BMRB Entry 16502

Name: Backbone and side chain 1H chemical shift assignments for acidic fibrobast growth factor bound to 1,3,6-naphthalenetrisulfonate
Published: 2009-10-20

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR16502

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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:

Backbone and side chain 1H chemical shift assignments for acidic fibrobast growth factor bound to 1,3,6-naphthalenetrisulfonate

Deposition date:

2009-09-18

Original release date:

2009-10-20

Authors:

Lozano, Rosa; Jimenez, M. Angeles; Santoro, Jorge; Rico, Manuel; Gimenez-Gallego, Guillermo

Citation:

Citation: Pineda-Lucena, Antonio; Jimenez, M. Angeles; Nieto, Jose; Santoro, Jorge; Rico, Manuel; Gimenez-Gallego, Guillermo. "Solution structure of acidic fibroblast growth factor bound to 1,3, 6-naphthalenetrisulfonate: a minimal model for the anti-tumoral action of suramins and suradistas." J. Mol. Biol. 281, 899-915 (1998).
PubMed: 9719643

Assembly members:

Assembly members:
aFGF, polymer, 132 residues, Formula weight is not available
NTS, non-polymer, 365.336 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: pMG47

Entity Sequences (FASTA):

Entity Sequences (FASTA):
aFGF: KKPKLLYCSNGGHFLRILPD GTVDGTRDRSDQHIQLQLSA ESVGEVYIKSTETGQYLAMD TDGLLYGSQTPNEECLFLER LEENHYNTYISKKHAEKNWF VGLKKNGSCKRGPRTHYGQK AILFLPLPVSSD

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
1H chemical shifts	790

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	acidic fibroblast growth factor	1
2	1,3,6-naphthalenetrisulfonate	2

Entities:

Entity 1, acidic fibroblast growth factor 132 residues - Formula weight is not available

Protein construct lacks the 22 N-terminal residues.

1

LYS

PRO

LYS

LEU

TYR

CYS

SER

ASN

2

GLY

HIS

PHE

LEU

ARG

ILE

LEU

PRO

ASP

3

GLY

THR

VAL

ASP

GLY

THR

ARG

ASP

ARG

SER

4

ASP

GLN

HIS

ILE

GLN

LEU

GLN

LEU

SER

ALA

5

GLU

SER

VAL

GLY

GLU

VAL

TYR

ILE

LYS

SER

6

THR

GLU

THR

GLY

GLN

TYR

LEU

ALA

MET

ASP

7

THR

ASP

GLY

LEU

TYR

GLY

SER

GLN

THR

8

PRO

ASN

GLU

CYS

LEU

PHE

LEU

GLU

ARG

9

LEU

GLU

ASN

HIS

TYR

ASN

THR

TYR

ILE

10

SER

LYS

HIS

ALA

GLU

LYS

ASN

TRP

PHE

11

VAL

GLY

LEU

LYS

ASN

GLY

SER

CYS

LYS

12

ARG

GLY

PRO

ARG

THR

HIS

TYR

GLY

GLN

LYS

13

ALA

ILE

LEU

PHE

LEU

PRO

LEU

PRO

VAL

SER

14

SER

ASP

Entity 2, 1,3,6-naphthalenetrisulfonate - C10 H5 O9 S3 - 365.336 Da.

1

NTS

Samples:

sample_1: aFGF1 – 2 mM; sodium phosphate 10 mM; TSP0.1 – 0.2 mM; beta-mercaptoethanol 1 mM; sodium chloride 150 mM; NTS 2 mM; H2O 90%; D2O 10%

sample_2: aFGF1 – 2 mM; sodium phosphate 10 mM; TSP0.1 – 0.2 mM; beta-mercaptoethanol 1 mM; sodium chloride 150 mM; NTS 2 mM; D2O 100%

sample_conditions_1: ionic strength: 10 mM; pH: 6; pressure: 1.0 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-1H COSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-1H COSY	sample_2	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_2	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_2	isotropic	sample_conditions_1

Software:

UXNMR, Bruker Biospin - processing

NMR spectrometers:

Bruker AMX 600 MHz