FMO DATABASE

FMODB ID: G67N1

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

Total energy (hartree)

FMO2-HF: Electronic energy	-935765.643591
FMO2-HF: Nuclear repulsion	890331.312714
FMO2-HF: Total energy	-45434.330877
FMO2-MP2: Total energy	-45566.031656

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.
19.723	17.332	15.63	-7.143	-6.098	0.059

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 : -0.901 / q_NPA : -0.947

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	3	GLN	0	-0.088	-0.044	1.703	-29.428	-32.392	15.629	-6.937	-5.729	0.060
4	A	4	LEU	0	-0.007	-0.008	4.853	-4.142	-4.092	-0.001	-0.008	-0.041	0.000
5	A	5	LEU	0	-0.003	0.004	8.649	-0.090	-0.090	0.000	0.000	0.000	0.000
6	A	6	GLU	-1	-0.788	-0.883	11.049	17.515	17.515	0.000	0.000	0.000	0.000
7	A	7	SER	0	-0.004	-0.006	14.519	-0.206	-0.206	0.000	0.000	0.000	0.000
8	A	8	GLY	0	0.002	0.004	17.894	-0.355	-0.355	0.000	0.000	0.000	0.000
9	A	9	GLY	0	0.035	0.002	21.464	0.281	0.281	0.000	0.000	0.000	0.000
10	A	10	GLY	0	-0.031	-0.010	23.351	-0.212	-0.212	0.000	0.000	0.000	0.000
11	A	11	LEU	0	-0.037	-0.021	26.179	-0.055	-0.055	0.000	0.000	0.000	0.000
12	A	12	VAL	0	-0.003	0.003	29.838	-0.125	-0.125	0.000	0.000	0.000	0.000
13	A	13	GLN	0	0.031	0.012	32.365	-0.227	-0.227	0.000	0.000	0.000	0.000
14	A	14	PRO	0	-0.001	-0.019	35.083	0.150	0.150	0.000	0.000	0.000	0.000
15	A	15	GLY	0	-0.033	-0.007	36.126	-0.181	-0.181	0.000	0.000	0.000	0.000
16	A	16	GLY	0	0.001	0.008	34.166	-0.008	-0.008	0.000	0.000	0.000	0.000
17	A	17	SER	0	-0.041	-0.033	30.721	0.026	0.026	0.000	0.000	0.000	0.000
18	A	18	LEU	0	0.012	0.007	25.765	0.076	0.076	0.000	0.000	0.000	0.000
19	A	19	ARG	1	0.887	0.947	21.447	-13.745	-13.745	0.000	0.000	0.000	0.000
20	A	20	LEU	0	0.011	0.024	19.889	0.249	0.249	0.000	0.000	0.000	0.000
21	A	21	SER	0	-0.014	-0.011	18.448	-0.585	-0.585	0.000	0.000	0.000	0.000
22	A	22	CYS	0	-0.073	-0.027	12.900	0.026	0.026	0.000	0.000	0.000	0.000
23	A	23	ALA	0	0.012	0.031	12.767	-0.411	-0.411	0.000	0.000	0.000	0.000
24	A	24	ALA	0	0.028	0.020	9.284	1.393	1.393	0.000	0.000	0.000	0.000
25	A	25	SER	0	0.004	0.001	4.912	-3.427	-3.427	0.000	0.000	0.000	0.000
26	A	26	GLY	0	0.059	0.032	4.082	2.095	2.175	0.001	-0.080	-0.001	0.000
27	A	27	PHE	0	0.038	0.015	4.855	-3.355	-3.186	-0.001	-0.014	-0.155	0.000
28	A	28	ARG	1	0.881	0.948	8.005	-21.380	-21.380	0.000	0.000	0.000	0.000
29	A	29	ILE	0	0.008	0.005	11.820	-0.755	-0.755	0.000	0.000	0.000	0.000
30	A	30	SER	0	-0.092	-0.076	13.849	-0.786	-0.786	0.000	0.000	0.000	0.000
31	A	31	ASP	-1	-0.874	-0.912	13.245	17.480	17.480	0.000	0.000	0.000	0.000
32	A	32	GLU	-1	-0.810	-0.899	10.931	20.692	20.692	0.000	0.000	0.000	0.000
33	A	33	ASP	-1	-0.851	-0.915	14.312	13.745	13.745	0.000	0.000	0.000	0.000
34	A	34	MET	0	-0.037	-0.010	12.120	1.172	1.172	0.000	0.000	0.000	0.000
35	A	35	GLY	0	-0.012	-0.028	16.276	-1.290	-1.290	0.000	0.000	0.000	0.000
36	A	36	TRP	0	-0.030	-0.008	16.816	0.998	0.998	0.000	0.000	0.000	0.000
37	A	37	VAL	0	-0.001	0.010	18.362	-0.801	-0.801	0.000	0.000	0.000	0.000
