FMO DATABASE

FMODB ID: 2JZYR

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:

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1128700.059354
FMO2-HF: Nuclear repulsion	1077556.801984
FMO2-HF: Total energy	-51143.257371
FMO2-MP2: Total energy	-51293.356501

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.
-2.96	1.79	1.866	-2.922	-3.692	0.005

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 : -0.003 / q_NPA : 0.014

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	0.028	0.042	3.627	-2.462	1.726	-0.087	-2.219	-1.882	0.010
4	A	5	LYS	1	0.801	0.883	3.959	0.402	0.493	-0.001	-0.016	-0.073	0.000
5	A	6	VAL	0	0.013	0.007	8.811	0.140	0.140	0.000	0.000	0.000	0.000
6	A	7	THR	0	-0.016	-0.020	12.480	-0.055	-0.055	0.000	0.000	0.000	0.000
7	A	8	VAL	0	-0.017	0.009	14.972	0.030	0.030	0.000	0.000	0.000	0.000
8	A	9	GLY	0	0.016	0.009	18.746	0.008	0.008	0.000	0.000	0.000	0.000
9	A	10	THR	0	-0.035	-0.034	20.660	-0.008	-0.008	0.000	0.000	0.000	0.000
10	A	11	ALA	0	0.003	0.019	23.921	0.009	0.009	0.000	0.000	0.000	0.000
11	A	12	ASN	0	-0.004	-0.014	27.493	-0.007	-0.007	0.000	0.000	0.000	0.000
12	A	13	GLY	0	0.029	0.014	30.740	0.003	0.003	0.000	0.000	0.000	0.000
13	A	14	LYS	1	0.952	0.985	34.202	0.030	0.030	0.000	0.000	0.000	0.000
14	A	15	PRO	0	-0.022	-0.015	37.626	-0.002	-0.002	0.000	0.000	0.000	0.000
15	A	16	GLY	0	-0.016	-0.004	38.738	0.004	0.004	0.000	0.000	0.000	0.000
16	A	17	ASP	-1	-0.851	-0.906	35.973	-0.040	-0.040	0.000	0.000	0.000	0.000
17	A	18	THR	0	-0.035	-0.034	33.353	-0.006	-0.006	0.000	0.000	0.000	0.000
18	A	19	VAL	0	-0.029	-0.008	29.389	0.005	0.005	0.000	0.000	0.000	0.000
19	A	20	THR	0	0.002	-0.012	25.979	-0.006	-0.006	0.000	0.000	0.000	0.000
20	A	21	VAL	0	-0.016	-0.008	22.951	0.005	0.005	0.000	0.000	0.000	0.000
21	A	22	PRO	0	0.003	0.015	20.698	-0.010	-0.010	0.000	0.000	0.000	0.000
22	A	23	VAL	0	0.035	0.014	17.242	-0.014	-0.014	0.000	0.000	0.000	0.000
23	A	24	THR	0	0.000	-0.008	14.606	0.023	0.023	0.000	0.000	0.000	0.000
24	A	25	PHE	0	0.001	-0.004	11.854	-0.082	-0.082	0.000	0.000	0.000	0.000
25	A	26	ALA	0	0.038	0.004	9.301	0.091	0.091	0.000	0.000	0.000	0.000
26	A	27	ASP	-1	-0.823	-0.898	5.019	0.488	0.488	0.000	0.000	0.000	0.000
27	A	28	VAL	0	0.020	0.005	5.979	-0.180	-0.180	0.000	0.000	0.000	0.000
28	A	29	ALA	0	0.037	0.020	7.821	-0.052	-0.052	0.000	0.000	0.000	0.000
29	A	30	LYS	1	0.801	0.883	3.444	-1.535	-1.302	0.009	-0.047	-0.195	0.000
30	A	31	MET	0	-0.067	-0.001	2.956	-1.079	-0.998	1.947	-0.605	-1.424	-0.005
31	A	32	LYS	1	0.905	0.950	5.287	0.249	0.253	-0.001	0.000	-0.002	0.000
32	A	33	ASN	0	0.076	0.026	8.768	0.028	0.028	0.000	0.000	0.000	0.000
33	A	34	VAL	0	-0.040	0.048	10.577	-0.115	-0.115	0.000	0.000	0.000	0.000
