FMO DATABASE

FMODB ID: 6Y55Z

Calculation Name: 4U4I-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4U4I

Chain ID: A

ChEMBL ID:

UniProt ID: G5CS11

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	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	124
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1073116.978408
FMO2-HF: Nuclear repulsion	1022917.474671
FMO2-HF: Total energy	-50199.503737
FMO2-MP2: Total energy	-50341.847035

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:9:PHE)

Summations of interaction energy for fragment #1(A:9:PHE)

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.
-6.703	-1.242	2.092	-1.915	-5.636	0.015

Interaction energy analysis for fragmet #1(A:9:PHE)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.014 / q_NPA : -0.009

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	11	ASN	0	0.004	-0.028	3.820	-0.609	0.772	-0.013	-0.555	-0.812	0.003
4	A	12	VAL	0	-0.007	0.002	2.935	-0.284	0.364	0.179	-0.140	-0.686	0.000
5	A	13	VAL	0	0.012	0.022	5.487	0.130	0.130	0.000	0.000	0.000	0.000
6	A	14	THR	0	0.030	0.006	8.775	-0.068	-0.068	0.000	0.000	0.000	0.000
7	A	15	ALA	0	-0.044	-0.027	10.787	0.070	0.070	0.000	0.000	0.000	0.000
8	A	16	ILE	0	0.015	0.015	14.393	-0.037	-0.037	0.000	0.000	0.000	0.000
9	A	17	CYS	0	-0.034	0.003	17.174	0.036	0.036	0.000	0.000	0.000	0.000
10	A	18	GLN	0	0.029	0.004	20.127	-0.004	-0.004	0.000	0.000	0.000	0.000
11	A	19	LEU	0	-0.025	-0.008	21.767	0.012	0.012	0.000	0.000	0.000	0.000
12	A	20	ASP	-1	-0.804	-0.887	25.224	-0.123	-0.123	0.000	0.000	0.000	0.000
13	A	21	LYS	1	0.888	0.961	28.373	0.098	0.098	0.000	0.000	0.000	0.000
14	A	22	PRO	0	-0.021	-0.030	30.056	-0.006	-0.006	0.000	0.000	0.000	0.000
15	A	23	HIS	0	0.037	0.007	31.834	0.003	0.003	0.000	0.000	0.000	0.000
16	A	24	ASP	-1	-0.802	-0.898	27.793	-0.143	-0.143	0.000	0.000	0.000	0.000
17	A	25	TYR	0	-0.006	0.004	27.196	0.003	0.003	0.000	0.000	0.000	0.000
18	A	26	GLY	0	0.010	0.021	24.187	-0.011	-0.011	0.000	0.000	0.000	0.000
19	A	27	TYR	0	-0.028	-0.028	17.230	-0.004	-0.004	0.000	0.000	0.000	0.000
20	A	28	ALA	0	0.020	0.016	17.157	-0.006	-0.006	0.000	0.000	0.000	0.000
21	A	29	ILE	0	-0.015	-0.011	11.666	0.029	0.029	0.000	0.000	0.000	0.000
22	A	30	PHE	0	0.002	-0.001	12.295	-0.013	-0.013	0.000	0.000	0.000	0.000
23	A	31	THR	0	0.065	0.020	6.136	0.030	0.030	0.000	0.000	0.000	0.000
24	A	32	GLN	0	0.025	0.011	8.019	0.044	0.044	0.000	0.000	0.000	0.000
