FMO DATABASE

FMODB ID: VV371

Calculation Name: 1XPP-A-Xray547

Preferred Name:

Target Type:

Ligand Name: thiocyanate ion | acetic acid | formic acid

Ligand 3-letter code: SCN | ACY | FMT

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1XPP

Chain ID: A

ChEMBL ID:

UniProt ID: Q9HIC5

Base Structure: X-ray

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	99
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-707798.186213
FMO2-HF: Nuclear repulsion	667516.450648
FMO2-HF: Total energy	-40281.735565
FMO2-MP2: Total energy	-40401.367771

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:7:ALA)

Summations of interaction energy for fragment #1(A:7: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.
24.064	26.337	1.192	-1.421	-2.044	-0.013

Interaction energy analysis for fragmet #1(A:7:ALA)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.825 / q_NPA : 0.906

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	9	SER	0	-0.006	-0.012	3.582	-5.000	-3.684	0.026	-0.669	-0.673	-0.002
21	A	27	ASN	0	-0.020	-0.018	2.716	-2.135	-1.178	1.166	-0.752	-1.371	-0.011
4	A	10	SER	0	-0.032	-0.005	5.966	3.474	3.474	0.000	0.000	0.000	0.000
5	A	11	LEU	0	0.007	-0.008	8.105	0.944	0.944	0.000	0.000	0.000	0.000
6	A	12	ARG	1	0.962	0.982	11.320	19.410	19.410	0.000	0.000	0.000	0.000
7	A	13	VAL	0	-0.018	0.001	13.956	0.277	0.277	0.000	0.000	0.000	0.000
8	A	14	ILE	0	-0.048	-0.016	14.779	-0.070	-0.070	0.000	0.000	0.000	0.000
9	A	15	SER	0	0.030	0.004	18.677	0.660	0.660	0.000	0.000	0.000	0.000
10	A	16	LYS	0	-0.006	0.006	22.423	-0.413	-0.413	0.000	0.000	0.000	0.000
11	A	17	GLU	-1	-0.840	-0.902	25.000	-10.357	-10.357	0.000	0.000	0.000	0.000
12	A	18	LYS	1	0.898	0.963	28.827	8.575	8.575	0.000	0.000	0.000	0.000
13	A	19	ASN	0	0.020	-0.007	30.695	-0.020	-0.020	0.000	0.000	0.000	0.000
14	A	20	SER	0	-0.026	-0.018	27.042	-0.223	-0.223	0.000	0.000	0.000	0.000
15	A	21	ILE	0	-0.040	-0.031	20.796	0.008	0.008	0.000	0.000	0.000	0.000
16	A	22	THR	0	0.049	0.029	18.907	-0.014	-0.014	0.000	0.000	0.000	0.000
17	A	23	VAL	0	-0.021	-0.023	14.814	-0.036	-0.036	0.000	0.000	0.000	0.000
18	A	24	GLU	-1	-0.850	-0.916	11.264	-22.875	-22.875	0.000	0.000	0.000	0.000
19	A	25	MET	0	-0.036	-0.023	11.289	-0.321	-0.321	0.000	0.000	0.000	0.000
20	A	26	ILE	0	0.012	0.007	5.270	-0.086	-0.086	0.000	0.000	0.000	0.000
22	A	28	TYR	0	0.020	0.018	5.796	-2.347	-2.347	0.000	0.000	0.000	0.000
23	A	29	ASP	-1	-0.826	-0.917	9.180	-24.316	-24.316	0.000	0.000	0.000	0.000
24	A	30	ASN	0	-0.002	-0.013	10.787	2.949	2.949	0.000	0.000	0.000	0.000
25	A	31	THR	0	0.018	0.020	13.993	1.845	1.845	0.000	0.000	0.000	0.000
26	A	32	LEU	0	0.023	0.023	12.567	1.052	1.052	0.000	0.000	0.000	0.000
27	A	33	LEU	0	0.016	0.010	11.950	1.368	1.368	0.000	0.000	0.000	0.000
28	A	34	ARG	1	1.002	1.004	15.985	14.960	14.960	0.000	0.000	0.000	0.000
29	A	35	THR	0	0.004	-0.012	18.355	0.724	0.724	0.000	0.000	0.000	0.000
30	A	36	LEU	0	-0.005	0.007	16.634	0.732	0.732	0.000	0.000	0.000	0.000
31	A	37	VAL	0	-0.015	-0.019	19.865	0.704	0.704	0.000	0.000	0.000	0.000
32	A	38	GLU	-1	-0.891	-0.928	22.100	-12.100	-12.100	0.000	0.000	0.000	0.000
33	A	39	GLU	-1	-0.811	-0.896	23.504	-11.294	-11.294	0.000	0.000	0.000	0.000
34	A	40	ILE	0	-0.052	-0.035	21.270	0.480	0.480	0.000	0.000	0.000	0.000
35	A	41	LEU	0	-0.037	-0.027	25.400	0.498	0.498	0.000	0.000	0.000	0.000
36	A	42	LYS	1	0.789	0.888	26.800	12.271	12.271	0.000	0.000	0.000	0.000
37	A	43	ASP	-1	-0.825	-0.884	29.307	-10.154	-10.154	0.000	0.000	0.000	0.000
38	A	44	ASP	-1	-0.815	-0.903	31.032	-9.062	-9.062	0.000	0.000	0.000	0.000
39	A	45	GLN	0	-0.048	-0.021	32.232	0.281	0.281	0.000	0.000	0.000	0.000
40	A	46	VAL	0	-0.051	-0.025	27.782	-0.068	-0.068	0.000	0.000	0.000	0.000
41	A	47	ASP	-1	-0.868	-0.918	30.372	-8.998	-8.998	0.000	0.000	0.000	0.000
42	A	48	GLU	-1	-0.803	-0.882	26.624	-11.189	-11.189	0.000	0.000	0.000	0.000
43	A	49	ALA	0	0.015	-0.002	23.909	-0.226	-0.226	0.000	0.000	0.000	0.000
44	A	50	ARG	1	0.871	0.950	22.533	12.769	12.769	0.000	0.000	0.000	0.000
45	A	51	TYR	0	0.016	-0.008	15.826	-0.548	-0.548	0.000	0.000	0.000	0.000
46	A	52	TYR	0	-0.047	-0.039	19.059	0.793	0.793	0.000	0.000	0.000	0.000
47	A	53	ILE	0	0.003	0.003	14.730	-0.762	-0.762	0.000	0.000	0.000	0.000
48	A	54	LYS	1	0.950	0.981	17.741	15.884	15.884	0.000	0.000	0.000	0.000
49	A	55	HIS	1	0.827	0.888	16.403	17.075	17.075	0.000	0.000	0.000	0.000
50	A	56	PRO	0	0.016	-0.009	16.065	-1.151	-1.151	0.000	0.000	0.000	0.000
51	A	57	VAL	0	0.014	0.017	14.982	-0.361	-0.361	0.000	0.000	0.000	0.000
52	A	58	ILE	0	-0.023	-0.008	13.001	-0.462	-0.462	0.000	0.000	0.000	0.000
53	A	59	ASP	-1	-0.775	-0.860	11.743	-19.468	-19.468	0.000	0.000	0.000	0.000
54	A	60	ASN	0	0.013	-0.011	8.089	-2.954	-2.954	0.000	0.000	0.000	0.000
55	A	61	PRO	0	-0.022	0.000	10.975	1.953	1.953	0.000	0.000	0.000	0.000
56	A	62	GLN	0	0.005	-0.009	13.499	0.024	0.024	0.000	0.000	0.000	0.000
57	A	63	ILE	0	-0.022	0.000	16.106	0.853	0.853	0.000	0.000	0.000	0.000
58	A	64	TYR	0	0.012	0.011	18.397	0.179	0.179	0.000	0.000	0.000	0.000
59	A	65	VAL	0	-0.011	-0.020	21.919	0.082	0.082	0.000	0.000	0.000	0.000
60	A	66	ARG	1	0.803	0.878	24.528	10.230	10.230	0.000	0.000	0.000	0.000
61	A	67	VAL	0	-0.029	-0.009	28.249	-0.038	-0.038	0.000	0.000	0.000	0.000
62	A	68	LYS	1	0.871	0.930	30.784	9.256	9.256	0.000	0.000	0.000	0.000
63	A	69	SER	0	-0.019	-0.022	33.726	0.282	0.282	0.000	0.000	0.000	0.000
64	A	70	GLY	0	0.001	0.007	32.855	-0.240	-0.240	0.000	0.000	0.000	0.000
65	A	71	LYS	1	0.971	0.982	28.151	10.478	10.478	0.000	0.000	0.000	0.000
66	A	72	PRO	0	0.086	0.055	25.650	-0.097	-0.097	0.000	0.000	0.000	0.000
67	A	73	GLN	0	0.020	-0.025	22.955	0.043	0.043	0.000	0.000	0.000	0.000
68	A	74	SER	0	-0.085	-0.047	24.349	-0.309	-0.309	0.000	0.000	0.000	0.000
69	A	75	ALA	0	0.065	0.043	26.370	-0.004	-0.004	0.000	0.000	0.000	0.000
70	A	76	ILE	0	0.026	0.021	19.760	-0.154	-0.154	0.000	0.000	0.000	0.000
71	A	77	LYS	1	0.925	0.960	22.390	12.216	12.216	0.000	0.000	0.000	0.000
72	A	78	ARG	1	0.840	0.901	23.748	10.448	10.448	0.000	0.000	0.000	0.000
73	A	79	ALA	0	0.041	0.030	23.042	0.059	0.059	0.000	0.000	0.000	0.000
74	A	80	VAL	0	0.047	0.017	18.869	-0.130	-0.130	0.000	0.000	0.000	0.000
75	A	81	ARG	1	0.929	0.974	21.412	13.335	13.335	0.000	0.000	0.000	0.000
76	A	82	LYS	1	0.916	0.962	24.260	11.398	11.398	0.000	0.000	0.000	0.000
77	A	83	LEU	0	0.009	0.006	19.963	0.116	0.116	0.000	0.000	0.000	0.000
78	A	84	SER	0	-0.066	-0.039	21.069	-0.407	-0.407	0.000	0.000	0.000	0.000
79	A	85	LYS	1	0.844	0.902	22.210	10.975	10.975	0.000	0.000	0.000	0.000
80	A	86	LEU	0	0.006	0.010	24.640	0.346	0.346	0.000	0.000	0.000	0.000
81	A	87	TYR	0	0.011	-0.002	21.305	0.255	0.255	0.000	0.000	0.000	0.000
82	A	88	GLU	-1	-0.919	-0.954	23.387	-13.368	-13.368	0.000	0.000	0.000	0.000
83	A	89	ASP	-1	-0.816	-0.883	25.322	-10.426	-10.426	0.000	0.000	0.000	0.000
84	A	90	LEU	0	0.003	0.005	24.716	0.273	0.273	0.000	0.000	0.000	0.000
85	A	91	GLY	0	0.010	0.004	25.513	0.163	0.163	0.000	0.000	0.000	0.000
86	A	92	THR	0	-0.044	-0.033	26.277	0.369	0.369	0.000	0.000	0.000	0.000
87	A	93	GLN	0	-0.055	-0.036	29.686	0.201	0.201	0.000	0.000	0.000	0.000
88	A	94	PHE	0	0.028	0.013	26.353	0.282	0.282	0.000	0.000	0.000	0.000
89	A	95	GLN	0	-0.032	0.001	28.648	0.387	0.387	0.000	0.000	0.000	0.000
90	A	96	LYS	1	0.945	0.959	30.656	9.374	9.374	0.000	0.000	0.000	0.000
91	A	97	GLU	-1	-0.926	-0.957	33.363	-8.429	-8.429	0.000	0.000	0.000	0.000
92	A	98	PHE	0	-0.007	-0.016	27.821	0.157	0.157	0.000	0.000	0.000	0.000
93	A	99	GLN	0	0.020	0.012	33.573	0.058	0.058	0.000	0.000	0.000	0.000
94	A	100	ARG	1	0.906	0.979	35.638	8.586	8.586	0.000	0.000	0.000	0.000
95	A	101	TYR	0	0.058	0.021	36.446	0.259	0.259	0.000	0.000	0.000	0.000
96	A	102	GLU	-1	-0.990	-1.004	35.014	-8.942	-8.942	0.000	0.000	0.000	0.000
97	A	103	SER	0	-0.039	-0.033	38.147	0.177	0.177	0.000	0.000	0.000	0.000
98	A	104	ASP	-1	-0.993	-0.988	40.963	-7.363	-7.363	0.000	0.000	0.000	0.000
99	A	105	HIS	0	-0.110	-0.033	40.601	0.434	0.434	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:7:ALA)