FMO DATABASE

FMODB ID: 5241Z

Calculation Name: 1NEU-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1NEU

Chain ID: A

ChEMBL ID:

UniProt ID: P06907

Base Structure: X-ray

Registration Date: 2023-09-19

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	OptHSide
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	118
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-986613.23798
FMO2-HF: Nuclear repulsion	939417.751191
FMO2-HF: Total energy	-47195.486789
FMO2-MP2: Total energy	-47335.029531

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:1:ILE)

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

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.
-13.541	-12.915	18.426	-6.443	-12.61	-0.041

Interaction energy analysis for fragmet #1(A:1:ILE)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.012 / q_NPA : 0.001

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	3	VAL	0	0.035	0.017	3.523	-1.766	0.952	-0.011	-1.380	-1.328	-0.001
4	A	4	TYR	0	-0.044	-0.026	5.714	-0.300	-0.300	0.000	0.000	0.000	0.000
5	A	5	THR	0	0.001	-0.007	9.495	0.093	0.093	0.000	0.000	0.000	0.000
6	A	6	ASP	-1	-0.884	-0.931	13.194	-0.103	-0.103	0.000	0.000	0.000	0.000
7	A	7	ARG	1	0.850	0.903	15.961	0.045	0.045	0.000	0.000	0.000	0.000
8	A	8	GLU	-1	-0.821	-0.895	17.308	0.031	0.031	0.000	0.000	0.000	0.000
9	A	9	VAL	0	0.006	0.007	20.367	-0.015	-0.015	0.000	0.000	0.000	0.000
10	A	10	TYR	0	-0.051	-0.040	22.974	0.005	0.005	0.000	0.000	0.000	0.000
11	A	11	GLY	0	0.035	0.017	26.716	-0.004	-0.004	0.000	0.000	0.000	0.000
12	A	12	ALA	0	-0.018	0.003	29.091	0.001	0.001	0.000	0.000	0.000	0.000
13	A	13	VAL	0	0.049	0.005	32.660	0.004	0.004	0.000	0.000	0.000	0.000
14	A	14	GLY	0	-0.044	-0.017	34.751	-0.004	-0.004	0.000	0.000	0.000	0.000
15	A	15	SER	0	-0.050	-0.014	31.827	-0.002	-0.002	0.000	0.000	0.000	0.000
16	A	16	GLN	0	-0.026	-0.009	27.656	0.007	0.007	0.000	0.000	0.000	0.000
17	A	17	VAL	0	0.009	0.005	23.587	-0.009	-0.009	0.000	0.000	0.000	0.000
18	A	18	THR	0	-0.038	-0.023	21.039	0.011	0.011	0.000	0.000	0.000	0.000
19	A	19	LEU	0	0.011	0.018	18.603	-0.010	-0.010	0.000	0.000	0.000	0.000
20	A	20	HIS	0	0.048	0.030	12.858	-0.012	-0.012	0.000	0.000	0.000	0.000
21	A	21	CYS	0	-0.022	-0.008	11.491	0.111	0.111	0.000	0.000	0.000	0.000
22	A	22	SER	0	-0.004	0.012	9.658	-0.056	-0.056	0.000	0.000	0.000	0.000
23	A	23	PHE	0	-0.016	-0.015	2.647	-1.286	-1.454	3.694	-1.186	-2.340	0.001
24	A	24	TRP	0	0.016	0.014	2.477	-1.871	-0.118	0.549	-0.539	-1.763	-0.003
25	A	25	SER	0	-0.032	-0.052	2.027	-7.773	-8.242	12.265	-7.045	-4.751	-0.041
26	A	26	SER	0	-0.041	-0.041	2.582	4.237	-0.067	0.222	5.039	-0.957	-0.004
27	A	27	GLU	-1	-0.899	-0.907	4.351	-0.783	-0.701	-0.001	-0.014	-0.067	0.000
28	A	28	TRP	0	0.008	-0.008	6.182	-0.070	-0.070	0.000	0.000	0.000	0.000
29	A	29	VAL	0	0.010	0.001	5.021	0.015	0.015	0.000	0.000	0.000	0.000
30	A	30	SER	0	-0.013	0.003	8.500	-0.011	-0.011	0.000	0.000	0.000	0.000
31	A	31	ASP	-1	-0.898	-0.959	10.702	0.206	0.206	0.000	0.000	0.000	0.000
32	A	32	ASP	-1	-0.874	-0.911	12.836	0.389	0.389	0.000	0.000	0.000	0.000
33	A	33	ILE	0	-0.072	-0.036	8.833	0.106	0.106	0.000	0.000	0.000	0.000
34	A	34	SER	0	-0.051	-0.050	11.809	-0.088	-0.088	0.000	0.000	0.000	0.000
35	A	35	PHE	0	0.017	0.002	10.027	0.190	0.190	0.000	0.000	0.000	0.000
36	A	36	THR	0	-0.025	-0.008	13.741	-0.100	-0.100	0.000	0.000	0.000	0.000
37	A	37	TRP	0	0.022	0.006	15.516	0.065	0.065	0.000	0.000	0.000	0.000
38	A	38	ARG	1	0.829	0.893	15.720	-0.508	-0.508	0.000	0.000	0.000	0.000
39	A	39	TYR	0	0.001	-0.010	20.163	0.003	0.003	0.000	0.000	0.000	0.000
40	A	40	GLN	0	-0.030	-0.008	22.665	0.021	0.021	0.000	0.000	0.000	0.000
41	A	41	PRO	0	0.023	0.022	24.806	-0.008	-0.008	0.000	0.000	0.000	0.000
42	A	42	GLU	-1	-0.858	-0.934	27.923	0.064	0.064	0.000	0.000	0.000	0.000
43	A	43	GLY	0	-0.022	-0.004	28.621	-0.004	-0.004	0.000	0.000	0.000	0.000
44	A	44	GLY	0	-0.015	0.007	28.660	-0.003	-0.003	0.000	0.000	0.000	0.000
45	A	45	ARG	1	0.891	0.920	25.901	-0.115	-0.115	0.000	0.000	0.000	0.000
46	A	46	ASP	-1	-0.922	-0.941	25.205	0.166	0.166	0.000	0.000	0.000	0.000
47	A	47	ALA	0	0.003	-0.001	21.131	-0.004	-0.004	0.000	0.000	0.000	0.000
48	A	48	ILE	0	-0.003	-0.008	23.228	0.019	0.019	0.000	0.000	0.000	0.000
49	A	49	SER	0	-0.018	-0.010	21.162	0.021	0.021	0.000	0.000	0.000	0.000
50	A	50	ILE	0	0.015	0.004	21.797	-0.020	-0.020	0.000	0.000	0.000	0.000
51	A	51	PHE	0	-0.001	-0.008	17.990	-0.021	-0.021	0.000	0.000	0.000	0.000
52	A	52	HIS	0	-0.036	-0.020	17.036	0.017	0.017	0.000	0.000	0.000	0.000
53	A	53	TYR	0	0.029	0.026	16.070	-0.047	-0.047	0.000	0.000	0.000	0.000
54	A	54	ALA	0	0.070	0.023	16.318	0.076	0.076	0.000	0.000	0.000	0.000
55	A	55	LYS	1	0.817	0.903	15.984	-0.434	-0.434	0.000	0.000	0.000	0.000
56	A	56	GLY	0	0.030	0.019	18.214	-0.028	-0.028	0.000	0.000	0.000	0.000
57	A	57	GLN	0	-0.039	-0.011	19.923	-0.033	-0.033	0.000	0.000	0.000	0.000
58	A	58	PRO	0	-0.007	-0.002	20.750	0.030	0.030	0.000	0.000	0.000	0.000
59	A	59	TYR	0	-0.028	-0.020	21.425	-0.027	-0.027	0.000	0.000	0.000	0.000
60	A	60	ILE	0	-0.005	-0.011	22.914	0.019	0.019	0.000	0.000	0.000	0.000
61	A	61	ASP	-1	-0.820	-0.893	25.302	0.140	0.140	0.000	0.000	0.000	0.000
62	A	62	GLU	-1	-0.958	-0.984	27.277	0.096	0.096	0.000	0.000	0.000	0.000
63	A	63	VAL	0	-0.076	-0.056	30.363	-0.010	-0.010	0.000	0.000	0.000	0.000
64	A	64	GLY	0	0.002	0.005	29.757	-0.006	-0.006	0.000	0.000	0.000	0.000
65	A	65	THR	0	-0.037	-0.025	28.224	-0.008	-0.008	0.000	0.000	0.000	0.000
66	A	66	PHE	0	0.024	0.014	26.391	-0.005	-0.005	0.000	0.000	0.000	0.000
67	A	67	LYS	1	0.852	0.940	28.859	-0.083	-0.083	0.000	0.000	0.000	0.000
68	A	68	GLU	-1	-0.869	-0.936	30.504	0.069	0.069	0.000	0.000	0.000	0.000
69	A	69	ARG	1	0.752	0.857	29.459	-0.086	-0.086	0.000	0.000	0.000	0.000
70	A	70	ILE	0	0.021	0.017	23.375	0.001	0.001	0.000	0.000	0.000	0.000
71	A	71	GLN	0	-0.007	0.012	24.666	-0.006	-0.006	0.000	0.000	0.000	0.000
72	A	72	TRP	0	0.007	0.002	15.444	0.011	0.011	0.000	0.000	0.000	0.000
73	A	73	VAL	0	-0.052	-0.037	19.583	-0.015	-0.015	0.000	0.000	0.000	0.000
74	A	74	GLY	0	0.044	0.045	16.548	-0.020	-0.020	0.000	0.000	0.000	0.000
75	A	75	ASP	-1	-0.843	-0.919	15.413	0.019	0.019	0.000	0.000	0.000	0.000
76	A	76	PRO	0	0.043	0.018	13.197	-0.015	-0.015	0.000	0.000	0.000	0.000
77	A	77	SER	0	-0.069	-0.049	12.503	0.006	0.006	0.000	0.000	0.000	0.000
78	A	78	TRP	0	-0.108	-0.052	12.807	-0.073	-0.073	0.000	0.000	0.000	0.000
79	A	79	LYS	1	0.837	0.925	7.170	-0.003	-0.003	0.000	0.000	0.000	0.000
80	A	80	ASP	-1	-0.794	-0.881	9.689	0.068	0.068	0.000	0.000	0.000	0.000
81	A	81	GLY	0	0.021	-0.005	12.470	0.030	0.030	0.000	0.000	0.000	0.000
82	A	82	SER	0	-0.029	-0.043	14.016	0.023	0.023	0.000	0.000	0.000	0.000
83	A	83	ILE	0	-0.027	-0.008	16.613	-0.001	-0.001	0.000	0.000	0.000	0.000
84	A	84	VAL	0	-0.021	-0.005	20.154	-0.013	-0.013	0.000	0.000	0.000	0.000
85	A	85	ILE	0	-0.003	0.012	22.925	0.011	0.011	0.000	0.000	0.000	0.000
86	A	86	HIS	0	-0.004	-0.040	25.768	-0.017	-0.017	0.000	0.000	0.000	0.000
87	A	87	ASN	0	-0.048	-0.037	29.335	0.001	0.001	0.000	0.000	0.000	0.000
88	A	88	LEU	0	0.024	0.020	27.688	0.003	0.003	0.000	0.000	0.000	0.000
89	A	89	ASP	-1	-0.780	-0.870	31.707	0.046	0.046	0.000	0.000	0.000	0.000
90	A	90	TYR	0	-0.015	-0.027	32.536	0.002	0.002	0.000	0.000	0.000	0.000
91	A	91	SER	0	-0.127	-0.076	33.257	0.003	0.003	0.000	0.000	0.000	0.000
92	A	92	ASP	-1	-0.730	-0.842	28.654	0.080	0.080	0.000	0.000	0.000	0.000
93	A	93	ASN	0	-0.011	0.000	28.016	0.007	0.007	0.000	0.000	0.000	0.000
94	A	94	GLY	0	0.023	0.003	26.112	0.006	0.006	0.000	0.000	0.000	0.000
95	A	95	THR	0	-0.043	-0.005	20.046	-0.016	-0.016	0.000	0.000	0.000	0.000
96	A	96	PHE	0	0.028	0.020	19.418	0.018	0.018	0.000	0.000	0.000	0.000
97	A	97	THR	0	-0.035	-0.030	14.837	-0.001	-0.001	0.000	0.000	0.000	0.000
98	A	99	ASP	-1	-0.831	-0.914	11.578	0.970	0.970	0.000	0.000	0.000	0.000
99	A	100	VAL	0	0.049	0.018	7.248	-0.090	-0.090	0.000	0.000	0.000	0.000
100	A	101	LYS	1	0.828	0.929	8.655	-0.388	-0.388	0.000	0.000	0.000	0.000
101	A	102	ASN	0	0.064	0.020	5.942	-0.462	-0.462	0.000	0.000	0.000	0.000
102	A	103	PRO	0	0.026	0.016	9.825	-0.115	-0.115	0.000	0.000	0.000	0.000
103	A	104	PRO	0	-0.054	-0.035	12.746	-0.065	-0.065	0.000	0.000	0.000	0.000
104	A	105	ASP	-1	-0.835	-0.895	13.808	0.566	0.566	0.000	0.000	0.000	0.000
105	A	106	ILE	0	-0.033	-0.018	12.871	-0.013	-0.013	0.000	0.000	0.000	0.000
106	A	107	VAL	0	-0.026	-0.025	10.505	0.090	0.090	0.000	0.000	0.000	0.000
107	A	108	GLY	0	0.038	0.034	9.361	0.169	0.169	0.000	0.000	0.000	0.000
108	A	109	LYS	1	0.834	0.927	2.173	-4.728	-3.714	1.708	-1.318	-1.404	0.007
109	A	110	THR	0	-0.005	-0.015	7.934	-0.083	-0.083	0.000	0.000	0.000	0.000
110	A	111	SER	0	-0.023	0.015	10.157	-0.066	-0.066	0.000	0.000	0.000	0.000
111	A	112	GLN	0	-0.039	-0.029	12.202	-0.001	-0.001	0.000	0.000	0.000	0.000
112	A	113	VAL	0	0.059	0.057	15.658	-0.035	-0.035	0.000	0.000	0.000	0.000
113	A	114	THR	0	-0.050	-0.033	18.172	0.019	0.019	0.000	0.000	0.000	0.000
114	A	115	LEU	0	-0.024	-0.006	21.822	-0.017	-0.017	0.000	0.000	0.000	0.000
115	A	116	TYR	0	-0.029	-0.030	24.078	0.007	0.007	0.000	0.000	0.000	0.000
116	A	117	VAL	0	-0.003	0.010	28.040	-0.006	-0.006	0.000	0.000	0.000	0.000
117	A	118	PHE	0	-0.044	-0.028	29.026	0.000	0.000	0.000	0.000	0.000	0.000
118	A	119	GLU	-1	-0.935	-0.967	33.880	0.008	0.008	0.000	0.000	0.000	0.000

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