BMRB Entry 5682

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR5682

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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 30S Ribosomal Protein S27E from Archaeoglobus Fulgidus: RS27_ARCFU: a novel fold

Deposition date:

2003-01-31

Original release date:

2004-06-30

Authors:

Herve Du Penhoat, C.; Atreya, H.; Shen, Y.; Liu, G.; Acton, T.; Xiao, R.; Montelione, G.; Szyperski, T.

Citation:

Citation: Herve Du Penhoat, C.; Atreya, H.; Shen, Y.; Liu, G.; Acton, T.; Xiao, R.; Dang, J.; Murray, D.; Montelione, G.; Szyperski, T.. "Solution Structure of 30S Ribosomal Protein S27E from Archaeoglobus Fulgidus: RS27_ARCFU: a novel fold" Protein Sci. 13, 1407-1416 (2004).
PubMed: 15096641

Assembly members:

Assembly members:
S27 ribosomal protein, polymer, 66 residues, 7578 Da.

Natural source:

Natural source: Common Name: Archaeoglobus fulgidus Taxonomy ID: 2234 Superkingdom: Archaea Kingdom: Fungi Genus/species: Archaeoglobus fulgidus

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
S27 ribosomal protein: MHSRFVKVKCPDCEHEQVIF DHPSTIVKCIICGRTVAEPT GGKGNIKAEIIEYVDQIELE HHHHHH

Data sets:

assigned_chemical_shifts
- chemical_shift_set_1
coupling_constants
- HNHA_set_1

Data type	Count
1H chemical shifts	408
13C chemical shifts	239
15N chemical shifts	58
coupling constants	33

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	30S RIBOSOMAL PROTEIN S27E	1

Entities:

Entity 1, 30S RIBOSOMAL PROTEIN S27E 66 residues - 7578 Da.

1

MET

HIS

SER

ARG

PHE

VAL

LYS

VAL

LYS

CYS

2

PRO

ASP

CYS

GLU

HIS

GLU

GLN

VAL

ILE

PHE

3

ASP

HIS

PRO

SER

THR

ILE

VAL

LYS

CYS

ILE

4

ILE

CYS

GLY

ARG

THR

VAL

ALA

GLU

PRO

THR

5

GLY

LYS

GLY

ASN

ILE

LYS

ALA

GLU

ILE

6

ILE

GLU

TYR

VAL

ASP

GLN

ILE

GLU

LEU

GLU

7

HIS

Samples:

Sample_1: S27 ribosomal protein, [U-100% 13C; U-100% 15N], 0.8 mM; MES 20 mM; NaCl 100 mM; DTT 10 mM; CaCl2 5 mM; NaN3 0.02%; D2O 5%; H2O 95%

Sample2: S27 ribosomal protein, [U-5% 13C; U-90% 15N], 0.8 mM; MES 20 mM; NaCl 100 mM; DTT 10 mM; CaCl2 5 mM; NaN3 0.02%; D2O 5%; H2O 95%

sample_cond_1: pH: 6.5 na; temperature: 298 K; pressure: 1.0 atm

Experiments:

Name	Sample	Sample state	Sample conditions
3D 13C-SEPARATED NOESY	not available	not available	sample_cond_1
3D 15N-SEPARATED NOESY	not available	not available	sample_cond_1
3D HNCACB	not available	not available	sample_cond_1
3D HCCH-COSY RD	not available	not available	sample_cond_1
3D HABCAB(CO)NH RD	not available	not available	sample_cond_1
3D HNHA	not available	not available	sample_cond_1
3D HNCO	not available	not available	sample_cond_1
2D [1H-1H] NOESY	not available	not available	sample_cond_1
2D C13HSQC	not available	not available	sample_cond_1
Constant time gChsqc	not available	not available	sample_cond_1
non-Constant time gChsqc	not available	not available	sample_cond_1
3D HNCO	not available	not available	sample_cond_1

Software:

CYANA v1.05 - refinement

DYANA v1.5 - structure solution

MOLMOL v1.0 - structure solution

XEASY v1.3.3 - structure solution

NMR spectrometers:

VARIAN UNITYPlus 500 MHz
VARIAN UNITYPlus 600 MHz

PDB	1QXF
GB	AAB89911 AIG98214
REF	NP_070163 WP_010878831
SP	O28935
AlphaFold	O28935