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- PDB-2lv2: Solution NMR structure of C2H2-type Zinc-fingers 4 and 5 from hum... -

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Basic information

Entry
Database: PDB / ID: 2lv2
TitleSolution NMR structure of C2H2-type Zinc-fingers 4 and 5 from human Insulinoma-associated protein 1 (fragment 424-497), Northeast Structural Genomics Consortium Target HR7614B
ComponentsInsulinoma-associated protein 1
KeywordsTRANSCRIPTION / Structural Genomics / NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG) / PSI-Biology / Protein Structure Initiative
Function / homology
Function and homology information


Regulation of gene expression in endocrine-committed (NEUROG3+) progenitor cells / pancreatic A cell differentiation / adrenal chromaffin cell differentiation / type B pancreatic cell differentiation / noradrenergic neuron development / transdifferentiation / norepinephrine biosynthetic process / sympathetic ganglion development / positive regulation of neural precursor cell proliferation / regulation of cell cycle process ...Regulation of gene expression in endocrine-committed (NEUROG3+) progenitor cells / pancreatic A cell differentiation / adrenal chromaffin cell differentiation / type B pancreatic cell differentiation / noradrenergic neuron development / transdifferentiation / norepinephrine biosynthetic process / sympathetic ganglion development / positive regulation of neural precursor cell proliferation / regulation of cell cycle process / transcription repressor complex / negative regulation of protein phosphorylation / regulation of protein-containing complex assembly / cyclin binding / positive regulation of cell differentiation / chromatin DNA binding / DNA-binding transcription repressor activity, RNA polymerase II-specific / histone deacetylase binding / regulation of gene expression / neuron differentiation / molecular adaptor activity / regulation of cell cycle / RNA polymerase II cis-regulatory region sequence-specific DNA binding / DNA-binding transcription factor activity / negative regulation of cell population proliferation / negative regulation of transcription by RNA polymerase II / DNA-templated transcription / nucleoplasm / zinc ion binding / nucleus
Similarity search - Function
Insulinoma-associated protein 1/2 / Classic Zinc Finger / Double Stranded RNA Binding Domain / Zinc finger, C2H2 type / zinc finger / Zinc finger C2H2 type domain profile. / Zinc finger C2H2 superfamily / Zinc finger C2H2 type domain signature. / Zinc finger C2H2-type / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
Insulinoma-associated protein 1
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR / simulated annealing
Model detailslowest energy, model
AuthorsYang, Y. / Ramelot, T.A. / Cort, J.R. / Shastry, R. / Kohan, E. / Janjua, H. / Xiao, R. / Acton, T. / Everett, J.K. / Montelione, G.T. ...Yang, Y. / Ramelot, T.A. / Cort, J.R. / Shastry, R. / Kohan, E. / Janjua, H. / Xiao, R. / Acton, T. / Everett, J.K. / Montelione, G.T. / Kennedy, M.A. / Northeast Structural Genomics Consortium (NESG)
CitationJournal: To be Published
Title: Solution NMR structure of C2H2-type Zinc-fingers 4 and 5 from human Insulinoma-associated protein 1 (fragment 424-497), Northeast Structural Genomics Consortium Target HR7614B (CASP Target)
Authors: Yang, Y. / Ramelot, T.A. / Cort, J.R. / Shastry, R. / Kohan, E. / Janjua, H. / Xiao, R. / Acton, T. / Everett, J.K. / Montelione, G.T. / Kennedy, M.A.
History
DepositionJun 27, 2012Deposition site: BMRB / Processing site: RCSB
Revision 1.0Oct 10, 2012Provider: repository / Type: Initial release
Revision 1.1Jun 14, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_nmr_software / pdbx_nmr_spectrometer / pdbx_struct_conn_angle / struct_conn / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_nmr_data / _pdbx_nmr_software.name / _pdbx_nmr_spectrometer.model / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_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_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.2May 15, 2024Group: Data collection / Database references / Category: chem_comp_atom / chem_comp_bond / database_2 / Item: _database_2.pdbx_DOI

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Insulinoma-associated protein 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)9,3863
Polymers9,2551
Non-polymers1312
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / 100structures with the lowest energy
RepresentativeModel #1lowest energy

