FMO DATABASE

FMODB ID: G68R1

Calculation Name: 5MC7-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 5MC7

Chain ID: A

ChEMBL ID:

UniProt ID: P61923

Base Structure: X-ray

Registration Date: 2023-06-22

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	139
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1327997.955941
FMO2-HF: Nuclear repulsion	1272404.78625
FMO2-HF: Total energy	-55593.169691
FMO2-MP2: Total energy	-55755.089879

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:12:THR)

Summations of interaction energy for fragment #1(A:12:THR)

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.
-16.805	-11.775	9.824	-7.032	-7.821	-0.064

Interaction energy analysis for fragmet #1(A:12:THR)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.075 / q_NPA : -0.046

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	14	LYS	1	0.816	0.879	3.082	0.690	2.659	0.183	-0.808	-1.343	0.000
4	A	15	ALA	0	-0.032	-0.030	4.535	0.660	0.735	-0.001	-0.006	-0.068	0.000
5	A	16	ILE	0	0.015	0.031	7.912	-0.115	-0.115	0.000	0.000	0.000	0.000
6	A	17	LEU	0	-0.022	-0.018	10.749	0.074	0.074	0.000	0.000	0.000	0.000
7	A	18	ILE	0	0.001	0.001	14.205	0.006	0.006	0.000	0.000	0.000	0.000
8	A	19	LEU	0	-0.017	-0.002	17.633	0.012	0.012	0.000	0.000	0.000	0.000
9	A	20	ASP	-1	-0.750	-0.875	20.384	-0.091	-0.091	0.000	0.000	0.000	0.000
10	A	21	ASN	0	-0.021	-0.027	24.028	-0.011	-0.011	0.000	0.000	0.000	0.000
11	A	22	ASP	-1	-0.917	-0.940	26.498	-0.090	-0.090	0.000	0.000	0.000	0.000
12	A	23	GLY	0	-0.064	-0.039	22.862	-0.006	-0.006	0.000	0.000	0.000	0.000
13	A	24	ASP	-1	-0.901	-0.959	22.186	-0.129	-0.129	0.000	0.000	0.000	0.000
14	A	25	ARG	1	0.720	0.831	16.560	0.169	0.169	0.000	0.000	0.000	0.000
15	A	26	LEU	0	-0.026	-0.009	20.330	0.019	0.019	0.000	0.000	0.000	0.000
16	A	27	PHE	0	-0.022	-0.030	13.080	0.028	0.028	0.000	0.000	0.000	0.000
17	A	28	ALA	0	-0.003	0.001	14.281	-0.039	-0.039	0.000	0.000	0.000	0.000
18	A	29	LYS	1	0.795	0.889	10.229	-0.142	-0.142	0.000	0.000	0.000	0.000
19	A	30	TYR	0	0.000	-0.033	8.819	-0.145	-0.145	0.000	0.000	0.000	0.000
20	A	31	TYR	0	0.008	-0.018	4.948	0.145	0.145	0.000	0.000	0.000	0.000
21	A	32	ASP	-1	-0.773	-0.834	5.344	-0.736	-0.736	0.000	0.000	0.000	0.000
22	A	33	ASP	-1	-0.920	-0.960	7.284	0.009	0.009	0.000	0.000	0.000	0.000
23	A	34	THR	0	-0.081	-0.064	8.083	-0.062	-0.062	0.000	0.000	0.000	0.000
24	A	35	TYR	0	-0.058	-0.042	10.737	0.054	0.054	0.000	0.000	0.000	0.000
25	A	36	PRO	0	0.062	0.057	13.301	0.030	0.030	0.000	0.000	0.000	0.000
26	A	37	SER	0	-0.057	-0.066	14.936	0.038	0.038	0.000	0.000	0.000	0.000
27	A	38	VAL	0	0.076	0.024	17.404	-0.028	-0.028	0.000	0.000	0.000	0.000
28	A	39	LYS	1	0.942	0.968	19.186	0.114	0.114	0.000	0.000	0.000	0.000
