FMO DATABASE

FMODB ID: 6N69Z

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1113550.428198
FMO2-HF: Nuclear repulsion	1063103.998417
FMO2-HF: Total energy	-50446.429781
FMO2-MP2: Total energy	-50595.990502

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.
-19.685	-3.347	13.64	-10.524	-19.451	-0.054

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 : -0.011 / q_NPA : 0.012

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	0.007	0.014	3.048	-2.916	0.836	0.226	-1.871	-2.107	0.003
4	A	6	MET	0	-0.016	0.005	4.603	0.194	0.247	-0.001	-0.010	-0.042	0.000
5	A	7	ILE	0	0.028	0.006	8.176	0.028	0.028	0.000	0.000	0.000	0.000
6	A	8	LYS	1	0.960	0.983	11.205	0.352	0.352	0.000	0.000	0.000	0.000
7	A	9	ILE	0	0.019	-0.003	14.795	0.010	0.010	0.000	0.000	0.000	0.000
8	A	10	ASN	0	-0.050	-0.019	17.932	0.009	0.009	0.000	0.000	0.000	0.000
9	A	11	GLU	-1	-0.824	-0.906	20.842	-0.183	-0.183	0.000	0.000	0.000	0.000
10	A	12	ALA	0	-0.041	-0.026	24.167	0.010	0.010	0.000	0.000	0.000	0.000
11	A	13	VAL	0	-0.016	-0.006	26.782	0.000	0.000	0.000	0.000	0.000	0.000
12	A	14	PHE	0	-0.005	-0.016	25.520	0.001	0.001	0.000	0.000	0.000	0.000
13	A	15	TYR	0	-0.027	-0.015	31.521	0.002	0.002	0.000	0.000	0.000	0.000
14	A	16	ASP	-1	-0.840	-0.907	33.849	-0.089	-0.089	0.000	0.000	0.000	0.000
15	A	17	ARG	1	0.791	0.842	33.052	0.085	0.085	0.000	0.000	0.000	0.000
16	A	18	ILE	0	-0.044	-0.001	25.317	0.000	0.000	0.000	0.000	0.000	0.000
17	A	19	THR	0	0.085	0.030	28.476	0.001	0.001	0.000	0.000	0.000	0.000
18	A	20	SER	0	-0.033	-0.023	26.213	-0.015	-0.015	0.000	0.000	0.000	0.000
19	A	21	ASN	0	-0.011	-0.015	22.871	-0.006	-0.006	0.000	0.000	0.000	0.000
20	A	22	LYS	1	0.960	1.009	23.414	0.186	0.186	0.000	0.000	0.000	0.000
21	A	23	ILE	0	0.025	0.003	18.361	-0.007	-0.007	0.000	0.000	0.000	0.000
22	A	24	ILE	0	-0.036	-0.031	19.119	0.018	0.018	0.000	0.000	0.000	0.000
23	A	25	GLY	0	-0.023	-0.019	16.801	-0.004	-0.004	0.000	0.000	0.000	0.000
24	A	26	THR	0	-0.061	-0.032	13.463	0.031	0.031	0.000	0.000	0.000	0.000
25	A	27	GLY	0	0.006	0.008	9.714	-0.030	-0.030	0.000	0.000	0.000	0.000
26	A	28	HIS	0	0.007	0.013	7.831	0.184	0.184	0.000	0.000	0.000	0.000
27	A	29	LEU	0	-0.004	-0.003	3.062	-0.891	-0.389	0.063	-0.105	-0.459	0.000
28	A	30	PHE	0	0.007	0.001	3.353	-0.037	0.412	0.012	-0.121	-0.341	0.000
29	A	31	ASN	0	0.014	-0.005	2.368	-5.867	-3.199	3.206	-2.757	-3.116	-0.028
30	A	32	ARG	1	0.838	0.891	2.163	2.317	4.775	6.179	-2.790	-5.847	-0.019
31	A	33	GLU	-1	-0.910	-0.941	3.753	0.140	0.333	0.023	-0.045	-0.171	0.000
32	A	34	GLY	0	0.056	0.030	7.380	0.320	0.320	0.000	0.000	0.000	0.000
33	A	35	LYS	1	0.807	0.907	2.447	-7.049	-6.076	0.323	-0.374	-0.922	0.003
34	A	36	LYS	1	0.915	0.964	5.834	-0.477	-0.477	0.000	0.000	0.000	0.000
35	A	37	ILE	0	0.007	0.009	3.103	-0.676	-0.025	0.124	-0.141	-0.634	-0.001
36	A	38	LEU	0	0.013	0.018	5.967	0.075	0.075	0.000	0.000	0.000	0.000
37	A	39	ILE	0	0.023	-0.004	5.796	-0.304	-0.304	0.000	0.000	0.000	0.000
38	A	40	SER	0	-0.005	-0.007	8.486	0.140	0.140	0.000	0.000	0.000	0.000
39	A	41	SER	0	-0.015	-0.037	10.295	-0.063	-0.063	0.000	0.000	0.000	0.000
40	A	42	SER	0	0.005	0.000	12.884	0.024	0.024	0.000	0.000	0.000	0.000
41	A	43	LEU	0	-0.037	-0.006	15.207	0.040	0.040	0.000	0.000	0.000	0.000
42	A	44	GLU	-1	-0.791	-0.892	17.994	-0.126	-0.126	0.000	0.000	0.000	0.000
43	A	45	LYS	1	0.913	0.947	16.516	0.171	0.171	0.000	0.000	0.000	0.000
44	A	46	ILE	0	-0.053	-0.017	20.968	0.021	0.021	0.000	0.000	0.000	0.000
45	A	47	LYS	1	0.864	0.911	22.507	0.120	0.120	0.000	0.000	0.000	0.000
46	A	48	ASN	0	-0.007	-0.003	24.260	-0.002	-0.002	0.000	0.000	0.000	0.000
47	A	49	THR	0	-0.019	-0.007	20.608	0.007	0.007	0.000	0.000	0.000	0.000
48	A	50	PRO	0	0.049	0.032	17.198	-0.012	-0.012	0.000	0.000	0.000	0.000
49	A	51	GLY	0	0.057	0.027	14.968	-0.004	-0.004	0.000	0.000	0.000	0.000
50	A	52	ALA	0	-0.015	0.018	15.820	-0.018	-0.018	0.000	0.000	0.000	0.000
51	A	53	TYR	0	-0.011	-0.001	14.371	-0.003	-0.003	0.000	0.000	0.000	0.000
52	A	54	ILE	0	-0.053	-0.016	19.632	0.006	0.006	0.000	0.000	0.000	0.000
53	A	55	ILE	0	0.003	0.009	18.895	-0.005	-0.005	0.000	0.000	0.000	0.000
54	A	56	ARG	1	0.836	0.903	22.479	0.154	0.154	0.000	0.000	0.000	0.000
55	A	57	GLY	0	0.009	0.017	25.009	-0.013	-0.013	0.000	0.000	0.000	0.000
56	A	58	GLN	0	-0.032	-0.027	23.429	-0.007	-0.007	0.000	0.000	0.000	0.000
57	A	59	ASN	0	-0.072	-0.032	27.144	0.012	0.012	0.000	0.000	0.000	0.000
58	A	60	ASN	0	0.039	0.020	30.910	0.006	0.006	0.000	0.000	0.000	0.000
59	A	61	SER	0	0.057	0.028	29.065	-0.002	-0.002	0.000	0.000	0.000	0.000
60	A	62	ALA	0	-0.001	-0.005	29.510	-0.003	-0.003	0.000	0.000	0.000	0.000
61	A	63	HIS	0	-0.080	-0.051	29.762	0.008	0.008	0.000	0.000	0.000	0.000
62	A	64	LYS	1	0.884	0.940	27.042	0.112	0.112	0.000	0.000	0.000	0.000
63	A	65	LEU	0	0.034	0.024	22.415	0.006	0.006	0.000	0.000	0.000	0.000
64	A	66	ARG	1	0.877	0.937	23.189	0.127	0.127	0.000	0.000	0.000	0.000
65	A	67	ILE	0	0.008	-0.010	17.010	0.000	0.000	0.000	0.000	0.000	0.000
66	A	68	ARG	1	0.960	0.969	18.158	0.209	0.209	0.000	0.000	0.000	0.000
67	A	69	ILE	0	-0.012	0.002	11.706	-0.006	-0.006	0.000	0.000	0.000	0.000
68	A	70	GLY	0	0.016	-0.001	13.810	0.032	0.032	0.000	0.000	0.000	0.000
69	A	71	GLY	0	0.007	0.009	13.758	-0.043	-0.043	0.000	0.000	0.000	0.000
70	A	72	GLU	-1	-0.886	-0.952	15.555	-0.202	-0.202	0.000	0.000	0.000	0.000
71	A	73	ASP	-1	-0.891	-0.926	12.743	-0.092	-0.092	0.000	0.000	0.000	0.000
72	A	74	TRP	0	-0.092	-0.037	6.766	-0.013	-0.013	0.000	0.000	0.000	0.000
73	A	75	GLN	0	0.005	-0.003	13.810	0.028	0.028	0.000	0.000	0.000	0.000
74	A	76	PRO	0	0.003	-0.014	14.934	-0.013	-0.013	0.000	0.000	0.000	0.000
75	A	77	ASP	-1	-0.780	-0.856	14.594	-0.036	-0.036	0.000	0.000	0.000	0.000
76	A	78	ASN	0	-0.066	-0.035	16.630	-0.003	-0.003	0.000	0.000	0.000	0.000
77	A	79	SER	0	-0.013	-0.028	16.377	-0.007	-0.007	0.000	0.000	0.000	0.000
78	A	80	GLY	0	0.004	-0.002	18.491	-0.003	-0.003	0.000	0.000	0.000	0.000
79	A	81	ILE	0	-0.008	0.009	12.674	-0.019	-0.019	0.000	0.000	0.000	0.000
80	A	82	GLY	0	-0.022	-0.039	12.333	-0.030	-0.030	0.000	0.000	0.000	0.000
81	A	83	MET	0	-0.076	-0.016	11.402	0.056	0.056	0.000	0.000	0.000	0.000
82	A	84	VAL	0	0.032	0.009	10.037	-0.082	-0.082	0.000	0.000	0.000	0.000
83	A	85	SER	0	0.018	0.025	9.113	0.056	0.056	0.000	0.000	0.000	0.000
84	A	86	HIS	0	0.019	-0.006	9.489	0.045	0.045	0.000	0.000	0.000	0.000
85	A	87	SER	0	0.024	0.015	10.830	0.087	0.087	0.000	0.000	0.000	0.000
86	A	88	ASP	-1	-0.900	-0.959	9.418	0.220	0.220	0.000	0.000	0.000	0.000
87	A	89	PHE	0	0.026	0.026	9.575	0.024	0.024	0.000	0.000	0.000	0.000
88	A	90	THR	0	-0.022	-0.014	8.952	-0.024	-0.024	0.000	0.000	0.000	0.000
89	A	91	ASN	0	-0.027	-0.021	7.925	-0.063	-0.063	0.000	0.000	0.000	0.000
90	A	92	GLU	-1	-0.846	-0.912	8.126	-0.639	-0.639	0.000	0.000	0.000	0.000
91	A	93	PHE	0	-0.019	-0.004	7.292	0.023	0.023	0.000	0.000	0.000	0.000
92	A	94	ASN	0	0.034	-0.004	11.522	-0.024	-0.024	0.000	0.000	0.000	0.000
93	A	95	ILE	0	0.012	0.000	12.660	-0.016	-0.016	0.000	0.000	0.000	0.000
94	A	96	TYR	0	-0.024	-0.014	16.292	0.021	0.021	0.000	0.000	0.000	0.000
95	A	97	PHE	0	0.054	0.027	19.813	-0.010	-0.010	0.000	0.000	0.000	0.000
96	A	98	PHE	0	-0.002	-0.010	22.163	0.006	0.006	0.000	0.000	0.000	0.000
97	A	99	GLY	0	0.009	0.011	24.281	0.008	0.008	0.000	0.000	0.000	0.000
98	A	100	ASN	0	-0.036	-0.021	27.709	-0.002	-0.002	0.000	0.000	0.000	0.000
