BMRB Entry 17389

Name: Solution NMR Structure of the serine-rich domain of hEF1( Enhancer of filamentation 1) from homo sapiens, Northeast Structural Genomics Consortium Target HR5554A
Published: 2011-01-31

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PDB ID: 2l81
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17389
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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 serine-rich domain of hEF1( Enhancer of filamentation 1) from homo sapiens, Northeast Structural Genomics Consortium Target HR5554A

Deposition date:

2010-12-31

Original release date:

2011-01-31

Authors:

Liu, Gaohua; Xiao, Rong; Huang, Yuanpeng; Patel, Daya; Ciccosanti, Colleen; Acton, Thomas; Tong, Saichu; Everett, John; Montelione, Gaetano

Citation:

Citation: Liu, Gaohua; Xiao, Rong; Huang, Yuanpeng; Patel, Daya; Ciccosanti, Colleen; Tong, Saichu; Acton, Thomas; Everett, John; Montelione, Gaetano. "Northeast Structural Genomics Consortium Target HR5554A" To be published ., .-..

Assembly members:

Assembly members:
HR5554A, polymer, 176 residues, 20238.305 Da.

Natural source:

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

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET 14-15C

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HR5554A: MGHHHHHHSHMDKRLFLDPD TAIERLQRLQQALEMGVSSL MALVTTDWRCYGYMERHINE IRTAVDKVELFLKEYLHFVK GAVANAACLPELILHNKMKR ELQRVEDSHQILSQTSHDLN ECSWSLNILAINKPQNKCDD LDRFVMVAKTVPDDAKQLTT TINTNAEALFRPGPGS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	569
15N chemical shifts	162
1H chemical shifts	1181

Time Domain Data

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	HR5554A	1

Entities:

Entity 1, HR5554A 176 residues - 20238.305 Da.

1

MET

GLY

HIS

SER

HIS

2

MET

ASP

LYS

ARG

LEU

PHE

LEU

ASP

PRO

ASP

3

THR

ALA

ILE

GLU

ARG

LEU

GLN

ARG

LEU

GLN

4

GLN

ALA

LEU

GLU

MET

GLY

VAL

SER

LEU

5

MET

ALA

LEU

VAL

THR

ASP

TRP

ARG

CYS

6

TYR

GLY

TYR

MET

GLU

ARG

HIS

ILE

ASN

GLU

7

ILE

ARG

THR

ALA

VAL

ASP

LYS

VAL

GLU

LEU

8

PHE

LEU

LYS

GLU

TYR

LEU

HIS

PHE

VAL

LYS

9

GLY

ALA

VAL

ALA

ASN

ALA

CYS

LEU

PRO

10

GLU

LEU

ILE

LEU

HIS

ASN

LYS

MET

LYS

ARG

11

GLU

LEU

GLN

ARG

VAL

GLU

ASP

SER

HIS

GLN

12

ILE

LEU

SER

GLN

THR

SER

HIS

ASP

LEU

ASN

13

GLU

CYS

SER

TRP

SER

LEU

ASN

ILE

LEU

ALA

14

ILE

ASN

LYS

PRO

GLN

ASN

LYS

CYS

ASP

15

LEU

ASP

ARG

PHE

VAL

MET

VAL

ALA

LYS

THR

16

VAL

PRO

ASP

ALA

LYS

GLN

LEU

THR

17

THR

ILE

ASN

THR

ASN

ALA

GLU

ALA

LEU

PHE

18

ARG

PRO

GLY

PRO

GLY

SER

Samples:

sample_NC: HR5554A, [U-100% 13C; U-100% 15N], 0.56 mM; H2O 95 mM; D2O 5 mM

sample_NC5: HR5554A, [U-5% 13C; U-100% 15N], 0.56 mM; H2O 95 mM; D2O 5 mM

sample_conditions_1: pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_NC	isotropic	sample_conditions_1
2D 1H-13C HSQC 28 ct	sample_NC	isotropic	sample_conditions_1
3D HNCO	sample_NC	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_NC	isotropic	sample_conditions_1
3D HNCACB	sample_NC	isotropic	sample_conditions_1
3D 1H-13C arom NOESY	sample_NC	isotropic	sample_conditions_1
3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESY	sample_NC	isotropic	sample_conditions_1
2D 1H-13C HSQC 28a ct	sample_NC	isotropic	sample_conditions_1
2D 1H-13C HSQC 42 ct	sample_NC	isotropic	sample_conditions_1
2D 1H-13C HSQC 42a ct	sample_NC	isotropic	sample_conditions_1
3D CC(CO)NH TOCSY	sample_NC	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_NC	isotropic	sample_conditions_1
3D HNCA	sample_NC	isotropic	sample_conditions_1
3D HN(CO)CA	sample_NC	isotropic	sample_conditions_1
3D (H)CCH TOCSY	sample_NC	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_NC	isotropic	sample_conditions_1
2D 1H-15N HSQC T1	sample_NC	isotropic	sample_conditions_1
2D 1H-15N HSQC T2	sample_NC	isotropic	sample_conditions_1

Software:

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

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

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

AutoAssign v2.1, Zimmerman, Moseley, Kulikowski and Montelione - data analysis,chemical shift assignment

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

XEASY, Bartels et al. - data analysis,peak picking,chemical shift assignment

TOPSPIN, Bruker Biospin - collection

VNMRJ, Varian - collection

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

NMR spectrometers:

Bruker Avance 800 MHz
Varian INOVA 600 MHz

PDB	2L81
DBJ	BAF85371 BAI46717
GB	AAA98770 AAB53696 AAH40207 ABM82651 ABM85828
REF	NP_001135865 NP_001257962 NP_006394 XP_001088846 XP_001089291
SP	Q14511
AlphaFold	Q14511