BMRB Entry 16189

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16189
MolProbity Validation Chart

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Title:
Structure of the amino-terminal domain of human FK506-binding protein 3 / Northeast Structural Genomics Consortium Target HT99A
Deposition date:
2009-02-27
Original release date:
2010-11-10
Authors:
Sunnerhagen, Maria; Davis, T. L.; Gutmanas, Alexandras; Fares, Christophe; Ouyang, Hui; Lemak, Alexander; Li, Y.; Weigelt, Johan; Bountra, C.; Edwards, A. M.; Arrowsmith, Cheryl; Dhe Paganon, Sirano
Citation:

Citation: Sunnerhagen, Maria. "Structure of the N-terminal domain of FK506-binding protein 3."  .

Assembly members:

Assembly members:
FKBP3-N, polymer, 92 residues, 8417.787 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: recombinant technology   Host organism: Escherichia coli   Vector: pET28aLIC

Entity Sequences (FASTA):

Entity Sequences (FASTA):
FKBP3-N: MGSSHHHHHHSSGLVPRGSM AAAVPQRAWTVEQLRSEQLP KKDIIKFLQEHGSDSFLAEH KLLGNIKNVAKTANKDHLVT AYNHLFETKRFK

Data sets:
Data typeCount
13C chemical shifts325
15N chemical shifts75
1H chemical shifts518

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1FKBP3-N1

Entities:

Entity 1, FKBP3-N 92 residues - 8417.787 Da.

Residues 1-19 represent a non-native affinity tag. Residues 20-92 represent residues 1-73 of the intact FK506-binding protein 3.

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYLEUVALPROARGGLYSERMET
3   ALAALAALAVALPROGLNARGALATRPTHR
4   VALGLUGLNLEUARGSERGLUGLNLEUPRO
5   LYSLYSASPILEILELYSPHELEUGLNGLU
6   HISGLYSERASPSERPHELEUALAGLUHIS
7   LYSLEULEUGLYASNILELYSASNVALALA
8   LYSTHRALAASNLYSASPHISLEUVALTHR
9   ALATYRASNHISLEUPHEGLUTHRLYSARG
10   PHELYS

Samples:

sample_1: FKBP3-N, [U-100% 13C; U-100% 15N], 12.5 mg/ml; TRIS 10 mM; NaCl 500 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.5 M; pH: 7.0; pressure: 1 atm; temperature: 398 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D IPAP HNCOsample_1anisotropicsample_conditions_1

Software:

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

MDD_NMR, Orekhov V - processing

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - MD water refinement

ABACUS, Alexander Lemak - chemical shift assignment, noe assignment

NMR spectrometers:

  • Varian INOVA 500 MHz
  • Bruker Avance 800 MHz

Related Database Links:

BMRB 19551
PDB
DBJ BAA24412 BAD96713 BAE01700 BAE87176 BAG34856
GB AAA30348 AAA58471 AAA58474 AAA58475 AAH16288
REF NP_001033201 NP_001100206 NP_001231086 NP_001270679 NP_002004
SP O46638 P26884 Q00688
TPG DAA17319
AlphaFold O46638 P26884 Q00688

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks