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Assignment of human AP4A hydrolase in complex with ATP
Authors
Swarbrick, J.D.
Assembly
AP4A hydrolase with ATP
Entity
1. AP4A (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


2. ATP (non-polymer), 507.181 Da
Total weight
17802.791 Da
Max. entity weight
17295.61 Da
Source organism
Homo sapiens
Exptl. method
NMR
Refine. method
CANDID
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 100.0 %, Completeness: 95.7 %, Completeness (bb): 98.9 % Detail

Polymer type: polypeptide(L)

Total1H13C15N
All95.7 % (1726 of 1804)96.5 % (905 of 938)94.0 % (662 of 704)98.1 % (159 of 162)
Backbone98.9 % (896 of 906)99.7 % (310 of 311)98.2 % (440 of 448)99.3 % (146 of 147)
Sidechain93.4 % (971 of 1040)94.9 % (595 of 627)91.2 % (363 of 398)86.7 % (13 of 15)
Aromatic82.4 % (117 of 142)95.8 % (68 of 71)67.6 % (46 of 68)100.0 % (3 of 3)
Methyl98.4 % (183 of 186)98.9 % (92 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

Sample

Temperature 293 (±1) K, pH 6.5 (±0.1)


#NameIsotope labelingTypeConcentration
1AP4A[U-95% 13C; U-95% 15N]1.0 mM
2ADENOSINE-5'-TRIPHOSPHATE[U-95% 13C; U-95% 15N]1.5 mM

LACS Plot; CA
Referencing offset: -0.02 ppm, Outliers: 1 Detail
LACS Plot; CB
Referencing offset: -0.02 ppm, Outliers: 1 Detail
LACS Plot; HA
Referencing offset: 0.05 ppm, Outliers: 1 Detail
LACS Plot; CO
Referencing offset: -0.07 ppm, Outliers: 2 Detail
Protein Blocks Logo
Calculated from 39 models in PDB: 1XSB, Strand ID: A Detail


Release date
2005-11-13
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 ,
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 ,
Entries sharing articles BMRB: 1, Swiss-Prot: 1 entries Detail
  BMRB: 6330 released on 2004-12-21
    Title Solution structure of human AP4A hydrolase
  Swiss-Prot: P50583 released on 1996-10-01
    Title AP4A_HUMAN Entity Bis(5'-nucleosyl)-tetraphosphatase [asymmetrical]
Related entities 1. AP4A, : 1 : 2 : 5 : 31 entities Detail
Interaction partners 1. AP4A, : 2 interactors Detail
Experiments performed 1 experiments Detail
nullKeywords NMR nudix assignment AP4A