BMRB Entry 6620

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR6620
MolProbity Validation Chart

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Title:
1H, 13C, and 15N Chemical Shift Assignments for murine p22HBP
Deposition date:
2005-05-05
Original release date:
2005-10-10
Authors:
Dias, Jorge; Macedo, Anjos; Ferreira, Gloria; Jeanty, Naomi; Taketani, Shigeru; Goodfellow, Brian; Peterson, Francis; Volkman, Brian
Citation:

Citation: Dias, Jorge; Macedo, Anjos; Ferreria, Gloria; Peterson, Francis; Volkman, Brian; Goodfellow, Brian. "The first structure from the soul/HBP family of heme binding proteins: Murine P22HBP."  J. Biol. Chem 281, 31553-31561 (2006).
PubMed: 16905545

Assembly members:

Assembly members:
murine heme binding protein p22HBP, polymer, 195 residues, 21053 Da.

Natural source:

Natural source:   Common Name: mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus Mus musculus

Experimental source:

Experimental source:   Production method: recombinant technology

Entity Sequences (FASTA):

Entity Sequences (FASTA):
murine heme binding protein p22HBP: MKQSTHHHHIHNSLFGSVET WPWQVLSTGGKEDVSYEERA CEGGKFATVEVTDKPVDEAL REAMPKIMKYVGGTNDKGVG MGMTVPVSFAVFPNEDGSLQ KKLKVWFRIPNQFQGSPPAP SDESVKIEEREGITVYSTQF GGYAKEADYVAHATQLRTTL EGTPATYQGDVYYCAGYDPP MKPYGRRNEVWLVKA

Data sets:
Data typeCount
13C chemical shifts470
15N chemical shifts154
1H chemical shifts939

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1monomer1

Entities:

Entity 1, monomer 195 residues - 21053 Da.

Taketani,S., Adachi,Y., Kohno,H., Ikehara,S., Tokunaga,R. and Ishii,T.: Molecular characterization of a newly identified heme-binding protein induced during differentiation of murine erythroleukemia cells: J. Biol. Chem. 273 (47), 31388-31394 (1998)

1   METLYSGLNSERTHRHISHISHISHISILE
2   HISASNSERLEUPHEGLYSERVALGLUTHR
3   TRPPROTRPGLNVALLEUSERTHRGLYGLY
4   LYSGLUASPVALSERTYRGLUGLUARGALA
5   CYSGLUGLYGLYLYSPHEALATHRVALGLU
6   VALTHRASPLYSPROVALASPGLUALALEU
7   ARGGLUALAMETPROLYSILEMETLYSTYR
8   VALGLYGLYTHRASNASPLYSGLYVALGLY
9   METGLYMETTHRVALPROVALSERPHEALA
10   VALPHEPROASNGLUASPGLYSERLEUGLN
11   LYSLYSLEULYSVALTRPPHEARGILEPRO
12   ASNGLNPHEGLNGLYSERPROPROALAPRO
13   SERASPGLUSERVALLYSILEGLUGLUARG
14   GLUGLYILETHRVALTYRSERTHRGLNPHE
15   GLYGLYTYRALALYSGLUALAASPTYRVAL
16   ALAHISALATHRGLNLEUARGTHRTHRLEU
17   GLUGLYTHRPROALATHRTYRGLNGLYASP
18   VALTYRTYRCYSALAGLYTYRASPPROPRO
19   METLYSPROTYRGLYARGARGASNGLUVAL
20   TRPLEUVALLYSALA

Samples:

15N_13C: murine heme binding protein p22HBP, [U-15N; U-13C], 1 mM; phosphate buffer 50 mM; KCL 100 mM

15N_13C_2H_50%: murine heme binding protein p22HBP, [U-15N; U-13C, U-50% 2H], 1 mM; phosphate buffer 50 mM; KCL 100 mM

15N: murine heme binding protein p22HBP, [U-15N], 1 mM; phosphate buffer 50 mM; KCL 100 mM

15N_13C_2H_100%: murine heme binding protein p22HBP, [U-15N; U-13C; U-2H], 1 mM; phosphate buffer 50 mM; KCL 100 mM

conditions_1: ionic strength: 0.1 M; pH: 8.0; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H15N HSQC15N_13Cnot availableconditions_1
2D 1H15N TROSY15N_13Cnot availableconditions_1
3D trHNCACB15N_13Cnot availableconditions_1
3D trHNCOCACB15N_13Cnot availableconditions_1
3D trHNCA15N_13Cnot availableconditions_1
3D trHNCOCA15N_13Cnot availableconditions_1
3D HCCH_TOCSY15N_13Cnot availableconditions_1
3D 15N HSQC-NOESY15N_13Cnot availableconditions_1
3D 15N HSQC-TOCSY15Nnot availableconditions_1
3D 13C HSQC-NOESY15N_13Cnot availableconditions_1
3D trHNCO15N_13C_2H_100%not availableconditions_1
3D trHNCACO15N_13C_2H_100%not availableconditions_1

Software:

NMRPipe - nmr data processing

XEASY - resonance assignment

xwinnmr v3.1 - data acquisition and processing

NMR spectrometers:

  • Bruker DRX600 600MHz MHz

Related Database Links:

BMRB 17953 7231
PDB
DBJ BAA33770
EMBL CAJ18470
GB AAD32096 AAH12654 AAI68221 EDL10544 EDM01631
REF NP_001102121 NP_038574 XP_006237591
SP Q9R257
AlphaFold Q9R257

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