FMO DATABASE

FMODB ID: G54N1

Calculation Name: 1KTJ-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1KTJ

Chain ID: A

ChEMBL ID:

UniProt ID: P49278

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:

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptAll
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	126
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1044458.149884
FMO2-HF: Nuclear repulsion	993960.892042
FMO2-HF: Total energy	-50497.257842
FMO2-MP2: Total energy	-50640.537183

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:1:SER)

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

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.
-12.669	-4.834	4.766	-5.081	-7.525	-0.024

Interaction energy analysis for fragmet #1(A:1:SER)

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 : -0.017

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

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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	3	VAL	0	-0.038	-0.013	3.850	-0.812	0.385	-0.008	-0.486	-0.703	0.002
4	A	4	ASP	-1	-0.848	-0.888	6.353	0.396	0.396	0.000	0.000	0.000	0.000
5	A	5	VAL	0	-0.045	-0.037	9.996	-0.085	-0.085	0.000	0.000	0.000	0.000
6	A	6	LYS	1	0.886	0.941	12.777	0.057	0.057	0.000	0.000	0.000	0.000
7	A	7	ASP	-1	-0.775	-0.891	16.468	0.080	0.080	0.000	0.000	0.000	0.000
8	A	8	CYS	0	-0.144	-0.079	17.908	-0.031	-0.031	0.000	0.000	0.000	0.000
9	A	9	ALA	0	-0.002	0.001	21.248	-0.005	-0.005	0.000	0.000	0.000	0.000
10	A	10	ASN	0	-0.051	-0.021	22.193	-0.009	-0.009	0.000	0.000	0.000	0.000
11	A	11	HIS	0	0.007	0.013	18.273	0.015	0.015	0.000	0.000	0.000	0.000
12	A	12	GLU	-1	-0.752	-0.859	18.428	0.120	0.120	0.000	0.000	0.000	0.000
13	A	13	ILE	0	-0.032	-0.026	13.161	0.029	0.029	0.000	0.000	0.000	0.000
14	A	14	LYS	1	0.759	0.869	13.293	-0.195	-0.195	0.000	0.000	0.000	0.000
15	A	15	LYS	1	0.825	0.895	6.998	-0.767	-0.767	0.000	0.000	0.000	0.000
16	A	16	VAL	0	0.014	0.002	7.471	0.062	0.062	0.000	0.000	0.000	0.000
17	A	17	LEU	0	-0.014	0.007	2.947	-2.476	-0.722	0.258	-0.830	-1.183	0.007
18	A	18	VAL	0	0.041	0.004	2.684	0.456	1.461	0.127	-0.377	-0.756	0.000
19	A	19	PRO	0	-0.021	-0.014	2.463	-5.771	-4.122	2.361	-1.627	-2.384	-0.015
20	A	20	GLY	0	-0.002	0.005	3.120	0.113	0.044	0.025	0.266	-0.223	0.000
21	A	21	CYS	0	-0.084	-0.015	3.493	0.870	1.144	0.000	-0.078	-0.196	0.000
22	A	22	HIS	0	-0.029	-0.041	2.447	-5.849	-3.921	2.000	-1.915	-2.014	-0.018
23	A	23	GLY	0	0.066	0.039	4.025	0.317	0.414	0.003	-0.034	-0.066	0.000
