BMRB Entry 16412

Name: Solution structure of Rtt103 bound to CTD peptide
Published: 2010-09-17

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16412

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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 Rtt103 bound to CTD peptide

Deposition date:

2009-07-21

Original release date:

2010-09-17

Authors:

Lunde, Bradley; Reichow, Steve; Kim, Minkyu; Leeper, Thomas; Becker, Roland; Buratowski, Stephen; Meinhart, Anton; Varani, Gabriele

Citation:

Citation: Lunde, Bradley; Reichow, Steve; Kim, Minkyu; Suh, Hyunsuk; Leeper, Thomas; Yang, Fan; Mutschler, Hannes; Buratowski, Stephen; Meinhart, Anton; Varani, Gabriele. "Cooperative interaction of transcription termination factors with the RNA polymerase II C-terminal domain." Nat. Struct. Mol. Biol. 17, 1195-1201 (2010).
PubMed: 20818393

Assembly members:

Assembly members:
Rtt103 bound to CTD peptide, polymer, 142 residues, 15747.308 Da.

Natural source:

Natural source: Common Name: baker's yeast Taxonomy ID: 4932 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Saccharomyces cerevisiae

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: PET-28b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Rtt103 bound to CTD peptide: MAFSSEQFTTKLNTLEDSQE SISSASKWLLLQYRDAPKVA EMWKEYMLRPSVNTRRKLLG LYLMNHVVQQAKGQKIIQFQ DSFGKVAAEVLGRINQEFPR DLKKKLSRVVNILKERNIFS KQVVNDIERSLAAALEHHHH HH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	393
15N chemical shifts	137
1H chemical shifts	1001

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Rtt103 bound to CTD peptide	1

Entities:

Entity 1, Rtt103 bound to CTD peptide 142 residues - 15747.308 Da.

1

MET

ALA

PHE

SER

GLU

GLN

PHE

THR

2

LYS

LEU

ASN

THR

LEU

GLU

ASP

SER

GLN

GLU

3

SER

ILE

SER

ALA

SER

LYS

TRP

LEU

4

LEU

GLN

TYR

ARG

ASP

ALA

PRO

LYS

VAL

ALA

5

GLU

MET

TRP

LYS

GLU

TYR

MET

LEU

ARG

PRO

6

SER

VAL

ASN

THR

ARG

LYS

LEU

GLY

7

LEU

TYR

LEU

MET

ASN

HIS

VAL

GLN

8

ALA

LYS

GLY

GLN

LYS

ILE

GLN

PHE

GLN

9

ASP

SER

PHE

GLY

LYS

VAL

ALA

GLU

VAL

10

LEU

GLY

ARG

ILE

ASN

GLN

GLU

PHE

PRO

ARG

11

ASP

LEU

LYS

LEU

SER

ARG

VAL

12

ASN

ILE

LEU

LYS

GLU

ARG

ASN

ILE

PHE

SER

13

LYS

GLN

VAL

ASN

ASP

ILE

GLU

ARG

SER

14

LEU

ALA

LEU

GLU

HIS

15

HIS

Samples:

sample_2: sodium chloride 120 mM; TRIS 10 mM; Rtt1030.5 – 1 mM; CTD1 – 1.5 mM; D2O 100%

sample_conditions_1: ionic strength: 120 mM; pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_2	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_2	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_2	isotropic	sample_conditions_1

Software:

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - refinement, structure solution

NMR spectrometers:

Bruker DMX 500 MHz
Bruker DMX 600 MHz
Bruker DMX 750 MHz
Varian INOVA 800 MHz

BMRB	16411 17044
PDB	2KM4 2L0I
DBJ	GAA22510
EMBL	CAY78790
GB	AAB64467 AAS56119 AHY75263 AJP37990 AJU58113
REF	NP_010575
SP	Q05543
TPG	DAA12129
AlphaFold	Q05543