FMO DATABASE

FMODB ID: 4QKZN

Calculation Name: 1IM5-A-Xray547

Preferred Name:

Target Type:

Ligand Name: zinc ion

Ligand 3-letter code: ZN

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1IM5

Chain ID: A

ChEMBL ID:

UniProt ID: O58727

Base Structure: X-ray

Registration Date: 2025-10-03

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	179
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1964006.893862
FMO2-HF: Nuclear repulsion	1893739.223752
FMO2-HF: Total energy	-70267.67011
FMO2-MP2: Total energy	-70473.148533

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:2:PRO)

Summations of interaction energy for fragment #1(A:2:PRO)

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.
-97.71	-88.16	16.274	-11.269	-14.554	-0.12

Interaction energy analysis for fragmet #1(A:2:PRO)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.817 / q_NPA : 0.900

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	4	GLU	-1	-0.879	-0.931	2.997	-35.558	-33.425	0.029	-0.915	-1.247	-0.001
4	A	5	ALA	0	0.032	0.010	2.747	-13.026	-11.040	0.398	-1.129	-1.255	-0.014
43	A	44	GLY	0	0.009	0.022	4.682	-2.620	-2.485	-0.001	-0.027	-0.107	0.000
44	A	45	ALA	0	-0.057	-0.031	2.383	-19.140	-16.242	3.219	-2.711	-3.406	-0.027
45	A	46	LEU	0	-0.004	-0.004	2.338	-0.999	0.466	2.132	-0.580	-3.017	-0.012
46	A	47	ILE	0	0.013	0.008	3.351	5.476	5.535	0.040	0.085	-0.184	0.000
117	A	118	ASN	0	-0.038	-0.023	2.703	-6.190	-4.577	0.481	-0.792	-1.301	-0.005
118	A	119	GLY	0	-0.009	-0.001	1.798	-39.317	-40.928	9.928	-4.976	-3.341	-0.060
119	A	120	VAL	0	-0.076	-0.023	3.112	-0.388	0.318	0.049	-0.208	-0.548	-0.001
120	A	121	LYS	1	0.841	0.896	4.914	40.902	41.068	-0.001	-0.016	-0.148	0.000
5	A	6	LEU	0	-0.027	0.005	5.460	4.434	4.434	0.000	0.000	0.000	0.000
6	A	7	ILE	0	-0.008	-0.020	8.711	-0.749	-0.749	0.000	0.000	0.000	0.000
7	A	8	VAL	0	0.022	-0.005	11.625	1.444	1.444	0.000	0.000	0.000	0.000
8	A	9	VAL	0	-0.012	-0.017	14.462	0.135	0.135	0.000	0.000	0.000	0.000
9	A	10	ASP	-1	-0.713	-0.833	17.393	-14.228	-14.228	0.000	0.000	0.000	0.000
10	A	11	MET	0	0.008	0.037	18.526	0.831	0.831	0.000	0.000	0.000	0.000
11	A	12	GLN	0	-0.040	-0.047	20.508	-0.198	-0.198	0.000	0.000	0.000	0.000
12	A	13	ARG	1	0.850	0.902	23.220	11.464	11.464	0.000	0.000	0.000	0.000
13	A	14	ASP	-1	-0.771	-0.901	26.618	-9.913	-9.913	0.000	0.000	0.000	0.000
14	A	15	PHE	0	-0.030	-0.007	24.204	0.358	0.358	0.000	0.000	0.000	0.000
15	A	16	MET	0	0.007	0.026	23.779	-0.063	-0.063	0.000	0.000	0.000	0.000
16	A	17	PRO	0	-0.040	-0.026	28.019	0.347	0.347	0.000	0.000	0.000	0.000
17	A	18	GLY	0	-0.006	0.000	31.569	-0.018	-0.018	0.000	0.000	0.000	0.000
18	A	19	GLY	0	-0.019	0.013	30.652	0.110	0.110	0.000	0.000	0.000	0.000
19	A	20	ALA	0	-0.019	-0.022	31.682	0.235	0.235	0.000	0.000	0.000	0.000
20	A	21	LEU	0	-0.085	-0.053	29.750	0.286	0.286	0.000	0.000	0.000	0.000
21	A	22	PRO	0	-0.046	0.006	30.113	-0.340	-0.340	0.000	0.000	0.000	0.000
22	A	23	VAL	0	0.022	-0.001	26.557	0.206	0.206	0.000	0.000	0.000	0.000
23	A	24	PRO	0	-0.007	-0.009	29.514	0.001	0.001	0.000	0.000	0.000	0.000
24	A	25	GLU	-1	-0.907	-0.979	29.751	-9.934	-9.934	0.000	0.000	0.000	0.000
25	A	26	GLY	0	0.024	0.017	26.184	-0.277	-0.277	0.000	0.000	0.000	0.000
26	A	27	ASP	-1	-0.823	-0.945	24.891	-10.867	-10.867	0.000	0.000	0.000	0.000
27	A	28	LYS	1	0.881	0.947	25.480	9.422	9.422	0.000	0.000	0.000	0.000
28	A	29	ILE	0	-0.007	0.013	20.893	-0.120	-0.120	0.000	0.000	0.000	0.000
29	A	30	ILE	0	0.011	0.020	20.889	-0.712	-0.712	0.000	0.000	0.000	0.000
30	A	31	PRO	0	-0.018	-0.010	20.087	-0.686	-0.686	0.000	0.000	0.000	0.000
31	A	32	LYS	1	0.862	0.933	18.346	14.392	14.392	0.000	0.000	0.000	0.000
32	A	33	VAL	0	0.043	0.015	15.917	-1.034	-1.034	0.000	0.000	0.000	0.000
33	A	34	ASN	0	0.039	0.008	15.286	-1.675	-1.675	0.000	0.000	0.000	0.000
34	A	35	GLU	-1	-0.903	-0.924	15.558	-16.057	-16.057	0.000	0.000	0.000	0.000
35	A	36	TYR	0	-0.031	-0.044	12.670	-1.200	-1.200	0.000	0.000	0.000	0.000
36	A	37	ILE	0	0.012	0.005	11.062	-2.137	-2.137	0.000	0.000	0.000	0.000
37	A	38	ARG	1	0.891	0.954	10.662	14.586	14.586	0.000	0.000	0.000	0.000
38	A	39	LYS	1	0.896	0.928	11.263	16.258	16.258	0.000	0.000	0.000	0.000
39	A	40	PHE	0	-0.037	-0.035	6.349	-0.841	-0.841	0.000	0.000	0.000	0.000
40	A	41	LYS	1	0.989	1.007	6.706	18.003	18.003	0.000	0.000	0.000	0.000
41	A	42	GLU	-1	-0.970	-0.990	7.810	-21.434	-21.434	0.000	0.000	0.000	0.000
42	A	43	LYS	1	0.864	0.949	6.476	29.152	29.152	0.000	0.000	0.000	0.000
47	A	48	VAL	0	-0.009	0.001	7.114	0.134	0.134	0.000	0.000	0.000	0.000
48	A	49	ALA	0	0.023	0.020	9.988	1.020	1.020	0.000	0.000	0.000	0.000
49	A	50	THR	0	-0.051	-0.053	13.686	-0.106	-0.106	0.000	0.000	0.000	0.000
50	A	51	ARG	1	0.901	0.954	16.303	15.292	15.292	0.000	0.000	0.000	0.000
