FMO DATABASE

FMODB ID: 9R4G2

Calculation Name: 1TFP-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1TFP

Chain ID: A

ChEMBL ID:

UniProt ID: P27731

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	114
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-865268.758916
FMO2-HF: Nuclear repulsion	821768.243582
FMO2-HF: Total energy	-43500.515334
FMO2-MP2: Total energy	-43628.975142

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:10:CYS)

Summations of interaction energy for fragment #1(A:10:CYS)

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.
-12.526	-17.717	21.916	-3.543	-13.182	-0.032

Interaction energy analysis for fragmet #1(A:10:CYS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.078 / q_NPA : -0.019

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	12	LEU	0	0.022	0.010	3.106	1.020	2.950	0.047	-0.880	-1.097	0.001
4	A	13	MET	0	-0.012	0.002	2.390	-6.672	-4.162	5.134	-3.136	-4.507	-0.030
5	A	14	VAL	0	0.034	0.009	4.086	-0.456	-0.325	0.001	-0.041	-0.090	0.000
47	A	56	HIS	0	-0.043	-0.022	3.538	0.963	1.907	0.449	-0.575	-0.818	0.004
48	A	57	GLU	-1	-0.891	-0.970	2.283	7.818	0.020	15.338	-3.924	-3.617	0.007
49	A	58	LEU	0	-0.034	-0.009	3.204	-6.666	-11.885	0.633	6.105	-1.519	-0.003
50	A	59	THR	0	-0.009	-0.015	2.948	-5.996	-5.407	0.030	-0.175	-0.445	0.000
51	A	60	THR	0	-0.004	-0.021	2.813	-0.083	1.670	0.285	-0.907	-1.131	-0.011
52	A	61	GLU	-1	-0.861	-0.951	4.634	-8.427	-8.458	-0.001	-0.010	0.042	0.000
6	A	15	LYS	1	0.788	0.880	7.587	0.285	0.285	0.000	0.000	0.000	0.000
7	A	16	VAL	0	0.013	0.008	10.537	-0.301	-0.301	0.000	0.000	0.000	0.000
8	A	17	LEU	0	0.011	0.002	13.808	0.102	0.102	0.000	0.000	0.000	0.000
9	A	18	ASP	-1	-0.736	-0.834	17.326	0.506	0.506	0.000	0.000	0.000	0.000
10	A	19	ALA	0	0.008	-0.007	20.775	-0.044	-0.044	0.000	0.000	0.000	0.000
11	A	20	VAL	0	-0.062	-0.028	23.743	-0.033	-0.033	0.000	0.000	0.000	0.000
12	A	21	ARG	1	0.834	0.901	23.034	-0.632	-0.632	0.000	0.000	0.000	0.000
13	A	22	GLY	0	0.000	0.024	23.827	-0.007	-0.007	0.000	0.000	0.000	0.000
14	A	23	SER	0	-0.027	-0.018	20.431	-0.042	-0.042	0.000	0.000	0.000	0.000
15	A	24	PRO	0	0.010	-0.001	15.339	-0.061	-0.061	0.000	0.000	0.000	0.000
16	A	25	ALA	0	0.001	0.020	16.142	0.008	0.008	0.000	0.000	0.000	0.000
17	A	26	ALA	0	0.050	0.041	15.346	0.233	0.233	0.000	0.000	0.000	0.000
18	A	27	ASN	0	-0.018	-0.025	15.541	-0.254	-0.254	0.000	0.000	0.000	0.000
19	A	28	VAL	0	0.012	0.015	14.123	-0.090	-0.090	0.000	0.000	0.000	0.000
20	A	29	ALA	0	-0.021	-0.018	14.424	0.366	0.366	0.000	0.000	0.000	0.000
21	A	30	VAL	0	-0.011	0.000	10.069	-0.279	-0.279	0.000	0.000	0.000	0.000
22	A	31	LYS	1	0.810	0.900	12.218	-0.766	-0.766	0.000	0.000	0.000	0.000
23	A	32	VAL	0	0.009	0.004	8.498	-0.301	-0.301	0.000	0.000	0.000	0.000
24	A	33	PHE	0	0.029	0.008	11.821	0.111	0.111	0.000	0.000	0.000	0.000
25	A	34	LYS	1	0.830	0.905	12.727	0.215	0.215	0.000	0.000	0.000	0.000
26	A	35	LYS	1	0.831	0.925	15.024	0.070	0.070	0.000	0.000	0.000	0.000
