FMO DATABASE

FMODB ID: 2N58R

Calculation Name: 2A1V-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2A1V

Chain ID: A

ChEMBL ID:

UniProt ID: Q9RRT5

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	OptAll
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	138
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1251885.365385
FMO2-HF: Nuclear repulsion	1197870.478982
FMO2-HF: Total energy	-54014.886403
FMO2-MP2: Total energy	-54173.961005

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:3:LEU)

Summations of interaction energy for fragment #1(A:3:LEU)

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.
-6.277	-2.807	0.378	-1.78	-2.068	-0.008

Interaction energy analysis for fragmet #1(A:3:LEU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.001 / q_NPA : 0.001

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	5	THR	0	0.029	0.027	2.833	-3.507	-0.187	0.379	-1.773	-1.926	-0.008
4	A	6	PRO	0	0.024	-0.006	4.711	0.506	0.656	-0.001	-0.007	-0.142	0.000
5	A	7	MET	0	-0.085	-0.024	7.457	0.295	0.295	0.000	0.000	0.000	0.000
6	A	8	GLN	0	-0.029	-0.031	10.161	0.292	0.292	0.000	0.000	0.000	0.000
7	A	9	THR	0	-0.014	-0.009	11.160	0.142	0.142	0.000	0.000	0.000	0.000
8	A	10	VAL	0	0.055	0.002	13.379	-0.077	-0.077	0.000	0.000	0.000	0.000
9	A	11	ASP	-1	-0.867	-0.942	11.813	-0.765	-0.765	0.000	0.000	0.000	0.000
10	A	12	ASP	-1	-0.768	-0.864	8.391	-2.026	-2.026	0.000	0.000	0.000	0.000
11	A	13	LEU	0	-0.013	0.005	9.902	-0.145	-0.145	0.000	0.000	0.000	0.000
12	A	14	ARG	1	0.813	0.885	12.674	0.589	0.589	0.000	0.000	0.000	0.000
13	A	15	SER	0	-0.040	-0.032	7.384	-0.215	-0.215	0.000	0.000	0.000	0.000
14	A	16	VAL	0	-0.006	0.009	8.259	-0.079	-0.079	0.000	0.000	0.000	0.000
15	A	17	CYS	0	-0.051	-0.043	10.081	0.206	0.206	0.000	0.000	0.000	0.000
16	A	18	ASP	-1	-0.875	-0.935	11.911	-0.592	-0.592	0.000	0.000	0.000	0.000
17	A	19	GLU	-1	-0.874	-0.913	8.113	-1.102	-1.102	0.000	0.000	0.000	0.000
18	A	20	LEU	0	-0.059	-0.016	12.006	0.144	0.144	0.000	0.000	0.000	0.000
19	A	21	PRO	0	0.011	-0.005	15.189	0.028	0.028	0.000	0.000	0.000	0.000
20	A	22	HIS	0	-0.003	-0.012	18.530	-0.016	-0.016	0.000	0.000	0.000	0.000
21	A	23	SER	0	0.000	0.012	16.710	0.023	0.023	0.000	0.000	0.000	0.000
22	A	24	LEU	0	-0.022	-0.014	19.439	0.021	0.021	0.000	0.000	0.000	0.000
23	A	25	GLU	-1	-0.738	-0.833	17.824	-0.522	-0.522	0.000	0.000	0.000	0.000
24	A	26	THR	0	-0.088	-0.049	21.817	0.048	0.048	0.000	0.000	0.000	0.000
25	A	27	PHE	0	0.116	0.055	22.484	-0.024	-0.024	0.000	0.000	0.000	0.000
26	A	28	PRO	0	-0.124	-0.055	27.177	0.018	0.018	0.000	0.000	0.000	0.000
27	A	29	PHE	0	-0.004	-0.012	28.382	0.012	0.012	0.000	0.000	0.000	0.000