34	A	35	GLY	0	0.073	0.059	12.638	0.062	0.062	0.000	0.000	0.000	0.000
35	A	36	THR	0	-0.028	-0.002	15.263	0.016	0.016	0.000	0.000	0.000	0.000
36	A	37	CYS	0	-0.038	-0.017	14.929	-0.066	-0.066	0.000	0.000	0.000	0.000
37	A	38	ASN	0	0.016	0.008	16.871	0.068	0.068	0.000	0.000	0.000	0.000
38	A	39	PHE	0	-0.030	-0.009	17.146	-0.060	-0.060	0.000	0.000	0.000	0.000
39	A	40	TYR	0	0.070	0.036	19.607	0.034	0.034	0.000	0.000	0.000	0.000
40	A	41	LEU	0	-0.029	-0.004	19.276	-0.025	-0.025	0.000	0.000	0.000	0.000
41	A	42	GLY	0	-0.003	-0.016	22.994	0.017	0.017	0.000	0.000	0.000	0.000
42	A	43	TYR	0	-0.028	-0.018	25.583	0.002	0.002	0.000	0.000	0.000	0.000
43	A	44	ASP	-1	-0.733	-0.848	28.256	-0.102	-0.102	0.000	0.000	0.000	0.000
44	A	45	ALA	0	0.036	0.019	31.599	0.007	0.007	0.000	0.000	0.000	0.000
45	A	46	SER	0	-0.091	-0.049	34.264	0.009	0.009	0.000	0.000	0.000	0.000
46	A	47	LEU	0	-0.001	-0.010	33.348	0.006	0.006	0.000	0.000	0.000	0.000
47	A	48	LEU	0	-0.036	-0.019	29.565	0.005	0.005	0.000	0.000	0.000	0.000
48	A	49	GLU	-1	-0.852	-0.907	33.556	-0.073	-0.073	0.000	0.000	0.000	0.000
49	A	50	VAL	0	-0.018	-0.006	29.677	0.001	0.001	0.000	0.000	0.000	0.000
50	A	51	VAL	0	-0.029	-0.008	32.373	0.003	0.003	0.000	0.000	0.000	0.000
51	A	52	SER	0	-0.038	-0.032	30.941	0.004	0.004	0.000	0.000	0.000	0.000
52	A	53	VAL	0	-0.001	-0.007	25.548	-0.004	-0.004	0.000	0.000	0.000	0.000
53	A	54	ASP	-1	-0.830	-0.881	26.740	-0.085	-0.085	0.000	0.000	0.000	0.000
54	A	55	ALA	0	0.027	0.019	23.139	-0.008	-0.008	0.000	0.000	0.000	0.000
55	A	56	GLY	0	-0.019	-0.019	21.690	0.014	0.014	0.000	0.000	0.000	0.000
56	A	57	PRO	0	-0.002	-0.025	21.183	-0.002	-0.002	0.000	0.000	0.000	0.000
57	A	58	ILE	0	-0.074	-0.013	14.911	0.006	0.006	0.000	0.000	0.000	0.000
58	A	59	VAL	0	-0.038	-0.010	18.343	-0.015	-0.015	0.000	0.000	0.000	0.000
59	A	60	LYS	1	0.846	0.944	18.082	0.079	0.079	0.000	0.000	0.000	0.000
60	A	61	ASN	0	-0.017	-0.022	22.729	-0.009	-0.009	0.000	0.000	0.000	0.000
61	A	62	ALA	0	0.061	0.019	24.698	-0.009	-0.009	0.000	0.000	0.000	0.000
62	A	63	ALA	0	-0.044	-0.025	25.643	-0.007	-0.007	0.000	0.000	0.000	0.000
63	A	64	VAL	0	-0.016	0.005	27.115	0.000	0.000	0.000	0.000	0.000	0.000
64	A	65	ASN	0	-0.003	-0.002	22.347	-0.010	-0.010	0.000	0.000	0.000	0.000
65	A	66	PHE	0	-0.027	-0.018	21.354	-0.022	-0.022	0.000	0.000	0.000	0.000
66	A	67	SER	0	-0.007	0.007	24.247	0.016	0.016	0.000	0.000	0.000	0.000
67	A	68	SER	0	-0.030	-0.026	24.941	-0.014	-0.014	0.000	0.000	0.000	0.000
68	A	69	SER	0	0.006	0.011	26.757	0.014	0.014	0.000	0.000	0.000	0.000
69	A	70	ALA	0	0.016	0.004	28.523	-0.013	-0.013	0.000	0.000	0.000	0.000
70	A	71	SER	0	-0.017	-0.010	30.489	0.013	0.013	0.000	0.000	0.000	0.000
71	A	72	ASN	0	0.036	-0.007	31.932	-0.005	-0.005	0.000	0.000	0.000	0.000
72	A	73	GLY	0	0.024	0.040	30.844	-0.002	-0.002	0.000	0.000	0.000	0.000
73	A	74	THR	0	-0.040	-0.023	26.495	-0.017	-0.017	0.000	0.000	0.000	0.000
74	A	75	ILE	0	-0.005	0.006	25.214	0.015	0.015	0.000	0.000	0.000	0.000
75	A	76	SER	0	0.000	0.009	24.413	-0.019	-0.019	0.000	0.000	0.000	0.000
76	A	77	PHE	0	0.009	-0.011	20.672	0.022	0.022	0.000	0.000	0.000	0.000
77	A	78	LEU	0	0.013	0.007	21.301	-0.029	-0.029	0.000	0.000	0.000	0.000
78	A	79	PHE	0	0.012	-0.015	17.436	0.017	0.017	0.000	0.000	0.000	0.000
79	A	80	LEU	0	-0.049	-0.037	19.695	-0.033	-0.033	0.000	0.000	0.000	0.000
80	A	81	ASP	-1	-0.750	-0.878	19.732	-0.114	-0.114	0.000	0.000	0.000	0.000
81	A	82	ASN	0	-0.026	-0.038	19.555	-0.027	-0.027	0.000	0.000	0.000	0.000
82	A	83	THR	0	-0.037	-0.027	21.325	0.003	0.003	0.000	0.000	0.000	0.000
83	A	84	ILE	0	0.008	0.025	22.636	0.013	0.013	0.000	0.000	0.000	0.000
84	A	85	THR	0	0.034	0.017	18.443	-0.002	-0.002	0.000	0.000	0.000	0.000
85	A	86	ASP	-1	-0.950	-0.980	19.246	-0.051	-0.051	0.000	0.000	0.000	0.000
86	A	87	GLU	-1	-0.850	-0.921	21.248	-0.077	-0.077	0.000	0.000	0.000	0.000
87	A	88	LEU	0	0.003	0.026	15.346	-0.020	-0.020	0.000	0.000	0.000	0.000
88	A	89	ILE	0	-0.036	-0.001	13.794	0.026	0.026	0.000	0.000	0.000	0.000
89	A	90	THR	0	-0.005	-0.032	12.972	-0.027	-0.027	0.000	0.000	0.000	0.000
90	A	91	ALA	0	-0.051	-0.015	12.874	0.046	0.046	0.000	0.000	0.000	0.000
91	A	92	ASP	-1	-0.787	-0.876	10.550	0.012	0.012	0.000	0.000	0.000	0.000
92	A	93	GLY	0	0.016	-0.010	13.289	0.029	0.029	0.000	0.000	0.000	0.000
93	A	94	VAL	0	-0.028	-0.019	16.141	-0.038	-0.038	0.000	0.000	0.000	0.000
94	A	95	PHE	0	0.035	0.021	16.503	0.005	0.005	0.000	0.000	0.000	0.000
95	A	96	ALA	0	0.031	0.012	18.521	0.008	0.008	0.000	0.000	0.000	0.000
96	A	97	ASN	0	-0.036	-0.020	21.855	0.002	0.002	0.000	0.000	0.000	0.000
97	A	98	ILE	0	0.030	0.024	23.094	0.000	0.000	0.000	0.000	0.000	0.000
98	A	99	LYS	1	0.873	0.935	26.630	0.086	0.086	0.000	0.000	0.000	0.000
99	A	100	PHE	0	0.031	0.000	26.209	-0.006	-0.006	0.000	0.000	0.000	0.000
100	A	101	LYS	1	0.890	0.922	31.620	0.069	0.069	0.000	0.000	0.000	0.000
101	A	102	LEU	0	-0.029	-0.007	32.258	-0.005	-0.005	0.000	0.000	0.000	0.000
102	A	103	LYS	1	0.912	0.959	35.729	0.086	0.086	0.000	0.000	0.000	0.000
103	A	104	SER	0	0.007	-0.008	38.279	0.001	0.001	0.000	0.000	0.000	0.000
104	A	105	VAL	0	0.005	-0.002	36.602	-0.003	-0.003	0.000	0.000	0.000	0.000
105	A	106	THR	0	-0.010	0.000	40.092	0.002	0.002	0.000	0.000	0.000	0.000
106	A	107	ALA	0	0.020	-0.006	39.806	0.004	0.004	0.000	0.000	0.000	0.000
107	A	108	LYS	1	0.853	0.913	33.381	0.034	0.034	0.000	0.000	0.000	0.000
108	A	109	THR	0	-0.015	-0.014	33.090	-0.002	-0.002	0.000	0.000	0.000	0.000
109	A	110	THR	0	-0.007	0.012	27.602	0.003	0.003	0.000	0.000	0.000	0.000
110	A	111	THR	0	0.011	0.013	29.287	-0.009	-0.009	0.000	0.000	0.000	0.000
111	A	112	PRO	0	0.008	-0.004	24.336	0.000	0.000	0.000	0.000	0.000	0.000
112	A	113	VAL	0	0.000	0.013	23.121	0.001	0.001	0.000	0.000	0.000	0.000
113	A	114	THR	0	-0.009	-0.020	21.131	-0.007	-0.007	0.000	0.000	0.000	0.000
114	A	115	PHE	0	-0.006	0.003	15.753	-0.005	-0.005	0.000	0.000	0.000	0.000
115	A	116	LYS	1	0.860	0.942	19.859	0.205	0.205	0.000	0.000	0.000	0.000
116	A	117	ASP	-1	-0.877	-0.953	21.274	-0.263	-0.263	0.000	0.000	0.000	0.000
117	A	118	GLY	0	-0.036	0.000	18.225	-0.012	-0.012	0.000	0.000	0.000	0.000
118	A	119	GLY	0	0.011	-0.014	17.994	0.020	0.020	0.000	0.000	0.000	0.000
119	A	120	ALA	0	-0.078	-0.030	15.807	-0.031	-0.031	0.000	0.000	0.000	0.000
120	A	121	PHE	0	0.015	-0.014	11.781	0.009	0.009	0.000	0.000	0.000	0.000
121	A	122	GLY	0	0.031	0.028	12.569	-0.096	-0.096	0.000	0.000	0.000	0.000
122	A	123	ASP	-1	-0.733	-0.909	9.835	-0.447	-0.447	0.000	0.000	0.000	0.000
123	A	124	GLY	0	-0.011	-0.029	11.826	0.045	0.045	0.000	0.000	0.000	0.000
124	A	125	THR	0	-0.129	-0.092	12.693	0.043	0.043	0.000	0.000	0.000	0.000
125	A	126	MET	0	-0.022	0.000	14.987	0.008	0.008	0.000	0.000	0.000	0.000
126	A	127	SER	0	-0.010	0.014	11.774	0.001	0.001	0.000	0.000	0.000	0.000
127	A	128	LYS	1	0.870	0.933	10.586	1.104	1.104	0.000	0.000	0.000	0.000
128	A	129	ILE	0	0.031	0.019	7.044	-0.143	-0.143	0.000	0.000	0.000	0.000
129	A	130	ALA	0	-0.031	-0.015	5.369	-0.047	-0.047	0.000	0.000	0.000	0.000
130	A	131	SER	0	-0.004	-0.008	4.639	0.409	0.562	-0.001	-0.035	-0.116	0.000
131	A	132	VAL	0	0.038	0.011	6.418	-0.221	-0.221	0.000	0.000	0.000	0.000
132	A	133	THR	0	-0.032	-0.003	7.077	-0.046	-0.046	0.000	0.000	0.000	0.000
133	A	134	LYS	1	0.941	0.981	9.259	0.793	0.793	0.000	0.000	0.000	0.000
134	A	135	THR	0	0.007	0.010	12.789	0.017	0.017	0.000	0.000	0.000	0.000
135	A	136	ASN	0	0.022	0.000	15.114	0.000	0.000	0.000	0.000	0.000	0.000
136	A	137	GLY	0	0.100	0.061	18.864	0.011	0.011	0.000	0.000	0.000	0.000
137	A	138	SER	0	-0.099	-0.054	21.231	0.003	0.003	0.000	0.000	0.000	0.000
138	A	139	VAL	0	0.027	0.013	24.986	0.006	0.006	0.000	0.000	0.000	0.000
139	A	140	THR	0	-0.064	-0.038	28.270	-0.001	-0.001	0.000	0.000	0.000	0.000
140	A	141	ILE	0	0.019	0.007	30.878	0.004	0.004	0.000	0.000	0.000	0.000
141	A	142	ASP	-1	-0.819	-0.930	34.427	-0.036	-0.036	0.000	0.000	0.000	0.000
142	A	143	PRO	0	-0.024	0.007	36.922	0.002	0.002	0.000	0.000	0.000	0.000
143	A	144	GLY	0	0.000	0.017	40.572	0.003	0.003	0.000	0.000	0.000	0.000

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