BMRB Entry 15925

Name: Filamin A Ig-like domains 18-19
Published: 2009-01-15

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PDB ID: 2k7q
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15925
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Filamin A Ig-like domains 18-19

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:
FLNa18-19, polymer, 191 residues, 20379.8945 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):
FLNa18-19: GAMGDDSMRMSHLKVGSAAD IPINISETDLSLLTATVVPP SGREEPCLLKRLRNGHVGIS FVPKETGEHLVHVKKNGQHV ASSPIPVVISQSEIGDASRV RVSGQGLHEGHTFEPAEFII DTRDAGYGGLSLSIEGPSKV DINTEDLEDGTCRVTYCPTE PGNYIINIKFADQHVPGSPF SVKVTGEGRVK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	761
15N chemical shifts	175
1H chemical shifts	1298

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	FLNa18-19	1

Entities:

Entity 1, FLNa18-19 191 residues - 20379.8945 Da.

1

GLY

ALA

MET

GLY

ASP

SER

MET

ARG

MET

2

SER

HIS

LEU

LYS

VAL

GLY

SER

ALA

ASP

3

ILE

PRO

ILE

ASN

ILE

SER

GLU

THR

ASP

LEU

4

SER

LEU

THR

ALA

THR

VAL

PRO

5

SER

GLY

ARG

GLU

PRO

CYS

LEU

LYS

6

ARG

LEU

ARG

ASN

GLY

HIS

VAL

GLY

ILE

SER

7

PHE

VAL

PRO

LYS

GLU

THR

GLY

GLU

HIS

LEU

8

VAL

HIS

VAL

LYS

ASN

GLY

GLN

HIS

VAL

9

ALA

SER

PRO

ILE

PRO

VAL

ILE

SER

10

GLN

SER

GLU

ILE

GLY

ASP

ALA

SER

ARG

VAL

11

ARG

VAL

SER

GLY

GLN

GLY

LEU

HIS

GLU

GLY

12

HIS

THR

PHE

GLU

PRO

ALA

GLU

PHE

ILE

13

ASP

THR

ARG

ASP

ALA

GLY

TYR

GLY

LEU

14

SER

LEU

SER

ILE

GLU

GLY

PRO

SER

LYS

VAL

15

ASP

ILE

ASN

THR

GLU

ASP

LEU

GLU

ASP

GLY

16

THR

CYS

ARG

VAL

THR

TYR

CYS

PRO

THR

GLU

17

PRO

GLY

ASN

TYR

ILE

ASN

ILE

LYS

PHE

18

ALA

ASP

GLN

HIS

VAL

PRO

GLY

SER

PRO

PHE

19

SER

VAL

LYS

VAL

THR

GLY

GLU

GLY

ARG

VAL

20

LYS

Samples:

sample_1: FLNa18-19, [U-13C; U-15N], 0.8 mM; sodium phosphate 50 mM; potassium chloride 100 mM; DTT 1 mM; sodium azide 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
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
HN(CA)CO	sample_1	isotropic	sample_conditions_1
HNCAHA	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
Bruker DRX 750 MHz