BMRB Entry 17038

Name: Solution NMR Structure of protein STY4237 (residues 36-120) from Salmonella enterica, Northeast Structural Genomics Consortium Target SlR115
Published: 2010-08-24

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PDB ID: 2l0c
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17038
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution NMR Structure of protein STY4237 (residues 36-120) from Salmonella enterica, Northeast Structural Genomics Consortium Target SlR115

Deposition date:

2010-06-30

Original release date:

2010-08-24

Authors:

Cort, John; Lee, D.; Ciccosanti, C.; Janjua, H.; Acton, T.; Xiao, R.; Everett, J.; Montelione, G.; Ramelot, T.; KENNEDY, M.

Citation:

Citation: Cort, John; Lee, Dan; Ciccosanti, Colleen; Janjua, Haleema; Acton, T.; Xiao, R.; Everett, J.; Montelione, G.; KENNEDY, M.. "Northeast Structural Genomics Consortium Target SlR115" To be published ., .-..

Assembly members:

Assembly members:
SlR115, polymer, 97 residues, 11129.551 Da.

Natural source:

Natural source: Common Name: Salmonella enterica Taxonomy ID: 28901 Superkingdom: Bacteria Kingdom: not available Genus/species: Salmonella enterica

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET21-23C

Entity Sequences (FASTA):

Entity Sequences (FASTA):
SlR115: MAPLQQKQVVVSNKREKPVN DRRSRQQEVSPAGTSMRYEA SFKPLNGGLEKTFRLQAQQY HALTVGDQGTLSYKGTRFVG FVSRTPDNELEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
spectral_peak_list

Data type	Count
13C chemical shifts	390
15N chemical shifts	96
1H chemical shifts	582

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	SlR115	1

Entities:

Entity 1, SlR115 97 residues - 11129.551 Da.

residue 2 of the structure corresponds to residue 36 of the sequence.

1

MET

ALA

PRO

LEU

GLN

LYS

GLN

VAL

2

VAL

SER

ASN

LYS

ARG

GLU

LYS

PRO

VAL

ASN

3

ASP

ARG

SER

ARG

GLN

GLU

VAL

SER

4

PRO

ALA

GLY

THR

SER

MET

ARG

TYR

GLU

ALA

5

SER

PHE

LYS

PRO

LEU

ASN

GLY

LEU

GLU

6

LYS

THR

PHE

ARG

LEU

GLN

ALA

GLN

TYR

7

HIS

ALA

LEU

THR

VAL

GLY

ASP

GLN

GLY

THR

8

LEU

SER

TYR

LYS

GLY

THR

ARG

PHE

VAL

GLY

9

PHE

VAL

SER

ARG

THR

PRO

ASP

ASN

GLU

LEU

10

GLU

HIS

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
3D HNCO	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D 1H-13C arom NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C aliph NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
4D 1H-13C-13C-1H HMQC NOESY	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_3	isotropic	sample_conditions_1

PDB	2L0C
DBJ	BAJ38571 BAP09540
EMBL	CAD08056 CAR34973 CAR39639 CAR61453 CBG26565
GB	AAL22434 AAO71419 AAV79236 AAX67409 ACF62437
PIR	AD0991
REF	NP_458347 NP_462475 WP_000042846 WP_000042847 WP_000042849

BMRB Entry 17038

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

Related Database Links: