FMO DATABASE

FMODB ID: 195LZ

Calculation Name: 2GBS-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2GBS

Chain ID: A

ChEMBL ID:

UniProt ID: Q6ND56

Base Structure: SolutionNMR

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	145
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1332632.361498
FMO2-HF: Nuclear repulsion	1275166.430132
FMO2-HF: Total energy	-57465.931365
FMO2-MP2: Total energy	-57631.964377

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:VAL)

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

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.
-61.887	-56.58	16.926	-10.867	-11.364	-0.117

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.750 / q_NPA : 0.869

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	TYR	0	-0.006	0.003	3.798	-0.791	1.041	-0.024	-0.737	-1.070	0.002
4	A	4	TRP	0	0.010	-0.004	3.815	8.953	9.116	-0.001	-0.044	-0.118	0.000
43	A	43	MET	0	-0.103	-0.016	4.125	-9.920	-9.841	-0.001	-0.022	-0.055	0.000
44	A	44	ARG	1	0.886	0.924	2.793	55.209	55.911	0.050	-0.231	-0.520	-0.001
45	A	45	ARG	1	0.864	0.920	4.380	26.123	26.301	-0.001	-0.022	-0.155	0.000
46	A	46	GLY	0	0.017	0.018	3.699	-7.717	-6.951	0.011	-0.316	-0.461	-0.002
47	A	47	ASP	-1	-0.805	-0.879	2.045	-143.966	-141.854	16.781	-10.214	-8.679	-0.115
48	A	48	ARG	1	0.760	0.844	2.960	45.639	45.114	0.111	0.719	-0.306	-0.001
5	A	5	LEU	0	-0.035	-0.009	9.079	1.674	1.674	0.000	0.000	0.000	0.000
6	A	6	VAL	0	0.012	0.000	11.589	-0.148	-0.148	0.000	0.000	0.000	0.000
7	A	7	LYS	1	0.790	0.906	14.277	18.096	18.096	0.000	0.000	0.000	0.000
8	A	8	SER	0	0.017	0.015	18.108	-0.055	-0.055	0.000	0.000	0.000	0.000
9	A	9	GLU	-1	-0.844	-0.914	20.160	-11.992	-11.992	0.000	0.000	0.000	0.000
10	A	10	PRO	0	0.003	0.006	23.949	-0.048	-0.048	0.000	0.000	0.000	0.000
11	A	11	SER	0	-0.003	0.004	25.273	0.102	0.102	0.000	0.000	0.000	0.000
12	A	12	VAL	0	-0.043	-0.010	24.552	0.186	0.186	0.000	0.000	0.000	0.000
13	A	13	TRP	0	-0.002	-0.028	18.508	0.269	0.269	0.000	0.000	0.000	0.000
14	A	14	SER	0	0.062	0.038	22.450	-0.411	-0.411	0.000	0.000	0.000	0.000
15	A	15	TRP	0	0.027	0.002	15.373	-0.873	-0.873	0.000	0.000	0.000	0.000
16	A	16	ASP	-1	-0.886	-0.948	20.811	-12.868	-12.868	0.000	0.000	0.000	0.000
17	A	17	GLN	0	-0.031	-0.001	22.773	0.277	0.277	0.000	0.000	0.000	0.000
18	A	18	GLN	0	0.008	0.009	16.368	-0.411	-0.411	0.000	0.000	0.000	0.000
19	A	19	VAL	0	-0.021	-0.024	18.597	-0.672	-0.672	0.000	0.000	0.000	0.000
20	A	20	ALA	0	-0.012	-0.001	19.863	-0.151	-0.151	0.000	0.000	0.000	0.000
21	A	21	LYS	1	0.856	0.922	19.291	14.366	14.366	0.000	0.000	0.000	0.000
22	A	22	GLY	0	-0.004	0.005	16.367	-0.936	-0.936	0.000	0.000	0.000	0.000
23	A	23	ALA	0	-0.050	-0.038	15.621	-1.163	-1.163	0.000	0.000	0.000	0.000
24	A	24	ALA	0	-0.045	-0.015	17.855	0.291	0.291	0.000	0.000	0.000	0.000
25	A	25	GLY	0	-0.035	-0.014	15.484	-0.649	-0.649	0.000	0.000	0.000	0.000
26	A	26	GLU	-1	-0.807	-0.901	15.612	-13.956	-13.956	0.000	0.000	0.000	0.000
27	A	27	ALA	0	0.006	0.020	15.557	-1.534	-1.534	0.000	0.000	0.000	0.000
28	A	28	TRP	0	-0.008	-0.008	13.959	1.030	1.030	0.000	0.000	0.000	0.000
29	A	29	THR	0	0.008	-0.014	15.813	-0.454	-0.454	0.000	0.000	0.000	0.000
30	A	30	GLY	0	0.000	0.002	18.692	0.388	0.388	0.000	0.000	0.000	0.000
31	A	31	VAL	0	-0.036	-0.008	15.797	0.596	0.596	0.000	0.000	0.000	0.000
32	A	32	ARG	1	0.962	0.961	18.900	12.426	12.426	0.000	0.000	0.000	0.000
33	A	33	ASN	0	-0.014	0.000	18.835	-0.253	-0.253	0.000	0.000	0.000	0.000
34	A	34	HIS	0	0.116	0.027	17.760	-1.609	-1.609	0.000	0.000	0.000	0.000
35	A	35	SER	0	0.003	0.024	16.546	-1.251	-1.251	0.000	0.000	0.000	0.000
36	A	36	ALA	0	0.023	0.002	14.367	-1.402	-1.402	0.000	0.000	0.000	0.000
37	A	37	LYS	1	0.946	0.989	12.941	16.343	16.343	0.000	0.000	0.000	0.000
38	A	38	LEU	0	-0.020	-0.006	12.570	-1.329	-1.329	0.000	0.000	0.000	0.000
39	A	39	HIS	0	-0.039	-0.042	9.983	-1.858	-1.858	0.000	0.000	0.000	0.000
40	A	40	MET	0	-0.009	0.002	8.259	-3.651	-3.651	0.000	0.000	0.000	0.000
41	A	41	VAL	0	-0.020	-0.010	8.720	-1.894	-1.894	0.000	0.000	0.000	0.000
42	A	42	ALA	0	-0.029	-0.002	6.225	-0.697	-0.697	0.000	0.000	0.000	0.000
49	A	49	ALA	0	0.021	0.003	5.996	-0.772	-0.772	0.000	0.000	0.000	0.000
50	A	50	PHE	0	-0.013	-0.016	9.212	1.554	1.554	0.000	0.000	0.000	0.000
51	A	51	TYR	0	0.026	0.015	12.716	-0.222	-0.222	0.000	0.000	0.000	0.000
52	A	52	TYR	0	0.016	-0.013	15.190	1.114	1.114	0.000	0.000	0.000	0.000
53	A	53	HIS	0	0.078	0.034	18.156	-0.198	-0.198	0.000	0.000	0.000	0.000
54	A	54	SER	0	-0.010	-0.026	21.643	0.287	0.287	0.000	0.000	0.000	0.000
55	A	55	ASN	0	-0.065	-0.037	23.286	0.444	0.444	0.000	0.000	0.000	0.000
56	A	56	GLU	-1	-0.866	-0.937	26.952	-10.326	-10.326	0.000	0.000	0.000	0.000
57	A	57	GLY	0	0.061	0.030	25.992	-0.433	-0.433	0.000	0.000	0.000	0.000
58	A	58	LYS	1	0.794	0.894	23.866	11.574	11.574	0.000	0.000	0.000	0.000
59	A	59	GLU	-1	-0.890	-0.959	22.136	-12.296	-12.296	0.000	0.000	0.000	0.000
60	A	60	ILE	0	-0.036	-0.003	15.788	-0.443	-0.443	0.000	0.000	0.000	0.000
61	A	61	VAL	0	0.037	0.018	18.739	0.395	0.395	0.000	0.000	0.000	0.000
62	A	62	GLY	0	0.011	0.009	16.122	0.448	0.448	0.000	0.000	0.000	0.000
63	A	63	ILE	0	-0.048	-0.007	9.673	-0.978	-0.978	0.000	0.000	0.000	0.000
64	A	64	ALA	0	0.046	0.017	11.289	1.201	1.201	0.000	0.000	0.000	0.000
65	A	65	GLU	-1	-0.837	-0.916	6.376	-35.619	-35.619	0.000	0.000	0.000	0.000
66	A	66	ILE	0	-0.003	0.014	6.084	3.799	3.799	0.000	0.000	0.000	0.000
67	A	67	ILE	0	0.022	-0.015	7.416	-3.323	-3.323	0.000	0.000	0.000	0.000
68	A	68	ARG	1	0.795	0.860	9.754	21.793	21.793	0.000	0.000	0.000	0.000
69	A	69	GLU	-1	-0.746	-0.865	7.037	-40.887	-40.887	0.000	0.000	0.000	0.000
70	A	70	ALA	0	0.003	0.009	8.902	2.720	2.720	0.000	0.000	0.000	0.000
71	A	71	TYR	0	-0.044	-0.025	10.859	1.423	1.423	0.000	0.000	0.000	0.000
72	A	72	PRO	0	0.032	-0.003	14.508	0.045	0.045	0.000	0.000	0.000	0.000
73	A	73	ASP	-1	-0.778	-0.873	18.069	-15.663	-15.663	0.000	0.000	0.000	0.000
74	A	74	PRO	0	0.028	0.008	19.372	0.604	0.604	0.000	0.000	0.000	0.000
75	A	75	THR	0	-0.064	-0.045	22.404	0.818	0.818	0.000	0.000	0.000	0.000
76	A	76	ASP	-1	-0.847	-0.911	22.394	-12.582	-12.582	0.000	0.000	0.000	0.000
77	A	77	ALA	0	0.015	0.006	23.740	-0.356	-0.356	0.000	0.000	0.000	0.000
78	A	78	SER	0	-0.093	-0.071	25.072	0.343	0.343	0.000	0.000	0.000	0.000
79	A	79	GLY	0	0.012	0.014	20.970	-0.165	-0.165	0.000	0.000	0.000	0.000
80	A	80	LYS	1	0.879	0.956	19.957	11.943	11.943	0.000	0.000	0.000	0.000
81	A	81	PHE	0	-0.036	-0.035	18.715	-0.498	-0.498	0.000	0.000	0.000	0.000
82	A	82	VAL	0	0.008	0.007	13.669	0.266	0.266	0.000	0.000	0.000	0.000
83	A	83	CYS	0	-0.034	-0.002	14.331	0.114	0.114	0.000	0.000	0.000	0.000
84	A	84	VAL	0	0.053	0.018	8.809	-1.018	-1.018	0.000	0.000	0.000	0.000
85	A	85	ASP	-1	-0.756	-0.834	11.743	-18.870	-18.870	0.000	0.000	0.000	0.000
86	A	86	ILE	0	-0.039	-0.018	10.960	-3.124	-3.124	0.000	0.000	0.000	0.000
87	A	87	LYS	1	0.912	0.973	10.125	27.242	27.242	0.000	0.000	0.000	0.000
88	A	88	ALA	0	0.029	0.016	12.547	-1.406	-1.406	0.000	0.000	0.000	0.000
89	A	89	ASP	-1	-0.855	-0.898	10.740	-24.004	-24.004	0.000	0.000	0.000	0.000
90	A	90	LYS	1	0.895	0.926	11.957	21.843	21.843	0.000	0.000	0.000	0.000
91	A	91	PRO	0	0.040	0.027	14.819	-0.913	-0.913	0.000	0.000	0.000	0.000
92	A	92	LEU	0	-0.043	-0.016	14.933	-0.546	-0.546	0.000	0.000	0.000	0.000
93	A	93	LYS	1	0.934	0.977	18.170	12.445	12.445	0.000	0.000	0.000	0.000
94	A	94	THR	0	-0.040	-0.031	21.178	0.857	0.857	0.000	0.000	0.000	0.000
95	A	95	PRO	0	0.043	0.041	21.243	-0.663	-0.663	0.000	0.000	0.000	0.000
96	A	96	VAL	0	0.004	0.011	18.836	0.513	0.513	0.000	0.000	0.000	0.000
97	A	97	THR	0	0.046	0.016	21.297	-0.453	-0.453	0.000	0.000	0.000	0.000
98	A	98	LEU	0	-0.005	-0.015	22.555	-0.073	-0.073	0.000	0.000	0.000	0.000
99	A	99	ALA	0	-0.008	-0.010	24.294	0.188	0.188	0.000	0.000	0.000	0.000
100	A	100	ALA	0	0.047	0.020	23.885	0.176	0.176	0.000	0.000	0.000	0.000
101	A	101	VAL	0	-0.020	-0.029	20.544	-0.119	-0.119	0.000	0.000	0.000	0.000
102	A	102	LYS	1	0.862	0.914	23.216	11.734	11.734	0.000	0.000	0.000	0.000
103	A	103	ALA	0	-0.015	0.012	26.639	0.316	0.316	0.000	0.000	0.000	0.000
104	A	104	GLU	-1	-0.821	-0.906	21.670	-13.052	-13.052	0.000	0.000	0.000	0.000
105	A	105	PRO	0	0.036	0.010	24.142	-0.442	-0.442	0.000	0.000	0.000	0.000
106	A	106	ARG	1	0.813	0.886	18.253	14.953	14.953	0.000	0.000	0.000	0.000
107	A	107	LEU	0	-0.035	-0.028	17.685	-0.855	-0.855	0.000	0.000	0.000	0.000
108	A	108	ALA	0	0.000	0.004	21.124	-0.279	-0.279	0.000	0.000	0.000	0.000
109	A	109	ASP	-1	-0.819	-0.902	22.021	-13.849	-13.849	0.000	0.000	0.000	0.000
110	A	110	MET	0	0.021	0.028	16.447	-0.959	-0.959	0.000	0.000	0.000	0.000
111	A	111	ALA	0	0.041	0.003	15.764	0.760	0.760	0.000	0.000	0.000	0.000
112	A	112	LEU	0	-0.039	-0.016	17.807	0.653	0.653	0.000	0.000	0.000	0.000
113	A	113	MET	0	-0.001	0.023	19.286	1.027	1.027	0.000	0.000	0.000	0.000
114	A	114	LYS	1	0.800	0.929	20.281	15.183	15.183	0.000	0.000	0.000	0.000
115	A	115	TYR	0	-0.037	-0.030	19.026	0.814	0.814	0.000	0.000	0.000	0.000
116	A	116	SER	0	0.027	0.010	20.426	-0.436	-0.436	0.000	0.000	0.000	0.000
117	A	117	ARG	1	0.967	0.975	21.900	12.127	12.127	0.000	0.000	0.000	0.000
118	A	118	LEU	0	-0.030	0.010	15.790	0.235	0.235	0.000	0.000	0.000	0.000
119	A	119	SER	0	0.016	0.003	17.301	-0.398	-0.398	0.000	0.000	0.000	0.000
120	A	120	VAL	0	0.012	0.011	11.238	-0.144	-0.144	0.000	0.000	0.000	0.000
121	A	121	GLN	0	0.004	-0.005	12.790	0.730	0.730	0.000	0.000	0.000	0.000
122	A	122	PRO	0	0.037	0.020	9.739	-2.048	-2.048	0.000	0.000	0.000	0.000
123	A	123	VAL	0	-0.041	-0.015	9.564	2.735	2.735	0.000	0.000	0.000	0.000
124	A	124	THR	0	0.004	-0.032	9.506	-3.427	-3.427	0.000	0.000	0.000	0.000
125	A	125	ALA	0	0.037	-0.001	8.132	0.483	0.483	0.000	0.000	0.000	0.000
126	A	126	GLU	-1	-0.815	-0.890	9.551	-16.787	-16.787	0.000	0.000	0.000	0.000
127	A	127	GLU	-1	-0.773	-0.860	13.319	-20.620	-20.620	0.000	0.000	0.000	0.000
128	A	128	TRP	0	0.015	0.006	8.939	0.149	0.149	0.000	0.000	0.000	0.000
129	A	129	LYS	1	0.972	0.971	11.001	21.653	21.653	0.000	0.000	0.000	0.000
130	A	130	LEU	0	-0.055	-0.022	13.192	1.091	1.091	0.000	0.000	0.000	0.000
131	A	131	VAL	0	0.047	0.019	14.883	0.995	0.995	0.000	0.000	0.000	0.000
132	A	132	CYS	0	-0.026	-0.013	12.616	0.484	0.484	0.000	0.000	0.000	0.000
133	A	133	LYS	1	0.875	0.954	15.408	16.659	16.659	0.000	0.000	0.000	0.000
134	A	134	MET	0	-0.007	0.002	18.231	0.829	0.829	0.000	0.000	0.000	0.000
135	A	135	GLY	0	0.033	0.013	18.909	0.648	0.648	0.000	0.000	0.000	0.000
136	A	136	GLY	0	0.020	0.005	19.947	0.049	0.049	0.000	0.000	0.000	0.000
137	A	137	LEU	0	-0.042	-0.020	13.879	0.223	0.223	0.000	0.000	0.000	0.000
138	A	138	LEU	0	-0.040	-0.025	17.080	-0.771	-0.771	0.000	0.000	0.000	0.000
139	A	139	GLU	-1	-0.865	-0.919	16.937	-13.834	-13.834	0.000	0.000	0.000	0.000
140	A	140	HIS	0	0.011	0.003	18.739	-0.378	-0.378	0.000	0.000	0.000	0.000
141	A	141	HIS	1	0.864	0.912	19.028	13.870	13.870	0.000	0.000	0.000	0.000
142	A	142	HIS	0	-0.098	-0.040	16.278	0.259	0.259	0.000	0.000	0.000	0.000
143	A	143	HIS	0	0.032	0.016	21.788	-0.041	-0.041	0.000	0.000	0.000	0.000
144	A	144	HIS	0	-0.047	-0.035	25.369	-0.274	-0.274	0.000	0.000	0.000	0.000
145	A	145	HIS	-1	-0.924	-0.937	28.642	-9.460	-9.460	0.000	0.000	0.000	0.000

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