FMO DATABASE

FMODB ID: 4951N

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

Total energy (hartree)

FMO2-HF: Electronic energy	-984872.17356
FMO2-HF: Nuclear repulsion	937677.278191
FMO2-HF: Total energy	-47194.895369
FMO2-MP2: Total energy	-47334.448928

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.
-0.745	-19.732	38.08	-4.206	-14.885	-0.04

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 : -0.023 / q_NPA : 0.013

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	0.021	0.009	3.835	-1.944	0.975	-0.019	-1.531	-1.369	0.000
4	A	4	TYR	0	-0.015	-0.007	5.063	-0.266	-0.266	0.000	0.000	0.000	0.000
5	A	5	THR	0	0.028	0.025	9.591	0.136	0.136	0.000	0.000	0.000	0.000
6	A	6	ASP	-1	-0.897	-0.929	13.398	-0.220	-0.220	0.000	0.000	0.000	0.000
7	A	7	ARG	1	0.914	0.941	16.205	0.117	0.117	0.000	0.000	0.000	0.000
8	A	8	GLU	-1	-0.905	-0.972	17.704	-0.008	-0.008	0.000	0.000	0.000	0.000
9	A	9	VAL	0	0.007	0.013	20.744	-0.018	-0.018	0.000	0.000	0.000	0.000
10	A	10	TYR	0	-0.037	-0.026	23.253	0.009	0.009	0.000	0.000	0.000	0.000
11	A	11	GLY	0	0.025	0.011	26.970	-0.005	-0.005	0.000	0.000	0.000	0.000
12	A	12	ALA	0	-0.018	0.002	29.191	0.002	0.002	0.000	0.000	0.000	0.000
13	A	13	VAL	0	0.054	0.006	32.562	0.003	0.003	0.000	0.000	0.000	0.000
14	A	14	GLY	0	-0.032	-0.013	34.659	-0.004	-0.004	0.000	0.000	0.000	0.000
15	A	15	SER	0	-0.056	-0.014	31.745	-0.002	-0.002	0.000	0.000	0.000	0.000
16	A	16	GLN	0	-0.016	-0.010	26.978	0.007	0.007	0.000	0.000	0.000	0.000
17	A	17	VAL	0	0.005	0.005	23.494	-0.010	-0.010	0.000	0.000	0.000	0.000
18	A	18	THR	0	-0.057	-0.026	20.468	0.010	0.010	0.000	0.000	0.000	0.000
19	A	19	LEU	0	0.027	0.019	18.506	-0.013	-0.013	0.000	0.000	0.000	0.000
20	A	20	HIS	0	0.094	0.060	12.406	-0.027	-0.027	0.000	0.000	0.000	0.000
21	A	21	CYS	0	-0.043	-0.023	11.265	0.108	0.108	0.000	0.000	0.000	0.000
22	A	22	SER	0	-0.018	-0.010	9.582	-0.056	-0.056	0.000	0.000	0.000	0.000
23	A	23	PHE	0	0.005	-0.002	2.649	-2.129	-1.952	3.419	-1.245	-2.350	0.001
24	A	24	TRP	0	0.013	0.009	2.453	-2.130	-0.157	1.298	-0.788	-2.483	-0.003
25	A	25	SER	0	0.000	-0.049	1.796	-1.076	-14.377	33.039	-12.940	-6.797	-0.030
26	A	26	SER	0	-0.061	-0.037	2.515	11.483	-0.139	0.173	12.518	-1.070	-0.009
27	A	27	GLU	-1	-0.899	-0.910	4.499	-0.662	-0.566	-0.001	-0.018	-0.076	0.000
28	A	28	TRP	0	-0.013	-0.022	6.483	-0.071	-0.071	0.000	0.000	0.000	0.000
29	A	29	VAL	0	-0.009	-0.010	4.945	0.038	0.038	0.000	0.000	0.000	0.000
30	A	30	SER	0	-0.041	-0.023	8.476	-0.024	-0.024	0.000	0.000	0.000	0.000
31	A	31	ASP	-1	-0.890	-0.952	10.702	0.216	0.216	0.000	0.000	0.000	0.000
32	A	32	ASP	-1	-0.892	-0.907	12.828	0.416	0.416	0.000	0.000	0.000	0.000
33	A	33	ILE	0	-0.050	-0.020	8.983	0.119	0.119	0.000	0.000	0.000	0.000
34	A	34	SER	0	-0.055	-0.047	11.779	-0.099	-0.099	0.000	0.000	0.000	0.000
35	A	35	PHE	0	0.015	0.004	9.968	0.187	0.187	0.000	0.000	0.000	0.000
36	A	36	THR	0	-0.036	-0.011	13.658	-0.087	-0.087	0.000	0.000	0.000	0.000
37	A	37	TRP	0	0.030	0.017	15.413	0.060	0.060	0.000	0.000	0.000	0.000
38	A	38	ARG	1	0.862	0.929	16.202	-0.458	-0.458	0.000	0.000	0.000	0.000
39	A	39	TYR	0	-0.002	-0.013	20.095	-0.003	-0.003	0.000	0.000	0.000	0.000
40	A	40	GLN	0	0.006	0.013	22.881	0.023	0.023	0.000	0.000	0.000	0.000
41	A	41	PRO	0	0.013	0.018	24.815	-0.011	-0.011	0.000	0.000	0.000	0.000
42	A	42	GLU	-1	-0.869	-0.953	27.991	0.042	0.042	0.000	0.000	0.000	0.000
43	A	43	GLY	0	-0.028	-0.005	28.642	-0.002	-0.002	0.000	0.000	0.000	0.000
44	A	44	GLY	0	-0.028	-0.002	28.839	0.000	0.000	0.000	0.000	0.000	0.000
45	A	45	ARG	1	0.870	0.907	26.085	-0.108	-0.108	0.000	0.000	0.000	0.000
46	A	46	ASP	-1	-0.887	-0.916	25.397	0.162	0.162	0.000	0.000	0.000	0.000
47	A	47	ALA	0	-0.019	-0.018	21.205	-0.006	-0.006	0.000	0.000	0.000	0.000
48	A	48	ILE	0	-0.001	-0.004	23.228	0.022	0.022	0.000	0.000	0.000	0.000
49	A	49	SER	0	-0.029	-0.016	21.518	0.017	0.017	0.000	0.000	0.000	0.000
50	A	50	ILE	0	0.025	0.004	21.570	-0.018	-0.018	0.000	0.000	0.000	0.000
51	A	51	PHE	0	0.000	-0.006	17.839	-0.022	-0.022	0.000	0.000	0.000	0.000
52	A	52	HIS	0	-0.036	-0.022	17.048	0.025	0.025	0.000	0.000	0.000	0.000
53	A	53	TYR	0	0.044	0.030	15.827	-0.046	-0.046	0.000	0.000	0.000	0.000
54	A	54	ALA	0	0.073	0.019	16.254	0.079	0.079	0.000	0.000	0.000	0.000
55	A	55	LYS	1	0.826	0.901	16.701	-0.419	-0.419	0.000	0.000	0.000	0.000
56	A	56	GLY	0	0.026	0.018	18.181	-0.028	-0.028	0.000	0.000	0.000	0.000
57	A	57	GLN	0	-0.032	-0.003	19.891	-0.033	-0.033	0.000	0.000	0.000	0.000
58	A	58	PRO	0	0.007	-0.003	20.692	0.030	0.030	0.000	0.000	0.000	0.000
59	A	59	TYR	0	-0.042	-0.024	21.242	-0.024	-0.024	0.000	0.000	0.000	0.000
60	A	60	ILE	0	0.006	-0.004	22.830	0.017	0.017	0.000	0.000	0.000	0.000
61	A	61	ASP	-1	-0.829	-0.896	25.216	0.130	0.130	0.000	0.000	0.000	0.000
62	A	62	GLU	-1	-0.953	-0.985	27.184	0.086	0.086	0.000	0.000	0.000	0.000
63	A	63	VAL	0	-0.059	-0.045	30.276	-0.010	-0.010	0.000	0.000	0.000	0.000
64	A	64	GLY	0	-0.010	-0.003	29.652	-0.006	-0.006	0.000	0.000	0.000	0.000
65	A	65	THR	0	-0.059	-0.032	28.198	-0.009	-0.009	0.000	0.000	0.000	0.000
66	A	66	PHE	0	0.035	0.015	26.399	-0.006	-0.006	0.000	0.000	0.000	0.000
67	A	67	LYS	1	0.968	1.011	28.759	-0.073	-0.073	0.000	0.000	0.000	0.000
68	A	68	GLU	-1	-0.984	-1.007	30.420	0.052	0.052	0.000	0.000	0.000	0.000
69	A	69	ARG	1	0.756	0.876	29.526	-0.064	-0.064	0.000	0.000	0.000	0.000
70	A	70	ILE	0	0.024	0.020	23.345	-0.002	-0.002	0.000	0.000	0.000	0.000
71	A	71	GLN	0	-0.012	0.006	24.445	-0.004	-0.004	0.000	0.000	0.000	0.000
72	A	72	TRP	0	-0.019	-0.006	15.459	0.005	0.005	0.000	0.000	0.000	0.000
73	A	73	VAL	0	-0.048	-0.034	19.454	-0.012	-0.012	0.000	0.000	0.000	0.000
74	A	74	GLY	0	0.043	0.043	16.480	-0.023	-0.023	0.000	0.000	0.000	0.000
75	A	75	ASP	-1	-0.874	-0.957	15.364	-0.013	-0.013	0.000	0.000	0.000	0.000
76	A	76	PRO	0	0.029	0.009	13.178	-0.026	-0.026	0.000	0.000	0.000	0.000
77	A	77	SER	0	-0.020	-0.003	12.489	0.004	0.004	0.000	0.000	0.000	0.000
78	A	78	TRP	0	-0.119	-0.057	12.798	-0.072	-0.072	0.000	0.000	0.000	0.000
79	A	79	LYS	1	0.878	0.953	6.801	0.165	0.165	0.000	0.000	0.000	0.000
80	A	80	ASP	-1	-0.830	-0.917	9.637	-0.073	-0.073	0.000	0.000	0.000	0.000
81	A	81	GLY	0	0.024	-0.009	12.414	0.049	0.049	0.000	0.000	0.000	0.000
82	A	82	SER	0	-0.015	-0.014	13.940	0.028	0.028	0.000	0.000	0.000	0.000
83	A	83	ILE	0	-0.024	-0.007	16.531	0.009	0.009	0.000	0.000	0.000	0.000
84	A	84	VAL	0	-0.010	0.003	20.066	-0.017	-0.017	0.000	0.000	0.000	0.000
85	A	85	ILE	0	-0.008	0.012	23.091	0.014	0.014	0.000	0.000	0.000	0.000
86	A	86	HIS	0	-0.006	-0.039	25.670	-0.017	-0.017	0.000	0.000	0.000	0.000
87	A	87	ASN	0	-0.040	-0.033	29.240	0.002	0.002	0.000	0.000	0.000	0.000
88	A	88	LEU	0	0.008	0.012	27.588	0.004	0.004	0.000	0.000	0.000	0.000
89	A	89	ASP	-1	-0.810	-0.889	31.605	0.030	0.030	0.000	0.000	0.000	0.000
90	A	90	TYR	0	-0.005	-0.023	32.428	0.001	0.001	0.000	0.000	0.000	0.000
91	A	91	SER	0	-0.121	-0.062	33.146	0.002	0.002	0.000	0.000	0.000	0.000
92	A	92	ASP	-1	-0.726	-0.860	28.579	0.057	0.057	0.000	0.000	0.000	0.000
93	A	93	ASN	0	0.030	0.027	27.904	0.005	0.005	0.000	0.000	0.000	0.000
94	A	94	GLY	0	0.016	-0.002	25.998	0.009	0.009	0.000	0.000	0.000	0.000
95	A	95	THR	0	-0.055	-0.011	19.966	-0.017	-0.017	0.000	0.000	0.000	0.000
96	A	96	PHE	0	0.022	0.015	19.241	0.023	0.023	0.000	0.000	0.000	0.000
97	A	97	THR	0	-0.043	-0.034	14.730	-0.014	-0.014	0.000	0.000	0.000	0.000
98	A	99	ASP	-1	-0.860	-0.957	11.560	1.027	1.027	0.000	0.000	0.000	0.000
99	A	100	VAL	0	0.046	0.018	7.072	-0.107	-0.107	0.000	0.000	0.000	0.000
100	A	101	LYS	1	0.847	0.950	8.655	-0.356	-0.356	0.000	0.000	0.000	0.000
101	A	102	ASN	0	0.074	0.036	5.678	-0.541	-0.541	0.000	0.000	0.000	0.000
102	A	103	PRO	0	0.025	0.002	9.907	-0.140	-0.140	0.000	0.000	0.000	0.000
103	A	104	PRO	0	-0.065	-0.032	12.860	-0.078	-0.078	0.000	0.000	0.000	0.000
104	A	105	ASP	-1	-0.827	-0.911	13.618	0.628	0.628	0.000	0.000	0.000	0.000
105	A	106	ILE	0	-0.066	-0.038	13.687	-0.017	-0.017	0.000	0.000	0.000	0.000
106	A	107	VAL	0	-0.025	-0.018	10.628	0.130	0.130	0.000	0.000	0.000	0.000
107	A	108	GLY	0	0.042	0.035	9.358	0.207	0.207	0.000	0.000	0.000	0.000
108	A	109	LYS	1	0.863	0.952	2.955	-4.762	-3.991	0.171	-0.202	-0.740	0.001
109	A	110	THR	0	-0.021	-0.021	8.151	-0.129	-0.129	0.000	0.000	0.000	0.000
110	A	111	SER	0	0.003	0.002	10.251	-0.087	-0.087	0.000	0.000	0.000	0.000
111	A	112	GLN	0	-0.045	-0.026	12.191	0.011	0.011	0.000	0.000	0.000	0.000
112	A	113	VAL	0	0.029	0.034	15.881	-0.047	-0.047	0.000	0.000	0.000	0.000
113	A	114	THR	0	-0.043	-0.019	18.415	0.026	0.026	0.000	0.000	0.000	0.000
114	A	115	LEU	0	-0.019	-0.007	22.142	-0.019	-0.019	0.000	0.000	0.000	0.000
115	A	116	TYR	0	-0.028	-0.011	24.877	0.010	0.010	0.000	0.000	0.000	0.000
116	A	117	VAL	0	0.001	0.015	28.433	-0.008	-0.008	0.000	0.000	0.000	0.000
117	A	118	PHE	0	-0.047	-0.031	29.331	0.001	0.001	0.000	0.000	0.000	0.000
118	A	119	GLU	-1	-0.938	-0.975	34.209	-0.010	-0.010	0.000	0.000	0.000	0.000

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