BMRB Entry 16486

Name: Solution NMR structure of the ACT domain from GTP pyrophosphokinase of Chlorobium tepidum. Northeast Structural Genomics Consortium Target CtR148A
Published: 2009-09-29

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PDB ID: 2ko1
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16486
MolProbity Validation Chart

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

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Title:

Solution NMR structure of the ACT domain from GTP pyrophosphokinase of Chlorobium tepidum. Northeast Structural Genomics Consortium Target CtR148A

Deposition date:

2009-09-08

Original release date:

2009-09-29

Authors:

Eletsky, Alexander; Garcia, Erwin; Wang, Huang; Ciccosanti, Colleen; Jiang, Mei; Nair, Rajesh; Rost, Burkhard; Acton, Thomas; Xiao, Rong; Everett, John; Lee, Hsiau-Wei; Prestegard, James; Montelione, Gaetano; Szyperski, Thomas

Citation:

Citation: Eletsky, Alexander; Garcia, Erwin; Wang, Huang; Ciccosanti, Colleen; Jiang, Mei; Nair, Rajesh; Rost, Burkhard; Acton, Thomas; Xiao, Rong; Everett, John; Lee, Hsiau-Wei; Prestegard, James; Montelione, Gaetano; Szyperski, Thomas. "Solution NMR structure of the ACT domain from GTP pyrophosphokinase of Chlorobium tepidum." Proteins: Struct. Funct. Genet. ., .-..

Assembly members:

Assembly members:
CtR148A, polymer, 88 residues, 10050.751 Da.

Natural source:

Natural source: Common Name: Chlorobium tepidum Taxonomy ID: 194439 Superkingdom: Bacteria Kingdom: not available Genus/species: Chlorobium tepidum

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET 21-23C

Entity Sequences (FASTA):

Entity Sequences (FASTA):
CtR148A: MTDFLAGIRIVGEDKNGMTN QITGVISKFDTNIRTIVLNA KDGIFTCNLMIFVKNTDKLT TLMDKLRKVQGVFTVERLSN LEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
spectral_peak_list
- n
- cali
- caro
- cali2

Data type	Count
13C chemical shifts	368
15N chemical shifts	94
1H chemical shifts	630

Time Domain Data

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1
2	entity_2	1

Entities:

Entity 1, entity_1 88 residues - 10050.751 Da.

Residues 2-80 correspond to the 653-731 fragment of the native protein. Residues 81-88 represent a non-native affinity tag. Residue M1 is a result of a new start codon.

1

MET

THR

ASP

PHE

LEU

ALA

GLY

ILE

ARG

ILE

2

VAL

GLY

GLU

ASP

LYS

ASN

GLY

MET

THR

ASN

3

GLN

ILE

THR

GLY

VAL

ILE

SER

LYS

PHE

ASP

4

THR

ASN

ILE

ARG

THR

ILE

VAL

LEU

ASN

ALA

5

LYS

ASP

GLY

ILE

PHE

THR

CYS

ASN

LEU

MET

6

ILE

PHE

VAL

LYS

ASN

THR

ASP

LYS

LEU

THR

7

THR

LEU

MET

ASP

LYS

LEU

ARG

LYS

VAL

GLN

8

GLY

VAL

PHE

THR

VAL

GLU

ARG

LEU

SER

ASN

9

LEU

GLU

HIS

Samples:

NC5_PEG: CtR148A, [U-5% 13C; U-100% 15N], 0.3 mM; MES 18 mM; sodium chloride 180 mM; calcium chloride 4.5 mM; DTT 9 mM; DSS 45 uM; sodium azide 0.045%; polyethylene glycol 4%; D2O 16%; H2O 84%

NC5_PAAG: CtR148A, [U-5% 13C; U-100% 15N], 0.45 mM; MES 18 mM; sodium chloride 180 mM; calcium chloride 4.5 mM; DTT 9 mM; DSS 45 uM; sodium azide 0.045%; polyacrylamide 7%; D2O 14%; H2O 86%

NC: CtR148A, [U-100% 13C; U-100% 15N], 0.3 mM; MES 20 mM; sodium chloride 200 mM; calcium chloride 5 mM; DTT 10 mM; DSS 50 uM; sodium azide 0.05%; D2O 10%; H2O 90%

NC5: CtR148A, [U-5% 13C; U-100% 15N], 0.5 mM; MES 20 mM; sodium chloride 200 mM; calcium chloride 5 mM; DTT 10 mM; DSS 50 uM; sodium azide 0.05%; D2O 10%; H2O 90%

MIX: CtR148A, [U-100% 13C; U-100% 15N], 0.5 mM; MES 20 mM; sodium chloride 200 mM; calcium chloride 5 mM; DTT 10 mM; DSS 50 uM; sodium azide 0.05%; CtR148A 0.5 mM; D2O 10%; H2O 90%

sample_conditions_1: ionic strength: 225 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
1D 15N T1	NC	isotropic	sample_conditions_1
1D 15N T2	NC	isotropic	sample_conditions_1
2D 1H-15N HSQC	NC	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	NC	isotropic	sample_conditions_1
2D 1H-13C CT-HSQC aliphatic	NC	isotropic	sample_conditions_1
2D 1H-13C CT-HSQC aromatic	NC	isotropic	sample_conditions_1
3D CBCA(CO)NH	NC	isotropic	sample_conditions_1
3D HNCACB	NC	isotropic	sample_conditions_1
3D HNCO	NC	isotropic	sample_conditions_1
3D HN(CA)CO	NC	isotropic	sample_conditions_1
3D HBHA(CO)NH	NC	isotropic	sample_conditions_1
3D HCCH-COSY	NC	isotropic	sample_conditions_1
3D HCCH-TOCSY	NC	isotropic	sample_conditions_1
3D 1H-13C NOESY	NC	isotropic	sample_conditions_1
3D 1H-15N/13C NOESY	NC	isotropic	sample_conditions_1
2D 1H-13C CT-HSQC methyl	NC5	isotropic	sample_conditions_1
2D 1H-15N HSQC J-modulated	NC5	isotropic	sample_conditions_1
2D 1H-15N HSQC J-modulated	NC5_PEG	anisotropic	sample_conditions_1
2D 1H-15N HSQC J-modulated	NC5_PAAG	anisotropic	sample_conditions_1
3D 1H-13C X-filtered NOESY	MIX	isotropic	sample_conditions_1

Software:

VNMRJ v2.1B, Varian - collection

PROSA v6.4, Guntert - processing

CARA v1.8.4, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking

PINE v1.0, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

TALOS+ v1.2009.0721.18, Yang,Cornilescu, Delaglio and Bax - data analysis

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution

CNS v1.2.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - structure validation

PSVS v1.3, Bhattacharya and Montelione - structure validation

NMR spectrometers:

Varian INOVA 750 MHz
Varian INOVA 600 MHz
Varian INOVA 600 MHz

PDB	2KO1
GB	AAM72771
REF	NP_662429 WP_010933210