FMO DATABASE

FMODB ID: MN6NZ

Calculation Name: 1ZS3-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1ZS3

Chain ID: A

ChEMBL ID:

UniProt ID:

Base Structure: X-ray

Registration Date: 2023-09-20

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	171
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1784852.28623
FMO2-HF: Nuclear repulsion	1716575.86561
FMO2-HF: Total energy	-68276.42062
FMO2-MP2: Total energy	-68477.755428

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:3:THR)

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

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.
-3.21	0.873	7.141	-4.552	-6.672	-0.006

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.036 / 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

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	0.104	0.076	3.912	-2.838	0.070	-0.002	-1.501	-1.405	0.002
4	A	6	MET	0	0.005	-0.005	1.918	-1.396	-1.140	5.940	-2.324	-3.872	-0.004
5	A	7	ILE	0	-0.045	-0.042	2.430	-0.009	0.840	1.204	-0.724	-1.329	-0.004
6	A	8	ASP	-1	-0.860	-0.924	5.392	0.052	0.122	-0.001	-0.003	-0.066	0.000
7	A	9	GLU	-1	-0.950	-0.947	7.880	-0.905	-0.905	0.000	0.000	0.000	0.000
8	A	10	LYS	1	0.932	0.951	7.151	1.135	1.135	0.000	0.000	0.000	0.000
9	A	11	TYR	0	0.060	0.043	9.683	0.152	0.152	0.000	0.000	0.000	0.000
10	A	12	ALA	0	0.016	0.009	11.520	0.102	0.102	0.000	0.000	0.000	0.000
11	A	13	LYS	1	0.870	0.919	11.845	0.793	0.793	0.000	0.000	0.000	0.000
12	A	14	GLU	-1	-0.949	-0.965	13.811	-0.228	-0.228	0.000	0.000	0.000	0.000
13	A	15	LEU	0	0.014	-0.011	15.423	0.052	0.052	0.000	0.000	0.000	0.000
14	A	16	ASP	-1	-0.951	-0.950	17.621	-0.215	-0.215	0.000	0.000	0.000	0.000
15	A	17	LYS	1	0.902	0.931	18.865	0.229	0.229	0.000	0.000	0.000	0.000
16	A	18	ALA	0	-0.032	-0.014	19.788	0.026	0.026	0.000	0.000	0.000	0.000
17	A	19	GLU	-1	-0.904	-0.945	21.480	-0.095	-0.095	0.000	0.000	0.000	0.000
18	A	20	ILE	0	0.018	0.012	22.660	0.017	0.017	0.000	0.000	0.000	0.000
19	A	21	ASP	-1	-0.806	-0.904	23.737	-0.145	-0.145	0.000	0.000	0.000	0.000
20	A	22	HIS	0	-0.054	-0.043	24.172	0.021	0.021	0.000	0.000	0.000	0.000
21	A	23	HIS	0	-0.082	-0.035	27.561	0.017	0.017	0.000	0.000	0.000	0.000
22	A	24	LYS	1	0.804	0.904	26.728	0.142	0.142	0.000	0.000	0.000	0.000
23	A	25	PRO	0	-0.048	-0.019	30.194	0.004	0.004	0.000	0.000	0.000	0.000
24	A	26	THR	0	0.035	0.034	25.983	0.005	0.005	0.000	0.000	0.000	0.000
25	A	27	ALA	0	-0.014	-0.023	29.172	0.007	0.007	0.000	0.000	0.000	0.000
26	A	28	GLY	0	0.060	0.018	25.213	0.007	0.007	0.000	0.000	0.000	0.000
27	A	29	ALA	0	-0.004	0.021	25.361	0.003	0.003	0.000	0.000	0.000	0.000
28	A	30	MET	0	-0.045	-0.031	26.383	0.011	0.011	0.000	0.000	0.000	0.000
29	A	31	LEU	0	0.030	-0.005	27.370	0.009	0.009	0.000	0.000	0.000	0.000
30	A	32	GLY	0	0.068	0.053	25.212	0.005	0.005	0.000	0.000	0.000	0.000
31	A	33	HIS	1	0.812	0.894	25.894	0.060	0.060	0.000	0.000	0.000	0.000
32	A	34	VAL	0	-0.050	-0.001	29.015	0.006	0.006	0.000	0.000	0.000	0.000
33	A	35	LEU	0	0.077	0.025	24.283	0.006	0.006	0.000	0.000	0.000	0.000
34	A	36	SER	0	-0.025	-0.013	25.708	0.007	0.007	0.000	0.000	0.000	0.000
35	A	37	ASN	0	-0.019	-0.029	27.349	0.006	0.006	0.000	0.000	0.000	0.000
36	A	38	LEU	0	-0.013	0.022	29.231	0.004	0.004	0.000	0.000	0.000	0.000
37	A	39	PHE	0	0.030	0.016	25.311	0.007	0.007	0.000	0.000	0.000	0.000
38	A	40	ILE	0	0.002	-0.003	27.810	0.006	0.006	0.000	0.000	0.000	0.000
39	A	41	GLH	0	-0.016	-0.034	30.784	0.003	0.003	0.000	0.000	0.000	0.000
40	A	42	ASN	0	0.048	0.018	29.353	0.003	0.003	0.000	0.000	0.000	0.000
41	A	43	ILE	0	-0.007	0.026	28.682	0.004	0.004	0.000	0.000	0.000	0.000
42	A	44	ARG	1	0.882	0.925	32.641	-0.007	-0.007	0.000	0.000	0.000	0.000
43	A	45	LEU	0	-0.025	-0.002	35.740	0.001	0.001	0.000	0.000	0.000	0.000
44	A	46	THR	0	-0.007	-0.019	33.396	0.002	0.002	0.000	0.000	0.000	0.000
45	A	47	GLN	0	-0.109	-0.057	36.002	0.000	0.000	0.000	0.000	0.000	0.000
46	A	48	ALA	0	0.016	-0.004	37.725	0.001	0.001	0.000	0.000	0.000	0.000
47	A	49	GLY	0	0.017	0.021	39.576	0.000	0.000	0.000	0.000	0.000	0.000
48	A	50	ILE	0	-0.070	-0.024	36.584	0.001	0.001	0.000	0.000	0.000	0.000
49	A	51	TYR	0	0.010	0.005	38.906	0.002	0.002	0.000	0.000	0.000	0.000
50	A	52	ALA	0	0.005	0.029	43.509	-0.001	-0.001	0.000	0.000	0.000	0.000
51	A	53	LYS	1	0.836	0.899	46.012	-0.018	-0.018	0.000	0.000	0.000	0.000
52	A	54	SER	0	0.000	0.006	49.307	0.001	0.001	0.000	0.000	0.000	0.000
53	A	55	PRO	0	0.059	0.019	47.843	0.000	0.000	0.000	0.000	0.000	0.000
54	A	56	VAL	0	0.013	0.011	47.498	0.000	0.000	0.000	0.000	0.000	0.000
55	A	57	LYS	1	0.891	0.941	47.183	-0.010	-0.010	0.000	0.000	0.000	0.000
56	A	58	CYS	0	-0.043	-0.008	43.974	0.000	0.000	0.000	0.000	0.000	0.000
57	A	59	GLU	-1	-0.973	-0.980	42.684	0.018	0.018	0.000	0.000	0.000	0.000
58	A	60	TYR	0	0.052	0.022	42.603	-0.001	-0.001	0.000	0.000	0.000	0.000
59	A	61	LEU	0	-0.015	-0.015	41.050	-0.001	-0.001	0.000	0.000	0.000	0.000
60	A	62	ARG	1	0.869	0.909	38.351	-0.028	-0.028	0.000	0.000	0.000	0.000
61	A	63	GLU	-1	-0.949	-0.958	37.669	0.009	0.009	0.000	0.000	0.000	0.000
62	A	64	ILE	0	-0.009	-0.011	37.927	-0.001	-0.001	0.000	0.000	0.000	0.000
63	A	65	ALA	0	-0.003	0.002	34.589	-0.002	-0.002	0.000	0.000	0.000	0.000
64	A	66	GLN	0	-0.044	-0.032	33.483	0.002	0.002	0.000	0.000	0.000	0.000
65	A	67	ARG	1	0.887	0.934	33.333	-0.001	-0.001	0.000	0.000	0.000	0.000
66	A	68	GLU	-1	-0.814	-0.909	32.374	-0.008	-0.008	0.000	0.000	0.000	0.000
67	A	69	VAL	0	-0.033	-0.030	27.735	-0.003	-0.003	0.000	0.000	0.000	0.000
68	A	70	GLU	-1	-0.834	-0.894	28.801	0.005	0.005	0.000	0.000	0.000	0.000
69	A	71	TYR	0	-0.008	-0.009	30.332	-0.003	-0.003	0.000	0.000	0.000	0.000
70	A	72	PHE	0	-0.025	0.003	22.694	-0.005	-0.005	0.000	0.000	0.000	0.000
71	A	73	PHE	0	0.007	-0.003	22.397	-0.005	-0.005	0.000	0.000	0.000	0.000
72	A	74	LYS	1	0.852	0.941	26.095	0.014	0.014	0.000	0.000	0.000	0.000
73	A	75	ILE	0	-0.002	-0.024	27.468	-0.005	-0.005	0.000	0.000	0.000	0.000
74	A	76	SER	0	-0.023	-0.013	22.464	-0.010	-0.010	0.000	0.000	0.000	0.000
75	A	77	ASP	-1	-0.901	-0.949	23.256	-0.036	-0.036	0.000	0.000	0.000	0.000
76	A	78	LEU	0	-0.035	-0.016	24.488	-0.006	-0.006	0.000	0.000	0.000	0.000
77	A	79	LEU	0	-0.032	-0.027	23.412	-0.007	-0.007	0.000	0.000	0.000	0.000
78	A	80	LEU	0	-0.028	-0.018	18.111	-0.012	-0.012	0.000	0.000	0.000	0.000
79	A	81	ASP	-1	-0.939	-0.944	21.424	-0.072	-0.072	0.000	0.000	0.000	0.000
80	A	82	GLU	-1	-0.964	-1.000	24.111	-0.082	-0.082	0.000	0.000	0.000	0.000
81	A	83	ASN	0	-0.121	-0.054	18.676	-0.018	-0.018	0.000	0.000	0.000	0.000
82	A	84	GLU	-1	-0.876	-0.935	21.020	-0.157	-0.157	0.000	0.000	0.000	0.000
83	A	85	ILE	0	-0.032	-0.023	15.417	-0.006	-0.006	0.000	0.000	0.000	0.000
84	A	86	VAL	0	0.004	0.001	18.532	0.013	0.013	0.000	0.000	0.000	0.000
85	A	87	PRO	0	-0.048	-0.015	18.759	-0.003	-0.003	0.000	0.000	0.000	0.000
86	A	88	SER	0	-0.026	-0.018	16.891	0.012	0.012	0.000	0.000	0.000	0.000
87	A	89	THR	0	0.006	-0.002	16.511	0.024	0.024	0.000	0.000	0.000	0.000
88	A	90	THR	0	0.037	-0.004	19.655	-0.009	-0.009	0.000	0.000	0.000	0.000
89	A	91	GLU	-1	-0.918	-0.952	18.353	0.034	0.034	0.000	0.000	0.000	0.000
90	A	92	GLU	-1	-0.824	-0.902	18.245	-0.075	-0.075	0.000	0.000	0.000	0.000
91	A	93	PHE	0	-0.047	-0.026	21.903	-0.005	-0.005	0.000	0.000	0.000	0.000
92	A	94	LEU	0	0.033	0.004	24.889	-0.004	-0.004	0.000	0.000	0.000	0.000
93	A	95	LYS	1	0.892	0.973	21.809	0.080	0.080	0.000	0.000	0.000	0.000
94	A	96	TYR	0	-0.001	-0.011	21.000	-0.005	-0.005	0.000	0.000	0.000	0.000
95	A	97	HIS	0	0.068	0.056	27.225	-0.004	-0.004	0.000	0.000	0.000	0.000
96	A	98	LYS	1	0.821	0.906	29.825	0.028	0.028	0.000	0.000	0.000	0.000
97	A	99	PHE	0	-0.025	-0.029	33.429	0.000	0.000	0.000	0.000	0.000	0.000
98	A	100	ILE	0	0.019	0.046	34.349	0.002	0.002	0.000	0.000	0.000	0.000
99	A	101	THR	0	-0.004	-0.019	34.679	0.000	0.000	0.000	0.000	0.000	0.000
100	A	102	GLU	-1	-0.913	-0.947	31.526	0.026	0.026	0.000	0.000	0.000	0.000
101	A	103	ASP	-1	-0.741	-0.875	36.116	0.018	0.018	0.000	0.000	0.000	0.000
102	A	104	PRO	0	-0.011	-0.005	36.356	0.001	0.001	0.000	0.000	0.000	0.000
103	A	105	LYS	1	0.821	0.877	38.829	-0.018	-0.018	0.000	0.000	0.000	0.000
104	A	106	ALA	0	0.057	0.031	40.790	-0.001	-0.001	0.000	0.000	0.000	0.000
105	A	107	LYS	1	0.847	0.938	38.474	-0.038	-0.038	0.000	0.000	0.000	0.000
106	A	108	TYR	0	-0.052	-0.038	43.160	0.001	0.001	0.000	0.000	0.000	0.000
107	A	109	TRP	0	-0.007	0.015	42.535	-0.001	-0.001	0.000	0.000	0.000	0.000
108	A	110	THR	0	0.015	0.016	47.457	0.002	0.002	0.000	0.000	0.000	0.000
109	A	111	ASP	-1	-0.774	-0.896	48.178	0.016	0.016	0.000	0.000	0.000	0.000
110	A	112	GLU	-1	-0.843	-0.947	48.618	0.010	0.010	0.000	0.000	0.000	0.000
111	A	113	ASP	-1	-0.869	-0.936	48.195	0.009	0.009	0.000	0.000	0.000	0.000
112	A	114	LEU	0	-0.071	-0.040	42.780	-0.001	-0.001	0.000	0.000	0.000	0.000
113	A	115	LEU	0	-0.006	0.016	44.414	-0.001	-0.001	0.000	0.000	0.000	0.000
114	A	116	GLU	-1	-0.766	-0.872	45.716	0.001	0.001	0.000	0.000	0.000	0.000
115	A	117	SER	0	-0.061	-0.038	42.816	-0.001	-0.001	0.000	0.000	0.000	0.000
116	A	118	PHE	0	0.010	-0.008	38.470	-0.001	-0.001	0.000	0.000	0.000	0.000
117	A	119	ILE	0	-0.010	0.016	42.088	-0.002	-0.002	0.000	0.000	0.000	0.000
118	A	120	VAL	0	0.022	0.007	42.644	-0.002	-0.002	0.000	0.000	0.000	0.000
119	A	121	ASP	-1	-0.756	-0.850	38.519	0.001	0.001	0.000	0.000	0.000	0.000
120	A	122	PHE	0	0.001	-0.007	37.268	-0.003	-0.003	0.000	0.000	0.000	0.000
121	A	123	GLN	0	-0.033	-0.016	40.239	-0.002	-0.002	0.000	0.000	0.000	0.000
122	A	124	ALA	0	-0.031	-0.008	38.837	-0.003	-0.003	0.000	0.000	0.000	0.000
123	A	125	GLN	0	-0.051	-0.038	35.123	-0.007	-0.007	0.000	0.000	0.000	0.000
124	A	126	ASN	0	0.048	0.015	36.443	-0.005	-0.005	0.000	0.000	0.000	0.000
125	A	127	MET	0	-0.021	0.007	38.542	-0.004	-0.004	0.000	0.000	0.000	0.000
126	A	128	PHE	0	-0.012	-0.021	33.129	-0.004	-0.004	0.000	0.000	0.000	0.000
127	A	129	ILE	0	0.047	0.047	34.427	-0.005	-0.005	0.000	0.000	0.000	0.000
128	A	130	THR	0	0.004	-0.016	35.666	-0.003	-0.003	0.000	0.000	0.000	0.000
129	A	131	ARG	1	0.840	0.911	35.729	0.038	0.038	0.000	0.000	0.000	0.000
130	A	132	ALA	0	0.075	0.037	32.116	-0.004	-0.004	0.000	0.000	0.000	0.000
131	A	133	ILE	0	0.015	0.025	33.760	-0.003	-0.003	0.000	0.000	0.000	0.000
132	A	134	LYS	1	0.924	0.961	36.312	0.034	0.034	0.000	0.000	0.000	0.000
133	A	135	LEU	0	-0.044	-0.018	32.202	0.000	0.000	0.000	0.000	0.000	0.000
134	A	136	ALA	0	0.069	0.038	32.436	-0.004	-0.004	0.000	0.000	0.000	0.000
135	A	137	ASN	0	-0.054	-0.038	33.392	-0.001	-0.001	0.000	0.000	0.000	0.000
136	A	138	LYS	1	0.877	0.951	35.564	0.059	0.059	0.000	0.000	0.000	0.000
137	A	139	GLU	-1	-0.830	-0.918	29.364	-0.098	-0.098	0.000	0.000	0.000	0.000
138	A	140	GLU	-1	-0.957	-0.969	32.175	-0.072	-0.072	0.000	0.000	0.000	0.000
139	A	141	LYS	1	0.842	0.942	26.321	0.106	0.106	0.000	0.000	0.000	0.000
140	A	142	PHE	0	0.005	-0.017	31.765	0.005	0.005	0.000	0.000	0.000	0.000
141	A	143	ALA	0	0.011	0.010	31.301	0.005	0.005	0.000	0.000	0.000	0.000
142	A	144	LEU	0	0.065	0.030	28.082	0.005	0.005	0.000	0.000	0.000	0.000
143	A	145	ALA	0	-0.010	-0.006	31.412	0.004	0.004	0.000	0.000	0.000	0.000
144	A	146	ALA	0	-0.022	-0.013	34.690	0.004	0.004	0.000	0.000	0.000	0.000
145	A	147	GLY	0	0.043	0.024	33.043	0.004	0.004	0.000	0.000	0.000	0.000
146	A	148	VAL	0	-0.011	-0.015	31.951	0.004	0.004	0.000	0.000	0.000	0.000
147	A	149	VAL	0	-0.029	-0.017	34.560	0.003	0.003	0.000	0.000	0.000	0.000
148	A	150	GLU	-1	-0.861	-0.911	36.393	-0.017	-0.017	0.000	0.000	0.000	0.000
149	A	151	LEU	0	0.023	0.018	32.921	0.002	0.002	0.000	0.000	0.000	0.000
150	A	152	TYR	0	-0.025	-0.012	36.785	0.002	0.002	0.000	0.000	0.000	0.000
151	A	153	GLY	0	-0.004	-0.005	39.303	0.002	0.002	0.000	0.000	0.000	0.000
152	A	154	TYR	0	0.030	0.011	37.498	0.002	0.002	0.000	0.000	0.000	0.000
153	A	155	ASN	0	0.047	0.011	36.727	0.004	0.004	0.000	0.000	0.000	0.000
154	A	156	LEU	0	-0.040	-0.026	40.703	0.002	0.002	0.000	0.000	0.000	0.000
155	A	157	GLN	0	-0.067	-0.011	43.905	0.000	0.000	0.000	0.000	0.000	0.000
156	A	158	VAL	0	0.051	0.019	40.822	0.001	0.001	0.000	0.000	0.000	0.000
157	A	159	ILE	0	-0.014	-0.003	42.787	0.001	0.001	0.000	0.000	0.000	0.000
158	A	160	ARG	1	0.932	0.966	45.772	0.006	0.006	0.000	0.000	0.000	0.000
159	A	161	ASN	0	-0.033	-0.013	46.680	0.000	0.000	0.000	0.000	0.000	0.000
160	A	162	LEU	0	0.020	0.007	43.376	0.001	0.001	0.000	0.000	0.000	0.000
161	A	163	ALA	0	-0.006	0.000	48.083	0.001	0.001	0.000	0.000	0.000	0.000
162	A	164	GLY	0	0.022	0.010	50.767	0.000	0.000	0.000	0.000	0.000	0.000
163	A	165	ASP	-1	-0.921	-0.963	50.345	0.008	0.008	0.000	0.000	0.000	0.000
164	A	166	LEU	0	-0.050	-0.015	49.648	0.001	0.001	0.000	0.000	0.000	0.000
165	A	167	GLY	0	-0.057	-0.023	53.572	0.000	0.000	0.000	0.000	0.000	0.000
166	A	168	LYS	1	0.795	0.895	52.579	-0.002	-0.002	0.000	0.000	0.000	0.000
167	A	169	SER	0	0.006	0.007	54.633	0.000	0.000	0.000	0.000	0.000	0.000
168	A	170	VAL	0	0.032	-0.003	49.581	0.000	0.000	0.000	0.000	0.000	0.000
169	A	171	ALA	0	-0.058	0.012	52.260	0.000	0.000	0.000	0.000	0.000	0.000
170	A	172	ASP	-1	-0.876	-0.927	54.284	-0.003	-0.003	0.000	0.000	0.000	0.000
171	A	173	PHE	0	-0.074	-0.081	49.391	-0.002	-0.002	0.000	0.000	0.000	0.000

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