FMO DATABASE

FMODB ID: ZYJ1N

Calculation Name: 1O6A-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1O6A

Chain ID: A

ChEMBL ID:

UniProt ID:

Base Structure: X-ray

Registration Date: 2023-06-20

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

Apendix: None

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
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	87
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-502732.162558
FMO2-HF: Nuclear repulsion	468831.001652
FMO2-HF: Total energy	-33901.160906
FMO2-MP2: Total energy	-34000.814438

3D Structure Molmil

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:68:SER)

Summations of interaction energy for fragment #1(A:68:SER)

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.
-14.378	-10.479	3.863	-2.878	-4.883	0.014

Interaction energy analysis for fragmet #1(A:68:SER)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.024 / 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

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	70	LYS	1	0.913	0.943	2.617	-6.505	-3.821	0.830	-1.391	-2.123	0.009
4	A	71	LEU	0	-0.018	-0.017	2.345	-6.527	-5.606	3.025	-1.398	-2.548	0.005
5	A	72	GLU	-1	-0.848	-0.921	3.959	-2.103	-1.809	0.008	-0.089	-0.212	0.000
6	A	73	LEU	0	-0.052	-0.027	6.030	-0.078	-0.078	0.000	0.000	0.000	0.000
7	A	74	LEU	0	-0.076	-0.049	6.704	-0.028	-0.028	0.000	0.000	0.000	0.000
8	A	75	LEU	0	-0.050	-0.009	6.691	-0.126	-0.126	0.000	0.000	0.000	0.000
9	A	76	ASP	-1	-0.889	-0.943	9.795	0.105	0.105	0.000	0.000	0.000	0.000
10	A	77	ILE	0	-0.083	-0.021	11.643	-0.014	-0.014	0.000	0.000	0.000	0.000
11	A	78	PRO	0	0.001	0.000	14.351	-0.030	-0.030	0.000	0.000	0.000	0.000
12	A	79	LEU	0	-0.026	-0.008	13.397	0.043	0.043	0.000	0.000	0.000	0.000
13	A	80	LYS	1	0.931	0.966	17.866	-0.249	-0.249	0.000	0.000	0.000	0.000
14	A	81	VAL	0	0.022	0.011	19.761	0.015	0.015	0.000	0.000	0.000	0.000
15	A	82	THR	0	-0.035	-0.022	22.268	-0.008	-0.008	0.000	0.000	0.000	0.000
16	A	83	VAL	0	0.015	0.005	25.139	0.002	0.002	0.000	0.000	0.000	0.000
17	A	84	GLU	-1	-0.844	-0.880	27.571	0.153	0.153	0.000	0.000	0.000	0.000
18	A	85	LEU	0	0.021	0.001	30.216	-0.007	-0.007	0.000	0.000	0.000	0.000
19	A	86	GLY	0	0.058	0.015	33.255	-0.007	-0.007	0.000	0.000	0.000	0.000
20	A	87	ARG	1	0.750	0.844	27.290	-0.152	-0.152	0.000	0.000	0.000	0.000
21	A	88	THR	0	0.075	0.033	34.962	-0.006	-0.006	0.000	0.000	0.000	0.000
22	A	89	ARG	1	0.914	0.961	36.440	-0.095	-0.095	0.000	0.000	0.000	0.000
23	A	90	MET	0	0.015	0.012	39.423	-0.007	-0.007	0.000	0.000	0.000	0.000
24	A	91	THR	0	0.011	0.004	42.199	0.005	0.005	0.000	0.000	0.000	0.000
25	A	92	LEU	0	0.075	0.030	44.053	-0.001	-0.001	0.000	0.000	0.000	0.000
26	A	93	LYS	1	0.831	0.892	45.423	-0.061	-0.061	0.000	0.000	0.000	0.000
27	A	94	ARG	1	0.951	0.985	46.247	-0.064	-0.064	0.000	0.000	0.000	0.000
28	A	95	VAL	0	0.016	-0.010	42.580	-0.002	-0.002	0.000	0.000	0.000	0.000
29	A	96	LEU	0	-0.042	-0.029	45.705	-0.001	-0.001	0.000	0.000	0.000	0.000
30	A	97	GLU	-1	-0.806	-0.874	48.724	0.057	0.057	0.000	0.000	0.000	0.000
31	A	98	MET	0	-0.110	-0.033	43.228	-0.004	-0.004	0.000	0.000	0.000	0.000
32	A	99	ILE	0	0.016	0.016	49.068	0.000	0.000	0.000	0.000	0.000	0.000
33	A	100	HIS	0	0.040	0.002	49.377	0.000	0.000	0.000	0.000	0.000	0.000
34	A	101	GLY	0	0.011	0.002	49.186	-0.002	-0.002	0.000	0.000	0.000	0.000
35	A	102	SER	0	-0.036	-0.008	47.917	-0.001	-0.001	0.000	0.000	0.000	0.000
36	A	103	ILE	0	0.027	0.016	46.167	0.001	0.001	0.000	0.000	0.000	0.000
37	A	104	ILE	0	-0.057	-0.039	41.233	0.001	0.001	0.000	0.000	0.000	0.000
38	A	105	GLU	-1	-0.933	-0.953	42.603	0.049	0.049	0.000	0.000	0.000	0.000
39	A	106	LEU	0	-0.072	-0.052	36.640	0.006	0.006	0.000	0.000	0.000	0.000
40	A	107	ASP	-1	-0.861	-0.927	34.270	0.088	0.088	0.000	0.000	0.000	0.000
41	A	108	LYS	1	0.812	0.912	30.850	-0.075	-0.075	0.000	0.000	0.000	0.000
42	A	109	LEU	0	0.000	0.010	36.355	-0.004	-0.004	0.000	0.000	0.000	0.000
43	A	110	THR	0	0.006	-0.003	37.156	-0.001	-0.001	0.000	0.000	0.000	0.000
44	A	111	GLY	0	-0.024	-0.025	37.458	-0.002	-0.002	0.000	0.000	0.000	0.000
45	A	112	GLU	-1	-0.870	-0.925	32.809	0.053	0.053	0.000	0.000	0.000	0.000
46	A	113	PRO	0	-0.053	-0.004	29.162	0.000	0.000	0.000	0.000	0.000	0.000
47	A	114	VAL	0	-0.001	-0.008	28.768	0.008	0.008	0.000	0.000	0.000	0.000
48	A	115	ASP	-1	-0.802	-0.900	26.775	0.090	0.090	0.000	0.000	0.000	0.000
49	A	116	ILE	0	-0.024	-0.012	21.944	0.003	0.003	0.000	0.000	0.000	0.000
50	A	117	LEU	0	-0.019	-0.019	21.953	0.010	0.010	0.000	0.000	0.000	0.000
51	A	118	VAL	0	0.016	0.003	16.479	-0.009	-0.009	0.000	0.000	0.000	0.000
52	A	119	ASN	0	0.013	-0.003	17.139	-0.017	-0.017	0.000	0.000	0.000	0.000
53	A	120	GLY	0	0.006	0.002	20.121	0.021	0.021	0.000	0.000	0.000	0.000
54	A	121	LYS	1	0.837	0.920	17.336	-0.452	-0.452	0.000	0.000	0.000	0.000
55	A	122	LEU	0	0.018	0.017	20.400	-0.007	-0.007	0.000	0.000	0.000	0.000
56	A	123	ILE	0	-0.002	-0.004	16.523	0.008	0.008	0.000	0.000	0.000	0.000
57	A	124	ALA	0	-0.009	-0.014	19.441	-0.030	-0.030	0.000	0.000	0.000	0.000
58	A	125	ARG	1	0.816	0.882	21.892	-0.040	-0.040	0.000	0.000	0.000	0.000
59	A	126	GLY	0	0.030	0.005	25.262	-0.014	-0.014	0.000	0.000	0.000	0.000
60	A	127	GLU	-1	-0.840	-0.891	27.580	-0.008	-0.008	0.000	0.000	0.000	0.000
61	A	128	VAL	0	0.005	-0.007	30.168	0.000	0.000	0.000	0.000	0.000	0.000
62	A	129	VAL	0	-0.052	-0.023	30.095	-0.008	-0.008	0.000	0.000	0.000	0.000
63	A	130	VAL	0	0.031	0.014	32.878	0.007	0.007	0.000	0.000	0.000	0.000
64	A	131	ILE	0	-0.060	-0.037	29.473	-0.009	-0.009	0.000	0.000	0.000	0.000
65	A	132	ASP	-1	-0.908	-0.953	32.815	0.011	0.011	0.000	0.000	0.000	0.000
66	A	133	GLU	-1	-0.912	-0.950	35.396	0.025	0.025	0.000	0.000	0.000	0.000
67	A	134	ASN	0	-0.085	-0.034	32.048	0.003	0.003	0.000	0.000	0.000	0.000
68	A	135	PHE	0	-0.015	-0.017	32.642	-0.006	-0.006	0.000	0.000	0.000	0.000
69	A	136	GLY	0	0.025	0.015	29.078	0.005	0.005	0.000	0.000	0.000	0.000
70	A	137	VAL	0	-0.034	-0.016	25.369	0.000	0.000	0.000	0.000	0.000	0.000
71	A	138	ARG	1	0.853	0.928	26.330	0.020	0.020	0.000	0.000	0.000	0.000
72	A	139	ILE	0	-0.015	-0.019	20.302	0.006	0.006	0.000	0.000	0.000	0.000
73	A	140	THR	0	0.009	-0.004	24.513	-0.013	-0.013	0.000	0.000	0.000	0.000
74	A	141	GLU	-1	-0.847	-0.879	24.065	0.025	0.025	0.000	0.000	0.000	0.000
75	A	142	ILE	0	-0.052	-0.034	17.441	0.014	0.014	0.000	0.000	0.000	0.000
76	A	143	VAL	0	0.051	0.050	15.860	-0.023	-0.023	0.000	0.000	0.000	0.000
77	A	144	SER	0	0.006	-0.035	14.194	-0.029	-0.029	0.000	0.000	0.000	0.000
78	A	145	PRO	0	0.010	-0.027	10.414	0.069	0.069	0.000	0.000	0.000	0.000
79	A	146	LYS	1	0.841	0.904	9.105	-0.035	-0.035	0.000	0.000	0.000	0.000
80	A	147	GLU	-1	-0.763	-0.850	10.409	0.203	0.203	0.000	0.000	0.000	0.000
81	A	148	ARG	1	0.835	0.918	12.266	0.053	0.053	0.000	0.000	0.000	0.000
82	A	149	LEU	0	0.013	0.005	6.049	0.090	0.090	0.000	0.000	0.000	0.000
83	A	150	GLU	-1	-0.802	-0.876	10.078	0.484	0.484	0.000	0.000	0.000	0.000
84	A	151	LEU	0	0.018	0.011	11.567	0.039	0.039	0.000	0.000	0.000	0.000
85	A	152	LEU	0	-0.055	-0.034	12.288	-0.009	-0.009	0.000	0.000	0.000	0.000
86	A	153	ASN	0	-0.105	-0.057	8.865	0.313	0.313	0.000	0.000	0.000	0.000
87	A	154	GLU	-1	-0.916	-0.916	12.248	0.406	0.406	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:68:SER)