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- PDB-1ctl: STRUCTURE OF THE CARBOXY-TERMINAL LIM DOMAIN FROM THE CYSTEINE RI... -

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Basic information

Entry
Database: PDB / ID: 1ctl
TitleSTRUCTURE OF THE CARBOXY-TERMINAL LIM DOMAIN FROM THE CYSTEINE RICH PROTEIN CRP
ComponentsAVIAN CYSTEINE RICH PROTEIN
KeywordsMETAL BINDING PROTEIN / LIM DOMAIN CONTAINING PROTEINS / METAL-BINDING PROTEIN
Function / homology
Function and homology information


muscle tissue development / actinin binding / structural constituent of muscle / sarcomere organization / alpha-actinin binding / cell leading edge / stress fiber / phosphoprotein binding / Z disc / focal adhesion ...muscle tissue development / actinin binding / structural constituent of muscle / sarcomere organization / alpha-actinin binding / cell leading edge / stress fiber / phosphoprotein binding / Z disc / focal adhesion / metal ion binding / nucleus / cytoplasm
Similarity search - Function
Cysteine Rich Protein / Cysteine Rich Protein / LIM zinc-binding domain signature. / LIM domain / Zinc-binding domain present in Lin-11, Isl-1, Mec-3. / Zinc finger, LIM-type / LIM domain profile. / Ribbon / Mainly Beta
Similarity search - Domain/homology
Cysteine and glycine-rich protein 1
Similarity search - Component
Biological speciesGallus gallus (chicken)
MethodSOLUTION NMR
AuthorsPerez-Alvarado, G.C. / Miles, C. / Michelsen, J.W. / Louis, H.A. / Winge, D.R. / Beckerle, M.C. / Summers, M.F.
CitationJournal: Nat.Struct.Biol. / Year: 1994
Title: Structure of the carboxy-terminal LIM domain from the cysteine rich protein CRP.
Authors: Perez-Alvarado, G.C. / Miles, C. / Michelsen, J.W. / Louis, H.A. / Winge, D.R. / Beckerle, M.C. / Summers, M.F.
History
DepositionJan 6, 1995Processing site: BNL
Revision 1.0Jun 3, 1995Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 16, 2022Group: Database references / Derived calculations ...Database references / Derived calculations / Other / Structure summary
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_struct_assembly / pdbx_struct_conn_angle / pdbx_struct_oper_list / struct_conn / struct_keywords / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_keywords.text / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: AVIAN CYSTEINE RICH PROTEIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)8,9703
Polymers8,8391
Non-polymers1312
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Atom site foot note1: GLU 56 - ILE 57 MODEL 1 OMEGA = 216.87 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
2: LYS 23 - VAL 24 MODEL 2 OMEGA = 212.09 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
3: GLU 56 - ILE 57 MODEL 2 OMEGA = 217.75 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
4: GLU 56 - ILE 57 MODEL 3 OMEGA = 217.70 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
5: TYR 58 - CYS 59 MODEL 3 OMEGA = 210.32 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
6: GLU 56 - ILE 57 MODEL 4 OMEGA = 217.45 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
7: GLU 56 - ILE 57 MODEL 5 OMEGA = 217.12 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
8: GLU 56 - ILE 57 MODEL 6 OMEGA = 217.24 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
9: GLU 56 - ILE 57 MODEL 7 OMEGA = 217.78 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
10: GLU 22 - LYS 23 MODEL 8 OMEGA = 213.73 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
11: GLU 56 - ILE 57 MODEL 8 OMEGA = 216.95 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
12: GLU 56 - ILE 57 MODEL 9 OMEGA = 217.36 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
13: GLU 56 - ILE 57 MODEL 10 OMEGA = 217.20 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
14: LYS 23 - VAL 24 MODEL 11 OMEGA = 210.89 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
15: GLU 56 - ILE 57 MODEL 11 OMEGA = 216.97 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
16: TYR 58 - CYS 59 MODEL 11 OMEGA = 210.33 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
17: GLU 56 - ILE 57 MODEL 12 OMEGA = 217.10 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
18: GLU 56 - ILE 57 MODEL 13 OMEGA = 217.31 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
19: LYS 23 - VAL 24 MODEL 14 OMEGA = 210.00 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
20: GLU 56 - ILE 57 MODEL 14 OMEGA = 217.54 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
21: GLU 56 - ILE 57 MODEL 15 OMEGA = 217.11 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
22: TYR 58 - CYS 59 MODEL 15 OMEGA = 218.10 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
23: GLU 56 - ILE 57 MODEL 16 OMEGA = 217.53 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
24: LYS 23 - VAL 24 MODEL 17 OMEGA = 212.33 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
25: GLU 56 - ILE 57 MODEL 17 OMEGA = 216.97 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
26: GLU 56 - ILE 57 MODEL 18 OMEGA = 217.12 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)18 / -
Representative

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Components

#1: Protein AVIAN CYSTEINE RICH PROTEIN


Mass: 8839.138 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Gallus gallus (chicken) / Organ: GIZZARD / Plasmid: PAED4-LIM2 / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: P67966
#2: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Zn

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR

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Sample preparation

Crystal grow
*PLUS
Method: other

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Processing

NMR softwareName: DSPACE / Developer: HARE RESEARCH INC. / Classification: refinement
NMR ensembleConformers submitted total number: 18

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