FMO DATABASE

FMODB ID: JVM19

Calculation Name: 1NUN-A-Xray547

Preferred Name:

Target Type:

Ligand Name: polyethylene glycol (n=34) | sulfate ion

Ligand 3-letter code: 15P | SO4

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1NUN

Chain ID: A

ChEMBL ID:

UniProt ID: O15520

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	139
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1368195.361213
FMO2-HF: Nuclear repulsion	1311833.868192
FMO2-HF: Total energy	-56361.49302
FMO2-MP2: Total energy	-56526.053017

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:69:SER)

Summations of interaction energy for fragment #1(A:69:SER)

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.
119.719	123.269	4.271	-3.725	-4.096	-0.042

Interaction energy analysis for fragmet #1(A:69:SER)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.840 / q_NPA : 0.910

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	71	ASN	0	0.062	0.046	1.999	-23.821	-20.710	4.273	-3.636	-3.749	-0.042
4	A	72	HIS	0	0.053	0.020	4.107	3.250	3.661	-0.001	-0.087	-0.323	0.000
137	A	205	VAL	0	0.014	-0.002	4.799	2.928	2.956	-0.001	-0.002	-0.024	0.000
5	A	73	LEU	0	-0.007	0.001	6.007	6.734	6.734	0.000	0.000	0.000	0.000
6	A	74	GLN	0	-0.010	0.013	7.360	2.091	2.091	0.000	0.000	0.000	0.000
7	A	75	GLY	0	0.048	0.020	9.327	-0.259	-0.259	0.000	0.000	0.000	0.000
8	A	76	ASP	-1	-0.875	-0.930	12.379	-16.699	-16.699	0.000	0.000	0.000	0.000
9	A	77	VAL	0	-0.007	0.003	15.688	-0.310	-0.310	0.000	0.000	0.000	0.000
10	A	78	ARG	1	0.786	0.885	11.029	23.628	23.628	0.000	0.000	0.000	0.000
11	A	79	TRP	0	0.015	0.012	12.902	0.445	0.445	0.000	0.000	0.000	0.000
12	A	80	ARG	1	0.828	0.901	9.000	28.149	28.149	0.000	0.000	0.000	0.000
13	A	81	LYS	1	0.924	0.983	11.995	21.906	21.906	0.000	0.000	0.000	0.000
14	A	82	LEU	0	0.005	0.011	13.242	-0.925	-0.925	0.000	0.000	0.000	0.000
15	A	83	PHE	0	0.010	0.001	13.766	1.470	1.470	0.000	0.000	0.000	0.000
16	A	84	SER	0	0.016	-0.002	15.703	-0.452	-0.452	0.000	0.000	0.000	0.000
17	A	85	PHE	0	0.065	0.035	17.806	-0.331	-0.331	0.000	0.000	0.000	0.000
18	A	86	THR	0	-0.086	-0.036	19.084	-0.047	-0.047	0.000	0.000	0.000	0.000
19	A	87	LYS	1	0.901	0.963	16.954	17.017	17.017	0.000	0.000	0.000	0.000
20	A	88	TYR	0	0.041	0.024	19.284	0.178	0.178	0.000	0.000	0.000	0.000
21	A	89	PHE	0	0.034	0.020	13.839	-0.417	-0.417	0.000	0.000	0.000	0.000
22	A	90	LEU	0	-0.036	-0.016	18.747	1.071	1.071	0.000	0.000	0.000	0.000
23	A	91	LYS	1	0.869	0.939	19.968	11.529	11.529	0.000	0.000	0.000	0.000
24	A	92	ILE	0	-0.002	0.001	22.627	0.541	0.541	0.000	0.000	0.000	0.000
25	A	93	GLU	-1	-0.799	-0.872	25.585	-11.343	-11.343	0.000	0.000	0.000	0.000
26	A	94	LYS	1	0.969	0.968	27.936	10.974	10.974	0.000	0.000	0.000	0.000
27	A	95	ASN	0	0.029	0.021	30.271	-0.018	-0.018	0.000	0.000	0.000	0.000
28	A	96	GLY	0	0.057	0.041	30.506	0.240	0.240	0.000	0.000	0.000	0.000
29	A	97	LYS	1	0.790	0.885	28.740	10.635	10.635	0.000	0.000	0.000	0.000
30	A	98	VAL	0	0.020	0.020	25.415	-0.288	-0.288	0.000	0.000	0.000	0.000
31	A	99	SER	0	-0.056	-0.030	25.786	0.548	0.548	0.000	0.000	0.000	0.000
32	A	100	GLY	0	0.039	0.014	22.997	-0.547	-0.547	0.000	0.000	0.000	0.000
33	A	101	THR	0	-0.034	-0.036	22.118	0.749	0.749	0.000	0.000	0.000	0.000
34	A	102	LYS	1	0.911	0.945	18.783	15.161	15.161	0.000	0.000	0.000	0.000
35	A	103	LYS	0	0.041	0.037	20.860	-0.434	-0.434	0.000	0.000	0.000	0.000
36	A	104	GLU	-1	-0.862	-0.937	16.210	-18.668	-18.668	0.000	0.000	0.000	0.000
37	A	105	ASN	0	0.042	0.011	16.845	-1.463	-1.463	0.000	0.000	0.000	0.000
38	A	106	CYS	0	-0.063	-0.015	19.194	0.462	0.462	0.000	0.000	0.000	0.000
39	A	107	PRO	0	0.112	0.056	19.730	-0.593	-0.593	0.000	0.000	0.000	0.000
40	A	108	TYR	0	-0.002	-0.009	20.801	0.014	0.014	0.000	0.000	0.000	0.000
41	A	109	SER	0	-0.051	-0.046	18.390	-0.065	-0.065	0.000	0.000	0.000	0.000
42	A	110	ILE	0	0.004	0.016	15.519	-0.989	-0.989	0.000	0.000	0.000	0.000
43	A	111	LEU	0	-0.055	-0.033	16.072	1.241	1.241	0.000	0.000	0.000	0.000
44	A	112	GLU	-1	-0.861	-0.934	15.674	-16.515	-16.515	0.000	0.000	0.000	0.000
45	A	113	ILE	0	-0.039	-0.024	14.545	1.137	1.137	0.000	0.000	0.000	0.000
46	A	114	THR	0	0.077	0.034	16.649	-0.835	-0.835	0.000	0.000	0.000	0.000
47	A	115	SER	0	-0.007	0.005	19.105	0.560	0.560	0.000	0.000	0.000	0.000
48	A	116	VAL	0	-0.013	-0.017	20.947	0.357	0.357	0.000	0.000	0.000	0.000
49	A	117	GLU	-1	-0.825	-0.905	24.304	-10.315	-10.315	0.000	0.000	0.000	0.000
50	A	118	ILE	0	0.063	0.028	23.190	-0.654	-0.654	0.000	0.000	0.000	0.000
51	A	119	GLY	0	-0.012	0.002	20.988	0.318	0.318	0.000	0.000	0.000	0.000
52	A	120	VAL	0	-0.084	-0.049	22.077	0.077	0.077	0.000	0.000	0.000	0.000
53	A	121	VAL	0	0.028	0.006	18.454	-0.166	-0.166	0.000	0.000	0.000	0.000
54	A	122	ALA	0	0.018	0.026	21.782	0.698	0.698	0.000	0.000	0.000	0.000
55	A	123	VAL	0	-0.007	-0.005	18.968	-0.703	-0.703	0.000	0.000	0.000	0.000
56	A	124	LYS	1	0.927	0.975	20.221	13.549	13.549	0.000	0.000	0.000	0.000
57	A	125	ALA	0	0.002	0.012	20.342	-0.823	-0.823	0.000	0.000	0.000	0.000
58	A	126	ILE	0	0.018	0.003	18.773	0.775	0.775	0.000	0.000	0.000	0.000
59	A	127	ASN	0	0.023	0.006	20.433	0.785	0.785	0.000	0.000	0.000	0.000
60	A	128	SER	0	-0.076	-0.075	23.799	0.547	0.547	0.000	0.000	0.000	0.000
61	A	129	ASN	0	0.008	0.007	25.084	0.370	0.370	0.000	0.000	0.000	0.000
62	A	130	TYR	0	-0.050	-0.022	25.698	0.506	0.506	0.000	0.000	0.000	0.000
63	A	131	TYR	0	0.082	0.028	24.206	-0.541	-0.541	0.000	0.000	0.000	0.000
64	A	132	LEU	0	-0.020	-0.026	22.287	0.506	0.506	0.000	0.000	0.000	0.000
