FMO DATABASE

FMODB ID: 82MRY

Calculation Name: 2V1L-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2V1L

Chain ID: A

ChEMBL ID:

UniProt ID: Q9KR41

Base Structure: X-ray

Registration Date: 2023-06-20

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

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

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	132
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1182548.131973
FMO2-HF: Nuclear repulsion	1129546.082807
FMO2-HF: Total energy	-53002.049166
FMO2-MP2: Total energy	-53158.132322

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:5:LEU)

Summations of interaction energy for fragment #1(A:5: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.
-7.841	-3.311	2.949	-1.754	-5.726	-0.004

Interaction energy analysis for fragmet #1(A:5:LEU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.027 / q_NPA : -0.021

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	7	LYS	1	0.872	0.937	3.201	0.324	1.919	0.002	-0.651	-0.946	0.001
4	A	8	PRO	0	0.006	0.024	6.027	-0.350	-0.350	0.000	0.000	0.000	0.000
5	A	9	THR	0	0.041	0.009	9.028	-0.126	-0.126	0.000	0.000	0.000	0.000
6	A	10	HIS	0	-0.015	-0.009	12.365	0.116	0.116	0.000	0.000	0.000	0.000
7	A	11	LEU	0	0.028	0.022	14.462	-0.019	-0.019	0.000	0.000	0.000	0.000
8	A	12	PRO	0	-0.075	-0.024	13.755	0.077	0.077	0.000	0.000	0.000	0.000
9	A	13	ILE	0	-0.003	0.010	9.353	0.005	0.005	0.000	0.000	0.000	0.000
10	A	14	SER	0	-0.031	-0.031	10.749	0.277	0.277	0.000	0.000	0.000	0.000
11	A	15	LYS	1	0.939	0.954	7.440	-2.582	-2.582	0.000	0.000	0.000	0.000
12	A	16	PRO	0	-0.002	-0.012	8.201	0.122	0.122	0.000	0.000	0.000	0.000
13	A	17	PHE	0	0.091	0.063	9.420	-0.104	-0.104	0.000	0.000	0.000	0.000
14	A	18	HIS	0	-0.001	-0.010	4.359	0.370	0.472	-0.001	-0.008	-0.092	0.000
15	A	19	ALA	0	-0.033	-0.017	4.455	-0.579	-0.439	-0.001	-0.014	-0.125	0.000
16	A	20	LEU	0	0.032	0.027	6.236	-0.251	-0.251	0.000	0.000	0.000	0.000
17	A	21	LEU	0	0.024	0.016	5.387	-0.156	-0.156	0.000	0.000	0.000	0.000
18	A	22	ALA	0	-0.007	-0.016	2.298	-0.867	-0.752	1.453	-0.351	-1.217	-0.001
19	A	23	ASN	0	-0.108	-0.041	3.458	0.030	-0.067	0.017	0.244	-0.164	0.000
20	A	24	ILE	0	0.111	0.051	7.135	-0.108	-0.108	0.000	0.000	0.000	0.000
21	A	25	LEU	0	-0.046	-0.016	3.116	-0.541	-0.142	0.040	-0.085	-0.355	-0.001
22	A	26	SER	0	-0.076	-0.055	5.483	0.201	0.201	0.000	0.000	0.000	0.000
23	A	27	GLU	-1	-0.888	-0.948	6.840	-0.155	-0.155	0.000	0.000	0.000	0.000
24	A	28	HIS	0	0.005	0.009	9.681	0.070	0.070	0.000	0.000	0.000	0.000
25	A	29	GLN	0	-0.078	-0.030	6.675	-0.213	-0.213	0.000	0.000	0.000	0.000
26	A	30	ALA	0	-0.068	-0.023	10.091	0.095	0.095	0.000	0.000	0.000	0.000
27	A	40	GLU	-1	-0.989	-1.012	11.820	-0.567	-0.567	0.000	0.000	0.000	0.000
28	A	41	VAL	0	-0.061	-0.027	8.740	0.002	0.002	0.000	0.000	0.000	0.000
29	A	42	VAL	0	0.053	0.027	11.795	-0.042	-0.042	0.000	0.000	0.000	0.000
30	A	43	MET	0	-0.033	-0.008	7.407	0.028	0.028	0.000	0.000	0.000	0.000
31	A	44	ASN	0	-0.062	-0.043	13.485	0.032	0.032	0.000	0.000	0.000	0.000
32	A	45	PHE	0	0.024	0.005	11.849	-0.008	-0.008	0.000	0.000	0.000	0.000
33	A	46	ARG	1	0.798	0.848	17.972	0.210	0.210	0.000	0.000	0.000	0.000
34	A	47	ASP	-1	-0.707	-0.816	21.768	-0.044	-0.044	0.000	0.000	0.000	0.000
35	A	48	SER	0	-0.106	-0.093	24.600	0.002	0.002	0.000	0.000	0.000	0.000
36	A	49	SER	0	-0.099	-0.073	27.206	0.004	0.004	0.000	0.000	0.000	0.000
37	A	50	TYR	0	-0.028	0.007	27.027	0.004	0.004	0.000	0.000	0.000	0.000
38	A	51	SER	0	-0.011	-0.045	29.108	-0.008	-0.008	0.000	0.000	0.000	0.000
39	A	52	ALA	0	-0.033	-0.027	32.429	0.003	0.003	0.000	0.000	0.000	0.000
40	A	53	GLU	-1	-0.963	-1.000	34.315	-0.020	-0.020	0.000	0.000	0.000	0.000
41	A	54	ASP	-1	-0.907	-0.916	34.536	-0.026	-0.026	0.000	0.000	0.000	0.000
42	A	55	GLY	0	-0.046	-0.008	32.153	0.005	0.005	0.000	0.000	0.000	0.000
43	A	56	GLY	0	0.068	0.026	28.927	-0.006	-0.006	0.000	0.000	0.000	0.000
44	A	57	PHE	0	-0.096	-0.056	23.294	0.008	0.008	0.000	0.000	0.000	0.000
45	A	58	HIS	1	0.820	0.883	23.339	0.022	0.022	0.000	0.000	0.000	0.000
46	A	59	PRO	0	0.034	0.023	21.838	-0.002	-0.002	0.000	0.000	0.000	0.000
47	A	60	VAL	0	-0.047	-0.013	16.296	0.011	0.011	0.000	0.000	0.000	0.000
48	A	61	GLU	-1	-0.860	-0.905	16.634	-0.307	-0.307	0.000	0.000	0.000	0.000
49	A	62	ILE	0	-0.017	-0.011	10.757	0.038	0.038	0.000	0.000	0.000	0.000
50	A	63	ALA	0	0.022	0.039	12.792	-0.077	-0.077	0.000	0.000	0.000	0.000
51	A	64	LEU	0	-0.003	-0.016	6.541	-0.072	-0.072	0.000	0.000	0.000	0.000
52	A	65	SER	0	0.002	-0.024	8.859	0.066	0.066	0.000	0.000	0.000	0.000
53	A	66	GLN	0	-0.057	-0.019	7.105	-0.143	-0.143	0.000	0.000	0.000	0.000
54	A	67	SER	0	0.010	-0.015	7.431	0.352	0.352	0.000	0.000	0.000	0.000
55	A	68	SER	0	-0.005	-0.012	8.946	-0.012	-0.012	0.000	0.000	0.000	0.000
56	A	69	ASP	-1	-0.922	-0.931	7.549	-0.896	-0.896	0.000	0.000	0.000	0.000
57	A	70	GLY	0	0.002	0.003	6.604	0.123	0.123	0.000	0.000	0.000	0.000
58	A	71	GLN	0	-0.136	-0.071	2.959	-1.186	-0.275	0.155	-0.243	-0.824	0.000
59	A	72	TRP	0	0.062	0.012	2.423	-0.534	0.849	1.285	-0.637	-2.031	-0.003
60	A	73	CYS	0	-0.012	-0.002	5.015	0.060	0.042	-0.001	-0.009	0.028	0.000
61	A	74	ILE	0	-0.012	-0.010	8.088	-0.128	-0.128	0.000	0.000	0.000	0.000
62	A	75	GLU	-1	-0.834	-0.891	9.523	-0.472	-0.472	0.000	0.000	0.000	0.000
63	A	76	TYR	0	-0.060	-0.072	12.989	0.085	0.085	0.000	0.000	0.000	0.000
64	A	77	ILE	0	-0.030	0.001	12.642	-0.057	-0.057	0.000	0.000	0.000	0.000
65	A	78	THR	0	-0.036	-0.038	15.814	0.027	0.027	0.000	0.000	0.000	0.000
66	A	79	ASP	-1	-0.770	-0.854	19.224	-0.050	-0.050	0.000	0.000	0.000	0.000
67	A	80	PHE	0	0.022	-0.010	20.545	0.004	0.004	0.000	0.000	0.000	0.000
68	A	81	ALA	0	-0.003	-0.009	24.682	0.009	0.009	0.000	0.000	0.000	0.000
69	A	82	TYR	0	-0.003	0.005	28.085	-0.008	-0.008	0.000	0.000	0.000	0.000
70	A	83	VAL	0	-0.024	0.004	31.562	0.008	0.008	0.000	0.000	0.000	0.000
71	A	84	GLY	0	-0.011	-0.010	34.168	-0.003	-0.003	0.000	0.000	0.000	0.000
72	A	85	ASN	0	-0.014	-0.011	37.340	-0.001	-0.001	0.000	0.000	0.000	0.000
73	A	86	HIS	0	-0.048	-0.029	40.113	0.001	0.001	0.000	0.000	0.000	0.000
74	A	87	PHE	0	-0.019	-0.015	39.665	0.000	0.000	0.000	0.000	0.000	0.000
75	A	88	PRO	0	-0.031	0.015	35.360	-0.001	-0.001	0.000	0.000	0.000	0.000
76	A	89	GLU	-1	-0.913	-0.961	33.187	-0.077	-0.077	0.000	0.000	0.000	0.000
77	A	90	LEU	0	-0.036	-0.019	26.903	0.004	0.004	0.000	0.000	0.000	0.000
78	A	91	GLU	-1	-0.915	-0.956	28.678	-0.064	-0.064	0.000	0.000	0.000	0.000
79	A	92	ARG	1	0.856	0.901	21.863	0.155	0.155	0.000	0.000	0.000	0.000
80	A	93	CYS	0	-0.041	-0.010	25.516	0.014	0.014	0.000	0.000	0.000	0.000
81	A	94	LEU	0	-0.050	-0.034	22.535	0.017	0.017	0.000	0.000	0.000	0.000
82	A	95	ASP	-1	-0.782	-0.861	20.700	-0.157	-0.157	0.000	0.000	0.000	0.000
83	A	96	PHE	0	-0.015	-0.013	17.182	0.042	0.042	0.000	0.000	0.000	0.000
84	A	97	ASP	-1	-0.797	-0.899	16.954	-0.230	-0.230	0.000	0.000	0.000	0.000
85	A	98	PHE	0	-0.008	-0.036	13.450	0.074	0.074	0.000	0.000	0.000	0.000
86	A	99	GLN	0	-0.043	-0.010	14.950	0.053	0.053	0.000	0.000	0.000	0.000
87	A	100	ARG	1	0.772	0.883	17.024	0.121	0.121	0.000	0.000	0.000	0.000
88	A	101	GLY	0	-0.018	-0.002	19.215	0.022	0.022	0.000	0.000	0.000	0.000
89	A	102	ASP	-1	-0.831	-0.905	20.306	-0.026	-0.026	0.000	0.000	0.000	0.000
90	A	103	PHE	0	-0.038	-0.028	20.903	-0.007	-0.007	0.000	0.000	0.000	0.000
91	A	104	PHE	0	0.023	0.008	22.809	0.003	0.003	0.000	0.000	0.000	0.000
92	A	105	THR	0	0.027	-0.001	24.684	0.008	0.008	0.000	0.000	0.000	0.000
93	A	106	ALA	0	0.011	0.020	27.459	0.002	0.002	0.000	0.000	0.000	0.000
94	A	107	TYR	0	-0.031	-0.019	30.969	0.000	0.000	0.000	0.000	0.000	0.000
95	A	108	HIS	0	-0.029	-0.028	28.620	-0.003	-0.003	0.000	0.000	0.000	0.000
96	A	109	GLY	0	-0.003	0.014	30.710	0.001	0.001	0.000	0.000	0.000	0.000
97	A	110	TRP	0	-0.004	-0.008	23.530	0.002	0.002	0.000	0.000	0.000	0.000
