BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 15088

Title: Northeast Structural Genomics Consortium Target ER411

Authors: Tian, Fang; Prestegard, Jim; Zhao, Li; Jiang, Mei; Cunningham, Kellie; Ma, Li-Chung; Xiao, Rong; Liu, Jinfeng; Baran, Michael; Swapna, G.V.T.; Acton, Thomas; Rost, Burkhard; Monteline, Gaetano

Citation: Tian, Fang; Prestegard, Jim; Monteline, Gaetano. "NMR solution structure of E.Coli hypothetical protein YFJZ"  . ., .-..

Assembly members:
ER411, polymer, 113 residues, 11754.372 Da.

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

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

Entity Sequences (FASTA):
ER411: MSNTTWGLQRDITPRLGARL VQEGNQLHYLADRASITGKF SDAECPKLDVVFPHFISQIE SMLTTGELNPRHAQCVTLYH NGFTCEADTLGSCGYVYIAV YPTQRLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts287
15N chemical shifts98
1H chemical shifts634
residual dipolar couplings249

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1ER4111

Entities:

Entity 1, ER411 113 residues - 11754.372 Da.

1   METSERASNTHRTHRTRPGLYLEUGLNARG
2   ASPILETHRPROARGLEUGLYALAARGLEU
3   VALGLNGLUGLYASNGLNLEUHISTYRLEU
4   ALAASPARGALASERILETHRGLYLYSPHE
5   SERASPALAGLUCYSPROLYSLEUASPVAL
6   VALPHEPROHISPHEILESERGLNILEGLU
7   SERMETLEUTHRTHRGLYGLULEUASNPRO
8   ARGHISALAGLNCYSVALTHRLEUTYRHIS
9   ASNGLYPHETHRCYSGLUALAASPTHRLEU
10   GLYSERCYSGLYTYRVALTYRILEALAVAL
11   TYRPROTHRGLNARGLEUGLUHISHISHIS
12   HISHISHIS

Samples:

sample_1: ER411, [U-100% 13C; U-100% 15N], 1.1 mM; sodium azide 0.02%; TRIS 10 mM; sodium chloride 100 mM; H2O 90%; D2O 10%

sample_2: ER411, [U-100% 13C; U-100% 15N], 0.5 mM; sodium azide 0.02%; TRIS 10 mM; sodium chloride 250 mM; Pf1 phage 5 mg; H2O 90%; D2O 10%

sample_conditions_1: pH: 6.5; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY (aliph)sample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2anisotropicsample_conditions_1
3D 1H-13C NOESY (arom)sample_1isotropicsample_conditions_1

Software:

FELIX v2004, Accelrys Software Inc. - data analysis

X-PLOR NIH v2.15, Schwieters, Kuszewski, Tjandra and Clore - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Varian INOVA 900 MHz

Related Database Links:

SWS P52141
PDB 2EA9 2JN7
DBJ BAA16513 BAJ44421
EMBL CDJ74165 CDY60737 CDZ21454 CQR82105 CUH56935
GB AAA79813 AAC75693 ACB03787 ACR62618 ACX38708
REF NP_417132 WP_000072689 WP_000072690 WP_001698961 WP_047666283
SP P52141