FMO DATABASE

FMODB ID: 9G182

Calculation Name: 3PU6-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3PU6

Chain ID: A

ChEMBL ID:

UniProt ID: Q7MR08

Base Structure: X-ray

Registration Date: 2023-06-20

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

DOI:

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	147
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1365521.640145
FMO2-HF: Nuclear repulsion	1308765.342496
FMO2-HF: Total energy	-56756.29765
FMO2-MP2: Total energy	-56921.83318

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.
-11.101	-2.167	4.007	-4.317	-8.625	-0.02

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 : -0.004 / q_NPA : 0.005

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	LYS	1	0.834	0.918	2.730	0.703	4.139	0.299	-1.262	-2.474	0.004
4	A	4	VAL	0	0.011	-0.001	5.267	0.178	0.245	-0.001	-0.005	-0.061	0.000
5	A	5	LEU	0	0.008	0.007	8.889	0.085	0.085	0.000	0.000	0.000	0.000
6	A	6	LEU	0	-0.043	-0.025	11.900	0.035	0.035	0.000	0.000	0.000	0.000
7	A	7	CYS	0	-0.042	-0.002	14.910	0.031	0.031	0.000	0.000	0.000	0.000
8	A	8	VAL	0	-0.002	-0.003	18.088	0.010	0.010	0.000	0.000	0.000	0.000
9	A	9	GLY	0	0.050	0.022	21.153	0.002	0.002	0.000	0.000	0.000	0.000
10	A	10	ASN	0	-0.063	-0.051	24.740	-0.001	-0.001	0.000	0.000	0.000	0.000
11	A	11	GLU	-1	-0.764	-0.876	26.276	-0.210	-0.210	0.000	0.000	0.000	0.000
12	A	12	LEU	0	-0.021	-0.002	28.891	0.010	0.010	0.000	0.000	0.000	0.000
13	A	13	ARG	1	0.862	0.938	31.101	0.132	0.132	0.000	0.000	0.000	0.000
14	A	14	GLY	0	0.076	0.044	31.897	0.000	0.000	0.000	0.000	0.000	0.000
15	A	15	ASP	-1	-0.756	-0.862	28.957	-0.143	-0.143	0.000	0.000	0.000	0.000
16	A	16	ASP	-1	-0.867	-0.950	27.443	-0.179	-0.179	0.000	0.000	0.000	0.000
17	A	17	GLY	0	0.019	0.016	25.705	-0.013	-0.013	0.000	0.000	0.000	0.000
18	A	18	VAL	0	-0.006	-0.004	23.030	-0.017	-0.017	0.000	0.000	0.000	0.000
19	A	19	ALA	0	0.016	0.009	19.831	-0.014	-0.014	0.000	0.000	0.000	0.000
20	A	20	ILE	0	-0.027	-0.004	19.722	-0.035	-0.035	0.000	0.000	0.000	0.000
21	A	21	ALA	0	0.002	-0.005	21.239	-0.018	-0.018	0.000	0.000	0.000	0.000
22	A	22	LEU	0	-0.014	-0.007	15.880	-0.014	-0.014	0.000	0.000	0.000	0.000
23	A	23	GLY	0	0.037	-0.001	16.663	-0.035	-0.035	0.000	0.000	0.000	0.000
24	A	24	ARG	1	0.851	0.885	17.187	0.208	0.208	0.000	0.000	0.000	0.000
25	A	25	LEU	0	-0.021	0.012	18.121	-0.003	-0.003	0.000	0.000	0.000	0.000
26	A	26	VAL	0	-0.022	-0.020	11.941	-0.009	-0.009	0.000	0.000	0.000	0.000
27	A	27	GLU	-1	-0.927	-0.960	14.083	-0.467	-0.467	0.000	0.000	0.000	0.000
28	A	28	GLU	-1	-0.985	-0.979	15.479	-0.272	-0.272	0.000	0.000	0.000	0.000
29	A	29	GLN	0	-0.011	-0.018	15.939	0.010	0.010	0.000	0.000	0.000	0.000
30	A	30	MET	0	-0.090	-0.032	9.574	0.052	0.052	0.000	0.000	0.000	0.000
31	A	31	PRO	0	0.072	0.028	10.864	-0.161	-0.161	0.000	0.000	0.000	0.000
32	A	32	GLU	-1	-0.884	-0.909	5.444	-1.494	-1.494	0.000	0.000	0.000	0.000
33	A	33	TRP	0	-0.081	-0.051	6.467	-0.782	-0.782	0.000	0.000	0.000	0.000
34	A	34	SER	0	-0.016	0.006	8.971	0.165	0.165	0.000	0.000	0.000	0.000
35	A	35	VAL	0	0.018	-0.003	10.992	-0.047	-0.047	0.000	0.000	0.000	0.000
36	A	36	PHE	0	-0.054	-0.032	13.283	0.030	0.030	0.000	0.000	0.000	0.000
37	A	37	PHE	0	0.018	0.008	15.893	0.009	0.009	0.000	0.000	0.000	0.000
38	A	38	GLY	0	0.015	0.004	19.343	0.014	0.014	0.000	0.000	0.000	0.000
39	A	39	TYR	0	-0.034	-0.013	20.734	0.021	0.021	0.000	0.000	0.000	0.000
40	A	40	ASP	-1	-0.816	-0.900	23.488	-0.179	-0.179	0.000	0.000	0.000	0.000
41	A	41	THR	0	-0.040	-0.010	24.591	0.018	0.018	0.000	0.000	0.000	0.000
42	A	42	PRO	0	0.054	0.029	19.616	-0.014	-0.014	0.000	0.000	0.000	0.000
43	A	43	GLU	-1	-0.872	-0.943	19.890	-0.228	-0.228	0.000	0.000	0.000	0.000
44	A	44	SER	0	-0.085	-0.048	21.768	0.002	0.002	0.000	0.000	0.000	0.000
45	A	45	GLU	-1	-0.795	-0.882	17.182	-0.379	-0.379	0.000	0.000	0.000	0.000
46	A	46	PHE	0	-0.013	-0.015	17.062	-0.036	-0.036	0.000	0.000	0.000	0.000
47	A	47	GLY	0	-0.046	-0.010	17.250	-0.010	-0.010	0.000	0.000	0.000	0.000
48	A	48	LYS	1	0.875	0.902	15.697	0.372	0.372	0.000	0.000	0.000	0.000
49	A	49	LEU	0	0.020	0.020	12.087	-0.062	-0.062	0.000	0.000	0.000	0.000
50	A	50	ARG	1	0.873	0.927	12.847	0.189	0.189	0.000	0.000	0.000	0.000
51	A	51	GLU	-1	-0.969	-0.979	13.711	-0.243	-0.243	0.000	0.000	0.000	0.000
52	A	52	LEU	0	-0.029	0.007	8.488	0.023	0.023	0.000	0.000	0.000	0.000
53	A	53	ALA	0	0.008	0.001	8.930	-0.137	-0.137	0.000	0.000	0.000	0.000
54	A	54	PRO	0	-0.018	-0.013	6.686	-0.035	-0.035	0.000	0.000	0.000	0.000
55	A	55	ASP	-1	-0.851	-0.918	2.436	-5.016	-1.873	2.577	-2.255	-3.465	-0.021
56	A	56	VAL	0	-0.031	-0.036	3.299	-0.291	0.361	0.044	-0.116	-0.580	0.000
57	A	57	ILE	0	-0.001	0.014	5.639	-0.164	-0.164	0.000	0.000	0.000	0.000
58	A	58	VAL	0	0.008	0.012	9.129	0.116	0.116	0.000	0.000	0.000	0.000
59	A	59	VAL	0	-0.021	-0.004	11.395	-0.020	-0.020	0.000	0.000	0.000	0.000
60	A	60	ALA	0	-0.002	-0.004	14.935	0.030	0.030	0.000	0.000	0.000	0.000
61	A	61	ASP	-1	-0.847	-0.950	17.459	-0.224	-0.224	0.000	0.000	0.000	0.000
62	A	62	ALA	0	0.021	0.036	21.249	0.005	0.005	0.000	0.000	0.000	0.000
63	A	63	MET	0	-0.071	-0.022	23.364	0.002	0.002	0.000	0.000	0.000	0.000
64	A	64	SER	0	0.008	0.007	26.148	0.008	0.008	0.000	0.000	0.000	0.000
65	A	65	GLY	0	0.001	-0.011	29.900	0.002	0.002	0.000	0.000	0.000	0.000
66	A	66	PHE	0	-0.043	-0.019	32.608	0.001	0.001	0.000	0.000	0.000	0.000
67	A	67	LYS	1	0.826	0.898	27.045	0.129	0.129	0.000	0.000	0.000	0.000
68	A	68	GLU	-1	-0.797	-0.898	28.525	-0.132	-0.132	0.000	0.000	0.000	0.000
69	A	69	GLY	0	-0.059	-0.027	27.241	0.006	0.006	0.000	0.000	0.000	0.000
70	A	70	GLU	-1	-0.867	-0.917	24.562	-0.122	-0.122	0.000	0.000	0.000	0.000
71	A	71	ILE	0	-0.059	-0.047	18.610	-0.014	-0.014	0.000	0.000	0.000	0.000
72	A	72	GLU	-1	-0.856	-0.895	19.438	-0.144	-0.144	0.000	0.000	0.000	0.000
73	A	73	PHE	0	-0.046	-0.032	11.512	-0.028	-0.028	0.000	0.000	0.000	0.000
74	A	74	LEU	0	0.004	0.015	15.468	0.020	0.020	0.000	0.000	0.000	0.000
75	A	75	ASP	-1	-0.754	-0.852	10.513	-0.293	-0.293	0.000	0.000	0.000	0.000
76	A	76	LEU	0	-0.001	-0.007	12.917	0.042	0.042	0.000	0.000	0.000	0.000
77	A	77	SER	0	-0.010	-0.007	11.104	0.039	0.039	0.000	0.000	0.000	0.000
78	A	78	ASP	-1	-0.844	-0.898	13.234	-0.045	-0.045	0.000	0.000	0.000	0.000
79	A	79	GLU	-1	-0.796	-0.873	15.680	-0.111	-0.111	0.000	0.000	0.000	0.000
80	A	80	ARG	1	0.930	0.962	18.881	0.048	0.048	0.000	0.000	0.000	0.000
81	A	81	THR	0	-0.019	-0.043	17.253	0.001	0.001	0.000	0.000	0.000	0.000
82	A	82	TYR	0	-0.023	-0.008	17.999	-0.004	-0.004	0.000	0.000	0.000	0.000
83	A	83	LEU	0	-0.048	-0.022	19.658	0.001	0.001	0.000	0.000	0.000	0.000
84	A	84	TYR	0	-0.078	-0.035	22.902	0.007	0.007	0.000	0.000	0.000	0.000
85	A	85	SER	0	-0.064	-0.040	21.147	-0.005	-0.005	0.000	0.000	0.000	0.000
86	A	86	THR	0	0.019	-0.007	22.253	0.000	0.000	0.000	0.000	0.000	0.000
87	A	87	HIS	0	-0.022	-0.006	23.211	0.007	0.007	0.000	0.000	0.000	0.000
88	A	88	ASN	0	-0.047	-0.032	24.958	-0.002	-0.002	0.000	0.000	0.000	0.000
89	A	89	LEU	0	0.046	0.019	21.082	-0.009	-0.009	0.000	0.000	0.000	0.000
90	A	90	PRO	0	0.011	0.003	22.166	0.007	0.007	0.000	0.000	0.000	0.000
91	A	91	THR	0	0.068	0.036	20.966	0.003	0.003	0.000	0.000	0.000	0.000
92	A	92	PRO	0	0.004	0.026	21.914	-0.012	-0.012	0.000	0.000	0.000	0.000
93	A	93	ILE	0	0.005	-0.011	22.231	-0.005	-0.005	0.000	0.000	0.000	0.000
94	A	94	LEU	0	0.023	0.023	18.072	-0.004	-0.004	0.000	0.000	0.000	0.000
95	A	95	ILE	0	0.024	-0.002	17.578	-0.019	-0.019	0.000	0.000	0.000	0.000
96	A	96	SER	0	-0.046	-0.035	17.440	-0.010	-0.010	0.000	0.000	0.000	0.000
97	A	97	TYR	0	-0.006	0.005	17.529	0.022	0.022	0.000	0.000	0.000	0.000
98	A	98	LEU	0	0.005	-0.001	13.846	-0.005	-0.005	0.000	0.000	0.000	0.000
99	A	99	ARG	1	0.765	0.856	13.600	0.135	0.135	0.000	0.000	0.000	0.000
100	A	100	GLY	0	-0.043	-0.009	14.016	0.021	0.021	0.000	0.000	0.000	0.000
101	A	101	ILE	0	-0.077	-0.031	11.586	0.023	0.023	0.000	0.000	0.000	0.000
102	A	102	CYS	0	-0.067	-0.022	7.696	-0.022	-0.022	0.000	0.000	0.000	0.000
103	A	103	SER	0	0.041	0.023	8.375	-0.003	-0.003	0.000	0.000	0.000	0.000
104	A	104	LYS	1	0.845	0.905	5.837	0.270	0.270	0.000	0.000	0.000	0.000
105	A	105	THR	0	0.016	0.007	8.486	-0.134	-0.134	0.000	0.000	0.000	0.000
106	A	106	ILE	0	-0.011	-0.017	8.142	0.070	0.070	0.000	0.000	0.000	0.000
107	A	107	PHE	0	-0.002	0.005	11.947	-0.032	-0.032	0.000	0.000	0.000	0.000
108	A	108	LEU	0	0.011	-0.002	14.134	0.007	0.007	0.000	0.000	0.000	0.000
109	A	109	GLY	0	0.018	0.004	16.717	-0.005	-0.005	0.000	0.000	0.000	0.000
110	A	110	ILE	0	0.041	0.013	19.309	0.009	0.009	0.000	0.000	0.000	0.000
111	A	111	SER	0	-0.059	-0.024	22.553	0.008	0.008	0.000	0.000	0.000	0.000
112	A	112	VAL	0	0.021	0.009	26.128	0.000	0.000	0.000	0.000	0.000	0.000
113	A	113	LEU	0	0.058	0.029	28.852	0.005	0.005	0.000	0.000	0.000	0.000
114	A	114	LEU	0	0.006	-0.010	32.639	-0.002	-0.002	0.000	0.000	0.000	0.000
115	A	115	GLU	-1	-0.953	-0.976	34.246	-0.086	-0.086	0.000	0.000	0.000	0.000
116	A	116	ASN	0	-0.021	-0.035	32.646	0.008	0.008	0.000	0.000	0.000	0.000
117	A	117	VAL	0	-0.018	0.001	30.188	-0.005	-0.005	0.000	0.000	0.000	0.000
118	A	118	LEU	0	-0.068	-0.028	33.423	0.000	0.000	0.000	0.000	0.000	0.000
119	A	119	HIS	0	-0.027	-0.002	36.554	0.006	0.006	0.000	0.000	0.000	0.000
120	A	120	PHE	0	-0.069	-0.030	36.166	-0.006	-0.006	0.000	0.000	0.000	0.000
121	A	121	SER	0	0.001	-0.018	35.158	0.008	0.008	0.000	0.000	0.000	0.000
122	A	122	GLU	-1	-0.922	-0.945	32.961	-0.132	-0.132	0.000	0.000	0.000	0.000
123	A	123	GLY	0	-0.015	-0.007	30.758	0.005	0.005	0.000	0.000	0.000	0.000
124	A	124	LEU	0	-0.051	-0.012	25.558	0.001	0.001	0.000	0.000	0.000	0.000
125	A	125	SER	0	-0.035	-0.040	30.258	0.008	0.008	0.000	0.000	0.000	0.000
126	A	126	GLN	0	-0.069	-0.055	30.245	-0.004	-0.004	0.000	0.000	0.000	0.000
127	A	127	GLY	0	0.035	0.024	29.536	-0.006	-0.006	0.000	0.000	0.000	0.000
128	A	128	ALA	0	0.073	0.038	27.126	-0.008	-0.008	0.000	0.000	0.000	0.000
129	A	129	SER	0	-0.007	-0.019	25.590	-0.018	-0.018	0.000	0.000	0.000	0.000
130	A	130	ASP	-1	-0.891	-0.941	24.935	-0.138	-0.138	0.000	0.000	0.000	0.000
131	A	131	SER	0	-0.011	-0.014	23.924	-0.009	-0.009	0.000	0.000	0.000	0.000
132	A	132	ALA	0	0.020	0.022	21.147	-0.016	-0.016	0.000	0.000	0.000	0.000
133	A	133	PHE	0	-0.006	-0.005	19.792	-0.028	-0.028	0.000	0.000	0.000	0.000
134	A	134	VAL	0	-0.027	-0.013	19.638	-0.011	-0.011	0.000	0.000	0.000	0.000
135	A	135	ALA	0	0.018	0.001	17.847	-0.007	-0.007	0.000	0.000	0.000	0.000
136	A	136	LEU	0	-0.017	-0.011	14.837	-0.038	-0.038	0.000	0.000	0.000	0.000
137	A	137	GLY	0	-0.034	-0.013	14.678	-0.030	-0.030	0.000	0.000	0.000	0.000
138	A	138	ARG	1	0.886	0.910	14.541	0.190	0.190	0.000	0.000	0.000	0.000
139	A	139	ILE	0	0.020	0.020	10.139	-0.020	-0.020	0.000	0.000	0.000	0.000
140	A	140	LYS	1	0.917	0.944	9.821	0.221	0.221	0.000	0.000	0.000	0.000
141	A	141	GLU	-1	-0.892	-0.912	10.610	-0.184	-0.184	0.000	0.000	0.000	0.000
142	A	142	LEU	0	-0.027	-0.012	7.114	0.038	0.038	0.000	0.000	0.000	0.000
143	A	143	ASP	-1	-0.759	-0.863	5.940	-1.115	-1.115	0.000	0.000	0.000	0.000
144	A	144	GLY	0	-0.014	-0.003	5.992	0.049	0.049	0.000	0.000	0.000	0.000
145	A	145	MET	0	-0.078	-0.033	6.834	0.105	0.105	0.000	0.000	0.000	0.000
146	A	146	LEU	0	-0.034	-0.015	2.513	-0.921	-0.182	1.015	-0.323	-1.431	0.000
147	A	147	LYS	1	0.741	0.862	3.270	-0.187	0.710	0.073	-0.356	-0.614	-0.003

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