FMO DATABASE

FMODB ID: 3ZMYL

Calculation Name: 4JUT-C-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 4JUT

Chain ID: C

ChEMBL ID:

UniProt ID: O14558

Base Structure: X-ray

Registration Date: 2025-10-04

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	90
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-514940.813316
FMO2-HF: Nuclear repulsion	481965.222967
FMO2-HF: Total energy	-32975.590349
FMO2-MP2: Total energy	-33074.820378

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:60:VAL)

Summations of interaction energy for fragment #1(A:60:VAL)

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.
-30.412	-27.662	0.304	-1.353	-1.7	-0.011

Interaction energy analysis for fragmet #1(A:60:VAL)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.857 / q_NPA : 0.916

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	62	LEU	0	0.043	0.019	2.827	-5.127	-2.377	0.304	-1.353	-1.700	-0.011
4	A	63	PRO	0	-0.011	-0.007	5.623	3.106	3.106	0.000	0.000	0.000	0.000
5	A	64	VAL	0	0.023	0.015	8.681	0.028	0.028	0.000	0.000	0.000	0.000
6	A	65	ALA	0	0.010	0.002	11.839	1.121	1.121	0.000	0.000	0.000	0.000
7	A	66	GLN	0	-0.016	-0.011	14.478	1.351	1.351	0.000	0.000	0.000	0.000
8	A	67	VAL	0	-0.006	0.005	17.362	0.562	0.562	0.000	0.000	0.000	0.000
9	A	68	PRO	0	0.006	-0.004	20.346	0.144	0.144	0.000	0.000	0.000	0.000
10	A	69	THR	0	-0.027	-0.019	24.000	-0.070	-0.070	0.000	0.000	0.000	0.000
11	A	70	ASP	-1	-0.891	-0.930	25.995	-9.934	-9.934	0.000	0.000	0.000	0.000
12	A	71	PRO	0	-0.048	-0.023	26.883	-0.250	-0.250	0.000	0.000	0.000	0.000
13	A	72	GLY	0	0.007	0.009	28.336	0.012	0.012	0.000	0.000	0.000	0.000
14	A	73	HIS	0	-0.034	-0.015	28.296	0.373	0.373	0.000	0.000	0.000	0.000
15	A	74	PHE	0	0.004	-0.004	32.563	-0.070	-0.070	0.000	0.000	0.000	0.000
16	A	75	SER	0	0.041	0.010	28.883	-0.224	-0.224	0.000	0.000	0.000	0.000
17	A	76	VAL	0	-0.051	-0.014	31.470	0.053	0.053	0.000	0.000	0.000	0.000
18	A	77	LEU	0	0.015	0.001	25.486	-0.222	-0.222	0.000	0.000	0.000	0.000
19	A	78	LEU	0	-0.056	-0.033	29.659	0.344	0.344	0.000	0.000	0.000	0.000
20	A	79	ASP	-1	-0.839	-0.900	28.588	-11.473	-11.473	0.000	0.000	0.000	0.000
21	A	80	VAL	0	-0.012	-0.021	29.936	0.459	0.459	0.000	0.000	0.000	0.000
22	A	81	LYS	1	0.945	0.963	27.377	11.597	11.597	0.000	0.000	0.000	0.000
23	A	82	HIS	0	-0.045	-0.008	30.477	0.143	0.143	0.000	0.000	0.000	0.000
24	A	83	PHE	0	-0.080	-0.030	33.724	0.351	0.351	0.000	0.000	0.000	0.000
25	A	84	SER	0	0.021	0.004	33.867	-0.231	-0.231	0.000	0.000	0.000	0.000
26	A	85	PRO	0	0.006	-0.016	33.419	0.082	0.082	0.000	0.000	0.000	0.000
27	A	86	GLU	-1	-0.879	-0.945	35.954	-8.405	-8.405	0.000	0.000	0.000	0.000
28	A	87	GLU	-1	-0.853	-0.907	38.207	-8.092	-8.092	0.000	0.000	0.000	0.000
29	A	88	ILE	0	-0.018	-0.016	34.330	0.026	0.026	0.000	0.000	0.000	0.000
30	A	89	ALA	0	0.000	0.002	38.705	0.062	0.062	0.000	0.000	0.000	0.000
31	A	90	VAL	0	-0.003	-0.007	36.061	0.030	0.030	0.000	0.000	0.000	0.000
32	A	91	LYS	1	0.927	0.967	39.542	7.130	7.130	0.000	0.000	0.000	0.000
33	A	92	VAL	0	0.054	0.030	41.162	-0.099	-0.099	0.000	0.000	0.000	0.000
34	A	93	VAL	0	-0.036	-0.019	43.673	0.171	0.171	0.000	0.000	0.000	0.000
35	A	94	GLY	0	0.007	0.002	47.140	0.031	0.031	0.000	0.000	0.000	0.000
36	A	95	GLU	-1	-0.799	-0.875	46.044	-6.787	-6.787	0.000	0.000	0.000	0.000
37	A	96	HIS	0	-0.021	-0.015	43.743	-0.155	-0.155	0.000	0.000	0.000	0.000
38	A	97	VAL	0	0.046	0.039	37.994	0.061	0.061	0.000	0.000	0.000	0.000
39	A	98	GLU	-1	-0.865	-0.929	41.356	-7.049	-7.049	0.000	0.000	0.000	0.000
40	A	99	VAL	0	0.009	0.002	36.724	-0.112	-0.112	0.000	0.000	0.000	0.000
41	A	100	HIS	1	0.754	0.845	39.910	7.482	7.482	0.000	0.000	0.000	0.000
42	A	101	ALA	0	0.044	0.043	37.878	-0.061	-0.061	0.000	0.000	0.000	0.000
43	A	102	ARG	1	0.937	0.962	39.863	7.100	7.100	0.000	0.000	0.000	0.000
44	A	103	HIS	0	0.012	0.028	37.906	-0.167	-0.167	0.000	0.000	0.000	0.000
45	A	104	ALA	0	-0.024	-0.018	41.366	0.134	0.134	0.000	0.000	0.000	0.000
46	A	105	ALA	0	-0.003	-0.005	42.767	-0.163	-0.163	0.000	0.000	0.000	0.000
47	A	106	ARG	1	0.842	0.922	36.304	8.588	8.588	0.000	0.000	0.000	0.000
48	A	107	PRO	0	0.017	-0.008	40.183	0.025	0.025	0.000	0.000	0.000	0.000
49	A	108	ASP	-1	-0.873	-0.949	36.681	-8.656	-8.656	0.000	0.000	0.000	0.000
50	A	109	GLU	-1	-0.962	-0.975	34.442	-9.123	-9.123	0.000	0.000	0.000	0.000
51	A	110	HIS	0	-0.002	-0.001	37.789	0.243	0.243	0.000	0.000	0.000	0.000
52	A	111	GLY	0	-0.007	-0.002	41.418	0.236	0.236	0.000	0.000	0.000	0.000
53	A	112	PHE	0	-0.038	-0.016	42.506	-0.092	-0.092	0.000	0.000	0.000	0.000
54	A	113	VAL	0	-0.005	0.012	39.023	0.078	0.078	0.000	0.000	0.000	0.000
55	A	114	ALA	0	-0.022	-0.008	42.109	-0.028	-0.028	0.000	0.000	0.000	0.000
56	A	115	ARG	1	0.869	0.937	37.003	8.635	8.635	0.000	0.000	0.000	0.000
57	A	116	GLU	-1	-0.825	-0.918	41.106	-7.031	-7.031	0.000	0.000	0.000	0.000
