FMO DATABASE

FMODB ID: 53RQZ

Calculation Name: 1AYY-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1AYY

Chain ID: A

ChEMBL ID:

UniProt ID: Q47898

Base Structure: X-ray

Registration Date: 2023-03-13

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	OptH
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	138
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1148761.986768
FMO2-HF: Nuclear repulsion	1094757.439093
FMO2-HF: Total energy	-54004.547675
FMO2-MP2: Total energy	-54160.354202

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:2:THR)

Summations of interaction energy for fragment #1(A:2: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.
-6.925	-2.583	0.741	-2.096	-2.988	0.014

Interaction energy analysis for fragmet #1(A:2:THR)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.000 / q_NPA : -0.019

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	4	LYS	1	0.973	1.015	2.714	-6.449	-2.142	0.742	-2.086	-2.964	0.014
4	A	5	PRO	0	-0.002	-0.015	4.920	-0.709	-0.674	-0.001	-0.010	-0.024	0.000
5	A	6	ILE	0	0.014	-0.009	6.711	-0.327	-0.327	0.000	0.000	0.000	0.000
6	A	7	VAL	0	-0.004	0.003	9.130	0.143	0.143	0.000	0.000	0.000	0.000
7	A	8	LEU	0	-0.021	-0.013	12.108	-0.054	-0.054	0.000	0.000	0.000	0.000
8	A	9	SER	0	-0.003	0.012	14.415	0.025	0.025	0.000	0.000	0.000	0.000
9	A	10	THR	0	0.006	-0.001	18.174	-0.013	-0.013	0.000	0.000	0.000	0.000
10	A	11	TRP	0	0.034	0.016	21.138	-0.004	-0.004	0.000	0.000	0.000	0.000
11	A	12	ASN	0	0.045	0.015	22.787	-0.005	-0.005	0.000	0.000	0.000	0.000
12	A	13	PHE	0	0.042	0.034	24.398	-0.009	-0.009	0.000	0.000	0.000	0.000
13	A	14	GLY	0	0.044	0.016	21.307	0.001	0.001	0.000	0.000	0.000	0.000
14	A	15	LEU	0	-0.043	-0.024	19.878	-0.006	-0.006	0.000	0.000	0.000	0.000
15	A	16	HIS	0	0.050	0.003	20.844	-0.013	-0.013	0.000	0.000	0.000	0.000
16	A	17	ALA	0	0.046	0.029	21.573	0.000	0.000	0.000	0.000	0.000	0.000
17	A	18	ASN	0	0.018	-0.003	16.750	0.028	0.028	0.000	0.000	0.000	0.000
18	A	19	VAL	0	-0.032	-0.006	17.716	-0.005	-0.005	0.000	0.000	0.000	0.000
19	A	20	GLU	-1	-0.847	-0.925	19.783	-0.022	-0.022	0.000	0.000	0.000	0.000
20	A	21	ALA	0	0.016	0.018	16.357	0.012	0.012	0.000	0.000	0.000	0.000
21	A	22	TRP	0	0.032	0.007	10.273	0.048	0.048	0.000	0.000	0.000	0.000
22	A	23	LYS	1	0.854	0.951	15.793	0.032	0.032	0.000	0.000	0.000	0.000
23	A	24	VAL	0	0.024	0.028	16.438	-0.003	-0.003	0.000	0.000	0.000	0.000
24	A	25	LEU	0	0.026	0.017	11.219	0.019	0.019	0.000	0.000	0.000	0.000
25	A	26	SER	0	-0.077	-0.048	12.473	0.026	0.026	0.000	0.000	0.000	0.000
26	A	27	LYS	1	0.839	0.913	13.574	0.016	0.016	0.000	0.000	0.000	0.000
27	A	28	GLY	0	-0.025	-0.006	12.356	0.002	0.002	0.000	0.000	0.000	0.000
28	A	29	GLY	0	-0.029	-0.017	13.432	0.037	0.037	0.000	0.000	0.000	0.000
29	A	30	LYS	1	0.983	0.976	13.666	-0.133	-0.133	0.000	0.000	0.000	0.000
30	A	31	ALA	0	0.059	0.016	11.999	-0.040	-0.040	0.000	0.000	0.000	0.000
31	A	32	LEU	0	0.052	0.031	14.033	-0.039	-0.039	0.000	0.000	0.000	0.000
32	A	33	ASP	-1	-0.820	-0.899	17.466	0.102	0.102	0.000	0.000	0.000	0.000
33	A	34	ALA	0	-0.069	-0.034	15.325	-0.027	-0.027	0.000	0.000	0.000	0.000
34	A	35	VAL	0	0.003	-0.012	15.409	-0.029	-0.029	0.000	0.000	0.000	0.000
35	A	36	GLU	-1	-0.822	-0.880	17.988	0.065	0.065	0.000	0.000	0.000	0.000
36	A	37	LYS	1	0.913	0.934	21.030	-0.074	-0.074	0.000	0.000	0.000	0.000
37	A	38	GLY	0	0.011	0.018	20.216	-0.012	-0.012	0.000	0.000	0.000	0.000
38	A	39	VAL	0	0.024	0.002	20.844	-0.010	-0.010	0.000	0.000	0.000	0.000
39	A	40	ARG	1	0.910	0.964	23.197	-0.036	-0.036	0.000	0.000	0.000	0.000
40	A	41	LEU	0	-0.031	0.007	24.405	-0.004	-0.004	0.000	0.000	0.000	0.000
41	A	42	VAL	0	0.005	-0.011	24.741	-0.004	-0.004	0.000	0.000	0.000	0.000
42	A	43	GLU	-1	-0.785	-0.889	27.552	0.039	0.039	0.000	0.000	0.000	0.000
43	A	44	ASP	-1	-0.851	-0.947	29.624	0.015	0.015	0.000	0.000	0.000	0.000
44	A	45	ASP	-1	-0.839	-0.890	30.410	-0.012	-0.012	0.000	0.000	0.000	0.000
45	A	46	PRO	0	-0.047	-0.020	32.286	0.001	0.001	0.000	0.000	0.000	0.000
46	A	47	THR	0	-0.095	-0.081	33.344	0.000	0.000	0.000	0.000	0.000	0.000
47	A	48	GLU	-1	-0.880	-0.928	29.297	-0.010	-0.010	0.000	0.000	0.000	0.000
48	A	49	ARG	1	0.841	0.890	32.362	0.001	0.001	0.000	0.000	0.000	0.000
49	A	50	SER	0	-0.105	-0.069	29.455	0.000	0.000	0.000	0.000	0.000	0.000
50	A	51	VAL	0	-0.062	-0.036	27.378	0.004	0.004	0.000	0.000	0.000	0.000
51	A	52	GLY	0	0.069	0.043	30.552	-0.002	-0.002	0.000	0.000	0.000	0.000
52	A	53	TYR	0	-0.046	-0.024	32.414	-0.001	-0.001	0.000	0.000	0.000	0.000
53	A	54	GLY	0	0.052	0.034	34.370	-0.002	-0.002	0.000	0.000	0.000	0.000
54	A	55	GLY	0	-0.039	-0.001	35.110	-0.001	-0.001	0.000	0.000	0.000	0.000
55	A	56	ARG	1	0.819	0.901	34.740	-0.006	-0.006	0.000	0.000	0.000	0.000
56	A	57	PRO	0	-0.016	-0.002	37.753	0.002	0.002	0.000	0.000	0.000	0.000
57	A	58	ASP	-1	-0.754	-0.872	40.351	0.018	0.018	0.000	0.000	0.000	0.000
58	A	59	ARG	1	0.916	0.930	41.511	-0.018	-0.018	0.000	0.000	0.000	0.000
59	A	60	ASP	-1	-0.924	-0.964	44.692	0.015	0.015	0.000	0.000	0.000	0.000
60	A	61	GLY	0	-0.084	-0.034	44.671	-0.001	-0.001	0.000	0.000	0.000	0.000
61	A	62	ARG	1	0.812	0.890	42.643	-0.021	-0.021	0.000	0.000	0.000	0.000
62	A	63	VAL	0	0.012	0.003	37.062	0.000	0.000	0.000	0.000	0.000	0.000
63	A	64	THR	0	-0.043	0.002	36.736	0.001	0.001	0.000	0.000	0.000	0.000
64	A	65	LEU	0	-0.057	-0.019	32.174	0.000	0.000	0.000	0.000	0.000	0.000
65	A	66	ASP	-1	-0.835	-0.917	30.464	0.039	0.039	0.000	0.000	0.000	0.000
66	A	67	ALA	0	-0.041	-0.023	26.687	-0.001	-0.001	0.000	0.000	0.000	0.000
67	A	68	CYS	0	-0.034	-0.027	24.085	0.001	0.001	0.000	0.000	0.000	0.000
68	A	69	ILE	0	-0.019	-0.004	20.516	0.001	0.001	0.000	0.000	0.000	0.000
69	A	70	MET	0	-0.009	-0.013	18.229	-0.007	-0.007	0.000	0.000	0.000	0.000
70	A	71	ASP	-1	-0.822	-0.872	17.041	0.212	0.212	0.000	0.000	0.000	0.000
71	A	72	GLU	-1	-0.943	-0.986	13.150	0.312	0.312	0.000	0.000	0.000	0.000
72	A	73	ASN	0	-0.098	-0.063	14.913	0.024	0.024	0.000	0.000	0.000	0.000
73	A	74	TYR	0	-0.023	-0.017	17.281	-0.028	-0.028	0.000	0.000	0.000	0.000
74	A	75	ASN	0	-0.064	-0.011	19.856	-0.031	-0.031	0.000	0.000	0.000	0.000
75	A	76	ILE	0	0.007	-0.024	21.296	0.007	0.007	0.000	0.000	0.000	0.000
76	A	77	GLY	0	0.034	0.015	23.640	-0.006	-0.006	0.000	0.000	0.000	0.000
77	A	78	SER	0	-0.032	-0.024	25.619	0.002	0.002	0.000	0.000	0.000	0.000
78	A	79	VAL	0	-0.001	-0.001	28.218	-0.002	-0.002	0.000	0.000	0.000	0.000
79	A	80	ALA	0	0.001	-0.004	30.955	0.000	0.000	0.000	0.000	0.000	0.000
80	A	81	CYS	0	0.000	-0.013	33.430	-0.002	-0.002	0.000	0.000	0.000	0.000
81	A	82	MET	0	0.018	0.040	32.817	-0.001	-0.001	0.000	0.000	0.000	0.000
82	A	83	GLU	-1	-0.780	-0.889	36.641	0.020	0.020	0.000	0.000	0.000	0.000
83	A	84	HIS	0	-0.010	-0.031	39.058	0.002	0.002	0.000	0.000	0.000	0.000
84	A	85	ILE	0	0.024	0.024	33.569	-0.001	-0.001	0.000	0.000	0.000	0.000
85	A	86	LYS	1	0.904	0.967	33.276	-0.011	-0.011	0.000	0.000	0.000	0.000
86	A	87	ASN	0	-0.068	-0.051	29.270	-0.001	-0.001	0.000	0.000	0.000	0.000
87	A	88	PRO	0	0.028	0.003	29.437	0.004	0.004	0.000	0.000	0.000	0.000
88	A	89	ILE	0	0.030	0.018	23.001	0.006	0.006	0.000	0.000	0.000	0.000
89	A	90	SER	0	-0.015	-0.015	26.080	0.005	0.005	0.000	0.000	0.000	0.000
90	A	91	VAL	0	-0.015	0.005	27.896	0.003	0.003	0.000	0.000	0.000	0.000
91	A	92	ALA	0	0.004	0.010	26.604	0.002	0.002	0.000	0.000	0.000	0.000
92	A	93	ARG	1	0.788	0.855	21.614	-0.101	-0.101	0.000	0.000	0.000	0.000
93	A	94	ALA	0	-0.009	0.001	26.221	0.004	0.004	0.000	0.000	0.000	0.000
94	A	95	VAL	0	-0.038	-0.015	29.640	0.000	0.000	0.000	0.000	0.000	0.000
95	A	96	MET	0	0.018	0.012	22.269	0.004	0.004	0.000	0.000	0.000	0.000
96	A	97	GLU	-1	-0.970	-0.981	24.641	0.103	0.103	0.000	0.000	0.000	0.000
97	A	98	LYS	1	0.876	0.934	28.052	-0.070	-0.070	0.000	0.000	0.000	0.000
98	A	99	THR	0	-0.047	-0.007	31.135	-0.008	-0.008	0.000	0.000	0.000	0.000
99	A	100	PRO	0	-0.021	0.004	31.339	0.004	0.004	0.000	0.000	0.000	0.000
100	A	101	HIS	0	-0.016	-0.012	32.596	0.003	0.003	0.000	0.000	0.000	0.000
101	A	102	VAL	0	0.077	0.028	27.840	0.003	0.003	0.000	0.000	0.000	0.000
102	A	103	MET	0	-0.048	-0.026	29.077	0.002	0.002	0.000	0.000	0.000	0.000
103	A	104	LEU	0	-0.024	0.007	31.546	-0.003	-0.003	0.000	0.000	0.000	0.000
104	A	105	VAL	0	0.014	-0.007	33.991	0.001	0.001	0.000	0.000	0.000	0.000
105	A	106	GLY	0	0.017	0.018	36.578	-0.001	-0.001	0.000	0.000	0.000	0.000
106	A	107	ASP	-1	-0.884	-0.953	39.215	0.026	0.026	0.000	0.000	0.000	0.000
107	A	108	GLY	0	0.033	0.022	39.921	0.000	0.000	0.000	0.000	0.000	0.000
108	A	109	ALA	0	-0.020	-0.008	35.319	0.002	0.002	0.000	0.000	0.000	0.000
109	A	110	LEU	0	-0.003	-0.003	36.785	0.001	0.001	0.000	0.000	0.000	0.000
110	A	111	GLU	-1	-0.940	-0.969	38.859	0.029	0.029	0.000	0.000	0.000	0.000
111	A	112	PHE	0	0.011	0.010	32.641	-0.001	-0.001	0.000	0.000	0.000	0.000
112	A	113	ALA	0	0.038	0.036	35.455	0.001	0.001	0.000	0.000	0.000	0.000
113	A	114	LEU	0	-0.007	-0.015	36.425	-0.001	-0.001	0.000	0.000	0.000	0.000
114	A	115	SER	0	-0.128	-0.071	38.221	-0.001	-0.001	0.000	0.000	0.000	0.000
115	A	116	GLN	0	-0.024	-0.026	33.862	0.003	0.003	0.000	0.000	0.000	0.000
116	A	117	GLY	0	-0.033	-0.004	35.881	0.001	0.001	0.000	0.000	0.000	0.000
117	A	118	PHE	0	-0.079	-0.021	30.878	-0.002	-0.002	0.000	0.000	0.000	0.000
118	A	119	LYS	1	0.974	0.980	36.633	-0.014	-0.014	0.000	0.000	0.000	0.000
119	A	120	LYS	1	0.953	0.986	38.463	-0.018	-0.018	0.000	0.000	0.000	0.000
120	A	121	GLU	-1	-0.976	-1.011	37.400	0.013	0.013	0.000	0.000	0.000	0.000
121	A	122	ASN	0	-0.001	-0.007	40.828	0.002	0.002	0.000	0.000	0.000	0.000
122	A	123	LEU	0	0.005	-0.002	36.019	-0.002	-0.002	0.000	0.000	0.000	0.000
123	A	124	LEU	0	0.037	0.033	39.051	-0.001	-0.001	0.000	0.000	0.000	0.000
124	A	125	THR	0	0.063	0.032	39.247	-0.001	-0.001	0.000	0.000	0.000	0.000
125	A	126	ALA	0	0.023	-0.004	42.180	0.000	0.000	0.000	0.000	0.000	0.000
126	A	127	GLU	-1	-0.885	-0.953	40.058	-0.002	-0.002	0.000	0.000	0.000	0.000
127	A	128	SER	0	-0.007	-0.013	39.056	-0.001	-0.001	0.000	0.000	0.000	0.000
128	A	129	GLU	-1	-0.873	-0.931	42.125	0.006	0.006	0.000	0.000	0.000	0.000
129	A	130	LYS	1	0.767	0.879	45.427	-0.003	-0.003	0.000	0.000	0.000	0.000
130	A	131	GLU	-1	-0.712	-0.825	40.658	0.003	0.003	0.000	0.000	0.000	0.000
131	A	132	TRP	0	-0.013	0.013	44.142	0.000	0.000	0.000	0.000	0.000	0.000
132	A	133	LYS	1	0.912	0.945	45.469	-0.005	-0.005	0.000	0.000	0.000	0.000
133	A	134	GLU	-1	-0.934	-0.961	47.418	0.002	0.002	0.000	0.000	0.000	0.000
134	A	135	TRP	0	-0.001	0.005	44.836	0.000	0.000	0.000	0.000	0.000	0.000
135	A	136	LEU	0	-0.040	-0.036	47.474	0.000	0.000	0.000	0.000	0.000	0.000
136	A	137	LYS	1	0.890	0.966	49.916	-0.004	-0.004	0.000	0.000	0.000	0.000
137	A	138	THR	0	-0.022	-0.004	48.248	0.000	0.000	0.000	0.000	0.000	0.000
138	A	139	SER	0	-0.060	-0.014	47.703	0.001	0.001	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:THR)