FMO DATABASE

FMODB ID: V5ZR1

Calculation Name: 1OHQ-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1OHQ

Chain ID: A

ChEMBL ID:

UniProt ID: P01764

Base Structure: X-ray

Registration Date: 2023-06-26

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	119
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-932148.885224
FMO2-HF: Nuclear repulsion	886715.225271
FMO2-HF: Total energy	-45433.659952
FMO2-MP2: Total energy	-45565.393136

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:GLU)

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

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.
59.704	62.158	0.021	-0.96	-1.514	0

Interaction energy analysis for fragmet #1(A:1:GLU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : -1 / q_Mulliken : -0.957 / q_NPA : -0.981

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

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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	GLN	0	-0.018	-0.007	3.350	2.757	4.750	0.018	-0.771	-1.240	0.001
4	A	4	LEU	0	-0.009	-0.015	5.423	-2.903	-2.903	0.000	0.000	0.000	0.000
5	A	5	LEU	0	-0.004	0.009	9.178	-0.282	-0.282	0.000	0.000	0.000	0.000
6	A	6	GLU	-1	-0.815	-0.894	11.283	16.918	16.918	0.000	0.000	0.000	0.000
7	A	7	SER	0	0.001	-0.001	14.908	-0.173	-0.173	0.000	0.000	0.000	0.000
8	A	8	GLY	0	0.004	0.007	18.044	-0.311	-0.311	0.000	0.000	0.000	0.000
9	A	9	GLY	0	0.032	-0.003	21.425	0.282	0.282	0.000	0.000	0.000	0.000
10	A	10	GLY	0	0.009	0.008	23.623	-0.024	-0.024	0.000	0.000	0.000	0.000
11	A	11	LEU	0	-0.034	-0.017	26.250	-0.070	-0.070	0.000	0.000	0.000	0.000
12	A	12	VAL	0	-0.014	0.002	29.859	-0.150	-0.150	0.000	0.000	0.000	0.000
13	A	13	GLN	0	0.026	0.006	32.392	-0.162	-0.162	0.000	0.000	0.000	0.000
14	A	14	PRO	0	-0.006	-0.023	35.141	0.152	0.152	0.000	0.000	0.000	0.000
15	A	15	GLY	0	-0.021	0.001	36.178	-0.186	-0.186	0.000	0.000	0.000	0.000
16	A	16	GLY	0	-0.017	0.005	34.314	-0.025	-0.025	0.000	0.000	0.000	0.000
17	A	17	SER	0	-0.052	-0.043	30.723	0.074	0.074	0.000	0.000	0.000	0.000
18	A	18	LEU	0	0.017	0.013	25.932	0.087	0.087	0.000	0.000	0.000	0.000
19	A	19	ARG	1	0.932	0.984	23.256	-12.722	-12.722	0.000	0.000	0.000	0.000
20	A	20	LEU	0	0.004	0.015	19.867	0.125	0.125	0.000	0.000	0.000	0.000
21	A	21	SER	0	-0.017	-0.021	18.094	-0.432	-0.432	0.000	0.000	0.000	0.000
22	A	22	CYS	0	-0.061	-0.025	13.574	0.052	0.052	0.000	0.000	0.000	0.000
23	A	23	ALA	0	-0.001	0.012	12.811	-0.274	-0.274	0.000	0.000	0.000	0.000
24	A	24	ALA	0	0.042	0.035	9.761	1.550	1.550	0.000	0.000	0.000	0.000
25	A	25	SER	0	-0.003	-0.002	5.386	-1.430	-1.430	0.000	0.000	0.000	0.000
26	A	26	GLY	0	0.046	0.030	4.416	2.689	2.685	-0.001	-0.046	0.052	0.000
27	A	27	PHE	0	0.022	0.004	5.363	-1.531	-1.404	-0.001	-0.007	-0.119	0.000
28	A	28	ARG	1	0.890	0.963	8.054	-21.662	-21.662	0.000	0.000	0.000	0.000
29	A	29	ILE	0	0.028	0.009	11.850	-0.492	-0.492	0.000	0.000	0.000	0.000
30	A	30	SER	0	-0.100	-0.053	13.766	-0.613	-0.613	0.000	0.000	0.000	0.000
31	A	31	ASP	-1	-0.907	-0.956	13.171	17.216	17.216	0.000	0.000	0.000	0.000
32	A	32	GLU	-1	-0.849	-0.923	10.946	20.775	20.775	0.000	0.000	0.000	0.000
33	A	33	ASP	-1	-0.918	-0.953	14.610	13.519	13.519	0.000	0.000	0.000	0.000
34	A	34	MET	0	-0.037	-0.010	12.389	0.880	0.880	0.000	0.000	0.000	0.000
35	A	35	GLY	0	-0.004	-0.029	16.604	-1.173	-1.173	0.000	0.000	0.000	0.000
36	A	36	TRP	0	-0.031	-0.007	17.481	0.800	0.800	0.000	0.000	0.000	0.000
37	A	37	VAL	0	0.023	0.011	18.583	-0.733	-0.733	0.000	0.000	0.000	0.000
38	A	38	ARG	1	0.808	0.924	20.254	-10.225	-10.225	0.000	0.000	0.000	0.000
39	A	39	GLN	0	0.052	0.024	21.291	0.118	0.118	0.000	0.000	0.000	0.000
40	A	40	ALA	0	0.009	0.002	23.777	-0.012	-0.012	0.000	0.000	0.000	0.000
41	A	41	PRO	0	0.002	0.005	27.123	0.033	0.033	0.000	0.000	0.000	0.000
42	A	42	GLY	0	-0.004	-0.017	28.776	-0.294	-0.294	0.000	0.000	0.000	0.000
43	A	43	LYS	1	0.925	0.958	29.378	-9.696	-9.696	0.000	0.000	0.000	0.000
44	A	44	GLY	0	-0.020	0.013	26.657	0.064	0.064	0.000	0.000	0.000	0.000
45	A	45	LEU	0	0.041	0.003	20.294	0.248	0.248	0.000	0.000	0.000	0.000
46	A	46	GLU	-1	-0.883	-0.940	23.841	9.936	9.936	0.000	0.000	0.000	0.000
47	A	47	TRP	0	0.018	0.018	16.991	0.110	0.110	0.000	0.000	0.000	0.000
48	A	48	VAL	0	-0.022	-0.001	23.020	-0.504	-0.504	0.000	0.000	0.000	0.000
49	A	49	SER	0	-0.043	-0.054	23.260	-0.390	-0.390	0.000	0.000	0.000	0.000
50	A	50	SER	0	0.033	0.011	20.735	0.398	0.398	0.000	0.000	0.000	0.000
51	A	51	ILE	0	-0.027	-0.012	19.563	-0.635	-0.635	0.000	0.000	0.000	0.000
52	A	52	TYR	0	0.021	0.009	19.782	0.467	0.467	0.000	0.000	0.000	0.000
53	A	53	GLY	0	0.101	0.061	18.665	-0.475	-0.475	0.000	0.000	0.000	0.000
54	A	54	PRO	0	-0.018	0.002	19.605	-0.151	-0.151	0.000	0.000	0.000	0.000
55	A	55	SER	0	-0.010	-0.025	22.259	-0.058	-0.058	0.000	0.000	0.000	0.000
56	A	56	GLY	0	0.005	0.020	23.133	-0.192	-0.192	0.000	0.000	0.000	0.000
57	A	57	SER	0	-0.035	-0.022	24.143	-0.235	-0.235	0.000	0.000	0.000	0.000
58	A	58	THR	0	0.007	-0.013	24.842	0.272	0.272	0.000	0.000	0.000	0.000
59	A	59	TYR	0	-0.019	0.015	25.087	-0.565	-0.565	0.000	0.000	0.000	0.000
60	A	60	TYR	0	-0.004	-0.007	26.287	0.378	0.378	0.000	0.000	0.000	0.000
61	A	61	ALA	0	0.087	0.054	28.097	-0.306	-0.306	0.000	0.000	0.000	0.000
62	A	62	ASP	-1	-0.840	-0.932	29.677	8.634	8.634	0.000	0.000	0.000	0.000
63	A	63	SER	0	-0.011	0.000	31.387	-0.114	-0.114	0.000	0.000	0.000	0.000
64	A	64	VAL	0	-0.034	-0.022	28.220	-0.168	-0.168	0.000	0.000	0.000	0.000
65	A	65	LYS	1	0.869	0.938	31.580	-9.029	-9.029	0.000	0.000	0.000	0.000
66	A	66	GLY	0	-0.011	0.000	32.980	-0.262	-0.262	0.000	0.000	0.000	0.000
67	A	67	ARG	1	0.731	0.878	32.128	-9.261	-9.261	0.000	0.000	0.000	0.000
68	A	68	PHE	0	0.017	-0.005	26.675	0.143	0.143	0.000	0.000	0.000	0.000
69	A	69	THR	0	-0.042	-0.020	27.668	-0.268	-0.268	0.000	0.000	0.000	0.000
70	A	70	ILE	0	-0.004	0.020	20.436	0.266	0.266	0.000	0.000	0.000	0.000
71	A	71	SER	0	-0.024	-0.020	22.652	-0.211	-0.211	0.000	0.000	0.000	0.000
72	A	72	ARG	1	0.937	0.968	17.968	-13.850	-13.850	0.000	0.000	0.000	0.000
73	A	73	ASP	-1	-0.835	-0.882	19.526	13.224	13.224	0.000	0.000	0.000	0.000
74	A	74	ASN	0	0.073	0.008	17.789	1.099	1.099	0.000	0.000	0.000	0.000
75	A	75	SER	0	-0.093	-0.063	17.288	0.820	0.820	0.000	0.000	0.000	0.000
76	A	76	LYS	1	0.954	0.976	17.113	-13.339	-13.339	0.000	0.000	0.000	0.000
