FMO DATABASE

FMODB ID: R9768

Calculation Name: 3FCD-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3FCD

Chain ID: A

ChEMBL ID:

UniProt ID: Q93AH5

Base Structure: X-ray

Registration Date: 2023-09-20

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	OptHSide
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	117
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-945125.590407
FMO2-HF: Nuclear repulsion	897729.234221
FMO2-HF: Total energy	-47396.356186
FMO2-MP2: Total energy	-47532.663158

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:4:ILE)

Summations of interaction energy for fragment #1(A:4:ILE)

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.
-6.724	-0.591	5.116	-3.341	-7.908	-0.013

Interaction energy analysis for fragmet #1(A:4:ILE)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.058 / 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

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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	6	GLN	0	0.031	0.011	3.537	-2.820	0.105	-0.012	-1.320	-1.592	-0.003
4	A	7	ILE	0	-0.012	-0.008	3.833	-0.164	0.292	0.005	-0.063	-0.399	0.000
5	A	8	THR	0	0.007	0.020	5.874	0.081	0.081	0.000	0.000	0.000	0.000
6	A	9	PRO	0	0.019	0.014	9.420	0.048	0.048	0.000	0.000	0.000	0.000
7	A	10	PHE	0	-0.030	-0.027	12.600	0.027	0.027	0.000	0.000	0.000	0.000
8	A	11	LEU	0	0.006	-0.001	14.671	0.005	0.005	0.000	0.000	0.000	0.000
9	A	12	HIS	1	0.784	0.871	17.249	0.045	0.045	0.000	0.000	0.000	0.000
10	A	13	ILE	0	-0.022	-0.018	21.363	-0.006	-0.006	0.000	0.000	0.000	0.000
11	A	14	PRO	0	0.048	0.019	24.314	0.007	0.007	0.000	0.000	0.000	0.000
12	A	15	ASP	-1	-0.770	-0.879	27.699	-0.009	-0.009	0.000	0.000	0.000	0.000
13	A	16	MET	0	-0.032	-0.028	21.928	-0.008	-0.008	0.000	0.000	0.000	0.000
14	A	17	GLN	0	-0.031	-0.012	26.319	0.001	0.001	0.000	0.000	0.000	0.000
15	A	18	GLU	-1	-0.941	-0.964	28.572	-0.033	-0.033	0.000	0.000	0.000	0.000
16	A	19	ALA	0	-0.022	-0.012	23.506	-0.007	-0.007	0.000	0.000	0.000	0.000
17	A	20	LEU	0	-0.030	-0.026	22.715	-0.007	-0.007	0.000	0.000	0.000	0.000
18	A	21	THR	0	-0.015	-0.008	25.044	-0.003	-0.003	0.000	0.000	0.000	0.000
19	A	22	LEU	0	-0.016	0.003	24.215	-0.005	-0.005	0.000	0.000	0.000	0.000
20	A	23	PHE	0	0.016	-0.015	19.685	-0.009	-0.009	0.000	0.000	0.000	0.000
21	A	24	CYS	0	-0.060	-0.028	21.999	-0.007	-0.007	0.000	0.000	0.000	0.000
22	A	25	ASP	-1	-0.899	-0.946	23.811	-0.036	-0.036	0.000	0.000	0.000	0.000
23	A	26	THR	0	-0.106	-0.042	26.436	0.000	0.000	0.000	0.000	0.000	0.000
24	A	27	LEU	0	-0.089	-0.055	21.430	-0.006	-0.006	0.000	0.000	0.000	0.000
25	A	28	GLY	0	0.008	0.027	22.271	-0.012	-0.012	0.000	0.000	0.000	0.000
26	A	29	PHE	0	-0.041	-0.040	15.315	-0.006	-0.006	0.000	0.000	0.000	0.000
27	A	30	GLU	-1	-0.811	-0.893	19.067	-0.015	-0.015	0.000	0.000	0.000	0.000
28	A	31	LEU	0	-0.027	-0.015	19.010	-0.003	-0.003	0.000	0.000	0.000	0.000
29	A	32	LYS	1	0.763	0.883	16.523	0.020	0.020	0.000	0.000	0.000	0.000
30	A	33	TYR	0	-0.001	-0.004	18.114	0.025	0.025	0.000	0.000	0.000	0.000
31	A	34	ARG	1	0.961	0.980	20.111	-0.030	-0.030	0.000	0.000	0.000	0.000
