FMO DATABASE

FMODB ID: 2J26R

Calculation Name: 3UIY-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3UIY

Chain ID: A

ChEMBL ID:

UniProt ID: P12061

Base Structure: X-ray

Registration Date: 2023-06-21

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	131
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1114250.895638
FMO2-HF: Nuclear repulsion	1063805.841097
FMO2-HF: Total energy	-50445.054542
FMO2-MP2: Total energy	-50594.790935

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:3:LEU)

Summations of interaction energy for fragment #1(A:3: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.
-3.412	-43.092	89.644	-22.091	-27.871	-0.013

Interaction energy analysis for fragmet #1(A:3:LEU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.027 / q_NPA : -0.013

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	5	LEU	0	0.018	0.016	3.811	-1.495	0.687	-0.027	-1.012	-1.143	0.003
4	A	6	MET	0	-0.019	0.003	5.560	0.337	0.337	0.000	0.000	0.000	0.000
5	A	7	ILE	0	0.026	0.004	9.258	0.024	0.024	0.000	0.000	0.000	0.000
6	A	8	LYS	1	0.957	0.982	12.288	0.350	0.350	0.000	0.000	0.000	0.000
7	A	9	ILE	0	0.016	-0.005	15.946	0.014	0.014	0.000	0.000	0.000	0.000
8	A	10	ASN	0	-0.061	-0.026	19.014	-0.001	-0.001	0.000	0.000	0.000	0.000
9	A	11	GLU	-1	-0.863	-0.916	22.005	-0.163	-0.163	0.000	0.000	0.000	0.000
10	A	12	ALA	0	-0.028	-0.023	25.295	0.005	0.005	0.000	0.000	0.000	0.000
11	A	13	VAL	0	-0.016	-0.002	27.903	0.004	0.004	0.000	0.000	0.000	0.000
12	A	14	PHE	0	-0.011	-0.019	26.370	-0.001	-0.001	0.000	0.000	0.000	0.000
13	A	15	TYR	0	-0.023	-0.012	32.452	0.004	0.004	0.000	0.000	0.000	0.000
14	A	16	ASP	-1	-0.896	-0.930	34.629	-0.077	-0.077	0.000	0.000	0.000	0.000
15	A	17	ARG	1	0.826	0.871	33.757	0.064	0.064	0.000	0.000	0.000	0.000
16	A	18	ILE	0	-0.024	0.005	26.072	-0.001	-0.001	0.000	0.000	0.000	0.000
17	A	19	THR	0	0.091	0.034	28.773	0.003	0.003	0.000	0.000	0.000	0.000
18	A	20	SER	0	-0.023	-0.020	26.511	-0.013	-0.013	0.000	0.000	0.000	0.000
19	A	21	ASN	0	-0.004	-0.013	23.165	-0.004	-0.004	0.000	0.000	0.000	0.000
20	A	22	LYS	1	0.961	1.012	23.707	0.175	0.175	0.000	0.000	0.000	0.000
21	A	23	ILE	0	0.028	0.003	19.028	-0.001	-0.001	0.000	0.000	0.000	0.000
22	A	24	ILE	0	-0.041	-0.037	19.847	0.014	0.014	0.000	0.000	0.000	0.000
23	A	25	GLY	0	-0.028	-0.024	17.837	0.000	0.000	0.000	0.000	0.000	0.000
24	A	26	THR	0	-0.024	0.003	14.071	0.041	0.041	0.000	0.000	0.000	0.000
25	A	27	GLY	0	-0.003	-0.003	10.579	-0.017	-0.017	0.000	0.000	0.000	0.000
26	A	28	HIS	0	0.021	0.006	8.487	0.197	0.197	0.000	0.000	0.000	0.000
27	A	29	LEU	0	0.002	-0.002	3.485	-0.764	-0.414	0.009	-0.066	-0.293	0.000
28	A	30	PHE	0	-0.017	-0.009	3.773	0.307	0.642	0.000	-0.082	-0.252	0.000
29	A	31	ASN	0	0.013	0.004	2.359	-6.087	-3.514	3.567	-3.015	-3.125	-0.024
30	A	32	ARG	1	0.837	0.914	1.860	15.583	-32.373	78.287	-17.038	-13.293	0.005
31	A	33	GLU	-1	-0.920	-0.944	3.202	2.624	-0.465	0.140	3.456	-0.507	0.008
32	A	34	GLY	0	0.041	0.026	6.837	0.145	0.145	0.000	0.000	0.000	0.000
33	A	35	LYS	1	0.788	0.900	2.259	-4.801	-3.523	0.592	-0.588	-1.282	0.005
34	A	36	LYS	1	0.955	0.983	6.001	-0.211	-0.211	0.000	0.000	0.000	0.000
35	A	37	ILE	0	0.007	0.005	2.852	-0.506	0.239	0.164	-0.188	-0.721	0.000
36	A	38	LEU	0	0.009	0.023	5.851	0.015	0.015	0.000	0.000	0.000	0.000
37	A	39	ILE	0	0.019	0.000	5.822	-0.266	-0.266	0.000	0.000	0.000	0.000
38	A	40	SER	0	-0.014	-0.030	8.643	0.101	0.101	0.000	0.000	0.000	0.000
39	A	41	SER	0	0.006	0.021	10.405	-0.031	-0.031	0.000	0.000	0.000	0.000
40	A	42	SER	0	0.021	0.009	12.859	0.023	0.023	0.000	0.000	0.000	0.000
41	A	43	LEU	0	-0.046	-0.015	14.908	0.021	0.021	0.000	0.000	0.000	0.000
42	A	44	GLU	-1	-0.883	-0.935	17.824	-0.047	-0.047	0.000	0.000	0.000	0.000
43	A	45	LYS	1	0.913	0.951	16.601	0.053	0.053	0.000	0.000	0.000	0.000
44	A	46	ILE	0	-0.046	-0.021	21.190	0.012	0.012	0.000	0.000	0.000	0.000
45	A	47	LYS	1	0.888	0.928	22.697	0.040	0.040	0.000	0.000	0.000	0.000
46	A	48	ASN	0	-0.013	-0.010	24.406	0.001	0.001	0.000	0.000	0.000	0.000
47	A	49	THR	0	-0.004	0.002	20.628	0.002	0.002	0.000	0.000	0.000	0.000
48	A	50	PRO	0	0.047	0.032	17.269	-0.006	-0.006	0.000	0.000	0.000	0.000
49	A	51	GLY	0	0.023	0.014	15.156	-0.011	-0.011	0.000	0.000	0.000	0.000
50	A	52	ALA	0	0.024	0.032	15.990	-0.025	-0.025	0.000	0.000	0.000	0.000
51	A	53	TYR	0	-0.025	0.001	13.905	0.022	0.022	0.000	0.000	0.000	0.000
52	A	54	ILE	0	-0.042	-0.013	19.897	-0.005	-0.005	0.000	0.000	0.000	0.000
53	A	55	ILE	0	0.018	0.013	18.897	0.003	0.003	0.000	0.000	0.000	0.000
54	A	56	ARG	1	0.853	0.905	22.388	0.068	0.068	0.000	0.000	0.000	0.000
55	A	57	GLY	0	0.006	0.011	24.929	-0.008	-0.008	0.000	0.000	0.000	0.000
56	A	58	GLN	0	-0.028	-0.022	23.697	0.002	0.002	0.000	0.000	0.000	0.000
57	A	59	ASN	0	-0.035	0.005	27.206	0.009	0.009	0.000	0.000	0.000	0.000
58	A	60	ASN	0	0.045	0.032	31.031	0.007	0.007	0.000	0.000	0.000	0.000
59	A	61	SER	0	0.071	0.033	28.707	-0.004	-0.004	0.000	0.000	0.000	0.000
60	A	62	ALA	0	0.007	-0.001	29.280	-0.001	-0.001	0.000	0.000	0.000	0.000
61	A	63	HIS	0	-0.091	-0.061	29.806	0.004	0.004	0.000	0.000	0.000	0.000
62	A	64	LYS	1	0.902	0.956	27.000	0.063	0.063	0.000	0.000	0.000	0.000
63	A	65	LEU	0	0.042	0.028	22.651	0.002	0.002	0.000	0.000	0.000	0.000
64	A	66	ARG	1	0.887	0.943	23.337	0.080	0.080	0.000	0.000	0.000	0.000
65	A	67	ILE	0	0.013	-0.004	17.295	-0.007	-0.007	0.000	0.000	0.000	0.000
66	A	68	ARG	1	0.970	0.967	18.450	0.175	0.175	0.000	0.000	0.000	0.000
67	A	69	ILE	0	-0.005	0.007	12.112	-0.011	-0.011	0.000	0.000	0.000	0.000
68	A	70	GLY	0	0.001	-0.008	13.921	0.039	0.039	0.000	0.000	0.000	0.000
69	A	71	GLY	0	-0.019	-0.008	13.932	-0.048	-0.048	0.000	0.000	0.000	0.000
70	A	72	GLU	-1	-0.867	-0.935	15.625	-0.203	-0.203	0.000	0.000	0.000	0.000
71	A	73	ASP	-1	-0.919	-0.935	12.841	-0.127	-0.127	0.000	0.000	0.000	0.000
72	A	74	TRP	0	-0.118	-0.064	6.826	0.011	0.011	0.000	0.000	0.000	0.000
73	A	75	GLN	0	0.007	-0.013	13.663	0.026	0.026	0.000	0.000	0.000	0.000
74	A	76	PRO	0	-0.003	-0.019	14.875	-0.001	-0.001	0.000	0.000	0.000	0.000
75	A	77	ASP	-1	-0.825	-0.909	14.533	0.058	0.058	0.000	0.000	0.000	0.000
76	A	78	ASN	0	-0.053	-0.019	16.592	-0.005	-0.005	0.000	0.000	0.000	0.000
77	A	79	SER	0	0.025	0.016	16.443	-0.009	-0.009	0.000	0.000	0.000	0.000
78	A	80	GLY	0	-0.010	-0.007	18.515	-0.003	-0.003	0.000	0.000	0.000	0.000
79	A	81	ILE	0	0.001	0.009	12.680	-0.014	-0.014	0.000	0.000	0.000	0.000
80	A	82	GLY	0	-0.033	-0.047	12.460	-0.024	-0.024	0.000	0.000	0.000	0.000
81	A	83	MET	0	-0.081	-0.010	11.497	0.036	0.036	0.000	0.000	0.000	0.000
82	A	84	VAL	0	0.045	0.011	9.811	-0.059	-0.059	0.000	0.000	0.000	0.000
83	A	85	SER	0	0.026	0.043	8.634	0.028	0.028	0.000	0.000	0.000	0.000
84	A	86	HIS	0	-0.001	-0.031	9.049	0.086	0.086	0.000	0.000	0.000	0.000
85	A	87	SER	0	0.017	-0.002	10.557	0.080	0.080	0.000	0.000	0.000	0.000
86	A	88	ASP	-1	-0.853	-0.951	8.768	0.175	0.175	0.000	0.000	0.000	0.000
87	A	89	PHE	0	0.011	0.019	9.156	-0.028	-0.028	0.000	0.000	0.000	0.000
88	A	90	THR	0	-0.008	0.013	8.659	-0.043	-0.043	0.000	0.000	0.000	0.000
89	A	91	ASN	0	-0.009	0.013	7.722	-0.010	-0.010	0.000	0.000	0.000	0.000
90	A	92	GLU	-1	-0.853	-0.944	8.261	-0.738	-0.738	0.000	0.000	0.000	0.000
91	A	93	PHE	0	-0.047	-0.009	8.157	0.056	0.056	0.000	0.000	0.000	0.000
92	A	94	ASN	0	0.059	0.005	11.752	-0.053	-0.053	0.000	0.000	0.000	0.000
93	A	95	ILE	0	0.010	-0.003	13.566	0.001	0.001	0.000	0.000	0.000	0.000
94	A	96	TYR	0	-0.035	-0.012	16.737	0.018	0.018	0.000	0.000	0.000	0.000
95	A	97	PHE	0	0.047	0.026	20.211	0.000	0.000	0.000	0.000	0.000	0.000
96	A	98	PHE	0	-0.011	-0.015	22.562	0.004	0.004	0.000	0.000	0.000	0.000
97	A	99	GLY	0	-0.003	-0.005	24.656	0.011	0.011	0.000	0.000	0.000	0.000
98	A	100	ASN	0	-0.041	-0.021	28.117	-0.006	-0.006	0.000	0.000	0.000	0.000
99	A	101	GLY	0	0.043	0.022	30.772	0.005	0.005	0.000	0.000	0.000	0.000
100	A	102	ASP	-1	-0.801	-0.879	30.782	-0.084	-0.084	0.000	0.000	0.000	0.000
101	A	103	ILE	0	-0.031	-0.014	26.973	0.000	0.000	0.000	0.000	0.000	0.000
102	A	104	PRO	0	-0.024	-0.001	30.131	0.001	0.001	0.000	0.000	0.000	0.000
103	A	105	VAL	0	0.029	0.012	30.690	-0.008	-0.008	0.000	0.000	0.000	0.000
104	A	106	ASP	-1	-0.756	-0.863	28.982	-0.091	-0.091	0.000	0.000	0.000	0.000
105	A	107	THR	0	-0.010	-0.016	24.242	-0.012	-0.012	0.000	0.000	0.000	0.000
106	A	108	TYR	0	-0.004	-0.012	23.058	0.013	0.013	0.000	0.000	0.000	0.000
107	A	109	LEU	0	0.028	0.021	18.049	-0.023	-0.023	0.000	0.000	0.000	0.000
108	A	110	ILE	0	-0.002	-0.001	15.750	0.015	0.015	0.000	0.000	0.000	0.000
109	A	111	SER	0	0.007	-0.002	13.314	-0.057	-0.057	0.000	0.000	0.000	0.000
110	A	112	ILE	0	0.020	0.001	9.036	0.034	0.034	0.000	0.000	0.000	0.000
111	A	113	TYR	0	0.004	0.008	6.928	-0.082	-0.082	0.000	0.000	0.000	0.000
112	A	114	ALA	0	-0.015	-0.015	3.889	-0.261	-0.038	0.004	-0.039	-0.187	0.000
113	A	115	THR	0	-0.023	0.000	3.126	-0.926	0.203	0.172	-0.578	-0.723	-0.005
114	A	116	GLU	-1	-0.766	-0.865	2.454	-0.128	1.814	1.544	-1.341	-2.145	-0.021
115	A	117	ILE	0	-0.047	-0.043	5.116	0.004	0.020	-0.001	-0.001	-0.014	0.000
116	A	118	GLU	-1	-0.924	-0.952	8.555	0.527	0.527	0.000	0.000	0.000	0.000
117	A	129	LYS	1	0.853	0.932	2.061	-6.243	-6.717	5.044	-1.281	-3.289	0.014
118	A	130	ALA	0	-0.016	-0.013	2.596	-1.360	-0.451	0.150	-0.308	-0.751	0.002
119	A	131	VAL	0	0.083	0.010	4.481	-0.148	0.009	-0.001	-0.010	-0.146	0.000
120	A	132	VAL	0	-0.093	-0.025	7.720	-0.135	-0.135	0.000	0.000	0.000	0.000
121	A	133	GLN	0	0.025	-0.009	10.612	0.130	0.130	0.000	0.000	0.000	0.000
122	A	134	ALA	0	0.007	0.027	14.325	-0.028	-0.028	0.000	0.000	0.000	0.000
123	A	135	ALA	0	0.006	0.005	16.783	0.026	0.026	0.000	0.000	0.000	0.000
124	A	136	VAL	0	0.011	-0.001	20.528	-0.012	-0.012	0.000	0.000	0.000	0.000
125	A	137	THR	0	0.013	0.004	22.300	0.012	0.012	0.000	0.000	0.000	0.000
126	A	138	ILE	0	-0.030	0.012	25.978	-0.005	-0.005	0.000	0.000	0.000	0.000
127	A	139	ALA	0	-0.002	-0.013	28.778	0.007	0.007	0.000	0.000	0.000	0.000
128	A	140	ALA	0	-0.003	-0.005	32.121	-0.001	-0.001	0.000	0.000	0.000	0.000
129	A	141	LYS	1	0.928	0.966	31.470	0.128	0.128	0.000	0.000	0.000	0.000
130	A	142	LEU	0	0.017	0.015	37.172	0.002	0.002	0.000	0.000	0.000	0.000
131	A	143	ASN	0	0.027	0.013	39.020	0.000	0.000	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:3:LEU)