FMO DATABASE

FMODB ID: 98K72

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

Total energy (hartree)

FMO2-HF: Electronic energy	-963768.433656
FMO2-HF: Nuclear repulsion	918797.983497
FMO2-HF: Total energy	-44970.450159
FMO2-MP2: Total energy	-45104.875307

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.
-213.196	-215.994	26.03	-13.243	-9.988	0.138

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 : -0.821 / q_NPA : -0.905

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	0.089	0.044	3.878	-3.352	-1.779	-0.004	-0.675	-0.893	0.002
4	A	6	LYS	1	0.881	0.922	1.781	-147.819	-152.693	26.034	-12.371	-8.789	0.135
5	A	7	ARG	1	0.972	0.979	4.071	-39.792	-39.289	0.000	-0.197	-0.306	0.001
6	A	8	PHE	0	0.008	0.003	6.090	-4.847	-4.847	0.000	0.000	0.000	0.000
7	A	9	LEU	0	0.030	0.006	7.353	-3.010	-3.010	0.000	0.000	0.000	0.000
8	A	10	TYR	0	-0.029	-0.012	8.150	-2.316	-2.316	0.000	0.000	0.000	0.000
9	A	11	LYS	1	0.896	0.938	9.865	-24.097	-24.097	0.000	0.000	0.000	0.000
10	A	12	LYS	1	0.881	0.923	11.816	-19.379	-19.379	0.000	0.000	0.000	0.000
11	A	13	LEU	0	-0.037	0.025	12.286	-1.581	-1.581	0.000	0.000	0.000	0.000
12	A	14	PRO	0	-0.019	-0.024	15.014	-1.091	-1.091	0.000	0.000	0.000	0.000
13	A	15	SER	0	-0.085	-0.043	17.139	-1.021	-1.021	0.000	0.000	0.000	0.000
14	A	16	VAL	0	-0.012	-0.011	19.310	-0.817	-0.817	0.000	0.000	0.000	0.000
15	A	17	GLU	-1	-0.897	-0.946	21.003	12.212	12.212	0.000	0.000	0.000	0.000
16	A	18	GLY	0	0.008	0.001	23.000	-0.267	-0.267	0.000	0.000	0.000	0.000
17	A	19	LEU	0	-0.053	-0.017	16.429	0.005	0.005	0.000	0.000	0.000	0.000
18	A	20	HIS	0	0.014	-0.001	18.007	0.846	0.846	0.000	0.000	0.000	0.000
19	A	21	ALA	0	-0.007	-0.021	14.287	1.313	1.313	0.000	0.000	0.000	0.000
20	A	22	ILE	0	-0.002	0.005	11.755	-1.453	-1.453	0.000	0.000	0.000	0.000
21	A	23	VAL	0	-0.024	-0.014	11.550	2.539	2.539	0.000	0.000	0.000	0.000
22	A	24	VAL	0	0.021	0.019	10.472	-1.913	-1.913	0.000	0.000	0.000	0.000
23	A	25	SER	0	-0.015	-0.014	11.632	2.076	2.076	0.000	0.000	0.000	0.000
24	A	26	ASP	-1	-0.745	-0.866	14.321	17.467	17.467	0.000	0.000	0.000	0.000
25	A	27	ARG	1	0.850	0.885	16.917	-12.648	-12.648	0.000	0.000	0.000	0.000
26	A	28	ASP	-1	-0.866	-0.926	19.742	13.667	13.667	0.000	0.000	0.000	0.000
27	A	29	GLY	0	-0.037	-0.001	17.722	-0.313	-0.313	0.000	0.000	0.000	0.000
28	A	30	VAL	0	-0.033	-0.031	13.774	1.179	1.179	0.000	0.000	0.000	0.000
29	A	31	PRO	0	-0.083	-0.046	10.482	-0.176	-0.176	0.000	0.000	0.000	0.000
30	A	32	VAL	0	0.043	0.021	7.963	1.475	1.475	0.000	0.000	0.000	0.000
31	A	33	ILE	0	-0.004	-0.009	5.557	5.722	5.722	0.000	0.000	0.000	0.000
32	A	34	LYS	1	0.847	0.924	7.557	-28.514	-28.514	0.000	0.000	0.000	0.000
33	A	35	VAL	0	-0.042	-0.006	7.269	4.322	4.322	0.000	0.000	0.000	0.000
34	A	36	ALA	0	0.027	-0.004	9.806	-2.724	-2.724	0.000	0.000	0.000	0.000
35	A	37	ASN	0	0.009	0.010	12.372	0.924	0.924	0.000	0.000	0.000	0.000
36	A	38	ASP	-1	-0.877	-0.945	15.112	17.239	17.239	0.000	0.000	0.000	0.000
37	A	39	ASN	0	-0.021	-0.007	17.803	-1.555	-1.555	0.000	0.000	0.000	0.000
