FMO DATABASE

FMODB ID: LNGR9

Calculation Name: 1M1S-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1M1S

Chain ID: A

ChEMBL ID:

UniProt ID: Q23246

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	109
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-800853.27249
FMO2-HF: Nuclear repulsion	759616.552512
FMO2-HF: Total energy	-41236.719978
FMO2-MP2: Total energy	-41358.274947

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:98:HIS)

Summations of interaction energy for fragment #1(A:98:HIS)

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.
-2.975	-0.088	0.067	-1.39	-1.563	0.007

Interaction energy analysis for fragmet #1(A:98:HIS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.075 / q_NPA : 0.046

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	100	MET	0	0.011	0.006	3.693	-4.704	-1.817	0.067	-1.390	-1.563	0.007
4	A	101	ILE	0	-0.003	0.011	5.644	-0.232	-0.232	0.000	0.000	0.000	0.000
5	A	102	ASN	0	0.000	0.012	6.852	1.469	1.469	0.000	0.000	0.000	0.000
6	A	103	VAL	0	-0.004	-0.014	9.127	-0.291	-0.291	0.000	0.000	0.000	0.000
7	A	104	ASP	-1	-0.850	-0.888	11.811	0.565	0.565	0.000	0.000	0.000	0.000
8	A	105	PRO	0	0.003	-0.019	14.485	-0.046	-0.046	0.000	0.000	0.000	0.000
9	A	106	PRO	0	0.093	0.057	10.404	-0.016	-0.016	0.000	0.000	0.000	0.000
10	A	107	THR	0	-0.063	-0.048	12.217	-0.133	-0.133	0.000	0.000	0.000	0.000
11	A	108	GLY	0	-0.010	0.007	15.155	0.042	0.042	0.000	0.000	0.000	0.000
12	A	109	ASN	0	-0.015	-0.016	18.856	-0.013	-0.013	0.000	0.000	0.000	0.000
13	A	110	TYR	0	0.000	-0.019	20.869	0.012	0.012	0.000	0.000	0.000	0.000
14	A	111	PRO	0	0.044	0.027	25.371	-0.012	-0.012	0.000	0.000	0.000	0.000
15	A	112	ALA	0	0.006	0.002	28.629	0.002	0.002	0.000	0.000	0.000	0.000
16	A	113	THR	0	0.036	0.012	29.576	0.000	0.000	0.000	0.000	0.000	0.000
17	A	114	GLY	0	0.003	0.010	29.944	0.002	0.002	0.000	0.000	0.000	0.000
18	A	115	GLY	0	0.011	-0.004	27.615	-0.001	-0.001	0.000	0.000	0.000	0.000
19	A	116	ASN	0	-0.040	-0.032	25.742	0.001	0.001	0.000	0.000	0.000	0.000
20	A	117	SER	0	0.022	0.042	21.109	-0.002	-0.002	0.000	0.000	0.000	0.000
21	A	118	THR	0	0.009	-0.008	21.452	-0.005	-0.005	0.000	0.000	0.000	0.000
22	A	119	HIS	1	0.769	0.881	15.857	-0.163	-0.163	0.000	0.000	0.000	0.000
23	A	120	ASN	0	-0.026	-0.029	15.531	-0.059	-0.059	0.000	0.000	0.000	0.000
24	A	121	ILE	0	0.016	0.005	12.757	0.033	0.033	0.000	0.000	0.000	0.000
25	A	122	THR	0	0.021	0.006	12.048	-0.029	-0.029	0.000	0.000	0.000	0.000
26	A	123	SER	0	-0.001	0.002	10.653	0.151	0.151	0.000	0.000	0.000	0.000
27	A	124	GLU	-1	-0.864	-0.961	6.109	0.299	0.299	0.000	0.000	0.000	0.000
28	A	125	SER	0	-0.035	-0.019	7.604	-0.235	-0.235	0.000	0.000	0.000	0.000
29	A	126	ASP	-1	-0.861	-0.925	8.718	0.187	0.187	0.000	0.000	0.000	0.000
30	A	127	SER	0	-0.005	0.003	10.985	0.018	0.018	0.000	0.000	0.000	0.000
31	A	128	ARG	1	0.813	0.906	12.489	-0.127	-0.127	0.000	0.000	0.000	0.000
32	A	129	LEU	0	0.006	0.012	10.054	0.011	0.011	0.000	0.000	0.000	0.000
33	A	130	ALA	0	-0.003	0.003	14.074	-0.020	-0.020	0.000	0.000	0.000	0.000
34	A	131	PHE	0	-0.023	-0.022	14.790	0.039	0.039	0.000	0.000	0.000	0.000
35	A	132	LYS	1	0.913	0.962	15.639	-0.056	-0.056	0.000	0.000	0.000	0.000
36	A	133	VAL	0	-0.045	-0.017	15.701	0.009	0.009	0.000	0.000	0.000	0.000
37	A	134	LYS	1	0.797	0.911	13.959	0.138	0.138	0.000	0.000	0.000	0.000
38	A	135	SER	0	0.003	-0.022	17.288	0.002	0.002	0.000	0.000	0.000	0.000
39	A	136	SER	0	-0.040	-0.035	19.512	-0.007	-0.007	0.000	0.000	0.000	0.000
40	A	137	ASN	0	-0.020	-0.024	21.028	0.006	0.006	0.000	0.000	0.000	0.000
41	A	138	ASN	0	-0.025	-0.006	23.676	0.013	0.013	0.000	0.000	0.000	0.000
42	A	139	GLU	-1	-0.852	-0.905	26.039	-0.044	-0.044	0.000	0.000	0.000	0.000
43	A	140	HIS	0	-0.019	-0.025	26.956	0.000	0.000	0.000	0.000	0.000	0.000
44	A	141	TYR	0	-0.016	-0.012	22.677	0.009	0.009	0.000	0.000	0.000	0.000
45	A	142	ARG	1	0.870	0.941	25.615	-0.037	-0.037	0.000	0.000	0.000	0.000
46	A	143	VAL	0	0.025	0.011	19.777	0.008	0.008	0.000	0.000	0.000	0.000
47	A	144	ARG	1	0.877	0.952	22.719	-0.049	-0.049	0.000	0.000	0.000	0.000
48	A	145	PRO	0	0.051	0.035	20.872	0.005	0.005	0.000	0.000	0.000	0.000
49	A	146	VAL	0	0.025	-0.009	20.999	0.004	0.004	0.000	0.000	0.000	0.000
50	A	147	TYR	0	0.022	0.000	19.849	-0.003	-0.003	0.000	0.000	0.000	0.000
51	A	148	GLY	0	0.003	0.001	19.719	-0.009	-0.009	0.000	0.000	0.000	0.000
52	A	149	PHE	0	0.051	0.026	18.043	0.008	0.008	0.000	0.000	0.000	0.000
53	A	150	VAL	0	-0.013	-0.001	14.220	0.006	0.006	0.000	0.000	0.000	0.000
54	A	151	ASP	-1	-0.861	-0.926	15.007	0.165	0.165	0.000	0.000	0.000	0.000
55	A	152	ALA	0	0.024	0.014	13.469	0.024	0.024	0.000	0.000	0.000	0.000
56	A	153	LYS	1	0.765	0.879	8.960	-0.059	-0.059	0.000	0.000	0.000	0.000
57	A	154	GLY	0	0.015	0.029	13.079	0.010	0.010	0.000	0.000	0.000	0.000
58	A	155	LYS	1	0.909	0.933	14.506	-0.167	-0.167	0.000	0.000	0.000	0.000
59	A	156	SER	0	-0.015	-0.014	16.899	-0.038	-0.038	0.000	0.000	0.000	0.000
60	A	157	LYS	1	0.823	0.893	18.100	-0.092	-0.092	0.000	0.000	0.000	0.000
61	A	158	LEU	0	-0.006	0.000	16.412	-0.013	-0.013	0.000	0.000	0.000	0.000
62	A	159	ASP	-1	-0.811	-0.871	19.697	0.107	0.107	0.000	0.000	0.000	0.000
63	A	160	ILE	0	0.006	-0.008	17.727	-0.010	-0.010	0.000	0.000	0.000	0.000
64	A	161	ASN	0	0.014	0.009	22.370	0.004	0.004	0.000	0.000	0.000	0.000
65	A	162	ARG	1	0.834	0.929	25.129	0.036	0.036	0.000	0.000	0.000	0.000
66	A	163	LEU	0	-0.032	-0.014	26.545	0.008	0.008	0.000	0.000	0.000	0.000
67	A	164	PRO	0	0.026	0.000	29.909	-0.005	-0.005	0.000	0.000	0.000	0.000
68	A	165	GLY	0	0.039	0.028	30.654	-0.001	-0.001	0.000	0.000	0.000	0.000
69	A	166	PRO	0	-0.003	0.005	29.374	0.002	0.002	0.000	0.000	0.000	0.000
70	A	167	PRO	0	0.001	0.003	28.324	0.001	0.001	0.000	0.000	0.000	0.000
