FMO DATABASE

FMODB ID: 6Z95Z

Calculation Name: 2CSJ-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2CSJ

Chain ID: A

ChEMBL ID:

UniProt ID: Q9Z0U1

Base Structure: SolutionNMR

Registration Date: 2025-10-03

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	-782244.655211
FMO2-HF: Nuclear repulsion	738839.406046
FMO2-HF: Total energy	-43405.249165
FMO2-MP2: Total energy	-43531.616069

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.
-33.055	-32.107	-0.014	-0.366	-0.568	-0.002

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 : 0.850 / q_NPA : 0.914

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	SER	0	0.024	0.020	3.836	4.082	5.030	-0.014	-0.366	-0.568	-0.002
4	A	4	GLY	0	0.051	0.023	7.050	2.407	2.407	0.000	0.000	0.000	0.000
5	A	5	SER	0	-0.042	-0.022	9.197	-1.697	-1.697	0.000	0.000	0.000	0.000
6	A	6	SER	0	-0.012	-0.006	11.577	1.607	1.607	0.000	0.000	0.000	0.000
7	A	7	GLY	0	0.063	0.031	13.240	-0.537	-0.537	0.000	0.000	0.000	0.000
8	A	8	MET	0	-0.053	-0.033	15.910	1.155	1.155	0.000	0.000	0.000	0.000
9	A	9	GLU	-1	-0.957	-0.977	18.618	-16.182	-16.182	0.000	0.000	0.000	0.000
10	A	10	GLU	-1	-0.865	-0.918	16.372	-18.717	-18.717	0.000	0.000	0.000	0.000
11	A	11	VAL	0	-0.066	-0.040	19.999	1.143	1.143	0.000	0.000	0.000	0.000
12	A	12	ILE	0	0.014	0.018	21.471	-0.497	-0.497	0.000	0.000	0.000	0.000
13	A	13	TRP	0	0.012	-0.009	20.040	0.892	0.892	0.000	0.000	0.000	0.000
14	A	14	GLU	-1	-0.867	-0.926	24.052	-10.676	-10.676	0.000	0.000	0.000	0.000
15	A	15	GLN	0	-0.016	-0.027	26.466	-0.089	-0.089	0.000	0.000	0.000	0.000
16	A	16	TYR	0	-0.029	-0.012	29.011	0.420	0.420	0.000	0.000	0.000	0.000
17	A	17	THR	0	-0.006	-0.007	32.563	-0.150	-0.150	0.000	0.000	0.000	0.000
18	A	18	VAL	0	0.010	0.011	34.513	0.238	0.238	0.000	0.000	0.000	0.000
19	A	19	THR	0	-0.016	-0.018	37.814	-0.123	-0.123	0.000	0.000	0.000	0.000
20	A	20	LEU	0	0.027	0.036	38.182	0.183	0.183	0.000	0.000	0.000	0.000
21	A	21	GLN	0	0.011	-0.017	41.910	0.149	0.149	0.000	0.000	0.000	0.000
22	A	22	LYS	1	0.892	0.967	44.664	7.028	7.028	0.000	0.000	0.000	0.000
23	A	23	ASP	-1	-0.848	-0.934	46.325	-6.297	-6.297	0.000	0.000	0.000	0.000
24	A	24	SER	0	-0.031	-0.013	48.912	0.001	0.001	0.000	0.000	0.000	0.000
25	A	25	LYS	1	0.932	0.954	50.133	6.231	6.231	0.000	0.000	0.000	0.000
26	A	26	ARG	1	0.981	0.994	46.014	6.792	6.792	0.000	0.000	0.000	0.000
27	A	27	GLY	0	0.020	0.019	44.772	-0.191	-0.191	0.000	0.000	0.000	0.000
28	A	28	PHE	0	-0.013	-0.020	40.749	0.072	0.072	0.000	0.000	0.000	0.000
29	A	29	GLY	0	0.017	0.010	41.729	-0.083	-0.083	0.000	0.000	0.000	0.000
30	A	30	ILE	0	0.024	0.013	36.695	-0.063	-0.063	0.000	0.000	0.000	0.000
31	A	31	ALA	0	-0.014	0.004	37.625	0.104	0.104	0.000	0.000	0.000	0.000
32	A	32	VAL	0	0.015	0.015	32.587	-0.179	-0.179	0.000	0.000	0.000	0.000
33	A	33	SER	0	-0.025	-0.024	31.902	0.310	0.310	0.000	0.000	0.000	0.000
34	A	34	GLY	0	0.005	0.025	28.169	-0.296	-0.296	0.000	0.000	0.000	0.000
35	A	35	GLY	0	0.007	-0.019	26.903	0.452	0.452	0.000	0.000	0.000	0.000
36	A	36	ARG	1	0.869	0.926	23.294	12.541	12.541	0.000	0.000	0.000	0.000
37	A	37	ASP	-1	-0.956	-0.957	23.500	-12.131	-12.131	0.000	0.000	0.000	0.000
38	A	38	ASN	0	-0.020	-0.011	26.046	0.104	0.104	0.000	0.000	0.000	0.000
39	A	39	PRO	0	0.018	0.014	22.793	0.447	0.447	0.000	0.000	0.000	0.000
40	A	40	HIS	0	-0.017	-0.030	25.539	0.154	0.154	0.000	0.000	0.000	0.000
41	A	41	PHE	0	-0.041	-0.011	23.048	0.169	0.169	0.000	0.000	0.000	0.000
42	A	42	GLU	-1	-0.906	-0.946	24.313	-12.213	-12.213	0.000	0.000	0.000	0.000
43	A	43	ASN	0	-0.022	-0.015	18.875	-0.244	-0.244	0.000	0.000	0.000	0.000
44	A	44	GLY	0	0.013	0.018	20.016	-0.700	-0.700	0.000	0.000	0.000	0.000
45	A	45	GLU	-1	-0.917	-0.941	19.469	-16.285	-16.285	0.000	0.000	0.000	0.000
46	A	46	THR	0	-0.033	-0.015	20.025	0.627	0.627	0.000	0.000	0.000	0.000
47	A	47	SER	0	-0.050	-0.044	21.447	0.350	0.350	0.000	0.000	0.000	0.000
48	A	48	ILE	0	-0.040	-0.014	23.839	0.397	0.397	0.000	0.000	0.000	0.000
49	A	49	VAL	0	0.007	0.002	26.976	-0.180	-0.180	0.000	0.000	0.000	0.000
50	A	50	ILE	0	-0.031	-0.013	29.591	0.250	0.250	0.000	0.000	0.000	0.000
51	A	51	SER	0	-0.010	-0.021	32.935	-0.253	-0.253	0.000	0.000	0.000	0.000
52	A	52	ASP	-1	-0.928	-0.951	34.441	-7.804	-7.804	0.000	0.000	0.000	0.000
53	A	53	VAL	0	0.004	-0.007	36.805	-0.078	-0.078	0.000	0.000	0.000	0.000
54	A	54	LEU	0	0.025	0.009	39.547	0.146	0.146	0.000	0.000	0.000	0.000
55	A	55	PRO	0	0.017	0.013	43.337	0.057	0.057	0.000	0.000	0.000	0.000
56	A	56	GLY	0	0.027	0.006	44.680	0.139	0.139	0.000	0.000	0.000	0.000
57	A	57	GLY	0	-0.029	-0.022	46.322	0.156	0.156	0.000	0.000	0.000	0.000
58	A	58	PRO	0	-0.053	-0.021	44.309	-0.067	-0.067	0.000	0.000	0.000	0.000
59	A	59	ALA	0	-0.009	-0.006	40.082	-0.095	-0.095	0.000	0.000	0.000	0.000
60	A	60	ASP	-1	-0.914	-0.946	40.664	-7.523	-7.523	0.000	0.000	0.000	0.000
61	A	61	GLY	0	0.021	0.021	40.988	0.123	0.123	0.000	0.000	0.000	0.000
62	A	62	LEU	0	-0.087	-0.032	39.890	-0.141	-0.141	0.000	0.000	0.000	0.000
63	A	63	LEU	0	-0.042	-0.036	34.263	-0.276	-0.276	0.000	0.000	0.000	0.000
64	A	64	GLN	0	-0.015	-0.023	34.570	0.038	0.038	0.000	0.000	0.000	0.000
65	A	65	GLU	-1	-0.829	-0.904	33.575	-9.613	-9.613	0.000	0.000	0.000	0.000
66	A	66	ASN	0	-0.081	-0.052	29.072	-0.219	-0.219	0.000	0.000	0.000	0.000
67	A	67	ASP	-1	-0.803	-0.915	28.548	-10.510	-10.510	0.000	0.000	0.000	0.000
68	A	68	ARG	1	0.894	0.937	23.573	12.625	12.625	0.000	0.000	0.000	0.000
69	A	69	VAL	0	0.002	0.004	26.650	-0.039	-0.039	0.000	0.000	0.000	0.000
70	A	70	VAL	0	0.002	0.013	24.475	-0.379	-0.379	0.000	0.000	0.000	0.000
71	A	71	MET	0	-0.028	-0.009	26.679	0.011	0.011	0.000	0.000	0.000	0.000
72	A	72	VAL	0	0.023	0.014	29.763	0.274	0.274	0.000	0.000	0.000	0.000
73	A	73	ASN	0	-0.045	-0.030	33.375	0.012	0.012	0.000	0.000	0.000	0.000
74	A	74	GLY	0	0.042	0.010	33.005	0.137	0.137	0.000	0.000	0.000	0.000
75	A	75	THR	0	-0.064	-0.025	30.690	-0.103	-0.103	0.000	0.000	0.000	0.000
76	A	76	PRO	0	0.031	0.017	25.784	0.120	0.120	0.000	0.000	0.000	0.000
