BMRB Entry 15609

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15609
MolProbity Validation Chart

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Title:
solution structure of 50S ribosomal protein L28 from Thermotoga maritima: Northeast Structural Genomics consortium target VR97
Deposition date:
2007-12-28
Original release date:
2008-01-25
Authors:
Wu, Yibing; Singarapu, Kiran Kumar; Guido, Valerie; Yee, Adelinda; Sukumaran, Dinesh; Arrowsmith, Cheryl; Szyperski, Thomas
Citation:

Citation: Wu, Yibing; Singarapu, Kiran Kumar; Guido, Valerie; Yee, Adelinda; Sukumaran, Dinesh; Arrowsmith, Cheryl; Szyperski, Thomas. "solution structure of 50S ribosomal protein L28 from Thermotoga maritima: Northeast Structural Genomics consortium target VR97"  .

Assembly members:

Assembly members:
ribosomal protein L28, polymer, 77 residues, 8612.257 Da.

Natural source:

Natural source:   Common Name: Thermotoga maritima   Taxonomy ID: 2336   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Thermotoga maritima

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET21

Entity Sequences (FASTA):

Entity Sequences (FASTA):
ribosomal protein L28: QGHMIMAKRCEVCGKAPRSG NTVSHSDKKSERWFRPNLQK VRVVLPDGTIKRMRVCTSCL KSGKVKKYVGQVSEVGS

Data sets:
Data typeCount
13C chemical shifts210
15N chemical shifts61
1H chemical shifts440

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1ribosomal protein L281

Entities:

Entity 1, ribosomal protein L28 77 residues - 8612.257 Da.

1   GLNGLYHISMETILEMETALALYSARGCYS
2   GLUVALCYSGLYLYSALAPROARGSERGLY
3   ASNTHRVALSERHISSERASPLYSLYSSER
4   GLUARGTRPPHEARGPROASNLEUGLNLYS
5   VALARGVALVALLEUPROASPGLYTHRILE
6   LYSARGMETARGVALCYSTHRSERCYSLEU
7   LYSSERGLYLYSVALLYSLYSTYRVALGLY
8   GLNVALSERGLUVALGLYSER

Samples:

sample_1: entity 1.0 mM; NaCl 300 mM; D2O, [U-100% 2H], 10%; H2O 90%

sample_conditions_1: ionic strength: 0.3 M; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
4,3D, GFT HNNCABCAsample_1isotropicsample_conditions_1
4,3D, GFT CABCACONNHsample_1isotropicsample_conditions_1
4,3D, GFT HCCH COSYsample_1isotropicsample_conditions_1
3D, 15N-13C RESOLVEDSIMULTANIOUS NOESYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

AutoAssign, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

XEASY, Bartels et al. - peak picking

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

AutoStruct, Huang, Tejero, Powers and Montelione - structure solution

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

  • Varian INOVA 750 MHz
  • Varian INOVA 600 MHz

Related Database Links:

PDB
GB AAD35344 ABQ46689 ACB09046 ADA66976 AGL49179
REF NP_228069 WP_010865082 WP_015646089
SP B1L9P8 Q9WY96
AlphaFold B1L9P8 Q9WY96

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks