FMO DATABASE

FMODB ID: 89N7Y

Calculation Name: 2IO5-A-Xray372

Preferred Name: Histone chaperone ASF1A

Target Type: SINGLE PROTEIN

Ligand Name:

ligand 3-letter code:

PDB ID: 2IO5

Chain ID: A

ChEMBL ID: CHEMBL3392950

UniProt ID: Q9Y294

Base Structure: X-ray

Registration Date: 2023-09-22

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	154
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1463317.509913
FMO2-HF: Nuclear repulsion	1401996.946805
FMO2-HF: Total energy	-61320.563108
FMO2-MP2: Total energy	-61500.410216

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:1:MET)

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

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.
-2.398	0.626	0.034	-0.887	-2.173	0.001

Interaction energy analysis for fragmet #1(A:1:MET)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.000 / q_NPA : -0.015

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	3	LYS	1	0.949	0.987	3.850	1.446	2.838	-0.011	-0.553	-0.829	0.001
4	A	4	VAL	0	0.022	0.023	5.661	0.559	0.559	0.000	0.000	0.000	0.000
5	A	5	GLN	0	-0.037	-0.003	8.226	0.093	0.093	0.000	0.000	0.000	0.000
6	A	6	VAL	0	0.019	0.006	9.797	-0.022	-0.022	0.000	0.000	0.000	0.000
7	A	7	ASN	0	-0.055	-0.045	12.759	0.017	0.017	0.000	0.000	0.000	0.000
8	A	8	ASN	0	0.013	-0.009	15.346	0.036	0.036	0.000	0.000	0.000	0.000
9	A	9	VAL	0	-0.004	0.004	18.902	-0.025	-0.025	0.000	0.000	0.000	0.000
10	A	10	VAL	0	0.003	0.022	21.590	0.014	0.014	0.000	0.000	0.000	0.000
11	A	11	VAL	0	-0.007	0.001	25.265	-0.009	-0.009	0.000	0.000	0.000	0.000
12	A	12	LEU	0	-0.039	-0.020	28.137	0.007	0.007	0.000	0.000	0.000	0.000
13	A	13	ASP	-1	-0.885	-0.939	31.012	-0.041	-0.041	0.000	0.000	0.000	0.000
14	A	14	ASN	0	0.012	0.017	32.423	-0.003	-0.003	0.000	0.000	0.000	0.000
15	A	15	PRO	0	-0.045	-0.024	34.617	0.003	0.003	0.000	0.000	0.000	0.000
16	A	16	SER	0	0.030	0.005	36.723	-0.001	-0.001	0.000	0.000	0.000	0.000
17	A	17	PRO	0	-0.006	0.001	38.718	0.000	0.000	0.000	0.000	0.000	0.000
18	A	18	PHE	0	0.035	0.016	37.186	-0.003	-0.003	0.000	0.000	0.000	0.000
19	A	19	TYR	0	-0.032	-0.043	37.715	-0.002	-0.002	0.000	0.000	0.000	0.000
20	A	20	ASN	0	-0.056	0.005	35.908	-0.001	-0.001	0.000	0.000	0.000	0.000
21	A	21	PRO	0	0.054	0.018	33.809	-0.001	-0.001	0.000	0.000	0.000	0.000
22	A	22	PHE	0	-0.048	-0.015	29.259	0.005	0.005	0.000	0.000	0.000	0.000
23	A	23	GLN	0	0.022	-0.007	29.088	-0.001	-0.001	0.000	0.000	0.000	0.000
24	A	24	PHE	0	0.012	0.011	24.203	0.008	0.008	0.000	0.000	0.000	0.000
25	A	25	GLU	-1	-0.943	-0.972	23.525	-0.073	-0.073	0.000	0.000	0.000	0.000
26	A	26	ILE	0	-0.035	-0.010	18.028	0.011	0.011	0.000	0.000	0.000	0.000
27	A	27	THR	0	0.004	-0.001	16.949	-0.005	-0.005	0.000	0.000	0.000	0.000
28	A	28	PHE	0	-0.030	-0.027	13.189	0.026	0.026	0.000	0.000	0.000	0.000
29	A	29	GLU	-1	-0.932	-0.960	10.436	-0.077	-0.077	0.000	0.000	0.000	0.000
30	A	30	CYS	0	-0.030	-0.010	9.482	-0.094	-0.094	0.000	0.000	0.000	0.000
31	A	31	ILE	0	0.004	0.003	4.301	0.038	0.121	-0.001	-0.005	-0.077	0.000
32	A	32	GLU	-1	-0.984	-0.990	6.454	-1.145	-1.145	0.000	0.000	0.000	0.000
33	A	33	ASP	-1	-0.857	-0.939	8.651	-0.356	-0.356	0.000	0.000	0.000	0.000
34	A	34	LEU	0	-0.082	-0.041	9.435	-0.157	-0.157	0.000	0.000	0.000	0.000
35	A	35	SER	0	-0.053	-0.032	12.379	0.098	0.098	0.000	0.000	0.000	0.000
36	A	36	GLU	-1	-0.964	-0.991	12.722	-0.299	-0.299	0.000	0.000	0.000	0.000
37	A	37	ASP	-1	-0.901	-0.942	14.555	-0.346	-0.346	0.000	0.000	0.000	0.000
38	A	38	LEU	0	-0.040	-0.035	12.920	-0.095	-0.095	0.000	0.000	0.000	0.000
39	A	39	GLU	-1	-0.909	-0.956	16.035	-0.190	-0.190	0.000	0.000	0.000	0.000
40	A	40	TRP	0	0.026	0.002	15.814	-0.013	-0.013	0.000	0.000	0.000	0.000
41	A	41	LYS	1	0.931	0.958	20.050	0.207	0.207	0.000	0.000	0.000	0.000
42	A	42	ILE	0	0.014	0.014	22.255	-0.001	-0.001	0.000	0.000	0.000	0.000
43	A	43	ILE	0	-0.008	0.009	22.753	0.001	0.001	0.000	0.000	0.000	0.000
44	A	44	TYR	0	0.018	-0.001	26.266	0.006	0.006	0.000	0.000	0.000	0.000
45	A	45	VAL	0	0.029	0.008	27.359	-0.001	-0.001	0.000	0.000	0.000	0.000
46	A	46	GLY	0	-0.034	-0.020	29.961	0.006	0.006	0.000	0.000	0.000	0.000
47	A	47	SER	0	-0.006	-0.021	32.829	0.004	0.004	0.000	0.000	0.000	0.000
48	A	48	ALA	0	-0.001	-0.003	31.627	-0.004	-0.004	0.000	0.000	0.000	0.000
49	A	49	GLU	-1	-0.964	-0.969	32.314	-0.038	-0.038	0.000	0.000	0.000	0.000
50	A	50	SER	0	-0.066	-0.046	32.003	-0.002	-0.002	0.000	0.000	0.000	0.000
51	A	51	GLU	-1	-0.886	-0.936	25.227	-0.105	-0.105	0.000	0.000	0.000	0.000
52	A	52	GLU	-1	-0.979	-0.988	29.713	-0.075	-0.075	0.000	0.000	0.000	0.000
53	A	53	TYR	0	-0.095	-0.041	32.343	0.002	0.002	0.000	0.000	0.000	0.000
54	A	54	ASP	-1	-0.861	-0.929	27.163	-0.091	-0.091	0.000	0.000	0.000	0.000
55	A	55	GLN	0	-0.028	-0.008	30.230	-0.002	-0.002	0.000	0.000	0.000	0.000
56	A	56	VAL	0	-0.037	-0.029	25.719	-0.004	-0.004	0.000	0.000	0.000	0.000
57	A	57	LEU	0	-0.051	-0.019	28.210	0.003	0.003	0.000	0.000	0.000	0.000
58	A	58	ASP	-1	-0.830	-0.916	27.559	-0.115	-0.115	0.000	0.000	0.000	0.000
59	A	59	SER	0	-0.147	-0.095	23.637	-0.012	-0.012	0.000	0.000	0.000	0.000
60	A	60	VAL	0	0.011	0.027	21.876	0.006	0.006	0.000	0.000	0.000	0.000
61	A	61	LEU	0	0.006	0.011	19.854	-0.025	-0.025	0.000	0.000	0.000	0.000
62	A	62	VAL	0	-0.015	-0.018	18.465	0.021	0.021	0.000	0.000	0.000	0.000
63	A	63	GLY	0	0.021	0.011	18.141	-0.048	-0.048	0.000	0.000	0.000	0.000
64	A	64	PRO	0	-0.003	0.006	17.059	0.035	0.035	0.000	0.000	0.000	0.000
65	A	65	VAL	0	-0.017	-0.026	14.261	0.037	0.037	0.000	0.000	0.000	0.000
66	A	66	PRO	0	-0.002	0.001	14.306	-0.061	-0.061	0.000	0.000	0.000	0.000
67	A	67	ALA	0	0.024	0.017	11.994	-0.028	-0.028	0.000	0.000	0.000	0.000
68	A	68	GLY	0	-0.018	0.002	12.068	0.078	0.078	0.000	0.000	0.000	0.000
69	A	69	ARG	1	0.919	0.967	13.196	0.027	0.027	0.000	0.000	0.000	0.000
70	A	70	HIS	0	0.024	-0.002	15.454	0.018	0.018	0.000	0.000	0.000	0.000
71	A	71	MET	0	-0.047	-0.026	17.877	0.012	0.012	0.000	0.000	0.000	0.000
72	A	72	PHE	0	-0.023	-0.006	19.207	-0.002	-0.002	0.000	0.000	0.000	0.000
73	A	73	VAL	0	0.045	0.024	23.116	0.004	0.004	0.000	0.000	0.000	0.000
74	A	74	PHE	0	-0.037	-0.013	22.799	-0.006	-0.006	0.000	0.000	0.000	0.000
75	A	75	GLN	0	0.007	-0.005	25.707	0.008	0.008	0.000	0.000	0.000	0.000
76	A	76	ALA	0	0.024	0.002	28.606	-0.008	-0.008	0.000	0.000	0.000	0.000
77	A	77	ASP	-1	-0.888	-0.924	30.649	-0.066	-0.066	0.000	0.000	0.000	0.000
78	A	78	ALA	0	-0.019	-0.015	32.995	-0.003	-0.003	0.000	0.000	0.000	0.000
79	A	79	PRO	0	0.004	-0.004	33.242	-0.001	-0.001	0.000	0.000	0.000	0.000
80	A	80	ASN	0	-0.003	-0.013	35.113	0.008	0.008	0.000	0.000	0.000	0.000
81	A	81	PRO	0	0.028	0.009	38.135	0.000	0.000	0.000	0.000	0.000	0.000
82	A	82	GLY	0	-0.051	-0.014	40.256	0.002	0.002	0.000	0.000	0.000	0.000
83	A	83	LEU	0	-0.047	-0.030	36.530	0.001	0.001	0.000	0.000	0.000	0.000
84	A	84	ILE	0	-0.056	-0.016	36.406	-0.002	-0.002	0.000	0.000	0.000	0.000
85	A	85	PRO	0	0.009	0.011	37.478	0.003	0.003	0.000	0.000	0.000	0.000
86	A	86	ASP	-1	-0.848	-0.942	40.442	-0.032	-0.032	0.000	0.000	0.000	0.000
87	A	87	ALA	0	-0.056	-0.032	41.607	0.001	0.001	0.000	0.000	0.000	0.000
88	A	88	ASP	-1	-0.805	-0.902	36.829	-0.038	-0.038	0.000	0.000	0.000	0.000
89	A	89	ALA	0	-0.091	-0.025	38.088	-0.001	-0.001	0.000	0.000	0.000	0.000
90	A	90	VAL	0	-0.042	-0.028	39.267	0.000	0.000	0.000	0.000	0.000	0.000
91	A	91	GLY	0	0.027	0.030	38.892	0.001	0.001	0.000	0.000	0.000	0.000
92	A	92	VAL	0	-0.038	-0.033	32.765	-0.001	-0.001	0.000	0.000	0.000	0.000
93	A	93	THR	0	0.035	0.040	31.912	0.000	0.000	0.000	0.000	0.000	0.000
94	A	94	VAL	0	-0.005	-0.023	25.967	0.004	0.004	0.000	0.000	0.000	0.000
95	A	95	VAL	0	0.004	0.030	26.836	-0.003	-0.003	0.000	0.000	0.000	0.000
96	A	96	LEU	0	-0.044	-0.033	22.012	0.005	0.005	0.000	0.000	0.000	0.000
97	A	97	ILE	0	0.012	0.006	19.453	-0.005	-0.005	0.000	0.000	0.000	0.000
98	A	98	THR	0	-0.002	0.011	18.021	0.010	0.010	0.000	0.000	0.000	0.000
99	A	99	CYS	0	-0.028	-0.016	14.469	-0.012	-0.012	0.000	0.000	0.000	0.000
100	A	100	THR	0	0.023	0.032	14.366	-0.045	-0.045	0.000	0.000	0.000	0.000
101	A	101	TYR	0	0.024	0.015	8.439	-0.067	-0.067	0.000	0.000	0.000	0.000
102	A	102	ARG	1	0.939	0.976	8.792	0.609	0.609	0.000	0.000	0.000	0.000
103	A	103	GLY	0	0.034	-0.001	13.692	0.024	0.024	0.000	0.000	0.000	0.000
104	A	104	GLN	0	-0.036	-0.021	9.362	0.067	0.067	0.000	0.000	0.000	0.000
105	A	105	GLU	-1	-0.773	-0.874	12.806	-0.290	-0.290	0.000	0.000	0.000	0.000
106	A	106	PHE	0	0.017	-0.005	9.259	-0.056	-0.056	0.000	0.000	0.000	0.000
107	A	107	ILE	0	-0.058	-0.037	10.962	0.072	0.072	0.000	0.000	0.000	0.000
108	A	108	ARG	1	0.916	0.947	13.451	0.139	0.139	0.000	0.000	0.000	0.000
109	A	109	VAL	0	-0.037	-0.023	17.104	0.032	0.032	0.000	0.000	0.000	0.000
110	A	110	GLY	0	0.017	0.020	19.395	-0.009	-0.009	0.000	0.000	0.000	0.000
111	A	111	TYR	0	-0.026	-0.024	22.734	0.017	0.017	0.000	0.000	0.000	0.000
112	A	112	TYR	0	0.040	0.019	26.177	-0.003	-0.003	0.000	0.000	0.000	0.000
113	A	113	VAL	0	-0.008	-0.011	29.437	0.001	0.001	0.000	0.000	0.000	0.000
114	A	114	ASN	0	0.014	0.000	32.303	-0.001	-0.001	0.000	0.000	0.000	0.000
115	A	115	ASN	0	0.006	0.004	35.731	-0.001	-0.001	0.000	0.000	0.000	0.000
116	A	116	GLU	-1	-0.854	-0.912	38.617	-0.016	-0.016	0.000	0.000	0.000	0.000
117	A	117	TYR	0	0.045	0.024	42.024	-0.002	-0.002	0.000	0.000	0.000	0.000
118	A	118	THR	0	0.000	-0.011	45.412	0.001	0.001	0.000	0.000	0.000	0.000
119	A	119	GLU	-1	-0.935	-0.964	46.730	-0.019	-0.019	0.000	0.000	0.000	0.000
120	A	120	THR	0	0.020	-0.011	50.252	0.000	0.000	0.000	0.000	0.000	0.000
121	A	121	GLU	-1	-0.884	-0.944	51.677	-0.015	-0.015	0.000	0.000	0.000	0.000
122	A	122	LEU	0	0.001	0.007	49.200	0.000	0.000	0.000	0.000	0.000	0.000
123	A	123	ARG	1	0.799	0.886	44.394	0.015	0.015	0.000	0.000	0.000	0.000
124	A	124	GLU	-1	-0.976	-0.967	48.954	-0.012	-0.012	0.000	0.000	0.000	0.000
125	A	125	ASN	0	-0.088	-0.054	51.979	0.001	0.001	0.000	0.000	0.000	0.000
126	A	126	PRO	0	0.004	0.019	48.172	-0.001	-0.001	0.000	0.000	0.000	0.000
127	A	127	PRO	0	-0.038	-0.023	48.914	0.000	0.000	0.000	0.000	0.000	0.000
128	A	128	VAL	0	-0.026	-0.018	49.292	-0.001	-0.001	0.000	0.000	0.000	0.000
129	A	129	LYS	1	0.900	0.951	45.873	0.033	0.033	0.000	0.000	0.000	0.000
130	A	130	PRO	0	0.012	0.007	43.818	0.001	0.001	0.000	0.000	0.000	0.000
131	A	131	ASP	-1	-0.846	-0.901	46.163	-0.029	-0.029	0.000	0.000	0.000	0.000
132	A	132	PHE	0	0.090	0.006	39.702	0.001	0.001	0.000	0.000	0.000	0.000
133	A	133	SER	0	-0.116	-0.061	43.346	0.000	0.000	0.000	0.000	0.000	0.000
134	A	134	LYS	1	0.926	0.965	45.683	0.026	0.026	0.000	0.000	0.000	0.000
135	A	135	LEU	0	-0.032	0.004	40.854	0.002	0.002	0.000	0.000	0.000	0.000
136	A	136	GLN	0	-0.021	-0.016	39.940	-0.001	-0.001	0.000	0.000	0.000	0.000
137	A	137	ARG	1	0.900	0.953	33.180	0.052	0.052	0.000	0.000	0.000	0.000
138	A	138	ASN	0	-0.013	-0.008	35.682	0.001	0.001	0.000	0.000	0.000	0.000
139	A	139	ILE	0	0.011	0.009	28.820	0.000	0.000	0.000	0.000	0.000	0.000
140	A	140	LEU	0	-0.011	-0.013	30.200	0.004	0.004	0.000	0.000	0.000	0.000
141	A	141	ALA	0	0.020	0.000	27.874	0.000	0.000	0.000	0.000	0.000	0.000
142	A	142	SER	0	-0.013	-0.015	26.976	0.001	0.001	0.000	0.000	0.000	0.000
143	A	143	ASN	0	-0.087	-0.040	26.169	0.012	0.012	0.000	0.000	0.000	0.000
144	A	144	PRO	0	0.052	0.052	21.570	-0.005	-0.005	0.000	0.000	0.000	0.000
145	A	145	ARG	1	0.902	0.947	20.933	0.019	0.019	0.000	0.000	0.000	0.000
146	A	146	VAL	0	-0.003	0.005	14.995	-0.016	-0.016	0.000	0.000	0.000	0.000
147	A	147	THR	0	-0.022	-0.001	14.778	0.037	0.037	0.000	0.000	0.000	0.000
148	A	148	ARG	1	0.934	0.964	9.674	-0.100	-0.100	0.000	0.000	0.000	0.000
149	A	149	PHE	0	0.003	0.006	10.518	0.068	0.068	0.000	0.000	0.000	0.000
150	A	150	HIS	0	-0.037	-0.018	3.368	-0.771	-0.029	0.027	-0.192	-0.577	0.000
151	A	151	ILE	0	0.044	0.030	6.074	0.176	0.176	0.000	0.000	0.000	0.000
152	A	152	ASN	0	-0.050	-0.021	5.181	-0.629	-0.566	-0.001	-0.002	-0.060	0.000
153	A	153	TRP	0	0.077	0.029	3.293	-0.764	-0.115	0.021	-0.131	-0.539	0.000
154	A	154	GLU	-1	-1.012	-0.994	5.315	-0.076	0.019	-0.001	-0.004	-0.091	0.000

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