FMO DATABASE

FMODB ID: NLG9Q

Calculation Name: 3ZOH-D-Xray547

Preferred Name:

Target Type:

Ligand Name: flavin mononucleotide | cyclohex-2-en-1-one

Ligand 3-letter code: FMN | A2Q

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 3ZOH

Chain ID: D

ChEMBL ID:

UniProt ID: Q72HI0

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	178
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1784336.397993
FMO2-HF: Nuclear repulsion	1716656.550381
FMO2-HF: Total energy	-67679.847613
FMO2-MP2: Total energy	-67882.291069

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:MET)

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

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.
20.32	22.937	0.586	-1.407	-1.797	-0.011

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.898 / q_NPA : 0.944

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	SER	0	0.054	0.025	2.685	-0.414	2.203	0.586	-1.407	-1.797	-0.011
4	A	4	TYR	0	-0.013	-0.016	5.423	2.011	2.011	0.000	0.000	0.000	0.000
5	A	5	ARG	1	0.986	0.993	9.019	26.549	26.549	0.000	0.000	0.000	0.000
6	A	6	ALA	0	0.033	0.023	12.016	0.206	0.206	0.000	0.000	0.000	0.000
7	A	7	GLN	0	-0.023	-0.029	13.665	0.963	0.963	0.000	0.000	0.000	0.000
8	A	8	GLY	0	0.054	0.041	16.942	0.850	0.850	0.000	0.000	0.000	0.000
9	A	9	PRO	0	-0.001	-0.007	16.316	-0.752	-0.752	0.000	0.000	0.000	0.000
10	A	10	LEU	0	-0.001	0.008	10.154	-0.567	-0.567	0.000	0.000	0.000	0.000
11	A	11	PRO	0	-0.012	-0.003	11.882	0.618	0.618	0.000	0.000	0.000	0.000
12	A	12	GLY	0	-0.007	-0.015	12.567	0.852	0.852	0.000	0.000	0.000	0.000
13	A	13	PHE	0	-0.047	-0.019	11.520	-1.601	-1.601	0.000	0.000	0.000	0.000
14	A	14	TYR	0	0.073	0.017	11.862	0.712	0.712	0.000	0.000	0.000	0.000
15	A	15	HIS	0	-0.044	-0.024	7.135	-1.169	-1.169	0.000	0.000	0.000	0.000
16	A	16	TYR	0	0.008	0.018	8.610	-0.745	-0.745	0.000	0.000	0.000	0.000
17	A	17	TYR	0	-0.039	0.015	11.229	1.238	1.238	0.000	0.000	0.000	0.000
18	A	18	PRO	0	-0.005	-0.010	12.628	-0.949	-0.949	0.000	0.000	0.000	0.000
19	A	19	GLY	0	0.031	0.020	16.236	-0.088	-0.088	0.000	0.000	0.000	0.000
20	A	20	VAL	0	0.046	0.014	18.587	0.194	0.194	0.000	0.000	0.000	0.000
21	A	21	PRO	0	-0.079	-0.036	22.278	-0.003	-0.003	0.000	0.000	0.000	0.000
22	A	22	ALA	0	0.041	0.034	24.492	0.320	0.320	0.000	0.000	0.000	0.000
23	A	23	VAL	0	-0.032	-0.025	27.084	-0.060	-0.060	0.000	0.000	0.000	0.000
24	A	24	VAL	0	0.013	0.013	29.238	0.215	0.215	0.000	0.000	0.000	0.000
25	A	25	GLY	0	0.020	0.015	31.866	0.033	0.033	0.000	0.000	0.000	0.000
26	A	26	VAL	0	-0.037	-0.028	35.680	0.023	0.023	0.000	0.000	0.000	0.000
27	A	27	ARG	1	0.886	0.920	37.968	6.432	6.432	0.000	0.000	0.000	0.000
28	A	28	VAL	0	-0.055	-0.019	41.573	-0.013	-0.013	0.000	0.000	0.000	0.000
