BMRB Entry 16352

Name: Solution NMR structure of protein AF2094 from Archaeoglobus fulgidus. Northeast Structural Genomics Consotium (NESG) target GT2
Published: 2009-07-07

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PDB ID: 2kk4
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16352
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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution NMR structure of protein AF2094 from Archaeoglobus fulgidus. Northeast Structural Genomics Consotium (NESG) target GT2

Deposition date:

2009-06-15

Original release date:

2009-07-07

Authors:

Lemak, Alexander; Yee, Adelinda; Wu, Bin; Karra, Murthy; Ramelot, Theresa; Fares, Christophe; Semesi, Antony; Kennedy, Michael; Montelione, Gaetano; Arrowsmith, Cheryl

Citation:

Citation: Lemak, Alexander; Yee, Adelinda; Wu, Bin; Karra, Murthy; Ramelot, Theresa; Fares, Christophe; Semesi, Antony; Kennedy, Michael; Montelione, Gaetano; Arrowsmith, Cheryl. "Solution NMR structure of proterin AF2094 from Archaeoglobus fulgidus." .

Assembly members:

Assembly members:
AF2094, polymer, 95 residues, 10726.126 Da.

Natural source:

Natural source: Common Name: Archaeoglobus fulgidus Taxonomy ID: 2234 Superkingdom: Archaea Kingdom: not available Genus/species: Archaeoglobus fulgidus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: p11

Entity Sequences (FASTA):

Entity Sequences (FASTA):
AF2094: QGHMDLICMYVFKGEESFGE SIDVYGDYLIVKVGTEFLAV PKKSIKSVEDGRIVIGEFDE EEARELGRKWLEEKSKPVTL EELKSYGFGEEGEGS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
spectral_peak_list

Data type	Count
13C chemical shifts	391
15N chemical shifts	91
1H chemical shifts	640

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	AF2094	1

Entities:

Entity 1, AF2094 95 residues - 10726.126 Da.

1

GLN

GLY

HIS

MET

ASP

LEU

ILE

CYS

MET

TYR

2

VAL

PHE

LYS

GLY

GLU

SER

PHE

GLY

GLU

3

SER

ILE

ASP

VAL

TYR

GLY

ASP

TYR

LEU

ILE

4

VAL

LYS

VAL

GLY

THR

GLU

PHE

LEU

ALA

VAL

5

PRO

LYS

SER

ILE

LYS

SER

VAL

GLU

ASP

6

GLY

ARG

ILE

VAL

ILE

GLY

GLU

PHE

ASP

GLU

7

GLU

ALA

ARG

GLU

LEU

GLY

ARG

LYS

TRP

8

LEU

GLU

LYS

SER

LYS

PRO

VAL

THR

LEU

9

GLU

LEU

LYS

SER

TYR

GLY

PHE

GLY

GLU

10

GLU

GLY

GLU

GLY

SER

Samples:

sample_1: af2094 0.5 mM; TRIS 10 mM; sodium chloride 300 mM; ZnSO4 10 uM; DTT 10 mM; NaN3 0.01%; benzamidine 10 mM; D2O 10%; H2O 90%

sample_conditions_1: ionic strength: 300 mM; pH: 7; 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 NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C_aromatic NOESY	sample_1	isotropic	sample_conditions_1

Software:

SPARKY, Goddard - peak picking

FMC, Lemak, Steren, Llinas, Arrowsmith - chemical shift assignment

TALOS, Cornilescu, Delaglio and Bax - data analysis

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

PSVS, Bhattacharya and Montelione - structure validation

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

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 500 MHz
Bruker Avance 800 MHz

PDB	2KK4
GB	AAB89165 AIG99081
REF	WP_010879585
SP	O28186
AlphaFold	O28186