FMO DATABASE

FMODB ID: 3ZYYL

Calculation Name: 7C9P-D-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 7C9P

Chain ID: D

ChEMBL ID:

UniProt ID:

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	84
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-521345.102987
FMO2-HF: Nuclear repulsion	487379.440338
FMO2-HF: Total energy	-33965.662649
FMO2-MP2: Total energy	-34064.849298

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:64:ASP)

Summations of interaction energy for fragment #1(A:64:ASP)

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.
-57.425	-53.764	14.501	-8.815	-9.346	0.088

Interaction energy analysis for fragmet #1(A:64:ASP)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.003 / q_NPA : -0.017

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	66	LYS	1	0.954	0.991	2.072	-28.354	-24.283	5.227	-4.554	-4.744	0.032
4	A	67	ASN	0	0.000	-0.003	1.839	-18.421	-18.948	9.269	-4.188	-4.553	0.056
5	A	68	HIS	0	0.019	-0.004	4.215	-4.364	-4.247	0.005	-0.073	-0.049	0.000
6	A	69	GLN	0	-0.011	0.020	6.470	-1.104	-1.104	0.000	0.000	0.000	0.000
7	A	70	LEU	0	0.053	0.017	8.306	-1.499	-1.499	0.000	0.000	0.000	0.000
8	A	71	PRO	0	-0.008	0.008	10.126	0.729	0.729	0.000	0.000	0.000	0.000
9	A	72	LEU	0	0.083	0.029	8.227	-0.806	-0.806	0.000	0.000	0.000	0.000
10	A	73	ALA	0	-0.009	-0.012	12.501	-0.518	-0.518	0.000	0.000	0.000	0.000
11	A	74	ARG	1	0.939	0.966	15.634	-1.587	-1.587	0.000	0.000	0.000	0.000
12	A	75	ILE	0	0.078	0.048	12.822	-0.191	-0.191	0.000	0.000	0.000	0.000
13	A	76	LYS	1	0.973	0.986	15.352	-1.883	-1.883	0.000	0.000	0.000	0.000
14	A	77	LYS	1	0.909	0.956	18.575	-1.032	-1.032	0.000	0.000	0.000	0.000
15	A	78	ILE	0	-0.003	0.004	19.001	-0.060	-0.060	0.000	0.000	0.000	0.000
16	A	79	MET	0	0.011	0.003	18.646	-0.048	-0.048	0.000	0.000	0.000	0.000
17	A	80	LYS	1	0.871	0.932	22.041	-0.682	-0.682	0.000	0.000	0.000	0.000
18	A	81	ALA	0	-0.024	0.001	24.619	0.013	0.013	0.000	0.000	0.000	0.000
19	A	82	ASP	-1	-0.871	-0.926	26.261	-0.023	-0.023	0.000	0.000	0.000	0.000
20	A	83	GLU	-1	-0.937	-0.974	28.013	0.176	0.176	0.000	0.000	0.000	0.000
21	A	84	ASP	-1	-0.898	-0.932	29.986	0.011	0.011	0.000	0.000	0.000	0.000
22	A	85	VAL	0	-0.122	-0.050	23.515	0.004	0.004	0.000	0.000	0.000	0.000
23	A	86	ARG	1	0.969	0.987	26.136	-0.057	-0.057	0.000	0.000	0.000	0.000
24	A	87	MET	0	-0.070	-0.051	23.257	0.145	0.145	0.000	0.000	0.000	0.000
25	A	88	ILE	0	0.001	-0.007	17.661	-0.065	-0.065	0.000	0.000	0.000	0.000
26	A	89	SER	0	0.034	0.027	16.747	0.272	0.272	0.000	0.000	0.000	0.000
27	A	90	ALA	0	-0.002	-0.020	13.802	0.104	0.104	0.000	0.000	0.000	0.000
28	A	91	GLU	-1	-0.886	-0.944	11.792	-0.491	-0.491	0.000	0.000	0.000	0.000
29	A	92	ALA	0	0.019	0.018	12.141	-0.306	-0.306	0.000	0.000	0.000	0.000
30	A	93	PRO	0	-0.014	-0.025	12.547	-0.179	-0.179	0.000	0.000	0.000	0.000
31	A	94	VAL	0	0.003	0.013	7.186	0.270	0.270	0.000	0.000	0.000	0.000
32	A	95	LEU	0	0.030	0.018	9.504	-0.797	-0.797	0.000	0.000	0.000	0.000
33	A	96	PHE	0	0.022	0.000	11.078	-0.223	-0.223	0.000	0.000	0.000	0.000
34	A	97	ALA	0	0.031	0.009	9.817	0.016	0.016	0.000	0.000	0.000	0.000
35	A	98	LYS	1	0.853	0.919	6.183	7.073	7.073	0.000	0.000	0.000	0.000
36	A	99	ALA	0	0.026	0.008	9.896	-0.174	-0.174	0.000	0.000	0.000	0.000
37	A	100	CYS	0	-0.044	-0.026	13.477	0.168	0.168	0.000	0.000	0.000	0.000
38	A	101	GLU	-1	-0.860	-0.918	8.499	-3.548	-3.548	0.000	0.000	0.000	0.000
39	A	102	LEU	0	-0.002	-0.007	11.272	-0.016	-0.016	0.000	0.000	0.000	0.000
40	A	103	PHE	0	0.021	0.024	13.996	0.147	0.147	0.000	0.000	0.000	0.000
41	A	104	ILE	0	0.012	0.005	15.509	0.129	0.129	0.000	0.000	0.000	0.000
42	A	105	LEU	0	-0.027	0.002	12.613	0.087	0.087	0.000	0.000	0.000	0.000
43	A	106	GLU	-1	-0.828	-0.891	17.081	-1.152	-1.152	0.000	0.000	0.000	0.000
44	A	107	LEU	0	0.018	0.010	19.633	0.097	0.097	0.000	0.000	0.000	0.000
45	A	108	THR	0	-0.031	-0.018	19.760	0.145	0.145	0.000	0.000	0.000	0.000
46	A	109	ILE	0	-0.016	-0.011	20.739	0.073	0.073	0.000	0.000	0.000	0.000
47	A	110	ARG	1	0.843	0.900	22.720	0.976	0.976	0.000	0.000	0.000	0.000
48	A	111	SER	0	-0.020	-0.018	25.073	0.077	0.077	0.000	0.000	0.000	0.000
49	A	112	TRP	0	-0.090	-0.065	24.821	0.086	0.086	0.000	0.000	0.000	0.000
50	A	113	LEU	0	0.022	0.019	26.344	0.033	0.033	0.000	0.000	0.000	0.000
51	A	114	HIS	0	-0.001	-0.008	28.905	0.033	0.033	0.000	0.000	0.000	0.000
52	A	115	ALA	0	-0.007	0.007	29.481	0.040	0.040	0.000	0.000	0.000	0.000
53	A	116	GLU	-1	-0.857	-0.930	28.753	-0.463	-0.463	0.000	0.000	0.000	0.000
54	A	117	GLU	-1	-0.834	-0.876	32.176	-0.393	-0.393	0.000	0.000	0.000	0.000
55	A	118	ASN	0	-0.109	-0.057	34.629	0.042	0.042	0.000	0.000	0.000	0.000
56	A	119	LYS	1	0.889	0.944	35.472	0.280	0.280	0.000	0.000	0.000	0.000
57	A	120	ARG	1	0.787	0.868	31.964	0.159	0.159	0.000	0.000	0.000	0.000
58	A	121	ARG	1	0.924	0.962	27.819	0.279	0.279	0.000	0.000	0.000	0.000
59	A	122	THR	0	0.010	0.003	29.246	0.028	0.028	0.000	0.000	0.000	0.000
60	A	123	LEU	0	0.020	0.021	25.347	-0.033	-0.033	0.000	0.000	0.000	0.000
61	A	124	GLN	0	-0.003	-0.017	28.489	0.071	0.071	0.000	0.000	0.000	0.000
62	A	125	ARG	1	0.922	0.951	29.890	-0.036	-0.036	0.000	0.000	0.000	0.000
63	A	126	ASN	0	0.033	0.012	30.906	0.003	0.003	0.000	0.000	0.000	0.000
64	A	127	ASP	-1	-0.711	-0.800	29.378	-0.193	-0.193	0.000	0.000	0.000	0.000
65	A	128	VAL	0	0.024	0.013	26.100	-0.047	-0.047	0.000	0.000	0.000	0.000
66	A	129	ALA	0	0.049	0.021	28.438	-0.040	-0.040	0.000	0.000	0.000	0.000
67	A	130	ALA	0	-0.066	-0.023	31.677	-0.022	-0.022	0.000	0.000	0.000	0.000
68	A	131	ALA	0	-0.005	-0.004	26.530	-0.040	-0.040	0.000	0.000	0.000	0.000
69	A	132	ILE	0	-0.032	-0.010	27.166	-0.065	-0.065	0.000	0.000	0.000	0.000
70	A	133	ALA	0	0.003	0.004	29.145	-0.030	-0.030	0.000	0.000	0.000	0.000
71	A	134	ARG	1	0.745	0.844	30.742	0.438	0.438	0.000	0.000	0.000	0.000
72	A	135	THR	0	-0.032	-0.026	25.671	-0.077	-0.077	0.000	0.000	0.000	0.000
73	A	136	ASP	-1	-0.817	-0.899	28.710	-0.578	-0.578	0.000	0.000	0.000	0.000
74	A	137	VAL	0	-0.046	-0.025	23.308	0.023	0.023	0.000	0.000	0.000	0.000
75	A	138	PHE	0	-0.044	-0.048	22.026	-0.004	-0.004	0.000	0.000	0.000	0.000
76	A	139	ASP	-1	-0.851	-0.916	26.895	-0.302	-0.302	0.000	0.000	0.000	0.000
77	A	140	PHE	0	-0.032	-0.019	23.523	0.055	0.055	0.000	0.000	0.000	0.000
78	A	141	LEU	0	-0.035	-0.025	24.670	0.061	0.061	0.000	0.000	0.000	0.000
79	A	142	VAL	0	0.019	0.014	29.342	0.043	0.043	0.000	0.000	0.000	0.000
80	A	143	ASP	-1	-0.898	-0.957	32.784	-0.098	-0.098	0.000	0.000	0.000	0.000
81	A	144	ILE	0	-0.098	-0.035	28.625	0.046	0.046	0.000	0.000	0.000	0.000
82	A	145	VAL	0	-0.119	-0.068	28.490	0.051	0.051	0.000	0.000	0.000	0.000
83	A	146	PRO	0	0.066	0.050	31.937	-0.031	-0.031	0.000	0.000	0.000	0.000
84	A	147	ARG	0	0.026	0.013	35.060	0.124	0.124	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:64:ASP)