FMO DATABASE

FMODB ID: 3MZNL

Calculation Name: 2I32-A-Xray547

Preferred Name: Histone chaperone ASF1A

Target Type: SINGLE PROTEIN

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2I32

Chain ID: A

ChEMBL ID: CHEMBL3392950

UniProt ID: Q9Y294

Base Structure: X-ray

Registration Date: 2025-10-05

Reference: Sci Data 11, 1164 (2024).

DOI: https://doi.org/10.1038/s41597-024-03999-2

Apendix: None

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptAll
Protonation	MOE:Protonate 3D
Complement	MOE:Homology Modeling
Water	No
Procedure	Manual calculation
Remarks	ac.sh, 23 2024 Oct; Missing atoms/residues were imported from a 100% homology model, which was constructed by MOE.

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. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1472573.377528
FMO2-HF: Nuclear repulsion	1411250.975751
FMO2-HF: Total energy	-61322.401777
FMO2-MP2: Total energy	-61502.372308

3D Structure Molmil

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.
-162.927	-158.544	2.322	-2.474	-4.228	-0.025

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 : 1 / q_Mulliken : 0.806 / q_NPA : 0.900

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	0.816	0.918	2.928	15.301	18.158	0.158	-1.530	-1.484	-0.012
4	A	4	VAL	0	0.024	0.026	5.343	3.904	4.024	-0.001	-0.007	-0.112	0.000
31	A	31	ILE	0	-0.046	-0.024	3.738	0.421	0.632	0.001	-0.044	-0.167	0.000
150	A	150	HIS	0	-0.036	-0.023	2.620	-9.398	-8.529	2.167	-0.869	-2.167	-0.013
151	A	151	ILE	0	0.023	0.014	4.231	3.040	3.174	-0.001	-0.011	-0.121	0.000
152	A	152	ASN	0	-0.068	-0.042	5.092	-5.947	-5.889	-0.001	0.000	-0.057	0.000
153	A	153	TRP	0	0.023	-0.005	4.472	-1.265	-1.131	-0.001	-0.013	-0.120	0.000
5	A	5	GLN	0	-0.034	-0.015	5.610	-4.392	-4.392	0.000	0.000	0.000	0.000
6	A	6	VAL	0	0.034	0.021	7.655	2.717	2.717	0.000	0.000	0.000	0.000
7	A	7	ASN	0	-0.136	-0.102	10.798	0.165	0.165	0.000	0.000	0.000	0.000
8	A	8	ASN	0	0.025	-0.002	13.225	0.651	0.651	0.000	0.000	0.000	0.000
9	A	9	VAL	0	0.006	0.008	16.825	-0.395	-0.395	0.000	0.000	0.000	0.000
10	A	10	VAL	0	0.022	0.028	19.507	0.385	0.385	0.000	0.000	0.000	0.000
11	A	11	VAL	0	-0.019	-0.012	23.014	0.031	0.031	0.000	0.000	0.000	0.000
12	A	12	LEU	0	-0.018	-0.012	25.720	0.344	0.344	0.000	0.000	0.000	0.000
13	A	13	ASP	-1	-0.875	-0.931	28.574	-9.308	-9.308	0.000	0.000	0.000	0.000
14	A	14	ASN	0	0.035	0.042	29.635	0.195	0.195	0.000	0.000	0.000	0.000
15	A	15	PRO	0	-0.025	-0.017	32.214	-0.060	-0.060	0.000	0.000	0.000	0.000
16	A	16	SER	0	-0.007	-0.005	34.356	0.015	0.015	0.000	0.000	0.000	0.000
17	A	17	PRO	0	0.014	0.000	36.100	0.045	0.045	0.000	0.000	0.000	0.000
18	A	18	PHE	0	0.015	0.012	34.507	-0.248	-0.248	0.000	0.000	0.000	0.000
19	A	19	TYR	0	-0.003	-0.015	35.113	-0.114	-0.114	0.000	0.000	0.000	0.000
20	A	20	ASN	0	-0.058	-0.027	34.487	0.227	0.227	0.000	0.000	0.000	0.000
21	A	21	PRO	0	0.048	0.030	31.549	-0.170	-0.170	0.000	0.000	0.000	0.000
22	A	22	PHE	0	-0.007	0.007	26.875	0.017	0.017	0.000	0.000	0.000	0.000
23	A	23	GLN	0	-0.006	-0.006	27.335	-0.212	-0.212	0.000	0.000	0.000	0.000
24	A	24	PHE	0	0.028	0.006	22.197	-0.051	-0.051	0.000	0.000	0.000	0.000
25	A	25	GLU	-1	-0.907	-0.947	21.765	-13.510	-13.510	0.000	0.000	0.000	0.000
26	A	26	ILE	0	-0.035	-0.005	16.442	-0.538	-0.538	0.000	0.000	0.000	0.000
27	A	27	THR	0	-0.025	-0.016	15.331	0.286	0.286	0.000	0.000	0.000	0.000
28	A	28	PHE	0	-0.002	-0.007	11.619	-0.962	-0.962	0.000	0.000	0.000	0.000
29	A	29	GLU	-1	-0.779	-0.852	8.556	-26.164	-26.164	0.000	0.000	0.000	0.000
30	A	30	CYS	0	-0.018	-0.001	8.534	-3.663	-3.663	0.000	0.000	0.000	0.000
32	A	32	GLU	-1	-0.875	-0.947	7.022	-31.541	-31.541	0.000	0.000	0.000	0.000
33	A	33	ASP	-1	-0.859	-0.921	9.387	-21.283	-21.283	0.000	0.000	0.000	0.000
34	A	34	LEU	0	-0.021	-0.006	9.597	-0.752	-0.752	0.000	0.000	0.000	0.000
35	A	35	SER	0	-0.042	-0.023	13.027	0.939	0.939	0.000	0.000	0.000	0.000
36	A	36	GLU	-1	-0.893	-0.942	15.343	-16.624	-16.624	0.000	0.000	0.000	0.000
37	A	37	ASP	-1	-0.868	-0.941	15.811	-16.820	-16.820	0.000	0.000	0.000	0.000
38	A	38	LEU	0	-0.064	-0.039	11.891	-1.035	-1.035	0.000	0.000	0.000	0.000
39	A	39	GLU	-1	-0.819	-0.914	15.714	-14.342	-14.342	0.000	0.000	0.000	0.000
40	A	40	TRP	0	0.011	-0.007	14.153	-1.369	-1.369	0.000	0.000	0.000	0.000
41	A	41	LYS	1	0.866	0.938	18.280	15.688	15.688	0.000	0.000	0.000	0.000
42	A	42	ILE	0	-0.012	0.009	19.811	-0.628	-0.628	0.000	0.000	0.000	0.000
43	A	43	ILE	0	0.003	-0.005	20.467	0.390	0.390	0.000	0.000	0.000	0.000
44	A	44	TYR	0	0.021	0.012	23.766	-0.291	-0.291	0.000	0.000	0.000	0.000
45	A	45	VAL	0	0.000	0.008	24.585	0.153	0.153	0.000	0.000	0.000	0.000
46	A	46	GLY	0	-0.011	-0.012	27.302	0.185	0.185	0.000	0.000	0.000	0.000
47	A	47	SER	0	-0.002	-0.048	30.265	0.291	0.291	0.000	0.000	0.000	0.000
48	A	48	ALA	0	-0.047	-0.023	28.896	-0.302	-0.302	0.000	0.000	0.000	0.000
49	A	49	GLU	-1	-0.950	-0.959	29.534	-8.626	-8.626	0.000	0.000	0.000	0.000
50	A	50	SER	0	-0.037	-0.035	29.182	-0.104	-0.104	0.000	0.000	0.000	0.000
