BMRB Entry 26604

Name: Protein resonance assignment at MAS frequencies approaching 100 kHz: a quantitative comparison of J-coupling and dipolar-coupling-based transfer methods
Published: 2015-09-30

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26604

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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:

Protein resonance assignment at MAS frequencies approaching 100 kHz: a quantitative comparison of J-coupling and dipolar-coupling-based transfer methods

Deposition date:

2015-07-10

Original release date:

2015-09-30

Authors:

Penzel, Susanne; Smith, Albert; Agarwal, Vipin; Hunkeler, Andreas; Samoson, Ago; Bockmann, Anja; Ernst, Matthias; Meier, Beat

Citation:

Citation: Penzel, Susanne; Smith, Albert; Agarwal, Vipin; Hunkeler, Andreas; Samoson, Ago; Bockmann, Anja; Ernst, Matthias; Meier, Beat. "Protein resonance assignment at MAS frequencies approaching 100 kHz: a quantitative comparison of J-coupling and dipolar-coupling-based transfer methods" J. Biomol. NMR 63, 165-186 (2015).
PubMed: 26267840

Assembly members:

Assembly members:
Ubiquitin_(microcrystalline), polymer, 76 residues, Formula weight is not available

Natural source:

Natural source: Common Name: human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: PET21b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Ubiquitin_(microcrystalline): MQIFVKTLTGKTITLEVEPS DTIENVKAKIQDKEGIPPDQ QRLIFAGKQLEDGRTLSDYN IQKESTLHLVLRLRGG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	203
15N chemical shifts	66
1H chemical shifts	66

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	ubiquitin (microcrystal)	1

Entities:

Entity 1, ubiquitin (microcrystal) 76 residues - Formula weight is not available

1

MET

GLN

ILE

PHE

VAL

LYS

THR

LEU

THR

GLY

2

LYS

THR

ILE

THR

LEU

GLU

VAL

GLU

PRO

SER

3

ASP

THR

ILE

GLU

ASN

VAL

LYS

ALA

LYS

ILE

4

GLN

ASP

LYS

GLU

GLY

ILE

PRO

ASP

GLN

5

GLN

ARG

LEU

ILE

PHE

ALA

GLY

LYS

GLN

LEU

6

GLU

ASP

GLY

ARG

THR

LEU

SER

ASP

TYR

ASN

7

ILE

GLN

LYS

GLU

SER

THR

LEU

HIS

LEU

VAL

8

LEU

ARG

LEU

ARG

GLY

Name	Sample	Sample state	Sample conditions
3D (H)CANH	sample_1	isotropic	sample_conditions_1
3D (H)CA(CO)NH	sample_1	isotropic	sample_conditions_1
3D (HCA)CB(CA)NH	sample_1	isotropic	sample_conditions_1
3D (HNCA)CB(CA)NH	sample_1	isotropic	sample_conditions_1
3D (HN)CONH	sample_1	isotropic	sample_conditions_1
3D (H)CO(CA)NH	sample_1	isotropic	sample_conditions_1

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks

BMRB Entry 26604

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers: