BMRB Entry 6189

Name: Solution structure of SEP domain from human p47
Published: 2004-11-08

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PDB ID: 1ss6
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR6189
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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution structure of SEP domain from human p47

Deposition date:

2004-04-22

Original release date:

2004-11-08

Authors:

Soukenik, M.; Leidert, M.; Sievert, V.; Buessow, K.; Leitner, D.; Labudde, D.; Ball, L.; Oschkinat, H.

Citation:

Citation: Soukenik, M.; Diehl, A.; Leidert, M.; Sievert, V.; Bussow, K.; Leitner, D.; Labudde, D.; Ball, L.; Lechner, A.; Nagler, D.; Oschkinat, H.. "The SEP domain of p47 acts as a reversible competitive inhibitor of cathepsin L" FEBS Lett. 576, 358-362 (2004).
PubMed: 15498563

Assembly members:

Assembly members:
NSFL1 cofactor p47, polymer, 102 residues, Formula weight is not available

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
NSFL1 cofactor p47: GSEKRQHSSQDVHVVLKLWK SGFSLDNGELRSYQDPSNAQ FLESIRRGEVPAELRRLAHG GQVNLDMEDHRDEDFVKPKG AFKAFTGEGQKLGSTAPQVL ST

Data sets:

assigned_chemical_shifts
- chemical_shift_set_1

Data type	Count
1H chemical shifts	609
13C chemical shifts	311
15N chemical shifts	106

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	NSFL1 cofactor p47	1

Entities:

Entity 1, NSFL1 cofactor p47 102 residues - Formula weight is not available

1

GLY

SER

GLU

LYS

ARG

GLN

HIS

SER

GLN

2

ASP

VAL

HIS

VAL

LEU

LYS

LEU

TRP

LYS

3

SER

GLY

PHE

SER

LEU

ASP

ASN

GLY

GLU

LEU

4

ARG

SER

TYR

GLN

ASP

PRO

SER

ASN

ALA

GLN

5

PHE

LEU

GLU

SER

ILE

ARG

GLY

GLU

VAL

6

PRO

ALA

GLU

LEU

ARG

LEU

ALA

HIS

GLY

7

GLY

GLN

VAL

ASN

LEU

ASP

MET

GLU

ASP

HIS

8

ARG

ASP

GLU

ASP

PHE

VAL

LYS

PRO

LYS

GLY

9

ALA

PHE

LYS

ALA

PHE

THR

GLY

GLU

GLY

GLN

10

LYS

LEU

GLY

SER

THR

ALA

PRO

GLN

VAL

LEU

11

SER

THR

Samples:

sample_1: NSFL1 cofactor p47, [U-15N], 2 mM; phosphate buffer 20 mM; sodium chloride 100 mM; H2O 90%; D2O 10%

sample_2: NSFL1 cofactor p47, [U-15N; U-13C], 1 mM; phosphate buffer 20 mM; sodium chloride 100 mM; H2O 90%; D2O 10%

sample_3: NSFL1 cofactor p47, [U-15N; U-13C], 1 mM; phosphate buffer 20 mM; sodium chloride 100 mM; D2O 100%

sample_cond_1: pH: 5.6; temperature: 300 K; ionic strength: 120 mM; pressure: 1 atm

Experiments:

Name	Sample	Sample state	Sample conditions
2D NOESY	not available	not available	sample_cond_1
3D 15N-separated NOESY	not available	not available	sample_cond_1
3D 13C-separated NOESY	not available	not available	sample_cond_1

Software:

XWINNMR v3.5, Bruker - processing

Paste-Papst v1.4, Labudde,D., Leitner,D. - collection

Platon v2.0, Labudde,D., Leitner,D. -

Sparky v3.1 - data analysis

Aria-CNS v1.2, Nilges. M. - structure solution, refinement

NMR spectrometers:

Bruker DRX 600 MHz

PDB	1SS6
DBJ	BAA91731 BAD97054 BAD97061 BAE88340 BAG37821
EMBL	CAH90897
GB	AAD44488 AAH02801 AAP97139 ABM84115 ABM87512
REF	NP_001125510 NP_001193665 NP_001253592 NP_057227 NP_061327
SP	Q5RBG3 Q9UNZ2
AlphaFold	Q5RBG3 Q9UNZ2