FMO DATABASE

FMODB ID: 49ZMN

Calculation Name: 1THX-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1THX

Chain ID: A

ChEMBL ID:

UniProt ID: P20857

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:

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	107
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-851131.113389
FMO2-HF: Nuclear repulsion	809313.344022
FMO2-HF: Total energy	-41817.769366
FMO2-MP2: Total energy	-41940.564129

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:SER)

Summations of interaction energy for fragment #1(A:1: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.
-29.998	-26.599	11.286	-7.646	-7.04	-0.047

Interaction energy analysis for fragmet #1(A:1: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 : -0.024

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	3	GLY	0	0.051	0.015	3.208	-2.769	-0.878	0.036	-0.906	-1.021	0.005
4	A	4	VAL	0	-0.030	-0.006	3.625	-1.063	-0.549	0.014	-0.188	-0.341	-0.001
5	A	5	ILE	0	-0.004	0.011	4.695	0.376	0.429	-0.001	-0.005	-0.047	0.000
6	A	6	THR	0	-0.049	-0.037	7.270	-0.344	-0.344	0.000	0.000	0.000	0.000
7	A	7	ILE	0	0.015	0.018	10.030	0.114	0.114	0.000	0.000	0.000	0.000
8	A	8	THR	0	0.027	0.004	12.673	-0.103	-0.103	0.000	0.000	0.000	0.000
9	A	9	ASP	-1	-0.754	-0.886	15.889	0.148	0.148	0.000	0.000	0.000	0.000
10	A	10	ALA	0	-0.057	-0.024	18.076	-0.001	-0.001	0.000	0.000	0.000	0.000
11	A	11	GLU	-1	-0.858	-0.933	13.281	0.586	0.586	0.000	0.000	0.000	0.000
12	A	12	PHE	0	0.004	0.000	13.368	0.054	0.054	0.000	0.000	0.000	0.000
13	A	13	GLU	-1	-0.920	-0.970	13.423	0.254	0.254	0.000	0.000	0.000	0.000
14	A	14	SER	0	0.009	-0.009	13.120	-0.036	-0.036	0.000	0.000	0.000	0.000
15	A	15	GLU	-1	-0.858	-0.906	8.294	1.579	1.579	0.000	0.000	0.000	0.000
16	A	16	VAL	0	-0.009	-0.010	8.579	0.049	0.049	0.000	0.000	0.000	0.000
17	A	17	LEU	0	-0.058	-0.017	10.716	-0.040	-0.040	0.000	0.000	0.000	0.000
18	A	18	LYS	1	0.937	0.961	13.065	-0.363	-0.363	0.000	0.000	0.000	0.000
19	A	19	ALA	0	-0.042	0.010	7.573	0.105	0.105	0.000	0.000	0.000	0.000
20	A	20	GLU	-1	-0.897	-0.955	8.794	0.258	0.258	0.000	0.000	0.000	0.000
21	A	21	GLN	0	-0.084	-0.034	3.138	-3.498	-2.547	0.032	-0.530	-0.452	0.005
22	A	22	PRO	0	-0.024	-0.010	8.197	0.138	0.138	0.000	0.000	0.000	0.000
23	A	23	VAL	0	0.021	0.004	7.043	-0.210	-0.210	0.000	0.000	0.000	0.000
24	A	24	LEU	0	-0.006	0.001	7.728	0.064	0.064	0.000	0.000	0.000	0.000
25	A	25	VAL	0	0.003	-0.002	9.138	0.026	0.026	0.000	0.000	0.000	0.000
26	A	26	TYR	0	-0.029	-0.023	11.688	-0.021	-0.021	0.000	0.000	0.000	0.000
27	A	27	PHE	0	0.019	0.001	13.646	0.081	0.081	0.000	0.000	0.000	0.000
28	A	28	TRP	0	-0.008	-0.024	15.278	-0.050	-0.050	0.000	0.000	0.000	0.000
29	A	29	ALA	0	0.073	0.025	18.820	0.032	0.032	0.000	0.000	0.000	0.000
30	A	30	SER	0	0.035	0.017	21.616	-0.024	-0.024	0.000	0.000	0.000	0.000