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Components

#1: Protein Insulinoma-associated protein 1 / Zinc finger protein IA-1


Mass: 9255.476 Da / Num. of mol.: 1 / Fragment: C2H2-type zinc fingers 4 and 5
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: IA1, INSM1 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)pMgK / References: UniProt: Q01101
#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
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1112D 1H-15N HSQC
1212D 1H-13C HSQC
1313D HNCO
1413D CBCA(CO)NH
1513D HN(CA)CB
1613D 1H-13C NOESY aromatic
1713D 1H-13C NOESY aliphatic
1813D C(CO)NH
1913D HNCA
11013D HN(CO)CA
11113D H(CCO)NH
11213D (H)CCH-TOCSY
11313D HNHA
11434D CC-NOESY
11522D 1H-13C HSQC CT aliphatic
11622D 1H-13C HSQC noCT aliphatic
11733D (H)CCH-TOCSY
11813D Nnoesy

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Sample preparation

Details
Solution-IDContentsSolvent system
10.69 mM [U-100% 13C; U-100% 15N] HR7614B.021, 100 mM NaCl, 5 mM DTT, 0.02 % NaN3, 10 mM Tris-HCl pH 7.5, 90% H2O/10% D2O90% H2O/10% D2O
21.25 mM [U-5% 13C; U-100% 15N] HR7614B.023, 100 mM NaCl, 5 mM DTT, 0.02 % NaN3, 10 mM Tris-HCl pH 7.5, 90% H2O/10% D2O90% H2O/10% D2O
31.25 mM [U-5% 13C; U-100% 15N] HR7614B.023, 100 mM NaCl, 5 mM DTT, 0.02 % NaN3, 10 mM Tris-HCl pH 7.5, 100% D2O100% D2O
Sample
Conc. (mg/ml)ComponentIsotopic labelingSolution-ID
0.69 mMHR7614B.021-1[U-100% 13C; U-100% 15N]1
100 mMNaCl-21
5 mMDTT-31
0.02 %NaN3-41
10 mMTris-HCl pH 7.5-51
1.25 mMHR7614B.023-6[U-5% 13C; U-100% 15N]2
100 mMNaCl-72
5 mMDTT-82
0.02 %NaN3-92
10 mMTris-HCl pH 7.5-102
1.25 mMHR7614B.023-11[U-5% 13C; U-100% 15N]3
100 mMNaCl-123
5 mMDTT-133
0.02 %NaN3-143
10 mMTris-HCl pH 7.5-153
Sample conditionspH: 6.5 / Pressure: ambient / Temperature: 298 K

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker AvanceBrukerAVANCE8501
Varian INOVAVarianINOVA6002

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Processing

NMR software
NameVersionDeveloperClassification
CNSBrunger, Adams, Clore, Gros, Nilges and Readrefinement
CNSBrunger, Adams, Clore, Gros, Nilges and Readstructure solution
CNSBrunger, Adams, Clore, Gros, Nilges and Readgeometry optimization
CYANA3Guntert, Mumenthaler and Wuthrichrefinement
CYANA3Guntert, Mumenthaler and Wuthrichgeometry optimization
CYANA3Guntert, Mumenthaler and Wuthrichstructure solution
AutoStructure2.1Huang, Tejero, Powers and Montelionedata analysis
AutoStructure2.1Huang, Tejero, Powers and Montelionerefinement
AutoAssign2.1Zimmerman, Moseley, Kulikowski and Montelionedata analysis
AutoAssign2.1Zimmerman, Moseley, Kulikowski and Montelionechemical shift assignment
NMRPipeDelaglio, Grzesiek, Vuister, Zhu, Pfeifer and Baxprocessing
XEASYBartels et al.data analysis,peak picking,chemical shift assignment
TopSpinBruker Biospincollection
VnmrJVariancollection
PINEBahrami, Markley, Assadi, and Eghbalniachemical shift assignment
SparkyGoddarddata analysis
TALOS+Shen, Cornilescu, Delaglio and Baxgeometry optimization
PSVSBhattacharya, Montelionestructure validation
RefinementMethod: simulated annealing / Software ordinal: 1
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: structures with the lowest energy
Conformers calculated total number: 100 / Conformers submitted total number: 20

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