HEADER ANTIVIRAL PROTEIN 21-JUN-20 6ZH9 TITLE TERNARY COMPLEX CR3022 H11-H4 AND RBD (SARS-COV-2) COMPND MOL_ID: 1; COMPND 2 MOLECULE: CR3022 HEAVY; COMPND 3 CHAIN: HHH; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: CR3022 LIGHT CHAIN; COMPND 7 CHAIN: LLL; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: SPIKE GLYCOPROTEIN; COMPND 11 CHAIN: EEE; COMPND 12 SYNONYM: S GLYCOPROTEIN,E2,PEPLOMER PROTEIN; COMPND 13 ENGINEERED: YES; COMPND 14 MOL_ID: 4; COMPND 15 MOLECULE: NANOBODY H11-H4; COMPND 16 CHAIN: FFF; COMPND 17 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 8 ORGANISM_TAXID: 9606; 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_COMMON: 2019-NCOV; SOURCE 15 ORGANISM_TAXID: 2697049; SOURCE 16 GENE: S, 2; SOURCE 17 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 18 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 19 MOL_ID: 4; SOURCE 20 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 21 ORGANISM_TAXID: 9844; SOURCE 22 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 23 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS COVID19, NANOBODY, SARS-COV-2, ANTIVIRAL PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR J.H.NAISMITH,H.MIKOLAJEK,A.LE BAS JRNL AUTH J.HUO,A.LE BAS,R.R.RUZA,H.M.E.DUYVESTEYN,H.MIKOLAJEK, JRNL AUTH 2 T.MALINAUSKAS,T.K.TAN,P.RIJAL,M.DUMOUX,P.N.WARD,J.REN, JRNL AUTH 3 D.ZHOU,P.J.HARRISON,M.WECKENER,D.K.CLARE,V.K.VOGIRALA, JRNL AUTH 4 J.RADECKE,L.MOYNIE,Y.ZHAO,J.GILBERT-JARAMILLO,M.L.KNIGHT, JRNL AUTH 5 J.A.TREE,K.R.BUTTIGIEG,N.COOMBES,M.J.ELMORE,M.W.CARROLL, JRNL AUTH 6 L.CARRIQUE,P.N.M.SHAH,W.JAMES,A.R.TOWNSEND,D.I.STUART, JRNL AUTH 7 R.J.OWENS,J.H.NAISMITH JRNL TITL NEUTRALIZING NANOBODIES BIND SARS-COV-2 SPIKE RBD AND BLOCK JRNL TITL 2 INTERACTION WITH ACE2. JRNL REF NAT.STRUCT.MOL.BIOL. V. 27 846 2020 JRNL REFN ESSN 1545-9985 JRNL PMID 32661423 JRNL DOI 10.1038/S41594-020-0469-6 REMARK 2 REMARK 2 RESOLUTION. 3.31 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) : 3.31 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 80.24 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 3 NUMBER OF REFLECTIONS : 22065 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) : 0.261 REMARK 3 FREE R VALUE : 0.305 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.931 REMARK 3 FREE R VALUE TEST SET COUNT : 1088 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) : 3.31 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.40 REMARK 3 REFLECTION IN BIN (WORKING SET) : 1494 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.62 REMARK 3 BIN R VALUE (WORKING SET) : 0.4050 REMARK 3 BIN FREE R VALUE SET COUNT : 89 REMARK 3 BIN FREE R VALUE : 0.4160 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 5856 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 0 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 134.0 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -1.69600 REMARK 3 B22 (A**2) : -1.69600 REMARK 3 B33 (A**2) : 3.39200 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): NULL REMARK 3 ESU BASED ON FREE R VALUE (A): 0.545 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.696 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 109.814 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.830 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.900 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6072 ; 0.008 ; 0.013 REMARK 3 BOND LENGTHS OTHERS (A): 5372 ; 0.001 ; 0.017 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8275 ; 1.626 ; 1.646 REMARK 3 BOND ANGLES OTHERS (DEGREES): 12533 ; 1.228 ; 1.571 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 797 ;21.543 ; 5.351 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 275 ;35.970 ;22.982 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 939 ;17.099 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 24 ;17.991 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 788 ; 0.059 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7576 ; 0.006 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 1299 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 920 ; 0.185 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 55 ; 0.254 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2807 ; 0.174 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 120 ; 0.143 ; 0.200 REMARK 3 H-BOND (X...Y) OTHERS (A): 1 ; 0.074 ; 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): 3051 ; 7.791 ;11.681 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3050 ; 7.787 ;11.682 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3812 ;12.289 ;17.510 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 3813 ;12.288 ;17.509 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3020 ; 7.250 ;11.932 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 3021 ; 7.249 ;11.931 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 4455 ;11.809 ;17.759 REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 4456 ;11.808 ;17.759 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 : 4 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 : HH 0 HH 219 REMARK 3 ORIGIN FOR THE GROUP (A): 21.2400 -32.6080 -52.8360 REMARK 3 T TENSOR REMARK 3 T11: 0.8045 T22: 0.8055 REMARK 3 T33: 0.6448 T12: 0.4208 REMARK 3 T13: 0.3793 T23: 0.5013 REMARK 3 L TENSOR REMARK 3 L11: 2.6597 L22: 2.4890 REMARK 3 L33: 2.9376 L12: -0.4119 REMARK 3 L13: -2.0767 L23: 1.9829 REMARK 3 S TENSOR REMARK 3 S11: 0.4842 S12: 0.0381 S13: 0.6667 REMARK 3 S21: -0.0637 S22: -0.0698 S23: 0.4182 REMARK 3 S31: -0.5798 S32: -0.3661 S33: -0.4144 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 : LL 1 LL 219 REMARK 3 ORIGIN FOR THE GROUP (A): 19.3860 -45.3110 -39.5160 REMARK 3 T