29	A	40	GLU	-1	-0.850	-0.890	16.949	-0.210	-0.210	0.000	0.000	0.000	0.000
30	A	41	GLN	0	0.029	0.026	13.997	-0.013	-0.013	0.000	0.000	0.000	0.000
31	A	42	LYS	1	0.901	0.953	16.377	0.107	0.107	0.000	0.000	0.000	0.000
32	A	43	ALA	0	-0.054	-0.019	19.613	-0.002	-0.002	0.000	0.000	0.000	0.000
33	A	44	PHE	0	0.055	0.031	12.214	-0.007	-0.007	0.000	0.000	0.000	0.000
34	A	45	GLU	-1	-0.693	-0.805	15.988	-0.262	-0.262	0.000	0.000	0.000	0.000
35	A	46	LYS	1	0.951	0.980	17.876	0.170	0.170	0.000	0.000	0.000	0.000
36	A	47	ASN	0	-0.063	-0.033	19.048	0.033	0.033	0.000	0.000	0.000	0.000
37	A	48	ILE	0	0.010	-0.006	14.908	0.000	0.000	0.000	0.000	0.000	0.000
38	A	49	PHE	0	0.007	0.040	18.393	0.011	0.011	0.000	0.000	0.000	0.000
39	A	50	ASN	0	-0.060	-0.037	21.168	0.022	0.022	0.000	0.000	0.000	0.000
40	A	51	LYS	1	0.769	0.880	20.197	0.373	0.373	0.000	0.000	0.000	0.000
41	A	52	THR	0	-0.046	-0.002	18.513	-0.016	-0.016	0.000	0.000	0.000	0.000
42	A	53	HIS	0	-0.048	-0.035	21.923	0.036	0.036	0.000	0.000	0.000	0.000
43	A	54	ARG	1	0.825	0.889	22.812	0.102	0.102	0.000	0.000	0.000	0.000
44	A	55	THR	0	0.054	0.020	20.142	0.005	0.005	0.000	0.000	0.000	0.000
45	A	56	ASP	-1	-0.887	-0.932	21.938	-0.101	-0.101	0.000	0.000	0.000	0.000
46	A	57	SER	0	-0.087	-0.073	17.573	0.014	0.014	0.000	0.000	0.000	0.000
47	A	58	GLU	-1	-0.874	-0.883	17.376	-0.292	-0.292	0.000	0.000	0.000	0.000
48	A	59	ILE	0	0.001	0.016	12.569	-0.038	-0.038	0.000	0.000	0.000	0.000
49	A	60	ALA	0	0.024	0.007	14.484	0.052	0.052	0.000	0.000	0.000	0.000
50	A	61	LEU	0	-0.006	0.012	12.775	-0.114	-0.114	0.000	0.000	0.000	0.000
51	A	62	LEU	0	-0.008	-0.019	14.343	0.116	0.116	0.000	0.000	0.000	0.000
52	A	63	GLU	-1	-0.808	-0.904	14.319	-0.504	-0.504	0.000	0.000	0.000	0.000
53	A	64	GLY	0	0.004	0.013	13.980	-0.019	-0.019	0.000	0.000	0.000	0.000
54	A	65	LEU	0	-0.073	-0.034	8.577	-0.183	-0.183	0.000	0.000	0.000	0.000
55	A	66	THR	0	0.013	-0.006	8.536	0.378	0.378	0.000	0.000	0.000	0.000
56	A	67	VAL	0	-0.022	-0.008	9.779	-0.207	-0.207	0.000	0.000	0.000	0.000
57	A	68	VAL	0	0.015	0.017	10.168	0.100	0.100	0.000	0.000	0.000	0.000
58	A	69	TYR	0	-0.068	-0.090	12.703	0.023	0.023	0.000	0.000	0.000	0.000
59	A	70	LYS	1	0.948	0.992	15.716	0.095	0.095	0.000	0.000	0.000	0.000
60	A	71	SER	0	-0.015	0.003	18.917	-0.002	-0.002	0.000	0.000	0.000	0.000
61	A	72	SER	0	-0.009	-0.019	22.222	0.008	0.008	0.000	0.000	0.000	0.000
62	A	73	ILE	0	0.019	0.001	24.605	-0.011	-0.011	0.000	0.000	0.000	0.000
63	A	74	ASP	-1	-0.843	-0.923	26.862	-0.061	-0.061	0.000	0.000	0.000	0.000
64	A	75	LEU	0	-0.010	0.012	22.027	-0.001	-0.001	0.000	0.000	0.000	0.000
65	A	76	TYR	0	0.020	0.015	20.040	0.010	0.010	0.000	0.000	0.000	0.000
