FMO DATABASE

FMODB ID: 3GZRL

Calculation Name: 6N1D-A-Xray547

Preferred Name:

Target Type:

Ligand 3-letter code: QUO | MIA | CM0 | G7M | 6MZ | PSU | 5MU | 4SU | SF4 | MG

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 6N1D

Chain ID: A

ChEMBL ID:

UniProt ID: P60493

Base Structure: X-ray

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	117
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-802313.183515
FMO2-HF: Nuclear repulsion	755926.77036
FMO2-HF: Total energy	-46386.413155
FMO2-MP2: Total energy	-46525.67862

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:PRO)

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

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.
242.442	243.748	-0.017	-0.553	-0.735	0.001

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.954 / q_NPA : 0.959

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	4	ALA	0	0.072	0.041	3.865	4.617	5.923	-0.017	-0.553	-0.735	0.001
4	A	5	LYS	1	0.961	0.983	6.732	28.005	28.005	0.000	0.000	0.000	0.000
5	A	6	THR	0	0.012	0.003	9.819	1.217	1.217	0.000	0.000	0.000	0.000
6	A	7	GLY	0	0.055	0.022	13.171	0.311	0.311	0.000	0.000	0.000	0.000
7	A	8	VAL	0	0.015	0.000	14.629	1.309	1.309	0.000	0.000	0.000	0.000
8	A	9	VAL	0	0.042	0.020	13.683	1.449	1.449	0.000	0.000	0.000	0.000
9	A	10	ARG	1	0.976	0.976	16.162	18.119	18.119	0.000	0.000	0.000	0.000
10	A	11	ARG	1	1.037	1.021	18.854	15.671	15.671	0.000	0.000	0.000	0.000
11	A	12	ARG	1	1.013	0.995	18.538	15.673	15.673	0.000	0.000	0.000	0.000
12	A	13	LYS	1	0.958	0.986	18.136	16.145	16.145	0.000	0.000	0.000	0.000
13	A	14	HIS	0	-0.003	-0.003	22.977	0.666	0.666	0.000	0.000	0.000	0.000
14	A	15	LYS	1	0.966	0.975	25.398	11.869	11.869	0.000	0.000	0.000	0.000
15	A	16	LYS	1	0.987	0.996	24.395	12.374	12.374	0.000	0.000	0.000	0.000
16	A	17	ILE	0	0.002	0.008	27.516	0.312	0.312	0.000	0.000	0.000	0.000
17	A	18	LEU	0	0.029	0.013	29.765	0.297	0.297	0.000	0.000	0.000	0.000
18	A	19	LYS	1	0.919	0.958	30.779	9.463	9.463	0.000	0.000	0.000	0.000
19	A	20	LEU	0	0.027	0.011	31.411	0.222	0.222	0.000	0.000	0.000	0.000
20	A	21	ALA	0	-0.043	0.001	33.997	0.277	0.277	0.000	0.000	0.000	0.000
21	A	22	LYS	1	0.909	0.948	35.285	8.693	8.693	0.000	0.000	0.000	0.000
22	A	23	GLY	0	0.097	0.047	38.424	0.124	0.124	0.000	0.000	0.000	0.000
23	A	24	TYR	0	-0.022	-0.005	37.155	0.161	0.161	0.000	0.000	0.000	0.000
24	A	25	TRP	0	0.119	0.071	40.988	-0.184	-0.184	0.000	0.000	0.000	0.000
25	A	26	GLY	0	0.081	0.046	41.260	-0.150	-0.150	0.000	0.000	0.000	0.000
26	A	27	LEU	0	0.049	0.002	36.561	-0.179	-0.179	0.000	0.000	0.000	0.000
27	A	28	ARG	1	0.926	0.975	36.310	7.485	7.485	0.000	0.000	0.000	0.000
28	A	29	SER	0	0.002	-0.018	36.525	-0.168	-0.168	0.000	0.000	0.000	0.000
29	A	30	LYS	1	0.895	0.946	33.789	8.011	8.011	0.000	0.000	0.000	0.000
30	A	31	SER	0	-0.010	0.003	32.277	-0.297	-0.297	0.000	0.000	0.000	0.000
31	A	32	PHE	0	0.024	-0.005	25.587	0.080	0.080	0.000	0.000	0.000	0.000
32	A	33	ARG	1	0.993	0.980	26.814	11.218	11.218	0.000	0.000	0.000	0.000
33	A	34	LYS	1	0.894	0.958	30.845	8.893	8.893	0.000	0.000	0.000	0.000
