0283 REMARK 3 T13: 0.0498 T23: -0.0660 REMARK 3 L TENSOR REMARK 3 L11: 2.5070 L22: 2.4628 REMARK 3 L33: 6.2290 L12: -0.5771 REMARK 3 L13: 1.8452 L23: -2.3599 REMARK 3 S TENSOR REMARK 3 S11: -0.0085 S12: 0.1175 S13: -0.0469 REMARK 3 S21: 0.0178 S22: -0.0303 S23: 0.5123 REMARK 3 S31: 0.1367 S32: -0.6813 S33: 0.0388 REMARK 3 REMARK 3 TLS GROUP : 6 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : NULL NULL NULL NULL REMARK 3 ORIGIN FOR THE GROUP (A): 26.5710 0.6170 -32.2000 REMARK 3 T TENSOR REMARK 3 T11: 0.2316 T22: 0.0102 REMARK 3 T33: 0.1438 T12: -0.0071 REMARK 3 T13: 0.0197 T23: 0.0102 REMARK 3 L TENSOR REMARK 3 L11: 0.8691 L22: 2.7535 REMARK 3 L33: 2.0508 L12: 0.0458 REMARK 3 L13: 0.5490 L23: 0.7243 REMARK 3 S TENSOR REMARK 3 S11: -0.0100 S12: 0.0150 S13: 0.0115 REMARK 3 S21: 0.1671 S22: -0.0326 S23: 0.1194 REMARK 3 S31: 0.0256 S32: -0.1115 S33: 0.0426 REMARK 3 REMARK 3 TLS GROUP : 7 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : NULL NULL NULL NULL REMARK 3 ORIGIN FOR THE GROUP (A): 23.5310 -8.0120 -9.1430 REMARK 3 T TENSOR REMARK 3 T11: 0.6662 T22: 0.1097 REMARK 3 T33: 0.1959 T12: -0.0403 REMARK 3 T13: 0.1041 T23: 0.0474 REMARK 3 L TENSOR REMARK 3 L11: 1.3595 L22: 1.5866 REMARK 3 L33: 5.2373 L12: 0.1296 REMARK 3 L13: -0.6354 L23: -0.0242 REMARK 3 S TENSOR REMARK 3 S11: -0.0394 S12: -0.2990 S13: -0.1085 REMARK 3 S21: 0.7688 S22: -0.0255 S23: 0.2452 REMARK 3 S31: 0.3937 S32: -0.2642 S33: 0.0649 REMARK 3 REMARK 3 TLS GROUP : 8 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : NULL NULL NULL NULL REMARK 3 ORIGIN FOR THE GROUP (A): 24.3620 0.8540 -30.7980 REMARK 3 T TENSOR REMARK 3 T11: 0.1597 T22: 0.0219 REMARK 3 T33: 0.1623 T12: 0.0134 REMARK 3 T13: 0.0330 T23: 0.0124 REMARK 3 L TENSOR REMARK 3 L11: 0.6916 L22: 3.6709 REMARK 3 L33: 1.4772 L12: 0.1920 REMARK 3 L13: 0.2054 L23: 0.9278 REMARK 3 S TENSOR REMARK 3 S11: -0.0321 S12: -0.0223 S13: -0.0316 REMARK 3 S21: 0.2076 S22: 0.0131 S23: 0.1040 REMARK 3 S31: -0.0240 S32: -0.0519 S33: 0.0190 REMARK 3 REMARK 3 TLS GROUP : 9 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : NULL NULL NULL NULL REMARK 3 ORIGIN FOR THE GROUP (A): 47.1490 -1.5890 0.6500 REMARK 3 T TENSOR REMARK 3 T11: 0.7080 T22: 0.2943 REMARK 3 T33: 0.1745 T12: 0.0324 REMARK 3 T13: -0.0763 T23: 0.0051 REMARK 3 L TENSOR REMARK 3 L11: 3.1550 L22: 4.8860 REMARK 3 L33: 2.1856 L12: 1.2981 REMARK 3 L13: 1.8010 L23: 1.8021 REMARK 3 S TENSOR REMARK 3 S11: 0.0939 S12: -0.5757 S13: -0.0071 REMARK 3 S21: 0.2465 S22: -0.0048 S23: -0.1632 REMARK 3 S31: 0.1268 S32: -0.0363 S33: -0.0891 REMARK 3 REMARK 3 TLS GROUP : 10 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : NULL NULL NULL NULL REMARK 3 ORIGIN FOR THE GROUP (A): 38.5380 9.4120 7.4460 REMARK 3 T TENSOR REMARK 3 T11: 0.4383 T22: 0.6490 REMARK 3 T33: 0.4986 T12: 0.0172 REMARK 3 T13: 0.0021 T23: -0.1987 REMARK 3 L TENSOR REMARK 3 L11: 4.7365 L22: 6.7137 REMARK 3 L33: 8.8247 L12: 3.9982 REMARK 3 L13: -1.5517 L23: 3.6072 REMARK 3 S TENSOR REMARK 3 S11: 0.1436 S12: -0.3790 S13: 0.4379 REMARK 3 S21: 0.0897 S22: -0.0480 S23: 0.0497 REMARK 3 S31: 0.0777 S32: -0.1449 S33: -0.0955 REMARK 3 REMARK 3 TLS GROUP : 11 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : NULL NULL NULL NULL REMARK 3 ORIGIN FOR THE GROUP (A): 44.2540 2.3740 -4.1220 REMARK 3 T TENSOR REMARK 3 T11: 0.7839 T22: 0.1503 REMARK 3 T33: 0.2102 T12: 0.0468 REMARK 3 T13: -0.1101 T23: -0.0200 REMARK 3 L TENSOR REMARK 3 L11: 2.0056 L22: 0.6945 REMARK 3 L33: 2.4557 L12: 0.7378 REMARK 3 L13: 1.5413 L23: 0.8653 REMARK 3 S TENSOR REMARK 3 S11: 0.0266 S12: -0.2230 S13: 0.1711 REMARK 3 S21: 0.4185 S22: 0.0206 S23: -0.0934 REMARK 3 S31: 0.0898 S32: 0.1522 S33: -0.0472 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK BULK SOLVENT REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.20 REMARK 3 ION PROBE RADIUS : 0.90 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THEIR REMARK 3 RIDING POSITIONS REMARK 4 REMARK 4 8OWV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE. REMARK 100 THE DEPOSITION ID IS D_1292129659. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 10-AUG-21 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 : I03 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.976 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 XE 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2 REMARK 200 DATA SCALING SOFTWARE : DIALS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 53452 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.730 REMARK 200 RESOLUTION RANGE LOW (A) : 59.520 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 12.50 REMARK 200 R MERGE (I) : 0.10500 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 11.5000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.73 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.76 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: PHASER REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 47.67 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, VAPOR DIFFUSION, SITTING REMARK 280 DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 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 28.88750 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 72.81200 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 29.71900 