FMO DATABASE

FMODB ID: ZY7MN

Calculation Name: 1S29-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1S29

Chain ID: A

ChEMBL ID:

UniProt ID: Q9NIH4

Base Structure: X-ray

Registration Date: 2023-03-13

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	92
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-670100.916751
FMO2-HF: Nuclear repulsion	633295.553072
FMO2-HF: Total energy	-36805.363679
FMO2-MP2: Total energy	-36912.642175

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:GLY)

Summations of interaction energy for fragment #1(A:1: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.
-4.279	-0.233	1.635	-2.458	-3.22	-0.013

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.068 / q_NPA : 0.019

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	HIS	0	0.019	0.013	3.391	-1.103	0.447	0.042	-0.743	-0.848	0.000
4	A	4	MET	0	-0.070	-0.041	3.160	1.001	1.584	0.049	-0.208	-0.425	0.000
5	A	5	PRO	0	0.035	0.038	2.685	-2.148	-0.850	1.546	-1.400	-1.444	-0.013
6	A	6	LEU	0	0.018	0.008	4.436	0.777	0.914	-0.001	-0.013	-0.122	0.000
7	A	7	SER	0	0.021	0.007	5.490	0.221	0.221	0.000	0.000	0.000	0.000
8	A	8	SER	0	0.057	0.021	8.801	0.000	0.000	0.000	0.000	0.000	0.000
9	A	9	GLU	-1	-0.794	-0.878	12.176	-0.173	-0.173	0.000	0.000	0.000	0.000
10	A	10	ASN	0	0.005	0.005	7.149	0.149	0.149	0.000	0.000	0.000	0.000
11	A	11	LYS	1	0.877	0.940	9.399	0.854	0.854	0.000	0.000	0.000	0.000
12	A	12	GLN	0	0.046	0.016	10.912	0.062	0.062	0.000	0.000	0.000	0.000
13	A	13	LYS	1	0.739	0.850	11.483	0.278	0.278	0.000	0.000	0.000	0.000
14	A	14	LEU	0	0.027	0.004	8.625	0.061	0.061	0.000	0.000	0.000	0.000
15	A	15	GLN	0	0.010	-0.002	12.097	0.026	0.026	0.000	0.000	0.000	0.000
16	A	16	LYS	1	0.950	0.977	15.363	0.217	0.217	0.000	0.000	0.000	0.000
17	A	17	GLN	0	-0.001	0.014	12.489	0.056	0.056	0.000	0.000	0.000	0.000
18	A	18	VAL	0	0.025	0.013	14.190	0.035	0.035	0.000	0.000	0.000	0.000
19	A	19	GLU	-1	-0.768	-0.846	16.851	-0.148	-0.148	0.000	0.000	0.000	0.000
20	A	20	PHE	0	-0.019	-0.010	18.715	0.025	0.025	0.000	0.000	0.000	0.000
21	A	21	TYR	0	0.012	0.013	15.857	0.022	0.022	0.000	0.000	0.000	0.000
22	A	22	PHE	0	0.072	0.030	19.080	0.013	0.013	0.000	0.000	0.000	0.000
23	A	23	SER	0	-0.026	-0.004	23.177	0.008	0.008	0.000	0.000	0.000	0.000
24	A	24	ASP	-1	-0.746	-0.856	25.238	-0.059	-0.059	0.000	0.000	0.000	0.000
25	A	25	VAL	0	-0.014	0.002	27.333	0.007	0.007	0.000	0.000	0.000	0.000
