FMO DATABASE

FMODB ID: 7G33K

Calculation Name: 3K1H-A-Xray317

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3K1H

Chain ID: A

ChEMBL ID:

UniProt ID: O25709

Base Structure: X-ray

Registration Date: 2021-09-07

Reference: C. Watanabe, S. Koyama, K. Kamisaka, D. Takaya, T. Honma et. al., Interaction energy analysis of Apo structure dataset on FMODB, To be pubulished.

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. 1.20200129

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	117
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver.1 Rev. 15 / 20190524

Total energy (hartree)

FMO2-HF: Electronic energy	-925602.859682
FMO2-HF: Nuclear repulsion	879380.99191
FMO2-HF: Total energy	-46221.867772
FMO2-MP2: Total energy	-46355.302268

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:32:ACE )

Summations of interaction energy for fragment #1(A:32:ACE )

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.
-0.141	2.172	0.899	-1.672	-1.541	-0.012

Interaction energy analysis for fragmet #1(A:32:ACE )

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.029 / q_NPA : 0.009

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	34	SER	0	0.035	0.018	3.843	1.042	1.824	-0.005	-0.380	-0.397	0.000
4	A	35	ARG	1	0.810	0.906	7.350	0.596	0.596	0.000	0.000	0.000	0.000
5	A	36	ASP	-1	-0.855	-0.912	10.514	-0.358	-0.358	0.000	0.000	0.000	0.000
6	A	37	MET	0	-0.082	-0.032	12.710	0.020	0.020	0.000	0.000	0.000	0.000
7	A	38	LYS	1	0.934	0.982	16.385	0.219	0.219	0.000	0.000	0.000	0.000
8	A	39	ASN	0	0.003	-0.016	19.576	0.019	0.019	0.000	0.000	0.000	0.000
9	A	40	ILE	0	0.098	0.046	20.785	-0.014	-0.014	0.000	0.000	0.000	0.000
10	A	41	ASN	0	-0.014	-0.009	22.278	0.006	0.006	0.000	0.000	0.000	0.000
11	A	42	GLU	-1	-0.895	-0.957	17.651	-0.261	-0.261	0.000	0.000	0.000	0.000
12	A	43	SER	0	0.036	0.021	17.459	-0.017	-0.017	0.000	0.000	0.000	0.000
13	A	44	VAL	0	0.037	0.020	18.213	0.004	0.004	0.000	0.000	0.000	0.000
14	A	45	GLY	0	-0.027	-0.011	19.812	0.009	0.009	0.000	0.000	0.000	0.000
15	A	46	ALA	0	0.016	0.000	14.120	0.006	0.006	0.000	0.000	0.000	0.000
16	A	47	LEU	0	0.046	0.020	15.228	0.011	0.011	0.000	0.000	0.000	0.000
17	A	48	GLN	0	-0.015	-0.006	17.131	0.030	0.030	0.000	0.000	0.000	0.000
18	A	49	VAL	0	-0.008	-0.004	15.499	0.019	0.019	0.000	0.000	0.000	0.000
19	A	50	LEU	0	0.039	0.015	11.782	0.018	0.018	0.000	0.000	0.000	0.000
