FMO DATABASE

FMODB ID: 989M2

Calculation Name: 3IV4-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3IV4

Chain ID: A

ChEMBL ID:

UniProt ID: A0A0H3

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	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	112
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-986652.476584
FMO2-HF: Nuclear repulsion	940646.160914
FMO2-HF: Total energy	-46006.31567
FMO2-MP2: Total energy	-46141.32956

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:ASN)

Summations of interaction energy for fragment #1(A:-5:ASN)

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.
-3.89	-0.408	0.908	-1.595	-2.792	0.007

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

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 : -0.036

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	-3	TYR	0	0.020	-0.011	3.695	-2.469	-1.027	0.020	-0.773	-0.689	0.002
4	A	-2	PHE	0	-0.023	-0.008	2.428	-1.041	0.599	0.889	-0.725	-1.803	0.006
5	A	-1	GLN	0	0.037	0.015	7.750	-0.301	-0.301	0.000	0.000	0.000	0.000
6	A	0	GLY	0	-0.024	0.002	9.829	-0.081	-0.081	0.000	0.000	0.000	0.000
7	A	1	VAL	0	0.044	0.033	9.664	-0.033	-0.033	0.000	0.000	0.000	0.000
8	A	2	ALA	0	-0.025	0.003	10.417	0.009	0.009	0.000	0.000	0.000	0.000
9	A	3	ILE	0	0.032	0.008	12.225	-0.223	-0.223	0.000	0.000	0.000	0.000
10	A	4	LYS	1	0.783	0.884	14.892	0.618	0.618	0.000	0.000	0.000	0.000
11	A	5	LEU	0	0.013	0.007	16.375	0.037	0.037	0.000	0.000	0.000	0.000
12	A	6	SER	0	-0.043	-0.043	20.025	-0.035	-0.035	0.000	0.000	0.000	0.000
13	A	7	SER	0	-0.048	-0.050	22.089	0.007	0.007	0.000	0.000	0.000	0.000
14	A	8	ILE	0	0.043	0.015	25.487	0.006	0.006	0.000	0.000	0.000	0.000
15	A	9	ASP	-1	-0.849	-0.892	28.020	-0.164	-0.164	0.000	0.000	0.000	0.000
16	A	10	GLN	0	0.016	0.012	22.552	-0.002	-0.002	0.000	0.000	0.000	0.000
17	A	11	PHE	0	0.005	0.004	23.121	0.014	0.014	0.000	0.000	0.000	0.000
18	A	12	GLU	-1	-0.736	-0.847	25.082	-0.049	-0.049	0.000	0.000	0.000	0.000
19	A	13	GLN	0	-0.080	-0.035	26.934	0.013	0.013	0.000	0.000	0.000	0.000
20	A	14	VAL	0	0.012	0.007	21.437	0.017	0.017	0.000	0.000	0.000	0.000
21	A	15	ILE	0	-0.082	-0.045	24.117	0.028	0.028	0.000	0.000	0.000	0.000
22	A	16	GLU	-1	-0.956	-0.961	26.073	0.007	0.007	0.000	0.000	0.000	0.000
23	A	17	GLU	-1	-0.923	-0.948	26.557	-0.062	-0.062	0.000	0.000	0.000	0.000
24	A	18	ASN	0	-0.096	-0.041	23.288	0.033	0.033	0.000	0.000	0.000	0.000
25	A	19	LYS	1	0.876	0.946	25.550	-0.117	-0.117	0.000	0.000	0.000	0.000
26	A	20	TYR	0	0.032	0.004	22.550	-0.006	-0.006	0.000	0.000	0.000	0.000
27	A	21	VAL	0	0.060	0.042	20.658	0.004	0.004	0.000	0.000	0.000	0.000
28	A	22	PHE	0	0.017	0.017	16.774	-0.008	-0.008	0.000	0.000	0.000	0.000
29	A	23	VAL	0	-0.009	-0.009	17.810	-0.039	-0.039	0.000	0.000	0.000	0.000
30	A	24	LEU	0	-0.036	-0.013	12.208	0.021	0.021	0.000	0.000	0.000	0.000
31	A	25	LYS	1	0.835	0.926	16.313	0.080	0.080	0.000	0.000	0.000	0.000
32	A	26	HIS	0	0.091	0.035	10.988	0.160	0.160	0.000	0.000	0.000	0.000
33	A	27	SER	0	-0.035	-0.030	15.252	0.013	0.013	0.000	0.000	0.000	0.000
34	A	28	GLU	-1	-0.858	-0.927	13.642	-0.807	-0.807	0.000	0.000	0.000	0.000
35	A	29	THR	0	-0.006	-0.002	13.771	-0.095	-0.095	0.000	0.000	0.000	0.000
36	A	30	CYS	0	-0.049	-0.008	14.461	0.094	0.094	0.000	0.000	0.000	0.000
37	A	31	PRO	0	0.063	0.027	12.009	-0.052	-0.052	0.000	0.000	0.000	0.000
38	A	32	ILE	0	0.046	0.018	12.029	0.029	0.029	0.000	0.000	0.000	0.000
39	A	33	SER	0	0.042	-0.006	13.004	0.106	0.106	0.000	0.000	0.000	0.000
40	A	34	ALA	0	-0.010	-0.002	8.406	-0.007	-0.007	0.000	0.000	0.000	0.000
41	A	35	ASN	0	-0.009	-0.004	8.067	-0.125	-0.125	0.000	0.000	0.000	0.000
42	A	36	ALA	0	0.047	0.022	9.019	0.165	0.165	0.000	0.000	0.000	0.000
43	A	37	TYR	0	0.007	0.000	7.076	0.078	0.078	0.000	0.000	0.000	0.000
44	A	38	ASP	-1	-0.825	-0.887	3.825	0.632	0.872	0.000	-0.089	-0.150	-0.001
45	A	39	GLN	0	-0.036	-0.010	6.013	0.547	0.547	0.000	0.000	0.000	0.000
46	A	40	PHE	0	0.015	0.009	8.877	0.195	0.195	0.000	0.000	0.000	0.000
47	A	41	ASN	0	-0.010	-0.027	5.992	0.076	0.076	0.000	0.000	0.000	0.000
48	A	42	LYS	1	0.815	0.893	4.081	-3.364	-3.204	-0.001	-0.008	-0.150	0.000
49	A	43	PHE	0	-0.012	-0.004	7.808	0.083	0.083	0.000	0.000	0.000	0.000
50	A	44	LEU	0	0.007	0.006	11.088	0.004	0.004	0.000	0.000	0.000	0.000
51	A	45	TYR	0	-0.030	-0.015	8.906	0.092	0.092	0.000	0.000	0.000	0.000
52	A	46	GLU	-1	-0.997	-0.992	10.825	1.795	1.795	0.000	0.000	0.000	0.000
53	A	47	ARG	1	0.760	0.858	12.728	-0.771	-0.771	0.000	0.000	0.000	0.000
54	A	48	ASP	-1	-0.976	-0.958	14.231	0.447	0.447	0.000	0.000	0.000	0.000
55	A	49	MET	0	-0.049	-0.026	14.900	-0.117	-0.117	0.000	0.000	0.000	0.000
56	A	50	ASP	-1	-0.894	-0.944	14.806	0.075	0.075	0.000	0.000	0.000	0.000
57	A	51	GLY	0	-0.024	-0.025	14.851	0.033	0.033	0.000	0.000	0.000	0.000
58	A	52	TYR	0	0.036	0.016	15.506	-0.096	-0.096	0.000	0.000	0.000	0.000
59	A	53	TYR	0	-0.028	-0.015	11.738	-0.006	-0.006	0.000	0.000	0.000	0.000
60	A	54	LEU	0	0.034	0.027	15.903	-0.019	-0.019	0.000	0.000	0.000	0.000
61	A	55	ILE	0	0.024	0.007	14.228	-0.009	-0.009	0.000	0.000	0.000	0.000
62	A	56	VAL	0	-0.010	-0.017	17.514	0.044	0.044	0.000	0.000	0.000	0.000
63	A	57	GLN	0	-0.019	-0.031	18.997	0.012	0.012	0.000	0.000	0.000	0.000
64	A	58	GLN	0	-0.056	-0.048	18.606	0.059	0.059	0.000	0.000	0.000	0.000
65	A	59	GLU	-1	-0.817	-0.877	20.531	-0.422	-0.422	0.000	0.000	0.000	0.000
66	A	60	ARG	1	0.936	0.959	23.268	0.304	0.304	0.000	0.000	0.000	0.000
67	A	61	ASP	-1	-0.867	-0.917	25.895	-0.196	-0.196	0.000	0.000	0.000	0.000
68	A	62	LEU	0	0.020	0.014	22.345	0.022	0.022	0.000	0.000	0.000	0.000
69	A	63	SER	0	-0.003	-0.017	23.414	0.016	0.016	0.000	0.000	0.000	0.000
70	A	64	ASP	-1	-0.858	-0.921	24.683	-0.107	-0.107	0.000	0.000	0.000	0.000
71	A	65	TYR	0	-0.039	-0.046	27.921	0.018	0.018	0.000	0.000	0.000	0.000
72	A	66	ILE	0	0.043	0.021	22.364	0.018	0.018	0.000	0.000	0.000	0.000
73	A	67	ALA	0	-0.039	-0.005	26.473	0.021	0.021	0.000	0.000	0.000	0.000
74	A	68	LYS	1	0.758	0.845	28.034	0.129	0.129	0.000	0.000	0.000	0.000
75	A	69	LYS	1	0.807	0.915	28.131	0.060	0.060	0.000	0.000	0.000	0.000
76	A	70	THR	0	0.008	-0.017	25.967	0.014	0.014	0.000	0.000	0.000	0.000
77	A	71	ASN	0	-0.026	-0.010	29.351	0.004	0.004	0.000	0.000	0.000	0.000
78	A	72	VAL	0	0.003	0.023	25.559	0.008	0.008	0.000	0.000	0.000	0.000
79	A	73	LYS	1	0.849	0.921	27.693	0.031	0.031	0.000	0.000	0.000	0.000
80	A	74	HIS	0	0.054	0.024	22.157	0.019	0.019	0.000	0.000	0.000	0.000
81	A	75	GLU	-1	-0.826	-0.913	21.753	-0.103	-0.103	0.000	0.000	0.000	0.000
82	A	76	SER	0	-0.094	-0.006	18.014	-0.043	-0.043	0.000	0.000	0.000	0.000
83	A	77	PRO	0	-0.036	-0.013	14.728	-0.003	-0.003	0.000	0.000	0.000	0.000
84	A	78	GLN	0	0.065	-0.001	16.889	0.026	0.026	0.000	0.000	0.000	0.000
85	A	79	ALA	0	0.010	0.014	16.140	-0.037	-0.037	0.000	0.000	0.000	0.000
86	A	80	PHE	0	-0.008	-0.017	18.181	0.019	0.019	0.000	0.000	0.000	0.000
87	A	81	TYR	0	0.047	0.026	19.914	-0.005	-0.005	0.000	0.000	0.000	0.000
88	A	82	PHE	0	-0.013	-0.024	21.948	-0.014	-0.014	0.000	0.000	0.000	0.000
89	A	83	VAL	0	0.041	0.018	24.477	0.017	0.017	0.000	0.000	0.000	0.000
90	A	84	ASN	0	-0.025	-0.029	27.046	0.006	0.006	0.000	0.000	0.000	0.000
91	A	85	GLY	0	0.093	0.058	27.951	-0.006	-0.006	0.000	0.000	0.000	0.000
92	A	86	GLU	-1	-0.979	-0.974	29.100	0.028	0.028	0.000	0.000	0.000	0.000
93	A	87	MET	0	-0.070	-0.015	25.161	0.007	0.007	0.000	0.000	0.000	0.000
94	A	88	VAL	0	0.021	0.006	25.438	0.000	0.000	0.000	0.000	0.000	0.000
95	A	89	TRP	0	0.002	-0.007	17.575	0.000	0.000	0.000	0.000	0.000	0.000
96	A	90	ASN	0	-0.020	-0.033	21.823	-0.022	-0.022	0.000	0.000	0.000	0.000
97	A	91	ARG	1	0.895	0.966	19.129	-0.147	-0.147	0.000	0.000	0.000	0.000
98	A	92	ASP	-1	-0.830	-0.904	18.966	-0.024	-0.024	0.000	0.000	0.000	0.000
99	A	93	HIS	1	0.789	0.869	17.218	0.099	0.099	0.000	0.000	0.000	0.000
100	A	94	GLY	0	0.009	-0.001	15.637	0.012	0.012	0.000	0.000	0.000	0.000
101	A	95	ASP	-1	-0.846	-0.914	16.473	0.276	0.276	0.000	0.000	0.000	0.000
102	A	96	ILE	0	-0.061	0.019	13.321	0.025	0.025	0.000	0.000	0.000	0.000
103	A	97	ASN	0	0.011	-0.006	12.604	0.054	0.054	0.000	0.000	0.000	0.000
104	A	98	VAL	0	0.045	0.017	10.394	-0.057	-0.057	0.000	0.000	0.000	0.000
105	A	99	SER	0	-0.011	-0.007	13.258	-0.013	-0.013	0.000	0.000	0.000	0.000
106	A	100	SER	0	-0.050	-0.049	16.749	-0.038	-0.038	0.000	0.000	0.000	0.000
107	A	101	LEU	0	-0.028	-0.015	13.064	-0.059	-0.059	0.000	0.000	0.000	0.000
108	A	102	ALA	0	0.007	-0.002	17.013	-0.030	-0.030	0.000	0.000	0.000	0.000
109	A	103	GLN	0	-0.007	-0.008	18.552	-0.058	-0.058	0.000	0.000	0.000	0.000
110	A	104	ALA	0	-0.080	-0.027	20.456	-0.035	-0.035	0.000	0.000	0.000	0.000
111	A	105	GLU	-1	-0.808	-0.900	19.408	0.436	0.436	0.000	0.000	0.000	0.000
112	A	106	GLU	-1	-1.018	-0.988	22.884	0.325	0.325	0.000	0.000	0.000	0.000

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