FMO DATABASE

FMODB ID: 6N98Z

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	OptHSide
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	-1082177.167832
FMO2-HF: Nuclear repulsion	1032759.167834
FMO2-HF: Total energy	-49417.999998
FMO2-MP2: Total energy	-49560.79294

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.
-25.213	-24.45	17.75	-7.55	-10.963	-0.006

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 : -0.051 / q_NPA : -0.011

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	0.777	0.869	2.365	-6.004	-9.436	13.374	-4.334	-5.608	0.023
4	A	4	VAL	0	0.012	0.013	4.324	0.372	0.477	-0.001	-0.019	-0.086	0.000
5	A	5	ILE	0	0.001	0.015	7.750	0.513	0.513	0.000	0.000	0.000	0.000
6	A	6	THR	0	-0.047	-0.035	10.782	-0.074	-0.074	0.000	0.000	0.000	0.000
7	A	7	TYR	0	0.022	-0.043	14.395	0.075	0.075	0.000	0.000	0.000	0.000
8	A	8	GLY	0	0.032	0.011	17.594	-0.026	-0.026	0.000	0.000	0.000	0.000
9	A	9	THR	0	-0.076	-0.039	20.669	0.026	0.026	0.000	0.000	0.000	0.000
10	A	10	TYR	0	0.055	0.020	17.669	0.026	0.026	0.000	0.000	0.000	0.000
11	A	11	ASP	-1	-0.726	-0.874	22.839	0.040	0.040	0.000	0.000	0.000	0.000
12	A	12	LEU	0	-0.025	0.001	26.257	0.010	0.010	0.000	0.000	0.000	0.000
13	A	13	LEU	0	-0.028	-0.004	21.572	-0.015	-0.015	0.000	0.000	0.000	0.000
14	A	14	HIS	0	0.079	0.046	25.269	0.004	0.004	0.000	0.000	0.000	0.000
15	A	15	TYR	0	-0.040	-0.049	21.386	0.004	0.004	0.000	0.000	0.000	0.000
16	A	16	GLY	0	0.050	0.030	23.178	-0.015	-0.015	0.000	0.000	0.000	0.000
17	A	17	HIS	0	0.008	-0.018	21.042	-0.021	-0.021	0.000	0.000	0.000	0.000
18	A	18	ILE	0	0.022	0.014	19.112	-0.015	-0.015	0.000	0.000	0.000	0.000
19	A	19	GLU	-1	-0.812	-0.881	18.329	-0.252	-0.252	0.000	0.000	0.000	0.000
20	A	20	LEU	0	-0.030	0.002	16.574	-0.043	-0.043	0.000	0.000	0.000	0.000
21	A	21	LEU	0	0.036	0.010	14.901	-0.062	-0.062	0.000	0.000	0.000	0.000
22	A	22	ARG	1	0.761	0.868	13.610	0.277	0.277	0.000	0.000	0.000	0.000
23	A	23	ARG	1	0.823	0.904	13.664	0.222	0.222	0.000	0.000	0.000	0.000
24	A	24	ALA	0	0.027	0.010	12.480	-0.111	-0.111	0.000	0.000	0.000	0.000
25	A	25	ARG	1	0.826	0.904	6.040	-0.246	-0.246	0.000	0.000	0.000	0.000
26	A	26	GLU	-1	-0.897	-0.934	8.983	-0.693	-0.693	0.000	0.000	0.000	0.000
27	A	27	MET	0	-0.080	-0.031	10.320	-0.020	-0.020	0.000	0.000	0.000	0.000
28	A	28	GLY	0	0.008	-0.003	6.124	-0.427	-0.427	0.000	0.000	0.000	0.000
29	A	29	ASP	-1	-0.910	-0.947	2.178	-9.299	-6.875	3.186	-2.514	-3.096	-0.026
30	A	30	TYR	0	-0.024	-0.027	3.133	0.667	2.261	1.192	-0.654	-2.132	-0.003
31	A	31	LEU	0	-0.040	-0.013	4.753	-1.127	-1.099	0.000	-0.025	-0.002	0.000
32	A	32	ILE	0	-0.016	-0.008	7.446	0.346	0.346	0.000	0.000	0.000	0.000
33	A	33	VAL	0	0.003	-0.013	10.085	-0.241	-0.241	0.000	0.000	0.000	0.000
34	A	34	ALA	0	0.010	0.000	13.799	0.091	0.091	0.000	0.000	0.000	0.000
35	A	35	LEU	0	-0.023	0.004	16.193	-0.053	-0.053	0.000	0.000	0.000	0.000
36	A	36	SER	0	-0.022	-0.026	19.296	0.010	0.010	0.000	0.000	0.000	0.000
37	A	37	THR	0	0.011	-0.012	22.566	0.006	0.006	0.000	0.000	0.000	0.000
38	A	38	ASP	-1	-0.740	-0.863	24.676	0.058	0.058	0.000	0.000	0.000	0.000
39	A	39	GLU	-1	-0.869	-0.916	27.631	0.066	0.066	0.000	0.000	0.000	0.000
40	A	40	PHE	0	0.024	0.010	23.635	-0.012	-0.012	0.000	0.000	0.000	0.000
41	A	41	ASN	0	0.004	-0.014	26.836	-0.029	-0.029	0.000	0.000	0.000	0.000
42	A	42	GLN	0	0.006	0.009	28.021	-0.007	-0.007	0.000	0.000	0.000	0.000
43	A	43	ILE	0	0.017	0.024	29.224	-0.009	-0.009	0.000	0.000	0.000	0.000
44	A	44	LYS	1	0.835	0.956	24.296	0.025	0.025	0.000	0.000	0.000	0.000
45	A	45	HIS	0	-0.120	-0.076	29.832	-0.006	-0.006	0.000	0.000	0.000	0.000
46	A	46	LYS	1	0.827	0.912	29.245	0.043	0.043	0.000	0.000	0.000	0.000
47	A	47	LYS	1	0.965	0.978	32.099	-0.006	-0.006	0.000	0.000	0.000	0.000
48	A	48	SER	0	-0.010	0.006	28.355	-0.005	-0.005	0.000	0.000	0.000	0.000
49	A	49	TYR	0	-0.067	-0.026	30.465	0.001	0.001	0.000	0.000	0.000	0.000
50	A	50	TYR	0	-0.034	-0.016	27.562	0.006	0.006	0.000	0.000	0.000	0.000
51	A	51	ASP	-1	-0.819	-0.889	27.488	0.108	0.108	0.000	0.000	0.000	0.000
52	A	52	TYR	0	0.016	-0.031	19.095	0.013	0.013	0.000	0.000	0.000	0.000
53	A	53	GLU	-1	-0.881	-0.940	22.691	0.251	0.251	0.000	0.000	0.000	0.000
54	A	54	GLN	0	-0.072	-0.055	23.111	0.012	0.012	0.000	0.000	0.000	0.000
55	A	55	ARG	1	0.702	0.838	22.995	-0.060	-0.060	0.000	0.000	0.000	0.000
56	A	56	LYS	1	0.896	0.934	17.071	-0.391	-0.391	0.000	0.000	0.000	0.000
57	A	57	MET	0	-0.026	-0.013	18.904	0.029	0.029	0.000	0.000	0.000	0.000
58	A	58	MET	0	-0.026	-0.001	20.091	0.014	0.014	0.000	0.000	0.000	0.000
59	A	59	LEU	0	0.014	0.014	16.827	-0.005	-0.005	0.000	0.000	0.000	0.000
60	A	60	GLU	-1	-0.818	-0.911	15.218	0.477	0.477	0.000	0.000	0.000	0.000
61	A	61	SER	0	-0.115	-0.047	15.632	0.024	0.024	0.000	0.000	0.000	0.000
62	A	62	ILE	0	-0.064	-0.039	16.162	-0.043	-0.043	0.000	0.000	0.000	0.000
63	A	63	ARG	1	0.957	0.962	14.284	-0.081	-0.081	0.000	0.000	0.000	0.000
64	A	64	TYR	0	-0.022	-0.021	12.165	0.036	0.036	0.000	0.000	0.000	0.000
65	A	65	VAL	0	0.007	0.011	11.040	-0.045	-0.045	0.000	0.000	0.000	0.000
66	A	66	ASP	-1	-0.795	-0.870	6.972	1.322	1.322	0.000	0.000	0.000	0.000
67	A	67	LEU	0	-0.027	-0.010	8.989	0.156	0.156	0.000	0.000	0.000	0.000
68	A	68	VAL	0	-0.004	0.012	10.822	-0.186	-0.186	0.000	0.000	0.000	0.000
69	A	69	ILE	0	-0.004	0.005	12.766	0.043	0.043	0.000	0.000	0.000	0.000
70	A	70	PRO	0	-0.042	-0.017	15.600	-0.067	-0.067	0.000	0.000	0.000	0.000
71	A	71	GLU	-1	-0.770	-0.883	19.131	-0.080	-0.080	0.000	0.000	0.000	0.000
72	A	72	LYS	1	0.938	0.932	20.375	-0.114	-0.114	0.000	0.000	0.000	0.000
73	A	73	GLY	0	-0.006	-0.009	22.862	-0.002	-0.002	0.000	0.000	0.000	0.000
74	A	74	TRP	0	0.027	-0.004	22.835	-0.005	-0.005	0.000	0.000	0.000	0.000
75	A	75	GLY	0	-0.015	0.008	23.075	-0.024	-0.024	0.000	0.000	0.000	0.000
76	A	76	GLN	0	-0.021	-0.020	17.884	0.013	0.013	0.000	0.000	0.000	0.000
77	A	77	LYS	1	0.869	0.967	17.213	0.175	0.175	0.000	0.000	0.000	0.000
78	A	78	GLU	-1	-0.840	-0.917	16.371	-0.292	-0.292	0.000	0.000	0.000	0.000
79	A	79	ASP	-1	-0.913	-0.950	16.513	-0.036	-0.036	0.000	0.000	0.000	0.000
80	A	80	ASP	-1	-0.793	-0.866	14.044	0.034	0.034	0.000	0.000	0.000	0.000
81	A	81	VAL	0	-0.011	-0.026	12.043	0.048	0.048	0.000	0.000	0.000	0.000
82	A	82	GLU	-1	-0.911	-0.932	11.270	-0.552	-0.552	0.000	0.000	0.000	0.000
83	A	83	LYS	1	0.833	0.913	11.683	-0.077	-0.077	0.000	0.000	0.000	0.000
84	A	84	PHE	0	-0.106	-0.072	9.465	0.221	0.221	0.000	0.000	0.000	0.000
85	A	85	ASP	-1	-0.840	-0.897	5.013	-1.430	-1.386	-0.001	-0.004	-0.039	0.000
86	A	86	VAL	0	-0.041	-0.018	6.528	-0.667	-0.667	0.000	0.000	0.000	0.000
87	A	87	ASP	-1	-0.802	-0.887	5.271	-6.636	-6.636	0.000	0.000	0.000	0.000
88	A	88	VAL	0	-0.061	-0.047	8.316	0.437	0.437	0.000	0.000	0.000	0.000
89	A	89	PHE	0	0.015	-0.001	10.202	0.191	0.191	0.000	0.000	0.000	0.000
90	A	90	VAL	0	-0.001	-0.001	12.211	0.034	0.034	0.000	0.000	0.000	0.000
91	A	91	MET	0	-0.037	0.014	14.722	0.105	0.105	0.000	0.000	0.000	0.000
92	A	92	GLY	0	0.011	-0.001	18.205	-0.025	-0.025	0.000	0.000	0.000	0.000
93	A	93	HIS	0	-0.028	-0.028	21.178	0.006	0.006	0.000	0.000	0.000	0.000
94	A	94	ASP	-1	-0.925	-0.962	23.782	-0.172	-0.172	0.000	0.000	0.000	0.000
95	A	95	TRP	0	-0.050	-0.030	22.164	0.025	0.025	0.000	0.000	0.000	0.000
96	A	96	GLU	-1	-0.901	-0.950	23.449	-0.313	-0.313	0.000	0.000	0.000	0.000
97	A	97	GLY	0	-0.029	-0.011	23.624	0.025	0.025	0.000	0.000	0.000	0.000
98	A	98	GLU	-1	-0.973	-0.982	24.131	-0.181	-0.181	0.000	0.000	0.000	0.000
99	A	99	PHE	0	-0.015	-0.035	19.910	0.023	0.023	0.000	0.000	0.000	0.000
100	A	100	ASP	-1	-0.751	-0.852	20.342	-0.446	-0.446	0.000	0.000	0.000	0.000
101	A	101	PHE	0	-0.047	-0.013	21.300	-0.033	-0.033	0.000	0.000	0.000	0.000
102	A	102	LEU	0	0.043	0.019	16.639	0.008	0.008	0.000	0.000	0.000	0.000
103	A	103	LYS	1	0.812	0.899	17.115	0.407	0.407	0.000	0.000	0.000	0.000
104	A	104	ASP	-1	-0.890	-0.926	17.213	-0.493	-0.493	0.000	0.000	0.000	0.000
105	A	105	LYS	1	0.767	0.875	15.153	0.395	0.395	0.000	0.000	0.000	0.000
106	A	106	CYS	0	-0.003	0.002	11.901	-0.081	-0.081	0.000	0.000	0.000	0.000
107	A	107	GLU	-1	-0.847	-0.895	11.317	-1.545	-1.545	0.000	0.000	0.000	0.000
108	A	108	VAL	0	-0.025	0.002	13.526	-0.017	-0.017	0.000	0.000	0.000	0.000
109	A	109	ILE	0	-0.030	-0.032	14.347	0.041	0.041	0.000	0.000	0.000	0.000
110	A	110	TYR	0	0.013	-0.006	16.855	0.025	0.025	0.000	0.000	0.000	0.000
111	A	111	LEU	0	-0.050	-0.028	16.074	0.007	0.007	0.000	0.000	0.000	0.000
112	A	112	LYN	0	0.149	0.070	19.263	0.057	0.057	0.000	0.000	0.000	0.000
113	A	113	ARG	1	0.953	0.986	23.319	0.211	0.211	0.000	0.000	0.000	0.000
114	A	114	THR	0	-0.065	-0.048	20.346	-0.003	-0.003	0.000	0.000	0.000	0.000
115	A	115	GLU	-1	-0.903	-0.938	23.742	-0.154	-0.154	0.000	0.000	0.000	0.000

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