BMRB Entry 18027

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18027
MolProbity Validation Chart

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Title:
Solution NMR structure of CaM bound to iNOS CaM binding domain peptide
Deposition date:
2011-10-29
Original release date:
2012-05-15
Authors:
Piazza, Michael; Futrega, Kathryn; Spratt, Donald; Dieckmann, Thorsten; Guillemette, J.
Citation:

Citation: Piazza, Michael; Futrega, Kathryn; Spratt, Donald; Dieckmann, Thorsten; Guillemette, J.. "Structure and Dynamics of Calmodulin (CaM) Bound to Nitric Oxide Synthase Peptides: Effects of a Phosphomimetic CaM Mutation"  Biochemistry 51, 3651-3661 (2012).
PubMed: 22486744

Assembly members:

Assembly members:
CaM, polymer, 148 residues, 16721.465 Da.
iNOS, polymer, 17 residues, 1967.644 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: pET9dCaM

Entity Sequences (FASTA):

Entity Sequences (FASTA):
CaM: ADQLTEEQIAEFKEAFSLFD KDGDGTITTKELGTVMRSLG QNPTEAELQDMINEVDADGN GTIDFPEFLTMMARKMKDTD SEEEIREAFRVFDKDGNGYI SAAELRHVMTNLGEKLTDEE VDEMIREADIDGDGQVNYEE FVQMMTAK
iNOS: LKVLVKAVLFACMLMRK

Data sets:
Data typeCount
13C chemical shifts431
15N chemical shifts162
1H chemical shifts986

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CaM1
2iNOS2

Entities:

Entity 1, CaM 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, iNOS 17 residues - 1967.644 Da.

1   LEULYSVALLEUVALLYSALAVALLEUPHE
2   ALACYSMETLEUMETARGLYS

Samples:

sample_1: entity_1, [U-99% 13C; U-99% 15N], 1.0 mM; entity_2 1.0 mM; potassium chloride 100 mM; calcium chloride 10 mM; sodium azide 0.2 mM; H2O 90%; D2O 10%

sample_2: entity_1 1.0 mM; entity_2, [U-99% 13C; U-99% 15N], 1.0 mM; potassium chloride 100 mM; calcium chloride 10 mM; sodium azide 0.2 mM; H2O 90%; D2O 10%

sample_conditions_1: pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_2isotropicsample_conditions_1

Software:

CNSSOLVE, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

NMR spectrometers:

  • Bruker DRX 600 MHz
  • Bruker DRX 700 MHz

Related Database Links:

BMRB 15184 15185 15186 15187 15188 15191 15470 15624 15650 15852 1634 16418 16465 1648 16764 17264 17360 17771 17807 18028 18556 19036 19238 19586 19604 25253 25257 26503 26626 26627 4056 4270 4284 4310
PDB
DBJ BAA08302 BAA11896 BAA19786 BAA19787 BAA19788 BAA05531 BAA37123 BAG65119
EMBL CAA10601 CAA32050 CAA32062 CAA32119 CAA32120 CAA51512
GB AAA35635 AAA35641 AAA37365 AAA40862 AAA40863 AAA36375 AAA56666 AAA59171 AAB49041 AAB60366
PIR JC1305 MCON
PRF 0409298A 0608335A 2001203A 2019232A
REF NP_001008160 NP_001009759 NP_001027633 NP_001039714 NP_001040234 NP_000616 XP_001106048 XP_001106185 XP_001106245 XP_002827195
SP O02367 O16305 O96081 P02594 P05932 P35228
TPG DAA13808 DAA18029 DAA19590 DAA24777 DAA24988
AlphaFold O02367 O16305 O96081 P02594 P05932 P35228

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