BMRB Entry 30410

Name: Solution structure of the four-helix bundle region of human J-protein Zuotin, a component of ribosome-associated complex (RAC)
Published: 2019-06-07

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PDB ID: 6cgh
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30410
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:

Solution structure of the four-helix bundle region of human J-protein Zuotin, a component of ribosome-associated complex (RAC)

Deposition date:

2018-02-20

Original release date:

2019-06-07

Authors:

Shrestha, O.; Lee, W.; Tonelli, M.; Cornilescu, G.; Markley, J.; Ciesielski, S.; Craig, E.

Citation:

Citation: Shrestha, Om Kumar; Sharma, Ruchika; Tomiczek, Bartlomiej; Lee, Woonghee; Tonelli, Marco; Cornilescu, Gabriel; Stolarska, Milena; Nierzwicki, Lukasz; Czub, Jacek; Markley, John; Marszalek, Jaroslaw; Ciesielski, Szymon; Craig, Elizabeth. "Structure and Evolution of the 4-helix Bundle Domain of Zuotin, a J-domain Protein Co-Chaperone of Hsp70" PLoS ONE 14, e0217098-e0217098 (2019).
PubMed: 31091298

Assembly members:

Assembly members:
entity_1, polymer, 89 residues, 10401.884 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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSKKAIKKERQKLRNSCKTW NHFSDNEAERVKMMEEVEKL CDRLELASLQCLNETLTSCT KEVGKAALEKQIEEINEQIR KEKEEAEAR

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	268
15N chemical shifts	85
1H chemical shifts	521

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 89 residues - 10401.884 Da.

1

GLY

SER

LYS

ALA

ILE

LYS

GLU

ARG

2

GLN

LYS

LEU

ARG

ASN

SER

CYS

LYS

THR

TRP

3

ASN

HIS

PHE

SER

ASP

ASN

GLU

ALA

GLU

ARG

4

VAL

LYS

MET

GLU

VAL

GLU

LYS

LEU

5

CYS

ASP

ARG

LEU

GLU

LEU

ALA

SER

LEU

GLN

6

CYS

LEU

ASN

GLU

THR

LEU

THR

SER

CYS

THR

7

LYS

GLU

VAL

GLY

LYS

ALA

LEU

GLU

LYS

8

GLN

ILE

GLU

ILE

ASN

GLU

GLN

ILE

ARG

9

LYS

GLU

LYS

GLU

ALA

GLU

ALA

ARG

Samples:

sample_1: Mpp11 (346-432), [U-100% 13C; U-100% 15N], 300 uM; NaCl 250 mM; sodium phosphate 20 mM

sample_2: Mpp11 (346-432), [U-100% 15N], 300 uM; NaCl 250 mM; sodium phosphate 20 mM

sample_3: Mpp11 (346-432), [U-100% 13C; U-100% 15N], 200 uM; NaCl 250 mM; sodium phosphate 20 mM

sample_4: Mpp11 (346-432), [U-100% 13C; U-100% 15N], 150 uM; NaCl 250 mM; sodium phosphate 20 mM

sample_conditions_1: ionic strength: 270 mM; pH: 7.5; pressure: 1 Pa; temperature: 278 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
1H-15N IPAP HSQC	sample_1	isotropic	sample_conditions_1
1H-15N IPAP HSQC	sample_3	anisotropic	sample_conditions_1
1H-15N IPAP HSQC	sample_4	anisotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

VNMR, Varian - collection

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

APES, Shin, Lee and Lee - peak picking

NMRFAM-SPARKY, Lee, Tonelli and Markley - peak picking

PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

PINE-SPARKY, Lee, Westler, Bahrami, Eghbalnia and Markley - chemical shift assignment

PONDEROSA-C/S, Lee, Stark and Markley - refinement, structure calculation

AUDANA, Lee, Petit, Cornilescu, Stark and Markley - structure calculation

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure calculation

NMR spectrometers:

Varian VNS 600 MHz
Bruker Avance 750 MHz
Bruker Avance 600 MHz
Varian VNS 900 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks