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 15804

Title: Solution NMR Structure of M. thermoautotrophicum protein MTH_1000, Northeast Structural Genomics Consortium Target TR8

Authors: Eletsky, Alexander; Sukumaran, Dinesh; Semesi, Anthony; Guido, Valerie; Yee, Adelinda; Arrowsmith, Cheryl; Szyperski, Thomas

Citation: Eletsky, Alexander; Sukumaran, Dinesh; Semesi, Anthony; Guido, Valerie; Yee, Adelinda; Arrowsmith, Cheryl; Szyperski, Thomas. "Solution NMR Structure of M. thermoautotrophicum protein MTH_1000, Northeast Structural Genomics Consortium Target TR8"  Proteins: Struct. Funct. Genet. ., .-..

Assembly members:
TR8_protein, polymer, 153 residues, 17284.062 Da.

Natural source:   Common Name: Methanobacterium thermoautotrophicum   Taxonomy ID: 145262   Superkingdom: Archaea   Kingdom: not available   Genus/species: Methanobacterium thermoautotrophicum

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

Entity Sequences (FASTA):
TR8_protein: MGSSHHHHHHSSGLVPRGSH MWNDLAVYIIRCSGPGTRVV EVGAGRFLYVSDYIRKHSKV DLVLTDIKPSHGGIVRDDIT SPRMEIYRGAALIYSIRPPA EIHSSLMRVADAVGARLIIK PLTGEDIVTERKMKLVNYGR TYFYEYIAEVRSR

Data sets:
Data typeCount
13C chemical shifts613
15N chemical shifts136
1H chemical shifts989

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1TR8_protein1

Entities:

Entity 1, TR8_protein 153 residues - 17284.062 Da.

20-residue N-terminal tag MGSSHHHHHHSSGLVPRGSH

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYLEUVALPROARGGLYSERHIS
3   METTRPASNASPLEUALAVALTYRILEILE
4   ARGCYSSERGLYPROGLYTHRARGVALVAL
5   GLUVALGLYALAGLYARGPHELEUTYRVAL
6   SERASPTYRILEARGLYSHISSERLYSVAL
7   ASPLEUVALLEUTHRASPILELYSPROSER
8   HISGLYGLYILEVALARGASPASPILETHR
9   SERPROARGMETGLUILETYRARGGLYALA
10   ALALEUILETYRSERILEARGPROPROALA
11   GLUILEHISSERSERLEUMETARGVALALA
12   ASPALAVALGLYALAARGLEUILEILELYS
13   PROLEUTHRGLYGLUASPILEVALTHRGLU
14   ARGLYSMETLYSLEUVALASNTYRGLYARG
15   THRTYRPHETYRGLUTYRILEALAGLUVAL
16   ARGSERARG

Samples:

NC: TR8 protein, [U-100% 13C; U-100% 15N], 0.8 mM; sodium phosphate 10 mM; sodium chloride 300 mM; benzamidine 1 mM; DTT 10 mM

NC5: TR8 protein, [U-5% 13C; U-100% 15N], 0.8 mM; sodium phosphate 10 mM; sodium chloride 450 mM; benzamidine 1 mM; DTT 10 mM

sample_conditions_NC: ionic strength: 300 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

sample_conditions_NC5: ionic strength: 450 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCNCisotropicsample_conditions_NC
2D 1H-13C HSQCNCisotropicsample_conditions_NC
3D HNCONCisotropicsample_conditions_NC
3D HNCACBNCisotropicsample_conditions_NC
3D HNCANCisotropicsample_conditions_NC
3D CBCA(CO)NHNCisotropicsample_conditions_NC
3D HBHA(CO)NHNCisotropicsample_conditions_NC
3D 1H-15N,13Cali,13Caro NOESYNCisotropicsample_conditions_NC
3D HCCH-COSY aliphaticNCisotropicsample_conditions_NC
3D HCCH-TOCSY aliphaticNCisotropicsample_conditions_NC
3D HCCH-COSY aromaticNCisotropicsample_conditions_NC
2D 1H-13C HSQC methylNC5isotropicsample_conditions_NC5
2D LR 1H-15N HSQC (His)NC5isotropicsample_conditions_NC5

Software:

TOPSPIN v1.3, Bruker Biospin - collection, processing

VNMR v6.1C, Varian - collection

VNMRJ v2.1B, Varian - collection

PROSA v6.0.2, Guntert - processing

XEASY v1.3.13, Bartels et al. - data analysis

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

CSI v2.0, Wishart and Sykes - data analysis

TALOS v2003.027.13.05, Cornilescu, Delaglio and Bax - data analysis

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - structure solution

AutoAssign v1.15.1, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

PSVS, Bhattacharya and Montelione - structure validation

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Varian INOVA 600 MHz
  • Varian INOVA 750 MHz

Related Database Links:

PDB
GB AAB85479
REF WP_010876631
SP O27081