66	A	77	PHE	0	-0.020	-0.015	16.237	0.005	0.005	0.000	0.000	0.000	0.000
67	A	78	TYR	0	0.007	-0.026	13.652	-0.012	-0.012	0.000	0.000	0.000	0.000
68	A	79	VAL	0	-0.001	-0.004	8.032	0.027	0.027	0.000	0.000	0.000	0.000
69	A	80	ILE	0	0.006	0.012	8.407	-0.017	-0.017	0.000	0.000	0.000	0.000
70	A	81	GLY	0	0.081	0.036	5.400	-0.692	-0.692	0.000	0.000	0.000	0.000
71	A	82	SER	0	0.026	0.011	4.709	1.392	1.492	-0.001	-0.004	-0.095	0.000
72	A	83	SER	0	0.026	0.011	6.527	-0.056	-0.056	0.000	0.000	0.000	0.000
73	A	84	TYR	0	-0.075	-0.049	7.789	0.281	0.281	0.000	0.000	0.000	0.000
74	A	85	GLU	-1	-0.871	-0.900	2.077	-17.587	-16.277	4.681	-3.175	-2.816	-0.042
75	A	86	ASN	0	0.007	-0.003	5.332	1.028	1.028	0.000	0.000	0.000	0.000
76	A	87	GLU	-1	-0.836	-0.942	6.654	-0.609	-0.609	0.000	0.000	0.000	0.000
77	A	88	LEU	0	0.003	-0.006	9.037	0.168	0.168	0.000	0.000	0.000	0.000
78	A	89	MET	0	-0.006	0.000	5.563	0.015	0.015	0.000	0.000	0.000	0.000
79	A	90	LEU	0	0.022	0.023	4.672	0.265	0.327	-0.001	-0.007	-0.054	0.000
80	A	91	MET	0	-0.022	-0.007	7.468	0.128	0.128	0.000	0.000	0.000	0.000
81	A	92	ALA	0	0.002	0.007	9.693	0.035	0.035	0.000	0.000	0.000	0.000
82	A	93	VAL	0	0.017	0.009	6.691	0.043	0.043	0.000	0.000	0.000	0.000
83	A	94	LEU	0	-0.008	0.011	10.026	-0.051	-0.051	0.000	0.000	0.000	0.000
84	A	95	ASN	0	0.005	-0.019	12.767	-0.008	-0.008	0.000	0.000	0.000	0.000
85	A	96	CYS	0	0.045	0.067	12.670	0.005	0.005	0.000	0.000	0.000	0.000
86	A	97	LEU	0	0.020	0.016	13.009	-0.014	-0.014	0.000	0.000	0.000	0.000
87	A	98	PHE	0	-0.016	-0.014	14.933	-0.017	-0.017	0.000	0.000	0.000	0.000
88	A	99	ASP	-1	-0.870	-0.948	17.885	0.052	0.052	0.000	0.000	0.000	0.000
89	A	100	SER	0	-0.043	-0.045	16.806	0.010	0.010	0.000	0.000	0.000	0.000
90	A	101	LEU	0	0.011	-0.001	18.251	-0.010	-0.010	0.000	0.000	0.000	0.000
91	A	102	SER	0	-0.011	0.000	20.942	-0.011	-0.011	0.000	0.000	0.000	0.000
92	A	103	GLN	0	-0.040	-0.012	22.818	0.002	0.002	0.000	0.000	0.000	0.000
93	A	104	MET	0	-0.074	-0.025	20.938	-0.004	-0.004	0.000	0.000	0.000	0.000
94	A	105	LEU	0	-0.005	0.012	23.802	-0.005	-0.005	0.000	0.000	0.000	0.000
95	A	106	ARG	1	0.861	0.923	26.549	-0.055	-0.055	0.000	0.000	0.000	0.000
96	A	107	LYS	1	0.913	0.944	27.044	-0.036	-0.036	0.000	0.000	0.000	0.000
97	A	108	ASN	0	-0.039	-0.009	28.061	-0.008	-0.008	0.000	0.000	0.000	0.000
98	A	109	VAL	0	0.026	0.026	22.000	0.003	0.003	0.000	0.000	0.000	0.000
99	A	110	GLU	-1	-0.897	-0.922	25.307	-0.031	-0.031	0.000	0.000	0.000	0.000
100	A	111	LYS	1	0.872	0.909	25.856	0.082	0.082	0.000	0.000	0.000	0.000
101	A	112	ARG	1	0.858	0.921	26.881	0.009	0.009	0.000	0.000	0.000	0.000
102	A	113	ALA	0	0.032	0.022	27.644	0.006	0.006	0.000	0.000	0.000	0.000
103	A	114	LEU	0	0.007	0.004	20.834	0.010	0.010	0.000	0.000	0.000	0.000
