FMO DATABASE

FMODB ID: MN15Z

Calculation Name: 2XHF-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2XHF

Chain ID: A

ChEMBL ID:

UniProt ID: G1K3P1

Base Structure: X-ray

Registration Date: 2023-09-23

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	OptAll
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	156
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1563269.519002
FMO2-HF: Nuclear repulsion	1501829.258337
FMO2-HF: Total energy	-61440.260665
FMO2-MP2: Total energy	-61617.951043

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:35:GLY)

Summations of interaction energy for fragment #1(A:35:GLY)

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.
-7.008	-5.323	10.451	-5.745	-6.392	-0.043

Interaction energy analysis for fragmet #1(A:35:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.023 / 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

Sort

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	37	PRO	0	-0.034	-0.020	3.851	-0.994	-0.087	0.000	-0.481	-0.426	0.002
4	A	38	ILE	0	0.025	0.010	6.203	0.438	0.438	0.000	0.000	0.000	0.000
5	A	39	LYS	1	0.809	0.887	7.669	0.708	0.708	0.000	0.000	0.000	0.000
6	A	40	VAL	0	0.001	0.004	11.080	0.038	0.038	0.000	0.000	0.000	0.000
7	A	41	GLY	0	-0.013	-0.013	14.290	0.020	0.020	0.000	0.000	0.000	0.000
8	A	42	ASP	-1	-0.825	-0.878	9.460	-0.533	-0.533	0.000	0.000	0.000	0.000
9	A	43	ILE	0	-0.012	-0.010	11.737	-0.009	-0.009	0.000	0.000	0.000	0.000
10	A	44	ILE	0	-0.014	-0.003	9.522	-0.028	-0.028	0.000	0.000	0.000	0.000
11	A	45	PRO	0	0.005	-0.009	5.956	0.113	0.113	0.000	0.000	0.000	0.000
12	A	46	ASP	-1	-0.899	-0.952	8.696	-0.003	-0.003	0.000	0.000	0.000	0.000
13	A	47	VAL	0	0.017	0.013	9.347	0.067	0.067	0.000	0.000	0.000	0.000
14	A	48	LEU	0	-0.014	-0.007	12.411	-0.059	-0.059	0.000	0.000	0.000	0.000
15	A	49	VAL	0	-0.020	-0.003	13.758	-0.026	-0.026	0.000	0.000	0.000	0.000
16	A	50	TYR	0	-0.009	-0.024	16.154	0.019	0.019	0.000	0.000	0.000	0.000
17	A	51	GLU	-1	-0.732	-0.836	19.436	-0.111	-0.111	0.000	0.000	0.000	0.000
18	A	52	ASP	-1	-0.816	-0.897	22.270	-0.053	-0.053	0.000	0.000	0.000	0.000
19	A	53	VAL	0	-0.016	-0.016	24.971	0.002	0.002	0.000	0.000	0.000	0.000
20	A	54	PRO	0	0.009	-0.003	22.463	0.000	0.000	0.000	0.000	0.000	0.000
21	A	55	SER	0	-0.014	-0.007	22.995	0.006	0.006	0.000	0.000	0.000	0.000
22	A	56	LYS	1	0.791	0.892	24.007	0.059	0.059	0.000	0.000	0.000	0.000
23	A	57	SER	0	0.011	-0.001	19.148	-0.008	-0.008	0.000	0.000	0.000	0.000
24	A	58	PHE	0	-0.021	-0.009	18.962	0.006	0.006	0.000	0.000	0.000	0.000
25	A	59	PRO	0	0.056	0.031	16.238	-0.010	-0.010	0.000	0.000	0.000	0.000
26	A	60	ILE	0	0.004	0.008	11.966	-0.016	-0.016	0.000	0.000	0.000	0.000
27	A	61	HIS	0	0.002	-0.012	12.647	-0.017	-0.017	0.000	0.000	0.000	0.000
28	A	62	ASP	-1	-0.811	-0.894	16.668	-0.015	-0.015	0.000	0.000	0.000	0.000
29	A	63	VAL	0	-0.070	-0.027	17.893	0.002	0.002	0.000	0.000	0.000	0.000
30	A	64	PHE	0	0.009	-0.012	15.642	-0.006	-0.006	0.000	0.000	0.000	0.000
31	A	65	ARG	1	0.866	0.928	18.710	0.011	0.011	0.000	0.000	0.000	0.000
32	A	66	GLY	0	-0.051	-0.031	20.977	0.004	0.004	0.000	0.000	0.000	0.000
33	A	67	ARG	1	0.825	0.918	22.419	0.089	0.089	0.000	0.000	0.000	0.000
34	A	68	LYS	1	0.898	0.973	21.565	0.121	0.121	0.000	0.000	0.000	0.000
35	A	69	GLY	0	-0.022	-0.015	20.712	0.015	0.015	0.000	0.000	0.000	0.000
36	A	70	ILE	0	-0.021	-0.011	18.558	-0.022	-0.022	0.000	0.000	0.000	0.000
37	A	71	LEU	0	0.008	0.009	12.307	0.023	0.023	0.000	0.000	0.000	0.000
38	A	72	PHE	0	0.036	0.014	14.894	-0.053	-0.053	0.000	0.000	0.000	0.000
39	A	73	SER	0	0.025	0.013	12.252	0.042	0.042	0.000	0.000	0.000	0.000
40	A	74	VAL	0	-0.056	-0.028	15.039	0.009	0.009	0.000	0.000	0.000	0.000
41	A	75	VAL	0	-0.006	-0.003	15.597	-0.010	-0.010	0.000	0.000	0.000	0.000
42	A	76	GLY	0	0.022	-0.015	16.634	0.010	0.010	0.000	0.000	0.000	0.000
43	A	77	ALA	0	0.015	0.023	18.885	-0.001	-0.001	0.000	0.000	0.000	0.000
44	A	78	PHE	0	0.006	-0.011	22.131	0.006	0.006	0.000	0.000	0.000	0.000
45	A	79	VAL	0	-0.021	0.024	20.203	0.007	0.007	0.000	0.000	0.000	0.000
46	A	80	PRO	0	0.021	0.005	23.200	-0.010	-0.010	0.000	0.000	0.000	0.000
47	A	81	GLY	0	0.004	0.002	22.632	-0.017	-0.017	0.000	0.000	0.000	0.000
48	A	82	SER	0	-0.069	-0.038	21.107	-0.009	-0.009	0.000	0.000	0.000	0.000
49	A	83	ASN	0	0.055	0.004	22.138	-0.010	-0.010	0.000	0.000	0.000	0.000
50	A	84	ASN	0	-0.030	-0.017	23.695	0.014	0.014	0.000	0.000	0.000	0.000
51	A	85	HIS	0	0.077	0.037	20.933	0.019	0.019	0.000	0.000	0.000	0.000
52	A	86	ILE	0	-0.006	0.016	22.189	0.002	0.002	0.000	0.000	0.000	0.000
53	A	87	PRO	0	0.043	0.014	25.172	0.006	0.006	0.000	0.000	0.000	0.000
54	A	88	GLU	-1	-0.781	-0.849	26.570	-0.171	-0.171	0.000	0.000	0.000	0.000
55	A	89	TYR	0	-0.010	-0.037	20.191	0.005	0.005	0.000	0.000	0.000	0.000
56	A	90	LEU	0	-0.018	-0.004	25.954	0.007	0.007	0.000	0.000	0.000	0.000
57	A	91	SER	0	-0.089	-0.049	28.820	0.008	0.008	0.000	0.000	0.000	0.000
58	A	92	LEU	0	0.007	0.005	27.480	0.006	0.006	0.000	0.000	0.000	0.000
59	A	93	TYR	0	0.013	0.006	27.534	0.002	0.002	0.000	0.000	0.000	0.000
60	A	94	ASP	-1	-0.828	-0.919	29.165	-0.088	-0.088	0.000	0.000	0.000	0.000
61	A	95	LYS	1	0.823	0.901	30.045	0.104	0.104	0.000	0.000	0.000	0.000
62	A	96	PHE	0	0.016	-0.004	24.852	-0.002	-0.002	0.000	0.000	0.000	0.000
63	A	97	LYS	1	0.807	0.893	27.733	0.087	0.087	0.000	0.000	0.000	0.000
64	A	98	GLU	-1	-0.858	-0.899	30.003	-0.089	-0.089	0.000	0.000	0.000	0.000
65	A	99	GLU	-1	-0.855	-0.933	27.344	-0.130	-0.130	0.000	0.000	0.000	0.000
66	A	100	GLY	0	-0.018	-0.012	27.558	-0.005	-0.005	0.000	0.000	0.000	0.000
67	A	101	TYR	0	-0.008	-0.009	20.502	0.002	0.002	0.000	0.000	0.000	0.000
68	A	102	HIS	0	0.002	0.008	24.294	-0.011	-0.011	0.000	0.000	0.000	0.000
69	A	103	THR	0	-0.014	0.003	21.606	0.005	0.005	0.000	0.000	0.000	0.000
70	A	104	ILE	0	0.048	0.027	21.224	-0.018	-0.018	0.000	0.000	0.000	0.000
71	A	105	ALA	0	-0.015	-0.007	17.736	0.019	0.019	0.000	0.000	0.000	0.000
72	A	106	CYS	0	-0.029	0.011	18.022	-0.032	-0.032	0.000	0.000	0.000	0.000
73	A	107	ILE	0	-0.022	-0.011	12.140	0.025	0.025	0.000	0.000	0.000	0.000
74	A	108	ALA	0	0.032	0.004	14.879	-0.046	-0.046	0.000	0.000	0.000	0.000
75	A	109	VAL	0	-0.059	-0.006	11.173	0.029	0.029	0.000	0.000	0.000	0.000
76	A	110	ASN	0	-0.006	-0.021	14.311	0.000	0.000	0.000	0.000	0.000	0.000
77	A	111	ASP	-1	-0.746	-0.875	17.701	-0.070	-0.070	0.000	0.000	0.000	0.000
78	A	112	PRO	0	0.037	-0.008	20.169	-0.014	-0.014	0.000	0.000	0.000	0.000
79	A	113	PHE	0	0.007	0.012	22.001	-0.002	-0.002	0.000	0.000	0.000	0.000
80	A	114	VAL	0	-0.006	-0.015	23.260	-0.004	-0.004	0.000	0.000	0.000	0.000
81	A	115	MET	0	-0.020	0.005	18.553	-0.007	-0.007	0.000	0.000	0.000	0.000
82	A	116	ALA	0	0.003	0.009	22.555	-0.006	-0.006	0.000	0.000	0.000	0.000
83	A	117	ALA	0	-0.025	-0.008	25.343	0.002	0.002	0.000	0.000	0.000	0.000
84	A	118	TRP	0	0.041	0.009	21.070	-0.004	-0.004	0.000	0.000	0.000	0.000
85	A	119	GLY	0	0.077	0.027	25.138	-0.002	-0.002	0.000	0.000	0.000	0.000
86	A	120	LYS	1	0.839	0.917	25.775	0.075	0.075	0.000	0.000	0.000	0.000
87	A	121	THR	0	-0.102	-0.061	28.537	0.005	0.005	0.000	0.000	0.000	0.000
88	A	122	VAL	0	-0.060	-0.026	25.112	0.000	0.000	0.000	0.000	0.000	0.000
89	A	123	ASP	-1	-0.781	-0.907	27.055	-0.117	-0.117	0.000	0.000	0.000	0.000
90	A	124	PRO	0	-0.024	-0.008	29.010	0.004	0.004	0.000	0.000	0.000	0.000
91	A	125	GLU	-1	-0.878	-0.926	31.471	-0.080	-0.080	0.000	0.000	0.000	0.000
92	A	126	HIS	0	-0.072	-0.027	26.395	0.003	0.003	0.000	0.000	0.000	0.000
93	A	127	LYS	1	0.809	0.895	28.018	0.094	0.094	0.000	0.000	0.000	0.000
94	A	128	ILE	0	-0.072	-0.023	22.023	-0.009	-0.009	0.000	0.000	0.000	0.000
95	A	129	ARG	1	0.842	0.890	20.783	0.099	0.099	0.000	0.000	0.000	0.000
96	A	130	MET	0	-0.026	0.000	20.869	-0.026	-0.026	0.000	0.000	0.000	0.000
97	A	131	LEU	0	0.010	0.006	16.027	0.018	0.018	0.000	0.000	0.000	0.000
98	A	132	ALA	0	0.045	0.018	16.816	-0.034	-0.034	0.000	0.000	0.000	0.000
99	A	133	ASP	-1	-0.690	-0.841	10.380	-0.291	-0.291	0.000	0.000	0.000	0.000
100	A	134	MET	0	-0.048	-0.019	13.509	-0.018	-0.018	0.000	0.000	0.000	0.000
101	A	135	HIS	0	0.017	0.022	12.342	0.032	0.032	0.000	0.000	0.000	0.000
102	A	136	GLY	0	0.001	0.002	9.937	0.045	0.045	0.000	0.000	0.000	0.000
103	A	137	GLU	-1	-0.934	-0.961	7.731	0.114	0.114	0.000	0.000	0.000	0.000
104	A	138	PHE	0	0.049	0.014	6.721	-0.060	-0.060	0.000	0.000	0.000	0.000
105	A	139	THR	0	-0.058	-0.044	6.308	-0.218	-0.218	0.000	0.000	0.000	0.000
106	A	140	ARG	1	0.802	0.884	3.882	-0.816	-0.474	0.000	-0.166	-0.176	0.000
107	A	141	ALA	0	-0.003	0.006	1.992	-5.880	-6.669	5.904	-2.535	-2.580	-0.030
108	A	142	LEU	0	-0.018	-0.011	2.634	-0.248	1.125	1.975	-1.725	-1.624	-0.014
109	A	143	GLY	0	0.030	0.023	2.570	-2.346	-1.516	2.295	-1.696	-1.429	-0.002
110	A	144	THR	0	-0.043	-0.025	2.956	1.970	0.992	0.277	0.858	-0.157	0.001
111	A	145	GLU	-1	-0.822	-0.892	5.905	0.145	0.145	0.000	0.000	0.000	0.000
112	A	146	LEU	0	-0.020	-0.005	7.767	-0.036	-0.036	0.000	0.000	0.000	0.000
113	A	147	ASP	-1	-0.809	-0.897	11.035	-0.089	-0.089	0.000	0.000	0.000	0.000
114	A	148	SER	0	-0.002	-0.025	13.122	0.024	0.024	0.000	0.000	0.000	0.000
115	A	149	SER	0	0.003	-0.014	14.624	0.035	0.035	0.000	0.000	0.000	0.000
116	A	150	LYS	1	0.806	0.897	16.218	0.139	0.139	0.000	0.000	0.000	0.000
117	A	151	MET	0	-0.041	-0.011	19.602	0.003	0.003	0.000	0.000	0.000	0.000
118	A	152	LEU	0	-0.004	-0.009	17.844	0.004	0.004	0.000	0.000	0.000	0.000
119	A	153	GLY	0	0.011	0.027	19.375	0.001	0.001	0.000	0.000	0.000	0.000
120	A	154	ASN	0	0.001	0.000	14.126	0.033	0.033	0.000	0.000	0.000	0.000
121	A	155	ASN	0	0.025	0.023	10.227	0.010	0.010	0.000	0.000	0.000	0.000
122	A	156	ARG	1	0.857	0.941	12.484	0.214	0.214	0.000	0.000	0.000	0.000
123	A	157	SER	0	0.081	0.014	10.292	-0.169	-0.169	0.000	0.000	0.000	0.000