28	A	30	ASP	-1	-0.919	-0.952	31.186	-0.167	-0.167	0.000	0.000	0.000	0.000
29	A	31	ASP	-1	-0.871	-0.908	29.004	-0.238	-0.238	0.000	0.000	0.000	0.000
30	A	32	GLU	-1	-0.878	-0.946	25.269	-0.270	-0.270	0.000	0.000	0.000	0.000
31	A	33	THR	0	-0.087	-0.069	24.503	-0.041	-0.041	0.000	0.000	0.000	0.000
32	A	34	LEU	0	-0.017	0.022	18.726	0.020	0.020	0.000	0.000	0.000	0.000
33	A	35	VAL	0	-0.069	-0.053	22.881	-0.011	-0.011	0.000	0.000	0.000	0.000
34	A	36	PHE	0	0.065	0.043	16.505	0.031	0.031	0.000	0.000	0.000	0.000
35	A	37	LYS	1	0.885	0.919	21.111	0.264	0.264	0.000	0.000	0.000	0.000
36	A	38	VAL	0	0.037	0.025	20.817	-0.015	-0.015	0.000	0.000	0.000	0.000
37	A	39	GLY	0	-0.015	-0.012	22.690	0.020	0.020	0.000	0.000	0.000	0.000
38	A	40	TYR	0	-0.015	-0.034	25.481	-0.009	-0.009	0.000	0.000	0.000	0.000
39	A	41	LEU	0	0.033	0.010	26.838	-0.007	-0.007	0.000	0.000	0.000	0.000
40	A	42	SER	0	-0.012	0.001	29.317	-0.005	-0.005	0.000	0.000	0.000	0.000
41	A	43	LYS	1	0.746	0.849	30.507	0.133	0.133	0.000	0.000	0.000	0.000
42	A	44	SER	0	0.062	0.059	25.715	-0.005	-0.005	0.000	0.000	0.000	0.000
43	A	45	ARG	1	0.796	0.879	25.936	0.183	0.183	0.000	0.000	0.000	0.000
44	A	46	MET	0	0.044	0.024	24.402	-0.008	-0.008	0.000	0.000	0.000	0.000
45	A	47	TYR	0	-0.043	-0.039	16.639	0.013	0.013	0.000	0.000	0.000	0.000
46	A	48	ALA	0	0.033	0.041	18.611	-0.026	-0.026	0.000	0.000	0.000	0.000
47	A	49	LEU	0	-0.039	-0.014	20.604	0.029	0.029	0.000	0.000	0.000	0.000
48	A	50	THR	0	-0.008	-0.037	18.452	-0.041	-0.041	0.000	0.000	0.000	0.000
49	A	51	ASP	-1	-0.760	-0.860	21.605	-0.300	-0.300	0.000	0.000	0.000	0.000
50	A	52	ILE	0	-0.029	-0.030	20.135	-0.031	-0.031	0.000	0.000	0.000	0.000
51	A	53	THR	0	-0.022	-0.008	21.863	-0.003	-0.003	0.000	0.000	0.000	0.000
52	A	54	GLN	0	-0.135	-0.070	23.151	0.018	0.018	0.000	0.000	0.000	0.000
53	A	55	ASP	-1	-0.894	-0.937	19.355	-0.478	-0.478	0.000	0.000	0.000	0.000
54	A	56	PRO	0	-0.027	-0.018	18.669	0.037	0.037	0.000	0.000	0.000	0.000
55	A	57	LEU	0	0.026	0.024	16.118	0.020	0.020	0.000	0.000	0.000	0.000
56	A	58	ARG	1	0.887	0.941	19.369	0.342	0.342	0.000	0.000	0.000	0.000
57	A	59	LEU	0	0.033	0.062	15.539	0.021	0.021	0.000	0.000	0.000	0.000
58	A	60	SER	0	-0.035	-0.032	19.339	0.044	0.044	0.000	0.000	0.000	0.000
59	A	61	LEU	0	0.010	0.002	17.893	-0.014	-0.014	0.000	0.000	0.000	0.000
60	A	62	LYS	1	0.830	0.905	21.579	0.263	0.263	0.000	0.000	0.000	0.000
61	A	63	VAL	0	-0.009	-0.007	21.712	-0.024	-0.024	0.000	0.000	0.000	0.000
62	A	64	ASP	-1	-0.846	-0.934	23.965	-0.143	-0.143	0.000	0.000	0.000	0.000
63	A	65	PRO	0	-0.037	-0.032	26.302	-0.009	-0.009	0.000	0.000	0.000	0.000
64	A	66	GLU	-1	-0.932	-0.945	28.606	-0.112	-0.112	0.000	0.000	0.000	0.000
65	A	67	ARG	1	0.854	0.884	17.336	0.298	0.298	0.000	0.000	0.000	0.000
66	A	68	GLY	0	-0.006	-0.014	24.446	-0.021	-0.021	0.000	0.000	0.000	0.000
67	A	69	GLU	-1	-0.856	-0.896	26.108	-0.163	-0.163	0.000	0.000	0.000	0.000
68	A	70	GLU	-1	-0.895	-0.948	24.111	-0.174	-0.174	0.000	0.000	0.000	0.000
69	A	71	LEU	0	-0.034	-0.025	19.690	-0.009	-0.009	0.000	0.000	0.000	0.000
70	A	72	ARG	1	0.784	0.859	23.374	0.176	0.176	0.000	0.000	0.000	0.000
71	A	73	GLN	0	-0.022	-0.012	26.039	0.007	0.007	0.000	0.000	0.000	0.000
72	A	74	ALA	0	-0.038	-0.010	22.473	0.009	0.009	0.000	0.000	0.000	0.000
73	A	75	HIS	0	0.014	0.005	18.272	-0.016	-0.016	0.000	0.000	0.000	0.000
74	A	76	PRO	0	0.020	0.013	22.819	-0.016	-0.016	0.000	0.000	0.000	0.000
75	A	77	GLN	0	-0.057	-0.030	24.490	0.011	0.011	0.000	0.000	0.000	0.000
76	A	78	SER	0	-0.015	-0.015	20.085	0.009	0.009	0.000	0.000	0.000	0.000
77	A	79	ILE	0	-0.019	0.001	19.365	-0.034	-0.034	0.000	0.000	0.000	0.000
78	A	80	ALA	0	0.024	0.019	23.045	0.032	0.032	0.000	0.000	0.000	0.000
79	A	81	PRO	0	0.011	-0.017	25.994	-0.014	-0.014	0.000	0.000	0.000	0.000
80	A	82	GLY	0	0.027	0.005	26.899	0.003	0.003	0.000	0.000	0.000	0.000
81	A	83	TYR	0	0.011	0.016	27.248	0.030	0.030	0.000	0.000	0.000	0.000
82	A	84	HIS	0	0.009	0.008	28.885	-0.004	-0.004	0.000	0.000	0.000	0.000
83	A	85	LEU	0	0.032	0.038	26.485	0.003	0.003	0.000	0.000	0.000	0.000
84	A	86	ASN	0	-0.003	-0.009	30.732	0.017	0.017	0.000	0.000	0.000	0.000
85	A	87	LYS	1	0.891	0.916	30.316	0.194	0.194	0.000	0.000	0.000	0.000
86	A	88	LYS	1	0.918	0.962	30.796	0.140	0.140	0.000	0.000	0.000	0.000
87	A	89	HIS	0	-0.020	-0.002	28.646	-0.003	-0.003	0.000	0.000	0.000	0.000
88	A	90	TRP	0	0.042	0.030	23.381	-0.009	-0.009	0.000	0.000	0.000	0.000
89	A	91	VAL	0	0.025	0.021	22.267	0.025	0.025	0.000	0.000	0.000	0.000
90	A	92	THR	0	-0.012	-0.011	22.831	-0.004	-0.004	0.000	0.000	0.000	0.000
91	A	93	VAL	0	0.011	0.005	17.668	0.032	0.032	0.000	0.000	0.000	0.000
92	A	94	THR	0	0.002	0.006	19.487	-0.011	-0.011	0.000	0.000	0.000	0.000
93	A	95	LEU	0	-0.050	-0.013	14.317	-0.018	-0.018	0.000	0.000	0.000	0.000
94	A	96	ASP	-1	-0.764	-0.871	15.848	-0.482	-0.482	0.000	0.000	0.000	0.000
95	A	97	GLY	0	-0.007	0.006	13.042	0.012	0.012	0.000	0.000	0.000	0.000
96	A	98	THR	0	-0.095	-0.061	13.927	0.036	0.036	0.000	0.000	0.000	0.000
97	A	99	VAL	0	0.010	0.011	15.437	0.044	0.044	0.000	0.000	0.000	0.000
98	A	100	PRO	0	-0.003	-0.014	12.509	-0.094	-0.094	0.000	0.000	0.000	0.000
99	A	101	ALA	0	0.071	0.034	8.047	0.016	0.016	0.000	0.000	0.000	0.000
100	A	102	GLU	-1	-0.769	-0.860	7.822	-0.488	-0.488	0.000	0.000	0.000	0.000
101	A	103	LEU	0	-0.033	-0.005	9.594	0.073	0.073	0.000	0.000	0.000	0.000
102	A	104	LEU	0	0.007	0.005	11.748	0.051	0.051	0.000	0.000	0.000	0.000
103	A	105	GLY	0	0.053	0.026	10.003	0.026	0.026	0.000	0.000	0.000	0.000
104	A	106	GLU	-1	-0.847	-0.887	11.086	-0.288	-0.288	0.000	0.000	0.000	0.000
105	A	107	LEU	0	0.025	0.008	12.903	0.081	0.081	0.000	0.000	0.000	0.000
106	A	108	LEU	0	-0.004	0.011	12.533	0.095	0.095	0.000	0.000	0.000	0.000
107	A	109	ARG	1	0.799	0.862	8.873	0.962	0.962	0.000	0.000	0.000	0.000
108	A	110	GLY	0	0.014	0.004	14.527	0.092	0.092	0.000	0.000	0.000	0.000
109	A	111	SER	0	-0.028	-0.029	17.681	0.081	0.081	0.000	0.000	0.000	0.000
110	A	112	TYR	0	0.035	-0.007	17.026	0.057	0.057	0.000	0.000	0.000	0.000
111	A	113	LEU	0	-0.015	0.012	16.976	0.055	0.055	0.000	0.000	0.000	0.000
112	A	114	LEU	0	-0.020	0.001	20.183	0.041	0.041	0.000	0.000	0.000	0.000
113	A	115	VAL	0	-0.002	-0.016	22.597	0.035	0.035	0.000	0.000	0.000	0.000
114	A	116	THR	0	-0.016	-0.013	21.350	0.036	0.036	0.000	0.000	0.000	0.000
115	A	117	LYS	1	0.806	0.897	22.753	0.165	0.165	0.000	0.000	0.000	0.000
116	A	118	LYS	1	0.889	0.944	25.886	0.147	0.147	0.000	0.000	0.000	0.000
117	A	119	GLY	0	-0.018	0.000	27.522	0.011	0.011	0.000	0.000	0.000	0.000
118	A	120	PHE	0	-0.034	-0.010	25.874	0.007	0.007	0.000	0.000	0.000	0.000
119	A	121	THR	0	-0.013	-0.029	29.687	0.005	0.005	0.000	0.000	0.000	0.000
120	A	122	LYS	1	0.972	0.968	29.694	0.045	0.045	0.000	0.000	0.000	0.000
121	A	123	ALA	0	-0.006	0.002	30.291	0.003	0.003	0.000	0.000	0.000	0.000
122	A	124	GLU	-1	-0.651	-0.795	29.765	-0.111	-0.111	0.000	0.000	0.000	0.000
123	A	125	ARG	1	0.876	0.953	24.689	0.122	0.122	0.000	0.000	0.000	0.000
124	A	126	LYS	1	0.922	0.966	26.171	0.031	0.031	0.000	0.000	0.000	0.000
125	A	127	GLU	-1	-0.922	-0.934	28.208	-0.074	-0.074	0.000	0.000	0.000	0.000
126	A	128	LEU	0	-0.001	0.009	24.942	0.003	0.003	0.000	0.000	0.000	0.000
127	A	129	GLY	0	0.015	0.016	23.890	-0.005	-0.005	0.000	0.000	0.000	0.000
128	A	130	LEU	0	-0.040	-0.018	21.723	-0.012	-0.012	0.000	0.000	0.000	0.000
129	A	131	PRO	0	0.003	0.008	17.765	0.023	0.023	0.000	0.000	0.000	0.000
130	A	132	ASP	-1	-0.904	-0.950	20.752	-0.109	-0.109	0.000	0.000	0.000	0.000
131	A	133	SER	0	-0.026	-0.025	17.680	-0.001	-0.001	0.000	0.000	0.000	0.000
132	A	134	LEU	0	0.021	0.001	13.145	0.007	0.007	0.000	0.000	0.000	0.000
133	A	135	GLU	-1	-0.892	-0.936	12.036	0.213	0.213	0.000	0.000	0.000	0.000
134	A	136	GLY	0	0.034	0.017	8.231	-0.149	-0.149	0.000	0.000	0.000	0.000
135	A	137	GLY	0	-0.004	0.014	7.132	-0.272	-0.272	0.000	0.000	0.000	0.000
136	A	138	SER	0	-0.015	-0.027	5.463	0.181	0.181	0.000	0.000	0.000	0.000
137	A	139	HIS	0	0.011	0.011	6.796	-0.169	-0.169	0.000	0.000	0.000	0.000
138	A	140	HIS	1	0.793	0.888	8.424	-0.004	-0.004	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:3:LEU)