FMO DATABASE

FMODB ID: 2N7NR

Calculation Name: 1ZO2-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1ZO2

Chain ID: A

ChEMBL ID:

UniProt ID: Q5CQI4

Base Structure: X-ray

Registration Date: 2023-09-20

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	124
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1084408.780894
FMO2-HF: Nuclear repulsion	1034757.257812
FMO2-HF: Total energy	-49651.523082
FMO2-MP2: Total energy	-49796.603126

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:SER)

Summations of interaction energy for fragment #1(A:3:SER)

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.
-4.389	-2.695	-0.01	-0.834	-0.85	0.001

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.029 / q_NPA : -0.027

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	ASN	0	-0.032	-0.022	3.815	-3.688	-1.937	-0.009	-0.826	-0.916	0.001
4	A	6	LEU	0	0.010	0.007	5.923	0.475	0.475	0.000	0.000	0.000	0.000
5	A	7	ASN	0	0.068	0.043	9.518	0.012	0.012	0.000	0.000	0.000	0.000
6	A	8	PRO	0	0.013	-0.003	12.562	0.126	0.126	0.000	0.000	0.000	0.000
7	A	9	GLN	0	-0.020	-0.011	15.295	0.053	0.053	0.000	0.000	0.000	0.000
8	A	10	PHE	0	0.038	0.009	15.241	0.020	0.020	0.000	0.000	0.000	0.000
9	A	11	ASP	-1	-0.783	-0.894	17.143	-0.051	-0.051	0.000	0.000	0.000	0.000
10	A	12	GLN	0	-0.036	-0.013	20.691	-0.011	-0.011	0.000	0.000	0.000	0.000
11	A	13	ILE	0	-0.001	-0.001	16.481	0.011	0.011	0.000	0.000	0.000	0.000
12	A	14	GLY	0	0.036	0.011	20.118	0.010	0.010	0.000	0.000	0.000	0.000
13	A	15	LYS	1	0.901	0.941	21.173	0.070	0.070	0.000	0.000	0.000	0.000
14	A	16	GLN	0	-0.016	0.005	24.123	-0.001	-0.001	0.000	0.000	0.000	0.000
15	A	17	PHE	0	-0.004	-0.004	21.872	0.006	0.006	0.000	0.000	0.000	0.000
16	A	18	VAL	0	0.011	-0.001	23.946	0.011	0.011	0.000	0.000	0.000	0.000
17	A	19	GLN	0	-0.030	-0.009	26.079	0.002	0.002	0.000	0.000	0.000	0.000
18	A	20	HIS	0	0.061	0.026	26.624	0.007	0.007	0.000	0.000	0.000	0.000
19	A	21	TYR	0	-0.002	0.000	25.518	0.010	0.010	0.000	0.000	0.000	0.000
20	A	22	TYR	0	0.045	-0.034	27.459	0.006	0.006	0.000	0.000	0.000	0.000
21	A	23	GLN	0	-0.002	0.023	31.041	0.011	0.011	0.000	0.000	0.000	0.000
22	A	24	THR	0	0.005	0.005	30.516	0.002	0.002	0.000	0.000	0.000	0.000
23	A	25	PHE	0	-0.052	-0.030	29.896	0.006	0.006	0.000	0.000	0.000	0.000
24	A	26	GLN	0	-0.026	-0.027	32.953	0.009	0.009	0.000	0.000	0.000	0.000
25	A	27	THR	0	-0.080	-0.029	35.830	0.001	0.001	0.000	0.000	0.000	0.000
