FMO DATABASE

FMODB ID: 1N34Z

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	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	126
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1044237.687209
FMO2-HF: Nuclear repulsion	993740.650394
FMO2-HF: Total energy	-50497.036815
FMO2-MP2: Total energy	-50640.269422

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.
-10.912	-5.02	9.454	-6.14	-9.206	-0.029

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 : 0.003 / 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

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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	-0.029	-0.010	3.798	-0.633	0.598	-0.003	-0.444	-0.784	0.002
4	A	4	ASP	-1	-0.838	-0.880	6.016	0.661	0.661	0.000	0.000	0.000	0.000
5	A	5	VAL	0	-0.060	-0.038	9.675	-0.137	-0.137	0.000	0.000	0.000	0.000
6	A	6	LYS	1	0.892	0.938	12.362	0.070	0.070	0.000	0.000	0.000	0.000
7	A	7	ASP	-1	-0.773	-0.880	16.080	0.092	0.092	0.000	0.000	0.000	0.000
8	A	8	CYS	0	-0.122	-0.073	17.545	-0.039	-0.039	0.000	0.000	0.000	0.000
9	A	9	ALA	0	-0.026	-0.016	20.560	-0.008	-0.008	0.000	0.000	0.000	0.000
10	A	10	ASN	0	-0.040	-0.013	21.533	-0.005	-0.005	0.000	0.000	0.000	0.000
11	A	11	HIS	0	0.013	0.013	18.076	0.026	0.026	0.000	0.000	0.000	0.000
12	A	12	GLU	-1	-0.765	-0.871	17.912	0.158	0.158	0.000	0.000	0.000	0.000
13	A	13	ILE	0	-0.028	-0.024	12.533	0.038	0.038	0.000	0.000	0.000	0.000
14	A	14	LYS	1	0.765	0.885	12.911	-0.261	-0.261	0.000	0.000	0.000	0.000
15	A	15	LYS	1	0.854	0.903	6.786	-1.247	-1.247	0.000	0.000	0.000	0.000
16	A	16	VAL	0	0.002	0.006	6.919	0.090	0.090	0.000	0.000	0.000	0.000
17	A	17	LEU	0	-0.013	-0.005	2.893	-2.570	-0.712	0.327	-0.844	-1.342	0.006
18	A	18	VAL	0	0.038	0.004	2.512	0.223	1.476	0.498	-0.543	-1.208	-0.002
19	A	19	PRO	0	-0.018	-0.018	2.315	-4.893	-4.611	5.334	-2.508	-3.109	-0.013
20	A	20	GLY	0	-0.023	-0.006	2.915	0.959	0.369	0.034	0.810	-0.254	0.000
21	A	21	CYS	0	-0.084	-0.018	3.666	0.945	1.244	0.000	-0.103	-0.195	0.000
22	A	22	HIS	0	-0.021	-0.033	2.250	-5.464	-3.994	3.262	-2.461	-2.270	-0.022
23	A	23	GLY	0	0.072	0.048	4.070	0.072	0.161	0.002	-0.047	-0.044	0.000
24	A	24	SER	0	-0.016	-0.067	7.246	-0.354	-0.354	0.000	0.000	0.000	0.000
25	A	25	GLU	-1	-0.935	-0.936	8.475	-0.281	-0.281	0.000	0.000	0.000	0.000
26	A	26	PRO	0	-0.054	-0.035	9.420	-0.146	-0.146	0.000	0.000	0.000	0.000
27	A	28	ILE	0	-0.046	-0.038	9.506	0.172	0.172	0.000	0.000	0.000	0.000
28	A	29	ILE	0	0.044	0.027	11.107	-0.080	-0.080	0.000	0.000	0.000	0.000
29	A	30	HIS	1	0.808	0.873	12.498	0.603	0.603	0.000	0.000	0.000	0.000
30	A	31	ARG	1	0.908	0.933	15.500	0.215	0.215	0.000	0.000	0.000	0.000
31	A	32	GLY	0	-0.053	-0.029	18.579	0.002	0.002	0.000	0.000	0.000	0.000
32	A	33	LYS	1	0.828	0.926	14.832	0.355	0.355	0.000	0.000	0.000	0.000
33	A	34	PRO	0	0.057	0.029	12.964	-0.003	-0.003	0.000	0.000	0.000	0.000
34	A	35	PHE	0	0.002	-0.006	8.506	-0.063	-0.063	0.000	0.000	0.000	0.000
35	A	36	GLN	0	-0.028	-0.010	7.281	0.220	0.220	0.000	0.000	0.000	0.000
36	A	37	LEU	0	0.011	0.006	6.202	-0.315	-0.315	0.000	0.000	0.000	0.000
37	A	38	GLU	-1	-0.772	-0.846	6.272	1.421	1.421	0.000	0.000	0.000	0.000
38	A	39	ALA	0	-0.017	0.010	7.301	-0.044	-0.044	0.000	0.000	0.000	0.000
39	A	40	VAL	0	0.000	0.005	9.315	0.010	0.010	0.000	0.000	0.000	0.000
40	A	41	PHE	0	0.008	0.005	11.986	-0.033	-0.033	0.000	0.000	0.000	0.000
41	A	42	GLU	-1	-0.824	-0.901	15.439	0.261	0.261	0.000	0.000	0.000	0.000
42	A	43	ALA	0	-0.003	0.011	18.789	-0.019	-0.019	0.000	0.000	0.000	0.000
43	A	44	ASN	0	0.026	-0.004	21.838	0.000	0.000	0.000	0.000	0.000	0.000
44	A	45	GLN	0	0.006	-0.016	24.461	-0.015	-0.015	0.000	0.000	0.000	0.000
45	A	46	ASN	0	0.004	0.007	26.109	0.015	0.015	0.000	0.000	0.000	0.000
46	A	47	THR	0	-0.013	0.008	25.246	-0.010	-0.010	0.000	0.000	0.000	0.000
47	A	48	LYS	1	0.879	0.916	27.077	-0.046	-0.046	0.000	0.000	0.000	0.000
48	A	49	THR	0	-0.039	-0.030	26.919	-0.002	-0.002	0.000	0.000	0.000	0.000
49	A	50	ALA	0	0.062	0.010	21.601	0.009	0.009	0.000	0.000	0.000	0.000
50	A	51	LYN	0	-0.047	-0.003	22.964	-0.001	-0.001	0.000	0.000	0.000	0.000
51	A	52	ILE	0	-0.017	-0.008	17.279	0.002	0.002	0.000	0.000	0.000	0.000
52	A	53	GLU	-1	-0.841	-0.909	21.047	-0.019	-0.019	0.000	0.000	0.000	0.000
53	A	54	ILE	0	-0.008	-0.017	16.349	-0.004	-0.004	0.000	0.000	0.000	0.000
54	A	55	LYS	1	0.837	0.912	19.939	0.064	0.064	0.000	0.000	0.000	0.000
55	A	56	ALA	0	0.027	0.013	18.933	-0.016	-0.016	0.000	0.000	0.000	0.000
56	A	57	SER	0	-0.032	-0.004	20.427	0.018	0.018	0.000	0.000	0.000	0.000
57	A	58	ILE	0	-0.001	-0.018	19.810	-0.025	-0.025	0.000	0.000	0.000	0.000
58	A	59	ASP	-1	-0.822	-0.893	22.722	-0.143	-0.143	0.000	0.000	0.000	0.000
59	A	60	GLY	0	-0.009	0.002	24.278	0.012	0.012	0.000	0.000	0.000	0.000
60	A	61	LEU	0	-0.028	-0.015	25.959	0.012	0.012	0.000	0.000	0.000	0.000
61	A	62	GLU	-1	-0.837	-0.899	24.793	-0.080	-0.080	0.000	0.000	0.000	0.000
62	A	63	VAL	0	-0.050	-0.029	22.195	0.004	0.004	0.000	0.000	0.000	0.000
63	A	64	ASP	-1	-0.889	-0.950	23.365	-0.088	-0.088	0.000	0.000	0.000	0.000
64	A	65	VAL	0	-0.045	-0.017	18.115	-0.019	-0.019	0.000	0.000	0.000	0.000
65	A	66	PRO	0	0.034	0.028	21.234	0.012	0.012	0.000	0.000	0.000	0.000
66	A	67	GLY	0	-0.015	-0.024	20.288	-0.014	-0.014	0.000	0.000	0.000	0.000
67	A	68	ILE	0	-0.012	-0.001	16.902	-0.003	-0.003	0.000	0.000	0.000	0.000
68	A	69	ASP	-1	-0.781	-0.839	19.851	0.018	0.018	0.000	0.000	0.000	0.000
69	A	70	PRO	0	0.027	0.014	20.698	0.007	0.007	0.000	0.000	0.000	0.000
70	A	71	ASN	0	0.023	0.007	22.756	0.015	0.015	0.000	0.000	0.000	0.000
71	A	72	ALA	0	0.059	0.017	18.909	0.004	0.004	0.000	0.000	0.000	0.000
72	A	73	CYS	0	-0.082	-0.016	20.113	0.028	0.028	0.000	0.000	0.000	0.000
73	A	74	HIS	0	-0.063	-0.041	22.058	0.005	0.005	0.000	0.000	0.000	0.000
74	A	75	TYR	0	-0.069	-0.066	17.159	-0.001	-0.001	0.000	0.000	0.000	0.000
75	A	76	MET	0	-0.045	-0.006	17.453	0.044	0.044	0.000	0.000	0.000	0.000
76	A	77	LYS	1	0.949	0.981	18.782	-0.221	-0.221	0.000	0.000	0.000	0.000
77	A	79	PRO	0	0.034	-0.020	25.096	-0.005	-0.005	0.000	0.000	0.000	0.000
78	A	80	LEU	0	-0.050	-0.017	21.405	0.009	0.009	0.000	0.000	0.000	0.000
79	A	81	VAL	0	0.015	0.006	24.169	-0.012	-0.012	0.000	0.000	0.000	0.000
80	A	82	LYS	1	0.898	0.922	24.164	-0.088	-0.088	0.000	0.000	0.000	0.000
81	A	83	GLY	0	-0.006	0.000	23.592	-0.003	-0.003	0.000	0.000	0.000	0.000
82	A	84	GLN	0	-0.035	-0.011	21.505	0.006	0.006	0.000	0.000	0.000	0.000
83	A	85	GLN	0	-0.051	-0.037	15.679	0.039	0.039	0.000	0.000	0.000	0.000
84	A	86	TYR	0	-0.040	-0.008	16.668	-0.011	-0.011	0.000	0.000	0.000	0.000
85	A	87	ASH	0	-0.060	-0.074	9.746	-0.015	-0.015	0.000	0.000	0.000	0.000
86	A	88	ILE	0	0.011	0.007	12.343	-0.053	-0.053	0.000	0.000	0.000	0.000
87	A	89	LYS	1	0.857	0.914	9.050	-0.710	-0.710	0.000	0.000	0.000	0.000
88	A	90	TYR	0	0.015	0.014	10.693	-0.069	-0.069	0.000	0.000	0.000	0.000
89	A	91	THR	0	-0.016	-0.017	10.853	-0.039	-0.039	0.000	0.000	0.000	0.000
90	A	92	TRP	0	0.017	0.006	12.397	-0.005	-0.005	0.000	0.000	0.000	0.000
91	A	93	ASN	0	0.003	-0.013	14.142	-0.056	-0.056	0.000	0.000	0.000	0.000
92	A	94	VAL	0	0.017	0.027	14.353	0.015	0.015	0.000	0.000	0.000	0.000
93	A	95	PRO	0	0.051	0.037	17.119	0.010	0.010	0.000	0.000	0.000	0.000
94	A	96	LYS	1	0.956	0.955	20.636	0.154	0.154	0.000	0.000	0.000	0.000
95	A	97	ILE	0	-0.017	-0.016	22.505	-0.005	-0.005	0.000	0.000	0.000	0.000
96	A	98	ALA	0	0.030	0.038	20.242	0.008	0.008	0.000	0.000	0.000	0.000
97	A	99	PRO	0	0.034	0.025	22.274	-0.009	-0.009	0.000	0.000	0.000	0.000
98	A	100	LYS	1	0.927	0.953	21.084	0.161	0.161	0.000	0.000	0.000	0.000
99	A	101	SER	0	0.009	-0.020	20.388	0.015	0.015	0.000	0.000	0.000	0.000
100	A	102	GLU	-1	-0.785	-0.891	18.005	-0.344	-0.344	0.000	0.000	0.000	0.000
101	A	103	ASN	0	-0.054	-0.017	19.009	-0.010	-0.010	0.000	0.000	0.000	0.000
102	A	104	VAL	0	0.015	0.020	16.671	0.016	0.016	0.000	0.000	0.000	0.000
103	A	105	VAL	0	-0.003	0.006	17.359	-0.016	-0.016	0.000	0.000	0.000	0.000
104	A	106	VAL	0	-0.001	-0.002	14.837	0.014	0.014	0.000	0.000	0.000	0.000
105	A	107	THR	0	-0.010	-0.007	16.459	0.005	0.005	0.000	0.000	0.000	0.000
106	A	108	VAL	0	-0.019	-0.005	14.641	0.000	0.000	0.000	0.000	0.000	0.000
107	A	109	LYS	1	0.848	0.901	17.770	0.032	0.032	0.000	0.000	0.000	0.000
108	A	110	VAL	0	0.011	0.013	17.783	-0.005	-0.005	0.000	0.000	0.000	0.000
109	A	111	MET	0	0.008	0.016	20.936	0.011	0.011	0.000	0.000	0.000	0.000
110	A	112	GLY	0	0.037	0.013	24.608	0.002	0.002	0.000	0.000	0.000	0.000
111	A	113	ASP	-1	-0.808	-0.886	26.274	0.050	0.050	0.000	0.000	0.000	0.000
112	A	114	ASP	-1	-0.926	-0.952	29.239	0.056	0.056	0.000	0.000	0.000	0.000
113	A	115	GLY	0	0.005	0.006	28.476	0.001	0.001	0.000	0.000	0.000	0.000
114	A	116	VAL	0	-0.022	-0.020	23.513	0.003	0.003	0.000	0.000	0.000	0.000
115	A	117	LEU	0	-0.043	-0.017	20.950	0.009	0.009	0.000	0.000	0.000	0.000
116	A	118	ALA	0	0.013	0.000	17.248	0.020	0.020	0.000	0.000	0.000	0.000
117	A	120	ALA	0	0.034	0.026	14.049	0.020	0.020	0.000	0.000	0.000	0.000
118	A	121	ILE	0	-0.020	-0.015	16.168	-0.019	-0.019	0.000	0.000	0.000	0.000
119	A	122	ALA	0	0.022	0.021	12.081	-0.002	-0.002	0.000	0.000	0.000	0.000
120	A	123	THR	0	0.021	-0.004	13.980	0.010	0.010	0.000	0.000	0.000	0.000
121	A	124	HIS	0	0.028	0.026	10.498	0.011	0.011	0.000	0.000	0.000	0.000
122	A	125	ALA	0	0.010	0.019	12.222	-0.084	-0.084	0.000	0.000	0.000	0.000
123	A	126	LYS	1	0.862	0.938	13.141	0.401	0.401	0.000	0.000	0.000	0.000
124	A	127	ILE	0	0.009	0.026	14.884	-0.053	-0.053	0.000	0.000	0.000	0.000
125	A	128	ARG	1	0.885	0.914	15.638	0.400	0.400	0.000	0.000	0.000	0.000
126	A	129	ASP	-1	-0.814	-0.885	18.064	-0.337	-0.337	0.000	0.000	0.000	0.000

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