BMRB Entry 16155

Name: Solution NMR structure of protein HS00059 from Homo Sapiens. Northeast Structural Genomics Consortium (NESG) target HT98A.
Published: 2009-03-12

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PDB ID: 2keo
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16155
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution NMR structure of protein HS00059 from Homo Sapiens. Northeast Structural Genomics Consortium (NESG) target HT98A.

Deposition date:

2009-01-30

Original release date:

2009-03-12

Authors:

Lemak, Alexander; Gutmanas, Aleksandras; Fares, Christophe; Quyang, Hui; Dhe-Paganon, Sirano; Montelione, Gaetano; Arrowsmith, Cheryl

Citation:

Citation: Lemak, Alexander; Gutmanas, Aleksandras; Fares, Christophe; Quyang, Hui; Dhe-Paganon, Sirano; Montelione, Gaetano; Arrowsmith, Cheryl. "Solution NMR Structure of human protein HS00059" .

Assembly members:

Assembly members:
hs00059, polymer, 112 residues, 14686.104 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):
hs00059: MHHHHHHSSGRENLYFQGNN EKVTLVRIADLENHNNDGGF WTVIDGKVYDIKDFQTQSLT ENSILAQFAGEDPVVALEAA LQFEDTRESMHAFCVGQYLE PDQEGVTIPDLG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
spectral_peak_list

Data type	Count
13C chemical shifts	374
15N chemical shifts	97
1H chemical shifts	620

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	hs00059	1

Entities:

Entity 1, hs00059 112 residues - 14686.104 Da.

1

MET

HIS

SER

GLY

2

ARG

GLU

ASN

LEU

TYR

PHE

GLN

GLY

ASN

3

GLU

LYS

VAL

THR

LEU

VAL

ARG

ILE

ALA

ASP

4

LEU

GLU

ASN

HIS

ASN

ASP

GLY

PHE

5

TRP

THR

VAL

ILE

ASP

GLY

LYS

VAL

TYR

ASP

6

ILE

LYS

ASP

PHE

GLN

THR

GLN

SER

LEU

THR

7

GLU

ASN

SER

ILE

LEU

ALA

GLN

PHE

ALA

GLY

8

GLU

ASP

PRO

VAL

ALA

LEU

GLU

ALA

9

LEU

GLN

PHE

GLU

ASP

THR

ARG

GLU

SER

MET

10

HIS

ALA

PHE

CYS

VAL

GLY

GLN

TYR

LEU

GLU

11

PRO

ASP

GLN

GLU

GLY

VAL

THR

ILE

PRO

ASP

12

LEU

GLY

Samples:

sample_1: hs00059, [U-13C; U-15N], 0.5 mM; TRIS 10 mM; sodium chloride 300 mM; ZnSO4 10 uM; DTT 10 mM; NaN3 0.01%; benzamidine 10 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 300 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	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 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D (H)CCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C_arom NOESY	sample_1	isotropic	sample_conditions_1

Software:

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

SPARKY, Goddard - peak picking

FMC, Lemak, Steren, Llinas, Arrowsmith - chemical shift assignment

TALOS, Cornilescu, Delaglio and Bax - data analysis

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

NMR spectrometers:

Bruker Avance 800 MHz
Varian INOVA 600 MHz