26	A	26	ASN	0	-0.050	-0.029	23.164	0.018	0.018	0.000	0.000	0.000	0.000
27	A	27	VAL	0	0.056	0.039	25.707	0.008	0.008	0.000	0.000	0.000	0.000
28	A	28	GLN	0	0.008	-0.010	26.783	0.006	0.006	0.000	0.000	0.000	0.000
29	A	29	ARG	1	0.842	0.929	27.670	0.016	0.016	0.000	0.000	0.000	0.000
30	A	30	ASP	-1	-0.824	-0.922	22.978	-0.012	-0.012	0.000	0.000	0.000	0.000
31	A	31	ILE	0	0.008	-0.008	26.612	-0.006	-0.006	0.000	0.000	0.000	0.000
32	A	32	PHE	0	0.004	0.021	20.667	-0.002	-0.002	0.000	0.000	0.000	0.000
33	A	33	LEU	0	0.010	0.004	21.152	-0.005	-0.005	0.000	0.000	0.000	0.000
34	A	34	LYS	1	0.826	0.907	24.243	0.012	0.012	0.000	0.000	0.000	0.000
35	A	35	GLY	0	-0.002	0.005	27.855	-0.003	-0.003	0.000	0.000	0.000	0.000
36	A	36	LYS	1	0.807	0.879	22.330	0.038	0.038	0.000	0.000	0.000	0.000
37	A	37	MET	0	-0.071	-0.022	25.291	-0.006	-0.006	0.000	0.000	0.000	0.000
38	A	38	ALA	0	0.004	-0.004	26.933	-0.003	-0.003	0.000	0.000	0.000	0.000
39	A	39	GLU	-1	-0.833	-0.888	25.779	-0.039	-0.039	0.000	0.000	0.000	0.000
40	A	40	ASN	0	-0.041	-0.033	26.342	-0.006	-0.006	0.000	0.000	0.000	0.000
41	A	41	ALA	0	0.020	0.002	30.420	0.000	0.000	0.000	0.000	0.000	0.000
42	A	42	GLU	-1	-0.845	-0.902	28.606	-0.105	-0.105	0.000	0.000	0.000	0.000
43	A	43	GLY	0	-0.020	-0.001	27.813	-0.005	-0.005	0.000	0.000	0.000	0.000
44	A	44	PHE	0	-0.051	-0.039	22.896	-0.007	-0.007	0.000	0.000	0.000	0.000
45	A	45	VAL	0	-0.006	-0.004	19.774	0.014	0.014	0.000	0.000	0.000	0.000
46	A	46	SER	0	0.033	-0.008	18.826	-0.020	-0.020	0.000	0.000	0.000	0.000
47	A	47	LEU	0	0.013	-0.019	13.915	0.007	0.007	0.000	0.000	0.000	0.000
48	A	48	GLU	-1	-0.869	-0.914	13.929	-0.112	-0.112	0.000	0.000	0.000	0.000
49	A	49	THR	0	-0.009	0.002	14.903	0.043	0.043	0.000	0.000	0.000	0.000
50	A	50	LEU	0	-0.016	0.006	14.609	0.026	0.026	0.000	0.000	0.000	0.000
51	A	51	LEU	0	-0.026	-0.012	8.817	0.001	0.001	0.000	0.000	0.000	0.000
52	A	52	THR	0	-0.055	-0.032	11.706	0.070	0.070	0.000	0.000	0.000	0.000
53	A	53	PHE	0	-0.001	0.008	14.320	0.037	0.037	0.000	0.000	0.000	0.000
54	A	54	LYS	1	0.996	0.984	13.060	-0.174	-0.174	0.000	0.000	0.000	0.000
55	A	55	ARG	1	0.841	0.913	12.051	0.063	0.063	0.000	0.000	0.000	0.000
56	A	56	VAL	0	0.020	0.025	10.007	-0.057	-0.057	0.000	0.000	0.000	0.000
57	A	57	ASN	0	0.068	0.034	8.457	-0.098	-0.098	0.000	0.000	0.000	0.000
58	A	58	SER	0	-0.093	-0.043	7.708	0.161	0.161	0.000	0.000	0.000	0.000
59	A	59	VAL	0	-0.097	-0.043	5.807	0.089	0.089	0.000	0.000	0.000	0.000
60	A	60	THR	0	-0.008	-0.046	3.794	-0.933	-0.638	0.001	-0.061	-0.234	0.000
61	A	61	THR	0	0.011	0.002	4.646	0.552	0.594	-0.001	-0.003	-0.037	0.000
62	A	62	ASP	-1	-0.778	-0.856	6.133	-0.664	-0.664	0.000	0.000	0.000	0.000
63	A	63	VAL	0	0.067	0.021	7.767	-0.117	-0.117	0.000	0.000	0.000	0.000
64	A	64	LYS	1	0.864	0.912	10.159	0.694	0.694	0.000	0.000	0.000	0.000
65	A	65	GLU	-1	-0.841	-0.902	4.409	-4.022	-3.881	-0.001	-0.030	-0.110	0.000
66	A	66	VAL	0	-0.009	-0.004	8.757	0.105	0.105	0.000	0.000	0.000	0.000
67	A	67	VAL	0	0.026	0.018	11.122	0.069	0.069	0.000	0.000	0.000	0.000
68	A	68	GLU	-1	-0.854	-0.898	10.502	-0.560	-0.560	0.000	0.000	0.000	0.000
69	A	69	ALA	0	-0.041	-0.021	10.741	0.042	0.042	0.000	0.000	0.000	0.000
70	A	70	ILE	0	0.010	0.000	12.638	0.071	0.071	0.000	0.000	0.000	0.000
71	A	71	ARG	1	0.867	0.915	15.083	0.477	0.477	0.000	0.000	0.000	0.000
72	A	72	PRO	0	-0.057	-0.033	16.012	0.028	0.028	0.000	0.000	0.000	0.000
73	A	73	SER	0	-0.057	-0.045	19.009	0.030	0.030	0.000	0.000	0.000	0.000
74	A	74	GLU	-1	-0.831	-0.912	20.785	-0.149	-0.149	0.000	0.000	0.000	0.000
75	A	75	LYS	1	0.790	0.873	22.405	0.161	0.161	0.000	0.000	0.000	0.000
76	A	76	LEU	0	-0.038	-0.019	18.854	0.009	0.009	0.000	0.000	0.000	0.000
77	A	77	VAL	0	0.001	0.004	22.804	-0.003	-0.003	0.000	0.000	0.000	0.000
78	A	78	LEU	0	-0.011	-0.009	17.162	0.001	0.001	0.000	0.000	0.000	0.000
79	A	79	SER	0	-0.011	-0.030	21.335	0.010	0.010	0.000	0.000	0.000	0.000
80	A	80	GLU	-1	-0.916	-0.960	22.192	-0.174	-0.174	0.000	0.000	0.000	0.000
81	A	81	ASP	-1	-0.839	-0.890	21.878	-0.186	-0.186	0.000	0.000	0.000	0.000
82	A	82	GLY	0	-0.050	-0.022	18.389	-0.025	-0.025	0.000	0.000	0.000	0.000
83	A	83	LEU	0	-0.026	-0.017	17.139	-0.036	-0.036	0.000	0.000	0.000	0.000
84	A	84	MET	0	-0.042	-0.020	18.238	0.014	0.014	0.000	0.000	0.000	0.000
85	A	85	VAL	0	-0.030	-0.008	18.119	-0.020	-0.020	0.000	0.000	0.000	0.000
86	A	86	ARG	1	0.870	0.949	20.618	0.131	0.131	0.000	0.000	0.000	0.000
87	A	87	ARG	1	0.777	0.829	23.401	0.064	0.064	0.000	0.000	0.000	0.000
88	A	88	ARG	1	0.896	0.966	25.508	0.108	0.108	0.000	0.000	0.000	0.000
89	A	89	ASP	-1	-0.900	-0.945	27.416	-0.088	-0.088	0.000	0.000	0.000	0.000
90	A	90	PRO	0	0.038	0.007	29.772	-0.001	-0.001	0.000	0.000	0.000	0.000
91	A	91	LEU	0	0.009	0.012	28.703	-0.001	-0.001	0.000	0.000	0.000	0.000
92	A	92	PRO	0	-0.040	-0.002	31.343	0.004	0.004	0.000	0.000	0.000	0.000

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