BMRB Entry 16316

Name: NMR structure of IntB phage-integrase-like protein fragment 90-199 from Erwinia carotova subsp. atroseptica: Northeast Structural Genomics Consortium target EwR217E
Published: 2012-08-03

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PDB ID: 2kj9
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16316
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

NMR structure of IntB phage-integrase-like protein fragment 90-199 from Erwinia carotova subsp. atroseptica: Northeast Structural Genomics Consortium target EwR217E

Deposition date:

2009-05-26

Original release date:

2012-08-03

Authors:

Cort, John; Ramelot, Theresa; Wang, Dongyan; Ciccosanti, Colleen; Janjua, Haleema; Nair, Rajesh; Rost, Burkhard; Swapna, G.V.T.; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Kennedy, Michael

Citation:

Citation: Cort, John; Montelione, Gaetano; Kennedy, Michael. "NMR structure of IntB phage-integrase-like protein fragment 90-199 from Erwinia carotova subsp. atroseptica" .

Assembly members:

Assembly members:
fragment 90-199, polymer, 118 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Bacterium carotovorum Taxonomy ID: 554 Superkingdom: Bacteria Kingdom: not available Genus/species: Erwinia carotovora

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET21-23C

Entity Sequences (FASTA):

Entity Sequences (FASTA):
fragment 90-199: KSVQEKRNNTRAFKTVAKSW FATKTTWSEDYQRSVWTRLE TYLFPDIGNKDIAELDTGDL LVPIKKIEKLGYLEIAMRVK QYATAIMRYAVQQKMIRFNP AYDLEGAVQKLEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	505
15N chemical shifts	122
1H chemical shifts	778

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	fragment 90-199	1

Entities:

Entity 1, fragment 90-199 118 residues - Formula weight is not available

1

LYS

SER

VAL

GLN

GLU

LYS

ARG

ASN

THR

2

ARG

ALA

PHE

LYS

THR

VAL

ALA

LYS

SER

TRP

3

PHE

ALA

THR

LYS

THR

TRP

SER

GLU

ASP

4

TYR

GLN

ARG

SER

VAL

TRP

THR

ARG

LEU

GLU

5

THR

TYR

LEU

PHE

PRO

ASP

ILE

GLY

ASN

LYS

6

ASP

ILE

ALA

GLU

LEU

ASP

THR

GLY

ASP

LEU

7

LEU

VAL

PRO

ILE

LYS

ILE

GLU

LYS

LEU

8

GLY

TYR

LEU

GLU

ILE

ALA

MET

ARG

VAL

LYS

9

GLN

TYR

ALA

THR

ALA

ILE

MET

ARG

TYR

ALA

10

VAL

GLN

LYS

MET

ILE

ARG

PHE

ASN

PRO

11

ALA

TYR

ASP

LEU

GLU

GLY

ALA

VAL

GLN

LYS

12

LEU

GLU

HIS

Samples:

sample_1: entity, [U-99% 13C; U-99% 15N], 1 mM; MES 20 mM; sodium chloride 200 mM; calcium chloride 5 mM; sodium azide 0.02 w/v; H2O 95%; D2O, [U-99% 2H], 5%

sample_2: entity, [5% biosynthetically directed 13C; U-99% 15N], 0.7 mM; MES 20 mM; sodium chloride 200 mM; calcium chloride 5 mM; sodium azide 0.02 w/v; H2O 95%; D2O, [U-99% 2H], 5%

sample_3: entity, [U-99% 13C; U-99% 15N], 0.7 mM; MES 20 mM; sodium chloride 200 mM; calcium chloride 5 mM; sodium azide 0.02 w/v; D2O, [U-99% 2H], 100%

sample_conditions_1: ionic strength: 215 mM; pH: 6.5; pressure: 1 atm; temperature: 293 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	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 HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HNHA	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_1
4D 1H-13C-13C-1H HMQC-NOESY-HMQC	sample_3	isotropic	sample_conditions_1

Software:

AutoStruct, Huang, Tejero, Powers and Montelione - structure solution

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement

SPARKY, Goddard - chemical shift assignment, data analysis

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

FELIX, Accelrys Software Inc. - processing

NMR spectrometers:

Varian INOVA 600 MHz
Varian INOVA 750 MHz