FMO DATABASE

FMODB ID: 5GGNZ

Calculation Name: 6FXC-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 6FXC

Chain ID: A

ChEMBL ID:

UniProt ID: Q2YSH7

Base Structure: ElectronMicroscopy

Registration Date: 2025-10-06

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	103
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-675055.934002
FMO2-HF: Nuclear repulsion	636236.460106
FMO2-HF: Total energy	-38819.473896
FMO2-MP2: Total energy	-38934.939744

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:2:HIS)

Summations of interaction energy for fragment #1(A:2:HIS)

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.
135.195	139.618	4.894	-3.52	-5.792	-0.032

Interaction energy analysis for fragmet #1(A:2:HIS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.813 / q_NPA : 0.901

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	4	LYS	1	0.950	0.965	3.833	42.650	44.370	-0.023	-0.581	-1.117	-0.001
27	A	28	PRO	0	0.046	0.023	4.681	0.161	0.196	-0.001	-0.003	-0.030	0.000
64	A	65	VAL	0	0.030	0.000	3.997	-1.120	-0.951	-0.001	-0.026	-0.142	0.000
69	A	70	LEU	0	0.004	0.009	3.925	0.420	0.599	0.000	-0.051	-0.127	0.000
80	A	81	VAL	0	0.005	0.009	2.021	-4.595	-4.691	3.587	-1.594	-1.896	-0.019
81	A	82	GLY	0	-0.031	-0.019	4.897	-1.942	-1.831	-0.001	-0.003	-0.106	0.000
82	A	83	TYR	0	-0.029	-0.028	2.400	-7.499	-5.338	1.334	-1.247	-2.247	-0.012
91	A	92	ARG	1	0.731	0.815	4.712	40.959	41.103	-0.001	-0.015	-0.127	0.000
4	A	5	LYS	1	0.945	0.960	6.504	22.410	22.410	0.000	0.000	0.000	0.000
5	A	6	GLY	0	0.104	0.065	9.375	1.817	1.817	0.000	0.000	0.000	0.000
6	A	7	ASP	-1	-0.784	-0.851	6.919	-40.939	-40.939	0.000	0.000	0.000	0.000
7	A	8	ASN	0	-0.002	-0.011	10.095	1.237	1.237	0.000	0.000	0.000	0.000
8	A	9	VAL	0	-0.066	-0.033	7.167	-3.189	-3.189	0.000	0.000	0.000	0.000
9	A	10	LYS	1	0.996	1.016	9.601	21.961	21.961	0.000	0.000	0.000	0.000
10	A	11	VAL	0	-0.007	0.013	10.123	-2.419	-2.419	0.000	0.000	0.000	0.000
11	A	12	ILE	0	-0.042	-0.018	9.364	1.471	1.471	0.000	0.000	0.000	0.000
12	A	13	ALA	0	-0.024	-0.028	13.303	1.748	1.748	0.000	0.000	0.000	0.000
13	A	14	GLY	0	0.047	0.020	14.783	-1.016	-1.016	0.000	0.000	0.000	0.000
14	A	15	LYS	1	0.942	0.971	17.571	13.677	13.677	0.000	0.000	0.000	0.000
15	A	16	ASP	-1	-0.770	-0.856	17.590	-14.705	-14.705	0.000	0.000	0.000	0.000
16	A	17	LYS	1	0.890	0.933	16.082	15.594	15.594	0.000	0.000	0.000	0.000
17	A	18	GLY	0	-0.042	-0.034	15.628	0.904	0.904	0.000	0.000	0.000	0.000
18	A	19	LYS	1	0.866	0.921	16.603	15.387	15.387	0.000	0.000	0.000	0.000
19	A	20	GLU	-1	-0.814	-0.920	14.397	-22.298	-22.298	0.000	0.000	0.000	0.000
20	A	21	GLY	0	0.064	0.029	14.014	1.071	1.071	0.000	0.000	0.000	0.000
21	A	22	LYS	1	0.861	0.938	12.783	19.206	19.206	0.000	0.000	0.000	0.000
22	A	23	VAL	0	-0.058	-0.015	8.850	0.684	0.684	0.000	0.000	0.000	0.000
23	A	24	ILE	0	0.053	0.025	11.892	0.445	0.445	0.000	0.000	0.000	0.000
24	A	25	ALA	0	-0.057	-0.044	10.895	0.484	0.484	0.000	0.000	0.000	0.000
25	A	26	THR	0	0.031	-0.008	5.126	-0.311	-0.311	0.000	0.000	0.000	0.000
26	A	27	LEU	0	0.001	0.011	7.430	-0.487	-0.487	0.000	0.000	0.000	0.000
28	A	29	LYS	1	0.947	0.960	6.171	17.631	17.631	0.000	0.000	0.000	0.000
29	A	30	LYS	1	0.917	0.960	8.842	19.169	19.169	0.000	0.000	0.000	0.000
30	A	31	ASP	-1	-0.823	-0.903	6.791	-26.986	-26.986	0.000	0.000	0.000	0.000
31	A	32	ARG	1	0.882	0.942	7.726	19.288	19.288	0.000	0.000	0.000	0.000
32	A	33	VAL	0	0.036	0.029	6.626	0.904	0.904	0.000	0.000	0.000	0.000
33	A	34	VAL	0	0.014	0.011	9.802	1.228	1.228	0.000	0.000	0.000	0.000
34	A	35	VAL	0	-0.014	-0.013	11.514	-1.245	-1.245	0.000	0.000	0.000	0.000
35	A	36	GLU	-1	-0.875	-0.929	14.160	-16.718	-16.718	0.000	0.000	0.000	0.000
36	A	37	GLY	0	0.038	0.010	17.576	-0.257	-0.257	0.000	0.000	0.000	0.000
37	A	38	VAL	0	-0.058	-0.031	15.325	0.161	0.161	0.000	0.000	0.000	0.000
38	A	39	ASN	0	-0.081	-0.043	16.293	0.380	0.380	0.000	0.000	0.000	0.000
39	A	40	ILE	0	0.062	0.039	19.689	-0.036	-0.036	0.000	0.000	0.000	0.000
40	A	41	MET	0	-0.067	-0.020	20.477	0.645	0.645	0.000	0.000	0.000	0.000
41	A	42	LYS	1	0.888	0.919	24.099	10.832	10.832	0.000	0.000	0.000	0.000
42	A	43	LYS	1	0.862	0.929	24.175	11.491	11.491	0.000	0.000	0.000	0.000
43	A	44	HIS	0	0.085	0.042	28.195	0.193	0.193	0.000	0.000	0.000	0.000
44	A	45	GLN	0	-0.028	-0.006	27.695	-0.540	-0.540	0.000	0.000	0.000	0.000
45	A	46	LYS	1	1.038	1.025	32.116	8.356	8.356	0.000	0.000	0.000	0.000
46	A	47	PRO	0	0.010	0.014	33.919	-0.238	-0.238	0.000	0.000	0.000	0.000
47	A	48	THR	0	-0.023	-0.026	31.305	0.032	0.032	0.000	0.000	0.000	0.000
48	A	49	GLN	0	0.008	-0.002	34.384	0.006	0.006	0.000	0.000	0.000	0.000
49	A	50	LEU	0	-0.023	-0.005	31.757	0.143	0.143	0.000	0.000	0.000	0.000
50	A	51	ASN	0	-0.032	-0.015	32.055	-0.324	-0.324	0.000	0.000	0.000	0.000
51	A	52	PRO	0	0.053	0.020	34.168	0.181	0.181	0.000	0.000	0.000	0.000
52	A	53	GLU	-1	-0.939	-0.955	34.927	-8.075	-8.075	0.000	0.000	0.000	0.000
53	A	54	GLY	0	-0.005	0.001	34.119	-0.288	-0.288	0.000	0.000	0.000	0.000
54	A	55	GLY	0	0.036	0.015	34.957	0.116	0.116	0.000	0.000	0.000	0.000
55	A	56	ILE	0	-0.035	-0.025	30.677	-0.162	-0.162	0.000	0.000	0.000	0.000
56	A	57	LEU	0	-0.022	-0.013	27.565	-0.005	-0.005	0.000	0.000	0.000	0.000
57	A	58	GLU	-1	-0.853	-0.923	26.658	-11.229	-11.229	0.000	0.000	0.000	0.000
58	A	59	THR	0	-0.014	-0.008	22.077	-0.198	-0.198	0.000	0.000	0.000	0.000
59	A	60	GLU	-1	-0.793	-0.890	17.886	-15.302	-15.302	0.000	0.000	0.000	0.000
60	A	61	ALA	0	-0.029	-0.008	18.285	-0.023	-0.023	0.000	0.000	0.000	0.000
61	A	62	ALA	0	-0.045	-0.024	12.978	-0.833	-0.833	0.000	0.000	0.000	0.000
62	A	63	ILE	0	-0.011	0.000	11.603	1.355	1.355	0.000	0.000	0.000	0.000
63	A	64	HIS	0	-0.013	0.012	9.267	-1.517	-1.517	0.000	0.000	0.000	0.000
65	A	66	SER	0	-0.049	-0.041	6.519	-2.967	-2.967	0.000	0.000	0.000	0.000
66	A	67	ASN	0	-0.029	-0.007	8.241	0.499	0.499	0.000	0.000	0.000	0.000
67	A	68	VAL	0	-0.004	-0.003	6.971	2.419	2.419	0.000	0.000	0.000	0.000
68	A	69	GLN	0	-0.048	-0.020	5.521	-7.095	-7.095	0.000	0.000	0.000	0.000
70	A	71	LEU	0	0.019	0.009	7.230	1.689	1.689	0.000	0.000	0.000	0.000
71	A	72	ASP	-1	-0.806	-0.866	10.643	-21.997	-21.997	0.000	0.000	0.000	0.000
72	A	73	PRO	0	-0.005	-0.003	11.596	1.438	1.438	0.000	0.000	0.000	0.000
73	A	74	LYS	1	0.925	0.968	14.531	16.610	16.610	0.000	0.000	0.000	0.000
74	A	75	THR	0	-0.031	-0.043	16.180	1.450	1.450	0.000	0.000	0.000	0.000
75	A	76	ASN	0	-0.012	-0.002	15.088	-0.122	-0.122	0.000	0.000	0.000	0.000
76	A	77	GLU	-1	-0.821	-0.878	14.726	-18.262	-18.262	0.000	0.000	0.000	0.000
77	A	78	PRO	0	-0.026	-0.016	10.704	-1.328	-1.328	0.000	0.000	0.000	0.000
78	A	79	THR	0	-0.046	-0.046	8.358	2.184	2.184	0.000	0.000	0.000	0.000
79	A	80	ARG	1	0.976	0.987	5.957	24.588	24.588	0.000	0.000	0.000	0.000
83	A	84	LYS	1	0.975	0.997	8.398	20.912	20.912	0.000	0.000	0.000	0.000
84	A	85	PHE	0	0.003	-0.001	11.005	-1.342	-1.342	0.000	0.000	0.000	0.000
85	A	86	VAL	0	0.012	-0.007	13.791	0.772	0.772	0.000	0.000	0.000	0.000
86	A	87	ASP	-1	-0.850	-0.916	15.375	-15.700	-15.700	0.000	0.000	0.000	0.000
87	A	88	GLY	0	-0.008	0.001	16.210	0.102	0.102	0.000	0.000	0.000	0.000
88	A	89	LYS	1	0.940	0.977	12.046	17.063	17.063	0.000	0.000	0.000	0.000
89	A	90	LYS	1	0.904	0.959	5.453	35.250	35.250	0.000	0.000	0.000	0.000
90	A	91	VAL	0	-0.037	-0.009	8.338	-2.078	-2.078	0.000	0.000	0.000	0.000
92	A	93	ILE	0	0.014	0.014	8.143	2.312	2.312	0.000	0.000	0.000	0.000
93	A	94	ALA	0	0.106	0.041	7.800	-4.458	-4.458	0.000	0.000	0.000	0.000
94	A	95	LYS	1	0.870	0.950	8.219	27.456	27.456	0.000	0.000	0.000	0.000
95	A	96	LYS	1	0.829	0.902	10.804	23.239	23.239	0.000	0.000	0.000	0.000
96	A	97	SER	0	-0.034	-0.045	12.895	1.426	1.426	0.000	0.000	0.000	0.000
97	A	98	GLY	0	0.008	0.006	13.095	-0.963	-0.963	0.000	0.000	0.000	0.000
98	A	99	GLU	-1	-0.813	-0.908	11.162	-28.795	-28.795	0.000	0.000	0.000	0.000
99	A	100	GLU	-1	-0.803	-0.903	6.006	-45.188	-45.188	0.000	0.000	0.000	0.000
100	A	101	ILE	0	-0.008	-0.010	10.648	-1.500	-1.500	0.000	0.000	0.000	0.000
101	A	102	LYS	1	0.821	0.899	10.645	22.231	22.231	0.000	0.000	0.000	0.000
102	A	103	SER	0	-0.055	-0.019	10.254	-2.091	-2.091	0.000	0.000	0.000	0.000
103	A	104	ASN	-1	-0.773	-0.879	12.033	-22.460	-22.460	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:HIS)