FMO DATABASE

FMODB ID: LNVM9

Calculation Name: 2F9F-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

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:

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	166
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1822671.638984
FMO2-HF: Nuclear repulsion	1755476.493412
FMO2-HF: Total energy	-67195.145572
FMO2-MP2: Total energy	-67390.58036

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: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.
-6.815	-0.033	6.972	-3.984	-9.769	-0.023

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 : -0.008 / q_NPA : -0.015

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	0.023	-0.021	2.579	-1.615	0.699	0.572	-1.080	-1.806	-0.002
4	A	5	SER	0	-0.007	-0.002	4.699	0.315	0.424	-0.001	-0.012	-0.095	0.000
5	A	6	LYS	1	0.870	0.924	7.019	0.153	0.153	0.000	0.000	0.000	0.000
6	A	7	PHE	0	-0.038	0.008	4.563	0.012	0.099	-0.001	-0.003	-0.083	0.000
7	A	8	LYS	1	0.949	0.975	9.363	0.201	0.201	0.000	0.000	0.000	0.000
8	A	9	PHE	0	0.014	0.002	12.577	0.016	0.016	0.000	0.000	0.000	0.000
9	A	10	LYS	1	0.805	0.910	15.285	0.165	0.165	0.000	0.000	0.000	0.000
10	A	11	CYS	0	-0.033	-0.024	18.542	0.014	0.014	0.000	0.000	0.000	0.000
11	A	12	TYR	0	0.005	-0.005	17.085	-0.009	-0.009	0.000	0.000	0.000	0.000
12	A	13	GLY	0	0.019	0.008	20.395	0.013	0.013	0.000	0.000	0.000	0.000
13	A	14	ASP	-1	-0.892	-0.956	22.354	-0.095	-0.095	0.000	0.000	0.000	0.000
14	A	15	PHE	0	-0.033	-0.009	18.036	0.009	0.009	0.000	0.000	0.000	0.000
15	A	16	TRP	0	0.012	0.011	17.712	-0.024	-0.024	0.000	0.000	0.000	0.000
16	A	17	LEU	0	0.000	-0.004	13.294	0.014	0.014	0.000	0.000	0.000	0.000
17	A	18	SER	0	0.031	0.026	14.954	-0.015	-0.015	0.000	0.000	0.000	0.000
18	A	19	VAL	0	0.045	0.021	10.935	0.016	0.016	0.000	0.000	0.000	0.000
19	A	20	ASN	0	0.004	-0.013	12.922	-0.011	-0.011	0.000	0.000	0.000	0.000
20	A	21	ARG	1	0.917	0.979	15.221	-0.113	-0.113	0.000	0.000	0.000	0.000
21	A	22	ILE	0	-0.001	0.010	17.746	-0.010	-0.010	0.000	0.000	0.000	0.000
22	A	23	TYR	0	0.012	-0.009	20.145	0.008	0.008	0.000	0.000	0.000	0.000
23	A	24	PRO	0	0.021	0.001	21.528	-0.008	-0.008	0.000	0.000	0.000	0.000
24	A	25	GLU	-1	-0.870	-0.926	18.369	0.043	0.043	0.000	0.000	0.000	0.000
25	A	26	LYS	1	0.802	0.881	14.011	-0.062	-0.062	0.000	0.000	0.000	0.000
26	A	27	ARG	1	0.792	0.910	18.850	0.041	0.041	0.000	0.000	0.000	0.000
27	A	28	ILE	0	0.052	0.027	19.378	-0.009	-0.009	0.000	0.000	0.000	0.000
28	A	29	GLU	-1	-0.834	-0.930	22.233	-0.018	-0.018	0.000	0.000	0.000	0.000
29	A	30	LEU	0	-0.006	0.013	21.645	-0.002	-0.002	0.000	0.000	0.000	0.000
30	A	31	GLN	0	0.023	-0.004	17.720	-0.004	-0.004	0.000	0.000	0.000	0.000
31	A	32	LEU	0	-0.018	-0.010	22.945	-0.003	-0.003	0.000	0.000	0.000	0.000
32	A	33	GLU	-1	-0.935	-0.973	26.210	-0.036	-0.036	0.000	0.000	0.000	0.000
33	A	34	VAL	0	-0.018	-0.004	23.681	-0.001	-0.001	0.000	0.000	0.000	0.000
34	A	35	PHE	0	0.001	-0.012	22.059	-0.003	-0.003	0.000	0.000	0.000	0.000
35	A	36	LYS	1	0.893	0.981	27.255	0.032	0.032	0.000	0.000	0.000	0.000
36	A	37	LYS	1	0.906	0.963	29.946	0.056	0.056	0.000	0.000	0.000	0.000
37	A	38	LEU	0	-0.028	-0.008	25.815	0.000	0.000	0.000	0.000	0.000	0.000
38	A	39	GLN	0	0.006	-0.006	29.004	0.000	0.000	0.000	0.000	0.000	0.000
39	A	40	ASP	-1	-0.930	-0.956	30.386	-0.070	-0.070	0.000	0.000	0.000	0.000
40	A	41	GLU	-1	-0.876	-0.912	25.281	-0.111	-0.111	0.000	0.000	0.000	0.000
41	A	42	LYS	1	0.911	0.943	24.886	0.078	0.078	0.000	0.000	0.000	0.000
42	A	43	LEU	0	-0.014	0.015	19.324	-0.012	-0.012	0.000	0.000	0.000	0.000
43	A	44	TYR	0	-0.049	-0.028	19.515	0.015	0.015	0.000	0.000	0.000	0.000
44	A	45	ILE	0	0.036	0.009	18.502	-0.010	-0.010	0.000	0.000	0.000	0.000
45	A	46	VAL	0	0.019	0.016	14.497	0.012	0.012	0.000	0.000	0.000	0.000
46	A	47	GLY	0	0.002	-0.007	16.216	0.005	0.005	0.000	0.000	0.000	0.000
47	A	48	TRP	0	0.000	-0.016	17.709	-0.008	-0.008	0.000	0.000	0.000	0.000
48	A	49	PHE	0	-0.006	-0.014	20.442	0.002	0.002	0.000	0.000	0.000	0.000
49	A	50	SER	0	0.008	0.023	22.478	0.004	0.004	0.000	0.000	0.000	0.000
50	A	51	LYS	1	1.013	0.982	24.200	-0.065	-0.065	0.000	0.000	0.000	0.000
51	A	52	GLY	0	-0.070	-0.025	27.702	0.005	0.005	0.000	0.000	0.000	0.000
52	A	53	ASP	-1	-0.830	-0.902	25.675	0.087	0.087	0.000	0.000	0.000	0.000
53	A	54	HIS	0	0.032	0.002	28.118	-0.006	-0.006	0.000	0.000	0.000	0.000
54	A	55	ALA	0	-0.005	-0.006	24.705	-0.006	-0.006	0.000	0.000	0.000	0.000
55	A	56	GLU	-1	-0.793	-0.870	26.775	0.035	0.035	0.000	0.000	0.000	0.000
56	A	57	ARG	1	0.935	0.967	28.352	-0.024	-0.024	0.000	0.000	0.000	0.000
57	A	58	TYR	0	-0.092	-0.062	23.609	-0.004	-0.004	0.000	0.000	0.000	0.000
58	A	59	ALA	0	0.097	0.038	25.299	-0.006	-0.006	0.000	0.000	0.000	0.000
59	A	60	ARG	1	0.869	0.902	26.690	-0.033	-0.033	0.000	0.000	0.000	0.000
60	A	61	LYS	1	0.882	0.938	29.933	-0.005	-0.005	0.000	0.000	0.000	0.000
61	A	62	ILE	0	0.042	0.017	24.702	-0.004	-0.004	0.000	0.000	0.000	0.000
62	A	63	MET	0	-0.020	-0.015	26.543	-0.004	-0.004	0.000	0.000	0.000	0.000
63	A	64	LYS	1	0.899	0.982	28.709	-0.004	-0.004	0.000	0.000	0.000	0.000
64	A	65	ILE	0	-0.086	-0.037	29.154	-0.001	-0.001	0.000	0.000	0.000	0.000
65	A	66	ALA	0	-0.003	-0.006	27.643	-0.004	-0.004	0.000	0.000	0.000	0.000
66	A	67	PRO	0	-0.023	0.002	28.179	0.003	0.003	0.000	0.000	0.000	0.000
67	A	68	ASP	-1	-0.866	-0.952	29.648	-0.031	-0.031	0.000	0.000	0.000	0.000
68	A	69	ASN	0	-0.070	-0.020	28.273	0.004	0.004	0.000	0.000	0.000	0.000
69	A	70	VAL	0	-0.012	-0.010	23.947	-0.008	-0.008	0.000	0.000	0.000	0.000
70	A	71	LYS	1	0.928	0.973	24.018	0.051	0.051	0.000	0.000	0.000	0.000
71	A	72	PHE	0	0.018	0.000	22.768	-0.004	-0.004	0.000	0.000	0.000	0.000
72	A	73	LEU	0	0.002	-0.005	18.968	0.004	0.004	0.000	0.000	0.000	0.000
73	A	74	GLY	0	0.031	0.026	21.041	0.007	0.007	0.000	0.000	0.000	0.000
74	A	75	SER	0	-0.057	-0.052	17.636	0.001	0.001	0.000	0.000	0.000	0.000
75	A	76	VAL	0	0.033	0.034	14.860	-0.003	-0.003	0.000	0.000	0.000	0.000
76	A	77	SER	0	-0.011	-0.004	15.533	0.018	0.018	0.000	0.000	0.000	0.000
77	A	78	GLU	-1	-0.781	-0.887	9.242	0.100	0.100	0.000	0.000	0.000	0.000
78	A	79	GLU	-1	-0.902	-0.962	12.836	-0.003	-0.003	0.000	0.000	0.000	0.000
79	A	80	GLU	-1	-0.869	-0.936	15.347	-0.026	-0.026	0.000	0.000	0.000	0.000
80	A	81	LEU	0	-0.003	0.011	9.228	-0.026	-0.026	0.000	0.000	0.000	0.000
81	A	82	ILE	0	0.014	0.005	10.015	-0.050	-0.050	0.000	0.000	0.000	0.000
82	A	83	ASP	-1	-0.818	-0.867	12.123	-0.151	-0.151	0.000	0.000	0.000	0.000
83	A	84	LEU	0	0.019	0.020	15.059	-0.015	-0.015	0.000	0.000	0.000	0.000
84	A	85	TYR	0	0.005	-0.020	8.002	-0.020	-0.020	0.000	0.000	0.000	0.000
85	A	86	SER	0	-0.032	-0.035	13.058	-0.013	-0.013	0.000	0.000	0.000	0.000
86	A	87	ARG	1	0.833	0.869	14.729	0.111	0.111	0.000	0.000	0.000	0.000
87	A	88	CYS	0	-0.018	0.042	14.737	0.001	0.001	0.000	0.000	0.000	0.000
88	A	89	LYS	1	0.870	0.927	17.823	0.103	0.103	0.000	0.000	0.000	0.000
89	A	90	GLY	0	0.045	0.002	15.744	-0.019	-0.019	0.000	0.000	0.000	0.000
90	A	91	LEU	0	-0.057	-0.015	10.208	0.023	0.023	0.000	0.000	0.000	0.000
91	A	92	LEU	0	0.008	0.007	14.390	-0.008	-0.008	0.000	0.000	0.000	0.000
92	A	93	CYS	0	-0.049	-0.021	11.214	0.009	0.009	0.000	0.000	0.000	0.000
93	A	94	THR	0	0.046	-0.007	14.838	-0.005	-0.005	0.000	0.000	0.000	0.000
94	A	95	ALA	0	-0.011	0.005	14.348	0.011	0.011	0.000	0.000	0.000	0.000
95	A	96	LYS	1	0.936	0.963	16.021	-0.002	-0.002	0.000	0.000	0.000	0.000
96	A	97	ASP	-1	-0.832	-0.922	15.447	0.052	0.052	0.000	0.000	0.000	0.000
97	A	98	GLU	-1	-0.827	-0.899	10.407	0.007	0.007	0.000	0.000	0.000	0.000
98	A	99	ASP	-1	-0.885	-0.952	10.504	0.007	0.007	0.000	0.000	0.000	0.000
99	A	100	PHE	0	-0.015	-0.018	5.071	-0.005	-0.005	0.000	0.000	0.000	0.000
100	A	101	GLY	0	0.028	0.025	5.350	-0.166	-0.166	0.000	0.000	0.000	0.000
101	A	102	LEU	0	0.036	0.001	2.283	-0.396	-0.895	3.224	-0.477	-2.248	0.000
102	A	103	THR	0	0.058	0.034	4.522	-0.245	-0.176	-0.001	-0.008	-0.060	0.000
103	A	104	PRO	0	0.009	-0.002	7.221	-0.057	-0.057	0.000	0.000	0.000	0.000
104	A	105	ILE	0	0.004	0.016	2.409	-1.324	-0.342	1.400	-0.408	-1.974	-0.002
105	A	106	GLU	-1	-0.812	-0.903	4.149	-0.460	-0.245	0.000	-0.020	-0.195	0.000
106	A	107	ALA	0	0.002	0.005	5.870	0.043	0.043	0.000	0.000	0.000	0.000
107	A	108	MET	0	-0.043	-0.005	7.685	0.073	0.073	0.000	0.000	0.000	0.000
108	A	109	ALA	0	0.026	0.010	5.962	0.039	0.039	0.000	0.000	0.000	0.000
109	A	110	SER	0	-0.034	-0.020	8.116	0.116	0.116	0.000	0.000	0.000	0.000
110	A	111	GLY	0	-0.053	-0.033	11.078	0.092	0.092	0.000	0.000	0.000	0.000
111	A	112	LYS	1	0.682	0.830	12.389	0.327	0.327	0.000	0.000	0.000	0.000
112	A	113	PRO	0	0.028	0.023	12.722	-0.047	-0.047	0.000	0.000	0.000	0.000
113	A	114	VAL	0	0.004	-0.009	10.491	0.018	0.018	0.000	0.000	0.000	0.000
114	A	115	ILE	0	-0.022	0.008	13.951	0.003	0.003	0.000	0.000	0.000	0.000
115	A	116	ALA	0	0.011	-0.006	13.814	0.011	0.011	0.000	0.000	0.000	0.000
116	A	117	VAL	0	-0.007	0.014	15.905	0.000	0.000	0.000	0.000	0.000	0.000
117	A	118	ASN	0	0.022	0.002	15.851	-0.039	-0.039	0.000	0.000	0.000	0.000
118	A	119	GLU	-1	-0.878	-0.949	15.571	-0.051	-0.051	0.000	0.000	0.000	0.000
119	A	120	GLY	0	0.037	0.016	12.930	-0.020	-0.020	0.000	0.000	0.000	0.000
120	A	121	GLY	0	0.055	0.015	8.706	-0.028	-0.028	0.000	0.000	0.000	0.000
121	A	122	PHE	0	-0.014	-0.008	8.896	-0.111	-0.111	0.000	0.000	0.000	0.000
122	A	123	LYS	1	0.893	0.961	11.163	0.127	0.127	0.000	0.000	0.000	0.000
123	A	124	GLU	-1	-0.911	-0.949	9.133	-0.306	-0.306	0.000	0.000	0.000	0.000
124	A	125	THR	0	-0.045	-0.024	5.947	-0.092	-0.092	0.000	0.000	0.000	0.000
125	A	126	VAL	0	-0.021	-0.005	8.870	-0.055	-0.055	0.000	0.000	0.000	0.000
126	A	127	ILE	0	0.014	0.013	12.073	0.043	0.043	0.000	0.000	0.000	0.000
127	A	128	ASN	0	0.064	0.013	15.016	0.012	0.012	0.000	0.000	0.000	0.000
128	A	129	GLU	-1	-0.974	-1.001	18.210	-0.169	-0.169	0.000	0.000	0.000	0.000
129	A	130	LYS	1	0.878	0.948	16.913	0.274	0.274	0.000	0.000	0.000	0.000
130	A	131	THR	0	0.017	-0.014	12.209	0.000	0.000	0.000	0.000	0.000	0.000
131	A	132	GLY	0	0.036	0.012	14.103	-0.016	-0.016	0.000	0.000	0.000	0.000
132	A	133	TYR	0	-0.064	-0.031	16.426	0.016	0.016	0.000	0.000	0.000	0.000
133	A	134	LEU	0	-0.006	0.013	14.186	-0.002	-0.002	0.000	0.000	0.000	0.000
134	A	135	VAL	0	-0.025	-0.004	18.166	0.010	0.010	0.000	0.000	0.000	0.000
135	A	136	ASN	0	-0.021	-0.012	20.089	-0.004	-0.004	0.000	0.000	0.000	0.000
136	A	137	ALA	0	-0.020	-0.015	21.678	-0.002	-0.002	0.000	0.000	0.000	0.000
137	A	138	ASP	-1	-0.839	-0.919	22.811	-0.061	-0.061	0.000	0.000	0.000	0.000
138	A	139	VAL	0	0.021	-0.009	25.102	-0.007	-0.007	0.000	0.000	0.000	0.000
139	A	140	ASN	0	-0.019	-0.013	26.585	-0.002	-0.002	0.000	0.000	0.000	0.000
140	A	141	GLU	-1	-0.783	-0.894	24.540	-0.104	-0.104	0.000	0.000	0.000	0.000
141	A	142	ILE	0	0.006	0.000	21.206	-0.012	-0.012	0.000	0.000	0.000	0.000
142	A	143	ILE	0	0.011	0.000	23.259	-0.009	-0.009	0.000	0.000	0.000	0.000
143	A	144	ASP	-1	-0.890	-0.942	25.881	-0.097	-0.097	0.000	0.000	0.000	0.000
144	A	145	ALA	0	-0.063	-0.028	21.062	-0.007	-0.007	0.000	0.000	0.000	0.000
145	A	146	MET	0	0.014	-0.011	21.328	-0.009	-0.009	0.000	0.000	0.000	0.000
146	A	147	LYS	1	0.953	0.983	22.978	0.084	0.084	0.000	0.000	0.000	0.000
147	A	148	LYS	1	0.908	0.968	23.635	0.144	0.144	0.000	0.000	0.000	0.000
148	A	149	VAL	0	-0.005	-0.002	19.479	-0.003	-0.003	0.000	0.000	0.000	0.000
149	A	150	SER	0	-0.032	-0.028	22.471	0.000	0.000	0.000	0.000	0.000	0.000
150	A	151	LYS	1	0.902	0.957	25.164	0.102	0.102	0.000	0.000	0.000	0.000
151	A	152	ASN	0	-0.051	-0.018	24.676	0.000	0.000	0.000	0.000	0.000	0.000
152	A	153	PRO	0	0.047	0.032	21.557	-0.014	-0.014	0.000	0.000	0.000	0.000
153	A	154	ASP	-1	-0.918	-0.959	19.902	-0.216	-0.216	0.000	0.000	0.000	0.000
154	A	155	LYS	1	0.909	0.968	20.947	0.173	0.173	0.000	0.000	0.000	0.000
155	A	156	PHE	0	0.014	0.001	16.704	0.002	0.002	0.000	0.000	0.000	0.000
156	A	157	LYS	1	0.963	1.013	16.199	0.221	0.221	0.000	0.000	0.000	0.000
157	A	158	LYS	1	0.945	0.953	15.148	0.221	0.221	0.000	0.000	0.000	0.000
158	A	159	ASP	-1	-0.848	-0.922	15.129	-0.395	-0.395	0.000	0.000	0.000	0.000
159	A	160	CYS	0	-0.059	-0.004	11.930	-0.059	-0.059	0.000	0.000	0.000	0.000
160	A	161	PHE	0	-0.013	-0.009	10.643	-0.081	-0.081	0.000	0.000	0.000	0.000
161	A	162	ARG	1	0.825	0.916	10.326	0.345	0.345	0.000	0.000	0.000	0.000
162	A	163	ARG	1	0.895	0.937	9.071	0.649	0.649	0.000	0.000	0.000	0.000
163	A	164	ALA	0	0.009	0.003	6.121	-0.163	-0.163	0.000	0.000	0.000	0.000
164	A	165	LYS	1	0.907	0.945	5.184	0.146	0.135	-0.001	-0.002	0.014	0.000
165	A	166	GLU	-1	-0.938	-0.951	6.979	-0.919	-0.919	0.000	0.000	0.000	0.000
166	A	167	PHE	0	-0.010	0.014	2.409	-3.417	0.099	1.780	-1.974	-3.322	-0.019

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