BMRB Entry 17952

Name: Backbone 1H, 13C, and 15N Chemical Shift Assignments for E.coli Ribonuclease P protein
Published: 2011-12-09

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PDB ID: 2ljp
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR17952
MolProbity Validation Chart

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

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Title:

Backbone 1H, 13C, and 15N Chemical Shift Assignments for E.coli Ribonuclease P protein

Deposition date:

2011-09-21

Original release date:

2011-12-09

Authors:

Shin, Jae-Sun; Kim, Kwang-Sun; Ryu, Kyongseok; Han, Kook; Lee, Younghoon; Choi, Byong-Seok

Citation:

Citation: Shin, Jae-Sun; Kim, Kwang-Sun; Ryu, Kyoung-Seok; Han, Kook; Lee, Younghoon; Choi, Byong-Seok. "Structural analysis of Escherichia coli C5 protein." Proteins 80, 963-967 (2012).
PubMed: 22423363

Assembly members:

Assembly members:
E.coli_Ribonuclease_P_protein, polymer, 119 residues, 13818.382 Da.

Natural source:

Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pSSC5

Entity Sequences (FASTA):

Entity Sequences (FASTA):
E.coli_Ribonuclease_P_protein: MVKLAFPRELRLLTPSQFTF VFQQPQRAGTPQITILGRLN SLGHPRIGLTVAKKNVRRAH ERNRIKRLTRESFRLRQHEL PAMDFVVVAKKGVADLDNRA LSEALEKLWRRHCRLARGS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	312
15N chemical shifts	116
1H chemical shifts	560

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	C5 protein monomer	1

Entities:

Entity 1, C5 protein monomer 119 residues - 13818.382 Da.

1

MET

VAL

LYS

LEU

ALA

PHE

PRO

ARG

GLU

LEU

2

ARG

LEU

THR

PRO

SER

GLN

PHE

THR

PHE

3

VAL

PHE

GLN

PRO

GLN

ARG

ALA

GLY

THR

4

PRO

GLN

ILE

THR

ILE

LEU

GLY

ARG

LEU

ASN

5

SER

LEU

GLY

HIS

PRO

ARG

ILE

GLY

LEU

THR

6

VAL

ALA

LYS

ASN

VAL

ARG

ALA

HIS

7

GLU

ARG

ASN

ARG

ILE

LYS

ARG

LEU

THR

ARG

8

GLU

SER

PHE

ARG

LEU

ARG

GLN

HIS

GLU

LEU

9

PRO

ALA

MET

ASP

PHE

VAL

ALA

LYS

10

LYS

GLY

VAL

ALA

ASP

LEU

ASP

ASN

ARG

ALA

11

LEU

SER

GLU

ALA

LEU

GLU

LYS

LEU

TRP

ARG

12

ARG

HIS

CYS

ARG

LEU

ALA

ARG

GLY

SER

Samples:

E.coli_Ribonuclease_P_protein_sample: E.coli Ribonuclease P protein, [U-95% 13C; U-95% 15N], 0.8 ± 0.2 mM; H2O 90%; D2O 10%; Sodium Phosphate 25 mM; Sodium Chloride 200 mM

E.coli_Ribonuclease_P_protein_conditions: ionic strength: 0.2 M; pH: 7.2; pressure: 1 atm; temperature: 293 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	E.coli_Ribonuclease_P_protein_sample	isotropic	E.coli_Ribonuclease_P_protein_conditions
2D 1H-13C HSQC	E.coli_Ribonuclease_P_protein_sample	isotropic	E.coli_Ribonuclease_P_protein_conditions
3D CBCA(CO)NH	E.coli_Ribonuclease_P_protein_sample	isotropic	E.coli_Ribonuclease_P_protein_conditions
3D C(CO)NH	E.coli_Ribonuclease_P_protein_sample	isotropic	E.coli_Ribonuclease_P_protein_conditions
3D HNCO	E.coli_Ribonuclease_P_protein_sample	isotropic	E.coli_Ribonuclease_P_protein_conditions
3D HNCACB	E.coli_Ribonuclease_P_protein_sample	isotropic	E.coli_Ribonuclease_P_protein_conditions
3D HBHA(CO)NH	E.coli_Ribonuclease_P_protein_sample	isotropic	E.coli_Ribonuclease_P_protein_conditions
3D HCCH-TOCSY	E.coli_Ribonuclease_P_protein_sample	isotropic	E.coli_Ribonuclease_P_protein_conditions
3D HCCH-COSY	E.coli_Ribonuclease_P_protein_sample	isotropic	E.coli_Ribonuclease_P_protein_conditions
3D 1H-13C NOESY aliphatic	E.coli_Ribonuclease_P_protein_sample	isotropic	E.coli_Ribonuclease_P_protein_conditions
3D 1H-15N NOESY	E.coli_Ribonuclease_P_protein_sample	isotropic	E.coli_Ribonuclease_P_protein_conditions

Software:

SPARKY, Goddard - data analysis

CNS v1.21, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

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

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

Varian INOVA 600 MHz
Bruker Avance 800 MHz

PDB	2LJP
DBJ	BAB38062 BAE77590 BAG79514 BAI28036 BAI33155
EMBL	CAA25983 CAD03155 CAP78163 CAQ34048 CAQ91434
GB	AAA24567 AAA62055 AAC76727 AAG58901 AAL22699
PIR	AG0957
PRF	1112173A
REF	NP_312666 NP_418159 NP_458102 NP_462740 NP_709496
SP	A1AHN8 A7ZTR0 A8A6G5 A8ACL6 A9MJT8
AlphaFold	A1AHN8 A7ZTR0 A8A6G5 A8ACL6 A9MJT8