BMRB Entry 11561

Name: Redox protein (oxidized form)
Published: 2015-05-18

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PDB ID: 2rue
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11561
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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: Redox protein (oxidized form)

Deposition date: 2014-03-27 Original release date: 2015-05-18

Authors: Inagaki, Koya; Satoh, Tadashi; Kato, Koichi

Citation: Inagaki, Koya; Satoh, Tadashi; Kato, Koichi. "1H , 13C and 15N Assigned Chemical Shifts for PDI" Not known ., .-..

Assembly members:
PDI, polymer, 121 residues, 13124.035 Da.

Natural source: Common Name: Soft-rot fungus Taxonomy ID: 34413 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Humicola isolens

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

Entity Sequences (FASTA):
PDI: GPLGSEGPVTVVVAKNYNEI VLDDTKDVLIEFYAPWCGHC KALAPKYEELGALYAKSEFK DRVVIAKVDATANDVPDEIQ GFPTIKLYPAGAKGQPVTYS GSRTVEDLIKFIAENGKYKA A

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	449
15N chemical shifts	110
1H chemical shifts	714

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity	1

Entities:

Entity 1, entity 121 residues - 13124.035 Da.

Residues 1-5 represent a non-native affinity tag

1

GLY

PRO

LEU

GLY

SER

GLU

GLY

PRO

VAL

THR

2

VAL

ALA

LYS

ASN

TYR

ASN

GLU

ILE

3

VAL

LEU

ASP

THR

LYS

ASP

VAL

LEU

ILE

4

GLU

PHE

TYR

ALA

PRO

TRP

CYS

GLY

HIS

CYS

5

LYS

ALA

LEU

ALA

PRO

LYS

TYR

GLU

LEU

6

GLY

ALA

LEU

TYR

ALA

LYS

SER

GLU

PHE

LYS

7

ASP

ARG

VAL

ILE

ALA

LYS

VAL

ASP

ALA

8

THR

ALA

ASN

ASP

VAL

PRO

ASP

GLU

ILE

GLN

9

GLY

PHE

PRO

THR

ILE

LYS

LEU

TYR

PRO

ALA

10

GLY

ALA

LYS

GLY

GLN

PRO

VAL

THR

TYR

SER

11

GLY

SER

ARG

THR

VAL

GLU

ASP

LEU

ILE

LYS

12

PHE

ILE

ALA

GLU

ASN

GLY

LYS

TYR

LYS

ALA

13

ALA

Samples:

sample_1: PDI, [U-15N], 0.1 mM; sodium phosphate 10 mM; potassium chloride 100 mM; H2O 90%; D2O 10%

sample_2: PDI, [U-13C; U-15N], 0.1 mM; sodium phosphate 10 mM; potassium chloride 100 mM; D2O 100%

sample_conditions_1: ionic strength: 0.16 M; pH: 6.0; pressure: 1 atm; temperature: 303 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_2	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_2	isotropic	sample_conditions_1

Software:

CNS v1.3, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - refinement

SPARKY v3.1, Goddard - chemical shift assignment

xwinnmr v2.6, Bruker Biospin - processing

NMR spectrometers:

Bruker Avance 800 MHz
JEOL ECA 920 MHz

UNP	P55059
BMRB	11562
PDB	2DJJ 2KP1 2RUE 2RUF 3WT1 3WT2 5CRW

Biological Magnetic Resonance Data Bank