FMO DATABASE

FMODB ID: R95G8

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	OptAll
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	-1213227.946234
FMO2-HF: Nuclear repulsion	1158632.295506
FMO2-HF: Total energy	-54595.650728
FMO2-MP2: Total energy	-54755.523217

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.
-13.334	-6.25	1.044	-3.51	-4.616	-0.001

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 : 0.026 / q_NPA : 0.004

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	-0.021	-0.001	2.866	-5.906	-1.382	0.210	-2.131	-2.603	0.013
4	A	-2	PHE	0	-0.041	-0.016	2.668	-6.071	-3.576	0.835	-1.372	-1.957	-0.014
5	A	-1	GLN	0	-0.003	0.005	4.752	0.882	0.947	-0.001	-0.007	-0.056	0.000
6	A	0	GLY	0	0.003	0.000	8.442	-0.136	-0.136	0.000	0.000	0.000	0.000
7	A	1	MET	0	0.008	0.010	9.968	-0.100	-0.100	0.000	0.000	0.000	0.000
8	A	2	LYS	1	0.801	0.900	6.041	1.356	1.356	0.000	0.000	0.000	0.000
9	A	3	ARG	1	0.776	0.862	9.286	0.744	0.744	0.000	0.000	0.000	0.000
10	A	4	HIS	0	-0.070	-0.041	8.518	0.206	0.206	0.000	0.000	0.000	0.000
11	A	5	TYR	0	0.030	0.006	13.212	0.053	0.053	0.000	0.000	0.000	0.000
12	A	6	ILE	0	-0.015	-0.007	16.802	0.020	0.020	0.000	0.000	0.000	0.000
13	A	7	PHE	0	-0.001	0.012	19.267	0.009	0.009	0.000	0.000	0.000	0.000
14	A	8	ALA	0	0.023	0.002	22.685	0.016	0.016	0.000	0.000	0.000	0.000
15	A	9	SER	0	-0.018	-0.024	24.816	-0.005	-0.005	0.000	0.000	0.000	0.000
16	A	10	HIS	0	-0.018	-0.036	28.375	0.014	0.014	0.000	0.000	0.000	0.000
17	A	11	GLY	0	0.032	0.024	31.194	-0.003	-0.003	0.000	0.000	0.000	0.000
18	A	12	SER	0	0.018	-0.021	28.698	-0.008	-0.008	0.000	0.000	0.000	0.000
19	A	13	PHE	0	-0.016	-0.009	28.522	-0.006	-0.006	0.000	0.000	0.000	0.000
20	A	14	ALA	0	0.049	0.024	24.264	-0.006	-0.006	0.000	0.000	0.000	0.000
21	A	15	ASN	0	0.080	0.038	23.331	-0.022	-0.022	0.000	0.000	0.000	0.000
22	A	16	GLY	0	0.001	0.015	25.444	-0.001	-0.001	0.000	0.000	0.000	0.000
23	A	17	LEU	0	-0.010	0.005	25.859	-0.002	-0.002	0.000	0.000	0.000	0.000
24	A	18	LEU	0	0.046	0.021	19.942	-0.009	-0.009	0.000	0.000	0.000	0.000
25	A	19	ASN	0	-0.019	-0.011	23.899	-0.002	-0.002	0.000	0.000	0.000	0.000
26	A	20	SER	0	-0.052	-0.049	26.051	0.001	0.001	0.000	0.000	0.000	0.000
27	A	21	VAL	0	0.023	0.016	22.310	-0.002	-0.002	0.000	0.000	0.000	0.000
28	A	22	GLU	-1	-0.805	-0.887	20.098	-0.136	-0.136	0.000	0.000	0.000	0.000
29	A	23	LEU	0	-0.094	-0.044	23.586	0.001	0.001	0.000	0.000	0.000	0.000
30	A	24	ILE	0	-0.061	-0.023	25.980	0.005	0.005	0.000	0.000	0.000	0.000
31	A	25	LEU	0	-0.013	-0.006	22.114	-0.005	-0.005	0.000	0.000	0.000	0.000
32	A	26	GLY	0	0.009	0.026	21.549	-0.021	-0.021	0.000	0.000	0.000	0.000
33	A	27	LYS	1	0.834	0.885	18.896	0.077	0.077	0.000	0.000	0.000	0.000
34	A	28	GLN	0	-0.003	-0.012	16.869	-0.058	-0.058	0.000	0.000	0.000	0.000
35	A	29	PRO	0	-0.014	-0.007	12.266	0.005	0.005	0.000	0.000	0.000	0.000
36	A	30	ASP	-1	-0.793	-0.869	10.172	-0.874	-0.874	0.000	0.000	0.000	0.000
37	A	31	ILE	0	-0.043	-0.020	12.846	-0.032	-0.032	0.000	0.000	0.000	0.000
38	A	32	HIS	0	0.019	0.027	11.706	0.132	0.132	0.000	0.000	0.000	0.000
39	A	33	THR	0	-0.047	-0.049	17.106	-0.005	-0.005	0.000	0.000	0.000	0.000
40	A	34	LEU	0	-0.001	0.008	20.634	0.012	0.012	0.000	0.000	0.000	0.000
41	A	35	CYS	0	-0.057	-0.013	23.165	-0.009	-0.009	0.000	0.000	0.000	0.000
42	A	36	ALA	0	0.085	0.051	26.721	0.011	0.011	0.000	0.000	0.000	0.000
43	A	37	TYR	0	-0.018	-0.027	28.959	-0.003	-0.003	0.000	0.000	0.000	0.000
44	A	38	VAL	0	-0.044	-0.013	28.235	-0.002	-0.002	0.000	0.000	0.000	0.000
45	A	39	GLU	-1	-0.971	-0.979	27.277	0.030	0.030	0.000	0.000	0.000	0.000
46	A	40	GLU	-1	-0.963	-0.978	31.622	0.006	0.006	0.000	0.000	0.000	0.000
47	A	41	GLU	-1	-0.956	-0.983	31.077	0.038	0.038	0.000	0.000	0.000	0.000
48	A	42	VAL	0	-0.040	-0.013	26.134	0.008	0.008	0.000	0.000	0.000	0.000
49	A	43	ASP	-1	-0.860	-0.917	28.762	0.020	0.020	0.000	0.000	0.000	0.000
50	A	44	LEU	0	0.017	-0.011	27.058	-0.002	-0.002	0.000	0.000	0.000	0.000
51	A	45	THR	0	-0.021	-0.027	26.419	-0.007	-0.007	0.000	0.000	0.000	0.000
52	A	46	GLN	0	-0.006	-0.008	23.162	0.000	0.000	0.000	0.000	0.000	0.000
53	A	47	GLN	0	0.012	0.007	22.985	-0.008	-0.008	0.000	0.000	0.000	0.000
54	A	48	VAL	0	-0.020	-0.018	21.790	-0.013	-0.013	0.000	0.000	0.000	0.000
55	A	49	GLU	-1	-0.874	-0.939	20.932	-0.023	-0.023	0.000	0.000	0.000	0.000
56	A	50	ALA	0	-0.009	0.001	19.150	-0.009	-0.009	0.000	0.000	0.000	0.000
57	A	51	LEU	0	-0.035	-0.008	16.392	-0.008	-0.008	0.000	0.000	0.000	0.000
58	A	52	VAL	0	0.010	-0.011	15.933	-0.046	-0.046	0.000	0.000	0.000	0.000
59	A	53	ALA	0	-0.021	-0.012	15.538	-0.047	-0.047	0.000	0.000	0.000	0.000
60	A	54	ARG	1	0.819	0.920	11.989	0.165	0.165	0.000	0.000	0.000	0.000
61	A	55	PHE	0	-0.006	0.014	10.564	-0.086	-0.086	0.000	0.000	0.000	0.000
62	A	56	PRO	0	0.039	0.018	7.369	0.206	0.206	0.000	0.000	0.000	0.000
63	A	57	ALA	0	0.012	0.007	10.628	-0.031	-0.031	0.000	0.000	0.000	0.000
64	A	58	GLN	0	-0.006	-0.006	9.742	0.184	0.184	0.000	0.000	0.000	0.000
65	A	59	ASP	-1	-0.822	-0.903	7.790	-2.265	-2.265	0.000	0.000	0.000	0.000
66	A	60	GLU	-1	-0.803	-0.865	10.643	-0.404	-0.404	0.000	0.000	0.000	0.000
67	A	61	LEU	0	-0.046	-0.022	13.214	-0.048	-0.048	0.000	0.000	0.000	0.000
68	A	62	ILE	0	0.013	0.011	15.667	0.069	0.069	0.000	0.000	0.000	0.000
69	A	63	VAL	0	0.000	-0.003	18.734	0.011	0.011	0.000	0.000	0.000	0.000
70	A	64	ILE	0	-0.014	-0.011	21.127	0.008	0.008	0.000	0.000	0.000	0.000
71	A	65	THR	0	0.029	-0.004	24.212	0.011	0.011	0.000	0.000	0.000	0.000
72	A	66	ASP	-1	-0.768	-0.868	27.036	-0.087	-0.087	0.000	0.000	0.000	0.000
73	A	67	ILE	0	-0.045	-0.020	30.126	-0.001	-0.001	0.000	0.000	0.000	0.000
74	A	68	PHE	0	0.072	0.022	31.741	0.003	0.003	0.000	0.000	0.000	0.000
75	A	69	ALA	0	-0.025	-0.012	33.302	0.006	0.006	0.000	0.000	0.000	0.000
76	A	70	GLY	0	0.034	0.039	34.028	0.008	0.008	0.000	0.000	0.000	0.000
77	A	71	SER	0	0.009	-0.015	32.408	-0.006	-0.006	0.000	0.000	0.000	0.000
78	A	72	VAL	0	0.027	0.014	27.003	0.000	0.000	0.000	0.000	0.000	0.000
79	A	73	ASN	0	0.012	0.020	27.799	-0.018	-0.018	0.000	0.000	0.000	0.000
80	A	74	ASN	0	-0.035	-0.039	28.387	-0.014	-0.014	0.000	0.000	0.000	0.000
81	A	75	GLU	-1	-0.773	-0.853	27.146	-0.035	-0.035	0.000	0.000	0.000	0.000
82	A	76	PHE	0	0.031	0.005	20.580	-0.001	-0.001	0.000	0.000	0.000	0.000
83	A	77	VAL	0	-0.016	-0.003	24.866	-0.013	-0.013	0.000	0.000	0.000	0.000
84	A	78	ARG	1	0.755	0.869	24.415	0.034	0.034	0.000	0.000	0.000	0.000
85	A	79	PHE	0	0.014	0.003	21.017	0.005	0.005	0.000	0.000	0.000	0.000
86	A	80	LEU	0	-0.004	0.004	22.102	-0.024	-0.024	0.000	0.000	0.000	0.000
87	A	81	SER	0	-0.051	-0.021	24.090	-0.004	-0.004	0.000	0.000	0.000	0.000
88	A	82	ARG	1	0.815	0.908	13.712	0.367	0.367	0.000	0.000	0.000	0.000
89	A	83	PRO	0	-0.006	-0.001	16.588	-0.002	-0.002	0.000	0.000	0.000	0.000
90	A	84	HIS	0	-0.024	-0.030	14.539	-0.016	-0.016	0.000	0.000	0.000	0.000
91	A	85	PHE	0	0.026	0.026	16.700	-0.041	-0.041	0.000	0.000	0.000	0.000
92	A	86	HIS	0	0.017	0.002	18.412	0.000	0.000	0.000	0.000	0.000	0.000
93	A	87	LEU	0	-0.010	-0.001	21.259	-0.002	-0.002	0.000	0.000	0.000	0.000
94	A	88	LEU	0	0.002	0.009	23.149	0.008	0.008	0.000	0.000	0.000	0.000
95	A	89	SER	0	-0.016	-0.015	26.337	0.007	0.007	0.000	0.000	0.000	0.000
96	A	90	GLY	0	-0.015	0.001	29.272	0.004	0.004	0.000	0.000	0.000	0.000
97	A	91	LEU	0	-0.068	-0.019	24.888	-0.006	-0.006	0.000	0.000	0.000	0.000
98	A	92	ASN	0	-0.003	-0.019	28.355	0.009	0.009	0.000	0.000	0.000	0.000
99	A	93	LEU	0	0.048	0.022	27.391	-0.012	-0.012	0.000	0.000	0.000	0.000
100	A	94	PRO	0	0.018	0.008	27.843	-0.013	-0.013	0.000	0.000	0.000	0.000
101	A	95	LEU	0	0.038	0.020	25.849	-0.011	-0.011	0.000	0.000	0.000	0.000
102	A	96	ILE	0	-0.005	0.001	22.347	-0.021	-0.021	0.000	0.000	0.000	0.000
103	A	97	ILE	0	-0.009	-0.013	23.339	-0.022	-0.022	0.000	0.000	0.000	0.000
104	A	98	ASP	-1	-0.832	-0.897	24.682	-0.270	-0.270	0.000	0.000	0.000	0.000
105	A	99	LEU	0	0.005	-0.010	21.280	-0.022	-0.022	0.000	0.000	0.000	0.000
