1. Complex: Neisseria meningitidis factor H binding protein in complex with monoclonal antibody JAR5

• CATH

• Resolution:  3 Å

• Species: Neisseria meningitidis, Mus musculus 

2. Antigen:  Factor H binding protein (fHbp)

• structure length (residues): 253

• mutations: No

• Uniprot

3. Antibody: monoclonal antibody JAR5

• Isotype/subclass: IgG2b

• Structure: Fab only

3.1 Heavy chain 

• structure length (residues): 212

• mutations: No

• disulfide bridges: 22-96, 143-198

• CDR (residue numbering): 28, 32, 33, 99, 103, 106, 108

3.2 Light chain

• structure length (residues): 216

• mutations: No

• disulfide bridges: 23-93, 139-199

• CDR (residue numbering): 

RCSB PDB - 5T5F - Neisseria meningitidis factor H binding protein in complex with monoclonal antibody JAR5

Neisseria meningitidis factor H binding protein in complex with monoclonal antibody JAR5 (310K, 37°C, 100 ns) RMSD, SASA, RMSF, Rg, H-bonds

Neisseria meningitidis factor H binding protein in complex with monoclonal antibody JAR5 (311K, 38°C, 100 ns) RMSD, SASA, RMSF, Rg, H-bonds

Neisseria meningitidis factor H binding protein in complex with monoclonal antibody JAR5 (312K, 39°C, 100 ns) RMSD, SASA, RMSF, Rg, H-bonds

Neisseria meningitidis factor H binding protein in complex with monoclonal antibody JAR5 (313K, 40°C, 100 ns) RMSD, SASA, RMSF, Rg, H-bonds

1. Complex: Fab fragment (MN14C11.6) in complex with a peptide antigen derived from Neisseria meningitidis P1.7 serosubtype antigen and domain II from Streptococcal protein G

• CATH

• Resolution: 1.95 Å

• Species: Mus musculus, Neisseria meningitidis. 

2. Antigen: G-prime protein

• structure length (residues): 64

• mutations: 1

• Uniprot

2.1 Antigen: Major Outer membrane protein P 1.16 (antigen peptide)

• structure length (residues): 10

• mutations: No

• Uniprot

3. Antibody: MN14C11.6 mAb

• Isotype/subclass: IgG2a

• Structure: Fab only

3.1 Heavy chain 

• structure length (residues): 219

• mutations: No

• disulfide bridges: 22-96, 146-201

3.2 Light chain

• structure length (residues): 217

• mutations: No

• disulfide bridges: 23-93, 138-198

RCSB PDB - 1QKZ - Crystal Structure of an Fab Fragment in Complex with a Meningococcal Serosubtype Antigen and a Protein G Domain

Fab Fragment in Complex with a Meningococcal Serosubtype Antigen and a Protein G Domain (310K, 37°C, 100 ns) RMSD, SASA, RMSF, Rg, H-bonds

Fab Fragment in Complex with a Meningococcal Serosubtype Antigen and a Protein G Domain (311K, 38°C, 100 ns) RMSD, SASA, RMSF, Rg, H-bonds

Fab Fragment in Complex with a Meningococcal Serosubtype Antigen and a Protein G Domain (312K, 39°C, 100 ns) RMSD, SASA, RMSF, Rg, H-bonds

Fab Fragment in Complex with a Meningococcal Serosubtype Antigen and a Protein G Domain (313K, 40°C, 100 ns) RMSD, SASA, RMSF, Rg, H-bonds

1. Complex: Factor H-binding protein from Neisseria meningitides in complex with mAb 1A12

• Resolution: 2.19 Å

• Species: Neisseria meningitides MC58

2. Antigen: Factor H binding protein variant 1.1 

• structure length (residues): 257

• mutations: No

• Uniprot

3. Antibody: mAb 1A12

• Isotype/subclass: IgG2a

• Structure: Fab only

3.1 Heavy chain 

• structure length (residues): 235

• mutations: No

• disulfide bridges: 22-96, 149-205

• CDR (residue numbering): 31-33, 52, 54, 55, 57, 101, 103-107

3.2 Light chain

• structure length (residues): 217

• mutations: No

• disulfide bridges: 24-89, 136-196

• CDR (residue numbering): 31, 32, 50, 92, 97

RCSB PDB - 5O14 - Factor H-binding protein from Neisseria meningitides in complex with mAb 1A12

Factor H-binding protein from Neisseria meningitides in complex with mAb 1A12 (310K, 37°C, 100 ns) RMSD, SASA, RMSF, Rg, H-bonds

Factor H-binding protein from Neisseria meningitides in complex with mAb 1A12 (311K, 38°C, 100 ns) RMSD, SASA, RMSF, Rg, H-bonds

Factor H-binding protein from Neisseria meningitides in complex with mAb 1A12 (312K, 39°C, 100 ns) RMSD, SASA, RMSF, Rg, H-bonds

Factor H-binding protein from Neisseria meningitides in complex with mAb 1A12 (313K, 40°C, 100 ns) RMSD, SASA, RMSF, Rg, H-bonds