FMO DATABASE

FMODB ID: Z631N

Calculation Name: 2B7L-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2B7L

Chain ID: A

ChEMBL ID:

UniProt ID: Q2G2X2

Base Structure: X-ray

Registration Date: 2023-09-20

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	115
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1082421.517236
FMO2-HF: Nuclear repulsion	1033002.84569
FMO2-HF: Total energy	-49418.671547
FMO2-MP2: Total energy	-49561.390273

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:1:MET)

Summations of interaction energy for fragment #1(A:1: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.
-22.529	-21.111	17.027	-7.921	-10.523	-0.016

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.048 / q_NPA : -0.014

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

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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	ARG	1	0.792	0.873	2.305	-6.095	-8.331	11.449	-4.245	-4.968	0.020
4	A	4	VAL	0	-0.004	-0.001	4.682	0.393	0.475	-0.001	-0.012	-0.068	0.000
5	A	5	ILE	0	-0.021	0.004	8.150	0.411	0.411	0.000	0.000	0.000	0.000
6	A	6	THR	0	-0.022	-0.020	11.118	-0.045	-0.045	0.000	0.000	0.000	0.000
7	A	7	TYR	0	0.027	-0.031	14.533	0.070	0.070	0.000	0.000	0.000	0.000
8	A	8	GLY	0	0.028	0.011	17.798	-0.023	-0.023	0.000	0.000	0.000	0.000
9	A	9	THR	0	-0.069	-0.045	20.805	0.025	0.025	0.000	0.000	0.000	0.000
10	A	10	TYR	0	0.045	0.019	17.794	0.025	0.025	0.000	0.000	0.000	0.000
11	A	11	ASP	-1	-0.726	-0.869	22.789	0.011	0.011	0.000	0.000	0.000	0.000
12	A	12	LEU	0	-0.015	-0.004	26.315	0.006	0.006	0.000	0.000	0.000	0.000
13	A	13	LEU	0	-0.023	-0.003	21.978	-0.017	-0.017	0.000	0.000	0.000	0.000
14	A	14	HIS	0	0.036	0.018	25.391	0.003	0.003	0.000	0.000	0.000	0.000
15	A	15	TYR	0	-0.003	-0.036	21.013	0.004	0.004	0.000	0.000	0.000	0.000
16	A	16	GLY	0	0.023	0.019	23.146	-0.018	-0.018	0.000	0.000	0.000	0.000
17	A	17	HIS	0	0.028	0.007	21.473	-0.027	-0.027	0.000	0.000	0.000	0.000
18	A	18	ILE	0	-0.004	0.001	19.268	-0.019	-0.019	0.000	0.000	0.000	0.000
19	A	19	GLU	-1	-0.774	-0.859	18.385	-0.322	-0.322	0.000	0.000	0.000	0.000
20	A	20	LEU	0	-0.031	0.008	16.976	-0.047	-0.047	0.000	0.000	0.000	0.000
21	A	21	LEU	0	0.023	0.008	15.105	-0.062	-0.062	0.000	0.000	0.000	0.000
22	A	22	ARG	1	0.715	0.814	13.817	0.340	0.340	0.000	0.000	0.000	0.000
23	A	23	ARG	1	0.818	0.880	13.755	0.268	0.268	0.000	0.000	0.000	0.000
24	A	24	ALA	0	0.016	0.009	12.642	-0.111	-0.111	0.000	0.000	0.000	0.000
25	A	25	ARG	1	0.798	0.896	5.721	0.628	0.628	0.000	0.000	0.000	0.000
26	A	26	GLU	-1	-0.854	-0.885	9.326	-0.686	-0.686	0.000	0.000	0.000	0.000
27	A	27	MET	0	-0.052	-0.018	10.826	-0.011	-0.011	0.000	0.000	0.000	0.000
28	A	28	GLY	0	0.023	0.002	6.671	-0.285	-0.285	0.000	0.000	0.000	0.000
29	A	29	ASP	-1	-0.880	-0.934	2.314	-8.836	-6.986	5.098	-3.225	-3.723	-0.034
30	A	30	TYR	0	-0.032	-0.024	2.902	0.399	2.109	0.482	-0.430	-1.762	-0.002
31	A	31	LEU	0	-0.032	-0.015	4.752	-0.720	-0.708	-0.001	-0.009	-0.002	0.000
32	A	32	ILE	0	-0.009	0.001	7.650	0.388	0.388	0.000	0.000	0.000	0.000
33	A	33	VAL	0	0.005	-0.014	10.165	-0.198	-0.198	0.000	0.000	0.000	0.000
34	A	34	ALA	0	0.025	0.004	13.950	0.086	0.086	0.000	0.000	0.000	0.000
35	A	35	LEU	0	-0.011	0.009	16.298	-0.047	-0.047	0.000	0.000	0.000	0.000
36	A	36	SER	0	-0.022	-0.033	19.405	0.015	0.015	0.000	0.000	0.000	0.000
37	A	37	THR	0	0.005	-0.015	22.812	0.007	0.007	0.000	0.000	0.000	0.000
38	A	38	ASP	-1	-0.763	-0.858	24.754	0.027	0.027	0.000	0.000	0.000	0.000
39	A	39	GLU	-1	-0.792	-0.863	27.715	0.048	0.048	0.000	0.000	0.000	0.000
40	A	40	PHE	0	0.034	0.025	23.998	-0.009	-0.009	0.000	0.000	0.000	0.000
41	A	41	ASN	0	-0.016	-0.025	27.048	-0.027	-0.027	0.000	0.000	0.000	0.000
42	A	42	GLN	0	-0.004	0.000	28.323	-0.005	-0.005	0.000	0.000	0.000	0.000
43	A	43	ILE	0	0.000	0.005	29.658	-0.005	-0.005	0.000	0.000	0.000	0.000
44	A	44	LYS	1	0.839	0.959	24.487	0.054	0.054	0.000	0.000	0.000	0.000
45	A	45	HIS	0	-0.072	-0.037	30.111	-0.005	-0.005	0.000	0.000	0.000	0.000
46	A	46	LYS	1	0.824	0.908	29.607	0.059	0.059	0.000	0.000	0.000	0.000
47	A	47	LYS	1	0.944	0.962	32.294	0.009	0.009	0.000	0.000	0.000	0.000
48	A	48	SER	0	-0.020	-0.019	28.632	-0.009	-0.009	0.000	0.000	0.000	0.000
49	A	49	TYR	0	-0.060	-0.018	30.595	0.002	0.002	0.000	0.000	0.000	0.000
50	A	50	TYR	0	-0.035	-0.010	27.770	0.007	0.007	0.000	0.000	0.000	0.000
51	A	51	ASP	-1	-0.810	-0.890	27.444	0.078	0.078	0.000	0.000	0.000	0.000
52	A	52	TYR	0	-0.006	-0.026	19.098	0.007	0.007	0.000	0.000	0.000	0.000
53	A	53	GLU	-1	-0.816	-0.908	22.202	0.219	0.219	0.000	0.000	0.000	0.000
54	A	54	GLN	0	-0.074	-0.054	23.325	0.006	0.006	0.000	0.000	0.000	0.000
55	A	55	ARG	1	0.727	0.846	23.109	-0.024	-0.024	0.000	0.000	0.000	0.000
56	A	56	LYS	1	0.816	0.901	17.680	-0.288	-0.288	0.000	0.000	0.000	0.000
57	A	57	MET	0	0.001	0.006	19.034	0.017	0.017	0.000	0.000	0.000	0.000
58	A	58	MET	0	-0.033	-0.011	20.334	0.005	0.005	0.000	0.000	0.000	0.000
59	A	59	LEU	0	-0.010	-0.005	16.961	-0.016	-0.016	0.000	0.000	0.000	0.000
60	A	60	GLU	-1	-0.819	-0.916	15.322	0.336	0.336	0.000	0.000	0.000	0.000
61	A	61	SER	0	-0.094	-0.042	16.015	0.017	0.017	0.000	0.000	0.000	0.000
62	A	62	ILE	0	-0.043	-0.017	16.153	-0.035	-0.035	0.000	0.000	0.000	0.000
63	A	63	ARG	1	0.941	0.949	13.931	0.011	0.011	0.000	0.000	0.000	0.000
64	A	64	TYR	0	-0.049	-0.027	12.095	-0.030	-0.030	0.000	0.000	0.000	0.000
65	A	65	VAL	0	0.038	0.017	11.712	-0.100	-0.100	0.000	0.000	0.000	0.000
66	A	66	ASP	-1	-0.815	-0.875	6.912	0.434	0.434	0.000	0.000	0.000	0.000
67	A	67	LEU	0	-0.024	-0.008	9.050	0.276	0.276	0.000	0.000	0.000	0.000
68	A	68	VAL	0	-0.016	0.003	10.806	-0.207	-0.207	0.000	0.000	0.000	0.000
69	A	69	ILE	0	0.020	0.023	13.146	0.068	0.068	0.000	0.000	0.000	0.000
70	A	70	PRO	0	-0.032	-0.020	15.994	-0.058	-0.058	0.000	0.000	0.000	0.000
71	A	71	GLU	-1	-0.747	-0.854	19.369	-0.107	-0.107	0.000	0.000	0.000	0.000
72	A	72	LYS	1	0.848	0.884	20.481	-0.072	-0.072	0.000	0.000	0.000	0.000
73	A	73	GLY	0	0.003	-0.009	22.895	0.001	0.001	0.000	0.000	0.000	0.000
74	A	74	TRP	0	0.007	-0.007	22.746	-0.008	-0.008	0.000	0.000	0.000	0.000
75	A	75	GLY	0	0.029	0.008	22.657	-0.021	-0.021	0.000	0.000	0.000	0.000
76	A	76	GLN	0	-0.042	-0.024	18.045	-0.006	-0.006	0.000	0.000	0.000	0.000
77	A	77	LYS	1	0.847	0.942	17.544	0.175	0.175	0.000	0.000	0.000	0.000
78	A	78	GLU	-1	-0.836	-0.911	16.474	-0.284	-0.284	0.000	0.000	0.000	0.000
79	A	79	ASP	-1	-0.838	-0.911	16.578	-0.031	-0.031	0.000	0.000	0.000	0.000
80	A	80	ASP	-1	-0.798	-0.882	14.296	0.049	0.049	0.000	0.000	0.000	0.000
81	A	81	VAL	0	-0.008	-0.008	12.180	0.038	0.038	0.000	0.000	0.000	0.000
82	A	82	GLU	-1	-0.920	-0.941	11.642	-0.438	-0.438	0.000	0.000	0.000	0.000
83	A	83	LYS	1	0.720	0.846	12.111	-0.024	-0.024	0.000	0.000	0.000	0.000
84	A	84	PHE	0	-0.074	-0.050	9.548	0.222	0.222	0.000	0.000	0.000	0.000
85	A	85	ASP	-1	-0.855	-0.902	5.435	-0.930	-0.930	0.000	0.000	0.000	0.000
86	A	86	VAL	0	-0.012	-0.009	6.694	-0.708	-0.708	0.000	0.000	0.000	0.000
87	A	87	ASP	-1	-0.795	-0.885	5.839	-5.266	-5.266	0.000	0.000	0.000	0.000
88	A	88	VAL	0	-0.055	-0.024	8.590	0.420	0.420	0.000	0.000	0.000	0.000
89	A	89	PHE	0	0.024	0.007	10.692	0.148	0.148	0.000	0.000	0.000	0.000
90	A	90	VAL	0	0.007	0.008	12.649	0.031	0.031	0.000	0.000	0.000	0.000
91	A	91	MET	0	-0.051	0.009	15.146	0.085	0.085	0.000	0.000	0.000	0.000
92	A	92	GLY	0	0.030	-0.002	18.643	-0.025	-0.025	0.000	0.000	0.000	0.000
93	A	93	HIS	0	-0.057	-0.038	21.719	0.014	0.014	0.000	0.000	0.000	0.000
94	A	94	ASP	-1	-0.920	-0.959	24.508	-0.185	-0.185	0.000	0.000	0.000	0.000
95	A	95	TRP	0	-0.046	-0.032	22.498	0.026	0.026	0.000	0.000	0.000	0.000
96	A	96	GLU	-1	-0.909	-0.951	23.838	-0.320	-0.320	0.000	0.000	0.000	0.000
97	A	97	GLY	0	0.006	0.007	23.850	0.024	0.024	0.000	0.000	0.000	0.000
98	A	98	GLU	-1	-0.963	-0.973	24.359	-0.183	-0.183	0.000	0.000	0.000	0.000
99	A	99	PHE	0	0.004	-0.024	19.886	0.022	0.022	0.000	0.000	0.000	0.000
100	A	100	ASP	-1	-0.770	-0.862	20.544	-0.441	-0.441	0.000	0.000	0.000	0.000
101	A	101	PHE	0	-0.068	-0.028	21.913	-0.023	-0.023	0.000	0.000	0.000	0.000
102	A	102	LEU	0	0.040	0.018	16.977	0.013	0.013	0.000	0.000	0.000	0.000
103	A	103	LYS	1	0.833	0.900	17.521	0.406	0.406	0.000	0.000	0.000	0.000
104	A	104	ASP	-1	-0.892	-0.923	17.988	-0.429	-0.429	0.000	0.000	0.000	0.000
105	A	105	LYS	1	0.751	0.870	15.544	0.357	0.357	0.000	0.000	0.000	0.000
106	A	106	CYS	0	-0.001	0.009	12.422	-0.073	-0.073	0.000	0.000	0.000	0.000
107	A	107	GLU	-1	-0.824	-0.912	11.385	-1.493	-1.493	0.000	0.000	0.000	0.000
108	A	108	VAL	0	-0.048	-0.011	14.002	-0.022	-0.022	0.000	0.000	0.000	0.000
109	A	109	ILE	0	-0.041	-0.027	14.996	0.051	0.051	0.000	0.000	0.000	0.000
110	A	110	TYR	0	-0.009	-0.022	17.483	0.027	0.027	0.000	0.000	0.000	0.000
111	A	111	LEU	0	-0.039	-0.020	16.526	-0.002	-0.002	0.000	0.000	0.000	0.000
112	A	112	LYN	0	0.099	0.050	19.925	0.053	0.053	0.000	0.000	0.000	0.000
113	A	113	ARG	1	0.803	0.871	23.876	0.226	0.226	0.000	0.000	0.000	0.000
114	A	114	THR	0	-0.022	-0.008	20.863	-0.019	-0.019	0.000	0.000	0.000	0.000
115	A	115	GLU	-1	-0.763	-0.841	24.276	-0.179	-0.179	0.000	0.000	0.000	0.000

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