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- PDB-7kf4: Crystal structure from SARS-CoV-2 NendoU NSP15 -

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Basic information

Entry
Database: PDB / ID: 7kf4
TitleCrystal structure from SARS-CoV-2 NendoU NSP15
ComponentsUridylate-specific endoribonuclease
KeywordsVIRAL PROTEIN / HYDROLASE / NSP15 / NendoU / covid-19 / covid / sars / sars-cov-2 / endoribonuclease
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
CITRIC ACID / Replicase polyprotein 1ab
Similarity search - Component
Biological speciesSevere acute respiratory syndrome coronavirus 2
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.61 Å
AuthorsGodoy, A.S. / Nakamura, A.M. / Pereira, H.M. / Noske, G.D. / Gawriljuk, V.O. / Fernandes, R.S. / Oliveira, K.I.Z. / Oliva, G.
Funding support Brazil, 1items
OrganizationGrant numberCountry
Sao Paulo Research Foundation (FAPESP)2013/07600-3 Brazil
CitationJournal: Nucleic Acids Res / Year: 2023
Title: Allosteric regulation and crystallographic fragment screening of SARS-CoV-2 NSP15 endoribonuclease.
Authors: Andre Schutzer Godoy / Aline Minalli Nakamura / Alice Douangamath / Yun Song / Gabriela Dias Noske / Victor Oliveira Gawriljuk / Rafaela Sachetto Fernandes / Humberto D Muniz Pereira / ...Authors: Andre Schutzer Godoy / Aline Minalli Nakamura / Alice Douangamath / Yun Song / Gabriela Dias Noske / Victor Oliveira Gawriljuk / Rafaela Sachetto Fernandes / Humberto D Muniz Pereira / Ketllyn Irene Zagato Oliveira / Daren Fearon / Alexandre Dias / Tobias Krojer / Michael Fairhead / Alisa Powell / Louise Dunnet / Jose Brandao-Neto / Rachael Skyner / Rod Chalk / Dávid Bajusz / Miklós Bege / Anikó Borbás / György Miklós Keserű / Frank von Delft / Glaucius Oliva /
Abstract: Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is the causative agent of coronavirus disease 2019 (COVID-19). The NSP15 endoribonuclease enzyme, known as NendoU, is highly conserved and ...Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is the causative agent of coronavirus disease 2019 (COVID-19). The NSP15 endoribonuclease enzyme, known as NendoU, is highly conserved and plays a critical role in the ability of the virus to evade the immune system. NendoU is a promising target for the development of new antiviral drugs. However, the complexity of the enzyme's structure and kinetics, along with the broad range of recognition sequences and lack of structural complexes, hampers the development of inhibitors. Here, we performed enzymatic characterization of NendoU in its monomeric and hexameric form, showing that hexamers are allosteric enzymes with a positive cooperative index, and with no influence of manganese on enzymatic activity. Through combining cryo-electron microscopy at different pHs, X-ray crystallography and biochemical and structural analysis, we showed that NendoU can shift between open and closed forms, which probably correspond to active and inactive states, respectively. We also explored the possibility of NendoU assembling into larger supramolecular structures and proposed a mechanism for allosteric regulation. In addition, we conducted a large fragment screening campaign against NendoU and identified several new allosteric sites that could be targeted for the development of new inhibitors. Overall, our findings provide insights into the complex structure and function of NendoU and offer new opportunities for the development of inhibitors.
History
DepositionOct 13, 2020Deposition site: RCSB / Processing site: RCSB
Revision 1.0Dec 2, 2020Provider: repository / Type: Initial release
Revision 1.1May 10, 2023Group: Database references / Category: citation / citation_author / database_2
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _database_2.pdbx_DOI / _database_2.pdbx_database_accession
Revision 1.2Oct 25, 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: Uridylate-specific endoribonuclease
B: Uridylate-specific endoribonuclease
C: Uridylate-specific endoribonuclease
D: Uridylate-specific endoribonuclease
E: Uridylate-specific endoribonuclease
F: Uridylate-specific endoribonuclease
hetero molecules


Theoretical massNumber of molelcules
Total (without water)235,82812
Polymers234,6756
Non-polymers1,1536
Water7,728429
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: native gel electrophoresis
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area20690 Å2
ΔGint-104 kcal/mol
Surface area84910 Å2
MethodPISA
Unit cell
Length a, b, c (Å)85.125, 151.163, 199.242
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number18
Space group name H-MP22121

