FMO DATABASE

FMODB ID: 767ZK

Calculation Name: 3S0A-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3S0A

Chain ID: A

ChEMBL ID:

UniProt ID: Q1W640

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	OptAll
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	117
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1030409.953767
FMO2-HF: Nuclear repulsion	981642.235841
FMO2-HF: Total energy	-48767.717926
FMO2-MP2: Total energy	-48905.502605

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:1:MET)

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

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.
-18.195	-8.671	8.143	-6.199	-11.467	-0.045

Interaction energy analysis for fragmet #1(A:1:MET)

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 : 0.003

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	3	ILE	0	0.038	0.007	2.577	-3.968	-0.638	0.795	-1.995	-2.130	-0.010
4	A	4	GLU	-1	-0.766	-0.878	5.205	-0.053	0.128	-0.001	-0.007	-0.173	0.000
5	A	5	GLU	-1	-0.822	-0.862	2.363	-10.716	-8.254	4.761	-3.086	-4.138	-0.030
6	A	6	LEU	0	0.017	0.007	3.038	0.773	3.129	1.707	-1.233	-2.830	-0.001
7	A	7	LYS	1	0.764	0.886	3.957	0.787	0.363	0.041	0.693	-0.309	-0.001
8	A	8	THR	0	0.030	0.010	6.918	0.137	0.137	0.000	0.000	0.000	0.000
9	A	9	ARG	1	0.770	0.875	3.878	-2.672	-2.191	0.015	-0.092	-0.404	0.000
10	A	10	LEU	0	-0.017	-0.016	6.474	-0.600	-0.578	-0.001	-0.002	-0.018	0.000
11	A	11	HIS	0	-0.028	-0.026	8.560	-0.221	-0.221	0.000	0.000	0.000	0.000
12	A	12	THR	0	-0.044	-0.030	9.151	-0.232	-0.232	0.000	0.000	0.000	0.000
13	A	13	GLU	-1	-0.792	-0.890	8.098	0.908	0.908	0.000	0.000	0.000	0.000
14	A	14	GLN	0	0.019	-0.007	11.003	-0.216	-0.216	0.000	0.000	0.000	0.000
15	A	15	SER	0	0.012	0.012	13.800	-0.121	-0.121	0.000	0.000	0.000	0.000
16	A	16	VAL	0	0.027	0.008	12.885	-0.073	-0.073	0.000	0.000	0.000	0.000
17	A	17	CYS	0	0.025	0.033	14.128	0.003	0.003	0.000	0.000	0.000	0.000
18	A	18	LYS	1	0.866	0.945	16.313	-0.313	-0.313	0.000	0.000	0.000	0.000
19	A	19	THR	0	-0.091	-0.042	18.646	-0.060	-0.060	0.000	0.000	0.000	0.000
20	A	20	GLU	-1	-0.954	-0.983	17.479	0.389	0.389	0.000	0.000	0.000	0.000
21	A	21	THR	0	-0.038	-0.045	19.204	-0.036	-0.036	0.000	0.000	0.000	0.000
22	A	22	GLY	0	0.005	0.010	21.872	-0.022	-0.022	0.000	0.000	0.000	0.000
23	A	23	ILE	0	-0.034	-0.001	20.174	-0.029	-0.029	0.000	0.000	0.000	0.000
24	A	24	ASP	-1	-0.794	-0.882	23.460	0.178	0.178	0.000	0.000	0.000	0.000
25	A	25	GLN	0	0.005	-0.016	19.996	0.015	0.015	0.000	0.000	0.000	0.000
26	A	26	GLN	0	-0.046	-0.025	22.949	0.006	0.006	0.000	0.000	0.000	0.000
27	A	27	LYS	1	0.893	0.934	23.710	-0.168	-0.168	0.000	0.000	0.000	0.000
28	A	28	ALA	0	-0.017	-0.005	19.372	0.019	0.019	0.000	0.000	0.000	0.000
29	A	29	ASN	0	0.034	0.018	19.077	0.052	0.052	0.000	0.000	0.000	0.000
30	A	30	ASP	-1	-0.802	-0.895	19.910	0.184	0.184	0.000	0.000	0.000	0.000
31	A	31	VAL	0	-0.025	-0.023	16.974	0.003	0.003	0.000	0.000	0.000	0.000
32	A	32	ILE	0	-0.014	0.002	14.715	0.033	0.033	0.000	0.000	0.000	0.000
33	A	33	GLU	-1	-0.840	-0.916	16.297	0.136	0.136	0.000	0.000	0.000	0.000
34	A	34	GLY	0	-0.005	-0.011	18.559	-0.032	-0.032	0.000	0.000	0.000	0.000
35	A	35	ASN	0	-0.065	-0.022	19.333	-0.028	-0.028	0.000	0.000	0.000	0.000
36	A	36	ILE	0	-0.040	-0.013	18.670	-0.001	-0.001	0.000	0.000	0.000	0.000
37	A	37	ASP	-1	-0.831	-0.917	22.727	0.149	0.149	0.000	0.000	0.000	0.000
38	A	38	VAL	0	-0.048	-0.038	22.938	0.014	0.014	0.000	0.000	0.000	0.000
39	A	39	GLU	-1	-0.723	-0.869	24.981	0.176	0.176	0.000	0.000	0.000	0.000
40	A	40	ASP	-1	-0.789	-0.859	26.143	0.194	0.194	0.000	0.000	0.000	0.000
41	A	41	LYS	1	0.964	0.969	25.483	-0.172	-0.172	0.000	0.000	0.000	0.000
42	A	42	LYS	1	0.822	0.892	24.063	-0.178	-0.178	0.000	0.000	0.000	0.000
43	A	43	VAL	0	0.037	0.021	21.278	0.034	0.034	0.000	0.000	0.000	0.000
44	A	44	GLN	0	-0.025	-0.016	20.596	0.039	0.039	0.000	0.000	0.000	0.000
45	A	45	LEU	0	-0.026	-0.009	20.312	0.024	0.024	0.000	0.000	0.000	0.000
46	A	46	TYR	0	-0.042	-0.017	16.430	0.038	0.038	0.000	0.000	0.000	0.000
47	A	47	CYS	0	-0.030	-0.006	16.197	0.062	0.062	0.000	0.000	0.000	0.000
48	A	48	GLU	-1	-0.755	-0.855	15.374	0.383	0.383	0.000	0.000	0.000	0.000
49	A	50	ILE	0	0.038	0.019	10.698	0.076	0.076	0.000	0.000	0.000	0.000
50	A	51	LEU	0	-0.016	-0.016	10.602	0.143	0.143	0.000	0.000	0.000	0.000
51	A	52	LYS	1	0.770	0.877	11.464	-0.341	-0.341	0.000	0.000	0.000	0.000
52	A	53	ASN	0	0.017	0.014	9.864	-0.041	-0.041	0.000	0.000	0.000	0.000
53	A	54	PHE	0	-0.043	-0.023	4.346	-0.110	0.055	-0.001	-0.018	-0.146	0.000
54	A	55	ASN	0	-0.082	-0.033	7.765	-0.069	-0.069	0.000	0.000	0.000	0.000
55	A	56	ILE	0	-0.010	0.007	9.197	-0.078	-0.078	0.000	0.000	0.000	0.000
56	A	57	LEU	0	-0.043	-0.012	11.916	-0.103	-0.103	0.000	0.000	0.000	0.000
57	A	58	ASP	-1	-0.748	-0.867	13.885	0.391	0.391	0.000	0.000	0.000	0.000
58	A	59	LYS	1	0.992	0.976	16.147	-0.285	-0.285	0.000	0.000	0.000	0.000
59	A	60	ASN	0	-0.070	-0.050	18.500	-0.029	-0.029	0.000	0.000	0.000	0.000
60	A	61	ASN	0	-0.023	-0.012	18.749	-0.024	-0.024	0.000	0.000	0.000	0.000
61	A	62	VAL	0	0.014	0.020	19.427	-0.007	-0.007	0.000	0.000	0.000	0.000
62	A	63	PHE	0	0.053	0.019	15.525	0.039	0.039	0.000	0.000	0.000	0.000
63	A	64	LYS	1	0.828	0.914	13.270	-0.453	-0.453	0.000	0.000	0.000	0.000
64	A	65	PRO	0	0.054	0.024	13.197	0.074	0.074	0.000	0.000	0.000	0.000
65	A	66	GLN	0	0.049	0.024	10.485	-0.051	-0.051	0.000	0.000	0.000	0.000
66	A	67	GLY	0	0.032	0.018	8.889	0.057	0.057	0.000	0.000	0.000	0.000
67	A	68	ILE	0	0.024	0.008	8.367	0.200	0.200	0.000	0.000	0.000	0.000
68	A	69	LYS	1	0.882	0.947	9.958	-0.199	-0.199	0.000	0.000	0.000	0.000
69	A	70	ALA	0	0.001	0.006	5.749	-0.121	-0.121	0.000	0.000	0.000	0.000
70	A	71	VAL	0	0.008	0.017	5.003	0.212	0.212	0.000	0.000	0.000	0.000
71	A	72	MET	0	-0.005	-0.013	6.771	-0.310	-0.310	0.000	0.000	0.000	0.000
72	A	73	GLU	-1	-0.913	-0.975	8.285	-0.053	-0.053	0.000	0.000	0.000	0.000
73	A	74	LEU	0	-0.043	-0.004	2.529	-1.314	-0.363	0.827	-0.459	-1.319	-0.003
74	A	75	LEU	0	-0.072	-0.041	6.708	-0.148	-0.148	0.000	0.000	0.000	0.000
75	A	76	ILE	0	-0.039	-0.016	9.881	0.023	0.023	0.000	0.000	0.000	0.000
76	A	77	ASP	-1	-0.775	-0.861	12.180	-0.206	-0.206	0.000	0.000	0.000	0.000
77	A	78	GLU	-1	-0.786	-0.889	13.556	-0.058	-0.058	0.000	0.000	0.000	0.000
78	A	79	ASN	0	-0.026	-0.023	14.480	0.098	0.098	0.000	0.000	0.000	0.000
79	A	80	SER	0	0.035	-0.006	16.315	0.046	0.046	0.000	0.000	0.000	0.000
80	A	81	VAL	0	-0.019	0.000	11.857	0.062	0.062	0.000	0.000	0.000	0.000
81	A	82	LYS	1	0.781	0.874	15.171	0.095	0.095	0.000	0.000	0.000	0.000
82	A	83	GLN	0	-0.040	-0.003	18.222	0.028	0.028	0.000	0.000	0.000	0.000
83	A	84	LEU	0	0.047	0.032	14.452	0.025	0.025	0.000	0.000	0.000	0.000
84	A	85	VAL	0	-0.016	-0.023	15.628	0.034	0.034	0.000	0.000	0.000	0.000
85	A	86	SER	0	-0.047	-0.029	18.114	0.007	0.007	0.000	0.000	0.000	0.000
86	A	87	ASP	-1	-0.839	-0.869	21.205	0.153	0.153	0.000	0.000	0.000	0.000
87	A	88	CYS	0	-0.065	-0.018	18.331	-0.024	-0.024	0.000	0.000	0.000	0.000
88	A	89	SER	0	-0.065	-0.048	19.142	0.014	0.014	0.000	0.000	0.000	0.000
89	A	90	THR	0	-0.025	-0.016	20.273	0.004	0.004	0.000	0.000	0.000	0.000
90	A	91	ILE	0	-0.001	0.009	21.298	-0.018	-0.018	0.000	0.000	0.000	0.000
91	A	92	SER	0	-0.005	0.002	24.706	0.005	0.005	0.000	0.000	0.000	0.000
92	A	93	GLU	-1	-0.785	-0.912	25.750	0.171	0.171	0.000	0.000	0.000	0.000
93	A	94	GLU	-1	-0.862	-0.934	26.511	0.194	0.194	0.000	0.000	0.000	0.000
94	A	95	ASN	0	-0.004	0.020	26.861	0.012	0.012	0.000	0.000	0.000	0.000
95	A	96	PRO	0	0.002	-0.008	23.011	0.011	0.011	0.000	0.000	0.000	0.000
96	A	97	HIS	1	0.819	0.884	21.988	-0.235	-0.235	0.000	0.000	0.000	0.000
97	A	98	LEU	0	0.001	0.013	22.394	0.019	0.019	0.000	0.000	0.000	0.000
98	A	99	LYS	1	0.856	0.930	21.726	-0.209	-0.209	0.000	0.000	0.000	0.000
99	A	100	ALA	0	0.009	0.014	18.143	0.015	0.015	0.000	0.000	0.000	0.000
100	A	101	SER	0	0.013	-0.013	18.494	0.031	0.031	0.000	0.000	0.000	0.000
101	A	102	LYS	1	0.833	0.909	20.493	-0.172	-0.172	0.000	0.000	0.000	0.000
102	A	103	LEU	0	-0.005	0.005	17.074	-0.001	-0.001	0.000	0.000	0.000	0.000
103	A	104	VAL	0	0.023	0.009	14.822	0.014	0.014	0.000	0.000	0.000	0.000
104	A	105	GLN	0	-0.032	-0.012	17.062	-0.006	-0.006	0.000	0.000	0.000	0.000
105	A	107	VAL	0	0.045	0.006	13.028	-0.023	-0.023	0.000	0.000	0.000	0.000
106	A	108	SER	0	-0.013	-0.026	16.261	-0.012	-0.012	0.000	0.000	0.000	0.000
107	A	109	LYS	1	0.765	0.878	17.465	-0.200	-0.200	0.000	0.000	0.000	0.000
108	A	110	TYR	0	-0.075	-0.053	16.089	-0.048	-0.048	0.000	0.000	0.000	0.000
109	A	111	LYS	1	0.882	0.924	12.169	-0.054	-0.054	0.000	0.000	0.000	0.000
110	A	112	THR	0	0.053	0.047	14.094	0.096	0.096	0.000	0.000	0.000	0.000
111	A	113	MET	0	0.024	0.039	11.623	0.037	0.037	0.000	0.000	0.000	0.000
112	A	114	LYS	1	0.863	0.919	12.439	-0.115	-0.115	0.000	0.000	0.000	0.000
113	A	115	SER	0	-0.092	-0.053	14.497	-0.092	-0.092	0.000	0.000	0.000	0.000
114	A	116	VAL	0	0.009	-0.002	7.985	-0.128	-0.128	0.000	0.000	0.000	0.000
115	A	117	ASP	-1	-0.784	-0.898	10.776	0.091	0.091	0.000	0.000	0.000	0.000
116	A	118	PHE	0	-0.067	-0.040	12.331	-0.093	-0.093	0.000	0.000	0.000	0.000
117	A	119	LEU	0	-0.017	0.022	9.807	-0.067	-0.067	0.000	0.000	0.000	0.000

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