FMO DATABASE

FMODB ID: Y1912

Calculation Name: 3ST9-F-Xray547

Preferred Name:

Target Type:

Ligand Name: sulfate ion | glycerol | calcium ion

Ligand 3-letter code: SO4 | GOL | CA

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 3ST9

Chain ID: F

ChEMBL ID:

UniProt ID: P63786

Base Structure: X-ray

Registration Date: 2025-10-04

Reference: Sci Data 11, 1164 (2024).

DOI: https://doi.org/10.1038/s41597-024-03999-2

Apendix: None

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptAll
Protonation	MOE:Protonate 3D
Complement	MOE:Homology Modeling
Water	No
Procedure	Manual calculation
Remarks	ac.sh, 23 2024 Oct; Missing atoms/residues were imported from a 100% homology model, which was constructed by MOE.

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	176
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1799620.338253
FMO2-HF: Nuclear repulsion	1731566.926217
FMO2-HF: Total energy	-68053.412036
FMO2-MP2: Total energy	-68251.155509

3D Structure Molmil

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:19:ASP)

Summations of interaction energy for fragment #1(A:19:ASP)

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.
-18.669	-14.628	4.611	-3.982	-4.669	-0.039

Interaction energy analysis for fragmet #1(A:19:ASP)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.055 / q_NPA : -0.045

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	21	TYR	0	0.062	0.026	3.451	-5.495	-3.439	0.021	-0.862	-1.215	0.001
4	A	22	SER	0	0.026	0.020	2.010	-15.719	-14.136	4.590	-3.031	-3.142	-0.040
5	A	23	ARG	1	0.865	0.937	3.848	2.859	3.261	0.000	-0.089	-0.312	0.000
6	A	24	LEU	0	0.103	0.046	6.336	0.807	0.807	0.000	0.000	0.000	0.000
7	A	25	LEU	0	0.008	0.022	7.021	0.852	0.852	0.000	0.000	0.000	0.000
8	A	26	LYS	1	0.874	0.924	8.328	2.687	2.687	0.000	0.000	0.000	0.000
9	A	27	ASP	-1	-0.912	-0.952	10.552	-0.335	-0.335	0.000	0.000	0.000	0.000
10	A	28	ARG	1	0.755	0.852	12.108	2.143	2.143	0.000	0.000	0.000	0.000
11	A	29	ILE	0	-0.002	0.009	10.897	0.239	0.239	0.000	0.000	0.000	0.000
12	A	30	ILE	0	-0.014	-0.007	10.393	-1.087	-1.087	0.000	0.000	0.000	0.000
13	A	31	MET	0	-0.038	-0.012	9.128	0.753	0.753	0.000	0.000	0.000	0.000
14	A	32	LEU	0	0.010	0.005	11.130	-0.611	-0.611	0.000	0.000	0.000	0.000
15	A	33	GLY	0	-0.008	0.000	12.536	0.460	0.460	0.000	0.000	0.000	0.000
16	A	34	SER	0	0.010	-0.001	13.688	0.000	0.000	0.000	0.000	0.000	0.000
17	A	35	GLN	0	0.045	0.027	15.565	-0.009	-0.009	0.000	0.000	0.000	0.000
18	A	36	ILE	0	-0.017	-0.001	17.051	-0.296	-0.296	0.000	0.000	0.000	0.000
19	A	37	ASP	-1	-0.745	-0.865	17.351	-2.249	-2.249	0.000	0.000	0.000	0.000
20	A	38	ASP	-1	-0.773	-0.884	18.552	-1.813	-1.813	0.000	0.000	0.000	0.000
21	A	39	ASN	0	-0.099	-0.039	13.976	-0.510	-0.510	0.000	0.000	0.000	0.000
22	A	40	VAL	0	-0.019	-0.003	13.690	-0.505	-0.505	0.000	0.000	0.000	0.000
23	A	41	ALA	0	0.005	0.004	14.732	-0.290	-0.290	0.000	0.000	0.000	0.000
24	A	42	ASN	0	0.003	-0.009	16.667	-0.036	-0.036	0.000	0.000	0.000	0.000
25	A	43	SER	0	-0.001	0.023	10.186	-0.400	-0.400	0.000	0.000	0.000	0.000
26	A	44	ILE	0	0.007	0.005	12.486	-0.462	-0.462	0.000	0.000	0.000	0.000
27	A	45	VAL	0	0.019	0.008	14.219	0.023	0.023	0.000	0.000	0.000	0.000
28	A	46	SER	0	-0.034	-0.033	12.961	0.170	0.170	0.000	0.000	0.000	0.000
29	A	47	GLN	0	-0.055	-0.039	9.411	-0.602	-0.602	0.000	0.000	0.000	0.000
30	A	48	LEU	0	0.035	0.017	12.531	0.220	0.220	0.000	0.000	0.000	0.000
31	A	49	LEU	0	-0.003	0.001	16.097	0.260	0.260	0.000	0.000	0.000	0.000
32	A	50	PHE	0	-0.034	-0.017	10.946	0.099	0.099	0.000	0.000	0.000	0.000
33	A	51	LEU	0	0.002	0.001	12.048	0.260	0.260	0.000	0.000	0.000	0.000
34	A	52	GLN	0	0.051	0.037	15.215	0.435	0.435	0.000	0.000	0.000	0.000
35	A	53	ALA	0	-0.052	-0.026	16.990	0.213	0.213	0.000	0.000	0.000	0.000
36	A	54	GLN	0	-0.092	-0.029	13.631	0.208	0.208	0.000	0.000	0.000	0.000
37	A	55	ASP	-1	-0.830	-0.908	17.093	-0.907	-0.907	0.000	0.000	0.000	0.000
38	A	56	SER	0	0.006	0.005	19.755	-0.112	-0.112	0.000	0.000	0.000	0.000
39	A	57	GLU	-1	-0.935	-0.960	22.475	-0.717	-0.717	0.000	0.000	0.000	0.000
40	A	58	LYS	1	0.849	0.907	19.227	1.044	1.044	0.000	0.000	0.000	0.000
41	A	59	ASP	-1	-0.763	-0.852	20.271	-1.025	-1.025	0.000	0.000	0.000	0.000
42	A	60	ILE	0	-0.039	-0.012	15.489	-0.196	-0.196	0.000	0.000	0.000	0.000
43	A	61	TYR	0	0.006	0.005	15.394	0.216	0.216	0.000	0.000	0.000	0.000
44	A	62	LEU	0	0.005	0.007	14.854	-0.390	-0.390	0.000	0.000	0.000	0.000
45	A	63	TYR	0	0.037	0.007	13.905	0.407	0.407	0.000	0.000	0.000	0.000
46	A	64	ILE	0	-0.049	-0.028	15.089	-0.363	-0.363	0.000	0.000	0.000	0.000
47	A	65	ASN	0	0.024	0.016	15.873	0.276	0.276	0.000	0.000	0.000	0.000
48	A	66	SER	0	-0.010	-0.022	16.869	-0.113	-0.113	0.000	0.000	0.000	0.000
49	A	67	PRO	0	0.008	-0.002	19.131	0.111	0.111	0.000	0.000	0.000	0.000
50	A	68	GLY	0	0.031	0.029	21.089	0.075	0.075	0.000	0.000	0.000	0.000
51	A	69	GLY	0	-0.008	-0.031	21.440	-0.095	-0.095	0.000	0.000	0.000	0.000
52	A	70	SER	0	0.015	0.027	23.053	0.131	0.131	0.000	0.000	0.000	0.000
53	A	71	VAL	0	0.045	-0.009	24.134	-0.080	-0.080	0.000	0.000	0.000	0.000
54	A	72	THR	0	-0.069	-0.017	25.617	-0.012	-0.012	0.000	0.000	0.000	0.000
55	A	73	ALA	0	0.036	0.027	20.667	-0.057	-0.057	0.000	0.000	0.000	0.000
56	A	74	GLY	0	0.020	-0.002	21.535	-0.123	-0.123	0.000	0.000	0.000	0.000
57	A	75	PHE	0	-0.013	-0.029	23.225	-0.009	-0.009	0.000	0.000	0.000	0.000
58	A	76	ALA	0	0.015	0.021	21.836	-0.003	-0.003	0.000	0.000	0.000	0.000
59	A	77	ILE	0	0.003	0.009	17.915	-0.112	-0.112	0.000	0.000	0.000	0.000
60	A	78	TYR	0	0.012	-0.002	20.830	0.024	0.024	0.000	0.000	0.000	0.000
61	A	79	ASP	-1	-0.868	-0.949	24.091	-1.112	-1.112	0.000	0.000	0.000	0.000
62	A	80	THR	0	-0.064	-0.044	19.273	0.004	0.004	0.000	0.000	0.000	0.000
63	A	81	ILE	0	-0.038	-0.031	19.965	-0.032	-0.032	0.000	0.000	0.000	0.000
64	A	82	GLN	0	-0.067	-0.028	22.560	0.149	0.149	0.000	0.000	0.000	0.000
65	A	83	HIS	0	-0.051	-0.004	23.758	0.129	0.129	0.000	0.000	0.000	0.000
66	A	84	ILE	0	-0.086	-0.039	19.127	-0.003	-0.003	0.000	0.000	0.000	0.000
67	A	85	LYS	1	0.933	0.964	23.228	1.002	1.002	0.000	0.000	0.000	0.000
68	A	86	PRO	0	-0.032	-0.015	19.885	0.075	0.075	0.000	0.000	0.000	0.000
69	A	87	ASP	-1	-0.754	-0.851	22.371	-0.907	-0.907	0.000	0.000	0.000	0.000
70	A	88	VAL	0	-0.036	-0.019	19.006	-0.083	-0.083	0.000	0.000	0.000	0.000
71	A	89	GLN	0	0.009	-0.002	20.145	0.149	0.149	0.000	0.000	0.000	0.000
72	A	90	THR	0	-0.064	-0.035	19.630	-0.186	-0.186	0.000	0.000	0.000	0.000
73	A	91	ILE	0	0.023	0.017	18.114	0.148	0.148	0.000	0.000	0.000	0.000
74	A	92	CYS	0	-0.053	-0.016	18.777	-0.085	-0.085	0.000	0.000	0.000	0.000
75	A	93	ILE	0	-0.002	-0.018	15.529	0.161	0.161	0.000	0.000	0.000	0.000
76	A	94	GLY	0	0.010	0.015	19.111	-0.087	-0.087	0.000	0.000	0.000	0.000
77	A	95	MET	0	0.048	0.020	20.601	0.029	0.029	0.000	0.000	0.000	0.000
78	A	96	ALA	0	0.014	-0.002	20.890	-0.158	-0.158	0.000	0.000	0.000	0.000
79	A	97	ALA	0	0.024	0.013	23.051	0.079	0.079	0.000	0.000	0.000	0.000
80	A	98	SER	0	0.059	0.030	24.356	-0.151	-0.151	0.000	0.000	0.000	0.000
81	A	99	MET	0	-0.058	-0.010	23.320	-0.026	-0.026	0.000	0.000	0.000	0.000
82	A	100	GLY	0	0.039	0.020	21.468	-0.093	-0.093	0.000	0.000	0.000	0.000
83	A	101	SER	0	-0.009	-0.027	22.357	-0.026	-0.026	0.000	0.000	0.000	0.000
84	A	102	PHE	0	-0.031	-0.015	25.550	0.020	0.020	0.000	0.000	0.000	0.000
85	A	103	LEU	0	-0.011	-0.021	20.063	-0.007	-0.007	0.000	0.000	0.000	0.000
86	A	104	LEU	0	-0.019	0.003	22.214	-0.041	-0.041	0.000	0.000	0.000	0.000
87	A	105	ALA	0	0.039	0.034	23.537	0.024	0.024	0.000	0.000	0.000	0.000
88	A	106	ALA	0	-0.012	-0.012	23.942	0.049	0.049	0.000	0.000	0.000	0.000
89	A	107	GLY	0	0.031	0.029	23.761	-0.045	-0.045	0.000	0.000	0.000	0.000
90	A	108	ALA	0	0.006	0.008	24.440	0.085	0.085	0.000	0.000	0.000	0.000
91	A	109	LYS	1	0.841	0.910	26.417	0.617	0.617	0.000	0.000	0.000	0.000
92	A	110	GLY	0	-0.023	-0.009	29.692	0.016	0.016	0.000	0.000	0.000	0.000
93	A	111	LYS	1	0.742	0.839	24.451	0.788	0.788	0.000	0.000	0.000	0.000
94	A	112	ARG	1	0.743	0.876	24.096	0.539	0.539	0.000	0.000	0.000	0.000
95	A	113	PHE	0	0.055	0.023	22.954	0.083	0.083	0.000	0.000	0.000	0.000
96	A	114	ALA	0	0.008	0.001	23.291	-0.093	-0.093	0.000	0.000	0.000	0.000
97	A	115	LEU	0	0.041	0.029	20.111	0.072	0.072	0.000	0.000	0.000	0.000
98	A	116	PRO	0	0.024	-0.003	24.410	-0.034	-0.034	0.000	0.000	0.000	0.000
99	A	117	ASN	0	-0.075	-0.031	25.264	-0.034	-0.034	0.000	0.000	0.000	0.000
100	A	118	ALA	0	-0.020	0.006	23.828	0.001	0.001	0.000	0.000	0.000	0.000
101	A	119	GLU	-1	-0.953	-0.974	24.769	-0.149	-0.149	0.000	0.000	0.000	0.000
102	A	120	VAL	0	0.003	-0.003	25.431	-0.097	-0.097	0.000	0.000	0.000	0.000
103	A	121	MET	0	-0.030	0.000	27.175	0.022	0.022	0.000	0.000	0.000	0.000
104	A	122	ILE	0	0.011	0.016	28.229	-0.082	-0.082	0.000	0.000	0.000	0.000
105	A	123	HIS	0	0.013	0.009	30.735	-0.035	-0.035	0.000	0.000	0.000	0.000
106	A	124	GLN	0	-0.043	-0.039	28.933	-0.107	-0.107	0.000	0.000	0.000	0.000
107	A	125	PRO	0	-0.002	0.010	31.979	-0.040	-0.040	0.000	0.000	0.000	0.000
108	A	126	LEU	0	0.002	0.006	30.405	-0.017	-0.017	0.000	0.000	0.000	0.000
