FMO DATABASE

FMODB ID: 85G7Y

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1329915.517142
FMO2-HF: Nuclear repulsion	1274321.753816
FMO2-HF: Total energy	-55593.763326
FMO2-MP2: Total energy	-55755.680882

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.
-22.853	-22.386	17.952	-9.11	-9.308	-0.087

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 : -0.081 / q_NPA : -0.045

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	0.823	0.883	3.841	1.164	2.637	-0.005	-0.491	-0.977	0.002
4	A	15	ALA	0	-0.028	-0.017	4.709	0.710	0.792	-0.001	-0.003	-0.077	0.000
5	A	16	ILE	0	0.017	0.020	8.114	-0.067	-0.067	0.000	0.000	0.000	0.000
6	A	17	LEU	0	-0.017	-0.012	11.077	0.045	0.045	0.000	0.000	0.000	0.000
7	A	18	ILE	0	-0.015	-0.008	14.575	0.020	0.020	0.000	0.000	0.000	0.000
8	A	19	LEU	0	-0.003	0.010	18.127	0.004	0.004	0.000	0.000	0.000	0.000
9	A	20	ASP	-1	-0.761	-0.886	20.831	-0.093	-0.093	0.000	0.000	0.000	0.000
10	A	21	ASN	0	-0.033	-0.023	24.572	-0.009	-0.009	0.000	0.000	0.000	0.000
11	A	22	ASP	-1	-0.930	-0.963	27.025	-0.088	-0.088	0.000	0.000	0.000	0.000
12	A	23	GLY	0	-0.015	0.000	23.844	-0.005	-0.005	0.000	0.000	0.000	0.000
13	A	24	ASP	-1	-0.895	-0.940	23.098	-0.152	-0.152	0.000	0.000	0.000	0.000
14	A	25	ARG	1	0.755	0.823	16.845	0.212	0.212	0.000	0.000	0.000	0.000
15	A	26	LEU	0	-0.005	0.011	20.933	0.016	0.016	0.000	0.000	0.000	0.000
16	A	27	PHE	0	0.008	-0.019	13.522	0.023	0.023	0.000	0.000	0.000	0.000
17	A	28	ALA	0	-0.026	-0.016	14.480	-0.039	-0.039	0.000	0.000	0.000	0.000
18	A	29	LYS	1	0.791	0.888	10.490	-0.058	-0.058	0.000	0.000	0.000	0.000
19	A	30	TYR	0	-0.030	-0.050	8.877	-0.126	-0.126	0.000	0.000	0.000	0.000
20	A	31	TYR	0	-0.004	-0.024	5.130	0.175	0.175	0.000	0.000	0.000	0.000
21	A	32	ASP	-1	-0.770	-0.831	5.031	-1.217	-1.125	-0.001	-0.001	-0.090	0.000
22	A	33	ASP	-1	-0.910	-0.962	7.348	-0.190	-0.190	0.000	0.000	0.000	0.000
23	A	34	THR	0	-0.094	-0.067	8.081	-0.041	-0.041	0.000	0.000	0.000	0.000
24	A	35	TYR	0	-0.015	-0.012	10.674	0.066	0.066	0.000	0.000	0.000	0.000
25	A	36	PRO	0	0.029	0.041	13.492	0.027	0.027	0.000	0.000	0.000	0.000
26	A	37	SER	0	-0.064	-0.074	15.097	0.040	0.040	0.000	0.000	0.000	0.000
27	A	38	VAL	0	0.056	0.006	17.706	-0.027	-0.027	0.000	0.000	0.000	0.000
28	A	39	LYS	1	0.941	0.973	19.339	0.146	0.146	0.000	0.000	0.000	0.000
29	A	40	GLU	-1	-0.816	-0.874	16.989	-0.256	-0.256	0.000	0.000	0.000	0.000
30	A	41	GLN	0	0.018	0.029	14.216	-0.003	-0.003	0.000	0.000	0.000	0.000
31	A	42	LYS	1	0.868	0.932	16.527	0.134	0.134	0.000	0.000	0.000	0.000
32	A	43	ALA	0	-0.043	-0.014	19.819	0.005	0.005	0.000	0.000	0.000	0.000
33	A	44	PHE	0	0.034	0.018	12.388	-0.005	-0.005	0.000	0.000	0.000	0.000
34	A	45	GLU	-1	-0.698	-0.807	16.134	-0.291	-0.291	0.000	0.000	0.000	0.000
35	A	46	LYS	1	0.952	0.981	18.043	0.189	0.189	0.000	0.000	0.000	0.000
36	A	47	ASN	0	-0.068	-0.050	19.473	0.043	0.043	0.000	0.000	0.000	0.000
37	A	48	ILE	0	0.009	0.005	14.997	0.002	0.002	0.000	0.000	0.000	0.000
38	A	49	PHE	0	0.002	0.042	18.673	0.014	0.014	0.000	0.000	0.000	0.000
39	A	50	ASN	0	-0.064	-0.048	21.732	0.022	0.022	0.000	0.000	0.000	0.000
40	A	51	LYS	1	0.748	0.868	20.172	0.378	0.378	0.000	0.000	0.000	0.000
41	A	52	THR	0	-0.015	0.004	18.306	-0.020	-0.020	0.000	0.000	0.000	0.000
42	A	53	HIS	0	-0.056	-0.035	21.717	0.029	0.029	0.000	0.000	0.000	0.000
43	A	54	ARG	1	0.822	0.894	22.719	0.095	0.095	0.000	0.000	0.000	0.000
44	A	55	THR	0	0.030	0.012	19.989	0.009	0.009	0.000	0.000	0.000	0.000
45	A	56	ASP	-1	-0.864	-0.924	21.698	-0.079	-0.079	0.000	0.000	0.000	0.000
46	A	57	SER	0	-0.062	-0.061	17.239	0.031	0.031	0.000	0.000	0.000	0.000
47	A	58	GLU	-1	-0.872	-0.874	16.914	-0.270	-0.270	0.000	0.000	0.000	0.000
48	A	59	ILE	0	0.023	0.005	12.228	-0.026	-0.026	0.000	0.000	0.000	0.000
49	A	60	ALA	0	0.008	0.008	13.931	0.051	0.051	0.000	0.000	0.000	0.000
50	A	61	LEU	0	-0.020	0.004	12.257	-0.128	-0.128	0.000	0.000	0.000	0.000
51	A	62	LEU	0	0.005	-0.011	13.581	0.117	0.117	0.000	0.000	0.000	0.000
52	A	63	GLU	-1	-0.784	-0.885	13.671	-0.520	-0.520	0.000	0.000	0.000	0.000
53	A	64	GLY	0	-0.008	0.009	13.434	-0.006	-0.006	0.000	0.000	0.000	0.000
54	A	65	LEU	0	-0.051	-0.024	8.237	-0.166	-0.166	0.000	0.000	0.000	0.000
55	A	66	THR	0	-0.001	-0.009	8.069	0.430	0.430	0.000	0.000	0.000	0.000
56	A	67	VAL	0	-0.026	-0.014	9.062	-0.249	-0.249	0.000	0.000	0.000	0.000
57	A	68	VAL	0	0.003	0.003	9.876	0.097	0.097	0.000	0.000	0.000	0.000
58	A	69	TYR	0	-0.059	-0.070	12.365	0.026	0.026	0.000	0.000	0.000	0.000
59	A	70	LYS	1	0.893	0.962	15.387	0.024	0.024	0.000	0.000	0.000	0.000
60	A	71	SER	0	-0.030	-0.013	18.612	-0.011	-0.011	0.000	0.000	0.000	0.000
61	A	72	SER	0	0.012	-0.014	21.934	0.012	0.012	0.000	0.000	0.000	0.000
62	A	73	ILE	0	0.020	0.014	25.008	-0.011	-0.011	0.000	0.000	0.000	0.000
63	A	74	ASP	-1	-0.860	-0.928	27.271	-0.056	-0.056	0.000	0.000	0.000	0.000
64	A	75	LEU	0	0.005	0.021	22.360	-0.004	-0.004	0.000	0.000	0.000	0.000
65	A	76	TYR	0	0.001	-0.001	20.273	0.012	0.012	0.000	0.000	0.000	0.000
66	A	77	PHE	0	0.007	-0.003	16.512	0.003	0.003	0.000	0.000	0.000	0.000
67	A	78	TYR	0	0.007	-0.023	13.807	-0.003	-0.003	0.000	0.000	0.000	0.000
68	A	79	VAL	0	0.007	0.010	7.940	0.030	0.030	0.000	0.000	0.000	0.000