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 72.81200 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 28.88750 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 29.71900 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: EEE, BBB, FFF 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 LYS E 529 REMARK 465 SER E 530 REMARK 465 THR E 531 REMARK 465 ASN E 532 REMARK 465 LYS E 533 REMARK 465 HIS E 534 REMARK 465 HIS E 535 REMARK 465 HIS E 536 REMARK 465 HIS E 537 REMARK 465 HIS E 538 REMARK 465 HIS E 539 REMARK 465 LYS B 128 REMARK 465 HIS B 129 REMARK 465 HIS B 130 REMARK 465 HIS B 131 REMARK 465 HIS B 132 REMARK 465 HIS B 133 REMARK 465 HIS B 134 REMARK 465 LYS F 128 REMARK 465 HIS F 129 REMARK 465 HIS F 130 REMARK 465 HIS F 131 REMARK 465 HIS F 132 REMARK 465 HIS F 133 REMARK 465 HIS F 134 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 HOHBB 308 O HOHBB 345 2.16 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 ALAEE 352 40.06 -107.70 REMARK 500 ASNEE 422 -57.24 -127.66 REMARK 500 SERBB 57 -6.55 93.65 REMARK 500 ALABB 94 166.16 175.39 REMARK 500 TYRBB 107 57.18 -99.64 REMARK 500 GLUFF 27 -18.76 74.39 REMARK 500 ALAFF 95 170.85 172.22 REMARK 500 ARGFF 114 23.55 -145.28 REMARK 500 SERFF 126 -165.20 -169.23 REMARK 500 REMARK 500 REMARK: NULL DBREF1 8OWVEE 331 532 UNP A0A8A5XRG7_SARS2 DBREF2 8OWVEE A0A8A5XRG7 328 529 DBREF 8OWVBB 3 134 PDB 8OWV 8OWV 3 134 DBREF 8OWVFF 2 134 PDB 8OWV 8OWV 2 134 SEQADV 8OWV VALEE 417 UNP A0A8A5XRG ASN 414 CONFLICT SEQADV 8OWV LYSEE 533 UNP A0A8A5XRG EXPRESSION TAG SEQADV 8OWV HISEE 534 UNP A0A8A5XRG EXPRESSION TAG SEQADV 8OWV HISEE 535 UNP A0A8A5XRG EXPRESSION TAG SEQADV 8OWV HISEE 536 UNP A0A8A5XRG EXPRESSION TAG SEQADV 8OWV HISEE 537 UNP A0A8A5XRG EXPRESSION TAG SEQADV 8OWV HISEE 538 UNP A0A8A5XRG EXPRESSION TAG SEQADV 8OWV HISEE 539 UNP A0A8A5XRG EXPRESSION TAG SEQRES 1EE 209 ASN ILE THR ASN LEU CYS PRO PHE GLY GLU VAL PHE ASN SEQRES 2EE 209 ALA THR ARG PHE ALA SER VAL TYR ALA TRP ASN ARG LYS SEQRES 3EE 209 ARG ILE SER ASN CYS VAL ALA ASP TYR SER VAL LEU TYR SEQRES 4EE 209 ASN SER ALA SER PHE SER THR PHE LYS CYS TYR GLY VAL SEQRES 5EE 209 SER PRO THR LYS LEU ASN ASP LEU CYS PHE THR ASN VAL SEQRES 6EE 209 TYR ALA ASP SER PHE VAL ILE ARG GLY ASP GLU VAL ARG SEQRES 7EE 209 GLN ILE ALA PRO GLY GLN THR GLY VAL ILE ALA ASP TYR SEQRES 8EE 209 ASN TYR LYS LEU PRO ASP ASP PHE THR GLY CYS VAL ILE SEQRES 9EE 209 ALA TRP ASN SER ASN ASN LEU ASP SER LYS VAL GLY GLY SEQRES 10EE 209 ASN TYR ASN TYR LEU TYR ARG LEU PHE ARG LYS SER ASN SEQRES 11EE 209 LEU LYS PRO PHE GLU ARG ASP ILE SER THR GLU ILE TYR SEQRES 12EE 209 GLN ALA GLY SER THR PRO CYS ASN GLY VAL