FMO DATABASE

FMODB ID: VRY91

Calculation Name: 3MTI-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3MTI

Chain ID: A

ChEMBL ID:

UniProt ID: Q5M2Z6

Base Structure: X-ray

Registration Date: 2023-03-14

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	172
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1795395.885126
FMO2-HF: Nuclear repulsion	1727355.035931
FMO2-HF: Total energy	-68040.849195
FMO2-MP2: Total energy	-68238.081848

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:0:ALA)

Summations of interaction energy for fragment #1(A:0:ALA)

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.
0.644	1.995	-0.009	-0.597	-0.744	0.003

Interaction energy analysis for fragmet #1(A:0:ALA)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.018 / q_NPA : -0.006

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	2	ILE	0	0.049	0.021	3.850	-0.517	0.679	-0.007	-0.589	-0.600	0.003
4	A	3	LYS	1	0.864	0.931	4.659	-1.727	-1.647	-0.001	-0.005	-0.073	0.000
5	A	4	ARG	1	1.002	1.007	7.755	-1.210	-1.210	0.000	0.000	0.000	0.000
6	A	5	PRO	0	0.071	0.030	10.878	0.143	0.143	0.000	0.000	0.000	0.000
7	A	6	ILE	0	0.069	0.043	12.427	0.040	0.040	0.000	0.000	0.000	0.000
8	A	7	HIS	0	-0.067	-0.031	5.359	1.604	1.679	-0.001	-0.003	-0.071	0.000
9	A	8	MET	0	0.008	0.012	9.686	0.116	0.116	0.000	0.000	0.000	0.000
10	A	9	SER	0	-0.007	-0.010	10.548	-0.074	-0.074	0.000	0.000	0.000	0.000
11	A	10	HIS	1	0.797	0.886	11.538	-0.701	-0.701	0.000	0.000	0.000	0.000
12	A	11	ASP	-1	-0.782	-0.896	7.024	1.767	1.767	0.000	0.000	0.000	0.000
13	A	12	PHE	0	-0.016	-0.007	10.687	-0.103	-0.103	0.000	0.000	0.000	0.000
14	A	13	LEU	0	0.019	0.015	13.401	-0.055	-0.055	0.000	0.000	0.000	0.000
15	A	14	ALA	0	0.016	-0.007	12.285	-0.039	-0.039	0.000	0.000	0.000	0.000
16	A	15	GLU	-1	-0.928	-0.936	12.703	0.137	0.137	0.000	0.000	0.000	0.000
17	A	16	VAL	0	-0.007	0.005	14.338	-0.042	-0.042	0.000	0.000	0.000	0.000
18	A	17	LEU	0	-0.051	-0.010	16.912	-0.019	-0.019	0.000	0.000	0.000	0.000
19	A	18	ASP	-1	-0.798	-0.867	18.499	0.119	0.119	0.000	0.000	0.000	0.000
20	A	19	ASP	-1	-0.892	-0.959	20.687	0.115	0.115	0.000	0.000	0.000	0.000
21	A	20	GLU	-1	-0.851	-0.917	23.126	0.082	0.082	0.000	0.000	0.000	0.000
22	A	21	SER	0	-0.063	-0.037	22.389	-0.001	-0.001	0.000	0.000	0.000	0.000
23	A	22	ILE	0	0.009	0.005	24.446	0.007	0.007	0.000	0.000	0.000	0.000
24	A	23	VAL	0	0.015	0.000	21.151	0.004	0.004	0.000	0.000	0.000	0.000
25	A	24	VAL	0	-0.011	-0.014	24.228	-0.010	-0.010	0.000	0.000	0.000	0.000
26	A	25	ASP	-1	-0.822	-0.909	23.031	0.249	0.249	0.000	0.000	0.000	0.000
27	A	26	ALA	0	0.021	0.005	24.773	-0.013	-0.013	0.000	0.000	0.000	0.000
28	A	27	THR	0	-0.020	0.006	24.486	-0.013	-0.013	0.000	0.000	0.000	0.000
29	A	28	MET	0	0.025	0.040	24.868	0.017	0.017	0.000	0.000	0.000	0.000
30	A	29	GLY	0	0.045	0.020	24.598	0.020	0.020	0.000	0.000	0.000	0.000
31	A	30	ASN	0	-0.085	-0.062	21.686	0.007	0.007	0.000	0.000	0.000	0.000
32	A	31	GLY	0	0.130	0.077	23.124	0.001	0.001	0.000	0.000	0.000	0.000
33	A	32	ASN	0	-0.054	-0.020	17.870	0.005	0.005	0.000	0.000	0.000	0.000
34	A	33	ASP	-1	-0.785	-0.871	17.698	0.447	0.447	0.000	0.000	0.000	0.000
35	A	34	THR	0	0.033	-0.004	18.927	0.004	0.004	0.000	0.000	0.000	0.000
36	A	35	ALA	0	-0.014	-0.010	19.075	-0.003	-0.003	0.000	0.000	0.000	0.000
37	A	36	PHE	0	-0.070	-0.040	11.262	0.035	0.035	0.000	0.000	0.000	0.000
38	A	37	LEU	0	0.036	0.004	16.522	0.007	0.007	0.000	0.000	0.000	0.000
39	A	38	ALA	0	0.045	0.029	18.215	-0.020	-0.020	0.000	0.000	0.000	0.000
40	A	39	GLY	0	-0.016	-0.004	18.070	-0.018	-0.018	0.000	0.000	0.000	0.000
41	A	40	LEU	0	-0.075	-0.036	13.735	-0.007	-0.007	0.000	0.000	0.000	0.000
42	A	41	SER	0	-0.050	-0.021	18.057	-0.018	-0.018	0.000	0.000	0.000	0.000
43	A	42	LYS	1	0.845	0.921	21.569	-0.100	-0.100	0.000	0.000	0.000	0.000
44	A	43	LYS	1	0.803	0.876	25.145	-0.112	-0.112	0.000	0.000	0.000	0.000
45	A	44	VAL	0	-0.009	0.020	22.347	0.007	0.007	0.000	0.000	0.000	0.000
46	A	45	TYR	0	-0.021	-0.023	25.483	-0.010	-0.010	0.000	0.000	0.000	0.000
47	A	46	ALA	0	0.006	-0.001	26.134	0.011	0.011	0.000	0.000	0.000	0.000
48	A	47	PHE	0	0.022	0.018	27.777	-0.012	-0.012	0.000	0.000	0.000	0.000
49	A	48	ASP	-1	-0.802	-0.919	29.193	0.152	0.152	0.000	0.000	0.000	0.000
50	A	49	VAL	0	0.022	0.019	31.446	-0.007	-0.007	0.000	0.000	0.000	0.000
51	A	50	GLN	0	-0.093	-0.046	31.235	-0.012	-0.012	0.000	0.000	0.000	0.000
52	A	51	GLU	-1	-0.852	-0.932	33.354	0.100	0.100	0.000	0.000	0.000	0.000
53	A	52	GLN	0	-0.016	-0.020	32.671	0.001	0.001	0.000	0.000	0.000	0.000
54	A	53	ALA	0	-0.019	0.001	29.141	0.006	0.006	0.000	0.000	0.000	0.000
55	A	54	LEU	0	0.084	0.044	29.236	0.012	0.012	0.000	0.000	0.000	0.000
56	A	55	GLY	0	0.015	0.032	30.736	0.004	0.004	0.000	0.000	0.000	0.000
57	A	56	LYS	1	0.804	0.892	25.944	-0.159	-0.159	0.000	0.000	0.000	0.000
58	A	57	THR	0	0.050	0.007	25.086	0.015	0.015	0.000	0.000	0.000	0.000
59	A	58	SER	0	0.012	-0.005	26.661	0.005	0.005	0.000	0.000	0.000	0.000
60	A	59	GLN	0	-0.011	-0.006	26.419	0.006	0.006	0.000	0.000	0.000	0.000
61	A	60	ARG	1	0.787	0.877	19.512	-0.275	-0.275	0.000	0.000	0.000	0.000
62	A	61	LEU	0	0.020	0.008	22.905	0.010	0.010	0.000	0.000	0.000	0.000
63	A	62	SER	0	0.053	0.020	25.109	-0.004	-0.004	0.000	0.000	0.000	0.000
64	A	63	ASP	-1	-0.930	-0.949	25.493	0.134	0.134	0.000	0.000	0.000	0.000
65	A	64	LEU	0	-0.118	-0.057	19.676	0.008	0.008	0.000	0.000	0.000	0.000
66	A	65	GLY	0	-0.021	-0.002	22.968	0.003	0.003	0.000	0.000	0.000	0.000
67	A	66	ILE	0	-0.088	-0.036	20.364	-0.003	-0.003	0.000	0.000	0.000	0.000
68	A	67	GLU	-1	-0.891	-0.961	24.795	0.109	0.109	0.000	0.000	0.000	0.000
69	A	68	ASN	0	-0.103	-0.031	22.972	-0.006	-0.006	0.000	0.000	0.000	0.000
70	A	69	THR	0	-0.009	-0.019	24.812	0.013	0.013	0.000	0.000	0.000	0.000
71	A	70	GLU	-1	-0.869	-0.928	27.602	0.088	0.088	0.000	0.000	0.000	0.000
72	A	71	LEU	0	-0.033	-0.016	27.353	0.007	0.007	0.000	0.000	0.000	0.000
73	A	72	ILE	0	-0.011	-0.005	30.876	-0.009	-0.009	0.000	0.000	0.000	0.000
74	A	73	LEU	0	-0.042	-0.019	32.974	0.005	0.005	0.000	0.000	0.000	0.000
75	A	74	ASP	-1	-0.792	-0.871	34.680	0.074	0.074	0.000	0.000	0.000	0.000
76	A	75	GLY	0	-0.022	-0.007	34.388	0.007	0.007	0.000	0.000	0.000	0.000
77	A	76	HIS	0	-0.033	-0.038	29.919	-0.008	-0.008	0.000	0.000	0.000	0.000
78	A	77	GLU	-1	-0.863	-0.948	32.831	0.090	0.090	0.000	0.000	0.000	0.000
79	A	78	ASN	0	-0.035	-0.011	35.378	-0.008	-0.008	0.000	0.000	0.000	0.000
80	A	79	LEU	0	0.033	0.019	30.573	-0.001	-0.001	0.000	0.000	0.000	0.000
81	A	80	ASP	-1	-0.869	-0.931	34.085	0.072	0.072	0.000	0.000	0.000	0.000
82	A	81	HIS	0	-0.092	-0.058	36.118	-0.006	-0.006	0.000	0.000	0.000	0.000
83	A	82	TYR	0	-0.085	-0.072	34.448	-0.003	-0.003	0.000	0.000	0.000	0.000
84	A	83	VAL	0	-0.023	0.006	30.479	0.001	0.001	0.000	0.000	0.000	0.000
85	A	84	ARG	1	0.815	0.903	33.617	-0.073	-0.073	0.000	0.000	0.000	0.000
86	A	85	GLU	-1	-0.851	-0.891	31.097	0.092	0.092	0.000	0.000	0.000	0.000
87	A	86	PRO	0	0.007	0.001	29.841	0.001	0.001	0.000	0.000	0.000	0.000
88	A	87	ILE	0	0.000	0.004	25.484	0.006	0.006	0.000	0.000	0.000	0.000
89	A	88	ARG	1	0.794	0.889	21.805	-0.128	-0.128	0.000	0.000	0.000	0.000
90	A	89	ALA	0	0.013	-0.004	19.999	0.008	0.008	0.000	0.000	0.000	0.000
91	A	90	ALA	0	0.025	0.014	21.849	-0.007	-0.007	0.000	0.000	0.000	0.000
92	A	91	ILE	0	-0.021	-0.007	17.908	0.021	0.021	0.000	0.000	0.000	0.000
93	A	92	PHE	0	0.041	0.012	21.744	-0.015	-0.015	0.000	0.000	0.000	0.000
94	A	93	ASN	0	-0.054	-0.045	20.659	0.025	0.025	0.000	0.000	0.000	0.000
95	A	94	LEU	0	0.057	0.029	23.691	-0.016	-0.016	0.000	0.000	0.000	0.000
96	A	95	GLY	0	-0.013	-0.011	25.237	0.007	0.007	0.000	0.000	0.000	0.000
97	A	107	LYS	1	0.986	0.984	35.033	-0.077	-0.077	0.000	0.000	0.000	0.000
98	A	108	PRO	0	0.049	0.008	34.278	0.003	0.003	0.000	0.000	0.000	0.000
99	A	109	HIS	0	0.024	0.011	34.977	0.002	0.002	0.000	0.000	0.000	0.000
100	A	110	THR	0	0.030	0.027	35.141	-0.001	-0.001	0.000	0.000	0.000	0.000
101	A	111	THR	0	0.019	0.015	29.822	0.006	0.006	0.000	0.000	0.000	0.000
102	A	112	LEU	0	-0.019	-0.022	31.530	0.005	0.005	0.000	0.000	0.000	0.000
103	A	113	GLU	-1	-0.905	-0.946	33.097	0.071	0.071	0.000	0.000	0.000	0.000
104	A	114	ALA	0	-0.008	-0.007	31.011	0.000	0.000	0.000	0.000	0.000	0.000
105	A	115	ILE	0	-0.008	-0.007	27.529	0.005	0.005	0.000	0.000	0.000	0.000
106	A	116	GLU	-1	-0.842	-0.888	29.726	0.068	0.068	0.000	0.000	0.000	0.000
107	A	117	LYS	1	0.808	0.906	32.379	-0.075	-0.075	0.000	0.000	0.000	0.000
108	A	118	ILE	0	0.034	0.014	26.184	0.000	0.000	0.000	0.000	0.000	0.000
109	A	119	LEU	0	0.014	0.009	26.138	0.001	0.001	0.000	0.000	0.000	0.000
110	A	120	ASP	-1	-0.895	-0.945	29.150	0.067	0.067	0.000	0.000	0.000	0.000
111	A	121	ARG	1	0.795	0.887	31.149	-0.083	-0.083	0.000	0.000	0.000	0.000
112	A	122	LEU	0	-0.055	0.000	24.596	0.002	0.002	0.000	0.000	0.000	0.000
113	A	123	GLU	-1	-0.845	-0.910	26.235	0.095	0.095	0.000	0.000	0.000	0.000
114	A	124	VAL	0	-0.030	-0.027	26.547	0.005	0.005	0.000	0.000	0.000	0.000
115	A	125	GLY	0	-0.021	-0.012	23.274	-0.001	-0.001	0.000	0.000	0.000	0.000
116	A	126	GLY	0	0.009	0.010	21.782	0.014	0.014	0.000	0.000	0.000	0.000
117	A	127	ARG	1	0.688	0.803	14.800	-0.192	-0.192	0.000	0.000	0.000	0.000
118	A	128	LEU	0	0.006	0.012	21.254	0.008	0.008	0.000	0.000	0.000	0.000
119	A	129	ALA	0	-0.025	-0.005	17.666	0.000	0.000	0.000	0.000	0.000	0.000
120	A	130	ILE	0	0.033	0.004	19.543	0.001	0.001	0.000	0.000	0.000	0.000
121	A	131	MET	0	-0.020	0.008	16.768	0.020	0.020	0.000	0.000	0.000	0.000
122	A	132	ILE	0	0.030	0.018	20.353	-0.016	-0.016	0.000	0.000	0.000	0.000
123	A	133	TYR	0	-0.021	-0.024	19.620	0.017	0.017	0.000	0.000	0.000	0.000
124	A	134	TYR	0	-0.053	-0.054	23.892	-0.014	-0.014	0.000	0.000	0.000	0.000
125	A	135	GLY	0	0.061	0.032	25.835	-0.008	-0.008	0.000	0.000	0.000	0.000
126	A	136	HIS	0	-0.040	-0.031	23.494	-0.005	-0.005	0.000	0.000	0.000	0.000
127	A	137	ASP	-1	-0.869	-0.895	28.317	0.070	0.070	0.000	0.000	0.000	0.000
128	A	138	GLY	0	-0.032	-0.012	29.326	-0.007	-0.007	0.000	0.000	0.000	0.000
129	A	139	GLY	0	-0.003	0.010	31.994	-0.005	-0.005	0.000	0.000	0.000	0.000
130	A	140	ASP	-1	-0.866	-0.931	31.267	0.093	0.093	0.000	0.000	0.000	0.000
131	A	141	MET	0	0.039	0.017	32.761	0.000	0.000	0.000	0.000	0.000	0.000
132	A	142	GLU	-1	-0.885	-0.940	30.317	0.110	0.110	0.000	0.000	0.000	0.000
133	A	143	LYS	1	0.775	0.859	27.631	-0.108	-0.108	0.000	0.000	0.000	0.000
134	A	144	ASP	-1	-0.889	-0.937	29.213	0.070	0.070	0.000	0.000	0.000	0.000
135	A	145	ALA	0	0.009	0.014	31.661	-0.002	-0.002	0.000	0.000	0.000	0.000
136	A	146	VAL	0	-0.006	-0.009	27.009	-0.001	-0.001	0.000	0.000	0.000	0.000
137	A	147	LEU	0	-0.007	-0.009	25.089	0.001	0.001	0.000	0.000	0.000	0.000