69	A	80	ILE	0	-0.016	-0.006	8.183	-0.003	-0.003	0.000	0.000	0.000	0.000
70	A	81	GLY	0	0.083	0.037	4.605	-0.642	-0.655	-0.001	-0.013	0.027	0.000
71	A	82	SER	0	0.029	0.004	3.951	1.686	1.882	-0.001	-0.020	-0.174	0.000
72	A	83	SER	0	0.012	0.011	5.765	-0.052	-0.052	0.000	0.000	0.000	0.000
73	A	84	TYR	0	-0.060	-0.033	7.433	0.440	0.440	0.000	0.000	0.000	0.000
74	A	85	GLU	-1	-0.862	-0.900	1.887	-24.576	-28.447	16.191	-6.710	-5.610	-0.072
75	A	86	ASN	0	0.012	-0.012	4.693	1.376	1.465	-0.001	-0.003	-0.084	0.000
76	A	87	GLU	-1	-0.858	-0.947	6.386	-0.175	-0.175	0.000	0.000	0.000	0.000
77	A	88	LEU	0	0.017	0.006	8.725	0.222	0.222	0.000	0.000	0.000	0.000
78	A	89	MET	0	-0.016	0.001	5.466	0.010	0.010	0.000	0.000	0.000	0.000
79	A	90	LEU	0	0.021	0.015	4.260	0.320	0.424	-0.001	-0.016	-0.088	0.000
80	A	91	MET	0	0.005	0.013	7.330	0.049	0.049	0.000	0.000	0.000	0.000
81	A	92	ALA	0	-0.010	0.002	9.691	0.001	0.001	0.000	0.000	0.000	0.000
82	A	93	VAL	0	0.021	0.010	6.736	-0.038	-0.038	0.000	0.000	0.000	0.000
83	A	94	LEU	0	-0.032	-0.006	10.000	-0.101	-0.101	0.000	0.000	0.000	0.000
84	A	95	ASN	0	-0.009	-0.006	12.608	-0.046	-0.046	0.000	0.000	0.000	0.000
85	A	96	CYS	0	0.016	0.041	12.749	-0.009	-0.009	0.000	0.000	0.000	0.000
86	A	97	LEU	0	0.031	0.036	13.169	-0.023	-0.023	0.000	0.000	0.000	0.000
87	A	98	PHE	0	-0.018	-0.015	15.218	-0.026	-0.026	0.000	0.000	0.000	0.000
88	A	99	ASP	-1	-0.844	-0.949	17.990	0.076	0.076	0.000	0.000	0.000	0.000
89	A	100	SER	0	-0.010	-0.025	17.309	-0.001	-0.001	0.000	0.000	0.000	0.000
90	A	101	LEU	0	0.000	0.000	18.253	-0.017	-0.017	0.000	0.000	0.000	0.000
91	A	102	SER	0	-0.002	-0.006	21.322	-0.016	-0.016	0.000	0.000	0.000	0.000
92	A	103	GLN	0	-0.040	-0.022	23.337	0.003	0.003	0.000	0.000	0.000	0.000
93	A	104	MET	0	-0.060	-0.019	21.171	-0.003	-0.003	0.000	0.000	0.000	0.000
94	A	105	LEU	0	-0.007	0.015	24.119	-0.006	-0.006	0.000	0.000	0.000	0.000
95	A	106	ARG	1	0.877	0.932	26.986	-0.059	-0.059	0.000	0.000	0.000	0.000
96	A	107	LYS	1	0.950	0.975	27.012	-0.040	-0.040	0.000	0.000	0.000	0.000
97	A	108	ASN	0	-0.086	-0.040	27.846	-0.005	-0.005	0.000	0.000	0.000	0.000
98	A	109	VAL	0	0.029	0.025	22.220	0.002	0.002	0.000	0.000	0.000	0.000
99	A	110	GLU	-1	-0.891	-0.922	25.346	-0.024	-0.024	0.000	0.000	0.000	0.000
100	A	111	LYS	1	0.841	0.897	26.138	0.085	0.085	0.000	0.000	0.000	0.000
101	A	112	ARG	1	0.818	0.892	27.173	0.009	0.009	0.000	0.000	0.000	0.000
102	A	113	ALA	0	0.040	0.016	27.928	0.004	0.004	0.000	0.000	0.000	0.000
103	A	114	LEU	0	0.005	0.001	20.799	0.009	0.009	0.000	0.000	0.000	0.000
104	A	115	LEU	0	-0.004	-0.012	24.827	0.006	0.006	0.000	0.000	0.000	0.000
105	A	116	GLU	-1	-0.888	-0.930	26.646	0.010	0.010	0.000	0.000	0.000	0.000
106	A	117	ASN	0	-0.044	-0.027	25.537	0.011	0.011	0.000	0.000	0.000	0.000
107	A	118	MET	0	0.011	0.023	21.301	0.009	0.009	0.000	0.000	0.000	0.000
108	A	119	GLU	-1	-0.883	-0.943	21.485	0.081	0.081	0.000	0.000	0.000	0.000
109	A	120	GLY	0	0.012	0.003	21.321	0.020	0.020	0.000	0.000	0.000	0.000
110	A	121	LEU	0	0.008	-0.005	17.019	0.024	0.024	0.000	0.000	0.000	0.000
111	A	122	PHE	0	-0.026	-0.016	17.163	0.013	0.013	0.000	0.000	0.000	0.000
112	A	123	LEU	0	0.004	0.004	16.327	0.032	0.032	0.000	0.000	0.000	0.000
113	A	124	ALA	0	-0.004	-0.009	16.534	0.046	0.046	0.000	0.000	0.000	0.000
114	A	125	VAL	0	-0.041	-0.025	11.521	0.057	0.057	0.000	0.000	0.000	0.000
115	A	126	ASP	-1	-0.806	-0.877	11.624	0.301	0.301	0.000	0.000	0.000	0.000
116	A	127	GLU	-1	-0.789	-0.863	12.645	0.477	0.477	0.000	0.000	0.000	0.000
117	A	128	ILE	0	-0.047	-0.011	9.380	0.086	0.086	0.000	0.000	0.000	0.000
118	A	129	VAL	0	-0.041	-0.027	5.431	0.366	0.366	0.000	0.000	0.000	0.000
119	A	130	ASP	-1	-0.843	-0.909	7.703	0.303	0.303	0.000	0.000	0.000	0.000
120	A	131	GLY	0	-0.018	-0.018	7.008	0.237	0.237	0.000	0.000	0.000	0.000
121	A	132	GLY	0	0.020	0.019	3.608	-0.226	0.013	0.010	-0.068	-0.181	0.000
122	A	133	VAL	0	-0.081	-0.037	2.496	-1.737	-0.005	1.758	-1.677	-1.813	-0.018
123	A	134	ILE	0	0.009	-0.009	4.141	-1.067	-0.723	0.004	-0.108	-0.241	0.001
124	A	135	LEU	0	-0.053	-0.022	6.231	-0.202	-0.202	0.000	0.000	0.000	0.000
125	A	136	GLU	-1	-0.795	-0.895	9.856	0.375	0.375	0.000	0.000	0.000	0.000
126	A	137	SER	0	-0.015	-0.034	10.825	0.148	0.148	0.000	0.000	0.000	0.000
127	A	138	ASP	-1	-0.833	-0.887	12.695	0.186	0.186	0.000	0.000	0.000	0.000
128	A	139	PRO	0	0.054	0.010	16.541	0.007	0.007	0.000	0.000	0.000	0.000
129	A	140	GLN	0	-0.100	-0.064	18.067	-0.044	-0.044	0.000	0.000	0.000	0.000
130	A	141	GLN	0	-0.040	-0.021	17.660	-0.028	-0.028	0.000	0.000	0.000	0.000
131	A	142	VAL	0	-0.005	0.014	15.168	-0.006	-0.006	0.000	0.000	0.000	0.000
132	A	143	VAL	0	0.001	-0.007	17.933	-0.024	-0.024	0.000	0.000	0.000	0.000
133	A	144	HIS	0	-0.027	-0.008	21.473	-0.028	-0.028	0.000	0.000	0.000	0.000
134	A	145	ARG	1	0.806	0.876	14.954	-0.544	-0.544	0.000	0.000	0.000	0.000
135	A	146	VAL	0	0.012	0.008	18.994	-0.011	-0.011	0.000	0.000	0.000	0.000
136	A	147	ALA	0	-0.005	0.004	21.293	-0.017	-0.017	0.000	0.000	0.000	0.000
137	A	148	LEU	0	-0.085	-0.034	23.206	-0.014	-0.014	0.000	0.000	0.000	0.000
138	A	149	ARG	1	0.775	0.866	17.987	-0.305	-0.305	0.000	0.000	0.000	0.000
139	A	150	GLY	0	-0.018	0.005	23.932	-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)