BMRB Entry 5390

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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/BMR5390
MolProbity Validation Chart

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Title:
1H,13C and 15N Chemical Shifts Assignments for the Oligomerization Domain of H-NS
Deposition date:
2002-06-12
Original release date:
2003-02-25
Authors:
Esposito, D.; Petrovic, A.; Harris, R.; Shusuke, O.; Eccleston, J.; Mbabaali, A.; Haq, I.; Higgins, C.; Hinton, J.; Driscoll, P.; Ladbury, J.
Citation:

Citation: Esposito, D.; Petrovic, A.; Harris, R.; Ono, S.; Eccleston, J.; Mbabaali, A.; Haq, I.; Higgins, C.; Hinton, J.; Driscoll, P.; Ladbury, J.. "H-NS Oligomerization Domain Structure Reveals the Mechanism for High Order Self-association of the Intact Protein"  J. Mol. Biol. 324, 841-850 (2002).
PubMed: 12460581

Assembly members:

Assembly members:
H-NS, polymer, 61 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Eubacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology

Entity Sequences (FASTA):

Entity Sequences (FASTA):
H-NS: GSHMSEALKILNNIRTLRAQ ARESTLETLEEMLEKLEVVV NERREEESAAAAEVEERTRK L

Data sets:
Data typeCount
1H chemical shifts366
13C chemical shifts193
15N chemical shifts62

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1dna-binding protein h-ns, chain A1
2dna-binding protein h-ns, chain B1

Entities:

Entity 1, dna-binding protein h-ns, chain A 61 residues - Formula weight is not available

1   GLYSERHISMETSERGLUALALEULYSILE
2   LEUASNASNILEARGTHRLEUARGALAGLN
3   ALAARGGLUSERTHRLEUGLUTHRLEUGLU
4   GLUMETLEUGLULYSLEUGLUVALVALVAL
5   ASNGLUARGARGGLUGLUGLUSERALAALA
6   ALAALAGLUVALGLUGLUARGTHRARGLYS
7   LEU

Samples:

sample_1: H-NS, [U-15N], 1.5 mM; NaCl 300 mM; potassium phosphate 20 mM; EDTA 1 mM

sample_2: H-NS, [U-13C; U-15N], 1.5 mM; NaCl 300 mM; potassium phosphate 20 mM; EDTA 1 mM

sample_3: H-NS, [U-13C; U-15N], 1.0 mM; H-NS 1.0 mM; NaCl 300 mM; potassium phosphate 20 mM; EDTA 1 mM

sample_cond_1: pH: 7.0; temperature: 298 K; ionic strength: 300 mM; pressure: 1 atm

Experiments:

NameSampleSample stateSample conditions
3D 15N-separated NOESYnot availablenot availablenot available
3D 13C-separated NOESYnot availablenot availablenot available
3D 13C F1-filtered F3-edited NOESY-HSQCnot availablenot availablenot available

Software:

AZARA v2.6 - processing

ANSIG v3.3 - data analysis

CNS v1.1 - structure solution, refinement

NMR spectrometers:

  • Bruker AVANCE 800 MHz

Related Database Links:

BMRB 18814 4802
PDB
DBJ BAA36117 BAB35162 BAG76811 BAI25048 BAI30173
EMBL CAA30530 CAA32549 CAA40507 CAA42565 CAA47322
GB AAB61148 AAC74319 AAG56094 AAL20669 AAN42850
PIR AC0650
PRF 1607341A
REF NP_287482 NP_309766 NP_415753 NP_455749 NP_460710
SP P09120 P0A1S2 P0A1S3 P0ACF8 P0ACF9
AlphaFold P09120 P0A1S2 P0A1S3 P0ACF8 P0ACF9

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