FMO DATABASE

FMODB ID: 5JR6Z

Calculation Name: 5AN3-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 5AN3

Chain ID: A

ChEMBL ID:

UniProt ID: Q08446

Base Structure: X-ray

Registration Date: 2023-09-22

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	132
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1235732.405744
FMO2-HF: Nuclear repulsion	1182540.101594
FMO2-HF: Total energy	-53192.30415
FMO2-MP2: Total energy	-53349.724072

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:VAL)

Summations of interaction energy for fragment #1(A:3:VAL)

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.
-18.064	-14.529	12.616	-6.651	-9.501	-0.053

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.032 / q_NPA : 0.001

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	5	LYS	1	0.954	0.972	3.287	-1.685	-0.237	0.001	-0.593	-0.856	0.002
4	A	6	ASP	-1	-0.801	-0.902	1.939	-14.482	-15.297	9.715	-4.497	-4.403	-0.052
5	A	7	LEU	0	0.007	-0.007	2.599	0.437	1.444	0.716	-0.400	-1.323	0.001
6	A	8	LYS	1	0.789	0.890	5.459	0.324	0.324	0.000	0.000	0.000	0.000
7	A	9	THR	0	-0.050	-0.036	7.346	0.159	0.159	0.000	0.000	0.000	0.000
8	A	10	ALA	0	0.019	0.018	8.090	0.176	0.176	0.000	0.000	0.000	0.000
9	A	11	TYR	0	0.010	0.005	9.566	0.153	0.153	0.000	0.000	0.000	0.000
10	A	12	LYS	1	0.858	0.914	11.326	0.312	0.312	0.000	0.000	0.000	0.000
11	A	13	ALA	0	0.081	0.055	12.865	0.060	0.060	0.000	0.000	0.000	0.000
12	A	14	LEU	0	0.008	0.008	13.854	0.055	0.055	0.000	0.000	0.000	0.000
13	A	15	TYR	0	-0.044	-0.035	13.613	0.054	0.054	0.000	0.000	0.000	0.000
14	A	16	ASP	-1	-0.828	-0.878	16.646	-0.139	-0.139	0.000	0.000	0.000	0.000
15	A	17	GLU	-1	-0.901	-0.965	15.334	-0.385	-0.385	0.000	0.000	0.000	0.000
16	A	18	LYS	1	0.758	0.880	18.744	0.156	0.156	0.000	0.000	0.000	0.000
17	A	19	GLU	-1	-0.783	-0.880	17.994	-0.291	-0.291	0.000	0.000	0.000	0.000
18	A	20	PRO	0	0.001	-0.015	16.786	-0.045	-0.045	0.000	0.000	0.000	0.000
19	A	21	LEU	0	0.046	0.028	16.423	-0.030	-0.030	0.000	0.000	0.000	0.000
20	A	22	LYS	1	0.797	0.896	14.313	0.337	0.337	0.000	0.000	0.000	0.000
21	A	23	ALA	0	0.003	-0.015	12.538	-0.084	-0.084	0.000	0.000	0.000	0.000
22	A	24	LEU	0	0.003	0.008	11.561	-0.078	-0.078	0.000	0.000	0.000	0.000
23	A	25	HIS	0	0.024	0.023	12.128	0.006	0.006	0.000	0.000	0.000	0.000
24	A	26	LEU	0	-0.009	-0.007	8.965	-0.092	-0.092	0.000	0.000	0.000	0.000
25	A	27	TYR	0	0.013	-0.017	7.088	-0.235	-0.235	0.000	0.000	0.000	0.000
26	A	28	ASP	-1	-0.794	-0.882	7.867	-0.439	-0.439	0.000	0.000	0.000	0.000
27	A	29	GLU	-1	-0.842	-0.909	8.475	-0.805	-0.805	0.000	0.000	0.000	0.000
28	A	30	ILE	0	-0.043	-0.015	2.496	-0.767	-0.146	0.430	-0.187	-0.865	-0.001
29	A	31	LEU	0	-0.057	-0.037	5.177	0.023	0.118	-0.001	-0.002	-0.092	0.000
30	A	32	LYS	1	0.825	0.917	7.375	0.793	0.793	0.000	0.000	0.000	0.000
31	A	33	GLY	0	0.005	0.016	5.357	0.128	0.128	0.000	0.000	0.000	0.000
32	A	34	SER	0	-0.064	-0.045	3.023	-1.092	0.050	0.221	-0.525	-0.838	-0.004
33	A	35	PRO	0	0.063	0.031	5.426	0.161	0.161	0.000	0.000	0.000	0.000
34	A	36	THR	0	-0.013	-0.008	7.907	0.017	0.017	0.000	0.000	0.000	0.000
35	A	37	ASN	0	0.049	0.024	2.272	-0.518	-0.481	1.534	-0.447	-1.124	0.001
36	A	38	LEU	0	0.094	0.031	5.831	-0.117	-0.117	0.000	0.000	0.000	0.000
37	A	39	THR	0	-0.025	-0.015	5.584	-0.079	-0.079	0.000	0.000	0.000	0.000
38	A	40	ALA	0	0.035	0.017	5.116	-0.137	-0.137	0.000	0.000	0.000	0.000
39	A	41	LEU	0	0.008	0.012	7.204	-0.071	-0.071	0.000	0.000	0.000	0.000
40	A	42	ILE	0	-0.017	-0.007	10.435	-0.020	-0.020	0.000	0.000	0.000	0.000
41	A	43	PHE	0	-0.001	-0.019	9.442	-0.005	-0.005	0.000	0.000	0.000	0.000
42	A	44	LYS	1	0.900	0.949	10.814	0.299	0.299	0.000	0.000	0.000	0.000
43	A	45	ALA	0	0.031	0.021	12.370	0.001	0.001	0.000	0.000	0.000	0.000
44	A	46	ALA	0	-0.013	-0.001	14.879	0.007	0.007	0.000	0.000	0.000	0.000
45	A	47	CYS	0	-0.080	-0.030	13.457	-0.012	-0.012	0.000	0.000	0.000	0.000
46	A	48	LEU	0	0.035	0.015	16.355	0.009	0.009	0.000	0.000	0.000	0.000
47	A	49	GLU	-1	-0.790	-0.887	18.588	-0.059	-0.059	0.000	0.000	0.000	0.000
48	A	50	LYS	1	0.855	0.927	19.201	0.181	0.181	0.000	0.000	0.000	0.000
49	A	51	LEU	0	-0.018	-0.006	18.360	0.004	0.004	0.000	0.000	0.000	0.000
50	A	52	TYR	0	0.033	0.018	22.086	0.009	0.009	0.000	0.000	0.000	0.000
51	A	53	PHE	0	-0.032	-0.026	24.510	0.010	0.010	0.000	0.000	0.000	0.000
52	A	54	GLY	0	-0.019	0.003	25.361	0.006	0.006	0.000	0.000	0.000	0.000
53	A	55	PHE	0	-0.037	-0.015	23.144	-0.006	-0.006	0.000	0.000	0.000	0.000
54	A	56	SER	0	0.048	0.018	26.911	0.006	0.006	0.000	0.000	0.000	0.000
55	A	57	ASP	-1	-0.907	-0.963	25.731	-0.153	-0.153	0.000	0.000	0.000	0.000
56	A	58	TRP	0	0.015	-0.001	19.176	-0.013	-0.013	0.000	0.000	0.000	0.000
57	A	59	HIS	0	-0.070	-0.011	25.159	0.008	0.008	0.000	0.000	0.000	0.000
58	A	60	SER	0	0.012	-0.004	26.732	0.006	0.006	0.000	0.000	0.000	0.000
59	A	61	ASP	-1	-0.879	-0.946	26.309	-0.075	-0.075	0.000	0.000	0.000	0.000
60	A	62	ALA	0	0.060	0.049	24.891	0.000	0.000	0.000	0.000	0.000	0.000
61	A	63	THR	0	-0.054	-0.038	21.177	-0.008	-0.008	0.000	0.000	0.000	0.000
62	A	64	MET	0	-0.024	-0.004	21.304	-0.002	-0.002	0.000	0.000	0.000	0.000
63	A	65	GLU	-1	-0.914	-0.955	22.463	-0.068	-0.068	0.000	0.000	0.000	0.000
64	A	66	ASN	0	-0.009	-0.017	18.803	-0.009	-0.009	0.000	0.000	0.000	0.000
65	A	67	ALA	0	-0.029	-0.017	17.728	-0.001	-0.001	0.000	0.000	0.000	0.000
66	A	68	LYS	1	0.843	0.898	18.011	0.032	0.032	0.000	0.000	0.000	0.000
67	A	69	GLU	-1	-0.876	-0.938	19.285	-0.067	-0.067	0.000	0.000	0.000	0.000
68	A	70	LEU	0	-0.064	-0.036	12.822	0.005	0.005	0.000	0.000	0.000	0.000
69	A	71	LEU	0	-0.028	-0.018	14.658	0.026	0.026	0.000	0.000	0.000	0.000
70	A	72	ASP	-1	-0.777	-0.844	16.782	0.011	0.011	0.000	0.000	0.000	0.000
71	A	73	LYS	1	0.895	0.952	11.319	0.121	0.121	0.000	0.000	0.000	0.000
72	A	74	ALA	0	-0.010	-0.005	12.565	0.030	0.030	0.000	0.000	0.000	0.000
73	A	75	LEU	0	0.019	0.014	13.521	0.039	0.039	0.000	0.000	0.000	0.000
74	A	76	MET	0	-0.005	0.005	15.258	0.013	0.013	0.000	0.000	0.000	0.000
75	A	77	THR	0	-0.082	-0.051	10.245	0.010	0.010	0.000	0.000	0.000	0.000
76	A	78	ALA	0	-0.041	-0.024	13.524	0.036	0.036	0.000	0.000	0.000	0.000
77	A	79	GLU	-1	-0.913	-0.969	14.268	0.137	0.137	0.000	0.000	0.000	0.000
78	A	80	GLY	0	-0.004	0.008	16.248	-0.002	-0.002	0.000	0.000	0.000	0.000
79	A	81	ARG	1	0.875	0.916	15.661	-0.182	-0.182	0.000	0.000	0.000	0.000
80	A	82	GLY	0	0.067	0.053	16.893	-0.003	-0.003	0.000	0.000	0.000	0.000
81	A	83	ASP	-1	-0.871	-0.936	12.504	0.448	0.448	0.000	0.000	0.000	0.000
82	A	84	ARG	1	0.952	0.975	15.926	-0.160	-0.160	0.000	0.000	0.000	0.000
83	A	85	SER	0	0.017	0.011	15.590	-0.016	-0.016	0.000	0.000	0.000	0.000
84	A	86	LYS	1	0.914	0.962	8.550	-0.493	-0.493	0.000	0.000	0.000	0.000
85	A	87	ILE	0	0.010	0.010	14.159	-0.028	-0.028	0.000	0.000	0.000	0.000
86	A	88	GLY	0	0.009	0.014	17.192	-0.028	-0.028	0.000	0.000	0.000	0.000
87	A	89	LEU	0	-0.016	-0.009	11.834	-0.017	-0.017	0.000	0.000	0.000	0.000
88	A	90	VAL	0	0.013	0.002	14.248	-0.027	-0.027	0.000	0.000	0.000	0.000
89	A	91	ASN	0	-0.015	-0.012	16.499	-0.034	-0.034	0.000	0.000	0.000	0.000
90	A	92	PHE	0	0.060	0.035	17.900	-0.014	-0.014	0.000	0.000	0.000	0.000
91	A	93	ARG	1	0.904	0.952	14.980	0.015	0.015	0.000	0.000	0.000	0.000
92	A	94	TYR	0	-0.006	-0.033	18.435	-0.012	-0.012	0.000	0.000	0.000	0.000
93	A	95	PHE	0	-0.020	-0.007	21.146	-0.009	-0.009	0.000	0.000	0.000	0.000
94	A	96	VAL	0	-0.042	-0.018	20.258	-0.008	-0.008	0.000	0.000	0.000	0.000
95	A	97	HIS	1	0.840	0.918	20.849	0.052	0.052	0.000	0.000	0.000	0.000
96	A	98	PHE	0	0.003	-0.019	22.712	-0.007	-0.007	0.000	0.000	0.000	0.000
97	A	99	PHE	0	-0.024	-0.005	25.778	-0.002	-0.002	0.000	0.000	0.000	0.000
98	A	100	ASN	0	-0.033	-0.004	22.911	0.002	0.002	0.000	0.000	0.000	0.000
99	A	101	ILE	0	-0.026	-0.008	25.858	-0.004	-0.004	0.000	0.000	0.000	0.000
100	A	102	LYS	1	0.886	0.917	28.519	0.053	0.053	0.000	0.000	0.000	0.000
101	A	103	ASP	-1	-0.794	-0.867	29.929	-0.008	-0.008	0.000	0.000	0.000	0.000
102	A	104	TYR	0	-0.030	-0.079	30.058	0.001	0.001	0.000	0.000	0.000	0.000
103	A	105	GLU	-1	-0.842	-0.879	31.676	0.002	0.002	0.000	0.000	0.000	0.000
104	A	106	LEU	0	-0.013	-0.003	27.510	0.006	0.006	0.000	0.000	0.000	0.000
105	A	107	ALA	0	-0.005	-0.011	26.789	0.006	0.006	0.000	0.000	0.000	0.000
106	A	108	GLN	0	0.073	0.034	27.236	0.010	0.010	0.000	0.000	0.000	0.000
107	A	109	SER	0	-0.002	0.008	28.953	0.008	0.008	0.000	0.000	0.000	0.000
108	A	110	TYR	0	-0.026	-0.031	22.932	0.006	0.006	0.000	0.000	0.000	0.000
109	A	111	PHE	0	0.001	0.017	24.282	0.011	0.011	0.000	0.000	0.000	0.000
110	A	112	LYS	1	0.909	0.956	25.658	-0.043	-0.043	0.000	0.000	0.000	0.000
111	A	113	LYS	1	0.912	0.968	24.237	-0.027	-0.027	0.000	0.000	0.000	0.000
112	A	114	ALA	0	0.009	0.007	21.316	0.012	0.012	0.000	0.000	0.000	0.000
113	A	115	LYS	1	0.831	0.897	22.516	-0.035	-0.035	0.000	0.000	0.000	0.000
114	A	116	ASN	0	-0.015	-0.018	25.059	0.003	0.003	0.000	0.000	0.000	0.000
115	A	117	LEU	0	-0.039	-0.011	20.898	0.005	0.005	0.000	0.000	0.000	0.000
116	A	118	GLY	0	-0.060	-0.027	21.677	0.018	0.018	0.000	0.000	0.000	0.000
117	A	119	TYR	0	-0.088	-0.066	16.064	0.023	0.023	0.000	0.000	0.000	0.000
118	A	120	VAL	0	-0.012	-0.008	19.325	-0.015	-0.015	0.000	0.000	0.000	0.000
119	A	121	ASP	-1	-0.793	-0.853	18.897	0.052	0.052	0.000	0.000	0.000	0.000
120	A	122	ASP	-1	-0.902	-0.947	20.670	0.037	0.037	0.000	0.000	0.000	0.000
121	A	123	THR	0	-0.012	-0.047	21.342	-0.012	-0.012	0.000	0.000	0.000	0.000
122	A	124	LEU	0	-0.047	-0.015	22.920	-0.007	-0.007	0.000	0.000	0.000	0.000
123	A	125	PRO	0	0.042	0.007	24.989	-0.004	-0.004	0.000	0.000	0.000	0.000
124	A	126	LEU	0	0.046	0.024	25.921	-0.005	-0.005	0.000	0.000	0.000	0.000
125	A	127	TRP	0	-0.046	-0.038	22.159	-0.011	-0.011	0.000	0.000	0.000	0.000
126	A	128	GLU	-1	-0.778	-0.865	27.261	0.037	0.037	0.000	0.000	0.000	0.000
127	A	129	ASP	-1	-0.832	-0.898	29.878	0.009	0.009	0.000	0.000	0.000	0.000
128	A	130	ARG	1	0.855	0.941	25.210	0.020	0.020	0.000	0.000	0.000	0.000
129	A	131	LEU	0	-0.092	-0.057	28.759	-0.003	-0.003	0.000	0.000	0.000	0.000
130	A	132	GLU	-1	-0.938	-0.965	31.475	0.013	0.013	0.000	0.000	0.000	0.000
131	A	133	THR	0	-0.107	-0.048	34.527	-0.002	-0.002	0.000	0.000	0.000	0.000
132	A	134	LYS	1	0.815	0.918	32.005	0.017	0.017	0.000	0.000	0.000	0.000

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