FMO DATABASE

FMODB ID: PLL99

Calculation Name: 3OXP-A-Xray13

Preferred Name:

Target Type:

Ligand Name: sulfate ion

ligand 3-letter code: SO4

PDB ID: 3OXP

Chain ID: A

ChEMBL ID:

UniProt ID: A0A384

Base Structure: X-ray

Registration Date: 2018-03-01

Reference:

DOI:

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptH
Protonation	MOE:Protonate 3D
Complement	Missing residues were capped by ACE, NME. Missing atoms were corrected by Structure prepareation by MOE.
Water	No
Procedure	Auto-FMO protocol ver. 1.20181228

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	150
LigandCharge	SO4=-2
Software	MIZUHO/ABINIT-MP 3.0

Total energy (hartree)

FMO2-HF: Electronic energy	-1361247.692909
FMO2-HF: Nuclear repulsion	1304993.900343
FMO2-HF: Total energy	-56253.792565
FMO2-MP2: Total energy	-56418.379632

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:ACE)

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

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.
-0.495	1.015	-0.011	-0.776	-0.723	-0.002

Interaction energy analysis for fragmet #1(A:-1:ACE)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.004 / q_NPA : -0.014

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	1	MET	0	0.031	0.040	3.881	0.450	1.826	-0.012	-0.703	-0.661	-0.002
4	A	2	LEU	0	0.049	0.024	6.074	0.280	0.280	0.000	0.000	0.000	0.000
5	A	3	LYS	1	0.886	0.955	7.403	1.246	1.246	0.000	0.000	0.000	0.000
6	A	4	THR	0	-0.100	-0.058	7.253	0.268	0.268	0.000	0.000	0.000	0.000
7	A	5	LEU	0	-0.020	-0.016	9.626	0.157	0.157	0.000	0.000	0.000	0.000
8	A	6	LEU	0	-0.052	-0.002	11.593	0.093	0.093	0.000	0.000	0.000	0.000
9	A	7	THR	0	-0.004	-0.024	13.619	-0.041	-0.041	0.000	0.000	0.000	0.000
10	A	8	SER	0	-0.017	-0.038	15.929	0.031	0.031	0.000	0.000	0.000	0.000
11	A	9	ASP	-1	-0.904	-0.932	18.879	-0.213	-0.213	0.000	0.000	0.000	0.000
12	A	10	VAL	0	-0.009	0.013	16.405	0.024	0.024	0.000	0.000	0.000	0.000
13	A	11	ILE	0	-0.043	-0.009	16.955	-0.001	-0.001	0.000	0.000	0.000	0.000
14	A	12	GLN	0	-0.050	-0.036	19.851	0.018	0.018	0.000	0.000	0.000	0.000
15	A	13	VAL	0	-0.029	-0.013	22.998	-0.004	-0.004	0.000	0.000	0.000	0.000
16	A	14	VAL	0	0.016	0.017	25.415	0.004	0.004	0.000	0.000	0.000	0.000
17	A	15	SER	0	-0.027	-0.013	28.733	-0.002	-0.002	0.000	0.000	0.000	0.000
18	A	16	GLN	0	0.010	-0.005	31.470	0.004	0.004	0.000	0.000	0.000	0.000
19	A	17	ALA	0	0.033	0.017	30.666	-0.004	-0.004	0.000	0.000	0.000	0.000
20	A	18	LYS	1	0.896	0.952	32.760	0.035	0.035	0.000	0.000	0.000	0.000
21	A	19	ASP	-1	-0.864	-0.955	34.041	-0.032	-0.032	0.000	0.000	0.000	0.000
22	A	20	TRP	0	0.010	-0.012	30.205	-0.006	-0.006	0.000	0.000	0.000	0.000
23	A	21	ARG	1	0.801	0.886	30.168	0.018	0.018	0.000	0.000	0.000	0.000
24	A	22	ASP	-1	-0.837	-0.900	31.002	-0.055	-0.055	0.000	0.000	0.000	0.000
25	A	23	ALA	0	0.008	0.005	27.800	-0.006	-0.006	0.000	0.000	0.000	0.000
26	A	24	ILE	0	-0.018	-0.007	25.580	-0.009	-0.009	0.000	0.000	0.000	0.000
27	A	25	ALA	0	0.016	0.008	26.421	-0.004	-0.004	0.000	0.000	0.000	0.000
28	A	26	ILE	0	0.004	-0.004	26.356	-0.006	-0.006	0.000	0.000	0.000	0.000
29	A	27	SER	0	-0.038	-0.026	22.795	-0.012	-0.012	0.000	0.000	0.000	0.000
30	A	28	CYS	0	-0.027	-0.002	22.410	-0.009	-0.009	0.000	0.000	0.000	0.000
31	A	29	GLN	0	-0.047	-0.022	24.046	0.002	0.002	0.000	0.000	0.000	0.000
32	A	30	PRO	0	0.028	0.021	21.609	0.001	0.001	0.000	0.000	0.000	0.000
33	A	31	LEU	0	-0.029	-0.023	18.432	-0.003	-0.003	0.000	0.000	0.000	0.000
34	A	32	ILE	0	-0.036	0.001	22.312	0.009	0.009	0.000	0.000	0.000	0.000
35	A	33	ASP	-1	-0.880	-0.922	25.610	-0.077	-0.077	0.000	0.000	0.000	0.000
36	A	34	ASN	0	-0.038	-0.021	19.960	0.015	0.015	0.000	0.000	0.000	0.000
37	A	35	GLY	0	0.020	0.015	23.406	0.000	0.000	0.000	0.000	0.000	0.000
38	A	36	ALA	0	-0.047	-0.016	19.610	0.009	0.009	0.000	0.000	0.000	0.000
39	A	37	VAL	0	0.005	-0.003	21.376	0.012	0.012	0.000	0.000	0.000	0.000
40	A	38	GLU	-1	-0.881	-0.935	23.816	-0.030	-0.030	0.000	0.000	0.000	0.000
41	A	39	ALA	0	0.053	0.016	27.336	-0.001	-0.001	0.000	0.000	0.000	0.000
42	A	40	ARG	1	0.883	0.934	29.322	0.006	0.006	0.000	0.000	0.000	0.000
43	A	41	TYR	0	-0.009	-0.015	20.416	0.008	0.008	0.000	0.000	0.000	0.000
44	A	42	VAL	0	0.033	0.007	27.084	0.002	0.002	0.000	0.000	0.000	0.000
45	A	43	GLU	-1	-0.905	-0.962	28.348	-0.021	-0.021	0.000	0.000	0.000	0.000
46	A	44	ALA	0	-0.041	-0.016	27.875	0.003	0.003	0.000	0.000	0.000	0.000
47	A	45	ILE	0	-0.018	-0.008	23.957	0.003	0.003	0.000	0.000	0.000	0.000
48	A	46	TYR	0	-0.009	-0.017	27.956	0.002	0.002	0.000	0.000	0.000	0.000
49	A	47	ARG	1	0.958	0.980	31.427	0.004	0.004	0.000	0.000	0.000	0.000
50	A	48	SER	0	-0.039	-0.016	28.657	0.005	0.005	0.000	0.000	0.000	0.000
51	A	49	HIS	0	0.058	0.059	29.886	0.002	0.002	0.000	0.000	0.000	0.000
52	A	50	GLU	-1	-0.881	-0.937	31.303	-0.011	-0.011	0.000	0.000	0.000	0.000
53	A	51	ALA	0	-0.098	-0.035	33.247	0.002	0.002	0.000	0.000	0.000	0.000
54	A	52	ILE	0	-0.077	-0.045	28.932	0.002	0.002	0.000	0.000	0.000	0.000
55	A	53	GLY	0	0.029	0.034	32.232	0.001	0.001	0.000	0.000	0.000	0.000
56	A	54	PRO	0	-0.005	0.001	28.406	0.002	0.002	0.000	0.000	0.000	0.000
57	A	55	TYR	0	-0.023	-0.027	23.672	-0.003	-0.003	0.000	0.000	0.000	0.000
58	A	56	TYR	0	-0.040	-0.038	22.612	0.001	0.001	0.000	0.000	0.000	0.000
59	A	57	VAL	0	-0.022	-0.018	22.428	-0.010	-0.010	0.000	0.000	0.000	0.000
60	A	58	VAL	0	-0.044	-0.014	18.633	0.008	0.008	0.000	0.000	0.000	0.000
61	A	59	GLY	0	0.007	-0.006	21.936	0.009	0.009	0.000	0.000	0.000	0.000
62	A	60	PRO	0	-0.021	-0.012	23.789	-0.006	-0.006	0.000	0.000	0.000	0.000
63	A	61	GLY	0	0.008	0.024	24.088	-0.007	-0.007	0.000	0.000	0.000	0.000
64	A	62	ILE	0	-0.024	-0.009	18.836	-0.012	-0.012	0.000	0.000	0.000	0.000
65	A	63	ALA	0	0.026	0.017	21.695	0.013	0.013	0.000	0.000	0.000	0.000
66	A	64	MET	0	0.011	0.008	16.428	-0.014	-0.014	0.000	0.000	0.000	0.000
67	A	65	PRO	0	0.001	0.009	19.674	0.015	0.015	0.000	0.000	0.000	0.000
68	A	66	HIS	0	-0.061	-0.048	19.505	0.003	0.003	0.000	0.000	0.000	0.000
69	A	67	ALA	0	0.049	0.028	21.581	0.003	0.003	0.000	0.000	0.000	0.000
70	A	68	ARG	1	0.837	0.898	22.065	-0.013	-0.013	0.000	0.000	0.000	0.000
71	A	69	PRO	0	0.053	0.022	20.763	-0.008	-0.008	0.000	0.000	0.000	0.000
72	A	70	GLU	-1	-0.957	-0.980	23.085	0.017	0.017	0.000	0.000	0.000	0.000
73	A	71	ASP	-1	-0.793	-0.879	25.912	0.005	0.005	0.000	0.000	0.000	0.000
74	A	72	GLY	0	-0.032	-0.022	26.225	-0.005	-0.005	0.000	0.000	0.000	0.000
75	A	73	VAL	0	-0.029	0.007	19.473	-0.008	-0.008	0.000	0.000	0.000	0.000
76	A	74	ASN	0	-0.073	-0.045	22.408	0.016	0.016	0.000	0.000	0.000	0.000
77	A	75	ARG	1	0.835	0.901	17.498	0.099	0.099	0.000	0.000	0.000	0.000
78	A	76	LEU	0	-0.011	-0.002	10.945	-0.008	-0.008	0.000	0.000	0.000	0.000
79	A	77	SER	0	-0.049	-0.032	15.050	-0.027	-0.027	0.000	0.000	0.000	0.000
80	A	78	LEU	0	0.025	0.007	10.804	0.013	0.013	0.000	0.000	0.000	0.000
81	A	79	ALA	0	0.053	0.034	15.246	-0.016	-0.016	0.000	0.000	0.000	0.000
82	A	80	LEU	0	-0.023	0.002	15.279	0.008	0.008	0.000	0.000	0.000	0.000
83	A	81	THR	0	0.014	0.004	18.298	-0.002	-0.002	0.000	0.000	0.000	0.000
84	A	82	VAL	0	-0.010	-0.007	21.112	0.004	0.004	0.000	0.000	0.000	0.000
85	A	83	ILE	0	0.019	0.019	23.549	0.002	0.002	0.000	0.000	0.000	0.000
86	A	84	THR	0	-0.064	-0.055	27.047	0.007	0.007	0.000	0.000	0.000	0.000
87	A	85	GLU	-1	-0.955	-0.988	28.732	-0.055	-0.055	0.000	0.000	0.000	0.000
88	A	86	GLY	0	-0.063	-0.013	29.137	0.005	0.005	0.000	0.000	0.000	0.000
89	A	87	VAL	0	-0.021	-0.002	29.569	0.003	0.003	0.000	0.000	0.000	0.000
90	A	88	THR	0	-0.042	-0.012	30.399	0.001	0.001	0.000	0.000	0.000	0.000
91	A	89	PHE	0	0.009	-0.032	27.366	-0.001	-0.001	0.000	0.000	0.000	0.000
92	A	90	ASN	0	-0.021	-0.005	31.187	0.003	0.003	0.000	0.000	0.000	0.000
93	A	91	ALA	0	-0.003	-0.002	28.916	0.004	0.004	0.000	0.000	0.000	0.000
94	A	92	GLU	-1	-0.910	-0.956	30.657	-0.002	-0.002	0.000	0.000	0.000	0.000
95	A	93	GLY	0	-0.048	-0.035	32.138	-0.003	-0.003	0.000	0.000	0.000	0.000
96	A	94	ASN	0	-0.010	-0.009	26.891	-0.003	-0.003	0.000	0.000	0.000	0.000
97	A	95	ASP	-1	-0.762	-0.840	28.004	-0.036	-0.036	0.000	0.000	0.000	0.000
98	A	96	PRO	0	-0.042	-0.048	30.217	0.002	0.002	0.000	0.000	0.000	0.000
99	A	97	VAL	0	0.018	0.016	24.642	-0.003	-0.003	0.000	0.000	0.000	0.000
100	A	98	LYS	1	0.875	0.932	25.087	0.083	0.083	0.000	0.000	0.000	0.000
101	A	99	LEU	0	-0.031	-0.004	17.599	-0.010	-0.010	0.000	0.000	0.000	0.000
102	A	100	LEU	0	0.000	0.008	21.142	0.013	0.013	0.000	0.000	0.000	0.000
103	A	101	ILE	0	-0.010	-0.014	14.282	-0.021	-0.021	0.000	0.000	0.000	0.000
104	A	102	VAL	0	-0.007	0.007	17.823	0.022	0.022	0.000	0.000	0.000	0.000
105	A	103	LEU	0	0.024	0.015	13.718	-0.024	-0.024	0.000	0.000	0.000	0.000
106	A	104	ALA	0	0.028	0.030	16.522	0.017	0.017	0.000	0.000	0.000	0.000
107	A	105	ALA	0	0.046	0.012	15.480	-0.009	-0.009	0.000	0.000	0.000	0.000
108	A	106	THR	0	0.029	0.009	17.233	-0.001	-0.001	0.000	0.000	0.000	0.000
109	A	107	ASP	-1	-0.889	-0.928	16.306	0.140	0.140	0.000	0.000	0.000	0.000
110	A	108	SER	0	0.027	-0.011	16.977	-0.001	-0.001	0.000	0.000	0.000	0.000
111	A	109	ASN	0	-0.052	-0.011	12.440	0.032	0.032	0.000	0.000	0.000	0.000
112	A	110	SER	0	0.062	0.007	11.957	0.041	0.041	0.000	0.000	0.000	0.000
113	A	111	HIS	0	0.019	0.017	11.917	-0.007	-0.007	0.000	0.000	0.000	0.000
114	A	112	ILE	0	-0.022	-0.018	11.542	-0.011	-0.011	0.000	0.000	0.000	0.000
115	A	113	GLU	-1	-0.941	-0.956	6.058	0.856	0.856	0.000	0.000	0.000	0.000
116	A	114	ALA	0	0.054	0.020	8.051	0.010	0.010	0.000	0.000	0.000	0.000
117	A	115	ILE	0	-0.024	-0.011	9.895	-0.056	-0.056	0.000	0.000	0.000	0.000
118	A	116	SER	0	-0.083	-0.051	7.733	0.055	0.055	0.000	0.000	0.000	0.000
