FMO DATABASE

FMODB ID: 98RN2

Calculation Name: 2F9F-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2F9F

Chain ID: A

ChEMBL ID:

UniProt ID: O30192

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:

Apendix: None

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
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	166
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1824179.780068
FMO2-HF: Nuclear repulsion	1756983.799612
FMO2-HF: Total energy	-67195.980456
FMO2-MP2: Total energy	-67391.403997

3D Structure Molmil

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:VAL)

Summations of interaction energy for fragment #1(A:2: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.
-6.011	1.322	7.512	-4.606	-10.234	-0.026

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.017 / q_NPA : 0.011

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	4	THR	0	0.017	-0.017	2.400	-1.551	1.414	0.667	-1.528	-2.103	0.002
4	A	5	SER	0	-0.037	-0.015	4.713	0.552	0.663	-0.001	-0.011	-0.099	0.000
5	A	6	LYS	1	0.862	0.921	7.173	0.735	0.735	0.000	0.000	0.000	0.000
6	A	7	PHE	0	0.009	0.018	5.181	0.178	0.178	0.000	0.000	0.000	0.000
7	A	8	LYS	1	0.900	0.950	9.401	0.407	0.407	0.000	0.000	0.000	0.000
8	A	9	PHE	0	0.034	0.010	12.574	0.042	0.042	0.000	0.000	0.000	0.000
9	A	10	LYS	1	0.835	0.915	15.251	0.216	0.216	0.000	0.000	0.000	0.000
10	A	11	CYS	0	-0.042	-0.030	18.521	0.014	0.014	0.000	0.000	0.000	0.000
11	A	12	TYR	0	-0.012	-0.020	16.818	-0.011	-0.011	0.000	0.000	0.000	0.000
12	A	13	GLY	0	0.016	0.007	20.362	0.012	0.012	0.000	0.000	0.000	0.000
13	A	14	ASP	-1	-0.882	-0.933	22.330	-0.065	-0.065	0.000	0.000	0.000	0.000
14	A	15	PHE	0	-0.040	-0.015	18.211	0.009	0.009	0.000	0.000	0.000	0.000
15	A	16	TRP	0	-0.003	-0.006	17.790	-0.019	-0.019	0.000	0.000	0.000	0.000
16	A	17	LEU	0	-0.011	-0.006	13.536	0.006	0.006	0.000	0.000	0.000	0.000
17	A	18	SER	0	0.030	0.003	14.904	-0.002	-0.002	0.000	0.000	0.000	0.000
18	A	19	VAL	0	0.030	0.016	10.946	-0.005	-0.005	0.000	0.000	0.000	0.000
19	A	20	ASN	0	0.024	0.005	12.923	0.038	0.038	0.000	0.000	0.000	0.000
20	A	21	ARG	1	0.907	0.956	15.229	-0.241	-0.241	0.000	0.000	0.000	0.000
21	A	22	ILE	0	0.000	0.006	17.760	-0.002	-0.002	0.000	0.000	0.000	0.000
22	A	23	TYR	0	0.009	-0.009	19.946	-0.009	-0.009	0.000	0.000	0.000	0.000
23	A	24	PRO	0	0.017	0.002	21.519	-0.002	-0.002	0.000	0.000	0.000	0.000
24	A	25	GLU	-1	-0.872	-0.929	18.447	0.216	0.216	0.000	0.000	0.000	0.000
25	A	26	LYS	1	0.772	0.855	13.778	-0.353	-0.353	0.000	0.000	0.000	0.000
26	A	27	ARG	1	0.745	0.845	18.811	-0.171	-0.171	0.000	0.000	0.000	0.000
