BMRB Entry 31064

Name: Human diaphanous inhibitory domain bound to diaphanous autoregulatory domain
Published: 2023-10-18

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PDB ID: 8fg1
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR31064
MolProbity Validation Chart

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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:

Human diaphanous inhibitory domain bound to diaphanous autoregulatory domain

Deposition date:

2022-12-12

Original release date:

2023-10-18

Authors:

Ramirez, L.; Theophall, G.; Premo, A.; Manigrasso, M.; Yepuri, G.; Burz, D.; Ramasamy, R.; Schmidt, A.; Shekhtman, A.

Citation:

Citation: Theophall, Gregory; Ramirez, Lisa; Premo, Aaron; Reverdatto, Sergey; Manigrasso, Michaele; Yepuri, Gautham; Burz, David; Ramasamy, Ravichandran; Schmidt, Ann Marie; Shekhtman, Alexander. "Disruption of the Productive Encounter Complex Results in Dysregulation of DIAPH1 Activity" J. Biol. Chem. 299, 105342-105342 (2023).
PubMed: 37832872

Assembly members:

Assembly members:
entity_1, polymer, 256 residues, 29116.410 Da.
entity_2, polymer, 29 residues, 3161.510 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: MGSSERSHHHHHHSGSESKS AMMYIQELRSGLRDMPLLSC LESLRVSLNNNPVSWVQTFG AEGLASLLDILKRLHDEKEE TAGSYDSRNKHEIIRCLKAF MNNKFGIKTMLETEEGILLL VRAMDPAVPNMMIDAAKLLS ALCILPQPEDMNERVLEAMT ERAEMDEVERFQPLLDGLKS GTTIALKVGCLQLINALITP AEELDFRVHIRSELMRLGLH QVLQDLREIENEDMRVQLNV FDEQGEEDSYDLKGRL
entity_2: DETGVLDSLLEALQSGAAFR RKRGPRQAN

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
- assigned_chemical_shifts_2
spectral_peak_list
- spectral_peak_list_1
- spectral_peak_list_2

Data type	Count
13C chemical shifts	463
15N chemical shifts	253
1H chemical shifts	1706

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1
2	unit_2	2

Entities:

Entity 1, unit_1 256 residues - 29116.410 Da.

1

MET

GLY

SER

GLU

ARG

SER

HIS

2

HIS

SER

GLY

SER

GLU

SER

LYS

SER

3

ALA

MET

TYR

ILE

GLN

GLU

LEU

ARG

SER

4

GLY

LEU

ARG

ASP

MET

PRO

LEU

SER

CYS

5

LEU

GLU

SER

LEU

ARG

VAL

SER

LEU

ASN

6

ASN

PRO

VAL

SER

TRP

VAL

GLN

THR

PHE

GLY

7

ALA

GLU

GLY

LEU

ALA

SER

LEU

ASP

ILE

8

LEU

LYS

ARG

LEU

HIS

ASP

GLU

LYS

GLU

9

THR

ALA

GLY

SER

TYR

ASP

SER

ARG

ASN

LYS

10

HIS

GLU

ILE

ARG

CYS

LEU

LYS

ALA

PHE

11

MET

ASN

LYS

PHE

GLY

ILE

LYS

THR

MET

12

LEU

GLU

THR

GLU

GLY

ILE

LEU

13

VAL

ARG

ALA

MET

ASP

PRO

ALA

VAL

PRO

ASN

14

MET

ILE

ASP

ALA

LYS

LEU

SER

15

ALA

LEU

CYS

ILE

LEU

PRO

GLN

PRO

GLU

ASP

16

MET

ASN

GLU

ARG

VAL

LEU

GLU

ALA

MET

THR

17

GLU

ARG

ALA

GLU

MET

ASP

GLU

VAL

GLU

ARG

18

PHE

GLN

PRO

LEU

ASP

GLY

LEU

LYS

SER

19

GLY

THR

ILE

ALA

LEU

LYS

VAL

GLY

CYS

20

LEU

GLN

LEU

ILE

ASN

ALA

LEU

ILE

THR

PRO

21

ALA

GLU

LEU

ASP

PHE

ARG

VAL

HIS

ILE

22

ARG

SER

GLU

LEU

MET

ARG

LEU

GLY

LEU

HIS

23

GLN

VAL

LEU

GLN

ASP

LEU

ARG

GLU

ILE

GLU

24

ASN

GLU

ASP

MET

ARG

VAL

GLN

LEU

ASN

VAL

25

PHE

ASP

GLU

GLN

GLY

GLU

ASP

SER

TYR

26

ASP

LEU

LYS

GLY

ARG

LEU

Entity 2, unit_2 29 residues - 3161.510 Da.

1

ASP

GLU

THR

GLY

VAL

LEU

ASP

SER

LEU

2

GLU

ALA

LEU

GLN

SER

GLY

ALA

PHE

ARG

3

ARG

LYS

ARG

GLY

PRO

ARG

GLN

ALA

ASN

Samples:

sample_1: Diaphanous inhibitory domain, [U-15N], 300 uM; Diaphanous autoregulatory domain 500 uM

sample_2: Diaphanous inhibitory domain, [U-15N], 300 uM; Diaphanous autoregulatory domain, [U-13C], 500 uM

sample_3: Diaphanous inhibitory domain, [U-100% 13C; U-100% 15N], 300 uM; Diaphanous autoregulatory domain 500 uM

sample_4: Diaphanous inhibitory domain 300 uM; Diaphanous autoregulatory domain, [U-100% 13C; U-100% 15N], 500 uM

sample_5: Diaphanous inhibitory domain 300 uM; Diaphanous autoregulatory domain, [U-100% 15N], 300 uM

sample_conditions_1: ionic strength: 140 mM; pH: 7.5; pressure: 1 atm; temperature: 305 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D CBCA(CO)NH	sample_3	isotropic	sample_conditions_1
3D HNCO	sample_3	isotropic	sample_conditions_1
3D HNCA	sample_3	isotropic	sample_conditions_1
3D HNCACB	sample_3	isotropic	sample_conditions_1
3D HN(CO)CA	sample_3	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_5	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_4	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_5	isotropic	sample_conditions_1
3D HN(CO)CA	sample_4	isotropic	sample_conditions_1
3D HNCACB	sample_4	isotropic	sample_conditions_1
3D H(CCO)NH	sample_3	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_4	isotropic	sample_conditions_1
H(CCH)-TOCSY	sample_4	isotropic	sample_conditions_1

Software:

TopSpin, Bruker Biospin - collection, processing

CARA, Keller and Wuthrich - chemical shift assignment, peak picking

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

YASARA, Krieger - refinement

NMR spectrometers:

Bruker Ascend 600 MHz

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