BMRB Entry 15213

Name: Assignments of {lambda}-IntCB bound to a DNA half-site
Published: 2008-02-11

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15213

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Assignments of {lambda}-IntCB bound to a DNA half-site

Deposition date:

2007-04-16

Original release date:

2008-02-11

Authors:

Kamadurai, Hari; Foster, Mark

Citation:

Citation: Kamadurai, Hari; Foster, Mark. "DNA recognition via mutual-induced fit by the core-binding domain of bacteriophage lambda integrase." Biochemistry 46, 13939-13947 (2007).
PubMed: 18001133

Assembly members:

Assembly members:
Protein, polymer, 86 residues, Formula weight is not available
DNA, polymer, 15 residues, Formula weight is not available

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: pT7

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Protein: TLHSWLDRYEKIASRGIKQK TINYMSKIAIRRGLDATTKE IAANGYIDEGKAASKLIRST LSDAFRAEGHITTHVAATRA AKSEVR
DNA: GCTCAAGGGAGTACG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	220
15N chemical shifts	86
1H chemical shifts	86

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	IntCB	1
2	DNA	2

Entities:

Entity 1, IntCB 86 residues - Formula weight is not available

1

THR

LEU

HIS

SER

TRP

LEU

ASP

ARG

TYR

GLU

2

LYS

ILE

ALA

SER

ARG

GLY

ILE

LYS

GLN

LYS

3

THR

ILE

ASN

TYR

MET

SER

LYS

ILE

ALA

ILE

4

ARG

GLY

LEU

ASP

ALA

THR

LYS

GLU

5

ILE

ALA

ASN

GLY

TYR

ILE

ASP

GLU

GLY

6

LYS

ALA

SER

LYS

LEU

ILE

ARG

SER

THR

7

LEU

SER

ASP

ALA

PHE

ARG

ALA

GLU

GLY

HIS

8

ILE

THR

HIS

VAL

ALA

THR

ARG

ALA

9

ALA

LYS

SER

GLU

VAL

ARG

Entity 2, DNA 15 residues - Formula weight is not available

1

DG

DC

DT

DC

DA

DG

DA

2

DG

DT

DA

DC

DG

Samples:

sample_1: Protein, [U-99% 13C; U-99% 15N], 1 mM; DNA 1 mM; TSP 0.02%; sodium phosphate 25 mM; sodium azide 0.02%; D2O 10%

sample_conditions_1: ionic strength: 0.05 M; pH: 7.2; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	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 HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - chemical shift assignment, processing

NMR spectrometers:

Bruker DRX 600 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks