FMO DATABASE

FMODB ID: MN2JZ

Calculation Name: 2A1V-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2A1V

Chain ID: A

ChEMBL ID:

UniProt ID: Q9RRT5

Base Structure: X-ray

Registration Date: 2023-09-23

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	138
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1250316.181578
FMO2-HF: Nuclear repulsion	1196302.498709
FMO2-HF: Total energy	-54013.682869
FMO2-MP2: Total energy	-54172.804483

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:3:LEU)

Summations of interaction energy for fragment #1(A:3: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.
-7.18	-3.273	0.492	-1.938	-2.46	-0.008

Interaction energy analysis for fragmet #1(A:3:LEU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.003 / q_NPA : -0.001

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	5	THR	0	0.049	0.041	2.751	-3.939	-0.261	0.494	-1.925	-2.247	-0.008
4	A	6	PRO	0	0.001	-0.031	4.782	0.415	0.545	-0.001	-0.006	-0.122	0.000
5	A	7	MET	0	-0.079	-0.026	7.549	0.294	0.294	0.000	0.000	0.000	0.000
6	A	8	GLN	0	-0.007	-0.015	10.145	0.299	0.299	0.000	0.000	0.000	0.000
7	A	9	THR	0	-0.002	0.029	10.857	0.141	0.141	0.000	0.000	0.000	0.000
8	A	10	VAL	0	0.048	0.004	12.735	-0.090	-0.090	0.000	0.000	0.000	0.000
9	A	11	ASP	-1	-0.865	-0.937	10.643	-0.897	-0.897	0.000	0.000	0.000	0.000
10	A	12	ASP	-1	-0.782	-0.903	8.079	-2.183	-2.183	0.000	0.000	0.000	0.000
11	A	13	LEU	0	-0.047	-0.013	9.589	-0.155	-0.155	0.000	0.000	0.000	0.000
12	A	14	ARG	1	0.885	0.926	12.502	0.646	0.646	0.000	0.000	0.000	0.000
13	A	15	SER	0	-0.032	-0.015	7.737	-0.194	-0.194	0.000	0.000	0.000	0.000
14	A	16	VAL	0	0.004	0.011	8.138	0.006	0.006	0.000	0.000	0.000	0.000
15	A	17	CYS	0	-0.079	-0.067	9.778	0.194	0.194	0.000	0.000	0.000	0.000
16	A	18	ASP	-1	-0.894	-0.935	11.676	-0.598	-0.598	0.000	0.000	0.000	0.000
17	A	19	GLU	-1	-0.933	-0.962	7.094	-1.286	-1.286	0.000	0.000	0.000	0.000
18	A	20	LEU	0	-0.120	-0.045	11.948	0.136	0.136	0.000	0.000	0.000	0.000
19	A	21	PRO	0	0.005	0.000	14.778	0.020	0.020	0.000	0.000	0.000	0.000
20	A	22	HIS	0	-0.006	-0.015	17.999	-0.014	-0.014	0.000	0.000	0.000	0.000
21	A	23	SER	0	0.058	0.051	17.263	0.013	0.013	0.000	0.000	0.000	0.000
22	A	24	LEU	0	-0.033	-0.020	19.383	0.012	0.012	0.000	0.000	0.000	0.000
23	A	25	GLU	-1	-0.790	-0.883	17.378	-0.541	-0.541	0.000	0.000	0.000	0.000
24	A	26	THR	0	-0.071	-0.042	21.578	0.043	0.043	0.000	0.000	0.000	0.000
25	A	27	PHE	0	0.083	0.036	22.446	-0.029	-0.029	0.000	0.000	0.000	0.000
26	A	28	PRO	0	-0.099	-0.041	26.883	0.017	0.017	0.000	0.000	0.000	0.000
27	A	29	PHE	0	-0.060	-0.030	27.696	0.015	0.015	0.000	0.000	0.000	0.000
28	A	30	ASP	-1	-0.873	-0.941	31.320	-0.165	-0.165	0.000	0.000	0.000	0.000
29	A	31	ASP	-1	-0.883	-0.904	29.075	-0.246	-0.246	0.000	0.000	0.000	0.000
30	A	32	GLU	-1	-0.914	-0.955	25.289	-0.257	-0.257	0.000	0.000	0.000	0.000
31	A	33	THR	0	-0.055	-0.067	24.413	-0.040	-0.040	0.000	0.000	0.000	0.000
32	A	34	LEU	0	-0.030	0.005	18.440	0.016	0.016	0.000	0.000	0.000	0.000
33	A	35	VAL	0	-0.082	-0.057	22.322	-0.010	-0.010	0.000	0.000	0.000	0.000
34	A	36	PHE	0	0.062	0.039	16.613	0.015	0.015	0.000	0.000	0.000	0.000
35	A	37	LYS	1	0.914	0.944	20.705	0.251	0.251	0.000	0.000	0.000	0.000
36	A	38	VAL	0	0.046	0.034	20.756	-0.013	-0.013	0.000	0.000	0.000	0.000
37	A	39	GLY	0	-0.013	-0.017	22.558	0.022	0.022	0.000	0.000	0.000	0.000
38	A	40	TYR	0	-0.006	-0.018	25.244	-0.008	-0.008	0.000	0.000	0.000	0.000
39	A	41	LEU	0	0.056	0.014	26.539	-0.008	-0.008	0.000	0.000	0.000	0.000
40	A	42	SER	0	-0.038	-0.011	28.931	-0.003	-0.003	0.000	0.000	0.000	0.000
41	A	43	LYS	1	0.763	0.854	30.113	0.123	0.123	0.000	0.000	0.000	0.000
42	A	44	SER	0	0.038	0.043	25.609	-0.003	-0.003	0.000	0.000	0.000	0.000
43	A	45	ARG	1	0.842	0.907	25.813	0.165	0.165	0.000	0.000	0.000	0.000
44	A	46	MET	0	0.002	0.006	23.997	-0.005	-0.005	0.000	0.000	0.000	0.000
45	A	47	TYR	0	-0.004	-0.035	16.547	0.019	0.019	0.000	0.000	0.000	0.000
46	A	48	ALA	0	0.034	0.053	18.490	-0.018	-0.018	0.000	0.000	0.000	0.000
47	A	49	LEU	0	-0.034	-0.015	20.381	0.023	0.023	0.000	0.000	0.000	0.000
48	A	50	THR	0	-0.025	-0.032	18.314	-0.029	-0.029	0.000	0.000	0.000	0.000
49	A	51	ASP	-1	-0.813	-0.906	21.486	-0.300	-0.300	0.000	0.000	0.000	0.000
50	A	52	ILE	0	-0.027	-0.030	19.864	-0.024	-0.024	0.000	0.000	0.000	0.000
51	A	53	THR	0	-0.015	0.001	21.665	-0.007	-0.007	0.000	0.000	0.000	0.000
52	A	54	GLN	0	-0.099	-0.037	23.018	0.008	0.008	0.000	0.000	0.000	0.000
53	A	55	ASP	-1	-0.913	-0.931	19.451	-0.487	-0.487	0.000	0.000	0.000	0.000
54	A	56	PRO	0	-0.002	-0.011	18.777	0.037	0.037	0.000	0.000	0.000	0.000
55	A	57	LEU	0	0.032	0.014	15.808	0.027	0.027	0.000	0.000	0.000	0.000
56	A	58	ARG	1	0.930	0.964	19.337	0.328	0.328	0.000	0.000	0.000	0.000
57	A	59	LEU	0	0.033	0.046	15.789	0.011	0.011	0.000	0.000	0.000	0.000
58	A	60	SER	0	-0.020	0.022	19.742	0.032	0.032	0.000	0.000	0.000	0.000
59	A	61	LEU	0	0.036	0.015	17.603	-0.015	-0.015	0.000	0.000	0.000	0.000
60	A	62	LYS	1	0.885	0.940	21.403	0.246	0.246	0.000	0.000	0.000	0.000
61	A	63	VAL	0	0.009	-0.002	21.104	-0.023	-0.023	0.000	0.000	0.000	0.000
62	A	64	ASP	-1	-0.863	-0.950	23.426	-0.116	-0.116	0.000	0.000	0.000	0.000
63	A	65	PRO	0	-0.044	-0.034	25.805	-0.005	-0.005	0.000	0.000	0.000	0.000
64	A	66	GLU	-1	-0.919	-0.937	27.737	-0.088	-0.088	0.000	0.000	0.000	0.000
65	A	67	ARG	1	0.887	0.917	17.029	0.234	0.234	0.000	0.000	0.000	0.000
66	A	68	GLY	0	-0.032	-0.024	24.223	-0.016	-0.016	0.000	0.000	0.000	0.000
67	A	69	GLU	-1	-1.001	-0.996	25.403	-0.137	-0.137	0.000	0.000	0.000	0.000
68	A	70	GLU	-1	-0.845	-0.920	24.308	-0.122	-0.122	0.000	0.000	0.000	0.000
69	A	71	LEU	0	-0.066	-0.036	19.669	-0.009	-0.009	0.000	0.000	0.000	0.000
70	A	72	ARG	1	0.899	0.940	23.313	0.166	0.166	0.000	0.000	0.000	0.000
71	A	73	GLN	0	-0.019	-0.001	25.990	0.005	0.005	0.000	0.000	0.000	0.000
72	A	74	ALA	0	-0.026	-0.017	22.382	0.007	0.007	0.000	0.000	0.000	0.000
73	A	75	HIS	0	-0.010	-0.001	18.503	-0.013	-0.013	0.000	0.000	0.000	0.000
74	A	76	PRO	0	0.032	0.022	23.093	-0.018	-0.018	0.000	0.000	0.000	0.000
75	A	77	GLN	0	-0.065	-0.045	24.754	0.003	0.003	0.000	0.000	0.000	0.000
76	A	78	SER	0	0.000	-0.018	20.094	0.006	0.006	0.000	0.000	0.000	0.000
77	A	79	ILE	0	-0.035	-0.011	19.836	-0.036	-0.036	0.000	0.000	0.000	0.000
78	A	80	ALA	0	0.025	0.031	23.457	0.029	0.029	0.000	0.000	0.000	0.000
79	A	81	PRO	0	-0.017	-0.032	26.318	-0.011	-0.011	0.000	0.000	0.000	0.000
80	A	82	GLY	0	0.041	0.022	27.043	-0.007	-0.007	0.000	0.000	0.000	0.000
81	A	83	TYR	0	0.005	0.020	27.433	0.030	0.030	0.000	0.000	0.000	0.000
82	A	84	HIS	0	0.018	0.010	29.243	-0.008	-0.008	0.000	0.000	0.000	0.000
83	A	85	LEU	0	0.012	0.025	26.363	0.002	0.002	0.000	0.000	0.000	0.000
84	A	86	ASN	0	-0.006	-0.018	30.656	0.015	0.015	0.000	0.000	0.000	0.000
85	A	87	LYS	1	0.919	0.929	30.134	0.178	0.178	0.000	0.000	0.000	0.000
86	A	88	LYS	1	0.908	0.962	30.756	0.129	0.129	0.000	0.000	0.000	0.000
87	A	89	HIS	0	-0.036	-0.031	27.943	-0.001	-0.001	0.000	0.000	0.000	0.000
88	A	90	TRP	0	-0.010	0.021	22.959	-0.006	-0.006	0.000	0.000	0.000	0.000
89	A	91	VAL	0	0.037	0.023	22.164	0.025	0.025	0.000	0.000	0.000	0.000
90	A	92	THR	0	-0.024	-0.055	22.926	-0.009	-0.009	0.000	0.000	0.000	0.000
91	A	93	VAL	0	0.028	0.003	17.776	0.033	0.033	0.000	0.000	0.000	0.000
92	A	94	THR	0	-0.022	-0.008	19.544	-0.021	-0.021	0.000	0.000	0.000	0.000
93	A	95	LEU	0	-0.043	-0.021	14.326	-0.005	-0.005	0.000	0.000	0.000	0.000
94	A	96	ASP	-1	-0.765	-0.836	15.908	-0.454	-0.454	0.000	0.000	0.000	0.000
95	A	97	GLY	0	-0.012	0.000	13.415	0.017	0.017	0.000	0.000	0.000	0.000
96	A	98	THR	0	-0.088	-0.069	14.407	0.036	0.036	0.000	0.000	0.000	0.000
97	A	99	VAL	0	-0.003	0.005	15.240	0.054	0.054	0.000	0.000	0.000	0.000
98	A	100	PRO	0	-0.010	-0.015	12.228	-0.092	-0.092	0.000	0.000	0.000	0.000
99	A	101	ALA	0	0.070	0.032	8.157	0.027	0.027	0.000	0.000	0.000	0.000
100	A	102	GLU	-1	-0.862	-0.922	8.093	-0.197	-0.197	0.000	0.000	0.000	0.000
101	A	103	LEU	0	-0.019	-0.002	9.378	0.037	0.037	0.000	0.000	0.000	0.000
102	A	104	LEU	0	0.016	-0.001	12.141	0.033	0.033	0.000	0.000	0.000	0.000
103	A	105	GLY	0	0.063	0.035	9.731	0.005	0.005	0.000	0.000	0.000	0.000
104	A	106	GLU	-1	-0.832	-0.895	10.793	-0.210	-0.210	0.000	0.000	0.000	0.000
105	A	107	LEU	0	-0.014	-0.002	12.687	0.086	0.086	0.000	0.000	0.000	0.000
106	A	108	LEU	0	-0.013	0.004	12.241	0.090	0.090	0.000	0.000	0.000	0.000
107	A	109	ARG	1	0.861	0.910	9.336	0.771	0.771	0.000	0.000	0.000	0.000
108	A	110	GLY	0	0.031	0.014	14.436	0.080	0.080	0.000	0.000	0.000	0.000
109	A	111	SER	0	-0.045	-0.047	17.618	0.073	0.073	0.000	0.000	0.000	0.000
110	A	112	TYR	0	0.027	-0.018	16.826	0.055	0.055	0.000	0.000	0.000	0.000
111	A	113	LEU	0	0.010	0.006	16.796	0.048	0.048	0.000	0.000	0.000	0.000
112	A	114	LEU	0	-0.020	0.022	19.977	0.041	0.041	0.000	0.000	0.000	0.000
113	A	115	VAL	0	-0.012	-0.018	22.363	0.033	0.033	0.000	0.000	0.000	0.000
114	A	116	THR	0	-0.048	-0.020	20.912	0.030	0.030	0.000	0.000	0.000	0.000
115	A	117	LYS	1	0.859	0.934	22.419	0.132	0.132	0.000	0.000	0.000	0.000
116	A	118	LYS	1	0.910	0.955	26.004	0.126	0.126	0.000	0.000	0.000	0.000
117	A	119	GLY	0	-0.054	-0.031	27.353	0.010	0.010	0.000	0.000	0.000	0.000
118	A	120	PHE	0	-0.019	-0.002	25.856	0.003	0.003	0.000	0.000	0.000	0.000
119	A	121	THR	0	-0.013	-0.014	29.265	0.008	0.008	0.000	0.000	0.000	0.000
120	A	122	LYS	1	0.998	0.983	29.538	0.025	0.025	0.000	0.000	0.000	0.000
121	A	123	ALA	0	-0.012	-0.012	29.938	0.003	0.003	0.000	0.000	0.000	0.000
122	A	124	GLU	-1	-0.679	-0.813	29.306	-0.104	-0.104	0.000	0.000	0.000	0.000
123	A	125	ARG	1	0.889	0.958	24.714	0.093	0.093	0.000	0.000	0.000	0.000
124	A	126	LYS	1	0.929	0.976	25.861	0.017	0.017	0.000	0.000	0.000	0.000
125	A	127	GLU	-1	-0.918	-0.928	27.802	-0.071	-0.071	0.000	0.000	0.000	0.000
126	A	128	LEU	0	0.003	0.010	24.825	0.002	0.002	0.000	0.000	0.000	0.000
127	A	129	GLY	0	0.026	0.026	23.832	-0.003	-0.003	0.000	0.000	0.000	0.000
128	A	130	LEU	0	-0.075	-0.048	21.467	-0.012	-0.012	0.000	0.000	0.000	0.000
129	A	131	PRO	0	0.013	0.014	17.519	0.023	0.023	0.000	0.000	0.000	0.000
130	A	132	ASP	-1	-0.964	-0.993	20.566	-0.060	-0.060	0.000	0.000	0.000	0.000
131	A	133	SER	0	-0.005	-0.009	17.516	-0.006	-0.006	0.000	0.000	0.000	0.000
132	A	134	LEU	0	0.010	-0.010	13.000	0.005	0.005	0.000	0.000	0.000	0.000
133	A	135	GLU	-1	-0.887	-0.934	11.813	0.275	0.275	0.000	0.000	0.000	0.000
134	A	136	GLY	0	0.040	0.030	8.251	-0.148	-0.148	0.000	0.000	0.000	0.000
135	A	137	GLY	0	-0.016	0.004	7.519	-0.298	-0.298	0.000	0.000	0.000	0.000
136	A	138	SER	0	0.036	0.007	4.007	0.530	0.629	-0.001	-0.007	-0.091	0.000
137	A	139	HIS	0	-0.002	0.002	6.858	-0.328	-0.328	0.000	0.000	0.000	0.000
138	A	140	HIS	1	0.851	0.929	8.550	-0.186	-0.186	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:3:LEU)