FMO DATABASE

FMODB ID: 8539Y

Calculation Name: 1N12-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1N12

Chain ID: A

ChEMBL ID:

UniProt ID: P08407

Base Structure: X-ray

Registration Date: 2023-09-20

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	137
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1100107.173045
FMO2-HF: Nuclear repulsion	1048021.921968
FMO2-HF: Total energy	-52085.251077
FMO2-MP2: Total energy	-52235.39118

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:VAL)

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

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.
-5.956	-0.098	6.826	-3.841	-8.845	-0.021

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.014 / q_NPA : 0.013

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	14	ALA	0	0.009	0.001	3.440	-2.428	0.279	0.020	-1.384	-1.343	0.004
4	A	15	CYS	0	-0.072	-0.049	5.150	0.218	0.286	-0.002	-0.004	-0.062	0.000
5	A	16	THR	0	-0.017	-0.008	7.858	0.036	0.036	0.000	0.000	0.000	0.000
6	A	17	VAL	0	-0.017	-0.020	11.323	0.090	0.090	0.000	0.000	0.000	0.000
7	A	18	SER	0	-0.022	0.001	13.609	0.043	0.043	0.000	0.000	0.000	0.000
8	A	19	ASN	0	-0.020	-0.015	17.282	-0.012	-0.012	0.000	0.000	0.000	0.000
9	A	20	THR	0	0.009	0.001	19.937	0.026	0.026	0.000	0.000	0.000	0.000
10	A	21	THR	0	-0.021	-0.016	22.252	-0.001	-0.001	0.000	0.000	0.000	0.000
11	A	22	VAL	0	-0.015	0.012	24.277	0.006	0.006	0.000	0.000	0.000	0.000
12	A	23	ASP	-1	-0.798	-0.894	26.978	-0.140	-0.140	0.000	0.000	0.000	0.000
13	A	24	TRP	0	-0.032	-0.046	27.619	-0.002	-0.002	0.000	0.000	0.000	0.000
14	A	25	GLN	0	-0.079	-0.036	33.342	0.014	0.014	0.000	0.000	0.000	0.000
15	A	26	ASP	-1	-0.903	-0.939	36.314	-0.098	-0.098	0.000	0.000	0.000	0.000
16	A	27	VAL	0	-0.038	-0.029	35.677	-0.001	-0.001	0.000	0.000	0.000	0.000
17	A	28	GLU	-1	-0.926	-0.953	39.135	-0.076	-0.076	0.000	0.000	0.000	0.000
18	A	29	ILE	0	0.068	0.026	41.114	-0.001	-0.001	0.000	0.000	0.000	0.000
19	A	30	GLN	0	-0.007	-0.009	42.291	0.000	0.000	0.000	0.000	0.000	0.000
20	A	31	THR	0	-0.026	-0.022	41.331	0.001	0.001	0.000	0.000	0.000	0.000
21	A	32	LEU	0	-0.018	0.010	36.671	-0.003	-0.003	0.000	0.000	0.000	0.000
22	A	33	SER	0	0.002	0.001	37.220	0.005	0.005	0.000	0.000	0.000	0.000
23	A	34	GLN	0	-0.038	-0.031	36.906	-0.002	-0.002	0.000	0.000	0.000	0.000
24	A	35	ASN	0	-0.030	-0.038	35.035	-0.005	-0.005	0.000	0.000	0.000	0.000
25	A	36	GLY	0	0.036	0.008	32.834	-0.007	-0.007	0.000	0.000	0.000	0.000
26	A	37	ASN	0	-0.067	-0.046	33.890	0.000	0.000	0.000	0.000	0.000	0.000
27	A	38	HIS	0	0.022	0.010	33.323	-0.011	-0.011	0.000	0.000	0.000	0.000
28	A	39	GLU	-1	-0.834	-0.936	29.639	-0.144	-0.144	0.000	0.000	0.000	0.000
29	A	40	LYS	1	0.885	0.956	28.673	0.160	0.160	0.000	0.000	0.000	0.000
30	A	41	GLU	-1	-0.837	-0.920	25.273	-0.182	-0.182	0.000	0.000	0.000	0.000
31	A	42	PHE	0	-0.049	-0.027	20.516	0.002	0.002	0.000	0.000	0.000	0.000
32	A	43	THR	0	0.019	0.001	20.720	-0.011	-0.011	0.000	0.000	0.000	0.000
33	A	44	VAL	0	0.008	0.007	15.872	-0.004	-0.004	0.000	0.000	0.000	0.000
34	A	45	ASN	0	0.039	0.036	16.671	-0.001	-0.001	0.000	0.000	0.000	0.000
35	A	46	MET	0	0.010	-0.012	11.395	-0.080	-0.080	0.000	0.000	0.000	0.000
36	A	47	ARG	1	0.878	0.942	11.604	0.346	0.346	0.000	0.000	0.000	0.000
37	A	49	PRO	0	0.034	0.003	6.924	0.117	0.117	0.000	0.000	0.000	0.000
38	A	50	TYR	0	0.020	0.020	2.555	-2.372	-0.473	4.721	-1.379	-5.241	-0.012
39	A	51	ASN	0	-0.036	-0.037	5.006	-0.396	-0.364	-0.001	-0.003	-0.028	0.000
40	A	52	LEU	0	0.041	0.039	5.526	0.111	0.111	0.000	0.000	0.000	0.000
41	A	53	GLY	0	0.007	0.007	5.463	-0.226	-0.226	0.000	0.000	0.000	0.000
42	A	54	THR	0	-0.011	-0.032	7.374	0.046	0.046	0.000	0.000	0.000	0.000
43	A	55	MET	0	0.023	0.022	7.168	-0.147	-0.147	0.000	0.000	0.000	0.000
44	A	56	LYS	1	0.897	0.966	7.826	0.629	0.629	0.000	0.000	0.000	0.000
45	A	57	VAL	0	0.027	0.001	8.801	-0.208	-0.208	0.000	0.000	0.000	0.000
46	A	58	THR	0	0.000	0.005	11.425	0.096	0.096	0.000	0.000	0.000	0.000
47	A	59	ILE	0	0.017	0.009	13.376	-0.043	-0.043	0.000	0.000	0.000	0.000
48	A	60	THR	0	0.020	0.010	16.564	0.039	0.039	0.000	0.000	0.000	0.000
49	A	61	ALA	0	0.050	0.017	18.765	-0.005	-0.005	0.000	0.000	0.000	0.000
50	A	62	THR	0	-0.004	0.000	22.175	0.004	0.004	0.000	0.000	0.000	0.000
51	A	63	ASN	0	0.014	0.023	24.700	0.021	0.021	0.000	0.000	0.000	0.000
52	A	64	THR	0	-0.026	-0.012	24.093	-0.004	-0.004	0.000	0.000	0.000	0.000
53	A	65	TYR	0	0.044	0.009	27.559	0.013	0.013	0.000	0.000	0.000	0.000
54	A	66	ASN	0	-0.019	-0.010	28.968	-0.005	-0.005	0.000	0.000	0.000	0.000
55	A	67	ASN	0	-0.008	-0.008	23.526	-0.014	-0.014	0.000	0.000	0.000	0.000
56	A	68	ALA	0	0.028	0.044	25.338	-0.011	-0.011	0.000	0.000	0.000	0.000
57	A	69	ILE	0	0.002	-0.014	23.160	-0.003	-0.003	0.000	0.000	0.000	0.000
58	A	70	LEU	0	-0.028	-0.014	26.894	0.011	0.011	0.000	0.000	0.000	0.000
59	A	71	VAL	0	-0.029	-0.016	30.177	-0.008	-0.008	0.000	0.000	0.000	0.000
60	A	72	GLN	0	0.022	0.007	31.175	0.007	0.007	0.000	0.000	0.000	0.000
61	A	73	ASN	0	-0.033	-0.026	33.683	0.003	0.003	0.000	0.000	0.000	0.000
62	A	74	THR	0	0.082	0.046	35.339	0.004	0.004	0.000	0.000	0.000	0.000
63	A	75	SER	0	0.031	0.017	38.027	0.005	0.005	0.000	0.000	0.000	0.000
64	A	76	ASN	0	-0.021	-0.010	40.499	-0.002	-0.002	0.000	0.000	0.000	0.000
65	A	77	THR	0	-0.054	-0.026	40.938	0.003	0.003	0.000	0.000	0.000	0.000
