FMO DATABASE

FMODB ID: 9G9J2

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1040199.696225
FMO2-HF: Nuclear repulsion	990902.457074
FMO2-HF: Total energy	-49297.239151
FMO2-MP2: Total energy	-49444.491253

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.
-3.219	1.873	0.194	-2.666	-2.62	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 : -0.002 / q_NPA : -0.001

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	-0.042	-0.017	2.870	-3.915	1.098	0.195	-2.664	-2.544	0.001
4	A	9	VAL	0	0.016	0.013	5.360	0.381	0.460	-0.001	-0.002	-0.076	0.000
5	A	10	ALA	0	0.005	0.003	8.789	0.062	0.062	0.000	0.000	0.000	0.000
6	A	11	PHE	0	-0.006	-0.001	10.386	0.043	0.043	0.000	0.000	0.000	0.000
7	A	12	ASP	-1	-0.896	-0.960	11.254	-0.107	-0.107	0.000	0.000	0.000	0.000
8	A	13	LYS	1	0.944	0.975	10.525	-0.101	-0.101	0.000	0.000	0.000	0.000
9	A	14	GLN	0	-0.064	-0.027	15.568	0.022	0.022	0.000	0.000	0.000	0.000
10	A	15	VAL	0	-0.012	-0.005	18.425	0.013	0.013	0.000	0.000	0.000	0.000
11	A	16	LEU	0	-0.046	-0.001	21.473	-0.010	-0.010	0.000	0.000	0.000	0.000
12	A	17	SER	0	-0.011	-0.023	24.361	0.006	0.006	0.000	0.000	0.000	0.000
13	A	18	PHE	0	-0.001	-0.019	27.003	-0.003	-0.003	0.000	0.000	0.000	0.000
14	A	19	ASP	-1	-0.877	-0.928	31.152	-0.011	-0.011	0.000	0.000	0.000	0.000
15	A	20	ALA	0	0.019	-0.016	34.537	0.002	0.002	0.000	0.000	0.000	0.000
16	A	21	TYR	0	-0.026	-0.007	36.721	-0.002	-0.002	0.000	0.000	0.000	0.000
17	A	22	LEU	0	0.007	0.016	39.124	0.002	0.002	0.000	0.000	0.000	0.000
18	A	23	GLU	-1	-0.820	-0.925	42.022	0.010	0.010	0.000	0.000	0.000	0.000
19	A	24	GLU	-1	-0.914	-0.953	45.030	0.015	0.015	0.000	0.000	0.000	0.000
20	A	25	GLU	-1	-0.960	-1.002	46.302	0.014	0.014	0.000	0.000	0.000	0.000
21	A	26	VAL	0	-0.021	-0.010	49.478	0.001	0.001	0.000	0.000	0.000	0.000
22	A	27	LEU	0	-0.017	-0.007	51.780	-0.001	-0.001	0.000	0.000	0.000	0.000
23	A	28	ASP	-1	-0.917	-0.955	54.600	0.012	0.012	0.000	0.000	0.000	0.000
24	A	29	LYS	1	0.909	0.936	57.735	-0.014	-0.014	0.000	0.000	0.000	0.000
25	A	30	SER	0	-0.018	-0.010	59.207	0.001	0.001	0.000	0.000	0.000	0.000
26	A	31	GLN	0	0.017	0.014	58.672	0.000	0.000	0.000	0.000	0.000	0.000
27	A	32	THR	0	0.019	0.013	52.909	0.001	0.001	0.000	0.000	0.000	0.000
28	A	33	ASN	0	-0.040	-0.004	54.590	-0.001	-0.001	0.000	0.000	0.000	0.000
29	A	34	TYR	0	0.024	-0.003	49.058	0.001	0.001	0.000	0.000	0.000	0.000
30	A	35	ARG	1	0.879	0.951	44.365	-0.008	-0.008	0.000	0.000	0.000	0.000
31	A	36	ILE	0	0.004	0.005	43.882	0.002	0.002	0.000	0.000	0.000	0.000
32	A	37	ARG	1	0.716	0.849	40.839	-0.012	-0.012	0.000	0.000	0.000	0.000
33	A	38	TYR	0	0.045	0.007	39.151	0.001	0.001	0.000	0.000	0.000	0.000
34	A	39	TYR	0	-0.028	-0.045	34.699	0.000	0.000	0.000	0.000	0.000	0.000
35	A	40	LYS	1	0.896	0.977	29.894	0.016	0.016	0.000	0.000	0.000	0.000
36	A	41	ILE	0	-0.014	-0.019	28.930	0.003	0.003	0.000	0.000	0.000	0.000
37	A	42	TYR	0	-0.029	-0.025	24.854	-0.007	-0.007	0.000	0.000	0.000	0.000
38	A	43	PHE	0	0.032	0.016	21.747	0.007	0.007	0.000	0.000	0.000	0.000
39	A	44	TYR	0	-0.012	-0.036	19.011	-0.018	-0.018	0.000	0.000	0.000	0.000
40	A	45	PRO	0	0.006	-0.012	17.539	0.018	0.018	0.000	0.000	0.000	0.000
41	A	46	GLU	-1	-0.995	-0.982	11.759	0.108	0.108	0.000	0.000	0.000	0.000
42	A	47	ASP	-1	-0.803	-0.879	15.228	0.146	0.146	0.000	0.000	0.000	0.000
43	A	48	ASP	-1	-0.871	-0.941	17.538	0.115	0.115	0.000	0.000	0.000	0.000
44	A	49	THR	0	-0.095	-0.052	20.257	-0.010	-0.010	0.000	0.000	0.000	0.000
45	A	50	ILE	0	0.015	0.002	22.615	-0.010	-0.010	0.000	0.000	0.000	0.000
46	A	51	GLN	0	-0.012	-0.002	25.270	0.002	0.002	0.000	0.000	0.000	0.000
47	A	52	VAL	0	0.001	0.014	27.449	-0.004	-0.004	0.000	0.000	0.000	0.000
48	A	53	ASN	0	-0.039	-0.020	30.142	0.000	0.000	0.000	0.000	0.000	0.000
49	A	54	GLU	-1	-0.672	-0.818	32.800	0.006	0.006	0.000	0.000	0.000	0.000
50	A	55	PRO	0	-0.042	-0.025	34.177	-0.001	-0.001	0.000	0.000	0.000	0.000
51	A	56	GLU	-1	-0.865	-0.912	36.138	-0.004	-0.004	0.000	0.000	0.000	0.000
52	A	57	VAL	0	0.024	0.026	39.030	0.002	0.002	0.000	0.000	0.000	0.000
53	A	58	LYN	0	-0.056	-0.041	39.322	0.002	0.002	0.000	0.000	0.000	0.000
54	A	59	ASN	0	-0.062	-0.039	38.352	0.000	0.000	0.000	0.000	0.000	0.000
55	A	60	SER	0	-0.008	-0.002	36.381	0.003	0.003	0.000	0.000	0.000	0.000
56	A	61	GLY	0	0.002	0.007	38.876	0.000	0.000	0.000	0.000	0.000	0.000
57	A	62	LEU	0	-0.008	-0.024	41.646	0.002	0.002	0.000	0.000	0.000	0.000
58	A	63	LEU	0	-0.024	0.011	41.699	0.001	0.001	0.000	0.000	0.000	0.000
59	A	64	GLN	0	0.040	0.020	40.984	0.001	0.001	0.000	0.000	0.000	0.000
60	A	65	GLY	0	0.037	0.010	39.033	-0.002	-0.002	0.000	0.000	0.000	0.000
61	A	66	THR	0	0.023	0.032	37.280	0.001	0.001	0.000	0.000	0.000	0.000
62	A	67	SER	0	-0.051	-0.030	32.391	-0.001	-0.001	0.000	0.000	0.000	0.000
63	A	68	ILE	0	0.022	0.033	30.155	0.003	0.003	0.000	0.000	0.000	0.000
64	A	69	ARG	1	0.976	0.979	26.051	-0.076	-0.076	0.000	0.000	0.000	0.000
65	A	70	ARG	1	0.895	0.946	17.456	-0.062	-0.062	0.000	0.000	0.000	0.000
66	A	71	HIS	0	-0.055	-0.026	23.978	0.009	0.009	0.000	0.000	0.000	0.000
67	A	72	ARG	1	0.946	0.993	21.592	-0.130	-0.130	0.000	0.000	0.000	0.000
68	A	73	ILE	0	-0.039	-0.007	25.225	-0.001	-0.001	0.000	0.000	0.000	0.000
69	A	74	THR	0	0.031	0.014	28.878	0.002	0.002	0.000	0.000	0.000	0.000
70	A	75	LEU	0	-0.031	-0.006	30.913	-0.006	-0.006	0.000	0.000	0.000	0.000
71	A	76	PRO	0	0.007	0.003	33.055	0.001	0.001	0.000	0.000	0.000	0.000
72	A	77	PRO	0	0.002	0.021	36.716	0.002	0.002	0.000	0.000	0.000	0.000
73	A	78	PRO	0	-0.073	-0.048	39.099	-0.003	-0.003	0.000	0.000	0.000	0.000
74	A	79	ASP	-1	-0.871	-0.946	34.194	0.064	0.064	0.000	0.000	0.000	0.000
75	A	80	GLU	-1	-0.957	-0.987	33.477	0.063	0.063	0.000	0.000	0.000	0.000
76	A	81	ASP	-1	-0.957	-0.975	32.179	0.090	0.090	0.000	0.000	0.000	0.000
77	A	82	GLN	0	-0.031	-0.010	29.106	0.012	0.012	0.000	0.000	0.000	0.000
78	A	83	PHE	0	-0.019	-0.021	25.404	-0.003	-0.003	0.000	0.000	0.000	0.000
79	A	84	TYR	0	0.030	0.021	27.942	-0.001	-0.001	0.000	0.000	0.000	0.000
80	A	85	THR	0	-0.012	-0.016	24.909	0.006	0.006	0.000	0.000	0.000	0.000
81	A	86	VAL	0	0.038	0.001	23.020	-0.008	-0.008	0.000	0.000	0.000	0.000
82	A	87	TYR	0	-0.024	-0.027	22.625	-0.011	-0.011	0.000	0.000	0.000	0.000
83	A	88	HIS	0	0.030	0.041	28.058	-0.003	-0.003	0.000	0.000	0.000	0.000
84	A	89	PHE	0	-0.033	-0.004	27.892	-0.004	-0.004	0.000	0.000	0.000	0.000
85	A	90	ASN	0	0.016	0.001	30.655	-0.006	-0.006	0.000	0.000	0.000	0.000
86	A	91	VAL	0	0.020	0.016	33.095	0.000	0.000	0.000	0.000	0.000	0.000
87	A	92	GLY	0	-0.001	-0.016	35.894	0.001	0.001	0.000	0.000	0.000	0.000
88	A	93	THR	0	-0.070	-0.019	35.069	0.002	0.002	0.000	0.000	0.000	0.000
89	A	94	GLU	-1	-0.920	-0.965	37.230	0.020	0.020	0.000	0.000	0.000	0.000
90	A	95	VAL	0	-0.027	-0.006	32.522	0.003	0.003	0.000	0.000	0.000	0.000
91	A	96	VAL	0	0.009	-0.004	35.432	-0.003	-0.003	0.000	0.000	0.000	0.000
92	A	97	PHE	0	0.020	0.008	30.937	0.004	0.004	0.000	0.000	0.000	0.000
93	A	98	TYR	0	-0.040	-0.053	31.199	-0.003	-0.003	0.000	0.000	0.000	0.000
94	A	99	GLY	0	0.020	0.012	36.944	-0.002	-0.002	0.000	0.000	0.000	0.000
95	A	100	ARG	1	0.905	0.959	38.762	-0.029	-0.029	0.000	0.000	0.000	0.000
96	A	101	THR	0	0.049	0.018	38.341	0.003	0.003	0.000	0.000	0.000	0.000
97	A	102	PHE	0	-0.036	-0.011	36.017	-0.003	-0.003	0.000	0.000	0.000	0.000
98	A	103	LYS	1	0.937	0.972	37.759	-0.014	-0.014	0.000	0.000	0.000	0.000
99	A	104	ILE	0	-0.001	0.002	32.731	-0.003	-0.003	0.000	0.000	0.000	0.000
100	A	105	TYR	0	-0.035	-0.021	36.623	0.001	0.001	0.000	0.000	0.000	0.000
101	A	106	ASP	-1	-0.833	-0.899	35.568	-0.015	-0.015	0.000	0.000	0.000	0.000
102	A	107	CYS	0	-0.026	-0.003	30.123	0.003	0.003	0.000	0.000	0.000	0.000
103	A	108	ASP	-1	-0.758	-0.849	27.892	-0.036	-0.036	0.000	0.000	0.000	0.000
104	A	109	ALA	0	0.038	-0.001	29.385	0.002	0.002	0.000	0.000	0.000	0.000
105	A	110	PHE	0	-0.035	-0.008	19.797	-0.002	-0.002	0.000	0.000	0.000	0.000
106	A	111	THR	0	0.059	0.010	24.855	0.003	0.003	0.000	0.000	0.000	0.000
107	A	112	ARG	1	0.874	0.915	26.393	0.019	0.019	0.000	0.000	0.000	0.000
108	A	113	ASN	0	-0.049	-0.034	25.105	0.007	0.007	0.000	0.000	0.000	0.000
109	A	114	PHE	0	0.011	0.010	18.828	0.000	0.000	0.000	0.000	0.000	0.000
110	A	115	LEU	0	0.065	0.019	23.644	0.008	0.008	0.000	0.000	0.000	0.000
111	A	116	ARG	1	0.910	0.971	25.777	0.035	0.035	0.000	0.000	0.000	0.000
112	A	117	LYS	1	0.866	0.926	20.362	0.066	0.066	0.000	0.000	0.000	0.000
113	A	118	ILE	0	-0.033	0.013	21.472	0.005	0.005	0.000	0.000	0.000	0.000
114	A	119	GLY	0	0.002	0.001	23.958	0.008	0.008	0.000	0.000	0.000	0.000
115	A	120	VAL	0	0.000	0.007	27.434	0.002	0.002	0.000	0.000	0.000	0.000
116	A	121	LYS	1	0.922	0.960	29.482	-0.018	-0.018	0.000	0.000	0.000	0.000
117	A	122	VAL	0	-0.017	-0.011	31.077	0.002	0.002	0.000	0.000	0.000	0.000
118	A	123	ASN	0	-0.057	-0.021	33.543	-0.002	-0.002	0.000	0.000	0.000	0.000
119	A	124	PRO	0	-0.018	-0.015	37.176	-0.003	-0.003	0.000	0.000	0.000	0.000
120	A	125	PRO	0	0.005	-0.008	39.839	0.001	0.001	0.000	0.000	0.000	0.000
121	A	126	VAL	0	0.031	0.037	40.249	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)