HEADER ANTIVIRAL PROTEIN 08-JUN-20 6ZBP TITLE H11-H4 COMPLEX WITH SARS-COV-2 COMPND MOL_ID: 1; COMPND 2 MOLECULE: SPIKE GLYCOPROTEIN; COMPND 3 CHAIN: EEE; COMPND 4 SYNONYM: S GLYCOPROTEIN,E2,PEPLOMER PROTEIN; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: H11-H4; COMPND 8 CHAIN: FFF; COMPND 9 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS SOURCE 3 2; SOURCE 4 ORGANISM_COMMON: 2019-NCOV; SOURCE 5 ORGANISM_TAXID: 2697049; SOURCE 6 GENE: S, 2; SOURCE 7 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 8 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 9 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 10 MOL_ID: 2; SOURCE 11 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 12 ORGANISM_COMMON: LLAMA; SOURCE 13 ORGANISM_TAXID: 9844; SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS COMPLEX, LLAMA, NANOBODY, ANTIBODY, SARS-COV-2, ANTIVIRAL PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR J.H.NAISMITH,J.HUO,H.MIKOLAJEK,P.WARD,M.DUMOUX,R.J.OWENS,A.LEBAS JRNL AUTH J.H.NAISMITH JRNL TITL H11-D4 COMPLEX WITH SARS-COV-2 RBD JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 1.85 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0258 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) : 1.85 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 57.15 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7 REMARK 3 NUMBER OF REFLECTIONS : 35472 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) : 0.185 REMARK 3 FREE R VALUE : 0.217 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.097 REMARK 3 FREE R VALUE TEST SET COUNT : 1808 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : NULL REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.85 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.90 REMARK 3 REFLECTION IN BIN (WORKING SET) : 2460 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.42 REMARK 3 BIN R VALUE (WORKING SET) : 0.3000 REMARK 3 BIN FREE R VALUE SET COUNT : 125 REMARK 3 BIN FREE R VALUE : 0.3330 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 2546 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 19 REMARK 3 SOLVENT ATOMS : 103 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 48.74 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 2.09100 REMARK 3 B22 (A**2) : 2.09100 REMARK 3 B33 (A**2) : -6.78400 REMARK 3 B12 (A**2) : 1.04600 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): 0.120 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.116 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.101 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.218 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.968 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): 2696 ; 0.012 ; 0.012 REMARK 3 BOND LENGTHS OTHERS (A): 2350 ; 0.001 ; 0.017 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3680 ; 1.682 ; 1.656 REMARK 3 BOND ANGLES OTHERS (DEGREES): 5454 ; 1.405 ; 1.580 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 347 ;17.387 ; 5.303 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 142 ;31.740 ;21.690 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 404 ;12.462 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 