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- PDB-5w8u: Crystal structure of MERS-CoV papain-like protease in complex wit... -

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Basic information

Entry
Database: PDB / ID: 5w8u
TitleCrystal structure of MERS-CoV papain-like protease in complex with the C-terminal domain of human ISG15
Components
  • ORF1ab
  • Ubiquitin-like protein ISG15
KeywordsSIGNALING PROTEIN / Hydrolase / papain-like protease / ISG15
Function / homology
Function and homology information


positive regulation of protein oligomerization / ISG15-protein conjugation / mRNA capping enzyme complex / regulation of type II interferon production / protein localization to mitochondrion / NS1 Mediated Effects on Host Pathways / response to type I interferon / Modulation of host responses by IFN-stimulated genes / negative regulation of type I interferon-mediated signaling pathway / negative regulation of viral genome replication ...positive regulation of protein oligomerization / ISG15-protein conjugation / mRNA capping enzyme complex / regulation of type II interferon production / protein localization to mitochondrion / NS1 Mediated Effects on Host Pathways / response to type I interferon / Modulation of host responses by IFN-stimulated genes / negative regulation of type I interferon-mediated signaling pathway / negative regulation of viral genome replication / RSV-host interactions / positive regulation of interleukin-10 production / 7-methylguanosine mRNA capping / host cell membrane / positive regulation of bone mineralization / negative regulation of protein ubiquitination / positive regulation of interferon-beta production / positive regulation of erythrocyte differentiation / integrin-mediated signaling pathway / Negative regulators of DDX58/IFIH1 signaling / Termination of translesion DNA synthesis / PKR-mediated signaling / DDX58/IFIH1-mediated induction of interferon-alpha/beta / modification-dependent protein catabolic process / integrin binding / ISG15 antiviral mechanism / response to virus / positive regulation of type II interferon production / protein tag activity / Interferon alpha/beta signaling / endonuclease activity / host cell endoplasmic reticulum-Golgi intermediate compartment / 5'-3' DNA helicase activity / 3'-5'-RNA exonuclease activity / symbiont-mediated degradation of host mRNA / symbiont-mediated suppression of host ISG15-protein conjugation / G-quadruplex RNA binding / defense response to virus / omega peptidase activity / symbiont-mediated suppression of host NF-kappaB cascade / symbiont-mediated perturbation of host ubiquitin-like protein modification / methyltransferase cap1 activity / cysteine-type deubiquitinase activity / mRNA 5'-cap (guanine-N7-)-methyltransferase activity / RNA helicase activity / single-stranded RNA binding / defense response to bacterium / viral protein processing / lyase activity / host cell perinuclear region of cytoplasm / symbiont-mediated suppression of host type I interferon-mediated signaling pathway / symbiont-mediated suppression of host gene expression / innate immune response / symbiont-mediated activation of host autophagy / viral translational frameshifting / cysteine-type endopeptidase activity / viral RNA genome replication / RNA-directed RNA polymerase activity / ubiquitin protein ligase binding / DNA-templated transcription / SARS-CoV-2 activates/modulates innate and adaptive immune responses / proteolysis / extracellular region / zinc ion binding / nucleoplasm / ATP binding / identical protein binding / nucleus / membrane / cytosol / cytoplasm
Similarity search - Function
Papain-like viral protease, N-terminal domain / Papain-like viral protease, thumb domain / Jelly Rolls - #1680 / RNA-dependent RNA polymerase, Middle East respiratory syndrome-related coronavirus / : / Non-structural protein 2, MERS-CoV-like / NSP3, SUD-C domain, MERS-CoV-like / AAA domain / Helicase, Ruva Protein; domain 3 / Ubiquitin-like (UB roll) ...Papain-like viral protease, N-terminal domain / Papain-like viral protease, thumb domain / Jelly Rolls - #1680 / RNA-dependent RNA polymerase, Middle East respiratory syndrome-related coronavirus / : / Non-structural protein 2, MERS-CoV-like / NSP3, SUD-C domain, MERS-CoV-like / AAA domain / Helicase, Ruva Protein; domain 3 / Ubiquitin-like (UB roll) / Ubiquitin domain / Ubiquitin family / Ubiquitin homologues / Ubiquitin domain profile. / Ubiquitin-like domain / Nonstructural protein 14, betacoronavirus / 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 / : / DNA2/NAM7 helicase-like, C-terminal / AAA domain / (+) RNA virus helicase core domain / (+)RNA virus helicase core domain profile. / Betacoronavirus single-stranded poly(A) binding domain / 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 / 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 / : / :
