FMO DATABASE

FMODB ID: NN28Q

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:

Apendix: None

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	154
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1464814.042854
FMO2-HF: Nuclear repulsion	1403492.378272
FMO2-HF: Total energy	-61321.664581
FMO2-MP2: Total energy	-61501.479053

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.
-2.373	1.025	0.124	-1.034	-2.487	-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 : -0.015 / q_NPA : -0.021

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	0.867	0.944	3.850	0.840	2.283	-0.010	-0.557	-0.875	0.001
4	A	4	VAL	0	0.023	0.024	5.655	0.551	0.551	0.000	0.000	0.000	0.000
5	A	5	GLN	0	-0.041	-0.007	8.208	0.043	0.043	0.000	0.000	0.000	0.000
6	A	6	VAL	0	0.019	0.006	9.782	-0.022	-0.022	0.000	0.000	0.000	0.000
7	A	7	ASN	0	-0.084	-0.058	12.856	0.025	0.025	0.000	0.000	0.000	0.000
8	A	8	ASN	0	-0.003	-0.012	15.332	0.028	0.028	0.000	0.000	0.000	0.000
9	A	9	VAL	0	0.005	0.006	18.887	-0.021	-0.021	0.000	0.000	0.000	0.000
10	A	10	VAL	0	-0.004	0.017	21.575	0.012	0.012	0.000	0.000	0.000	0.000
11	A	11	VAL	0	-0.010	0.001	25.250	-0.007	-0.007	0.000	0.000	0.000	0.000
12	A	12	LEU	0	-0.016	-0.004	28.141	0.005	0.005	0.000	0.000	0.000	0.000
13	A	13	ASP	-1	-0.851	-0.910	30.998	-0.024	-0.024	0.000	0.000	0.000	0.000
14	A	14	ASN	0	-0.001	0.028	32.474	-0.002	-0.002	0.000	0.000	0.000	0.000
15	A	15	PRO	0	-0.037	-0.017	34.602	0.002	0.002	0.000	0.000	0.000	0.000
16	A	16	SER	0	0.015	-0.022	35.967	-0.001	-0.001	0.000	0.000	0.000	0.000
17	A	17	PRO	0	0.004	0.005	38.736	0.000	0.000	0.000	0.000	0.000	0.000
18	A	18	PHE	0	0.037	0.019	37.294	-0.002	-0.002	0.000	0.000	0.000	0.000
19	A	19	TYR	0	-0.038	-0.041	37.806	-0.002	-0.002	0.000	0.000	0.000	0.000
20	A	20	ASN	0	-0.077	-0.021	36.394	-0.002	-0.002	0.000	0.000	0.000	0.000
21	A	21	PRO	0	0.070	0.036	33.732	-0.001	-0.001	0.000	0.000	0.000	0.000
22	A	22	PHE	0	-0.033	-0.008	29.340	0.004	0.004	0.000	0.000	0.000	0.000
23	A	23	GLN	0	0.014	-0.019	29.071	-0.001	-0.001	0.000	0.000	0.000	0.000
24	A	24	PHE	0	0.016	0.009	24.203	0.006	0.006	0.000	0.000	0.000	0.000
25	A	25	GLU	-1	-0.922	-0.966	23.610	-0.048	-0.048	0.000	0.000	0.000	0.000
26	A	26	ILE	0	-0.031	-0.007	18.099	0.009	0.009	0.000	0.000	0.000	0.000
27	A	27	THR	0	-0.014	-0.007	17.274	-0.003	-0.003	0.000	0.000	0.000	0.000
28	A	28	PHE	0	0.004	-0.008	13.101	0.021	0.021	0.000	0.000	0.000	0.000
29	A	29	GLU	-1	-0.835	-0.909	10.729	-0.029	-0.029	0.000	0.000	0.000	0.000
30	A	30	CYS	0	-0.012	0.008	9.482	-0.082	-0.082	0.000	0.000	0.000	0.000
31	A	31	ILE	0	-0.021	-0.012	4.424	0.036	0.113	-0.001	-0.003	-0.073	0.000
32	A	32	GLU	-1	-0.891	-0.939	6.516	-0.713	-0.713	0.000	0.000	0.000	0.000
33	A	33	ASP	-1	-0.841	-0.935	8.655	-0.267	-0.267	0.000	0.000	0.000	0.000
34	A	34	LEU	0	-0.069	-0.031	9.493	-0.102	-0.102	0.000	0.000	0.000	0.000
35	A	35	SER	0	-0.043	-0.029	12.413	0.078	0.078	0.000	0.000	0.000	0.000
36	A	36	GLU	-1	-0.889	-0.945	12.693	-0.156	-0.156	0.000	0.000	0.000	0.000
37	A	37	ASP	-1	-0.914	-0.953	14.446	-0.231	-0.231	0.000	0.000	0.000	0.000
38	A	38	LEU	0	-0.026	-0.025	12.749	-0.069	-0.069	0.000	0.000	0.000	0.000
39	A	39	GLU	-1	-0.846	-0.906	15.652	-0.111	-0.111	0.000	0.000	0.000	0.000
40	A	40	TRP	0	0.003	-0.011	15.660	-0.010	-0.010	0.000	0.000	0.000	0.000
41	A	41	LYS	1	0.840	0.909	19.658	0.144	0.144	0.000	0.000	0.000	0.000
42	A	42	ILE	0	0.010	0.010	22.119	-0.001	-0.001	0.000	0.000	0.000	0.000
43	A	43	ILE	0	-0.011	0.008	22.337	0.001	0.001	0.000	0.000	0.000	0.000
44	A	44	TYR	0	0.028	0.009	26.165	0.004	0.004	0.000	0.000	0.000	0.000
45	A	45	VAL	0	0.026	0.011	27.507	-0.001	-0.001	0.000	0.000	0.000	0.000
46	A	46	GLY	0	-0.044	-0.028	30.077	0.004	0.004	0.000	0.000	0.000	0.000
47	A	47	SER	0	-0.037	-0.061	32.874	0.003	0.003	0.000	0.000	0.000	0.000
48	A	48	ALA	0	-0.019	-0.005	31.674	-0.002	-0.002	0.000	0.000	0.000	0.000
49	A	49	GLU	-1	-0.963	-0.966	32.222	-0.019	-0.019	0.000	0.000	0.000	0.000
50	A	50	SER	0	-0.067	-0.051	31.823	-0.001	-0.001	0.000	0.000	0.000	0.000
51	A	51	GLU	-1	-0.886	-0.943	25.347	-0.060	-0.060	0.000	0.000	0.000	0.000
52	A	52	GLU	-1	-0.981	-0.986	29.584	-0.041	-0.041	0.000	0.000	0.000	0.000
53	A	53	TYR	0	-0.086	-0.036	32.182	0.001	0.001	0.000	0.000	0.000	0.000
54	A	54	ASP	-1	-0.848	-0.928	26.696	-0.054	-0.054	0.000	0.000	0.000	0.000
55	A	55	GLN	0	-0.047	-0.019	29.988	0.000	0.000	0.000	0.000	0.000	0.000
56	A	56	VAL	0	-0.020	-0.020	25.330	-0.002	-0.002	0.000	0.000	0.000	0.000
57	A	57	LEU	0	-0.059	-0.022	27.893	0.002	0.002	0.000	0.000	0.000	0.000
58	A	58	ASP	-1	-0.853	-0.923	27.223	-0.076	-0.076	0.000	0.000	0.000	0.000
59	A	59	SER	0	-0.073	-0.083	22.792	-0.008	-0.008	0.000	0.000	0.000	0.000
