BMRB Entry 5354

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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/BMR5354
MolProbity Validation Chart

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Title:
Structure and Interactions of PAS kinase N-terminal PAS domain: Model for intramolecular kinase regulation
Deposition date:
2002-04-26
Original release date:
2003-01-27
Authors:
Amezcua, Carlos; Harper, Shannon; Rutter, Jared; Gardner, Kevin
Citation:

Citation: Amezcua, Carlos; Harper, Shannon; Rutter, Jared; Gardner, Kevin. "Structure and Interactions of PAS kinase N-terminal PAS domain: Model for Intramolecular Kinase Regulation"  Structure 10, 1349-1361 (2002).
PubMed: 12377121

Assembly members:

Assembly members:
PAS Kinase PAS-A domain, polymer, 114 residues, 12644.5 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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PAS Kinase PAS-A domain: GAMDPEFNKAIFTVDAKTTE ILVANDKACGLLGYSSQDLI GQKLTQFFLRSDSDVVEALS EEHMEADGHAAVVFGTVVDI ISRSGEKIPVSVWMKRMRQE RRLCCVVVLEPVER

Data sets:
Data typeCount
15N chemical shifts120
1H chemical shifts808
13C chemical shifts502

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1PAS Kinase PAS-A1

Entities:

Entity 1, PAS Kinase PAS-A 114 residues - 12644.5 Da.

1   GLYALAMETASPPROGLUPHEASNLYSALA
2   ILEPHETHRVALASPALALYSTHRTHRGLU
3   ILELEUVALALAASNASPLYSALACYSGLY
4   LEULEUGLYTYRSERSERGLNASPLEUILE
5   GLYGLNLYSLEUTHRGLNPHEPHELEUARG
6   SERASPSERASPVALVALGLUALALEUSER
7   GLUGLUHISMETGLUALAASPGLYHISALA
8   ALAVALVALPHEGLYTHRVALVALASPILE
9   ILESERARGSERGLYGLULYSILEPROVAL
10   SERVALTRPMETLYSARGMETARGGLNGLU
11   ARGARGLEUCYSCYSVALVALVALLEUGLU
12   PROVALGLUARG

Samples:

sample_1: PAS Kinase PAS-A domain, [U-15N; U-13C], 0.8 – 1.2 mM

experimental_conditions: pH: 6.5; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
1H-15N HSQCsample_1not availableexperimental_conditions
1H-13C HSQCsample_1not availableexperimental_conditions
HNCACBsample_1not availableexperimental_conditions
CBCA(CO)NHsample_1not availableexperimental_conditions
HNCOsample_1not availableexperimental_conditions
C(CO)NNH TOCSYsample_1not availableexperimental_conditions
H(CCO)NNH TOCSYsample_1not availableexperimental_conditions
HCCH TOCSYsample_1not availableexperimental_conditions
1H-1H TOCSYsample_1not availableexperimental_conditions
DQF COSYsample_1not availableexperimental_conditions
HNHAsample_1not availableexperimental_conditions
1H-1H NOESYsample_1not availableexperimental_conditions
15N-Edited NOESYsample_1not availableexperimental_conditions
13C,15N-Edited NOESYsample_1not availableexperimental_conditions
1H-15N IPAPsample_1not availableexperimental_conditions

Software:

NMRVIEW v5.04 - Data Analysis

NMRPipe - Data Processing

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Varian INOVA 500 MHz

Related Database Links:

PDB
DBJ BAA09484 BAG09616 BAH13702
EMBL CAH18087
GB AAH50565 AAH63585 AAK69752 EAW71236 EAW71237
REF NP_001239048 NP_001239049 NP_001239051 NP_001239053 NP_055963
SP Q96RG2
AlphaFold Q96RG2

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