32	A	35	HIS	0	-0.016	-0.004	22.344	0.003	0.003	0.000	0.000	0.000	0.000
33	A	36	SER	0	-0.011	0.007	23.437	-0.004	-0.004	0.000	0.000	0.000	0.000
34	A	37	ASN	0	0.003	-0.007	24.115	0.003	0.003	0.000	0.000	0.000	0.000
35	A	38	TYR	0	0.035	0.021	15.102	-0.014	-0.014	0.000	0.000	0.000	0.000
36	A	39	ALA	0	0.004	-0.008	19.575	0.009	0.009	0.000	0.000	0.000	0.000
37	A	40	TYR	0	-0.058	-0.038	11.833	-0.021	-0.021	0.000	0.000	0.000	0.000
38	A	41	LEU	0	0.038	-0.004	16.197	0.016	0.016	0.000	0.000	0.000	0.000
39	A	42	GLU	-1	-0.826	-0.898	13.210	-0.033	-0.033	0.000	0.000	0.000	0.000
40	A	43	LEU	0	0.027	0.028	14.722	0.024	0.024	0.000	0.000	0.000	0.000
41	A	44	SER	0	-0.025	-0.028	14.861	-0.030	-0.030	0.000	0.000	0.000	0.000
42	A	45	GLY	0	0.001	-0.003	13.421	-0.036	-0.036	0.000	0.000	0.000	0.000
43	A	46	CYS	0	-0.061	-0.007	10.457	-0.076	-0.076	0.000	0.000	0.000	0.000
44	A	47	GLY	0	0.033	0.011	10.023	0.074	0.074	0.000	0.000	0.000	0.000
45	A	48	LEU	0	-0.033	-0.023	11.461	-0.060	-0.060	0.000	0.000	0.000	0.000
46	A	49	ARG	1	0.799	0.875	9.325	-0.015	-0.015	0.000	0.000	0.000	0.000
47	A	50	LEU	0	0.002	-0.004	15.265	-0.017	-0.017	0.000	0.000	0.000	0.000
48	A	51	LEU	0	-0.019	-0.023	18.811	0.019	0.019	0.000	0.000	0.000	0.000
49	A	52	GLU	-1	-0.882	-0.930	21.066	-0.009	-0.009	0.000	0.000	0.000	0.000
50	A	53	GLU	-1	-0.797	-0.881	22.759	-0.008	-0.008	0.000	0.000	0.000	0.000
51	A	54	PRO	0	-0.016	0.005	26.549	-0.005	-0.005	0.000	0.000	0.000	0.000
52	A	64	ALA	0	-0.041	-0.022	20.918	-0.001	-0.001	0.000	0.000	0.000	0.000
53	A	65	ARG	1	0.821	0.886	19.274	0.048	0.048	0.000	0.000	0.000	0.000
54	A	66	VAL	0	0.028	0.028	13.076	-0.013	-0.013	0.000	0.000	0.000	0.000
55	A	67	ALA	0	0.030	0.042	14.643	0.001	0.001	0.000	0.000	0.000	0.000
56	A	68	ILE	0	-0.010	-0.006	8.412	-0.039	-0.039	0.000	0.000	0.000	0.000
57	A	69	CYS	0	-0.038	-0.005	8.950	0.080	0.080	0.000	0.000	0.000	0.000
58	A	70	ILE	0	-0.008	-0.001	2.735	-0.985	-0.324	0.654	-0.234	-1.080	-0.001
59	A	71	ASP	-1	-0.755	-0.821	5.138	0.207	0.384	-0.001	-0.016	-0.160	0.000
60	A	72	VAL	0	-0.039	-0.036	2.194	-1.708	-0.948	3.609	-1.397	-2.972	-0.008
61	A	73	SER	0	0.057	0.034	3.669	-0.922	-0.623	0.008	-0.076	-0.232	0.000
62	A	74	ASP	-1	-0.858	-0.912	5.423	1.011	1.011	0.000	0.000	0.000	0.000
63	A	75	ILE	0	0.019	0.008	6.175	-0.064	-0.064	0.000	0.000	0.000	0.000
64	A	76	ASP	-1	-0.773	-0.855	7.208	0.328	0.328	0.000	0.000	0.000	0.000
65	A	77	SER	0	-0.019	-0.031	8.291	-0.194	-0.194	0.000	0.000	0.000	0.000
66	A	78	LEU	0	-0.057	-0.024	2.732	-0.898	-0.347	0.850	-0.197	-1.204	-0.001
67	A	79	HIS	0	0.027	0.006	6.012	-0.176	-0.176	0.000	0.000	0.000	0.000
68	A	80	THR	0	-0.001	0.014	8.780	-0.100	-0.100	0.000	0.000	0.000	0.000
69	A	81	LYS	1	0.905	0.954	6.475	0.002	0.002	0.000	0.000	0.000	0.000
70	A	82	LEU	0	-0.026	-0.020	5.157	-0.068	-0.068	0.000	0.000	0.000	0.000
71	A	83	SER	0	0.026	0.001	9.250	-0.028	-0.028	0.000	0.000	0.000	0.000
72	A	84	PRO	0	0.011	0.015	12.436	-0.016	-0.016	0.000	0.000	0.000	0.000
73	A	85	ALA	0	-0.022	-0.011	11.936	-0.012	-0.012	0.000	0.000	0.000	0.000
74	A	86	LEU	0	-0.012	-0.012	9.936	-0.012	-0.012	0.000	0.000	0.000	0.000
75	A	87	GLU	-1	-0.942	-0.970	13.842	0.065	0.065	0.000	0.000	0.000	0.000
