FMO DATABASE

FMODB ID: JQ4Z9

Calculation Name: 2H36-X-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2H36

Chain ID: X

ChEMBL ID:

UniProt ID: Q914L6

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	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	108
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-862135.33181
FMO2-HF: Nuclear repulsion	816540.144862
FMO2-HF: Total energy	-45595.186948
FMO2-MP2: Total energy	-45729.191736

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(X:2:LYS)

Summations of interaction energy for fragment #1(X:2:LYS)

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.
-178.345	-173.2	0.081	-2.481	-2.745	-0.014

Interaction energy analysis for fragmet #1(X:2:LYS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.931 / q_NPA : 0.950

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	X	4	ASP	-1	-0.870	-0.923	3.312	-43.333	-38.188	0.081	-2.481	-2.745	-0.014
4	X	5	LEU	0	-0.015	-0.008	4.912	2.840	2.840	0.000	0.000	0.000	0.000
5	X	6	GLU	-1	-0.859	-0.923	7.165	-23.687	-23.687	0.000	0.000	0.000	0.000
6	X	7	LYS	1	0.837	0.907	8.502	21.147	21.147	0.000	0.000	0.000	0.000
7	X	8	ILE	0	-0.048	-0.024	8.064	1.322	1.322	0.000	0.000	0.000	0.000
8	X	9	GLU	-1	-0.954	-0.969	11.129	-22.067	-22.067	0.000	0.000	0.000	0.000
9	X	10	SER	0	-0.077	-0.041	12.890	1.363	1.363	0.000	0.000	0.000	0.000
10	X	11	ASP	-1	-0.925	-0.948	13.973	-16.315	-16.315	0.000	0.000	0.000	0.000
11	X	12	ILE	0	-0.029	-0.009	15.778	0.296	0.296	0.000	0.000	0.000	0.000
12	X	13	ILE	0	-0.058	-0.013	18.325	-0.065	-0.065	0.000	0.000	0.000	0.000
13	X	14	ASN	0	-0.028	0.002	21.121	-0.099	-0.099	0.000	0.000	0.000	0.000
14	X	15	ASP	-1	-0.901	-0.998	23.219	-11.561	-11.561	0.000	0.000	0.000	0.000
15	X	16	TRP	0	-0.125	-0.054	26.069	-0.057	-0.057	0.000	0.000	0.000	0.000
16	X	17	THR	0	-0.051	-0.027	28.310	-0.265	-0.265	0.000	0.000	0.000	0.000
17	X	18	GLU	-1	-0.895	-0.968	30.930	-8.443	-8.443	0.000	0.000	0.000	0.000
18	X	19	ALA	0	-0.006	-0.011	34.276	0.247	0.247	0.000	0.000	0.000	0.000
19	X	20	ASP	-1	-0.774	-0.895	31.439	-9.217	-9.217	0.000	0.000	0.000	0.000
20	X	21	ASP	-1	-0.914	-0.939	34.762	-8.172	-8.172	0.000	0.000	0.000	0.000
21	X	22	LEU	0	-0.063	-0.034	36.314	0.264	0.264	0.000	0.000	0.000	0.000
22	X	23	ASP	-1	-0.883	-0.951	37.941	-7.525	-7.525	0.000	0.000	0.000	0.000
23	X	24	ASP	-1	-0.922	-0.952	37.463	-7.679	-7.679	0.000	0.000	0.000	0.000
24	X	25	ALA	0	-0.039	-0.019	39.584	0.205	0.205	0.000	0.000	0.000	0.000
25	X	26	LEU	0	-0.062	-0.046	42.438	0.251	0.251	0.000	0.000	0.000	0.000
26	X	27	ASP	-1	-0.852	-0.925	41.916	-6.957	-6.957	0.000	0.000	0.000	0.000
27	X	28	PHE	0	-0.075	-0.040	44.045	0.246	0.246	0.000	0.000	0.000	0.000
28	X	29	LEU	0	-0.083	-0.060	45.765	0.200	0.200	0.000	0.000	0.000	0.000
29	X	30	PHE	0	0.053	0.031	46.968	0.157	0.157	0.000	0.000	0.000	0.000
30	X	31	MET	0	-0.049	-0.005	47.736	0.155	0.155	0.000	0.000	0.000	0.000
