FMO DATABASE

FMODB ID: KGV93

Calculation Name: 2GEC-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2GEC

Chain ID: A

ChEMBL ID:

UniProt ID: P32923

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	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	138
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1205737.714384
FMO2-HF: Nuclear repulsion	1152597.674842
FMO2-HF: Total energy	-53140.039543
FMO2-MP2: Total energy	-53299.767844

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:23:ARG)

Summations of interaction energy for fragment #1(A:23:ARG)

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.
89.879	93.018	0.653	-1.479	-2.312	-0.013

Interaction energy analysis for fragmet #1(A:23:ARG)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.956 / q_NPA : 0.964

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	25	PRO	0	0.028	0.003	2.652	-10.729	-7.800	0.654	-1.472	-2.111	-0.013
4	A	26	LYS	1	0.968	0.972	4.707	43.566	43.776	-0.001	-0.007	-0.201	0.000
5	A	27	VAL	0	-0.009	-0.016	6.800	1.285	1.285	0.000	0.000	0.000	0.000
6	A	28	GLY	0	0.046	0.021	10.241	0.392	0.392	0.000	0.000	0.000	0.000
7	A	29	SER	0	-0.028	-0.018	12.858	1.196	1.196	0.000	0.000	0.000	0.000
8	A	30	SER	0	0.042	0.019	16.067	-0.102	-0.102	0.000	0.000	0.000	0.000
9	A	31	GLY	0	0.027	0.008	18.600	0.589	0.589	0.000	0.000	0.000	0.000
10	A	32	ASN	0	0.002	0.009	16.838	0.457	0.457	0.000	0.000	0.000	0.000
11	A	33	ALA	0	0.021	0.051	20.949	0.194	0.194	0.000	0.000	0.000	0.000
12	A	34	SER	0	0.017	-0.018	24.134	0.282	0.282	0.000	0.000	0.000	0.000
13	A	35	TRP	0	0.047	0.022	27.090	0.148	0.148	0.000	0.000	0.000	0.000
14	A	36	PHE	0	0.013	0.023	29.993	0.231	0.231	0.000	0.000	0.000	0.000
15	A	37	GLN	0	-0.004	-0.003	30.869	-0.174	-0.174	0.000	0.000	0.000	0.000
16	A	38	ALA	0	-0.047	-0.017	30.300	-0.022	-0.022	0.000	0.000	0.000	0.000
17	A	39	ILE	0	0.016	0.021	31.974	0.338	0.338	0.000	0.000	0.000	0.000
18	A	40	LYS	1	0.884	0.924	32.696	8.819	8.819	0.000	0.000	0.000	0.000
19	A	41	ALA	0	0.057	0.045	33.854	0.276	0.276	0.000	0.000	0.000	0.000
20	A	42	LYS	1	0.872	0.933	35.712	7.431	7.431	0.000	0.000	0.000	0.000
21	A	43	LYS	1	0.887	0.941	37.366	7.734	7.734	0.000	0.000	0.000	0.000
22	A	44	LEU	0	-0.019	-0.030	33.239	-0.163	-0.163	0.000	0.000	0.000	0.000
23	A	45	ASN	0	0.025	0.017	33.522	-0.420	-0.420	0.000	0.000	0.000	0.000
24	A	46	SER	0	-0.023	0.002	35.408	0.268	0.268	0.000	0.000	0.000	0.000
25	A	47	PRO	0	0.048	0.024	34.611	-0.251	-0.251	0.000	0.000	0.000	0.000
26	A	48	GLN	0	0.011	0.018	31.696	-0.361	-0.361	0.000	0.000	0.000	0.000
27	A	49	PRO	0	-0.043	-0.020	32.390	0.250	0.250	0.000	0.000	0.000	0.000
28	A	50	LYS	1	0.964	0.989	35.536	7.589	7.589	0.000	0.000	0.000	0.000
29	A	51	PHE	0	-0.003	-0.019	34.665	-0.029	-0.029	0.000	0.000	0.000	0.000
30	A	52	GLU	-1	-0.967	-0.952	40.266	-6.708	-6.708	0.000	0.000	0.000	0.000
31	A	53	GLY	0	0.036	0.025	42.892	0.112	0.112	0.000	0.000	0.000	0.000
32	A	54	SER	0	-0.104	-0.071	39.032	-0.221	-0.221	0.000	0.000	0.000	0.000
33	A	55	GLY	0	0.040	-0.001	37.094	-0.211	-0.211	0.000	0.000	0.000	0.000
34	A	56	VAL	0	-0.051	-0.023	35.118	-0.352	-0.352	0.000	0.000	0.000	0.000
35	A	57	PRO	0	-0.075	-0.032	34.045	0.226	0.226	0.000	0.000	0.000	0.000
36	A	58	ASP	-1	-0.747	-0.845	37.285	-7.415	-7.415	0.000	0.000	0.000	0.000
37	A	59	ASN	0	-0.058	-0.066	34.676	0.034	0.034	0.000	0.000	0.000	0.000
38	A	60	GLU	-1	-0.897	-0.947	38.645	-7.108	-7.108	0.000	0.000	0.000	0.000
39	A	61	ASN	0	-0.076	-0.032	34.771	0.206	0.206	0.000	0.000	0.000	0.000
40	A	62	LEU	0	-0.046	-0.005	33.519	-0.165	-0.165	0.000	0.000	0.000	0.000
41	A	63	LYS	1	1.010	0.994	37.686	8.155	8.155	0.000	0.000	0.000	0.000
42	A	64	THR	0	0.066	0.025	38.622	-0.201	-0.201	0.000	0.000	0.000	0.000
43	A	65	SER	0	0.019	0.011	37.715	-0.074	-0.074	0.000	0.000	0.000	0.000
44	A	66	GLN	0	-0.029	-0.027	34.314	-0.066	-0.066	0.000	0.000	0.000	0.000
45	A	67	GLN	0	0.000	0.015	34.154	-0.465	-0.465	0.000	0.000	0.000	0.000
46	A	68	HIS	0	0.028	0.031	30.587	-0.027	-0.027	0.000	0.000	0.000	0.000
47	A	69	GLY	0	0.026	0.009	29.582	-0.222	-0.222	0.000	0.000	0.000	0.000
48	A	70	TYR	0	-0.058	-0.034	23.152	-0.023	-0.023	0.000	0.000	0.000	0.000
49	A	71	TRP	0	-0.018	-0.007	28.738	-0.219	-0.219	0.000	0.000	0.000	0.000
50	A	72	ARG	1	0.968	0.972	19.060	14.441	14.441	0.000	0.000	0.000	0.000
51	A	73	ARG	1	0.770	0.880	24.512	11.927	11.927	0.000	0.000	0.000	0.000
52	A	74	GLN	0	-0.039	-0.021	23.211	-0.657	-0.657	0.000	0.000	0.000	0.000
53	A	75	ALA	0	0.076	0.037	24.258	0.496	0.496	0.000	0.000	0.000	0.000
54	A	76	ARG	1	0.853	0.910	25.296	9.740	9.740	0.000	0.000	0.000	0.000
55	A	77	PHE	0	-0.012	-0.024	24.133	0.192	0.192	0.000	0.000	0.000	0.000
56	A	78	LYS	1	0.955	0.998	28.417	8.842	8.842	0.000	0.000	0.000	0.000
57	A	79	PRO	0	0.204	0.103	30.181	-0.211	-0.211	0.000	0.000	0.000	0.000
58	A	80	GLY	0	-0.109	-0.053	31.218	0.327	0.327	0.000	0.000	0.000	0.000
59	A	81	LYS	1	0.890	1.109	31.555	8.077	8.077	0.000	0.000	0.000	0.000
60	A	82	GLY	0	0.073	-0.121	32.370	0.209	0.209	0.000	0.000	0.000	0.000
61	A	83	ARG	1	0.957	0.957	25.287	10.976	10.976	0.000	0.000	0.000	0.000
62	A	84	ARG	1	1.009	1.023	21.210	13.500	13.500	0.000	0.000	0.000	0.000
63	A	85	LYS	1	0.925	0.965	28.682	9.330	9.330	0.000	0.000	0.000	0.000
64	A	86	PRO	0	0.075	0.025	29.613	-0.042	-0.042	0.000	0.000	0.000	0.000
65	A	87	VAL	0	-0.072	-0.050	30.529	0.439	0.439	0.000	0.000	0.000	0.000
66	A	88	PRO	0	0.024	0.022	31.356	-0.267	-0.267	0.000	0.000	0.000	0.000
67	A	89	ASP	-1	-0.790	-0.883	29.295	-10.819	-10.819	0.000	0.000	0.000	0.000
68	A	90	ALA	0	-0.084	-0.037	28.606	0.425	0.425	0.000	0.000	0.000	0.000
69	A	91	TRP	0	0.046	0.013	28.601	-0.425	-0.425	0.000	0.000	0.000	0.000
70	A	92	TYR	0	0.016	0.001	26.535	0.426	0.426	0.000	0.000	0.000	0.000
71	A	93	PHE	0	0.097	0.047	28.081	-0.264	-0.264	0.000	0.000	0.000	0.000
72	A	94	TYR	0	-0.057	-0.033	23.491	-0.172	-0.172	0.000	0.000	0.000	0.000
73	A	95	TYR	0	0.098	0.062	27.600	0.127	0.127	0.000	0.000	0.000	0.000
74	A	96	THR	0	0.000	-0.040	26.704	-0.565	-0.565	0.000	0.000	0.000	0.000
75	A	97	GLY	0	0.004	0.025	23.645	0.189	0.189	0.000	0.000	0.000	0.000
76	A	98	THR	0	-0.057	-0.025	22.813	-0.353	-0.353	0.000	0.000	0.000	0.000
77	A	99	GLY	0	0.049	0.029	21.600	0.179	0.179	0.000	0.000	0.000	0.000
78	A	100	PRO	0	-0.058	-0.037	18.391	-0.513	-0.513	0.000	0.000	0.000	0.000
79	A	101	ALA	0	-0.029	-0.021	18.158	-0.869	-0.869	0.000	0.000	0.000	0.000
80	A	102	ALA	0	-0.035	0.006	19.438	0.493	0.493	0.000	0.000	0.000	0.000
81	A	103	ASP	-1	-0.880	-0.949	16.281	-17.185	-17.185	0.000	0.000	0.000	0.000
82	A	104	LEU	0	-0.096	-0.025	19.796	0.278	0.278	0.000	0.000	0.000	0.000
83	A	105	ASN	0	-0.067	-0.034	22.454	0.466	0.466	0.000	0.000	0.000	0.000
84	A	106	TRP	0	-0.015	-0.030	25.798	0.045	0.045	0.000	0.000	0.000	0.000
85	A	107	GLY	0	-0.001	-0.011	28.863	0.205	0.205	0.000	0.000	0.000	0.000
86	A	108	ASP	-1	-0.872	-0.919	24.473	-12.134	-12.134	0.000	0.000	0.000	0.000
87	A	109	SER	0	-0.019	-0.002	26.520	-0.061	-0.061	0.000	0.000	0.000	0.000
88	A	110	GLN	0	0.048	0.003	20.495	-0.815	-0.815	0.000	0.000	0.000	0.000
89	A	111	ASP	-1	-0.778	-0.861	23.873	-11.521	-11.521	0.000	0.000	0.000	0.000
90	A	112	GLY	0	-0.050	-0.029	24.016	-0.465	-0.465	0.000	0.000	0.000	0.000
91	A	113	ILE	0	-0.013	0.002	23.043	-0.115	-0.115	0.000	0.000	0.000	0.000
92	A	114	VAL	0	-0.029	-0.011	26.758	0.220	0.220	0.000	0.000	0.000	0.000
93	A	115	TRP	0	-0.023	-0.007	25.358	0.083	0.083	0.000	0.000	0.000	0.000
94	A	116	VAL	0	-0.026	-0.007	31.186	0.246	0.246	0.000	0.000	0.000	0.000
95	A	117	ALA	0	0.012	-0.001	33.665	-0.218	-0.218	0.000	0.000	0.000	0.000
96	A	118	ALA	0	0.041	0.030	36.208	0.192	0.192	0.000	0.000	0.000	0.000
97	A	119	LYS	1	0.996	0.988	39.574	6.741	6.741	0.000	0.000	0.000	0.000
98	A	120	GLY	0	-0.010	-0.013	42.064	0.075	0.075	0.000	0.000	0.000	0.000
99	A	121	ALA	0	-0.045	-0.005	36.416	-0.039	-0.039	0.000	0.000	0.000	0.000
100	A	122	ASP	-1	-0.889	-0.948	35.682	-8.666	-8.666	0.000	0.000	0.000	0.000
101	A	123	VAL	0	0.035	0.008	32.154	-0.169	-0.169	0.000	0.000	0.000	0.000
102	A	124	LYS	1	0.961	0.982	28.636	10.113	10.113	0.000	0.000	0.000	0.000
103	A	125	SER	0	-0.040	-0.002	31.019	-0.273	-0.273	0.000	0.000	0.000	0.000
104	A	126	ARG	1	0.930	0.942	25.852	11.007	11.007	0.000	0.000	0.000	0.000
105	A	127	SER	0	0.000	0.012	30.295	0.168	0.168	0.000	0.000	0.000	0.000
106	A	128	ASN	0	0.022	0.006	28.876	-0.567	-0.567	0.000	0.000	0.000	0.000
107	A	129	GLN	0	0.032	0.032	29.459	0.237	0.237	0.000	0.000	0.000	0.000
108	A	130	GLY	0	0.036	0.025	25.729	-0.054	-0.054	0.000	0.000	0.000	0.000
109	A	131	THR	0	-0.089	-0.049	22.555	0.161	0.161	0.000	0.000	0.000	0.000
110	A	132	ARG	1	0.858	0.936	25.679	10.720	10.720	0.000	0.000	0.000	0.000
111	A	133	ASP	-1	-0.824	-0.924	24.649	-12.057	-12.057	0.000	0.000	0.000	0.000
112	A	134	PRO	0	-0.086	-0.066	23.875	0.413	0.413	0.000	0.000	0.000	0.000
113	A	135	ASP	-1	-0.940	-0.968	25.516	-10.497	-10.497	0.000	0.000	0.000	0.000
114	A	136	LYS	1	0.917	0.986	27.060	10.975	10.975	0.000	0.000	0.000	0.000
115	A	137	PHE	0	-0.017	-0.013	29.411	0.330	0.330	0.000	0.000	0.000	0.000
116	A	138	ASP	-1	-0.836	-0.906	30.385	-9.176	-9.176	0.000	0.000	0.000	0.000
117	A	139	GLN	0	-0.105	-0.065	31.354	-0.316	-0.316	0.000	0.000	0.000	0.000
118	A	140	TYR	0	0.046	0.017	32.509	0.344	0.344	0.000	0.000	0.000	0.000
119	A	141	PRO	0	-0.032	-0.027	35.259	-0.167	-0.167	0.000	0.000	0.000	0.000
120	A	142	LEU	0	-0.006	0.004	34.442	-0.050	-0.050	0.000	0.000	0.000	0.000
121	A	143	ARG	1	0.829	0.905	37.995	7.591	7.591	0.000	0.000	0.000	0.000
122	A	144	PHE	0	0.042	0.014	36.648	-0.205	-0.205	0.000	0.000	0.000	0.000
123	A	145	SER	0	-0.056	-0.060	42.109	0.183	0.183	0.000	0.000	0.000	0.000
124	A	146	ASP	-1	-0.841	-0.902	42.487	-7.374	-7.374	0.000	0.000	0.000	0.000
125	A	147	GLY	0	0.089	0.051	44.828	0.046	0.046	0.000	0.000	0.000	0.000
126	A	148	GLY	0	-0.030	-0.024	41.168	-0.188	-0.188	0.000	0.000	0.000	0.000
127	A	149	PRO	0	-0.049	-0.019	38.007	0.052	0.052	0.000	0.000	0.000	0.000
128	A	150	ASP	-1	-0.741	-0.869	40.043	-7.778	-7.778	0.000	0.000	0.000	0.000
129	A	151	GLY	0	0.058	0.018	41.355	-0.083	-0.083	0.000	0.000	0.000	0.000
130	A	152	ASN	0	-0.107	-0.069	38.844	0.101	0.101	0.000	0.000	0.000	0.000
131	A	153	PHE	0	-0.051	-0.024	34.009	-0.242	-0.242	0.000	0.000	0.000	0.000
132	A	154	ARG	1	0.942	0.968	36.717	8.453	8.453	0.000	0.000	0.000	0.000
133	A	155	TRP	0	-0.008	-0.020	37.110	-0.350	-0.350	0.000	0.000	0.000	0.000
134	A	156	ASP	-1	-0.910	-0.944	37.704	-7.833	-7.833	0.000	0.000	0.000	0.000
135	A	157	PHE	0	0.017	0.012	39.545	-0.088	-0.088	0.000	0.000	0.000	0.000
136	A	158	ILE	0	0.004	0.012	36.329	-0.052	-0.052	0.000	0.000	0.000	0.000
137	A	159	PRO	0	0.023	0.025	40.938	0.045	0.045	0.000	0.000	0.000	0.000
138	A	160	LEU	0	0.032	0.016	42.150	-0.101	-0.101	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:23:ARG)