BMRB Entry 27240

Name: NMR backbone and side chain assignments of the Kringle domain of ROR1
Published: 2017-10-31

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27240

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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:

NMR backbone and side chain assignments of the Kringle domain of ROR1

Deposition date:

2017-08-30

Original release date:

2017-10-31

Authors:

Ma, Xiaofang; Hu, Kaifeng

Citation:

Citation: Ma, Xiaofang; Zhang, Yingying; Liu, Bin; Yang, Jiahui; Hu, Kaifeng. "Backbone and side-chain chemical shift assignments of the kringle domain of human receptor tyrosine kinase-like orphan receptor 1 (ROR1)" Biomol. NMR Assign. 12, 145-148 (2018).
PubMed: 29313214

Assembly members:

Assembly members:
Kringle_domain_of_ROR1, polymer, 85 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: recombinant technology Host organism: Escherichia coli Vector: pET32a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Kringle_domain_of_ROR1: GSKCYNSTGVDYRGTVSVTK SGRQCQPWNSQYPHTHTFTA LRFPELNGGHSYCRNPGNQK EAPWCFTLDENFKSDLCDIP ACDSK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	331
15N chemical shifts	84
1H chemical shifts	512

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	ROR1 Kringle monomer	1

Entities:

Entity 1, ROR1 Kringle monomer 85 residues - Formula weight is not available

1

GLY

SER

LYS

CYS

TYR

ASN

SER

THR

GLY

VAL

2

ASP

TYR

ARG

GLY

THR

VAL

SER

VAL

THR

LYS

3

SER

GLY

ARG

GLN

CYS

GLN

PRO

TRP

ASN

SER

4

GLN

TYR

PRO

HIS

THR

HIS

THR

PHE

THR

ALA

5

LEU

ARG

PHE

PRO

GLU

LEU

ASN

GLY

HIS

6

SER

TYR

CYS

ARG

ASN

PRO

GLY

ASN

GLN

LYS

7

GLU

ALA

PRO

TRP

CYS

PHE

THR

LEU

ASP

GLU

8

ASN

PHE

LYS

SER

ASP

LEU

CYS

ASP

ILE

PRO

9

ALA

CYS

ASP

SER

LYS

Samples:

sample_1: Kringle domain of ROR1, [U-99% 13C; U-99% 15N], 0.8 mM

sample_conditions_1: ionic strength: 150 mM; pH: 8.0; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
2D 1H-13C CT-HSQC aliphatic	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D H(C)CH-TOCSY	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
3D CCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D CCH-TOCSY aromatic	sample_1	isotropic	sample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY, Goddard - data analysis

PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

NMR spectrometers:

Bruker Avance 800 MHz
Bruker Avance 600 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks