BMRB Entry 30374

Name: HSPB5 alpha-crystallin domain mutant R120G-ACD
Published: 2018-11-19

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PDB ID: 6bp9
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30374
MolProbity Validation Chart

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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: HSPB5 alpha-crystallin domain mutant R120G-ACD

Deposition date: 2017-11-22 Original release date: 2018-11-19

Authors: Rajagopal, P.; Klevit, R.

Citation: Rajagopal, P.; Klevit, R.. "HSPB5 alpha-crystallin domain mutant R120G-ACD" . ., .-..

Assembly members:
entity_1, polymer, 89 residues, 10099.370 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):
entity_1: GLSEMRLEKDRFSVNLDVKH FSPEELKVKVLGDVIEVHGK HEERQDEHGFISREFHGKYR IPADVDPLTITSSLSSDGVL TVNGPRKQV

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list

Data type	Count
13C chemical shifts	375
15N chemical shifts	98
1H chemical shifts	492

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1, 1	1
2	entity_1, 2	1

Entities:

Entity 1, entity_1, 1 89 residues - 10099.370 Da.

1

GLY

LEU

SER

GLU

MET

ARG

LEU

GLU

LYS

ASP

2

ARG

PHE

SER

VAL

ASN

LEU

ASP

VAL

LYS

HIS

3

PHE

SER

PRO

GLU

LEU

LYS

VAL

LYS

VAL

4

LEU

GLY

ASP

VAL

ILE

GLU

VAL

HIS

GLY

LYS

5

HIS

GLU

ARG

GLN

ASP

GLU

HIS

GLY

PHE

6

ILE

SER

ARG

GLU

PHE

HIS

GLY

LYS

TYR

ARG

7

ILE

PRO

ALA

ASP

VAL

ASP

PRO

LEU

THR

ILE

8

THR

SER

LEU

SER

ASP

GLY

VAL

LEU

9

THR

VAL

ASN

GLY

PRO

ARG

LYS

GLN

VAL

Samples:

sample_1: HSPB5 mutant R120G-ACD, [U-13C; U-15N], 1 mM; sodium phosphate 50 mM; sodium chloride 100 mM; EDTA 100 uM; PMSF 1 mM

sample_2: HSPB5 mutant R120G-ACD, [U-13C; U-15N; 50%-2H], 1 mM; sodium phosphate 50 mM; sodium chloride 100 mM; EDTA 100 uM; PMSF 1 mM

sample_3: HSPB5 mutant R120G-ACD, [U-13C; U-15N; U-2H], 1 mM; sodium phosphate 50 mM; sodium chloride 100 mM; EDTA 100 uM; PMSF 1 mM

sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 303 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D NOESY	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1
3D HNCA	sample_3	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_3	isotropic	sample_conditions_1
3D HN(COCA)CB	sample_3	isotropic	sample_conditions_1
3D HN(CO)CA	sample_3	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1

Software:

CSRosetta, David Baker - structure calculation

NMRView, Johnson, One Moon Scientific - chemical shift assignment, peak picking

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

NMR spectrometers:

Bruker AvanceII 600 MHz
Varian UNITYPLUS 800 MHz
Bruker AvanceIII 500 MHz
Varian UNITYPLUS 900 MHz
Varian UNITYPLUS 600 MHz

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