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Components

#1: Protein
Uridylate-specific endoribonuclease / NSP15 / NendoU


Mass: 39112.535 Da / Num. of mol.: 6
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, Hydrolases; Acting on ester bonds
#2: Chemical
ChemComp-CIT / CITRIC ACID / Citric acid


Mass: 192.124 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C6H8O7
#3: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 429 / Source method: isolated from a natural source / Formula: H2O
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: 2.74 Å3/Da / Density % sol: 55.05 %
Crystal growTemperature: 293 K / Method: vapor diffusion / pH: 5 / Details: 0.1 M trisodium citrate pH 5, 14 % w/v PEG6000

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: MAX IV / Beamline: BioMAX / Wavelength: 0.976254 Å
DetectorType: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Jun 13, 2020
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.976254 Å / Relative weight: 1
ReflectionResolution: 2.61→49.16 Å / Num. obs: 78886 / % possible obs: 99.73 % / Redundancy: 13.8 % / CC1/2: 0.998 / Net I/σ(I): 8.24
Reflection shellResolution: 2.61→2.703 Å / Num. unique obs: 7756 / CC1/2: 0.527

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Processing

Software
NameVersionClassification
BUSTER2.10.3refinement
PDB_EXTRACT3.25data extraction
XDSdata reduction
Aimlessdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 6x1b

6x1b


Resolution: 2.61→49.16 Å / Cor.coef. Fo:Fc: 0.926 / Cor.coef. Fo:Fc free: 0.915 / Rfactor Rfree error: 0 / SU R Cruickshank DPI: 0.717 / Cross valid method: THROUGHOUT / σ(F): 0 / SU R Blow DPI: 0.712 / SU Rfree Blow DPI: 0.293 / SU Rfree Cruickshank DPI: 0.298
RfactorNum. reflection% reflectionSelection details
Rfree0.246 4004 5.09 %RANDOM
Rwork0.219 ---
obs0.22 78707 99.8 %-
Displacement parametersBiso max: 282.46 Å2 / Biso mean: 74.07 Å2 / Biso min: 25.11 Å2
Baniso -1Baniso -2Baniso -3
1--27.3512 Å20 Å20 Å2
2--17.6677 Å20 Å2
3---9.6835 Å2
Refine analyzeLuzzati coordinate error obs: 0.44 Å
Refinement stepCycle: final / Resolution: 2.61→49.16 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms16447 0 78 429 16954
Biso mean--108.38 57.7 -
Num. residues----2088
Refine LS restraints
Refine-IDTypeNumberRestraint functionWeightDev ideal
X-RAY DIFFRACTIONt_dihedral_angle_d5856SINUSOIDAL2
X-RAY DIFFRACTIONt_trig_c_planes469HARMONIC2
X-RAY DIFFRACTIONt_gen_planes2412HARMONIC5
X-RAY DIFFRACTIONt_it16897HARMONIC20
X-RAY DIFFRACTIONt_nbd
X-RAY DIFFRACTIONt_improper_torsion
X-RAY DIFFRACTIONt_pseud_angle
X-RAY DIFFRACTIONt_chiral_improper_torsion2226SEMIHARMONIC5
X-RAY DIFFRACTIONt_sum_occupancies
X-RAY DIFFRACTIONt_utility_distance
X-RAY DIFFRACTIONt_utility_angle
X-RAY DIFFRACTIONt_utility_torsion
X-RAY DIFFRACTIONt_ideal_dist_contact19009SEMIHARMONIC4
X-RAY DIFFRACTIONt_bond_d16897HARMONIC20.01
X-RAY DIFFRACTIONt_angle_deg22946HARMONIC21.11
X-RAY DIFFRACTIONt_omega_torsion3.3
X-RAY DIFFRACTIONt_other_torsion19.7
LS refinement shellResolution: 2.61→2.68 Å / Rfactor Rfree error: 0 / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.303 298 5.21 %
Rwork0.266 5423 -
all0.268 5721 -
obs--99.69 %
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)
10.00070.49360.04570.00041.42350.00260.1213-0.1053-0.1407-0.0469-0.1399-0.07490.3616-0.09280.01860.3273-0.04880.01040.2980.01170.3666.819746.625835.4651
20.1308-0.16591.06751.70941.23412.1755-0.04250.04780.22620.05210.0261-0.0676-0.0712-0.18380.01640.27930.0096-0.02810.2412-0.01980.392715.944767.90426.9555
31.4538-1.1410.48171.0101-0.38590.79650.30990.31320.1801-0.3723-0.3235-0.2990.28880.20420.01360.59720.13370.17570.49340.16480.423737.368457.64768.4215
40.0416-0.612-1.48990.24710.77760.63220.04460.2520.1614-0.1344-0.0326-0.25050.10610.113-0.01190.43540.08060.0970.45420.08410.583342.336561.878816.2166
52.01761.93951.94342.21922.34172.2385-1.1757-0.633.1517-4.4371-1.99970.8413-5.4473-3.48263.17540.50710.07720.75491.0198-0.33741.071745.655461.470726.3093
60.58450.4495-0.60671.0639-2.130200.08140.0129-0.0558-0.0547-0.1445-0.00330.2322-0.05830.06310.36380.02940.05110.3621-0.0110.387836.684546.571255.3226
70.22020.60260.55242.1698-1.26782.0557-0.01810.00520.08260.1070.01310.1621-0.06750.07280.0050.36170.005-0.06470.2582-0.02440.437227.551467.939863.7281
81.31530.5401-0.48770.511-1.09190.28920.1029-0.19740.04880.3082-0.06320.14560.0985-0.0922-0.03970.5496-0.06230.02260.4364-0.04770.39176.470857.409680.6584
90.06461.124-0.23690.04010.28980.34980.0078-0.10640.05490.13340.0784-0.07620.0522-0.1231-0.08630.4247-0.02990.08190.4073-0.06790.5297-0.20262.560575.6244
101.99631.98221.99872.01311.95412.028-0.4983-0.03490.46831.0826-0.3542-1.2449-1.3725-0.22990.85260.64170.33370.06311.15030.20050.8712-2.61261.764263.49
110.0039-0.16760.4381.0814-0.5060-0.17730.08370.05420.01380.1431-0.0480.0393-0.06410.03420.6885-0.02580.03360.39140.04120.37423.555320.797337.0657
120.54841.0421-0.8840.01370.37641.5460.02630.0048-0.1481-0.0329-0.02420.06190.08090.0031-0.00220.7584-0.04740.01870.2232-0.00070.44671.989917.145725.6717
130.2376-0.34110.0430.7073-0.12870.35130.09110.0924-0.01040.034-0.0910.01040.2097-0.0253-0.00010.6081-0.1105-0.0690.4819-0.01390.3516-0.487740.61618.5154
149.0345-8.8894-5.87249.14517.28829.6051-0.21680.0557-0.7543-0.04790.1524-0.2024-0.007-0.44440.06430.71830.24560.11720.81630.03991.1155-7.79846.484422.3961
150.0104-0.0340.24230.3907-0.56810.5484-0.207-0.09020.0191-0.01380.13840.16430.155-0.03470.06860.66550.00310.04970.42180.00170.466420.084120.730453.6662
160.4551-0.7303-0.16980.0627-0.14761.6992-0.1274-0.0506-0.253-0.08360.125-0.108-0.1162-0.01150.00240.42670.01210.15580.28020.02810.405541.515717.161965.1775
170-0.8932-0.39252.25390.80860-0.1813-0.11390.00650.14660.1696-0.1172-0.0880.16840.01170.55790.1614-0.05540.5076-0.04730.35940.104639.071183.6929
180.4346-0.2938-0.90060.0010.41510.4198-0.0158-0.08430.1461-0.02970.011-0.13140.1187-0.12470.00480.48060.1463-0.00530.4759-0.05780.453948.723942.531680.4701
192.0679-3.38672.11582.0372-2.73392.11460.9532-1.55461.4-0.6349-0.824-2.18860.4084-3.5272-0.12921.21540.05510.08010.9758-0.24690.531349.444145.305869.5477
200-0.4432-0.45060.4834-0.02760.46130.0044-0.01110.1177-0.0405-0.0143-0.1079-0.1293-0.01790.00990.3648-0.02030.02620.40970.03680.41444.587751.561652.2398
210.3891-0.1125-0.79910.3546-0.76960.9757-0.0019-0.0395-0.0017-0.17570.023-0.03090.359-0.0985-0.02110.4343-0.1514-0.0140.35970.01060.3356-6.13232.258358.9963
220.08860.06721.35760.0106-0.4470.0097-0.0487-0.51320.4194-0.1751-0.0150.25460.2892-0.24180.06370.6812-0.16940.03020.49330.0140.5306-4.966220.95970.9219
231.8724-0.23260.20530.69510.34550.6671-0.0825-0.202-0.1496-0.0220.06170.00960.31630.20480.02080.505-0.01670.0670.46260.030.379911.259717.806583.5372
2400.6570.29580.05630.77390.00020.06-0.12260.0122-0.2504-0.01740.00440.2166-0.0488-0.04260.5325-0.07080.05880.5062-0.00090.48327.541112.453676.2867
250.40630.36340.30780.57240.14960.10620.10880.2008-0.2696-0.1616-0.1719-0.17870.0454-0.07730.06310.6845-0.07130.02930.51430.010.5317.14164.079475.831
261.99341.99732.00181.99742.00411.99130.8149-2.1481-0.84383.71860.8111-2.99834.74322.649-1.6260.88270.49440.05880.77160.62681.343910.99459.240165.8591
270.8066-0.5611-0.79880.1063-0.64841.1705-0.02940.11110.00320.1950.02040.00720.20440.05860.0090.33560.03720.06110.35590.06350.426237.373848.276938.3603
280.7146-1.2890.03590.60520.66470.06130.1095-0.0065-0.0161-0.2003-0.0731-0.11050.39020.0632-0.03640.50530.16770.14480.33760.10330.329152.715330.610130.6557
291.2717-1.20010.3470.096-0.15870.00720.24660.3227-0.229-0.1393-0.21730.04890.83220.1183-0.02921.10660.26410.15110.58660.04770.404236.055316.896211.8043
300.85550.06451.34060.2073-0.16950.3860.1318-0.6054-0.7099-0.2475-0.0521-0.25021.7887-0.2589-0.07971.2765-0.0202-0.07430.64-0.08350.625136.84274.613715.1956
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1{ B|0 - B|60 }B0 - 60
2X-RAY DIFFRACTION2{ B|61 - B|183 }B61 - 183
3X-RAY DIFFRACTION3{ B|184 - B|267 }B184 - 267
4X-RAY DIFFRACTION4{ B|268 - B|345 }B268 - 345
5X-RAY DIFFRACTION5{ B|346 - B|346 }B346
6X-RAY DIFFRACTION6{ A|0 - A|60 }A0 - 60
7X-RAY DIFFRACTION7{ A|61 - A|183 }A61 - 183
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10X-RAY DIFFRACTION10{ A|346 - A|346 }A346
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12X-RAY DIFFRACTION12{ C|61 - C|183 }C61 - 183
13X-RAY DIFFRACTION13{ C|184 - C|345 }C184 - 345
14X-RAY DIFFRACTION14{ C|346 - C|346 }C346
15X-RAY DIFFRACTION15{ D|0 - D|60 }D0 - 60
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17X-RAY DIFFRACTION17{ D|184 - D|276 }D184 - 276
18X-RAY DIFFRACTION18{ D|277 - D|345 }D277 - 345
19X-RAY DIFFRACTION19{ D|346 - D|346 }D346
20X-RAY DIFFRACTION20{ E|0 - E|38 }E0 - 38
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22X-RAY DIFFRACTION22{ E|184 - E|203 }E184 - 203
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24X-RAY DIFFRACTION24{ E|277 - E|325 }E277 - 325
25X-RAY DIFFRACTION25{ E|326 - E|345 }E326 - 345
26X-RAY DIFFRACTION26{ E|346 - E|346 }E346
27X-RAY DIFFRACTION27{ F|0 - F|60 }F0 - 60
28X-RAY DIFFRACTION28{ F|61 - F|183 }F61 - 183
29X-RAY DIFFRACTION29{ F|184 - F|325 }F184 - 325
30X-RAY DIFFRACTION30{ F|326 - F|345 }F326 - 345

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