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- PDB-7nfv: Structure of SARS-CoV-2 Papain-like protease PLpro -

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Basic information

Entry
Database: PDB / ID: 7nfv
TitleStructure of SARS-CoV-2 Papain-like protease PLpro
ComponentsPapain-like protease nsp3
KeywordsHYDROLASE / Papain-like protease SARS-CoV-2 Hydrolase Zinc binding protein
Function / homology
Function and homology information


viral genome replication / methyltransferase activity / protein guanylyltransferase activity / RNA endonuclease activity producing 3'-phosphomonoesters, hydrolytic mechanism / mRNA guanylyltransferase activity / 5'-3' RNA helicase activity / Lyases; Phosphorus-oxygen lyases / Assembly of the SARS-CoV-2 Replication-Transcription Complex (RTC) / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of TBK1 activity / Maturation of replicase proteins ...viral genome replication / methyltransferase activity / protein guanylyltransferase activity / RNA endonuclease activity producing 3'-phosphomonoesters, hydrolytic mechanism / mRNA guanylyltransferase activity / 5'-3' RNA helicase activity / Lyases; Phosphorus-oxygen lyases / Assembly of the SARS-CoV-2 Replication-Transcription Complex (RTC) / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of TBK1 activity / Maturation of replicase proteins / TRAF3-dependent IRF activation pathway / ISG15-specific peptidase activity / Transcription of SARS-CoV-2 sgRNAs / Translation of Replicase and Assembly of the Replication Transcription Complex / snRNP Assembly / Replication of the SARS-CoV-2 genome / Hydrolases; Acting on ester bonds; Exoribonucleases producing 5'-phosphomonoesters / host cell endoplasmic reticulum-Golgi intermediate compartment / double membrane vesicle viral factory outer membrane / SARS coronavirus main proteinase / 5'-3' DNA helicase activity / 3'-5'-RNA exonuclease activity / endonuclease activity / host cell endosome / symbiont-mediated degradation of host mRNA / mRNA guanylyltransferase / symbiont-mediated suppression of host ISG15-protein conjugation / G-quadruplex RNA binding / symbiont-mediated suppression of host toll-like receptor signaling pathway / methylation / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF3 activity / omega peptidase activity / SARS-CoV-2 modulates host translation machinery / mRNA (guanine-N7)-methyltransferase / methyltransferase cap1 / host cell Golgi apparatus / symbiont-mediated suppression of host NF-kappaB cascade / symbiont-mediated perturbation of host ubiquitin-like protein modification / DNA helicase / methyltransferase cap1 activity / ubiquitinyl hydrolase 1 / cysteine-type deubiquitinase activity / mRNA 5'-cap (guanine-N7-)-methyltransferase activity / Hydrolases; Acting on peptide bonds (peptidases); Cysteine endopeptidases / single-stranded RNA binding / regulation of autophagy / host cell perinuclear region of cytoplasm / viral protein processing / lyase activity / host cell endoplasmic reticulum membrane / RNA helicase / symbiont-mediated suppression of host type I interferon-mediated signaling pathway / symbiont-mediated suppression of host gene expression / copper ion binding / viral translational frameshifting / symbiont-mediated activation of host autophagy / RNA-directed RNA polymerase / cysteine-type endopeptidase activity / viral RNA genome replication / RNA-directed RNA polymerase activity / DNA-templated transcription / lipid binding / 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 / Nonstructural protein 15, middle domain, alpha/betacoronavirus / Nonstructural protein 15, N-terminal domain, alpha/beta-coronavirus / NSP14, guanine-N7-methyltransferase domain, coronavirus / Coronavirus (CoV) guanine-N7-methyltransferase (N7-MTase) domain profile. / Coronavirus (CoV) Nsp15 N-terminal oligomerization domain profile. / NSP12 RNA-dependent RNA polymerase, coronavirus / : ...RNA-dependent RNA polymerase, SARS-CoV-like / Nonstructural protein 14, betacoronavirus / NSP15, NendoU domain, coronavirus / Nonstructural protein 15, middle domain, alpha/betacoronavirus / Nonstructural protein 15, N-terminal domain, alpha/beta-coronavirus / NSP14, guanine-N7-methyltransferase domain, coronavirus / Coronavirus (CoV) guanine-N7-methyltransferase (N7-MTase) domain profile. / Coronavirus (CoV) Nsp15 N-terminal oligomerization domain profile. / NSP12 RNA-dependent RNA polymerase, coronavirus / : / Coronavirus Nsp12 RNA-dependent RNA polymerase (RdRp) domain profile. / Coronavirus Nsp12 Interface domain profile. / : / : / Coronavirus Nonstructural protein 13, 1B domain / Coronavirus Non-structural protein 13, zinc-binding domain / Coronavirus Nonstructural protein 13, stalk domain / Nidovirus 2-O-methyltransferase / Nidovirus 2'-O-methyltransferase (2'-O-MTase) domain profile. / 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 / Nonstructural protein 13, 1B domain, coronavirus / Coronavirus replicase NSP15, middle domain / Coronavirus replicase NSP15, N-terminal oligomerisation / Nidovirus 3'-5' exoribonuclease domain / Nidovirus 3'-5' exoribonuclease (ExoN) 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 / Nonstructural protein 13, zinc-binding domain, coronavirus-like / Coronaviridae zinc-binding (CV ZBD) domain profile. / Arterivirus Nsp11 N-terminal/Coronavirus NSP15 middle domain / Arterivirus Nsp11 N-terminal/coronavirus NSP15 middle (AV-Nsp11N/CoV-Nsp15M) domain profile. / Nidoviral uridylate-specific endoribonuclease (NendoU) domain profile. / Nidovirus RdRp-associated nucleotidyl transferase (NiRAN) domain / Nidovirus RdRp-associated nucleotidyl transferase (NiRAN) domain profile. / Endoribonuclease EndoU-like / NendoU domain, nidovirus / Coronavirus replicase NSP15, uridylate-specific endoribonuclease / : / Lipocalin signature. / DNA2/NAM7 helicase-like, C-terminal / AAA domain / (+) RNA virus helicase core domain / (+)RNA virus helicase core domain profile. / 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. / 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 / NSP1, C-terminal domain, betacoronavirus / : / Betacoronavirus (BetaCoV) Nsp1 C-terminal domain profile. / Betacoronavirus Nsp3e group 2-specific marker (G2M) 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, betacoronavirus / Non-structural protein NSP3A domain-like superfamily / Non-structural protein NSP3, nucleic acid-binding domain superfamily, betacoronavirus / Non-structural protein 6, betacoronavirus / Betacoronavirus nucleic acid-binding (NAB) / Papain-like viral protease, palm and finger domains, coronavirus / Papain-like protease, N-terminal domain superfamily, coronavirus / Coronavirus replicase NSP2, N-terminal / : / Coronavirus replicase NSP2, C-terminal / Coronavirus (CoV) Nsp2 middle domain profile. / NSP1, globular domain, alpha/betacoronavirus / Coronavirus (CoV) Nsp1 globular domain profile. / Coronavirus (CoV) Nsp2 N-terminal domain profile. / Coronavirus (CoV) Nsp2 C-terminal domain profile. / Nonstructural protein 2, N-terminal domain, coronavirus / Non-structural protein 2, C-terminal domain, coronavirus / NSP3, second ubiquitin-like (Ubl) domain, coronavirus / Coronavirus Nsp3a Ubl domain profile. / Coronavirus Nsp3d Ubl domain profile. / NSP3, first ubiquitin-like (Ubl) domain, coronavirus / Peptidase family C16 domain profile. / : / : / Coronavirus replicase NSP7 / Coronavirus 3Ecto domain profile. / Coronavirus RNA-dependent RNA polymerase (RdRp) Nsp7 cofactor domain profile.
Similarity search - Domain/homology
PHOSPHATE ION / Replicase polyprotein 1a / Replicase polyprotein 1ab
Similarity search - Component
Biological speciesSevere acute respiratory syndrome coronavirus 2
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.42 Å
AuthorsSrinivasan, V. / Gunther, S. / Reinke, P. / Werner, N. / Falke, S. / Brognaro, H. / Ullah, N. / Andaleeb, H. / Perbandt, M. / Alves Franca, B. ...Srinivasan, V. / Gunther, S. / Reinke, P. / Werner, N. / Falke, S. / Brognaro, H. / Ullah, N. / Andaleeb, H. / Perbandt, M. / Alves Franca, B. / Schwinzer, M. / Wang, M. / Sprenger, J. / Lieske, J. / Ginn, H. / Lane, T.J. / Yefanov, O. / Gelisio, L. / Koua, F. / Saouane, S. / Tolstikova, A. / Groessler, M. / Fleckenstein, H. / Ewert, W. / Trost, F. / Lorenzen, K. / Schubert, R. / Han, H. / Schmidt, C. / Brings, L. / Ehrt, C. / Rarey, M. / Galchenkova, M. / Gevorkov, Y. / Li, C. / Perk, A. / Awel, S. / Hinrichs, W. / Meents, A. / Betzel, C.
Funding support Germany, European Union, 2items
OrganizationGrant numberCountry
German Research Foundation (DFG)EXC 2056 - project ID 390715994 Germany
European CommissionEU project 101003551 - EXSCALATE4CoV (E4C)European Union
CitationJournal: Commun Biol / Year: 2022
Title: Antiviral activity of natural phenolic compounds in complex at an allosteric site of SARS-CoV-2 papain-like protease.
Authors: Srinivasan, V. / Brognaro, H. / Prabhu, P.R. / de Souza, E.E. / Gunther, S. / Reinke, P.Y.A. / Lane, T.J. / Ginn, H. / Han, H. / Ewert, W. / Sprenger, J. / Koua, F.H.M. / Falke, S. / Werner, ...Authors: Srinivasan, V. / Brognaro, H. / Prabhu, P.R. / de Souza, E.E. / Gunther, S. / Reinke, P.Y.A. / Lane, T.J. / Ginn, H. / Han, H. / Ewert, W. / Sprenger, J. / Koua, F.H.M. / Falke, S. / Werner, N. / Andaleeb, H. / Ullah, N. / Franca, B.A. / Wang, M. / Barra, A.L.C. / Perbandt, M. / Schwinzer, M. / Schmidt, C. / Brings, L. / Lorenzen, K. / Schubert, R. / Machado, R.R.G. / Candido, E.D. / Oliveira, D.B.L. / Durigon, E.L. / Niebling, S. / Garcia, A.S. / Yefanov, O. / Lieske, J. / Gelisio, L. / Domaracky, M. / Middendorf, P. / Groessler, M. / Trost, F. / Galchenkova, M. / Mashhour, A.R. / Saouane, S. / Hakanpaa, J. / Wolf, M. / Alai, M.G. / Turk, D. / Pearson, A.R. / Chapman, H.N. / Hinrichs, W. / Wrenger, C. / Meents, A. / Betzel, C.
History
DepositionFeb 7, 2021Deposition site: PDBE / Processing site: PDBE
Revision 1.0Feb 24, 2021Provider: repository / Type: Initial release
Revision 1.1Mar 10, 2021Group: Database references / Source and taxonomy / Structure summary
Category: audit_author / citation_author ...audit_author / citation_author / entity / entity_name_com / entity_src_gen / struct / struct_ref / struct_ref_seq
Item: _entity.pdbx_description / _entity.pdbx_ec ..._entity.pdbx_description / _entity.pdbx_ec / _entity_name_com.name / _entity_src_gen.gene_src_common_name / _entity_src_gen.pdbx_gene_src_gene / _struct.pdbx_descriptor / _struct_ref.db_code / _struct_ref.pdbx_db_accession / _struct_ref_seq.pdbx_db_accession
Revision 1.2Sep 7, 2022Group: Database references / Derived calculations ...Database references / Derived calculations / Source and taxonomy / Structure summary
Category: atom_type / citation ...atom_type / citation / citation_author / database_2 / entity / entity_name_com / entity_src_gen
Item: _atom_type.pdbx_N_electrons / _atom_type.pdbx_scat_Z ..._atom_type.pdbx_N_electrons / _atom_type.pdbx_scat_Z / _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 / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _entity.pdbx_description / _entity.pdbx_ec / _entity_name_com.name / _entity_src_gen.gene_src_common_name
Revision 1.3Jan 31, 2024Group: 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
AAA: Papain-like protease nsp3
hetero molecules


