FMO DATABASE

FMODB ID: 15RGZ

Calculation Name: 2B67-A-Xray547

Preferred Name:

Target Type:

Ligand Name: flavin mononucleotide | acetic acid

Ligand 3-letter code: FMN | ACY

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2B67

Chain ID: A

ChEMBL ID:

UniProt ID: A0A0H2

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	201
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-2179801.147015
FMO2-HF: Nuclear repulsion	2101376.108756
FMO2-HF: Total energy	-78425.038259
FMO2-MP2: Total energy	-78657.627489

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.
10.451	13.603	0.001	-1.16	-1.994	-0.003

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 : 0.917 / q_NPA : 0.936

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	PHE	0	0.107	0.057	3.757	2.801	5.018	-0.004	-0.918	-1.296	-0.002
4	A	4	LEU	0	-0.001	0.009	3.344	5.482	6.218	0.006	-0.222	-0.520	-0.001
5	A	5	GLU	-1	-0.885	-0.935	4.957	-29.298	-29.099	-0.001	-0.020	-0.178	0.000
6	A	6	LEU	0	0.020	0.004	6.984	3.756	3.756	0.000	0.000	0.000	0.000
7	A	7	ASN	0	-0.023	-0.026	8.189	5.658	5.658	0.000	0.000	0.000	0.000
8	A	8	LYS	1	0.916	0.962	7.400	36.861	36.861	0.000	0.000	0.000	0.000
9	A	9	LYS	1	0.893	0.948	10.387	28.940	28.940	0.000	0.000	0.000	0.000
10	A	10	ARG	1	0.975	1.014	12.878	21.387	21.387	0.000	0.000	0.000	0.000
11	A	11	HIS	0	-0.018	-0.016	14.830	0.691	0.691	0.000	0.000	0.000	0.000
12	A	12	ALA	0	-0.042	-0.024	17.903	0.331	0.331	0.000	0.000	0.000	0.000
13	A	13	THR	0	-0.026	-0.009	21.128	0.356	0.356	0.000	0.000	0.000	0.000
14	A	14	LYS	1	0.906	0.959	23.360	12.269	12.269	0.000	0.000	0.000	0.000
15	A	15	HIS	0	0.004	-0.004	26.934	0.714	0.714	0.000	0.000	0.000	0.000
16	A	16	PHE	0	-0.037	-0.023	25.050	-0.553	-0.553	0.000	0.000	0.000	0.000
17	A	17	THR	0	0.006	0.006	27.457	0.356	0.356	0.000	0.000	0.000	0.000
18	A	18	ASP	-1	-0.886	-0.944	29.848	-9.451	-9.451	0.000	0.000	0.000	0.000
19	A	19	LYS	1	0.813	0.935	24.445	12.747	12.747	0.000	0.000	0.000	0.000
20	A	20	LEU	0	0.041	0.008	29.341	-0.259	-0.259	0.000	0.000	0.000	0.000
21	A	21	VAL	0	0.035	0.022	25.459	-0.331	-0.331	0.000	0.000	0.000	0.000
22	A	22	ASP	-1	-0.768	-0.874	26.483	-10.517	-10.517	0.000	0.000	0.000	0.000
23	A	23	PRO	0	-0.023	-0.031	27.011	-0.346	-0.346	0.000	0.000	0.000	0.000
24	A	24	LYS	1	0.905	0.953	26.308	10.155	10.155	0.000	0.000	0.000	0.000
25	A	25	ASP	-1	-0.815	-0.886	22.735	-13.480	-13.480	0.000	0.000	0.000	0.000
26	A	26	VAL	0	-0.004	-0.006	22.569	-0.540	-0.540	0.000	0.000	0.000	0.000
27	A	27	ARG	1	0.833	0.909	24.288	11.188	11.188	0.000	0.000	0.000	0.000
28	A	28	THR	0	0.009	-0.007	19.582	-0.136	-0.136	0.000	0.000	0.000	0.000
29	A	29	ALA	0	0.007	0.002	19.530	-0.596	-0.596	0.000	0.000	0.000	0.000
30	A	30	ILE	0	0.001	-0.005	20.267	-0.411	-0.411	0.000	0.000	0.000	0.000
31	A	31	GLU	-1	-0.889	-0.923	22.010	-12.334	-12.334	0.000	0.000	0.000	0.000
32	A	32	ILE	0	0.026	0.012	15.594	-0.294	-0.294	0.000	0.000	0.000	0.000
33	A	33	ALA	0	-0.014	-0.005	18.055	-0.427	-0.427	0.000	0.000	0.000	0.000
34	A	34	THR	0	-0.067	-0.058	19.671	-0.077	-0.077	0.000	0.000	0.000	0.000
35	A	35	LEU	0	-0.003	0.013	16.682	0.372	0.372	0.000	0.000	0.000	0.000
36	A	36	ALA	0	-0.030	-0.002	17.472	-0.601	-0.601	0.000	0.000	0.000	0.000
37	A	37	PRO	0	-0.007	0.005	16.739	0.840	0.840	0.000	0.000	0.000	0.000
38	A	38	SER	0	0.057	0.016	19.669	0.321	0.321	0.000	0.000	0.000	0.000
39	A	39	ALA	0	0.019	0.019	23.333	0.092	0.092	0.000	0.000	0.000	0.000
40	A	40	HIS	1	0.826	0.894	25.898	10.348	10.348	0.000	0.000	0.000	0.000
41	A	41	ASN	0	0.027	0.020	24.233	0.035	0.035	0.000	0.000	0.000	0.000
42	A	42	SER	0	-0.009	-0.010	25.713	0.267	0.267	0.000	0.000	0.000	0.000
43	A	43	GLN	0	0.009	0.000	25.479	0.383	0.383	0.000	0.000	0.000	0.000
44	A	44	PRO	0	0.000	0.017	26.794	0.265	0.265	0.000	0.000	0.000	0.000
45	A	45	TRP	0	0.064	0.026	22.563	0.306	0.306	0.000	0.000	0.000	0.000
46	A	46	LYS	1	0.883	0.944	29.247	9.255	9.255	0.000	0.000	0.000	0.000
47	A	47	PHE	0	0.041	0.023	24.280	-0.029	-0.029	0.000	0.000	0.000	0.000
48	A	48	VAL	0	-0.002	0.002	29.696	0.210	0.210	0.000	0.000	0.000	0.000
49	A	49	VAL	0	-0.008	-0.008	28.707	-0.171	-0.171	0.000	0.000	0.000	0.000
50	A	50	VAL	0	-0.032	-0.007	31.339	0.270	0.270	0.000	0.000	0.000	0.000
51	A	51	ARG	1	0.898	0.935	29.436	9.983	9.983	0.000	0.000	0.000	0.000
52	A	52	GLU	-1	-0.852	-0.923	35.305	-8.302	-8.302	0.000	0.000	0.000	0.000
53	A	53	LYS	1	0.843	0.916	38.417	7.737	7.737	0.000	0.000	0.000	0.000
54	A	54	ASN	0	0.013	0.012	33.697	0.190	0.190	0.000	0.000	0.000	0.000
55	A	55	ALA	0	0.063	0.023	36.997	-0.037	-0.037	0.000	0.000	0.000	0.000
56	A	56	GLU	-1	-0.970	-0.989	39.956	-7.252	-7.252	0.000	0.000	0.000	0.000
57	A	57	LEU	0	0.008	-0.003	33.636	0.008	0.008	0.000	0.000	0.000	0.000
58	A	58	ALA	0	0.033	0.013	36.329	-0.086	-0.086	0.000	0.000	0.000	0.000
59	A	59	LYS	1	0.910	0.959	37.335	7.280	7.280	0.000	0.000	0.000	0.000
60	A	60	LEU	0	-0.015	0.012	37.674	0.142	0.142	0.000	0.000	0.000	0.000
61	A	61	ALA	0	-0.030	-0.008	34.069	-0.129	-0.129	0.000	0.000	0.000	0.000
62	A	62	TYR	0	0.007	-0.008	35.101	0.209	0.209	0.000	0.000	0.000	0.000
63	A	63	GLY	0	0.028	0.012	34.725	-0.264	-0.264	0.000	0.000	0.000	0.000
64	A	64	SER	0	0.059	0.030	32.332	-0.007	-0.007	0.000	0.000	0.000	0.000
65	A	65	ASN	0	-0.045	-0.021	30.620	-0.564	-0.564	0.000	0.000	0.000	0.000
66	A	66	PHE	0	0.005	0.020	32.758	-0.098	-0.098	0.000	0.000	0.000	0.000
67	A	67	GLU	-1	-0.802	-0.911	34.275	-8.685	-8.685	0.000	0.000	0.000	0.000
68	A	68	GLN	0	-0.055	-0.019	28.070	-0.582	-0.582	0.000	0.000	0.000	0.000
69	A	69	VAL	0	-0.017	-0.020	31.349	-0.188	-0.188	0.000	0.000	0.000	0.000
70	A	70	SER	0	-0.068	-0.042	32.954	0.149	0.149	0.000	0.000	0.000	0.000
71	A	71	SER	0	-0.035	-0.023	32.223	0.193	0.193	0.000	0.000	0.000	0.000
72	A	72	ALA	0	-0.045	-0.005	29.241	-0.142	-0.142	0.000	0.000	0.000	0.000
73	A	73	PRO	0	-0.009	-0.006	29.243	0.193	0.193	0.000	0.000	0.000	0.000
74	A	74	VAL	0	-0.044	-0.018	28.448	0.201	0.201	0.000	0.000	0.000	0.000
75	A	75	THR	0	0.030	0.016	29.263	-0.323	-0.323	0.000	0.000	0.000	0.000
76	A	76	ILE	0	-0.030	-0.016	25.251	0.274	0.274	0.000	0.000	0.000	0.000
77	A	77	ALA	0	0.035	0.026	28.741	-0.208	-0.208	0.000	0.000	0.000	0.000
78	A	78	LEU	0	-0.044	-0.016	25.458	-0.001	-0.001	0.000	0.000	0.000	0.000
79	A	79	PHE	0	0.044	0.002	29.479	0.104	0.104	0.000	0.000	0.000	0.000
80	A	80	THR	0	-0.047	-0.055	29.683	-0.184	-0.184	0.000	0.000	0.000	0.000
81	A	81	ASP	-1	-0.794	-0.862	32.202	-8.554	-8.554	0.000	0.000	0.000	0.000
82	A	82	THR	0	0.009	-0.019	34.614	-0.024	-0.024	0.000	0.000	0.000	0.000
83	A	83	ASP	-1	-0.823	-0.902	37.135	-7.679	-7.679	0.000	0.000	0.000	0.000
84	A	84	LEU	0	0.037	0.004	32.498	-0.088	-0.088	0.000	0.000	0.000	0.000
85	A	85	ALA	0	0.014	0.018	35.721	-0.101	-0.101	0.000	0.000	0.000	0.000
86	A	86	LYS	1	0.877	0.924	38.149	7.381	7.381	0.000	0.000	0.000	0.000
87	A	87	ARG	1	0.686	0.855	30.095	9.952	9.952	0.000	0.000	0.000	0.000
88	A	88	ALA	0	0.042	0.021	33.390	-0.149	-0.149	0.000	0.000	0.000	0.000
89	A	89	ARG	1	0.942	0.947	34.448	7.451	7.451	0.000	0.000	0.000	0.000
90	A	90	LYS	1	0.866	0.944	33.103	9.190	9.190	0.000	0.000	0.000	0.000
91	A	91	ILE	0	0.017	0.027	29.646	0.035	0.035	0.000	0.000	0.000	0.000
92	A	92	ALA	0	0.019	0.012	32.554	-0.016	-0.016	0.000	0.000	0.000	0.000
93	A	93	ARG	1	0.909	0.952	35.069	7.917	7.917	0.000	0.000	0.000	0.000
94	A	94	VAL	0	-0.045	-0.020	32.143	0.139	0.139	0.000	0.000	0.000	0.000
95	A	95	GLY	0	0.023	0.028	31.797	-0.084	-0.084	0.000	0.000	0.000	0.000
96	A	96	GLY	0	0.037	0.016	32.473	0.050	0.050	0.000	0.000	0.000	0.000
97	A	97	ALA	0	0.041	-0.001	34.142	-0.205	-0.205	0.000	0.000	0.000	0.000
98	A	98	ASN	0	-0.030	-0.004	32.960	0.078	0.078	0.000	0.000	0.000	0.000
99	A	99	ASN	0	-0.080	-0.041	28.708	-0.546	-0.546	0.000	0.000	0.000	0.000
100	A	100	PHE	0	-0.072	-0.024	28.558	-0.289	-0.289	0.000	0.000	0.000	0.000
101	A	101	SER	0	0.072	0.018	32.285	0.294	0.294	0.000	0.000	0.000	0.000
102	A	102	GLU	-1	-0.868	-0.947	34.590	-7.512	-7.512	0.000	0.000	0.000	0.000
103	A	103	GLU	-1	-0.938	-0.965	35.178	-8.337	-8.337	0.000	0.000	0.000	0.000
104	A	104	GLN	0	0.038	0.029	28.881	0.131	0.131	0.000	0.000	0.000	0.000
105	A	105	LEU	0	0.011	0.014	33.871	-0.059	-0.059	0.000	0.000	0.000	0.000
106	A	106	GLN	0	0.013	0.002	36.454	0.124	0.124	0.000	0.000	0.000	0.000
107	A	107	TYR	0	-0.001	-0.005	31.197	-0.019	-0.019	0.000	0.000	0.000	0.000
108	A	108	PHE	0	0.019	0.001	28.980	0.047	0.047	0.000	0.000	0.000	0.000
109	A	109	MET	0	-0.013	-0.007	35.223	0.067	0.067	0.000	0.000	0.000	0.000
110	A	110	LYS	1	0.892	0.949	38.908	7.241	7.241	0.000	0.000	0.000	0.000
111	A	111	ASN	0	0.019	0.016	37.038	0.091	0.091	0.000	0.000	0.000	0.000
112	A	112	LEU	0	0.051	0.024	31.394	0.008	0.008	0.000	0.000	0.000	0.000
113	A	113	PRO	0	-0.052	-0.025	35.964	0.004	0.004	0.000	0.000	0.000	0.000
114	A	114	ALA	0	0.049	0.034	38.859	0.086	0.086	0.000	0.000	0.000	0.000
115	A	115	GLU	-1	-0.912	-0.938	33.950	-9.007	-9.007	0.000	0.000	0.000	0.000
116	A	116	PHE	0	-0.007	-0.014	32.025	-0.008	-0.008	0.000	0.000	0.000	0.000
117	A	117	ALA	0	-0.029	-0.010	37.642	0.040	0.040	0.000	0.000	0.000	0.000
118	A	118	ARG	1	0.869	0.921	40.093	7.895	7.895	0.000	0.000	0.000	0.000
119	A	119	TYR	0	-0.016	0.004	32.983	-0.234	-0.234	0.000	0.000	0.000	0.000
120	A	120	SER	0	0.042	0.021	38.747	0.101	0.101	0.000	0.000	0.000	0.000
121	A	121	GLU	-1	-0.864	-0.947	38.238	-7.732	-7.732	0.000	0.000	0.000	0.000
122	A	122	GLN	0	-0.061	-0.028	34.164	0.058	0.058	0.000	0.000	0.000	0.000
123	A	123	GLN	0	0.038	0.025	34.207	-0.174	-0.174	0.000	0.000	0.000	0.000
124	A	124	VAL	0	0.016	-0.002	33.391	-0.361	-0.361	0.000	0.000	0.000	0.000