27	A	28	ILE	0	0.061	0.029	19.232	-0.015	-0.015	0.000	0.000	0.000	0.000
28	A	29	GLU	-1	-0.771	-0.874	22.215	0.086	0.086	0.000	0.000	0.000	0.000
29	A	30	LEU	0	-0.020	0.007	21.645	-0.009	-0.009	0.000	0.000	0.000	0.000
30	A	31	GLN	0	0.020	0.006	17.680	-0.024	-0.024	0.000	0.000	0.000	0.000
31	A	32	LEU	0	-0.018	-0.012	22.915	-0.011	-0.011	0.000	0.000	0.000	0.000
32	A	33	GLU	-1	-0.861	-0.916	26.189	0.033	0.033	0.000	0.000	0.000	0.000
33	A	34	VAL	0	-0.027	-0.006	23.594	-0.006	-0.006	0.000	0.000	0.000	0.000
34	A	35	PHE	0	0.001	-0.010	22.070	-0.007	-0.007	0.000	0.000	0.000	0.000
35	A	36	LYS	1	0.852	0.935	27.229	-0.041	-0.041	0.000	0.000	0.000	0.000
36	A	37	LYS	1	0.914	0.967	29.913	-0.021	-0.021	0.000	0.000	0.000	0.000
37	A	38	LEU	0	-0.027	-0.007	25.895	-0.004	-0.004	0.000	0.000	0.000	0.000
38	A	39	GLN	0	-0.020	-0.021	28.979	-0.003	-0.003	0.000	0.000	0.000	0.000
39	A	40	ASP	-1	-0.925	-0.953	30.433	-0.026	-0.026	0.000	0.000	0.000	0.000
40	A	41	GLU	-1	-0.845	-0.888	24.820	-0.059	-0.059	0.000	0.000	0.000	0.000
41	A	42	LYS	1	0.907	0.931	24.947	0.050	0.050	0.000	0.000	0.000	0.000
42	A	43	LEU	0	-0.009	0.017	19.384	-0.009	-0.009	0.000	0.000	0.000	0.000
43	A	44	TYR	0	-0.036	-0.022	19.672	0.006	0.006	0.000	0.000	0.000	0.000
44	A	45	ILE	0	0.041	0.014	18.508	-0.001	-0.001	0.000	0.000	0.000	0.000
45	A	46	VAL	0	0.021	0.016	14.436	-0.001	-0.001	0.000	0.000	0.000	0.000
46	A	47	GLY	0	0.000	-0.009	16.182	0.030	0.030	0.000	0.000	0.000	0.000
47	A	48	TRP	0	0.007	-0.008	17.695	-0.018	-0.018	0.000	0.000	0.000	0.000
48	A	49	PHE	0	-0.015	-0.015	20.463	0.018	0.018	0.000	0.000	0.000	0.000
49	A	50	SER	0	-0.012	-0.013	22.512	-0.008	-0.008	0.000	0.000	0.000	0.000
50	A	51	LYS	1	0.951	0.957	24.257	-0.105	-0.105	0.000	0.000	0.000	0.000
51	A	52	GLY	0	-0.040	-0.018	27.751	0.003	0.003	0.000	0.000	0.000	0.000
52	A	53	ASP	-1	-0.817	-0.870	25.646	0.161	0.161	0.000	0.000	0.000	0.000
53	A	54	HIS	0	0.031	0.001	27.996	-0.011	-0.011	0.000	0.000	0.000	0.000
54	A	55	ALA	0	0.001	-0.001	24.574	-0.007	-0.007	0.000	0.000	0.000	0.000
55	A	56	GLU	-1	-0.768	-0.856	26.639	0.082	0.082	0.000	0.000	0.000	0.000
56	A	57	ARG	1	0.940	0.970	28.387	-0.086	-0.086	0.000	0.000	0.000	0.000
57	A	58	TYR	0	-0.061	-0.059	23.639	-0.006	-0.006	0.000	0.000	0.000	0.000
58	A	59	ALA	0	0.082	0.035	25.262	-0.006	-0.006	0.000	0.000	0.000	0.000
59	A	60	ARG	1	0.860	0.896	26.698	-0.078	-0.078	0.000	0.000	0.000	0.000
60	A	61	LYS	1	0.813	0.908	29.560	-0.089	-0.089	0.000	0.000	0.000	0.000
61	A	62	ILE	0	0.004	0.000	24.608	-0.008	-0.008	0.000	0.000	0.000	0.000
62	A	63	MET	0	-0.017	-0.009	26.560	-0.007	-0.007	0.000	0.000	0.000	0.000
63	A	64	LYS	1	0.914	0.978	28.710	-0.057	-0.057	0.000	0.000	0.000	0.000
64	A	65	ILE	0	-0.071	-0.035	29.506	-0.004	-0.004	0.000	0.000	0.000	0.000
65	A	66	ALA	0	-0.010	-0.002	27.698	-0.002	-0.002	0.000	0.000	0.000	0.000
66	A	67	PRO	0	-0.010	0.004	28.171	-0.001	-0.001	0.000	0.000	0.000	0.000
67	A	68	ASP	-1	-0.875	-0.950	29.648	0.002	0.002	0.000	0.000	0.000	0.000
68	A	69	ASN	0	-0.076	-0.026	28.371	0.002	0.002	0.000	0.000	0.000	0.000
69	A	70	VAL	0	-0.016	-0.012	23.941	-0.004	-0.004	0.000	0.000	0.000	0.000
70	A	71	LYS	1	0.918	0.967	23.957	0.025	0.025	0.000	0.000	0.000	0.000
71	A	72	PHE	0	0.024	-0.002	22.774	0.003	0.003	0.000	0.000	0.000	0.000
72	A	73	LEU	0	-0.001	-0.005	18.972	-0.003	-0.003	0.000	0.000	0.000	0.000
73	A	74	GLY	0	0.037	0.030	21.014	0.000	0.000	0.000	0.000	0.000	0.000
74	A	75	SER	0	-0.050	-0.043	17.631	0.017	0.017	0.000	0.000	0.000	0.000
75	A	76	VAL	0	0.016	0.027	14.977	-0.008	-0.008	0.000	0.000	0.000	0.000
76	A	77	SER	0	-0.017	-0.033	15.516	0.018	0.018	0.000	0.000	0.000	0.000
77	A	78	GLU	-1	-0.777	-0.896	8.989	-0.283	-0.283	0.000	0.000	0.000	0.000
78	A	79	GLU	-1	-0.888	-0.951	12.791	-0.148	-0.148	0.000	0.000	0.000	0.000
79	A	80	GLU	-1	-0.841	-0.889	15.273	-0.041	-0.041	0.000	0.000	0.000	0.000
80	A	81	LEU	0	-0.008	0.006	9.349	-0.015	-0.015	0.000	0.000	0.000	0.000
81	A	82	ILE	0	-0.010	-0.004	10.027	-0.037	-0.037	0.000	0.000	0.000	0.000
82	A	83	ASP	-1	-0.813	-0.865	12.217	-0.180	-0.180	0.000	0.000	0.000	0.000
83	A	84	LEU	0	0.017	0.013	15.088	-0.004	-0.004	0.000	0.000	0.000	0.000
84	A	85	TYR	0	0.004	-0.048	7.958	-0.005	-0.005	0.000	0.000	0.000	0.000
85	A	86	SER	0	-0.025	-0.020	13.077	-0.009	-0.009	0.000	0.000	0.000	0.000
86	A	87	ARG	1	0.833	0.883	14.735	0.125	0.125	0.000	0.000	0.000	0.000
87	A	88	CYS	0	-0.039	0.030	14.819	0.012	0.012	0.000	0.000	0.000	0.000
88	A	89	LYS	1	0.848	0.902	17.824	0.043	0.043	0.000	0.000	0.000	0.000
89	A	90	GLY	0	0.038	-0.003	15.713	-0.018	-0.018	0.000	0.000	0.000	0.000
90	A	91	LEU	0	-0.054	-0.013	10.125	0.013	0.013	0.000	0.000	0.000	0.000
91	A	92	LEU	0	-0.002	0.004	14.360	-0.001	-0.001	0.000	0.000	0.000	0.000
92	A	93	CYS	0	-0.020	-0.011	12.079	0.008	0.008	0.000	0.000	0.000	0.000
93	A	94	THR	0	0.038	-0.002	14.793	-0.012	-0.012	0.000	0.000	0.000	0.000
94	A	95	ALA	0	-0.024	0.008	14.236	-0.003	-0.003	0.000	0.000	0.000	0.000
95	A	96	LYS	1	0.951	0.969	15.935	-0.186	-0.186	0.000	0.000	0.000	0.000
96	A	97	ASP	-1	-0.817	-0.903	15.328	0.359	0.359	0.000	0.000	0.000	0.000
97	A	98	GLU	-1	-0.822	-0.899	10.275	0.442	0.442	0.000	0.000	0.000	0.000
98	A	99	ASP	-1	-0.892	-0.947	10.404	0.513	0.513	0.000	0.000	0.000	0.000
99	A	100	PHE	0	-0.017	-0.022	4.933	0.071	0.071	0.000	0.000	0.000	0.000
100	A	101	GLY	0	0.014	0.017	5.291	-0.019	-0.019	0.000	0.000	0.000	0.000
101	A	102	LEU	0	0.025	-0.002	2.327	-0.480	-0.825	3.308	-0.478	-2.484	0.000
102	A	103	THR	0	0.054	0.028	4.506	-0.414	-0.331	-0.001	-0.009	-0.072	0.000
103	A	104	PRO	0	0.037	0.012	7.204	-0.131	-0.131	0.000	0.000	0.000	0.000
104	A	105	ILE	0	-0.014	0.012	2.423	-1.318	-0.480	1.535	-0.407	-1.965	-0.002
105	A	106	GLU	-1	-0.812	-0.876	4.138	-0.348	-0.176	0.000	-0.018	-0.154	0.000
106	A	107	ALA	0	0.003	0.005	5.877	-0.038	-0.038	0.000	0.000	0.000	0.000
107	A	108	MET	0	-0.033	-0.001	7.582	0.006	0.006	0.000	0.000	0.000	0.000
108	A	109	ALA	0	0.017	0.009	5.852	-0.008	-0.008	0.000	0.000	0.000	0.000
109	A	110	SER	0	-0.046	-0.028	8.012	0.042	0.042	0.000	0.000	0.000	0.000
110	A	111	GLY	0	-0.045	-0.031	11.021	0.081	0.081	0.000	0.000	0.000	0.000
111	A	112	LYS	1	0.688	0.844	12.291	0.298	0.298	0.000	0.000	0.000	0.000
112	A	113	PRO	0	0.034	0.025	12.675	-0.021	-0.021	0.000	0.000	0.000	0.000
113	A	114	VAL	0	-0.007	-0.016	10.394	0.015	0.015	0.000	0.000	0.000	0.000
114	A	115	ILE	0	-0.019	0.008	13.889	0.004	0.004	0.000	0.000	0.000	0.000
115	A	116	ALA	0	0.007	-0.005	13.734	0.014	0.014	0.000	0.000	0.000	0.000
116	A	117	VAL	0	0.012	0.021	15.835	-0.013	-0.013	0.000	0.000	0.000	0.000
117	A	118	ASN	0	-0.006	-0.007	15.816	0.015	0.015	0.000	0.000	0.000	0.000
118	A	119	GLU	-1	-0.826	-0.900	15.530	0.175	0.175	0.000	0.000	0.000	0.000
119	A	120	GLY	0	0.063	0.030	12.856	0.000	0.000	0.000	0.000	0.000	0.000
120	A	121	GLY	0	0.050	0.015	8.638	-0.014	-0.014	0.000	0.000	0.000	0.000
121	A	122	PHE	0	-0.009	-0.004	8.874	-0.070	-0.070	0.000	0.000	0.000	0.000
122	A	123	LYS	1	0.824	0.913	11.137	-0.276	-0.276	0.000	0.000	0.000	0.000
123	A	124	GLU	-1	-0.842	-0.903	8.867	0.230	0.230	0.000	0.000	0.000	0.000
124	A	125	THR	0	-0.056	-0.036	5.926	-0.081	-0.081	0.000	0.000	0.000	0.000
125	A	126	VAL	0	-0.022	-0.004	8.914	-0.126	-0.126	0.000	0.000	0.000	0.000
126	A	127	ILE	0	0.018	0.016	11.977	0.036	0.036	0.000	0.000	0.000	0.000
127	A	128	ASN	0	0.068	0.017	14.997	-0.016	-0.016	0.000	0.000	0.000	0.000
128	A	129	GLU	-1	-0.908	-0.969	18.114	-0.064	-0.064	0.000	0.000	0.000	0.000
129	A	130	LYS	1	0.893	0.948	17.056	0.120	0.120	0.000	0.000	0.000	0.000
130	A	131	THR	0	0.010	-0.016	12.065	-0.012	-0.012	0.000	0.000	0.000	0.000
131	A	132	GLY	0	0.041	0.015	14.029	-0.009	-0.009	0.000	0.000	0.000	0.000
132	A	133	TYR	0	-0.065	-0.033	16.349	0.001	0.001	0.000	0.000	0.000	0.000
