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Biological Magnetic Resonance Data Bank


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BMRB Entry 17850

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR17850
MolProbity Validation Chart

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Title: Solution structure of Ca2+/CNA1 peptide-bound yCaM   PubMed: 22280008

Deposition date: 2011-08-10 Original release date: 2012-02-01

Authors: Ogura, Kenji; Takahashi, Kiyohiro; Kobashigawa, Yoshihiro; Yoshida, Ryosuke; Itoh, Hiroyuki; Yazawa, Michio; Inagaki, Fuyuhiko

Citation: Ogura, Kenji; Kumeta, Hiroyuki; Takahasi, Kiyohiro; Kobashigawa, Yoshihiro; Yoshida, Ryosuke; Itoh, Hiroyuki; Yazawa, Michio; Inagaki, Fuyuhiko. "Solution structures of yeast Saccharomyces cerevisiae calmodulin in calcium- and target peptide-bound states reveal similarities and differences to vertebrate calmodulin."  Genes Cells 17, 159-172 (2012).

Assembly members:
yCaM_GS_CNA1, polymer, 176 residues, 19281.693 Da.
CA, non-polymer, 40.078 Da.

Natural source:   Common Name: baker   Taxonomy ID: 4932   Superkingdom: not available   Kingdom: not available   Genus/species: Eukaryota Fungi

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

Entity Sequences (FASTA):
yCaM_GS_CNA1: GSSNLTEEQIAEFKEAFALF DKDNNGSISSSELATVMRSL GLSPSEAEVNDLMNEIDVDG NHQIEFSEFLALMSRQLKSN DSEQELLEAFKVFDKNGDGL ISAAELKHVLTSIGEKLTDA EVDDMLREVSDGSGEINIQQ FAALLSKGSSTGTRRKALRN KILAIAKVSRMFSVLR

Data sets:
Data typeCount
13C chemical shifts757
15N chemical shifts199
1H chemical shifts1248

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1yCaM_GS_CNA11
2CALCIUM ION_12
3CALCIUM ION_22
4CALCIUM ION_32

Entities:

Entity 1, yCaM_GS_CNA1 176 residues - 19281.693 Da.

1   GLYSERSERASNLEUTHRGLUGLUGLNILE
2   ALAGLUPHELYSGLUALAPHEALALEUPHE
3   ASPLYSASPASNASNGLYSERILESERSER
4   SERGLULEUALATHRVALMETARGSERLEU
5   GLYLEUSERPROSERGLUALAGLUVALASN
6   ASPLEUMETASNGLUILEASPVALASPGLY
7   ASNHISGLNILEGLUPHESERGLUPHELEU
8   ALALEUMETSERARGGLNLEULYSSERASN
9   ASPSERGLUGLNGLULEULEUGLUALAPHE
10   LYSVALPHEASPLYSASNGLYASPGLYLEU
11   ILESERALAALAGLULEULYSHISVALLEU
12   THRSERILEGLYGLULYSLEUTHRASPALA
13   GLUVALASPASPMETLEUARGGLUVALSER
14   ASPGLYSERGLYGLUILEASNILEGLNGLN
15   PHEALAALALEULEUSERLYSGLYSERSER
16   THRGLYTHRARGARGLYSALALEUARGASN
17   LYSILELEUALAILEALALYSVALSERARG
18   METPHESERVALLEUARG

Entity 2, CALCIUM ION_1 - Ca - 40.078 Da.

1   CA

Samples:

13C15N: yCaM_GS_CNA1, [U-99% 13C; U-99% 15N], 1 mM; MES 20 mM; sodium chloride 150 mM; CaCl2 5 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 150 mM; pH: 6.3; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQC13C15Nisotropicsample_conditions_1
2D 1H-13C HSQC aliphatic13C15Nisotropicsample_conditions_1
2D 1H-13C HSQC aromatic13C15Nisotropicsample_conditions_1
3D HNCO13C15Nisotropicsample_conditions_1
3D HN(CO)CA13C15Nisotropicsample_conditions_1
3D HNCA13C15Nisotropicsample_conditions_1
3D CBCA(CO)NH13C15Nisotropicsample_conditions_1
3D HNCACB13C15Nisotropicsample_conditions_1
3D HBHA(CO)NH13C15Nisotropicsample_conditions_1
3D C(CO)NH13C15Nisotropicsample_conditions_1
3D HCCH-TOCSY aliphatic13C15Nisotropicsample_conditions_1
3D CCH-TOCSY13C15Nisotropicsample_conditions_1
2D HbCbCgCdHd13C15Nisotropicsample_conditions_1
2D HbCbCgCdCeHe13C15Nisotropicsample_conditions_1
3D 1H-15N NOESY13C15Nisotropicsample_conditions_1
3D 1H-13C NOESY aliphatic13C15Nisotropicsample_conditions_1
3D 1H-13C NOESY aromatic13C15Nisotropicsample_conditions_1
3D HCCH-TOCSY aromatic13C15Nisotropicsample_conditions_1

Software:

VNMR v6.1C, Varian - collection

NMRPipe v5.2, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY v3.113, Goddard - chemical shift assignment, peak picking, refinement

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

TALOS v2003.027.13.05, Cornilescu, Delaglio and Bax - structure solution

RNMRTK vv3, Mobli M, Maciejewski MW, Gryk MR, Hoch JC. - processing

NMR spectrometers:

  • Varian INOVA 800 MHz
  • Varian INOVA 800 MHz
  • Varian INOVA 600 MHz

Related Database Links:

PDB
DBJ GAA21657
EMBL CAA55612 CAA85064 CAG58389 CAR27417 CBK39182
GB AAA34504 AAC68888 AAS56510 AHY74589 AJP37188
REF NP_009667 XP_001642859 XP_002496350 XP_003678123 XP_003680602
SP P06787
TPG DAA07228

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