77	A	77	MET	0	-0.064	-0.045	27.066	0.377	0.377	0.000	0.000	0.000	0.000
78	A	78	GLU	-1	-0.910	-0.948	21.331	-14.846	-14.846	0.000	0.000	0.000	0.000
79	A	79	ASP	-1	-0.837	-0.934	20.947	-14.615	-14.615	0.000	0.000	0.000	0.000
80	A	80	VAL	0	-0.031	0.001	23.068	0.466	0.466	0.000	0.000	0.000	0.000
81	A	81	LEU	0	0.001	-0.004	26.915	-0.080	-0.080	0.000	0.000	0.000	0.000
82	A	82	HIS	0	0.042	0.016	29.499	0.205	0.205	0.000	0.000	0.000	0.000
83	A	83	SER	0	0.022	0.000	31.887	0.094	0.094	0.000	0.000	0.000	0.000
84	A	84	PHE	0	0.009	-0.002	30.155	0.348	0.348	0.000	0.000	0.000	0.000
85	A	85	ALA	0	0.062	0.027	30.762	0.141	0.141	0.000	0.000	0.000	0.000
86	A	86	VAL	0	0.013	0.005	32.650	0.240	0.240	0.000	0.000	0.000	0.000
87	A	87	GLN	0	-0.007	-0.010	35.931	0.442	0.442	0.000	0.000	0.000	0.000
88	A	88	GLN	0	0.051	0.025	33.703	0.550	0.550	0.000	0.000	0.000	0.000
89	A	89	LEU	0	0.034	0.029	36.128	0.235	0.235	0.000	0.000	0.000	0.000
90	A	90	ARG	1	0.892	0.942	38.948	7.823	7.823	0.000	0.000	0.000	0.000
91	A	91	LYS	1	0.859	0.930	37.726	8.592	8.592	0.000	0.000	0.000	0.000
92	A	92	SER	0	-0.021	-0.007	40.466	0.059	0.059	0.000	0.000	0.000	0.000
93	A	93	GLY	0	-0.009	-0.002	42.374	0.094	0.094	0.000	0.000	0.000	0.000
94	A	94	LYS	1	0.906	0.929	46.162	6.586	6.586	0.000	0.000	0.000	0.000
95	A	95	ILE	0	0.026	0.021	42.635	-0.003	-0.003	0.000	0.000	0.000	0.000
96	A	96	ALA	0	0.018	0.033	38.822	-0.038	-0.038	0.000	0.000	0.000	0.000
97	A	97	ALA	0	0.002	0.010	37.185	0.050	0.050	0.000	0.000	0.000	0.000
98	A	98	ILE	0	-0.011	-0.010	32.892	-0.178	-0.178	0.000	0.000	0.000	0.000
99	A	99	VAL	0	0.008	0.015	29.156	0.146	0.146	0.000	0.000	0.000	0.000
100	A	100	VAL	0	0.004	0.012	28.909	-0.326	-0.326	0.000	0.000	0.000	0.000
101	A	101	LYS	1	0.958	0.987	20.495	15.107	15.107	0.000	0.000	0.000	0.000
102	A	102	ARG	1	0.899	0.954	26.980	9.964	9.964	0.000	0.000	0.000	0.000
103	A	103	PRO	0	-0.015	-0.003	24.296	-0.161	-0.161	0.000	0.000	0.000	0.000
104	A	104	ARG	1	0.894	0.955	25.730	11.011	11.011	0.000	0.000	0.000	0.000
105	A	105	LYS	1	0.976	0.979	24.314	11.716	11.716	0.000	0.000	0.000	0.000
106	A	106	VAL	0	0.032	0.017	23.321	0.677	0.677	0.000	0.000	0.000	0.000
107	A	107	GLN	0	-0.042	-0.021	26.126	0.234	0.234	0.000	0.000	0.000	0.000
108	A	108	VAL	0	0.004	0.003	29.717	0.041	0.041	0.000	0.000	0.000	0.000
109	A	109	ALA	0	0.024	0.008	32.840	0.061	0.061	0.000	0.000	0.000	0.000
110	A	110	PRO	0	0.000	0.009	36.580	-0.023	-0.023	0.000	0.000	0.000	0.000
111	A	111	LEU	0	0.008	0.000	39.907	0.018	0.018	0.000	0.000	0.000	0.000
112	A	112	SER	0	-0.028	-0.015	42.580	0.101	0.101	0.000	0.000	0.000	0.000
113	A	113	GLY	0	0.022	0.000	45.051	-0.007	-0.007	0.000	0.000	0.000	0.000
114	A	114	PRO	0	-0.029	-0.003	48.094	-0.044	-0.044	0.000	0.000	0.000	0.000
115	A	115	SER	0	-0.019	-0.010	51.260	-0.045	-0.045	0.000	0.000	0.000	0.000
116	A	116	SER	0	-0.076	-0.057	53.304	0.029	0.029	0.000	0.000	0.000	0.000
117	A	117	GLY	-1	-0.870	-0.907	56.153	-5.609	-5.609	0.000	0.000	0.000	0.000

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