FMO DATABASE

FMODB ID: 6Z54Z

Calculation Name: 1EPF-A-Xray547

Preferred Name:

Target Type:

Ligand Name: calcium ion

Ligand 3-letter code: CA

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1EPF

Chain ID: A

ChEMBL ID:

UniProt ID: P13596

Base Structure: X-ray

Registration Date: 2025-09-02

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	187
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1771374.87648
FMO2-HF: Nuclear repulsion	1697506.204179
FMO2-HF: Total energy	-73868.672301
FMO2-MP2: Total energy	-74084.995222

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:LEU)

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

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.
-156.598	-150.059	6.931	-3.846	-9.625	-0.025

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.846 / q_NPA : 0.920

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	VAL	0	0.025	0.015	3.036	-1.053	1.797	0.112	-1.141	-1.821	-0.005
4	A	4	ASP	-1	-0.883	-0.941	5.037	-22.967	-22.937	-0.001	-0.003	-0.026	0.000
24	A	24	VAL	0	0.042	0.021	2.379	-3.767	-3.949	1.814	-0.345	-1.287	-0.004
25	A	25	ALA	0	-0.068	-0.035	3.871	3.336	3.548	0.001	-0.043	-0.171	0.000
26	A	26	GLY	0	0.001	0.004	4.505	-4.040	-3.864	-0.001	-0.013	-0.162	0.000
29	A	29	LYS	1	0.828	0.919	4.725	37.149	37.239	-0.001	-0.003	-0.086	0.000
31	A	31	LYS	1	0.825	0.883	3.120	27.301	27.779	0.032	-0.077	-0.433	0.000
78	A	79	VAL	0	0.007	0.003	2.345	0.327	0.766	1.527	-0.385	-1.581	-0.002
79	A	80	THR	0	-0.016	-0.011	3.133	-5.916	-4.747	0.210	-0.633	-0.746	-0.006
80	A	81	ALA	0	-0.012	-0.011	2.638	0.742	1.231	0.293	-0.176	-0.606	-0.002
81	A	82	GLU	-1	-0.895	-0.954	4.576	-25.791	-25.753	-0.001	-0.010	-0.027	0.000
85	A	86	GLN	0	-0.008	-0.016	3.571	-0.332	-0.081	0.007	-0.053	-0.206	0.000
86	A	87	SER	0	-0.036	-0.008	2.335	-5.584	-5.218	2.938	-1.102	-2.202	-0.006
87	A	88	GLU	-1	-0.835	-0.905	3.575	-21.608	-21.475	0.001	0.138	-0.271	0.000
5	A	5	ILE	0	-0.046	-0.025	8.853	0.684	0.684	0.000	0.000	0.000	0.000
6	A	6	VAL	0	-0.008	0.029	12.056	1.074	1.074	0.000	0.000	0.000	0.000
7	A	7	PRO	0	-0.041	-0.037	15.380	0.421	0.421	0.000	0.000	0.000	0.000
8	A	8	SER	0	0.088	0.025	14.784	0.281	0.281	0.000	0.000	0.000	0.000
9	A	9	GLN	0	-0.056	-0.026	16.148	-0.130	-0.130	0.000	0.000	0.000	0.000
10	A	10	GLY	0	0.001	-0.003	19.203	0.240	0.240	0.000	0.000	0.000	0.000
11	A	11	GLU	-1	-0.977	-0.969	21.931	-10.436	-10.436	0.000	0.000	0.000	0.000
12	A	12	ILE	0	0.000	0.000	23.362	-0.050	-0.050	0.000	0.000	0.000	0.000
13	A	13	SER	0	-0.024	-0.021	27.342	0.110	0.110	0.000	0.000	0.000	0.000
14	A	14	VAL	0	-0.009	-0.006	30.655	-0.125	-0.125	0.000	0.000	0.000	0.000
15	A	15	GLY	0	-0.022	-0.001	31.953	0.257	0.257	0.000	0.000	0.000	0.000
16	A	16	GLU	-1	-0.913	-0.939	30.478	-9.190	-9.190	0.000	0.000	0.000	0.000
17	A	17	SER	0	-0.041	-0.042	26.545	-0.043	-0.043	0.000	0.000	0.000	0.000
18	A	18	LYS	1	0.855	0.928	22.270	12.095	12.095	0.000	0.000	0.000	0.000
19	A	19	PHE	0	0.000	0.022	18.559	0.128	0.128	0.000	0.000	0.000	0.000
20	A	20	PHE	0	0.002	-0.017	16.034	0.321	0.321	0.000	0.000	0.000	0.000
21	A	21	LEU	0	0.031	0.033	12.690	-0.082	-0.082	0.000	0.000	0.000	0.000
22	A	22	CYS	0	-0.037	-0.001	8.457	-0.646	-0.646	0.000	0.000	0.000	0.000
23	A	23	GLN	0	0.035	0.010	8.675	-0.120	-0.120	0.000	0.000	0.000	0.000
27	A	27	ASP	-1	-0.864	-0.951	5.408	-40.006	-40.006	0.000	0.000	0.000	0.000
28	A	28	ALA	0	-0.043	-0.022	7.635	-0.134	-0.134	0.000	0.000	0.000	0.000
30	A	30	ASP	-1	-0.917	-0.938	7.483	-23.544	-23.544	0.000	0.000	0.000	0.000
32	A	32	ASP	-1	-0.846	-0.876	6.570	-20.132	-20.132	0.000	0.000	0.000	0.000
33	A	33	ILE	0	-0.026	-0.016	5.981	-3.507	-3.507	0.000	0.000	0.000	0.000
34	A	34	SER	0	-0.045	-0.046	7.840	3.079	3.079	0.000	0.000	0.000	0.000
35	A	35	TRP	0	-0.016	-0.029	9.953	-1.058	-1.058	0.000	0.000	0.000	0.000
36	A	36	PHE	0	-0.029	-0.019	10.710	0.668	0.668	0.000	0.000	0.000	0.000
37	A	37	SER	0	0.036	0.007	14.816	-0.383	-0.383	0.000	0.000	0.000	0.000
38	A	38	PRO	0	-0.035	-0.016	18.058	-0.289	-0.289	0.000	0.000	0.000	0.000
39	A	39	ASN	0	-0.058	-0.034	19.911	-0.434	-0.434	0.000	0.000	0.000	0.000
40	A	40	GLY	0	-0.001	0.003	17.516	0.250	0.250	0.000	0.000	0.000	0.000
41	A	41	GLU	-1	-0.899	-0.923	17.769	-12.280	-12.280	0.000	0.000	0.000	0.000
42	A	42	LYS	1	0.923	0.964	12.118	18.039	18.039	0.000	0.000	0.000	0.000
43	A	43	LEU	0	-0.032	-0.021	15.823	0.708	0.708	0.000	0.000	0.000	0.000
44	A	44	SER	0	0.012	0.004	15.661	-0.816	-0.816	0.000	0.000	0.000	0.000
45	A	45	PRO	0	0.011	-0.002	15.671	0.452	0.452	0.000	0.000	0.000	0.000
46	A	46	ASN	0	-0.050	-0.034	18.169	1.088	1.088	0.000	0.000	0.000	0.000
47	A	47	GLN	0	0.012	0.009	21.542	-0.565	-0.565	0.000	0.000	0.000	0.000
48	A	48	GLN	0	0.016	0.016	23.912	0.643	0.643	0.000	0.000	0.000	0.000
49	A	49	ARG	1	0.772	0.837	24.793	10.208	10.208	0.000	0.000	0.000	0.000
50	A	50	ILE	0	-0.007	0.005	20.498	-0.097	-0.097	0.000	0.000	0.000	0.000
51	A	51	SER	0	-0.029	0.001	21.325	-0.145	-0.145	0.000	0.000	0.000	0.000
52	A	52	VAL	0	0.023	0.000	15.062	-0.499	-0.499	0.000	0.000	0.000	0.000
53	A	53	VAL	0	-0.023	-0.011	16.877	0.526	0.526	0.000	0.000	0.000	0.000
54	A	54	TRP	0	0.020	0.025	11.513	0.211	0.211	0.000	0.000	0.000	0.000
55	A	55	ASN	0	-0.052	-0.017	13.302	0.532	0.532	0.000	0.000	0.000	0.000
56	A	56	ASP	-1	-0.780	-0.882	11.063	-19.895	-19.895	0.000	0.000	0.000	0.000
57	A	57	ASP	-1	-0.891	-0.951	9.750	-20.339	-20.339	0.000	0.000	0.000	0.000
58	A	58	ASP	-1	-0.882	-0.920	6.637	-31.832	-31.832	0.000	0.000	0.000	0.000
59	A	59	SER	0	-0.050	-0.054	7.221	-1.330	-1.330	0.000	0.000	0.000	0.000
60	A	60	SER	0	0.029	0.009	9.805	1.694	1.694	0.000	0.000	0.000	0.000
61	A	61	THR	0	-0.027	-0.020	12.205	-0.479	-0.479	0.000	0.000	0.000	0.000
62	A	62	LEU	0	0.024	0.041	15.353	0.604	0.604	0.000	0.000	0.000	0.000
63	A	63	THR	0	-0.078	-0.067	16.961	0.311	0.311	0.000	0.000	0.000	0.000
64	A	64	ILE	0	0.014	0.032	20.752	0.261	0.261	0.000	0.000	0.000	0.000
65	A	65	TYR	0	0.016	-0.011	23.355	0.144	0.144	0.000	0.000	0.000	0.000
66	A	66	ASN	0	-0.053	-0.032	26.853	0.117	0.117	0.000	0.000	0.000	0.000
67	A	67	ALA	0	0.026	0.027	27.294	0.034	0.034	0.000	0.000	0.000	0.000
68	A	68	ASN	0	-0.008	-0.015	28.531	0.482	0.482	0.000	0.000	0.000	0.000
69	A	69	ILE	0	0.022	-0.015	28.589	-0.279	-0.279	0.000	0.000	0.000	0.000
70	A	70	ASP	-1	-0.909	-0.941	28.258	-9.764	-9.764	0.000	0.000	0.000	0.000
71	A	71	ASP	-1	-0.745	-0.824	24.590	-11.111	-11.111	0.000	0.000	0.000	0.000
72	A	72	ALA	0	-0.014	-0.005	23.625	-0.544	-0.544	0.000	0.000	0.000	0.000
73	A	73	GLY	0	0.010	0.007	22.460	0.017	0.017	0.000	0.000	0.000	0.000
74	A	74	ILE	0	-0.040	-0.029	16.361	-0.177	-0.177	0.000	0.000	0.000	0.000
75	A	75	TYR	0	0.008	-0.010	15.883	0.029	0.029	0.000	0.000	0.000	0.000
76	A	76	LYS	1	0.808	0.879	10.491	21.059	21.059	0.000	0.000	0.000	0.000
77	A	78	VAL	0	0.001	-0.011	6.725	-1.873	-1.873	0.000	0.000	0.000	0.000
82	A	83	ASP	-1	-0.964	-0.975	7.837	-25.954	-25.954	0.000	0.000	0.000	0.000
83	A	84	GLY	0	0.017	0.008	7.872	2.396	2.396	0.000	0.000	0.000	0.000
84	A	85	THR	0	-0.050	-0.010	4.878	-0.985	-0.985	0.000	0.000	0.000	0.000
88	A	89	ALA	0	0.012	0.019	6.764	-1.935	-1.935	0.000	0.000	0.000	0.000
89	A	90	THR	0	-0.015	-0.019	8.931	1.791	1.791	0.000	0.000	0.000	0.000
90	A	91	VAL	0	0.024	0.024	12.754	-0.018	-0.018	0.000	0.000	0.000	0.000
91	A	92	ASN	0	-0.041	-0.021	15.742	0.784	0.784	0.000	0.000	0.000	0.000
92	A	93	VAL	0	0.016	0.017	19.370	0.225	0.225	0.000	0.000	0.000	0.000
93	A	94	LYS	1	0.947	0.969	21.956	11.837	11.837	0.000	0.000	0.000	0.000
94	A	95	ILE	0	0.044	0.020	25.603	0.011	0.011	0.000	0.000	0.000	0.000
95	A	96	PHE	0	-0.010	-0.008	28.581	0.326	0.326	0.000	0.000	0.000	0.000
96	A	97	GLN	0	0.011	-0.012	31.425	0.090	0.090	0.000	0.000	0.000	0.000
97	A	98	LYS	1	0.979	0.999	34.945	8.444	8.444	0.000	0.000	0.000	0.000
98	A	99	LEU	0	0.032	0.022	36.757	0.126	0.126	0.000	0.000	0.000	0.000
99	A	100	MET	0	-0.060	-0.019	39.115	0.070	0.070	0.000	0.000	0.000	0.000
100	A	101	PHE	0	0.005	-0.008	42.355	0.045	0.045	0.000	0.000	0.000	0.000
101	A	102	LYS	1	0.925	0.980	42.129	7.032	7.032	0.000	0.000	0.000	0.000
102	A	103	ASN	0	-0.007	-0.020	44.447	0.072	0.072	0.000	0.000	0.000	0.000
103	A	104	ALA	0	0.004	-0.007	48.220	-0.009	-0.009	0.000	0.000	0.000	0.000
104	A	105	PRO	0	0.001	0.019	51.147	0.026	0.026	0.000	0.000	0.000	0.000
105	A	106	THR	0	0.030	0.030	53.998	0.088	0.088	0.000	0.000	0.000	0.000
106	A	107	PRO	0	0.026	0.001	56.879	-0.035	-0.035	0.000	0.000	0.000	0.000
107	A	108	GLN	0	-0.056	-0.037	55.121	-0.040	-0.040	0.000	0.000	0.000	0.000
108	A	109	GLU	-1	-0.928	-0.957	60.208	-4.787	-4.787	0.000	0.000	0.000	0.000
109	A	110	PHE	0	-0.008	-0.011	59.498	-0.060	-0.060	0.000	0.000	0.000	0.000
110	A	111	LYS	1	0.917	0.958	65.416	4.431	4.431	0.000	0.000	0.000	0.000
111	A	112	GLU	-1	-0.817	-0.909	69.119	-4.318	-4.318	0.000	0.000	0.000	0.000
112	A	113	GLY	0	-0.058	-0.034	71.065	0.056	0.056	0.000	0.000	0.000	0.000
113	A	114	GLU	-1	-0.898	-0.937	64.795	-4.796	-4.796	0.000	0.000	0.000	0.000
114	A	115	ASP	-1	-0.854	-0.926	64.391	-4.776	-4.776	0.000	0.000	0.000	0.000
115	A	116	ALA	0	0.031	0.038	62.833	-0.058	-0.058	0.000	0.000	0.000	0.000
116	A	117	VAL	0	-0.033	-0.037	56.677	-0.043	-0.043	0.000	0.000	0.000	0.000
117	A	118	ILE	0	-0.023	0.004	56.399	-0.034	-0.034	0.000	0.000	0.000	0.000
118	A	119	VAL	0	0.000	-0.002	51.801	-0.102	-0.102	0.000	0.000	0.000	0.000
119	A	120	CYS	0	-0.021	0.000	50.361	-0.033	-0.033	0.000	0.000	0.000	0.000
120	A	121	ASP	-1	-0.802	-0.855	45.802	-6.551	-6.551	0.000	0.000	0.000	0.000
121	A	122	VAL	0	-0.015	-0.018	43.873	-0.099	-0.099	0.000	0.000	0.000	0.000
122	A	123	VAL	0	-0.033	-0.019	39.909	-0.060	-0.060	0.000	0.000	0.000	0.000
123	A	124	SER	0	0.001	-0.034	38.315	-0.050	-0.050	0.000	0.000	0.000	0.000
124	A	125	SER	0	0.039	0.027	33.016	0.035	0.035	0.000	0.000	0.000	0.000
125	A	126	LEU	0	-0.036	-0.005	34.348	-0.111	-0.111	0.000	0.000	0.000	0.000
126	A	127	PRO	0	0.039	0.018	37.498	0.161	0.161	0.000	0.000	0.000	0.000
127	A	128	PRO	0	-0.020	0.011	41.026	0.020	0.020	0.000	0.000	0.000	0.000
128	A	129	THR	0	-0.052	-0.031	43.672	0.146	0.146	0.000	0.000	0.000	0.000
129	A	130	ILE	0	0.020	0.001	46.688	-0.038	-0.038	0.000	0.000	0.000	0.000
130	A	131	ILE	0	-0.047	-0.015	49.663	0.090	0.090	0.000	0.000	0.000	0.000
131	A	132	TRP	0	0.039	0.008	53.005	0.004	0.004	0.000	0.000	0.000	0.000
132	A	133	LYS	1	0.788	0.884	54.123	5.870	5.870	0.000	0.000	0.000	0.000
133	A	134	HIS	0	0.046	0.028	58.388	-0.008	-0.008	0.000	0.000	0.000	0.000
134	A	135	LYS	1	0.903	0.951	61.684	4.788	4.788	0.000	0.000	0.000	0.000
135	A	136	GLY	0	0.027	0.022	59.241	0.032	0.032	0.000	0.000	0.000	0.000
136	A	137	ARG	1	0.920	0.965	59.585	4.804	4.804	0.000	0.000	0.000	0.000
137	A	138	ASP	-1	-0.823	-0.920	57.322	-5.511	-5.511	0.000	0.000	0.000	0.000
138	A	139	VAL	0	0.049	0.013	58.597	0.115	0.115	0.000	0.000	0.000	0.000
139	A	140	ILE	0	0.024	0.015	58.173	0.109	0.109	0.000	0.000	0.000	0.000
140	A	141	LEU	0	-0.101	-0.053	61.582	0.102	0.102	0.000	0.000	0.000	0.000
141	A	142	LYS	1	0.806	0.906	64.003	4.959	4.959	0.000	0.000	0.000	0.000
142	A	143	LYS	1	0.911	0.957	65.326	4.824	4.824	0.000	0.000	0.000	0.000
143	A	144	ASP	-1	-0.786	-0.861	66.474	-4.575	-4.575	0.000	0.000	0.000	0.000
144	A	145	VAL	0	0.030	-0.005	65.629	-0.070	-0.070	0.000	0.000	0.000	0.000
145	A	146	ARG	1	0.693	0.811	65.560	4.617	4.617	0.000	0.000	0.000	0.000
146	A	147	PHE	0	-0.036	-0.015	61.944	-0.046	-0.046	0.000	0.000	0.000	0.000
147	A	148	ILE	0	-0.006	-0.001	58.506	-0.023	-0.023	0.000	0.000	0.000	0.000
148	A	149	VAL	0	-0.017	-0.005	53.461	-0.019	-0.019	0.000	0.000	0.000	0.000
149	A	150	LEU	0	0.009	0.011	54.541	-0.004	-0.004	0.000	0.000	0.000	0.000
150	A	151	SER	0	0.001	-0.011	50.571	-0.067	-0.067	0.000	0.000	0.000	0.000
151	A	152	ASN	0	0.014	0.006	48.815	-0.083	-0.083	0.000	0.000	0.000	0.000
152	A	153	ASN	0	-0.011	-0.012	46.748	-0.031	-0.031	0.000	0.000	0.000	0.000
153	A	154	TYR	0	0.000	-0.016	49.421	0.108	0.108	0.000	0.000	0.000	0.000
154	A	155	LEU	0	-0.008	0.008	53.859	0.029	0.029	0.000	0.000	0.000	0.000
155	A	156	GLN	0	0.009	0.005	57.242	0.053	0.053	0.000	0.000	0.000	0.000
156	A	157	ILE	0	-0.024	-0.016	60.217	0.006	0.006	0.000	0.000	0.000	0.000
157	A	158	ARG	1	0.892	0.938	63.555	4.955	4.955	0.000	0.000	0.000	0.000
158	A	159	GLY	0	0.014	-0.001	66.389	0.039	0.039	0.000	0.000	0.000	0.000
159	A	160	ILE	0	-0.071	-0.018	64.693	0.044	0.044	0.000	0.000	0.000	0.000
160	A	161	LYS	1	0.971	0.979	68.442	4.495	4.495	0.000	0.000	0.000	0.000
161	A	162	LYS	1	0.905	0.937	69.922	4.380	4.380	0.000	0.000	0.000	0.000
162	A	163	THR	0	-0.031	-0.029	70.733	-0.051	-0.051	0.000	0.000	0.000	0.000
163	A	164	ASP	-1	-0.791	-0.857	66.395	-4.692	-4.692	0.000	0.000	0.000	0.000
164	A	165	GLU	-1	-0.828	-0.889	65.896	-4.625	-4.625	0.000	0.000	0.000	0.000
165	A	166	GLY	0	-0.050	-0.032	64.980	0.021	0.021	0.000	0.000	0.000	0.000
166	A	167	THR	0	-0.036	-0.031	59.324	-0.025	-0.025	0.000	0.000	0.000	0.000
167	A	168	TYR	0	-0.024	-0.037	58.300	0.019	0.019	0.000	0.000	0.000	0.000
168	A	169	ARG	1	0.777	0.866	53.093	5.766	5.766	0.000	0.000	0.000	0.000
169	A	171	GLU	-1	-0.809	-0.924	50.067	-6.098	-6.098	0.000	0.000	0.000	0.000
170	A	172	GLY	0	0.043	0.024	46.316	0.021	0.021	0.000	0.000	0.000	0.000
171	A	173	ARG	1	0.952	0.964	45.391	6.428	6.428	0.000	0.000	0.000	0.000
172	A	174	ILE	0	0.045	0.028	39.061	0.041	0.041	0.000	0.000	0.000	0.000
173	A	175	LEU	0	-0.003	-0.008	42.086	-0.079	-0.079	0.000	0.000	0.000	0.000
174	A	176	ALA	0	0.000	-0.008	39.301	0.005	0.005	0.000	0.000	0.000	0.000
175	A	177	ARG	1	0.888	0.947	32.438	8.841	8.841	0.000	0.000	0.000	0.000
176	A	178	GLY	0	-0.007	0.013	39.681	-0.001	-0.001	0.000	0.000	0.000	0.000
177	A	179	GLU	-1	-0.863	-0.919	37.100	-8.234	-8.234	0.000	0.000	0.000	0.000
178	A	180	ILE	0	-0.026	-0.025	42.042	0.116	0.116	0.000	0.000	0.000	0.000
179	A	181	ASN	0	-0.033	-0.026	43.086	0.076	0.076	0.000	0.000	0.000	0.000
180	A	182	PHE	0	-0.032	-0.022	46.062	0.074	0.074	0.000	0.000	0.000	0.000
181	A	183	LYS	1	0.964	0.985	47.410	6.406	6.406	0.000	0.000	0.000	0.000
182	A	184	ASP	-1	-0.795	-0.855	51.483	-5.635	-5.635	0.000	0.000	0.000	0.000
183	A	185	ILE	0	-0.022	-0.019	53.548	-0.036	-0.036	0.000	0.000	0.000	0.000
184	A	186	GLN	0	0.001	0.013	57.213	0.019	0.019	0.000	0.000	0.000	0.000
185	A	187	VAL	0	0.019	0.013	60.400	-0.017	-0.017	0.000	0.000	0.000	0.000
186	A	188	ILE	0	-0.004	-0.009	62.541	0.060	0.060	0.000	0.000	0.000	0.000
187	A	189	VAL	-1	-0.836	-0.905	65.707	-4.534	-4.534	0.000	0.000	0.000	0.000

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