24	A	24	SER	0	-0.003	-0.055	7.290	-0.254	-0.254	0.000	0.000	0.000	0.000
25	A	25	GLU	-1	-0.924	-0.925	8.314	-0.293	-0.293	0.000	0.000	0.000	0.000
26	A	26	PRO	0	-0.035	-0.038	9.721	-0.117	-0.117	0.000	0.000	0.000	0.000
27	A	28	ILE	0	-0.041	-0.033	9.702	0.164	0.164	0.000	0.000	0.000	0.000
28	A	29	ILE	0	0.046	0.029	11.045	-0.034	-0.034	0.000	0.000	0.000	0.000
29	A	30	HIS	1	0.810	0.880	11.779	0.463	0.463	0.000	0.000	0.000	0.000
30	A	31	ARG	1	0.867	0.914	15.003	0.158	0.158	0.000	0.000	0.000	0.000
31	A	32	GLY	0	-0.036	-0.027	18.351	0.001	0.001	0.000	0.000	0.000	0.000
32	A	33	LYS	1	0.840	0.923	14.769	0.225	0.225	0.000	0.000	0.000	0.000
33	A	34	PRO	0	0.053	0.027	12.840	-0.004	-0.004	0.000	0.000	0.000	0.000
34	A	35	PHE	0	-0.020	-0.017	8.540	-0.039	-0.039	0.000	0.000	0.000	0.000
35	A	36	GLN	0	-0.010	-0.007	7.356	0.209	0.209	0.000	0.000	0.000	0.000
36	A	37	LEU	0	-0.001	0.000	6.654	-0.155	-0.155	0.000	0.000	0.000	0.000
37	A	38	GLU	-1	-0.789	-0.853	6.323	0.999	0.999	0.000	0.000	0.000	0.000
38	A	39	ALA	0	-0.003	0.011	7.737	-0.009	-0.009	0.000	0.000	0.000	0.000
39	A	40	VAL	0	-0.004	-0.001	9.943	-0.018	-0.018	0.000	0.000	0.000	0.000
40	A	41	PHE	0	0.007	0.001	12.332	-0.031	-0.031	0.000	0.000	0.000	0.000
41	A	42	GLU	-1	-0.808	-0.885	15.812	0.182	0.182	0.000	0.000	0.000	0.000
42	A	43	ALA	0	0.002	0.014	19.364	-0.013	-0.013	0.000	0.000	0.000	0.000
43	A	44	ASN	0	0.019	-0.011	22.485	-0.005	-0.005	0.000	0.000	0.000	0.000
44	A	45	GLN	0	-0.024	-0.018	24.934	-0.012	-0.012	0.000	0.000	0.000	0.000
45	A	46	ASN	0	0.004	0.004	26.637	0.013	0.013	0.000	0.000	0.000	0.000
46	A	47	THR	0	-0.024	0.002	25.829	-0.009	-0.009	0.000	0.000	0.000	0.000
47	A	48	LYS	1	0.862	0.888	27.442	-0.046	-0.046	0.000	0.000	0.000	0.000
48	A	49	THR	0	-0.042	-0.036	27.293	0.001	0.001	0.000	0.000	0.000	0.000
49	A	50	ALA	0	0.083	0.015	21.964	0.006	0.006	0.000	0.000	0.000	0.000
50	A	51	LYN	0	-0.040	-0.001	23.285	0.004	0.004	0.000	0.000	0.000	0.000
51	A	52	ILE	0	-0.030	-0.015	18.008	0.002	0.002	0.000	0.000	0.000	0.000
52	A	53	GLU	-1	-0.839	-0.905	21.699	0.007	0.007	0.000	0.000	0.000	0.000
53	A	54	ILE	0	-0.008	-0.021	16.583	0.000	0.000	0.000	0.000	0.000	0.000
54	A	55	LYS	1	0.822	0.898	20.191	0.029	0.029	0.000	0.000	0.000	0.000
55	A	56	ALA	0	0.032	0.022	18.955	-0.011	-0.011	0.000	0.000	0.000	0.000
56	A	57	SER	0	-0.025	-0.012	20.316	0.014	0.014	0.000	0.000	0.000	0.000
57	A	58	ILE	0	-0.008	-0.015	19.982	-0.021	-0.021	0.000	0.000	0.000	0.000
58	A	59	ASP	-1	-0.809	-0.888	22.642	-0.108	-0.108	0.000	0.000	0.000	0.000
59	A	60	GLY	0	-0.010	0.008	24.447	0.009	0.009	0.000	0.000	0.000	0.000
60	A	61	LEU	0	-0.032	-0.008	26.247	0.009	0.009	0.000	0.000	0.000	0.000
61	A	62	GLU	-1	-0.803	-0.889	24.885	-0.042	-0.042	0.000	0.000	0.000	0.000
62	A	63	VAL	0	-0.082	-0.045	22.180	0.001	0.001	0.000	0.000	0.000	0.000
63	A	64	ASP	-1	-0.837	-0.924	23.410	-0.033	-0.033	0.000	0.000	0.000	0.000
64	A	65	VAL	0	-0.063	-0.037	18.225	-0.015	-0.015	0.000	0.000	0.000	0.000
65	A	66	PRO	0	0.033	0.036	21.314	0.011	0.011	0.000	0.000	0.000	0.000
66	A	67	GLY	0	-0.023	-0.021	20.529	-0.006	-0.006	0.000	0.000	0.000	0.000
67	A	68	ILE	0	-0.002	-0.005	16.839	0.008	0.008	0.000	0.000	0.000	0.000
68	A	69	ASP	-1	-0.770	-0.832	20.094	0.059	0.059	0.000	0.000	0.000	0.000
69	A	70	PRO	0	0.019	0.010	21.060	0.009	0.009	0.000	0.000	0.000	0.000
70	A	71	ASN	0	0.012	0.001	23.393	0.007	0.007	0.000	0.000	0.000	0.000
71	A	72	ALA	0	0.066	0.025	19.115	0.008	0.008	0.000	0.000	0.000	0.000
72	A	73	CYS	0	-0.045	-0.018	20.282	0.020	0.020	0.000	0.000	0.000	0.000
73	A	74	HIS	0	-0.063	-0.034	22.272	-0.006	-0.006	0.000	0.000	0.000	0.000
74	A	75	TYR	0	-0.084	-0.069	17.195	0.005	0.005	0.000	0.000	0.000	0.000
75	A	76	MET	0	-0.019	-0.008	17.582	0.039	0.039	0.000	0.000	0.000	0.000
76	A	77	LYS	1	0.931	0.982	19.269	-0.189	-0.189	0.000	0.000	0.000	0.000
77	A	79	PRO	0	0.023	-0.009	24.854	-0.005	-0.005	0.000	0.000	0.000	0.000
78	A	80	LEU	0	-0.043	-0.007	21.428	0.008	0.008	0.000	0.000	0.000	0.000
79	A	81	VAL	0	-0.003	-0.002	24.632	-0.010	-0.010	0.000	0.000	0.000	0.000
80	A	82	LYS	1	0.914	0.924	24.820	-0.069	-0.069	0.000	0.000	0.000	0.000
81	A	83	GLY	0	-0.021	-0.006	24.045	-0.004	-0.004	0.000	0.000	0.000	0.000
82	A	84	GLN	0	-0.044	-0.013	22.074	0.006	0.006	0.000	0.000	0.000	0.000
83	A	85	GLN	0	-0.038	-0.035	16.126	0.024	0.024	0.000	0.000	0.000	0.000
84	A	86	TYR	0	-0.053	-0.020	17.035	-0.011	-0.011	0.000	0.000	0.000	0.000
85	A	87	ASH	0	-0.064	-0.069	10.276	0.005	0.005	0.000	0.000	0.000	0.000
86	A	88	ILE	0	0.023	0.016	12.503	-0.051	-0.051	0.000	0.000	0.000	0.000
87	A	89	LYS	1	0.850	0.910	9.349	-0.591	-0.591	0.000	0.000	0.000	0.000
88	A	90	TYR	0	0.031	0.019	11.003	-0.108	-0.108	0.000	0.000	0.000	0.000
89	A	91	THR	0	-0.045	-0.039	11.009	0.075	0.075	0.000	0.000	0.000	0.000
90	A	92	TRP	0	0.030	0.031	12.673	-0.035	-0.035	0.000	0.000	0.000	0.000
91	A	93	ASN	0	0.001	-0.016	14.203	-0.019	-0.019	0.000	0.000	0.000	0.000
92	A	94	VAL	0	0.018	0.033	14.276	0.003	0.003	0.000	0.000	0.000	0.000
93	A	95	PRO	0	0.058	0.028	17.089	0.001	0.001	0.000	0.000	0.000	0.000
