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- PDB-7mhl: Ensemble refinement structure of SARS-CoV-2 main protease (Mpro) ... -

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Basic information

Entry
Database: PDB / ID: 7mhl
TitleEnsemble refinement structure of SARS-CoV-2 main protease (Mpro) at 100 K
Components3C-like proteinase
KeywordsHYDROLASE / SARS-CoV-2 / Coronavirus / main protease / 3CLpro / Mpro / ensemble refinement / temperature series / temperature / multitemperature
Function / homology
Function and homology information


Assembly of the SARS-CoV-2 Replication-Transcription Complex (RTC) / Maturation of replicase proteins / suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of TBK1 activity / viral RNA-directed RNA polymerase complex / exoribonuclease complex / endoribonuclease complex / Transcription of SARS-CoV-2 sgRNAs / endopeptidase complex / 5'-3' RNA helicase activity / mRNA cap methyltransferase complex ...Assembly of the SARS-CoV-2 Replication-Transcription Complex (RTC) / Maturation of replicase proteins / suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of TBK1 activity / viral RNA-directed RNA polymerase complex / exoribonuclease complex / endoribonuclease complex / Transcription of SARS-CoV-2 sgRNAs / endopeptidase complex / 5'-3' RNA helicase activity / mRNA cap methyltransferase complex / RNA phosphodiester bond hydrolysis, exonucleolytic / Translation of Replicase and Assembly of the Replication Transcription Complex / Replication of the SARS-CoV-2 genome / positive regulation of RNA biosynthetic process / Lyases; Phosphorus-oxygen lyases / modulation by virus of host autophagy / mRNA methylation / double membrane vesicle viral factory outer membrane / suppression by virus of host translation / ISG15-specific peptidase activity / SARS coronavirus main proteinase / suppression by virus of host type I interferon production / Hydrolases; Acting on ester bonds; Exoribonucleases producing 5'-phosphomonoesters / 3'-5'-exoribonuclease activity / host cell endosome / host cell endoplasmic reticulum-Golgi intermediate compartment / induction by virus of catabolism of host mRNA / cytoplasmic viral factory / protein K48-linked deubiquitination / G-quadruplex RNA binding / suppression by virus of host ISG15-protein conjugation / 7-methylguanosine mRNA capping / transcription, RNA-templated / viral transcription / suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF3 activity / host cell Golgi apparatus / suppression by virus of host toll-like receptor signaling pathway / host cell endoplasmic reticulum / suppression by virus of host NF-kappaB cascade / modulation by virus of host protein ubiquitination / protein K63-linked deubiquitination / methyltransferase cap1 / positive regulation of viral genome replication / mRNA (nucleoside-2'-O-)-methyltransferase activity / positive stranded viral RNA replication / suppression by virus of host TRAF activity / protein autoprocessing / cysteine-type peptidase activity / helicase activity / ubiquitinyl hydrolase 1 / DNA helicase / DNA helicase activity / cysteine-type deubiquitinase activity / single-stranded RNA binding / Hydrolases; Acting on peptide bonds (peptidases); Cysteine endopeptidases / protein processing / host cell perinuclear region of cytoplasm / viral protein processing / RNA helicase / lyase activity / induction by virus of host autophagy / RNA-directed RNA polymerase / suppression by virus of host gene expression / endonuclease activity / cysteine-type endopeptidase activity / viral RNA genome replication / RNA-directed 5'-3' RNA polymerase activity / transcription, DNA-templated / suppression by virus of host type I interferon-mediated signaling pathway / host cell cytoplasm / protein dimerization activity / host cell nucleus / ATP hydrolysis activity / protein homodimerization activity / zinc ion binding / integral component of membrane / ATP binding / identical protein binding / cytosol
Similarity search - Function
RNA-dependent RNA polymerase, SARS-CoV-like / Coronavirus Nsp12 RNA-dependent RNA polymerase (RdRp) domain profile. / Nidovirus 2'-O-methyltransferase (2'-O-MTase) domain profile. / Nonstructural protein 15, middle domain, alpha/betacoronavirus / Nidovirus 3'-5' exoribonuclease (ExoN) domain profile. / Coronavirus (CoV) guanine-N7-methyltransferase (N7-MTase) domain profile. / Nonstructural protein 14, betacoronavirus / Coronavirus (CoV) Nsp15 N-terminal oligomerization domain profile. / Nidoviral uridylate-specific endoribonuclease (NendoU) domain profile. / Arterivirus Nsp11 N-terminal/coronavirus NSP15 middle (AV-Nsp11N/CoV-Nsp15M) domain profile. ...RNA-dependent RNA polymerase, SARS-CoV-like / Coronavirus Nsp12 RNA-dependent RNA polymerase (RdRp) domain profile. / Nidovirus 2'-O-methyltransferase (2'-O-MTase) domain profile. / Nonstructural protein 15, middle domain, alpha/betacoronavirus / Nidovirus 3'-5' exoribonuclease (ExoN) domain profile. / Coronavirus (CoV) guanine-N7-methyltransferase (N7-MTase) domain profile. / Nonstructural protein 14, betacoronavirus / Coronavirus (CoV) Nsp15 N-terminal oligomerization domain profile. / Nidoviral uridylate-specific endoribonuclease (NendoU) domain profile. / Arterivirus Nsp11 N-terminal/coronavirus NSP15 middle (AV-Nsp11N/CoV-Nsp15M) domain profile. / Viral (Superfamily 1) RNA helicase / Nonstructural protein 15, N-terminal domain, alpha/beta-coronavirus / NSP15, NendoU domain, coronavirus / Nonstructural protein 13, 1B domain, coronavirus / Coronavirus replicase NSP15, middle domain / Coronavirus replicase NSP15, N-terminal oligomerisation / Coronavirus proofreading exoribonuclease / Non-structural protein NSP16, coronavirus-like / Coronavirus RNA-dependent RNA polymerase, N-terminal / RNA polymerase, N-terminal, coronavirus / Coronavirus 2'-O-methyltransferase / Non-structural protein 14, coronavirus / Non-structural protein NSP15, N-terminal domain superfamily, coronavirus / Non-structural protein NSP15, middle domain superfamily / Coronavirus replicase NSP15, N-terminal oligomerisation / Nonstructural protein 15, middle domain, coronavirus / Nidovirus RdRp-associated nucleotidyl transferase (NiRAN) domain / Nonstructural protein 13, zinc-binding domain, coronavirus-like / Nidovirus RdRp-associated nucleotidyl transferase (NiRAN) domain profile. / Coronaviridae zinc-binding (CV ZBD) domain profile. / NendoU domain, nidovirus / Coronavirus replicase NSP15, uridylate-specific endoribonuclease / Endoribonuclease EndoU-like / Non-structural protein NSP3, SUD-N (Mac2) domain, betacoronavirus / Sarbecovirus Nsp3c-N domain profile. / Non-structural protein 2, SARS-CoV-like / Non-structural protein NSP3, SUD-N (Mac2) domain superfamily, betacoronavirus / Betacoronavirus replicase NSP3, N-terminal / Polyprotein cleavage domain PL2pro superfamily, betacoronavirus / Betacoronavirus SUD-C domain / Non-structural protein NSP3, N-terminal, betacoronavirus / Non-structural protein NSP1 superfamily, betacoronavirus / (+) RNA virus helicase core domain / (+)RNA virus helicase core domain profile. / Carbamoyl-phosphate synthase subdomain signature 2. / Betacoronavirus (BetaCoV) Nsp1 C-terminal domain profile. / Lipocalin signature. / Coronavirus (CoV) Nsp1 globular domain profile. / Betacoronavirus Nsp3c-M domain profile. / Betacoronavirus single-stranded poly(A) binding domain / Betacoronavirus replicase NSP1 / Non-structural protein NSP3, SUD-M domain, betacoronavirus / Non-structural protein NSP3, SUD-M domain superfamily, betacoronavirus / Non-structural protein NSP1, betacoronavirus / Betacoronavirus Nsp3e nucleic acid-binding (NAB) domain profile. / Betacoronavirus Nsp3c-C domain profile. / Coronavirus RNA-dependent RNA polymerase (RdRp) Nsp7 cofactor domain profile. / DPUP/SUD, C-terminal, betacoronavirus / Coronavirus RNA-dependent RNA polymerase (RdRp) Nsp8 cofactor domain profile. / Coronavirus (CoV) ExoN/MTase coactivator domain profile. / Coronavirus Nsp9 single-stranded RNA (ssRNA)-binding domain profile. / Non-structural protein NSP3, nucleic acid-binding domain superfamily, betacoronavirus / Non-structural protein 6, betacoronavirus / Betacoronavirus nucleic acid-binding (NAB) / Non-structural protein NSP3A domain-like superfamily / Non-structural protein NSP3, nucleic acid-binding domain, betacoronavirus / Papain-like protease, N-terminal domain superfamily, coronavirus / Papain-like viral protease, palm and finger domains, coronavirus / Nonstructural protein 2, N-terminal domain, coronavirus / Coronavirus replicase NSP2, N-terminal / Non-structural protein 2, C-terminal domain, coronavirus / Coronavirus replicase NSP2, C-terminal / Coronavirus Nsp3d Ubl domain profile. / Coronavirus Nsp3a Ubl domain profile. / NSP3, first ubiquitin-like (Ubl) domain, coronavirus / Coronavirus Nsp4 C-terminal (Nsp4C) domain profile. / NSP3, second ubiquitin-like (Ubl) domain, coronavirus / Papain-like protease, thumb domain superfamily, coronavirus / Non-structural protein NSP7, coronavirus / Peptidase family C16 domain profile. / Coronavirus replicase NSP7 / Non-structural protein 6, coronavirus / Coronavirus replicase NSP3, C-terminal / Non-structural protein NSP4, N-terminal, coronavirus / Coronavirus RNA synthesis protein NSP10 / Coronavirus replicase NSP8 / Coronavirus endopeptidase C30 / Coronavirus main protease (M-pro) domain profile. / Non-structural protein NSP7 superfamily, coronavirus / Peptidase C30, domain 3, coronavirus / Non-structural protein NSP8, coronavirus / Coronavirus replicase NSP3, C-terminal / Coronavirus replicase NSP4, N-terminal / Coronavirus replicase NSP6 / Non-structural protein NSP4, C-terminal superfamily, coronavirus / Peptidase C30, coronavirus / Peptidase C16, coronavirus / Non-structural protein NSP9, coronavirus / Coronavirus papain-like peptidase / RNA synthesis protein NSP10, coronavirus
Similarity search - Domain/homology
Replicase polyprotein 1ab
Similarity search - Component
Biological speciesSevere acute respiratory syndrome coronavirus 2
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 1.55 Å
AuthorsEbrahim, A. / Riley, B.T. / Kumaran, D. / Andi, B. / Fuchs, M.R. / McSweeney, S. / Keedy, D.A.
Funding support United States, 7items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM133769 United States
Department of Energy (DOE, United States)National Virtual Biotechnology Laboratory (NVBL) United States
Department of Energy (DOE, United States)Coronavirus CARES Act United States
Department of Energy (DOE, United States)BNL LDRD 20-042 United States
