FMO DATABASE

FMODB ID: RMLV8

Calculation Name: 4HNZ-A-Xray547

Preferred Name:

Target Type:

Ligand Name: magnesium ion

Ligand 3-letter code: MG

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 4HNZ

Chain ID: A

ChEMBL ID:

UniProt ID: Q383Q5

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	174
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1732061.138073
FMO2-HF: Nuclear repulsion	1666130.552699
FMO2-HF: Total energy	-65930.585374
FMO2-MP2: Total energy	-66123.938396

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:1:THR)

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

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.
-252.473	-243.572	38.307	-21.139	-26.069	-0.193

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.712 / q_NPA : 0.854

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	ILE	0	-0.003	0.010	2.475	3.663	5.645	0.676	-0.650	-2.008	-0.005
4	A	4	LEU	0	-0.007	-0.003	4.654	0.779	0.785	-0.001	-0.004	-0.001	0.000
17	A	17	ASP	-1	-0.767	-0.862	2.160	-77.080	-75.415	6.183	-4.000	-3.848	-0.045
18	A	18	ARG	1	0.840	0.891	4.694	24.398	24.522	-0.001	-0.007	-0.117	0.000
19	A	19	GLN	0	-0.062	-0.020	4.397	6.630	6.701	-0.001	-0.009	-0.061	0.000
20	A	20	VAL	0	-0.005	-0.004	4.268	-4.961	-4.720	-0.001	-0.015	-0.225	0.000
21	A	21	THR	0	0.034	0.013	4.248	3.791	3.852	-0.001	-0.001	-0.059	0.000
34	A	34	LYS	1	0.789	0.895	1.988	51.855	51.206	7.134	-2.548	-3.937	0.029
47	A	47	ALA	0	-0.010	-0.007	2.334	-8.147	-7.072	1.426	-0.866	-1.635	-0.003
48	A	48	GLY	0	0.071	0.026	3.143	6.083	5.573	0.045	0.681	-0.215	-0.001
49	A	49	SER	0	-0.068	-0.060	5.160	-1.702	-1.626	-0.001	0.000	-0.075	0.000
123	A	123	ILE	0	-0.003	0.020	4.126	0.575	0.729	-0.001	-0.016	-0.137	0.000
124	A	124	GLY	0	0.005	-0.007	2.991	-7.111	-6.542	0.124	-0.295	-0.398	-0.001
125	A	125	SER	0	-0.038	-0.043	2.138	-7.727	-6.809	3.643	-2.024	-2.538	-0.026
126	A	126	GLY	0	0.051	0.028	3.474	10.428	10.841	0.001	-0.135	-0.278	0.000
127	A	127	GLY	0	0.005	0.008	5.111	7.422	7.523	-0.001	-0.007	-0.093	0.000
160	A	160	ASP	-1	-0.732	-0.829	1.849	-117.709	-118.405	8.471	-4.546	-3.229	-0.062
161	A	161	VAL	0	0.042	0.021	4.863	-4.050	-3.997	-0.001	-0.003	-0.049	0.000
162	A	162	PHE	0	-0.062	-0.030	2.841	3.873	5.054	0.397	-0.664	-0.915	-0.003
163	A	163	SER	0	-0.074	-0.066	1.965	-37.177	-35.312	10.200	-5.963	-6.102	-0.075
164	A	164	ASN	0	0.000	0.004	3.607	6.318	6.519	0.016	-0.067	-0.149	-0.001
5	A	5	SER	0	-0.048	-0.024	8.356	1.365	1.365	0.000	0.000	0.000	0.000
6	A	6	VAL	0	0.021	-0.002	11.654	-0.061	-0.061	0.000	0.000	0.000	0.000
7	A	7	ARG	1	0.875	0.932	15.150	15.232	15.232	0.000	0.000	0.000	0.000
8	A	8	LYS	1	0.809	0.902	18.618	13.404	13.404	0.000	0.000	0.000	0.000
9	A	9	GLY	0	-0.020	-0.006	21.689	0.139	0.139	0.000	0.000	0.000	0.000
10	A	10	ASP	-1	-0.901	-0.960	23.588	-11.194	-11.194	0.000	0.000	0.000	0.000
11	A	11	THR	0	-0.030	-0.013	19.850	-0.111	-0.111	0.000	0.000	0.000	0.000
12	A	12	VAL	0	-0.058	-0.036	15.931	-0.441	-0.441	0.000	0.000	0.000	0.000
13	A	13	VAL	0	-0.009	0.000	13.979	-0.019	-0.019	0.000	0.000	0.000	0.000
14	A	14	LEU	0	0.002	0.002	8.902	-0.886	-0.886	0.000	0.000	0.000	0.000
15	A	15	LEU	0	0.009	-0.003	9.239	0.682	0.682	0.000	0.000	0.000	0.000
16	A	16	GLY	0	0.032	0.002	5.241	-2.462	-2.462	0.000	0.000	0.000	0.000
22	A	22	LEU	0	0.000	-0.005	6.809	0.573	0.573	0.000	0.000	0.000	0.000
23	A	23	GLY	0	-0.009	-0.020	10.062	0.345	0.345	0.000	0.000	0.000	0.000
24	A	24	GLU	-1	-0.918	-0.955	8.308	-27.642	-27.642	0.000	0.000	0.000	0.000
25	A	25	ARG	1	0.903	0.953	9.398	21.378	21.378	0.000	0.000	0.000	0.000
26	A	26	ILE	0	-0.006	0.007	10.568	0.892	0.892	0.000	0.000	0.000	0.000
27	A	27	VAL	0	0.025	0.019	7.882	-2.023	-2.023	0.000	0.000	0.000	0.000
28	A	28	ALA	0	-0.009	0.002	9.974	2.292	2.292	0.000	0.000	0.000	0.000
29	A	29	LYS	1	0.877	0.923	10.111	22.971	22.971	0.000	0.000	0.000	0.000
30	A	30	SER	0	0.044	0.032	9.089	-2.520	-2.520	0.000	0.000	0.000	0.000
31	A	31	SER	0	0.046	0.025	10.144	-0.379	-0.379	0.000	0.000	0.000	0.000
32	A	32	ALA	0	-0.040	-0.022	7.978	2.395	2.395	0.000	0.000	0.000	0.000
33	A	33	CYS	0	0.046	0.050	7.656	-2.636	-2.636	0.000	0.000	0.000	0.000
35	A	35	LEU	0	0.024	0.018	6.395	-0.706	-0.706	0.000	0.000	0.000	0.000
36	A	36	ARG	1	0.832	0.887	9.242	22.836	22.836	0.000	0.000	0.000	0.000
37	A	37	ARG	1	0.840	0.914	12.671	14.355	14.355	0.000	0.000	0.000	0.000
38	A	38	ILE	0	-0.009	-0.001	15.239	0.242	0.242	0.000	0.000	0.000	0.000
39	A	39	ASN	0	-0.006	-0.004	17.993	0.474	0.474	0.000	0.000	0.000	0.000
40	A	40	ASP	-1	-0.907	-0.953	20.277	-12.089	-12.089	0.000	0.000	0.000	0.000
41	A	41	ASP	-1	-0.899	-0.930	21.920	-11.814	-11.814	0.000	0.000	0.000	0.000
42	A	42	VAL	0	-0.053	-0.030	16.819	-0.449	-0.449	0.000	0.000	0.000	0.000
43	A	43	VAL	0	-0.005	0.001	13.904	-0.190	-0.190	0.000	0.000	0.000	0.000
44	A	44	ILE	0	-0.001	-0.009	10.467	-0.157	-0.157	0.000	0.000	0.000	0.000
45	A	45	GLY	0	0.016	0.006	7.697	-0.176	-0.176	0.000	0.000	0.000	0.000
46	A	46	PHE	0	-0.025	-0.015	5.188	0.708	0.708	0.000	0.000	0.000	0.000
50	A	50	THR	0	0.022	-0.009	7.817	-0.185	-0.185	0.000	0.000	0.000	0.000
51	A	51	ALA	0	0.025	0.021	9.836	1.023	1.023	0.000	0.000	0.000	0.000
52	A	52	ASP	-1	-0.799	-0.851	9.875	-21.084	-21.084	0.000	0.000	0.000	0.000
53	A	53	ALA	0	0.059	0.022	7.892	0.767	0.767	0.000	0.000	0.000	0.000
54	A	54	ILE	0	-0.030	-0.015	10.011	0.798	0.798	0.000	0.000	0.000	0.000
55	A	55	SER	0	-0.011	-0.016	13.162	1.177	1.177	0.000	0.000	0.000	0.000
56	A	56	LEU	0	-0.027	-0.017	11.602	0.920	0.920	0.000	0.000	0.000	0.000
57	A	57	MET	0	-0.050	-0.014	10.385	0.230	0.230	0.000	0.000	0.000	0.000
58	A	58	GLU	-1	-0.860	-0.929	14.393	-13.811	-13.811	0.000	0.000	0.000	0.000
59	A	59	LYS	1	0.820	0.910	17.278	13.810	13.810	0.000	0.000	0.000	0.000
60	A	60	LEU	0	0.015	0.000	14.741	0.538	0.538	0.000	0.000	0.000	0.000
61	A	61	GLU	-1	-0.890	-0.948	17.332	-14.211	-14.211	0.000	0.000	0.000	0.000
62	A	62	ASN	0	-0.040	-0.017	19.915	0.836	0.836	0.000	0.000	0.000	0.000
63	A	63	LYS	1	0.837	0.927	20.613	12.250	12.250	0.000	0.000	0.000	0.000
64	A	64	ILE	0	0.010	-0.004	18.388	0.318	0.318	0.000	0.000	0.000	0.000
65	A	65	GLY	0	-0.015	-0.003	22.619	0.403	0.403	0.000	0.000	0.000	0.000
66	A	66	GLU	-1	-0.933	-0.964	25.324	-10.360	-10.360	0.000	0.000	0.000	0.000
67	A	67	PHE	0	-0.072	-0.047	24.848	0.459	0.459	0.000	0.000	0.000	0.000
68	A	68	PRO	0	0.021	0.008	25.648	-0.263	-0.263	0.000	0.000	0.000	0.000
69	A	69	ASN	0	0.002	0.003	25.773	0.021	0.021	0.000	0.000	0.000	0.000
70	A	70	GLN	0	-0.009	0.005	25.052	0.025	0.025	0.000	0.000	0.000	0.000
71	A	71	LEU	0	0.062	0.048	17.464	-0.136	-0.136	0.000	0.000	0.000	0.000
72	A	72	THR	0	0.003	-0.044	20.134	-0.579	-0.579	0.000	0.000	0.000	0.000
73	A	73	ARG	1	0.848	0.929	21.185	10.164	10.164	0.000	0.000	0.000	0.000
74	A	74	ALA	0	0.037	0.017	20.709	-0.035	-0.035	0.000	0.000	0.000	0.000
75	A	75	ALA	0	0.034	0.016	17.100	-0.332	-0.332	0.000	0.000	0.000	0.000
76	A	76	VAL	0	0.007	0.003	18.440	-0.334	-0.334	0.000	0.000	0.000	0.000
77	A	77	GLU	-1	-0.843	-0.913	20.992	-11.288	-11.288	0.000	0.000	0.000	0.000
78	A	78	LEU	0	0.013	0.018	14.532	0.127	0.127	0.000	0.000	0.000	0.000
79	A	79	ALA	0	0.016	0.012	17.518	-0.204	-0.204	0.000	0.000	0.000	0.000
80	A	80	LYS	1	0.776	0.864	18.425	11.404	11.404	0.000	0.000	0.000	0.000
81	A	81	GLU	-1	-0.833	-0.896	20.577	-12.538	-12.538	0.000	0.000	0.000	0.000
82	A	82	TRP	0	0.013	-0.005	10.729	0.245	0.245	0.000	0.000	0.000	0.000
83	A	83	ARG	1	0.870	0.935	17.610	15.881	15.881	0.000	0.000	0.000	0.000
84	A	84	THR	0	-0.085	-0.057	20.279	0.504	0.504	0.000	0.000	0.000	0.000
85	A	85	ASP	-1	-0.789	-0.888	21.362	-12.325	-12.325	0.000	0.000	0.000	0.000
86	A	86	ARG	1	0.897	0.932	21.572	10.702	10.702	0.000	0.000	0.000	0.000
87	A	87	ALA	0	-0.038	-0.016	20.802	-0.212	-0.212	0.000	0.000	0.000	0.000
88	A	88	LEU	0	0.048	0.024	17.017	-0.711	-0.711	0.000	0.000	0.000	0.000
89	A	89	ARG	1	0.886	0.941	16.468	13.392	13.392	0.000	0.000	0.000	0.000
90	A	90	ARG	1	0.804	0.905	17.257	13.566	13.566	0.000	0.000	0.000	0.000
91	A	91	LEU	0	-0.013	0.022	13.025	-0.239	-0.239	0.000	0.000	0.000	0.000
92	A	92	GLU	-1	-0.955	-0.969	9.675	-24.253	-24.253	0.000	0.000	0.000	0.000
93	A	93	ALA	0	-0.015	-0.026	7.663	-2.191	-2.191	0.000	0.000	0.000	0.000
94	A	94	SER	0	-0.072	-0.046	6.708	1.065	1.065	0.000	0.000	0.000	0.000
95	A	95	LEU	0	-0.011	-0.007	6.597	-2.851	-2.851	0.000	0.000	0.000	0.000
96	A	96	ILE	0	0.011	0.009	7.391	0.447	0.447	0.000	0.000	0.000	0.000
97	A	97	VAL	0	0.012	0.006	9.825	-0.132	-0.132	0.000	0.000	0.000	0.000
98	A	98	CYS	0	-0.029	-0.005	12.883	-0.184	-0.184	0.000	0.000	0.000	0.000
99	A	99	SER	0	0.088	0.052	15.527	0.080	0.080	0.000	0.000	0.000	0.000
100	A	100	ALA	0	0.092	0.042	18.829	-0.528	-0.528	0.000	0.000	0.000	0.000
101	A	101	GLU	-1	-0.915	-0.955	21.286	-12.053	-12.053	0.000	0.000	0.000	0.000
102	A	102	GLU	-1	-0.820	-0.891	19.633	-13.000	-13.000	0.000	0.000	0.000	0.000
103	A	103	THR	0	-0.007	-0.024	13.541	-0.102	-0.102	0.000	0.000	0.000	0.000
104	A	104	LEU	0	-0.034	-0.009	14.484	0.385	0.385	0.000	0.000	0.000	0.000
105	A	105	GLU	-1	-0.901	-0.948	10.209	-25.850	-25.850	0.000	0.000	0.000	0.000
106	A	106	ILE	0	-0.012	-0.005	10.991	1.619	1.619	0.000	0.000	0.000	0.000
107	A	107	ASP	-1	-0.751	-0.865	10.738	-23.195	-23.195	0.000	0.000	0.000	0.000
108	A	108	GLY	0	0.088	0.054	11.891	1.562	1.562	0.000	0.000	0.000	0.000
109	A	109	GLN	0	-0.096	-0.053	12.200	1.999	1.999	0.000	0.000	0.000	0.000
110	A	110	GLY	0	-0.041	-0.032	15.761	1.269	1.269	0.000	0.000	0.000	0.000
111	A	111	ASN	0	-0.122	-0.059	14.556	1.890	1.890	0.000	0.000	0.000	0.000
112	A	112	VAL	0	0.003	-0.015	15.336	-0.614	-0.614	0.000	0.000	0.000	0.000
113	A	113	ILE	0	-0.033	-0.006	13.548	0.919	0.919	0.000	0.000	0.000	0.000
114	A	114	THR	0	0.036	0.028	15.174	-0.511	-0.511	0.000	0.000	0.000	0.000
115	A	115	PRO	0	-0.049	-0.014	16.124	-0.386	-0.386	0.000	0.000	0.000	0.000
116	A	116	GLU	-1	-0.902	-0.946	17.172	-14.215	-14.215	0.000	0.000	0.000	0.000
117	A	117	ALA	0	-0.020	-0.026	20.261	-0.023	-0.023	0.000	0.000	0.000	0.000
118	A	118	ASP	-1	-0.810	-0.895	18.129	-16.610	-16.610	0.000	0.000	0.000	0.000
119	A	119	GLY	0	0.042	0.022	18.397	-0.271	-0.271	0.000	0.000	0.000	0.000
120	A	120	ILE	0	-0.067	-0.032	13.250	-0.916	-0.916	0.000	0.000	0.000	0.000
121	A	121	VAL	0	-0.007	-0.007	10.382	0.023	0.023	0.000	0.000	0.000	0.000
122	A	122	ALA	0	-0.019	-0.021	7.901	-0.828	-0.828	0.000	0.000	0.000	0.000
128	A	128	THR	0	0.011	-0.012	6.916	4.364	4.364	0.000	0.000	0.000	0.000
129	A	129	PHE	0	0.015	0.010	7.099	3.805	3.805	0.000	0.000	0.000	0.000
130	A	130	ALA	0	0.028	0.022	8.521	2.877	2.877	0.000	0.000	0.000	0.000
131	A	131	LYS	1	0.972	0.983	10.449	25.837	25.837	0.000	0.000	0.000	0.000
132	A	132	ALA	0	-0.021	-0.011	12.414	2.048	2.048	0.000	0.000	0.000	0.000
133	A	133	ALA	0	-0.018	-0.012	13.241	1.623	1.623	0.000	0.000	0.000	0.000
134	A	134	ALA	0	0.021	-0.003	13.771	1.258	1.258	0.000	0.000	0.000	0.000
135	A	135	ARG	1	0.839	0.896	15.635	18.658	18.658	0.000	0.000	0.000	0.000
136	A	136	ALA	0	-0.034	-0.001	18.157	0.991	0.991	0.000	0.000	0.000	0.000
137	A	137	LEU	0	-0.051	-0.035	17.987	0.729	0.729	0.000	0.000	0.000	0.000
138	A	138	ILE	0	-0.003	0.010	18.681	0.390	0.390	0.000	0.000	0.000	0.000
139	A	139	ASP	-1	-0.897	-0.949	20.951	-12.446	-12.446	0.000	0.000	0.000	0.000
140	A	140	VAL	0	-0.031	0.006	23.754	0.524	0.524	0.000	0.000	0.000	0.000
141	A	141	ASP	-1	-0.868	-0.937	25.486	-10.808	-10.808	0.000	0.000	0.000	0.000
142	A	142	GLY	0	-0.020	-0.023	26.969	-0.222	-0.222	0.000	0.000	0.000	0.000
143	A	143	TYR	0	-0.040	-0.028	20.426	-0.656	-0.656	0.000	0.000	0.000	0.000
144	A	144	ASP	-1	-0.773	-0.874	21.021	-13.991	-13.991	0.000	0.000	0.000	0.000
145	A	145	ALA	0	0.078	0.028	17.938	-0.627	-0.627	0.000	0.000	0.000	0.000
146	A	146	GLU	-1	-0.756	-0.853	16.197	-17.592	-17.592	0.000	0.000	0.000	0.000
147	A	147	LYS	1	0.815	0.904	16.579	12.284	12.284	0.000	0.000	0.000	0.000
148	A	148	ILE	0	-0.027	-0.007	15.866	-0.559	-0.559	0.000	0.000	0.000	0.000
149	A	149	ALA	0	0.035	0.022	12.695	-1.118	-1.118	0.000	0.000	0.000	0.000
150	A	150	ARG	1	0.846	0.888	12.733	16.454	16.454	0.000	0.000	0.000	0.000
151	A	151	LYS	1	0.881	0.956	13.630	15.572	15.572	0.000	0.000	0.000	0.000
152	A	152	ALA	0	0.020	0.006	12.828	-0.395	-0.395	0.000	0.000	0.000	0.000
153	A	153	MET	0	0.006	0.004	6.056	-2.695	-2.695	0.000	0.000	0.000	0.000
154	A	154	ARG	1	0.864	0.964	9.469	19.135	19.135	0.000	0.000	0.000	0.000
155	A	155	ILE	0	0.019	0.009	10.900	-0.934	-0.934	0.000	0.000	0.000	0.000
156	A	156	ALA	0	-0.014	-0.003	7.395	-0.299	-0.299	0.000	0.000	0.000	0.000
157	A	157	THR	0	-0.066	-0.064	5.418	-3.559	-3.559	0.000	0.000	0.000	0.000
158	A	158	ASP	-1	-0.885	-0.939	7.048	-25.106	-25.106	0.000	0.000	0.000	0.000
159	A	159	ILE	0	-0.076	-0.026	8.517	2.088	2.088	0.000	0.000	0.000	0.000
165	A	165	GLU	-1	-0.803	-0.912	7.036	-27.774	-27.774	0.000	0.000	0.000	0.000
166	A	166	HIS	0	-0.125	-0.049	9.069	2.865	2.865	0.000	0.000	0.000	0.000
167	A	167	TRP	0	-0.004	-0.033	7.355	-0.914	-0.914	0.000	0.000	0.000	0.000
168	A	168	ASP	-1	-0.828	-0.873	8.449	-21.711	-21.711	0.000	0.000	0.000	0.000
169	A	169	VAL	0	-0.018	-0.038	9.777	-1.660	-1.660	0.000	0.000	0.000	0.000
170	A	170	GLU	-1	-0.842	-0.907	12.397	-15.962	-15.962	0.000	0.000	0.000	0.000
171	A	171	VAL	0	-0.013	-0.009	14.311	-0.603	-0.603	0.000	0.000	0.000	0.000
172	A	172	LEU	0	-0.038	-0.014	17.449	0.418	0.418	0.000	0.000	0.000	0.000
173	A	173	GLU	-1	-0.830	-0.895	20.104	-12.981	-12.981	0.000	0.000	0.000	0.000
174	A	174	HIS	0	-0.034	-0.003	23.462	0.482	0.482	0.000	0.000	0.000	0.000

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