29	A	29	GLU	-1	-0.931	-0.963	44.034	-6.039	-6.039	0.000	0.000	0.000	0.000
30	A	30	GLU	-1	-0.872	-0.938	47.251	-6.171	-6.171	0.000	0.000	0.000	0.000
31	A	31	ARG	1	0.807	0.916	41.574	6.785	6.785	0.000	0.000	0.000	0.000
32	A	32	VAL	0	0.004	0.005	40.264	-0.123	-0.123	0.000	0.000	0.000	0.000
33	A	33	ASN	0	-0.018	-0.030	35.210	0.005	0.005	0.000	0.000	0.000	0.000
34	A	34	PHE	0	0.037	0.033	34.278	-0.088	-0.088	0.000	0.000	0.000	0.000
35	A	35	CYS	0	-0.073	-0.056	29.046	-0.047	-0.047	0.000	0.000	0.000	0.000
36	A	36	PRO	0	0.019	0.043	26.468	-0.019	-0.019	0.000	0.000	0.000	0.000
37	A	37	ALA	0	0.002	0.000	25.271	-0.163	-0.163	0.000	0.000	0.000	0.000
38	A	38	VAL	0	0.004	0.001	19.399	-0.016	-0.016	0.000	0.000	0.000	0.000
39	A	39	TRP	0	-0.046	-0.015	17.425	-0.159	-0.159	0.000	0.000	0.000	0.000
40	A	40	ASN	0	-0.059	-0.038	21.264	0.567	0.567	0.000	0.000	0.000	0.000
41	A	41	THR	0	0.035	0.005	21.067	-0.603	-0.603	0.000	0.000	0.000	0.000
42	A	42	GLY	0	0.017	0.028	23.053	0.443	0.443	0.000	0.000	0.000	0.000
43	A	43	LEU	0	-0.059	-0.034	23.911	-0.405	-0.405	0.000	0.000	0.000	0.000
44	A	44	SER	0	-0.012	-0.017	26.149	-0.062	-0.062	0.000	0.000	0.000	0.000
45	A	45	ALA	0	0.007	0.009	28.793	0.025	0.025	0.000	0.000	0.000	0.000
46	A	46	ASP	-1	-0.910	-0.932	30.609	-7.452	-7.452	0.000	0.000	0.000	0.000
47	A	47	PRO	0	0.014	-0.007	33.650	-0.003	-0.003	0.000	0.000	0.000	0.000
48	A	48	PRO	0	0.020	0.024	32.005	-0.245	-0.245	0.000	0.000	0.000	0.000
49	A	49	LEU	0	-0.045	-0.016	29.829	0.160	0.160	0.000	0.000	0.000	0.000
50	A	50	PHE	0	0.045	0.002	25.806	-0.309	-0.309	0.000	0.000	0.000	0.000
51	A	51	GLY	0	0.015	0.013	26.497	0.269	0.269	0.000	0.000	0.000	0.000
52	A	52	VAL	0	-0.015	-0.017	25.640	-0.302	-0.302	0.000	0.000	0.000	0.000
53	A	53	SER	0	-0.003	0.003	22.785	0.320	0.320	0.000	0.000	0.000	0.000
54	A	54	ILE	0	-0.025	-0.018	25.193	-0.135	-0.135	0.000	0.000	0.000	0.000
55	A	55	SER	0	0.004	0.006	26.522	0.174	0.174	0.000	0.000	0.000	0.000
56	A	56	PRO	0	0.051	0.015	28.156	0.203	0.203	0.000	0.000	0.000	0.000
57	A	57	LYS	1	0.946	0.977	28.339	9.762	9.762	0.000	0.000	0.000	0.000
58	A	58	ARG	1	0.857	0.935	25.205	10.445	10.445	0.000	0.000	0.000	0.000
59	A	59	PHE	0	0.040	0.027	32.076	0.061	0.061	0.000	0.000	0.000	0.000
60	A	60	THR	0	0.050	0.002	32.460	0.202	0.202	0.000	0.000	0.000	0.000
61	A	61	HIS	0	-0.036	-0.011	31.111	0.294	0.294	0.000	0.000	0.000	0.000
62	A	62	GLY	0	0.056	0.022	34.174	0.092	0.092	0.000	0.000	0.000	0.000
63	A	63	LEU	0	-0.003	-0.001	37.677	0.156	0.156	0.000	0.000	0.000	0.000
64	A	64	LEU	0	0.008	0.012	32.474	0.131	0.131	0.000	0.000	0.000	0.000
65	A	65	LEU	0	-0.025	-0.010	35.043	0.131	0.131	0.000	0.000	0.000	0.000
66	A	66	LYS	1	0.944	0.986	38.015	6.493	6.493	0.000	0.000	0.000	0.000
67	A	67	ALA	0	0.035	0.015	39.798	0.146	0.146	0.000	0.000	0.000	0.000
68	A	68	ARG	1	0.825	0.913	37.976	7.428	7.428	0.000	0.000	0.000	0.000
69	A	69	ARG	1	0.961	0.991	38.617	6.675	6.675	0.000	0.000	0.000	0.000
70	A	70	PHE	0	-0.011	-0.021	31.199	-0.003	-0.003	0.000	0.000	0.000	0.000
71	A	71	SER	0	0.010	-0.006	35.332	-0.006	-0.006	0.000	0.000	0.000	0.000
72	A	72	ALA	0	-0.005	-0.005	29.772	-0.196	-0.196	0.000	0.000	0.000	0.000
73	A	73	SER	0	0.041	0.026	31.599	0.109	0.109	0.000	0.000	0.000	0.000
74	A	74	PHE	0	-0.029	-0.012	26.708	-0.312	-0.312	0.000	0.000	0.000	0.000
75	A	75	HIS	1	0.849	0.913	28.984	8.734	8.734	0.000	0.000	0.000	0.000
76	A	76	PRO	0	0.094	0.048	28.665	-0.375	-0.375	0.000	0.000	0.000	0.000
77	A	77	PHE	0	-0.004	-0.016	26.927	0.060	0.060	0.000	0.000	0.000	0.000
78	A	78	GLY	0	-0.015	-0.001	28.486	-0.028	-0.028	0.000	0.000	0.000	0.000
79	A	79	GLN	0	0.010	0.003	31.459	0.011	0.011	0.000	0.000	0.000	0.000
80	A	80	LYS	1	0.884	0.935	27.359	9.399	9.399	0.000	0.000	0.000	0.000
81	A	81	ASP	-1	-0.825	-0.902	29.114	-9.177	-9.177	0.000	0.000	0.000	0.000
82	A	82	LEU	0	0.022	0.020	31.565	0.029	0.029	0.000	0.000	0.000	0.000
83	A	83	VAL	0	0.022	-0.001	27.692	0.025	0.025	0.000	0.000	0.000	0.000
84	A	84	HIS	0	0.056	0.041	26.624	-0.265	-0.265	0.000	0.000	0.000	0.000
85	A	85	TRP	0	0.015	0.012	29.107	-0.056	-0.056	0.000	0.000	0.000	0.000
86	A	86	LEU	0	0.006	-0.001	31.963	0.072	0.072	0.000	0.000	0.000	0.000
87	A	87	GLY	0	-0.010	-0.014	28.446	0.030	0.030	0.000	0.000	0.000	0.000
88	A	88	SER	0	-0.087	-0.039	29.137	-0.242	-0.242	0.000	0.000	0.000	0.000
89	A	89	HIS	0	-0.017	0.001	30.695	0.152	0.152	0.000	0.000	0.000	0.000
90	A	90	SER	0	-0.070	-0.052	33.778	-0.072	-0.072	0.000	0.000	0.000	0.000
91	A	91	GLY	0	0.072	0.025	35.430	0.131	0.131	0.000	0.000	0.000	0.000
92	A	92	ARG	1	0.822	0.916	33.823	8.334	8.334	0.000	0.000	0.000	0.000
93	A	93	GLU	-1	-0.800	-0.886	37.204	-7.709	-7.709	0.000	0.000	0.000	0.000
94	A	94	VAL	0	0.010	0.003	38.117	0.123	0.123	0.000	0.000	0.000	0.000
95	A	95	ASP	-1	-0.788	-0.891	40.279	-6.866	-6.866	0.000	0.000	0.000	0.000
96	A	96	LYS	1	0.753	0.874	33.481	8.437	8.437	0.000	0.000	0.000	0.000
97	A	97	GLY	0	0.026	0.023	39.444	-0.085	-0.085	0.000	0.000	0.000	0.000
98	A	98	GLN	0	-0.044	-0.036	42.097	0.136	0.136	0.000	0.000	0.000	0.000
99	A	99	ALA	0	-0.044	-0.007	38.269	-0.007	-0.007	0.000	0.000	0.000	0.000
100	A	100	PRO	0	0.009	0.009	40.064	0.023	0.023	0.000	0.000	0.000	0.000
101	A	101	HIS	0	-0.020	-0.021	40.008	-0.163	-0.163	0.000	0.000	0.000	0.000
102	A	102	PHE	0	0.061	0.052	39.680	0.164	0.164	0.000	0.000	0.000	0.000
103	A	103	LEU	0	-0.028	-0.028	42.099	-0.140	-0.140	0.000	0.000	0.000	0.000
104	A	104	GLY	0	0.030	0.019	41.834	0.051	0.051	0.000	0.000	0.000	0.000
105	A	105	HIS	0	0.021	0.001	42.561	0.226	0.226	0.000	0.000	0.000	0.000
106	A	106	THR	0	-0.112	-0.082	41.548	0.085	0.085	0.000	0.000	0.000	0.000
107	A	107	GLY	0	0.006	0.003	44.082	0.008	0.008	0.000	0.000	0.000	0.000
108	A	108	VAL	0	-0.035	-0.002	38.833	0.004	0.004	0.000	0.000	0.000	0.000
109	A	109	PRO	0	0.019	0.023	38.812	0.060	0.060	0.000	0.000	0.000	0.000
110	A	110	ILE	0	0.003	0.009	36.586	-0.281	-0.281	0.000	0.000	0.000	0.000
111	A	111	LEU	0	-0.038	-0.011	34.152	0.098	0.098	0.000	0.000	0.000	0.000
112	A	112	GLU	-1	-0.850	-0.944	36.846	-6.953	-6.953	0.000	0.000	0.000	0.000
113	A	113	GLY	0	0.005	0.000	36.694	-0.193	-0.193	0.000	0.000	0.000	0.000
114	A	114	ALA	0	-0.081	-0.039	33.494	-0.225	-0.225	0.000	0.000	0.000	0.000
115	A	115	TYR	0	0.063	0.024	27.064	0.034	0.034	0.000	0.000	0.000	0.000
116	A	116	ALA	0	0.042	0.023	31.532	0.074	0.074	0.000	0.000	0.000	0.000
117	A	117	ALA	0	-0.040	-0.030	32.828	-0.178	-0.178	0.000	0.000	0.000	0.000
118	A	118	TYR	0	-0.006	0.016	28.791	0.158	0.158	0.000	0.000	0.000	0.000
119	A	119	GLU	-1	-0.724	-0.825	34.455	-6.899	-6.899	0.000	0.000	0.000	0.000
120	A	120	LEU	0	-0.041	-0.020	31.873	-0.054	-0.054	0.000	0.000	0.000	0.000
121	A	121	GLU	-1	-0.887	-0.949	35.943	-6.883	-6.883	0.000	0.000	0.000	0.000
122	A	122	LEU	0	-0.084	-0.042	33.518	-0.193	-0.193	0.000	0.000	0.000	0.000
123	A	123	LEU	0	0.004	0.019	33.998	0.176	0.176	0.000	0.000	0.000	0.000
124	A	124	GLU	-1	-0.864	-0.919	32.327	-8.463	-8.463	0.000	0.000	0.000	0.000
125	A	125	VAL	0	-0.023	-0.019	31.302	-0.127	-0.127	0.000	0.000	0.000	0.000
126	A	126	HIS	1	0.816	0.891	27.970	9.164	9.164	0.000	0.000	0.000	0.000
127	A	127	THR	0	0.007	0.001	27.464	-0.155	-0.155	0.000	0.000	0.000	0.000
128	A	128	PHE	0	-0.032	-0.022	22.543	-0.081	-0.081	0.000	0.000	0.000	0.000
129	A	129	GLY	0	0.003	0.011	22.976	-0.392	-0.392	0.000	0.000	0.000	0.000
130	A	130	ASP	-1	-0.877	-0.927	22.881	-11.490	-11.490	0.000	0.000	0.000	0.000
131	A	131	HIS	0	-0.050	-0.059	23.380	0.434	0.434	0.000	0.000	0.000	0.000
132	A	132	ASP	-1	-0.745	-0.837	25.678	-9.419	-9.419	0.000	0.000	0.000	0.000
133	A	133	LEU	0	-0.025	-0.009	24.256	-0.043	-0.043	0.000	0.000	0.000	0.000
134	A	134	PHE	0	0.017	-0.006	26.990	0.299	0.299	0.000	0.000	0.000	0.000
135	A	135	VAL	0	0.010	-0.004	28.478	-0.242	-0.242	0.000	0.000	0.000	0.000
136	A	136	GLY	0	0.042	0.012	30.624	0.283	0.283	0.000	0.000	0.000	0.000
137	A	137	ARG	1	0.976	0.984	32.182	7.177	7.177	0.000	0.000	0.000	0.000
138	A	138	VAL	0	-0.013	-0.008	32.548	0.109	0.109	0.000	0.000	0.000	0.000
139	A	139	VAL	0	-0.057	-0.038	35.267	0.108	0.108	0.000	0.000	0.000	0.000
140	A	140	ALA	0	0.001	0.007	38.196	0.188	0.188	0.000	0.000	0.000	0.000
141	A	141	VAL	0	-0.016	-0.012	34.971	-0.226	-0.226	0.000	0.000	0.000	0.000
142	A	142	TRP	0	-0.046	-0.027	36.711	0.216	0.216	0.000	0.000	0.000	0.000
