FMO DATABASE

FMODB ID: YVZQ2

Calculation Name: 2O5H-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2O5H

Chain ID: A

ChEMBL ID:

UniProt ID: Q9K0R7

Base Structure: X-ray

Registration Date: 2023-09-21

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	134
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1311508.993585
FMO2-HF: Nuclear repulsion	1255670.954248
FMO2-HF: Total energy	-55838.039337
FMO2-MP2: Total energy	-56003.153201

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:-2:SER)

Summations of interaction energy for fragment #1(A:-2: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.
-3.661	-0.6	0.411	-1.255	-2.216	0.003

Interaction energy analysis for fragmet #1(A:-2:SER)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.023 / q_NPA : 0.000

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	0	ALA	0	0.035	0.008	3.795	0.088	1.243	-0.002	-0.405	-0.748	0.003
4	A	1	MET	0	0.016	0.008	5.454	0.278	0.278	0.000	0.000	0.000	0.000
5	A	2	ARG	1	0.941	0.981	3.754	-7.955	-7.352	0.011	-0.250	-0.364	0.002
6	A	3	LYS	1	0.967	0.970	2.628	-3.320	-2.738	0.363	-0.296	-0.649	0.000
7	A	4	LEU	0	-0.032	-0.015	7.336	-0.201	-0.201	0.000	0.000	0.000	0.000
8	A	5	ASN	0	-0.065	-0.055	10.409	-0.147	-0.147	0.000	0.000	0.000	0.000
9	A	6	ASN	0	0.025	0.022	10.243	-0.200	-0.200	0.000	0.000	0.000	0.000
10	A	7	HIS	0	-0.036	-0.007	11.989	-0.006	-0.006	0.000	0.000	0.000	0.000
11	A	8	ASP	-1	-0.870	-0.926	12.781	0.325	0.325	0.000	0.000	0.000	0.000
12	A	9	VAL	0	0.045	0.036	14.617	-0.045	-0.045	0.000	0.000	0.000	0.000
13	A	10	HIS	0	0.002	-0.004	10.620	-0.101	-0.101	0.000	0.000	0.000	0.000
14	A	11	LYS	1	0.929	0.958	14.178	-0.285	-0.285	0.000	0.000	0.000	0.000
15	A	12	ARG	1	0.776	0.856	17.025	-0.447	-0.447	0.000	0.000	0.000	0.000
16	A	13	TYR	0	-0.020	-0.051	16.272	-0.007	-0.007	0.000	0.000	0.000	0.000
17	A	14	GLN	0	-0.066	-0.046	14.851	-0.049	-0.049	0.000	0.000	0.000	0.000
18	A	15	ASP	-1	-0.955	-0.969	18.986	0.215	0.215	0.000	0.000	0.000	0.000
19	A	16	ARG	1	0.767	0.842	21.557	-0.324	-0.324	0.000	0.000	0.000	0.000
20	A	17	LEU	0	-0.018	0.009	16.967	0.003	0.003	0.000	0.000	0.000	0.000
21	A	18	GLU	-1	-0.779	-0.863	20.641	0.186	0.186	0.000	0.000	0.000	0.000
22	A	19	GLU	-1	-0.879	-0.920	23.358	0.179	0.179	0.000	0.000	0.000	0.000
23	A	20	ASP	-1	-0.749	-0.822	21.520	0.320	0.320	0.000	0.000	0.000	0.000
24	A	21	VAL	0	-0.046	-0.032	19.793	0.001	0.001	0.000	0.000	0.000	0.000
25	A	22	GLU	-1	-0.954	-0.974	22.408	0.129	0.129	0.000	0.000	0.000	0.000
26	A	23	PHE	0	-0.042	-0.019	25.460	-0.014	-0.014	0.000	0.000	0.000	0.000
27	A	24	THR	0	-0.043	-0.055	21.800	-0.006	-0.006	0.000	0.000	0.000	0.000
