FMO DATABASE

FMODB ID: VYVV1

Calculation Name: 2F1D-A-Xray547

Preferred Name:

Target Type:

Ligand Name: sulfate ion | manganese (ii) ion

Ligand 3-letter code: SO4 | MN

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2F1D

Chain ID: A

ChEMBL ID:

UniProt ID: P34047

Base Structure: X-ray

Registration Date: 2025-10-05

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	183
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1950408.685271
FMO2-HF: Nuclear repulsion	1880851.145687
FMO2-HF: Total energy	-69557.539584
FMO2-MP2: Total energy	-69764.294673

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:10:GLY)

Summations of interaction energy for fragment #1(A:10: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.
-215.675	-210.395	12.866	-10.744	-7.401	-0.119

Interaction energy analysis for fragmet #1(A:10:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.763 / q_NPA : 0.868

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	12	ILE	0	0.001	-0.003	3.081	-0.485	0.691	0.042	-0.406	-0.812	-0.001
20	A	29	ASN	0	-0.040	-0.023	1.859	-38.992	-38.201	8.132	-5.416	-3.506	-0.073
21	A	30	LEU	0	0.027	0.001	4.583	5.926	6.049	-0.001	-0.012	-0.110	0.000
22	A	31	ASP	-1	-0.812	-0.867	2.103	-70.429	-68.261	4.672	-4.311	-2.529	-0.040
23	A	32	GLY	0	-0.015	-0.001	3.445	-15.903	-14.881	0.021	-0.599	-0.444	-0.005
4	A	13	GLY	0	-0.001	0.027	5.445	5.051	5.051	0.000	0.000	0.000	0.000
5	A	14	GLU	-1	-0.856	-0.930	9.121	-28.278	-28.278	0.000	0.000	0.000	0.000
6	A	15	VAL	0	-0.035	-0.019	11.728	1.410	1.410	0.000	0.000	0.000	0.000
7	A	16	LYS	1	0.883	0.950	15.433	15.368	15.368	0.000	0.000	0.000	0.000
8	A	17	ARG	1	0.898	0.932	18.548	13.370	13.370	0.000	0.000	0.000	0.000
9	A	18	VAL	0	-0.030	-0.017	21.804	0.001	0.001	0.000	0.000	0.000	0.000
10	A	19	THR	0	-0.006	0.015	25.395	0.110	0.110	0.000	0.000	0.000	0.000
11	A	20	LYS	1	0.801	0.898	28.575	9.665	9.665	0.000	0.000	0.000	0.000
12	A	21	GLU	-1	-0.895	-0.962	29.678	-9.930	-9.930	0.000	0.000	0.000	0.000
13	A	22	THR	0	-0.045	-0.046	25.628	-0.223	-0.223	0.000	0.000	0.000	0.000
14	A	23	ASN	0	-0.010	-0.002	23.721	-0.621	-0.621	0.000	0.000	0.000	0.000
15	A	24	VAL	0	0.055	0.025	19.171	-0.180	-0.180	0.000	0.000	0.000	0.000
16	A	25	SER	0	-0.025	-0.025	16.439	0.129	0.129	0.000	0.000	0.000	0.000
17	A	26	VAL	0	0.026	0.021	12.849	0.191	0.191	0.000	0.000	0.000	0.000
18	A	27	LYS	1	0.825	0.905	7.857	31.709	31.709	0.000	0.000	0.000	0.000
19	A	28	ILE	0	0.034	0.020	7.995	0.751	0.751	0.000	0.000	0.000	0.000
24	A	33	THR	0	-0.073	-0.051	5.605	4.194	4.194	0.000	0.000	0.000	0.000
25	A	34	GLY	0	0.031	0.026	9.045	3.085	3.085	0.000	0.000	0.000	0.000
26	A	35	VAL	0	-0.073	-0.030	9.899	2.512	2.512	0.000	0.000	0.000	0.000
27	A	36	ALA	0	0.036	0.022	11.358	-1.374	-1.374	0.000	0.000	0.000	0.000
28	A	37	ASP	-1	-0.796	-0.878	13.952	-18.360	-18.360	0.000	0.000	0.000	0.000
29	A	38	SER	0	-0.021	-0.001	15.504	-0.467	-0.467	0.000	0.000	0.000	0.000
30	A	39	SER	0	0.002	-0.003	17.729	0.863	0.863	0.000	0.000	0.000	0.000
31	A	40	SER	0	-0.040	-0.070	21.047	0.255	0.255	0.000	0.000	0.000	0.000
32	A	41	GLY	0	0.009	0.006	22.505	0.385	0.385	0.000	0.000	0.000	0.000
33	A	42	ILE	0	-0.043	-0.006	24.948	0.533	0.533	0.000	0.000	0.000	0.000
34	A	43	PRO	0	0.029	0.002	24.881	-0.403	-0.403	0.000	0.000	0.000	0.000
35	A	44	PHE	0	0.014	0.005	24.983	-0.298	-0.298	0.000	0.000	0.000	0.000
36	A	45	LEU	0	0.015	0.006	21.427	-0.322	-0.322	0.000	0.000	0.000	0.000
37	A	46	ASP	-1	-0.790	-0.868	20.320	-15.215	-15.215	0.000	0.000	0.000	0.000
38	A	47	HIS	0	0.015	0.002	19.907	-1.002	-1.002	0.000	0.000	0.000	0.000
39	A	48	MET	0	-0.025	-0.013	20.950	-0.351	-0.351	0.000	0.000	0.000	0.000
40	A	49	LEU	0	-0.033	-0.015	16.046	-0.835	-0.835	0.000	0.000	0.000	0.000
41	A	50	ASP	-1	-0.843	-0.927	15.897	-18.064	-18.064	0.000	0.000	0.000	0.000
42	A	51	GLN	0	-0.072	-0.026	16.933	-0.593	-0.593	0.000	0.000	0.000	0.000
43	A	52	LEU	0	-0.018	-0.012	13.705	-0.473	-0.473	0.000	0.000	0.000	0.000
44	A	53	ALA	0	0.001	0.004	12.122	-1.171	-1.171	0.000	0.000	0.000	0.000
45	A	54	SER	0	-0.017	-0.028	12.589	-0.973	-0.973	0.000	0.000	0.000	0.000
46	A	55	HIS	0	-0.022	-0.008	15.080	0.084	0.084	0.000	0.000	0.000	0.000
47	A	56	GLY	0	-0.005	0.009	12.791	0.501	0.501	0.000	0.000	0.000	0.000
48	A	57	LEU	0	-0.050	-0.026	10.036	-1.280	-1.280	0.000	0.000	0.000	0.000
49	A	58	PHE	0	0.008	0.016	7.679	-3.373	-3.373	0.000	0.000	0.000	0.000
50	A	59	ASP	-1	-0.801	-0.890	5.813	-43.258	-43.258	0.000	0.000	0.000	0.000
51	A	60	VAL	0	-0.005	-0.017	8.233	-1.908	-1.908	0.000	0.000	0.000	0.000
52	A	61	HIS	0	-0.067	-0.031	11.056	2.328	2.328	0.000	0.000	0.000	0.000
53	A	62	VAL	0	0.027	-0.007	12.896	-0.183	-0.183	0.000	0.000	0.000	0.000
54	A	63	ARG	1	0.780	0.871	16.254	18.377	18.377	0.000	0.000	0.000	0.000
55	A	64	ALA	0	-0.019	-0.005	19.364	-0.178	-0.178	0.000	0.000	0.000	0.000
56	A	65	THR	0	-0.004	-0.006	22.491	0.362	0.362	0.000	0.000	0.000	0.000
57	A	66	GLY	0	0.071	0.027	26.305	-0.215	-0.215	0.000	0.000	0.000	0.000
58	A	67	ASP	-1	-0.771	-0.845	28.925	-9.707	-9.707	0.000	0.000	0.000	0.000
59	A	68	VAL	0	0.030	0.009	29.409	0.211	0.211	0.000	0.000	0.000	0.000
60	A	69	HIS	0	-0.038	-0.013	32.148	0.036	0.036	0.000	0.000	0.000	0.000
61	A	70	ILE	0	-0.096	-0.038	35.125	0.320	0.320	0.000	0.000	0.000	0.000
62	A	71	ASP	-1	-0.824	-0.940	33.729	-9.328	-9.328	0.000	0.000	0.000	0.000
63	A	72	ASP	-1	-0.839	-0.925	29.204	-10.876	-10.876	0.000	0.000	0.000	0.000
64	A	73	HIS	0	-0.043	-0.018	28.659	-0.415	-0.415	0.000	0.000	0.000	0.000
65	A	74	HIS	0	-0.048	-0.045	28.473	-0.247	-0.247	0.000	0.000	0.000	0.000
66	A	75	THR	0	0.042	0.017	25.023	-0.433	-0.433	0.000	0.000	0.000	0.000
67	A	76	ASN	0	0.033	0.017	24.262	-0.865	-0.865	0.000	0.000	0.000	0.000
68	A	77	GLU	-1	-0.843	-0.910	23.680	-11.763	-11.763	0.000	0.000	0.000	0.000
69	A	78	ASP	-1	-0.750	-0.856	23.492	-13.012	-13.012	0.000	0.000	0.000	0.000
70	A	79	ILE	0	-0.023	-0.011	18.799	-0.890	-0.890	0.000	0.000	0.000	0.000
71	A	80	ALA	0	0.003	0.024	18.908	-1.047	-1.047	0.000	0.000	0.000	0.000
72	A	81	LEU	0	-0.012	-0.002	19.408	-0.747	-0.747	0.000	0.000	0.000	0.000
73	A	82	ALA	0	-0.026	0.004	17.589	-0.643	-0.643	0.000	0.000	0.000	0.000
74	A	83	ILE	0	0.033	0.011	14.399	-1.414	-1.414	0.000	0.000	0.000	0.000
75	A	84	GLY	0	0.020	0.019	14.535	-1.478	-1.478	0.000	0.000	0.000	0.000
76	A	85	THR	0	-0.020	-0.027	15.869	-0.473	-0.473	0.000	0.000	0.000	0.000
77	A	86	ALA	0	-0.061	-0.036	11.684	-0.843	-0.843	0.000	0.000	0.000	0.000
78	A	87	LEU	0	0.049	0.023	11.126	-2.778	-2.778	0.000	0.000	0.000	0.000
79	A	88	LEU	0	0.003	0.004	11.665	-1.669	-1.669	0.000	0.000	0.000	0.000
80	A	89	LYS	1	0.834	0.897	12.032	21.757	21.757	0.000	0.000	0.000	0.000
81	A	90	ALA	0	0.007	0.017	7.240	-1.463	-1.463	0.000	0.000	0.000	0.000
82	A	91	LEU	0	-0.013	-0.007	7.936	-2.789	-2.789	0.000	0.000	0.000	0.000
83	A	92	GLY	0	0.011	0.019	10.390	-0.077	-0.077	0.000	0.000	0.000	0.000
84	A	93	GLU	-1	-0.854	-0.941	11.833	-16.409	-16.409	0.000	0.000	0.000	0.000
85	A	94	ARG	1	0.888	0.957	12.145	19.828	19.828	0.000	0.000	0.000	0.000
86	A	95	LYS	1	0.791	0.880	12.539	19.667	19.667	0.000	0.000	0.000	0.000
87	A	96	GLY	0	0.043	0.020	11.806	-1.571	-1.571	0.000	0.000	0.000	0.000
88	A	97	ILE	0	-0.039	-0.003	10.123	-0.695	-0.695	0.000	0.000	0.000	0.000
89	A	98	ASN	0	0.035	0.015	12.793	1.955	1.955	0.000	0.000	0.000	0.000
90	A	99	ARG	1	0.789	0.885	14.785	16.396	16.396	0.000	0.000	0.000	0.000
91	A	100	PHE	0	-0.016	-0.029	16.442	0.355	0.355	0.000	0.000	0.000	0.000
92	A	101	GLY	0	0.010	0.012	17.856	-0.809	-0.809	0.000	0.000	0.000	0.000
93	A	102	ASP	-1	-0.838	-0.883	18.992	-11.990	-11.990	0.000	0.000	0.000	0.000
94	A	103	PHE	0	0.004	-0.005	20.709	-0.337	-0.337	0.000	0.000	0.000	0.000
95	A	104	THR	0	0.017	0.001	22.854	0.404	0.404	0.000	0.000	0.000	0.000
96	A	105	ALA	0	-0.014	0.005	23.369	-0.135	-0.135	0.000	0.000	0.000	0.000
97	A	106	PRO	0	0.002	0.002	25.486	0.264	0.264	0.000	0.000	0.000	0.000
98	A	107	LEU	0	-0.071	-0.040	26.641	-0.513	-0.513	0.000	0.000	0.000	0.000
99	A	108	ASP	-1	-0.878	-0.941	29.294	-9.718	-9.718	0.000	0.000	0.000	0.000
100	A	109	GLU	-1	-0.703	-0.823	32.935	-9.361	-9.361	0.000	0.000	0.000	0.000
101	A	110	ALA	0	-0.022	-0.012	30.585	0.098	0.098	0.000	0.000	0.000	0.000
102	A	111	LEU	0	-0.027	-0.017	29.478	-0.232	-0.232	0.000	0.000	0.000	0.000
103	A	112	ILE	0	0.004	0.007	26.523	0.272	0.272	0.000	0.000	0.000	0.000
104	A	113	HIS	0	-0.015	-0.009	26.209	0.048	0.048	0.000	0.000	0.000	0.000
105	A	114	VAL	0	-0.019	-0.021	21.529	0.097	0.097	0.000	0.000	0.000	0.000
106	A	115	SER	0	-0.030	-0.031	23.012	-0.274	-0.274	0.000	0.000	0.000	0.000
107	A	116	LEU	0	-0.034	-0.017	17.142	0.261	0.261	0.000	0.000	0.000	0.000
108	A	117	ASP	-1	-0.785	-0.876	19.878	-14.696	-14.696	0.000	0.000	0.000	0.000
109	A	118	LEU	0	0.002	0.023	13.586	0.209	0.209	0.000	0.000	0.000	0.000
110	A	119	SER	0	-0.071	-0.052	17.723	-0.359	-0.359	0.000	0.000	0.000	0.000
111	A	120	GLY	0	-0.032	-0.012	20.171	0.292	0.292	0.000	0.000	0.000	0.000
112	A	121	ARG	1	0.909	0.952	21.163	13.147	13.147	0.000	0.000	0.000	0.000
113	A	122	PRO	0	-0.001	0.019	23.701	-0.143	-0.143	0.000	0.000	0.000	0.000
114	A	123	TYR	0	-0.030	-0.031	24.617	0.628	0.628	0.000	0.000	0.000	0.000
115	A	124	LEU	0	0.026	0.016	25.050	-0.589	-0.589	0.000	0.000	0.000	0.000
116	A	125	GLY	0	-0.019	0.007	27.166	0.494	0.494	0.000	0.000	0.000	0.000
117	A	126	TYR	0	0.063	0.016	27.574	-0.345	-0.345	0.000	0.000	0.000	0.000
118	A	127	ASN	0	-0.070	-0.045	30.065	0.241	0.241	0.000	0.000	0.000	0.000
119	A	128	LEU	0	0.019	0.004	28.559	-0.088	-0.088	0.000	0.000	0.000	0.000
120	A	129	GLU	-1	-0.908	-0.956	32.552	-8.345	-8.345	0.000	0.000	0.000	0.000
121	A	130	ILE	0	-0.019	-0.004	30.576	-0.159	-0.159	0.000	0.000	0.000	0.000
122	A	131	PRO	0	0.041	0.034	34.983	0.096	0.096	0.000	0.000	0.000	0.000
123	A	132	THR	0	-0.059	-0.018	35.877	0.185	0.185	0.000	0.000	0.000	0.000
124	A	133	GLN	0	0.052	0.016	36.073	-0.201	-0.201	0.000	0.000	0.000	0.000
125	A	134	ARG	1	0.865	0.920	34.430	8.854	8.854	0.000	0.000	0.000	0.000
126	A	135	VAL	0	0.002	0.033	29.938	0.191	0.191	0.000	0.000	0.000	0.000
127	A	136	GLY	0	0.009	0.004	31.704	-0.287	-0.287	0.000	0.000	0.000	0.000
128	A	137	THR	0	-0.005	-0.023	32.215	0.233	0.233	0.000	0.000	0.000	0.000
129	A	138	TYR	0	-0.026	-0.011	25.930	0.136	0.136	0.000	0.000	0.000	0.000
130	A	139	ASP	-1	-0.802	-0.899	31.285	-9.037	-9.037	0.000	0.000	0.000	0.000
131	A	140	THR	0	0.024	-0.006	31.173	-0.439	-0.439	0.000	0.000	0.000	0.000
132	A	141	GLN	0	-0.022	-0.006	31.159	-0.122	-0.122	0.000	0.000	0.000	0.000
133	A	142	LEU	0	-0.049	-0.023	27.996	-0.261	-0.261	0.000	0.000	0.000	0.000
134	A	143	VAL	0	0.029	0.026	26.033	-0.584	-0.584	0.000	0.000	0.000	0.000
135	A	144	GLU	-1	-0.897	-0.941	26.001	-10.648	-10.648	0.000	0.000	0.000	0.000
136	A	145	HIS	1	0.792	0.896	26.941	10.948	10.948	0.000	0.000	0.000	0.000
137	A	146	PHE	0	0.040	0.026	18.449	-0.403	-0.403	0.000	0.000	0.000	0.000
138	A	147	PHE	0	0.044	0.009	20.360	-0.505	-0.505	0.000	0.000	0.000	0.000
139	A	148	GLN	0	0.021	0.011	23.016	-0.125	-0.125	0.000	0.000	0.000	0.000
140	A	149	SER	0	-0.047	-0.044	23.366	0.127	0.127	0.000	0.000	0.000	0.000
141	A	150	LEU	0	-0.003	0.007	16.894	-0.388	-0.388	0.000	0.000	0.000	0.000
142	A	151	VAL	0	-0.018	-0.012	19.683	-0.687	-0.687	0.000	0.000	0.000	0.000
143	A	152	ASN	0	-0.009	-0.019	21.851	-0.179	-0.179	0.000	0.000	0.000	0.000
144	A	153	THR	0	-0.053	-0.032	19.578	0.072	0.072	0.000	0.000	0.000	0.000
145	A	154	SER	0	-0.020	-0.005	16.788	-1.006	-1.006	0.000	0.000	0.000	0.000
146	A	155	GLY	0	-0.021	0.003	18.088	-0.508	-0.508	0.000	0.000	0.000	0.000
147	A	156	MET	0	-0.050	-0.014	16.728	0.098	0.098	0.000	0.000	0.000	0.000
148	A	157	THR	0	0.012	0.009	20.477	0.818	0.818	0.000	0.000	0.000	0.000
149	A	158	LEU	0	-0.002	-0.001	21.029	-0.568	-0.568	0.000	0.000	0.000	0.000
150	A	159	HIS	0	0.007	0.011	23.601	0.294	0.294	0.000	0.000	0.000	0.000
151	A	160	ILE	0	0.038	0.011	23.725	-0.413	-0.413	0.000	0.000	0.000	0.000
152	A	161	ARG	1	0.858	0.919	26.898	10.792	10.792	0.000	0.000	0.000	0.000
