BMRB Entry 16686
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16686
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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
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 428 |
| 15N chemical shifts | 101 |
| 1H chemical shifts | 689 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | lmr64a_protein | 1 |
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 | MET | ASP | THR | ASN | ASN | PHE | THR | VAL | LYS | VAL | ||||
| 2 | GLU | TYR | VAL | ASP | ALA | ASP | GLY | ALA | GLU | ILE | ||||
| 3 | ALA | PRO | SER | ASP | THR | LEU | THR | ASP | TYR | HIS | ||||
| 4 | TYR | VAL | SER | THR | PRO | LYS | ASP | ILE | PRO | GLY | ||||
| 5 | TYR | LYS | LEU | ARG | GLU | ILE | PRO | HIS | ASN | ALA | ||||
| 6 | THR | GLY | ASN | ILE | THR | ASP | THR | GLY | ILE | ILE | ||||
| 7 | VAL | ARG | TYR | ILE | TYR | ASP | LYS | ILE | ILE | ASP | ||||
| 8 | VAL | SER | TYR | VAL | ASP | GLU | THR | GLY | LYS | ASP | ||||
| 9 | LEU | LEU | PRO | VAL | VAL | GLU | ILE | ILE | ASN | SER | ||||
| 10 | GLU | ALA | ALA | VAL | LEU | GLU | HIS | HIS | HIS | HIS | ||||
| 11 | HIS | HIS |
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:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 1D 15N T1 | NC | isotropic | sample_conditions_1 |
| 1D 15N T2 | NC | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | NC | isotropic | sample_conditions_1 |
| 2D 1H-13C CT-HSQC aliphatic | NC | isotropic | sample_conditions_1 |
| 2D 1H-13C CT-HSQC aromatic | NC | isotropic | sample_conditions_1 |
| 3D HNCO | NC | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | NC | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | NC | isotropic | sample_conditions_1 |
| 3D HNCACB | NC | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | NC | isotropic | sample_conditions_1 |
| 3D (H)CCH-TOCSY aliphatic | NC | isotropic | sample_conditions_1 |
| 3D (H)CCH-COSY aliphatic | NC | isotropic | sample_conditions_1 |
| 3D (H)CCH-COSY aromatic | NC | isotropic | sample_conditions_1 |
| 3D 1H-15N,13C NOESY | NC | isotropic | sample_conditions_1 |
| 2D 1H-15N LR-HSQC (Histidine) | NC5 | isotropic | sample_conditions_1 |
| 2D 1H-13C CT-HSQC methyl | NC5 | isotropic | sample_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