BMRB Entry 11142

Name: Solution structure of the CH domain from human Smoothelin splice isoform L2
Published: 2011-04-01

Click here to enlarge.

PDB ID: 2d87
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11142
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 CH domain from human Smoothelin splice isoform L2

Deposition date:

2010-03-31

Original release date:

2011-04-01

Authors:

Tomizawa, T.; Kigawa, T.; Koshiba, S.; Inoue, M.; Yokoyama, S.

Citation:

Citation: Tomizawa, T.; Kigawa, T.; Koshiba, S.; Inoue, M.; Yokoyama, S.. "Solution structure of the CH domain from human Smoothelin splice isoform L2" .

Assembly members:

Assembly members:
CH domain, polymer, 128 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: P050425-09

Entity Sequences (FASTA):

Entity Sequences (FASTA):
CH domain: GSSGSSGIKQMLLDWCRAKT RGYEHVDIQNFSSSWSDGMA FCALVHNFFPEAFDYGQLSP QNRRQNFEVAFSSAETHADC PQLLDTEDMVRLREPDWKCV YTYIQEFYRCLVQKGLVKTK KSSGPSSG

Data sets:

assigned_chemical_shifts
- chemical_shift_1

Data type	Count
13C chemical shifts	531
15N chemical shifts	123
1H chemical shifts	811

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	CH domain	1

Entities:

Entity 1, CH domain 128 residues - Formula weight is not available

1

GLY

SER

GLY

SER

GLY

ILE

LYS

GLN

2

MET

LEU

ASP

TRP

CYS

ARG

ALA

LYS

THR

3

ARG

GLY

TYR

GLU

HIS

VAL

ASP

ILE

GLN

ASN

4

PHE

SER

TRP

SER

ASP

GLY

MET

ALA

5

PHE

CYS

ALA

LEU

VAL

HIS

ASN

PHE

PRO

6

GLU

ALA

PHE

ASP

TYR

GLY

GLN

LEU

SER

PRO

7

GLN

ASN

ARG

GLN

ASN

PHE

GLU

VAL

ALA

8

PHE

SER

ALA

GLU

THR

HIS

ALA

ASP

CYS

9

PRO

GLN

LEU

ASP

THR

GLU

ASP

MET

VAL

10

ARG

LEU

ARG

GLU

PRO

ASP

TRP

LYS

CYS

VAL

11

TYR

THR

TYR

ILE

GLN

GLU

PHE

TYR

ARG

CYS

12

LEU

VAL

GLN

LYS

GLY

LEU

VAL

LYS

THR

LYS

13

LYS

SER

GLY

PRO

SER

GLY

Samples:

sample_1: CH domain, [U-13C; U-15N], 0.68 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: 296 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:

xwinnmr v3.5, Bruker - collection

NMRPipe v20030801, Delaglio, F. - processing

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

Kujira v0.932, Kobayashi, N. - data analysis

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

NMR spectrometers:

Bruker AVANCE 800 MHz