5NQP: PDB entry 5NQP

Structure of a fHbp(V1.4):PorA(P1.16) chimera. Fusion at fHbp position 151. Determined by X-ray diffraction at 2.86 Å resolution. Released 28 Feb 2018.

Method: X-ray diffraction
Resolution: 2.86 Å
Organisms: Neisseria meningitidis, Neisseria meningitidis serogroup C
Chains: 3
Atoms: 6,007
Mol. weight: 89.41 kDa
Released: 28 Feb 2018

Explore 5NQP in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5NQP contains 23 α-helices and 58 β-strands across 3 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 8 helices, 20 β-strands

Element	Residues	Length	Sheet
α-helix	76-79	4
α-helix	81-86	6
β-strand	99-100	2	5
β-strand	109-115	7	6
β-strand	118-122	5	6
α-helix	126	1
β-strand	127-128	2	5
α-helix	130-132	3
α-helix	134	1
β-strand	138-150D	17	6
β-strand	150J-165	19	6
β-strand	169-180	12	6
β-strand	188-201	14	6
β-strand	203	1	7
α-helix	204	1
β-strand	205	1	8
α-helix	206-208	3
β-strand	214-223	10	7
β-strand	226-236	11	7
β-strand	241-247	7	7
α-helix	252-254	3
β-strand	257-262	6	7
β-strand	264-265	2	7
β-strand	270	1	8
β-strand	271-278	8	7
β-strand	283-292	10	7
β-strand	298-307	10	7
β-strand	310-319	10	7

Chain B: 8 helices, 19 β-strands

Element	Residues	Length	Sheet
α-helix	82-86	5
β-strand	99-100	2	9
β-strand	109-115	7	10
β-strand	118-122	5	10
α-helix	126	1
β-strand	127-128	2	9
α-helix	130-132	3
α-helix	134	1
β-strand	138-150D	17	10
α-helix	150F-150H	3
β-strand	150J-165	19	10
β-strand	169-180	12	10
β-strand	188-201	14	10
β-strand	203	1	11
α-helix	204	1
β-strand	205	1	12
α-helix	206-208	3
β-strand	214-223	10	11
β-strand	226-236	11	11
β-strand	241-247	7	11
α-helix	252-254	3
β-strand	257-265	9	11
β-strand	270	1	12
β-strand	271-278	8	11
β-strand	283-292	10	11
β-strand	298-307	10	11
β-strand	310-319	10	11

Chain C: 7 helices, 19 β-strands

Element	Residues	Length	Sheet
α-helix	80-86	7
β-strand	99-100	2	1
β-strand	109-115	7	2
β-strand	118-122	5	2
α-helix	126	1
β-strand	127-128	2	1
α-helix	130-132	3
α-helix	134	1
β-strand	138-150D	17	2
β-strand	150J-165	19	2
β-strand	169-180	12	2
β-strand	188-201	14	2
β-strand	203	1	3
α-helix	204	1
β-strand	205	1	4
α-helix	206-208	3
β-strand	214-223	10	3
β-strand	226-236	11	3
β-strand	241-247	7	3
α-helix	252-254	3
β-strand	257-265	9	3
β-strand	270	1	4
β-strand	271-278	8	3
β-strand	283-292	10	3
β-strand	298-307	10	3
β-strand	310-320	11	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Factor H binding protein variant B16_001,Major outer membrane protein P.IA,Factor H binding…	A, B, C	protein	271	Neisseria meningitidis, Neisseria meningitidis serogroup C	P13415 (AlphaFold model), Q6VS06 (AlphaFold model)

Sequence of entity 1 (A, B, C), FASTA

>5NQP_1 Factor H binding protein variant B16_001,Major outer membrane protein P.IA,Factor H binding protein variant B16_001 (chains A, B, C)
MGVAADIGAGLADALTAPLDHKDKSLQSLTLDQSVRKNEKLKLAAQGAEKTYGNGDSLNT
GKLKNDKVSRFDFIRQIEVDYYTKDTNNNLTLVPQLITLESGEFQVYKQSHSALTALQTE
QVQDSEHSGKMVAKRQFRIGDIAGEHTSFDKLPEGGRATYRGTAFGSDDASGKLTYTIDF
AAKQGHGKIEHLKSPELNVDLAASDIKPDKKRHAVISGSVLYNQAEKGSYSLGIFGGQAQ
EVAGSAEVETANGIRHIGLAAKQLEHHHHHH

Primary citation

Structure-based design of chimeric antigens for multivalent protein vaccines. Hollingshead, S., Jongerius, I., Exley, R.M. et al. Nat Commun (2018) 9:1051-1051. DOI 10.1038/s41467-018-03146-7 · PubMed

Other PDB entries of the same protein (UniProt P13415 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5NQZ 1.63 Å, Structure of a fHbp(V1.1):PorA(P1.16) chimera. Fusion at fHbp position 309.
5NQY 2.6 Å, Structure of a fHbp(V1.4):PorA(P1.16) chimera. Fusion at fHbp position 309.
5NQX 3.66 Å, Structure of a fHbp(V1.1):PorA(P1.16) chimera. Fusion at fHbp position 294.

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