FMO DATABASE

FMODB ID: 8278Y

Calculation Name: 1TX9-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1TX9

Chain ID: A

ChEMBL ID:

UniProt ID: P69486

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	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	141
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1289005.189441
FMO2-HF: Nuclear repulsion	1234081.146218
FMO2-HF: Total energy	-54924.043223
FMO2-MP2: Total energy	-55084.906693

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:4:VAL)

Summations of interaction energy for fragment #1(A:4:VAL)

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.
-1.222	2.114	0.217	-1.102	-2.454	0.001

Interaction energy analysis for fragmet #1(A:4:VAL)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.012 / 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

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	6	GLU	-1	-0.783	-0.882	3.897	-0.344	1.302	0.004	-0.629	-1.021	0.001
4	A	7	GLN	0	0.014	0.000	2.873	-1.463	-0.533	0.193	-0.236	-0.889	0.000
5	A	8	SER	0	-0.062	-0.036	3.202	-0.170	0.477	0.021	-0.228	-0.441	0.000
6	A	9	VAL	0	0.069	0.028	4.830	0.180	0.293	-0.001	-0.009	-0.103	0.000
7	A	10	ARG	1	0.801	0.896	7.818	-0.287	-0.287	0.000	0.000	0.000	0.000
8	A	11	PHE	0	-0.009	-0.007	7.145	0.031	0.031	0.000	0.000	0.000	0.000
9	A	12	GLN	0	0.003	0.007	8.894	0.035	0.035	0.000	0.000	0.000	0.000
10	A	13	THR	0	0.011	0.002	10.818	0.030	0.030	0.000	0.000	0.000	0.000
11	A	14	ALA	0	0.003	0.022	12.421	0.026	0.026	0.000	0.000	0.000	0.000
12	A	15	LEU	0	0.012	-0.006	11.791	0.026	0.026	0.000	0.000	0.000	0.000
13	A	16	ALA	0	-0.039	-0.016	14.569	0.022	0.022	0.000	0.000	0.000	0.000
14	A	17	SER	0	-0.032	-0.028	16.621	0.027	0.027	0.000	0.000	0.000	0.000
15	A	18	ILE	0	-0.006	0.005	17.121	0.012	0.012	0.000	0.000	0.000	0.000
16	A	19	LYS	1	0.813	0.899	19.347	0.130	0.130	0.000	0.000	0.000	0.000
17	A	20	LEU	0	-0.034	0.000	21.136	0.009	0.009	0.000	0.000	0.000	0.000
18	A	21	ILE	0	0.015	-0.003	20.665	0.005	0.005	0.000	0.000	0.000	0.000
19	A	22	GLN	0	0.046	0.021	22.881	-0.003	-0.003	0.000	0.000	0.000	0.000
20	A	23	ALA	0	-0.047	-0.001	25.356	0.003	0.003	0.000	0.000	0.000	0.000
21	A	24	SER	0	-0.063	-0.036	27.276	0.007	0.007	0.000	0.000	0.000	0.000
22	A	25	ALA	0	0.085	0.068	29.089	0.002	0.002	0.000	0.000	0.000	0.000
23	A	26	VAL	0	-0.090	-0.051	30.408	0.003	0.003	0.000	0.000	0.000	0.000
24	A	27	LEU	0	0.000	-0.010	28.674	0.002	0.002	0.000	0.000	0.000	0.000
25	A	28	ASP	-1	-0.942	-0.968	32.629	-0.010	-0.010	0.000	0.000	0.000	0.000
26	A	29	LEU	0	-0.032	-0.029	30.835	0.000	0.000	0.000	0.000	0.000	0.000
27	A	30	THR	0	-0.015	-0.004	35.547	-0.001	-0.001	0.000	0.000	0.000	0.000
28	A	31	GLU	-1	-0.788	-0.890	36.649	-0.035	-0.035	0.000	0.000	0.000	0.000
29	A	32	ASP	-1	-0.816	-0.893	36.456	-0.027	-0.027	0.000	0.000	0.000	0.000
30	A	33	ASP	-1	-0.789	-0.875	34.517	-0.020	-0.020	0.000	0.000	0.000	0.000
31	A	34	PHE	0	0.007	0.013	29.767	-0.001	-0.001	0.000	0.000	0.000	0.000
32	A	35	ASP	-1	-0.835	-0.909	31.798	-0.045	-0.045	0.000	0.000	0.000	0.000
33	A	36	PHE	0	-0.081	-0.051	31.992	-0.002	-0.002	0.000	0.000	0.000	0.000
34	A	37	LEU	0	-0.054	-0.028	27.113	-0.002	-0.002	0.000	0.000	0.000	0.000
35	A	38	THR	0	0.023	-0.006	27.726	-0.004	-0.004	0.000	0.000	0.000	0.000
36	A	39	SER	0	-0.033	0.005	28.674	-0.005	-0.005	0.000	0.000	0.000	0.000
37	A	40	ASN	0	-0.057	-0.040	28.905	0.001	0.001	0.000	0.000	0.000	0.000
38	A	41	LYS	1	0.880	0.947	29.953	0.032	0.032	0.000	0.000	0.000	0.000
39	A	42	VAL	0	0.011	0.005	29.323	0.000	0.000	0.000	0.000	0.000	0.000
40	A	43	TRP	0	-0.018	-0.023	26.455	0.005	0.005	0.000	0.000	0.000	0.000
41	A	44	ILE	0	-0.050	-0.021	31.088	0.001	0.001	0.000	0.000	0.000	0.000
42	A	45	ALA	0	-0.003	-0.017	33.405	0.001	0.001	0.000	0.000	0.000	0.000
43	A	46	THR	0	0.009	-0.007	34.368	0.002	0.002	0.000	0.000	0.000	0.000
44	A	47	ASP	-1	-0.775	-0.884	33.449	-0.023	-0.023	0.000	0.000	0.000	0.000
45	A	48	ARG	1	0.935	0.983	29.549	0.015	0.015	0.000	0.000	0.000	0.000
46	A	49	SER	0	0.032	0.006	32.285	0.001	0.001	0.000	0.000	0.000	0.000
47	A	50	ARG	1	0.794	0.887	34.499	0.025	0.025	0.000	0.000	0.000	0.000
48	A	51	ALA	0	0.014	0.004	29.375	-0.001	-0.001	0.000	0.000	0.000	0.000
49	A	52	ARG	1	0.800	0.891	27.451	-0.007	-0.007	0.000	0.000	0.000	0.000
50	A	53	ARG	1	0.879	0.922	30.076	0.015	0.015	0.000	0.000	0.000	0.000
51	A	54	CYS	0	-0.028	-0.011	31.056	0.000	0.000	0.000	0.000	0.000	0.000
52	A	55	VAL	0	0.039	0.015	24.688	-0.003	-0.003	0.000	0.000	0.000	0.000
53	A	56	GLU	-1	-0.816	-0.895	26.689	0.004	0.004	0.000	0.000	0.000	0.000
54	A	57	ALA	0	0.010	0.015	28.381	0.001	0.001	0.000	0.000	0.000	0.000
55	A	58	CYS	0	-0.021	0.003	25.934	-0.002	-0.002	0.000	0.000	0.000	0.000
56	A	59	VAL	0	-0.054	-0.029	23.083	-0.002	-0.002	0.000	0.000	0.000	0.000
57	A	60	TYR	0	-0.008	-0.015	25.326	0.005	0.005	0.000	0.000	0.000	0.000
58	A	61	GLY	0	0.045	0.034	28.179	0.002	0.002	0.000	0.000	0.000	0.000
59	A	62	THR	0	-0.002	-0.016	29.939	0.001	0.001	0.000	0.000	0.000	0.000
60	A	63	LEU	0	-0.065	-0.022	29.480	0.002	0.002	0.000	0.000	0.000	0.000
61	A	64	ASP	-1	-0.730	-0.847	32.461	0.000	0.000	0.000	0.000	0.000	0.000
62	A	65	PHE	0	-0.027	-0.016	34.213	0.000	0.000	0.000	0.000	0.000	0.000
63	A	66	VAL	0	-0.046	-0.020	36.228	0.000	0.000	0.000	0.000	0.000	0.000
64	A	67	GLY	0	0.007	0.015	37.286	0.001	0.001	0.000	0.000	0.000	0.000
65	A	68	TYR	0	-0.063	-0.022	35.043	0.003	0.003	0.000	0.000	0.000	0.000
66	A	69	PRO	0	-0.020	-0.021	34.497	0.000	0.000	0.000	0.000	0.000	0.000
67	A	70	ARG	1	0.778	0.856	30.235	-0.004	-0.004	0.000	0.000	0.000	0.000
68	A	71	PHE	0	-0.031	-0.017	26.033	0.004	0.004	0.000	0.000	0.000	0.000
69	A	72	PRO	0	0.004	-0.008	24.005	-0.005	-0.005	0.000	0.000	0.000	0.000
70	A	73	ALA	0	0.041	0.036	22.351	0.003	0.003	0.000	0.000	0.000	0.000
71	A	74	PRO	0	0.031	0.005	17.423	0.004	0.004	0.000	0.000	0.000	0.000
72	A	75	VAL	0	0.006	-0.004	14.534	-0.024	-0.024	0.000	0.000	0.000	0.000
73	A	76	GLU	-1	-0.813	-0.890	12.577	0.043	0.043	0.000	0.000	0.000	0.000
74	A	77	PHE	0	0.032	0.019	15.019	-0.029	-0.029	0.000	0.000	0.000	0.000
75	A	78	ILE	0	0.020	0.007	18.590	-0.012	-0.012	0.000	0.000	0.000	0.000
76	A	79	ALA	0	-0.025	-0.026	14.529	-0.010	-0.010	0.000	0.000	0.000	0.000
77	A	80	ALA	0	0.005	0.006	16.602	-0.018	-0.018	0.000	0.000	0.000	0.000
78	A	81	VAL	0	0.026	0.011	17.636	-0.005	-0.005	0.000	0.000	0.000	0.000
79	A	82	ILE	0	-0.071	-0.050	18.640	-0.002	-0.002	0.000	0.000	0.000	0.000
80	A	83	ALA	0	-0.025	-0.019	16.160	-0.004	-0.004	0.000	0.000	0.000	0.000
81	A	84	TYR	0	-0.074	-0.044	18.242	-0.012	-0.012	0.000	0.000	0.000	0.000
82	A	85	TYR	0	-0.012	-0.032	21.212	0.001	0.001	0.000	0.000	0.000	0.000
83	A	86	VAL	0	-0.029	-0.001	22.582	0.004	0.004	0.000	0.000	0.000	0.000
84	A	87	HIS	0	0.082	0.050	22.758	-0.012	-0.012	0.000	0.000	0.000	0.000
85	A	88	PRO	0	0.000	-0.032	20.738	0.005	0.005	0.000	0.000	0.000	0.000
86	A	89	VAL	0	-0.051	-0.017	22.229	0.001	0.001	0.000	0.000	0.000	0.000
87	A	90	ASN	0	0.035	0.024	24.958	0.009	0.009	0.000	0.000	0.000	0.000
88	A	91	ILE	0	0.023	0.029	18.411	0.007	0.007	0.000	0.000	0.000	0.000
89	A	92	GLN	0	-0.004	0.007	20.509	0.013	0.013	0.000	0.000	0.000	0.000
90	A	93	THR	0	-0.053	-0.040	21.503	0.012	0.012	0.000	0.000	0.000	0.000
91	A	94	ALA	0	0.052	0.025	22.484	0.008	0.008	0.000	0.000	0.000	0.000
92	A	95	CYS	0	-0.066	-0.008	18.724	0.001	0.001	0.000	0.000	0.000	0.000
93	A	96	LEU	0	-0.018	-0.017	20.818	0.011	0.011	0.000	0.000	0.000	0.000
94	A	97	ILE	0	-0.056	-0.018	23.581	0.008	0.008	0.000	0.000	0.000	0.000
95	A	98	MET	0	-0.015	-0.005	21.819	0.005	0.005	0.000	0.000	0.000	0.000
96	A	99	GLU	-1	-0.819	-0.881	20.651	0.048	0.048	0.000	0.000	0.000	0.000
97	A	100	GLY	0	-0.072	-0.037	20.450	-0.001	-0.001	0.000	0.000	0.000	0.000
98	A	101	ALA	0	0.056	0.040	19.949	0.010	0.010	0.000	0.000	0.000	0.000
99	A	102	GLU	-1	-0.805	-0.906	17.352	0.173	0.173	0.000	0.000	0.000	0.000
100	A	103	PHE	0	0.008	-0.008	11.962	-0.022	-0.022	0.000	0.000	0.000	0.000
101	A	104	THR	0	0.006	-0.036	14.478	0.015	0.015	0.000	0.000	0.000	0.000
102	A	105	GLU	-1	-0.820	-0.891	10.852	0.431	0.431	0.000	0.000	0.000	0.000
103	A	106	ASN	0	-0.057	-0.033	14.612	0.017	0.017	0.000	0.000	0.000	0.000
104	A	107	ILE	0	0.019	0.015	17.034	-0.016	-0.016	0.000	0.000	0.000	0.000
