FMO DATABASE

FMODB ID: YV882

Calculation Name: 4BOU-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4BOU

Chain ID: A

ChEMBL ID:

UniProt ID: Q5T2D3

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	141
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1325904.80278
FMO2-HF: Nuclear repulsion	1269989.646382
FMO2-HF: Total energy	-55915.156398
FMO2-MP2: Total energy	-56081.350843

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:50:GLY)

Summations of interaction energy for fragment #1(A:50:GLY)

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.
-2.165	-0.397	-0.007	-0.801	-0.96	0.003

Interaction energy analysis for fragmet #1(A:50:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.047 / q_NPA : 0.023

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	52	GLU	-1	-0.873	-0.921	3.631	-4.217	-2.449	-0.007	-0.801	-0.960	0.003
4	A	53	PHE	0	-0.025	-0.011	5.848	0.902	0.902	0.000	0.000	0.000	0.000
5	A	54	VAL	0	0.033	0.012	9.509	-0.073	-0.073	0.000	0.000	0.000	0.000
6	A	55	SER	0	-0.017	-0.029	11.873	0.160	0.160	0.000	0.000	0.000	0.000
7	A	56	PHE	0	0.070	0.020	13.454	-0.045	-0.045	0.000	0.000	0.000	0.000
8	A	57	ALA	0	0.039	0.014	14.787	0.049	0.049	0.000	0.000	0.000	0.000
9	A	58	ASN	0	0.012	0.020	14.092	0.069	0.069	0.000	0.000	0.000	0.000
10	A	59	GLN	0	0.036	0.038	10.981	-0.099	-0.099	0.000	0.000	0.000	0.000
11	A	60	LEU	0	-0.016	-0.014	13.572	0.087	0.087	0.000	0.000	0.000	0.000
12	A	61	GLN	0	0.017	0.018	16.899	0.025	0.025	0.000	0.000	0.000	0.000
13	A	62	ALA	0	-0.031	-0.006	14.037	0.057	0.057	0.000	0.000	0.000	0.000
14	A	63	LEU	0	-0.031	-0.010	14.072	0.060	0.060	0.000	0.000	0.000	0.000
15	A	64	GLY	0	0.011	0.010	17.432	0.046	0.046	0.000	0.000	0.000	0.000
16	A	65	LEU	0	-0.090	-0.055	18.504	0.039	0.039	0.000	0.000	0.000	0.000
17	A	66	LYS	1	0.878	0.930	20.650	0.160	0.160	0.000	0.000	0.000	0.000
18	A	67	LEU	0	-0.008	0.002	19.003	0.022	0.022	0.000	0.000	0.000	0.000
19	A	68	ARG	1	0.790	0.878	22.749	0.154	0.154	0.000	0.000	0.000	0.000
20	A	69	GLU	-1	-0.798	-0.901	23.139	-0.288	-0.288	0.000	0.000	0.000	0.000
21	A	70	VAL	0	-0.085	-0.033	26.463	0.022	0.022	0.000	0.000	0.000	0.000
22	A	71	PRO	0	-0.009	-0.019	28.037	-0.010	-0.010	0.000	0.000	0.000	0.000
23	A	72	GLY	0	0.038	0.032	28.131	0.000	0.000	0.000	0.000	0.000	0.000
24	A	73	ASP	-1	-0.779	-0.877	29.005	-0.109	-0.109	0.000	0.000	0.000	0.000
25	A	74	GLY	0	0.097	0.043	29.885	-0.006	-0.006	0.000	0.000	0.000	0.000
26	A	75	ASN	0	-0.086	-0.047	31.452	0.014	0.014	0.000	0.000	0.000	0.000
27	A	76	CYS	0	-0.029	0.021	26.920	0.008	0.008	0.000	0.000	0.000	0.000
28	A	77	LEU	0	0.088	0.048	25.425	-0.004	-0.004	0.000	0.000	0.000	0.000
29	A	78	PHE	0	0.060	0.027	28.067	0.001	0.001	0.000	0.000	0.000	0.000
