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Biological Magnetic Resonance Data Bank


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BMRB Entry 18818

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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/BMR18818
MolProbity Validation Chart

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Title: Solution structure and dynamics of human S100A14   PubMed: 23197251

Deposition date: 2012-11-05 Original release date: 2013-01-22

Authors: Bertini, Ivano; Borsi, Valentina; Cerofolini, Linda; Das Gupta, Soumyasri; Fragai, Marco; Luchinat, Claudio

Citation: Bertini, Ivano; Borsi, Valentina; Cerofolini, Linda; Das Gupta, Soumyasri; Fragai, Marco; Luchinat, Claudio. "Solution structure and dynamics of human S100A14."  J. Biol. Inorg. Chem. 18, 183-194 (2013).

Assembly members:
entity, polymer, 104 residues, 11677.180 Da.

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

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

Entity Sequences (FASTA):
entity: MGQCRSANAEDAQEFSDVER AIETLIKNFHQYSVEGGKET LTPSELRDLVTQQLPHLMPS NCGLEEKIANLGSCNDSKLE FRSFWELIGEAAKSVKLERP VRGH

Data sets:
Data typeCount
13C chemical shifts417
15N chemical shifts102
1H chemical shifts558

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1human S100A14, 11
2human S100A14, 21

Entities:

Entity 1, human S100A14, 1 104 residues - 11677.180 Da.

1   METGLYGLNCYSARGSERALAASNALAGLU
2   ASPALAGLNGLUPHESERASPVALGLUARG
3   ALAILEGLUTHRLEUILELYSASNPHEHIS
4   GLNTYRSERVALGLUGLYGLYLYSGLUTHR
5   LEUTHRPROSERGLULEUARGASPLEUVAL
6   THRGLNGLNLEUPROHISLEUMETPROSER
7   ASNCYSGLYLEUGLUGLULYSILEALAASN
8   LEUGLYSERCYSASNASPSERLYSLEUGLU
9   PHEARGSERPHETRPGLULEUILEGLYGLU
10   ALAALALYSSERVALLYSLEUGLUARGPRO
11   VALARGGLYHIS

Samples:

sample_1: human S100A14 mM; sodium chloride 100 mM; DTT 5 mM; MES 30 mM

sample_conditions_1: ionic strength: 0.2 M; pH: 6.5; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
2D CONsample_1isotropicsample_conditions_1
2D CACOsample_1isotropicsample_conditions_1
2D CBCACOsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1

Software:

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

AMBER v11, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

CARA v2, (CARA) Keller, R.L.J. - chemical shift assignment

CING, (CING) Vuister, G.W. - structure validation

NMR spectrometers:

  • Bruker Avance 900 MHz
  • Bruker Avance 800 MHz
  • Bruker Avance 700 MHz
  • Bruker DRX 500 MHz

Related Database Links:

PDB
GB AAG01893 AAH05019 AAM19206 ADQ32442 AIC52003
REF NP_001177097 NP_065723 XP_001139808 XP_001140053 XP_002760048
SP Q9HCY8

Download simulated HSQC data in one of the following formats:
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