Similarity search - Domain/homology
prop-2-en-1-amine / ORF1ab polyprotein / ORF1ab polyprotein / Ubiquitin-like protein ISG15
Similarity search - Component
Biological speciesHuman betacoronavirus 2c EMC/2012
Homo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.411 Å
AuthorsDaczkowski, C.M. / Goodwin, O.Y. / Dzimianski, J.D. / Pegan, S.D.
Funding support United States, 2items
OrganizationGrant numberCountry
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)AI109008 United States
United States Department of Agriculture (USDA)58-5030-5-034 United States
CitationJournal: J. Virol. / Year: 2017
Title: Structurally Guided Removal of DeISGylase Biochemical Activity from Papain-Like Protease Originating from Middle East Respiratory Syndrome Coronavirus.
Authors: Daczkowski, C.M. / Goodwin, O.Y. / Dzimianski, J.V. / Farhat, J.J. / Pegan, S.D.
History
DepositionJun 22, 2017Deposition site: RCSB / Processing site: RCSB
Revision 1.0Sep 27, 2017Provider: repository / Type: Initial release
Revision 1.1Oct 4, 2017Group: Database references / Category: citation / citation_author
Item: _citation.journal_abbrev / _citation.pdbx_database_id_PubMed ..._citation.journal_abbrev / _citation.pdbx_database_id_PubMed / _citation.title / _citation_author.name
Revision 1.2Nov 29, 2017Group: Database references / Category: citation / citation_author
Item: _citation.journal_volume / _citation.title / _citation_author.name
Revision 1.3Dec 11, 2019Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 2.0Apr 29, 2020Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Database references / Derived calculations / Source and taxonomy / Structure summary
Category: atom_site / entity ...atom_site / entity / entity_src_gen / pdbx_nonpoly_scheme / pdbx_struct_assembly_gen / pdbx_struct_conn_angle / pdbx_validate_close_contact / struct_conn / struct_ref / struct_ref_seq / struct_site / struct_site_gen
Item: _atom_site.B_iso_or_equiv / _atom_site.Cartn_x ..._atom_site.B_iso_or_equiv / _atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _atom_site.auth_asym_id / _atom_site.auth_seq_id / _entity.pdbx_description / _entity_src_gen.pdbx_gene_src_gene / _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id / _entity_src_gen.pdbx_gene_src_scientific_name / _pdbx_nonpoly_scheme.auth_seq_num / _pdbx_nonpoly_scheme.pdb_seq_num / _pdbx_nonpoly_scheme.pdb_strand_id / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_struct_conn_angle.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_validate_close_contact.auth_seq_id_2 / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_ref.db_code / _struct_ref.pdbx_db_accession / _struct_ref_seq.pdbx_db_accession / _struct_site.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_seq_id / _struct_site.pdbx_num_residues / _struct_site_gen.auth_asym_id / _struct_site_gen.auth_comp_id / _struct_site_gen.auth_seq_id / _struct_site_gen.label_asym_id / _struct_site_gen.label_comp_id / _struct_site_gen.label_seq_id / _struct_site_gen.pdbx_num_res / _struct_site_gen.site_id
Revision 3.0Apr 24, 2024Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Database references / Derived calculations / Polymer sequence / Source and taxonomy / Structure summary
Category: atom_site / chem_comp_atom ...atom_site / chem_comp_atom / chem_comp_bond / database_2 / entity / entity_poly / entity_poly_seq / entity_src_gen / pdbx_nonpoly_scheme / pdbx_poly_seq_scheme / pdbx_struct_assembly_gen / pdbx_struct_conn_angle / pdbx_unobs_or_zero_occ_residues / pdbx_validate_close_contact / struct_conn / struct_conn_type / struct_ref_seq_dif / struct_site
Item: _atom_site.auth_asym_id / _atom_site.auth_seq_id ..._atom_site.auth_asym_id / _atom_site.auth_seq_id / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _entity.formula_weight / _entity_poly.nstd_monomer / _entity_poly.pdbx_seq_one_letter_code / _entity_poly.pdbx_seq_one_letter_code_can / _entity_src_gen.gene_src_common_name / _entity_src_gen.pdbx_end_seq_num / _pdbx_nonpoly_scheme.pdb_seq_num / _pdbx_nonpoly_scheme.pdb_strand_id / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _pdbx_validate_close_contact.auth_seq_id_2 / _struct_conn.conn_type_id / _struct_conn.id / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr1_symmetry / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_conn.ptnr2_symmetry / _struct_conn_type.id / _struct_site.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: ORF1ab
B: Ubiquitin-like protein ISG15
C: ORF1ab
D: Ubiquitin-like protein ISG15
hetero molecules


Theoretical massNumber of molelcules
Total (without water)90,82720
Polymers89,3754
Non-polymers1,45216
Water2,900161
1
A: ORF1ab
B: Ubiquitin-like protein ISG15
hetero molecules


Theoretical massNumber of molelcules
Total (without water)45,41310
Polymers44,6872
Non-polymers7268
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3830 Å2
ΔGint-102 kcal/mol
Surface area18270 Å2
MethodPISA
2
C: ORF1ab
D: Ubiquitin-like protein ISG15
hetero molecules


Theoretical massNumber of molelcules
Total (without water)45,41310
Polymers44,6872
Non-polymers7268
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3820 Å2
ΔGint-100 kcal/mol
Surface area18110 Å2
MethodPISA
Unit cell
Length a, b, c (Å)86.370, 86.370, 224.087
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number78
Space group name H-MP43

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Components

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Protein , 2 types, 4 molecules ACBD

#1: Protein ORF1ab


Mass: 35817.227 Da / Num. of mol.: 2 / Fragment: UNP residues 1482-1803
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Human betacoronavirus 2c EMC/2012 / Gene: orf1ab / Production host: Escherichia coli (E. coli) / References: UniProt: K0BWD0, UniProt: M4STU1*PLUS
#2: Protein Ubiquitin-like protein ISG15 / Interferon-induced 15 kDa protein / Interferon-induced 17 kDa protein / IP17 / Ubiquitin cross- ...Interferon-induced 15 kDa protein / Interferon-induced 17 kDa protein / IP17 / Ubiquitin cross-reactive protein / hUCRP


Mass: 8870.178 Da / Num. of mol.: 2 / Fragment: UNP residues 80-156
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: ISG15, G1P2, UCRP / Production host: Escherichia coli (E. coli) / References: UniProt: P05161

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Non-polymers , 4 types, 177 molecules

#3: Chemical
ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: Zn
#4: Chemical ChemComp-AYE / prop-2-en-1-amine / ALLYLAMINE


Mass: 57.094 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C3H7N
#5: Chemical
ChemComp-MPD / (4S)-2-METHYL-2,4-PENTANEDIOL


Mass: 118.174 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: C6H14O2 / Comment: precipitant*YM
#6: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 161 / Source method: isolated from a natural source / Formula: H2O

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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: 4.67 Å3/Da / Density % sol: 73.67 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop
Details: 200 mM CaCl2, 100 mM NaO2C2H3 pH 4.6, 28% (v/v) MPD

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 22-ID / Wavelength: 1 Å
DetectorType: RAYONIX MX300-HS / Detector: CCD / Date: Jun 1, 2017
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.41→50 Å / Num. obs: 62651 / % possible obs: 99.45 % / Redundancy: 4.9 % / CC1/2: 0.998 / Net I/σ(I): 31.6
Reflection shellResolution: 2.41→2.45 Å / Mean I/σ(I) obs: 1.49 / CC1/2: 0.723

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Processing

Software
NameVersionClassification
PHENIX(1.11.1_2575: ???)refinement
HKL-2000data reduction
HKL-2000data scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.411→38.626 Å / SU ML: 0.34 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 28.51
RfactorNum. reflection% reflection
Rfree0.2367 3133 5.01 %
Rwork0.2125 --
obs0.2137 62588 99.48 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Refinement stepCycle: LAST / Resolution: 2.411→38.626 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms6216 0 78 161 6455
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0076430
X-RAY DIFFRACTIONf_angle_d0.6158680
X-RAY DIFFRACTIONf_dihedral_angle_d6.4573792
X-RAY DIFFRACTIONf_chiral_restr0.0421000
X-RAY DIFFRACTIONf_plane_restr0.0041088
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.4112-2.44890.39531260.34342627X-RAY DIFFRACTION97
2.4489-2.48910.33091540.32772704X-RAY DIFFRACTION100
2.4891-2.5320.30561430.30242702X-RAY DIFFRACTION100
2.532-2.5780.36271490.28552695X-RAY DIFFRACTION100
2.578-2.62760.27851360.29342704X-RAY DIFFRACTION100
2.6276-2.68120.29681600.28062688X-RAY DIFFRACTION100
2.6812-2.73950.28991450.28852694X-RAY DIFFRACTION100
2.7395-2.80320.31251310.28312756X-RAY DIFFRACTION100
2.8032-2.87330.26991560.27362695X-RAY DIFFRACTION100
2.8733-2.95090.2711370.27552687X-RAY DIFFRACTION100
2.9509-3.03770.23091430.27052718X-RAY DIFFRACTION100
3.0377-3.13570.28951220.25822714X-RAY DIFFRACTION100
3.1357-3.24780.31581540.25652715X-RAY DIFFRACTION100
3.2478-3.37770.30371440.24852705X-RAY DIFFRACTION100
3.3777-3.53130.24611800.23142684X-RAY DIFFRACTION100
3.5313-3.71740.2088910.21132770X-RAY DIFFRACTION100
3.7174-3.95010.23951690.20392714X-RAY DIFFRACTION100
3.9501-4.25470.25431320.182687X-RAY DIFFRACTION100
4.2547-4.68220.18061260.16372747X-RAY DIFFRACTION100
4.6822-5.35820.21731480.16862732X-RAY DIFFRACTION100
5.3582-6.74490.20321550.19382713X-RAY DIFFRACTION100
6.7449-38.63080.15061320.16052604X-RAY DIFFRACTION94
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)
15.82020.71151.72924.98690.5266.06190.190.61320.2319-0.77080.1652-0.1253-0.28430.7102-0.31990.7963-0.01620.1060.57350.02080.5057-4.413419.2964-47.5195
25.537-1.8076-1.0418.75890.37411.45290.0211-0.1786-0.40430.3132-0.55110.313-0.3033-0.46860.28340.581-0.022-0.08340.39350.01240.5827-26.425229.0713-26.7538
35.6457-2.2256-2.71624.52414.38677.8785-0.1420.7005-0.448-0.5398-1.24831.3380.5506-1.33521.34330.7016-0.0549-0.04930.5608-0.13110.7971-29.407524.446-33.9657
42.2637-2.23370.64418.4483.1412.4534-0.2577-0.2681-0.79181.2912-0.28390.95611.4975-1.24370.41170.7472-0.21240.1010.54510.03140.5974-26.787119.8393-24.0154
59.1521-2.50190.58454.241.11298.0682-0.06570.0725-1.38420.53130.10110.74591.4876-0.9424-0.09250.6998-0.13890.03070.4084-0.01870.6535-23.397514.4738-32.158
69.4899-3.6682-1.67492.45243.22686.6996-0.486-0.5292-0.08351.05960.72810.15770.22710.935-0.28290.8011-0.05860.06730.4642-0.00480.5423-14.876319.4518-26.318
77.6044-1.72920.31892.0562.51076.62290.1736-0.21820.56420.413-0.0713-0.5893-0.75160.7244-0.09050.7017-0.0469-0.07240.2896-0.02970.605-18.524628.7743-25.1381
