BMRB Entry 25995

Name: Protein complex
Published: 2016-07-18

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PDB ID: 2nbv
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25995
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:

Protein complex

Deposition date:

2016-03-12

Original release date:

2016-07-18

Authors:

Chen, Xiang; Walters, Kylie

Citation:

Citation: Chen, Xiang; Randles, Leah; Shi, Ke; Tarasov, Sergey; Aihara, Hideki; Walters, Kylie. "Structures of Rpn1 T1:Rad23 and hRpn13:hPLIC2 Reveal Distinct Binding Mechanisms between Substrate Receptors and Shuttle Factors of the Proteasome" Structure 24, 1257-1270 (2016).
PubMed: 27396824

Assembly members:

Assembly members:
entity_1, polymer, 150 residues, Formula weight is not available
entity_2, polymer, 78 residues, 8764.290 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: pRSET

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MTTSGALFPSLVPGSRGASN KYLVEFRAGKMSLKGTTVTP DKRKGLVYIQQTDDSLIHFC WKDRTSGNVEDDLIIFPDDC EFKRVPQCPSGRVYVLKFKA GSKRLFFWMQEPKTDQDEEH CRKVNEYLNNPPMPGALGAS GSSGHELSAL
entity_2: APAEPKIIKVTVKTPKEKEE FAVPENSSVQQFKEAISKRF KSQTDQLVLIFAGKILKDQD TLIQHGIHDGLTVHLVIK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	581
15N chemical shifts	149
1H chemical shifts	915

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

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

Entities:

Entity 1, entity_1 150 residues - Formula weight is not available

1	MET	THR	THR	SER	GLY	ALA	LEU	PHE	PRO	SER
2	LEU	VAL	PRO	GLY	SER	ARG	GLY	ALA	SER	ASN
3	LYS	TYR	LEU	VAL	GLU	PHE	ARG	ALA	GLY	LYS
4	MET	SER	LEU	LYS	GLY	THR	THR	VAL	THR	PRO
5	ASP	LYS	ARG	LYS	GLY	LEU	VAL	TYR	ILE	GLN
6	GLN	THR	ASP	ASP	SER	LEU	ILE	HIS	PHE	CYS
7	TRP	LYS	ASP	ARG	THR	SER	GLY	ASN	VAL	GLU
8	ASP	ASP	LEU	ILE	ILE	PHE	PRO	ASP	ASP	CYS
9	GLU	PHE	LYS	ARG	VAL	PRO	GLN	CYS	PRO	SER
10	GLY	ARG	VAL	TYR	VAL	LEU	LYS	PHE	LYS	ALA
11	GLY	SER	LYS	ARG	LEU	PHE	PHE	TRP	MET	GLN
12	GLU	PRO	LYS	THR	ASP	GLN	ASP	GLU	GLU	HIS
13	CYS	ARG	LYS	VAL	ASN	GLU	TYR	LEU	ASN	ASN
14	PRO	PRO	MET	PRO	GLY	ALA	LEU	GLY	ALA	SER
15	GLY	SER	SER	GLY	HIS	GLU	LEU	SER	ALA	LEU

Entity 2, entity_2 78 residues - 8764.290 Da.

1

ALA

PRO

ALA

GLU

PRO

LYS

ILE

LYS

VAL

2

THR

VAL

LYS

THR

PRO

LYS

GLU

LYS

GLU

3

PHE

ALA

VAL

PRO

GLU

ASN

SER

VAL

GLN

4

GLN

PHE

LYS

GLU

ALA

ILE

SER

LYS

ARG

PHE

5

LYS

SER

GLN

THR

ASP

GLN

LEU

VAL

LEU

ILE

6

PHE

ALA

GLY

LYS

ILE

LEU

LYS

ASP

GLN

ASP

7

THR

LEU

ILE

GLN

HIS

GLY

ILE

HIS

ASP

GLY

8

LEU

THR

VAL

HIS

LEU

VAL

ILE

LYS

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_3	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_3	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_3	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 25995

