FMO DATABASE

FMODB ID: 2K1RR

Calculation Name: 1HLV-A-Xray309

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1HLV

Chain ID: A

ChEMBL ID:

UniProt ID: P07199

Base Structure: X-ray

Registration Date: 2021-09-06

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:

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. 1.20200116

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	131
LigandCharge
Software	ABINIT-MP - Open Ver.1 Rev. 15 / 20190524

Total energy (hartree)

FMO2-HF: Electronic energy	-1079528.585637
FMO2-HF: Nuclear repulsion	1027113.020453
FMO2-HF: Total energy	-52415.565185
FMO2-MP2: Total energy	-52570.505446

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:MET )

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

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.
1.726	4.801	0.067	-1.784	-1.358	0.007

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.054 / q_NPA : 0.028

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	3	PRO	0	-0.024	-0.016	3.292	-2.499	0.576	0.067	-1.784	-1.358	0.007
4	A	4	LYS	1	1.018	0.995	5.034	1.235	1.235	0.000	0.000	0.000	0.000
5	A	5	ARG	1	0.943	0.963	7.173	0.649	0.649	0.000	0.000	0.000	0.000
6	A	6	ARG	1	1.011	1.021	10.755	0.294	0.294	0.000	0.000	0.000	0.000
7	A	7	GLN	0	-0.027	-0.018	12.882	0.101	0.101	0.000	0.000	0.000	0.000
8	A	8	LEU	0	0.013	0.010	15.609	-0.011	-0.011	0.000	0.000	0.000	0.000
9	A	9	THR	0	-0.024	-0.031	18.942	0.008	0.008	0.000	0.000	0.000	0.000
10	A	10	PHE	0	-0.038	-0.047	21.946	0.013	0.013	0.000	0.000	0.000	0.000
11	A	11	ARG	1	0.974	0.998	25.270	0.183	0.183	0.000	0.000	0.000	0.000
12	A	12	GLU	-1	-0.862	-0.919	20.410	-0.322	-0.322	0.000	0.000	0.000	0.000
13	A	13	LYS	1	0.855	0.921	21.176	0.294	0.294	0.000	0.000	0.000	0.000
14	A	14	SER	0	-0.015	-0.005	24.742	0.016	0.016	0.000	0.000	0.000	0.000
15	A	15	ARG	1	1.025	1.022	26.411	0.162	0.162	0.000	0.000	0.000	0.000
16	A	16	ILE	0	-0.038	-0.014	22.227	0.008	0.008	0.000	0.000	0.000	0.000
17	A	17	ILE	0	-0.058	-0.042	26.828	0.010	0.010	0.000	0.000	0.000	0.000
18	A	18	GLN	0	-0.014	-0.008	29.476	-0.002	-0.002	0.000	0.000	0.000	0.000
19	A	19	GLU	-1	-0.872	-0.939	28.965	-0.101	-0.101	0.000	0.000	0.000	0.000
20	A	20	VAL	0	-0.108	-0.070	29.043	0.008	0.008	0.000	0.000	0.000	0.000
21	A	21	GLU	-1	-0.988	-0.999	31.774	-0.098	-0.098	0.000	0.000	0.000	0.000
22	A	22	GLU	-1	-0.863	-0.917	34.601	-0.090	-0.090	0.000	0.000	0.000	0.000
23	A	23	ASN	0	-0.059	-0.027	33.349	0.010	0.010	0.000	0.000	0.000	0.000
24	A	24	PRO	0	-0.016	-0.016	34.549	-0.002	-0.002	0.000	0.000	0.000	0.000
25	A	25	ASP	-1	-0.894	-0.926	36.435	-0.055	-0.055	0.000	0.000	0.000	0.000
26	A	26	LEU	0	-0.032	-0.004	31.976	0.002	0.002	0.000	0.000	0.000	0.000
27	A	27	ARG	1	0.959	0.975	29.956	0.047	0.047	0.000	0.000	0.000	0.000
28	A	28	LYS	1	1.017	0.997	27.596	0.087	0.087	0.000	0.000	0.000	0.000
29	A	29	GLY	0	0.000	-0.007	25.067	-0.009	-0.009	0.000	0.000	0.000	0.000
30	A	30	GLU	-1	-0.814	-0.909	25.072	-0.078	-0.078	0.000	0.000	0.000	0.000
31	A	31	ILE	0	0.048	0.021	26.475	-0.006	-0.006	0.000	0.000	0.000	0.000
32	A	32	ALA	0	-0.040	-0.033	22.172	-0.011	-0.011	0.000	0.000	0.000	0.000
33	A	33	ARG	1	0.944	0.976	21.975	0.061	0.061	0.000	0.000	0.000	0.000
34	A	34	ARG	1	0.871	0.956	22.523	0.080	0.080	0.000	0.000	0.000	0.000
35	A	35	PHE	0	-0.018	-0.004	21.911	-0.010	-0.010	0.000	0.000	0.000	0.000
36	A	36	ASN	0	-0.051	-0.016	15.988	-0.010	-0.010	0.000	0.000	0.000	0.000
37	A	37	ILE	0	-0.071	-0.031	17.405	-0.042	-0.042	0.000	0.000	0.000	0.000
38	A	38	PRO	0	0.046	0.014	15.632	0.027	0.027	0.000	0.000	0.000	0.000
39	A	39	PRO	0	0.104	0.039	18.463	-0.007	-0.007	0.000	0.000	0.000	0.000
40	A	40	SER	0	0.003	0.006	18.910	0.000	0.000	0.000	0.000	0.000	0.000
41	A	41	THR	0	0.041	-0.007	17.715	-0.005	-0.005	0.000	0.000	0.000	0.000
42	A	42	LEU	0	0.032	0.025	20.280	-0.003	-0.003	0.000	0.000	0.000	0.000
43	A	43	SER	0	0.007	0.004	23.541	0.010	0.010	0.000	0.000	0.000	0.000
44	A	44	THR	0	-0.053	-0.013	21.087	0.005	0.005	0.000	0.000	0.000	0.000
45	A	45	ILE	0	0.020	0.010	21.540	-0.001	-0.001	0.000	0.000	0.000	0.000
46	A	46	LEU	0	0.024	0.000	24.986	0.008	0.008	0.000	0.000	0.000	0.000
47	A	47	LYS	1	0.952	0.980	27.685	0.123	0.123	0.000	0.000	0.000	0.000
48	A	48	ASN	0	-0.061	-0.023	24.836	0.012	0.012	0.000	0.000	0.000	0.000
49	A	49	LYS	1	0.982	1.002	28.502	0.103	0.103	0.000	0.000	0.000	0.000
50	A	50	ARG	1	1.012	0.991	30.477	0.092	0.092	0.000	0.000	0.000	0.000
51	A	51	ALA	0	0.020	0.023	29.202	0.000	0.000	0.000	0.000	0.000	0.000
52	A	52	ILE	0	-0.028	-0.023	25.227	-0.009	-0.009	0.000	0.000	0.000	0.000
53	A	53	LEU	0	0.084	0.038	28.654	-0.005	-0.005	0.000	0.000	0.000	0.000
54	A	54	ALA	0	-0.047	-0.016	31.772	0.004	0.004	0.000	0.000	0.000	0.000
55	A	55	SER	0	-0.045	-0.031	27.964	-0.003	-0.003	0.000	0.000	0.000	0.000
56	A	56	GLU	-1	-0.828	-0.907	29.446	-0.164	-0.164	0.000	0.000	0.000	0.000
57	A	57	ARG	1	0.963	0.985	30.292	0.121	0.121	0.000	0.000	0.000	0.000
58	A	58	LYS	1	0.882	0.961	29.476	0.174	0.174	0.000	0.000	0.000	0.000
59	A	59	TYR	0	-0.041	-0.045	27.443	-0.006	-0.006	0.000	0.000	0.000	0.000
60	A	60	GLY	0	0.111	0.075	30.552	-0.003	-0.003	0.000	0.000	0.000	0.000
61	A	61	VAL	0	0.039	0.006	30.836	-0.010	-0.010	0.000	0.000	0.000	0.000
62	A	62	ALA	0	0.073	0.046	27.164	-0.012	-0.012	0.000	0.000	0.000	0.000
63	A	63	SER	0	-0.054	-0.032	26.104	-0.026	-0.026	0.000	0.000	0.000	0.000
64	A	64	THR	0	0.014	0.003	24.937	-0.009	-0.009	0.000	0.000	0.000	0.000
65	A	65	CYS	0	-0.033	-0.020	22.131	-0.021	-0.021	0.000	0.000	0.000	0.000
66	A	66	ARG	1	0.864	0.951	21.325	0.218	0.218	0.000	0.000	0.000	0.000
67	A	67	LYS	1	0.991	0.994	15.962	0.547	0.547	0.000	0.000	0.000	0.000
68	A	68	THR	0	0.026	0.013	19.468	0.014	0.014	0.000	0.000	0.000	0.000
69	A	69	ASN	0	0.057	0.035	22.113	0.003	0.003	0.000	0.000	0.000	0.000
70	A	70	LYS	1	0.952	0.983	21.837	0.262	0.262	0.000	0.000	0.000	0.000
71	A	71	LEU	0	0.020	0.011	24.891	0.000	0.000	0.000	0.000	0.000	0.000
72	A	72	SER	0	-0.043	-0.009	27.333	-0.011	-0.011	0.000	0.000	0.000	0.000
73	A	73	PRO	0	0.053	0.018	28.480	0.004	0.004	0.000	0.000	0.000	0.000
74	A	74	TYR	0	0.066	0.022	31.221	0.007	0.007	0.000	0.000	0.000	0.000
75	A	75	ASP	-1	-0.958	-0.983	32.226	-0.134	-0.134	0.000	0.000	0.000	0.000
76	A	76	LYS	1	1.034	1.018	34.059	0.091	0.091	0.000	0.000	0.000	0.000
77	A	77	LEU	0	0.036	0.016	36.964	0.003	0.003	0.000	0.000	0.000	0.000
78	A	78	GLU	-1	-0.778	-0.891	32.307	-0.155	-0.155	0.000	0.000	0.000	0.000
79	A	79	GLY	0	0.006	0.018	36.760	0.001	0.001	0.000	0.000	0.000	0.000
80	A	80	LEU	0	0.024	0.009	38.732	0.003	0.003	0.000	0.000	0.000	0.000
81	A	81	LEU	0	-0.010	-0.004	37.517	0.003	0.003	0.000	0.000	0.000	0.000
82	A	82	ILE	0	-0.013	-0.013	35.495	0.001	0.001	0.000	0.000	0.000	0.000
83	A	83	ALA	0	-0.010	0.000	39.974	0.003	0.003	0.000	0.000	0.000	0.000
84	A	84	TRP	0	0.050	0.021	42.539	0.002	0.002	0.000	0.000	0.000	0.000
85	A	85	PHE	0	0.022	0.000	37.702	0.002	0.002	0.000	0.000	0.000	0.000
86	A	86	GLN	0	-0.046	-0.037	39.834	-0.005	-0.005	0.000	0.000	0.000	0.000
87	A	87	GLN	0	0.013	0.012	43.542	0.001	0.001	0.000	0.000	0.000	0.000
88	A	88	ILE	0	-0.016	0.003	45.981	0.003	0.003	0.000	0.000	0.000	0.000
89	A	89	ARG	1	0.917	0.951	40.442	0.100	0.100	0.000	0.000	0.000	0.000
90	A	90	ALA	0	-0.020	0.010	45.908	0.001	0.001	0.000	0.000	0.000	0.000
91	A	91	ALA	0	-0.010	0.002	48.156	0.002	0.002	0.000	0.000	0.000	0.000
92	A	92	GLY	0	0.015	0.012	48.273	0.002	0.002	0.000	0.000	0.000	0.000
93	A	93	LEU	0	-0.015	0.002	48.285	0.001	0.001	0.000	0.000	0.000	0.000
94	A	94	PRO	0	-0.025	-0.010	44.375	-0.004	-0.004	0.000	0.000	0.000	0.000
95	A	95	VAL	0	0.037	0.010	41.304	0.003	0.003	0.000	0.000	0.000	0.000
96	A	96	LYS	1	0.988	0.986	42.112	0.063	0.063	0.000	0.000	0.000	0.000
97	A	97	GLY	0	0.004	-0.006	39.750	-0.001	-0.001	0.000	0.000	0.000	0.000
98	A	98	ILE	0	0.065	0.023	40.432	-0.003	-0.003	0.000	0.000	0.000	0.000
99	A	99	ILE	0	0.054	0.027	42.726	0.001	0.001	0.000	0.000	0.000	0.000
100	A	100	LEU	0	-0.041	-0.017	37.203	0.000	0.000	0.000	0.000	0.000	0.000
101	A	101	LYS	1	0.949	0.964	37.516	0.096	0.096	0.000	0.000	0.000	0.000
102	A	102	GLU	-1	-0.878	-0.919	40.334	-0.069	-0.069	0.000	0.000	0.000	0.000
103	A	103	LYS	1	0.934	0.964	43.203	0.076	0.076	0.000	0.000	0.000	0.000
104	A	104	ALA	0	-0.011	-0.017	38.842	0.000	0.000	0.000	0.000	0.000	0.000
105	A	105	LEU	0	0.001	-0.005	39.782	-0.001	-0.001	0.000	0.000	0.000	0.000
106	A	106	ARG	1	0.970	0.994	42.226	0.069	0.069	0.000	0.000	0.000	0.000
107	A	107	ILE	0	-0.027	-0.008	42.016	0.001	0.001	0.000	0.000	0.000	0.000
108	A	108	ALA	0	-0.010	-0.040	40.185	0.000	0.000	0.000	0.000	0.000	0.000
109	A	109	GLU	-1	-0.913	-0.934	41.963	-0.066	-0.066	0.000	0.000	0.000	0.000
110	A	110	GLU	-1	-0.978	-0.983	45.278	-0.064	-0.064	0.000	0.000	0.000	0.000
111	A	111	LEU	0	-0.125	-0.086	40.340	0.000	0.000	0.000	0.000	0.000	0.000
112	A	112	GLY	0	0.055	0.050	43.332	0.000	0.000	0.000	0.000	0.000	0.000
113	A	113	MET	0	-0.160	-0.053	38.369	-0.006	-0.006	0.000	0.000	0.000	0.000
114	A	114	ASP	-1	-0.833	-0.928	40.451	-0.074	-0.074	0.000	0.000	0.000	0.000
115	A	115	ASP	-1	-0.900	-0.937	35.778	-0.092	-0.092	0.000	0.000	0.000	0.000
116	A	116	PHE	0	-0.125	-0.060	34.566	-0.009	-0.009	0.000	0.000	0.000	0.000
117	A	117	THR	0	0.055	0.019	35.111	0.004	0.004	0.000	0.000	0.000	0.000
118	A	118	ALA	0	-0.034	-0.022	35.798	0.001	0.001	0.000	0.000	0.000	0.000
119	A	119	SER	0	-0.006	0.000	31.105	-0.004	-0.004	0.000	0.000	0.000	0.000
120	A	120	ASN	0	0.102	0.028	31.293	-0.002	-0.002	0.000	0.000	0.000	0.000
121	A	121	GLY	0	0.012	0.009	28.223	-0.008	-0.008	0.000	0.000	0.000	0.000
122	A	122	TRP	0	-0.050	-0.015	28.580	-0.013	-0.013	0.000	0.000	0.000	0.000
123	A	123	LEU	0	0.041	0.016	30.492	-0.004	-0.004	0.000	0.000	0.000	0.000
124	A	124	ASP	-1	-0.896	-0.947	27.219	-0.196	-0.196	0.000	0.000	0.000	0.000
125	A	125	ARG	1	0.903	0.939	24.391	0.205	0.205	0.000	0.000	0.000	0.000
126	A	126	PHE	0	-0.008	0.008	27.935	-0.006	-0.006	0.000	0.000	0.000	0.000
127	A	127	ARG	1	0.972	0.971	31.128	0.127	0.127	0.000	0.000	0.000	0.000
128	A	128	ARG	1	0.967	0.984	22.697	0.253	0.253	0.000	0.000	0.000	0.000
129	A	129	ARG	1	0.714	0.847	27.550	0.171	0.171	0.000	0.000	0.000	0.000
130	A	130	ARG	1	0.776	0.898	28.491	0.132	0.132	0.000	0.000	0.000	0.000
131	A	131	SER	-1	-0.840	-0.897	30.026	-0.140	-0.140	0.000	0.000	0.000	0.000

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