153	A	162	GLN	0	0.033	0.028	29.804	-0.417	-0.417	0.000	0.000	0.000	0.000
154	A	163	LEU	0	-0.068	-0.037	31.127	0.294	0.294	0.000	0.000	0.000	0.000
155	A	164	ALA	0	0.004	0.008	33.223	0.339	0.339	0.000	0.000	0.000	0.000
156	A	165	GLY	0	0.009	0.005	33.194	-0.387	-0.387	0.000	0.000	0.000	0.000
157	A	166	GLU	-1	-0.982	-0.981	34.792	-7.895	-7.895	0.000	0.000	0.000	0.000
158	A	167	ASN	0	-0.010	-0.018	33.525	-0.193	-0.193	0.000	0.000	0.000	0.000
159	A	168	SER	0	0.057	-0.006	33.026	-0.271	-0.271	0.000	0.000	0.000	0.000
160	A	169	HIS	0	-0.016	-0.003	27.604	-0.066	-0.066	0.000	0.000	0.000	0.000
161	A	170	HIS	1	0.783	0.865	28.797	9.408	9.408	0.000	0.000	0.000	0.000
162	A	171	ILE	0	0.038	0.032	28.693	-0.434	-0.434	0.000	0.000	0.000	0.000
163	A	172	ILE	0	0.017	0.018	25.703	-0.425	-0.425	0.000	0.000	0.000	0.000
164	A	173	GLU	-1	-0.776	-0.892	23.998	-13.105	-13.105	0.000	0.000	0.000	0.000
165	A	174	ALA	0	-0.019	-0.008	23.683	-0.648	-0.648	0.000	0.000	0.000	0.000
166	A	175	THR	0	0.020	-0.002	24.012	-0.315	-0.315	0.000	0.000	0.000	0.000
167	A	176	PHE	0	-0.003	-0.006	19.125	-0.520	-0.520	0.000	0.000	0.000	0.000
168	A	177	LYS	1	0.863	0.947	19.446	12.283	12.283	0.000	0.000	0.000	0.000
169	A	178	ALA	0	-0.004	-0.006	19.826	-0.698	-0.698	0.000	0.000	0.000	0.000
170	A	179	PHE	0	0.028	0.004	16.737	-0.588	-0.588	0.000	0.000	0.000	0.000
171	A	180	ALA	0	-0.002	0.002	15.546	-0.817	-0.817	0.000	0.000	0.000	0.000
172	A	181	ARG	1	0.885	0.943	15.241	15.490	15.490	0.000	0.000	0.000	0.000
173	A	182	ALA	0	0.014	0.012	16.704	-0.557	-0.557	0.000	0.000	0.000	0.000
174	A	183	LEU	0	0.017	0.001	12.679	-0.446	-0.446	0.000	0.000	0.000	0.000
175	A	184	ARG	1	0.850	0.921	11.279	22.189	22.189	0.000	0.000	0.000	0.000
176	A	185	GLN	0	-0.003	0.002	12.350	-0.524	-0.524	0.000	0.000	0.000	0.000
177	A	186	ALA	0	0.032	0.025	14.639	-0.072	-0.072	0.000	0.000	0.000	0.000
178	A	187	THR	0	-0.050	-0.049	9.173	-1.054	-1.054	0.000	0.000	0.000	0.000
179	A	188	GLU	-1	-0.815	-0.879	9.219	-26.908	-26.908	0.000	0.000	0.000	0.000
180	A	189	THR	0	-0.050	-0.034	8.968	0.395	0.395	0.000	0.000	0.000	0.000
181	A	190	ASP	-1	-0.889	-0.947	11.692	-15.735	-15.735	0.000	0.000	0.000	0.000
182	A	191	PRO	0	-0.104	-0.052	15.458	-0.273	-0.273	0.000	0.000	0.000	0.000
183	A	192	ARG	0	0.008	0.023	17.066	0.714	0.714	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:10:GLY)