BMRB Entry 19144

Title:
A structural model of CAP mutant (T127L and S128I) in the apo state
Deposition date:
2013-04-05
Original release date:
2013-05-30
Authors:
Tzeng, Shiou-Ru; Kalodimos, C.
Citation:

Citation: Tzeng, Shiou-Ru; Kalodimos, Charalampos. "Allosteric inhibition through suppression of transient conformational states."  Nat. Chem. Biol. 9, 462-465 (2013).
PubMed: 23644478

Assembly members:

Assembly members:
CAMP_RECEPTOR_PROTEIN, polymer, 209 residues, 23555.3638 Da.

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: purified from the natural source

Data sets:
Data typeCount
13C chemical shifts217
15N chemical shifts122

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CAMP RECEPTOR PROTEIN1

Entities:

Entity 1, CAMP RECEPTOR PROTEIN 209 residues - 23555.3638 Da.

1   VALLEUGLYLYSPROGLNTHRASPPROTHR
2   LEUGLUTRPPHELEUSERHISCYSHISILE
3   HISLYSTYRPROSERLYSSERTHRLEUILE
4   HISGLNGLYGLULYSALAGLUTHRLEUTYR
5   TYRILEVALLYSGLYSERVALALAVALLEU
6   ILELYSASPGLUGLUGLYLYSGLUMETILE
7   LEUSERTYRLEUASNGLNGLYASPPHEILE
8   GLYGLULEUGLYLEUPHEGLUGLUGLYGLN
9   GLUARGSERALATRPVALARGALALYSTHR
10   ALACYSGLUVALALAGLUILESERTYRLYS
11   LYSPHEARGGLNLEUILEGLNVALASNPRO
12   ASPILELEUMETARGLEUSERALAGLNMET
13   ALAARGARGLEUGLNVALLEUILEGLULYS
14   VALGLYASNLEUALAPHELEUASPVALTHR
15   GLYARGILEALAGLNTHRLEULEUASNLEU
16   ALALYSGLNPROASPALAMETTHRHISPRO
17   ASPGLYMETGLNILELYSILETHRARGGLN
18   GLUILEGLYGLNILEVALGLYCYSSERARG
19   GLUTHRVALGLYARGILELEULYSMETLEU
20   GLUASPGLNASNLEUILESERALAHISGLY
21   LYSTHRILEVALVALTYRGLYTHRARG

Samples:

sample_1: CAMP RECEPTOR PROTEIN, [U-13C; U-15N], 0.2 mM

sample_conditions_1: ionic strength: 500.000 mM; pH: 6.000; pressure: 1.000 atm; temperature: 305.000 K

Experiments:

NameSampleSample stateSample conditions
HNCAsample_1solutionsample_conditions_1
HNCACBsample_1solutionsample_conditions_1
HNCOsample_1solutionsample_conditions_1
HNCOCAsample_1solutionsample_conditions_1
3D-15N-NOESYsample_1solutionsample_conditions_1
3D-13C-NOESYsample_1solutionsample_conditions_1
HNCAsample_1solutionsample_conditions_1
HNCACBsample_1solutionsample_conditions_1
HNCOsample_1solutionsample_conditions_1
HNCOCAsample_1solutionsample_conditions_1
3D-15N-NOESYsample_1solutionsample_conditions_1
3D-13C-NOESYsample_1solutionsample_conditions_1

Software:

AutoDep v4.3, PDBe - collection

CARA vany - chemical shift assignment

CNS vany, Brunger, Adams, Clore, Gros, Nilges and Read - chemical shift assignment

HADDOCK vany - chemical shift calculation

NMRPipe vany - chemical shift assignment

NMR spectrometers:

  • Bruker AvanceIII 700 MHz
  • Varian VNMRS 600 MHz

Related Database Links:

UNP CRP_ECOLI
BMRB 19145 4388
PDB
DBJ BAB37631 BAC10627 BAE75576 BAE77933 BAG79143
EMBL CAA04867 CAA61609 CAC07215 CAD08147 CAE12690
GB AAA23601 AAA25058 AAA26515 AAA27039 AAA58154
PIR A44903 AG1002
REF NP_312235 NP_417816 NP_458435 NP_462369 NP_709132
SP P0A2T6 P0A2T7 P0ACJ8 P0ACJ9 P0ACK0
AlphaFold Q2M723 P0A2T6 P0ACK0 P0ACJ9 P0ACJ8 P0A2T7