FMO DATABASE

FMODB ID: G5321

Calculation Name: 1KLX-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1KLX

Chain ID: A

ChEMBL ID:

UniProt ID: O25103

Base Structure: X-ray

Registration Date: 2023-09-24

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	129
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1123252.62584
FMO2-HF: Nuclear repulsion	1070295.197515
FMO2-HF: Total energy	-52957.428325
FMO2-MP2: Total energy	-53107.069314

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:3:GLY)

Summations of interaction energy for fragment #1(A:3:GLY)

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.
2.919	5.287	0.966	-1.506	-1.828	-0.002

Interaction energy analysis for fragmet #1(A:3:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.082 / q_NPA : 0.030

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	5	GLY	0	0.074	0.034	3.271	-0.971	0.855	-0.005	-0.926	-0.895	-0.001
4	A	6	THR	0	-0.049	-0.017	2.573	0.788	1.296	0.972	-0.576	-0.904	-0.001
5	A	7	VAL	0	0.140	0.054	5.129	0.221	0.255	-0.001	-0.004	-0.029	0.000
6	A	8	LYS	1	0.958	0.983	5.788	0.667	0.667	0.000	0.000	0.000	0.000
7	A	9	LYS	1	0.841	0.918	5.774	1.090	1.090	0.000	0.000	0.000	0.000
8	A	10	ASP	-1	-0.753	-0.862	7.394	-0.306	-0.306	0.000	0.000	0.000	0.000
9	A	11	LEU	0	-0.016	-0.002	10.412	0.104	0.104	0.000	0.000	0.000	0.000
10	A	12	LYS	1	0.892	0.930	8.285	0.520	0.520	0.000	0.000	0.000	0.000
11	A	13	LYS	1	0.901	0.945	11.593	0.363	0.363	0.000	0.000	0.000	0.000
12	A	14	ALA	0	0.006	0.004	13.512	0.050	0.050	0.000	0.000	0.000	0.000
13	A	15	ILE	0	-0.047	-0.010	14.269	0.034	0.034	0.000	0.000	0.000	0.000
14	A	16	GLN	0	0.040	0.003	17.341	0.025	0.025	0.000	0.000	0.000	0.000
15	A	17	TYR	0	0.018	0.032	19.193	0.011	0.011	0.000	0.000	0.000	0.000
16	A	18	TYR	0	0.071	0.014	18.402	0.005	0.005	0.000	0.000	0.000	0.000
17	A	19	VAL	0	-0.057	-0.020	21.152	0.010	0.010	0.000	0.000	0.000	0.000
18	A	20	LYS	1	0.872	0.931	23.378	0.078	0.078	0.000	0.000	0.000	0.000
19	A	21	ALA	0	0.088	0.056	24.624	0.006	0.006	0.000	0.000	0.000	0.000
20	A	22	CYS	0	-0.111	-0.047	23.924	-0.002	-0.002	0.000	0.000	0.000	0.000
21	A	23	GLU	-1	-0.810	-0.904	27.180	-0.056	-0.056	0.000	0.000	0.000	0.000
22	A	24	LEU	0	0.007	0.010	28.998	0.005	0.005	0.000	0.000	0.000	0.000
23	A	25	ASN	0	-0.031	-0.011	30.568	0.002	0.002	0.000	0.000	0.000	0.000
24	A	26	GLU	-1	-0.862	-0.928	27.399	-0.076	-0.076	0.000	0.000	0.000	0.000
25	A	27	MET	0	0.012	0.004	29.020	-0.005	-0.005	0.000	0.000	0.000	0.000
26	A	28	PHE	0	0.053	0.019	25.867	-0.007	-0.007	0.000	0.000	0.000	0.000
27	A	29	GLY	0	0.046	0.032	24.725	-0.012	-0.012	0.000	0.000	0.000	0.000
28	A	31	LEU	0	0.063	0.039	24.521	-0.006	-0.006	0.000	0.000	0.000	0.000
29	A	32	SER	0	0.004	0.008	20.526	-0.014	-0.014	0.000	0.000	0.000	0.000
30	A	33	LEU	0	-0.053	-0.033	19.801	-0.022	-0.022	0.000	0.000	0.000	0.000
31	A	34	VAL	0	-0.037	-0.027	20.321	-0.009	-0.009	0.000	0.000	0.000	0.000
32	A	35	SER	0	-0.005	-0.015	19.875	-0.003	-0.003	0.000	0.000	0.000	0.000
33	A	36	ASN	0	0.002	0.004	14.636	-0.052	-0.052	0.000	0.000	0.000	0.000
34	A	37	SER	0	0.022	0.000	12.928	0.001	0.001	0.000	0.000	0.000	0.000
35	A	38	GLN	0	-0.068	-0.027	9.826	-0.037	-0.037	0.000	0.000	0.000	0.000
36	A	39	ILE	0	-0.019	0.019	13.261	0.019	0.019	0.000	0.000	0.000	0.000
37	A	40	ASN	0	0.029	0.009	16.912	0.014	0.014	0.000	0.000	0.000	0.000
38	A	41	LYS	1	0.951	0.967	18.499	0.163	0.163	0.000	0.000	0.000	0.000
39	A	42	GLN	0	0.070	0.047	22.085	0.009	0.009	0.000	0.000	0.000	0.000
40	A	43	LYS	1	0.874	0.930	19.217	0.092	0.092	0.000	0.000	0.000	0.000
41	A	44	LEU	0	-0.018	0.005	21.559	0.002	0.002	0.000	0.000	0.000	0.000
42	A	45	PHE	0	0.051	0.032	22.982	0.005	0.005	0.000	0.000	0.000	0.000
43	A	46	GLN	0	0.050	0.043	24.328	-0.001	-0.001	0.000	0.000	0.000	0.000
44	A	47	TYR	0	-0.007	-0.021	19.224	0.008	0.008	0.000	0.000	0.000	0.000
45	A	48	LEU	0	0.024	0.007	25.662	0.003	0.003	0.000	0.000	0.000	0.000
46	A	49	SER	0	-0.020	-0.010	28.141	0.006	0.006	0.000	0.000	0.000	0.000
47	A	50	LYS	1	0.937	0.974	28.320	0.053	0.053	0.000	0.000	0.000	0.000
48	A	51	ALA	0	0.008	0.005	28.546	0.003	0.003	0.000	0.000	0.000	0.000
49	A	52	CYS	0	-0.096	-0.032	30.558	0.004	0.004	0.000	0.000	0.000	0.000
50	A	53	GLU	-1	-0.935	-0.980	33.275	-0.040	-0.040	0.000	0.000	0.000	0.000
51	A	54	LEU	0	-0.037	-0.024	30.968	0.003	0.003	0.000	0.000	0.000	0.000
52	A	55	ASN	0	-0.017	0.002	34.792	0.001	0.001	0.000	0.000	0.000	0.000
53	A	56	SER	0	0.029	0.014	30.730	0.000	0.000	0.000	0.000	0.000	0.000
54	A	57	GLY	0	0.044	0.016	33.755	0.000	0.000	0.000	0.000	0.000	0.000
55	A	58	ASN	0	0.014	-0.019	30.137	-0.006	-0.006	0.000	0.000	0.000	0.000
56	A	59	GLY	0	0.029	0.000	29.859	-0.004	-0.004	0.000	0.000	0.000	0.000
57	A	61	ARG	1	0.814	0.868	31.906	0.071	0.071	0.000	0.000	0.000	0.000
58	A	62	PHE	0	-0.031	-0.012	28.225	-0.001	-0.001	0.000	0.000	0.000	0.000
59	A	63	LEU	0	-0.043	-0.009	30.053	-0.002	-0.002	0.000	0.000	0.000	0.000
60	A	64	GLY	0	0.025	0.010	31.322	0.002	0.002	0.000	0.000	0.000	0.000
61	A	65	ASP	-1	-0.767	-0.847	30.370	-0.069	-0.069	0.000	0.000	0.000	0.000
62	A	66	PHE	0	-0.032	-0.012	24.931	-0.001	-0.001	0.000	0.000	0.000	0.000
63	A	67	TYR	0	0.022	0.008	30.805	0.002	0.002	0.000	0.000	0.000	0.000
64	A	68	GLU	-1	-0.746	-0.847	34.349	-0.046	-0.046	0.000	0.000	0.000	0.000
65	A	69	ASN	0	-0.060	-0.032	31.010	0.002	0.002	0.000	0.000	0.000	0.000
66	A	70	GLY	0	-0.022	-0.014	32.668	0.002	0.002	0.000	0.000	0.000	0.000
67	A	71	LYS	1	0.912	0.969	24.989	0.088	0.088	0.000	0.000	0.000	0.000
68	A	72	TYR	0	0.007	-0.015	24.061	-0.004	-0.004	0.000	0.000	0.000	0.000
69	A	73	VAL	0	0.031	0.030	28.015	0.001	0.001	0.000	0.000	0.000	0.000
70	A	74	LYS	1	0.906	0.955	31.350	0.034	0.034	0.000	0.000	0.000	0.000
71	A	75	LYS	1	0.908	0.924	34.922	0.051	0.051	0.000	0.000	0.000	0.000
72	A	76	ASP	-1	-0.889	-0.937	36.307	-0.032	-0.032	0.000	0.000	0.000	0.000
73	A	77	LEU	0	0.070	0.030	38.519	-0.001	-0.001	0.000	0.000	0.000	0.000
74	A	78	ARG	1	0.978	1.003	40.269	0.028	0.028	0.000	0.000	0.000	0.000
75	A	79	LYS	1	0.881	0.951	37.243	0.037	0.037	0.000	0.000	0.000	0.000
76	A	80	ALA	0	-0.006	-0.007	36.769	-0.001	-0.001	0.000	0.000	0.000	0.000
77	A	81	ALA	0	0.030	0.015	37.738	-0.001	-0.001	0.000	0.000	0.000	0.000
78	A	82	GLN	0	-0.002	0.004	40.100	-0.001	-0.001	0.000	0.000	0.000	0.000
79	A	83	TYR	0	0.025	0.012	35.622	0.001	0.001	0.000	0.000	0.000	0.000
80	A	84	TYR	0	0.021	-0.036	34.398	0.001	0.001	0.000	0.000	0.000	0.000
81	A	85	SER	0	0.008	0.009	38.600	0.001	0.001	0.000	0.000	0.000	0.000
82	A	86	LYS	1	0.807	0.891	37.558	0.040	0.040	0.000	0.000	0.000	0.000
83	A	87	ALA	0	0.005	0.007	36.495	0.000	0.000	0.000	0.000	0.000	0.000
84	A	88	CYS	0	-0.055	-0.002	37.944	0.003	0.003	0.000	0.000	0.000	0.000
85	A	89	GLY	0	-0.007	-0.003	41.292	0.001	0.001	0.000	0.000	0.000	0.000
86	A	90	LEU	0	-0.044	-0.031	37.296	0.001	0.001	0.000	0.000	0.000	0.000
87	A	91	ASN	0	-0.013	0.004	40.048	0.001	0.001	0.000	0.000	0.000	0.000
88	A	92	ASP	-1	-0.786	-0.892	34.635	-0.062	-0.062	0.000	0.000	0.000	0.000
89	A	93	GLN	0	-0.001	-0.013	37.612	0.000	0.000	0.000	0.000	0.000	0.000
90	A	94	ASP	-1	-0.750	-0.859	33.951	-0.064	-0.064	0.000	0.000	0.000	0.000
91	A	95	GLY	0	-0.025	-0.028	36.896	0.001	0.001	0.000	0.000	0.000	0.000
92	A	97	LEU	0	0.060	0.040	38.242	0.002	0.002	0.000	0.000	0.000	0.000
93	A	98	ILE	0	-0.013	-0.009	35.202	0.002	0.002	0.000	0.000	0.000	0.000
94	A	99	LEU	0	-0.041	-0.024	39.681	0.002	0.002	0.000	0.000	0.000	0.000
95	A	100	GLY	0	0.033	0.018	42.324	0.002	0.002	0.000	0.000	0.000	0.000
96	A	101	TYR	0	0.054	0.021	40.885	0.003	0.003	0.000	0.000	0.000	0.000
97	A	102	LYS	1	0.780	0.900	37.726	0.050	0.050	0.000	0.000	0.000	0.000
98	A	103	GLN	0	0.048	0.037	44.036	0.002	0.002	0.000	0.000	0.000	0.000
99	A	104	TYR	0	0.033	0.000	47.288	0.001	0.001	0.000	0.000	0.000	0.000
100	A	105	ALA	0	-0.031	-0.009	45.692	0.001	0.001	0.000	0.000	0.000	0.000
101	A	106	GLY	0	0.039	0.016	47.696	0.001	0.001	0.000	0.000	0.000	0.000
102	A	107	LYS	1	0.817	0.908	38.921	0.047	0.047	0.000	0.000	0.000	0.000
103	A	108	GLY	0	0.008	-0.010	43.144	-0.002	-0.002	0.000	0.000	0.000	0.000
104	A	109	VAL	0	-0.061	-0.034	44.272	0.001	0.001	0.000	0.000	0.000	0.000
105	A	110	VAL	0	0.024	0.009	47.327	0.000	0.000	0.000	0.000	0.000	0.000
106	A	111	LYS	1	0.870	0.924	50.534	0.028	0.028	0.000	0.000	0.000	0.000
107	A	112	ASN	0	-0.017	-0.007	51.109	0.002	0.002	0.000	0.000	0.000	0.000
108	A	113	GLU	-1	-0.767	-0.860	52.003	-0.028	-0.028	0.000	0.000	0.000	0.000
109	A	114	LYS	1	0.980	0.987	52.974	0.021	0.021	0.000	0.000	0.000	0.000
110	A	115	GLN	0	-0.044	-0.015	49.658	0.001	0.001	0.000	0.000	0.000	0.000
111	A	116	ALA	0	0.029	0.012	48.625	-0.001	-0.001	0.000	0.000	0.000	0.000
112	A	117	VAL	0	0.043	0.030	48.826	-0.001	-0.001	0.000	0.000	0.000	0.000
113	A	118	LYS	1	0.989	0.998	50.496	0.024	0.024	0.000	0.000	0.000	0.000
114	A	119	THR	0	-0.074	-0.057	44.989	0.000	0.000	0.000	0.000	0.000	0.000
115	A	120	PHE	0	0.029	0.005	43.920	-0.002	-0.002	0.000	0.000	0.000	0.000
116	A	121	GLU	-1	-0.798	-0.885	46.937	-0.028	-0.028	0.000	0.000	0.000	0.000
117	A	122	LYS	1	0.778	0.884	44.225	0.035	0.035	0.000	0.000	0.000	0.000
118	A	123	ALA	0	0.025	-0.002	42.583	-0.001	-0.001	0.000	0.000	0.000	0.000
119	A	124	CYS	0	-0.055	-0.013	43.240	0.001	0.001	0.000	0.000	0.000	0.000
120	A	125	ARG	1	0.855	0.898	45.416	0.029	0.029	0.000	0.000	0.000	0.000
121	A	126	LEU	0	-0.076	-0.024	41.279	0.000	0.000	0.000	0.000	0.000	0.000
122	A	127	GLY	0	0.024	0.018	41.092	-0.003	-0.003	0.000	0.000	0.000	0.000
123	A	128	SER	0	-0.026	-0.012	40.255	-0.001	-0.001	0.000	0.000	0.000	0.000
124	A	129	GLU	-1	-0.870	-0.949	40.982	-0.046	-0.046	0.000	0.000	0.000	0.000
125	A	130	ASP	-1	-0.901	-0.945	40.176	-0.050	-0.050	0.000	0.000	0.000	0.000
126	A	131	ALA	0	-0.022	-0.020	42.991	0.002	0.002	0.000	0.000	0.000	0.000
127	A	133	GLY	0	0.020	0.020	46.272	0.002	0.002	0.000	0.000	0.000	0.000
128	A	134	ILE	0	-0.084	-0.036	44.522	0.001	0.001	0.000	0.000	0.000	0.000
129	A	135	LEU	0	-0.111	-0.044	48.551	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:3:GLY)