BMRB Entry 18808

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18808
MolProbity Validation Chart

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Title:
Structure, phosphorylation and U2AF65 binding of the Nterminal domain of splicing factor 1 during 3 splice site recognition
Deposition date:
2012-10-25
Original release date:
2013-01-28
Authors:
Madl, Tobias; Sattler, Michael; Zhang, Yun; Bagdiul, Ivona; Kern, Thomas; Kang, Hyun-Seo; Zou, Peijian; Maeusbacher, Nina; Sieber, Stephan; Kraemer, Angela
Citation:

Citation: Zhang, Yun; Madl, Tobias; Bagdiul, Ivona; Kern, Thomas; Kang, Hyun-Seo; Zou, Peijian; Maeusbacher, Nina; Sieber, Stephan; Kraemer, Angela; Sattler, Michael. "Structure, phosphorylation and U2AF65 binding of the N-terminal domain of splicing factor 1 during 3'-splice site recognition"  Nucleic Acids Res. 41, 1343-1354 (2013).
PubMed: 23175611

Assembly members:

Assembly members:
entity_1, polymer, 145 residues, 16675.199 Da.
entity_2, polymer, 104 residues, 11976.698 Da.

Natural source:

Natural source:   Common Name: Humans   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: petM11

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MATGANATPLDFPSKKRKRS RWNQDTMEQKTVIPGMPTVI PPGLTREQERAYIVQLQIED LTRKLRTGDLGIPPNPEDRS PSPEPIYNSEGKRLNTREFR TRKKLEEERHNLITEMVALN PDFKPPADYKPPATRVCDKV MIPQD
entity_2: GHPTEVLCLMNMVLPEELLD DEEYEEIVEDVRDECSKYGL VKSIEIPRPVDGVEVPGCGK IFVEFTSVFDCQKAMQGLTG RKFANRVVVTKYCDPDSYHR RDFW

Data sets:
Data typeCount
13C chemical shifts468
15N chemical shifts209
1H chemical shifts576

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22

Entities:

Entity 1, entity_1 145 residues - 16675.199 Da.

1   METALATHRGLYALAASNALATHRPROLEU
2   ASPPHEPROSERLYSLYSARGLYSARGSER
3   ARGTRPASNGLNASPTHRMETGLUGLNLYS
4   THRVALILEPROGLYMETPROTHRVALILE
5   PROPROGLYLEUTHRARGGLUGLNGLUARG
6   ALATYRILEVALGLNLEUGLNILEGLUASP
7   LEUTHRARGLYSLEUARGTHRGLYASPLEU
8   GLYILEPROPROASNPROGLUASPARGSER
9   PROSERPROGLUPROILETYRASNSERGLU
10   GLYLYSARGLEUASNTHRARGGLUPHEARG
11   THRARGLYSLYSLEUGLUGLUGLUARGHIS
12   ASNLEUILETHRGLUMETVALALALEUASN
13   PROASPPHELYSPROPROALAASPTYRLYS
14   PROPROALATHRARGVALCYSASPLYSVAL
15   METILEPROGLNASP

Entity 2, entity_2 104 residues - 11976.698 Da.

1   GLYHISPROTHRGLUVALLEUCYSLEUMET
2   ASNMETVALLEUPROGLUGLULEULEUASP
3   ASPGLUGLUTYRGLUGLUILEVALGLUASP
4   VALARGASPGLUCYSSERLYSTYRGLYLEU
5   VALLYSSERILEGLUILEPROARGPROVAL
6   ASPGLYVALGLUVALPROGLYCYSGLYLYS
7   ILEPHEVALGLUPHETHRSERVALPHEASP
8   CYSGLNLYSALAMETGLNGLYLEUTHRGLY
9   ARGLYSPHEALAASNARGVALVALVALTHR
10   LYSTYRCYSASPPROASPSERTYRHISARG
11   ARGASPPHETRP

Samples:

sample_1: entity, [U-15N], 100 – 600 uM; entity, [U-13C; U-15N], 100 – 600 uM; entity, [U-13C; U-15N; U-2H], 100 – 600 uM; sodium phosphate 20 mM; NaCl 50 mM; sodium azide 0.1%; DTT 1 mM; EDTA 1 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 70 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1

Software:

ARIA v2.1, Linge, O'Donoghue and Nilges - structure solution

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY, Goddard - chemical shift assignment

TOPSPIN, Bruker Biospin - collection, processing

NMR spectrometers:

  • Bruker Avance 900 MHz
  • Bruker Avance 750 MHz
  • Bruker Avance 600 MHz
  • Bruker Avance 500 MHz

Related Database Links:

BMRB 18802 19034
PDB
DBJ BAA05116 BAA05117 BAE01434 BAE26935 BAE27661 BAC37309 BAG70075 BAG70201 BAI45669
EMBL CAA03883 CAA59797 CAA70018 CAA70019 CAA73359 CAA45409 CAA45874 CAA45875
GB AAB03514 AAB04033 AAH08080 AAH08724 AAH09091 AAH07487 AAH08740 AAH30574 AAH43071 AAH89996
PIR S52735
REF NP_001075083 NP_001104261 NP_001104263 NP_001162562 NP_001164798 NP_001012496 NP_001068804 NP_001192160 NP_009210 NP_598432
SP Q15637 Q64213 P26368 P26369
TPG DAA13585 DAA19368
PRF 1805352A
AlphaFold Q15637 Q64213 P26368 P26369

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks