FMO DATABASE

FMODB ID: M31YZ

Calculation Name: 1OFT-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1OFT

Chain ID: A

ChEMBL ID:

UniProt ID: Q9HZJ8

Base Structure: X-ray

Registration Date: 2023-06-20

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	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	119
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-955043.01645
FMO2-HF: Nuclear repulsion	910110.659575
FMO2-HF: Total energy	-44932.356875
FMO2-MP2: Total energy	-45065.880382

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:43:PRO)

Summations of interaction energy for fragment #1(A:43:PRO)

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.
-10.331	-2.318	2.955	-4.135	-6.83	-0.017

Interaction energy analysis for fragmet #1(A:43:PRO)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.073 / q_NPA : -0.039

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	45	ALA	0	0.038	0.032	3.374	-2.859	0.031	0.013	-1.516	-1.387	0.001
4	A	46	PHE	0	0.010	-0.003	2.182	-1.527	-0.098	1.454	-0.848	-2.035	-0.007
5	A	47	SER	0	0.008	0.006	4.297	0.719	0.717	-0.001	-0.024	0.028	0.000
6	A	48	GLU	-1	-0.853	-0.919	6.442	0.205	0.205	0.000	0.000	0.000	0.000
7	A	49	LEU	0	0.018	0.021	8.130	0.017	0.017	0.000	0.000	0.000	0.000
8	A	50	SER	0	-0.026	-0.018	11.607	0.003	0.003	0.000	0.000	0.000	0.000
9	A	51	LEU	0	-0.018	-0.006	13.873	-0.009	-0.009	0.000	0.000	0.000	0.000
10	A	52	SER	0	0.010	0.009	17.635	0.002	0.002	0.000	0.000	0.000	0.000
11	A	53	GLY	0	0.071	0.022	20.293	-0.004	-0.004	0.000	0.000	0.000	0.000
12	A	54	LEU	0	0.019	-0.003	24.020	0.001	0.001	0.000	0.000	0.000	0.000
13	A	55	PRO	0	0.059	0.040	24.320	0.000	0.000	0.000	0.000	0.000	0.000
14	A	56	GLY	0	0.016	0.001	24.955	-0.002	-0.002	0.000	0.000	0.000	0.000
15	A	57	HIS	0	0.048	0.003	25.013	-0.004	-0.004	0.000	0.000	0.000	0.000
16	A	58	CYS	0	-0.021	0.002	21.006	0.001	0.001	0.000	0.000	0.000	0.000
17	A	59	LEU	0	0.019	0.004	21.756	-0.002	-0.002	0.000	0.000	0.000	0.000
18	A	60	THR	0	-0.036	-0.012	23.608	-0.006	-0.006	0.000	0.000	0.000	0.000
19	A	61	LEU	0	0.020	-0.006	20.771	-0.004	-0.004	0.000	0.000	0.000	0.000
20	A	62	LEU	0	-0.034	0.001	17.762	-0.002	-0.002	0.000	0.000	0.000	0.000
21	A	63	ALA	0	-0.021	-0.009	20.581	-0.008	-0.008	0.000	0.000	0.000	0.000
22	A	64	PRO	0	-0.032	-0.002	21.954	-0.006	-0.006	0.000	0.000	0.000	0.000
23	A	65	ILE	0	0.060	0.041	16.152	-0.004	-0.004	0.000	0.000	0.000	0.000
24	A	66	LEU	0	-0.026	-0.022	17.678	-0.010	-0.010	0.000	0.000	0.000	0.000
25	A	67	ARG	1	0.910	0.923	19.958	0.016	0.016	0.000	0.000	0.000	0.000
26	A	68	GLU	-1	-0.832	-0.917	20.433	-0.045	-0.045	0.000	0.000	0.000	0.000
27	A	69	LEU	0	-0.043	-0.020	15.303	-0.007	-0.007	0.000	0.000	0.000	0.000
28	A	70	SER	0	-0.080	-0.054	19.472	-0.005	-0.005	0.000	0.000	0.000	0.000
29	A	71	GLU	-1	-1.032	-1.006	22.259	-0.044	-0.044	0.000	0.000	0.000	0.000
30	A	72	GLU	-1	-0.842	-0.919	18.570	-0.134	-0.134	0.000	0.000	0.000	0.000
31	A	73	GLN	0	-0.008	-0.002	22.213	0.008	0.008	0.000	0.000	0.000	0.000
32	A	74	ASP	-1	-0.817	-0.922	18.551	-0.154	-0.154	0.000	0.000	0.000	0.000
33	A	75	ALA	0	-0.036	-0.025	21.779	0.004	0.004	0.000	0.000	0.000	0.000
34	A	76	ARG	1	0.718	0.876	15.310	0.207	0.207	0.000	0.000	0.000	0.000
35	A	77	TRP	0	-0.008	-0.004	20.064	0.007	0.007	0.000	0.000	0.000	0.000
36	A	78	LEU	0	0.033	0.066	16.875	-0.018	-0.018	0.000	0.000	0.000	0.000
37	A	79	THR	0	-0.052	-0.046	16.436	0.011	0.011	0.000	0.000	0.000	0.000
38	A	80	LEU	0	-0.018	-0.011	16.350	-0.007	-0.007	0.000	0.000	0.000	0.000
39	A	81	ILE	0	-0.003	0.000	14.937	0.003	0.003	0.000	0.000	0.000	0.000
40	A	82	ALA	0	-0.028	-0.009	16.879	0.008	0.008	0.000	0.000	0.000	0.000
41	A	83	PRO	0	-0.020	0.005	19.080	0.007	0.007	0.000	0.000	0.000	0.000
42	A	84	PRO	0	0.031	0.004	19.401	0.001	0.001	0.000	0.000	0.000	0.000
43	A	85	ALA	0	0.039	0.005	22.239	-0.004	-0.004	0.000	0.000	0.000	0.000
44	A	86	SER	0	-0.029	-0.011	24.317	-0.002	-0.002	0.000	0.000	0.000	0.000
45	A	87	LEU	0	0.009	0.017	20.987	-0.003	-0.003	0.000	0.000	0.000	0.000
46	A	88	THR	0	0.003	0.019	25.186	-0.002	-0.002	0.000	0.000	0.000	0.000
47	A	89	HIS	0	0.051	0.005	28.241	-0.002	-0.002	0.000	0.000	0.000	0.000
48	A	90	GLU	-1	-0.956	-0.996	30.098	-0.005	-0.005	0.000	0.000	0.000	0.000
49	A	91	TRP	0	0.019	0.004	23.020	-0.002	-0.002	0.000	0.000	0.000	0.000
50	A	92	LEU	0	0.062	0.024	24.449	-0.001	-0.001	0.000	0.000	0.000	0.000
51	A	93	ARG	1	0.951	0.989	27.439	0.007	0.007	0.000	0.000	0.000	0.000
52	A	94	ARG	1	0.902	0.947	30.584	0.004	0.004	0.000	0.000	0.000	0.000
53	A	95	ALA	0	-0.058	-0.014	26.324	0.000	0.000	0.000	0.000	0.000	0.000
54	A	96	GLY	0	0.014	0.002	27.369	-0.002	-0.002	0.000	0.000	0.000	0.000
55	A	97	LEU	0	-0.015	0.028	23.040	-0.003	-0.003	0.000	0.000	0.000	0.000
56	A	98	ASN	0	0.105	0.054	25.699	0.006	0.006	0.000	0.000	0.000	0.000
57	A	99	ARG	1	0.909	0.919	26.081	0.018	0.018	0.000	0.000	0.000	0.000
58	A	100	GLU	-1	-0.942	-0.943	27.652	-0.035	-0.035	0.000	0.000	0.000	0.000
59	A	101	ARG	1	0.846	0.922	22.599	0.076	0.076	0.000	0.000	0.000	0.000
60	A	102	ILE	0	-0.004	-0.006	21.569	-0.006	-0.006	0.000	0.000	0.000	0.000
61	A	103	LEU	0	-0.015	0.010	20.911	0.005	0.005	0.000	0.000	0.000	0.000
62	A	104	LEU	0	-0.009	-0.007	20.824	-0.003	-0.003	0.000	0.000	0.000	0.000
63	A	105	LEU	0	0.007	0.010	19.494	0.004	0.004	0.000	0.000	0.000	0.000
64	A	106	GLN	0	0.067	0.017	21.172	0.005	0.005	0.000	0.000	0.000	0.000
65	A	107	ALA	0	-0.016	-0.012	19.712	-0.002	-0.002	0.000	0.000	0.000	0.000
66	A	108	LYS	1	0.942	0.967	21.675	-0.007	-0.007	0.000	0.000	0.000	0.000
67	A	109	ASP	-1	-0.813	-0.903	19.984	0.052	0.052	0.000	0.000	0.000	0.000
68	A	110	ASN	0	0.017	0.020	14.740	-0.011	-0.011	0.000	0.000	0.000	0.000
69	A	111	ALA	0	0.032	-0.002	15.533	0.011	0.011	0.000	0.000	0.000	0.000
70	A	112	ALA	0	0.007	0.000	16.199	-0.006	-0.006	0.000	0.000	0.000	0.000
71	A	113	ALA	0	0.033	0.017	15.820	-0.011	-0.011	0.000	0.000	0.000	0.000
72	A	114	LEU	0	-0.018	0.009	9.732	-0.010	-0.010	0.000	0.000	0.000	0.000
73	A	115	ALA	0	-0.010	-0.002	12.755	-0.017	-0.017	0.000	0.000	0.000	0.000
74	A	116	LEU	0	0.071	0.021	15.371	-0.018	-0.018	0.000	0.000	0.000	0.000
75	A	117	SER	0	-0.012	-0.035	11.766	-0.017	-0.017	0.000	0.000	0.000	0.000
76	A	118	CYS	0	-0.048	-0.017	10.649	-0.046	-0.046	0.000	0.000	0.000	0.000
77	A	119	GLU	-1	-0.981	-0.988	12.532	-0.068	-0.068	0.000	0.000	0.000	0.000
78	A	120	ALA	0	0.005	-0.007	14.913	-0.014	-0.014	0.000	0.000	0.000	0.000
79	A	121	LEU	0	-0.045	-0.019	9.026	-0.016	-0.016	0.000	0.000	0.000	0.000
80	A	122	ARG	1	1.002	1.013	12.771	0.086	0.086	0.000	0.000	0.000	0.000
81	A	123	LEU	0	-0.084	-0.031	14.081	-0.002	-0.002	0.000	0.000	0.000	0.000
82	A	124	GLY	0	0.062	0.019	15.402	0.009	0.009	0.000	0.000	0.000	0.000
83	A	125	ARG	1	0.895	0.962	16.216	0.093	0.093	0.000	0.000	0.000	0.000
84	A	126	SER	0	-0.010	-0.014	15.992	0.020	0.020	0.000	0.000	0.000	0.000
85	A	127	HIS	0	0.082	0.053	15.589	-0.044	-0.044	0.000	0.000	0.000	0.000
86	A	128	THR	0	-0.005	-0.013	12.459	-0.048	-0.048	0.000	0.000	0.000	0.000
87	A	129	VAL	0	-0.063	-0.032	11.988	0.031	0.031	0.000	0.000	0.000	0.000
88	A	130	VAL	0	-0.012	-0.011	11.592	-0.016	-0.016	0.000	0.000	0.000	0.000
89	A	131	SER	0	-0.061	-0.025	10.917	0.000	0.000	0.000	0.000	0.000	0.000
90	A	132	TRP	0	0.048	0.019	12.896	0.014	0.014	0.000	0.000	0.000	0.000
91	A	133	LEU	0	-0.033	-0.016	10.983	0.004	0.004	0.000	0.000	0.000	0.000
92	A	134	GLU	-1	-0.899	-0.930	12.104	0.139	0.139	0.000	0.000	0.000	0.000
93	A	135	PRO	0	0.029	-0.006	13.307	-0.011	-0.011	0.000	0.000	0.000	0.000
94	A	136	LEU	0	0.009	0.008	6.972	0.000	0.000	0.000	0.000	0.000	0.000
95	A	137	SER	0	0.053	0.029	8.771	0.089	0.089	0.000	0.000	0.000	0.000
96	A	138	ARG	1	1.036	0.998	4.823	-1.073	-1.073	0.000	0.000	0.000	0.000
97	A	139	ALA	0	-0.029	-0.021	5.078	0.140	0.233	-0.001	-0.001	-0.090	0.000
98	A	140	ALA	0	0.061	0.020	6.355	0.001	0.001	0.000	0.000	0.000	0.000
99	A	141	ARG	1	0.893	0.961	2.763	-1.464	-0.695	0.252	-0.210	-0.811	0.000
100	A	142	LYS	1	0.931	0.975	3.314	-2.114	-1.204	0.052	-0.253	-0.710	-0.001
101	A	143	GLN	0	-0.025	-0.010	4.008	-0.373	-0.335	0.001	-0.005	-0.034	0.000
102	A	144	LEU	0	0.066	0.024	5.614	-0.088	-0.088	0.000	0.000	0.000	0.000
103	A	145	SER	0	-0.043	-0.037	2.441	-2.144	-0.322	1.186	-1.258	-1.749	-0.010
104	A	146	ARG	1	0.960	0.969	4.360	0.090	0.154	-0.001	-0.020	-0.042	0.000
105	A	147	ALA	0	-0.032	-0.014	6.954	0.022	0.022	0.000	0.000	0.000	0.000
106	A	148	ALA	0	0.041	0.009	6.829	0.037	0.037	0.000	0.000	0.000	0.000
107	A	149	GLN	0	-0.047	-0.022	4.900	0.161	0.161	0.000	0.000	0.000	0.000
108	A	150	LEU	0	-0.080	-0.030	9.009	0.079	0.079	0.000	0.000	0.000	0.000
109	A	151	GLY	0	0.009	0.019	11.996	0.034	0.034	0.000	0.000	0.000	0.000
110	A	152	GLN	0	-0.016	0.000	12.417	0.024	0.024	0.000	0.000	0.000	0.000
111	A	153	ALA	0	0.019	0.013	11.283	0.047	0.047	0.000	0.000	0.000	0.000
112	A	154	GLN	0	0.053	0.024	8.559	-0.233	-0.233	0.000	0.000	0.000	0.000
113	A	155	SER	0	-0.039	-0.021	6.266	0.118	0.118	0.000	0.000	0.000	0.000
114	A	156	LEU	0	0.014	0.006	7.285	-0.014	-0.014	0.000	0.000	0.000	0.000
115	A	157	ASN	0	-0.032	-0.025	8.525	-0.024	-0.024	0.000	0.000	0.000	0.000
116	A	158	ILE	0	0.019	-0.009	10.076	0.039	0.039	0.000	0.000	0.000	0.000
117	A	159	ARG	1	0.895	0.966	10.496	-0.195	-0.195	0.000	0.000	0.000	0.000
118	A	160	LEU	0	0.002	-0.009	14.252	-0.002	-0.002	0.000	0.000	0.000	0.000
119	A	161	GLY	0	0.015	0.021	17.885	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:43:PRO)