FMO DATABASE

FMODB ID: G6JG1

Calculation Name: 1NCN-A-Xray372

Preferred Name: T-lymphocyte activation antigen CD86

Target Type: SINGLE PROTEIN

Ligand Name:

ligand 3-letter code:

PDB ID: 1NCN

Chain ID: A

ChEMBL ID: CHEMBL2364156

UniProt ID: P42081

Base Structure: X-ray

Registration Date: 2023-09-19

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptAll
Protonation	MOE:Protonate 3D
Complement	MOE:Structure Preparation
Water	No
Procedure	Auto-FMO protocol ver. 2.20220422

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	109
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-926490.819253
FMO2-HF: Nuclear repulsion	880835.465026
FMO2-HF: Total energy	-45655.354227
FMO2-MP2: Total energy	-45786.378078

3D Structure

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:0:MET)

Summations of interaction energy for fragment #1(A:0:MET)

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.
-7.096	-0.61	7.191	-3.677	-10	-0.02

Interaction energy analysis for fragmet #1(A:0:MET)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.012 / 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

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	2	LYS	1	0.811	0.885	3.249	3.370	6.359	0.084	-1.061	-2.012	0.001
4	A	3	ILE	0	0.018	0.016	4.300	0.503	0.636	0.000	-0.023	-0.109	0.000
5	A	4	GLN	0	-0.021	-0.018	7.621	-0.118	-0.118	0.000	0.000	0.000	0.000
6	A	5	ALA	0	0.027	0.022	10.523	0.065	0.065	0.000	0.000	0.000	0.000
7	A	6	TYR	0	0.010	0.001	13.981	-0.051	-0.051	0.000	0.000	0.000	0.000
8	A	7	PHE	0	0.009	-0.014	17.064	0.030	0.030	0.000	0.000	0.000	0.000
9	A	8	ASN	0	-0.054	-0.014	19.210	0.008	0.008	0.000	0.000	0.000	0.000
10	A	9	GLU	-1	-0.892	-0.939	18.451	-0.119	-0.119	0.000	0.000	0.000	0.000
11	A	10	THR	0	-0.048	-0.039	17.761	0.035	0.035	0.000	0.000	0.000	0.000
12	A	11	ALA	0	-0.033	-0.009	12.332	-0.053	-0.053	0.000	0.000	0.000	0.000
13	A	12	ASP	-1	-0.781	-0.845	13.214	0.057	0.057	0.000	0.000	0.000	0.000
14	A	13	LEU	0	-0.008	-0.007	9.542	-0.049	-0.049	0.000	0.000	0.000	0.000
15	A	14	PRO	0	0.030	0.025	8.491	0.018	0.018	0.000	0.000	0.000	0.000
16	A	15	CYS	0	-0.036	0.004	7.959	-0.016	-0.016	0.000	0.000	0.000	0.000
17	A	16	GLN	0	-0.014	-0.026	6.271	0.546	0.546	0.000	0.000	0.000	0.000
18	A	17	PHE	0	0.013	0.016	10.944	-0.004	-0.004	0.000	0.000	0.000	0.000
19	A	18	ALA	0	0.008	-0.005	14.010	-0.065	-0.065	0.000	0.000	0.000	0.000
20	A	19	ASN	0	-0.002	-0.003	15.981	-0.026	-0.026	0.000	0.000	0.000	0.000
21	A	20	SER	0	0.019	0.015	18.157	-0.020	-0.020	0.000	0.000	0.000	0.000
22	A	21	GLN	0	-0.036	-0.021	16.369	-0.039	-0.039	0.000	0.000	0.000	0.000
23	A	22	ASN	0	-0.043	-0.016	21.689	-0.019	-0.019	0.000	0.000	0.000	0.000
24	A	23	GLN	0	-0.042	-0.007	22.191	-0.013	-0.013	0.000	0.000	0.000	0.000
25	A	24	SER	0	0.000	-0.020	23.737	0.001	0.001	0.000	0.000	0.000	0.000
26	A	25	LEU	0	0.049	0.005	21.163	0.011	0.011	0.000	0.000	0.000	0.000
27	A	26	SER	0	0.017	-0.001	24.133	0.004	0.004	0.000	0.000	0.000	0.000
28	A	27	GLU	-1	-0.860	-0.887	25.513	0.153	0.153	0.000	0.000	0.000	0.000
29	A	28	LEU	0	-0.043	-0.020	20.058	0.014	0.014	0.000	0.000	0.000	0.000
30	A	29	VAL	0	-0.005	-0.005	20.159	-0.020	-0.020	0.000	0.000	0.000	0.000
31	A	30	VAL	0	-0.010	0.010	15.751	0.036	0.036	0.000	0.000	0.000	0.000
32	A	31	PHE	0	-0.008	-0.012	15.281	-0.043	-0.043	0.000	0.000	0.000	0.000
33	A	32	TRP	0	0.056	0.021	10.055	0.113	0.113	0.000	0.000	0.000	0.000
34	A	33	GLN	0	-0.022	-0.007	11.078	-0.054	-0.054	0.000	0.000	0.000	0.000
35	A	34	ASP	-1	-0.680	-0.809	10.584	0.382	0.382	0.000	0.000	0.000	0.000
36	A	35	GLN	0	0.035	0.013	8.408	-0.090	-0.090	0.000	0.000	0.000	0.000
37	A	36	GLU	-1	-0.890	-0.920	10.390	0.033	0.033	0.000	0.000	0.000	0.000
38	A	37	ASN	0	-0.071	-0.041	12.483	0.015	0.015	0.000	0.000	0.000	0.000
39	A	38	LEU	0	-0.017	0.000	13.904	0.000	0.000	0.000	0.000	0.000	0.000
40	A	39	VAL	0	0.008	0.002	15.152	0.045	0.045	0.000	0.000	0.000	0.000
41	A	40	LEU	0	-0.010	-0.002	13.351	-0.038	-0.038	0.000	0.000	0.000	0.000
42	A	41	ASN	0	-0.041	-0.040	16.629	-0.023	-0.023	0.000	0.000	0.000	0.000
43	A	42	GLU	-1	-0.753	-0.864	17.457	0.244	0.244	0.000	0.000	0.000	0.000
44	A	43	VAL	0	-0.006	0.004	19.533	-0.032	-0.032	0.000	0.000	0.000	0.000
45	A	44	TYR	0	0.011	0.000	21.618	0.019	0.019	0.000	0.000	0.000	0.000
46	A	45	LEU	0	-0.064	-0.031	24.078	-0.018	-0.018	0.000	0.000	0.000	0.000
47	A	46	GLY	0	0.043	0.025	24.604	-0.014	-0.014	0.000	0.000	0.000	0.000
48	A	47	LYS	1	0.874	0.935	25.894	-0.123	-0.123	0.000	0.000	0.000	0.000
49	A	48	GLU	-1	-0.784	-0.887	21.836	0.159	0.159	0.000	0.000	0.000	0.000
50	A	49	LYS	1	0.723	0.849	23.510	-0.184	-0.184	0.000	0.000	0.000	0.000
51	A	50	PHE	0	0.082	0.014	22.993	0.010	0.010	0.000	0.000	0.000	0.000
52	A	51	ASP	-1	-0.896	-0.934	25.082	0.130	0.130	0.000	0.000	0.000	0.000
53	A	52	SER	0	-0.028	-0.025	21.545	-0.003	-0.003	0.000	0.000	0.000	0.000
54	A	53	VAL	0	-0.066	-0.012	20.310	0.012	0.012	0.000	0.000	0.000	0.000
55	A	54	HIS	0	0.069	0.039	19.674	-0.020	-0.020	0.000	0.000	0.000	0.000
56	A	55	SER	0	0.027	-0.005	21.523	0.000	0.000	0.000	0.000	0.000	0.000
57	A	56	LYS	1	0.768	0.874	15.910	-0.107	-0.107	0.000	0.000	0.000	0.000
58	A	57	TYR	0	-0.025	-0.060	14.788	-0.011	-0.011	0.000	0.000	0.000	0.000
59	A	58	MET	0	-0.008	0.016	20.128	0.001	0.001	0.000	0.000	0.000	0.000
60	A	59	GLY	0	-0.008	-0.001	23.582	-0.013	-0.013	0.000	0.000	0.000	0.000
61	A	60	ARG	1	0.725	0.839	17.825	-0.038	-0.038	0.000	0.000	0.000	0.000
62	A	61	THR	0	-0.028	-0.021	17.081	-0.008	-0.008	0.000	0.000	0.000	0.000
63	A	62	SER	0	-0.023	0.000	18.895	-0.018	-0.018	0.000	0.000	0.000	0.000
64	A	63	PHE	0	0.010	-0.004	15.893	0.015	0.015	0.000	0.000	0.000	0.000
65	A	64	ASP	-1	-0.784	-0.857	18.352	0.082	0.082	0.000	0.000	0.000	0.000
66	A	65	SER	0	-0.034	-0.045	18.667	0.034	0.034	0.000	0.000	0.000	0.000
67	A	66	ASP	-1	-0.923	-0.943	20.753	0.111	0.111	0.000	0.000	0.000	0.000
68	A	67	SER	0	-0.091	-0.077	17.240	-0.004	-0.004	0.000	0.000	0.000	0.000
69	A	68	TRP	0	-0.006	-0.001	15.655	0.057	0.057	0.000	0.000	0.000	0.000
70	A	69	THR	0	-0.011	-0.018	13.683	0.109	0.109	0.000	0.000	0.000	0.000
71	A	70	LEU	0	-0.043	-0.008	13.620	-0.040	-0.040	0.000	0.000	0.000	0.000
72	A	71	ARG	1	0.858	0.901	14.279	0.000	0.000	0.000	0.000	0.000	0.000
73	A	72	LEU	0	-0.019	-0.016	13.587	0.021	0.021	0.000	0.000	0.000	0.000
74	A	73	HIS	0	0.001	-0.025	16.576	-0.055	-0.055	0.000	0.000	0.000	0.000
75	A	74	ASN	0	0.001	-0.004	19.491	-0.001	-0.001	0.000	0.000	0.000	0.000
76	A	75	LEU	0	0.031	0.032	14.406	0.009	0.009	0.000	0.000	0.000	0.000
77	A	76	GLN	0	-0.001	-0.006	17.106	-0.024	-0.024	0.000	0.000	0.000	0.000
78	A	77	ILE	0	0.010	-0.002	16.123	-0.011	-0.011	0.000	0.000	0.000	0.000
79	A	78	LYS	1	0.849	0.899	15.662	0.041	0.041	0.000	0.000	0.000	0.000
80	A	79	ASP	-1	-0.708	-0.802	14.103	0.004	0.004	0.000	0.000	0.000	0.000
81	A	80	LYS	1	0.907	0.985	10.932	0.383	0.383	0.000	0.000	0.000	0.000
82	A	81	GLY	0	0.033	0.008	8.416	-0.010	-0.010	0.000	0.000	0.000	0.000
83	A	82	LEU	0	-0.059	-0.034	2.582	-0.313	-0.898	3.237	-0.547	-2.105	-0.002
84	A	83	TYR	0	-0.037	-0.046	6.085	-0.441	-0.441	0.000	0.000	0.000	0.000
85	A	84	GLN	0	-0.007	-0.003	6.179	0.953	0.953	0.000	0.000	0.000	0.000
86	A	86	ILE	0	-0.017	-0.025	9.946	0.090	0.090	0.000	0.000	0.000	0.000
87	A	87	ILE	0	0.033	0.022	12.654	-0.064	-0.064	0.000	0.000	0.000	0.000
88	A	88	HIS	0	-0.020	-0.013	15.933	0.015	0.015	0.000	0.000	0.000	0.000
89	A	89	HIS	0	0.042	0.024	18.868	-0.014	-0.014	0.000	0.000	0.000	0.000
90	A	90	LYS	1	0.862	0.940	22.203	-0.164	-0.164	0.000	0.000	0.000	0.000
91	A	91	LYS	1	0.989	0.987	25.125	-0.199	-0.199	0.000	0.000	0.000	0.000
92	A	92	PRO	0	0.010	-0.006	27.468	0.001	0.001	0.000	0.000	0.000	0.000
93	A	93	THR	0	-0.022	-0.019	29.016	0.000	0.000	0.000	0.000	0.000	0.000
94	A	94	GLY	0	0.024	0.015	26.742	-0.005	-0.005	0.000	0.000	0.000	0.000
95	A	95	MET	0	0.001	0.013	21.368	0.002	0.002	0.000	0.000	0.000	0.000
96	A	96	ILE	0	-0.011	-0.001	20.195	-0.006	-0.006	0.000	0.000	0.000	0.000
97	A	97	ARG	1	0.897	0.952	12.721	-0.501	-0.501	0.000	0.000	0.000	0.000
98	A	98	ILE	0	-0.028	-0.024	16.962	-0.004	-0.004	0.000	0.000	0.000	0.000
99	A	99	HIS	0	-0.008	-0.015	11.128	-0.062	-0.062	0.000	0.000	0.000	0.000
100	A	100	GLN	0	0.006	-0.001	8.494	-0.148	-0.148	0.000	0.000	0.000	0.000
101	A	101	MET	0	-0.015	0.026	4.754	-0.263	-0.127	-0.001	-0.015	-0.120	0.000
102	A	102	ASN	0	0.004	-0.005	2.544	-1.943	-1.230	0.834	-0.353	-1.194	0.000
103	A	103	SER	0	0.016	-0.002	3.503	0.037	1.311	0.671	-0.536	-1.409	-0.004
104	A	104	GLU	-1	-0.814	-0.889	2.518	-8.511	-6.743	2.363	-1.119	-3.013	-0.015
105	A	105	LEU	0	0.009	0.028	4.146	-0.917	-0.859	0.003	-0.023	-0.038	0.000
106	A	106	SER	0	-0.003	-0.013	7.729	0.000	0.000	0.000	0.000	0.000	0.000
107	A	107	VAL	0	-0.003	-0.001	9.910	0.031	0.031	0.000	0.000	0.000	0.000
108	A	108	LEU	0	-0.028	-0.007	13.626	0.009	0.009	0.000	0.000	0.000	0.000
109	A	109	ALA	0	0.033	0.009	16.096	0.035	0.035	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:0:MET)