20	A	51	GLN	0	0.000	0.003	15.132	0.038	0.038	0.000	0.000	0.000	0.000
21	A	52	ILE	0	-0.055	-0.026	18.267	0.020	0.020	0.000	0.000	0.000	0.000
22	A	53	ALA	0	0.003	0.003	15.186	0.015	0.015	0.000	0.000	0.000	0.000
23	A	54	CYS	0	0.042	0.017	14.651	0.028	0.028	0.000	0.000	0.000	0.000
24	A	55	LYS	1	0.981	0.991	16.997	0.023	0.023	0.000	0.000	0.000	0.000
25	A	56	LYS	1	0.869	0.946	19.630	0.028	0.028	0.000	0.000	0.000	0.000
26	A	57	LEU	0	0.002	0.007	14.435	0.005	0.005	0.000	0.000	0.000	0.000
27	A	58	PHE	0	0.035	0.029	19.043	0.006	0.006	0.000	0.000	0.000	0.000
28	A	59	ASN	0	0.011	-0.016	21.202	0.004	0.004	0.000	0.000	0.000	0.000
29	A	60	LYS	1	0.899	0.956	21.816	-0.024	-0.024	0.000	0.000	0.000	0.000
30	A	61	SER	0	-0.010	0.002	21.341	0.005	0.005	0.000	0.000	0.000	0.000
31	A	62	MET	0	-0.014	0.000	23.471	0.005	0.005	0.000	0.000	0.000	0.000
32	A	63	GLY	0	0.027	0.013	26.757	-0.004	-0.004	0.000	0.000	0.000	0.000
33	A	64	LEU	0	-0.085	-0.037	22.925	-0.001	-0.001	0.000	0.000	0.000	0.000
34	A	65	GLU	-1	-0.896	-0.959	26.930	0.072	0.072	0.000	0.000	0.000	0.000
35	A	66	ASP	-1	-0.910	-0.941	28.340	0.053	0.053	0.000	0.000	0.000	0.000
36	A	67	LYS	1	0.811	0.921	28.430	-0.052	-0.052	0.000	0.000	0.000	0.000
37	A	68	ASP	-1	-0.821	-0.905	30.687	0.050	0.050	0.000	0.000	0.000	0.000
38	A	69	ALA	0	0.042	-0.006	29.809	0.003	0.003	0.000	0.000	0.000	0.000
39	A	70	LEU	0	-0.020	0.010	29.067	0.003	0.003	0.000	0.000	0.000	0.000
40	A	71	GLN	0	0.024	0.004	28.972	0.001	0.001	0.000	0.000	0.000	0.000
41	A	72	ALA	0	0.022	0.016	26.214	0.003	0.003	0.000	0.000	0.000	0.000
42	A	73	SER	0	-0.096	-0.063	24.684	0.006	0.006	0.000	0.000	0.000	0.000
43	A	74	ILE	0	0.014	0.000	24.121	0.003	0.003	0.000	0.000	0.000	0.000
44	A	75	ILE	0	0.048	0.024	22.871	0.000	0.000	0.000	0.000	0.000	0.000
45	A	76	LYS	1	0.946	0.970	20.528	-0.115	-0.115	0.000	0.000	0.000	0.000
46	A	77	GLN	0	-0.016	0.001	19.051	0.024	0.024	0.000	0.000	0.000	0.000
47	A	78	GLU	-1	-0.904	-0.956	19.657	0.033	0.033	0.000	0.000	0.000	0.000
48	A	79	LEU	0	-0.061	-0.035	17.560	-0.008	-0.008	0.000	0.000	0.000	0.000
49	A	80	ARG	1	0.942	0.963	15.081	-0.142	-0.142	0.000	0.000	0.000	0.000
50	A	81	GLU	-1	-0.881	-0.935	14.783	0.023	0.023	0.000	0.000	0.000	0.000
51	A	82	ILE	0	-0.097	-0.046	15.790	-0.027	-0.027	0.000	0.000	0.000	0.000
52	A	83	VAL	0	-0.023	-0.014	10.396	-0.029	-0.029	0.000	0.000	0.000	0.000
53	A	84	GLU	-1	-0.960	-0.982	11.688	0.050	0.050	0.000	0.000	0.000	0.000
54	A	85	ASN	0	-0.048	-0.020	12.839	-0.053	-0.053	0.000	0.000	0.000	0.000
55	A	86	CYS	0	-0.098	-0.019	12.100	-0.035	-0.035	0.000	0.000	0.000	0.000
56	A	87	GLN	0	-0.016	-0.012	11.752	-0.045	-0.045	0.000	0.000	0.000	0.000
57	A	88	PHE	0	0.019	0.003	13.183	0.049	0.049	0.000	0.000	0.000	0.000
58	A	89	LEU	0	-0.023	-0.013	14.027	-0.056	-0.056	0.000	0.000	0.000	0.000
59	A	90	ALA	0	-0.002	0.012	15.181	-0.026	-0.026	0.000	0.000	0.000	0.000
60	A	91	SER	0	0.047	0.020	9.537	-0.068	-0.068	0.000	0.000	0.000	0.000
61	A	92	PRO	0	0.035	0.010	6.775	0.121	0.121	0.000	0.000	0.000	0.000
62	A	93	LEU	0	-0.020	-0.014	8.854	-0.090	-0.090	0.000	0.000	0.000	0.000
63	A	94	PHE	0	0.063	0.023	7.691	-0.002	-0.002	0.000	0.000	0.000	0.000
64	A	95	ASP	-1	-0.848	-0.914	2.726	0.544	0.824	0.163	-0.212	-0.231	-0.001
65	A	96	THR	0	-0.087	-0.049	2.689	-2.473	-1.290	0.741	-1.077	-0.848	-0.011
66	A	97	GLN	0	-0.046	-0.025	5.291	0.369	0.437	0.000	-0.003	-0.065	0.000
67	A	98	LEU	0	-0.024	-0.023	7.918	-0.157	-0.157	0.000	0.000	0.000	0.000
68	A	99	ASN	0	0.017	0.017	10.981	0.145	0.145	0.000	0.000	0.000	0.000
69	A	100	ILE	0	0.031	-0.004	13.858	-0.015	-0.015	0.000	0.000	0.000	0.000
70	A	101	ALA	0	-0.007	0.016	17.210	0.019	0.019	0.000	0.000	0.000	0.000
71	A	102	ILE	0	-0.023	-0.030	20.675	0.002	0.002	0.000	0.000	0.000	0.000
72	A	103	ASN	0	-0.018	-0.016	23.453	0.002	0.002	0.000	0.000	0.000	0.000
73	A	104	ASP	-1	-0.942	-0.961	25.471	-0.070	-0.070	0.000	0.000	0.000	0.000
74	A	105	GLU	-1	-0.947	-0.950	22.729	-0.055	-0.055	0.000	0.000	0.000	0.000
75	A	106	ILE	0	-0.047	-0.041	16.359	-0.013	-0.013	0.000	0.000	0.000	0.000
76	A	107	PHE	0	0.022	0.015	17.727	0.015	0.015	0.000	0.000	0.000	0.000
77	A	108	SER	0	-0.012	-0.033	12.230	-0.025	-0.025	0.000	0.000	0.000	0.000
78	A	109	MET	0	-0.020	0.015	12.500	0.045	0.045	0.000	0.000	0.000	0.000
79	A	110	ILE	0	0.011	0.004	5.384	-0.076	-0.076	0.000	0.000	0.000	0.000
80	A	111	VAL	0	-0.008	-0.004	8.968	0.056	0.056	0.000	0.000	0.000	0.000
81	A	112	VAL	0	0.027	0.001	6.641	-0.049	-0.049	0.000	0.000	0.000	0.000
82	A	113	ASN	0	0.038	-0.011	7.065	-0.280	-0.280	0.000	0.000	0.000	0.000
83	A	114	PRO	0	0.017	0.011	8.939	0.036	0.036	0.000	0.000	0.000	0.000
84	A	115	LEU	0	-0.046	-0.033	12.179	-0.035	-0.035	0.000	0.000	0.000	0.000
85	A	116	ASP	-1	-0.905	-0.943	11.024	0.548	0.548	0.000	0.000	0.000	0.000
