FMO DATABASE

FMODB ID: 3Q6ML

Calculation Name: 1AY9-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1AY9

Chain ID: A

ChEMBL ID:

UniProt ID: P0AG11

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:

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	108
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-722775.158472
FMO2-HF: Nuclear repulsion	681945.850335
FMO2-HF: Total energy	-40829.308137
FMO2-MP2: Total energy	-40948.371165

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:32:ASP)

Summations of interaction energy for fragment #1(A:32:ASP)

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.
31.016	33.866	0.027	-1.322	-1.554	0.005

Interaction energy analysis for fragmet #1(A:32:ASP)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : -1 / q_Mulliken : -0.937 / q_NPA : -0.973

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	34	VAL	0	0.026	0.013	3.701	5.164	7.984	0.028	-1.319	-1.528	0.005
4	A	35	GLU	-1	-0.895	-0.958	5.578	19.857	19.887	-0.001	-0.003	-0.026	0.000
5	A	36	GLN	0	-0.029	-0.016	8.889	-1.914	-1.914	0.000	0.000	0.000	0.000
6	A	37	ARG	1	0.885	0.939	11.719	-22.673	-22.673	0.000	0.000	0.000	0.000
7	A	38	ILE	0	0.006	0.008	14.119	-0.474	-0.474	0.000	0.000	0.000	0.000
8	A	39	ASP	-1	-0.840	-0.930	17.690	14.425	14.425	0.000	0.000	0.000	0.000
9	A	40	LEU	0	0.002	-0.019	20.223	-0.254	-0.254	0.000	0.000	0.000	0.000
10	A	41	ASN	0	-0.002	0.006	23.769	-0.854	-0.854	0.000	0.000	0.000	0.000
11	A	42	GLN	0	-0.010	0.003	18.923	-0.209	-0.209	0.000	0.000	0.000	0.000
12	A	43	LEU	0	-0.038	-0.010	21.903	-0.206	-0.206	0.000	0.000	0.000	0.000
13	A	44	LEU	0	-0.043	-0.026	24.279	-0.379	-0.379	0.000	0.000	0.000	0.000
14	A	45	ILE	0	0.015	0.018	27.483	-0.468	-0.468	0.000	0.000	0.000	0.000
15	A	46	GLN	0	0.014	0.021	28.290	0.057	0.057	0.000	0.000	0.000	0.000
16	A	47	HIS	1	0.826	0.891	30.563	-9.085	-9.085	0.000	0.000	0.000	0.000
17	A	48	PRO	0	0.045	0.025	29.319	-0.293	-0.293	0.000	0.000	0.000	0.000
18	A	49	SER	0	-0.006	-0.017	31.469	-0.047	-0.047	0.000	0.000	0.000	0.000
19	A	50	ALA	0	-0.015	0.007	34.375	-0.246	-0.246	0.000	0.000	0.000	0.000
20	A	51	THR	0	-0.004	0.002	32.759	-0.141	-0.141	0.000	0.000	0.000	0.000
21	A	52	TYR	0	-0.037	-0.014	35.148	0.074	0.074	0.000	0.000	0.000	0.000
22	A	53	PHE	0	-0.032	-0.016	34.867	0.065	0.065	0.000	0.000	0.000	0.000
23	A	54	VAL	0	0.038	0.022	37.024	-0.150	-0.150	0.000	0.000	0.000	0.000
24	A	55	LYS	1	0.910	0.965	39.402	-7.727	-7.727	0.000	0.000	0.000	0.000
25	A	56	ALA	0	0.017	0.009	41.128	-0.189	-0.189	0.000	0.000	0.000	0.000
26	A	57	SER	0	-0.014	-0.017	43.229	-0.031	-0.031	0.000	0.000	0.000	0.000
27	A	58	GLY	0	0.002	0.008	46.640	-0.083	-0.083	0.000	0.000	0.000	0.000
28	A	59	ASP	-1	-0.860	-0.949	47.215	6.490	6.490	0.000	0.000	0.000	0.000
29	A	60	SER	0	-0.020	0.002	48.847	-0.016	-0.016	0.000	0.000	0.000	0.000
30	A	61	MET	0	-0.013	-0.001	45.560	-0.107	-0.107	0.000	0.000	0.000	0.000
31	A	62	ILE	0	0.031	0.023	45.202	0.174	0.174	0.000	0.000	0.000	0.000
32	A	63	ASP	-1	-0.917	-0.945	44.894	6.686	6.686	0.000	0.000	0.000	0.000
33	A	64	GLY	0	-0.049	-0.047	44.269	0.088	0.088	0.000	0.000	0.000	0.000
34	A	65	GLY	0	-0.063	-0.023	40.774	0.209	0.209	0.000	0.000	0.000	0.000
35	A	66	ILE	0	-0.028	-0.014	40.333	0.217	0.217	0.000	0.000	0.000	0.000
36	A	67	SER	0	-0.009	-0.027	41.448	-0.178	-0.178	0.000	0.000	0.000	0.000
37	A	68	ASP	-1	-0.856	-0.917	42.412	7.036	7.036	0.000	0.000	0.000	0.000
38	A	69	GLY	0	-0.010	-0.006	41.551	0.089	0.089	0.000	0.000	0.000	0.000
39	A	70	ASP	-1	-0.850	-0.924	38.088	8.350	8.350	0.000	0.000	0.000	0.000
40	A	71	LEU	0	-0.060	-0.030	33.378	-0.156	-0.156	0.000	0.000	0.000	0.000
41	A	72	LEU	0	0.006	0.004	36.399	0.141	0.141	0.000	0.000	0.000	0.000
42	A	73	ILE	0	0.006	0.004	31.346	-0.011	-0.011	0.000	0.000	0.000	0.000
43	A	74	VAL	0	-0.003	-0.012	35.519	-0.059	-0.059	0.000	0.000	0.000	0.000
44	A	75	ASP	-1	-0.739	-0.855	35.622	9.089	9.089	0.000	0.000	0.000	0.000
45	A	76	SER	0	-0.009	-0.028	37.573	-0.227	-0.227	0.000	0.000	0.000	0.000
46	A	77	ALA	0	-0.045	-0.015	37.428	-0.162	-0.162	0.000	0.000	0.000	0.000
47	A	78	ILE	0	-0.068	-0.028	37.354	0.035	0.035	0.000	0.000	0.000	0.000
48	A	79	THR	0	-0.019	-0.015	40.409	-0.165	-0.165	0.000	0.000	0.000	0.000
49	A	80	ALA	0	0.040	0.027	43.611	0.064	0.064	0.000	0.000	0.000	0.000
50	A	81	SER	0	-0.007	0.003	44.341	-0.182	-0.182	0.000	0.000	0.000	0.000
51	A	82	HIS	0	-0.037	-0.032	46.337	-0.059	-0.059	0.000	0.000	0.000	0.000
52	A	83	GLY	0	-0.037	-0.023	46.236	0.094	0.094	0.000	0.000	0.000	0.000
53	A	84	ASP	-1	-0.844	-0.914	42.523	7.667	7.667	0.000	0.000	0.000	0.000
54	A	85	ILE	0	-0.025	-0.020	42.224	-0.198	-0.198	0.000	0.000	0.000	0.000
55	A	86	VAL	0	-0.006	-0.008	42.970	0.176	0.176	0.000	0.000	0.000	0.000
56	A	87	ILE	0	0.014	0.014	42.178	-0.088	-0.088	0.000	0.000	0.000	0.000
57	A	88	ALA	0	0.001	-0.020	45.698	0.021	0.021	0.000	0.000	0.000	0.000
58	A	89	ALA	0	-0.021	-0.016	49.264	0.013	0.013	0.000	0.000	0.000	0.000
59	A	90	VAL	0	0.013	-0.004	52.346	-0.012	-0.012	0.000	0.000	0.000	0.000
60	A	91	ASP	-1	-0.813	-0.908	55.690	5.336	5.336	0.000	0.000	0.000	0.000
61	A	92	GLY	0	-0.057	-0.025	55.896	-0.041	-0.041	0.000	0.000	0.000	0.000
62	A	93	GLU	-1	-0.962	-0.968	54.579	5.622	5.622	0.000	0.000	0.000	0.000
63	A	94	PHE	0	-0.029	-0.017	48.601	0.046	0.046	0.000	0.000	0.000	0.000
64	A	95	THR	0	-0.043	-0.030	49.706	-0.051	-0.051	0.000	0.000	0.000	0.000
65	A	96	VAL	0	-0.008	0.012	43.912	0.080	0.080	0.000	0.000	0.000	0.000
66	A	97	LYS	1	0.886	0.937	46.965	-6.430	-6.430	0.000	0.000	0.000	0.000
67	A	98	LYS	1	0.952	0.989	46.271	-6.597	-6.597	0.000	0.000	0.000	0.000
68	A	99	LEU	0	0.020	0.022	47.841	-0.179	-0.179	0.000	0.000	0.000	0.000
69	A	100	GLN	0	0.017	0.013	49.600	0.185	0.185	0.000	0.000	0.000	0.000
70	A	101	LEU	0	0.026	0.014	49.996	-0.080	-0.080	0.000	0.000	0.000	0.000
71	A	102	ARG	1	0.929	0.989	49.643	-6.325	-6.325	0.000	0.000	0.000	0.000
72	A	103	PRO	0	-0.031	-0.044	54.905	0.097	0.097	0.000	0.000	0.000	0.000
73	A	104	THR	0	0.031	0.005	57.815	-0.048	-0.048	0.000	0.000	0.000	0.000
74	A	105	VAL	0	0.027	0.010	54.526	0.089	0.089	0.000	0.000	0.000	0.000
75	A	106	GLN	0	-0.014	-0.018	54.936	-0.136	-0.136	0.000	0.000	0.000	0.000
76	A	107	LEU	0	0.021	0.031	50.951	0.153	0.153	0.000	0.000	0.000	0.000
77	A	108	ILE	0	-0.038	-0.021	51.157	-0.112	-0.112	0.000	0.000	0.000	0.000
78	A	109	PRO	0	0.024	0.000	50.622	0.171	0.171	0.000	0.000	0.000	0.000
79	A	110	MET	0	-0.051	-0.022	45.536	0.057	0.057	0.000	0.000	0.000	0.000
80	A	111	ASN	0	0.069	0.019	49.021	0.001	0.001	0.000	0.000	0.000	0.000
81	A	112	SER	0	0.015	0.007	51.787	-0.054	-0.054	0.000	0.000	0.000	0.000
82	A	113	ALA	0	-0.044	-0.009	54.913	-0.117	-0.117	0.000	0.000	0.000	0.000
83	A	114	TYR	0	-0.042	-0.013	53.392	-0.082	-0.082	0.000	0.000	0.000	0.000
84	A	115	SER	0	-0.009	-0.015	56.289	-0.026	-0.026	0.000	0.000	0.000	0.000
85	A	116	PRO	0	-0.061	-0.038	56.154	0.066	0.066	0.000	0.000	0.000	0.000
86	A	117	ILE	0	0.052	0.048	55.111	-0.084	-0.084	0.000	0.000	0.000	0.000
87	A	118	THR	0	-0.032	-0.025	57.196	0.064	0.064	0.000	0.000	0.000	0.000
88	A	119	ILE	0	0.003	0.012	55.844	0.005	0.005	0.000	0.000	0.000	0.000
89	A	120	SER	0	-0.039	-0.014	59.241	0.018	0.018	0.000	0.000	0.000	0.000
90	A	121	SER	0	-0.032	-0.031	61.975	0.050	0.050	0.000	0.000	0.000	0.000
91	A	122	GLU	-1	-0.976	-0.986	64.103	4.899	4.899	0.000	0.000	0.000	0.000
92	A	123	ASP	-1	-0.853	-0.900	60.184	5.200	5.200	0.000	0.000	0.000	0.000
93	A	124	THR	0	-0.073	-0.038	57.677	0.036	0.036	0.000	0.000	0.000	0.000
94	A	125	LEU	0	-0.034	-0.017	52.336	0.059	0.059	0.000	0.000	0.000	0.000
95	A	126	ASP	-1	-0.903	-0.954	51.634	6.168	6.168	0.000	0.000	0.000	0.000
96	A	127	VAL	0	-0.034	-0.011	46.253	0.071	0.071	0.000	0.000	0.000	0.000
97	A	128	PHE	0	0.028	-0.001	45.194	0.049	0.049	0.000	0.000	0.000	0.000
98	A	129	GLY	0	0.004	-0.014	42.042	0.183	0.183	0.000	0.000	0.000	0.000
99	A	130	VAL	0	-0.019	0.002	39.969	-0.164	-0.164	0.000	0.000	0.000	0.000
100	A	131	VAL	0	-0.029	-0.011	38.528	0.222	0.222	0.000	0.000	0.000	0.000
101	A	132	ILE	0	-0.022	-0.009	32.974	-0.058	-0.058	0.000	0.000	0.000	0.000
102	A	133	HIS	0	-0.021	-0.009	30.754	0.070	0.070	0.000	0.000	0.000	0.000
103	A	134	VAL	0	0.020	0.009	34.688	-0.180	-0.180	0.000	0.000	0.000	0.000
104	A	135	VAL	0	-0.031	-0.015	31.423	0.277	0.277	0.000	0.000	0.000	0.000
105	A	136	LYS	1	0.891	0.951	33.759	-8.319	-8.319	0.000	0.000	0.000	0.000
106	A	137	ALA	0	-0.008	0.000	33.279	0.317	0.317	0.000	0.000	0.000	0.000
107	A	138	MET	0	0.013	-0.007	32.277	-0.157	-0.157	0.000	0.000	0.000	0.000
108	A	139	ARG	1	0.954	0.991	30.588	-8.573	-8.573	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:32:ASP)