BMRB Entry 27041

Name: Backbone 1H, 13C, and 15N and partial sidechain 1H and 13C Chemical Shift
Published: 2017-06-06

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27041

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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:

Backbone 1H, 13C, and 15N and partial sidechain 1H and 13C Chemical Shift

Deposition date:

2017-03-05

Original release date:

2017-06-06

Authors:

Forcada-Nadal, Alicia; Palomino-Schaetzlein, Martina; Neira, Jose Luis; Pineda-Lucena, Antonio; Rubio, Vicente

Citation:

Citation: Forcada-Nadal, Alicia; Palomino-Schaetzlein, Martina; Neira, Jose Luis; Pineda-Lucena, Antonio; Rubio, Vicente. "The PipX protein, when not bound to its targets, has its signalling C-terminal helix in a flexed conformation" Biochemistry 56, 3211-3224 (2017).
PubMed: 28581722

Assembly members:

Assembly members:
PipX, polymer, 89 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Synechococcus elongatus Taxonomy ID: 32046 Superkingdom: Bacteria Kingdom: not available Genus/species: Synechococcus elongatus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pTrc99A

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PipX: MASENYLNHPTFGLLYQICS FGDSKELFATLYAQRLFFLV AFDARGTRFEPIGRNEARML VDNRLRQLRRDASLQEYNQL QQVFKQTFL

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	170
15N chemical shifts	84
1H chemical shifts	531

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	PipX monomer	1

Entities:

Entity 1, PipX monomer 89 residues - Formula weight is not available

1

MET

ALA

SER

GLU

ASN

TYR

LEU

ASN

HIS

PRO

2

THR

PHE

GLY

LEU

TYR

GLN

ILE

CYS

SER

3

PHE

GLY

ASP

SER

LYS

GLU

LEU

PHE

ALA

THR

4

LEU

TYR

ALA

GLN

ARG

LEU

PHE

LEU

VAL

5

ALA

PHE

ASP

ALA

ARG

GLY

THR

ARG

PHE

GLU

6

PRO

ILE

GLY

ARG

ASN

GLU

ALA

ARG

MET

LEU

7

VAL

ASP

ASN

ARG

LEU

ARG

GLN

LEU

ARG

8

ASP

ALA

SER

LEU

GLN

GLU

TYR

ASN

GLN

LEU

9

GLN

VAL

PHE

LYS

GLN

THR

PHE

LEU

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_4	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_5	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_4	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_5	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_2	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_3	isotropic	sample_conditions_1

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

BMRB Entry 27041

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers: