FMO DATABASE

FMODB ID: 3J8ZL

Calculation Name: 3CPT-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3CPT

Chain ID: A

ChEMBL ID:

UniProt ID: Q9JHS3

Base Structure: X-ray

Registration Date: 2023-09-23

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	119
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-963959.0456
FMO2-HF: Nuclear repulsion	918989.508699
FMO2-HF: Total energy	-44969.536901
FMO2-MP2: Total energy	-45104.019147

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:3:ASP)

Summations of interaction energy for fragment #1(A:3:ASP)

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.
-124.747	-120.091	0.821	-2.369	-3.109	0.014

Interaction energy analysis for fragmet #1(A:3:ASP)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : -1 / q_Mulliken : -0.901 / q_NPA : -0.955

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

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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	5	LEU	0	0.074	0.034	3.636	-6.379	-4.046	0.010	-1.074	-1.269	0.005
4	A	6	LYS	1	0.968	0.989	2.477	-60.504	-58.613	0.811	-1.094	-1.609	0.008
5	A	7	ARG	1	0.986	0.985	3.925	-37.467	-37.035	0.000	-0.201	-0.231	0.001
6	A	8	PHE	0	0.012	0.006	5.784	-4.619	-4.619	0.000	0.000	0.000	0.000
7	A	9	LEU	0	0.038	0.008	7.856	-2.969	-2.969	0.000	0.000	0.000	0.000
8	A	10	TYR	0	-0.017	0.000	8.159	-2.332	-2.332	0.000	0.000	0.000	0.000
9	A	11	LYS	1	0.889	0.928	9.806	-23.612	-23.612	0.000	0.000	0.000	0.000
10	A	12	LYS	1	0.968	0.992	11.851	-18.967	-18.967	0.000	0.000	0.000	0.000
11	A	13	LEU	0	-0.044	0.012	12.719	-1.320	-1.320	0.000	0.000	0.000	0.000
12	A	14	PRO	0	-0.017	-0.018	14.809	-0.967	-0.967	0.000	0.000	0.000	0.000
13	A	15	SER	0	-0.089	-0.043	17.403	-0.914	-0.914	0.000	0.000	0.000	0.000
14	A	16	VAL	0	-0.003	0.002	19.346	-0.749	-0.749	0.000	0.000	0.000	0.000
15	A	17	GLU	-1	-0.903	-0.949	20.757	11.738	11.738	0.000	0.000	0.000	0.000
16	A	18	GLY	0	0.003	-0.004	22.377	-0.294	-0.294	0.000	0.000	0.000	0.000
17	A	19	LEU	0	-0.041	-0.004	16.481	-0.032	-0.032	0.000	0.000	0.000	0.000
18	A	20	HIS	0	0.020	-0.001	17.670	0.748	0.748	0.000	0.000	0.000	0.000
19	A	21	ALA	0	-0.003	-0.015	14.131	1.098	1.098	0.000	0.000	0.000	0.000
20	A	22	ILE	0	0.003	0.019	11.979	-1.192	-1.192	0.000	0.000	0.000	0.000
21	A	23	VAL	0	-0.025	-0.023	11.790	2.229	2.229	0.000	0.000	0.000	0.000