17 ;16.664 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 338 ; 0.081 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3306 ; 0.010 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 640 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 380 ; 0.189 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 51 ; 0.183 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1283 ; 0.179 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 91 ; 0.150 ; 0.200 REMARK 3 H-BOND (X...Y) OTHERS (A): 1 ; 0.082 ; 0.200 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): 1314 ; 3.014 ; 2.519 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1313 ; 3.006 ; 2.516 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1646 ; 3.896 ; 3.761 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1647 ; 3.895 ; 3.765 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1382 ; 4.612 ; 3.060 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1379 ; 4.553 ; 3.052 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2027 ; 6.874 ; 4.396 REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2022 ; 6.777 ; 4.381 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 : 8 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 : EE 334 EE 387 REMARK 3 ORIGIN FOR THE GROUP (A): 32.4630 -0.3420 -8.2310 REMARK 3 T TENSOR REMARK 3 T11: 0.1630 T22: 0.1136 REMARK 3 T33: 0.5533 T12: 0.0535 REMARK 3 T13: -0.0221 T23: 0.0008 REMARK 3 L TENSOR REMARK 3 L11: 2.5606 L22: 1.2580 REMARK 3 L33: 3.8177 L12: -0.4707 REMARK 3 L13: 0.9316 L23: -0.4326 REMARK 3 S TENSOR REMARK 3 S11: 0.1069 S12: 0.0558 S13: -0.2388 REMARK 3 S21: 0.0292 S22: -0.1307 S23: -0.4566 REMARK 3 S31: 0.5136 S32: 0.5094 S33: 0.0238 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 : EE 388 EE 417 REMARK 3 ORIGIN FOR THE GROUP (A): 22.4300 2.0800 -7.9890 REMARK 3 T TENSOR REMARK 3 T11: 0.1163 T22: 0.0108 REMARK 3 T33: 0.3363 T12: -0.0155 REMARK 3 T13: -0.0271 T23: 0.0228 REMARK 3 L TENSOR REMARK 3 L11: 2.3523 L22: 3.9846 REMARK 3 L33: 3.0845 L12: -0.3272 REMARK 3 L13: 0.1284 L23: -0.4168 REMARK 3 S TENSOR REMARK 3 S11: 0.0138 S12: -0.1013 S13: -0.1228 REMARK 3 S21: 0.2361 S22: 0.0284 S23: 0.1443 REMARK 3 S31: 0.2202 S32: -0.1345 S33: -0.0422 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 : EE 418 EE 479 REMARK 3 ORIGIN FOR THE GROUP (A): 17.7570 10.8960 -14.1660 REMARK 3 T TENSOR REMARK 3 T11: 0.0369 T22: 0.0107 REMARK 3 T33: 0.3513 T12: 0.0137 REMARK 3 T13: 0.0448 T23: -0.0004 REMARK 3 L TENSOR REMARK 3 L11: 2.1007 L22: 2.7011 REMARK 3 L33: 3.9669 L12: -0.8653 REMARK 3 L13: 2.0231 L23: -1.5163 REMARK 3 S TENSOR REMARK 3 S11: 0.0566 S12: 0.0398 S13: -0.0184 REMARK 3 S21: 0.0742 S22: 0.0313 S23: 0.1065 REMARK 3 S31: -0.0486 S32: -0.0898 S33: -0.0879 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 : EE 480 EE 488 REMARK 3 ORIGIN FOR THE GROUP (A): 5.9690 24.8380 -26.5800 REMARK 3 T TENSOR REMARK 3 T11: 0.1365 T22: 0.1951 REMARK 3 T33: 0.5116 T12: 0.0677 REMARK 3 T13: 0.0088 T23: 0.0864 REMARK 3 L TENSOR REMARK 3 L11: 9.0909 L22: 6.2173 REMARK 3 L33: 7.6775 L12: 0.7373 REMARK 3 L13: -5.0952 L23: 1.2884 REMARK 3 S TENSOR REMARK 3 S11: -0.0084 S12: 1.0655 S13: 0.1477 REMARK 3 S21: -0.4062 S22: 0.0862 S23: 0.7049 REMARK 3 S31: -0.1427 S32: -0.9554 S33: -0.0777 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 : EE 489 EE 528 REMARK 3 ORIGIN FOR THE GROUP (A): 25.9720 5.7870 -9.9600 REMARK 3 T TENSOR REMARK 3 T11: 0.1734 T22: 0.0249 REMARK 3 T33: 0.4177 T12: 0.0166 REMARK 3 T13: -0.0395 T23: 0.0005 REMARK 3 L TENSOR REMARK 3 L11: 1.4569 L22: 1.9709 REMARK 3 L33: 3.4643 L12: -0.5379 REMARK 3 L13: 0.7988 L23: -0.4844 REMARK 3 S TENSOR REMARK 3 S11: -0.0512 S12: 0.0221 S13: -0.0177 REMARK 3 S21: 0.5467 S22: 0.0427 S23: -0.2737 REMARK 3 S31: 0.0484 S32: 0.1856 S33: 0.0085 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 : FF 1 FF 64 REMARK 3 ORIGIN FOR THE GROUP (A): 22.8990 38.3250 -27.5860 REMARK 3 T TENSOR REMARK 3 T11: 0.1329 T22: 0.0290 REMARK 3 T33: 0.4167 T12: -0.0069 REMARK 3 T13: 0.0014 T23: 0.0332 REMARK 3 L TENSOR REMARK 3 L11: 1.6596 L22: 3.2321 REMARK 3 L33: 2.5488 L12: 0.1038 REMARK 3 L13: -0.5454 L23: -0.6823 REMARK 3 S TENSOR REMARK 3 S11: 0.1427 S12: -0.0138 S13: 0.1451 REMARK 3 S21: 0.4101 S22: -0.1510 S23: -0.2293 REMARK 3 S31: -0.4317 S32: 0.0791 S33: 0.0083 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 : FF 65 FF 88 REMARK 3 ORIGIN FOR THE GROUP (A): 19.4630 37.7620 -34.0820 REMARK 3 T TENSOR REMARK 3 T11: 0.0429 T22: 0.0915 REMARK 3 T33: 0.3381 T12: 0.0259 REMARK 3 T13: 0.0259 T23: 0.0227 REMARK 3 L TENSOR REMARK 3 L11: 4.2503 L22: 9.6934 REMARK 3 L33: 4.3100 L12: -3.7509 REMARK 3 L13: 1.0647 L23: -1.5301 REMARK 3 S TENSOR REMARK 3 S11: 0.1348 S12: 0.1012 S13: 0.0269 REMARK 3 S21: -0.1012 S22: -0.1630 S23: 0.1411 REMARK 3 S31: -0.1626 S32: -0.2529 S33: 0.0282 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 : FF 89 FF 128 REMARK 3 ORIGIN FOR THE GROUP (A): 21.3780 39.4260 -23.6510 REMARK 3 T TENSOR REMARK 3 T11: 0.3294 T22: 0.0189 REMARK 3 T33: 0.4264 T12: -0.0148 REMARK 3 T13: -0.0099 T23: 0.0146 REMARK 3 L TENSOR REMARK 3 L11: 1.4474 L22: 5.1929 REMARK 3 L33: 1.7619 L12: 1.1916 REMARK 3 L13: -0.8304 L23: -1.6301 REMARK 3 S TENSOR REMARK 3 S11: 0.1433 S12: 0.0167 S13: 0.1004 REMARK 3 S21: 0.7147 S22: -0.1484 S23: 0.0523 REMARK 3 S31: -0.6497 S32: 0.0484 S33: 0.0051 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 : 1.30 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THEIR REMARK 3 RIDING POSITIONS REMARK 4 REMARK 4 6ZBP 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_1292109248. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 30-APR-20 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) : 0.97623 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XSCALE REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35506 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850 REMARK 200 RESOLUTION RANGE LOW (A) : 57.151 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5 REMARK 200 DATA REDUNDANCY : 19.70 REMARK 200 R MERGE (I) : 0.08600 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 18.2000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.90 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5 REMARK 200 DATA REDUNDANCY IN SHELL : 20.90 REMARK 200 R MERGE FOR SHELL (I) : 2.05000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.700 