FMO DATABASE

FMODB ID: MV72Z

Calculation Name: 3F6A-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3F6A

Chain ID: A

ChEMBL ID:

UniProt ID: A0A0H2

Base Structure: X-ray

Registration Date: 2023-09-20

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

DOI:

Apendix: None

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	150
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1418181.079587
FMO2-HF: Nuclear repulsion	1358856.421551
FMO2-HF: Total energy	-59324.658036
FMO2-MP2: Total energy	-59498.100829

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:1:LEU)

Summations of interaction energy for fragment #1(A:1: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.
-1.22	1.957	0.089	-1.649	-1.617	0.007

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.038 / q_NPA : 0.020

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	3	ARG	1	1.005	1.023	3.826	-0.492	1.827	-0.032	-1.279	-1.008	0.003
4	A	4	HIS	0	-0.050	-0.030	5.526	-0.658	-0.658	0.000	0.000	0.000	0.000
5	A	5	PHE	0	-0.010	-0.006	3.327	-0.937	-0.079	0.121	-0.370	-0.609	0.004
6	A	6	THR	0	-0.003	-0.003	8.613	-0.156	-0.156	0.000	0.000	0.000	0.000
7	A	7	VAL	0	-0.040	-0.006	12.348	0.052	0.052	0.000	0.000	0.000	0.000
8	A	8	SER	0	0.034	-0.012	15.180	-0.053	-0.053	0.000	0.000	0.000	0.000
9	A	9	VAL	0	-0.014	-0.023	18.722	-0.006	-0.006	0.000	0.000	0.000	0.000
10	A	10	PHE	0	-0.023	-0.004	21.762	-0.017	-0.017	0.000	0.000	0.000	0.000
11	A	11	ILE	0	0.013	0.002	25.060	-0.009	-0.009	0.000	0.000	0.000	0.000
12	A	12	VAL	0	0.033	0.008	27.669	-0.004	-0.004	0.000	0.000	0.000	0.000
13	A	13	CYS	0	-0.062	-0.013	30.978	-0.005	-0.005	0.000	0.000	0.000	0.000
14	A	14	LYS	1	0.901	0.953	34.237	-0.080	-0.080	0.000	0.000	0.000	0.000
15	A	15	ASP	-1	-0.827	-0.907	36.177	0.078	0.078	0.000	0.000	0.000	0.000
16	A	16	LYS	1	0.857	0.909	35.201	-0.083	-0.083	0.000	0.000	0.000	0.000
17	A	17	VAL	0	0.053	0.031	28.749	0.002	0.002	0.000	0.000	0.000	0.000
18	A	18	LEU	0	-0.021	-0.005	28.599	-0.006	-0.006	0.000	0.000	0.000	0.000
19	A	19	LEU	0	-0.031	-0.007	26.964	0.014	0.014	0.000	0.000	0.000	0.000
20	A	20	HIS	0	0.065	0.012	23.814	-0.035	-0.035	0.000	0.000	0.000	0.000
21	A	21	LEU	0	-0.088	-0.023	27.526	0.010	0.010	0.000	0.000	0.000	0.000
22	A	22	HIS	0	0.096	0.076	21.046	-0.015	-0.015	0.000	0.000	0.000	0.000
23	A	23	LYS	1	0.903	0.950	26.174	-0.140	-0.140	0.000	0.000	0.000	0.000
24	A	24	LYS	1	0.903	0.949	25.989	-0.125	-0.125	0.000	0.000	0.000	0.000
25	A	25	ALA	0	0.079	0.021	25.318	0.005	0.005	0.000	0.000	0.000	0.000
26	A	26	LYS	1	0.918	0.951	27.364	-0.100	-0.100	0.000	0.000	0.000	0.000
27	A	27	LYS	1	0.914	0.977	23.358	-0.231	-0.231	0.000	0.000	0.000	0.000
28	A	28	MET	0	-0.052	-0.010	27.807	0.003	0.003	0.000	0.000	0.000	0.000
29	A	29	LEU	0	-0.020	-0.019	22.138	0.003	0.003	0.000	0.000	0.000	0.000
30	A	30	PRO	0	0.023	0.029	21.776	-0.022	-0.022	0.000	0.000	0.000	0.000
31	A	31	LEU	0	-0.001	0.006	22.962	0.006	0.006	0.000	0.000	0.000	0.000
32	A	32	GLY	0	-0.011	-0.024	19.097	0.019	0.019	0.000	0.000	0.000	0.000
33	A	33	GLY	0	0.052	0.051	16.975	-0.031	-0.031	0.000	0.000	0.000	0.000
34	A	34	HIS	0	-0.052	-0.039	12.514	0.108	0.108	0.000	0.000	0.000	0.000
35	A	35	ILE	0	0.004	0.011	9.743	-0.056	-0.056	0.000	0.000	0.000	0.000
36	A	36	GLU	-1	-0.958	-0.991	10.892	0.172	0.172	0.000	0.000	0.000	0.000
37	A	37	VAL	0	-0.047	-0.035	7.253	0.043	0.043	0.000	0.000	0.000	0.000
38	A	38	ASN	0	-0.060	-0.038	8.984	-0.100	-0.100	0.000	0.000	0.000	0.000
39	A	39	GLU	-1	-0.746	-0.852	10.878	0.287	0.287	0.000	0.000	0.000	0.000
40	A	40	LEU	0	-0.046	-0.018	11.285	0.115	0.115	0.000	0.000	0.000	0.000
41	A	41	PRO	0	0.036	0.004	10.735	0.000	0.000	0.000	0.000	0.000	0.000
42	A	42	GLU	-1	-0.816	-0.928	13.415	0.170	0.170	0.000	0.000	0.000	0.000
43	A	43	GLU	-1	-0.870	-0.953	16.151	0.127	0.127	0.000	0.000	0.000	0.000
44	A	44	ALA	0	0.033	0.018	14.546	-0.023	-0.023	0.000	0.000	0.000	0.000
45	A	45	CYS	0	-0.052	-0.015	16.677	-0.018	-0.018	0.000	0.000	0.000	0.000
46	A	46	ILE	0	-0.040	-0.019	19.241	-0.028	-0.028	0.000	0.000	0.000	0.000
47	A	47	ARG	1	0.785	0.912	16.112	-0.311	-0.311	0.000	0.000	0.000	0.000
48	A	48	GLU	-1	-0.778	-0.884	18.391	0.282	0.282	0.000	0.000	0.000	0.000
49	A	49	ALA	0	-0.052	-0.020	21.472	-0.019	-0.019	0.000	0.000	0.000	0.000
50	A	50	LYS	1	0.825	0.913	24.334	-0.117	-0.117	0.000	0.000	0.000	0.000
51	A	51	GLU	-1	-0.819	-0.909	21.252	0.171	0.171	0.000	0.000	0.000	0.000
52	A	52	GLU	-1	-0.795	-0.901	22.172	0.229	0.229	0.000	0.000	0.000	0.000
53	A	53	ALA	0	-0.043	-0.047	26.139	-0.010	-0.010	0.000	0.000	0.000	0.000
54	A	54	GLY	0	0.025	0.035	28.493	-0.011	-0.011	0.000	0.000	0.000	0.000
55	A	55	LEU	0	-0.106	-0.052	28.522	-0.010	-0.010	0.000	0.000	0.000	0.000
56	A	56	ASN	0	0.042	0.032	27.771	0.011	0.011	0.000	0.000	0.000	0.000
57	A	57	VAL	0	0.007	-0.007	24.506	-0.004	-0.004	0.000	0.000	0.000	0.000
58	A	58	THR	0	-0.035	-0.015	26.926	-0.007	-0.007	0.000	0.000	0.000	0.000
59	A	59	LEU	0	0.011	-0.003	20.210	-0.001	-0.001	0.000	0.000	0.000	0.000
60	A	60	TYR	0	-0.011	0.000	24.181	-0.019	-0.019	0.000	0.000	0.000	0.000
61	A	61	ASN	0	0.036	-0.015	22.451	0.019	0.019	0.000	0.000	0.000	0.000
62	A	62	PRO	0	-0.030	0.009	23.271	-0.015	-0.015	0.000	0.000	0.000	0.000
63	A	63	ILE	0	0.001	-0.009	23.899	0.001	0.001	0.000	0.000	0.000	0.000
64	A	64	ASP	-1	-0.842	-0.901	23.308	0.053	0.053	0.000	0.000	0.000	0.000
65	A	65	ILE	0	-0.025	-0.039	25.026	-0.007	-0.007	0.000	0.000	0.000	0.000
66	A	66	ASN	0	0.007	-0.008	27.223	-0.010	-0.010	0.000	0.000	0.000	0.000
67	A	67	LEU	0	0.057	0.044	19.536	-0.009	-0.009	0.000	0.000	0.000	0.000
68	A	68	LYS	1	0.969	0.987	22.903	-0.060	-0.060	0.000	0.000	0.000	0.000
69	A	69	LYS	1	0.948	0.967	23.947	-0.023	-0.023	0.000	0.000	0.000	0.000
70	A	70	SER	0	-0.015	-0.013	24.554	-0.007	-0.007	0.000	0.000	0.000	0.000
71	A	71	CYS	0	0.014	0.016	20.100	-0.009	-0.009	0.000	0.000	0.000	0.000
72	A	72	ASP	-1	-0.883	-0.939	22.210	0.008	0.008	0.000	0.000	0.000	0.000
73	A	73	LEU	0	-0.115	-0.050	24.130	-0.008	-0.008	0.000	0.000	0.000	0.000
74	A	74	SER	0	-0.074	-0.039	21.520	-0.008	-0.008	0.000	0.000	0.000	0.000
75	A	75	GLY	0	-0.024	-0.002	20.930	-0.014	-0.014	0.000	0.000	0.000	0.000
76	A	76	GLU	-1	-0.987	-0.987	16.414	-0.086	-0.086	0.000	0.000	0.000	0.000
77	A	77	LYS	1	0.946	0.948	17.799	-0.003	-0.003	0.000	0.000	0.000	0.000
78	A	78	LEU	0	-0.014	0.004	17.288	0.008	0.008	0.000	0.000	0.000	0.000
79	A	79	LEU	0	-0.019	-0.005	13.530	-0.005	-0.005	0.000	0.000	0.000	0.000
80	A	80	ILE	0	-0.066	0.003	17.538	-0.008	-0.008	0.000	0.000	0.000	0.000
81	A	81	ASN	0	0.029	-0.007	15.466	0.059	0.059	0.000	0.000	0.000	0.000
82	A	82	PRO	0	-0.040	-0.005	13.821	-0.019	-0.019	0.000	0.000	0.000	0.000
83	A	83	ILE	0	-0.027	-0.014	16.986	-0.028	-0.028	0.000	0.000	0.000	0.000
84	A	84	HIS	1	0.798	0.877	18.296	-0.256	-0.256	0.000	0.000	0.000	0.000
85	A	85	THR	0	0.046	0.025	12.025	0.053	0.053	0.000	0.000	0.000	0.000
86	A	86	ILE	0	-0.038	-0.019	14.919	-0.057	-0.057	0.000	0.000	0.000	0.000
87	A	87	LEU	0	-0.005	0.012	11.293	0.095	0.095	0.000	0.000	0.000	0.000
88	A	88	GLY	0	-0.001	0.002	13.756	-0.097	-0.097	0.000	0.000	0.000	0.000
89	A	89	ASP	-1	-0.927	-0.976	14.246	0.418	0.418	0.000	0.000	0.000	0.000
90	A	90	VAL	0	-0.062	-0.049	16.605	-0.033	-0.033	0.000	0.000	0.000	0.000
91	A	91	SER	0	-0.085	-0.020	18.556	0.002	0.002	0.000	0.000	0.000	0.000
92	A	92	PRO	0	0.123	0.061	14.060	-0.020	-0.020	0.000	0.000	0.000	0.000
93	A	93	ASN	0	-0.049	-0.040	16.543	0.016	0.016	0.000	0.000	0.000	0.000
94	A	94	HIS	0	-0.023	-0.017	11.215	-0.140	-0.140	0.000	0.000	0.000	0.000
95	A	95	SER	0	0.017	0.021	11.006	0.068	0.068	0.000	0.000	0.000	0.000
96	A	96	HIS	0	-0.048	-0.029	9.758	0.138	0.138	0.000	0.000	0.000	0.000
97	A	97	ILE	0	0.012	0.017	7.125	-0.237	-0.237	0.000	0.000	0.000	0.000
98	A	98	ASP	-1	-0.805	-0.872	10.682	0.605	0.605	0.000	0.000	0.000	0.000
99	A	99	PHE	0	-0.039	-0.022	8.815	-0.059	-0.059	0.000	0.000	0.000	0.000
100	A	100	VAL	0	0.032	0.010	14.158	-0.045	-0.045	0.000	0.000	0.000	0.000
101	A	101	TYR	0	0.038	0.012	14.959	-0.005	-0.005	0.000	0.000	0.000	0.000
102	A	102	TYR	0	-0.011	-0.025	20.183	-0.002	-0.002	0.000	0.000	0.000	0.000
103	A	103	ALA	0	0.023	0.006	23.979	-0.002	-0.002	0.000	0.000	0.000	0.000
104	A	104	THR	0	0.022	0.035	26.110	-0.006	-0.006	0.000	0.000	0.000	0.000
105	A	105	THR	0	0.026	-0.010	29.189	0.002	0.002	0.000	0.000	0.000	0.000
106	A	106	THR	0	0.000	-0.006	31.558	-0.002	-0.002	0.000	0.000	0.000	0.000
107	A	107	SER	0	0.004	0.003	34.928	-0.006	-0.006	0.000	0.000	0.000	0.000
108	A	108	PHE	0	0.010	-0.024	34.858	0.003	0.003	0.000	0.000	0.000	0.000
109	A	109	GLU	-1	-0.981	-0.977	35.806	0.071	0.071	0.000	0.000	0.000	0.000
110	A	110	THR	0	-0.011	-0.007	32.184	0.005	0.005	0.000	0.000	0.000	0.000
111	A	111	SER	0	-0.042	-0.032	32.489	-0.008	-0.008	0.000	0.000	0.000	0.000
112	A	112	PRO	0	-0.056	-0.015	29.347	-0.001	-0.001	0.000	0.000	0.000	0.000
113	A	113	GLU	-1	-0.877	-0.926	26.607	0.101	0.101	0.000	0.000	0.000	0.000
114	A	114	ILE	0	-0.041	-0.049	28.374	0.003	0.003	0.000	0.000	0.000	0.000
115	A	115	GLY	0	-0.063	-0.035	27.826	0.005	0.005	0.000	0.000	0.000	0.000
116	A	116	GLU	-1	-0.800	-0.873	24.160	0.188	0.188	0.000	0.000	0.000	0.000
117	A	117	SER	0	-0.140	-0.112	26.993	-0.020	-0.020	0.000	0.000	0.000	0.000
118	A	118	LYS	1	0.930	0.963	28.877	-0.100	-0.100	0.000	0.000	0.000	0.000
119	A	119	ILE	0	-0.071	-0.024	31.590	-0.008	-0.008	0.000	0.000	0.000	0.000
120	A	120	LEU	0	0.078	0.041	29.750	0.009	0.009	0.000	0.000	0.000	0.000
121	A	121	LYS	1	0.874	0.938	32.150	-0.107	-0.107	0.000	0.000	0.000	0.000
122	A	122	TRP	0	0.025	0.013	31.851	0.008	0.008	0.000	0.000	0.000	0.000
123	A	123	TYR	0	-0.048	-0.032	32.274	-0.006	-0.006	0.000	0.000	0.000	0.000
124	A	124	SER	0	0.010	0.005	34.870	0.002	0.002	0.000	0.000	0.000	0.000
125	A	125	LYS	1	0.990	0.988	34.992	-0.091	-0.091	0.000	0.000	0.000	0.000
126	A	126	GLU	-1	-0.932	-0.965	36.640	0.070	0.070	0.000	0.000	0.000	0.000
127	A	127	ASP	-1	-0.949	-0.937	37.046	0.085	0.085	0.000	0.000	0.000	0.000
128	A	128	LEU	0	0.032	0.002	33.423	0.005	0.005	0.000	0.000	0.000	0.000
129	A	129	LYS	1	0.910	0.944	35.464	-0.075	-0.075	0.000	0.000	0.000	0.000
130	A	130	ASN	0	0.008	-0.007	37.231	-0.004	-0.004	0.000	0.000	0.000	0.000
131	A	131	ALA	0	-0.042	-0.002	34.497	-0.003	-0.003	0.000	0.000	0.000	0.000
132	A	132	HIS	0	0.043	0.018	35.582	0.003	0.003	0.000	0.000	0.000	0.000
133	A	133	ASN	0	-0.072	-0.051	32.371	-0.002	-0.002	0.000	0.000	0.000	0.000
134	A	134	ILE	0	0.029	0.017	28.883	0.008	0.008	0.000	0.000	0.000	0.000
135	A	135	GLN	0	0.040	0.024	22.893	-0.005	-0.005	0.000	0.000	0.000	0.000
136	A	136	GLU	-1	-0.807	-0.921	27.951	0.133	0.133	0.000	0.000	0.000	0.000
137	A	137	ASN	0	0.039	0.011	21.753	-0.018	-0.018	0.000	0.000	0.000	0.000
138	A	138	ILE	0	-0.010	0.003	22.710	0.007	0.007	0.000	0.000	0.000	0.000
139	A	139	LEU	0	0.003	0.001	25.935	-0.005	-0.005	0.000	0.000	0.000	0.000
140	A	140	VAL	0	-0.002	0.011	26.843	-0.007	-0.007	0.000	0.000	0.000	0.000
141	A	141	MET	0	0.011	0.016	21.087	0.002	0.002	0.000	0.000	0.000	0.000
142	A	142	ALA	0	0.010	0.015	25.906	-0.003	-0.003	0.000	0.000	0.000	0.000
143	A	143	THR	0	-0.045	-0.039	28.402	-0.013	-0.013	0.000	0.000	0.000	0.000
144	A	144	GLU	-1	-0.828	-0.886	25.380	0.174	0.174	0.000	0.000	0.000	0.000
145	A	145	ALA	0	-0.016	-0.002	26.700	-0.006	-0.006	0.000	0.000	0.000	0.000
146	A	146	LEU	0	-0.044	-0.025	28.296	-0.009	-0.009	0.000	0.000	0.000	0.000
147	A	147	ASP	-1	-0.922	-0.965	31.699	0.099	0.099	0.000	0.000	0.000	0.000
148	A	148	LEU	0	-0.086	-0.037	26.798	-0.005	-0.005	0.000	0.000	0.000	0.000
149	A	149	LEU	0	-0.120	-0.069	27.519	-0.005	-0.005	0.000	0.000	0.000	0.000
150	A	150	GLU	-1	-0.978	-0.972	31.866	0.073	0.073	0.000	0.000	0.000	0.000

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