FMO DATABASE

FMODB ID: NNQQQ

Calculation Name: 4B9I-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4B9I

Chain ID: A

ChEMBL ID:

UniProt ID: P53508

Base Structure: X-ray

Registration Date: 2023-09-23

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	OptH
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	137
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1213949.244603
FMO2-HF: Nuclear repulsion	1160517.200024
FMO2-HF: Total energy	-53432.044579
FMO2-MP2: Total energy	-53589.911767

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:13:PHE)

Summations of interaction energy for fragment #1(A:13:PHE)

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.
-14.609	-2.981	9.121	-5.255	-15.497	0.004

Interaction energy analysis for fragmet #1(A:13:PHE)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.007 / q_NPA : -0.022

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	15	ALA	0	0.000	0.004	2.532	-1.763	1.330	1.282	-1.477	-2.899	0.007
4	A	16	PRO	0	-0.015	0.001	4.652	-0.800	-0.587	0.002	-0.058	-0.157	0.000
5	A	17	GLU	-1	-0.922	-0.966	7.449	-0.342	-0.342	0.000	0.000	0.000	0.000
6	A	18	PRO	0	-0.025	-0.011	7.744	0.076	0.076	0.000	0.000	0.000	0.000
7	A	19	GLN	0	-0.034	-0.016	10.354	0.005	0.005	0.000	0.000	0.000	0.000
8	A	20	ILE	0	0.045	0.026	14.149	0.000	0.000	0.000	0.000	0.000	0.000
9	A	21	GLN	0	-0.048	-0.021	15.943	0.012	0.012	0.000	0.000	0.000	0.000
10	A	22	PRO	0	0.061	0.028	19.878	-0.006	-0.006	0.000	0.000	0.000	0.000
11	A	23	SER	0	-0.038	-0.014	23.001	0.011	0.011	0.000	0.000	0.000	0.000
12	A	24	PHE	0	0.092	0.029	25.539	-0.001	-0.001	0.000	0.000	0.000	0.000
13	A	25	GLY	0	0.023	0.024	29.265	0.004	0.004	0.000	0.000	0.000	0.000
14	A	26	LYS	1	0.929	0.957	30.906	0.011	0.011	0.000	0.000	0.000	0.000
15	A	27	ASN	0	-0.042	-0.052	28.027	0.001	0.001	0.000	0.000	0.000	0.000
16	A	28	VAL	0	0.049	0.048	27.578	0.000	0.000	0.000	0.000	0.000	0.000
17	A	29	GLY	0	0.050	0.021	29.678	-0.005	-0.005	0.000	0.000	0.000	0.000
18	A	30	LYS	1	0.882	0.959	32.091	0.029	0.029	0.000	0.000	0.000	0.000
19	A	31	GLU	-1	-0.811	-0.904	30.637	-0.045	-0.045	0.000	0.000	0.000	0.000
20	A	32	GLY	0	-0.046	-0.031	27.702	0.004	0.004	0.000	0.000	0.000	0.000
21	A	33	GLY	0	-0.054	-0.022	27.579	0.003	0.003	0.000	0.000	0.000	0.000
22	A	34	LEU	0	-0.082	-0.043	21.801	-0.005	-0.005	0.000	0.000	0.000	0.000
23	A	35	LEU	0	0.010	0.001	23.098	0.004	0.004	0.000	0.000	0.000	0.000
24	A	36	PHE	0	0.009	0.004	16.674	0.003	0.003	0.000	0.000	0.000	0.000
25	A	37	SER	0	-0.008	-0.006	18.161	0.002	0.002	0.000	0.000	0.000	0.000
26	A	38	VAL	0	0.033	0.025	11.773	-0.005	-0.005	0.000	0.000	0.000	0.000
27	A	39	SER	0	-0.011	0.012	13.622	0.008	0.008	0.000	0.000	0.000	0.000
28	A	40	LEU	0	-0.005	-0.001	7.230	-0.020	-0.020	0.000	0.000	0.000	0.000
29	A	41	THR	0	0.035	0.022	8.731	-0.020	-0.020	0.000	0.000	0.000	0.000
30	A	42	VAL	0	-0.031	0.003	6.144	-0.032	-0.032	0.000	0.000	0.000	0.000
31	A	43	PRO	0	0.009	0.015	2.175	-0.791	-0.094	1.688	-0.548	-1.838	0.002
32	A	44	GLU	-1	-0.857	-0.943	4.554	1.252	1.430	-0.001	-0.018	-0.159	0.000
33	A	45	ASN	0	-0.075	-0.047	3.613	-1.859	-1.032	0.007	-0.234	-0.600	-0.001
34	A	46	VAL	0	-0.015	0.006	2.279	-1.106	-0.551	1.059	-0.336	-1.278	-0.004
35	A	47	SER	0	0.032	0.019	5.525	0.055	0.055	0.000	0.000	0.000	0.000
36	A	48	GLN	0	0.052	0.027	7.599	-0.037	-0.037	0.000	0.000	0.000	0.000
37	A	49	VAL	0	0.010	0.010	5.891	-0.060	-0.060	0.000	0.000	0.000	0.000
38	A	50	THR	0	-0.024	-0.016	8.378	0.080	0.080	0.000	0.000	0.000	0.000
39	A	51	VAL	0	0.005	0.006	9.094	-0.097	-0.097	0.000	0.000	0.000	0.000
40	A	52	TYR	0	-0.003	-0.003	10.476	0.049	0.049	0.000	0.000	0.000	0.000
41	A	53	PRO	0	0.023	0.020	13.995	-0.034	-0.034	0.000	0.000	0.000	0.000
42	A	54	VAL	0	0.042	-0.003	15.205	0.000	0.000	0.000	0.000	0.000	0.000
43	A	55	TYR	0	-0.055	-0.003	17.993	0.007	0.007	0.000	0.000	0.000	0.000
44	A	56	ASP	-1	-0.878	-0.952	21.483	-0.113	-0.113	0.000	0.000	0.000	0.000
45	A	57	GLU	-1	-0.901	-0.970	16.402	-0.234	-0.234	0.000	0.000	0.000	0.000
46	A	58	ASP	-1	-0.909	-0.940	18.897	-0.134	-0.134	0.000	0.000	0.000	0.000
47	A	59	TYR	0	-0.082	-0.044	21.205	0.015	0.015	0.000	0.000	0.000	0.000
48	A	60	GLY	0	0.008	0.005	18.789	0.009	0.009	0.000	0.000	0.000	0.000
49	A	61	LEU	0	-0.069	-0.036	19.744	0.008	0.008	0.000	0.000	0.000	0.000
50	A	62	GLY	0	0.042	0.004	20.601	-0.015	-0.015	0.000	0.000	0.000	0.000
51	A	63	ARG	1	0.889	0.932	21.277	0.124	0.124	0.000	0.000	0.000	0.000
52	A	64	LEU	0	-0.019	0.008	21.418	-0.007	-0.007	0.000	0.000	0.000	0.000
53	A	65	VAL	0	0.005	-0.001	24.237	0.010	0.010	0.000	0.000	0.000	0.000
54	A	66	ASN	0	0.008	0.013	26.545	-0.006	-0.006	0.000	0.000	0.000	0.000
55	A	67	THR	0	-0.021	-0.028	26.131	0.001	0.001	0.000	0.000	0.000	0.000
56	A	68	ALA	0	-0.054	-0.021	28.753	0.000	0.000	0.000	0.000	0.000	0.000
57	A	69	ASP	-1	-0.882	-0.942	31.805	-0.061	-0.061	0.000	0.000	0.000	0.000
58	A	70	ASP	-1	-0.830	-0.920	31.478	-0.094	-0.094	0.000	0.000	0.000	0.000
59	A	71	SER	0	-0.195	-0.091	32.087	-0.002	-0.002	0.000	0.000	0.000	0.000
60	A	72	GLN	0	0.002	0.003	32.493	0.002	0.002	0.000	0.000	0.000	0.000
61	A	73	SER	0	-0.013	-0.018	28.409	-0.008	-0.008	0.000	0.000	0.000	0.000
62	A	74	ILE	0	-0.024	0.003	26.454	0.007	0.007	0.000	0.000	0.000	0.000
63	A	75	ILE	0	0.001	0.007	25.620	-0.009	-0.009	0.000	0.000	0.000	0.000
64	A	76	TYR	0	-0.090	-0.072	18.615	0.006	0.006	0.000	0.000	0.000	0.000
65	A	77	GLN	0	0.054	0.035	20.926	-0.010	-0.010	0.000	0.000	0.000	0.000
66	A	78	ILE	0	0.024	0.004	15.095	0.007	0.007	0.000	0.000	0.000	0.000
67	A	79	VAL	0	-0.039	-0.005	18.115	0.001	0.001	0.000	0.000	0.000	0.000
68	A	80	ASP	-1	-0.721	-0.880	16.004	-0.053	-0.053	0.000	0.000	0.000	0.000
69	A	81	ASP	-1	-0.918	-0.969	17.190	0.005	0.005	0.000	0.000	0.000	0.000
70	A	82	LYS	1	0.894	0.942	19.280	-0.007	-0.007	0.000	0.000	0.000	0.000
71	A	83	GLY	0	-0.069	-0.028	20.912	0.003	0.003	0.000	0.000	0.000	0.000
72	A	84	ARG	1	0.852	0.922	16.208	0.051	0.051	0.000	0.000	0.000	0.000
73	A	85	LYS	1	0.886	0.944	18.958	0.082	0.082	0.000	0.000	0.000	0.000
74	A	86	MET	0	-0.088	-0.008	14.239	0.002	0.002	0.000	0.000	0.000	0.000
75	A	87	LEU	0	0.027	0.009	15.442	-0.003	-0.003	0.000	0.000	0.000	0.000
76	A	88	LYS	1	0.975	1.016	11.869	0.300	0.300	0.000	0.000	0.000	0.000
77	A	89	ASP	-1	-0.863	-0.924	11.921	-0.169	-0.169	0.000	0.000	0.000	0.000
78	A	90	HIS	0	-0.059	-0.028	12.951	0.046	0.046	0.000	0.000	0.000	0.000
79	A	91	GLY	0	0.017	-0.002	12.223	-0.015	-0.015	0.000	0.000	0.000	0.000
80	A	92	ALA	0	-0.005	-0.003	12.244	0.032	0.032	0.000	0.000	0.000	0.000
81	A	93	GLU	-1	-0.938	-0.965	11.437	0.045	0.045	0.000	0.000	0.000	0.000
82	A	94	VAL	0	-0.074	-0.038	8.206	-0.008	-0.008	0.000	0.000	0.000	0.000
83	A	95	THR	0	-0.020	-0.022	10.880	0.031	0.031	0.000	0.000	0.000	0.000
84	A	96	PRO	0	0.016	0.000	7.940	-0.039	-0.039	0.000	0.000	0.000	0.000
85	A	97	ASN	0	-0.026	-0.030	8.510	0.048	0.048	0.000	0.000	0.000	0.000
86	A	98	GLN	0	-0.009	0.034	10.528	-0.034	-0.034	0.000	0.000	0.000	0.000
87	A	99	GLN	0	-0.025	-0.036	10.738	-0.044	-0.044	0.000	0.000	0.000	0.000
88	A	100	ILE	0	-0.017	-0.004	9.268	-0.002	-0.002	0.000	0.000	0.000	0.000
89	A	101	THR	0	0.009	-0.021	13.093	-0.010	-0.010	0.000	0.000	0.000	0.000
90	A	102	PHE	0	-0.026	-0.010	10.661	0.003	0.003	0.000	0.000	0.000	0.000
91	A	103	ARG	1	0.887	0.935	15.727	0.046	0.046	0.000	0.000	0.000	0.000
92	A	104	ALA	0	0.042	0.043	19.009	-0.004	-0.004	0.000	0.000	0.000	0.000
93	A	105	LEU	0	-0.050	-0.033	20.330	0.012	0.012	0.000	0.000	0.000	0.000
94	A	106	ASN	0	0.044	0.009	23.812	-0.011	-0.011	0.000	0.000	0.000	0.000
95	A	107	TYR	0	-0.031	-0.019	25.824	0.007	0.007	0.000	0.000	0.000	0.000
96	A	108	THR	0	-0.019	0.001	27.739	-0.001	-0.001	0.000	0.000	0.000	0.000
97	A	109	SER	0	0.013	0.013	30.513	0.003	0.003	0.000	0.000	0.000	0.000
98	A	110	GLY	0	0.038	0.008	33.934	-0.002	-0.002	0.000	0.000	0.000	0.000
99	A	111	ASP	-1	-0.903	-0.949	36.517	-0.034	-0.034	0.000	0.000	0.000	0.000
100	A	112	LYS	1	0.806	0.885	33.684	0.047	0.047	0.000	0.000	0.000	0.000
101	A	113	GLU	-1	-0.945	-0.965	35.221	-0.040	-0.040	0.000	0.000	0.000	0.000
102	A	114	ILE	0	-0.002	0.003	29.795	0.000	0.000	0.000	0.000	0.000	0.000
103	A	115	PRO	0	-0.002	0.024	33.721	0.003	0.003	0.000	0.000	0.000	0.000
104	A	116	PRO	0	0.015	0.008	32.615	-0.004	-0.004	0.000	0.000	0.000	0.000
105	A	117	GLY	0	0.002	0.007	31.098	0.000	0.000	0.000	0.000	0.000	0.000
106	A	118	ILE	0	-0.017	-0.004	25.664	0.001	0.001	0.000	0.000	0.000	0.000
107	A	119	TYR	0	-0.023	-0.033	25.314	-0.002	-0.002	0.000	0.000	0.000	0.000
108	A	120	ASN	0	-0.021	-0.032	20.600	-0.003	-0.003	0.000	0.000	0.000	0.000
109	A	121	ASP	-1	-0.744	-0.857	19.587	-0.169	-0.169	0.000	0.000	0.000	0.000
110	A	122	GLN	0	-0.078	-0.028	14.730	-0.028	-0.028	0.000	0.000	0.000	0.000
111	A	123	VAL	0	-0.030	-0.007	12.519	0.011	0.011	0.000	0.000	0.000	0.000
112	A	124	MET	0	-0.032	-0.013	9.365	-0.052	-0.052	0.000	0.000	0.000	0.000
113	A	125	VAL	0	-0.008	0.001	5.830	0.080	0.080	0.000	0.000	0.000	0.000
114	A	126	GLY	0	-0.007	-0.003	6.219	-0.183	-0.183	0.000	0.000	0.000	0.000
115	A	127	TYR	0	0.038	-0.006	2.588	-3.634	-1.647	3.271	-1.308	-3.950	-0.011
116	A	128	TYR	0	-0.009	0.001	4.694	0.531	0.622	-0.001	-0.009	-0.082	0.000
117	A	129	VAL	0	0.029	0.026	2.791	-1.885	-0.152	1.089	-0.572	-2.250	0.004
118	A	130	ASN	0	-0.049	-0.057	5.713	-0.214	-0.214	0.000	0.000	0.000	0.000
119	A	131	ASP	-1	-0.836	-0.897	7.144	-0.362	-0.362	0.000	0.000	0.000	0.000
120	A	132	ASN	0	-0.014	-0.004	9.946	0.051	0.051	0.000	0.000	0.000	0.000
121	A	133	LYS	1	0.901	0.940	12.315	0.039	0.039	0.000	0.000	0.000	0.000
122	A	134	GLN	0	-0.049	-0.029	12.606	-0.004	-0.004	0.000	0.000	0.000	0.000
123	A	135	GLY	0	0.060	0.047	9.510	0.029	0.029	0.000	0.000	0.000	0.000
124	A	136	ASN	0	-0.069	-0.046	6.930	0.105	0.105	0.000	0.000	0.000	0.000
125	A	137	TRP	0	0.044	0.026	7.439	0.247	0.247	0.000	0.000	0.000	0.000
126	A	138	GLN	0	-0.056	-0.012	2.962	-3.436	-1.363	0.726	-0.688	-2.112	0.007
127	A	139	TYR	0	-0.043	-0.059	4.762	-0.395	-0.214	-0.001	-0.007	-0.172	0.000
128	A	140	LYS	1	0.922	0.968	4.876	0.503	0.503	0.000	0.000	0.000	0.000
129	A	141	SER	0	0.026	0.016	6.683	0.098	0.098	0.000	0.000	0.000	0.000
130	A	142	LEU	0	-0.009	-0.015	10.186	-0.036	-0.036	0.000	0.000	0.000	0.000
131	A	143	ASP	-1	-0.854	-0.917	12.101	-0.259	-0.259	0.000	0.000	0.000	0.000
132	A	144	VAL	0	-0.023	-0.020	15.819	0.013	0.013	0.000	0.000	0.000	0.000
133	A	145	ASN	0	-0.006	-0.004	18.020	0.011	0.011	0.000	0.000	0.000	0.000
134	A	146	VAL	0	-0.001	0.001	20.566	0.008	0.008	0.000	0.000	0.000	0.000
135	A	147	ASN	0	-0.040	-0.004	23.260	-0.003	-0.003	0.000	0.000	0.000	0.000
136	A	148	ILE	0	-0.001	0.011	24.707	0.002	0.002	0.000	0.000	0.000	0.000
137	A	149	GLU	-1	-0.921	-0.975	28.385	-0.044	-0.044	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:13:PHE)