FMO DATABASE

FMODB ID: 6YLYZ

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	OptHSide
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	-1084135.888734
FMO2-HF: Nuclear repulsion	1034483.761205
FMO2-HF: Total energy	-49652.12753
FMO2-MP2: Total energy	-49797.098252

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.
-3.479	-1.569	-0.017	-0.932	-0.961	0.002

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 : 0.020 / q_NPA : 0.006

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	-0.027	-0.017	3.815	-3.135	-1.183	-0.016	-0.926	-1.009	0.002
4	A	6	LEU	0	0.012	0.009	5.976	0.523	0.523	0.000	0.000	0.000	0.000
5	A	7	ASN	0	0.045	0.030	9.580	0.116	0.116	0.000	0.000	0.000	0.000
6	A	8	PRO	0	0.020	-0.005	12.610	0.096	0.096	0.000	0.000	0.000	0.000
7	A	9	GLN	0	-0.026	-0.017	15.350	0.058	0.058	0.000	0.000	0.000	0.000
8	A	10	PHE	0	0.038	0.012	15.225	0.033	0.033	0.000	0.000	0.000	0.000
9	A	11	ASP	-1	-0.778	-0.860	17.143	-0.197	-0.197	0.000	0.000	0.000	0.000
10	A	12	GLN	0	0.011	0.015	20.691	0.002	0.002	0.000	0.000	0.000	0.000
11	A	13	ILE	0	-0.008	-0.006	16.598	0.024	0.024	0.000	0.000	0.000	0.000
12	A	14	GLY	0	0.034	0.010	20.126	0.019	0.019	0.000	0.000	0.000	0.000
13	A	15	LYS	1	0.871	0.907	21.161	0.218	0.218	0.000	0.000	0.000	0.000
14	A	16	GLN	0	-0.031	0.000	24.079	0.009	0.009	0.000	0.000	0.000	0.000
15	A	17	PHE	0	0.002	-0.003	21.878	0.015	0.015	0.000	0.000	0.000	0.000
16	A	18	VAL	0	0.015	-0.001	23.761	0.018	0.018	0.000	0.000	0.000	0.000
17	A	19	GLN	0	-0.045	-0.019	25.949	0.009	0.009	0.000	0.000	0.000	0.000
18	A	20	HIS	0	0.057	0.024	26.246	0.015	0.015	0.000	0.000	0.000	0.000
19	A	21	TYR	0	0.004	0.014	25.550	0.016	0.016	0.000	0.000	0.000	0.000
20	A	22	TYR	0	0.051	-0.025	27.278	0.009	0.009	0.000	0.000	0.000	0.000
21	A	23	GLN	0	0.000	0.032	30.932	0.014	0.014	0.000	0.000	0.000	0.000
22	A	24	THR	0	0.006	0.002	30.452	0.008	0.008	0.000	0.000	0.000	0.000
23	A	25	PHE	0	-0.036	-0.019	29.642	0.010	0.010	0.000	0.000	0.000	0.000
24	A	26	GLN	0	-0.032	-0.030	32.873	0.014	0.014	0.000	0.000	0.000	0.000
25	A	27	THR	0	-0.072	-0.035	35.747	0.005	0.005	0.000	0.000	0.000	0.000
26	A	28	ASN	0	-0.028	-0.023	35.259	0.007	0.007	0.000	0.000	0.000	0.000
27	A	29	ARG	1	0.968	0.987	33.254	0.064	0.064	0.000	0.000	0.000	0.000
28	A	30	PRO	0	0.034	0.029	32.176	-0.006	-0.006	0.000	0.000	0.000	0.000
