BMRB Entry 16795

Name: Solution NMR of Putative excisionase from Klebsiella pneumoniae, Northeast Structural Genomics Consortium Target Target KpR49
Published: 2010-04-26

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PDB ID: 2kvv
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16795
MolProbity Validation Chart

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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution NMR of Putative excisionase from Klebsiella pneumoniae, Northeast Structural Genomics Consortium Target Target KpR49

Deposition date:

2010-03-28

Original release date:

2010-04-26

Authors:

Liu, G.; Hamilton, H.; Xiao, R.; Acton, T.; Rost, B.; Montelione, G.

Citation:

Citation: Liu, G.; Hamilton, H.; Xiao, R.; Acton, T.; Rost, B.; Montelione, G.. "Northeast Structural Genomics Consortium Target KpR49" To be published ., .-..

Assembly members:

Assembly members:
KpR49, polymer, 78 residues, 9304.643 Da.

Natural source:

Natural source: Common Name: Klebsiella pneumoniae Taxonomy ID: 573 Superkingdom: Bacteria Kingdom: not available Genus/species: Klebsiella pneumoniae

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: BL21

Entity Sequences (FASTA):

Entity Sequences (FASTA):
KpR49: MAQIIFNEEWMVEKALMVRT GLGARQIESYRQGAWIEGVH FKRVSPSGEKTLRGTTWYNY PEINKFIRDSLEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
spectral_peak_list
- spectral_peak_list_1
- spectral_peak_list_2

Data type	Count
13C chemical shifts	251
15N chemical shifts	77
1H chemical shifts	522

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	KpR49	1

Entities:

Entity 1, KpR49 78 residues - 9304.643 Da.

1

MET

ALA

GLN

ILE

PHE

ASN

GLU

TRP

2

MET

VAL

GLU

LYS

ALA

LEU

MET

VAL

ARG

THR

3

GLY

LEU

GLY

ALA

ARG

GLN

ILE

GLU

SER

TYR

4

ARG

GLN

GLY

ALA

TRP

ILE

GLU

GLY

VAL

HIS

5

PHE

LYS

ARG

VAL

SER

PRO

SER

GLY

GLU

LYS

6

THR

LEU

ARG

GLY

THR

TRP

TYR

ASN

TYR

7

PRO

GLU

ILE

ASN

LYS

PHE

ILE

ARG

ASP

SER

8

LEU

GLU

HIS

Samples:

sample_NC: KpR49, [U-100% 13C; U-100% 15N], 0.7 mM

sample_nc5: KpR49, [U-10% 13C; U-100% 15N], 0.8 mM

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_NC	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_nc5	isotropic	sample_conditions_1
3D HNCO	sample_NC	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_NC	isotropic	sample_conditions_1
3D HNCACB	sample_NC	isotropic	sample_conditions_1
3D 1H-13C arom NOESY	sample_NC	isotropic	sample_conditions_1
3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESY	sample_NC	isotropic	sample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinemen,structure solution,geometry optimization

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

AutoStruct v2.1, Huang, Tejero, Powers and Montelione - data analysis,refinement

AutoAssign v2.1, Zimmerman, Moseley, Kulikowski and Montelione - data analysis,chemical shift assignment

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

XEASY, Bartels et al. - data analysis,peak picking,chemical shift assignment

TOPSPIN, Bruker Biospin - collection

VNMRJ, Varian - collection

NMR spectrometers:

Bruker Avance 800 MHz
Varian INOVA 600 MHz

PDB	2KVV
EMBL	CEL82146 CEL85567 CEP30669 CTQ13220 CTQ20086
GB	ABR76809 ALD08109 ALD56363 EKB75770 ESA97574
REF	WP_004179593 WP_023159475