BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 15549

Title: Solution Structure of Human C6orf115 Protein

Deposition date: 2007-11-08 Original release date: 2012-08-03

Authors: Lin, Jinzhong; Wang, Jinfeng

Citation: Lin, Jinzhong; Wang, Jinfeng. "Solution Structure of Human C6orf115 protein"  Not known ., .-..

Assembly members:
c6orf115, polymer, 89 residues, 10105.53 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):
c6orf115: MNVDHEVNLLVEEIHRLGSK NADGKLSVKFGVLFRDDKSA NLFEALVGTLKAAKRRKIVT YPGELLLQGVHDDVDIILLQ DLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts363
15N chemical shifts90
1H chemical shifts611

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1c6orf1151

Entities:

Entity 1, c6orf115 89 residues - 10105.53 Da.

1   METASNVALASPHISGLUVALASNLEULEU
2   VALGLUGLUILEHISARGLEUGLYSERLYS
3   ASNALAASPGLYLYSLEUSERVALLYSPHE
4   GLYVALLEUPHEARGASPASPLYSSERALA
5   ASNLEUPHEGLUALALEUVALGLYTHRLEU
6   LYSALAALALYSARGARGLYSILEVALTHR
7   TYRPROGLYGLULEULEULEUGLNGLYVAL
8   HISASPASPVALASPILEILELEULEUGLN
9   ASPLEUGLUHISHISHISHISHISHIS

Samples:

13C_15N-labeled: entity, [U-100% 13C; U-100% 15N], 1.5 mM; potassium chloride 20 mM; sodium acetate/acetic acid 50 mM; sodium azide 0.05%

15N-labeled: entity, [U-100% 15N], 1.5 mM; potassium chloride 20 mM; sodium acetate/acetic acid 50 mM; sodium azide 0.05%

sample_conditions_1: ionic strength: 0.07 M; pH: 4.4; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQC15N-labeledisotropicsample_conditions_1
2D 1H-13C HSQC13C_15N-labeledisotropicsample_conditions_1
3D CBCA(CO)NH13C_15N-labeledisotropicsample_conditions_1
3D HNCACB13C_15N-labeledisotropicsample_conditions_1
3D HCCH-TOCSY13C_15N-labeledisotropicsample_conditions_1
3D 1H-15N NOESY15N-labeledisotropicsample_conditions_1
3D 1H-15N TOCSY15N-labeledisotropicsample_conditions_1
3D 1H-13C NOESY13C_15N-labeledisotropicsample_conditions_1
3D HN(CO)CA13C_15N-labeledisotropicsample_conditions_1
3D HNCA13C_15N-labeledisotropicsample_conditions_1
3D H(CCO)NH13C_15N-labeledisotropicsample_conditions_1
3D HNCO13C_15N-labeledisotropicsample_conditions_1
3D CCH-TOCSY13C_15N-labeledisotropicsample_conditions_1

Software:

SPARKY v3.113, Goddard - data analysis

FELIX, Accelrys Software Inc. - processing

AutoAssign, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

NMR spectrometers:

  • Bruker DMX 600 MHz

Related Database Links:

PDB
GB AAF28958 AAF71102 AAH14953 AIC62228 EAW47902
REF NP_067066 XP_001159255 XP_002817467 XP_003121220 XP_003255842
SP Q9P1F3

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