86	A	117	LEU	0	0.000	-0.005	14.246	-0.031	-0.031	0.000	0.000	0.000	0.000
87	A	118	LEU	0	-0.062	-0.025	16.631	-0.037	-0.037	0.000	0.000	0.000	0.000
88	A	119	GLU	-1	-1.028	-1.004	18.831	0.141	0.141	0.000	0.000	0.000	0.000
89	A	120	ASN	0	0.015	0.018	20.472	-0.028	-0.028	0.000	0.000	0.000	0.000
90	A	121	VAL	0	0.049	0.007	21.131	0.007	0.007	0.000	0.000	0.000	0.000
91	A	122	GLY	0	0.043	0.021	22.245	-0.003	-0.003	0.000	0.000	0.000	0.000
92	A	123	GLU	-1	-0.914	-0.956	19.391	0.178	0.178	0.000	0.000	0.000	0.000
93	A	124	PHE	0	-0.041	-0.018	15.758	0.002	0.002	0.000	0.000	0.000	0.000
94	A	125	GLN	0	-0.039	-0.030	18.219	-0.006	-0.006	0.000	0.000	0.000	0.000
95	A	126	ALA	0	0.043	0.024	20.731	-0.010	-0.010	0.000	0.000	0.000	0.000
96	A	127	TYR	0	0.073	0.047	11.192	0.001	0.001	0.000	0.000	0.000	0.000
97	A	128	LEU	0	-0.028	-0.027	15.042	-0.017	-0.017	0.000	0.000	0.000	0.000
98	A	129	GLU	-1	-0.974	-0.978	17.464	0.034	0.034	0.000	0.000	0.000	0.000
99	A	130	GLU	-1	-0.948	-0.971	18.082	0.110	0.110	0.000	0.000	0.000	0.000
100	A	131	LYS	1	0.864	0.934	12.496	-0.145	-0.145	0.000	0.000	0.000	0.000
101	A	132	LEU	0	-0.063	-0.043	16.609	-0.029	-0.029	0.000	0.000	0.000	0.000
102	A	133	ASN	0	-0.023	-0.013	19.177	-0.021	-0.021	0.000	0.000	0.000	0.000
103	A	134	GLU	-1	-0.865	-0.925	15.908	0.041	0.041	0.000	0.000	0.000	0.000
104	A	135	ILE	0	-0.004	-0.011	14.928	-0.019	-0.019	0.000	0.000	0.000	0.000
105	A	136	LYS	1	0.916	0.961	18.573	-0.009	-0.009	0.000	0.000	0.000	0.000
106	A	137	GLU	-1	-0.932	-0.963	21.688	-0.017	-0.017	0.000	0.000	0.000	0.000
107	A	138	LEU	0	0.013	0.012	16.894	-0.009	-0.009	0.000	0.000	0.000	0.000
108	A	139	LEU	0	-0.055	-0.037	20.573	-0.008	-0.008	0.000	0.000	0.000	0.000
109	A	140	GLY	0	-0.002	0.012	22.700	-0.001	-0.001	0.000	0.000	0.000	0.000
110	A	141	TYR	0	0.062	0.024	22.708	-0.002	-0.002	0.000	0.000	0.000	0.000
111	A	142	LEU	0	-0.010	-0.013	20.138	-0.005	-0.005	0.000	0.000	0.000	0.000
112	A	143	SER	0	-0.034	-0.037	24.761	-0.001	-0.001	0.000	0.000	0.000	0.000
113	A	144	GLU	-1	-0.950	-0.963	27.726	-0.035	-0.035	0.000	0.000	0.000	0.000
114	A	145	SER	0	-0.036	-0.022	26.940	-0.001	-0.001	0.000	0.000	0.000	0.000
115	A	146	LEU	0	-0.102	-0.049	26.243	-0.002	-0.002	0.000	0.000	0.000	0.000
116	A	147	SER	0	-0.092	-0.023	29.770	0.004	0.004	0.000	0.000	0.000	0.000
117	A	148	NME	0	-0.020	-0.001	32.693	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:32:ACE )