BMRB Entry 17688

Name: Solution NMR Structure of Tfu_2981 from Thermobifida fusca, Northeast Structural Genomics Consortium Target TfR85A
Published: 2011-07-06

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PDB ID: 2le1
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17688
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution NMR Structure of Tfu_2981 from Thermobifida fusca, Northeast Structural Genomics Consortium Target TfR85A

Deposition date:

2011-06-03

Original release date:

2011-07-06

Authors:

Pulavarti, S. V. S. R. K; Eletsky, A; Mills, J.; Sukumaran, D.; Wang, D; Ciccosanti, C.; Hamilton, K.; Rost, B.; Acton, T.; Xiao, R.; Everett, J.; Lee, H; Prestegard, J.; Montelione, G.; Szyperski, Thomas

Citation:

Citation: Pulavarti, S. V. S. R. K; Eletsky, A; Mills, J.; Sukumaran, D.; Wang, D.; Ciccosanti, C.; Hamilton, K.; Rost, B.; Acton, T; Xiao, R.; Everett, J.; Lee, H; Prestegard, J.; Montelione, G.; Szyperski, Thomas. "Solution NMR Structure of Tfu_2981 from Thermobifida fusca, Northeast Structural Genomics Consortium Target TfR85A" To be published ., .-..

Assembly members:

Assembly members:
TfR85A, polymer, 151 residues, 16854.9 Da.

Natural source:

Natural source: Common Name: Thermobifida fusca Taxonomy ID: 2021 Superkingdom: Bacteria Kingdom: not available Genus/species: Thermobifida fusca

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
TfR85A: MATLRRSVEVAAPAADVWTL VGDFSAIHRWHPQVSAPTLR GASPHTPGAERVFGAGTEEE LVERLVERDESARRLVYTMP DPPFPITNHRAVLEVVPRDD RHCTVVWTAMFDCSPETARE LESVIGDGVFAVGLNALAER YGRLEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
spectral_peak_list

Data type	Count
13C chemical shifts	631
15N chemical shifts	149
1H chemical shifts	990

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	TfR85A	1

Entities:

Entity 1, TfR85A 151 residues - 16854.9 Da.

Residues1-143 in the sequence correspond to residues 1-143 of native protein. Residues from 144-151 represent non native affinity tag.

1

MET

ALA

THR

LEU

ARG

SER

VAL

GLU

VAL

2

ALA

PRO

ALA

ASP

VAL

TRP

THR

LEU

3

VAL

GLY

ASP

PHE

SER

ALA

ILE

HIS

ARG

TRP

4

HIS

PRO

GLN

VAL

SER

ALA

PRO

THR

LEU

ARG

5

GLY

ALA

SER

PRO

HIS

THR

PRO

GLY

ALA

GLU

6

ARG

VAL

PHE

GLY

ALA

GLY

THR

GLU

7

LEU

VAL

GLU

ARG

LEU

VAL

GLU

ARG

ASP

GLU

8

SER

ALA

ARG

LEU

VAL

TYR

THR

MET

PRO

9

ASP

PRO

PHE

PRO

ILE

THR

ASN

HIS

ARG

10

ALA

VAL

LEU

GLU

VAL

PRO

ARG

ASP

11

ARG

HIS

CYS

THR

VAL

TRP

THR

ALA

MET

12

PHE

ASP

CYS

SER

PRO

GLU

THR

ALA

ARG

GLU

13

LEU

GLU

SER

VAL

ILE

GLY

ASP

GLY

VAL

PHE

14

ALA

VAL

GLY

LEU

ASN

ALA

LEU

ALA

GLU

ARG

15

TYR

GLY

ARG

LEU

GLU

HIS

16

HIS

Samples:

NC5: TfR85A, [U-5% 13C; U-100% 15N], 1.338 mM; MES 20 mM; sodium chloride 100 mM; DTT 10 mM; DSS 50 uM; calcium chloride 5 mM; sodium azide 0.02%; H2O 90%; D2O 10%

NC: TfR85A, [U-100% 13C; U-100% 15N], 1.07 mM; MES 20 mM; sodium chloride 100 mM; DTT 10 mM; DSS 50 uM; calcium chloride 5 mM; sodium azide 0.02%; H2O 90%; D2O 10%

NC5_Pf1_phage: TfR85A, [U-5% 13C; U-100% 15N], 1.338 mM; MES 20 mM; sodium chloride 100 mM; DTT 10 mM; DSS 50 uM; calcium chloride 5 mM; sodium azide 0.02%; Pf1 phage 12.5 mg/mL; H2O 90%; D2O 10%

NC5_PEG: TfR85A, [U-5% 13C; U-100% 15N], 1.338 mM; MES 20 mM; sodium chloride 100 mM; DTT 10 mM; DSS 50 uM; calcium chloride 5 mM; sodium azide 0.02%; PEG 4%; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.11 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	NC	isotropic	sample_conditions_1
2D 1H-13C CT-HSQC	NC	isotropic	sample_conditions_1
3D HNCACB	NC	isotropic	sample_conditions_1
3D CBCA(CO)NH	NC	isotropic	sample_conditions_1
3D HNCO	NC	isotropic	sample_conditions_1
3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESY	NC	isotropic	sample_conditions_1
3D HN(CA)CO	NC	isotropic	sample_conditions_1
3D HCCH-TOCSY	NC	isotropic	sample_conditions_1
(4,3)D GFT HCCH-COSY-aliphatic	NC	isotropic	sample_conditions_1
(4,3)D GFT HCCH-COSY-aromatic	NC	isotropic	sample_conditions_1
2D 1H-13C CT-HSQC aromatic	NC	isotropic	sample_conditions_1
2D 1H-13C CT-HSQC methyl	NC5	isotropic	sample_conditions_1
2D J-modulation 1H-15N HSQC	NC5	isotropic	sample_conditions_1
2D J-modulation 1H-15N HSQC	NC5_Pf1_phage	anisotropic	sample_conditions_1
2D J-modulation 1H-15N HSQC	NC5_PEG	anisotropic	sample_conditions_1
2D 1H-15N LR-HSQC for Histidine	NC	isotropic	sample_conditions_1
3D HBHA(CO)NH	NC	isotropic	sample_conditions_1
2D (HB)CB(CGCDCE)HDHE	NC	isotropic	sample_conditions_1

Software:

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinemen,structure solution,geometry optimization

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - refinement, geometry optimization, solution structure

AutoStruct v2.1, Huang, Tejero, Powers and Montelione - data analysis,refinement

AutoAssign v2.3.0, Zimmerman, Moseley, Kulikowski and Montelione - data analysis,chemical shift assignment

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

PROSA v6.4, Guntert - processing

TOPSPIN v2.1, Bruker Biospin - collection, processing

PSVS, Bhattacharya and Montelione - structure analysis

TALOS+, Shen, Cornilescu, Delaglio and Bax - geometry optimization

PALES, PALES (Zweckstetter, Bax) - geometry optimization

CARA v1.8.4, Keller and Wuthrich - data analysis

NMR spectrometers:

Bruker Avance 900 MHz
Bruker Avance 600 MHz
Varian INOVA 750 MHz
Varian INOVA 600 MHz
Varian INOVA 500 MHz

PDB	2LE1
GB	AAZ57014 EOR69926
REF	WP_011293398