BMRB Entry 18166

Name: Solution NMR Structure of Stress-induced-phosphoprotein 1 STI1 from Homo sapiens, Northeast Structural Genomics Consortium Target HR4403E
Published: 2012-02-17

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PDB ID: 2lni
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18166
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution NMR Structure of Stress-induced-phosphoprotein 1 STI1 from Homo sapiens, Northeast Structural Genomics Consortium Target HR4403E

Deposition date:

2011-12-28

Original release date:

2012-02-17

Authors:

Tang, Yuefeng; Liu, Gaohua; Hamilton, Keith; Ciccosanti, Colleen; Shastry, Ritu; Rost, Burkhard; Acton, Tom; Xiao, Rong; Everett, John; Montelione, Gaetano

Citation:

Citation: Tang, Yuefeng; Liu, Gaohua; Hamilton, Keith; Ciccosanti, Colleen; Shastry, Ritu; Rost, Burkhard; Acton, Tom; Xiao, Rong; Everett, John; Montelione, Gaetano. "Northeast Structural Genomics Consortium Target HR4403E" To be published ., .-..

Assembly members:

Assembly members:
HR4403E, polymer, 133 residues, 15365.743 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: HR4403E-356-477-14.2

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HR4403E: MGHHHHHHSHMNPDLALMVK NKGNECFQKGDYPQAMKHYT EAIKRNPKDAKLYSNRAACY TKLLEFQLALKDCEECIQLE PTFIKGYTRKAAALEAMKDY TKAMDVYQKALDLDSSCKEA ADGYQRCMMAQYN

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	434
15N chemical shifts	141
1H chemical shifts	909

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	HR4403E	1

Entities:

Entity 1, HR4403E 133 residues - 15365.743 Da.

1

MET

GLY

HIS

SER

HIS

2

MET

ASN

PRO

ASP

LEU

ALA

LEU

MET

VAL

LYS

3

ASN

LYS

GLY

ASN

GLU

CYS

PHE

GLN

LYS

GLY

4

ASP

TYR

PRO

GLN

ALA

MET

LYS

HIS

TYR

THR

5

GLU

ALA

ILE

LYS

ARG

ASN

PRO

LYS

ASP

ALA

6

LYS

LEU

TYR

SER

ASN

ARG

ALA

CYS

TYR

7

THR

LYS

LEU

GLU

PHE

GLN

LEU

ALA

LEU

8

LYS

ASP

CYS

GLU

CYS

ILE

GLN

LEU

GLU

9

PRO

THR

PHE

ILE

LYS

GLY

TYR

THR

ARG

LYS

10

ALA

LEU

GLU

ALA

MET

LYS

ASP

TYR

11

THR

LYS

ALA

MET

ASP

VAL

TYR

GLN

LYS

ALA

12

LEU

ASP

LEU

ASP

SER

CYS

LYS

GLU

ALA

13

ALA

ASP

GLY

TYR

GLN

ARG

CYS

MET

ALA

14

GLN

TYR

ASN

Samples:

sample_1: HR4403E, [U-100% 13C; U-100% 15N], 0.807 mM; H2O 95%; D2O 5%

sample_2: HR4403E, [U-5% 13C; U-100% 15N], 0.763 mM; H2O 95%; D2O 5%

sample_3: HR4403E, [U-100% 13C; U-100% 15N], 0.4 mM; D2O 100%

sample_conditions_1: pH: 4.5; pressure: 1 atm; temperature: 293 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D 1H-13C arom NOESY	sample_1	isotropic	sample_conditions_1
3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_3	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HCCH-COSY	sample_1	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

PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

SPARKY, Goddard - data analysis

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

PALES, PALES (Zweckstetter, Bax) - geometry optimization

REDCAT, Valafar, Prestegard - geometry optimization

PSVS, Bhattacharya, Montelione - structure validation

NMR spectrometers:

Bruker Avance 800 MHz