FMO DATABASE

FMODB ID: 6N6VZ

Calculation Name: 3MTQ-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3MTQ

Chain ID: A

ChEMBL ID:

UniProt ID: A6THW4

Base Structure: X-ray

Registration Date: 2023-06-21

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	140
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1210587.597241
FMO2-HF: Nuclear repulsion	1155992.886671
FMO2-HF: Total energy	-54594.710571
FMO2-MP2: Total energy	-54754.63103

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:ASN)

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

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.
-2.541	2.701	0.425	-2.303	-3.363	-0.003

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.028 / q_NPA : -0.044

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	TYR	0	-0.006	0.015	3.194	-2.973	-0.086	0.016	-1.406	-1.497	0.003
4	A	-2	PHE	0	-0.042	-0.018	2.686	2.603	4.923	0.410	-0.895	-1.834	-0.006
5	A	-1	GLN	0	0.005	0.012	4.987	-0.268	-0.233	-0.001	-0.002	-0.032	0.000
6	A	0	GLY	0	0.005	0.000	8.178	-0.357	-0.357	0.000	0.000	0.000	0.000
7	A	1	MET	0	0.026	0.016	9.604	0.001	0.001	0.000	0.000	0.000	0.000
8	A	2	LYS	1	0.858	0.941	6.607	1.741	1.741	0.000	0.000	0.000	0.000
9	A	3	ARG	1	0.810	0.901	9.593	0.578	0.578	0.000	0.000	0.000	0.000
10	A	4	HIS	0	-0.093	-0.049	7.939	0.002	0.002	0.000	0.000	0.000	0.000
11	A	5	TYR	0	0.031	0.010	13.067	0.124	0.124	0.000	0.000	0.000	0.000
12	A	6	ILE	0	0.006	0.011	16.502	-0.019	-0.019	0.000	0.000	0.000	0.000
13	A	7	PHE	0	-0.014	0.005	18.783	0.030	0.030	0.000	0.000	0.000	0.000
14	A	8	ALA	0	0.011	-0.004	22.245	-0.001	-0.001	0.000	0.000	0.000	0.000
15	A	9	SER	0	-0.012	-0.011	24.441	0.006	0.006	0.000	0.000	0.000	0.000
16	A	10	HIS	0	-0.034	-0.039	28.023	0.007	0.007	0.000	0.000	0.000	0.000
17	A	11	GLY	0	0.012	0.013	30.845	-0.001	-0.001	0.000	0.000	0.000	0.000
18	A	12	SER	0	0.015	-0.022	28.665	-0.009	-0.009	0.000	0.000	0.000	0.000
19	A	13	PHE	0	-0.011	-0.001	28.689	-0.014	-0.014	0.000	0.000	0.000	0.000
20	A	14	ALA	0	0.062	0.021	24.045	-0.008	-0.008	0.000	0.000	0.000	0.000
21	A	15	ASN	0	0.071	0.023	23.659	-0.038	-0.038	0.000	0.000	0.000	0.000
22	A	16	GLY	0	-0.015	0.005	25.553	-0.010	-0.010	0.000	0.000	0.000	0.000
23	A	17	LEU	0	-0.020	-0.015	25.928	0.001	0.001	0.000	0.000	0.000	0.000
24	A	18	LEU	0	0.043	0.012	19.961	0.000	0.000	0.000	0.000	0.000	0.000
25	A	19	ASN	0	0.020	0.011	23.891	-0.026	-0.026	0.000	0.000	0.000	0.000
26	A	20	SER	0	-0.044	-0.023	26.258	0.004	0.004	0.000	0.000	0.000	0.000
27	A	21	VAL	0	0.019	0.005	22.081	0.005	0.005	0.000	0.000	0.000	0.000
28	A	22	GLU	-1	-0.874	-0.923	20.175	-0.445	-0.445	0.000	0.000	0.000	0.000
29	A	23	LEU	0	-0.093	-0.034	23.884	-0.001	-0.001	0.000	0.000	0.000	0.000
30	A	24	ILE	0	-0.057	-0.022	26.749	0.012	0.012	0.000	0.000	0.000	0.000
31	A	25	LEU	0	-0.032	-0.023	22.534	0.006	0.006	0.000	0.000	0.000	0.000
32	A	26	GLY	0	0.004	0.018	21.955	-0.032	-0.032	0.000	0.000	0.000	0.000
33	A	27	LYS	1	0.916	0.933	18.294	0.405	0.405	0.000	0.000	0.000	0.000
34	A	28	GLN	0	-0.005	-0.010	17.121	-0.074	-0.074	0.000	0.000	0.000	0.000
35	A	29	PRO	0	-0.034	-0.004	12.214	0.022	0.022	0.000	0.000	0.000	0.000
36	A	30	ASP	-1	-0.845	-0.924	10.417	-1.370	-1.370	0.000	0.000	0.000	0.000
37	A	31	ILE	0	-0.015	-0.005	13.173	0.048	0.048	0.000	0.000	0.000	0.000
38	A	32	HIS	0	-0.008	0.002	12.052	0.080	0.080	0.000	0.000	0.000	0.000
39	A	33	THR	0	-0.024	-0.031	17.187	0.026	0.026	0.000	0.000	0.000	0.000
40	A	34	LEU	0	-0.023	-0.005	20.770	0.004	0.004	0.000	0.000	0.000	0.000
41	A	35	CYS	0	-0.063	-0.024	22.773	0.008	0.008	0.000	0.000	0.000	0.000
42	A	36	ALA	0	0.051	0.027	26.309	0.006	0.006	0.000	0.000	0.000	0.000
43	A	37	TYR	0	0.009	-0.013	28.706	0.000	0.000	0.000	0.000	0.000	0.000
44	A	38	VAL	0	-0.029	-0.005	28.256	0.003	0.003	0.000	0.000	0.000	0.000
45	A	39	GLU	-1	-0.977	-0.995	27.835	-0.153	-0.153	0.000	0.000	0.000	0.000
46	A	40	GLU	-1	-0.968	-0.969	31.830	-0.084	-0.084	0.000	0.000	0.000	0.000
47	A	41	GLU	-1	-0.969	-0.987	31.296	-0.095	-0.095	0.000	0.000	0.000	0.000
48	A	42	VAL	0	-0.043	-0.011	26.102	0.006	0.006	0.000	0.000	0.000	0.000
49	A	43	ASP	-1	-0.858	-0.938	28.851	-0.089	-0.089	0.000	0.000	0.000	0.000
50	A	44	LEU	0	-0.015	-0.012	26.882	-0.007	-0.007	0.000	0.000	0.000	0.000
51	A	45	THR	0	0.013	-0.007	26.198	-0.008	-0.008	0.000	0.000	0.000	0.000
52	A	46	GLN	0	-0.002	0.007	23.708	-0.007	-0.007	0.000	0.000	0.000	0.000
53	A	47	GLN	0	0.010	0.009	22.996	-0.001	-0.001	0.000	0.000	0.000	0.000
54	A	48	VAL	0	-0.024	-0.027	21.638	-0.020	-0.020	0.000	0.000	0.000	0.000
55	A	49	GLU	-1	-0.967	-0.994	20.602	-0.098	-0.098	0.000	0.000	0.000	0.000
56	A	50	ALA	0	-0.016	0.006	19.232	-0.006	-0.006	0.000	0.000	0.000	0.000
57	A	51	LEU	0	-0.021	-0.012	15.977	-0.019	-0.019	0.000	0.000	0.000	0.000
58	A	52	VAL	0	-0.015	-0.014	15.585	-0.047	-0.047	0.000	0.000	0.000	0.000
59	A	53	ALA	0	-0.028	-0.013	15.040	-0.036	-0.036	0.000	0.000	0.000	0.000
60	A	54	ARG	1	0.893	0.959	10.785	0.478	0.478	0.000	0.000	0.000	0.000
61	A	55	PHE	0	-0.038	-0.001	10.318	-0.037	-0.037	0.000	0.000	0.000	0.000
62	A	56	PRO	0	0.016	0.017	6.803	0.206	0.206	0.000	0.000	0.000	0.000
63	A	57	ALA	0	0.025	0.012	10.148	-0.044	-0.044	0.000	0.000	0.000	0.000
64	A	58	GLN	0	0.006	0.009	9.645	0.085	0.085	0.000	0.000	0.000	0.000
65	A	59	ASP	-1	-0.855	-0.920	7.599	-1.859	-1.859	0.000	0.000	0.000	0.000
66	A	60	GLU	-1	-0.774	-0.823	10.674	-0.228	-0.228	0.000	0.000	0.000	0.000
67	A	61	LEU	0	-0.041	-0.017	13.191	-0.102	-0.102	0.000	0.000	0.000	0.000
68	A	62	ILE	0	0.012	0.002	15.478	0.074	0.074	0.000	0.000	0.000	0.000
69	A	63	VAL	0	0.007	0.002	18.575	-0.023	-0.023	0.000	0.000	0.000	0.000
70	A	64	ILE	0	0.003	0.006	20.857	0.028	0.028	0.000	0.000	0.000	0.000
71	A	65	THR	0	0.022	-0.010	23.905	-0.005	-0.005	0.000	0.000	0.000	0.000
72	A	66	ASP	-1	-0.772	-0.861	26.573	-0.147	-0.147	0.000	0.000	0.000	0.000
73	A	67	ILE	0	-0.039	-0.024	29.770	0.006	0.006	0.000	0.000	0.000	0.000
74	A	68	PHE	0	0.053	0.022	31.613	0.002	0.002	0.000	0.000	0.000	0.000
75	A	69	ALA	0	-0.036	-0.020	32.952	0.005	0.005	0.000	0.000	0.000	0.000
76	A	70	GLY	0	0.025	0.022	33.663	0.006	0.006	0.000	0.000	0.000	0.000
77	A	71	SER	0	0.020	-0.014	32.415	0.000	0.000	0.000	0.000	0.000	0.000
78	A	72	VAL	0	0.056	0.034	26.738	0.000	0.000	0.000	0.000	0.000	0.000
79	A	73	ASN	0	0.023	0.025	27.658	-0.016	-0.016	0.000	0.000	0.000	0.000
80	A	74	ASN	0	-0.018	-0.022	28.181	-0.002	-0.002	0.000	0.000	0.000	0.000
81	A	75	GLU	-1	-0.853	-0.921	26.767	-0.094	-0.094	0.000	0.000	0.000	0.000
82	A	76	PHE	0	0.007	-0.014	20.756	-0.004	-0.004	0.000	0.000	0.000	0.000
83	A	77	VAL	0	-0.014	-0.003	24.693	-0.002	-0.002	0.000	0.000	0.000	0.000
84	A	78	ARG	1	0.948	0.987	24.487	0.085	0.085	0.000	0.000	0.000	0.000
85	A	79	PHE	0	-0.001	-0.017	20.612	0.009	0.009	0.000	0.000	0.000	0.000
86	A	80	LEU	0	-0.006	0.006	21.947	-0.011	-0.011	0.000	0.000	0.000	0.000
87	A	81	SER	0	-0.032	-0.005	23.807	0.010	0.010	0.000	0.000	0.000	0.000
88	A	82	ARG	1	0.840	0.916	13.710	0.295	0.295	0.000	0.000	0.000	0.000
89	A	83	PRO	0	0.008	0.009	16.389	0.002	0.002	0.000	0.000	0.000	0.000
90	A	84	HIS	0	-0.040	-0.043	14.252	0.011	0.011	0.000	0.000	0.000	0.000
91	A	85	PHE	0	0.019	0.018	16.849	-0.061	-0.061	0.000	0.000	0.000	0.000
92	A	86	HIS	0	0.016	0.006	18.499	0.029	0.029	0.000	0.000	0.000	0.000
93	A	87	LEU	0	-0.019	0.001	21.153	-0.023	-0.023	0.000	0.000	0.000	0.000
94	A	88	LEU	0	-0.007	-0.006	23.072	0.019	0.019	0.000	0.000	0.000	0.000
95	A	89	SER	0	-0.023	-0.030	26.048	-0.002	-0.002	0.000	0.000	0.000	0.000
96	A	90	GLY	0	-0.017	0.005	28.963	0.009	0.009	0.000	0.000	0.000	0.000
97	A	91	LEU	0	-0.043	-0.018	24.525	-0.003	-0.003	0.000	0.000	0.000	0.000
98	A	92	ASN	0	-0.008	-0.016	28.059	0.010	0.010	0.000	0.000	0.000	0.000
99	A	93	LEU	0	0.049	0.019	27.311	-0.013	-0.013	0.000	0.000	0.000	0.000
100	A	94	PRO	0	0.025	0.021	27.992	-0.014	-0.014	0.000	0.000	0.000	0.000
101	A	95	LEU	0	0.033	0.003	25.746	-0.007	-0.007	0.000	0.000	0.000	0.000
102	A	96	ILE	0	-0.014	-0.002	22.306	-0.014	-0.014	0.000	0.000	0.000	0.000
103	A	97	ILE	0	0.006	-0.002	23.489	-0.025	-0.025	0.000	0.000	0.000	0.000
104	A	98	ASP	-1	-0.835	-0.923	24.925	-0.208	-0.208	0.000	0.000	0.000	0.000
105	A	99	LEU	0	-0.017	-0.018	21.332	-0.006	-0.006	0.000	0.000	0.000	0.000
106	A	100	LEU	0	-0.046	-0.020	18.606	-0.024	-0.024	0.000	0.000	0.000	0.000
107	A	101	ILE	0	-0.019	-0.007	20.728	-0.025	-0.025	0.000	0.000	0.000	0.000
108	A	102	SER	0	-0.016	-0.002	22.846	0.002	0.002	0.000	0.000	0.000	0.000
109	A	103	ALA	0	0.026	0.016	17.310	0.002	0.002	0.000	0.000	0.000	0.000
110	A	104	ALA	0	-0.080	-0.048	17.363	-0.047	-0.047	0.000	0.000	0.000	0.000
111	A	105	GLU	-1	-0.852	-0.909	18.747	-0.135	-0.135	0.000	0.000	0.000	0.000
112	A	106	ASP	-1	-0.904	-0.958	18.114	-0.169	-0.169	0.000	0.000	0.000	0.000
113	A	107	ASN	0	-0.010	0.002	19.145	0.002	0.002	0.000	0.000	0.000	0.000
114	A	108	THR	0	-0.004	-0.081	18.101	-0.003	-0.003	0.000	0.000	0.000	0.000
115	A	109	GLU	-1	-0.925	-0.957	21.123	-0.091	-0.091	0.000	0.000	0.000	0.000
116	A	110	LYS	1	0.813	0.945	24.687	0.141	0.141	0.000	0.000	0.000	0.000
117	A	111	LEU	0	0.024	0.019	19.878	0.002	0.002	0.000	0.000	0.000	0.000
118	A	112	ILE	0	-0.005	-0.005	21.193	0.000	0.000	0.000	0.000	0.000	0.000
119	A	113	THR	0	-0.052	-0.051	24.922	0.009	0.009	0.000	0.000	0.000	0.000
120	A	114	GLU	-1	-0.875	-0.943	27.667	-0.127	-0.127	0.000	0.000	0.000	0.000
121	A	115	ALA	0	0.051	0.042	25.644	0.004	0.004	0.000	0.000	0.000	0.000
122	A	116	LEU	0	-0.103	-0.063	27.750	0.007	0.007	0.000	0.000	0.000	0.000
123	A	117	THR	0	-0.094	-0.043	29.878	0.011	0.011	0.000	0.000	0.000	0.000
124	A	118	ASN	0	0.029	0.019	30.553	0.016	0.016	0.000	0.000	0.000	0.000
125	A	119	ALA	0	-0.027	-0.016	29.922	0.002	0.002	0.000	0.000	0.000	0.000
126	A	120	LYS	1	0.895	0.924	31.989	0.119	0.119	0.000	0.000	0.000	0.000
127	A	121	GLU	-1	-0.940	-0.955	35.062	-0.103	-0.103	0.000	0.000	0.000	0.000
128	A	122	SER	0	-0.013	-0.007	34.194	0.002	0.002	0.000	0.000	0.000	0.000
129	A	123	ILE	0	-0.090	-0.020	33.468	0.000	0.000	0.000	0.000	0.000	0.000
130	A	124	GLN	0	0.042	0.048	37.409	0.014	0.014	0.000	0.000	0.000	0.000
131	A	125	TYR	0	0.013	0.004	41.131	-0.001	-0.001	0.000	0.000	0.000	0.000
132	A	126	CYS	0	0.063	0.011	42.611	0.003	0.003	0.000	0.000	0.000	0.000
133	A	127	ASN	0	-0.044	-0.008	45.093	-0.001	-0.001	0.000	0.000	0.000	0.000
134	A	128	GLN	0	-0.020	-0.015	47.720	0.002	0.002	0.000	0.000	0.000	0.000
135	A	129	THR	0	0.018	-0.031	43.260	0.004	0.004	0.000	0.000	0.000	0.000
136	A	130	ILE	0	0.014	0.007	44.014	0.001	0.001	0.000	0.000	0.000	0.000
137	A	131	ALA	0	-0.022	-0.014	47.274	0.002	0.002	0.000	0.000	0.000	0.000
138	A	132	SER	0	-0.051	-0.023	48.662	0.004	0.004	0.000	0.000	0.000	0.000
139	A	133	ALA	0	-0.026	0.003	46.653	0.002	0.002	0.000	0.000	0.000	0.000
140	A	134	MET	0	-0.068	-0.019	48.189	0.003	0.003	0.000	0.000	0.000	0.000

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