104	A	115	LEU	0	-0.009	-0.031	24.883	0.008	0.008	0.000	0.000	0.000	0.000
105	A	116	GLU	-1	-0.902	-0.941	26.677	0.016	0.016	0.000	0.000	0.000	0.000
106	A	117	ASN	0	-0.061	-0.031	25.262	0.014	0.014	0.000	0.000	0.000	0.000
107	A	118	MET	0	0.017	0.024	21.294	0.006	0.006	0.000	0.000	0.000	0.000
108	A	119	GLU	-1	-0.876	-0.934	21.353	0.116	0.116	0.000	0.000	0.000	0.000
109	A	120	GLY	0	0.006	-0.007	20.926	0.022	0.022	0.000	0.000	0.000	0.000
110	A	121	LEU	0	0.042	0.018	16.890	0.021	0.021	0.000	0.000	0.000	0.000
111	A	122	PHE	0	-0.052	-0.032	16.925	0.014	0.014	0.000	0.000	0.000	0.000
112	A	123	LEU	0	-0.001	-0.010	16.231	0.036	0.036	0.000	0.000	0.000	0.000
113	A	124	ALA	0	0.000	0.002	16.240	0.045	0.045	0.000	0.000	0.000	0.000
114	A	125	VAL	0	-0.058	-0.035	11.161	0.056	0.056	0.000	0.000	0.000	0.000
115	A	126	ASP	-1	-0.807	-0.883	11.376	0.390	0.390	0.000	0.000	0.000	0.000
116	A	127	GLU	-1	-0.773	-0.857	12.528	0.530	0.530	0.000	0.000	0.000	0.000
117	A	128	ILE	0	-0.057	-0.005	8.937	0.081	0.081	0.000	0.000	0.000	0.000
118	A	129	VAL	0	-0.044	-0.027	5.185	0.289	0.289	0.000	0.000	0.000	0.000
119	A	130	ASP	-1	-0.905	-0.940	6.980	0.655	0.655	0.000	0.000	0.000	0.000
120	A	131	GLY	0	0.024	-0.001	6.706	0.283	0.283	0.000	0.000	0.000	0.000
121	A	132	GLY	0	-0.007	0.002	2.939	-0.159	0.225	0.109	-0.169	-0.323	0.000
122	A	133	VAL	0	-0.029	-0.010	2.242	-1.181	-0.672	4.829	-2.649	-2.689	-0.023
123	A	134	ILE	0	0.005	-0.007	3.566	-1.817	-1.196	0.025	-0.214	-0.433	0.001
124	A	135	LEU	0	-0.031	-0.007	5.558	-0.171	-0.171	0.000	0.000	0.000	0.000
125	A	136	GLU	-1	-0.873	-0.943	9.092	0.393	0.393	0.000	0.000	0.000	0.000
126	A	137	SER	0	0.024	-0.006	10.501	0.021	0.021	0.000	0.000	0.000	0.000
127	A	138	ASP	-1	-0.825	-0.893	12.311	0.160	0.160	0.000	0.000	0.000	0.000
128	A	139	PRO	0	0.077	0.026	16.158	0.012	0.012	0.000	0.000	0.000	0.000
129	A	140	GLN	0	-0.112	-0.073	17.772	-0.038	-0.038	0.000	0.000	0.000	0.000
130	A	141	GLN	0	-0.051	-0.024	16.972	-0.019	-0.019	0.000	0.000	0.000	0.000
131	A	142	VAL	0	0.010	0.009	14.561	-0.004	-0.004	0.000	0.000	0.000	0.000
132	A	143	VAL	0	0.015	0.003	17.428	-0.018	-0.018	0.000	0.000	0.000	0.000
133	A	144	HIS	0	-0.040	-0.016	20.789	-0.029	-0.029	0.000	0.000	0.000	0.000
134	A	145	ARG	1	0.812	0.889	15.183	-0.542	-0.542	0.000	0.000	0.000	0.000
135	A	146	VAL	0	0.000	0.009	18.550	-0.008	-0.008	0.000	0.000	0.000	0.000
136	A	147	ALA	0	-0.009	-0.001	20.873	-0.016	-0.016	0.000	0.000	0.000	0.000
137	A	148	LEU	0	-0.116	-0.056	23.000	-0.014	-0.014	0.000	0.000	0.000	0.000
138	A	149	ARG	1	0.807	0.886	17.516	-0.362	-0.362	0.000	0.000	0.000	0.000
139	A	150	GLY	0	-0.008	0.016	23.312	-0.004	-0.004	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:12:THR)