29	A	31	ALA	0	-0.007	0.001	31.256	-0.005	-0.005	0.000	0.000	0.000	0.000
30	A	32	LEU	0	-0.012	-0.005	28.303	-0.013	-0.013	0.000	0.000	0.000	0.000
31	A	33	GLY	0	0.013	-0.003	26.736	-0.012	-0.012	0.000	0.000	0.000	0.000
32	A	34	GLY	0	-0.046	-0.014	26.186	-0.005	-0.005	0.000	0.000	0.000	0.000
33	A	35	LEU	0	-0.023	-0.003	23.282	-0.018	-0.018	0.000	0.000	0.000	0.000
34	A	36	TYR	0	-0.063	-0.052	21.145	-0.024	-0.024	0.000	0.000	0.000	0.000
35	A	37	GLY	0	0.070	0.030	19.577	0.000	0.000	0.000	0.000	0.000	0.000
36	A	38	PRO	0	-0.010	-0.034	19.540	0.019	0.019	0.000	0.000	0.000	0.000
37	A	39	GLN	0	-0.014	-0.017	15.519	-0.010	-0.010	0.000	0.000	0.000	0.000
38	A	40	SER	0	-0.011	-0.004	18.026	0.000	0.000	0.000	0.000	0.000	0.000
39	A	41	MET	0	-0.059	-0.027	16.136	0.038	0.038	0.000	0.000	0.000	0.000
40	A	42	LEU	0	0.000	0.011	20.916	-0.013	-0.013	0.000	0.000	0.000	0.000
41	A	43	THR	0	-0.012	-0.019	22.895	0.018	0.018	0.000	0.000	0.000	0.000
42	A	44	TRP	0	0.017	-0.009	25.299	-0.008	-0.008	0.000	0.000	0.000	0.000
43	A	45	GLU	-1	-0.802	-0.909	28.718	-0.032	-0.032	0.000	0.000	0.000	0.000
44	A	46	ASP	-1	-0.848	-0.918	28.416	-0.010	-0.010	0.000	0.000	0.000	0.000
45	A	47	THR	0	-0.048	-0.005	28.683	0.007	0.007	0.000	0.000	0.000	0.000
46	A	48	GLN	0	-0.012	-0.004	21.642	-0.009	-0.009	0.000	0.000	0.000	0.000
47	A	49	PHE	0	-0.005	-0.008	25.249	0.006	0.006	0.000	0.000	0.000	0.000
48	A	50	GLN	0	0.005	-0.003	21.991	-0.012	-0.012	0.000	0.000	0.000	0.000
49	A	51	GLY	0	0.063	0.039	22.314	0.008	0.008	0.000	0.000	0.000	0.000
50	A	52	GLN	0	-0.036	-0.027	23.401	0.008	0.008	0.000	0.000	0.000	0.000
51	A	53	ALA	0	0.017	0.006	24.849	0.004	0.004	0.000	0.000	0.000	0.000
52	A	54	ASN	0	-0.023	-0.028	26.730	0.006	0.006	0.000	0.000	0.000	0.000
53	A	55	ILE	0	-0.020	0.005	22.898	0.005	0.005	0.000	0.000	0.000	0.000
54	A	56	VAL	0	0.013	0.010	27.422	0.001	0.001	0.000	0.000	0.000	0.000
55	A	57	ASN	0	-0.024	-0.021	29.950	0.002	0.002	0.000	0.000	0.000	0.000
56	A	58	LYS	1	0.923	0.998	29.871	0.054	0.054	0.000	0.000	0.000	0.000
57	A	59	PHE	0	0.023	-0.003	26.847	0.005	0.005	0.000	0.000	0.000	0.000
58	A	60	ASN	0	-0.035	-0.029	32.387	0.001	0.001	0.000	0.000	0.000	0.000
59	A	61	SER	0	-0.040	-0.002	34.834	0.005	0.005	0.000	0.000	0.000	0.000
60	A	62	LEU	0	-0.084	-0.034	32.478	0.004	0.004	0.000	0.000	0.000	0.000
61	A	63	ASN	0	-0.047	-0.018	36.697	0.003	0.003	0.000	0.000	0.000	0.000
62	A	64	PHE	0	0.028	0.022	35.037	0.001	0.001	0.000	0.000	0.000	0.000
63	A	65	GLN	0	0.024	0.005	40.175	-0.002	-0.002	0.000	0.000	0.000	0.000
64	A	66	ARG	1	0.756	0.844	41.483	0.053	0.053	0.000	0.000	0.000	0.000
65	A	67	VAL	0	-0.006	0.011	35.804	0.002	0.002	0.000	0.000	0.000	0.000
66	A	68	GLN	0	0.001	0.020	38.075	-0.001	-0.001	0.000	0.000	0.000	0.000
67	A	69	PHE	0	0.007	-0.015	31.991	0.002	0.002	0.000	0.000	0.000	0.000
68	A	70	GLU	-1	-0.902	-0.934	35.497	-0.078	-0.078	0.000	0.000	0.000	0.000
69	A	71	ILE	0	-0.067	-0.029	29.299	0.002	0.002	0.000	0.000	0.000	0.000
70	A	72	THR	0	0.008	-0.001	32.211	-0.001	-0.001	0.000	0.000	0.000	0.000
71	A	73	ARG	1	0.787	0.849	26.803	0.108	0.108	0.000	0.000	0.000	0.000
72	A	74	VAL	0	0.029	0.009	24.070	-0.003	-0.003	0.000	0.000	0.000	0.000
73	A	75	ASP	-1	-0.839	-0.867	22.915	-0.124	-0.124	0.000	0.000	0.000	0.000
74	A	76	CYS	0	-0.033	-0.016	19.066	-0.001	-0.001	0.000	0.000	0.000	0.000
75	A	77	GLN	0	0.003	0.000	15.495	0.021	0.021	0.000	0.000	0.000	0.000
76	A	78	PRO	0	0.004	0.023	12.165	-0.025	-0.025	0.000	0.000	0.000	0.000
77	A	79	SER	0	0.017	0.009	10.685	-0.028	-0.028	0.000	0.000	0.000	0.000
78	A	80	PRO	0	0.015	0.002	5.223	-0.086	-0.086	0.000	0.000	0.000	0.000
79	A	81	ASN	0	0.026	0.005	5.705	-1.658	-1.700	-0.001	-0.006	0.048	0.000
80	A	82	ASN	0	0.008	-0.009	7.643	0.285	0.285	0.000	0.000	0.000	0.000
81	A	83	GLY	0	0.042	0.018	9.773	0.213	0.213	0.000	0.000	0.000	0.000
82	A	84	SER	0	-0.079	-0.052	12.639	0.005	0.005	0.000	0.000	0.000	0.000
83	A	85	ILE	0	-0.008	0.011	12.491	0.022	0.022	0.000	0.000	0.000	0.000
84	A	86	VAL	0	-0.020	-0.020	16.088	0.017	0.017	0.000	0.000	0.000	0.000
85	A	87	PHE	0	-0.007	0.006	19.870	0.020	0.020	0.000	0.000	0.000	0.000
86	A	88	VAL	0	0.023	0.002	22.436	-0.001	-0.001	0.000	0.000	0.000	0.000
87	A	89	THR	0	-0.047	-0.033	25.926	0.013	0.013	0.000	0.000	0.000	0.000
88	A	90	GLY	0	0.034	0.016	29.376	-0.007	-0.007	0.000	0.000	0.000	0.000
89	A	91	ASP	-1	-0.808	-0.879	32.875	-0.048	-0.048	0.000	0.000	0.000	0.000
90	A	92	VAL	0	0.012	0.000	34.559	-0.005	-0.005	0.000	0.000	0.000	0.000
91	A	93	ARG	1	0.803	0.919	36.777	0.052	0.052	0.000	0.000	0.000	0.000
92	A	94	ILE	0	0.022	-0.001	36.572	-0.004	-0.004	0.000	0.000	0.000	0.000
93	A	95	ASP	-1	-0.789	-0.895	40.537	-0.044	-0.044	0.000	0.000	0.000	0.000
94	A	96	ASP	-1	-0.842	-0.906	43.479	-0.046	-0.046	0.000	0.000	0.000	0.000
95	A	97	GLY	0	0.037	0.036	43.857	0.003	0.003	0.000	0.000	0.000	0.000
96	A	98	GLN	0	-0.017	-0.019	42.759	-0.001	-0.001	0.000	0.000	0.000	0.000
97	A	99	PRO	0	-0.026	-0.025	40.769	-0.001	-0.001	0.000	0.000	0.000	0.000
98	A	100	LEU	0	-0.001	0.007	37.496	0.003	0.003	0.000	0.000	0.000	0.000
99	A	101	LYS	1	0.839	0.899	34.739	0.045	0.045	0.000	0.000	0.000	0.000
100	A	102	PHE	0	-0.011	0.010	28.767	0.004	0.004	0.000	0.000	0.000	0.000
101	A	103	SER	0	0.031	0.022	27.107	0.000	0.000	0.000	0.000	0.000	0.000
102	A	104	GLN	0	-0.009	-0.014	24.406	0.010	0.010	0.000	0.000	0.000	0.000
103	A	105	VAL	0	-0.030	-0.008	19.039	-0.008	-0.008	0.000	0.000	0.000	0.000
104	A	106	PHE	0	0.025	0.011	19.571	0.000	0.000	0.000	0.000	0.000	0.000
105	A	107	ASN	0	-0.045	-0.015	11.851	-0.074	-0.074	0.000	0.000	0.000	0.000
106	A	108	LEU	0	-0.004	-0.005	15.806	0.004	0.004	0.000	0.000	0.000	0.000
107	A	109	MET	0	0.009	0.003	9.920	-0.075	-0.075	0.000	0.000	0.000	0.000
108	A	110	PRO	0	0.036	0.009	11.103	0.100	0.100	0.000	0.000	0.000	0.000
109	A	111	SER	0	-0.031	-0.033	14.108	-0.015	-0.015	0.000	0.000	0.000	0.000
110	A	112	GLY	0	0.004	0.005	14.999	0.026	0.026	0.000	0.000	0.000	0.000
111	A	113	ASN	0	-0.022	-0.008	15.964	-0.011	-0.011	0.000	0.000	0.000	0.000
112	A	114	GLY	0	-0.002	0.003	17.495	0.031	0.031	0.000	0.000	0.000	0.000
113	A	115	GLY	0	0.010	0.022	18.688	0.004	0.004	0.000	0.000	0.000	0.000
114	A	116	PHE	0	-0.017	-0.017	14.131	-0.065	-0.065	0.000	0.000	0.000	0.000
115	A	117	MET	0	-0.021	0.011	16.606	0.036	0.036	0.000	0.000	0.000	0.000
116	A	118	ILE	0	0.029	0.012	17.435	-0.044	-0.044	0.000	0.000	0.000	0.000
117	A	119	PHE	0	0.006	0.022	13.844	0.015	0.015	0.000	0.000	0.000	0.000
118	A	120	ASN	0	-0.006	-0.012	14.579	0.006	0.006	0.000	0.000	0.000	0.000
119	A	121	ASP	-1	-0.711	-0.821	17.818	-0.158	-0.158	0.000	0.000	0.000	0.000
120	A	122	LEU	0	-0.021	0.003	19.704	0.019	0.019	0.000	0.000	0.000	0.000
121	A	123	PHE	0	0.010	0.009	23.451	-0.006	-0.006	0.000	0.000	0.000	0.000
122	A	124	ARG	1	0.887	0.927	26.472	0.028	0.028	0.000	0.000	0.000	0.000
123	A	125	LEU	0	-0.023	-0.008	29.471	-0.006	-0.006	0.000	0.000	0.000	0.000
124	A	126	ASN	0	-0.058	-0.046	30.646	0.010	0.010	0.000	0.000	0.000	0.000

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