BMRB Entry 16569

Name: Solution NMR structure of the N-terminal domain of cg2496 protein from Corynebacterium glutamicum. Northeast Structural Genomics Consortium Target CgR26A
Published: 2010-11-24

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PDB ID: 2kpt
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16569
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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 N-terminal domain of cg2496 protein from Corynebacterium glutamicum. Northeast Structural Genomics Consortium Target CgR26A

Deposition date:

2009-10-19

Original release date:

2010-11-24

Authors:

Eletsky, Alexander; Sathyamoorthy, Bharathwaj; Sukumaran, Dinesh; Wang, Dongyan; Buchwald, Willam; Ciccosanti, Colleen; Janjua, Haleema; Nair, Rajesh; Rost, Burkhard; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Szyperski, Thomas

Citation:

Citation: Eletsky, Alexander; Sathyamoorthy, Bharathwaj; Sukumaran, Dinesh; Wang, Dongyan; Buchwald, Willam; Ciccosanti, Colleen; Janjua, Haleema; Nair, Rajesh; Rost, Burkhard; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Szyperski, Thomas. "Solution NMR structure of the N-terminal domain of cg2496 protein from Corynebacterium glutamicum" Proteins: Struct. Funct. Genet. ., .-..

Assembly members:

Assembly members:
cgr26a, polymer, 148 residues, 15831.934 Da.

Natural source:

Natural source: Common Name: Corynebacterium glutamicum Taxonomy ID: 1718 Superkingdom: Eubacteria Kingdom: not available Genus/species: Corynebacterium glutamicum

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
cgr26a: TETYVLAESPEFYQDNVTDY TGQISSSDITNIQAAIDDVK ASEQKVIFVVFLSSFDGVDP ETWTQQALQANGGGNVLIYA LAPEERQYGIQGGTQWTDAE LDAANNAAFQALSQEDWAGS ALALAESVGSSSSSSSGSSS LEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	573
15N chemical shifts	155
1H chemical shifts	909

Time Domain Data

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	cgr26a	1

Entities:

Entity 1, cgr26a 148 residues - 15831.934 Da.

Residues 181-188 represent a non-native affinity tag

1

THR

GLU

THR

TYR

VAL

LEU

ALA

GLU

SER

PRO

2

GLU

PHE

TYR

GLN

ASP

ASN

VAL

THR

ASP

TYR

3

THR

GLY

GLN

ILE

SER

ASP

ILE

THR

4

ASN

ILE

GLN

ALA

ILE

ASP

VAL

LYS

5

ALA

SER

GLU

GLN

LYS

VAL

ILE

PHE

VAL

6

PHE

LEU

SER

PHE

ASP

GLY

VAL

ASP

PRO

7

GLU

THR

TRP

THR

GLN

ALA

LEU

GLN

ALA

8

ASN

GLY

ASN

VAL

LEU

ILE

TYR

ALA

9

LEU

ALA

PRO

GLU

ARG

GLN

TYR

GLY

ILE

10

GLN

GLY

THR

GLN

TRP

THR

ASP

ALA

GLU

11

LEU

ASP

ALA

ASN

ALA

PHE

GLN

12

ALA

LEU

SER

GLN

GLU

ASP

TRP

ALA

GLY

SER

13

ALA

LEU

ALA

LEU

ALA

GLU

SER

VAL

GLY

SER

14

SER

GLY

SER

15

LEU

GLU

HIS

Samples:

sample_1: cgr26a, [U-100% 13C; U-100% 15N], 0.9 mM; MES 20 mM; sodium chloride 200 mM; calcium chloride 5 mM; DSS 50 uM; sodium azide 0.02%; H2O 90%; D2O 10%

sample_2: cgr26a, [U-100% 13C; U-100% 15N], 0.9 mM; MES 20 mM; sodium chloride 200 mM; calcium chloride 5 mM; DSS 50 uM; sodium azide 0.02%; H2O 90%; D2O 10%

sample_3: cgr26a, [U-5% 13C; U-100% 15N], 0.9 mM; MES 20 mM; sodium chloride 200 mM; calcium chloride 5 mM; DSS 50 uM; sodium azide 0.02%; H2O 90%; D2O 10%

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

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
2D 1H-13C CT-HSQC aliphatic	sample_2	isotropic	sample_conditions_1
2D 1H-13C CT-HSQC aromatic	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D (H)CCH-COSY aliphatic	sample_1	isotropic	sample_conditions_1
3D (H)CCH-COSY aromatic	sample_1	isotropic	sample_conditions_1
3D (H)CCH-TOCSY aliphatic	sample_1	isotropic	sample_conditions_1
1D 15N T1	sample_1	isotropic	sample_conditions_1
1D 15N T2	sample_1	isotropic	sample_conditions_1
3D 1H-15N/13C NOESY	sample_2	isotropic	sample_conditions_1
2D (HB)CB(CGCDCE)HE aromatic	sample_2	isotropic	sample_conditions_1
2D 1H-13C CT-HSQC methyl 28ms	sample_3	isotropic	sample_conditions_1
2D 1H-13C CT-HSQC methyl 56ms	sample_3	isotropic	sample_conditions_1

Software:

VNMRJ v2.1B, Varian - collection

TOPSPIN v2.1, Bruker Biospin - collection, processing

PROSA v6.4, Guntert - processing

XEASY v1.3.13, Bartels et al. - data analysis

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, Shen, Cornilescu, Delaglio and Bax - data analysis

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

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

PSVS v1.4, Bhattacharya and Montelione - structure validation

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

NMR spectrometers:

Varian INOVA 600 MHz
Bruker Avance 800 MHz

PDB	2KPT
DBJ	BAB99668 BAF55148
EMBL	CAF20617 CCH25415
GB	AGN19771 AGN22796 AGT06004 AIK85704 AIK88489
REF	NP_601475 WP_003857041 WP_003859550 WP_006287490 WP_011015004