FMO DATABASE

FMODB ID: 1991Z

Calculation Name: 2R6V-A-Xray547

Preferred Name:

Target Type:

Ligand Name: flavin mononucleotide | nicotinamide | 1,2-ethanediol

Ligand 3-letter code: FMN | NCA | EDO

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2R6V

Chain ID: A

ChEMBL ID:

UniProt ID: O58586

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	-1951828.025664
FMO2-HF: Nuclear repulsion	1880293.680854
FMO2-HF: Total energy	-71534.34481
FMO2-MP2: Total energy	-71745.188645

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:-9:HIS)

Summations of interaction energy for fragment #1(A:-9: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.
13.682	22.998	12.199	-5.936	-15.58	-0.054

Interaction energy analysis for fragmet #1(A:-9:HIS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 2 / q_Mulliken : 1.769 / q_NPA : 1.889

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	-7	HIS	0	-0.038	-0.033	2.496	-22.283	-19.910	4.192	-2.661	-3.905	-0.028
4	A	-6	GLU	-1	-0.841	-0.904	4.337	-53.190	-53.065	-0.001	-0.013	-0.111	0.000
12	A	2	GLU	-1	-0.791	-0.889	4.629	-92.519	-92.552	-0.001	-0.017	0.051	0.000
168	A	158	TRP	0	-0.021	-0.033	2.598	-19.046	-12.438	8.010	-3.211	-11.407	-0.026
169	A	159	SER	0	0.031	0.007	4.503	2.539	2.782	-0.001	-0.034	-0.208	0.000
5	A	-5	ASN	0	-0.020	-0.023	5.758	5.634	5.634	0.000	0.000	0.000	0.000
6	A	-4	LEU	0	-0.009	0.019	7.042	3.427	3.427	0.000	0.000	0.000	0.000
7	A	-3	TYR	0	-0.008	-0.016	9.250	-1.795	-1.795	0.000	0.000	0.000	0.000
8	A	-2	PHE	0	0.018	0.021	12.111	1.964	1.964	0.000	0.000	0.000	0.000
9	A	-1	GLN	0	0.002	0.003	6.363	-0.294	-0.294	0.000	0.000	0.000	0.000
10	A	0	GLY	0	0.056	0.022	7.604	5.048	5.048	0.000	0.000	0.000	0.000
11	A	1	MET	0	-0.033	-0.011	7.052	-10.592	-10.592	0.000	0.000	0.000	0.000
13	A	3	GLY	0	0.050	0.021	9.190	2.068	2.068	0.000	0.000	0.000	0.000
14	A	4	TYR	0	0.045	0.011	6.267	-0.143	-0.143	0.000	0.000	0.000	0.000
15	A	5	ARG	1	0.817	0.901	5.298	74.351	74.351	0.000	0.000	0.000	0.000
16	A	6	LEU	0	0.009	-0.001	11.150	1.025	1.025	0.000	0.000	0.000	0.000
17	A	7	LEU	0	0.006	0.013	14.173	2.275	2.275	0.000	0.000	0.000	0.000
18	A	8	TYR	0	-0.113	-0.065	10.234	-0.555	-0.555	0.000	0.000	0.000	0.000
19	A	9	PRO	0	0.011	-0.010	13.571	0.349	0.349	0.000	0.000	0.000	0.000
20	A	10	MET	0	0.000	0.030	13.529	1.639	1.639	0.000	0.000	0.000	0.000
21	A	11	ARG	1	0.883	0.941	15.285	28.784	28.784	0.000	0.000	0.000	0.000
22	A	12	THR	0	-0.026	-0.032	13.436	-1.348	-1.348	0.000	0.000	0.000	0.000
23	A	13	TYR	0	-0.024	-0.020	16.028	2.471	2.471	0.000	0.000	0.000	0.000
24	A	14	LEU	0	0.006	-0.005	16.239	-2.424	-2.424	0.000	0.000	0.000	0.000
25	A	15	ILE	0	-0.022	-0.009	17.435	1.324	1.324	0.000	0.000	0.000	0.000
26	A	16	VAL	0	0.027	0.020	18.997	-1.177	-1.177	0.000	0.000	0.000	0.000
27	A	17	SER	0	-0.004	-0.019	20.856	0.163	0.163	0.000	0.000	0.000	0.000
28	A	18	GLY	0	0.044	0.021	22.915	-0.297	-0.297	0.000	0.000	0.000	0.000
29	A	19	HIS	0	0.055	0.007	25.719	-0.194	-0.194	0.000	0.000	0.000	0.000
30	A	20	GLY	0	0.024	0.025	28.368	0.215	0.215	0.000	0.000	0.000	0.000
31	A	21	GLU	-1	-0.884	-0.934	27.629	-19.795	-19.795	0.000	0.000	0.000	0.000
32	A	22	GLU	-1	-0.824	-0.883	25.301	-22.016	-22.016	0.000	0.000	0.000	0.000
33	A	23	THR	0	-0.042	-0.028	23.902	-0.530	-0.530	0.000	0.000	0.000	0.000
34	A	24	ASN	0	-0.015	-0.028	17.191	-1.231	-1.231	0.000	0.000	0.000	0.000
35	A	25	VAL	0	0.060	0.035	17.701	0.462	0.462	0.000	0.000	0.000	0.000
36	A	26	MET	0	-0.073	-0.018	13.545	-1.682	-1.682	0.000	0.000	0.000	0.000
37	A	27	ALA	0	0.044	0.029	11.787	1.661	1.661	0.000	0.000	0.000	0.000
38	A	28	ALA	0	-0.029	-0.023	12.809	-1.457	-1.457	0.000	0.000	0.000	0.000
39	A	29	ASP	-1	-0.718	-0.808	10.717	-49.194	-49.194	0.000	0.000	0.000	0.000
40	A	30	TRP	0	-0.059	-0.029	10.156	2.671	2.671	0.000	0.000	0.000	0.000
41	A	31	VAL	0	-0.005	-0.014	15.779	1.124	1.124	0.000	0.000	0.000	0.000
42	A	32	THR	0	-0.020	-0.012	19.199	-0.371	-0.371	0.000	0.000	0.000	0.000
43	A	33	VAL	0	0.009	0.004	22.608	0.341	0.341	0.000	0.000	0.000	0.000
44	A	34	VAL	0	-0.054	-0.036	25.616	-0.545	-0.545	0.000	0.000	0.000	0.000
45	A	35	SER	0	-0.007	-0.004	28.178	0.575	0.575	0.000	0.000	0.000	0.000
46	A	36	PHE	0	0.002	-0.001	31.612	-0.414	-0.414	0.000	0.000	0.000	0.000
47	A	37	ASP	-1	-0.894	-0.937	33.949	-15.828	-15.828	0.000	0.000	0.000	0.000
48	A	38	PRO	0	0.058	0.021	35.383	0.179	0.179	0.000	0.000	0.000	0.000
49	A	39	PHE	0	-0.012	0.003	28.856	-0.608	-0.608	0.000	0.000	0.000	0.000
50	A	40	ILE	0	-0.025	-0.008	28.714	-0.102	-0.102	0.000	0.000	0.000	0.000
51	A	41	VAL	0	0.009	0.006	24.813	-0.446	-0.446	0.000	0.000	0.000	0.000
52	A	42	GLY	0	0.045	0.013	23.376	0.596	0.596	0.000	0.000	0.000	0.000
53	A	43	VAL	0	-0.028	-0.009	17.411	-0.998	-0.998	0.000	0.000	0.000	0.000
54	A	44	ALA	0	-0.001	0.022	15.768	0.809	0.809	0.000	0.000	0.000	0.000
55	A	45	VAL	0	-0.022	-0.024	14.925	-2.120	-2.120	0.000	0.000	0.000	0.000
56	A	46	ALA	0	0.037	0.028	12.474	1.306	1.306	0.000	0.000	0.000	0.000
57	A	47	PRO	0	0.060	0.024	14.481	0.097	0.097	0.000	0.000	0.000	0.000
58	A	48	LYS	1	0.875	0.925	9.816	47.871	47.871	0.000	0.000	0.000	0.000
59	A	49	ARG	1	0.890	0.957	8.638	48.665	48.665	0.000	0.000	0.000	0.000
60	A	50	THR	0	0.034	0.001	14.506	0.928	0.928	0.000	0.000	0.000	0.000
61	A	51	THR	0	0.061	0.011	16.345	1.273	1.273	0.000	0.000	0.000	0.000
62	A	52	HIS	0	-0.010	0.011	17.601	1.661	1.661	0.000	0.000	0.000	0.000
63	A	53	LYS	1	0.873	0.928	17.391	31.412	31.412	0.000	0.000	0.000	0.000
64	A	54	LEU	0	0.004	0.009	20.874	0.944	0.944	0.000	0.000	0.000	0.000
65	A	55	ILE	0	0.031	0.017	20.570	0.900	0.900	0.000	0.000	0.000	0.000
66	A	56	LYS	1	0.874	0.937	23.392	23.904	23.904	0.000	0.000	0.000	0.000
67	A	57	LYS	1	0.803	0.909	25.517	21.141	21.141	0.000	0.000	0.000	0.000
68	A	58	TYR	0	-0.014	-0.040	26.880	1.028	1.028	0.000	0.000	0.000	0.000
69	A	59	GLY	0	0.033	0.024	27.971	0.631	0.631	0.000	0.000	0.000	0.000
70	A	60	GLU	-1	-0.795	-0.896	27.640	-18.380	-18.380	0.000	0.000	0.000	0.000
71	A	61	PHE	0	-0.017	-0.026	22.996	-0.824	-0.824	0.000	0.000	0.000	0.000
72	A	62	VAL	0	0.005	0.020	23.981	0.783	0.783	0.000	0.000	0.000	0.000
73	A	63	ILE	0	0.000	0.002	21.048	-1.435	-1.435	0.000	0.000	0.000	0.000
74	A	64	SER	0	0.018	-0.008	21.817	0.955	0.955	0.000	0.000	0.000	0.000
75	A	65	VAL	0	-0.036	-0.026	21.129	-1.721	-1.721	0.000	0.000	0.000	0.000
76	A	66	PRO	0	0.000	0.014	18.049	0.995	0.995	0.000	0.000	0.000	0.000
77	A	67	SER	0	0.067	0.026	21.161	-0.429	-0.429	0.000	0.000	0.000	0.000
78	A	68	LEU	0	-0.009	-0.020	16.337	-1.229	-1.229	0.000	0.000	0.000	0.000
79	A	69	ASP	-1	-0.840	-0.903	18.952	-26.920	-26.920	0.000	0.000	0.000	0.000
80	A	70	VAL	0	-0.004	0.003	20.248	-0.214	-0.214	0.000	0.000	0.000	0.000
81	A	71	LEU	0	0.020	0.012	12.908	-1.031	-1.031	0.000	0.000	0.000	0.000
82	A	72	ARG	1	0.954	0.969	15.058	28.633	28.633	0.000	0.000	0.000	0.000
83	A	73	ASP	-1	-0.763	-0.877	15.114	-31.652	-31.652	0.000	0.000	0.000	0.000
84	A	74	VAL	0	0.004	0.005	13.452	-0.852	-0.852	0.000	0.000	0.000	0.000
85	A	75	TRP	0	0.014	0.009	6.027	-3.203	-3.203	0.000	0.000	0.000	0.000
86	A	76	ILE	0	0.002	0.018	10.926	-3.387	-3.387	0.000	0.000	0.000	0.000
87	A	77	ALA	0	0.015	0.005	13.104	-0.369	-0.369	0.000	0.000	0.000	0.000
88	A	78	GLY	0	-0.025	-0.015	10.230	0.377	0.377	0.000	0.000	0.000	0.000
89	A	79	THR	0	-0.076	-0.044	6.875	-3.288	-3.288	0.000	0.000	0.000	0.000
90	A	80	LYS	1	0.971	0.993	9.194	37.026	37.026	0.000	0.000	0.000	0.000
91	A	81	LYS	1	0.858	0.907	8.722	49.871	49.871	0.000	0.000	0.000	0.000
92	A	82	GLY	0	0.035	0.015	14.525	1.248	1.248	0.000	0.000	0.000	0.000
93	A	83	PRO	0	0.082	0.034	18.231	-1.071	-1.071	0.000	0.000	0.000	0.000
94	A	84	SER	0	-0.034	0.003	18.349	0.031	0.031	0.000	0.000	0.000	0.000
95	A	85	LYS	1	0.814	0.903	14.152	36.659	36.659	0.000	0.000	0.000	0.000
96	A	86	LEU	0	0.024	0.009	18.219	-0.464	-0.464	0.000	0.000	0.000	0.000
97	A	87	LYS	1	0.869	0.941	21.037	26.605	26.605	0.000	0.000	0.000	0.000
98	A	88	GLU	-1	-0.959	-0.969	17.220	-29.179	-29.179	0.000	0.000	0.000	0.000
99	A	89	MET	0	-0.072	-0.028	17.901	-1.530	-1.530	0.000	0.000	0.000	0.000
100	A	90	SER	0	-0.007	0.000	20.374	1.465	1.465	0.000	0.000	0.000	0.000
101	A	91	VAL	0	-0.079	-0.047	21.693	-0.161	-0.161	0.000	0.000	0.000	0.000
102	A	92	THR	0	0.032	-0.004	24.398	0.436	0.436	0.000	0.000	0.000	0.000
103	A	93	LEU	0	-0.060	-0.033	24.791	-0.122	-0.122	0.000	0.000	0.000	0.000
104	A	94	ILE	0	0.020	0.016	28.593	0.749	0.749	0.000	0.000	0.000	0.000
105	A	95	PRO	0	-0.022	-0.013	30.932	-0.432	-0.432	0.000	0.000	0.000	0.000
106	A	96	SER	0	-0.026	-0.017	29.784	-0.043	-0.043	0.000	0.000	0.000	0.000
107	A	97	LYS	1	0.897	0.937	32.574	17.744	17.744	0.000	0.000	0.000	0.000
108	A	98	LYS	1	0.844	0.910	34.192	16.963	16.963	0.000	0.000	0.000	0.000
109	A	99	VAL	0	-0.078	-0.012	29.284	0.225	0.225	0.000	0.000	0.000	0.000
110	A	100	LYS	1	0.891	0.942	31.380	18.557	18.557	0.000	0.000	0.000	0.000
111	A	101	VAL	0	-0.040	0.003	25.309	-0.065	-0.065	0.000	0.000	0.000	0.000
112	A	102	PRO	0	-0.001	0.019	26.644	0.292	0.292	0.000	0.000	0.000	0.000
113	A	103	SER	0	0.012	-0.010	26.711	-0.950	-0.950	0.000	0.000	0.000	0.000
114	A	104	ILE	0	-0.020	-0.015	22.124	-0.002	-0.002	0.000	0.000	0.000	0.000
115	A	105	GLU	-1	-0.883	-0.937	26.377	-18.962	-18.962	0.000	0.000	0.000	0.000
116	A	106	GLU	-1	-0.775	-0.868	25.158	-22.395	-22.395	0.000	0.000	0.000	0.000
117	A	107	ALA	0	-0.083	-0.028	24.338	-0.370	-0.370	0.000	0.000	0.000	0.000
118	A	108	LEU	0	-0.009	-0.005	24.492	1.049	1.049	0.000	0.000	0.000	0.000
119	A	109	ALA	0	0.024	-0.006	26.126	0.980	0.980	0.000	0.000	0.000	0.000
120	A	110	ASN	0	-0.007	0.020	25.803	-1.894	-1.894	0.000	0.000	0.000	0.000
121	A	111	ILE	0	0.041	0.017	25.658	0.943	0.943	0.000	0.000	0.000	0.000
122	A	112	GLU	-1	-0.752	-0.870	26.762	-19.263	-19.263	0.000	0.000	0.000	0.000
123	A	113	CYS	0	-0.045	-0.011	26.218	0.405	0.405	0.000	0.000	0.000	0.000
124	A	114	ARG	1	0.932	0.948	28.292	17.252	17.252	0.000	0.000	0.000	0.000
125	A	115	VAL	0	-0.071	-0.041	25.767	-0.237	-0.237	0.000	0.000	0.000	0.000
126	A	116	ILE	0	0.028	0.022	28.448	0.498	0.498	0.000	0.000	0.000	0.000
127	A	117	ASP	-1	-0.783	-0.856	28.440	-20.190	-20.190	0.000	0.000	0.000	0.000
128	A	118	ALA	0	-0.072	-0.045	24.365	-0.847	-0.847	0.000	0.000	0.000	0.000
129	A	119	ARG	1	0.831	0.903	24.067	20.876	20.876	0.000	0.000	0.000	0.000
130	A	120	SER	0	-0.027	-0.021	21.050	-1.146	-1.146	0.000	0.000	0.000	0.000
131	A	121	TYR	0	0.036	0.014	19.778	1.127	1.127	0.000	0.000	0.000	0.000
132	A	122	GLY	0	0.026	0.018	17.597	-1.581	-1.581	0.000	0.000	0.000	0.000
133	A	123	ASP	-1	-0.866	-0.915	12.289	-40.635	-40.635	0.000	0.000	0.000	0.000
134	A	124	HIS	0	-0.070	-0.076	11.019	-2.375	-2.375	0.000	0.000	0.000	0.000
135	A	125	THR	0	-0.027	-0.006	16.238	1.419	1.419	0.000	0.000	0.000	0.000
136	A	126	PHE	0	0.024	0.018	18.957	-1.066	-1.066	0.000	0.000	0.000	0.000
137	A	127	PHE	0	-0.012	-0.017	19.728	1.290	1.290	0.000	0.000	0.000	0.000
138	A	128	VAL	0	0.025	0.009	23.066	-0.677	-0.677	0.000	0.000	0.000	0.000
139	A	129	GLY	0	0.003	-0.011	26.062	0.462	0.462	0.000	0.000	0.000	0.000
140	A	130	GLU	-1	-0.886	-0.941	27.470	-17.391	-17.391	0.000	0.000	0.000	0.000
141	A	131	VAL	0	-0.021	-0.013	28.861	-0.255	-0.255	0.000	0.000	0.000	0.000
142	A	132	VAL	0	0.016	0.015	31.324	0.624	0.624	0.000	0.000	0.000	0.000
143	A	133	GLY	0	-0.019	-0.016	32.691	0.719	0.719	0.000	0.000	0.000	0.000
144	A	134	TYR	0	0.031	0.012	30.872	-0.743	-0.743	0.000	0.000	0.000	0.000
145	A	135	THR	0	-0.035	-0.009	30.974	0.585	0.585	0.000	0.000	0.000	0.000
146	A	136	TYR	0	0.020	0.002	30.413	-0.852	-0.852	0.000	0.000	0.000	0.000
147	A	137	LYS	1	0.877	0.951	28.940	21.269	21.269	0.000	0.000	0.000	0.000
148	A	138	ASP	-1	-0.853	-0.928	32.489	-17.373	-17.373	0.000	0.000	0.000	0.000
149	A	139	TYR	0	0.025	-0.006	28.718	-0.183	-0.183	0.000	0.000	0.000	0.000
