BMRB Entry 30518

Name: Lim5 domain of PINCH1 protein
Published: 2018-10-26

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PDB ID: 6mif
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30518
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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: Lim5 domain of PINCH1 protein

Deposition date: 2018-09-19 Original release date: 2018-10-26

Authors: Qin, J.; Vaynberg, J.

Citation: Qin, J.; Vaynberg, J.. "Lim5 domain of PINCH1 protein" . ., .-..

Assembly members:
entity_1, polymer, 79 residues, 8994.751 Da.
entity_ZN, non-polymer, 65.409 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: GSGDVCFHCNRVIEGDVVSA LNKAWCVNCFACSTCNTKLT LKNKFVEFDMKPVCKKCYEK FPLELKKRLKKLAETLGRK

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	240
15N chemical shifts	76
1H chemical shifts	481

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1
2	entity_2, 1	2
3	entity_2, 2	2

Entities:

Entity 1, entity_1 79 residues - 8994.751 Da.

1

GLY

SER

GLY

ASP

VAL

CYS

PHE

HIS

CYS

ASN

2

ARG

VAL

ILE

GLU

GLY

ASP

VAL

SER

ALA

3

LEU

ASN

LYS

ALA

TRP

CYS

VAL

ASN

CYS

PHE

4

ALA

CYS

SER

THR

CYS

ASN

THR

LYS

LEU

THR

5

LEU

LYS

ASN

LYS

PHE

VAL

GLU

PHE

ASP

MET

6

LYS

PRO

VAL

CYS

LYS

CYS

TYR

GLU

LYS

7

PHE

PRO

LEU

GLU

LEU

LYS

ARG

LEU

LYS

8

LYS

LEU

ALA

GLU

THR

LEU

GLY

ARG

LYS

Entity 2, entity_2, 1 - Zn - 65.409 Da.

1

ZN

Samples:

sample_1: Lim5-T, [U-15N], 0.5 mM; NaCl 20 mM

sample_2: 15N 13C Lim5-T, [U-13C; U-15N], 1.0 mM; NaCl 20 mM

sample_conditions_1: ionic strength: 20 mM; pH: 6.5; pressure: 1 Pa; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D HNHA	sample_2	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
3D C(CO)NH	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_2	isotropic	sample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

PIPP, Garrett - peak picking

xwinnmr, Bruker Biospin - processing

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

TALOS, Cornilescu, Delaglio and Bax - data analysis

NMR spectrometers:

Bruker Avance 600 MHz

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