109	A	127	GLY	0	0.050	0.016	29.001	-0.041	-0.041	0.000	0.000	0.000	0.000
110	A	128	GLY	0	-0.058	-0.031	29.185	-0.061	-0.061	0.000	0.000	0.000	0.000
111	A	129	ALA	0	-0.007	-0.014	30.168	-0.016	-0.016	0.000	0.000	0.000	0.000
112	A	130	GLN	0	0.010	0.035	25.537	-0.025	-0.025	0.000	0.000	0.000	0.000
113	A	131	GLY	0	0.005	-0.009	23.554	-0.073	-0.073	0.000	0.000	0.000	0.000
114	A	132	GLN	0	-0.026	-0.013	22.730	-0.050	-0.050	0.000	0.000	0.000	0.000
115	A	133	ALA	0	0.012	0.017	24.822	-0.071	-0.071	0.000	0.000	0.000	0.000
116	A	134	THR	0	-0.014	-0.003	26.515	0.081	0.081	0.000	0.000	0.000	0.000
117	A	135	GLU	-1	-0.809	-0.917	28.389	-0.871	-0.871	0.000	0.000	0.000	0.000
118	A	136	ILE	0	-0.007	-0.011	30.716	0.041	0.041	0.000	0.000	0.000	0.000
119	A	137	GLU	0	-0.052	-0.062	24.678	0.041	0.041	0.000	0.000	0.000	0.000
120	A	138	ILE	0	0.002	0.013	30.194	0.041	0.041	0.000	0.000	0.000	0.000
121	A	139	ALA	0	-0.016	-0.006	32.633	0.043	0.043	0.000	0.000	0.000	0.000
122	A	140	ALA	0	0.008	-0.001	32.109	0.038	0.038	0.000	0.000	0.000	0.000
123	A	141	ASN	0	0.044	0.007	29.530	0.006	0.006	0.000	0.000	0.000	0.000
124	A	142	HIS	0	-0.042	-0.022	33.600	0.029	0.029	0.000	0.000	0.000	0.000
125	A	143	ILE	0	-0.004	-0.004	37.335	0.026	0.026	0.000	0.000	0.000	0.000
126	A	144	LEU	0	-0.028	-0.014	34.084	0.025	0.025	0.000	0.000	0.000	0.000
127	A	145	LYS	1	0.828	0.904	36.522	0.478	0.478	0.000	0.000	0.000	0.000
128	A	146	THR	0	0.046	0.020	31.367	0.037	0.037	0.000	0.000	0.000	0.000
129	A	147	ARG	1	0.956	0.990	33.684	0.577	0.577	0.000	0.000	0.000	0.000
130	A	148	GLU	-1	-0.864	-0.926	34.934	-0.476	-0.476	0.000	0.000	0.000	0.000
131	A	149	LYS	1	0.935	0.968	33.777	0.750	0.750	0.000	0.000	0.000	0.000
132	A	150	LEU	0	0.019	0.024	29.015	0.005	0.005	0.000	0.000	0.000	0.000
133	A	151	ASN	0	0.055	0.011	32.548	-0.011	-0.011	0.000	0.000	0.000	0.000
134	A	152	ARG	1	0.902	0.958	35.563	0.546	0.546	0.000	0.000	0.000	0.000
135	A	153	ILE	0	0.073	0.045	30.052	0.021	0.021	0.000	0.000	0.000	0.000
136	A	154	LEU	0	0.013	0.000	29.822	0.008	0.008	0.000	0.000	0.000	0.000
137	A	155	SER	0	-0.061	-0.010	33.162	0.032	0.032	0.000	0.000	0.000	0.000
138	A	156	GLU	-1	-0.917	-0.975	34.974	-0.591	-0.591	0.000	0.000	0.000	0.000
139	A	157	ARG	1	0.787	0.886	28.087	0.870	0.870	0.000	0.000	0.000	0.000
140	A	158	THR	0	-0.028	-0.022	32.406	0.008	0.008	0.000	0.000	0.000	0.000
141	A	159	GLY	0	-0.012	0.005	34.480	0.029	0.029	0.000	0.000	0.000	0.000
142	A	160	GLN	0	0.012	0.023	37.346	0.060	0.060	0.000	0.000	0.000	0.000
143	A	161	SER	0	-0.009	-0.016	39.138	-0.022	-0.022	0.000	0.000	0.000	0.000
144	A	162	ILE	0	0.058	0.020	39.049	-0.009	-0.009	0.000	0.000	0.000	0.000
145	A	163	GLU	-1	-0.873	-0.920	40.612	-0.351	-0.351	0.000	0.000	0.000	0.000
146	A	164	LYS	1	0.838	0.927	39.581	0.296	0.296	0.000	0.000	0.000	0.000
147	A	165	ILE	0	0.045	0.026	35.526	0.000	0.000	0.000	0.000	0.000	0.000
148	A	166	GLN	0	-0.019	0.008	37.471	0.008	0.008	0.000	0.000	0.000	0.000
149	A	167	LYS	1	0.929	0.966	39.148	0.284	0.284	0.000	0.000	0.000	0.000
150	A	168	ASP	-1	-0.814	-0.888	36.630	-0.302	-0.302	0.000	0.000	0.000	0.000
151	A	169	THR	0	-0.035	-0.030	33.337	-0.014	-0.014	0.000	0.000	0.000	0.000
152	A	170	ASP	-1	-0.947	-0.982	34.952	-0.469	-0.469	0.000	0.000	0.000	0.000
153	A	171	ARG	1	0.803	0.887	36.436	0.323	0.323	0.000	0.000	0.000	0.000
154	A	172	ASP	-1	-0.844	-0.921	33.287	-0.410	-0.410	0.000	0.000	0.000	0.000
155	A	173	ASN	0	-0.054	-0.016	33.957	0.067	0.067	0.000	0.000	0.000	0.000
156	A	174	PHE	0	0.012	-0.015	28.487	-0.046	-0.046	0.000	0.000	0.000	0.000
157	A	175	LEU	0	-0.014	0.003	30.919	0.024	0.024	0.000	0.000	0.000	0.000
158	A	176	THR	0	0.007	-0.028	30.019	-0.016	-0.016	0.000	0.000	0.000	0.000
159	A	177	ALA	0	0.029	0.013	27.508	-0.039	-0.039	0.000	0.000	0.000	0.000
160	A	178	GLU	-1	-0.801	-0.905	29.153	-0.138	-0.138	0.000	0.000	0.000	0.000
161	A	179	GLU	-1	-0.801	-0.870	32.637	-0.188	-0.188	0.000	0.000	0.000	0.000
162	A	180	ALA	0	-0.023	-0.018	29.539	-0.030	-0.030	0.000	0.000	0.000	0.000
163	A	181	LYS	1	0.807	0.892	31.167	0.139	0.139	0.000	0.000	0.000	0.000
164	A	182	GLU	-1	-0.921	-0.957	32.252	-0.169	-0.169	0.000	0.000	0.000	0.000
165	A	183	TYR	0	-0.115	-0.085	33.577	-0.014	-0.014	0.000	0.000	0.000	0.000
166	A	184	GLY	0	0.050	0.031	33.671	-0.018	-0.018	0.000	0.000	0.000	0.000
167	A	185	LEU	0	-0.069	-0.043	29.023	-0.053	-0.053	0.000	0.000	0.000	0.000
168	A	186	ILE	0	-0.051	-0.019	26.000	-0.078	-0.078	0.000	0.000	0.000	0.000
169	A	187	ASP	-1	-0.793	-0.883	28.440	-0.525	-0.525	0.000	0.000	0.000	0.000
170	A	188	GLU	-1	-0.914	-0.962	28.507	-0.142	-0.142	0.000	0.000	0.000	0.000
171	A	189	VAL	0	-0.036	-0.010	27.658	-0.049	-0.049	0.000	0.000	0.000	0.000
172	A	190	MET	0	-0.004	-0.007	22.441	0.033	0.033	0.000	0.000	0.000	0.000
173	A	191	VAL	0	-0.005	-0.006	26.265	0.048	0.048	0.000	0.000	0.000	0.000
174	A	192	PRO	0	-0.064	-0.026	24.652	-0.003	-0.003	0.000	0.000	0.000	0.000
175	A	193	GLU	-1	-0.949	-0.977	24.715	0.551	0.551	0.000	0.000	0.000	0.000
176	A	194	THR	-1	-0.985	-0.985	27.560	0.387	0.387	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:19:ASP)