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- PDB-1ygw: NMR STRUCTURE OF RIBONUCLEASE T1, 34 STRUCTURES -

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Basic information

Entry
Database: PDB / ID: 1ygw
TitleNMR STRUCTURE OF RIBONUCLEASE T1, 34 STRUCTURES
ComponentsRIBONUCLEASE T1
KeywordsHYDROLASE / RIBONUCLEASE / ENDONUCLEASE / RIBONUCLEASE T1 PRECURSOR / ENDORIBONUCLEASE
Function / homology
Function and homology information


hyphal tip / ribonuclease T1 activity / ribonuclease T1 / cell septum / endonuclease activity / lyase activity / RNA binding
Similarity search - Function
: / ribonuclease / Microbial ribonucleases / Ribonuclease/ribotoxin / Nuclear Transport Factor 2; Chain: A, / Roll / Alpha Beta
Similarity search - Domain/homology
Guanyl-specific ribonuclease T1
Similarity search - Component
Biological speciesAspergillus oryzae (mold)
MethodSOLUTION NMR / VARIABLE TARGET FUNCTION
AuthorsPfeiffer, S. / Karimi-Nejad, Y. / Ruterjans, H.
Citation
Journal: J.Mol.Biol. / Year: 1997
Title: Limits of NMR structure determination using variable target function calculations: ribonuclease T1, a case study.
Authors: Pfeiffer, S. / Karimi-Nejad, Y. / Ruterjans, H.
#1: Journal: Q.Magn.Reson.Biol.Med. / Year: 1996
Title: Complete 1H, 15N and 13C Resonance Assignment of Ribonuclease T1: Secondary Structure and Backbone Dynamics as Derived from the Chemical Shifts
Authors: Pfeiffer, S. / Engelke, J. / Ruterjans, H.
#2: Journal: Biochemistry / Year: 1994
Title: Conformation of Valine Side Chains in Ribonuclease T1 Determined by NMR Studies of Homonuclear and Heteronuclear 3J Coupling Constants
Authors: Karimi-Nejad, Y. / Schmidt, J.M. / Ruterjans, H. / Schwalbe, H. / Griesinger, C.
History
DepositionSep 28, 1996Processing site: BNL
Revision 1.0Oct 8, 1997Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Nov 29, 2017Group: Derived calculations / Other
Category: pdbx_database_status / pdbx_struct_assembly ...pdbx_database_status / pdbx_struct_assembly / pdbx_struct_oper_list / struct_conf / struct_conf_type
Item: _pdbx_database_status.process_site

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: RIBONUCLEASE T1


Theoretical massNumber of molelcules
Total (without water)11,0951
Polymers11,0951
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_5551
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)34 / 50SEE JRNL REFERENCE
Representative

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Components

#1: Protein RIBONUCLEASE T1 / / GUANYLORIBONUCLEASE / RNASE T1


Mass: 11094.694 Da / Num. of mol.: 1 / Mutation: ISOENZYME WITH LYSINE AT POSITION 25
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Aspergillus oryzae (mold) / Gene: RIBONUCLEASE T1 / Plasmid: PA2T1-1 / Gene (production host): RIBONUCLEASE T1 / Production host: Escherichia coli (E. coli) / Strain (production host): DH5 ALPHA / References: UniProt: P00651, EC: 3.1.27.3

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR

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Sample preparation

Sample conditionspH: 5.5 / Temperature: 313 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker AMXBrukerAMX6001
Bruker DMXBrukerDMX6002

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Processing

NMR software
NameDeveloperClassification
DIANAWUTHRICHrefinement
DIANAstructure solution
RefinementMethod: VARIABLE TARGET FUNCTION / Software ordinal: 1
NMR ensembleConformer selection criteria: SEE JRNL REFERENCE / Conformers calculated total number: 50 / Conformers submitted total number: 34

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