BMRB Entry 18190

Name: NMR structure of the protein BC008182, a DNAJ-like domain from Homo sapiens
Published: 2012-02-13

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PDB ID: 2lo1
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18190
MolProbity Validation Chart

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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

NMR structure of the protein BC008182, a DNAJ-like domain from Homo sapiens

Deposition date:

2012-01-09

Original release date:

2012-02-13

Authors:

Dutta, Samit; Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt; JCSG, JCSG

Citation:

Citation: Dutta, Samit; Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt; JCSG, JCSG. "NMR structure of the protein BC008182, DNAJ homolog from Homo sapiens" .

Assembly members:

Assembly members:
entity, polymer, 71 residues, 8224.376 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: pSpeedet

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: GMVKETTYYDVLGVKPNATQ EELKKAYRKLALKYHPDKNP NEGEKFKQISQAYEVLSDAK KRELYDKGGEQ

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	249
15N chemical shifts	75
1H chemical shifts	498

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	BC008182	1

Entities:

Entity 1, BC008182 71 residues - 8224.376 Da.

1

GLY

MET

VAL

LYS

GLU

THR

TYR

ASP

2

VAL

LEU

GLY

VAL

LYS

PRO

ASN

ALA

THR

GLN

3

GLU

LEU

LYS

ALA

TYR

ARG

LYS

LEU

4

ALA

LEU

LYS

TYR

HIS

PRO

ASP

LYS

ASN

PRO

5

ASN

GLU

GLY

GLU

LYS

PHE

LYS

GLN

ILE

SER

6

GLN

ALA

TYR

GLU

VAL

LEU

SER

ASP

ALA

LYS

7

LYS

ARG

GLU

LEU

TYR

ASP

LYS

GLY

GLU

8

GLN

Samples:

sample_1: entity, [U-98% 13C; U-98% 15N], 1.2 mM; sodium phosphate 20 mM; sodium azide 5 mM; sodium chloride 50 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0.080 M; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

CYANA v3.0, G ntert P. - structure solution

TOPSPIN v2.1, Bruker - collection, processing

CARA, Keller and Wuthrich - chemical shift assignment, data analysis

OPAL, Luginbuhl, Guntert, Billeter and Wuthrich - refinement

NMR spectrometers:

Bruker Avance 600 MHz

BMRB	19163
PDB	2LO1 2M6Y
DBJ	BAA02656 BAC38744 BAC82111 BAD82815 BAE26788
EMBL	CAI29674
GB	AAA98855 AAC37517 AAC78597 AAH08182 AAH57876
PIR	S34632
REF	NP_001015637 NP_001127102 NP_001158143 NP_001158144 NP_001231092
SP	P31689 P63036 P63037 Q5E954 Q5NVI9
TPG	DAA12974 DAA26671
AlphaFold	P31689 P63036 P63037 Q5E954 Q5NVI9