94	A	96	LYS	1	0.954	0.966	20.794	0.088	0.088	0.000	0.000	0.000	0.000
95	A	97	ILE	0	-0.030	-0.019	22.234	-0.005	-0.005	0.000	0.000	0.000	0.000
96	A	98	ALA	0	0.034	0.032	20.376	0.004	0.004	0.000	0.000	0.000	0.000
97	A	99	PRO	0	0.048	0.031	22.442	-0.006	-0.006	0.000	0.000	0.000	0.000
98	A	100	LYS	1	0.927	0.957	20.755	0.115	0.115	0.000	0.000	0.000	0.000
99	A	101	SER	0	-0.003	-0.024	19.895	0.010	0.010	0.000	0.000	0.000	0.000
100	A	102	GLU	-1	-0.773	-0.885	17.800	-0.293	-0.293	0.000	0.000	0.000	0.000
101	A	103	ASN	0	-0.061	-0.034	18.765	-0.017	-0.017	0.000	0.000	0.000	0.000
102	A	104	VAL	0	-0.018	0.002	16.422	0.020	0.020	0.000	0.000	0.000	0.000
103	A	105	VAL	0	0.003	0.003	17.377	-0.021	-0.021	0.000	0.000	0.000	0.000
104	A	106	VAL	0	-0.005	-0.001	15.392	0.017	0.017	0.000	0.000	0.000	0.000
105	A	107	THR	0	-0.009	0.000	16.954	-0.003	-0.003	0.000	0.000	0.000	0.000
106	A	108	VAL	0	-0.012	-0.008	15.001	0.001	0.001	0.000	0.000	0.000	0.000
107	A	109	LYS	1	0.850	0.901	18.210	-0.006	-0.006	0.000	0.000	0.000	0.000
108	A	110	VAL	0	0.002	0.011	18.542	0.001	0.001	0.000	0.000	0.000	0.000
109	A	111	MET	0	-0.006	0.010	21.623	0.002	0.002	0.000	0.000	0.000	0.000
110	A	112	GLY	0	0.053	0.020	25.248	0.006	0.006	0.000	0.000	0.000	0.000
111	A	113	ASP	-1	-0.810	-0.873	27.108	0.053	0.053	0.000	0.000	0.000	0.000
112	A	114	ASP	-1	-0.871	-0.932	29.682	0.055	0.055	0.000	0.000	0.000	0.000
113	A	115	GLY	0	-0.008	-0.001	29.085	-0.003	-0.003	0.000	0.000	0.000	0.000
114	A	116	VAL	0	-0.011	-0.015	24.144	0.004	0.004	0.000	0.000	0.000	0.000
115	A	117	LEU	0	-0.039	-0.001	21.498	0.005	0.005	0.000	0.000	0.000	0.000
116	A	118	ALA	0	0.013	0.001	18.016	0.015	0.015	0.000	0.000	0.000	0.000
117	A	120	ALA	0	0.024	0.015	14.939	0.010	0.010	0.000	0.000	0.000	0.000
118	A	121	ILE	0	-0.003	-0.004	16.712	-0.008	-0.008	0.000	0.000	0.000	0.000
119	A	122	ALA	0	0.016	0.011	12.471	-0.012	-0.012	0.000	0.000	0.000	0.000
120	A	123	THR	0	0.034	0.007	14.383	0.013	0.013	0.000	0.000	0.000	0.000
121	A	124	HIS	0	0.046	0.033	10.673	0.012	0.012	0.000	0.000	0.000	0.000
122	A	125	ALA	0	0.000	0.020	11.966	-0.075	-0.075	0.000	0.000	0.000	0.000
123	A	126	LYS	1	0.825	0.928	12.895	0.359	0.359	0.000	0.000	0.000	0.000
124	A	127	ILE	0	-0.004	0.015	14.250	-0.039	-0.039	0.000	0.000	0.000	0.000
125	A	128	ARG	1	0.889	0.918	15.659	0.333	0.333	0.000	0.000	0.000	0.000
126	A	129	ASP	-1	-0.803	-0.867	17.324	-0.230	-0.230	0.000	0.000	0.000	0.000

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