38	A	40	ALA	0	-0.039	-0.013	17.272	-0.702	-0.702	0.000	0.000	0.000	0.000
39	A	41	PRO	0	0.001	-0.011	19.244	-0.069	-0.069	0.000	0.000	0.000	0.000
40	A	42	GLU	-1	-0.788	-0.862	18.296	16.856	16.856	0.000	0.000	0.000	0.000
41	A	43	HIS	0	0.014	-0.013	19.606	0.767	0.767	0.000	0.000	0.000	0.000
42	A	44	ALA	0	-0.011	-0.008	20.831	0.041	0.041	0.000	0.000	0.000	0.000
43	A	45	LEU	0	0.006	0.009	14.953	0.620	0.620	0.000	0.000	0.000	0.000
44	A	46	ARG	1	0.806	0.886	16.583	-14.195	-14.195	0.000	0.000	0.000	0.000
45	A	47	PRO	0	0.002	-0.003	16.558	-0.600	-0.600	0.000	0.000	0.000	0.000
46	A	48	GLY	0	0.087	0.042	18.946	-0.318	-0.318	0.000	0.000	0.000	0.000
47	A	49	PHE	0	-0.013	0.020	21.511	-0.689	-0.689	0.000	0.000	0.000	0.000
48	A	50	LEU	0	0.020	0.005	16.953	-0.410	-0.410	0.000	0.000	0.000	0.000
49	A	51	SER	0	0.029	0.017	20.948	-0.565	-0.565	0.000	0.000	0.000	0.000
50	A	52	THR	0	-0.016	-0.011	22.438	-0.765	-0.765	0.000	0.000	0.000	0.000
51	A	53	PHE	0	-0.002	0.002	22.859	-0.617	-0.617	0.000	0.000	0.000	0.000
52	A	54	ALA	0	0.053	0.043	22.427	-0.440	-0.440	0.000	0.000	0.000	0.000
53	A	55	LEU	0	-0.007	-0.002	24.585	-0.465	-0.465	0.000	0.000	0.000	0.000
54	A	56	ALA	0	0.010	0.001	27.502	-0.483	-0.483	0.000	0.000	0.000	0.000
55	A	57	THR	0	-0.042	-0.037	26.604	-0.343	-0.343	0.000	0.000	0.000	0.000
56	A	58	ASP	-1	-0.849	-0.890	27.546	10.712	10.712	0.000	0.000	0.000	0.000
57	A	59	GLN	0	0.031	-0.003	29.551	-0.264	-0.264	0.000	0.000	0.000	0.000
58	A	60	GLY	0	0.047	0.025	32.120	-0.339	-0.339	0.000	0.000	0.000	0.000
59	A	61	SER	0	-0.043	-0.048	31.908	-0.142	-0.142	0.000	0.000	0.000	0.000
60	A	62	LYS	1	0.807	0.902	30.821	-10.349	-10.349	0.000	0.000	0.000	0.000
61	A	63	LEU	0	-0.028	-0.005	35.685	-0.263	-0.263	0.000	0.000	0.000	0.000
62	A	64	GLY	0	0.013	0.016	37.354	-0.243	-0.243	0.000	0.000	0.000	0.000
63	A	65	LEU	0	-0.055	-0.009	33.801	-0.053	-0.053	0.000	0.000	0.000	0.000
64	A	66	SER	0	0.040	0.019	34.237	0.076	0.076	0.000	0.000	0.000	0.000
65	A	67	LYS	1	0.889	0.946	25.564	-11.420	-11.420	0.000	0.000	0.000	0.000
66	A	68	ASN	0	0.001	-0.007	26.842	0.445	0.445	0.000	0.000	0.000	0.000
67	A	69	LYS	1	0.976	0.976	25.906	-10.083	-10.083	0.000	0.000	0.000	0.000
68	A	70	SER	0	0.048	0.019	24.250	0.560	0.560	0.000	0.000	0.000	0.000
69	A	71	ILE	0	-0.027	0.006	24.729	-0.619	-0.619	0.000	0.000	0.000	0.000
70	A	72	ILE	0	0.017	0.015	24.844	0.568	0.568	0.000	0.000	0.000	0.000
71	A	73	CYS	0	-0.060	-0.022	26.083	-0.563	-0.563	0.000	0.000	0.000	0.000
72	A	74	TYR	0	0.040	-0.004	26.788	0.350	0.350	0.000	0.000	0.000	0.000
73	A	75	TYR	0	0.009	0.003	26.498	-0.162	-0.162	0.000	0.000	0.000	0.000
74	A	76	ASN	0	0.019	0.002	30.047	-0.146	-0.146	0.000	0.000	0.000	0.000
75	A	77	THR	0	0.019	0.012	28.443	-0.074	-0.074	0.000	0.000	0.000	0.000
76	A	78	TYR	0	-0.001	0.004	23.958	0.397	0.397	0.000	0.000	0.000	0.000
77	A	79	GLN	0	-0.001	0.003	23.907	-0.548	-0.548	0.000	0.000	0.000	0.000
78	A	80	VAL	0	-0.010	-0.001	20.949	0.751	0.751	0.000	0.000	0.000	0.000
79	A	81	VAL	0	0.007	0.008	21.214	-0.731	-0.731	0.000	0.000	0.000	0.000
80	A	82	GLN	0	-0.040	-0.034	20.068	0.338	0.338	0.000	0.000	0.000	0.000
81	A	83	PHE	0	0.009	-0.002	19.255	-0.955	-0.955	0.000	0.000	0.000	0.000
82	A	84	ASN	0	0.004	0.000	20.006	0.698	0.698	0.000	0.000	0.000	0.000
83	A	85	ARG	1	0.783	0.859	18.173	-14.926	-14.926	0.000	0.000	0.000	0.000
84	A	86	LEU	0	0.044	0.039	18.845	0.440	0.440	0.000	0.000	0.000	0.000
85	A	87	PRO	0	0.014	0.001	17.404	-0.374	-0.374	0.000	0.000	0.000	0.000
86	A	88	LEU	0	0.014	0.024	13.152	0.154	0.154	0.000	0.000	0.000	0.000
87	A	89	VAL	0	-0.043	-0.022	16.673	-1.331	-1.331	0.000	0.000	0.000	0.000
88	A	90	VAL	0	0.018	0.021	14.343	1.278	1.278	0.000	0.000	0.000	0.000
89	A	91	SER	0	-0.005	-0.013	15.597	-1.800	-1.800	0.000	0.000	0.000	0.000
90	A	92	PHE	0	0.034	0.018	15.839	1.390	1.390	0.000	0.000	0.000	0.000
91	A	93	ILE	0	-0.033	-0.016	16.855	-0.980	-0.980	0.000	0.000	0.000	0.000
92	A	94	ALA	0	0.036	0.031	18.886	0.723	0.723	0.000	0.000	0.000	0.000
93	A	95	SER	0	0.053	0.013	21.642	-0.197	-0.197	0.000	0.000	0.000	0.000
94	A	96	SER	0	-0.067	-0.032	25.099	0.092	0.092	0.000	0.000	0.000	0.000
95	A	97	SER	0	0.029	0.018	28.234	-0.082	-0.082	0.000	0.000	0.000	0.000
96	A	98	ALA	0	0.016	0.035	24.079	-0.172	-0.172	0.000	0.000	0.000	0.000
97	A	99	ASN	0	0.056	0.016	26.180	-0.127	-0.127	0.000	0.000	0.000	0.000
98	A	100	THR	0	0.058	0.007	25.012	0.220	0.220	0.000	0.000	0.000	0.000
99	A	101	GLY	0	0.010	0.018	25.070	0.290	0.290	0.000	0.000	0.000	0.000
100	A	102	LEU	0	0.000	-0.007	23.726	0.143	0.143	0.000	0.000	0.000	0.000
101	A	103	ILE	0	0.023	0.020	19.764	0.535	0.535	0.000	0.000	0.000	0.000
102	A	104	VAL	0	0.003	0.000	20.670	0.558	0.558	0.000	0.000	0.000	0.000
103	A	105	SER	0	-0.050	-0.017	22.361	0.181	0.181	0.000	0.000	0.000	0.000
104	A	106	LEU	0	0.050	0.036	15.991	0.125	0.125	0.000	0.000	0.000	0.000
105	A	107	GLU	-1	-0.828	-0.892	17.686	15.866	15.866	0.000	0.000	0.000	0.000
106	A	108	LYS	1	0.884	0.920	18.356	-12.575	-12.575	0.000	0.000	0.000	0.000
107	A	109	GLU	-1	-0.869	-0.910	17.877	15.899	15.899	0.000	0.000	0.000	0.000
108	A	110	LEU	0	0.001	-0.006	12.617	0.602	0.602	0.000	0.000	0.000	0.000
109	A	111	ALA	0	-0.008	0.006	14.581	0.887	0.887	0.000	0.000	0.000	0.000
110	A	112	PRO	0	-0.011	-0.006	15.867	0.189	0.189	0.000	0.000	0.000	0.000
111	A	113	LEU	0	0.063	0.038	10.712	0.394	0.394	0.000	0.000	0.000	0.000
112	A	114	PHE	0	-0.046	-0.039	11.281	1.452	1.452	0.000	0.000	0.000	0.000
113	A	115	GLU	-1	-0.807	-0.862	13.364	15.536	15.536	0.000	0.000	0.000	0.000
114	A	116	GLU	-1	-0.885	-0.950	11.958	19.777	19.777	0.000	0.000	0.000	0.000
115	A	117	LEU	0	-0.042	-0.019	7.678	0.809	0.809	0.000	0.000	0.000	0.000
116	A	118	ARG	1	0.746	0.828	10.919	-14.866	-14.866	0.000	0.000	0.000	0.000
117	A	119	GLN	0	-0.078	-0.040	13.645	-0.792	-0.792	0.000	0.000	0.000	0.000
118	A	120	VAL	0	-0.030	-0.009	9.752	0.424	0.424	0.000	0.000	0.000	0.000
119	A	121	VAL	0	-0.060	-0.016	12.495	-0.803	-0.803	0.000	0.000	0.000	0.000

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