106	A	100	LEU	0	-0.028	-0.012	18.457	-0.040	-0.040	0.000	0.000	0.000	0.000
107	A	101	ILE	0	-0.049	-0.016	20.386	-0.026	-0.026	0.000	0.000	0.000	0.000
108	A	102	SER	0	-0.024	-0.026	22.296	-0.022	-0.022	0.000	0.000	0.000	0.000
109	A	103	ALA	0	0.001	0.008	17.053	-0.025	-0.025	0.000	0.000	0.000	0.000
110	A	104	ALA	0	-0.046	-0.029	17.110	-0.072	-0.072	0.000	0.000	0.000	0.000
111	A	105	GLU	-1	-0.840	-0.897	18.496	-0.407	-0.407	0.000	0.000	0.000	0.000
112	A	106	ASP	-1	-0.909	-0.951	18.051	-0.525	-0.525	0.000	0.000	0.000	0.000
113	A	107	ASN	0	0.011	0.014	19.079	0.009	0.009	0.000	0.000	0.000	0.000
114	A	108	THR	0	0.019	-0.040	17.958	0.026	0.026	0.000	0.000	0.000	0.000
115	A	109	GLU	-1	-0.942	-0.961	20.913	-0.230	-0.230	0.000	0.000	0.000	0.000
116	A	110	LYS	1	0.755	0.875	24.561	0.327	0.327	0.000	0.000	0.000	0.000
117	A	111	LEU	0	-0.013	0.007	19.569	0.020	0.020	0.000	0.000	0.000	0.000
118	A	112	ILE	0	-0.003	-0.009	21.313	0.023	0.023	0.000	0.000	0.000	0.000
119	A	113	THR	0	-0.048	-0.052	24.814	0.025	0.025	0.000	0.000	0.000	0.000
120	A	114	GLU	-1	-0.814	-0.882	27.420	-0.247	-0.247	0.000	0.000	0.000	0.000
121	A	115	ALA	0	0.056	0.046	25.636	0.019	0.019	0.000	0.000	0.000	0.000
122	A	116	LEU	0	-0.079	-0.054	27.594	0.021	0.021	0.000	0.000	0.000	0.000
123	A	117	THR	0	-0.120	-0.059	29.758	0.021	0.021	0.000	0.000	0.000	0.000
124	A	118	ASN	0	0.049	0.005	30.011	0.023	0.023	0.000	0.000	0.000	0.000
125	A	119	ALA	0	-0.019	-0.005	29.940	0.010	0.010	0.000	0.000	0.000	0.000
126	A	120	LYS	1	0.882	0.932	31.983	0.156	0.156	0.000	0.000	0.000	0.000
127	A	121	GLU	-1	-0.914	-0.952	35.284	-0.141	-0.141	0.000	0.000	0.000	0.000
128	A	122	SER	0	-0.033	-0.015	33.975	0.006	0.006	0.000	0.000	0.000	0.000
129	A	123	ILE	0	-0.078	-0.022	33.330	0.008	0.008	0.000	0.000	0.000	0.000
130	A	124	GLN	0	0.034	0.037	37.257	0.008	0.008	0.000	0.000	0.000	0.000
131	A	125	TYR	0	0.006	-0.005	40.959	0.004	0.004	0.000	0.000	0.000	0.000
132	A	126	CYS	0	0.059	0.021	42.185	0.001	0.001	0.000	0.000	0.000	0.000
133	A	127	ASN	0	-0.032	-0.018	44.759	-0.001	-0.001	0.000	0.000	0.000	0.000
134	A	128	GLN	0	-0.002	0.003	47.523	0.000	0.000	0.000	0.000	0.000	0.000
135	A	129	THR	0	0.012	-0.004	43.062	0.002	0.002	0.000	0.000	0.000	0.000
136	A	130	ILE	0	0.027	0.009	43.982	-0.001	-0.001	0.000	0.000	0.000	0.000
137	A	131	ALA	0	-0.001	0.003	47.056	0.001	0.001	0.000	0.000	0.000	0.000
138	A	132	SER	0	-0.043	-0.032	48.167	0.002	0.002	0.000	0.000	0.000	0.000
139	A	133	ALA	0	-0.039	-0.006	46.336	-0.001	-0.001	0.000	0.000	0.000	0.000
140	A	134	MET	0	-0.102	-0.046	48.204	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)