BMRB Entry 27290

Name: (1)H, (13)C, (15)N resonance assignment of human YAP 50-171 fragment
Published: 2018-01-25

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27290

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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:

(1)H, (13)C, (15)N resonance assignment of human YAP 50-171 fragment

Deposition date:

2017-10-24

Original release date:

2018-01-25

Authors:

Feichtinger, Michael; Sara, Tomas; Platzer, Gerald; Mateos, Borja; Bokhovchuk, Fedir; Chene, Patrick; Konrat, Robert

Citation:

Citation: Feichtinger, Michael; Sara, Tomas; Platzer, Gerald; Mateos, Borja; Bokhovchuk, Fedir; Chene, Patrick; Konrat, Robert. "1H, 13C, 15N resonance assignment of human YAP 50-171 fragment" Biomol. NMR Assign. 12, 179-182 (2018).
PubMed: 29372459

Assembly members:

Assembly members:
YAP_50-171, polymer, 122 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: PETM14

Entity Sequences (FASTA):

Entity Sequences (FASTA):
YAP_50-171: AGHQIVHVRGDSETDLEALF NAVMNPKTANVPQTVPMRLR KLPDSFFKPPEPKSHSRQAS TDAGTAGALTPQHVRAHSSP ASLQLGAVSPGTLTPTGVVS GPAATPTAQHLRQSSFEIPD DV

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	274
15N chemical shifts	102
1H chemical shifts	101

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	human YAP 50-171 fragment	1

Entities:

Entity 1, human YAP 50-171 fragment 122 residues - Formula weight is not available

1

ALA

GLY

HIS

GLN

ILE

VAL

HIS

VAL

ARG

GLY

2

ASP

SER

GLU

THR

ASP

LEU

GLU

ALA

LEU

PHE

3

ASN

ALA

VAL

MET

ASN

PRO

LYS

THR

ALA

ASN

4

VAL

PRO

GLN

THR

VAL

PRO

MET

ARG

LEU

ARG

5

LYS

LEU

PRO

ASP

SER

PHE

LYS

PRO

6

GLU

PRO

LYS

SER

HIS

SER

ARG

GLN

ALA

SER

7

THR

ASP

ALA

GLY

THR

ALA

GLY

ALA

LEU

THR

8

PRO

GLN

HIS

VAL

ARG

ALA

HIS

SER

PRO

9

ALA

SER

LEU

GLN

LEU

GLY

ALA

VAL

SER

PRO

10

GLY

THR

LEU

THR

PRO

THR

GLY

VAL

SER

11

GLY

PRO

ALA

THR

PRO

THR

ALA

GLN

HIS

12

LEU

ARG

GLN

SER

PHE

GLU

ILE

PRO

ASP

13

ASP

VAL

Samples:

sample_1: YAP 50-171, [U-95% 13C; U-90% 15N], 0.5 mM; sodium chloride 150 mM; EDTA 1 mM; TRIS 20 mM

sample_conditions_1: ionic strength: 171 mM; pH: 6; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCANNH	sample_1	isotropic	sample_conditions_1
3D HN(COCA)NNH	sample_1	isotropic	sample_conditions_1
3D HN(CO)CACB	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1

Software:

CCPNMR, CCPN - chemical shift assignment

SPARKY, Goddard - data analysis

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

Bruker Avance 800 MHz

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