FMO DATABASE

FMODB ID: LZJ39

Calculation Name: 3N7C-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 3N7C

Chain ID: A

ChEMBL ID:

UniProt ID: Q75DJ0

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:

Apendix: None

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
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	113
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-899219.764995
FMO2-HF: Nuclear repulsion	854879.642078
FMO2-HF: Total energy	-44340.122918
FMO2-MP2: Total energy	-44469.381571

3D Structure Molmil

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:503:GLU)

Summations of interaction energy for fragment #1(A:503:GLU)

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.
-319.343	-320.303	44.534	-22.328	-21.246	0.168

Interaction energy analysis for fragmet #1(A:503:GLU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : -1 / q_Mulliken : -0.806 / q_NPA : -0.884

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	505	VAL	0	-0.014	-0.024	3.806	2.861	4.652	-0.008	-0.889	-0.894	0.002
4	A	506	LEU	0	-0.004	0.007	5.821	-3.161	-3.161	0.000	0.000	0.000	0.000
5	A	507	PHE	0	0.027	-0.003	8.456	-2.694	-2.694	0.000	0.000	0.000	0.000
6	A	508	CYS	0	-0.026	-0.033	9.301	3.518	3.518	0.000	0.000	0.000	0.000
7	A	509	GLU	-1	-0.815	-0.873	11.645	15.009	15.009	0.000	0.000	0.000	0.000
8	A	510	LYS	1	0.844	0.927	14.884	-16.058	-16.058	0.000	0.000	0.000	0.000
9	A	511	ALA	0	-0.035	-0.026	16.335	-0.547	-0.547	0.000	0.000	0.000	0.000
10	A	512	LYS	1	0.948	0.971	18.178	-13.006	-13.006	0.000	0.000	0.000	0.000
11	A	513	LEU	0	0.004	0.025	16.249	0.108	0.108	0.000	0.000	0.000	0.000
12	A	514	LEU	0	-0.059	-0.040	19.500	-0.692	-0.692	0.000	0.000	0.000	0.000
13	A	515	ILE	0	0.014	0.004	19.078	0.437	0.437	0.000	0.000	0.000	0.000
14	A	516	PHE	0	0.019	0.009	23.144	-0.477	-0.477	0.000	0.000	0.000	0.000
15	A	517	ASP	-1	-0.940	-0.974	26.482	11.218	11.218	0.000	0.000	0.000	0.000
16	A	518	SER	0	0.015	-0.017	28.968	-0.167	-0.167	0.000	0.000	0.000	0.000
17	A	519	ASP	-1	-0.822	-0.893	32.236	9.256	9.256	0.000	0.000	0.000	0.000
18	A	520	THR	0	-0.023	-0.009	34.300	-0.246	-0.246	0.000	0.000	0.000	0.000
19	A	521	LYS	1	0.817	0.912	32.880	-9.056	-9.056	0.000	0.000	0.000	0.000
20	A	522	GLY	0	0.054	0.031	31.503	-0.213	-0.213	0.000	0.000	0.000	0.000
21	A	523	TYR	0	-0.064	-0.032	23.658	0.097	0.097	0.000	0.000	0.000	0.000
22	A	524	THR	0	0.048	0.024	26.625	-0.010	-0.010	0.000	0.000	0.000	0.000
23	A	525	SER	0	-0.007	-0.019	23.906	0.684	0.684	0.000	0.000	0.000	0.000
24	A	526	ARG	1	0.917	0.960	20.499	-13.643	-13.643	0.000	0.000	0.000	0.000
25	A	527	GLY	0	0.017	0.011	19.835	0.285	0.285	0.000	0.000	0.000	0.000
26	A	528	VAL	0	-0.069	-0.040	19.306	0.037	0.037	0.000	0.000	0.000	0.000
27	A	529	GLY	0	0.076	0.019	15.467	-0.011	-0.011	0.000	0.000	0.000	0.000
28	A	530	GLU	-1	-0.860	-0.909	12.350	18.594	18.594	0.000	0.000	0.000	0.000
29	A	531	LEU	0	-0.046	-0.034	11.639	2.238	2.238	0.000	0.000	0.000	0.000
30	A	532	LYS	1	0.980	0.969	6.996	-33.718	-33.718	0.000	0.000	0.000	0.000
31	A	533	LEU	0	-0.001	0.016	7.746	2.219	2.219	0.000	0.000	0.000	0.000
32	A	534	LEU	0	-0.054	-0.026	2.579	-7.013	-3.835	1.310	-1.630	-2.858	0.019
33	A	535	ARG	1	0.948	0.986	3.527	-28.691	-27.662	0.011	-0.238	-0.801	0.000
34	A	536	LYS	1	0.910	0.946	2.209	-38.895	-37.666	8.521	-5.299	-4.451	-0.030
35	A	537	LYS	1	0.903	0.949	2.675	-48.316	-47.365	1.731	0.126	-2.809	0.009
36	A	538	ASP	-1	-0.828	-0.901	4.413	32.515	32.645	0.000	-0.028	-0.102	0.000
37	A	539	ASP	-1	-0.873	-0.940	6.308	27.865	27.865	0.000	0.000	0.000	0.000
38	A	540	LYS	1	0.843	0.906	5.762	-27.949	-27.949	0.000	0.000	0.000	0.000
39	A	541	GLY	0	0.064	0.032	8.724	-0.111	-0.111	0.000	0.000	0.000	0.000
40	A	542	LYS	1	0.886	0.958	4.740	-39.971	-39.865	-0.001	-0.004	-0.100	0.000
41	A	543	VAL	0	0.025	0.000	5.085	6.810	6.889	-0.001	-0.004	-0.074	0.000
42	A	544	ARG	1	0.773	0.842	1.654	-139.397	-148.850	32.971	-14.362	-9.157	0.168
43	A	545	VAL	0	0.012	0.011	6.138	1.192	1.192	0.000	0.000	0.000	0.000
44	A	546	LEU	0	-0.042	-0.021	5.212	0.245	0.245	0.000	0.000	0.000	0.000
45	A	547	CYS	0	-0.038	0.000	8.245	-2.207	-2.207	0.000	0.000	0.000	0.000
46	A	548	ARG	1	0.899	0.949	8.234	-31.144	-31.144	0.000	0.000	0.000	0.000
47	A	549	SER	0	0.088	0.033	12.391	-0.539	-0.539	0.000	0.000	0.000	0.000
48	A	550	GLU	-1	-0.888	-0.932	16.087	16.377	16.377	0.000	0.000	0.000	0.000
49	A	551	GLY	0	0.012	0.015	18.242	-0.853	-0.853	0.000	0.000	0.000	0.000
50	A	552	MET	0	0.017	0.015	18.793	-0.586	-0.586	0.000	0.000	0.000	0.000
51	A	553	GLY	0	-0.043	-0.025	14.464	0.704	0.704	0.000	0.000	0.000	0.000
52	A	554	HIS	0	0.073	0.038	13.865	2.100	2.100	0.000	0.000	0.000	0.000
53	A	555	VAL	0	-0.030	-0.018	10.456	1.236	1.236	0.000	0.000	0.000	0.000
54	A	556	LEU	0	-0.026	-0.002	12.904	-1.221	-1.221	0.000	0.000	0.000	0.000
55	A	557	LEU	0	0.003	0.002	11.794	-0.923	-0.923	0.000	0.000	0.000	0.000
56	A	558	ASN	0	0.035	0.002	7.051	8.370	8.370	0.000	0.000	0.000	0.000
57	A	559	THR	0	0.004	0.015	8.941	-1.054	-1.054	0.000	0.000	0.000	0.000
58	A	560	SER	0	0.013	0.011	8.140	4.554	4.554	0.000	0.000	0.000	0.000
59	A	561	VAL	0	0.006	0.006	8.973	-2.509	-2.509	0.000	0.000	0.000	0.000
60	A	562	VAL	0	0.009	0.012	11.010	0.420	0.420	0.000	0.000	0.000	0.000
61	A	563	LYS	1	0.909	0.923	14.109	-18.513	-18.513	0.000	0.000	0.000	0.000
62	A	564	SER	0	-0.005	-0.009	16.201	-0.476	-0.476	0.000	0.000	0.000	0.000
63	A	565	PHE	0	-0.009	0.014	16.771	-0.885	-0.885	0.000	0.000	0.000	0.000
64	A	566	LYS	1	0.984	0.994	18.260	-12.306	-12.306	0.000	0.000	0.000	0.000
65	A	567	TYR	0	0.064	0.044	14.455	-0.022	-0.022	0.000	0.000	0.000	0.000
66	A	568	GLN	0	0.002	-0.009	18.653	-0.319	-0.319	0.000	0.000	0.000	0.000
67	A	569	PRO	0	0.058	0.035	21.654	0.278	0.278	0.000	0.000	0.000	0.000
68	A	570	ILE	0	-0.006	-0.011	23.905	-0.170	-0.170	0.000	0.000	0.000	0.000
69	A	571	ASP	-1	-0.782	-0.883	26.410	10.358	10.358	0.000	0.000	0.000	0.000
70	A	572	ALA	0	0.010	-0.001	28.335	0.307	0.307	0.000	0.000	0.000	0.000
71	A	573	ASP	-1	-0.840	-0.918	30.133	9.554	9.554	0.000	0.000	0.000	0.000
72	A	574	ASN	0	-0.119	-0.067	27.718	0.076	0.076	0.000	0.000	0.000	0.000
