FMO DATABASE

FMODB ID: 98V32

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1557600.717567
FMO2-HF: Nuclear repulsion	1496160.53005
FMO2-HF: Total energy	-61440.187517
FMO2-MP2: Total energy	-61617.801617

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.
-6.864	-2.7	5.328	-4.156	-5.338	-0.027

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 : 0.026 / 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

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	-0.021	-0.020	3.795	-1.287	-0.213	-0.009	-0.586	-0.479	0.004
4	A	38	ILE	0	0.026	0.020	5.952	0.416	0.416	0.000	0.000	0.000	0.000
5	A	39	LYS	1	0.846	0.905	7.484	0.665	0.665	0.000	0.000	0.000	0.000
6	A	40	VAL	0	0.000	0.003	10.934	0.046	0.046	0.000	0.000	0.000	0.000
7	A	41	GLY	0	-0.020	-0.009	14.167	0.031	0.031	0.000	0.000	0.000	0.000
8	A	42	ASP	-1	-0.843	-0.900	9.095	-0.497	-0.497	0.000	0.000	0.000	0.000
9	A	43	ILE	0	-0.025	-0.015	11.376	-0.012	-0.012	0.000	0.000	0.000	0.000
10	A	44	ILE	0	-0.020	-0.006	9.314	-0.038	-0.038	0.000	0.000	0.000	0.000
11	A	45	PRO	0	0.010	-0.001	5.990	0.126	0.126	0.000	0.000	0.000	0.000
12	A	46	ASP	-1	-0.913	-0.951	8.773	-0.048	-0.048	0.000	0.000	0.000	0.000
13	A	47	VAL	0	0.023	0.008	9.321	0.050	0.050	0.000	0.000	0.000	0.000
14	A	48	LEU	0	-0.009	-0.003	12.400	-0.042	-0.042	0.000	0.000	0.000	0.000
15	A	49	VAL	0	-0.020	-0.004	13.846	-0.031	-0.031	0.000	0.000	0.000	0.000
16	A	50	TYR	0	-0.012	-0.027	16.213	0.029	0.029	0.000	0.000	0.000	0.000
17	A	51	GLU	-1	-0.764	-0.854	19.557	-0.138	-0.138	0.000	0.000	0.000	0.000
18	A	52	ASP	-1	-0.859	-0.933	22.275	-0.075	-0.075	0.000	0.000	0.000	0.000
19	A	53	VAL	0	-0.025	-0.021	25.186	0.003	0.003	0.000	0.000	0.000	0.000
20	A	54	PRO	0	0.025	0.003	22.675	-0.001	-0.001	0.000	0.000	0.000	0.000
21	A	55	SER	0	-0.014	-0.005	23.040	0.003	0.003	0.000	0.000	0.000	0.000
22	A	56	LYS	1	0.806	0.915	24.099	0.088	0.088	0.000	0.000	0.000	0.000
23	A	57	SER	0	0.009	-0.002	19.392	-0.009	-0.009	0.000	0.000	0.000	0.000
24	A	58	PHE	0	-0.016	-0.008	19.279	0.010	0.010	0.000	0.000	0.000	0.000
25	A	59	PRO	0	0.046	0.031	16.262	-0.019	-0.019	0.000	0.000	0.000	0.000
26	A	60	ILE	0	0.027	0.016	12.168	-0.005	-0.005	0.000	0.000	0.000	0.000
27	A	61	HIS	0	-0.005	-0.014	12.511	-0.002	-0.002	0.000	0.000	0.000	0.000
28	A	62	ASP	-1	-0.827	-0.907	16.641	-0.042	-0.042	0.000	0.000	0.000	0.000
