FMO DATABASE

FMODB ID: MNL6Z

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	OptAll
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	-1826818.170067
FMO2-HF: Nuclear repulsion	1759621.85775
FMO2-HF: Total energy	-67196.312317
FMO2-MP2: Total energy	-67391.723604

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.
-7.058	-3.979	15.052	-6.32	-11.811	-0.037

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 : 0.018 / 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

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	-0.022	-0.026	2.454	-1.988	1.079	0.901	-1.698	-2.270	-0.002
4	A	5	SER	0	-0.082	-0.062	4.593	0.620	0.738	-0.001	-0.015	-0.103	0.000
5	A	6	LYS	1	0.854	0.919	6.766	0.780	0.780	0.000	0.000	0.000	0.000
6	A	7	PHE	0	-0.002	0.009	5.117	0.198	0.198	0.000	0.000	0.000	0.000
7	A	8	LYS	1	0.884	0.933	9.362	0.415	0.415	0.000	0.000	0.000	0.000
8	A	9	PHE	0	0.041	0.022	12.510	0.052	0.052	0.000	0.000	0.000	0.000
9	A	10	LYS	1	0.827	0.908	15.262	0.200	0.200	0.000	0.000	0.000	0.000
10	A	11	CYS	0	-0.047	-0.025	18.728	0.013	0.013	0.000	0.000	0.000	0.000
11	A	12	TYR	0	0.003	-0.016	16.869	-0.012	-0.012	0.000	0.000	0.000	0.000
12	A	13	GLY	0	0.023	0.017	20.588	0.010	0.010	0.000	0.000	0.000	0.000
13	A	14	ASP	-1	-0.870	-0.931	22.549	-0.045	-0.045	0.000	0.000	0.000	0.000
14	A	15	PHE	0	-0.049	-0.015	18.471	0.008	0.008	0.000	0.000	0.000	0.000
15	A	16	TRP	0	-0.003	-0.008	17.516	-0.018	-0.018	0.000	0.000	0.000	0.000
16	A	17	LEU	0	-0.007	0.000	13.214	0.003	0.003	0.000	0.000	0.000	0.000
17	A	18	SER	0	0.017	-0.012	14.787	0.005	0.005	0.000	0.000	0.000	0.000
18	A	19	VAL	0	0.033	0.011	10.962	-0.015	-0.015	0.000	0.000	0.000	0.000
19	A	20	ASN	0	0.025	0.016	12.744	0.055	0.055	0.000	0.000	0.000	0.000
20	A	21	ARG	1	0.893	0.945	15.314	-0.258	-0.258	0.000	0.000	0.000	0.000
21	A	22	ILE	0	-0.013	0.001	17.888	0.002	0.002	0.000	0.000	0.000	0.000
22	A	23	TYR	0	0.025	-0.002	19.885	-0.014	-0.014	0.000	0.000	0.000	0.000
23	A	24	PRO	0	0.008	0.001	21.207	0.002	0.002	0.000	0.000	0.000	0.000
24	A	25	GLU	-1	-0.860	-0.923	18.224	0.250	0.250	0.000	0.000	0.000	0.000
25	A	26	LYS	1	0.785	0.860	13.376	-0.421	-0.421	0.000	0.000	0.000	0.000
26	A	27	ARG	1	0.765	0.855	18.524	-0.218	-0.218	0.000	0.000	0.000	0.000
27	A	28	ILE	0	0.037	0.023	19.288	-0.015	-0.015	0.000	0.000	0.000	0.000
28	A	29	GLU	-1	-0.745	-0.858	22.395	0.109	0.109	0.000	0.000	0.000	0.000
29	A	30	LEU	0	-0.030	0.006	21.407	-0.010	-0.010	0.000	0.000	0.000	0.000
30	A	31	GLN	0	0.025	0.010	17.655	-0.027	-0.027	0.000	0.000	0.000	0.000
31	A	32	LEU	0	-0.016	-0.005	22.818	-0.013	-0.013	0.000	0.000	0.000	0.000
32	A	33	GLU	-1	-0.855	-0.921	26.242	0.052	0.052	0.000	0.000	0.000	0.000
33	A	34	VAL	0	-0.016	0.000	23.163	-0.007	-0.007	0.000	0.000	0.000	0.000
34	A	35	PHE	0	-0.004	-0.010	21.822	-0.009	-0.009	0.000	0.000	0.000	0.000
35	A	36	LYS	1	0.832	0.920	27.092	-0.061	-0.061	0.000	0.000	0.000	0.000
36	A	37	LYS	1	0.893	0.969	29.696	-0.040	-0.040	0.000	0.000	0.000	0.000
37	A	38	LEU	0	-0.021	-0.010	25.461	-0.006	-0.006	0.000	0.000	0.000	0.000
38	A	39	GLN	0	-0.030	-0.030	28.617	-0.004	-0.004	0.000	0.000	0.000	0.000
39	A	40	ASP	-1	-0.879	-0.932	30.211	-0.010	-0.010	0.000	0.000	0.000	0.000
40	A	41	GLU	-1	-0.836	-0.879	24.577	-0.040	-0.040	0.000	0.000	0.000	0.000
41	A	42	LYS	1	0.896	0.924	24.945	0.034	0.034	0.000	0.000	0.000	0.000
42	A	43	LEU	0	-0.011	0.011	19.057	-0.008	-0.008	0.000	0.000	0.000	0.000
43	A	44	TYR	0	-0.026	-0.014	19.739	0.004	0.004	0.000	0.000	0.000	0.000
44	A	45	ILE	0	0.039	0.017	18.378	0.002	0.002	0.000	0.000	0.000	0.000
45	A	46	VAL	0	0.034	0.014	14.551	-0.001	-0.001	0.000	0.000	0.000	0.000
46	A	47	GLY	0	0.020	0.007	16.100	0.037	0.037	0.000	0.000	0.000	0.000
47	A	48	TRP	0	-0.001	-0.002	18.443	-0.024	-0.024	0.000	0.000	0.000	0.000
48	A	49	PHE	0	-0.014	-0.007	20.651	0.022	0.022	0.000	0.000	0.000	0.000
49	A	50	SER	0	0.001	-0.011	22.912	-0.008	-0.008	0.000	0.000	0.000	0.000
50	A	51	LYS	1	0.929	0.941	24.345	-0.110	-0.110	0.000	0.000	0.000	0.000
51	A	52	GLY	0	-0.012	-0.004	27.791	0.000	0.000	0.000	0.000	0.000	0.000
52	A	53	ASP	-1	-0.828	-0.873	25.689	0.172	0.172	0.000	0.000	0.000	0.000
53	A	54	HIS	0	0.006	-0.010	28.182	-0.012	-0.012	0.000	0.000	0.000	0.000
54	A	55	ALA	0	0.027	0.014	24.360	-0.006	-0.006	0.000	0.000	0.000	0.000
55	A	56	GLU	-1	-0.751	-0.849	26.437	0.091	0.091	0.000	0.000	0.000	0.000
56	A	57	ARG	1	0.936	0.967	28.431	-0.100	-0.100	0.000	0.000	0.000	0.000
57	A	58	TYR	0	-0.059	-0.053	23.518	-0.005	-0.005	0.000	0.000	0.000	0.000
58	A	59	ALA	0	0.073	0.029	25.324	-0.006	-0.006	0.000	0.000	0.000	0.000
59	A	60	ARG	1	0.844	0.891	26.862	-0.086	-0.086	0.000	0.000	0.000	0.000
60	A	61	LYS	1	0.815	0.906	29.315	-0.109	-0.109	0.000	0.000	0.000	0.000
61	A	62	ILE	0	0.008	0.002	24.641	-0.008	-0.008	0.000	0.000	0.000	0.000
62	A	63	MET	0	-0.037	-0.021	26.915	-0.008	-0.008	0.000	0.000	0.000	0.000
63	A	64	LYS	1	0.918	0.980	28.960	-0.068	-0.068	0.000	0.000	0.000	0.000
64	A	65	ILE	0	-0.063	-0.029	29.728	-0.003	-0.003	0.000	0.000	0.000	0.000
65	A	66	ALA	0	0.034	0.008	27.847	0.000	0.000	0.000	0.000	0.000	0.000
66	A	67	PRO	0	-0.026	0.004	28.200	-0.002	-0.002	0.000	0.000	0.000	0.000
67	A	68	ASP	-1	-0.883	-0.956	29.359	0.013	0.013	0.000	0.000	0.000	0.000
68	A	69	ASN	0	-0.063	-0.025	28.101	0.001	0.001	0.000	0.000	0.000	0.000
69	A	70	VAL	0	-0.027	-0.018	23.763	-0.003	-0.003	0.000	0.000	0.000	0.000
70	A	71	LYS	1	0.922	0.966	24.058	0.010	0.010	0.000	0.000	0.000	0.000
71	A	72	PHE	0	0.033	0.000	22.504	0.002	0.002	0.000	0.000	0.000	0.000
72	A	73	LEU	0	0.007	-0.003	19.095	-0.009	-0.009	0.000	0.000	0.000	0.000
73	A	74	GLY	0	0.025	0.013	21.297	-0.003	-0.003	0.000	0.000	0.000	0.000
74	A	75	SER	0	-0.070	-0.052	17.769	0.035	0.035	0.000	0.000	0.000	0.000
75	A	76	VAL	0	0.002	0.026	15.362	-0.007	-0.007	0.000	0.000	0.000	0.000
76	A	77	SER	0	0.002	-0.032	15.687	0.015	0.015	0.000	0.000	0.000	0.000
77	A	78	GLU	-1	-0.774	-0.883	8.853	-0.275	-0.275	0.000	0.000	0.000	0.000
78	A	79	GLU	-1	-0.862	-0.942	12.756	-0.146	-0.146	0.000	0.000	0.000	0.000
79	A	80	GLU	-1	-0.837	-0.887	15.292	-0.034	-0.034	0.000	0.000	0.000	0.000
80	A	81	LEU	0	-0.007	0.008	9.825	-0.007	-0.007	0.000	0.000	0.000	0.000
81	A	82	ILE	0	-0.004	-0.003	10.127	-0.026	-0.026	0.000	0.000	0.000	0.000
82	A	83	ASP	-1	-0.823	-0.865	12.396	-0.157	-0.157	0.000	0.000	0.000	0.000
83	A	84	LEU	0	0.014	0.015	15.293	-0.004	-0.004	0.000	0.000	0.000	0.000
84	A	85	TYR	0	0.010	-0.039	8.230	-0.009	-0.009	0.000	0.000	0.000	0.000
85	A	86	SER	0	-0.036	-0.026	13.145	-0.011	-0.011	0.000	0.000	0.000	0.000
86	A	87	ARG	1	0.823	0.872	14.942	0.106	0.106	0.000	0.000	0.000	0.000
87	A	88	CYS	0	-0.019	0.022	15.115	0.009	0.009	0.000	0.000	0.000	0.000
88	A	89	LYS	1	0.828	0.890	17.754	0.023	0.023	0.000	0.000	0.000	0.000
89	A	90	GLY	0	0.033	0.002	15.471	-0.020	-0.020	0.000	0.000	0.000	0.000
90	A	91	LEU	0	-0.045	-0.010	10.171	0.010	0.010	0.000	0.000	0.000	0.000
91	A	92	LEU	0	-0.004	0.000	14.321	-0.001	-0.001	0.000	0.000	0.000	0.000
92	A	93	CYS	0	-0.017	-0.002	11.930	0.007	0.007	0.000	0.000	0.000	0.000
93	A	94	THR	0	0.035	-0.006	14.873	-0.009	-0.009	0.000	0.000	0.000	0.000
94	A	95	ALA	0	-0.023	0.003	14.098	-0.008	-0.008	0.000	0.000	0.000	0.000
95	A	96	LYS	1	0.922	0.959	16.047	-0.238	-0.238	0.000	0.000	0.000	0.000
96	A	97	ASP	-1	-0.778	-0.882	14.956	0.426	0.426	0.000	0.000	0.000	0.000
97	A	98	GLU	-1	-0.821	-0.901	9.302	0.555	0.555	0.000	0.000	0.000	0.000
98	A	99	ASP	-1	-0.906	-0.968	9.664	0.670	0.670	0.000	0.000	0.000	0.000
99	A	100	PHE	0	-0.005	-0.007	5.090	0.049	0.049	0.000	0.000	0.000	0.000
100	A	101	GLY	0	-0.011	0.005	4.680	0.105	0.207	-0.001	-0.005	-0.096	0.000
101	A	102	LEU	0	0.015	-0.005	2.371	-0.512	-0.788	3.063	-0.424	-2.363	0.000
102	A	103	THR	0	0.042	0.024	4.662	-0.477	-0.412	-0.001	-0.006	-0.058	0.000
103	A	104	PRO	0	0.024	-0.012	7.432	-0.152	-0.152	0.000	0.000	0.000	0.000
104	A	105	ILE	0	-0.004	0.015	2.401	-1.364	-0.645	2.015	-0.466	-2.267	-0.003
105	A	106	GLU	-1	-0.807	-0.872	4.485	-0.245	-0.131	-0.001	-0.008	-0.105	0.000
106	A	107	ALA	0	0.008	0.008	6.061	-0.055	-0.055	0.000	0.000	0.000	0.000
107	A	108	MET	0	-0.043	-0.010	7.371	-0.025	-0.025	0.000	0.000	0.000	0.000
108	A	109	ALA	0	0.021	0.002	5.831	-0.024	-0.024	0.000	0.000	0.000	0.000
109	A	110	SER	0	-0.050	-0.028	8.001	0.033	0.033	0.000	0.000	0.000	0.000
110	A	111	GLY	0	-0.020	-0.019	11.081	0.079	0.079	0.000	0.000	0.000	0.000
111	A	112	LYS	1	0.702	0.836	12.148	0.265	0.265	0.000	0.000	0.000	0.000
112	A	113	PRO	0	0.032	0.024	12.394	-0.018	-0.018	0.000	0.000	0.000	0.000
113	A	114	VAL	0	-0.004	-0.007	10.218	0.013	0.013	0.000	0.000	0.000	0.000
114	A	115	ILE	0	-0.025	0.000	13.692	-0.002	-0.002	0.000	0.000	0.000	0.000
115	A	116	ALA	0	0.010	-0.001	13.686	0.016	0.016	0.000	0.000	0.000	0.000
116	A	117	VAL	0	0.024	0.026	15.813	-0.017	-0.017	0.000	0.000	0.000	0.000
117	A	118	ASN	0	-0.011	-0.002	15.529	0.029	0.029	0.000	0.000	0.000	0.000
118	A	119	GLU	-1	-0.826	-0.902	15.418	0.227	0.227	0.000	0.000	0.000	0.000
119	A	120	GLY	0	0.055	0.025	12.535	0.007	0.007	0.000	0.000	0.000	0.000
120	A	121	GLY	0	0.064	0.029	8.255	-0.025	-0.025	0.000	0.000	0.000	0.000
121	A	122	PHE	0	-0.023	-0.005	8.620	-0.052	-0.052	0.000	0.000	0.000	0.000
122	A	123	LYS	1	0.821	0.916	10.751	-0.368	-0.368	0.000	0.000	0.000	0.000
123	A	124	GLU	-1	-0.820	-0.888	8.591	0.334	0.334	0.000	0.000	0.000	0.000
124	A	125	THR	0	-0.059	-0.040	5.615	-0.110	-0.110	0.000	0.000	0.000	0.000
125	A	126	VAL	0	-0.011	0.002	8.555	-0.153	-0.153	0.000	0.000	0.000	0.000
126	A	127	ILE	0	0.018	0.012	11.789	0.034	0.034	0.000	0.000	0.000	0.000
127	A	128	ASN	0	0.089	0.032	14.611	-0.022	-0.022	0.000	0.000	0.000	0.000
128	A	129	GLU	-1	-0.854	-0.938	17.758	-0.039	-0.039	0.000	0.000	0.000	0.000
129	A	130	LYS	1	0.900	0.945	17.201	0.089	0.089	0.000	0.000	0.000	0.000
130	A	131	THR	0	0.005	-0.015	11.956	-0.021	-0.021	0.000	0.000	0.000	0.000
131	A	132	GLY	0	0.037	0.007	13.653	-0.011	-0.011	0.000	0.000	0.000	0.000
132	A	133	TYR	0	-0.079	-0.039	15.801	-0.006	-0.006	0.000	0.000	0.000	0.000
133	A	134	LEU	0	-0.016	0.003	13.837	0.009	0.009	0.000	0.000	0.000	0.000
