BMRB Entry 19168

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PDB ID: 2m71
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19168
MolProbity Validation Chart

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Solution structure of the a C-terminal domain of translation initiation factor IF-3 from Campylobacter jejuni

Deposition date: 2013-04-16 Original release date: 2013-05-13

Authors: Harris, R.; Ahmed, M.; Attonito, J.; Bonanno, J.; Chamala, S.; Chowdhury, S.; Evans, B.; Fiser, A.; Glenn, A.; Hammonds, J.; Hillerich, B.; Khafizov, K.; Lafleur, J.; Love, J.; Seidel, R.; Stead, M.; Girvin, M.; Almo, S.

Citation: Harris, R.; Ahmed, M.; Attonito, J.; Bonanno, J.; Chamala, S.; Chowdhury, S.; Evans, B.; Fiser, A.; Glenn, A.; Hammonds, J.; Hillerich, B.; Khafizov, K.; Lafleur, J.; Love, J.; Seidel, R.; Stead, M.; Girvin, M.; Almo, S.. "Solution structure of the a C-terminal domain of translation initiation factor IF-3 from Campylobacter jejuni" To be published ., .-..

Assembly members:
IF-3, polymer, 101 residues, 11502.454 Da.

Natural source: Common Name: e-proteobacteria Taxonomy ID: 197 Superkingdom: Bacteria Kingdom: not available Genus/species: Campylobacter jejuni

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

Entity Sequences (FASTA):
IF-3: MSLKVIDIKEIKLSVKIAQN DINYKVKHALEFLEQGKHVR FRVFLKGREMATPEAGVALL EKIWTMIENEANRDKEPNFE GRYVNMLVTPKKAEGHHHHH H

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	433
15N chemical shifts	95
1H chemical shifts	703

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	IF-3	1

Entities:

Entity 1, IF-3 101 residues - 11502.454 Da.

expressed sequence start-stop 83-172 N-term cloning artifact: MSL C-term cloning artifact: EGHHHHHH

1

MET

SER

LEU

LYS

VAL

ILE

ASP

ILE

LYS

GLU

2

ILE

LYS

LEU

SER

VAL

LYS

ILE

ALA

GLN

ASN

3

ASP

ILE

ASN

TYR

LYS

VAL

LYS

HIS

ALA

LEU

4

GLU

PHE

LEU

GLU

GLN

GLY

LYS

HIS

VAL

ARG

5

PHE

ARG

VAL

PHE

LEU

LYS

GLY

ARG

GLU

MET

6

ALA

THR

PRO

GLU

ALA

GLY

VAL

ALA

LEU

7

GLU

LYS

ILE

TRP

THR

MET

ILE

GLU

ASN

GLU

8

ALA

ASN

ARG

ASP

LYS

GLU

PRO

ASN

PHE

GLU

9

GLY

ARG

TYR

VAL

ASN

MET

LEU

VAL

THR

PRO

10

LYS

ALA

GLU

GLY

HIS

11

HIS

Samples:

sample_1: IF-3, [U-100% 13C; U-100% 15N], 1 mM; H2O 90%; D2O 10%; Na phosphate buffer 20 mM; NaCl 50 mM; EDTA 0.1 mM

sample_2: IF-3, [U-100% 13C; U-100% 15N], 1 mM; D2O 100%; Na phosphate buffer 20 mM; NaCl 50 mM; EDTA 0.1 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.8; pressure: 1 ATM; temperature: 298 K

sample_conditions_2: ionic strength: 50 mM; pH: 6.8; pressure: 1 ATM; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
15N HSQC	sample_1	isotropic	sample_conditions_1
15N NOESY-HSQC	sample_1	isotropic	sample_conditions_1
13C HSQC	sample_2	isotropic	sample_conditions_2
aromatic 13C HSQC	sample_2	isotropic	sample_conditions_2
13C NOESY-HSQC	sample_2	isotropic	sample_conditions_2
13C aromatic NOESY-HSQC	sample_2	isotropic	sample_conditions_2
HNCO	sample_1	isotropic	sample_conditions_1
HNCACO	sample_1	isotropic	sample_conditions_1
HNCA	sample_1	isotropic	sample_conditions_1
HNCOCA	sample_1	isotropic	sample_conditions_1
HNCACB	sample_1	isotropic	sample_conditions_1
CBCACONH	sample_1	isotropic	sample_conditions_1

Software:

CNS v1.21, Brunger A. T. et.al. - structure calcuation

X-PLOR NIH v2.32, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution

ARIA v2.3, Linge, O'Donoghue and Nilges - structure solution

CCPN_Analysis v2.2, CCPN - chemical shift assignment, data analysis, peak picking

MDDNMR v2.2, (MDDNMR) Orekhov, Jaravine, Kazimierczuk - collection, processing

MDDGUI v1.0, (MDDGUI) Lemak, Gutmanas, Chitayat, Karra, Fares, Sunnerhagen, Arrowsmith - collection, processing

NMRPipe v7.5, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

VNMRJ v2.2D, Varian - collection

TOPSPIN v2.1, Bruker Biospin - collection

MolProbity v4.01a, Richardson - data analysis

NMR spectrometers:

Varian Inova 600 MHz
Bruker Avance 700 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts