BMRB Entry 11208

Name: Solution structure of the second fn3 domain of Eph receptor A8 protein
Published: 2011-07-21

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PDB ID: 1x5l
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11208
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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution structure of the second fn3 domain of Eph receptor A8 protein

Deposition date:

2010-07-22

Original release date:

2011-07-21

Authors:

Qin, X.; Nagashima, T.; Hayashi, F.; Yokoyama, S.

Citation:

Citation: Qin, X.; Nagashima, T.; Hayashi, F.; Yokoyama, S.. "Solution structure of the second fn3 domain of Eph receptor A8 protein" .

Assembly members:

Assembly members:
fn3 domain, polymer, 111 residues, Formula weight is not available

Natural source:

Natural source: Common Name: human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: cell free synthesis Host organism: E. coli - cell free Vector: p040705-14

Entity Sequences (FASTA):

Entity Sequences (FASTA):
fn3 domain: GSSGSSGQAAPSQVVVIRQE RAGQTSVSLLWQEPEQPNGI ILEYEIKYYEKDKEMQSYST LKAVTTRATVSGLKPGTRYV FQVRARTSAGCGRFSQAMEV ETGKPSGPSSG

Data sets:

assigned_chemical_shifts
- chemical_shift_1

Data type	Count
13C chemical shifts	454
15N chemical shifts	108
1H chemical shifts	724

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	fn3 domain of Eph receptor A8 protein	1

Entities:

Entity 1, fn3 domain of Eph receptor A8 protein 111 residues - Formula weight is not available

1

GLY

SER

GLY

SER

GLY

GLN

ALA

2

PRO

SER

GLN

VAL

ILE

ARG

GLN

GLU

3

ARG

ALA

GLY

GLN

THR

SER

VAL

SER

LEU

4

TRP

GLN

GLU

PRO

GLU

GLN

PRO

ASN

GLY

ILE

5

ILE

LEU

GLU

TYR

GLU

ILE

LYS

TYR

GLU

6

LYS

ASP

LYS

GLU

MET

GLN

SER

TYR

SER

THR

7

LEU

LYS

ALA

VAL

THR

ARG

ALA

THR

VAL

8

SER

GLY

LEU

LYS

PRO

GLY

THR

ARG

TYR

VAL

9

PHE

GLN

VAL

ARG

ALA

ARG

THR

SER

ALA

GLY

10

CYS

GLY

ARG

PHE

SER

GLN

ALA

MET

GLU

VAL

11

GLU

THR

GLY

LYS

PRO

SER

GLY

PRO

SER

12

GLY

Samples:

sample_1: fn3 domain, [U-13C; U-15N], 1.42 mM; d-Tris-HCl 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; H2O 90%; D2O 10%

condition_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 15N-separated NOESY	sample_1	isotropic	condition_1
3D 13C-separated NOESY	sample_1	isotropic	condition_1

Software:

VNMR v6.1C, Varian - collection

NMRPipe v20031121, Delaglio, F. - processing

NMRView v5.0.4, Johnson, B.A. - data analysis

Kujira v0.9296, Kobayashi, N. - data analysis

CYANA v2.0.17, Guntert, P. - refinement, structure solution

NMR spectrometers:

Varian INOVA 800 MHz
Varian INOVA 900 MHz

PDB	1X5L
DBJ	BAA95983 BAD90254 BAI45300
GB	AAB39218 AAI41437 AAI67187 EAW95013 EDL29925
REF	NP_031965 NP_065387 XP_001101560 XP_001501554 XP_002685829
SP	O09127 P29322
TPG	DAA32242
AlphaFold	P29322 O09127