Structural features of residue 112 in chain A

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Hydrophobic Interactions:
LEU A 3	VAL A 112	Dist=6.032	INTRA-CHAIN
LEU A 5	VAL A 112	Dist=6.274	INTRA-CHAIN
VAL A 112	ALA B 126	Dist=6.569	INTER-CHAIN
VAL A 112	LEU B 127	Dist=4.859	INTER-CHAIN

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Protrusion Index:
VAL A 112 N	-0.35
VAL A 112 CA	-0.40
VAL A 112 C	-0.39
VAL A 112 O	-0.33
VAL A 112 CB	-0.46
VAL A 112 CG1	-0.49
VAL A 112 CG2	-0.47
VAL A 112 H	-0.33
VAL A 112 HA	-0.42
VAL A 112 HB	-0.44
VAL A 112 HG11	-0.49
VAL A 112 HG12	-0.51
VAL A 112 HG13	-0.51
VAL A 112 HG21	-0.48
VAL A 112 HG22	-0.49
VAL A 112 HG23	-0.45

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Short Contacts:
VAL A 112 O	LEU B 127 H	-0.120	INTER-CHAIN
VAL A 112 H	LEU B 127 O	-0.140	INTER-CHAIN

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Van der Waal's Interactions:
LEU A 5 HD23 83	VAL A 112 HG23 1735	-0.000	INTRA-CHAIN
ALA A 22 HB3 316	VAL A 112 HG23 1735	-0.000	INTRA-CHAIN
MET A 39 HE3 602	VAL A 112 HG23 1735	-0.002	INTRA-CHAIN
ASN A 40 HD22 616	VAL A 112 HG23 1735	-0.000	INTRA-CHAIN
GLU A 41 HG3 631	VAL A 112 HG23 1735	-0.000	INTRA-CHAIN
THR A 66 HG23 1084	VAL A 112 HG23 1735	-0.000	INTRA-CHAIN
PHE A 93 HZ 1461	VAL A 112 HG23 1735	-0.000	INTRA-CHAIN
VAL A 95 HG23 1489	VAL A 112 HG23 1735	-0.000	INTRA-CHAIN
PHE A 110 HZ 1708	VAL A 112 HG23 1735	-0.000	INTRA-CHAIN
SER A 111 HG 1719	VAL A 112 HG23 1735	-0.000	INTRA-CHAIN