76	A	88	ASN	0	-0.131	-0.060	16.788	-0.008	-0.008	0.000	0.000	0.000	0.000
77	A	89	LEU	0	-0.044	-0.003	13.684	-0.013	-0.013	0.000	0.000	0.000	0.000
78	A	90	PRO	0	-0.003	0.000	18.208	0.009	0.009	0.000	0.000	0.000	0.000
79	A	91	ALA	0	0.056	0.018	19.723	0.003	0.003	0.000	0.000	0.000	0.000
80	A	92	ASP	-1	-0.926	-0.959	20.313	0.008	0.008	0.000	0.000	0.000	0.000
81	A	93	GLN	0	-0.086	-0.053	17.789	-0.010	-0.010	0.000	0.000	0.000	0.000
82	A	94	VAL	0	0.001	-0.002	13.784	-0.006	-0.006	0.000	0.000	0.000	0.000
83	A	95	GLU	-1	-0.868	-0.912	14.787	0.098	0.098	0.000	0.000	0.000	0.000
84	A	96	PRO	0	-0.020	-0.017	14.282	0.019	0.019	0.000	0.000	0.000	0.000
85	A	97	LEU	0	-0.025	-0.011	10.420	0.008	0.008	0.000	0.000	0.000	0.000
86	A	98	LYS	1	0.855	0.920	14.278	-0.158	-0.158	0.000	0.000	0.000	0.000
87	A	99	ASN	0	0.016	0.012	15.471	0.055	0.055	0.000	0.000	0.000	0.000
88	A	100	MET	0	-0.010	0.012	16.051	-0.039	-0.039	0.000	0.000	0.000	0.000
89	A	101	PRO	0	-0.028	-0.029	18.386	0.014	0.014	0.000	0.000	0.000	0.000
90	A	102	TYR	0	-0.075	-0.071	15.431	-0.020	-0.020	0.000	0.000	0.000	0.000
91	A	103	GLY	0	0.018	0.016	17.383	0.004	0.004	0.000	0.000	0.000	0.000
92	A	104	GLN	0	-0.012	-0.021	10.424	0.043	0.043	0.000	0.000	0.000	0.000
93	A	105	ARG	1	0.784	0.856	11.967	-0.483	-0.483	0.000	0.000	0.000	0.000
94	A	106	GLU	-1	-0.771	-0.859	10.683	0.304	0.304	0.000	0.000	0.000	0.000
95	A	107	PHE	0	0.015	0.009	6.957	-0.021	-0.021	0.000	0.000	0.000	0.000
96	A	108	GLN	0	-0.054	-0.040	10.523	-0.001	-0.001	0.000	0.000	0.000	0.000
97	A	109	VAL	0	0.036	0.017	10.483	0.006	0.006	0.000	0.000	0.000	0.000
98	A	110	ARG	1	0.877	0.962	12.975	0.012	0.012	0.000	0.000	0.000	0.000
99	A	111	MET	0	-0.026	-0.011	13.096	-0.027	-0.027	0.000	0.000	0.000	0.000
100	A	112	PRO	0	-0.013	-0.031	15.356	0.013	0.013	0.000	0.000	0.000	0.000
101	A	113	ASP	-1	-0.879	-0.928	17.481	-0.113	-0.113	0.000	0.000	0.000	0.000
102	A	114	GLY	0	-0.062	-0.024	19.335	0.009	0.009	0.000	0.000	0.000	0.000
103	A	115	ASP	-1	-0.775	-0.886	16.890	-0.044	-0.044	0.000	0.000	0.000	0.000
104	A	116	TRP	0	-0.032	-0.028	14.825	-0.004	-0.004	0.000	0.000	0.000	0.000
105	A	117	LEU	0	0.004	-0.003	7.357	-0.023	-0.023	0.000	0.000	0.000	0.000
106	A	118	ASN	0	0.015	0.000	10.041	0.009	0.009	0.000	0.000	0.000	0.000
107	A	119	PHE	0	0.015	0.027	3.634	-0.391	-0.087	0.003	-0.038	-0.269	0.000
108	A	120	THR	0	-0.024	-0.053	7.038	0.030	0.030	0.000	0.000	0.000	0.000
109	A	121	ALA	0	0.036	0.013	7.140	0.239	0.239	0.000	0.000	0.000	0.000
110	A	122	PRO	0	0.059	0.046	9.133	-0.141	-0.141	0.000	0.000	0.000	0.000
111	A	123	LEU	0	-0.052	-0.014	12.206	0.081	0.081	0.000	0.000	0.000	0.000
112	A	124	ALA	0	0.044	0.025	13.024	0.012	0.012	0.000	0.000	0.000	0.000
113	A	125	GLU	-1	-0.869	-0.948	14.832	0.469	0.469	0.000	0.000	0.000	0.000
114	A	126	GLY	0	-0.045	-0.020	17.911	-0.013	-0.013	0.000	0.000	0.000	0.000
115	A	127	HIS	0	-0.088	-0.041	18.499	-0.050	-0.050	0.000	0.000	0.000	0.000
116	A	128	HIS	0	-0.006	0.007	20.246	0.016	0.016	0.000	0.000	0.000	0.000
117	A	129	HIS	0	-0.036	-0.014	16.857	-0.019	-0.019	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:4:ILE)