FMO DATABASE

FMODB ID: 2M2MR

Calculation Name: 1QNA-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1QNA

Chain ID: A

ChEMBL ID:

UniProt ID: P28147

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	182
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1820416.860962
FMO2-HF: Nuclear repulsion	1748927.348351
FMO2-HF: Total energy	-71489.51261
FMO2-MP2: Total energy	-71697.511369

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:17:HIS)

Summations of interaction energy for fragment #1(A:17:HIS)

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.
105.193	118.589	15.244	-10.197	-18.442	-0.08

Interaction energy analysis for fragmet #1(A:17:HIS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.805 / q_NPA : 0.889

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	19	SER	0	0.001	-0.016	2.809	7.193	10.151	0.054	-1.311	-1.700	-0.005
4	A	20	GLY	0	0.007	0.014	3.627	7.638	8.147	0.004	-0.210	-0.303	0.000
5	A	21	ILE	0	-0.043	-0.019	3.236	5.565	6.074	0.022	-0.153	-0.378	-0.001
6	A	22	VAL	0	0.011	-0.004	2.617	-17.598	-12.786	2.670	-2.294	-5.187	-0.008
7	A	23	PRO	0	-0.070	-0.031	2.879	4.850	5.478	0.169	-0.072	-0.725	0.000
166	A	182	TYR	0	-0.003	-0.007	2.427	-10.784	-8.188	5.138	-2.060	-5.675	-0.019
167	A	183	LYS	1	0.852	0.919	4.454	24.317	24.529	-0.001	-0.027	-0.183	0.000
169	A	185	PHE	0	0.010	-0.002	3.493	3.155	3.475	0.003	-0.052	-0.271	0.000
170	A	186	GLU	-1	-0.769	-0.875	2.183	-81.643	-80.791	7.185	-4.018	-4.020	-0.047
8	A	24	THR	0	0.016	0.023	5.750	-0.351	-0.351	0.000	0.000	0.000	0.000
9	A	25	LEU	0	0.013	-0.005	7.116	1.194	1.194	0.000	0.000	0.000	0.000
10	A	26	GLN	0	-0.011	-0.015	10.011	2.396	2.396	0.000	0.000	0.000	0.000
11	A	27	ASN	0	0.020	0.005	13.682	1.557	1.557	0.000	0.000	0.000	0.000
12	A	28	ILE	0	-0.015	0.024	11.720	-0.735	-0.735	0.000	0.000	0.000	0.000
13	A	29	VAL	0	0.007	0.005	15.699	0.946	0.946	0.000	0.000	0.000	0.000
14	A	30	SER	0	-0.003	-0.017	18.070	-0.299	-0.299	0.000	0.000	0.000	0.000
15	A	31	THR	0	0.001	0.003	20.029	0.488	0.488	0.000	0.000	0.000	0.000
16	A	32	VAL	0	-0.005	-0.002	23.253	-0.337	-0.337	0.000	0.000	0.000	0.000
17	A	33	ASN	0	-0.011	-0.013	25.933	0.391	0.391	0.000	0.000	0.000	0.000
18	A	34	LEU	0	0.023	0.006	29.518	-0.068	-0.068	0.000	0.000	0.000	0.000
19	A	35	ASP	-1	-0.895	-0.952	31.804	-8.407	-8.407	0.000	0.000	0.000	0.000
20	A	36	CYS	0	0.006	0.021	34.304	0.157	0.157	0.000	0.000	0.000	0.000
21	A	37	LYS	1	0.862	0.926	36.763	7.757	7.757	0.000	0.000	0.000	0.000
22	A	38	LEU	0	-0.023	-0.011	34.416	0.006	0.006	0.000	0.000	0.000	0.000
23	A	39	ASP	-1	-0.784	-0.878	38.949	-6.850	-6.850	0.000	0.000	0.000	0.000
24	A	40	LEU	0	-0.005	-0.018	36.133	-0.061	-0.061	0.000	0.000	0.000	0.000
25	A	41	LYS	1	0.904	0.963	39.596	6.929	6.929	0.000	0.000	0.000	0.000
