BMRB Entry 5497

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR5497

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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, 15N, 13C resonance assignments of the carboxy-terminal domain of the transmembrane electron transfer protein DsbD

Deposition date:

2002-08-08

Original release date:

2002-12-23

Authors:

Bushell, Mark; Ferguson, Stuart; Redfield, Christina

Citation:

Citation: Bushell, K.; Ferguson, Stuart; Redfield, Christina. "Letter to the Editor: 1H, 15N and 13C assignments of the carboxy-terminal domain of the transmembrane electron transfer protein DsbD" J. Biomol. NMR 24, 359-360 (2002).

Assembly members:

Assembly members:
E. coli DsbD C-terminal domain, polymer, 160 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: pET22b(+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
E. coli DsbD C-terminal domain: MDIGINSDPVRPLQDWAFGA THTAQTQTHLNFTQIKTVDE LNQALVEAKGKPVMLDLYAD WCVACKEFEKYTFSDPQVQK ALADTVLLQANVTANDAQDV ALLKHLNVLGLPTILFFDGQ GQEHPQARVTGFMDAETFSA HLRDRQPKLAAALEHHHHHH

Data sets:

assigned_chemical_shifts
- shift_set_1

Data type	Count
1H chemical shifts	719
13C chemical shifts	469
15N chemical shifts	121

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	DsbD C-terminal domain	1

Entities:

Entity 1, DsbD C-terminal domain 160 residues - Formula weight is not available

1	MET	ASP	ILE	GLY	ILE	ASN	SER	ASP	PRO	VAL
2	ARG	PRO	LEU	GLN	ASP	TRP	ALA	PHE	GLY	ALA
3	THR	HIS	THR	ALA	GLN	THR	GLN	THR	HIS	LEU
4	ASN	PHE	THR	GLN	ILE	LYS	THR	VAL	ASP	GLU
5	LEU	ASN	GLN	ALA	LEU	VAL	GLU	ALA	LYS	GLY
6	LYS	PRO	VAL	MET	LEU	ASP	LEU	TYR	ALA	ASP
7	TRP	CYS	VAL	ALA	CYS	LYS	GLU	PHE	GLU	LYS
8	TYR	THR	PHE	SER	ASP	PRO	GLN	VAL	GLN	LYS
9	ALA	LEU	ALA	ASP	THR	VAL	LEU	LEU	GLN	ALA
10	ASN	VAL	THR	ALA	ASN	ASP	ALA	GLN	ASP	VAL
11	ALA	LEU	LEU	LYS	HIS	LEU	ASN	VAL	LEU	GLY
12	LEU	PRO	THR	ILE	LEU	PHE	PHE	ASP	GLY	GLN
13	GLY	GLN	GLU	HIS	PRO	GLN	ALA	ARG	VAL	THR
14	GLY	PHE	MET	ASP	ALA	GLU	THR	PHE	SER	ALA
15	HIS	LEU	ARG	ASP	ARG	GLN	PRO	LYS	LEU	ALA
16	ALA	ALA	LEU	GLU	HIS	HIS	HIS	HIS	HIS	HIS

Samples:

sample1: E. coli DsbD C-terminal domain, [U-99% 15N], 1.5 mM

sample_2: E. coli DsbD C-terminal domain, [U-95% 13C; U-99% 15N], 1.5 mM

condition_1: pH: 6.5; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
The home-built spectrometers are equipped with Oxford Instruments	not available	not available	condition_1
Company magnets, Omega software and digital control equipment	not available	not available	condition_1
(Bruker), home-built triple resonance pulsed field gradient probe	not available	not available	condition_1
heads and home-built linear amplifiers.	not available	not available	condition_1

Software:

FELIX v2.3 - data processing

NMR spectrometers:

home built . 600 MHz
home built . 750 MHz

PDB	1UC7 4IP1 4IP6
DBJ	BAB38540 BAE78138 BAG66862 BAG79959 BAI28440
EMBL	CAA54781 CAA85375 CAP78654 CAQ34485 CAR01112
GB	AAA97035 AAC77096 AAG59335 AAL50628 AAN45708
REF	NP_290769 NP_313144 NP_418559 NP_710001 NP_757066
SP	P36655 P58162 Q0SXE3 Q0T9Q5 Q1R3C4
AlphaFold	P36655 P58162 Q0SXE3 Q0T9Q5 Q1R3C4

1	MET	ASP	ILE	GLY	ILE	ASN	SER	ASP	PRO	VAL
2	ARG	PRO	LEU	GLN	ASP	TRP	ALA	PHE	GLY	ALA
3	THR	HIS	THR	ALA	GLN	THR	GLN	THR	HIS	LEU
4	ASN	PHE	THR	GLN	ILE	LYS	THR	VAL	ASP	GLU
5	LEU	ASN	GLN	ALA	LEU	VAL	GLU	ALA	LYS	GLY
6	LYS	PRO	VAL	MET	LEU	ASP	LEU	TYR	ALA	ASP
7	TRP	CYS	VAL	ALA	CYS	LYS	GLU	PHE	GLU	LYS
8	TYR	THR	PHE	SER	ASP	PRO	GLN	VAL	GLN	LYS
9	ALA	LEU	ALA	ASP	THR	VAL	LEU	LEU	GLN	ALA
10	ASN	VAL	THR	ALA	ASN	ASP	ALA	GLN	ASP	VAL
11	ALA	LEU	LEU	LYS	HIS	LEU	ASN	VAL	LEU	GLY
12	LEU	PRO	THR	ILE	LEU	PHE	PHE	ASP	GLY	GLN
13	GLY	GLN	GLU	HIS	PRO	GLN	ALA	ARG	VAL	THR
14	GLY	PHE	MET	ASP	ALA	GLU	THR	PHE	SER	ALA
15	HIS	LEU	ARG	ASP	ARG	GLN	PRO	LYS	LEU	ALA
16	ALA	ALA	LEU	GLU	HIS	HIS	HIS	HIS	HIS	HIS

1	MET	ASP	ILE	GLY	ILE	ASN	SER	ASP	PRO	VAL
2	ARG	PRO	LEU	GLN	ASP	TRP	ALA	PHE	GLY	ALA
3	THR	HIS	THR	ALA	GLN	THR	GLN	THR	HIS	LEU
4	ASN	PHE	THR	GLN	ILE	LYS	THR	VAL	ASP	GLU
5	LEU	ASN	GLN	ALA	LEU	VAL	GLU	ALA	LYS	GLY
6	LYS	PRO	VAL	MET	LEU	ASP	LEU	TYR	ALA	ASP
7	TRP	CYS	VAL	ALA	CYS	LYS	GLU	PHE	GLU	LYS
8	TYR	THR	PHE	SER	ASP	PRO	GLN	VAL	GLN	LYS
9	ALA	LEU	ALA	ASP	THR	VAL	LEU	LEU	GLN	ALA
10	ASN	VAL	THR	ALA	ASN	ASP	ALA	GLN	ASP	VAL
11	ALA	LEU	LEU	LYS	HIS	LEU	ASN	VAL	LEU	GLY
12	LEU	PRO	THR	ILE	LEU	PHE	PHE	ASP	GLY	GLN
13	GLY	GLN	GLU	HIS	PRO	GLN	ALA	ARG	VAL	THR
14	GLY	PHE	MET	ASP	ALA	GLU	THR	PHE	SER	ALA
15	HIS	LEU	ARG	ASP	ARG	GLN	PRO	LYS	LEU	ALA
16	ALA	ALA	LEU	GLU	HIS	HIS	HIS	HIS	HIS	HIS