TENSOR REMARK 3 T11: 0.7090 T22: 0.5765 REMARK 3 T33: 0.4918 T12: 0.1125 REMARK 3 T13: 0.4336 T23: 0.2537 REMARK 3 L TENSOR REMARK 3 L11: 4.8350 L22: 1.0817 REMARK 3 L33: 4.1466 L12: -1.7169 REMARK 3 L13: -2.7547 L23: 1.8806 REMARK 3 S TENSOR REMARK 3 S11: 0.0385 S12: -0.1652 S13: -0.1541 REMARK 3 S21: 0.3322 S22: -0.0645 S23: 0.2715 REMARK 3 S31: 0.3703 S32: -0.2009 S33: 0.0260 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 334 EE 528 REMARK 3 ORIGIN FOR THE GROUP (A): 40.2430 -60.0630 -86.0950 REMARK 3 T TENSOR REMARK 3 T11: 0.3471 T22: 0.8091 REMARK 3 T33: 0.1049 T12: -0.0450 REMARK 3 T13: -0.0231 T23: -0.1115 REMARK 3 L TENSOR REMARK 3 L11: 3.7665 L22: 6.1422 REMARK 3 L33: 3.2516 L12: 1.6413 REMARK 3 L13: 0.4344 L23: 1.7619 REMARK 3 S TENSOR REMARK 3 S11: -0.3634 S12: 0.8443 S13: -0.0714 REMARK 3 S21: -0.2389 S22: 0.7744 S23: -0.1956 REMARK 3 S31: -0.0859 S32: -0.3469 S33: -0.4111 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 : FF 1 FF 128 REMARK 3 ORIGIN FOR THE GROUP (A): 44.7910 -67.0160-122.0690 REMARK 3 T TENSOR REMARK 3 T11: 2.2600 T22: 2.9487 REMARK 3 T33: 0.6839 T12: -0.7234 REMARK 3 T13: 0.2571 T23: -0.5278 REMARK 3 L TENSOR REMARK 3 L11: 1.4255 L22: 2.2119 REMARK 3 L33: 0.3569 L12: -1.7493 REMARK 3 L13: 0.6797 L23: -0.8065 REMARK 3 S TENSOR REMARK 3 S11: 0.6456 S12: 0.6357 S13: 0.2229 REMARK 3 S21: -1.1106 S22: -0.5932 S23: -0.4475 REMARK 3 S31: 0.2691 S32: 0.2289 S33: -0.0524 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 : 1.00 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 6ZH9 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_1292109531. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 18-JUN-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) : 0.98 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 : XDS REMARK 200 DATA SCALING SOFTWARE : POINTLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22105 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.310 REMARK 200 RESOLUTION RANGE LOW (A) : 80.253 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 25.60 REMARK 200 R MERGE (I) : 0.09100 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 0.0180 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.31 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.40 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 3.90000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 0.500 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: 6ZBY REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 70.85 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.22 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: MIXING 0.2 UL OF THE 18 MG/ML COMPLEX REMARK 280 WITH 0.1 UL OF THE CRYSTALLIZATION BUFFER CONTAINING 0.2 M REMARK 280 SODIUM ACETATE TRIHYDRATE, 0.1 M MES PH 6.0, 20 % W/V PEG 8000., REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 42 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 -Y+1/2,X+1/2,Z+1/2 REMARK 290 4555 Y+1/2,-X+1/2,Z+1/2 REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/2 REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/2 REMARK 290 7555 Y,X,-Z REMARK 290 8555 -Y,-X,-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 0.000000 -1.000000 0.000000 78.20550 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 78.20550 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 58.10250 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 78.20550 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 78.20550 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 58.10250 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 78.20550 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 78.20550 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 58.10250 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 78.20550 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 78.20550 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 58.10250 REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 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: TETRAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 6510 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 33960 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: HHH, LLL, 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 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 ILE E 332 REMARK 465 THR E 333 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: 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 CYSHH 22 103.10 -160.24 REMARK 500 METHH 48 -62.17 -91.06 REMARK 500 ASPHH 55 16.53 -146.79 REMARK 500 PROHH 62 -28.58 -39.04 REMARK 500 VALHH 117 74.94 -112.07 REMARK 500 ASPHH 148 82.79 58.05 REMARK 500 THRHH 195 -70.20 -111.73 REMARK 500 LEULL 15 142.48 -34.33 REMARK 500 ASNLL 35 66.87 -64.15 REMARK 500 ALALL 57 -33.22 72.92 REMARK 500 ALALL 90 -175.49 -172.91 REMARK 500 ASNLL 144 74.47 58.73 REMARK 500 GLULL 149 108.48 -40.93 REMARK 500 ASPLL 157 37.15 77.12 REMARK 500 PHEEE 377 84.32 -151.98 REMARK 500 ASNEE 422 -56.27 -123.71 REMARK 500 HISEE 519 42.14 -96.33 REMARK 500 VALFF 48 -62.57 -108.95 REMARK 500 REMARK 500 REMARK: NULL DBREF 6ZH9HH 0 219 PDB 6ZH9 6ZH9 0 219 DBREF 6ZH9LL 1 219 PDB 6ZH9 6ZH9 1 219 DBREF 6ZH9EE 332 528 UNP P0DTC2 SPIKE_SARS2 332 528 DBREF 6ZH9FF 1 134 PDB 6ZH9 6ZH9 1 134 SEQRES 1HH 216 THR GLN MET GLN LEU VAL GLN SER GLY THR GLU VAL LYS SEQRES 2HH 216 LYS PRO GLY GLU SER LEU LYS ILE SER CYS LYS GLY SER SEQRES 3HH 216 GLY TYR GLY PHE ILE THR TYR TRP ILE GLY TRP VAL ARG SEQRES 4HH 216 GLN MET PRO GLY LYS GLY LEU GLU TRP MET GLY ILE ILE SEQRES 5HH 216 TYR PRO GLY ASP SER GLU THR ARG TYR SER PRO SER PHE SEQRES 6HH 216 GLN GLY GLN VAL THR ILE SER ALA ASP LYS SER ILE ASN SEQRES 7HH 216 THR ALA TYR LEU GLN TRP SER SER LEU LYS ALA SER ASP SEQRES 8HH 216 THR ALA ILE TYR TYR CYS ALA GLY GLY SER GLY ILE SER SEQRES 9HH 216 THR PRO MET ASP VAL TRP GLY GLN GLY THR THR VAL THR SEQRES 10HH 216 VAL ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA SEQRES 11HH 216 PRO SER SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL SEQRES 12HH 216 LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SEQRES 13HH 216 SER GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA SEQRES 14HH 216 VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL SEQRES 15HH 216 VAL THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR SEQRES 16HH 216 ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL SEQRES 17HH 216 ASP LYS LYS VAL GLU PRO LYS SER SEQRES 1LL 219 ASP ILE GLN LEU THR GLN SER PRO ASP SER LEU ALA VAL SEQRES 2LL 219 SER LEU GLY GLU ARG ALA THR ILE ASN CYS LYS SER SER SEQRES 3LL 219 GLN SER VAL LEU TYR SER SER ILE ASN LYS ASN TYR LEU SEQRES 4LL 219 ALA TRP TYR GLN GLN LYS PRO GLY GLN PRO PRO LYS LEU SEQRES 5LL 219 LEU ILE TYR TRP ALA SER THR ARG GLU SER GLY VAL PRO SEQRES 6LL 219 ASP ARG PHE SER GLY SER GLY SER GLY THR ASP PHE THR SEQRES 7LL 219 LEU THR ILE SER SER LEU GLN ALA GLU ASP VAL ALA VAL SEQRES 8LL 219 TYR TYR CYS GLN GLN TYR TYR SER THR PRO TYR THR PHE SEQRES 9LL 219 GLY GLN GLY THR LYS VAL GLU ILE LYS ARG THR VAL ALA SEQRES 10LL 219 ALA PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN SEQRES 11LL 219 LEU LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN SEQRES 12LL 219 ASN PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL SEQRES 13LL 219 ASP ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL SEQRES 14LL 219 THR GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER SEQRES 15LL 219 SER THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS SEQRES 16LL 219 LYS VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SEQRES 17LL 219 SER PRO VAL THR LYS SER PHE ASN ARG GLY GLU SEQRES 1EE 197 ILE THR ASN LEU CYS PRO PHE GLY GLU VAL PHE ASN ALA SEQRES 2EE 197 THR ARG PHE ALA SER VAL TYR ALA TRP ASN ARG LYS ARG SEQRES 3EE 197 ILE SER ASN CYS VAL ALA ASP TYR SER VAL LEU TYR ASN SEQRES 4EE 197 SER ALA SER PHE SER THR PHE LYS CYS TYR GLY VAL SER SEQRES 5EE 197 PRO THR LYS LEU ASN ASP LEU CYS PHE THR ASN VAL TYR SEQRES 6EE 197 ALA ASP SER PHE VAL ILE ARG GLY ASP GLU VAL ARG GLN SEQRES 7EE 197 ILE ALA PRO GLY GLN THR GLY LYS ILE ALA ASP TYR ASN SEQRES 8EE 197 TYR LYS LEU PRO ASP ASP PHE THR GLY CYS VAL ILE ALA SEQRES 9EE 197 TRP ASN SER ASN ASN LEU ASP SER LYS VAL GLY GLY ASN SEQRES 10EE 197 TYR ASN TYR LEU TYR ARG LEU PHE ARG LYS SER ASN LEU SEQRES 11EE 197 LYS PRO PHE GLU ARG ASP ILE SER THR GLU ILE TYR GLN SEQRES 12EE 197 ALA GLY SER THR PRO CYS ASN GLY VAL GLU GLY PHE ASN SEQRES 13EE 197 CYS TYR PHE PRO LEU GLN SER TYR GLY PHE GLN PRO THR SEQRES 14EE 197 ASN GLY VAL GLY TYR GLN PRO TYR ARG VAL VAL VAL LEU SEQRES 15EE 197 SER PHE GLU LEU LEU HIS ALA PRO ALA THR VAL CYS GLY SEQRES 16EE 197 PRO LYS 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 HELIX 1 AA1 GLYHH 28 TYRHH 32 5 5 HELIX 2 AA2 LYSHH 74 ILEHH 76 5 3 HELIX 3 AA3 LYSHH 87 THRHH 91 5 5 HELIX 4 AA4 SERHH 160 ALAHH 162 5 3 HELIX 5 AA5 SERHH 191 THRHH 195 5 5 HELIX 6 AA6 LYSHH 205 ASNHH 208 5 4 HELIX 7 AA7 GLNLL 85 VALLL 89 5 5 HELIX 8 AA8 GLULL 129 SERLL 133 5 5 HELIX 9 AA9 LYSLL 189 GLULL 193 1 5 HELIX 10 AB1 PROEE 337 ASNEE 343 1 7 HELIX 11 AB2 SEREE 349 TRPEE 353 5 5 HELIX 12 AB3 TYREE 365 ASNEE 370 1 6 HELIX 13 AB4 LYSEE 386 ASPEE 389 5 4 HELIX 14 AB5 ASPEE 405 ILEEE 410 5 6 HELIX 15 AB6 GLYEE 416 ASNEE 422 1 7 HELIX 16 AB7 SEREE 438 SEREE 443 1 6 HELIX 17 AB8 GLYEE 502 TYREE 505 5 4 HELIX 18 AB9 THRFF 28 THRFF 31 5 4 HELIX 19 AC1 LYSFF 87 THRFF 91 5 5 HELIX 20 AC2 LEUFF 105 THRFF 111 5 7 SHEET 1 AA1 4 GLNHH 3 GLNHH 6 0 SHEET 2 AA1 4 LEUHH 18 SERHH 25 -1 O SERHH 25 N GLNHH 3 SHEET 3 AA1 4 THRHH 78 TRPHH 83 -1 O TRPHH 83 N LEUHH 18 SHEET 4 AA1 4 THRHH 69 ASPHH 73 -1 N SERHH 71 O TYRHH 80 SHEET 1 AA2 6 GLUHH 10 LYSHH 12 0 SHEET 2 AA2 6 THRHH 113 VALHH 117 1 O THRHH 116 N LYSHH 12 SHEET 3 AA2 6 ALAHH 92 GLYHH 99 -1 N TYRHH 94 O THRHH 113 SHEET 4 AA2 6 TRPHH 33 GLNHH 39 -1 N GLYHH 35 O ALAHH 97 SHEET 5 AA2 6 GLUHH 46 TYRHH 52 -1 O GLUHH 46 N ARGHH 38 SHEET 6 AA2 6 GLUHH 57 TYRHH 60 -1 O ARGHH 59 N ILEHH 50 SHEET 1 AA3 4 GLUHH 10 LYSHH 12 0 SHEET 2 AA3 4 THRHH 113 VALHH 117 1 O THRHH 116 N LYSHH 12 SHEET 3 AA3 4 ALAHH 92 GLYHH 99 -1 N TYRHH 94 O THRHH 113 SHEET 4 AA3 4 VALHH 108 TRPHH 109 -1 O VALHH 108 N GLYHH 98 SHEET 1 AA4 4 SERHH 124 LEUHH 128 0 SHEET 2 AA4 4 THRHH 139 TYRHH 149 -1 O LEUHH 145 N PHEHH 126 SHEET 3 AA4 4 TYRHH 180 PROHH 189 -1 O TYRHH 180 N TYRHH 149 SHEET 4 AA4 4 VALHH 167 THRHH 169 -1 N HISHH 168 O VALHH 185 SHEET 1 AA5 4 SERHH 124 LEUHH 128 0 SHEET 2 AA5 4 THRHH 139 TYRHH 149 -1 O LEUHH 145 N PHEHH 126 SHEET 3 AA5 4 TYRHH 180 PROHH 189 -1 O TYRHH 180 N TYRHH 149 SHEET 4 AA5 4 VALHH 173 LEUHH 174 -1 N VALHH 173 O SERHH 181 SHEET 1 AA6 3 THRHH 155 TRPHH 158 0 SHEET 2 AA6 3 TYRHH 198 HISHH 204 -1 O ASNHH 201 N SERHH 157 SHEET 3 AA6 3 THRHH 209 VALHH 215 -1 O VALHH 211 N VALHH 202 SHEET 1 AA7 4 LEULL 4 SERLL 7 0 SHEET 2 AA7 4 ALALL 19 SERLL 25 -1 O ASNLL 22 N SERLL 7 SHEET 3 AA7 4 ASPLL 76 ILELL 81 -1 O ILELL 81 N ALALL 19 SHEET 4 AA7 4 PHELL 68 SERLL 73 -1 N SERLL 71 O THRLL 78 SHEET 1 AA8 6 SERLL 10 VALLL 13 0 SHEET 2 AA8 6 THRLL 108 ILELL 112 1 O GLULL 111 N VALLL 13 SHEET 3 AA8 6 ALALL 90 GLNLL 96 -1 N TYRLL 92 O THRLL 108 SHEET 4 AA8 6 LEULL 39 GLNLL 44 -1 N TYRLL 42 O TYRLL 93 SHEET 5 AA8 6 LYSLL 51 TYRLL 55 -1 O LYSLL 51 N GLNLL 43 SHEET 6 AA8 6 THRLL 59 ARGLL 60 -1 O THRLL 59 N TYRLL 55 SHEET 1 AA9 4 SERLL 10 VALLL 13 0 SHEET 2 AA9 4 THRLL 108 ILELL 112 