BMRB Entry 15806

Name: 1H and 15N Chemical Shift Assignments and Experimental NMR Restraints for the Neurotrypsin Kringle Domain
Published: 2008-07-02

Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR15806

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:

1H and 15N Chemical Shift Assignments and Experimental NMR Restraints for the Neurotrypsin Kringle Domain

Deposition date:

2008-06-16

Original release date:

2008-07-02

Authors:

Ozhogina, Olga

Citation:

Citation: Ozhogina, Olga; Grishaev, Alexander; Bominaar, Emile; Llinas, Miguel. "NMR Solution Structure of the Neurotrypsin Kringle Domain" Biochemistry 47, 12290-12298 (2008).
PubMed: 18956887

Assembly members:

Assembly members:
Neurotrypsin_kringle_domain, polymer, 77 residues, 8533 Da.

Natural source:

Natural source: Common Name: Norway rat Taxonomy ID: 10116 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Rattus norvegicus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pmed23

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Neurotrypsin_kringle_domain: RCGAGEPWGNATNLGVPCLH WDEVPPFLERSPPASWAELR GQPHNFCRSPDGAGRPWCFY RNAQGKVDWGYCDCGQG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
15N chemical shifts	84
1H chemical shifts	473

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Neurotrypsin kringle domain	1

Entities:

Entity 1, Neurotrypsin kringle domain 77 residues - 8533 Da.

1

ARG

CYS

GLY

ALA

GLY

GLU

PRO

TRP

GLY

ASN

2

ALA

THR

ASN

LEU

GLY

VAL

PRO

CYS

LEU

HIS

3

TRP

ASP

GLU

VAL

PRO

PHE

LEU

GLU

ARG

4

SER

PRO

ALA

SER

TRP

ALA

GLU

LEU

ARG

5

GLY

GLN

PRO

HIS

ASN

PHE

CYS

ARG

SER

PRO

6

ASP

GLY

ALA

GLY

ARG

PRO

TRP

CYS

PHE

TYR

7

ARG

ASN

ALA

GLN

GLY

LYS

VAL

ASP

TRP

GLY

8

TYR

CYS

ASP

CYS

GLY

GLN

GLY

Name	Sample	Sample state	Sample conditions
2D [1H-15N]-HSQC	sample_1	isotropic	sample_conditions_1
2D [1H-15N]-HMBC	sample_1	isotropic	sample_conditions_1
2D [1H-13C]-HSQC	sample_1	isotropic	sample_conditions_1
2D [1H-1H]-TOCSY	sample_1	isotropic	sample_conditions_1
2D [1H-1H]-COSY	sample_1	isotropic	sample_conditions_1
2D [1H-1H]-NOESY	sample_1	isotropic	sample_conditions_1
3D [1H-15N]-NOESY	sample_1	isotropic	sample_conditions_1
3D [1H-15N]-TOCSY	sample_1	isotropic	sample_conditions_1
3D HNHA	sample_1	isotropic	sample_conditions_1
3D HNHB	sample_1	isotropic	sample_conditions_1

BMRB	15806
PDB	2K4R 2K51 2K4R 2K51
DDBJ	Q99JC8
EMBL	AJ311671 Q99JC8 CAA73646 CAC35028
GB	NP_445956 AAH31429 EDL12300 EDL82129
IUBMB	EC: 3.4.21
MEROPS	S01.237
NCBI	CAC35028 NP_445956
PFAM	PF00051
PIR	PIRSF037929
REFSEQ	NM_053504
SCOP	57441
SWS	Q99JC8
UNP	Q99JC8
DBJ	BAA23986
REF	NP_032965 NP_445956
SP	G3V801 O08762
AlphaFold	Q99JC8 G3V801 O08762

BMRB Entry 15806

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

Related Database Links: