Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15520
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Citation: Religa, Tomasz; Markson, Joseph; Mayor, Ugo; Freund, Stefan; Fersht, Alan. "Solution Structure of a Protein Denatured State and Folding Intermediate." Nature 437, 1053-1056 (2005).
PubMed: 16222301
Assembly members:
SEGMENTATION_POLARITY_HOMEOBOX_PROTEIN_ENGRAILED, polymer, 61 residues, 7337.3 Da.
Natural source: Common Name: FRUIT FLY Taxonomy ID: 7227 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: DROSOPHILA MELANOGASTER
Experimental source: Production method: recombinant technology Host organism: ESCHERICHIA COLI Vector: PRSET
Entity Sequences (FASTA):
SEGMENTATION_POLARITY_HOMEOBOX_PROTEIN_ENGRAILED: GDEKRPRTAFSSEQLARAKR
EFNENRYLTERRRQQLSSEL
GLNEAQIKIWFQNKRAKIKK
S
Data type | Count |
13C chemical shifts | 163 |
15N chemical shifts | 58 |
1H chemical shifts | 454 |
coupling constants | 51 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | SEGMENTATION POLARITY HOMEOBOX PROTEIN ENGRAILED | 1 |
Entity 1, SEGMENTATION POLARITY HOMEOBOX PROTEIN ENGRAILED 61 residues - 7337.3 Da.
1 | GLY | ASP | GLU | LYS | ARG | PRO | ARG | THR | ALA | PHE | ||||
2 | SER | SER | GLU | GLN | LEU | ALA | ARG | ALA | LYS | ARG | ||||
3 | GLU | PHE | ASN | GLU | ASN | ARG | TYR | LEU | THR | GLU | ||||
4 | ARG | ARG | ARG | GLN | GLN | LEU | SER | SER | GLU | LEU | ||||
5 | GLY | LEU | ASN | GLU | ALA | GLN | ILE | LYS | ILE | TRP | ||||
6 | PHE | GLN | ASN | LYS | ARG | ALA | LYS | ILE | LYS | LYS | ||||
7 | SER |
15N: SEGMENTATION POLARITY HOMEOBOX PROTEIN ENGRAILED, [U-15N], 500 uM; D-ACETATE 50 mM; NACL 100 mM; D2O 7%; H2O 93%
15N_PheTyr-H: SEGMENTATION POLARITY HOMEOBOX PROTEIN ENGRAILED, [U-15N; U-2H] [U-15N; U-1H]-Phe,Trp, 500 uM; D-ACETATE 50 mM; NACL 100 mM; D2O 7%; H2O 93%
15N_U-D: SEGMENTATION POLARITY HOMEOBOX PROTEIN ENGRAILED, [U-15N; U-2H], 500 uM; D-ACETATE 50 mM; NACL 100 mM; D2O 7%; H2O 93%
13C15N: SEGMENTATION POLARITY HOMEOBOX PROTEIN ENGRAILED, [U-13C; U-15N], 500 uM; D-ACETATE 50 mM; NACL 100 mM; D2O 7%; H2O 93%
sample_conditions_1: ionic strength: 150 mM; pH: 5.7; pressure: 1 atm; temperature: 278 K
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D NOESY | 15N | isotropic | sample_conditions_1 |
3D_15N-SEPARATED_ NOESY | 15N_PheTyr-H | isotropic | sample_conditions_1 |
HSQC-NOESY-HSQC, 600MS MIXING TIME | 15N_U-D | isotropic | sample_conditions_1 |
3D_13C-SEPARATED_ NOESY | 13C15N | isotropic | sample_conditions_1 |
3D HNHA | 15N | isotropic | sample_conditions_1 |
NMRPIPE 2004-04-12 v2004-04-12, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - structure solution
SPARKY v3.106, Goddard - structure solution
CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution
PDB | |
BMRB | 15536 |
DBJ | BAN82729 BAN82730 BAN82731 |
EMBL | CAA28436 |
GB | AAA65478 AAF58639 AAL39593 AAM68711 ACL84189 |
REF | NP_523700 NP_725059 XP_001958778 XP_001976053 XP_002006437 |
SP | P02836 P09145 |
AlphaFold | P02836 P09145 |
Download HSQC peak lists in one of the following formats:
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or all simulated peaks