Department of Energy (DOE, United States)DE-SC0012704 United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)P30GM133893 United States
Department of Energy (DOE, United States)KP1605010 United States
CitationJournal: Biorxiv / Year: 2021
Title: The temperature-dependent conformational ensemble of SARS-CoV-2 main protease (M pro ).
Authors: Ebrahim, A. / Riley, B.T. / Kumaran, D. / Andi, B. / Fuchs, M.R. / McSweeney, S. / Keedy, D.A.
History
DepositionApr 15, 2021Deposition site: RCSB / Processing site: RCSB
Revision 1.0May 12, 2021Provider: repository / Type: Initial release
Revision 1.1May 26, 2021Group: Database references / Category: citation / citation_author
Item: _citation.pdbx_database_id_PubMed / _citation.title / _citation_author.identifier_ORCID
Revision 2.0Apr 6, 2022Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Database references / Derived calculations / Refinement description / Source and taxonomy / Structure summary
Category: atom_site / atom_site_anisotrop ...atom_site / atom_site_anisotrop / atom_type / chem_comp / citation_author / database_2 / database_PDB_caveat / entity / entity_src_gen / pdbx_contact_author / pdbx_distant_solvent_atoms / pdbx_entity_nonpoly / pdbx_nonpoly_scheme / pdbx_refine_tls / pdbx_refine_tls_group / pdbx_struct_assembly / pdbx_struct_assembly_gen / pdbx_struct_assembly_prop / pdbx_struct_conn_angle / pdbx_struct_sheet_hbond / pdbx_struct_special_symmetry / pdbx_validate_main_chain_plane / pdbx_validate_peptide_omega / pdbx_validate_planes / pdbx_validate_polymer_linkage / pdbx_validate_rmsd_angle / pdbx_validate_rmsd_bond / pdbx_validate_torsion / refine / refine_ls_shell / software / struct / struct_asym / struct_conf / struct_conn / struct_keywords / struct_sheet_range / struct_site / struct_site_gen
Item: _citation_author.identifier_ORCID / _database_2.pdbx_DOI ..._citation_author.identifier_ORCID / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _database_PDB_caveat.text / _entity_src_gen.gene_src_common_name / _pdbx_struct_assembly.details / _pdbx_struct_assembly.method_details / _pdbx_struct_sheet_hbond.range_1_auth_comp_id / _pdbx_struct_sheet_hbond.range_1_auth_seq_id / _pdbx_struct_sheet_hbond.range_1_label_comp_id / _pdbx_struct_sheet_hbond.range_1_label_seq_id / _pdbx_struct_sheet_hbond.range_2_auth_comp_id / _pdbx_struct_sheet_hbond.range_2_auth_seq_id / _pdbx_struct_sheet_hbond.range_2_label_comp_id / _pdbx_struct_sheet_hbond.range_2_label_seq_id / _refine.ls_R_factor_R_free / _refine.ls_R_factor_R_work / _refine.ls_R_factor_obs / _refine.ls_number_reflns_R_free / _refine_ls_shell.R_factor_R_free / _refine_ls_shell.R_factor_R_work / _refine_ls_shell.d_res_low / _refine_ls_shell.number_reflns_R_work / _refine_ls_shell.number_reflns_all / _refine_ls_shell.pdbx_total_number_of_bins_used / _software.version / _struct.title / _struct_conf.beg_auth_comp_id / _struct_conf.beg_auth_seq_id / _struct_conf.beg_label_comp_id / _struct_conf.beg_label_seq_id / _struct_conf.end_auth_comp_id / _struct_conf.end_auth_seq_id / _struct_conf.end_label_comp_id / _struct_conf.end_label_seq_id / _struct_conf.pdbx_PDB_helix_class / _struct_conf.pdbx_PDB_helix_length / _struct_keywords.text / _struct_sheet_range.beg_auth_comp_id / _struct_sheet_range.beg_auth_seq_id / _struct_sheet_range.beg_label_comp_id / _struct_sheet_range.beg_label_seq_id
Description: Ligand identity
Details: X-ray fluorescence is consistent with the presence of Zn.
Provider: author / Type: Coordinate replacement

