FMO DATABASE

FMODB ID: ZYMJN

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

Total energy (hartree)

FMO2-HF: Electronic energy	-858860.773357
FMO2-HF: Nuclear repulsion	816436.916277
FMO2-HF: Total energy	-42423.85708
FMO2-MP2: Total energy	-42549.648497

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.
-1.887	1.23	1.102	-1.103	-3.115	0.001

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 : 0.029 / 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

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	0.094	0.040	3.064	-1.846	0.785	0.163	-0.909	-1.885	0.002
4	A	56	PRO	0	0.050	0.020	3.762	0.232	0.418	0.003	0.024	-0.213	0.000
5	A	57	ALA	0	-0.068	-0.034	5.451	0.100	0.100	0.000	0.000	0.000	0.000
6	A	58	LEU	0	0.000	0.003	2.502	-0.466	-0.166	0.936	-0.218	-1.017	-0.001
7	A	59	GLU	-1	-0.838	-0.869	6.440	-0.308	-0.308	0.000	0.000	0.000	0.000
8	A	60	ARG	1	0.969	0.972	9.530	0.267	0.267	0.000	0.000	0.000	0.000
9	A	61	GLY	0	0.022	0.012	12.910	-0.011	-0.011	0.000	0.000	0.000	0.000
10	A	62	PRO	0	-0.037	-0.020	14.948	-0.006	-0.006	0.000	0.000	0.000	0.000
11	A	63	GLY	0	0.014	0.009	18.626	0.017	0.017	0.000	0.000	0.000	0.000
12	A	64	LEU	0	0.013	0.005	20.435	0.001	0.001	0.000	0.000	0.000	0.000
13	A	65	LYS	1	0.894	0.941	23.001	0.069	0.069	0.000	0.000	0.000	0.000
14	A	66	ASP	-1	-0.814	-0.904	20.368	-0.067	-0.067	0.000	0.000	0.000	0.000
15	A	67	LEU	0	0.010	0.013	23.823	-0.001	-0.001	0.000	0.000	0.000	0.000
16	A	68	ALA	0	0.025	0.021	25.513	0.002	0.002	0.000	0.000	0.000	0.000
17	A	69	ILE	0	-0.001	0.000	26.564	0.000	0.000	0.000	0.000	0.000	0.000
18	A	70	PHE	0	0.034	0.017	26.599	0.002	0.002	0.000	0.000	0.000	0.000
19	A	71	SER	0	0.006	-0.007	28.553	0.004	0.004	0.000	0.000	0.000	0.000
20	A	72	ARG	1	0.831	0.873	31.064	0.010	0.010	0.000	0.000	0.000	0.000
21	A	73	GLN	0	-0.010	-0.005	29.498	0.001	0.001	0.000	0.000	0.000	0.000
22	A	74	LEU	0	0.005	0.007	31.778	0.000	0.000	0.000	0.000	0.000	0.000
23	A	75	ALA	0	0.018	0.010	34.039	0.001	0.001	0.000	0.000	0.000	0.000
24	A	76	THR	0	-0.045	-0.029	36.475	0.001	0.001	0.000	0.000	0.000	0.000
25	A	77	MET	0	-0.047	-0.018	33.517	-0.001	-0.001	0.000	0.000	0.000	0.000
26	A	78	LEU	0	-0.021	-0.014	36.316	0.001	0.001	0.000	0.000	0.000	0.000
27	A	79	GLY	0	0.016	0.013	39.659	0.001	0.001	0.000	0.000	0.000	0.000
28	A	80	ALA	0	-0.075	-0.030	41.639	0.000	0.000	0.000	0.000	0.000	0.000
29	A	81	GLY	0	0.025	0.018	42.687	0.000	0.000	0.000	0.000	0.000	0.000
30	A	82	LEU	0	-0.073	-0.026	38.596	0.000	0.000	0.000	0.000	0.000	0.000
31	A	83	THR	0	0.019	-0.019	39.932	0.002	0.002	0.000	0.000	0.000	0.000
32	A	84	LEU	0	0.050	0.015	33.455	-0.003	-0.003	0.000	0.000	0.000	0.000
33	A	85	LEU	0	0.045	0.013	33.605	-0.003	-0.003	0.000	0.000	0.000	0.000
34	A	86	GLN	0	0.025	0.033	34.830	-0.003	-0.003	0.000	0.000	0.000	0.000
35	A	87	ALA	0	0.030	0.012	35.022	-0.004	-0.004	0.000	0.000	0.000	0.000
36	A	88	LEU	0	0.028	0.004	29.466	-0.004	-0.004	0.000	0.000	0.000	0.000
37	A	89	ALA	0	0.029	0.022	30.363	-0.006	-0.006	0.000	0.000	0.000	0.000
38	A	90	ILE	0	-0.050	-0.022	31.459	-0.007	-0.007	0.000	0.000	0.000	0.000
39	A	91	LEU	0	0.019	0.008	28.594	-0.006	-0.006	0.000	0.000	0.000	0.000
40	A	92	GLU	-1	-0.909	-0.923	26.606	-0.054	-0.054	0.000	0.000	0.000	0.000
41	A	93	ARG	1	0.884	0.939	26.350	0.044	0.044	0.000	0.000	0.000	0.000
42	A	94	GLN	0	-0.049	-0.014	28.165	-0.004	-0.004	0.000	0.000	0.000	0.000
43	A	95	THR	0	0.007	0.009	22.777	0.004	0.004	0.000	0.000	0.000	0.000
44	A	96	GLU	-1	-0.842	-0.908	22.011	-0.109	-0.109	0.000	0.000	0.000	0.000
45	A	97	ASN	0	-0.009	-0.008	17.020	-0.028	-0.028	0.000	0.000	0.000	0.000
46	A	98	ARG	1	0.880	0.915	13.309	0.250	0.250	0.000	0.000	0.000	0.000
47	A	99	LYS	1	0.912	0.943	10.592	0.156	0.156	0.000	0.000	0.000	0.000
48	A	100	PHE	0	0.005	-0.002	16.615	0.020	0.020	0.000	0.000	0.000	0.000
49	A	101	ARG	1	0.912	0.938	20.015	0.141	0.141	0.000	0.000	0.000	0.000
50	A	102	GLU	-1	-0.868	-0.918	16.964	-0.136	-0.136	0.000	0.000	0.000	0.000
51	A	103	ILE	0	-0.048	-0.023	17.958	0.014	0.014	0.000	0.000	0.000	0.000
52	A	104	LEU	0	0.018	0.006	21.025	0.010	0.010	0.000	0.000	0.000	0.000
53	A	105	LYS	1	0.904	0.950	21.452	0.112	0.112	0.000	0.000	0.000	0.000
54	A	106	GLN	0	-0.066	-0.014	22.373	-0.003	-0.003	0.000	0.000	0.000	0.000
55	A	107	VAL	0	-0.021	-0.015	24.413	0.008	0.008	0.000	0.000	0.000	0.000
56	A	108	ARG	1	0.791	0.858	26.793	0.038	0.038	0.000	0.000	0.000	0.000
57	A	109	THR	0	-0.015	-0.019	27.072	0.000	0.000	0.000	0.000	0.000	0.000
58	A	110	ASP	-1	-0.804	-0.884	26.562	0.026	0.026	0.000	0.000	0.000	0.000
59	A	111	VAL	0	-0.032	-0.021	29.645	0.002	0.002	0.000	0.000	0.000	0.000
60	A	112	GLU	-1	-0.895	-0.926	32.337	-0.023	-0.023	0.000	0.000	0.000	0.000
61	A	113	GLY	0	-0.023	0.002	32.871	0.000	0.000	0.000	0.000	0.000	0.000
62	A	114	GLY	0	-0.023	-0.009	34.216	0.003	0.003	0.000	0.000	0.000	0.000
63	A	115	MET	0	-0.072	-0.010	29.328	0.004	0.004	0.000	0.000	0.000	0.000
64	A	116	ALA	0	0.015	0.008	33.788	-0.004	-0.004	0.000	0.000	0.000	0.000
65	A	117	PHE	0	0.061	0.006	30.105	0.001	0.001	0.000	0.000	0.000	0.000
66	A	118	SER	0	-0.053	-0.068	30.685	0.003	0.003	0.000	0.000	0.000	0.000
67	A	119	GLU	-1	-0.875	-0.943	29.702	0.056	0.056	0.000	0.000	0.000	0.000
68	A	120	ALA	0	0.054	0.034	27.821	0.006	0.006	0.000	0.000	0.000	0.000
69	A	121	LEU	0	-0.039	-0.022	26.073	0.001	0.001	0.000	0.000	0.000	0.000
70	A	122	SER	0	-0.088	-0.047	25.210	0.008	0.008	0.000	0.000	0.000	0.000
71	A	123	LYS	1	0.838	0.918	23.008	-0.027	-0.027	0.000	0.000	0.000	0.000
72	A	124	HIS	0	-0.044	-0.026	20.072	0.006	0.006	0.000	0.000	0.000	0.000
73	A	125	LYS	1	0.953	0.957	15.548	-0.194	-0.194	0.000	0.000	0.000	0.000
74	A	126	ILE	0	-0.056	-0.013	20.146	0.004	0.004	0.000	0.000	0.000	0.000