77	A	77	ASN	0	-0.054	-0.038	10.651	-0.415	-0.415	0.000	0.000	0.000	0.000
78	A	78	THR	0	-0.015	-0.009	13.870	1.122	1.122	0.000	0.000	0.000	0.000
79	A	79	LEU	0	0.008	0.008	16.039	-1.008	-1.008	0.000	0.000	0.000	0.000
80	A	80	TYR	0	-0.026	-0.029	17.818	0.237	0.237	0.000	0.000	0.000	0.000
81	A	81	LEU	0	0.043	0.013	20.790	-0.215	-0.215	0.000	0.000	0.000	0.000
82	A	82	GLN	0	-0.034	-0.021	23.205	0.219	0.219	0.000	0.000	0.000	0.000
83	A	83	MET	0	-0.021	0.007	24.013	-0.330	-0.330	0.000	0.000	0.000	0.000
84	A	84	ASN	0	0.091	0.027	28.364	0.026	0.026	0.000	0.000	0.000	0.000
85	A	85	SER	0	0.001	-0.011	32.096	-0.103	-0.103	0.000	0.000	0.000	0.000
86	A	86	LEU	0	-0.026	0.017	28.887	-0.108	-0.108	0.000	0.000	0.000	0.000
87	A	87	ARG	1	0.904	0.937	32.966	-8.760	-8.760	0.000	0.000	0.000	0.000
88	A	88	ALA	0	0.059	0.020	32.979	0.247	0.247	0.000	0.000	0.000	0.000
89	A	89	GLU	-1	-0.905	-0.945	33.123	8.907	8.907	0.000	0.000	0.000	0.000
90	A	90	ASP	-1	-0.766	-0.886	29.108	9.828	9.828	0.000	0.000	0.000	0.000
91	A	91	THR	0	-0.032	-0.014	27.984	0.455	0.455	0.000	0.000	0.000	0.000
92	A	92	ALA	0	-0.020	-0.002	25.049	-0.153	-0.153	0.000	0.000	0.000	0.000
93	A	93	VAL	0	0.003	0.009	19.541	0.021	0.021	0.000	0.000	0.000	0.000
94	A	94	TYR	0	-0.049	-0.051	20.567	-0.111	-0.111	0.000	0.000	0.000	0.000
95	A	95	TYR	0	0.031	0.029	14.993	0.338	0.338	0.000	0.000	0.000	0.000
96	A	97	ALA	0	0.019	-0.003	13.408	0.863	0.863	0.000	0.000	0.000	0.000
97	A	98	SER	0	0.062	0.031	11.270	-0.426	-0.426	0.000	0.000	0.000	0.000
98	A	99	ALA	0	-0.002	0.004	13.392	-0.684	-0.684	0.000	0.000	0.000	0.000
99	A	100	LEU	0	-0.023	-0.027	14.289	0.768	0.768	0.000	0.000	0.000	0.000
100	A	101	GLU	-1	-0.953	-0.977	14.918	15.261	15.261	0.000	0.000	0.000	0.000
101	A	102	PRO	0	-0.079	-0.020	10.566	-0.613	-0.613	0.000	0.000	0.000	0.000
102	A	103	LEU	0	-0.004	0.011	12.447	-0.435	-0.435	0.000	0.000	0.000	0.000
103	A	104	SER	0	-0.055	-0.032	8.608	-0.498	-0.498	0.000	0.000	0.000	0.000
104	A	105	GLU	-1	-0.904	-0.959	3.787	38.971	39.309	0.005	-0.136	-0.207	-0.001
105	A	106	PRO	0	-0.028	-0.012	7.973	-1.850	-1.850	0.000	0.000	0.000	0.000
106	A	107	LEU	0	-0.010	-0.009	9.510	-1.862	-1.862	0.000	0.000	0.000	0.000
107	A	108	GLY	0	0.042	0.022	9.358	1.339	1.339	0.000	0.000	0.000	0.000
108	A	109	PHE	0	-0.011	-0.005	7.328	1.182	1.182	0.000	0.000	0.000	0.000
109	A	110	TRP	0	-0.016	-0.025	9.403	-2.236	-2.236	0.000	0.000	0.000	0.000
110	A	111	GLY	0	0.016	0.015	9.632	2.056	2.056	0.000	0.000	0.000	0.000
111	A	112	GLN	0	-0.010	-0.025	11.541	0.947	0.947	0.000	0.000	0.000	0.000
112	A	113	GLY	0	-0.009	0.010	13.103	-0.833	-0.833	0.000	0.000	0.000	0.000
113	A	114	THR	0	-0.051	-0.052	16.684	-0.079	-0.079	0.000	0.000	0.000	0.000
114	A	115	LEU	0	-0.045	-0.023	19.343	-0.447	-0.447	0.000	0.000	0.000	0.000
115	A	116	VAL	0	0.012	0.016	22.929	-0.136	-0.136	0.000	0.000	0.000	0.000
116	A	117	THR	0	-0.037	-0.038	25.583	-0.151	-0.151	0.000	0.000	0.000	0.000
117	A	118	VAL	0	0.009	0.019	29.172	-0.067	-0.067	0.000	0.000	0.000	0.000
118	A	119	SER	0	0.011	-0.005	32.497	-0.091	-0.091	0.000	0.000	0.000	0.000
119	A	120	SER	0	-0.001	0.007	35.704	0.030	0.030	0.000	0.000	0.000	0.000

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