FMO DATABASE

FMODB ID: 4J61N

Calculation Name: 1U61-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1U61

Chain ID: A

ChEMBL ID:

UniProt ID: Q81J58

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	127
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1117071.205198
FMO2-HF: Nuclear repulsion	1067108.819928
FMO2-HF: Total energy	-49962.385271
FMO2-MP2: Total energy	-50111.639367

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:2:ILE)

Summations of interaction energy for fragment #1(A:2:ILE)

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.
-3.612	-1.285	5.482	-1.624	-6.185	-0.004

Interaction energy analysis for fragmet #1(A:2:ILE)

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 : -0.025

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

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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	4	ALA	0	0.030	-0.002	3.054	-0.875	1.321	0.295	-0.752	-1.739	0.000
4	A	5	LYS	1	0.946	0.976	3.576	1.001	1.146	0.019	0.049	-0.213	0.000
5	A	6	GLN	0	-0.025	-0.003	5.884	0.101	0.101	0.000	0.000	0.000	0.000
6	A	7	LEU	0	-0.063	-0.003	2.679	-0.587	0.114	0.392	-0.155	-0.938	0.000
7	A	8	ASN	0	0.004	0.000	5.778	-0.184	-0.184	0.000	0.000	0.000	0.000
8	A	9	SER	0	0.093	-0.005	8.103	-0.085	-0.085	0.000	0.000	0.000	0.000
9	A	10	LEU	0	-0.009	0.027	10.786	-0.043	-0.043	0.000	0.000	0.000	0.000
10	A	11	ALA	0	-0.014	-0.010	6.070	-0.018	-0.018	0.000	0.000	0.000	0.000
11	A	12	LEU	0	-0.007	0.005	5.229	-0.109	-0.109	0.000	0.000	0.000	0.000
12	A	13	ALA	0	0.027	0.011	7.416	-0.075	-0.075	0.000	0.000	0.000	0.000
13	A	14	TYR	0	-0.019	-0.005	7.701	0.003	0.003	0.000	0.000	0.000	0.000
14	A	15	MET	0	-0.046	-0.016	5.382	-0.043	-0.043	0.000	0.000	0.000	0.000
15	A	16	GLY	0	0.046	-0.001	7.927	-0.031	-0.031	0.000	0.000	0.000	0.000
16	A	17	ASP	-1	-0.946	-0.961	10.562	-0.209	-0.209	0.000	0.000	0.000	0.000
17	A	18	ALA	0	0.004	0.004	10.700	0.019	0.019	0.000	0.000	0.000	0.000
18	A	19	VAL	0	-0.046	-0.021	8.913	0.018	0.018	0.000	0.000	0.000	0.000
19	A	20	TYR	0	0.010	-0.016	11.968	0.030	0.030	0.000	0.000	0.000	0.000
20	A	21	GLU	-1	-0.770	-0.866	15.328	-0.172	-0.172	0.000	0.000	0.000	0.000
21	A	22	GLN	0	-0.057	-0.030	13.426	0.011	0.011	0.000	0.000	0.000	0.000
22	A	23	TYR	0	-0.032	-0.033	13.960	0.010	0.010	0.000	0.000	0.000	0.000
23	A	24	ILE	0	-0.005	0.012	18.054	0.033	0.033	0.000	0.000	0.000	0.000
24	A	25	ARG	1	0.770	0.861	20.011	0.207	0.207	0.000	0.000	0.000	0.000
25	A	26	TYR	0	0.000	0.006	20.370	0.018	0.018	0.000	0.000	0.000	0.000
26	A	27	HIS	0	-0.019	-0.028	22.098	0.010	0.010	0.000	0.000	0.000	0.000
27	A	28	LEU	0	-0.036	-0.024	24.173	0.019	0.019	0.000	0.000	0.000	0.000
28	A	29	LEU	0	-0.089	-0.048	24.143	0.015	0.015	0.000	0.000	0.000	0.000
29	A	30	GLN	0	0.006	0.015	25.919	0.013	0.013	0.000	0.000	0.000	0.000
30	A	31	LYS	1	0.917	0.975	27.877	0.137	0.137	0.000	0.000	0.000	0.000
31	A	32	GLY	0	0.000	0.011	29.874	0.010	0.010	0.000	0.000	0.000	0.000
32	A	33	LYS	1	0.900	0.936	31.726	0.102	0.102	0.000	0.000	0.000	0.000
33	A	34	VAL	0	0.008	0.018	31.042	0.004	0.004	0.000	0.000	0.000	0.000
34	A	35	ARG	1	0.975	0.988	33.302	0.068	0.068	0.000	0.000	0.000	0.000
35	A	36	PRO	0	0.082	0.025	30.866	-0.003	-0.003	0.000	0.000	0.000	0.000
36	A	37	ASN	0	-0.008	-0.013	30.450	-0.004	-0.004	0.000	0.000	0.000	0.000
37	A	38	GLN	0	-0.024	-0.024	32.213	0.004	0.004	0.000	0.000	0.000	0.000
38	A	39	LEU	0	0.041	0.039	26.897	-0.002	-0.002	0.000	0.000	0.000	0.000
39	A	40	HIS	0	0.059	0.040	24.816	-0.010	-0.010	0.000	0.000	0.000	0.000
40	A	41	ARG	1	0.962	0.975	26.865	0.084	0.084	0.000	0.000	0.000	0.000
41	A	42	LEU	0	-0.017	-0.022	28.725	0.000	0.000	0.000	0.000	0.000	0.000
42	A	43	GLY	0	0.116	0.064	24.562	-0.005	-0.005	0.000	0.000	0.000	0.000
43	A	44	THR	0	-0.007	0.007	24.229	-0.007	-0.007	0.000	0.000	0.000	0.000
44	A	45	SER	0	-0.131	-0.078	25.848	-0.001	-0.001	0.000	0.000	0.000	0.000
45	A	46	PHE	0	0.038	0.010	22.841	0.001	0.001	0.000	0.000	0.000	0.000
46	A	47	VAL	0	0.024	0.023	19.997	-0.010	-0.010	0.000	0.000	0.000	0.000
47	A	48	SER	0	-0.053	0.002	21.262	0.006	0.006	0.000	0.000	0.000	0.000
48	A	49	ALA	0	0.070	0.014	22.147	-0.007	-0.007	0.000	0.000	0.000	0.000
49	A	50	LYS	1	0.945	0.949	23.194	0.080	0.080	0.000	0.000	0.000	0.000
50	A	51	ALA	0	0.003	0.018	24.152	0.001	0.001	0.000	0.000	0.000	0.000
51	A	52	GLN	0	0.044	0.002	17.898	-0.015	-0.015	0.000	0.000	0.000	0.000
52	A	53	ALA	0	-0.005	-0.003	21.700	-0.007	-0.007	0.000	0.000	0.000	0.000
53	A	54	LYS	1	0.949	0.988	23.475	0.123	0.123	0.000	0.000	0.000	0.000
54	A	55	VAL	0	0.018	0.012	20.937	0.003	0.003	0.000	0.000	0.000	0.000
55	A	56	VAL	0	0.002	-0.003	19.521	-0.003	-0.003	0.000	0.000	0.000	0.000
56	A	57	TYR	0	-0.037	-0.030	22.201	0.004	0.004	0.000	0.000	0.000	0.000
57	A	58	HIS	0	0.062	0.037	25.622	-0.001	-0.001	0.000	0.000	0.000	0.000
58	A	59	LEU	0	-0.032	-0.017	19.802	0.001	0.001	0.000	0.000	0.000	0.000
59	A	60	LEU	0	-0.039	-0.030	21.559	0.000	0.000	0.000	0.000	0.000	0.000
60	A	61	GLU	-1	-1.001	-0.983	24.621	-0.111	-0.111	0.000	0.000	0.000	0.000
61	A	62	THR	0	-0.041	-0.034	26.707	0.001	0.001	0.000	0.000	0.000	0.000
62	A	63	ALA	0	0.007	0.020	25.101	0.000	0.000	0.000	0.000	0.000	0.000
63	A	64	PHE	0	-0.026	-0.013	20.598	-0.007	-0.007	0.000	0.000	0.000	0.000
64	A	65	LEU	0	-0.041	-0.023	17.840	-0.022	-0.022	0.000	0.000	0.000	0.000
65	A	66	THR	0	0.056	0.027	17.385	0.016	0.016	0.000	0.000	0.000	0.000
66	A	67	GLU	-1	-0.870	-0.949	19.035	-0.171	-0.171	0.000	0.000	0.000	0.000
67	A	68	GLU	-1	-0.883	-0.933	12.510	-0.500	-0.500	0.000	0.000	0.000	0.000
68	A	69	GLU	-1	-0.745	-0.849	14.492	-0.418	-0.418	0.000	0.000	0.000	0.000
69	A	70	GLU	-1	-0.872	-0.937	15.561	-0.182	-0.182	0.000	0.000	0.000	0.000
70	A	71	ALA	0	-0.066	-0.031	15.518	0.026	0.026	0.000	0.000	0.000	0.000
71	A	72	VAL	0	-0.022	-0.002	11.105	0.028	0.028	0.000	0.000	0.000	0.000
72	A	73	LEU	0	0.035	0.028	13.458	0.023	0.023	0.000	0.000	0.000	0.000
73	A	74	ARG	1	0.947	0.967	16.287	0.161	0.161	0.000	0.000	0.000	0.000
74	A	75	ARG	1	0.911	0.947	12.553	0.132	0.132	0.000	0.000	0.000	0.000
75	A	76	GLY	0	0.066	0.033	13.889	0.025	0.025	0.000	0.000	0.000	0.000
76	A	77	ARG	1	0.823	0.920	14.744	0.120	0.120	0.000	0.000	0.000	0.000
77	A	78	ASN	0	-0.073	-0.055	16.637	0.008	0.008	0.000	0.000	0.000	0.000
78	A	79	ALA	0	0.026	-0.006	16.411	0.005	0.005	0.000	0.000	0.000	0.000
79	A	80	ASN	0	-0.041	-0.018	17.361	0.035	0.035	0.000	0.000	0.000	0.000
80	A	81	SER	0	0.092	0.055	16.926	-0.003	-0.003	0.000	0.000	0.000	0.000
81	A	82	GLY	0	-0.037	-0.002	18.209	0.010	0.010	0.000	0.000	0.000	0.000
82	A	83	THR	0	-0.040	-0.006	21.544	-0.003	-0.003	0.000	0.000	0.000	0.000
83	A	84	VAL	0	0.006	0.006	21.900	-0.009	-0.009	0.000	0.000	0.000	0.000
84	A	85	PRO	0	0.014	0.014	22.124	0.008	0.008	0.000	0.000	0.000	0.000
85	A	86	LYS	1	1.004	0.987	24.813	0.037	0.037	0.000	0.000	0.000	0.000
86	A	87	ASN	0	-0.038	-0.030	28.614	-0.002	-0.002	0.000	0.000	0.000	0.000
87	A	88	THR	0	-0.010	0.014	24.819	-0.007	-0.007	0.000	0.000	0.000	0.000
88	A	89	ASP	-1	-0.812	-0.904	28.131	-0.069	-0.069	0.000	0.000	0.000	0.000
89	A	90	VAL	0	0.053	0.017	24.909	-0.008	-0.008	0.000	0.000	0.000	0.000
90	A	91	GLN	0	0.046	0.027	24.368	-0.014	-0.014	0.000	0.000	0.000	0.000
91	A	92	THR	0	-0.013	-0.006	24.229	-0.011	-0.011	0.000	0.000	0.000	0.000
92	A	93	TYR	0	0.023	-0.002	18.691	-0.009	-0.009	0.000	0.000	0.000	0.000
93	A	94	ARG	1	0.880	0.948	20.032	0.052	0.052	0.000	0.000	0.000	0.000
94	A	95	HIS	0	0.042	0.016	19.219	-0.017	-0.017	0.000	0.000	0.000	0.000
95	A	96	SER	0	0.015	0.022	19.139	-0.021	-0.021	0.000	0.000	0.000	0.000
96	A	97	THR	0	-0.004	-0.001	15.207	-0.012	-0.012	0.000	0.000	0.000	0.000
97	A	98	ALA	0	-0.042	-0.018	14.648	-0.033	-0.033	0.000	0.000	0.000	0.000
98	A	99	PHE	0	0.026	0.010	14.746	-0.044	-0.044	0.000	0.000	0.000	0.000
99	A	100	GLU	-1	-0.827	-0.906	12.908	-0.283	-0.283	0.000	0.000	0.000	0.000
100	A	101	ALA	0	-0.007	-0.008	10.353	-0.079	-0.079	0.000	0.000	0.000	0.000
101	A	102	LEU	0	-0.009	-0.003	9.909	-0.115	-0.115	0.000	0.000	0.000	0.000
102	A	103	ILE	0	-0.004	0.000	11.185	-0.093	-0.093	0.000	0.000	0.000	0.000
103	A	104	GLY	0	0.005	0.002	7.921	-0.100	-0.100	0.000	0.000	0.000	0.000
104	A	105	TYR	0	-0.102	-0.063	6.500	-0.394	-0.394	0.000	0.000	0.000	0.000
105	A	106	HIS	0	0.046	0.002	7.111	-0.375	-0.375	0.000	0.000	0.000	0.000
106	A	107	HIS	0	-0.007	0.006	5.867	-0.035	-0.035	0.000	0.000	0.000	0.000
107	A	108	LEU	0	-0.042	-0.028	2.081	-0.615	-1.414	4.777	-0.748	-3.230	-0.004
108	A	109	LEU	0	-0.053	-0.017	4.536	-0.918	-0.834	-0.001	-0.018	-0.065	0.000
109	A	110	ASN	0	-0.053	-0.017	6.739	0.346	0.346	0.000	0.000	0.000	0.000
110	A	111	ASN	0	0.002	-0.006	9.139	0.201	0.201	0.000	0.000	0.000	0.000
111	A	112	ARG	1	0.959	0.966	12.169	0.603	0.603	0.000	0.000	0.000	0.000
112	A	113	GLU	-1	-0.918	-0.945	14.194	-0.308	-0.308	0.000	0.000	0.000	0.000
113	A	114	ARG	1	0.846	0.895	15.047	0.380	0.380	0.000	0.000	0.000	0.000
114	A	115	LEU	0	-0.012	-0.013	11.404	0.033	0.033	0.000	0.000	0.000	0.000
115	A	116	ASP	-1	-0.856	-0.928	15.145	-0.373	-0.373	0.000	0.000	0.000	0.000
116	A	117	GLU	-1	-0.918	-0.944	18.313	-0.275	-0.275	0.000	0.000	0.000	0.000
117	A	118	ILE	0	-0.033	-0.017	15.611	0.034	0.034	0.000	0.000	0.000	0.000
118	A	119	VAL	0	0.003	0.007	16.098	0.035	0.035	0.000	0.000	0.000	0.000
119	A	120	TYR	0	-0.004	-0.014	19.023	0.032	0.032	0.000	0.000	0.000	0.000
120	A	121	LYS	1	0.934	0.993	22.030	0.213	0.213	0.000	0.000	0.000	0.000
121	A	122	ALA	0	-0.002	-0.013	20.559	0.021	0.021	0.000	0.000	0.000	0.000
122	A	123	ILE	0	-0.008	-0.014	21.544	0.019	0.019	0.000	0.000	0.000	0.000
123	A	124	ALA	0	-0.008	0.001	24.540	0.016	0.016	0.000	0.000	0.000	0.000
124	A	125	VAL	0	-0.010	-0.002	25.691	0.013	0.013	0.000	0.000	0.000	0.000
125	A	126	LEU	0	-0.110	-0.051	23.709	0.014	0.014	0.000	0.000	0.000	0.000
126	A	127	GLU	-1	-0.897	-0.940	27.775	-0.144	-0.144	0.000	0.000	0.000	0.000
127	A	128	GLU	-1	-1.050	-0.999	30.360	-0.109	-0.109	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:ILE)