FMO DATABASE

FMODB ID: 5J3QZ

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	OptH
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	-2047615.275057
FMO2-HF: Nuclear repulsion	1975105.788798
FMO2-HF: Total energy	-72509.486259
FMO2-MP2: Total energy	-72723.0919

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.
-14.097	-2.927	9.301	-5.933	-14.537	-0.032

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 : -0.021 / q_NPA : -0.019

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	-0.734	-0.846	3.292	-4.579	-2.659	0.117	-0.998	-1.038	-0.001
4	A	118	LEU	0	0.010	0.004	5.859	0.546	0.546	0.000	0.000	0.000	0.000
5	A	119	ALA	0	-0.081	-0.060	6.941	0.350	0.350	0.000	0.000	0.000	0.000
6	A	120	GLU	-1	-0.908	-0.957	7.110	-1.502	-1.502	0.000	0.000	0.000	0.000
7	A	121	GLN	0	-0.068	-0.023	2.905	0.097	1.198	0.401	-0.434	-1.068	-0.003
8	A	122	PHE	0	-0.015	-0.019	7.189	0.245	0.245	0.000	0.000	0.000	0.000
9	A	123	ALA	0	0.004	0.009	10.829	-0.101	-0.101	0.000	0.000	0.000	0.000
10	A	124	PRO	0	-0.020	-0.039	14.124	0.045	0.045	0.000	0.000	0.000	0.000
11	A	125	PRO	0	0.006	0.037	17.283	-0.007	-0.007	0.000	0.000	0.000	0.000
12	A	126	ASP	-1	-0.925	-0.945	14.014	-0.160	-0.160	0.000	0.000	0.000	0.000
13	A	127	ILE	0	-0.005	-0.026	15.057	-0.040	-0.040	0.000	0.000	0.000	0.000
14	A	128	ALA	0	-0.019	-0.013	11.300	-0.026	-0.026	0.000	0.000	0.000	0.000
15	A	129	PRO	0	0.040	0.037	6.789	0.058	0.058	0.000	0.000	0.000	0.000
16	A	130	PRO	0	0.098	0.033	8.101	0.106	0.106	0.000	0.000	0.000	0.000
17	A	131	LEU	0	-0.028	-0.009	3.174	-0.429	0.026	0.100	-0.097	-0.458	0.000
18	A	132	LEU	0	0.020	0.013	6.709	0.061	0.061	0.000	0.000	0.000	0.000
19	A	133	ILE	0	0.017	0.012	8.092	0.011	0.011	0.000	0.000	0.000	0.000
20	A	134	LYS	1	0.970	0.993	9.317	-0.296	-0.296	0.000	0.000	0.000	0.000
21	A	135	LEU	0	-0.014	-0.011	6.414	-0.016	-0.016	0.000	0.000	0.000	0.000
22	A	136	VAL	0	-0.040	-0.013	10.506	-0.024	-0.024	0.000	0.000	0.000	0.000
23	A	137	GLU	-1	-0.883	-0.950	13.257	0.020	0.020	0.000	0.000	0.000	0.000
24	A	138	ALA	0	-0.046	-0.015	13.734	-0.004	-0.004	0.000	0.000	0.000	0.000
25	A	139	ILE	0	0.002	0.001	11.880	-0.015	-0.015	0.000	0.000	0.000	0.000
26	A	140	GLU	-1	-0.846	-0.917	15.987	-0.053	-0.053	0.000	0.000	0.000	0.000
27	A	141	LYS	1	0.882	0.954	17.082	-0.127	-0.127	0.000	0.000	0.000	0.000
28	A	142	LYS	1	0.843	0.939	17.335	-0.166	-0.166	0.000	0.000	0.000	0.000
29	A	143	GLY	0	0.016	0.003	19.683	0.002	0.002	0.000	0.000	0.000	0.000
30	A	144	LEU	0	0.005	0.013	20.629	-0.011	-0.011	0.000	0.000	0.000	0.000
31	A	145	GLU	-1	-0.947	-0.988	22.526	0.005	0.005	0.000	0.000	0.000	0.000
32	A	146	CYM	-1	-0.826	-0.881	21.487	0.053	0.053	0.000	0.000	0.000	0.000
33	A	147	SER	0	-0.027	-0.016	22.695	-0.005	-0.005	0.000	0.000	0.000	0.000
34	A	148	THR	0	-0.023	-0.021	22.115	0.000	0.000	0.000	0.000	0.000	0.000
35	A	149	LEU	0	0.030	0.015	16.510	0.005	0.005	0.000	0.000	0.000	0.000
36	A	150	TYR	0	-0.012	0.008	12.735	-0.031	-0.031	0.000	0.000	0.000	0.000
37	A	151	ARG	1	0.865	0.921	16.520	-0.003	-0.003	0.000	0.000	0.000	0.000
38	A	152	THR	0	-0.006	0.003	17.970	0.003	0.003	0.000	0.000	0.000	0.000
39	A	153	GLN	0	-0.106	-0.032	13.787	-0.013	-0.013	0.000	0.000	0.000	0.000
40	A	154	SER	0	-0.073	-0.041	14.547	0.006	0.006	0.000	0.000	0.000	0.000
41	A	155	SER	0	0.008	-0.011	16.990	-0.013	-0.013	0.000	0.000	0.000	0.000
42	A	156	SER	0	0.004	0.015	13.533	-0.001	-0.001	0.000	0.000	0.000	0.000
43	A	157	ASN	0	0.053	0.029	13.924	-0.076	-0.076	0.000	0.000	0.000	0.000
44	A	158	LEU	0	0.046	-0.005	9.412	0.054	0.054	0.000	0.000	0.000	0.000
45	A	159	ALA	0	-0.073	-0.029	9.250	-0.039	-0.039	0.000	0.000	0.000	0.000
46	A	160	GLU	-1	-0.867	-0.936	10.450	0.568	0.568	0.000	0.000	0.000	0.000
47	A	161	LEU	0	-0.021	-0.024	8.333	0.073	0.073	0.000	0.000	0.000	0.000
48	A	162	ARG	1	0.847	0.908	5.763	-1.220	-1.220	0.000	0.000	0.000	0.000
49	A	163	GLN	0	-0.009	0.002	6.113	0.423	0.423	0.000	0.000	0.000	0.000
50	A	164	LEU	0	0.030	0.009	7.891	-0.057	-0.057	0.000	0.000	0.000	0.000
51	A	165	LEU	0	-0.069	-0.003	2.190	-1.068	-0.450	1.395	-0.493	-1.520	0.000
52	A	166	ASP	-1	-0.917	-0.998	3.890	0.949	1.275	0.006	-0.098	-0.234	0.000
53	A	167	CYS	0	-0.029	0.022	5.051	-0.020	-0.020	0.000	0.000	0.000	0.000
54	A	168	ASP	-1	-0.984	-1.008	6.371	0.385	0.385	0.000	0.000	0.000	0.000
55	A	169	THR	0	-0.054	-0.063	10.106	0.016	0.016	0.000	0.000	0.000	0.000
56	A	170	PRO	0	-0.050	0.024	9.990	0.074	0.074	0.000	0.000	0.000	0.000
57	A	171	SER	0	0.005	-0.005	8.952	-0.059	-0.059	0.000	0.000	0.000	0.000
58	A	172	VAL	0	0.004	0.015	10.854	-0.067	-0.067	0.000	0.000	0.000	0.000
59	A	173	ASP	-1	-0.816	-0.892	12.685	0.251	0.251	0.000	0.000	0.000	0.000