66	A	78	SER	0	0.033	0.007	38.172	-0.003	-0.003	0.000	0.000	0.000	0.000
67	A	79	SER	0	0.011	0.017	36.170	-0.005	-0.005	0.000	0.000	0.000	0.000
68	A	80	ASP	-1	-0.904	-0.933	36.116	-0.098	-0.098	0.000	0.000	0.000	0.000
69	A	81	GLY	0	0.058	0.022	36.131	-0.003	-0.003	0.000	0.000	0.000	0.000
70	A	82	LEU	0	0.010	0.007	33.360	0.000	0.000	0.000	0.000	0.000	0.000
71	A	83	LEU	0	-0.043	-0.015	31.006	-0.007	-0.007	0.000	0.000	0.000	0.000
72	A	84	VAL	0	0.035	0.018	26.655	0.004	0.004	0.000	0.000	0.000	0.000
73	A	85	TYR	0	0.001	0.009	26.696	-0.013	-0.013	0.000	0.000	0.000	0.000
74	A	86	LEU	0	0.016	0.002	20.916	-0.001	-0.001	0.000	0.000	0.000	0.000
75	A	87	TYR	0	0.006	-0.006	23.085	0.010	0.010	0.000	0.000	0.000	0.000
76	A	88	ASN	0	0.044	0.024	17.832	-0.027	-0.027	0.000	0.000	0.000	0.000
77	A	89	SER	0	-0.006	-0.032	20.388	0.023	0.023	0.000	0.000	0.000	0.000
78	A	90	ASN	0	-0.023	-0.019	21.080	-0.012	-0.012	0.000	0.000	0.000	0.000
79	A	91	ALA	0	0.014	-0.003	22.626	0.012	0.012	0.000	0.000	0.000	0.000
80	A	92	GLY	0	-0.019	-0.014	24.232	0.010	0.010	0.000	0.000	0.000	0.000
81	A	93	ASN	0	-0.016	0.022	26.210	0.008	0.008	0.000	0.000	0.000	0.000
82	A	94	ILE	0	0.001	0.020	25.714	-0.011	-0.011	0.000	0.000	0.000	0.000
83	A	95	GLY	0	0.013	-0.003	23.843	0.011	0.011	0.000	0.000	0.000	0.000
84	A	96	THR	0	-0.013	-0.019	21.683	0.005	0.005	0.000	0.000	0.000	0.000
85	A	97	ALA	0	0.014	0.005	22.788	-0.018	-0.018	0.000	0.000	0.000	0.000
86	A	98	ILE	0	-0.044	-0.018	18.523	-0.005	-0.005	0.000	0.000	0.000	0.000
87	A	99	THR	0	0.004	0.020	20.179	0.022	0.022	0.000	0.000	0.000	0.000
88	A	100	LEU	0	-0.011	-0.022	19.097	-0.038	-0.038	0.000	0.000	0.000	0.000
89	A	101	GLY	0	-0.016	-0.017	17.012	0.019	0.019	0.000	0.000	0.000	0.000
90	A	102	THR	0	-0.069	-0.026	15.865	-0.006	-0.006	0.000	0.000	0.000	0.000
91	A	103	PRO	0	-0.011	-0.007	11.516	-0.020	-0.020	0.000	0.000	0.000	0.000
92	A	104	PHE	0	0.021	0.011	13.374	0.073	0.073	0.000	0.000	0.000	0.000
93	A	105	THR	0	-0.002	-0.021	11.480	-0.070	-0.070	0.000	0.000	0.000	0.000
94	A	106	PRO	0	-0.023	-0.020	12.730	0.053	0.053	0.000	0.000	0.000	0.000
95	A	107	GLY	0	0.035	0.020	15.692	0.007	0.007	0.000	0.000	0.000	0.000
96	A	108	LYS	1	0.846	0.934	18.372	0.208	0.208	0.000	0.000	0.000	0.000
97	A	109	ILE	0	-0.019	-0.018	12.513	-0.035	-0.035	0.000	0.000	0.000	0.000
98	A	110	THR	0	0.014	0.008	16.599	0.036	0.036	0.000	0.000	0.000	0.000
99	A	111	GLY	0	0.049	0.024	16.634	-0.034	-0.034	0.000	0.000	0.000	0.000
100	A	112	ASN	0	-0.008	-0.018	15.447	-0.036	-0.036	0.000	0.000	0.000	0.000
101	A	113	ASN	0	-0.003	0.001	14.736	0.017	0.017	0.000	0.000	0.000	0.000
102	A	114	ALA	0	0.044	0.016	11.312	-0.029	-0.029	0.000	0.000	0.000	0.000
103	A	115	ASP	-1	-0.870	-0.902	12.242	-0.374	-0.374	0.000	0.000	0.000	0.000
104	A	116	LYS	1	0.852	0.935	11.037	0.368	0.368	0.000	0.000	0.000	0.000
105	A	117	THR	0	0.019	-0.005	14.484	-0.019	-0.019	0.000	0.000	0.000	0.000
106	A	118	ILE	0	-0.017	-0.003	13.961	0.014	0.014	0.000	0.000	0.000	0.000
107	A	119	SER	0	-0.012	-0.009	17.139	0.020	0.020	0.000	0.000	0.000	0.000
108	A	120	LEU	0	-0.030	0.016	17.393	-0.013	-0.013	0.000	0.000	0.000	0.000
109	A	121	HIS	0	0.022	0.002	21.425	0.009	0.009	0.000	0.000	0.000	0.000
110	A	122	ALA	0	-0.019	-0.007	24.355	-0.014	-0.014	0.000	0.000	0.000	0.000
111	A	123	LYS	1	0.874	0.964	26.623	0.142	0.142	0.000	0.000	0.000	0.000
112	A	124	LEU	0	0.036	0.023	29.774	-0.009	-0.009	0.000	0.000	0.000	0.000
113	A	125	GLY	0	0.057	0.028	32.448	0.008	0.008	0.000	0.000	0.000	0.000
114	A	126	TYR	0	-0.082	-0.024	34.362	-0.003	-0.003	0.000	0.000	0.000	0.000
115	A	127	LYS	1	0.826	0.916	34.647	0.112	0.112	0.000	0.000	0.000	0.000
116	A	128	GLY	0	0.057	0.027	37.004	0.001	0.001	0.000	0.000	0.000	0.000
117	A	129	ASN	0	0.001	-0.013	40.658	0.001	0.001	0.000	0.000	0.000	0.000
118	A	130	MET	0	0.068	0.032	42.256	-0.001	-0.001	0.000	0.000	0.000	0.000
119	A	131	GLN	0	-0.018	-0.022	43.545	0.000	0.000	0.000	0.000	0.000	0.000
120	A	132	ASN	0	-0.010	0.011	43.447	0.004	0.004	0.000	0.000	0.000	0.000
121	A	133	LEU	0	-0.024	0.007	38.875	-0.004	-0.004	0.000	0.000	0.000	0.000
122	A	134	ILE	0	-0.037	-0.014	40.992	0.004	0.004	0.000	0.000	0.000	0.000
123	A	135	ALA	0	-0.008	0.002	40.858	-0.004	-0.004	0.000	0.000	0.000	0.000
124	A	136	GLY	0	0.030	0.011	41.227	0.001	0.001	0.000	0.000	0.000	0.000
125	A	137	PRO	0	-0.017	-0.017	37.262	-0.004	-0.004	0.000	0.000	0.000	0.000
126	A	138	PHE	0	0.020	0.022	31.925	-0.001	-0.001	0.000	0.000	0.000	0.000
127	A	139	SER	0	-0.009	-0.014	30.142	-0.008	-0.008	0.000	0.000	0.000	0.000
128	A	140	ALA	0	0.004	0.001	27.694	0.004	0.004	0.000	0.000	0.000	0.000
129	A	141	THR	0	-0.014	-0.009	23.213	-0.013	-0.013	0.000	0.000	0.000	0.000
130	A	142	ALA	0	0.013	0.005	20.504	0.008	0.008	0.000	0.000	0.000	0.000
131	A	143	THR	0	-0.025	-0.001	15.330	-0.014	-0.014	0.000	0.000	0.000	0.000
132	A	144	LEU	0	0.000	-0.002	12.855	0.005	0.005	0.000	0.000	0.000	0.000
133	A	145	VAL	0	0.005	0.010	9.848	-0.053	-0.053	0.000	0.000	0.000	0.000
134	A	146	ALA	0	0.052	0.006	8.684	0.116	0.116	0.000	0.000	0.000	0.000
135	A	147	SER	0	0.021	0.015	3.190	-0.186	0.052	0.022	-0.069	-0.192	0.000
136	A	148	TYR	0	0.048	0.020	3.747	0.149	0.487	0.003	-0.071	-0.270	0.000
137	A	149	SER	0	-0.012	0.023	2.461	-1.652	-1.076	2.063	-0.931	-1.709	-0.013

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