31	A	31	TRP	0	-0.012	-0.009	23.050	-0.020	-0.020	0.000	0.000	0.000	0.000
32	A	32	CYS	0	0.001	0.025	19.546	-0.055	-0.055	0.000	0.000	0.000	0.000
33	A	33	GLY	0	0.053	0.028	23.354	-0.010	-0.010	0.000	0.000	0.000	0.000
34	A	34	PRO	0	0.029	-0.006	23.726	-0.013	-0.013	0.000	0.000	0.000	0.000
35	A	36	GLN	0	-0.043	-0.023	18.949	-0.019	-0.019	0.000	0.000	0.000	0.000
36	A	37	LEU	0	-0.019	-0.010	19.752	-0.017	-0.017	0.000	0.000	0.000	0.000
37	A	38	MET	0	0.038	0.031	15.824	-0.048	-0.048	0.000	0.000	0.000	0.000
38	A	39	SER	0	-0.004	0.006	14.610	-0.069	-0.069	0.000	0.000	0.000	0.000
39	A	40	PRO	0	-0.038	-0.025	13.443	-0.078	-0.078	0.000	0.000	0.000	0.000
40	A	41	LEU	0	0.031	0.010	13.469	-0.110	-0.110	0.000	0.000	0.000	0.000
41	A	42	ILE	0	0.037	0.023	9.764	-0.181	-0.181	0.000	0.000	0.000	0.000
42	A	43	ASN	0	-0.023	-0.015	9.019	-0.404	-0.404	0.000	0.000	0.000	0.000
43	A	44	LEU	0	-0.031	-0.013	8.699	-0.329	-0.329	0.000	0.000	0.000	0.000
44	A	45	ALA	0	0.034	0.013	9.119	-0.236	-0.236	0.000	0.000	0.000	0.000
45	A	46	ALA	0	0.005	0.005	4.765	-0.463	-0.412	-0.001	-0.003	-0.047	0.000
46	A	47	ASN	0	-0.006	-0.006	4.625	-1.681	-1.724	-0.001	-0.010	0.053	0.000
47	A	48	THR	0	-0.080	-0.041	6.969	-0.230	-0.230	0.000	0.000	0.000	0.000
48	A	49	TYR	0	-0.098	-0.068	6.349	0.411	0.411	0.000	0.000	0.000	0.000
49	A	50	SER	0	-0.007	0.006	2.990	-0.174	0.595	0.064	-0.340	-0.492	-0.001
50	A	51	ASP	-1	-0.898	-0.933	1.753	-20.612	-23.533	10.048	-4.457	-2.670	-0.047
51	A	52	ARG	1	0.900	0.947	4.172	4.095	4.214	-0.001	-0.009	-0.109	0.000
52	A	53	LEU	0	-0.039	-0.009	3.999	1.717	1.846	-0.001	-0.022	-0.106	0.000
53	A	54	LYS	1	0.828	0.909	2.639	-6.748	-4.893	1.092	-1.261	-1.687	-0.008
54	A	55	VAL	0	-0.003	-0.006	3.636	0.167	0.198	0.005	0.085	-0.121	0.000
55	A	56	VAL	0	0.020	0.013	5.939	0.453	0.453	0.000	0.000	0.000	0.000
56	A	57	LYS	1	0.909	0.955	8.420	-0.095	-0.095	0.000	0.000	0.000	0.000
57	A	58	LEU	0	0.019	0.012	11.876	0.116	0.116	0.000	0.000	0.000	0.000
58	A	59	GLU	-1	-0.952	-0.954	15.219	0.045	0.045	0.000	0.000	0.000	0.000
59	A	60	ILE	0	0.014	-0.025	18.408	0.020	0.020	0.000	0.000	0.000	0.000
60	A	61	ASP	-1	-0.853	-0.918	21.294	0.031	0.031	0.000	0.000	0.000	0.000
61	A	62	PRO	0	-0.029	-0.012	20.528	0.002	0.002	0.000	0.000	0.000	0.000
62	A	63	ASN	0	-0.048	-0.018	18.158	0.052	0.052	0.000	0.000	0.000	0.000
63	A	64	PRO	0	0.045	0.019	21.238	-0.023	-0.023	0.000	0.000	0.000	0.000
64	A	65	THR	0	-0.002	-0.007	21.728	-0.023	-0.023	0.000	0.000	0.000	0.000
65	A	66	THR	0	-0.016	-0.045	16.218	-0.013	-0.013	0.000	0.000	0.000	0.000
66	A	67	VAL	0	-0.003	0.009	19.608	-0.032	-0.032	0.000	0.000	0.000	0.000
67	A	68	LYS	1	0.931	0.967	21.439	-0.038	-0.038	0.000	0.000	0.000	0.000
68	A	69	LYS	1	0.821	0.924	18.109	-0.033	-0.033	0.000	0.000	0.000	0.000
69	A	70	TYR	0	-0.019	-0.007	16.141	-0.007	-0.007	0.000	0.000	0.000	0.000
