FMO DATABASE

FMODB ID: 66JMZ

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

Total energy (hartree)

FMO2-HF: Electronic energy	-858982.422593
FMO2-HF: Nuclear repulsion	816559.24634
FMO2-HF: Total energy	-42423.176253
FMO2-MP2: Total energy	-42549.004488

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.
-1.71	1.477	1.034	-1.014	-3.208	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 : 0.043 / 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

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	0.086	0.038	2.928	-1.856	0.814	0.300	-0.909	-2.061	0.002
4	A	56	PRO	0	0.043	0.018	3.579	0.330	0.481	0.009	0.080	-0.240	0.000
5	A	57	ALA	0	-0.071	-0.037	5.323	0.133	0.133	0.000	0.000	0.000	0.000
6	A	58	LEU	0	-0.003	0.001	2.547	-0.443	-0.077	0.725	-0.185	-0.907	-0.001
7	A	59	GLU	-1	-0.867	-0.899	6.526	-0.390	-0.390	0.000	0.000	0.000	0.000
8	A	60	ARG	1	0.967	0.973	9.534	0.303	0.303	0.000	0.000	0.000	0.000
9	A	61	GLY	0	0.009	0.009	12.959	-0.014	-0.014	0.000	0.000	0.000	0.000
10	A	62	PRO	0	-0.036	-0.018	14.972	-0.002	-0.002	0.000	0.000	0.000	0.000
11	A	63	GLY	0	0.024	0.002	18.688	0.018	0.018	0.000	0.000	0.000	0.000
12	A	64	LEU	0	0.012	0.015	20.504	0.001	0.001	0.000	0.000	0.000	0.000
13	A	65	LYS	1	0.999	1.002	23.691	0.072	0.072	0.000	0.000	0.000	0.000
14	A	66	ASP	-1	-0.876	-0.926	20.910	-0.082	-0.082	0.000	0.000	0.000	0.000
15	A	67	LEU	0	0.023	0.017	23.856	-0.001	-0.001	0.000	0.000	0.000	0.000
16	A	68	ALA	0	0.029	0.018	25.547	0.002	0.002	0.000	0.000	0.000	0.000
17	A	69	ILE	0	-0.001	-0.002	26.493	0.000	0.000	0.000	0.000	0.000	0.000
18	A	70	PHE	0	0.021	0.015	26.598	0.002	0.002	0.000	0.000	0.000	0.000
19	A	71	SER	0	0.010	-0.001	28.546	0.004	0.004	0.000	0.000	0.000	0.000
20	A	72	ARG	1	0.824	0.877	31.074	0.017	0.017	0.000	0.000	0.000	0.000
21	A	73	GLN	0	-0.014	-0.017	29.451	0.001	0.001	0.000	0.000	0.000	0.000
22	A	74	LEU	0	0.004	0.006	31.793	0.000	0.000	0.000	0.000	0.000	0.000
23	A	75	ALA	0	0.018	0.009	34.010	0.001	0.001	0.000	0.000	0.000	0.000
24	A	76	THR	0	-0.031	-0.006	36.468	0.001	0.001	0.000	0.000	0.000	0.000
25	A	77	MET	0	-0.047	-0.021	33.498	0.000	0.000	0.000	0.000	0.000	0.000
26	A	78	LEU	0	-0.020	-0.012	36.355	0.001	0.001	0.000	0.000	0.000	0.000
27	A	79	GLY	0	0.020	0.015	39.619	0.002	0.002	0.000	0.000	0.000	0.000
28	A	80	ALA	0	-0.075	-0.031	41.609	0.001	0.001	0.000	0.000	0.000	0.000
29	A	81	GLY	0	0.024	0.018	42.659	0.000	0.000	0.000	0.000	0.000	0.000
30	A	82	LEU	0	-0.063	-0.024	38.406	0.000	0.000	0.000	0.000	0.000	0.000
31	A	83	THR	0	0.028	0.005	39.637	0.002	0.002	0.000	0.000	0.000	0.000
32	A	84	LEU	0	0.065	0.019	33.496	-0.003	-0.003	0.000	0.000	0.000	0.000
33	A	85	LEU	0	0.059	0.018	33.500	-0.003	-0.003	0.000	0.000	0.000	0.000
34	A	86	GLN	0	-0.009	0.001	34.718	-0.004	-0.004	0.000	0.000	0.000	0.000
