FMO DATABASE

FMODB ID: 526LZ

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	OptHSide
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	-851615.458984
FMO2-HF: Nuclear repulsion	809797.148929
FMO2-HF: Total energy	-41818.310055
FMO2-MP2: Total energy	-41941.091585

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.
-29.8	-24.875	9.373	-7.045	-7.251	-0.045

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 : -0.016 / 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	0.026	-0.001	3.184	-2.610	-0.768	0.037	-0.862	-1.017	0.004
4	A	4	VAL	0	-0.025	-0.005	3.643	-1.148	-0.638	0.013	-0.181	-0.341	-0.001
5	A	5	ILE	0	-0.006	0.013	4.716	0.394	0.451	-0.001	-0.005	-0.051	0.000
6	A	6	THR	0	-0.062	-0.042	7.275	-0.314	-0.314	0.000	0.000	0.000	0.000
7	A	7	ILE	0	0.002	0.004	9.948	0.113	0.113	0.000	0.000	0.000	0.000
8	A	8	THR	0	-0.020	-0.044	12.683	-0.102	-0.102	0.000	0.000	0.000	0.000
9	A	9	ASP	-1	-0.732	-0.854	15.816	0.112	0.112	0.000	0.000	0.000	0.000
10	A	10	ALA	0	-0.055	-0.020	18.002	0.001	0.001	0.000	0.000	0.000	0.000
11	A	11	GLU	-1	-0.795	-0.873	13.280	0.465	0.465	0.000	0.000	0.000	0.000
12	A	12	PHE	0	0.016	0.007	13.285	0.051	0.051	0.000	0.000	0.000	0.000
13	A	13	GLU	-1	-0.830	-0.911	13.358	0.272	0.272	0.000	0.000	0.000	0.000
14	A	14	SER	0	0.043	0.010	13.025	-0.032	-0.032	0.000	0.000	0.000	0.000
15	A	15	GLU	-1	-0.853	-0.906	8.081	1.448	1.448	0.000	0.000	0.000	0.000
16	A	16	VAL	0	-0.005	-0.005	8.513	0.041	0.041	0.000	0.000	0.000	0.000
17	A	17	LEU	0	-0.067	-0.023	10.665	-0.028	-0.028	0.000	0.000	0.000	0.000
18	A	18	LYS	1	0.833	0.896	13.006	-0.337	-0.337	0.000	0.000	0.000	0.000
19	A	19	ALA	0	-0.047	0.007	7.540	0.111	0.111	0.000	0.000	0.000	0.000
20	A	20	GLU	-1	-0.910	-0.959	8.508	0.291	0.291	0.000	0.000	0.000	0.000
21	A	21	GLN	0	-0.062	-0.030	2.849	-3.634	-2.485	0.140	-0.586	-0.704	0.007
22	A	22	PRO	0	-0.021	-0.009	8.131	0.104	0.104	0.000	0.000	0.000	0.000
23	A	23	VAL	0	0.009	-0.001	6.884	-0.210	-0.210	0.000	0.000	0.000	0.000
24	A	24	LEU	0	-0.001	0.006	7.693	0.084	0.084	0.000	0.000	0.000	0.000
25	A	25	VAL	0	0.004	-0.001	9.147	0.004	0.004	0.000	0.000	0.000	0.000
26	A	26	TYR	0	-0.034	-0.026	11.687	-0.006	-0.006	0.000	0.000	0.000	0.000
27	A	27	PHE	0	0.021	0.001	13.593	0.075	0.075	0.000	0.000	0.000	0.000
28	A	28	TRP	0	0.000	-0.024	14.962	-0.039	-0.039	0.000	0.000	0.000	0.000
29	A	29	ALA	0	0.075	0.025	18.847	0.030	0.030	0.000	0.000	0.000	0.000
30	A	30	SER	0	0.005	-0.006	21.637	-0.021	-0.021	0.000	0.000	0.000	0.000
31	A	31	TRP	0	-0.060	-0.033	23.065	-0.018	-0.018	0.000	0.000	0.000	0.000
32	A	32	CYS	0	-0.007	0.024	19.494	-0.054	-0.054	0.000	0.000	0.000	0.000
33	A	33	GLY	0	0.058	0.029	23.377	-0.012	-0.012	0.000	0.000	0.000	0.000
34	A	34	PRO	0	0.027	-0.007	23.615	-0.014	-0.014	0.000	0.000	0.000	0.000
35	A	36	GLN	0	-0.031	-0.018	18.974	-0.028	-0.028	0.000	0.000	0.000	0.000
36	A	37	LEU	0	-0.014	-0.007	19.772	-0.018	-0.018	0.000	0.000	0.000	0.000
37	A	38	MET	0	0.024	0.037	16.080	-0.049	-0.049	0.000	0.000	0.000	0.000
38	A	39	SER	0	0.008	0.007	14.011	-0.063	-0.063	0.000	0.000	0.000	0.000
39	A	40	PRO	0	-0.029	-0.020	13.465	-0.084	-0.084	0.000	0.000	0.000	0.000
40	A	41	LEU	0	0.020	0.016	13.493	-0.112	-0.112	0.000	0.000	0.000	0.000
41	A	42	ILE	0	0.041	0.022	9.818	-0.179	-0.179	0.000	0.000	0.000	0.000
42	A	43	ASN	0	-0.002	-0.003	8.884	-0.442	-0.442	0.000	0.000	0.000	0.000
43	A	44	LEU	0	-0.010	0.001	8.735	-0.354	-0.354	0.000	0.000	0.000	0.000
44	A	45	ALA	0	0.038	0.026	9.162	-0.230	-0.230	0.000	0.000	0.000	0.000
45	A	46	ALA	0	0.005	0.003	4.763	-0.436	-0.386	-0.001	-0.003	-0.046	0.000
46	A	47	ASN	0	-0.046	-0.036	4.699	-1.403	-1.421	-0.001	-0.008	0.028	0.000
47	A	48	THR	0	-0.065	-0.042	7.046	-0.146	-0.146	0.000	0.000	0.000	0.000
48	A	49	TYR	0	-0.094	-0.069	6.501	0.412	0.412	0.000	0.000	0.000	0.000
49	A	50	SER	0	0.002	-0.002	3.096	-0.144	0.580	0.042	-0.305	-0.461	-0.001
50	A	51	ASP	-1	-0.919	-0.943	1.809	-20.160	-21.802	8.021	-3.819	-2.560	-0.045
51	A	52	ARG	1	0.885	0.946	4.223	3.886	4.002	-0.001	-0.007	-0.108	0.000
52	A	53	LEU	0	-0.007	0.006	3.966	1.685	1.811	-0.001	-0.023	-0.101	0.000
53	A	54	LYS	1	0.809	0.900	2.668	-6.894	-4.922	1.120	-1.325	-1.767	-0.009
54	A	55	VAL	0	0.000	-0.005	3.660	0.280	0.319	0.005	0.079	-0.123	0.000
55	A	56	VAL	0	0.018	0.010	5.881	0.402	0.402	0.000	0.000	0.000	0.000
56	A	57	LYS	1	0.895	0.952	8.389	-0.017	-0.017	0.000	0.000	0.000	0.000
57	A	58	LEU	0	0.014	0.013	11.901	0.111	0.111	0.000	0.000	0.000	0.000
58	A	59	GLU	-1	-0.887	-0.922	15.241	-0.010	-0.010	0.000	0.000	0.000	0.000
59	A	60	ILE	0	0.022	-0.023	18.427	0.020	0.020	0.000	0.000	0.000	0.000
60	A	61	ASP	-1	-0.859	-0.908	21.288	0.006	0.006	0.000	0.000	0.000	0.000
61	A	62	PRO	0	-0.013	-0.009	20.789	0.004	0.004	0.000	0.000	0.000	0.000
62	A	63	ASN	0	-0.049	-0.014	18.114	0.052	0.052	0.000	0.000	0.000	0.000
63	A	64	PRO	0	0.053	0.018	21.182	-0.021	-0.021	0.000	0.000	0.000	0.000
64	A	65	THR	0	-0.047	-0.039	21.510	-0.020	-0.020	0.000	0.000	0.000	0.000
65	A	66	THR	0	-0.026	-0.050	16.145	-0.013	-0.013	0.000	0.000	0.000	0.000
66	A	67	VAL	0	-0.007	0.006	19.564	-0.030	-0.030	0.000	0.000	0.000	0.000
67	A	68	LYS	1	0.936	0.966	21.407	-0.026	-0.026	0.000	0.000	0.000	0.000
68	A	69	LYS	1	0.784	0.893	18.176	-0.016	-0.016	0.000	0.000	0.000	0.000
69	A	70	TYR	0	-0.008	-0.008	16.416	-0.007	-0.007	0.000	0.000	0.000	0.000
70	A	71	LYS	1	0.855	0.912	20.836	0.071	0.071	0.000	0.000	0.000	0.000
71	A	72	VAL	0	0.003	0.009	19.393	-0.018	-0.018	0.000	0.000	0.000	0.000
72	A	73	GLU	-1	-0.891	-0.939	22.725	-0.071	-0.071	0.000	0.000	0.000	0.000
73	A	74	GLY	0	0.011	0.009	24.242	0.005	0.005	0.000	0.000	0.000	0.000
74	A	75	VAL	0	-0.022	0.015	20.624	-0.014	-0.014	0.000	0.000	0.000	0.000
75	A	76	PRO	0	-0.009	-0.034	18.752	0.012	0.012	0.000	0.000	0.000	0.000
76	A	77	ALA	0	0.013	0.020	18.518	0.000	0.000	0.000	0.000	0.000	0.000
77	A	78	LEU	0	-0.039	-0.016	13.255	-0.028	-0.028	0.000	0.000	0.000	0.000
78	A	79	ARG	1	0.800	0.881	14.508	0.280	0.280	0.000	0.000	0.000	0.000
79	A	80	LEU	0	-0.017	0.014	10.758	-0.056	-0.056	0.000	0.000	0.000	0.000
80	A	81	VAL	0	0.017	-0.002	12.123	0.066	0.066	0.000	0.000	0.000	0.000
81	A	82	LYS	1	1.025	1.003	11.776	0.232	0.232	0.000	0.000	0.000	0.000
82	A	83	GLY	0	0.039	0.044	12.887	0.018	0.018	0.000	0.000	0.000	0.000
83	A	84	GLU	-1	-0.805	-0.908	14.844	-0.010	-0.010	0.000	0.000	0.000	0.000
84	A	85	GLN	0	-0.058	-0.006	17.114	-0.023	-0.023	0.000	0.000	0.000	0.000
85	A	86	ILE	0	0.009	-0.005	16.360	-0.033	-0.033	0.000	0.000	0.000	0.000
86	A	87	LEU	0	-0.074	-0.042	13.576	0.006	0.006	0.000	0.000	0.000	0.000
87	A	88	ASP	-1	-0.787	-0.879	16.848	-0.421	-0.421	0.000	0.000	0.000	0.000
88	A	89	SER	0	-0.104	-0.051	17.056	0.004	0.004	0.000	0.000	0.000	0.000
89	A	90	THR	0	0.032	0.009	17.341	0.003	0.003	0.000	0.000	0.000	0.000
90	A	91	GLU	-1	-0.787	-0.869	19.586	-0.223	-0.223	0.000	0.000	0.000	0.000
91	A	92	GLY	0	-0.007	0.001	21.807	0.000	0.000	0.000	0.000	0.000	0.000
92	A	93	VAL	0	-0.038	-0.040	20.413	-0.035	-0.035	0.000	0.000	0.000	0.000
93	A	94	ILE	0	-0.010	0.003	16.622	0.016	0.016	0.000	0.000	0.000	0.000
94	A	95	SER	0	0.031	-0.021	19.395	-0.028	-0.028	0.000	0.000	0.000	0.000
95	A	96	LYS	1	0.988	0.980	15.522	0.694	0.694	0.000	0.000	0.000	0.000
96	A	97	ASP	-1	-0.875	-0.943	16.789	-0.601	-0.601	0.000	0.000	0.000	0.000
97	A	98	LYN	0	0.044	0.058	18.702	-0.045	-0.045	0.000	0.000	0.000	0.000
98	A	99	LEU	0	0.015	0.000	12.276	-0.018	-0.018	0.000	0.000	0.000	0.000
99	A	100	LEU	0	0.010	-0.003	13.190	-0.087	-0.087	0.000	0.000	0.000	0.000
100	A	101	SER	0	0.021	0.015	14.934	-0.040	-0.040	0.000	0.000	0.000	0.000
101	A	102	PHE	0	-0.055	-0.004	13.902	0.011	0.011	0.000	0.000	0.000	0.000
102	A	103	LEU	0	-0.009	-0.016	9.710	0.010	0.010	0.000	0.000	0.000	0.000
103	A	104	ASP	-1	-0.833	-0.905	13.255	-1.117	-1.117	0.000	0.000	0.000	0.000
104	A	105	THR	0	-0.076	-0.041	15.001	0.061	0.061	0.000	0.000	0.000	0.000
105	A	106	HIS	1	0.797	0.871	14.428	0.593	0.593	0.000	0.000	0.000	0.000
106	A	107	LEU	0	-0.040	-0.009	9.240	0.013	0.013	0.000	0.000	0.000	0.000
107	A	108	ASN	0	-0.073	-0.016	12.796	0.000	0.000	0.000	0.000	0.000	0.000

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