FMO DATABASE

FMODB ID: R53Z8

Calculation Name: 2WHN-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2WHN

Chain ID: A

ChEMBL ID:

UniProt ID: Q5SK58

Base Structure: X-ray

Registration Date: 2023-06-21

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	OptAll
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	110
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-861237.508752
FMO2-HF: Nuclear repulsion	818813.519477
FMO2-HF: Total energy	-42423.989275
FMO2-MP2: Total energy	-42549.749662

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:53:VAL)

Summations of interaction energy for fragment #1(A:53:VAL)

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.
-2.599	1.008	0.805	-1.316	-3.094	0

Interaction energy analysis for fragmet #1(A:53:VAL)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.046 / q_NPA : 0.011

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	A	55	ILE	0	0.092	0.038	2.883	-2.139	0.768	0.407	-1.212	-2.101	0.001
4	A	56	PRO	0	0.035	0.018	3.646	0.162	0.363	0.011	0.030	-0.242	0.000
5	A	57	ALA	0	-0.044	-0.023	6.069	0.094	0.094	0.000	0.000	0.000	0.000
6	A	58	LEU	0	-0.003	0.002	2.773	-0.552	-0.053	0.387	-0.134	-0.751	-0.001
7	A	59	GLU	-1	-0.810	-0.860	6.887	-0.198	-0.198	0.000	0.000	0.000	0.000
8	A	60	ARG	1	0.995	0.985	9.717	0.189	0.189	0.000	0.000	0.000	0.000
9	A	61	GLY	0	0.036	0.019	12.912	-0.014	-0.014	0.000	0.000	0.000	0.000
10	A	62	PRO	0	-0.012	-0.008	15.132	-0.014	-0.014	0.000	0.000	0.000	0.000
11	A	63	GLY	0	0.022	0.013	18.975	0.021	0.021	0.000	0.000	0.000	0.000
12	A	64	LEU	0	-0.007	-0.004	20.755	-0.004	-0.004	0.000	0.000	0.000	0.000
13	A	65	LYS	1	0.878	0.923	22.798	0.028	0.028	0.000	0.000	0.000	0.000
14	A	66	ASP	-1	-0.802	-0.890	20.753	-0.020	-0.020	0.000	0.000	0.000	0.000
15	A	67	LEU	0	-0.010	-0.002	24.205	-0.002	-0.002	0.000	0.000	0.000	0.000
16	A	68	ALA	0	0.029	0.020	25.906	0.000	0.000	0.000	0.000	0.000	0.000
17	A	69	ILE	0	0.003	0.004	27.059	-0.002	-0.002	0.000	0.000	0.000	0.000
18	A	70	PHE	0	0.032	0.013	26.871	-0.001	-0.001	0.000	0.000	0.000	0.000
19	A	71	SER	0	0.015	0.009	28.880	0.001	0.001	0.000	0.000	0.000	0.000
20	A	72	ARG	1	0.815	0.870	31.505	-0.011	-0.011	0.000	0.000	0.000	0.000
21	A	73	GLN	0	-0.028	-0.015	29.480	0.001	0.001	0.000	0.000	0.000	0.000
22	A	74	LEU	0	0.007	0.001	31.783	-0.001	-0.001	0.000	0.000	0.000	0.000
23	A	75	ALA	0	0.014	0.007	34.100	0.000	0.000	0.000	0.000	0.000	0.000
24	A	76	THR	0	-0.043	-0.031	36.764	0.000	0.000	0.000	0.000	0.000	0.000
25	A	77	MET	0	-0.043	-0.010	33.368	-0.002	-0.002	0.000	0.000	0.000	0.000
26	A	78	LEU	0	-0.019	-0.007	36.382	0.000	0.000	0.000	0.000	0.000	0.000
27	A	79	GLY	0	0.018	0.008	39.792	0.000	0.000	0.000	0.000	0.000	0.000
28	A	80	ALA	0	-0.064	-0.023	41.749	-0.001	-0.001	0.000	0.000	0.000	0.000
29	A	81	GLY	0	0.010	0.012	42.932	-0.001	-0.001	0.000	0.000	0.000	0.000
30	A	82	LEU	0	-0.075	-0.031	38.479	-0.001	-0.001	0.000	0.000	0.000	0.000
31	A	83	THR	0	0.017	-0.022	39.901	0.003	0.003	0.000	0.000	0.000	0.000
32	A	84	LEU	0	0.050	0.012	33.396	-0.002	-0.002	0.000	0.000	0.000	0.000
33	A	85	LEU	0	0.044	0.021	34.048	-0.001	-0.001	0.000	0.000	0.000	0.000
34	A	86	GLN	0	0.036	0.041	34.694	-0.002	-0.002	0.000	0.000	0.000	0.000
35	A	87	ALA	0	0.043	0.016	35.178	-0.004	-0.004	0.000	0.000	0.000	0.000
36	A	88	LEU	0	0.013	-0.005	29.428	-0.003	-0.003	0.000	0.000	0.000	0.000
37	A	89	ALA	0	0.017	0.012	30.416	-0.005	-0.005	0.000	0.000	0.000	0.000
38	A	90	ILE	0	-0.038	-0.013	31.901	-0.006	-0.006	0.000	0.000	0.000	0.000
39	A	91	LEU	0	0.010	0.002	28.441	-0.005	-0.005	0.000	0.000	0.000	0.000
40	A	92	GLU	-1	-0.860	-0.892	26.386	-0.031	-0.031	0.000	0.000	0.000	0.000
41	A	93	ARG	1	0.817	0.900	26.022	0.027	0.027	0.000	0.000	0.000	0.000
42	A	94	GLN	0	-0.024	-0.007	28.315	-0.002	-0.002	0.000	0.000	0.000	0.000
43	A	95	THR	0	0.010	0.018	22.974	0.006	0.006	0.000	0.000	0.000	0.000
44	A	96	GLU	-1	-0.835	-0.900	22.250	-0.067	-0.067	0.000	0.000	0.000	0.000
45	A	97	ASN	0	-0.051	-0.032	17.505	-0.026	-0.026	0.000	0.000	0.000	0.000
46	A	98	ARG	1	0.839	0.880	13.791	0.170	0.170	0.000	0.000	0.000	0.000
47	A	99	LYS	1	0.818	0.892	10.555	0.035	0.035	0.000	0.000	0.000	0.000
48	A	100	PHE	0	-0.011	-0.014	16.456	0.018	0.018	0.000	0.000	0.000	0.000
49	A	101	ARG	1	0.915	0.945	19.936	0.096	0.096	0.000	0.000	0.000	0.000
50	A	102	GLU	-1	-0.825	-0.877	16.798	-0.097	-0.097	0.000	0.000	0.000	0.000
51	A	103	ILE	0	-0.035	-0.012	18.032	0.013	0.013	0.000	0.000	0.000	0.000
52	A	104	LEU	0	0.020	0.010	21.212	0.006	0.006	0.000	0.000	0.000	0.000
53	A	105	LYS	1	0.897	0.941	21.181	0.075	0.075	0.000	0.000	0.000	0.000
54	A	106	GLN	0	-0.056	-0.006	22.609	-0.004	-0.004	0.000	0.000	0.000	0.000
55	A	107	VAL	0	-0.024	-0.022	24.642	0.004	0.004	0.000	0.000	0.000	0.000
56	A	108	ARG	1	0.760	0.829	27.009	0.016	0.016	0.000	0.000	0.000	0.000
57	A	109	THR	0	-0.009	-0.022	27.234	-0.001	-0.001	0.000	0.000	0.000	0.000
58	A	110	ASP	-1	-0.789	-0.880	26.939	0.053	0.053	0.000	0.000	0.000	0.000
59	A	111	VAL	0	-0.033	-0.011	29.983	0.001	0.001	0.000	0.000	0.000	0.000
60	A	112	GLU	-1	-0.874	-0.907	32.531	-0.008	-0.008	0.000	0.000	0.000	0.000
61	A	113	GLY	0	-0.019	0.002	32.919	-0.002	-0.002	0.000	0.000	0.000	0.000
62	A	114	GLY	0	-0.024	-0.008	34.212	0.002	0.002	0.000	0.000	0.000	0.000
63	A	115	MET	0	-0.080	-0.014	29.814	0.005	0.005	0.000	0.000	0.000	0.000
64	A	116	ALA	0	0.031	0.017	33.975	-0.004	-0.004	0.000	0.000	0.000	0.000
65	A	117	PHE	0	0.055	0.004	30.159	0.002	0.002	0.000	0.000	0.000	0.000
66	A	118	SER	0	-0.054	-0.067	30.847	0.005	0.005	0.000	0.000	0.000	0.000
67	A	119	GLU	-1	-0.871	-0.943	30.162	0.074	0.074	0.000	0.000	0.000	0.000
68	A	120	ALA	0	0.052	0.035	28.041	0.009	0.009	0.000	0.000	0.000	0.000
69	A	121	LEU	0	-0.050	-0.022	26.333	0.003	0.003	0.000	0.000	0.000	0.000
70	A	122	SER	0	-0.066	-0.057	25.441	0.011	0.011	0.000	0.000	0.000	0.000
71	A	123	LYS	1	0.824	0.913	23.283	-0.054	-0.054	0.000	0.000	0.000	0.000