27	A	36	ALA	0	0.033	0.028	18.621	-0.070	-0.070	0.000	0.000	0.000	0.000
28	A	37	ALA	0	0.009	-0.011	20.590	-0.041	-0.041	0.000	0.000	0.000	0.000
29	A	38	ASP	-1	-0.901	-0.956	23.634	0.136	0.136	0.000	0.000	0.000	0.000
30	A	39	GLY	0	-0.037	-0.007	24.164	0.011	0.011	0.000	0.000	0.000	0.000
31	A	40	THR	0	-0.027	-0.015	22.163	0.006	0.006	0.000	0.000	0.000	0.000
32	A	41	TRP	0	-0.023	-0.022	16.425	-0.048	-0.048	0.000	0.000	0.000	0.000
33	A	42	GLN	0	0.039	0.025	16.814	0.017	0.017	0.000	0.000	0.000	0.000
34	A	43	ASP	-1	-0.914	-0.963	15.041	1.578	1.578	0.000	0.000	0.000	0.000
35	A	44	PHE	0	-0.057	-0.032	7.469	-0.095	-0.095	0.000	0.000	0.000	0.000
36	A	45	ALA	0	0.039	0.022	8.270	0.324	0.324	0.000	0.000	0.000	0.000
37	A	46	THR	0	-0.005	-0.006	10.248	-0.464	-0.464	0.000	0.000	0.000	0.000
38	A	47	GLY	0	0.045	0.026	10.444	0.836	0.836	0.000	0.000	0.000	0.000
39	A	48	LYS	1	0.830	0.906	11.514	-2.518	-2.518	0.000	0.000	0.000	0.000
40	A	49	THR	0	-0.042	-0.015	10.937	0.558	0.558	0.000	0.000	0.000	0.000
41	A	50	THR	0	0.031	0.002	10.144	-0.768	-0.768	0.000	0.000	0.000	0.000
42	A	51	GLU	-1	-0.927	-0.975	12.700	1.149	1.149	0.000	0.000	0.000	0.000
43	A	52	PHE	0	0.020	0.011	12.028	-0.350	-0.350	0.000	0.000	0.000	0.000
44	A	53	GLY	0	0.016	0.018	13.095	-0.336	-0.336	0.000	0.000	0.000	0.000
45	A	54	GLU	-1	-0.839	-0.896	7.847	0.924	0.924	0.000	0.000	0.000	0.000
46	A	55	ILE	0	-0.013	-0.008	6.417	-0.724	-0.724	0.000	0.000	0.000	0.000
53	A	62	GLU	-1	-0.903	-0.938	6.388	-0.249	-0.249	0.000	0.000	0.000	0.000
54	A	63	GLN	0	-0.007	0.012	7.676	-0.033	-0.033	0.000	0.000	0.000	0.000
55	A	64	PHE	0	-0.055	-0.026	6.212	0.016	0.016	0.000	0.000	0.000	0.000
56	A	65	VAL	0	0.002	0.000	8.323	-0.591	-0.591	0.000	0.000	0.000	0.000
57	A	66	GLU	-1	-0.869	-0.935	12.020	-1.030	-1.030	0.000	0.000	0.000	0.000
58	A	67	GLY	0	-0.016	0.003	14.575	0.271	0.271	0.000	0.000	0.000	0.000
59	A	68	VAL	0	-0.046	-0.016	14.797	-0.132	-0.132	0.000	0.000	0.000	0.000
60	A	69	TYR	0	0.037	0.003	10.623	0.289	0.289	0.000	0.000	0.000	0.000
61	A	70	ARG	1	0.817	0.911	14.066	-0.618	-0.618	0.000	0.000	0.000	0.000
62	A	71	VAL	0	-0.024	-0.004	10.186	0.194	0.194	0.000	0.000	0.000	0.000
63	A	72	GLU	-1	-0.779	-0.879	13.058	0.702	0.702	0.000	0.000	0.000	0.000
64	A	73	PHE	0	0.009	-0.014	11.580	0.314	0.314	0.000	0.000	0.000	0.000
65	A	74	ASP	-1	-0.811	-0.874	15.914	0.793	0.793	0.000	0.000	0.000	0.000
66	A	75	THR	0	-0.004	-0.019	18.181	0.092	0.092	0.000	0.000	0.000	0.000
67	A	76	SER	0	0.033	0.016	20.588	-0.088	-0.088	0.000	0.000	0.000	0.000
68	A	77	SER	0	-0.083	-0.061	23.221	-0.050	-0.050	0.000	0.000	0.000	0.000
69	A	78	TYR	0	-0.037	-0.034	19.690	0.030	0.030	0.000	0.000	0.000	0.000
70	A	79	TRP	0	0.054	0.015	22.654	-0.003	-0.003	0.000	0.000	0.000	0.000
71	A	80	LYS	1	0.903	0.960	26.096	-0.640	-0.640	0.000	0.000	0.000	0.000
72	A	81	GLY	0	-0.017	-0.016	27.645	-0.037	-0.037	0.000	0.000	0.000	0.000
73	A	82	LEU	0	-0.005	-0.006	26.588	-0.013	-0.013	0.000	0.000	0.000	0.000
74	A	83	GLY	0	-0.022	0.006	30.070	-0.037	-0.037	0.000	0.000	0.000	0.000
