FMO DATABASE

FMODB ID: Z639N

Calculation Name: 1XHN-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1XHN

Chain ID: A

ChEMBL ID:

UniProt ID: O75629

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	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	171
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1729213.859358
FMO2-HF: Nuclear repulsion	1662296.793363
FMO2-HF: Total energy	-66917.065995
FMO2-MP2: Total energy	-67112.541852

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:11:GLY)

Summations of interaction energy for fragment #1(A:11: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.
1.771	3.684	0.013	-0.961	-0.964	0.003

Interaction energy analysis for fragmet #1(A:11:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.055 / q_NPA : 0.035

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	13	LEU	0	-0.009	0.004	3.817	-0.209	1.423	-0.021	-0.912	-0.699	0.003
4	A	14	PRO	0	-0.009	0.007	6.495	0.174	0.174	0.000	0.000	0.000	0.000
5	A	15	PRO	0	0.008	-0.007	8.609	-0.001	-0.001	0.000	0.000	0.000	0.000
6	A	16	ARG	1	0.872	0.914	12.288	0.852	0.852	0.000	0.000	0.000	0.000
7	A	17	GLU	-1	-0.994	-0.983	14.320	-0.221	-0.221	0.000	0.000	0.000	0.000
8	A	18	ASP	-1	-0.784	-0.878	13.207	-0.202	-0.202	0.000	0.000	0.000	0.000
9	A	19	ALA	0	0.045	0.006	13.565	-0.057	-0.057	0.000	0.000	0.000	0.000
10	A	20	ALA	0	0.052	0.030	14.724	-0.015	-0.015	0.000	0.000	0.000	0.000
11	A	21	ARG	1	0.932	0.954	8.274	0.304	0.304	0.000	0.000	0.000	0.000
12	A	22	VAL	0	-0.036	-0.010	9.986	-0.083	-0.083	0.000	0.000	0.000	0.000
13	A	23	ALA	0	0.013	0.006	10.922	-0.045	-0.045	0.000	0.000	0.000	0.000
14	A	24	ARG	1	0.834	0.924	10.761	-0.138	-0.138	0.000	0.000	0.000	0.000
15	A	25	PHE	0	-0.030	-0.023	3.224	0.067	0.348	0.034	-0.049	-0.265	0.000
16	A	26	VAL	0	0.000	-0.014	8.056	-0.017	-0.017	0.000	0.000	0.000	0.000
17	A	27	THR	0	0.005	-0.006	10.568	0.028	0.028	0.000	0.000	0.000	0.000
18	A	28	HIS	0	-0.113	-0.049	6.425	0.341	0.341	0.000	0.000	0.000	0.000
19	A	29	VAL	0	-0.052	-0.033	5.559	0.062	0.062	0.000	0.000	0.000	0.000
20	A	30	SER	0	-0.049	-0.021	8.339	-0.044	-0.044	0.000	0.000	0.000	0.000
21	A	31	ASP	-1	-0.830	-0.908	12.072	0.137	0.137	0.000	0.000	0.000	0.000
22	A	32	TRP	0	-0.007	-0.022	14.293	0.025	0.025	0.000	0.000	0.000	0.000
23	A	33	GLY	0	0.036	0.021	16.376	-0.046	-0.046	0.000	0.000	0.000	0.000
24	A	34	ALA	0	-0.026	0.003	19.015	0.021	0.021	0.000	0.000	0.000	0.000
25	A	35	LEU	0	-0.003	-0.011	22.477	-0.006	-0.006	0.000	0.000	0.000	0.000
26	A	36	ALA	0	-0.014	-0.008	24.826	0.002	0.002	0.000	0.000	0.000	0.000
27	A	37	THR	0	0.040	0.011	27.942	0.007	0.007	0.000	0.000	0.000	0.000