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: 6YZ5 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 53.12 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.62 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALS WERE GROWN AT USING THE REMARK 280 SITTING DROP VAPOR DIFFUSION METHOD BY MIXING 0.2 UL OF THE 18 REMARK 280 MG/ML H11-H4 RBD COMPLEX WITH 0.1 UL OF THE CRYSTALLIZATION REMARK 280 BUFFER CONTAINING 0.2 M SODIUM ACETATE TRIHYDRATE, 0.1 M MES PH REMARK 280 6.0, 20 % W/V PEG 8000. THE CRYSTALS GREW OVERNIGHT AND WERE REMARK 280 FLASH COOLED IN A SOLUTION CONTAINING THE MOTHER LIQUOR WITH 30 % REMARK 280 (V/V) ETHYLENE GLYCOL., VAPOR DIFFUSION, SITTING DROP, REMARK 280 TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1 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 Y,X,-Z REMARK 290 5555 X-Y,-Y,-Z+2/3 REMARK 290 6555 -X,-X+Y,-Z+1/3 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 43.89000 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 87.78000 REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000 REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 87.78000 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 43.89000 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 APPLY THE FOLLOWING TO CHAINS: EEE, 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 375 REMARK 375 SPECIAL POSITION REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL REMARK 375 POSITIONS. REMARK 375 REMARK 375 ATOM RES CSSEQI REMARK 375 HOH E 763 LIES ON A SPECIAL POSITION. 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 PRO E 330 REMARK 465 ASN E 331 REMARK 465 ILE E 332 REMARK 465 THR E 333 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 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 OE1 GLUFF 6 OE1 GLNFF 119 2.16 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 OD1 ASNEE 354 HH12 ARGEE 357 5554 1.54 REMARK 500 OD1 ASNEE 354 NH1 ARGEE 357 5554 2.18 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 PHEEE 377 88.53 -156.89 REMARK 500 ASNEE 422 -58.75 -124.74 REMARK 500 ALAFF 92 173.70 179.16 REMARK 500 REMARK 500 REMARK: NULL DBREF 6ZBPEE 330 532 UNP P0DTC2 SPIKE_SARS2 330 532 DBREF 6ZBPFF 1 134 PDB 6ZBP 6ZBP 1 134 SEQADV 6ZBP LYSEE 533 UNP P0DTC2 EXPRESSION TAG SEQADV 6ZBP HISEE 534 UNP P0DTC2 EXPRESSION TAG SEQADV 6ZBP HISEE 535 UNP P0DTC2 EXPRESSION TAG SEQADV 6ZBP HISEE 536 UNP P0DTC2 EXPRESSION TAG SEQADV 6ZBP HISEE 537 UNP P0DTC2 EXPRESSION TAG SEQADV 6ZBP HISEE 538 UNP P0DTC2 EXPRESSION TAG SEQADV 6ZBP HISEE 539 UNP P0DTC2 EXPRESSION TAG SEQRES 1EE 210 PRO ASN ILE THR ASN LEU CYS PRO PHE GLY GLU VAL PHE SEQRES 2EE 210 ASN ALA THR ARG PHE ALA SER VAL TYR ALA TRP ASN ARG SEQRES 3EE 210 LYS ARG ILE SER ASN CYS VAL ALA ASP TYR SER VAL LEU SEQRES 4EE 210 TYR ASN SER ALA SER PHE SER THR PHE LYS CYS TYR GLY SEQRES 5EE 210 VAL SER PRO THR LYS LEU ASN ASP LEU CYS PHE THR ASN SEQRES 6EE 210 VAL TYR ALA ASP SER PHE VAL ILE ARG GLY ASP GLU VAL SEQRES 7EE 210 ARG GLN ILE ALA PRO GLY GLN THR GLY LYS ILE ALA ASP SEQRES 8EE 210 TYR ASN TYR LYS LEU PRO ASP ASP PHE THR GLY CYS VAL SEQRES 9EE 210 ILE ALA TRP ASN SER ASN ASN LEU ASP SER LYS VAL GLY SEQRES 10EE 210 GLY ASN TYR ASN TYR LEU TYR ARG LEU PHE ARG LYS SER SEQRES 11EE 210 ASN LEU LYS PRO PHE GLU ARG ASP ILE SER THR GLU ILE SEQRES 12EE 210 TYR GLN ALA GLY SER THR PRO CYS ASN GLY VAL GLU GLY SEQRES 13EE 210 PHE ASN CYS TYR PHE PRO LEU GLN SER TYR GLY PHE GLN SEQRES 14EE 210 PRO THR ASN GLY VAL GLY TYR GLN PRO TYR ARG VAL VAL SEQRES 15EE 210 VAL LEU SER PHE GLU LEU LEU HIS ALA PRO ALA THR VAL SEQRES 16EE 210 CYS GLY PRO LYS LYS SER THR ASN LYS HIS HIS HIS HIS SEQRES 17EE 210 HIS HIS SEQRES 1FF 134 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU MET GLN SEQRES 2FF 134 ALA GLY GLY SER LEU ARG LEU SER CYS ALA VAL SER GLY SEQRES 3FF 134 ARG THR PHE SER THR ALA ALA MET GLY TRP PHE ARG GLN SEQRES 4FF 134 ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA ALA ILE ARG SEQRES 5FF 134 TRP SER GLY GLY SER ALA TYR TYR ALA ASP SER VAL LYS SEQRES 6FF 134 GLY ARG PHE THR ILE SER ARG ASP LYS ALA LYS ASN THR SEQRES 7FF 134 VAL TYR LEU GLN MET ASN SER LEU LYS TYR GLU ASP THR SEQRES 8FF 134 ALA VAL TYR TYR CYS ALA GLN THR HIS TYR VAL SER TYR SEQRES 9FF 134 LEU LEU SER ASP TYR ALA THR TRP PRO TYR ASP TYR TRP SEQRES 10FF 134 GLY GLN GLY THR GLN VAL THR VAL SER SER LYS HIS HIS SEQRES 11FF 134 HIS HIS HIS HIS HET NAG EE 601 28 HET SO4 FF 201 5 HETNAM NAG N-ACETYL-D-GLUCOSAMINE HETNAM SO4 SULFATE ION FORMUL 3 NAG C8 H15 N O6 FORMUL 4 SO4 O4 S 2- FORMUL 5 HOH *103(H2 O) HELIX 1 AA1 PROEE 337 ASNEE 343 1 7 HELIX 2 AA2 SEREE 349 TRPEE 353 5 5 HELIX 3 AA3 TYREE 365 ASNEE 370 1 6 HELIX 4 AA4 SEREE 383 ASNEE 388 1 6 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 THRFF 28 THRFF 31 5 4 HELIX 10 AB1 LYSFF 87 THRFF 91 5 5 HELIX 11 AB2 LEUFF 105 THRFF 111 5 7 SHEET 1 AA1 5 ASNEE 354 ILEEE 358 0 SHEET 2 AA1 5 ASNEE 394 ARGEE 403 -1 O VALEE 395 N ILEEE 358 SHEET 3 AA1 5 PROEE 507 GLUEE 516 -1 O VALEE 512 N ASPEE 398 SHEET 4 AA1 5 GLYEE 431 ASNEE 437 -1 N ILEEE 434 O VALEE 511 SHEET 5 AA1 5 THREE 376 TYREE 380 -1 N LYSEE 378 O VALEE 433 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 VALFF 2 SERFF 7 0 SHEET 2 AA5 4 LEUFF 18 GLYFF 26 -1 O SERFF 21 N SERFF 7 SHEET 3 AA5 4 THRFF 78 METFF 83 -1 O METFF 83 N LEUFF 18 SHEET 4 AA5 4 PHEFF 68 ASPFF 73 -1 N THRFF 69 O GLNFF 82 SHEET 1 AA6 6 GLYFF 10 GLNFF 13 0 SHEET 2 AA6 6 THRFF 121 SERFF 126 1 O SERFF 126 N METFF 12 SHEET 3 AA6 6 ALAFF 92 THRFF 99 -1 N TYRFF 94 O THRFF 121 SHEET 4 AA6 6 ALAFF 33 GLNFF 39 -1 N PHEFF 37 O TYRFF 95 SHEET 5 AA6 6 GLUFF 46 ARGFF 52 -1 O ALAFF 49 N TRPFF 36 SHEET 6 AA6 6 ALAFF 58 TYRFF 60 -1 O TYRFF 59 N ALAFF 50 SHEET 1 AA7 4 GLYFF 10 GLNFF 13 0 SHEET 2 AA7 4 THRFF 121 SERFF 126 1 O SERFF 126 N METFF 12 SHEET 3 AA7 4 ALAFF 92 THRFF 99 -1 N TYRFF 94 O THRFF 121 SHEET 4 AA7 4 TYRFF 116 TRPFF 117 -1 O TYRFF 116 N GLNFF 98 SSBOND 1 CYSEE 336 CYSEE 361 1555 1555 2.06 SSBOND 2 CYSEE 379 CYSEE 432 1555 1555 2.25 SSBOND 3 CYSEE 391 CYSEE 525 1555 1555 2.12 SSBOND 4 CYSEE 480 CYSEE 488 1555 1555 2.19 SSBOND 5 CYSFF 22 CYSFF 96 1555 1555 2.09 LINK ND2 ASNEE 343 C1 NAGEE 601 1555 1555 1.44 CRYST1 73.150 73.150 131.670 90.00 90.00 120.00 P 31 2 1 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 0.013671 0.007893 0.000000 0.00000 SCALE2 0.000000 0.015785 0.000000 0.00000 SCALE3 0.000000 0.000000 0.007595 0.00000