FMO DATABASE

FMODB ID: Z7KLN

Calculation Name: 1O1V-A-Other547

Preferred Name:

Target Type:

Ligand Name: taurocholic acid

Ligand 3-letter code: TCH

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1O1V

Chain ID: A

ChEMBL ID:

UniProt ID: P51161

Base Structure: SolutionNMR

Registration Date: 2025-10-03

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	127
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1105006.55111
FMO2-HF: Nuclear repulsion	1054617.227162
FMO2-HF: Total energy	-50389.323948
FMO2-MP2: Total energy	-50535.040251

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:ALA)

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

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.
-68.373	-64.146	4.048	-3.744	-4.529	-0.037

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.823 / q_NPA : 0.905

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	THR	0	0.026	-0.005	3.046	0.397	2.199	0.204	-0.745	-1.261	-0.004
4	A	4	GLY	0	0.050	0.039	5.150	-0.660	-0.637	-0.001	-0.004	-0.018	0.000
42	A	42	GLN	0	0.020	0.019	2.307	-17.097	-15.139	3.843	-2.880	-2.920	-0.032
43	A	43	ASP	-1	-0.930	-0.965	5.004	-27.908	-27.863	-0.001	-0.002	-0.042	0.000
103	A	103	ILE	0	-0.026	-0.004	3.465	-0.319	-0.020	0.004	-0.103	-0.199	-0.001
125	A	125	ARG	1	0.815	0.896	4.240	47.314	47.414	-0.001	-0.010	-0.089	0.000
5	A	5	LYS	1	0.862	0.928	8.714	20.589	20.589	0.000	0.000	0.000	0.000
6	A	6	PHE	0	-0.002	-0.020	6.454	-2.639	-2.639	0.000	0.000	0.000	0.000
7	A	7	GLU	-1	-0.815	-0.875	12.669	-14.978	-14.978	0.000	0.000	0.000	0.000
8	A	8	MET	0	-0.066	-0.020	15.393	-0.234	-0.234	0.000	0.000	0.000	0.000
9	A	9	GLU	-1	-0.873	-0.922	17.142	-16.003	-16.003	0.000	0.000	0.000	0.000
10	A	10	SER	0	-0.009	0.002	19.045	1.016	1.016	0.000	0.000	0.000	0.000
11	A	11	GLU	-1	-0.846	-0.936	18.617	-17.346	-17.346	0.000	0.000	0.000	0.000
12	A	12	LYS	1	0.805	0.901	19.939	16.097	16.097	0.000	0.000	0.000	0.000
13	A	13	ASN	0	-0.005	-0.022	22.669	-0.583	-0.583	0.000	0.000	0.000	0.000
14	A	14	TYR	0	0.072	0.038	21.655	0.356	0.356	0.000	0.000	0.000	0.000
15	A	15	ASP	-1	-0.864	-0.929	24.571	-10.985	-10.985	0.000	0.000	0.000	0.000
16	A	16	GLU	-1	-0.855	-0.938	28.135	-10.112	-10.112	0.000	0.000	0.000	0.000
17	A	17	PHE	0	0.046	0.020	20.843	-0.033	-0.033	0.000	0.000	0.000	0.000
18	A	18	MET	0	-0.009	-0.008	21.456	0.073	0.073	0.000	0.000	0.000	0.000
19	A	19	LYS	1	0.939	0.971	26.384	9.820	9.820	0.000	0.000	0.000	0.000
20	A	20	LEU	0	-0.064	-0.035	27.859	0.333	0.333	0.000	0.000	0.000	0.000
21	A	21	LEU	0	-0.012	0.008	22.825	0.121	0.121	0.000	0.000	0.000	0.000
22	A	22	GLY	0	-0.014	0.007	26.831	0.068	0.068	0.000	0.000	0.000	0.000
23	A	23	ILE	0	-0.028	-0.017	25.975	-0.084	-0.084	0.000	0.000	0.000	0.000
24	A	24	SER	0	0.032	0.012	29.639	0.235	0.235	0.000	0.000	0.000	0.000
25	A	25	SER	0	-0.003	-0.026	31.358	-0.284	-0.284	0.000	0.000	0.000	0.000
26	A	26	ASP	-1	-0.801	-0.907	32.328	-9.853	-9.853	0.000	0.000	0.000	0.000
27	A	27	VAL	0	-0.008	-0.004	28.741	-0.128	-0.128	0.000	0.000	0.000	0.000
28	A	28	ILE	0	0.000	0.013	27.790	-0.457	-0.457	0.000	0.000	0.000	0.000
29	A	29	GLU	-1	-0.901	-0.938	28.214	-9.661	-9.661	0.000	0.000	0.000	0.000
30	A	30	LYS	1	0.837	0.906	29.678	9.445	9.445	0.000	0.000	0.000	0.000
31	A	31	ALA	0	-0.019	-0.007	24.502	-0.216	-0.216	0.000	0.000	0.000	0.000
32	A	32	ARG	1	0.871	0.940	24.665	10.774	10.774	0.000	0.000	0.000	0.000
33	A	33	ASN	0	-0.034	-0.016	26.212	-0.205	-0.205	0.000	0.000	0.000	0.000
34	A	34	PHE	0	-0.050	-0.015	22.404	0.156	0.156	0.000	0.000	0.000	0.000
35	A	35	LYS	1	0.905	0.934	21.579	14.140	14.140	0.000	0.000	0.000	0.000
36	A	36	ILE	0	0.011	0.014	17.887	0.045	0.045	0.000	0.000	0.000	0.000
37	A	37	VAL	0	-0.013	0.004	16.518	-0.600	-0.600	0.000	0.000	0.000	0.000
38	A	38	THR	0	-0.019	-0.035	11.513	0.870	0.870	0.000	0.000	0.000	0.000
39	A	39	GLU	-1	-0.923	-0.958	11.430	-22.358	-22.358	0.000	0.000	0.000	0.000
40	A	40	VAL	0	-0.032	-0.009	6.778	0.777	0.777	0.000	0.000	0.000	0.000
41	A	41	GLN	0	-0.004	-0.006	6.917	-1.253	-1.253	0.000	0.000	0.000	0.000
44	A	44	GLY	0	0.028	0.016	6.576	1.808	1.808	0.000	0.000	0.000	0.000
45	A	45	GLN	0	-0.052	-0.040	7.269	3.320	3.320	0.000	0.000	0.000	0.000
46	A	46	ASP	-1	-0.842	-0.915	8.940	-21.765	-21.765	0.000	0.000	0.000	0.000
47	A	47	PHE	0	0.018	-0.001	4.896	-6.199	-6.199	0.000	0.000	0.000	0.000
48	A	48	THR	0	0.014	0.015	9.040	3.387	3.387	0.000	0.000	0.000	0.000
49	A	49	TRP	0	-0.013	-0.020	7.431	-3.267	-3.267	0.000	0.000	0.000	0.000
50	A	50	SER	0	0.010	-0.003	11.544	2.479	2.479	0.000	0.000	0.000	0.000
51	A	51	GLN	0	0.027	0.037	14.238	-2.447	-2.447	0.000	0.000	0.000	0.000
52	A	52	HIS	0	0.083	0.048	16.286	1.642	1.642	0.000	0.000	0.000	0.000
53	A	53	TYR	0	0.005	-0.004	19.960	0.038	0.038	0.000	0.000	0.000	0.000
54	A	54	SER	0	0.011	-0.007	22.573	0.294	0.294	0.000	0.000	0.000	0.000
55	A	55	GLY	0	0.004	0.002	26.277	0.473	0.473	0.000	0.000	0.000	0.000
56	A	56	GLY	0	-0.014	0.002	23.250	0.173	0.173	0.000	0.000	0.000	0.000
57	A	57	HIS	0	-0.015	0.003	23.465	-0.220	-0.220	0.000	0.000	0.000	0.000
58	A	58	THR	0	0.008	-0.010	18.951	-0.353	-0.353	0.000	0.000	0.000	0.000
59	A	59	MET	0	-0.079	-0.014	18.981	0.971	0.971	0.000	0.000	0.000	0.000
60	A	60	THR	0	0.012	0.015	15.299	-0.575	-0.575	0.000	0.000	0.000	0.000
61	A	61	ASN	0	-0.040	-0.024	14.881	1.050	1.050	0.000	0.000	0.000	0.000
62	A	62	LYS	1	1.003	0.994	13.102	15.434	15.434	0.000	0.000	0.000	0.000
63	A	63	PHE	0	0.007	-0.002	8.854	1.561	1.561	0.000	0.000	0.000	0.000
64	A	64	THR	0	0.011	0.007	11.603	-1.234	-1.234	0.000	0.000	0.000	0.000
65	A	65	VAL	0	-0.035	-0.011	8.340	1.210	1.210	0.000	0.000	0.000	0.000
66	A	66	GLY	0	-0.033	-0.030	11.381	0.492	0.492	0.000	0.000	0.000	0.000
67	A	67	LYS	1	0.833	0.934	13.493	21.950	21.950	0.000	0.000	0.000	0.000
68	A	68	GLU	-1	-0.895	-0.947	16.212	-14.068	-14.068	0.000	0.000	0.000	0.000
69	A	69	SER	0	-0.032	-0.032	16.192	-0.742	-0.742	0.000	0.000	0.000	0.000
70	A	70	ASN	0	-0.029	-0.023	18.254	0.507	0.507	0.000	0.000	0.000	0.000
71	A	71	ILE	0	-0.021	-0.005	15.984	-0.633	-0.633	0.000	0.000	0.000	0.000
72	A	72	GLN	0	-0.007	-0.004	19.580	1.175	1.175	0.000	0.000	0.000	0.000
73	A	73	THR	0	-0.043	-0.038	20.487	-0.599	-0.599	0.000	0.000	0.000	0.000
74	A	74	MET	0	0.067	0.016	22.381	0.247	0.247	0.000	0.000	0.000	0.000
75	A	75	GLY	0	0.025	0.010	24.140	0.219	0.219	0.000	0.000	0.000	0.000
76	A	76	GLY	0	0.004	0.002	27.283	0.428	0.428	0.000	0.000	0.000	0.000
77	A	77	LYS	1	0.819	0.927	26.415	11.832	11.832	0.000	0.000	0.000	0.000
78	A	78	THR	0	-0.030	-0.027	23.725	-0.374	-0.374	0.000	0.000	0.000	0.000
79	A	79	PHE	0	0.005	0.019	19.367	0.526	0.526	0.000	0.000	0.000	0.000
80	A	80	LYS	1	0.929	0.971	21.456	11.790	11.790	0.000	0.000	0.000	0.000
81	A	81	ALA	0	0.048	0.028	18.201	0.349	0.349	0.000	0.000	0.000	0.000
82	A	82	THR	0	0.005	0.008	16.293	-0.124	-0.124	0.000	0.000	0.000	0.000
83	A	83	VAL	0	0.025	0.025	10.757	-0.099	-0.099	0.000	0.000	0.000	0.000
84	A	84	GLN	0	0.007	-0.005	11.892	0.342	0.342	0.000	0.000	0.000	0.000
85	A	85	MET	0	-0.011	-0.004	4.902	-3.569	-3.569	0.000	0.000	0.000	0.000
86	A	86	GLU	-1	-0.882	-0.924	9.229	-21.189	-21.189	0.000	0.000	0.000	0.000
87	A	87	GLY	0	-0.021	-0.019	8.927	0.497	0.497	0.000	0.000	0.000	0.000
88	A	88	GLY	0	-0.010	-0.014	5.120	-4.298	-4.298	0.000	0.000	0.000	0.000
89	A	89	LYS	1	0.895	0.959	5.370	21.431	21.431	0.000	0.000	0.000	0.000
90	A	90	LEU	0	0.008	0.010	6.531	0.713	0.713	0.000	0.000	0.000	0.000
91	A	91	VAL	0	-0.005	-0.005	8.265	2.141	2.141	0.000	0.000	0.000	0.000
92	A	92	VAL	0	-0.012	-0.009	12.057	-0.180	-0.180	0.000	0.000	0.000	0.000
93	A	93	ASN	0	0.000	0.013	14.648	1.323	1.323	0.000	0.000	0.000	0.000
94	A	94	PHE	0	0.035	0.005	16.438	-0.046	-0.046	0.000	0.000	0.000	0.000
95	A	95	PRO	0	0.020	-0.002	21.210	0.304	0.304	0.000	0.000	0.000	0.000
96	A	96	ASN	0	-0.047	-0.023	25.070	0.033	0.033	0.000	0.000	0.000	0.000
97	A	97	TYR	0	-0.012	0.001	18.059	0.291	0.291	0.000	0.000	0.000	0.000
98	A	98	HIS	0	-0.020	-0.009	17.083	-0.784	-0.784	0.000	0.000	0.000	0.000
99	A	99	GLN	0	-0.003	-0.008	13.273	1.821	1.821	0.000	0.000	0.000	0.000
100	A	100	THR	0	-0.040	0.002	12.121	-0.857	-0.857	0.000	0.000	0.000	0.000
101	A	101	SER	0	0.012	-0.017	9.439	2.084	2.084	0.000	0.000	0.000	0.000
102	A	102	GLU	-1	-0.930	-0.977	6.851	-32.189	-32.189	0.000	0.000	0.000	0.000
104	A	104	VAL	0	0.028	0.011	5.934	0.001	0.001	0.000	0.000	0.000	0.000
105	A	105	GLY	0	0.004	-0.002	9.008	1.416	1.416	0.000	0.000	0.000	0.000
106	A	106	ASP	-1	-0.875	-0.931	7.249	-35.847	-35.847	0.000	0.000	0.000	0.000
107	A	107	LYS	1	0.875	0.942	8.647	27.752	27.752	0.000	0.000	0.000	0.000
108	A	108	LEU	0	0.001	0.022	8.050	-3.709	-3.709	0.000	0.000	0.000	0.000
109	A	109	VAL	0	-0.016	-0.010	9.360	3.493	3.493	0.000	0.000	0.000	0.000
110	A	110	GLU	-1	-0.771	-0.882	10.561	-27.088	-27.088	0.000	0.000	0.000	0.000
111	A	111	VAL	0	0.020	0.014	13.055	1.677	1.677	0.000	0.000	0.000	0.000
112	A	112	SER	0	0.004	0.010	15.853	-0.312	-0.312	0.000	0.000	0.000	0.000
113	A	113	THR	0	-0.046	-0.040	18.039	0.629	0.629	0.000	0.000	0.000	0.000
114	A	114	ILE	0	0.021	0.017	21.487	-0.156	-0.156	0.000	0.000	0.000	0.000
115	A	115	GLY	0	0.021	0.009	24.634	0.296	0.296	0.000	0.000	0.000	0.000
116	A	116	GLY	0	-0.004	0.003	28.322	0.119	0.119	0.000	0.000	0.000	0.000
117	A	117	VAL	0	-0.050	-0.010	25.471	0.187	0.187	0.000	0.000	0.000	0.000
118	A	118	THR	0	0.035	0.009	20.782	-0.595	-0.595	0.000	0.000	0.000	0.000
119	A	119	TYR	0	0.008	-0.012	20.089	0.330	0.330	0.000	0.000	0.000	0.000
120	A	120	GLU	-1	-0.847	-0.901	16.915	-17.476	-17.476	0.000	0.000	0.000	0.000
121	A	121	ARG	1	0.833	0.907	15.067	20.276	20.276	0.000	0.000	0.000	0.000
122	A	122	VAL	0	0.018	0.016	14.483	-1.520	-1.520	0.000	0.000	0.000	0.000
123	A	123	SER	0	-0.007	-0.033	12.586	0.631	0.631	0.000	0.000	0.000	0.000
124	A	124	LYS	1	0.866	0.914	12.236	14.586	14.586	0.000	0.000	0.000	0.000
126	A	126	LEU	0	-0.043	-0.018	11.065	1.905	1.905	0.000	0.000	0.000	0.000
127	A	127	ALA	-1	-0.853	-0.913	11.557	-22.122	-22.122	0.000	0.000	0.000	0.000

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