BMRB Entry 15549

Name: Solution Structure of Human C6orf115 Protein
Published: 2012-08-03

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15549

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

Solution Structure of Human C6orf115 Protein

Deposition date:

2007-11-08

Original release date:

2012-08-03

Authors:

Lin, Jinzhong; Wang, Jinfeng

Citation:

Citation: Lin, Jinzhong; Wang, Jinfeng. "Solution Structure of Human C6orf115 protein" .

Assembly members:

Assembly members:
c6orf115, polymer, 89 residues, 10105.53 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: PET22b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
c6orf115: MNVDHEVNLLVEEIHRLGSK NADGKLSVKFGVLFRDDKSA NLFEALVGTLKAAKRRKIVT YPGELLLQGVHDDVDIILLQ DLEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	363
15N chemical shifts	90
1H chemical shifts	611

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	c6orf115	1

Entities:

Entity 1, c6orf115 89 residues - 10105.53 Da.

1

MET

ASN

VAL

ASP

HIS

GLU

VAL

ASN

LEU

2

VAL

GLU

ILE

HIS

ARG

LEU

GLY

SER

LYS

3

ASN

ALA

ASP

GLY

LYS

LEU

SER

VAL

LYS

PHE

4

GLY

VAL

LEU

PHE

ARG

ASP

LYS

SER

ALA

5

ASN

LEU

PHE

GLU

ALA

LEU

VAL

GLY

THR

LEU

6

LYS

ALA

LYS

ARG

LYS

ILE

VAL

THR

7

TYR

PRO

GLY

GLU

LEU

GLN

GLY

VAL

8

HIS

ASP

VAL

ASP

ILE

LEU

GLN

9

ASP

LEU

GLU

HIS

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:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	15N-labeled	isotropic	sample_conditions_1
2D 1H-13C HSQC	13C_15N-labeled	isotropic	sample_conditions_1
3D CBCA(CO)NH	13C_15N-labeled	isotropic	sample_conditions_1
3D HNCACB	13C_15N-labeled	isotropic	sample_conditions_1
3D HCCH-TOCSY	13C_15N-labeled	isotropic	sample_conditions_1
3D 1H-15N NOESY	15N-labeled	isotropic	sample_conditions_1
3D 1H-15N TOCSY	15N-labeled	isotropic	sample_conditions_1
3D 1H-13C NOESY	13C_15N-labeled	isotropic	sample_conditions_1
3D HN(CO)CA	13C_15N-labeled	isotropic	sample_conditions_1
3D HNCA	13C_15N-labeled	isotropic	sample_conditions_1
3D H(CCO)NH	13C_15N-labeled	isotropic	sample_conditions_1
3D HNCO	13C_15N-labeled	isotropic	sample_conditions_1
3D CCH-TOCSY	13C_15N-labeled	isotropic	sample_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

PDB	2L2O
GB	AAF28958 AAF71102 AAH14953 AIC62228 EAW47902
REF	NP_067066 XP_001159255 XP_002817467 XP_003121220 XP_003255842
SP	Q9P1F3
AlphaFold	Q9P1F3