FMO DATABASE

FMODB ID: M353Z

Calculation Name: 4FQN-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4FQN

Chain ID: A

ChEMBL ID:

UniProt ID: Q9BSQ5

Base Structure: X-ray

Registration Date: 2023-06-20

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

Apendix: None

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	95
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-714350.002322
FMO2-HF: Nuclear repulsion	676471.670678
FMO2-HF: Total energy	-37878.331644
FMO2-MP2: Total energy	-37989.980675

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:282:GLY)

Summations of interaction energy for fragment #1(A:282:GLY)

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.
-10.812	-6.112	2.699	-3.831	-3.567	-0.003

Interaction energy analysis for fragmet #1(A:282:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.053 / q_NPA : 0.025

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	284	LYS	1	0.850	0.933	3.899	2.004	3.430	-0.005	-0.768	-0.653	0.002
4	A	285	THR	0	-0.094	-0.056	2.833	1.523	2.344	0.120	-0.354	-0.586	0.001
5	A	286	ILE	0	0.044	0.039	3.248	-2.635	-1.965	0.032	-0.404	-0.298	-0.003
6	A	287	SER	0	-0.041	-0.041	4.835	0.807	0.807	0.000	0.000	0.000	0.000
7	A	288	GLU	-1	-0.803	-0.918	6.125	-0.055	-0.055	0.000	0.000	0.000	0.000
8	A	289	SER	0	0.030	0.024	8.392	-0.019	-0.019	0.000	0.000	0.000	0.000
9	A	290	GLU	-1	-0.882	-0.922	6.409	-2.287	-2.287	0.000	0.000	0.000	0.000
10	A	291	LEU	0	-0.065	-0.028	9.776	-0.017	-0.017	0.000	0.000	0.000	0.000
11	A	292	SER	0	-0.027	-0.007	12.512	0.093	0.093	0.000	0.000	0.000	0.000
12	A	293	ALA	0	0.013	0.013	14.844	0.003	0.003	0.000	0.000	0.000	0.000
13	A	294	SER	0	0.045	0.003	18.165	0.007	0.007	0.000	0.000	0.000	0.000
14	A	295	ALA	0	0.000	0.019	13.522	0.037	0.037	0.000	0.000	0.000	0.000
15	A	296	THR	0	-0.015	-0.023	15.452	-0.007	-0.007	0.000	0.000	0.000	0.000
16	A	297	GLU	-1	-0.913	-0.958	16.587	-0.119	-0.119	0.000	0.000	0.000	0.000
17	A	298	LEU	0	0.027	0.007	17.928	0.019	0.019	0.000	0.000	0.000	0.000
18	A	299	LEU	0	-0.013	0.005	13.562	0.025	0.025	0.000	0.000	0.000	0.000
19	A	300	GLN	0	-0.022	-0.014	17.450	-0.005	-0.005	0.000	0.000	0.000	0.000
20	A	301	ASP	-1	-0.906	-0.957	20.553	0.002	0.002	0.000	0.000	0.000	0.000
21	A	302	TYR	0	0.010	0.008	17.394	0.024	0.024	0.000	0.000	0.000	0.000
22	A	303	MET	0	-0.022	-0.020	18.145	0.025	0.025	0.000	0.000	0.000	0.000
23	A	304	LEU	0	-0.037	-0.012	20.731	0.007	0.007	0.000	0.000	0.000	0.000
24	A	305	THR	0	-0.006	-0.004	23.357	0.012	0.012	0.000	0.000	0.000	0.000
25	A	306	LEU	0	-0.014	0.004	18.782	0.014	0.014	0.000	0.000	0.000	0.000
26	A	307	ARG	1	0.971	0.994	23.495	0.006	0.006	0.000	0.000	0.000	0.000
27	A	308	THR	0	-0.081	-0.045	26.443	-0.002	-0.002	0.000	0.000	0.000	0.000
28	A	309	LYS	1	0.858	0.922	25.977	-0.074	-0.074	0.000	0.000	0.000	0.000
29	A	310	LEU	0	-0.008	0.016	21.159	0.012	0.012	0.000	0.000	0.000	0.000
30	A	311	SER	0	-0.017	-0.034	25.413	-0.017	-0.017	0.000	0.000	0.000	0.000
31	A	312	SER	0	0.038	-0.006	24.451	0.003	0.003	0.000	0.000	0.000	0.000
32	A	313	GLN	0	0.040	0.022	23.185	-0.014	-0.014	0.000	0.000	0.000	0.000
33	A	314	GLU	-1	-0.729	-0.808	21.762	0.073	0.073	0.000	0.000	0.000	0.000
34	A	315	ILE	0	0.009	0.002	20.036	0.013	0.013	0.000	0.000	0.000	0.000
35	A	316	GLN	0	-0.022	-0.012	18.614	-0.005	-0.005	0.000	0.000	0.000	0.000
36	A	317	GLN	0	0.004	-0.002	17.375	-0.022	-0.022	0.000	0.000	0.000	0.000
37	A	318	PHE	0	0.033	0.011	14.322	0.013	0.013	0.000	0.000	0.000	0.000
38	A	319	ALA	0	0.002	-0.002	14.044	0.010	0.010	0.000	0.000	0.000	0.000
39	A	320	ALA	0	-0.033	-0.006	12.909	-0.067	-0.067	0.000	0.000	0.000	0.000
40	A	321	LEU	0	0.042	0.017	11.466	-0.031	-0.031	0.000	0.000	0.000	0.000
41	A	322	LEU	0	-0.022	-0.003	9.501	0.117	0.117	0.000	0.000	0.000	0.000
42	A	323	HIS	0	0.006	-0.004	8.215	-0.187	-0.187	0.000	0.000	0.000	0.000
43	A	324	GLU	-1	-0.931	-0.975	7.336	-0.232	-0.232	0.000	0.000	0.000	0.000
44	A	325	TYR	0	-0.061	-0.053	5.986	-0.222	-0.222	0.000	0.000	0.000	0.000
45	A	326	ARG	1	0.889	0.952	3.717	0.825	1.387	0.004	-0.185	-0.381	-0.001
46	A	327	ASN	0	-0.043	-0.022	3.139	-4.204	-3.542	0.126	-0.568	-0.220	-0.005
47	A	328	GLY	0	-0.049	-0.039	2.387	-0.891	-0.749	2.119	-1.634	-0.627	-0.003
48	A	329	ALA	0	-0.015	0.024	3.290	1.441	0.716	0.050	0.743	-0.068	-0.001
49	A	330	SER	0	-0.027	-0.040	5.645	0.807	0.807	0.000	0.000	0.000	0.000
50	A	331	ILE	0	0.032	0.007	7.646	-0.470	-0.470	0.000	0.000	0.000	0.000
51	A	332	HIS	0	0.037	0.021	9.206	-0.344	-0.344	0.000	0.000	0.000	0.000
52	A	333	GLU	-1	-0.831	-0.896	9.731	0.998	0.998	0.000	0.000	0.000	0.000
53	A	334	PHE	0	0.045	0.023	9.051	-0.236	-0.236	0.000	0.000	0.000	0.000
54	A	335	CYS	0	-0.043	-0.020	11.157	-0.201	-0.201	0.000	0.000	0.000	0.000
55	A	336	ILE	0	-0.015	-0.011	14.179	-0.137	-0.137	0.000	0.000	0.000	0.000
56	A	337	ASN	0	0.009	-0.001	13.187	-0.100	-0.100	0.000	0.000	0.000	0.000
57	A	338	LEU	0	0.009	0.015	13.197	-0.097	-0.097	0.000	0.000	0.000	0.000
58	A	339	ARG	1	0.862	0.908	16.544	-0.323	-0.323	0.000	0.000	0.000	0.000
59	A	340	GLN	0	-0.096	-0.038	18.410	-0.075	-0.075	0.000	0.000	0.000	0.000
60	A	341	LEU	0	-0.009	0.023	17.790	-0.030	-0.030	0.000	0.000	0.000	0.000