51	A	52	ASP	-1	-0.746	-0.839	19.883	-12.462	-12.462	0.000	0.000	0.000	0.000
52	A	53	TRP	0	0.011	-0.002	22.206	0.039	0.039	0.000	0.000	0.000	0.000
53	A	54	HIS	1	0.873	0.943	24.235	11.440	11.440	0.000	0.000	0.000	0.000
54	A	55	PRO	0	0.016	0.031	27.678	0.024	0.024	0.000	0.000	0.000	0.000
55	A	56	GLU	-1	-0.734	-0.855	30.603	-8.998	-8.998	0.000	0.000	0.000	0.000
56	A	57	ASN	0	-0.065	-0.047	34.044	0.002	0.002	0.000	0.000	0.000	0.000
57	A	58	HIS	0	0.024	0.032	28.696	0.215	0.215	0.000	0.000	0.000	0.000
58	A	59	ILE	0	-0.004	-0.004	31.639	0.217	0.217	0.000	0.000	0.000	0.000
59	A	60	SER	0	-0.034	-0.025	30.549	0.191	0.191	0.000	0.000	0.000	0.000
60	A	61	PHE	0	-0.016	-0.013	30.634	0.083	0.083	0.000	0.000	0.000	0.000
61	A	62	ARG	1	0.906	0.947	35.173	8.514	8.514	0.000	0.000	0.000	0.000
62	A	63	GLU	-1	-0.890	-0.935	37.383	-8.220	-8.220	0.000	0.000	0.000	0.000
63	A	64	ARG	1	0.768	0.872	35.226	8.837	8.837	0.000	0.000	0.000	0.000
64	A	65	GLY	0	-0.013	-0.001	39.571	0.017	0.017	0.000	0.000	0.000	0.000
65	A	66	GLY	0	0.012	0.026	35.819	-0.020	-0.020	0.000	0.000	0.000	0.000
66	A	67	PRO	0	0.005	-0.019	33.831	0.152	0.152	0.000	0.000	0.000	0.000
67	A	68	TRP	0	-0.008	0.010	30.367	0.262	0.262	0.000	0.000	0.000	0.000
68	A	69	PRO	0	0.006	0.013	33.675	0.226	0.226	0.000	0.000	0.000	0.000
69	A	70	ARG	1	0.839	0.886	33.327	8.759	8.759	0.000	0.000	0.000	0.000
70	A	71	HIS	1	0.811	0.899	27.494	10.726	10.726	0.000	0.000	0.000	0.000
71	A	72	CYS	0	-0.061	-0.031	24.966	-0.026	-0.026	0.000	0.000	0.000	0.000
72	A	73	VAL	0	-0.018	0.015	27.058	-0.272	-0.272	0.000	0.000	0.000	0.000
73	A	74	GLN	0	-0.033	-0.021	26.235	0.148	0.148	0.000	0.000	0.000	0.000
74	A	75	ASN	0	-0.026	-0.029	26.681	0.018	0.018	0.000	0.000	0.000	0.000
75	A	76	THR	0	-0.031	-0.013	28.182	0.375	0.375	0.000	0.000	0.000	0.000
76	A	77	PRO	0	0.055	0.009	28.042	-0.343	-0.343	0.000	0.000	0.000	0.000
77	A	78	GLY	0	0.028	0.027	28.204	-0.163	-0.163	0.000	0.000	0.000	0.000
78	A	79	ALA	0	-0.009	-0.004	25.150	-0.306	-0.306	0.000	0.000	0.000	0.000
79	A	80	GLU	-1	-0.838	-0.891	23.408	-11.904	-11.904	0.000	0.000	0.000	0.000
80	A	81	PHE	0	-0.004	-0.012	17.199	0.119	0.119	0.000	0.000	0.000	0.000
81	A	82	VAL	0	-0.045	-0.025	21.181	0.448	0.448	0.000	0.000	0.000	0.000
82	A	83	VAL	0	-0.015	-0.013	17.001	0.132	0.132	0.000	0.000	0.000	0.000
83	A	84	ASP	-1	-0.897	-0.947	17.223	-14.699	-14.699	0.000	0.000	0.000	0.000
84	A	85	LEU	0	-0.051	-0.031	12.707	-1.141	-1.141	0.000	0.000	0.000	0.000
85	A	86	PRO	0	-0.034	-0.009	9.927	1.102	1.102	0.000	0.000	0.000	0.000
86	A	87	GLU	-1	-0.914	-0.969	12.358	-18.029	-18.029	0.000	0.000	0.000	0.000
87	A	88	ASP	-1	-0.938	-0.964	7.769	-30.309	-30.309	0.000	0.000	0.000	0.000
88	A	89	ALA	0	-0.052	-0.015	8.197	-3.140	-3.140	0.000	0.000	0.000	0.000
89	A	90	VAL	0	-0.012	-0.021	7.822	1.685	1.685	0.000	0.000	0.000	0.000
90	A	91	ILE	0	0.009	0.003	10.689	0.703	0.703	0.000	0.000	0.000	0.000
91	A	92	ILE	0	-0.039	-0.016	12.000	0.606	0.606	0.000	0.000	0.000	0.000
92	A	93	SER	0	-0.002	-0.010	15.325	0.905	0.905	0.000	0.000	0.000	0.000
93	A	94	LYS	1	0.802	0.906	19.157	14.211	14.211	0.000	0.000	0.000	0.000
94	A	95	ALA	0	0.008	-0.002	21.097	0.428	0.428	0.000	0.000	0.000	0.000
95	A	96	THR	0	0.013	0.007	22.893	0.471	0.471	0.000	0.000	0.000	0.000
96	A	97	GLU	-1	-0.812	-0.888	25.710	-11.011	-11.011	0.000	0.000	0.000	0.000
97	A	98	PRO	0	0.015	-0.012	28.528	-0.058	-0.058	0.000	0.000	0.000	0.000
98	A	99	ASP	-1	-0.806	-0.894	31.623	-8.940	-8.940	0.000	0.000	0.000	0.000
99	A	100	LYS	1	0.830	0.906	26.808	11.362	11.362	0.000	0.000	0.000	0.000
100	A	101	GLU	-1	-0.831	-0.928	27.203	-11.275	-11.275	0.000	0.000	0.000	0.000
101	A	102	ALA	0	-0.036	-0.017	22.142	-0.195	-0.195	0.000	0.000	0.000	0.000
102	A	103	TYR	0	0.014	0.008	23.403	-0.029	-0.029	0.000	0.000	0.000	0.000
103	A	104	SER	0	-0.019	-0.058	18.706	-0.857	-0.857	0.000	0.000	0.000	0.000
104	A	105	GLY	0	0.016	-0.006	15.860	0.184	0.184	0.000	0.000	0.000	0.000
105	A	106	PHE	0	-0.047	-0.030	12.184	-1.054	-1.054	0.000	0.000	0.000	0.000
106	A	107	GLU	-1	-0.840	-0.912	16.940	-12.836	-12.836	0.000	0.000	0.000	0.000
107	A	108	GLY	0	-0.016	0.001	20.684	0.251	0.251	0.000	0.000	0.000	0.000
108	A	109	THR	0	-0.030	-0.030	15.872	-0.379	-0.379	0.000	0.000	0.000	0.000
109	A	110	ASP	-1	-0.866	-0.933	14.288	-18.369	-18.369	0.000	0.000	0.000	0.000
110	A	111	LEU	0	0.006	0.017	9.921	-1.929	-1.929	0.000	0.000	0.000	0.000
111	A	112	ALA	0	0.023	0.002	10.355	-2.553	-2.553	0.000	0.000	0.000	0.000
112	A	113	LYS	1	0.906	0.942	11.143	18.667	18.667	0.000	0.000	0.000	0.000
113	A	114	ILE	0	0.043	0.026	7.470	-2.091	-2.091	0.000	0.000	0.000	0.000
114	A	115	LEU	0	0.018	0.018	6.022	-5.184	-5.184	0.000	0.000	0.000	0.000
