FMO DATABASE

FMODB ID: 53Y1Z

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

Total energy (hartree)

FMO2-HF: Electronic energy	-855580.297591
FMO2-HF: Nuclear repulsion	810212.327985
FMO2-HF: Total energy	-45367.969606
FMO2-MP2: Total energy	-45502.434471

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.
-9.431	-1.161	3.917	-4.317	-7.869	-0.023

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 : 0.032 / q_NPA : 0.007

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	-0.776	-0.894	3.379	0.880	2.843	0.039	-0.714	-1.287	0.001
4	A	6	LEU	0	-0.025	-0.012	2.430	-0.734	0.648	0.764	-0.504	-1.642	0.001
5	A	7	SER	0	0.025	0.015	3.203	-0.327	0.589	0.067	-0.391	-0.592	-0.002
6	A	8	ALA	0	0.016	0.013	5.014	1.000	1.116	-0.001	-0.006	-0.108	0.000
7	A	9	LEU	0	0.012	0.008	7.731	0.377	0.377	0.000	0.000	0.000	0.000
8	A	10	ARG	1	0.925	0.959	7.643	1.426	1.426	0.000	0.000	0.000	0.000
9	A	11	ILE	0	-0.015	-0.011	8.797	0.287	0.287	0.000	0.000	0.000	0.000
10	A	12	ALA	0	0.019	0.027	11.054	0.164	0.164	0.000	0.000	0.000	0.000
11	A	13	ILE	0	-0.050	-0.032	12.642	0.113	0.113	0.000	0.000	0.000	0.000
12	A	14	GLY	0	0.016	-0.002	13.387	0.077	0.077	0.000	0.000	0.000	0.000
13	A	15	GLU	-1	-0.900	-0.971	14.824	-0.344	-0.344	0.000	0.000	0.000	0.000
14	A	16	LEU	0	-0.068	-0.024	17.159	0.056	0.056	0.000	0.000	0.000	0.000
15	A	17	LEU	0	-0.109	-0.050	16.207	0.039	0.039	0.000	0.000	0.000	0.000
16	A	18	GLU	-1	-0.970	-0.978	19.547	-0.212	-0.212	0.000	0.000	0.000	0.000
17	A	19	LYS	1	0.866	0.943	15.194	0.414	0.414	0.000	0.000	0.000	0.000
18	A	20	GLU	-1	-0.877	-0.939	17.967	-0.280	-0.280	0.000	0.000	0.000	0.000
19	A	21	ALA	0	0.038	0.005	16.607	-0.050	-0.050	0.000	0.000	0.000	0.000
20	A	22	HIS	0	-0.021	-0.011	15.127	-0.073	-0.073	0.000	0.000	0.000	0.000
21	A	23	ASP	-1	-0.931	-0.966	14.391	-0.451	-0.451	0.000	0.000	0.000	0.000
22	A	24	LEU	0	-0.084	-0.035	10.733	-0.093	-0.093	0.000	0.000	0.000	0.000
23	A	25	LEU	0	-0.002	0.003	10.678	-0.121	-0.121	0.000	0.000	0.000	0.000
24	A	26	HIS	0	0.049	0.002	8.289	-0.047	-0.047	0.000	0.000	0.000	0.000
25	A	27	GLU	-1	-0.846	-0.924	5.599	-1.693	-1.693	0.000	0.000	0.000	0.000
26	A	28	ARG	1	0.889	0.939	6.932	0.480	0.480	0.000	0.000	0.000	0.000
27	A	29	GLU	-1	-0.988	-0.987	9.497	-0.291	-0.291	0.000	0.000	0.000	0.000
28	A	30	GLU	-1	-0.961	-0.979	3.422	-5.344	-4.045	0.050	-0.680	-0.669	-0.006
29	A	31	LEU	0	-0.010	-0.006	6.140	0.508	0.508	0.000	0.000	0.000	0.000
30	A	32	ALA	0	-0.025	-0.006	7.801	0.366	0.366	0.000	0.000	0.000	0.000
31	A	33	PRO	0	-0.046	-0.019	9.622	0.127	0.127	0.000	0.000	0.000	0.000
32	A	34	VAL	0	0.004	0.001	7.368	0.113	0.113	0.000	0.000	0.000	0.000
33	A	35	LEU	0	-0.010	-0.009	10.524	0.073	0.073	0.000	0.000	0.000	0.000
34	A	36	GLY	0	-0.059	-0.016	12.628	0.003	0.003	0.000	0.000	0.000	0.000
35	A	37	GLN	0	-0.037	-0.035	12.810	0.007	0.007	0.000	0.000	0.000	0.000
36	A	38	ARG	1	0.770	0.888	6.880	-1.458	-1.458	0.000	0.000	0.000	0.000
37	A	39	PRO	0	0.021	0.005	12.802	-0.100	-0.100	0.000	0.000	0.000	0.000
38	A	40	GLU	-1	-0.719	-0.861	11.216	0.398	0.398	0.000	0.000	0.000	0.000
39	A	41	LEU	0	0.002	0.011	7.297	-0.124	-0.124	0.000	0.000	0.000	0.000
40	A	42	LYS	1	0.934	0.979	11.015	-0.048	-0.048	0.000	0.000	0.000	0.000
41	A	43	ARG	1	0.823	0.891	13.897	-0.077	-0.077	0.000	0.000	0.000	0.000
42	A	44	LEU	0	-0.019	-0.009	9.128	-0.018	-0.018	0.000	0.000	0.000	0.000
43	A	45	ALA	0	0.002	-0.006	10.829	-0.052	-0.052	0.000	0.000	0.000	0.000
44	A	46	GLU	-1	-0.951	-0.979	12.506	-0.262	-0.262	0.000	0.000	0.000	0.000
45	A	47	ALA	0	0.008	0.025	15.905	0.057	0.057	0.000	0.000	0.000	0.000
46	A	48	LYS	1	0.876	0.936	17.827	0.304	0.304	0.000	0.000	0.000	0.000
47	A	49	THR	0	-0.005	0.006	20.601	0.006	0.006	0.000	0.000	0.000	0.000
48	A	50	LEU	0	0.113	0.042	19.010	-0.011	-0.011	0.000	0.000	0.000	0.000
49	A	51	PRO	0	-0.022	-0.014	18.953	-0.004	-0.004	0.000	0.000	0.000	0.000
50	A	52	ALA	0	0.029	0.017	19.502	0.011	0.011	0.000	0.000	0.000	0.000
51	A	53	LEU	0	0.003	0.008	13.782	0.005	0.005	0.000	0.000	0.000	0.000
52	A	54	GLU	-1	-0.826	-0.940	14.808	-0.156	-0.156	0.000	0.000	0.000	0.000
53	A	55	GLU	-1	-1.035	-1.009	15.611	-0.017	-0.017	0.000	0.000	0.000	0.000
54	A	56	ALA	0	0.041	0.022	13.983	0.036	0.036	0.000	0.000	0.000	0.000
55	A	57	LEU	0	0.000	0.002	9.214	0.034	0.034	0.000	0.000	0.000	0.000
56	A	58	ARG	1	0.985	0.982	11.606	0.113	0.113	0.000	0.000	0.000	0.000
57	A	59	GLU	-1	-0.878	-0.916	13.933	0.129	0.129	0.000	0.000	0.000	0.000
58	A	60	ALA	0	-0.021	-0.017	8.503	0.093	0.093	0.000	0.000	0.000	0.000
59	A	61	LEU	0	0.012	0.001	9.067	0.226	0.226	0.000	0.000	0.000	0.000
60	A	62	LEU	0	0.000	0.026	10.844	0.059	0.059	0.000	0.000	0.000	0.000
61	A	63	HIS	0	0.014	0.011	9.503	0.196	0.196	0.000	0.000	0.000	0.000
62	A	64	LEU	0	0.019	0.006	5.791	0.120	0.120	0.000	0.000	0.000	0.000
63	A	65	GLU	-1	-0.944	-0.976	9.262	0.299	0.299	0.000	0.000	0.000	0.000
64	A	66	GLU	-1	-0.961	-0.993	12.483	0.434	0.434	0.000	0.000	0.000	0.000
65	A	67	ARG	1	0.812	0.906	8.474	-1.235	-1.235	0.000	0.000	0.000	0.000
66	A	68	ALA	0	0.006	-0.016	10.746	-0.060	-0.060	0.000	0.000	0.000	0.000
67	A	69	ALA	0	-0.069	-0.025	11.926	-0.092	-0.092	0.000	0.000	0.000	0.000
68	A	70	GLN	0	-0.060	-0.038	14.042	0.026	0.026	0.000	0.000	0.000	0.000
69	A	71	GLU	-1	-0.832	-0.885	11.218	0.742	0.742	0.000	0.000	0.000	0.000
70	A	72	PRO	0	-0.025	-0.025	13.372	0.007	0.007	0.000	0.000	0.000	0.000
71	A	73	GLU	-1	-0.935	-0.965	15.292	0.326	0.326	0.000	0.000	0.000	0.000
72	A	74	GLU	-1	-0.882	-0.919	9.537	0.372	0.372	0.000	0.000	0.000	0.000
73	A	75	PRO	0	-0.044	-0.037	11.326	0.047	0.047	0.000	0.000	0.000	0.000
74	A	76	TYR	0	0.007	0.005	2.276	-4.206	-2.696	1.825	-1.248	-2.087	-0.014
75	A	77	TRP	0	-0.003	-0.019	4.148	-0.076	0.063	-0.001	-0.018	-0.120	0.000
76	A	78	ARG	1	0.978	0.990	7.992	-0.336	-0.336	0.000	0.000	0.000	0.000
77	A	79	GLY	0	-0.016	0.004	9.272	-0.072	-0.072	0.000	0.000	0.000	0.000
78	A	80	LEU	0	-0.060	-0.028	2.396	-1.380	-0.435	1.174	-0.756	-1.364	-0.003
79	A	81	LEU	0	0.041	0.015	6.027	-0.148	-0.148	0.000	0.000	0.000	0.000
80	A	82	LEU	0	0.032	0.027	8.754	-0.124	-0.124	0.000	0.000	0.000	0.000
81	A	83	ALA	0	-0.037	-0.020	6.552	-0.079	-0.079	0.000	0.000	0.000	0.000
82	A	84	VAL	0	-0.011	-0.020	5.459	-0.193	-0.193	0.000	0.000	0.000	0.000
83	A	85	GLU	-1	-0.862	-0.937	7.923	0.069	0.069	0.000	0.000	0.000	0.000
84	A	86	ALA	0	-0.048	-0.007	11.262	-0.023	-0.023	0.000	0.000	0.000	0.000
85	A	87	MET	0	-0.074	-0.051	8.717	-0.001	-0.001	0.000	0.000	0.000	0.000
86	A	88	GLU	-1	-0.886	-0.934	11.691	-0.072	-0.072	0.000	0.000	0.000	0.000
87	A	89	GLY	0	-0.006	-0.001	13.350	0.015	0.015	0.000	0.000	0.000	0.000
88	A	90	ARG	1	0.898	0.933	13.859	0.310	0.310	0.000	0.000	0.000	0.000
89	A	91	LEU	0	0.005	0.024	13.923	0.004	0.004	0.000	0.000	0.000	0.000
90	A	92	LYS	1	0.989	0.983	16.214	0.104	0.104	0.000	0.000	0.000	0.000
91	A	93	ALA	0	-0.061	-0.022	19.023	0.016	0.016	0.000	0.000	0.000	0.000
92	A	94	LEU	0	0.013	0.009	17.540	0.009	0.009	0.000	0.000	0.000	0.000
93	A	95	ARG	1	0.898	0.942	20.399	0.128	0.128	0.000	0.000	0.000	0.000
94	A	96	ALA	0	-0.034	-0.014	22.220	0.014	0.014	0.000	0.000	0.000	0.000
95	A	97	GLU	-1	-0.918	-0.951	23.694	-0.118	-0.118	0.000	0.000	0.000	0.000
96	A	98	ALA	0	-0.027	-0.005	24.286	0.007	0.007	0.000	0.000	0.000	0.000
97	A	99	GLU	-1	-0.908	-0.926	26.088	-0.078	-0.078	0.000	0.000	0.000	0.000
98	A	100	ALA	0	0.025	0.005	28.184	0.009	0.009	0.000	0.000	0.000	0.000
99	A	101	LEU	0	-0.006	0.006	28.399	0.006	0.006	0.000	0.000	0.000	0.000
100	A	102	TYR	0	-0.033	-0.033	30.185	0.006	0.006	0.000	0.000	0.000	0.000
101	A	103	GLN	0	-0.068	-0.078	31.263	0.010	0.010	0.000	0.000	0.000	0.000
102	A	104	ASP	-1	-0.906	-0.952	33.915	-0.070	-0.070	0.000	0.000	0.000	0.000
103	A	105	LEU	0	-0.100	-0.044	33.016	0.004	0.004	0.000	0.000	0.000	0.000
104	A	106	ASP	-1	-0.943	-0.963	36.565	-0.051	-0.051	0.000	0.000	0.000	0.000
105	A	107	ALA	0	0.048	0.022	38.871	0.004	0.004	0.000	0.000	0.000	0.000
106	A	108	LEU	0	-0.018	-0.002	38.471	0.004	0.004	0.000	0.000	0.000	0.000
107	A	109	HIS	0	0.005	0.007	41.078	0.003	0.003	0.000	0.000	0.000	0.000
108	A	110	GLY	0	0.043	0.016	42.956	0.003	0.003	0.000	0.000	0.000	0.000
109	A	111	ARG	1	0.835	0.887	44.137	0.047	0.047	0.000	0.000	0.000	0.000
110	A	112	LEU	0	0.011	-0.007	43.645	0.002	0.002	0.000	0.000	0.000	0.000
111	A	113	HIS	0	0.007	0.013	46.922	0.001	0.001	0.000	0.000	0.000	0.000
112	A	114	ARG	1	0.937	0.975	45.855	0.043	0.043	0.000	0.000	0.000	0.000
113	A	115	LEU	0	-0.063	-0.023	47.568	0.002	0.002	0.000	0.000	0.000	0.000
114	A	116	PHE	0	-0.073	-0.021	48.265	0.000	0.000	0.000	0.000	0.000	0.000
115	A	117	PRO	0	0.007	0.024	52.816	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)