FMO DATABASE

FMODB ID: YVY72

Calculation Name: 1PBW-A-Xray372

Preferred Name: PI3-kinase p85-alpha subunit

Target Type: SINGLE PROTEIN

Ligand Name:

ligand 3-letter code:

PDB ID: 1PBW

Chain ID: A

ChEMBL ID: CHEMBL2506

UniProt ID: P27986

Base Structure: X-ray

Registration Date: 2023-09-21

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptHSide
Protonation	MOE:Protonate 3D
Complement	MOE:Structure Preparation
Water	No
Procedure	Auto-FMO protocol ver. 2.20220422

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	184
LigandCharge	CYM=-1
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-2045995.658144
FMO2-HF: Nuclear repulsion	1973484.517647
FMO2-HF: Total energy	-72511.140497
FMO2-MP2: Total energy	-72724.658159

3D Structure

Snapshot

Ligand structure

Ligand Interaction

Ligand binding energy

IFIE [kcal/mol]	PIEDA [kcal/mol]				Charge transfer value [e]
IFIE SUMIFIE SUM at MP2 level.	ESElectro static interaction energy.	EXExchange-repulsion energy.	CT+mixCharge transfer and mixing terms energy.	DI(MP2)Dispersion energy.	q(I=>J)Charge transfer value from I to J fragments.
N/A	N/A	N/A	N/A	N/A	N/A

Interactive mode: IFIE and PIEDA for fragment #1(A:115:LEU)

Summations of interaction energy for fragment #1(A:115:LEU)

IFIE [kcal/mol]	PIEDA [kcal/mol]				Charge transfer value [e]
IFIE SUMIFIE SUM at MP2 level.	ESElectro static interaction energy.	EXExchange-repulsion energy.	CT+mixCharge transfer and mixing terms energy.	DI(MP2)Dispersion energy.	q(I=>J)Charge transfer value from I to J fragments.
-14.295	-2.581	8.14	-5.687	-14.165	-0.03

Interaction energy analysis for fragmet #1(A:115:LEU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.041 / q_NPA : -0.022

Distance from base fragment(s) [Å]

Dist

Interaction energy by IFIE and PIEDA
[kcal/mol]

| Total | > | ES | > | EX | >
| CT+mix | > | DI(MP2) | >

Fragment charge [e]

FCHARGE q_Mulliken
q_NPA q(I=>J)

Residue

Res # RES

Sort

Graph Options

X Axis Label
Y Axis Max Y Axis Min
Display ES EX CT+mix DI(MP2)

frag_NumFragment number.	ChainChain species.	Res #Residue number.	RES3-letter code of amino acid residue, ligand and solvent molecule.	FCHARGEFormal charge [e].	q_MullikenFragment charge evaluated by Mulliken charge [e].	q_NPAFragment charge evaluated by natural population analysis(NPA) charge [e].	DISTDistance from Ligand [Å].	TotalIFIE at MP2 level [kcal/mol].	ESElectro static interaction energy by PIEDA [kcal/mol].	EXExchange-repulsion energy by PIEDA [kcal/mol].	CT+mixCharge transfer and mixing terms energy by PIEDA [kcal/mol].	DI(MP2)Dispersion energy by PIEDA [kcal/mol].	q(I=>J)Charge transfer value from I to J fragmens [e].
3	A	117	ASP	-1	-0.739	-0.857	3.150	-4.911	-2.982	0.132	-0.998	-1.064	-0.002
4	A	118	LEU	0	0.003	0.005	5.591	0.449	0.449	0.000	0.000	0.000	0.000
5	A	119	ALA	0	-0.074	-0.062	6.825	0.337	0.337	0.000	0.000	0.000	0.000
6	A	120	GLU	-1	-0.881	-0.933	6.974	-1.474	-1.474	0.000	0.000	0.000	0.000
7	A	121	GLN	0	-0.062	-0.013	2.900	0.004	1.131	0.377	-0.429	-1.075	-0.003
8	A	122	PHE	0	-0.003	-0.007	7.277	0.241	0.241	0.000	0.000	0.000	0.000
9	A	123	ALA	0	-0.006	-0.002	10.901	-0.085	-0.085	0.000	0.000	0.000	0.000
10	A	124	PRO	0	0.000	-0.045	14.157	0.040	0.040	0.000	0.000	0.000	0.000
11	A	125	PRO	0	-0.036	0.028	17.303	-0.002	-0.002	0.000	0.000	0.000	0.000
12	A	126	ASP	-1	-0.892	-0.921	14.191	-0.219	-0.219	0.000	0.000	0.000	0.000
13	A	127	ILE	0	-0.005	-0.029	15.270	-0.035	-0.035	0.000	0.000	0.000	0.000
14	A	128	ALA	0	-0.024	-0.012	11.145	-0.021	-0.021	0.000	0.000	0.000	0.000
15	A	129	PRO	0	0.033	0.031	6.945	0.063	0.063	0.000	0.000	0.000	0.000
16	A	130	PRO	0	0.093	0.032	8.383	0.087	0.087	0.000	0.000	0.000	0.000
17	A	131	LEU	0	-0.019	0.003	3.123	-0.394	0.055	0.087	-0.091	-0.445	0.000
18	A	132	LEU	0	0.015	0.008	6.730	0.074	0.074	0.000	0.000	0.000	0.000
19	A	133	ILE	0	0.016	0.007	8.082	0.035	0.035	0.000	0.000	0.000	0.000
20	A	134	LYS	1	0.880	0.945	9.187	-0.230	-0.230	0.000	0.000	0.000	0.000
21	A	135	LEU	0	-0.014	-0.012	6.229	0.009	0.009	0.000	0.000	0.000	0.000
22	A	136	VAL	0	-0.037	-0.014	10.652	-0.007	-0.007	0.000	0.000	0.000	0.000
23	A	137	GLU	-1	-0.896	-0.956	13.043	-0.034	-0.034	0.000	0.000	0.000	0.000
24	A	138	ALA	0	-0.030	-0.011	13.963	0.005	0.005	0.000	0.000	0.000	0.000
25	A	139	ILE	0	-0.021	-0.008	11.587	-0.004	-0.004	0.000	0.000	0.000	0.000
26	A	140	GLU	-1	-0.817	-0.877	15.771	-0.098	-0.098	0.000	0.000	0.000	0.000
27	A	141	LYS	1	0.830	0.921	17.593	-0.043	-0.043	0.000	0.000	0.000	0.000
28	A	142	LYS	1	0.815	0.889	17.260	-0.101	-0.101	0.000	0.000	0.000	0.000
29	A	143	GLY	0	0.008	0.001	19.424	0.004	0.004	0.000	0.000	0.000	0.000
30	A	144	LEU	0	-0.002	0.010	20.355	-0.009	-0.009	0.000	0.000	0.000	0.000
31	A	145	GLU	-1	-0.893	-0.948	22.278	-0.020	-0.020	0.000	0.000	0.000	0.000
32	A	146	CYM	-1	-0.809	-0.839	21.289	0.014	0.014	0.000	0.000	0.000	0.000
33	A	147	SER	0	-0.018	-0.014	22.595	-0.006	-0.006	0.000	0.000	0.000	0.000
34	A	148	THR	0	-0.056	-0.059	22.254	0.000	0.000	0.000	0.000	0.000	0.000
35	A	149	LEU	0	0.044	0.018	15.917	0.003	0.003	0.000	0.000	0.000	0.000
36	A	150	TYR	0	-0.012	-0.011	12.345	-0.020	-0.020	0.000	0.000	0.000	0.000
37	A	151	ARG	1	0.853	0.924	16.573	0.031	0.031	0.000	0.000	0.000	0.000
38	A	152	THR	0	-0.020	-0.001	18.078	0.007	0.007	0.000	0.000	0.000	0.000
39	A	153	GLN	0	-0.090	-0.037	14.418	-0.016	-0.016	0.000	0.000	0.000	0.000
40	A	154	SER	0	-0.070	-0.053	14.350	0.010	0.010	0.000	0.000	0.000	0.000
41	A	155	SER	0	0.017	-0.010	16.948	-0.009	-0.009	0.000	0.000	0.000	0.000
42	A	156	SER	0	-0.028	-0.018	13.412	0.002	0.002	0.000	0.000	0.000	0.000
43	A	157	ASN	0	0.029	0.029	14.106	-0.038	-0.038	0.000	0.000	0.000	0.000
44	A	158	LEU	0	0.045	-0.006	9.407	0.044	0.044	0.000	0.000	0.000	0.000
45	A	159	ALA	0	-0.048	-0.016	9.186	-0.019	-0.019	0.000	0.000	0.000	0.000
46	A	160	GLU	-1	-0.816	-0.895	10.305	0.447	0.447	0.000	0.000	0.000	0.000
47	A	161	LEU	0	-0.016	-0.020	8.226	0.054	0.054	0.000	0.000	0.000	0.000
48	A	162	ARG	1	0.803	0.853	5.319	-0.874	-0.874	0.000	0.000	0.000	0.000
49	A	163	GLN	0	-0.037	-0.017	5.839	0.353	0.353	0.000	0.000	0.000	0.000
50	A	164	LEU	0	0.013	0.009	7.889	-0.046	-0.046	0.000	0.000	0.000	0.000
51	A	165	LEU	0	-0.063	-0.006	2.212	-1.404	-0.418	1.364	-0.500	-1.850	-0.001
52	A	166	ASP	-1	-0.844	-0.951	3.655	0.498	1.009	0.019	-0.201	-0.329	-0.001
53	A	167	CYS	0	-0.019	0.017	4.541	-0.108	-0.010	-0.001	-0.006	-0.091	0.000
54	A	168	ASP	-1	-0.965	-0.995	6.251	0.315	0.315	0.000	0.000	0.000	0.000
55	A	169	THR	0	-0.052	-0.064	9.921	0.054	0.054	0.000	0.000	0.000	0.000
56	A	170	PRO	0	-0.028	0.026	9.937	0.077	0.077	0.000	0.000	0.000	0.000
57	A	171	SER	0	-0.023	-0.004	8.554	-0.035	-0.035	0.000	0.000	0.000	0.000
58	A	172	VAL	0	-0.008	0.000	10.576	-0.047	-0.047	0.000	0.000	0.000	0.000
59	A	173	ASP	-1	-0.828	-0.895	12.543	0.165	0.165	0.000	0.000	0.000	0.000
60	A	174	LEU	0	0.031	-0.009	9.452	-0.016	-0.016	0.000	0.000	0.000	0.000
61	A	175	GLU	-1	-0.769	-0.903	13.556	0.050	0.050	0.000	0.000	0.000	0.000
62	A	176	MET	0	-0.070	-0.021	16.917	-0.013	-0.013	0.000	0.000	0.000	0.000
63	A	177	ILE	0	-0.050	-0.010	13.003	0.004	0.004	0.000	0.000	0.000	0.000
64	A	178	ASP	-1	-0.772	-0.898	16.201	0.087	0.087	0.000	0.000	0.000	0.000
65	A	179	VAL	0	0.030	0.008	15.916	0.013	0.013	0.000	0.000	0.000	0.000
66	A	180	HIS	1	0.872	0.927	15.372	-0.058	-0.058	0.000	0.000	0.000	0.000
67	A	181	VAL	0	0.044	0.025	12.589	-0.003	-0.003	0.000	0.000	0.000	0.000
68	A	182	LEU	0	-0.012	0.006	11.288	0.035	0.035	0.000	0.000	0.000	0.000
69	A	183	ALA	0	-0.012	-0.011	10.473	-0.011	-0.011	0.000	0.000	0.000	0.000
70	A	184	ASP	-1	-0.763	-0.860	11.070	0.051	0.051	0.000	0.000	0.000	0.000
