FMO DATABASE

FMODB ID: ZVR7N

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

Total energy (hartree)

FMO2-HF: Electronic energy	-861379.822609
FMO2-HF: Nuclear repulsion	818531.871509
FMO2-HF: Total energy	-42847.9511
FMO2-MP2: Total energy	-42971.699851

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.
-52.215	-46.043	3.221	-4.389	-5.002	-0.021

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 : 0.926 / q_NPA : 0.958

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	-0.883	-0.951	3.798	-30.299	-27.275	-0.035	-1.620	-1.368	0.004
4	A	11	ILE	0	-0.061	-0.018	6.799	1.193	1.193	0.000	0.000	0.000	0.000
5	A	12	PRO	0	0.086	0.044	9.549	0.114	0.114	0.000	0.000	0.000	0.000
6	A	13	VAL	0	0.002	-0.006	11.721	-0.339	-0.339	0.000	0.000	0.000	0.000
7	A	14	LEU	0	0.010	0.015	14.163	0.829	0.829	0.000	0.000	0.000	0.000
8	A	15	PRO	0	-0.017	-0.003	17.469	-0.268	-0.268	0.000	0.000	0.000	0.000
9	A	16	LEU	0	-0.027	-0.023	19.208	0.533	0.533	0.000	0.000	0.000	0.000
10	A	17	ARG	1	0.835	0.884	21.395	9.698	9.698	0.000	0.000	0.000	0.000
11	A	18	ASP	-1	-0.840	-0.917	24.568	-9.946	-9.946	0.000	0.000	0.000	0.000
12	A	19	VAL	0	-0.019	0.007	22.990	0.212	0.212	0.000	0.000	0.000	0.000
13	A	20	VAL	0	0.007	0.004	19.587	-0.460	-0.460	0.000	0.000	0.000	0.000
14	A	21	VAL	0	0.011	0.012	18.543	0.342	0.342	0.000	0.000	0.000	0.000
15	A	22	TYR	0	-0.011	-0.027	17.386	-1.068	-1.068	0.000	0.000	0.000	0.000
16	A	23	PRO	0	-0.041	-0.028	14.293	0.199	0.199	0.000	0.000	0.000	0.000
17	A	24	HIS	0	0.030	0.001	16.669	0.740	0.740	0.000	0.000	0.000	0.000
18	A	25	MET	0	-0.039	0.034	19.437	0.464	0.464	0.000	0.000	0.000	0.000
19	A	26	VAL	0	0.041	0.018	20.598	-0.428	-0.428	0.000	0.000	0.000	0.000
20	A	27	ILE	0	-0.028	-0.017	22.068	0.432	0.432	0.000	0.000	0.000	0.000
21	A	28	PRO	0	-0.017	-0.012	23.876	-0.292	-0.292	0.000	0.000	0.000	0.000
22	A	29	LEU	0	-0.006	0.000	20.974	0.136	0.136	0.000	0.000	0.000	0.000
23	A	30	PHE	0	0.002	-0.007	25.330	0.155	0.155	0.000	0.000	0.000	0.000
24	A	31	VAL	0	-0.014	-0.010	23.077	-0.232	-0.232	0.000	0.000	0.000	0.000
25	A	32	GLY	0	0.079	0.041	26.397	0.212	0.212	0.000	0.000	0.000	0.000
26	A	33	ARG	1	0.876	0.930	25.798	10.538	10.538	0.000	0.000	0.000	0.000
27	A	34	GLU	-1	-0.810	-0.907	25.805	-10.129	-10.129	0.000	0.000	0.000	0.000
28	A	35	LYS	1	0.885	0.965	20.990	12.449	12.449	0.000	0.000	0.000	0.000
29	A	36	SER	0	0.021	-0.009	21.158	-0.537	-0.537	0.000	0.000	0.000	0.000
30	A	37	ILE	0	-0.029	-0.012	21.444	-0.364	-0.364	0.000	0.000	0.000	0.000
31	A	38	ARG	1	0.879	0.911	21.914	10.960	10.960	0.000	0.000	0.000	0.000
32	A	39	CYS	0	-0.083	-0.030	16.813	-0.706	-0.706	0.000	0.000	0.000	0.000
33	A	40	LEU	0	-0.011	-0.016	17.655	-0.571	-0.571	0.000	0.000	0.000	0.000
34	A	41	GLU	-1	-0.827	-0.904	19.362	-11.371	-11.371	0.000	0.000	0.000	0.000
35	A	42	ALA	0	0.071	0.047	16.426	-0.201	-0.201	0.000	0.000	0.000	0.000
36	A	43	ALA	0	-0.021	-0.009	15.063	-0.568	-0.568	0.000	0.000	0.000	0.000
37	A	44	MET	0	-0.081	-0.056	16.038	-0.335	-0.335	0.000	0.000	0.000	0.000
38	A	45	ASP	-1	-0.944	-0.942	18.784	-12.974	-12.974	0.000	0.000	0.000	0.000
39	A	46	HIS	0	-0.090	-0.061	10.396	-1.034	-1.034	0.000	0.000	0.000	0.000
40	A	47	ASP	-1	-0.830	-0.906	11.117	-21.024	-21.024	0.000	0.000	0.000	0.000
41	A	48	LYS	1	0.909	0.960	14.628	13.025	13.025	0.000	0.000	0.000	0.000
42	A	49	LYS	1	0.865	0.946	9.774	21.759	21.759	0.000	0.000	0.000	0.000
43	A	50	ILE	0	0.047	0.007	12.972	-0.314	-0.314	0.000	0.000	0.000	0.000
44	A	51	MET	0	-0.061	-0.017	8.943	-0.709	-0.709	0.000	0.000	0.000	0.000
45	A	52	LEU	0	0.014	0.016	12.273	0.713	0.713	0.000	0.000	0.000	0.000
46	A	53	VAL	0	-0.021	-0.017	13.162	-0.662	-0.662	0.000	0.000	0.000	0.000
47	A	54	ALA	0	0.019	0.023	15.877	0.667	0.667	0.000	0.000	0.000	0.000
48	A	55	GLN	0	0.014	-0.015	18.762	-0.630	-0.630	0.000	0.000	0.000	0.000
49	A	56	LYS	1	0.847	0.911	18.678	14.322	14.322	0.000	0.000	0.000	0.000
50	A	57	GLU	-1	-0.943	-0.986	23.145	-10.970	-10.970	0.000	0.000	0.000	0.000
51	A	58	ALA	0	-0.014	0.005	26.798	0.148	0.148	0.000	0.000	0.000	0.000
52	A	59	SER	0	-0.026	0.014	24.928	0.134	0.134	0.000	0.000	0.000	0.000
53	A	60	THR	0	0.023	0.000	26.980	0.176	0.176	0.000	0.000	0.000	0.000
54	A	61	ASP	-1	-0.822	-0.902	26.734	-10.096	-10.096	0.000	0.000	0.000	0.000
55	A	62	GLU	-1	-0.932	-0.954	25.184	-11.450	-11.450	0.000	0.000	0.000	0.000
56	A	63	PRO	0	-0.037	-0.003	22.023	0.011	0.011	0.000	0.000	0.000	0.000
57	A	64	GLY	0	0.108	0.041	22.327	-0.142	-0.142	0.000	0.000	0.000	0.000
58	A	65	VAL	0	0.022	-0.014	16.711	-0.181	-0.181	0.000	0.000	0.000	0.000
59	A	66	ASN	0	-0.041	-0.020	17.825	-1.003	-1.003	0.000	0.000	0.000	0.000
60	A	67	ASP	-1	-0.826	-0.899	19.773	-11.789	-11.789	0.000	0.000	0.000	0.000
61	A	68	LEU	0	-0.019	0.004	16.244	0.305	0.305	0.000	0.000	0.000	0.000
62	A	69	PHE	0	-0.042	-0.018	16.206	-0.355	-0.355	0.000	0.000	0.000	0.000
63	A	70	THR	0	0.021	0.005	12.136	-0.241	-0.241	0.000	0.000	0.000	0.000
64	A	71	VAL	0	-0.016	-0.011	11.124	-1.832	-1.832	0.000	0.000	0.000	0.000
65	A	72	GLY	0	0.047	0.018	11.505	1.204	1.204	0.000	0.000	0.000	0.000
66	A	73	THR	0	-0.089	-0.072	11.955	-1.089	-1.089	0.000	0.000	0.000	0.000
67	A	74	VAL	0	0.008	0.020	7.953	0.431	0.431	0.000	0.000	0.000	0.000
68	A	75	ALA	0	0.012	-0.008	11.390	0.573	0.573	0.000	0.000	0.000	0.000
69	A	76	SER	0	0.032	0.031	14.305	-0.639	-0.639	0.000	0.000	0.000	0.000
70	A	77	ILE	0	-0.003	-0.014	16.020	0.768	0.768	0.000	0.000	0.000	0.000
71	A	78	LEU	0	-0.017	-0.013	19.164	0.133	0.133	0.000	0.000	0.000	0.000
72	A	79	GLN	0	-0.076	-0.042	21.832	0.546	0.546	0.000	0.000	0.000	0.000
73	A	80	MET	0	0.032	0.023	23.509	-0.306	-0.306	0.000	0.000	0.000	0.000
74	A	81	LEU	0	-0.020	0.000	25.585	0.178	0.178	0.000	0.000	0.000	0.000
75	A	82	LYS	1	0.847	0.899	26.987	10.366	10.366	0.000	0.000	0.000	0.000
76	A	83	LEU	0	-0.024	0.001	30.197	0.240	0.240	0.000	0.000	0.000	0.000
77	A	84	PRO	0	0.013	-0.013	33.552	-0.075	-0.075	0.000	0.000	0.000	0.000
78	A	85	ASP	-1	-0.924	-0.971	34.517	-8.353	-8.353	0.000	0.000	0.000	0.000
79	A	86	GLY	0	0.017	0.024	32.644	0.005	0.005	0.000	0.000	0.000	0.000
80	A	87	THR	0	-0.035	0.002	30.488	-0.389	-0.389	0.000	0.000	0.000	0.000
81	A	88	VAL	0	-0.013	-0.022	25.404	-0.002	-0.002	0.000	0.000	0.000	0.000
82	A	89	LYS	1	0.954	0.987	27.809	9.072	9.072	0.000	0.000	0.000	0.000
83	A	90	VAL	0	0.012	-0.002	21.536	-0.024	-0.024	0.000	0.000	0.000	0.000
84	A	91	LEU	0	-0.043	-0.008	23.993	0.054	0.054	0.000	0.000	0.000	0.000
85	A	92	VAL	0	0.007	-0.001	18.798	-0.344	-0.344	0.000	0.000	0.000	0.000
86	A	93	GLU	-1	-0.878	-0.940	17.981	-12.907	-12.907	0.000	0.000	0.000	0.000
87	A	94	GLY	0	-0.002	0.005	15.989	-0.826	-0.826	0.000	0.000	0.000	0.000
88	A	95	LEU	0	-0.025	-0.012	12.210	0.235	0.235	0.000	0.000	0.000	0.000
89	A	96	GLN	0	0.002	-0.015	8.160	0.544	0.544	0.000	0.000	0.000	0.000
90	A	97	ARG	1	0.934	0.979	11.140	16.820	16.820	0.000	0.000	0.000	0.000
91	A	98	ALA	0	0.010	0.004	6.341	-1.481	-1.481	0.000	0.000	0.000	0.000
92	A	99	ARG	1	0.865	0.917	6.945	30.786	30.786	0.000	0.000	0.000	0.000
93	A	100	ILE	0	0.004	0.004	6.429	-3.402	-3.402	0.000	0.000	0.000	0.000
94	A	101	SER	0	-0.069	-0.030	5.036	0.895	0.895	0.000	0.000	0.000	0.000
95	A	102	ALA	0	0.004	-0.008	7.437	1.753	1.753	0.000	0.000	0.000	0.000
96	A	103	LEU	0	-0.006	0.011	9.702	-0.967	-0.967	0.000	0.000	0.000	0.000
97	A	104	SER	0	-0.034	-0.017	12.376	0.667	0.667	0.000	0.000	0.000	0.000
98	A	105	ASP	-1	-0.805	-0.918	14.513	-13.905	-13.905	0.000	0.000	0.000	0.000
99	A	106	ASN	0	-0.082	-0.050	13.618	0.362	0.362	0.000	0.000	0.000	0.000
100	A	107	GLY	0	0.017	0.021	17.779	0.235	0.235	0.000	0.000	0.000	0.000
101	A	108	GLU	-1	-0.854	-0.907	19.808	-11.505	-11.505	0.000	0.000	0.000	0.000
102	A	109	HIS	0	-0.021	-0.035	15.076	0.576	0.576	0.000	0.000	0.000	0.000
103	A	110	PHE	0	-0.017	-0.003	15.510	-0.497	-0.497	0.000	0.000	0.000	0.000
104	A	111	SER	0	0.003	0.009	11.521	-0.460	-0.460	0.000	0.000	0.000	0.000
105	A	112	ALA	0	0.029	0.006	9.226	0.429	0.429	0.000	0.000	0.000	0.000
106	A	113	LYS	1	0.955	1.017	4.885	28.086	28.086	0.000	0.000	0.000	0.000
107	A	114	ALA	0	-0.005	-0.026	4.444	1.573	1.781	-0.001	-0.054	-0.153	0.000
108	A	115	GLU	-1	-0.841	-0.910	2.425	-53.145	-50.436	3.228	-2.795	-3.141	-0.024
109	A	116	TYR	0	0.018	-0.001	3.374	5.155	5.386	0.029	0.080	-0.340	-0.001
110	A	117	LEU	0	-0.031	0.002	5.872	-0.531	-0.531	0.000	0.000	0.000	0.000

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