1 O GLULL 111 N VALLL 13 SHEET 3 AA9 4 ALALL 90 GLNLL 96 -1 N TYRLL 92 O THRLL 108 SHEET 4 AA9 4 THRLL 103 PHELL 104 -1 O THRLL 103 N GLNLL 96 SHEET 1 AB1 2 LEULL 30 TYRLL 31 0 SHEET 2 AB1 2 LYSLL 36 ASNLL 37 -1 O LYSLL 36 N TYRLL 31 SHEET 1 AB2 4 SERLL 120 PHELL 124 0 SHEET 2 AB2 4 THRLL 135 PHELL 145 -1 O LEULL 141 N PHELL 122 SHEET 3 AB2 4 TYRLL 179 SERLL 188 -1 O LEULL 185 N VALLL 138 SHEET 4 AB2 4 SERLL 165 VALLL 169 -1 N GLNLL 166 O THRLL 184 SHEET 1 AB3 4 LEULL 160 GLNLL 161 0 SHEET 2 AB3 4 ALALL 150 LYSLL 155 -1 N TRPLL 154 O GLNLL 161 SHEET 3 AB3 4 VALLL 197 HISLL 204 -1 O GLULL 201 N GLNLL 153 SHEET 4 AB3 4 VALLL 211 ASNLL 216 -1 O PHELL 215 N TYRLL 198 SHEET 1 AB4 5 ASNEE 354 ILEEE 358 0 SHEET 2 AB4 5 ASNEE 394 ARGEE 403 -1 O VALEE 395 N ILEEE 358 SHEET 3 AB4 5 PROEE 507 GLUEE 516 -1 O TYREE 508 N ILEEE 402 SHEET 4 AB4 5 GLYEE 431 ASNEE 437 -1 N ILEEE 434 O VALEE 511 SHEET 5 AB4 5 THREE 376 TYREE 380 -1 N LYSEE 378 O VALEE 433 SHEET 1 AB5 3 CYSEE 361 VALEE 362 0 SHEET 2 AB5 3 VALEE 524 CYSEE 525 1 O CYSEE 525 N CYSEE 361 SHEET 3 AB5 3 CYSEE 391 PHEEE 392 -1 N PHEEE 392 O VALEE 524 SHEET 1 AB6 2 LEUEE 452 ARGEE 454 0 SHEET 2 AB6 2 LEUEE 492 SEREE 494 -1 O GLNEE 493 N TYREE 453 SHEET 1 AB7 2 TYREE 473 GLNEE 474 0 SHEET 2 AB7 2 CYSEE 488 TYREE 489 -1 O TYREE 489 N TYREE 473 SHEET 1 AB8 4 VALFF 2 SERFF 7 0 SHEET 2 AB8 4 LEUFF 18 GLYFF 26 -1 O ALAFF 23 N VALFF 5 SHEET 3 AB8 4 THRFF 78 METFF 83 -1 O METFF 83 N LEUFF 18 SHEET 4 AB8 4 PHEFF 68 ASPFF 73 -1 N THRFF 69 O GLNFF 82 SHEET 1 AB9 6 LEUFF 11 GLNFF 13 0 SHEET 2 AB9 6 THRFF 121 SERFF 126 1 O SERFF 126 N METFF 12 SHEET 3 AB9 6 ALAFF 92 THRFF 99 -1 N TYRFF 94 O THRFF 121 SHEET 4 AB9 6 ALAFF 33 GLNFF 39 -1 N PHEFF 37 O TYRFF 95 SHEET 5 AB9 6 GLUFF 46 ARGFF 52 -1 O ALAFF 49 N TRPFF 36 SHEET 6 AB9 6 ALAFF 58 TYRFF 60 -1 O TYRFF 59 N ALAFF 50 SHEET 1 AC1 4 LEUFF 11 GLNFF 13 0 SHEET 2 AC1 4 THRFF 121 SERFF 126 1 O SERFF 126 N METFF 12 SHEET 3 AC1 4 ALAFF 92 THRFF 99 -1 N TYRFF 94 O THRFF 121 SHEET 4 AC1 4 TYRFF 116 TRPFF 117 -1 O TYRFF 116 N GLNFF 98 SSBOND 1 CYSHH 22 CYSHH 96 1555 1555 2.02 SSBOND 2 CYSHH 144 CYSHH 200 1555 1555 2.06 SSBOND 3 CYSLL 23 CYSLL 94 1555 1555 2.09 SSBOND 4 CYSLL 140 CYSLL 200 1555 1555 2.03 SSBOND 5 CYSEE 336 CYSEE 361 1555 1555 2.08 SSBOND 6 CYSEE 379 CYSEE 432 1555 1555 2.06 SSBOND 7 CYSEE 391 CYSEE 525 1555 1555 2.06 SSBOND 8 CYSEE 480 CYSEE 488 1555 1555 2.05 SSBOND 9 CYSFF 22 CYSFF 96 1555 1555 2.04 CISPEP 1 PHEHH 150 PROHH 151 0 -16.96 CISPEP 2 GLUHH 152 PROHH 153 0 4.55 CISPEP 3 SERLL 7 PROLL 8 0 -1.57 CISPEP 4 THRLL 100 PROLL 101 0 2.95 CISPEP 5 TYRLL 146 PROLL 147 0 -9.13 CRYST1 156.411 156.411 116.205 90.00 90.00 90.00 P 42 21 2 8 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 0.006393 0.000000 0.000000 0.00000 SCALE2 0.000000 0.006393 0.000000 0.00000 SCALE3 0.000000 0.000000 0.008605 0.00000