60	A	60	VAL	0	-0.024	0.016	21.808	0.004	0.004	0.000	0.000	0.000	0.000
61	A	61	LEU	0	0.004	0.007	19.425	-0.019	-0.019	0.000	0.000	0.000	0.000
62	A	62	VAL	0	-0.019	-0.018	18.318	0.015	0.015	0.000	0.000	0.000	0.000
63	A	63	GLY	0	0.036	0.018	18.172	-0.035	-0.035	0.000	0.000	0.000	0.000
64	A	64	PRO	0	-0.014	0.001	17.101	0.027	0.027	0.000	0.000	0.000	0.000
65	A	65	VAL	0	-0.017	-0.024	14.248	0.025	0.025	0.000	0.000	0.000	0.000
66	A	66	PRO	0	-0.009	0.001	14.304	-0.046	-0.046	0.000	0.000	0.000	0.000
67	A	67	ALA	0	0.024	0.010	12.006	-0.025	-0.025	0.000	0.000	0.000	0.000
68	A	68	GLY	0	-0.020	0.000	12.065	0.063	0.063	0.000	0.000	0.000	0.000
69	A	69	ARG	1	0.835	0.910	13.189	-0.004	-0.004	0.000	0.000	0.000	0.000
70	A	70	HIS	0	0.008	-0.001	15.447	0.013	0.013	0.000	0.000	0.000	0.000
71	A	71	MET	0	-0.053	-0.036	17.866	0.010	0.010	0.000	0.000	0.000	0.000
72	A	72	PHE	0	-0.013	0.000	19.170	-0.001	-0.001	0.000	0.000	0.000	0.000
73	A	73	VAL	0	0.045	0.023	23.105	0.003	0.003	0.000	0.000	0.000	0.000
74	A	74	PHE	0	-0.040	-0.013	22.521	-0.005	-0.005	0.000	0.000	0.000	0.000
75	A	75	GLN	0	0.025	0.012	25.695	0.007	0.007	0.000	0.000	0.000	0.000
76	A	76	ALA	0	0.025	0.006	28.407	-0.005	-0.005	0.000	0.000	0.000	0.000
77	A	77	ASP	-1	-0.884	-0.929	30.512	-0.040	-0.040	0.000	0.000	0.000	0.000
78	A	78	ALA	0	-0.020	-0.011	32.873	-0.002	-0.002	0.000	0.000	0.000	0.000
79	A	79	PRO	0	0.002	-0.001	33.351	-0.001	-0.001	0.000	0.000	0.000	0.000
80	A	80	ASN	0	0.011	-0.002	34.988	0.004	0.004	0.000	0.000	0.000	0.000
81	A	81	PRO	0	0.035	0.014	37.887	0.000	0.000	0.000	0.000	0.000	0.000
82	A	82	GLY	0	-0.051	-0.015	40.150	0.001	0.001	0.000	0.000	0.000	0.000
83	A	83	LEU	0	-0.048	-0.030	36.171	0.001	0.001	0.000	0.000	0.000	0.000
84	A	84	ILE	0	-0.050	-0.012	36.328	-0.001	-0.001	0.000	0.000	0.000	0.000
85	A	85	PRO	0	0.007	0.013	37.567	0.002	0.002	0.000	0.000	0.000	0.000
86	A	86	ASP	-1	-0.825	-0.914	40.492	-0.017	-0.017	0.000	0.000	0.000	0.000
87	A	87	ALA	0	-0.033	-0.022	41.735	0.000	0.000	0.000	0.000	0.000	0.000
88	A	88	ASP	-1	-0.765	-0.863	36.650	-0.021	-0.021	0.000	0.000	0.000	0.000
89	A	89	ALA	0	-0.076	-0.020	38.197	0.000	0.000	0.000	0.000	0.000	0.000
90	A	90	VAL	0	-0.037	-0.026	39.365	0.000	0.000	0.000	0.000	0.000	0.000
91	A	91	GLY	0	0.027	0.030	38.950	0.001	0.001	0.000	0.000	0.000	0.000
