BMRB Entry 10095

Name: Solution structure of the KH domain of human ribosomal protein S3
Published: 2008-08-29

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PDB ID: 1wh9
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR10095
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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 KH domain of human ribosomal protein S3

Deposition date:

2007-02-13

Original release date:

2008-08-29

Authors:

Nameki, N.; Tomizawa, T.; Koshiba, S.; Kigawa, T.; Yokoyama, S.

Citation:

Citation: Nameki, N.; Tomizawa, T.; Koshiba, S.; Kigawa, T.; Yokoyama, S.. "Solution structure of the KH domain of human ribosomal protein S3" .

Assembly members:

Assembly members:
40S ribosomal protein S3, polymer, 92 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source: Production method: cell free synthesis Vector: P040301-10

Entity Sequences (FASTA):

Entity Sequences (FASTA):
40S ribosomal protein S3: GSSGSSGFKAELNEFLTREL AEDGYSGVEVRVTPTRTEII ILATRTQNVLGEKGRRIREL TAVVQKRFGFPEGSVELYAE KVATRGSGPSSG

Data sets:

assigned_chemical_shifts
- chemical_shift_1

Data type	Count
13C chemical shifts	362
15N chemical shifts	81
1H chemical shifts	572

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	40S ribosomal protein S3	1

Entities:

Entity 1, 40S ribosomal protein S3 92 residues - Formula weight is not available

1

GLY

SER

GLY

SER

GLY

PHE

LYS

ALA

2

GLU

LEU

ASN

GLU

PHE

LEU

THR

ARG

GLU

LEU

3

ALA

GLU

ASP

GLY

TYR

SER

GLY

VAL

GLU

VAL

4

ARG

VAL

THR

PRO

THR

ARG

THR

GLU

ILE

5

ILE

LEU

ALA

THR

ARG

THR

GLN

ASN

VAL

LEU

6

GLY

GLU

LYS

GLY

ARG

ILE

ARG

GLU

LEU

7

THR

ALA

VAL

GLN

LYS

ARG

PHE

GLY

PHE

8

PRO

GLU

GLY

SER

VAL

GLU

LEU

TYR

ALA

GLU

9

LYS

VAL

ALA

THR

ARG

GLY

SER

GLY

PRO

SER

10

SER

GLY

Samples:

sample_1: KH domain, [U-13C; U-15N], 0.6 mM; d-Tris-HCl 20 mM; NaCl 200 mM; d-DTT 1 mM; NaN3 0.02%; H2O 90%; D2O 10%

condition_1: ionic strength: 220 mM; pH: 7.0; pressure: 1 atm; temperature: 296 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 15N-separated NOESY	sample_1	isotropic	condition_1
3D 13C-separated NOESY	sample_1	isotropic	condition_1

Software:

xwinnmr v2.6, Bruker - collection

NMRPipe v20020425, Delaglio, F. - processing

NMRView v5.0.4, Johnson, B.A. - data analysis

Kujira v0.901, Kobayashi, N. - data analysis

CYANA v1.0.7, Guntert, P. - structure solution

OPALp, Billeter, M., Guntert, P., Koradi, R. - refinement

NMR spectrometers:

Bruker AVANCE 800 MHz

PDB	1WH9 2ZKQ 3J3A 4CXC 4D5L 4D61 4KZX 4KZY 4KZZ 4UQ4 4UQ5 4W23 4W28 5A2Q
DBJ	BAB22624 BAB27042 BAB27761 BAB28111 BAB28159
EMBL	CAA35916 CAA39248 CAA40592 CAA54167 CAA84290
GB	AAA18095 AAB19349 AAB46849 AAB60336 AAB60337
REF	NP_000996 NP_001009239 NP_001026007 NP_001029219 NP_001038066
SP	E2RH47 P02350 P23396 P47835 P62908
TPG	DAA21909
AlphaFold	E2RH47 P02350 P23396 P47835 P62908