65	A	133	ALA	0	0.047	0.028	25.439	-0.088	-0.088	0.000	0.000	0.000	0.000
66	A	134	MET	0	-0.058	-0.035	28.650	0.134	0.134	0.000	0.000	0.000	0.000
67	A	135	ASN	0	0.063	0.044	30.771	0.234	0.234	0.000	0.000	0.000	0.000
68	A	136	LYS	1	1.016	0.999	34.565	7.750	7.750	0.000	0.000	0.000	0.000
69	A	137	LYS	1	0.961	0.993	36.860	7.942	7.942	0.000	0.000	0.000	0.000
70	A	138	GLY	0	0.038	0.001	33.547	0.082	0.082	0.000	0.000	0.000	0.000
71	A	139	LYS	1	0.837	0.917	32.972	9.258	9.258	0.000	0.000	0.000	0.000
72	A	140	LEU	0	0.046	0.020	26.517	0.036	0.036	0.000	0.000	0.000	0.000
73	A	141	TYR	0	-0.131	-0.113	29.923	0.326	0.326	0.000	0.000	0.000	0.000
74	A	142	GLY	0	0.084	0.055	28.502	-0.367	-0.367	0.000	0.000	0.000	0.000
75	A	143	SER	0	-0.017	-0.011	29.290	0.365	0.365	0.000	0.000	0.000	0.000
76	A	144	LYS	1	0.974	0.986	29.298	9.153	9.153	0.000	0.000	0.000	0.000
77	A	145	GLU	-1	-0.919	-0.945	30.124	-9.150	-9.150	0.000	0.000	0.000	0.000
78	A	146	PHE	0	0.011	0.006	26.507	-0.156	-0.156	0.000	0.000	0.000	0.000
79	A	147	ASN	0	0.106	0.030	29.881	0.171	0.171	0.000	0.000	0.000	0.000
80	A	148	ASN	0	0.045	-0.002	30.360	-0.523	-0.523	0.000	0.000	0.000	0.000
81	A	149	ASP	-1	-0.772	-0.851	31.007	-9.449	-9.449	0.000	0.000	0.000	0.000
82	A	150	CYS	0	-0.076	-0.012	26.926	-0.277	-0.277	0.000	0.000	0.000	0.000
83	A	151	LYS	1	0.878	0.955	25.945	10.041	10.041	0.000	0.000	0.000	0.000
84	A	152	LEU	0	-0.026	-0.019	22.790	0.237	0.237	0.000	0.000	0.000	0.000
85	A	153	LYS	1	0.926	0.951	23.253	10.887	10.887	0.000	0.000	0.000	0.000
86	A	154	GLU	-1	-0.819	-0.877	16.335	-18.741	-18.741	0.000	0.000	0.000	0.000
87	A	155	ARG	1	0.837	0.907	19.674	14.178	14.178	0.000	0.000	0.000	0.000
88	A	156	ILE	0	0.063	0.040	13.608	-0.421	-0.421	0.000	0.000	0.000	0.000
89	A	157	GLU	-1	-0.790	-0.860	17.381	-12.581	-12.581	0.000	0.000	0.000	0.000
90	A	158	GLU	-1	-0.912	-0.963	17.348	-13.843	-13.843	0.000	0.000	0.000	0.000
91	A	159	ASN	0	-0.043	-0.030	17.514	-0.540	-0.540	0.000	0.000	0.000	0.000
92	A	160	GLY	0	0.030	0.017	13.580	-0.604	-0.604	0.000	0.000	0.000	0.000
93	A	161	TYR	0	-0.046	-0.021	13.024	-1.373	-1.373	0.000	0.000	0.000	0.000
94	A	162	ASN	0	0.014	0.007	14.213	0.248	0.248	0.000	0.000	0.000	0.000
95	A	163	THR	0	-0.105	-0.069	16.652	0.553	0.553	0.000	0.000	0.000	0.000
96	A	164	TYR	0	0.007	-0.028	16.192	-0.170	-0.170	0.000	0.000	0.000	0.000
97	A	165	ALA	0	-0.041	-0.019	22.113	0.540	0.540	0.000	0.000	0.000	0.000
98	A	166	SER	0	-0.010	-0.018	25.713	-0.191	-0.191	0.000	0.000	0.000	0.000
99	A	167	PHE	0	0.020	0.005	27.616	0.037	0.037	0.000	0.000	0.000	0.000
100	A	168	ASN	0	-0.023	-0.001	29.361	0.405	0.405	0.000	0.000	0.000	0.000
101	A	169	TRP	0	-0.032	-0.018	32.927	0.380	0.380	0.000	0.000	0.000	0.000
102	A	170	GLN	0	0.010	0.001	32.739	-0.515	-0.515	0.000	0.000	0.000	0.000
103	A	171	HIS	0	0.040	-0.003	34.873	0.072	0.072	0.000	0.000	0.000	0.000
104	A	172	ASN	0	-0.008	-0.010	36.658	-0.191	-0.191	0.000	0.000	0.000	0.000
105	A	173	GLY	0	0.089	0.051	37.630	0.036	0.036	0.000	0.000	0.000	0.000
106	A	174	ARG	1	0.901	0.965	33.272	8.227	8.227	0.000	0.000	0.000	0.000
107	A	175	GLN	0	0.068	0.049	28.175	-0.088	-0.088	0.000	0.000	0.000	0.000
108	A	176	MET	0	-0.085	-0.015	30.570	0.071	0.071	0.000	0.000	0.000	0.000
109	A	177	TYR	0	0.037	0.006	24.355	0.001	0.001	0.000	0.000	0.000	0.000
110	A	178	VAL	0	0.061	0.030	22.915	0.433	0.433	0.000	0.000	0.000	0.000
111	A	179	ALA	0	-0.004	-0.014	24.043	-0.309	-0.309	0.000	0.000	0.000	0.000
112	A	180	LEU	0	-0.003	0.020	21.924	0.409	0.409	0.000	0.000	0.000	0.000
113	A	181	ASN	0	-0.006	-0.025	25.481	-0.148	-0.148	0.000	0.000	0.000	0.000
114	A	182	GLY	0	0.019	-0.001	26.172	-0.378	-0.378	0.000	0.000	0.000	0.000
115	A	183	LYS	1	0.975	0.998	27.216	9.629	9.629	0.000	0.000	0.000	0.000
116	A	184	GLY	0	0.057	0.042	25.470	0.218	0.218	0.000	0.000	0.000	0.000
117	A	185	ALA	0	-0.004	0.002	26.455	0.040	0.040	0.000	0.000	0.000	0.000
118	A	186	PRO	0	0.015	0.015	27.955	-0.236	-0.236	0.000	0.000	0.000	0.000
119	A	187	ARG	1	0.824	0.895	28.132	10.905	10.905	0.000	0.000	0.000	0.000
120	A	188	ARG	1	0.855	0.923	30.190	8.341	8.341	0.000	0.000	0.000	0.000
121	A	189	GLY	0	0.090	0.043	30.659	0.012	0.012	0.000	0.000	0.000	0.000
122	A	190	GLN	0	0.057	0.045	31.701	0.023	0.023	0.000	0.000	0.000	0.000
123	A	191	LYS	1	0.927	0.974	33.614	8.800	8.800	0.000	0.000	0.000	0.000
124	A	192	THR	0	-0.039	-0.018	28.203	-0.180	-0.180	0.000	0.000	0.000	0.000
125	A	193	ARG	1	0.915	0.923	28.549	9.645	9.645	0.000	0.000	0.000	0.000
126	A	194	ARG	1	0.923	0.960	24.055	12.206	12.206	0.000	0.000	0.000	0.000
127	A	195	LYS	1	1.047	1.024	24.182	10.316	10.316	0.000	0.000	0.000	0.000
128	A	196	ASN	0	-0.019	0.002	25.282	0.028	0.028	0.000	0.000	0.000	0.000
129	A	197	THR	0	0.094	0.040	22.169	0.189	0.189	0.000	0.000	0.000	0.000
130	A	198	SER	0	-0.050	-0.003	22.324	-0.241	-0.241	0.000	0.000	0.000	0.000
131	A	199	ALA	0	-0.016	-0.019	23.378	-0.086	-0.086	0.000	0.000	0.000	0.000
132	A	200	HIS	0	-0.038	0.006	18.713	-0.564	-0.564	0.000	0.000	0.000	0.000
133	A	201	PHE	0	-0.015	-0.030	16.659	0.389	0.389	0.000	0.000	0.000	0.000
134	A	202	LEU	0	0.061	0.037	9.129	-0.061	-0.061	0.000	0.000	0.000	0.000
135	A	203	PRO	0	0.014	0.012	10.548	0.278	0.278	0.000	0.000	0.000	0.000
136	A	204	MET	0	-0.028	-0.014	8.589	-1.783	-1.783	0.000	0.000	0.000	0.000
138	A	206	VAL	0	-0.054	-0.026	7.833	1.008	1.008	0.000	0.000	0.000	0.000
139	A	207	HIS	-1	-0.883	-0.930	6.137	-34.185	-34.185	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:69:SER)