BMRB Entry 30570

Name: NMR solution structure of Bcd1p120-303 from Saccharomyces cerevisiae
Published: 2020-08-14

Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR30570

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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: NMR solution structure of Bcd1p120-303 from Saccharomyces cerevisiae

Deposition date: 2019-02-12 Original release date: 2020-08-14

Authors: Bragantini, B.; Quinternet, M.; Charpentier, B.; Manival, X.

Citation: Bragantini, B.; Terral, G.; Tiotiu, D.; Charron, C.; Bourguet, M.; Rothe, B.; Paul, A.; Marty, H.; Labialle, S.; Quinternet, M.; Cianferani, S.; Manival, X.; Charpentier, B.. "Box C/D protein 1 and the histone chaperone Rtt106 are components of pre-snoRNPs through direct interaction" . ., .-..

Assembly members:
entity_1, polymer, 188 residues, 21864.262 Da.

Natural source: Common Name: Baker's yeast Taxonomy ID: 559292 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Saccharomyces cerevisiae

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

Entity Sequences (FASTA):
entity_1: GPHMRDSTECQRIIRRGVNC LMLPKGMQRSSQNRSKWDKT MDLFVWSVEWILCPMQEKGE KKELFKHVSHRIKETDFLVQ GMGKNVFQKCCEFYRLAGTS SCIEGEDGSETKEERTQILQ KSGLKFYTKTFPYNTTHIMD SKKLVELAIHEKCIGELLKN TTVIEFPTIFVAMTEADLPE GYEVLHQE

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	824
15N chemical shifts	202
1H chemical shifts	1355

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 188 residues - 21864.262 Da.

1

GLY

PRO

HIS

MET

ARG

ASP

SER

THR

GLU

CYS

2

GLN

ARG

ILE

ARG

GLY

VAL

ASN

CYS

3

LEU

MET

LEU

PRO

LYS

GLY

MET

GLN

ARG

SER

4

SER

GLN

ASN

ARG

SER

LYS

TRP

ASP

LYS

THR

5

MET

ASP

LEU

PHE

VAL

TRP

SER

VAL

GLU

TRP

6

ILE

LEU

CYS

PRO

MET

GLN

GLU

LYS

GLY

GLU

7

LYS

GLU

LEU

PHE

LYS

HIS

VAL

SER

HIS

8

ARG

ILE

LYS

GLU

THR

ASP

PHE

LEU

VAL

GLN

9

GLY

MET

GLY

LYS

ASN

VAL

PHE

GLN

LYS

CYS

10

CYS

GLU

PHE

TYR

ARG

LEU

ALA

GLY

THR

SER

11

SER

CYS

ILE

GLU

GLY

GLU

ASP

GLY

SER

GLU

12

THR

LYS

GLU

ARG

THR

GLN

ILE

LEU

GLN

13

LYS

SER

GLY

LEU

LYS

PHE

TYR

THR

LYS

THR

14

PHE

PRO

TYR

ASN

THR

HIS

ILE

MET

ASP

15

SER

LYS

LEU

VAL

GLU

LEU

ALA

ILE

HIS

16

GLU

LYS

CYS

ILE

GLY

GLU

LEU

LYS

ASN

17

THR

VAL

ILE

GLU

PHE

PRO

THR

ILE

PHE

18

VAL

ALA

MET

THR

GLU

ALA

ASP

LEU

PRO

GLU

19

GLY

TYR

GLU

VAL

LEU

HIS

GLN

GLU

Samples:

sample_1: Box C/D snoRNA protein 1, [U-13C; U-15N], 1 mM; sodium chloride 150 mM; sodium phosphate 10 mM; TCEP 0.5 mM

sample_2: Box C/D snoRNA protein 1, [U-13C; U-15N; U-2H], 1 mM; sodium chloride 150 mM; sodium phosphate 10 mM; TCEP 0.5 mM

sample_3: Box C/D snoRNA protein 1, [U-15N], 1 mM; sodium chloride 150 mM; sodium phosphate 10 mM; TCEP 0.5 mM; Pf1 phage 12 mg/mL

sample_conditions_1: ionic strength: 150 mM; pH: 6.4; pressure: 1 atm; temperature: 303 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_2	isotropic	sample_conditions_1
3D CCCONH	sample_2	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D HNHA	sample_1	isotropic	sample_conditions_1
3D HCCH-COSY	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D HNCACO	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_3	isotropic	sample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

CARA, Keller and Wuthrich - chemical shift assignment

TALOS, Cornilescu, Delaglio and Bax - structure calculation

TOPSPIN, Bruker Biospin - collection, processing

NMR spectrometers:

Bruker AvanceIII 600 MHz
Bruker AvanceIII 950 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts