BMRB Entry 17020

Name: Solution NMR structure of CV_0373(175-257) protein from Chromobacterium violaceum, Northeast Structural Genomics Consortium Target CvR118A
Published: 2012-08-02

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PDB ID: 2kzv
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17020
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution NMR structure of CV_0373(175-257) protein from Chromobacterium violaceum, Northeast Structural Genomics Consortium Target CvR118A

Deposition date:

2010-06-25

Original release date:

2012-08-02

Authors:

Yang, Yunhuang; Ramelot, Theresa; Wang, Dongyan; Ciccosanti, Colleen; Mao, Lei; Janjua, Haleema; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Kennedy, Michael

Citation:

Citation: Ramelot, Theresa; Yang, Yunhuang; Xiao, Rong; Acton, Thomas; Everett, John; Montelione, Gaetano; Kennedy, Michael. "Solution NMR structure of BT_0084, a conjugative transposon lipoprotein from Bacteroides thetaiotamicron" Proteins ., .-. (2011).
PubMed: 22116783

Assembly members:

Assembly members:
CV_0373(175-257)_protein, polymer, 92 residues, 10580 Da.

Natural source:

Natural source: Common Name: Chromobacterium violaceum Taxonomy ID: 536 Superkingdom: Bacteria Kingdom: not available Genus/species: Chromobacterium violaceum

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
CV_0373(175-257)_protein: MPHKEKHPLQDMFTSAIEAV ARDSGWAELSAVGSYLAKND PSFDPRNWGHGRLSQMVKKL DFLTVQESRNGSKLHSEIRL RHDGLEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
spectral_peak_list

Data type	Count
13C chemical shifts	382
15N chemical shifts	100
1H chemical shifts	618

Time Domain Data

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	CV_0373(175-257) protein	1

Entities:

Entity 1, CV_0373(175-257) protein 92 residues - 10580 Da.

CV_0373(175-257) protein from Chromobacterium violaceum, preceded by non-native N-terminal Met and followed by 8 non-native C-terminal residues (LEHHHHHH)

1

MET

PRO

HIS

LYS

GLU

LYS

HIS

PRO

LEU

GLN

2

ASP

MET

PHE

THR

SER

ALA

ILE

GLU

ALA

VAL

3

ALA

ARG

ASP

SER

GLY

TRP

ALA

GLU

LEU

SER

4

ALA

VAL

GLY

SER

TYR

LEU

ALA

LYS

ASN

ASP

5

PRO

SER

PHE

ASP

PRO

ARG

ASN

TRP

GLY

HIS

6

GLY

ARG

LEU

SER

GLN

MET

VAL

LYS

LEU

7

ASP

PHE

LEU

THR

VAL

GLN

GLU

SER

ARG

ASN

8

GLY

SER

LYS

LEU

HIS

SER

GLU

ILE

ARG

LEU

9

ARG

HIS

ASP

GLY

LEU

GLU

HIS

10

HIS

Samples:

NC_sample: CV_0373(175-257) protein, [U-100% 13C; U-100% 15N], 0.9 ± 0.09 mM; ammonium acetate 20 ± 1 mM; sodium chloride 100 ± 5 mM; calcium chloride 5 ± 0.2 mM; DTT 10 ± 0.5 mM; sodium azide 0.02 ± 0.001 %

NC5_sample: CV_0373(175-257) protein, [U-5% 13C; U-100% 15N], 0.82 ± 0.08 mM; ammonium acetate 20 ± 1 mM; sodium chloride 100 ± 5 mM; calcium chloride 5 ± 0.2 mM; DTT 10 ± 0.5 mM; sodium azide 0.02 ± 0.001 %

NC_sample_in_D2O: CV_0373(175-257) protein, [U-100% 13C; U-100% 15N], 0.9 ± 0.09 mM; ammonium acetate 20 ± 1 mM; sodium chloride 100 ± 5 mM; calcium chloride 5 ± 0.2 mM; DTT 10 ± 0.5 mM; sodium azide 0.02 ± 0.001 %

sample_conditions_1: ionic strength: 0.2 M; pH: 4.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	NC_sample	isotropic	sample_conditions_1
2D 1H-13C HSQC_CT	NC5_sample	isotropic	sample_conditions_1
3D 1H-15N NOESY	NC_sample	isotropic	sample_conditions_1
3D 1H-13C NOESY	NC_sample	isotropic	sample_conditions_1
3D HNCO	NC_sample	isotropic	sample_conditions_1
3D HNCA	NC_sample	isotropic	sample_conditions_1
3D HNCACB	NC_sample	isotropic	sample_conditions_1
3D CBCA(CO)NH	NC_sample	isotropic	sample_conditions_1
3D HN(CO)CA	NC_sample	isotropic	sample_conditions_1
3D HBHA(CO)NH	NC_sample	isotropic	sample_conditions_1
3D H(CCO)NH	NC_sample	isotropic	sample_conditions_1
3D C(CO)NH	NC_sample	isotropic	sample_conditions_1
3D HCCH-TOCSY	NC_sample	isotropic	sample_conditions_1
3D HCCH-COSY	NC_sample	isotropic	sample_conditions_1
3D (H)CCH-TOCSY	NC_sample_in_D2O	isotropic	sample_conditions_1
4D CC NOESY	NC_sample_in_D2O	isotropic	sample_conditions_1
2D 1H-15N HSQC_swN150ppm	NC_sample	isotropic	sample_conditions_1

Software:

NMRPipe v2008, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

VNMR v6.1C, Varian - collection

TOPSPIN v2.1.4, Bruker Biospin - collection

AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - data analysis

X-PLOR NIH v2.20, Schwieters, Kuszewski, Tjandra and Clore - structure solution

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

SPARKY v3.113, Goddard - data analysis

PSVS v1.4, Bhattacharya and Montelione - refinement

AutoAssign v2.30, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

PDBStat v5.1, (PdbStat)-Roberto Tejero and Gaetano T. Montelione - structure solution

PINE v1.0, Bahrami, A., Assadi, A., Markley, J. L. & Eghbalnia, H. - autoassignment

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

NMR spectrometers:

Varian INOVA 600 MHz
Bruker AvanceIII 850 MHz

PDB	2KZV
GB	AAQ58051 ERE17978 KJH66165 KMN49431 KMN84167
REF	WP_021475679 WP_045052090 WP_046158018 WP_048404151