BMRB Entry 15922

Name: Solution structure of the PPIL1 bound to a fragment of SKIP
Published: 2010-01-11

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PDB ID: 2k7n
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15922
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Solution structure of the PPIL1 bound to a fragment of SKIP PubMed: 20007319

Deposition date: 2008-08-17 Original release date: 2010-01-11

Authors: Wang, Xingsheng; Wu, Jihui; Shi, Yunyu

Citation: Wang, Xingsheng; Zhang, Shaojie; Zhang, Jiahai; Huang, Xiaojuan; Xu, Chao; Wang, Weiwei; Liu, Zhijun; Wu, Jihui; Shi, Yunyu. "A large intrinsically disordered region in SKIP and its disorder-order transition induced by PPIL1 binding revealed by NMR." J. Biol. Chem. 285, 4951-4963 (2010).

Assembly members:
PPIL1/SKIP, polymer, 203 residues, Formula weight is not available

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

Entity Sequences (FASTA):
PPIL1/SKIP: MAAIPPDSWQPPNVYLETSM GIIVLELYWKHAPKTCKNFA ELARRGYYNGTKFHRIIKDF MIQGGDPTGTGRGGASIYGK QFEDELHPDLKFTGAGILAM ANAGPDTNGSQFFVTLAPTQ WLDGKHTIFGRVCQGIGMVN RVGMVETNSQDRPVDDVKII KAYPSGGGGSGGGSGGGSGG GSGDGGAFPEIHVAQYPLDM GRK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	519
15N chemical shifts	186
1H chemical shifts	1176

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	PPIL1/SKIP	1

Entities:

Entity 1, PPIL1/SKIP 203 residues - Formula weight is not available

1

MET

ALA

ILE

PRO

ASP

SER

TRP

GLN

2

PRO

ASN

VAL

TYR

LEU

GLU

THR

SER

MET

3

GLY

ILE

VAL

LEU

GLU

LEU

TYR

TRP

LYS

4

HIS

ALA

PRO

LYS

THR

CYS

LYS

ASN

PHE

ALA

5

GLU

LEU

ALA

ARG

GLY

TYR

ASN

GLY

6

THR

LYS

PHE

HIS

ARG

ILE

LYS

ASP

PHE

7

MET

ILE

GLN

GLY

ASP

PRO

THR

GLY

THR

8

GLY

ARG

GLY

ALA

SER

ILE

TYR

GLY

LYS

9

GLN

PHE

GLU

ASP

GLU

LEU

HIS

PRO

ASP

LEU

10

LYS

PHE

THR

GLY

ALA

GLY

ILE

LEU

ALA

MET

11

ALA

ASN

ALA

GLY

PRO

ASP

THR

ASN

GLY

SER

12

GLN

PHE

VAL

THR

LEU

ALA

PRO

THR

GLN

13

TRP

LEU

ASP

GLY

LYS

HIS

THR

ILE

PHE

GLY

14

ARG

VAL

CYS

GLN

GLY

ILE

GLY

MET

VAL

ASN

15

ARG

VAL

GLY

MET

VAL

GLU

THR

ASN

SER

GLN

16

ASP

ARG

PRO

VAL

ASP

VAL

LYS

ILE

17

LYS

ALA

TYR

PRO

SER

GLY

SER

18

GLY

SER

GLY

SER

GLY

19

GLY

SER

GLY

ASP

GLY

ALA

PHE

PRO

GLU

20

ILE

HIS

VAL

ALA

GLN

TYR

PRO

LEU

ASP

MET

21

GLY

ARG

LYS

Samples:

sample: D2O 100%; entity_2; phosphate buffer 50 mM; NaCl 50 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D_15N-separated_NOESY	sample	isotropic	sample_conditions_1
3D_13C-separated_NOES	sample	isotropic	sample_conditions_1

Software:

CNS, Brunger A. T. et.al. - refinement

NMR spectrometers:

Bruker DMX 600 MHz

PDB	1XWN 2K7N 2X7K
DBJ	BAB23265 BAE00661 BAE29731 BAE30513 BAE33862
GB	AAD34119 AAH03048 AAH58369 AAH99188 AAI02397
REF	NP_001014869 NP_001029360 NP_001233365 NP_001271748 NP_057143
SP	Q5E992 Q9D0W5 Q9Y3C6
TPG	DAA16620

Biological Magnetic Resonance Data Bank