BMRB Entry 15837

Name: NMR CHEMICAL SHIFT ASSIGNMENTS OF IRON(II) TRANSPORT PROTEIN A FROM CLOSTRIDIUM THERMOCELLUM , NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG) TARGET VR131
Published: 2008-08-22

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PDB ID: 2k5i
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15837
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

NMR CHEMICAL SHIFT ASSIGNMENTS OF IRON(II) TRANSPORT PROTEIN A FROM CLOSTRIDIUM THERMOCELLUM , NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG) TARGET VR131

Deposition date:

2008-06-27

Original release date:

2008-08-22

Authors:

LIU, GAOHUA; WANG, HUANG; FOOTE, ERICA; JIANG, MEI; XIAO, RONG; SWAPNA, G.V.T; NAIR, RAJESH; EVERETT, JOHN; ACTON, THOMAS; ROST, BURKHARD; Montelione, Gaetano

Citation:

Citation: LIU, GAOHUA; XIAO, RONG; Montelione, Gaetano. "NMR CHEMICAL SHIFT ASSIGNMENTS OF IRON(II) TRANSPORT PROTEIN A FROM CLOSTRIDIUM THERMOCELLUM , NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG) TARGET VR131" .

Assembly members:

Assembly members:
IRON(II) TRANSPORT PROTEIN A, polymer, 324 residues, 36536.531 Da.

Natural source:

Natural source: Common Name: Clostridium thermocellum Taxonomy ID: 1515 Superkingdom: Bacteria Kingdom: not available Genus/species: Clostridium thermocellum

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
IRON(II) TRANSPORT PROTEIN A: MKLSRLVPGVPARIKRLEVS GELHEKLVGMGFVPGEEIEI VQVAPLGDPIVCKIGNRNIT LRKREADLIEVEVVGGELPL ILADDGTYEITKLNGGRRFL FRMKNLGIESGKKIQVSGRR YYIEGREIDLGYGEATKIWV RRVSDAGEESHPQKLEHHHH HHMKLSRLVPGVPARIKRLE VSGELHEKLVGMGFVPGEEI EIVQVAPLGDPIVCKIGNRN ITLRKREADLIEVEVVGGEL PLILADDGTYEITKLNGGRR FLFRMKNLGIESGKKIQVSG RRYYIEGREIDLGYGEATKI WVRRVSDAGEESHPQKLEHH HHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	547
15N chemical shifts	164
1H chemical shifts	1168

Time Domain Data

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	IRON(II) TRANSPORT PROTEIN A	1

Entities:

Entity 1, IRON(II) TRANSPORT PROTEIN A 324 residues - 36536.531 Da.

1

MET

LYS

LEU

SER

ARG

LEU

VAL

PRO

GLY

VAL

2

PRO

ALA

ARG

ILE

LYS

ARG

LEU

GLU

VAL

SER

3

GLY

GLU

LEU

HIS

GLU

LYS

LEU

VAL

GLY

MET

4

GLY

PHE

VAL

PRO

GLY

GLU

ILE

GLU

ILE

5

VAL

GLN

VAL

ALA

PRO

LEU

GLY

ASP

PRO

ILE

6

VAL

CYS

LYS

ILE

GLY

ASN

ARG

ASN

ILE

THR

7

LEU

ARG

LYS

ARG

GLU

ALA

ASP

LEU

ILE

GLU

8

VAL

GLU

VAL

GLY

GLU

LEU

PRO

LEU

9

ILE

LEU

ALA

ASP

GLY

THR

TYR

GLU

ILE

10

THR

LYS

LEU

ASN

GLY

ARG

PHE

LEU

11

PHE

ARG

MET

LYS

ASN

LEU

GLY

ILE

GLU

SER

12

GLY

LYS

ILE

GLN

VAL

SER

GLY

ARG

13

TYR

ILE

GLU

GLY

ARG

GLU

ILE

ASP

LEU

14

GLY

TYR

GLY

GLU

ALA

THR

LYS

ILE

TRP

VAL

15

ARG

VAL

SER

ASP

ALA

GLY

GLU

SER

16

HIS

PRO

GLN

LYS

LEU

GLU

HIS

17

HIS

MET

LYS

LEU

SER

ARG

LEU

VAL

PRO

18

GLY

VAL

PRO

ALA

ARG

ILE

LYS

ARG

LEU

GLU

19

VAL

SER

GLY

GLU

LEU

HIS

GLU

LYS

LEU

VAL

20

GLY

MET

GLY

PHE

VAL

PRO

GLY

GLU

ILE

21

GLU

ILE

VAL

GLN

VAL

ALA

PRO

LEU

GLY

ASP

22

PRO

ILE

VAL

CYS

LYS

ILE

GLY

ASN

ARG

ASN

23

ILE

THR

LEU

ARG

LYS

ARG

GLU

ALA

ASP

LEU

24

ILE

GLU

VAL

GLU

VAL

GLY

GLU

LEU

25

PRO

LEU

ILE

LEU

ALA

ASP

GLY

THR

TYR

26

GLU

ILE

THR

LYS

LEU

ASN

GLY

ARG

27

PHE

LEU

PHE

ARG

MET

LYS

ASN

LEU

GLY

ILE

28

GLU

SER

GLY

LYS

ILE

GLN

VAL

SER

GLY

29

ARG

TYR

ILE

GLU

GLY

ARG

GLU

ILE

30

ASP

LEU

GLY

TYR

GLY

GLU

ALA

THR

LYS

ILE

31

TRP

VAL

ARG

VAL

SER

ASP

ALA

GLY

GLU

32

GLU

SER

HIS

PRO

GLN

LYS

LEU

GLU

HIS

33

HIS

Samples:

sample_1: entity, [U-100% 13C; U-100% 15N], 0.92 mM; H2O 90%; D2O, [U-100% 2H], 10%

sample_12: entity, [U-10% 13C; U-100% 15N], 0.65 mM; H2O 90%; D2O, [U-100% 2H], 10%

sample_conditions_1: 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 1H-13C NOESY (aliph)	sample_1	isotropic	sample_conditions_1
3D SIMULTANEOUS CN-NOESY	sample_1	isotropic	sample_conditions_1
4,3D GFT CABCACONHN	sample_1	isotropic	sample_conditions_1
4,3D GFT HNNCABCA	sample_1	isotropic	sample_conditions_1
4,3D GFT HABCABCONHN	sample_1	isotropic	sample_conditions_1
3D CCH-COSY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_12	isotropic	sample_conditions_1
3D 1H-13C NOESY (arom)	sample_1	isotropic	sample_conditions_1

Software:

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

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

AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - data analysis

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

XEASY v1.3.1, Bartels et al. - data analysis

NMRPipe v2.3, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

TOPSPIN, Bruker Biospin - collection

VNMRJ, Varian - collection

NMR spectrometers:

Bruker Avance 800 MHz
Varian INOVA 600 MHz