BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 19314

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: 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:
HR9151A, polymer, 112 residues, 13040.079 Da.

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

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

Data sets:
Data typeCount
13C chemical shifts453
15N chemical shifts98
1H chemical shifts743

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1HR9151A1

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   METGLYHISHISHISHISHISHISSERHIS
2   METPROLYSALATHRALAGLNMETGLUGLU
3   LYSLEUARGASPPHETHRARGALATYRGLU
4   PROASPSERVALLEUPROLEUALAASPGLY
5   VALLEUSERPHEILEHISHISGLNILEILE
6   GLULEUALAARGASPCYSLEUTHRLYSSER
7   ARGASPGLYLEUILETHRTHRVALTYRPHE
8   TYRGLULEUGLNGLUASNLEUGLULYSLEU
9   LEUGLNASPALATYRGLUARGSERGLUSER
10   LEUGLUVALALAPHEVALTHRGLNLEUVAL
11   LYSLYSLEULEUILEILEILESERARGPRO
12   ALAARG

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCHR9151A.011isotropicsample_conditions_1
2D 1H-13C CT HSQC aliphaticHR9151A.011isotropicsample_conditions_1
3D HNCOHR9151A.011isotropicsample_conditions_1
3D CBCA(CO)NHHR9151A.011isotropicsample_conditions_1
3D HNCACBHR9151A.011isotropicsample_conditions_1
2D 1H-13C CT HSQC aromaticHR9151A.011isotropicsample_conditions_1
3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESYHR9151A.011isotropicsample_conditions_1
3D (H)CCH-TOCSYHR9151A.011isotropicsample_conditions_1
3D HBHA(CO)NHHR9151A.011isotropicsample_conditions_1
3D HN(CA)COHR9151A.011isotropicsample_conditions_1
2D 1H-15N HSQC_wideHR9151A.011isotropicsample_conditions_1
3D (H)CCH-COSYaliHR9151A.011isotropicsample_conditions_1
3D (H)CCH-COSYaroHR9151A.011isotropicsample_conditions_1
2D 1H-13C HSQC methylHR9151A.009isotropicsample_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

Related Database Links:

UNP Q9Y2H9
PDB
REF XP_004023623 XP_007622501 XP_008046233 XP_010853832 XP_011287990

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts