FMO DATABASE

FMODB ID: 1N7YZ

Calculation Name: 2PIH-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2PIH

Chain ID: A

ChEMBL ID:

UniProt ID: O31779

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	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	123
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-857598.373474
FMO2-HF: Nuclear repulsion	808612.341577
FMO2-HF: Total energy	-48986.031897
FMO2-MP2: Total energy	-49130.408199

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:THR)

Summations of interaction energy for fragment #1(A:2:THR)

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.
-2.284	-0.183	-0.001	-1.062	-1.038	0.002

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.027 / q_NPA : -0.004

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	4	TYR	0	0.041	0.031	3.570	-2.284	-0.183	-0.001	-1.062	-1.038	0.002
4	A	5	SER	0	-0.002	-0.004	5.756	1.109	1.109	0.000	0.000	0.000	0.000
5	A	6	LYS	1	1.014	0.974	7.613	0.798	0.798	0.000	0.000	0.000	0.000
6	A	7	LYS	1	0.947	0.977	10.730	0.699	0.699	0.000	0.000	0.000	0.000
7	A	8	ASP	-1	-0.779	-0.877	6.421	-2.494	-2.494	0.000	0.000	0.000	0.000
8	A	9	ILE	0	0.030	0.013	9.906	0.177	0.177	0.000	0.000	0.000	0.000
9	A	10	VAL	0	-0.022	-0.005	12.020	0.178	0.178	0.000	0.000	0.000	0.000
10	A	11	GLN	0	-0.050	-0.033	12.233	0.033	0.033	0.000	0.000	0.000	0.000
11	A	12	GLN	0	0.019	0.001	8.845	0.235	0.235	0.000	0.000	0.000	0.000
12	A	13	ALA	0	0.041	0.029	14.275	0.083	0.083	0.000	0.000	0.000	0.000
13	A	14	ARG	1	0.901	0.944	17.242	0.533	0.533	0.000	0.000	0.000	0.000
14	A	15	ASN	0	-0.014	-0.019	15.029	0.124	0.124	0.000	0.000	0.000	0.000
15	A	16	LEU	0	0.037	0.027	18.376	0.038	0.038	0.000	0.000	0.000	0.000
16	A	17	ALA	0	0.032	0.009	20.007	0.045	0.045	0.000	0.000	0.000	0.000
17	A	18	LYS	1	0.912	0.964	19.663	0.439	0.439	0.000	0.000	0.000	0.000
18	A	19	MET	0	0.040	0.045	19.091	0.022	0.022	0.000	0.000	0.000	0.000
19	A	20	ILE	0	0.024	0.022	23.631	0.018	0.018	0.000	0.000	0.000	0.000
20	A	21	SER	0	-0.117	-0.068	26.111	0.029	0.029	0.000	0.000	0.000	0.000
21	A	22	GLU	-1	-1.015	-1.002	26.859	-0.243	-0.243	0.000	0.000	0.000	0.000
22	A	23	THR	0	-0.002	-0.009	28.181	0.004	0.004	0.000	0.000	0.000	0.000
23	A	24	GLU	-1	-0.928	-0.975	30.732	-0.163	-0.163	0.000	0.000	0.000	0.000
24	A	25	GLU	-1	-0.838	-0.919	32.405	-0.200	-0.200	0.000	0.000	0.000	0.000
25	A	26	VAL	0	-0.029	-0.019	30.152	0.008	0.008	0.000	0.000	0.000	0.000
26	A	27	ASP	-1	-0.966	-0.979	33.370	-0.149	-0.149	0.000	0.000	0.000	0.000
27	A	28	PHE	0	-0.044	-0.023	35.543	0.011	0.011	0.000	0.000	0.000	0.000
28	A	29	PHE	0	0.036	0.002	35.551	0.007	0.007	0.000	0.000	0.000	0.000
29	A	30	LYS	1	0.917	0.959	32.807	0.188	0.188	0.000	0.000	0.000	0.000
30	A	31	ARG	1	0.916	0.974	37.759	0.143	0.143	0.000	0.000	0.000	0.000
31	A	32	ALA	0	0.028	0.020	40.740	0.008	0.008	0.000	0.000	0.000	0.000
32	A	33	GLU	-1	-0.950	-0.986	38.084	-0.146	-0.146	0.000	0.000	0.000	0.000
33	A	34	ALA	0	-0.054	-0.034	41.653	0.006	0.006	0.000	0.000	0.000	0.000
34	A	35	GLN	0	0.012	0.006	43.283	0.009	0.009	0.000	0.000	0.000	0.000
35	A	36	ILE	0	-0.032	-0.014	43.266	0.006	0.006	0.000	0.000	0.000	0.000
36	A	37	ASN	0	-0.089	-0.037	42.108	0.005	0.005	0.000	0.000	0.000	0.000
37	A	38	GLU	-1	-0.962	-0.973	46.473	-0.091	-0.091	0.000	0.000	0.000	0.000
38	A	39	ASN	0	-0.005	0.016	49.382	0.006	0.006	0.000	0.000	0.000	0.000
39	A	40	ASP	-1	-0.845	-0.934	51.641	-0.071	-0.071	0.000	0.000	0.000	0.000
40	A	41	LYS	1	0.867	0.946	54.717	0.071	0.071	0.000	0.000	0.000	0.000
41	A	42	VAL	0	0.066	0.027	48.614	0.001	0.001	0.000	0.000	0.000	0.000
42	A	43	SER	0	0.013	0.018	51.637	-0.001	-0.001	0.000	0.000	0.000	0.000
43	A	44	THR	0	-0.061	-0.031	52.541	0.002	0.002	0.000	0.000	0.000	0.000
44	A	45	ILE	0	0.057	0.018	53.493	0.001	0.001	0.000	0.000	0.000	0.000
45	A	46	VAL	0	0.033	0.018	48.793	0.000	0.000	0.000	0.000	0.000	0.000
46	A	47	ASN	0	-0.022	-0.016	51.820	-0.002	-0.002	0.000	0.000	0.000	0.000
47	A	48	GLN	0	-0.028	-0.016	54.032	0.001	0.001	0.000	0.000	0.000	0.000
48	A	49	ILE	0	0.044	0.031	51.194	0.002	0.002	0.000	0.000	0.000	0.000
49	A	50	LYS	1	0.940	0.977	47.883	0.092	0.092	0.000	0.000	0.000	0.000
50	A	51	ALA	0	-0.022	-0.009	52.939	0.001	0.001	0.000	0.000	0.000	0.000
51	A	52	LEU	0	0.006	-0.001	56.464	0.002	0.002	0.000	0.000	0.000	0.000
52	A	53	GLN	0	0.037	0.015	49.307	0.001	0.001	0.000	0.000	0.000	0.000
53	A	54	LYS	1	0.950	0.988	54.226	0.061	0.061	0.000	0.000	0.000	0.000
54	A	55	GLN	0	-0.081	-0.055	55.594	0.002	0.002	0.000	0.000	0.000	0.000
55	A	56	ALA	0	0.044	0.034	55.240	0.002	0.002	0.000	0.000	0.000	0.000
56	A	57	VAL	0	0.018	-0.001	52.699	0.001	0.001	0.000	0.000	0.000	0.000
57	A	58	ASN	0	-0.015	-0.007	55.697	0.001	0.001	0.000	0.000	0.000	0.000
58	A	59	LEU	0	-0.048	-0.033	59.145	0.002	0.002	0.000	0.000	0.000	0.000
59	A	60	LYS	1	0.974	1.006	53.250	0.075	0.075	0.000	0.000	0.000	0.000
60	A	61	HIS	0	-0.039	0.002	57.940	0.001	0.001	0.000	0.000	0.000	0.000
61	A	62	TYR	0	-0.072	-0.040	59.225	0.001	0.001	0.000	0.000	0.000	0.000
62	A	63	GLU	-1	-0.904	-0.944	61.545	-0.049	-0.049	0.000	0.000	0.000	0.000
63	A	64	LYS	1	0.880	0.947	62.882	0.050	0.050	0.000	0.000	0.000	0.000
64	A	65	HIS	0	0.077	0.016	61.272	-0.002	-0.002	0.000	0.000	0.000	0.000
65	A	66	GLU	-1	-0.884	-0.942	63.194	-0.050	-0.050	0.000	0.000	0.000	0.000
66	A	67	ALA	0	-0.047	-0.035	64.871	-0.001	-0.001	0.000	0.000	0.000	0.000
67	A	68	LEU	0	-0.012	-0.011	57.454	-0.001	-0.001	0.000	0.000	0.000	0.000
68	A	69	LYS	1	1.015	1.005	60.390	0.055	0.055	0.000	0.000	0.000	0.000
69	A	70	GLN	0	-0.027	-0.003	61.442	-0.002	-0.002	0.000	0.000	0.000	0.000
70	A	71	VAL	0	-0.054	-0.028	58.067	-0.001	-0.001	0.000	0.000	0.000	0.000
71	A	72	GLU	-1	-0.937	-0.984	56.366	-0.071	-0.071	0.000	0.000	0.000	0.000
72	A	73	ALA	0	0.062	0.047	57.436	-0.002	-0.002	0.000	0.000	0.000	0.000
73	A	74	LYS	1	0.872	0.933	59.359	0.056	0.056	0.000	0.000	0.000	0.000
74	A	75	ILE	0	-0.012	-0.006	53.420	-0.001	-0.001	0.000	0.000	0.000	0.000
75	A	76	ASP	-1	-0.854	-0.919	54.668	-0.078	-0.078	0.000	0.000	0.000	0.000
76	A	77	ALA	0	-0.056	-0.031	55.640	-0.001	-0.001	0.000	0.000	0.000	0.000
77	A	78	LEU	0	-0.033	-0.028	55.495	0.000	0.000	0.000	0.000	0.000	0.000
78	A	79	GLN	0	-0.033	-0.024	49.815	-0.001	-0.001	0.000	0.000	0.000	0.000
79	A	80	GLU	-1	-0.859	-0.926	52.231	-0.089	-0.089	0.000	0.000	0.000	0.000
80	A	81	GLU	-1	-0.952	-0.976	54.131	-0.069	-0.069	0.000	0.000	0.000	0.000
81	A	82	LEU	0	-0.062	-0.053	48.769	0.000	0.000	0.000	0.000	0.000	0.000
82	A	83	GLU	-1	-0.774	-0.882	47.687	-0.109	-0.109	0.000	0.000	0.000	0.000
83	A	84	GLU	-1	-0.924	-0.943	50.796	-0.080	-0.080	0.000	0.000	0.000	0.000
84	A	85	ILE	0	-0.110	-0.040	51.603	0.002	0.002	0.000	0.000	0.000	0.000
85	A	86	PRO	0	0.036	0.014	50.706	-0.004	-0.004	0.000	0.000	0.000	0.000
86	A	87	VAL	0	0.037	0.011	48.012	-0.003	-0.003	0.000	0.000	0.000	0.000
87	A	88	ILE	0	-0.026	-0.003	46.624	-0.005	-0.005	0.000	0.000	0.000	0.000
88	A	89	GLN	0	-0.024	-0.019	46.074	-0.006	-0.006	0.000	0.000	0.000	0.000
89	A	90	GLU	-1	-0.887	-0.946	44.919	-0.115	-0.115	0.000	0.000	0.000	0.000
90	A	91	PHE	0	-0.040	-0.014	39.663	-0.008	-0.008	0.000	0.000	0.000	0.000
91	A	92	ARG	1	0.736	0.843	41.293	0.111	0.111	0.000	0.000	0.000	0.000
