BMRB Entry 19977

Title:
Solution structure human HCN2 CNBD in the cAMP-unbound state
Deposition date:
2014-05-16
Original release date:
2014-09-02
Authors:
Saponaro, Andrea; Pauleta, Sofia; Cantini, Francesca; Matzapetakis, Manolis; Hammann, Christian; Banci, Lucia; Thiel, Gerard; Santoro, Bina; Moroni, Anna
Citation:

Citation: Saponaro, Andrea; Pauleta, Sofia; Cantini, Francesca; Matzapetakis, Manolis; Hammann, Christian; Banci, Lucia; Thiel, Gerard; Santoro, Bina; Moroni, Anna. "Structural basis for the mutual antagonism of cAMP and TRIP8b in regulating HCN channel function"  .

Assembly members:

Assembly members:
entity, polymer, 158 residues, 15918.672 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: pET-24b

Data sets:
Data typeCount
1H chemical shifts1113
13C chemical shifts624
15N chemical shifts149

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1human HCN2 CNBD1

Entities:

Entity 1, human HCN2 CNBD 158 residues - 15918.672 Da.

Residues 515-520 represent a non-native affinity tag Residues 521-533 are unstructured and were omitted for simplicity

1   GLYPROSERSERPROMETGLULEUASNGLY
2   PROLEUARGGLUGLUILEVALASNPHEASN
3   CYSARGLYSLEUVALALASERMETPROLEU
4   PHEALAASNALAASPPROASNPHEVALTHR
5   ALAMETLEUTHRLYSLEULYSPHEGLUVAL
6   PHEGLNPROGLYASPTYRILEILEARGGLU
7   GLYTHRILEGLYLYSLYSMETTYRPHEILE
8   GLNHISGLYVALVALSERVALLEUTHRLYS
9   GLYASNLYSGLUMETLYSLEUSERASPGLY
10   SERTYRPHEGLYGLUILECYSLEULEUTHR
11   ARGGLYARGARGTHRALASERVALARGALA
12   ASPTHRTYRCYSARGLEUTYRSERLEUSER
13   VALASPASNPHEASNGLUVALLEUGLUGLU
14   TYRPROMETMETARGARGALAPHEGLUTHR
15   VALALAILEASPARGLEUASPARGILEGLY
16   LYSLYSASNSERILELEULEUHIS

Samples:

sample_1: entity, [U-15N], 1 mM; potassium phosphate 20 mM; potassium chloride 150 mM

sample_2: entity, [U-13C; U-15N], 1 mM; potassium phosphate 20 mM; potassium chloride 150 mM

sample_3: entity 1 mM; potassium phosphate 20 mM; potassium chloride 150 mM

sample_conditions_1: temperature: 298 K; pH: 7.0; pressure: 1 atm; ionic strength: 170 mM

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_3isotropicsample_conditions_1
2D 1H-1H TOCSYsample_3isotropicsample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection, processing

CARA v1.8, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

AMBER v12, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

CING, Geerten Vuister, Jurgen F. Doreleijers and Alan Wilter Sousa da Silva - structure validation

PSVS, Bhattacharya and Montelione - structure validation

CANDID, Herrmann, Guntert and Wuthrich - structure solution

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz
  • Bruker Avance 900 MHz

Related Database Links:

PDB
DBJ BAD32628 BAI44633 BAI45607
EMBL CAA12406 CAB42602 CAB42630
GB AAC28444 AAC39760 AAC40125 AAF62174 AAI18002
REF NP_001185 NP_032252 NP_446136 XP_002193445 XP_002689207
SP O88703 Q9JKA9 Q9UL51
TPG DAA27526
AlphaFold Q9UL51 O88703 Q9JKA9

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