BMRB Entry 17234

Name: NMR structure of the DNA-binding domain of E.coli Lrp
Published: 2011-02-24

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PDB ID: 2l4a
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17234
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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

NMR structure of the DNA-binding domain of E.coli Lrp

Deposition date:

2010-10-01

Original release date:

2011-02-24

Authors:

Kawamura, Tetsuya; Zhou, Hongjun; Dahlquist, Frederick

Citation:

Citation: Kawamura, Tetsuya; Vartanian, Armand; Zhou, Hongjun; Dahlquist, Frederick. "The Design Involved in PapI and Lrp Regulation of the pap Operon." J. Mol. Biol. 409, 311-332 (2011).
PubMed: 21338611

Assembly members:

Assembly members:
Lrp_DNA-binding_domain, polymer, 66 residues, 7621.872 Da.

Natural source:

Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: bacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28b(+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Lrp_DNA-binding_domain: MVDSKKRPGKDLDRIDRNIL NELQKDGRISNVELSKRVGL SPTPCLERVRRLERQGFIQG YTALLN

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	275
15N chemical shifts	62
1H chemical shifts	451

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Lrp_DNA-binding_domain	1

Entities:

Entity 1, Lrp_DNA-binding_domain 66 residues - 7621.872 Da.

1

MET

VAL

ASP

SER

LYS

ARG

PRO

GLY

LYS

2

ASP

LEU

ASP

ARG

ILE

ASP

ARG

ASN

ILE

LEU

3

ASN

GLU

LEU

GLN

LYS

ASP

GLY

ARG

ILE

SER

4

ASN

VAL

GLU

LEU

SER

LYS

ARG

VAL

GLY

LEU

5

SER

PRO

THR

PRO

CYS

LEU

GLU

ARG

VAL

ARG

6

ARG

LEU

GLU

ARG

GLN

GLY

PHE

ILE

GLN

GLY

7

TYR

THR

ALA

LEU

ASN

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 CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
4D 15N-13C edited NOESY	sample_1	isotropic	sample_conditions_1
4D 13C-131C edited NOESY	sample_2	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_3	isotropic	sample_conditions_1

PDB	2GQQ 2L4A
DBJ	BAA01880 BAA35614 BAB34397 BAE74382 BAG76471
EMBL	CAA76565 CAD05359 CAG75548 CAP75362 CAQ31417
GB	AAA24089 AAA75439 AAA75465 AAA75466 AAA75467
PIR	AE0611
REF	NP_309001 NP_415409 NP_455447 NP_459935 NP_706774
SP	P0A2S0 P0ACJ0 P0ACJ1 P0ACJ2 P0ACJ3
AlphaFold	P0A2S0 P0ACJ0 P0ACJ1 P0ACJ2 P0ACJ3

BMRB Entry 17234

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

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