FMO DATABASE

FMODB ID: 7MM7K

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1441269.33919
FMO2-HF: Nuclear repulsion	1382505.547219
FMO2-HF: Total energy	-58763.79197
FMO2-MP2: Total energy	-58935.120558

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.
-22.171	-12.505	11.787	-9.049	-12.403	0.008

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 : 0.015 / q_NPA : 0.004

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	0.027	0.008	3.187	0.290	3.681	0.160	-1.612	-1.939	0.002
4	A	8	TYR	0	0.045	0.017	5.700	-0.315	-0.315	0.000	0.000	0.000	0.000
5	A	9	ARG	1	0.874	0.949	9.083	0.559	0.559	0.000	0.000	0.000	0.000
6	A	10	LEU	0	0.012	0.002	11.654	-0.075	-0.075	0.000	0.000	0.000	0.000
7	A	11	ARG	1	0.839	0.914	14.334	0.044	0.044	0.000	0.000	0.000	0.000
8	A	12	ASP	-1	-0.662	-0.812	18.173	0.242	0.242	0.000	0.000	0.000	0.000
9	A	13	GLU	-1	-0.898	-0.970	20.662	0.106	0.106	0.000	0.000	0.000	0.000
10	A	14	GLN	0	-0.042	-0.027	23.288	-0.016	-0.016	0.000	0.000	0.000	0.000
11	A	15	GLN	0	-0.036	-0.022	21.594	-0.025	-0.025	0.000	0.000	0.000	0.000
12	A	16	LYS	1	0.775	0.907	22.864	-0.254	-0.254	0.000	0.000	0.000	0.000
13	A	17	SER	0	-0.016	-0.024	19.203	0.010	0.010	0.000	0.000	0.000	0.000
14	A	18	LEU	0	0.010	0.013	15.045	0.023	0.023	0.000	0.000	0.000	0.000
15	A	19	VAL	0	0.029	0.008	16.652	-0.029	-0.029	0.000	0.000	0.000	0.000
16	A	20	LEU	0	-0.030	-0.020	14.005	0.110	0.110	0.000	0.000	0.000	0.000
17	A	21	SER	0	-0.028	-0.018	17.263	-0.108	-0.108	0.000	0.000	0.000	0.000
18	A	22	ASP	-1	-0.863	-0.936	19.395	0.457	0.457	0.000	0.000	0.000	0.000
19	A	23	PRO	0	-0.031	0.000	20.353	0.040	0.040	0.000	0.000	0.000	0.000
20	A	24	TYR	0	-0.053	-0.042	14.951	0.016	0.016	0.000	0.000	0.000	0.000
21	A	25	GLU	-1	-0.788	-0.870	17.119	0.594	0.594	0.000	0.000	0.000	0.000
22	A	26	LEU	0	0.012	0.001	13.075	-0.027	-0.027	0.000	0.000	0.000	0.000
23	A	27	LYS	1	0.821	0.910	17.424	-0.485	-0.485	0.000	0.000	0.000	0.000
24	A	28	ALA	0	0.028	0.011	19.480	0.025	0.025	0.000	0.000	0.000	0.000
25	A	29	LEU	0	-0.019	-0.017	21.835	-0.023	-0.023	0.000	0.000	0.000	0.000
26	A	30	HIS	0	-0.009	-0.015	23.224	0.007	0.007	0.000	0.000	0.000	0.000
27	A	31	LEU	0	-0.051	-0.005	20.259	-0.020	-0.020	0.000	0.000	0.000	0.000
28	A	32	ASN	0	0.056	0.013	24.201	-0.011	-0.011	0.000	0.000	0.000	0.000
29	A	33	GLY	0	0.038	0.003	23.336	-0.001	-0.001	0.000	0.000	0.000	0.000
30	A	34	GLN	0	-0.011	0.000	23.328	-0.006	-0.006	0.000	0.000	0.000	0.000
31	A	35	ASN	0	0.004	0.000	23.211	0.005	0.005	0.000	0.000	0.000	0.000
32	A	36	ILE	0	0.040	0.034	17.733	0.037	0.037	0.000	0.000	0.000	0.000
33	A	37	ASN	0	-0.074	-0.055	17.676	0.036	0.036	0.000	0.000	0.000	0.000
34	A	38	GLN	0	0.033	0.013	17.999	0.049	0.049	0.000	0.000	0.000	0.000
35	A	39	GLN	0	-0.099	-0.041	15.254	-0.010	-0.010	0.000	0.000	0.000	0.000
36	A	40	VAL	0	-0.024	-0.004	11.364	-0.035	-0.035	0.000	0.000	0.000	0.000
37	A	41	ILE	0	-0.051	-0.015	7.941	-0.114	-0.114	0.000	0.000	0.000	0.000
38	A	42	PHE	0	0.054	0.009	7.794	0.344	0.344	0.000	0.000	0.000	0.000
39	A	43	SER	0	-0.049	-0.039	2.358	-2.719	-1.502	1.028	-0.821	-1.424	0.005
40	A	44	MET	0	0.008	0.013	3.307	1.735	2.588	0.018	-0.197	-0.674	-0.001
41	A	45	SER	0	-0.036	-0.029	2.256	-7.372	-4.576	3.653	-3.261	-3.188	-0.025
42	A	46	PHE	0	0.033	0.024	3.849	0.177	0.375	0.010	-0.096	-0.112	-0.001
43	A	47	VAL	0	-0.036	-0.009	7.240	0.494	0.494	0.000	0.000	0.000	0.000
44	A	48	GLN	0	-0.061	-0.047	9.689	-0.226	-0.226	0.000	0.000	0.000	0.000
45	A	49	GLY	0	0.045	0.023	13.225	0.101	0.101	0.000	0.000	0.000	0.000
46	A	50	GLU	-1	-0.930	-0.961	15.554	0.561	0.561	0.000	0.000	0.000	0.000
47	A	51	PRO	0	-0.049	-0.039	18.004	-0.003	-0.003	0.000	0.000	0.000	0.000
48	A	52	SER	0	0.023	0.032	18.892	0.033	0.033	0.000	0.000	0.000	0.000
49	A	53	ASN	0	-0.053	-0.050	19.819	0.007	0.007	0.000	0.000	0.000	0.000
50	A	54	ASP	-1	-0.879	-0.925	19.330	0.091	0.091	0.000	0.000	0.000	0.000
51	A	55	LYS	1	0.799	0.892	16.794	-0.422	-0.422	0.000	0.000	0.000	0.000
52	A	56	ILE	0	-0.025	-0.016	10.975	-0.067	-0.067	0.000	0.000	0.000	0.000
53	A	57	PRO	0	0.033	0.037	12.434	0.073	0.073	0.000	0.000	0.000	0.000
54	A	58	VAL	0	-0.041	-0.043	7.499	-0.067	-0.067	0.000	0.000	0.000	0.000
55	A	59	ALA	0	0.029	0.032	5.773	-0.037	-0.037	0.000	0.000	0.000	0.000
56	A	60	LEU	0	-0.003	-0.010	6.118	0.368	0.368	0.000	0.000	0.000	0.000
57	A	61	GLY	0	0.062	0.026	5.267	-0.173	-0.173	0.000	0.000	0.000	0.000
58	A	62	LEU	0	-0.026	-0.001	6.049	-0.956	-0.956	0.000	0.000	0.000	0.000
59	A	63	LYS	1	0.965	0.989	5.807	1.279	1.279	0.000	0.000	0.000	0.000
60	A	64	GLY	0	-0.051	-0.025	5.191	-0.691	-0.691	0.000	0.000	0.000	0.000
61	A	65	LYS	1	0.954	0.978	6.362	-1.307	-1.307	0.000	0.000	0.000	0.000
62	A	66	ASN	0	-0.019	0.001	6.284	0.974	0.974	0.000	0.000	0.000	0.000
63	A	67	LEU	0	-0.005	-0.010	7.572	-0.359	-0.359	0.000	0.000	0.000	0.000
64	A	68	TYR	0	0.006	-0.019	1.960	-10.115	-10.292	4.684	-2.116	-2.390	0.025
65	A	69	LEU	0	-0.008	0.000	8.339	-0.717	-0.717	0.000	0.000	0.000	0.000
66	A	70	SER	0	-0.043	-0.044	10.965	0.178	0.178	0.000	0.000	0.000	0.000
67	A	71	CYS	0	-0.013	0.030	13.642	-0.181	-0.181	0.000	0.000	0.000	0.000
68	A	72	VAL	0	0.005	-0.007	17.137	-0.012	-0.012	0.000	0.000	0.000	0.000
69	A	73	MET	0	0.005	0.010	20.230	-0.027	-0.027	0.000	0.000	0.000	0.000
70	A	74	LYS	1	0.866	0.921	20.495	-0.711	-0.711	0.000	0.000	0.000	0.000
71	A	75	ASP	-1	-0.878	-0.939	25.355	0.431	0.431	0.000	0.000	0.000	0.000
72	A	76	GLY	0	-0.011	0.003	28.697	-0.024	-0.024	0.000	0.000	0.000	0.000
73	A	77	THR	0	-0.019	-0.015	25.776	-0.029	-0.029	0.000	0.000	0.000	0.000
74	A	78	PRO	0	0.007	0.007	22.707	0.038	0.038	0.000	0.000	0.000	0.000
75	A	79	THR	0	-0.025	0.002	20.685	-0.038	-0.038	0.000	0.000	0.000	0.000
76	A	80	LEU	0	-0.021	-0.003	14.779	0.081	0.081	0.000	0.000	0.000	0.000
77	A	81	GLN	0	-0.010	-0.014	15.670	-0.218	-0.218	0.000	0.000	0.000	0.000
78	A	82	LEU	0	-0.002	0.003	11.178	0.260	0.260	0.000	0.000	0.000	0.000
79	A	83	GLU	-1	-0.771	-0.842	12.092	1.196	1.196	0.000	0.000	0.000	0.000
80	A	84	SER	0	0.003	-0.005	11.218	0.342	0.342	0.000	0.000	0.000	0.000
81	A	85	VAL	0	-0.017	0.002	8.329	-0.126	-0.126	0.000	0.000	0.000	0.000
82	A	86	ASP	-1	-0.773	-0.879	11.185	0.560	0.560	0.000	0.000	0.000	0.000
83	A	87	PRO	0	0.001	-0.015	8.208	0.211	0.211	0.000	0.000	0.000	0.000
84	A	88	LYS	1	0.903	0.947	8.442	-0.357	-0.357	0.000	0.000	0.000	0.000
85	A	89	GLN	0	-0.056	-0.031	10.009	-0.008	-0.008	0.000	0.000	0.000	0.000
86	A	90	TYR	0	-0.056	-0.049	6.532	0.139	0.139	0.000	0.000	0.000	0.000
87	A	91	PRO	0	0.006	0.008	2.506	-2.877	-1.501	2.235	-0.943	-2.668	0.003
88	A	92	LYS	1	0.861	0.925	5.262	-2.942	-2.930	-0.001	-0.003	-0.008	0.000
89	A	93	LYS	1	0.967	0.968	7.351	-0.234	-0.234	0.000	0.000	0.000	0.000
90	A	94	LYS	1	0.920	0.964	8.911	-0.831	-0.831	0.000	0.000	0.000	0.000
91	A	95	MET	0	0.022	0.036	6.821	0.071	0.071	0.000	0.000	0.000	0.000
92	A	96	GLU	-1	-0.772	-0.858	10.668	1.435	1.435	0.000	0.000	0.000	0.000
93	A	97	LYS	1	0.865	0.907	13.288	-0.566	-0.566	0.000	0.000	0.000	0.000
94	A	98	ARG	1	0.930	0.956	14.200	-1.312	-1.312	0.000	0.000	0.000	0.000
95	A	99	PHE	0	-0.061	-0.037	9.654	0.055	0.055	0.000	0.000	0.000	0.000
96	A	100	VAL	0	-0.053	-0.011	10.486	0.402	0.402	0.000	0.000	0.000	0.000
97	A	101	PHE	0	0.011	-0.007	11.097	-0.268	-0.268	0.000	0.000	0.000	0.000
98	A	102	ASN	0	-0.012	-0.019	12.432	0.033	0.033	0.000	0.000	0.000	0.000
99	A	103	LYS	1	0.823	0.899	10.428	-0.089	-0.089	0.000	0.000	0.000	0.000
100	A	104	ILE	0	0.029	0.007	13.775	-0.070	-0.070	0.000	0.000	0.000	0.000
101	A	105	GLU	-1	-0.814	-0.887	14.215	-0.063	-0.063	0.000	0.000	0.000	0.000
102	A	106	VAL	0	0.005	0.005	17.908	-0.008	-0.008	0.000	0.000	0.000	0.000
103	A	107	LYS	1	0.924	0.946	21.563	-0.008	-0.008	0.000	0.000	0.000	0.000
104	A	108	SER	0	0.008	0.002	19.825	0.005	0.005	0.000	0.000	0.000	0.000
105	A	109	LYS	1	0.868	0.962	19.022	-0.144	-0.144	0.000	0.000	0.000	0.000
106	A	110	VAL	0	-0.042	-0.022	13.664	-0.020	-0.020	0.000	0.000	0.000	0.000
107	A	111	GLU	-1	-0.772	-0.854	17.024	0.290	0.290	0.000	0.000	0.000	0.000
108	A	112	PHE	0	0.027	-0.018	11.069	0.040	0.040	0.000	0.000	0.000	0.000
109	A	113	GLU	-1	-0.725	-0.821	16.089	0.546	0.546	0.000	0.000	0.000	0.000
110	A	114	SER	0	0.023	-0.020	16.294	0.095	0.095	0.000	0.000	0.000	0.000
111	A	115	ALA	0	0.018	-0.002	15.528	-0.102	-0.102	0.000	0.000	0.000	0.000
112	A	116	GLU	-1	-0.896	-0.930	17.305	0.774	0.774	0.000	0.000	0.000	0.000
113	A	117	PHE	0	-0.031	-0.021	19.393	-0.075	-0.075	0.000	0.000	0.000	0.000
114	A	118	PRO	0	0.066	0.027	21.712	-0.010	-0.010	0.000	0.000	0.000	0.000
115	A	119	ASN	0	-0.056	-0.039	22.617	-0.048	-0.048	0.000	0.000	0.000	0.000
116	A	120	TRP	0	-0.008	0.008	22.093	-0.024	-0.024	0.000	0.000	0.000	0.000
117	A	121	TYR	0	0.004	0.000	19.292	0.068	0.068	0.000	0.000	0.000	0.000
118	A	122	ILE	0	-0.032	-0.005	13.453	-0.008	-0.008	0.000	0.000	0.000	0.000
119	A	123	SER	0	-0.010	-0.011	18.018	-0.091	-0.091	0.000	0.000	0.000	0.000
120	A	124	THR	0	-0.023	-0.033	20.270	0.052	0.052	0.000	0.000	0.000	0.000
121	A	125	SER	0	0.047	0.020	22.764	-0.022	-0.022	0.000	0.000	0.000	0.000
122	A	126	GLN	0	0.029	0.017	26.297	-0.025	-0.025	0.000	0.000	0.000	0.000
123	A	127	ALA	0	-0.030	-0.015	28.718	-0.010	-0.010	0.000	0.000	0.000	0.000
124	A	128	GLU	-1	-0.733	-0.860	27.061	0.200	0.200	0.000	0.000	0.000	0.000
125	A	129	HIS	0	-0.048	-0.031	25.353	0.021	0.021	0.000	0.000	0.000	0.000
126	A	130	LYS	1	0.862	0.939	25.446	-0.260	-0.260	0.000	0.000	0.000	0.000
127	A	131	PRO	0	0.037	0.006	21.660	0.008	0.008	0.000	0.000	0.000	0.000
128	A	132	VAL	0	-0.033	-0.007	16.710	-0.029	-0.029	0.000	0.000	0.000	0.000
129	A	133	PHE	0	-0.070	-0.033	19.343	0.065	0.065	0.000	0.000	0.000	0.000
130	A	134	LEU	0	0.006	-0.008	18.268	0.039	0.039	0.000	0.000	0.000	0.000
131	A	135	GLY	0	0.063	0.035	20.993	-0.041	-0.041	0.000	0.000	0.000	0.000
132	A	136	ASN	0	-0.039	-0.021	23.626	0.030	0.030	0.000	0.000	0.000	0.000
133	A	137	ASN	0	0.007	-0.005	25.367	-0.027	-0.027	0.000	0.000	0.000	0.000
134	A	138	SER	0	-0.034	-0.012	26.766	-0.039	-0.039	0.000	0.000	0.000	0.000
135	A	139	GLY	0	0.042	0.002	29.672	-0.003	-0.003	0.000	0.000	0.000	0.000
136	A	141	GLN	0	-0.034	-0.040	30.534	-0.008	-0.008	0.000	0.000	0.000	0.000
137	A	142	ASP	-1	-0.834	-0.870	25.460	0.358	0.358	0.000	0.000	0.000	0.000
138	A	143	ILE	0	-0.053	-0.020	22.839	-0.033	-0.033	0.000	0.000	0.000	0.000
139	A	144	ILE	0	0.029	0.021	21.328	0.047	0.047	0.000	0.000	0.000	0.000
140	A	145	ASH	0	-0.107	-0.070	20.109	0.017	0.017	0.000	0.000	0.000	0.000
141	A	146	PHE	0	-0.016	-0.006	16.672	0.006	0.006	0.000	0.000	0.000	0.000
142	A	147	THR	0	-0.003	-0.002	17.575	-0.067	-0.067	0.000	0.000	0.000	0.000
143	A	148	MET	0	-0.015	-0.003	11.834	0.077	0.077	0.000	0.000	0.000	0.000
144	A	149	GLU	-1	-0.775	-0.861	13.103	-0.288	-0.288	0.000	0.000	0.000	0.000
145	A	150	SER	0	-0.004	-0.005	10.250	0.068	0.068	0.000	0.000	0.000	0.000
146	A	151	VAL	0	-0.048	-0.018	8.969	-0.138	-0.138	0.000	0.000	0.000	0.000

Top

Graph

Manual

About

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