70	A	71	LYS	1	0.968	0.972	20.851	0.066	0.066	0.000	0.000	0.000	0.000
71	A	72	VAL	0	-0.016	0.001	19.452	-0.019	-0.019	0.000	0.000	0.000	0.000
72	A	73	GLU	-1	-0.964	-0.983	22.733	-0.058	-0.058	0.000	0.000	0.000	0.000
73	A	74	GLY	0	0.012	0.008	24.243	0.004	0.004	0.000	0.000	0.000	0.000
74	A	75	VAL	0	-0.032	0.010	20.742	-0.012	-0.012	0.000	0.000	0.000	0.000
75	A	76	PRO	0	-0.012	-0.037	18.786	0.011	0.011	0.000	0.000	0.000	0.000
76	A	77	ALA	0	0.024	0.025	18.557	-0.003	-0.003	0.000	0.000	0.000	0.000
77	A	78	LEU	0	-0.033	-0.015	13.106	-0.020	-0.020	0.000	0.000	0.000	0.000
78	A	79	ARG	1	0.829	0.918	14.554	0.255	0.255	0.000	0.000	0.000	0.000
79	A	80	LEU	0	-0.016	0.015	10.789	-0.049	-0.049	0.000	0.000	0.000	0.000
80	A	81	VAL	0	0.009	-0.004	11.998	0.060	0.060	0.000	0.000	0.000	0.000
81	A	82	LYS	1	1.016	0.998	11.758	0.291	0.291	0.000	0.000	0.000	0.000
82	A	83	GLY	0	0.043	0.045	12.898	0.017	0.017	0.000	0.000	0.000	0.000
83	A	84	GLU	-1	-0.841	-0.936	14.861	0.008	0.008	0.000	0.000	0.000	0.000
84	A	85	GLN	0	-0.044	-0.003	17.112	-0.023	-0.023	0.000	0.000	0.000	0.000
85	A	86	ILE	0	-0.004	-0.011	16.349	-0.032	-0.032	0.000	0.000	0.000	0.000
86	A	87	LEU	0	-0.073	-0.043	13.651	0.005	0.005	0.000	0.000	0.000	0.000
87	A	88	ASP	-1	-0.784	-0.876	16.891	-0.423	-0.423	0.000	0.000	0.000	0.000
88	A	89	SER	0	-0.115	-0.058	17.092	0.007	0.007	0.000	0.000	0.000	0.000
89	A	90	THR	0	0.003	-0.002	17.408	0.010	0.010	0.000	0.000	0.000	0.000
90	A	91	GLU	-1	-0.798	-0.895	19.618	-0.198	-0.198	0.000	0.000	0.000	0.000
91	A	92	GLY	0	-0.008	0.000	21.826	-0.001	-0.001	0.000	0.000	0.000	0.000
92	A	93	VAL	0	-0.037	-0.028	20.417	-0.034	-0.034	0.000	0.000	0.000	0.000
93	A	94	ILE	0	-0.007	0.004	16.663	0.013	0.013	0.000	0.000	0.000	0.000
94	A	95	SER	0	0.020	-0.004	19.379	-0.031	-0.031	0.000	0.000	0.000	0.000
95	A	96	LYS	1	0.988	0.982	15.398	0.710	0.710	0.000	0.000	0.000	0.000
96	A	97	ASP	-1	-0.868	-0.930	16.745	-0.602	-0.602	0.000	0.000	0.000	0.000
97	A	98	LYN	0	0.029	0.023	18.658	-0.044	-0.044	0.000	0.000	0.000	0.000
98	A	99	LEU	0	0.001	-0.008	12.458	-0.018	-0.018	0.000	0.000	0.000	0.000
99	A	100	LEU	0	0.022	-0.002	12.802	-0.090	-0.090	0.000	0.000	0.000	0.000
100	A	101	SER	0	0.042	0.032	14.888	-0.043	-0.043	0.000	0.000	0.000	0.000
101	A	102	PHE	0	-0.062	-0.005	13.951	0.011	0.011	0.000	0.000	0.000	0.000
102	A	103	LEU	0	-0.011	-0.020	9.790	0.008	0.008	0.000	0.000	0.000	0.000
103	A	104	ASP	-1	-0.834	-0.902	13.230	-1.123	-1.123	0.000	0.000	0.000	0.000
104	A	105	THR	0	-0.073	-0.041	14.957	0.057	0.057	0.000	0.000	0.000	0.000
105	A	106	HIS	1	0.789	0.870	14.288	0.617	0.617	0.000	0.000	0.000	0.000
106	A	107	LEU	0	-0.035	-0.010	9.028	0.008	0.008	0.000	0.000	0.000	0.000
107	A	108	ASN	0	-0.068	-0.015	12.816	-0.023	-0.023	0.000	0.000	0.000	0.000

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