FMO DATABASE

FMODB ID: G5L51

Calculation Name: 1ZTD-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1ZTD

Chain ID: A

ChEMBL ID:

UniProt ID: Q8U363

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	125
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1033125.127391
FMO2-HF: Nuclear repulsion	986034.46781
FMO2-HF: Total energy	-47090.659581
FMO2-MP2: Total energy	-47231.647773

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:SER)

Summations of interaction energy for fragment #1(A:1: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.
-38.365	-38.279	25.89	-14.16	-11.815	-0.052

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.094 / q_NPA : -0.085

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	3	ILE	0	-0.044	-0.019	2.041	-7.903	-5.614	5.342	-3.536	-4.095	0.032
4	A	4	ASP	-1	-0.849	-0.925	3.746	1.289	1.557	0.009	0.053	-0.329	0.001
5	A	5	LYS	1	0.980	0.964	5.800	-0.659	-0.659	0.000	0.000	0.000	0.000
6	A	6	GLY	0	-0.001	0.009	7.842	-0.190	-0.190	0.000	0.000	0.000	0.000
7	A	7	LEU	0	0.015	0.010	9.433	-0.073	-0.073	0.000	0.000	0.000	0.000
8	A	8	ALA	0	0.028	0.018	8.226	-0.085	-0.085	0.000	0.000	0.000	0.000
9	A	9	LYS	1	0.944	0.971	10.295	-0.186	-0.186	0.000	0.000	0.000	0.000
10	A	10	PHE	0	0.006	0.015	13.147	-0.040	-0.040	0.000	0.000	0.000	0.000
11	A	11	GLY	0	0.040	0.017	13.636	-0.028	-0.028	0.000	0.000	0.000	0.000
12	A	12	ASP	-1	-0.905	-0.950	14.227	-0.033	-0.033	0.000	0.000	0.000	0.000
13	A	13	SER	0	-0.080	-0.040	15.773	-0.018	-0.018	0.000	0.000	0.000	0.000
14	A	14	LEU	0	0.015	0.010	18.052	-0.009	-0.009	0.000	0.000	0.000	0.000
15	A	15	ILE	0	0.014	-0.001	16.687	-0.008	-0.008	0.000	0.000	0.000	0.000
16	A	16	ASN	0	0.004	0.002	18.805	-0.014	-0.014	0.000	0.000	0.000	0.000
17	A	17	PHE	0	-0.012	0.018	21.475	-0.003	-0.003	0.000	0.000	0.000	0.000
18	A	18	LEU	0	0.012	0.000	20.886	-0.002	-0.002	0.000	0.000	0.000	0.000
19	A	19	TYR	0	0.014	0.007	22.630	-0.002	-0.002	0.000	0.000	0.000	0.000
20	A	20	SER	0	-0.006	-0.012	24.502	-0.001	-0.001	0.000	0.000	0.000	0.000
21	A	21	LEU	0	0.007	0.028	27.097	0.000	0.000	0.000	0.000	0.000	0.000
22	A	22	ALA	0	0.033	0.008	27.330	0.000	0.000	0.000	0.000	0.000	0.000
23	A	23	LEU	0	-0.028	-0.019	28.347	0.000	0.000	0.000	0.000	0.000	0.000
24	A	24	THR	0	0.011	0.009	30.208	0.001	0.001	0.000	0.000	0.000	0.000
25	A	25	GLU	-1	-0.910	-0.963	32.500	-0.011	-0.011	0.000	0.000	0.000	0.000
