FMO DATABASE

FMODB ID: YV9G2

Calculation Name: 5AN3-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 5AN3

Chain ID: A

ChEMBL ID:

UniProt ID: Q08446

Base Structure: X-ray

Registration Date: 2023-09-22

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	132
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1241290.488619
FMO2-HF: Nuclear repulsion	1188097.766497
FMO2-HF: Total energy	-53192.722122
FMO2-MP2: Total energy	-53350.092073

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:3:VAL)

Summations of interaction energy for fragment #1(A:3:VAL)

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.
-17.445	-16.576	15.824	-7.394	-9.299	-0.052

Interaction energy analysis for fragmet #1(A:3:VAL)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.037 / 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	5	LYS	1	0.952	0.972	3.236	-2.151	-0.396	0.006	-0.778	-0.983	0.002
4	A	6	ASP	-1	-0.825	-0.904	1.839	-13.085	-16.417	13.120	-5.199	-4.589	-0.054
5	A	7	LEU	0	0.032	0.009	3.013	0.445	1.483	0.119	-0.320	-0.837	0.001
6	A	8	LYS	1	0.795	0.899	5.727	0.198	0.198	0.000	0.000	0.000	0.000
7	A	9	THR	0	-0.044	-0.032	7.245	0.166	0.166	0.000	0.000	0.000	0.000
8	A	10	ALA	0	0.023	0.015	7.918	0.158	0.158	0.000	0.000	0.000	0.000
9	A	11	TYR	0	-0.007	-0.004	9.616	0.149	0.149	0.000	0.000	0.000	0.000
10	A	12	LYS	1	0.856	0.910	11.506	0.258	0.258	0.000	0.000	0.000	0.000
11	A	13	ALA	0	0.063	0.026	12.741	0.058	0.058	0.000	0.000	0.000	0.000
12	A	14	LEU	0	-0.013	-0.002	13.676	0.047	0.047	0.000	0.000	0.000	0.000
13	A	15	TYR	0	-0.037	-0.026	13.607	0.046	0.046	0.000	0.000	0.000	0.000
14	A	16	ASP	-1	-0.838	-0.880	16.754	-0.109	-0.109	0.000	0.000	0.000	0.000
15	A	17	GLU	-1	-0.881	-0.949	15.251	-0.333	-0.333	0.000	0.000	0.000	0.000
16	A	18	LYS	1	0.766	0.884	18.306	0.131	0.131	0.000	0.000	0.000	0.000
17	A	19	GLU	-1	-0.729	-0.856	17.849	-0.265	-0.265	0.000	0.000	0.000	0.000
18	A	20	PRO	0	0.007	0.004	17.073	-0.039	-0.039	0.000	0.000	0.000	0.000
19	A	21	LEU	0	0.049	0.022	16.478	-0.031	-0.031	0.000	0.000	0.000	0.000
20	A	22	LYS	1	0.804	0.891	13.959	0.297	0.297	0.000	0.000	0.000	0.000
21	A	23	ALA	0	0.004	-0.005	12.522	-0.084	-0.084	0.000	0.000	0.000	0.000
22	A	24	LEU	0	0.010	0.008	11.603	-0.079	-0.079	0.000	0.000	0.000	0.000
23	A	25	HIS	0	-0.007	-0.001	11.940	0.007	0.007	0.000	0.000	0.000	0.000
24	A	26	LEU	0	-0.010	-0.007	8.595	-0.099	-0.099	0.000	0.000	0.000	0.000
25	A	27	TYR	0	0.010	-0.016	7.219	-0.248	-0.248	0.000	0.000	0.000	0.000
26	A	28	ASP	-1	-0.795	-0.879	7.802	-0.422	-0.422	0.000	0.000	0.000	0.000
27	A	29	GLU	-1	-0.839	-0.895	8.004	-0.782	-0.782	0.000	0.000	0.000	0.000
28	A	30	ILE	0	-0.033	-0.015	2.423	-0.867	-0.185	0.527	-0.221	-0.988	-0.002
29	A	31	LEU	0	-0.056	-0.035	5.042	0.034	0.141	-0.001	-0.001	-0.104	0.000
30	A	32	LYS	1	0.834	0.906	7.395	0.756	0.756	0.000	0.000	0.000	0.000
31	A	33	GLY	0	0.022	0.030	5.072	0.112	0.112	0.000	0.000	0.000	0.000
32	A	34	SER	0	-0.068	-0.046	3.326	-1.097	-0.201	0.063	-0.354	-0.605	-0.002
33	A	35	PRO	0	0.055	0.042	5.639	0.196	0.196	0.000	0.000	0.000	0.000
34	A	36	THR	0	-0.007	-0.008	7.644	0.029	0.029	0.000	0.000	0.000	0.000
35	A	37	ASN	0	0.046	0.017	2.261	-0.693	-0.970	1.990	-0.521	-1.193	0.003
36	A	38	LEU	0	0.078	0.029	5.990	-0.087	-0.087	0.000	0.000	0.000	0.000
37	A	39	THR	0	-0.008	-0.007	5.858	-0.086	-0.086	0.000	0.000	0.000	0.000
38	A	40	ALA	0	0.034	0.022	5.369	-0.111	-0.111	0.000	0.000	0.000	0.000
39	A	41	LEU	0	-0.022	0.002	7.424	-0.063	-0.063	0.000	0.000	0.000	0.000
40	A	42	ILE	0	0.024	0.001	10.609	-0.023	-0.023	0.000	0.000	0.000	0.000
41	A	43	PHE	0	-0.007	-0.006	9.653	0.008	0.008	0.000	0.000	0.000	0.000
42	A	44	LYS	1	0.923	0.952	11.039	0.298	0.298	0.000	0.000	0.000	0.000
43	A	45	ALA	0	0.016	0.013	12.637	0.006	0.006	0.000	0.000	0.000	0.000
44	A	46	ALA	0	-0.006	0.001	15.099	0.006	0.006	0.000	0.000	0.000	0.000
45	A	47	CYS	0	-0.092	-0.039	13.678	-0.011	-0.011	0.000	0.000	0.000	0.000
46	A	48	LEU	0	0.022	0.010	16.509	0.008	0.008	0.000	0.000	0.000	0.000
47	A	49	GLU	-1	-0.800	-0.891	18.757	-0.062	-0.062	0.000	0.000	0.000	0.000
48	A	50	LYS	1	0.805	0.909	19.055	0.173	0.173	0.000	0.000	0.000	0.000
49	A	51	LEU	0	-0.020	0.001	18.370	0.001	0.001	0.000	0.000	0.000	0.000
50	A	52	TYR	0	0.009	-0.009	22.138	0.008	0.008	0.000	0.000	0.000	0.000
51	A	53	PHE	0	-0.041	-0.032	24.486	0.011	0.011	0.000	0.000	0.000	0.000
52	A	54	GLY	0	-0.023	-0.004	25.192	0.006	0.006	0.000	0.000	0.000	0.000
53	A	55	PHE	0	-0.031	-0.017	23.285	-0.005	-0.005	0.000	0.000	0.000	0.000
54	A	56	SER	0	0.028	0.008	26.580	0.004	0.004	0.000	0.000	0.000	0.000
55	A	57	ASP	-1	-0.892	-0.956	25.422	-0.147	-0.147	0.000	0.000	0.000	0.000
56	A	58	TRP	0	0.003	-0.010	19.053	-0.014	-0.014	0.000	0.000	0.000	0.000
57	A	59	HIS	0	-0.072	-0.013	25.075	0.007	0.007	0.000	0.000	0.000	0.000
58	A	60	SER	0	0.029	0.009	26.708	0.006	0.006	0.000	0.000	0.000	0.000
59	A	61	ASP	-1	-0.833	-0.913	26.152	-0.079	-0.079	0.000	0.000	0.000	0.000
60	A	62	ALA	0	0.076	0.049	24.763	-0.001	-0.001	0.000	0.000	0.000	0.000
61	A	63	THR	0	-0.072	-0.043	21.119	-0.010	-0.010	0.000	0.000	0.000	0.000
62	A	64	MET	0	-0.030	-0.013	21.073	-0.004	-0.004	0.000	0.000	0.000	0.000
63	A	65	GLU	-1	-0.926	-0.958	22.479	-0.070	-0.070	0.000	0.000	0.000	0.000
64	A	66	ASN	0	0.007	-0.001	18.614	-0.010	-0.010	0.000	0.000	0.000	0.000
65	A	67	ALA	0	-0.037	-0.023	17.573	-0.003	-0.003	0.000	0.000	0.000	0.000
66	A	68	LYS	1	0.805	0.893	18.107	0.040	0.040	0.000	0.000	0.000	0.000
67	A	69	GLU	-1	-0.870	-0.943	19.223	-0.081	-0.081	0.000	0.000	0.000	0.000
68	A	70	LEU	0	-0.053	-0.031	12.726	0.004	0.004	0.000	0.000	0.000	0.000
69	A	71	LEU	0	-0.002	-0.004	14.730	0.021	0.021	0.000	0.000	0.000	0.000
70	A	72	ASP	-1	-0.750	-0.828	16.864	-0.003	-0.003	0.000	0.000	0.000	0.000
71	A	73	LYS	1	0.902	0.953	11.868	0.148	0.148	0.000	0.000	0.000	0.000
72	A	74	ALA	0	-0.008	-0.001	12.620	0.025	0.025	0.000	0.000	0.000	0.000
73	A	75	LEU	0	0.004	0.005	13.606	0.035	0.035	0.000	0.000	0.000	0.000
74	A	76	MET	0	-0.023	-0.011	15.070	0.012	0.012	0.000	0.000	0.000	0.000
75	A	77	THR	0	-0.066	-0.049	10.435	0.003	0.003	0.000	0.000	0.000	0.000
76	A	78	ALA	0	-0.033	-0.013	13.667	0.033	0.033	0.000	0.000	0.000	0.000
77	A	79	GLU	-1	-0.892	-0.964	14.451	0.112	0.112	0.000	0.000	0.000	0.000
78	A	80	GLY	0	0.000	0.027	16.002	-0.004	-0.004	0.000	0.000	0.000	0.000
79	A	81	ARG	1	0.853	0.890	15.461	-0.149	-0.149	0.000	0.000	0.000	0.000
80	A	82	GLY	0	0.051	0.051	17.117	0.000	0.000	0.000	0.000	0.000	0.000
81	A	83	ASP	-1	-0.865	-0.925	12.583	0.352	0.352	0.000	0.000	0.000	0.000
82	A	84	ARG	1	0.901	0.938	16.079	-0.128	-0.128	0.000	0.000	0.000	0.000
83	A	85	SER	0	0.031	0.017	15.749	-0.014	-0.014	0.000	0.000	0.000	0.000
84	A	86	LYS	1	0.907	0.959	8.652	-0.396	-0.396	0.000	0.000	0.000	0.000
85	A	87	ILE	0	0.044	0.028	14.229	-0.026	-0.026	0.000	0.000	0.000	0.000
86	A	88	GLY	0	0.016	0.009	17.223	-0.024	-0.024	0.000	0.000	0.000	0.000
87	A	89	LEU	0	-0.011	-0.006	11.922	-0.014	-0.014	0.000	0.000	0.000	0.000
88	A	90	VAL	0	-0.007	-0.007	14.210	-0.026	-0.026	0.000	0.000	0.000	0.000
89	A	91	ASN	0	-0.032	-0.031	16.450	-0.030	-0.030	0.000	0.000	0.000	0.000
90	A	92	PHE	0	0.044	0.021	17.832	-0.012	-0.012	0.000	0.000	0.000	0.000
91	A	93	ARG	1	0.917	0.961	15.061	0.027	0.027	0.000	0.000	0.000	0.000
92	A	94	TYR	0	-0.008	-0.035	18.443	-0.011	-0.011	0.000	0.000	0.000	0.000
93	A	95	PHE	0	-0.008	-0.003	21.148	-0.008	-0.008	0.000	0.000	0.000	0.000
94	A	96	VAL	0	-0.021	-0.002	20.538	-0.006	-0.006	0.000	0.000	0.000	0.000
95	A	97	HIS	1	0.851	0.923	20.430	0.059	0.059	0.000	0.000	0.000	0.000
96	A	98	PHE	0	-0.002	-0.024	22.698	-0.005	-0.005	0.000	0.000	0.000	0.000
97	A	99	PHE	0	0.010	0.011	25.980	-0.002	-0.002	0.000	0.000	0.000	0.000
98	A	100	ASN	0	-0.053	-0.029	22.549	0.002	0.002	0.000	0.000	0.000	0.000
99	A	101	ILE	0	-0.048	-0.021	25.646	-0.003	-0.003	0.000	0.000	0.000	0.000
100	A	102	LYS	1	0.876	0.941	28.252	0.052	0.052	0.000	0.000	0.000	0.000
101	A	103	ASP	-1	-0.744	-0.856	29.566	-0.011	-0.011	0.000	0.000	0.000	0.000
102	A	104	TYR	0	-0.098	-0.113	30.550	-0.001	-0.001	0.000	0.000	0.000	0.000
103	A	105	GLU	-1	-0.822	-0.862	31.707	-0.002	-0.002	0.000	0.000	0.000	0.000
104	A	106	LEU	0	0.001	0.000	27.768	0.006	0.006	0.000	0.000	0.000	0.000
105	A	107	ALA	0	-0.006	-0.005	27.003	0.004	0.004	0.000	0.000	0.000	0.000
106	A	108	GLN	0	0.084	0.035	27.304	0.009	0.009	0.000	0.000	0.000	0.000
107	A	109	SER	0	0.023	0.015	29.199	0.007	0.007	0.000	0.000	0.000	0.000
108	A	110	TYR	0	-0.032	-0.016	22.713	0.005	0.005	0.000	0.000	0.000	0.000
109	A	111	PHE	0	-0.011	0.011	24.497	0.009	0.009	0.000	0.000	0.000	0.000
110	A	112	LYS	1	0.890	0.940	25.898	-0.034	-0.034	0.000	0.000	0.000	0.000
111	A	113	LYS	1	0.862	0.937	24.179	-0.018	-0.018	0.000	0.000	0.000	0.000
112	A	114	ALA	0	0.016	0.007	21.527	0.010	0.010	0.000	0.000	0.000	0.000
113	A	115	LYS	1	0.834	0.897	22.666	-0.032	-0.032	0.000	0.000	0.000	0.000
114	A	116	ASN	0	0.009	0.007	25.203	0.004	0.004	0.000	0.000	0.000	0.000
115	A	117	LEU	0	-0.037	-0.009	20.767	0.006	0.006	0.000	0.000	0.000	0.000
116	A	118	GLY	0	-0.050	-0.019	21.745	0.015	0.015	0.000	0.000	0.000	0.000
117	A	119	TYR	0	-0.087	-0.071	16.125	0.021	0.021	0.000	0.000	0.000	0.000
118	A	120	VAL	0	-0.027	-0.019	19.462	-0.012	-0.012	0.000	0.000	0.000	0.000
119	A	121	ASP	-1	-0.795	-0.849	19.011	0.051	0.051	0.000	0.000	0.000	0.000
120	A	122	ASP	-1	-0.899	-0.950	20.745	0.038	0.038	0.000	0.000	0.000	0.000
121	A	123	THR	0	-0.004	-0.035	21.391	-0.012	-0.012	0.000	0.000	0.000	0.000
122	A	124	LEU	0	-0.039	-0.012	22.748	-0.007	-0.007	0.000	0.000	0.000	0.000
123	A	125	PRO	0	0.058	0.020	24.727	-0.004	-0.004	0.000	0.000	0.000	0.000
124	A	126	LEU	0	0.068	0.034	26.235	-0.005	-0.005	0.000	0.000	0.000	0.000
125	A	127	TRP	0	-0.070	-0.039	22.253	-0.013	-0.013	0.000	0.000	0.000	0.000
126	A	128	GLU	-1	-0.770	-0.869	27.268	0.033	0.033	0.000	0.000	0.000	0.000
127	A	129	ASP	-1	-0.855	-0.920	29.885	0.009	0.009	0.000	0.000	0.000	0.000
128	A	130	ARG	1	0.819	0.912	25.411	0.015	0.015	0.000	0.000	0.000	0.000
129	A	131	LEU	0	-0.077	-0.033	28.769	-0.004	-0.004	0.000	0.000	0.000	0.000
130	A	132	GLU	-1	-0.910	-0.950	31.590	0.010	0.010	0.000	0.000	0.000	0.000
131	A	133	THR	0	-0.093	-0.052	34.719	-0.001	-0.001	0.000	0.000	0.000	0.000
132	A	134	LYS	1	0.779	0.905	31.704	0.017	0.017	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:3:VAL)