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 18087

Title: solution structure of human apo-S100A1 C85M

Authors: Budzinska, Monika; Jaremko, Lukasz; Jaremko, Mariusz; Zdanowski, Konrad; Zhukov, Igor; Bierzynski, Andrzej; Ejchart, Andrzej

Citation: Budzinska, Monika; Jaremko, Lukasz; Jaremko, Mariusz; Zdanowski, Konrad; Zhukov, Igor; Bierzynski, Andrzej; Ejchart, Andrzej. "Chemical Shift Assignments and solution structure of human apo-S100A1 C85M mutant"  Not known ., .-..

Assembly members:
S100A1C85M, polymer, 93 residues, 10453.736 Da.

Natural source:   Common Name: E. 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):
S100A1C85M: GSELETAMETLINVFHAHSG KEGDKYKLSKKELKELLQTE LSGFLDAQKDVDAVDKVMKE LDENGDGEVDFQEYVVLVAA LTVAMNNFFWENS

Data typeCount
13C chemical shifts396
15N chemical shifts95
1H chemical shifts658
heteronuclear NOE values194
T1 relaxation values188
T2 relaxation values190

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1S100A1C85M, chain 11
2S100A1C85M, chain 21

Entities:

Entity 1, S100A1C85M, chain 1 93 residues - 10453.736 Da.

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

Samples:

sample_1: TRIS-d11 50 mM; D2O 10%; sodium chloride 50 mM; S100A1C85M, [U-99% 13C; U-99% 15N], 1 mM; H2O 90%

sample_2: TRIS-d11 50 mM; sodium chloride 50 mM; S100A1C85M, [U-99% 13C; U-99% 15N], 1 mM; D2O 100%

sample_3: TRIS-d11 50 mM; D2O 10%; sodium chloride 50 mM; S100A1C85M, [U-99% 15N], 1 mM; H2O 90%

sample_conditions_1: ionic strength: 50 mM; pH: 6.8; pressure: 1 atm; temperature: 310 K

sample_conditions_2: ionic strength: 50 mM; pH: 7.2; pressure: 1 atm; temperature: 310 K

sample_conditions_3: ionic strength: 50 mM; pH: 6.8; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQC NH2 onlysample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_2isotropicsample_conditions_2
2D 1H-13C HSQC aromaticsample_2isotropicsample_conditions_2
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_2
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_2
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_2
2D 1H-15N heteronuclear NOEsample_3isotropicsample_conditions_3
2D 1H-15N heteronuclear NOEsample_3isotropicsample_conditions_3
2D 1H-15N heteronuclear NOEsample_3isotropicsample_conditions_3
2D 1H-15N T1 relaxationsample_3isotropicsample_conditions_3
2D 1H-15N T1 relaxationsample_3isotropicsample_conditions_3
2D 1H-15N T1 relaxationsample_3isotropicsample_conditions_3
2D 1H-15N T2 relaxationsample_3isotropicsample_conditions_3
2D 1H-15N T2 relaxationsample_3isotropicsample_conditions_3
2D 1H-15N T2 relaxationsample_3isotropicsample_conditions_3

Software:

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

CYANA, Guntert, Mumenthaler and Wuthrich - constraints assignments, data analysis, structure solution

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

SPARKY, Goddard - chemical shift assignment, data analysis

CARA, Keller and Wuthrich - chemical shift assignment

MARS, Jung, Zweckstetter - automated chemical shift assignments

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 17857 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