133	A	134	LEU	0	-0.012	0.010	14.163	0.005	0.005	0.000	0.000	0.000	0.000
134	A	135	VAL	0	-0.027	-0.007	18.106	-0.006	-0.006	0.000	0.000	0.000	0.000
135	A	136	ASN	0	-0.028	-0.034	20.065	0.028	0.028	0.000	0.000	0.000	0.000
136	A	137	ALA	0	-0.023	-0.020	21.493	-0.007	-0.007	0.000	0.000	0.000	0.000
137	A	138	ASP	-1	-0.816	-0.918	22.758	0.037	0.037	0.000	0.000	0.000	0.000
138	A	139	VAL	0	-0.006	-0.013	25.039	-0.006	-0.006	0.000	0.000	0.000	0.000
139	A	140	ASN	0	-0.045	-0.024	26.527	-0.006	-0.006	0.000	0.000	0.000	0.000
140	A	141	GLU	-1	-0.762	-0.864	24.460	0.029	0.029	0.000	0.000	0.000	0.000
141	A	142	ILE	0	-0.002	-0.005	20.968	-0.009	-0.009	0.000	0.000	0.000	0.000
142	A	143	ILE	0	0.015	0.000	23.197	-0.012	-0.012	0.000	0.000	0.000	0.000
143	A	144	ASP	-1	-0.877	-0.938	25.825	-0.017	-0.017	0.000	0.000	0.000	0.000
144	A	145	ALA	0	-0.042	-0.017	21.011	-0.011	-0.011	0.000	0.000	0.000	0.000
145	A	146	MET	0	0.009	-0.012	21.253	-0.010	-0.010	0.000	0.000	0.000	0.000
146	A	147	LYS	1	0.949	0.978	22.911	0.014	0.014	0.000	0.000	0.000	0.000
147	A	148	LYS	1	0.844	0.941	23.523	0.040	0.040	0.000	0.000	0.000	0.000
148	A	149	VAL	0	0.000	-0.002	19.281	-0.009	-0.009	0.000	0.000	0.000	0.000
149	A	150	SER	0	-0.015	-0.014	22.417	-0.009	-0.009	0.000	0.000	0.000	0.000
150	A	151	LYS	1	0.912	0.965	25.120	0.055	0.055	0.000	0.000	0.000	0.000
151	A	152	ASN	0	-0.059	-0.026	24.425	-0.011	-0.011	0.000	0.000	0.000	0.000
152	A	153	PRO	0	0.064	0.038	21.514	-0.007	-0.007	0.000	0.000	0.000	0.000
153	A	154	ASP	-1	-0.933	-0.964	19.821	-0.191	-0.191	0.000	0.000	0.000	0.000
154	A	155	LYS	1	0.924	0.984	20.805	0.104	0.104	0.000	0.000	0.000	0.000
155	A	156	PHE	0	-0.021	-0.019	16.599	-0.001	-0.001	0.000	0.000	0.000	0.000
156	A	157	LYS	1	0.945	1.009	16.140	0.236	0.236	0.000	0.000	0.000	0.000
157	A	158	LYS	1	0.955	0.960	14.995	0.200	0.200	0.000	0.000	0.000	0.000
158	A	159	ASP	-1	-0.811	-0.885	14.951	-0.332	-0.332	0.000	0.000	0.000	0.000
159	A	160	CYS	0	-0.058	-0.002	11.923	-0.026	-0.026	0.000	0.000	0.000	0.000
160	A	161	PHE	0	-0.009	-0.007	10.464	-0.068	-0.068	0.000	0.000	0.000	0.000
161	A	162	ARG	1	0.770	0.873	10.153	0.230	0.230	0.000	0.000	0.000	0.000
162	A	163	ARG	1	0.883	0.930	9.155	0.186	0.186	0.000	0.000	0.000	0.000
163	A	164	ALA	0	0.003	0.000	6.013	-0.079	-0.079	0.000	0.000	0.000	0.000
164	A	165	LYS	1	0.919	0.953	5.316	0.317	0.317	0.000	0.000	0.000	0.000
165	A	166	GLU	-1	-0.914	-0.940	7.011	-0.761	-0.761	0.000	0.000	0.000	0.000
166	A	167	PHE	0	0.008	0.019	2.382	-3.922	-0.413	2.004	-2.155	-3.357	-0.026

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