FMO DATABASE

FMODB ID: 6NGRZ

Calculation Name: 4B6H-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4B6H

Chain ID: A

ChEMBL ID:

UniProt ID: Q9NPI6

Base Structure: X-ray

Registration Date: 2023-06-22

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	130
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1178879.081002
FMO2-HF: Nuclear repulsion	1125662.817054
FMO2-HF: Total energy	-53216.263948
FMO2-MP2: Total energy	-53370.245521

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:0:LEU)

Summations of interaction energy for fragment #1(A:0:LEU)

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.
-5.625	-1.428	2.129	-1.942	-4.385	0.005

Interaction energy analysis for fragmet #1(A:0:LEU)

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 : 0.014

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	2	GLU	-1	-0.827	-0.935	3.154	-1.258	1.471	0.107	-1.113	-1.723	0.008
4	A	3	ALA	0	-0.040	-0.009	2.521	-1.769	-1.122	1.433	-0.571	-1.510	-0.002
5	A	4	LEU	0	0.030	0.003	2.575	-1.065	-0.244	0.589	-0.258	-1.152	-0.001
6	A	5	SER	0	-0.035	0.016	5.876	-0.021	-0.021	0.000	0.000	0.000	0.000
7	A	6	ARG	1	0.971	0.973	5.228	-1.956	-1.956	0.000	0.000	0.000	0.000
8	A	7	ALA	0	0.033	0.022	7.908	-0.138	-0.138	0.000	0.000	0.000	0.000
9	A	8	GLY	0	0.023	0.011	9.669	-0.033	-0.033	0.000	0.000	0.000	0.000
10	A	9	GLN	0	0.012	0.037	11.671	0.048	0.048	0.000	0.000	0.000	0.000
11	A	10	GLU	-1	-0.966	-0.981	11.795	0.138	0.138	0.000	0.000	0.000	0.000
12	A	11	MET	0	-0.061	-0.047	11.239	-0.034	-0.034	0.000	0.000	0.000	0.000
13	A	12	SER	0	-0.013	-0.030	15.061	-0.015	-0.015	0.000	0.000	0.000	0.000
14	A	13	LEU	0	-0.001	0.015	17.461	-0.009	-0.009	0.000	0.000	0.000	0.000
15	A	14	ALA	0	-0.029	-0.018	18.824	-0.010	-0.010	0.000	0.000	0.000	0.000
16	A	15	ALA	0	0.008	-0.004	19.780	-0.007	-0.007	0.000	0.000	0.000	0.000
17	A	16	LEU	0	-0.027	-0.016	21.067	-0.003	-0.003	0.000	0.000	0.000	0.000
18	A	17	LYS	1	0.935	0.972	21.844	-0.075	-0.075	0.000	0.000	0.000	0.000
19	A	18	GLN	0	-0.077	-0.019	24.506	-0.007	-0.007	0.000	0.000	0.000	0.000
20	A	19	HIS	0	-0.037	-0.017	26.393	-0.009	-0.009	0.000	0.000	0.000	0.000
21	A	20	ASP	-1	-0.766	-0.888	27.848	0.054	0.054	0.000	0.000	0.000	0.000
22	A	21	PRO	0	0.044	0.018	28.138	0.007	0.007	0.000	0.000	0.000	0.000
23	A	22	TYR	0	-0.051	-0.005	29.396	0.001	0.001	0.000	0.000	0.000	0.000
24	A	23	ILE	0	-0.012	0.029	24.479	0.009	0.009	0.000	0.000	0.000	0.000
25	A	24	THR	0	-0.017	-0.017	25.569	0.001	0.001	0.000	0.000	0.000	0.000
26	A	25	SER	0	-0.051	-0.020	21.780	0.011	0.011	0.000	0.000	0.000	0.000
27	A	26	ILE	0	0.047	0.022	17.902	-0.012	-0.012	0.000	0.000	0.000	0.000
28	A	27	ALA	0	-0.093	-0.052	20.479	0.019	0.019	0.000	0.000	0.000	0.000
29	A	28	ASP	-1	-0.765	-0.859	19.793	0.322	0.322	0.000	0.000	0.000	0.000
30	A	29	LEU	0	-0.044	-0.018	14.613	-0.032	-0.032	0.000	0.000	0.000	0.000
31	A	30	THR	0	0.011	0.007	18.344	0.021	0.021	0.000	0.000	0.000	0.000
32	A	31	GLY	0	-0.025	-0.008	15.883	0.006	0.006	0.000	0.000	0.000	0.000
33	A	32	GLN	0	-0.061	-0.024	16.822	-0.018	-0.018	0.000	0.000	0.000	0.000
34	A	33	VAL	0	0.005	0.009	19.111	0.005	0.005	0.000	0.000	0.000	0.000
35	A	34	ALA	0	0.016	-0.004	22.668	-0.011	-0.011	0.000	0.000	0.000	0.000
36	A	35	LEU	0	-0.018	0.014	25.383	0.005	0.005	0.000	0.000	0.000	0.000
37	A	36	TYR	0	-0.034	-0.002	28.605	-0.010	-0.010	0.000	0.000	0.000	0.000
38	A	37	THR	0	0.058	0.023	32.168	0.002	0.002	0.000	0.000	0.000	0.000
39	A	38	PHE	0	-0.023	-0.019	35.511	-0.002	-0.002	0.000	0.000	0.000	0.000
40	A	39	CYS	0	0.009	0.026	38.856	-0.003	-0.003	0.000	0.000	0.000	0.000
41	A	40	PRO	0	0.049	0.014	41.756	-0.001	-0.001	0.000	0.000	0.000	0.000
42	A	41	LYS	1	0.921	0.961	45.065	-0.022	-0.022	0.000	0.000	0.000	0.000
43	A	42	ALA	0	-0.054	-0.048	43.949	-0.001	-0.001	0.000	0.000	0.000	0.000
44	A	43	ASN	0	-0.023	-0.003	44.830	0.001	0.001	0.000	0.000	0.000	0.000
45	A	44	GLN	0	0.030	0.016	40.366	0.002	0.002	0.000	0.000	0.000	0.000
46	A	45	TRP	0	-0.016	-0.002	35.759	0.000	0.000	0.000	0.000	0.000	0.000
47	A	46	GLU	-1	-0.967	-0.976	35.974	0.028	0.028	0.000	0.000	0.000	0.000
48	A	47	LYS	1	0.944	0.978	30.759	-0.025	-0.025	0.000	0.000	0.000	0.000
49	A	48	THR	0	0.050	0.002	29.708	-0.004	-0.004	0.000	0.000	0.000	0.000
50	A	49	ASP	-1	-0.941	-0.973	28.643	0.025	0.025	0.000	0.000	0.000	0.000
51	A	50	ILE	0	0.016	0.015	25.385	-0.002	-0.002	0.000	0.000	0.000	0.000
52	A	51	GLU	-1	-0.898	-0.958	21.836	0.073	0.073	0.000	0.000	0.000	0.000
53	A	52	GLY	0	-0.030	-0.011	19.343	-0.014	-0.014	0.000	0.000	0.000	0.000
54	A	53	THR	0	-0.013	0.023	16.266	0.003	0.003	0.000	0.000	0.000	0.000
55	A	54	LEU	0	0.006	0.019	18.874	-0.021	-0.021	0.000	0.000	0.000	0.000
56	A	55	PHE	0	-0.009	-0.011	16.275	0.032	0.032	0.000	0.000	0.000	0.000
57	A	56	VAL	0	0.066	0.025	21.753	-0.021	-0.021	0.000	0.000	0.000	0.000
58	A	57	TYR	0	-0.022	-0.006	23.065	0.018	0.018	0.000	0.000	0.000	0.000
59	A	58	ARG	1	0.966	0.966	22.472	-0.179	-0.179	0.000	0.000	0.000	0.000
60	A	59	ARG	1	0.785	0.873	27.146	-0.063	-0.063	0.000	0.000	0.000	0.000
61	A	60	SER	0	-0.060	-0.057	29.869	0.001	0.001	0.000	0.000	0.000	0.000
62	A	61	ALA	0	-0.016	-0.022	31.921	-0.006	-0.006	0.000	0.000	0.000	0.000
63	A	62	SER	0	-0.030	0.032	34.236	0.002	0.002	0.000	0.000	0.000	0.000
64	A	63	PRO	0	-0.008	-0.014	34.090	-0.005	-0.005	0.000	0.000	0.000	0.000
65	A	64	TYR	0	0.029	-0.004	32.535	-0.001	-0.001	0.000	0.000	0.000	0.000
66	A	65	HIS	0	0.074	0.046	28.536	0.013	0.013	0.000	0.000	0.000	0.000
67	A	66	GLY	0	0.022	0.009	28.567	-0.010	-0.010	0.000	0.000	0.000	0.000
68	A	67	PHE	0	-0.011	-0.015	26.257	0.014	0.014	0.000	0.000	0.000	0.000
69	A	68	THR	0	0.003	0.006	23.394	-0.010	-0.010	0.000	0.000	0.000	0.000
70	A	69	ILE	0	0.019	0.003	22.631	0.016	0.016	0.000	0.000	0.000	0.000
71	A	70	VAL	0	-0.039	-0.017	19.487	-0.015	-0.015	0.000	0.000	0.000	0.000
72	A	71	ASN	0	0.026	0.004	20.457	0.016	0.016	0.000	0.000	0.000	0.000
73	A	72	ARG	1	0.916	0.939	16.253	-0.093	-0.093	0.000	0.000	0.000	0.000
74	A	73	LEU	0	-0.065	-0.058	18.641	-0.004	-0.004	0.000	0.000	0.000	0.000
75	A	74	ASN	0	-0.024	0.010	21.616	0.000	0.000	0.000	0.000	0.000	0.000
76	A	75	MET	0	-0.038	-0.032	23.131	0.004	0.004	0.000	0.000	0.000	0.000
77	A	76	HIS	0	0.036	0.029	24.707	0.002	0.002	0.000	0.000	0.000	0.000
78	A	77	ASN	0	0.039	0.008	23.327	0.004	0.004	0.000	0.000	0.000	0.000
79	A	78	LEU	0	0.025	0.024	26.102	-0.004	-0.004	0.000	0.000	0.000	0.000
80	A	79	VAL	0	-0.057	-0.036	27.021	0.007	0.007	0.000	0.000	0.000	0.000
81	A	80	GLU	-1	-0.806	-0.875	29.401	0.054	0.054	0.000	0.000	0.000	0.000
82	A	81	PRO	0	-0.023	-0.007	30.797	0.007	0.007	0.000	0.000	0.000	0.000
83	A	82	VAL	0	-0.008	-0.007	30.570	-0.001	-0.001	0.000	0.000	0.000	0.000
84	A	83	ASN	0	0.015	0.017	33.603	0.000	0.000	0.000	0.000	0.000	0.000
85	A	84	LYS	1	0.996	0.976	37.336	-0.051	-0.051	0.000	0.000	0.000	0.000
86	A	85	ASP	-1	-0.979	-0.981	39.959	0.046	0.046	0.000	0.000	0.000	0.000
87	A	86	LEU	0	-0.094	-0.016	33.178	-0.001	-0.001	0.000	0.000	0.000	0.000
88	A	87	GLU	-1	-0.871	-0.919	37.881	0.059	0.059	0.000	0.000	0.000	0.000
89	A	88	PHE	0	0.028	-0.014	31.662	0.001	0.001	0.000	0.000	0.000	0.000
90	A	89	GLN	0	-0.018	-0.016	35.488	-0.005	-0.005	0.000	0.000	0.000	0.000
91	A	90	LEU	0	-0.003	0.006	30.251	0.001	0.001	0.000	0.000	0.000	0.000
92	A	91	HIS	0	-0.004	-0.002	33.030	-0.002	-0.002	0.000	0.000	0.000	0.000
93	A	92	GLU	-1	-0.862	-0.904	28.339	0.145	0.145	0.000	0.000	0.000	0.000
94	A	93	PRO	0	-0.076	-0.043	27.023	-0.006	-0.006	0.000	0.000	0.000	0.000
95	A	94	PHE	0	0.030	-0.014	28.038	0.006	0.006	0.000	0.000	0.000	0.000
96	A	95	LEU	0	-0.015	-0.005	28.992	0.002	0.002	0.000	0.000	0.000	0.000