34	A	35	ALA	0	0.047	0.028	32.346	0.205	0.205	0.000	0.000	0.000	0.000
35	A	36	ARG	1	0.862	0.926	25.814	11.266	11.266	0.000	0.000	0.000	0.000
36	A	37	GLU	-1	-0.786	-0.875	31.766	-8.820	-8.820	0.000	0.000	0.000	0.000
37	A	38	THR	0	0.014	0.004	34.733	0.242	0.242	0.000	0.000	0.000	0.000
38	A	39	LEU	0	-0.013	-0.006	32.202	0.184	0.184	0.000	0.000	0.000	0.000
39	A	40	PHE	0	0.026	0.022	30.110	-0.047	-0.047	0.000	0.000	0.000	0.000
40	A	41	ALA	0	0.027	0.027	35.676	0.158	0.158	0.000	0.000	0.000	0.000
41	A	42	ALA	0	0.032	0.018	38.210	0.179	0.179	0.000	0.000	0.000	0.000
42	A	43	GLY	0	0.013	0.008	37.235	0.164	0.164	0.000	0.000	0.000	0.000
43	A	44	ASN	0	0.025	0.007	37.844	0.076	0.076	0.000	0.000	0.000	0.000
44	A	45	TYR	0	0.046	0.015	40.463	0.176	0.176	0.000	0.000	0.000	0.000
45	A	46	ALA	0	0.059	0.034	41.005	0.205	0.205	0.000	0.000	0.000	0.000
46	A	47	TYR	0	-0.017	0.005	40.871	0.175	0.175	0.000	0.000	0.000	0.000
47	A	48	ALA	0	0.053	0.025	42.897	0.160	0.160	0.000	0.000	0.000	0.000
48	A	49	HIS	0	0.009	-0.017	46.006	0.294	0.294	0.000	0.000	0.000	0.000
49	A	50	ARG	1	0.883	0.940	39.789	7.671	7.671	0.000	0.000	0.000	0.000
50	A	51	LYS	1	0.909	0.966	45.066	7.002	7.002	0.000	0.000	0.000	0.000
51	A	52	ARG	1	0.936	0.970	48.791	6.070	6.070	0.000	0.000	0.000	0.000
52	A	53	ARG	1	1.019	1.002	47.343	6.574	6.574	0.000	0.000	0.000	0.000
53	A	54	LYS	1	0.914	0.960	49.801	6.357	6.357	0.000	0.000	0.000	0.000
54	A	55	ARG	1	0.954	0.969	51.522	6.068	6.068	0.000	0.000	0.000	0.000
55	A	56	ASP	-1	-0.862	-0.926	54.356	-5.693	-5.693	0.000	0.000	0.000	0.000
56	A	57	PHE	0	0.027	0.003	56.951	0.093	0.093	0.000	0.000	0.000	0.000
57	A	58	ARG	1	0.946	0.970	56.001	5.624	5.624	0.000	0.000	0.000	0.000
58	A	59	ARG	1	0.963	0.987	59.254	5.370	5.370	0.000	0.000	0.000	0.000
59	A	60	LEU	0	0.029	0.024	61.243	0.085	0.085	0.000	0.000	0.000	0.000
60	A	61	TRP	0	0.006	-0.004	58.125	0.023	0.023	0.000	0.000	0.000	0.000
61	A	62	ILE	0	0.010	0.018	64.360	0.063	0.063	0.000	0.000	0.000	0.000
62	A	63	VAL	0	-0.010	-0.009	66.322	0.078	0.078	0.000	0.000	0.000	0.000
63	A	64	ARG	1	0.962	0.981	64.726	4.898	4.898	0.000	0.000	0.000	0.000
64	A	65	ILE	0	0.047	0.033	67.428	0.052	0.052	0.000	0.000	0.000	0.000
65	A	66	ASN	0	0.009	0.005	70.753	0.121	0.121	0.000	0.000	0.000	0.000
66	A	67	ALA	0	-0.011	0.002	72.156	0.058	0.058	0.000	0.000	0.000	0.000
67	A	68	ALA	0	0.046	0.027	73.401	0.059	0.059	0.000	0.000	0.000	0.000
68	A	69	CYS	0	-0.054	-0.019	75.022	0.036	0.036	0.000	0.000	0.000	0.000
69	A	70	ARG	1	0.884	0.917	74.687	4.274	4.274	0.000	0.000	0.000	0.000
70	A	71	GLN	0	-0.028	-0.002	77.887	0.006	0.006	0.000	0.000	0.000	0.000
71	A	72	HIS	0	0.061	0.028	79.570	0.008	0.008	0.000	0.000	0.000	0.000
72	A	73	GLY	0	0.004	0.029	81.384	0.050	0.050	0.000	0.000	0.000	0.000
73	A	74	LEU	0	-0.034	-0.012	78.703	0.025	0.025	0.000	0.000	0.000	0.000
74	A	75	ASN	0	0.028	0.022	76.884	-0.108	-0.108	0.000	0.000	0.000	0.000
75	A	76	TYR	0	0.119	0.026	67.760	-0.038	-0.038	0.000	0.000	0.000	0.000
76	A	77	SER	0	-0.089	-0.047	73.522	-0.022	-0.022	0.000	0.000	0.000	0.000