92	A	93	ASP	-1	-0.859	-0.924	41.280	-0.127	-0.127	0.000	0.000	0.000	0.000
93	A	94	SER	0	-0.052	-0.019	38.626	-0.010	-0.010	0.000	0.000	0.000	0.000
94	A	95	GLN	0	-0.017	-0.022	37.116	-0.006	-0.006	0.000	0.000	0.000	0.000
95	A	96	MET	0	-0.034	-0.002	36.215	-0.010	-0.010	0.000	0.000	0.000	0.000
96	A	97	GLU	-1	-0.812	-0.912	35.967	-0.170	-0.170	0.000	0.000	0.000	0.000
97	A	98	VAL	0	-0.008	-0.006	31.440	-0.016	-0.016	0.000	0.000	0.000	0.000
98	A	99	ASN	0	-0.036	-0.034	31.557	-0.031	-0.031	0.000	0.000	0.000	0.000
99	A	100	ASP	-1	-0.903	-0.951	32.011	-0.197	-0.197	0.000	0.000	0.000	0.000
100	A	101	LEU	0	-0.022	0.002	28.177	-0.018	-0.018	0.000	0.000	0.000	0.000
101	A	102	LEU	0	-0.032	-0.030	26.734	-0.031	-0.031	0.000	0.000	0.000	0.000
102	A	103	GLN	0	-0.010	-0.004	27.044	-0.024	-0.024	0.000	0.000	0.000	0.000
103	A	104	LEU	0	0.035	0.027	27.528	-0.014	-0.014	0.000	0.000	0.000	0.000
104	A	105	VAL	0	0.008	0.015	22.511	-0.028	-0.028	0.000	0.000	0.000	0.000
105	A	106	ALA	0	-0.022	-0.013	23.365	-0.042	-0.042	0.000	0.000	0.000	0.000
106	A	107	HIS	0	0.007	0.003	23.912	-0.036	-0.036	0.000	0.000	0.000	0.000
107	A	108	THR	0	-0.006	-0.008	22.069	-0.003	-0.003	0.000	0.000	0.000	0.000
108	A	109	ILE	0	-0.035	-0.017	18.251	-0.035	-0.035	0.000	0.000	0.000	0.000
109	A	110	SER	0	-0.045	-0.019	19.867	-0.043	-0.043	0.000	0.000	0.000	0.000
110	A	111	ASN	0	-0.035	-0.045	21.657	0.021	0.021	0.000	0.000	0.000	0.000
111	A	112	GLN	0	-0.001	0.011	17.356	0.067	0.067	0.000	0.000	0.000	0.000
112	A	113	VAL	0	-0.034	-0.013	16.253	-0.036	-0.036	0.000	0.000	0.000	0.000
113	A	114	THR	0	0.005	0.003	17.513	0.003	0.003	0.000	0.000	0.000	0.000
114	A	115	ASN	0	0.024	0.012	19.860	0.046	0.046	0.000	0.000	0.000	0.000
115	A	116	GLU	-1	-0.877	-0.941	13.331	-0.666	-0.666	0.000	0.000	0.000	0.000
116	A	117	ILE	0	-0.034	-0.018	15.612	0.021	0.021	0.000	0.000	0.000	0.000
117	A	118	ILE	0	-0.019	-0.008	16.790	0.062	0.062	0.000	0.000	0.000	0.000
118	A	119	THR	0	-0.086	-0.049	16.403	0.037	0.037	0.000	0.000	0.000	0.000
119	A	120	SER	0	-0.043	-0.011	12.553	0.084	0.084	0.000	0.000	0.000	0.000
120	A	121	THR	0	-0.085	-0.037	15.579	0.066	0.066	0.000	0.000	0.000	0.000
121	A	122	GLY	0	0.010	0.005	18.166	0.039	0.039	0.000	0.000	0.000	0.000
122	A	123	GLY	0	-0.056	-0.021	21.080	0.005	0.005	0.000	0.000	0.000	0.000
123	A	124	ASP	-1	-0.986	-0.989	22.923	-0.155	-0.155	0.000	0.000	0.000	0.000

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