BMRB Entry 16466

Name: Solution structure and functional characterization of human plasminogen kringle 5
Published: 2009-12-11

Click here to enlarge.

PDB ID: 2knf
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16466
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 and functional characterization of human plasminogen kringle 5

Deposition date:

2009-08-21

Original release date:

2009-12-11

Authors:

Battistel, Marcos; Grishaev, Alexander; An, Seong Soo; Castellino, Francis; Llinas, Miguel

Citation:

Citation: Battistel, Marcos; Grishaev, Alexander; An, Seong Soo A; Castellino, Francis; Llinas, Miguel. "Solution structure and functional characterization of human plasminogen kringle 5." Biochemistry 48, 10208-10219 (2009).
PubMed: 19821587

Assembly members:

Assembly members:
rK5, polymer, 86 residues, 9569.646 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: Pichia pastoris Vector: not applicable

Entity Sequences (FASTA):

Entity Sequences (FASTA):
rK5: SNADCMFGNGKGYRGKRVTT VTGTPCQDWAAQEPHRHSIF TPETNPRAGLEKNYCRNPDG DVGGPWCYTTNPRKLYDYCD VPQCAA

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
15N chemical shifts	95
1H chemical shifts	469

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	rK5	1

Entities:

Entity 1, rK5 86 residues - 9569.646 Da.

1

SER

ASN

ALA

ASP

CYS

MET

PHE

GLY

ASN

GLY

2

LYS

GLY

TYR

ARG

GLY

LYS

ARG

VAL

THR

3

VAL

THR

GLY

THR

PRO

CYS

GLN

ASP

TRP

ALA

4

ALA

GLN

GLU

PRO

HIS

ARG

HIS

SER

ILE

PHE

5

THR

PRO

GLU

THR

ASN

PRO

ARG

ALA

GLY

LEU

6

GLU

LYS

ASN

TYR

CYS

ARG

ASN

PRO

ASP

GLY

7

ASP

VAL

GLY

PRO

TRP

CYS

TYR

THR

8

ASN

PRO

ARG

LYS

LEU

TYR

ASP

TYR

CYS

ASP

9

VAL

PRO

GLN

CYS

ALA

Samples:

sample_1: D2O 10%; H2O 90%; sodium phosphate 50 mM; AMCHA 11 mM; rK5 2.2 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 5.1; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D DQF-COSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
3D HNHA	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

Software:

ARIA, Linge, O'Donoghue and Nilges - chemical shift assignment, refinement, structure solution

NMR spectrometers:

Bruker DRX 500 MHz