138	A	148	GLU	-1	-0.949	-0.973	28.566	0.049	0.049	0.000	0.000	0.000	0.000
139	A	149	TYR	0	-0.096	-0.077	29.664	-0.001	-0.001	0.000	0.000	0.000	0.000
140	A	150	VAL	0	-0.012	-0.013	24.896	-0.001	-0.001	0.000	0.000	0.000	0.000
141	A	151	ILE	0	-0.072	-0.034	27.922	-0.005	-0.005	0.000	0.000	0.000	0.000
142	A	152	GLY	0	-0.018	-0.004	29.346	-0.005	-0.005	0.000	0.000	0.000	0.000
143	A	153	LEU	0	-0.053	-0.006	27.368	-0.004	-0.004	0.000	0.000	0.000	0.000
144	A	154	ASP	-1	-0.753	-0.850	30.743	0.031	0.031	0.000	0.000	0.000	0.000
145	A	155	GLN	0	0.036	0.018	28.414	0.003	0.003	0.000	0.000	0.000	0.000
146	A	156	ARG	1	0.760	0.848	28.445	-0.030	-0.030	0.000	0.000	0.000	0.000
147	A	157	VAL	0	-0.022	-0.006	30.101	-0.001	-0.001	0.000	0.000	0.000	0.000
148	A	158	PHE	0	0.064	0.027	26.042	0.006	0.006	0.000	0.000	0.000	0.000
149	A	159	THR	0	-0.007	0.010	21.258	-0.012	-0.012	0.000	0.000	0.000	0.000
150	A	160	ALA	0	0.038	0.008	22.560	0.014	0.014	0.000	0.000	0.000	0.000
151	A	161	MET	0	-0.047	-0.017	18.094	-0.018	-0.018	0.000	0.000	0.000	0.000
152	A	162	LEU	0	0.007	0.014	19.563	0.022	0.022	0.000	0.000	0.000	0.000
153	A	163	TYR	0	-0.039	-0.042	10.313	-0.049	-0.049	0.000	0.000	0.000	0.000
154	A	164	GLN	0	0.024	-0.003	16.421	0.030	0.030	0.000	0.000	0.000	0.000
155	A	165	PRO	0	-0.039	-0.018	15.561	-0.025	-0.025	0.000	0.000	0.000	0.000
156	A	166	LEU	0	0.023	0.015	17.190	-0.008	-0.008	0.000	0.000	0.000	0.000
157	A	167	ASN	0	-0.017	-0.011	17.086	0.004	0.004	0.000	0.000	0.000	0.000
158	A	168	GLN	0	-0.047	-0.014	17.507	-0.018	-0.018	0.000	0.000	0.000	0.000
159	A	169	ILE	0	0.020	0.005	20.504	-0.001	-0.001	0.000	0.000	0.000	0.000
160	A	170	ASN	0	-0.030	-0.012	23.005	0.012	0.012	0.000	0.000	0.000	0.000
161	A	171	THR	0	0.031	-0.013	22.496	0.012	0.012	0.000	0.000	0.000	0.000
162	A	172	PRO	0	-0.049	-0.009	18.663	0.012	0.012	0.000	0.000	0.000	0.000
163	A	173	PRO	0	0.011	-0.012	18.491	-0.010	-0.010	0.000	0.000	0.000	0.000
164	A	174	PHE	0	-0.047	-0.020	17.892	0.015	0.015	0.000	0.000	0.000	0.000
165	A	175	LEU	0	-0.035	-0.015	14.419	0.019	0.019	0.000	0.000	0.000	0.000
166	A	176	VAL	0	0.020	0.015	18.069	-0.025	-0.025	0.000	0.000	0.000	0.000
167	A	177	MET	0	-0.058	-0.018	13.791	0.030	0.030	0.000	0.000	0.000	0.000
168	A	178	LEU	0	0.031	0.009	18.908	-0.026	-0.026	0.000	0.000	0.000	0.000
169	A	179	GLU	-1	-0.819	-0.899	19.338	0.124	0.124	0.000	0.000	0.000	0.000
170	A	180	LYS	1	0.791	0.899	22.347	-0.095	-0.095	0.000	0.000	0.000	0.000
171	A	181	LEU	0	0.000	0.005	24.141	-0.001	-0.001	0.000	0.000	0.000	0.000
172	A	182	GLN	0	-0.080	-0.040	27.019	-0.005	-0.005	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:0:ALA)