FMO DATABASE

FMODB ID: M3YGZ

Calculation Name: 2Z14-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2Z14

Chain ID: A

ChEMBL ID:

UniProt ID: Q5JST6

Base Structure: X-ray

Registration Date: 2023-06-20

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	121
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1040564.521592
FMO2-HF: Nuclear repulsion	991266.958737
FMO2-HF: Total energy	-49297.562855
FMO2-MP2: Total energy	-49444.839716

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:6:SER)

Summations of interaction energy for fragment #1(A:6: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.
-3.523	1.482	0.08	-2.591	-2.495	0.001

Interaction energy analysis for fragmet #1(A:6:SER)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.003 / q_NPA : 0.000

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	8	TRP	0	-0.046	-0.018	3.136	-4.367	0.559	0.081	-2.589	-2.419	0.001
4	A	9	VAL	0	0.015	0.012	5.333	0.405	0.484	-0.001	-0.002	-0.076	0.000
5	A	10	ALA	0	0.011	0.005	8.778	0.073	0.073	0.000	0.000	0.000	0.000
6	A	11	PHE	0	-0.003	-0.002	10.383	0.044	0.044	0.000	0.000	0.000	0.000
7	A	12	ASP	-1	-0.892	-0.955	11.515	-0.059	-0.059	0.000	0.000	0.000	0.000
8	A	13	LYS	1	0.865	0.926	9.695	-0.027	-0.027	0.000	0.000	0.000	0.000
9	A	14	GLN	0	-0.084	-0.041	15.595	0.018	0.018	0.000	0.000	0.000	0.000
10	A	15	VAL	0	-0.018	-0.004	18.448	0.013	0.013	0.000	0.000	0.000	0.000
11	A	16	LEU	0	-0.029	0.001	21.411	-0.011	-0.011	0.000	0.000	0.000	0.000
12	A	17	SER	0	-0.046	-0.046	24.353	0.007	0.007	0.000	0.000	0.000	0.000
13	A	18	PHE	0	0.030	-0.009	27.027	-0.003	-0.003	0.000	0.000	0.000	0.000
14	A	19	ASP	-1	-0.850	-0.905	31.085	-0.010	-0.010	0.000	0.000	0.000	0.000
15	A	20	ALA	0	0.030	-0.007	34.473	0.002	0.002	0.000	0.000	0.000	0.000
16	A	21	TYR	0	-0.023	-0.006	36.657	-0.003	-0.003	0.000	0.000	0.000	0.000
17	A	22	LEU	0	0.017	0.021	39.090	0.003	0.003	0.000	0.000	0.000	0.000
18	A	23	GLU	-1	-0.765	-0.876	41.963	0.012	0.012	0.000	0.000	0.000	0.000
19	A	24	GLU	-1	-0.832	-0.892	44.670	0.016	0.016	0.000	0.000	0.000	0.000
20	A	25	GLU	-1	-0.948	-0.993	46.249	0.015	0.015	0.000	0.000	0.000	0.000
21	A	26	VAL	0	-0.035	-0.018	49.424	0.002	0.002	0.000	0.000	0.000	0.000
22	A	27	LEU	0	-0.006	-0.002	51.729	-0.001	-0.001	0.000	0.000	0.000	0.000
23	A	28	ASP	-1	-0.855	-0.917	54.548	0.013	0.013	0.000	0.000	0.000	0.000
24	A	29	LYS	1	0.839	0.894	57.686	-0.014	-0.014	0.000	0.000	0.000	0.000
25	A	30	SER	0	0.003	0.001	59.155	0.001	0.001	0.000	0.000	0.000	0.000
26	A	31	GLN	0	0.010	0.021	58.669	0.000	0.000	0.000	0.000	0.000	0.000
27	A	32	THR	0	0.018	0.009	52.919	0.001	0.001	0.000	0.000	0.000	0.000
28	A	33	ASN	0	-0.056	-0.021	54.536	-0.001	-0.001	0.000	0.000	0.000	0.000
29	A	34	TYR	0	0.025	-0.002	48.924	0.001	0.001	0.000	0.000	0.000	0.000
30	A	35	ARG	1	0.809	0.893	44.194	-0.010	-0.010	0.000	0.000	0.000	0.000
31	A	36	ILE	0	-0.013	0.000	43.911	0.002	0.002	0.000	0.000	0.000	0.000
32	A	37	ARG	1	0.687	0.810	40.788	-0.014	-0.014	0.000	0.000	0.000	0.000
33	A	38	TYR	0	0.039	0.003	39.069	0.001	0.001	0.000	0.000	0.000	0.000
34	A	39	TYR	0	-0.026	-0.048	34.691	-0.001	-0.001	0.000	0.000	0.000	0.000
35	A	40	LYS	1	0.803	0.912	30.024	0.011	0.011	0.000	0.000	0.000	0.000
36	A	41	ILE	0	-0.016	-0.021	28.958	0.004	0.004	0.000	0.000	0.000	0.000
37	A	42	TYR	0	-0.028	-0.020	24.875	-0.006	-0.006	0.000	0.000	0.000	0.000
38	A	43	PHE	0	0.027	0.016	21.783	0.007	0.007	0.000	0.000	0.000	0.000
39	A	44	TYR	0	-0.003	-0.036	18.979	-0.018	-0.018	0.000	0.000	0.000	0.000
40	A	45	PRO	0	0.011	-0.005	17.334	0.018	0.018	0.000	0.000	0.000	0.000
41	A	46	GLU	-1	-0.922	-0.934	11.601	0.108	0.108	0.000	0.000	0.000	0.000
42	A	47	ASP	-1	-0.788	-0.855	15.165	0.153	0.153	0.000	0.000	0.000	0.000
43	A	48	ASP	-1	-0.816	-0.917	17.480	0.117	0.117	0.000	0.000	0.000	0.000
44	A	49	THR	0	-0.109	-0.059	20.294	-0.010	-0.010	0.000	0.000	0.000	0.000
45	A	50	ILE	0	0.007	0.000	22.560	-0.010	-0.010	0.000	0.000	0.000	0.000
46	A	51	GLN	0	0.001	0.007	25.014	0.004	0.004	0.000	0.000	0.000	0.000
47	A	52	VAL	0	-0.004	0.010	27.400	-0.004	-0.004	0.000	0.000	0.000	0.000
48	A	53	ASN	0	-0.046	-0.020	29.828	-0.002	-0.002	0.000	0.000	0.000	0.000
49	A	54	GLU	-1	-0.672	-0.810	32.754	0.008	0.008	0.000	0.000	0.000	0.000
50	A	55	PRO	0	-0.033	-0.018	34.250	-0.001	-0.001	0.000	0.000	0.000	0.000
51	A	56	GLU	-1	-0.879	-0.917	36.093	-0.004	-0.004	0.000	0.000	0.000	0.000
52	A	57	VAL	0	0.027	0.023	38.991	0.002	0.002	0.000	0.000	0.000	0.000
53	A	58	LYN	0	-0.038	-0.013	39.249	0.002	0.002	0.000	0.000	0.000	0.000
54	A	59	ASN	0	-0.062	-0.040	38.521	0.000	0.000	0.000	0.000	0.000	0.000
55	A	60	SER	0	0.005	-0.007	36.119	0.001	0.001	0.000	0.000	0.000	0.000
56	A	61	GLY	0	-0.004	0.018	39.162	0.001	0.001	0.000	0.000	0.000	0.000
57	A	62	LEU	0	-0.008	-0.027	42.962	0.002	0.002	0.000	0.000	0.000	0.000
58	A	63	LEU	0	-0.024	0.008	41.852	0.001	0.001	0.000	0.000	0.000	0.000
59	A	64	GLN	0	0.041	0.022	40.950	0.001	0.001	0.000	0.000	0.000	0.000
60	A	65	GLY	0	0.043	0.019	38.990	-0.002	-0.002	0.000	0.000	0.000	0.000
61	A	66	THR	0	0.039	0.039	37.250	0.001	0.001	0.000	0.000	0.000	0.000
62	A	67	SER	0	-0.051	-0.034	32.306	-0.001	-0.001	0.000	0.000	0.000	0.000
63	A	68	ILE	0	0.003	0.026	30.353	0.003	0.003	0.000	0.000	0.000	0.000
64	A	69	ARG	1	0.981	0.983	25.610	-0.082	-0.082	0.000	0.000	0.000	0.000
65	A	70	ARG	1	0.874	0.921	17.303	-0.072	-0.072	0.000	0.000	0.000	0.000
66	A	71	HIS	0	-0.058	-0.025	23.936	0.009	0.009	0.000	0.000	0.000	0.000
67	A	72	ARG	1	0.913	0.965	21.617	-0.136	-0.136	0.000	0.000	0.000	0.000
68	A	73	ILE	0	-0.045	-0.014	25.174	-0.001	-0.001	0.000	0.000	0.000	0.000
69	A	74	THR	0	0.045	0.021	28.824	0.002	0.002	0.000	0.000	0.000	0.000
70	A	75	LEU	0	-0.033	-0.009	30.857	-0.007	-0.007	0.000	0.000	0.000	0.000
71	A	76	PRO	0	0.006	0.003	32.993	0.001	0.001	0.000	0.000	0.000	0.000
72	A	77	PRO	0	0.007	0.021	36.656	0.002	0.002	0.000	0.000	0.000	0.000
73	A	78	PRO	0	-0.081	-0.045	39.040	-0.003	-0.003	0.000	0.000	0.000	0.000
74	A	79	ASP	-1	-0.845	-0.943	34.141	0.069	0.069	0.000	0.000	0.000	0.000
75	A	80	GLU	-1	-0.946	-0.978	33.416	0.067	0.067	0.000	0.000	0.000	0.000
76	A	81	ASP	-1	-0.921	-0.953	32.139	0.096	0.096	0.000	0.000	0.000	0.000
77	A	82	GLN	0	-0.107	-0.048	29.048	0.012	0.012	0.000	0.000	0.000	0.000
78	A	83	PHE	0	-0.025	-0.025	25.795	-0.004	-0.004	0.000	0.000	0.000	0.000
79	A	84	TYR	0	0.022	0.021	27.877	-0.001	-0.001	0.000	0.000	0.000	0.000
80	A	85	THR	0	-0.004	-0.013	24.820	0.007	0.007	0.000	0.000	0.000	0.000
81	A	86	VAL	0	0.040	0.002	22.897	-0.009	-0.009	0.000	0.000	0.000	0.000
82	A	87	TYR	0	-0.027	-0.027	23.569	-0.007	-0.007	0.000	0.000	0.000	0.000
83	A	88	HIS	0	0.026	0.040	27.996	-0.003	-0.003	0.000	0.000	0.000	0.000
84	A	89	PHE	0	-0.024	0.000	27.943	-0.004	-0.004	0.000	0.000	0.000	0.000
85	A	90	ASN	0	0.015	0.000	30.685	-0.006	-0.006	0.000	0.000	0.000	0.000
86	A	91	VAL	0	0.023	0.017	33.123	0.000	0.000	0.000	0.000	0.000	0.000
87	A	92	GLY	0	0.006	-0.008	35.919	0.001	0.001	0.000	0.000	0.000	0.000
88	A	93	THR	0	-0.079	-0.024	34.922	0.002	0.002	0.000	0.000	0.000	0.000
89	A	94	GLU	-1	-0.894	-0.958	37.158	0.022	0.022	0.000	0.000	0.000	0.000
90	A	95	VAL	0	-0.027	-0.010	32.455	0.003	0.003	0.000	0.000	0.000	0.000
91	A	96	VAL	0	0.011	-0.001	35.387	-0.003	-0.003	0.000	0.000	0.000	0.000
92	A	97	PHE	0	0.019	0.006	30.842	0.004	0.004	0.000	0.000	0.000	0.000
93	A	98	TYR	0	-0.035	-0.049	31.137	-0.004	-0.004	0.000	0.000	0.000	0.000
94	A	99	GLY	0	0.018	0.012	36.894	-0.003	-0.003	0.000	0.000	0.000	0.000
95	A	100	ARG	1	0.908	0.962	38.708	-0.030	-0.030	0.000	0.000	0.000	0.000
96	A	101	THR	0	0.046	0.016	38.283	0.003	0.003	0.000	0.000	0.000	0.000
97	A	102	PHE	0	-0.031	-0.009	35.940	-0.003	-0.003	0.000	0.000	0.000	0.000
98	A	103	LYS	1	0.880	0.932	37.692	-0.015	-0.015	0.000	0.000	0.000	0.000
99	A	104	ILE	0	-0.012	-0.004	32.764	-0.003	-0.003	0.000	0.000	0.000	0.000
100	A	105	TYR	0	-0.028	-0.018	36.554	0.001	0.001	0.000	0.000	0.000	0.000
101	A	106	ASP	-1	-0.809	-0.892	35.583	-0.013	-0.013	0.000	0.000	0.000	0.000
102	A	107	CYS	0	-0.039	-0.008	30.135	0.004	0.004	0.000	0.000	0.000	0.000
103	A	108	ASP	-1	-0.755	-0.828	27.635	-0.032	-0.032	0.000	0.000	0.000	0.000
104	A	109	ALA	0	0.063	0.009	29.442	0.003	0.003	0.000	0.000	0.000	0.000
105	A	110	PHE	0	-0.022	0.008	19.817	-0.002	-0.002	0.000	0.000	0.000	0.000
106	A	111	THR	0	0.061	0.014	24.866	0.004	0.004	0.000	0.000	0.000	0.000
107	A	112	ARG	1	0.868	0.914	26.410	0.016	0.016	0.000	0.000	0.000	0.000
108	A	113	ASN	0	-0.064	-0.042	24.924	0.004	0.004	0.000	0.000	0.000	0.000
109	A	114	PHE	0	0.013	0.013	18.727	0.001	0.001	0.000	0.000	0.000	0.000
110	A	115	LEU	0	0.063	0.020	23.656	0.008	0.008	0.000	0.000	0.000	0.000
111	A	116	ARG	1	0.895	0.952	26.376	0.031	0.031	0.000	0.000	0.000	0.000
112	A	117	LYS	1	0.891	0.942	19.841	0.061	0.061	0.000	0.000	0.000	0.000
113	A	118	ILE	0	-0.034	0.006	21.409	0.007	0.007	0.000	0.000	0.000	0.000
114	A	119	GLY	0	-0.007	-0.003	23.975	0.008	0.008	0.000	0.000	0.000	0.000
115	A	120	VAL	0	-0.006	0.004	27.491	0.001	0.001	0.000	0.000	0.000	0.000
116	A	121	LYS	1	0.922	0.961	29.501	-0.022	-0.022	0.000	0.000	0.000	0.000
117	A	122	VAL	0	-0.015	-0.011	31.042	0.002	0.002	0.000	0.000	0.000	0.000
118	A	123	ASN	0	-0.057	-0.027	33.560	-0.002	-0.002	0.000	0.000	0.000	0.000
119	A	124	PRO	0	-0.013	-0.013	37.195	-0.003	-0.003	0.000	0.000	0.000	0.000
120	A	125	PRO	0	-0.003	-0.011	39.856	0.001	0.001	0.000	0.000	0.000	0.000
121	A	126	VAL	0	0.026	0.038	40.206	0.001	0.001	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:6:SER)