BMRB Entry 17360

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR17360
MolProbity Validation Chart

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Title:
Solution structure of Ca2+/calmodulin complexed with a peptide representing the calmodulin-binding domain of calmodulin kinase I
Deposition date:
2010-12-13
Original release date:
2011-03-07
Authors:
Gifford, Jessica; Ishida, Hiroaki; Vogel, Hans
Citation:

Citation: Gifford, Jessica; Ishida, Hiroaki; Vogel, Hans. "Fast methionine-based solution structure determination of calcium-calmodulin complexes."  J. Biomol. NMR 50, 71-81 (2011).
PubMed: 21360154

Assembly members:

Assembly members:
entity_1, polymer, 148 residues, 16721.465 Da.
entity_2, polymer, 22 residues, 2606.146 Da.
CA, non-polymer, 40.078 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: recombinant technology   Host organism: Escherichia coli   Vector: pET30b(+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: ADQLTEEQIAEFKEAFSLFD KDGDGTITTKELGTVMRSLG QNPTEAELQDMINEVDADGN GTIDFPEFLTMMARKMKDTD SEEEIREAFRVFDKDGNGYI SAAELRHVMTNLGEKLTDEE VDEMIREADIDGDGQVNYEE FVQMMTAK
entity_2: AKSKWKQAFNATAVVRHMRK LQ

Data sets:
Data typeCount
13C chemical shifts9
1H chemical shifts185

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22
3CALCIUM ION_13
4CALCIUM ION_23
5CALCIUM ION_33
6CALCIUM ION_43

Entities:

Entity 1, entity_1 148 residues - 16721.465 Da.

1   ALAASPGLNLEUTHRGLUGLUGLNILEALA
2   GLUPHELYSGLUALAPHESERLEUPHEASP
3   LYSASPGLYASPGLYTHRILETHRTHRLYS
4   GLULEUGLYTHRVALMETARGSERLEUGLY
5   GLNASNPROTHRGLUALAGLULEUGLNASP
6   METILEASNGLUVALASPALAASPGLYASN
7   GLYTHRILEASPPHEPROGLUPHELEUTHR
8   METMETALAARGLYSMETLYSASPTHRASP
9   SERGLUGLUGLUILEARGGLUALAPHEARG
10   VALPHEASPLYSASPGLYASNGLYTYRILE
11   SERALAALAGLULEUARGHISVALMETTHR
12   ASNLEUGLYGLULYSLEUTHRASPGLUGLU
13   VALASPGLUMETILEARGGLUALAASPILE
14   ASPGLYASPGLYGLNVALASNTYRGLUGLU
15   PHEVALGLNMETMETTHRALALYS

Entity 2, entity_2 22 residues - 2606.146 Da.

N-terminal acetylation C-terminal amidation

1   ALALYSSERLYSTRPLYSGLNALAPHEASN
2   ALATHRALAVALVALARGHISMETARGLYS
3   LEUGLN

Entity 3, CALCIUM ION_1 - Ca - 40.078 Da.

1   CA

Samples:

sample_1: entity_1, [U-13C; U-15N], 0.95 mM; entity_2 1.05 mM; CALCIUM ION 4 mM; DSS 0.5 mM; potassium chloride 100 mM; Bis-Tris 20 mM; sodium azide 0.03%

sample_2: entity_1, [U-2H; U-15N], 0.66 mM; entity_2 0.40 mM; Bis-Tris 20 mM; potassium chloride 100 mM; CALCIUM ION 4 mM; sodium azide 0.03%; DSS 0.5 mM

sample_3: entity_1, [1H/13C-methyl Met; U-2H; U-15N], 0.64 mM; entity_2 0.83 mM; Bis-Tris 20 mM; potassium chloride 100 mM; CALCIUM ION 4 mM; sodium azide 0.03%; DSS 0.5 mM

sample_4: entity_1, [U-13C; U-15N], 0.95 mM; entity_2 1.05 mM; Bis-Tris 20 mM; potassium chloride 300 mM; CALCIUM ION 4 mM; sodium azide 0.03%; DSS 0.5 mM

sample_5: entity_1, [U-13C; U-15N], 0.95 mM; entity_2 1.05 mM; Bis-Tris 20 mM; potassium chloride 300 mM; CALCIUM ION 4 mM; sodium azide 0.03%; DSS 0.5 mM; Pf1 phage 16 w/v

sample_conditions_1: ionic strength: 0.1 M; pH: 6.8; pressure: 1 atm; temperature: 303 K

sample_conditions_2: ionic strength: 0.3 M; pH: 6.8; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_3isotropicsample_conditions_1
2D 1H-1H COSYsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_3isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
2D HMBCsample_1isotropicsample_conditions_1
3D LRCHsample_1isotropicsample_conditions_1
F2-filtered 2D 1H-1H NOESYsample_2isotropicsample_conditions_1
2D 1H-15N IPAP HSQCsample_4isotropicsample_conditions_2
2D 1H-15N IPAP HSQCsample_5anisotropicsample_conditions_2

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRView, Johnson, One Moon Scientific - chemical shift assignment, peak picking

CYANA, Guntert, Mumenthaler and Wuthrich - chemical shift assignment, refinement, structure solution

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution

ProcheckNMR, Laskowski and MacArthur - data analysis

TALOS, Cornilescu, Delaglio and Bax - data analysis

Molmol, Koradi, Billeter and Wuthrich - data analysis

xwinnmr, Bruker Biospin - collection

NMR spectrometers:

  • Bruker Avance 500 MHz

Related Database Links:

BMRB 15184 15185 15186 15187 15188 15191 15470 15624 15650 15852 1634 16418 16465 1648 16764 17264 17771 17807 18027 18028 18556 19036 19238 19586 19604 25253 25257 26503 26626 26627 4056 4270 4284 4310 5286 5287 6798 7018
PDB
DBJ BAA08302 BAA11896 BAA19786 BAA19787 BAA19788 BAE22345 BAE41623 BAG37428 BAG70091 BAG70221
EMBL CAA10601 CAA32050 CAA32062 CAA32119 CAA32120
GB AAA35635 AAA35641 AAA37365 AAA40862 AAA40863 AAA66944 AAA99458 AAH14825 AAH71177 AAI06755
PIR JC1305 MCON
PRF 0409298A 0608335A 2024225A
REF NP_001008160 NP_001009759 NP_001027633 NP_001039714 NP_001040234 NP_001070336 NP_001177124 NP_001244800 NP_003647 NP_598687
SP O02367 O16305 O96081 P02594 P05932 Q14012 Q63450 Q91YS8
TPG DAA13808 DAA18029 DAA19590 DAA24777 DAA24988 DAA17160
AlphaFold O02367 O16305 O96081 P02594 P05932 Q14012 Q63450 Q91YS8