FMO DATABASE

FMODB ID: ZLLGN

Calculation Name: 4B9C-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 4B9C

Chain ID: A

ChEMBL ID:

UniProt ID: A3DBH1

Base Structure: X-ray

Registration Date: 2025-10-04

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	150
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1601039.879272
FMO2-HF: Nuclear repulsion	1538340.613855
FMO2-HF: Total energy	-62699.265417
FMO2-MP2: Total energy	-62881.532395

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:1:GLY)

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

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.
-71.764	-69.583	4.076	-3.338	-2.918	-0.033

Interaction energy analysis for fragmet #1(A:1:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.786 / q_NPA : 0.879

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	3	HIS	0	0.040	0.024	3.788	7.767	9.771	-0.027	-0.884	-1.093	-0.006
32	A	32	ASN	0	-0.052	-0.050	2.401	-13.847	-13.827	4.103	-2.381	-1.741	-0.027
33	A	33	GLU	-1	-0.848	-0.926	4.127	-53.060	-52.903	0.000	-0.073	-0.084	0.000
4	A	4	MET	0	0.053	0.052	5.667	-0.692	-0.692	0.000	0.000	0.000	0.000
5	A	5	GLY	0	0.029	0.013	8.509	0.824	0.824	0.000	0.000	0.000	0.000
6	A	6	LEU	0	0.024	0.008	10.746	0.329	0.329	0.000	0.000	0.000	0.000
7	A	7	LYS	1	0.848	0.907	14.181	16.830	16.830	0.000	0.000	0.000	0.000
8	A	8	ILE	0	0.022	0.022	16.778	0.142	0.142	0.000	0.000	0.000	0.000
9	A	9	GLN	0	-0.015	-0.021	20.517	0.317	0.317	0.000	0.000	0.000	0.000
10	A	10	TYR	0	0.022	-0.008	23.007	0.018	0.018	0.000	0.000	0.000	0.000
11	A	11	TYR	0	-0.011	0.007	26.658	0.090	0.090	0.000	0.000	0.000	0.000
12	A	12	SER	0	0.031	0.032	30.291	0.085	0.085	0.000	0.000	0.000	0.000
13	A	13	ARG	1	0.974	0.976	33.678	8.678	8.678	0.000	0.000	0.000	0.000
14	A	14	LYS	1	0.827	0.928	36.697	8.332	8.332	0.000	0.000	0.000	0.000
15	A	15	PRO	0	-0.003	0.002	38.973	-0.076	-0.076	0.000	0.000	0.000	0.000
16	A	16	HIS	1	0.776	0.841	40.526	7.145	7.145	0.000	0.000	0.000	0.000
17	A	17	ASP	-1	-0.812	-0.874	41.586	-6.922	-6.922	0.000	0.000	0.000	0.000
18	A	18	SER	0	-0.018	-0.033	40.477	0.186	0.186	0.000	0.000	0.000	0.000
19	A	19	ALA	0	0.045	0.014	43.009	0.027	0.027	0.000	0.000	0.000	0.000
20	A	20	GLY	0	0.035	0.017	40.292	0.004	0.004	0.000	0.000	0.000	0.000
21	A	21	ILE	0	-0.030	0.020	34.581	-0.005	-0.005	0.000	0.000	0.000	0.000
22	A	22	ASP	-1	-0.863	-0.915	33.066	-9.501	-9.501	0.000	0.000	0.000	0.000
23	A	23	PHE	0	-0.008	-0.014	29.096	-0.150	-0.150	0.000	0.000	0.000	0.000
24	A	24	SER	0	-0.012	-0.028	28.881	-0.410	-0.410	0.000	0.000	0.000	0.000
25	A	25	PHE	0	-0.033	-0.013	21.930	-0.100	-0.100	0.000	0.000	0.000	0.000
26	A	26	ARG	1	0.838	0.925	21.816	13.148	13.148	0.000	0.000	0.000	0.000
27	A	27	MET	0	-0.022	-0.016	17.434	-0.039	-0.039	0.000	0.000	0.000	0.000
28	A	28	PHE	0	-0.010	0.003	14.876	0.191	0.191	0.000	0.000	0.000	0.000
29	A	29	ASN	0	-0.012	-0.019	9.850	-1.199	-1.199	0.000	0.000	0.000	0.000
30	A	30	THR	0	-0.048	-0.041	10.689	-0.259	-0.259	0.000	0.000	0.000	0.000
31	A	31	GLY	0	0.005	0.018	7.025	-1.217	-1.217	0.000	0.000	0.000	0.000
34	A	34	ALA	0	-0.013	-0.009	6.493	3.112	3.112	0.000	0.000	0.000	0.000
35	A	35	ILE	0	-0.031	-0.009	10.110	-0.234	-0.234	0.000	0.000	0.000	0.000
36	A	36	ASP	-1	-0.791	-0.887	13.090	-15.024	-15.024	0.000	0.000	0.000	0.000
37	A	37	LEU	0	0.017	-0.012	16.544	-0.153	-0.153	0.000	0.000	0.000	0.000
38	A	38	LYS	1	0.813	0.917	19.181	15.479	15.479	0.000	0.000	0.000	0.000
39	A	39	ASP	-1	-0.915	-0.940	17.114	-16.845	-16.845	0.000	0.000	0.000	0.000
40	A	40	VAL	0	-0.070	-0.036	16.554	-0.417	-0.417	0.000	0.000	0.000	0.000
41	A	41	LYS	1	0.839	0.934	19.209	13.628	13.628	0.000	0.000	0.000	0.000
42	A	42	VAL	0	-0.011	-0.014	20.984	-0.696	-0.696	0.000	0.000	0.000	0.000
43	A	43	ARG	1	0.788	0.896	23.292	12.304	12.304	0.000	0.000	0.000	0.000
44	A	44	TYR	0	0.022	0.004	26.407	-0.323	-0.323	0.000	0.000	0.000	0.000
45	A	45	TYR	0	0.020	-0.012	25.990	0.329	0.329	0.000	0.000	0.000	0.000
46	A	46	PHE	0	-0.025	-0.026	31.501	-0.028	-0.028	0.000	0.000	0.000	0.000
47	A	47	LYS	1	0.907	0.949	35.205	7.410	7.410	0.000	0.000	0.000	0.000
48	A	48	GLU	-1	-0.769	-0.895	38.821	-7.169	-7.169	0.000	0.000	0.000	0.000
49	A	49	ASP	-1	-0.926	-0.953	41.512	-7.176	-7.176	0.000	0.000	0.000	0.000
50	A	50	VAL	0	-0.024	0.012	42.878	0.095	0.095	0.000	0.000	0.000	0.000
51	A	51	SER	0	-0.025	-0.044	42.765	-0.228	-0.228	0.000	0.000	0.000	0.000
52	A	52	ILE	0	-0.028	-0.035	37.430	-0.063	-0.063	0.000	0.000	0.000	0.000
53	A	53	ASP	-1	-0.926	-0.953	40.092	-7.799	-7.799	0.000	0.000	0.000	0.000
54	A	54	GLU	-1	-0.894	-0.917	42.442	-6.667	-6.667	0.000	0.000	0.000	0.000
55	A	55	MET	0	-0.049	-0.008	38.931	0.014	0.014	0.000	0.000	0.000	0.000
56	A	56	ASN	0	-0.044	-0.028	39.696	-0.123	-0.123	0.000	0.000	0.000	0.000
57	A	57	TRP	0	0.046	0.006	32.975	-0.126	-0.126	0.000	0.000	0.000	0.000
58	A	58	ALA	0	-0.006	0.005	36.074	0.091	0.091	0.000	0.000	0.000	0.000
59	A	59	VAL	0	-0.002	-0.011	29.899	-0.178	-0.178	0.000	0.000	0.000	0.000
60	A	60	TYR	0	-0.040	-0.032	32.893	0.191	0.191	0.000	0.000	0.000	0.000
61	A	61	PHE	0	-0.016	-0.010	27.171	0.020	0.020	0.000	0.000	0.000	0.000
62	A	62	TYR	0	0.021	-0.028	22.556	-0.362	-0.362	0.000	0.000	0.000	0.000
63	A	63	SER	0	-0.009	0.001	22.463	0.085	0.085	0.000	0.000	0.000	0.000
64	A	64	LEU	0	-0.074	-0.023	19.433	-0.245	-0.245	0.000	0.000	0.000	0.000
65	A	65	GLY	0	0.014	0.012	23.343	-0.210	-0.210	0.000	0.000	0.000	0.000
66	A	66	SER	0	-0.037	-0.003	26.525	0.318	0.318	0.000	0.000	0.000	0.000
67	A	67	GLU	-1	-0.808	-0.926	29.174	-9.698	-9.698	0.000	0.000	0.000	0.000
68	A	68	LYS	1	0.913	0.956	31.191	8.685	8.685	0.000	0.000	0.000	0.000
69	A	69	ASP	-1	-0.858	-0.914	26.668	-11.178	-11.178	0.000	0.000	0.000	0.000
70	A	70	VAL	0	-0.012	0.001	26.476	-0.484	-0.484	0.000	0.000	0.000	0.000
71	A	71	GLN	0	-0.051	-0.034	28.127	0.620	0.620	0.000	0.000	0.000	0.000
72	A	72	CYS	0	-0.020	0.010	28.905	-0.512	-0.512	0.000	0.000	0.000	0.000
73	A	73	ARG	1	0.937	0.973	30.979	9.492	9.492	0.000	0.000	0.000	0.000
74	A	74	PHE	0	0.049	0.029	32.243	-0.302	-0.302	0.000	0.000	0.000	0.000
75	A	75	TYR	0	-0.038	-0.028	30.390	0.139	0.139	0.000	0.000	0.000	0.000
76	A	76	GLU	-1	-0.736	-0.864	34.843	-7.929	-7.929	0.000	0.000	0.000	0.000
77	A	77	LEU	0	-0.058	-0.031	31.879	-0.264	-0.264	0.000	0.000	0.000	0.000
78	A	78	PRO	0	0.014	0.005	35.251	0.166	0.166	0.000	0.000	0.000	0.000
79	A	79	GLY	0	-0.013	-0.018	36.131	-0.208	-0.208	0.000	0.000	0.000	0.000
80	A	80	LYS	1	0.866	0.950	31.552	9.606	9.606	0.000	0.000	0.000	0.000
81	A	81	LYS	1	0.972	0.969	36.204	8.680	8.680	0.000	0.000	0.000	0.000
82	A	82	GLU	-1	-0.898	-0.944	33.044	-8.969	-8.969	0.000	0.000	0.000	0.000
83	A	83	ALA	0	0.006	0.002	33.500	-0.056	-0.056	0.000	0.000	0.000	0.000
84	A	84	ASN	0	-0.025	-0.017	35.573	-0.085	-0.085	0.000	0.000	0.000	0.000
85	A	85	LYS	1	0.806	0.923	35.798	7.940	7.940	0.000	0.000	0.000	0.000
86	A	86	TYR	0	-0.030	-0.026	29.369	-0.256	-0.256	0.000	0.000	0.000	0.000
87	A	87	LEU	0	-0.004	0.023	30.890	0.206	0.206	0.000	0.000	0.000	0.000
88	A	88	GLU	-1	-0.821	-0.915	26.452	-12.065	-12.065	0.000	0.000	0.000	0.000
89	A	89	ILE	0	0.003	-0.005	25.566	0.343	0.343	0.000	0.000	0.000	0.000
90	A	90	THR	0	-0.037	-0.030	24.453	-0.572	-0.572	0.000	0.000	0.000	0.000
91	A	91	PHE	0	0.060	0.023	21.890	0.332	0.332	0.000	0.000	0.000	0.000
92	A	92	LYS	1	0.873	0.939	24.808	11.217	11.217	0.000	0.000	0.000	0.000
93	A	93	SER	0	-0.013	-0.014	23.393	-0.238	-0.238	0.000	0.000	0.000	0.000
94	A	94	GLY	0	0.089	0.061	21.001	0.009	0.009	0.000	0.000	0.000	0.000
95	A	95	THR	0	-0.032	-0.028	15.320	-0.676	-0.676	0.000	0.000	0.000	0.000
96	A	96	LEU	0	0.033	0.021	14.711	0.746	0.746	0.000	0.000	0.000	0.000
97	A	97	SER	0	0.028	0.020	11.174	-1.855	-1.855	0.000	0.000	0.000	0.000
98	A	98	PRO	0	-0.037	-0.025	6.860	1.083	1.083	0.000	0.000	0.000	0.000
99	A	99	ASN	0	-0.036	-0.021	9.669	0.462	0.462	0.000	0.000	0.000	0.000
100	A	100	ASP	-1	-0.838	-0.889	12.478	-18.161	-18.161	0.000	0.000	0.000	0.000
101	A	101	VAL	0	-0.068	-0.049	15.235	-0.254	-0.254	0.000	0.000	0.000	0.000
102	A	102	MET	0	-0.015	0.016	18.197	0.382	0.382	0.000	0.000	0.000	0.000
103	A	103	TYR	0	0.027	-0.014	20.654	0.181	0.181	0.000	0.000	0.000	0.000
104	A	104	ILE	0	0.018	0.013	24.237	0.039	0.039	0.000	0.000	0.000	0.000
105	A	105	THR	0	0.000	-0.016	27.115	0.031	0.031	0.000	0.000	0.000	0.000
106	A	106	GLY	0	0.047	0.021	30.696	0.026	0.026	0.000	0.000	0.000	0.000
107	A	107	GLU	-1	-0.823	-0.889	32.956	-8.153	-8.153	0.000	0.000	0.000	0.000
108	A	108	PHE	0	-0.031	-0.014	33.663	-0.046	-0.046	0.000	0.000	0.000	0.000
109	A	109	TYR	0	0.012	0.008	37.339	0.046	0.046	0.000	0.000	0.000	0.000
110	A	110	LYS	1	0.852	0.923	41.076	6.978	6.978	0.000	0.000	0.000	0.000
111	A	111	ASN	0	0.000	-0.006	43.804	0.006	0.006	0.000	0.000	0.000	0.000
112	A	112	ASP	-1	-0.837	-0.893	46.213	-6.525	-6.525	0.000	0.000	0.000	0.000
113	A	113	TRP	0	-0.077	-0.037	47.118	0.127	0.127	0.000	0.000	0.000	0.000
114	A	114	THR	0	-0.060	-0.042	47.659	-0.008	-0.008	0.000	0.000	0.000	0.000
115	A	115	LYS	1	0.824	0.894	45.239	6.638	6.638	0.000	0.000	0.000	0.000
116	A	116	PHE	0	0.037	0.035	40.208	0.065	0.065	0.000	0.000	0.000	0.000
117	A	117	GLU	-1	-0.748	-0.854	42.438	-7.256	-7.256	0.000	0.000	0.000	0.000
118	A	118	GLN	0	0.029	0.004	37.416	-0.301	-0.301	0.000	0.000	0.000	0.000
119	A	119	ARG	1	0.831	0.905	37.764	6.995	6.995	0.000	0.000	0.000	0.000
120	A	120	ASP	-1	-0.899	-0.944	38.803	-7.762	-7.762	0.000	0.000	0.000	0.000
121	A	121	ASP	-1	-0.802	-0.898	34.869	-8.635	-8.635	0.000	0.000	0.000	0.000
122	A	122	TYR	0	-0.071	-0.056	27.113	-0.063	-0.063	0.000	0.000	0.000	0.000
123	A	123	SER	0	-0.013	-0.032	28.757	-0.229	-0.229	0.000	0.000	0.000	0.000
124	A	124	TYR	0	0.018	0.016	30.450	-0.164	-0.164	0.000	0.000	0.000	0.000
125	A	125	ASN	0	-0.049	-0.027	28.819	0.194	0.194	0.000	0.000	0.000	0.000
126	A	126	PRO	0	-0.019	0.005	32.224	-0.035	-0.035	0.000	0.000	0.000	0.000
127	A	127	ALA	0	0.004	0.001	31.830	0.050	0.050	0.000	0.000	0.000	0.000
128	A	128	ASP	-1	-0.922	-0.977	33.728	-8.988	-8.988	0.000	0.000	0.000	0.000
129	A	129	SER	0	-0.015	-0.001	29.903	-0.155	-0.155	0.000	0.000	0.000	0.000
130	A	130	TYR	0	-0.026	-0.020	24.707	-0.107	-0.107	0.000	0.000	0.000	0.000
131	A	131	SER	0	0.023	0.014	24.639	-0.089	-0.089	0.000	0.000	0.000	0.000
132	A	132	ASP	-1	-0.816	-0.893	19.493	-15.518	-15.518	0.000	0.000	0.000	0.000
133	A	133	TRP	0	0.012	-0.003	22.327	0.112	0.112	0.000	0.000	0.000	0.000
134	A	134	LYS	1	0.917	0.958	18.901	14.930	14.930	0.000	0.000	0.000	0.000
135	A	135	ARG	1	0.925	0.980	23.493	9.896	9.896	0.000	0.000	0.000	0.000
136	A	136	MET	0	0.003	0.058	24.765	0.462	0.462	0.000	0.000	0.000	0.000
137	A	137	THR	0	-0.016	-0.018	21.965	-0.347	-0.347	0.000	0.000	0.000	0.000
138	A	138	ALA	0	0.017	0.001	18.048	0.281	0.281	0.000	0.000	0.000	0.000
139	A	139	TYR	0	-0.090	-0.077	18.095	-0.453	-0.453	0.000	0.000	0.000	0.000
140	A	140	ILE	0	0.074	0.031	12.560	0.117	0.117	0.000	0.000	0.000	0.000
141	A	141	SER	0	0.003	0.001	16.561	-0.206	-0.206	0.000	0.000	0.000	0.000
142	A	142	ASN	0	-0.044	-0.030	18.511	0.309	0.309	0.000	0.000	0.000	0.000
143	A	143	LYS	1	0.936	0.979	16.397	18.053	18.053	0.000	0.000	0.000	0.000
144	A	144	LEU	0	0.016	0.017	17.607	-0.469	-0.469	0.000	0.000	0.000	0.000
145	A	145	VAL	0	-0.030	-0.017	13.442	-0.737	-0.737	0.000	0.000	0.000	0.000
146	A	146	TRP	0	-0.037	-0.029	15.396	-0.899	-0.899	0.000	0.000	0.000	0.000
147	A	147	GLY	0	0.023	0.014	17.913	0.616	0.616	0.000	0.000	0.000	0.000
148	A	148	ILE	0	-0.046	-0.025	21.228	-0.478	-0.478	0.000	0.000	0.000	0.000
149	A	149	GLU	-1	-0.840	-0.870	24.092	-12.208	-12.208	0.000	0.000	0.000	0.000
150	A	150	PRO	-1	-0.894	-0.938	26.592	-10.077	-10.077	0.000	0.000	0.000	0.000

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