BMRB Entry 6152

Title:
Solution structure of TIP-B1
Deposition date:
2004-03-19
Original release date:
2004-05-15
Authors:
Xu, Chao; Tang, Yajun; Xu, Yingqi; Wu, Jihui; Shi, Yunyu; Zhang, Qinghua; Zheng, Peicheng; Du, Yanzhi
Citation:

Citation: Xu, C.; Tang, Y.; Xu, Y.; Wu, J.; Shi, Y.; Zhang, Q.; Zheng, P.; Du, Y.. "Solution structure of recombinant TIP-B1, a novel TNF inhibitory protein"  The BMRB entry is the only known published source for the data..

Assembly members:

Assembly members:
TUMOR INHIBITORY PROTIEIN;SH3 domain binding glutamic acid-rich protein-like 3, polymer, 101 residues, Formula weight is not available

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
TUMOR INHIBITORY PROTIEIN;SH3 domain binding glutamic acid-rich protein-like 3: MSGLRVYSTSVTGSREIKSQ QSEVTRILDGKRIQYQLVDI SQDNALRDEMRALAGNPKAT PPQIVNGDQYCGDYELFVEA VEQNTLQEFLKLALEHHHHH H

Data sets:
Data typeCount
1H chemical shifts612
13C chemical shifts392
15N chemical shifts101

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1TIP, momomer1

Entities:

Entity 1, TIP, momomer 101 residues - Formula weight is not available

1   METSERGLYLEUARGVALTYRSERTHRSER
2   VALTHRGLYSERARGGLUILELYSSERGLN
3   GLNSERGLUVALTHRARGILELEUASPGLY
4   LYSARGILEGLNTYRGLNLEUVALASPILE
5   SERGLNASPASNALALEUARGASPGLUMET
6   ARGALALEUALAGLYASNPROLYSALATHR
7   PROPROGLNILEVALASNGLYASPGLNTYR
8   CYSGLYASPTYRGLULEUPHEVALGLUALA
9   VALGLUGLNASNTHRLEUGLNGLUPHELEU
10   LYSLEUALALEUGLUHISHISHISHISHIS
11   HIS

Samples:

sample_1: TUMOR INHIBITORY PROTIEIN;SH3 domain binding glutamic acid-rich protein-like 3, [U-95% 13C; U-90% 15N], 2 mM; phosphate buffer 20 mM; NaCl 100 mM; H2O 90%; D2O 10%

sample_cond_1: pH: 7.0; temperature: 295 K; ionic strength: 120 mM; pressure: 1 atm

Experiments:

NameSampleSample stateSample conditions
2D NOESYsample_1not availablesample_cond_1
3D HCCH COSYsample_1not availablesample_cond_1
3D 13C-separated NOESYsample_1not availablesample_cond_1
3D 15N-separated NOESYsample_1not availablesample_cond_1
3D CBCA(CO)NHsample_1not availablesample_cond_1
3D CBCANHsample_1not availablesample_cond_1
3D HNCOsample_1not availablesample_cond_1
3D H(CCO)NH TOCSYsample_1not availablesample_cond_1
3D C(CO)NH TOCSYsample_1not availablesample_cond_1
3D HCCH TOCSYsample_1not availablesample_cond_1

Software:

NMRPipe v2.2 - processing

CNS v1.1 - structure solution, refinement

sparky vSPARKY3 - data analysis

NMR spectrometers:

  • Bruker DMX 600 MHz

Related Database Links:

PDB
DBJ BAE88615
EMBL CAC35770 CAH90649
GB AAG41412 AAH30135 AAI02049 AAI67002 AAL95695
REF NP_001029935 NP_001100158 NP_001125350 NP_001229384 NP_112576
SP Q3ZCL8 Q5RC61 Q9H299
TPG DAA32143
AlphaFold Q3ZCL8 Q5RC61 Q9H299

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