143	A	143	GLU	-1	-0.922	-0.980	35.313	-8.043	-8.043	0.000	0.000	0.000	0.000
144	A	144	GLU	-1	-0.911	-0.943	36.289	-7.049	-7.049	0.000	0.000	0.000	0.000
145	A	145	GLU	-1	-0.859	-0.939	37.093	-7.049	-7.049	0.000	0.000	0.000	0.000
146	A	146	GLY	0	-0.049	-0.020	37.978	0.027	0.027	0.000	0.000	0.000	0.000
147	A	147	LEU	0	-0.044	-0.027	33.970	-0.229	-0.229	0.000	0.000	0.000	0.000
148	A	148	LEU	0	-0.010	0.006	31.645	-0.378	-0.378	0.000	0.000	0.000	0.000
149	A	149	ASP	-1	-0.864	-0.932	30.157	-8.923	-8.923	0.000	0.000	0.000	0.000
150	A	150	GLU	-1	-0.909	-0.966	33.481	-8.017	-8.017	0.000	0.000	0.000	0.000
151	A	151	LYS	1	0.880	0.941	30.593	8.842	8.842	0.000	0.000	0.000	0.000
152	A	152	GLY	0	0.075	0.049	31.325	-0.142	-0.142	0.000	0.000	0.000	0.000
153	A	153	ARG	1	0.819	0.904	26.640	9.525	9.525	0.000	0.000	0.000	0.000
154	A	154	PRO	0	0.006	0.004	26.884	0.230	0.230	0.000	0.000	0.000	0.000
155	A	155	LYS	1	0.918	0.963	28.393	8.388	8.388	0.000	0.000	0.000	0.000
156	A	156	PRO	0	0.036	0.016	26.340	-0.198	-0.198	0.000	0.000	0.000	0.000
157	A	157	GLY	0	-0.003	0.020	25.690	0.264	0.264	0.000	0.000	0.000	0.000
158	A	158	LEU	0	-0.002	-0.008	26.784	-0.036	-0.036	0.000	0.000	0.000	0.000
159	A	159	ALA	0	0.021	0.005	24.664	0.112	0.112	0.000	0.000	0.000	0.000
160	A	160	LEU	0	-0.014	0.001	25.103	-0.254	-0.254	0.000	0.000	0.000	0.000
161	A	161	LEU	0	-0.023	-0.009	19.104	-0.199	-0.199	0.000	0.000	0.000	0.000
162	A	162	TYR	0	-0.002	-0.006	20.605	0.075	0.075	0.000	0.000	0.000	0.000
163	A	163	TYR	0	0.059	0.004	14.920	-0.214	-0.214	0.000	0.000	0.000	0.000
164	A	164	GLY	0	-0.009	0.005	16.134	-0.760	-0.760	0.000	0.000	0.000	0.000
165	A	165	LYS	1	0.879	0.921	17.070	15.307	15.307	0.000	0.000	0.000	0.000
166	A	166	GLY	0	0.051	0.027	20.651	0.050	0.050	0.000	0.000	0.000	0.000
167	A	167	LEU	0	0.005	0.023	17.504	0.361	0.361	0.000	0.000	0.000	0.000
168	A	168	TYR	0	-0.014	-0.037	20.572	-0.329	-0.329	0.000	0.000	0.000	0.000
169	A	169	GLY	0	-0.012	-0.008	21.563	-0.149	-0.149	0.000	0.000	0.000	0.000
170	A	170	ARG	1	0.858	0.948	22.359	10.426	10.426	0.000	0.000	0.000	0.000
171	A	171	PRO	0	-0.023	-0.002	21.311	-0.482	-0.482	0.000	0.000	0.000	0.000
172	A	172	ALA	0	0.017	0.010	21.562	0.267	0.267	0.000	0.000	0.000	0.000
173	A	173	GLU	-1	-0.828	-0.939	23.277	-9.608	-9.608	0.000	0.000	0.000	0.000
174	A	174	GLU	-1	-0.920	-0.961	23.890	-10.691	-10.691	0.000	0.000	0.000	0.000
175	A	175	THR	0	-0.089	-0.047	23.350	-0.235	-0.235	0.000	0.000	0.000	0.000
176	A	176	PHE	0	0.005	0.004	21.115	0.134	0.134	0.000	0.000	0.000	0.000
177	A	177	ALA	0	-0.042	-0.025	22.821	-0.201	-0.201	0.000	0.000	0.000	0.000
178	A	178	PRO	-1	-0.939	-0.949	20.803	-10.705	-10.705	0.000	0.000	0.000	0.000

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