FMO DATABASE

FMODB ID: M99YZ

Calculation Name: 8I1B-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 8I1B

Chain ID: A

ChEMBL ID:

UniProt ID: P10749

Base Structure: X-ray

Registration Date: 2023-09-27

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	146
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1435982.948424
FMO2-HF: Nuclear repulsion	1377220.319118
FMO2-HF: Total energy	-58762.629306
FMO2-MP2: Total energy	-58934.092657

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:5:GLN)

Summations of interaction energy for fragment #1(A:5:GLN)

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.
-15.038	-5.89	7.214	-6.684	-9.677	-0.002

Interaction energy analysis for fragmet #1(A:5:GLN)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.016 / 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

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	7	HIS	0	0.020	0.006	3.134	0.933	3.614	0.130	-1.074	-1.737	0.005
4	A	8	TYR	0	0.031	0.008	5.867	-0.432	-0.432	0.000	0.000	0.000	0.000
5	A	9	ARG	1	0.923	0.975	9.264	0.532	0.532	0.000	0.000	0.000	0.000
6	A	10	LEU	0	-0.015	-0.009	11.934	-0.113	-0.113	0.000	0.000	0.000	0.000
7	A	11	ARG	1	0.864	0.914	14.773	0.042	0.042	0.000	0.000	0.000	0.000
8	A	12	ASP	-1	-0.685	-0.807	18.542	0.224	0.224	0.000	0.000	0.000	0.000
9	A	13	GLU	-1	-0.891	-0.960	20.980	0.093	0.093	0.000	0.000	0.000	0.000
10	A	14	GLN	0	-0.085	-0.052	23.533	-0.021	-0.021	0.000	0.000	0.000	0.000
11	A	15	GLN	0	-0.035	-0.023	22.670	-0.008	-0.008	0.000	0.000	0.000	0.000
12	A	16	LYS	1	0.795	0.920	23.085	-0.244	-0.244	0.000	0.000	0.000	0.000
13	A	17	SER	0	-0.006	-0.018	19.190	-0.006	-0.006	0.000	0.000	0.000	0.000
14	A	18	LEU	0	-0.001	0.002	15.595	0.019	0.019	0.000	0.000	0.000	0.000
15	A	19	VAL	0	0.039	0.013	17.005	-0.008	-0.008	0.000	0.000	0.000	0.000
16	A	20	LEU	0	-0.017	-0.012	14.219	0.080	0.080	0.000	0.000	0.000	0.000
17	A	21	SER	0	-0.014	-0.016	17.334	-0.089	-0.089	0.000	0.000	0.000	0.000
18	A	22	ASP	-1	-0.886	-0.970	20.083	0.446	0.446	0.000	0.000	0.000	0.000
19	A	23	PRO	0	-0.027	0.012	20.537	0.037	0.037	0.000	0.000	0.000	0.000
20	A	24	TYR	0	-0.073	-0.036	15.450	0.014	0.014	0.000	0.000	0.000	0.000
21	A	25	GLU	-1	-0.790	-0.886	17.977	0.540	0.540	0.000	0.000	0.000	0.000
22	A	26	LEU	0	-0.001	0.005	13.602	0.010	0.010	0.000	0.000	0.000	0.000
23	A	27	LYS	1	0.840	0.924	17.962	-0.462	-0.462	0.000	0.000	0.000	0.000
24	A	28	ALA	0	0.025	0.019	19.942	0.026	0.026	0.000	0.000	0.000	0.000
25	A	29	LEU	0	-0.045	-0.039	21.950	-0.017	-0.017	0.000	0.000	0.000	0.000
26	A	30	HIS	0	0.008	0.001	23.486	0.005	0.005	0.000	0.000	0.000	0.000
27	A	31	LEU	0	-0.034	0.003	20.838	-0.001	-0.001	0.000	0.000	0.000	0.000
28	A	32	ASN	0	0.032	-0.002	24.664	-0.010	-0.010	0.000	0.000	0.000	0.000
29	A	33	GLY	0	0.041	0.007	23.663	0.003	0.003	0.000	0.000	0.000	0.000
30	A	34	GLN	0	0.000	0.000	23.560	-0.006	-0.006	0.000	0.000	0.000	0.000
31	A	35	ASN	0	-0.039	-0.009	23.602	0.001	0.001	0.000	0.000	0.000	0.000
32	A	36	ILE	0	0.064	0.037	17.959	0.033	0.033	0.000	0.000	0.000	0.000
33	A	37	ASN	0	-0.084	-0.066	18.009	0.050	0.050	0.000	0.000	0.000	0.000
34	A	38	GLN	0	0.023	0.006	17.507	0.051	0.051	0.000	0.000	0.000	0.000
35	A	39	GLN	0	-0.031	0.006	15.465	-0.001	-0.001	0.000	0.000	0.000	0.000
36	A	40	VAL	0	-0.031	-0.007	11.469	-0.033	-0.033	0.000	0.000	0.000	0.000
37	A	41	ILE	0	-0.070	-0.026	7.734	-0.157	-0.157	0.000	0.000	0.000	0.000
38	A	42	PHE	0	0.041	0.007	7.832	0.432	0.432	0.000	0.000	0.000	0.000
39	A	43	SER	0	-0.056	-0.037	2.534	-2.918	-1.519	0.974	-0.843	-1.531	0.007
40	A	44	MET	0	0.027	0.033	4.052	1.984	2.602	0.001	-0.099	-0.519	0.000
41	A	45	SER	0	-0.016	-0.024	2.247	-6.252	-4.643	4.738	-3.275	-3.072	-0.028
42	A	46	PHE	0	0.023	0.017	3.897	-0.182	-0.004	0.007	-0.082	-0.103	0.000
43	A	47	VAL	0	-0.031	-0.016	7.255	0.525	0.525	0.000	0.000	0.000	0.000
44	A	48	GLN	0	-0.058	-0.034	9.792	-0.268	-0.268	0.000	0.000	0.000	0.000
45	A	49	GLY	0	0.071	0.034	13.210	0.112	0.112	0.000	0.000	0.000	0.000
46	A	50	GLU	-1	-0.990	-0.995	15.481	0.491	0.491	0.000	0.000	0.000	0.000
47	A	51	PRO	0	-0.060	-0.059	18.069	0.001	0.001	0.000	0.000	0.000	0.000
48	A	52	SER	0	0.024	0.025	19.053	0.030	0.030	0.000	0.000	0.000	0.000
49	A	53	ASN	0	-0.074	-0.031	20.043	0.041	0.041	0.000	0.000	0.000	0.000
50	A	54	ASP	-1	-0.848	-0.921	19.092	0.063	0.063	0.000	0.000	0.000	0.000
51	A	55	LYS	1	0.887	0.922	16.470	-0.357	-0.357	0.000	0.000	0.000	0.000
52	A	56	ILE	0	-0.050	-0.011	10.538	-0.024	-0.024	0.000	0.000	0.000	0.000
53	A	57	PRO	0	0.020	0.037	12.213	0.058	0.058	0.000	0.000	0.000	0.000
54	A	58	VAL	0	-0.033	-0.040	7.407	-0.032	-0.032	0.000	0.000	0.000	0.000
55	A	59	ALA	0	0.038	0.035	6.363	-0.113	-0.113	0.000	0.000	0.000	0.000
56	A	60	LEU	0	-0.011	-0.014	6.381	0.483	0.483	0.000	0.000	0.000	0.000
57	A	61	GLY	0	0.053	0.006	5.067	-0.586	-0.501	-0.001	-0.001	-0.083	0.000
58	A	62	LEU	0	-0.009	0.005	5.981	-1.003	-1.003	0.000	0.000	0.000	0.000
59	A	63	LYS	1	0.999	0.995	5.658	0.835	0.835	0.000	0.000	0.000	0.000
60	A	64	GLY	0	-0.082	-0.050	5.486	-0.643	-0.643	0.000	0.000	0.000	0.000
61	A	65	LYS	1	0.934	0.971	6.607	-1.587	-1.587	0.000	0.000	0.000	0.000
62	A	66	ASN	0	-0.027	-0.002	6.457	1.102	1.102	0.000	0.000	0.000	0.000
63	A	67	LEU	0	0.019	0.004	8.000	-0.489	-0.489	0.000	0.000	0.000	0.000
64	A	68	TYR	0	0.000	-0.005	2.731	-4.372	-3.054	0.162	-0.627	-0.852	0.008
65	A	69	LEU	0	0.019	0.028	9.040	-0.549	-0.549	0.000	0.000	0.000	0.000
66	A	70	SER	0	-0.062	-0.051	11.779	0.135	0.135	0.000	0.000	0.000	0.000
67	A	71	CYS	0	-0.006	0.006	14.423	-0.133	-0.133	0.000	0.000	0.000	0.000
68	A	72	VAL	0	0.007	0.008	17.931	0.015	0.015	0.000	0.000	0.000	0.000
69	A	73	MET	0	0.009	0.018	20.857	-0.016	-0.016	0.000	0.000	0.000	0.000
70	A	74	LYS	1	0.878	0.932	21.222	-0.663	-0.663	0.000	0.000	0.000	0.000
71	A	75	ASP	-1	-0.857	-0.928	25.861	0.390	0.390	0.000	0.000	0.000	0.000
72	A	76	GLY	0	-0.041	-0.023	29.335	-0.017	-0.017	0.000	0.000	0.000	0.000
73	A	77	THR	0	0.005	0.008	26.603	-0.031	-0.031	0.000	0.000	0.000	0.000
74	A	78	PRO	0	0.017	0.018	23.342	0.033	0.033	0.000	0.000	0.000	0.000
75	A	79	THR	0	-0.035	-0.020	21.224	-0.029	-0.029	0.000	0.000	0.000	0.000
76	A	80	LEU	0	-0.013	0.007	15.287	0.069	0.069	0.000	0.000	0.000	0.000
77	A	81	GLN	0	-0.035	-0.038	16.207	-0.192	-0.192	0.000	0.000	0.000	0.000
78	A	82	LEU	0	0.008	0.011	11.918	0.204	0.204	0.000	0.000	0.000	0.000
79	A	83	GLU	-1	-0.790	-0.856	12.791	1.107	1.107	0.000	0.000	0.000	0.000
80	A	84	SER	0	0.013	-0.010	11.667	0.304	0.304	0.000	0.000	0.000	0.000
81	A	85	VAL	0	-0.006	0.013	8.748	-0.089	-0.089	0.000	0.000	0.000	0.000
82	A	86	ASP	-1	-0.776	-0.886	11.360	0.664	0.664	0.000	0.000	0.000	0.000
83	A	87	PRO	0	0.014	-0.018	8.433	0.187	0.187	0.000	0.000	0.000	0.000
84	A	88	LYS	1	0.920	0.969	8.142	-0.270	-0.270	0.000	0.000	0.000	0.000
85	A	89	GLN	0	-0.089	-0.047	10.070	-0.074	-0.074	0.000	0.000	0.000	0.000
86	A	90	TYR	0	-0.088	-0.045	6.877	0.089	0.089	0.000	0.000	0.000	0.000
87	A	91	PRO	0	0.012	0.003	2.716	-2.506	-1.230	1.204	-0.681	-1.799	0.006
88	A	92	LYS	1	0.888	0.931	5.655	-2.636	-2.652	-0.001	-0.002	0.019	0.000
89	A	93	LYS	1	0.975	0.978	7.610	-0.199	-0.199	0.000	0.000	0.000	0.000
90	A	94	LYS	1	0.935	0.973	9.342	-0.612	-0.612	0.000	0.000	0.000	0.000
91	A	95	MET	0	0.011	0.027	7.314	0.051	0.051	0.000	0.000	0.000	0.000
92	A	96	GLU	-1	-0.754	-0.860	11.342	1.292	1.292	0.000	0.000	0.000	0.000
93	A	97	LYS	1	0.908	0.922	13.734	-0.484	-0.484	0.000	0.000	0.000	0.000
94	A	98	ARG	1	0.889	0.932	14.750	-1.206	-1.206	0.000	0.000	0.000	0.000
95	A	99	PHE	0	-0.062	-0.031	10.241	0.024	0.024	0.000	0.000	0.000	0.000
96	A	100	VAL	0	-0.072	-0.028	11.091	0.359	0.359	0.000	0.000	0.000	0.000
97	A	101	PHE	0	0.016	0.016	11.560	-0.213	-0.213	0.000	0.000	0.000	0.000
98	A	102	ASN	0	-0.030	-0.027	12.577	0.078	0.078	0.000	0.000	0.000	0.000
99	A	103	LYS	1	0.852	0.908	10.380	0.048	0.048	0.000	0.000	0.000	0.000
100	A	104	ILE	0	0.019	0.000	13.747	-0.076	-0.076	0.000	0.000	0.000	0.000
101	A	105	GLU	-1	-0.865	-0.906	13.958	-0.229	-0.229	0.000	0.000	0.000	0.000
102	A	106	VAL	0	0.035	0.013	17.956	-0.011	-0.011	0.000	0.000	0.000	0.000
103	A	107	LYS	1	0.925	0.948	21.502	0.017	0.017	0.000	0.000	0.000	0.000
104	A	108	SER	0	-0.001	-0.012	19.686	0.003	0.003	0.000	0.000	0.000	0.000
105	A	109	LYS	1	0.870	0.962	19.098	-0.106	-0.106	0.000	0.000	0.000	0.000
106	A	110	VAL	0	-0.044	-0.029	13.468	-0.021	-0.021	0.000	0.000	0.000	0.000
107	A	111	GLU	-1	-0.799	-0.865	16.875	0.251	0.251	0.000	0.000	0.000	0.000
108	A	112	PHE	0	0.023	-0.015	10.944	0.034	0.034	0.000	0.000	0.000	0.000
109	A	113	GLU	-1	-0.736	-0.834	15.930	0.463	0.463	0.000	0.000	0.000	0.000
110	A	114	SER	0	0.040	0.003	16.771	0.076	0.076	0.000	0.000	0.000	0.000
111	A	115	ALA	0	0.019	-0.006	16.098	-0.092	-0.092	0.000	0.000	0.000	0.000
112	A	116	GLU	-1	-0.906	-0.937	17.936	0.666	0.666	0.000	0.000	0.000	0.000
113	A	117	PHE	0	-0.060	-0.034	19.984	-0.065	-0.065	0.000	0.000	0.000	0.000
114	A	118	PRO	0	0.100	0.044	22.193	-0.003	-0.003	0.000	0.000	0.000	0.000
115	A	119	ASN	0	-0.075	-0.051	23.007	-0.035	-0.035	0.000	0.000	0.000	0.000
116	A	120	TRP	0	-0.004	0.011	22.375	-0.026	-0.026	0.000	0.000	0.000	0.000
117	A	121	TYR	0	0.022	0.007	19.629	0.062	0.062	0.000	0.000	0.000	0.000
118	A	122	ILE	0	-0.048	-0.013	14.211	0.001	0.001	0.000	0.000	0.000	0.000
119	A	123	SER	0	-0.014	-0.014	18.721	-0.079	-0.079	0.000	0.000	0.000	0.000
120	A	124	THR	0	-0.017	-0.034	20.691	0.051	0.051	0.000	0.000	0.000	0.000
121	A	125	SER	0	0.049	0.027	23.213	-0.021	-0.021	0.000	0.000	0.000	0.000
122	A	126	GLN	0	0.016	0.016	26.788	-0.020	-0.020	0.000	0.000	0.000	0.000
123	A	127	ALA	0	-0.059	-0.026	29.532	-0.013	-0.013	0.000	0.000	0.000	0.000
124	A	128	GLU	-1	-0.725	-0.846	27.346	0.194	0.194	0.000	0.000	0.000	0.000
125	A	129	HIS	0	-0.025	-0.032	25.849	0.018	0.018	0.000	0.000	0.000	0.000
126	A	130	LYS	1	0.873	0.947	26.026	-0.245	-0.245	0.000	0.000	0.000	0.000
127	A	131	PRO	0	0.008	-0.012	22.194	0.003	0.003	0.000	0.000	0.000	0.000
128	A	132	VAL	0	-0.024	-0.006	17.369	-0.032	-0.032	0.000	0.000	0.000	0.000
129	A	133	PHE	0	-0.081	-0.041	20.264	0.055	0.055	0.000	0.000	0.000	0.000
130	A	134	LEU	0	0.014	0.005	19.302	0.034	0.034	0.000	0.000	0.000	0.000
131	A	135	GLY	0	0.061	0.033	21.624	-0.035	-0.035	0.000	0.000	0.000	0.000
132	A	136	ASN	0	-0.031	-0.016	24.179	0.028	0.028	0.000	0.000	0.000	0.000
133	A	137	ASN	0	-0.019	-0.005	25.358	-0.029	-0.029	0.000	0.000	0.000	0.000
134	A	138	SER	0	-0.055	-0.018	26.891	-0.031	-0.031	0.000	0.000	0.000	0.000
135	A	139	GLY	0	0.115	0.027	29.603	0.003	0.003	0.000	0.000	0.000	0.000
136	A	141	GLN	0	-0.077	-0.027	30.944	0.013	0.013	0.000	0.000	0.000	0.000
137	A	142	ASP	-1	-0.810	-0.892	25.941	0.314	0.314	0.000	0.000	0.000	0.000
138	A	143	ILE	0	-0.062	-0.020	22.852	-0.028	-0.028	0.000	0.000	0.000	0.000
139	A	144	ILE	0	0.034	-0.001	21.374	0.046	0.046	0.000	0.000	0.000	0.000
140	A	145	ASH	0	-0.114	-0.069	20.145	0.011	0.011	0.000	0.000	0.000	0.000
141	A	146	PHE	0	-0.017	-0.008	16.493	0.019	0.019	0.000	0.000	0.000	0.000
142	A	147	THR	0	0.036	0.032	17.445	-0.058	-0.058	0.000	0.000	0.000	0.000
143	A	148	MET	0	-0.004	-0.002	11.347	0.117	0.117	0.000	0.000	0.000	0.000
144	A	149	GLU	-1	-0.803	-0.871	13.464	-0.266	-0.266	0.000	0.000	0.000	0.000
145	A	150	SER	0	0.013	-0.011	10.243	0.086	0.086	0.000	0.000	0.000	0.000
146	A	151	VAL	0	-0.035	-0.007	9.122	-0.074	-0.074	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:5:GLN)