98	A	111	ASN	0	-0.060	-0.033	26.405	0.011	0.011	0.000	0.000	0.000	0.000
99	A	112	PRO	0	0.059	0.041	24.389	-0.001	-0.001	0.000	0.000	0.000	0.000
100	A	113	ILE	0	0.006	-0.001	18.426	0.020	0.020	0.000	0.000	0.000	0.000
101	A	114	VAL	0	-0.046	-0.021	19.936	0.022	0.022	0.000	0.000	0.000	0.000
102	A	115	GLY	0	0.020	0.015	20.609	0.026	0.026	0.000	0.000	0.000	0.000
103	A	116	ASN	0	-0.049	-0.020	22.944	0.010	0.010	0.000	0.000	0.000	0.000
104	A	117	ARG	1	0.865	0.900	23.625	-0.076	-0.076	0.000	0.000	0.000	0.000
105	A	118	ASP	-1	-0.785	-0.869	25.136	0.075	0.075	0.000	0.000	0.000	0.000
106	A	119	ALA	0	0.040	0.036	22.089	0.003	0.003	0.000	0.000	0.000	0.000
107	A	120	ARG	1	0.868	0.918	19.307	-0.257	-0.257	0.000	0.000	0.000	0.000
108	A	121	GLU	-1	-0.898	-0.946	20.660	0.194	0.194	0.000	0.000	0.000	0.000
109	A	122	LEU	0	-0.008	0.002	22.782	0.007	0.007	0.000	0.000	0.000	0.000
110	A	123	TYR	0	0.008	-0.024	13.197	-0.033	-0.033	0.000	0.000	0.000	0.000
111	A	124	GLN	0	-0.037	-0.016	18.591	0.056	0.056	0.000	0.000	0.000	0.000
112	A	125	LEU	0	-0.021	-0.009	19.623	0.005	0.005	0.000	0.000	0.000	0.000
113	A	126	TRP	0	-0.008	-0.005	15.257	0.006	0.006	0.000	0.000	0.000	0.000
114	A	127	GLU	-1	-0.722	-0.830	12.884	0.408	0.408	0.000	0.000	0.000	0.000
115	A	128	SER	0	-0.056	-0.023	16.991	0.000	0.000	0.000	0.000	0.000	0.000
116	A	129	ASN	0	-0.029	-0.016	19.083	-0.012	-0.012	0.000	0.000	0.000	0.000
117	A	130	PHE	0	0.067	0.033	13.021	0.001	0.001	0.000	0.000	0.000	0.000
118	A	131	LEU	0	-0.017	-0.021	12.302	0.000	0.000	0.000	0.000	0.000	0.000
119	A	132	ALA	0	-0.019	-0.003	16.057	-0.005	-0.005	0.000	0.000	0.000	0.000
120	A	133	TYR	0	-0.017	-0.015	19.387	-0.012	-0.012	0.000	0.000	0.000	0.000
121	A	134	VAL	0	0.025	0.015	13.636	-0.013	-0.013	0.000	0.000	0.000	0.000
122	A	135	ALA	0	-0.072	-0.035	16.682	-0.005	-0.005	0.000	0.000	0.000	0.000
123	A	136	THR	0	-0.111	-0.072	17.698	0.002	0.002	0.000	0.000	0.000	0.000
124	A	137	GLU	-1	-0.954	-0.973	19.282	-0.020	-0.020	0.000	0.000	0.000	0.000
125	A	138	ALA	0	-0.040	-0.009	20.666	-0.011	-0.011	0.000	0.000	0.000	0.000
126	A	139	PHE	0	-0.061	-0.041	17.957	-0.006	-0.006	0.000	0.000	0.000	0.000
127	A	140	ASP	-1	-0.780	-0.849	20.005	-0.089	-0.089	0.000	0.000	0.000	0.000
128	A	141	ASP	-1	-0.840	-0.871	21.226	-0.179	-0.179	0.000	0.000	0.000	0.000
129	A	142	ILE	0	0.008	-0.001	14.539	-0.006	-0.006	0.000	0.000	0.000	0.000
130	A	143	SER	0	-0.011	0.006	16.506	0.009	0.009	0.000	0.000	0.000	0.000
131	A	144	LEU	0	-0.004	0.007	9.719	-0.034	-0.034	0.000	0.000	0.000	0.000
132	A	145	THR	0	-0.036	-0.015	14.122	0.039	0.039	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:5:LEU)