25	A	33	LEU	0	0.000	0.002	2.592	-1.226	-0.106	0.766	-0.375	-1.510	0.003
26	A	34	PRO	0	-0.017	-0.005	2.938	-3.095	-0.783	1.160	-0.845	-2.628	0.009
27	A	35	ASP	-1	-0.900	-0.946	5.571	-0.844	-0.844	0.000	0.000	0.000	0.000
28	A	36	CYS	0	-0.142	-0.094	7.019	-0.279	-0.279	0.000	0.000	0.000	0.000
29	A	37	THR	0	-0.023	-0.024	8.011	0.113	0.113	0.000	0.000	0.000	0.000
30	A	38	GLU	-1	-0.886	-0.947	7.207	-1.156	-1.156	0.000	0.000	0.000	0.000
31	A	39	ILE	0	-0.030	-0.024	9.609	0.028	0.028	0.000	0.000	0.000	0.000
32	A	40	GLN	0	-0.002	0.000	10.514	-0.024	-0.024	0.000	0.000	0.000	0.000
33	A	41	PHE	0	0.025	-0.002	14.025	0.034	0.034	0.000	0.000	0.000	0.000
34	A	42	HIS	1	0.856	0.932	15.423	0.330	0.330	0.000	0.000	0.000	0.000
35	A	43	LEU	0	0.004	0.015	20.119	0.016	0.016	0.000	0.000	0.000	0.000
36	A	44	LYS	1	0.899	0.941	23.412	0.141	0.141	0.000	0.000	0.000	0.000
37	A	45	ASN	0	-0.034	-0.034	26.895	0.004	0.004	0.000	0.000	0.000	0.000
38	A	46	LEU	0	0.004	0.008	26.237	0.007	0.007	0.000	0.000	0.000	0.000
39	A	47	PRO	0	0.032	0.010	30.236	0.001	0.001	0.000	0.000	0.000	0.000
40	A	48	PRO	0	0.031	0.030	29.906	-0.007	-0.007	0.000	0.000	0.000	0.000
41	A	49	GLY	0	0.001	0.010	29.015	0.007	0.007	0.000	0.000	0.000	0.000
42	A	50	LYS	1	0.919	0.963	26.553	0.116	0.116	0.000	0.000	0.000	0.000
43	A	51	HIS	1	0.803	0.897	26.120	0.131	0.131	0.000	0.000	0.000	0.000
44	A	52	GLY	0	0.086	0.064	25.207	-0.011	-0.011	0.000	0.000	0.000	0.000
45	A	53	CYS	0	-0.078	-0.013	20.641	0.003	0.003	0.000	0.000	0.000	0.000
46	A	54	HIS	1	0.787	0.872	22.767	0.123	0.123	0.000	0.000	0.000	0.000
47	A	55	ILE	0	0.051	0.022	19.066	0.000	0.000	0.000	0.000	0.000	0.000
48	A	56	HIS	1	0.722	0.839	22.956	0.113	0.113	0.000	0.000	0.000	0.000
49	A	57	LYS	1	0.977	0.982	25.167	0.055	0.055	0.000	0.000	0.000	0.000
50	A	58	SER	0	-0.013	0.006	26.334	0.002	0.002	0.000	0.000	0.000	0.000
51	A	59	GLY	0	0.123	0.053	26.537	-0.006	-0.006	0.000	0.000	0.000	0.000
52	A	60	ASP	-1	-0.871	-0.908	27.138	-0.067	-0.067	0.000	0.000	0.000	0.000
53	A	61	ARG	1	0.861	0.905	28.146	0.112	0.112	0.000	0.000	0.000	0.000
54	A	62	ARG	1	0.843	0.893	32.296	0.057	0.057	0.000	0.000	0.000	0.000
55	A	63	ASN	0	-0.018	-0.011	35.760	0.002	0.002	0.000	0.000	0.000	0.000
56	A	64	GLY	0	0.043	0.030	34.094	-0.001	-0.001	0.000	0.000	0.000	0.000
57	A	65	CYS	0	-0.031	-0.030	26.324	0.000	0.000	0.000	0.000	0.000	0.000
58	A	66	THR	0	0.016	0.009	31.966	-0.003	-0.003	0.000	0.000	0.000	0.000
59	A	67	SER	0	0.005	0.020	33.344	0.002	0.002	0.000	0.000	0.000	0.000
60	A	68	MET	0	-0.010	0.031	26.287	0.000	0.000	0.000	0.000	0.000	0.000
61	A	69	GLY	0	-0.002	0.013	29.547	0.000	0.000	0.000	0.000	0.000	0.000
62	A	70	PRO	0	0.022	0.020	30.877	-0.005	-0.005	0.000	0.000	0.000	0.000
63	A	71	HIS	0	0.066	0.026	27.026	-0.003	-0.003	0.000	0.000	0.000	0.000
64	A	72	PHE	0	-0.035	-0.024	20.967	0.009	0.009	0.000	0.000	0.000	0.000
65	A	73	ASN	0	0.061	0.006	24.321	-0.010	-0.010	0.000	0.000	0.000	0.000
66	A	74	PRO	0	-0.008	0.013	22.154	0.005	0.005	0.000	0.000	0.000	0.000
67	A	75	PHE	0	0.017	-0.003	20.059	0.005	0.005	0.000	0.000	0.000	0.000
68	A	76	ASN	0	-0.018	0.017	25.651	0.001	0.001	0.000	0.000	0.000	0.000
69	A	89	LEU	0	0.044	0.017	19.886	0.004	0.004	0.000	0.000	0.000	0.000
70	A	90	GLY	0	-0.048	-0.017	19.970	-0.008	-0.008	0.000	0.000	0.000	0.000
71	A	91	ASP	-1	-0.944	-0.981	21.840	-0.138	-0.138	0.000	0.000	0.000	0.000
72	A	92	LEU	0	-0.022	-0.018	17.388	-0.005	-0.005	0.000	0.000	0.000	0.000
73	A	93	GLY	0	0.068	0.058	19.282	-0.017	-0.017	0.000	0.000	0.000	0.000
74	A	94	ASN	0	-0.058	-0.034	22.008	0.006	0.006	0.000	0.000	0.000	0.000
75	A	95	ILE	0	0.029	0.023	20.055	-0.012	-0.012	0.000	0.000	0.000	0.000
76	A	96	VAL	0	-0.023	-0.034	22.306	0.021	0.021	0.000	0.000	0.000	0.000
77	A	97	VAL	0	-0.049	0.002	23.683	-0.013	-0.013	0.000	0.000	0.000	0.000
78	A	98	ASN	0	0.015	-0.002	24.218	0.013	0.013	0.000	0.000	0.000	0.000
79	A	99	ASN	0	0.018	-0.021	27.597	0.009	0.009	0.000	0.000	0.000	0.000
80	A	100	ASN	0	-0.005	0.008	27.443	0.004	0.004	0.000	0.000	0.000	0.000
81	A	101	GLY	0	0.040	0.021	29.664	0.001	0.001	0.000	0.000	0.000	0.000
82	A	102	GLU	-1	-0.955	-0.981	24.755	-0.176	-0.176	0.000	0.000	0.000	0.000
83	A	103	CYS	0	-0.031	-0.003	21.450	-0.003	-0.003	0.000	0.000	0.000	0.000
84	A	104	ASN	0	-0.035	-0.021	18.996	-0.019	-0.019	0.000	0.000	0.000	0.000
85	A	105	GLU	-1	-0.823	-0.904	17.294	-0.269	-0.269	0.000	0.000	0.000	0.000
86	A	106	ILE	0	0.014	-0.007	10.880	-0.005	-0.005	0.000	0.000	0.000	0.000
87	A	107	ILE	0	0.011	0.027	13.535	0.011	0.011	0.000	0.000	0.000	0.000
88	A	109	VAL	0	-0.001	0.010	11.166	0.035	0.035	0.000	0.000	0.000	0.000
89	A	110	LYS	1	0.978	0.987	11.605	0.275	0.275	0.000	0.000	0.000	0.000
90	A	111	TYR	0	-0.029	-0.019	13.294	-0.006	-0.006	0.000	0.000	0.000	0.000
91	A	112	LEU	0	0.075	0.043	14.003	-0.004	-0.004	0.000	0.000	0.000	0.000
92	A	113	PRO	0	-0.014	0.037	13.069	-0.014	-0.014	0.000	0.000	0.000	0.000
93	A	114	LEU	0	0.052	0.002	10.794	-0.012	-0.012	0.000	0.000	0.000	0.000
94	A	115	THR	0	0.039	0.011	12.489	-0.001	-0.001	0.000	0.000	0.000	0.000
95	A	116	GLY	0	0.031	0.015	14.619	0.019	0.019	0.000	0.000	0.000	0.000
96	A	117	SER	0	-0.001	-0.025	17.000	-0.011	-0.011	0.000	0.000	0.000	0.000
97	A	118	ASN	0	-0.039	-0.025	19.124	-0.007	-0.007	0.000	0.000	0.000	0.000
98	A	119	GLN	0	-0.026	0.021	17.078	-0.015	-0.015	0.000	0.000	0.000	0.000
99	A	120	ILE	0	0.003	-0.014	16.118	0.005	0.005	0.000	0.000	0.000	0.000
100	A	121	ILE	0	0.019	0.018	14.203	-0.008	-0.008	0.000	0.000	0.000	0.000
101	A	122	GLY	0	-0.053	-0.027	18.401	0.017	0.017	0.000	0.000	0.000	0.000
102	A	123	ARG	1	0.811	0.909	21.428	0.092	0.092	0.000	0.000	0.000	0.000
103	A	124	GLY	0	0.011	-0.001	23.067	-0.008	-0.008	0.000	0.000	0.000	0.000
104	A	125	LEU	0	0.007	0.022	19.531	0.002	0.002	0.000	0.000	0.000	0.000
105	A	126	VAL	0	-0.039	-0.043	23.013	0.005	0.005	0.000	0.000	0.000	0.000
106	A	127	ILE	0	0.056	0.023	23.236	-0.005	-0.005	0.000	0.000	0.000	0.000
107	A	128	HIS	0	-0.058	-0.039	26.715	0.009	0.009	0.000	0.000	0.000	0.000
108	A	129	GLU	-1	-0.915	-0.975	29.528	-0.099	-0.099	0.000	0.000	0.000	0.000
109	A	130	LYS	1	1.002	0.973	31.844	0.077	0.077	0.000	0.000	0.000	0.000
110	A	131	GLU	-1	-0.924	-0.958	28.467	-0.114	-0.114	0.000	0.000	0.000	0.000
111	A	132	ASP	-1	-0.807	-0.906	25.645	-0.115	-0.115	0.000	0.000	0.000	0.000
112	A	133	ASP	-1	-0.969	-0.981	28.534	-0.092	-0.092	0.000	0.000	0.000	0.000
113	A	149	GLY	0	0.004	0.011	32.156	0.001	0.001	0.000	0.000	0.000	0.000
114	A	150	ASP	-1	-0.880	-0.926	33.638	-0.072	-0.072	0.000	0.000	0.000	0.000
115	A	151	ARG	1	0.773	0.864	31.011	0.079	0.079	0.000	0.000	0.000	0.000
116	A	152	ILE	0	0.044	0.030	29.727	0.003	0.003	0.000	0.000	0.000	0.000
117	A	153	ALA	0	0.055	0.037	27.383	-0.001	-0.001	0.000	0.000	0.000	0.000
118	A	155	GLY	0	0.067	0.029	24.539	0.003	0.003	0.000	0.000	0.000	0.000
119	A	156	ILE	0	-0.044	-0.026	22.915	0.003	0.003	0.000	0.000	0.000	0.000
120	A	157	ILE	0	-0.015	0.004	17.439	-0.013	-0.013	0.000	0.000	0.000	0.000
121	A	158	ALA	0	0.035	0.019	19.151	0.020	0.020	0.000	0.000	0.000	0.000
122	A	159	TYR	0	0.035	0.007	13.931	-0.023	-0.023	0.000	0.000	0.000	0.000
123	A	160	LEU	0	-0.013	0.008	12.650	0.016	0.016	0.000	0.000	0.000	0.000
124	A	161	ASN	0	0.002	0.004	12.097	0.025	0.025	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:9:PHE)