FMO DATABASE

FMODB ID: LN479

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	OptH
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	-986239.259367
FMO2-HF: Nuclear repulsion	940233.623593
FMO2-HF: Total energy	-46005.635773
FMO2-MP2: Total energy	-46140.62816

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.
-4.885	-1.462	0.168	-1.455	-2.135	0

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 : -0.032 / q_NPA : -0.035

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	0.017	-0.011	3.647	-2.800	-1.463	0.023	-0.691	-0.669	0.000
4	A	-2	PHE	0	-0.011	0.000	2.843	-0.432	0.850	0.139	-0.404	-1.017	0.003
5	A	-1	GLN	0	0.013	0.001	8.093	-0.111	-0.111	0.000	0.000	0.000	0.000
6	A	0	GLY	0	-0.018	0.006	9.786	-0.003	-0.003	0.000	0.000	0.000	0.000
7	A	1	VAL	0	0.051	0.037	9.894	0.021	0.021	0.000	0.000	0.000	0.000
8	A	2	ALA	0	-0.021	0.005	10.432	0.088	0.088	0.000	0.000	0.000	0.000
9	A	3	ILE	0	0.031	0.009	12.239	-0.310	-0.310	0.000	0.000	0.000	0.000
10	A	4	LYS	1	0.870	0.933	14.844	1.137	1.137	0.000	0.000	0.000	0.000
11	A	5	LEU	0	0.009	0.003	16.346	0.049	0.049	0.000	0.000	0.000	0.000
12	A	6	SER	0	-0.069	-0.043	20.002	-0.037	-0.037	0.000	0.000	0.000	0.000
13	A	7	SER	0	0.060	0.024	22.067	0.021	0.021	0.000	0.000	0.000	0.000
14	A	8	ILE	0	0.035	0.007	25.458	0.005	0.005	0.000	0.000	0.000	0.000
15	A	9	ASP	-1	-0.906	-0.938	27.872	-0.217	-0.217	0.000	0.000	0.000	0.000
16	A	10	GLN	0	0.008	-0.004	22.495	-0.011	-0.011	0.000	0.000	0.000	0.000
17	A	11	PHE	0	0.000	0.004	23.000	0.014	0.014	0.000	0.000	0.000	0.000
18	A	12	GLU	-1	-0.757	-0.863	24.984	-0.084	-0.084	0.000	0.000	0.000	0.000
19	A	13	GLN	0	-0.030	0.003	26.871	0.022	0.022	0.000	0.000	0.000	0.000
20	A	14	VAL	0	0.003	0.003	21.518	0.019	0.019	0.000	0.000	0.000	0.000
21	A	15	ILE	0	-0.082	-0.036	24.206	0.035	0.035	0.000	0.000	0.000	0.000
22	A	16	GLU	-1	-0.957	-0.963	26.125	-0.026	-0.026	0.000	0.000	0.000	0.000
23	A	17	GLU	-1	-0.955	-0.978	26.651	-0.147	-0.147	0.000	0.000	0.000	0.000
24	A	18	ASN	0	-0.096	-0.045	23.371	0.029	0.029	0.000	0.000	0.000	0.000
25	A	19	LYS	1	0.856	0.928	25.719	-0.102	-0.102	0.000	0.000	0.000	0.000
26	A	20	TYR	0	0.018	-0.002	22.755	0.004	0.004	0.000	0.000	0.000	0.000
27	A	21	VAL	0	0.063	0.042	20.683	-0.005	-0.005	0.000	0.000	0.000	0.000
28	A	22	PHE	0	0.019	0.018	16.881	0.007	0.007	0.000	0.000	0.000	0.000
29	A	23	VAL	0	0.000	-0.006	17.792	-0.066	-0.066	0.000	0.000	0.000	0.000
30	A	24	LEU	0	-0.024	-0.012	12.035	0.044	0.044	0.000	0.000	0.000	0.000
31	A	25	LYS	1	0.839	0.930	16.188	0.082	0.082	0.000	0.000	0.000	0.000
32	A	26	HIS	0	0.094	0.047	10.962	0.262	0.262	0.000	0.000	0.000	0.000
33	A	27	SER	0	-0.050	-0.042	14.936	0.011	0.011	0.000	0.000	0.000	0.000
34	A	28	GLU	-1	-0.876	-0.946	13.542	-1.070	-1.070	0.000	0.000	0.000	0.000
35	A	29	THR	0	-0.020	-0.006	13.775	-0.116	-0.116	0.000	0.000	0.000	0.000
36	A	30	CYS	0	-0.047	-0.003	14.412	0.141	0.141	0.000	0.000	0.000	0.000
37	A	31	PRO	0	0.067	0.029	11.858	-0.077	-0.077	0.000	0.000	0.000	0.000
38	A	32	ILE	0	0.040	0.015	11.630	0.077	0.077	0.000	0.000	0.000	0.000
39	A	33	SER	0	0.044	-0.023	12.705	0.153	0.153	0.000	0.000	0.000	0.000
40	A	34	ALA	0	-0.015	-0.004	8.188	-0.027	-0.027	0.000	0.000	0.000	0.000
41	A	35	ASN	0	-0.006	-0.002	7.734	-0.031	-0.031	0.000	0.000	0.000	0.000
42	A	36	ALA	0	0.042	0.016	8.900	0.299	0.299	0.000	0.000	0.000	0.000
43	A	37	TYR	0	-0.012	-0.005	6.609	0.059	0.059	0.000	0.000	0.000	0.000
44	A	38	ASP	-1	-0.888	-0.949	3.399	1.907	2.565	0.007	-0.357	-0.308	-0.003
45	A	39	GLN	0	-0.041	-0.011	5.947	0.816	0.816	0.000	0.000	0.000	0.000
46	A	40	PHE	0	0.010	0.009	9.012	0.191	0.191	0.000	0.000	0.000	0.000
47	A	41	ASN	0	0.033	0.000	6.104	0.000	0.000	0.000	0.000	0.000	0.000
48	A	42	LYS	1	0.870	0.946	4.931	-6.216	-6.070	-0.001	-0.003	-0.141	0.000
49	A	43	PHE	0	-0.016	-0.006	8.225	-0.013	-0.013	0.000	0.000	0.000	0.000
50	A	44	LEU	0	0.011	0.007	11.404	-0.030	-0.030	0.000	0.000	0.000	0.000
51	A	45	TYR	0	-0.036	-0.018	8.889	-0.133	-0.133	0.000	0.000	0.000	0.000
52	A	46	GLU	-1	-0.995	-0.992	11.273	1.909	1.909	0.000	0.000	0.000	0.000
53	A	47	ARG	1	0.811	0.903	12.977	-0.965	-0.965	0.000	0.000	0.000	0.000
54	A	48	ASP	-1	-0.965	-0.951	14.690	0.288	0.288	0.000	0.000	0.000	0.000
55	A	49	MET	0	-0.049	-0.024	15.284	-0.111	-0.111	0.000	0.000	0.000	0.000
56	A	50	ASP	-1	-0.873	-0.938	15.047	-0.141	-0.141	0.000	0.000	0.000	0.000
57	A	51	GLY	0	-0.025	-0.024	15.005	0.078	0.078	0.000	0.000	0.000	0.000
58	A	52	TYR	0	0.028	0.018	15.552	-0.143	-0.143	0.000	0.000	0.000	0.000
59	A	53	TYR	0	-0.033	-0.022	12.266	-0.012	-0.012	0.000	0.000	0.000	0.000
60	A	54	LEU	0	0.042	0.031	15.738	-0.034	-0.034	0.000	0.000	0.000	0.000
61	A	55	ILE	0	0.009	0.003	14.148	-0.012	-0.012	0.000	0.000	0.000	0.000
62	A	56	VAL	0	-0.031	-0.043	17.496	0.079	0.079	0.000	0.000	0.000	0.000
63	A	57	GLN	0	-0.023	-0.026	18.283	0.002	0.002	0.000	0.000	0.000	0.000
64	A	58	GLN	0	-0.040	-0.027	18.766	0.072	0.072	0.000	0.000	0.000	0.000
65	A	59	GLU	-1	-0.883	-0.910	20.818	-0.514	-0.514	0.000	0.000	0.000	0.000
66	A	60	ARG	1	0.949	0.969	22.917	0.385	0.385	0.000	0.000	0.000	0.000
67	A	61	ASP	-1	-0.851	-0.909	25.820	-0.245	-0.245	0.000	0.000	0.000	0.000
68	A	62	LEU	0	0.008	0.011	22.224	0.030	0.030	0.000	0.000	0.000	0.000
69	A	63	SER	0	0.001	-0.017	22.961	0.029	0.029	0.000	0.000	0.000	0.000
70	A	64	ASP	-1	-0.972	-0.993	24.398	-0.129	-0.129	0.000	0.000	0.000	0.000
71	A	65	TYR	0	-0.057	-0.068	27.616	0.026	0.026	0.000	0.000	0.000	0.000
72	A	66	ILE	0	0.035	0.013	22.279	0.025	0.025	0.000	0.000	0.000	0.000
73	A	67	ALA	0	-0.017	0.005	26.301	0.029	0.029	0.000	0.000	0.000	0.000
74	A	68	LYS	1	0.892	0.927	27.838	0.142	0.142	0.000	0.000	0.000	0.000
75	A	69	LYS	1	0.831	0.947	27.948	0.088	0.088	0.000	0.000	0.000	0.000
76	A	70	THR	0	0.002	-0.019	25.843	0.020	0.020	0.000	0.000	0.000	0.000
77	A	71	ASN	0	-0.062	-0.028	29.269	0.008	0.008	0.000	0.000	0.000	0.000
78	A	72	VAL	0	-0.005	0.023	25.448	0.014	0.014	0.000	0.000	0.000	0.000
79	A	73	LYS	1	0.909	0.943	27.511	0.029	0.029	0.000	0.000	0.000	0.000
80	A	74	HIS	0	0.062	0.017	21.646	0.020	0.020	0.000	0.000	0.000	0.000
81	A	75	GLU	-1	-0.862	-0.911	21.724	-0.039	-0.039	0.000	0.000	0.000	0.000
82	A	76	SER	0	-0.095	-0.020	17.695	-0.065	-0.065	0.000	0.000	0.000	0.000
83	A	77	PRO	0	-0.053	-0.018	14.483	0.003	0.003	0.000	0.000	0.000	0.000
84	A	78	GLN	0	0.056	-0.006	16.619	0.039	0.039	0.000	0.000	0.000	0.000
85	A	79	ALA	0	-0.002	0.010	16.109	-0.061	-0.061	0.000	0.000	0.000	0.000
86	A	80	PHE	0	-0.005	-0.011	18.124	0.034	0.034	0.000	0.000	0.000	0.000
87	A	81	TYR	0	0.047	0.023	19.961	-0.005	-0.005	0.000	0.000	0.000	0.000
88	A	82	PHE	0	-0.015	-0.022	22.050	-0.011	-0.011	0.000	0.000	0.000	0.000
89	A	83	VAL	0	0.048	0.020	24.631	0.014	0.014	0.000	0.000	0.000	0.000
90	A	84	ASN	0	-0.018	-0.017	27.219	0.010	0.010	0.000	0.000	0.000	0.000
91	A	85	GLY	0	0.096	0.057	28.076	-0.006	-0.006	0.000	0.000	0.000	0.000
92	A	86	GLU	-1	-0.972	-0.971	29.179	0.034	0.034	0.000	0.000	0.000	0.000
93	A	87	MET	0	-0.076	-0.029	25.226	0.010	0.010	0.000	0.000	0.000	0.000
94	A	88	VAL	0	0.026	0.010	25.474	0.003	0.003	0.000	0.000	0.000	0.000
95	A	89	TRP	0	-0.011	-0.011	17.676	0.004	0.004	0.000	0.000	0.000	0.000
96	A	90	ASN	0	-0.006	-0.017	21.847	-0.028	-0.028	0.000	0.000	0.000	0.000
97	A	91	ARG	1	0.923	0.978	19.084	-0.248	-0.248	0.000	0.000	0.000	0.000
98	A	92	ASP	-1	-0.770	-0.867	18.794	0.038	0.038	0.000	0.000	0.000	0.000
99	A	93	HIS	1	0.784	0.856	17.004	0.045	0.045	0.000	0.000	0.000	0.000
100	A	94	GLY	0	0.006	-0.006	15.528	0.028	0.028	0.000	0.000	0.000	0.000
101	A	95	ASP	-1	-0.878	-0.920	16.459	0.460	0.460	0.000	0.000	0.000	0.000
102	A	96	ILE	0	-0.084	0.001	13.276	0.016	0.016	0.000	0.000	0.000	0.000
103	A	97	ASN	0	0.015	-0.017	12.729	0.088	0.088	0.000	0.000	0.000	0.000
104	A	98	VAL	0	0.043	0.014	10.858	-0.108	-0.108	0.000	0.000	0.000	0.000
105	A	99	SER	0	-0.039	-0.012	13.555	-0.073	-0.073	0.000	0.000	0.000	0.000
106	A	100	SER	0	-0.041	-0.045	16.949	-0.073	-0.073	0.000	0.000	0.000	0.000
107	A	101	LEU	0	-0.018	-0.011	13.330	-0.088	-0.088	0.000	0.000	0.000	0.000
108	A	102	ALA	0	0.005	-0.006	17.307	-0.057	-0.057	0.000	0.000	0.000	0.000
109	A	103	GLN	0	-0.002	-0.007	18.888	-0.089	-0.089	0.000	0.000	0.000	0.000
110	A	104	ALA	0	-0.080	-0.026	20.685	-0.051	-0.051	0.000	0.000	0.000	0.000
111	A	105	GLU	-1	-0.854	-0.941	19.844	0.470	0.470	0.000	0.000	0.000	0.000
112	A	106	GLU	-1	-1.027	-0.992	23.187	0.425	0.425	0.000	0.000	0.000	0.000

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