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Biological Magnetic Resonance Data Bank


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BMRB Entry 15242

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15242
MolProbity Validation Chart

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Title: FHA domain of NIPP1   PubMed: 18253837

Deposition date: 2007-05-08 Original release date: 2007-06-13

Authors: Kumeta, Hiroyuki; Ogura, Kenji; Fujioka, Yuko; Tanuma, Nobuhiro; Kikuchi, Kunimi; Inagaki, Fuyuhiko

Citation: Kumeta, Hiroyuki; Ogura, Kenji; Adachi, Souichirou; Fujioka, Yuko; Tanuma, Kiminobu; Kikuchi, Kunimi; Inagaki, Fuyuhiko. "The NMR structure of the NIPP1 FHA domain"  J. Biomol. NMR 40, 219-224 (2008).

Assembly members:
FHA_domain, polymer, 140 residues, 14823.263 Da.

Natural source:   Common Name: mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

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

Entity Sequences (FASTA):
FHA_domain: GPLGSPNSMAAAVNSGSSLP LFDCPTWAGKPPPGLHLDVV KGDKLIEKLIIDEKKYYLFG RNPDLCDFTIDHQSCSRVHA ALVYHKHLKRVFLIDLNSTH GTFLGHIRLEPHKPQQIPID STVSFGASTRAYTLREKPQT

Data sets:
Data typeCount
13C chemical shifts608
15N chemical shifts134
1H chemical shifts950

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1FHA domain1

Entities:

Entity 1, FHA domain 140 residues - 14823.263 Da.

1   GLYPROLEUGLYSERPROASNSERMETALA
2   ALAALAVALASNSERGLYSERSERLEUPRO
3   LEUPHEASPCYSPROTHRTRPALAGLYLYS
4   PROPROPROGLYLEUHISLEUASPVALVAL
5   LYSGLYASPLYSLEUILEGLULYSLEUILE
6   ILEASPGLULYSLYSTYRTYRLEUPHEGLY
7   ARGASNPROASPLEUCYSASPPHETHRILE
8   ASPHISGLNSERCYSSERARGVALHISALA
9   ALALEUVALTYRHISLYSHISLEULYSARG
10   VALPHELEUILEASPLEUASNSERTHRHIS
11   GLYTHRPHELEUGLYHISILEARGLEUGLU
12   PROHISLYSPROGLNGLNILEPROILEASP
13   SERTHRVALSERPHEGLYALASERTHRARG
14   ALATYRTHRLEUARGGLULYSPROGLNTHR

Samples:

sample: FHA domain, [U-100% 13C; U-100% 15N], 0.5 mM; H2O 90%; D2O 10%

sample_conditions: ionic strength: 0.1 M; pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsampleisotropicsample_conditions
2D 1H-13C HSQCsampleisotropicsample_conditions
3D CBCA(CO)NHsampleisotropicsample_conditions
3D HNCOsampleisotropicsample_conditions
3D HNCAsampleisotropicsample_conditions
3D HNCACBsampleisotropicsample_conditions
3D HBHA(CO)NHsampleisotropicsample_conditions
3D HN(CO)CAsampleisotropicsample_conditions
3D HCCH-TOCSYsampleisotropicsample_conditions
3D (H)CCH-TOCSYsampleisotropicsample_conditions
3D HACANsampleisotropicsample_conditions
2D HbCbCgCdHdsampleisotropicsample_conditions
2D HbCbCgCdCeHesampleisotropicsample_conditions
3D 1H-15N NOESYsampleisotropicsample_conditions
3D 1H-13C NOESYsampleisotropicsample_conditions
3D (HCA)CO(CA)NHsampleisotropicsample_conditions

Software:

VNMR v6.1C, Varian - collection

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

SPARKY v3.110, Goddard - chemical shift assignment, peak picking, refinement

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

NMR spectrometers:

  • Varian INOVA 800 MHz
  • Varian INOVA 600 MHz

Related Database Links:

BMRB 18448
PDB
DBJ BAC27653 BAF84766 BAG65401 BAG73611
EMBL CAA90625
GB AAD22486 AAD24669 AAD31541 AAH01597 AAH25479
REF NP_001026062 NP_001101381 NP_001230343 NP_001253391 NP_001277654
SP Q12972 Q28147 Q8R3G1
TPG DAA32062

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