BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 18714

Title: Solution NMR Structure of Homeobox 2 Domain from Human ZHX1 repressor, Northeast Structural Genomics Consortium (NESG) Target HR7907F

Authors: Xu, Xianzhong; Eletsky, Alexander; Mills, Jeffrey; Pulavarti, Surya; Lee, Dan; Kohan, Eitan; Janjua, Haleema; Xiao, Rong; Acton, Thomas; Everett, John; Montelione, Gaetano; Szyperski, Thomas

Citation: Xu, Xianzhong; Eletsky, Alexander; Mills, Jeffrey; Pulavarti, Surya; Lee, Dan; Kohan, Eitan; Janjua, Haleema; Xiao, Rong; Acton, Thomas; Everett, John; Montelione, Gaetano; Szyperski, Thomas. "Solution NMR Structure of Homeobox 2 Domain from Human ZHX1 repressor, Northeast Structural Genomics Consortium (NESG) Target HR7907F"  To be published ., .-..

Assembly members:
HR7907F, polymer, 74 residues, 8710.092 Da.

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
HR7907F: SHMPDSFGIRAKKTKEQLAE LKVSYLKNQFPHDSEIIRLM KITGLTKGEIKKWFSDTRYN QRNSKSNQCLHLNN

Data sets:
Data typeCount
13C chemical shifts332
15N chemical shifts83
1H chemical shifts537

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1HR7907F1

Entities:

Entity 1, HR7907F 74 residues - 8710.092 Da.

Residues 4-74 correspond to residues 462-532 of the native protein. Residues 1-3 represent the remainder of the affinity tag.

1   SERHISMETPROASPSERPHEGLYILEARG
2   ALALYSLYSTHRLYSGLUGLNLEUALAGLU
3   LEULYSVALSERTYRLEULYSASNGLNPHE
4   PROHISASPSERGLUILEILEARGLEUMET
5   LYSILETHRGLYLEUTHRLYSGLYGLUILE
6   LYSLYSTRPPHESERASPTHRARGTYRASN
7   GLNARGASNSERLYSSERASNGLNCYSLEU
8   HISLEUASNASN

Samples:

NC: HR7907F, [U-100% 13C; U-100% 15N], 0.4 mM; sodium azide 0.02%; DTT 10 mM; calcium chloride 5 mM; sodium chloride 100 mM; Proteinase Inhibitors 1 x; MES 20 mM; DSS 50 uM; H2O 90%; D2O 10%

NC5: HR7907F, [5% 13C; U-100% 15N], 0.3 mM; sodium azide 0.02%; DTT 10 mM; calcium chloride 5 mM; sodium chloride 100 mM; Proteinase Inhibitors 1 x; MES 20 mM; DSS 50 uM; H2O 90%; D2O 10%

Conditions_1: pH: 6.5; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCNCisotropicConditions_1
2D 1H-13C HSQCNCisotropicConditions_1
3D HNCONCisotropicConditions_1
(4,3)D GFT CABCA(CO)NHNNCisotropicConditions_1
(4,3)D GFT HNNCABCANCisotropicConditions_1
2D 1H-13C HSQCNC5isotropicConditions_1
(4,3)D GFT HCCH-COSY alipahticNCisotropicConditions_1
3D (H)CCH-TOCSY aliphaticNCisotropicConditions_1
3D 13C/15N-edited NOESYNCisotropicConditions_1
(4,3)D GFT HABCAB(CO)NHNCisotropicConditions_1
3D (H)CCH-COSY aromaticNCisotropicConditions_1

Software:

CARA v1.8.4, Keller and Wuthrich - chemical shift assignment, peak picking

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - refinement,geometry optimization,structure solution

AS-DP v1.0, Huang, Tejero, Powers and Montelione - data analysis,refinement

AutoAssign v2.3.0, Zimmerman, Moseley, Kulikowski and Montelione - data analysis,chemical shift assignment

XEASY, Bartels et al. - data analysis

VNMRJ, Varian - collection

TALOS+, Shen, Cornilescu, Delaglio and Bax - geometry optimization

PSVS, Bhattacharya, Montelione - structure validation

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Varian INOVA 750 MHz

Related Database Links:

UNP Q9UKY1
PDB