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- PDB-8drz: Product structure of SARS-CoV-2 Mpro C145A mutant in complex with... -

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Basic information

Entry
Database: PDB / ID: 8drz
TitleProduct structure of SARS-CoV-2 Mpro C145A mutant in complex with nsp13-nsp14 (C13) cut site sequence
Components3C-like proteinase nsp5
KeywordsVIRAL PROTEIN / Viral protease / SARS-CoV-2
Function / homology
Function and homology information


protein guanylyltransferase activity / RNA endonuclease activity, producing 3'-phosphomonoesters / mRNA guanylyltransferase activity / 5'-3' RNA helicase activity / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of TBK1 activity / Lyases; Phosphorus-oxygen lyases / Assembly of the SARS-CoV-2 Replication-Transcription Complex (RTC) / Maturation of replicase proteins / ISG15-specific peptidase activity / Transcription of SARS-CoV-2 sgRNAs ...protein guanylyltransferase activity / RNA endonuclease activity, producing 3'-phosphomonoesters / mRNA guanylyltransferase activity / 5'-3' RNA helicase activity / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of TBK1 activity / Lyases; Phosphorus-oxygen lyases / Assembly of the SARS-CoV-2 Replication-Transcription Complex (RTC) / Maturation of replicase proteins / ISG15-specific peptidase activity / Transcription of SARS-CoV-2 sgRNAs / Translation of Replicase and Assembly of the Replication Transcription Complex / TRAF3-dependent IRF activation pathway / snRNP Assembly / Replication of the SARS-CoV-2 genome / double membrane vesicle viral factory outer membrane / Hydrolases; Acting on ester bonds; Exoribonucleases producing 5'-phosphomonoesters / SARS coronavirus main proteinase / host cell endosome / 3'-5'-RNA exonuclease activity / : / host cell endoplasmic reticulum-Golgi intermediate compartment / symbiont-mediated suppression of host toll-like receptor signaling pathway / symbiont-mediated degradation of host mRNA / mRNA guanylyltransferase / symbiont-mediated suppression of host ISG15-protein conjugation / G-quadruplex RNA binding / SARS-CoV-2 modulates host translation machinery / omega peptidase activity / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF3 activity / mRNA (guanine-N7)-methyltransferase / methyltransferase cap1 / host cell Golgi apparatus / symbiont-mediated perturbation of host ubiquitin-like protein modification / mRNA (nucleoside-2'-O-)-methyltransferase activity / mRNA 5'-cap (guanine-N7-)-methyltransferase activity / DNA helicase / ubiquitinyl hydrolase 1 / cysteine-type deubiquitinase activity / Hydrolases; Acting on peptide bonds (peptidases); Cysteine endopeptidases / single-stranded RNA binding / host cell endoplasmic reticulum membrane / host cell perinuclear region of cytoplasm / viral protein processing / lyase activity / RNA helicase / induction by virus of host autophagy / RNA-directed RNA polymerase / copper ion binding / symbiont-mediated suppression of host gene expression / viral RNA genome replication / cysteine-type endopeptidase activity / RNA-dependent RNA polymerase activity / DNA-templated transcription / lipid binding / symbiont-mediated suppression of host type I interferon-mediated signaling pathway / host cell nucleus / SARS-CoV-2 activates/modulates innate and adaptive immune responses / ATP hydrolysis activity / proteolysis / RNA binding / zinc ion binding / ATP binding / membrane
Similarity search - Function
RNA-dependent RNA polymerase, SARS-CoV-like / Nonstructural protein 14, betacoronavirus / NSP15, NendoU domain, coronavirus / : / : / Coronavirus Nonstructural protein 13, 1B domain / Coronavirus Non-structural protein 13, zinc-binding domain / Coronavirus Nonstructural protein 13, stalk domain / : / Coronavirus Nsp12 Interface domain profile. ...RNA-dependent RNA polymerase, SARS-CoV-like / Nonstructural protein 14, betacoronavirus / NSP15, NendoU domain, coronavirus / : / : / Coronavirus Nonstructural protein 13, 1B domain / Coronavirus Non-structural protein 13, zinc-binding domain / Coronavirus Nonstructural protein 13, stalk domain / : / Coronavirus Nsp12 Interface domain profile. / Nonstructural protein 15, middle domain, alpha/betacoronavirus / Nonstructural protein 15, N-terminal domain, alpha/beta-coronavirus / NSP14, guanine-N7-methyltransferase domain, coronavirus / NSP12 RNA-dependent RNA polymerase, coronavirus / Coronavirus (CoV) guanine-N7-methyltransferase (N7-MTase) domain profile. / Coronavirus (CoV) Nsp15 N-terminal oligomerization domain profile. / Nidovirus 2-O-methyltransferase / Coronavirus Nsp12 RNA-dependent RNA polymerase (RdRp) domain profile. / Nidovirus 3'-5' exoribonuclease domain / Nidovirus 2'-O-methyltransferase (2'-O-MTase) domain profile. / Nidovirus 3'-5' exoribonuclease (ExoN) domain profile. / Nonstructural protein 13, 1B domain, coronavirus / Arterivirus Nsp11 N-terminal/Coronavirus NSP15 middle domain / Non-structural protein NSP15, N-terminal domain superfamily, coronavirus / Non-structural protein NSP15, middle domain superfamily / Coronavirus replicase NSP15, N-terminal oligomerization / Nonstructural protein 15, middle domain, coronavirus / Coronavirus replicase NSP15, middle domain / Coronavirus replicase NSP15, N-terminal oligomerisation / Arterivirus Nsp11 N-terminal/coronavirus NSP15 middle (AV-Nsp11N/CoV-Nsp15M) domain profile. / Non-structural protein NSP16, coronavirus-like / Non-structural protein 14, coronavirus / RNA polymerase, N-terminal, coronavirus / Coronavirus 2'-O-methyltransferase / Coronavirus proofreading exoribonuclease / Coronavirus RNA-dependent RNA polymerase, N-terminal / Nidoviral uridylate-specific endoribonuclease (NendoU) domain profile. / Nidovirus RdRp-associated nucleotidyl transferase (NiRAN) domain / Nonstructural protein 13, zinc-binding domain, coronavirus-like / Coronaviridae zinc-binding (CV ZBD) domain profile. / Nidovirus RdRp-associated nucleotidyl transferase (NiRAN) domain profile. / Endoribonuclease EndoU-like / NendoU domain, nidovirus / Coronavirus replicase NSP15, uridylate-specific endoribonuclease / DNA2/NAM7 helicase-like, C-terminal / AAA domain / (+) RNA virus helicase core domain / (+)RNA virus helicase core domain profile. / Lipocalin signature. / Non-structural protein NSP3, SUD-N (Mac2) domain, betacoronavirus / Sarbecovirus Nsp3c-N domain profile. / Non-structural protein NSP3, N-terminal, betacoronavirus / Polyprotein cleavage domain PL2pro superfamily, betacoronavirus / Non-structural protein NSP3, SUD-N (Mac2) domain superfamily, betacoronavirus / Betacoronavirus SUD-C domain / Betacoronavirus replicase NSP3, N-terminal / NSP1 globular domain superfamily, betacoronavirus / Non-structural protein 2, SARS-CoV-like / Carbamoyl-phosphate synthase subdomain signature 2. / Coronavirus 3Ecto domain profile. / : / Betacoronavirus Nsp3e group 2-specific marker (G2M) domain profile. / NSP1, C-terminal domain, betacoronavirus / Betacoronavirus Nsp3c-M domain profile. / NSP1, globular domain, betacoronavirus / Non-structural protein NSP3, SUD-M domain, betacoronavirus / Non-structural protein NSP3, SUD-M domain superfamily, betacoronavirus / Betacoronavirus replicase NSP1 / Betacoronavirus single-stranded poly(A) binding domain / Betacoronavirus (BetaCoV) Nsp1 C-terminal domain profile. / Betacoronavirus Nsp3c-C domain profile. / Betacoronavirus Nsp3e nucleic acid-binding (NAB) domain profile. / DPUP/SUD, C-terminal, betacoronavirus / Non-structural protein NSP3, nucleic acid-binding domain superfamily, betacoronavirus / Non-structural protein 6, betacoronavirus / Betacoronavirus nucleic acid-binding (NAB) / Non-structural protein NSP3, nucleic acid-binding domain, betacoronavirus / Non-structural protein NSP3A domain-like superfamily / Papain-like protease, N-terminal domain superfamily, coronavirus / Papain-like viral protease, palm and finger domains, coronavirus / : / Coronavirus (CoV) Nsp2 middle domain profile. / Coronavirus (CoV) Nsp2 N-terminal domain profile. / Coronavirus (CoV) Nsp2 C-terminal domain profile. / NSP1, globular domain, alpha/betacoronavirus / : / Coronavirus (CoV) Nsp3 Y domain profile. / Coronavirus (CoV) Nsp1 globular domain profile. / Coronavirus replicase NSP2, N-terminal / Nonstructural protein 2, N-terminal domain, coronavirus / Coronavirus replicase NSP2, C-terminal / Non-structural protein 2, C-terminal domain, coronavirus / Coronavirus Nsp3a Ubl domain profile. / Coronavirus Nsp3d Ubl domain profile. / Coronavirus RNA-dependent RNA polymerase (RdRp) Nsp7 cofactor domain profile. / Coronavirus RNA-dependent RNA polymerase (RdRp) Nsp8 cofactor domain profile. / Coronavirus Nsp9 single-stranded RNA (ssRNA)-binding domain profile. / Coronavirus (CoV) ExoN/MTase coactivator domain profile. / NSP3, first ubiquitin-like (Ubl) domain, coronavirus / NSP3, second ubiquitin-like (Ubl) domain, coronavirus
Similarity search - Domain/homology
DI(HYDROXYETHYL)ETHER / Replicase polyprotein 1ab
Similarity search - Component
Biological speciesSevere acute respiratory syndrome coronavirus 2
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.98 Å
AuthorsLee, J. / Kenward, C. / Worrall, L.J. / Vuckovic, M. / Paetzel, M. / Strynadka, N.C.J.
Funding support Canada, 1items
OrganizationGrant numberCountry
Canadian Institutes of Health Research (CIHR) Canada
CitationJournal: Nat Commun / Year: 2022
Title: X-ray crystallographic characterization of the SARS-CoV-2 main protease polyprotein cleavage sites essential for viral processing and maturation.
Authors: Lee, J. / Kenward, C. / Worrall, L.J. / Vuckovic, M. / Gentile, F. / Ton, A.T. / Ng, M. / Cherkasov, A. / Strynadka, N.C.J. / Paetzel, M.
History
DepositionJul 21, 2022Deposition site: RCSB / Processing site: RCSB
Revision 1.0Sep 28, 2022Provider: repository / Type: Initial release
Revision 1.1Oct 12, 2022Group: Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _citation_author.identifier_ORCID / _citation_author.name
Revision 1.2Oct 18, 2023Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: 3C-like proteinase nsp5
B: 3C-like proteinase nsp5
C: 3C-like proteinase nsp5
D: 3C-like proteinase nsp5
E: 3C-like proteinase nsp5
F: 3C-like proteinase nsp5
G: 3C-like proteinase nsp5
hetero molecules


