FMO DATABASE

FMODB ID: MNY2Z

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1027823.339115
FMO2-HF: Nuclear repulsion	979055.786867
FMO2-HF: Total energy	-48767.552247
FMO2-MP2: Total energy	-48905.28257

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.
-17.022	-6.903	7.575	-6.07	-11.623	-0.032

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 : -0.013 / q_NPA : 0.005

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	0.037	0.006	2.689	-4.219	-0.372	0.482	-2.083	-2.247	-0.004
4	A	4	GLU	-1	-0.801	-0.889	5.273	-0.184	-0.001	-0.001	-0.007	-0.174	0.000
5	A	5	GLU	-1	-0.815	-0.874	2.345	-9.151	-6.919	3.955	-2.645	-3.542	-0.024
6	A	6	LEU	0	0.004	-0.003	3.036	0.654	2.861	1.821	-1.169	-2.859	-0.001
7	A	7	LYS	1	0.811	0.904	3.975	1.042	0.739	0.038	0.562	-0.298	-0.001
8	A	8	THR	0	0.018	0.009	6.846	0.155	0.155	0.000	0.000	0.000	0.000
9	A	9	ARG	1	0.775	0.875	3.597	-2.591	-2.046	0.017	-0.115	-0.446	0.001
10	A	10	LEU	0	-0.020	-0.021	6.547	-0.471	-0.471	0.000	0.000	0.000	0.000
11	A	11	HIS	0	-0.019	-0.010	8.441	-0.230	-0.230	0.000	0.000	0.000	0.000
12	A	12	THR	0	-0.049	-0.030	9.510	-0.201	-0.201	0.000	0.000	0.000	0.000
13	A	13	GLU	-1	-0.776	-0.883	8.075	0.900	0.900	0.000	0.000	0.000	0.000
14	A	14	GLN	0	0.005	-0.012	10.945	-0.214	-0.214	0.000	0.000	0.000	0.000
15	A	15	SER	0	-0.019	-0.006	13.747	-0.110	-0.110	0.000	0.000	0.000	0.000
16	A	16	VAL	0	0.026	0.005	12.813	-0.069	-0.069	0.000	0.000	0.000	0.000
17	A	17	CYS	0	0.022	0.039	14.028	0.009	0.009	0.000	0.000	0.000	0.000
18	A	18	LYS	1	0.886	0.954	16.186	-0.280	-0.280	0.000	0.000	0.000	0.000
19	A	19	THR	0	-0.081	-0.044	18.811	-0.049	-0.049	0.000	0.000	0.000	0.000
20	A	20	GLU	-1	-0.954	-0.965	17.368	0.368	0.368	0.000	0.000	0.000	0.000
21	A	21	THR	0	-0.047	-0.041	19.287	-0.032	-0.032	0.000	0.000	0.000	0.000
22	A	22	GLY	0	-0.003	0.000	21.916	-0.025	-0.025	0.000	0.000	0.000	0.000
23	A	23	ILE	0	-0.036	0.005	20.236	-0.026	-0.026	0.000	0.000	0.000	0.000
24	A	24	ASP	-1	-0.868	-0.937	23.576	0.161	0.161	0.000	0.000	0.000	0.000
25	A	25	GLN	0	-0.019	-0.036	19.626	0.015	0.015	0.000	0.000	0.000	0.000
26	A	26	GLN	0	-0.039	-0.022	22.649	0.003	0.003	0.000	0.000	0.000	0.000
27	A	27	LYS	1	0.917	0.955	23.893	-0.156	-0.156	0.000	0.000	0.000	0.000
28	A	28	ALA	0	-0.020	-0.010	18.926	0.016	0.016	0.000	0.000	0.000	0.000
29	A	29	ASN	0	0.031	0.012	18.996	0.051	0.051	0.000	0.000	0.000	0.000
30	A	30	ASP	-1	-0.798	-0.884	20.090	0.163	0.163	0.000	0.000	0.000	0.000
31	A	31	VAL	0	-0.018	-0.022	16.686	0.006	0.006	0.000	0.000	0.000	0.000
32	A	32	ILE	0	-0.051	-0.021	14.812	0.024	0.024	0.000	0.000	0.000	0.000
33	A	33	GLU	-1	-0.890	-0.940	16.248	0.135	0.135	0.000	0.000	0.000	0.000
34	A	34	GLY	0	-0.020	-0.010	18.601	-0.027	-0.027	0.000	0.000	0.000	0.000
35	A	35	ASN	0	-0.067	-0.021	19.273	-0.028	-0.028	0.000	0.000	0.000	0.000
36	A	36	ILE	0	-0.017	-0.002	18.571	0.006	0.006	0.000	0.000	0.000	0.000
37	A	37	ASP	-1	-0.851	-0.925	22.531	0.137	0.137	0.000	0.000	0.000	0.000
38	A	38	VAL	0	-0.036	-0.030	22.904	0.011	0.011	0.000	0.000	0.000	0.000
39	A	39	GLU	-1	-0.803	-0.913	24.935	0.165	0.165	0.000	0.000	0.000	0.000
40	A	40	ASP	-1	-0.790	-0.855	25.933	0.178	0.178	0.000	0.000	0.000	0.000
41	A	41	LYS	1	0.988	0.980	25.190	-0.165	-0.165	0.000	0.000	0.000	0.000
42	A	42	LYS	1	0.880	0.916	23.929	-0.166	-0.166	0.000	0.000	0.000	0.000
43	A	43	VAL	0	0.047	0.035	21.242	0.030	0.030	0.000	0.000	0.000	0.000
44	A	44	GLN	0	-0.060	-0.036	20.356	0.038	0.038	0.000	0.000	0.000	0.000
45	A	45	LEU	0	-0.053	-0.023	19.958	0.023	0.023	0.000	0.000	0.000	0.000
46	A	46	TYR	0	-0.012	-0.002	16.278	0.041	0.041	0.000	0.000	0.000	0.000
47	A	47	CYS	0	-0.027	-0.011	16.013	0.057	0.057	0.000	0.000	0.000	0.000
48	A	48	GLU	-1	-0.775	-0.883	15.105	0.365	0.365	0.000	0.000	0.000	0.000
49	A	50	ILE	0	0.044	0.019	10.361	0.073	0.073	0.000	0.000	0.000	0.000
50	A	51	LEU	0	-0.030	-0.020	10.374	0.126	0.126	0.000	0.000	0.000	0.000
51	A	52	LYS	1	0.794	0.881	11.082	-0.321	-0.321	0.000	0.000	0.000	0.000
52	A	53	ASN	0	0.001	0.012	9.893	-0.046	-0.046	0.000	0.000	0.000	0.000
53	A	54	PHE	0	-0.035	-0.018	3.729	-0.194	0.066	0.002	-0.039	-0.222	0.000
54	A	55	ASN	0	-0.085	-0.039	7.519	-0.081	-0.081	0.000	0.000	0.000	0.000
55	A	56	ILE	0	-0.016	0.003	8.365	-0.072	-0.072	0.000	0.000	0.000	0.000
56	A	57	LEU	0	-0.034	0.001	11.412	-0.088	-0.088	0.000	0.000	0.000	0.000
57	A	58	ASP	-1	-0.758	-0.882	13.915	0.361	0.361	0.000	0.000	0.000	0.000
58	A	59	LYS	1	0.999	0.976	15.938	-0.270	-0.270	0.000	0.000	0.000	0.000
59	A	60	ASN	0	-0.062	-0.028	18.205	-0.017	-0.017	0.000	0.000	0.000	0.000
60	A	61	ASN	0	-0.027	-0.020	18.489	-0.023	-0.023	0.000	0.000	0.000	0.000
61	A	62	VAL	0	0.017	0.028	18.787	-0.010	-0.010	0.000	0.000	0.000	0.000
62	A	63	PHE	0	0.060	0.025	14.811	0.038	0.038	0.000	0.000	0.000	0.000
63	A	64	LYS	1	0.818	0.898	13.000	-0.422	-0.422	0.000	0.000	0.000	0.000
64	A	65	PRO	0	0.067	0.023	12.950	0.066	0.066	0.000	0.000	0.000	0.000
65	A	66	GLN	0	0.042	0.024	10.487	-0.038	-0.038	0.000	0.000	0.000	0.000
66	A	67	GLY	0	0.031	0.016	8.641	0.046	0.046	0.000	0.000	0.000	0.000
67	A	68	ILE	0	0.021	0.006	8.005	0.177	0.177	0.000	0.000	0.000	0.000
68	A	69	LYS	1	0.890	0.941	9.681	-0.204	-0.204	0.000	0.000	0.000	0.000
69	A	70	ALA	0	-0.017	0.000	5.696	-0.093	-0.093	0.000	0.000	0.000	0.000
70	A	71	VAL	0	0.026	0.018	4.295	-0.209	-0.019	-0.001	-0.022	-0.167	0.000
71	A	72	MET	0	-0.005	-0.012	6.318	-0.212	-0.212	0.000	0.000	0.000	0.000
72	A	73	GLU	-1	-0.918	-0.965	8.219	-0.099	-0.099	0.000	0.000	0.000	0.000
73	A	74	LEU	0	-0.049	-0.014	2.366	-1.204	-0.246	1.262	-0.552	-1.668	-0.003
74	A	75	LEU	0	-0.077	-0.041	6.589	-0.231	-0.231	0.000	0.000	0.000	0.000
75	A	76	ILE	0	-0.039	-0.016	9.799	-0.003	-0.003	0.000	0.000	0.000	0.000
76	A	77	ASP	-1	-0.787	-0.865	11.991	-0.188	-0.188	0.000	0.000	0.000	0.000
77	A	78	GLU	-1	-0.788	-0.896	13.670	-0.034	-0.034	0.000	0.000	0.000	0.000
78	A	79	ASN	0	-0.008	-0.017	14.500	0.089	0.089	0.000	0.000	0.000	0.000
79	A	80	SER	0	0.006	-0.022	16.181	0.051	0.051	0.000	0.000	0.000	0.000
80	A	81	VAL	0	-0.001	0.015	11.529	0.062	0.062	0.000	0.000	0.000	0.000
81	A	82	LYS	1	0.798	0.887	14.848	0.079	0.079	0.000	0.000	0.000	0.000
82	A	83	GLN	0	-0.024	-0.008	17.700	0.032	0.032	0.000	0.000	0.000	0.000
83	A	84	LEU	0	0.047	0.037	14.219	0.021	0.021	0.000	0.000	0.000	0.000
84	A	85	VAL	0	-0.023	-0.018	15.028	0.028	0.028	0.000	0.000	0.000	0.000
85	A	86	SER	0	-0.055	-0.034	17.542	0.004	0.004	0.000	0.000	0.000	0.000
86	A	87	ASP	-1	-0.843	-0.864	20.614	0.147	0.147	0.000	0.000	0.000	0.000
87	A	88	CYS	0	-0.062	-0.025	17.761	-0.026	-0.026	0.000	0.000	0.000	0.000
88	A	89	SER	0	-0.057	-0.043	18.517	0.019	0.019	0.000	0.000	0.000	0.000
89	A	90	THR	0	-0.029	-0.019	19.703	0.005	0.005	0.000	0.000	0.000	0.000
90	A	91	ILE	0	0.020	0.026	20.491	-0.019	-0.019	0.000	0.000	0.000	0.000
91	A	92	SER	0	-0.003	-0.007	23.999	0.004	0.004	0.000	0.000	0.000	0.000
92	A	93	GLU	-1	-0.819	-0.911	24.951	0.160	0.160	0.000	0.000	0.000	0.000
93	A	94	GLU	-1	-0.874	-0.945	25.910	0.171	0.171	0.000	0.000	0.000	0.000
94	A	95	ASN	0	-0.020	0.009	26.711	0.016	0.016	0.000	0.000	0.000	0.000
95	A	96	PRO	0	0.024	-0.003	22.608	0.010	0.010	0.000	0.000	0.000	0.000
96	A	97	HIS	1	0.838	0.911	21.836	-0.226	-0.226	0.000	0.000	0.000	0.000
97	A	98	LEU	0	0.035	0.027	22.392	0.017	0.017	0.000	0.000	0.000	0.000
98	A	99	LYS	1	0.893	0.952	20.953	-0.207	-0.207	0.000	0.000	0.000	0.000
99	A	100	ALA	0	-0.003	0.007	18.098	0.018	0.018	0.000	0.000	0.000	0.000
100	A	101	SER	0	0.014	-0.013	18.266	0.030	0.030	0.000	0.000	0.000	0.000
101	A	102	LYS	1	0.886	0.938	20.197	-0.165	-0.165	0.000	0.000	0.000	0.000
102	A	103	LEU	0	-0.013	-0.002	16.447	-0.002	-0.002	0.000	0.000	0.000	0.000
103	A	104	VAL	0	0.024	0.013	14.479	0.016	0.016	0.000	0.000	0.000	0.000
104	A	105	GLN	0	-0.019	-0.002	16.589	-0.004	-0.004	0.000	0.000	0.000	0.000
105	A	107	VAL	0	0.050	0.011	12.526	-0.023	-0.023	0.000	0.000	0.000	0.000
106	A	108	SER	0	-0.038	-0.035	15.791	-0.001	-0.001	0.000	0.000	0.000	0.000
107	A	109	LYS	1	0.781	0.884	16.825	-0.194	-0.194	0.000	0.000	0.000	0.000
108	A	110	TYR	0	-0.074	-0.054	15.714	-0.044	-0.044	0.000	0.000	0.000	0.000
109	A	111	LYS	1	0.930	0.958	12.289	-0.016	-0.016	0.000	0.000	0.000	0.000
110	A	112	THR	0	0.045	0.044	14.073	0.083	0.083	0.000	0.000	0.000	0.000
111	A	113	MET	0	0.040	0.028	11.019	0.053	0.053	0.000	0.000	0.000	0.000
112	A	114	LYS	1	0.907	0.944	12.266	-0.109	-0.109	0.000	0.000	0.000	0.000
113	A	115	SER	0	-0.095	-0.052	13.946	-0.084	-0.084	0.000	0.000	0.000	0.000
114	A	116	VAL	0	0.010	-0.008	7.830	-0.126	-0.126	0.000	0.000	0.000	0.000
115	A	117	ASP	-1	-0.794	-0.899	10.610	0.048	0.048	0.000	0.000	0.000	0.000
116	A	118	PHE	0	-0.098	-0.042	12.372	-0.074	-0.074	0.000	0.000	0.000	0.000
117	A	119	LEU	0	-0.025	0.009	9.861	-0.052	-0.052	0.000	0.000	0.000	0.000

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