97	A	96	LEU	0	-0.008	-0.007	31.321	-0.004	-0.004	0.000	0.000	0.000	0.000
98	A	97	TYR	0	-0.044	-0.046	31.125	0.005	0.005	0.000	0.000	0.000	0.000
99	A	98	ARG	1	0.899	0.954	35.551	-0.055	-0.055	0.000	0.000	0.000	0.000
100	A	99	ASN	0	0.081	0.028	35.793	0.000	0.000	0.000	0.000	0.000	0.000
101	A	100	ALA	0	0.081	0.035	38.618	-0.002	-0.002	0.000	0.000	0.000	0.000
102	A	101	SER	0	-0.086	-0.022	39.618	-0.003	-0.003	0.000	0.000	0.000	0.000
103	A	102	LEU	0	-0.025	-0.019	41.587	-0.002	-0.002	0.000	0.000	0.000	0.000
104	A	103	SER	0	-0.029	-0.019	38.363	-0.001	-0.001	0.000	0.000	0.000	0.000
105	A	104	ILE	0	-0.025	-0.012	37.984	0.003	0.003	0.000	0.000	0.000	0.000
106	A	105	TYR	0	0.026	0.009	32.785	-0.003	-0.003	0.000	0.000	0.000	0.000
107	A	106	SER	0	-0.011	-0.013	32.468	0.005	0.005	0.000	0.000	0.000	0.000
108	A	107	ILE	0	0.027	0.023	26.188	-0.003	-0.003	0.000	0.000	0.000	0.000
109	A	108	TRP	0	-0.025	-0.010	22.798	0.006	0.006	0.000	0.000	0.000	0.000
110	A	109	PHE	0	0.049	0.007	22.865	0.003	0.003	0.000	0.000	0.000	0.000
111	A	110	TYR	0	-0.036	-0.006	17.972	0.001	0.001	0.000	0.000	0.000	0.000
112	A	111	ASP	-1	-0.827	-0.902	18.337	0.322	0.322	0.000	0.000	0.000	0.000
113	A	112	LYS	1	0.931	0.934	21.106	-0.151	-0.151	0.000	0.000	0.000	0.000
114	A	113	ASN	0	0.002	-0.019	20.362	-0.037	-0.037	0.000	0.000	0.000	0.000
115	A	114	ASP	-1	-0.808	-0.907	19.098	0.333	0.333	0.000	0.000	0.000	0.000
116	A	115	CYS	0	-0.084	-0.010	21.904	-0.018	-0.018	0.000	0.000	0.000	0.000
117	A	116	HIS	0	-0.015	-0.018	25.517	-0.009	-0.009	0.000	0.000	0.000	0.000
118	A	117	ARG	1	0.774	0.863	19.077	-0.323	-0.323	0.000	0.000	0.000	0.000
119	A	118	ILE	0	0.003	0.007	21.954	-0.008	-0.008	0.000	0.000	0.000	0.000
120	A	119	ALA	0	0.022	0.008	25.599	-0.014	-0.014	0.000	0.000	0.000	0.000
121	A	120	LYS	1	0.904	0.957	27.816	-0.149	-0.149	0.000	0.000	0.000	0.000
122	A	121	LEU	0	0.021	0.015	24.605	-0.006	-0.006	0.000	0.000	0.000	0.000
123	A	122	MET	0	-0.039	-0.028	28.139	-0.009	-0.009	0.000	0.000	0.000	0.000
124	A	123	ALA	0	-0.011	-0.013	30.518	-0.008	-0.008	0.000	0.000	0.000	0.000
125	A	124	ASP	-1	-0.915	-0.948	30.718	0.124	0.124	0.000	0.000	0.000	0.000
126	A	125	VAL	0	-0.066	-0.033	29.516	-0.005	-0.005	0.000	0.000	0.000	0.000
127	A	126	VAL	0	-0.048	-0.033	32.737	-0.005	-0.005	0.000	0.000	0.000	0.000
128	A	127	GLU	-1	-1.019	-1.018	35.717	0.077	0.077	0.000	0.000	0.000	0.000
129	A	128	GLU	-1	-0.845	-0.898	34.743	0.080	0.080	0.000	0.000	0.000	0.000
130	A	129	GLU	-1	-1.073	-1.033	35.171	0.064	0.064	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:0:LEU)