22	A	24	VAL	0	0.028	0.029	10.442	-1.640	-1.640	0.000	0.000	0.000	0.000
23	A	25	SER	0	-0.004	-0.006	11.524	1.769	1.769	0.000	0.000	0.000	0.000
24	A	26	ASP	-1	-0.744	-0.867	14.096	16.771	16.771	0.000	0.000	0.000	0.000
25	A	27	ARG	1	0.932	0.928	16.601	-12.822	-12.822	0.000	0.000	0.000	0.000
26	A	28	ASP	-1	-0.862	-0.906	19.234	13.277	13.277	0.000	0.000	0.000	0.000
27	A	29	GLY	0	-0.097	-0.043	17.746	-0.123	-0.123	0.000	0.000	0.000	0.000
28	A	30	VAL	0	-0.012	-0.024	13.903	0.999	0.999	0.000	0.000	0.000	0.000
29	A	31	PRO	0	-0.085	-0.037	10.778	0.138	0.138	0.000	0.000	0.000	0.000
30	A	32	VAL	0	0.028	0.011	7.940	0.994	0.994	0.000	0.000	0.000	0.000
31	A	33	ILE	0	-0.002	-0.004	5.503	4.842	4.842	0.000	0.000	0.000	0.000
32	A	34	LYS	1	0.940	0.974	7.705	-26.239	-26.239	0.000	0.000	0.000	0.000
33	A	35	VAL	0	-0.079	-0.037	7.096	3.582	3.582	0.000	0.000	0.000	0.000
34	A	36	ALA	0	0.024	-0.004	9.715	-2.080	-2.080	0.000	0.000	0.000	0.000
35	A	37	ASN	0	0.020	0.012	12.656	0.793	0.793	0.000	0.000	0.000	0.000
36	A	38	ASP	-1	-0.902	-0.956	15.095	15.982	15.982	0.000	0.000	0.000	0.000
37	A	39	ASN	0	0.022	0.019	17.994	-1.140	-1.140	0.000	0.000	0.000	0.000
38	A	40	ALA	0	-0.079	-0.033	17.282	-0.691	-0.691	0.000	0.000	0.000	0.000
39	A	41	PRO	0	0.017	0.006	19.213	0.030	0.030	0.000	0.000	0.000	0.000
40	A	42	GLU	-1	-0.865	-0.938	19.306	16.498	16.498	0.000	0.000	0.000	0.000
41	A	43	HIS	0	-0.097	-0.062	19.949	0.687	0.687	0.000	0.000	0.000	0.000
42	A	44	ALA	0	-0.013	-0.008	20.865	0.021	0.021	0.000	0.000	0.000	0.000
43	A	45	LEU	0	0.012	0.003	14.933	0.610	0.610	0.000	0.000	0.000	0.000
44	A	46	ARG	1	0.904	0.954	16.853	-13.561	-13.561	0.000	0.000	0.000	0.000
45	A	47	PRO	0	0.030	0.022	16.856	-0.510	-0.510	0.000	0.000	0.000	0.000
46	A	48	GLY	0	0.071	0.036	19.027	-0.422	-0.422	0.000	0.000	0.000	0.000
47	A	49	PHE	0	-0.004	0.006	21.714	-0.577	-0.577	0.000	0.000	0.000	0.000
48	A	50	LEU	0	0.015	-0.006	16.902	-0.427	-0.427	0.000	0.000	0.000	0.000
49	A	51	SER	0	0.026	0.009	20.913	-0.534	-0.534	0.000	0.000	0.000	0.000
50	A	52	THR	0	0.004	0.006	22.249	-0.659	-0.659	0.000	0.000	0.000	0.000
51	A	53	PHE	0	-0.039	-0.014	22.950	-0.533	-0.533	0.000	0.000	0.000	0.000
52	A	54	ALA	0	0.037	0.020	22.408	-0.392	-0.392	0.000	0.000	0.000	0.000
53	A	55	LEU	0	0.009	0.013	24.550	-0.373	-0.373	0.000	0.000	0.000	0.000
54	A	56	ALA	0	-0.001	0.001	27.328	-0.442	-0.442	0.000	0.000	0.000	0.000
55	A	57	THR	0	-0.047	-0.037	26.517	-0.326	-0.326	0.000	0.000	0.000	0.000
56	A	58	ASP	-1	-0.939	-0.958	27.576	10.100	10.100	0.000	0.000	0.000	0.000
57	A	59	GLN	0	0.019	-0.011	29.453	-0.298	-0.298	0.000	0.000	0.000	0.000
58	A	60	GLY	0	0.011	0.011	32.165	-0.328	-0.328	0.000	0.000	0.000	0.000
59	A	61	SER	0	-0.032	-0.034	31.905	-0.135	-0.135	0.000	0.000	0.000	0.000
60	A	62	LYS	1	0.872	0.954	31.588	-9.821	-9.821	0.000	0.000	0.000	0.000
61	A	63	LEU	0	-0.031	-0.017	35.611	-0.261	-0.261	0.000	0.000	0.000	0.000
62	A	64	GLY	0	0.003	0.013	37.260	-0.252	-0.252	0.000	0.000	0.000	0.000
63	A	65	LEU	0	-0.061	-0.011	33.309	-0.052	-0.052	0.000	0.000	0.000	0.000
64	A	66	SER	0	0.019	0.010	34.843	0.122	0.122	0.000	0.000	0.000	0.000
65	A	67	LYS	1	0.972	0.982	26.522	-10.718	-10.718	0.000	0.000	0.000	0.000
66	A	68	ASN	0	0.028	0.007	26.956	0.327	0.327	0.000	0.000	0.000	0.000
67	A	69	LYS	1	0.950	0.968	25.924	-9.881	-9.881	0.000	0.000	0.000	0.000
68	A	70	SER	0	0.042	0.012	24.394	0.539	0.539	0.000	0.000	0.000	0.000
69	A	71	ILE	0	0.006	0.017	25.043	-0.566	-0.566	0.000	0.000	0.000	0.000
70	A	72	ILE	0	0.004	0.003	25.178	0.546	0.546	0.000	0.000	0.000	0.000
71	A	73	CYS	0	-0.058	-0.007	26.524	-0.532	-0.532	0.000	0.000	0.000	0.000
72	A	74	TYR	0	0.026	-0.019	27.165	0.384	0.384	0.000	0.000	0.000	0.000
73	A	75	TYR	0	-0.011	-0.012	26.887	-0.397	-0.397	0.000	0.000	0.000	0.000
74	A	76	ASN	0	0.022	0.000	30.071	-0.140	-0.140	0.000	0.000	0.000	0.000
75	A	77	THR	0	0.007	-0.003	27.776	-0.015	-0.015	0.000	0.000	0.000	0.000
76	A	78	TYR	0	0.036	0.031	23.867	0.261	0.261	0.000	0.000	0.000	0.000
77	A	79	GLN	0	0.013	0.023	24.099	-0.467	-0.467	0.000	0.000	0.000	0.000
78	A	80	VAL	0	-0.022	-0.012	21.319	0.666	0.666	0.000	0.000	0.000	0.000
79	A	81	VAL	0	0.003	0.011	21.703	-0.610	-0.610	0.000	0.000	0.000	0.000
80	A	82	GLN	0	-0.024	-0.027	20.067	0.365	0.365	0.000	0.000	0.000	0.000
81	A	83	PHE	0	0.004	-0.002	19.512	-0.888	-0.888	0.000	0.000	0.000	0.000
82	A	84	ASN	0	0.000	-0.003	19.964	0.998	0.998	0.000	0.000	0.000	0.000
83	A	85	ARG	1	0.838	0.916	18.003	-14.291	-14.291	0.000	0.000	0.000	0.000
84	A	86	LEU	0	0.012	0.036	18.705	0.472	0.472	0.000	0.000	0.000	0.000
85	A	87	PRO	0	0.014	-0.018	17.134	-0.379	-0.379	0.000	0.000	0.000	0.000
86	A	88	LEU	0	-0.002	0.015	13.148	0.237	0.237	0.000	0.000	0.000	0.000
87	A	89	VAL	0	-0.008	-0.002	16.275	-1.160	-1.160	0.000	0.000	0.000	0.000
