FMO DATABASE

FMODB ID: 7212K

Calculation Name: 2F51-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2F51

Chain ID: A

ChEMBL ID:

UniProt ID: Q8IEV4

Base Structure: X-ray

Registration Date: 2023-09-20

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

Apendix: None

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	111
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-858170.752601
FMO2-HF: Nuclear repulsion	816150.595403
FMO2-HF: Total energy	-42020.157198
FMO2-MP2: Total energy	-42144.564221

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:2:SER)

Summations of interaction energy for fragment #1(A:2:SER)

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.
0.384	2.288	-0.005	-0.803	-1.095	0.004

Interaction energy analysis for fragmet #1(A:2:SER)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.023 / q_NPA : -0.018

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	4	PRO	0	-0.010	0.007	3.827	1.042	2.830	-0.004	-0.796	-0.988	0.004
4	A	5	ILE	0	-0.056	-0.020	5.784	0.744	0.860	-0.001	-0.007	-0.107	0.000
5	A	6	VAL	0	-0.013	-0.004	7.881	0.089	0.089	0.000	0.000	0.000	0.000
6	A	7	HIS	0	-0.059	-0.054	8.313	0.217	0.217	0.000	0.000	0.000	0.000
7	A	8	PHE	0	-0.028	-0.007	11.948	0.084	0.084	0.000	0.000	0.000	0.000
8	A	9	ASN	0	-0.043	-0.031	14.403	-0.054	-0.054	0.000	0.000	0.000	0.000
9	A	10	GLY	0	0.018	0.014	17.221	0.044	0.044	0.000	0.000	0.000	0.000
10	A	11	THR	0	0.019	0.010	20.222	-0.017	-0.017	0.000	0.000	0.000	0.000
11	A	12	HIS	0	0.143	0.050	22.325	-0.001	-0.001	0.000	0.000	0.000	0.000
12	A	13	GLU	-1	-0.923	-0.958	23.681	0.071	0.071	0.000	0.000	0.000	0.000
13	A	14	ALA	0	-0.033	-0.012	19.812	0.017	0.017	0.000	0.000	0.000	0.000
14	A	15	LEU	0	0.017	0.014	18.377	0.024	0.024	0.000	0.000	0.000	0.000
15	A	16	LEU	0	-0.001	-0.006	19.767	0.014	0.014	0.000	0.000	0.000	0.000
16	A	17	ASN	0	-0.012	-0.021	20.894	0.012	0.012	0.000	0.000	0.000	0.000
17	A	18	ARG	1	0.978	1.002	10.753	-0.404	-0.404	0.000	0.000	0.000	0.000
18	A	19	ILE	0	-0.015	-0.009	16.688	0.040	0.040	0.000	0.000	0.000	0.000
19	A	20	LYS	1	0.906	0.952	18.505	-0.083	-0.083	0.000	0.000	0.000	0.000
20	A	21	GLU	-1	-0.932	-0.965	15.542	0.383	0.383	0.000	0.000	0.000	0.000
21	A	22	ALA	0	-0.062	-0.011	14.681	0.074	0.074	0.000	0.000	0.000	0.000
22	A	23	PRO	0	0.012	0.009	13.367	-0.037	-0.037	0.000	0.000	0.000	0.000
23	A	24	GLY	0	0.004	-0.010	16.082	-0.034	-0.034	0.000	0.000	0.000	0.000
24	A	25	LEU	0	-0.097	-0.033	17.545	-0.002	-0.002	0.000	0.000	0.000	0.000
25	A	26	VAL	0	0.035	0.022	16.060	0.016	0.016	0.000	0.000	0.000	0.000
26	A	27	LEU	0	-0.028	0.001	16.182	-0.012	-0.012	0.000	0.000	0.000	0.000
27	A	28	VAL	0	-0.002	-0.001	16.480	-0.021	-0.021	0.000	0.000	0.000	0.000
28	A	29	ASP	-1	-0.855	-0.952	17.253	-0.388	-0.388	0.000	0.000	0.000	0.000
29	A	30	PHE	0	-0.003	0.006	18.653	-0.013	-0.013	0.000	0.000	0.000	0.000
30	A	31	PHE	0	0.018	-0.014	16.895	-0.018	-0.018	0.000	0.000	0.000	0.000
31	A	32	ALA	0	0.121	0.053	21.700	0.018	0.018	0.000	0.000	0.000	0.000
32	A	33	THR	0	0.022	-0.002	19.525	-0.016	-0.016	0.000	0.000	0.000	0.000
33	A	34	TRP	0	0.049	0.048	21.999	-0.026	-0.026	0.000	0.000	0.000	0.000
34	A	35	CYS	0	0.002	0.043	24.654	0.009	0.009	0.000	0.000	0.000	0.000
35	A	36	GLY	0	0.048	0.016	24.092	-0.027	-0.027	0.000	0.000	0.000	0.000
36	A	37	PRO	0	-0.017	-0.036	24.195	-0.030	-0.030	0.000	0.000	0.000	0.000
37	A	38	CYS	0	0.025	0.035	21.537	-0.018	-0.018	0.000	0.000	0.000	0.000
38	A	39	GLN	0	-0.055	-0.037	20.040	-0.056	-0.056	0.000	0.000	0.000	0.000
39	A	40	ARG	1	0.930	0.962	19.425	0.243	0.243	0.000	0.000	0.000	0.000
40	A	41	LEU	0	0.032	0.023	18.325	-0.041	-0.041	0.000	0.000	0.000	0.000
41	A	42	GLY	0	-0.006	-0.017	16.131	-0.066	-0.066	0.000	0.000	0.000	0.000
42	A	43	GLN	0	-0.015	-0.003	14.729	-0.085	-0.085	0.000	0.000	0.000	0.000
43	A	44	ILE	0	-0.029	-0.017	14.738	-0.099	-0.099	0.000	0.000	0.000	0.000
44	A	45	LEU	0	-0.006	-0.006	13.422	-0.069	-0.069	0.000	0.000	0.000	0.000
45	A	46	PRO	0	0.023	0.013	9.010	-0.030	-0.030	0.000	0.000	0.000	0.000
46	A	47	SER	0	0.017	0.019	9.074	-0.181	-0.181	0.000	0.000	0.000	0.000
47	A	48	ILE	0	-0.026	-0.014	11.195	0.053	0.053	0.000	0.000	0.000	0.000
48	A	49	ALA	0	0.016	0.009	9.160	0.103	0.103	0.000	0.000	0.000	0.000
49	A	50	GLU	-1	-0.995	-0.993	5.798	-2.952	-2.952	0.000	0.000	0.000	0.000
50	A	51	ALA	0	-0.052	-0.025	7.856	0.194	0.194	0.000	0.000	0.000	0.000
51	A	52	ASN	0	-0.060	-0.034	10.822	0.244	0.244	0.000	0.000	0.000	0.000
52	A	53	LYS	1	1.014	0.991	5.326	0.692	0.692	0.000	0.000	0.000	0.000
53	A	54	ASP	-1	-0.939	-0.961	9.982	0.125	0.125	0.000	0.000	0.000	0.000
54	A	55	VAL	0	-0.077	-0.026	12.731	0.054	0.054	0.000	0.000	0.000	0.000
55	A	56	THR	0	-0.027	-0.013	11.498	0.027	0.027	0.000	0.000	0.000	0.000
56	A	57	PHE	0	0.019	0.008	11.398	-0.046	-0.046	0.000	0.000	0.000	0.000
57	A	58	ILE	0	-0.002	-0.004	11.835	-0.024	-0.024	0.000	0.000	0.000	0.000
58	A	59	LYS	1	0.927	0.985	13.405	0.642	0.642	0.000	0.000	0.000	0.000
59	A	60	VAL	0	-0.001	-0.012	15.377	0.030	0.030	0.000	0.000	0.000	0.000
60	A	61	ASP	-1	-0.855	-0.930	18.110	-0.250	-0.250	0.000	0.000	0.000	0.000
61	A	62	VAL	0	0.030	-0.022	19.798	0.030	0.030	0.000	0.000	0.000	0.000
62	A	63	ASP	-1	-0.884	-0.930	23.132	-0.149	-0.149	0.000	0.000	0.000	0.000
63	A	64	LYS	1	0.840	0.925	17.791	0.185	0.185	0.000	0.000	0.000	0.000
64	A	65	ASN	0	-0.068	-0.030	18.335	0.051	0.051	0.000	0.000	0.000	0.000
65	A	66	GLY	0	0.097	0.055	22.586	0.002	0.002	0.000	0.000	0.000	0.000
66	A	67	ASN	0	0.030	0.008	26.187	-0.001	-0.001	0.000	0.000	0.000	0.000
67	A	68	ALA	0	-0.037	-0.017	22.691	0.007	0.007	0.000	0.000	0.000	0.000
68	A	69	ALA	0	0.015	0.003	24.228	0.003	0.003	0.000	0.000	0.000	0.000
69	A	70	ASP	-1	-0.891	-0.946	25.465	-0.073	-0.073	0.000	0.000	0.000	0.000
70	A	71	ALA	0	-0.076	-0.040	27.717	0.004	0.004	0.000	0.000	0.000	0.000
71	A	72	TYR	0	-0.064	-0.034	23.844	0.014	0.014	0.000	0.000	0.000	0.000
