BMRB Entry 15996

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15996
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
1H, 15N and 13C resonance assignment of the pair of Factor-I like modules of the complement protein C7
Deposition date:
2008-10-21
Original release date:
2009-01-15
Authors:
Phelan, Marie; Thai, Chuong-Thu; Herbert, Andrew; Bella, Juraj; Uhrin, Dusan; Ogata, Ronald; Barlow, Paul; Bramham, Janice
Citation:

Citation: Phelan, Marie; Thai, Chuong-Thu; Herbert, Andrew; Bella, Juraj; Uhrin, Dusan; Ogata, Ronald; Barlow, Paul; Bramham, Janice. "1H, 15N and 13C resonance assignment of the pair of Factor-I like modules of the complement protein C7"  Biomol. NMR Assign. 3, 49-52 (2009).
PubMed: 19636945

Assembly members:

Assembly members:
C7-FIMs, polymer, 155 residues, 16937.6 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: pET15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
C7-FIMs: GSHMNPLTQAVPKCQRWEKL QNSRCVCKMPYECGPSLDVC AQDERSKRILPLTVCKMHVL HCQGRNYTLTGRDSCTLPAS AEKACGACPLWGKCDAESSK CVCREASECEEEGFSICVEV NGKEQTMSECEAGALRCRGQ SISVTSIRPCAAETQ

Data sets:
Data typeCount
13C chemical shifts578
15N chemical shifts159
1H chemical shifts939

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1C7-FIMs1

Entities:

Entity 1, C7-FIMs 155 residues - 16937.6 Da.

1   GLYSERHISMETASNPROLEUTHRGLNALA
2   VALPROLYSCYSGLNARGTRPGLULYSLEU
3   GLNASNSERARGCYSVALCYSLYSMETPRO
4   TYRGLUCYSGLYPROSERLEUASPVALCYS
5   ALAGLNASPGLUARGSERLYSARGILELEU
6   PROLEUTHRVALCYSLYSMETHISVALLEU
7   HISCYSGLNGLYARGASNTYRTHRLEUTHR
8   GLYARGASPSERCYSTHRLEUPROALASER
9   ALAGLULYSALACYSGLYALACYSPROLEU
10   TRPGLYLYSCYSASPALAGLUSERSERLYS
11   CYSVALCYSARGGLUALASERGLUCYSGLU
12   GLUGLUGLYPHESERILECYSVALGLUVAL
13   ASNGLYLYSGLUGLNTHRMETSERGLUCYS
14   GLUALAGLYALALEUARGCYSARGGLYGLN
15   SERILESERVALTHRSERILEARGPROCYS
16   ALAALAGLUTHRGLN

Samples:

sample_1: C7-FIMs, [U-98% 13C; U-98% 15N], 0.2-0.3 mM; potassium phosphate 20 mM

sample_2: C7-FIMs, [U-98% 13C; U-98% 15N], 0.2-0.3 mM; potassium phosphate 20 mM

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

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HBHANHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
2D (HB)CB(CGCD)HDsample_2isotropicsample_conditions_1
2D (HB)CB(CGCDCE)HEsample_2isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

AZARA, Boucher - processing

CCPN_Analysis, CCPN - data analysis

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz

Related Database Links:

PDB
DBJ BAF83038 BAG35608 BAJ20698
EMBL CAA60121 CAH91280
GB AAA51861 AAH63851 ADR82762 AIC48386 AKI71774
REF NP_000578 NP_001125756 XP_001085533 XP_001138984 XP_003811023
SP P10643 Q5RAD0
AlphaFold P10643 Q5RAD0

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