9NFB: Cross-HLA supertype antibody R302

Structure of the cross-HLA supertype antibody R302 bound to a class I MHC presenting a divarasib-modified KRAS-G12C peptide on HLA-A*02. Determined by electron microscopy at 3.23 Å resolution. Released 8 Oct 2025.

Method: Electron microscopy
Resolution: 3.23 Å
Organism: Homo sapiens
Chains: 5
Atoms: 4,693
Mol. weight: 96.99 kDa
Ligands: A1AWR
Released: 8 Oct 2025

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

Secondary structure: helices and β-sheets

9NFB contains 12 α-helices and 51 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: 7 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	3-12	10	1
α-helix	20	1
β-strand	21-28	8	1
β-strand	31-37	7	1
β-strand	46-47	2	1
α-helix	52-54	3
α-helix	57-85	29
β-strand	94-103	10	1
β-strand	109-118	10	1
β-strand	121-126	6	1
β-strand	133-135	3	1
α-helix	138-150	13
α-helix	152-158	7
α-helix	159-164	6
α-helix	165-174	10
β-strand	183	1	2
β-strand	186-191	6	3
β-strand	201-208	8	3
β-strand	209	1	2
β-strand	213-218	6	4
β-strand	230	1	3
β-strand	234-235	2	3
β-strand	241-247	7	3
β-strand	258-263	6	4
β-strand	270-272	3	4

Chain B: 1 helix, 11 β-strands

Element	Residues	Length	Sheet
β-strand	23	1	5
β-strand	26-31	6	6
β-strand	41-50	10	6
β-strand	51	1	5
β-strand	56-61	6	7
β-strand	64-65	2	7
β-strand	70-71	2	6
α-helix	72-74	3
β-strand	75-76	2	6
β-strand	82-90	9	6
β-strand	98-103	6	7
β-strand	111-114	4	7

Chain D: 2 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	4-7	4	8
β-strand	10-12	3	9
β-strand	19-29	11	8
α-helix	31-33	3
β-strand	34-39	6	9
β-strand	46-50	5	9
β-strand	54-55	2	9
β-strand	63-76	14	8
α-helix	81-83	3
β-strand	86-91	6	9
β-strand	97-98	2	9
β-strand	102-105	4	9

Chain E: 2 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	10
β-strand	11-12	2	11
β-strand	18-25	8	10
α-helix	29-31	3
β-strand	34-39	6	12
β-strand	45-51	7	12
β-strand	58-60	3	12
β-strand	68-73	6	10
β-strand	78-83	6	10
α-helix	88-90	3
β-strand	92-98	7	12
β-strand	107-108	2	12
β-strand	112-114	3	12
β-strand	115-116	2	11

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
MHC class I antigen	A	protein	307	Homo sapiens	A0A6S7XV52 (AlphaFold model)
Beta-2-microglobulin	B	protein	101	Homo sapiens	P61769 (AlphaFold model)
GTPase KRas	C	protein	10	Homo sapiens	P01116 (AlphaFold model)
R302 Fab light chain	D	protein	224	Homo sapiens
R302 Fab heavy chain	E	protein	225	Homo sapiens

Sequence of entity 1 (A), FASTA

>9NFB_1 MHC class I antigen (chains A)
MGSHSMRYFFTSVSRPGRGEPRFIAVGYVDDTQFVRFDSDAASQRMEPRAPWIEQEGPEY
WDGETRKVKAHSQTHRVDLGTLRGYYNQSEAGSHTVQRMYGCDVGSDWRFLRGYHQYAYD
GKDYIALKEDLRSWTAADMAAQTTKHKWEAAHVAEQLRAYLEGTCVEWLRRYLENGKETL
QRTDAPKTHMTHHAVSDHEATLRCWALSFYPAEITLTWQRDGEDQTQDTELVETRPAGDG
TFQKWAAVVVPSGQEQRYTCHVQHEGLPKPLTLRWEGGGSGLNDIFEAQKIEWHEGGGSH
HHHHHHH

Sequence of entity 2 (B), FASTA

>9NFB_2 Beta-2-microglobulin (chains B)
GSIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSK
DWSFYLLYYTEFTPTEKDEYACRVNHVTLSQPKIVKWDRDM

Sequence of entity 3 (C), FASTA

>9NFB_3 GTPase KRas (chains C)
KLVVVGACGV

Sequence of entity 4 (D), FASTA

>9NFB_4 R302 Fab light chain (chains D)
DIVMTQSPATLSLSPGERATLSCRASQSLSSSFLAWYQQKPGQAPRLLIYGASSRATGIP
DRFSGSGSGTDFTLTISRLEPEDFAVYYCQQSESALTFGGGTKVEIKRTVAAPSVFIFPP
SDSQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLT
LSKADYEKHKVYACEVTHQGLSSPVTKSFNRGECGGGGSLPETG

Sequence of entity 5 (E), FASTA

>9NFB_5 R302 Fab heavy chain (chains E)
EVQLLESGGGVVQPGRSLRLSCAASGFTFSSYGMHWVRQAPGKGLEWVAVISYDGSNKYY
ADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCLYGGNSYGMDVWGQGTMVTVFNQI
KGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLY
SLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHT

Ligands and cofactors

ID	Name	Formula	Copies
A1AWR	1-{(3S)-4-[(7M)-7-[6-amino-4-methyl-3-(trifluoromethyl)pyridin-2-yl]-6-chloro-8…	C29 H34 Cl F4 N7 O2	1

Primary citation

Engineered antibodies that stabilize drug-modified KRAS G12C neoantigens enable selective and potent cross-HLA immunotherapy. Maso, L., Mosure, S.A., Rodriguez-Aponte, S.A. et al. Nat Commun (2025) 16:11264-11264. DOI 10.1038/s41467-025-66132-w · PubMed

Other PDB entries of the same protein (UniProt A0A6S7XV52 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7SR5 2.35 Å, Single chain trimer HLA-A*02:01 (Y108C, A163C) with Wilms tumor protein peptide RMFPNAPYL
7SR3 2.49 Å, Single chain trimer HLA-A*02:01 (H98L, Y108C) with HPV.16 E7 peptide YMLDLQPETTDL
7SQP 2.53 Å, Single chain trimer HLA-A*02:01 (Y108C) with HPV.16 E7 peptide YMLDLQPETTDL
7SR0 2.54 Å, Single chain trimer HLA-A*02:01 (H98L, Y108C) with HPV.16 E7 peptide YMLDLQPET
7SR4 2.59 Å, Single chain trimer HLA-A*02:01 (H98L, Y108C) with HPV.16 E7 peptide YMLDLQPETTDLYC

Browse structure collections

About this viewer

MolViewer shows 9NFB directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.