BMRB Entry 15761

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15761

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Title:
Chemical shift assignments for JHP0511 (HP0564) from Helicobacter pylori.
Deposition date:
2008-05-06
Original release date:
2008-07-28
Authors:
Borin, Brendan
Citation:

Citation: Borin, Brendan; Krezel, Andrzej. "Structure of HP0564 from Helicobacter pylori identifies it as a new transcriptional regulator"  Proteins 73, 265-268 (2008).
PubMed: 18623065

Assembly members:

Assembly members:
JHP0511, polymer, 66 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Helicobacter pylori   Taxonomy ID: 210   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Helicobacter pylori

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
JHP0511: MRGSHHHHHHGSKRNFSVTF YLSKEEHDVLRRLADEEVES VNSFVKRHILKTIIYKKGTN QDSSIN

Data sets:
Data typeCount
13C chemical shifts242
15N chemical shifts56
1H chemical shifts362

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1subunit 11
2subunit 21

Entities:

Entity 1, subunit 1 66 residues - Formula weight is not available

Residues 1-12 represent a non-native purification tag. The rest of the sequence represents residues 21-74 of JHP0511.

1   METARGGLYSERHISHISHISHISHISHIS
2   GLYSERLYSARGASNPHESERVALTHRPHE
3   TYRLEUSERLYSGLUGLUHISASPVALLEU
4   ARGARGLEUALAASPGLUGLUVALGLUSER
5   VALASNSERPHEVALLYSARGHISILELEU
6   LYSTHRILEILETYRLYSLYSGLYTHRASN
7   GLNASPSERSERILEASN

Samples:

sample_1: JHP0511 1 mM; potassium phosphate 50 mM; D2O 10%; H2O 90%

sample_2: JHP0511, [U-100% 15N], 1 mM; potassium phosphate 50 mM; D2O 10%; H2O 90%

sample_3: JHP0511, [U-100% 13C; U-100% 15N], 1 mM; potassium phosphate 50 mM; D2O 10%; H2O 90%

sample_conditions_1: ionic strength: 50 mM; pH: 4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_3isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_3isotropicsample_conditions_1
3D C(CO)NHsample_3isotropicsample_conditions_1
3D HNCOsample_3isotropicsample_conditions_1
3D H(CCO)NHsample_3isotropicsample_conditions_1
3D HCCH-TOCSYsample_3isotropicsample_conditions_1

Software:

xwinnmr, Bruker Biospin - processing

SPARKY, Goddard - peak picking

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

AMBER, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - geometry optimization

ProcheckNMR, Laskowski and MacArthur - structure checking

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
DBJ BAM96488 BAM98200 BAO98238
EMBL CAX29340
GB AAD06087 ACI27284 ACJ07724 ACX97959 ACX99372
REF NP_207359 WP_000418252 WP_000418864 WP_000418865 WP_000418866

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