4NM4: Broadly neutralizing antibody CR8043

Crystal structure of broadly neutralizing antibody CR8043. Determined by X-ray diffraction at 2.65 Å resolution. Released 25 Dec 2013.

Method: X-ray diffraction
Resolution: 2.65 Å
Organism: Homo sapiens
Chains: 4
Atoms: 6,750
Mol. weight: 96.63 kDa
Released: 25 Dec 2013

Explore 4NM4 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4NM4 contains 35 α-helices and 90 β-strands across 4 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 H: 8 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	3-6	4	7
β-strand	10-12	3	8
β-strand	18-25	8	7
α-helix	29-31	3
β-strand	34-39	6	8
β-strand	45-51	7	8
β-strand	57-59	3	8
α-helix	61-63	3
β-strand	67-72	6	7
β-strand	77-82	6	7
α-helix	84-86	3
β-strand	88-95	8	8
β-strand	100D-103	4	8
β-strand	107-111	5	8
β-strand	117	1	9
α-helix	118-119	2
β-strand	120-124	5	10
β-strand	135-145	11	10
β-strand	146	1	9
β-strand	151-154	4	11
α-helix	155-157	3
β-strand	163-165	3	10
α-helix	166-168	3
β-strand	169-170	2	10
β-strand	176-185	10	10
α-helix	186-188	3
β-strand	194-200	7	11
α-helix	201-203	3
β-strand	205-211	7	11

Chain I: 9 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	3-6	4	18
α-helix	7-9	3
β-strand	10-12	3	19
β-strand	18-25	8	18
α-helix	29-31	3
β-strand	34-39	6	19
β-strand	45-51	7	19
β-strand	57-59	3	19
α-helix	61-63	3
β-strand	67-72	6	18
β-strand	77-82	6	18
α-helix	84-86	3
β-strand	88-95	8	19
β-strand	100D-103	4	19
β-strand	107-111	5	19
β-strand	117	1	20
α-helix	118-119	2
β-strand	120-124	5	21
β-strand	131-132	2	21
β-strand	135-145	11	21
β-strand	146	1	20
β-strand	151-154	4	22
α-helix	155-157	3
β-strand	159	1	22
β-strand	163-165	3	21
α-helix	166-168	3
β-strand	169-170	2	21
β-strand	176-185	10	21
α-helix	186-188	3
β-strand	194-200	7	22
α-helix	201-203	3
β-strand	205-211	7	22

Chain L: 9 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	4-7	4	1
β-strand	10-13	4	2
β-strand	19-25	7	1
β-strand	27C-27D	2	3
β-strand	30-31	2	3
β-strand	33-38	6	2
α-helix	43-44	2
β-strand	45-49	5	2
β-strand	53-54	2	2
α-helix	55	1
β-strand	62-67	6	1
β-strand	70-75	6	1
α-helix	80-82	3
β-strand	84-90	7	2
α-helix	96	1
β-strand	97-98	2	2
β-strand	102-106	5	2
β-strand	111	1	4
α-helix	112-113	2
β-strand	114-118	5	5
α-helix	119-121	3
α-helix	122-126	5
β-strand	129-139	11	5
β-strand	140	1	4
β-strand	145-150	6	6
β-strand	153-154	2	6
β-strand	159-163	5	5
α-helix	164-167	4
β-strand	173-182	10	5
α-helix	183-186	4
β-strand	191-197	7	6
β-strand	205-210	6	6

Chain M: 9 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	4-7	4	12
β-strand	10-13	4	13
β-strand	19-25	7	12
β-strand	27C	1	14
β-strand	31	1	14
β-strand	33-38	6	13
α-helix	43-44	2
β-strand	45-49	5	13
β-strand	53-54	2	13
α-helix	55	1
β-strand	62-67	6	12
β-strand	70-75	6	12
α-helix	80-82	3
β-strand	85-90	6	13
α-helix	96	1
β-strand	97-98	2	13
β-strand	102-106	5	13
β-strand	111	1	15
α-helix	112-113	2
β-strand	114-118	5	16
α-helix	119-121	3
α-helix	122-126	5
β-strand	129-139	11	16
β-strand	140	1	15
β-strand	144-150	7	17
β-strand	153-154	2	17
β-strand	159-163	5	16
α-helix	164-167	4
β-strand	173-182	10	16
α-helix	183-186	4
β-strand	191-198	8	17
β-strand	205-210	6	17

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Antibody CR8043, Light Chain	L, M	protein	220	Homo sapiens	P01834 (AlphaFold model)
Antibody CR8043, Heavy Chain	H, I	protein	224	Homo sapiens	S6C4S0 (AlphaFold model)

Sequence of entity 1 (L, M), FASTA

>4NM4_1 Antibody CR8043, Light Chain (chains L, M)
DIQMTQSPDSLAVSLGERATINCKSSQSVFSSSTNKNYLAWYQQKPGQPPKVLIYWSSTR
ESGVPDRFSASGSGTDFTLTISSLQAADVAVYYCHQYYTAPWTFGQGTKVEIKRTVAAPS
VFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYS
LSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC

Sequence of entity 2 (H, I), FASTA

>4NM4_2 Antibody CR8043, Heavy Chain (chains H, I)
QVQLVQSGAEVKKPGASVKLSCKASGYTFTAYSMHWVRQAPGQSLEWLGWINTAIGNTQY
SQKFQDRVTITRDTSARTSYMELSSLRSGDTAVYFCARGASWDARGWSGYWGKGTLVTVS
SASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQS
SGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKRVEPKSC

Primary citation

A common solution to group 2 influenza virus neutralization. Friesen, R.H., Lee, P.S., Stoop, E.J. et al. Proc Natl Acad Sci U S A (2014) 111:445-450. DOI 10.1073/pnas.1319058110 · PubMed

Other PDB entries of the same protein (UniProt P01834 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5EWI 1.6 Å, Crystal Structure of the Human Fab VRC38.01, an HIV-1 V1V2-Directed Neutralizing…
1NGZ 1.6 Å, Chimeric Germline Fab 7g12-apo
6N35 1.75 Å, Anti-HIV-1 Fab 2G12 + Man1-2 re-refinement
4XMP 1.78 Å, Crystal structure of broadly and potently neutralizing antibody VRC08 in complex with…
1N0X 1.8 Å, Crystal Structure of a Broadly Neutralizing Anti-HIV-1 Antibody in Complex with a…
3VH8 1.8 Å, KIR3DL1 in complex with HLA-B*5701
3X12 1.8 Å, Crystal structure of HLA-B*57:01.I80N
6B9Z 1.82 Å, Trastuzumab Fab v3
2VXQ 1.9 Å, Crystal structure of the major grass pollen allergen Phl p 2 in complex with its…
3D85 1.9 Å, Crystal structure of IL-23 in complex with neutralizing FAB
6BAH 1.9 Å, Trastuzumab Fab v3 with 5-diphenyl meditope variant
6DCV 1.9 Å, Crystal structure of human anti-tau antibody CBTAU-27.1

Browse structure collections

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