75	A	84	LEU	0	-0.004	-0.003	28.654	-0.028	-0.028	0.000	0.000	0.000	0.000
76	A	85	SER	0	-0.006	-0.012	27.563	-0.024	-0.024	0.000	0.000	0.000	0.000
77	A	86	PRO	0	-0.042	-0.018	29.562	0.035	0.035	0.000	0.000	0.000	0.000
78	A	87	PHE	0	0.003	-0.009	30.743	-0.001	-0.001	0.000	0.000	0.000	0.000
79	A	88	HIS	0	-0.108	-0.049	27.056	0.019	0.019	0.000	0.000	0.000	0.000
80	A	89	GLU	-1	-0.845	-0.924	24.579	0.223	0.223	0.000	0.000	0.000	0.000
81	A	90	TYR	0	-0.064	-0.024	19.847	0.075	0.075	0.000	0.000	0.000	0.000
82	A	91	ALA	0	0.023	0.017	19.112	-0.073	-0.073	0.000	0.000	0.000	0.000
83	A	92	ASP	-1	-0.824	-0.913	17.268	0.544	0.544	0.000	0.000	0.000	0.000
84	A	93	VAL	0	-0.041	-0.015	14.159	-0.117	-0.117	0.000	0.000	0.000	0.000
85	A	94	VAL	0	-0.020	-0.018	15.227	0.061	0.061	0.000	0.000	0.000	0.000
86	A	95	PHE	0	-0.010	-0.004	9.942	-0.083	-0.083	0.000	0.000	0.000	0.000
87	A	96	THR	0	0.020	0.002	15.261	0.126	0.126	0.000	0.000	0.000	0.000
88	A	97	ALA	0	-0.008	0.009	11.101	-0.163	-0.163	0.000	0.000	0.000	0.000
89	A	98	ASN	0	0.022	0.006	9.848	-0.026	-0.026	0.000	0.000	0.000	0.000
90	A	99	ASP	-1	-0.867	-0.929	14.221	-1.047	-1.047	0.000	0.000	0.000	0.000
91	A	100	SER	0	-0.058	-0.033	16.742	0.067	0.067	0.000	0.000	0.000	0.000
92	A	101	GLY	0	-0.003	0.010	16.010	-0.158	-0.158	0.000	0.000	0.000	0.000
93	A	102	HIS	0	0.029	0.010	10.375	-0.029	-0.029	0.000	0.000	0.000	0.000
94	A	103	ARG	1	0.947	0.986	10.367	2.419	2.419	0.000	0.000	0.000	0.000
95	A	104	HIS	1	0.806	0.898	5.281	9.501	9.501	0.000	0.000	0.000	0.000
96	A	105	TYR	0	0.028	0.008	6.570	1.882	1.882	0.000	0.000	0.000	0.000
97	A	106	THR	0	0.013	0.007	6.265	-1.078	-1.078	0.000	0.000	0.000	0.000
98	A	107	ILE	0	-0.016	-0.007	8.000	0.489	0.489	0.000	0.000	0.000	0.000
99	A	108	ALA	0	0.021	0.014	10.232	0.466	0.466	0.000	0.000	0.000	0.000
100	A	109	ALA	0	-0.004	-0.007	12.493	0.009	0.009	0.000	0.000	0.000	0.000
101	A	110	LEU	0	-0.036	-0.012	15.120	0.086	0.086	0.000	0.000	0.000	0.000
102	A	111	LEU	0	0.000	0.002	17.108	-0.011	-0.011	0.000	0.000	0.000	0.000
103	A	112	SER	0	0.016	-0.005	20.538	-0.024	-0.024	0.000	0.000	0.000	0.000
104	A	113	PRO	0	-0.051	-0.030	24.354	0.011	0.011	0.000	0.000	0.000	0.000
105	A	114	PHE	0	-0.003	0.016	26.665	0.023	0.023	0.000	0.000	0.000	0.000
106	A	115	SER	0	0.030	0.014	25.315	-0.048	-0.048	0.000	0.000	0.000	0.000
107	A	116	TYR	0	0.034	0.004	19.333	0.029	0.029	0.000	0.000	0.000	0.000
108	A	117	SER	0	-0.017	0.007	20.105	-0.082	-0.082	0.000	0.000	0.000	0.000
109	A	118	THR	0	0.031	-0.005	15.472	0.093	0.093	0.000	0.000	0.000	0.000
110	A	119	THR	0	-0.031	-0.009	15.243	-0.040	-0.040	0.000	0.000	0.000	0.000
111	A	120	ALA	0	0.009	0.004	12.314	-0.080	-0.080	0.000	0.000	0.000	0.000
112	A	121	VAL	0	-0.008	-0.007	11.071	0.087	0.087	0.000	0.000	0.000	0.000
113	A	122	VAL	0	-0.029	-0.014	10.501	-0.617	-0.617	0.000	0.000	0.000	0.000
114	A	123	SER	-1	-0.894	-0.938	9.308	-4.934	-4.934	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:10:CYS)