BMRB Entry 15740

Name: Structure ensemble Backbone and side-chain 1H, 13C, and 15N Chemical Shift Assignments, 1H-15N RDCs and 1H-1H nOe restraints for protein K7 from the Vaccinia virus
Published: 2008-11-11

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PDB ID: 2k36
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15740
MolProbity Validation Chart

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

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Title: Structure ensemble Backbone and side-chain 1H, 13C, and 15N Chemical Shift Assignments, 1H-15N RDCs and 1H-1H nOe restraints for protein K7 from the Vaccinia virus PubMed: 18845156

Deposition date: 2008-04-22 Original release date: 2008-11-11

Authors: Kalverda, Arnout; Thompson, Gary; Vogel, Andre; Schr der, Martina; Bowie, Andrew; Khan, Amir; Homans, Steve

Citation: Kalverda, Arnout; Thompson, Gary; Vogel, Andre; Schroeder, Martina; Bowie, Andrew; Khan, Amir; Homans, Steve. "Poxvirus K7 protein adopts a Bcl-2 fold: Biochemical mapping of its interactions with human DEAD box RNA helicase DDX3" J. Mol. Biol. 385, 843-853 (2009).

Assembly members:
K7, polymer, 145 residues, 17489.023 Da.

Natural source: Common Name: Vaccinia Virus Taxonomy ID: 10245 Superkingdom: Viruses Kingdom: not available Genus/species: Vaccinia Virus

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

Entity Sequences (FASTA):
K7: GAMEDAVFYFVDDDKICSRD SIIDLIDEYITWRNHVIVFN KDITSCGRLYKELMKFDDVA IRYYGIDKINEIVEAMSEGD HYINFTKVHDQESLFATIGI CAKITEHWGYKKISESRFQS LGNITDLMTDDNINILILFL EKKLN

Data sets:

assigned_chemical_shifts
- K7D8_SHIFT_LIST_1
RDCs
- RDC_list_1

Data type	Count
13C chemical shifts	612
15N chemical shifts	145
1H chemical shifts	941
residual dipolar couplings	70

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	K7	1

Entities:

Entity 1, K7 145 residues - 17489.023 Da.

The sequence matches the natural polymer from residue 4 onwards which is equivalent to residue 8 in the natural sequence The GAM n-terminal tag is an expression artifact

1

GLY

ALA

MET

GLU

ASP

ALA

VAL

PHE

TYR

PHE

2

VAL

ASP

LYS

ILE

CYS

SER

ARG

ASP

3

SER

ILE

ASP

LEU

ILE

ASP

GLU

TYR

ILE

4

THR

TRP

ARG

ASN

HIS

VAL

ILE

VAL

PHE

ASN

5

LYS

ASP

ILE

THR

SER

CYS

GLY

ARG

LEU

TYR

6

LYS

GLU

LEU

MET

LYS

PHE

ASP

VAL

ALA

7

ILE

ARG

TYR

GLY

ILE

ASP

LYS

ILE

ASN

8

GLU

ILE

VAL

GLU

ALA

MET

SER

GLU

GLY

ASP

9

HIS

TYR

ILE

ASN

PHE

THR

LYS

VAL

HIS

ASP

10

GLN

GLU

SER

LEU

PHE

ALA

THR

ILE

GLY

ILE

11

CYS

ALA

LYS

ILE

THR

GLU

HIS

TRP

GLY

TYR

12

LYS

ILE

SER

GLU

SER

ARG

PHE

GLN

SER

13

LEU

GLY

ASN

ILE

THR

ASP

LEU

MET

THR

ASP

14

ASP

ASN

ILE

ASN

ILE

LEU

ILE

LEU

PHE

LEU

15

GLU

LYS

LEU

ASN

Samples:

K7D8_UCN: K7D8, [U-13C; U-15N], 0.8 mM; sodium phosphate 10 mM; sodium chloride 100 mM; DTT 10 mM; DSS 0.1 mM; D2O 10%; H2O 90%

K7D8_UN: K7D8, [U-15N], 0.8 mM; sodium phosphate 10 mM; sodium chloride 100 mM; DTT 10 mM; DSS 0.1 mM; D2O 10%; H2O 90%

K7D8_UN_PF1: K7D8, [U-15N], 0.8 mM; sodium phosphate 10 mM; sodium chloride 100 mM; DTT 10 mM; DSS 0.1 mM; Pf1 phage 12 mg/ml; D2O 10%; H2O 90%

K7R_CONDITIONS_1: ionic strength: 122.5 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	K7D8_UN	isotropic	K7R_CONDITIONS_1
2D 1H-13C HSQC	K7D8_UCN	isotropic	K7R_CONDITIONS_1
3D HNCA	K7D8_UCN	isotropic	K7R_CONDITIONS_1
3D HN(CO)CA	K7D8_UCN	isotropic	K7R_CONDITIONS_1
3D CBCA(CO)NH	K7D8_UCN	isotropic	K7R_CONDITIONS_1
3D HNCO	K7D8_UCN	isotropic	K7R_CONDITIONS_1
3D HNHA	K7D8_UCN	isotropic	K7R_CONDITIONS_1
3D 1H-15N NOESY	K7D8_UN	isotropic	K7R_CONDITIONS_1
3D CBCA(CO)NH	K7D8_UCN	isotropic	K7R_CONDITIONS_1
2D 1H-13C constant time aromatic selected HSQC	K7D8_UCN	isotropic	K7R_CONDITIONS_1
3D H(C)CH-TOCSY	K7D8_UCN	isotropic	K7R_CONDITIONS_1
3D (H)CCH-TOCSY	K7D8_UCN	isotropic	K7R_CONDITIONS_1
2D HB(CBCGCD)HD	K7D8_UCN	isotropic	K7R_CONDITIONS_1
2D HB(CBCGCDCE)HE	K7D8_UCN	isotropic	K7R_CONDITIONS_1
3D 1H-13C NOESY	K7D8_UCN	isotropic	K7R_CONDITIONS_1
2D j modulated 1H-15N HSQC	K7D8_UN	isotropic	K7R_CONDITIONS_1
2D 1H-(13C)-1H aromatic optimised 13C filtered (HSQC) NOESY	K7D8_UCN	isotropic	K7R_CONDITIONS_1

Software:

VNMR v6.1c, Varian - nmr data collection

NMRPipe v2.5 Rev 2006.184.15.37, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - determination of RDC Da & Dr parameters, processing

ccpn_analysis v1.0.9-1.0.15, CCPN - chemical shift assignment, peak picking

X-PLOR NIH v2.17, Schwieters, Kuszewski, Tjandra and Clore - structure solution

ARIA v2.17, Linge, O, nilges@pasteur.fr - refinement

NMRView v5.22, Johnson, One Moon Scientific - rdc data analysis

NMR spectrometers:

Varian INOVA 750 MHz
Varian INOVA 600 MHz
Varian INOVA 500 MHz

PDB	2K36 3JRV
DBJ	BAA00293
EMBL	CAA48965 CAA64114 CAB54624 CAM58208 CRL86498
GB	AAA48013 AAA60772 AAB96484 AAF33890 AAO89318
PRF	2015436AB
REF	NP_042068 YP_232921
SP	P68466 P68467 Q76ZX2

Biological Magnetic Resonance Data Bank