88	A	90	VAL	0	0.005	0.015	14.535	1.153	1.153	0.000	0.000	0.000	0.000
89	A	91	SER	0	0.010	0.002	15.936	-1.577	-1.577	0.000	0.000	0.000	0.000
90	A	92	PHE	0	0.006	0.007	16.294	1.257	1.257	0.000	0.000	0.000	0.000
91	A	93	ILE	0	-0.010	-0.005	17.134	-0.904	-0.904	0.000	0.000	0.000	0.000
92	A	94	ALA	0	0.033	0.019	19.066	0.562	0.562	0.000	0.000	0.000	0.000
93	A	95	SER	0	0.050	0.022	21.738	-0.294	-0.294	0.000	0.000	0.000	0.000
94	A	96	SER	0	-0.033	-0.022	24.960	0.068	0.068	0.000	0.000	0.000	0.000
95	A	97	SER	0	0.006	0.000	28.033	-0.056	-0.056	0.000	0.000	0.000	0.000
96	A	98	ALA	0	0.010	0.032	24.228	-0.147	-0.147	0.000	0.000	0.000	0.000
97	A	99	ASN	0	0.045	0.007	26.287	-0.219	-0.219	0.000	0.000	0.000	0.000
98	A	100	THR	0	0.065	0.020	25.548	0.223	0.223	0.000	0.000	0.000	0.000
99	A	101	GLY	0	0.012	0.014	25.490	0.310	0.310	0.000	0.000	0.000	0.000
100	A	102	LEU	0	-0.007	-0.009	23.733	0.149	0.149	0.000	0.000	0.000	0.000
101	A	103	ILE	0	0.026	0.019	20.197	0.528	0.528	0.000	0.000	0.000	0.000
102	A	104	VAL	0	-0.009	-0.001	21.100	0.469	0.469	0.000	0.000	0.000	0.000
103	A	105	SER	0	-0.058	-0.035	22.632	0.033	0.033	0.000	0.000	0.000	0.000
104	A	106	LEU	0	0.068	0.019	16.229	0.226	0.226	0.000	0.000	0.000	0.000
105	A	107	GLU	-1	-0.874	-0.944	17.772	15.317	15.317	0.000	0.000	0.000	0.000
106	A	108	LYS	1	0.922	0.979	18.383	-12.030	-12.030	0.000	0.000	0.000	0.000
107	A	109	GLU	-1	-0.978	-0.997	17.390	15.584	15.584	0.000	0.000	0.000	0.000
108	A	110	LEU	0	-0.033	-0.023	12.991	0.619	0.619	0.000	0.000	0.000	0.000
109	A	111	ALA	0	0.005	0.016	14.598	0.902	0.902	0.000	0.000	0.000	0.000
110	A	112	PRO	0	-0.001	-0.004	16.101	0.373	0.373	0.000	0.000	0.000	0.000
111	A	113	LEU	0	0.061	0.037	10.554	0.494	0.494	0.000	0.000	0.000	0.000
112	A	114	PHE	0	-0.035	-0.028	11.625	1.169	1.169	0.000	0.000	0.000	0.000
113	A	115	GLU	-1	-0.908	-0.960	13.228	15.392	15.392	0.000	0.000	0.000	0.000
114	A	116	GLU	-1	-0.900	-0.955	11.454	19.574	19.574	0.000	0.000	0.000	0.000
115	A	117	LEU	0	-0.038	-0.014	7.613	0.801	0.801	0.000	0.000	0.000	0.000
116	A	118	ARG	1	0.821	0.902	11.060	-14.971	-14.971	0.000	0.000	0.000	0.000
117	A	119	GLN	0	-0.064	-0.030	13.718	-0.876	-0.876	0.000	0.000	0.000	0.000
118	A	120	VAL	0	-0.035	0.007	9.814	1.008	1.008	0.000	0.000	0.000	0.000
119	A	121	VAL	0	-0.049	-0.021	12.966	-0.708	-0.708	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:3:ASP)