FMO DATABASE

FMODB ID: 3M7GL

Calculation Name: 2C0L-B-Xray547

Preferred Name: Non-specific lipid-transfer protein

Target Type: SINGLE PROTEIN

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2C0L

Chain ID: B

ChEMBL ID: CHEMBL5950

UniProt ID: P22307

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	122
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-972097.674435
FMO2-HF: Nuclear repulsion	925442.467977
FMO2-HF: Total energy	-46655.206458
FMO2-MP2: Total energy	-46789.10208

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:22:SER)

Summations of interaction energy for fragment #1(A:22:SER)

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.
-28.635	-30.184	26.091	-14.773	-9.769	-0.143

Interaction energy analysis for fragmet #1(A:22:SER)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.758 / q_NPA : 0.853

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	24	SER	0	0.080	0.041	3.231	2.359	4.629	0.122	-1.001	-1.392	0.002
4	A	25	ASP	-1	-0.797	-0.871	1.722	-128.763	-133.015	25.964	-13.580	-8.131	-0.145
5	A	26	GLY	0	-0.005	-0.006	4.163	2.799	2.902	-0.001	-0.042	-0.060	0.000
63	A	84	ASN	0	-0.065	-0.046	3.643	-1.641	-1.311	0.006	-0.150	-0.186	0.000
6	A	27	PHE	0	-0.059	-0.030	7.239	5.087	5.087	0.000	0.000	0.000	0.000
7	A	28	LYS	1	0.908	0.941	9.503	23.463	23.463	0.000	0.000	0.000	0.000
8	A	29	ALA	0	0.042	0.018	10.705	0.572	0.572	0.000	0.000	0.000	0.000
9	A	30	ASN	0	-0.036	-0.020	4.991	3.244	3.244	0.000	0.000	0.000	0.000
10	A	31	LEU	0	-0.036	-0.010	8.662	0.297	0.297	0.000	0.000	0.000	0.000
11	A	32	VAL	0	0.030	0.013	11.617	1.061	1.061	0.000	0.000	0.000	0.000
12	A	33	PHE	0	0.014	-0.010	10.070	1.265	1.265	0.000	0.000	0.000	0.000
13	A	34	LYS	1	0.978	0.995	5.861	38.507	38.507	0.000	0.000	0.000	0.000
14	A	35	GLU	-1	-0.874	-0.924	11.614	-17.039	-17.039	0.000	0.000	0.000	0.000
15	A	36	ILE	0	-0.095	-0.041	14.598	1.214	1.214	0.000	0.000	0.000	0.000
16	A	37	GLU	-1	-0.919	-0.981	10.622	-24.644	-24.644	0.000	0.000	0.000	0.000
17	A	38	LYS	1	0.853	0.926	13.741	20.660	20.660	0.000	0.000	0.000	0.000
18	A	39	LYS	1	0.999	1.004	16.790	15.535	15.535	0.000	0.000	0.000	0.000
19	A	40	LEU	0	-0.066	-0.027	16.751	0.833	0.833	0.000	0.000	0.000	0.000
20	A	41	GLU	-1	-0.907	-0.957	17.142	-14.924	-14.924	0.000	0.000	0.000	0.000
21	A	42	GLU	-1	-0.986	-0.972	19.777	-13.523	-13.523	0.000	0.000	0.000	0.000
22	A	43	GLU	-1	-0.961	-0.998	22.516	-10.996	-10.996	0.000	0.000	0.000	0.000
23	A	44	GLY	0	-0.003	0.007	21.812	0.292	0.292	0.000	0.000	0.000	0.000
24	A	45	GLU	-1	-0.888	-0.953	22.649	-10.466	-10.466	0.000	0.000	0.000	0.000
25	A	46	GLN	0	0.005	-0.010	25.928	0.244	0.244	0.000	0.000	0.000	0.000
26	A	47	PHE	0	-0.035	-0.012	23.204	0.263	0.263	0.000	0.000	0.000	0.000
27	A	48	VAL	0	-0.021	-0.002	23.201	0.172	0.172	0.000	0.000	0.000	0.000
28	A	49	LYS	1	0.909	0.947	25.528	9.495	9.495	0.000	0.000	0.000	0.000
29	A	50	LYS	1	0.928	0.983	27.670	10.808	10.808	0.000	0.000	0.000	0.000
30	A	51	ILE	0	-0.047	-0.015	23.294	0.231	0.231	0.000	0.000	0.000	0.000
31	A	52	GLY	0	0.045	0.032	26.316	0.281	0.281	0.000	0.000	0.000	0.000
32	A	53	GLY	0	-0.027	-0.033	24.586	0.311	0.311	0.000	0.000	0.000	0.000
33	A	54	ILE	0	-0.094	-0.027	18.919	-0.421	-0.421	0.000	0.000	0.000	0.000
34	A	55	PHE	0	0.043	0.016	18.155	0.395	0.395	0.000	0.000	0.000	0.000
35	A	56	ALA	0	0.034	0.021	15.981	-0.884	-0.884	0.000	0.000	0.000	0.000
36	A	57	PHE	0	0.005	-0.015	13.638	0.908	0.908	0.000	0.000	0.000	0.000
37	A	58	LYS	1	0.955	0.980	13.275	15.250	15.250	0.000	0.000	0.000	0.000
38	A	59	VAL	0	0.004	0.000	11.640	1.269	1.269	0.000	0.000	0.000	0.000
39	A	60	LYS	1	0.895	0.924	12.845	15.928	15.928	0.000	0.000	0.000	0.000
40	A	61	ASP	-1	-0.868	-0.955	15.184	-17.754	-17.754	0.000	0.000	0.000	0.000
41	A	62	GLY	0	0.033	0.033	11.856	0.380	0.380	0.000	0.000	0.000	0.000
42	A	63	PRO	0	-0.043	-0.028	8.825	1.114	1.114	0.000	0.000	0.000	0.000
43	A	64	GLY	0	-0.002	-0.003	10.188	-2.432	-2.432	0.000	0.000	0.000	0.000
44	A	65	GLY	0	0.024	0.020	12.434	0.467	0.467	0.000	0.000	0.000	0.000
45	A	66	LYS	1	0.851	0.932	6.553	39.064	39.064	0.000	0.000	0.000	0.000
46	A	67	GLU	-1	-0.838	-0.908	11.802	-19.045	-19.045	0.000	0.000	0.000	0.000
47	A	68	ALA	0	-0.027	-0.010	7.572	-2.923	-2.923	0.000	0.000	0.000	0.000
48	A	69	THR	0	0.012	0.001	8.895	3.282	3.282	0.000	0.000	0.000	0.000
49	A	70	TRP	0	0.016	0.005	6.986	-2.930	-2.930	0.000	0.000	0.000	0.000
50	A	71	VAL	0	-0.010	0.002	10.913	1.684	1.684	0.000	0.000	0.000	0.000
51	A	72	VAL	0	0.004	0.006	13.480	-0.808	-0.808	0.000	0.000	0.000	0.000
52	A	73	ASP	-1	-0.793	-0.897	15.941	-13.088	-13.088	0.000	0.000	0.000	0.000
53	A	74	VAL	0	0.051	0.021	18.472	-0.135	-0.135	0.000	0.000	0.000	0.000
54	A	75	LYS	1	0.830	0.908	21.455	12.204	12.204	0.000	0.000	0.000	0.000
55	A	76	ASN	0	-0.040	-0.036	21.404	0.969	0.969	0.000	0.000	0.000	0.000
56	A	77	GLY	0	0.042	0.020	22.295	-0.479	-0.479	0.000	0.000	0.000	0.000
57	A	78	LYS	1	0.937	0.967	21.278	12.011	12.011	0.000	0.000	0.000	0.000
58	A	79	GLY	0	0.044	0.031	19.941	-0.239	-0.239	0.000	0.000	0.000	0.000
59	A	80	SER	0	-0.059	-0.044	14.999	-0.274	-0.274	0.000	0.000	0.000	0.000
60	A	81	VAL	0	0.012	0.014	10.366	0.253	0.253	0.000	0.000	0.000	0.000
61	A	82	LEU	0	-0.008	-0.003	10.661	-0.624	-0.624	0.000	0.000	0.000	0.000
62	A	83	PRO	0	0.003	-0.018	5.638	0.548	0.548	0.000	0.000	0.000	0.000
64	A	85	SER	0	-0.010	0.018	7.522	1.295	1.295	0.000	0.000	0.000	0.000
65	A	86	ASP	-1	-0.884	-0.941	10.854	-18.867	-18.867	0.000	0.000	0.000	0.000
66	A	87	LYS	1	0.867	0.941	13.834	16.354	16.354	0.000	0.000	0.000	0.000
67	A	88	LYS	1	0.945	0.966	16.318	12.099	12.099	0.000	0.000	0.000	0.000
68	A	89	ALA	0	0.018	-0.005	18.821	-0.128	-0.128	0.000	0.000	0.000	0.000
69	A	90	ASP	-1	-0.794	-0.869	20.896	-11.452	-11.452	0.000	0.000	0.000	0.000
70	A	91	CYS	0	-0.075	-0.015	22.320	0.435	0.435	0.000	0.000	0.000	0.000
71	A	92	THR	0	-0.007	0.001	18.423	-0.884	-0.884	0.000	0.000	0.000	0.000
72	A	93	ILE	0	0.039	0.024	18.156	0.705	0.705	0.000	0.000	0.000	0.000
73	A	94	THR	0	-0.069	-0.040	17.878	-0.887	-0.887	0.000	0.000	0.000	0.000
74	A	95	MET	0	0.006	0.021	17.614	0.930	0.930	0.000	0.000	0.000	0.000
75	A	96	ALA	0	0.094	0.069	16.947	-1.050	-1.050	0.000	0.000	0.000	0.000
76	A	97	ASP	-1	-0.721	-0.877	12.647	-24.884	-24.884	0.000	0.000	0.000	0.000
77	A	98	SER	0	-0.015	-0.004	15.241	0.052	0.052	0.000	0.000	0.000	0.000
78	A	99	ASP	-1	-0.762	-0.889	18.200	-13.402	-13.402	0.000	0.000	0.000	0.000
79	A	100	PHE	0	-0.002	-0.009	13.857	0.596	0.596	0.000	0.000	0.000	0.000
80	A	101	LEU	0	0.018	0.008	15.773	0.290	0.290	0.000	0.000	0.000	0.000
81	A	102	ALA	0	0.005	0.019	17.687	0.632	0.632	0.000	0.000	0.000	0.000
82	A	103	LEU	0	-0.037	-0.019	20.866	0.575	0.575	0.000	0.000	0.000	0.000
83	A	104	MET	0	0.019	0.008	17.507	0.756	0.756	0.000	0.000	0.000	0.000
84	A	105	THR	0	-0.033	-0.022	19.067	0.189	0.189	0.000	0.000	0.000	0.000
85	A	106	GLY	0	0.040	0.026	21.709	0.464	0.464	0.000	0.000	0.000	0.000
86	A	107	LYS	1	0.852	0.925	24.113	12.924	12.924	0.000	0.000	0.000	0.000
87	A	108	MET	0	-0.064	-0.011	23.182	0.589	0.589	0.000	0.000	0.000	0.000
88	A	109	ASN	0	0.064	0.037	25.728	-0.557	-0.557	0.000	0.000	0.000	0.000
89	A	110	PRO	0	0.031	0.011	24.661	-0.060	-0.060	0.000	0.000	0.000	0.000
90	A	111	GLN	0	0.092	0.028	26.222	-0.219	-0.219	0.000	0.000	0.000	0.000
91	A	112	SER	0	0.030	0.016	28.895	0.090	0.090	0.000	0.000	0.000	0.000
92	A	113	ALA	0	0.022	0.021	24.421	0.075	0.075	0.000	0.000	0.000	0.000
93	A	114	PHE	0	-0.028	-0.008	26.576	-0.120	-0.120	0.000	0.000	0.000	0.000
94	A	115	PHE	0	0.009	-0.006	27.872	0.093	0.093	0.000	0.000	0.000	0.000
95	A	116	GLN	0	-0.043	-0.040	27.922	0.078	0.078	0.000	0.000	0.000	0.000
96	A	117	GLY	0	-0.006	0.007	28.344	-0.092	-0.092	0.000	0.000	0.000	0.000
97	A	118	LYS	1	0.857	0.920	23.769	12.246	12.246	0.000	0.000	0.000	0.000
98	A	119	LEU	0	-0.045	-0.008	21.590	-0.762	-0.762	0.000	0.000	0.000	0.000
99	A	120	LYS	1	0.884	0.939	22.487	12.451	12.451	0.000	0.000	0.000	0.000
100	A	121	ILE	0	0.040	0.002	22.460	-0.556	-0.556	0.000	0.000	0.000	0.000
101	A	122	THR	0	-0.023	-0.004	23.624	0.322	0.322	0.000	0.000	0.000	0.000
102	A	123	GLY	0	0.052	0.029	24.516	-0.349	-0.349	0.000	0.000	0.000	0.000
103	A	124	ASN	0	0.019	-0.007	26.473	0.431	0.431	0.000	0.000	0.000	0.000
104	A	125	MET	0	0.070	0.036	26.845	-0.391	-0.391	0.000	0.000	0.000	0.000
105	A	126	GLY	0	0.025	0.012	28.397	-0.082	-0.082	0.000	0.000	0.000	0.000
106	A	127	LEU	0	-0.054	-0.018	23.032	0.008	0.008	0.000	0.000	0.000	0.000
107	A	128	ALA	0	0.070	0.008	23.837	-0.321	-0.321	0.000	0.000	0.000	0.000
108	A	129	MET	0	-0.065	-0.029	24.782	-0.159	-0.159	0.000	0.000	0.000	0.000
109	A	130	LYS	1	0.880	0.942	26.227	10.360	10.360	0.000	0.000	0.000	0.000
110	A	131	LEU	0	0.014	0.016	19.536	-0.186	-0.186	0.000	0.000	0.000	0.000
111	A	132	GLN	0	0.002	-0.004	22.758	-0.498	-0.498	0.000	0.000	0.000	0.000
112	A	133	ASN	0	-0.051	-0.028	25.119	0.075	0.075	0.000	0.000	0.000	0.000
113	A	134	LEU	0	0.000	0.000	18.876	-0.078	-0.078	0.000	0.000	0.000	0.000
114	A	135	GLN	0	-0.064	-0.028	20.112	-0.383	-0.383	0.000	0.000	0.000	0.000
115	A	136	LEU	0	-0.040	-0.006	16.585	0.087	0.087	0.000	0.000	0.000	0.000
116	A	137	GLN	0	-0.020	-0.017	21.272	0.195	0.195	0.000	0.000	0.000	0.000
117	A	138	PRO	0	-0.002	0.008	24.389	-0.228	-0.228	0.000	0.000	0.000	0.000
118	A	139	GLY	0	0.039	0.018	26.448	0.184	0.184	0.000	0.000	0.000	0.000
119	A	140	ASN	0	-0.023	-0.022	28.566	0.014	0.014	0.000	0.000	0.000	0.000
120	A	141	ALA	0	0.019	0.003	32.363	-0.102	-0.102	0.000	0.000	0.000	0.000
121	A	142	LYS	1	0.851	0.923	31.701	9.592	9.592	0.000	0.000	0.000	0.000
122	A	143	LEU	-1	-0.870	-0.915	36.569	-7.811	-7.811	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:22:SER)