BMRB Entry 16033

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16033
MolProbity Validation Chart

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Title:
Solution structure and dynamics of S100A5 in the apo states
Deposition date:
2008-11-17
Original release date:
2009-06-24
Authors:
Bertini, Ivano; Das Gupta, Soumyasr; Hu, Xiaoyu; Karavelas, Tilemachos; Luchinat, Claudio; Parigi, Giacomo; Yuan, Jing
Citation:

Citation: Bertini, Ivano; Das Gupta, Soumyasri; Hu, Xiaoyu; Karavelas, Tilemachos; Luchinat, Claudio; Parigi, Giacomo; Yuan, Jing. "Solution structure and dynamics of S100A5 in the apo and Ca2+-bound states."  J. Biol. Inorg. Chem. 14, 1097-1107 (2009).
PubMed: 19536568

Assembly members:

Assembly members:
S100A5, polymer, 92 residues, 10759.492 Da.

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Eubacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET21a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
S100A5: METPLEKALTTMVTTFHKYS GREGSKLTLSRKELKELIKK ELCLGEMKESSIDDLMKSLD KNSDQEIDFKEYSVFLTMLC MAYNDFFLEDNK

Data sets:
Data typeCount
13C chemical shifts392
15N chemical shifts92
1H chemical shifts676
heteronuclear NOE values76
T1 relaxation values67
T2 relaxation values67

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_21

Entities:

Entity 1, entity_1 92 residues - 10759.492 Da.

1   METGLUTHRPROLEUGLULYSALALEUTHR
2   THRMETVALTHRTHRPHEHISLYSTYRSER
3   GLYARGGLUGLYSERLYSLEUTHRLEUSER
4   ARGLYSGLULEULYSGLULEUILELYSLYS
5   GLULEUCYSLEUGLYGLUMETLYSGLUSER
6   SERILEASPASPLEUMETLYSSERLEUASP
7   LYSASNSERASPGLNGLUILEASPPHELYS
8   GLUTYRSERVALPHELEUTHRMETLEUCYS
9   METALATYRASNASPPHEPHELEUGLUASP
10   ASNLYS

Samples:

sample_1: entity, [U-100% 15N], 0.4 mM; NaCl 100 mM

sample_2: entity, [U-100% 13C; U-100% 15N], 0.4 mM; NaCl 100 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
1H-15N NOEsample_1isotropicsample_conditions_1
15N R1sample_1isotropicsample_conditions_1
15N R2sample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

CARA v2.0, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

AMBER, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - refinement

NMR spectrometers:

  • Bruker Avance 900 MHz
  • Bruker Avance 700 MHz
  • Bruker Avance 500 MHz

Related Database Links:

BMRB 16034
PDB
EMBL CAA79472 CAA79475 CAA79479
GB AAH93955 AAH93957 EAW53316 EAW53317
PIR B48219
REF NP_002953 XP_001138899 XP_003817219 XP_004436112 XP_005610168
SP P33763
AlphaFold P33763

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