BMRB Entry 19013

Name: Solution structure of the RRM domain of the hypothetical protein CAGL0M09691g from Candida glabrata
Published: 2013-03-06

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PDB ID: 2m4m
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19013
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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 RRM domain of the hypothetical protein CAGL0M09691g from Candida glabrata

Deposition date:

2013-02-07

Original release date:

2013-03-06

Authors:

Harris, R.; Hillerich, B.; Ahmed, M.; Bonanno, J.; Chamala, S.; Evans, B.; Lafleur, J.; Hammonds, J.; Washington, E.; Stead, M.; Love, J.; Attonito, J.; Seidel, R.; Chook, Y.; Rout, M.; Girvin, M.; Almo, S.; Harris, R.; Hillerich, B.; Ahmed, M.; Bonanno, J.; Chamala, S.; Evans, B.; Lafleur, J.; Washington, E.; Stead, M.; Love, J.; Attonito, J.; Patel, H.; Seidel, R.; Chook, Y.; Rout, M.; Girvin, M.; Almo, S.

Citation:

Citation: Harris, R.; Hillerich, B.; Ahmed, M.; Bonanno, J.; Chamala, S.; Evans, B.; Lafleur, J.; Hammonds, J.; Washington, E.; Stead, M.; Love, J.; Attonito, J.; Patel, H.; Seidel, R.; Chook, Y.; Rout, M.; Girvin, M.; Almo, S.. "Solution structure of the RRM domain of the hypothetical protein CAGL0M09691g from Candida glabrata" To be published ., .-..

Assembly members:

Assembly members:
RRM_domain_of_the_hypothetical_protein, polymer, 124 residues, 14227.990 Da.

Natural source:

Natural source: Common Name: ascomycetes Taxonomy ID: 5478 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Candida glabrata

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: modified pET26

Entity Sequences (FASTA):

Entity Sequences (FASTA):
RRM_domain_of_the_hypothetical_protein: MSLGSESETGNAVVVFGYRE AITKQILAYFAQFGEILEDL ESELGDTETMRTPGYFFQQA PNRRRISREHGRTWTKLTYA NHSSYLRALREHGTIYCGAA IGCVPYKHELISELSREGHH HHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	532
15N chemical shifts	131
1H chemical shifts	816

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	RRM domain of the hypothetical protein	1

Entities:

Entity 1, RRM domain of the hypothetical protein 124 residues - 14227.990 Da.

expressed sequence start-stop 171-283 N-term cloning artifact: MSL C-term cloning artifact: EGHHHHHH

1

MET

SER

LEU

GLY

SER

GLU

SER

GLU

THR

GLY

2

ASN

ALA

VAL

PHE

GLY

TYR

ARG

GLU

3

ALA

ILE

THR

LYS

GLN

ILE

LEU

ALA

TYR

PHE

4

ALA

GLN

PHE

GLY

GLU

ILE

LEU

GLU

ASP

LEU

5

GLU

SER

GLU

LEU

GLY

ASP

THR

GLU

THR

MET

6

ARG

THR

PRO

GLY

TYR

PHE

GLN

ALA

7

PRO

ASN

ARG

ILE

SER

ARG

GLU

HIS

8

GLY

ARG

THR

TRP

THR

LYS

LEU

THR

TYR

ALA

9

ASN

HIS

SER

TYR

LEU

ARG

ALA

LEU

ARG

10

GLU

HIS

GLY

THR

ILE

TYR

CYS

GLY

ALA

11

ILE

GLY

CYS

VAL

PRO

TYR

LYS

HIS

GLU

LEU

12

ILE

SER

GLU

LEU

SER

ARG

GLU

GLY

HIS

13

HIS

Samples:

sample_1: RRM domain of the hypothetical protein, [U-100% 13C; U-100% 15N], 1.0 mM; sodium acetate 10 mM; sodium chloride 100 mM; DTT 0.5 mM; EDTA 0.5 mM; H2O 90%; D2O 10%

sample_2: RRM domain of the hypothetical protein, [U-100% 13C; U-100% 15N], 1.0 mM; sodium acetate 10 mM; sodium chloride 100 mM; DTT 0.5 mM; EDTA 0.5 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 110 mM; pH: 4.5; 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_1
aromatic 13C HSQC	sample_2	isotropic	sample_conditions_1
13C NOESY-HSQC	sample_2	isotropic	sample_conditions_1
13C aromatic NOESY-HSQC	sample_2	isotropic	sample_conditions_1
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. - refinement

VNMRJ v2.2D, Varian - collection

TOPSPIN v2.1, Bruker Biospin - collection

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

CCPN_Analysis v2.2, CCPN - data analysis

ARIA v2.3, Linge, O'Donoghue and Nilges - data analysis

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

NMR spectrometers:

Varian Inova 600 MHz
Bruker Avance 800 MHz

UNP	Q6FJ27
PDB	2M4M
AlphaFold	Q6FJ27