BMRB Entry 5599

Title:
The Tertiary Structure and Backbone Dynamics of Human Prolactin: Evidence for Reversible Oligomerization in Solution
Deposition date:
2002-11-25
Original release date:
2003-05-14
Authors:
Keeler, Camille; Dannies, Priscilla; Hodsdon, Michael
Citation:

Citation: Keeler, Camille; Dannies, Priscilla; Hodsdon, Michael. "The Tertiary Structure and Backbone Dynamics of Human Prolactin"  J. Mol. Biol. 328, 1105-1121 (2003).
PubMed: 12729745

Assembly members:

Assembly members:
Human Prolactin, polymer, 199 residues, Formula weight is not available

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: pT7L-hPrl

Data sets:
Data typeCount
1H chemical shifts814
13C chemical shifts668
15N chemical shifts170

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1prolactin1

Entities:

Entity 1, prolactin 199 residues - Formula weight is not available

1   LEUPROILECYSPROGLYGLYALAALAARG
2   CYSGLNVALTHRLEUARGASPLEUPHEASP
3   ARGALAVALVALLEUSERHISTYRILEHIS
4   ASNLEUSERSERGLUMETPHESERGLUPHE
5   ASPLYSARGTYRTHRHISGLYARGGLYPHE
6   ILETHRLYSALAILEASNSERCYSHISTHR
7   SERSERLEUALATHRPROGLUASPLYSGLU
8   GLNALAGLNGLNMETASNGLNLYSASPPHE
9   LEUSERLEUILEVALSERILELEUARGSER
10   TRPASNGLUPROLEUTYRHISLEUVALTHR
11   GLUVALARGGLYMETGLNGLUALAPROGLU
12   ALAILELEUSERLYSALAVALGLUILEGLU
13   GLUGLNTHRLYSARGLEULEUGLUGLYMET
14   GLULEUILEVALSERGLNVALHISPROGLU
15   THRLYSGLUASNGLUILETYRPROVALTRP
16   SERGLYLEUPROSERLEUGLNMETALAASP
17   GLUGLUSERARGLEUSERALATYRTYRASN
18   LEULEUHISCYSLEUARGARGASPSERHIS
19   LYSILEASPASNTYRLEULYSLEULEULYS
20   CYSARGILEILEHISASNASNASNCYS

Samples:

sample_1: Human Prolactin, [U-13C; U-15N], 1.0 mM; phosphate buffer 20 mM; NaCl 100 mM

conditions_1: pH: 6.8; temperature: 298 K; ionic strength: 0.2 M

Experiments:

NameSampleSample stateSample conditions
HNCOsample_1not availableconditions_1
HNCAsample_1not availableconditions_1
HNCACAsample_1not availableconditions_1
HN(CO)CAsample_1not availableconditions_1
CBCA(CO)NHsample_1not availableconditions_1
H(CA)CO(CA)NHsample_1not availableconditions_1
C(CO)NHsample_1not availableconditions_1
H(CCO)NHsample_1not availableconditions_1
HCCH-TOCSYsample_1not availableconditions_1
(4D) 13C 15N HMQC-NOESY-HSQCsample_1not availableconditions_1
(3D) 15N HSQC-NOESYsample_1not availableconditions_1
(3D) 13C NOESY-HSQCsample_1not availableconditions_1

Software:

nmrView v5.0.4 - 4D data analysis

Sparky v3.106 - 3D data analysis

CYANA v1.0.5 - structure solution

NMRPipe v1.0 - processing varian format data

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

BMRB 15773 6643
PDB
DBJ BAA00312 BAI46568
EMBL CAA23829 CAA25214 CAA38264
GB AAA18471 AAA60173 AAB70858 AAH15850 AAH88370
PRF 1005222A
REF NP_000939 NP_001040593 NP_001157030 XP_002816520 XP_003263607
SP P01236 P55151
AlphaFold P01236 P55151

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