72	A	124	HIS	0	-0.050	-0.021	20.416	0.016	0.016	0.000	0.000	0.000	0.000
73	A	125	LYS	1	0.950	0.944	16.221	-0.271	-0.271	0.000	0.000	0.000	0.000
74	A	126	ILE	0	-0.039	0.011	20.618	0.007	0.007	0.000	0.000	0.000	0.000
75	A	127	PHE	0	0.021	0.017	22.057	-0.007	-0.007	0.000	0.000	0.000	0.000
76	A	128	SER	0	0.026	0.013	25.653	0.008	0.008	0.000	0.000	0.000	0.000
77	A	129	ARG	1	1.016	0.985	25.806	-0.160	-0.160	0.000	0.000	0.000	0.000
78	A	130	LEU	0	0.022	0.025	29.749	-0.004	-0.004	0.000	0.000	0.000	0.000
79	A	131	TYR	0	0.046	0.017	29.153	-0.005	-0.005	0.000	0.000	0.000	0.000
80	A	132	VAL	0	0.018	0.008	28.355	-0.006	-0.006	0.000	0.000	0.000	0.000
81	A	133	ASN	0	0.000	-0.010	31.317	-0.004	-0.004	0.000	0.000	0.000	0.000
82	A	134	LEU	0	0.001	0.009	34.583	-0.004	-0.004	0.000	0.000	0.000	0.000
83	A	135	VAL	0	0.023	0.014	32.418	-0.005	-0.005	0.000	0.000	0.000	0.000
84	A	136	ARG	1	0.881	0.936	35.170	-0.054	-0.054	0.000	0.000	0.000	0.000
85	A	137	ALA	0	-0.012	-0.005	36.757	-0.002	-0.002	0.000	0.000	0.000	0.000
86	A	138	GLY	0	0.058	0.008	38.817	-0.003	-0.003	0.000	0.000	0.000	0.000
87	A	139	GLU	-1	-0.781	-0.872	35.532	0.044	0.044	0.000	0.000	0.000	0.000
88	A	140	THR	0	-0.074	-0.039	39.785	-0.002	-0.002	0.000	0.000	0.000	0.000
89	A	141	SER	0	-0.008	-0.006	42.725	0.000	0.000	0.000	0.000	0.000	0.000
90	A	142	GLY	0	-0.008	0.012	43.478	-0.002	-0.002	0.000	0.000	0.000	0.000
91	A	143	GLY	0	0.030	0.025	42.634	-0.002	-0.002	0.000	0.000	0.000	0.000
92	A	144	LEU	0	-0.036	-0.034	36.268	0.002	0.002	0.000	0.000	0.000	0.000
93	A	145	ASP	-1	-0.805	-0.898	38.139	0.018	0.018	0.000	0.000	0.000	0.000
94	A	146	LEU	0	0.012	0.003	39.510	0.000	0.000	0.000	0.000	0.000	0.000
95	A	147	ILE	0	-0.044	-0.012	36.386	0.002	0.002	0.000	0.000	0.000	0.000
96	A	148	LEU	0	-0.019	-0.012	32.356	0.003	0.003	0.000	0.000	0.000	0.000
97	A	149	ASP	-1	-0.818	-0.897	35.384	0.017	0.017	0.000	0.000	0.000	0.000
98	A	150	ARG	1	0.914	0.969	37.392	-0.028	-0.028	0.000	0.000	0.000	0.000
99	A	151	LEU	0	-0.025	-0.010	32.070	0.003	0.003	0.000	0.000	0.000	0.000
100	A	152	ALA	0	0.001	0.000	32.789	0.002	0.002	0.000	0.000	0.000	0.000
101	A	153	SER	0	0.005	-0.010	33.742	-0.001	-0.001	0.000	0.000	0.000	0.000
102	A	154	PHE	0	-0.099	-0.032	31.159	0.000	0.000	0.000	0.000	0.000	0.000
103	A	155	LEU	0	0.011	-0.004	28.103	0.001	0.001	0.000	0.000	0.000	0.000
104	A	156	GLU	-1	-0.791	-0.884	30.450	0.010	0.010	0.000	0.000	0.000	0.000
105	A	157	LYS	1	0.963	0.991	32.533	-0.026	-0.026	0.000	0.000	0.000	0.000
106	A	158	GLU	-1	-0.845	-0.921	27.717	0.066	0.066	0.000	0.000	0.000	0.000
107	A	159	LEU	0	-0.063	-0.048	26.518	0.002	0.002	0.000	0.000	0.000	0.000
108	A	160	GLU	-1	-0.961	-0.976	29.540	0.012	0.012	0.000	0.000	0.000	0.000
109	A	161	LEU	0	-0.031	-0.008	32.385	-0.001	-0.001	0.000	0.000	0.000	0.000
110	A	162	ARG	1	0.798	0.910	23.141	-0.068	-0.068	0.000	0.000	0.000	0.000

Top

Graph

Overview

Highlights

Manual

Support

Interactive mode: IFIE and PIEDA for fragment #1(A:53:VAL)