FMO DATABASE

FMODB ID: LN9N9

Calculation Name: 3B93-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3B93

Chain ID: A

ChEMBL ID:

UniProt ID: Q9UNG2

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	122
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1051987.077514
FMO2-HF: Nuclear repulsion	1002899.522732
FMO2-HF: Total energy	-49087.554781
FMO2-MP2: Total energy	-49230.332706

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:55:LYS)

Summations of interaction energy for fragment #1(A:55:LYS)

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.
-12.218	-9.722	0.005	-1.252	-1.249	0.005

Interaction energy analysis for fragmet #1(A:55:LYS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.888 / q_NPA : 0.918

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	57	PRO	0	0.040	-0.005	3.535	-1.480	0.576	0.000	-1.106	-0.950	0.005
4	A	58	CYS	0	-0.018	0.008	5.223	4.978	5.055	-0.002	-0.005	-0.070	0.000
5	A	59	MET	0	0.001	0.006	7.338	3.798	3.798	0.000	0.000	0.000	0.000
6	A	60	ALA	0	-0.011	0.001	10.635	0.438	0.438	0.000	0.000	0.000	0.000
7	A	61	LYS	1	0.921	0.970	13.463	16.435	16.435	0.000	0.000	0.000	0.000
8	A	62	PHE	0	0.018	0.019	16.112	0.302	0.302	0.000	0.000	0.000	0.000
9	A	63	GLY	0	0.021	0.033	19.567	0.323	0.323	0.000	0.000	0.000	0.000
10	A	64	PRO	0	-0.004	-0.021	19.319	-0.864	-0.864	0.000	0.000	0.000	0.000
11	A	65	LEU	0	-0.036	-0.026	22.460	-0.137	-0.137	0.000	0.000	0.000	0.000
12	A	66	PRO	0	0.003	-0.012	23.497	0.187	0.187	0.000	0.000	0.000	0.000
13	A	67	SER	0	-0.011	0.009	18.800	0.085	0.085	0.000	0.000	0.000	0.000
14	A	68	LYS	1	0.884	0.913	20.245	11.825	11.825	0.000	0.000	0.000	0.000
15	A	69	TRP	0	-0.009	0.006	16.877	-0.643	-0.643	0.000	0.000	0.000	0.000
16	A	70	GLN	0	-0.087	-0.047	13.687	-0.087	-0.087	0.000	0.000	0.000	0.000
17	A	71	MET	0	0.015	-0.018	11.076	0.517	0.517	0.000	0.000	0.000	0.000
18	A	72	ALA	0	0.006	0.013	6.516	0.314	0.314	0.000	0.000	0.000	0.000
19	A	73	SER	0	0.010	-0.001	3.866	-2.326	-1.993	0.008	-0.141	-0.200	0.000
20	A	74	SER	0	-0.019	-0.014	5.396	-1.502	-1.472	-0.001	0.000	-0.029	0.000
21	A	75	GLU	-1	-0.926	-0.937	6.867	-22.748	-22.748	0.000	0.000	0.000	0.000
22	A	76	PRO	0	0.035	0.029	6.328	-3.569	-3.569	0.000	0.000	0.000	0.000
23	A	77	PRO	0	-0.001	-0.004	9.460	-1.621	-1.621	0.000	0.000	0.000	0.000
24	A	79	VAL	0	-0.002	-0.009	12.337	1.423	1.423	0.000	0.000	0.000	0.000
25	A	80	ASN	0	-0.010	-0.014	15.144	-0.562	-0.562	0.000	0.000	0.000	0.000
26	A	81	LYS	1	0.908	0.973	16.563	16.340	16.340	0.000	0.000	0.000	0.000
27	A	82	VAL	0	0.032	0.011	19.679	0.360	0.360	0.000	0.000	0.000	0.000
28	A	83	SER	0	0.012	0.006	23.316	0.568	0.568	0.000	0.000	0.000	0.000
29	A	84	ASP	-1	-0.844	-0.905	23.706	-12.209	-12.209	0.000	0.000	0.000	0.000
30	A	85	TRP	0	-0.012	-0.022	23.621	0.180	0.180	0.000	0.000	0.000	0.000
31	A	86	LYS	1	0.896	0.947	23.640	11.468	11.468	0.000	0.000	0.000	0.000
32	A	87	LEU	0	-0.063	-0.031	16.524	-0.206	-0.206	0.000	0.000	0.000	0.000
33	A	88	GLU	-1	-0.821	-0.917	20.101	-13.732	-13.732	0.000	0.000	0.000	0.000
34	A	89	ILE	0	-0.028	-0.011	16.488	-1.056	-1.056	0.000	0.000	0.000	0.000
35	A	90	LEU	0	-0.014	-0.017	15.165	0.791	0.791	0.000	0.000	0.000	0.000
36	A	91	GLN	0	0.012	0.002	12.145	-0.512	-0.512	0.000	0.000	0.000	0.000
37	A	92	ASN	0	0.023	0.021	15.070	0.176	0.176	0.000	0.000	0.000	0.000
38	A	93	GLY	0	-0.004	0.002	13.754	-1.745	-1.745	0.000	0.000	0.000	0.000
39	A	94	LEU	0	0.015	0.020	13.570	1.648	1.648	0.000	0.000	0.000	0.000
40	A	95	TYR	0	0.024	-0.032	12.679	-2.982	-2.982	0.000	0.000	0.000	0.000
41	A	96	LEU	0	-0.031	-0.008	14.135	1.559	1.559	0.000	0.000	0.000	0.000
42	A	97	ILE	0	0.005	-0.001	15.532	-0.824	-0.824	0.000	0.000	0.000	0.000
43	A	98	TYR	0	-0.008	0.003	13.929	1.066	1.066	0.000	0.000	0.000	0.000
44	A	99	GLY	0	0.059	0.003	19.368	-0.114	-0.114	0.000	0.000	0.000	0.000
45	A	100	GLN	0	-0.055	-0.001	21.602	0.001	0.001	0.000	0.000	0.000	0.000
46	A	101	VAL	0	0.068	0.029	24.408	0.048	0.048	0.000	0.000	0.000	0.000
47	A	102	ALA	0	-0.004	-0.015	27.648	0.239	0.239	0.000	0.000	0.000	0.000
48	A	103	PRO	0	0.005	0.011	29.780	0.124	0.124	0.000	0.000	0.000	0.000
49	A	104	ASN	0	-0.020	-0.007	33.305	0.115	0.115	0.000	0.000	0.000	0.000
50	A	105	ALA	0	0.006	-0.003	35.905	0.179	0.179	0.000	0.000	0.000	0.000
51	A	106	ASN	0	-0.022	-0.017	38.389	0.255	0.255	0.000	0.000	0.000	0.000
52	A	107	TYR	0	-0.064	-0.037	38.677	0.103	0.103	0.000	0.000	0.000	0.000
53	A	108	ASN	0	-0.050	-0.052	40.693	0.024	0.024	0.000	0.000	0.000	0.000
54	A	109	ASP	-1	-0.894	-0.920	42.119	-7.197	-7.197	0.000	0.000	0.000	0.000
55	A	110	VAL	0	0.021	0.004	44.704	-0.016	-0.016	0.000	0.000	0.000	0.000
56	A	111	ALA	0	0.006	0.025	41.660	0.020	0.020	0.000	0.000	0.000	0.000
57	A	112	PRO	0	0.072	0.042	42.293	-0.045	-0.045	0.000	0.000	0.000	0.000
58	A	113	PHE	0	-0.001	-0.006	34.664	-0.160	-0.160	0.000	0.000	0.000	0.000
59	A	114	GLU	-1	-0.812	-0.869	35.360	-8.873	-8.873	0.000	0.000	0.000	0.000
60	A	115	VAL	0	-0.039	-0.008	30.290	-0.045	-0.045	0.000	0.000	0.000	0.000
61	A	116	ARG	1	0.816	0.885	31.084	9.105	9.105	0.000	0.000	0.000	0.000
62	A	117	LEU	0	-0.015	0.008	23.464	-0.219	-0.219	0.000	0.000	0.000	0.000
63	A	118	TYR	0	-0.011	-0.018	26.984	0.414	0.414	0.000	0.000	0.000	0.000
64	A	119	LYS	1	0.917	0.963	22.337	13.468	13.468	0.000	0.000	0.000	0.000
65	A	120	ASN	0	-0.027	-0.028	25.375	0.275	0.275	0.000	0.000	0.000	0.000
66	A	121	LYS	1	0.920	0.951	27.766	10.108	10.108	0.000	0.000	0.000	0.000
67	A	122	ASP	-1	-0.887	-0.936	29.120	-10.183	-10.183	0.000	0.000	0.000	0.000
68	A	123	MET	0	-0.041	0.001	29.154	-0.505	-0.505	0.000	0.000	0.000	0.000
69	A	124	ILE	0	0.007	-0.001	24.273	0.060	0.060	0.000	0.000	0.000	0.000
70	A	125	GLN	0	0.023	0.003	26.303	-0.529	-0.529	0.000	0.000	0.000	0.000
71	A	126	THR	0	-0.017	-0.028	29.368	0.043	0.043	0.000	0.000	0.000	0.000
72	A	127	LEU	0	-0.028	-0.013	29.237	-0.034	-0.034	0.000	0.000	0.000	0.000
73	A	128	THR	0	0.069	0.023	33.465	0.077	0.077	0.000	0.000	0.000	0.000
74	A	129	ASN	0	-0.004	0.026	36.054	0.275	0.275	0.000	0.000	0.000	0.000
75	A	130	LYS	1	0.948	0.962	35.623	7.336	7.336	0.000	0.000	0.000	0.000
76	A	131	SER	0	-0.047	-0.046	36.934	0.019	0.019	0.000	0.000	0.000	0.000
77	A	132	LYS	1	0.930	0.969	33.539	9.483	9.483	0.000	0.000	0.000	0.000
78	A	133	ILE	0	0.032	0.016	27.741	-0.061	-0.061	0.000	0.000	0.000	0.000
79	A	134	GLN	0	-0.095	-0.046	29.153	0.113	0.113	0.000	0.000	0.000	0.000
80	A	135	ASN	0	0.053	0.018	22.880	0.218	0.218	0.000	0.000	0.000	0.000
81	A	136	VAL	0	-0.040	-0.006	23.253	0.480	0.480	0.000	0.000	0.000	0.000
82	A	137	GLY	0	-0.003	-0.006	21.458	-0.682	-0.682	0.000	0.000	0.000	0.000
83	A	138	GLY	0	0.005	0.000	20.491	0.792	0.792	0.000	0.000	0.000	0.000
84	A	139	THR	0	-0.033	-0.015	16.664	-1.214	-1.214	0.000	0.000	0.000	0.000
85	A	140	TYR	0	-0.002	-0.009	18.258	1.121	1.121	0.000	0.000	0.000	0.000
86	A	141	GLU	-1	-0.891	-0.936	17.827	-16.746	-16.746	0.000	0.000	0.000	0.000
87	A	142	LEU	0	-0.095	-0.046	17.176	1.041	1.041	0.000	0.000	0.000	0.000
88	A	143	HIS	0	0.035	-0.002	18.142	-0.888	-0.888	0.000	0.000	0.000	0.000
89	A	144	VAL	0	0.022	0.009	18.227	0.129	0.129	0.000	0.000	0.000	0.000
90	A	145	GLY	0	0.007	0.012	20.226	0.719	0.719	0.000	0.000	0.000	0.000
91	A	146	ASP	-1	-0.788	-0.869	21.029	-13.604	-13.604	0.000	0.000	0.000	0.000
92	A	147	THR	0	-0.039	-0.030	21.775	-0.317	-0.317	0.000	0.000	0.000	0.000
93	A	148	ILE	0	-0.026	-0.016	19.985	0.158	0.158	0.000	0.000	0.000	0.000
94	A	149	ASP	-1	-0.803	-0.895	23.328	-11.708	-11.708	0.000	0.000	0.000	0.000
95	A	150	LEU	0	-0.014	0.008	25.103	0.080	0.080	0.000	0.000	0.000	0.000
96	A	151	ILE	0	-0.001	0.002	27.168	0.175	0.175	0.000	0.000	0.000	0.000
97	A	152	PHE	0	0.009	-0.013	27.521	0.130	0.130	0.000	0.000	0.000	0.000
98	A	153	ASN	0	-0.012	-0.005	33.287	-0.013	-0.013	0.000	0.000	0.000	0.000
99	A	154	SER	0	0.007	0.002	36.670	0.189	0.189	0.000	0.000	0.000	0.000
100	A	155	GLU	-1	-0.773	-0.891	32.423	-9.863	-9.863	0.000	0.000	0.000	0.000
101	A	156	HIS	0	0.041	0.024	34.077	-0.382	-0.382	0.000	0.000	0.000	0.000
102	A	157	GLN	0	0.015	0.012	35.454	-0.091	-0.091	0.000	0.000	0.000	0.000
103	A	158	VAL	0	-0.038	-0.008	30.289	-0.081	-0.081	0.000	0.000	0.000	0.000
104	A	159	LEU	0	0.037	0.018	30.980	0.168	0.168	0.000	0.000	0.000	0.000
105	A	160	LYS	1	0.791	0.895	27.897	9.560	9.560	0.000	0.000	0.000	0.000
106	A	161	ASN	0	0.004	0.013	26.360	-0.433	-0.433	0.000	0.000	0.000	0.000
107	A	162	ASN	0	-0.008	-0.007	25.599	-0.510	-0.510	0.000	0.000	0.000	0.000
108	A	163	THR	0	0.000	0.008	25.565	-0.072	-0.072	0.000	0.000	0.000	0.000
109	A	164	TYR	0	-0.036	-0.041	19.592	-0.411	-0.411	0.000	0.000	0.000	0.000
110	A	165	TRP	0	-0.033	-0.014	19.081	-0.018	-0.018	0.000	0.000	0.000	0.000
111	A	166	GLY	0	0.035	0.017	16.437	-0.075	-0.075	0.000	0.000	0.000	0.000
112	A	167	ILE	0	-0.036	-0.012	14.432	0.674	0.674	0.000	0.000	0.000	0.000
113	A	168	ILE	0	-0.010	-0.012	8.690	-1.266	-1.266	0.000	0.000	0.000	0.000
114	A	169	LEU	0	0.025	0.013	8.173	1.913	1.913	0.000	0.000	0.000	0.000
115	A	170	LEU	0	-0.056	-0.035	8.451	-4.146	-4.146	0.000	0.000	0.000	0.000
116	A	171	ALA	0	0.034	0.015	9.315	-2.035	-2.035	0.000	0.000	0.000	0.000
117	A	172	ASN	0	0.019	0.016	10.608	2.564	2.564	0.000	0.000	0.000	0.000
118	A	173	PRO	0	0.016	0.021	12.424	-0.444	-0.444	0.000	0.000	0.000	0.000
119	A	174	GLN	0	0.041	0.014	14.178	1.655	1.655	0.000	0.000	0.000	0.000
120	A	175	PHE	0	-0.060	-0.014	16.578	0.505	0.505	0.000	0.000	0.000	0.000
121	A	176	ILE	0	0.049	0.080	16.720	1.050	1.050	0.000	0.000	0.000	0.000
122	A	177	SER	0	-0.103	-0.095	18.538	-0.419	-0.419	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:55:LYS)