FMO DATABASE

FMODB ID: 2NMYR

Calculation Name: 3FVW-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3FVW

Chain ID: A

ChEMBL ID:

UniProt ID: Q8DWD8

Base Structure: X-ray

Registration Date: 2023-09-23

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	OptAll
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	182
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1895907.193125
FMO2-HF: Nuclear repulsion	1826679.10464
FMO2-HF: Total energy	-69228.088485
FMO2-MP2: Total energy	-69434.980236

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:3:LYS)

Summations of interaction energy for fragment #1(A:3:LYS)

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.
-398.494	-395.998	42.342	-20.974	-23.864	-0.229

Interaction energy analysis for fragmet #1(A:3:LYS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.830 / q_NPA : 0.897

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	5	ILE	0	-0.012	-0.013	3.317	-2.174	0.186	0.017	-1.066	-1.312	0.004
4	A	6	LEU	0	0.017	0.026	5.636	2.287	2.287	0.000	0.000	0.000	0.000
5	A	7	PHE	0	0.007	-0.010	8.625	0.684	0.684	0.000	0.000	0.000	0.000
6	A	8	ILE	0	0.024	0.003	12.007	1.234	1.234	0.000	0.000	0.000	0.000
7	A	9	VAL	0	0.014	0.013	15.397	0.337	0.337	0.000	0.000	0.000	0.000
8	A	10	GLY	0	0.032	0.022	18.372	0.472	0.472	0.000	0.000	0.000	0.000
9	A	11	SER	0	-0.023	-0.031	21.492	0.752	0.752	0.000	0.000	0.000	0.000
10	A	12	PHE	0	0.068	0.045	22.590	-0.300	-0.300	0.000	0.000	0.000	0.000
11	A	13	SER	0	-0.025	0.003	24.966	0.097	0.097	0.000	0.000	0.000	0.000
12	A	14	GLU	-1	-0.815	-0.909	22.417	-12.932	-12.932	0.000	0.000	0.000	0.000
13	A	15	GLY	0	0.072	0.023	23.925	-0.403	-0.403	0.000	0.000	0.000	0.000
14	A	16	SER	0	-0.014	0.016	23.544	-0.030	-0.030	0.000	0.000	0.000	0.000
15	A	17	PHE	0	0.042	0.006	23.493	-0.518	-0.518	0.000	0.000	0.000	0.000
16	A	18	ASN	0	0.053	0.026	20.890	-0.773	-0.773	0.000	0.000	0.000	0.000
17	A	19	ARG	1	0.877	0.932	19.231	12.408	12.408	0.000	0.000	0.000	0.000
18	A	20	GLN	0	-0.058	-0.042	19.140	-0.594	-0.594	0.000	0.000	0.000	0.000
19	A	21	LEU	0	-0.007	-0.007	17.610	-0.252	-0.252	0.000	0.000	0.000	0.000
20	A	22	ALA	0	0.036	0.031	15.345	-0.752	-0.752	0.000	0.000	0.000	0.000
21	A	23	LYS	1	0.906	0.945	14.606	13.366	13.366	0.000	0.000	0.000	0.000
22	A	24	LYS	1	0.835	0.932	15.704	13.184	13.184	0.000	0.000	0.000	0.000
23	A	25	ALA	0	0.028	0.008	12.729	-0.492	-0.492	0.000	0.000	0.000	0.000
24	A	26	GLU	-1	-0.823	-0.890	10.692	-20.676	-20.676	0.000	0.000	0.000	0.000
25	A	27	THR	0	-0.062	-0.041	10.903	-1.087	-1.087	0.000	0.000	0.000	0.000
26	A	28	ILE	0	-0.061	-0.017	11.791	-0.165	-0.165	0.000	0.000	0.000	0.000
27	A	29	ILE	0	-0.023	-0.006	6.080	-1.395	-1.395	0.000	0.000	0.000	0.000
28	A	30	GLY	0	-0.009	-0.003	7.998	-2.061	-2.061	0.000	0.000	0.000	0.000
29	A	31	ASP	-1	-0.936	-0.966	7.323	-29.498	-29.498	0.000	0.000	0.000	0.000
30	A	32	ARG	1	0.765	0.860	4.763	31.000	31.151	-0.001	-0.016	-0.134	0.000
31	A	33	ALA	0	0.000	-0.009	2.399	-14.609	-12.627	2.515	-1.686	-2.810	-0.008
32	A	34	GLN	0	-0.026	0.004	3.066	6.425	6.284	0.022	0.843	-0.724	-0.001
33	A	35	VAL	0	0.016	0.015	5.343	-0.603	-0.551	-0.001	-0.008	-0.042	0.000
34	A	36	SER	0	-0.040	-0.010	8.095	0.872	0.872	0.000	0.000	0.000	0.000
35	A	37	TYR	0	-0.087	-0.082	10.864	0.035	0.035	0.000	0.000	0.000	0.000
36	A	38	LEU	0	0.022	0.027	13.954	0.714	0.714	0.000	0.000	0.000	0.000
37	A	39	SER	0	-0.036	-0.014	15.734	0.480	0.480	0.000	0.000	0.000	0.000
38	A	40	TYR	0	-0.006	-0.043	19.355	0.264	0.264	0.000	0.000	0.000	0.000
39	A	41	ASP	-1	-0.854	-0.923	21.752	-11.535	-11.535	0.000	0.000	0.000	0.000
40	A	42	ARG	1	0.782	0.872	24.807	11.112	11.112	0.000	0.000	0.000	0.000
41	A	43	VAL	0	0.039	0.026	22.875	-0.333	-0.333	0.000	0.000	0.000	0.000
42	A	44	PRO	0	0.012	0.028	26.227	0.247	0.247	0.000	0.000	0.000	0.000
43	A	45	PHE	0	-0.001	0.005	28.406	-0.288	-0.288	0.000	0.000	0.000	0.000
44	A	46	PHE	0	0.005	0.005	27.834	0.147	0.147	0.000	0.000	0.000	0.000
45	A	47	ASN	0	-0.044	-0.060	29.853	0.271	0.271	0.000	0.000	0.000	0.000
46	A	48	GLN	0	0.058	0.034	31.672	0.085	0.085	0.000	0.000	0.000	0.000
47	A	49	ASP	-1	-0.905	-0.930	33.528	-8.016	-8.016	0.000	0.000	0.000	0.000
48	A	50	LEU	0	-0.038	-0.010	32.164	0.084	0.084	0.000	0.000	0.000	0.000
49	A	51	GLU	-1	-0.849	-0.944	29.121	-10.244	-10.244	0.000	0.000	0.000	0.000
50	A	52	THR	0	-0.036	-0.009	29.853	-0.179	-0.179	0.000	0.000	0.000	0.000
51	A	53	SER	0	-0.056	-0.020	31.210	0.269	0.269	0.000	0.000	0.000	0.000
52	A	54	VAL	0	-0.025	-0.016	26.791	-0.308	-0.308	0.000	0.000	0.000	0.000
53	A	55	HIS	0	0.010	0.004	26.741	0.246	0.246	0.000	0.000	0.000	0.000
54	A	56	PRO	0	-0.015	-0.017	25.008	-0.442	-0.442	0.000	0.000	0.000	0.000
55	A	57	GLU	-1	-0.872	-0.941	23.143	-10.980	-10.980	0.000	0.000	0.000	0.000