72	A	73	GLY	0	-0.010	0.010	27.389	-0.002	-0.002	0.000	0.000	0.000	0.000
73	A	74	VAL	0	-0.071	-0.032	25.001	-0.008	-0.008	0.000	0.000	0.000	0.000
74	A	75	SER	0	0.045	0.022	28.424	0.002	0.002	0.000	0.000	0.000	0.000
75	A	76	SER	0	-0.054	-0.028	29.648	-0.009	-0.009	0.000	0.000	0.000	0.000
76	A	77	ILE	0	-0.001	0.016	25.106	-0.004	-0.004	0.000	0.000	0.000	0.000
77	A	78	PRO	0	-0.002	-0.034	22.717	0.001	0.001	0.000	0.000	0.000	0.000
78	A	79	ALA	0	-0.004	0.002	23.711	0.012	0.012	0.000	0.000	0.000	0.000
79	A	80	LEU	0	-0.011	0.001	20.231	-0.014	-0.014	0.000	0.000	0.000	0.000
80	A	81	PHE	0	0.034	0.008	21.865	0.023	0.023	0.000	0.000	0.000	0.000
81	A	82	PHE	0	0.017	0.015	18.983	-0.006	-0.006	0.000	0.000	0.000	0.000
82	A	83	VAL	0	0.013	-0.002	20.588	0.015	0.015	0.000	0.000	0.000	0.000
83	A	84	LYS	1	0.983	0.977	20.621	-0.028	-0.028	0.000	0.000	0.000	0.000
84	A	85	LYS	1	0.883	0.959	21.300	-0.210	-0.210	0.000	0.000	0.000	0.000
85	A	86	GLU	-1	-0.925	-0.975	23.049	0.037	0.037	0.000	0.000	0.000	0.000
86	A	87	GLY	0	0.039	0.028	26.586	-0.005	-0.005	0.000	0.000	0.000	0.000
87	A	88	ASN	0	-0.046	-0.037	26.166	0.013	0.013	0.000	0.000	0.000	0.000
88	A	89	GLU	-1	-0.924	-0.959	27.836	0.041	0.041	0.000	0.000	0.000	0.000
89	A	90	ILE	0	-0.013	-0.007	23.044	0.011	0.011	0.000	0.000	0.000	0.000
90	A	91	LYS	1	0.971	1.003	25.516	0.001	0.001	0.000	0.000	0.000	0.000
91	A	92	THR	0	0.029	-0.005	25.170	-0.005	-0.005	0.000	0.000	0.000	0.000
92	A	93	LEU	0	-0.173	-0.086	23.342	0.006	0.006	0.000	0.000	0.000	0.000
93	A	94	ASP	-1	-0.737	-0.836	25.540	-0.131	-0.131	0.000	0.000	0.000	0.000
94	A	95	GLN	0	-0.011	0.002	25.610	-0.002	-0.002	0.000	0.000	0.000	0.000
95	A	96	PHE	0	-0.043	-0.019	23.257	0.005	0.005	0.000	0.000	0.000	0.000
96	A	97	VAL	0	0.068	0.040	26.472	-0.010	-0.010	0.000	0.000	0.000	0.000
97	A	98	GLY	0	-0.008	0.001	26.470	0.006	0.006	0.000	0.000	0.000	0.000
98	A	99	ALA	0	-0.016	-0.015	23.044	-0.007	-0.007	0.000	0.000	0.000	0.000
99	A	100	ASP	-1	-0.899	-0.947	24.176	-0.230	-0.230	0.000	0.000	0.000	0.000
100	A	101	VAL	0	0.034	-0.004	19.749	-0.002	-0.002	0.000	0.000	0.000	0.000
101	A	102	SER	0	-0.002	-0.010	21.568	-0.021	-0.021	0.000	0.000	0.000	0.000
102	A	103	ARG	1	0.898	0.969	23.960	0.153	0.153	0.000	0.000	0.000	0.000
103	A	104	ILE	0	-0.006	-0.002	18.273	0.012	0.012	0.000	0.000	0.000	0.000
104	A	105	LYS	1	0.953	0.968	17.709	0.470	0.470	0.000	0.000	0.000	0.000
105	A	106	ALA	0	0.053	0.035	20.500	0.015	0.015	0.000	0.000	0.000	0.000
106	A	107	ASH	0	-0.087	-0.088	22.462	0.026	0.026	0.000	0.000	0.000	0.000
107	A	108	ILE	0	-0.031	-0.014	16.345	0.025	0.025	0.000	0.000	0.000	0.000
108	A	109	GLU	-1	-0.961	-0.977	20.030	-0.206	-0.206	0.000	0.000	0.000	0.000
109	A	110	LYS	1	0.917	0.972	21.834	0.116	0.116	0.000	0.000	0.000	0.000
110	A	111	PHE	0	-0.050	-0.039	22.079	0.023	0.023	0.000	0.000	0.000	0.000
111	A	112	LYS	1	0.942	0.994	19.222	-0.007	-0.007	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:SER)