FMO DATABASE

FMODB ID: NNGZQ

Calculation Name: 2F9H-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2F9H

Chain ID: A

ChEMBL ID:

UniProt ID: Q831B0

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	121
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1001572.818754
FMO2-HF: Nuclear repulsion	955186.095192
FMO2-HF: Total energy	-46386.723562
FMO2-MP2: Total energy	-46523.74441

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:3:TRP)

Summations of interaction energy for fragment #1(A:3:TRP)

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.
-21.773	-19.892	12.738	-5.614	-9.007	-0.028

Interaction energy analysis for fragmet #1(A:3:TRP)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.004 / q_NPA : -0.015

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	5	MET	0	-0.018	0.012	2.018	-3.295	-0.707	4.386	-2.052	-4.922	-0.002
4	A	6	GLN	0	-0.083	-0.040	3.816	2.092	2.303	0.005	-0.012	-0.204	0.000
5	A	7	ALA	0	0.004	0.024	7.564	-0.168	-0.168	0.000	0.000	0.000	0.000
6	A	8	THR	0	-0.017	-0.025	10.578	0.285	0.285	0.000	0.000	0.000	0.000
7	A	9	VAL	0	-0.022	0.001	14.082	-0.009	-0.009	0.000	0.000	0.000	0.000
8	A	10	THR	0	-0.010	-0.015	17.393	0.073	0.073	0.000	0.000	0.000	0.000
9	A	11	GLU	-1	-0.868	-0.940	19.876	-0.458	-0.458	0.000	0.000	0.000	0.000
10	A	12	ILE	0	-0.024	-0.002	21.647	-0.051	-0.051	0.000	0.000	0.000	0.000
11	A	13	GLY	0	0.017	0.031	24.062	0.042	0.042	0.000	0.000	0.000	0.000
12	A	14	LYS	1	0.855	0.903	26.824	0.291	0.291	0.000	0.000	0.000	0.000
13	A	15	HIS	0	-0.014	-0.013	29.100	0.025	0.025	0.000	0.000	0.000	0.000
14	A	16	ALA	0	-0.034	0.012	24.000	-0.005	-0.005	0.000	0.000	0.000	0.000
15	A	17	ILE	0	-0.007	-0.009	22.760	-0.022	-0.022	0.000	0.000	0.000	0.000
16	A	18	ASP	-1	-0.794	-0.858	26.294	-0.233	-0.233	0.000	0.000	0.000	0.000
17	A	19	ASP	-1	-0.921	-0.985	28.028	-0.245	-0.245	0.000	0.000	0.000	0.000
18	A	20	SER	0	-0.127	-0.090	29.141	0.012	0.012	0.000	0.000	0.000	0.000
19	A	21	GLU	-1	-0.937	-0.964	28.132	-0.349	-0.349	0.000	0.000	0.000	0.000
20	A	22	LYS	1	0.891	0.957	24.750	0.223	0.223	0.000	0.000	0.000	0.000
21	A	23	MET	0	-0.059	-0.035	23.250	-0.031	-0.031	0.000	0.000	0.000	0.000
22	A	24	ILE	0	0.021	0.011	19.980	0.010	0.010	0.000	0.000	0.000	0.000
23	A	25	ILE	0	0.015	0.018	20.061	-0.072	-0.072	0.000	0.000	0.000	0.000
24	A	26	LEU	0	-0.010	0.006	14.411	0.005	0.005	0.000	0.000	0.000	0.000
25	A	27	PHE	0	0.028	-0.014	18.220	0.028	0.028	0.000	0.000	0.000	0.000
26	A	28	GLY	0	0.045	0.045	16.757	-0.046	-0.046	0.000	0.000	0.000	0.000
27	A	29	GLU	-1	-0.877	-0.974	17.302	-0.881	-0.881	0.000	0.000	0.000	0.000
28	A	30	THR	0	-0.090	-0.030	19.543	0.053	0.053	0.000	0.000	0.000	0.000
29	A	31	ALA	0	0.023	0.027	21.903	0.055	0.055	0.000	0.000	0.000	0.000
30	A	32	THR	0	0.012	0.003	23.694	0.016	0.016	0.000	0.000	0.000	0.000
31	A	33	ASP	-1	-0.827	-0.934	27.294	-0.397	-0.397	0.000	0.000	0.000	0.000
32	A	34	THR	0	-0.068	-0.039	29.452	0.003	0.003	0.000	0.000	0.000	0.000
33	A	35	LEU	0	0.007	-0.008	25.523	0.013	0.013	0.000	0.000	0.000	0.000
34	A	36	LYS	1	0.889	0.958	23.949	0.517	0.517	0.000	0.000	0.000	0.000
35	A	37	GLN	0	-0.080	-0.034	26.050	0.010	0.010	0.000	0.000	0.000	0.000
36	A	38	HIS	0	0.012	-0.003	26.619	0.015	0.015	0.000	0.000	0.000	0.000
37	A	39	ALA	0	0.026	0.024	21.492	-0.012	-0.012	0.000	0.000	0.000	0.000
38	A	40	VAL	0	0.002	0.015	18.194	0.036	0.036	0.000	0.000	0.000	0.000
39	A	41	ILE	0	-0.029	-0.016	19.046	-0.064	-0.064	0.000	0.000	0.000	0.000
40	A	42	GLN	0	0.026	0.005	12.596	-0.151	-0.151	0.000	0.000	0.000	0.000
41	A	43	SER	0	0.014	0.026	13.903	-0.082	-0.082	0.000	0.000	0.000	0.000
42	A	44	PHE	0	0.038	-0.015	6.369	0.017	0.017	0.000	0.000	0.000	0.000
43	A	45	PRO	0	-0.033	-0.035	8.196	0.037	0.037	0.000	0.000	0.000	0.000
44	A	46	GLU	-1	-0.879	-0.944	3.319	-13.365	-11.886	0.013	-0.858	-0.635	-0.007
45	A	47	LYS	1	0.922	0.987	7.002	1.273	1.273	0.000	0.000	0.000	0.000
46	A	48	ASP	-1	-0.902	-0.950	9.093	-2.055	-2.055	0.000	0.000	0.000	0.000
47	A	49	GLN	0	-0.073	-0.054	5.603	0.782	0.782	0.000	0.000	0.000	0.000
48	A	50	VAL	0	-0.043	-0.003	6.341	-0.143	-0.143	0.000	0.000	0.000	0.000
49	A	51	THR	0	-0.042	-0.033	6.625	0.867	0.867	0.000	0.000	0.000	0.000
50	A	52	LEU	0	-0.036	-0.017	7.541	-0.312	-0.312	0.000	0.000	0.000	0.000
51	A	53	ALA	0	-0.007	-0.013	9.083	0.301	0.301	0.000	0.000	0.000	0.000
52	A	54	GLU	-1	-0.910	-0.962	10.316	-0.445	-0.445	0.000	0.000	0.000	0.000
53	A	55	GLY	0	-0.051	-0.016	11.034	0.039	0.039	0.000	0.000	0.000	0.000
54	A	56	ASP	-1	-0.804	-0.898	6.443	-1.668	-1.668	0.000	0.000	0.000	0.000
55	A	57	HIS	0	-0.020	-0.025	7.172	0.295	0.295	0.000	0.000	0.000	0.000
56	A	58	LEU	0	-0.001	0.006	8.234	-0.538	-0.538	0.000	0.000	0.000	0.000
57	A	59	LYS	1	0.906	0.966	10.471	0.423	0.423	0.000	0.000	0.000	0.000
58	A	60	ILE	0	0.022	0.012	12.204	-0.190	-0.190	0.000	0.000	0.000	0.000
59	A	61	GLY	0	0.054	0.030	15.090	0.121	0.121	0.000	0.000	0.000	0.000
60	A	62	ASP	-1	-0.986	-0.996	16.379	-0.190	-0.190	0.000	0.000	0.000	0.000
61	A	63	THR	0	-0.027	-0.016	17.344	0.090	0.090	0.000	0.000	0.000	0.000
62	A	64	ASN	0	-0.077	-0.045	11.240	-0.082	-0.082	0.000	0.000	0.000	0.000
63	A	65	TYR	0	-0.037	-0.037	13.164	0.067	0.067	0.000	0.000	0.000	0.000
64	A	66	THR	0	-0.020	-0.004	11.989	-0.046	-0.046	0.000	0.000	0.000	0.000
65	A	67	ILE	0	0.004	-0.014	9.666	0.012	0.012	0.000	0.000	0.000	0.000
66	A	68	THR	0	-0.027	-0.029	13.224	0.050	0.050	0.000	0.000	0.000	0.000
67	A	69	LYS	1	0.955	0.987	15.997	0.440	0.440	0.000	0.000	0.000	0.000
68	A	70	VAL	0	-0.013	0.007	12.650	-0.069	-0.069	0.000	0.000	0.000	0.000
69	A	71	GLY	0	0.021	0.027	16.109	0.069	0.069	0.000	0.000	0.000	0.000
70	A	72	SER	0	0.001	-0.025	17.548	-0.083	-0.083	0.000	0.000	0.000	0.000
71	A	73	PHE	0	-0.051	-0.032	18.632	0.002	0.002	0.000	0.000	0.000	0.000
72	A	74	ALA	0	0.042	0.044	15.365	-0.038	-0.038	0.000	0.000	0.000	0.000
73	A	75	ASN	0	0.074	0.045	11.389	-0.330	-0.330	0.000	0.000	0.000	0.000
74	A	76	SER	0	0.009	0.009	13.456	-0.110	-0.110	0.000	0.000	0.000	0.000
75	A	77	ASN	0	-0.038	-0.035	16.003	0.028	0.028	0.000	0.000	0.000	0.000
76	A	78	LEU	0	0.002	0.015	10.835	-0.018	-0.018	0.000	0.000	0.000	0.000
77	A	79	GLN	0	-0.016	-0.014	10.835	0.131	0.131	0.000	0.000	0.000	0.000
78	A	80	SER	0	-0.079	-0.026	12.806	0.025	0.025	0.000	0.000	0.000	0.000
79	A	81	ILE	0	-0.038	-0.025	16.290	0.023	0.023	0.000	0.000	0.000	0.000
80	A	82	ALA	0	0.005	0.007	13.697	0.025	0.025	0.000	0.000	0.000	0.000
81	A	83	HIS	0	-0.067	-0.034	14.591	0.096	0.096	0.000	0.000	0.000	0.000
82	A	84	SER	0	-0.038	-0.032	15.461	-0.072	-0.072	0.000	0.000	0.000	0.000
83	A	85	THR	0	0.005	0.008	17.548	0.044	0.044	0.000	0.000	0.000	0.000
84	A	86	LEU	0	-0.022	0.000	14.972	-0.013	-0.013	0.000	0.000	0.000	0.000
85	A	87	ILE	0	0.026	0.002	18.851	0.067	0.067	0.000	0.000	0.000	0.000
86	A	88	PHE	0	-0.033	-0.007	18.336	-0.015	-0.015	0.000	0.000	0.000	0.000
87	A	89	ALA	0	0.049	0.000	21.599	0.045	0.045	0.000	0.000	0.000	0.000
88	A	90	ASP	-1	-0.927	-0.956	22.056	-0.243	-0.243	0.000	0.000	0.000	0.000
89	A	91	ALA	0	-0.019	-0.015	21.072	-0.015	-0.015	0.000	0.000	0.000	0.000
90	A	92	PRO	0	-0.035	-0.010	23.117	0.031	0.031	0.000	0.000	0.000	0.000
91	A	93	THR	0	-0.008	-0.023	25.584	-0.004	-0.004	0.000	0.000	0.000	0.000
92	A	94	ASP	-1	-0.940	-0.959	27.696	-0.205	-0.205	0.000	0.000	0.000	0.000
93	A	95	GLU	-1	-0.814	-0.928	23.244	-0.355	-0.355	0.000	0.000	0.000	0.000
94	A	96	ASP	-1	-1.006	-0.981	26.341	-0.270	-0.270	0.000	0.000	0.000	0.000
95	A	97	ASP	-1	-0.922	-0.974	28.407	-0.253	-0.253	0.000	0.000	0.000	0.000
96	A	98	VAL	0	-0.111	-0.038	21.584	-0.029	-0.029	0.000	0.000	0.000	0.000
97	A	99	ILE	0	-0.005	0.000	22.429	-0.008	-0.008	0.000	0.000	0.000	0.000
98	A	100	ARG	1	0.988	0.972	21.706	0.367	0.367	0.000	0.000	0.000	0.000
99	A	101	ASN	0	-0.011	0.007	19.014	-0.010	-0.010	0.000	0.000	0.000	0.000
100	A	102	GLY	0	0.045	0.017	18.624	-0.071	-0.071	0.000	0.000	0.000	0.000
101	A	103	VAL	0	-0.005	0.000	13.384	-0.045	-0.045	0.000	0.000	0.000	0.000
102	A	104	TYR	0	0.050	0.030	16.511	0.020	0.020	0.000	0.000	0.000	0.000
103	A	105	LEU	0	-0.018	-0.002	13.864	-0.048	-0.048	0.000	0.000	0.000	0.000
104	A	106	THR	0	0.029	0.018	16.550	0.070	0.070	0.000	0.000	0.000	0.000
105	A	107	PRO	0	0.022	-0.001	16.645	-0.004	-0.004	0.000	0.000	0.000	0.000
106	A	108	HIS	0	-0.007	-0.011	19.936	-0.033	-0.033	0.000	0.000	0.000	0.000
107	A	109	GLN	0	-0.040	-0.003	22.124	-0.001	-0.001	0.000	0.000	0.000	0.000
108	A	110	LEU	0	0.053	0.048	21.502	-0.029	-0.029	0.000	0.000	0.000	0.000
109	A	111	PRO	0	0.005	0.025	18.878	0.039	0.039	0.000	0.000	0.000	0.000
110	A	112	LYS	1	0.922	0.949	21.009	0.226	0.226	0.000	0.000	0.000	0.000
111	A	113	ILE	0	0.023	0.014	18.736	-0.030	-0.030	0.000	0.000	0.000	0.000
112	A	114	THR	0	-0.036	-0.036	20.712	0.041	0.041	0.000	0.000	0.000	0.000
113	A	115	ILE	0	0.028	0.004	20.465	-0.056	-0.056	0.000	0.000	0.000	0.000
114	A	116	GLY	0	0.001	0.004	18.425	0.056	0.056	0.000	0.000	0.000	0.000
115	A	117	THR	0	-0.042	-0.014	16.313	0.009	0.009	0.000	0.000	0.000	0.000
116	A	118	THR	0	0.023	0.015	11.965	-0.025	-0.025	0.000	0.000	0.000	0.000
117	A	119	ILE	0	-0.020	-0.017	10.989	0.199	0.199	0.000	0.000	0.000	0.000
118	A	120	ASP	-1	-0.875	-0.946	7.936	-1.598	-1.598	0.000	0.000	0.000	0.000
119	A	121	TYR	0	0.026	-0.010	5.674	0.605	0.605	0.000	0.000	0.000	0.000
120	A	122	LEU	0	-0.061	-0.037	4.016	-1.913	-1.713	-0.001	-0.076	-0.123	0.000
121	A	123	VAL	0	0.028	0.033	1.995	-1.011	-3.608	8.335	-2.616	-3.123	-0.019

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Interactive mode: IFIE and PIEDA for fragment #1(A:3:TRP)