BMRB Entry 18698

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18698
MolProbity Validation Chart

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Title:
Solution NMR Structure of the eukaryotic RNA recognition motif, RRM1, from the heterogeneous nuclear ribonucleoprotein H from Homo sapiens, Northeast Structural Genomics Consortium (NESG) Target HR8614A
Deposition date:
2012-08-31
Original release date:
2012-10-29
Authors:
Ramelot, Theresa; Yang, Yunhuang; Pederson, Kari; Shastry, Ritu; Kohan, Eitan; Janjua, Haleema; Xiao, Rong; Acton, Thomas; Everett, John; Prestegard, James; Montelione, Gaetano; Kennedy, Michael
Citation:

Citation: Ramelot, Theresa; Yang, Yunhuang; Pederson, Kari; Shastry, Ritu; Kohan, Eitan; Janjua, Haleema; Xiao, Rong; Acton, Thomas; Everett, John; Prestegard, James; Montelione, Gaetano; Kennedy, Michael. "Solution NMR Structure of the eukaryotic RNA recognition motif, RRM1, from the heterogeneous nuclear ribonucleoprotein H from Homo sapiens, Northeast Structural Genomics Consortium (NESG) Target HR8614A"  To be published ., .-..

Assembly members:

Assembly members:
HR8614A, polymer, 108 residues, 12381.880 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET15Avi6HT_NESG

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HR8614A: SHMGGEGFVVKVRGLPWSCS ADEVQRFFSDCKIQNGAQGI RFIYTREGRPSGEAFVELES EDEVKLALKKDRETMGHRYV EVFKSNNVEMDWVLKHTGPN SPDTANDG

Data sets:
Data typeCount
13C chemical shifts466
15N chemical shifts113
1H chemical shifts723

Time Domain Data

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1HR8614A1

Entities:

Entity 1, HR8614A 108 residues - 12381.880 Da.

1   SERHISMETGLYGLYGLUGLYPHEVALVAL
2   LYSVALARGGLYLEUPROTRPSERCYSSER
3   ALAASPGLUVALGLNARGPHEPHESERASP
4   CYSLYSILEGLNASNGLYALAGLNGLYILE
5   ARGPHEILETYRTHRARGGLUGLYARGPRO
6   SERGLYGLUALAPHEVALGLULEUGLUSER
7   GLUASPGLUVALLYSLEUALALEULYSLYS
8   ASPARGGLUTHRMETGLYHISARGTYRVAL
9   GLUVALPHELYSSERASNASNVALGLUMET
10   ASPTRPVALLEULYSHISTHRGLYPROASN
11   SERPROASPTHRALAASNASPGLY

Samples:

HR8614A.007_NC_sample: HR8614A.007, [U-100% 13C; U-100% 15N], 1.0 mM; MES 20 mM; sodium chloride 100 mM; calcium chloride 5 mM; DTT 10 mM; DSS 50 uM

HR8614A.009_NC5_sample: HR8614A.008, [biosynthetically directed-5% 13C; U-100% 15N], 0.8 mM; MES 20 mM; sodium chloride 100 mM; calcium chloride 5 mM; DTT 10 mM; DSS 50 uM

HR8614A.007_NC_D2O_sample: HR8614A.007, [U-100% 13C; U-100% 15N], 1.0 mM; MES 20 mM; sodium chloride 100 mM; calcium chloride 5 mM; DTT 10 mM; DSS 50 uM

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCHR8614A.007_NC_sampleisotropicsample_conditions_1
2D 1H-13C HSQC aliphaticHR8614A.007_NC_sampleisotropicsample_conditions_1
3D HNCOHR8614A.007_NC_sampleisotropicsample_conditions_1
3D CBCA(CO)NHHR8614A.007_NC_sampleisotropicsample_conditions_1
3D HNCACBHR8614A.007_NC_sampleisotropicsample_conditions_1
3D 1H-13C arom NOESYHR8614A.007_NC_sampleisotropicsample_conditions_1
3D 1H-13C NOESY aliphaticHR8614A.007_NC_sampleisotropicsample_conditions_1
3D 1H-15N NOESYHR8614A.007_NC_sampleisotropicsample_conditions_1
3D C(CO)NHHR8614A.007_NC_sampleisotropicsample_conditions_1
3D HBHA(CO)NHHR8614A.007_NC_sampleisotropicsample_conditions_1
3D HCCH-TOCSYHR8614A.007_NC_sampleisotropicsample_conditions_1
3D (H)CCH-TOCSYHR8614A.007_NC_D2O_sampleisotropicsample_conditions_1
3D NUS 1H-13C NOESY aliphaticHR8614A.007_NC_D2O_sampleisotropicsample_conditions_1
2D 1H-15N HSQC NH2onlyHR8614A.007_NC_sampleisotropicsample_conditions_1
4D 13C-13C-HMQC-NOESY-HMQCHR8614A.007_NC_D2O_sampleisotropicsample_conditions_1
1D T1 Nhsqc arrayHR8614A.007_NC_sampleisotropicsample_conditions_1
1D T2 Nhsqc arrayHR8614A.007_NC_sampleisotropicsample_conditions_1
2D 1H-15N HSQCHR8614A.009_NC5_sampleisotropicsample_conditions_1
2D 1H-13C HSQC aliphaticHR8614A.009_NC5_sampleisotropicsample_conditions_1
2D 1H-13C HSQC arom CTHR8614A.007_NC_sampleisotropicsample_conditions_1
2D 1H-13C HSQC arom noCTHR8614A.007_NC_sampleisotropicsample_conditions_1
2D 1H-15N HSQC_HisHR8614A.009_NC5_sampleisotropicsample_conditions_1
2D 1H-15N heteronuclear NOE interleavedHR8614A.009_NC5_sampleisotropicsample_conditions_1

Software:

CNS vcns_solve_1.3, Brunger, Adams, Clore, Gros, Nilges and Read - refinemen,structure solution,geometry optimization

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

AutoStruct vASDP-1.0, Huang, Tejero, Powers and Montelione - data analysis,refinement

NMRPipe vNMRPipe-201109, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

TOPSPIN v2.1.4 and 3.1, Bruker Biospin - collection

VNMRJ v1.1 D, Varian - collection

PINE vPINE Server v.2.0, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

SPARKY v3.113, Goddard - data analysis

TALOS+ v1.2009.0721.18, Shen, Cornilescu, Delaglio and Bax - geometry optimization

PALES vpales_linux 2000, PALES (Zweckstetter, Bax) - geometry optimization

PSVS v1.4, Bhattacharya, Montelione - structure validation

FMCGUI vfmcgui_2.5_linux, Lemak, Gutmanas, Chitayat, Karra, Fares, Sunnerhagan, and Arrowsmith - structure solution

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Varian INOVA 600 MHz

Related Database Links:

UNP P31943
HUGO HNRNPH1
BMRB 15212
PDB
GB AAH99792 EDM04272 EDM04274
AlphaFold Q6IBM4

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