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 15593

Title: Solution structure of human protein C6orf130, a putative macro domain

Deposition date: 2007-12-12 Original release date: 2008-01-23

Authors: Volkman, B.; Lytle, B.; Peterson, F.

Citation: Lytle, B.; Peterson, F.; Volkman, B.. "Solution structure of human C6orf130, a putative macro domain"  To be published ., .-..

Assembly members:
C6orf130, polymer, 160 residues, 18050.891 Da.

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

Experimental source:   Production method: cell free synthesis   Host organism: wheat germ - cell free

Entity Sequences (FASTA):
C6orf130: GHHHHHHLEASSLNEDPEGS RITYVKGDLFACPKTDSLAH CISEDCRMGAGIAVLFKKKF GGVQELLNQQKKSGEVAVLK RDGRYIYYLITKKRASHKPT YENLQKSLEAMKSHCLKNGV TDLSMPRIGCGLDRLQWENV SAMIEEVFEATDIKITVYTL

Data sets:
Data typeCount
13C chemical shifts663
15N chemical shifts164
1H chemical shifts1039

Time Domain Data

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1C6orf1301

Entities:

Entity 1, C6orf130 160 residues - 18050.891 Da.

1   GLYHISHISHISHISHISHISLEUGLUALA
2   SERSERLEUASNGLUASPPROGLUGLYSER
3   ARGILETHRTYRVALLYSGLYASPLEUPHE
4   ALACYSPROLYSTHRASPSERLEUALAHIS
5   CYSILESERGLUASPCYSARGMETGLYALA
6   GLYILEALAVALLEUPHELYSLYSLYSPHE
7   GLYGLYVALGLNGLULEULEUASNGLNGLN
8   LYSLYSSERGLYGLUVALALAVALLEULYS
9   ARGASPGLYARGTYRILETYRTYRLEUILE
10   THRLYSLYSARGALASERHISLYSPROTHR
11   TYRGLUASNLEUGLNLYSSERLEUGLUALA
12   METLYSSERHISCYSLEULYSASNGLYVAL
13   THRASPLEUSERMETPROARGILEGLYCYS
14   GLYLEUASPARGLEUGLNTRPGLUASNVAL
15   SERALAMETILEGLUGLUVALPHEGLUALA
16   THRASPILELYSILETHRVALTYRTHRLEU

Samples:

sample: C6orf130, [U-100% 13C; U-100% 15N], 0.55 mM; BisTris 20 mM; sodium chloride 200 mM; DTT 2 mM; D2O, [U-100% 2H], 7%; H2O 93%

sample_conditions_1: ionic strength: 200 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D_15N-separated_NOESYsampleisotropicsample_conditions_1
3D_13C-separated_NOESYsampleisotropicsample_conditions_1
3D_13C-separated_NOESY (AROMATIC)sampleisotropicsample_conditions_1

Software:

X-PLOR NIH v2.9.3, Schwieters, Kuszewski, Tjandra and Clore - refinement

xwinnmr v3.5, Bruker Biospin - collection

NMRPipe v2004, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

XEASY v1.3, Bartels et al. - data analysis

SPSCAN v1.1.0, Glaser - peak picking

GARANT v2.1, Bartels, Guntert, Billeter and Wuthrich - chemical shift assignment

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

NMR spectrometers:

  • Bruker DRX 600 MHz

Related Database Links:

BMRB 10164 17421
PDB
DBJ BAF83628 BAG36161
GB AAH11709 AIC53444 AIC58012 EAX04010 EAX04011
REF NP_001181654 NP_659500 XP_001117219 XP_001117235 XP_001174030
SP Q9Y530

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