FMO DATABASE

FMODB ID: VQLL1

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1326811.639338
FMO2-HF: Nuclear repulsion	1270896.306847
FMO2-HF: Total energy	-55915.332491
FMO2-MP2: Total energy	-56081.489811

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.
-1.006	0.811	0.008	-0.819	-1.005	0.002

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 : 0.064 / q_NPA : 0.031

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	-0.882	-0.930	3.228	-3.090	-1.273	0.008	-0.819	-1.005	0.002
4	A	53	PHE	0	-0.027	-0.012	5.465	0.812	0.812	0.000	0.000	0.000	0.000
5	A	54	VAL	0	0.024	0.006	9.254	0.031	0.031	0.000	0.000	0.000	0.000
6	A	55	SER	0	-0.012	-0.025	11.619	0.193	0.193	0.000	0.000	0.000	0.000
7	A	56	PHE	0	0.047	0.024	13.261	-0.024	-0.024	0.000	0.000	0.000	0.000
8	A	57	ALA	0	0.050	0.017	14.323	0.060	0.060	0.000	0.000	0.000	0.000
9	A	58	ASN	0	0.000	0.010	13.895	0.006	0.006	0.000	0.000	0.000	0.000
10	A	59	GLN	0	0.032	0.027	10.897	-0.076	-0.076	0.000	0.000	0.000	0.000
11	A	60	LEU	0	-0.022	-0.011	13.059	0.092	0.092	0.000	0.000	0.000	0.000
12	A	61	GLN	0	0.021	0.008	16.525	0.010	0.010	0.000	0.000	0.000	0.000
13	A	62	ALA	0	-0.034	-0.015	13.631	0.051	0.051	0.000	0.000	0.000	0.000
14	A	63	LEU	0	-0.016	0.000	13.860	0.054	0.054	0.000	0.000	0.000	0.000
15	A	64	GLY	0	0.009	0.014	17.152	0.043	0.043	0.000	0.000	0.000	0.000
16	A	65	LEU	0	-0.088	-0.043	18.042	0.034	0.034	0.000	0.000	0.000	0.000
17	A	66	LYS	1	0.867	0.918	20.323	0.136	0.136	0.000	0.000	0.000	0.000
18	A	67	LEU	0	0.006	0.007	19.110	0.023	0.023	0.000	0.000	0.000	0.000
19	A	68	ARG	1	0.772	0.867	22.863	0.126	0.126	0.000	0.000	0.000	0.000
20	A	69	GLU	-1	-0.764	-0.879	22.862	-0.251	-0.251	0.000	0.000	0.000	0.000
21	A	70	VAL	0	-0.091	-0.031	26.224	0.018	0.018	0.000	0.000	0.000	0.000
22	A	71	PRO	0	0.003	-0.014	28.098	-0.008	-0.008	0.000	0.000	0.000	0.000
23	A	72	GLY	0	0.037	0.024	27.987	0.004	0.004	0.000	0.000	0.000	0.000
24	A	73	ASP	-1	-0.762	-0.855	28.848	-0.084	-0.084	0.000	0.000	0.000	0.000
25	A	74	GLY	0	0.101	0.042	29.960	-0.003	-0.003	0.000	0.000	0.000	0.000
26	A	75	ASN	0	-0.059	-0.035	31.028	0.014	0.014	0.000	0.000	0.000	0.000
27	A	76	CYS	0	-0.076	-0.002	26.745	0.007	0.007	0.000	0.000	0.000	0.000
28	A	77	LEU	0	0.096	0.050	25.380	-0.004	-0.004	0.000	0.000	0.000	0.000
29	A	78	PHE	0	0.061	0.025	27.951	0.000	0.000	0.000	0.000	0.000	0.000
30	A	79	ARG	1	0.762	0.865	30.487	0.094	0.094	0.000	0.000	0.000	0.000
31	A	80	ALA	0	0.002	0.006	26.119	0.000	0.000	0.000	0.000	0.000	0.000
32	A	81	LEU	0	0.016	0.007	27.098	0.000	0.000	0.000	0.000	0.000	0.000
33	A	82	GLY	0	0.059	0.022	29.519	0.004	0.004	0.000	0.000	0.000	0.000
34	A	83	ASP	-1	-0.801	-0.855	29.513	-0.107	-0.107	0.000	0.000	0.000	0.000
35	A	84	GLN	0	-0.038	-0.014	25.901	0.009	0.009	0.000	0.000	0.000	0.000
36	A	85	LEU	0	-0.009	0.013	29.736	0.005	0.005	0.000	0.000	0.000	0.000
37	A	86	GLU	-1	-0.756	-0.878	32.921	-0.036	-0.036	0.000	0.000	0.000	0.000
38	A	87	GLY	0	-0.021	0.002	33.372	0.000	0.000	0.000	0.000	0.000	0.000
39	A	88	HIS	0	-0.025	-0.022	33.982	-0.013	-0.013	0.000	0.000	0.000	0.000
40	A	89	SER	0	0.069	0.036	32.105	0.007	0.007	0.000	0.000	0.000	0.000
41	A	90	ARG	1	0.938	0.967	34.043	0.065	0.065	0.000	0.000	0.000	0.000
42	A	91	ASN	0	-0.026	-0.027	37.371	0.001	0.001	0.000	0.000	0.000	0.000
43	A	92	HIS	0	0.018	0.004	34.227	0.005	0.005	0.000	0.000	0.000	0.000
44	A	93	LEU	0	0.017	0.012	35.743	0.003	0.003	0.000	0.000	0.000	0.000
45	A	94	LYS	1	0.822	0.912	38.706	0.032	0.032	0.000	0.000	0.000	0.000
46	A	95	HIS	0	-0.028	-0.015	34.215	0.007	0.007	0.000	0.000	0.000	0.000
47	A	96	ARG	1	0.808	0.909	33.123	0.048	0.048	0.000	0.000	0.000	0.000
48	A	97	GLN	0	-0.060	-0.035	36.161	0.002	0.002	0.000	0.000	0.000	0.000
49	A	98	GLU	-1	-0.800	-0.908	37.842	-0.016	-0.016	0.000	0.000	0.000	0.000
50	A	99	THR	0	-0.061	-0.040	32.670	0.005	0.005	0.000	0.000	0.000	0.000
51	A	100	VAL	0	0.038	0.013	36.019	0.005	0.005	0.000	0.000	0.000	0.000
52	A	101	ASP	-1	-0.852	-0.915	37.942	-0.003	-0.003	0.000	0.000	0.000	0.000
53	A	102	TYR	0	-0.041	-0.031	35.760	0.005	0.005	0.000	0.000	0.000	0.000
54	A	103	MET	0	-0.013	-0.010	33.284	0.002	0.002	0.000	0.000	0.000	0.000
55	A	104	ILE	0	-0.010	-0.005	37.377	0.004	0.004	0.000	0.000	0.000	0.000
56	A	105	LYS	1	0.770	0.876	40.917	-0.019	-0.019	0.000	0.000	0.000	0.000
57	A	106	GLN	0	0.008	0.017	37.830	-0.002	-0.002	0.000	0.000	0.000	0.000
58	A	107	ARG	1	0.789	0.857	38.013	-0.023	-0.023	0.000	0.000	0.000	0.000
59	A	108	GLU	-1	-0.874	-0.950	38.115	0.039	0.039	0.000	0.000	0.000	0.000
60	A	109	ASP	-1	-0.822	-0.886	34.441	0.058	0.058	0.000	0.000	0.000	0.000
61	A	110	PHE	0	-0.040	-0.043	31.473	0.004	0.004	0.000	0.000	0.000	0.000
62	A	111	GLU	-1	-0.804	-0.869	33.965	0.031	0.031	0.000	0.000	0.000	0.000
63	A	112	PRO	0	-0.026	-0.019	32.673	0.000	0.000	0.000	0.000	0.000	0.000
64	A	113	PHE	0	-0.058	-0.028	27.232	0.008	0.008	0.000	0.000	0.000	0.000
65	A	114	VAL	0	-0.092	-0.035	30.126	-0.005	-0.005	0.000	0.000	0.000	0.000
66	A	115	GLU	-1	-0.933	-0.961	28.662	0.032	0.032	0.000	0.000	0.000	0.000
67	A	116	ASP	-1	-0.885	-0.958	31.727	0.059	0.059	0.000	0.000	0.000	0.000
68	A	117	ASP	-1	-0.967	-0.982	34.449	0.023	0.023	0.000	0.000	0.000	0.000
69	A	118	ILE	0	-0.058	-0.011	33.609	-0.007	-0.007	0.000	0.000	0.000	0.000
70	A	119	PRO	0	-0.020	-0.011	37.457	0.002	0.002	0.000	0.000	0.000	0.000
71	A	120	PHE	0	0.084	0.040	36.673	-0.004	-0.004	0.000	0.000	0.000	0.000
72	A	121	GLU	-1	-0.813	-0.901	38.814	0.014	0.014	0.000	0.000	0.000	0.000
73	A	122	LYS	1	0.931	0.969	38.156	0.005	0.005	0.000	0.000	0.000	0.000
74	A	123	HIS	0	0.005	-0.002	31.523	-0.007	-0.007	0.000	0.000	0.000	0.000
75	A	124	VAL	0	0.014	0.001	36.605	-0.006	-0.006	0.000	0.000	0.000	0.000
76	A	125	ALA	0	0.002	0.002	38.158	-0.005	-0.005	0.000	0.000	0.000	0.000
77	A	126	SER	0	-0.060	-0.030	36.303	-0.005	-0.005	0.000	0.000	0.000	0.000
78	A	127	LEU	0	-0.005	0.008	32.547	-0.007	-0.007	0.000	0.000	0.000	0.000
79	A	128	ALA	0	0.041	0.022	35.840	-0.005	-0.005	0.000	0.000	0.000	0.000
80	A	129	LYS	1	0.908	0.968	38.327	0.029	0.029	0.000	0.000	0.000	0.000
81	A	130	PRO	0	0.020	-0.010	37.111	-0.003	-0.003	0.000	0.000	0.000	0.000
82	A	131	GLY	0	-0.052	-0.023	34.747	0.000	0.000	0.000	0.000	0.000	0.000
83	A	132	THR	0	-0.060	-0.025	33.206	-0.007	-0.007	0.000	0.000	0.000	0.000
84	A	133	PHE	0	0.048	0.030	27.061	-0.001	-0.001	0.000	0.000	0.000	0.000
85	A	134	ALA	0	0.007	0.007	28.476	0.009	0.009	0.000	0.000	0.000	0.000
86	A	135	GLY	0	0.088	0.051	25.667	-0.010	-0.010	0.000	0.000	0.000	0.000
87	A	136	ASN	0	0.023	-0.022	21.099	-0.015	-0.015	0.000	0.000	0.000	0.000
88	A	137	ASP	-1	-0.769	-0.866	25.306	0.014	0.014	0.000	0.000	0.000	0.000
89	A	138	ALA	0	0.039	0.015	28.877	0.001	0.001	0.000	0.000	0.000	0.000
90	A	139	ILE	0	-0.054	-0.021	23.946	-0.003	-0.003	0.000	0.000	0.000	0.000
91	A	140	VAL	0	0.013	0.004	26.831	0.001	0.001	0.000	0.000	0.000	0.000
92	A	141	ALA	0	0.025	0.020	29.079	0.001	0.001	0.000	0.000	0.000	0.000
93	A	142	PHE	0	-0.030	-0.021	30.351	-0.002	-0.002	0.000	0.000	0.000	0.000
94	A	143	ALA	0	-0.010	-0.011	28.667	-0.001	-0.001	0.000	0.000	0.000	0.000
95	A	144	ARG	1	0.881	0.933	30.806	-0.056	-0.056	0.000	0.000	0.000	0.000
96	A	145	ASN	0	-0.026	0.003	33.653	0.002	0.002	0.000	0.000	0.000	0.000
97	A	146	HIS	1	0.767	0.879	33.802	0.007	0.007	0.000	0.000	0.000	0.000
98	A	147	GLN	0	0.006	0.007	34.157	0.001	0.001	0.000	0.000	0.000	0.000
99	A	148	LEU	0	-0.058	-0.007	29.500	0.000	0.000	0.000	0.000	0.000	0.000
100	A	149	ASN	0	0.015	-0.014	25.374	0.010	0.010	0.000	0.000	0.000	0.000
101	A	150	VAL	0	-0.009	-0.020	23.725	-0.014	-0.014	0.000	0.000	0.000	0.000
102	A	151	VAL	0	0.029	0.027	18.859	0.014	0.014	0.000	0.000	0.000	0.000
103	A	152	ILE	0	-0.036	-0.023	18.225	-0.026	-0.026	0.000	0.000	0.000	0.000
104	A	153	HIS	0	0.044	0.018	15.782	0.038	0.038	0.000	0.000	0.000	0.000
105	A	154	GLN	0	0.093	0.026	12.626	0.070	0.070	0.000	0.000	0.000	0.000
106	A	155	LEU	0	-0.025	-0.010	10.311	0.019	0.019	0.000	0.000	0.000	0.000
107	A	156	ASN	0	-0.035	-0.036	6.089	0.187	0.187	0.000	0.000	0.000	0.000
108	A	157	ALA	0	0.026	0.034	6.839	0.030	0.030	0.000	0.000	0.000	0.000
109	A	158	PRO	0	-0.022	-0.020	9.194	-0.022	-0.022	0.000	0.000	0.000	0.000
110	A	159	LEU	0	-0.038	-0.006	11.339	-0.085	-0.085	0.000	0.000	0.000	0.000
111	A	160	TRP	0	0.029	0.012	13.009	0.098	0.098	0.000	0.000	0.000	0.000
112	A	161	GLN	0	-0.015	-0.025	17.150	-0.017	-0.017	0.000	0.000	0.000	0.000
113	A	162	ILE	0	-0.004	0.016	20.765	0.023	0.023	0.000	0.000	0.000	0.000
114	A	163	ARG	1	0.916	0.943	22.675	-0.136	-0.136	0.000	0.000	0.000	0.000
115	A	164	GLY	0	0.043	0.026	27.077	0.003	0.003	0.000	0.000	0.000	0.000
116	A	165	THR	0	-0.080	-0.051	30.418	-0.004	-0.004	0.000	0.000	0.000	0.000
117	A	166	GLU	-1	-0.865	-0.931	30.410	0.092	0.092	0.000	0.000	0.000	0.000
118	A	167	LYS	1	0.867	0.942	32.105	-0.029	-0.029	0.000	0.000	0.000	0.000
119	A	168	SER	0	0.032	0.017	29.847	0.001	0.001	0.000	0.000	0.000	0.000
120	A	169	SER	0	-0.044	-0.033	29.449	-0.001	-0.001	0.000	0.000	0.000	0.000
121	A	170	VAL	0	-0.018	0.009	29.243	-0.002	-0.002	0.000	0.000	0.000	0.000
122	A	171	ARG	1	0.862	0.941	29.938	0.032	0.032	0.000	0.000	0.000	0.000
123	A	172	GLU	-1	-0.807	-0.895	23.333	0.035	0.035	0.000	0.000	0.000	0.000
124	A	173	LEU	0	-0.060	-0.017	26.315	-0.012	-0.012	0.000	0.000	0.000	0.000
125	A	174	HIS	0	0.024	0.012	20.408	0.018	0.018	0.000	0.000	0.000	0.000
126	A	175	ILE	0	-0.005	-0.002	21.855	-0.012	-0.012	0.000	0.000	0.000	0.000
127	A	176	ALA	0	-0.011	-0.013	18.844	-0.005	-0.005	0.000	0.000	0.000	0.000
128	A	177	TYR	0	-0.023	-0.003	16.680	0.002	0.002	0.000	0.000	0.000	0.000
129	A	178	ARG	1	0.739	0.837	17.212	0.242	0.242	0.000	0.000	0.000	0.000
130	A	179	TYR	0	0.016	0.006	18.609	0.010	0.010	0.000	0.000	0.000	0.000
131	A	180	GLY	0	0.028	0.012	19.820	0.017	0.017	0.000	0.000	0.000	0.000
132	A	181	GLU	-1	-0.863	-0.921	21.501	-0.054	-0.054	0.000	0.000	0.000	0.000
133	A	182	HIS	0	-0.079	-0.053	22.637	0.020	0.020	0.000	0.000	0.000	0.000
134	A	183	TYR	0	0.048	-0.001	21.712	-0.014	-0.014	0.000	0.000	0.000	0.000
135	A	184	ASP	-1	-0.792	-0.861	22.518	-0.194	-0.194	0.000	0.000	0.000	0.000
136	A	185	SER	0	-0.016	-0.036	23.493	0.009	0.009	0.000	0.000	0.000	0.000
137	A	186	VAL	0	0.032	0.019	19.992	-0.023	-0.023	0.000	0.000	0.000	0.000
138	A	187	ARG	1	0.857	0.916	23.105	0.128	0.128	0.000	0.000	0.000	0.000
139	A	188	ARG	1	0.864	0.923	23.269	0.091	0.091	0.000	0.000	0.000	0.000
140	A	189	ILE	0	0.003	0.005	21.158	0.003	0.003	0.000	0.000	0.000	0.000
141	A	190	ASN	0	0.036	0.028	25.219	0.003	0.003	0.000	0.000	0.000	0.000

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