BMRB Entry 17265

Name: NMR structure of fusion of CtIP (641-685) to LMO4-LIM1 (18-82)
Published: 2011-06-07

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PDB ID: 2l4z
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17265
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: NMR structure of fusion of CtIP (641-685) to LMO4-LIM1 (18-82) PubMed: 21643835

Deposition date: 2010-10-24 Original release date: 2011-06-07

Authors: Liew, Chu Wai; Stokes, Philippa; Kwan, Ann; Matthews, Jacqui

Citation: Liew, Chu Wai; Kwan, Ann; Stokes, Philippa; Mackay, Joel; Matthews, Jacqueline. "(1)H, (15)N and (13)C assignments of an intramolecular LMO4-LIM1/CtIP complex." Biomol. NMR Assignments 6, 31-34 (2012).

Assembly members:
Fusion_protein, polymer, 123 residues, 13075.729 Da.
ZN, non-polymer, 65.409 Da.

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pGEX-2T

Entity Sequences (FASTA):
Fusion_protein: GSSLQNNQDVSFENIQWSID PGADLSQYKMDVTVIDTKDG SQSKLGGGGSGGHMGSGGLS WKRCAGCGGKIADRFLLYAM DSYWHSRCLKCSSCQAQLGD IGTSSYTKSGMILCRNDYIR LFG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	429
15N chemical shifts	128
1H chemical shifts	758

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Fusion_protein	1
2	ZINC ION_1	2
3	ZINC ION_2	2

Entities:

Entity 1, Fusion_protein 123 residues - 13075.729 Da.

Initial GS from protease site not included in deposited NMR structure. LMO4 C52S/C64S mutations.

1

GLY

SER

LEU

GLN

ASN

GLN

ASP

VAL

2

SER

PHE

GLU

ASN

ILE

GLN

TRP

SER

ILE

ASP

3

PRO

GLY

ALA

ASP

LEU

SER

GLN

TYR

LYS

MET

4

ASP

VAL

THR

VAL

ILE

ASP

THR

LYS

ASP

GLY

5

SER

GLN

SER

LYS

LEU

GLY

SER

6

GLY

HIS

MET

GLY

SER

GLY

LEU

SER

7

TRP

LYS

ARG

CYS

ALA

GLY

CYS

GLY

LYS

8

ILE

ALA

ASP

ARG

PHE

LEU

TYR

ALA

MET

9

ASP

SER

TYR

TRP

HIS

SER

ARG

CYS

LEU

LYS

10

CYS

SER

CYS

GLN

ALA

GLN

LEU

GLY

ASP

11

ILE

GLY

THR

SER

TYR

THR

LYS

SER

GLY

12

MET

ILE

LEU

CYS

ARG

ASN

ASP

TYR

ILE

ARG

13

LEU

PHE

GLY

Entity 2, ZINC ION_1 - Zn - 65.409 Da.

1

ZN

Samples:

sample_1: Fusion protein, [U-15N], 150 uM; sodium phosphate 20 mM; sodium chloride 150 mM; DTT 1 mM; H2O 90%; D2O 10%

sample_2: Fusion protein, [U-99% 13C; U-99% 15N], 500 uM; sodium phosphate 20 mM; sodium chloride 150 mM; DTT 1 mM; H2O 90%; D2O 10%

sample_3: Fusion protein, [U-99% 13C; U-99% 15N], 300 uM; sodium phosphate 20 mM; sodium chloride 150 mM; DTT 1 mM; D2O 10%

sample_4: Fusion protein 500 uM; sodium phosphate 20 mM; sodium chloride 150 mM; DTT 1 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 150 mM; pH: 6; pressure: 1 atm; temperature: 291 K

sample_conditions_2: ionic strength: 150 mM; pH: 6; pressure: 1 atm; temperature: 281 K

sample_conditions_3: ionic strength: 150 mM; pH: 6; pressure: 1 atm; temperature: 303 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1
3D HNHA	sample_2	isotropic	sample_conditions_1
3D C(CO)NH	sample_2	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_3	isotropic	sample_conditions_1
3D CCH-TOCSY	sample_3	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_3	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_4	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_4	isotropic	sample_conditions_1

Software:

TOPSPIN v1.1-2.1, Bruker - collection

SPARKY v3.114, Goddard - data analysis

ARIA v1.2, Linge, O'Donoghue and Nilges - structure solution

TALOS, Cornilescu, Delaglio and Bax - data analysis

NMR spectrometers:

Bruker DRX 600 MHz
Bruker Avance 800 MHz

Biological Magnetic Resonance Data Bank