BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 17857

Title: Chemical Shift Assignments and solution structure of human apo-S100A1 E32Q mutant

Authors: Ruszczynska-Bartnik, Katarzyna; Zdanowski, Konrad; Zhukov, Igor; Bierzynski, Andrzej; Ejchart, Andrzej

Citation: Ruszczynska-Bartnik, Katarzyna; Zdanowski, Konrad; Zhukov, Igor; Bierzynski, Andrzej; Ejchart, Andrzej. "Chemical Shift Assignments and solution structure of human apo-S100A1 E32Q mutant"  Not known ., .-..

Assembly members:
S100A1E32Q_calcium_binding_protein, polymer, 93 residues, 10424.699 Da.

Natural source:   Common Name: Escherichia coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

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

Entity Sequences (FASTA):
S100A1E32Q_calcium_binding_protein: GSELETAMETLINVFHAHSG KEGDKYKLSKKQLKELLQTE LSGFLDAQKDVDAVDKVMKE LDENGDGEVDFQEYVVLVAA LTVACNNFFWENS

Data typeCount
13C chemical shifts415
15N chemical shifts101
1H chemical shifts663
heteronuclear NOE values230
T1 relaxation values231
T2 relaxation values231

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1S100A1E32Q_11
2S100A1E32Q_21

Entities:

Entity 1, S100A1E32Q_1 93 residues - 10424.699 Da.

1   GLYSERGLULEUGLUTHRALAMETGLUTHR
2   LEUILEASNVALPHEHISALAHISSERGLY
3   LYSGLUGLYASPLYSTYRLYSLEUSERLYS
4   LYSGLNLEULYSGLULEULEUGLNTHRGLU
5   LEUSERGLYPHELEUASPALAGLNLYSASP
6   VALASPALAVALASPLYSVALMETLYSGLU
7   LEUASPGLUASNGLYASPGLYGLUVALASP
8   PHEGLNGLUTYRVALVALLEUVALALAALA
9   LEUTHRVALALACYSASNASNPHEPHETRP
10   GLUASNSER

Samples:

sample_1: S100A1E32Q, [U-98% 13C; U-98% 15N], 1 mM; TRIS-d11 50 mM; EDTA 1 mM; sodium chloride 50 mM; D2O 10%; H2O 90%

sample_conditions_1: ionic strength: 0.05 M; pH: 7.0; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
2D 1H-15N T2 relaxationsample_1isotropicsample_conditions_1
2D 1H-15N T1 relaxationsample_1isotropicsample_conditions_1
2D 1H-15N heteronuclear NOEsample_1isotropicsample_conditions_1

Software:

Analysis-CCPN v2.1.5, CCPN - chemical shift assignment

CARA v1.8, Keller and Wuthrich - chemical shift assignment

SPARKY, Goddard - data analysis

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

X-PLOR NIH v2.26, Schwieters, Kuszewski, Tjandra and Clore - structure solution

NMR spectrometers:

  • Varian INOVA 400 MHz
  • Varian UnityPlus 500 MHz
  • Varian Varian NMR System 700 MHz
  • Varian Varian NMR System 800 MHz

Related Database Links:

BMRB 16360 18087 18088 18089 18101 18230 18231 18545
PDB
DBJ BAE90380 BAG35086 BAG70130 BAG70260
EMBL CAA41107 CAH90674
GB AAH14392 AAI41992 AAI48020 AAP35584 AAP36328
PRF 2003367A
REF NP_001092512 NP_001127319 NP_001270255 NP_006262 XP_001111015
SP P02639 P23297 Q5RC36
TPG DAA31796