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Backbone and side-chain 1H, 13C, and 15N Chemical Shift Assignments for SIP (1-77)
Authors
Bhattacharya, S., Lee, Y., Michowski, W., Filipek, A., Kuznicki, J., Chazin, W.J.
Assembly
Siah-Interacting Protein (Residues 1-77)
Entity
1. Siah-Interacting Protein (Residues 1-77) (polymer, Thiol state: not present), 77 monomers, 8771.068 Da Detail

MASVLEELQK DLEEVKVLLE KSTRKRLRDT LTSEKSKIET ELKNKMQQKS QKKPELDNEK PAAVVAPLTT GYTVKIS


Formula weight
8771.068 Da
Source organism
Mus musculus
Exptl. method
NMR
Refine. method
Torsion Angle Dynamics
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 98.7 %, Completeness: 93.6 %, Completeness (bb): 94.7 % Detail

Polymer type: polypeptide(L)

Total1H13C15N
All93.6 % (875 of 935)94.4 % (469 of 497)91.9 % (329 of 358)96.2 % (77 of 80)
Backbone94.7 % (432 of 456)95.4 % (145 of 152)93.9 % (216 of 230)95.9 % (71 of 74)
Sidechain93.0 % (516 of 555)93.9 % (324 of 345)91.2 % (186 of 204)100.0 % (6 of 6)
Aromatic25.0 % (2 of 8)50.0 % (2 of 4) 0.0 % (0 of 4)
Methyl91.5 % (86 of 94)91.5 % (43 of 47)91.5 % (43 of 47)

1. single chain biopolymer

MASVLEELQK DLEEVKVLLE KSTRKRLRDT LTSEKSKIET ELKNKMQQKS QKKPELDNEK PAAVVAPLTT GYTVKIS

Sample #1

Temperature 303 (±1) K, pH 7.0 (±0.2)


#NameIsotope labelingTypeConcentration
1single chain biopolymer[U-100% 13C; U-100% 15N]1.0 mM
2NaPi20.0 mM
3NaCl50 mM
4H2O90 %
Sample #2

Temperature 303 (±1) K, pH 7.0 (±0.2)


#NameIsotope labelingTypeConcentration
5single chain biopolymer[U-100% 13C]1 mM
6NaPi20 mM
7NaCl50 mM
8D2O100 %
Sample #3

Temperature 303 (±1) K, pH 7.0 (±0.2)


#NameIsotope labelingTypeConcentration
9single chain biopolymer[U-10% 13C]1 mM
10NaPi20 mM
11NaCl50 mM
12D2O100 %

LACS Plot; CA
Referencing offset: 0.19 ppm, Outliers: 1 Detail
LACS Plot; CB
Referencing offset: 0.19 ppm, Outliers: 1 Detail
LACS Plot; HA
Referencing offset: 0.15 ppm, Outliers: 1 Detail
LACS Plot; CO
Referencing offset: 0.09 ppm, Outliers: 1 Detail
Protein Blocks Logo
Calculated from 20 models in PDB: 1YSM, Strand ID: A Detail


Release date
2005-08-15
Citation
The modular structure of SIP facilitates its role in stabilizing multiprotein assemblies
Bhattacharya, S., Lee, Y., Michowski, W., Filipek, A., Kuznicki, J., Chazin, W.J.
Biochemistry (2005), 44, 9462-9471, PubMed 15996101 , DOI 10.1021/bi0502689 ,
Entries sharing articles BMRB: 1, Swiss-Prot: 1 entries Detail
  BMRB: 6500 released on 2005-08-15
    Title Backbone 1H, 13C, and 15N Chemical Shift Assignments for SIP (74-178)
  Swiss-Prot: Q9CXW3 released on 2004-04-26
    Title CYBP_MOUSE Entity Calcyclin-binding protein
Related entities 1. Siah-Interacting Protein (Residues 1-77), : 1 : 2 : 11 entities Detail
Interaction partners 1. Siah-Interacting Protein (Residues 1-77), : 20 interactors Detail
Experiments performed 8 experiments Detail
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