BMRB Entry 18749

Name: Ligase 10C
Published: 2012-11-02

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PDB ID: 2lze
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18749
MolProbity Validation Chart

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

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Title:

Ligase 10C

Deposition date:

2012-10-01

Original release date:

2012-11-02

Authors:

Chao, Fa-An; Morelli, Aleardo; Haugner, John; Churchfield, Lewis; Hagmann, Leonardo; Shi, Lei; Masterson, Larry; Sarangi, Ritimukta; Veglia, Gianluigi; Seelig, Burckhard

Citation:

Citation: Chao, Fa-An; Morelli, Aleardo; Iii, John C Haugner; Churchfield, Lewis; Hagmann, Leonardo; Shi, Lei; Masterson, Larry; Sarangi, Ritimukta; Veglia, Gianluigi; Seelig, Burckhard. "Structure and dynamics of a primordial catalytic fold generated by in vitro evolution." Nat. Chem. Biol. 9, 81-83 (2013).
PubMed: 23222886

Assembly members:

Assembly members:
entity, polymer, 87 residues, 9795.925 Da.
ZINC ION, non-polymer, 65.409 Da.

Natural source:

Natural source: Common Name: not available Taxonomy ID: not available Superkingdom: not available Kingdom: not available Genus/species: not available not available

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET24

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: MGAPVPYPDPLEPRGGKHIC AICGNNAEDYKHTDMDLTYT DRDYKNCESYHKCSDLCQYC RYQKDLAIHHQHHHGGSMGM SGSGTGY

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	227
15N chemical shifts	61
1H chemical shifts	320

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Ligase 10C	1
2	Zinc Ion	2

Entities:

Entity 1, Ligase 10C 87 residues - 9795.925 Da.

1

MET

GLY

ALA

PRO

VAL

PRO

TYR

PRO

ASP

PRO

2

LEU

GLU

PRO

ARG

GLY

LYS

HIS

ILE

CYS

3

ALA

ILE

CYS

GLY

ASN

ALA

GLU

ASP

TYR

4

LYS

HIS

THR

ASP

MET

ASP

LEU

THR

TYR

THR

5

ASP

ARG

ASP

TYR

LYS

ASN

CYS

GLU

SER

TYR

6

HIS

LYS

CYS

SER

ASP

LEU

CYS

GLN

TYR

CYS

7

ARG

TYR

GLN

LYS

ASP

LEU

ALA

ILE

HIS

8

GLN

HIS

GLY

SER

MET

GLY

MET

9

SER

GLY

SER

GLY

THR

GLY

TYR

Entity 2, Zinc Ion - Zn - 65.409 Da.

1

ZN

Samples:

sample_1: entity, [U-99% 15N], 1 mM; H2O 90%; D2O 10%; NaCl 150 mM; HEPES 20 mM; beta-mercaptoenthanol 10 mM

sample_2: entity, [U-99% 13C; U-99% 15N], 1 mM; H2O 90%; D2O 10%; NaCl 150 mM; HEPES 20 mM; beta-mercaptoenthanol 10 mM

sample_conditions_1: ionic strength: 0.16 M; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D 1H-15N TOCSY	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 H(CCO)NH	sample_2	isotropic	sample_conditions_1
3D C(CO)NH	sample_2	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N CPMG	sample_1	isotropic	sample_conditions_1
2D 1H-15N T1	sample_1	isotropic	sample_conditions_1
2D 1H-15N T2	sample_1	isotropic	sample_conditions_1
2D 1H-15N ssNOE	sample_1	isotropic	sample_conditions_1

Software:

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution

PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

NMR spectrometers:

Bruker Avance 700 MHz
Varian INOVA 600 MHz