119	A	117	GLN	0	0.012	0.004	4.091	-0.680	-0.546	0.001	-0.073	-0.062	0.000
120	A	118	LEU	0	0.011	-0.004	7.337	-0.105	-0.105	0.000	0.000	0.000	0.000
121	A	119	ALA	0	-0.025	-0.008	10.841	-0.020	-0.020	0.000	0.000	0.000	0.000
122	A	120	GLN	0	-0.001	-0.002	5.865	0.191	0.191	0.000	0.000	0.000	0.000
123	A	121	LEU	0	-0.005	0.015	10.218	-0.026	-0.026	0.000	0.000	0.000	0.000
124	A	122	PHE	0	-0.025	-0.038	11.682	0.005	0.005	0.000	0.000	0.000	0.000
125	A	123	ASP	-1	-0.967	-0.970	13.585	0.044	0.044	0.000	0.000	0.000	0.000
126	A	124	THR	0	-0.018	0.005	12.522	0.012	0.012	0.000	0.000	0.000	0.000
127	A	125	ALA	0	0.020	-0.002	15.128	-0.024	-0.024	0.000	0.000	0.000	0.000
128	A	126	SER	0	-0.028	-0.026	16.652	0.002	0.002	0.000	0.000	0.000	0.000
129	A	127	ASP	-1	-0.799	-0.885	13.204	-0.306	-0.306	0.000	0.000	0.000	0.000
130	A	128	VAL	0	0.038	0.026	16.315	-0.009	-0.009	0.000	0.000	0.000	0.000
131	A	129	GLN	0	-0.029	-0.020	18.119	0.007	0.007	0.000	0.000	0.000	0.000
132	A	130	ALA	0	-0.042	-0.028	18.281	0.004	0.004	0.000	0.000	0.000	0.000
133	A	131	LEU	0	0.032	0.014	15.179	0.000	0.000	0.000	0.000	0.000	0.000
134	A	132	LEU	0	0.019	0.019	19.668	0.010	0.010	0.000	0.000	0.000	0.000
135	A	133	ASN	0	-0.095	-0.050	22.894	0.019	0.019	0.000	0.000	0.000	0.000
136	A	134	ALA	0	-0.014	0.002	21.308	0.003	0.003	0.000	0.000	0.000	0.000
137	A	135	LYS	1	0.881	0.932	23.403	0.111	0.111	0.000	0.000	0.000	0.000
138	A	136	THR	0	-0.003	0.007	24.426	0.001	0.001	0.000	0.000	0.000	0.000
139	A	137	PRO	0	0.096	0.026	21.556	-0.011	-0.011	0.000	0.000	0.000	0.000
140	A	138	GLN	0	-0.009	-0.004	20.058	-0.025	-0.025	0.000	0.000	0.000	0.000
141	A	139	ASP	-1	-0.819	-0.909	19.738	-0.188	-0.188	0.000	0.000	0.000	0.000
142	A	140	ILE	0	0.009	-0.001	16.601	-0.019	-0.019	0.000	0.000	0.000	0.000
143	A	141	LEU	0	0.017	0.004	15.245	-0.037	-0.037	0.000	0.000	0.000	0.000
144	A	142	SER	0	-0.044	-0.014	14.759	-0.064	-0.064	0.000	0.000	0.000	0.000
145	A	143	VAL	0	-0.054	-0.025	13.620	-0.027	-0.027	0.000	0.000	0.000	0.000
146	A	144	ILE	0	0.045	0.030	10.638	-0.060	-0.060	0.000	0.000	0.000	0.000
147	A	145	ALA	0	-0.068	-0.038	10.069	-0.195	-0.195	0.000	0.000	0.000	0.000
148	A	146	ARG	1	0.844	0.918	9.929	0.248	0.248	0.000	0.000	0.000	0.000
149	A	147	TYR	-1	-0.877	-0.952	6.007	-2.620	-2.620	0.000	0.000	0.000	0.000
150	A	148	SO4	-2	-1.781	-1.871	36.724	-0.035	-0.035	0.000	0.000	0.000	0.000

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