BMRB Entry 11065

Name: Solution structure of the 4.1R FERM alpha lobe domain
Published: 2009-04-23

Click here to enlarge.

PDB ID: 2rq1
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/BMR11065
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

Solution structure of the 4.1R FERM alpha lobe domain

Deposition date:

2009-01-09

Original release date:

2009-04-23

Authors:

Kusunoki, Hideki; Kohno, Toshiyuki

Citation:

Citation: Kusunoki, Hideki; Kohno, Toshiyuki. "Solution structure and glycophorin C binding studies of the 4.1R FERM alpha-lobe domain" Proteins 76, 255-260 (2009).
PubMed: 19338061

Assembly members:

Assembly members:
4.1R FERM alpha-lobe domain, polymer, 109 residues, 12420.137 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: pET15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
4.1R FERM alpha-lobe domain: GSHMDPAQLTEDITRYYLCL QLRQDIVAGRLPCSFATLAL LGSYTIQSELGDYDPELHGV DYVSDFKLAPNQTKELEEKV MELHKSYRSMTPAQADLEFL ENAKKLSMY

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	489
15N chemical shifts	109
1H chemical shifts	777

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	4.1R FERM alpha-lobe domain	1

Entities:

Entity 1, 4.1R FERM alpha-lobe domain 109 residues - 12420.137 Da.

Residues 79-82 represent vector-derived amino acid residues

1

GLY

SER

HIS

MET

ASP

PRO

ALA

GLN

LEU

THR

2

GLU

ASP

ILE

THR

ARG

TYR

LEU

CYS

LEU

3

GLN

LEU

ARG

GLN

ASP

ILE

VAL

ALA

GLY

ARG

4

LEU

PRO

CYS

SER

PHE

ALA

THR

LEU

ALA

LEU

5

LEU

GLY

SER

TYR

THR

ILE

GLN

SER

GLU

LEU

6

GLY

ASP

TYR

ASP

PRO

GLU

LEU

HIS

GLY

VAL

7

ASP

TYR

VAL

SER

ASP

PHE

LYS

LEU

ALA

PRO

8

ASN

GLN

THR

LYS

GLU

LEU

GLU

LYS

VAL

9

MET

GLU

LEU

HIS

LYS

SER

TYR

ARG

SER

MET

10

THR

PRO

ALA

GLN

ALA

ASP

LEU

GLU

PHE

LEU

11

GLU

ASN

ALA

LYS

LEU

SER

MET

TYR

Samples:

sample_1: 4.1R FERM alpha-lobe domain0.12 – 0.8 mM; NaCl 45 mM; D2O 100%

sample_2: 4.1R FERM alpha-lobe domain, [U-98% 15N], 0.12 – 0.8 mM; NaCl 45 mM; H2O 90%; D2O 10%

sample_3: 4.1R FERM alpha-lobe domain, [U-98% 13C; U-98% 15N], 0.12 – 0.8 mM; NaCl 45 mM; H2O 90%; D2O 10%

sample_4: 4.1R FERM alpha-lobe domain, [U-98% 13C; U-98% 15N], 0.12 – 0.8 mM; NaCl 45 mM; D2O 100%

sample_5: 4.1R FERM alpha-lobe domain, [U-10% 13C; U-98% 15N], 0.48 mM; NaCl 45 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 45 mM; pH: 6.4; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY No1	sample_3	isotropic	sample_conditions_1
3D 1H-13C NOESY No2	sample_4	isotropic	sample_conditions_1
2D 1H-15N HSQC No1	sample_2	isotropic	sample_conditions_1
2D 1H-15N HSQC No2	sample_3	isotropic	sample_conditions_1
2D 1H-13C HSQC No1	sample_3	isotropic	sample_conditions_1
2D 1H-13C HSQC No2	sample_5	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_3	isotropic	sample_conditions_1
3D C(CO)NH	sample_3	isotropic	sample_conditions_1
3D HNCO	sample_3	isotropic	sample_conditions_1
3D HNCA	sample_3	isotropic	sample_conditions_1
3D HNCACB	sample_3	isotropic	sample_conditions_1
3D H(CCO)NH	sample_3	isotropic	sample_conditions_1
3D HCCH-TOCSY No1	sample_3	isotropic	sample_conditions_1
3D HCCH-TOCSY No2	sample_4	isotropic	sample_conditions_1
3D HNHA	sample_3	isotropic	sample_conditions_1
3D HNHB	sample_3	isotropic	sample_conditions_1
3D HN(CO)CA	sample_3	isotropic	sample_conditions_1
3D HN(CA)CO	sample_3	isotropic	sample_conditions_1

Software:

CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - NOE collection

TOPSPIN, Bruker Biospin - processing

SPARKY, Goddard - data analysis

NMR spectrometers:

Bruker Avance 500 MHz

PDB	1GG3 2RQ1 3QIJ
DBJ	BAD90280 BAD92886 BAE27807 BAE28045 BAG84710
EMBL	CDR98361 CDR98362
GB	AAA35793 AAA35794 AAA35795 AAA35797 AAA37122
REF	NP_001003362 NP_001122078 NP_001122079 NP_001159477 NP_001159478
SP	P11171 P48193 Q6Q7P4 Q9N179
TPG	DAA32059
AlphaFold	P11171 P48193 Q6Q7P4 Q9N179