105	A	108	ILE	0	-0.052	-0.019	17.435	-0.012	-0.012	0.000	0.000	0.000	0.000
106	A	109	ASN	0	-0.042	-0.036	16.110	-0.025	-0.025	0.000	0.000	0.000	0.000
107	A	110	GLY	0	0.032	0.029	20.260	-0.002	-0.002	0.000	0.000	0.000	0.000
108	A	111	VAL	0	-0.073	-0.023	18.153	-0.006	-0.006	0.000	0.000	0.000	0.000
109	A	112	GLU	-1	-0.920	-0.955	18.762	0.144	0.144	0.000	0.000	0.000	0.000
110	A	113	ARG	1	0.717	0.819	12.241	-0.268	-0.268	0.000	0.000	0.000	0.000
111	A	114	PRO	0	0.005	0.004	17.250	-0.002	-0.002	0.000	0.000	0.000	0.000
112	A	115	VAL	0	-0.024	-0.001	14.773	0.006	0.006	0.000	0.000	0.000	0.000
113	A	116	LYS	1	0.893	0.934	17.257	-0.085	-0.085	0.000	0.000	0.000	0.000
114	A	117	ALA	0	0.038	-0.002	17.526	-0.005	-0.005	0.000	0.000	0.000	0.000
115	A	118	ALA	0	-0.032	-0.005	16.937	-0.017	-0.017	0.000	0.000	0.000	0.000
116	A	119	GLU	-1	-0.794	-0.866	11.410	0.196	0.196	0.000	0.000	0.000	0.000
117	A	120	LEU	0	0.033	0.014	13.114	-0.032	-0.032	0.000	0.000	0.000	0.000
118	A	121	PHE	0	0.045	0.004	14.702	-0.032	-0.032	0.000	0.000	0.000	0.000
119	A	122	ALA	0	-0.025	-0.010	11.680	-0.029	-0.029	0.000	0.000	0.000	0.000
120	A	123	PHE	0	-0.052	-0.018	8.334	-0.054	-0.054	0.000	0.000	0.000	0.000
121	A	124	THR	0	0.054	-0.002	11.353	-0.046	-0.046	0.000	0.000	0.000	0.000
122	A	125	LEU	0	0.006	0.005	13.551	-0.017	-0.017	0.000	0.000	0.000	0.000
123	A	126	ARG	1	0.825	0.914	5.814	0.426	0.426	0.000	0.000	0.000	0.000
124	A	127	VAL	0	0.020	0.008	10.538	-0.050	-0.050	0.000	0.000	0.000	0.000
125	A	128	ARG	1	0.912	0.957	12.211	0.121	0.121	0.000	0.000	0.000	0.000
126	A	129	ALA	0	-0.065	-0.029	12.058	0.008	0.008	0.000	0.000	0.000	0.000
127	A	130	GLY	0	-0.030	-0.006	11.539	-0.019	-0.019	0.000	0.000	0.000	0.000
128	A	131	ASN	0	-0.008	-0.033	12.572	-0.010	-0.010	0.000	0.000	0.000	0.000
129	A	132	THR	0	0.039	0.013	15.592	0.011	0.011	0.000	0.000	0.000	0.000
130	A	133	ASP	-1	-0.940	-0.934	18.489	-0.153	-0.153	0.000	0.000	0.000	0.000
131	A	134	VAL	0	-0.036	-0.031	18.005	0.013	0.013	0.000	0.000	0.000	0.000
132	A	135	LEU	0	-0.001	0.001	20.805	-0.007	-0.007	0.000	0.000	0.000	0.000
133	A	136	THR	0	0.002	0.012	23.824	0.002	0.002	0.000	0.000	0.000	0.000
134	A	137	ASP	-1	-0.904	-0.946	26.899	-0.082	-0.082	0.000	0.000	0.000	0.000
135	A	138	ALA	0	-0.003	-0.023	30.154	0.003	0.003	0.000	0.000	0.000	0.000
136	A	139	GLU	-1	-0.948	-0.974	32.689	-0.039	-0.039	0.000	0.000	0.000	0.000
137	A	140	GLU	-1	-0.763	-0.850	28.376	-0.057	-0.057	0.000	0.000	0.000	0.000
138	A	141	ASN	0	-0.094	-0.042	32.631	0.000	0.000	0.000	0.000	0.000	0.000
139	A	142	VAL	0	0.013	0.005	35.007	0.003	0.003	0.000	0.000	0.000	0.000
140	A	143	ARG	1	0.808	0.906	34.355	0.027	0.027	0.000	0.000	0.000	0.000
141	A	144	GLN	0	0.009	0.018	37.252	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:4:VAL)