PDBe < PISA < EMBL-EBI

PISA Interface List.

Session Map (id=439-41-51G)

Interfaces in PDB 1lav crystal.
Space symmetry group: P 21 21 21. Resolution: 1.80 Å

STABILIZATION OF ESCHERICHIA COLI RIBONUCLEASE HI BY CAVITY- FILLING MUTATIONS WITHIN A HYDROPHOBIC CORE

Interfaces

##		Structure 1				×	Structure 2						interface area, Å²	ΔⁱG kcal/mol	ΔⁱG P-value	N_HB	N_SB	N_DS	CSS
NN	«»	Range	ⁱN_at	ⁱN_res	Surface Å²	×	Range	Symmetry op-n	Sym.ID	ⁱN_at	ⁱN_res	Surface Å²	interface area, Å²	ΔⁱG kcal/mol	ΔⁱG P-value	N_HB	N_SB	N_DS	CSS
`1`		A	`68`	`17`	`8673`	`x`	A	x-1/2,-y+1/2,-z+1	`4_456`	`74`	`21`	`8673`	`599.7`	`0.1`	`0.589`	`13`	`5`	`0`	`0.000`
`2`		A	`47`	`16`	`8673`	`x`	A	-x-1/2,-y,z-1/2	`2_454`	`48`	`15`	`8673`	`458.4`	`-0.3`	`0.388`	`6`	`4`	`0`	`0.000`
`3`		A	`25`	`6`	`8673`	`x`	A	-x,y-1/2,-z+1/2	`3_545`	`20`	`5`	`8673`	`227.3`	`-2.1`	`0.302`	`2`	`2`	`0`	`0.000`
`4`		A	`29`	`7`	`8673`	`x`	A	x-1/2,-y+1/2,-z	`4_455`	`24`	`6`	`8673`	`208.8`	`-0.6`	`0.483`	`0`	`0`	`0`	`0.000`
`5`		A	`20`	`6`	`8673`	`x`	A	x,y,z-1	`1_554`	`14`	`4`	`8673`	`189.3`	`0.0`	`0.572`	`3`	`3`	`0`	`0.000`
`6`		A	`1`	`1`	`8673`	`x`	A	-x+1/2,-y,z-1/2	`2_554`	`3`	`1`	`8673`	`14.4`	`-0.0`	`0.343`	`0`	`0`	`0`	`0.000`

PDBe PISA v1.52 [20/10/2014]

Protein Data Bank
in Europe