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: 3C-like proteinase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)34,2827
Polymers33,8261
Non-polymers4566
Water3,423190
1
A: 3C-like proteinase
hetero molecules

A: 3C-like proteinase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)68,56314
Polymers67,6512
Non-polymers91212
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_555-x,y,-z1
Buried area4420 Å2
ΔGint-9 kcal/mol
Surface area27170 Å2
MethodPISA
Unit cell
Length a, b, c (Å)113.706, 53.320, 44.567
Angle α, β, γ (deg.)90.000, 102.960, 90.000
Int Tables number5
Space group name H-MC121
Number of models54
Components on special symmetry positions
IDModelComponents
11A-605-

HOH

23A-531-

HOH

33A-537-

HOH

44A-545-

HOH

54A-645-

HOH

65A-510-

HOH

75A-554-

HOH

86A-567-

HOH

96A-621-

HOH

107A-507-

HOH

117A-653-

HOH

128A-503-

HOH

138A-571-

HOH

148A-592-

HOH

158A-636-

HOH

169A-583-

HOH

179A-592-

HOH

189A-632-

HOH

199A-650-

HOH

2010A-552-

HOH

2110A-557-

HOH

2210A-600-

HOH

2311A-544-

HOH

2411A-557-

HOH

2511A-633-

HOH

2612A-565-

HOH

2712A-573-

HOH

2812A-679-

HOH

2913A-634-

HOH

3013A-652-

HOH

3114A-598-

HOH

3214A-640-

HOH

3315A-530-

HOH

3416A-564-

HOH

3516A-666-

HOH

3617A-520-

HOH

3717A-668-

HOH

3818A-553-

HOH

3918A-629-

HOH

4018A-654-

HOH

4119A-539-

HOH

4219A-540-

HOH

4319A-589-

HOH

4420A-524-

HOH

4521A-513-

HOH

4621A-646-

HOH

4722A-587-

HOH

4822A-637-

HOH

4923A-623-

HOH

5023A-666-

HOH

5124A-577-

HOH

5224A-655-

HOH

5325A-597-

HOH

5425A-603-

HOH

5526A-583-

HOH

5626A-591-

HOH

5726A-674-

HOH

5827A-629-

HOH

5927A-641-

HOH

6028A-557-

HOH

6129A-507-

HOH

6229A-640-

HOH

6330A-541-

HOH

6431A-674-

HOH

6532A-635-

HOH

6633A-536-

HOH

6733A-551-

HOH

6833A-674-

HOH

6934A-600-

HOH

7035A-519-

HOH

7135A-579-

HOH

7236A-520-

HOH

7336A-610-

HOH

7436A-623-

HOH

7537A-501-

HOH

7637A-530-

HOH

7737A-655-

HOH

7838A-648-

HOH

7938A-662-

HOH

8039A-543-

HOH

8139A-613-

HOH

8240A-531-

HOH

8340A-661-

HOH

8441A-513-

HOH

8541A-537-

HOH

8641A-555-

HOH

8742A-515-

HOH

8842A-629-

HOH

8943A-552-

HOH

9043A-556-

HOH

9143A-581-

HOH

9244A-503-

HOH

9344A-610-

HOH

9444A-637-

HOH

9545A-646-

HOH

9647A-506-

HOH

9748A-578-

HOH

9849A-609-

HOH

9950A-512-

HOH

10050A-660-

HOH

10151A-567-

HOH

10251A-661-

HOH

10352A-507-

HOH

10452A-642-

HOH

10553A-521-

HOH

10653A-551-

HOH

10754A-624-

HOH

10854A-668-

HOH

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Components

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


Mass: 33825.547 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Severe acute respiratory syndrome coronavirus 2
Gene: rep, 1a-1b / Plasmid: pET29b / Production host: Escherichia coli BL21(DE3) (bacteria)
References: UniProt: P0DTD1, SARS coronavirus main proteinase
#2: Chemical
ChemComp-DMS / DIMETHYL SULFOXIDE / Dimethyl sulfoxide


Mass: 78.133 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: C2H6OS / Comment: DMSO, precipitant*YM
#3: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Formula: Zn
#4: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 190 / 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: 1.95 Å3/Da / Density % sol: 36.8 %
Crystal growTemperature: 298 K / Method: vapor diffusion, sitting drop / pH: 7 / Details: 22% PEG4000, 100 mM HEPES, pH 7.0, 3-5% DMSO

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: NSLS-II / Beamline: 17-ID-2 / Wavelength: 0.9793 Å
DetectorType: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Jun 3, 2020
RadiationMonochromator: Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9793 Å / Relative weight: 1
ReflectionResolution: 1.5477→48.047 Å / Num. obs: 37901 / % possible obs: 99.7185 % / Redundancy: 3.3653 % / CC1/2: 0.9769 / Rmerge(I) obs: 0.1579 / Rpim(I) all: 0.1004 / Rrim(I) all: 0.1876 / Net I/σ(I): 3.2643 / Num. measured all: 127548
Reflection shell

Diffraction-ID: 1

Resolution (Å)% possible obs (%)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsNum. measured obsNum. unique obsCC1/2Rpim(I) allRrim(I) all
1.5477-1.574495.95593.39520.50741.0276620318270.69480.32480.6044
1.5744-1.603199.73453.40360.47731.113639218780.73820.30330.5672
1.6031-1.63391003.36860.45881.1926627918640.72340.29460.5472
1.6339-1.667299.9473.32130.43021.3178626418860.73270.27850.5141
1.6672-1.703599.94783.27310.39751.5079626819150.73770.25910.476
1.7035-1.743199.94683.10370.37141.6182583518800.77140.25040.4494
1.7431-1.78671003.30850.34541.8623633919160.80470.22350.4127
1.7867-1.83599.89213.24510.31862.1269601018520.81460.20640.3807
1.835-1.88999.89423.33740.31522.4798630118880.82640.20020.3744
1.889-1.9599.47153.52230.28282.978662918820.86380.17470.3331
1.95-2.01971003.47980.26363.3583662219030.88320.16420.3112
2.0197-2.10061003.4620.24533.7137660919090.8920.1530.2897
2.1006-2.19621003.42240.23414.0265637618630.90560.14690.277
2.1962-2.311999.89693.32990.21674.2126645019370.89410.13910.2583
2.3119-2.456899.89353.1610.19794.271593018760.910.13150.2384
2.4568-2.64651003.32430.1774.6905635619120.93290.1150.2117
2.6465-2.912899.94733.53350.1645.3012669618950.94480.10180.1934
2.9128-3.33421003.58630.1445.9356690019240.95990.08870.1695
3.3342-4.200399.9483.40760.12566.2065654619210.96120.07970.1492
4.2003-48.070299.89873.31630.09825.986654319730.97740.06380.1175

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Phasing

PhasingMethod: molecular replacement

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Processing

Software
NameVersionClassification
PHENIX(phenix.ensemble_refinement:1.19.2_4158)refinement
xia20.5.902-gffa11588-dials-1.14data reduction
DIALS1.14.13-g10ecfbb15-releasedata scaling
PHASER1.18.2_3874phasing
PDB_EXTRACT3.28data extraction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 6YB7

6yb7


Resolution: 1.55→48.047 Å / Cross valid method: THROUGHOUT
RfactorNum. reflection% reflection
Rfree0.2272 --
Rwork0.1658 --
obs0.1689 37898 99.71 %
Refinement stepCycle: final / Resolution: 1.55→48.047 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2367 0 0 0 2367
Num. residues----0
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection Rwork% reflection obs (%)
1.55-1.590.29231410.225248397
1.59-1.630.29481430.2082520100
1.63-1.680.27651420.20312590100
1.68-1.730.26431480.19082542100
1.73-1.790.26531270.18322588100
1.79-1.870.3141120.19142575100
1.87-1.950.26981260.18372550100
1.95-2.050.25011350.17962591100
2.05-2.180.25791330.18062578100
2.18-2.350.2241420.16272553100
2.35-2.590.23011430.15722582100
2.59-2.960.20931480.1512578100
2.96-3.730.19971300.15592596100
3.73-48.0470.18621360.14752666100

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