BMRB Entry 19607

Name: The C-terminal domain of SRA1p has a fold more similar to PRP18 than to an RRM and does not directly bind to the SRA1 RNA STR7 region.
Published: 2014-02-10

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PDB ID: 2mgx
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19607
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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:

The C-terminal domain of SRA1p has a fold more similar to PRP18 than to an RRM and does not directly bind to the SRA1 RNA STR7 region.

Deposition date:

2013-11-10

Original release date:

2014-02-10

Authors:

Bilinovich, Stephanie; Davis, Caroline; Morris, Daniel; Ray, Louis; Prokop, Jeremy; Buchan, Greg; Leeper, Thomas

Citation:

Citation: Bilinovich, Stephanie; Davis, Caroline; Morris, Daniel; Ray, Louis; Prokop, Jeremy; Buchan, Gregory; Leeper, Thomas. "The C-Terminal Domain of SRA1p Has a Fold More Similar to PRP18 than to an RRM and Does Not Directly Bind to the SRA1 RNA STR7 Region." J. Mol. Biol. ., .-. (2014).
PubMed: 24486611

Assembly members:

Assembly members:
SRA1p_C-terminal_domain, polymer, 131 residues, 14769.870 Da.

Natural source:

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
SRA1p_C-terminal_domain: GSEAVMEDVLRPLEQALEDC RGHTRKQVCDDISRRLALLQ EQWAGGKLSIPVKKRMALLV QELSSHRWDAADDIHRSLMV DHVTEVSQWMVGVKRLIAEK RSLFSEEAANEEKSAATAEK NHTIPGFQQAS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	536
15N chemical shifts	130
1H chemical shifts	789

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	C-terminal domain of SRA1p	1

Entities:

Entity 1, C-terminal domain of SRA1p 131 residues - 14769.870 Da.

1

GLY

SER

GLU

ALA

VAL

MET

GLU

ASP

VAL

LEU

2

ARG

PRO

LEU

GLU

GLN

ALA

LEU

GLU

ASP

CYS

3

ARG

GLY

HIS

THR

ARG

LYS

GLN

VAL

CYS

ASP

4

ASP

ILE

SER

ARG

LEU

ALA

LEU

GLN

5

GLU

GLN

TRP

ALA

GLY

LYS

LEU

SER

ILE

6

PRO

VAL

LYS

ARG

MET

ALA

LEU

VAL

7

GLN

GLU

LEU

SER

HIS

ARG

TRP

ASP

ALA

8

ALA

ASP

ILE

HIS

ARG

SER

LEU

MET

VAL

9

ASP

HIS

VAL

THR

GLU

VAL

SER

GLN

TRP

MET

10

VAL

GLY

VAL

LYS

ARG

LEU

ILE

ALA

GLU

LYS

11

ARG

SER

LEU

PHE

SER

GLU

ALA

ASN

12

GLU

LYS

SER

ALA

THR

ALA

GLU

LYS

13

ASN

HIS

THR

ILE

PRO

GLY

PHE

GLN

ALA

14

SER

Samples:

sample_1: sodium phosphate 50 mM; DTT 2 mM; sodium chloride 50 mM; SRA1p C-terminal domain, [U-98% 13C; U-98% 15N], 0.6 mM; H2O 95%; D2O 5%

sample_2: sodium phosphate 50 mM; DTT 2 mM; sodium chloride 50 mM; SRA1p C-terminal domain, [U-98% 13C; U-98% 15N], 0.6 mM; D2O 100%

sample_conditions_1: ionic strength: 100 mM; pH: 7.4; pressure: 1 atm; temperature: 273 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_1
3D HN(COCA)CB	sample_1	anisotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3d HNCAintra	sample_1	isotropic	sample_conditions_1
3D HNCACBintra	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
2D HBCBCGCDCDHE	sample_1	isotropic	sample_conditions_1
2D HBCBCGCDHD	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1

Software:

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

CCPN, CCPN - chemical shift assignment

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

NMR spectrometers:

Varian INOVA 750 MHz

UNP	Q9HD15.1
PDB	2MGX 4NBO
DBJ	BAG51445 BAJ20657
EMBL	CAH93286
GB	AAG02114 AAG02115 AAG02116 AAH40043 AAI52789
REF	NP_001030312 NP_001240693 XP_001086694 XP_001137717 XP_002816012
SP	Q9HD15
AlphaFold	Q9HD14 Q9HD15