Theoretical massNumber of molelcules
Total (without water)239,69334
Polymers236,6047
Non-polymers3,08927
Water25,1311395
1
A: 3C-like proteinase nsp5
B: 3C-like proteinase nsp5
hetero molecules


Theoretical massNumber of molelcules
Total (without water)69,03013
Polymers67,6012
Non-polymers1,42911
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3880 Å2
ΔGint1 kcal/mol
Surface area27300 Å2
MethodPISA
2
C: 3C-like proteinase nsp5
D: 3C-like proteinase nsp5
hetero molecules


Theoretical massNumber of molelcules
Total (without water)68,53110
Polymers67,6012
Non-polymers9308
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3590 Å2
ΔGint3 kcal/mol
Surface area27920 Å2
MethodPISA
3
E: 3C-like proteinase nsp5
hetero molecules

E: 3C-like proteinase nsp5
hetero molecules


Theoretical massNumber of molelcules
Total (without water)67,8454
Polymers67,6012
Non-polymers2442
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_556-x,y,-z+11
Buried area2970 Å2
ΔGint-2 kcal/mol
Surface area26950 Å2
MethodPISA
4
F: 3C-like proteinase nsp5
G: 3C-like proteinase nsp5
hetero molecules


Theoretical massNumber of molelcules
Total (without water)68,2109
Polymers67,6012
Non-polymers6097
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3190 Å2
ΔGint0 kcal/mol
Surface area27390 Å2
MethodPISA
Unit cell
Length a, b, c (Å)105.944, 216.821, 121.255
Angle α, β, γ (deg.)90.000, 94.010, 90.000
Int Tables number5
Space group name H-MC121
Components on special symmetry positions
IDModelComponents
11B-401-

NA

21D-660-

HOH

31D-679-

HOH

41E-664-

HOH

51F-634-

HOH

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Components

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Protein , 1 types, 7 molecules ABCDEFG

#1: Protein
3C-like proteinase nsp5 / 3CL-PRO / 3CLp / Main protease / Mpro / Non-structural protein 5 / nsp5 / SARS coronavirus main proteinase


Mass: 33800.516 Da / Num. of mol.: 7 / Mutation: C145A
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Severe acute respiratory syndrome coronavirus 2
Gene: rep, 1a-1b / Production host: Escherichia coli (E. coli)
References: UniProt: P0DTD1, SARS coronavirus main proteinase

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Non-polymers , 5 types, 1422 molecules

#2: Chemical
ChemComp-PEG / DI(HYDROXYETHYL)ETHER / Diethylene glycol


Mass: 106.120 Da / Num. of mol.: 10 / Source method: obtained synthetically / Formula: C4H10O3
#3: Chemical
ChemComp-TRS / 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL / TRIS BUFFER / Tris


Mass: 122.143 Da / Num. of mol.: 10 / Source method: obtained synthetically / Formula: C4H12NO3 / Comment: pH buffer*YM
#4: Chemical ChemComp-1PE / PENTAETHYLENE GLYCOL / PEG400 / Polyethylene glycol


Mass: 238.278 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C10H22O6 / Comment: precipitant*YM
#5: Chemical
ChemComp-NA / SODIUM ION


Mass: 22.990 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Na
#6: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 1395 / Source method: isolated from a natural source / Formula: H2O

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Details

Has ligand of interestN

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 2.94 Å3/Da / Density % sol: 58.1 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / Details: 0.1M Na citrate (pH 5.6), 16% PEG 2K

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: ALS / Beamline: 5.0.1 / Wavelength: 0.9774 Å
DetectorType: DECTRIS PILATUS3 2M / Detector: PIXEL / Date: Jun 21, 2021
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9774 Å / Relative weight: 1
ReflectionResolution: 1.98→47.5 Å / Num. obs: 188635 / % possible obs: 100 % / Redundancy: 6.1 % / Biso Wilson estimate: 32.95 Å2 / CC1/2: 0.998 / Rmerge(I) obs: 0.134 / Rpim(I) all: 0.059 / Rrim(I) all: 0.147 / Net I/σ(I): 10.7 / Num. measured all: 1157133 / Scaling rejects: 45
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsNum. measured allNum. unique obsCC1/2Rpim(I) allRrim(I) allNet I/σ(I) obs% possible all
1.98-2.015.82.0265389493170.3060.9192.2290.9100
10.84-47.55.90.0236859116810.010.02557.198.6

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Processing

Software
NameVersionClassification
PHENIX1.20.1_4487refinement
Aimless0.7.7data scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 7JOY

7joy


Resolution: 1.98→47.5 Å / SU ML: 0.27 / Cross valid method: THROUGHOUT / σ(F): 1.34 / Phase error: 24.29 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2233 9527 5.05 %
Rwork0.1768 179008 -
obs0.1792 188535 99.91 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 148.2 Å2 / Biso mean: 46.0788 Å2 / Biso min: 18.12 Å2
Refinement stepCycle: final / Resolution: 1.98→47.5 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms16473 0 187 1395 18055
Biso mean--63.46 45.3 -
Num. residues----2136
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 30

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
1.98-20.36763340.318859126246100
2-2.030.35423320.296959426274100
2.03-2.050.33023080.287459466254100
2.05-2.080.31143220.282159566278100
2.08-2.10.30062800.268159766256100
2.1-2.130.33533700.271959186288100
2.13-2.160.30933230.252459676290100
2.16-2.20.31613160.247159576273100
2.2-2.230.28262980.241959616259100
2.23-2.270.3663340.29115887622199
2.27-2.310.26283650.224559686333100
2.31-2.350.27293120.215659616273100
2.35-2.390.28273360.223458786214100
2.39-2.440.28523380.217359646302100
2.44-2.490.283160.202859556271100
2.49-2.550.26563360.201659796315100
2.55-2.620.24432990.194859706269100
2.62-2.690.2773410.196159476288100
2.69-2.770.24023250.188159706295100
2.77-2.860.22793080.182959806288100
2.86-2.960.23642990.177560056304100
2.96-3.080.22983130.170659466259100
3.08-3.220.23553330.175759776310100
3.22-3.390.22653030.162759976300100
3.39-3.60.20952590.159659956254100
3.6-3.880.17843210.141260286349100
3.88-4.260.15442250.126960606285100
4.26-4.880.15133280.120559736301100
4.88-6.150.17073150.144360076322100
6.15-47.50.16823380.152660266364100
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL11 (°2)L12 (°2)L13 (°2)L22 (°2)L23 (°2)L33 (°2)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T11 (Å2)T12 (Å2)T13 (Å2)T22 (Å2)T23 (Å2)T33 (Å2)Origin x (Å)Origin y (Å)Origin z (Å)
11.5163-0.32450.38742.0678-0.13941.1557-0.0115-0.0163-0.1313-0.004-0.00580.0620.0103-0.07270.0190.16590.01210.02360.2125-0.01880.188622.872956.914827.7739
21.44431.29690.05292.3518-1.8133.2591-0.0171-0.3290.36090.6101-0.1465-0.0245-0.7171-0.1710.14140.58960.0931-0.05040.3548-0.09270.453426.563289.569534.2767
31.72290.2311-1.21441.3808-2.01574.7764-0.0049-0.02020.0212-0.1395-0.027-0.01190.12480.13480.04020.2160.0088-0.0060.1996-0.03930.193717.877374.88344.5907
43.1562-0.1463-0.47435.72940.14333.17590.00820.3420.184-0.35720.0421-0.2825-0.14970.2476-0.05140.3192-0.02440.00880.28560.00890.151719.588980.6059-7.675
54.6714-0.1225-0.44360.2576-0.25552.85960.031-0.1462-0.07930.00490.02180.07560.1793-0.0771-0.05060.3021-0.0029-0.01460.1566-0.00910.214811.571376.837810.9407
62.16751.384-1.36483.5773-2.84883.53790.2068-0.1160.3840.21930.07740.341-0.3088-0.1171-0.26780.25810.0284-0.0090.2179-0.04850.27085.892683.07612.9008
74.5551-0.6083-0.93273.2971-2.66014.56890.2856-0.52950.13050.6370.30462.1076-0.2481-0.4973-0.53860.66120.05050.170.57410.00430.8934-10.418978.946628.7907
82.2893-0.4140.37935.4745-2.49391.80420.181-0.56730.32080.5711-0.3183-0.2899-0.54570.16590.14950.413-0.05380.02190.5216-0.0990.40492.357171.642131.6788
90.7790.20560.46291.52320.76812.82440.03630.019-0.1192-0.04610.0092-0.00680.1665-0.0593-0.04610.16380.01610.00360.33150.00350.274-4.38740.349347.9586
102.22770.4012-0.35373.6183-1.57785.1612-0.04070.3302-0.3267-0.4885-0.075-0.17650.50770.18070.11240.2758-0.00440.01940.388-0.10040.3529-2.788734.751235.6187
111.3764-0.5838-0.32271.3503-0.08123.09860.0457-0.0374-0.00310.00710.00280.1436-0.2596-0.162-0.03390.1626-0.01090.02680.3312-0.01080.2448-10.037452.100148.1059
122.327-0.2554-1.61752.02140.37182.97780.63040.84680.46780.3228-0.30550.5258-1.9094-2.312-0.14781.32320.5060.23411.45890.05620.555-23.03371.374556.2002
134.50810.5735-1.35733.2538-3.2575.86320.36940.8550.6413-0.2155-0.00560.1545-2.481-2.3464-0.78821.13560.42360.24881.10630.05350.5349-24.548370.241162.3033
143.06291.7728-3.39271.8365-3.62137.1783-0.0645-0.0433-0.0417-0.1837-0.4153-0.2954-0.51751.4380.5010.4389-0.03980.0450.57090.02360.405-15.804860.459666.9039
151.255-0.1762-0.03992.50410.4142.06050.06220.1846-0.1526-0.26220.1395-0.82970.01580.363-0.16730.3205-0.01040.10520.2813-0.07930.583934.5491108.7296.5277
161.4311-1.36860.92717.8241-0.16723.6927-0.1027-0.2599-0.18291.45610.3408-0.40340.68610.0682-0.22870.65020.0067-0.04310.3309-0.05320.444827.0359125.58634.2357
172.48840.0464-0.87131.2544-0.2081.42860.04860.32480.0634-0.2364-0.0695-0.1369-0.07280.05840.00720.2462-0.01520.01580.24520.02490.206124.2721163.47525.3043
185.4383-1.63920.0082.535-1.55762.5740.0227-0.00580.05520.2201-0.02110.0891-0.2401-0.001-0.02610.242-0.03510.03870.2168-0.02090.215517.201157.674635.9928
191.5226-0.2026-0.85451.08730.12132.6071-0.2151-0.261-0.16280.22240.09950.08860.37360.1540.12370.2790.02980.03140.28420.03620.26719.4206148.288545.8362
203.8685-3.5272-2.9184.31512.98114.3532-0.2307-0.327-0.2194-0.07140.1766-0.04590.40110.5060.04320.3738-0.00810.04090.36270.04290.259612.3553150.030657.7563
212.3488-1.2294-0.43162.36080.91031.6304-0.08550.09270.1390.00090.0068-0.1403-0.16550.11130.05850.1898-0.0317-0.01810.19040.01710.18850.0566174.509540.6846
223.1792-0.0852-1.44982.3705-0.25823.90660.0109-0.17220.48140.2013-0.0465-0.0563-0.4914-0.0154-0.00110.31710.0309-0.07840.2031-0.01220.3235-7.3846184.792845.6314
233.21090.570.36463.07650.59440.9324-0.03080.0993-0.0689-0.06880.0544-0.08680.05860.0817-0.0180.19560.00980.02480.19590.01430.1487-2.5583165.609739.3419
240.586-0.3008-0.42771.72131.84952.5722-0.108-0.093-0.09290.2861-0.0670.05030.22810.00920.18830.22220.0120.01840.24460.00820.2344-9.0579160.571342.2016
254.1468-0.0496-1.4842.3694-0.07082.8443-0.14960.0752-0.36470.24360.02010.24930.4853-0.23530.1110.3468-0.02370.04670.2199-0.0390.3241-11.3128140.913630.241
264.245-0.9126-1.82520.83641.18132.3317-0.1305-0.329-0.30370.36220.1125-0.02970.38890.2460.03360.39380.032-0.01060.2460.03150.3268-1.4422141.78632.199
271.51840.039-0.43952.1052-0.48121.8246-0.11340.30880.1023-0.17080.06690.01410.0016-0.17750.03470.2735-0.04840.01110.23190.01470.221914.3965136.69484.0464
284.51.28151.30163.6640.43955.5557-0.1343-0.4771-0.33990.33350.1331.3350.3319-0.35430.02270.5581-0.00970.2330.32110.00580.7393-1.3215110.051520.4886
294.4694-4.5739-2.27318.72622.61151.39850.1342-0.3211-0.27460.0930.04570.833-0.23770.0927-0.1430.5045-0.07970.07650.31670.01260.47064.5946107.840316.1093
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'C' and (resid 1 through 200 )C1 - 200
2X-RAY DIFFRACTION2chain 'C' and (resid 201 through 306 )C201 - 306
3X-RAY DIFFRACTION3chain 'D' and (resid 1 through 43 )D1 - 43
4X-RAY DIFFRACTION4chain 'D' and (resid 44 through 100 )D44 - 100
5X-RAY DIFFRACTION5chain 'D' and (resid 101 through 155 )D101 - 155
6X-RAY DIFFRACTION6chain 'D' and (resid 156 through 214 )D156 - 214
7X-RAY DIFFRACTION7chain 'D' and (resid 215 through 274 )D215 - 274
8X-RAY DIFFRACTION8chain 'D' and (resid 275 through 306 )D275 - 306
9X-RAY DIFFRACTION9chain 'E' and (resid 1 through 43 )E1 - 43
10X-RAY DIFFRACTION10chain 'E' and (resid 44 through 100 )E44 - 100
11X-RAY DIFFRACTION11chain 'E' and (resid 101 through 214 )E101 - 214
12X-RAY DIFFRACTION12chain 'E' and (resid 215 through 250 )E215 - 250
13X-RAY DIFFRACTION13chain 'E' and (resid 251 through 273 )E251 - 273
14X-RAY DIFFRACTION14chain 'E' and (resid 274 through 306 )E274 - 306
15X-RAY DIFFRACTION15chain 'G' and (resid 1 through 200 )G1 - 200
16X-RAY DIFFRACTION16chain 'G' and (resid 201 through 306 )G201 - 306
17X-RAY DIFFRACTION17chain 'A' and (resid 1 through 120 )A1 - 120
18X-RAY DIFFRACTION18chain 'A' and (resid 121 through 155 )A121 - 155
19X-RAY DIFFRACTION19chain 'A' and (resid 156 through 236 )A156 - 236
20X-RAY DIFFRACTION20chain 'A' and (resid 237 through 306 )A237 - 306
21X-RAY DIFFRACTION21chain 'B' and (resid 1 through 43 )B1 - 43
22X-RAY DIFFRACTION22chain 'B' and (resid 44 through 100 )B44 - 100
23X-RAY DIFFRACTION23chain 'B' and (resid 101 through 155 )B101 - 155
24X-RAY DIFFRACTION24chain 'B' and (resid 156 through 213 )B156 - 213
25X-RAY DIFFRACTION25chain 'B' and (resid 214 through 260 )B214 - 260
26X-RAY DIFFRACTION26chain 'B' and (resid 261 through 306 )B261 - 306
27X-RAY DIFFRACTION27chain 'F' and (resid 1 through 200 )F1 - 200
28X-RAY DIFFRACTION28chain 'F' and (resid 201 through 243 )F201 - 243
29X-RAY DIFFRACTION29chain 'F' and (resid 244 through 306 )F244 - 306

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