BMRB Entry 15541

Name: NMR study of the interaction of HscB with apo-IscU
Published: 2008-08-18

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR15541

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

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Title:

NMR study of the interaction of HscB with apo-IscU

Deposition date:

2007-10-31

Original release date:

2008-08-18

Authors:

Fuezery, Anna; Tonelli, Marco; Ta, Dennis; Cornilescu, Gabriel; Vickery, Larry; Markley, John

Citation:

Citation: Fuezery, Anna; Tonelli, Marco; Ta, Dennis; Cornilescu, Gabriel; Vickery, Larry; Markley, John. "Solution Structure of the Iron-Sulfur Cluster Cochaperone HscB and Its Binding Surface for the Iron-Sulfur Assembly Scaffold Protein IscU" Biochemistry 47, 9394-9404 (2008).
PubMed: 18702525

Assembly members:

Assembly members:
HscB, polymer, 171 residues, 20137 Da.
IscU, polymer, 127 residues, Formula weight is not available

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: pTrcIscU

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HscB: MDYFTLFGLPARYQLDTQAL SLRFQDLQRQYHPDKFASGS QAEQLAAVQQSATINQAWQT LRHPLMRAEYLLSLHGFDLA SEQHTVRDTAFLMEQLELRE ELDEIEQAKDEARLESFIKR VKKMFDTRHQLMVEQLDNET WDAAADTVRKLRFLDKLRSS AEQLEEKLLDF
IscU: AYSEKVIDHYENPRNVGSFD NNDENVGSGMVGAPACGDVM KLQIKVNDEGIIEDARFKTY GCGSAIASSSLVTEWVKGKS LDEAQAIKNTDIAEELELPP VKIHCSILAEDAIKAAIADY KSKREAK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
- assigned_chem_shift_list_2
heteronucl_NOEs
- heteronuclear_noe_list_1
- heteronuclear_noe_list_2
heteronucl_T1_relaxation
- heteronuclear_T1_list_1
- heteronuclear_T1_list_2
heteronucl_T2_relaxation
- heteronuclear_T2_list_1
- heteronuclear_T2_list_2
RDCs
- RDC_list_1
- RDC_list_2

Data type	Count
13C chemical shifts	469
15N chemical shifts	276
1H chemical shifts	698
heteronuclear NOE values	229
residual dipolar couplings	274
T1 relaxation values	228
T2 relaxation values	228

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	IscU	2
2	HscB	1

Entities:

Entity 2, IscU 127 residues - Formula weight is not available

1

ALA

TYR

SER

GLU

LYS

VAL

ILE

ASP

HIS

TYR

2

GLU

ASN

PRO

ARG

ASN

VAL

GLY

SER

PHE

ASP

3

ASN

ASP

GLU

ASN

VAL

GLY

SER

GLY

MET

4

VAL

GLY

ALA

PRO

ALA

CYS

GLY

ASP

VAL

MET

5

LYS

LEU

GLN

ILE

LYS

VAL

ASN

ASP

GLU

GLY

6

ILE

GLU

ASP

ALA

ARG

PHE

LYS

THR

TYR

7

GLY

CYS

GLY

SER

ALA

ILE

ALA

SER

8

LEU

VAL

THR

GLU

TRP

VAL

LYS

GLY

LYS

SER

9

LEU

ASP

GLU

ALA

GLN

ALA

ILE

LYS

ASN

THR

10

ASP

ILE

ALA

GLU

LEU

GLU

LEU

PRO

11

VAL

LYS

ILE

HIS

CYS

SER

ILE

LEU

ALA

GLU

12

ASP

ALA

ILE

LYS

ALA

ILE

ALA

ASP

TYR

13

LYS

SER

LYS

ARG

GLU

ALA

LYS

Entity 1, HscB 171 residues - 20137 Da.

1

MET

ASP

TYR

PHE

THR

LEU

PHE

GLY

LEU

PRO

2

ALA

ARG

TYR

GLN

LEU

ASP

THR

GLN

ALA

LEU

3

SER

LEU

ARG

PHE

GLN

ASP

LEU

GLN

ARG

GLN

4

TYR

HIS

PRO

ASP

LYS

PHE

ALA

SER

GLY

SER

5

GLN

ALA

GLU

GLN

LEU

ALA

VAL

GLN

6

SER

ALA

THR

ILE

ASN

GLN

ALA

TRP

GLN

THR

7

LEU

ARG

HIS

PRO

LEU

MET

ARG

ALA

GLU

TYR

8

LEU

SER

LEU

HIS

GLY

PHE

ASP

LEU

ALA

9

SER

GLU

GLN

HIS

THR

VAL

ARG

ASP

THR

ALA

10

PHE

LEU

MET

GLU

GLN

LEU

GLU

LEU

ARG

GLU

11

GLU

LEU

ASP

GLU

ILE

GLU

GLN

ALA

LYS

ASP

12

GLU

ALA

ARG

LEU

GLU

SER

PHE

ILE

LYS

ARG

13

VAL

LYS

MET

PHE

ASP

THR

ARG

HIS

GLN

14

LEU

MET

VAL

GLU

GLN

LEU

ASP

ASN

GLU

THR

15

TRP

ASP

ALA

ASP

THR

VAL

ARG

LYS

16

LEU

ARG

PHE

LEU

ASP

LYS

LEU

ARG

SER

17

ALA

GLU

GLN

LEU

GLU

LYS

LEU

ASP

18

PHE

Name	Sample	Sample state	Sample conditions
2D 1H-15N TROSY	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D TROSY-HNCO	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	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
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_5	isotropic	sample_conditions_1
3D HN-coupled HNCO	sample_2	isotropic	sample_conditions_1
3D HN-coupled HNCO	sample_3	anisotropic	sample_conditions_1
3D HA-coupled HN(CO)CA	sample_2	isotropic	sample_conditions_1
3D HA-coupled HN(CO)CA	sample_3	anisotropic	sample_conditions_1
2D 1H-15N HSQC	sample_4	isotropic	sample_conditions_1

PDB	1FPO 2KQK 2L4X 3LVL
DBJ	BAA16421 BAB36816 BAG78337 BAI26772 BAI31801 BAA16423 BAB36818 BAG78339 BAH64655 BAI26774
EMBL	CAP76979 CAQ32900 CAQ88189 CAQ99418 CAR03969 CAD02745 CAP76981 CAQ32902 CAQ88187 CAQ99420
GB	AAA18299 AAC75580 AAG57641 AAN44073 AAN81502 AAC75582 AAG57643 AAL21436 AAN44075 AAN81505
PIR	E85897 AE0824
REF	NP_311420 NP_417022 NP_708366 WP_000384389 WP_000384404 NP_289086 NP_311422 NP_417024 NP_457073 NP_461477
SP	A1AE64 A7ZPX0 A8A333 B1IWD4 B1LNI2 P0ACD4 P0ACD5 P0ACD6 P0ACD7
BMRB	15967 16245 16603 17282 17836 17837 17844 18359 18360 18361 18362 18381 18750 18754 7432
AlphaFold	A1AE64 A7ZPX0 A8A333 B1IWD4 B1LNI2 P0ACD4 P0ACD5 P0ACD6 P0ACD7

BMRB Entry 15541

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

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