FMO DATABASE

FMODB ID: R9YK8

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	OptAll
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	-1179685.527306
FMO2-HF: Nuclear repulsion	1126467.678531
FMO2-HF: Total energy	-53217.848775
FMO2-MP2: Total energy	-53371.740449

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.
-12.821	-9.955	9.387	-5.449	-6.803	-0.047

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 : 0.003 / q_NPA : -0.006

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	-0.736	-0.854	1.925	-15.366	-14.828	8.176	-4.455	-4.258	-0.046
4	A	3	ALA	0	-0.012	0.001	2.536	-0.215	0.817	0.807	-0.672	-1.167	-0.001
5	A	4	LEU	0	-0.007	-0.005	2.791	0.005	1.093	0.406	-0.314	-1.181	0.000
6	A	5	SER	0	0.006	0.006	5.379	0.420	0.521	-0.001	-0.003	-0.096	0.000
7	A	6	ARG	1	0.832	0.906	4.359	2.149	2.256	-0.001	-0.005	-0.101	0.000
8	A	7	ALA	0	0.063	0.038	8.070	0.198	0.198	0.000	0.000	0.000	0.000
9	A	8	GLY	0	0.027	0.009	9.437	0.146	0.146	0.000	0.000	0.000	0.000
10	A	9	GLN	0	-0.005	0.011	11.273	0.055	0.055	0.000	0.000	0.000	0.000
11	A	10	GLU	-1	-0.935	-0.981	11.024	-0.659	-0.659	0.000	0.000	0.000	0.000
12	A	11	MET	0	-0.026	-0.024	11.625	0.069	0.069	0.000	0.000	0.000	0.000
13	A	12	SER	0	-0.013	-0.011	14.963	0.060	0.060	0.000	0.000	0.000	0.000
14	A	13	LEU	0	-0.035	-0.009	17.187	0.035	0.035	0.000	0.000	0.000	0.000
15	A	14	ALA	0	-0.038	-0.020	18.622	0.025	0.025	0.000	0.000	0.000	0.000
16	A	15	ALA	0	-0.004	-0.008	19.191	0.022	0.022	0.000	0.000	0.000	0.000
17	A	16	LEU	0	0.014	0.009	20.983	0.019	0.019	0.000	0.000	0.000	0.000
18	A	17	LYS	1	0.860	0.936	22.562	0.184	0.184	0.000	0.000	0.000	0.000
19	A	18	GLN	0	-0.048	-0.021	23.307	-0.002	-0.002	0.000	0.000	0.000	0.000
20	A	19	HIS	0	-0.039	-0.012	26.094	0.005	0.005	0.000	0.000	0.000	0.000
21	A	20	ASP	-1	-0.768	-0.872	27.462	-0.075	-0.075	0.000	0.000	0.000	0.000
22	A	21	PRO	0	0.011	0.006	28.142	-0.007	-0.007	0.000	0.000	0.000	0.000
23	A	22	TYR	0	-0.019	-0.002	29.125	-0.003	-0.003	0.000	0.000	0.000	0.000
24	A	23	ILE	0	-0.009	0.027	24.093	-0.002	-0.002	0.000	0.000	0.000	0.000
25	A	24	THR	0	0.015	0.009	25.456	-0.014	-0.014	0.000	0.000	0.000	0.000
26	A	25	SER	0	-0.028	-0.031	21.284	-0.017	-0.017	0.000	0.000	0.000	0.000
27	A	26	ILE	0	0.031	0.025	17.075	0.016	0.016	0.000	0.000	0.000	0.000
28	A	27	ALA	0	-0.074	-0.040	20.146	-0.010	-0.010	0.000	0.000	0.000	0.000
29	A	28	ASP	-1	-0.785	-0.866	18.833	-0.046	-0.046	0.000	0.000	0.000	0.000
30	A	29	LEU	0	-0.041	-0.027	13.821	-0.018	-0.018	0.000	0.000	0.000	0.000
31	A	30	THR	0	-0.016	-0.008	17.434	0.007	0.007	0.000	0.000	0.000	0.000
32	A	31	GLY	0	0.011	0.005	15.770	-0.010	-0.010	0.000	0.000	0.000	0.000
33	A	32	GLN	0	-0.074	-0.047	16.677	-0.011	-0.011	0.000	0.000	0.000	0.000
34	A	33	VAL	0	-0.006	0.004	19.058	0.009	0.009	0.000	0.000	0.000	0.000
35	A	34	ALA	0	0.020	0.002	22.630	-0.004	-0.004	0.000	0.000	0.000	0.000
36	A	35	LEU	0	-0.005	0.021	25.578	0.001	0.001	0.000	0.000	0.000	0.000
37	A	36	TYR	0	-0.030	-0.004	28.654	0.002	0.002	0.000	0.000	0.000	0.000
38	A	37	THR	0	0.062	0.024	32.327	-0.004	-0.004	0.000	0.000	0.000	0.000
39	A	38	PHE	0	-0.026	-0.010	35.789	0.003	0.003	0.000	0.000	0.000	0.000
40	A	39	CYS	0	-0.005	0.001	39.158	-0.004	-0.004	0.000	0.000	0.000	0.000
41	A	40	PRO	0	0.051	0.010	41.964	0.001	0.001	0.000	0.000	0.000	0.000
42	A	41	LYS	1	0.906	0.955	45.330	-0.004	-0.004	0.000	0.000	0.000	0.000
43	A	42	ALA	0	-0.052	-0.039	44.463	0.000	0.000	0.000	0.000	0.000	0.000
44	A	43	ASN	0	-0.053	-0.009	45.095	0.001	0.001	0.000	0.000	0.000	0.000
45	A	44	GLN	0	0.042	0.024	40.439	0.001	0.001	0.000	0.000	0.000	0.000
46	A	45	TRP	0	0.009	0.002	35.661	-0.002	-0.002	0.000	0.000	0.000	0.000
47	A	46	GLU	-1	-0.924	-0.958	36.550	0.011	0.011	0.000	0.000	0.000	0.000
48	A	47	LYS	1	0.867	0.922	30.976	-0.016	-0.016	0.000	0.000	0.000	0.000
49	A	48	THR	0	0.029	0.004	29.758	-0.003	-0.003	0.000	0.000	0.000	0.000
50	A	49	ASP	-1	-0.864	-0.929	29.054	-0.006	-0.006	0.000	0.000	0.000	0.000
51	A	50	ILE	0	0.011	0.012	25.399	-0.004	-0.004	0.000	0.000	0.000	0.000
52	A	51	GLU	-1	-0.868	-0.922	21.360	0.061	0.061	0.000	0.000	0.000	0.000
53	A	52	GLY	0	-0.018	-0.028	19.368	-0.009	-0.009	0.000	0.000	0.000	0.000
54	A	53	THR	0	-0.024	0.014	16.158	0.011	0.011	0.000	0.000	0.000	0.000
55	A	54	LEU	0	0.019	0.016	18.822	-0.014	-0.014	0.000	0.000	0.000	0.000
56	A	55	PHE	0	-0.018	-0.027	16.308	-0.011	-0.011	0.000	0.000	0.000	0.000
57	A	56	VAL	0	0.064	0.033	21.210	0.008	0.008	0.000	0.000	0.000	0.000
58	A	57	TYR	0	-0.025	-0.021	22.248	-0.017	-0.017	0.000	0.000	0.000	0.000
59	A	58	ARG	1	0.958	0.976	21.443	0.136	0.136	0.000	0.000	0.000	0.000
60	A	59	ARG	1	0.751	0.839	26.656	0.064	0.064	0.000	0.000	0.000	0.000
61	A	60	SER	0	-0.032	-0.027	29.493	0.003	0.003	0.000	0.000	0.000	0.000
62	A	61	ALA	0	-0.022	-0.020	31.778	0.003	0.003	0.000	0.000	0.000	0.000
63	A	62	SER	0	-0.036	-0.010	33.878	-0.001	-0.001	0.000	0.000	0.000	0.000
64	A	63	PRO	0	-0.024	-0.007	33.677	-0.001	-0.001	0.000	0.000	0.000	0.000
65	A	64	TYR	0	0.033	0.008	32.261	-0.005	-0.005	0.000	0.000	0.000	0.000
66	A	65	HIS	0	0.039	0.019	28.567	-0.013	-0.013	0.000	0.000	0.000	0.000
67	A	66	GLY	0	0.012	0.009	27.981	0.006	0.006	0.000	0.000	0.000	0.000
68	A	67	PHE	0	-0.008	-0.005	25.686	-0.006	-0.006	0.000	0.000	0.000	0.000
69	A	68	THR	0	-0.025	-0.024	22.757	-0.001	-0.001	0.000	0.000	0.000	0.000
70	A	69	ILE	0	0.027	0.009	22.577	0.001	0.001	0.000	0.000	0.000	0.000
71	A	70	VAL	0	-0.013	-0.004	19.110	0.001	0.001	0.000	0.000	0.000	0.000
72	A	71	ASN	0	-0.005	-0.017	20.114	0.012	0.012	0.000	0.000	0.000	0.000
73	A	72	ARG	1	0.865	0.923	16.266	0.052	0.052	0.000	0.000	0.000	0.000
74	A	73	LEU	0	-0.037	-0.023	18.844	0.009	0.009	0.000	0.000	0.000	0.000
75	A	74	ASN	0	-0.004	-0.008	21.568	0.000	0.000	0.000	0.000	0.000	0.000
76	A	75	MET	0	-0.028	-0.011	23.122	-0.006	-0.006	0.000	0.000	0.000	0.000
77	A	76	HIS	0	0.000	0.010	24.982	-0.010	-0.010	0.000	0.000	0.000	0.000
78	A	77	ASN	0	0.055	0.031	23.225	0.008	0.008	0.000	0.000	0.000	0.000
79	A	78	LEU	0	0.040	0.039	25.927	0.002	0.002	0.000	0.000	0.000	0.000
80	A	79	VAL	0	-0.039	-0.023	26.646	-0.009	-0.009	0.000	0.000	0.000	0.000
81	A	80	GLU	-1	-0.785	-0.852	29.004	-0.022	-0.022	0.000	0.000	0.000	0.000
82	A	81	PRO	0	-0.040	-0.012	30.551	-0.005	-0.005	0.000	0.000	0.000	0.000
83	A	82	VAL	0	0.000	-0.006	29.522	0.005	0.005	0.000	0.000	0.000	0.000
84	A	83	ASN	0	0.008	-0.009	32.702	-0.002	-0.002	0.000	0.000	0.000	0.000
85	A	84	LYS	1	0.886	0.930	36.311	0.036	0.036	0.000	0.000	0.000	0.000
86	A	85	ASP	-1	-0.943	-0.966	38.855	-0.024	-0.024	0.000	0.000	0.000	0.000
87	A	86	LEU	0	-0.064	-0.022	32.335	0.002	0.002	0.000	0.000	0.000	0.000
88	A	87	GLU	-1	-0.832	-0.881	36.647	-0.006	-0.006	0.000	0.000	0.000	0.000
89	A	88	PHE	0	0.051	-0.010	30.640	0.001	0.001	0.000	0.000	0.000	0.000
90	A	89	GLN	0	-0.019	-0.005	34.554	0.003	0.003	0.000	0.000	0.000	0.000
91	A	90	LEU	0	-0.012	-0.003	28.934	0.001	0.001	0.000	0.000	0.000	0.000
92	A	91	HIS	0	-0.037	-0.029	31.948	0.003	0.003	0.000	0.000	0.000	0.000
93	A	92	GLU	-1	-0.807	-0.876	28.259	0.056	0.056	0.000	0.000	0.000	0.000
94	A	93	PRO	0	-0.068	-0.025	26.455	0.002	0.002	0.000	0.000	0.000	0.000
95	A	94	PHE	0	0.028	-0.019	27.357	0.000	0.000	0.000	0.000	0.000	0.000
96	A	95	LEU	0	-0.002	0.000	28.222	0.000	0.000	0.000	0.000	0.000	0.000
97	A	96	LEU	0	-0.012	0.002	30.607	-0.003	-0.003	0.000	0.000	0.000	0.000
98	A	97	TYR	0	-0.035	-0.048	31.163	-0.001	-0.001	0.000	0.000	0.000	0.000
99	A	98	ARG	1	0.809	0.891	34.917	0.008	0.008	0.000	0.000	0.000	0.000
100	A	99	ASN	0	0.022	-0.005	36.297	0.001	0.001	0.000	0.000	0.000	0.000
101	A	100	ALA	0	0.094	0.042	38.254	0.002	0.002	0.000	0.000	0.000	0.000
102	A	101	SER	0	-0.077	-0.037	39.676	0.000	0.000	0.000	0.000	0.000	0.000
103	A	102	LEU	0	-0.029	-0.028	41.803	0.002	0.002	0.000	0.000	0.000	0.000
104	A	103	SER	0	-0.036	0.010	38.425	0.002	0.002	0.000	0.000	0.000	0.000
105	A	104	ILE	0	0.008	0.004	38.333	-0.001	-0.001	0.000	0.000	0.000	0.000
106	A	105	TYR	0	0.035	0.014	33.000	0.002	0.002	0.000	0.000	0.000	0.000
107	A	106	SER	0	-0.024	-0.021	32.578	0.002	0.002	0.000	0.000	0.000	0.000
108	A	107	ILE	0	0.021	0.022	26.061	-0.001	-0.001	0.000	0.000	0.000	0.000
109	A	108	TRP	0	-0.004	0.005	23.019	0.003	0.003	0.000	0.000	0.000	0.000
110	A	109	PHE	0	0.049	0.001	22.171	-0.007	-0.007	0.000	0.000	0.000	0.000
111	A	110	TYR	0	-0.018	0.000	18.495	0.018	0.018	0.000	0.000	0.000	0.000
112	A	111	ASP	-1	-0.812	-0.892	18.262	0.167	0.167	0.000	0.000	0.000	0.000
113	A	112	LYS	1	0.898	0.927	20.890	-0.096	-0.096	0.000	0.000	0.000	0.000
114	A	113	ASN	0	-0.068	-0.052	19.779	-0.026	-0.026	0.000	0.000	0.000	0.000
115	A	114	ASP	-1	-0.775	-0.878	18.298	0.042	0.042	0.000	0.000	0.000	0.000
116	A	115	CYS	0	-0.098	-0.017	21.062	-0.015	-0.015	0.000	0.000	0.000	0.000
117	A	116	HIS	0	-0.017	-0.026	24.798	-0.014	-0.014	0.000	0.000	0.000	0.000
118	A	117	ARG	1	0.757	0.855	18.113	-0.012	-0.012	0.000	0.000	0.000	0.000
119	A	118	ILE	0	0.016	0.008	21.064	-0.011	-0.011	0.000	0.000	0.000	0.000
120	A	119	ALA	0	0.021	0.008	24.592	-0.007	-0.007	0.000	0.000	0.000	0.000
121	A	120	LYS	1	0.784	0.876	27.185	0.012	0.012	0.000	0.000	0.000	0.000
122	A	121	LEU	0	0.005	0.006	23.361	-0.005	-0.005	0.000	0.000	0.000	0.000
123	A	122	MET	0	-0.027	-0.019	26.451	-0.007	-0.007	0.000	0.000	0.000	0.000
124	A	123	ALA	0	-0.002	0.001	29.501	-0.002	-0.002	0.000	0.000	0.000	0.000
125	A	124	ASP	-1	-0.795	-0.877	29.122	-0.024	-0.024	0.000	0.000	0.000	0.000
126	A	125	VAL	0	-0.062	-0.043	28.146	-0.003	-0.003	0.000	0.000	0.000	0.000
127	A	126	VAL	0	-0.049	-0.020	31.252	-0.002	-0.002	0.000	0.000	0.000	0.000
128	A	127	GLU	-1	-0.979	-0.980	34.447	-0.021	-0.021	0.000	0.000	0.000	0.000
129	A	128	GLU	-1	-0.980	-0.978	32.709	-0.045	-0.045	0.000	0.000	0.000	0.000
130	A	129	GLU	-1	-0.842	-0.899	35.124	-0.045	-0.045	0.000	0.000	0.000	0.000

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