Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR54031

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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Assignments for the Doc2B C2B domain (aa265-412) bearing K316Q & K319Q mutations

Deposition date:

2026-09-23

Original release date:

2026-11-03

Authors:

Rastegar, Cyrus; Powell, Julia; Rizo, Josep

Citation:

Citation: Rastegar, Cyrus; Powell, Julia; Wosztyl, Aleksandra; David, Guillaume; Jaczynska, Klaudia; Bai, Xiao-chen; Han, Yan; Chen, Zhe; Rizo, Josep. "Cryo-EM and NMR Reveal a Membrane-Gated Doc2B-Munc13-1 Complex and a Helical Doc2B-SNARE-Binding Interface " Adv. Sci. (Weinh) ., e78011-e78011 (2026).
PubMed: 42973246

Assembly members:

Assembly members:
entity_1, polymer, 150 residues, 17023.44 Da.

Natural source:

Natural source: Common Name: Rat Taxonomy ID: 10116 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Rattus norvegicus

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSEERGRILISLKYSSQKQG LLVGIVRCAHLAAMDANGYS DPYVKTYLKPDVDQKSQHKT AVKKKTLNPEFNEEFCYEIK HGDLAKKTLEVTVWDYDIGK SNDFIGGVVLGINAKGERLK HWFDCLKNKDKRIERWHTLT NEIPGAVLSD

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	414
15N chemical shifts	136
1H chemical shifts	136

Time Domain Data

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	C2B	1

Entities:

Entity 1, C2B 150 residues - 17023.44 Da.

Doc2B C2B Domain (aa265-412) from Rattus norvegicus; K316Q, K319Q mutation; Contains an N-terminal Gly-Ser leftover from thrombin cleavage.

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

Samples:

sample_1: Double C2-like domain-containing protein beta (Doc2B) C2B Domain Polybasic Mutant, [U-99% 13C; U-99% 15N], 816 uM; HEPES 20 mM; potassium chloride 100 mM; EDTA 1 mM; TCEP 1 mM; Aprotinin 800 nM; Leupeptin 20 uM; Antipain 1 uM

sample_conditions_1: ionic strength: 120 mM; pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

NMRFx Analyst v11.4.40 - data analysis

NMRViewJ v8.0.a15 - data analysis, peak picking, processing

NMRDraw v5.2 Rev 2010.108.19.28 - processing

VNMRj v4.2 Revision A - collection

NMR spectrometers:

Agilent DD2 600 MHz

BMRB Entry 54031