BMRB Entry 34395

Name: Solution structure and 1H, 13C and 15N chemical shift assignments for the complex of NECAP1 PHear domain with phosphorylated AP2 mu2 148-163
Published: 2019-10-22

Click here to enlarge.

PDB ID: 6rh6
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34395
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

Solution structure and 1H, 13C and 15N chemical shift assignments for the complex of NECAP1 PHear domain with phosphorylated AP2 mu2 148-163

Deposition date:

2019-04-18

Original release date:

2019-10-22

Authors:

Owen, D.; Neuhaus, D.; Yang, J.; Herrmann, T.

Citation:

Citation: Wrobel, A.; Kadlecova, Z.; Kamenicky, J.; Yang, J.; Herrmann, T.; Kelly, B.; McCoy, A.; Evans, P.; Martin, S.; Muller, S.; Sroubek, F.; Neuhaus, D.; Honing, S.; Owen, D.. "Temporal Ordering in Endocytic Clathrin-Coated Vesicle Formation via AP2 Phosphorylation." Dev. Cell 50, 494-508 (2019).
PubMed: 31430451

Assembly members:

Assembly members:
entity_1, polymer, 138 residues, 15562.371 Da.
entity_2, polymer, 15 residues, 1798.892 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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSPNSMATELEYESVLCVKP DVSVYRIPPRASNRGYRASD WKLDQPDWTGRLRITSKGKT AYIKLEDKVSGELFAQAPVE QYPGIAVETVTDSSRYFVIR IQDGTGRSAFIGIGFTDRGD AFDFNVSLQDHFKWVKQE
entity_2: SQITSQVXGQIGWRR

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	475
15N chemical shifts	140
1H chemical shifts	1040

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1
2	entity_2	2

Entities:

Entity 1, entity_1 138 residues - 15562.371 Da.

1

GLY

SER

PRO

ASN

SER

MET

ALA

THR

GLU

LEU

2

GLU

TYR

GLU

SER

VAL

LEU

CYS

VAL

LYS

PRO

3

ASP

VAL

SER

VAL

TYR

ARG

ILE

PRO

ARG

4

ALA

SER

ASN

ARG

GLY

TYR

ARG

ALA

SER

ASP

5

TRP

LYS

LEU

ASP

GLN

PRO

ASP

TRP

THR

GLY

6

ARG

LEU

ARG

ILE

THR

SER

LYS

GLY

LYS

THR

7

ALA

TYR

ILE

LYS

LEU

GLU

ASP

LYS

VAL

SER

8

GLY

GLU

LEU

PHE

ALA

GLN

ALA

PRO

VAL

GLU

9

GLN

TYR

PRO

GLY

ILE

ALA

VAL

GLU

THR

VAL

10

THR

ASP

SER

ARG

TYR

PHE

VAL

ILE

ARG

11

ILE

GLN

ASP

GLY

THR

GLY

ARG

SER

ALA

PHE

12

ILE

GLY

ILE

GLY

PHE

THR

ASP

ARG

GLY

ASP

13

ALA

PHE

ASP

PHE

ASN

VAL

SER

LEU

GLN

ASP

14

HIS

PHE

LYS

TRP

VAL

LYS

GLN

GLU

Entity 2, entity_2 15 residues - 1798.892 Da.

1

SER

GLN

ILE

THR

SER

GLN

VAL

TPO

GLY

GLN

2

ILE

GLY

TRP

ARG

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY (reject 15N,13C coupled 1H in F1, accept 15N,13C coupled 1H in F2) tau(m) 150ms	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY (reject 15N,13C coupled 1H in F1 and F2) tau(m) 150ms	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY (reject 15N,13C coupled 1H in F2)	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic (constant time)	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic (constant time)	sample_2	isotropic	sample_conditions_1
2D 1H-1H NOESY (reject 15N,13C coupled 1H in F1, accept 13C coupled 1H in F2) tau(m) 150ms	sample_2	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HCCH-COSY (1H,13C,1H)	sample_2	isotropic	sample_conditions_1
3D HCCH-TOCSY (13C,13C,1H)	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY tau(m) 150ms	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic tau(m) 150ms	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic tau(m) 150ms	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic tau(m) 150ms	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic tau(m) 150ms	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic (reject 15N,13C coupled 1H in F1) tau(m) 150ms	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic (reject 15N,13C coupled 1H in F1) tau(m) 150ms	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic (reject 15N,13C coupled 1H in F1) tau(m) 150ms	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic (reject 15N,13C coupled 1H in F1) tau(m) 150ms	sample_2	isotropic	sample_conditions_1

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks

BMRB Entry 34395

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers: