FMO DATABASE

FMODB ID: R8NQ8

Calculation Name: 2ANE-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2ANE

Chain ID: A

ChEMBL ID:

UniProt ID: P0A9M0

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	110
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-860567.037368
FMO2-HF: Nuclear repulsion	817718.751301
FMO2-HF: Total energy	-42848.286068
FMO2-MP2: Total energy	-42972.005053

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:8:ARG)

Summations of interaction energy for fragment #1(A:8:ARG)

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.
-60.083	-53.397	3.019	-4.086	-5.619	-0.026

Interaction energy analysis for fragmet #1(A:8:ARG)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.918 / q_NPA : 0.952

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	10	GLU	-1	-0.853	-0.929	3.498	-30.218	-27.704	0.001	-1.351	-1.164	-0.001
4	A	11	ILE	0	-0.051	-0.006	6.247	1.145	1.145	0.000	0.000	0.000	0.000
5	A	12	PRO	0	0.105	0.054	9.292	0.216	0.216	0.000	0.000	0.000	0.000
6	A	13	VAL	0	0.001	-0.009	11.580	-0.605	-0.605	0.000	0.000	0.000	0.000
7	A	14	LEU	0	0.012	0.016	14.162	0.901	0.901	0.000	0.000	0.000	0.000
8	A	15	PRO	0	-0.003	0.003	17.626	-0.324	-0.324	0.000	0.000	0.000	0.000
9	A	16	LEU	0	-0.035	-0.024	19.370	0.496	0.496	0.000	0.000	0.000	0.000
10	A	17	ARG	1	0.842	0.893	21.818	9.852	9.852	0.000	0.000	0.000	0.000
11	A	18	ASP	-1	-0.833	-0.904	25.034	-10.123	-10.123	0.000	0.000	0.000	0.000
12	A	19	VAL	0	-0.025	-0.009	23.483	0.223	0.223	0.000	0.000	0.000	0.000
13	A	20	VAL	0	-0.001	0.000	19.680	-0.484	-0.484	0.000	0.000	0.000	0.000
14	A	21	VAL	0	0.031	0.014	18.803	0.383	0.383	0.000	0.000	0.000	0.000
15	A	22	TYR	0	0.011	-0.003	17.355	-1.151	-1.151	0.000	0.000	0.000	0.000
16	A	23	PRO	0	-0.009	-0.020	14.793	0.245	0.245	0.000	0.000	0.000	0.000
17	A	24	HIS	0	0.026	0.014	17.318	0.761	0.761	0.000	0.000	0.000	0.000
18	A	25	MET	0	-0.039	0.022	20.127	0.491	0.491	0.000	0.000	0.000	0.000
19	A	26	VAL	0	0.024	0.018	21.055	-0.429	-0.429	0.000	0.000	0.000	0.000
20	A	27	ILE	0	-0.013	-0.012	22.118	0.462	0.462	0.000	0.000	0.000	0.000
21	A	28	PRO	0	-0.034	-0.022	24.175	-0.266	-0.266	0.000	0.000	0.000	0.000
22	A	29	LEU	0	0.000	0.006	21.716	0.065	0.065	0.000	0.000	0.000	0.000
23	A	30	PHE	0	-0.004	-0.005	26.040	0.185	0.185	0.000	0.000	0.000	0.000
24	A	31	VAL	0	-0.014	-0.007	23.685	-0.163	-0.163	0.000	0.000	0.000	0.000
25	A	32	GLY	0	0.079	0.044	26.975	0.151	0.151	0.000	0.000	0.000	0.000
26	A	33	ARG	1	0.891	0.922	25.758	10.675	10.675	0.000	0.000	0.000	0.000
27	A	34	GLU	-1	-0.834	-0.902	25.348	-10.391	-10.391	0.000	0.000	0.000	0.000
28	A	35	LYS	1	0.855	0.944	20.106	12.712	12.712	0.000	0.000	0.000	0.000
29	A	36	SER	0	0.031	-0.002	20.754	-0.665	-0.665	0.000	0.000	0.000	0.000
30	A	37	ILE	0	-0.050	-0.017	21.346	-0.341	-0.341	0.000	0.000	0.000	0.000
31	A	38	ARG	1	0.878	0.900	21.764	11.053	11.053	0.000	0.000	0.000	0.000
