BMRB Entry 17745

Name: NMR Assignment of PFV RNase H domain
Published: 2012-03-27

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PDB ID: 2lsn
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17745
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

NMR Assignment of PFV RNase H domain

Deposition date:

2011-06-29

Original release date:

2012-03-27

Authors:

Leo, Berit; Schweimer, Kristian; Woehrl, Birgitta

Citation:

Citation: Leo, Berit; Hartl, Maximilian; Schweimer, Kristian; Mayr, Florian; Wohrl, Birgitta. "Insights into the structure and activity of prototype foamy virus RNase H." Retrovirology 9, 14-14 (2012).
PubMed: 22325739

Assembly members:

Assembly members:
PFV_RNase_H, polymer, 165 residues, Formula weight is not available

Natural source:

Natural source: Common Name: prototype foamy virus Taxonomy ID: not available Superkingdom: Viruses Kingdom: not available Genus/species: foamy virus prototype foamy virus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-GB1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PFV_RNase_H: GAMGQYEGVFYTDGSAIKSP DPTKSNNAGMGIVHATYKPE YQVLNQWSIPLGNHTAQMAE IAAVEFACKKALKIPGPVLV ITDSFYVAESANKELPYWKS NGFVNNKKKPLKHISKWKSI AECLSMKPDITIQHEKGHQP TNTSIHTEGNALADKLATQG SYVVN

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	600
15N chemical shifts	142
1H chemical shifts	1006

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	PFV RNase H	1

Entities:

Entity 1, PFV RNase H 165 residues - Formula weight is not available

1

GLY

ALA

MET

GLY

GLN

TYR

GLU

GLY

VAL

PHE

2

TYR

THR

ASP

GLY

SER

ALA

ILE

LYS

SER

PRO

3

ASP

PRO

THR

LYS

SER

ASN

ALA

GLY

MET

4

GLY

ILE

VAL

HIS

ALA

THR

TYR

LYS

PRO

GLU

5

TYR

GLN

VAL

LEU

ASN

GLN

TRP

SER

ILE

PRO

6

LEU

GLY

ASN

HIS

THR

ALA

GLN

MET

ALA

GLU

7

ILE

ALA

VAL

GLU

PHE

ALA

CYS

LYS

8

ALA

LEU

LYS

ILE

PRO

GLY

PRO

VAL

LEU

VAL

9

ILE

THR

ASP

SER

PHE

TYR

VAL

ALA

GLU

SER

10

ALA

ASN

LYS

GLU

LEU

PRO

TYR

TRP

LYS

SER

11

ASN

GLY

PHE

VAL

ASN

LYS

PRO

12

LEU

LYS

HIS

ILE

SER

LYS

TRP

LYS

SER

ILE

13

ALA

GLU

CYS

LEU

SER

MET

LYS

PRO

ASP

ILE

14

THR

ILE

GLN

HIS

GLU

LYS

GLY

HIS

GLN

PRO

15

THR

ASN

THR

SER

ILE

HIS

THR

GLU

GLY

ASN

16

ALA

LEU

ALA

ASP

LYS

LEU

ALA

THR

GLN

GLY

17

SER

TYR

VAL

ASN

Samples:

sample_1: PFV RNase H, [U-13C; U-15N], 1 mM; H2O 90%; D2O 10%

sample_conditions_1: pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D C(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 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1

Software:

xwinnmr, Bruker Biospin - collection

NMRView, Johnson, One Moon Scientific - chemical shift assignment

NMR spectrometers:

Bruker Avance 700 MHz