FMO DATABASE

FMODB ID: 175YZ

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1327355.960506
FMO2-HF: Nuclear repulsion	1271764.321984
FMO2-HF: Total energy	-55591.638522
FMO2-MP2: Total energy	-55753.579948

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.
-8.678	-2.751	5.785	-5.344	-6.368	-0.043

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 : -0.053 / q_NPA : -0.040

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	0.892	0.937	3.347	1.668	3.502	0.180	-0.620	-1.395	0.001
4	A	15	ALA	0	-0.032	-0.030	4.465	0.509	0.591	-0.001	-0.008	-0.073	0.000
5	A	16	ILE	0	0.016	0.029	7.937	-0.040	-0.040	0.000	0.000	0.000	0.000
6	A	17	LEU	0	-0.023	-0.012	10.806	0.030	0.030	0.000	0.000	0.000	0.000
7	A	18	ILE	0	-0.008	-0.004	14.208	0.029	0.029	0.000	0.000	0.000	0.000
8	A	19	LEU	0	-0.014	-0.004	17.645	-0.004	-0.004	0.000	0.000	0.000	0.000
9	A	20	ASP	-1	-0.732	-0.867	20.334	-0.059	-0.059	0.000	0.000	0.000	0.000
10	A	21	ASN	0	-0.028	-0.039	23.918	-0.017	-0.017	0.000	0.000	0.000	0.000
11	A	22	ASP	-1	-0.902	-0.917	26.435	-0.072	-0.072	0.000	0.000	0.000	0.000
12	A	23	GLY	0	-0.096	-0.055	22.719	-0.012	-0.012	0.000	0.000	0.000	0.000
13	A	24	ASP	-1	-0.956	-0.973	22.091	-0.133	-0.133	0.000	0.000	0.000	0.000
14	A	25	ARG	1	0.734	0.844	16.860	0.214	0.214	0.000	0.000	0.000	0.000
15	A	26	LEU	0	-0.037	-0.013	20.381	0.015	0.015	0.000	0.000	0.000	0.000
16	A	27	PHE	0	-0.021	-0.029	13.269	0.017	0.017	0.000	0.000	0.000	0.000
17	A	28	ALA	0	-0.006	-0.003	14.429	-0.032	-0.032	0.000	0.000	0.000	0.000
18	A	29	LYS	1	0.935	0.983	10.132	-0.052	-0.052	0.000	0.000	0.000	0.000
19	A	30	TYR	0	-0.011	-0.039	9.038	-0.101	-0.101	0.000	0.000	0.000	0.000
20	A	31	TYR	0	-0.014	-0.031	4.990	0.231	0.231	0.000	0.000	0.000	0.000
21	A	32	ASP	-1	-0.842	-0.900	5.347	-1.648	-1.648	0.000	0.000	0.000	0.000
22	A	33	ASP	-1	-0.901	-0.952	7.497	-0.432	-0.432	0.000	0.000	0.000	0.000
23	A	34	THR	0	-0.085	-0.053	7.974	0.010	0.010	0.000	0.000	0.000	0.000
24	A	35	TYR	0	-0.060	-0.046	10.655	0.106	0.106	0.000	0.000	0.000	0.000
25	A	36	PRO	0	0.074	0.061	13.286	0.049	0.049	0.000	0.000	0.000	0.000
26	A	37	SER	0	-0.059	-0.037	15.074	0.066	0.066	0.000	0.000	0.000	0.000
27	A	38	VAL	0	0.057	0.020	17.478	-0.018	-0.018	0.000	0.000	0.000	0.000
28	A	39	LYS	1	0.939	0.965	19.312	0.197	0.197	0.000	0.000	0.000	0.000
29	A	40	GLU	-1	-0.848	-0.925	16.777	-0.367	-0.367	0.000	0.000	0.000	0.000
30	A	41	GLN	0	0.026	0.020	14.045	0.021	0.021	0.000	0.000	0.000	0.000
31	A	42	LYS	1	0.953	0.982	16.356	0.155	0.155	0.000	0.000	0.000	0.000
32	A	43	ALA	0	-0.046	-0.021	19.569	0.011	0.011	0.000	0.000	0.000	0.000
33	A	44	PHE	0	0.039	0.029	11.837	0.003	0.003	0.000	0.000	0.000	0.000
34	A	45	GLU	-1	-0.695	-0.813	16.032	-0.279	-0.279	0.000	0.000	0.000	0.000
35	A	46	LYS	1	0.990	0.995	17.708	0.190	0.190	0.000	0.000	0.000	0.000
36	A	47	ASN	0	-0.058	-0.020	18.617	0.041	0.041	0.000	0.000	0.000	0.000
37	A	48	ILE	0	0.004	-0.010	14.525	0.009	0.009	0.000	0.000	0.000	0.000
38	A	49	PHE	0	0.015	0.044	18.047	0.019	0.019	0.000	0.000	0.000	0.000
39	A	50	ASN	0	-0.044	-0.031	20.880	0.028	0.028	0.000	0.000	0.000	0.000
40	A	51	LYS	1	0.843	0.939	19.593	0.362	0.362	0.000	0.000	0.000	0.000
41	A	52	THR	0	-0.059	-0.013	18.104	-0.004	-0.004	0.000	0.000	0.000	0.000
42	A	53	HIS	0	-0.034	-0.028	21.515	0.014	0.014	0.000	0.000	0.000	0.000
43	A	54	ARG	1	0.829	0.887	22.789	0.044	0.044	0.000	0.000	0.000	0.000
44	A	55	THR	0	0.039	0.016	20.213	0.007	0.007	0.000	0.000	0.000	0.000
45	A	56	ASP	-1	-0.885	-0.934	21.910	0.019	0.019	0.000	0.000	0.000	0.000
46	A	57	SER	0	-0.111	-0.079	17.411	0.043	0.043	0.000	0.000	0.000	0.000
47	A	58	GLU	-1	-0.908	-0.934	17.338	-0.169	-0.169	0.000	0.000	0.000	0.000
48	A	59	ILE	0	-0.003	0.013	12.584	-0.021	-0.021	0.000	0.000	0.000	0.000
49	A	60	ALA	0	0.018	0.000	14.455	0.028	0.028	0.000	0.000	0.000	0.000
50	A	61	LEU	0	-0.004	0.019	13.065	-0.097	-0.097	0.000	0.000	0.000	0.000
51	A	62	LEU	0	-0.026	-0.028	14.089	0.091	0.091	0.000	0.000	0.000	0.000
52	A	63	GLU	-1	-0.906	-0.975	13.782	-0.530	-0.530	0.000	0.000	0.000	0.000
53	A	64	GLY	0	0.004	0.014	13.614	-0.048	-0.048	0.000	0.000	0.000	0.000
54	A	65	LEU	0	-0.069	-0.037	8.025	-0.214	-0.214	0.000	0.000	0.000	0.000
55	A	66	THR	0	0.030	0.012	8.560	0.287	0.287	0.000	0.000	0.000	0.000
56	A	67	VAL	0	-0.022	-0.004	9.629	-0.178	-0.178	0.000	0.000	0.000	0.000
57	A	68	VAL	0	0.027	0.026	10.151	0.091	0.091	0.000	0.000	0.000	0.000
58	A	69	TYR	0	-0.012	-0.030	12.680	0.011	0.011	0.000	0.000	0.000	0.000
59	A	70	LYS	1	0.998	1.020	15.690	-0.058	-0.058	0.000	0.000	0.000	0.000
60	A	71	SER	0	-0.021	-0.006	18.889	-0.013	-0.013	0.000	0.000	0.000	0.000
61	A	72	SER	0	-0.018	-0.014	22.194	0.013	0.013	0.000	0.000	0.000	0.000
62	A	73	ILE	0	0.016	-0.001	24.605	-0.015	-0.015	0.000	0.000	0.000	0.000
63	A	74	ASP	-1	-0.861	-0.932	26.843	-0.013	-0.013	0.000	0.000	0.000	0.000
64	A	75	LEU	0	0.004	0.018	21.885	-0.006	-0.006	0.000	0.000	0.000	0.000
65	A	76	TYR	0	0.003	0.015	19.723	0.014	0.014	0.000	0.000	0.000	0.000
66	A	77	PHE	0	-0.028	-0.021	16.136	-0.004	-0.004	0.000	0.000	0.000	0.000
67	A	78	TYR	0	0.005	-0.032	13.203	-0.001	-0.001	0.000	0.000	0.000	0.000
68	A	79	VAL	0	-0.002	-0.008	7.937	0.008	0.008	0.000	0.000	0.000	0.000
69	A	80	ILE	0	0.012	0.017	7.960	-0.006	-0.006	0.000	0.000	0.000	0.000
70	A	81	GLY	0	0.075	0.028	4.850	-0.643	-0.643	0.000	0.000	0.000	0.000
71	A	82	SER	0	0.013	0.001	4.915	1.190	1.190	0.000	0.000	0.000	0.000
72	A	83	SER	0	0.042	0.008	6.707	0.055	0.055	0.000	0.000	0.000	0.000
73	A	84	TYR	0	-0.087	-0.051	7.787	0.266	0.266	0.000	0.000	0.000	0.000
74	A	85	GLU	-1	-0.888	-0.911	2.692	-8.504	-6.129	0.510	-1.493	-1.392	-0.018
75	A	86	ASN	0	-0.007	-0.010	5.347	0.565	0.565	0.000	0.000	0.000	0.000
76	A	87	GLU	-1	-0.842	-0.942	6.640	-0.182	-0.182	0.000	0.000	0.000	0.000
77	A	88	LEU	0	0.000	-0.011	9.023	0.115	0.115	0.000	0.000	0.000	0.000
78	A	89	MET	0	-0.019	-0.003	5.530	-0.111	-0.111	0.000	0.000	0.000	0.000
79	A	90	LEU	0	0.031	0.025	4.556	0.170	0.239	-0.001	-0.008	-0.060	0.000
80	A	91	MET	0	-0.013	-0.007	7.440	0.008	0.008	0.000	0.000	0.000	0.000
81	A	92	ALA	0	-0.014	0.007	9.590	-0.036	-0.036	0.000	0.000	0.000	0.000
82	A	93	VAL	0	0.021	0.007	6.702	-0.020	-0.020	0.000	0.000	0.000	0.000
83	A	94	LEU	0	0.009	0.012	10.026	-0.123	-0.123	0.000	0.000	0.000	0.000
84	A	95	ASN	0	-0.018	-0.023	12.767	-0.072	-0.072	0.000	0.000	0.000	0.000
85	A	96	CYS	0	0.022	0.061	12.623	-0.030	-0.030	0.000	0.000	0.000	0.000
86	A	97	LEU	0	0.051	0.023	13.115	-0.057	-0.057	0.000	0.000	0.000	0.000
87	A	98	PHE	0	-0.012	-0.014	14.884	-0.051	-0.051	0.000	0.000	0.000	0.000
88	A	99	ASP	-1	-0.880	-0.947	17.847	0.238	0.238	0.000	0.000	0.000	0.000
89	A	100	SER	0	-0.048	-0.049	16.747	-0.011	-0.011	0.000	0.000	0.000	0.000
90	A	101	LEU	0	0.006	-0.003	18.111	-0.029	-0.029	0.000	0.000	0.000	0.000
91	A	102	SER	0	-0.011	-0.003	20.894	-0.029	-0.029	0.000	0.000	0.000	0.000
92	A	103	GLN	0	-0.026	-0.007	22.776	-0.009	-0.009	0.000	0.000	0.000	0.000
93	A	104	MET	0	-0.085	-0.025	20.930	-0.012	-0.012	0.000	0.000	0.000	0.000
94	A	105	LEU	0	0.001	0.011	23.538	-0.015	-0.015	0.000	0.000	0.000	0.000
95	A	106	ARG	1	0.863	0.930	26.502	-0.119	-0.119	0.000	0.000	0.000	0.000
96	A	107	LYS	1	0.914	0.941	27.019	-0.125	-0.125	0.000	0.000	0.000	0.000
97	A	108	ASN	0	0.008	0.024	28.012	-0.011	-0.011	0.000	0.000	0.000	0.000
98	A	109	VAL	0	0.023	0.024	21.957	0.000	0.000	0.000	0.000	0.000	0.000
99	A	110	GLU	-1	-0.951	-0.967	25.256	0.020	0.020	0.000	0.000	0.000	0.000
100	A	111	LYS	1	0.910	0.932	25.803	0.046	0.046	0.000	0.000	0.000	0.000
101	A	112	ARG	1	0.952	0.968	26.833	-0.015	-0.015	0.000	0.000	0.000	0.000
102	A	113	ALA	0	0.053	0.038	27.498	0.002	0.002	0.000	0.000	0.000	0.000
103	A	114	LEU	0	0.009	0.008	20.833	0.009	0.009	0.000	0.000	0.000	0.000
104	A	115	LEU	0	-0.014	-0.041	24.839	0.005	0.005	0.000	0.000	0.000	0.000
105	A	116	GLU	-1	-0.993	-0.986	26.633	0.049	0.049	0.000	0.000	0.000	0.000
106	A	117	ASN	0	-0.071	-0.035	25.065	0.007	0.007	0.000	0.000	0.000	0.000
107	A	118	MET	0	0.008	0.018	21.273	0.015	0.015	0.000	0.000	0.000	0.000
108	A	119	GLU	-1	-0.880	-0.937	21.314	0.145	0.145	0.000	0.000	0.000	0.000
109	A	120	GLY	0	-0.002	-0.008	20.891	0.027	0.027	0.000	0.000	0.000	0.000
110	A	121	LEU	0	0.039	0.020	16.722	0.034	0.034	0.000	0.000	0.000	0.000
111	A	122	PHE	0	-0.043	-0.036	16.885	0.023	0.023	0.000	0.000	0.000	0.000
112	A	123	LEU	0	0.016	-0.003	16.198	0.038	0.038	0.000	0.000	0.000	0.000
113	A	124	ALA	0	-0.011	0.001	16.208	0.058	0.058	0.000	0.000	0.000	0.000
114	A	125	VAL	0	-0.066	-0.049	11.166	0.082	0.082	0.000	0.000	0.000	0.000
115	A	126	ASP	-1	-0.895	-0.948	11.342	0.476	0.476	0.000	0.000	0.000	0.000
116	A	127	GLU	-1	-0.852	-0.907	12.506	0.652	0.652	0.000	0.000	0.000	0.000
117	A	128	ILE	0	-0.050	-0.013	8.791	0.118	0.118	0.000	0.000	0.000	0.000
118	A	129	VAL	0	-0.048	-0.035	5.392	0.398	0.398	0.000	0.000	0.000	0.000
119	A	130	ASP	-1	-0.892	-0.924	6.965	0.575	0.575	0.000	0.000	0.000	0.000
120	A	131	GLY	0	0.024	-0.009	6.829	0.356	0.356	0.000	0.000	0.000	0.000
121	A	132	GLY	0	-0.016	-0.002	2.822	-0.430	-0.028	0.131	-0.186	-0.346	0.000
122	A	133	VAL	0	-0.026	-0.002	2.224	-1.215	-0.529	4.954	-2.892	-2.748	-0.027
123	A	134	ILE	0	0.000	-0.012	3.730	-2.129	-1.650	0.012	-0.137	-0.354	0.001
124	A	135	LEU	0	-0.038	-0.009	5.535	-0.096	-0.096	0.000	0.000	0.000	0.000
125	A	136	GLU	-1	-0.890	-0.945	9.077	0.680	0.680	0.000	0.000	0.000	0.000
126	A	137	SER	0	-0.015	-0.022	10.516	0.005	0.005	0.000	0.000	0.000	0.000
127	A	138	ASP	-1	-0.829	-0.926	12.311	0.351	0.351	0.000	0.000	0.000	0.000
128	A	139	PRO	0	0.046	0.011	16.158	-0.002	-0.002	0.000	0.000	0.000	0.000
129	A	140	GLN	0	-0.109	-0.065	17.733	-0.081	-0.081	0.000	0.000	0.000	0.000
130	A	141	GLN	0	-0.038	-0.007	16.977	-0.028	-0.028	0.000	0.000	0.000	0.000
131	A	142	VAL	0	0.036	0.021	14.585	-0.026	-0.026	0.000	0.000	0.000	0.000
132	A	143	VAL	0	0.007	-0.004	17.394	-0.039	-0.039	0.000	0.000	0.000	0.000
133	A	144	HIS	0	-0.042	-0.013	20.752	-0.046	-0.046	0.000	0.000	0.000	0.000
134	A	145	ARG	1	0.911	0.953	17.016	-0.650	-0.650	0.000	0.000	0.000	0.000
135	A	146	VAL	0	0.014	0.014	18.508	-0.021	-0.021	0.000	0.000	0.000	0.000
136	A	147	ALA	0	-0.008	0.000	20.842	-0.027	-0.027	0.000	0.000	0.000	0.000
137	A	148	LEU	0	-0.131	-0.064	22.782	-0.024	-0.024	0.000	0.000	0.000	0.000
138	A	149	ARG	1	0.831	0.908	17.939	-0.435	-0.435	0.000	0.000	0.000	0.000
139	A	150	GLY	0	-0.018	0.014	23.289	-0.010	-0.010	0.000	0.000	0.000	0.000

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