FMO DATABASE

FMODB ID: YYJ82

Calculation Name: 2FI0-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2FI0

Chain ID: A

ChEMBL ID:

UniProt ID: Q8CZ42

Base Structure: X-ray

Registration Date: 2023-06-19

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	79
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-491256.141247
FMO2-HF: Nuclear repulsion	461114.108391
FMO2-HF: Total energy	-30142.032856
FMO2-MP2: Total energy	-30229.584248

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:VAL)

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

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.
-4.174	-1.041	0.332	-1.282	-2.183	0.003

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.005 / q_NPA : -0.008

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	MET	0	-0.054	-0.024	2.773	-1.404	1.594	0.333	-1.273	-2.059	0.003
4	A	6	ASP	-1	-0.893	-0.943	4.822	-1.280	-1.145	-0.001	-0.009	-0.124	0.000
5	A	7	ASN	0	-0.024	-0.020	8.219	-0.036	-0.036	0.000	0.000	0.000	0.000
6	A	8	ILE	0	0.042	0.031	7.195	0.101	0.101	0.000	0.000	0.000	0.000
7	A	9	ILE	0	-0.020	-0.009	11.470	0.134	0.134	0.000	0.000	0.000	0.000
8	A	10	ASP	-1	-0.775	-0.858	15.016	-0.303	-0.303	0.000	0.000	0.000	0.000
9	A	11	VAL	0	-0.028	-0.034	16.590	0.029	0.029	0.000	0.000	0.000	0.000
10	A	12	SER	0	-0.141	-0.105	19.127	0.047	0.047	0.000	0.000	0.000	0.000
11	A	13	ILE	0	0.018	0.028	18.438	0.024	0.024	0.000	0.000	0.000	0.000
12	A	14	PRO	0	-0.028	-0.020	21.973	-0.003	-0.003	0.000	0.000	0.000	0.000
13	A	15	VAL	0	0.036	-0.004	23.396	-0.022	-0.022	0.000	0.000	0.000	0.000
14	A	16	ALA	0	-0.058	-0.043	23.718	-0.021	-0.021	0.000	0.000	0.000	0.000
15	A	17	GLU	-1	-0.878	-0.938	21.315	-0.259	-0.259	0.000	0.000	0.000	0.000
16	A	18	VAL	0	-0.028	-0.008	18.429	-0.036	-0.036	0.000	0.000	0.000	0.000
17	A	19	VAL	0	-0.036	-0.029	19.515	-0.030	-0.030	0.000	0.000	0.000	0.000
18	A	20	ASP	-1	-0.960	-0.977	21.698	-0.281	-0.281	0.000	0.000	0.000	0.000
19	A	21	LYS	1	0.886	0.957	13.270	0.647	0.647	0.000	0.000	0.000	0.000
20	A	22	HIS	0	-0.030	-0.017	13.074	-0.058	-0.058	0.000	0.000	0.000	0.000
21	A	23	PRO	0	0.014	0.011	18.153	0.035	0.035	0.000	0.000	0.000	0.000
22	A	24	GLU	-1	-0.813	-0.907	17.169	-0.560	-0.560	0.000	0.000	0.000	0.000
23	A	25	VAL	0	0.011	0.023	18.647	0.022	0.022	0.000	0.000	0.000	0.000
24	A	26	LEU	0	-0.064	-0.032	20.592	0.039	0.039	0.000	0.000	0.000	0.000
25	A	27	GLU	-1	-0.935	-0.978	23.965	-0.263	-0.263	0.000	0.000	0.000	0.000
26	A	28	ILE	0	0.029	0.019	19.246	0.023	0.023	0.000	0.000	0.000	0.000
27	A	29	LEU	0	0.001	-0.003	21.784	0.031	0.031	0.000	0.000	0.000	0.000
28	A	30	VAL	0	-0.061	-0.030	24.867	0.028	0.028	0.000	0.000	0.000	0.000
29	A	31	GLU	-1	-0.786	-0.872	26.631	-0.162	-0.162	0.000	0.000	0.000	0.000
30	A	32	LEU	0	-0.064	-0.031	22.534	0.011	0.011	0.000	0.000	0.000	0.000
31	A	33	GLY	0	0.017	0.020	27.083	0.006	0.006	0.000	0.000	0.000	0.000
32	A	34	PHE	0	-0.011	-0.008	25.786	0.009	0.009	0.000	0.000	0.000	0.000
33	A	35	LYS	1	0.851	0.913	29.444	0.165	0.165	0.000	0.000	0.000	0.000
34	A	36	PRO	0	-0.010	-0.014	31.710	0.000	0.000	0.000	0.000	0.000	0.000
35	A	37	LEU	0	-0.035	-0.015	28.289	0.004	0.004	0.000	0.000	0.000	0.000
36	A	38	ALA	0	0.088	0.058	29.770	-0.013	-0.013	0.000	0.000	0.000	0.000
37	A	39	ASN	0	0.008	-0.001	30.927	-0.006	-0.006	0.000	0.000	0.000	0.000
38	A	40	PRO	0	0.067	0.020	30.960	-0.001	-0.001	0.000	0.000	0.000	0.000
39	A	41	LEU	0	0.041	0.037	31.992	-0.002	-0.002	0.000	0.000	0.000	0.000
40	A	42	MET	0	0.015	0.016	34.044	0.005	0.005	0.000	0.000	0.000	0.000
41	A	43	ARG	1	0.935	0.960	26.331	0.238	0.238	0.000	0.000	0.000	0.000
42	A	44	ASN	0	-0.043	-0.026	29.181	-0.011	-0.011	0.000	0.000	0.000	0.000
43	A	45	THR	0	-0.039	-0.031	31.270	0.009	0.009	0.000	0.000	0.000	0.000
44	A	46	VAL	0	-0.015	-0.012	32.421	0.000	0.000	0.000	0.000	0.000	0.000
45	A	47	GLY	0	0.044	0.014	29.150	0.000	0.000	0.000	0.000	0.000	0.000
46	A	48	ARG	1	0.961	0.986	27.785	0.171	0.171	0.000	0.000	0.000	0.000
47	A	49	LYS	1	0.892	0.954	29.258	0.120	0.120	0.000	0.000	0.000	0.000
48	A	50	VAL	0	-0.047	-0.001	28.573	0.007	0.007	0.000	0.000	0.000	0.000
49	A	51	SER	0	0.087	0.040	23.602	-0.012	-0.012	0.000	0.000	0.000	0.000
50	A	52	LEU	0	0.056	0.015	20.213	0.016	0.016	0.000	0.000	0.000	0.000
51	A	53	LYS	1	0.845	0.910	21.412	0.177	0.177	0.000	0.000	0.000	0.000
52	A	54	GLN	0	-0.014	0.013	24.707	0.005	0.005	0.000	0.000	0.000	0.000
53	A	55	GLY	0	0.038	0.005	27.593	0.011	0.011	0.000	0.000	0.000	0.000
54	A	56	SER	0	-0.034	-0.008	25.706	0.010	0.010	0.000	0.000	0.000	0.000
55	A	57	LYS	1	0.909	0.957	26.789	0.127	0.127	0.000	0.000	0.000	0.000
56	A	58	LEU	0	-0.044	-0.016	30.544	0.008	0.008	0.000	0.000	0.000	0.000
57	A	59	ALA	0	-0.031	-0.013	30.180	0.006	0.006	0.000	0.000	0.000	0.000
58	A	60	GLY	0	0.002	0.016	31.972	0.003	0.003	0.000	0.000	0.000	0.000
59	A	61	THR	0	-0.062	-0.034	26.495	0.008	0.008	0.000	0.000	0.000	0.000
60	A	62	PRO	0	-0.013	-0.015	26.649	-0.005	-0.005	0.000	0.000	0.000	0.000
61	A	63	MET	0	0.050	0.024	21.433	-0.022	-0.022	0.000	0.000	0.000	0.000
62	A	64	ASP	-1	-0.846	-0.918	21.488	-0.145	-0.145	0.000	0.000	0.000	0.000
63	A	65	LYS	1	0.865	0.938	21.456	0.189	0.189	0.000	0.000	0.000	0.000
64	A	66	ILE	0	0.005	0.003	20.450	-0.018	-0.018	0.000	0.000	0.000	0.000
65	A	67	VAL	0	0.031	0.016	16.206	-0.032	-0.032	0.000	0.000	0.000	0.000
66	A	68	ARG	1	0.991	0.998	17.114	0.125	0.125	0.000	0.000	0.000	0.000
67	A	69	THR	0	-0.043	-0.033	18.203	-0.013	-0.013	0.000	0.000	0.000	0.000
68	A	70	LEU	0	0.011	0.013	16.201	-0.019	-0.019	0.000	0.000	0.000	0.000
69	A	71	GLU	-1	-0.863	-0.932	12.990	-0.413	-0.413	0.000	0.000	0.000	0.000
70	A	72	ALA	0	-0.093	-0.047	13.898	-0.055	-0.055	0.000	0.000	0.000	0.000
71	A	73	ASN	0	-0.109	-0.067	16.341	0.029	0.029	0.000	0.000	0.000	0.000
72	A	74	GLY	0	0.007	0.012	12.038	-0.013	-0.013	0.000	0.000	0.000	0.000
73	A	75	TYR	0	-0.091	-0.072	11.091	-0.205	-0.205	0.000	0.000	0.000	0.000
74	A	76	GLU	-1	-0.899	-0.937	7.551	-1.127	-1.127	0.000	0.000	0.000	0.000
75	A	77	VAL	0	-0.027	-0.014	10.625	0.050	0.050	0.000	0.000	0.000	0.000
76	A	78	ILE	0	0.021	0.008	11.086	0.055	0.055	0.000	0.000	0.000	0.000
77	A	79	GLY	0	0.076	0.032	14.191	0.014	0.014	0.000	0.000	0.000	0.000
78	A	80	LEU	0	-0.007	-0.013	15.902	0.025	0.025	0.000	0.000	0.000	0.000
79	A	81	ASP	-1	-0.881	-0.918	19.107	-0.107	-0.107	0.000	0.000	0.000	0.000

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