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- PDB-2n6e: NMR structure of a DUF1491 family protein (CC_1065) from Caulobac... -

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Basic information

Entry
Database: PDB / ID: 2n6e
TitleNMR structure of a DUF1491 family protein (CC_1065) from Caulobacter crescentus CB15
ComponentsUncharacterized protein
KeywordsUNKNOWN FUNCTION / PSI-Biology / Structural Genomics / Joint Center for Structural Genomics / JCSG
Function / homologyProtein of unknown function (DUF1491) / Protein of unknown function DUF1491 / Protein of unknown function (DUF1491) / hypothetical protein tt1805 / 3-Layer(aba) Sandwich / Alpha Beta / DUF1491 domain-containing protein
Function and homology information
Biological speciesCaulobacter crescentus (bacteria)
MethodSOLUTION NMR / molecular dynamics, Torsion Angle Dynamics
AuthorsQin, H. / Serrano, P. / Wuthrich, K. / Joint Center for Structural Genomics (JCSG)
CitationJournal: To be Published
Title: NMR structure of a DUF1491 family protein (CC_1065) from Caulobacter crescentus CB15
Authors: Qin, H.T. / Wuthrich, K. / Serrano, P.
History
DepositionAug 19, 2015Deposition site: BMRB / Processing site: RCSB
Revision 1.0Oct 14, 2015Provider: repository / Type: Initial release
Revision 1.1Jun 14, 2023Group: Data collection / Database references / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_nmr_spectrometer / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_nmr_data / _pdbx_nmr_spectrometer.model / _struct_ref_seq_dif.details
Revision 1.2May 15, 2024Group: Data collection / Database references / Category: chem_comp_atom / chem_comp_bond / database_2 / Item: _database_2.pdbx_DOI

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Uncharacterized protein


Theoretical massNumber of molelcules
Total (without water)12,2631
Polymers12,2631
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / 80target function
RepresentativeModel #1lowest energy

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Components

#1: Protein Uncharacterized protein


Mass: 12262.771 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Caulobacter crescentus (bacteria) / Strain: ATCC 19089 / CB15 / Gene: CC_1065 / Plasmid: pSpeedET / Production host: Escherichia coli (E. coli) / References: UniProt: Q9A9C4

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1112D 1H-15N HSQC
1213D 1H-13C NOESY aliphatic
1313D 1H-13C NOESY aromatic
1413D 1H-15N NOESY
151APSY 4D-HACANH
161APSY 5D-CBCA(CO)NH
171APSY 5D-(HA)CA(CO)NH

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Sample preparation

DetailsContents: 1.2 mM [U-98% 13C; U-98% 15N] protein, 50 mM sodium chloride, 20 mM sodium phosphate, 5 mM sodium azide, 90% H2O/10% D2O
Solvent system: 90% H2O/10% D2O
Sample
Conc. (mg/ml)ComponentIsotopic labelingSolution-ID
1.2 mMprotein-1[U-98% 13C; U-98% 15N]1
50 mMsodium chloride-21
20 mMsodium phosphate-31
5 mMsodium azide-41
Sample conditionsIonic strength: 0.24 / pH: 6 / Pressure: ambient / Temperature: 298 K

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker AvanceBrukerAVANCE6001
Bruker AvanceBrukerAVANCE8002

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Processing

NMR softwareName: CYANA / Developer: Guntert, P. et al. / Classification: refinement
RefinementMethod: molecular dynamics, Torsion Angle Dynamics / Software ordinal: 1
Details: SEMI-AUTOMATED STRUCTURE DETERMINATION WITH THE J-UNIO SUITE
NMR constraintsNOE constraints total: 1795 / NOE intraresidue total count: 428 / NOE long range total count: 535 / NOE medium range total count: 323 / NOE sequential total count: 509
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: target function / Conformers calculated total number: 80 / Conformers submitted total number: 20

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