BMRB Entry 4355

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR4355

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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, 15N Chemical Shift Assignments for the Asymmetric Strands of the Tetramerization Domain of the Mnt Repressor

Deposition date:

1999-06-13

Original release date:

1999-10-07

Authors:

Nooren, Irene; Kaptein, Robert; Sauer, Robert; Boelens, Rolf

Citation:

Citation: Nooren, Irene; Kaptein, Robert; Sauer, Robert; Boelens, Rolf. "The Tetramerization Domain of the Mnt Repressor Consists of two Right-handed Coiled Coils" Nat. Struct. Biol. 6, 755-759 (1999).
PubMed: 10426954

Assembly members:

Assembly members:
homotetrameric peptide, polymer, 37 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Bacteriophage P22 Taxonomy ID: 10754 Superkingdom: Viruses Kingdom: not available Genus/species: not available Bacteriophage P22

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pTM203-st6

Entity Sequences (FASTA):

Entity Sequences (FASTA):
homotetrameric peptide: RNDAERLADEQSELVKKMVF DTLKDLYKKTTHHHHHH

Data sets:

assigned_chemical_shifts
- resonance_set_A
- resonance_set_B

Data type	Count
13C chemical shifts	266
15N chemical shifts	68
1H chemical shifts	463

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Mnt-C subunit A	1
2	Mnt-C subunit B	1
3	Mnt-C subunit C	1
4	Mnt-C subunit D	1

Entities:

Entity 1, Mnt-C subunit A 37 residues - Formula weight is not available

1

ARG

ASN

ASP

ALA

GLU

ARG

LEU

ALA

ASP

GLU

2

GLN

SER

GLU

LEU

VAL

LYS

MET

VAL

PHE

3

ASP

THR

LEU

LYS

ASP

LEU

TYR

LYS

THR

4

THR

HIS

Samples:

15N_labelled: homotetrameric peptide, [U-95% 15N], 3.0 mM

13C_15N_labelled: homotetrameric peptide, [U-95% 13C; U-95% 15N], 3.0 mM

10%_13C_labelled: homotetrameric peptide, [U-10% 13C], 3.0 mM

unlabelled_labelled_mixture: homotetrameric peptide, [50/50 U-95% 13C; U-95% 15N / unlabelled], 3.0 mM

conditions_1: ionic strength: 0.20 M; pH: 5.2; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D (1H,15N)-HSQC	not available	not available	not available
2D (1H,1H) NOESY	not available	not available	not available
3D TOCSY (15N,1H) HSQC	not available	not available	not available
3D NOESY (15N,1H) HSQC	not available	not available	not available
3D HNCO	not available	not available	not available
3D HNCA	not available	not available	not available
3D HN(CO)CA	not available	not available	not available
3D HNHA	not available	not available	not available
3D HCACO	not available	not available	not available
3D TOCSY (13C,1H) HSQC	not available	not available	not available
3D HNHB	not available	not available	not available
3D H(C)CH DISPSY	not available	not available	not available
3D HCC(H) DISPSY	not available	not available	not available

Software:

Regine - bookkeeping

NMR spectrometers:

Bruker AMXT 600 MHz
Varian Unity-Plus 750 MHz

BMRB	4356
PDB	1MNT 1QEY
DBJ	BAF80731 BAG12614
EMBL	CAA25989
GB	AAF75057 AAM81380 ADM32399 ADW81950 AKJ74157
REF	NP_059641 WP_015975190
SP	P03049
TPG	DAA00978
AlphaFold	P03049