BMRB Entry 16563

Name: Solution NMR structure of Lin0431 protein from Listeria innocua. Northeast Structural Genomics Consortium Target LkR112
Published: 2009-11-23

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PDB ID: 2kpp
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16563
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution NMR structure of Lin0431 protein from Listeria innocua. Northeast Structural Genomics Consortium Target LkR112

Deposition date:

2009-10-18

Original release date:

2009-11-23

Authors:

Tang, Yuefeng; Montelione, Gaetano; Ciccosanti, Colleen; Lee, Dan; Janjua, Haleema; Everett, John; Swapna, G.V.T.; Acton, Thomas; Rose, Burkhard; Xiao, Rong

Citation:

Citation: Tang, Yuefeng; Montelione, Gaetano; Ciccosanti, Colleen; Lee, Dan; Janjua, Haleema; Everett, John; Swapna, G.V.T.; Acton, Thomas; Rose, Burkhard; Xiao, Rong. "Solution NMR structure of Lin0431 protein from Listeria innocua. Northeast Structural Genomics Consortium Target LkR112" .

Assembly members:

Assembly members:
LkR112, polymer, 114 residues, 12784.5 Da.

Natural source:

Natural source: Common Name: Listeria innocua Taxonomy ID: 1642 Superkingdom: Eubacteria Kingdom: not available Genus/species: Listeria innocua

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: LkR112-36-140-21.21

Entity Sequences (FASTA):

Entity Sequences (FASTA):
LkR112: MKNTGDEVVAIISQNGKVIR EIPLTGHKGNEQFTIKGKGA QYNLMEVDGERIRIKEDNSP DQVGVKMGWKSKAGDTIVCL PHKVFVEIKSTQKDSKDPDT DLIVPNLEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	474
15N chemical shifts	117
1H chemical shifts	781

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	LkR112	1

Entities:

Entity 1, LkR112 114 residues - 12784.5 Da.

1

MET

LYS

ASN

THR

GLY

ASP

GLU

VAL

ALA

2

ILE

SER

GLN

ASN

GLY

LYS

VAL

ILE

ARG

3

GLU

ILE

PRO

LEU

THR

GLY

HIS

LYS

GLY

ASN

4

GLU

GLN

PHE

THR

ILE

LYS

GLY

LYS

GLY

ALA

5

GLN

TYR

ASN

LEU

MET

GLU

VAL

ASP

GLY

GLU

6

ARG

ILE

ARG

ILE

LYS

GLU

ASP

ASN

SER

PRO

7

ASP

GLN

VAL

GLY

VAL

LYS

MET

GLY

TRP

LYS

8

SER

LYS

ALA

GLY

ASP

THR

ILE

VAL

CYS

LEU

9

PRO

HIS

LYS

VAL

PHE

VAL

GLU

ILE

LYS

SER

10

THR

GLN

LYS

ASP

SER

LYS

ASP

PRO

ASP

THR

11

ASP

LEU

ILE

VAL

PRO

ASN

LEU

GLU

HIS

12

HIS

Samples:

sample_1: LkR112, [U-100% 13C; U-100% 15N], 0.851 mM; MES 20 mM; NaCl 200 mM; CaCl2 5 mM; DTT 10 mM; NaN3 0.02%; DSS 50 uM; H2O 95%; D2O 5%

sample_2: LkR112, [U-5% 13C; U-100% 15N], 0.887 mM; MES 20 mM; NaCl 200 mM; CaCl2 5 mM; DTT 10 mM; NaN3 0.02%; DSS 50 uM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 200 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
2D High Resolution 1H-13C HSQC	sample_2	isotropic	sample_conditions_1
2D aromatic 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HN(CO)CACB	sample_1	isotropic	sample_conditions_1
3D HCCH-COSY	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D CCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-13C aliphatic NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C aromatic NOESY	sample_1	isotropic	sample_conditions_1
3D simutaeous NOESY	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection

AutoAssign, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

SPARKY v3.110, Goddard - data analysis

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

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution

NMRPipe v2.3, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

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

PSVS, Bhattacharya and Montelione - structure validation

PDBStat v5.1, Tejero and Montelione - PDB analysis

NMR spectrometers:

Bruker Avance 800 MHz

PDB	2KPP
EMBL	CAC95664
GB	EFR91908 EFR94989 EHN61892 KJR52371 KJR53096
REF	WP_003760402