28	A	38	ILE	0	0.002	0.001	31.073	-0.006	-0.006	0.000	0.000	0.000	0.000
29	A	39	SER	0	-0.001	-0.003	34.772	0.007	0.007	0.000	0.000	0.000	0.000
30	A	40	THR	0	0.007	0.000	36.641	0.001	0.001	0.000	0.000	0.000	0.000
31	A	41	LEU	0	0.014	-0.002	37.214	0.003	0.003	0.000	0.000	0.000	0.000
32	A	42	GLU	-1	-0.795	-0.895	40.615	-0.023	-0.023	0.000	0.000	0.000	0.000
33	A	43	ALA	0	-0.042	-0.021	42.184	-0.002	-0.002	0.000	0.000	0.000	0.000
34	A	44	VAL	0	-0.088	-0.054	38.174	-0.003	-0.003	0.000	0.000	0.000	0.000
35	A	45	ARG	1	0.878	0.949	39.879	0.019	0.019	0.000	0.000	0.000	0.000
36	A	46	GLY	0	0.021	0.005	39.636	-0.001	-0.001	0.000	0.000	0.000	0.000
37	A	47	ARG	1	0.909	0.963	37.336	0.050	0.050	0.000	0.000	0.000	0.000
38	A	48	PRO	0	0.014	0.018	32.398	0.003	0.003	0.000	0.000	0.000	0.000
39	A	49	PHE	0	-0.019	-0.015	31.283	-0.002	-0.002	0.000	0.000	0.000	0.000
40	A	50	ALA	0	-0.001	-0.005	27.155	-0.003	-0.003	0.000	0.000	0.000	0.000
41	A	51	ASP	-1	-0.814	-0.877	26.702	-0.039	-0.039	0.000	0.000	0.000	0.000
42	A	52	VAL	0	-0.022	-0.002	21.707	-0.010	-0.010	0.000	0.000	0.000	0.000
43	A	53	LEU	0	-0.026	-0.007	22.252	0.017	0.017	0.000	0.000	0.000	0.000
44	A	54	SER	0	0.024	0.002	19.208	-0.025	-0.025	0.000	0.000	0.000	0.000
45	A	55	LEU	0	-0.067	-0.030	15.134	0.004	0.004	0.000	0.000	0.000	0.000
46	A	56	SER	0	-0.001	-0.024	14.835	0.020	0.020	0.000	0.000	0.000	0.000
47	A	57	ASP	-1	-0.720	-0.840	12.173	0.261	0.261	0.000	0.000	0.000	0.000
48	A	58	GLY	0	0.043	0.032	13.831	0.025	0.025	0.000	0.000	0.000	0.000
49	A	59	PRO	0	-0.006	-0.005	12.933	0.004	0.004	0.000	0.000	0.000	0.000
50	A	60	PRO	0	0.062	0.002	8.789	0.029	0.029	0.000	0.000	0.000	0.000
51	A	61	GLY	0	-0.010	0.005	8.629	0.284	0.284	0.000	0.000	0.000	0.000
52	A	62	ALA	0	-0.071	-0.037	9.633	-0.115	-0.115	0.000	0.000	0.000	0.000
53	A	63	GLY	0	0.008	0.030	10.344	-0.118	-0.118	0.000	0.000	0.000	0.000
54	A	64	SER	0	-0.010	-0.021	11.538	-0.039	-0.039	0.000	0.000	0.000	0.000
55	A	65	GLY	0	0.041	0.001	13.457	-0.046	-0.046	0.000	0.000	0.000	0.000
56	A	66	VAL	0	-0.029	0.003	14.559	-0.055	-0.055	0.000	0.000	0.000	0.000
57	A	67	PRO	0	-0.014	0.001	17.470	0.021	0.021	0.000	0.000	0.000	0.000
58	A	68	TYR	0	-0.024	-0.032	18.360	-0.004	-0.004	0.000	0.000	0.000	0.000
59	A	69	PHE	0	0.038	0.001	19.966	-0.006	-0.006	0.000	0.000	0.000	0.000
60	A	70	TYR	0	-0.022	-0.018	22.658	0.012	0.012	0.000	0.000	0.000	0.000
61	A	71	LEU	0	0.024	0.010	25.036	-0.009	-0.009	0.000	0.000	0.000	0.000
62	A	72	SER	0	-0.011	-0.023	28.114	0.005	0.005	0.000	0.000	0.000	0.000
63	A	73	PRO	0	0.026	-0.015	31.704	-0.006	-0.006	0.000	0.000	0.000	0.000
64	A	74	LEU	0	-0.041	-0.012	34.513	-0.004	-0.004	0.000	0.000	0.000	0.000
65	A	75	GLN	0	0.003	0.015	27.205	0.003	0.003	0.000	0.000	0.000	0.000
66	A	76	LEU	0	0.076	0.031	32.687	0.000	0.000	0.000	0.000	0.000	0.000
67	A	77	SER	0	-0.019	-0.042	28.898	-0.003	-0.003	0.000	0.000	0.000	0.000
68	A	78	VAL	0	-0.017	0.001	30.310	0.000	0.000	0.000	0.000	0.000	0.000
69	A	79	SER	0	0.027	0.006	32.360	0.002	0.002	0.000	0.000	0.000	0.000
70	A	80	ASN	0	-0.019	-0.010	32.949	0.003	0.003	0.000	0.000	0.000	0.000
71	A	81	LEU	0	-0.027	-0.012	28.727	0.000	0.000	0.000	0.000	0.000	0.000
72	A	82	GLN	0	-0.085	-0.037	33.351	0.006	0.006	0.000	0.000	0.000	0.000
73	A	83	GLU	-1	-0.930	-0.956	36.435	-0.005	-0.005	0.000	0.000	0.000	0.000
74	A	84	ASN	0	-0.021	-0.019	34.923	0.000	0.000	0.000	0.000	0.000	0.000
75	A	85	PRO	0	0.040	0.031	31.913	-0.003	-0.003	0.000	0.000	0.000	0.000
76	A	86	TYR	0	-0.042	-0.020	30.420	0.001	0.001	0.000	0.000	0.000	0.000
77	A	87	ALA	0	0.006	-0.003	27.062	-0.001	-0.001	0.000	0.000	0.000	0.000
78	A	88	THR	0	-0.018	0.000	23.984	-0.001	-0.001	0.000	0.000	0.000	0.000
79	A	89	LEU	0	0.006	0.020	18.389	0.003	0.003	0.000	0.000	0.000	0.000
80	A	90	THR	0	-0.073	-0.030	19.789	-0.018	-0.018	0.000	0.000	0.000	0.000
81	A	91	MET	0	0.019	0.023	14.819	0.028	0.028	0.000	0.000	0.000	0.000
82	A	92	THR	0	0.049	0.007	15.379	-0.043	-0.043	0.000	0.000	0.000	0.000
83	A	93	LEU	0	0.056	0.025	9.254	-0.008	-0.008	0.000	0.000	0.000	0.000
84	A	94	ALA	0	-0.030	-0.027	12.523	-0.060	-0.060	0.000	0.000	0.000	0.000
85	A	95	GLN	0	-0.014	-0.006	13.543	0.025	0.025	0.000	0.000	0.000	0.000
86	A	96	THR	0	-0.004	0.011	8.748	-0.060	-0.060	0.000	0.000	0.000	0.000
87	A	97	ASN	0	0.012	-0.015	11.153	0.084	0.084	0.000	0.000	0.000	0.000
88	A	98	PHE	0	-0.002	-0.006	8.557	0.010	0.010	0.000	0.000	0.000	0.000
89	A	99	CYS	0	-0.082	-0.014	11.288	-0.144	-0.144	0.000	0.000	0.000	0.000
90	A	100	LYS	1	0.999	1.006	14.829	0.388	0.388	0.000	0.000	0.000	0.000
91	A	101	LYS	1	0.878	0.949	10.744	1.074	1.074	0.000	0.000	0.000	0.000
92	A	102	HIS	0	-0.030	-0.014	10.031	-0.017	-0.017	0.000	0.000	0.000	0.000
93	A	103	GLY	0	0.017	0.034	15.531	0.043	0.043	0.000	0.000	0.000	0.000
94	A	104	PHE	0	-0.070	-0.044	13.655	0.012	0.012	0.000	0.000	0.000	0.000
95	A	105	ASP	-1	-0.830	-0.926	18.470	-0.303	-0.303	0.000	0.000	0.000	0.000
96	A	106	PRO	0	-0.007	-0.035	18.896	-0.028	-0.028	0.000	0.000	0.000	0.000
97	A	107	GLN	0	0.003	0.012	19.950	0.005	0.005	0.000	0.000	0.000	0.000
98	A	108	SER	0	-0.015	-0.001	20.040	0.014	0.014	0.000	0.000	0.000	0.000
99	A	109	PRO	0	0.046	0.032	19.291	-0.035	-0.035	0.000	0.000	0.000	0.000
100	A	110	LEU	0	-0.015	-0.013	16.458	-0.056	-0.056	0.000	0.000	0.000	0.000
101	A	112	VAL	0	0.029	0.009	12.485	0.054	0.054	0.000	0.000	0.000	0.000
102	A	113	HIS	0	-0.005	0.009	14.798	-0.004	-0.004	0.000	0.000	0.000	0.000
103	A	114	ILE	0	0.008	0.010	14.199	0.004	0.004	0.000	0.000	0.000	0.000
104	A	115	MET	0	-0.042	-0.023	17.644	0.008	0.008	0.000	0.000	0.000	0.000
105	A	116	LEU	0	0.008	0.014	16.696	0.006	0.006	0.000	0.000	0.000	0.000
106	A	117	SER	0	0.015	-0.014	21.126	0.011	0.011	0.000	0.000	0.000	0.000
107	A	118	GLY	0	0.073	0.033	24.794	0.004	0.004	0.000	0.000	0.000	0.000
108	A	119	THR	0	-0.002	0.007	26.782	-0.001	-0.001	0.000	0.000	0.000	0.000
109	A	120	VAL	0	-0.001	0.009	25.623	0.006	0.006	0.000	0.000	0.000	0.000
110	A	121	THR	0	0.002	0.012	27.539	-0.002	-0.002	0.000	0.000	0.000	0.000
111	A	122	LYS	1	0.904	0.953	27.980	-0.031	-0.031	0.000	0.000	0.000	0.000
112	A	123	VAL	0	-0.035	-0.006	25.018	-0.002	-0.002	0.000	0.000	0.000	0.000
113	A	124	ASN	0	0.024	0.008	28.084	-0.007	-0.007	0.000	0.000	0.000	0.000
114	A	125	GLU	-1	-0.887	-0.949	29.087	0.092	0.092	0.000	0.000	0.000	0.000
115	A	126	THR	0	-0.015	-0.017	28.980	0.007	0.007	0.000	0.000	0.000	0.000
116	A	127	GLU	-1	-0.787	-0.858	23.132	0.122	0.122	0.000	0.000	0.000	0.000
117	A	128	MET	0	0.003	0.001	24.706	0.008	0.008	0.000	0.000	0.000	0.000
118	A	129	ASP	-1	-0.850	-0.915	25.406	0.192	0.192	0.000	0.000	0.000	0.000
119	A	130	ILE	0	0.059	0.038	18.607	0.017	0.017	0.000	0.000	0.000	0.000
120	A	131	ALA	0	0.039	0.043	20.445	0.021	0.021	0.000	0.000	0.000	0.000
121	A	132	LYS	1	0.879	0.936	21.122	-0.167	-0.167	0.000	0.000	0.000	0.000
122	A	133	HIS	0	-0.011	-0.012	18.427	-0.017	-0.017	0.000	0.000	0.000	0.000
123	A	134	SER	0	-0.027	-0.034	16.890	0.040	0.040	0.000	0.000	0.000	0.000
124	A	135	LEU	0	-0.036	-0.009	16.803	0.013	0.013	0.000	0.000	0.000	0.000
125	A	136	PHE	0	-0.009	-0.016	18.800	-0.003	-0.003	0.000	0.000	0.000	0.000
126	A	137	ILE	0	-0.065	-0.019	14.924	0.002	0.002	0.000	0.000	0.000	0.000
127	A	138	ARG	1	0.809	0.919	11.478	-0.214	-0.214	0.000	0.000	0.000	0.000
128	A	139	HIS	0	-0.005	-0.011	15.538	-0.030	-0.030	0.000	0.000	0.000	0.000
129	A	140	PRO	0	-0.004	-0.010	18.082	-0.014	-0.014	0.000	0.000	0.000	0.000
130	A	141	GLU	-1	-0.844	-0.914	21.062	0.036	0.036	0.000	0.000	0.000	0.000
131	A	142	MET	0	-0.007	0.021	21.176	-0.003	-0.003	0.000	0.000	0.000	0.000
132	A	143	LYS	1	0.887	0.952	22.537	-0.193	-0.193	0.000	0.000	0.000	0.000
133	A	144	THR	0	-0.075	-0.048	26.559	-0.006	-0.006	0.000	0.000	0.000	0.000
134	A	145	TRP	0	-0.031	-0.015	24.195	-0.006	-0.006	0.000	0.000	0.000	0.000
135	A	146	PRO	0	0.016	0.008	29.629	0.004	0.004	0.000	0.000	0.000	0.000
136	A	147	SER	0	0.070	0.024	33.363	-0.004	-0.004	0.000	0.000	0.000	0.000
137	A	148	SER	0	0.012	0.010	34.675	-0.002	-0.002	0.000	0.000	0.000	0.000
138	A	149	HIS	1	0.873	0.941	32.724	-0.027	-0.027	0.000	0.000	0.000	0.000
139	A	150	ASN	0	-0.010	0.014	34.139	0.000	0.000	0.000	0.000	0.000	0.000
140	A	151	TRP	0	0.038	0.012	28.581	-0.004	-0.004	0.000	0.000	0.000	0.000
141	A	152	PHE	0	-0.019	-0.009	29.740	0.004	0.004	0.000	0.000	0.000	0.000
142	A	153	PHE	0	0.032	0.017	24.174	-0.003	-0.003	0.000	0.000	0.000	0.000
143	A	154	ALA	0	0.001	-0.006	25.387	-0.004	-0.004	0.000	0.000	0.000	0.000
144	A	155	LYS	1	0.877	0.921	22.889	-0.071	-0.071	0.000	0.000	0.000	0.000
145	A	156	LEU	0	-0.015	0.004	21.027	-0.009	-0.009	0.000	0.000	0.000	0.000
146	A	157	ASN	0	-0.058	-0.040	22.415	0.019	0.019	0.000	0.000	0.000	0.000
147	A	158	ILE	0	-0.013	-0.012	18.976	-0.011	-0.011	0.000	0.000	0.000	0.000
148	A	159	THR	0	0.028	-0.002	23.397	0.008	0.008	0.000	0.000	0.000	0.000
149	A	160	ASN	0	-0.050	-0.016	24.783	0.003	0.003	0.000	0.000	0.000	0.000
150	A	161	ILE	0	0.030	0.019	18.190	-0.001	-0.001	0.000	0.000	0.000	0.000
151	A	162	TRP	0	-0.025	-0.001	21.140	0.004	0.004	0.000	0.000	0.000	0.000
152	A	163	VAL	0	0.003	-0.001	15.759	-0.015	-0.015	0.000	0.000	0.000	0.000
153	A	164	LEU	0	0.002	0.008	18.205	0.019	0.019	0.000	0.000	0.000	0.000
154	A	165	ASP	-1	-0.751	-0.872	14.791	-0.512	-0.512	0.000	0.000	0.000	0.000
155	A	166	TYR	0	-0.006	-0.008	16.686	-0.073	-0.073	0.000	0.000	0.000	0.000
156	A	167	PHE	0	0.027	0.002	19.421	0.029	0.029	0.000	0.000	0.000	0.000
157	A	168	GLY	0	0.014	0.005	22.978	-0.003	-0.003	0.000	0.000	0.000	0.000
158	A	169	GLY	0	-0.020	0.001	24.512	0.018	0.018	0.000	0.000	0.000	0.000
159	A	170	PRO	0	-0.025	-0.022	22.320	-0.019	-0.019	0.000	0.000	0.000	0.000
160	A	171	LYS	1	0.838	0.914	17.730	0.398	0.398	0.000	0.000	0.000	0.000
161	A	172	ILE	0	-0.006	-0.009	21.046	-0.007	-0.007	0.000	0.000	0.000	0.000
162	A	173	VAL	0	-0.013	0.001	17.635	-0.008	-0.008	0.000	0.000	0.000	0.000
163	A	174	THR	0	-0.030	-0.043	20.869	0.014	0.014	0.000	0.000	0.000	0.000
164	A	175	PRO	0	0.031	0.008	20.762	-0.004	-0.004	0.000	0.000	0.000	0.000
165	A	176	GLU	-1	-0.844	-0.930	20.511	-0.003	-0.003	0.000	0.000	0.000	0.000
166	A	177	GLU	-1	-0.812	-0.866	18.967	-0.085	-0.085	0.000	0.000	0.000	0.000
167	A	178	TYR	0	-0.061	-0.041	14.727	-0.010	-0.010	0.000	0.000	0.000	0.000
168	A	179	TYR	0	-0.019	-0.039	15.630	0.011	0.011	0.000	0.000	0.000	0.000
169	A	180	ASN	0	-0.064	-0.031	17.546	0.048	0.048	0.000	0.000	0.000	0.000
170	A	181	VAL	0	-0.059	-0.003	11.367	0.015	0.015	0.000	0.000	0.000	0.000
171	A	182	THR	0	-0.018	-0.002	9.794	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:11:GLY)