26	A	42	ALA	0	0.082	0.038	42.716	0.012	0.012	0.000	0.000	0.000	0.000
27	A	43	ILE	0	-0.019	-0.013	36.284	-0.059	-0.059	0.000	0.000	0.000	0.000
28	A	44	ALA	0	-0.058	-0.040	38.945	-0.046	-0.046	0.000	0.000	0.000	0.000
29	A	45	LEU	0	0.010	0.022	39.893	0.012	0.012	0.000	0.000	0.000	0.000
30	A	46	GLN	0	0.003	0.015	41.284	0.094	0.094	0.000	0.000	0.000	0.000
31	A	47	ALA	0	-0.010	-0.004	36.448	-0.036	-0.036	0.000	0.000	0.000	0.000
32	A	48	ARG	1	0.874	0.920	37.594	7.265	7.265	0.000	0.000	0.000	0.000
33	A	49	ASN	0	-0.050	-0.026	31.677	0.211	0.211	0.000	0.000	0.000	0.000
34	A	50	ALA	0	0.006	-0.010	33.282	-0.318	-0.318	0.000	0.000	0.000	0.000
35	A	51	GLU	-1	-0.811	-0.886	33.545	-8.520	-8.520	0.000	0.000	0.000	0.000
36	A	52	TYR	0	0.020	-0.018	35.801	-0.078	-0.078	0.000	0.000	0.000	0.000
37	A	53	ASN	0	0.043	0.019	38.276	0.294	0.294	0.000	0.000	0.000	0.000
38	A	54	PRO	0	0.029	0.018	39.348	-0.139	-0.139	0.000	0.000	0.000	0.000
39	A	55	LYS	1	0.953	0.978	40.871	6.495	6.495	0.000	0.000	0.000	0.000
40	A	56	ARG	1	0.947	0.988	33.983	8.350	8.350	0.000	0.000	0.000	0.000
41	A	57	PHE	0	0.012	-0.012	30.735	-0.237	-0.237	0.000	0.000	0.000	0.000
42	A	58	ALA	0	0.026	0.015	35.367	0.150	0.150	0.000	0.000	0.000	0.000
43	A	59	ALA	0	-0.034	-0.015	32.557	0.008	0.008	0.000	0.000	0.000	0.000
44	A	60	VAL	0	-0.003	0.007	33.755	0.112	0.112	0.000	0.000	0.000	0.000
45	A	61	ILE	0	-0.021	0.003	30.012	-0.329	-0.329	0.000	0.000	0.000	0.000
46	A	62	MET	0	-0.004	0.007	30.403	0.181	0.181	0.000	0.000	0.000	0.000
47	A	63	ARG	1	0.873	0.924	28.233	9.201	9.201	0.000	0.000	0.000	0.000
48	A	64	ILE	0	-0.014	0.006	24.959	0.388	0.388	0.000	0.000	0.000	0.000
49	A	65	ARG	1	0.974	0.982	26.420	9.630	9.630	0.000	0.000	0.000	0.000
50	A	66	GLU	-1	-0.844	-0.908	23.237	-12.287	-12.287	0.000	0.000	0.000	0.000
51	A	67	PRO	0	-0.001	-0.008	19.900	0.363	0.363	0.000	0.000	0.000	0.000
52	A	68	LYS	1	1.007	1.016	21.903	11.862	11.862	0.000	0.000	0.000	0.000
53	A	69	THR	0	-0.031	-0.015	20.933	-0.359	-0.359	0.000	0.000	0.000	0.000
54	A	70	THR	0	-0.054	-0.027	23.372	0.600	0.600	0.000	0.000	0.000	0.000
55	A	71	ALA	0	0.003	0.020	24.700	-0.449	-0.449	0.000	0.000	0.000	0.000
56	A	72	LEU	0	-0.012	0.002	26.992	0.323	0.323	0.000	0.000	0.000	0.000
57	A	73	ILE	0	0.047	0.012	29.252	-0.201	-0.201	0.000	0.000	0.000	0.000
58	A	74	PHE	0	0.036	0.013	29.382	0.244	0.244	0.000	0.000	0.000	0.000
59	A	75	ALA	0	0.085	0.041	34.095	-0.015	-0.015	0.000	0.000	0.000	0.000
60	A	76	SER	0	0.003	0.001	33.905	0.077	0.077	0.000	0.000	0.000	0.000
61	A	77	GLY	0	0.071	0.051	34.289	0.036	0.036	0.000	0.000	0.000	0.000
62	A	78	LYS	1	0.876	0.946	29.702	9.216	9.216	0.000	0.000	0.000	0.000
63	A	79	MET	0	0.003	0.010	26.458	0.259	0.259	0.000	0.000	0.000	0.000
64	A	80	VAL	0	-0.006	0.001	23.611	-0.348	-0.348	0.000	0.000	0.000	0.000
