FMO DATABASE

FMODB ID: 76K9K

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1889334.89899
FMO2-HF: Nuclear repulsion	1820107.410802
FMO2-HF: Total energy	-69227.488188
FMO2-MP2: Total energy	-69434.450276

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.
-398.563	-395.947	40.015	-21.375	-21.251	-0.222

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 : 0.820 / q_NPA : 0.886

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	-0.018	-0.010	3.328	-1.901	0.756	0.001	-1.218	-1.440	0.005
4	A	6	LEU	0	0.028	0.032	5.647	2.172	2.172	0.000	0.000	0.000	0.000
5	A	7	PHE	0	-0.003	-0.019	8.791	0.277	0.277	0.000	0.000	0.000	0.000
6	A	8	ILE	0	0.049	0.016	11.942	1.133	1.133	0.000	0.000	0.000	0.000
7	A	9	VAL	0	0.016	0.008	15.413	0.171	0.171	0.000	0.000	0.000	0.000
8	A	10	GLY	0	0.026	0.026	18.443	0.505	0.505	0.000	0.000	0.000	0.000
9	A	11	SER	0	-0.058	-0.061	21.608	0.736	0.736	0.000	0.000	0.000	0.000
10	A	12	PHE	0	0.076	0.044	22.599	-0.269	-0.269	0.000	0.000	0.000	0.000
11	A	13	SER	0	-0.046	-0.003	24.951	0.134	0.134	0.000	0.000	0.000	0.000
12	A	14	GLU	-1	-0.877	-0.964	23.439	-12.327	-12.327	0.000	0.000	0.000	0.000
13	A	15	GLY	0	0.051	0.035	24.477	-0.308	-0.308	0.000	0.000	0.000	0.000
14	A	16	SER	0	-0.025	0.003	23.211	-0.108	-0.108	0.000	0.000	0.000	0.000
15	A	17	PHE	0	0.055	0.012	23.545	-0.420	-0.420	0.000	0.000	0.000	0.000
16	A	18	ASN	0	0.064	0.028	20.677	-0.713	-0.713	0.000	0.000	0.000	0.000
17	A	19	ARG	1	0.903	0.948	19.093	12.351	12.351	0.000	0.000	0.000	0.000
18	A	20	GLN	0	-0.044	-0.029	18.893	-0.616	-0.616	0.000	0.000	0.000	0.000
19	A	21	LEU	0	-0.016	-0.006	17.698	-0.246	-0.246	0.000	0.000	0.000	0.000
20	A	22	ALA	0	0.039	0.019	15.188	-0.733	-0.733	0.000	0.000	0.000	0.000
21	A	23	LYS	1	0.977	0.998	14.480	13.421	13.421	0.000	0.000	0.000	0.000
22	A	24	LYS	1	0.876	0.953	15.362	13.083	13.083	0.000	0.000	0.000	0.000
23	A	25	ALA	0	0.026	0.020	12.508	-0.602	-0.602	0.000	0.000	0.000	0.000
24	A	26	GLU	-1	-0.808	-0.890	10.726	-20.504	-20.504	0.000	0.000	0.000	0.000
25	A	27	THR	0	-0.061	-0.033	10.748	-0.793	-0.793	0.000	0.000	0.000	0.000
26	A	28	ILE	0	-0.075	-0.025	11.724	-0.287	-0.287	0.000	0.000	0.000	0.000
27	A	29	ILE	0	-0.017	-0.001	6.316	-1.055	-1.055	0.000	0.000	0.000	0.000
28	A	30	GLY	0	-0.012	-0.004	8.128	-1.908	-1.908	0.000	0.000	0.000	0.000
29	A	31	ASP	-1	-0.927	-0.961	7.425	-28.319	-28.319	0.000	0.000	0.000	0.000
30	A	32	ARG	1	0.766	0.873	4.606	30.627	30.774	-0.001	-0.012	-0.133	0.000
31	A	33	ALA	0	-0.005	-0.017	2.377	-13.206	-10.778	1.569	-1.539	-2.457	-0.008
32	A	34	GLN	0	-0.010	0.017	3.192	5.968	6.044	0.016	0.551	-0.643	0.000
33	A	35	VAL	0	0.011	0.010	5.390	-0.556	-0.520	-0.001	-0.008	-0.027	0.000
34	A	36	SER	0	0.010	0.014	7.993	1.163	1.163	0.000	0.000	0.000	0.000
35	A	37	TYR	0	-0.097	-0.079	10.796	0.004	0.004	0.000	0.000	0.000	0.000
36	A	38	LEU	0	0.031	0.029	13.826	0.489	0.489	0.000	0.000	0.000	0.000
37	A	39	SER	0	-0.044	-0.020	15.719	0.485	0.485	0.000	0.000	0.000	0.000
38	A	40	TYR	0	-0.002	-0.033	19.333	0.139	0.139	0.000	0.000	0.000	0.000
39	A	41	ASP	-1	-0.864	-0.928	21.784	-11.425	-11.425	0.000	0.000	0.000	0.000
40	A	42	ARG	1	0.788	0.883	24.895	10.870	10.870	0.000	0.000	0.000	0.000
41	A	43	VAL	0	0.041	0.024	23.359	-0.234	-0.234	0.000	0.000	0.000	0.000
42	A	44	PRO	0	0.011	0.024	26.675	0.251	0.251	0.000	0.000	0.000	0.000
43	A	45	PHE	0	0.002	-0.003	28.815	-0.272	-0.272	0.000	0.000	0.000	0.000
44	A	46	PHE	0	0.005	-0.005	28.241	0.156	0.156	0.000	0.000	0.000	0.000
45	A	47	ASN	0	-0.037	-0.058	30.294	0.277	0.277	0.000	0.000	0.000	0.000
46	A	48	GLN	0	0.072	0.033	32.678	0.069	0.069	0.000	0.000	0.000	0.000
47	A	49	ASP	-1	-0.932	-0.934	33.730	-8.009	-8.009	0.000	0.000	0.000	0.000
48	A	50	LEU	0	-0.026	-0.015	32.565	0.110	0.110	0.000	0.000	0.000	0.000
49	A	51	GLU	-1	-0.861	-0.948	29.069	-10.225	-10.225	0.000	0.000	0.000	0.000
50	A	52	THR	0	-0.040	-0.004	30.101	-0.194	-0.194	0.000	0.000	0.000	0.000
51	A	53	SER	0	-0.062	-0.026	31.959	0.173	0.173	0.000	0.000	0.000	0.000
52	A	54	VAL	0	-0.013	-0.011	26.729	-0.296	-0.296	0.000	0.000	0.000	0.000
53	A	55	HIS	0	0.010	0.001	27.014	0.270	0.270	0.000	0.000	0.000	0.000
54	A	56	PRO	0	0.000	0.000	25.067	-0.444	-0.444	0.000	0.000	0.000	0.000
55	A	57	GLU	-1	-0.879	-0.946	23.218	-10.909	-10.909	0.000	0.000	0.000	0.000
56	A	58	VAL	0	-0.014	-0.017	22.143	-0.513	-0.513	0.000	0.000	0.000	0.000
57	A	59	ALA	0	-0.041	-0.022	21.100	-0.505	-0.505	0.000	0.000	0.000	0.000
58	A	60	HIS	0	0.012	0.010	17.211	-0.345	-0.345	0.000	0.000	0.000	0.000
59	A	61	ALA	0	0.003	-0.005	17.274	-0.773	-0.773	0.000	0.000	0.000	0.000
60	A	62	ARG	1	0.841	0.907	16.235	12.417	12.417	0.000	0.000	0.000	0.000
61	A	63	GLU	-1	-0.790	-0.880	15.102	-14.780	-14.780	0.000	0.000	0.000	0.000
62	A	64	GLU	-1	-0.908	-0.951	12.637	-19.927	-19.927	0.000	0.000	0.000	0.000
63	A	65	VAL	0	-0.039	-0.021	11.198	-1.749	-1.749	0.000	0.000	0.000	0.000
64	A	66	GLN	0	-0.040	-0.024	11.332	-0.848	-0.848	0.000	0.000	0.000	0.000
65	A	67	GLU	-1	-0.933	-0.962	9.208	-22.309	-22.309	0.000	0.000	0.000	0.000
66	A	68	ALA	0	-0.065	-0.017	6.815	-2.774	-2.774	0.000	0.000	0.000	0.000
67	A	69	ASP	-1	-0.811	-0.891	2.304	-52.526	-49.937	3.368	-3.152	-2.804	-0.032
68	A	70	ALA	0	-0.052	-0.028	5.772	0.943	0.943	0.000	0.000	0.000	0.000
69	A	71	ILE	0	0.002	-0.004	7.255	1.189	1.189	0.000	0.000	0.000	0.000
70	A	72	TRP	0	-0.009	-0.016	9.379	-0.730	-0.730	0.000	0.000	0.000	0.000
71	A	73	ILE	0	-0.007	0.004	11.705	0.843	0.843	0.000	0.000	0.000	0.000
72	A	74	PHE	0	0.046	0.024	12.615	0.678	0.678	0.000	0.000	0.000	0.000
73	A	75	SER	0	0.014	0.015	17.633	0.462	0.462	0.000	0.000	0.000	0.000
74	A	76	PRO	0	-0.048	0.013	21.074	-0.033	-0.033	0.000	0.000	0.000	0.000
75	A	77	VAL	0	0.049	0.038	24.721	-0.085	-0.085	0.000	0.000	0.000	0.000
76	A	78	TYR	0	-0.049	-0.030	26.856	0.322	0.322	0.000	0.000	0.000	0.000
77	A	79	ASN	0	-0.029	-0.020	30.261	-0.022	-0.022	0.000	0.000	0.000	0.000
78	A	80	TYR	0	0.008	-0.008	30.195	0.254	0.254	0.000	0.000	0.000	0.000
79	A	81	ALA	0	0.017	0.029	28.561	-0.193	-0.193	0.000	0.000	0.000	0.000
80	A	82	ILE	0	0.021	0.010	23.267	-0.187	-0.187	0.000	0.000	0.000	0.000
81	A	83	PRO	0	-0.042	-0.021	23.809	0.395	0.395	0.000	0.000	0.000	0.000
82	A	84	GLY	0	0.055	0.026	25.702	-0.223	-0.223	0.000	0.000	0.000	0.000
83	A	85	PRO	0	-0.004	-0.025	24.941	-0.090	-0.090	0.000	0.000	0.000	0.000
84	A	86	VAL	0	0.014	0.020	20.400	-0.250	-0.250	0.000	0.000	0.000	0.000
85	A	87	LYS	1	0.849	0.911	22.556	10.501	10.501	0.000	0.000	0.000	0.000
86	A	88	ASN	0	0.016	0.008	24.976	0.200	0.200	0.000	0.000	0.000	0.000
87	A	89	LEU	0	-0.004	0.002	18.605	0.029	0.029	0.000	0.000	0.000	0.000
88	A	90	LEU	0	0.031	0.007	18.534	-0.237	-0.237	0.000	0.000	0.000	0.000
89	A	91	ASP	-1	-0.808	-0.863	21.896	-10.997	-10.997	0.000	0.000	0.000	0.000
90	A	92	TRP	0	-0.017	-0.007	23.552	0.149	0.149	0.000	0.000	0.000	0.000
91	A	93	LEU	0	0.007	-0.005	17.274	-0.072	-0.072	0.000	0.000	0.000	0.000
92	A	94	SER	0	-0.051	-0.029	20.293	-0.248	-0.248	0.000	0.000	0.000	0.000
93	A	95	ARG	1	0.824	0.915	22.256	11.481	11.481	0.000	0.000	0.000	0.000
94	A	96	SER	0	0.005	-0.005	22.908	-0.706	-0.706	0.000	0.000	0.000	0.000
95	A	97	LEU	0	-0.007	-0.016	18.231	0.154	0.154	0.000	0.000	0.000	0.000
96	A	98	ASP	-1	-0.857	-0.907	22.891	-10.333	-10.333	0.000	0.000	0.000	0.000
97	A	99	LEU	0	-0.024	-0.013	26.143	0.169	0.169	0.000	0.000	0.000	0.000
98	A	100	SER	0	-0.125	-0.077	29.412	0.485	0.485	0.000	0.000	0.000	0.000
99	A	101	ASP	-1	-0.850	-0.929	27.979	-10.378	-10.378	0.000	0.000	0.000	0.000
100	A	102	PRO	0	-0.014	0.006	28.099	-0.386	-0.386	0.000	0.000	0.000	0.000
101	A	103	THR	0	-0.126	-0.065	28.691	-0.045	-0.045	0.000	0.000	0.000	0.000
102	A	104	GLY	0	0.027	0.034	25.660	-0.196	-0.196	0.000	0.000	0.000	0.000
103	A	105	PRO	0	-0.033	-0.022	20.111	-0.023	-0.023	0.000	0.000	0.000	0.000
104	A	106	SER	0	0.043	0.032	20.374	-0.128	-0.128	0.000	0.000	0.000	0.000
105	A	107	VAL	0	0.003	-0.017	15.528	-0.470	-0.470	0.000	0.000	0.000	0.000
106	A	108	LEU	0	-0.035	-0.034	15.108	-1.224	-1.224	0.000	0.000	0.000	0.000
107	A	109	GLN	0	-0.076	-0.046	16.383	0.290	0.290	0.000	0.000	0.000	0.000
108	A	110	ASP	-1	-0.882	-0.935	13.842	-18.778	-18.778	0.000	0.000	0.000	0.000
109	A	111	LYS	1	0.805	0.914	9.407	22.678	22.678	0.000	0.000	0.000	0.000
110	A	112	ILE	0	0.026	0.027	6.792	1.352	1.352	0.000	0.000	0.000	0.000
111	A	113	VAL	0	-0.010	-0.008	10.102	-0.406	-0.406	0.000	0.000	0.000	0.000
112	A	114	THR	0	0.003	0.004	10.841	0.558	0.558	0.000	0.000	0.000	0.000
113	A	115	VAL	0	0.011	-0.001	13.096	0.159	0.159	0.000	0.000	0.000	0.000
114	A	116	SER	0	0.022	0.031	15.723	-0.388	-0.388	0.000	0.000	0.000	0.000
115	A	117	SER	0	-0.055	-0.035	17.662	0.428	0.428	0.000	0.000	0.000	0.000
116	A	118	VAL	0	-0.055	-0.038	21.209	0.025	0.025	0.000	0.000	0.000	0.000
117	A	119	ALA	0	0.001	-0.007	23.862	0.404	0.404	0.000	0.000	0.000	0.000
118	A	120	ASN	0	-0.052	-0.038	27.342	-0.188	-0.188	0.000	0.000	0.000	0.000
119	A	121	GLY	0	0.078	0.044	29.181	0.299	0.299	0.000	0.000	0.000	0.000
120	A	122	ALA	0	0.033	0.021	29.477	-0.202	-0.202	0.000	0.000	0.000	0.000
121	A	123	SER	0	-0.036	0.011	27.604	-0.479	-0.479	0.000	0.000	0.000	0.000
122	A	124	PRO	0	-0.060	-0.045	25.935	0.367	0.367	0.000	0.000	0.000	0.000
123	A	125	GLU	-1	-0.933	-0.963	25.657	-12.428	-12.428	0.000	0.000	0.000	0.000
124	A	126	GLU	-1	-0.808	-0.917	27.243	-9.062	-9.062	0.000	0.000	0.000	0.000
125	A	127	VAL	0	-0.085	-0.031	23.694	-0.007	-0.007	0.000	0.000	0.000	0.000
126	A	128	PHE	0	-0.012	-0.028	20.067	-0.160	-0.160	0.000	0.000	0.000	0.000
127	A	129	GLU	-1	-0.882	-0.928	23.054	-10.828	-10.828	0.000	0.000	0.000	0.000
128	A	130	ASP	-1	-0.838	-0.935	25.132	-11.267	-11.267	0.000	0.000	0.000	0.000
129	A	131	TYR	0	0.015	-0.037	19.798	-0.163	-0.163	0.000	0.000	0.000	0.000
130	A	132	ARG	1	0.806	0.863	20.319	13.422	13.422	0.000	0.000	0.000	0.000
131	A	133	SER	0	-0.047	-0.010	21.779	-0.093	-0.093	0.000	0.000	0.000	0.000
132	A	134	LEU	0	0.004	-0.002	22.736	0.002	0.002	0.000	0.000	0.000	0.000
133	A	135	LEU	0	0.007	-0.010	16.564	-0.049	-0.049	0.000	0.000	0.000	0.000
134	A	136	PRO	0	0.021	0.013	18.914	-0.425	-0.425	0.000	0.000	0.000	0.000
135	A	137	PHE	0	-0.050	-0.006	20.017	0.187	0.187	0.000	0.000	0.000	0.000
136	A	138	ILE	0	-0.087	-0.045	19.777	0.363	0.363	0.000	0.000	0.000	0.000
137	A	139	ARG	1	0.928	0.959	19.706	12.834	12.834	0.000	0.000	0.000	0.000
138	A	140	MET	0	0.041	0.072	14.216	-0.352	-0.352	0.000	0.000	0.000	0.000
139	A	141	HIS	0	-0.017	-0.016	11.983	1.104	1.104	0.000	0.000	0.000	0.000
140	A	142	LEU	0	-0.006	-0.009	12.878	-1.484	-1.484	0.000	0.000	0.000	0.000
141	A	143	VAL	0	0.015	0.004	9.604	0.434	0.434	0.000	0.000	0.000	0.000
142	A	144	ASP	-1	-0.835	-0.894	13.056	-15.216	-15.216	0.000	0.000	0.000	0.000
143	A	145	GLN	0	-0.036	-0.016	13.753	1.467	1.467	0.000	0.000	0.000	0.000
144	A	146	LEU	0	-0.031	-0.008	15.548	-0.666	-0.666	0.000	0.000	0.000	0.000
145	A	147	THR	0	0.008	0.008	16.361	0.944	0.944	0.000	0.000	0.000	0.000
146	A	148	GLY	0	0.018	0.003	18.875	0.004	0.004	0.000	0.000	0.000	0.000
147	A	149	VAL	0	-0.051	-0.042	20.703	0.234	0.234	0.000	0.000	0.000	0.000
148	A	150	PRO	0	0.045	0.034	23.546	0.186	0.186	0.000	0.000	0.000	0.000
149	A	151	ILE	0	-0.001	-0.014	26.725	-0.228	-0.228	0.000	0.000	0.000	0.000
150	A	152	ASN	0	-0.026	-0.014	29.034	0.025	0.025	0.000	0.000	0.000	0.000
151	A	153	SER	0	0.048	-0.012	31.034	0.012	0.012	0.000	0.000	0.000	0.000
152	A	154	GLU	-1	-0.809	-0.892	33.194	-9.057	-9.057	0.000	0.000	0.000	0.000
153	A	155	ALA	0	-0.036	0.006	29.871	0.122	0.122	0.000	0.000	0.000	0.000
154	A	156	TRP	0	0.008	0.014	31.745	-0.037	-0.037	0.000	0.000	0.000	0.000
155	A	157	SER	0	-0.019	-0.001	34.426	0.097	0.097	0.000	0.000	0.000	0.000
156	A	158	THR	0	-0.036	-0.033	32.566	-0.073	-0.073	0.000	0.000	0.000	0.000
157	A	159	GLY	0	0.045	0.021	31.156	-0.093	-0.093	0.000	0.000	0.000	0.000
158	A	160	ILE	0	-0.038	-0.018	26.687	-0.355	-0.355	0.000	0.000	0.000	0.000
159	A	161	LEU	0	0.007	0.010	22.875	0.303	0.303	0.000	0.000	0.000	0.000
160	A	162	LYS	1	0.786	0.882	25.640	9.724	9.724	0.000	0.000	0.000	0.000
161	A	163	VAL	0	0.007	0.003	21.223	0.181	0.181	0.000	0.000	0.000	0.000
162	A	164	SER	0	-0.016	-0.031	24.445	-0.137	-0.137	0.000	0.000	0.000	0.000
163	A	165	ALA	0	0.055	0.005	23.007	-0.493	-0.493	0.000	0.000	0.000	0.000
164	A	166	GLU	-1	-0.818	-0.887	22.145	-12.127	-12.127	0.000	0.000	0.000	0.000
165	A	167	LYS	1	0.827	0.898	21.733	12.676	12.676	0.000	0.000	0.000	0.000
166	A	168	LEU	0	-0.045	-0.018	18.306	-0.655	-0.655	0.000	0.000	0.000	0.000
167	A	169	ALA	0	0.021	0.014	17.608	-1.013	-1.013	0.000	0.000	0.000	0.000
168	A	170	GLU	-1	-0.817	-0.887	16.787	-15.056	-15.056	0.000	0.000	0.000	0.000
169	A	171	LEU	0	0.008	0.007	14.708	-0.920	-0.920	0.000	0.000	0.000	0.000
170	A	172	SER	0	-0.023	-0.021	13.030	-1.323	-1.323	0.000	0.000	0.000	0.000
171	A	173	ALA	0	0.052	0.027	11.908	-1.861	-1.861	0.000	0.000	0.000	0.000
172	A	174	GLN	0	0.002	0.004	11.675	-0.723	-0.723	0.000	0.000	0.000	0.000
173	A	175	ALA	0	0.000	-0.013	9.291	-1.573	-1.573	0.000	0.000	0.000	0.000
174	A	176	ASP	-1	-0.818	-0.893	7.635	-33.424	-33.424	0.000	0.000	0.000	0.000
175	A	177	ALA	0	-0.051	-0.022	7.337	-3.581	-3.581	0.000	0.000	0.000	0.000
176	A	178	LEU	0	-0.023	-0.012	5.559	-1.251	-1.251	0.000	0.000	0.000	0.000
177	A	179	LEU	0	0.024	0.002	2.764	-4.668	-3.792	0.464	-0.197	-1.143	-0.001
178	A	180	SER	0	0.003	-0.005	2.849	-14.481	-12.748	0.228	-0.867	-1.093	-0.011
179	A	181	ALA	0	-0.072	-0.014	5.573	-0.332	-0.332	0.000	0.000	0.000	0.000
180	A	182	ILE	0	-0.001	-0.011	2.029	-0.134	0.414	2.768	-0.729	-2.587	-0.009
181	A	183	GLU	-1	-0.851	-0.882	1.712	-156.926	-165.462	31.602	-14.189	-8.877	-0.166
182	A	184	ASN	0	-0.099	-0.050	4.410	9.197	9.259	0.001	-0.015	-0.047	0.000

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