FMO DATABASE

FMODB ID: 2N21R

Calculation Name: 2G2D-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2G2D

Chain ID: A

ChEMBL ID:

UniProt ID: P9WP99

Base Structure: X-ray

Registration Date: 2023-09-21

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	160
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1429067.43866
FMO2-HF: Nuclear repulsion	1369828.420034
FMO2-HF: Total energy	-59239.018625
FMO2-MP2: Total energy	-59415.130973

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:29:THR)

Summations of interaction energy for fragment #1(A:29:THR)

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.
-2.881	0.131	0.402	-1.356	-2.058	0.002

Interaction energy analysis for fragmet #1(A:29:THR)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.008 / q_NPA : 0.001

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	31	ALA	0	0.046	0.020	3.808	-2.940	-1.299	-0.006	-0.837	-0.799	0.004
4	A	32	ARG	1	0.871	0.936	6.145	0.690	0.690	0.000	0.000	0.000	0.000
5	A	33	LEU	0	-0.024	-0.014	3.490	-0.224	0.267	0.008	-0.119	-0.380	0.000
6	A	34	VAL	0	-0.023	-0.006	2.488	-0.672	0.144	0.401	-0.395	-0.822	-0.002
7	A	35	ALA	0	0.044	0.025	5.005	0.614	0.678	-0.001	-0.005	-0.057	0.000
8	A	36	TYR	0	-0.036	-0.013	8.335	0.280	0.280	0.000	0.000	0.000	0.000
9	A	37	ALA	0	0.022	0.002	7.151	0.192	0.192	0.000	0.000	0.000	0.000
10	A	38	ASP	-1	-0.793	-0.858	8.937	-0.799	-0.799	0.000	0.000	0.000	0.000
11	A	39	CYS	0	-0.071	-0.032	10.685	0.133	0.133	0.000	0.000	0.000	0.000
12	A	40	ASP	-1	-0.900	-0.939	12.447	-0.085	-0.085	0.000	0.000	0.000	0.000
13	A	41	GLU	-1	-0.839	-0.881	12.452	-0.235	-0.235	0.000	0.000	0.000	0.000
14	A	42	ALA	0	-0.026	-0.029	14.345	0.044	0.044	0.000	0.000	0.000	0.000
15	A	43	ASN	0	0.002	-0.012	16.551	0.049	0.049	0.000	0.000	0.000	0.000
16	A	44	ALA	0	0.018	0.009	17.436	0.029	0.029	0.000	0.000	0.000	0.000
17	A	45	ALA	0	-0.022	-0.007	18.711	0.022	0.022	0.000	0.000	0.000	0.000
18	A	46	ILE	0	0.011	0.001	20.581	0.015	0.015	0.000	0.000	0.000	0.000
19	A	47	GLY	0	0.027	0.019	22.145	0.014	0.014	0.000	0.000	0.000	0.000
20	A	48	ALA	0	-0.026	-0.012	23.141	0.013	0.013	0.000	0.000	0.000	0.000
21	A	49	ALA	0	-0.003	-0.001	24.891	0.009	0.009	0.000	0.000	0.000	0.000
22	A	50	LEU	0	-0.024	-0.012	26.211	0.008	0.008	0.000	0.000	0.000	0.000
23	A	51	ALA	0	-0.041	-0.014	27.508	0.007	0.007	0.000	0.000	0.000	0.000
24	A	52	LEU	0	-0.068	-0.051	27.176	0.007	0.007	0.000	0.000	0.000	0.000
25	A	53	GLY	0	-0.005	-0.002	30.211	0.001	0.001	0.000	0.000	0.000	0.000
26	A	54	HIS	0	-0.105	-0.037	31.706	0.001	0.001	0.000	0.000	0.000	0.000
27	A	55	PRO	0	0.047	0.029	31.085	0.001	0.001	0.000	0.000	0.000	0.000
28	A	56	ASP	-1	-0.813	-0.903	34.323	-0.055	-0.055	0.000	0.000	0.000	0.000
29	A	57	THR	0	0.021	-0.007	35.628	-0.003	-0.003	0.000	0.000	0.000	0.000
30	A	58	GLN	0	0.016	0.036	35.911	-0.005	-0.005	0.000	0.000	0.000	0.000
31	A	59	ILE	0	0.033	0.011	31.771	-0.005	-0.005	0.000	0.000	0.000	0.000
32	A	60	THR	0	-0.024	-0.020	31.513	-0.007	-0.007	0.000	0.000	0.000	0.000
33	A	61	ASP	-1	-0.828	-0.918	30.856	-0.057	-0.057	0.000	0.000	0.000	0.000
34	A	62	VAL	0	-0.019	0.010	29.478	-0.004	-0.004	0.000	0.000	0.000	0.000
35	A	63	LEU	0	0.012	-0.008	26.585	-0.009	-0.009	0.000	0.000	0.000	0.000
36	A	64	ARG	1	0.849	0.913	26.184	0.047	0.047	0.000	0.000	0.000	0.000
37	A	65	GLN	0	-0.044	-0.016	26.616	0.006	0.006	0.000	0.000	0.000	0.000
38	A	66	ILE	0	0.014	0.002	22.830	-0.008	-0.008	0.000	0.000	0.000	0.000
39	A	67	GLN	0	-0.042	-0.020	21.751	-0.004	-0.004	0.000	0.000	0.000	0.000
40	A	68	ASN	0	-0.033	-0.018	21.617	0.002	0.002	0.000	0.000	0.000	0.000
41	A	69	ASP	-1	-0.727	-0.797	22.274	-0.133	-0.133	0.000	0.000	0.000	0.000
42	A	70	LEU	0	0.002	-0.002	17.513	-0.023	-0.023	0.000	0.000	0.000	0.000
43	A	71	PHE	0	-0.045	0.001	17.292	-0.031	-0.031	0.000	0.000	0.000	0.000
44	A	72	ASP	-1	-0.790	-0.890	17.393	-0.128	-0.128	0.000	0.000	0.000	0.000
45	A	73	ALA	0	-0.029	-0.020	16.873	-0.014	-0.014	0.000	0.000	0.000	0.000
46	A	74	GLY	0	0.043	0.027	13.488	-0.056	-0.056	0.000	0.000	0.000	0.000
47	A	75	ALA	0	0.026	0.013	13.226	-0.031	-0.031	0.000	0.000	0.000	0.000
48	A	76	ASP	-1	-0.831	-0.891	15.041	-0.234	-0.234	0.000	0.000	0.000	0.000
49	A	77	LEU	0	-0.005	-0.021	11.462	-0.009	-0.009	0.000	0.000	0.000	0.000
50	A	78	SER	0	-0.060	-0.040	10.207	-0.046	-0.046	0.000	0.000	0.000	0.000
51	A	79	THR	0	-0.046	-0.015	11.208	0.123	0.123	0.000	0.000	0.000	0.000
52	A	80	PRO	0	-0.005	0.012	12.607	-0.055	-0.055	0.000	0.000	0.000	0.000
53	A	81	ILE	0	-0.039	-0.026	14.741	0.041	0.041	0.000	0.000	0.000	0.000
54	A	82	VAL	0	-0.035	-0.019	18.349	0.018	0.018	0.000	0.000	0.000	0.000
55	A	83	GLU	-1	-0.866	-0.944	20.958	-0.067	-0.067	0.000	0.000	0.000	0.000
56	A	84	ASN	0	-0.086	-0.035	24.613	0.013	0.013	0.000	0.000	0.000	0.000
57	A	85	PRO	0	-0.002	0.016	23.099	0.013	0.013	0.000	0.000	0.000	0.000
58	A	86	LYS	1	0.938	0.954	25.072	-0.030	-0.030	0.000	0.000	0.000	0.000
59	A	87	HIS	0	-0.019	0.007	20.526	0.015	0.015	0.000	0.000	0.000	0.000
60	A	88	PRO	0	0.032	0.001	25.434	-0.008	-0.008	0.000	0.000	0.000	0.000
61	A	89	PRO	0	-0.028	-0.006	22.522	0.002	0.002	0.000	0.000	0.000	0.000
62	A	90	LEU	0	0.018	0.017	19.551	0.003	0.003	0.000	0.000	0.000	0.000
63	A	91	ARG	1	0.754	0.845	16.193	0.165	0.165	0.000	0.000	0.000	0.000
64	A	92	ILE	0	0.001	0.019	19.546	0.014	0.014	0.000	0.000	0.000	0.000
65	A	93	ALA	0	-0.007	-0.007	22.048	-0.002	-0.002	0.000	0.000	0.000	0.000
66	A	94	GLN	0	-0.009	-0.034	25.473	-0.017	-0.017	0.000	0.000	0.000	0.000
67	A	95	SER	0	0.023	0.014	27.399	-0.004	-0.004	0.000	0.000	0.000	0.000
68	A	96	TYR	0	-0.083	-0.064	23.937	0.004	0.004	0.000	0.000	0.000	0.000
69	A	97	ILE	0	-0.009	-0.015	23.335	-0.003	-0.003	0.000	0.000	0.000	0.000
70	A	98	ASP	-1	-0.812	-0.898	26.757	-0.118	-0.118	0.000	0.000	0.000	0.000
71	A	99	ARG	1	0.786	0.872	26.608	0.122	0.122	0.000	0.000	0.000	0.000
72	A	100	LEU	0	-0.016	-0.004	24.092	0.006	0.006	0.000	0.000	0.000	0.000
73	A	101	GLU	-1	-0.794	-0.876	28.824	-0.147	-0.147	0.000	0.000	0.000	0.000
74	A	102	GLY	0	0.027	0.025	30.885	0.006	0.006	0.000	0.000	0.000	0.000
75	A	103	TRP	0	0.010	-0.016	28.084	0.003	0.003	0.000	0.000	0.000	0.000
76	A	104	CYS	0	-0.054	-0.021	29.809	0.001	0.001	0.000	0.000	0.000	0.000
77	A	105	ASP	-1	-0.880	-0.941	32.449	-0.097	-0.097	0.000	0.000	0.000	0.000
78	A	106	ALA	0	-0.084	-0.045	35.933	0.006	0.006	0.000	0.000	0.000	0.000
79	A	107	TYR	0	-0.053	-0.059	33.353	0.003	0.003	0.000	0.000	0.000	0.000
80	A	108	ASN	0	-0.021	-0.024	34.864	0.003	0.003	0.000	0.000	0.000	0.000
81	A	109	ALA	0	-0.004	0.011	36.761	0.003	0.003	0.000	0.000	0.000	0.000
82	A	110	GLY	0	-0.035	-0.009	40.142	0.003	0.003	0.000	0.000	0.000	0.000
83	A	111	LEU	0	-0.025	-0.001	36.008	0.002	0.002	0.000	0.000	0.000	0.000
84	A	112	PRO	0	-0.006	0.008	40.455	0.000	0.000	0.000	0.000	0.000	0.000
85	A	113	ALA	0	0.020	0.001	40.219	-0.004	-0.004	0.000	0.000	0.000	0.000
86	A	114	LEU	0	-0.015	-0.002	34.730	0.003	0.003	0.000	0.000	0.000	0.000
87	A	115	LYS	1	0.958	0.978	39.284	0.060	0.060	0.000	0.000	0.000	0.000
88	A	116	SER	0	-0.042	-0.035	38.522	0.000	0.000	0.000	0.000	0.000	0.000
89	A	117	PHE	0	0.034	0.019	33.081	-0.002	-0.002	0.000	0.000	0.000	0.000
90	A	118	VAL	0	0.023	0.007	31.607	0.005	0.005	0.000	0.000	0.000	0.000
91	A	119	LEU	0	-0.058	-0.030	31.002	-0.008	-0.008	0.000	0.000	0.000	0.000
92	A	120	PRO	0	-0.029	-0.023	26.840	0.003	0.003	0.000	0.000	0.000	0.000
93	A	121	GLY	0	0.028	0.007	29.337	0.003	0.003	0.000	0.000	0.000	0.000
94	A	122	GLY	0	0.001	0.002	31.324	-0.002	-0.002	0.000	0.000	0.000	0.000
95	A	123	SER	0	0.008	0.013	34.713	0.003	0.003	0.000	0.000	0.000	0.000
96	A	124	PRO	0	0.046	0.004	32.325	-0.005	-0.005	0.000	0.000	0.000	0.000
97	A	125	LEU	0	0.070	0.040	30.169	-0.006	-0.006	0.000	0.000	0.000	0.000
98	A	126	SER	0	0.052	0.003	29.821	-0.008	-0.008	0.000	0.000	0.000	0.000
99	A	127	ALA	0	-0.065	-0.027	29.224	-0.010	-0.010	0.000	0.000	0.000	0.000
100	A	128	LEU	0	0.003	0.002	26.122	-0.010	-0.010	0.000	0.000	0.000	0.000
101	A	129	LEU	0	0.027	0.023	25.058	-0.012	-0.012	0.000	0.000	0.000	0.000
102	A	130	HIS	0	0.053	0.034	25.015	-0.027	-0.027	0.000	0.000	0.000	0.000
103	A	131	VAL	0	-0.020	0.000	21.409	-0.018	-0.018	0.000	0.000	0.000	0.000
104	A	132	ALA	0	0.064	0.031	20.698	-0.023	-0.023	0.000	0.000	0.000	0.000
105	A	133	ARG	1	0.872	0.942	20.282	0.137	0.137	0.000	0.000	0.000	0.000
106	A	134	THR	0	-0.118	-0.073	20.060	-0.025	-0.025	0.000	0.000	0.000	0.000
107	A	135	VAL	0	0.019	0.016	15.120	-0.035	-0.035	0.000	0.000	0.000	0.000
108	A	136	VAL	0	0.051	0.023	15.794	-0.059	-0.059	0.000	0.000	0.000	0.000
109	A	137	ARG	1	0.854	0.916	16.804	0.254	0.254	0.000	0.000	0.000	0.000
110	A	138	ARG	1	0.688	0.805	11.281	0.404	0.404	0.000	0.000	0.000	0.000
111	A	139	ALA	0	0.063	0.024	12.231	-0.102	-0.102	0.000	0.000	0.000	0.000
112	A	140	GLU	-1	-0.807	-0.885	13.012	-0.413	-0.413	0.000	0.000	0.000	0.000
113	A	141	ARG	1	0.899	0.950	13.455	0.452	0.452	0.000	0.000	0.000	0.000
114	A	142	SER	0	0.000	-0.027	8.558	0.007	0.007	0.000	0.000	0.000	0.000
115	A	143	ALA	0	0.024	0.017	10.333	-0.129	-0.129	0.000	0.000	0.000	0.000
116	A	144	TRP	0	-0.034	-0.031	12.583	0.041	0.041	0.000	0.000	0.000	0.000
117	A	145	ALA	0	0.022	0.021	9.882	0.021	0.021	0.000	0.000	0.000	0.000
118	A	146	ALA	0	-0.020	-0.011	9.734	-0.076	-0.076	0.000	0.000	0.000	0.000
119	A	147	VAL	0	-0.034	-0.025	10.806	0.100	0.100	0.000	0.000	0.000	0.000
120	A	148	ASP	-1	-0.923	-0.964	13.376	-0.527	-0.527	0.000	0.000	0.000	0.000
121	A	149	ALA	0	-0.085	-0.031	9.925	0.038	0.038	0.000	0.000	0.000	0.000
122	A	150	HIS	0	-0.041	-0.023	8.550	0.285	0.285	0.000	0.000	0.000	0.000
123	A	151	PRO	0	0.024	0.013	13.887	0.039	0.039	0.000	0.000	0.000	0.000
124	A	152	GLU	-1	-0.908	-0.949	17.407	-0.176	-0.176	0.000	0.000	0.000	0.000
125	A	153	GLY	0	-0.037	-0.016	15.792	0.039	0.039	0.000	0.000	0.000	0.000
126	A	154	VAL	0	0.010	0.001	12.344	0.012	0.012	0.000	0.000	0.000	0.000
127	A	155	SER	0	0.070	0.051	15.675	0.020	0.020	0.000	0.000	0.000	0.000
128	A	156	VAL	0	0.052	0.001	17.041	-0.042	-0.042	0.000	0.000	0.000	0.000
129	A	157	LEU	0	-0.042	-0.020	19.153	-0.004	-0.004	0.000	0.000	0.000	0.000
130	A	158	PRO	0	0.052	0.032	15.901	0.006	0.006	0.000	0.000	0.000	0.000
131	A	159	ALA	0	0.046	0.021	16.181	0.003	0.003	0.000	0.000	0.000	0.000
132	A	160	LYS	1	0.916	0.959	17.515	0.278	0.278	0.000	0.000	0.000	0.000
133	A	161	TYR	0	0.019	-0.018	20.016	0.015	0.015	0.000	0.000	0.000	0.000
134	A	162	LEU	0	0.008	-0.006	15.191	0.020	0.020	0.000	0.000	0.000	0.000
135	A	163	ASN	0	-0.090	-0.043	19.494	0.036	0.036	0.000	0.000	0.000	0.000
136	A	164	ARG	1	0.846	0.900	21.505	0.206	0.206	0.000	0.000	0.000	0.000
137	A	165	LEU	0	0.008	0.014	20.423	0.015	0.015	0.000	0.000	0.000	0.000
138	A	166	SER	0	-0.053	-0.026	21.388	0.014	0.014	0.000	0.000	0.000	0.000
139	A	167	ASP	-1	-0.867	-0.937	23.347	-0.174	-0.174	0.000	0.000	0.000	0.000
140	A	168	LEU	0	0.024	0.002	26.560	0.014	0.014	0.000	0.000	0.000	0.000
141	A	169	LEU	0	0.011	0.002	22.801	0.012	0.012	0.000	0.000	0.000	0.000
142	A	170	PHE	0	-0.038	-0.004	26.894	0.011	0.011	0.000	0.000	0.000	0.000
143	A	171	ILE	0	-0.014	-0.002	28.665	0.010	0.010	0.000	0.000	0.000	0.000
144	A	172	LEU	0	0.030	0.007	28.955	0.008	0.008	0.000	0.000	0.000	0.000
145	A	173	SER	0	-0.063	-0.049	28.702	0.007	0.007	0.000	0.000	0.000	0.000
146	A	174	ARG	1	0.809	0.898	31.245	0.092	0.092	0.000	0.000	0.000	0.000
147	A	175	VAL	0	-0.022	-0.003	34.337	0.006	0.006	0.000	0.000	0.000	0.000
148	A	176	ALA	0	-0.019	-0.002	33.230	0.006	0.006	0.000	0.000	0.000	0.000
149	A	177	ASN	0	-0.056	-0.014	33.951	0.007	0.007	0.000	0.000	0.000	0.000
150	A	178	PRO	0	0.027	0.016	37.100	-0.001	-0.001	0.000	0.000	0.000	0.000
151	A	179	ASP	-1	-0.949	-0.971	40.690	-0.048	-0.048	0.000	0.000	0.000	0.000
152	A	180	GLY	0	-0.042	-0.010	40.208	0.001	0.001	0.000	0.000	0.000	0.000
153	A	181	ASP	-1	-0.811	-0.902	35.163	-0.086	-0.086	0.000	0.000	0.000	0.000
154	A	182	VAL	0	0.004	0.007	34.203	0.004	0.004	0.000	0.000	0.000	0.000
155	A	183	LEU	0	-0.040	-0.017	35.053	-0.005	-0.005	0.000	0.000	0.000	0.000
156	A	184	TRP	0	0.048	0.017	34.255	0.004	0.004	0.000	0.000	0.000	0.000
157	A	185	ARG	1	0.944	0.969	36.372	0.061	0.061	0.000	0.000	0.000	0.000
158	A	186	PRO	0	0.006	0.006	38.879	-0.001	-0.001	0.000	0.000	0.000	0.000
159	A	187	GLY	0	0.001	0.010	39.392	0.003	0.003	0.000	0.000	0.000	0.000
160	A	188	GLY	0	-0.006	0.009	40.554	0.004	0.004	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:29:THR)