LYS GLY PHE SEQRES 13EE 209 ASN CYS TYR PHE PRO LEU GLN SER TYR GLY PHE GLN PRO SEQRES 14EE 209 THR TYR GLY VAL GLY TYR GLN PRO TYR ARG VAL VAL VAL SEQRES 15EE 209 LEU SER PHE GLU LEU LEU HIS ALA PRO ALA THR VAL CYS SEQRES 16EE 209 GLY PRO LYS LYS SER THR ASN LYS HIS HIS HIS HIS HIS SEQRES 17EE 209 HIS SEQRES 1BB 132 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2BB 132 ALA GLY GLY SER LEU ARG LEU ALA CYS ILE ALA SER GLY SEQRES 3BB 132 ARG THR PHE HIS SER TYR VAL MET ALA TRP PHE ARG GLN SEQRES 4BB 132 ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA ALA ILE SER SEQRES 5BB 132 TRP SER SER THR PRO THR TYR TYR GLY GLU SER VAL LYS SEQRES 6BB 132 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR SEQRES 7BB 132 VAL TYR LEU GLN MET ASN ARG LEU LYS PRO GLU ASP THR SEQRES 8BB 132 ALA VAL TYR PHE CYS ALA ALA ASP ARG GLY GLU SER TYR SEQRES 9BB 132 TYR TYR THR ARG PRO THR GLU TYR GLU PHE TRP GLY GLN SEQRES 10BB 132 GLY THR GLN VAL THR VAL SER SER LYS HIS HIS HIS HIS SEQRES 11BB 132 HIS HIS SEQRES 1FF 133 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2FF 133 PRO GLY GLY SER LEU THR LEU SER CYS VAL ALA SER GLU SEQRES 3FF 133 SER SER LEU ALA PRO TYR ARG VAL ALA TRP PHE ARG GLN SEQRES 4FF 133 ALA PRO GLY LYS GLU ARG GLU GLY VAL SER CYS ILE SER SEQRES 5FF 133 ARG ASP ALA HIS PRO THR SER THR TYR TYR THR ALA SER SEQRES 6FF 133 VAL LYS GLY ARG PHE THR MET SER ARG ASP ASN ALA LYS SEQRES 7FF 133 ASN THR VAL TYR LEU GLN MET ASN SER LEU LYS PRO SER SEQRES 8FF 133 ASP THR ALA VAL TYR TYR CYS ALA THR ASP LEU GLY GLY SEQRES 9FF 133 TYR CYS SER ASP SER ASN TYR PRO ARG ALA TRP TRP GLY SEQRES 10FF 133 GLN GLY THR GLN VAL THR VAL SER SER LYS HIS HIS HIS SEQRES 11FF 133 HIS HIS HIS HET NAG EE 601 14 HET GOL EE 602 6 HET GOL EE 603 6 HET GOL BB 201 6 HETNAM NAG N-ACETYL-D-GLUCOSAMINE HETNAM GOL GLYCEROL HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 4 NAG C8 H15 N O6 FORMUL 5 GOL 3(C3 H8 O3) FORMUL 8 HOH *216(H2 O) HELIX 1 AA1 PROEE 337 ASNEE 343 1 7 HELIX 2 AA2 SEREE 349 TRPEE 353 5 5 HELIX 3 AA3 ASPEE 364 TYREE 369 5 6 HELIX 4 AA4 SEREE 383 ASPEE 389 5 7 HELIX 5 AA5 ASPEE 405 ILEEE 410 5 6 HELIX 6 AA6 GLYEE 416 ASNEE 422 1 7 HELIX 7 AA7 SEREE 438 SEREE 443 1 6 HELIX 8 AA8 GLYEE 502 TYREE 505 5 4 HELIX 9 AA9 THRBB 30 TYRBB 34 5 5 HELIX 10 AB1 LYSBB 89 THRBB 93 5 5 HELIX 11 AB2 ARGBB 110 TYRBB 114 5 5 HELIX 12 AB3 HISFF 57 THRFF 61 5 5 HELIX 13 AB4 ALAFF 65 LYSFF 68 5 4 HELIX 14 AB5 ASNFF 77 LYSFF 79 5 3 HELIX 15 AB6 LYSFF 90 THRFF 94 5 5 SHEET 1 AA1 6 ASNEE 354 ILEEE 358 0 SHEET 2 AA1 6 ASNEE 394 ARGEE 403 -1 O VALEE 395 N ILEEE 358 SHEET 3 AA1 6 PROEE 507 GLUEE 516 -1 O VALEE 512 N ASPEE 