BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 15919

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   PubMed: 19215094

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

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).

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

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: chemical synthesis

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

Data sets:
Data typeCount
13C chemical shifts345
15N chemical shifts85
1H chemical shifts589

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1centFCP1-T584PO41
2cterRAP742

Entities:

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

1   GLUASPTPOASPGLUASPASPHISLEUILE
2   TYRLEUGLUGLUILELEUVALARGVAL

Entity 2, cterRAP74 82 residues - 7906.366 Da.

1   SERTHRPROGLNPROPROSERGLYLYSTHR
2   THRPROASNSERGLYASPVALGLNVALTHR
3   GLUASPALAVALARGARGTYRLEUTHRARG
4   LYSPROMETTHRTHRLYSASPLEULEULYS
5   LYSPHEGLNTHRLYSLYSTHRGLYLEUSER
6   SERGLUGLNTHRVALASNVALLEUALAGLN
7   ILELEULYSARGLEUASNPROGLUARGLYS
8   METILEASNASPLYSMETHISPHESERLEU
9   LYSGLU

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQC15N-labeledisotropicsample_conditions_1
2D 1H-15N HSQC13C_15N-labeled-H2Oisotropicsample_conditions_1
2D 1H-13C HSQC13C_15N-labeled-D2Oisotropicsample_conditions_1
3D HNHA15N-labeledisotropicsample_conditions_1
3D HNCACB13C_15N-labeled-H2Oisotropicsample_conditions_1
3D HNCO13C_15N-labeled-H2Oisotropicsample_conditions_1
3D CBCA(CO)NH13C_15N-labeled-H2Oisotropicsample_conditions_1
3D HCCH-TOCSY13C_15N-labeled-D2Oisotropicsample_conditions_1
3D HCCH-COSY13C_15N-labeled-D2Oisotropicsample_conditions_1
3D 1H-15N NOESY15N-labeledisotropicsample_conditions_1
3D CCCTOCSY-NHH13C_15N-labeled-H2Oisotropicsample_conditions_1
3D HCCTOCSY-NHH13C_15N-labeled-H2Oisotropicsample_conditions_1
3D 13C-edited HMQC-NOESY13C_15N-labeled-D2Oisotropicsample_conditions_1
HBCBCGCDHD_ARO13C_15N-labeled-D2Oisotropicsample_conditions_1
HBCBCGCDCEHE_ARO13C_15N-labeled-D2Oisotropicsample_conditions_1
2D isotope filtered 1H-1H TOCSY13C_15N-labeled-D2Oisotropicsample_conditions_1
2D isotope filtered 1H-1H NOESY13C_15N-labeled-D2Oisotropicsample_conditions_1
2D isotope filtered 1H-1H TOCSY13C_15N-labeled-H2Oisotropicsample_conditions_1
2D isotope filtered 1H-1H NOESY13C_15N-labeled-H2Oisotropicsample_conditions_1
2D 13C F1-filtered, F2-edited NOESY13C_15N-labeled-H2Oisotropicsample_conditions_1
3D 15N/13C F1-filtered, F3-edited NOESY13C_15N-labeled-D2Oisotropicsample_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

Related Database Links:

PDB
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