FMO DATABASE

FMODB ID: 3MZML

Calculation Name: 2JSF-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2JSF

Chain ID: A

ChEMBL ID:

UniProt ID: P18356

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	116
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-925612.467436
FMO2-HF: Nuclear repulsion	878657.742198
FMO2-HF: Total energy	-46954.725238
FMO2-MP2: Total energy	-47089.912865

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.
45.456	48.093	-0.018	-1.252	-1.367	-0.002

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 : 0.826 / q_NPA : 0.902

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

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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	0.921	0.948	3.278	48.998	51.587	-0.017	-1.220	-1.352	-0.002
4	A	4	LEU	0	0.012	0.012	4.356	-5.128	-5.080	-0.001	-0.032	-0.015	0.000
5	A	5	GLN	0	0.015	0.008	7.207	2.424	2.424	0.000	0.000	0.000	0.000
6	A	6	LEU	0	0.034	0.022	9.322	1.403	1.403	0.000	0.000	0.000	0.000
7	A	7	LYS	1	0.934	0.966	8.089	26.315	26.315	0.000	0.000	0.000	0.000
8	A	8	GLY	0	0.045	0.014	10.529	2.041	2.041	0.000	0.000	0.000	0.000
9	A	9	MET	0	-0.031	-0.003	12.676	-0.804	-0.804	0.000	0.000	0.000	0.000
10	A	10	SER	0	-0.021	-0.018	8.801	-0.456	-0.456	0.000	0.000	0.000	0.000
11	A	11	TYR	0	0.083	0.024	8.197	-0.510	-0.510	0.000	0.000	0.000	0.000
12	A	12	SER	0	0.018	0.023	6.443	-6.077	-6.077	0.000	0.000	0.000	0.000
13	A	13	MET	0	-0.144	-0.080	8.085	1.209	1.209	0.000	0.000	0.000	0.000
14	A	14	CYS	0	-0.076	0.010	10.766	-2.425	-2.425	0.000	0.000	0.000	0.000
15	A	15	THR	0	0.016	-0.022	12.778	0.864	0.864	0.000	0.000	0.000	0.000
16	A	16	GLY	0	0.013	0.025	14.803	0.705	0.705	0.000	0.000	0.000	0.000
17	A	17	LYS	1	0.834	0.927	17.840	12.300	12.300	0.000	0.000	0.000	0.000
18	A	18	PHE	0	0.060	0.015	17.740	-0.405	-0.405	0.000	0.000	0.000	0.000
19	A	19	LYS	1	0.910	0.948	23.285	11.463	11.463	0.000	0.000	0.000	0.000
20	A	20	VAL	0	0.031	0.014	26.624	-0.265	-0.265	0.000	0.000	0.000	0.000
21	A	21	VAL	0	-0.061	-0.030	27.396	0.219	0.219	0.000	0.000	0.000	0.000
22	A	22	LYS	1	0.923	0.939	29.814	9.556	9.556	0.000	0.000	0.000	0.000
23	A	23	GLU	-1	-0.881	-0.939	30.314	-9.166	-9.166	0.000	0.000	0.000	0.000
24	A	24	ILE	0	-0.041	-0.018	28.379	-0.204	-0.204	0.000	0.000	0.000	0.000
25	A	25	ALA	0	0.002	0.009	31.472	0.356	0.356	0.000	0.000	0.000	0.000
26	A	26	GLU	-1	-0.913	-0.967	32.132	-8.655	-8.655	0.000	0.000	0.000	0.000
27	A	27	THR	0	-0.017	-0.028	29.419	0.166	0.166	0.000	0.000	0.000	0.000
28	A	28	GLN	0	-0.049	-0.023	32.693	0.140	0.140	0.000	0.000	0.000	0.000
29	A	29	HIS	0	-0.006	0.007	32.633	0.297	0.297	0.000	0.000	0.000	0.000
30	A	30	GLY	0	-0.001	0.014	33.191	-0.159	-0.159	0.000	0.000	0.000	0.000
31	A	31	THR	0	0.022	0.003	27.855	-0.061	-0.061	0.000	0.000	0.000	0.000
32	A	32	ILE	0	-0.017	-0.001	28.945	0.325	0.325	0.000	0.000	0.000	0.000
33	A	33	VAL	0	-0.015	0.000	27.254	-0.547	-0.547	0.000	0.000	0.000	0.000
34	A	34	ILE	0	0.015	0.016	25.162	0.348	0.348	0.000	0.000	0.000	0.000
35	A	35	ARG	1	0.865	0.932	25.969	10.995	10.995	0.000	0.000	0.000	0.000
36	A	36	VAL	0	0.023	0.007	22.599	0.345	0.345	0.000	0.000	0.000	0.000
37	A	37	GLN	0	0.001	0.011	23.938	0.079	0.079	0.000	0.000	0.000	0.000
38	A	38	TYR	0	-0.042	-0.040	15.419	-0.013	-0.013	0.000	0.000	0.000	0.000
39	A	39	GLU	-1	-0.867	-0.928	20.958	-12.086	-12.086	0.000	0.000	0.000	0.000
40	A	40	GLY	0	0.008	0.010	19.425	-0.602	-0.602	0.000	0.000	0.000	0.000
41	A	41	ASP	-1	-0.831	-0.936	15.795	-17.516	-17.516	0.000	0.000	0.000	0.000
42	A	42	GLY	0	-0.013	0.006	13.004	-0.754	-0.754	0.000	0.000	0.000	0.000
43	A	43	SER	0	0.000	-0.002	12.776	-1.131	-1.131	0.000	0.000	0.000	0.000
44	A	44	PRO	0	0.010	0.006	12.037	0.142	0.142	0.000	0.000	0.000	0.000
45	A	46	LYS	1	0.895	0.965	9.453	28.823	28.823	0.000	0.000	0.000	0.000
46	A	47	ILE	0	0.023	0.001	13.183	-0.236	-0.236	0.000	0.000	0.000	0.000
47	A	48	PRO	0	-0.042	0.002	15.154	-0.225	-0.225	0.000	0.000	0.000	0.000
48	A	49	PHE	0	0.044	-0.007	16.858	0.903	0.903	0.000	0.000	0.000	0.000
49	A	50	GLU	-1	-0.872	-0.925	19.583	-14.271	-14.271	0.000	0.000	0.000	0.000
50	A	51	ILE	0	-0.031	-0.012	22.219	0.516	0.516	0.000	0.000	0.000	0.000
51	A	52	MET	0	-0.013	0.014	22.372	-0.144	-0.144	0.000	0.000	0.000	0.000
52	A	53	ASP	-1	-0.828	-0.930	25.923	-11.329	-11.329	0.000	0.000	0.000	0.000
53	A	54	LEU	0	0.036	0.013	25.701	-0.294	-0.294	0.000	0.000	0.000	0.000
54	A	55	GLU	-1	-0.936	-0.970	25.099	-12.162	-12.162	0.000	0.000	0.000	0.000
55	A	56	LYS	1	0.780	0.896	21.978	13.676	13.676	0.000	0.000	0.000	0.000
56	A	57	ARG	1	0.872	0.935	27.185	9.979	9.979	0.000	0.000	0.000	0.000
57	A	58	HIS	0	0.016	0.024	29.110	0.331	0.331	0.000	0.000	0.000	0.000
58	A	59	VAL	0	-0.007	-0.010	31.146	0.082	0.082	0.000	0.000	0.000	0.000
59	A	60	LEU	0	0.023	0.003	27.230	-0.090	-0.090	0.000	0.000	0.000	0.000
60	A	61	GLY	0	0.027	0.032	27.770	0.179	0.179	0.000	0.000	0.000	0.000
61	A	62	ARG	1	0.897	0.942	23.245	12.201	12.201	0.000	0.000	0.000	0.000
62	A	63	LEU	0	-0.006	-0.003	20.322	0.079	0.079	0.000	0.000	0.000	0.000
63	A	64	ILE	0	-0.015	-0.004	22.600	-0.286	-0.286	0.000	0.000	0.000	0.000
64	A	65	THR	0	-0.016	-0.002	20.338	-0.558	-0.558	0.000	0.000	0.000	0.000
65	A	66	VAL	0	-0.003	-0.020	16.001	-0.207	-0.207	0.000	0.000	0.000	0.000
66	A	67	ASN	0	-0.041	-0.030	13.837	-1.678	-1.678	0.000	0.000	0.000	0.000
67	A	68	PRO	0	0.069	0.057	15.099	-1.172	-1.172	0.000	0.000	0.000	0.000
68	A	69	ILE	0	-0.024	-0.021	12.333	-1.196	-1.196	0.000	0.000	0.000	0.000
69	A	70	VAL	0	-0.021	0.014	15.990	1.152	1.152	0.000	0.000	0.000	0.000
70	A	71	THR	0	-0.023	-0.024	15.936	-0.946	-0.946	0.000	0.000	0.000	0.000
71	A	72	GLU	-1	-0.888	-0.957	17.040	-14.357	-14.357	0.000	0.000	0.000	0.000
72	A	73	LYS	1	0.802	0.913	17.594	14.276	14.276	0.000	0.000	0.000	0.000
73	A	74	ASP	-1	-0.815	-0.922	19.016	-12.271	-12.271	0.000	0.000	0.000	0.000
74	A	75	SER	0	-0.011	0.003	21.334	0.715	0.715	0.000	0.000	0.000	0.000
75	A	76	PRO	0	0.022	-0.011	22.341	-0.409	-0.409	0.000	0.000	0.000	0.000
76	A	77	VAL	0	0.035	0.043	19.364	0.254	0.254	0.000	0.000	0.000	0.000
77	A	78	ASN	0	-0.020	-0.016	22.721	0.650	0.650	0.000	0.000	0.000	0.000
78	A	79	ILE	0	-0.050	-0.024	20.666	-0.641	-0.641	0.000	0.000	0.000	0.000
79	A	80	GLU	-1	-0.869	-0.934	23.333	-11.209	-11.209	0.000	0.000	0.000	0.000
80	A	81	ALA	0	0.000	-0.002	24.165	-0.577	-0.577	0.000	0.000	0.000	0.000
81	A	82	GLU	-1	-0.851	-0.943	25.988	-10.102	-10.102	0.000	0.000	0.000	0.000
82	A	83	PRO	0	-0.026	0.002	28.450	-0.288	-0.288	0.000	0.000	0.000	0.000
83	A	84	PRO	0	-0.038	0.001	30.096	0.203	0.203	0.000	0.000	0.000	0.000
84	A	85	PHE	0	0.024	-0.015	32.703	0.329	0.329	0.000	0.000	0.000	0.000
85	A	86	GLY	0	0.024	0.018	35.254	-0.144	-0.144	0.000	0.000	0.000	0.000
86	A	87	ASP	-1	-0.896	-0.958	35.827	-8.314	-8.314	0.000	0.000	0.000	0.000
87	A	88	SER	0	-0.011	-0.005	31.509	-0.271	-0.271	0.000	0.000	0.000	0.000
88	A	89	TYR	0	-0.024	-0.023	30.517	-0.043	-0.043	0.000	0.000	0.000	0.000
89	A	90	ILE	0	0.029	0.013	25.553	-0.390	-0.390	0.000	0.000	0.000	0.000
90	A	91	ILE	0	-0.014	0.005	23.200	0.299	0.299	0.000	0.000	0.000	0.000
91	A	92	ILE	0	0.004	0.002	21.322	-0.486	-0.486	0.000	0.000	0.000	0.000
92	A	93	GLY	0	-0.002	-0.018	18.914	0.394	0.394	0.000	0.000	0.000	0.000
93	A	94	VAL	0	0.005	0.002	16.233	-0.143	-0.143	0.000	0.000	0.000	0.000
94	A	95	GLU	-1	-0.872	-0.952	19.510	-12.979	-12.979	0.000	0.000	0.000	0.000
95	A	96	PRO	0	-0.025	0.002	19.307	0.727	0.727	0.000	0.000	0.000	0.000
96	A	97	GLY	0	0.020	0.001	22.197	-0.180	-0.180	0.000	0.000	0.000	0.000
97	A	98	GLN	0	-0.032	-0.006	22.180	-0.240	-0.240	0.000	0.000	0.000	0.000
98	A	99	LEU	0	-0.050	-0.018	23.735	0.651	0.651	0.000	0.000	0.000	0.000
99	A	100	LYS	1	0.947	0.947	25.865	10.169	10.169	0.000	0.000	0.000	0.000
100	A	101	LEU	0	-0.030	-0.005	27.415	0.293	0.293	0.000	0.000	0.000	0.000
101	A	102	ASN	0	0.001	0.007	30.872	-0.286	-0.286	0.000	0.000	0.000	0.000
102	A	103	TRP	0	0.074	0.037	32.786	0.085	0.085	0.000	0.000	0.000	0.000
103	A	104	PHE	0	0.016	0.017	34.516	0.001	0.001	0.000	0.000	0.000	0.000
104	A	105	LYS	1	0.795	0.895	36.585	8.093	8.093	0.000	0.000	0.000	0.000
105	A	106	LYS	1	0.909	0.957	38.711	7.391	7.391	0.000	0.000	0.000	0.000
106	A	107	GLY	0	0.057	0.017	41.665	0.038	0.038	0.000	0.000	0.000	0.000
107	A	108	SER	0	-0.026	-0.006	43.277	0.024	0.024	0.000	0.000	0.000	0.000
108	A	109	SER	0	0.034	0.014	40.773	-0.245	-0.245	0.000	0.000	0.000	0.000
109	A	110	LEU	0	0.001	0.002	40.724	0.137	0.137	0.000	0.000	0.000	0.000
110	A	111	GLU	-1	-0.839	-0.915	41.494	-7.439	-7.439	0.000	0.000	0.000	0.000
111	A	112	HIS	0	-0.045	-0.024	44.433	0.021	0.021	0.000	0.000	0.000	0.000
112	A	113	HIS	0	-0.003	-0.003	46.711	0.213	0.213	0.000	0.000	0.000	0.000
113	A	114	HIS	0	-0.001	-0.012	47.744	-0.024	-0.024	0.000	0.000	0.000	0.000
114	A	115	HIS	0	-0.002	0.007	50.935	0.028	0.028	0.000	0.000	0.000	0.000
115	A	116	HIS	0	-0.080	-0.042	53.976	-0.041	-0.041	0.000	0.000	0.000	0.000
116	A	117	HIS	-1	-0.913	-0.938	56.275	-5.309	-5.309	0.000	0.000	0.000	0.000

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