FMO DATABASE

FMODB ID: JQM89

Calculation Name: 4V2B-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4V2B

Chain ID: A

ChEMBL ID:

UniProt ID: F1LW30

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	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	108
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-859649.865689
FMO2-HF: Nuclear repulsion	814832.64827
FMO2-HF: Total energy	-44817.21742
FMO2-MP2: Total energy	-44946.486688

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:47:ALA)

Summations of interaction energy for fragment #1(A:47:ALA)

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.
4.218	0.237	1.24	5.139	-2.398	-0.021

Interaction energy analysis for fragmet #1(A:47:ALA)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.044 / q_NPA : 0.040

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	49	GLY	0	-0.013	-0.006	2.609	7.334	1.682	0.910	6.031	-1.290	-0.010
4	A	50	THR	0	0.022	-0.010	2.680	-3.761	-2.098	0.331	-0.892	-1.102	-0.011
5	A	51	LEU	0	0.016	0.009	5.211	-0.074	-0.066	-0.001	0.000	-0.006	0.000
6	A	52	PRO	0	-0.043	-0.017	8.240	0.181	0.181	0.000	0.000	0.000	0.000
7	A	53	HIS	0	0.036	0.029	10.960	0.065	0.065	0.000	0.000	0.000	0.000
8	A	54	PHE	0	0.004	-0.026	12.625	-0.036	-0.036	0.000	0.000	0.000	0.000
9	A	55	ILE	0	-0.079	-0.031	16.445	0.034	0.034	0.000	0.000	0.000	0.000
10	A	56	GLU	-1	-0.902	-0.964	18.433	0.129	0.129	0.000	0.000	0.000	0.000
11	A	57	GLU	-1	-0.835	-0.926	19.888	0.128	0.128	0.000	0.000	0.000	0.000
12	A	58	PRO	0	-0.013	0.010	22.313	-0.002	-0.002	0.000	0.000	0.000	0.000
13	A	59	GLU	-1	-0.899	-0.955	25.682	0.093	0.093	0.000	0.000	0.000	0.000
14	A	60	ASP	-1	-0.876	-0.931	28.449	0.051	0.051	0.000	0.000	0.000	0.000
15	A	61	ALA	0	0.014	0.016	31.536	0.002	0.002	0.000	0.000	0.000	0.000
16	A	62	TYR	0	0.008	-0.016	34.367	-0.004	-0.004	0.000	0.000	0.000	0.000
17	A	63	ILE	0	-0.004	0.012	38.168	0.000	0.000	0.000	0.000	0.000	0.000
18	A	64	ILE	0	-0.028	-0.023	40.630	-0.001	-0.001	0.000	0.000	0.000	0.000
19	A	65	LYS	1	0.971	0.985	43.682	-0.018	-0.018	0.000	0.000	0.000	0.000
20	A	66	SER	0	-0.046	-0.031	44.638	-0.001	-0.001	0.000	0.000	0.000	0.000
21	A	67	ASN	0	0.024	0.028	40.725	-0.004	-0.004	0.000	0.000	0.000	0.000
22	A	68	PRO	0	-0.003	-0.004	38.299	0.001	0.001	0.000	0.000	0.000	0.000
23	A	69	ILE	0	-0.028	0.000	33.670	0.003	0.003	0.000	0.000	0.000	0.000
24	A	70	ALA	0	0.042	0.015	32.158	-0.004	-0.004	0.000	0.000	0.000	0.000
25	A	71	LEU	0	-0.038	-0.015	28.208	0.006	0.006	0.000	0.000	0.000	0.000
26	A	72	ARG	1	0.948	0.985	25.029	-0.094	-0.094	0.000	0.000	0.000	0.000
27	A	73	CYS	0	-0.008	0.007	21.187	-0.010	-0.010	0.000	0.000	0.000	0.000
28	A	74	LYS	1	0.963	0.993	19.902	-0.104	-0.104	0.000	0.000	0.000	0.000
29	A	75	ALA	0	0.006	0.013	15.340	0.024	0.024	0.000	0.000	0.000	0.000
30	A	76	ARG	1	0.919	0.975	12.141	-0.333	-0.333	0.000	0.000	0.000	0.000
31	A	77	PRO	0	-0.027	-0.002	9.151	0.087	0.087	0.000	0.000	0.000	0.000
32	A	78	ALA	0	0.028	-0.010	12.325	-0.054	-0.054	0.000	0.000	0.000	0.000
33	A	79	MET	0	-0.023	-0.001	13.819	0.014	0.014	0.000	0.000	0.000	0.000
34	A	80	GLN	0	-0.029	-0.021	17.346	0.030	0.030	0.000	0.000	0.000	0.000
35	A	81	ILE	0	0.010	0.009	18.208	-0.009	-0.009	0.000	0.000	0.000	0.000
36	A	82	PHE	0	0.000	0.007	20.675	0.004	0.004	0.000	0.000	0.000	0.000
37	A	83	PHE	0	0.038	0.004	22.926	0.003	0.003	0.000	0.000	0.000	0.000
38	A	84	LYS	1	0.847	0.933	24.269	0.058	0.058	0.000	0.000	0.000	0.000
39	A	85	CYS	0	-0.030	-0.026	26.663	0.000	0.000	0.000	0.000	0.000	0.000
40	A	86	ASN	0	0.060	0.029	30.016	-0.001	-0.001	0.000	0.000	0.000	0.000
41	A	87	GLY	0	0.007	0.014	28.561	-0.002	-0.002	0.000	0.000	0.000	0.000
42	A	88	GLU	-1	-0.910	-0.952	29.126	-0.049	-0.049	0.000	0.000	0.000	0.000
43	A	89	TRP	0	-0.079	-0.056	21.844	0.003	0.003	0.000	0.000	0.000	0.000
44	A	90	VAL	0	0.021	0.015	28.361	0.002	0.002	0.000	0.000	0.000	0.000
45	A	91	HIS	0	0.057	0.028	29.221	-0.010	-0.010	0.000	0.000	0.000	0.000
46	A	92	GLN	0	0.029	0.003	27.631	-0.001	-0.001	0.000	0.000	0.000	0.000
47	A	93	ASN	0	-0.063	-0.032	30.077	0.000	0.000	0.000	0.000	0.000	0.000
48	A	94	GLU	-1	-0.861	-0.930	32.508	-0.024	-0.024	0.000	0.000	0.000	0.000
49	A	95	HIS	0	-0.089	-0.027	26.083	0.006	0.006	0.000	0.000	0.000	0.000
50	A	96	VAL	0	0.013	0.013	29.235	-0.004	-0.004	0.000	0.000	0.000	0.000
51	A	97	SER	0	-0.041	-0.038	24.902	0.001	0.001	0.000	0.000	0.000	0.000
52	A	98	GLU	-1	-0.939	-0.960	24.984	0.020	0.020	0.000	0.000	0.000	0.000
53	A	99	GLU	-1	-0.922	-0.970	20.442	-0.091	-0.091	0.000	0.000	0.000	0.000
54	A	100	SER	0	0.032	0.014	20.881	0.009	0.009	0.000	0.000	0.000	0.000
55	A	101	LEU	0	-0.048	-0.038	17.362	-0.013	-0.013	0.000	0.000	0.000	0.000
56	A	102	ASP	-1	-0.830	-0.918	15.110	0.167	0.167	0.000	0.000	0.000	0.000
57	A	102	GLU	-1	-0.842	-0.933	11.110	0.416	0.416	0.000	0.000	0.000	0.000
58	A	102	SER	0	-0.074	-0.019	9.275	-0.070	-0.070	0.000	0.000	0.000	0.000
59	A	102	SER	0	-0.034	-0.025	11.432	-0.075	-0.075	0.000	0.000	0.000	0.000
60	A	102	GLY	0	-0.030	-0.008	13.852	-0.037	-0.037	0.000	0.000	0.000	0.000
61	A	103	LEU	0	-0.042	-0.013	9.102	-0.062	-0.062	0.000	0.000	0.000	0.000
62	A	104	LYS	1	0.932	0.965	13.084	0.109	0.109	0.000	0.000	0.000	0.000
63	A	105	VAL	0	-0.007	0.003	15.400	0.004	0.004	0.000	0.000	0.000	0.000
64	A	106	ARG	1	0.914	0.969	17.675	0.064	0.064	0.000	0.000	0.000	0.000
65	A	107	GLU	-1	-0.870	-0.963	20.167	0.076	0.076	0.000	0.000	0.000	0.000
66	A	108	VAL	0	-0.047	-0.021	23.009	-0.012	-0.012	0.000	0.000	0.000	0.000
67	A	109	PHE	0	0.010	0.009	25.171	0.009	0.009	0.000	0.000	0.000	0.000
68	A	110	ILE	0	-0.003	0.001	28.423	-0.007	-0.007	0.000	0.000	0.000	0.000
69	A	111	ASN	0	-0.003	-0.010	30.798	0.010	0.010	0.000	0.000	0.000	0.000