58	A	117	PHE	0	-0.032	-0.010	35.774	-0.011	-0.011	0.000	0.000	0.000	0.000
59	A	118	HIS	0	0.014	0.004	41.316	-0.075	-0.075	0.000	0.000	0.000	0.000
60	A	119	ARG	1	0.918	0.967	36.638	8.799	8.799	0.000	0.000	0.000	0.000
61	A	120	ARG	1	0.876	0.930	41.167	7.084	7.084	0.000	0.000	0.000	0.000
62	A	121	TYR	0	0.044	0.022	35.885	-0.071	-0.071	0.000	0.000	0.000	0.000
63	A	122	ARG	1	0.832	0.895	40.857	7.002	7.002	0.000	0.000	0.000	0.000
64	A	123	LEU	0	0.024	0.015	39.444	-0.214	-0.214	0.000	0.000	0.000	0.000
65	A	124	PRO	0	0.002	0.001	37.666	0.170	0.170	0.000	0.000	0.000	0.000
66	A	125	PRO	0	-0.017	-0.023	40.965	0.067	0.067	0.000	0.000	0.000	0.000
67	A	126	GLY	0	0.022	0.021	42.599	-0.095	-0.095	0.000	0.000	0.000	0.000
68	A	127	VAL	0	-0.016	0.007	38.594	-0.009	-0.009	0.000	0.000	0.000	0.000
69	A	128	ASP	-1	-0.814	-0.909	41.246	-7.313	-7.313	0.000	0.000	0.000	0.000
70	A	129	PRO	0	-0.037	-0.033	41.070	-0.198	-0.198	0.000	0.000	0.000	0.000
71	A	130	ALA	0	-0.046	-0.025	41.689	-0.117	-0.117	0.000	0.000	0.000	0.000
72	A	131	ALA	0	0.003	0.010	37.859	-0.136	-0.136	0.000	0.000	0.000	0.000
73	A	132	VAL	0	-0.066	-0.030	36.708	-0.309	-0.309	0.000	0.000	0.000	0.000
74	A	133	THR	0	-0.037	-0.012	33.197	-0.043	-0.043	0.000	0.000	0.000	0.000
75	A	134	SER	0	-0.016	-0.029	32.388	-0.041	-0.041	0.000	0.000	0.000	0.000
76	A	135	ALA	0	0.016	0.021	28.309	0.021	0.021	0.000	0.000	0.000	0.000
77	A	136	LEU	0	-0.006	0.002	28.950	0.008	0.008	0.000	0.000	0.000	0.000
78	A	137	SER	0	-0.027	-0.033	23.361	0.071	0.071	0.000	0.000	0.000	0.000
79	A	138	PRO	0	0.013	-0.006	21.931	0.462	0.462	0.000	0.000	0.000	0.000
80	A	139	GLU	-1	-0.879	-0.916	20.491	-14.667	-14.667	0.000	0.000	0.000	0.000
81	A	140	GLY	0	-0.007	0.004	23.917	0.278	0.278	0.000	0.000	0.000	0.000
82	A	141	VAL	0	-0.015	-0.010	24.347	0.395	0.395	0.000	0.000	0.000	0.000
83	A	142	LEU	0	-0.014	0.005	27.175	-0.011	-0.011	0.000	0.000	0.000	0.000
84	A	143	SER	0	-0.027	-0.022	27.504	-0.132	-0.132	0.000	0.000	0.000	0.000
85	A	144	ILE	0	-0.013	-0.029	29.652	0.284	0.284	0.000	0.000	0.000	0.000
86	A	145	GLN	0	0.002	-0.002	26.923	-0.092	-0.092	0.000	0.000	0.000	0.000
87	A	146	ALA	0	0.025	0.020	32.654	0.230	0.230	0.000	0.000	0.000	0.000
88	A	147	ALA	0	-0.009	-0.001	33.813	-0.185	-0.185	0.000	0.000	0.000	0.000
89	A	148	PRO	0	-0.038	-0.036	33.364	0.174	0.174	0.000	0.000	0.000	0.000
90	A	149	ALA	-1	-0.910	-0.931	36.361	-7.875	-7.875	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:60:VAL)