FMO DATABASE

FMODB ID: 66MYZ

Calculation Name: 4HTJ-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4HTJ

Chain ID: A

ChEMBL ID:

UniProt ID: Q92932

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:

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	89
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-588994.856911
FMO2-HF: Nuclear repulsion	555802.41033
FMO2-HF: Total energy	-33192.446581
FMO2-MP2: Total energy	-33291.630552

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:510:ALA)

Summations of interaction energy for fragment #1(A:510:ALA)

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.
-24.635	-20.008	2.488	-2.929	-4.186	0.013

Interaction energy analysis for fragmet #1(A:510:ALA)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.022 / q_NPA : -0.002

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	512	GLY	0	0.095	0.049	3.819	-1.854	-0.333	-0.020	-0.716	-0.786	0.001
4	A	513	TYR	0	-0.094	-0.064	6.150	0.609	0.609	0.000	0.000	0.000	0.000
5	A	514	ILE	0	0.029	0.017	9.677	-0.102	-0.102	0.000	0.000	0.000	0.000
6	A	515	VAL	0	-0.017	-0.006	13.042	0.087	0.087	0.000	0.000	0.000	0.000
7	A	516	THR	0	0.001	-0.007	15.914	-0.023	-0.023	0.000	0.000	0.000	0.000
8	A	517	ASP	-1	-0.834	-0.927	19.338	-0.090	-0.090	0.000	0.000	0.000	0.000
9	A	518	ARG	1	0.826	0.903	22.045	0.061	0.061	0.000	0.000	0.000	0.000
10	A	519	ASP	-1	-0.866	-0.928	22.057	0.030	0.030	0.000	0.000	0.000	0.000
11	A	520	PRO	0	-0.085	-0.049	22.388	0.003	0.003	0.000	0.000	0.000	0.000
12	A	521	LEU	0	-0.030	-0.011	17.549	-0.006	-0.006	0.000	0.000	0.000	0.000
13	A	522	ARG	1	0.919	0.950	20.776	-0.027	-0.027	0.000	0.000	0.000	0.000
14	A	523	PRO	0	0.043	0.011	19.510	-0.014	-0.014	0.000	0.000	0.000	0.000
15	A	524	GLU	-1	-0.880	-0.953	19.816	0.036	0.036	0.000	0.000	0.000	0.000
16	A	525	GLU	-1	-0.827	-0.901	21.807	-0.040	-0.040	0.000	0.000	0.000	0.000
17	A	526	GLY	0	0.065	0.035	17.737	-0.029	-0.029	0.000	0.000	0.000	0.000
18	A	527	ARG	1	0.882	0.937	15.782	-0.084	-0.084	0.000	0.000	0.000	0.000
19	A	528	ARG	1	0.930	0.964	18.328	-0.006	-0.006	0.000	0.000	0.000	0.000
20	A	529	LEU	0	0.078	0.049	16.673	-0.020	-0.020	0.000	0.000	0.000	0.000
21	A	530	VAL	0	-0.005	-0.003	13.245	-0.043	-0.043	0.000	0.000	0.000	0.000
22	A	531	GLU	-1	-0.871	-0.942	15.579	-0.086	-0.086	0.000	0.000	0.000	0.000
23	A	532	ASP	-1	-0.816	-0.901	18.103	-0.171	-0.171	0.000	0.000	0.000	0.000