65	A	81	CYS	0	-0.071	-0.031	21.836	0.383	0.383	0.000	0.000	0.000	0.000
66	A	82	THR	0	0.002	-0.013	20.386	-0.488	-0.488	0.000	0.000	0.000	0.000
67	A	83	GLY	0	0.057	0.017	19.564	0.463	0.463	0.000	0.000	0.000	0.000
68	A	84	ALA	0	-0.007	0.008	17.354	-0.235	-0.235	0.000	0.000	0.000	0.000
69	A	85	LYS	1	0.881	0.917	13.730	16.232	16.232	0.000	0.000	0.000	0.000
70	A	86	SER	0	0.060	0.031	12.197	-1.044	-1.044	0.000	0.000	0.000	0.000
71	A	87	GLU	-1	-0.730	-0.842	9.938	-22.143	-22.143	0.000	0.000	0.000	0.000
72	A	88	ASP	-1	-0.871	-0.926	14.232	-16.383	-16.383	0.000	0.000	0.000	0.000
73	A	89	PHE	0	-0.005	-0.021	15.659	1.121	1.121	0.000	0.000	0.000	0.000
74	A	90	SER	0	0.030	0.023	17.011	1.081	1.081	0.000	0.000	0.000	0.000
75	A	91	LYS	1	0.975	1.000	18.495	14.366	14.366	0.000	0.000	0.000	0.000
76	A	92	MET	0	-0.016	-0.012	20.025	0.548	0.548	0.000	0.000	0.000	0.000
77	A	93	ALA	0	-0.001	0.006	21.599	0.621	0.621	0.000	0.000	0.000	0.000
78	A	94	ALA	0	0.010	0.007	22.781	0.550	0.550	0.000	0.000	0.000	0.000
79	A	95	ARG	1	0.961	0.972	24.057	11.652	11.652	0.000	0.000	0.000	0.000
80	A	96	LYS	1	0.872	0.938	25.460	11.426	11.426	0.000	0.000	0.000	0.000
81	A	97	TYR	0	0.032	-0.011	24.874	0.521	0.521	0.000	0.000	0.000	0.000
82	A	98	ALA	0	0.021	0.010	28.666	0.324	0.324	0.000	0.000	0.000	0.000
83	A	99	ARG	1	0.971	0.987	30.381	9.263	9.263	0.000	0.000	0.000	0.000
84	A	100	ILE	0	-0.039	-0.017	31.205	0.272	0.272	0.000	0.000	0.000	0.000
85	A	101	VAL	0	0.020	0.005	33.221	0.243	0.243	0.000	0.000	0.000	0.000
86	A	102	GLN	0	-0.044	-0.034	33.229	0.160	0.160	0.000	0.000	0.000	0.000
87	A	103	LYS	1	0.911	0.951	35.927	8.156	8.156	0.000	0.000	0.000	0.000
88	A	104	LEU	0	-0.028	-0.001	37.365	0.137	0.137	0.000	0.000	0.000	0.000
89	A	105	GLY	0	0.037	0.034	39.919	0.136	0.136	0.000	0.000	0.000	0.000
90	A	106	PHE	0	0.029	0.014	37.826	0.079	0.079	0.000	0.000	0.000	0.000
91	A	107	PRO	0	0.056	0.032	38.188	-0.185	-0.185	0.000	0.000	0.000	0.000
92	A	108	ALA	0	-0.010	-0.016	33.497	-0.098	-0.098	0.000	0.000	0.000	0.000
93	A	109	LYS	1	0.870	0.934	32.216	8.104	8.104	0.000	0.000	0.000	0.000
94	A	110	PHE	0	-0.051	-0.047	23.387	-0.212	-0.212	0.000	0.000	0.000	0.000
95	A	111	LYS	1	0.886	0.944	27.412	9.334	9.334	0.000	0.000	0.000	0.000
96	A	112	ASP	-1	-0.809	-0.902	25.562	-10.270	-10.270	0.000	0.000	0.000	0.000
97	A	113	PHE	0	-0.012	-0.004	18.304	-0.172	-0.172	0.000	0.000	0.000	0.000
98	A	114	LYS	1	0.968	0.987	19.581	12.904	12.904	0.000	0.000	0.000	0.000
99	A	115	ILE	0	0.021	0.010	14.056	0.485	0.485	0.000	0.000	0.000	0.000
100	A	116	GLN	0	-0.028	-0.039	17.343	-0.338	-0.338	0.000	0.000	0.000	0.000
101	A	117	ASN	0	-0.019	-0.012	15.916	-0.313	-0.313	0.000	0.000	0.000	0.000
102	A	118	ILE	0	-0.007	0.021	9.631	0.521	0.521	0.000	0.000	0.000	0.000
103	A	119	VAL	0	0.004	0.006	12.860	-0.132	-0.132	0.000	0.000	0.000	0.000
104	A	120	GLY	0	0.033	0.005	9.481	-0.280	-0.280	0.000	0.000	0.000	0.000
105	A	121	SER	0	-0.022	-0.005	10.047	0.854	0.854	0.000	0.000	0.000	0.000
106	A	122	CYS	0	-0.027	-0.006	6.971	-1.267	-1.267	0.000	0.000	0.000	0.000
107	A	123	ASP	-1	-0.813	-0.904	9.233	-17.447	-17.447	0.000	0.000	0.000	0.000
108	A	124	VAL	0	0.010	0.002	8.948	-1.634	-1.634	0.000	0.000	0.000	0.000
109	A	125	LYS	1	0.906	0.964	11.040	21.638	21.638	0.000	0.000	0.000	0.000
110	A	126	PHE	0	0.026	0.016	11.952	1.101	1.101	0.000	0.000	0.000	0.000
111	A	127	PRO	0	0.025	0.020	16.217	-0.509	-0.509	0.000	0.000	0.000	0.000
112	A	128	ILE	0	-0.001	-0.003	15.044	-0.265	-0.265	0.000	0.000	0.000	0.000
113	A	129	ARG	1	0.902	0.946	19.162	14.214	14.214	0.000	0.000	0.000	0.000
114	A	130	LEU	0	-0.034	-0.015	18.842	-0.075	-0.075	0.000	0.000	0.000	0.000
115	A	131	GLU	-1	-0.860	-0.922	21.844	-10.884	-10.884	0.000	0.000	0.000	0.000
116	A	132	GLY	0	0.036	0.023	24.397	0.101	0.101	0.000	0.000	0.000	0.000
117	A	133	LEU	0	-0.023	0.011	16.556	-0.183	-0.183	0.000	0.000	0.000	0.000
118	A	134	ALA	0	0.020	-0.015	21.160	-0.204	-0.204	0.000	0.000	0.000	0.000
119	A	135	TYR	0	0.012	0.010	22.946	0.055	0.055	0.000	0.000	0.000	0.000
120	A	136	SER	0	0.001	-0.015	21.980	-0.109	-0.109	0.000	0.000	0.000	0.000
121	A	137	HIS	1	0.820	0.915	17.963	15.442	15.442	0.000	0.000	0.000	0.000
122	A	138	ALA	0	0.119	0.074	21.984	-0.307	-0.307	0.000	0.000	0.000	0.000
123	A	139	ALA	0	0.008	0.008	23.874	0.034	0.034	0.000	0.000	0.000	0.000
124	A	140	PHE	0	-0.081	-0.049	19.119	-0.272	-0.272	0.000	0.000	0.000	0.000
125	A	141	SER	0	-0.015	-0.005	20.557	-0.715	-0.715	0.000	0.000	0.000	0.000
126	A	142	SER	0	-0.019	-0.011	21.984	0.525	0.525	0.000	0.000	0.000	0.000
127	A	143	TYR	0	-0.013	-0.026	22.862	-0.609	-0.609	0.000	0.000	0.000	0.000
128	A	144	GLU	-1	-0.814	-0.884	24.883	-10.200	-10.200	0.000	0.000	0.000	0.000
129	A	145	PRO	0	-0.023	-0.013	26.727	-0.012	-0.012	0.000	0.000	0.000	0.000
130	A	146	GLU	-1	-0.925	-0.957	27.720	-9.017	-9.017	0.000	0.000	0.000	0.000
131	A	147	LEU	0	-0.051	-0.008	28.350	0.173	0.173	0.000	0.000	0.000	0.000
132	A	148	PHE	0	-0.049	-0.054	20.491	-0.358	-0.358	0.000	0.000	0.000	0.000
133	A	149	PRO	0	0.038	0.018	23.509	-0.249	-0.249	0.000	0.000	0.000	0.000
134	A	150	GLY	0	-0.033	-0.005	20.302	-0.375	-0.375	0.000	0.000	0.000	0.000
135	A	151	LEU	0	-0.027	-0.009	18.501	0.398	0.398	0.000	0.000	0.000	0.000
136	A	152	ILE	0	-0.013	-0.017	18.373	-0.959	-0.959	0.000	0.000	0.000	0.000
137	A	153	TYR	0	0.055	0.014	15.623	0.464	0.464	0.000	0.000	0.000	0.000
138	A	154	ARG	1	0.921	0.953	16.391	12.240	12.240	0.000	0.000	0.000	0.000
139	A	155	MET	0	-0.007	0.014	11.712	0.157	0.157	0.000	0.000	0.000	0.000
140	A	156	LYS	1	0.915	0.949	16.243	14.320	14.320	0.000	0.000	0.000	0.000
141	A	157	VAL	0	0.021	0.030	14.744	0.334	0.334	0.000	0.000	0.000	0.000
142	A	158	PRO	0	0.044	0.025	10.755	-0.954	-0.954	0.000	0.000	0.000	0.000
143	A	159	LYS	1	0.967	0.979	14.095	14.759	14.759	0.000	0.000	0.000	0.000
144	A	160	ILE	0	-0.044	-0.013	11.237	0.153	0.153	0.000	0.000	0.000	0.000
145	A	161	VAL	0	-0.015	-0.010	14.600	0.600	0.600	0.000	0.000	0.000	0.000
146	A	162	LEU	0	-0.010	-0.011	10.512	-0.850	-0.850	0.000	0.000	0.000	0.000
147	A	163	LEU	0	-0.042	-0.007	14.253	1.175	1.175	0.000	0.000	0.000	0.000
148	A	164	ILE	0	0.034	0.017	14.121	-1.035	-1.035	0.000	0.000	0.000	0.000
149	A	165	PHE	0	0.044	0.016	16.084	1.067	1.067	0.000	0.000	0.000	0.000
150	A	166	VAL	0	0.042	0.013	17.781	-0.598	-0.598	0.000	0.000	0.000	0.000
151	A	167	SER	0	0.011	0.004	18.409	-0.198	-0.198	0.000	0.000	0.000	0.000
152	A	168	GLY	0	0.073	0.058	15.069	-0.198	-0.198	0.000	0.000	0.000	0.000
153	A	169	LYS	1	0.838	0.909	13.206	15.684	15.684	0.000	0.000	0.000	0.000
154	A	170	ILE	0	0.007	0.003	10.543	0.749	0.749	0.000	0.000	0.000	0.000
155	A	171	VAL	0	-0.021	-0.014	11.963	-0.668	-0.668	0.000	0.000	0.000	0.000
156	A	172	ILE	0	0.007	0.007	7.720	0.062	0.062	0.000	0.000	0.000	0.000
157	A	173	THR	0	0.040	0.009	11.863	0.191	0.191	0.000	0.000	0.000	0.000
158	A	174	GLY	0	0.000	0.002	13.961	-0.050	-0.050	0.000	0.000	0.000	0.000
159	A	175	ALA	0	0.001	0.019	10.795	0.552	0.552	0.000	0.000	0.000	0.000
160	A	176	LYS	1	0.822	0.897	12.754	16.461	16.461	0.000	0.000	0.000	0.000
161	A	177	MET	0	0.019	0.003	10.475	0.492	0.492	0.000	0.000	0.000	0.000
162	A	178	ARG	1	0.885	0.902	5.604	28.488	28.488	0.000	0.000	0.000	0.000
163	A	179	ASP	-1	-0.816	-0.913	5.225	-39.870	-39.870	0.000	0.000	0.000	0.000
164	A	180	GLU	-1	-0.839	-0.916	6.286	-22.844	-22.844	0.000	0.000	0.000	0.000
165	A	181	THR	0	-0.005	-0.013	6.333	1.138	1.138	0.000	0.000	0.000	0.000
168	A	184	ALA	0	0.022	-0.009	7.381	1.285	1.285	0.000	0.000	0.000	0.000
171	A	187	ASN	0	-0.022	-0.002	5.836	4.659	4.659	0.000	0.000	0.000	0.000
172	A	188	ILE	0	0.016	0.015	9.422	2.028	2.028	0.000	0.000	0.000	0.000
173	A	189	TYR	0	0.044	0.027	7.522	1.505	1.505	0.000	0.000	0.000	0.000
174	A	190	PRO	0	0.042	0.023	9.045	1.640	1.640	0.000	0.000	0.000	0.000
175	A	191	VAL	0	0.042	0.019	11.815	1.699	1.699	0.000	0.000	0.000	0.000
176	A	192	LEU	0	-0.049	-0.039	10.650	1.278	1.278	0.000	0.000	0.000	0.000
177	A	193	SER	0	-0.011	-0.021	11.904	0.899	0.899	0.000	0.000	0.000	0.000
178	A	194	GLU	-1	-0.935	-0.953	14.560	-15.259	-15.259	0.000	0.000	0.000	0.000
179	A	195	PHE	0	-0.052	-0.036	17.374	1.242	1.242	0.000	0.000	0.000	0.000
180	A	196	ARG	1	0.982	1.006	16.173	16.532	16.532	0.000	0.000	0.000	0.000
181	A	197	LYS	1	0.836	0.914	18.494	13.434	13.434	0.000	0.000	0.000	0.000
182	A	198	ILE	-1	-0.878	-0.929	21.257	-12.612	-12.612	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:17:HIS)