FMO DATABASE

FMODB ID: 6N1NZ

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

Total energy (hartree)

FMO2-HF: Electronic energy	-862593.690036
FMO2-HF: Nuclear repulsion	820572.922053
FMO2-HF: Total energy	-42020.767983
FMO2-MP2: Total energy	-42145.221245

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.
1.647	3.676	-0.001	-0.844	-1.184	0.003

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 : 0.013 / q_NPA : 0.001

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	-0.022	-0.002	3.790	-1.012	0.856	0.001	-0.834	-1.036	0.003
4	A	5	ILE	0	-0.056	-0.021	4.915	1.638	1.743	-0.001	-0.006	-0.098	0.000
5	A	6	VAL	0	-0.011	-0.010	8.041	0.068	0.068	0.000	0.000	0.000	0.000
6	A	7	HIS	0	-0.036	-0.041	8.526	0.597	0.597	0.000	0.000	0.000	0.000
7	A	8	PHE	0	-0.013	0.003	11.984	0.121	0.121	0.000	0.000	0.000	0.000
8	A	9	ASN	0	-0.021	-0.015	14.138	0.081	0.081	0.000	0.000	0.000	0.000
9	A	10	GLY	0	0.018	0.015	17.132	0.037	0.037	0.000	0.000	0.000	0.000
10	A	11	THR	0	0.030	0.012	20.190	-0.010	-0.010	0.000	0.000	0.000	0.000
11	A	12	HIS	0	0.114	0.043	22.200	-0.034	-0.034	0.000	0.000	0.000	0.000
12	A	13	GLU	-1	-0.774	-0.879	23.216	-0.179	-0.179	0.000	0.000	0.000	0.000
13	A	14	ALA	0	-0.023	-0.001	19.735	0.005	0.005	0.000	0.000	0.000	0.000
14	A	15	LEU	0	0.013	0.018	17.941	-0.023	-0.023	0.000	0.000	0.000	0.000
15	A	16	LEU	0	0.014	0.003	19.341	-0.023	-0.023	0.000	0.000	0.000	0.000
16	A	17	ASN	0	-0.073	-0.045	20.394	0.017	0.017	0.000	0.000	0.000	0.000
17	A	18	ARG	1	0.969	0.990	10.279	0.528	0.528	0.000	0.000	0.000	0.000
18	A	19	ILE	0	-0.027	-0.008	15.926	-0.046	-0.046	0.000	0.000	0.000	0.000
19	A	20	LYS	1	0.844	0.912	18.314	0.172	0.172	0.000	0.000	0.000	0.000
20	A	21	GLU	-1	-0.923	-0.970	14.586	-0.204	-0.204	0.000	0.000	0.000	0.000
21	A	22	ALA	0	-0.063	-0.013	14.644	0.020	0.020	0.000	0.000	0.000	0.000
22	A	23	PRO	0	-0.018	-0.010	13.116	0.039	0.039	0.000	0.000	0.000	0.000
23	A	24	GLY	0	0.024	0.002	16.116	0.035	0.035	0.000	0.000	0.000	0.000
24	A	25	LEU	0	-0.070	-0.021	16.694	0.014	0.014	0.000	0.000	0.000	0.000
25	A	26	VAL	0	0.022	0.014	15.330	-0.070	-0.070	0.000	0.000	0.000	0.000
26	A	27	LEU	0	-0.021	-0.003	15.441	0.059	0.059	0.000	0.000	0.000	0.000
27	A	28	VAL	0	0.004	0.011	15.770	-0.111	-0.111	0.000	0.000	0.000	0.000
28	A	29	ASP	-1	-0.773	-0.906	17.114	-0.666	-0.666	0.000	0.000	0.000	0.000
29	A	30	PHE	0	0.006	0.013	18.759	-0.041	-0.041	0.000	0.000	0.000	0.000
30	A	31	PHE	0	0.025	-0.017	16.783	0.013	0.013	0.000	0.000	0.000	0.000
31	A	32	ALA	0	0.096	0.041	21.752	0.017	0.017	0.000	0.000	0.000	0.000
32	A	33	THR	0	-0.008	0.001	19.501	-0.003	-0.003	0.000	0.000	0.000	0.000
33	A	34	TRP	0	0.000	-0.007	21.749	-0.009	-0.009	0.000	0.000	0.000	0.000
34	A	35	CYS	0	0.006	0.041	24.472	0.021	0.021	0.000	0.000	0.000	0.000
35	A	36	GLY	0	0.032	0.014	24.111	-0.036	-0.036	0.000	0.000	0.000	0.000
36	A	37	PRO	0	-0.032	-0.040	24.142	-0.033	-0.033	0.000	0.000	0.000	0.000
37	A	38	CYS	0	0.005	0.023	21.403	-0.036	-0.036	0.000	0.000	0.000	0.000
38	A	39	GLN	0	-0.036	-0.013	19.843	-0.069	-0.069	0.000	0.000	0.000	0.000
39	A	40	ARG	1	0.958	0.972	19.125	0.324	0.324	0.000	0.000	0.000	0.000
40	A	41	LEU	0	0.021	0.022	18.292	-0.032	-0.032	0.000	0.000	0.000	0.000
41	A	42	GLY	0	0.002	-0.012	15.997	-0.100	-0.100	0.000	0.000	0.000	0.000
42	A	43	GLN	0	-0.045	-0.020	14.641	-0.130	-0.130	0.000	0.000	0.000	0.000
43	A	44	ILE	0	-0.029	-0.018	14.780	-0.063	-0.063	0.000	0.000	0.000	0.000
44	A	45	LEU	0	0.021	0.011	13.215	-0.078	-0.078	0.000	0.000	0.000	0.000
45	A	46	PRO	0	0.043	0.020	8.927	-0.114	-0.114	0.000	0.000	0.000	0.000
46	A	47	SER	0	-0.031	0.003	9.507	-0.223	-0.223	0.000	0.000	0.000	0.000
47	A	48	ILE	0	-0.004	-0.009	11.902	0.084	0.084	0.000	0.000	0.000	0.000
48	A	49	ALA	0	0.029	0.018	8.478	0.107	0.107	0.000	0.000	0.000	0.000
49	A	50	GLU	-1	-0.895	-0.944	6.403	-3.572	-3.572	0.000	0.000	0.000	0.000
50	A	51	ALA	0	-0.044	-0.025	8.274	0.304	0.304	0.000	0.000	0.000	0.000
51	A	52	ASN	0	-0.069	-0.039	10.541	0.351	0.351	0.000	0.000	0.000	0.000
52	A	53	LYS	1	0.895	0.938	4.482	2.966	3.022	-0.001	-0.004	-0.050	0.000
53	A	54	ASP	-1	-0.899	-0.945	9.067	-0.339	-0.339	0.000	0.000	0.000	0.000
54	A	55	VAL	0	-0.063	-0.027	11.639	0.115	0.115	0.000	0.000	0.000	0.000
55	A	56	THR	0	-0.029	-0.016	10.925	-0.193	-0.193	0.000	0.000	0.000	0.000
56	A	57	PHE	0	0.030	0.012	10.325	0.156	0.156	0.000	0.000	0.000	0.000
57	A	58	ILE	0	-0.005	-0.006	11.407	-0.178	-0.178	0.000	0.000	0.000	0.000
58	A	59	LYS	1	0.825	0.936	12.986	1.001	1.001	0.000	0.000	0.000	0.000
59	A	60	VAL	0	0.011	-0.008	15.104	0.019	0.019	0.000	0.000	0.000	0.000
60	A	61	ASP	-1	-0.828	-0.923	17.926	-0.436	-0.436	0.000	0.000	0.000	0.000
61	A	62	VAL	0	0.037	-0.010	19.754	0.031	0.031	0.000	0.000	0.000	0.000
62	A	63	ASP	-1	-0.820	-0.895	23.340	-0.305	-0.305	0.000	0.000	0.000	0.000
63	A	64	LYS	1	0.813	0.901	17.743	0.442	0.442	0.000	0.000	0.000	0.000
64	A	65	ASN	0	-0.058	-0.038	18.136	0.018	0.018	0.000	0.000	0.000	0.000
65	A	66	GLY	0	0.079	0.055	22.440	0.004	0.004	0.000	0.000	0.000	0.000
66	A	67	ASN	0	0.015	-0.001	26.097	-0.007	-0.007	0.000	0.000	0.000	0.000
67	A	68	ALA	0	-0.038	-0.020	22.590	0.013	0.013	0.000	0.000	0.000	0.000
68	A	69	ALA	0	-0.001	-0.005	24.198	-0.002	-0.002	0.000	0.000	0.000	0.000
69	A	70	ASP	-1	-0.889	-0.948	25.440	-0.217	-0.217	0.000	0.000	0.000	0.000
70	A	71	ALA	0	-0.046	-0.023	27.758	0.011	0.011	0.000	0.000	0.000	0.000
71	A	72	TYR	0	-0.045	-0.022	23.136	0.003	0.003	0.000	0.000	0.000	0.000
72	A	73	GLY	0	-0.014	0.009	27.336	-0.003	-0.003	0.000	0.000	0.000	0.000
73	A	74	VAL	0	-0.071	-0.035	24.997	-0.004	-0.004	0.000	0.000	0.000	0.000
74	A	75	SER	0	0.026	0.005	28.391	0.016	0.016	0.000	0.000	0.000	0.000
75	A	76	SER	0	-0.039	-0.004	29.920	-0.003	-0.003	0.000	0.000	0.000	0.000
76	A	77	ILE	0	-0.003	0.004	24.965	-0.015	-0.015	0.000	0.000	0.000	0.000
77	A	78	PRO	0	-0.011	-0.030	22.179	0.019	0.019	0.000	0.000	0.000	0.000
78	A	79	ALA	0	-0.024	-0.015	23.373	0.026	0.026	0.000	0.000	0.000	0.000
79	A	80	LEU	0	-0.010	0.012	19.489	-0.040	-0.040	0.000	0.000	0.000	0.000
80	A	81	PHE	0	0.028	-0.004	21.038	0.053	0.053	0.000	0.000	0.000	0.000
81	A	82	PHE	0	0.014	0.018	18.028	-0.040	-0.040	0.000	0.000	0.000	0.000
82	A	83	VAL	0	0.006	-0.005	19.888	0.053	0.053	0.000	0.000	0.000	0.000
83	A	84	LYS	1	0.919	0.958	19.905	0.235	0.235	0.000	0.000	0.000	0.000
84	A	85	LYS	1	0.931	0.976	20.333	0.137	0.137	0.000	0.000	0.000	0.000
85	A	86	GLU	-1	-0.903	-0.969	22.218	-0.155	-0.155	0.000	0.000	0.000	0.000
86	A	87	GLY	0	0.023	0.019	25.851	0.006	0.006	0.000	0.000	0.000	0.000
87	A	88	ASN	0	-0.078	-0.040	25.947	0.003	0.003	0.000	0.000	0.000	0.000
88	A	89	GLU	-1	-0.911	-0.955	27.050	-0.127	-0.127	0.000	0.000	0.000	0.000
89	A	90	ILE	0	-0.010	-0.014	22.548	-0.010	-0.010	0.000	0.000	0.000	0.000
90	A	91	LYS	1	0.893	0.965	24.940	0.207	0.207	0.000	0.000	0.000	0.000
91	A	92	THR	0	0.025	0.001	24.499	-0.024	-0.024	0.000	0.000	0.000	0.000
92	A	93	LEU	0	-0.093	-0.042	22.500	0.028	0.028	0.000	0.000	0.000	0.000
93	A	94	ASP	-1	-0.765	-0.830	24.529	-0.298	-0.298	0.000	0.000	0.000	0.000
94	A	95	GLN	0	0.003	0.002	24.538	-0.032	-0.032	0.000	0.000	0.000	0.000
95	A	96	PHE	0	-0.041	-0.020	22.484	0.025	0.025	0.000	0.000	0.000	0.000
96	A	97	VAL	0	0.048	0.022	25.745	-0.024	-0.024	0.000	0.000	0.000	0.000
97	A	98	GLY	0	0.017	0.017	25.765	0.025	0.025	0.000	0.000	0.000	0.000
98	A	99	ALA	0	-0.015	-0.012	22.944	-0.022	-0.022	0.000	0.000	0.000	0.000
99	A	100	ASP	-1	-0.867	-0.929	23.815	-0.373	-0.373	0.000	0.000	0.000	0.000
100	A	101	VAL	0	0.024	-0.010	19.381	-0.021	-0.021	0.000	0.000	0.000	0.000
101	A	102	SER	0	-0.021	-0.005	21.220	-0.033	-0.033	0.000	0.000	0.000	0.000
102	A	103	ARG	1	0.860	0.913	23.511	0.314	0.314	0.000	0.000	0.000	0.000
103	A	104	ILE	0	-0.013	-0.010	17.684	-0.004	-0.004	0.000	0.000	0.000	0.000
104	A	105	LYS	1	0.943	0.977	17.948	0.584	0.584	0.000	0.000	0.000	0.000
105	A	106	ALA	0	0.087	0.048	20.137	0.011	0.011	0.000	0.000	0.000	0.000
106	A	107	ASH	0	-0.080	-0.090	22.011	0.050	0.050	0.000	0.000	0.000	0.000
107	A	108	ILE	0	-0.014	0.000	15.631	0.017	0.017	0.000	0.000	0.000	0.000
108	A	109	GLU	-1	-0.924	-0.974	19.346	-0.375	-0.375	0.000	0.000	0.000	0.000
109	A	110	LYS	1	0.873	0.959	21.336	0.311	0.311	0.000	0.000	0.000	0.000
110	A	111	PHE	0	-0.050	-0.036	21.152	0.036	0.036	0.000	0.000	0.000	0.000
111	A	112	LYS	1	0.909	0.980	17.445	0.257	0.257	0.000	0.000	0.000	0.000

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