61	A	342	TYR	0	0.018	0.002	17.858	-0.024	-0.024	0.000	0.000	0.000	0.000
62	A	343	GLY	0	0.059	0.039	22.144	-0.024	-0.024	0.000	0.000	0.000	0.000
63	A	344	ASP	-1	-0.802	-0.904	24.748	0.218	0.218	0.000	0.000	0.000	0.000
64	A	345	SER	0	-0.023	-0.013	26.792	0.001	0.001	0.000	0.000	0.000	0.000
65	A	346	ARG	1	0.725	0.816	24.297	-0.127	-0.127	0.000	0.000	0.000	0.000
66	A	347	LYS	1	0.825	0.921	22.355	-0.220	-0.220	0.000	0.000	0.000	0.000
67	A	348	PHE	0	0.040	0.015	22.147	0.019	0.019	0.000	0.000	0.000	0.000
68	A	349	LEU	0	-0.022	-0.007	21.764	0.001	0.001	0.000	0.000	0.000	0.000
69	A	350	LEU	0	0.020	0.009	17.147	-0.003	-0.003	0.000	0.000	0.000	0.000
70	A	351	LEU	0	0.021	0.013	17.933	0.038	0.038	0.000	0.000	0.000	0.000
71	A	352	GLY	0	-0.019	-0.015	19.342	0.004	0.004	0.000	0.000	0.000	0.000
72	A	353	LEU	0	-0.028	-0.018	14.095	-0.031	-0.031	0.000	0.000	0.000	0.000
73	A	354	ARG	1	0.757	0.827	13.970	-0.276	-0.276	0.000	0.000	0.000	0.000
74	A	355	PRO	0	0.013	0.010	13.641	0.051	0.051	0.000	0.000	0.000	0.000
75	A	356	PHE	0	-0.041	-0.026	11.144	-0.103	-0.103	0.000	0.000	0.000	0.000
76	A	357	ILE	0	-0.033	0.008	8.933	0.082	0.082	0.000	0.000	0.000	0.000
77	A	358	PRO	0	0.017	0.017	5.059	-0.190	-0.190	0.000	0.000	0.000	0.000
78	A	359	GLU	-1	-0.866	-0.941	8.331	0.858	0.858	0.000	0.000	0.000	0.000
79	A	360	LYS	1	0.828	0.891	3.114	-11.682	-10.540	0.253	-0.661	-0.734	0.007
80	A	361	ASP	-1	-0.794	-0.855	6.255	5.244	5.244	0.000	0.000	0.000	0.000
81	A	362	SER	0	0.014	-0.005	9.537	-0.314	-0.314	0.000	0.000	0.000	0.000
82	A	363	GLN	0	0.004	-0.006	12.536	-0.118	-0.118	0.000	0.000	0.000	0.000
83	A	364	HIS	0	-0.025	-0.018	12.251	-0.023	-0.023	0.000	0.000	0.000	0.000
84	A	365	PHE	0	0.034	0.011	12.729	-0.082	-0.082	0.000	0.000	0.000	0.000
85	A	366	GLU	-1	-0.741	-0.842	14.639	0.299	0.299	0.000	0.000	0.000	0.000
86	A	367	ASN	0	0.052	0.031	17.552	-0.103	-0.103	0.000	0.000	0.000	0.000
87	A	368	PHE	0	-0.005	0.013	16.280	-0.066	-0.066	0.000	0.000	0.000	0.000
88	A	369	LEU	0	-0.011	-0.003	17.902	-0.067	-0.067	0.000	0.000	0.000	0.000
89	A	370	GLU	-1	-0.869	-0.928	20.231	0.291	0.291	0.000	0.000	0.000	0.000
90	A	371	THR	0	-0.057	-0.037	21.354	-0.036	-0.036	0.000	0.000	0.000	0.000
91	A	372	ILE	0	-0.073	-0.026	20.132	-0.035	-0.035	0.000	0.000	0.000	0.000
92	A	373	GLY	0	-0.022	-0.003	23.611	-0.032	-0.032	0.000	0.000	0.000	0.000
93	A	374	VAL	0	-0.089	-0.049	22.270	-0.030	-0.030	0.000	0.000	0.000	0.000
94	A	375	LYS	1	0.819	0.885	21.138	-0.337	-0.337	0.000	0.000	0.000	0.000
95	A	376	ASP	-1	-0.827	-0.871	23.947	0.210	0.210	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:282:GLY)