FMO DATABASE

FMODB ID: 2JVJR

Calculation Name: 2F51-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2F51

Chain ID: A

ChEMBL ID:

UniProt ID: Q8IEV4

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	111
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-859379.656876
FMO2-HF: Nuclear repulsion	817359.196301
FMO2-HF: Total energy	-42020.460574
FMO2-MP2: Total energy	-42144.903824

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:2:SER)

Summations of interaction energy for fragment #1(A:2:SER)

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.
-0.214	2.089	-0.002	-1.065	-1.236	0.003

Interaction energy analysis for fragmet #1(A:2:SER)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.021 / q_NPA : 0.005

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	4	PRO	0	-0.031	-0.002	3.665	-2.163	0.015	-0.001	-1.055	-1.122	0.003
4	A	5	ILE	0	-0.051	-0.017	4.691	1.699	1.824	-0.001	-0.010	-0.114	0.000
5	A	6	VAL	0	-0.010	-0.002	7.806	-0.076	-0.076	0.000	0.000	0.000	0.000
6	A	7	HIS	0	-0.042	-0.037	8.518	0.664	0.664	0.000	0.000	0.000	0.000
7	A	8	PHE	0	-0.010	-0.002	11.999	0.111	0.111	0.000	0.000	0.000	0.000
8	A	9	ASN	0	-0.047	-0.034	14.354	0.100	0.100	0.000	0.000	0.000	0.000
9	A	10	GLY	0	0.034	0.020	17.257	0.027	0.027	0.000	0.000	0.000	0.000
10	A	11	THR	0	0.018	0.008	20.260	-0.010	-0.010	0.000	0.000	0.000	0.000
11	A	12	HIS	0	0.144	0.054	22.378	-0.043	-0.043	0.000	0.000	0.000	0.000
12	A	13	GLU	-1	-0.826	-0.916	23.455	-0.236	-0.236	0.000	0.000	0.000	0.000
13	A	14	ALA	0	-0.031	-0.010	19.895	-0.002	-0.002	0.000	0.000	0.000	0.000
14	A	15	LEU	0	0.018	0.017	17.900	-0.029	-0.029	0.000	0.000	0.000	0.000
15	A	16	LEU	0	0.004	0.000	19.270	-0.029	-0.029	0.000	0.000	0.000	0.000
16	A	17	ASN	0	-0.043	-0.033	20.619	0.014	0.014	0.000	0.000	0.000	0.000
17	A	18	ARG	1	0.987	1.008	10.222	0.749	0.749	0.000	0.000	0.000	0.000
18	A	19	ILE	0	-0.022	-0.011	15.904	-0.040	-0.040	0.000	0.000	0.000	0.000
19	A	20	LYS	1	0.840	0.916	17.650	0.235	0.235	0.000	0.000	0.000	0.000
20	A	21	GLU	-1	-0.914	-0.963	14.958	-0.320	-0.320	0.000	0.000	0.000	0.000
21	A	22	ALA	0	-0.067	-0.014	13.919	0.009	0.009	0.000	0.000	0.000	0.000
22	A	23	PRO	0	0.001	0.006	12.628	0.057	0.057	0.000	0.000	0.000	0.000
23	A	24	GLY	0	0.014	-0.006	15.298	0.058	0.058	0.000	0.000	0.000	0.000
24	A	25	LEU	0	-0.090	-0.028	16.705	0.005	0.005	0.000	0.000	0.000	0.000
25	A	26	VAL	0	0.040	0.019	14.861	-0.088	-0.088	0.000	0.000	0.000	0.000
26	A	27	LEU	0	-0.032	0.002	15.113	0.082	0.082	0.000	0.000	0.000	0.000
27	A	28	VAL	0	0.004	0.003	15.402	-0.124	-0.124	0.000	0.000	0.000	0.000
28	A	29	ASP	-1	-0.842	-0.953	16.652	-0.726	-0.726	0.000	0.000	0.000	0.000
29	A	30	PHE	0	-0.003	0.004	18.280	-0.048	-0.048	0.000	0.000	0.000	0.000
30	A	31	PHE	0	0.033	-0.011	16.969	0.016	0.016	0.000	0.000	0.000	0.000
31	A	32	ALA	0	0.116	0.055	21.599	0.012	0.012	0.000	0.000	0.000	0.000
32	A	33	THR	0	0.016	-0.001	19.487	-0.001	-0.001	0.000	0.000	0.000	0.000
33	A	34	TRP	0	0.004	0.001	22.013	0.000	0.000	0.000	0.000	0.000	0.000
34	A	35	CYS	0	0.001	0.041	24.666	0.028	0.028	0.000	0.000	0.000	0.000
35	A	36	GLY	0	0.044	0.021	24.102	-0.035	-0.035	0.000	0.000	0.000	0.000
36	A	37	PRO	0	-0.012	-0.029	24.155	-0.031	-0.031	0.000	0.000	0.000	0.000
37	A	38	CYS	0	0.016	0.020	21.550	-0.035	-0.035	0.000	0.000	0.000	0.000
38	A	39	GLN	0	-0.029	-0.015	20.054	-0.065	-0.065	0.000	0.000	0.000	0.000
39	A	40	ARG	1	0.935	0.964	19.346	0.334	0.334	0.000	0.000	0.000	0.000
40	A	41	LEU	0	0.028	0.017	18.246	-0.029	-0.029	0.000	0.000	0.000	0.000
41	A	42	GLY	0	-0.011	-0.018	16.127	-0.098	-0.098	0.000	0.000	0.000	0.000
42	A	43	GLN	0	-0.028	-0.005	14.590	-0.129	-0.129	0.000	0.000	0.000	0.000
43	A	44	ILE	0	-0.016	-0.017	14.368	-0.063	-0.063	0.000	0.000	0.000	0.000
44	A	45	LEU	0	0.005	0.002	13.230	-0.070	-0.070	0.000	0.000	0.000	0.000
45	A	46	PRO	0	0.033	0.020	8.719	-0.121	-0.121	0.000	0.000	0.000	0.000
46	A	47	SER	0	0.004	0.016	9.146	-0.238	-0.238	0.000	0.000	0.000	0.000
47	A	48	ILE	0	-0.019	-0.015	11.138	0.080	0.080	0.000	0.000	0.000	0.000
48	A	49	ALA	0	0.019	0.009	8.735	0.103	0.103	0.000	0.000	0.000	0.000
49	A	50	GLU	-1	-0.988	-0.988	5.603	-2.515	-2.515	0.000	0.000	0.000	0.000
50	A	51	ALA	0	-0.047	-0.029	8.258	0.334	0.334	0.000	0.000	0.000	0.000
51	A	52	ASN	0	-0.058	-0.030	11.017	0.352	0.352	0.000	0.000	0.000	0.000
52	A	53	LYS	1	0.987	0.985	5.049	1.205	1.205	0.000	0.000	0.000	0.000
53	A	54	ASP	-1	-0.939	-0.963	9.469	-0.491	-0.491	0.000	0.000	0.000	0.000
54	A	55	VAL	0	-0.065	-0.020	11.909	0.110	0.110	0.000	0.000	0.000	0.000
55	A	56	THR	0	-0.031	-0.013	10.503	-0.222	-0.222	0.000	0.000	0.000	0.000
56	A	57	PHE	0	0.028	0.010	10.322	0.202	0.202	0.000	0.000	0.000	0.000
57	A	58	ILE	0	0.001	-0.003	10.984	-0.239	-0.239	0.000	0.000	0.000	0.000
58	A	59	LYS	1	0.880	0.974	13.019	1.153	1.153	0.000	0.000	0.000	0.000
59	A	60	VAL	0	-0.007	-0.014	15.109	-0.005	-0.005	0.000	0.000	0.000	0.000
60	A	61	ASP	-1	-0.855	-0.929	18.164	-0.501	-0.501	0.000	0.000	0.000	0.000
61	A	62	VAL	0	0.030	-0.021	19.847	0.029	0.029	0.000	0.000	0.000	0.000
62	A	63	ASP	-1	-0.852	-0.909	23.182	-0.327	-0.327	0.000	0.000	0.000	0.000
63	A	64	LYS	1	0.826	0.918	17.449	0.535	0.535	0.000	0.000	0.000	0.000
64	A	65	ASN	0	-0.075	-0.036	18.340	0.040	0.040	0.000	0.000	0.000	0.000
65	A	66	GLY	0	0.097	0.055	22.629	-0.005	-0.005	0.000	0.000	0.000	0.000
66	A	67	ASN	0	0.022	0.003	26.234	-0.001	-0.001	0.000	0.000	0.000	0.000
67	A	68	ALA	0	-0.021	-0.013	22.647	0.010	0.010	0.000	0.000	0.000	0.000
68	A	69	ALA	0	0.016	0.003	24.153	0.001	0.001	0.000	0.000	0.000	0.000
69	A	70	ASP	-1	-0.891	-0.940	25.364	-0.255	-0.255	0.000	0.000	0.000	0.000
70	A	71	ALA	0	-0.081	-0.045	27.563	0.015	0.015	0.000	0.000	0.000	0.000
71	A	72	TYR	0	-0.065	-0.038	22.816	0.003	0.003	0.000	0.000	0.000	0.000
72	A	73	GLY	0	-0.007	0.014	26.956	-0.001	-0.001	0.000	0.000	0.000	0.000
73	A	74	VAL	0	-0.074	-0.035	24.603	0.000	0.000	0.000	0.000	0.000	0.000
74	A	75	SER	0	0.045	0.019	28.028	0.014	0.014	0.000	0.000	0.000	0.000
75	A	76	SER	0	-0.049	-0.019	29.420	-0.006	-0.006	0.000	0.000	0.000	0.000
76	A	77	ILE	0	0.003	0.015	24.878	-0.020	-0.020	0.000	0.000	0.000	0.000
77	A	78	PRO	0	-0.006	-0.033	22.100	0.027	0.027	0.000	0.000	0.000	0.000
78	A	79	ALA	0	-0.015	-0.002	23.212	0.030	0.030	0.000	0.000	0.000	0.000
79	A	80	LEU	0	-0.008	0.006	19.412	-0.054	-0.054	0.000	0.000	0.000	0.000
80	A	81	PHE	0	0.023	-0.001	20.843	0.058	0.058	0.000	0.000	0.000	0.000
81	A	82	PHE	0	0.014	0.015	18.021	-0.057	-0.057	0.000	0.000	0.000	0.000
82	A	83	VAL	0	0.008	-0.005	19.580	0.060	0.060	0.000	0.000	0.000	0.000
83	A	84	LYS	1	0.975	0.976	19.641	0.258	0.258	0.000	0.000	0.000	0.000
84	A	85	LYS	1	0.890	0.961	20.203	0.210	0.210	0.000	0.000	0.000	0.000
85	A	86	GLU	-1	-0.908	-0.971	22.214	-0.180	-0.180	0.000	0.000	0.000	0.000
86	A	87	GLY	0	0.026	0.024	25.778	0.008	0.008	0.000	0.000	0.000	0.000
87	A	88	ASN	0	-0.065	-0.041	25.447	-0.002	-0.002	0.000	0.000	0.000	0.000
88	A	89	GLU	-1	-0.930	-0.961	27.019	-0.161	-0.161	0.000	0.000	0.000	0.000
89	A	90	ILE	0	-0.017	-0.007	22.283	-0.010	-0.010	0.000	0.000	0.000	0.000
90	A	91	LYS	1	0.953	0.995	24.591	0.244	0.244	0.000	0.000	0.000	0.000
91	A	92	THR	0	0.031	-0.005	24.189	-0.032	-0.032	0.000	0.000	0.000	0.000
92	A	93	LEU	0	-0.142	-0.069	22.640	0.032	0.032	0.000	0.000	0.000	0.000
93	A	94	ASP	-1	-0.737	-0.823	24.503	-0.317	-0.317	0.000	0.000	0.000	0.000
94	A	95	GLN	0	-0.011	0.000	24.533	-0.035	-0.035	0.000	0.000	0.000	0.000
95	A	96	PHE	0	-0.041	-0.019	22.577	0.029	0.029	0.000	0.000	0.000	0.000
96	A	97	VAL	0	0.056	0.031	25.533	-0.029	-0.029	0.000	0.000	0.000	0.000
97	A	98	GLY	0	0.005	0.008	25.799	0.025	0.025	0.000	0.000	0.000	0.000
98	A	99	ALA	0	-0.018	-0.014	23.034	-0.025	-0.025	0.000	0.000	0.000	0.000
99	A	100	ASP	-1	-0.891	-0.942	24.045	-0.360	-0.360	0.000	0.000	0.000	0.000
100	A	101	VAL	0	0.036	-0.005	19.639	-0.019	-0.019	0.000	0.000	0.000	0.000
101	A	102	SER	0	-0.001	-0.005	21.757	-0.033	-0.033	0.000	0.000	0.000	0.000
102	A	103	ARG	1	0.873	0.931	24.101	0.332	0.332	0.000	0.000	0.000	0.000
103	A	104	ILE	0	-0.012	-0.005	18.049	-0.006	-0.006	0.000	0.000	0.000	0.000
104	A	105	LYS	1	0.955	0.970	17.907	0.553	0.553	0.000	0.000	0.000	0.000
105	A	106	ALA	0	0.054	0.037	20.597	0.012	0.012	0.000	0.000	0.000	0.000
106	A	107	ASH	0	-0.092	-0.088	21.996	0.041	0.041	0.000	0.000	0.000	0.000
107	A	108	ILE	0	-0.027	-0.012	15.994	0.011	0.011	0.000	0.000	0.000	0.000
108	A	109	GLU	-1	-0.953	-0.974	19.551	-0.345	-0.345	0.000	0.000	0.000	0.000
109	A	110	LYS	1	0.916	0.973	21.687	0.286	0.286	0.000	0.000	0.000	0.000
110	A	111	PHE	0	-0.049	-0.040	21.184	0.034	0.034	0.000	0.000	0.000	0.000
111	A	112	LYS	1	0.940	0.996	18.392	0.252	0.252	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:SER)