FMO DATABASE

FMODB ID: 22YNR

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	OptH
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	-587480.467822
FMO2-HF: Nuclear repulsion	554288.656274
FMO2-HF: Total energy	-33191.811548
FMO2-MP2: Total energy	-33291.007378

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.
-18.31	-13.72	0.876	-2.301	-3.164	0.011

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 : 0.028 / 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	0.093	0.055	3.819	-1.705	-0.149	-0.020	-0.741	-0.795	0.002
4	A	513	TYR	0	-0.099	-0.059	6.073	0.567	0.567	0.000	0.000	0.000	0.000
5	A	514	ILE	0	0.035	0.020	9.595	-0.091	-0.091	0.000	0.000	0.000	0.000
6	A	515	VAL	0	-0.025	-0.015	12.961	0.079	0.079	0.000	0.000	0.000	0.000
7	A	516	THR	0	0.008	0.004	15.830	-0.021	-0.021	0.000	0.000	0.000	0.000
8	A	517	ASP	-1	-0.841	-0.936	19.255	-0.084	-0.084	0.000	0.000	0.000	0.000
9	A	518	ARG	1	0.861	0.935	21.950	0.063	0.063	0.000	0.000	0.000	0.000
10	A	519	ASP	-1	-0.895	-0.938	21.982	0.030	0.030	0.000	0.000	0.000	0.000
11	A	520	PRO	0	-0.065	-0.043	22.376	0.004	0.004	0.000	0.000	0.000	0.000
12	A	521	LEU	0	-0.027	-0.008	17.565	-0.007	-0.007	0.000	0.000	0.000	0.000
13	A	522	ARG	1	0.892	0.935	20.776	-0.021	-0.021	0.000	0.000	0.000	0.000
14	A	523	PRO	0	0.041	0.012	19.504	-0.015	-0.015	0.000	0.000	0.000	0.000
15	A	524	GLU	-1	-0.893	-0.956	19.816	0.013	0.013	0.000	0.000	0.000	0.000
16	A	525	GLU	-1	-0.840	-0.930	21.807	-0.048	-0.048	0.000	0.000	0.000	0.000
17	A	526	GLY	0	0.060	0.033	17.736	-0.027	-0.027	0.000	0.000	0.000	0.000
18	A	527	ARG	1	0.929	0.969	16.037	-0.049	-0.049	0.000	0.000	0.000	0.000
19	A	528	ARG	1	0.931	0.965	18.290	0.014	0.014	0.000	0.000	0.000	0.000
20	A	529	LEU	0	0.082	0.058	16.574	-0.020	-0.020	0.000	0.000	0.000	0.000
21	A	530	VAL	0	-0.007	-0.006	13.177	-0.043	-0.043	0.000	0.000	0.000	0.000
22	A	531	GLU	-1	-0.955	-1.004	15.535	-0.131	-0.131	0.000	0.000	0.000	0.000
23	A	532	ASP	-1	-0.860	-0.940	18.066	-0.191	-0.191	0.000	0.000	0.000	0.000
24	A	533	VAL	0	0.008	0.001	13.375	-0.011	-0.011	0.000	0.000	0.000	0.000
25	A	534	ALA	0	-0.031	-0.015	14.966	-0.036	-0.036	0.000	0.000	0.000	0.000
26	A	535	ARG	1	0.885	0.941	15.843	0.184	0.184	0.000	0.000	0.000	0.000
27	A	536	LEU	0	-0.035	-0.007	17.925	0.015	0.015	0.000	0.000	0.000	0.000
28	A	537	LEU	0	-0.024	-0.001	12.315	-0.006	-0.006	0.000	0.000	0.000	0.000
29	A	538	GLN	0	-0.065	-0.019	16.468	0.016	0.016	0.000	0.000	0.000	0.000
30	A	539	VAL	0	0.043	0.029	12.996	0.001	0.001	0.000	0.000	0.000	0.000
31	A	540	PRO	0	0.017	0.013	16.151	0.020	0.020	0.000	0.000	0.000	0.000
32	A	541	SER	0	0.086	0.032	15.583	-0.033	-0.033	0.000	0.000	0.000	0.000
33	A	542	SER	0	-0.051	-0.024	14.901	-0.008	-0.008	0.000	0.000	0.000	0.000
34	A	543	ALA	0	0.004	0.010	11.938	0.052	0.052	0.000	0.000	0.000	0.000
35	A	544	PHE	0	-0.034	-0.016	10.385	-0.099	-0.099	0.000	0.000	0.000	0.000
36	A	545	ALA	0	-0.001	-0.003	8.691	0.094	0.094	0.000	0.000	0.000	0.000
37	A	546	ASP	-1	-0.936	-0.985	9.064	1.270	1.270	0.000	0.000	0.000	0.000
38	A	547	VAL	0	-0.039	-0.017	11.067	0.016	0.016	0.000	0.000	0.000	0.000
39	A	548	GLU	-1	-0.965	-0.969	12.341	0.745	0.745	0.000	0.000	0.000	0.000
40	A	549	VAL	0	-0.013	-0.009	13.796	-0.081	-0.081	0.000	0.000	0.000	0.000
41	A	550	LEU	0	-0.046	-0.023	12.250	0.060	0.060	0.000	0.000	0.000	0.000
42	A	551	GLY	0	0.011	0.022	16.460	-0.033	-0.033	0.000	0.000	0.000	0.000
43	A	552	PRO	0	0.091	0.039	18.241	-0.003	-0.003	0.000	0.000	0.000	0.000
44	A	553	ALA	0	-0.013	0.003	13.845	-0.046	-0.046	0.000	0.000	0.000	0.000
45	A	554	VAL	0	0.013	0.020	13.317	0.068	0.068	0.000	0.000	0.000	0.000
46	A	555	THR	0	-0.058	-0.038	8.937	-0.016	-0.016	0.000	0.000	0.000	0.000
47	A	556	PHE	0	0.065	0.019	7.806	0.137	0.137	0.000	0.000	0.000	0.000
48	A	557	LYS	1	0.894	0.957	3.141	-13.010	-11.190	0.096	-1.060	-0.856	0.012
49	A	558	VAL	0	0.016	0.027	5.414	0.311	0.311	0.000	0.000	0.000	0.000
50	A	559	SER	0	-0.044	-0.015	6.190	-0.234	-0.234	0.000	0.000	0.000	0.000
51	A	560	ALA	0	0.047	0.008	8.346	-0.148	-0.148	0.000	0.000	0.000	0.000
52	A	561	ASN	0	-0.035	-0.037	10.311	0.183	0.183	0.000	0.000	0.000	0.000
53	A	562	VAL	0	0.001	-0.020	13.403	-0.019	-0.019	0.000	0.000	0.000	0.000
54	A	563	GLN	0	-0.036	-0.009	14.718	0.018	0.018	0.000	0.000	0.000	0.000
55	A	564	ASN	0	-0.095	-0.041	12.381	-0.062	-0.062	0.000	0.000	0.000	0.000
56	A	565	VAL	0	0.025	0.036	9.966	-0.088	-0.088	0.000	0.000	0.000	0.000
57	A	566	THR	0	0.016	-0.010	5.604	-0.040	-0.040	0.000	0.000	0.000	0.000
58	A	567	THR	0	-0.010	-0.024	3.091	0.427	0.931	0.071	-0.151	-0.424	0.000
59	A	568	GLU	-1	-0.860	-0.932	4.711	-3.053	-2.853	-0.001	-0.010	-0.189	0.000
60	A	569	ASP	-1	-0.863	-0.906	7.094	-0.745	-0.745	0.000	0.000	0.000	0.000
61	A	570	VAL	0	-0.028	-0.020	8.421	0.226	0.226	0.000	0.000	0.000	0.000
62	A	571	GLU	-1	-0.895	-0.946	8.281	-0.924	-0.924	0.000	0.000	0.000	0.000
63	A	572	LYS	1	0.945	0.967	10.020	0.982	0.982	0.000	0.000	0.000	0.000
64	A	573	ALA	0	0.033	0.029	12.690	0.110	0.110	0.000	0.000	0.000	0.000
65	A	574	THR	0	-0.020	-0.018	12.736	0.113	0.113	0.000	0.000	0.000	0.000
66	A	575	VAL	0	-0.053	-0.030	13.627	0.083	0.083	0.000	0.000	0.000	0.000
67	A	576	ASP	-1	-0.907	-0.956	16.060	-0.409	-0.409	0.000	0.000	0.000	0.000
68	A	577	ASN	0	-0.136	-0.085	17.823	0.085	0.085	0.000	0.000	0.000	0.000
69	A	578	LYS	1	0.982	1.012	18.846	0.276	0.276	0.000	0.000	0.000	0.000
70	A	579	ASP	-1	-0.883	-0.946	19.910	-0.182	-0.182	0.000	0.000	0.000	0.000
71	A	580	LYS	1	0.952	0.963	22.588	0.263	0.263	0.000	0.000	0.000	0.000
72	A	581	LEU	0	-0.002	0.014	17.347	0.012	0.012	0.000	0.000	0.000	0.000
73	A	582	GLU	-1	-0.855	-0.896	21.388	-0.177	-0.177	0.000	0.000	0.000	0.000
74	A	583	GLU	-1	-1.001	-0.993	23.297	-0.116	-0.116	0.000	0.000	0.000	0.000
75	A	584	THR	0	-0.115	-0.055	23.270	0.012	0.012	0.000	0.000	0.000	0.000
76	A	585	SER	0	-0.046	-0.055	21.863	0.019	0.019	0.000	0.000	0.000	0.000
77	A	586	GLY	0	-0.028	0.002	23.973	0.016	0.016	0.000	0.000	0.000	0.000
78	A	587	LEU	0	-0.077	-0.031	20.205	0.016	0.016	0.000	0.000	0.000	0.000
79	A	588	LYS	1	0.912	0.959	22.736	0.113	0.113	0.000	0.000	0.000	0.000
80	A	589	ILE	0	-0.010	-0.020	16.472	0.001	0.001	0.000	0.000	0.000	0.000
81	A	590	LEU	0	-0.059	-0.041	18.332	-0.001	-0.001	0.000	0.000	0.000	0.000
82	A	591	GLN	0	-0.016	-0.003	13.279	-0.017	-0.017	0.000	0.000	0.000	0.000
83	A	592	THR	0	0.010	0.010	11.470	0.049	0.049	0.000	0.000	0.000	0.000
84	A	593	GLY	0	0.050	0.040	8.810	0.094	0.094	0.000	0.000	0.000	0.000
85	A	594	VAL	0	-0.005	-0.004	2.528	-1.002	-0.639	0.731	-0.328	-0.766	-0.003
86	A	595	GLY	0	-0.012	0.000	4.955	0.478	0.478	0.000	0.000	0.000	0.000
87	A	596	SER	0	0.000	-0.005	4.607	-0.290	-0.143	-0.001	-0.011	-0.134	0.000
88	A	597	LYS	1	0.904	0.943	5.095	-2.069	-2.069	0.000	0.000	0.000	0.000
89	A	598	SER	0	0.036	0.027	7.509	-0.234	-0.234	0.000	0.000	0.000	0.000

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