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 16686

Title: Solution NMR structure of mucin-binding domain of protein lmo0835 from Listeria monocytogenes. Northeast Structural Genomics Consortium Target LmR64A

Deposition date: 2010-01-20 Original release date: 2010-02-25

Authors: Eletsky, Alexander; He, Yunfen; Lee, Dan; Ciccosanti, Colleen; Janjua, Haleema; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Szyperski, Thomas

Citation: Eletsky, Alexander; He, Yunfen; Lee, Dan; Ciccosanti, Colleen; Janjua, Haleema; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Szyperski, Thomas. "Solution NMR structure of mucin-binding domain of protein lmo0835 from Listeria monocytogenes."  Proteins: Struct. Funct. Genet. ., .-..

Assembly members:
lmr64a_protein, polymer, 102 residues, 11501.830 Da.

Natural source:   Common Name: Listeria monocytogenes   Taxonomy ID: 1639   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Listeria monocytogenes

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

Entity Sequences (FASTA):
lmr64a_protein: MDTNNFTVKVEYVDADGAEI APSDTLTDYHYVSTPKDIPG YKLREIPHNATGNITDTGII VRYIYDKIIDVSYVDETGKD LLPVVEIINSEAAVLEHHHH HH

Data sets:
Data typeCount
13C chemical shifts428
15N chemical shifts101
1H chemical shifts689

Time Domain Data

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1lmr64a_protein1

Entities:

Entity 1, lmr64a_protein 102 residues - 11501.830 Da.

Residues 35-127 correspond to the fragment 34-126 of the published native sequence, with the exception of strain variations I58T, T101I and R105S. Residues 128-133 represent a non-native affinity tag, and methionine at position 34 was introduced to promote expression.

1   METASPTHRASNASNPHETHRVALLYSVAL
2   GLUTYRVALASPALAASPGLYALAGLUILE
3   ALAPROSERASPTHRLEUTHRASPTYRHIS
4   TYRVALSERTHRPROLYSASPILEPROGLY
5   TYRLYSLEUARGGLUILEPROHISASNALA
6   THRGLYASNILETHRASPTHRGLYILEILE
7   VALARGTYRILETYRASPLYSILEILEASP
8   VALSERTYRVALASPGLUTHRGLYLYSASP
9   LEULEUPROVALVALGLUILEILEASNSER
10   GLUALAALAVALLEUGLUHISHISHISHIS
11   HISHIS

Samples:

NC: lmr64a_protein, [U-13C; U-15N], 0.9 mM; MES 20 mM; sodium chloride 100 mM; calcium chloride 5 mM; sodium azide 0.01%; H2O 95%; D2O 5%

NC5: lmr64a_protein, [U-5% 13C; U-15N], 0.9 mM; MES 20 mM; sodium chloride 100 mM; calcium chloride 5 mM; sodium azide 0.01%; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 225 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
1D 15N T1NCisotropicsample_conditions_1
1D 15N T2NCisotropicsample_conditions_1
2D 1H-15N HSQCNCisotropicsample_conditions_1
2D 1H-13C CT-HSQC aliphaticNCisotropicsample_conditions_1
2D 1H-13C CT-HSQC aromaticNCisotropicsample_conditions_1
3D HNCONCisotropicsample_conditions_1
3D CBCA(CO)NHNCisotropicsample_conditions_1
3D HN(CA)CONCisotropicsample_conditions_1
3D HNCACBNCisotropicsample_conditions_1
3D HBHA(CO)NHNCisotropicsample_conditions_1
3D (H)CCH-TOCSY aliphaticNCisotropicsample_conditions_1
3D (H)CCH-COSY aliphaticNCisotropicsample_conditions_1
3D (H)CCH-COSY aromaticNCisotropicsample_conditions_1
3D 1H-15N,13C NOESYNCisotropicsample_conditions_1
2D 1H-15N LR-HSQC (Histidine)NC5isotropicsample_conditions_1
2D 1H-13C CT-HSQC methylNC5isotropicsample_conditions_1

Software:

VNMRJ v2.1B, Varian - collection

PROSA v6.4, Guntert - processing

CARA v1.8.4, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking

PINE v1.0, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

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

AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - structure solution

TALOS+ v1.2009.0721.18, Shen, Cornilescu, Delaglio and Bax - data analysis

CNS v1.2.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

PSVS v1.4, Bhattacharya and Montelione - validation

NMR spectrometers:

  • Varian INOVA 500 MHz
  • Varian INOVA 750 MHz

Related Database Links:

PDB
DBJ GAM91864 GAM94621
EMBL CAS04619 CBY03397 CBY48425 CBY66913 CBY69752
GB AAT03632 ABN80104 AFH79417 AGR06974 AGR12775
REF WP_003733401 WP_003743756 WP_010958814 WP_012681181 WP_021496215

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