FMO DATABASE

FMODB ID: 52J3Z

Calculation Name: 5UK3-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 5UK3

Chain ID: A

ChEMBL ID:

UniProt ID: T1KZQ3

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	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	135
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1089532.488327
FMO2-HF: Nuclear repulsion	1035249.674943
FMO2-HF: Total energy	-54282.813384
FMO2-MP2: Total energy	-54439.433001

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:22:ASN)

Summations of interaction energy for fragment #1(A:22:ASN)

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.
-15.597	-8.771	2.364	-3.566	-5.623	0.017

Interaction energy analysis for fragmet #1(A:22:ASN)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.004 / q_NPA : -0.017

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	24	PHE	0	0.036	0.015	2.906	-1.666	1.166	0.252	-1.280	-1.803	0.007
4	A	25	ILE	0	-0.014	-0.009	2.324	-6.224	-3.349	2.101	-2.020	-2.957	0.009
5	A	26	LYS	1	0.892	0.927	3.422	-6.897	-6.231	0.007	-0.178	-0.495	0.001
6	A	27	ALA	0	0.027	0.016	5.462	-0.568	-0.568	0.000	0.000	0.000	0.000
7	A	28	LYS	1	0.870	0.933	6.992	-3.227	-3.227	0.000	0.000	0.000	0.000
8	A	29	GLU	-1	-0.902	-0.935	5.763	5.288	5.288	0.000	0.000	0.000	0.000
9	A	30	SER	0	-0.028	-0.013	9.573	-0.435	-0.435	0.000	0.000	0.000	0.000
10	A	31	LYS	1	0.883	0.947	11.647	-0.866	-0.866	0.000	0.000	0.000	0.000
11	A	32	GLY	0	0.007	0.025	12.806	-0.122	-0.122	0.000	0.000	0.000	0.000
12	A	33	LEU	0	-0.003	0.018	12.135	-0.085	-0.085	0.000	0.000	0.000	0.000
13	A	34	THR	0	-0.010	-0.038	12.111	0.288	0.288	0.000	0.000	0.000	0.000
14	A	35	TYR	0	0.015	-0.030	6.934	-0.039	-0.039	0.000	0.000	0.000	0.000
15	A	36	GLN	0	0.013	0.002	12.991	-0.087	-0.087	0.000	0.000	0.000	0.000
16	A	37	GLN	0	0.076	0.057	16.107	0.026	0.026	0.000	0.000	0.000	0.000
17	A	38	MET	0	0.032	0.021	10.323	0.048	0.048	0.000	0.000	0.000	0.000
18	A	39	ALA	0	0.005	0.007	15.101	-0.086	-0.086	0.000	0.000	0.000	0.000
19	A	40	GLN	0	-0.034	-0.021	16.707	-0.079	-0.079	0.000	0.000	0.000	0.000
20	A	41	LEU	0	-0.007	0.004	17.125	-0.057	-0.057	0.000	0.000	0.000	0.000
21	A	42	LEU	0	-0.019	-0.009	14.204	-0.067	-0.067	0.000	0.000	0.000	0.000
22	A	43	SER	0	-0.025	0.001	18.598	-0.065	-0.065	0.000	0.000	0.000	0.000
23	A	44	VAL	0	-0.006	0.004	15.649	-0.040	-0.040	0.000	0.000	0.000	0.000
24	A	45	ASN	0	0.033	0.009	17.463	0.087	0.087	0.000	0.000	0.000	0.000
25	A	46	LYS	1	0.941	0.960	14.893	-0.775	-0.775	0.000	0.000	0.000	0.000
26	A	47	VAL	0	-0.005	0.008	13.721	0.183	0.183	0.000	0.000	0.000	0.000
27	A	48	TRP	0	0.055	0.028	12.862	0.133	0.133	0.000	0.000	0.000	0.000
28	A	49	LEU	0	0.067	0.056	11.412	0.019	0.019	0.000	0.000	0.000	0.000
29	A	50	THR	0	-0.043	-0.040	9.184	0.255	0.255	0.000	0.000	0.000	0.000
30	A	51	SER	0	-0.042	-0.041	7.957	0.240	0.240	0.000	0.000	0.000	0.000
31	A	52	VAL	0	0.009	0.008	8.441	-0.187	-0.187	0.000	0.000	0.000	0.000
32	A	53	LEU	0	-0.026	-0.004	5.654	-0.114	-0.114	0.000	0.000	0.000	0.000
33	A	54	HIS	0	-0.024	-0.010	3.824	1.443	1.877	0.005	-0.087	-0.352	0.000
34	A	55	GLY	0	0.043	0.042	4.934	-0.976	-0.957	-0.001	-0.001	-0.016	0.000
35	A	56	GLN	0	-0.042	-0.029	6.777	-0.091	-0.091	0.000	0.000	0.000	0.000
36	A	57	ASN	0	-0.019	-0.018	9.791	-0.074	-0.074	0.000	0.000	0.000	0.000
37	A	58	CYS	0	-0.008	0.025	10.408	0.006	0.006	0.000	0.000	0.000	0.000
38	A	59	CYS	0	-0.044	-0.016	12.685	0.093	0.093	0.000	0.000	0.000	0.000
39	A	60	ASP	-1	-0.784	-0.886	14.748	0.094	0.094	0.000	0.000	0.000	0.000
40	A	61	ILE	0	0.089	0.025	15.973	0.048	0.048	0.000	0.000	0.000	0.000
41	A	62	GLN	0	-0.029	-0.012	16.733	0.017	0.017	0.000	0.000	0.000	0.000
42	A	63	LEU	0	-0.028	-0.021	14.779	0.036	0.036	0.000	0.000	0.000	0.000
43	A	64	ALA	0	0.028	0.011	12.549	0.097	0.097	0.000	0.000	0.000	0.000
44	A	65	HIS	0	0.058	0.029	13.014	0.084	0.084	0.000	0.000	0.000	0.000
45	A	66	ARG	1	0.988	1.007	15.328	-0.322	-0.322	0.000	0.000	0.000	0.000
46	A	67	ILE	0	-0.019	0.002	9.737	0.104	0.104	0.000	0.000	0.000	0.000
47	A	68	CYS	0	-0.083	-0.049	11.325	0.123	0.123	0.000	0.000	0.000	0.000
48	A	69	ASP	-1	-0.917	-0.947	12.300	0.323	0.323	0.000	0.000	0.000	0.000
49	A	70	THR	0	-0.071	-0.031	13.679	0.036	0.036	0.000	0.000	0.000	0.000
50	A	71	LEU	0	-0.045	-0.034	8.017	0.143	0.143	0.000	0.000	0.000	0.000
51	A	72	GLY	0	-0.071	-0.042	11.775	-0.131	-0.131	0.000	0.000	0.000	0.000
52	A	73	ILE	0	-0.020	0.005	8.055	-0.090	-0.090	0.000	0.000	0.000	0.000
53	A	74	SER	0	0.072	0.036	11.896	0.060	0.060	0.000	0.000	0.000	0.000
54	A	75	HIS	0	0.048	-0.008	12.463	-0.003	-0.003	0.000	0.000	0.000	0.000
55	A	76	GLU	-1	-0.936	-0.964	13.856	-0.353	-0.353	0.000	0.000	0.000	0.000
56	A	77	TYR	0	-0.027	-0.015	7.776	0.052	0.052	0.000	0.000	0.000	0.000
57	A	78	ALA	0	-0.002	0.002	9.874	-0.038	-0.038	0.000	0.000	0.000	0.000
58	A	79	ASN	0	0.008	-0.010	11.861	0.104	0.104	0.000	0.000	0.000	0.000
59	A	80	GLU	-1	-0.853	-0.932	6.616	-2.132	-2.132	0.000	0.000	0.000	0.000
60	A	81	LEU	0	-0.043	-0.017	6.999	0.027	0.027	0.000	0.000	0.000	0.000
61	A	82	THR	0	-0.006	-0.005	9.704	0.123	0.123	0.000	0.000	0.000	0.000
62	A	83	SER	0	-0.056	-0.003	11.386	0.005	0.005	0.000	0.000	0.000	0.000
63	A	84	ILE	0	0.018	-0.011	12.301	0.034	0.034	0.000	0.000	0.000	0.000
64	A	85	PRO	0	-0.031	0.014	10.329	-0.085	-0.085	0.000	0.000	0.000	0.000
65	A	86	LEU	0	0.006	-0.013	12.286	0.119	0.119	0.000	0.000	0.000	0.000
66	A	87	ARG	1	0.867	0.908	12.115	-0.004	-0.004	0.000	0.000	0.000	0.000
67	A	88	GLY	0	0.000	0.005	12.980	0.018	0.018	0.000	0.000	0.000	0.000
68	A	89	ASN	0	-0.016	-0.011	13.062	0.092	0.092	0.000	0.000	0.000	0.000
69	A	90	GLN	0	-0.002	0.021	7.831	0.132	0.132	0.000	0.000	0.000	0.000
70	A	91	ASN	0	0.014	-0.009	11.839	0.171	0.171	0.000	0.000	0.000	0.000
71	A	92	ILE	0	0.015	-0.005	10.243	0.024	0.024	0.000	0.000	0.000	0.000
72	A	93	ILE	0	0.020	0.012	14.271	0.080	0.080	0.000	0.000	0.000	0.000
73	A	94	ASN	0	0.004	-0.012	17.758	0.017	0.017	0.000	0.000	0.000	0.000
74	A	95	ASP	-1	-0.861	-0.906	14.364	0.852	0.852	0.000	0.000	0.000	0.000
75	A	96	PRO	0	0.024	-0.001	16.870	-0.032	-0.032	0.000	0.000	0.000	0.000
76	A	97	LEU	0	-0.011	0.004	15.770	-0.057	-0.057	0.000	0.000	0.000	0.000
77	A	98	ILE	0	0.032	0.005	14.479	-0.030	-0.030	0.000	0.000	0.000	0.000
78	A	99	TYR	0	-0.042	-0.032	18.231	-0.061	-0.061	0.000	0.000	0.000	0.000
79	A	100	ARG	1	0.933	0.963	21.353	-0.398	-0.398	0.000	0.000	0.000	0.000
80	A	101	PHE	0	0.009	0.005	18.824	-0.027	-0.027	0.000	0.000	0.000	0.000
81	A	102	ASN	0	-0.007	-0.007	19.804	-0.060	-0.060	0.000	0.000	0.000	0.000
82	A	103	GLU	-1	-0.856	-0.897	23.665	0.188	0.188	0.000	0.000	0.000	0.000
83	A	104	LEU	0	0.019	0.005	25.839	-0.021	-0.021	0.000	0.000	0.000	0.000
84	A	105	PHE	0	0.014	-0.004	23.235	-0.015	-0.015	0.000	0.000	0.000	0.000
85	A	106	LYS	1	0.822	0.915	27.951	-0.186	-0.186	0.000	0.000	0.000	0.000
86	A	107	VAL	0	-0.045	-0.017	29.937	-0.014	-0.014	0.000	0.000	0.000	0.000
87	A	108	TYR	0	0.020	0.002	30.642	-0.006	-0.006	0.000	0.000	0.000	0.000
88	A	109	GLY	0	0.031	0.032	30.989	-0.003	-0.003	0.000	0.000	0.000	0.000
89	A	110	SER	0	-0.020	-0.023	31.726	-0.002	-0.002	0.000	0.000	0.000	0.000
90	A	111	SER	0	0.025	0.009	35.062	-0.006	-0.006	0.000	0.000	0.000	0.000
91	A	112	LEU	0	0.012	0.003	29.496	-0.001	-0.001	0.000	0.000	0.000	0.000
92	A	113	ARG	1	0.880	0.951	33.597	-0.077	-0.077	0.000	0.000	0.000	0.000
93	A	114	GLY	0	-0.006	-0.009	34.810	-0.006	-0.006	0.000	0.000	0.000	0.000
94	A	115	ILE	0	0.045	0.024	35.977	-0.003	-0.003	0.000	0.000	0.000	0.000
95	A	116	ILE	0	0.004	0.008	31.368	-0.002	-0.002	0.000	0.000	0.000	0.000
96	A	117	HIS	0	-0.050	-0.037	35.844	-0.008	-0.008	0.000	0.000	0.000	0.000
97	A	118	GLU	-1	-0.975	-0.974	38.588	0.090	0.090	0.000	0.000	0.000	0.000
98	A	119	GLU	-1	-0.947	-0.975	37.520	0.134	0.134	0.000	0.000	0.000	0.000
99	A	120	PHE	0	-0.086	-0.038	34.080	0.003	0.003	0.000	0.000	0.000	0.000
100	A	121	GLY	0	0.018	0.023	38.184	-0.007	-0.007	0.000	0.000	0.000	0.000
101	A	122	ASP	-1	-0.933	-0.980	37.870	0.058	0.058	0.000	0.000	0.000	0.000
102	A	123	GLY	0	0.000	-0.024	35.065	-0.006	-0.006	0.000	0.000	0.000	0.000
103	A	124	ILE	0	-0.052	-0.002	28.528	0.002	0.002	0.000	0.000	0.000	0.000
104	A	125	MET	0	0.034	0.026	24.935	0.006	0.006	0.000	0.000	0.000	0.000
105	A	126	SER	0	-0.012	-0.011	25.473	0.000	0.000	0.000	0.000	0.000	0.000
106	A	127	ALA	0	0.039	0.008	21.039	0.022	0.022	0.000	0.000	0.000	0.000
107	A	128	ILE	0	-0.046	-0.018	20.431	0.015	0.015	0.000	0.000	0.000	0.000
108	A	129	ASP	-1	-0.889	-0.931	21.189	0.180	0.180	0.000	0.000	0.000	0.000
109	A	130	CYS	0	-0.016	-0.023	20.933	0.007	0.007	0.000	0.000	0.000	0.000
110	A	131	LYS	1	0.854	0.932	20.451	-0.227	-0.227	0.000	0.000	0.000	0.000
111	A	132	ILE	0	0.021	0.009	17.763	-0.006	-0.006	0.000	0.000	0.000	0.000
112	A	133	ASP	-1	-0.854	-0.920	19.512	0.531	0.531	0.000	0.000	0.000	0.000
113	A	134	VAL	0	-0.030	-0.021	17.059	-0.017	-0.017	0.000	0.000	0.000	0.000
114	A	135	THR	0	-0.007	-0.008	20.122	0.077	0.077	0.000	0.000	0.000	0.000
115	A	136	LYS	1	0.949	0.996	22.264	-0.596	-0.596	0.000	0.000	0.000	0.000
116	A	137	ASN	0	0.032	0.010	23.875	0.016	0.016	0.000	0.000	0.000	0.000
117	A	138	GLU	-1	-0.820	-0.907	27.579	0.356	0.356	0.000	0.000	0.000	0.000
118	A	139	GLN	0	0.022	-0.003	30.300	-0.001	-0.001	0.000	0.000	0.000	0.000
119	A	140	SER	0	-0.089	-0.053	26.209	0.005	0.005	0.000	0.000	0.000	0.000
120	A	141	ARG	1	0.955	0.990	26.682	-0.312	-0.312	0.000	0.000	0.000	0.000
121	A	142	VAL	0	-0.020	-0.010	21.422	0.023	0.023	0.000	0.000	0.000	0.000
122	A	143	ILE	0	-0.008	-0.006	23.925	-0.036	-0.036	0.000	0.000	0.000	0.000
123	A	144	LEU	0	-0.008	-0.008	19.701	0.042	0.042	0.000	0.000	0.000	0.000
124	A	145	ARG	1	0.895	0.940	22.831	-0.339	-0.339	0.000	0.000	0.000	0.000
125	A	146	ILE	0	0.018	-0.009	21.910	0.032	0.032	0.000	0.000	0.000	0.000
126	A	147	ASP	-1	-0.830	-0.879	23.883	0.226	0.226	0.000	0.000	0.000	0.000
127	A	148	GLY	0	0.055	0.014	24.961	0.008	0.008	0.000	0.000	0.000	0.000
128	A	149	LYS	1	0.875	0.936	26.412	-0.131	-0.131	0.000	0.000	0.000	0.000
129	A	150	PHE	0	0.060	0.040	28.968	-0.001	-0.001	0.000	0.000	0.000	0.000
130	A	151	LEU	0	-0.063	-0.035	28.594	-0.006	-0.006	0.000	0.000	0.000	0.000
131	A	152	PRO	0	-0.001	0.002	32.715	-0.002	-0.002	0.000	0.000	0.000	0.000
132	A	153	TYR	0	0.050	0.021	33.879	-0.009	-0.009	0.000	0.000	0.000	0.000
133	A	154	TYR	0	-0.023	-0.014	37.142	0.002	0.002	0.000	0.000	0.000	0.000
134	A	155	LYS	1	0.931	0.950	39.329	-0.046	-0.046	0.000	0.000	0.000	0.000
135	A	156	GLY	0	-0.003	0.026	42.942	-0.002	-0.002	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:22:ASN)