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

1	MET	THR	THR	SER	GLY	ALA	LEU	PHE	PRO	SER
2	LEU	VAL	PRO	GLY	SER	ARG	GLY	ALA	SER	ASN
3	LYS	TYR	LEU	VAL	GLU	PHE	ARG	ALA	GLY	LYS
4	MET	SER	LEU	LYS	GLY	THR	THR	VAL	THR	PRO
5	ASP	LYS	ARG	LYS	GLY	LEU	VAL	TYR	ILE	GLN
6	GLN	THR	ASP	ASP	SER	LEU	ILE	HIS	PHE	CYS
7	TRP	LYS	ASP	ARG	THR	SER	GLY	ASN	VAL	GLU
8	ASP	ASP	LEU	ILE	ILE	PHE	PRO	ASP	ASP	CYS
9	GLU	PHE	LYS	ARG	VAL	PRO	GLN	CYS	PRO	SER
10	GLY	ARG	VAL	TYR	VAL	LEU	LYS	PHE	LYS	ALA
11	GLY	SER	LYS	ARG	LEU	PHE	PHE	TRP	MET	GLN
12	GLU	PRO	LYS	THR	ASP	GLN	ASP	GLU	GLU	HIS
13	CYS	ARG	LYS	VAL	ASN	GLU	TYR	LEU	ASN	ASN
14	PRO	PRO	MET	PRO	GLY	ALA	LEU	GLY	ALA	SER
15	GLY	SER	SER	GLY	HIS	GLU	LEU	SER	ALA	LEU

1	MET	THR	THR	SER	GLY	ALA	LEU	PHE	PRO	SER
2	LEU	VAL	PRO	GLY	SER	ARG	GLY	ALA	SER	ASN
3	LYS	TYR	LEU	VAL	GLU	PHE	ARG	ALA	GLY	LYS
4	MET	SER	LEU	LYS	GLY	THR	THR	VAL	THR	PRO
5	ASP	LYS	ARG	LYS	GLY	LEU	VAL	TYR	ILE	GLN
6	GLN	THR	ASP	ASP	SER	LEU	ILE	HIS	PHE	CYS
7	TRP	LYS	ASP	ARG	THR	SER	GLY	ASN	VAL	GLU
8	ASP	ASP	LEU	ILE	ILE	PHE	PRO	ASP	ASP	CYS
9	GLU	PHE	LYS	ARG	VAL	PRO	GLN	CYS	PRO	SER
10	GLY	ARG	VAL	TYR	VAL	LEU	LYS	PHE	LYS	ALA
11	GLY	SER	LYS	ARG	LEU	PHE	PHE	TRP	MET	GLN
12	GLU	PRO	LYS	THR	ASP	GLN	ASP	GLU	GLU	HIS
13	CYS	ARG	LYS	VAL	ASN	GLU	TYR	LEU	ASN	ASN
14	PRO	PRO	MET	PRO	GLY	ALA	LEU	GLY	ALA	SER
15	GLY	SER	SER	GLY	HIS	GLU	LEU	SER	ALA	LEU

1	MET	THR	THR	SER	GLY	ALA	LEU	PHE	PRO	SER
2	LEU	VAL	PRO	GLY	SER	ARG	GLY	ALA	SER	ASN
3	LYS	TYR	LEU	VAL	GLU	PHE	ARG	ALA	GLY	LYS
4	MET	SER	LEU	LYS	GLY	THR	THR	VAL	THR	PRO
5	ASP	LYS	ARG	LYS	GLY	LEU	VAL	TYR	ILE	GLN
6	GLN	THR	ASP	ASP	SER	LEU	ILE	HIS	PHE	CYS
7	TRP	LYS	ASP	ARG	THR	SER	GLY	ASN	VAL	GLU
8	ASP	ASP	LEU	ILE	ILE	PHE	PRO	ASP	ASP	CYS
9	GLU	PHE	LYS	ARG	VAL	PRO	GLN	CYS	PRO	SER
10	GLY	ARG	VAL	TYR	VAL	LEU	LYS	PHE	LYS	ALA
11	GLY	SER	LYS	ARG	LEU	PHE	PHE	TRP	MET	GLN
12	GLU	PRO	LYS	THR	ASP	GLN	ASP	GLU	GLU	HIS
13	CYS	ARG	LYS	VAL	ASN	GLU	TYR	LEU	ASN	ASN
14	PRO	PRO	MET	PRO	GLY	ALA	LEU	GLY	ALA	SER
15	GLY	SER	SER	GLY	HIS	GLU	LEU	SER	ALA	LEU