26	A	28	ASN	0	-0.022	-0.022	34.911	0.005	0.005	0.000	0.000	0.000	0.000
27	A	29	ARG	1	1.034	1.017	33.316	0.033	0.033	0.000	0.000	0.000	0.000
28	A	30	PRO	0	0.029	0.031	32.209	-0.005	-0.005	0.000	0.000	0.000	0.000
29	A	31	ALA	0	-0.005	0.000	31.173	-0.007	-0.007	0.000	0.000	0.000	0.000
30	A	32	LEU	0	-0.014	-0.007	28.196	-0.014	-0.014	0.000	0.000	0.000	0.000
31	A	33	GLY	0	0.015	0.000	26.759	-0.008	-0.008	0.000	0.000	0.000	0.000
32	A	34	GLY	0	-0.049	-0.019	26.171	-0.009	-0.009	0.000	0.000	0.000	0.000
33	A	35	LEU	0	-0.024	-0.003	23.301	-0.022	-0.022	0.000	0.000	0.000	0.000
34	A	36	TYR	0	-0.060	-0.052	21.145	-0.018	-0.018	0.000	0.000	0.000	0.000
35	A	37	GLY	0	0.065	0.029	19.526	-0.014	-0.014	0.000	0.000	0.000	0.000
36	A	38	PRO	0	-0.009	-0.033	19.304	0.031	0.031	0.000	0.000	0.000	0.000
37	A	39	GLN	0	-0.010	-0.017	15.406	-0.021	-0.021	0.000	0.000	0.000	0.000
38	A	40	SER	0	-0.021	-0.014	17.998	0.011	0.011	0.000	0.000	0.000	0.000
39	A	41	MET	0	-0.053	-0.023	16.279	0.030	0.030	0.000	0.000	0.000	0.000
40	A	42	LEU	0	0.001	0.011	20.943	-0.002	-0.002	0.000	0.000	0.000	0.000
41	A	43	THR	0	-0.019	-0.019	23.058	0.013	0.013	0.000	0.000	0.000	0.000
42	A	44	TRP	0	0.002	-0.015	25.382	-0.003	-0.003	0.000	0.000	0.000	0.000
43	A	45	GLU	-1	-0.818	-0.920	28.809	0.044	0.044	0.000	0.000	0.000	0.000
44	A	46	ASP	-1	-0.897	-0.946	28.664	0.072	0.072	0.000	0.000	0.000	0.000
45	A	47	THR	0	-0.054	-0.016	28.769	0.006	0.006	0.000	0.000	0.000	0.000
46	A	48	GLN	0	-0.043	-0.021	21.699	-0.016	-0.016	0.000	0.000	0.000	0.000
47	A	49	PHE	0	-0.011	-0.012	25.294	-0.003	-0.003	0.000	0.000	0.000	0.000
48	A	50	GLN	0	0.018	0.001	22.242	-0.004	-0.004	0.000	0.000	0.000	0.000
49	A	51	GLY	0	0.062	0.034	22.289	-0.001	-0.001	0.000	0.000	0.000	0.000
50	A	52	GLN	0	-0.031	-0.023	23.332	0.005	0.005	0.000	0.000	0.000	0.000
51	A	53	ALA	0	0.018	0.009	24.812	0.007	0.007	0.000	0.000	0.000	0.000
52	A	54	ASN	0	-0.015	-0.018	26.844	0.005	0.005	0.000	0.000	0.000	0.000
53	A	55	ILE	0	-0.023	0.003	22.921	0.007	0.007	0.000	0.000	0.000	0.000
54	A	56	VAL	0	0.011	0.010	27.428	0.004	0.004	0.000	0.000	0.000	0.000
55	A	57	ASN	0	-0.015	-0.019	29.946	0.002	0.002	0.000	0.000	0.000	0.000
56	A	58	LYS	1	0.922	0.997	29.926	0.006	0.006	0.000	0.000	0.000	0.000
57	A	59	PHE	0	0.025	-0.005	26.951	0.005	0.005	0.000	0.000	0.000	0.000
58	A	60	ASN	0	-0.033	-0.028	32.425	0.002	0.002	0.000	0.000	0.000	0.000
59	A	61	SER	0	-0.048	-0.006	34.862	0.004	0.004	0.000	0.000	0.000	0.000
60	A	62	LEU	0	-0.082	-0.037	32.576	0.005	0.005	0.000	0.000	0.000	0.000
61	A	63	ASN	0	-0.041	-0.012	36.754	0.000	0.000	0.000	0.000	0.000	0.000
62	A	64	PHE	0	-0.001	0.010	34.924	0.001	0.001	0.000	0.000	0.000	0.000
63	A	65	GLN	0	0.019	-0.003	40.249	-0.003	-0.003	0.000	0.000	0.000	0.000
64	A	66	ARG	1	0.825	0.901	41.554	0.021	0.021	0.000	0.000	0.000	0.000
65	A	67	VAL	0	-0.030	0.001	35.849	0.004	0.004	0.000	0.000	0.000	0.000
66	A	68	GLN	0	-0.010	0.000	38.182	-0.007	-0.007	0.000	0.000	0.000	0.000
67	A	69	PHE	0	0.001	-0.010	32.319	0.004	0.004	0.000	0.000	0.000	0.000
68	A	70	GLU	-1	-0.909	-0.938	35.668	-0.028	-0.028	0.000	0.000	0.000	0.000
69	A	71	ILE	0	-0.052	-0.020	29.580	0.006	0.006	0.000	0.000	0.000	0.000
70	A	72	THR	0	-0.008	-0.009	32.403	0.000	0.000	0.000	0.000	0.000	0.000
71	A	73	ARG	1	0.837	0.908	27.219	-0.023	-0.023	0.000	0.000	0.000	0.000
72	A	74	VAL	0	0.022	0.007	24.318	-0.003	-0.003	0.000	0.000	0.000	0.000
73	A	75	ASP	-1	-0.895	-0.927	23.207	0.036	0.036	0.000	0.000	0.000	0.000
74	A	76	CYS	0	-0.029	-0.006	19.127	-0.003	-0.003	0.000	0.000	0.000	0.000
75	A	77	GLN	0	0.014	0.003	15.470	0.057	0.057	0.000	0.000	0.000	0.000
76	A	78	PRO	0	-0.014	0.015	12.232	-0.039	-0.039	0.000	0.000	0.000	0.000
77	A	79	SER	0	0.032	0.024	10.634	0.063	0.063	0.000	0.000	0.000	0.000
78	A	80	PRO	0	0.009	-0.006	5.485	-0.140	-0.140	0.000	0.000	0.000	0.000
79	A	81	ASN	0	0.031	0.011	5.705	-1.752	-1.809	-0.001	-0.008	0.066	0.000
80	A	82	ASN	0	0.018	-0.003	7.625	0.146	0.146	0.000	0.000	0.000	0.000
81	A	83	GLY	0	0.021	0.000	9.768	0.127	0.127	0.000	0.000	0.000	0.000
82	A	84	SER	0	-0.084	-0.049	12.626	0.055	0.055	0.000	0.000	0.000	0.000
83	A	85	ILE	0	0.002	0.017	12.956	0.004	0.004	0.000	0.000	0.000	0.000
84	A	86	VAL	0	-0.015	-0.021	16.273	0.010	0.010	0.000	0.000	0.000	0.000
85	A	87	PHE	0	-0.021	-0.001	20.050	0.015	0.015	0.000	0.000	0.000	0.000
86	A	88	VAL	0	0.022	0.002	22.633	-0.008	-0.008	0.000	0.000	0.000	0.000
87	A	89	THR	0	-0.029	-0.014	26.111	0.013	0.013	0.000	0.000	0.000	0.000
88	A	90	GLY	0	0.032	0.011	29.566	-0.009	-0.009	0.000	0.000	0.000	0.000
89	A	91	ASP	-1	-0.834	-0.883	33.058	0.020	0.020	0.000	0.000	0.000	0.000
90	A	92	VAL	0	0.018	0.004	34.833	-0.006	-0.006	0.000	0.000	0.000	0.000
91	A	93	ARG	1	0.856	0.929	36.924	0.010	0.010	0.000	0.000	0.000	0.000
92	A	94	ILE	0	0.028	0.004	36.838	-0.005	-0.005	0.000	0.000	0.000	0.000
93	A	95	ASP	-1	-0.810	-0.902	40.654	-0.012	-0.012	0.000	0.000	0.000	0.000
94	A	96	ASP	-1	-0.911	-0.947	43.613	-0.014	-0.014	0.000	0.000	0.000	0.000
95	A	97	GLY	0	0.030	0.023	44.009	0.002	0.002	0.000	0.000	0.000	0.000
96	A	98	GLN	0	-0.030	-0.019	42.807	-0.001	-0.001	0.000	0.000	0.000	0.000
97	A	99	PRO	0	-0.035	-0.021	40.922	-0.001	-0.001	0.000	0.000	0.000	0.000
98	A	100	LEU	0	0.017	0.008	37.585	0.004	0.004	0.000	0.000	0.000	0.000
99	A	101	LYS	1	0.871	0.912	34.919	-0.025	-0.025	0.000	0.000	0.000	0.000
100	A	102	PHE	0	-0.007	0.012	28.874	0.003	0.003	0.000	0.000	0.000	0.000
101	A	103	SER	0	0.024	0.004	27.278	-0.002	-0.002	0.000	0.000	0.000	0.000
102	A	104	GLN	0	-0.017	-0.004	24.542	0.001	0.001	0.000	0.000	0.000	0.000
103	A	105	VAL	0	-0.033	-0.008	19.191	0.002	0.002	0.000	0.000	0.000	0.000
104	A	106	PHE	0	0.025	0.010	19.706	-0.009	-0.009	0.000	0.000	0.000	0.000
105	A	107	ASN	0	-0.049	-0.020	12.023	-0.027	-0.027	0.000	0.000	0.000	0.000
106	A	108	LEU	0	-0.010	-0.009	15.920	-0.025	-0.025	0.000	0.000	0.000	0.000
107	A	109	MET	0	0.012	0.003	9.804	-0.021	-0.021	0.000	0.000	0.000	0.000
108	A	110	PRO	0	0.024	0.002	11.271	0.081	0.081	0.000	0.000	0.000	0.000
109	A	111	SER	0	-0.040	-0.028	14.094	-0.035	-0.035	0.000	0.000	0.000	0.000
110	A	112	GLY	0	0.012	0.008	14.995	0.005	0.005	0.000	0.000	0.000	0.000
111	A	113	ASN	0	-0.003	-0.003	15.959	-0.035	-0.035	0.000	0.000	0.000	0.000
112	A	114	GLY	0	-0.005	-0.001	17.495	0.042	0.042	0.000	0.000	0.000	0.000
113	A	115	GLY	0	0.012	0.023	18.688	0.022	0.022	0.000	0.000	0.000	0.000
114	A	116	PHE	0	-0.027	-0.022	14.185	-0.070	-0.070	0.000	0.000	0.000	0.000
115	A	117	MET	0	-0.019	0.012	16.701	0.041	0.041	0.000	0.000	0.000	0.000
116	A	118	ILE	0	0.024	0.014	17.480	-0.020	-0.020	0.000	0.000	0.000	0.000
117	A	119	PHE	0	0.004	0.025	14.025	-0.003	-0.003	0.000	0.000	0.000	0.000
118	A	120	ASN	0	0.006	0.000	14.650	0.019	0.019	0.000	0.000	0.000	0.000
119	A	121	ASP	-1	-0.716	-0.825	17.897	-0.049	-0.049	0.000	0.000	0.000	0.000
120	A	122	LEU	0	-0.010	0.004	19.719	0.014	0.014	0.000	0.000	0.000	0.000
121	A	123	PHE	0	0.012	0.011	23.571	-0.001	-0.001	0.000	0.000	0.000	0.000
122	A	124	ARG	1	0.960	0.974	25.830	-0.097	-0.097	0.000	0.000	0.000	0.000
123	A	125	LEU	0	-0.012	0.001	29.617	-0.004	-0.004	0.000	0.000	0.000	0.000
124	A	126	ASN	0	-0.055	-0.040	31.016	0.013	0.013	0.000	0.000	0.000	0.000

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