PDBe < PISA < EMBL-EBI

PISA Interface List.

Session Map (id=166-43-6AI)

Interfaces in PDB 1dyc crystal.
Space symmetry group: P 32 2 1. Resolution: 2.10 Å

DETERMINATION OF ALPHA-HELIX PROPENSITY WITHIN THE CONTEXT OF A FOLDED PROTEIN: SITES 44 AND 131 IN BACTERIOPHAGE T4 LYSOZYME

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	`75`	`24`	`8525`	`◊`	A	x-y,-y,-z+1/3	`5_555`	`75`	`24`	`8525`	`720.0`	`-2.8`	`0.396`	`8`	`4`	`0`	`0.000`
`2`		A	`47`	`14`	`8525`	`x`	A	y,x-1,-z	`4_545`	`39`	`12`	`8525`	`373.5`	`1.5`	`0.713`	`4`	`4`	`0`	`0.000`
`3`		A	`49`	`12`	`8525`	`x`	A	-y+1,x-y,z-1/3	`2_654`	`42`	`13`	`8525`	`373.3`	`1.9`	`0.727`	`9`	`0`	`0`	`0.000`
`4`		A	`8`	`2`	`8525`	`◊`	A	-x+2,-x+y+1,-z+2/3	`6_765`	`8`	`2`	`8525`	`90.0`	`0.6`	`0.717`	`0`	`0`	`0`	`0.000`
`5`		[BME]A:900	`4`	`1`	`205`	`◊`	A	x-y,-y,-z+1/3	`5_555`	`15`	`7`	`8525`	`79.7`	`-0.6`	`0.364`	`0`	`0`	`0`	`0.000`
`6`		[BME]A:900	`4`	`1`	`205`	`◊`	A	x,y,z	`1_555`	`10`	`7`	`8525`	`64.3`	`-0.2`	`0.327`	`0`	`0`	`0`	`0.000`
`7`		[CL]A:173	`1`	`1`	`125`	`f`	A	x,y,z	`1_555`	`11`	`5`	`8525`	`61.8`	`-9.2`	`0.000`	`0`	`0`	`0`	`0.057`
`8`		[CL]A:178	`1`	`1`	`125`	`f`	A	-y+1,x-y,z-1/3	`2_654`	`8`	`5`	`8525`	`56.0`	`-6.9`	`0.000`	`0`	`0`	`0`	`0.043`
`9`		[CL]A:178	`1`	`1`	`125`	`◊`	A	x,y,z	`1_555`	`10`	`4`	`8525`	`46.8`	`-5.9`	`0.000`	`0`	`0`	`0`	`0.000`
`10`		[BME]A:900	`4`	`1`	`205`	`f`	[BME]A:900	x-y,-y,-z+1/3	`5_555`	`4`	`1`	`205`	`40.5`	`-2.0`	`0.262`	`1`	`0`	`0`	`0.100`
`11`		A	`5`	`3`	`8525`	`◊`	[CL]A:173	y,x-1,-z	`4_545`	`1`	`1`	`125`	`33.9`	`-4.1`	`0.000`	`0`	`0`	`0`	`0.000`

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

Protein Data Bank
in Europe