28	A	25	ILE	0	0.026	0.009	22.845	-0.009	-0.009	0.000	0.000	0.000	0.000
29	A	26	ASN	0	-0.090	-0.031	25.441	-0.021	-0.021	0.000	0.000	0.000	0.000
30	A	27	TYR	0	-0.064	-0.039	28.009	-0.012	-0.012	0.000	0.000	0.000	0.000
31	A	28	GLU	-1	-0.906	-0.942	25.703	0.112	0.112	0.000	0.000	0.000	0.000
32	A	29	LEU	0	-0.020	-0.003	24.333	0.001	0.001	0.000	0.000	0.000	0.000
33	A	30	PRO	0	0.033	0.015	23.242	0.012	0.012	0.000	0.000	0.000	0.000
34	A	31	LEU	0	0.078	0.020	16.735	0.015	0.015	0.000	0.000	0.000	0.000
35	A	32	SER	0	0.025	0.015	20.260	0.029	0.029	0.000	0.000	0.000	0.000
36	A	33	CYS	0	-0.038	-0.025	22.400	-0.003	-0.003	0.000	0.000	0.000	0.000
37	A	34	LEU	0	0.044	0.041	17.755	-0.003	-0.003	0.000	0.000	0.000	0.000
38	A	35	TRP	0	0.030	0.013	17.040	0.027	0.027	0.000	0.000	0.000	0.000
39	A	36	SER	0	-0.060	-0.049	20.544	-0.007	-0.007	0.000	0.000	0.000	0.000
40	A	37	THR	0	-0.042	-0.024	22.241	-0.019	-0.019	0.000	0.000	0.000	0.000
41	A	38	ILE	0	0.014	0.023	18.289	-0.008	-0.008	0.000	0.000	0.000	0.000
42	A	39	LYS	1	0.823	0.908	21.645	-0.313	-0.313	0.000	0.000	0.000	0.000
43	A	40	ASP	-1	-0.876	-0.913	23.722	0.278	0.278	0.000	0.000	0.000	0.000
44	A	41	PHE	0	-0.031	-0.005	18.278	-0.010	-0.010	0.000	0.000	0.000	0.000
45	A	42	SER	0	0.011	-0.032	21.198	-0.012	-0.012	0.000	0.000	0.000	0.000
46	A	43	SER	0	-0.003	-0.005	23.307	-0.005	-0.005	0.000	0.000	0.000	0.000
47	A	44	ASP	-1	-0.868	-0.938	19.107	0.525	0.525	0.000	0.000	0.000	0.000
48	A	45	PHE	0	-0.009	-0.002	17.313	0.020	0.020	0.000	0.000	0.000	0.000
49	A	46	GLU	-1	-0.836	-0.905	13.071	1.065	1.065	0.000	0.000	0.000	0.000
50	A	47	GLU	-1	-0.780	-0.869	15.096	0.552	0.552	0.000	0.000	0.000	0.000
51	A	48	LYS	1	0.762	0.884	16.812	-0.388	-0.388	0.000	0.000	0.000	0.000
52	A	49	THR	0	-0.013	-0.005	12.325	0.003	0.003	0.000	0.000	0.000	0.000
53	A	50	GLU	-1	-0.840	-0.892	10.157	2.094	2.094	0.000	0.000	0.000	0.000
54	A	51	ALA	0	0.011	0.015	13.161	0.024	0.024	0.000	0.000	0.000	0.000
55	A	52	PHE	0	-0.014	-0.005	13.520	-0.046	-0.046	0.000	0.000	0.000	0.000
56	A	53	PHE	0	0.023	-0.014	9.786	0.046	0.046	0.000	0.000	0.000	0.000
57	A	54	ILE	0	-0.059	-0.014	11.576	0.003	0.003	0.000	0.000	0.000	0.000
58	A	55	LEU	0	0.034	0.033	13.072	-0.083	-0.083	0.000	0.000	0.000	0.000
59	A	56	PHE	0	0.008	-0.002	10.582	-0.053	-0.053	0.000	0.000	0.000	0.000
60	A	57	LYS	1	0.797	0.883	7.559	-1.549	-1.549	0.000	0.000	0.000	0.000
61	A	58	GLU	-1	-0.751	-0.832	12.209	0.133	0.133	0.000	0.000	0.000	0.000
62	A	59	LEU	0	0.012	0.009	15.300	-0.072	-0.072	0.000	0.000	0.000	0.000
63	A	60	LEU	0	-0.052	-0.022	12.314	-0.051	-0.051	0.000	0.000	0.000	0.000
64	A	61	ARG	1	0.769	0.863	13.481	-0.221	-0.221	0.000	0.000	0.000	0.000
65	A	62	ARG	1	0.673	0.783	15.233	-0.235	-0.235	0.000	0.000	0.000	0.000
66	A	63	GLY	0	-0.015	0.008	18.087	-0.021	-0.021	0.000	0.000	0.000	0.000
67	A	64	HIS	0	0.049	0.025	19.844	0.005	0.005	0.000	0.000	0.000	0.000
68	A	65	LEU	0	-0.019	0.015	16.756	0.001	0.001	0.000	0.000	0.000	0.000
69	A	66	LYS	1	0.836	0.917	17.984	-0.052	-0.052	0.000	0.000	0.000	0.000
70	A	67	LEU	0	0.007	-0.002	14.221	0.023	0.023	0.000	0.000	0.000	0.000
71	A	68	GLN	0	0.012	0.011	18.222	-0.038	-0.038	0.000	0.000	0.000	0.000
72	A	69	ARG	1	0.893	0.936	19.280	-0.156	-0.156	0.000	0.000	0.000	0.000
73	A	70	ASP	-1	-0.919	-0.961	21.553	0.082	0.082	0.000	0.000	0.000	0.000
74	A	71	GLY	0	0.005	0.000	25.018	-0.013	-0.013	0.000	0.000	0.000	0.000
75	A	72	GLN	0	-0.050	-0.032	23.512	-0.021	-0.021	0.000	0.000	0.000	0.000
76	A	73	ILE	0	0.021	0.015	19.697	0.012	0.012	0.000	0.000	0.000	0.000
77	A	74	ILE	0	-0.045	-0.011	16.009	-0.025	-0.025	0.000	0.000	0.000	0.000
78	A	75	GLY	0	0.001	-0.001	16.656	0.024	0.024	0.000	0.000	0.000	0.000
79	A	76	HIS	1	0.824	0.892	11.041	0.061	0.061	0.000	0.000	0.000	0.000
80	A	77	THR	0	0.012	-0.012	9.086	0.062	0.062	0.000	0.000	0.000	0.000
81	A	78	PRO	0	0.061	0.021	9.985	0.053	0.053	0.000	0.000	0.000	0.000
82	A	79	GLU	-1	-0.890	-0.966	4.894	0.534	0.534	0.000	0.000	0.000	0.000
83	A	80	GLU	-1	-0.844	-0.884	5.417	-0.281	-0.281	0.000	0.000	0.000	0.000
84	A	81	TRP	0	0.041	0.016	7.267	0.185	0.185	0.000	0.000	0.000	0.000
85	A	82	GLU	-1	-0.764	-0.834	5.877	3.628	3.628	0.000	0.000	0.000	0.000
86	A	83	GLN	0	-0.138	-0.083	3.554	2.265	2.986	0.039	-0.304	-0.455	-0.002
87	A	84	ILE	0	-0.008	-0.002	5.892	-0.027	-0.027	0.000	0.000	0.000	0.000
88	A	85	PHE	0	0.020	-0.006	9.529	-0.039	-0.039	0.000	0.000	0.000	0.000
89	A	86	ARG	1	0.753	0.810	6.047	-2.592	-2.592	0.000	0.000	0.000	0.000
90	A	87	GLU	-1	-0.946	-0.946	6.937	0.807	0.807	0.000	0.000	0.000	0.000
91	A	88	VAL	0	-0.042	-0.017	9.881	-0.142	-0.142	0.000	0.000	0.000	0.000
92	A	89	TRP	0	-0.032	-0.002	12.307	-0.070	-0.070	0.000	0.000	0.000	0.000
93	A	90	PRO	0	0.013	0.007	14.047	-0.005	-0.005	0.000	0.000	0.000	0.000
94	A	91	GLU	-1	-0.934	-0.973	16.507	0.514	0.514	0.000	0.000	0.000	0.000
95	A	92	TYR	0	-0.048	-0.025	17.915	-0.009	-0.009	0.000	0.000	0.000	0.000
96	A	93	GLU	-1	-0.796	-0.870	20.732	0.385	0.385	0.000	0.000	0.000	0.000
97	A	94	ILE	0	-0.036	-0.040	21.781	-0.019	-0.019	0.000	0.000	0.000	0.000
98	A	95	GLU	-1	-0.909	-0.951	24.054	0.283	0.283	0.000	0.000	0.000	0.000
99	A	96	PRO	0	-0.012	-0.012	24.181	-0.026	-0.026	0.000	0.000	0.000	0.000
