BMRB Entry 25125

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25125
MolProbity Validation Chart

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Title:
Solution Structure and Chemical Shift Assignments for the Apo form of the Receiver Domain of Nitrogen Regulatory Protein C ( NTRC ) at 35C
Deposition date:
2014-08-04
Original release date:
2015-06-29
Authors:
Clarkson, Michael; Pontiggia, Francesco; Villali, Janice; Kern, Dorothee
Citation:

Citation: Pontiggia, Francesco; Pachov, Dimitar; Clarkson, Michael; Villali, Janice; Hagan, Michael; Pande, Vijay; Kern, Dorothee. "Free energy landscape of activation in a signalling protein at atomic resolution"  Nat. Commun. 6, 7284-7284 (2015).
PubMed: 26073309

Assembly members:

Assembly members:
Receiver_Domain_of_NtrC, polymer, 124 residues, 13636.716 Da.

Natural source:

Natural source:   Common Name: enterobacteria   Taxonomy ID: 90371   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Salmonella typhimurium

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-7

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Receiver_Domain_of_NtrC: MQRGIVWVVDDDSSIRWVLE RALAGAGLTCTTFENGNEVL AALASKTPDVLLSDIRMPGM DGLALLKQIKQRHPMLPVII MTAHSDLDAAVSAYQQGAFD YLPKPFDIDEAVALVERAIS HYQE

Data sets:
Data typeCount
13C chemical shifts542
15N chemical shifts124
1H chemical shifts891

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 124 residues - 13636.716 Da.

1   METGLNARGGLYILEVALTRPVALVALASP
2   ASPASPSERSERILEARGTRPVALLEUGLU
3   ARGALALEUALAGLYALAGLYLEUTHRCYS
4   THRTHRPHEGLUASNGLYASNGLUVALLEU
5   ALAALALEUALASERLYSTHRPROASPVAL
6   LEULEUSERASPILEARGMETPROGLYMET
7   ASPGLYLEUALALEULEULYSGLNILELYS
8   GLNARGHISPROMETLEUPROVALILEILE
9   METTHRALAHISSERASPLEUASPALAALA
10   VALSERALATYRGLNGLNGLYALAPHEASP
11   TYRLEUPROLYSPROPHEASPILEASPGLU
12   ALAVALALALEUVALGLUARGALAILESER
13   HISTYRGLNGLU

Samples:

sample_1: Receiver Domain of NtrC, [U-100% 13C; U-100% 15N], 1 mM; sodium phosphate 50 mM; sodium chloride 50 mM; H2O 93%; D2O 7%

sample_conditions_1: ionic strength: 50 mM; pH: 6.75; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH3-TOCSYsample_1isotropicsample_conditions_1
2D (HB)CB(CGCD)HDsample_1isotropicsample_conditions_1
2D (HB)CB(CGCDCE)HEsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

CARA, Professor Kurt W thrich - chemical shift assignment

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

TALOS, Cornilescu, Delaglio and Bax - data analysis

NMR spectrometers:

  • Agilent INOVA 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

BMRB 25124 4527 4528
PDB
DBJ BAB38213 BAE77441 BAG79675 BAI27885 BAI33008
EMBL CAA28808 CAA59425 CAD03095 CAP78325 CAQ34219
GB AAB03002 AAC76865 AAG59057 AAL22844 AAN45373
PIR AC0950 E86074
REF NP_312817 NP_418304 NP_458044 NP_462885 NP_709666
SP P0AFB8 P0AFB9 P41789
AlphaFold P0AFB8 P0AFB9 P41789

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