31	X	32	GLU	-1	-0.916	-0.964	50.824	-5.429	-5.429	0.000	0.000	0.000	0.000
32	X	33	LYS	1	0.846	0.913	51.148	5.996	5.996	0.000	0.000	0.000	0.000
33	X	34	VAL	0	-0.049	-0.005	50.744	0.098	0.098	0.000	0.000	0.000	0.000
34	X	35	SER	0	0.015	0.003	54.121	-0.004	-0.004	0.000	0.000	0.000	0.000
35	X	36	GLU	-1	-0.960	-0.989	54.826	-5.274	-5.274	0.000	0.000	0.000	0.000
36	X	37	PHE	0	-0.027	0.004	47.962	0.005	0.005	0.000	0.000	0.000	0.000
37	X	38	LYS	1	0.811	0.881	51.306	5.794	5.794	0.000	0.000	0.000	0.000
38	X	39	ILE	0	-0.016	0.001	44.924	0.017	0.017	0.000	0.000	0.000	0.000
39	X	40	LYS	1	0.899	0.954	48.064	5.862	5.862	0.000	0.000	0.000	0.000
40	X	41	PHE	0	0.001	-0.004	41.406	-0.010	-0.010	0.000	0.000	0.000	0.000
41	X	42	LYS	1	0.779	0.875	43.031	7.062	7.062	0.000	0.000	0.000	0.000
42	X	43	ASP	-1	-0.870	-0.915	40.478	-7.192	-7.192	0.000	0.000	0.000	0.000
43	X	44	PRO	0	-0.017	-0.014	40.940	0.007	0.007	0.000	0.000	0.000	0.000
44	X	45	LEU	0	0.030	0.023	37.538	-0.124	-0.124	0.000	0.000	0.000	0.000
45	X	46	LYS	1	0.881	0.944	33.584	9.048	9.048	0.000	0.000	0.000	0.000
46	X	47	VAL	0	0.080	0.056	35.686	-0.088	-0.088	0.000	0.000	0.000	0.000
47	X	48	THR	0	-0.068	-0.062	32.390	0.132	0.132	0.000	0.000	0.000	0.000
48	X	49	GLU	-1	-0.850	-0.954	35.810	-7.872	-7.872	0.000	0.000	0.000	0.000
49	X	50	GLU	-1	-0.979	-1.003	32.767	-9.156	-9.156	0.000	0.000	0.000	0.000
50	X	51	GLU	-1	-0.662	-0.775	32.905	-9.180	-9.180	0.000	0.000	0.000	0.000
51	X	52	TYR	0	-0.046	-0.060	36.440	0.146	0.146	0.000	0.000	0.000	0.000
52	X	53	ARG	1	0.890	0.942	37.522	8.337	8.337	0.000	0.000	0.000	0.000
53	X	54	GLU	-1	-0.974	-0.986	35.303	-8.654	-8.654	0.000	0.000	0.000	0.000
54	X	55	LEU	0	-0.004	0.016	38.542	0.081	0.081	0.000	0.000	0.000	0.000
55	X	56	LEU	0	-0.102	-0.022	41.443	0.192	0.192	0.000	0.000	0.000	0.000
56	X	57	GLY	0	0.028	0.015	43.296	0.162	0.162	0.000	0.000	0.000	0.000
57	X	58	ASN	0	-0.086	-0.050	44.382	0.012	0.012	0.000	0.000	0.000	0.000
58	X	59	TYR	0	0.035	0.056	46.674	0.034	0.034	0.000	0.000	0.000	0.000
59	X	60	ASP	-1	-0.824	-0.916	50.463	-5.941	-5.941	0.000	0.000	0.000	0.000
60	X	61	SER	0	-0.090	-0.059	53.809	0.067	0.067	0.000	0.000	0.000	0.000
61	X	62	SER	0	0.013	0.007	50.988	-0.035	-0.035	0.000	0.000	0.000	0.000
62	X	63	ASN	0	-0.070	-0.024	53.709	0.088	0.088	0.000	0.000	0.000	0.000
63	X	64	SER	0	0.032	0.028	50.949	-0.013	-0.013	0.000	0.000	0.000	0.000
64	X	65	VAL	0	-0.051	-0.017	53.567	0.089	0.089	0.000	0.000	0.000	0.000
65	X	66	SER	0	0.022	-0.004	51.557	-0.089	-0.089	0.000	0.000	0.000	0.000
66	X	67	SER	0	-0.026	0.016	53.603	0.027	0.027	0.000	0.000	0.000	0.000
67	X	68	ASN	0	-0.033	-0.038	53.576	-0.040	-0.040	0.000	0.000	0.000	0.000
68	X	69	GLY	0	0.013	-0.008	49.245	-0.042	-0.042	0.000	0.000	0.000	0.000
69	X	70	ILE	0	-0.040	-0.015	48.428	-0.130	-0.130	0.000	0.000	0.000	0.000
70	X	71	THR	0	0.012	0.009	48.408	0.156	0.156	0.000	0.000	0.000	0.000