115	A	116	ARG	1	0.859	0.923	5.692	16.804	16.804	0.000	0.000	0.000	0.000
116	A	117	GLY	0	-0.010	0.004	6.871	-1.803	-1.803	0.000	0.000	0.000	0.000
121	A	122	ARG	1	0.837	0.918	6.232	40.169	40.169	0.000	0.000	0.000	0.000
122	A	123	VAL	0	0.003	-0.010	7.073	-3.998	-3.998	0.000	0.000	0.000	0.000
123	A	124	TYR	0	0.013	0.006	8.229	2.164	2.164	0.000	0.000	0.000	0.000
124	A	125	ILE	0	-0.013	0.007	11.065	-0.673	-0.673	0.000	0.000	0.000	0.000
125	A	126	CYS	0	-0.038	-0.007	13.962	0.922	0.922	0.000	0.000	0.000	0.000
126	A	127	GLY	0	0.037	0.016	16.306	-0.442	-0.442	0.000	0.000	0.000	0.000
127	A	128	VAL	0	-0.003	-0.005	19.150	0.571	0.571	0.000	0.000	0.000	0.000
128	A	129	ALA	0	0.032	0.014	21.955	-0.276	-0.276	0.000	0.000	0.000	0.000
129	A	130	THR	0	-0.009	-0.035	22.755	-0.464	-0.464	0.000	0.000	0.000	0.000
130	A	131	GLU	-1	-0.732	-0.889	23.477	-11.467	-11.467	0.000	0.000	0.000	0.000
131	A	132	TYR	0	-0.029	-0.009	25.371	0.222	0.222	0.000	0.000	0.000	0.000
132	A	133	CYS	0	-0.001	-0.002	20.994	-0.089	-0.089	0.000	0.000	0.000	0.000
133	A	134	VAL	0	-0.025	0.029	18.735	-0.862	-0.862	0.000	0.000	0.000	0.000
134	A	135	ARG	1	0.881	0.902	19.307	11.118	11.118	0.000	0.000	0.000	0.000
135	A	136	ALA	0	-0.009	-0.001	21.064	-0.294	-0.294	0.000	0.000	0.000	0.000
136	A	137	THR	0	0.020	-0.009	14.948	-0.518	-0.518	0.000	0.000	0.000	0.000
137	A	138	ALA	0	0.003	-0.002	16.297	-1.123	-1.123	0.000	0.000	0.000	0.000
138	A	139	LEU	0	-0.012	-0.015	17.604	-0.384	-0.384	0.000	0.000	0.000	0.000
139	A	140	ASP	-1	-0.776	-0.853	17.701	-15.008	-15.008	0.000	0.000	0.000	0.000
140	A	141	ALA	0	-0.012	-0.008	13.395	-0.641	-0.641	0.000	0.000	0.000	0.000
141	A	142	LEU	0	-0.006	-0.001	14.846	-0.798	-0.798	0.000	0.000	0.000	0.000
142	A	143	LYS	1	0.820	0.910	17.338	14.170	14.170	0.000	0.000	0.000	0.000
143	A	144	HIS	0	-0.014	-0.006	13.883	-0.254	-0.254	0.000	0.000	0.000	0.000
144	A	145	GLY	0	0.019	0.020	14.218	-1.099	-1.099	0.000	0.000	0.000	0.000
145	A	146	PHE	0	-0.060	-0.018	8.893	-0.765	-0.765	0.000	0.000	0.000	0.000
146	A	147	GLU	-1	-0.874	-0.936	11.622	-20.201	-20.201	0.000	0.000	0.000	0.000
147	A	148	VAL	0	-0.018	-0.005	11.654	-1.724	-1.724	0.000	0.000	0.000	0.000
148	A	149	TYR	0	-0.045	-0.043	11.629	1.956	1.956	0.000	0.000	0.000	0.000
149	A	150	LEU	0	-0.017	-0.005	14.285	-0.553	-0.553	0.000	0.000	0.000	0.000
150	A	151	LEU	0	0.015	0.004	12.409	0.435	0.435	0.000	0.000	0.000	0.000
151	A	152	ARG	1	0.961	0.972	16.696	12.536	12.536	0.000	0.000	0.000	0.000
152	A	153	ASP	-1	-0.808	-0.892	19.166	-14.446	-14.446	0.000	0.000	0.000	0.000
153	A	154	ALA	0	-0.014	-0.011	17.353	0.214	0.214	0.000	0.000	0.000	0.000
154	A	155	VAL	0	0.004	0.007	18.957	-0.529	-0.529	0.000	0.000	0.000	0.000
155	A	156	LYS	1	0.893	0.963	21.336	11.276	11.276	0.000	0.000	0.000	0.000
156	A	157	GLY	0	0.008	-0.002	24.868	-0.380	-0.380	0.000	0.000	0.000	0.000
157	A	158	ILE	0	-0.044	-0.032	27.272	0.216	0.216	0.000	0.000	0.000	0.000
158	A	159	LYS	1	0.886	0.933	30.864	9.378	9.378	0.000	0.000	0.000	0.000
159	A	160	PRO	0	0.066	0.039	31.641	-0.198	-0.198	0.000	0.000	0.000	0.000
160	A	161	GLU	-1	-0.843	-0.914	32.009	-8.691	-8.691	0.000	0.000	0.000	0.000
161	A	162	ASP	-1	-0.870	-0.931	31.182	-9.356	-9.356	0.000	0.000	0.000	0.000
162	A	163	GLU	-1	-0.889	-0.956	27.499	-11.269	-11.269	0.000	0.000	0.000	0.000
163	A	164	GLU	-1	-0.926	-0.968	27.658	-9.725	-9.725	0.000	0.000	0.000	0.000
164	A	165	ARG	1	0.882	0.935	28.886	8.732	8.732	0.000	0.000	0.000	0.000
165	A	166	ALA	0	0.008	0.018	25.588	-0.224	-0.224	0.000	0.000	0.000	0.000
166	A	167	LEU	0	-0.019	-0.023	22.577	-0.581	-0.581	0.000	0.000	0.000	0.000
167	A	168	GLU	-1	-0.948	-0.960	24.841	-10.240	-10.240	0.000	0.000	0.000	0.000
168	A	169	GLU	-1	-0.778	-0.853	26.211	-11.771	-11.771	0.000	0.000	0.000	0.000
169	A	170	MET	0	-0.005	0.003	21.142	-0.574	-0.574	0.000	0.000	0.000	0.000
170	A	171	LYS	1	0.972	0.988	22.312	11.469	11.469	0.000	0.000	0.000	0.000
171	A	172	SER	0	-0.088	-0.049	23.696	-0.083	-0.083	0.000	0.000	0.000	0.000
172	A	173	ARG	1	0.872	0.930	22.912	12.508	12.508	0.000	0.000	0.000	0.000
173	A	174	GLY	0	0.028	0.021	21.318	-0.476	-0.476	0.000	0.000	0.000	0.000
174	A	175	ILE	0	-0.033	-0.008	17.084	-0.940	-0.940	0.000	0.000	0.000	0.000
175	A	176	LYS	1	0.856	0.929	16.161	18.269	18.269	0.000	0.000	0.000	0.000
176	A	177	ILE	0	-0.022	-0.006	17.044	-0.712	-0.712	0.000	0.000	0.000	0.000
177	A	178	VAL	0	-0.034	-0.016	14.832	0.455	0.455	0.000	0.000	0.000	0.000
178	A	179	GLN	0	-0.028	-0.023	17.229	0.336	0.336	0.000	0.000	0.000	0.000
179	A	180	PHE	-1	-0.842	-0.895	11.533	-17.387	-17.387	0.000	0.000	0.000	0.000

Top

Graph

Overview

Highlights

Data Search

Manual

Support

Interactive mode: IFIE and PIEDA for fragment #1(A:2:PRO)