BMRB Entry 15674

Name: Solution NMR structure of the chromobox protein homolog 7
Published: 2008-03-05

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PDB ID: 2k1b
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15674
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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution NMR structure of the chromobox protein homolog 7

Deposition date:

2008-02-25

Original release date:

2008-03-05

Authors:

Kaustov, Lilia; Lemak, Alexander; Quyang, Hui; Gutmanas, Alexandras; Fares, Christophe; Bountra, Chas; Weigelt, Johan; Ravichandran, Mani; Loppnau, Peter; Edwards, Aled; Min, Jinrong; Arrowsmith, Cheryl

Citation:

Citation: Kaustov, Lilia; Lemak, Alexander; Quyang, Hui; Gutmanas, Alexandras; Fares, Christophe; Bountra, Chas; Weigelt, Johan; Ravichandran, Mani; Loppnau, Peter; Edwards, Aled; Min, Jinrong; Arrowsmith, Cheryl. "Solution NMR structure of the chromobox protein homolog 7" .

Assembly members:

Assembly members:
cbx7, polymer, 73 residues, Formula weight is not available

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: pET28a-mhl

Entity Sequences (FASTA):

Entity Sequences (FASTA):
cbx7: MHHHHHHSSGRENLYFQGEQ VFAVESIRKKRVRKGKVEYL VKWKGWPPKYSTWEPEEHIL DPRLVMAYEEKEE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
spectral_peak_list

Data type	Count
13C chemical shifts	248
15N chemical shifts	51
1H chemical shifts	410

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	chromodomain	1

Entities:

Entity 1, chromodomain 73 residues - Formula weight is not available

1

MET

HIS

SER

GLY

2

ARG

GLU

ASN

LEU

TYR

PHE

GLN

GLY

GLU

GLN

3

VAL

PHE

ALA

VAL

GLU

SER

ILE

ARG

LYS

4

ARG

VAL

ARG

LYS

GLY

LYS

VAL

GLU

TYR

LEU

5

VAL

LYS

TRP

LYS

GLY

TRP

PRO

LYS

TYR

6

SER

THR

TRP

GLU

PRO

GLU

HIS

ILE

LEU

7

ASP

PRO

ARG

LEU

VAL

MET

ALA

TYR

GLU

8

LYS

GLU

Samples:

sample_1: phosphate 10 mM; sodium chloride 300 mM; DTT 2 mM; D2O 10%; H2O 90%

sample_conditions_1: ionic strength: 300 mM; pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D (H)CCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D aromat 1H-13C NOESY	sample_1	isotropic	sample_conditions_1

Software:

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

NMR spectrometers:

Bruker Avance 800 MHz
Bruker Avance 500 MHz

BMRB	16778 17072 17079
PDB	2K1B 2KVM 2L12 2L1B 4MN3 4X3K 4X3S 4X3T 4X3U
DBJ	BAI46775
GB	AAH51773 AAX94038 AAY68391 ABZ92314 AIC56058
REF	NP_001179547 NP_001247702 NP_783640 XP_002743799 XP_003126060
SP	O95931
TPG	DAA29144
AlphaFold	O95931