82.7158-4.4511-1.0737.60291.51633.84580.2679-0.0101-0.4871-0.7921-0.16471.09040.2636-0.5098-0.1240.6901-0.0647-0.06990.528-0.00710.5937-21.017414.8792-36.591
93.3931-1.66950.33425.08782.12594.95030.26830.5321-0.2015-0.6023-0.1283-0.02720.2736-0.6048-0.18980.75010.1365-0.08470.7693-0.00130.5382-34.4159-49.1192-49.4619
102.6579-0.5161-0.84772.77462.38825.67940.25210.0855-0.4170.4543-0.10430.08861.0896-0.3982-0.06010.685-0.0434-0.12590.43020.02030.459-38.8278-41.4178-26.215
111.52511.32090.0874.3478-0.48993.92450.1522-0.08320.42810.5295-0.01750.2155-0.7118-0.2475-0.12790.57630.15020.05050.38050.02720.5208-34.375-16.0712-18.2556
123.87860.4178-0.72843.13840.08945.07460.299-0.4424-0.16341.1435-0.1169-0.05390.6968-0.4498-0.15171.0349-0.133-0.07140.48850.08470.4503-37.7637-36.9349-7.2428
135.3502-1.4431.91915.28450.11925.6542-0.0144-0.69970.21490.7570.3014-0.1020.0948-0.7428-0.30260.6942-0.01710.09690.5272-0.02350.4494-38.7605-23.9996-8.8636
143.54281.6244-0.73547.7606-1.777.67240.08920.0996-0.53920.0062-0.1907-0.60790.39581.1310.24140.49130.0438-0.02870.38920.00850.6055-16.0754-17.1705-28.302
153.16383.2158-1.24944.8345-4.12766.592-0.08470.1277-0.4817-0.2874-0.132-0.4960.49890.37060.20290.57010.11070.01830.332-0.05010.5318-21.5865-24.4801-26.8581
162.84831.7208-0.6975.8973-2.86714.46530.32-0.5625-0.16020.6832-0.23380.23790.160.6016-0.05940.7018-0.1455-0.09880.7402-0.01410.5075-8.7425-5.9192-6.8829
173.88280.8966-1.36893.9573-2.54765.9070.2965-0.1125-0.3882-0.4239-0.228-0.14261.17450.6321-0.06160.68840.0716-0.12760.4193-0.01660.4635-3.08691.7968-30.0113
181.9669-0.98370.78343.49450.42794.36170.1384-0.0160.3885-0.55680.0421-0.3066-0.49340.1924-0.180.4984-0.11890.0310.3877-0.03240.4747-9.44625.0024-37.5819
195.3219-0.5266-0.64313.9710.46854.77080.29940.5914-0.215-1.036-0.059-0.04620.70820.4431-0.23760.9780.1129-0.08810.4608-0.07070.4237-5.40196.2766-49.1305
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'C' and (resid 302 through 320 )
2X-RAY DIFFRACTION2chain 'D' and (resid 80 through 87 )
3X-RAY DIFFRACTION3chain 'D' and (resid 88 through 98 )
4X-RAY DIFFRACTION4chain 'D' and (resid 99 through 115 )
5X-RAY DIFFRACTION5chain 'D' and (resid 116 through 126 )
6X-RAY DIFFRACTION6chain 'D' and (resid 127 through 136 )
7X-RAY DIFFRACTION7chain 'D' and (resid 137 through 146 )
8X-RAY DIFFRACTION8chain 'D' and (resid 147 through 156 )
9X-RAY DIFFRACTION9chain 'A' and (resid 2 through 78 )
10X-RAY DIFFRACTION10chain 'A' and (resid 79 through 165 )
11X-RAY DIFFRACTION11chain 'A' and (resid 166 through 256 )
12X-RAY DIFFRACTION12chain 'A' and (resid 257 through 301 )
13X-RAY DIFFRACTION13chain 'A' and (resid 302 through 320 )
14X-RAY DIFFRACTION14chain 'B' and (resid 80 through 103 )
15X-RAY DIFFRACTION15chain 'B' and (resid 104 through 156 )
16X-RAY DIFFRACTION16chain 'C' and (resid 2 through 78 )
17X-RAY DIFFRACTION17chain 'C' and (resid 79 through 156 )
18X-RAY DIFFRACTION18chain 'C' and (resid 157 through 256 )
19X-RAY DIFFRACTION19chain 'C' and (resid 257 through 301 )

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