FMO DATABASE

FMODB ID: LN319

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1555702.113468
FMO2-HF: Nuclear repulsion	1494262.633271
FMO2-HF: Total energy	-61439.480197
FMO2-MP2: Total energy	-61617.018353

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.
-6.997	-2.774	5.357	-4.198	-5.382	-0.03

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 : 0.034 / q_NPA : 0.008

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	-0.030	-0.024	3.795	-1.165	-0.123	-0.010	-0.556	-0.476	0.003
4	A	38	ILE	0	0.036	0.026	5.962	0.435	0.435	0.000	0.000	0.000	0.000
5	A	39	LYS	1	0.946	0.973	7.487	0.566	0.566	0.000	0.000	0.000	0.000
6	A	40	VAL	0	-0.001	0.004	10.936	0.056	0.056	0.000	0.000	0.000	0.000
7	A	41	GLY	0	-0.037	-0.020	14.167	0.031	0.031	0.000	0.000	0.000	0.000
8	A	42	ASP	-1	-0.899	-0.944	9.017	-0.508	-0.508	0.000	0.000	0.000	0.000
9	A	43	ILE	0	-0.057	-0.032	11.324	-0.015	-0.015	0.000	0.000	0.000	0.000
10	A	44	ILE	0	-0.018	-0.005	9.307	-0.025	-0.025	0.000	0.000	0.000	0.000
11	A	45	PRO	0	0.013	0.003	6.061	0.126	0.126	0.000	0.000	0.000	0.000
12	A	46	ASP	-1	-0.928	-0.950	8.765	0.013	0.013	0.000	0.000	0.000	0.000
13	A	47	VAL	0	0.027	0.007	9.294	0.058	0.058	0.000	0.000	0.000	0.000
14	A	48	LEU	0	-0.011	-0.005	12.392	-0.051	-0.051	0.000	0.000	0.000	0.000
15	A	49	VAL	0	-0.023	-0.006	13.797	-0.029	-0.029	0.000	0.000	0.000	0.000
16	A	50	TYR	0	0.002	-0.007	16.208	0.028	0.028	0.000	0.000	0.000	0.000
17	A	51	GLU	-1	-0.768	-0.859	19.553	-0.126	-0.126	0.000	0.000	0.000	0.000
18	A	52	ASP	-1	-0.848	-0.908	22.271	-0.063	-0.063	0.000	0.000	0.000	0.000
19	A	53	VAL	0	-0.043	-0.035	25.167	0.002	0.002	0.000	0.000	0.000	0.000
20	A	54	PRO	0	0.027	0.002	22.663	0.000	0.000	0.000	0.000	0.000	0.000
21	A	55	SER	0	-0.030	-0.011	23.043	0.005	0.005	0.000	0.000	0.000	0.000
22	A	56	LYS	1	0.838	0.918	23.812	0.065	0.065	0.000	0.000	0.000	0.000
23	A	57	SER	0	0.000	-0.005	19.433	-0.008	-0.008	0.000	0.000	0.000	0.000
24	A	58	PHE	0	-0.023	-0.010	19.290	0.010	0.010	0.000	0.000	0.000	0.000
25	A	59	PRO	0	0.044	0.028	16.246	-0.016	-0.016	0.000	0.000	0.000	0.000
26	A	60	ILE	0	0.036	0.020	12.199	-0.012	-0.012	0.000	0.000	0.000	0.000
27	A	61	HIS	0	-0.011	-0.025	12.473	-0.005	-0.005	0.000	0.000	0.000	0.000
28	A	62	ASP	-1	-0.851	-0.930	16.634	-0.020	-0.020	0.000	0.000	0.000	0.000
29	A	63	VAL	0	-0.100	-0.038	18.047	0.002	0.002	0.000	0.000	0.000	0.000
30	A	64	PHE	0	0.000	-0.027	15.806	-0.006	-0.006	0.000	0.000	0.000	0.000
31	A	65	ARG	1	0.904	0.967	19.348	0.018	0.018	0.000	0.000	0.000	0.000
32	A	66	GLY	0	-0.037	-0.022	20.982	0.002	0.002	0.000	0.000	0.000	0.000
33	A	67	ARG	1	0.880	0.948	22.205	0.095	0.095	0.000	0.000	0.000	0.000
34	A	68	LYS	1	0.935	0.990	21.368	0.118	0.118	0.000	0.000	0.000	0.000
35	A	69	GLY	0	-0.009	-0.018	20.410	0.014	0.014	0.000	0.000	0.000	0.000
36	A	70	ILE	0	-0.032	-0.005	18.557	-0.021	-0.021	0.000	0.000	0.000	0.000
37	A	71	LEU	0	0.009	0.013	12.146	0.024	0.024	0.000	0.000	0.000	0.000
38	A	72	PHE	0	0.010	0.002	15.115	-0.048	-0.048	0.000	0.000	0.000	0.000
39	A	73	SER	0	0.015	0.021	12.548	0.050	0.050	0.000	0.000	0.000	0.000
40	A	74	VAL	0	-0.046	-0.022	14.882	0.023	0.023	0.000	0.000	0.000	0.000
41	A	75	VAL	0	-0.005	-0.002	15.720	-0.017	-0.017	0.000	0.000	0.000	0.000
42	A	76	GLY	0	0.017	-0.024	16.791	0.005	0.005	0.000	0.000	0.000	0.000
43	A	77	ALA	0	0.039	0.030	19.188	0.006	0.006	0.000	0.000	0.000	0.000
44	A	78	PHE	0	-0.018	-0.023	22.306	0.006	0.006	0.000	0.000	0.000	0.000
45	A	79	VAL	0	-0.022	0.019	20.405	0.010	0.010	0.000	0.000	0.000	0.000
46	A	80	PRO	0	0.023	0.015	23.472	-0.009	-0.009	0.000	0.000	0.000	0.000
47	A	81	GLY	0	0.030	0.006	23.082	-0.017	-0.017	0.000	0.000	0.000	0.000
48	A	82	SER	0	-0.078	-0.044	21.334	-0.009	-0.009	0.000	0.000	0.000	0.000
49	A	83	ASN	0	0.042	0.000	22.303	-0.008	-0.008	0.000	0.000	0.000	0.000
50	A	84	ASN	0	-0.022	-0.011	23.715	0.022	0.022	0.000	0.000	0.000	0.000
51	A	85	HIS	0	0.069	0.023	20.979	0.019	0.019	0.000	0.000	0.000	0.000
52	A	86	ILE	0	0.008	0.021	22.346	0.002	0.002	0.000	0.000	0.000	0.000
53	A	87	PRO	0	0.031	0.020	25.100	0.008	0.008	0.000	0.000	0.000	0.000
54	A	88	GLU	-1	-0.844	-0.909	26.588	-0.169	-0.169	0.000	0.000	0.000	0.000
55	A	89	TYR	0	0.025	-0.003	19.715	0.004	0.004	0.000	0.000	0.000	0.000
56	A	90	LEU	0	-0.025	-0.010	25.987	0.008	0.008	0.000	0.000	0.000	0.000
57	A	91	SER	0	-0.082	-0.040	28.841	0.010	0.010	0.000	0.000	0.000	0.000
58	A	92	LEU	0	-0.001	0.000	27.389	0.008	0.008	0.000	0.000	0.000	0.000
59	A	93	TYR	0	0.038	0.027	27.758	0.004	0.004	0.000	0.000	0.000	0.000
60	A	94	ASP	-1	-0.861	-0.957	29.477	-0.093	-0.093	0.000	0.000	0.000	0.000
61	A	95	LYS	1	0.891	0.954	30.181	0.112	0.112	0.000	0.000	0.000	0.000
62	A	96	PHE	0	0.022	0.006	24.981	-0.003	-0.003	0.000	0.000	0.000	0.000
63	A	97	LYS	1	0.864	0.935	27.746	0.092	0.092	0.000	0.000	0.000	0.000
64	A	98	GLU	-1	-0.935	-0.958	29.743	-0.093	-0.093	0.000	0.000	0.000	0.000
65	A	99	GLU	-1	-0.889	-0.933	27.757	-0.116	-0.116	0.000	0.000	0.000	0.000
66	A	100	GLY	0	-0.073	-0.046	27.643	-0.004	-0.004	0.000	0.000	0.000	0.000
67	A	101	TYR	0	-0.017	-0.002	20.888	0.003	0.003	0.000	0.000	0.000	0.000
68	A	102	HIS	0	0.028	0.002	24.917	-0.011	-0.011	0.000	0.000	0.000	0.000
69	A	103	THR	0	-0.051	-0.006	21.339	0.006	0.006	0.000	0.000	0.000	0.000
70	A	104	ILE	0	0.046	0.028	21.105	-0.018	-0.018	0.000	0.000	0.000	0.000
71	A	105	ALA	0	-0.002	0.005	17.725	0.018	0.018	0.000	0.000	0.000	0.000
72	A	106	CYS	0	-0.012	0.010	17.911	-0.040	-0.040	0.000	0.000	0.000	0.000
73	A	107	ILE	0	-0.005	0.002	12.162	0.029	0.029	0.000	0.000	0.000	0.000
74	A	108	ALA	0	0.022	-0.006	14.968	-0.046	-0.046	0.000	0.000	0.000	0.000
75	A	109	VAL	0	-0.032	0.009	11.594	0.031	0.031	0.000	0.000	0.000	0.000
76	A	110	ASN	0	-0.005	-0.014	14.759	-0.003	-0.003	0.000	0.000	0.000	0.000
77	A	111	ASP	-1	-0.791	-0.898	18.141	-0.083	-0.083	0.000	0.000	0.000	0.000
78	A	112	PRO	0	0.046	0.001	20.374	-0.012	-0.012	0.000	0.000	0.000	0.000
79	A	113	PHE	0	0.016	0.017	22.366	0.001	0.001	0.000	0.000	0.000	0.000
80	A	114	VAL	0	-0.016	-0.012	23.057	-0.004	-0.004	0.000	0.000	0.000	0.000
81	A	115	MET	0	-0.034	-0.012	18.705	-0.004	-0.004	0.000	0.000	0.000	0.000
82	A	116	ALA	0	0.031	0.016	22.866	-0.004	-0.004	0.000	0.000	0.000	0.000
83	A	117	ALA	0	-0.057	-0.025	25.709	0.002	0.002	0.000	0.000	0.000	0.000
84	A	118	TRP	0	0.045	0.012	21.454	-0.003	-0.003	0.000	0.000	0.000	0.000
85	A	119	GLY	0	0.065	0.029	25.507	-0.002	-0.002	0.000	0.000	0.000	0.000
86	A	120	LYS	1	0.931	0.965	26.124	0.085	0.085	0.000	0.000	0.000	0.000
87	A	121	THR	0	-0.115	-0.055	28.605	0.003	0.003	0.000	0.000	0.000	0.000
88	A	122	VAL	0	-0.042	-0.018	25.344	0.001	0.001	0.000	0.000	0.000	0.000
89	A	123	ASP	-1	-0.786	-0.901	26.985	-0.133	-0.133	0.000	0.000	0.000	0.000
90	A	124	PRO	0	-0.003	0.009	29.164	0.004	0.004	0.000	0.000	0.000	0.000
91	A	125	GLU	-1	-0.962	-0.981	31.854	-0.084	-0.084	0.000	0.000	0.000	0.000
92	A	126	HIS	0	-0.071	-0.030	25.882	-0.002	-0.002	0.000	0.000	0.000	0.000
93	A	127	LYS	1	0.861	0.927	28.124	0.102	0.102	0.000	0.000	0.000	0.000
94	A	128	ILE	0	-0.060	-0.022	21.996	-0.010	-0.010	0.000	0.000	0.000	0.000
95	A	129	ARG	1	0.811	0.879	21.165	0.115	0.115	0.000	0.000	0.000	0.000
96	A	130	MET	0	0.001	0.007	20.744	-0.029	-0.029	0.000	0.000	0.000	0.000
97	A	131	LEU	0	0.003	0.001	16.331	0.019	0.019	0.000	0.000	0.000	0.000
98	A	132	ALA	0	0.046	0.012	17.118	-0.034	-0.034	0.000	0.000	0.000	0.000
99	A	133	ASP	-1	-0.703	-0.852	10.634	-0.376	-0.376	0.000	0.000	0.000	0.000
100	A	134	MET	0	-0.029	-0.008	13.590	-0.023	-0.023	0.000	0.000	0.000	0.000
101	A	135	HIS	0	-0.013	-0.006	12.853	0.007	0.007	0.000	0.000	0.000	0.000
102	A	136	GLY	0	0.008	-0.008	10.480	0.039	0.039	0.000	0.000	0.000	0.000
103	A	137	GLU	-1	-0.959	-0.976	8.256	0.085	0.085	0.000	0.000	0.000	0.000
104	A	138	PHE	0	0.047	0.012	7.145	-0.059	-0.059	0.000	0.000	0.000	0.000
105	A	139	THR	0	-0.029	-0.032	6.417	-0.236	-0.236	0.000	0.000	0.000	0.000
106	A	140	ARG	1	0.852	0.928	4.302	-0.711	-0.577	-0.001	-0.038	-0.094	0.000
107	A	141	ALA	0	-0.018	-0.001	2.326	-5.690	-3.944	1.370	-1.390	-1.726	-0.018
108	A	142	LEU	0	-0.033	-0.020	2.584	-0.421	1.152	1.875	-1.731	-1.717	-0.015
109	A	143	GLY	0	0.018	0.025	2.698	-2.346	-1.604	1.864	-1.369	-1.237	-0.001
110	A	144	THR	0	-0.084	-0.041	2.955	2.288	1.274	0.259	0.886	-0.132	0.001
111	A	145	GLU	-1	-0.831	-0.930	5.959	-0.034	-0.034	0.000	0.000	0.000	0.000
112	A	146	LEU	0	-0.093	-0.045	7.849	-0.022	-0.022	0.000	0.000	0.000	0.000
113	A	147	ASP	-1	-0.925	-0.955	11.170	-0.181	-0.181	0.000	0.000	0.000	0.000
114	A	148	SER	0	0.006	-0.024	12.948	0.016	0.016	0.000	0.000	0.000	0.000
115	A	149	SER	0	0.031	0.014	14.855	0.040	0.040	0.000	0.000	0.000	0.000
116	A	150	LYS	1	0.913	0.954	17.239	0.109	0.109	0.000	0.000	0.000	0.000
117	A	151	MET	0	-0.020	0.000	19.570	0.004	0.004	0.000	0.000	0.000	0.000
118	A	152	LEU	0	-0.018	-0.020	17.887	0.008	0.008	0.000	0.000	0.000	0.000
119	A	153	GLY	0	0.003	0.016	19.641	0.003	0.003	0.000	0.000	0.000	0.000
120	A	154	ASN	0	0.032	0.029	14.871	0.014	0.014	0.000	0.000	0.000	0.000
121	A	155	ASN	0	-0.006	0.010	10.091	0.019	0.019	0.000	0.000	0.000	0.000
122	A	156	ARG	1	0.881	0.939	12.216	0.239	0.239	0.000	0.000	0.000	0.000
123	A	157	SER	0	0.061	0.015	10.470	-0.142	-0.142	0.000	0.000	0.000	0.000
124	A	158	ARG	1	0.888	0.945	8.742	1.169	1.169	0.000	0.000	0.000	0.000
125	A	159	ARG	1	0.851	0.929	11.982	0.351	0.351	0.000	0.000	0.000	0.000
126	A	160	TYR	0	0.040	0.012	9.629	-0.028	-0.028	0.000	0.000	0.000	0.000
127	A	161	ALA	0	0.018	0.005	13.455	0.060	0.060	0.000	0.000	0.000	0.000
128	A	162	MET	0	-0.027	-0.008	10.679	-0.075	-0.075	0.000	0.000	0.000	0.000
129	A	163	LEU	0	-0.008	0.008	15.016	0.045	0.045	0.000	0.000	0.000	0.000
130	A	164	ILE	0	-0.018	-0.005	13.561	-0.029	-0.029	0.000	0.000	0.000	0.000
131	A	165	ASP	-1	-0.874	-0.953	17.085	-0.111	-0.111	0.000	0.000	0.000	0.000
132	A	166	ASP	-1	-0.845	-0.920	18.661	-0.065	-0.065	0.000	0.000	0.000	0.000
133	A	167	ASN	0	-0.034	-0.029	14.922	-0.008	-0.008	0.000	0.000	0.000	0.000
134	A	168	LYS	1	0.956	0.990	13.939	0.067	0.067	0.000	0.000	0.000	0.000
135	A	169	ILE	0	0.017	0.011	9.597	-0.005	-0.005	0.000	0.000	0.000	0.000
136	A	170	ARG	1	0.850	0.917	14.093	0.199	0.199	0.000	0.000	0.000	0.000
137	A	171	SER	0	-0.020	-0.013	16.134	0.001	0.001	0.000	0.000	0.000	0.000
138	A	172	VAL	0	0.023	0.004	10.965	-0.022	-0.022	0.000	0.000	0.000	0.000
139	A	173	SER	0	0.010	0.029	14.259	0.036	0.036	0.000	0.000	0.000	0.000
140	A	174	THR	0	0.018	-0.007	12.172	-0.087	-0.087	0.000	0.000	0.000	0.000
141	A	175	GLU	-1	-0.854	-0.903	15.207	-0.296	-0.296	0.000	0.000	0.000	0.000
142	A	176	PRO	0	0.019	-0.012	18.084	-0.019	-0.019	0.000	0.000	0.000	0.000
143	A	177	ASP	-1	-0.939	-0.958	19.205	-0.287	-0.287	0.000	0.000	0.000	0.000
144	A	178	ILE	0	-0.056	-0.042	16.657	-0.022	-0.022	0.000	0.000	0.000	0.000
145	A	179	THR	0	0.019	0.014	19.694	0.008	0.008	0.000	0.000	0.000	0.000
146	A	180	GLY	0	0.050	0.012	22.780	-0.009	-0.009	0.000	0.000	0.000	0.000
147	A	181	LEU	0	0.011	-0.011	24.924	-0.001	-0.001	0.000	0.000	0.000	0.000
148	A	182	ALA	0	-0.009	0.001	22.006	0.005	0.005	0.000	0.000	0.000	0.000
149	A	183	CYS	0	-0.002	0.004	21.613	-0.007	-0.007	0.000	0.000	0.000	0.000
150	A	184	LEU	0	-0.002	0.005	22.540	0.005	0.005	0.000	0.000	0.000	0.000
151	A	185	LEU	0	0.013	-0.001	25.717	0.011	0.011	0.000	0.000	0.000	0.000
152	A	186	SER	0	-0.014	-0.004	21.417	0.003	0.003	0.000	0.000	0.000	0.000
153	A	187	ILE	0	-0.002	-0.001	23.041	0.007	0.007	0.000	0.000	0.000	0.000
154	A	188	GLN	0	-0.001	-0.007	24.711	0.015	0.015	0.000	0.000	0.000	0.000
155	A	189	ARG	1	0.856	0.949	25.096	0.174	0.174	0.000	0.000	0.000	0.000
156	A	190	GLN	0	-0.043	-0.024	22.085	-0.010	-0.010	0.000	0.000	0.000	0.000

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