71	A	185	ALA	0	0.002	0.004	7.555	-0.014	-0.014	0.000	0.000	0.000	0.000
72	A	186	PHE	0	-0.019	-0.012	6.044	0.034	0.034	0.000	0.000	0.000	0.000
73	A	187	LYS	1	0.912	0.951	6.859	-0.042	-0.042	0.000	0.000	0.000	0.000
74	A	188	ARG	1	0.844	0.920	5.183	-0.063	-0.063	0.000	0.000	0.000	0.000
75	A	189	TYR	0	0.035	-0.008	2.316	-1.916	-1.054	3.642	-1.214	-3.290	-0.003
76	A	190	LEU	0	0.000	0.000	2.975	-1.575	-1.005	0.289	0.021	-0.879	-0.006
77	A	191	LEU	0	-0.043	-0.017	5.682	-0.326	-0.326	0.000	0.000	0.000	0.000
78	A	192	ASP	-1	-0.752	-0.831	2.538	-0.650	0.533	0.626	-0.398	-1.410	0.001
79	A	193	LEU	0	-0.036	0.008	2.647	-6.829	-3.666	1.539	-1.734	-2.967	-0.015
80	A	194	PRO	0	0.022	0.044	2.988	0.925	1.669	0.067	-0.134	-0.677	0.000
81	A	195	ASN	0	-0.047	-0.029	5.239	0.963	1.055	-0.001	-0.003	-0.088	0.000
82	A	196	PRO	0	-0.025	-0.019	7.599	-0.268	-0.268	0.000	0.000	0.000	0.000
83	A	197	VAL	0	0.038	0.009	8.567	0.022	0.022	0.000	0.000	0.000	0.000
84	A	198	ILE	0	-0.023	-0.005	10.471	0.077	0.077	0.000	0.000	0.000	0.000
85	A	199	PRO	0	0.027	0.018	12.677	0.002	0.002	0.000	0.000	0.000	0.000
86	A	200	ALA	0	0.061	0.010	13.761	0.091	0.091	0.000	0.000	0.000	0.000
87	A	201	ALA	0	0.011	0.006	15.741	0.063	0.063	0.000	0.000	0.000	0.000
88	A	202	VAL	0	0.032	0.023	17.326	0.046	0.046	0.000	0.000	0.000	0.000
89	A	203	TYR	0	0.026	0.006	17.285	0.046	0.046	0.000	0.000	0.000	0.000
90	A	204	SER	0	0.007	-0.002	19.185	0.043	0.043	0.000	0.000	0.000	0.000
91	A	205	GLU	-1	-0.928	-0.963	21.523	-0.245	-0.245	0.000	0.000	0.000	0.000
92	A	206	MET	0	-0.068	-0.014	21.339	0.025	0.025	0.000	0.000	0.000	0.000
93	A	207	ILE	0	-0.007	0.010	22.557	0.024	0.024	0.000	0.000	0.000	0.000
94	A	208	SER	0	-0.007	-0.006	25.227	0.014	0.014	0.000	0.000	0.000	0.000
95	A	209	LEU	0	0.007	0.004	27.010	0.013	0.013	0.000	0.000	0.000	0.000
96	A	210	ALA	0	-0.044	-0.006	27.581	0.010	0.010	0.000	0.000	0.000	0.000
97	A	211	PRO	0	-0.025	-0.019	29.377	0.009	0.009	0.000	0.000	0.000	0.000
98	A	212	GLU	-1	-0.970	-0.982	32.308	-0.143	-0.143	0.000	0.000	0.000	0.000
99	A	213	VAL	0	-0.092	-0.031	29.372	0.002	0.002	0.000	0.000	0.000	0.000
100	A	214	GLN	0	0.000	-0.008	32.682	-0.001	-0.001	0.000	0.000	0.000	0.000
101	A	215	SER	0	-0.069	-0.063	33.579	0.006	0.006	0.000	0.000	0.000	0.000
102	A	216	SER	0	0.048	0.008	29.365	-0.008	-0.008	0.000	0.000	0.000	0.000
103	A	217	GLU	-1	-0.862	-0.927	29.264	-0.168	-0.168	0.000	0.000	0.000	0.000
104	A	218	GLU	-1	-0.820	-0.872	29.398	-0.139	-0.139	0.000	0.000	0.000	0.000
105	A	219	TYR	0	0.005	-0.010	25.096	-0.015	-0.015	0.000	0.000	0.000	0.000
106	A	220	ILE	0	0.027	0.001	24.595	-0.022	-0.022	0.000	0.000	0.000	0.000
107	A	221	GLN	0	-0.074	-0.061	24.740	-0.030	-0.030	0.000	0.000	0.000	0.000
108	A	222	LEU	0	0.004	0.012	25.610	-0.011	-0.011	0.000	0.000	0.000	0.000
109	A	223	LEU	0	0.054	0.031	18.713	-0.021	-0.021	0.000	0.000	0.000	0.000
110	A	224	LYS	1	0.864	0.927	21.325	0.174	0.174	0.000	0.000	0.000	0.000
111	A	225	LYS	1	0.932	0.967	22.403	0.182	0.182	0.000	0.000	0.000	0.000
112	A	226	LEU	0	0.017	0.007	21.378	-0.011	-0.011	0.000	0.000	0.000	0.000
113	A	227	ILE	0	-0.036	-0.014	14.870	-0.021	-0.021	0.000	0.000	0.000	0.000
114	A	228	ARG	1	0.898	0.955	18.370	0.241	0.241	0.000	0.000	0.000	0.000
115	A	229	SER	0	0.008	0.018	20.698	0.028	0.028	0.000	0.000	0.000	0.000
116	A	230	PRO	0	0.026	-0.012	20.491	-0.027	-0.027	0.000	0.000	0.000	0.000
117	A	231	SER	0	-0.055	-0.018	19.924	0.007	0.007	0.000	0.000	0.000	0.000
118	A	232	ILE	0	-0.037	0.000	15.116	-0.060	-0.060	0.000	0.000	0.000	0.000
119	A	233	PRO	0	0.018	0.013	13.161	0.042	0.042	0.000	0.000	0.000	0.000
120	A	234	HIS	0	0.051	0.008	15.123	-0.042	-0.042	0.000	0.000	0.000	0.000
121	A	235	GLN	0	0.049	0.021	10.814	0.073	0.073	0.000	0.000	0.000	0.000
122	A	236	TYR	0	-0.047	-0.029	9.486	0.033	0.033	0.000	0.000	0.000	0.000
123	A	237	TRP	0	0.035	0.015	12.761	0.042	0.042	0.000	0.000	0.000	0.000
124	A	238	LEU	0	-0.037	-0.010	14.170	0.037	0.037	0.000	0.000	0.000	0.000
125	A	239	THR	0	0.014	-0.009	8.400	0.031	0.031	0.000	0.000	0.000	0.000
126	A	240	LEU	0	0.002	-0.005	11.693	0.047	0.047	0.000	0.000	0.000	0.000
127	A	241	GLN	0	-0.039	-0.035	13.817	0.072	0.072	0.000	0.000	0.000	0.000
128	A	242	TYR	0	0.021	0.026	11.600	0.042	0.042	0.000	0.000	0.000	0.000
129	A	243	LEU	0	-0.017	-0.025	9.578	0.051	0.051	0.000	0.000	0.000	0.000
130	A	244	LEU	0	-0.002	0.011	13.794	0.038	0.038	0.000	0.000	0.000	0.000
131	A	245	LYS	1	0.929	0.964	17.365	0.242	0.242	0.000	0.000	0.000	0.000
132	A	246	HIS	1	0.808	0.904	13.848	0.151	0.151	0.000	0.000	0.000	0.000
133	A	247	PHE	0	-0.001	-0.022	13.264	0.026	0.026	0.000	0.000	0.000	0.000
134	A	248	PHE	0	0.053	0.029	18.438	0.019	0.019	0.000	0.000	0.000	0.000
135	A	249	LYS	1	0.894	0.937	19.898	0.103	0.103	0.000	0.000	0.000	0.000
136	A	250	LEU	0	-0.019	-0.016	17.135	0.014	0.014	0.000	0.000	0.000	0.000
137	A	251	SER	0	-0.030	0.010	21.578	0.010	0.010	0.000	0.000	0.000	0.000
138	A	252	GLN	0	-0.044	-0.033	24.263	0.013	0.013	0.000	0.000	0.000	0.000
139	A	253	THR	0	-0.054	-0.024	25.111	0.009	0.009	0.000	0.000	0.000	0.000
140	A	254	SER	0	-0.001	0.010	26.038	0.006	0.006	0.000	0.000	0.000	0.000
141	A	255	SER	0	-0.049	-0.024	26.955	0.003	0.003	0.000	0.000	0.000	0.000
142	A	256	LYS	1	0.882	0.933	27.696	0.024	0.024	0.000	0.000	0.000	0.000
143	A	257	ASN	0	0.030	0.004	22.850	-0.001	-0.001	0.000	0.000	0.000	0.000
144	A	258	LEU	0	-0.017	-0.015	24.239	-0.001	-0.001	0.000	0.000	0.000	0.000
145	A	259	LEU	0	-0.066	-0.028	19.462	-0.006	-0.006	0.000	0.000	0.000	0.000
146	A	260	ASN	0	0.064	0.041	23.357	-0.013	-0.013	0.000	0.000	0.000	0.000
147	A	261	ALA	0	0.051	0.005	22.616	-0.006	-0.006	0.000	0.000	0.000	0.000
148	A	262	ARG	1	0.706	0.809	22.461	0.118	0.118	0.000	0.000	0.000	0.000
149	A	263	VAL	0	0.024	0.023	21.563	-0.009	-0.009	0.000	0.000	0.000	0.000
150	A	264	LEU	0	-0.007	-0.014	17.765	-0.007	-0.007	0.000	0.000	0.000	0.000
151	A	265	SER	0	-0.027	-0.012	17.881	-0.033	-0.033	0.000	0.000	0.000	0.000
152	A	266	GLU	-1	-0.827	-0.922	18.591	-0.141	-0.141	0.000	0.000	0.000	0.000
153	A	267	ILE	0	-0.072	-0.018	15.379	-0.006	-0.006	0.000	0.000	0.000	0.000
154	A	268	PHE	0	0.000	-0.032	11.553	-0.012	-0.012	0.000	0.000	0.000	0.000
155	A	269	SER	0	0.027	0.026	13.677	-0.068	-0.068	0.000	0.000	0.000	0.000
156	A	270	PRO	0	0.017	0.007	15.081	-0.052	-0.052	0.000	0.000	0.000	0.000
157	A	271	MET	0	-0.059	-0.035	9.763	-0.044	-0.044	0.000	0.000	0.000	0.000
158	A	272	LEU	0	-0.033	-0.013	10.137	-0.142	-0.142	0.000	0.000	0.000	0.000
159	A	273	PHE	0	0.027	0.006	11.966	-0.078	-0.078	0.000	0.000	0.000	0.000
160	A	274	ARG	1	0.789	0.882	5.916	1.854	1.854	0.000	0.000	0.000	0.000
161	A	275	PHE	0	0.010	0.001	13.161	0.027	0.027	0.000	0.000	0.000	0.000
162	A	276	SER	0	-0.010	0.012	15.991	0.003	0.003	0.000	0.000	0.000	0.000
163	A	277	ALA	0	-0.024	-0.031	17.729	0.027	0.027	0.000	0.000	0.000	0.000
164	A	278	ALA	0	0.007	0.025	20.652	0.008	0.008	0.000	0.000	0.000	0.000
165	A	279	SER	0	0.037	0.014	22.496	0.009	0.009	0.000	0.000	0.000	0.000
166	A	280	SER	0	0.046	0.016	25.179	-0.012	-0.012	0.000	0.000	0.000	0.000
167	A	281	ASP	-1	-0.803	-0.883	26.698	-0.135	-0.135	0.000	0.000	0.000	0.000
168	A	282	ASN	0	-0.001	0.001	24.327	-0.012	-0.012	0.000	0.000	0.000	0.000
169	A	283	THR	0	-0.039	-0.027	21.347	-0.021	-0.021	0.000	0.000	0.000	0.000
170	A	284	GLU	-1	-0.810	-0.885	23.024	-0.148	-0.148	0.000	0.000	0.000	0.000
171	A	285	ASN	0	-0.056	-0.048	25.386	0.002	0.002	0.000	0.000	0.000	0.000
172	A	286	LEU	0	-0.015	-0.006	19.947	-0.007	-0.007	0.000	0.000	0.000	0.000
173	A	287	ILE	0	0.008	0.013	20.400	-0.015	-0.015	0.000	0.000	0.000	0.000
174	A	288	LYS	1	0.882	0.944	21.925	0.132	0.132	0.000	0.000	0.000	0.000
175	A	289	VAL	0	0.007	0.005	21.674	0.003	0.003	0.000	0.000	0.000	0.000
176	A	290	ILE	0	-0.017	-0.007	17.417	-0.002	-0.002	0.000	0.000	0.000	0.000
177	A	291	GLU	-1	-0.792	-0.884	20.722	-0.127	-0.127	0.000	0.000	0.000	0.000
178	A	292	ILE	0	-0.013	-0.009	23.141	0.011	0.011	0.000	0.000	0.000	0.000
179	A	293	LEU	0	-0.005	-0.001	20.256	0.005	0.005	0.000	0.000	0.000	0.000
180	A	294	ILE	0	-0.023	0.000	18.814	0.004	0.004	0.000	0.000	0.000	0.000
181	A	295	SER	0	-0.059	-0.040	21.913	0.013	0.013	0.000	0.000	0.000	0.000
182	A	296	THR	0	-0.048	-0.035	25.162	0.007	0.007	0.000	0.000	0.000	0.000
183	A	297	GLU	-1	-0.837	-0.910	20.813	-0.210	-0.210	0.000	0.000	0.000	0.000
184	A	298	TRP	0	-0.099	-0.030	24.294	0.010	0.010	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:115:LEU)