77	A	78	THR	0	0.074	0.030	74.494	-0.018	-0.018	0.000	0.000	0.000	0.000
78	A	79	PHE	0	0.083	0.044	71.956	0.002	0.002	0.000	0.000	0.000	0.000
79	A	80	ILE	0	-0.043	-0.029	69.775	-0.031	-0.031	0.000	0.000	0.000	0.000
80	A	81	HIS	0	0.010	0.005	73.155	-0.070	-0.070	0.000	0.000	0.000	0.000
81	A	82	GLY	0	0.088	0.050	75.321	0.010	0.010	0.000	0.000	0.000	0.000
82	A	83	LEU	0	0.002	0.002	71.969	0.000	0.000	0.000	0.000	0.000	0.000
83	A	84	LYS	1	0.845	0.918	67.636	4.614	4.614	0.000	0.000	0.000	0.000
84	A	85	LYS	1	0.933	0.978	73.375	4.056	4.056	0.000	0.000	0.000	0.000
85	A	86	ALA	0	0.019	0.015	76.315	0.032	0.032	0.000	0.000	0.000	0.000
86	A	87	GLY	0	-0.005	0.012	73.450	-0.006	-0.006	0.000	0.000	0.000	0.000
87	A	88	ILE	0	-0.012	-0.008	71.484	-0.052	-0.052	0.000	0.000	0.000	0.000
88	A	89	GLU	-1	-0.979	-1.002	65.848	-4.854	-4.854	0.000	0.000	0.000	0.000
89	A	90	VAL	0	0.011	0.007	66.128	-0.083	-0.083	0.000	0.000	0.000	0.000
90	A	91	ASP	-1	-0.877	-0.918	66.181	-4.700	-4.700	0.000	0.000	0.000	0.000
91	A	92	ARG	1	0.847	0.904	57.931	5.224	5.224	0.000	0.000	0.000	0.000
92	A	93	LYS	1	0.941	0.947	63.480	4.799	4.799	0.000	0.000	0.000	0.000
93	A	94	ASN	0	-0.062	-0.034	60.863	0.042	0.042	0.000	0.000	0.000	0.000
94	A	95	LEU	0	0.039	0.009	62.853	-0.011	-0.011	0.000	0.000	0.000	0.000
95	A	96	ALA	0	0.083	0.059	65.821	0.056	0.056	0.000	0.000	0.000	0.000
96	A	97	ASP	-1	-0.956	-0.973	65.284	-4.812	-4.812	0.000	0.000	0.000	0.000
97	A	98	LEU	0	0.031	0.010	68.215	0.005	0.005	0.000	0.000	0.000	0.000
98	A	99	ALA	0	-0.001	0.008	71.189	0.059	0.059	0.000	0.000	0.000	0.000
99	A	100	VAL	0	-0.059	-0.037	70.159	0.042	0.042	0.000	0.000	0.000	0.000
100	A	101	ARG	1	0.808	0.892	63.954	4.777	4.777	0.000	0.000	0.000	0.000
101	A	102	GLU	-1	-0.825	-0.909	71.581	-4.239	-4.239	0.000	0.000	0.000	0.000
102	A	103	PRO	0	0.028	0.032	75.190	-0.006	-0.006	0.000	0.000	0.000	0.000
103	A	104	GLN	0	0.038	0.006	76.668	0.003	0.003	0.000	0.000	0.000	0.000
104	A	105	VAL	0	0.000	0.006	73.585	0.016	0.016	0.000	0.000	0.000	0.000
105	A	106	PHE	0	-0.018	-0.024	72.281	-0.046	-0.046	0.000	0.000	0.000	0.000
106	A	107	ALA	0	0.023	0.004	75.624	0.010	0.010	0.000	0.000	0.000	0.000
107	A	108	GLU	-1	-0.897	-0.949	79.305	-3.830	-3.830	0.000	0.000	0.000	0.000
108	A	109	LEU	0	-0.085	-0.045	73.302	-0.010	-0.010	0.000	0.000	0.000	0.000
109	A	110	VAL	0	-0.051	-0.025	77.544	-0.014	-0.014	0.000	0.000	0.000	0.000
110	A	111	GLU	-1	-0.865	-0.933	79.372	-3.785	-3.785	0.000	0.000	0.000	0.000
111	A	112	ARG	1	0.922	0.960	78.936	4.010	4.010	0.000	0.000	0.000	0.000
112	A	113	ALA	0	-0.090	-0.031	77.829	-0.019	-0.019	0.000	0.000	0.000	0.000
113	A	114	LYS	1	0.947	0.957	79.390	3.797	3.797	0.000	0.000	0.000	0.000
114	A	115	ALA	0	0.040	0.043	82.883	0.033	0.033	0.000	0.000	0.000	0.000
115	A	116	ALA	0	-0.004	-0.004	80.681	0.028	0.028	0.000	0.000	0.000	0.000
116	A	117	GLN	0	-0.147	-0.105	79.188	-0.047	-0.047	0.000	0.000	0.000	0.000
117	A	118	GLY	-1	-0.896	-0.908	83.468	-3.644	-3.644	0.000	0.000	0.000	0.000

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