BMRB Entry 15721

Name: Solution structure of protein ATU1203 from AGROBACTERIUM TUMEFACIENS. NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG) target ATT10, Ontario Center for Structural Proteomics target ATC1183
Published: 2008-04-17

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PDB ID: 2n4d
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15721
MolProbity Validation Chart

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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution structure of protein ATU1203 from AGROBACTERIUM TUMEFACIENS. NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG) target ATT10, Ontario Center for Structural Proteomics target ATC1183

Deposition date:

2008-04-08

Original release date:

2008-04-17

Authors:

Lemak, Alexander; Gutmanas, Alexandras; Yee, Adelinda; Semesi, Antony; Arrowsmith, Cheryl

Citation:

Citation: Lemak, Alexander; Gutmanas, Alexandras; Yee, Adelinda; Semesi, Antony; Arrowsmith, Cheryl. "Solution structure of protein Atu1203 from Agrobacterium tumefaciens" .

Assembly members:

Assembly members:
ATU1203, polymer, 85 residues, 6335.192 Da.

Natural source:

Natural source: Common Name: Agrobacterium Tumefaciens Taxonomy ID: 358 Superkingdom: Bacteria Kingdom: not available Genus/species: Agrobacterium Tumefaciens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: P11

Entity Sequences (FASTA):

Entity Sequences (FASTA):
ATU1203: MGSSHHHHHHSSGRENLYFQ GAGLSFHVEDMTCGHCAGVI KGAIEKTVPGAAVHADPASR TVVVGGVSDAAHIAEIITAA GYTPE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	221
15N chemical shifts	49
1H chemical shifts	369

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	ATU1203	1

Entities:

Entity 1, ATU1203 85 residues - 6335.192 Da.

1

MET

GLY

SER

HIS

2

SER

GLY

ARG

GLU

ASN

LEU

TYR

PHE

GLN

3

GLY

ALA

GLY

LEU

SER

PHE

HIS

VAL

GLU

ASP

4

MET

THR

CYS

GLY

HIS

CYS

ALA

GLY

VAL

ILE

5

LYS

GLY

ALA

ILE

GLU

LYS

THR

VAL

PRO

GLY

6

ALA

VAL

HIS

ALA

ASP

PRO

ALA

SER

ARG

7

THR

VAL

GLY

VAL

SER

ASP

ALA

8

ALA

HIS

ILE

ALA

GLU

ILE

THR

ALA

9

GLY

TYR

THR

PRO

GLU

Samples:

sample_1: ATU1203, [U-13C; U-15N], 0.5 mM; MOPS 10 mM; sodium chloride 450 mM; DTT 10 mM; benzamidine 10 mM; NaN3 0.01%; ZnSO4 10 uM

sample_conditions_1: ionic strength: 450 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D (H)CCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C_aliph NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C_arom NOESY	sample_1	isotropic	sample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY, Goddard - peak picking

TALOS, Cornilescu, Delaglio and Bax - data analysis

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

NMR spectrometers:

Varian INOVA 500 MHz
Varian INOVA 600 MHz
Bruker Avance 800 MHz