BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 15190

Title: Solution Structure of Protein HP0495 from H. pylori; Northeast structural genomics consortium target PT2; Ontario Centre for Structural Proteomics target HP0488

Deposition date: 2007-03-19 Original release date: 2009-06-15

Authors: Gutmanas, Aleksandras; Lemak, Alexander; Yee, Adelinda; Karra, Murthy; Srisailam, Sampath; Semesi, Anthony; Arrowsmith, Cheryl

Citation: Gutmanas, Aleksandras; Lemak, Alexander; Yee, Adelinda; Karra, Murthy; Srisailam, Sampath; Semesi, Anthony; Arrowsmith, Cheryl. "Solution Structure of Protein HP0495 from H. pylori"  The BMRB entry is the only known published source for the data..

Assembly members:
HP0495, polymer, 91 residues, 10677.271 Da.

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

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

Entity Sequences (FASTA):
HP0495: QGHMPSDSKKPTIIYPCLWD YRVIMTTKDTSTLKELLETY QRPFKLEFKNTSKNAKFYSF NVSMEVSNESERNEIFQKIS QLDKVVQTLGS

Data sets:
Data typeCount
13C chemical shifts413
15N chemical shifts91
1H chemical shifts653

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1HP04951

Entities:

Entity 1, HP0495 91 residues - 10677.271 Da.

Residues 1-3 are from a non-native N-terminal affinity tag; Residues 90-91 are from non-native C-terminal affinity tag

1   GLNGLYHISMETPROSERASPSERLYSLYS
2   PROTHRILEILETYRPROCYSLEUTRPASP
3   TYRARGVALILEMETTHRTHRLYSASPTHR
4   SERTHRLEULYSGLULEULEUGLUTHRTYR
5   GLNARGPROPHELYSLEUGLUPHELYSASN
6   THRSERLYSASNALALYSPHETYRSERPHE
7   ASNVALSERMETGLUVALSERASNGLUSER
8   GLUARGASNGLUILEPHEGLNLYSILESER
9   GLNLEUASPLYSVALVALGLNTHRLEUGLY
10   SER

Samples:

sample_1: HP0495, [U-13C; U-15N], 0.5 mM; TRIS 10 mM; sodium chloride 300 mM; benzamidine 1 mM; DTT 10 mM; sodium azide 0.01%; H2O 95%; D2O 5%

sample_2: HP0495, [U-13C; U-15N], 0.5 mM; TRIS 10 mM; sodium chloride 300 mM; benzamidine 1 mM; DTT 10 mM; sodium azide 0.01%; D2O 100%

sample_conditions_1: ionic strength: 300 mM; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCO sparsesample_1isotropicsample_conditions_1
3D HNCA sparsesample_1isotropicsample_conditions_1
3D H(CCCO)NH-TOCSY sparsesample_1isotropicsample_conditions_1
3D (H)C(CCO)NH-TOCSYsample_1isotropicsample_conditions_1
4D HBHACBCA(CO)NH PRsample_1isotropicsample_conditions_1
4D HC(CCO)NH-TOCSY PRsample_1isotropicsample_conditions_1
3D 1H-15N NOESY sparsesample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D H(C)CH-TOCSY sparsesample_2isotropicsample_conditions_1
3D (H)CCH-TOCSY sparsesample_2isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY sparsesample_2isotropicsample_conditions_1
3D H(C)CH-TOCSY aromatic, sparsesample_2isotropicsample_conditions_1
3D (H)CCH-TOCSY aromaticsample_2isotropicsample_conditions_1
2D CT 1H-13C HSQCsample_2isotropicsample_conditions_1
2D CT 1H-13C HSQC aromaticsample_2isotropicsample_conditions_1

Software:

CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

SPARKY, Goddard - peak picking

TALOS, Cornilescu, Delaglio and Bax - dihedral angle constraints prediction

ABACUS, A. Lemak, A. Grishaev, M. Llinas, CH Arrowsmith - chemical shift and NOE assignment

MDD/MDDgui, A. Gutmanas, CH Arrowsmith, I Ibraghimov, V Yu Orekhov - processing of non-uniformly sampled data

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

PR, M Karra, CH Arrowsmith - processing of Projection-Reconstruction spectra

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz
  • Varian INOVA 500 MHz

Related Database Links:

BMRB 15101
PDB
GB AAD07569 ADU82921 AFV41714 AFV43308 AFV44901
REF NP_207292 WP_001138777 WP_001138778
SP O25237

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts