BMRB Entry 19314

Name: Solution NMR Structure of Microtubule-associated serine/threonine-protein kinase 1 from Homo sapiens, Northeast Structural Genomics Consortium (NESG) Target HR9151A
Published: 2013-07-08

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PDB ID: 2m9x
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19314
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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 Microtubule-associated serine/threonine-protein kinase 1 from Homo sapiens, Northeast Structural Genomics Consortium (NESG) Target HR9151A

Deposition date:

2013-06-20

Original release date:

2013-07-08

Authors:

Xu, Xianzhong; Eletsky, Alexander; Shastry, Ritu; Lee, Dan; Hamilton, Keith; Xiao, Rong; Acton, Thomas; Everett, John; Montelione, Gaetano; Szyperski, Thomas

Citation:

Citation: Xu, Xianzhong; Eletsky, Alexander; Shastry, Ritu; Lee, Dan; Hamilton, Keith; Xiao, Rong; Acton, Thomas; Everett, John; Montelione, Gaetano; Szyperski, Thomas. "Solution NMR Structure of Microtubule-associated serine/threonine-protein kinase 1 from Homo sapiens, Northeast Structural Genomics Consortium (NESG) Target HR9151A" To be published ., .-..

Assembly members:

Assembly members:
HR9151A, polymer, 112 residues, 13040.079 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: pET15_NESG

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HR9151A: MGHHHHHHSHMPKATAQMEE KLRDFTRAYEPDSVLPLADG VLSFIHHQIIELARDCLTKS RDGLITTVYFYELQENLEKL LQDAYERSESLEVAFVTQLV KKLLIIISRPAR

Data sets:

assigned_chemical_shifts
- hr9151a.str
spectral_peak_list

Data type	Count
13C chemical shifts	453
15N chemical shifts	98
1H chemical shifts	743

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	HR9151A	1

Entities:

Entity 1, HR9151A 112 residues - 13040.079 Da.

First 11 residues are the purification His tag. Residues 12-112 represents that native protein from residue 187 to 287.

1

MET

GLY

HIS

SER

HIS

2

MET

PRO

LYS

ALA

THR

ALA

GLN

MET

GLU

3

LYS

LEU

ARG

ASP

PHE

THR

ARG

ALA

TYR

GLU

4

PRO

ASP

SER

VAL

LEU

PRO

LEU

ALA

ASP

GLY

5

VAL

LEU

SER

PHE

ILE

HIS

GLN

ILE

6

GLU

LEU

ALA

ARG

ASP

CYS

LEU

THR

LYS

SER

7

ARG

ASP

GLY

LEU

ILE

THR

VAL

TYR

PHE

8

TYR

GLU

LEU

GLN

GLU

ASN

LEU

GLU

LYS

LEU

9

LEU

GLN

ASP

ALA

TYR

GLU

ARG

SER

GLU

SER

10

LEU

GLU

VAL

ALA

PHE

VAL

THR

GLN

LEU

VAL

11

LYS

LEU

ILE

SER

ARG

PRO

12

ALA

ARG

Samples:

HR9151A.011: HR9151A.011, [U-100% 13C; U-100% 15N], 0.508 mM; DTT 5 mM; NaCl 100 mM; Tris-HCl pH 7.5 10 mM; NaN3 0.02%; DSS 50 uM

HR9151A.009: HR9151A.011, [%5-13C; U-100% 15N], 0.39 mM; DTT 5 mM; NaCl 100 mM; Tris-HCl pH 7.5 10 mM; NaN3 0.02%; DSS 50 uM

sample_conditions_1: pH: 7.5; pressure: 1 atm; temperature: 283 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	HR9151A.011	isotropic	sample_conditions_1
2D 1H-13C CT HSQC aliphatic	HR9151A.011	isotropic	sample_conditions_1
3D HNCO	HR9151A.011	isotropic	sample_conditions_1
3D CBCA(CO)NH	HR9151A.011	isotropic	sample_conditions_1
3D HNCACB	HR9151A.011	isotropic	sample_conditions_1
2D 1H-13C CT HSQC aromatic	HR9151A.011	isotropic	sample_conditions_1
3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESY	HR9151A.011	isotropic	sample_conditions_1
3D (H)CCH-TOCSY	HR9151A.011	isotropic	sample_conditions_1
3D HBHA(CO)NH	HR9151A.011	isotropic	sample_conditions_1
3D HN(CA)CO	HR9151A.011	isotropic	sample_conditions_1
2D 1H-15N HSQC_wide	HR9151A.011	isotropic	sample_conditions_1
3D (H)CCH-COSYali	HR9151A.011	isotropic	sample_conditions_1
3D (H)CCH-COSYaro	HR9151A.011	isotropic	sample_conditions_1
2D 1H-13C HSQC methyl	HR9151A.009	isotropic	sample_conditions_1

Software:

CNS v1.3, Brunger, Adams, Clore, Gros, Nilges and Read - refinemen,structure solution,geometry optimization

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - refinement,geometry optimization,structure solution

AutoStruct v2.1, Huang, Tejero, Powers and Montelione - data analysis,refinement

AutoAssign v2.3.1, Zimmerman, Moseley, Kulikowski and Montelione - data analysis,chemical shift assignment

XEASY, Bartels et al. - data analysis,peak picking,chemical shift assignment

VNMRJ v2.2D, Varian - collection

TALOS+, Shen, Cornilescu, Delaglio and Bax - geometry optimization

PSVS v1.4, Bhattacharya, Montelione - structure validation

CARA v1.8.4, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking

PROSA, Guntert - processing

CSI, (CSI)-Wishart and Sykes - data analysis

NMR spectrometers:

Varian INOVA 750 MHz

UNP	Q9Y2H9
PDB	2M9X
REF	XP_004023623 XP_007622501 XP_008046233 XP_010853832 XP_011287990
AlphaFold	Q8N6X0