56	A	58	VAL	0	0.005	-0.004	21.834	-0.540	-0.540	0.000	0.000	0.000	0.000
57	A	59	ALA	0	-0.035	-0.007	20.970	-0.511	-0.511	0.000	0.000	0.000	0.000
58	A	60	HIS	0	0.010	0.005	17.405	-0.578	-0.578	0.000	0.000	0.000	0.000
59	A	61	ALA	0	-0.002	-0.007	17.171	-0.807	-0.807	0.000	0.000	0.000	0.000
60	A	62	ARG	1	0.827	0.875	16.243	12.518	12.518	0.000	0.000	0.000	0.000
61	A	63	GLU	-1	-0.785	-0.869	15.411	-14.855	-14.855	0.000	0.000	0.000	0.000
62	A	64	GLU	-1	-0.889	-0.943	12.276	-21.026	-21.026	0.000	0.000	0.000	0.000
63	A	65	VAL	0	-0.036	-0.019	11.130	-1.791	-1.791	0.000	0.000	0.000	0.000
64	A	66	GLN	0	-0.014	-0.005	11.619	-0.649	-0.649	0.000	0.000	0.000	0.000
65	A	67	GLU	-1	-0.891	-0.941	9.155	-23.252	-23.252	0.000	0.000	0.000	0.000
66	A	68	ALA	0	-0.044	-0.014	6.593	-2.586	-2.586	0.000	0.000	0.000	0.000
67	A	69	ASP	-1	-0.817	-0.892	2.352	-53.882	-50.641	3.482	-3.424	-3.300	-0.037
68	A	70	ALA	0	-0.041	-0.021	5.539	1.594	1.594	0.000	0.000	0.000	0.000
69	A	71	ILE	0	-0.006	-0.006	6.966	0.931	0.931	0.000	0.000	0.000	0.000
70	A	72	TRP	0	-0.003	-0.017	9.261	-0.975	-0.975	0.000	0.000	0.000	0.000
71	A	73	ILE	0	-0.018	0.004	11.608	0.888	0.888	0.000	0.000	0.000	0.000
72	A	74	PHE	0	0.043	0.014	12.395	0.443	0.443	0.000	0.000	0.000	0.000
73	A	75	SER	0	-0.008	-0.015	17.497	0.568	0.568	0.000	0.000	0.000	0.000
74	A	76	PRO	0	-0.014	0.025	21.008	0.025	0.025	0.000	0.000	0.000	0.000
75	A	77	VAL	0	0.036	0.025	24.440	-0.171	-0.171	0.000	0.000	0.000	0.000
76	A	78	TYR	0	-0.064	-0.036	26.363	0.367	0.367	0.000	0.000	0.000	0.000
77	A	79	ASN	0	-0.032	-0.028	30.036	-0.015	-0.015	0.000	0.000	0.000	0.000
78	A	80	TYR	0	0.002	-0.002	30.029	0.269	0.269	0.000	0.000	0.000	0.000
79	A	81	ALA	0	0.027	0.038	28.300	-0.205	-0.205	0.000	0.000	0.000	0.000
80	A	82	ILE	0	0.006	-0.010	22.760	-0.164	-0.164	0.000	0.000	0.000	0.000
81	A	83	PRO	0	-0.058	-0.025	23.625	0.388	0.388	0.000	0.000	0.000	0.000
82	A	84	GLY	0	0.047	0.022	25.245	-0.243	-0.243	0.000	0.000	0.000	0.000
83	A	85	PRO	0	-0.012	-0.018	24.710	-0.065	-0.065	0.000	0.000	0.000	0.000
84	A	86	VAL	0	0.038	0.030	19.926	-0.196	-0.196	0.000	0.000	0.000	0.000
85	A	87	LYS	1	0.837	0.910	22.178	10.631	10.631	0.000	0.000	0.000	0.000
86	A	88	ASN	0	0.015	-0.005	24.568	0.136	0.136	0.000	0.000	0.000	0.000
87	A	89	LEU	0	-0.009	-0.001	18.147	0.010	0.010	0.000	0.000	0.000	0.000
