BMRB Entry 25069

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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/BMR25069
MolProbity Validation Chart

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Title:
Solution structure of human Ca2+-loaded S100A4 cys-free mutant
Deposition date:
2014-07-03
Original release date:
2015-07-13
Authors:
Cho, Ching-Chang; Hung, Kuo-Wei; Yu, Chin
Citation:

Citation: Cho, Ching-Chang; Hung, Kuo-Wei; Gorja, Dhilli; Yu, Chin. "The solution structure of human calcium-bound S100A4 mutated at four cysteine loci"  J. Biomol. NMR 62, 233-238 (2015).
PubMed: 25855140

Assembly members:

Assembly members:
S100A4, polymer, 101 residues, 11681.374 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: pET21a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
S100A4: MASPLEKALDVMVSTFHKYS GKEGDKFKLNKSELKELLTR ELPSFLGKRTDEAAFQKLMS NLDSNRDNEVDFQEYSVFLS SIAMMSNEFFEGFPDKQPRK K

Data sets:
Data typeCount
13C chemical shifts400
15N chemical shifts103
1H chemical shifts634

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1S100A4_11
2S100A4_21

Entities:

Entity 1, S100A4_1 101 residues - 11681.374 Da.

1   METALASERPROLEUGLULYSALALEUASP
2   VALMETVALSERTHRPHEHISLYSTYRSER
3   GLYLYSGLUGLYASPLYSPHELYSLEUASN
4   LYSSERGLULEULYSGLULEULEUTHRARG
5   GLULEUPROSERPHELEUGLYLYSARGTHR
6   ASPGLUALAALAPHEGLNLYSLEUMETSER
7   ASNLEUASPSERASNARGASPASNGLUVAL
8   ASPPHEGLNGLUTYRSERVALPHELEUSER
9   SERILEALAMETMETSERASNGLUPHEPHE
10   GLUGLYPHEPROASPLYSGLNPROARGLYS
11   LYS

Samples:

sample_1: S100A4, [U-100% 13C; U-100% 15N], 1 mM; TRIS 16 mM; sodium chloride 8 mM; calcium chloride 6 mM; EDTA 0.1 mM; sodium azide 0.34 mM

sample_conditions_1: ionic strength: 0.02 M; pH: 6; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 13C F1-filtered, F3-edited NOESY-HSQC'sample_1isotropicsample_conditions_1

Software:

ARIA, Linge, O'Donoghue and Nilges - refinement, structure solution

VNMRJ, Varian - collection, processing

SPARKY, Goddard - chemical shift assignment, data analysis

NMR spectrometers:

  • Varian VNMRS 700 MHz

Related Database Links:

PDB
REF XP_003892716

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