FMO DATABASE

FMODB ID: 7289K

Calculation Name: 1G1K-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1G1K

Chain ID: A

ChEMBL ID:

UniProt ID: Q45996

Base Structure: X-ray

Registration Date: 2023-09-20

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	143
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1128497.41917
FMO2-HF: Nuclear repulsion	1077354.967387
FMO2-HF: Total energy	-51142.451783
FMO2-MP2: Total energy	-51292.626311

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:2:ALA)

Summations of interaction energy for fragment #1(A:2:ALA)

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.
-4.007	-0.579	2.06	-2.264	-3.224	-0.007

Interaction energy analysis for fragmet #1(A:2:ALA)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.038 / q_NPA : -0.021

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	4	LEU	0	0.052	0.052	3.627	-1.091	1.752	-0.085	-1.407	-1.351	0.000
4	A	5	LYS	1	0.833	0.899	4.352	-1.593	-1.534	-0.001	-0.008	-0.051	0.000
5	A	6	VAL	0	0.007	0.005	8.805	-0.018	-0.018	0.000	0.000	0.000	0.000
6	A	7	THR	0	-0.020	-0.013	12.474	0.056	0.056	0.000	0.000	0.000	0.000
7	A	8	VAL	0	-0.024	0.006	14.971	-0.023	-0.023	0.000	0.000	0.000	0.000
8	A	9	GLY	0	0.003	-0.001	18.744	0.027	0.027	0.000	0.000	0.000	0.000
9	A	10	THR	0	-0.036	-0.033	20.659	-0.007	-0.007	0.000	0.000	0.000	0.000
10	A	11	ALA	0	0.018	0.024	23.922	-0.001	-0.001	0.000	0.000	0.000	0.000
11	A	12	ASN	0	-0.018	-0.024	27.493	-0.002	-0.002	0.000	0.000	0.000	0.000
12	A	13	GLY	0	0.038	0.020	30.742	-0.001	-0.001	0.000	0.000	0.000	0.000
13	A	14	LYS	1	0.954	0.990	34.202	-0.041	-0.041	0.000	0.000	0.000	0.000
14	A	15	PRO	0	-0.022	-0.018	37.626	-0.003	-0.003	0.000	0.000	0.000	0.000
15	A	16	GLY	0	-0.016	-0.002	38.733	0.000	0.000	0.000	0.000	0.000	0.000
16	A	17	ASP	-1	-0.856	-0.915	36.019	0.030	0.030	0.000	0.000	0.000	0.000
17	A	18	THR	0	-0.038	-0.036	33.272	-0.004	-0.004	0.000	0.000	0.000	0.000
18	A	19	VAL	0	-0.026	-0.003	29.280	0.004	0.004	0.000	0.000	0.000	0.000
19	A	20	THR	0	0.005	-0.017	25.938	-0.009	-0.009	0.000	0.000	0.000	0.000
20	A	21	VAL	0	-0.017	-0.006	22.869	0.011	0.011	0.000	0.000	0.000	0.000
21	A	22	PRO	0	0.001	0.013	20.767	-0.012	-0.012	0.000	0.000	0.000	0.000
22	A	23	VAL	0	0.038	0.020	17.268	0.013	0.013	0.000	0.000	0.000	0.000
23	A	24	THR	0	-0.040	-0.030	15.313	-0.002	-0.002	0.000	0.000	0.000	0.000
24	A	25	PHE	0	0.031	0.011	11.697	-0.027	-0.027	0.000	0.000	0.000	0.000
25	A	26	ALA	0	0.046	0.006	9.049	0.050	0.050	0.000	0.000	0.000	0.000
26	A	27	ASP	-1	-0.867	-0.935	4.941	1.059	1.059	0.000	0.000	0.000	0.000
27	A	28	VAL	0	0.022	0.011	5.856	-0.335	-0.335	0.000	0.000	0.000	0.000
28	A	29	ALA	0	0.039	0.018	7.715	-0.136	-0.136	0.000	0.000	0.000	0.000
29	A	30	LYS	1	0.849	0.926	3.355	-1.557	-1.298	0.014	-0.052	-0.221	0.000
30	A	31	MET	0	-0.066	0.003	2.894	-1.632	-1.535	2.134	-0.764	-1.467	-0.007
31	A	32	LYS	1	0.906	0.948	5.178	0.877	0.889	-0.001	-0.001	-0.009	0.000
32	A	33	ASN	0	0.082	0.029	8.703	0.082	0.082	0.000	0.000	0.000	0.000
33	A	34	VAL	0	-0.040	0.049	10.471	-0.116	-0.116	0.000	0.000	0.000	0.000
34	A	35	GLY	0	0.080	0.054	12.488	0.066	0.066	0.000	0.000	0.000	0.000
35	A	36	THR	0	-0.036	-0.006	15.112	0.029	0.029	0.000	0.000	0.000	0.000
36	A	37	CYS	0	-0.069	-0.030	14.814	-0.052	-0.052	0.000	0.000	0.000	0.000
37	A	38	ASN	0	0.053	0.022	16.688	0.056	0.056	0.000	0.000	0.000	0.000
38	A	39	PHE	0	-0.032	-0.004	16.892	-0.032	-0.032	0.000	0.000	0.000	0.000
39	A	40	TYR	0	0.080	0.038	19.493	0.013	0.013	0.000	0.000	0.000	0.000
40	A	41	LEU	0	-0.032	-0.006	19.391	0.002	0.002	0.000	0.000	0.000	0.000
41	A	42	GLY	0	-0.005	-0.043	22.993	-0.003	-0.003	0.000	0.000	0.000	0.000
42	A	43	TYR	0	-0.042	-0.017	25.585	0.011	0.011	0.000	0.000	0.000	0.000
43	A	44	ASP	-1	-0.750	-0.864	28.258	0.005	0.005	0.000	0.000	0.000	0.000
44	A	45	ALA	0	0.047	0.029	31.603	0.003	0.003	0.000	0.000	0.000	0.000
45	A	46	SER	0	-0.085	-0.042	34.265	0.001	0.001	0.000	0.000	0.000	0.000
46	A	47	LEU	0	-0.005	-0.009	32.751	0.003	0.003	0.000	0.000	0.000	0.000
47	A	48	LEU	0	-0.045	-0.025	29.558	0.003	0.003	0.000	0.000	0.000	0.000
48	A	49	GLU	-1	-0.912	-0.962	33.556	-0.008	-0.008	0.000	0.000	0.000	0.000
49	A	50	VAL	0	-0.032	-0.012	29.839	0.003	0.003	0.000	0.000	0.000	0.000
50	A	51	VAL	0	-0.008	0.003	32.366	-0.002	-0.002	0.000	0.000	0.000	0.000
51	A	52	SER	0	-0.005	-0.013	31.496	-0.001	-0.001	0.000	0.000	0.000	0.000
52	A	53	VAL	0	-0.007	-0.003	25.333	0.005	0.005	0.000	0.000	0.000	0.000
53	A	54	ASP	-1	-0.922	-0.950	26.555	-0.033	-0.033	0.000	0.000	0.000	0.000
54	A	55	ALA	0	0.016	0.010	22.883	0.002	0.002	0.000	0.000	0.000	0.000
55	A	56	GLY	0	-0.029	-0.023	21.535	0.013	0.013	0.000	0.000	0.000	0.000
56	A	57	PRO	0	-0.005	-0.029	21.074	-0.009	-0.009	0.000	0.000	0.000	0.000
57	A	58	ILE	0	-0.063	-0.009	14.897	-0.003	-0.003	0.000	0.000	0.000	0.000
58	A	59	VAL	0	-0.034	-0.004	18.207	-0.026	-0.026	0.000	0.000	0.000	0.000
59	A	60	LYS	1	0.835	0.931	17.829	0.145	0.145	0.000	0.000	0.000	0.000
60	A	61	ASN	0	0.012	0.008	22.597	0.000	0.000	0.000	0.000	0.000	0.000
61	A	62	ALA	0	0.054	0.015	24.534	-0.007	-0.007	0.000	0.000	0.000	0.000
62	A	63	ALA	0	-0.038	-0.024	25.486	-0.004	-0.004	0.000	0.000	0.000	0.000
63	A	64	VAL	0	-0.015	0.004	26.691	0.001	0.001	0.000	0.000	0.000	0.000
64	A	65	ASN	0	0.008	0.007	22.117	-0.012	-0.012	0.000	0.000	0.000	0.000
65	A	66	PHE	0	-0.038	-0.021	21.314	-0.015	-0.015	0.000	0.000	0.000	0.000
66	A	67	SER	0	-0.003	0.005	24.065	0.014	0.014	0.000	0.000	0.000	0.000
67	A	68	SER	0	-0.017	-0.007	24.754	-0.005	-0.005	0.000	0.000	0.000	0.000
68	A	69	SER	0	0.007	0.008	26.568	0.006	0.006	0.000	0.000	0.000	0.000
69	A	70	ALA	0	0.028	0.012	28.330	-0.004	-0.004	0.000	0.000	0.000	0.000
70	A	71	SER	0	-0.013	-0.003	30.324	0.006	0.006	0.000	0.000	0.000	0.000
71	A	72	ASN	0	0.026	-0.010	31.932	0.001	0.001	0.000	0.000	0.000	0.000
72	A	73	GLY	0	0.021	0.027	30.845	-0.001	-0.001	0.000	0.000	0.000	0.000
73	A	74	THR	0	-0.032	-0.025	26.439	0.000	0.000	0.000	0.000	0.000	0.000
74	A	75	ILE	0	-0.011	0.005	25.173	0.003	0.003	0.000	0.000	0.000	0.000
75	A	76	SER	0	0.011	0.012	24.244	-0.009	-0.009	0.000	0.000	0.000	0.000
76	A	77	PHE	0	-0.021	-0.027	20.455	0.015	0.015	0.000	0.000	0.000	0.000
77	A	78	LEU	0	0.015	0.003	21.110	-0.021	-0.021	0.000	0.000	0.000	0.000
78	A	79	PHE	0	0.018	-0.006	17.376	0.020	0.020	0.000	0.000	0.000	0.000
79	A	80	LEU	0	-0.048	-0.047	19.522	-0.032	-0.032	0.000	0.000	0.000	0.000
80	A	81	ASP	-1	-0.748	-0.869	19.432	-0.167	-0.167	0.000	0.000	0.000	0.000
81	A	82	ASN	0	-0.035	-0.036	19.423	-0.039	-0.039	0.000	0.000	0.000	0.000
82	A	83	THR	0	-0.051	-0.049	21.198	-0.004	-0.004	0.000	0.000	0.000	0.000
83	A	84	ILE	0	0.009	0.037	22.465	0.006	0.006	0.000	0.000	0.000	0.000
84	A	85	THR	0	0.041	0.018	18.384	-0.009	-0.009	0.000	0.000	0.000	0.000
85	A	86	ASP	-1	-0.966	-0.984	19.159	-0.117	-0.117	0.000	0.000	0.000	0.000
86	A	87	GLU	-1	-0.869	-0.949	21.133	-0.100	-0.100	0.000	0.000	0.000	0.000
87	A	88	LEU	0	0.019	0.030	15.290	-0.014	-0.014	0.000	0.000	0.000	0.000
88	A	89	ILE	0	-0.037	0.010	13.593	0.030	0.030	0.000	0.000	0.000	0.000
89	A	90	THR	0	0.008	-0.026	12.880	-0.042	-0.042	0.000	0.000	0.000	0.000
90	A	91	ALA	0	-0.055	-0.022	12.796	0.017	0.017	0.000	0.000	0.000	0.000
91	A	92	ASP	-1	-0.784	-0.871	10.567	0.079	0.079	0.000	0.000	0.000	0.000
92	A	93	GLY	0	0.007	-0.015	13.180	0.011	0.011	0.000	0.000	0.000	0.000
93	A	94	VAL	0	-0.026	-0.020	15.998	-0.011	-0.011	0.000	0.000	0.000	0.000
94	A	95	PHE	0	0.032	0.023	16.325	-0.009	-0.009	0.000	0.000	0.000	0.000
95	A	96	ALA	0	0.035	0.018	18.355	-0.008	-0.008	0.000	0.000	0.000	0.000
96	A	97	ASN	0	-0.026	-0.018	21.724	0.024	0.024	0.000	0.000	0.000	0.000
97	A	98	ILE	0	0.028	0.026	23.180	-0.008	-0.008	0.000	0.000	0.000	0.000
98	A	99	LYS	1	0.926	0.970	26.620	0.014	0.014	0.000	0.000	0.000	0.000
99	A	100	PHE	0	0.031	0.008	26.306	-0.006	-0.006	0.000	0.000	0.000	0.000
100	A	101	LYS	1	0.982	0.995	31.615	0.001	0.001	0.000	0.000	0.000	0.000
101	A	102	LEU	0	-0.036	-0.016	32.176	-0.002	-0.002	0.000	0.000	0.000	0.000
102	A	103	LYS	1	0.908	0.954	35.728	-0.002	-0.002	0.000	0.000	0.000	0.000
103	A	104	SER	0	-0.014	-0.015	38.282	0.003	0.003	0.000	0.000	0.000	0.000
104	A	105	VAL	0	0.032	0.018	36.652	-0.001	-0.001	0.000	0.000	0.000	0.000
105	A	106	THR	0	-0.022	-0.007	40.098	0.000	0.000	0.000	0.000	0.000	0.000
106	A	107	ALA	0	0.038	0.000	39.817	0.001	0.001	0.000	0.000	0.000	0.000
107	A	108	LYS	1	0.952	0.983	32.969	-0.074	-0.074	0.000	0.000	0.000	0.000
108	A	109	THR	0	-0.033	-0.023	33.003	0.001	0.001	0.000	0.000	0.000	0.000
109	A	110	THR	0	-0.037	-0.013	27.612	-0.001	-0.001	0.000	0.000	0.000	0.000
110	A	111	THR	0	0.005	-0.001	29.295	0.001	0.001	0.000	0.000	0.000	0.000
111	A	112	PRO	0	0.018	-0.002	24.517	0.004	0.004	0.000	0.000	0.000	0.000
112	A	113	VAL	0	0.006	0.018	23.053	-0.011	-0.011	0.000	0.000	0.000	0.000
113	A	114	THR	0	-0.045	-0.039	21.143	0.008	0.008	0.000	0.000	0.000	0.000
114	A	115	PHE	0	0.028	0.016	15.823	-0.021	-0.021	0.000	0.000	0.000	0.000
115	A	116	LYS	1	0.865	0.967	19.859	0.063	0.063	0.000	0.000	0.000	0.000
116	A	117	ASP	-1	-0.885	-0.955	21.274	-0.104	-0.104	0.000	0.000	0.000	0.000
117	A	118	GLY	0	-0.053	-0.008	18.052	-0.019	-0.019	0.000	0.000	0.000	0.000
118	A	119	GLY	0	0.024	-0.008	17.992	0.019	0.019	0.000	0.000	0.000	0.000
119	A	120	ALA	0	-0.087	-0.038	15.642	-0.029	-0.029	0.000	0.000	0.000	0.000
120	A	121	PHE	0	0.007	-0.008	11.626	0.030	0.030	0.000	0.000	0.000	0.000
121	A	122	GLY	0	0.045	0.027	12.412	-0.101	-0.101	0.000	0.000	0.000	0.000
122	A	123	ASP	-1	-0.728	-0.896	9.735	-0.683	-0.683	0.000	0.000	0.000	0.000
123	A	124	GLY	0	-0.021	-0.038	11.696	0.073	0.073	0.000	0.000	0.000	0.000
124	A	125	THR	0	-0.136	-0.082	12.254	0.048	0.048	0.000	0.000	0.000	0.000
125	A	126	MET	0	-0.008	0.000	14.910	0.021	0.021	0.000	0.000	0.000	0.000
126	A	127	SER	0	-0.036	-0.005	11.736	0.021	0.021	0.000	0.000	0.000	0.000
127	A	128	LYS	1	0.921	0.963	11.130	0.773	0.773	0.000	0.000	0.000	0.000
128	A	129	ILE	0	0.027	0.015	6.754	-0.149	-0.149	0.000	0.000	0.000	0.000
129	A	130	ALA	0	-0.044	-0.034	5.237	0.046	0.046	0.000	0.000	0.000	0.000
130	A	131	SER	0	-0.010	-0.006	4.365	0.403	0.561	-0.001	-0.032	-0.125	0.000
131	A	132	VAL	0	0.033	0.013	6.418	-0.327	-0.327	0.000	0.000	0.000	0.000
132	A	133	THR	0	-0.031	-0.007	7.525	0.225	0.225	0.000	0.000	0.000	0.000
133	A	134	LYS	1	0.932	0.972	9.384	0.276	0.276	0.000	0.000	0.000	0.000
134	A	135	THR	0	0.020	0.019	12.651	0.074	0.074	0.000	0.000	0.000	0.000
135	A	136	ASN	0	0.031	0.007	15.122	-0.046	-0.046	0.000	0.000	0.000	0.000
136	A	137	GLY	0	0.092	0.052	18.871	0.028	0.028	0.000	0.000	0.000	0.000
137	A	138	SER	0	-0.117	-0.058	21.236	-0.006	-0.006	0.000	0.000	0.000	0.000
138	A	139	VAL	0	0.052	0.026	24.991	0.003	0.003	0.000	0.000	0.000	0.000
139	A	140	THR	0	-0.051	-0.018	28.274	0.001	0.001	0.000	0.000	0.000	0.000
140	A	141	ILE	0	0.020	0.010	30.884	-0.001	-0.001	0.000	0.000	0.000	0.000
141	A	142	ASP	-1	-0.892	-0.985	34.432	0.056	0.056	0.000	0.000	0.000	0.000
142	A	143	PRO	0	-0.043	0.003	36.928	-0.003	-0.003	0.000	0.000	0.000	0.000
143	A	144	GLY	0	0.007	0.016	40.578	0.001	0.001	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:ALA)