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- PDB-5wuc: Structural basis for conductance through TRIC cation channels -

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Basic information

Entry
Database: PDB / ID: 5wuc
TitleStructural basis for conductance through TRIC cation channels
ComponentsUncharacterized protein
KeywordsMEMBRANE PROTEIN / TRIC / cation channel / Structural Genomics / PSI-Biology / New York Consortium on Membrane Protein Structure / NYCOMPS
Function / homologyGlycine transporter / Glycine transporter / membrane => GO:0016020 / plasma membrane / Glycine transporter domain-containing protein / Membrane protein
Function and homology information
Biological speciesSulfolobus acidocaldarius (acidophilic)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.6 Å
AuthorsSu, M. / Gao, F. / Mao, Y. / Li, D.L. / Guo, Y.Z. / Wang, X.H. / Bruni, R. / Kloss, B. / Hendrickson, W.A. / Chen, Y.H. / New York Consortium on Membrane Protein Structure (NYCOMPS)
CitationJournal: Nat Commun / Year: 2017
Title: Structural basis for conductance through TRIC cation channels.
Authors: Su, M. / Gao, F. / Yuan, Q. / Mao, Y. / Li, D.L. / Guo, Y. / Yang, C. / Wang, X.H. / Bruni, R. / Kloss, B. / Zhao, H. / Zeng, Y. / Zhang, F.B. / Marks, A.R. / Hendrickson, W.A. / Chen, Y.H.
History
DepositionDec 17, 2016Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Jul 12, 2017Provider: repository / Type: Initial release
Revision 1.1Mar 20, 2024Group: Data collection / Database references / Derived calculations
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_struct_conn_angle / struct_conn
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _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.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 / _struct_conn.pdbx_dist_value / _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.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_symmetry

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Uncharacterized protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)25,7633
Polymers25,7171
Non-polymers462
Water1,60389
1
A: Uncharacterized protein
hetero molecules

A: Uncharacterized protein
hetero molecules

A: Uncharacterized protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)77,2899
Polymers77,1513
Non-polymers1386
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_755-y+2,x-y,z1
crystal symmetry operation3_775-x+y+2,-x+2,z1
Buried area6140 Å2
ΔGint-92 kcal/mol
Surface area21520 Å2
MethodPISA
Unit cell
Length a, b, c (Å)64.253, 64.253, 80.811
Angle α, β, γ (deg.)90.000, 90.000, 120.000
Int Tables number173
Space group name H-MP63
Components on special symmetry positions
IDModelComponents
11A-301-

NA

21A-302-

NA

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Components

#1: Protein Uncharacterized protein / prokaryotic SaTRIC


Mass: 25716.924 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Sulfolobus acidocaldarius (acidophilic)
Gene: ATY89_00310, ATZ20_03355 / Production host: Escherichia coli (E. coli) / Strain (production host): 'BL21-Gold(DE3)pLysS AG' / References: UniProt: A0A0U3H1E6, UniProt: Q4J9E6*PLUS
#2: Chemical ChemComp-NA / SODIUM ION


Mass: 22.990 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Na
#3: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 89 / 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: 1.87 Å3/Da / Density % sol: 34.31 %
Crystal growTemperature: 291 K / Method: lipidic cubic phase / pH: 6
Details: PEG 200 40%, NaCl 100mM, MgCl2 100mM, MES pH 6.0 100mM

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SSRF / Beamline: BL19U1 / Wavelength: 0.97876 Å
DetectorType: DECTRIS PILATUS3 S 6M / Detector: PIXEL / Date: Dec 18, 2014
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97876 Å / Relative weight: 1
Reflection twinOperator: h,-h-k,-l / Fraction: 0.261
ReflectionResolution: 1.6→46.03 Å / Num. obs: 48871 / % possible obs: 100 % / Redundancy: 20.3 % / Biso Wilson estimate: 22.1 Å2 / CC1/2: 0.999 / Rmerge(I) obs: 0.0246 / Net I/σ(I): 14.5
Reflection shell
Resolution (Å)Redundancy (%)Rmerge(I) obsCC1/2Diffraction-ID% possible all
1.8-1.8420.40.04920.318199.4
9-46.03210.0331199.4

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Processing

Software
NameVersionClassification
PHENIXdev_2481refinement
Aimless0.5.28data scaling
PDB_EXTRACT3.22data extraction
XDSdata reduction
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.6→32.695 Å / SU ML: 0.24 / Cross valid method: NONE / σ(F): 1.34 / Phase error: 25.33 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2392 2459 5.03 %
Rwork0.2189 46412 -
obs0.22 48871 99.14 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 78.76 Å2 / Biso mean: 26.1731 Å2 / Biso min: 13.76 Å2
Refinement stepCycle: LAST / Resolution: 1.6→32.695 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1455 0 2 89 1546

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