35	A	87	ALA	0	0.034	0.016	34.853	-0.005	-0.005	0.000	0.000	0.000	0.000
36	A	88	LEU	0	0.027	0.004	29.610	-0.005	-0.005	0.000	0.000	0.000	0.000
37	A	89	ALA	0	0.022	0.012	30.264	-0.007	-0.007	0.000	0.000	0.000	0.000
38	A	90	ILE	0	-0.037	-0.011	31.343	-0.008	-0.008	0.000	0.000	0.000	0.000
39	A	91	LEU	0	0.026	0.005	29.002	-0.007	-0.007	0.000	0.000	0.000	0.000
40	A	92	GLU	-1	-0.940	-0.956	26.517	-0.077	-0.077	0.000	0.000	0.000	0.000
41	A	93	ARG	1	0.889	0.935	26.239	0.057	0.057	0.000	0.000	0.000	0.000
42	A	94	GLN	0	-0.059	-0.017	28.071	-0.005	-0.005	0.000	0.000	0.000	0.000
43	A	95	THR	0	0.004	0.000	22.735	0.005	0.005	0.000	0.000	0.000	0.000
44	A	96	GLU	-1	-0.926	-0.965	22.793	-0.142	-0.142	0.000	0.000	0.000	0.000
45	A	97	ASN	0	0.045	0.020	16.381	-0.014	-0.014	0.000	0.000	0.000	0.000
46	A	98	ARG	1	0.862	0.903	12.788	0.322	0.322	0.000	0.000	0.000	0.000
47	A	99	LYS	1	0.969	0.992	11.030	0.192	0.192	0.000	0.000	0.000	0.000
48	A	100	PHE	0	0.007	-0.007	16.542	0.021	0.021	0.000	0.000	0.000	0.000
49	A	101	ARG	1	0.915	0.948	19.964	0.168	0.168	0.000	0.000	0.000	0.000
50	A	102	GLU	-1	-0.947	-0.973	17.050	-0.176	-0.176	0.000	0.000	0.000	0.000
51	A	103	ILE	0	-0.047	-0.013	17.863	0.016	0.016	0.000	0.000	0.000	0.000
52	A	104	LEU	0	-0.001	-0.004	20.932	0.012	0.012	0.000	0.000	0.000	0.000
53	A	105	LYS	1	0.977	0.997	22.657	0.132	0.132	0.000	0.000	0.000	0.000
54	A	106	GLN	0	-0.056	0.012	22.246	-0.003	-0.003	0.000	0.000	0.000	0.000
55	A	107	VAL	0	-0.019	-0.011	24.277	0.009	0.009	0.000	0.000	0.000	0.000
56	A	108	ARG	1	0.936	0.968	26.687	0.057	0.057	0.000	0.000	0.000	0.000
57	A	109	THR	0	-0.026	-0.040	26.760	0.000	0.000	0.000	0.000	0.000	0.000
58	A	110	ASP	-1	-0.839	-0.923	26.567	0.002	0.002	0.000	0.000	0.000	0.000
59	A	111	VAL	0	-0.034	-0.026	29.509	0.004	0.004	0.000	0.000	0.000	0.000
60	A	112	GLU	-1	-1.008	-1.001	32.195	-0.035	-0.035	0.000	0.000	0.000	0.000
61	A	113	GLY	0	-0.023	0.002	32.718	0.000	0.000	0.000	0.000	0.000	0.000
62	A	114	GLY	0	-0.021	-0.008	34.060	0.003	0.003	0.000	0.000	0.000	0.000
63	A	115	MET	0	-0.064	-0.008	28.932	0.005	0.005	0.000	0.000	0.000	0.000
64	A	116	ALA	0	0.006	0.003	33.673	-0.004	-0.004	0.000	0.000	0.000	0.000
65	A	117	PHE	0	0.054	0.008	29.997	0.000	0.000	0.000	0.000	0.000	0.000
66	A	118	SER	0	-0.046	-0.040	30.624	0.002	0.002	0.000	0.000	0.000	0.000
67	A	119	GLU	-1	-0.918	-0.965	29.661	0.047	0.047	0.000	0.000	0.000	0.000
68	A	120	ALA	0	0.060	0.034	27.736	0.005	0.005	0.000	0.000	0.000	0.000
69	A	121	LEU	0	-0.050	-0.028	26.000	0.000	0.000	0.000	0.000	0.000	0.000
70	A	122	SER	0	-0.089	-0.045	25.176	0.008	0.008	0.000	0.000	0.000	0.000
71	A	123	LYS	1	0.903	0.965	22.902	-0.011	-0.011	0.000	0.000	0.000	0.000
72	A	124	HIS	0	-0.037	-0.020	19.657	-0.001	-0.001	0.000	0.000	0.000	0.000
