BMRB Entry 16802

Name: Solution structure of N-terminal domain of CcmH from Escherichia.coli
Published: 2014-03-04

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PDB ID: 2kw0
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16802
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution structure of N-terminal domain of CcmH from Escherichia.coli

Deposition date:

2010-03-30

Original release date:

2014-03-04

Authors:

Hong, Jing; Zheng, Xueming; Hu, Hongyu; Lin, Donghai

Citation:

Citation: Zheng, Xue-Ming; Hong, Jing; Li, Hai-Yin; Lin, Dong-Hai; Hu, Hong-Yu. "Biochemical properties and catalytic domain structure of the CcmH protein from Escherichia coli." Biochim. Biophys. Acta 1824, 1394-1400 (2012).
PubMed: 22789558

Assembly members:

Assembly members:
CcmH, polymer, 81 residues, 9459.733 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: pet22b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
CcmH: TIDVLQFKDEAQEQQFRQLT EELRCPKCQNNSIADSNSMI ATDLRQKVYELMQEGKSKKE IVDYMVARYGNFVTYDPPLT P

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	323
15N chemical shifts	73
1H chemical shifts	566

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	CcmH	1

Entities:

Entity 1, CcmH 81 residues - 9459.733 Da.

1

THR

ILE

ASP

VAL

LEU

GLN

PHE

LYS

ASP

GLU

2

ALA

GLN

GLU

GLN

PHE

ARG

GLN

LEU

THR

3

GLU

LEU

ARG

CYS

PRO

LYS

CYS

GLN

ASN

4

ASN

SER

ILE

ALA

ASP

SER

ASN

SER

MET

ILE

5

ALA

THR

ASP

LEU

ARG

GLN

LYS

VAL

TYR

GLU

6

LEU

MET

GLN

GLU

GLY

LYS

SER

LYS

GLU

7

ILE

VAL

ASP

TYR

MET

VAL

ALA

ARG

TYR

GLY

8

ASN

PHE

VAL

THR

TYR

ASP

PRO

LEU

THR

9

PRO

Samples:

sample_1: entity 1 mM; D2O 10%; sodium phosphate 50 mM; sodium chloride 100 mM; DTT 5 mM; H2O 90%

sample_2: entity 1 mM; D2O 100%; sodium phosphate 50 mM; sodium chloride 100 mM; DTT 5 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_2	isotropic	sample_conditions_1

Software:

CNS, Brunger A. T. et.al. - refinement

NMR spectrometers:

Varian INOVA 600 MHz

PDB	2KW0
DBJ	BAB36506 BAE76657 BAG77986 BAI26332 BAI31440
EMBL	CAP76696 CAQ32597 CAQ89785 CAQ99121 CAR03622
GB	AAA16386 AAC75254 AAG57329 AAN43797 AAN81185
REF	NP_311110 NP_416698 NP_708090 WP_001211546 WP_001211547
SP	P0ABM9 P0ABN0
AlphaFold	P0ABM9 P0ABN0