88	A	90	LEU	0	0.037	0.013	17.996	-0.291	-0.291	0.000	0.000	0.000	0.000
89	A	91	ASP	-1	-0.818	-0.873	21.375	-11.104	-11.104	0.000	0.000	0.000	0.000
90	A	92	TRP	0	-0.024	-0.023	23.338	0.084	0.084	0.000	0.000	0.000	0.000
91	A	93	LEU	0	-0.009	-0.007	16.892	-0.080	-0.080	0.000	0.000	0.000	0.000
92	A	94	SER	0	-0.052	-0.029	20.024	-0.184	-0.184	0.000	0.000	0.000	0.000
93	A	95	ARG	1	0.836	0.918	21.896	11.543	11.543	0.000	0.000	0.000	0.000
94	A	96	SER	0	0.011	-0.001	22.598	-0.719	-0.719	0.000	0.000	0.000	0.000
95	A	97	LEU	0	-0.011	-0.023	18.020	0.149	0.149	0.000	0.000	0.000	0.000
96	A	98	ASP	-1	-0.866	-0.904	22.606	-10.285	-10.285	0.000	0.000	0.000	0.000
97	A	99	LEU	0	-0.015	-0.008	26.136	0.186	0.186	0.000	0.000	0.000	0.000
98	A	100	SER	0	-0.109	-0.074	29.500	0.464	0.464	0.000	0.000	0.000	0.000
99	A	101	ASP	-1	-0.850	-0.916	27.892	-10.366	-10.366	0.000	0.000	0.000	0.000
100	A	102	PRO	0	-0.028	-0.008	27.980	-0.402	-0.402	0.000	0.000	0.000	0.000
101	A	103	THR	0	-0.117	-0.069	28.575	0.010	0.010	0.000	0.000	0.000	0.000
102	A	104	GLY	0	0.013	0.027	25.644	-0.233	-0.233	0.000	0.000	0.000	0.000
103	A	105	PRO	0	-0.026	-0.017	19.958	-0.084	-0.084	0.000	0.000	0.000	0.000
104	A	106	SER	0	0.048	0.032	19.960	-0.143	-0.143	0.000	0.000	0.000	0.000
105	A	107	VAL	0	-0.014	-0.018	15.676	-0.501	-0.501	0.000	0.000	0.000	0.000
106	A	108	LEU	0	-0.013	-0.022	14.955	-1.135	-1.135	0.000	0.000	0.000	0.000
107	A	109	GLN	0	-0.073	-0.049	15.807	0.169	0.169	0.000	0.000	0.000	0.000
108	A	110	ASP	-1	-0.881	-0.930	13.893	-18.624	-18.624	0.000	0.000	0.000	0.000
109	A	111	LYS	1	0.794	0.908	9.446	22.415	22.415	0.000	0.000	0.000	0.000
110	A	112	ILE	0	0.023	0.021	6.780	1.448	1.448	0.000	0.000	0.000	0.000
111	A	113	VAL	0	-0.013	-0.002	9.770	-0.421	-0.421	0.000	0.000	0.000	0.000
112	A	114	THR	0	0.009	0.006	10.729	0.618	0.618	0.000	0.000	0.000	0.000
113	A	115	VAL	0	0.017	0.003	12.894	0.231	0.231	0.000	0.000	0.000	0.000
114	A	116	SER	0	0.009	0.027	15.616	-0.352	-0.352	0.000	0.000	0.000	0.000
115	A	117	SER	0	-0.046	-0.036	17.537	0.522	0.522	0.000	0.000	0.000	0.000
116	A	118	VAL	0	-0.046	-0.025	21.186	0.047	0.047	0.000	0.000	0.000	0.000
117	A	119	ALA	0	0.017	-0.001	23.881	0.302	0.302	0.000	0.000	0.000	0.000
118	A	120	ASN	0	-0.051	-0.046	27.283	-0.065	-0.065	0.000	0.000	0.000	0.000
119	A	121	GLY	0	0.048	0.036	29.942	0.168	0.168	0.000	0.000	0.000	0.000
120	A	122	ALA	0	-0.021	0.005	29.977	-0.112	-0.112	0.000	0.000	0.000	0.000
