BMRB Entry 17345

Name: Solution NMR structure of human NFATC2IP ubiquitin-like domain, NFATC2IP_244_338, NESG target HT65A/OCSP target hs00387_244_338/SGC-toronto
Published: 2011-01-05

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PDB ID: 2l76
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17345
MolProbity Validation Chart

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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:

Solution NMR structure of human NFATC2IP ubiquitin-like domain, NFATC2IP_244_338, NESG target HT65A/OCSP target hs00387_244_338/SGC-toronto

Deposition date:

2010-12-03

Original release date:

2011-01-05

Authors:

Wu, Bin; Yee, Adelinda; Houliston, Scott; Doherty, Ryan; Semesi, Anthony; Dhe-Paganon, Sirano; Arrowsmith, Cheryl

Citation:

Citation: Doherty, Ryan; Wu, Bin; Yee, Adelinda; Lemak, Alexander; Houliston, Scott; Fares, Christophe; Srisalam, Sampath; Bulter, C; Edwards, Aled; Weigelt, Johan; Dhe-Paganon, Sirano; Arrowsmith, Cheryl. "Human NFATC2IP ubiquitin-like domains" .

Assembly members:

Assembly members:
NFATC2IP_244_338, polymer, 95 residues, 10396.201 Da.

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: p15Tv lic

Entity Sequences (FASTA):

Entity Sequences (FASTA):
NFATC2IP_244_338: QGQEDEVVLVEGPTLPETPR LFPLKIRCRADLVRLPLRMS EPLQSVVDHMATHLGVSPSR ILLLFGETELSPTATPRTLK LGVADIIDCVVLTSS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
spectral_peak_list

Data type	Count
13C chemical shifts	414
15N chemical shifts	87
1H chemical shifts	693

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	NFATC2IP_244_338	1

Entities:

Entity 1, NFATC2IP_244_338 95 residues - 10396.201 Da.

1

GLN

GLY

GLN

GLU

ASP

GLU

VAL

LEU

VAL

2

GLU

GLY

PRO

THR

LEU

PRO

GLU

THR

PRO

ARG

3

LEU

PHE

PRO

LEU

LYS

ILE

ARG

CYS

ARG

ALA

4

ASP

LEU

VAL

ARG

LEU

PRO

LEU

ARG

MET

SER

5

GLU

PRO

LEU

GLN

SER

VAL

ASP

HIS

MET

6

ALA

THR

HIS

LEU

GLY

VAL

SER

PRO

SER

ARG

7

ILE

LEU

PHE

GLY

GLU

THR

GLU

LEU

8

SER

PRO

THR

ALA

THR

PRO

ARG

THR

LEU

LYS

9

LEU

GLY

VAL

ALA

ASP

ILE

ASP

CYS

VAL

10

VAL

LEU

THR

SER

Samples:

sample_1: NFATC2IP_244_338, [U-100% 13C; U-100% 15N], 0.5 mM; TRIS, [U-100% 2H], 10 mM; sodium chloride 300 mM; zinc sulphate 10 uM; DTT, [U-100% 2H], 10 mM; NaN3 0.01%; benzamidine 10 mM; inhibitor cocktail 1 x; H2O 90%; D2O 10%

sample_2: NFATC2IP_244_338, [U-100% 13C; U-100% 15N], 0.5 mM; TRIS, [U-100% 2H], 10 mM; sodium chloride 300 mM; zinc sulphate 10 uM; DTT, [U-100% 2H], 10 mM; NaN3 0.01%; benzamidine 10 mM; inhibitor cocktail 1 x; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 300 mM; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCO	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D CCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_1

Software:

NMRPipe v2.3, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

MDDGUI v1.0, Gutmanas, Arrowsmith - processing

SPARKY v3.95, Goddard - data analysis

FMCGUI v2.4, Lemak, Arrowsmith - chemical shift assignment

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

AutoStruct, Huang, Tejero, Powers and Montelione - NMR structure quality assessment

PSVS, Bhattacharya and Montelione - NMR structure quality assessment

NMR spectrometers:

Bruker Avance 500 MHz
Bruker Avance 800 MHz

PDB	2L76
DBJ	BAC11189
GB	AAH18311 AAH21551 AAH80628 AAI01742 AAI12183
REF	NP_116204 XP_001146533 XP_002826318 XP_003804645 XP_004057462
SP	Q8NCF5
AlphaFold	Q8NCF5