73	A	125	LYS	1	0.947	0.953	15.525	-0.171	-0.171	0.000	0.000	0.000	0.000
74	A	126	ILE	0	-0.049	-0.009	20.235	0.006	0.006	0.000	0.000	0.000	0.000
75	A	127	PHE	0	0.025	0.027	21.605	-0.006	-0.006	0.000	0.000	0.000	0.000
76	A	128	SER	0	0.035	0.018	25.191	0.010	0.010	0.000	0.000	0.000	0.000
77	A	129	ARG	1	1.021	0.987	25.553	-0.118	-0.118	0.000	0.000	0.000	0.000
78	A	130	LEU	0	0.017	0.022	29.240	-0.003	-0.003	0.000	0.000	0.000	0.000
79	A	131	TYR	0	0.026	0.005	28.868	-0.004	-0.004	0.000	0.000	0.000	0.000
80	A	132	VAL	0	0.047	0.018	28.007	-0.005	-0.005	0.000	0.000	0.000	0.000
81	A	133	ASN	0	-0.008	-0.016	30.978	-0.003	-0.003	0.000	0.000	0.000	0.000
82	A	134	LEU	0	-0.015	-0.002	34.077	-0.003	-0.003	0.000	0.000	0.000	0.000
83	A	135	VAL	0	0.018	0.006	31.899	-0.003	-0.003	0.000	0.000	0.000	0.000
84	A	136	ARG	1	0.899	0.957	34.753	-0.031	-0.031	0.000	0.000	0.000	0.000
85	A	137	ALA	0	-0.023	-0.017	36.225	-0.001	-0.001	0.000	0.000	0.000	0.000
86	A	138	GLY	0	0.058	-0.053	38.284	-0.002	-0.002	0.000	0.000	0.000	0.000
87	A	139	GLU	-1	-0.819	-0.921	34.855	0.017	0.017	0.000	0.000	0.000	0.000
88	A	140	THR	0	-0.057	-0.019	39.351	-0.001	-0.001	0.000	0.000	0.000	0.000
89	A	141	SER	0	-0.009	-0.006	42.407	0.000	0.000	0.000	0.000	0.000	0.000
90	A	142	GLY	0	-0.009	0.010	43.139	-0.001	-0.001	0.000	0.000	0.000	0.000
91	A	143	GLY	0	0.042	0.030	42.570	-0.002	-0.002	0.000	0.000	0.000	0.000
92	A	144	LEU	0	-0.014	-0.023	36.063	0.001	0.001	0.000	0.000	0.000	0.000
93	A	145	ASP	-1	-0.827	-0.909	38.362	-0.003	-0.003	0.000	0.000	0.000	0.000
94	A	146	LEU	0	0.009	0.004	39.659	0.000	0.000	0.000	0.000	0.000	0.000
95	A	147	ILE	0	-0.050	0.052	36.000	0.001	0.001	0.000	0.000	0.000	0.000
96	A	148	LEU	0	-0.026	-0.022	32.423	0.002	0.002	0.000	0.000	0.000	0.000
97	A	149	ASP	-1	-0.821	-0.882	35.442	-0.007	-0.007	0.000	0.000	0.000	0.000
98	A	150	ARG	1	0.931	0.966	37.499	-0.011	-0.011	0.000	0.000	0.000	0.000
99	A	151	LEU	0	-0.020	-0.011	32.344	0.002	0.002	0.000	0.000	0.000	0.000
100	A	152	ALA	0	0.023	0.011	32.620	0.001	0.001	0.000	0.000	0.000	0.000
101	A	153	SER	0	0.010	0.009	33.562	-0.002	-0.002	0.000	0.000	0.000	0.000
102	A	154	PHE	0	-0.103	-0.042	30.864	0.000	0.000	0.000	0.000	0.000	0.000
103	A	155	LEU	0	0.002	-0.005	27.982	0.001	0.001	0.000	0.000	0.000	0.000
104	A	156	GLU	-1	-0.802	-0.893	30.491	-0.018	-0.018	0.000	0.000	0.000	0.000
105	A	157	LYS	1	0.968	0.983	32.507	-0.007	-0.007	0.000	0.000	0.000	0.000
106	A	158	GLU	-1	-0.856	-0.915	27.494	0.031	0.031	0.000	0.000	0.000	0.000
107	A	159	LEU	0	-0.078	-0.069	26.569	0.000	0.000	0.000	0.000	0.000	0.000
108	A	160	GLU	-1	-0.984	-0.985	29.258	-0.010	-0.010	0.000	0.000	0.000	0.000
109	A	161	LEU	0	-0.051	-0.010	31.741	0.001	0.001	0.000	0.000	0.000	0.000
110	A	162	ARG	1	0.834	0.920	22.896	-0.031	-0.031	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)