BMRB Entry 18433

Name: Solution structure of the mouse Rev1 CTD in complex with the Rev1-interacting Region (RIR)of Pol Kappa
Published: 2012-06-18

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PDB ID: 2lsj
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18433
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution structure of the mouse Rev1 CTD in complex with the Rev1-interacting Region (RIR)of Pol Kappa

Deposition date:

2012-05-01

Original release date:

2012-06-18

Authors:

Liu, Jiangxin; Wojtaszek, Jessica; Zhou, Pei

Citation:

Citation: Wojtaszek, Jessica; Liu, Jiangxin; Wang, Sanjay; Xue, Su; Walker, Yaohua; Zhou, Graham. "Multifaceted recognition of vertebrate Rev1 by translesion polymerases and ." J. Biol. Chem. 287, 26400-26408 (2012).
PubMed: 22700975

Assembly members:

Assembly members:
entity_1, polymer, 119 residues, 11166.953 Da.
entity_2, polymer, 25 residues, 1747.002 Da.

Natural source:

Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pMAL-C2

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSGGGAQDLSSLLPGQSSCF RPAAPNLAGAVEFSDVKTLL KEWITTISDPMEEDILQVVR YCTDLIEEKDLEKLDLVIKY MKRLMQQSVESVWNMAFDFI LDNVQVVLQQTYGSTLKVT
entity_2: SHMSHKKSFFDKKRSERISN CQDTS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	460
15N chemical shifts	132
1H chemical shifts	960

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	mouse Rev1 CTD	1
2	RIR of Pol Kappa	2

Entities:

Entity 1, mouse Rev1 CTD 119 residues - 11166.953 Da.

1

GLY

SER

GLY

ALA

GLN

ASP

LEU

SER

2

SER

LEU

PRO

GLY

GLN

SER

CYS

PHE

3

ARG

PRO

ALA

PRO

ASN

LEU

ALA

GLY

ALA

4

VAL

GLU

PHE

SER

ASP

VAL

LYS

THR

LEU

5

LYS

GLU

TRP

ILE

THR

ILE

SER

ASP

PRO

6

MET

GLU

ASP

ILE

LEU

GLN

VAL

ARG

7

TYR

CYS

THR

ASP

LEU

ILE

GLU

LYS

ASP

8

LEU

GLU

LYS

LEU

ASP

LEU

VAL

ILE

LYS

TYR

9

MET

LYS

ARG

LEU

MET

GLN

SER

VAL

GLU

10

SER

VAL

TRP

ASN

MET

ALA

PHE

ASP

PHE

ILE

11

LEU

ASP

ASN

VAL

GLN

VAL

LEU

GLN

12

THR

TYR

GLY

SER

THR

LEU

LYS

VAL

THR

Entity 2, RIR of Pol Kappa 25 residues - 1747.002 Da.

1

SER

HIS

MET

SER

HIS

LYS

SER

PHE

2

ASP

LYS

ARG

SER

GLU

ARG

ILE

SER

ASN

3

CYS

GLN

ASP

THR

SER

Samples:

sample_1: Rev1_CTD, [U-100% 15N], 0.7 – 1 mM; RIR, [U-100% 15N], 0.7 – 1 mM; sodium phosphate 25 mM; potassium chloride 100 mM; DTT 10 mM; EDTA 1 mM; H2O 90%; D2O 10%

sample_2: Rev1_CTD, [U-100% 13C; U-100% 15N], 0.7 – 1 mM; RIR, [U-100% 13C; U-100% 15N], 0.7 – 1 mM; sodium phosphate 25 mM; potassium chloride 100 mM; DTT 10 mM; EDTA 1 mM; H2O 90%; D2O 10%

sample_3: Rev1_CTD, [U-100% 13C; U-100% 15N], 0.7 – 1 mM; RIR, [U-100% 13C; U-100% 15N], 0.7 – 1 mM; sodium phosphate 25 mM; potassium chloride 100 mM; DTT 10 mM; EDTA 1 mM; D2O 100%

sample_conditions_1: ionic strength: 0.1 M; pH: 7; pressure: 1 atm; temperature: 310 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1
3D HN(CO)CA	sample_2	isotropic	sample_conditions_1
3D HN(CA)CB	sample_2	isotropic	sample_conditions_1
3D HN(COCA)CB	sample_2	isotropic	sample_conditions_1
3D HA(CA)NH	sample_2	isotropic	sample_conditions_1
3D HA(CACO)NH	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D (HCA)CO(CA)NH	sample_2	isotropic	sample_conditions_1
4D HCCH-TOCSY	sample_3	isotropic	sample_conditions_1
4D HCCONH-TOCSY	sample_3	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_3	isotropic	sample_conditions_1
4D 13C-HMQC-NOESY-15N-HSQC	sample_2	isotropic	sample_conditions_1
4D 13C-HMQC-NOESY-13C-HSQC	sample_3	isotropic	sample_conditions_1

Software:

TALOS, Cornilescu, Delaglio and Bax - data analysis

SPARKY, Goddard - data analysis

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

Varian INOVA 600 MHz
Varian INOVA 800 MHz

BMRB	18431
PDB	2LSG 2LSJ 4FJO 2LSJ
DBJ	BAB64933
GB	AAF23323 AAH58093 EDL14541
REF	NP_062516 XP_006496216 XP_006496217 XP_006496218 XP_006496219
SP	Q920Q2
AlphaFold	Q920Q2