BMRB Entry 34908

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34908
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
Solution Structure of cAMP-dependent Protein Kinase RII-alpha Subunit Dimerization and Docking Domain Complex with Microtubule Associated Protein 2c (84-111)
Deposition date:
2024-03-06
Original release date:
2024-10-15
Authors:
Bartosik, V.; Lanikova, A.; Janackova, Z.; Padrta, P.; Zidek, L.
Citation:

Citation: Bartosik, V.; Plucarova, J.; Lanikova, A.; Janackova, Z.; Padrta, P.; Jansen, S.; Varecka, V.; Gruber, T.; Feller, S.; Zidek, L.. "Structural basis of binding the unique N-terminal domain of microtubule-associated protein 2c to proteins regulating kinases of signaling pathways."  J. Biol. Chem. 300, 107551-107551 (2024).
PubMed: 39002671

Assembly members:

Assembly members:
entity_1, polymer, 52 residues, 5789.617 Da.
entity_2, polymer, 28 residues, 3015.349 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 BL21(DE3)   Vector: pETM11

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GAMGMSHIQIPPGLTELLQG YTVEVLRQQPPDLVEFAVEY FTRLREARAPAS
entity_2: RETAEEVSARIVQVVTAEAV AVLKGEQE

Data sets:
Data typeCount
13C chemical shifts249
15N chemical shifts90
1H chemical shifts575

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11
2unit_21
3unit_32

Entities:

Entity 1, unit_1 52 residues - 5789.617 Da.

1   GLYALAMETGLYMETSERHISILEGLNILE
2   PROPROGLYLEUTHRGLULEULEUGLNGLY
3   TYRTHRVALGLUVALLEUARGGLNGLNPRO
4   PROASPLEUVALGLUPHEALAVALGLUTYR
5   PHETHRARGLEUARGGLUALAARGALAPRO
6   ALASER

Entity 2, unit_3 28 residues - 3015.349 Da.

1   ARGGLUTHRALAGLUGLUVALSERALAARG
2   ILEVALGLNVALVALTHRALAGLUALAVAL
3   ALAVALLEULYSGLYGLUGLNGLU

Samples:

sample_1: Microtubule associated protein 2c, [U-13C; U-15N], 0.5 mM; cAMP-dependent protein kinase type II-alpha regulatory subunit 2 mM; MOPS 50 mM; sodium chloride 100 mM; D2O 10 % v/v; sodium azide 17 mM

sample_2: Microtubule associated protein 2c 0.56 mM; cAMP-dependent protein kinase type II-alpha regulatory subunit, [U-13C; U-15N], 1.12 mM; MOPS 50 mM; sodium chloride 100 mM; D2O 10 % v/v; sodium azide 10 mM

sample_3: Microtubule associated protein 2c, [U-15N], 0.1 mM; cAMP-dependent protein kinase type II-alpha regulatory subunit 0.4 mM; MOPS 50 mM; sodium chloride 100 mM; D2O 8 % v/v; Pf1 phage 40 mg/mL

sample_4: Microtubule associated protein 2c, [U-15N], 0.23 mM; cAMP-dependent protein kinase type II-alpha regulatory subunit 0.92 mM; MOPS 50 mM; sodium chloride 100 mM; D2O 7.5 % v/v

sample_5: Microtubule associated protein 2c, [I,V-13C; I,L,V-15N], 0.45 mM; cAMP-dependent protein kinase type II-alpha regulatory subunit 1.8 mM; MOPS 50 mM; sodium chloride 100 mM; D2O 7.5 % v/v

sample_conditions_1: ionic strength: 100 mM; pH: 6.9; pressure: 1 bar; temperature: 300.2 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1
3D 1H-15N NOESY filteredsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphatic filteredsample_1isotropicsample_conditions_1
3D 1H-15N NOESY filteredsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aliphatic filteredsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_4isotropicsample_conditions_1
2D 1H-15N HSQCsample_3anisotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-15N HSQC IPAPsample_4isotropicsample_conditions_1
2D 1H-15N HSQC IPAPsample_3anisotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_5isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_5isotropicsample_conditions_1
3D HCCH-TOCSYsample_5isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1

Software:

TopSpin v3, Bruker Biospin - collection

NMRPipe v11.2, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

Sparky v3.115, Goddard - chemical shift assignment, peak picking

CYANA v3.98.15, Guntert, Mumenthaler and Wuthrich - chemical shift assignment

CNS v1.21, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure calculation

SCULPTOR v3.1, Charavay, Eynard, Hus, Bouvignies and Blackledge - refinement, structure calculation

NMR spectrometers:

  • Bruker AVANCE III HD 950 MHz
  • Bruker AVANCE III HD 850 MHz
  • Bruker AVANCE III HD 600 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks