BMRB Entry 15919

Name: NMR structure of a complex formed by the C-terminal domain of human RAP74 and a phosphorylated peptide from the central domain of the FCP1
Published: 2009-02-16

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PDB ID: 2k7l
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15919
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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

NMR structure of a complex formed by the C-terminal domain of human RAP74 and a phosphorylated peptide from the central domain of the FCP1

Deposition date:

2008-08-13

Original release date:

2009-02-16

Authors:

Yang, Ao; Abbott, Karen; Desjardins, Alexandre; Di Lello, Paola; Omichinski, James; Legault, Pascale

Citation:

Citation: Yang, Ao; Abbott, Karen; Desjardins, Alexandre; Di Lello, Paola; Omichinski, James; Legault, Pascale. "NMR structure of a complex formed by the carboxyl-terminal domain of human RAP74 and a phosphorylated peptide from the central domain of the FCP1 Phosphatase" Biochemistry 48, 1964-1974 (2009).
PubMed: 19215094

Assembly members:

Assembly members:
centFCP1-T584PO4, polymer, 19 residues, 2398.493 Da.
cterRAP74, polymer, 82 residues, 7906.366 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: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
centFCP1-T584PO4: EDXDEDDHLIYLEEILVRV
cterRAP74: STPQPPSGKTTPNSGDVQVT EDAVRRYLTRKPMTTKDLLK KFQTKKTGLSSEQTVNVLAQ ILKRLNPERKMINDKMHFSL KE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	345
15N chemical shifts	85
1H chemical shifts	589

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	centFCP1-T584PO4	1
2	cterRAP74	2

Entities:

Entity 1, centFCP1-T584PO4 19 residues - 2398.493 Da.

1

GLU

ASP

TPO

ASP

GLU

ASP

HIS

LEU

ILE

2

TYR

LEU

GLU

ILE

LEU

VAL

ARG

VAL

Entity 2, cterRAP74 82 residues - 7906.366 Da.

1

SER

THR

PRO

GLN

PRO

SER

GLY

LYS

THR

2

THR

PRO

ASN

SER

GLY

ASP

VAL

GLN

VAL

THR

3

GLU

ASP

ALA

VAL

ARG

TYR

LEU

THR

ARG

4

LYS

PRO

MET

THR

LYS

ASP

LEU

LYS

5

LYS

PHE

GLN

THR

LYS

THR

GLY

LEU

SER

6

SER

GLU

GLN

THR

VAL

ASN

VAL

LEU

ALA

GLN

7

ILE

LEU

LYS

ARG

LEU

ASN

PRO

GLU

ARG

LYS

8

MET

ILE

ASN

ASP

LYS

MET

HIS

PHE

SER

LEU

9

LYS

GLU

Samples:

15N-labeled: cterRAP74, [U-98% 15N], 1 mM; centFCP1-T584PO4 1 mM; H2O 90%; D2O, [U-100% 2H], 10%; sodium phosphate 10-40 mM; EDTA 0.25 mM

13C_15N-labeled-H2O: cterRAP74, [U-98% 13C; U-98% 15N], 1 mM; centFCP1-T584PO4 1 mM; H2O 90%; D2O, [U-100% 2H], 10%; sodium phosphate 10-40 mM; EDTA 0.25 mM

13C_15N-labeled-D2O: cterRAP74, [U-98% 13C; U-98% 15N], 1 mM; centFCP1-T584PO4 1 mM; D2O, [U-100% 2H], 100%; sodium phosphate 10-40 mM; EDTA 0.25 mM

sample_conditions_1: ionic strength: 25 mM; pH: 6.5; pressure: 1 atm; temperature: 300 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	15N-labeled	isotropic	sample_conditions_1
2D 1H-15N HSQC	13C_15N-labeled-H2O	isotropic	sample_conditions_1
2D 1H-13C HSQC	13C_15N-labeled-D2O	isotropic	sample_conditions_1
3D HNHA	15N-labeled	isotropic	sample_conditions_1
3D HNCACB	13C_15N-labeled-H2O	isotropic	sample_conditions_1
3D HNCO	13C_15N-labeled-H2O	isotropic	sample_conditions_1
3D CBCA(CO)NH	13C_15N-labeled-H2O	isotropic	sample_conditions_1
3D HCCH-TOCSY	13C_15N-labeled-D2O	isotropic	sample_conditions_1
3D HCCH-COSY	13C_15N-labeled-D2O	isotropic	sample_conditions_1
3D 1H-15N NOESY	15N-labeled	isotropic	sample_conditions_1
3D CCCTOCSY-NHH	13C_15N-labeled-H2O	isotropic	sample_conditions_1
3D HCCTOCSY-NHH	13C_15N-labeled-H2O	isotropic	sample_conditions_1
3D 13C-edited HMQC-NOESY	13C_15N-labeled-D2O	isotropic	sample_conditions_1
HBCBCGCDHD_ARO	13C_15N-labeled-D2O	isotropic	sample_conditions_1
HBCBCGCDCEHE_ARO	13C_15N-labeled-D2O	isotropic	sample_conditions_1
2D isotope filtered 1H-1H TOCSY	13C_15N-labeled-D2O	isotropic	sample_conditions_1
2D isotope filtered 1H-1H NOESY	13C_15N-labeled-D2O	isotropic	sample_conditions_1
2D isotope filtered 1H-1H TOCSY	13C_15N-labeled-H2O	isotropic	sample_conditions_1
2D isotope filtered 1H-1H NOESY	13C_15N-labeled-H2O	isotropic	sample_conditions_1
2D 13C F1-filtered, F2-edited NOESY	13C_15N-labeled-H2O	isotropic	sample_conditions_1
3D 15N/13C F1-filtered, F3-edited NOESY	13C_15N-labeled-D2O	isotropic	sample_conditions_1

Software:

NMRPipe v2.5, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRView v5.2.2_01, Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking

NMRDraw v2.5, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis, processing

CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

NMR spectrometers:

Varian Unity 600 MHz

PDB	2K7L 1I27 1J2X 1NHA 1ONV 2K7L
DBJ	BAG11094 BAG37667 BAG56676 BAG63544 BAK63776
EMBL	CAA45404 CAA45408 CAG33079
GB	AAH00120 AAH13007 AAP35761 AAP36816 AAX32213
PRF	1804352A 1804353A
REF	NP_001267379 NP_002087 XP_003281617 XP_003461160 XP_003819382
SP	P35269
AlphaFold	P35269