BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 16439

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16439
MolProbity Validation Chart

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Title: Combined high- and low-resolution techniques reveal compact structure in central portion of factor H despite long inter-modular linkers   PubMed: 19835885

Deposition date: 2009-08-04 Original release date: 2009-11-19

Authors: Schmidt, Christoph; Herbert, Andrew; Guariento, Mara; Mertens, Haydyn; Soares, Dinesh; Uhrin, Dusan; Rowe, Arthur; Svergun, Dmitri; Barlow, Paul

Citation: Schmidt, Christoph; Herbert, Andrew; Mertens, Haydyn; Guariento, Mara; Soares, Dinesh; Uhrin, Dusan; Rowe, Arthur; Svergun, Dmitri; Barlow, Paul. "The central portion of factor H (modules 10-15) is compact and contains a structurally deviant CCP module."  J. Mol. Biol. 395, 105-122 (2010).

Assembly members:
factor H (modules 10-15), polymer, 121 residues, Formula weight is not available

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

Experimental source:   Production method: recombinant technology   Host organism: Pichia pastoris   Vector: pPICZalphaB

Entity Sequences (FASTA):
factor H (modules 10-15): EAEAAGTCGDIPELEHGWAQ LSSPPYYYGDSVEFNCSESF TMIGHRSITCIHGVWTQLPQ CVAIDKLKKCKSSNLIILEE HLKNKKEFDHNSNIRYRCRG KEGWIHTVCINGRWDPEVNC S

Data sets:
Data typeCount
13C chemical shifts508
15N chemical shifts127
1H chemical shifts746

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1factor H (modules 10-15)1

Entities:

Entity 1, factor H (modules 10-15) 121 residues - Formula weight is not available

1   GLUALAGLUALAALAGLYTHRCYSGLYASP
2   ILEPROGLULEUGLUHISGLYTRPALAGLN
3   LEUSERSERPROPROTYRTYRTYRGLYASP
4   SERVALGLUPHEASNCYSSERGLUSERPHE
5   THRMETILEGLYHISARGSERILETHRCYS
6   ILEHISGLYVALTRPTHRGLNLEUPROGLN
7   CYSVALALAILEASPLYSLEULYSLYSCYS
8   LYSSERSERASNLEUILEILELEUGLUGLU
9   HISLEULYSASNLYSLYSGLUPHEASPHIS
10   ASNSERASNILEARGTYRARGCYSARGGLY
11   LYSGLUGLYTRPILEHISTHRVALCYSILE
12   ASNGLYARGTRPASPPROGLUVALASNCYS
13   SER

Samples:

sample_1: potassium phosphate 20 mM; entity, [U-100% 13C; U-100% 15N], 0.62 mM; D2O 7%; H2O 93%

sample_conditions_1: ionic strength: 20 mM; pH: 6.6; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D CBCANHsample_1isotropicsample_conditions_1

Software:

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

Molmol, Koradi, Billeter and Wuthrich - data analysis

AZARA, Boucher - processing

ProcheckNMR, Laskowski and MacArthur - data analysis

TOPSPIN, Bruker Biospin - collection

WhatIF, Vriend - data analysis

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz

Related Database Links:

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