92	A	92	VAL	0	-0.046	-0.039	32.692	-0.001	-0.001	0.000	0.000	0.000	0.000
93	A	93	THR	0	0.023	0.027	32.210	0.000	0.000	0.000	0.000	0.000	0.000
94	A	94	VAL	0	0.006	-0.011	26.001	0.003	0.003	0.000	0.000	0.000	0.000
95	A	95	VAL	0	0.019	0.032	26.790	-0.002	-0.002	0.000	0.000	0.000	0.000
96	A	96	LEU	0	-0.060	-0.039	22.205	0.004	0.004	0.000	0.000	0.000	0.000
97	A	97	ILE	0	-0.003	0.000	19.878	-0.004	-0.004	0.000	0.000	0.000	0.000
98	A	98	THR	0	-0.008	-0.009	17.399	0.007	0.007	0.000	0.000	0.000	0.000
99	A	99	CYS	0	-0.039	-0.013	14.422	-0.014	-0.014	0.000	0.000	0.000	0.000
100	A	100	THR	0	0.027	0.028	13.684	-0.037	-0.037	0.000	0.000	0.000	0.000
101	A	101	TYR	0	0.032	0.016	8.303	-0.066	-0.066	0.000	0.000	0.000	0.000
102	A	102	ARG	1	0.812	0.890	9.007	0.138	0.138	0.000	0.000	0.000	0.000
103	A	103	GLY	0	0.021	-0.005	13.364	0.028	0.028	0.000	0.000	0.000	0.000
104	A	104	GLN	0	-0.029	-0.022	8.903	0.065	0.065	0.000	0.000	0.000	0.000
105	A	105	GLU	-1	-0.764	-0.863	12.242	-0.209	-0.209	0.000	0.000	0.000	0.000
106	A	106	PHE	0	0.017	-0.007	9.211	-0.046	-0.046	0.000	0.000	0.000	0.000
107	A	107	ILE	0	-0.066	-0.042	11.096	0.057	0.057	0.000	0.000	0.000	0.000
108	A	108	ARG	1	0.942	0.970	13.563	0.087	0.087	0.000	0.000	0.000	0.000
109	A	109	VAL	0	-0.039	-0.022	17.207	0.026	0.026	0.000	0.000	0.000	0.000
110	A	110	GLY	0	0.022	0.028	19.436	-0.007	-0.007	0.000	0.000	0.000	0.000
111	A	111	TYR	0	-0.022	-0.023	22.781	0.008	0.008	0.000	0.000	0.000	0.000
112	A	112	TYR	0	0.043	0.020	26.197	-0.002	-0.002	0.000	0.000	0.000	0.000
113	A	113	VAL	0	0.003	-0.007	29.462	0.001	0.001	0.000	0.000	0.000	0.000
114	A	114	ASN	0	-0.008	-0.006	32.340	0.000	0.000	0.000	0.000	0.000	0.000
115	A	115	ASN	0	0.002	-0.002	35.912	0.000	0.000	0.000	0.000	0.000	0.000
116	A	116	GLU	-1	-0.805	-0.881	38.667	-0.006	-0.006	0.000	0.000	0.000	0.000
117	A	117	TYR	0	0.040	0.022	42.058	-0.001	-0.001	0.000	0.000	0.000	0.000
118	A	118	THR	0	-0.015	-0.016	45.156	0.001	0.001	0.000	0.000	0.000	0.000
119	A	119	GLU	-1	-0.900	-0.955	46.744	-0.010	-0.010	0.000	0.000	0.000	0.000
120	A	120	THR	0	0.007	-0.031	50.276	0.000	0.000	0.000	0.000	0.000	0.000
121	A	121	GLU	-1	-0.884	-0.928	51.684	-0.007	-0.007	0.000	0.000	0.000	0.000
122	A	122	LEU	0	-0.006	0.006	49.316	0.000	0.000	0.000	0.000	0.000	0.000
123	A	123	ARG	1	0.786	0.871	44.212	0.006	0.006	0.000	0.000	0.000	0.000