51	A	51	GLU	-1	-0.903	-0.948	22.481	-12.084	-12.084	0.000	0.000	0.000	0.000
52	A	52	GLU	-1	-0.990	-0.976	27.062	-8.729	-8.729	0.000	0.000	0.000	0.000
53	A	53	TYR	0	-0.074	-0.048	30.040	0.273	0.273	0.000	0.000	0.000	0.000
54	A	54	ASP	-1	-0.894	-0.947	24.663	-11.408	-11.408	0.000	0.000	0.000	0.000
55	A	55	GLN	0	-0.033	-0.017	27.758	0.136	0.136	0.000	0.000	0.000	0.000
56	A	56	VAL	0	-0.025	-0.022	23.903	-0.341	-0.341	0.000	0.000	0.000	0.000
57	A	57	LEU	0	-0.060	-0.013	25.969	0.280	0.280	0.000	0.000	0.000	0.000
58	A	58	ASP	-1	-0.812	-0.914	25.551	-11.433	-11.433	0.000	0.000	0.000	0.000
59	A	59	SER	0	-0.068	-0.052	22.684	-0.745	-0.745	0.000	0.000	0.000	0.000
60	A	60	VAL	0	-0.004	0.017	21.327	0.322	0.322	0.000	0.000	0.000	0.000
61	A	61	LEU	0	-0.009	-0.003	20.224	-0.756	-0.756	0.000	0.000	0.000	0.000
62	A	62	VAL	0	-0.025	-0.016	17.778	0.500	0.500	0.000	0.000	0.000	0.000
63	A	63	GLY	0	0.016	0.007	17.870	-1.330	-1.330	0.000	0.000	0.000	0.000
64	A	64	PRO	0	0.032	0.019	18.844	0.876	0.876	0.000	0.000	0.000	0.000
65	A	65	VAL	0	-0.026	-0.021	13.025	0.150	0.150	0.000	0.000	0.000	0.000
66	A	66	PRO	0	0.028	0.030	13.950	-1.234	-1.234	0.000	0.000	0.000	0.000
67	A	67	ALA	0	0.017	0.011	11.283	-1.076	-1.076	0.000	0.000	0.000	0.000
68	A	68	GLY	0	-0.009	-0.007	11.345	2.139	2.139	0.000	0.000	0.000	0.000
69	A	69	ARG	1	0.809	0.875	12.171	22.018	22.018	0.000	0.000	0.000	0.000
70	A	70	HIS	1	0.790	0.882	14.129	22.027	22.027	0.000	0.000	0.000	0.000
71	A	71	MET	0	0.016	0.009	16.238	-0.496	-0.496	0.000	0.000	0.000	0.000
72	A	72	PHE	0	0.002	0.005	17.296	0.418	0.418	0.000	0.000	0.000	0.000
73	A	73	VAL	0	0.039	0.016	21.324	-0.260	-0.260	0.000	0.000	0.000	0.000
74	A	74	PHE	0	-0.040	-0.009	20.520	0.066	0.066	0.000	0.000	0.000	0.000
75	A	75	GLN	0	-0.002	-0.008	23.903	0.132	0.132	0.000	0.000	0.000	0.000
76	A	76	ALA	0	0.017	0.012	26.129	-0.171	-0.171	0.000	0.000	0.000	0.000
77	A	77	ASP	-1	-0.871	-0.930	28.146	-9.395	-9.395	0.000	0.000	0.000	0.000
78	A	78	ALA	0	-0.016	-0.015	30.486	-0.261	-0.261	0.000	0.000	0.000	0.000
79	A	79	PRO	0	-0.003	0.003	30.841	0.075	0.075	0.000	0.000	0.000	0.000
80	A	80	ASN	0	0.032	0.004	32.649	0.420	0.420	0.000	0.000	0.000	0.000
81	A	81	PRO	0	0.029	-0.003	35.885	-0.042	-0.042	0.000	0.000	0.000	0.000
82	A	82	GLY	0	-0.041	-0.014	38.058	0.078	0.078	0.000	0.000	0.000	0.000
83	A	83	LEU	0	-0.072	-0.033	34.160	0.094	0.094	0.000	0.000	0.000	0.000
84	A	84	ILE	0	-0.012	0.004	33.768	-0.259	-0.259	0.000	0.000	0.000	0.000
85	A	85	PRO	0	0.007	0.016	35.191	0.275	0.275	0.000	0.000	0.000	0.000
86	A	86	ASP	-1	-0.797	-0.897	37.940	-7.292	-7.292	0.000	0.000	0.000	0.000
87	A	87	ALA	0	-0.041	-0.026	38.975	0.036	0.036	0.000	0.000	0.000	0.000
88	A	88	ASP	-1	-0.801	-0.873	33.888	-8.786	-8.786	0.000	0.000	0.000	0.000
89	A	89	ALA	0	-0.060	-0.023	34.763	-0.222	-0.222	0.000	0.000	0.000	0.000
90	A	90	VAL	0	-0.035	-0.023	36.585	-0.075	-0.075	0.000	0.000	0.000	0.000
91	A	91	GLY	0	0.060	0.053	36.075	0.030	0.030	0.000	0.000	0.000	0.000
92	A	92	VAL	0	-0.077	-0.049	29.661	-0.212	-0.212	0.000	0.000	0.000	0.000
93	A	93	THR	0	0.078	0.057	29.497	0.008	0.008	0.000	0.000	0.000	0.000
94	A	94	VAL	0	-0.072	-0.047	23.838	-0.311	-0.311	0.000	0.000	0.000	0.000
95	A	95	VAL	0	0.021	0.030	23.864	0.195	0.195	0.000	0.000	0.000	0.000
96	A	96	LEU	0	-0.033	-0.016	19.072	-0.634	-0.634	0.000	0.000	0.000	0.000
97	A	97	ILE	0	0.018	0.019	17.397	0.329	0.329	0.000	0.000	0.000	0.000
98	A	98	THR	0	-0.038	-0.025	15.449	-0.907	-0.907	0.000	0.000	0.000	0.000
99	A	99	CYS	0	-0.037	-0.014	12.724	0.118	0.118	0.000	0.000	0.000	0.000
100	A	100	THR	0	-0.018	-0.009	12.352	-1.428	-1.428	0.000	0.000	0.000	0.000
101	A	101	TYR	0	0.024	0.006	10.179	0.301	0.301	0.000	0.000	0.000	0.000
102	A	102	ARG	1	0.875	0.930	11.980	21.962	21.962	0.000	0.000	0.000	0.000
103	A	103	GLY	0	0.022	0.018	14.248	0.257	0.257	0.000	0.000	0.000	0.000
104	A	104	GLN	0	0.020	0.029	9.634	-0.088	-0.088	0.000	0.000	0.000	0.000
105	A	105	GLU	-1	-0.783	-0.880	11.217	-19.197	-19.197	0.000	0.000	0.000	0.000
106	A	106	PHE	0	0.009	-0.010	6.993	-1.405	-1.405	0.000	0.000	0.000	0.000
107	A	107	ILE	0	-0.061	-0.031	8.119	-2.024	-2.024	0.000	0.000	0.000	0.000
108	A	108	ARG	1	0.905	0.926	10.704	17.641	17.641	0.000	0.000	0.000	0.000
109	A	109	VAL	0	-0.025	-0.002	14.263	-0.297	-0.297	0.000	0.000	0.000	0.000
110	A	110	GLY	0	0.021	0.011	16.525	0.708	0.708	0.000	0.000	0.000	0.000
111	A	111	TYR	0	-0.005	-0.001	19.642	-0.124	-0.124	0.000	0.000	0.000	0.000
112	A	112	TYR	0	0.039	0.000	22.868	-0.056	-0.056	0.000	0.000	0.000	0.000
113	A	113	VAL	0	-0.014	-0.003	26.171	-0.129	-0.129	0.000	0.000	0.000	0.000
114	A	114	ASN	0	-0.118	-0.075	29.158	0.175	0.175	0.000	0.000	0.000	0.000
115	A	115	ASN	0	0.017	0.003	32.665	-0.097	-0.097	0.000	0.000	0.000	0.000
116	A	116	GLU	-1	-0.798	-0.897	35.612	-7.989	-7.989	0.000	0.000	0.000	0.000
117	A	117	TYR	0	0.065	0.038	39.016	-0.001	-0.001	0.000	0.000	0.000	0.000
118	A	118	THR	0	-0.005	0.001	41.067	0.079	0.079	0.000	0.000	0.000	0.000
119	A	119	GLU	-1	-0.852	-0.938	43.446	-6.379	-6.379	0.000	0.000	0.000	0.000
120	A	120	THR	0	0.017	-0.009	46.941	-0.035	-0.035	0.000	0.000	0.000	0.000
121	A	121	GLU	-1	-0.895	-0.940	48.272	-6.103	-6.103	0.000	0.000	0.000	0.000
122	A	122	LEU	0	0.054	0.025	46.799	-0.026	-0.026	0.000	0.000	0.000	0.000
123	A	123	ARG	1	0.824	0.901	42.622	7.085	7.085	0.000	0.000	0.000	0.000
124	A	124	GLU	-1	-1.012	-0.989	46.007	-6.199	-6.199	0.000	0.000	0.000	0.000
125	A	125	ASN	0	-0.090	-0.044	49.039	0.050	0.050	0.000	0.000	0.000	0.000
126	A	126	PRO	0	0.021	0.022	44.816	0.005	0.005	0.000	0.000	0.000	0.000
127	A	127	PRO	0	-0.037	-0.012	45.964	0.095	0.095	0.000	0.000	0.000	0.000
128	A	128	VAL	0	-0.012	-0.024	46.152	-0.110	-0.110	0.000	0.000	0.000	0.000
129	A	129	LYS	1	0.785	0.885	43.069	6.995	6.995	0.000	0.000	0.000	0.000
130	A	130	PRO	0	0.015	0.008	41.217	0.088	0.088	0.000	0.000	0.000	0.000
131	A	131	ASP	-1	-0.791	-0.866	43.615	-6.897	-6.897	0.000	0.000	0.000	0.000
132	A	132	PHE	0	0.027	-0.017	37.112	-0.063	-0.063	0.000	0.000	0.000	0.000
133	A	133	SER	0	-0.107	-0.069	40.694	-0.108	-0.108	0.000	0.000	0.000	0.000
134	A	134	LYS	1	0.845	0.919	43.345	6.549	6.549	0.000	0.000	0.000	0.000
135	A	135	LEU	0	-0.040	0.007	38.123	-0.031	-0.031	0.000	0.000	0.000	0.000
136	A	136	GLN	0	-0.058	-0.028	36.908	0.006	0.006	0.000	0.000	0.000	0.000
137	A	137	ARG	1	0.863	0.925	30.771	9.770	9.770	0.000	0.000	0.000	0.000
138	A	138	ASN	0	0.000	-0.018	32.493	-0.141	-0.141	0.000	0.000	0.000	0.000
139	A	139	ILE	0	0.020	0.014	25.862	-0.141	-0.141	0.000	0.000	0.000	0.000
140	A	140	LEU	0	-0.002	0.001	26.984	0.011	0.011	0.000	0.000	0.000	0.000
141	A	141	ALA	0	0.003	-0.022	24.673	-0.443	-0.443	0.000	0.000	0.000	0.000
142	A	142	SER	0	-0.022	-0.012	23.705	-0.382	-0.382	0.000	0.000	0.000	0.000
143	A	143	ASN	0	-0.063	-0.028	22.376	-0.669	-0.669	0.000	0.000	0.000	0.000
144	A	144	PRO	0	0.017	0.028	18.202	0.161	0.161	0.000	0.000	0.000	0.000
145	A	145	ARG	1	0.903	0.950	18.071	12.668	12.668	0.000	0.000	0.000	0.000
146	A	146	VAL	0	-0.025	-0.012	11.979	-0.271	-0.271	0.000	0.000	0.000	0.000
147	A	147	THR	0	-0.018	0.004	12.189	-0.218	-0.218	0.000	0.000	0.000	0.000
148	A	148	ARG	1	0.885	0.934	5.611	35.355	35.355	0.000	0.000	0.000	0.000
149	A	149	PHE	0	-0.015	-0.002	7.389	1.006	1.006	0.000	0.000	0.000	0.000
154	A	154	GLU	-2	-1.768	-1.870	8.423	-50.655	-50.655	0.000	0.000	0.000	0.000

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