71	X	72	ILE	0	-0.026	0.005	49.871	-0.079	-0.079	0.000	0.000	0.000	0.000
72	X	73	ASP	-1	-0.774	-0.878	47.950	-6.474	-6.474	0.000	0.000	0.000	0.000
73	X	74	GLN	0	-0.023	-0.017	50.988	0.023	0.023	0.000	0.000	0.000	0.000
74	X	75	TYR	0	-0.024	-0.044	47.802	-0.036	-0.036	0.000	0.000	0.000	0.000
75	X	76	THR	0	0.004	0.004	52.057	0.097	0.097	0.000	0.000	0.000	0.000
76	X	77	TYR	0	-0.029	-0.046	47.274	-0.046	-0.046	0.000	0.000	0.000	0.000
77	X	78	ASP	-1	-0.916	-0.957	53.826	-5.389	-5.389	0.000	0.000	0.000	0.000
78	X	79	GLU	-1	-0.840	-0.916	54.468	-5.772	-5.772	0.000	0.000	0.000	0.000
79	X	80	ASP	-1	-0.957	-0.976	57.036	-5.426	-5.426	0.000	0.000	0.000	0.000
80	X	81	ASP	-1	-1.003	-1.011	59.749	-4.943	-4.943	0.000	0.000	0.000	0.000
81	X	82	ASP	-1	-0.971	-0.980	62.865	-4.814	-4.814	0.000	0.000	0.000	0.000
82	X	83	ILE	0	-0.062	-0.022	58.985	0.072	0.072	0.000	0.000	0.000	0.000
83	X	84	MET	0	0.011	0.018	58.174	-0.083	-0.083	0.000	0.000	0.000	0.000
84	X	85	TYR	0	0.011	0.004	51.428	0.027	0.027	0.000	0.000	0.000	0.000
85	X	86	LYS	1	0.841	0.922	54.453	5.417	5.417	0.000	0.000	0.000	0.000
86	X	87	LEU	0	0.023	0.020	46.715	0.001	0.001	0.000	0.000	0.000	0.000
87	X	88	GLU	-1	-0.884	-0.955	51.017	-5.691	-5.691	0.000	0.000	0.000	0.000
88	X	89	PHE	0	0.054	0.018	43.876	-0.047	-0.047	0.000	0.000	0.000	0.000
89	X	90	THR	0	-0.026	-0.008	48.519	0.085	0.085	0.000	0.000	0.000	0.000
90	X	91	TYR	0	-0.053	-0.047	44.575	-0.161	-0.161	0.000	0.000	0.000	0.000
91	X	92	ARG	1	0.840	0.928	44.589	7.044	7.044	0.000	0.000	0.000	0.000
92	X	93	LYS	1	0.853	0.913	41.401	7.391	7.391	0.000	0.000	0.000	0.000
93	X	94	GLU	-1	-0.917	-0.907	40.838	-7.104	-7.104	0.000	0.000	0.000	0.000
94	X	95	ASP	-1	-0.754	-0.905	38.370	-7.700	-7.700	0.000	0.000	0.000	0.000
95	X	96	ASN	0	-0.116	-0.046	36.403	-0.493	-0.493	0.000	0.000	0.000	0.000
96	X	97	LYS	1	0.860	0.932	33.209	8.832	8.832	0.000	0.000	0.000	0.000
97	X	98	ILE	0	-0.003	-0.013	37.677	0.179	0.179	0.000	0.000	0.000	0.000
98	X	99	TYR	0	0.001	-0.005	37.217	-0.259	-0.259	0.000	0.000	0.000	0.000
99	X	100	ILE	0	0.062	0.032	41.210	0.244	0.244	0.000	0.000	0.000	0.000
100	X	101	TYR	0	-0.023	-0.029	43.467	-0.070	-0.070	0.000	0.000	0.000	0.000
101	X	102	GLU	-1	-0.899	-0.963	46.161	-5.837	-5.837	0.000	0.000	0.000	0.000
102	X	103	VAL	0	0.070	0.067	44.931	0.000	0.000	0.000	0.000	0.000	0.000
103	X	104	GLN	0	-0.033	0.001	48.291	0.107	0.107	0.000	0.000	0.000	0.000
104	X	105	GLY	0	0.084	0.045	51.344	-0.079	-0.079	0.000	0.000	0.000	0.000
105	X	106	TRP	0	-0.092	-0.055	52.640	0.034	0.034	0.000	0.000	0.000	0.000
106	X	107	ARG	1	0.824	0.925	53.196	5.665	5.665	0.000	0.000	0.000	0.000
107	X	108	GLU	-1	-0.912	-0.947	58.313	-5.137	-5.137	0.000	0.000	0.000	0.000
108	X	109	LYS	1	0.922	0.961	61.588	4.687	4.687	0.000	0.000	0.000	0.000

Top

Graph

Manual

About

Interactive mode: IFIE and PIEDA for fragment #1(X:2:LYS)