FMO DATABASE

FMODB ID: 98VZ2

Calculation Name: 2OHW-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2OHW

Chain ID: A

ChEMBL ID:

UniProt ID: O32092

Base Structure: X-ray

Registration Date: 2023-09-23

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	128
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1184309.455412
FMO2-HF: Nuclear repulsion	1133011.072263
FMO2-HF: Total energy	-51298.38315
FMO2-MP2: Total energy	-51449.694196

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:3:GLU)

Summations of interaction energy for fragment #1(A:3: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.
-68.939	-82.066	41.188	-16.179	-11.882	0.138

Interaction energy analysis for fragmet #1(A:3:GLU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : -1 / q_Mulliken : -0.805 / q_NPA : -0.911

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	5	LYS	1	0.789	0.897	1.777	-138.328	-153.461	41.070	-15.585	-10.352	0.137
4	A	6	MET	0	-0.026	-0.012	2.948	-7.004	-5.570	0.120	-0.517	-1.038	0.001
5	A	7	ASP	-1	-0.825	-0.919	4.344	23.842	24.232	-0.001	-0.074	-0.314	0.000
6	A	8	LEU	0	-0.027	-0.012	6.091	-2.800	-2.800	0.000	0.000	0.000	0.000
7	A	9	TYR	0	-0.027	-0.026	7.590	-2.640	-2.640	0.000	0.000	0.000	0.000
8	A	10	LEU	0	0.002	-0.010	7.009	-2.502	-2.502	0.000	0.000	0.000	0.000
9	A	11	GLN	0	-0.021	0.001	10.045	-2.069	-2.069	0.000	0.000	0.000	0.000
10	A	12	GLN	0	-0.030	-0.030	12.041	-1.077	-1.077	0.000	0.000	0.000	0.000
11	A	13	GLY	0	0.004	0.005	13.755	-0.811	-0.811	0.000	0.000	0.000	0.000
12	A	14	MET	0	-0.065	-0.021	11.710	-0.512	-0.512	0.000	0.000	0.000	0.000
13	A	15	TYR	0	0.037	0.026	13.573	-0.874	-0.874	0.000	0.000	0.000	0.000
14	A	16	GLY	0	0.022	0.013	13.680	1.071	1.071	0.000	0.000	0.000	0.000
15	A	17	PRO	0	-0.031	-0.006	13.623	0.159	0.159	0.000	0.000	0.000	0.000
16	A	18	LEU	0	-0.010	-0.002	7.715	1.350	1.350	0.000	0.000	0.000	0.000
17	A	19	GLU	-1	-0.909	-0.956	4.661	61.247	61.429	-0.001	-0.003	-0.178	0.000
18	A	20	THR	0	-0.040	-0.013	8.325	-4.957	-4.957	0.000	0.000	0.000	0.000
19	A	21	LYS	1	0.965	0.956	10.610	-19.742	-19.742	0.000	0.000	0.000	0.000
20	A	22	PRO	0	0.006	-0.014	10.963	-1.011	-1.011	0.000	0.000	0.000	0.000
21	A	23	ASP	-1	-0.759	-0.864	6.899	42.377	42.377	0.000	0.000	0.000	0.000
22	A	24	GLU	-1	-0.849	-0.927	9.636	20.223	20.223	0.000	0.000	0.000	0.000
23	A	25	ARG	1	0.863	0.937	12.151	-18.341	-18.341	0.000	0.000	0.000	0.000
24	A	26	HIS	0	0.017	0.011	10.017	-2.401	-2.401	0.000	0.000	0.000	0.000
25	A	27	LEU	0	0.041	0.046	9.158	-0.544	-0.544	0.000	0.000	0.000	0.000
26	A	28	PHE	0	-0.027	-0.029	11.074	-1.583	-1.583	0.000	0.000	0.000	0.000
27	A	29	LEU	0	-0.002	-0.001	14.648	-1.143	-1.143	0.000	0.000	0.000	0.000
28	A	30	GLY	0	0.069	0.031	15.829	-1.004	-1.004	0.000	0.000	0.000	0.000
29	A	31	SER	0	-0.072	-0.037	17.500	-0.595	-0.595	0.000	0.000	0.000	0.000
30	A	32	LEU	0	-0.011	-0.012	16.205	1.054	1.054	0.000	0.000	0.000	0.000
31	A	33	ARG	1	0.887	0.936	14.555	-18.400	-18.400	0.000	0.000	0.000	0.000
32	A	34	GLU	-1	-0.878	-0.918	16.570	14.125	14.125	0.000	0.000	0.000	0.000
33	A	35	ARG	1	0.820	0.894	19.852	-14.308	-14.308	0.000	0.000	0.000	0.000
34	A	36	VAL	0	-0.029	0.007	16.943	-0.668	-0.668	0.000	0.000	0.000	0.000
35	A	37	VAL	0	-0.044	-0.016	20.303	-0.096	-0.096	0.000	0.000	0.000	0.000
36	A	38	LEU	0	-0.009	-0.018	21.215	-0.197	-0.197	0.000	0.000	0.000	0.000
37	A	39	ALA	0	-0.001	0.009	16.854	0.057	0.057	0.000	0.000	0.000	0.000
38	A	40	LEU	0	-0.022	0.005	18.884	-0.245	-0.245	0.000	0.000	0.000	0.000
39	A	41	THR	0	0.083	0.025	14.680	0.129	0.129	0.000	0.000	0.000	0.000
40	A	42	LYS	1	0.933	0.949	15.302	-15.058	-15.058	0.000	0.000	0.000	0.000
41	A	43	GLY	0	0.010	0.006	17.307	-0.612	-0.612	0.000	0.000	0.000	0.000
42	A	44	GLN	0	0.003	-0.001	19.130	-0.183	-0.183	0.000	0.000	0.000	0.000
43	A	45	VAL	0	-0.054	-0.030	20.684	-0.585	-0.585	0.000	0.000	0.000	0.000
44	A	46	LEU	0	-0.031	-0.015	20.469	-0.438	-0.438	0.000	0.000	0.000	0.000
45	A	47	ARG	1	0.861	0.951	23.786	-10.544	-10.544	0.000	0.000	0.000	0.000
46	A	48	SER	0	0.017	0.000	25.809	-0.047	-0.047	0.000	0.000	0.000	0.000
47	A	49	LYS	1	0.929	0.974	29.498	-8.467	-8.467	0.000	0.000	0.000	0.000
48	A	50	PRO	0	0.037	0.031	28.139	0.251	0.251	0.000	0.000	0.000	0.000
49	A	51	TYR	0	-0.045	-0.063	23.503	-0.263	-0.263	0.000	0.000	0.000	0.000
50	A	52	LYS	1	0.877	0.923	27.907	-8.475	-8.475	0.000	0.000	0.000	0.000
51	A	53	GLU	-1	-0.829	-0.925	26.488	10.086	10.086	0.000	0.000	0.000	0.000
52	A	54	ALA	0	0.038	0.015	25.659	0.113	0.113	0.000	0.000	0.000	0.000
53	A	55	GLU	-1	-0.799	-0.878	27.227	8.343	8.343	0.000	0.000	0.000	0.000
54	A	56	HIS	0	-0.070	-0.028	30.052	-0.471	-0.471	0.000	0.000	0.000	0.000
55	A	57	GLU	-1	-0.780	-0.897	25.814	10.549	10.549	0.000	0.000	0.000	0.000
56	A	58	LEU	0	-0.010	-0.012	27.815	-0.050	-0.050	0.000	0.000	0.000	0.000
57	A	59	LYS	1	0.896	0.966	30.517	-8.262	-8.262	0.000	0.000	0.000	0.000
58	A	60	ASN	0	-0.102	-0.055	32.210	-0.425	-0.425	0.000	0.000	0.000	0.000
59	A	61	SER	0	-0.049	-0.005	30.206	0.084	0.084	0.000	0.000	0.000	0.000
60	A	62	HIS	0	0.019	-0.004	31.137	-0.441	-0.441	0.000	0.000	0.000	0.000
61	A	63	ASN	0	-0.001	0.010	30.872	0.114	0.114	0.000	0.000	0.000	0.000
62	A	64	VAL	0	0.021	0.017	26.872	0.378	0.378	0.000	0.000	0.000	0.000
63	A	65	THR	0	-0.065	-0.036	25.616	-0.426	-0.426	0.000	0.000	0.000	0.000
64	A	66	LEU	0	-0.007	0.000	24.438	0.378	0.378	0.000	0.000	0.000	0.000
65	A	67	LEU	0	-0.039	-0.013	20.189	-0.323	-0.323	0.000	0.000	0.000	0.000
66	A	68	ILE	0	0.007	-0.006	21.880	0.158	0.158	0.000	0.000	0.000	0.000
67	A	69	ASN	0	0.040	0.017	15.816	-0.411	-0.411	0.000	0.000	0.000	0.000
68	A	70	GLY	0	0.017	-0.003	19.848	-0.461	-0.461	0.000	0.000	0.000	0.000
69	A	71	GLU	-1	-0.922	-0.958	17.053	14.851	14.851	0.000	0.000	0.000	0.000
70	A	72	LEU	0	-0.127	-0.051	20.202	-0.267	-0.267	0.000	0.000	0.000	0.000
71	A	73	GLN	0	0.089	0.056	22.350	-0.483	-0.483	0.000	0.000	0.000	0.000
72	A	74	TYR	0	0.059	0.019	26.016	-0.037	-0.037	0.000	0.000	0.000	0.000
73	A	75	GLN	0	0.011	-0.030	28.729	-0.055	-0.055	0.000	0.000	0.000	0.000
74	A	76	SER	0	-0.051	-0.014	24.684	-0.041	-0.041	0.000	0.000	0.000	0.000
75	A	77	TYR	0	0.053	0.022	24.570	0.084	0.084	0.000	0.000	0.000	0.000
76	A	78	SER	0	-0.012	0.004	26.811	-0.145	-0.145	0.000	0.000	0.000	0.000
77	A	79	SER	0	0.019	-0.004	29.964	-0.283	-0.283	0.000	0.000	0.000	0.000
78	A	80	TYR	0	0.051	0.018	25.713	-0.195	-0.195	0.000	0.000	0.000	0.000
79	A	81	ILE	0	0.018	0.028	29.012	-0.032	-0.032	0.000	0.000	0.000	0.000
80	A	82	GLN	0	-0.036	-0.016	30.962	-0.334	-0.334	0.000	0.000	0.000	0.000
81	A	83	MET	0	-0.084	-0.020	28.579	-0.191	-0.191	0.000	0.000	0.000	0.000
82	A	84	ALA	0	0.034	0.013	29.919	-0.118	-0.118	0.000	0.000	0.000	0.000
83	A	85	SER	0	0.017	0.000	31.965	-0.161	-0.161	0.000	0.000	0.000	0.000
84	A	86	ARG	1	0.839	0.932	35.258	-8.296	-8.296	0.000	0.000	0.000	0.000
85	A	87	TYR	0	-0.076	-0.070	33.695	-0.316	-0.316	0.000	0.000	0.000	0.000
86	A	88	GLY	0	0.007	0.022	35.763	0.038	0.038	0.000	0.000	0.000	0.000
87	A	89	VAL	0	-0.050	-0.011	29.295	0.118	0.118	0.000	0.000	0.000	0.000
88	A	90	PRO	0	0.000	0.010	29.995	-0.056	-0.056	0.000	0.000	0.000	0.000
89	A	91	PHE	0	0.037	-0.006	27.715	0.286	0.286	0.000	0.000	0.000	0.000
90	A	92	LYS	1	0.937	0.963	24.947	-11.489	-11.489	0.000	0.000	0.000	0.000
91	A	93	ILE	0	0.004	0.004	24.162	0.252	0.252	0.000	0.000	0.000	0.000
92	A	94	VAL	0	-0.027	-0.013	18.758	-0.213	-0.213	0.000	0.000	0.000	0.000
93	A	95	SER	0	-0.008	-0.021	20.769	0.316	0.316	0.000	0.000	0.000	0.000
94	A	96	ASP	-1	-0.939	-0.951	20.042	15.040	15.040	0.000	0.000	0.000	0.000
95	A	97	LEU	0	-0.033	-0.015	15.148	0.610	0.610	0.000	0.000	0.000	0.000
96	A	98	GLN	0	0.018	0.006	13.679	-0.474	-0.474	0.000	0.000	0.000	0.000
97	A	99	PHE	0	-0.027	-0.010	6.370	1.049	1.049	0.000	0.000	0.000	0.000
98	A	100	HIS	0	0.014	0.012	10.302	-0.924	-0.924	0.000	0.000	0.000	0.000
99	A	101	THR	0	0.028	0.004	9.663	1.545	1.545	0.000	0.000	0.000	0.000
100	A	102	PRO	0	0.026	0.021	9.391	-1.426	-1.426	0.000	0.000	0.000	0.000
101	A	103	LEU	0	-0.012	-0.007	12.277	-1.435	-1.435	0.000	0.000	0.000	0.000
102	A	104	GLY	0	-0.013	-0.025	14.995	-0.146	-0.146	0.000	0.000	0.000	0.000
103	A	105	ILE	0	-0.033	-0.018	18.515	-0.526	-0.526	0.000	0.000	0.000	0.000
104	A	106	VAL	0	0.013	0.012	16.982	0.485	0.485	0.000	0.000	0.000	0.000
105	A	107	ILE	0	-0.018	0.002	20.125	-0.476	-0.476	0.000	0.000	0.000	0.000
106	A	108	ALA	0	0.024	0.010	21.248	0.380	0.380	0.000	0.000	0.000	0.000
107	A	109	ALA	0	0.017	0.002	23.051	-0.567	-0.567	0.000	0.000	0.000	0.000
108	A	110	ASP	-1	-0.885	-0.955	24.830	10.931	10.931	0.000	0.000	0.000	0.000
109	A	111	ILE	0	-0.022	-0.015	26.766	0.103	0.103	0.000	0.000	0.000	0.000
110	A	112	ALA	0	-0.057	-0.035	23.901	0.288	0.288	0.000	0.000	0.000	0.000
111	A	113	VAL	0	-0.003	-0.007	23.624	-0.504	-0.504	0.000	0.000	0.000	0.000
112	A	114	ASN	0	-0.063	-0.031	21.561	0.535	0.535	0.000	0.000	0.000	0.000
113	A	115	ARG	1	0.944	0.972	22.133	-11.699	-11.699	0.000	0.000	0.000	0.000
114	A	116	GLU	-1	-0.909	-0.953	19.989	14.037	14.037	0.000	0.000	0.000	0.000
115	A	117	LEU	0	-0.019	-0.004	19.243	0.702	0.702	0.000	0.000	0.000	0.000
116	A	118	ILE	0	-0.018	0.000	15.891	-0.556	-0.556	0.000	0.000	0.000	0.000
117	A	119	TYR	0	0.010	0.011	17.523	0.111	0.111	0.000	0.000	0.000	0.000
118	A	120	ILE	0	0.001	-0.001	19.636	-0.490	-0.490	0.000	0.000	0.000	0.000
119	A	121	GLN	0	0.027	0.017	20.224	-0.157	-0.157	0.000	0.000	0.000	0.000
120	A	122	ASP	-1	-0.758	-0.863	20.824	11.339	11.339	0.000	0.000	0.000	0.000
121	A	123	ASP	-1	-0.856	-0.941	20.598	11.456	11.456	0.000	0.000	0.000	0.000
122	A	124	ILE	0	-0.004	-0.007	19.930	0.389	0.389	0.000	0.000	0.000	0.000
123	A	125	TYR	0	-0.027	0.007	13.574	0.297	0.297	0.000	0.000	0.000	0.000
124	A	126	ASN	0	-0.004	-0.012	15.833	1.117	1.117	0.000	0.000	0.000	0.000
125	A	127	ARG	1	0.852	0.930	15.510	-11.167	-11.167	0.000	0.000	0.000	0.000
126	A	128	SER	0	-0.074	-0.046	15.565	0.294	0.294	0.000	0.000	0.000	0.000
127	A	129	VAL	0	-0.025	0.003	11.178	0.384	0.384	0.000	0.000	0.000	0.000
128	A	130	LEU	0	-0.014	0.012	7.426	0.989	0.989	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:3:GLU)