BMRB Entry 16649

Name: Solution NMR structure of the PCP_red domain of light-independent protochlorophyllide reductase subunit B from Chlorobium tepidum. Northeast Structural Genomics Consortium Target CtR69A
Published: 2010-02-22

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PDB ID: 2kru
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR16649
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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution NMR structure of the PCP_red domain of light-independent protochlorophyllide reductase subunit B from Chlorobium tepidum. Northeast Structural Genomics Consortium Target CtR69A

Deposition date:

2009-12-22

Original release date:

2010-02-22

Authors:

He, Yunfen; Eletsky, Alexander; Lee, Dan; Ciccosanti, Colleen; Janjua, Haleema; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Szyperski, Thomas

Citation:

Citation: He, Yunfen; Eletsky, Alexander; Lee, Dan; Ciccosanti, Colleen; Janjua, Haleema; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Szyperski, Thomas. "Solution NMR structure of the PCP_red domain of light-independent protochlorophyllide reductase subunit B from Chlorobium tepidum. Northeast Structural Genomics Consortium Target CtR69A" .

Assembly members:

Assembly members:
CtR69A, polymer, 63 residues, 7319.465 Da.

Natural source:

Natural source: Common Name: green sulfur bacteria Taxonomy ID: 1097 Superkingdom: Bacteria Kingdom: not available Genus/species: Chlorobium tepidum

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET 21-23C

Entity Sequences (FASTA):

Entity Sequences (FASTA):
CtR69A: MGELSWTAEAEKMLGKVPFF VRKKVRKNTDNYAREIGEPV VTADVFRKAKEHLGGLEHHH HHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
spectral_peak_list

Data type	Count
13C chemical shifts	255
15N chemical shifts	63
1H chemical shifts	414

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	CtR69A	1

Entities:

Entity 1, CtR69A 63 residues - 7319.465 Da.

Residues 2-55 correspond to residues 484-537 of the native protein. Residues 56-63 represent a non-native affinity tag. Residue 1 corresponds the introduced start-codon.

1

MET

GLY

GLU

LEU

SER

TRP

THR

ALA

GLU

ALA

2

GLU

LYS

MET

LEU

GLY

LYS

VAL

PRO

PHE

3

VAL

ARG

LYS

VAL

ARG

LYS

ASN

THR

ASP

4

ASN

TYR

ALA

ARG

GLU

ILE

GLY

GLU

PRO

VAL

5

VAL

THR

ALA

ASP

VAL

PHE

ARG

LYS

ALA

LYS

6

GLU

HIS

LEU

GLY

LEU

GLU

HIS

7

HIS

Samples:

sample_1: entity, [U-100% 13C; U-100% 15N], 1.080 mM; MES 20 mM; sodium chloride 100 mM; calcium chloride 5 mM; NaN3 0.02%

sample_2: entity, [U-5% 13C; U-100% 15N], 0.986 mM; MES 20 mM; sodium chloride 100 mM; calcium chloride 5 mM; NaN3 0.02%

sample_conditions_1: ionic strength: 117.5 mM; 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
2D 1H-13C CT-HSQC ali	sample_1	isotropic	sample_conditions_1
2D 1H-13C CT-HSQC (methyl)	sample_2	isotropic	sample_conditions_1
3D HNCO	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 HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HCCH-COSY ali	sample_1	isotropic	sample_conditions_1
13C/15N-NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-13C CT-HSQC aro	sample_1	isotropic	sample_conditions_1
3D HCCH-COSY aro	sample_1	isotropic	sample_conditions_1
2D 1H-15N LR-HSQC (Histidine)	sample_1	isotropic	sample_conditions_1

Software:

VNMRJ v2.1B, Varian - collection

PROSA v6.4, Guntert - processing

XEASY, Bartels et al. - data analysis

PINE v1.0, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

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

AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - structure solution

TALOS+ v1.2009.0721.18, Shen, Cornilescu, Delaglio and Bax - data analysis

CNS v1.2.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CARA v1.8.4, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking

PSVS v1.3, Bhattacharya and Montelione - validation

NMR spectrometers:

Varian INOVA 500 MHz
Varian INOVA 750 MHz

PDB	2KRU
GB	AAG12202 AAM73367
REF	NP_663025 WP_010933804
SP	Q9F715
AlphaFold	Q9F715