BMRB Entry 18200

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18200
MolProbity Validation Chart

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Title:
Resonance assignments for C-terminal DNA-binding domain of RstA protein from Klebsiella pneumonia
Deposition date:
2012-01-17
Original release date:
2012-05-08
Authors:
Chen, Sheng-Chia; Fang, Pei-Ju; Cheng, Ya-Hsin; Chang, Chi-Fon; Yu, Tsunai; Huang, Tai-huang
Citation:

Citation: Chen, Sheng-Chia; Chang, Chi-Fon; Fan, Pei-Ju; Cheng, Ya-Hsin; Yu, Tsunai; Huang, Tai-Huang. "(1)H, (13)C and (15)N resonance assignments of the C-terminal DNA-binding domain of RstA protein from Klebsiella pneumoniae."  Biomol. NMR Assignments 7, 85-88 (2013).
PubMed: 22481468

Assembly members:

Assembly members:
RstA_C, polymer, 119 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Klebsiella pneumonia   Taxonomy ID: 573   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Klebsiella pneumonia

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: BL21

Entity Sequences (FASTA):

Entity Sequences (FASTA):
RstA_C: MHHHHHHAMGTLTPHKTISF GSLTIDPVNRQVLLGGENVA LSTADFDLLWELATHAGQIM DRDALLKNLRGVTYDGMDRS VDVAISRLRKKLLDNATEPY RIKTVRNKGYLFAPHAWDN

Data sets:
Data typeCount
13C chemical shifts389
15N chemical shifts103
1H chemical shifts681

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1RstA_C1

Entities:

Entity 1, RstA_C 119 residues - Formula weight is not available

1   METHISHISHISHISHISHISALAMETGLY
2   THRLEUTHRPROHISLYSTHRILESERPHE
3   GLYSERLEUTHRILEASPPROVALASNARG
4   GLNVALLEULEUGLYGLYGLUASNVALALA
5   LEUSERTHRALAASPPHEASPLEULEUTRP
6   GLULEUALATHRHISALAGLYGLNILEMET
7   ASPARGASPALALEULEULYSASNLEUARG
8   GLYVALTHRTYRASPGLYMETASPARGSER
9   VALASPVALALAILESERARGLEUARGLYS
10   LYSLEULEUASPASNALATHRGLUPROTYR
11   ARGILELYSTHRVALARGASNLYSGLYTYR
12   LEUPHEALAPROHISALATRPASPASN

Samples:

sample_1: RstA_C, [U-13C; U-15N], 0.1-1.0 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

CARA, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
DBJ BAH63203 BAS35643
EMBL CCI77052 CCM80542 CCM87616 CCM95853 CCN29569
GB ABR76952 ACI11717 ADC58723 AEJ97988 AEW61123
REF WP_002903377 WP_008805070 WP_017898700 WP_020313713 WP_021440054

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