FMO DATABASE

FMODB ID: NLVQQ

Calculation Name: 1ITF-A-Other547

Preferred Name: Interferon alpha

Target Type: PROTEIN FAMILY

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1ITF

Chain ID: A

ChEMBL ID: CHEMBL3856161

UniProt ID: P01563

Base Structure: SolutionNMR

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	163
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1786030.415284
FMO2-HF: Nuclear repulsion	1717650.169792
FMO2-HF: Total energy	-68380.245491
FMO2-MP2: Total energy	-68576.521845

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:CYS)

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

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.
-110.274	-92.145	23.498	-15.277	-26.351	-0.034

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.659 / q_NPA : 0.813

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	LEU	0	0.016	0.016	2.249	-0.534	3.708	4.908	-3.539	-5.611	-0.003
4	A	4	PRO	0	0.011	0.012	3.533	2.418	3.363	0.261	-0.191	-1.015	0.000
50	A	50	ALA	0	-0.018	-0.027	2.196	-8.693	-9.140	4.586	-1.553	-2.586	-0.006
51	A	51	GLU	-1	-0.718	-0.822	4.286	-29.823	-29.614	-0.002	-0.027	-0.180	0.000
53	A	53	ILE	0	-0.019	0.012	2.100	1.834	0.649	6.321	-1.337	-3.798	0.001
94	A	94	ASP	-1	-0.852	-0.918	3.631	-39.020	-38.581	0.059	-0.141	-0.357	-0.003
95	A	95	LEU	0	-0.102	-0.062	2.872	-11.578	-8.693	0.215	-1.215	-1.884	-0.013
96	A	96	GLU	-1	-0.884	-0.954	2.703	-40.972	-36.260	0.747	-2.739	-2.720	-0.025
99	A	100	ILE	0	-0.017	0.013	2.947	2.064	5.802	0.428	-1.700	-2.467	0.012
100	A	101	GLN	0	-0.028	-0.010	2.997	-2.048	0.551	0.184	-1.156	-1.628	0.012
101	A	102	GLY	0	0.024	0.009	4.872	-2.801	-2.891	-0.002	-0.013	0.104	0.000
102	A	103	VAL	0	-0.046	-0.018	2.252	-4.621	-5.234	5.779	-1.387	-3.780	-0.008
103	A	104	GLY	0	0.032	0.024	3.625	-0.981	-0.441	0.015	-0.256	-0.299	-0.001
104	A	105	VAL	0	-0.102	-0.063	4.361	4.965	5.120	-0.001	-0.023	-0.130	0.000
5	A	5	GLN	0	0.001	0.009	6.544	0.886	0.886	0.000	0.000	0.000	0.000
6	A	6	THR	0	-0.013	-0.004	9.342	1.835	1.835	0.000	0.000	0.000	0.000
7	A	7	HIS	0	-0.016	-0.021	10.643	1.148	1.148	0.000	0.000	0.000	0.000
8	A	8	SER	0	0.076	0.041	9.559	-2.799	-2.799	0.000	0.000	0.000	0.000
9	A	9	LEU	0	-0.035	-0.025	10.782	0.826	0.826	0.000	0.000	0.000	0.000
10	A	10	GLY	0	0.074	0.041	12.572	1.498	1.498	0.000	0.000	0.000	0.000
11	A	11	SER	0	0.029	0.030	12.647	1.420	1.420	0.000	0.000	0.000	0.000
12	A	12	ARG	1	0.891	0.938	14.339	17.195	17.195	0.000	0.000	0.000	0.000
13	A	13	ARG	1	0.961	0.985	16.175	18.055	18.055	0.000	0.000	0.000	0.000
14	A	14	THR	0	0.039	0.011	15.117	0.648	0.648	0.000	0.000	0.000	0.000
15	A	15	LEU	0	-0.022	-0.008	17.567	0.895	0.895	0.000	0.000	0.000	0.000
16	A	16	MET	0	-0.029	-0.007	20.309	0.690	0.690	0.000	0.000	0.000	0.000
17	A	17	LEU	0	-0.003	0.006	18.929	0.654	0.654	0.000	0.000	0.000	0.000
18	A	18	LEU	0	0.034	0.004	19.444	0.680	0.680	0.000	0.000	0.000	0.000
19	A	19	ALA	0	-0.045	-0.033	23.237	0.538	0.538	0.000	0.000	0.000	0.000
20	A	20	GLN	0	-0.048	-0.040	25.389	0.126	0.126	0.000	0.000	0.000	0.000
21	A	21	MET	0	-0.015	0.011	22.894	0.220	0.220	0.000	0.000	0.000	0.000
22	A	22	ARG	1	0.913	0.976	27.336	10.563	10.563	0.000	0.000	0.000	0.000
23	A	23	LYS	1	0.850	0.929	30.048	9.482	9.482	0.000	0.000	0.000	0.000
24	A	24	ILE	0	-0.017	-0.007	33.527	0.300	0.300	0.000	0.000	0.000	0.000
25	A	25	SER	0	0.013	-0.004	33.435	-0.282	-0.282	0.000	0.000	0.000	0.000
26	A	26	LEU	0	0.040	0.030	30.880	0.323	0.323	0.000	0.000	0.000	0.000
27	A	27	PHE	0	-0.002	-0.023	34.168	0.122	0.122	0.000	0.000	0.000	0.000
28	A	28	SER	0	-0.012	0.002	37.615	0.273	0.273	0.000	0.000	0.000	0.000
29	A	29	CYS	0	-0.062	-0.036	33.647	0.034	0.034	0.000	0.000	0.000	0.000
30	A	30	LEU	0	-0.006	0.003	36.454	-0.151	-0.151	0.000	0.000	0.000	0.000
31	A	31	LYS	1	0.944	0.971	38.217	7.290	7.290	0.000	0.000	0.000	0.000
32	A	32	ASP	-1	-0.796	-0.899	35.011	-8.213	-8.213	0.000	0.000	0.000	0.000
33	A	33	ARG	1	0.918	0.973	33.069	8.859	8.859	0.000	0.000	0.000	0.000
34	A	34	HIS	0	-0.017	-0.013	32.223	0.036	0.036	0.000	0.000	0.000	0.000
35	A	35	ASP	-1	-0.879	-0.918	27.658	-11.295	-11.295	0.000	0.000	0.000	0.000
36	A	36	PHE	0	-0.055	-0.054	26.036	0.336	0.336	0.000	0.000	0.000	0.000
37	A	37	GLY	0	0.001	0.008	26.521	-0.001	-0.001	0.000	0.000	0.000	0.000
38	A	38	PHE	0	-0.012	-0.015	17.067	-0.053	-0.053	0.000	0.000	0.000	0.000
39	A	39	PRO	0	-0.001	0.001	19.243	0.159	0.159	0.000	0.000	0.000	0.000
40	A	40	GLN	0	-0.027	-0.043	18.992	-0.149	-0.149	0.000	0.000	0.000	0.000
41	A	41	GLU	-1	-0.935	-0.950	19.798	-13.468	-13.468	0.000	0.000	0.000	0.000
42	A	42	GLU	-1	-0.904	-0.956	16.772	-16.791	-16.791	0.000	0.000	0.000	0.000
43	A	43	PHE	0	-0.015	-0.020	12.169	-1.343	-1.343	0.000	0.000	0.000	0.000
44	A	44	GLY	0	0.025	0.021	16.503	0.073	0.073	0.000	0.000	0.000	0.000
45	A	45	ASN	0	0.015	-0.003	15.888	-0.345	-0.345	0.000	0.000	0.000	0.000
46	A	46	GLN	0	-0.075	-0.026	10.835	0.877	0.877	0.000	0.000	0.000	0.000
47	A	47	PHE	0	0.022	0.012	10.822	-1.630	-1.630	0.000	0.000	0.000	0.000
48	A	48	GLN	0	-0.014	-0.021	9.140	1.080	1.080	0.000	0.000	0.000	0.000
49	A	49	LYS	1	0.822	0.897	5.947	27.604	27.604	0.000	0.000	0.000	0.000
52	A	52	THR	0	0.041	0.013	7.321	2.996	2.996	0.000	0.000	0.000	0.000
54	A	54	PRO	0	0.062	0.023	5.259	1.353	1.353	0.000	0.000	0.000	0.000
55	A	55	VAL	0	0.001	0.002	6.883	2.277	2.277	0.000	0.000	0.000	0.000
56	A	56	LEU	0	-0.048	-0.024	7.679	2.106	2.106	0.000	0.000	0.000	0.000
57	A	57	HIS	0	-0.018	0.002	6.525	0.918	0.918	0.000	0.000	0.000	0.000
58	A	58	GLU	-1	-0.825	-0.915	8.627	-18.882	-18.882	0.000	0.000	0.000	0.000
59	A	59	MET	0	-0.079	-0.026	11.867	1.441	1.441	0.000	0.000	0.000	0.000
60	A	60	ILE	0	-0.009	-0.004	10.224	1.551	1.551	0.000	0.000	0.000	0.000
61	A	61	GLN	0	0.051	0.038	12.214	1.703	1.703	0.000	0.000	0.000	0.000
62	A	62	GLN	0	-0.036	-0.017	13.938	1.361	1.361	0.000	0.000	0.000	0.000
63	A	63	ILE	0	-0.047	-0.028	15.629	1.109	1.109	0.000	0.000	0.000	0.000
64	A	64	PHE	0	0.003	0.010	15.270	0.893	0.893	0.000	0.000	0.000	0.000
65	A	65	ASN	0	0.026	0.003	17.337	1.072	1.072	0.000	0.000	0.000	0.000
66	A	66	LEU	0	-0.045	-0.013	19.855	0.687	0.687	0.000	0.000	0.000	0.000
67	A	67	PHE	0	0.023	-0.016	20.613	0.680	0.680	0.000	0.000	0.000	0.000
68	A	68	SER	0	0.030	0.048	20.416	0.573	0.573	0.000	0.000	0.000	0.000
69	A	69	THR	0	-0.065	-0.020	22.502	0.605	0.605	0.000	0.000	0.000	0.000
70	A	70	LYS	1	0.976	0.982	25.567	8.917	8.917	0.000	0.000	0.000	0.000
71	A	71	ASP	-1	-0.912	-0.971	28.628	-9.308	-9.308	0.000	0.000	0.000	0.000
72	A	72	SER	0	0.006	-0.010	25.449	0.075	0.075	0.000	0.000	0.000	0.000
73	A	73	SER	0	-0.048	-0.034	25.651	0.166	0.166	0.000	0.000	0.000	0.000
74	A	74	ALA	0	0.007	0.015	27.531	0.131	0.131	0.000	0.000	0.000	0.000
75	A	75	ALA	0	-0.040	0.003	29.462	0.271	0.271	0.000	0.000	0.000	0.000
76	A	76	TRP	0	-0.028	-0.028	26.042	0.190	0.190	0.000	0.000	0.000	0.000
77	A	77	ASP	-1	-0.802	-0.897	28.883	-9.231	-9.231	0.000	0.000	0.000	0.000
78	A	78	GLU	-1	-0.781	-0.872	27.049	-9.886	-9.886	0.000	0.000	0.000	0.000
79	A	79	THR	0	-0.020	-0.034	25.641	-0.402	-0.402	0.000	0.000	0.000	0.000
80	A	80	LEU	0	-0.069	-0.039	24.892	-0.432	-0.432	0.000	0.000	0.000	0.000
81	A	81	LEU	0	-0.039	-0.020	22.940	-0.638	-0.638	0.000	0.000	0.000	0.000
82	A	82	ASP	-1	-0.898	-0.929	21.413	-12.644	-12.644	0.000	0.000	0.000	0.000
83	A	83	LYS	1	0.950	0.984	19.005	13.729	13.729	0.000	0.000	0.000	0.000
84	A	84	PHE	0	-0.005	-0.015	18.694	-0.912	-0.912	0.000	0.000	0.000	0.000
85	A	85	TYR	0	0.015	-0.028	17.370	-0.744	-0.744	0.000	0.000	0.000	0.000
86	A	86	THR	0	0.020	0.004	15.526	-0.897	-0.897	0.000	0.000	0.000	0.000
87	A	87	GLU	-1	-0.947	-0.983	14.089	-19.090	-19.090	0.000	0.000	0.000	0.000
88	A	88	LEU	0	-0.023	-0.017	13.048	-1.424	-1.424	0.000	0.000	0.000	0.000
89	A	89	TYR	0	0.028	0.002	11.319	-1.576	-1.576	0.000	0.000	0.000	0.000
90	A	90	GLN	0	-0.085	-0.025	9.133	-0.030	-0.030	0.000	0.000	0.000	0.000
91	A	91	GLN	0	0.011	-0.017	8.461	-2.291	-2.291	0.000	0.000	0.000	0.000
92	A	92	LEU	0	-0.031	-0.011	7.221	-2.999	-2.999	0.000	0.000	0.000	0.000
93	A	93	ASN	0	0.038	0.021	5.633	-3.210	-3.210	0.000	0.000	0.000	0.000
105	A	106	THR	0	0.052	0.038	6.639	1.528	1.528	0.000	0.000	0.000	0.000
106	A	107	GLU	-1	-0.909	-0.968	9.306	-23.614	-23.614	0.000	0.000	0.000	0.000
107	A	108	THR	0	-0.041	-0.015	9.880	1.842	1.842	0.000	0.000	0.000	0.000
108	A	109	PRO	0	0.033	0.019	12.584	-0.241	-0.241	0.000	0.000	0.000	0.000
109	A	110	LEU	0	0.030	-0.011	14.496	-0.968	-0.968	0.000	0.000	0.000	0.000
110	A	111	MET	0	0.050	0.045	14.876	0.082	0.082	0.000	0.000	0.000	0.000
111	A	112	LYS	1	0.894	0.947	10.011	24.602	24.602	0.000	0.000	0.000	0.000
112	A	113	GLU	-1	-0.945	-0.976	13.011	-16.696	-16.696	0.000	0.000	0.000	0.000
113	A	114	ASP	-1	-0.867	-0.923	14.997	-14.836	-14.836	0.000	0.000	0.000	0.000
114	A	115	SER	0	0.035	0.002	13.619	0.646	0.646	0.000	0.000	0.000	0.000
115	A	116	ILE	0	0.000	0.013	11.231	0.444	0.444	0.000	0.000	0.000	0.000
116	A	117	LEU	0	0.001	-0.008	15.082	1.059	1.059	0.000	0.000	0.000	0.000
117	A	118	ALA	0	-0.031	-0.029	18.450	0.983	0.983	0.000	0.000	0.000	0.000
118	A	119	VAL	0	0.045	0.021	15.229	0.843	0.843	0.000	0.000	0.000	0.000
119	A	120	ARG	1	0.933	0.970	18.149	13.664	13.664	0.000	0.000	0.000	0.000
120	A	121	LYS	1	0.912	0.964	19.676	13.604	13.604	0.000	0.000	0.000	0.000
121	A	122	TYR	0	-0.026	-0.022	20.707	0.310	0.310	0.000	0.000	0.000	0.000
122	A	123	PHE	0	0.074	0.011	18.490	0.485	0.485	0.000	0.000	0.000	0.000
123	A	124	GLN	0	-0.023	0.010	22.274	0.221	0.221	0.000	0.000	0.000	0.000
124	A	125	ARG	1	0.951	0.979	24.970	10.341	10.341	0.000	0.000	0.000	0.000
125	A	126	ILE	0	0.027	0.018	22.832	0.466	0.466	0.000	0.000	0.000	0.000
126	A	127	THR	0	-0.029	-0.035	24.766	0.368	0.368	0.000	0.000	0.000	0.000
127	A	128	LEU	0	-0.025	-0.006	27.333	0.316	0.316	0.000	0.000	0.000	0.000
128	A	129	TYR	0	-0.008	-0.033	30.037	0.469	0.469	0.000	0.000	0.000	0.000
129	A	130	LEU	0	0.020	0.016	27.090	0.327	0.327	0.000	0.000	0.000	0.000
130	A	131	LYS	1	0.899	0.946	29.620	9.704	9.704	0.000	0.000	0.000	0.000
131	A	132	GLU	-1	-0.944	-0.962	33.486	-7.952	-7.952	0.000	0.000	0.000	0.000
132	A	133	LYS	1	0.841	0.917	34.720	8.710	8.710	0.000	0.000	0.000	0.000
133	A	134	LYS	1	0.865	0.942	35.707	7.768	7.768	0.000	0.000	0.000	0.000
134	A	135	TYR	0	0.040	0.025	28.931	0.149	0.149	0.000	0.000	0.000	0.000
135	A	136	SER	0	0.015	0.026	33.659	0.045	0.045	0.000	0.000	0.000	0.000
136	A	137	PRO	0	0.065	0.024	33.896	-0.277	-0.277	0.000	0.000	0.000	0.000
137	A	139	ALA	0	0.022	0.014	32.716	-0.212	-0.212	0.000	0.000	0.000	0.000
138	A	140	TRP	0	0.034	0.020	25.729	-0.498	-0.498	0.000	0.000	0.000	0.000
139	A	141	GLU	-1	-0.876	-0.962	29.026	-10.308	-10.308	0.000	0.000	0.000	0.000
140	A	142	VAL	0	-0.041	-0.014	29.619	-0.289	-0.289	0.000	0.000	0.000	0.000
141	A	143	VAL	0	0.003	-0.010	25.334	-0.348	-0.348	0.000	0.000	0.000	0.000
142	A	144	ARG	1	0.835	0.960	23.780	11.036	11.036	0.000	0.000	0.000	0.000
143	A	145	ALA	0	-0.010	-0.012	25.011	-0.485	-0.485	0.000	0.000	0.000	0.000
144	A	146	GLU	-1	-0.813	-0.882	25.065	-12.015	-12.015	0.000	0.000	0.000	0.000
145	A	147	ILE	0	-0.005	0.019	19.867	-0.580	-0.580	0.000	0.000	0.000	0.000
146	A	148	MET	0	-0.033	0.005	20.230	-0.648	-0.648	0.000	0.000	0.000	0.000
147	A	149	ARG	1	0.961	0.980	20.727	11.172	11.172	0.000	0.000	0.000	0.000
148	A	150	SER	0	0.037	0.006	19.353	-0.712	-0.712	0.000	0.000	0.000	0.000
149	A	151	PHE	0	0.040	0.014	12.670	-0.821	-0.821	0.000	0.000	0.000	0.000
150	A	152	SER	0	-0.102	-0.047	16.026	-0.972	-0.972	0.000	0.000	0.000	0.000
151	A	153	LEU	0	-0.037	-0.018	17.497	-0.612	-0.612	0.000	0.000	0.000	0.000
152	A	154	SER	0	0.029	0.002	13.384	-0.227	-0.227	0.000	0.000	0.000	0.000
153	A	155	THR	0	-0.008	-0.034	11.924	-1.403	-1.403	0.000	0.000	0.000	0.000
154	A	156	ASN	0	-0.069	-0.037	13.498	-0.614	-0.614	0.000	0.000	0.000	0.000
155	A	157	LEU	0	-0.057	-0.013	11.354	0.031	0.031	0.000	0.000	0.000	0.000
156	A	158	GLN	0	-0.038	-0.007	6.046	-2.201	-2.201	0.000	0.000	0.000	0.000
157	A	159	GLU	-1	-0.831	-0.923	10.527	-22.008	-22.008	0.000	0.000	0.000	0.000
158	A	160	SER	0	-0.091	-0.022	13.283	1.930	1.930	0.000	0.000	0.000	0.000
159	A	161	LEU	0	0.035	0.005	16.125	1.141	1.141	0.000	0.000	0.000	0.000
160	A	162	ARG	1	0.897	0.931	18.645	12.935	12.935	0.000	0.000	0.000	0.000
161	A	163	SER	0	-0.021	-0.002	20.701	0.481	0.481	0.000	0.000	0.000	0.000
162	A	164	LYS	1	0.923	0.947	18.497	15.383	15.383	0.000	0.000	0.000	0.000
163	A	165	GLU	-2	-1.864	-1.901	22.667	-22.445	-22.445	0.000	0.000	0.000	0.000

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