BMRB Entry 15924

Name: Filamin A Ig-like domains 16-17
Published: 2009-01-15

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PDB ID: 2k7p
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15924
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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 A Ig-like domains 16-17

Deposition date:

2008-08-19

Original release date:

2009-01-15

Authors:

Heikkinen, Outi; Kilpelainen, Ilkka; Koskela, Harri; Permi, Perttu; Heikkinen, Sami; Ylanne, Jari

Citation:

Citation: Heikkinen, Outi; Permi, Perttu; Koskela, Harri; Ylanne, Jari; Kilpelainen, Ilkka. "1H, 13C and 15N resonance assignments of the human filamin A tandem immunoglobulin-like domains 16-17 and 18-19" Biomol. NMR Assignments 3, 53-56 (2009).
PubMed: 19636946

Assembly members:

Assembly members:
FLNa16-17, polymer, 188 residues, 19994.4375 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: pGEX-4T1-HTb

Entity Sequences (FASTA):

Entity Sequences (FASTA):
FLNa16-17: GAMAPERPLVGVNGLDVTSL RPFDLVIPFTIKKGEITGEV RMPSGKVAQPTITDNKDGTV TVRYAPSEAGLHEMDIRYDN MHIPGSPLQFYVDYVNCGHV TAYGPGLTHGVVNKPATFTV NTKDAGEGGLSLAIEGPSKA EISCTDNQDGTCSVSYLPVL PGDYSILVKYNEQHVPGSPF TARVTGDD

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	590
15N chemical shifts	183
1H chemical shifts	1261

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	FLNa16-17	1

Entities:

Entity 1, FLNa16-17 188 residues - 19994.4375 Da.

1

GLY

ALA

MET

ALA

PRO

GLU

ARG

PRO

LEU

VAL

2

GLY

VAL

ASN

GLY

LEU

ASP

VAL

THR

SER

LEU

3

ARG

PRO

PHE

ASP

LEU

VAL

ILE

PRO

PHE

THR

4

ILE

LYS

GLY

GLU

ILE

THR

GLY

GLU

VAL

5

ARG

MET

PRO

SER

GLY

LYS

VAL

ALA

GLN

PRO

6

THR

ILE

THR

ASP

ASN

LYS

ASP

GLY

THR

VAL

7

THR

VAL

ARG

TYR

ALA

PRO

SER

GLU

ALA

GLY

8

LEU

HIS

GLU

MET

ASP

ILE

ARG

TYR

ASP

ASN

9

MET

HIS

ILE

PRO

GLY

SER

PRO

LEU

GLN

PHE

10

TYR

VAL

ASP

TYR

VAL

ASN

CYS

GLY

HIS

VAL

11

THR

ALA

TYR

GLY

PRO

GLY

LEU

THR

HIS

GLY

12

VAL

ASN

LYS

PRO

ALA

THR

PHE

THR

VAL

13

ASN

THR

LYS

ASP

ALA

GLY

GLU

GLY

LEU

14

SER

LEU

ALA

ILE

GLU

GLY

PRO

SER

LYS

ALA

15

GLU

ILE

SER

CYS

THR

ASP

ASN

GLN

ASP

GLY

16

THR

CYS

SER

VAL

SER

TYR

LEU

PRO

VAL

LEU

17

PRO

GLY

ASP

TYR

SER

ILE

LEU

VAL

LYS

TYR

18

ASN

GLU

GLN

HIS

VAL

PRO

GLY

SER

PRO

PHE

19

THR

ALA

ARG

VAL

THR

GLY

ASP

Samples:

sample_1: FLNa16-17, [U-13C; U-15N], 1 mM; sodium phosphate 50 mM; potassium chloride 100 mM; DTT 1 mM; sodium azide 2 mM; EDTA 2 mM; H2O 93%; D2O, [U-100% 2H], 7%

sample_conditions_1: ionic strength: 100 mM; pH: 6.8; pressure: 1 atm; temperature: 303.15 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C-CT-HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-COSY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-13C-CT-HSQC_aromatics	sample_1	isotropic	sample_conditions_1
2D (HB)CB(CGCDCE)HE	sample_1	isotropic	sample_conditions_1
2D (HB)CB(CGCD)HD	sample_1	isotropic	sample_conditions_1

Software:

VNMRJ, Varian - collection, processing

SPARKY, Goddard - chemical shift assignment, data analysis, peak picking

AutoAssign, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

AMBER v8.0, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - refinement

NMR spectrometers:

Varian INOVA 600 MHz
Varian INOVA 800 MHz