26	A	26	PHE	0	-0.056	-0.021	32.180	0.000	0.000	0.000	0.000	0.000	0.000
27	A	27	LEU	0	-0.051	-0.028	33.113	0.000	0.000	0.000	0.000	0.000	0.000
28	A	28	GLY	0	0.012	0.025	36.079	0.001	0.001	0.000	0.000	0.000	0.000
29	A	29	LYS	1	0.907	0.945	36.215	0.021	0.021	0.000	0.000	0.000	0.000
30	A	30	PRO	0	-0.008	-0.008	34.527	-0.001	-0.001	0.000	0.000	0.000	0.000
31	A	31	THR	0	-0.025	-0.014	31.367	-0.001	-0.001	0.000	0.000	0.000	0.000
32	A	32	GLY	0	0.026	0.006	28.486	0.002	0.002	0.000	0.000	0.000	0.000
33	A	33	ASP	-1	-0.879	-0.928	26.424	-0.045	-0.045	0.000	0.000	0.000	0.000
34	A	34	ARG	1	0.951	0.979	21.461	0.036	0.036	0.000	0.000	0.000	0.000
35	A	35	VAL	0	0.039	0.020	18.101	-0.006	-0.006	0.000	0.000	0.000	0.000
36	A	36	PRO	0	-0.064	-0.020	18.618	-0.007	-0.007	0.000	0.000	0.000	0.000
37	A	37	ASN	0	0.082	0.026	11.555	-0.023	-0.023	0.000	0.000	0.000	0.000
38	A	38	ALA	0	0.014	-0.013	14.747	-0.021	-0.021	0.000	0.000	0.000	0.000
39	A	39	SER	0	-0.013	-0.016	16.838	-0.003	-0.003	0.000	0.000	0.000	0.000
40	A	40	LEU	0	0.023	0.031	13.437	0.000	0.000	0.000	0.000	0.000	0.000
41	A	41	ALA	0	-0.026	-0.017	13.021	-0.016	-0.016	0.000	0.000	0.000	0.000
42	A	42	ILE	0	0.019	0.009	13.964	0.001	0.001	0.000	0.000	0.000	0.000
43	A	43	ALA	0	0.029	0.018	16.698	0.011	0.011	0.000	0.000	0.000	0.000
44	A	44	LEU	0	-0.001	-0.008	10.128	0.003	0.003	0.000	0.000	0.000	0.000
45	A	45	GLU	-1	-1.005	-1.010	14.581	-0.169	-0.169	0.000	0.000	0.000	0.000
46	A	46	LEU	0	-0.048	-0.017	16.185	0.022	0.022	0.000	0.000	0.000	0.000
47	A	47	THR	0	-0.002	0.009	16.688	0.010	0.010	0.000	0.000	0.000	0.000
48	A	48	GLY	0	-0.040	-0.009	17.462	0.014	0.014	0.000	0.000	0.000	0.000
49	A	49	LEU	0	0.065	0.024	13.096	0.000	0.000	0.000	0.000	0.000	0.000
50	A	50	SER	0	-0.027	-0.023	11.239	-0.020	-0.020	0.000	0.000	0.000	0.000
51	A	51	LYS	1	0.905	0.936	11.508	0.025	0.025	0.000	0.000	0.000	0.000
52	A	52	ASN	0	0.013	0.018	11.048	0.078	0.078	0.000	0.000	0.000	0.000
53	A	53	LEU	0	-0.023	0.025	7.039	0.058	0.058	0.000	0.000	0.000	0.000
54	A	54	ARG	1	1.040	1.014	4.108	-2.585	-2.245	0.000	-0.101	-0.240	0.001
55	A	55	ARG	1	0.971	0.964	6.059	-0.580	-0.580	0.000	0.000	0.000	0.000
56	A	56	VAL	0	-0.032	-0.013	2.282	-1.619	-0.650	2.573	-1.523	-2.018	0.004
57	A	57	ASP	-1	-0.678	-0.815	1.670	-27.828	-31.657	17.967	-9.018	-5.121	-0.090
58	A	58	LYS	1	0.819	0.924	4.456	1.035	1.084	-0.001	-0.035	-0.012	0.000
59	A	59	HIS	0	-0.002	-0.008	7.649	0.176	0.176	0.000	0.000	0.000	0.000
