FMO DATABASE

FMODB ID: 76VQK

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1189944.813142
FMO2-HF: Nuclear repulsion	1138645.68331
FMO2-HF: Total energy	-51299.129832
FMO2-MP2: Total energy	-51450.425607

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.
-71.198	-70.094	20.1	-10.498	-10.707	0.117

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 : -0.816 / q_NPA : -0.902

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	5	LYS	1	0.765	0.865	1.805	-141.659	-142.866	19.944	-9.751	-8.986	0.117
4	A	6	MET	0	-0.001	0.006	2.921	-8.080	-6.457	0.157	-0.599	-1.181	0.000
5	A	7	ASP	-1	-0.854	-0.939	4.167	23.532	24.032	0.000	-0.136	-0.364	0.000
6	A	8	LEU	0	-0.010	-0.009	6.062	-3.223	-3.223	0.000	0.000	0.000	0.000
7	A	9	TYR	0	-0.002	-0.009	7.601	-2.704	-2.704	0.000	0.000	0.000	0.000
8	A	10	LEU	0	0.009	-0.008	6.459	-2.869	-2.869	0.000	0.000	0.000	0.000
9	A	11	GLN	0	-0.031	-0.003	9.893	-2.491	-2.491	0.000	0.000	0.000	0.000
10	A	12	GLN	0	0.003	-0.004	11.923	-1.032	-1.032	0.000	0.000	0.000	0.000
11	A	13	GLY	0	0.003	-0.015	13.307	-1.399	-1.399	0.000	0.000	0.000	0.000
12	A	14	MET	0	-0.058	-0.015	11.457	-0.548	-0.548	0.000	0.000	0.000	0.000
13	A	15	TYR	0	0.029	0.031	13.238	-0.834	-0.834	0.000	0.000	0.000	0.000
14	A	16	GLY	0	0.041	0.027	13.933	1.072	1.072	0.000	0.000	0.000	0.000
15	A	17	PRO	0	-0.029	-0.018	13.897	0.177	0.177	0.000	0.000	0.000	0.000
16	A	18	LEU	0	0.022	0.009	7.603	1.121	1.121	0.000	0.000	0.000	0.000
17	A	19	GLU	-1	-0.858	-0.921	4.647	67.989	68.177	-0.001	-0.012	-0.176	0.000
18	A	20	THR	0	-0.036	-0.045	8.202	-4.536	-4.536	0.000	0.000	0.000	0.000
19	A	21	LYS	1	0.846	0.889	10.434	-20.131	-20.131	0.000	0.000	0.000	0.000
20	A	22	PRO	0	-0.009	-0.015	10.920	-1.077	-1.077	0.000	0.000	0.000	0.000
21	A	23	ASP	-1	-0.773	-0.847	7.154	40.393	40.393	0.000	0.000	0.000	0.000
22	A	24	GLU	-1	-0.793	-0.889	9.560	19.915	19.915	0.000	0.000	0.000	0.000
23	A	25	ARG	1	0.866	0.936	12.612	-18.372	-18.372	0.000	0.000	0.000	0.000
24	A	26	HIS	0	0.015	0.016	10.019	-2.256	-2.256	0.000	0.000	0.000	0.000
25	A	27	LEU	0	0.042	0.041	9.113	-0.905	-0.905	0.000	0.000	0.000	0.000
26	A	28	PHE	0	-0.011	-0.019	11.240	-1.742	-1.742	0.000	0.000	0.000	0.000
27	A	29	LEU	0	0.001	0.003	14.849	-1.193	-1.193	0.000	0.000	0.000	0.000
28	A	30	GLY	0	0.066	0.029	16.151	-1.033	-1.033	0.000	0.000	0.000	0.000
29	A	31	SER	0	-0.075	-0.042	17.996	-0.655	-0.655	0.000	0.000	0.000	0.000
30	A	32	LEU	0	-0.028	-0.006	16.384	0.976	0.976	0.000	0.000	0.000	0.000
31	A	33	ARG	1	0.822	0.891	14.259	-19.296	-19.296	0.000	0.000	0.000	0.000
32	A	34	GLU	-1	-0.836	-0.913	16.495	15.608	15.608	0.000	0.000	0.000	0.000
33	A	35	ARG	1	0.797	0.888	19.797	-14.471	-14.471	0.000	0.000	0.000	0.000
34	A	36	VAL	0	-0.012	0.015	17.014	-0.687	-0.687	0.000	0.000	0.000	0.000
35	A	37	VAL	0	-0.031	-0.013	20.473	-0.148	-0.148	0.000	0.000	0.000	0.000
36	A	38	LEU	0	-0.009	-0.014	21.209	-0.228	-0.228	0.000	0.000	0.000	0.000
37	A	39	ALA	0	-0.006	0.006	16.695	-0.006	-0.006	0.000	0.000	0.000	0.000
38	A	40	LEU	0	-0.002	0.003	18.455	-0.345	-0.345	0.000	0.000	0.000	0.000
39	A	41	THR	0	0.068	0.021	14.982	0.163	0.163	0.000	0.000	0.000	0.000
40	A	42	LYS	1	0.861	0.903	14.902	-16.169	-16.169	0.000	0.000	0.000	0.000
41	A	43	GLY	0	0.004	0.006	17.521	-0.644	-0.644	0.000	0.000	0.000	0.000
42	A	44	GLN	0	-0.012	-0.014	19.083	-0.180	-0.180	0.000	0.000	0.000	0.000
43	A	45	VAL	0	-0.036	-0.017	20.395	-0.598	-0.598	0.000	0.000	0.000	0.000
44	A	46	LEU	0	-0.017	-0.012	20.786	-0.549	-0.549	0.000	0.000	0.000	0.000
45	A	47	ARG	1	0.841	0.948	23.999	-10.887	-10.887	0.000	0.000	0.000	0.000
46	A	48	SER	0	-0.001	-0.015	25.891	-0.137	-0.137	0.000	0.000	0.000	0.000
47	A	49	LYS	1	0.929	0.975	29.224	-8.667	-8.667	0.000	0.000	0.000	0.000
48	A	50	PRO	0	0.046	0.034	27.752	0.205	0.205	0.000	0.000	0.000	0.000
49	A	51	TYR	0	-0.052	-0.060	23.299	-0.228	-0.228	0.000	0.000	0.000	0.000
50	A	52	LYS	1	0.863	0.922	27.498	-8.536	-8.536	0.000	0.000	0.000	0.000
51	A	53	GLU	-1	-0.812	-0.925	26.468	10.298	10.298	0.000	0.000	0.000	0.000
52	A	54	ALA	0	0.055	0.016	25.167	0.105	0.105	0.000	0.000	0.000	0.000
53	A	55	GLU	-1	-0.797	-0.862	26.920	8.462	8.462	0.000	0.000	0.000	0.000
54	A	56	HIS	0	-0.049	-0.034	30.151	-0.502	-0.502	0.000	0.000	0.000	0.000
55	A	57	GLU	-1	-0.777	-0.867	25.987	10.621	10.621	0.000	0.000	0.000	0.000
56	A	58	LEU	0	-0.016	-0.003	27.765	-0.001	-0.001	0.000	0.000	0.000	0.000
57	A	59	LYS	1	0.856	0.925	30.516	-8.588	-8.588	0.000	0.000	0.000	0.000
58	A	60	ASN	0	-0.069	-0.021	32.126	-0.600	-0.600	0.000	0.000	0.000	0.000
59	A	61	SER	0	-0.022	0.002	30.446	0.145	0.145	0.000	0.000	0.000	0.000
60	A	62	HIS	0	0.031	0.004	30.904	-0.548	-0.548	0.000	0.000	0.000	0.000
61	A	63	ASN	0	-0.072	-0.038	30.560	0.121	0.121	0.000	0.000	0.000	0.000
62	A	64	VAL	0	0.020	0.015	26.952	0.368	0.368	0.000	0.000	0.000	0.000
63	A	65	THR	0	-0.060	-0.031	25.536	-0.389	-0.389	0.000	0.000	0.000	0.000
64	A	66	LEU	0	0.006	0.010	24.040	0.413	0.413	0.000	0.000	0.000	0.000
65	A	67	LEU	0	-0.036	-0.009	20.131	-0.356	-0.356	0.000	0.000	0.000	0.000
66	A	68	ILE	0	-0.006	-0.015	21.597	0.101	0.101	0.000	0.000	0.000	0.000
67	A	69	ASN	0	0.031	0.008	15.656	-0.505	-0.505	0.000	0.000	0.000	0.000
68	A	70	GLY	0	0.015	-0.002	19.416	-0.533	-0.533	0.000	0.000	0.000	0.000
69	A	71	GLU	-1	-0.814	-0.874	16.367	15.403	15.403	0.000	0.000	0.000	0.000
70	A	72	LEU	0	-0.079	-0.027	19.834	-0.351	-0.351	0.000	0.000	0.000	0.000
71	A	73	GLN	0	0.053	0.030	22.579	-0.474	-0.474	0.000	0.000	0.000	0.000
72	A	74	TYR	0	0.057	0.018	26.336	-0.055	-0.055	0.000	0.000	0.000	0.000
73	A	75	GLN	0	0.038	-0.006	28.847	-0.035	-0.035	0.000	0.000	0.000	0.000
74	A	76	SER	0	-0.012	0.002	24.823	-0.133	-0.133	0.000	0.000	0.000	0.000
75	A	77	TYR	0	0.064	0.024	24.273	-0.014	-0.014	0.000	0.000	0.000	0.000
76	A	78	SER	0	-0.053	-0.013	26.836	-0.159	-0.159	0.000	0.000	0.000	0.000
77	A	79	SER	0	0.010	-0.006	30.138	-0.234	-0.234	0.000	0.000	0.000	0.000
78	A	80	TYR	0	0.057	0.015	25.417	-0.150	-0.150	0.000	0.000	0.000	0.000
79	A	81	ILE	0	0.018	0.024	28.544	-0.027	-0.027	0.000	0.000	0.000	0.000
80	A	82	GLN	0	-0.029	-0.003	30.614	-0.301	-0.301	0.000	0.000	0.000	0.000
81	A	83	MET	0	-0.097	-0.040	28.473	-0.204	-0.204	0.000	0.000	0.000	0.000
82	A	84	ALA	0	0.023	0.011	29.589	-0.085	-0.085	0.000	0.000	0.000	0.000
83	A	85	SER	0	0.008	-0.015	31.654	-0.163	-0.163	0.000	0.000	0.000	0.000
84	A	86	ARG	1	0.810	0.914	34.984	-8.505	-8.505	0.000	0.000	0.000	0.000
85	A	87	TYR	0	-0.054	-0.056	33.690	-0.302	-0.302	0.000	0.000	0.000	0.000
86	A	88	GLY	0	0.011	0.019	35.767	0.050	0.050	0.000	0.000	0.000	0.000
87	A	89	VAL	0	-0.041	-0.004	29.277	0.124	0.124	0.000	0.000	0.000	0.000
88	A	90	PRO	0	0.002	0.012	30.140	-0.045	-0.045	0.000	0.000	0.000	0.000
89	A	91	PHE	0	0.026	-0.010	27.556	0.332	0.332	0.000	0.000	0.000	0.000
90	A	92	LYS	1	0.914	0.946	24.819	-11.633	-11.633	0.000	0.000	0.000	0.000
91	A	93	ILE	0	0.003	0.007	24.010	0.375	0.375	0.000	0.000	0.000	0.000
92	A	94	VAL	0	-0.017	-0.005	18.954	-0.263	-0.263	0.000	0.000	0.000	0.000
93	A	95	SER	0	0.005	-0.012	20.295	0.439	0.439	0.000	0.000	0.000	0.000
94	A	96	ASP	-1	-0.943	-0.957	19.617	15.543	15.543	0.000	0.000	0.000	0.000
95	A	97	LEU	0	-0.042	-0.021	15.369	0.543	0.543	0.000	0.000	0.000	0.000
96	A	98	GLN	0	0.017	-0.001	14.368	1.212	1.212	0.000	0.000	0.000	0.000
97	A	99	PHE	0	-0.005	0.004	5.885	1.068	1.068	0.000	0.000	0.000	0.000
98	A	100	HIS	0	-0.056	-0.036	10.160	-0.550	-0.550	0.000	0.000	0.000	0.000
99	A	101	THR	0	0.012	-0.002	9.536	1.206	1.206	0.000	0.000	0.000	0.000
100	A	102	PRO	0	0.043	0.026	9.152	-1.570	-1.570	0.000	0.000	0.000	0.000
101	A	103	LEU	0	-0.023	-0.011	12.043	-1.512	-1.512	0.000	0.000	0.000	0.000
102	A	104	GLY	0	0.002	-0.018	14.669	-0.161	-0.161	0.000	0.000	0.000	0.000
103	A	105	ILE	0	-0.051	-0.028	18.203	-0.608	-0.608	0.000	0.000	0.000	0.000
104	A	106	VAL	0	0.008	0.006	16.725	0.534	0.534	0.000	0.000	0.000	0.000
105	A	107	ILE	0	-0.019	0.010	19.966	-0.402	-0.402	0.000	0.000	0.000	0.000
106	A	108	ALA	0	0.038	0.014	21.233	0.427	0.427	0.000	0.000	0.000	0.000
107	A	109	ALA	0	0.027	0.011	23.218	-0.575	-0.575	0.000	0.000	0.000	0.000
108	A	110	ASP	-1	-0.801	-0.903	25.093	11.100	11.100	0.000	0.000	0.000	0.000
109	A	111	ILE	0	-0.025	-0.003	26.656	0.318	0.318	0.000	0.000	0.000	0.000
110	A	112	ALA	0	-0.015	-0.019	23.351	0.226	0.226	0.000	0.000	0.000	0.000
111	A	113	VAL	0	0.013	0.007	23.208	-0.331	-0.331	0.000	0.000	0.000	0.000
112	A	114	ASN	0	-0.068	-0.035	21.505	0.439	0.439	0.000	0.000	0.000	0.000
113	A	115	ARG	1	0.844	0.921	21.859	-11.954	-11.954	0.000	0.000	0.000	0.000
114	A	116	GLU	-1	-0.882	-0.934	19.529	14.781	14.781	0.000	0.000	0.000	0.000
115	A	117	LEU	0	-0.006	-0.004	18.711	0.852	0.852	0.000	0.000	0.000	0.000
116	A	118	ILE	0	-0.014	-0.005	15.571	-0.564	-0.564	0.000	0.000	0.000	0.000
117	A	119	TYR	0	-0.028	0.008	17.079	-0.210	-0.210	0.000	0.000	0.000	0.000
118	A	120	ILE	0	-0.001	-0.001	19.189	-0.574	-0.574	0.000	0.000	0.000	0.000
119	A	121	GLN	0	0.007	-0.003	19.767	-0.186	-0.186	0.000	0.000	0.000	0.000
120	A	122	ASP	-1	-0.730	-0.829	20.598	11.714	11.714	0.000	0.000	0.000	0.000
121	A	123	ASP	-1	-0.791	-0.894	20.264	11.828	11.828	0.000	0.000	0.000	0.000
122	A	124	ILE	0	-0.025	-0.009	20.120	0.312	0.312	0.000	0.000	0.000	0.000
123	A	125	TYR	0	-0.012	-0.001	13.410	0.165	0.165	0.000	0.000	0.000	0.000
124	A	126	ASN	0	0.002	-0.006	15.825	1.213	1.213	0.000	0.000	0.000	0.000
125	A	127	ARG	1	0.797	0.890	15.567	-11.513	-11.513	0.000	0.000	0.000	0.000
126	A	128	SER	0	-0.046	-0.035	14.885	0.070	0.070	0.000	0.000	0.000	0.000
127	A	129	VAL	0	-0.024	-0.003	11.155	0.352	0.352	0.000	0.000	0.000	0.000
128	A	130	LEU	0	-0.053	-0.009	7.427	0.771	0.771	0.000	0.000	0.000	0.000

Top

Graph

Manual

About

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