134	A	135	VAL	0	-0.021	0.004	17.852	-0.012	-0.012	0.000	0.000	0.000	0.000
135	A	136	ASN	0	-0.029	-0.048	19.892	0.035	0.035	0.000	0.000	0.000	0.000
136	A	137	ALA	0	-0.032	-0.019	21.449	-0.003	-0.003	0.000	0.000	0.000	0.000
137	A	138	ASP	-1	-0.820	-0.915	22.571	0.058	0.058	0.000	0.000	0.000	0.000
138	A	139	VAL	0	-0.021	-0.020	24.707	-0.003	-0.003	0.000	0.000	0.000	0.000
139	A	140	ASN	0	-0.068	-0.049	26.656	-0.006	-0.006	0.000	0.000	0.000	0.000
140	A	141	GLU	-1	-0.746	-0.856	24.268	0.061	0.061	0.000	0.000	0.000	0.000
141	A	142	ILE	0	0.016	0.009	20.761	-0.009	-0.009	0.000	0.000	0.000	0.000
142	A	143	ILE	0	0.031	0.012	22.913	-0.012	-0.012	0.000	0.000	0.000	0.000
143	A	144	ASP	-1	-0.861	-0.922	25.612	0.006	0.006	0.000	0.000	0.000	0.000
144	A	145	ALA	0	-0.019	-0.008	21.006	-0.012	-0.012	0.000	0.000	0.000	0.000
145	A	146	MET	0	0.007	-0.003	21.088	-0.010	-0.010	0.000	0.000	0.000	0.000
146	A	147	LYS	1	0.874	0.946	22.818	-0.003	-0.003	0.000	0.000	0.000	0.000
147	A	148	LYS	1	0.809	0.912	23.252	0.014	0.014	0.000	0.000	0.000	0.000
148	A	149	VAL	0	-0.011	-0.004	19.058	-0.011	-0.011	0.000	0.000	0.000	0.000
149	A	150	SER	0	-0.029	-0.029	22.228	-0.011	-0.011	0.000	0.000	0.000	0.000
150	A	151	LYS	1	0.912	0.969	25.026	0.041	0.041	0.000	0.000	0.000	0.000
151	A	152	ASN	0	-0.072	-0.038	24.326	-0.005	-0.005	0.000	0.000	0.000	0.000
152	A	153	PRO	0	0.050	0.035	20.998	-0.004	-0.004	0.000	0.000	0.000	0.000
153	A	154	ASP	-1	-0.890	-0.953	19.390	-0.171	-0.171	0.000	0.000	0.000	0.000
154	A	155	LYS	1	0.905	0.981	20.063	0.076	0.076	0.000	0.000	0.000	0.000
155	A	156	PHE	0	0.004	-0.002	16.195	-0.001	-0.001	0.000	0.000	0.000	0.000
156	A	157	LYS	1	0.889	0.980	15.823	0.222	0.222	0.000	0.000	0.000	0.000
157	A	158	LYS	1	0.946	0.964	14.711	0.179	0.179	0.000	0.000	0.000	0.000
158	A	159	ASP	-1	-0.791	-0.880	14.649	-0.330	-0.330	0.000	0.000	0.000	0.000
159	A	160	CYS	0	-0.060	-0.002	11.549	-0.025	-0.025	0.000	0.000	0.000	0.000
160	A	161	PHE	0	0.012	0.004	10.205	-0.083	-0.083	0.000	0.000	0.000	0.000
161	A	162	ARG	1	0.760	0.888	10.607	0.238	0.238	0.000	0.000	0.000	0.000
162	A	163	ARG	1	0.880	0.917	8.606	0.029	0.029	0.000	0.000	0.000	0.000
163	A	164	ALA	0	-0.008	-0.002	5.994	-0.086	-0.086	0.000	0.000	0.000	0.000
164	A	165	LYS	1	0.876	0.925	5.390	0.366	0.366	0.000	0.000	0.000	0.000
165	A	166	GLU	-1	-0.881	-0.927	7.201	-0.616	-0.616	0.000	0.000	0.000	0.000
166	A	167	PHE	0	-0.003	0.006	1.915	-4.817	-5.647	9.077	-3.698	-4.549	-0.032

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