Theoretical massNumber of molelcules
Total (without water)35,9956
Polymers35,6721
Non-polymers3235
Water9,548530
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area700 Å2
ΔGint-27 kcal/mol
Surface area15400 Å2
MethodPISA
Unit cell
Length a, b, c (Å)82.330, 82.330, 134.320
Angle α, β, γ (deg.)90.000, 90.000, 120.000
Int Tables number154
Space group name H-MP3221

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Components

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Protein , 1 types, 1 molecules AAA

#1: Protein Papain-like protease nsp3 / Non-structural protein 3 / nsp3 / PL2-PRO / Papain-like proteinase / PL-PRO


Mass: 35671.500 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Severe acute respiratory syndrome coronavirus 2
Production host: Escherichia coli BL21(DE3) (bacteria)
References: UniProt: P0DTC1, UniProt: P0DTD1*PLUS, ubiquitinyl hydrolase 1, Hydrolases; Acting on peptide bonds (peptidases); Cysteine endopeptidases

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Non-polymers , 5 types, 535 molecules

#2: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Zn / Feature type: SUBJECT OF INVESTIGATION
#3: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C3H8O3 / Feature type: SUBJECT OF INVESTIGATION
#4: Chemical ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Cl / Feature type: SUBJECT OF INVESTIGATION
#5: Chemical ChemComp-PO4 / PHOSPHATE ION


Mass: 94.971 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: PO4 / Feature type: SUBJECT OF INVESTIGATION
#6: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 530 / Source method: isolated from a natural source / Formula: H2O

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Details

Has ligand of interestY

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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: 3.68 Å3/Da / Density % sol: 66 %
Crystal growTemperature: 277 K / Method: vapor diffusion / Details: 1.0M NaH2PO4/1.0MKH2PO4 100mM Tris_HCl pH=7.5

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: PETRA III, DESY / Beamline: P11 / Wavelength: 1.0332 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Dec 19, 2020
RadiationMonochromator: M / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.0332 Å / Relative weight: 1
ReflectionResolution: 1.42→48.89 Å / Num. obs: 99793 / % possible obs: 100 % / Redundancy: 52.9 % / CC1/2: 0.97 / Net I/σ(I): 28.3
Reflection shellResolution: 1.42→1.44 Å / Num. unique obs: 4864 / CC1/2: 0.36

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Processing

Software
NameVersionClassification
REFMAC5.8.0267refinement
XDSdata reduction
XSCALEdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 7jrn

