9AWE: Engineered Protein GF with Human Kappa Fab

The crystal structure of an engineered Protein GF with Human Kappa Fab. Determined by X-ray diffraction at 2.8 Å resolution. Released 5 Feb 2025.

Method: X-ray diffraction
Resolution: 2.8 Å
Organisms: Homo sapiens, Streptococcus sp. 'group G'
Chains: 4
Atoms: 4,822
Mol. weight: 72.91 kDa
Released: 5 Feb 2025

Explore 9AWE in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9AWE contains 19 α-helices and 57 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 A: 5 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	4-11	8	11
β-strand	16-17	2	12
β-strand	22-30	9	11
β-strand	38-45	8	12
β-strand	48	1	13
β-strand	51	1	13
β-strand	54-62	9	12
β-strand	68-76	9	11
α-helix	77-79	3
α-helix	81-83	3
α-helix	86-89	4
β-strand	93-101	9	12
β-strand	104-117	14	12
α-helix	120-124	5
α-helix	132-134	3
β-strand	135-139	5	12
β-strand	145-148	4	12

Chain B: 6 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	4-6	3	1
β-strand	11-13	3	2
β-strand	19-26	8	1
β-strand	35-40	6	2
β-strand	47-52	6	2
β-strand	59-61	3	2
α-helix	63-65	3
β-strand	69-74	6	1
β-strand	79-84	6	1
α-helix	89-91	3
β-strand	93-101	9	2
β-strand	104-108	5	2
β-strand	112-116	5	2
β-strand	122	1	3
α-helix	123-124	2
β-strand	125-129	5	4
β-strand	140-150	11	4
β-strand	151	1	3
β-strand	156-159	4	5
α-helix	160-162	3
β-strand	168-170	3	4
α-helix	171-173	3
β-strand	174-175	2	4
β-strand	181-190	10	4
β-strand	200-205	6	5
α-helix	206-208	3
β-strand	210-215	6	5

Chain C: 2 helices, 3 β-strands

Element	Residues	Length	Sheet
β-strand	11-13	3	5
β-strand	17-20	4	5
α-helix	28-37	10
α-helix	43-45	3
β-strand	58-60	3	5

Chain D: 6 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	5-7	3	6
β-strand	10-13	4	7
β-strand	19-24	6	6
α-helix	30-32	3
β-strand	33-38	6	7
β-strand	45-49	5	7
β-strand	53-54	2	7
β-strand	62-67	6	6
β-strand	70-75	6	6
α-helix	80-82	3
β-strand	85-91	7	7
β-strand	96-98	3	7
β-strand	102-106	5	7
α-helix	107	1
β-strand	111	1	8
β-strand	114-118	5	9
α-helix	122-125	4
β-strand	129-139	11	9
β-strand	140	1	8
β-strand	146-150	5	10
β-strand	153-154	2	10
β-strand	159-163	5	9
β-strand	173-182	10	9
α-helix	183-188	6
β-strand	192-196	5	10
α-helix	204	1
β-strand	205-209	5	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Fab Heavy Chain	B	protein	228	Homo sapiens
Fab Light Chain	D	protein	215	Homo sapiens
Histone chaperone ASF1	A	protein	161	Homo sapiens	P32447 (AlphaFold model)
Immunoglobulin G-binding protein G	C	protein	65	Streptococcus sp. 'group G'	P19909 (AlphaFold model)

Sequence of entity 1 (B), FASTA

>9AWE_1 Fab Heavy Chain (chains B)
EISEVQLVESGGGLVQPGGSLRLSCAASGFNVSYYSIHWVRQAPGKGLEWVASIYPYYGS
TSYADSVKGRFTISADTSKNTAYLQMNSLRAEDTAVYYCARGYGWALDYWGQGTLVTVSS
ASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSS
GLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHT

Sequence of entity 2 (D), FASTA

>9AWE_2 Fab Light Chain (chains D)
SDIQMTQSPSSLSASVGDRVTITCRASQSVSSAVAWYQQKPGKAPKLLIYSASSLYSGVP
SRFSGSRSGTDFTLTISSLQPEDFATYYCQQDGWSLITFGQGTKVEIKRTVAAPSVFIFP
PSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTL
TLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC

Sequence of entity 3 (A), FASTA

>9AWE_3 Histone chaperone ASF1 (chains A)
SSIVSLLGIKVLNNPAKFTDPYEFEITFECLESLKHDLEWKLTYVGSSRSLDHDQELDSI
LVGPVPVGVNKFVFSADPPSAELIPASELVSVTVILLSCSYDGREFVRVGYYVNNEYDEE
ELRENPPAKVQVDHIVRNILAEKPRVTRFNIVWDNENEGLE

Sequence of entity 4 (C), FASTA

>9AWE_4 Immunoglobulin G-binding protein G (chains C)
TPAVTTYKLVINGRTLSGYTTTTAVDAATAEKVFKQYAFGNGVDGEWTYDDATKTFTVTE
KPEKL

Primary citation

Engineered protein G variants for multifunctional antibody-based assemblies. Slezak, T., O'Leary, K.M., Li, J. et al. Protein Sci (2025) 34:e70019-e70019. DOI 10.1002/pro.70019 · PubMed

Other PDB entries of the same protein (UniProt P32447 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1ROC 1.5 Å, Crystal structure of the histone deposition protein Asf1
5UCB 1.52 Å, Structure of antigen-Fab complex with engineered switch residue region.
2HUE 1.7 Å, Structure of the H3-H4 chaperone Asf1 bound to histones H3 and H4
5UEK 1.7 Å, Structure of antigen-Fab 12E complex with Histone chaperone ASF1
5UEA 1.7 Å, Structure of antigen-Fab complex with Histone chaperone ASF1
6AYZ 2.1 Å, Crystal structure of Asf1-Fab 12E complex
2IDC 2.2 Å, Structure of the Histone H3-Asf1 Chaperone Interaction
4ZBJ 2.25 Å, UBN1 peptide bound to H3.3/H4/Asf1
4EO5 2.35 Å, Yeast Asf1 bound to H3/H4G94P mutant
5EII 2.44 Å, Structural determination of an protein complex of a Fab with increased solubility
6AZ2 2.48 Å, Crystal structure of Asf1-Fab 12E complex
4RRP 2.79 Å, Crystal Structure of the Fab complexed with antigen Asf1p, Northeast Structural Genomics…

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