BMRB Entry 15468

Name: Solution NMR structure of protein NE1242 from N. europaea. Northeast Structural Genomics Target NeT4
Published: 2007-10-19

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15468

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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:

Solution NMR structure of protein NE1242 from N. europaea. Northeast Structural Genomics Target NeT4

Deposition date:

2007-09-12

Original release date:

2007-10-19

Authors:

Wu, Yibing; Yee, Adelinda; Zeri, Ana; Guido, Valerie; Sukumaran, Dinesh; Arrowsmith, Cheryl; Szyperski, Thomas

Citation:

Citation: Wu, Yibing; Yee, Adelinda; Zeri, Ana; Guido, Valerie; Sukumaran, Dinesh; Arrowsmith, Cheryl; Szyperski, Thomas. "Solution NMR structure of protein NE1242 from N. europaea. Northeast Structural Genomics Target NeT4" .

Assembly members:

Assembly members:
NE1242, polymer, 73 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Neurospora crassa Taxonomy ID: 5141 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Neurospora crassa

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: BL21 DE3

Entity Sequences (FASTA):

Entity Sequences (FASTA):
NE1242: MTHHTEVFEGGTIDIEDDTS LTINGKEISYVHDAVKNKWS SRYLPYTQYDSLLDLARAII RDTVEFSGVKEGS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
spectral_peak_list
- spectral_peak_list_1
- spectral_peak_list_2

Data type	Count
13C chemical shifts	311
15N chemical shifts	76
1H chemical shifts	503

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	NE1242	1

Entities:

Entity 1, NE1242 73 residues - Formula weight is not available

1

MET

THR

HIS

THR

GLU

VAL

PHE

GLU

GLY

2

GLY

THR

ILE

ASP

ILE

GLU

ASP

THR

SER

3

LEU

THR

ILE

ASN

GLY

LYS

GLU

ILE

SER

TYR

4

VAL

HIS

ASP

ALA

VAL

LYS

ASN

LYS

TRP

SER

5

SER

ARG

TYR

LEU

PRO

TYR

THR

GLN

TYR

ASP

6

SER

LEU

ASP

LEU

ALA

ARG

ALA

ILE

7

ARG

ASP

THR

VAL

GLU

PHE

SER

GLY

VAL

LYS

8

GLU

GLY

SER

Samples:

sample_1: NE1242 0.5 mM

sample_conditions_1: ionic strength: 0.32 M; pH: .; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
4,3D, GFT HNNCABCA	sample_1	isotropic	sample_conditions_1
4,3D, GFT CABCACONNH	sample_1	isotropic	sample_conditions_1
4,3D, GFT HCCH COSY	sample_1	isotropic	sample_conditions_1
3D, 15N-13C RESOLVEDSIMULTANIOUS NOESY	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
4,3D, GFT HABCABCONNH	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1

Software:

AutoStruct, Huang, Tejero, Powers and Montelione - structure solution

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

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

XEASY, Bartels et al. - peak picking

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

AutoAssign, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

NMR spectrometers:

Varian INOVA 600 MHz

PDB	2JV8
EMBL	CAD85153
REF	WP_011111828