7jrn


Resolution: 1.42→48.89 Å / Cor.coef. Fo:Fc: 0.98 / Cor.coef. Fo:Fc free: 0.975 / SU B: 2.331 / SU ML: 0.038 / Cross valid method: FREE R-VALUE / ESU R: 0.044 / ESU R Free: 0.046
Details: Hydrogens have been added in their riding positions
RfactorNum. reflection% reflection
Rfree0.1714 4919 4.929 %
Rwork0.1538 94872 -
all0.155 --
obs-99791 99.989 %
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK BULK SOLVENT
Displacement parametersBiso mean: 31.543 Å2
Baniso -1Baniso -2Baniso -3
1-0.299 Å20.15 Å20 Å2
2--0.299 Å2-0 Å2
3----0.972 Å2
Refinement stepCycle: LAST / Resolution: 1.42→48.89 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2502 0 14 530 3046
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.020.0132769
X-RAY DIFFRACTIONr_bond_other_d0.0010.0172516
X-RAY DIFFRACTIONr_angle_refined_deg2.3081.6553780
X-RAY DIFFRACTIONr_angle_other_deg1.6091.585839
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.0895353
X-RAY DIFFRACTIONr_dihedral_angle_2_deg41.59924.296135
X-RAY DIFFRACTIONr_dihedral_angle_3_deg14.27115474
X-RAY DIFFRACTIONr_dihedral_angle_4_deg12.021157
X-RAY DIFFRACTIONr_chiral_restr0.1190.2360
X-RAY DIFFRACTIONr_gen_planes_refined0.0140.023252
X-RAY DIFFRACTIONr_gen_planes_other0.0020.02642
X-RAY DIFFRACTIONr_nbd_refined0.2440.2455
X-RAY DIFFRACTIONr_symmetry_nbd_other0.180.22246
X-RAY DIFFRACTIONr_nbtor_refined0.1870.21263
X-RAY DIFFRACTIONr_symmetry_nbtor_other0.0880.21324
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.2450.2395
X-RAY DIFFRACTIONr_symmetry_xyhbond_nbd_other0.0910.25
X-RAY DIFFRACTIONr_symmetry_nbd_refined0.3140.219
X-RAY DIFFRACTIONr_nbd_other0.2130.244
X-RAY DIFFRACTIONr_symmetry_xyhbond_nbd_refined0.2660.241
X-RAY DIFFRACTIONr_mcbond_it1.942.6851358
X-RAY DIFFRACTIONr_mcbond_other1.9392.6831357
X-RAY DIFFRACTIONr_mcangle_it2.6074.0221729
X-RAY DIFFRACTIONr_mcangle_other2.6064.0251730
X-RAY DIFFRACTIONr_scbond_it3.8923.0791409
X-RAY DIFFRACTIONr_scbond_other3.893.081406
X-RAY DIFFRACTIONr_scangle_it5.6364.4632051
X-RAY DIFFRACTIONr_scangle_other5.6314.4632046
X-RAY DIFFRACTIONr_lrange_it7.26134.0583228
X-RAY DIFFRACTIONr_lrange_other6.90731.9473028
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.42-1.4570.3513660.3346893X-RAY DIFFRACTION99.9725
1.457-1.4970.2853460.2776812X-RAY DIFFRACTION99.9581
1.497-1.540.2583350.2536556X-RAY DIFFRACTION100
1.54-1.5880.2433380.2236412X-RAY DIFFRACTION99.9852
1.588-1.640.2153530.2046169X-RAY DIFFRACTION99.9693
1.64-1.6970.2093050.186009X-RAY DIFFRACTION100
1.697-1.7610.1893330.1695752X-RAY DIFFRACTION100
1.761-1.8330.1953030.1615624X-RAY DIFFRACTION100
1.833-1.9140.1733090.155335X-RAY DIFFRACTION100
1.914-2.0080.1492790.1415125X-RAY DIFFRACTION100
2.008-2.1160.1622490.1434892X-RAY DIFFRACTION100
2.116-2.2450.1582370.1414649X-RAY DIFFRACTION100
2.245-2.3990.1732000.1414386X-RAY DIFFRACTION100
2.399-2.5910.1552150.1374093X-RAY DIFFRACTION100
2.591-2.8380.1681780.1423804X-RAY DIFFRACTION100
2.838-3.1730.1671560.1583429X-RAY DIFFRACTION100
3.173-3.6620.1521520.1483053X-RAY DIFFRACTION100
3.662-4.4820.1411120.122616X-RAY DIFFRACTION100
4.482-6.3270.159930.1562061X-RAY DIFFRACTION100
6.327-70.235600.1921202X-RAY DIFFRACTION99.7628
Refinement TLS params.Method: refined / Origin x: 36.9797 Å / Origin y: 9.5722 Å / Origin z: 16.052 Å
111213212223313233
T0.0222 Å2-0.0072 Å20.0026 Å2-0.0263 Å20.0023 Å2--0.0047 Å2
L0.1039 °2-0.0375 °2-0.0352 °2-0.1466 °20.1024 °2--0.1079 °2
S0.0058 Å °0.004 Å °0.0181 Å °-0.0133 Å °-0.0117 Å °0.0033 Å °0.0095 Å °0.0042 Å °0.0058 Å °
Refinement TLS group
IDRefine-IDRefine TLS-IDSelectionAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1ALLAAA1 - 315
2X-RAY DIFFRACTION1ALLAAA401
3X-RAY DIFFRACTION1ALLAAA402
4X-RAY DIFFRACTION1ALLAAA403
5X-RAY DIFFRACTION1ALLAAA404

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