FMO DATABASE

FMODB ID: JLJV9

Calculation Name: 1VLA-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1VLA

Chain ID: A

ChEMBL ID:

UniProt ID: Q9X021

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	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	144
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1283857.416777
FMO2-HF: Nuclear repulsion	1223219.550935
FMO2-HF: Total energy	-60637.865842
FMO2-MP2: Total energy	-60808.764295

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:-5:HIS)

Summations of interaction energy for fragment #1(A:-5:HIS)

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.
-0.709	0.572	-0.013	-0.499	-0.769	0.003

Interaction energy analysis for fragmet #1(A:-5:HIS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.030 / q_NPA : -0.025

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	HIS	0	0.023	0.015	3.782	-1.042	0.239	-0.013	-0.499	-0.769	0.003
4	A	-2	HIS	0	-0.057	-0.018	5.303	0.331	0.331	0.000	0.000	0.000	0.000
5	A	-1	HIS	0	0.031	0.010	8.860	-0.043	-0.043	0.000	0.000	0.000	0.000
6	A	0	HIS	0	-0.008	-0.016	12.233	0.045	0.045	0.000	0.000	0.000	0.000
7	A	1	MET	0	-0.001	-0.007	15.307	-0.023	-0.023	0.000	0.000	0.000	0.000
8	A	2	GLN	0	0.004	0.014	18.974	0.020	0.020	0.000	0.000	0.000	0.000
9	A	3	ALA	0	0.020	0.010	22.178	-0.009	-0.009	0.000	0.000	0.000	0.000
10	A	4	ARG	1	0.882	0.930	25.829	-0.090	-0.090	0.000	0.000	0.000	0.000
11	A	5	TRP	0	-0.023	-0.012	28.531	-0.005	-0.005	0.000	0.000	0.000	0.000
12	A	6	ILE	0	-0.044	-0.039	32.069	-0.001	-0.001	0.000	0.000	0.000	0.000
13	A	7	GLY	0	0.050	0.039	34.569	-0.005	-0.005	0.000	0.000	0.000	0.000
14	A	8	ASN	0	-0.031	-0.018	37.501	0.000	0.000	0.000	0.000	0.000	0.000
15	A	9	MET	0	0.006	0.012	36.749	0.004	0.004	0.000	0.000	0.000	0.000
16	A	10	MET	0	-0.015	0.016	34.576	0.003	0.003	0.000	0.000	0.000	0.000
17	A	11	PHE	0	-0.022	-0.021	29.389	0.003	0.003	0.000	0.000	0.000	0.000
18	A	12	HIS	0	0.000	0.001	28.349	0.000	0.000	0.000	0.000	0.000	0.000
19	A	13	VAL	0	-0.003	0.002	23.562	0.007	0.007	0.000	0.000	0.000	0.000
20	A	14	ARG	1	0.851	0.927	23.905	-0.091	-0.091	0.000	0.000	0.000	0.000
21	A	15	THR	0	-0.002	-0.018	21.589	0.009	0.009	0.000	0.000	0.000	0.000
22	A	16	ASP	-1	-0.861	-0.922	15.964	0.153	0.153	0.000	0.000	0.000	0.000
23	A	17	SER	0	-0.009	-0.009	18.811	-0.007	-0.007	0.000	0.000	0.000	0.000
24	A	18	ASN	0	-0.050	-0.022	20.801	-0.016	-0.016	0.000	0.000	0.000	0.000
25	A	19	HIS	0	-0.032	-0.015	23.363	-0.013	-0.013	0.000	0.000	0.000	0.000
26	A	20	ASP	-1	-0.830	-0.897	25.779	0.088	0.088	0.000	0.000	0.000	0.000
27	A	21	VAL	0	0.002	0.003	26.417	-0.001	-0.001	0.000	0.000	0.000	0.000
28	A	22	LEU	0	0.000	-0.001	28.967	0.003	0.003	0.000	0.000	0.000	0.000
29	A	23	MET	0	-0.011	0.000	27.736	0.003	0.003	0.000	0.000	0.000	0.000
30	A	24	ASP	-1	-0.743	-0.870	33.039	0.072	0.072	0.000	0.000	0.000	0.000
31	A	25	THR	0	-0.042	-0.048	36.519	0.002	0.002	0.000	0.000	0.000	0.000
32	A	26	LYS	1	0.924	0.946	38.875	-0.062	-0.062	0.000	0.000	0.000	0.000
33	A	27	GLU	-1	-0.814	-0.887	42.548	0.055	0.055	0.000	0.000	0.000	0.000
34	A	28	GLU	-1	-0.863	-0.925	45.005	0.058	0.058	0.000	0.000	0.000	0.000
35	A	29	VAL	0	-0.060	-0.029	40.386	0.000	0.000	0.000	0.000	0.000	0.000
36	A	30	GLY	0	0.012	0.009	41.330	0.003	0.003	0.000	0.000	0.000	0.000
37	A	31	GLY	0	-0.042	-0.024	40.490	0.001	0.001	0.000	0.000	0.000	0.000
38	A	32	LYS	1	0.804	0.871	40.791	-0.061	-0.061	0.000	0.000	0.000	0.000
39	A	33	ASP	-1	-0.869	-0.898	41.058	0.063	0.063	0.000	0.000	0.000	0.000
40	A	34	ALA	0	0.015	0.008	39.777	-0.002	-0.002	0.000	0.000	0.000	0.000
41	A	35	ALA	0	-0.054	-0.031	35.016	0.000	0.000	0.000	0.000	0.000	0.000
42	A	36	PRO	0	0.028	0.019	33.787	0.000	0.000	0.000	0.000	0.000	0.000
43	A	37	ARG	1	0.845	0.907	34.650	-0.070	-0.070	0.000	0.000	0.000	0.000
44	A	38	PRO	0	0.049	0.004	30.187	0.003	0.003	0.000	0.000	0.000	0.000
45	A	39	LEU	0	-0.033	-0.019	30.405	0.005	0.005	0.000	0.000	0.000	0.000
46	A	40	GLU	-1	-0.788	-0.890	31.819	0.084	0.084	0.000	0.000	0.000	0.000
47	A	41	LEU	0	-0.002	0.015	28.656	0.001	0.001	0.000	0.000	0.000	0.000
48	A	42	VAL	0	-0.033	-0.011	26.626	0.005	0.005	0.000	0.000	0.000	0.000
49	A	43	LEU	0	0.004	0.002	27.841	0.005	0.005	0.000	0.000	0.000	0.000
50	A	44	THR	0	0.010	-0.011	30.296	-0.002	-0.002	0.000	0.000	0.000	0.000
51	A	45	GLY	0	0.007	0.004	26.190	-0.001	-0.001	0.000	0.000	0.000	0.000
52	A	46	LEU	0	-0.008	0.001	24.556	0.004	0.004	0.000	0.000	0.000	0.000
53	A	47	MET	0	0.015	0.011	26.848	0.000	0.000	0.000	0.000	0.000	0.000
54	A	48	GLY	0	0.008	0.010	27.514	-0.003	-0.003	0.000	0.000	0.000	0.000
55	A	49	CYS	0	-0.068	-0.037	23.157	0.003	0.003	0.000	0.000	0.000	0.000
56	A	50	THR	0	0.027	0.021	24.748	-0.003	-0.003	0.000	0.000	0.000	0.000
57	A	51	GLY	0	0.064	0.008	26.944	-0.005	-0.005	0.000	0.000	0.000	0.000
58	A	52	MET	0	-0.026	-0.022	24.935	-0.009	-0.009	0.000	0.000	0.000	0.000
59	A	53	ASP	-1	-0.795	-0.835	23.330	0.156	0.156	0.000	0.000	0.000	0.000
60	A	54	VAL	0	0.013	-0.002	25.979	-0.006	-0.006	0.000	0.000	0.000	0.000
61	A	55	VAL	0	0.009	0.012	29.262	-0.007	-0.007	0.000	0.000	0.000	0.000
62	A	56	SER	0	-0.022	-0.013	24.181	-0.011	-0.011	0.000	0.000	0.000	0.000
63	A	57	ILE	0	-0.035	-0.018	25.763	-0.006	-0.006	0.000	0.000	0.000	0.000
64	A	58	LEU	0	0.065	0.019	28.395	-0.006	-0.006	0.000	0.000	0.000	0.000
65	A	59	ARG	1	0.973	0.985	28.393	-0.073	-0.073	0.000	0.000	0.000	0.000
66	A	60	LYS	1	0.924	0.975	24.751	-0.092	-0.092	0.000	0.000	0.000	0.000
67	A	61	MET	0	-0.089	-0.045	29.464	-0.006	-0.006	0.000	0.000	0.000	0.000
68	A	62	LYS	1	0.899	0.957	32.388	-0.039	-0.039	0.000	0.000	0.000	0.000
69	A	63	VAL	0	0.072	0.030	34.645	-0.003	-0.003	0.000	0.000	0.000	0.000
70	A	64	ILE	0	-0.033	-0.003	32.471	0.000	0.000	0.000	0.000	0.000	0.000
71	A	65	ASP	-1	-0.922	-0.952	35.915	0.039	0.039	0.000	0.000	0.000	0.000
72	A	66	GLN	0	0.028	0.019	38.571	-0.001	-0.001	0.000	0.000	0.000	0.000
73	A	67	MET	0	-0.067	-0.029	34.520	0.002	0.002	0.000	0.000	0.000	0.000
74	A	68	LYS	1	0.837	0.907	39.239	-0.036	-0.036	0.000	0.000	0.000	0.000
75	A	69	ASP	-1	-0.830	-0.914	39.855	0.048	0.048	0.000	0.000	0.000	0.000
76	A	70	PHE	0	-0.072	-0.054	31.960	0.002	0.002	0.000	0.000	0.000	0.000
77	A	71	ARG	1	0.766	0.873	36.398	-0.059	-0.059	0.000	0.000	0.000	0.000
78	A	72	ILE	0	-0.003	0.012	31.167	0.001	0.001	0.000	0.000	0.000	0.000
79	A	73	GLU	-1	-0.817	-0.897	35.317	0.063	0.063	0.000	0.000	0.000	0.000
80	A	74	ILE	0	-0.001	-0.008	31.490	0.003	0.003	0.000	0.000	0.000	0.000
81	A	75	GLU	-1	-0.841	-0.903	35.549	0.068	0.068	0.000	0.000	0.000	0.000
82	A	76	TYR	0	-0.012	-0.029	34.796	0.005	0.005	0.000	0.000	0.000	0.000
83	A	77	GLU	-1	-0.828	-0.892	36.486	0.071	0.071	0.000	0.000	0.000	0.000
84	A	78	ARG	1	0.929	0.955	32.348	-0.104	-0.104	0.000	0.000	0.000	0.000
85	A	79	THR	0	0.014	0.025	36.655	-0.003	-0.003	0.000	0.000	0.000	0.000
86	A	80	GLU	-1	-0.796	-0.881	38.234	0.080	0.080	0.000	0.000	0.000	0.000
87	A	81	GLU	-1	-0.884	-0.928	40.120	0.081	0.081	0.000	0.000	0.000	0.000
88	A	82	HIS	0	-0.062	-0.024	36.381	0.009	0.009	0.000	0.000	0.000	0.000
89	A	83	PRO	0	-0.007	-0.013	32.478	-0.001	-0.001	0.000	0.000	0.000	0.000
90	A	84	ARG	1	0.776	0.865	34.365	-0.088	-0.088	0.000	0.000	0.000	0.000
91	A	85	ILE	0	-0.014	-0.017	31.293	0.008	0.008	0.000	0.000	0.000	0.000
92	A	86	PHE	0	0.028	0.002	30.374	-0.006	-0.006	0.000	0.000	0.000	0.000
93	A	87	THR	0	0.024	0.007	32.840	0.004	0.004	0.000	0.000	0.000	0.000
94	A	88	LYS	1	0.871	0.938	35.234	-0.080	-0.080	0.000	0.000	0.000	0.000
95	A	89	VAL	0	0.020	0.000	30.911	0.001	0.001	0.000	0.000	0.000	0.000
96	A	90	HIS	0	-0.035	0.011	33.841	0.006	0.006	0.000	0.000	0.000	0.000
97	A	91	LEU	0	-0.006	-0.013	30.184	0.001	0.001	0.000	0.000	0.000	0.000
98	A	92	LYS	1	0.851	0.930	34.495	-0.069	-0.069	0.000	0.000	0.000	0.000
99	A	93	TYR	0	-0.033	-0.036	29.494	0.001	0.001	0.000	0.000	0.000	0.000
100	A	94	ILE	0	-0.002	0.004	36.182	-0.003	-0.003	0.000	0.000	0.000	0.000
101	A	95	PHE	0	0.007	-0.020	34.512	0.001	0.001	0.000	0.000	0.000	0.000
102	A	96	LYS	1	0.845	0.942	40.196	-0.050	-0.050	0.000	0.000	0.000	0.000
103	A	97	PHE	0	0.014	-0.017	37.469	0.001	0.001	0.000	0.000	0.000	0.000
104	A	98	ASP	-1	-0.880	-0.916	43.160	0.031	0.031	0.000	0.000	0.000	0.000
105	A	99	GLY	0	-0.004	-0.001	45.372	0.000	0.000	0.000	0.000	0.000	0.000
106	A	100	GLU	-1	-0.812	-0.899	45.603	0.043	0.043	0.000	0.000	0.000	0.000
107	A	101	PRO	0	-0.024	-0.003	41.938	0.001	0.001	0.000	0.000	0.000	0.000
108	A	102	PRO	0	0.003	0.016	38.459	-0.001	-0.001	0.000	0.000	0.000	0.000
109	A	103	LYS	1	0.850	0.901	38.529	-0.041	-0.041	0.000	0.000	0.000	0.000
110	A	104	ASP	-1	-0.821	-0.901	38.023	0.057	0.057	0.000	0.000	0.000	0.000
111	A	105	LYS	1	0.808	0.891	34.832	-0.045	-0.045	0.000	0.000	0.000	0.000
112	A	106	VAL	0	0.023	0.017	33.732	0.007	0.007	0.000	0.000	0.000	0.000
113	A	107	GLU	-1	-0.884	-0.940	33.860	0.071	0.071	0.000	0.000	0.000	0.000
114	A	108	LYS	1	0.942	0.980	28.939	-0.094	-0.094	0.000	0.000	0.000	0.000
115	A	109	ALA	0	-0.022	-0.025	29.552	0.009	0.009	0.000	0.000	0.000	0.000
116	A	110	VAL	0	0.032	0.018	28.938	0.010	0.010	0.000	0.000	0.000	0.000
117	A	111	GLN	0	0.017	0.017	29.378	0.010	0.010	0.000	0.000	0.000	0.000
118	A	112	LEU	0	-0.095	-0.042	25.059	0.010	0.010	0.000	0.000	0.000	0.000
119	A	113	SER	0	-0.004	-0.005	24.935	0.013	0.013	0.000	0.000	0.000	0.000
120	A	114	GLN	0	0.004	-0.007	24.843	0.018	0.018	0.000	0.000	0.000	0.000
121	A	115	GLU	-1	-0.791	-0.886	25.915	0.137	0.137	0.000	0.000	0.000	0.000
122	A	116	LYS	1	0.843	0.930	20.866	-0.177	-0.177	0.000	0.000	0.000	0.000
123	A	117	TYR	0	-0.070	-0.046	20.353	0.020	0.020	0.000	0.000	0.000	0.000
124	A	118	CYS	0	-0.020	0.015	20.450	0.014	0.014	0.000	0.000	0.000	0.000
125	A	119	SER	0	-0.010	-0.042	21.756	0.013	0.013	0.000	0.000	0.000	0.000
126	A	120	VAL	0	0.004	0.013	22.825	0.001	0.001	0.000	0.000	0.000	0.000
127	A	121	SER	0	0.032	-0.004	24.370	0.002	0.002	0.000	0.000	0.000	0.000
128	A	122	ALA	0	-0.031	0.004	18.908	0.005	0.005	0.000	0.000	0.000	0.000
129	A	123	ILE	0	-0.053	-0.021	19.919	0.015	0.015	0.000	0.000	0.000	0.000
130	A	124	LEU	0	-0.043	-0.015	21.786	0.000	0.000	0.000	0.000	0.000	0.000
131	A	125	LYS	1	0.947	0.969	23.269	-0.197	-0.197	0.000	0.000	0.000	0.000
132	A	126	CYS	0	-0.012	-0.008	26.721	-0.009	-0.009	0.000	0.000	0.000	0.000
133	A	127	SER	0	-0.029	-0.010	29.988	0.003	0.003	0.000	0.000	0.000	0.000
134	A	128	SER	0	-0.043	-0.042	32.495	-0.005	-0.005	0.000	0.000	0.000	0.000
135	A	129	LYS	1	0.828	0.891	28.963	-0.119	-0.119	0.000	0.000	0.000	0.000
136	A	130	VAL	0	0.022	0.020	28.408	-0.005	-0.005	0.000	0.000	0.000	0.000
137	A	131	THR	0	-0.042	-0.032	31.368	0.001	0.001	0.000	0.000	0.000	0.000
138	A	132	TYR	0	-0.020	-0.049	30.958	0.004	0.004	0.000	0.000	0.000	0.000
139	A	133	GLU	-1	-0.860	-0.912	34.958	0.066	0.066	0.000	0.000	0.000	0.000
140	A	134	ILE	0	-0.017	-0.011	35.097	0.003	0.003	0.000	0.000	0.000	0.000
141	A	135	VAL	0	0.022	0.021	38.542	-0.003	-0.003	0.000	0.000	0.000	0.000
142	A	136	TYR	0	0.020	-0.005	39.654	0.001	0.001	0.000	0.000	0.000	0.000
143	A	137	GLU	-1	-0.813	-0.891	43.578	0.051	0.051	0.000	0.000	0.000	0.000
144	A	138	ASN	0	0.016	-0.002	46.029	0.000	0.000	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:-5:HIS)