124	A	124	GLU	-1	-0.971	-0.964	48.983	-0.005	-0.005	0.000	0.000	0.000	0.000
125	A	125	ASN	0	-0.123	-0.071	52.008	0.000	0.000	0.000	0.000	0.000	0.000
126	A	126	PRO	0	0.013	0.021	48.221	-0.001	-0.001	0.000	0.000	0.000	0.000
127	A	127	PRO	0	-0.039	-0.022	49.073	0.000	0.000	0.000	0.000	0.000	0.000
128	A	128	VAL	0	-0.023	-0.016	49.397	0.000	0.000	0.000	0.000	0.000	0.000
129	A	129	LYS	1	0.849	0.905	45.604	0.018	0.018	0.000	0.000	0.000	0.000
130	A	130	PRO	0	0.015	0.013	43.925	0.000	0.000	0.000	0.000	0.000	0.000
131	A	131	ASP	-1	-0.784	-0.852	46.282	-0.016	-0.016	0.000	0.000	0.000	0.000
132	A	132	PHE	0	0.091	0.011	40.030	0.000	0.000	0.000	0.000	0.000	0.000
133	A	133	SER	0	-0.125	-0.078	43.440	0.000	0.000	0.000	0.000	0.000	0.000
134	A	134	LYS	1	0.862	0.922	45.780	0.014	0.014	0.000	0.000	0.000	0.000
135	A	135	LEU	0	-0.033	0.007	41.122	0.001	0.001	0.000	0.000	0.000	0.000
136	A	136	GLN	0	-0.013	-0.005	39.895	-0.001	-0.001	0.000	0.000	0.000	0.000
137	A	137	ARG	1	0.847	0.914	33.408	0.031	0.031	0.000	0.000	0.000	0.000
138	A	138	ASN	0	-0.041	-0.033	35.683	0.001	0.001	0.000	0.000	0.000	0.000
139	A	139	ILE	0	0.032	0.016	28.867	0.001	0.001	0.000	0.000	0.000	0.000
140	A	140	LEU	0	-0.012	-0.008	30.128	0.003	0.003	0.000	0.000	0.000	0.000
141	A	141	ALA	0	0.020	0.002	27.822	0.001	0.001	0.000	0.000	0.000	0.000
142	A	142	SER	0	-0.013	-0.014	26.893	0.001	0.001	0.000	0.000	0.000	0.000
143	A	143	ASN	0	-0.063	-0.032	26.053	0.009	0.009	0.000	0.000	0.000	0.000
144	A	144	PRO	0	0.058	0.053	21.490	-0.004	-0.004	0.000	0.000	0.000	0.000
145	A	145	ARG	1	0.855	0.927	20.876	0.001	0.001	0.000	0.000	0.000	0.000
146	A	146	VAL	0	0.000	0.005	14.894	-0.012	-0.012	0.000	0.000	0.000	0.000
147	A	147	THR	0	-0.031	-0.006	14.998	0.029	0.029	0.000	0.000	0.000	0.000
148	A	148	ARG	1	0.933	0.963	9.715	-0.109	-0.109	0.000	0.000	0.000	0.000
149	A	149	PHE	0	-0.010	0.003	10.646	0.058	0.058	0.000	0.000	0.000	0.000
150	A	150	HIS	0	-0.036	-0.018	3.095	-0.856	0.080	0.073	-0.270	-0.739	-0.001
151	A	151	ILE	0	0.036	0.020	5.941	0.173	0.173	0.000	0.000	0.000	0.000
152	A	152	ASN	0	-0.040	-0.014	5.176	-0.489	-0.421	-0.001	-0.002	-0.064	0.000
153	A	153	TRP	0	0.068	0.025	3.074	-1.053	-0.261	0.064	-0.196	-0.661	-0.001
154	A	154	GLU	-1	-0.934	-0.935	5.102	0.211	0.293	-0.001	-0.006	-0.075	0.000

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