100	A	97	ASN	0	0.034	-0.001	27.396	-0.020	-0.020	0.000	0.000	0.000	0.000
101	A	98	PRO	0	-0.083	-0.044	30.247	-0.012	-0.012	0.000	0.000	0.000	0.000
102	A	99	LEU	0	-0.033	-0.007	30.016	-0.007	-0.007	0.000	0.000	0.000	0.000
103	A	100	PRO	0	-0.008	0.019	27.979	-0.012	-0.012	0.000	0.000	0.000	0.000
104	A	101	GLY	0	0.011	-0.007	31.118	-0.001	-0.001	0.000	0.000	0.000	0.000
105	A	102	TYR	0	-0.017	-0.010	26.642	-0.021	-0.021	0.000	0.000	0.000	0.000
106	A	103	ALA	0	0.006	0.011	30.224	0.001	0.001	0.000	0.000	0.000	0.000
107	A	104	PRO	0	-0.050	-0.011	29.799	0.012	0.012	0.000	0.000	0.000	0.000
108	A	105	PHE	0	0.051	0.017	22.953	0.002	0.002	0.000	0.000	0.000	0.000
109	A	106	ASP	-1	-0.807	-0.910	24.403	0.297	0.297	0.000	0.000	0.000	0.000
110	A	107	ILE	0	0.043	0.012	17.364	-0.007	-0.007	0.000	0.000	0.000	0.000
111	A	108	GLY	0	0.025	0.021	21.118	0.010	0.010	0.000	0.000	0.000	0.000
112	A	109	MET	0	-0.066	-0.025	23.469	-0.019	-0.019	0.000	0.000	0.000	0.000
113	A	110	TRP	0	0.043	0.024	14.720	0.015	0.015	0.000	0.000	0.000	0.000
114	A	111	LEU	0	-0.045	-0.027	16.882	-0.007	-0.007	0.000	0.000	0.000	0.000
115	A	112	THR	0	-0.088	-0.047	20.567	-0.025	-0.025	0.000	0.000	0.000	0.000
116	A	113	VAL	0	-0.060	-0.044	23.770	-0.022	-0.022	0.000	0.000	0.000	0.000
117	A	114	GLU	-1	-0.968	-0.984	21.078	0.260	0.260	0.000	0.000	0.000	0.000
118	A	115	ALA	0	0.006	0.041	17.741	0.030	0.030	0.000	0.000	0.000	0.000
119	A	116	PRO	0	-0.008	-0.014	13.610	-0.054	-0.054	0.000	0.000	0.000	0.000
120	A	117	ALA	0	-0.045	-0.012	16.299	-0.060	-0.060	0.000	0.000	0.000	0.000
121	A	118	TYR	0	-0.022	-0.011	18.034	0.038	0.038	0.000	0.000	0.000	0.000
122	A	119	ALA	0	0.013	-0.007	20.204	-0.015	-0.015	0.000	0.000	0.000	0.000
123	A	120	VAL	0	-0.045	-0.005	21.069	-0.015	-0.015	0.000	0.000	0.000	0.000
124	A	121	TRP	0	0.015	0.012	21.711	0.010	0.010	0.000	0.000	0.000	0.000
125	A	122	ILE	0	-0.053	-0.039	22.542	-0.018	-0.018	0.000	0.000	0.000	0.000
126	A	123	ASP	-1	-0.836	-0.920	25.324	0.070	0.070	0.000	0.000	0.000	0.000
127	A	124	PRO	0	-0.026	-0.036	26.796	-0.008	-0.008	0.000	0.000	0.000	0.000
128	A	125	GLU	-1	-1.021	-0.991	28.291	0.036	0.036	0.000	0.000	0.000	0.000
129	A	126	ASP	-1	-0.920	-0.978	31.945	0.009	0.009	0.000	0.000	0.000	0.000
130	A	127	GLY	0	-0.058	-0.009	28.267	-0.007	-0.007	0.000	0.000	0.000	0.000
131	A	128	SER	0	-0.057	-0.023	28.534	-0.005	-0.005	0.000	0.000	0.000	0.000
132	A	129	GLU	-1	-0.833	-0.930	25.040	0.054	0.054	0.000	0.000	0.000	0.000
133	A	130	TYR	0	-0.002	0.017	27.146	-0.010	-0.010	0.000	0.000	0.000	0.000
134	A	131	TRP	0	-0.041	-0.024	25.644	0.016	0.016	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:-2:SER)