BMRB Entry 17062

Name: Solution Structure of Human Plasminogen Kringle 3
Published: 2010-08-19

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PDB ID: 2l0s
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR17062
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution Structure of Human Plasminogen Kringle 3

Deposition date:

2010-07-15

Original release date:

2010-08-19

Authors:

Christen, Martin; Frank, Pascal; Schaller, Johann; Llinas, Miguel

Citation:

Citation: Christen, Martin; Frank, Pascal; Schaller, Johann; Llinas, Miguel. "Human plasminogen kringle 3: solution structure, functional insights, phylogenetic landscape" Biochemistry 49, 7131-7150 (2010).
PubMed: 20617841

Assembly members:

Assembly members:
hPgn_rK3, polymer, 83 residues, 9505.4 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: Escherichia coli Vector: pQE-8

Entity Sequences (FASTA):

Entity Sequences (FASTA):
hPgn_rK3: TYQCLKGTGENYRGNVAVTV SGHTCQHWSAQTPHTHNRTP ENFPSKNLDENYCRNPDGKR APWCHTTNSQVRWEYCKIPS CDS

Data sets:

assigned_chemical_shifts
- Chemical_shifts_at_pH*_5.7
- Chemical_shifts_at_pH*_7.0

Data type	Count
15N chemical shifts	186
1H chemical shifts	603

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	hPgn_rK3	1

Entities:

Entity 1, hPgn_rK3 83 residues - 9505.4 Da.

Residues -3 to -1 and 81 to 82 are outside of the kringle domain proper. Sequence follows standard kringle amino acid numbering convention

1

THR

TYR

GLN

CYS

LEU

LYS

GLY

THR

GLY

GLU

2

ASN

TYR

ARG

GLY

ASN

VAL

ALA

VAL

THR

VAL

3

SER

GLY

HIS

THR

CYS

GLN

HIS

TRP

SER

ALA

4

GLN

THR

PRO

HIS

THR

HIS

ASN

ARG

THR

PRO

5

GLU

ASN

PHE

PRO

SER

LYS

ASN

LEU

ASP

GLU

6

ASN

TYR

CYS

ARG

ASN

PRO

ASP

GLY

LYS

ARG

7

ALA

PRO

TRP

CYS

HIS

THR

ASN

SER

GLN

8

VAL

ARG

TRP

GLU

TYR

CYS

LYS

ILE

PRO

SER

9

CYS

ASP

SER

Samples:

sample_1: hPgn_rK3, [U-97% 15N], 1.0 mM; H2O 90%; D2O 90%; sodium azide 0.02%

Structure_determination: ionic strength: 0 M; pH*: 5.7; pressure: 1 atm; temperature: 273 K

Titrations: ionic strength: 0 M; pH*: 7.0; pressure: 1 atm; temperature: 273 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	Structure_determination
3D 1H-15N TOCSY	sample_1	isotropic	Structure_determination
3D 1H-15N NOESY	sample_1	isotropic	Structure_determination
3D HNHA	sample_1	isotropic	Structure_determination
3D HNHB	sample_1	isotropic	Structure_determination
2D 1H-1H COSY	sample_1	isotropic	Structure_determination
2D 1H-1H TOCSY	sample_1	isotropic	Structure_determination
2D 1H-1H NOESY	sample_1	isotropic	Structure_determination
2D 1H-15N HSQC	sample_1	isotropic	Titrations

Software:

xwinnmr v2.6, Bruker Biospin - collection

FELIX v98, Accelrys Software Inc. - processing

CcpNMR v1.0, CCPN - chemical shift assignment, data analysis, peak picking

ARIA v2.2, Linge, O'Donoghue and Nilges - refinement, structure solution

NMR spectrometers:

Bruker DRX 500 MHz
Bruker DRX 600 MHz