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BMRB: 6330


6330
1XSA
Solution structure of human AP4A hydrolase
Authors
Swarbrick, J.D.
Assembly
AP4A hydrolase monomer
Entity
1. AP4A hydrolase monomer (polymer, Thiol state: all free), 153 monomers, 17295.61 Da Detail

GPLGSMALRA CGLIIFRRCL IPKVDNNAIE FLLLQASDGI HHWTPPKGHV EPGEDDLETA LRATQEEAGI EAGQLTIIEG FKRELNYVAR NKPKTVIYWL AEVKDYDVEI RLSHEHQAYR WLGLEEACQL AQFKEMKAAL QEGHQFLCSI EAL


Formula weight
17295.61 Da
Source organism
Homo sapiens
Exptl. method
NMR
Refine. method
CANDID with talos for NOE assignments.
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 98.7 %, Completeness: 90.3 %, Completeness (bb): 91.6 % Detail
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Polymer type: polypeptide(L)

Total1H13C15N
All90.3 % (1629 of 1804)91.7 % (860 of 938)88.2 % (621 of 704)91.4 % (148 of 162)
Backbone91.6 % (830 of 906)93.9 % (292 of 311)90.2 % (404 of 448)91.2 % (134 of 147)
Sidechain89.4 % (930 of 1040)90.6 % (568 of 627)87.4 % (348 of 398)93.3 % (14 of 15)
Aromatic78.9 % (112 of 142)91.5 % (65 of 71)64.7 % (44 of 68)100.0 % (3 of 3)
Methyl97.8 % (182 of 186)97.8 % (91 of 93)97.8 % (91 of 93)

1. AP4A

GPLGSMALRA CGLIIFRRCL IPKVDNNAIE FLLLQASDGI HHWTPPKGHV EPGEDDLETA LRATQEEAGI EAGQLTIIEG FKRELNYVAR NKPKTVIYWL AEVKDYDVEI RLSHEHQAYR WLGLEEACQL AQFKEMKAAL QEGHQFLCSI EAL

Show sample condition
Sample

Temperature 293 (±1) K, pH 6.5 (±0.1)


#NameIsotope labelingTypeConcentration
1AP4A0.0 ~ 0.0 mM
2MgCl220 mM
3Imidazole20 mM
4H2o90 %
5D2o10 %

LACS Plot; CA
Referencing offset: 0.09 ppm, Outliers: 2 Detail
LACS Plot; CB
Referencing offset: 0.09 ppm, Outliers: 2 Detail
LACS Plot; HA
Referencing offset: 0.0 ppm, Outliers: 1 Detail
LACS Plot; CO
Referencing offset: 0.2 ppm, Outliers: 2 Detail
Protein Blocks Logo
Calculated from 33 models in PDB: 1XSA, Strand ID: A Detail

Release date
2004-12-21
Citation 1
1H, 13C, and 15N resonance assignments of the 17 kDa Ap4A hydrolase from Homo sapiens in the presence and absence of ATP
Swarbrick, J.D., Buyya, S., Gunawardana, D., Fletcher, J.L., Branson, K., Smith, B., Pepe, S., McLennan, A.G., Gayler, K.R., Gooley, P.R.
J. Biomol. NMR (2005), 31, 181-182, PubMed 15772762 , DOI 10.1007/s10858-004-7440-4 ,
Show more 1 citaion
Citation 2
Structure and substrate-binding mechanism of human Ap4A hydrolase
Swarbrick, J.D., Buyya, S., Gunawardana, D., Gayler, K.R., McLennan, A.G., Gooley, P.R.
J. Biol. Chem. (2005), 280, 8471-8481, PubMed 15596429 , DOI 10.1074/jbc.M412318200 ,
Related entities 1. AP4A hydrolase monomer, : 1 : 2 : 5 : 31 entities Detail
More details for 39 related entities
Interaction partners 1. AP4A hydrolase monomer, : 2 interactors Detail
More details for 2 interactors identified by 2 citations
Experiments performed 1 experiments Detail
nullKeywords NMR nudix assignment AP4A