FMO DATABASE

FMODB ID: VQR91

Calculation Name: 1W8I-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1W8I

Chain ID: A

ChEMBL ID:

UniProt ID: O28590

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	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	155
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1550484.703534
FMO2-HF: Nuclear repulsion	1489289.11014
FMO2-HF: Total energy	-61195.593394
FMO2-MP2: Total energy	-61378.12669

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:MET)

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

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.
-22.824	-16.613	4.838	-5.573	-5.476	-0.021

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.044 / q_NPA : -0.034

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	ALA	0	-0.013	-0.002	3.836	2.412	4.038	-0.020	-0.832	-0.774	0.001
4	A	4	LEU	0	0.003	0.012	6.277	-0.416	-0.416	0.000	0.000	0.000	0.000
5	A	5	ILE	0	-0.012	-0.007	10.101	0.189	0.189	0.000	0.000	0.000	0.000
6	A	6	ASP	-1	-0.717	-0.848	12.305	0.032	0.032	0.000	0.000	0.000	0.000
7	A	7	THR	0	0.031	-0.020	15.786	-0.016	-0.016	0.000	0.000	0.000	0.000
8	A	8	GLY	0	-0.032	-0.022	19.154	-0.005	-0.005	0.000	0.000	0.000	0.000
9	A	9	ILE	0	-0.041	-0.014	14.047	0.008	0.008	0.000	0.000	0.000	0.000
10	A	10	PHE	0	0.046	0.017	14.358	-0.004	-0.004	0.000	0.000	0.000	0.000
11	A	11	PHE	0	-0.003	-0.005	19.140	-0.001	-0.001	0.000	0.000	0.000	0.000
12	A	12	GLY	0	0.025	0.010	21.200	0.001	0.001	0.000	0.000	0.000	0.000
13	A	13	PHE	0	-0.006	-0.004	19.011	0.003	0.003	0.000	0.000	0.000	0.000
14	A	14	TYR	0	0.072	0.017	21.102	-0.001	-0.001	0.000	0.000	0.000	0.000
15	A	15	SER	0	-0.013	0.007	24.378	0.003	0.003	0.000	0.000	0.000	0.000
16	A	16	LEU	0	0.035	0.007	26.003	0.012	0.012	0.000	0.000	0.000	0.000
17	A	17	LYS	1	0.848	0.911	27.675	-0.026	-0.026	0.000	0.000	0.000	0.000
18	A	18	ASP	-1	-0.819	-0.904	23.652	0.060	0.060	0.000	0.000	0.000	0.000
19	A	19	VAL	0	-0.056	-0.021	24.861	0.003	0.003	0.000	0.000	0.000	0.000
20	A	20	HIS	1	0.872	0.932	20.395	-0.116	-0.116	0.000	0.000	0.000	0.000
21	A	21	HIS	1	0.813	0.936	20.960	-0.003	-0.003	0.000	0.000	0.000	0.000
22	A	22	MET	0	0.021	0.000	21.421	-0.011	-0.011	0.000	0.000	0.000	0.000
23	A	23	ASP	-1	-0.806	-0.887	17.757	0.162	0.162	0.000	0.000	0.000	0.000
24	A	24	SER	0	0.041	0.018	16.887	0.003	0.003	0.000	0.000	0.000	0.000
25	A	25	VAL	0	-0.017	0.006	16.986	-0.022	-0.022	0.000	0.000	0.000	0.000
26	A	26	ALA	0	-0.005	-0.003	16.313	-0.019	-0.019	0.000	0.000	0.000	0.000
27	A	27	ILE	0	-0.034	-0.008	11.776	-0.003	-0.003	0.000	0.000	0.000	0.000
28	A	28	VAL	0	0.032	0.018	12.327	-0.055	-0.055	0.000	0.000	0.000	0.000
29	A	29	VAL	0	-0.013	-0.003	13.764	-0.053	-0.053	0.000	0.000	0.000	0.000
30	A	30	HIS	0	-0.002	-0.010	10.435	0.012	0.012	0.000	0.000	0.000	0.000
31	A	31	ALA	0	-0.016	0.001	8.968	-0.082	-0.082	0.000	0.000	0.000	0.000
32	A	32	VAL	0	-0.004	-0.002	9.659	-0.158	-0.158	0.000	0.000	0.000	0.000
33	A	33	GLU	-1	-0.830	-0.876	11.875	-0.042	-0.042	0.000	0.000	0.000	0.000
34	A	34	GLY	0	0.026	0.019	7.970	0.058	0.058	0.000	0.000	0.000	0.000
35	A	35	LYS	1	0.832	0.924	6.121	-0.692	-0.692	0.000	0.000	0.000	0.000
36	A	36	TRP	0	-0.019	-0.023	3.395	-0.075	0.537	0.011	-0.210	-0.413	-0.001
37	A	37	GLY	0	-0.006	0.006	2.097	-7.958	-6.687	4.070	-2.950	-2.391	-0.043
38	A	38	ARG	1	0.881	0.941	3.964	2.634	2.958	0.000	-0.049	-0.275	0.000
39	A	39	LEU	0	0.004	0.012	6.232	-0.167	-0.167	0.000	0.000	0.000	0.000
40	A	40	PHE	0	0.005	-0.008	6.221	-0.034	-0.034	0.000	0.000	0.000	0.000
41	A	41	VAL	0	0.026	0.018	11.145	0.142	0.142	0.000	0.000	0.000	0.000
42	A	42	THR	0	0.073	0.041	14.459	-0.058	-0.058	0.000	0.000	0.000	0.000
43	A	43	ASN	0	0.045	0.009	16.525	0.004	0.004	0.000	0.000	0.000	0.000
44	A	44	HIS	0	-0.025	-0.022	19.860	0.031	0.031	0.000	0.000	0.000	0.000
45	A	45	ILE	0	0.004	0.007	15.700	0.013	0.013	0.000	0.000	0.000	0.000
46	A	46	LEU	0	-0.016	0.004	19.351	0.014	0.014	0.000	0.000	0.000	0.000
47	A	47	ASP	-1	-0.873	-0.925	20.590	-0.099	-0.099	0.000	0.000	0.000	0.000
48	A	48	GLU	-1	-0.796	-0.853	22.045	-0.031	-0.031	0.000	0.000	0.000	0.000
49	A	49	THR	0	-0.012	-0.023	19.988	0.022	0.022	0.000	0.000	0.000	0.000
50	A	50	LEU	0	-0.018	-0.003	22.499	0.013	0.013	0.000	0.000	0.000	0.000
51	A	51	THR	0	-0.036	-0.031	25.085	0.014	0.014	0.000	0.000	0.000	0.000
52	A	52	LEU	0	-0.035	-0.011	23.977	0.012	0.012	0.000	0.000	0.000	0.000
53	A	53	LEU	0	-0.021	-0.013	22.569	0.012	0.012	0.000	0.000	0.000	0.000
54	A	54	LYS	1	1.000	1.004	26.877	0.088	0.088	0.000	0.000	0.000	0.000
55	A	55	TYR	0	-0.032	-0.017	30.069	0.010	0.010	0.000	0.000	0.000	0.000
56	A	56	LYS	1	0.843	0.919	29.063	0.018	0.018	0.000	0.000	0.000	0.000
57	A	57	LYS	1	0.908	0.956	31.200	0.034	0.034	0.000	0.000	0.000	0.000
58	A	58	LEU	0	-0.004	0.017	26.339	0.003	0.003	0.000	0.000	0.000	0.000
59	A	59	PRO	0	0.027	0.008	26.482	-0.005	-0.005	0.000	0.000	0.000	0.000
60	A	60	ALA	0	0.018	0.001	25.514	-0.009	-0.009	0.000	0.000	0.000	0.000
61	A	61	ASP	-1	-0.819	-0.881	25.602	-0.104	-0.104	0.000	0.000	0.000	0.000
62	A	62	LYS	1	0.775	0.851	24.677	0.088	0.088	0.000	0.000	0.000	0.000
63	A	63	PHE	0	-0.011	0.005	18.135	-0.012	-0.012	0.000	0.000	0.000	0.000
64	A	64	LEU	0	0.006	0.001	21.245	-0.025	-0.025	0.000	0.000	0.000	0.000
65	A	65	GLU	-1	-0.788	-0.891	22.321	-0.143	-0.143	0.000	0.000	0.000	0.000
66	A	66	GLY	0	0.004	0.004	21.006	-0.014	-0.014	0.000	0.000	0.000	0.000
67	A	67	PHE	0	-0.063	-0.025	15.320	-0.021	-0.021	0.000	0.000	0.000	0.000
68	A	68	VAL	0	-0.025	-0.009	17.191	-0.051	-0.051	0.000	0.000	0.000	0.000
69	A	69	GLU	-1	-0.931	-0.978	19.715	-0.212	-0.212	0.000	0.000	0.000	0.000
70	A	70	SER	0	-0.059	-0.038	18.529	-0.020	-0.020	0.000	0.000	0.000	0.000
71	A	71	GLY	0	-0.018	-0.005	17.072	-0.018	-0.018	0.000	0.000	0.000	0.000
72	A	72	VAL	0	-0.055	-0.021	13.399	-0.086	-0.086	0.000	0.000	0.000	0.000
73	A	73	LEU	0	-0.011	0.010	12.544	-0.098	-0.098	0.000	0.000	0.000	0.000
74	A	74	ASN	0	-0.047	-0.024	10.593	-0.180	-0.180	0.000	0.000	0.000	0.000
75	A	75	ILE	0	0.030	0.006	13.261	-0.002	-0.002	0.000	0.000	0.000	0.000
76	A	76	ILE	0	-0.011	-0.004	10.523	-0.020	-0.020	0.000	0.000	0.000	0.000
77	A	77	TYR	0	-0.019	-0.025	14.783	0.086	0.086	0.000	0.000	0.000	0.000
78	A	78	THR	0	-0.035	-0.041	17.262	-0.035	-0.035	0.000	0.000	0.000	0.000
79	A	79	ASP	-1	-0.830	-0.905	18.148	-0.280	-0.280	0.000	0.000	0.000	0.000
80	A	80	ASP	-1	-0.898	-0.968	20.879	-0.166	-0.166	0.000	0.000	0.000	0.000
81	A	81	GLU	-1	-0.773	-0.852	20.695	-0.112	-0.112	0.000	0.000	0.000	0.000
82	A	82	VAL	0	-0.009	-0.013	16.716	0.023	0.023	0.000	0.000	0.000	0.000
83	A	83	GLU	-1	-0.765	-0.829	19.801	-0.122	-0.122	0.000	0.000	0.000	0.000
84	A	84	ARG	1	0.712	0.831	22.900	0.115	0.115	0.000	0.000	0.000	0.000
85	A	85	LYS	1	0.809	0.898	18.210	0.206	0.206	0.000	0.000	0.000	0.000
86	A	86	ALA	0	0.022	0.020	20.847	0.026	0.026	0.000	0.000	0.000	0.000
87	A	87	LEU	0	0.000	-0.005	22.270	0.022	0.022	0.000	0.000	0.000	0.000
88	A	88	GLU	-1	-0.905	-0.950	24.749	-0.035	-0.035	0.000	0.000	0.000	0.000
89	A	89	VAL	0	0.012	0.004	20.511	0.014	0.014	0.000	0.000	0.000	0.000
90	A	90	PHE	0	-0.011	-0.016	23.873	0.011	0.011	0.000	0.000	0.000	0.000
91	A	91	LYS	1	0.915	0.954	25.945	0.019	0.019	0.000	0.000	0.000	0.000
92	A	92	ALA	0	-0.064	-0.034	26.080	0.005	0.005	0.000	0.000	0.000	0.000
93	A	93	ARG	1	0.753	0.842	21.506	-0.109	-0.109	0.000	0.000	0.000	0.000
94	A	94	VAL	0	-0.021	0.012	27.552	0.003	0.003	0.000	0.000	0.000	0.000
95	A	95	TYR	0	-0.036	-0.022	30.341	-0.004	-0.004	0.000	0.000	0.000	0.000
96	A	96	GLU	-1	-0.856	-0.889	26.627	0.102	0.102	0.000	0.000	0.000	0.000
97	A	97	LYS	1	0.920	0.942	28.793	-0.053	-0.053	0.000	0.000	0.000	0.000
98	A	98	GLY	0	-0.043	-0.029	27.237	0.010	0.010	0.000	0.000	0.000	0.000
99	A	99	PHE	0	0.016	0.035	20.848	-0.003	-0.003	0.000	0.000	0.000	0.000
100	A	100	SER	0	-0.024	-0.046	23.405	-0.018	-0.018	0.000	0.000	0.000	0.000
101	A	101	TYR	0	-0.028	-0.052	23.824	0.015	0.015	0.000	0.000	0.000	0.000
102	A	102	THR	0	0.029	-0.011	20.012	-0.015	-0.015	0.000	0.000	0.000	0.000
103	A	103	ASP	-1	-0.817	-0.858	19.425	0.037	0.037	0.000	0.000	0.000	0.000
104	A	104	ALA	0	0.009	-0.003	18.896	0.015	0.015	0.000	0.000	0.000	0.000
105	A	105	ILE	0	0.000	-0.001	18.055	-0.005	-0.005	0.000	0.000	0.000	0.000
106	A	106	SER	0	-0.055	-0.041	15.504	-0.038	-0.038	0.000	0.000	0.000	0.000
107	A	107	GLU	-1	-0.807	-0.889	14.363	0.166	0.166	0.000	0.000	0.000	0.000
108	A	108	VAL	0	0.011	0.014	14.665	0.025	0.025	0.000	0.000	0.000	0.000
109	A	109	VAL	0	0.005	-0.003	12.170	-0.031	-0.031	0.000	0.000	0.000	0.000
110	A	110	ALA	0	-0.028	-0.016	10.270	-0.096	-0.096	0.000	0.000	0.000	0.000
111	A	111	GLU	-1	-0.835	-0.908	9.744	0.246	0.246	0.000	0.000	0.000	0.000
112	A	112	GLU	-1	-0.802	-0.892	11.037	-0.227	-0.227	0.000	0.000	0.000	0.000
113	A	113	LEU	0	-0.049	-0.021	8.408	-0.137	-0.137	0.000	0.000	0.000	0.000
114	A	114	LYS	1	0.735	0.853	6.708	-0.378	-0.378	0.000	0.000	0.000	0.000
115	A	115	LEU	0	-0.037	0.010	5.257	0.511	0.511	0.000	0.000	0.000	0.000
116	A	116	LYS	1	0.913	0.941	2.680	-16.948	-14.570	0.777	-1.532	-1.623	0.022
117	A	117	LEU	0	0.051	0.039	7.079	-0.462	-0.462	0.000	0.000	0.000	0.000
118	A	118	ILE	0	-0.026	-0.008	7.399	0.085	0.085	0.000	0.000	0.000	0.000
119	A	119	SER	0	0.036	-0.026	11.162	-0.117	-0.117	0.000	0.000	0.000	0.000
120	A	120	TYR	0	-0.066	-0.045	14.967	0.062	0.062	0.000	0.000	0.000	0.000
121	A	121	ASP	-1	-0.751	-0.860	18.192	0.165	0.165	0.000	0.000	0.000	0.000
122	A	122	SER	0	-0.127	-0.080	18.566	0.041	0.041	0.000	0.000	0.000	0.000
123	A	123	ARG	1	0.860	0.926	20.962	-0.150	-0.150	0.000	0.000	0.000	0.000
124	A	124	PHE	0	0.042	0.038	17.004	-0.001	-0.001	0.000	0.000	0.000	0.000
125	A	125	SER	0	-0.085	-0.050	18.199	0.040	0.040	0.000	0.000	0.000	0.000
126	A	126	LEU	0	-0.007	0.007	12.465	0.042	0.042	0.000	0.000	0.000	0.000
127	A	127	PRO	0	-0.037	-0.017	11.931	-0.037	-0.037	0.000	0.000	0.000	0.000
128	A	128	THR	0	-0.021	-0.010	12.401	0.069	0.069	0.000	0.000	0.000	0.000
129	A	129	ILE	0	-0.042	-0.016	7.966	0.029	0.029	0.000	0.000	0.000	0.000
130	A	130	GLY	0	0.093	0.018	12.145	-0.087	-0.087	0.000	0.000	0.000	0.000
131	A	131	ARG	1	0.877	0.929	14.898	-0.382	-0.382	0.000	0.000	0.000	0.000
132	A	132	ASP	-1	-0.863	-0.928	17.612	0.224	0.224	0.000	0.000	0.000	0.000
133	A	133	TYR	0	0.046	0.027	11.832	0.037	0.037	0.000	0.000	0.000	0.000
134	A	134	TRP	0	0.038	0.009	16.895	0.005	0.005	0.000	0.000	0.000	0.000
135	A	135	LYS	1	0.835	0.892	19.403	-0.168	-0.168	0.000	0.000	0.000	0.000
136	A	136	SER	0	-0.080	-0.043	16.573	0.013	0.013	0.000	0.000	0.000	0.000
137	A	137	LEU	0	-0.002	0.015	14.619	0.014	0.014	0.000	0.000	0.000	0.000
138	A	138	ASP	-1	-0.861	-0.932	18.362	0.210	0.210	0.000	0.000	0.000	0.000
139	A	139	GLU	-1	-0.821	-0.898	20.977	0.086	0.086	0.000	0.000	0.000	0.000
140	A	140	SER	0	-0.011	-0.015	22.499	-0.012	-0.012	0.000	0.000	0.000	0.000
141	A	141	GLU	-1	-0.694	-0.801	16.175	0.082	0.082	0.000	0.000	0.000	0.000
142	A	142	ARG	1	0.857	0.934	20.220	-0.174	-0.174	0.000	0.000	0.000	0.000
143	A	143	LYS	1	0.861	0.928	21.873	-0.095	-0.095	0.000	0.000	0.000	0.000
144	A	144	ARG	1	0.720	0.791	15.614	-0.045	-0.045	0.000	0.000	0.000	0.000
145	A	145	ILE	0	0.018	0.007	16.702	-0.016	-0.016	0.000	0.000	0.000	0.000
146	A	146	SER	0	-0.036	-0.039	20.674	-0.013	-0.013	0.000	0.000	0.000	0.000
147	A	147	ALA	0	-0.057	-0.022	24.321	-0.008	-0.008	0.000	0.000	0.000	0.000
148	A	148	ILE	0	-0.035	-0.027	18.899	-0.009	-0.009	0.000	0.000	0.000	0.000
149	A	149	LEU	0	-0.004	-0.002	22.862	-0.009	-0.009	0.000	0.000	0.000	0.000
150	A	150	ARG	1	0.822	0.905	24.046	-0.025	-0.025	0.000	0.000	0.000	0.000
151	A	151	GLU	-1	-0.842	-0.924	26.904	0.001	0.001	0.000	0.000	0.000	0.000
152	A	152	LYS	1	0.879	0.941	23.151	0.021	0.021	0.000	0.000	0.000	0.000
153	A	153	GLY	0	-0.003	0.022	25.371	-0.010	-0.010	0.000	0.000	0.000	0.000
154	A	154	ILE	0	-0.005	0.013	20.210	-0.008	-0.008	0.000	0.000	0.000	0.000
155	A	155	ASP	-1	-0.837	-0.925	22.587	-0.010	-0.010	0.000	0.000	0.000	0.000

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