99	A	101	GLY	0	0.035	0.020	30.343	0.006	0.006	0.000	0.000	0.000	0.000
100	A	102	ASP	-1	-0.794	-0.870	30.224	-0.112	-0.112	0.000	0.000	0.000	0.000
101	A	103	ILE	0	-0.036	-0.005	26.254	-0.003	-0.003	0.000	0.000	0.000	0.000
102	A	104	PRO	0	-0.016	-0.003	29.842	0.002	0.002	0.000	0.000	0.000	0.000
103	A	105	VAL	0	0.019	0.022	30.014	-0.009	-0.009	0.000	0.000	0.000	0.000
104	A	106	ASP	-1	-0.703	-0.827	28.401	-0.149	-0.149	0.000	0.000	0.000	0.000
105	A	107	THR	0	-0.004	-0.020	23.790	-0.004	-0.004	0.000	0.000	0.000	0.000
106	A	108	TYR	0	-0.035	-0.037	22.611	0.008	0.008	0.000	0.000	0.000	0.000
107	A	109	LEU	0	0.021	0.019	18.151	-0.020	-0.020	0.000	0.000	0.000	0.000
108	A	110	ILE	0	0.011	0.005	15.010	0.008	0.008	0.000	0.000	0.000	0.000
109	A	111	SER	0	0.004	0.006	13.612	-0.075	-0.075	0.000	0.000	0.000	0.000
110	A	112	ILE	0	0.011	0.018	9.053	0.059	0.059	0.000	0.000	0.000	0.000
111	A	113	TYR	0	0.017	0.011	7.276	-0.104	-0.104	0.000	0.000	0.000	0.000
112	A	114	ALA	0	0.011	0.010	3.463	-0.237	0.080	0.014	-0.062	-0.269	0.000
113	A	115	THR	0	-0.048	-0.027	3.379	-0.863	-0.088	0.077	-0.380	-0.472	-0.003
114	A	116	GLU	-1	-0.713	-0.848	2.664	2.346	3.776	1.325	-0.922	-1.832	-0.013
115	A	117	ILE	0	-0.077	-0.036	5.220	-0.012	-0.004	-0.001	-0.002	-0.005	0.000
116	A	118	GLU	-1	-0.920	-0.948	8.769	0.426	0.426	0.000	0.000	0.000	0.000
117	A	129	LYS	1	0.854	0.918	2.302	-5.627	-4.470	1.932	-0.698	-2.391	0.004
118	A	130	ALA	0	-0.017	-0.005	3.065	-1.106	-0.317	0.139	-0.233	-0.694	0.000
119	A	131	VAL	0	0.048	0.001	4.457	0.034	0.197	-0.001	-0.013	-0.149	0.000
120	A	132	VAL	0	-0.071	-0.029	7.731	-0.155	-0.155	0.000	0.000	0.000	0.000
121	A	133	GLN	0	0.023	-0.006	10.272	0.133	0.133	0.000	0.000	0.000	0.000
122	A	134	ALA	0	0.024	0.030	13.894	-0.019	-0.019	0.000	0.000	0.000	0.000
123	A	135	ALA	0	0.003	0.006	16.117	0.024	0.024	0.000	0.000	0.000	0.000
124	A	136	VAL	0	0.013	-0.002	19.867	-0.002	-0.002	0.000	0.000	0.000	0.000
125	A	137	THR	0	0.021	0.016	21.548	0.012	0.012	0.000	0.000	0.000	0.000
126	A	138	ILE	0	-0.021	0.012	25.036	-0.001	-0.001	0.000	0.000	0.000	0.000
127	A	139	ALA	0	0.005	-0.010	27.974	0.006	0.006	0.000	0.000	0.000	0.000
128	A	140	ALA	0	0.000	-0.004	31.281	0.000	0.000	0.000	0.000	0.000	0.000
129	A	141	LYS	1	0.895	0.951	29.843	0.151	0.151	0.000	0.000	0.000	0.000
130	A	142	LEU	0	0.026	0.022	36.209	0.002	0.002	0.000	0.000	0.000	0.000
131	A	143	ASN	0	0.027	0.015	37.915	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)