29	A	63	VAL	0	-0.089	-0.033	18.081	0.005	0.005	0.000	0.000	0.000	0.000
30	A	64	PHE	0	0.010	-0.021	15.856	-0.002	-0.002	0.000	0.000	0.000	0.000
31	A	65	ARG	1	0.873	0.939	19.012	0.048	0.048	0.000	0.000	0.000	0.000
32	A	66	GLY	0	-0.041	-0.028	20.988	0.003	0.003	0.000	0.000	0.000	0.000
33	A	67	ARG	1	0.854	0.941	22.192	0.113	0.113	0.000	0.000	0.000	0.000
34	A	68	LYS	1	0.911	0.967	21.364	0.125	0.125	0.000	0.000	0.000	0.000
35	A	69	GLY	0	-0.007	-0.019	20.410	0.015	0.015	0.000	0.000	0.000	0.000
36	A	70	ILE	0	-0.031	-0.012	18.554	-0.021	-0.021	0.000	0.000	0.000	0.000
37	A	71	LEU	0	0.009	0.014	12.321	0.022	0.022	0.000	0.000	0.000	0.000
38	A	72	PHE	0	0.032	0.009	15.113	-0.047	-0.047	0.000	0.000	0.000	0.000
39	A	73	SER	0	0.023	0.027	12.325	0.050	0.050	0.000	0.000	0.000	0.000
40	A	74	VAL	0	-0.057	-0.026	14.879	0.024	0.024	0.000	0.000	0.000	0.000
41	A	75	VAL	0	-0.015	-0.008	15.717	-0.019	-0.019	0.000	0.000	0.000	0.000
42	A	76	GLY	0	0.026	-0.015	16.787	0.003	0.003	0.000	0.000	0.000	0.000
43	A	77	ALA	0	0.035	0.031	19.185	0.007	0.007	0.000	0.000	0.000	0.000
44	A	78	PHE	0	-0.013	-0.023	22.304	0.006	0.006	0.000	0.000	0.000	0.000
45	A	79	VAL	0	-0.019	0.022	20.513	0.010	0.010	0.000	0.000	0.000	0.000
46	A	80	PRO	0	0.029	0.019	23.475	-0.009	-0.009	0.000	0.000	0.000	0.000
47	A	81	GLY	0	0.023	0.005	23.065	-0.016	-0.016	0.000	0.000	0.000	0.000
48	A	82	SER	0	-0.079	-0.048	21.317	-0.009	-0.009	0.000	0.000	0.000	0.000
49	A	83	ASN	0	0.031	-0.004	22.299	-0.009	-0.009	0.000	0.000	0.000	0.000
50	A	84	ASN	0	-0.016	-0.010	23.732	0.019	0.019	0.000	0.000	0.000	0.000
51	A	85	HIS	0	0.069	0.027	20.866	0.020	0.020	0.000	0.000	0.000	0.000
52	A	86	ILE	0	0.009	0.023	22.407	0.002	0.002	0.000	0.000	0.000	0.000
53	A	87	PRO	0	0.034	0.019	25.097	0.007	0.007	0.000	0.000	0.000	0.000
54	A	88	GLU	-1	-0.789	-0.877	26.594	-0.173	-0.173	0.000	0.000	0.000	0.000
55	A	89	TYR	0	0.011	-0.009	20.202	0.002	0.002	0.000	0.000	0.000	0.000
56	A	90	LEU	0	-0.016	-0.005	25.984	0.007	0.007	0.000	0.000	0.000	0.000
57	A	91	SER	0	-0.083	-0.041	28.840	0.010	0.010	0.000	0.000	0.000	0.000
58	A	92	LEU	0	-0.008	-0.004	27.375	0.008	0.008	0.000	0.000	0.000	0.000
59	A	93	TYR	0	0.033	0.021	27.743	0.003	0.003	0.000	0.000	0.000	0.000
60	A	94	ASP	-1	-0.831	-0.924	29.476	-0.098	-0.098	0.000	0.000	0.000	0.000
61	A	95	LYS	1	0.829	0.904	30.156	0.110	0.110	0.000	0.000	0.000	0.000
62	A	96	PHE	0	0.018	0.006	25.110	-0.003	-0.003	0.000	0.000	0.000	0.000
63	A	97	LYS	1	0.821	0.898	27.746	0.097	0.097	0.000	0.000	0.000	0.000
64	A	98	GLU	-1	-0.867	-0.906	29.744	-0.096	-0.096	0.000	0.000	0.000	0.000
65	A	99	GLU	-1	-0.868	-0.927	27.647	-0.124	-0.124	0.000	0.000	0.000	0.000
66	A	100	GLY	0	-0.050	-0.023	27.645	-0.004	-0.004	0.000	0.000	0.000	0.000
67	A	101	TYR	0	-0.036	-0.014	20.655	0.000	0.000	0.000	0.000	0.000	0.000
68	A	102	HIS	0	0.036	0.010	24.918	-0.009	-0.009	0.000	0.000	0.000	0.000
69	A	103	THR	0	-0.047	-0.007	21.338	0.005	0.005	0.000	0.000	0.000	0.000
70	A	104	ILE	0	0.045	0.028	21.108	-0.019	-0.019	0.000	0.000	0.000	0.000
71	A	105	ALA	0	-0.011	-0.001	17.735	0.018	0.018	0.000	0.000	0.000	0.000
72	A	106	CYS	0	-0.024	0.008	17.901	-0.032	-0.032	0.000	0.000	0.000	0.000
73	A	107	ILE	0	-0.002	-0.001	12.261	0.027	0.027	0.000	0.000	0.000	0.000
74	A	108	ALA	0	0.023	-0.002	14.957	-0.041	-0.041	0.000	0.000	0.000	0.000
75	A	109	VAL	0	-0.035	0.005	11.709	0.027	0.027	0.000	0.000	0.000	0.000
76	A	110	ASN	0	-0.005	-0.021	14.826	0.000	0.000	0.000	0.000	0.000	0.000
77	A	111	ASP	-1	-0.773	-0.892	18.187	-0.102	-0.102	0.000	0.000	0.000	0.000
78	A	112	PRO	0	0.035	-0.002	20.502	-0.011	-0.011	0.000	0.000	0.000	0.000
79	A	113	PHE	0	0.023	0.018	22.404	0.001	0.001	0.000	0.000	0.000	0.000
80	A	114	VAL	0	-0.017	-0.013	23.170	-0.003	-0.003	0.000	0.000	0.000	0.000
81	A	115	MET	0	-0.033	-0.007	18.702	-0.002	-0.002	0.000	0.000	0.000	0.000
82	A	116	ALA	0	0.012	0.009	22.866	-0.003	-0.003	0.000	0.000	0.000	0.000
83	A	117	ALA	0	-0.032	-0.014	25.710	0.003	0.003	0.000	0.000	0.000	0.000
84	A	118	TRP	0	0.050	0.012	21.333	-0.003	-0.003	0.000	0.000	0.000	0.000
85	A	119	GLY	0	0.050	0.027	25.512	-0.001	-0.001	0.000	0.000	0.000	0.000
86	A	120	LYS	1	0.889	0.948	26.123	0.097	0.097	0.000	0.000	0.000	0.000
87	A	121	THR	0	-0.098	-0.054	28.669	0.004	0.004	0.000	0.000	0.000	0.000
88	A	122	VAL	0	-0.052	-0.021	25.299	0.002	0.002	0.000	0.000	0.000	0.000
89	A	123	ASP	-1	-0.781	-0.901	27.078	-0.137	-0.137	0.000	0.000	0.000	0.000
90	A	124	PRO	0	-0.007	0.007	29.163	0.004	0.004	0.000	0.000	0.000	0.000
91	A	125	GLU	-1	-0.929	-0.963	31.848	-0.090	-0.090	0.000	0.000	0.000	0.000
92	A	126	HIS	0	-0.073	-0.031	26.316	0.001	0.001	0.000	0.000	0.000	0.000
93	A	127	LYS	1	0.843	0.921	28.043	0.105	0.105	0.000	0.000	0.000	0.000
94	A	128	ILE	0	-0.057	-0.022	21.990	-0.010	-0.010	0.000	0.000	0.000	0.000
95	A	129	ARG	1	0.817	0.878	21.093	0.130	0.130	0.000	0.000	0.000	0.000
96	A	130	MET	0	-0.005	0.006	20.745	-0.030	-0.030	0.000	0.000	0.000	0.000
97	A	131	LEU	0	0.001	-0.003	16.406	0.019	0.019	0.000	0.000	0.000	0.000
98	A	132	ALA	0	0.037	0.009	17.119	-0.033	-0.033	0.000	0.000	0.000	0.000
99	A	133	ASP	-1	-0.701	-0.844	10.653	-0.422	-0.422	0.000	0.000	0.000	0.000
100	A	134	MET	0	-0.036	-0.007	13.632	-0.019	-0.019	0.000	0.000	0.000	0.000
101	A	135	HIS	0	0.021	0.023	12.854	0.014	0.014	0.000	0.000	0.000	0.000
102	A	136	GLY	0	-0.001	0.000	10.523	0.037	0.037	0.000	0.000	0.000	0.000
103	A	137	GLU	-1	-0.943	-0.967	8.290	-0.034	-0.034	0.000	0.000	0.000	0.000
104	A	138	PHE	0	0.050	0.011	7.143	-0.099	-0.099	0.000	0.000	0.000	0.000
105	A	139	THR	0	-0.052	-0.048	6.420	-0.243	-0.243	0.000	0.000	0.000	0.000
106	A	140	ARG	1	0.820	0.895	4.363	-0.554	-0.427	-0.001	-0.035	-0.091	0.000
107	A	141	ALA	0	-0.027	-0.004	2.368	-5.334	-3.597	1.260	-1.339	-1.658	-0.017
108	A	142	LEU	0	-0.023	-0.016	2.592	-0.469	1.113	1.864	-1.731	-1.716	-0.014
109	A	143	GLY	0	0.021	0.026	2.643	-2.407	-1.697	1.949	-1.403	-1.256	-0.001
110	A	144	THR	0	-0.046	-0.023	2.947	2.206	1.140	0.265	0.938	-0.138	0.001
111	A	145	GLU	-1	-0.796	-0.893	5.857	0.104	0.104	0.000	0.000	0.000	0.000
112	A	146	LEU	0	-0.050	-0.015	7.752	-0.015	-0.015	0.000	0.000	0.000	0.000
113	A	147	ASP	-1	-0.844	-0.920	11.089	-0.120	-0.120	0.000	0.000	0.000	0.000
114	A	148	SER	0	0.007	-0.022	12.887	0.011	0.011	0.000	0.000	0.000	0.000
115	A	149	SER	0	0.012	0.001	14.765	0.033	0.033	0.000	0.000	0.000	0.000
116	A	150	LYS	1	0.849	0.919	16.397	0.138	0.138	0.000	0.000	0.000	0.000
117	A	151	MET	0	-0.039	-0.006	19.497	0.002	0.002	0.000	0.000	0.000	0.000
118	A	152	LEU	0	-0.010	-0.015	17.790	0.005	0.005	0.000	0.000	0.000	0.000
119	A	153	GLY	0	0.012	0.020	19.712	0.001	0.001	0.000	0.000	0.000	0.000
120	A	154	ASN	0	0.027	0.022	14.680	0.026	0.026	0.000	0.000	0.000	0.000
121	A	155	ASN	0	-0.024	-0.004	10.080	0.030	0.030	0.000	0.000	0.000	0.000
122	A	156	ARG	1	0.901	0.960	12.293	0.221	0.221	0.000	0.000	0.000	0.000
123	A	157	SER	0	0.058	0.006	10.483	-0.155	-0.155	0.000	0.000	0.000	0.000
124	A	158	ARG	1	0.831	0.905	8.822	1.052	1.052	0.000	0.000	0.000	0.000
125	A	159	ARG	1	0.844	0.912	11.977	0.330	0.330	0.000	0.000	0.000	0.000
126	A	160	TYR	0	0.038	0.011	9.490	-0.023	-0.023	0.000	0.000	0.000	0.000
127	A	161	ALA	0	0.008	0.001	13.451	0.057	0.057	0.000	0.000	0.000	0.000
128	A	162	MET	0	-0.017	0.000	9.949	-0.063	-0.063	0.000	0.000	0.000	0.000
129	A	163	LEU	0	-0.009	0.009	15.015	0.044	0.044	0.000	0.000	0.000	0.000
130	A	164	ILE	0	-0.024	-0.008	13.396	-0.028	-0.028	0.000	0.000	0.000	0.000
131	A	165	ASP	-1	-0.827	-0.912	17.087	-0.120	-0.120	0.000	0.000	0.000	0.000
132	A	166	ASP	-1	-0.812	-0.896	18.665	-0.087	-0.087	0.000	0.000	0.000	0.000
133	A	167	ASN	0	-0.016	-0.012	14.925	-0.006	-0.006	0.000	0.000	0.000	0.000
134	A	168	LYS	1	0.871	0.944	13.944	0.097	0.097	0.000	0.000	0.000	0.000
135	A	169	ILE	0	0.012	0.005	9.570	-0.003	-0.003	0.000	0.000	0.000	0.000
136	A	170	ARG	1	0.812	0.871	14.095	0.200	0.200	0.000	0.000	0.000	0.000
137	A	171	SER	0	-0.019	-0.019	16.131	0.006	0.006	0.000	0.000	0.000	0.000
138	A	172	VAL	0	0.006	-0.001	10.981	-0.027	-0.027	0.000	0.000	0.000	0.000
139	A	173	SER	0	0.037	0.038	14.256	0.018	0.018	0.000	0.000	0.000	0.000
140	A	174	THR	0	0.011	-0.008	12.150	-0.087	-0.087	0.000	0.000	0.000	0.000
141	A	175	GLU	-1	-0.839	-0.887	15.200	-0.295	-0.295	0.000	0.000	0.000	0.000
142	A	176	PRO	0	-0.002	-0.012	18.077	-0.017	-0.017	0.000	0.000	0.000	0.000
143	A	177	ASP	-1	-0.910	-0.952	19.387	-0.269	-0.269	0.000	0.000	0.000	0.000
144	A	178	ILE	0	-0.058	-0.045	16.515	-0.022	-0.022	0.000	0.000	0.000	0.000
145	A	179	THR	0	-0.007	-0.008	19.688	0.006	0.006	0.000	0.000	0.000	0.000
146	A	180	GLY	0	0.050	0.018	22.776	-0.011	-0.011	0.000	0.000	0.000	0.000
147	A	181	LEU	0	-0.009	-0.027	24.920	-0.001	-0.001	0.000	0.000	0.000	0.000
148	A	182	ALA	0	-0.009	0.005	22.049	0.004	0.004	0.000	0.000	0.000	0.000
149	A	183	CYS	0	0.001	0.004	21.315	-0.010	-0.010	0.000	0.000	0.000	0.000
150	A	184	LEU	0	0.002	0.007	22.537	0.004	0.004	0.000	0.000	0.000	0.000
151	A	185	LEU	0	0.015	0.005	25.651	0.010	0.010	0.000	0.000	0.000	0.000
152	A	186	SER	0	-0.030	-0.011	21.374	0.002	0.002	0.000	0.000	0.000	0.000
153	A	187	ILE	0	-0.028	-0.015	22.968	0.006	0.006	0.000	0.000	0.000	0.000
154	A	188	GLN	0	0.043	0.014	24.710	0.010	0.010	0.000	0.000	0.000	0.000
155	A	189	ARG	1	0.861	0.952	25.135	0.170	0.170	0.000	0.000	0.000	0.000
156	A	190	GLN	0	-0.052	-0.012	22.233	0.008	0.008	0.000	0.000	0.000	0.000

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