FMO DATABASE

FMODB ID: 224ZR

Calculation Name: 1S29-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1S29

Chain ID: A

ChEMBL ID:

UniProt ID: Q9NIH4

Base Structure: X-ray

Registration Date: 2023-03-13

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	92
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-668506.007657
FMO2-HF: Nuclear repulsion	631701.417759
FMO2-HF: Total energy	-36804.589898
FMO2-MP2: Total energy	-36911.904924

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:1:GLY)

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

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.
-5.71	-2.121	0.692	-1.657	-2.625	-0.008

Interaction energy analysis for fragmet #1(A:1:GLY)

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 : 0.010

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

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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	3	HIS	0	0.018	0.014	3.281	-1.706	-0.143	0.123	-0.724	-0.962	-0.001
4	A	4	MET	0	-0.086	-0.046	3.063	1.080	1.680	0.063	-0.182	-0.481	0.000
5	A	5	PRO	0	0.038	0.030	2.818	-2.732	-1.661	0.510	-0.728	-0.854	-0.007
6	A	6	LEU	0	0.057	0.038	4.993	0.307	0.468	-0.001	-0.007	-0.153	0.000
7	A	7	SER	0	0.019	-0.011	6.047	0.226	0.226	0.000	0.000	0.000	0.000
8	A	8	SER	0	0.079	0.027	9.286	-0.019	-0.019	0.000	0.000	0.000	0.000
9	A	9	GLU	-1	-0.881	-0.948	12.679	-0.218	-0.218	0.000	0.000	0.000	0.000
10	A	10	ASN	0	-0.020	-0.026	7.204	0.167	0.167	0.000	0.000	0.000	0.000
11	A	11	LYS	1	0.951	0.996	9.848	0.855	0.855	0.000	0.000	0.000	0.000
12	A	12	GLN	0	0.023	0.009	11.325	0.048	0.048	0.000	0.000	0.000	0.000
13	A	13	LYS	1	0.881	0.948	11.987	0.299	0.299	0.000	0.000	0.000	0.000
14	A	14	LEU	0	0.032	0.020	9.196	0.067	0.067	0.000	0.000	0.000	0.000
15	A	15	GLN	0	-0.002	-0.002	12.620	0.030	0.030	0.000	0.000	0.000	0.000
16	A	16	LYS	1	0.964	0.973	15.765	0.229	0.229	0.000	0.000	0.000	0.000
17	A	17	GLN	0	0.002	0.008	13.338	0.058	0.058	0.000	0.000	0.000	0.000
18	A	18	VAL	0	0.020	0.009	14.562	0.038	0.038	0.000	0.000	0.000	0.000
19	A	19	GLU	-1	-0.825	-0.892	17.146	-0.169	-0.169	0.000	0.000	0.000	0.000
20	A	20	PHE	0	-0.055	-0.025	18.988	0.028	0.028	0.000	0.000	0.000	0.000
21	A	21	TYR	0	0.033	0.009	15.743	0.025	0.025	0.000	0.000	0.000	0.000
22	A	22	PHE	0	0.045	0.029	19.433	0.015	0.015	0.000	0.000	0.000	0.000
23	A	23	SER	0	-0.014	0.012	23.385	0.007	0.007	0.000	0.000	0.000	0.000
24	A	24	ASP	-1	-0.746	-0.878	25.585	-0.066	-0.066	0.000	0.000	0.000	0.000
25	A	25	VAL	0	-0.047	-0.017	28.035	0.007	0.007	0.000	0.000	0.000	0.000
26	A	26	ASN	0	-0.048	-0.042	23.597	0.018	0.018	0.000	0.000	0.000	0.000
27	A	27	VAL	0	0.076	0.058	26.170	0.008	0.008	0.000	0.000	0.000	0.000
28	A	28	GLN	0	-0.049	-0.043	27.005	0.008	0.008	0.000	0.000	0.000	0.000
29	A	29	ARG	1	0.876	0.928	28.195	0.024	0.024	0.000	0.000	0.000	0.000
30	A	30	ASP	-1	-0.869	-0.927	23.501	-0.021	-0.021	0.000	0.000	0.000	0.000
31	A	31	ILE	0	-0.002	-0.008	27.101	-0.006	-0.006	0.000	0.000	0.000	0.000
32	A	32	PHE	0	0.007	0.011	21.297	-0.001	-0.001	0.000	0.000	0.000	0.000
33	A	33	LEU	0	0.011	0.009	21.730	-0.004	-0.004	0.000	0.000	0.000	0.000
34	A	34	LYS	1	0.912	0.946	24.688	0.022	0.022	0.000	0.000	0.000	0.000
35	A	35	GLY	0	-0.001	0.010	27.978	-0.002	-0.002	0.000	0.000	0.000	0.000
36	A	36	LYS	1	0.949	0.979	22.472	0.030	0.030	0.000	0.000	0.000	0.000
37	A	37	MET	0	-0.044	-0.014	25.619	-0.005	-0.005	0.000	0.000	0.000	0.000
38	A	38	ALA	0	-0.012	-0.006	27.286	-0.003	-0.003	0.000	0.000	0.000	0.000
39	A	39	GLU	-1	-0.971	-0.974	26.187	-0.042	-0.042	0.000	0.000	0.000	0.000
40	A	40	ASN	0	-0.014	-0.014	26.630	-0.004	-0.004	0.000	0.000	0.000	0.000
41	A	41	ALA	0	0.010	-0.005	30.714	0.000	0.000	0.000	0.000	0.000	0.000
42	A	42	GLU	-1	-0.946	-0.965	29.060	-0.099	-0.099	0.000	0.000	0.000	0.000
43	A	43	GLY	0	-0.026	-0.003	28.178	-0.007	-0.007	0.000	0.000	0.000	0.000
44	A	44	PHE	0	-0.063	-0.045	23.483	-0.010	-0.010	0.000	0.000	0.000	0.000
45	A	45	VAL	0	0.010	0.006	19.990	0.014	0.014	0.000	0.000	0.000	0.000
46	A	46	SER	0	0.061	0.034	19.214	-0.021	-0.021	0.000	0.000	0.000	0.000
47	A	47	LEU	0	0.042	-0.005	14.398	0.005	0.005	0.000	0.000	0.000	0.000
48	A	48	GLU	-1	-0.917	-0.962	14.230	-0.105	-0.105	0.000	0.000	0.000	0.000
49	A	49	THR	0	-0.011	-0.007	15.204	0.043	0.043	0.000	0.000	0.000	0.000
50	A	50	LEU	0	-0.029	0.000	14.851	0.024	0.024	0.000	0.000	0.000	0.000
51	A	51	LEU	0	-0.027	-0.011	9.317	0.005	0.005	0.000	0.000	0.000	0.000
52	A	52	THR	0	-0.068	-0.036	11.984	0.069	0.069	0.000	0.000	0.000	0.000
53	A	53	PHE	0	0.003	0.007	14.693	0.037	0.037	0.000	0.000	0.000	0.000
54	A	54	LYS	1	1.012	0.995	13.362	-0.131	-0.131	0.000	0.000	0.000	0.000
55	A	55	ARG	1	0.837	0.914	12.246	0.064	0.064	0.000	0.000	0.000	0.000
56	A	56	VAL	0	0.030	0.033	10.516	-0.050	-0.050	0.000	0.000	0.000	0.000
57	A	57	ASN	0	0.045	0.013	9.040	-0.063	-0.063	0.000	0.000	0.000	0.000
58	A	58	SER	0	-0.125	-0.047	7.852	0.087	0.087	0.000	0.000	0.000	0.000
59	A	59	VAL	0	-0.062	-0.026	6.264	0.097	0.097	0.000	0.000	0.000	0.000
60	A	60	THR	0	-0.019	-0.052	4.395	-0.615	-0.482	-0.001	-0.009	-0.123	0.000
61	A	61	THR	0	-0.008	-0.005	4.723	0.624	0.660	-0.001	-0.002	-0.033	0.000
62	A	62	ASP	-1	-0.803	-0.896	6.376	-0.899	-0.899	0.000	0.000	0.000	0.000
63	A	63	VAL	0	0.038	0.009	7.775	-0.097	-0.097	0.000	0.000	0.000	0.000
64	A	64	LYS	1	0.949	0.959	10.279	0.532	0.532	0.000	0.000	0.000	0.000
65	A	65	GLU	-1	-0.877	-0.898	4.792	-3.989	-3.964	-0.001	-0.005	-0.019	0.000
66	A	66	VAL	0	-0.031	-0.019	9.152	0.115	0.115	0.000	0.000	0.000	0.000
67	A	67	VAL	0	0.030	0.025	11.400	0.080	0.080	0.000	0.000	0.000	0.000
68	A	68	GLU	-1	-0.876	-0.931	11.521	-0.514	-0.514	0.000	0.000	0.000	0.000
69	A	69	ALA	0	-0.075	-0.039	11.250	0.054	0.054	0.000	0.000	0.000	0.000
70	A	70	ILE	0	-0.008	-0.009	13.196	0.074	0.074	0.000	0.000	0.000	0.000
71	A	71	ARG	1	0.831	0.905	16.102	0.465	0.465	0.000	0.000	0.000	0.000
72	A	72	PRO	0	-0.038	-0.025	17.050	0.031	0.031	0.000	0.000	0.000	0.000
73	A	73	SER	0	-0.047	-0.037	19.718	0.032	0.032	0.000	0.000	0.000	0.000
74	A	74	GLU	-1	-0.916	-0.950	21.364	-0.148	-0.148	0.000	0.000	0.000	0.000
75	A	75	LYS	1	0.897	0.939	23.719	0.155	0.155	0.000	0.000	0.000	0.000
76	A	76	LEU	0	-0.025	-0.011	19.197	0.011	0.011	0.000	0.000	0.000	0.000
77	A	77	VAL	0	-0.011	-0.002	23.113	-0.004	-0.004	0.000	0.000	0.000	0.000
78	A	78	LEU	0	-0.008	-0.008	17.637	0.004	0.004	0.000	0.000	0.000	0.000
79	A	79	SER	0	-0.012	-0.028	21.721	0.008	0.008	0.000	0.000	0.000	0.000
80	A	80	GLU	-1	-0.909	-0.955	22.661	-0.180	-0.180	0.000	0.000	0.000	0.000
81	A	81	ASP	-1	-0.857	-0.906	22.186	-0.189	-0.189	0.000	0.000	0.000	0.000
82	A	82	GLY	0	-0.041	-0.019	19.051	-0.021	-0.021	0.000	0.000	0.000	0.000
83	A	83	LEU	0	-0.022	-0.006	17.475	-0.041	-0.041	0.000	0.000	0.000	0.000
84	A	84	MET	0	-0.048	-0.027	18.693	0.015	0.015	0.000	0.000	0.000	0.000
85	A	85	VAL	0	-0.017	0.000	18.624	-0.018	-0.018	0.000	0.000	0.000	0.000
86	A	86	ARG	1	0.958	1.006	21.106	0.141	0.141	0.000	0.000	0.000	0.000
87	A	87	ARG	1	0.796	0.864	24.111	0.074	0.074	0.000	0.000	0.000	0.000
88	A	88	ARG	1	0.924	0.968	25.949	0.123	0.123	0.000	0.000	0.000	0.000
89	A	89	ASP	-1	-0.910	-0.955	28.038	-0.092	-0.092	0.000	0.000	0.000	0.000
90	A	90	PRO	0	0.018	0.002	30.077	-0.001	-0.001	0.000	0.000	0.000	0.000
91	A	91	LEU	0	-0.012	0.001	29.686	0.000	0.000	0.000	0.000	0.000	0.000
92	A	92	PRO	0	-0.009	0.008	31.520	0.003	0.003	0.000	0.000	0.000	0.000

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