121	A	123	SER	0	0.001	-0.001	27.306	-0.560	-0.560	0.000	0.000	0.000	0.000
122	A	124	PRO	0	-0.057	-0.037	25.349	0.392	0.392	0.000	0.000	0.000	0.000
123	A	125	GLU	-1	-0.878	-0.933	25.221	-12.676	-12.676	0.000	0.000	0.000	0.000
124	A	126	GLU	-1	-0.857	-0.920	27.451	-9.308	-9.308	0.000	0.000	0.000	0.000
125	A	127	VAL	0	-0.058	-0.033	23.727	-0.108	-0.108	0.000	0.000	0.000	0.000
126	A	128	PHE	0	0.011	-0.007	20.065	-0.296	-0.296	0.000	0.000	0.000	0.000
127	A	129	GLU	-1	-0.853	-0.920	22.960	-10.876	-10.876	0.000	0.000	0.000	0.000
128	A	130	ASP	-1	-0.817	-0.905	25.065	-11.435	-11.435	0.000	0.000	0.000	0.000
129	A	131	TYR	0	0.029	0.008	19.641	-0.348	-0.348	0.000	0.000	0.000	0.000
130	A	132	ARG	1	0.787	0.843	20.377	13.365	13.365	0.000	0.000	0.000	0.000
131	A	133	SER	0	-0.052	-0.022	21.574	-0.096	-0.096	0.000	0.000	0.000	0.000
132	A	134	LEU	0	0.002	-0.006	22.519	-0.077	-0.077	0.000	0.000	0.000	0.000
133	A	135	LEU	0	-0.005	-0.009	16.373	-0.077	-0.077	0.000	0.000	0.000	0.000
134	A	136	PRO	0	0.045	0.021	18.939	-0.341	-0.341	0.000	0.000	0.000	0.000
135	A	137	PHE	0	-0.070	-0.012	19.900	0.211	0.211	0.000	0.000	0.000	0.000
136	A	138	ILE	0	-0.061	-0.041	19.327	0.310	0.310	0.000	0.000	0.000	0.000
137	A	139	ARG	1	0.920	0.965	19.435	12.848	12.848	0.000	0.000	0.000	0.000
138	A	140	MET	0	0.030	0.047	13.569	-0.396	-0.396	0.000	0.000	0.000	0.000
139	A	141	HIS	0	0.005	-0.003	11.870	1.000	1.000	0.000	0.000	0.000	0.000
140	A	142	LEU	0	-0.030	-0.022	12.501	-1.636	-1.636	0.000	0.000	0.000	0.000
141	A	143	VAL	0	0.012	0.003	9.657	0.456	0.456	0.000	0.000	0.000	0.000
142	A	144	ASP	-1	-0.816	-0.878	13.103	-15.334	-15.334	0.000	0.000	0.000	0.000
143	A	145	GLN	0	-0.046	-0.023	13.131	1.252	1.252	0.000	0.000	0.000	0.000
144	A	146	LEU	0	-0.038	-0.008	15.638	-0.454	-0.454	0.000	0.000	0.000	0.000
145	A	147	THR	0	0.024	0.005	16.037	1.045	1.045	0.000	0.000	0.000	0.000
146	A	148	GLY	0	0.027	0.014	18.518	0.049	0.049	0.000	0.000	0.000	0.000
147	A	149	VAL	0	-0.037	-0.030	20.833	0.174	0.174	0.000	0.000	0.000	0.000
148	A	150	PRO	0	0.030	0.021	23.681	0.213	0.213	0.000	0.000	0.000	0.000
149	A	151	ILE	0	-0.009	-0.005	26.995	-0.204	-0.204	0.000	0.000	0.000	0.000
150	A	152	ASN	0	-0.023	-0.013	28.685	0.026	0.026	0.000	0.000	0.000	0.000
151	A	153	SER	0	0.027	-0.009	30.861	0.107	0.107	0.000	0.000	0.000	0.000
152	A	154	GLU	-1	-0.719	-0.851	32.436	-9.392	-9.392	0.000	0.000	0.000	0.000
153	A	155	ALA	0	-0.042	0.027	29.802	0.035	0.035	0.000	0.000	0.000	0.000
154	A	156	TRP	0	-0.006	-0.013	31.578	-0.019	-0.019	0.000	0.000	0.000	0.000
155	A	157	SER	0	-0.040	-0.014	34.507	0.146	0.146	0.000	0.000	0.000	0.000
156	A	158	THR	0	-0.017	-0.049	32.263	-0.052	-0.052	0.000	0.000	0.000	0.000
157	A	159	GLY	0	0.034	0.032	31.047	-0.098	-0.098	0.000	0.000	0.000	0.000
158	A	160	ILE	0	-0.018	-0.002	26.632	-0.380	-0.380	0.000	0.000	0.000	0.000
159	A	161	LEU	0	0.023	0.015	22.640	0.282	0.282	0.000	0.000	0.000	0.000
160	A	162	LYS	1	0.736	0.860	25.291	9.654	9.654	0.000	0.000	0.000	0.000
161	A	163	VAL	0	0.014	0.002	21.277	0.180	0.180	0.000	0.000	0.000	0.000
162	A	164	SER	0	-0.017	-0.030	24.468	-0.026	-0.026	0.000	0.000	0.000	0.000
163	A	165	ALA	0	0.039	-0.001	23.068	-0.487	-0.487	0.000	0.000	0.000	0.000
164	A	166	GLU	-1	-0.807	-0.871	21.969	-12.595	-12.595	0.000	0.000	0.000	0.000
165	A	167	LYS	1	0.827	0.885	21.189	12.609	12.609	0.000	0.000	0.000	0.000
166	A	168	LEU	0	-0.020	-0.005	17.957	-0.623	-0.623	0.000	0.000	0.000	0.000
167	A	169	ALA	0	0.007	0.010	17.363	-1.055	-1.055	0.000	0.000	0.000	0.000
168	A	170	GLU	-1	-0.831	-0.887	16.534	-15.094	-15.094	0.000	0.000	0.000	0.000
169	A	171	LEU	0	0.012	0.014	14.678	-0.947	-0.947	0.000	0.000	0.000	0.000
170	A	172	SER	0	-0.039	-0.037	12.888	-1.436	-1.436	0.000	0.000	0.000	0.000
171	A	173	ALA	0	0.042	0.014	11.748	-2.009	-2.009	0.000	0.000	0.000	0.000
172	A	174	GLN	0	0.002	0.000	11.817	-0.418	-0.418	0.000	0.000	0.000	0.000
173	A	175	ALA	0	0.011	-0.003	9.230	-1.800	-1.800	0.000	0.000	0.000	0.000
174	A	176	ASP	-1	-0.805	-0.886	7.443	-34.570	-34.570	0.000	0.000	0.000	0.000
175	A	177	ALA	0	-0.036	0.000	7.073	-3.730	-3.730	0.000	0.000	0.000	0.000
176	A	178	LEU	0	-0.010	0.000	5.584	-1.569	-1.569	0.000	0.000	0.000	0.000
177	A	179	LEU	0	0.006	-0.010	2.681	-4.586	-3.655	0.495	-0.219	-1.206	-0.001
178	A	180	SER	0	-0.017	-0.030	2.725	-15.067	-13.181	0.401	-0.993	-1.295	-0.014
179	A	181	ALA	0	-0.051	-0.015	5.337	0.474	0.510	-0.001	-0.003	-0.031	0.000
180	A	182	ILE	0	-0.003	-0.006	2.117	-0.513	0.138	4.231	-0.903	-3.979	-0.011
181	A	183	GLU	-1	-0.823	-0.870	1.760	-152.372	-161.090	31.179	-13.485	-8.977	-0.161
182	A	184	ASN	0	-0.158	-0.076	4.073	14.793	14.858	0.003	-0.014	-0.054	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:3:LYS)