BMRB Entry 16686

Name: Solution NMR structure of mucin-binding domain of protein lmo0835 from Listeria monocytogenes. Northeast Structural Genomics Consortium Target LmR64A
Published: 2010-02-25

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PDB ID: 2kt7
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
MolProbity Validation Chart

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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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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:

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:

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

Natural source:

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

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET 21-23C

Entity Sequences (FASTA):

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

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	428
15N chemical shifts	101
1H chemical shifts	689

Time Domain Data

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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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

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

7

VAL

ARG

TYR

ILE

TYR

ASP

LYS

ILE

ASP

8

VAL

SER

TYR

VAL

ASP

GLU

THR

GLY

LYS

ASP

9

LEU

PRO

VAL

GLU

ILE

ASN

SER

10

GLU

ALA

VAL

LEU

GLU

HIS

11

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

PDB	2KT7
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