2O3L

crystal structure of a duf1048 protein with a left-handed superhelix fold (bce_3448) from bacillus cereus atcc 10987 at 2.05 a resolution

• Total interactions analyzed: 1
• Total true interactions: 1
• Strongest Interaction:
  • Chains: A-B
  • Int. Res.: 60
  • Norm. En. per Res.: -2.9166
• Hub Node: A(1)

All Interactions

Chains	Hydro. Bond Ener. (kJ/mol)	Elec. Ener. (kJ/mol)	VDW. Ener. (kJ/mol)	Tot. Stab. Ener. (kJ/mol)	#int. res.	# Short cont.	#Hydr. int.	#VDW pairs	#salt bridges	#Pot. fav. elec. int	#Pot. unfav. elec. int
A-B	-31.0459	-14.5709	-129.378	-174.9949	60	2	3	4774	0	17	10

Interface residues

• A-B: ALA20B, ALA45B, ALA64A, ALA66A, ALA67A, ALA89A, ALA91A, ARG21B, ARG70A, ASN38B, ASN42B, ASN47B, ASN90A, ASP50A, ASP50B, ASP60A, ASP74A, GLN37B, GLN55B, GLN71A, GLU14A, GLU14B, GLU57A, GLU63A, GLU68A, GLU86A, GLY46B, GLY48B, GLY65A, GLY69A, GLY77A, HIS53A, HIS53B, ILE54A, ILE59A, ILE75A, LEU52A, LEU52B, LEU58A, LEU61A, LEU73A, LEU87A, LYS16B, LYS92B, PHE43B, PHE62A, PHE83A, SER44B, THR76A, THR93A, TRP41B, TYR15B, TYR29A, TYR39B, TYR56A, TYR56B, TYR94A, TYR94B, VAL72A, VAL95A