FMO DATABASE

FMODB ID: YY182

Calculation Name: 2EHW-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2EHW

Chain ID: A

ChEMBL ID:

UniProt ID: Q53WA3

Base Structure: X-ray

Registration Date: 2023-03-13

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	115
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-856230.619789
FMO2-HF: Nuclear repulsion	810861.883845
FMO2-HF: Total energy	-45368.735944
FMO2-MP2: Total energy	-45503.184938

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:CYS)

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

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.
-11.126	-4.815	7.826	-5.715	-8.422	-0.017

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

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 : -0.004

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	GLU	-1	-0.771	-0.884	3.331	1.924	4.032	0.048	-0.808	-1.348	0.001
4	A	6	LEU	0	-0.033	-0.018	2.468	-0.614	0.720	0.979	-0.546	-1.766	0.001
5	A	7	SER	0	0.022	0.008	3.323	0.590	1.150	0.015	-0.194	-0.381	0.000
6	A	8	ALA	0	0.005	0.008	5.580	1.128	1.128	0.000	0.000	0.000	0.000
7	A	9	LEU	0	0.009	0.002	7.689	0.424	0.424	0.000	0.000	0.000	0.000
8	A	10	ARG	1	0.842	0.900	7.606	1.816	1.816	0.000	0.000	0.000	0.000
9	A	11	ILE	0	-0.014	-0.012	9.066	0.307	0.307	0.000	0.000	0.000	0.000
10	A	12	ALA	0	0.016	0.025	11.625	0.189	0.189	0.000	0.000	0.000	0.000
11	A	13	ILE	0	-0.044	-0.029	12.656	0.130	0.130	0.000	0.000	0.000	0.000
12	A	14	GLY	0	0.022	0.003	13.491	0.088	0.088	0.000	0.000	0.000	0.000
13	A	15	GLU	-1	-0.814	-0.899	15.062	-0.534	-0.534	0.000	0.000	0.000	0.000
14	A	16	LEU	0	-0.081	-0.027	17.267	0.068	0.068	0.000	0.000	0.000	0.000
15	A	17	LEU	0	-0.097	-0.046	16.392	0.049	0.049	0.000	0.000	0.000	0.000
16	A	18	GLU	-1	-0.988	-0.986	19.564	-0.280	-0.280	0.000	0.000	0.000	0.000
17	A	19	LYS	1	0.859	0.940	15.759	0.521	0.521	0.000	0.000	0.000	0.000
18	A	20	GLU	-1	-0.823	-0.905	18.424	-0.411	-0.411	0.000	0.000	0.000	0.000
19	A	21	ALA	0	0.019	0.000	17.039	-0.068	-0.068	0.000	0.000	0.000	0.000
20	A	22	HIS	0	-0.044	-0.028	15.497	-0.088	-0.088	0.000	0.000	0.000	0.000
21	A	23	ASP	-1	-0.918	-0.962	14.641	-0.627	-0.627	0.000	0.000	0.000	0.000
22	A	24	LEU	0	-0.083	-0.043	11.184	-0.131	-0.131	0.000	0.000	0.000	0.000
23	A	25	LEU	0	-0.005	0.008	11.062	-0.141	-0.141	0.000	0.000	0.000	0.000
24	A	26	HIS	0	0.037	0.001	8.331	-0.051	-0.051	0.000	0.000	0.000	0.000
25	A	27	GLU	-1	-0.799	-0.873	5.960	-2.214	-2.214	0.000	0.000	0.000	0.000
26	A	28	ARG	1	0.801	0.863	7.302	0.669	0.669	0.000	0.000	0.000	0.000
27	A	29	GLU	-1	-0.954	-0.975	9.736	-0.568	-0.568	0.000	0.000	0.000	0.000
28	A	30	GLU	-1	-0.923	-0.953	3.294	-10.097	-8.304	0.114	-1.014	-0.893	-0.009
29	A	31	LEU	0	-0.012	-0.013	6.836	0.541	0.541	0.000	0.000	0.000	0.000
30	A	32	ALA	0	-0.014	-0.002	8.152	0.436	0.436	0.000	0.000	0.000	0.000
31	A	33	PRO	0	-0.041	-0.018	9.554	0.175	0.175	0.000	0.000	0.000	0.000
32	A	34	VAL	0	-0.009	-0.005	7.071	0.159	0.159	0.000	0.000	0.000	0.000
