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 6001

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR6001

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Title: 1H, 15N and 13C resonance assignments of the C345C domain of the complement component C5   PubMed: 15014240

Deposition date: 2003-11-11 Original release date: 2004-04-07

Authors: Bramham, Janice; Thai, Chuong-Thu; Mark, Rance; Uhrin, Dusan; Assa-Munt, Nuria; Ogata, Ronald; Barlow, Paul

Citation: Bramham, Janice; Rance, Mark; Thai, Chuong-Thu; Uhrin, Dusan; Assa-Munt, Nuria; Ogata, Ronald; Barlow, Paul. "Letter to the Editor: 1H, 15N and 13C resonance assignments of the C345C domain of the complement component C5 "  J. Biomol. NMR 29, 217-218 (2004).

Assembly members:
C terminal domain of C5, polymer, 151 residues, 17129.6 Da.

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

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

Entity Sequences (FASTA):
C terminal domain of C5: GSHMADCGQMQEELDLTISA ETRKQTACKPEIAYAYKVSI TSITVENVFVKYKATLLDIY KTGEAVAEKDSEITFIKKVT CTNAELVKGRQYLIMGKEAL QIKYNASFRYIYPLDSLTWI EYWPRDTTCSSCQAFLANLD EFAEDIFLNGC

Data sets:
Data typeCount
13C chemical shifts510
1H chemical shifts1039
15N chemical shifts157

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1C5 C345C domain1

Entities:

Entity 1, C5 C345C domain 151 residues - 17129.6 Da.

1   GLYSERHISMETALAASPCYSGLYGLNMET
2   GLNGLUGLULEUASPLEUTHRILESERALA
3   GLUTHRARGLYSGLNTHRALACYSLYSPRO
4   GLUILEALATYRALATYRLYSVALSERILE
5   THRSERILETHRVALGLUASNVALPHEVAL
6   LYSTYRLYSALATHRLEULEUASPILETYR
7   LYSTHRGLYGLUALAVALALAGLULYSASP
8   SERGLUILETHRPHEILELYSLYSVALTHR
9   CYSTHRASNALAGLULEUVALLYSGLYARG
10   GLNTYRLEUILEMETGLYLYSGLUALALEU
11   GLNILELYSTYRASNALASERPHEARGTYR
12   ILETYRPROLEUASPSERLEUTHRTRPILE
13   GLUTYRTRPPROARGASPTHRTHRCYSSER
14   SERCYSGLNALAPHELEUALAASNLEUASP
15   GLUPHEALAGLUASPILEPHELEUASNGLY
16   CYS

Samples:

sample_1: C terminal domain of C5, [U->98% 13C; U->98% 15N], 0.5 – 1.0 mM; NaCl 100 mM; Na phosphate 20 mM

Sample_conditions: pH: 6.0; temperature: 303 K; ionic strength: 0.1 M

Experiments:

NameSampleSample stateSample conditions
1H,15N-HSQCsample_1not availableSample_conditions
HNCACBsample_1not availableSample_conditions
CBCA(CO)NHsample_1not availableSample_conditions
(H)C(CO)NH-TOCSYsample_1not availableSample_conditions
TOCSY-HSQCsample_1not availableSample_conditions
H(C)(CO)NH-TOCSYsample_1not availableSample_conditions
HCCH-TOCSYsample_1not availableSample_conditions
13C-editted NOESYsample_1not availableSample_conditions
(HB)CB(CGCD)HDsample_1not availableSample_conditions
(HB)CB(CGCDCE)HEsample_1not availableSample_conditions
TOCSYsample_1not availableSample_conditions

Software:

AZARA v2.6 - processing raw NMR data

ANSIG v3.3 - peak assignment

NMR spectrometers:

  • Bruker AVANCE 600 MHz
  • Bruker AVANCE 800 MHz
  • Varian INOVA 600 MHz
  • Varian INOVA 800 MHz

Related Database Links:

PDB
GB AAA51856 AAA51925 AAI13739 AAI13741 ABD48959
REF NP_001726 XP_003264119 XP_003833147 XP_004048612 XP_008956866
SP P01031

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts