FMO DATABASE

FMODB ID: QV1GY

Calculation Name: 1WVT-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1WVT

Chain ID: A

ChEMBL ID:

UniProt ID: Q96YJ2

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	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	148
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1383332.019879
FMO2-HF: Nuclear repulsion	1326075.843649
FMO2-HF: Total energy	-57256.17623
FMO2-MP2: Total energy	-57426.617953

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:22:LYS)

Summations of interaction energy for fragment #1(A:22: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.
-25.725	-26.012	7.314	-3.279	-3.747	-0.005

Interaction energy analysis for fragmet #1(A:22:LYS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.949 / q_NPA : 0.939

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	24	SER	0	-0.043	-0.054	3.770	1.933	2.985	0.004	-0.251	-0.805	0.002
4	A	25	GLU	-1	-0.880	-0.952	5.318	-20.013	-19.890	-0.001	-0.004	-0.117	0.000
5	A	26	ILE	0	0.034	0.015	4.355	0.865	1.050	-0.001	-0.019	-0.165	0.000
6	A	27	VAL	0	-0.054	-0.019	2.142	-0.724	-2.432	7.313	-2.980	-2.625	-0.007
7	A	28	LYS	1	0.957	0.989	4.802	21.019	21.080	-0.001	-0.025	-0.035	0.000
8	A	29	ALA	0	0.014	0.003	8.163	1.383	1.383	0.000	0.000	0.000	0.000
9	A	30	LEU	0	-0.026	-0.018	6.011	0.914	0.914	0.000	0.000	0.000	0.000
10	A	31	GLY	0	0.012	0.022	8.894	0.214	0.214	0.000	0.000	0.000	0.000
11	A	32	ASP	-1	-0.795	-0.877	9.936	-18.869	-18.869	0.000	0.000	0.000	0.000
12	A	33	LEU	0	-0.028	-0.019	11.768	1.585	1.585	0.000	0.000	0.000	0.000
13	A	34	ASP	-1	-0.901	-0.936	10.994	-23.377	-23.377	0.000	0.000	0.000	0.000
14	A	35	GLU	-1	-0.842	-0.916	13.085	-18.252	-18.252	0.000	0.000	0.000	0.000
15	A	36	LEU	0	-0.036	-0.016	15.510	1.373	1.373	0.000	0.000	0.000	0.000
16	A	37	ASN	0	0.051	0.005	16.150	1.831	1.831	0.000	0.000	0.000	0.000
17	A	38	SER	0	-0.001	0.005	15.829	0.850	0.850	0.000	0.000	0.000	0.000
18	A	39	VAL	0	-0.043	-0.017	18.532	0.922	0.922	0.000	0.000	0.000	0.000
19	A	40	LEU	0	-0.011	-0.009	20.736	0.845	0.845	0.000	0.000	0.000	0.000
20	A	41	GLY	0	0.050	0.032	21.558	0.631	0.631	0.000	0.000	0.000	0.000
21	A	42	VAL	0	-0.021	-0.004	22.511	0.585	0.585	0.000	0.000	0.000	0.000
22	A	43	VAL	0	-0.010	-0.017	24.762	0.594	0.594	0.000	0.000	0.000	0.000
23	A	44	SER	0	-0.005	0.015	26.056	0.679	0.679	0.000	0.000	0.000	0.000
24	A	45	SER	0	-0.030	-0.014	25.752	0.296	0.296	0.000	0.000	0.000	0.000
25	A	46	LEU	0	-0.061	-0.032	28.363	0.417	0.417	0.000	0.000	0.000	0.000
26	A	47	TYR	0	-0.014	-0.015	30.699	0.441	0.441	0.000	0.000	0.000	0.000
27	A	48	PRO	0	0.083	0.040	31.494	-0.095	-0.095	0.000	0.000	0.000	0.000
28	A	49	GLU	-1	-0.971	-0.972	32.540	-8.381	-8.381	0.000	0.000	0.000	0.000
29	A	50	LEU	0	-0.042	-0.026	31.123	0.091	0.091	0.000	0.000	0.000	0.000
30	A	51	SER	0	0.017	-0.009	28.876	-0.222	-0.222	0.000	0.000	0.000	0.000
31	A	52	GLU	-1	-0.940	-0.950	28.344	-9.721	-9.721	0.000	0.000	0.000	0.000
32	A	53	VAL	0	-0.020	-0.021	29.101	-0.228	-0.228	0.000	0.000	0.000	0.000
33	A	54	ILE	0	-0.001	-0.015	24.787	-0.342	-0.342	0.000	0.000	0.000	0.000
34	A	55	GLN	0	0.025	0.002	24.263	-0.307	-0.307	0.000	0.000	0.000	0.000
35	A	56	LYS	1	0.959	0.993	23.807	9.584	9.584	0.000	0.000	0.000	0.000
36	A	57	LEU	0	-0.003	0.008	23.965	-0.312	-0.312	0.000	0.000	0.000	0.000
37	A	58	GLN	0	-0.008	-0.011	20.319	-0.110	-0.110	0.000	0.000	0.000	0.000
38	A	59	ASN	0	-0.047	-0.026	19.321	-0.371	-0.371	0.000	0.000	0.000	0.000
39	A	60	ASP	-1	-0.789	-0.900	19.841	-13.276	-13.276	0.000	0.000	0.000	0.000
40	A	61	ILE	0	-0.049	-0.018	15.992	-0.498	-0.498	0.000	0.000	0.000	0.000
41	A	62	PHE	0	-0.010	-0.008	13.558	-1.142	-1.142	0.000	0.000	0.000	0.000
42	A	63	SER	0	0.016	0.003	15.225	-0.866	-0.866	0.000	0.000	0.000	0.000
43	A	64	ILE	0	-0.035	-0.007	14.592	-0.493	-0.493	0.000	0.000	0.000	0.000
44	A	65	SER	0	-0.027	-0.019	11.549	-1.154	-1.154	0.000	0.000	0.000	0.000
45	A	66	SER	0	0.049	0.009	10.989	-2.014	-2.014	0.000	0.000	0.000	0.000
46	A	67	GLU	-1	-0.785	-0.870	11.312	-16.175	-16.175	0.000	0.000	0.000	0.000
47	A	68	ILE	0	-0.040	-0.009	8.586	-0.359	-0.359	0.000	0.000	0.000	0.000
48	A	69	ALA	0	-0.075	-0.031	7.161	-1.225	-1.225	0.000	0.000	0.000	0.000
49	A	70	GLY	0	-0.026	-0.020	7.781	-1.625	-1.625	0.000	0.000	0.000	0.000
50	A	71	PHE	0	-0.079	-0.032	8.814	1.139	1.139	0.000	0.000	0.000	0.000
51	A	72	ASP	-1	-0.919	-0.977	12.851	-15.986	-15.986	0.000	0.000	0.000	0.000
52	A	73	MET	0	-0.057	-0.039	15.698	-0.049	-0.049	0.000	0.000	0.000	0.000
53	A	74	ASN	0	-0.070	-0.022	18.757	0.358	0.358	0.000	0.000	0.000	0.000
54	A	75	PHE	0	0.002	0.017	19.285	0.551	0.551	0.000	0.000	0.000	0.000
55	A	76	SER	0	0.052	0.017	21.248	0.016	0.016	0.000	0.000	0.000	0.000
56	A	77	ASP	-1	-0.889	-0.956	24.524	-11.281	-11.281	0.000	0.000	0.000	0.000
57	A	78	GLU	-1	-0.971	-0.993	26.185	-9.698	-9.698	0.000	0.000	0.000	0.000
58	A	79	LYS	1	0.887	0.945	23.370	12.296	12.296	0.000	0.000	0.000	0.000
59	A	80	VAL	0	0.002	-0.002	24.459	0.040	0.040	0.000	0.000	0.000	0.000
60	A	81	LYS	1	0.957	0.989	26.840	9.178	9.178	0.000	0.000	0.000	0.000
61	A	82	GLY	0	0.049	0.031	29.435	0.253	0.253	0.000	0.000	0.000	0.000
62	A	83	ILE	0	-0.030	-0.010	25.812	0.182	0.182	0.000	0.000	0.000	0.000
63	A	84	GLU	-1	-0.916	-0.977	29.245	-9.295	-9.295	0.000	0.000	0.000	0.000
64	A	85	GLU	-1	-0.943	-0.959	31.791	-8.322	-8.322	0.000	0.000	0.000	0.000
65	A	86	LEU	0	-0.010	-0.008	29.823	0.245	0.245	0.000	0.000	0.000	0.000
66	A	87	ILE	0	-0.047	-0.026	29.613	0.204	0.204	0.000	0.000	0.000	0.000
67	A	88	THR	0	-0.033	-0.010	33.641	0.292	0.292	0.000	0.000	0.000	0.000
68	A	89	ASN	0	-0.024	-0.035	36.964	0.391	0.391	0.000	0.000	0.000	0.000
69	A	90	TYR	0	0.017	0.013	33.552	0.186	0.186	0.000	0.000	0.000	0.000
70	A	91	SER	0	-0.001	-0.019	36.571	0.105	0.105	0.000	0.000	0.000	0.000
71	A	92	LYS	1	0.891	0.969	38.855	7.541	7.541	0.000	0.000	0.000	0.000
72	A	93	GLU	-1	-0.778	-0.855	40.033	-7.723	-7.723	0.000	0.000	0.000	0.000
73	A	94	LEU	0	-0.113	-0.051	37.594	0.097	0.097	0.000	0.000	0.000	0.000
74	A	95	GLU	-1	-0.897	-0.938	42.229	-6.544	-6.544	0.000	0.000	0.000	0.000
75	A	96	PRO	0	-0.004	-0.002	42.870	-0.180	-0.180	0.000	0.000	0.000	0.000
76	A	97	LEU	0	0.000	0.006	38.332	0.070	0.070	0.000	0.000	0.000	0.000
77	A	98	ARG	1	0.915	0.943	42.372	6.576	6.576	0.000	0.000	0.000	0.000
78	A	99	ASN	0	0.012	0.002	41.821	0.147	0.147	0.000	0.000	0.000	0.000
79	A	100	PHE	0	0.031	0.023	36.121	-0.132	-0.132	0.000	0.000	0.000	0.000
80	A	101	VAL	0	-0.003	-0.006	35.564	0.109	0.109	0.000	0.000	0.000	0.000
81	A	102	LEU	0	-0.043	-0.030	34.696	-0.226	-0.226	0.000	0.000	0.000	0.000
82	A	103	PRO	0	-0.018	-0.019	30.883	0.109	0.109	0.000	0.000	0.000	0.000
83	A	104	GLY	0	0.047	0.016	33.352	0.095	0.095	0.000	0.000	0.000	0.000
84	A	105	GLY	0	-0.012	0.015	35.601	-0.018	-0.018	0.000	0.000	0.000	0.000
85	A	106	HIS	0	0.082	0.042	34.793	-0.232	-0.232	0.000	0.000	0.000	0.000
86	A	107	ILE	0	0.024	0.001	31.318	-0.205	-0.205	0.000	0.000	0.000	0.000
87	A	108	ALA	0	0.054	0.018	30.768	-0.354	-0.354	0.000	0.000	0.000	0.000
88	A	109	SER	0	-0.026	-0.010	30.604	-0.330	-0.330	0.000	0.000	0.000	0.000
89	A	110	SER	0	-0.019	-0.017	31.233	-0.169	-0.169	0.000	0.000	0.000	0.000
90	A	111	PHE	0	0.043	0.004	25.544	-0.317	-0.317	0.000	0.000	0.000	0.000
91	A	112	LEU	0	0.016	0.030	26.364	-0.518	-0.518	0.000	0.000	0.000	0.000
92	A	113	HIS	0	-0.012	-0.012	27.210	-0.481	-0.481	0.000	0.000	0.000	0.000
93	A	114	LEU	0	-0.025	0.001	22.607	-0.200	-0.200	0.000	0.000	0.000	0.000
94	A	115	ALA	0	0.069	0.032	22.714	-0.570	-0.570	0.000	0.000	0.000	0.000
95	A	116	ARG	1	0.906	0.948	22.670	10.075	10.075	0.000	0.000	0.000	0.000
96	A	117	ALA	0	-0.042	-0.021	23.487	-0.185	-0.185	0.000	0.000	0.000	0.000
97	A	118	VAL	0	0.003	-0.002	18.089	-0.295	-0.295	0.000	0.000	0.000	0.000
98	A	119	CYS	0	0.005	0.016	18.663	-0.661	-0.661	0.000	0.000	0.000	0.000
99	A	120	ARG	1	0.948	0.966	19.482	11.268	11.268	0.000	0.000	0.000	0.000
100	A	121	ARG	1	0.719	0.854	15.198	18.115	18.115	0.000	0.000	0.000	0.000
101	A	122	ALA	0	0.077	0.026	14.951	-0.493	-0.493	0.000	0.000	0.000	0.000
102	A	123	GLU	-1	-0.901	-0.963	15.366	-12.936	-12.936	0.000	0.000	0.000	0.000
103	A	124	ARG	1	0.892	0.952	17.047	14.540	14.540	0.000	0.000	0.000	0.000
104	A	125	SER	0	-0.053	-0.051	11.558	0.221	0.221	0.000	0.000	0.000	0.000
105	A	126	VAL	0	0.048	0.024	12.587	-0.565	-0.565	0.000	0.000	0.000	0.000
106	A	127	VAL	0	-0.010	-0.006	14.069	0.247	0.247	0.000	0.000	0.000	0.000
107	A	128	THR	0	-0.071	-0.030	12.584	0.536	0.536	0.000	0.000	0.000	0.000
108	A	129	LEU	0	0.000	-0.006	8.770	-0.102	-0.102	0.000	0.000	0.000	0.000
109	A	130	LEU	0	0.000	0.027	12.684	0.200	0.200	0.000	0.000	0.000	0.000
110	A	131	LYS	1	0.943	0.976	15.809	13.209	13.209	0.000	0.000	0.000	0.000
111	A	132	GLU	-1	-0.955	-0.995	12.722	-16.570	-16.570	0.000	0.000	0.000	0.000
112	A	133	SER	0	-0.061	-0.017	13.684	-0.032	-0.032	0.000	0.000	0.000	0.000
113	A	134	LYS	1	0.848	0.920	8.341	21.942	21.942	0.000	0.000	0.000	0.000
114	A	135	ALA	0	-0.012	-0.011	10.985	-1.077	-1.077	0.000	0.000	0.000	0.000
115	A	136	LYS	1	0.973	0.983	13.739	15.260	15.260	0.000	0.000	0.000	0.000
116	A	137	GLU	-1	-0.910	-0.962	17.277	-11.787	-11.787	0.000	0.000	0.000	0.000
117	A	138	VAL	0	0.010	0.003	19.712	0.185	0.185	0.000	0.000	0.000	0.000
118	A	139	HIS	0	-0.003	-0.009	14.572	0.004	0.004	0.000	0.000	0.000	0.000
119	A	140	ALA	0	0.041	0.015	18.422	0.046	0.046	0.000	0.000	0.000	0.000
120	A	141	LYN	0	0.050	0.060	19.417	0.356	0.356	0.000	0.000	0.000	0.000
121	A	142	TYR	0	0.007	-0.019	20.670	0.292	0.292	0.000	0.000	0.000	0.000
122	A	143	LEU	0	0.018	0.010	16.393	0.320	0.320	0.000	0.000	0.000	0.000
123	A	144	ASN	0	-0.047	-0.006	21.052	0.621	0.621	0.000	0.000	0.000	0.000
124	A	145	ARG	1	0.907	0.922	23.796	10.429	10.429	0.000	0.000	0.000	0.000
125	A	146	LEU	0	0.038	0.034	21.333	0.369	0.369	0.000	0.000	0.000	0.000
126	A	147	SER	0	-0.006	-0.011	23.712	0.399	0.399	0.000	0.000	0.000	0.000
127	A	148	SER	0	-0.048	-0.023	25.441	0.404	0.404	0.000	0.000	0.000	0.000
128	A	149	LEU	0	0.046	0.028	27.764	0.354	0.354	0.000	0.000	0.000	0.000
129	A	150	LEU	0	-0.001	-0.005	24.075	0.271	0.271	0.000	0.000	0.000	0.000
130	A	151	PHE	0	-0.026	-0.011	28.640	0.181	0.181	0.000	0.000	0.000	0.000
131	A	152	VAL	0	0.018	0.011	31.137	0.254	0.254	0.000	0.000	0.000	0.000
132	A	153	LEU	0	0.040	0.015	29.360	0.240	0.240	0.000	0.000	0.000	0.000
133	A	154	ALA	0	-0.001	0.007	31.404	0.165	0.165	0.000	0.000	0.000	0.000
134	A	155	LEU	0	-0.042	-0.013	33.160	0.262	0.262	0.000	0.000	0.000	0.000
135	A	156	VAL	0	0.006	0.011	35.795	0.246	0.246	0.000	0.000	0.000	0.000
136	A	157	VAL	0	0.005	0.014	33.350	0.215	0.215	0.000	0.000	0.000	0.000
137	A	158	ASN	0	0.015	0.002	36.617	0.159	0.159	0.000	0.000	0.000	0.000
138	A	159	LYS	1	0.872	0.951	38.833	7.293	7.293	0.000	0.000	0.000	0.000
139	A	160	ARG	1	0.837	0.879	37.787	8.332	8.332	0.000	0.000	0.000	0.000
140	A	161	THR	0	-0.062	-0.030	38.467	0.121	0.121	0.000	0.000	0.000	0.000
141	A	162	ASN	0	-0.052	-0.015	41.597	0.135	0.135	0.000	0.000	0.000	0.000
142	A	163	ASN	0	-0.030	-0.021	40.100	0.094	0.094	0.000	0.000	0.000	0.000
143	A	164	PRO	0	0.000	-0.004	41.386	-0.088	-0.088	0.000	0.000	0.000	0.000
144	A	165	ASN	0	0.039	0.017	38.557	-0.347	-0.347	0.000	0.000	0.000	0.000
145	A	166	VAL	0	0.039	0.031	37.915	0.204	0.204	0.000	0.000	0.000	0.000
146	A	167	ILE	0	-0.027	-0.007	38.839	-0.177	-0.177	0.000	0.000	0.000	0.000
147	A	168	TRP	0	-0.023	-0.017	38.460	0.101	0.101	0.000	0.000	0.000	0.000
148	A	169	ARG	1	0.982	1.002	40.382	7.674	7.674	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:22:LYS)