398 SHEET 4 AA1 6 GLYEE 431 ASNEE 437 -1 N ILEEE 434 O VALEE 511 SHEET 5 AA1 6 PHEEE 374 TYREE 380 -1 N TYREE 380 O GLYEE 431 SHEET 6 AA1 6 GLUBB 104 SERBB 105 -1 O GLUBB 104 N CYSEE 379 SHEET 1 AA2 3 CYSEE 361 VALEE 362 0 SHEET 2 AA2 3 VALEE 524 CYSEE 525 1 O CYSEE 525 N CYSEE 361 SHEET 3 AA2 3 CYSEE 391 PHEEE 392 -1 N PHEEE 392 O VALEE 524 SHEET 1 AA3 2 LEUEE 452 ARGEE 454 0 SHEET 2 AA3 2 LEUEE 492 SEREE 494 -1 O GLNEE 493 N TYREE 453 SHEET 1 AA4 2 TYREE 473 GLNEE 474 0 SHEET 2 AA4 2 CYSEE 488 TYREE 489 -1 O TYREE 489 N TYREE 473 SHEET 1 AA5 4 GLNBB 5 SERBB 9 0 SHEET 2 AA5 4 LEUBB 20 SERBB 27 -1 O ALABB 23 N SERBB 9 SHEET 3 AA5 4 THRBB 80 METBB 85 -1 O METBB 85 N LEUBB 20 SHEET 4 AA5 4 PHEBB 70 ASPBB 75 -1 N THRBB 71 O GLNBB 84 SHEET 1 AA6 6 GLYBB 12 GLNBB 15 0 SHEET 2 AA6 6 THRBB 121 SERBB 126 1 O THRBB 124 N VALBB 14 SHEET 3 AA6 6 ALABB 94 ASPBB 101 -1 N TYRBB 96 O THRBB 121 SHEET 4 AA6 6 VALBB 35 GLNBB 41 -1 N VALBB 35 O ASPBB 101 SHEET 5 AA6 6 GLUBB 48 ILEBB 53 -1 O GLUBB 48 N ARGBB 40 SHEET 6 AA6 6 THRBB 60 TYRBB 62 -1 O TYRBB 61 N ALABB 52 SHEET 1 AA7 4 GLYBB 12 GLNBB 15 0 SHEET 2 AA7 4 THRBB 121 SERBB 126 1 O THRBB 124 N VALBB 14 SHEET 3 AA7 4 ALABB 94 ASPBB 101 -1 N TYRBB 96 O THRBB 121 SHEET 4 AA7 4 PHEBB 116 TRPBB 117 -1 O PHEBB 116 N ALABB 100 SHEET 1 AA8 4 GLNFF 4 SERFF 8 0 SHEET 2 AA8 4 LEUFF 19 SERFF 26 -1 O SERFF 22 N SERFF 8 SHEET 3 AA8 4 THRFF 81 METFF 86 -1 O METFF 86 N LEUFF 19 SHEET 4 AA8 4 PHEFF 71 ASPFF 76 -1 N THRFF 72 O GLNFF 85 SHEET 1 AA9 6 LEUFF 12 VALFF 13 0 SHEET 2 AA9 6 THRFF 121 VALFF 125 1 O THRFF 124 N VALFF 13 SHEET 3 AA9 6 ALAFF 95 THRFF 101 -1 N TYRFF 97 O THRFF 121 SHEET 4 AA9 6 VALFF 35 GLNFF 40 -1 N PHEFF 38 O TYRFF 98 SHEET 5 AA9 6 GLUFF 47 ILEFF 52 -1 O VALFF 49 N TRPFF 37 SHEET 6 AA9 6 TYRFF 62 TYRFF 63 -1 O TYRFF 62 N CYSFF 51 SHEET 1 AB1 4 LEUFF 12 VALFF 13 0 SHEET 2 AB1 4 THRFF 121 VALFF 125 1 O THRFF 124 N VALFF 13 SHEET 3 AB1 4 ALAFF 95 THRFF 101 -1 N TYRFF 97 O THRFF 121 SHEET 4 AB1 4 TRPFF 116 TRPFF 117 -1 O TRPFF 116 N THRFF 101 SSBOND 1 CYSEE 336 CYSEE 361 1555 1555 2.07 SSBOND 2 CYSEE 379 CYSEE 432 1555 1555 2.02 SSBOND 3 CYSEE 391 CYSEE 525 1555 1555 2.08 SSBOND 4 CYSEE 480 CYSEE 488 1555 1555 2.06 SSBOND 5 CYSBB 24 CYSBB 98 1555 1555 2.04 SSBOND 6 CYSFF 23 CYSFF 99 1555 1555 2.03 SSBOND 7 CYSFF 51 CYSFF 107 1555 1555 2.05 LINK ND2 ASNEE 343 C1 NAGEE 601 1555 1555 1.43 CISPEP 1 THRBB 58 PROBB 59 0 -6.48 CRYST1 57.775 59.438 145.624 90.00 90.00 90.00 P 21 21 21 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 0.017309 0.000000 0.000000 0.00000 SCALE2 0.000000 0.016824 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006867 0.00000