70	A	112	VAL	0	0.012	0.021	33.026	-0.004	-0.004	0.000	0.000	0.000	0.000
71	A	113	THR	0	0.000	-0.017	35.835	0.004	0.004	0.000	0.000	0.000	0.000
72	A	114	ARG	1	0.910	0.940	39.618	-0.006	-0.006	0.000	0.000	0.000	0.000
73	A	115	GLN	0	0.013	-0.004	42.245	-0.001	-0.001	0.000	0.000	0.000	0.000
74	A	116	GLN	0	0.075	0.051	35.525	0.001	0.001	0.000	0.000	0.000	0.000
75	A	117	VAL	0	-0.029	-0.018	37.438	-0.001	-0.001	0.000	0.000	0.000	0.000
76	A	118	GLU	-1	-0.932	-0.977	39.743	0.002	0.002	0.000	0.000	0.000	0.000
77	A	119	ASP	-1	-0.888	-0.936	42.075	-0.008	-0.008	0.000	0.000	0.000	0.000
78	A	120	PHE	0	-0.083	-0.032	35.843	-0.003	-0.003	0.000	0.000	0.000	0.000
79	A	121	HIS	0	-0.021	-0.008	40.465	0.003	0.003	0.000	0.000	0.000	0.000
80	A	122	GLY	0	-0.007	0.007	38.420	-0.002	-0.002	0.000	0.000	0.000	0.000
81	A	123	PRO	0	-0.046	-0.026	36.860	0.002	0.002	0.000	0.000	0.000	0.000
82	A	124	GLU	-1	-0.959	-0.976	32.388	0.014	0.014	0.000	0.000	0.000	0.000
83	A	125	ASP	-1	-0.910	-0.970	35.311	0.021	0.021	0.000	0.000	0.000	0.000
84	A	126	TYR	0	-0.010	0.003	33.639	-0.003	-0.003	0.000	0.000	0.000	0.000
85	A	127	TRP	0	0.050	0.017	26.575	0.003	0.003	0.000	0.000	0.000	0.000
86	A	129	GLN	0	-0.054	-0.019	21.818	-0.005	-0.005	0.000	0.000	0.000	0.000
87	A	131	VAL	0	-0.036	-0.010	18.315	0.007	0.007	0.000	0.000	0.000	0.000
88	A	132	ALA	0	0.063	0.030	15.642	-0.006	-0.006	0.000	0.000	0.000	0.000
89	A	133	TRP	0	0.006	-0.019	15.170	-0.019	-0.019	0.000	0.000	0.000	0.000
90	A	134	SER	0	0.008	-0.002	9.828	-0.003	-0.003	0.000	0.000	0.000	0.000
91	A	135	HIS	0	0.027	0.008	7.515	0.189	0.189	0.000	0.000	0.000	0.000
92	A	136	LEU	0	-0.024	-0.011	5.091	-0.079	-0.079	0.000	0.000	0.000	0.000
93	A	137	GLY	0	0.011	0.013	9.472	0.027	0.027	0.000	0.000	0.000	0.000
94	A	138	THR	0	-0.045	-0.022	12.126	0.041	0.041	0.000	0.000	0.000	0.000
95	A	139	SER	0	0.007	-0.004	12.447	-0.019	-0.019	0.000	0.000	0.000	0.000
96	A	140	LYS	1	0.907	0.954	14.392	0.046	0.046	0.000	0.000	0.000	0.000
97	A	141	SER	0	0.053	0.046	17.541	0.018	0.018	0.000	0.000	0.000	0.000
98	A	142	ARG	1	0.832	0.902	19.637	-0.095	-0.095	0.000	0.000	0.000	0.000
99	A	143	LYS	1	0.869	0.931	22.771	-0.014	-0.014	0.000	0.000	0.000	0.000
100	A	144	ALA	0	0.001	0.021	26.024	0.006	0.006	0.000	0.000	0.000	0.000
101	A	145	SER	0	0.003	-0.013	28.508	-0.010	-0.010	0.000	0.000	0.000	0.000
102	A	146	VAL	0	-0.047	-0.025	32.187	0.004	0.004	0.000	0.000	0.000	0.000
103	A	147	ARG	1	0.966	0.992	34.880	-0.040	-0.040	0.000	0.000	0.000	0.000
104	A	148	ILE	0	-0.002	-0.004	38.668	0.002	0.002	0.000	0.000	0.000	0.000
105	A	149	ALA	0	0.011	0.023	41.956	0.001	0.001	0.000	0.000	0.000	0.000
106	A	150	TYR	0	-0.005	-0.021	43.638	-0.002	-0.002	0.000	0.000	0.000	0.000
107	A	151	LEU	0	-0.008	-0.004	45.566	0.001	0.001	0.000	0.000	0.000	0.000
108	A	152	ARG	1	0.991	1.000	48.594	-0.030	-0.030	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:47:ALA)