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 17403

Title: 1H, 15N and 13C resonance assignment of the N-terminal C39-peptidase like domain of the ABC transporter Haemolysin B (HlyB)   PubMed: 21347827

Deposition date: 2011-01-10 Original release date: 2011-03-07

Authors: Lecher, Justin; Willbold, Dieter; Stoldt, Matthias; Schmitt, Lutz; Smits, Sander; Schwarz, Christian

Citation: Lecher, Justin; Stoldt, Matthias; Schwarz, Christian; Smits, Sander; Schmitt, Lutz; Willbold, Dieter. "1H, 15N and 13C resonance assignment of the N-terminal C39 peptidase-like domain of the ABC transporter Haemolysin B (HlyB)."  Biomol. NMR Assignments 5, 199-201 (2011).

Assembly members:
HlyB_C39_domain, polymer, 142 residues, 16089.4973 Da.

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET22a

Entity Sequences (FASTA):
HlyB_C39_domain: GAMANSDSCHKIDYGLYALE ILAQYHNVSVNPEEIKHRFD TDGTGLGLTSWLLAAKSLEL KVKQVKKTIDRLNFISLPAL VWREDGRHFILTKVSKEANR YLIFDLEQRNPRVLEQSEFE ALYQGHIILIASRSSVAGKL AK

Data sets:
Data typeCount
13C chemical shifts657
15N chemical shifts169
1H chemical shifts1069

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1C39-1371

Entities:

Entity 1, C39-137 142 residues - 16089.4973 Da.

1   GLYALAMETALAASNSERASPSERCYSHIS
2   LYSILEASPTYRGLYLEUTYRALALEUGLU
3   ILELEUALAGLNTYRHISASNVALSERVAL
4   ASNPROGLUGLUILELYSHISARGPHEASP
5   THRASPGLYTHRGLYLEUGLYLEUTHRSER
6   TRPLEULEUALAALALYSSERLEUGLULEU
7   LYSVALLYSGLNVALLYSLYSTHRILEASP
8   ARGLEUASNPHEILESERLEUPROALALEU
9   VALTRPARGGLUASPGLYARGHISPHEILE
10   LEUTHRLYSVALSERLYSGLUALAASNARG
11   TYRLEUILEPHEASPLEUGLUGLNARGASN
12   PROARGVALLEUGLUGLNSERGLUPHEGLU
13   ALALEUTYRGLNGLYHISILEILELEUILE
14   ALASERARGSERSERVALALAGLYLYSLEU
15   ALALYS

Samples:

Uniform_15N13C: C39-137, [U-13C; U-15N], 2.0 mM; H2O, [U-13C; U-15N], 93%; D2O, [U-13C; U-15N], 7%

Uniform_15N: C39-137, [U-15N], 2.5 mM; H2O, [U-15N], 93%; D2O, [U-15N], 7%

Uniform_15N13C_deuterated_buffer: C39-137, [U-13C; U-15N], 2.5 mM; H2O, [U-13C; U-15N], 93%; D2O, [U-13C; U-15N], 7%

Uniform_15N13C_deuterated_buffer-D2O: C39-137, [U-13C; U-15N], 2.5 mM; D2O, [U-13C; U-15N], 100%

standard: ionic strength: 0.200 M; pH: 6.000; pressure: 1.000 atm; temperature: 303.000 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCUniform_15Nisotropicstandard
3D CBCA(CO)NHUniform_15N13Cisotropicstandard
3D HBHA(CO)NHUniform_15N13Cisotropicstandard
3D HNHAUniform_15Nisotropicstandard
3D HNCOUniform_15N13Cisotropicstandard
3D HNCACBUniform_15N13Cisotropicstandard
3D H(CCO)NHUniform_15N13Cisotropicstandard
3D C(CO)NHUniform_15N13Cisotropicstandard
3D HCCH-COSYUniform_15N13C_deuterated_bufferisotropicstandard
2D 1H-15N HMQCUniform_15Nisotropicstandard
2D 1H-13C HSQC aromaticUniform_15N13C_deuterated_bufferisotropicstandard
2D 1H-13C HSQC aliphaticUniform_15N13C_deuterated_buffer-D2Oisotropicstandard
3D 1H-15N NOESYUniform_15Nisotropicstandard
3D 1H-13C NOESY aliphaticUniform_15N13C_deuterated_bufferisotropicstandard
3D 1H-13C NOESY aromaticUniform_15N13C_deuterated_bufferisotropicstandard

Software:

AZARA v2.8, Wayne Boucher - processing

ANALYSIS v2.1, CCPN - assignment, data evaluation

NMRPipe v5.4.2010.250.17.50, NIH - conversion, processing

VnmrJ v2.3A, Agilent Technologies (formerly Varian) - data recording, spectrometer operation

NMR spectrometers:

  • Varian VNMRS 900 MHz
  • Varian VNMRS 800 MHz

Related Database Links:

UNP Q47258
PDB
EMBL CAD33760 CAD42038 CAK02716 CAM84370 CAM84374
GB AAA23976 AAA23978 AAN82021 ABE10328 ABG71799
REF WP_000376537 WP_000376540 WP_000376541 WP_000376543 WP_000376544
SP P10089 Q47258 Q8FDZ8

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