FMO DATABASE

FMODB ID: 3JN2L

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	OptHSide
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	-861242.980553
FMO2-HF: Nuclear repulsion	816425.10287
FMO2-HF: Total energy	-44817.877683
FMO2-MP2: Total energy	-44947.239571

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.
4.562	0.803	1.138	4.953	-2.332	-0.02

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 : 0.040 / q_NPA : 0.041

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	-0.005	-0.002	2.630	7.085	1.742	0.847	5.793	-1.296	-0.010
4	A	50	THR	0	-0.001	-0.020	2.732	-3.000	-1.422	0.292	-0.840	-1.031	-0.010
5	A	51	LEU	0	0.017	0.010	5.297	-0.214	-0.208	-0.001	0.000	-0.005	0.000
6	A	52	PRO	0	-0.013	-0.004	8.298	0.187	0.187	0.000	0.000	0.000	0.000
7	A	53	HIS	0	0.029	0.037	11.122	0.069	0.069	0.000	0.000	0.000	0.000
8	A	54	PHE	0	0.004	-0.025	12.744	-0.044	-0.044	0.000	0.000	0.000	0.000
9	A	55	ILE	0	-0.062	-0.026	16.563	0.034	0.034	0.000	0.000	0.000	0.000
10	A	56	GLU	-1	-0.819	-0.906	18.569	0.162	0.162	0.000	0.000	0.000	0.000
11	A	57	GLU	-1	-0.835	-0.916	20.079	0.164	0.164	0.000	0.000	0.000	0.000
12	A	58	PRO	0	-0.025	0.003	22.424	-0.005	-0.005	0.000	0.000	0.000	0.000
13	A	59	GLU	-1	-0.884	-0.943	25.784	0.115	0.115	0.000	0.000	0.000	0.000
14	A	60	ASP	-1	-0.833	-0.894	28.558	0.071	0.071	0.000	0.000	0.000	0.000
15	A	61	ALA	0	0.012	0.016	31.638	0.002	0.002	0.000	0.000	0.000	0.000
16	A	62	TYR	0	0.028	-0.003	34.469	-0.005	-0.005	0.000	0.000	0.000	0.000
17	A	63	ILE	0	0.003	0.013	38.269	0.000	0.000	0.000	0.000	0.000	0.000
18	A	64	ILE	0	-0.028	-0.021	40.726	-0.002	-0.002	0.000	0.000	0.000	0.000
19	A	65	LYS	1	0.938	0.975	43.785	-0.027	-0.027	0.000	0.000	0.000	0.000
20	A	66	SER	0	-0.027	-0.024	44.733	-0.001	-0.001	0.000	0.000	0.000	0.000
21	A	67	ASN	0	0.006	0.023	40.591	-0.003	-0.003	0.000	0.000	0.000	0.000
22	A	68	PRO	0	0.005	-0.002	38.347	0.001	0.001	0.000	0.000	0.000	0.000
23	A	69	ILE	0	-0.026	-0.003	33.594	0.003	0.003	0.000	0.000	0.000	0.000
24	A	70	ALA	0	0.031	0.010	32.322	-0.004	-0.004	0.000	0.000	0.000	0.000
25	A	71	LEU	0	-0.032	-0.012	28.343	0.006	0.006	0.000	0.000	0.000	0.000
26	A	72	ARG	1	0.809	0.887	24.732	-0.128	-0.128	0.000	0.000	0.000	0.000
27	A	73	CYS	0	-0.020	0.001	21.400	-0.009	-0.009	0.000	0.000	0.000	0.000
28	A	74	LYS	1	0.816	0.899	19.940	-0.118	-0.118	0.000	0.000	0.000	0.000
29	A	75	ALA	0	-0.001	0.011	15.466	0.026	0.026	0.000	0.000	0.000	0.000
30	A	76	ARG	1	0.787	0.885	11.568	-0.464	-0.464	0.000	0.000	0.000	0.000
31	A	77	PRO	0	-0.047	-0.008	9.067	0.097	0.097	0.000	0.000	0.000	0.000
32	A	78	ALA	0	0.021	-0.012	12.366	-0.048	-0.048	0.000	0.000	0.000	0.000
33	A	79	MET	0	-0.041	-0.011	13.908	0.003	0.003	0.000	0.000	0.000	0.000
34	A	80	GLN	0	-0.019	-0.018	17.385	0.021	0.021	0.000	0.000	0.000	0.000
35	A	81	ILE	0	0.008	0.010	18.400	-0.002	-0.002	0.000	0.000	0.000	0.000
36	A	82	PHE	0	-0.006	0.002	20.730	-0.001	-0.001	0.000	0.000	0.000	0.000
37	A	83	PHE	0	0.043	0.002	22.973	0.005	0.005	0.000	0.000	0.000	0.000
38	A	84	LYS	1	0.825	0.919	24.583	0.028	0.028	0.000	0.000	0.000	0.000
39	A	85	CYS	0	-0.037	-0.023	26.701	0.000	0.000	0.000	0.000	0.000	0.000
40	A	86	ASN	0	0.059	0.029	30.060	-0.001	-0.001	0.000	0.000	0.000	0.000
41	A	87	GLY	0	0.018	0.019	28.579	-0.003	-0.003	0.000	0.000	0.000	0.000
42	A	88	GLU	-1	-0.889	-0.945	29.134	-0.034	-0.034	0.000	0.000	0.000	0.000
43	A	89	TRP	0	-0.090	-0.061	21.821	0.005	0.005	0.000	0.000	0.000	0.000
44	A	90	VAL	0	0.022	0.018	28.398	0.000	0.000	0.000	0.000	0.000	0.000
45	A	91	HIS	0	0.045	0.021	29.250	-0.009	-0.009	0.000	0.000	0.000	0.000
46	A	92	GLN	0	0.022	0.007	27.924	0.000	0.000	0.000	0.000	0.000	0.000
47	A	93	ASN	0	-0.046	-0.026	30.108	0.000	0.000	0.000	0.000	0.000	0.000
48	A	94	GLU	-1	-0.842	-0.925	32.593	-0.009	-0.009	0.000	0.000	0.000	0.000
49	A	95	HIS	0	-0.086	-0.023	26.392	0.010	0.010	0.000	0.000	0.000	0.000
50	A	96	VAL	0	0.009	0.012	29.294	-0.005	-0.005	0.000	0.000	0.000	0.000
51	A	97	SER	0	-0.016	-0.024	25.046	0.003	0.003	0.000	0.000	0.000	0.000
52	A	98	GLU	-1	-0.809	-0.886	24.396	0.065	0.065	0.000	0.000	0.000	0.000
53	A	99	GLU	-1	-0.861	-0.900	20.544	-0.039	-0.039	0.000	0.000	0.000	0.000
54	A	100	SER	0	-0.003	-0.014	20.897	0.004	0.004	0.000	0.000	0.000	0.000
55	A	101	LEU	0	-0.058	-0.035	17.520	-0.006	-0.006	0.000	0.000	0.000	0.000
56	A	102	ASP	-1	-0.773	-0.883	15.360	0.236	0.236	0.000	0.000	0.000	0.000
57	A	102	GLU	-1	-0.790	-0.890	11.360	0.528	0.528	0.000	0.000	0.000	0.000
58	A	102	SER	0	-0.058	-0.008	9.265	-0.089	-0.089	0.000	0.000	0.000	0.000
59	A	102	SER	0	-0.041	-0.032	11.470	-0.067	-0.067	0.000	0.000	0.000	0.000
60	A	102	GLY	0	-0.014	0.003	13.647	-0.042	-0.042	0.000	0.000	0.000	0.000
61	A	103	LEU	0	-0.037	-0.013	9.046	-0.053	-0.053	0.000	0.000	0.000	0.000
62	A	104	LYS	1	0.876	0.914	13.087	0.056	0.056	0.000	0.000	0.000	0.000
63	A	105	VAL	0	0.004	0.013	15.400	0.012	0.012	0.000	0.000	0.000	0.000
64	A	106	ARG	1	0.895	0.940	17.672	0.011	0.011	0.000	0.000	0.000	0.000
65	A	107	GLU	-1	-0.757	-0.876	20.246	0.120	0.120	0.000	0.000	0.000	0.000
66	A	108	VAL	0	-0.051	-0.026	22.900	-0.014	-0.014	0.000	0.000	0.000	0.000
67	A	109	PHE	0	0.019	0.016	25.256	0.010	0.010	0.000	0.000	0.000	0.000
68	A	110	ILE	0	0.006	0.006	28.390	-0.008	-0.008	0.000	0.000	0.000	0.000
69	A	111	ASN	0	-0.009	-0.010	30.875	0.009	0.009	0.000	0.000	0.000	0.000
70	A	112	VAL	0	0.001	0.011	33.121	-0.004	-0.004	0.000	0.000	0.000	0.000
71	A	113	THR	0	-0.004	-0.036	35.911	0.003	0.003	0.000	0.000	0.000	0.000
72	A	114	ARG	1	0.833	0.885	39.690	-0.015	-0.015	0.000	0.000	0.000	0.000
73	A	115	GLN	0	-0.011	-0.029	42.321	-0.001	-0.001	0.000	0.000	0.000	0.000
74	A	116	GLN	0	0.071	0.067	36.016	0.001	0.001	0.000	0.000	0.000	0.000
75	A	117	VAL	0	-0.017	-0.011	37.490	-0.001	-0.001	0.000	0.000	0.000	0.000
76	A	118	GLU	-1	-0.821	-0.889	39.805	0.012	0.012	0.000	0.000	0.000	0.000
77	A	119	ASP	-1	-0.880	-0.928	42.122	0.001	0.001	0.000	0.000	0.000	0.000
78	A	120	PHE	0	-0.089	-0.037	35.841	-0.003	-0.003	0.000	0.000	0.000	0.000
79	A	121	HIS	0	-0.035	-0.015	40.508	0.003	0.003	0.000	0.000	0.000	0.000
80	A	122	GLY	0	-0.006	0.008	38.456	-0.002	-0.002	0.000	0.000	0.000	0.000
81	A	123	PRO	0	-0.044	-0.025	36.818	0.002	0.002	0.000	0.000	0.000	0.000
82	A	124	GLU	-1	-0.896	-0.954	32.247	0.027	0.027	0.000	0.000	0.000	0.000
83	A	125	ASP	-1	-0.813	-0.907	35.331	0.035	0.035	0.000	0.000	0.000	0.000
84	A	126	TYR	0	-0.013	-0.003	33.494	-0.002	-0.002	0.000	0.000	0.000	0.000
85	A	127	TRP	0	-0.003	-0.004	26.855	0.005	0.005	0.000	0.000	0.000	0.000
86	A	129	GLN	0	-0.007	0.002	21.925	-0.008	-0.008	0.000	0.000	0.000	0.000
87	A	131	VAL	0	-0.035	-0.012	18.381	0.010	0.010	0.000	0.000	0.000	0.000
88	A	132	ALA	0	0.055	0.028	15.773	-0.010	-0.010	0.000	0.000	0.000	0.000
89	A	133	TRP	0	0.008	-0.021	15.189	-0.011	-0.011	0.000	0.000	0.000	0.000
90	A	134	SER	0	0.009	0.000	9.851	-0.009	-0.009	0.000	0.000	0.000	0.000
91	A	135	HIS	0	0.028	0.007	7.723	0.141	0.141	0.000	0.000	0.000	0.000
92	A	136	LEU	0	-0.024	-0.007	4.958	-0.100	-0.100	0.000	0.000	0.000	0.000
93	A	137	GLY	0	0.011	0.011	9.421	0.013	0.013	0.000	0.000	0.000	0.000
94	A	138	THR	0	-0.039	-0.019	12.097	0.043	0.043	0.000	0.000	0.000	0.000
95	A	139	SER	0	-0.003	-0.021	12.448	-0.018	-0.018	0.000	0.000	0.000	0.000
96	A	140	LYS	1	0.858	0.923	14.437	-0.007	-0.007	0.000	0.000	0.000	0.000
97	A	141	SER	0	0.059	0.051	17.608	0.019	0.019	0.000	0.000	0.000	0.000
98	A	142	ARG	1	0.787	0.864	19.716	-0.124	-0.124	0.000	0.000	0.000	0.000
99	A	143	LYS	1	0.845	0.926	22.853	-0.039	-0.039	0.000	0.000	0.000	0.000
100	A	144	ALA	0	0.004	0.013	26.095	0.004	0.004	0.000	0.000	0.000	0.000
101	A	145	SER	0	-0.036	-0.026	28.592	-0.011	-0.011	0.000	0.000	0.000	0.000
102	A	146	VAL	0	-0.030	-0.020	32.268	0.004	0.004	0.000	0.000	0.000	0.000
103	A	147	ARG	1	0.869	0.926	34.575	-0.054	-0.054	0.000	0.000	0.000	0.000
104	A	148	ILE	0	-0.007	-0.009	38.751	0.002	0.002	0.000	0.000	0.000	0.000
105	A	149	ALA	0	-0.001	0.016	42.014	0.000	0.000	0.000	0.000	0.000	0.000
106	A	150	TYR	0	0.012	-0.013	43.734	-0.002	-0.002	0.000	0.000	0.000	0.000
107	A	151	LEU	0	-0.004	-0.005	45.449	0.001	0.001	0.000	0.000	0.000	0.000
108	A	152	ARG	1	1.015	1.008	48.703	-0.037	-0.037	0.000	0.000	0.000	0.000

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