71	A	168	LYS	1	0.842	0.901	23.664	0.107	0.107	0.000	0.000	0.000	0.000
72	A	169	GLU	-1	-0.794	-0.883	18.405	-0.204	-0.204	0.000	0.000	0.000	0.000
73	A	170	ASP	-1	-0.778	-0.850	20.316	-0.107	-0.107	0.000	0.000	0.000	0.000
74	A	171	LYS	1	0.934	0.966	14.179	0.342	0.342	0.000	0.000	0.000	0.000
75	A	172	ILE	0	0.032	0.025	14.537	0.009	0.009	0.000	0.000	0.000	0.000
76	A	173	VAL	0	-0.072	-0.048	11.345	-0.044	-0.044	0.000	0.000	0.000	0.000
77	A	174	ILE	0	0.035	0.021	11.638	-0.016	-0.016	0.000	0.000	0.000	0.000
78	A	175	GLN	0	0.017	-0.007	11.055	0.081	0.081	0.000	0.000	0.000	0.000
79	A	176	TYR	0	-0.026	-0.032	5.940	0.012	0.012	0.000	0.000	0.000	0.000
80	A	177	ALA	0	0.047	0.017	12.127	-0.006	-0.006	0.000	0.000	0.000	0.000
81	A	178	GLU	-1	-0.818	-0.869	9.348	0.154	0.154	0.000	0.000	0.000	0.000
82	A	179	VAL	0	-0.041	-0.028	12.871	-0.015	-0.015	0.000	0.000	0.000	0.000
83	A	180	PRO	0	0.055	0.027	16.518	0.002	0.002	0.000	0.000	0.000	0.000
84	A	181	ALA	0	-0.001	-0.014	18.992	0.002	0.002	0.000	0.000	0.000	0.000
85	A	182	GLU	-1	-0.939	-0.964	21.009	0.085	0.085	0.000	0.000	0.000	0.000
86	A	183	GLU	-1	-0.853	-0.907	20.352	0.088	0.088	0.000	0.000	0.000	0.000
87	A	184	THR	0	0.010	-0.003	22.541	0.004	0.004	0.000	0.000	0.000	0.000
88	A	185	ASP	-1	-0.788	-0.890	24.335	0.067	0.067	0.000	0.000	0.000	0.000
89	A	186	PRO	0	-0.026	-0.009	20.843	0.003	0.003	0.000	0.000	0.000	0.000
90	A	187	MET	0	-0.043	-0.043	20.461	0.003	0.003	0.000	0.000	0.000	0.000
91	A	188	ALA	0	0.021	0.041	22.162	-0.008	-0.008	0.000	0.000	0.000	0.000
92	A	189	PRO	0	0.057	0.024	17.244	-0.010	-0.010	0.000	0.000	0.000	0.000
93	A	190	PHE	0	-0.044	-0.025	15.107	-0.013	-0.013	0.000	0.000	0.000	0.000
94	A	191	LYS	1	0.764	0.862	19.801	-0.068	-0.068	0.000	0.000	0.000	0.000
95	A	192	ALA	0	-0.006	0.008	20.799	-0.011	-0.011	0.000	0.000	0.000	0.000
96	A	193	GLY	0	-0.025	0.003	19.460	-0.003	-0.003	0.000	0.000	0.000	0.000
97	A	194	ALA	0	0.009	0.000	16.450	-0.011	-0.011	0.000	0.000	0.000	0.000
98	A	195	GLN	0	-0.093	-0.051	13.457	0.035	0.035	0.000	0.000	0.000	0.000
99	A	196	GLN	0	-0.009	-0.023	9.006	-0.068	-0.068	0.000	0.000	0.000	0.000
100	A	197	GLY	0	0.016	0.015	8.146	0.119	0.119	0.000	0.000	0.000	0.000
101	A	198	GLU	-1	-0.825	-0.916	7.891	-0.243	-0.243	0.000	0.000	0.000	0.000
102	A	199	ILE	0	0.027	0.033	5.646	-0.311	-0.311	0.000	0.000	0.000	0.000
103	A	200	ILE	0	-0.047	-0.029	8.136	-0.004	-0.004	0.000	0.000	0.000	0.000
104	A	201	VAL	0	0.008	0.015	10.116	0.030	0.030	0.000	0.000	0.000	0.000
105	A	202	LYS	1	0.879	0.921	12.924	0.253	0.253	0.000	0.000	0.000	0.000
106	A	203	LEU	0	-0.010	-0.011	15.553	0.051	0.051	0.000	0.000	0.000	0.000
107	A	204	ILE	0	0.015	0.010	18.177	-0.012	-0.012	0.000	0.000	0.000	0.000
108	A	205	ALA	0	0.002	0.005	21.363	0.020	0.020	0.000	0.000	0.000	0.000
109	A	206	ALA	0	0.030	0.016	25.082	-0.006	-0.006	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:98:HIS)