60	A	60	ALA	0	0.011	0.015	5.024	0.180	0.180	0.000	0.000	0.000	0.000
61	A	61	LYS	1	0.943	0.968	6.932	0.389	0.389	0.000	0.000	0.000	0.000
62	A	62	GLY	0	0.021	0.009	9.116	0.089	0.089	0.000	0.000	0.000	0.000
63	A	63	ASP	-1	-0.840	-0.922	6.687	-0.082	-0.082	0.000	0.000	0.000	0.000
64	A	64	TYR	0	-0.008	-0.011	5.593	0.266	0.266	0.000	0.000	0.000	0.000
65	A	65	ALA	0	-0.003	-0.008	7.597	0.113	0.113	0.000	0.000	0.000	0.000
66	A	66	GLU	-1	-0.878	-0.942	10.887	0.043	0.043	0.000	0.000	0.000	0.000
67	A	67	ALA	0	0.017	-0.002	8.456	0.024	0.024	0.000	0.000	0.000	0.000
68	A	68	LEU	0	-0.054	-0.016	10.400	-0.012	-0.012	0.000	0.000	0.000	0.000
69	A	69	ILE	0	0.022	-0.004	12.260	0.001	0.001	0.000	0.000	0.000	0.000
70	A	70	ALA	0	0.004	0.002	13.090	-0.004	-0.004	0.000	0.000	0.000	0.000
71	A	71	LYS	1	0.941	0.977	10.046	-0.062	-0.062	0.000	0.000	0.000	0.000
72	A	72	ALA	0	0.025	0.011	14.763	-0.010	-0.010	0.000	0.000	0.000	0.000
73	A	73	TRP	0	0.009	0.000	17.787	-0.005	-0.005	0.000	0.000	0.000	0.000
74	A	74	LEU	0	-0.039	-0.021	15.546	-0.003	-0.003	0.000	0.000	0.000	0.000
75	A	75	MET	0	-0.042	-0.012	18.628	-0.003	-0.003	0.000	0.000	0.000	0.000
76	A	76	GLY	0	-0.011	0.009	20.465	-0.003	-0.003	0.000	0.000	0.000	0.000
77	A	77	LEU	0	-0.037	-0.013	19.170	-0.002	-0.002	0.000	0.000	0.000	0.000
78	A	78	ILE	0	-0.024	-0.022	20.745	-0.003	-0.003	0.000	0.000	0.000	0.000
79	A	79	SER	0	0.003	0.019	23.502	0.002	0.002	0.000	0.000	0.000	0.000
80	A	80	GLU	-1	-0.827	-0.931	25.316	-0.005	-0.005	0.000	0.000	0.000	0.000
81	A	81	ARG	1	0.994	0.986	26.294	0.003	0.003	0.000	0.000	0.000	0.000
82	A	82	GLU	-1	-0.810	-0.871	26.342	-0.006	-0.006	0.000	0.000	0.000	0.000
83	A	83	ALA	0	0.030	0.007	23.156	-0.002	-0.002	0.000	0.000	0.000	0.000
84	A	84	VAL	0	0.017	0.009	25.012	-0.004	-0.004	0.000	0.000	0.000	0.000
85	A	85	GLU	-1	-0.927	-0.974	27.415	-0.014	-0.014	0.000	0.000	0.000	0.000
86	A	86	ILE	0	-0.051	-0.013	24.359	-0.001	-0.001	0.000	0.000	0.000	0.000
87	A	87	ILE	0	0.003	0.006	22.693	-0.003	-0.003	0.000	0.000	0.000	0.000
88	A	88	LYS	1	0.887	0.928	26.135	0.012	0.012	0.000	0.000	0.000	0.000
89	A	89	LYS	1	0.877	0.948	29.767	0.013	0.013	0.000	0.000	0.000	0.000
90	A	90	ASN	0	-0.053	-0.020	26.887	0.000	0.000	0.000	0.000	0.000	0.000
91	A	91	LEU	0	-0.054	0.002	26.925	-0.004	-0.004	0.000	0.000	0.000	0.000
92	A	92	TYR	0	0.026	0.007	29.643	0.002	0.002	0.000	0.000	0.000	0.000
93	A	93	PRO	0	0.041	0.012	31.668	-0.001	-0.001	0.000	0.000	0.000	0.000