75	A	127	PHE	0	0.027	0.029	21.576	-0.007	-0.007	0.000	0.000	0.000	0.000
76	A	128	SER	0	0.032	0.016	25.170	0.010	0.010	0.000	0.000	0.000	0.000
77	A	129	ARG	1	1.027	0.991	25.618	-0.125	-0.125	0.000	0.000	0.000	0.000
78	A	130	LEU	0	0.022	0.024	29.332	-0.003	-0.003	0.000	0.000	0.000	0.000
79	A	131	TYR	0	0.030	0.006	28.823	-0.003	-0.003	0.000	0.000	0.000	0.000
80	A	132	VAL	0	0.038	0.014	27.951	-0.005	-0.005	0.000	0.000	0.000	0.000
81	A	133	ASN	0	-0.010	-0.016	30.973	-0.002	-0.002	0.000	0.000	0.000	0.000
82	A	134	LEU	0	-0.007	0.001	34.049	-0.003	-0.003	0.000	0.000	0.000	0.000
83	A	135	VAL	0	0.021	0.005	31.955	-0.003	-0.003	0.000	0.000	0.000	0.000
84	A	136	ARG	1	0.883	0.937	34.769	-0.037	-0.037	0.000	0.000	0.000	0.000
85	A	137	ALA	0	-0.016	-0.015	36.243	-0.001	-0.001	0.000	0.000	0.000	0.000
86	A	138	GLY	0	0.054	0.003	38.288	-0.002	-0.002	0.000	0.000	0.000	0.000
87	A	139	GLU	-1	-0.803	-0.878	35.322	0.027	0.027	0.000	0.000	0.000	0.000
88	A	140	THR	0	-0.065	-0.027	39.394	-0.001	-0.001	0.000	0.000	0.000	0.000
89	A	141	SER	0	-0.009	-0.004	42.438	0.000	0.000	0.000	0.000	0.000	0.000
90	A	142	GLY	0	-0.011	0.010	43.188	-0.001	-0.001	0.000	0.000	0.000	0.000
91	A	143	GLY	0	0.040	0.031	42.597	-0.002	-0.002	0.000	0.000	0.000	0.000
92	A	144	LEU	0	-0.035	-0.029	36.066	0.001	0.001	0.000	0.000	0.000	0.000
93	A	145	ASP	-1	-0.818	-0.906	38.371	0.004	0.004	0.000	0.000	0.000	0.000
94	A	146	LEU	0	0.006	0.004	39.656	0.000	0.000	0.000	0.000	0.000	0.000
95	A	147	ILE	0	-0.041	-0.011	36.153	0.001	0.001	0.000	0.000	0.000	0.000
96	A	148	LEU	0	-0.022	-0.015	32.413	0.002	0.002	0.000	0.000	0.000	0.000
97	A	149	ASP	-1	-0.827	-0.895	35.417	-0.001	-0.001	0.000	0.000	0.000	0.000
98	A	150	ARG	1	0.929	0.977	37.455	-0.014	-0.014	0.000	0.000	0.000	0.000
99	A	151	LEU	0	-0.022	-0.011	32.070	0.002	0.002	0.000	0.000	0.000	0.000
100	A	152	ALA	0	0.016	0.007	32.573	0.001	0.001	0.000	0.000	0.000	0.000
101	A	153	SER	0	0.004	-0.004	33.497	-0.002	-0.002	0.000	0.000	0.000	0.000
102	A	154	PHE	0	-0.099	-0.043	30.997	0.000	0.000	0.000	0.000	0.000	0.000
103	A	155	LEU	0	-0.007	-0.009	27.926	0.001	0.001	0.000	0.000	0.000	0.000
104	A	156	GLU	-1	-0.799	-0.875	30.570	-0.012	-0.012	0.000	0.000	0.000	0.000
105	A	157	LYS	1	0.968	0.991	32.512	-0.009	-0.009	0.000	0.000	0.000	0.000
106	A	158	GLU	-1	-0.855	-0.920	27.434	0.033	0.033	0.000	0.000	0.000	0.000
107	A	159	LEU	0	-0.076	-0.059	26.545	0.000	0.000	0.000	0.000	0.000	0.000
108	A	160	GLU	-1	-0.962	-0.977	29.374	-0.008	-0.008	0.000	0.000	0.000	0.000
109	A	161	LEU	0	-0.056	-0.015	31.871	0.000	0.000	0.000	0.000	0.000	0.000
110	A	162	ARG	1	0.834	0.924	22.792	-0.032	-0.032	0.000	0.000	0.000	0.000

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Highlights

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Support

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