BMRB Entry 26703

Name: RDPheH25-117
Published: 2017-03-03

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26703

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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:

RDPheH25-117

Deposition date:

2015-11-06

Original release date:

2017-03-03

Authors:

Zhang, Shengnan; Fitzpatrick, Paul

Citation:

Citation: Zhang, Shengnan; Fitzpatrick, Paul. "Identification of the Allosteric Site for Phenylalanine in Rat Phenylalanine Hydroxylase" J. Biol. Chem. 291, 7418-7425 (2016).
PubMed: 26823465

Assembly members:

Assembly members:
RDPheH25-117, polymer, 93 residues, Formula weight is not available

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: pET28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
RDPheH25-117: IEDNSNQNGAISLIFSLKEE VGALAKVLRLFEENDINLTH IESRPSRLNKDEYEFFTYLD KRSKPVLGSIIKSLRNDIGA TVHELSRDKEKNT

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	152
15N chemical shifts	70
1H chemical shifts	71

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	RDPheH25-117	1

Entities:

Entity 1, RDPheH25-117 93 residues - Formula weight is not available

1

ILE

GLU

ASP

ASN

SER

ASN

GLN

ASN

GLY

ALA

2

ILE

SER

LEU

ILE

PHE

SER

LEU

LYS

GLU

3

VAL

GLY

ALA

LEU

ALA

LYS

VAL

LEU

ARG

LEU

4

PHE

GLU

ASN

ASP

ILE

ASN

LEU

THR

HIS

5

ILE

GLU

SER

ARG

PRO

SER

ARG

LEU

ASN

LYS

6

ASP

GLU

TYR

GLU

PHE

THR

TYR

LEU

ASP

7

LYS

ARG

SER

LYS

PRO

VAL

LEU

GLY

SER

ILE

8

ILE

LYS

SER

LEU

ARG

ASN

ASP

ILE

GLY

ALA

9

THR

VAL

HIS

GLU

LEU

SER

ARG

ASP

LYS

GLU

10

LYS

ASN

THR

Samples:

sample_1: sodium phosphate 50 mM; sodium chloride 100 mM; phenylalanine 5 mM; leupeptin 1 uM; pepstain A 1 uM; H2O 95%; D2O 5%

sample_conditions_1: pH: 8; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1

Software:

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

NMRView, Johnson, One Moon Scientific - chemical shift assignment

NMR spectrometers:

Bruker Avance 700 MHz

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