BMRB Entry 15539

Name: Backbone 1H, 13C, and 15N NMR assignments for the Cyanothece 51142 protein A1KYE3 - a protein in the DUF683 family associated with nitrogen fixation.
Published: 2008-01-17

Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15539

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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 NMR assignments for the Cyanothece 51142 protein A1KYE3 - a protein in the DUF683 family associated with nitrogen fixation.

Deposition date:

2007-10-28

Original release date:

2008-01-17

Authors:

Buchko, Garry

Citation:

Citation: Buchko, Garry; Sofia, Heidi. "Backbone 1H, 13C, and 15N NMR assignments for the Cyanothece 51142 protein cce_0567: a protein associated with nitrogen fixation in the DUF683 family" Biomol. NMR Assignments 2, 25-28 (2008).
PubMed: 19636916

Assembly members:

Assembly members:
DUF683_containing_polypeptide, polymer, 81 residues, 37000 Da.

Natural source:

Natural source: Common Name: Cyanothece 51142 Taxonomy ID: 43989 Superkingdom: Eubacteria Kingdom: not available Genus/species: Cyanothece Cyanothece sp. ATCC 51142

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
DUF683_containing_polypeptide: GSHMTVATDNNPTPEAVADL KKKVRKLNSKAGQMKMDLHD LAEGLPTDYENLVETAEKTY EIFRELDQLKKKLNIWEETL K

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	248
15N chemical shifts	75
1H chemical shifts	150

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Polypeptide 1	1
2	Polypeptide 2	1
3	Polypeptide 3	1
4	Polypeptide 4	1

Entities:

Entity 1, Polypeptide 1 81 residues - 37000 Da.

Residues 1-3 remain after cleavage with thrombin. Fourth residue is M1.

1

GLY

SER

HIS

MET

THR

VAL

ALA

THR

ASP

ASN

2

ASN

PRO

THR

PRO

GLU

ALA

VAL

ALA

ASP

LEU

3

LYS

VAL

ARG

LYS

LEU

ASN

SER

LYS

4

ALA

GLY

GLN

MET

LYS

MET

ASP

LEU

HIS

ASP

5

LEU

ALA

GLU

GLY

LEU

PRO

THR

ASP

TYR

GLU

6

ASN

LEU

VAL

GLU

THR

ALA

GLU

LYS

THR

TYR

7

GLU

ILE

PHE

ARG

GLU

LEU

ASP

GLN

LEU

LYS

8

LYS

LEU

ASN

ILE

TRP

GLU

THR

LEU

9

LYS

Samples:

sample_1: sodium chloride 500 ± 2 mM; TRIS 20 ± 0.5 mM; DTT 1 ± 0.1 mM; DUF683 containing polypeptide, [U-100% 13C; U-100% 15N], 1 ± 0.2 mM

sample_2: sodium chloride 500 ± 2 mM; TRIS 20 ± 0.5 mM; DTT 1 ± 0.1 mM; DUF683 containing polypeptide, [U-100% 13C; U-100% 15N; 90% 2H], 1 ± 0.2 mM

sample_3: sodium chloride 500 ± 2 mM; TRIS 20 ± 0.5 mM; DTT 1 ± 0.1 mM; DUF683 containing polypeptide, [U-15N]-His, 0.1 ± 0.2 mM

sample_4: sodium chloride 500 ± 2 mM; TRIS 20 ± 0.5 mM; DTT 1 ± 0.1 mM; DUF683 containing polypeptide, [U-15N]-Leu, 0.1 ± 0.2 mM

sample_5: sodium chloride 500 ± 2 mM; TRIS 20 ± 0.5 mM; DTT 1 ± 0.1 mM; DUF683 containing polypeptide, [U-15N]-Lys, 0.1 ± 0.2 mM

sample_6: sodium chloride 500 ± 2 mM; TRIS 20 ± 0.5 mM; DTT 1 ± 0.1 mM; DUF683 containing polypeptide, [U-15N]-Glu, 0.1 ± 0.2 mM

sample_7: sodium chloride 500 ± 2 mM; TRIS 20 ± 0.5 mM; DTT 1 ± 0.1 mM; DUF683 containing polypeptide, [U-15N]-Val, 0.1 ± 0.2 mM

sample_conditions_1: ionic strength: 521 mM; pH: 7.2; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D C(CO)NH	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HN(COCA)CB	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_2	isotropic	sample_conditions_1
3D HCCH-COSY	sample_2	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_3	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_4	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_5	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_6	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_7	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1

Software:

FELIX v95, Accelrys Software Inc. - data analysis, peak picking, processing

NMR spectrometers:

Varian INOVA 600 MHz
Varian UnityPlus 500 MHz
Varian INOVA 750 MHz
Varian INOVA 800 MHz

PDB	3CSX
GB	AAW56996 ACB49918
REF	WP_009546647