32	A	39	CYS	0	-0.077	-0.025	16.666	-0.747	-0.747	0.000	0.000	0.000	0.000
33	A	40	LEU	0	-0.001	-0.008	17.644	-0.634	-0.634	0.000	0.000	0.000	0.000
34	A	41	GLU	-1	-0.817	-0.898	19.745	-11.462	-11.462	0.000	0.000	0.000	0.000
35	A	42	ALA	0	0.063	0.036	16.624	-0.150	-0.150	0.000	0.000	0.000	0.000
36	A	43	ALA	0	-0.021	-0.005	15.414	-0.762	-0.762	0.000	0.000	0.000	0.000
37	A	44	MET	0	-0.093	-0.061	16.414	-0.343	-0.343	0.000	0.000	0.000	0.000
38	A	45	ASP	-1	-0.934	-0.947	19.346	-13.209	-13.209	0.000	0.000	0.000	0.000
39	A	46	HIS	0	-0.081	-0.044	10.625	-1.085	-1.085	0.000	0.000	0.000	0.000
40	A	47	ASP	-1	-0.802	-0.893	11.932	-21.770	-21.770	0.000	0.000	0.000	0.000
41	A	48	LYS	1	0.882	0.945	15.291	13.032	13.032	0.000	0.000	0.000	0.000
42	A	49	LYS	1	0.799	0.905	10.962	21.136	21.136	0.000	0.000	0.000	0.000
43	A	50	ILE	0	0.050	0.016	13.353	-0.307	-0.307	0.000	0.000	0.000	0.000
44	A	51	MET	0	-0.063	-0.016	9.580	-0.728	-0.728	0.000	0.000	0.000	0.000
45	A	52	LEU	0	0.016	0.014	12.676	0.753	0.753	0.000	0.000	0.000	0.000
46	A	53	VAL	0	-0.027	-0.022	13.306	-0.732	-0.732	0.000	0.000	0.000	0.000
47	A	54	ALA	0	0.023	0.021	16.189	0.695	0.695	0.000	0.000	0.000	0.000
48	A	55	GLN	0	-0.003	-0.029	18.670	-0.642	-0.642	0.000	0.000	0.000	0.000
49	A	56	LYS	1	0.856	0.923	17.662	14.777	14.777	0.000	0.000	0.000	0.000
50	A	57	GLU	-1	-0.904	-0.953	22.998	-11.306	-11.306	0.000	0.000	0.000	0.000
51	A	58	ALA	0	-0.018	-0.003	26.596	0.297	0.297	0.000	0.000	0.000	0.000
52	A	59	SER	0	-0.056	-0.005	24.450	0.084	0.084	0.000	0.000	0.000	0.000
53	A	60	THR	0	0.011	0.000	26.426	0.248	0.248	0.000	0.000	0.000	0.000
54	A	61	ASP	-1	-0.817	-0.911	26.041	-10.298	-10.298	0.000	0.000	0.000	0.000
55	A	62	GLU	-1	-0.911	-0.938	24.257	-11.744	-11.744	0.000	0.000	0.000	0.000
56	A	63	PRO	0	-0.021	0.010	21.284	0.048	0.048	0.000	0.000	0.000	0.000
57	A	64	GLY	0	0.069	0.022	21.161	-0.151	-0.151	0.000	0.000	0.000	0.000
58	A	65	VAL	0	0.013	-0.021	15.926	-0.143	-0.143	0.000	0.000	0.000	0.000
59	A	66	ASN	0	-0.006	-0.005	17.183	-1.004	-1.004	0.000	0.000	0.000	0.000
60	A	67	ASP	-1	-0.826	-0.898	19.360	-12.098	-12.098	0.000	0.000	0.000	0.000
61	A	68	LEU	0	-0.002	0.008	15.838	0.219	0.219	0.000	0.000	0.000	0.000
62	A	69	PHE	0	-0.046	-0.025	15.649	-0.310	-0.310	0.000	0.000	0.000	0.000
63	A	70	THR	0	0.004	0.001	11.451	-0.333	-0.333	0.000	0.000	0.000	0.000
64	A	71	VAL	0	-0.010	-0.018	10.639	-1.946	-1.946	0.000	0.000	0.000	0.000
65	A	72	GLY	0	0.033	0.014	11.990	1.402	1.402	0.000	0.000	0.000	0.000
66	A	73	THR	0	-0.087	-0.072	12.479	-1.000	-1.000	0.000	0.000	0.000	0.000
67	A	74	VAL	0	0.013	0.032	8.261	0.546	0.546	0.000	0.000	0.000	0.000
68	A	75	ALA	0	0.014	0.000	11.706	0.600	0.600	0.000	0.000	0.000	0.000
69	A	76	SER	0	0.025	0.023	14.769	-0.633	-0.633	0.000	0.000	0.000	0.000
70	A	77	ILE	0	0.046	0.013	16.919	0.750	0.750	0.000	0.000	0.000	0.000
71	A	78	LEU	0	-0.021	-0.008	19.863	0.293	0.293	0.000	0.000	0.000	0.000
72	A	79	GLN	0	-0.034	-0.022	22.739	0.497	0.497	0.000	0.000	0.000	0.000
73	A	80	MET	0	0.028	0.019	23.626	-0.309	-0.309	0.000	0.000	0.000	0.000
74	A	81	LEU	0	-0.026	-0.009	26.063	0.209	0.209	0.000	0.000	0.000	0.000
75	A	82	LYS	1	0.844	0.909	27.170	10.589	10.589	0.000	0.000	0.000	0.000
76	A	83	LEU	0	-0.023	-0.004	30.518	0.228	0.228	0.000	0.000	0.000	0.000
77	A	84	PRO	0	-0.010	-0.019	33.992	-0.082	-0.082	0.000	0.000	0.000	0.000
78	A	85	ASP	-1	-0.876	-0.940	34.973	-8.389	-8.389	0.000	0.000	0.000	0.000
79	A	86	GLY	0	0.005	0.015	32.823	0.020	0.020	0.000	0.000	0.000	0.000
80	A	87	THR	0	-0.055	-0.025	30.730	-0.462	-0.462	0.000	0.000	0.000	0.000
81	A	88	VAL	0	0.000	-0.012	26.017	0.025	0.025	0.000	0.000	0.000	0.000
82	A	89	LYS	1	0.918	0.977	28.148	9.389	9.389	0.000	0.000	0.000	0.000
83	A	90	VAL	0	0.001	-0.016	22.198	-0.092	-0.092	0.000	0.000	0.000	0.000
84	A	91	LEU	0	-0.051	-0.011	24.536	0.107	0.107	0.000	0.000	0.000	0.000
85	A	92	VAL	0	0.018	-0.002	19.242	-0.338	-0.338	0.000	0.000	0.000	0.000
86	A	93	GLU	-1	-0.885	-0.945	18.713	-13.303	-13.303	0.000	0.000	0.000	0.000
87	A	94	GLY	0	0.005	0.012	16.335	-0.876	-0.876	0.000	0.000	0.000	0.000
88	A	95	LEU	0	-0.020	-0.007	12.957	0.247	0.247	0.000	0.000	0.000	0.000
89	A	96	GLN	0	-0.015	-0.024	9.110	0.811	0.811	0.000	0.000	0.000	0.000
90	A	97	ARG	1	0.906	0.958	11.489	17.447	17.447	0.000	0.000	0.000	0.000
91	A	98	ALA	0	0.023	0.007	7.186	-1.652	-1.652	0.000	0.000	0.000	0.000
92	A	99	ARG	1	0.860	0.912	6.771	32.548	32.548	0.000	0.000	0.000	0.000
93	A	100	ILE	0	-0.015	-0.014	6.374	-3.517	-3.517	0.000	0.000	0.000	0.000
94	A	101	SER	0	-0.107	-0.059	4.474	0.552	0.638	-0.001	-0.007	-0.077	0.000
95	A	102	ALA	0	0.027	-0.001	6.443	2.153	2.153	0.000	0.000	0.000	0.000
96	A	103	LEU	0	-0.018	0.006	8.946	-1.151	-1.151	0.000	0.000	0.000	0.000
97	A	104	SER	0	-0.041	-0.024	11.612	0.696	0.696	0.000	0.000	0.000	0.000
98	A	105	ASP	-1	-0.796	-0.917	13.777	-14.146	-14.146	0.000	0.000	0.000	0.000
99	A	106	ASN	0	-0.066	-0.028	13.495	0.410	0.410	0.000	0.000	0.000	0.000
100	A	107	GLY	0	0.008	0.014	17.659	0.303	0.303	0.000	0.000	0.000	0.000
101	A	108	GLU	-1	-0.878	-0.923	19.487	-11.697	-11.697	0.000	0.000	0.000	0.000
102	A	109	HIS	0	-0.017	-0.038	14.695	0.556	0.556	0.000	0.000	0.000	0.000
103	A	110	PHE	0	-0.007	0.002	14.707	-0.480	-0.480	0.000	0.000	0.000	0.000
104	A	111	SER	0	-0.031	-0.017	10.551	-0.331	-0.331	0.000	0.000	0.000	0.000
105	A	112	ALA	0	0.024	0.011	8.705	0.458	0.458	0.000	0.000	0.000	0.000
106	A	113	LYS	1	0.965	1.006	4.747	26.768	26.827	-0.001	-0.004	-0.054	0.000
107	A	114	ALA	0	0.017	0.012	3.785	1.158	1.442	0.000	-0.074	-0.210	0.000
108	A	115	GLU	-1	-0.834	-0.905	2.232	-60.269	-56.724	3.005	-2.650	-3.900	-0.025
109	A	116	TYR	0	0.024	0.005	3.675	6.040	6.238	0.015	0.000	-0.214	0.000
110	A	117	LEU	0	-0.036	-0.005	6.234	-0.399	-0.399	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:8:ARG)