73	A	575	GLU	-1	-0.799	-0.918	24.078	12.444	12.444	0.000	0.000	0.000	0.000
74	A	576	ASN	0	-0.019	-0.023	22.871	0.330	0.330	0.000	0.000	0.000	0.000
75	A	577	LEU	0	-0.039	-0.011	22.853	0.454	0.454	0.000	0.000	0.000	0.000
76	A	578	ILE	0	-0.020	0.001	18.059	-0.388	-0.388	0.000	0.000	0.000	0.000
77	A	579	LYS	1	0.878	0.943	20.392	-12.370	-12.370	0.000	0.000	0.000	0.000
78	A	580	TRP	0	0.009	-0.021	11.539	0.411	0.411	0.000	0.000	0.000	0.000
79	A	581	PRO	0	-0.004	0.003	17.964	-0.089	-0.089	0.000	0.000	0.000	0.000
80	A	582	ILE	0	-0.045	-0.025	14.399	1.705	1.705	0.000	0.000	0.000	0.000
81	A	583	ILE	0	-0.005	0.008	16.944	-1.069	-1.069	0.000	0.000	0.000	0.000
82	A	584	THR	0	0.008	-0.020	17.607	1.445	1.445	0.000	0.000	0.000	0.000
83	A	585	ASP	-1	-0.847	-0.910	20.044	13.568	13.568	0.000	0.000	0.000	0.000
84	A	586	GLY	0	-0.006	-0.011	21.437	-0.605	-0.605	0.000	0.000	0.000	0.000
85	A	587	LYS	1	0.854	0.924	23.091	-13.826	-13.826	0.000	0.000	0.000	0.000
86	A	588	LEU	0	-0.048	-0.024	20.705	0.720	0.720	0.000	0.000	0.000	0.000
87	A	589	GLU	-1	-0.831	-0.894	20.711	14.200	14.200	0.000	0.000	0.000	0.000
88	A	590	THR	0	-0.006	-0.004	20.731	0.683	0.683	0.000	0.000	0.000	0.000
89	A	591	PHE	0	0.022	0.022	16.303	-0.287	-0.287	0.000	0.000	0.000	0.000
90	A	592	ILE	0	-0.008	-0.011	20.201	-0.113	-0.113	0.000	0.000	0.000	0.000
91	A	593	ILE	0	0.012	0.013	14.927	0.332	0.332	0.000	0.000	0.000	0.000
92	A	594	LYS	1	0.938	0.978	19.200	-12.550	-12.550	0.000	0.000	0.000	0.000
93	A	595	VAL	0	0.039	0.033	18.020	0.515	0.515	0.000	0.000	0.000	0.000
94	A	596	LYS	1	0.777	0.864	19.509	-16.008	-16.008	0.000	0.000	0.000	0.000
95	A	597	GLN	0	0.040	0.017	22.785	-0.676	-0.676	0.000	0.000	0.000	0.000
96	A	598	LYS	1	0.865	0.937	22.854	-10.261	-10.261	0.000	0.000	0.000	0.000
97	A	599	ALA	0	0.010	0.007	23.207	0.171	0.171	0.000	0.000	0.000	0.000
98	A	600	ASP	-1	-0.757	-0.880	18.852	15.081	15.081	0.000	0.000	0.000	0.000
99	A	601	GLY	0	0.007	0.017	18.339	0.940	0.940	0.000	0.000	0.000	0.000
100	A	602	ARG	1	0.883	0.924	19.591	-11.607	-11.607	0.000	0.000	0.000	0.000
101	A	603	ARG	1	0.880	0.937	16.052	-15.538	-15.538	0.000	0.000	0.000	0.000
102	A	604	LEU	0	-0.021	0.014	13.609	0.822	0.822	0.000	0.000	0.000	0.000
103	A	605	VAL	0	0.031	-0.002	15.272	0.892	0.892	0.000	0.000	0.000	0.000
104	A	606	GLY	0	-0.002	0.004	17.413	0.195	0.195	0.000	0.000	0.000	0.000
105	A	607	ALA	0	0.000	-0.001	12.197	0.324	0.324	0.000	0.000	0.000	0.000
106	A	608	VAL	0	-0.023	-0.017	12.474	1.277	1.277	0.000	0.000	0.000	0.000
107	A	609	ALA	0	0.024	0.014	13.921	0.362	0.362	0.000	0.000	0.000	0.000
108	A	610	ASP	-1	-0.942	-0.960	13.360	19.773	19.773	0.000	0.000	0.000	0.000
109	A	611	ALA	0	-0.002	-0.014	10.371	0.468	0.468	0.000	0.000	0.000	0.000
110	A	612	GLN	0	-0.056	-0.047	12.295	-0.060	-0.060	0.000	0.000	0.000	0.000
111	A	613	GLN	0	-0.070	-0.040	14.504	-1.224	-1.224	0.000	0.000	0.000	0.000
112	A	614	ALA	0	0.005	0.014	12.361	-0.423	-0.423	0.000	0.000	0.000	0.000
113	A	615	MET	0	-0.057	0.008	10.725	-1.114	-1.114	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:503:GLU)