BMRB Entry 15814

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15814

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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:

1H, 13C and 15N resonance assignments of the domain 5 of ABP-120 from Dictyostelium in native and 8M urea-denatured states.

Deposition date:

2008-06-22

Original release date:

2009-01-06

Authors:

Hsu, Shang-Te Danny; Cabrita, Lisa; Christodoulou, John; Dobson, Christopher

Citation:

Citation: Hsu, Shang-Te Danny; Cabrita, Lisa; Christodoulou, John; Dobson, Christopher. "1H, 15N and 13C assignments of domain 5 of Dictyostelium discoideum gelation factor (ABP-120) in its native and 8M urea-denatured states" Biomol. NMR Assignments 3, 29-31 (2009).
PubMed: 19636940

Assembly members:

Assembly members:
Domain_5_of_Dictyostelium_ABP-120, polymer, 108 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: N/A

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Domain_5_of_Dictyostelium_ABP-120: MTVKPAPSAEHSYAEGEGLV KVFDNAPAEFTIFAVDTKGV ARTDGGDPFEVAINGPDGLV VDAKVTDNNDGTYGVVYDAP VEGNYNVNVTLRGNPIKNMP IDVKCIEG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
- assigned_chem_shift_list_2

Data type	Count
13C chemical shifts	688
15N chemical shifts	192
1H chemical shifts	819

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Domain 5 of ABP-120	1

Entities:

Entity 1, Domain 5 of ABP-120 108 residues - Formula weight is not available

1

MET

THR

VAL

LYS

PRO

ALA

PRO

SER

ALA

GLU

2

HIS

SER

TYR

ALA

GLU

GLY

GLU

GLY

LEU

VAL

3

LYS

VAL

PHE

ASP

ASN

ALA

PRO

ALA

GLU

PHE

4

THR

ILE

PHE

ALA

VAL

ASP

THR

LYS

GLY

VAL

5

ALA

ARG

THR

ASP

GLY

ASP

PRO

PHE

GLU

6

VAL

ALA

ILE

ASN

GLY

PRO

ASP

GLY

LEU

VAL

7

VAL

ASP

ALA

LYS

VAL

THR

ASP

ASN

ASP

8

GLY

THR

TYR

GLY

VAL

TYR

ASP

ALA

PRO

9

VAL

GLU

GLY

ASN

TYR

ASN

VAL

ASN

VAL

THR

10

LEU

ARG

GLY

ASN

PRO

ILE

LYS

ASN

MET

PRO

11

ILE

ASP

VAL

LYS

CYS

ILE

GLU

GLY

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	298K
3D HNCO	sample_1	isotropic	298K
3D HNCACB	sample_1	isotropic	298K
3D CBCA(CO)NH	sample_1	isotropic	298K
3D HN(CA)CO	sample_1	isotropic	298K
3D 1H-15N TOCSY	sample_1	isotropic	298K
(H)N(COCA)NH	sample_1	isotropic	298K
2D 1H-15N HSQC	sample_2	isotropic	298K
3D HNCO	sample_2	isotropic	298K
3D HNCACB	sample_2	isotropic	298K
3D CBCA(CO)NH	sample_2	isotropic	298K
3D HN(CA)CO	sample_2	isotropic	298K
3D 1H-15N TOCSY	sample_2	isotropic	298K
(H)N(COCA)NH	sample_2	isotropic	298K
2D 1H-13C HSQC	sample_2	isotropic	298K
3D HCCH-TOCSY	sample_2	isotropic	298K
3D HBHA(CO)NH	sample_2	isotropic	298K
3D HCCH-COSY	sample_2	isotropic	298K

PDB	1WLH 1QFH
EMBL	P13466

BMRB Entry 15814

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

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