38	A	38	ARG	1	0.729	0.841	19.931	-10.538	-10.538	0.000	0.000	0.000	0.000
39	A	39	GLN	0	0.052	0.033	20.685	0.165	0.165	0.000	0.000	0.000	0.000
40	A	40	ALA	0	0.018	0.006	23.258	0.067	0.067	0.000	0.000	0.000	0.000
41	A	41	PRO	0	0.018	0.013	26.571	-0.067	-0.067	0.000	0.000	0.000	0.000
42	A	42	GLY	0	-0.008	-0.005	28.878	-0.249	-0.249	0.000	0.000	0.000	0.000
43	A	43	LYS	1	0.851	0.906	28.872	-9.989	-9.989	0.000	0.000	0.000	0.000
44	A	44	GLY	0	-0.002	0.025	26.539	-0.013	-0.013	0.000	0.000	0.000	0.000
45	A	45	LEU	0	0.017	-0.013	19.864	0.300	0.300	0.000	0.000	0.000	0.000
46	A	46	GLU	-1	-0.790	-0.865	23.899	10.192	10.192	0.000	0.000	0.000	0.000
47	A	47	TRP	0	0.062	0.025	17.155	0.181	0.181	0.000	0.000	0.000	0.000
48	A	48	VAL	0	-0.006	0.009	22.468	-0.486	-0.486	0.000	0.000	0.000	0.000
49	A	49	SER	0	-0.029	-0.042	22.813	-0.418	-0.418	0.000	0.000	0.000	0.000
50	A	50	SER	0	0.031	0.011	20.752	0.456	0.456	0.000	0.000	0.000	0.000
51	A	51	ILE	0	-0.048	-0.032	19.533	-0.689	-0.689	0.000	0.000	0.000	0.000
52	A	52	TYR	0	0.033	0.015	19.781	0.480	0.480	0.000	0.000	0.000	0.000
53	A	53	GLY	0	0.029	0.015	18.517	-0.386	-0.386	0.000	0.000	0.000	0.000
54	A	54	PRO	0	0.003	0.016	19.306	-0.119	-0.119	0.000	0.000	0.000	0.000
55	A	55	SER	0	-0.009	-0.028	21.829	-0.142	-0.142	0.000	0.000	0.000	0.000
56	A	56	GLY	0	-0.029	-0.002	22.923	-0.306	-0.306	0.000	0.000	0.000	0.000
57	A	57	SER	0	-0.005	0.010	23.917	-0.185	-0.185	0.000	0.000	0.000	0.000
58	A	58	THR	0	0.012	-0.006	24.378	0.308	0.308	0.000	0.000	0.000	0.000
59	A	59	TYR	0	-0.032	-0.002	24.443	-0.635	-0.635	0.000	0.000	0.000	0.000
60	A	60	TYR	0	0.008	0.021	25.803	0.436	0.436	0.000	0.000	0.000	0.000
61	A	61	ALA	0	0.073	0.053	27.552	-0.389	-0.389	0.000	0.000	0.000	0.000
62	A	62	ASP	-1	-0.854	-0.939	29.310	8.914	8.914	0.000	0.000	0.000	0.000
63	A	63	SER	0	-0.058	-0.019	30.037	-0.185	-0.185	0.000	0.000	0.000	0.000
64	A	64	VAL	0	0.016	-0.002	27.562	-0.172	-0.172	0.000	0.000	0.000	0.000
65	A	65	LYS	1	0.857	0.931	30.970	-9.264	-9.264	0.000	0.000	0.000	0.000
66	A	66	GLY	0	-0.007	0.007	32.157	-0.265	-0.265	0.000	0.000	0.000	0.000
67	A	67	ARG	1	0.715	0.830	31.622	-9.520	-9.520	0.000	0.000	0.000	0.000
68	A	68	PHE	0	0.008	-0.013	26.254	0.128	0.128	0.000	0.000	0.000	0.000
69	A	69	THR	0	-0.052	-0.035	27.011	-0.336	-0.336	0.000	0.000	0.000	0.000
70	A	70	ILE	0	-0.005	0.023	19.799	0.280	0.280	0.000	0.000	0.000	0.000
71	A	71	SER	0	-0.012	-0.014	22.041	-0.258	-0.258	0.000	0.000	0.000	0.000
72	A	72	ARG	1	0.878	0.927	17.372	-14.777	-14.777	0.000	0.000	0.000	0.000
73	A	73	ASP	-1	-0.756	-0.824	19.388	14.111	14.111	0.000	0.000	0.000	0.000
74	A	74	ASN	0	0.077	0.012	17.415	1.306	1.306	0.000	0.000	0.000	0.000
75	A	75	SER	0	-0.102	-0.056	17.307	0.545	0.545	0.000	0.000	0.000	0.000
76	A	76	LYS	1	0.857	0.896	16.796	-13.674	-13.674	0.000	0.000	0.000	0.000
77	A	77	ASN	0	-0.021	-0.011	10.659	-0.867	-0.867	0.000	0.000	0.000	0.000
78	A	78	THR	0	-0.007	-0.011	13.621	1.377	1.377	0.000	0.000	0.000	0.000
79	A	79	LEU	0	0.012	0.017	15.444	-1.239	-1.239	0.000	0.000	0.000	0.000
80	A	80	TYR	0	-0.048	-0.042	17.200	0.330	0.330	0.000	0.000	0.000	0.000
81	A	81	LEU	0	0.033	0.004	20.254	-0.213	-0.213	0.000	0.000	0.000	0.000
82	A	82	GLN	0	-0.019	-0.007	22.636	0.249	0.249	0.000	0.000	0.000	0.000
83	A	83	MET	0	-0.030	-0.005	24.772	-0.121	-0.121	0.000	0.000	0.000	0.000
84	A	84	ASN	0	0.063	0.022	28.122	0.031	0.031	0.000	0.000	0.000	0.000
85	A	85	SER	0	0.009	0.003	31.914	-0.022	-0.022	0.000	0.000	0.000	0.000
86	A	86	LEU	0	0.004	0.027	28.702	-0.085	-0.085	0.000	0.000	0.000	0.000
87	A	87	ARG	1	0.844	0.898	32.732	-9.150	-9.150	0.000	0.000	0.000	0.000
88	A	88	ALA	0	0.062	0.029	32.773	0.246	0.246	0.000	0.000	0.000	0.000
89	A	89	GLU	-1	-0.821	-0.895	32.616	9.501	9.501	0.000	0.000	0.000	0.000
90	A	90	ASP	-1	-0.730	-0.812	28.907	10.054	10.054	0.000	0.000	0.000	0.000
91	A	91	THR	0	-0.029	-0.011	27.739	0.486	0.486	0.000	0.000	0.000	0.000
92	A	92	ALA	0	-0.024	-0.005	24.600	-0.170	-0.170	0.000	0.000	0.000	0.000
93	A	93	VAL	0	0.008	0.012	19.220	-0.003	-0.003	0.000	0.000	0.000	0.000
94	A	94	TYR	0	-0.024	-0.042	20.216	-0.315	-0.315	0.000	0.000	0.000	0.000
95	A	95	TYR	0	0.021	0.010	14.757	0.344	0.344	0.000	0.000	0.000	0.000
96	A	97	ALA	0	0.022	0.000	12.978	1.055	1.055	0.000	0.000	0.000	0.000
97	A	98	SER	0	0.059	0.025	11.632	-0.239	-0.239	0.000	0.000	0.000	0.000
98	A	99	ALA	0	-0.009	-0.008	13.690	-0.812	-0.812	0.000	0.000	0.000	0.000
99	A	100	LEU	0	-0.025	-0.019	14.230	0.929	0.929	0.000	0.000	0.000	0.000
100	A	101	GLU	-1	-0.944	-0.973	14.636	15.118	15.118	0.000	0.000	0.000	0.000
101	A	102	PRO	0	-0.078	-0.024	10.291	-0.663	-0.663	0.000	0.000	0.000	0.000
102	A	103	LEU	0	-0.034	-0.014	12.925	-0.646	-0.646	0.000	0.000	0.000	0.000
103	A	104	SER	0	-0.045	-0.032	8.890	-0.290	-0.290	0.000	0.000	0.000	0.000
104	A	105	GLU	-1	-0.891	-0.945	3.890	37.721	37.995	0.002	-0.104	-0.172	-0.001
105	A	106	PRO	0	-0.042	-0.023	7.732	-1.834	-1.834	0.000	0.000	0.000	0.000
106	A	107	LEU	0	-0.030	-0.022	9.737	-1.645	-1.645	0.000	0.000	0.000	0.000
107	A	108	GLY	0	0.010	0.017	9.627	1.519	1.519	0.000	0.000	0.000	0.000
108	A	109	PHE	0	0.000	-0.005	7.685	1.042	1.042	0.000	0.000	0.000	0.000
109	A	110	TRP	0	0.001	-0.024	9.035	-2.414	-2.414	0.000	0.000	0.000	0.000
110	A	111	GLY	0	0.023	0.018	8.949	2.570	2.570	0.000	0.000	0.000	0.000
111	A	112	GLN	0	-0.023	-0.020	10.996	0.653	0.653	0.000	0.000	0.000	0.000
112	A	113	GLY	0	-0.003	0.010	12.634	-1.040	-1.040	0.000	0.000	0.000	0.000
113	A	114	THR	0	-0.060	-0.059	16.116	-0.013	-0.013	0.000	0.000	0.000	0.000
114	A	115	LEU	0	-0.030	-0.011	19.058	-0.502	-0.502	0.000	0.000	0.000	0.000
115	A	116	VAL	0	0.025	0.019	22.612	-0.081	-0.081	0.000	0.000	0.000	0.000
116	A	117	THR	0	-0.032	-0.034	25.470	-0.186	-0.186	0.000	0.000	0.000	0.000
117	A	118	VAL	0	0.013	0.018	29.125	-0.046	-0.046	0.000	0.000	0.000	0.000
118	A	119	SER	0	0.004	-0.010	32.389	-0.147	-0.147	0.000	0.000	0.000	0.000
119	A	120	SER	0	0.004	0.011	35.679	0.100	0.100	0.000	0.000	0.000	0.000

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