FMO DATABASE

FMODB ID: JQGG9

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:

Apendix: None

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	137
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1215397.440757
FMO2-HF: Nuclear repulsion	1161965.017884
FMO2-HF: Total energy	-53432.422873
FMO2-MP2: Total energy	-53590.320915

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.
-15.858	-2.659	8.684	-5.833	-16.048	0.013

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 : 0.028 / q_NPA : 0.013

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	0.007	0.007	2.669	-2.756	1.276	1.009	-1.980	-3.061	0.013
4	A	16	PRO	0	-0.012	0.003	4.808	-0.778	-0.598	0.001	-0.045	-0.136	0.000
5	A	17	GLU	-1	-0.863	-0.929	7.580	-0.590	-0.590	0.000	0.000	0.000	0.000
6	A	18	PRO	0	-0.004	0.007	7.766	0.074	0.074	0.000	0.000	0.000	0.000
7	A	19	GLN	0	-0.052	-0.032	10.454	0.020	0.020	0.000	0.000	0.000	0.000
8	A	20	ILE	0	0.053	0.032	14.253	0.017	0.017	0.000	0.000	0.000	0.000
9	A	21	GLN	0	-0.068	-0.034	16.024	0.014	0.014	0.000	0.000	0.000	0.000
10	A	22	PRO	0	0.054	0.025	19.969	0.003	0.003	0.000	0.000	0.000	0.000
11	A	23	SER	0	-0.058	-0.020	23.069	0.009	0.009	0.000	0.000	0.000	0.000
12	A	24	PHE	0	0.080	0.013	25.613	0.000	0.000	0.000	0.000	0.000	0.000
13	A	25	GLY	0	0.042	0.015	29.343	0.004	0.004	0.000	0.000	0.000	0.000
14	A	26	LYS	1	0.931	0.970	31.091	0.040	0.040	0.000	0.000	0.000	0.000
15	A	27	ASN	0	-0.027	-0.035	28.101	0.003	0.003	0.000	0.000	0.000	0.000
16	A	28	VAL	0	0.038	0.040	28.221	0.003	0.003	0.000	0.000	0.000	0.000
17	A	29	GLY	0	0.046	0.022	29.694	-0.002	-0.002	0.000	0.000	0.000	0.000
18	A	30	LYS	1	0.864	0.942	32.141	0.038	0.038	0.000	0.000	0.000	0.000
19	A	31	GLU	-1	-0.795	-0.891	30.651	-0.037	-0.037	0.000	0.000	0.000	0.000
20	A	32	GLY	0	-0.041	-0.029	27.722	0.004	0.004	0.000	0.000	0.000	0.000
21	A	33	GLY	0	-0.051	-0.019	27.619	0.001	0.001	0.000	0.000	0.000	0.000
22	A	34	LEU	0	-0.069	-0.037	21.786	-0.002	-0.002	0.000	0.000	0.000	0.000
23	A	35	LEU	0	0.023	0.008	23.113	0.002	0.002	0.000	0.000	0.000	0.000
24	A	36	PHE	0	0.008	0.004	16.608	-0.003	-0.003	0.000	0.000	0.000	0.000
25	A	37	SER	0	-0.005	-0.007	18.250	0.011	0.011	0.000	0.000	0.000	0.000
26	A	38	VAL	0	0.039	0.028	11.904	-0.014	-0.014	0.000	0.000	0.000	0.000
27	A	39	SER	0	0.002	0.005	13.736	0.022	0.022	0.000	0.000	0.000	0.000
28	A	40	LEU	0	-0.015	-0.005	7.177	-0.040	-0.040	0.000	0.000	0.000	0.000
29	A	41	THR	0	0.026	0.007	9.353	0.024	0.024	0.000	0.000	0.000	0.000
30	A	42	VAL	0	-0.023	0.007	6.335	-0.053	-0.053	0.000	0.000	0.000	0.000
31	A	43	PRO	0	0.018	0.018	2.381	-1.114	0.004	0.855	-0.462	-1.510	0.003
32	A	44	GLU	-1	-0.821	-0.916	4.519	0.556	0.739	-0.001	-0.015	-0.166	0.000
33	A	45	ASN	0	-0.089	-0.057	3.648	-1.469	-0.732	0.006	-0.205	-0.538	-0.001
34	A	46	VAL	0	-0.005	0.012	2.354	-0.962	-0.268	0.883	-0.316	-1.260	-0.004
35	A	47	SER	0	-0.013	-0.007	5.528	-0.062	-0.062	0.000	0.000	0.000	0.000
36	A	48	GLN	0	0.000	-0.004	7.490	-0.118	-0.118	0.000	0.000	0.000	0.000
37	A	49	VAL	0	0.004	0.002	5.675	-0.021	-0.021	0.000	0.000	0.000	0.000
38	A	50	THR	0	-0.019	-0.012	8.231	0.054	0.054	0.000	0.000	0.000	0.000
39	A	51	VAL	0	-0.001	0.002	9.070	-0.107	-0.107	0.000	0.000	0.000	0.000
40	A	52	TYR	0	-0.021	-0.011	10.246	0.044	0.044	0.000	0.000	0.000	0.000
41	A	53	PRO	0	0.018	0.020	13.901	-0.039	-0.039	0.000	0.000	0.000	0.000
42	A	54	VAL	0	0.039	-0.003	14.993	0.012	0.012	0.000	0.000	0.000	0.000
43	A	55	TYR	0	-0.052	-0.004	17.854	0.006	0.006	0.000	0.000	0.000	0.000
44	A	56	ASP	-1	-0.880	-0.952	21.383	-0.040	-0.040	0.000	0.000	0.000	0.000
45	A	57	GLU	-1	-0.846	-0.949	15.525	-0.109	-0.109	0.000	0.000	0.000	0.000
46	A	58	ASP	-1	-0.919	-0.946	18.770	-0.012	-0.012	0.000	0.000	0.000	0.000
47	A	59	TYR	0	-0.071	-0.035	21.069	0.017	0.017	0.000	0.000	0.000	0.000
48	A	60	GLY	0	0.018	0.011	18.696	0.003	0.003	0.000	0.000	0.000	0.000
49	A	61	LEU	0	-0.077	-0.042	19.658	-0.001	-0.001	0.000	0.000	0.000	0.000
50	A	62	GLY	0	0.039	0.003	20.521	-0.011	-0.011	0.000	0.000	0.000	0.000
51	A	63	ARG	1	0.880	0.926	21.192	0.107	0.107	0.000	0.000	0.000	0.000
52	A	64	LEU	0	-0.017	0.010	21.449	-0.009	-0.009	0.000	0.000	0.000	0.000
53	A	65	VAL	0	0.001	-0.005	24.173	0.013	0.013	0.000	0.000	0.000	0.000
54	A	66	ASN	0	0.010	0.007	26.480	-0.013	-0.013	0.000	0.000	0.000	0.000
55	A	67	THR	0	-0.020	-0.028	26.072	0.002	0.002	0.000	0.000	0.000	0.000
56	A	68	ALA	0	-0.056	-0.020	28.687	0.000	0.000	0.000	0.000	0.000	0.000
57	A	69	ASP	-1	-0.855	-0.913	31.735	-0.065	-0.065	0.000	0.000	0.000	0.000
58	A	70	ASP	-1	-0.849	-0.930	31.377	-0.094	-0.094	0.000	0.000	0.000	0.000
59	A	71	SER	0	-0.182	-0.101	31.987	0.002	0.002	0.000	0.000	0.000	0.000
60	A	72	GLN	0	-0.024	-0.004	32.389	0.005	0.005	0.000	0.000	0.000	0.000
61	A	73	SER	0	-0.037	-0.029	28.237	-0.009	-0.009	0.000	0.000	0.000	0.000
62	A	74	ILE	0	-0.010	0.012	26.468	0.007	0.007	0.000	0.000	0.000	0.000
63	A	75	ILE	0	0.002	0.008	25.591	-0.008	-0.008	0.000	0.000	0.000	0.000
64	A	76	TYR	0	-0.093	-0.076	18.596	0.003	0.003	0.000	0.000	0.000	0.000
65	A	77	GLN	0	0.050	0.035	20.879	0.002	0.002	0.000	0.000	0.000	0.000
66	A	78	ILE	0	0.026	0.009	15.108	-0.002	-0.002	0.000	0.000	0.000	0.000
67	A	79	VAL	0	-0.030	-0.004	18.113	0.013	0.013	0.000	0.000	0.000	0.000
68	A	80	ASP	-1	-0.688	-0.852	15.915	-0.002	-0.002	0.000	0.000	0.000	0.000
69	A	81	ASP	-1	-0.858	-0.920	17.038	0.021	0.021	0.000	0.000	0.000	0.000
70	A	82	LYS	1	0.813	0.890	19.247	-0.031	-0.031	0.000	0.000	0.000	0.000
71	A	83	GLY	0	-0.058	-0.026	20.834	0.003	0.003	0.000	0.000	0.000	0.000
72	A	84	ARG	1	0.833	0.905	16.038	-0.064	-0.064	0.000	0.000	0.000	0.000
73	A	85	LYS	1	0.877	0.934	18.984	0.019	0.019	0.000	0.000	0.000	0.000
74	A	86	MET	0	-0.086	-0.001	14.265	0.016	0.016	0.000	0.000	0.000	0.000
75	A	87	LEU	0	0.026	0.011	15.390	-0.014	-0.014	0.000	0.000	0.000	0.000
76	A	88	LYS	1	0.907	0.969	12.124	0.011	0.011	0.000	0.000	0.000	0.000
77	A	89	ASP	-1	-0.813	-0.866	11.612	0.125	0.125	0.000	0.000	0.000	0.000
78	A	90	HIS	0	-0.054	-0.028	12.842	0.062	0.062	0.000	0.000	0.000	0.000
79	A	91	GLY	0	0.037	0.009	12.143	-0.043	-0.043	0.000	0.000	0.000	0.000
80	A	92	ALA	0	-0.016	-0.008	12.100	0.028	0.028	0.000	0.000	0.000	0.000
81	A	93	GLU	-1	-0.838	-0.910	11.332	0.343	0.343	0.000	0.000	0.000	0.000
82	A	94	VAL	0	-0.087	-0.046	8.308	-0.048	-0.048	0.000	0.000	0.000	0.000
83	A	95	THR	0	-0.007	-0.008	10.895	0.081	0.081	0.000	0.000	0.000	0.000
84	A	96	PRO	0	0.008	-0.004	7.788	-0.080	-0.080	0.000	0.000	0.000	0.000
85	A	97	ASN	0	-0.075	-0.059	8.720	-0.079	-0.079	0.000	0.000	0.000	0.000
86	A	98	GLN	0	0.019	0.039	10.750	-0.013	-0.013	0.000	0.000	0.000	0.000
87	A	99	GLN	0	-0.015	-0.015	10.892	-0.035	-0.035	0.000	0.000	0.000	0.000
88	A	100	ILE	0	-0.022	-0.003	9.358	0.025	0.025	0.000	0.000	0.000	0.000
89	A	101	THR	0	-0.016	-0.028	13.143	-0.025	-0.025	0.000	0.000	0.000	0.000
90	A	102	PHE	0	-0.012	-0.005	10.580	0.021	0.021	0.000	0.000	0.000	0.000
91	A	103	ARG	1	0.860	0.915	15.808	0.029	0.029	0.000	0.000	0.000	0.000
92	A	104	ALA	0	0.042	0.042	19.060	0.006	0.006	0.000	0.000	0.000	0.000
93	A	105	LEU	0	-0.049	-0.030	20.349	0.006	0.006	0.000	0.000	0.000	0.000
94	A	106	ASN	0	0.054	0.014	23.829	-0.005	-0.005	0.000	0.000	0.000	0.000
95	A	107	TYR	0	-0.025	-0.018	25.739	0.009	0.009	0.000	0.000	0.000	0.000
96	A	108	THR	0	-0.022	-0.001	27.710	0.002	0.002	0.000	0.000	0.000	0.000
97	A	109	SER	0	0.000	0.007	30.472	0.001	0.001	0.000	0.000	0.000	0.000
98	A	110	GLY	0	0.037	0.011	33.895	-0.003	-0.003	0.000	0.000	0.000	0.000
99	A	111	ASP	-1	-0.908	-0.946	36.375	-0.028	-0.028	0.000	0.000	0.000	0.000
100	A	112	LYS	1	0.796	0.875	33.661	0.040	0.040	0.000	0.000	0.000	0.000
101	A	113	GLU	-1	-0.945	-0.965	35.354	-0.044	-0.044	0.000	0.000	0.000	0.000
102	A	114	ILE	0	-0.014	0.000	29.766	-0.001	-0.001	0.000	0.000	0.000	0.000
103	A	115	PRO	0	0.029	0.038	33.592	0.001	0.001	0.000	0.000	0.000	0.000
104	A	116	PRO	0	0.002	-0.004	32.606	-0.005	-0.005	0.000	0.000	0.000	0.000
105	A	117	GLY	0	0.004	0.011	31.100	0.001	0.001	0.000	0.000	0.000	0.000
106	A	118	ILE	0	-0.012	0.001	25.674	-0.001	-0.001	0.000	0.000	0.000	0.000
107	A	119	TYR	0	-0.018	-0.027	25.253	0.002	0.002	0.000	0.000	0.000	0.000
108	A	120	ASN	0	-0.020	-0.032	20.304	-0.004	-0.004	0.000	0.000	0.000	0.000
109	A	121	ASP	-1	-0.748	-0.852	19.507	-0.145	-0.145	0.000	0.000	0.000	0.000
110	A	122	GLN	0	-0.095	-0.053	14.734	-0.028	-0.028	0.000	0.000	0.000	0.000
111	A	123	VAL	0	-0.027	-0.008	12.501	0.023	0.023	0.000	0.000	0.000	0.000
112	A	124	MET	0	-0.008	0.007	9.302	-0.065	-0.065	0.000	0.000	0.000	0.000
113	A	125	VAL	0	-0.015	-0.005	5.857	0.083	0.083	0.000	0.000	0.000	0.000
114	A	126	GLY	0	0.009	0.006	6.082	-0.185	-0.185	0.000	0.000	0.000	0.000
115	A	127	TYR	0	0.025	-0.013	2.706	-3.845	-1.362	2.507	-1.310	-3.680	-0.011
116	A	128	TYR	0	-0.011	0.000	4.670	0.801	0.906	-0.001	-0.009	-0.095	0.000
117	A	129	VAL	0	0.012	0.007	2.535	-1.853	-0.501	2.485	-0.753	-3.084	0.005
118	A	130	ASN	0	-0.039	-0.045	5.519	-0.402	-0.402	0.000	0.000	0.000	0.000
119	A	131	ASP	-1	-0.823	-0.892	7.246	0.788	0.788	0.000	0.000	0.000	0.000
120	A	132	ASN	0	0.001	0.002	10.004	-0.203	-0.203	0.000	0.000	0.000	0.000
121	A	133	LYS	1	0.882	0.930	12.372	-0.418	-0.418	0.000	0.000	0.000	0.000
122	A	134	GLN	0	-0.051	-0.028	12.650	-0.142	-0.142	0.000	0.000	0.000	0.000
123	A	135	GLY	0	0.055	0.047	9.509	0.186	0.186	0.000	0.000	0.000	0.000
124	A	136	ASN	0	-0.060	-0.030	7.063	0.136	0.136	0.000	0.000	0.000	0.000
125	A	137	TRP	0	0.035	0.018	7.264	0.426	0.426	0.000	0.000	0.000	0.000
126	A	138	GLN	0	-0.055	-0.015	2.919	-3.473	-1.361	0.941	-0.725	-2.329	0.008
127	A	139	TYR	0	-0.044	-0.073	4.570	-0.615	-0.412	-0.001	-0.013	-0.189	0.000
128	A	140	LYS	1	0.849	0.926	4.929	0.453	0.453	0.000	0.000	0.000	0.000
129	A	141	SER	0	0.051	0.021	6.694	0.105	0.105	0.000	0.000	0.000	0.000
130	A	142	LEU	0	-0.036	-0.029	10.164	-0.064	-0.064	0.000	0.000	0.000	0.000
131	A	143	ASP	-1	-0.842	-0.902	12.034	-0.290	-0.290	0.000	0.000	0.000	0.000
132	A	144	VAL	0	-0.022	-0.016	15.757	0.001	0.001	0.000	0.000	0.000	0.000
133	A	145	ASN	0	-0.013	-0.006	17.991	0.026	0.026	0.000	0.000	0.000	0.000
134	A	146	VAL	0	-0.005	-0.002	20.538	0.000	0.000	0.000	0.000	0.000	0.000
135	A	147	ASN	0	-0.053	-0.026	23.271	-0.002	-0.002	0.000	0.000	0.000	0.000
136	A	148	ILE	0	-0.016	0.003	24.711	0.002	0.002	0.000	0.000	0.000	0.000
137	A	149	GLU	-1	-0.887	-0.941	28.403	-0.080	-0.080	0.000	0.000	0.000	0.000

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