150	A	140	ALA	0	0.022	0.008	28.933	-0.207	-0.207	0.000	0.000	0.000	0.000
151	A	141	PHE	0	-0.026	-0.022	27.722	-0.758	-0.758	0.000	0.000	0.000	0.000
152	A	142	GLU	-1	-0.836	-0.894	32.958	-16.911	-16.911	0.000	0.000	0.000	0.000
153	A	143	LYS	1	0.853	0.918	35.741	17.253	17.253	0.000	0.000	0.000	0.000
154	A	144	GLY	0	0.037	0.028	36.774	0.300	0.300	0.000	0.000	0.000	0.000
155	A	145	LYS	1	0.902	0.944	32.652	16.859	16.859	0.000	0.000	0.000	0.000
156	A	146	PRO	0	-0.024	-0.010	27.958	0.174	0.174	0.000	0.000	0.000	0.000
157	A	147	ASN	0	-0.011	-0.002	30.076	-0.174	-0.174	0.000	0.000	0.000	0.000
158	A	148	LEU	0	0.024	0.004	25.816	-0.604	-0.604	0.000	0.000	0.000	0.000
159	A	149	LYS	1	0.988	1.000	26.201	18.025	18.025	0.000	0.000	0.000	0.000
160	A	150	ALA	0	-0.035	-0.010	27.050	-0.089	-0.089	0.000	0.000	0.000	0.000
161	A	151	LYS	1	0.828	0.911	22.121	24.182	24.182	0.000	0.000	0.000	0.000
162	A	152	PHE	0	0.020	0.008	21.592	-1.577	-1.577	0.000	0.000	0.000	0.000
163	A	153	LEU	0	-0.007	0.029	15.286	-0.700	-0.700	0.000	0.000	0.000	0.000
164	A	154	ALA	0	0.033	0.024	16.130	0.603	0.603	0.000	0.000	0.000	0.000
165	A	155	HIS	1	0.786	0.874	7.904	58.116	58.116	0.000	0.000	0.000	0.000
166	A	156	VAL	0	0.051	0.026	10.413	1.155	1.155	0.000	0.000	0.000	0.000
167	A	157	SER	0	-0.014	-0.045	5.674	-5.471	-5.471	0.000	0.000	0.000	0.000
170	A	160	GLU	-1	-0.859	-0.870	6.629	-56.330	-56.330	0.000	0.000	0.000	0.000
171	A	161	PHE	0	-0.014	-0.028	9.148	-0.788	-0.788	0.000	0.000	0.000	0.000
172	A	162	VAL	0	0.015	0.011	12.545	0.983	0.983	0.000	0.000	0.000	0.000
173	A	163	THR	0	0.000	-0.027	15.988	0.661	0.661	0.000	0.000	0.000	0.000
174	A	164	PHE	0	-0.008	-0.007	19.531	-0.531	-0.531	0.000	0.000	0.000	0.000
175	A	165	SER	0	0.036	0.021	22.369	0.483	0.483	0.000	0.000	0.000	0.000
176	A	166	GLU	-1	-0.904	-0.970	24.839	-20.964	-20.964	0.000	0.000	0.000	0.000
177	A	167	LYS	1	0.769	0.894	27.990	20.678	20.678	0.000	0.000	0.000	0.000
178	A	168	VAL	0	0.029	0.012	28.566	-0.660	-0.660	0.000	0.000	0.000	0.000
179	A	169	HIS	-1	-0.886	-0.941	28.671	-20.282	-20.282	0.000	0.000	0.000	0.000
180	A	170	LYS	0	-0.048	-0.033	32.008	-0.282	-0.282	0.000	0.000	0.000	0.000
181	A	171	ALA	0	-0.033	-0.027	34.037	-0.039	-0.039	0.000	0.000	0.000	0.000
182	A	172	GLU	-2	-1.889	-1.916	35.931	-31.408	-31.408	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:-9:HIS)