60	A	174	LEU	0	0.018	-0.021	9.575	-0.031	-0.031	0.000	0.000	0.000	0.000
61	A	175	GLU	-1	-0.891	-0.980	13.489	0.108	0.108	0.000	0.000	0.000	0.000
62	A	176	MET	0	-0.066	-0.025	16.894	-0.022	-0.022	0.000	0.000	0.000	0.000
63	A	177	ILE	0	-0.061	-0.016	12.932	0.003	0.003	0.000	0.000	0.000	0.000
64	A	178	ASP	-1	-0.834	-0.926	16.073	0.141	0.141	0.000	0.000	0.000	0.000
65	A	179	VAL	0	0.076	0.022	15.919	0.022	0.022	0.000	0.000	0.000	0.000
66	A	180	HIS	1	0.874	0.925	15.621	-0.098	-0.098	0.000	0.000	0.000	0.000
67	A	181	VAL	0	0.064	0.034	12.632	-0.003	-0.003	0.000	0.000	0.000	0.000
68	A	182	LEU	0	-0.005	0.009	11.357	0.051	0.051	0.000	0.000	0.000	0.000
69	A	183	ALA	0	-0.011	-0.006	10.721	0.000	0.000	0.000	0.000	0.000	0.000
70	A	184	ASP	-1	-0.750	-0.866	11.098	0.127	0.127	0.000	0.000	0.000	0.000
71	A	185	ALA	0	-0.001	-0.002	7.556	-0.010	-0.010	0.000	0.000	0.000	0.000
72	A	186	PHE	0	-0.031	-0.019	6.188	0.056	0.056	0.000	0.000	0.000	0.000
73	A	187	LYS	1	0.898	0.929	6.815	-0.059	-0.059	0.000	0.000	0.000	0.000
74	A	188	ARG	1	0.797	0.919	5.048	-0.226	-0.226	0.000	0.000	0.000	0.000
75	A	189	TYR	0	0.048	0.011	2.163	-2.440	-0.821	2.504	-1.327	-2.797	-0.002
76	A	190	LEU	0	-0.004	-0.004	3.176	-1.297	-0.833	0.392	0.182	-1.038	-0.007
77	A	191	LEU	0	-0.064	-0.038	5.667	-0.348	-0.348	0.000	0.000	0.000	0.000
78	A	192	ASP	-1	-0.769	-0.887	2.491	-0.369	0.392	1.789	-0.625	-1.925	0.001
79	A	193	LEU	0	-0.052	-0.005	2.575	-7.875	-4.765	2.517	-1.980	-3.648	-0.020
80	A	194	PRO	0	0.037	0.048	3.013	1.084	1.792	0.081	-0.061	-0.727	0.000
81	A	195	ASN	0	-0.038	-0.013	5.326	0.974	1.062	-0.001	-0.002	-0.084	0.000
82	A	196	PRO	0	-0.028	-0.021	7.601	-0.254	-0.254	0.000	0.000	0.000	0.000
83	A	197	VAL	0	0.034	0.009	8.166	0.029	0.029	0.000	0.000	0.000	0.000
84	A	198	ILE	0	-0.019	-0.003	10.144	0.080	0.080	0.000	0.000	0.000	0.000
85	A	199	PRO	0	0.018	0.008	12.738	-0.008	-0.008	0.000	0.000	0.000	0.000
86	A	200	ALA	0	0.065	0.018	13.762	0.100	0.100	0.000	0.000	0.000	0.000
87	A	201	ALA	0	0.010	0.003	15.700	0.070	0.070	0.000	0.000	0.000	0.000
88	A	202	VAL	0	0.040	0.026	17.213	0.052	0.052	0.000	0.000	0.000	0.000
89	A	203	TYR	0	0.018	0.001	16.925	0.053	0.053	0.000	0.000	0.000	0.000
90	A	204	SER	0	-0.014	-0.006	18.903	0.054	0.054	0.000	0.000	0.000	0.000
91	A	205	GLU	-1	-0.887	-0.954	21.324	-0.257	-0.257	0.000	0.000	0.000	0.000
92	A	206	MET	0	-0.071	-0.008	21.024	0.026	0.026	0.000	0.000	0.000	0.000
93	A	207	ILE	0	-0.027	-0.005	22.194	0.027	0.027	0.000	0.000	0.000	0.000
94	A	208	SER	0	-0.052	-0.029	24.946	0.024	0.024	0.000	0.000	0.000	0.000
95	A	209	LEU	0	0.072	0.034	26.998	0.014	0.014	0.000	0.000	0.000	0.000
96	A	210	ALA	0	-0.046	-0.009	27.399	0.012	0.012	0.000	0.000	0.000	0.000
97	A	211	PRO	0	-0.043	-0.026	29.153	0.011	0.011	0.000	0.000	0.000	0.000
98	A	212	GLU	-1	-0.961	-0.978	32.053	-0.157	-0.157	0.000	0.000	0.000	0.000
99	A	213	VAL	0	-0.110	-0.039	29.248	0.003	0.003	0.000	0.000	0.000	0.000
100	A	214	GLN	0	0.049	0.034	32.511	0.001	0.001	0.000	0.000	0.000	0.000
101	A	215	SER	0	-0.085	-0.067	33.402	0.006	0.006	0.000	0.000	0.000	0.000
102	A	216	SER	0	0.003	-0.010	29.857	-0.013	-0.013	0.000	0.000	0.000	0.000
103	A	217	GLU	-1	-0.815	-0.912	28.994	-0.161	-0.161	0.000	0.000	0.000	0.000
104	A	218	GLU	-1	-0.828	-0.894	29.101	-0.145	-0.145	0.000	0.000	0.000	0.000
105	A	219	TYR	0	0.003	-0.013	25.229	-0.015	-0.015	0.000	0.000	0.000	0.000
106	A	220	ILE	0	0.016	0.001	24.236	-0.024	-0.024	0.000	0.000	0.000	0.000
107	A	221	GLN	0	-0.113	-0.086	24.449	-0.029	-0.029	0.000	0.000	0.000	0.000
108	A	222	LEU	0	-0.004	0.010	25.306	-0.012	-0.012	0.000	0.000	0.000	0.000
109	A	223	LEU	0	0.061	0.032	18.468	-0.024	-0.024	0.000	0.000	0.000	0.000
110	A	224	LYS	1	0.909	0.956	21.025	0.178	0.178	0.000	0.000	0.000	0.000
111	A	225	LYS	1	0.922	0.961	22.176	0.191	0.191	0.000	0.000	0.000	0.000
112	A	226	LEU	0	0.022	0.004	21.350	-0.013	-0.013	0.000	0.000	0.000	0.000
113	A	227	ILE	0	-0.032	-0.011	14.511	-0.024	-0.024	0.000	0.000	0.000	0.000
114	A	228	ARG	1	0.881	0.949	18.203	0.241	0.241	0.000	0.000	0.000	0.000
115	A	229	SER	0	-0.009	0.016	20.645	0.027	0.027	0.000	0.000	0.000	0.000
116	A	230	PRO	0	0.057	-0.001	20.351	-0.026	-0.026	0.000	0.000	0.000	0.000
117	A	231	SER	0	-0.059	-0.016	19.618	0.008	0.008	0.000	0.000	0.000	0.000
118	A	232	ILE	0	-0.043	-0.009	14.757	-0.072	-0.072	0.000	0.000	0.000	0.000
119	A	233	PRO	0	0.015	0.014	13.174	0.055	0.055	0.000	0.000	0.000	0.000
120	A	234	HIS	0	0.064	0.013	15.194	-0.043	-0.043	0.000	0.000	0.000	0.000
121	A	235	GLN	0	0.043	0.016	10.860	0.063	0.063	0.000	0.000	0.000	0.000
122	A	236	TYR	0	-0.059	-0.047	9.243	-0.004	-0.004	0.000	0.000	0.000	0.000
123	A	237	TRP	0	0.033	0.011	12.604	0.050	0.050	0.000	0.000	0.000	0.000
124	A	238	LEU	0	-0.045	-0.014	14.217	0.040	0.040	0.000	0.000	0.000	0.000
125	A	239	THR	0	0.036	0.008	8.292	0.052	0.052	0.000	0.000	0.000	0.000
126	A	240	LEU	0	-0.004	-0.008	11.654	0.051	0.051	0.000	0.000	0.000	0.000
127	A	241	GLN	0	-0.016	-0.021	13.659	0.071	0.071	0.000	0.000	0.000	0.000
128	A	242	TYR	0	0.001	0.016	11.966	0.046	0.046	0.000	0.000	0.000	0.000
129	A	243	LEU	0	-0.003	-0.016	9.564	0.051	0.051	0.000	0.000	0.000	0.000
130	A	244	LEU	0	-0.010	0.007	13.727	0.036	0.036	0.000	0.000	0.000	0.000
131	A	245	LYS	1	1.008	1.004	17.250	0.216	0.216	0.000	0.000	0.000	0.000
132	A	246	HIS	1	0.817	0.897	14.155	0.088	0.088	0.000	0.000	0.000	0.000
133	A	247	PHE	0	0.002	-0.025	13.122	0.025	0.025	0.000	0.000	0.000	0.000
134	A	248	PHE	0	0.053	0.032	18.349	0.018	0.018	0.000	0.000	0.000	0.000
135	A	249	LYS	1	0.941	0.986	20.199	0.057	0.057	0.000	0.000	0.000	0.000
136	A	250	LEU	0	-0.016	-0.015	17.249	0.013	0.013	0.000	0.000	0.000	0.000
137	A	251	SER	0	-0.047	-0.006	21.621	0.009	0.009	0.000	0.000	0.000	0.000
138	A	252	GLN	0	-0.011	-0.017	24.184	0.010	0.010	0.000	0.000	0.000	0.000
139	A	253	THR	0	-0.047	-0.015	25.263	0.008	0.008	0.000	0.000	0.000	0.000
140	A	254	SER	0	0.007	-0.006	25.837	0.007	0.007	0.000	0.000	0.000	0.000
141	A	255	SER	0	-0.082	-0.033	27.001	0.004	0.004	0.000	0.000	0.000	0.000
142	A	256	LYS	1	0.925	0.972	27.934	0.005	0.005	0.000	0.000	0.000	0.000
143	A	257	ASN	0	0.031	0.011	22.947	-0.003	-0.003	0.000	0.000	0.000	0.000
144	A	258	LEU	0	-0.023	-0.013	24.260	0.001	0.001	0.000	0.000	0.000	0.000
145	A	259	LEU	0	-0.042	-0.014	19.552	-0.008	-0.008	0.000	0.000	0.000	0.000
146	A	260	ASN	0	0.064	0.049	23.318	-0.012	-0.012	0.000	0.000	0.000	0.000
147	A	261	ALA	0	0.060	0.007	22.413	-0.005	-0.005	0.000	0.000	0.000	0.000
148	A	262	ARG	1	0.730	0.844	22.262	0.111	0.111	0.000	0.000	0.000	0.000
149	A	263	VAL	0	0.024	0.019	21.427	-0.010	-0.010	0.000	0.000	0.000	0.000
150	A	264	LEU	0	-0.002	-0.010	17.567	-0.007	-0.007	0.000	0.000	0.000	0.000
151	A	265	SER	0	-0.026	-0.014	17.795	-0.032	-0.032	0.000	0.000	0.000	0.000
152	A	266	GLU	-1	-0.866	-0.950	18.683	-0.131	-0.131	0.000	0.000	0.000	0.000
153	A	267	ILE	0	-0.055	-0.008	14.985	-0.007	-0.007	0.000	0.000	0.000	0.000
154	A	268	PHE	0	-0.016	-0.041	11.654	-0.010	-0.010	0.000	0.000	0.000	0.000
155	A	269	SER	0	0.029	0.029	13.740	-0.071	-0.071	0.000	0.000	0.000	0.000
156	A	270	PRO	0	0.009	-0.005	15.050	-0.058	-0.058	0.000	0.000	0.000	0.000
157	A	271	MET	0	-0.053	-0.031	9.727	-0.044	-0.044	0.000	0.000	0.000	0.000
158	A	272	LEU	0	-0.044	-0.018	10.039	-0.147	-0.147	0.000	0.000	0.000	0.000
159	A	273	PHE	0	0.032	0.010	11.917	-0.086	-0.086	0.000	0.000	0.000	0.000
160	A	274	ARG	1	0.807	0.902	5.791	1.912	1.912	0.000	0.000	0.000	0.000
161	A	275	PHE	0	0.001	0.003	12.903	0.022	0.022	0.000	0.000	0.000	0.000
162	A	276	SER	0	-0.001	0.010	15.447	0.007	0.007	0.000	0.000	0.000	0.000
163	A	277	ALA	0	-0.017	-0.024	17.388	0.031	0.031	0.000	0.000	0.000	0.000
164	A	278	ALA	0	0.011	0.024	20.334	0.009	0.009	0.000	0.000	0.000	0.000
165	A	279	SER	0	0.053	0.026	22.222	0.012	0.012	0.000	0.000	0.000	0.000
166	A	280	SER	0	0.051	0.012	24.982	-0.012	-0.012	0.000	0.000	0.000	0.000
167	A	281	ASP	-1	-0.832	-0.913	26.563	-0.131	-0.131	0.000	0.000	0.000	0.000
168	A	282	ASN	0	-0.033	-0.010	24.110	-0.008	-0.008	0.000	0.000	0.000	0.000
169	A	283	THR	0	-0.053	-0.026	21.440	-0.022	-0.022	0.000	0.000	0.000	0.000
170	A	284	GLU	-1	-0.804	-0.887	22.935	-0.144	-0.144	0.000	0.000	0.000	0.000
171	A	285	ASN	0	-0.018	-0.019	25.343	0.008	0.008	0.000	0.000	0.000	0.000
172	A	286	LEU	0	-0.032	-0.019	19.740	-0.006	-0.006	0.000	0.000	0.000	0.000
173	A	287	ILE	0	0.026	0.023	20.519	-0.013	-0.013	0.000	0.000	0.000	0.000
174	A	288	LYS	1	0.924	0.984	21.925	0.129	0.129	0.000	0.000	0.000	0.000
175	A	289	VAL	0	0.003	0.007	21.472	0.005	0.005	0.000	0.000	0.000	0.000
176	A	290	ILE	0	-0.013	-0.007	17.134	0.000	0.000	0.000	0.000	0.000	0.000
177	A	291	GLU	-1	-0.825	-0.926	20.460	-0.114	-0.114	0.000	0.000	0.000	0.000
178	A	292	ILE	0	-0.029	-0.014	22.889	0.013	0.013	0.000	0.000	0.000	0.000
179	A	293	LEU	0	-0.003	-0.015	19.972	0.005	0.005	0.000	0.000	0.000	0.000
180	A	294	ILE	0	-0.017	0.007	18.802	0.006	0.006	0.000	0.000	0.000	0.000
181	A	295	SER	0	-0.062	-0.038	21.738	0.014	0.014	0.000	0.000	0.000	0.000
182	A	296	THR	0	-0.055	-0.031	25.001	0.007	0.007	0.000	0.000	0.000	0.000
183	A	297	GLU	-1	-0.886	-0.941	20.805	-0.187	-0.187	0.000	0.000	0.000	0.000
184	A	298	TRP	0	-0.120	-0.042	24.220	0.012	0.012	0.000	0.000	0.000	0.000

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