124	A	158	ARG	1	0.826	0.897	8.946	1.053	1.053	0.000	0.000	0.000	0.000
125	A	159	ARG	1	0.848	0.920	11.886	0.290	0.290	0.000	0.000	0.000	0.000
126	A	160	TYR	0	0.028	0.014	9.542	-0.020	-0.020	0.000	0.000	0.000	0.000
127	A	161	ALA	0	0.011	0.004	13.685	0.061	0.061	0.000	0.000	0.000	0.000
128	A	162	MET	0	-0.013	0.006	9.914	-0.086	-0.086	0.000	0.000	0.000	0.000
129	A	163	LEU	0	-0.024	0.004	14.910	0.049	0.049	0.000	0.000	0.000	0.000
130	A	164	ILE	0	-0.019	-0.004	13.680	-0.028	-0.028	0.000	0.000	0.000	0.000
131	A	165	ASP	-1	-0.822	-0.912	17.241	-0.113	-0.113	0.000	0.000	0.000	0.000
132	A	166	ASP	-1	-0.798	-0.878	18.916	-0.067	-0.067	0.000	0.000	0.000	0.000
133	A	167	ASN	0	-0.014	-0.004	14.966	-0.008	-0.008	0.000	0.000	0.000	0.000
134	A	168	LYS	1	0.835	0.915	14.104	0.086	0.086	0.000	0.000	0.000	0.000
135	A	169	ILE	0	0.028	0.008	9.657	0.004	0.004	0.000	0.000	0.000	0.000
136	A	170	ARG	1	0.811	0.869	14.172	0.175	0.175	0.000	0.000	0.000	0.000
137	A	171	SER	0	-0.011	-0.014	16.127	0.000	0.000	0.000	0.000	0.000	0.000
138	A	172	VAL	0	0.007	-0.003	10.973	-0.019	-0.019	0.000	0.000	0.000	0.000
139	A	173	SER	0	0.018	0.031	14.211	0.016	0.016	0.000	0.000	0.000	0.000
140	A	174	THR	0	0.018	-0.007	12.396	-0.076	-0.076	0.000	0.000	0.000	0.000
141	A	175	GLU	-1	-0.824	-0.892	15.244	-0.287	-0.287	0.000	0.000	0.000	0.000
142	A	176	PRO	0	-0.005	-0.003	18.302	-0.017	-0.017	0.000	0.000	0.000	0.000
143	A	177	ASP	-1	-0.897	-0.946	19.625	-0.271	-0.271	0.000	0.000	0.000	0.000
144	A	178	ILE	0	-0.047	-0.037	16.327	-0.017	-0.017	0.000	0.000	0.000	0.000
145	A	179	THR	0	-0.019	-0.012	19.431	0.008	0.008	0.000	0.000	0.000	0.000
146	A	180	GLY	0	0.052	0.026	22.675	-0.010	-0.010	0.000	0.000	0.000	0.000
147	A	181	LEU	0	0.002	-0.015	24.613	0.002	0.002	0.000	0.000	0.000	0.000
148	A	182	ALA	0	0.008	0.011	22.334	0.004	0.004	0.000	0.000	0.000	0.000
149	A	183	CYS	0	0.004	0.018	20.948	-0.012	-0.012	0.000	0.000	0.000	0.000
150	A	184	LEU	0	0.001	0.003	22.215	0.004	0.004	0.000	0.000	0.000	0.000
151	A	185	LEU	0	-0.012	-0.012	25.568	0.010	0.010	0.000	0.000	0.000	0.000
152	A	186	SER	0	-0.040	-0.028	21.055	0.000	0.000	0.000	0.000	0.000	0.000
153	A	187	ILE	0	-0.062	-0.022	22.586	0.003	0.003	0.000	0.000	0.000	0.000
154	A	188	GLN	0	0.073	0.022	24.398	0.009	0.009	0.000	0.000	0.000	0.000
155	A	189	ARG	1	0.848	0.940	25.232	0.174	0.174	0.000	0.000	0.000	0.000
156	A	190	GLN	0	-0.041	-0.003	22.515	0.009	0.009	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:35:GLY)