94	A	94	GLU	-1	-0.853	-0.941	30.046	-0.033	-0.033	0.000	0.000	0.000	0.000
95	A	95	VAL	0	-0.065	-0.012	28.205	-0.003	-0.003	0.000	0.000	0.000	0.000
96	A	96	LEU	0	-0.076	-0.043	29.779	-0.001	-0.001	0.000	0.000	0.000	0.000
97	A	97	ASP	-1	-0.862	-0.927	31.185	-0.037	-0.037	0.000	0.000	0.000	0.000
98	A	98	PHE	0	-0.022	-0.023	26.996	-0.005	-0.005	0.000	0.000	0.000	0.000
99	A	99	SER	0	-0.017	-0.013	28.087	-0.006	-0.006	0.000	0.000	0.000	0.000
100	A	100	LYS	1	0.932	0.959	27.976	0.043	0.043	0.000	0.000	0.000	0.000
101	A	101	LYS	1	0.893	0.959	25.262	0.045	0.045	0.000	0.000	0.000	0.000
102	A	102	LYS	1	0.930	0.964	20.313	0.097	0.097	0.000	0.000	0.000	0.000
103	A	103	GLU	-1	-0.885	-0.938	22.134	-0.073	-0.073	0.000	0.000	0.000	0.000
104	A	104	ALA	0	0.007	0.008	23.813	0.000	0.000	0.000	0.000	0.000	0.000
105	A	105	ILE	0	0.030	0.011	21.091	0.002	0.002	0.000	0.000	0.000	0.000
106	A	106	GLY	0	0.028	0.006	19.958	0.000	0.000	0.000	0.000	0.000	0.000
107	A	107	ARG	1	0.908	0.948	20.825	0.054	0.054	0.000	0.000	0.000	0.000
108	A	108	ALA	0	0.019	0.017	23.615	0.004	0.004	0.000	0.000	0.000	0.000
109	A	109	LEU	0	-0.011	-0.012	18.294	0.004	0.004	0.000	0.000	0.000	0.000
110	A	110	ALA	0	-0.005	0.003	19.385	0.000	0.000	0.000	0.000	0.000	0.000
111	A	111	PRO	0	0.030	0.011	20.364	0.001	0.001	0.000	0.000	0.000	0.000
112	A	112	LEU	0	0.017	0.014	19.784	0.005	0.005	0.000	0.000	0.000	0.000
113	A	113	LEU	0	-0.012	-0.018	14.740	0.003	0.003	0.000	0.000	0.000	0.000
114	A	114	VAL	0	0.017	0.022	17.825	0.001	0.001	0.000	0.000	0.000	0.000
115	A	115	ILE	0	0.060	0.034	20.025	0.005	0.005	0.000	0.000	0.000	0.000
116	A	116	ILE	0	-0.020	-0.008	16.347	0.005	0.005	0.000	0.000	0.000	0.000
117	A	117	SER	0	-0.069	-0.052	16.009	0.004	0.004	0.000	0.000	0.000	0.000
118	A	118	GLU	-1	-0.906	-0.955	17.306	-0.005	-0.005	0.000	0.000	0.000	0.000
119	A	119	ARG	1	0.789	0.858	20.778	0.008	0.008	0.000	0.000	0.000	0.000
120	A	120	LEU	0	-0.026	0.004	14.690	0.004	0.004	0.000	0.000	0.000	0.000
121	A	121	TYR	0	-0.016	-0.007	14.309	0.005	0.005	0.000	0.000	0.000	0.000
122	A	122	SER	0	-0.039	-0.019	19.326	0.004	0.004	0.000	0.000	0.000	0.000
123	A	123	SER	0	-0.042	-0.035	20.662	0.000	0.000	0.000	0.000	0.000	0.000
124	A	124	GLN	0	-0.107	-0.042	17.530	0.000	0.000	0.000	0.000	0.000	0.000
125	A	125	VAL	0	0.026	0.022	21.810	0.002	0.002	0.000	0.000	0.000	0.000

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