BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 34226

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR34226
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry

Title: Solution Structure of CaM/Kv7.2-hAB Complex   PubMed: 29463698

Deposition date: 2018-01-02 Original release date: 2018-02-19

Authors: Bernardo-Seisdedos, G.; Villarroel, A.; Millet, O.

Citation: Bernardo-Seisdedos, G.; Nunez-Viadero, E.; Gomis-Perez, C.; Malo, C.; Villarroel, A.; Millet, O.. "Structural basis and energy landscape for the Ca2+-gating and calmodulation of the Kv7.2 K+channel"  Proc. Natl. Acad. Sci. U. S. A. 115, 2395-2400 (2018).

Assembly members:
entity_1, polymer, 115 residues, 13599.536 Da.
entity_2, polymer, 149 residues, 16852.545 Da.
entity_CA, non-polymer, 40.078 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):
entity_1: MSYYHHHHHHDYDIPTTENL YFQGAMGILGSGQKHFEKRR NPAAGLIQSAWRFYATNLSR TDLHSTWQYYERTVTVPMYR GLEDLTPGLKVSIRAVCVMR FLVSKRKFKESLRLD
entity_2: MADQLTEEQIAEFKEAFSLF DKDGDGTITTKELGTVMRSL GQNPTEAELQDMINEVDADG NGTIDFPEFLTMMARKMKDT DSEEEIREAFRVFDKDGNGY ISAAELRHVMTNLGEKLTDE EVDEMIREADIDGDGQVNYE EFVQMMTAK

Data sets:
Data typeCount
13C chemical shifts991
15N chemical shifts239
1H chemical shifts1620

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22
3entity_3, 13
4entity_3, 23
5entity_3, 33
6entity_3, 43

Entities:

Entity 1, entity_1 115 residues - 13599.536 Da.

1   METSERTYRTYRHISHISHISHISHISHIS
2   ASPTYRASPILEPROTHRTHRGLUASNLEU
3   TYRPHEGLNGLYALAMETGLYILELEUGLY
4   SERGLYGLNLYSHISPHEGLULYSARGARG
5   ASNPROALAALAGLYLEUILEGLNSERALA
6   TRPARGPHETYRALATHRASNLEUSERARG
7   THRASPLEUHISSERTHRTRPGLNTYRTYR
8   GLUARGTHRVALTHRVALPROMETTYRARG
9   GLYLEUGLUASPLEUTHRPROGLYLEULYS
10   VALSERILEARGALAVALCYSVALMETARG
11   PHELEUVALSERLYSARGLYSPHELYSGLU
12   SERLEUARGLEUASP

Entity 2, entity_2 149 residues - 16852.545 Da.

1   METALAASPGLNLEUTHRGLUGLUGLNILE
2   ALAGLUPHELYSGLUALAPHESERLEUPHE
3   ASPLYSASPGLYASPGLYTHRILETHRTHR
4   LYSGLULEUGLYTHRVALMETARGSERLEU
5   GLYGLNASNPROTHRGLUALAGLULEUGLN
6   ASPMETILEASNGLUVALASPALAASPGLY
7   ASNGLYTHRILEASPPHEPROGLUPHELEU
8   THRMETMETALAARGLYSMETLYSASPTHR
9   ASPSERGLUGLUGLUILEARGGLUALAPHE
10   ARGVALPHEASPLYSASPGLYASNGLYTYR
11   ILESERALAALAGLULEUARGHISVALMET
12   THRASNLEUGLYGLULYSLEUTHRASPGLU
13   GLUVALASPGLUMETILEARGGLUALAASP
14   ILEASPGLYASPGLYGLNVALASNTYRGLU
15   GLUPHEVALGLNMETMETTHRALALYS

Entity 3, entity_3, 1 - Ca - 40.078 Da.

1   CA

Samples:

sample_1: Kv7.2-hAB, [U-100% 13C; U-100% 15N; U-50% 2H], 1 mM; Calmodulin, [U-100% 13C; U-100% 15N; U-50% 2H], 1 mM; potassium chloride 120 mM; MES 20 mM; CaCl2 5 mM; sodium azide 2 uM; DSS, [U-2H], 200 uM

sample_2: Kv7.2-hAB, [U-100% 13C; U-100% 15N], 500 uM; Calmodulin 500 uM; potassium chloride 120 mM; MES 20 mM; CaCl2 5 mM; sodium azide 2 uM; DSS, [U-2H], 200 uM

sample_3: Kv7.2-hAB, [U-100% 15N], 250 uM; Calmodulin, [U-100% 15N], 250 uM; potassium chloride 120 mM; MES 20 mM; CaCl2 5 mM; sodium azide 2 uM; DSS, [U-2H], 200 uM

sample_conditions_1: ionic strength: 120 mM; pH: 6; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N TROSY-HSQCsample_1isotropicsample_conditions_1
2D 1H-13C TROSY-HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)HAsample_1isotropicsample_conditions_1
3D HN(COCA)HAsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HNC(CCO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
2D 1H-15N TROSY-HSQCsample_2isotropicsample_conditions_1
2D 1H-13C TROSY-HSQCsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HN(CA)COsample_2isotropicsample_conditions_1
3D HN(CA)HAsample_2isotropicsample_conditions_1
3D HN(COCA)HAsample_2isotropicsample_conditions_1
3D H(CCO)NHsample_2isotropicsample_conditions_1
3D HNC(CCO)NHsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
2D 1H-15N TROSY-HSQCsample_3isotropicsample_conditions_1
2D 1H-15N semiTROSY-HSQCsample_3isotropicsample_conditions_1
2D 1H-15N TROSY-HSQCsample_3anisotropicsample_conditions_1
2D 1H-15N semiTROSY-HSQCsample_3anisotropicsample_conditions_1
2D 1H-15N TROSY-HSQCsample_1isotropicsample_conditions_1
2D 1H-15N TROSY-HSQCsample_2isotropicsample_conditions_1

Software:

TOPSPIN v3.1, Bruker Biospin - collection

SPARKY v3.115, Goddard - chemical shift assignment, data analysis, peak picking

Analysis v2.4, CCPN - chemical shift assignment, data analysis

NMRPipe v8.2, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

ARIA v2.3.1, Linge, O'Donoghue and Nilges - data analysis, refinement, structure calculation

ProcheckNMR, Laskowski and MacArthur - data analysis

MOLPROBITY, Richardson - data analysis

AQUA, Rullmann, Doreleijers and Kaptein - data analysis

NMR spectrometers:

  • Bruker AvanceIII 800 MHz
  • Bruker AvanceIII 600 MHz

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