BMRB Entry 10139

Name: Backbone NMR assignments of RimM from Thermus thermophilus
Published: 2008-06-12

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR10139

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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:

Backbone NMR assignments of RimM from Thermus thermophilus

Deposition date:

2007-06-13

Original release date:

2008-06-12

Authors:

Suzuki, S.; Tatsuguchi, A.; Matsumoto, E.; Kawazoe, M.; Kaminishi, T.; Shirouzu, M.; Muto, Y.; Takemoto, C.; Yokoyama, S.

Citation:

Citation: Suzuki, S.; Tatsuguchi, A.; Matsumoto, E.; Kawazoe, M.; Kaminishi, T.; Shirouzu, M.; Muto, Y.; Takemoto, C.; Yokoyama, S.. "Structural characterization of the ribosome maturation protein, RimM" J. Bacteriol. 189, .-6397 (6406).
PubMed: 17616598

Assembly members:

Assembly members:
RimM, polymer, 162 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Thermus thermophilus Taxonomy ID: 274 Superkingdom: Bacteria Kingdom: not available Genus/species: Thermus thermophilus

Experimental source:

Experimental source: Production method: recombinant technology Vector: PC011033-04

Entity Sequences (FASTA):

Entity Sequences (FASTA):
RimM: MRLVEIGRFGAPYALKGGLR FRGEPVVLHLERVYVEGHGW RAIEDLYRVGEELVVHLAGV TDRTLAEALVGLRVYAEVAD LPPLEEGRYYYFALIGLPVY VEGRQVGEVVDILDAGAQDV LIIRGVGERLRDRAERLVPL QAPYVRVEEGSIHVDPIPGL FD

Data sets:

assigned_chemical_shifts
- chemical_shift_1

Data type	Count
13C chemical shifts	413
15N chemical shifts	136
1H chemical shifts	136

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	RimM	1

Entities:

Entity 1, RimM 162 residues - Formula weight is not available

1

MET

ARG

LEU

VAL

GLU

ILE

GLY

ARG

PHE

GLY

2

ALA

PRO

TYR

ALA

LEU

LYS

GLY

LEU

ARG

3

PHE

ARG

GLY

GLU

PRO

VAL

LEU

HIS

LEU

4

GLU

ARG

VAL

TYR

VAL

GLU

GLY

HIS

GLY

TRP

5

ARG

ALA

ILE

GLU

ASP

LEU

TYR

ARG

VAL

GLY

6

GLU

LEU

VAL

HIS

LEU

ALA

GLY

VAL

7

THR

ASP

ARG

THR

LEU

ALA

GLU

ALA

LEU

VAL

8

GLY

LEU

ARG

VAL

TYR

ALA

GLU

VAL

ALA

ASP

9

LEU

PRO

LEU

GLU

GLY

ARG

TYR

10

TYR

PHE

ALA

LEU

ILE

GLY

LEU

PRO

VAL

TYR

11

VAL

GLU

GLY

ARG

GLN

VAL

GLY

GLU

VAL

12

ASP

ILE

LEU

ASP

ALA

GLY

ALA

GLN

ASP

VAL

13

LEU

ILE

ARG

GLY

VAL

GLY

GLU

ARG

LEU

14

ARG

ASP

ARG

ALA

GLU

ARG

LEU

VAL

PRO

LEU

15

GLN

ALA

PRO

TYR

VAL

ARG

VAL

GLU

GLY

16

SER

ILE

HIS

VAL

ASP

PRO

ILE

PRO

GLY

LEU

17

PHE

ASP

Samples:

sample_1: RimM, [U-13C; U-15N], 0.2 mM; HEPES 20 mM; D2O 10%; H2O 90%; NaCl 300 mM

condition_1: ionic strength: 320 mM; pH: 7.0; pressure: 1 atm; temperature: 318 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCA	sample_1	not available	condition_1
3D HN(CO)CA	sample_1	not available	condition_1
3D HNCO	sample_1	not available	condition_1
3D HN(CA)CO	sample_1	not available	condition_1
3D CBCA(CO)NH	sample_1	not available	condition_1
3D HNCACB	sample_1	not available	condition_1
3D C(CO)NH	sample_1	not available	condition_1

Software:

xwinnmr v3.5, Bruker - collection

NMRPipe v20031121, Delaglio, F. - processing

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

Kujira v0.9321, Kobayashi, N. - data analysis

Olivia v1.10.5, Yokochi, M. - data analysis

SPARKY v3.110, Goddard, T.D., Kneller, D.G. - data analysis

NMR spectrometers:

Bruker AVANCE 800 MHz

BMRB	10138 10140
PDB	2DOG 2DYI 3A1P
DBJ	BAD70856
GB	AAS81019 AEG33454 AFH38925 EIA39096
REF	WP_008632437 WP_011228392 YP_144299
SP	Q5SJH5 Q72JU7
AlphaFold	Q5SJH5 Q72JU7