BMRB Entry 30958

Name: Filamin complex-2
Published: 2023-04-04

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PDB ID: 7sft
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30958
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:

Filamin complex-2

Deposition date:

2021-10-04

Original release date:

2023-04-04

Authors:

Liu, J.; Qin, J.

Citation:

Citation: Liu, J.; Qin, J.. "Filamin complex-2" .

Assembly members:

Assembly members:
entity_1, polymer, 95 residues, 9762.721 Da.
entity_2, polymer, 21 residues, 2581.789 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 phage EcSzw-2

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GGAHKVRAGGPGLERAEAGV PAEFSIWTREAGAGGLAIAV EGPSKAEISFEDRKDGSCGV AYVVQEPGDYEVSVKFNEEH IPDSPFVVPVASPSG
entity_2: WKVGFFKRNRPPLEEDDEEG E

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	167
15N chemical shifts	90
1H chemical shifts	550

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1
2	unit_2	2

Entities:

Entity 1, unit_1 95 residues - 9762.721 Da.

1

GLY

ALA

HIS

LYS

VAL

ARG

ALA

GLY

2

PRO

GLY

LEU

GLU

ARG

ALA

GLU

ALA

GLY

VAL

3

PRO

ALA

GLU

PHE

SER

ILE

TRP

THR

ARG

GLU

4

ALA

GLY

ALA

GLY

LEU

ALA

ILE

ALA

VAL

5

GLU

GLY

PRO

SER

LYS

ALA

GLU

ILE

SER

PHE

6

GLU

ASP

ARG

LYS

ASP

GLY

SER

CYS

GLY

VAL

7

ALA

TYR

VAL

GLN

GLU

PRO

GLY

ASP

TYR

8

GLU

VAL

SER

VAL

LYS

PHE

ASN

GLU

HIS

9

ILE

PRO

ASP

SER

PRO

PHE

VAL

PRO

VAL

10

ALA

SER

PRO

SER

GLY

Entity 2, unit_2 21 residues - 2581.789 Da.

1

TRP

LYS

VAL

GLY

PHE

LYS

ARG

ASN

ARG

2

PRO

LEU

GLU

ASP

GLU

GLY

3

GLU

Samples:

sample_1: filamin Ig21, [U-100% 13C; U-100% 15N], 1 mM; Integrin alpha-IIb light chain 2 mM

sample_2: filamin Ig21, [U-15N; U-2H], 1 mM; Integrin alpha-IIb light chain 2 mM

sample_3: Integrin alpha-IIb light chain 2 mM; GST-filamin-Ig21 0.05 mM

sample_conditions_1: ionic strength: 61 mM; pH: 6.4; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-1H NOESY	sample_3	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_3	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1

Software:

TopSpin, Bruker Biospin - collection

Sparky, Goddard - chemical shift assignment, peak picking

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

NMR spectrometers:

Bruker AVANCE 600 MHz
Bruker AVANCE 900 MHz

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