33	A	35	LEU	0	0.002	0.002	10.392	0.123	0.123	0.000	0.000	0.000	0.000
34	A	36	GLY	0	-0.057	-0.016	12.477	0.027	0.027	0.000	0.000	0.000	0.000
35	A	37	GLN	0	-0.045	-0.037	12.632	0.033	0.033	0.000	0.000	0.000	0.000
36	A	38	ARG	1	0.772	0.877	6.634	-1.781	-1.781	0.000	0.000	0.000	0.000
37	A	39	PRO	0	0.026	0.003	12.762	-0.122	-0.122	0.000	0.000	0.000	0.000
38	A	40	GLU	-1	-0.736	-0.860	11.006	0.468	0.468	0.000	0.000	0.000	0.000
39	A	41	LEU	0	0.012	0.018	7.305	-0.155	-0.155	0.000	0.000	0.000	0.000
40	A	42	LYS	1	0.889	0.958	11.015	0.033	0.033	0.000	0.000	0.000	0.000
41	A	43	ARG	1	0.789	0.851	14.025	-0.073	-0.073	0.000	0.000	0.000	0.000
42	A	44	LEU	0	-0.023	-0.015	8.992	-0.017	-0.017	0.000	0.000	0.000	0.000
43	A	45	ALA	0	-0.002	-0.001	11.427	-0.053	-0.053	0.000	0.000	0.000	0.000
44	A	46	GLU	-1	-0.882	-0.949	13.081	-0.328	-0.328	0.000	0.000	0.000	0.000
45	A	47	ALA	0	0.008	0.036	16.101	0.067	0.067	0.000	0.000	0.000	0.000
46	A	48	LYS	1	0.856	0.906	17.907	0.389	0.389	0.000	0.000	0.000	0.000
47	A	49	THR	0	-0.005	0.003	20.680	0.008	0.008	0.000	0.000	0.000	0.000
48	A	50	LEU	0	0.107	0.046	18.693	-0.012	-0.012	0.000	0.000	0.000	0.000
49	A	51	PRO	0	-0.001	0.002	18.958	-0.004	-0.004	0.000	0.000	0.000	0.000
50	A	52	ALA	0	0.012	0.008	19.499	0.016	0.016	0.000	0.000	0.000	0.000
51	A	53	LEU	0	0.002	0.008	13.430	0.006	0.006	0.000	0.000	0.000	0.000
52	A	54	GLU	-1	-0.807	-0.917	14.806	-0.168	-0.168	0.000	0.000	0.000	0.000
53	A	55	GLU	-1	-0.897	-0.936	15.604	0.006	0.006	0.000	0.000	0.000	0.000
54	A	56	ALA	0	0.023	0.013	14.084	0.047	0.047	0.000	0.000	0.000	0.000
55	A	57	LEU	0	0.003	0.003	9.170	0.046	0.046	0.000	0.000	0.000	0.000
56	A	58	ARG	1	0.850	0.908	11.589	0.129	0.129	0.000	0.000	0.000	0.000
57	A	59	GLU	-1	-0.837	-0.874	13.908	0.142	0.142	0.000	0.000	0.000	0.000
58	A	60	ALA	0	-0.008	-0.014	8.495	0.112	0.112	0.000	0.000	0.000	0.000
59	A	61	LEU	0	-0.006	-0.008	9.312	0.275	0.275	0.000	0.000	0.000	0.000
60	A	62	LEU	0	-0.001	0.023	10.818	0.088	0.088	0.000	0.000	0.000	0.000
61	A	63	HIS	0	0.025	0.016	10.048	0.275	0.275	0.000	0.000	0.000	0.000
62	A	64	LEU	0	0.002	-0.001	5.822	0.171	0.171	0.000	0.000	0.000	0.000
63	A	65	GLU	-1	-0.936	-0.969	9.220	0.555	0.555	0.000	0.000	0.000	0.000
64	A	66	GLU	-1	-0.962	-0.990	12.449	0.558	0.558	0.000	0.000	0.000	0.000
65	A	67	ARG	1	0.793	0.878	8.788	-1.593	-1.593	0.000	0.000	0.000	0.000
66	A	68	ALA	0	0.013	-0.012	10.804	-0.052	-0.052	0.000	0.000	0.000	0.000
67	A	69	ALA	0	-0.066	-0.025	12.194	-0.125	-0.125	0.000	0.000	0.000	0.000
68	A	70	GLN	0	-0.070	-0.038	14.309	-0.011	-0.011	0.000	0.000	0.000	0.000
69	A	71	GLU	-1	-0.824	-0.866	11.232	1.190	1.190	0.000	0.000	0.000	0.000
70	A	72	PRO	0	-0.018	-0.014	13.590	0.039	0.039	0.000	0.000	0.000	0.000
71	A	73	GLU	-1	-0.893	-0.959	15.689	0.509	0.509	0.000	0.000	0.000	0.000
72	A	74	GLU	-1	-0.884	-0.923	9.633	0.863	0.863	0.000	0.000	0.000	0.000
73	A	75	PRO	0	-0.033	-0.024	11.514	0.086	0.086	0.000	0.000	0.000	0.000
74	A	76	TYR	0	0.004	0.000	1.830	-4.120	-4.504	4.840	-2.055	-2.402	-0.006
75	A	77	TRP	0	0.008	-0.011	4.885	0.395	0.395	0.000	0.000	0.000	0.000
76	A	78	ARG	1	0.928	0.964	8.217	-0.636	-0.636	0.000	0.000	0.000	0.000
77	A	79	GLY	0	-0.020	0.002	9.071	-0.147	-0.147	0.000	0.000	0.000	0.000
78	A	80	LEU	0	-0.055	-0.028	2.326	-1.385	-0.485	1.830	-1.098	-1.632	-0.004
79	A	81	LEU	0	0.025	0.014	6.030	-0.282	-0.282	0.000	0.000	0.000	0.000
80	A	82	LEU	0	0.033	0.025	8.747	-0.199	-0.199	0.000	0.000	0.000	0.000
81	A	83	ALA	0	-0.027	-0.016	6.595	-0.139	-0.139	0.000	0.000	0.000	0.000
82	A	84	VAL	0	-0.003	-0.020	5.381	-0.272	-0.272	0.000	0.000	0.000	0.000
83	A	85	GLU	-1	-0.885	-0.947	7.938	0.175	0.175	0.000	0.000	0.000	0.000
84	A	86	ALA	0	-0.036	-0.004	11.274	-0.045	-0.045	0.000	0.000	0.000	0.000
85	A	87	MET	0	-0.060	-0.042	8.762	-0.023	-0.023	0.000	0.000	0.000	0.000
86	A	88	GLU	-1	-0.775	-0.867	11.762	-0.079	-0.079	0.000	0.000	0.000	0.000
87	A	89	GLY	0	0.024	0.014	13.365	0.009	0.009	0.000	0.000	0.000	0.000
88	A	90	ARG	1	0.888	0.931	13.763	0.392	0.392	0.000	0.000	0.000	0.000
89	A	91	LEU	0	0.004	0.018	14.015	0.001	0.001	0.000	0.000	0.000	0.000
90	A	92	LYS	1	0.847	0.904	16.254	0.086	0.086	0.000	0.000	0.000	0.000
91	A	93	ALA	0	-0.047	-0.015	19.052	0.016	0.016	0.000	0.000	0.000	0.000
92	A	94	LEU	0	0.005	0.006	17.744	0.008	0.008	0.000	0.000	0.000	0.000
93	A	95	ARG	1	0.884	0.921	20.439	0.144	0.144	0.000	0.000	0.000	0.000
94	A	96	ALA	0	-0.022	-0.008	22.248	0.016	0.016	0.000	0.000	0.000	0.000
95	A	97	GLU	-1	-0.920	-0.949	23.791	-0.142	-0.142	0.000	0.000	0.000	0.000
96	A	98	ALA	0	-0.030	-0.011	24.273	0.008	0.008	0.000	0.000	0.000	0.000
97	A	99	GLU	-1	-0.908	-0.944	26.102	-0.092	-0.092	0.000	0.000	0.000	0.000
98	A	100	ALA	0	0.023	0.006	28.208	0.010	0.010	0.000	0.000	0.000	0.000
99	A	101	LEU	0	-0.006	0.003	28.808	0.007	0.007	0.000	0.000	0.000	0.000
100	A	102	TYR	0	-0.050	-0.033	30.217	0.007	0.007	0.000	0.000	0.000	0.000
101	A	103	GLN	0	-0.060	-0.056	31.548	0.012	0.012	0.000	0.000	0.000	0.000
102	A	104	ASP	-1	-0.900	-0.951	33.933	-0.083	-0.083	0.000	0.000	0.000	0.000
103	A	105	LEU	0	-0.104	-0.048	33.081	0.004	0.004	0.000	0.000	0.000	0.000
104	A	106	ASP	-1	-0.940	-0.959	36.573	-0.063	-0.063	0.000	0.000	0.000	0.000
105	A	107	ALA	0	0.043	0.018	38.884	0.005	0.005	0.000	0.000	0.000	0.000
106	A	108	LEU	0	-0.010	0.002	38.718	0.005	0.005	0.000	0.000	0.000	0.000
107	A	109	HIS	0	0.007	0.008	41.085	0.004	0.004	0.000	0.000	0.000	0.000
108	A	110	GLY	0	0.076	0.032	42.962	0.004	0.004	0.000	0.000	0.000	0.000
109	A	111	ARG	1	0.846	0.914	44.124	0.057	0.057	0.000	0.000	0.000	0.000
110	A	112	LEU	0	0.015	-0.003	43.282	0.003	0.003	0.000	0.000	0.000	0.000
111	A	113	HIS	0	0.016	0.015	46.929	0.001	0.001	0.000	0.000	0.000	0.000
112	A	114	ARG	1	0.866	0.921	45.517	0.053	0.053	0.000	0.000	0.000	0.000
113	A	115	LEU	0	-0.069	-0.027	47.575	0.002	0.002	0.000	0.000	0.000	0.000
114	A	116	PHE	0	-0.060	-0.017	48.302	0.000	0.000	0.000	0.000	0.000	0.000
115	A	117	PRO	0	0.008	0.025	52.821	0.000	0.000	0.000	0.000	0.000	0.000

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