FMO DATABASE

FMODB ID: LNL59

Calculation Name: 4V2B-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4V2B

Chain ID: A

ChEMBL ID:

UniProt ID: F1LW30

Base Structure: X-ray

Registration Date: 2023-09-20

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

DOI:

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	108
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-864303.521846
FMO2-HF: Nuclear repulsion	819485.284937
FMO2-HF: Total energy	-44818.236909
FMO2-MP2: Total energy	-44947.642488

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:47:ALA)

Summations of interaction energy for fragment #1(A:47:ALA)

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.
3.614	-2.509	4.181	5.42	-3.477	-0.035

Interaction energy analysis for fragmet #1(A:47:ALA)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.025 / q_NPA : 0.036

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	49	GLY	0	0.007	0.004	2.571	8.699	2.010	0.984	7.176	-1.470	-0.010
4	A	50	THR	0	-0.004	-0.021	2.119	-5.700	-5.191	3.199	-1.743	-1.966	-0.025
5	A	51	LEU	0	0.020	0.015	4.683	-0.082	-0.059	-0.001	-0.010	-0.011	0.000
6	A	52	PRO	0	-0.005	0.002	8.008	0.215	0.215	0.000	0.000	0.000	0.000
7	A	53	HIS	0	0.024	0.031	10.606	0.064	0.064	0.000	0.000	0.000	0.000
8	A	54	PHE	0	0.006	-0.022	12.081	-0.052	-0.052	0.000	0.000	0.000	0.000
9	A	55	ILE	0	-0.037	-0.021	15.709	0.036	0.036	0.000	0.000	0.000	0.000
10	A	56	GLU	-1	-0.815	-0.892	17.583	0.157	0.157	0.000	0.000	0.000	0.000
11	A	57	GLU	-1	-0.817	-0.911	19.754	0.121	0.121	0.000	0.000	0.000	0.000
12	A	58	PRO	0	-0.016	0.009	21.918	-0.003	-0.003	0.000	0.000	0.000	0.000
13	A	59	GLU	-1	-0.888	-0.945	25.296	0.100	0.100	0.000	0.000	0.000	0.000
14	A	60	ASP	-1	-0.786	-0.861	28.030	0.048	0.048	0.000	0.000	0.000	0.000
15	A	61	ALA	0	-0.003	0.005	31.082	0.002	0.002	0.000	0.000	0.000	0.000
16	A	62	TYR	0	0.027	-0.001	33.920	-0.005	-0.005	0.000	0.000	0.000	0.000
17	A	63	ILE	0	0.014	0.017	37.746	0.001	0.001	0.000	0.000	0.000	0.000
18	A	64	ILE	0	-0.037	-0.022	40.091	-0.002	-0.002	0.000	0.000	0.000	0.000
19	A	65	LYS	1	0.907	0.943	43.252	-0.021	-0.021	0.000	0.000	0.000	0.000
20	A	66	SER	0	-0.009	-0.011	44.250	-0.001	-0.001	0.000	0.000	0.000	0.000
21	A	67	ASN	0	-0.036	-0.006	40.019	-0.003	-0.003	0.000	0.000	0.000	0.000
22	A	68	PRO	0	0.016	0.008	37.664	0.001	0.001	0.000	0.000	0.000	0.000
23	A	69	ILE	0	-0.028	-0.001	33.010	0.004	0.004	0.000	0.000	0.000	0.000
24	A	70	ALA	0	0.030	0.003	31.731	-0.005	-0.005	0.000	0.000	0.000	0.000
25	A	71	LEU	0	-0.026	-0.008	27.832	0.007	0.007	0.000	0.000	0.000	0.000
26	A	72	ARG	1	0.804	0.873	24.053	-0.119	-0.119	0.000	0.000	0.000	0.000
27	A	73	CYS	0	-0.035	0.003	20.729	-0.011	-0.011	0.000	0.000	0.000	0.000
28	A	74	LYS	1	0.809	0.892	19.132	-0.115	-0.115	0.000	0.000	0.000	0.000
29	A	75	ALA	0	-0.015	-0.006	14.695	0.026	0.026	0.000	0.000	0.000	0.000
30	A	76	ARG	1	0.781	0.873	10.901	-0.501	-0.501	0.000	0.000	0.000	0.000
31	A	77	PRO	0	-0.044	-0.010	8.088	0.108	0.108	0.000	0.000	0.000	0.000
32	A	78	ALA	0	0.003	-0.011	11.392	-0.057	-0.057	0.000	0.000	0.000	0.000
33	A	79	MET	0	-0.042	-0.020	13.117	0.005	0.005	0.000	0.000	0.000	0.000
34	A	80	GLN	0	0.000	-0.006	16.516	0.026	0.026	0.000	0.000	0.000	0.000
35	A	81	ILE	0	0.006	-0.006	17.616	-0.009	-0.009	0.000	0.000	0.000	0.000
36	A	82	PHE	0	-0.011	0.003	19.977	0.002	0.002	0.000	0.000	0.000	0.000
37	A	83	PHE	0	0.048	0.007	22.296	0.005	0.005	0.000	0.000	0.000	0.000
38	A	84	LYS	1	0.815	0.913	24.275	0.059	0.059	0.000	0.000	0.000	0.000
39	A	85	CYS	0	-0.017	-0.014	26.294	0.001	0.001	0.000	0.000	0.000	0.000
40	A	86	ASN	0	0.048	0.019	29.509	-0.002	-0.002	0.000	0.000	0.000	0.000
41	A	87	GLY	0	0.026	0.018	29.074	0.000	0.000	0.000	0.000	0.000	0.000
42	A	88	GLU	-1	-0.885	-0.932	28.632	-0.054	-0.054	0.000	0.000	0.000	0.000
43	A	89	TRP	0	-0.066	-0.045	21.459	0.003	0.003	0.000	0.000	0.000	0.000
44	A	90	VAL	0	0.023	0.015	28.049	0.002	0.002	0.000	0.000	0.000	0.000
45	A	91	HIS	0	0.030	0.016	28.882	-0.011	-0.011	0.000	0.000	0.000	0.000
46	A	92	GLN	0	0.010	0.000	27.615	-0.001	-0.001	0.000	0.000	0.000	0.000
47	A	93	ASN	0	-0.040	-0.020	29.709	0.000	0.000	0.000	0.000	0.000	0.000
48	A	94	GLU	-1	-0.843	-0.927	31.889	-0.024	-0.024	0.000	0.000	0.000	0.000
49	A	95	HIS	0	-0.053	-0.023	25.709	0.008	0.008	0.000	0.000	0.000	0.000
50	A	96	VAL	0	0.008	0.015	28.840	-0.004	-0.004	0.000	0.000	0.000	0.000
51	A	97	SER	0	-0.005	-0.019	24.428	0.001	0.001	0.000	0.000	0.000	0.000
52	A	98	GLU	-1	-0.817	-0.873	23.267	0.060	0.060	0.000	0.000	0.000	0.000
53	A	99	GLU	-1	-0.824	-0.894	19.820	-0.069	-0.069	0.000	0.000	0.000	0.000
54	A	100	SER	0	-0.031	-0.029	20.367	0.004	0.004	0.000	0.000	0.000	0.000
55	A	101	LEU	0	-0.051	-0.040	17.418	-0.016	-0.016	0.000	0.000	0.000	0.000
56	A	102	ASP	-1	-0.802	-0.889	15.035	0.268	0.268	0.000	0.000	0.000	0.000
57	A	102	GLU	-1	-0.786	-0.867	10.896	0.651	0.651	0.000	0.000	0.000	0.000
58	A	102	SER	0	-0.014	-0.013	8.768	-0.124	-0.124	0.000	0.000	0.000	0.000
59	A	102	SER	0	-0.049	-0.036	11.067	-0.078	-0.078	0.000	0.000	0.000	0.000
60	A	102	GLY	0	-0.003	0.014	13.236	-0.051	-0.051	0.000	0.000	0.000	0.000
61	A	103	LEU	0	-0.051	-0.017	9.109	-0.061	-0.061	0.000	0.000	0.000	0.000
62	A	104	LYS	1	0.888	0.923	13.042	0.086	0.086	0.000	0.000	0.000	0.000
63	A	105	VAL	0	0.015	0.008	14.559	0.014	0.014	0.000	0.000	0.000	0.000
64	A	106	ARG	1	0.857	0.918	17.108	0.030	0.030	0.000	0.000	0.000	0.000
65	A	107	GLU	-1	-0.772	-0.869	19.315	0.113	0.113	0.000	0.000	0.000	0.000
66	A	108	VAL	0	-0.044	-0.025	22.094	-0.015	-0.015	0.000	0.000	0.000	0.000
67	A	109	PHE	0	0.010	0.004	24.403	0.011	0.011	0.000	0.000	0.000	0.000
68	A	110	ILE	0	0.008	0.023	27.666	-0.009	-0.009	0.000	0.000	0.000	0.000
69	A	111	ASN	0	-0.019	-0.016	30.034	0.011	0.011	0.000	0.000	0.000	0.000
