BMRB Entry 15577

Name: C Repressor
Published: 2008-10-14

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15577

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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:

C Repressor

Deposition date:

2007-12-03

Original release date:

2008-10-14

Authors:

Massad, Tariq; Papadopoulos, Evangelos; Damberg, Peter

Citation:

Citation: Massad, Tariq; Papadopoulos, Evangelos; Henriksson-Peltola, Petri; Haggard-Ljungquist, Elisabeth; Damberg, Peter. "Assignment of 1H, 13C, and 15N chemical shift resonances of P2 C-repressor protein" Biomol. NMR Assignments 2, 215-217 (2008).
PubMed: 19636908

Assembly members:

Assembly members:
Crepressor, polymer, 99 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Enterobacteria phage P2 Taxonomy ID: 10679 Superkingdom: Viruses Kingdom: not available Genus/species: P2-like viruses Enterobacteria phage P2

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pEE679

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Crepressor: MSNTISEKIVLMRKSEYLSR QQLADLTGVPYGTLSYYESG RSTPPTDVMMNILQTPQFTK YTLWFMTNQIAPESGQIAPA LAHFGQNETTSPHSGQKTG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	422
15N chemical shifts	106
1H chemical shifts	670

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Crepressor	1

Entities:

Entity 1, Crepressor 99 residues - Formula weight is not available

1

MET

SER

ASN

THR

ILE

SER

GLU

LYS

ILE

VAL

2

LEU

MET

ARG

LYS

SER

GLU

TYR

LEU

SER

ARG

3

GLN

LEU

ALA

ASP

LEU

THR

GLY

VAL

PRO

4

TYR

GLY

THR

LEU

SER

TYR

GLU

SER

GLY

5

ARG

SER

THR

PRO

THR

ASP

VAL

MET

6

ASN

ILE

LEU

GLN

THR

PRO

GLN

PHE

THR

LYS

7

TYR

THR

LEU

TRP

PHE

MET

THR

ASN

GLN

ILE

8

ALA

PRO

GLU

SER

GLY

GLN

ILE

ALA

PRO

ALA

9

LEU

ALA

HIS

PHE

GLY

GLN

ASN

GLU

THR

10

SER

PRO

HIS

SER

GLY

GLN

LYS

THR

GLY

Samples:

sample_1: Crepressor, [U-100% 13C; U-100% 15N], 0.6 mM; sodium phosphate 5 mM; D2O, [U-100% 2H], 10%; H2O 90%

sample_conditions_1: ionic strength: 0.005 M; pH: 6; pressure: 0.7 atm; temperature: 310 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HNHA	sample_1	isotropic	sample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

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

NMR spectrometers:

Varian INOVA 900 MHz
Varian INOVA 800 MHz
Varian INOVA 600 MHz
Bruker Avance 500 MHz

PDB	2L49 2XCJ
EMBL	CAJ43636 CAJ43638 CAJ43640 CAJ43642 CAJ43644
GB	AAD03298 AAO64734 ABJ01492 AHM44333 AHM48945
REF	NP_046787 WP_001306384 WP_001350698
SP	P04132
AlphaFold	P04132