FMO DATABASE

FMODB ID: GN1V1

Calculation Name: 1B9L-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1B9L

Chain ID: A

ChEMBL ID:

UniProt ID: P0AC19

Base Structure: X-ray

Registration Date: 2023-06-20

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	119
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1006493.943522
FMO2-HF: Nuclear repulsion	958409.231658
FMO2-HF: Total energy	-48084.711863
FMO2-MP2: Total energy	-48228.152833

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:2:ALA)

Summations of interaction energy for fragment #1(A:2:ALA)

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.
0.253	2.536	-0.007	-1.067	-1.209	0.004

Interaction energy analysis for fragmet #1(A:2:ALA)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.042 / q_NPA : 0.019

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	4	PRO	0	0.005	0.001	3.710	-0.228	1.952	-0.006	-1.060	-1.114	0.004
4	A	5	ALA	0	0.011	0.018	5.009	0.296	0.399	-0.001	-0.007	-0.095	0.000
5	A	6	ALA	0	0.004	0.013	8.138	0.055	0.055	0.000	0.000	0.000	0.000
6	A	7	ILE	0	-0.035	-0.027	9.466	-0.025	-0.025	0.000	0.000	0.000	0.000
7	A	8	ILE	0	-0.002	0.011	12.727	0.063	0.063	0.000	0.000	0.000	0.000
8	A	9	ARG	1	0.919	0.942	14.643	0.178	0.178	0.000	0.000	0.000	0.000
9	A	10	ILE	0	-0.021	0.006	19.070	0.025	0.025	0.000	0.000	0.000	0.000
10	A	11	LYS	1	0.951	0.969	19.553	0.009	0.009	0.000	0.000	0.000	0.000
11	A	12	ASN	0	-0.010	-0.020	24.422	0.005	0.005	0.000	0.000	0.000	0.000
12	A	13	LEU	0	0.024	0.021	27.924	0.009	0.009	0.000	0.000	0.000	0.000
13	A	14	ARG	1	0.926	0.970	29.558	0.024	0.024	0.000	0.000	0.000	0.000
14	A	15	LEU	0	-0.001	0.005	32.192	0.004	0.004	0.000	0.000	0.000	0.000
15	A	16	ARG	1	0.805	0.860	35.506	0.023	0.023	0.000	0.000	0.000	0.000
16	A	17	THR	0	0.033	0.012	37.752	0.002	0.002	0.000	0.000	0.000	0.000
17	A	18	PHE	0	-0.005	0.002	40.366	0.000	0.000	0.000	0.000	0.000	0.000
18	A	19	ILE	0	0.027	0.008	37.647	-0.003	-0.003	0.000	0.000	0.000	0.000
19	A	20	GLY	0	0.004	0.013	41.758	0.001	0.001	0.000	0.000	0.000	0.000
20	A	21	ILE	0	-0.017	-0.031	44.202	0.001	0.001	0.000	0.000	0.000	0.000
21	A	22	LYS	1	0.871	0.944	46.066	0.048	0.048	0.000	0.000	0.000	0.000
22	A	23	GLU	-1	-0.814	-0.922	49.755	-0.030	-0.030	0.000	0.000	0.000	0.000
23	A	24	GLU	-1	-0.940	-0.957	48.982	-0.030	-0.030	0.000	0.000	0.000	0.000
24	A	25	GLU	-1	-0.798	-0.901	44.895	-0.047	-0.047	0.000	0.000	0.000	0.000
25	A	26	ILE	0	-0.022	0.002	46.207	-0.001	-0.001	0.000	0.000	0.000	0.000
26	A	27	ASN	0	-0.019	-0.021	48.361	0.002	0.002	0.000	0.000	0.000	0.000
27	A	28	ASN	0	-0.042	-0.018	47.433	0.003	0.003	0.000	0.000	0.000	0.000
28	A	29	ARG	1	0.748	0.875	40.459	0.028	0.028	0.000	0.000	0.000	0.000
29	A	30	GLN	0	0.003	-0.001	41.375	0.000	0.000	0.000	0.000	0.000	0.000
30	A	31	ASP	-1	-0.810	-0.868	38.123	-0.029	-0.029	0.000	0.000	0.000	0.000
31	A	32	ILE	0	0.011	0.008	34.189	-0.004	-0.004	0.000	0.000	0.000	0.000
32	A	33	VAL	0	-0.042	-0.027	29.799	0.007	0.007	0.000	0.000	0.000	0.000
33	A	34	ILE	0	0.015	0.023	27.253	-0.007	-0.007	0.000	0.000	0.000	0.000
34	A	35	ASN	0	-0.007	-0.007	24.257	0.013	0.013	0.000	0.000	0.000	0.000
35	A	36	VAL	0	0.023	0.013	21.534	-0.008	-0.008	0.000	0.000	0.000	0.000
36	A	37	THR	0	-0.047	-0.036	16.801	0.016	0.016	0.000	0.000	0.000	0.000
37	A	38	ILE	0	0.025	0.012	16.695	-0.010	-0.010	0.000	0.000	0.000	0.000
38	A	39	HIS	0	-0.009	-0.006	12.418	-0.046	-0.046	0.000	0.000	0.000	0.000
39	A	40	TYR	0	0.018	-0.002	11.941	0.037	0.037	0.000	0.000	0.000	0.000
40	A	41	PRO	0	0.021	0.013	9.382	-0.052	-0.052	0.000	0.000	0.000	0.000
41	A	42	ALA	0	0.014	-0.003	5.438	0.122	0.122	0.000	0.000	0.000	0.000
42	A	43	ASP	-1	-0.859	-0.927	7.520	-0.068	-0.068	0.000	0.000	0.000	0.000
43	A	44	LYS	1	0.983	0.990	8.677	0.269	0.269	0.000	0.000	0.000	0.000
44	A	45	ALA	0	-0.051	-0.019	9.788	0.033	0.033	0.000	0.000	0.000	0.000
45	A	46	ARG	1	0.831	0.912	8.069	-0.298	-0.298	0.000	0.000	0.000	0.000
46	A	47	THR	0	0.057	0.027	11.958	0.012	0.012	0.000	0.000	0.000	0.000
47	A	48	SER	0	-0.030	-0.018	14.660	-0.028	-0.028	0.000	0.000	0.000	0.000
48	A	49	GLU	-1	-0.994	-0.981	16.690	0.207	0.207	0.000	0.000	0.000	0.000
49	A	50	ASP	-1	-0.952	-0.965	17.697	0.102	0.102	0.000	0.000	0.000	0.000
50	A	51	ILE	0	-0.029	-0.016	16.722	-0.019	-0.019	0.000	0.000	0.000	0.000
51	A	52	ASN	0	-0.014	-0.014	20.460	0.007	0.007	0.000	0.000	0.000	0.000
52	A	53	ASP	-1	-0.924	-0.949	21.281	-0.032	-0.032	0.000	0.000	0.000	0.000
53	A	54	ALA	0	0.028	0.000	18.592	-0.019	-0.019	0.000	0.000	0.000	0.000
54	A	55	LEU	0	-0.013	0.008	16.257	-0.006	-0.006	0.000	0.000	0.000	0.000
55	A	56	ASN	0	0.011	-0.006	19.035	0.010	0.010	0.000	0.000	0.000	0.000
56	A	57	TYR	0	0.093	0.034	19.615	-0.004	-0.004	0.000	0.000	0.000	0.000
57	A	58	ARG	1	0.939	0.984	21.941	-0.027	-0.027	0.000	0.000	0.000	0.000
58	A	59	THR	0	0.012	0.007	25.235	0.002	0.002	0.000	0.000	0.000	0.000
59	A	60	VAL	0	0.042	0.033	22.310	-0.001	-0.001	0.000	0.000	0.000	0.000
60	A	61	THR	0	-0.006	-0.023	24.971	-0.002	-0.002	0.000	0.000	0.000	0.000
61	A	62	LYS	1	0.863	0.936	27.192	0.033	0.033	0.000	0.000	0.000	0.000
62	A	63	ASN	0	-0.054	-0.033	28.603	0.010	0.010	0.000	0.000	0.000	0.000
63	A	64	ILE	0	0.040	0.029	25.889	0.000	0.000	0.000	0.000	0.000	0.000
64	A	65	ILE	0	0.006	-0.004	30.313	0.001	0.001	0.000	0.000	0.000	0.000
65	A	66	GLN	0	-0.015	0.000	33.001	0.002	0.002	0.000	0.000	0.000	0.000
66	A	67	HIS	0	-0.012	-0.009	33.405	0.005	0.005	0.000	0.000	0.000	0.000
67	A	68	VAL	0	0.029	0.019	32.779	0.001	0.001	0.000	0.000	0.000	0.000
68	A	69	GLU	-1	-0.813	-0.900	35.749	-0.030	-0.030	0.000	0.000	0.000	0.000
69	A	70	ASN	0	-0.087	-0.048	38.142	0.005	0.005	0.000	0.000	0.000	0.000
70	A	71	ASN	0	-0.020	-0.010	38.045	0.000	0.000	0.000	0.000	0.000	0.000
71	A	72	ARG	1	0.836	0.908	40.997	0.037	0.037	0.000	0.000	0.000	0.000
72	A	73	PHE	0	-0.013	0.011	36.574	-0.002	-0.002	0.000	0.000	0.000	0.000
73	A	74	SER	0	0.012	0.006	40.864	0.000	0.000	0.000	0.000	0.000	0.000
74	A	75	LEU	0	-0.007	-0.009	38.918	0.001	0.001	0.000	0.000	0.000	0.000
75	A	76	LEU	0	0.058	0.029	34.084	0.000	0.000	0.000	0.000	0.000	0.000
76	A	77	GLU	-1	-0.840	-0.926	34.188	-0.085	-0.085	0.000	0.000	0.000	0.000
77	A	78	LYS	1	0.913	0.958	33.731	0.076	0.076	0.000	0.000	0.000	0.000
78	A	79	LEU	0	0.035	0.036	33.743	-0.003	-0.003	0.000	0.000	0.000	0.000
79	A	80	THR	0	0.000	-0.027	29.133	-0.001	-0.001	0.000	0.000	0.000	0.000
80	A	81	GLN	0	-0.040	-0.033	28.746	-0.012	-0.012	0.000	0.000	0.000	0.000
81	A	82	ASP	-1	-0.816	-0.904	29.785	-0.082	-0.082	0.000	0.000	0.000	0.000
82	A	83	VAL	0	-0.010	-0.015	27.441	0.000	0.000	0.000	0.000	0.000	0.000
83	A	84	LEU	0	-0.043	-0.013	23.635	-0.005	-0.005	0.000	0.000	0.000	0.000
84	A	85	ASP	-1	-0.808	-0.890	25.264	-0.138	-0.138	0.000	0.000	0.000	0.000
85	A	86	ILE	0	-0.015	-0.003	26.418	-0.001	-0.001	0.000	0.000	0.000	0.000
86	A	87	ALA	0	-0.064	-0.033	22.661	0.002	0.002	0.000	0.000	0.000	0.000
87	A	88	ARG	1	0.788	0.869	21.622	0.139	0.139	0.000	0.000	0.000	0.000
88	A	89	GLU	-1	-0.876	-0.919	22.674	-0.079	-0.079	0.000	0.000	0.000	0.000
89	A	90	HIS	0	-0.006	0.000	18.819	-0.014	-0.014	0.000	0.000	0.000	0.000
90	A	91	HIS	0	0.055	0.023	20.504	-0.031	-0.031	0.000	0.000	0.000	0.000
91	A	92	TRP	0	-0.045	-0.029	15.039	-0.026	-0.026	0.000	0.000	0.000	0.000
92	A	93	VAL	0	-0.034	-0.011	15.468	-0.049	-0.049	0.000	0.000	0.000	0.000
93	A	94	THR	0	-0.017	-0.016	12.980	-0.018	-0.018	0.000	0.000	0.000	0.000
94	A	95	TYR	0	-0.081	-0.076	15.681	-0.031	-0.031	0.000	0.000	0.000	0.000
95	A	96	ALA	0	0.005	0.019	17.303	0.014	0.014	0.000	0.000	0.000	0.000
96	A	97	GLU	-1	-0.795	-0.885	19.989	-0.263	-0.263	0.000	0.000	0.000	0.000
97	A	98	VAL	0	-0.033	-0.007	21.932	0.011	0.011	0.000	0.000	0.000	0.000
98	A	99	GLU	-1	-0.822	-0.886	25.071	-0.124	-0.124	0.000	0.000	0.000	0.000
99	A	100	ILE	0	-0.030	-0.024	27.306	0.009	0.009	0.000	0.000	0.000	0.000
100	A	101	ASP	-1	-0.817	-0.879	30.813	-0.074	-0.074	0.000	0.000	0.000	0.000
101	A	102	LYS	1	0.827	0.909	33.030	0.054	0.054	0.000	0.000	0.000	0.000
102	A	103	LEU	0	-0.001	-0.028	34.585	-0.001	-0.001	0.000	0.000	0.000	0.000
103	A	104	HIS	0	-0.022	-0.021	37.992	0.001	0.001	0.000	0.000	0.000	0.000
104	A	105	ALA	0	-0.033	0.002	39.401	0.002	0.002	0.000	0.000	0.000	0.000
105	A	106	LEU	0	-0.021	-0.005	39.884	0.000	0.000	0.000	0.000	0.000	0.000
106	A	107	ARG	1	0.934	0.961	42.619	0.034	0.034	0.000	0.000	0.000	0.000
107	A	108	TYR	0	-0.019	-0.030	44.012	0.000	0.000	0.000	0.000	0.000	0.000
108	A	109	ALA	0	0.032	0.029	38.754	-0.001	-0.001	0.000	0.000	0.000	0.000
109	A	110	ASP	-1	-0.888	-0.940	36.074	-0.041	-0.041	0.000	0.000	0.000	0.000
110	A	111	SER	0	-0.099	-0.069	33.483	0.003	0.003	0.000	0.000	0.000	0.000
111	A	112	VAL	0	-0.018	0.007	35.370	-0.001	-0.001	0.000	0.000	0.000	0.000
112	A	113	SER	0	-0.023	-0.018	29.750	0.004	0.004	0.000	0.000	0.000	0.000
113	A	114	MET	0	-0.023	0.000	31.028	0.000	0.000	0.000	0.000	0.000	0.000
114	A	115	THR	0	0.014	-0.007	25.486	0.004	0.004	0.000	0.000	0.000	0.000
115	A	116	LEU	0	-0.031	-0.003	26.870	-0.004	-0.004	0.000	0.000	0.000	0.000
116	A	117	SER	0	0.000	-0.010	21.579	0.002	0.002	0.000	0.000	0.000	0.000
117	A	118	TRP	0	0.009	0.009	20.081	0.002	0.002	0.000	0.000	0.000	0.000
118	A	119	GLN	0	0.025	0.003	15.865	-0.016	-0.016	0.000	0.000	0.000	0.000
119	A	120	ARG	1	0.932	0.985	18.019	0.344	0.344	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:ALA)