24	A	533	VAL	0	0.014	0.008	13.357	-0.012	-0.012	0.000	0.000	0.000	0.000
25	A	534	ALA	0	-0.042	-0.018	14.993	-0.037	-0.037	0.000	0.000	0.000	0.000
26	A	535	ARG	1	0.841	0.896	15.878	0.161	0.161	0.000	0.000	0.000	0.000
27	A	536	LEU	0	-0.029	-0.001	18.040	0.011	0.011	0.000	0.000	0.000	0.000
28	A	537	LEU	0	-0.013	0.002	12.342	-0.011	-0.011	0.000	0.000	0.000	0.000
29	A	538	GLN	0	-0.078	-0.032	16.502	0.017	0.017	0.000	0.000	0.000	0.000
30	A	539	VAL	0	0.040	0.028	13.045	0.003	0.003	0.000	0.000	0.000	0.000
31	A	540	PRO	0	0.010	0.009	16.185	0.017	0.017	0.000	0.000	0.000	0.000
32	A	541	SER	0	0.043	0.004	15.596	-0.023	-0.023	0.000	0.000	0.000	0.000
33	A	542	SER	0	-0.045	-0.024	14.970	0.003	0.003	0.000	0.000	0.000	0.000
34	A	543	ALA	0	0.004	0.009	12.104	0.063	0.063	0.000	0.000	0.000	0.000
35	A	544	PHE	0	-0.032	-0.013	10.453	-0.060	-0.060	0.000	0.000	0.000	0.000
36	A	545	ALA	0	0.004	0.002	8.777	0.062	0.062	0.000	0.000	0.000	0.000
37	A	546	ASP	-1	-0.927	-0.982	8.858	1.557	1.557	0.000	0.000	0.000	0.000
38	A	547	VAL	0	-0.034	-0.013	11.106	0.006	0.006	0.000	0.000	0.000	0.000
39	A	548	GLU	-1	-0.876	-0.914	11.550	0.961	0.961	0.000	0.000	0.000	0.000
40	A	549	VAL	0	-0.002	0.002	13.796	-0.081	-0.081	0.000	0.000	0.000	0.000
41	A	550	LEU	0	-0.057	-0.028	12.482	0.061	0.061	0.000	0.000	0.000	0.000
42	A	551	GLY	0	0.018	0.026	16.467	-0.037	-0.037	0.000	0.000	0.000	0.000
43	A	552	PRO	0	0.091	0.038	18.304	0.000	0.000	0.000	0.000	0.000	0.000
44	A	553	ALA	0	-0.019	0.004	13.865	-0.048	-0.048	0.000	0.000	0.000	0.000
45	A	554	VAL	0	0.011	0.017	13.409	0.075	0.075	0.000	0.000	0.000	0.000
46	A	555	THR	0	-0.036	-0.025	8.891	-0.005	-0.005	0.000	0.000	0.000	0.000
47	A	556	PHE	0	0.069	0.025	7.961	0.138	0.138	0.000	0.000	0.000	0.000
48	A	557	LYS	1	0.911	0.968	2.654	-18.679	-17.183	1.626	-1.445	-1.677	0.018
49	A	558	VAL	0	0.003	0.019	5.465	0.195	0.195	0.000	0.000	0.000	0.000
50	A	559	SER	0	-0.031	-0.009	6.226	-0.151	-0.151	0.000	0.000	0.000	0.000
51	A	560	ALA	0	0.024	-0.006	8.391	-0.193	-0.193	0.000	0.000	0.000	0.000
52	A	561	ASN	0	-0.018	-0.028	10.321	0.162	0.162	0.000	0.000	0.000	0.000
53	A	562	VAL	0	-0.004	-0.022	13.415	-0.027	-0.027	0.000	0.000	0.000	0.000
54	A	563	GLN	0	-0.024	0.001	14.635	0.012	0.012	0.000	0.000	0.000	0.000
55	A	564	ASN	0	-0.091	-0.039	12.559	-0.027	-0.027	0.000	0.000	0.000	0.000
56	A	565	VAL	0	0.011	0.024	9.993	-0.107	-0.107	0.000	0.000	0.000	0.000
57	A	566	THR	0	0.003	-0.027	5.711	-0.134	-0.134	0.000	0.000	0.000	0.000
58	A	567	THR	0	-0.013	-0.023	2.927	0.485	1.106	0.062	-0.225	-0.458	-0.001
59	A	568	GLU	-1	-0.846	-0.926	3.812	-4.395	-3.934	0.005	-0.146	-0.320	-0.001
60	A	569	ASP	-1	-0.812	-0.863	7.109	-0.814	-0.814	0.000	0.000	0.000	0.000
61	A	570	VAL	0	-0.001	0.000	8.380	0.231	0.231	0.000	0.000	0.000	0.000
62	A	571	GLU	-1	-0.916	-0.948	8.132	-1.017	-1.017	0.000	0.000	0.000	0.000
63	A	572	LYS	1	0.889	0.932	10.071	1.205	1.205	0.000	0.000	0.000	0.000
64	A	573	ALA	0	0.038	0.029	12.726	0.116	0.116	0.000	0.000	0.000	0.000
65	A	574	THR	0	-0.022	-0.032	12.714	0.119	0.119	0.000	0.000	0.000	0.000
66	A	575	VAL	0	-0.053	-0.030	13.611	0.086	0.086	0.000	0.000	0.000	0.000
67	A	576	ASP	-1	-0.906	-0.957	16.114	-0.442	-0.442	0.000	0.000	0.000	0.000
68	A	577	ASN	0	-0.117	-0.063	17.906	0.093	0.093	0.000	0.000	0.000	0.000
69	A	578	LYS	1	0.896	0.953	18.624	0.279	0.279	0.000	0.000	0.000	0.000
70	A	579	ASP	-1	-0.898	-0.955	19.971	-0.196	-0.196	0.000	0.000	0.000	0.000
71	A	580	LYS	1	0.952	0.961	22.617	0.279	0.279	0.000	0.000	0.000	0.000
72	A	581	LEU	0	-0.002	0.024	17.250	0.016	0.016	0.000	0.000	0.000	0.000
73	A	582	GLU	-1	-0.768	-0.833	21.450	-0.178	-0.178	0.000	0.000	0.000	0.000
74	A	583	GLU	-1	-0.999	-0.988	23.366	-0.117	-0.117	0.000	0.000	0.000	0.000
75	A	584	THR	0	-0.116	-0.069	23.317	0.014	0.014	0.000	0.000	0.000	0.000
76	A	585	SER	0	-0.044	-0.053	21.946	0.018	0.018	0.000	0.000	0.000	0.000
77	A	586	GLY	0	-0.031	0.001	24.041	0.017	0.017	0.000	0.000	0.000	0.000
78	A	587	LEU	0	-0.070	-0.027	20.177	0.015	0.015	0.000	0.000	0.000	0.000
79	A	588	LYS	1	0.846	0.911	22.814	0.129	0.129	0.000	0.000	0.000	0.000
80	A	589	ILE	0	0.014	-0.002	16.552	0.002	0.002	0.000	0.000	0.000	0.000
81	A	590	LEU	0	-0.060	-0.043	18.381	-0.003	-0.003	0.000	0.000	0.000	0.000
82	A	591	GLN	0	-0.004	0.005	13.575	-0.019	-0.019	0.000	0.000	0.000	0.000
83	A	592	THR	0	0.014	0.016	11.578	0.061	0.061	0.000	0.000	0.000	0.000
84	A	593	GLY	0	0.041	0.031	8.882	0.093	0.093	0.000	0.000	0.000	0.000
85	A	594	VAL	0	-0.008	-0.001	2.433	-0.943	-0.562	0.816	-0.388	-0.809	-0.004
86	A	595	GLY	0	-0.014	0.000	5.031	0.502	0.502	0.000	0.000	0.000	0.000
87	A	596	SER	0	-0.017	-0.017	4.622	-0.421	-0.274	-0.001	-0.009	-0.136	0.000
88	A	597	LYS	1	0.928	0.960	5.291	-1.731	-1.731	0.000	0.000	0.000	0.000
89	A	598	SER	0	0.027	0.021	7.505	-0.222	-0.222	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:510:ALA)