30	A	79	ARG	1	0.794	0.883	30.666	0.120	0.120	0.000	0.000	0.000	0.000
31	A	80	ALA	0	0.004	0.010	26.044	0.001	0.001	0.000	0.000	0.000	0.000
32	A	81	LEU	0	0.022	0.003	26.872	0.000	0.000	0.000	0.000	0.000	0.000
33	A	82	GLY	0	0.031	0.016	29.355	0.006	0.006	0.000	0.000	0.000	0.000
34	A	83	ASP	-1	-0.775	-0.838	29.450	-0.134	-0.134	0.000	0.000	0.000	0.000
35	A	84	GLN	0	-0.037	-0.013	25.902	0.012	0.012	0.000	0.000	0.000	0.000
36	A	85	LEU	0	-0.021	-0.005	29.578	0.006	0.006	0.000	0.000	0.000	0.000
37	A	86	GLU	-1	-0.777	-0.894	32.661	-0.056	-0.056	0.000	0.000	0.000	0.000
38	A	87	GLY	0	-0.021	0.003	32.999	0.001	0.001	0.000	0.000	0.000	0.000
39	A	88	HIS	0	-0.018	-0.017	33.992	-0.010	-0.010	0.000	0.000	0.000	0.000
40	A	89	SER	0	0.047	0.026	32.421	0.005	0.005	0.000	0.000	0.000	0.000
41	A	90	ARG	1	0.959	0.972	34.417	0.079	0.079	0.000	0.000	0.000	0.000
42	A	91	ASN	0	-0.051	-0.031	37.377	0.004	0.004	0.000	0.000	0.000	0.000
43	A	92	HIS	0	0.030	0.005	34.347	0.004	0.004	0.000	0.000	0.000	0.000
44	A	93	LEU	0	0.025	0.014	35.978	0.002	0.002	0.000	0.000	0.000	0.000
45	A	94	LYS	1	0.884	0.959	38.803	0.052	0.052	0.000	0.000	0.000	0.000
46	A	95	HIS	0	-0.016	-0.016	34.513	0.007	0.007	0.000	0.000	0.000	0.000
47	A	96	ARG	1	0.808	0.919	33.244	0.074	0.074	0.000	0.000	0.000	0.000
48	A	97	GLN	0	-0.054	-0.036	36.277	0.001	0.001	0.000	0.000	0.000	0.000
49	A	98	GLU	-1	-0.866	-0.949	38.091	-0.035	-0.035	0.000	0.000	0.000	0.000
50	A	99	THR	0	-0.072	-0.057	32.716	0.004	0.004	0.000	0.000	0.000	0.000
51	A	100	VAL	0	0.040	0.013	36.110	0.005	0.005	0.000	0.000	0.000	0.000
52	A	101	ASP	-1	-0.853	-0.919	37.884	-0.020	-0.020	0.000	0.000	0.000	0.000
53	A	102	TYR	0	-0.043	-0.026	35.359	0.006	0.006	0.000	0.000	0.000	0.000
54	A	103	MET	0	-0.018	-0.017	33.285	0.002	0.002	0.000	0.000	0.000	0.000
55	A	104	ILE	0	-0.013	-0.003	37.232	0.004	0.004	0.000	0.000	0.000	0.000
56	A	105	LYS	1	0.820	0.912	40.213	0.001	0.001	0.000	0.000	0.000	0.000
57	A	106	GLN	0	-0.025	0.005	37.617	0.000	0.000	0.000	0.000	0.000	0.000
58	A	107	ARG	1	0.818	0.872	37.815	-0.005	-0.005	0.000	0.000	0.000	0.000
59	A	108	GLU	-1	-0.898	-0.954	37.947	0.019	0.019	0.000	0.000	0.000	0.000
60	A	109	ASP	-1	-0.837	-0.907	34.514	0.033	0.033	0.000	0.000	0.000	0.000
61	A	110	PHE	0	-0.057	-0.057	31.297	0.001	0.001	0.000	0.000	0.000	0.000
62	A	111	GLU	-1	-0.808	-0.869	33.699	0.010	0.010	0.000	0.000	0.000	0.000
63	A	112	PRO	0	-0.021	-0.010	32.066	0.000	0.000	0.000	0.000	0.000	0.000
64	A	113	PHE	0	-0.057	-0.032	27.035	0.004	0.004	0.000	0.000	0.000	0.000
65	A	114	VAL	0	-0.094	-0.034	29.979	-0.006	-0.006	0.000	0.000	0.000	0.000
66	A	115	GLU	-1	-0.937	-0.959	28.626	-0.007	-0.007	0.000	0.000	0.000	0.000
67	A	116	ASP	-1	-0.867	-0.954	31.678	0.031	0.031	0.000	0.000	0.000	0.000
68	A	117	ASP	-1	-0.976	-0.987	34.456	0.003	0.003	0.000	0.000	0.000	0.000
69	A	118	ILE	0	-0.063	-0.012	33.624	-0.006	-0.006	0.000	0.000	0.000	0.000
70	A	119	PRO	0	-0.025	-0.012	37.369	0.002	0.002	0.000	0.000	0.000	0.000
71	A	120	PHE	0	0.096	0.041	36.694	-0.005	-0.005	0.000	0.000	0.000	0.000
72	A	121	GLU	-1	-0.810	-0.910	38.973	-0.004	-0.004	0.000	0.000	0.000	0.000
73	A	122	LYS	1	0.925	0.967	38.440	0.026	0.026	0.000	0.000	0.000	0.000
74	A	123	HIS	0	0.002	-0.007	31.492	-0.006	-0.006	0.000	0.000	0.000	0.000
75	A	124	VAL	0	0.018	0.003	36.371	-0.006	-0.006	0.000	0.000	0.000	0.000
76	A	125	ALA	0	-0.010	0.000	38.084	-0.004	-0.004	0.000	0.000	0.000	0.000
77	A	126	SER	0	-0.046	-0.030	36.141	-0.004	-0.004	0.000	0.000	0.000	0.000
78	A	127	LEU	0	-0.005	0.012	32.596	-0.008	-0.008	0.000	0.000	0.000	0.000
79	A	128	ALA	0	0.039	0.025	35.944	-0.005	-0.005	0.000	0.000	0.000	0.000
80	A	129	LYS	1	0.906	0.967	38.571	0.050	0.050	0.000	0.000	0.000	0.000
81	A	130	PRO	0	0.018	-0.012	37.298	-0.004	-0.004	0.000	0.000	0.000	0.000
82	A	131	GLY	0	-0.060	-0.031	34.925	0.001	0.001	0.000	0.000	0.000	0.000
83	A	132	THR	0	-0.060	-0.023	33.319	-0.007	-0.007	0.000	0.000	0.000	0.000
84	A	133	PHE	0	0.055	0.035	27.513	0.001	0.001	0.000	0.000	0.000	0.000
85	A	134	ALA	0	-0.002	0.008	29.177	0.010	0.010	0.000	0.000	0.000	0.000
86	A	135	GLY	0	0.101	0.050	25.815	-0.013	-0.013	0.000	0.000	0.000	0.000
87	A	136	ASN	0	0.021	-0.025	21.124	-0.014	-0.014	0.000	0.000	0.000	0.000
88	A	137	ASP	-1	-0.785	-0.868	25.313	-0.024	-0.024	0.000	0.000	0.000	0.000
89	A	138	ALA	0	0.041	0.015	28.792	0.003	0.003	0.000	0.000	0.000	0.000
90	A	139	ILE	0	-0.049	-0.019	23.658	-0.001	-0.001	0.000	0.000	0.000	0.000
91	A	140	VAL	0	0.005	0.005	26.586	0.003	0.003	0.000	0.000	0.000	0.000
92	A	141	ALA	0	0.030	0.021	28.745	0.003	0.003	0.000	0.000	0.000	0.000
93	A	142	PHE	0	-0.025	-0.013	30.296	0.001	0.001	0.000	0.000	0.000	0.000
94	A	143	ALA	0	-0.016	-0.018	28.323	0.000	0.000	0.000	0.000	0.000	0.000
95	A	144	ARG	1	0.897	0.939	30.457	-0.025	-0.025	0.000	0.000	0.000	0.000
96	A	145	ASN	0	-0.057	-0.011	33.107	0.005	0.005	0.000	0.000	0.000	0.000
97	A	146	HIS	1	0.803	0.900	33.404	0.035	0.035	0.000	0.000	0.000	0.000
98	A	147	GLN	0	-0.002	0.006	33.726	0.003	0.003	0.000	0.000	0.000	0.000
99	A	148	LEU	0	-0.065	-0.024	29.188	0.000	0.000	0.000	0.000	0.000	0.000
100	A	149	ASN	0	0.022	-0.003	25.303	0.010	0.010	0.000	0.000	0.000	0.000
101	A	150	VAL	0	-0.004	-0.007	23.354	-0.013	-0.013	0.000	0.000	0.000	0.000
102	A	151	VAL	0	0.013	0.015	18.929	0.012	0.012	0.000	0.000	0.000	0.000
103	A	152	ILE	0	-0.023	-0.018	17.956	-0.024	-0.024	0.000	0.000	0.000	0.000
104	A	153	HIS	0	0.027	0.011	15.602	0.036	0.036	0.000	0.000	0.000	0.000
105	A	154	GLN	0	0.089	0.027	12.609	0.079	0.079	0.000	0.000	0.000	0.000
106	A	155	LEU	0	-0.027	-0.009	10.575	0.011	0.011	0.000	0.000	0.000	0.000
107	A	156	ASN	0	-0.034	-0.042	6.322	0.164	0.164	0.000	0.000	0.000	0.000
108	A	157	ALA	0	0.022	0.025	7.193	-0.051	-0.051	0.000	0.000	0.000	0.000
109	A	158	PRO	0	-0.028	-0.014	8.901	-0.004	-0.004	0.000	0.000	0.000	0.000
110	A	159	LEU	0	-0.046	-0.011	10.859	-0.045	-0.045	0.000	0.000	0.000	0.000
111	A	160	TRP	0	0.035	0.013	12.868	0.114	0.114	0.000	0.000	0.000	0.000
112	A	161	GLN	0	-0.018	-0.029	17.046	-0.006	-0.006	0.000	0.000	0.000	0.000
113	A	162	ILE	0	0.003	0.012	20.590	0.023	0.023	0.000	0.000	0.000	0.000
114	A	163	ARG	1	0.911	0.946	22.156	-0.099	-0.099	0.000	0.000	0.000	0.000
115	A	164	GLY	0	0.048	0.028	26.550	0.004	0.004	0.000	0.000	0.000	0.000
116	A	165	THR	0	-0.089	-0.047	29.993	0.001	0.001	0.000	0.000	0.000	0.000
117	A	166	GLU	-1	-0.857	-0.929	30.263	0.068	0.068	0.000	0.000	0.000	0.000
118	A	167	LYS	1	0.854	0.935	32.131	-0.010	-0.010	0.000	0.000	0.000	0.000
119	A	168	SER	0	0.037	0.021	29.853	0.001	0.001	0.000	0.000	0.000	0.000
120	A	169	SER	0	-0.029	-0.021	29.225	0.000	0.000	0.000	0.000	0.000	0.000
121	A	170	VAL	0	-0.001	0.011	29.453	-0.003	-0.003	0.000	0.000	0.000	0.000
122	A	171	ARG	1	0.863	0.938	29.695	0.056	0.056	0.000	0.000	0.000	0.000
123	A	172	GLU	-1	-0.809	-0.899	23.957	-0.007	-0.007	0.000	0.000	0.000	0.000
124	A	173	LEU	0	-0.063	-0.022	26.423	-0.012	-0.012	0.000	0.000	0.000	0.000
125	A	174	HIS	0	0.045	0.025	20.556	0.020	0.020	0.000	0.000	0.000	0.000
126	A	175	ILE	0	-0.003	-0.005	21.792	-0.007	-0.007	0.000	0.000	0.000	0.000
127	A	176	ALA	0	-0.012	-0.007	18.806	-0.013	-0.013	0.000	0.000	0.000	0.000
128	A	177	TYR	0	-0.031	-0.012	16.522	0.016	0.016	0.000	0.000	0.000	0.000
129	A	178	ARG	1	0.777	0.858	17.074	0.298	0.298	0.000	0.000	0.000	0.000
130	A	179	TYR	0	0.018	0.012	18.548	0.017	0.017	0.000	0.000	0.000	0.000
131	A	180	GLY	0	0.032	0.016	19.730	0.020	0.020	0.000	0.000	0.000	0.000
132	A	181	GLU	-1	-0.876	-0.930	21.665	-0.109	-0.109	0.000	0.000	0.000	0.000
133	A	182	HIS	0	-0.077	-0.055	22.654	0.026	0.026	0.000	0.000	0.000	0.000
134	A	183	TYR	0	0.050	-0.001	21.647	-0.022	-0.022	0.000	0.000	0.000	0.000
135	A	184	ASP	-1	-0.778	-0.860	22.362	-0.247	-0.247	0.000	0.000	0.000	0.000
136	A	185	SER	0	-0.026	-0.038	23.453	0.008	0.008	0.000	0.000	0.000	0.000
137	A	186	VAL	0	0.036	0.027	19.890	-0.022	-0.022	0.000	0.000	0.000	0.000
138	A	187	ARG	1	0.845	0.904	23.027	0.159	0.159	0.000	0.000	0.000	0.000
139	A	188	ARG	1	0.862	0.928	23.711	0.122	0.122	0.000	0.000	0.000	0.000
140	A	189	ILE	0	-0.012	0.008	21.598	0.005	0.005	0.000	0.000	0.000	0.000
141	A	190	ASN	0	0.047	0.027	25.679	0.004	0.004	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:50:GLY)