FMO DATABASE

FMODB ID: ZV99N

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1074356.622621
FMO2-HF: Nuclear repulsion	1024156.576448
FMO2-HF: Total energy	-50200.046173
FMO2-MP2: Total energy	-50342.405274

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.
-7.063	-1.432	3.279	-2.263	-6.647	0.02

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 : 0.009 / 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	11	ASN	0	-0.013	-0.030	3.820	-0.549	0.827	-0.012	-0.539	-0.825	0.003
4	A	12	VAL	0	-0.004	-0.002	2.876	-0.338	0.375	0.280	-0.180	-0.812	0.000
5	A	13	VAL	0	0.025	0.031	5.445	0.120	0.120	0.000	0.000	0.000	0.000
6	A	14	THR	0	0.038	0.007	8.750	-0.035	-0.035	0.000	0.000	0.000	0.000
7	A	15	ALA	0	-0.042	-0.031	10.751	0.064	0.064	0.000	0.000	0.000	0.000
8	A	16	ILE	0	0.007	0.016	14.371	-0.036	-0.036	0.000	0.000	0.000	0.000
9	A	17	CYS	0	-0.077	-0.020	17.109	0.036	0.036	0.000	0.000	0.000	0.000
10	A	18	GLN	0	0.040	0.011	20.079	-0.010	-0.010	0.000	0.000	0.000	0.000
11	A	19	LEU	0	-0.018	-0.010	21.690	0.013	0.013	0.000	0.000	0.000	0.000
12	A	20	ASP	-1	-0.803	-0.868	25.176	-0.117	-0.117	0.000	0.000	0.000	0.000
13	A	21	LYS	1	0.900	0.970	28.313	0.100	0.100	0.000	0.000	0.000	0.000
14	A	22	PRO	0	-0.003	-0.023	30.021	-0.005	-0.005	0.000	0.000	0.000	0.000
15	A	23	HIS	0	0.051	0.022	31.808	0.002	0.002	0.000	0.000	0.000	0.000
16	A	24	ASP	-1	-0.797	-0.880	27.802	-0.144	-0.144	0.000	0.000	0.000	0.000
17	A	25	TYR	0	-0.003	-0.010	27.226	0.003	0.003	0.000	0.000	0.000	0.000
18	A	26	GLY	0	0.007	0.022	24.113	-0.010	-0.010	0.000	0.000	0.000	0.000
19	A	27	TYR	0	-0.026	-0.027	17.163	-0.003	-0.003	0.000	0.000	0.000	0.000
20	A	28	ALA	0	0.018	0.016	17.212	-0.005	-0.005	0.000	0.000	0.000	0.000
21	A	29	ILE	0	-0.009	-0.010	11.602	0.023	0.023	0.000	0.000	0.000	0.000
22	A	30	PHE	0	0.014	0.003	12.288	-0.007	-0.007	0.000	0.000	0.000	0.000
23	A	31	THR	0	0.032	0.006	6.045	-0.001	-0.001	0.000	0.000	0.000	0.000
24	A	32	GLN	0	0.037	0.013	7.924	0.076	0.076	0.000	0.000	0.000	0.000
25	A	33	LEU	0	0.005	0.006	2.636	-1.455	-0.056	0.710	-0.482	-1.627	0.005
26	A	34	PRO	0	-0.001	0.000	2.692	-3.371	-1.228	2.301	-1.062	-3.383	0.012
27	A	35	ASP	-1	-0.863	-0.935	5.316	-0.684	-0.684	0.000	0.000	0.000	0.000
28	A	36	CYS	0	-0.124	-0.081	6.999	-0.349	-0.349	0.000	0.000	0.000	0.000
29	A	37	THR	0	-0.017	-0.014	7.924	0.175	0.175	0.000	0.000	0.000	0.000
30	A	38	GLU	-1	-0.842	-0.907	7.363	-1.100	-1.100	0.000	0.000	0.000	0.000
31	A	39	ILE	0	-0.027	-0.025	9.435	0.011	0.011	0.000	0.000	0.000	0.000
32	A	40	GLN	0	-0.038	-0.029	9.725	0.089	0.089	0.000	0.000	0.000	0.000
33	A	41	PHE	0	0.019	-0.005	13.959	0.028	0.028	0.000	0.000	0.000	0.000
34	A	42	HIS	1	0.850	0.924	15.090	0.339	0.339	0.000	0.000	0.000	0.000
35	A	43	LEU	0	0.000	0.011	20.051	0.015	0.015	0.000	0.000	0.000	0.000
36	A	44	LYS	1	0.868	0.912	23.357	0.144	0.144	0.000	0.000	0.000	0.000
37	A	45	ASN	0	-0.036	-0.036	26.832	0.004	0.004	0.000	0.000	0.000	0.000
38	A	46	LEU	0	0.009	0.015	26.013	0.007	0.007	0.000	0.000	0.000	0.000
39	A	47	PRO	0	0.027	0.006	30.046	0.000	0.000	0.000	0.000	0.000	0.000
40	A	48	PRO	0	0.019	0.019	29.715	-0.005	-0.005	0.000	0.000	0.000	0.000
41	A	49	GLY	0	0.001	0.010	28.837	0.007	0.007	0.000	0.000	0.000	0.000
42	A	50	LYS	1	0.789	0.873	25.756	0.095	0.095	0.000	0.000	0.000	0.000
43	A	51	HIS	1	0.794	0.904	25.957	0.117	0.117	0.000	0.000	0.000	0.000
44	A	52	GLY	0	0.090	0.061	25.047	-0.010	-0.010	0.000	0.000	0.000	0.000
45	A	53	CYS	0	-0.078	-0.014	20.629	0.000	0.000	0.000	0.000	0.000	0.000
46	A	54	HIS	1	0.790	0.872	22.624	0.104	0.104	0.000	0.000	0.000	0.000
47	A	55	ILE	0	0.050	0.023	18.933	-0.002	-0.002	0.000	0.000	0.000	0.000
48	A	56	HIS	1	0.745	0.858	22.984	0.097	0.097	0.000	0.000	0.000	0.000
49	A	57	LYS	1	0.968	0.980	25.158	0.042	0.042	0.000	0.000	0.000	0.000
50	A	58	SER	0	0.003	0.005	26.320	0.001	0.001	0.000	0.000	0.000	0.000
51	A	59	GLY	0	0.116	0.048	26.517	-0.005	-0.005	0.000	0.000	0.000	0.000
52	A	60	ASP	-1	-0.872	-0.911	27.119	-0.064	-0.064	0.000	0.000	0.000	0.000
53	A	61	ARG	1	0.828	0.869	28.134	0.109	0.109	0.000	0.000	0.000	0.000
54	A	62	ARG	1	0.852	0.901	32.278	0.054	0.054	0.000	0.000	0.000	0.000
55	A	63	ASN	0	-0.006	0.007	35.783	0.002	0.002	0.000	0.000	0.000	0.000
56	A	64	GLY	0	0.052	0.032	34.068	0.000	0.000	0.000	0.000	0.000	0.000
57	A	65	CYS	0	-0.031	-0.030	26.307	0.002	0.002	0.000	0.000	0.000	0.000
58	A	66	THR	0	0.015	0.009	31.971	-0.002	-0.002	0.000	0.000	0.000	0.000
59	A	67	SER	0	0.018	0.019	33.557	0.003	0.003	0.000	0.000	0.000	0.000
60	A	68	MET	0	-0.033	0.024	26.243	0.000	0.000	0.000	0.000	0.000	0.000
61	A	69	GLY	0	-0.008	0.012	29.538	0.001	0.001	0.000	0.000	0.000	0.000
62	A	70	PRO	0	0.017	0.010	30.820	-0.005	-0.005	0.000	0.000	0.000	0.000
63	A	71	HIS	0	0.071	0.028	26.953	-0.002	-0.002	0.000	0.000	0.000	0.000
64	A	72	PHE	0	-0.038	-0.022	20.781	0.007	0.007	0.000	0.000	0.000	0.000
65	A	73	ASN	0	0.049	0.005	24.273	-0.006	-0.006	0.000	0.000	0.000	0.000
66	A	74	PRO	0	-0.009	0.005	22.200	0.004	0.004	0.000	0.000	0.000	0.000
67	A	75	PHE	0	0.015	-0.003	19.850	0.004	0.004	0.000	0.000	0.000	0.000
68	A	76	ASN	0	-0.012	0.020	25.654	0.000	0.000	0.000	0.000	0.000	0.000
69	A	89	LEU	0	0.015	-0.012	19.396	0.000	0.000	0.000	0.000	0.000	0.000
70	A	90	GLY	0	0.004	0.020	19.885	-0.004	-0.004	0.000	0.000	0.000	0.000
71	A	91	ASP	-1	-0.926	-0.968	21.735	-0.111	-0.111	0.000	0.000	0.000	0.000
72	A	92	LEU	0	-0.028	-0.021	17.063	-0.001	-0.001	0.000	0.000	0.000	0.000
73	A	93	GLY	0	0.049	0.042	19.157	-0.014	-0.014	0.000	0.000	0.000	0.000
74	A	94	ASN	0	-0.037	-0.031	21.886	0.002	0.002	0.000	0.000	0.000	0.000
75	A	95	ILE	0	0.002	0.016	19.755	-0.011	-0.011	0.000	0.000	0.000	0.000
76	A	96	VAL	0	-0.016	-0.038	22.147	0.019	0.019	0.000	0.000	0.000	0.000
77	A	97	VAL	0	-0.061	-0.003	23.503	-0.014	-0.014	0.000	0.000	0.000	0.000
78	A	98	ASN	0	-0.010	-0.021	23.544	0.014	0.014	0.000	0.000	0.000	0.000
79	A	99	ASN	0	0.036	-0.011	27.411	0.008	0.008	0.000	0.000	0.000	0.000
80	A	100	ASN	0	-0.044	-0.026	27.397	0.005	0.005	0.000	0.000	0.000	0.000
81	A	101	GLY	0	0.033	0.023	29.460	0.000	0.000	0.000	0.000	0.000	0.000
82	A	102	GLU	-1	-0.878	-0.932	24.450	-0.181	-0.181	0.000	0.000	0.000	0.000
83	A	103	CYS	0	-0.049	-0.009	21.289	-0.001	-0.001	0.000	0.000	0.000	0.000
84	A	104	ASN	0	-0.020	-0.013	18.888	-0.024	-0.024	0.000	0.000	0.000	0.000
85	A	105	GLU	-1	-0.805	-0.886	17.292	-0.243	-0.243	0.000	0.000	0.000	0.000
86	A	106	ILE	0	0.006	-0.016	10.714	-0.012	-0.012	0.000	0.000	0.000	0.000
87	A	107	ILE	0	0.017	0.030	13.362	0.013	0.013	0.000	0.000	0.000	0.000
88	A	109	VAL	0	0.014	0.017	11.045	0.026	0.026	0.000	0.000	0.000	0.000
89	A	110	LYS	1	0.885	0.940	9.622	0.126	0.126	0.000	0.000	0.000	0.000
90	A	111	TYR	0	-0.035	-0.024	12.977	-0.018	-0.018	0.000	0.000	0.000	0.000
91	A	112	LEU	0	0.072	0.044	13.939	-0.017	-0.017	0.000	0.000	0.000	0.000
92	A	113	PRO	0	-0.013	0.031	13.060	-0.005	-0.005	0.000	0.000	0.000	0.000
93	A	114	LEU	0	0.061	0.009	10.838	-0.024	-0.024	0.000	0.000	0.000	0.000
94	A	115	THR	0	0.037	0.014	12.509	-0.017	-0.017	0.000	0.000	0.000	0.000
95	A	116	GLY	0	0.017	0.006	14.595	0.025	0.025	0.000	0.000	0.000	0.000
96	A	117	SER	0	0.015	-0.016	16.978	-0.010	-0.010	0.000	0.000	0.000	0.000
97	A	118	ASN	0	-0.043	-0.023	19.134	-0.010	-0.010	0.000	0.000	0.000	0.000
98	A	119	GLN	0	-0.046	0.011	17.047	0.000	0.000	0.000	0.000	0.000	0.000
99	A	120	ILE	0	0.016	-0.010	16.115	0.001	0.001	0.000	0.000	0.000	0.000
100	A	121	ILE	0	0.013	0.018	14.096	-0.009	-0.009	0.000	0.000	0.000	0.000
101	A	122	GLY	0	-0.047	-0.023	18.380	0.017	0.017	0.000	0.000	0.000	0.000
102	A	123	ARG	1	0.818	0.917	21.411	0.075	0.075	0.000	0.000	0.000	0.000
103	A	124	GLY	0	0.010	-0.004	23.051	-0.010	-0.010	0.000	0.000	0.000	0.000
104	A	125	LEU	0	0.012	0.026	19.453	0.004	0.004	0.000	0.000	0.000	0.000
105	A	126	VAL	0	-0.053	-0.051	23.017	0.003	0.003	0.000	0.000	0.000	0.000
106	A	127	ILE	0	0.061	0.025	23.024	-0.003	-0.003	0.000	0.000	0.000	0.000
107	A	128	HIS	0	-0.077	-0.051	26.546	0.008	0.008	0.000	0.000	0.000	0.000
108	A	129	GLU	-1	-0.870	-0.959	29.358	-0.091	-0.091	0.000	0.000	0.000	0.000
109	A	130	LYS	1	0.935	0.950	31.676	0.067	0.067	0.000	0.000	0.000	0.000
110	A	131	GLU	-1	-0.783	-0.867	28.370	-0.101	-0.101	0.000	0.000	0.000	0.000
111	A	132	ASP	-1	-0.834	-0.913	25.726	-0.094	-0.094	0.000	0.000	0.000	0.000
112	A	133	ASP	-1	-0.958	-0.969	28.419	-0.075	-0.075	0.000	0.000	0.000	0.000
113	A	149	GLY	0	0.014	0.015	32.099	0.001	0.001	0.000	0.000	0.000	0.000
114	A	150	ASP	-1	-0.871	-0.925	33.482	-0.065	-0.065	0.000	0.000	0.000	0.000
115	A	151	ARG	1	0.788	0.878	31.145	0.069	0.069	0.000	0.000	0.000	0.000
116	A	152	ILE	0	0.038	0.025	29.659	0.002	0.002	0.000	0.000	0.000	0.000
117	A	153	ALA	0	0.054	0.036	27.392	-0.002	-0.002	0.000	0.000	0.000	0.000
118	A	155	GLY	0	0.077	0.030	24.500	0.001	0.001	0.000	0.000	0.000	0.000
119	A	156	ILE	0	-0.034	-0.022	22.893	0.004	0.004	0.000	0.000	0.000	0.000
120	A	157	ILE	0	-0.017	0.011	17.524	-0.015	-0.015	0.000	0.000	0.000	0.000
121	A	158	ALA	0	0.027	0.018	19.106	0.020	0.020	0.000	0.000	0.000	0.000
122	A	159	TYR	0	0.039	0.006	13.898	-0.020	-0.020	0.000	0.000	0.000	0.000
123	A	160	LEU	0	-0.011	0.009	12.479	0.015	0.015	0.000	0.000	0.000	0.000
124	A	161	ASN	0	0.006	0.007	11.833	0.036	0.036	0.000	0.000	0.000	0.000

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