FMO DATABASE

FMODB ID: Y7L62

Calculation Name: 1UW4-A-Xray549

Preferred Name:

Target Type:

Ligand Name: beta-mercaptoethanol

Ligand 3-letter code: BME

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1UW4

Chain ID: A

ChEMBL ID:

UniProt ID: Q9BZI7

Base Structure: X-ray

Registration Date: 2025-10-11

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	OptH
Protonation	MOE:Protonate 3D
Complement	ac.sh, 23 2024 Oct
Water	No
Procedure	Manual calculation
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	91
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-697006.959542
FMO2-HF: Nuclear repulsion	659295.633735
FMO2-HF: Total energy	-37711.325808
FMO2-MP2: Total energy	-37822.875409

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:50:LEU)

Summations of interaction energy for fragment #1(A:50:LEU)

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.
-106.216	-96.448	7.53	-6.517	-10.776	-0.064

Interaction energy analysis for fragmet #1(A:50:LEU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.776 / q_NPA : 0.887

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	52	LYS	1	0.871	0.964	3.848	35.869	38.725	-0.029	-1.433	-1.393	-0.007
4	A	53	VAL	0	0.043	0.026	4.996	-2.922	-2.799	-0.001	-0.004	-0.117	0.000
55	A	104	GLN	0	-0.014	-0.033	2.861	-21.225	-19.704	0.077	-0.878	-0.720	-0.010
58	A	107	ILE	0	-0.055	-0.018	4.689	0.088	0.195	-0.001	-0.014	-0.092	0.000
84	A	133	PHE	0	0.016	-0.007	2.786	-8.445	-5.897	4.844	-2.209	-5.182	-0.030
85	A	134	ALA	0	-0.008	-0.004	5.216	3.936	3.999	-0.001	-0.002	-0.060	0.000
86	A	135	PRO	0	0.023	0.012	5.074	-3.888	-3.795	-0.001	0.000	-0.091	0.000
88	A	137	GLN	0	0.019	-0.034	2.397	-14.098	-11.641	2.642	-1.977	-3.121	-0.017
5	A	54	VAL	0	-0.058	-0.035	6.961	2.658	2.658	0.000	0.000	0.000	0.000
6	A	55	ILE	0	0.044	0.040	10.020	-0.205	-0.205	0.000	0.000	0.000	0.000
7	A	56	ARG	1	0.944	0.954	12.731	19.300	19.300	0.000	0.000	0.000	0.000
8	A	57	ARG	1	0.912	0.957	15.656	13.920	13.920	0.000	0.000	0.000	0.000
9	A	58	LEU	0	0.075	0.055	17.391	0.513	0.513	0.000	0.000	0.000	0.000
10	A	59	PRO	0	0.056	0.024	20.703	0.168	0.168	0.000	0.000	0.000	0.000
11	A	60	PRO	0	-0.030	-0.012	24.053	-0.238	-0.238	0.000	0.000	0.000	0.000
12	A	61	THR	0	-0.061	-0.035	25.422	0.012	0.012	0.000	0.000	0.000	0.000
13	A	62	LEU	0	-0.015	0.016	21.575	0.245	0.245	0.000	0.000	0.000	0.000
14	A	63	THR	0	0.006	-0.015	24.761	-0.152	-0.152	0.000	0.000	0.000	0.000
15	A	64	LYS	1	0.896	0.952	19.207	15.033	15.033	0.000	0.000	0.000	0.000
16	A	65	GLU	-1	-0.854	-0.941	21.718	-13.057	-13.057	0.000	0.000	0.000	0.000
17	A	66	GLN	0	0.071	0.044	24.245	-0.338	-0.338	0.000	0.000	0.000	0.000
18	A	67	LEU	0	-0.029	-0.017	17.385	-0.211	-0.211	0.000	0.000	0.000	0.000
19	A	68	GLN	0	-0.011	-0.018	20.080	-0.021	-0.021	0.000	0.000	0.000	0.000
20	A	69	GLU	-1	-0.957	-0.977	21.314	-11.313	-11.313	0.000	0.000	0.000	0.000
21	A	70	HIS	0	0.002	0.005	21.822	-0.177	-0.177	0.000	0.000	0.000	0.000
22	A	71	LEU	0	-0.024	-0.009	15.941	-0.478	-0.478	0.000	0.000	0.000	0.000
23	A	72	GLN	0	-0.030	0.023	19.378	-0.259	-0.259	0.000	0.000	0.000	0.000
24	A	73	PRO	0	-0.023	-0.016	20.931	0.432	0.432	0.000	0.000	0.000	0.000
25	A	74	MET	0	0.010	0.002	15.789	-0.071	-0.071	0.000	0.000	0.000	0.000
26	A	75	PRO	0	0.035	0.033	13.351	0.639	0.639	0.000	0.000	0.000	0.000
27	A	76	GLU	-1	-0.854	-0.924	13.625	-20.404	-20.404	0.000	0.000	0.000	0.000
28	A	77	HIS	0	-0.081	-0.060	11.878	-1.967	-1.967	0.000	0.000	0.000	0.000
29	A	78	ASP	-1	-0.855	-0.918	10.736	-26.133	-26.133	0.000	0.000	0.000	0.000
30	A	79	TYR	0	-0.047	-0.023	11.752	1.055	1.055	0.000	0.000	0.000	0.000
31	A	80	PHE	0	0.029	-0.006	13.053	-1.484	-1.484	0.000	0.000	0.000	0.000
32	A	81	GLU	-1	-0.892	-0.928	15.004	-14.508	-14.508	0.000	0.000	0.000	0.000
33	A	82	PHE	0	0.018	-0.004	15.909	-0.986	-0.986	0.000	0.000	0.000	0.000
34	A	83	PHE	0	-0.016	-0.010	15.816	0.380	0.380	0.000	0.000	0.000	0.000
35	A	84	SER	0	0.031	0.004	19.559	-0.208	-0.208	0.000	0.000	0.000	0.000
36	A	85	ASN	0	-0.033	-0.019	22.285	0.203	0.203	0.000	0.000	0.000	0.000
37	A	86	ASP	-1	-0.765	-0.838	19.821	-14.222	-14.222	0.000	0.000	0.000	0.000
38	A	87	THR	0	-0.021	-0.002	22.027	-0.243	-0.243	0.000	0.000	0.000	0.000
39	A	88	SER	0	0.023	0.005	23.067	0.348	0.348	0.000	0.000	0.000	0.000
40	A	89	LEU	0	-0.026	-0.011	22.293	0.419	0.419	0.000	0.000	0.000	0.000
41	A	90	TYR	0	0.056	0.032	25.928	-0.031	-0.031	0.000	0.000	0.000	0.000
42	A	91	PRO	0	-0.003	-0.008	28.842	0.171	0.171	0.000	0.000	0.000	0.000
43	A	92	HIS	0	-0.054	-0.037	25.254	0.114	0.114	0.000	0.000	0.000	0.000
44	A	93	MET	0	-0.041	-0.010	24.617	-0.520	-0.520	0.000	0.000	0.000	0.000
45	A	94	TYR	0	0.009	-0.001	20.971	0.025	0.025	0.000	0.000	0.000	0.000
46	A	95	ALA	0	0.001	0.005	20.704	0.022	0.022	0.000	0.000	0.000	0.000
47	A	96	ARG	1	0.744	0.828	14.968	16.203	16.203	0.000	0.000	0.000	0.000
48	A	97	ALA	0	0.035	0.024	14.961	0.734	0.734	0.000	0.000	0.000	0.000
49	A	98	TYR	0	-0.051	-0.012	9.939	-0.910	-0.910	0.000	0.000	0.000	0.000
50	A	99	ILE	0	0.041	0.022	10.042	1.453	1.453	0.000	0.000	0.000	0.000
51	A	100	ASN	0	-0.057	-0.012	6.642	-8.390	-8.390	0.000	0.000	0.000	0.000
52	A	101	PHE	0	0.018	-0.004	7.164	2.932	2.932	0.000	0.000	0.000	0.000
53	A	102	LYS	1	0.874	0.930	7.395	19.053	19.053	0.000	0.000	0.000	0.000
54	A	103	ASN	0	-0.027	-0.004	8.632	-1.657	-1.657	0.000	0.000	0.000	0.000
56	A	105	GLU	-1	-0.888	-0.947	6.947	-26.692	-26.692	0.000	0.000	0.000	0.000
57	A	106	ASP	-1	-0.810	-0.914	10.469	-23.102	-23.102	0.000	0.000	0.000	0.000
59	A	108	ILE	0	-0.055	-0.015	8.506	1.383	1.383	0.000	0.000	0.000	0.000
60	A	109	LEU	0	0.045	0.017	10.231	1.766	1.766	0.000	0.000	0.000	0.000
61	A	110	PHE	0	0.001	0.005	11.177	1.376	1.376	0.000	0.000	0.000	0.000
62	A	111	ARG	1	0.832	0.883	9.716	25.046	25.046	0.000	0.000	0.000	0.000
63	A	112	ASP	-1	-0.831	-0.899	12.382	-19.544	-19.544	0.000	0.000	0.000	0.000
64	A	113	ARG	1	0.809	0.919	15.118	16.941	16.941	0.000	0.000	0.000	0.000
65	A	114	PHE	0	-0.015	-0.019	15.047	0.935	0.935	0.000	0.000	0.000	0.000
66	A	115	ASP	-1	-0.875	-0.939	13.693	-19.255	-19.255	0.000	0.000	0.000	0.000
67	A	116	GLY	0	-0.015	-0.004	15.643	0.717	0.717	0.000	0.000	0.000	0.000
68	A	117	TYR	0	-0.066	-0.033	18.637	0.848	0.848	0.000	0.000	0.000	0.000
69	A	118	VAL	0	-0.006	-0.005	20.573	-0.210	-0.210	0.000	0.000	0.000	0.000
70	A	119	PHE	0	0.011	0.010	19.043	0.244	0.244	0.000	0.000	0.000	0.000
71	A	120	LEU	0	0.015	0.003	24.221	0.247	0.247	0.000	0.000	0.000	0.000
72	A	121	ASP	-1	-0.789	-0.900	27.560	-10.144	-10.144	0.000	0.000	0.000	0.000
73	A	122	ASN	0	-0.056	-0.047	29.529	0.339	0.339	0.000	0.000	0.000	0.000
74	A	123	LYS	1	0.914	0.961	32.915	8.475	8.475	0.000	0.000	0.000	0.000
75	A	124	GLY	0	0.010	0.019	32.156	0.194	0.194	0.000	0.000	0.000	0.000
76	A	125	GLN	0	-0.058	-0.025	29.841	0.241	0.241	0.000	0.000	0.000	0.000
77	A	126	GLU	-1	-0.897	-0.960	26.709	-10.776	-10.776	0.000	0.000	0.000	0.000
78	A	127	TYR	0	-0.105	-0.060	22.860	-0.085	-0.085	0.000	0.000	0.000	0.000
79	A	128	PRO	0	-0.005	0.008	20.890	-0.344	-0.344	0.000	0.000	0.000	0.000
80	A	129	ALA	0	-0.027	-0.008	17.061	-0.223	-0.223	0.000	0.000	0.000	0.000
81	A	130	ILE	0	-0.024	-0.007	12.534	0.089	0.089	0.000	0.000	0.000	0.000
82	A	131	VAL	0	-0.038	-0.025	10.089	-0.455	-0.455	0.000	0.000	0.000	0.000
83	A	132	GLU	-1	-0.907	-0.947	7.886	-23.156	-23.156	0.000	0.000	0.000	0.000
87	A	136	PHE	0	-0.001	-0.002	6.897	0.011	0.011	0.000	0.000	0.000	0.000
89	A	138	LYS	1	0.929	0.986	5.584	19.979	19.979	0.000	0.000	0.000	0.000
90	A	139	ALA	0	0.035	0.018	8.859	0.779	0.779	0.000	0.000	0.000	0.000
91	A	140	ALA	-1	-0.907	-0.944	10.347	-19.004	-19.004	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:50:LEU)