BMRB Entry 18901

Name: NMR structure of the C-terminal domain of the protein HCFC1 from MUS MUSCULUS
Published: 2013-02-15

Click here to enlarge.

PDB ID: 2m26
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18901
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
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: NMR structure of the C-terminal domain of the protein HCFC1 from MUS MUSCULUS

Deposition date: 2012-12-14 Original release date: 2013-02-15

Authors: Serrano, Pedro; Geralt, Michael; Dutta, Samit; Wuthrich, Kurt

Citation: Serrano, Pedro; Wuthrich, Kurt. "NMR structure of the C-terminal domain of the protein HCFC1 from MUS MUSCULUS" Not known ., .-..

Assembly members:
entity, polymer, 126 residues, 13347.151 Da.

Natural source: Common Name: Mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus

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

Entity Sequences (FASTA):
entity: GCLPGFPGAPCAIKISKSPD GAHLTWEPPSVTSGKIIEYS VYLAIQSSQASGEPKSSTPA QLAFMRVYCGPSPSCLVQSS SLSNAHIDYTTKPAIIFRIA ARNEKGYGPATQVRWLQETS KDSSGT

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	464
15N chemical shifts	111
1H chemical shifts	736

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	C-terminal domain of the protein HCFC1	1

Entities:

Entity 1, C-terminal domain of the protein HCFC1 126 residues - 13347.151 Da.

1

GLY

CYS

LEU

PRO

GLY

PHE

PRO

GLY

ALA

PRO

2

CYS

ALA

ILE

LYS

ILE

SER

LYS

SER

PRO

ASP

3

GLY

ALA

HIS

LEU

THR

TRP

GLU

PRO

SER

4

VAL

THR

SER

GLY

LYS

ILE

GLU

TYR

SER

5

VAL

TYR

LEU

ALA

ILE

GLN

SER

GLN

ALA

6

SER

GLY

GLU

PRO

LYS

SER

THR

PRO

ALA

7

GLN

LEU

ALA

PHE

MET

ARG

VAL

TYR

CYS

GLY

8

PRO

SER

PRO

SER

CYS

LEU

VAL

GLN

SER

9

SER

LEU

SER

ASN

ALA

HIS

ILE

ASP

TYR

THR

10

THR

LYS

PRO

ALA

ILE

PHE

ARG

ILE

ALA

11

ALA

ARG

ASN

GLU

LYS

GLY

TYR

GLY

PRO

ALA

12

THR

GLN

VAL

ARG

TRP

LEU

GLN

GLU

THR

SER

13

LYS

ASP

SER

GLY

THR

Samples:

sample_1: entity, [U-98% 13C; U-98% 15N], 1.2 mM; sodium chloride 50 mM; sodium phosphate 20 mM; sodium azide 5 mM

sample_conditions_1: ionic strength: 0.220 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
4D APSY HACANH	sample_1	isotropic	sample_conditions_1
5D APSY CBCACONH	sample_1	isotropic	sample_conditions_1
5D APSY HACACONH	sample_1	isotropic	sample_conditions_1

Software:

CYANA, G ntert P. - refinement

UNIO, Herrmann & Wuthrich - chemical shift assignment, structure solution

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 800 MHz

PDB	2M26 4GO6
DBJ	BAA08258
EMBL	CAA55790
GB	AAB01163 AAB27583 AAD09225 AAH53742 ABX10979
REF	NP_001132979 NP_001162266 NP_001268286 NP_005325 NP_032250
SP	P51610 P51611 Q61191
TPG	DAA13208

Biological Magnetic Resonance Data Bank