70	A	112	VAL	0	0.005	0.009	32.808	-0.005	-0.005	0.000	0.000	0.000	0.000
71	A	113	THR	0	0.006	-0.026	35.586	0.004	0.004	0.000	0.000	0.000	0.000
72	A	114	ARG	1	0.820	0.878	39.308	-0.008	-0.008	0.000	0.000	0.000	0.000
73	A	115	GLN	0	0.002	-0.007	41.844	-0.001	-0.001	0.000	0.000	0.000	0.000
74	A	116	GLN	0	0.062	0.046	35.289	0.001	0.001	0.000	0.000	0.000	0.000
75	A	117	VAL	0	-0.006	0.002	37.039	-0.001	-0.001	0.000	0.000	0.000	0.000
76	A	118	GLU	-1	-0.812	-0.882	39.469	0.005	0.005	0.000	0.000	0.000	0.000
77	A	119	ASP	-1	-0.883	-0.929	41.538	-0.008	-0.008	0.000	0.000	0.000	0.000
78	A	120	PHE	0	-0.100	-0.046	35.560	-0.003	-0.003	0.000	0.000	0.000	0.000
79	A	121	HIS	0	-0.047	-0.025	40.229	0.003	0.003	0.000	0.000	0.000	0.000
80	A	122	GLY	0	0.006	0.015	37.850	-0.002	-0.002	0.000	0.000	0.000	0.000
81	A	123	PRO	0	-0.038	-0.027	36.360	0.002	0.002	0.000	0.000	0.000	0.000
82	A	124	GLU	-1	-0.874	-0.942	32.119	0.008	0.008	0.000	0.000	0.000	0.000
83	A	125	ASP	-1	-0.807	-0.902	34.736	0.024	0.024	0.000	0.000	0.000	0.000
84	A	126	TYR	0	-0.005	0.006	32.677	-0.003	-0.003	0.000	0.000	0.000	0.000
85	A	127	TRP	0	-0.038	-0.019	26.428	0.007	0.007	0.000	0.000	0.000	0.000
86	A	129	GLN	0	0.005	0.009	21.463	-0.009	-0.009	0.000	0.000	0.000	0.000
87	A	131	VAL	0	-0.029	-0.018	18.146	0.004	0.004	0.000	0.000	0.000	0.000
88	A	132	ALA	0	0.056	0.031	15.186	0.002	0.002	0.000	0.000	0.000	0.000
89	A	133	TRP	0	0.009	-0.005	14.377	-0.023	-0.023	0.000	0.000	0.000	0.000
90	A	134	SER	0	0.014	0.001	8.619	0.017	0.017	0.000	0.000	0.000	0.000
91	A	135	HIS	0	0.039	0.011	7.462	0.161	0.161	0.000	0.000	0.000	0.000
92	A	136	LEU	0	-0.027	-0.006	4.753	-0.187	-0.153	-0.001	-0.003	-0.030	0.000
93	A	137	GLY	0	-0.005	0.008	9.034	0.007	0.007	0.000	0.000	0.000	0.000
94	A	138	THR	0	-0.038	-0.023	11.757	0.044	0.044	0.000	0.000	0.000	0.000
95	A	139	SER	0	-0.019	-0.019	12.093	-0.028	-0.028	0.000	0.000	0.000	0.000
96	A	140	LYS	1	0.857	0.905	14.064	0.033	0.033	0.000	0.000	0.000	0.000
97	A	141	SER	0	0.034	0.034	17.312	0.018	0.018	0.000	0.000	0.000	0.000
98	A	142	ARG	1	0.788	0.874	19.543	-0.105	-0.105	0.000	0.000	0.000	0.000
99	A	143	LYS	1	0.824	0.935	22.488	-0.019	-0.019	0.000	0.000	0.000	0.000
100	A	144	ALA	0	-0.015	0.003	25.737	0.010	0.010	0.000	0.000	0.000	0.000
101	A	145	SER	0	-0.015	-0.039	27.971	-0.011	-0.011	0.000	0.000	0.000	0.000
102	A	146	VAL	0	-0.035	-0.018	31.713	0.005	0.005	0.000	0.000	0.000	0.000
103	A	147	ARG	1	0.806	0.896	33.559	-0.043	-0.043	0.000	0.000	0.000	0.000
104	A	148	ILE	0	0.010	0.003	38.160	0.002	0.002	0.000	0.000	0.000	0.000
105	A	149	ALA	0	-0.005	0.005	41.561	0.001	0.001	0.000	0.000	0.000	0.000
106	A	150	TYR	0	0.020	-0.013	43.408	-0.001	-0.001	0.000	0.000	0.000	0.000
107	A	151	LEU	0	0.017	0.014	44.353	0.001	0.001	0.000	0.000	0.000	0.000
108	A	152	ARG	1	1.023	1.024	47.802	-0.032	-0.032	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:47:ALA)