BMRB Entry 19749

Name: Solution NMR structure of N-terminal domain (SH2 domain) of human Inositol polyphosphate phosphatase-like protein 1 (INPPL1) (fragment 20-117), Northeast Structural Genomics Consortium Target HR9134A.
Published: 2014-03-03

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PDB ID: 2mk2
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19749
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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution NMR structure of N-terminal domain (SH2 domain) of human Inositol polyphosphate phosphatase-like protein 1 (INPPL1) (fragment 20-117), Northeast Structural Genomics Consortium Target HR9134A.

Deposition date:

2014-01-23

Original release date:

2014-03-03

Authors:

Yang, Yunhuang; Ramelot, Theresa; Janjua, Haleema; Xiao, Rong; Everett, John; Montelione, Gaetano; Kennedy, Michael

Citation:

Citation: Yang, Yunhuang; Ramelot, Theresa; Janjua, Haleema; Xiao, Rong; Everett, John; Montelione, Gaetano; Kennedy, Michael. "Solution NMR structure of N-terminal domain (SH2 domain) of human Inositol polyphosphate phosphatase-like protein 1 (INPPL1) (fragment 20-117), Northeast Structural Genomics Consortium Target HR9134A." To be published ., .-..

Assembly members:

Assembly members:
HR9134A, polymer, 109 residues, 12198.978 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: HR9134A-20-117-15.4

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HR9134A: MGHHHHHHSHMSWYHRDLSR AAAEELLARAGRDGSFLVRD SESVAGAFALCVLYQKHVHT YRILPDGEDFLAVQTSQGVP VRRFQTLGELIGLYAQPNQG LVCALLLPV

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	427
15N chemical shifts	112
1H chemical shifts	704

Time Domain Data

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	HR9134A	1

Entities:

Entity 1, HR9134A 109 residues - 12198.978 Da.

1

MET

GLY

HIS

SER

HIS

2

MET

SER

TRP

TYR

HIS

ARG

ASP

LEU

SER

ARG

3

ALA

GLU

LEU

ALA

ARG

ALA

4

GLY

ARG

ASP

GLY

SER

PHE

LEU

VAL

ARG

ASP

5

SER

GLU

SER

VAL

ALA

GLY

ALA

PHE

ALA

LEU

6

CYS

VAL

LEU

TYR

GLN

LYS

HIS

VAL

HIS

THR

7

TYR

ARG

ILE

LEU

PRO

ASP

GLY

GLU

ASP

PHE

8

LEU

ALA

VAL

GLN

THR

SER

GLN

GLY

VAL

PRO

9

VAL

ARG

PHE

GLN

THR

LEU

GLY

GLU

LEU

10

ILE

GLY

LEU

TYR

ALA

GLN

PRO

ASN

GLN

GLY

11

LEU

VAL

CYS

ALA

LEU

PRO

VAL

Samples:

sample_1: HR9134A, [U-100% 13C; U-100% 15N], 0.58 mM; H2O 90%; D2O 10%

sample_2: HR9134A, [U-100% 13C; U-100% 15N], 0.58 mM; D2O 100%

sample_3: HR9134A, [U-5% 13C; U-100% 15N], 1.05 mM; H2O 90%; D2O 10%

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

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_3	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_3	isotropic	sample_conditions_1
3D HNCO	sample_3	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_3	isotropic	sample_conditions_1
3D HNCACB	sample_3	isotropic	sample_conditions_1
3D 1H-13C arom NOESY	sample_3	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_3	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_3	isotropic	sample_conditions_1
3D HN(CO)CA	sample_3	isotropic	sample_conditions_1
3D HNCA	sample_3	isotropic	sample_conditions_1
2D 1H-15N HSQC NH2 only	sample_3	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_3	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_3	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_3	isotropic	sample_conditions_1
3D HCCH-COSY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_1
2D 1H-15N HSQC histidine	sample_3	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

AutoStructure 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 850 MHz
Varian INOVA 600 MHz

PDB	2MK2
DBJ	BAA81818 BAA82308
EMBL	CAA74743
GB	AAF28187 AAH63080 AAI40854 ADG23056 EAW74854
REF	NP_001116211 NP_001177208 NP_001178105 NP_001247768 NP_001257772
SP	O15357 Q6P549 Q9WVR3
TPG	DAA21965
AlphaFold	O15357 Q6P549 Q9WVR3