FMO DATABASE

FMODB ID: MVY1Z

Calculation Name: 1A68-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1A68

Chain ID: A

ChEMBL ID:

UniProt ID: Q16968

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:

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptAll
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	87
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-669134.509521
FMO2-HF: Nuclear repulsion	633481.782635
FMO2-HF: Total energy	-35652.726886
FMO2-MP2: Total energy	-35760.169118

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:66:GLU)

Summations of interaction energy for fragment #1(A:66:GLU)

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.
-205.177	-215.181	42.814	-17.943	-14.864	0.2

Interaction energy analysis for fragmet #1(A:66:GLU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : -1 / q_Mulliken : -0.744 / q_NPA : -0.849

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	68	VAL	0	0.001	0.003	3.859	-3.191	-1.507	-0.018	-0.839	-0.827	0.001
4	A	69	VAL	0	0.050	0.028	6.581	-0.549	-0.549	0.000	0.000	0.000	0.000
5	A	70	ILE	0	-0.014	-0.011	10.021	-0.540	-0.540	0.000	0.000	0.000	0.000
6	A	71	ASN	0	-0.044	-0.037	13.161	-0.780	-0.780	0.000	0.000	0.000	0.000
7	A	72	VAL	0	0.044	0.021	16.541	-0.327	-0.327	0.000	0.000	0.000	0.000
8	A	73	SER	0	0.026	-0.033	19.841	-0.185	-0.185	0.000	0.000	0.000	0.000
9	A	74	GLY	0	-0.017	0.003	20.915	-0.578	-0.578	0.000	0.000	0.000	0.000
10	A	75	LEU	0	-0.048	-0.012	19.007	0.069	0.069	0.000	0.000	0.000	0.000
11	A	76	ARG	1	0.802	0.866	14.898	-15.460	-15.460	0.000	0.000	0.000	0.000
12	A	77	PHE	0	0.016	0.013	13.562	-0.295	-0.295	0.000	0.000	0.000	0.000
13	A	78	GLU	-1	-0.848	-0.910	8.697	26.946	26.946	0.000	0.000	0.000	0.000
14	A	79	THR	0	-0.001	-0.003	7.618	0.289	0.289	0.000	0.000	0.000	0.000
15	A	80	GLN	0	-0.023	-0.023	1.777	-22.096	-26.578	13.403	-4.755	-4.165	0.052
16	A	81	LEU	0	0.016	0.002	3.608	-5.835	-5.096	0.009	-0.254	-0.493	0.001
17	A	82	LYS	1	0.825	0.881	1.791	-154.993	-162.976	29.421	-12.094	-9.344	0.146
18	A	83	THR	0	0.028	0.021	5.372	-4.433	-4.395	-0.001	-0.001	-0.035	0.000
19	A	84	LEU	0	0.022	0.017	7.903	-3.851	-3.851	0.000	0.000	0.000	0.000
20	A	85	ASN	0	0.014	-0.006	8.183	-4.534	-4.534	0.000	0.000	0.000	0.000
21	A	86	GLN	0	-0.075	-0.034	9.735	-1.805	-1.805	0.000	0.000	0.000	0.000
22	A	87	PHE	0	0.002	0.026	11.874	-1.451	-1.451	0.000	0.000	0.000	0.000
23	A	88	PRO	0	0.010	0.019	14.238	-0.503	-0.503	0.000	0.000	0.000	0.000
24	A	89	ASP	-1	-0.846	-0.925	15.786	16.413	16.413	0.000	0.000	0.000	0.000
25	A	90	THR	0	-0.012	0.006	16.476	-0.447	-0.447	0.000	0.000	0.000	0.000
26	A	91	LEU	0	0.024	0.019	17.260	0.946	0.946	0.000	0.000	0.000	0.000
27	A	92	LEU	0	0.005	-0.006	13.732	0.583	0.583	0.000	0.000	0.000	0.000
28	A	93	GLY	0	0.058	0.042	12.621	2.339	2.339	0.000	0.000	0.000	0.000
29	A	94	ASN	0	-0.016	-0.012	13.055	1.164	1.164	0.000	0.000	0.000	0.000
30	A	95	PRO	0	0.000	-0.015	11.751	-0.451	-0.451	0.000	0.000	0.000	0.000
31	A	96	GLN	0	-0.008	0.001	13.560	-0.538	-0.538	0.000	0.000	0.000	0.000
32	A	97	LYS	1	0.762	0.873	16.973	-15.558	-15.558	0.000	0.000	0.000	0.000
33	A	98	ARG	1	0.836	0.910	9.619	-27.501	-27.501	0.000	0.000	0.000	0.000
34	A	99	ASN	0	0.044	0.012	12.243	0.467	0.467	0.000	0.000	0.000	0.000
35	A	100	ARG	1	0.909	0.973	14.924	-13.219	-13.219	0.000	0.000	0.000	0.000
36	A	101	TYR	0	-0.008	-0.003	16.539	-1.048	-1.048	0.000	0.000	0.000	0.000
37	A	102	TYR	0	-0.045	-0.026	9.861	0.004	0.004	0.000	0.000	0.000	0.000
38	A	103	ASP	-1	-0.789	-0.873	14.004	13.848	13.848	0.000	0.000	0.000	0.000
39	A	104	PRO	0	0.008	-0.012	13.263	0.785	0.785	0.000	0.000	0.000	0.000
40	A	105	LEU	0	-0.067	-0.016	14.353	0.007	0.007	0.000	0.000	0.000	0.000
41	A	106	ARG	1	0.858	0.898	15.112	-13.676	-13.676	0.000	0.000	0.000	0.000
42	A	107	ASN	0	-0.031	0.013	7.521	0.748	0.748	0.000	0.000	0.000	0.000
43	A	108	GLU	-1	-0.743	-0.831	10.022	18.277	18.277	0.000	0.000	0.000	0.000
44	A	109	TYR	0	-0.026	-0.027	8.869	0.080	0.080	0.000	0.000	0.000	0.000
45	A	110	PHE	0	-0.039	-0.016	13.678	-0.029	-0.029	0.000	0.000	0.000	0.000
46	A	111	PHE	0	0.016	-0.008	15.286	-0.291	-0.291	0.000	0.000	0.000	0.000
47	A	112	ASP	-1	-0.869	-0.903	20.161	11.542	11.542	0.000	0.000	0.000	0.000
48	A	113	ARG	1	0.847	0.907	22.299	-12.718	-12.718	0.000	0.000	0.000	0.000
49	A	114	ASN	0	0.028	0.019	24.550	0.258	0.258	0.000	0.000	0.000	0.000
50	A	115	ARG	1	0.916	0.958	22.302	-12.119	-12.119	0.000	0.000	0.000	0.000
51	A	116	PRO	0	0.000	-0.003	22.274	0.461	0.461	0.000	0.000	0.000	0.000
52	A	117	SER	0	0.026	0.000	23.668	-0.085	-0.085	0.000	0.000	0.000	0.000
53	A	118	PHE	0	0.011	0.001	14.888	0.425	0.425	0.000	0.000	0.000	0.000
54	A	119	ASP	-1	-0.857	-0.924	18.003	16.027	16.027	0.000	0.000	0.000	0.000
55	A	120	ALA	0	-0.017	-0.014	18.022	0.760	0.760	0.000	0.000	0.000	0.000
56	A	121	ILE	0	-0.046	-0.010	17.580	0.282	0.282	0.000	0.000	0.000	0.000
57	A	122	LEU	0	0.012	0.005	11.518	1.038	1.038	0.000	0.000	0.000	0.000
58	A	123	TYR	0	0.036	0.018	14.485	0.958	0.958	0.000	0.000	0.000	0.000
59	A	124	PHE	0	-0.004	0.028	16.201	0.269	0.269	0.000	0.000	0.000	0.000
60	A	125	TYR	0	0.021	-0.012	11.868	0.283	0.283	0.000	0.000	0.000	0.000
61	A	126	GLN	0	-0.036	-0.030	10.377	-0.212	-0.212	0.000	0.000	0.000	0.000
62	A	127	SER	0	-0.077	-0.049	12.690	-0.261	-0.261	0.000	0.000	0.000	0.000
63	A	128	GLY	0	0.024	0.019	14.247	-0.901	-0.901	0.000	0.000	0.000	0.000
64	A	129	GLY	0	0.063	0.029	15.396	-0.805	-0.805	0.000	0.000	0.000	0.000
65	A	130	ARG	1	0.853	0.929	18.477	-15.926	-15.926	0.000	0.000	0.000	0.000
66	A	131	LEU	0	0.045	0.027	20.610	-0.002	-0.002	0.000	0.000	0.000	0.000
67	A	132	ARG	1	0.873	0.917	22.106	-13.114	-13.114	0.000	0.000	0.000	0.000
68	A	133	ARG	1	0.907	0.949	24.359	-9.752	-9.752	0.000	0.000	0.000	0.000
69	A	134	PRO	0	0.028	0.023	24.174	-0.235	-0.235	0.000	0.000	0.000	0.000
70	A	135	VAL	0	-0.004	-0.003	26.895	-0.310	-0.310	0.000	0.000	0.000	0.000
71	A	136	ASN	0	0.006	0.000	27.091	-0.235	-0.235	0.000	0.000	0.000	0.000
72	A	137	VAL	0	0.009	0.016	26.701	-0.106	-0.106	0.000	0.000	0.000	0.000
73	A	138	PRO	0	0.029	0.027	30.080	-0.023	-0.023	0.000	0.000	0.000	0.000
74	A	139	LEU	0	0.003	0.001	31.272	0.331	0.331	0.000	0.000	0.000	0.000
75	A	140	ASP	-1	-0.822	-0.921	31.629	9.489	9.489	0.000	0.000	0.000	0.000
76	A	141	VAL	0	0.028	0.005	28.720	0.260	0.260	0.000	0.000	0.000	0.000
77	A	142	PHE	0	0.001	-0.009	23.570	0.335	0.335	0.000	0.000	0.000	0.000
78	A	143	SER	0	-0.023	-0.031	27.143	0.450	0.450	0.000	0.000	0.000	0.000
79	A	144	GLU	-1	-0.797	-0.861	28.648	10.280	10.280	0.000	0.000	0.000	0.000
80	A	145	GLU	-1	-0.815	-0.875	24.040	13.005	13.005	0.000	0.000	0.000	0.000
81	A	146	ILE	0	-0.025	-0.015	23.846	0.525	0.525	0.000	0.000	0.000	0.000
82	A	147	LYS	1	0.811	0.884	24.210	-9.741	-9.741	0.000	0.000	0.000	0.000
83	A	148	PHE	0	-0.025	-0.001	20.727	0.135	0.135	0.000	0.000	0.000	0.000
84	A	149	TYR	0	-0.006	-0.040	19.042	0.618	0.618	0.000	0.000	0.000	0.000
85	A	150	GLU	-1	-0.814	-0.896	20.278	15.365	15.365	0.000	0.000	0.000	0.000
86	A	151	LEU	0	-0.046	-0.016	18.556	0.004	0.004	0.000	0.000	0.000	0.000
87	A	152	GLY	0	-0.048	-0.004	21.563	-0.533	-0.533	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:66:GLU)