125	A	125	SER	0	0.016	0.021	33.446	-0.272	-0.272	0.000	0.000	0.000	0.000
126	A	126	ASP	-1	-0.817	-0.906	30.554	-10.043	-10.043	0.000	0.000	0.000	0.000
127	A	127	TYR	0	-0.020	-0.014	29.124	-0.525	-0.525	0.000	0.000	0.000	0.000
128	A	128	LEU	0	-0.028	-0.009	28.580	-0.472	-0.472	0.000	0.000	0.000	0.000
129	A	129	ALA	0	0.061	0.034	28.481	-0.363	-0.363	0.000	0.000	0.000	0.000
130	A	130	LEU	0	0.000	0.008	23.468	-0.499	-0.499	0.000	0.000	0.000	0.000
131	A	131	ASN	0	-0.028	-0.046	23.792	-0.919	-0.919	0.000	0.000	0.000	0.000
132	A	132	ALA	0	0.024	0.016	24.233	-0.380	-0.380	0.000	0.000	0.000	0.000
133	A	133	GLY	0	0.018	0.010	22.849	-0.363	-0.363	0.000	0.000	0.000	0.000
134	A	134	LEU	0	-0.049	-0.023	18.962	-0.774	-0.774	0.000	0.000	0.000	0.000
135	A	135	VAL	0	-0.007	0.001	19.189	-0.826	-0.826	0.000	0.000	0.000	0.000
136	A	136	ALA	0	0.029	0.013	20.874	-0.301	-0.301	0.000	0.000	0.000	0.000
137	A	137	MET	0	-0.023	-0.007	14.181	-0.301	-0.301	0.000	0.000	0.000	0.000
138	A	138	ASN	0	-0.034	-0.026	15.396	-2.060	-2.060	0.000	0.000	0.000	0.000
139	A	139	LEU	0	0.018	0.014	16.946	-0.411	-0.411	0.000	0.000	0.000	0.000
140	A	140	VAL	0	0.017	0.002	16.846	-0.216	-0.216	0.000	0.000	0.000	0.000
141	A	141	LEU	0	-0.060	-0.008	11.680	-0.749	-0.749	0.000	0.000	0.000	0.000
142	A	142	ALA	0	0.029	0.015	14.780	-0.649	-0.649	0.000	0.000	0.000	0.000
143	A	143	LEU	0	-0.010	-0.002	16.353	0.476	0.476	0.000	0.000	0.000	0.000
144	A	144	THR	0	-0.029	-0.023	13.858	0.092	0.092	0.000	0.000	0.000	0.000
145	A	145	ASP	-1	-0.999	-0.999	11.475	-25.168	-25.168	0.000	0.000	0.000	0.000
146	A	146	GLN	0	-0.055	-0.023	14.142	0.608	0.608	0.000	0.000	0.000	0.000
147	A	147	GLY	0	-0.022	-0.010	16.768	0.879	0.879	0.000	0.000	0.000	0.000
148	A	148	ILE	0	-0.087	-0.042	18.261	0.882	0.882	0.000	0.000	0.000	0.000
149	A	149	GLY	0	0.044	0.031	19.899	-0.685	-0.685	0.000	0.000	0.000	0.000
150	A	150	SER	0	0.025	-0.020	20.254	0.427	0.427	0.000	0.000	0.000	0.000
151	A	151	ASN	0	-0.018	-0.006	21.648	-0.916	-0.916	0.000	0.000	0.000	0.000
152	A	152	ILE	0	-0.014	0.003	20.494	0.274	0.274	0.000	0.000	0.000	0.000
153	A	153	ILE	0	-0.020	-0.004	24.417	0.134	0.134	0.000	0.000	0.000	0.000
154	A	154	LEU	0	0.037	0.006	28.053	0.124	0.124	0.000	0.000	0.000	0.000
155	A	155	GLY	0	-0.024	-0.005	29.739	0.310	0.310	0.000	0.000	0.000	0.000
156	A	156	PHE	0	0.014	-0.001	30.970	0.013	0.013	0.000	0.000	0.000	0.000
157	A	157	ASP	-1	-0.767	-0.846	35.209	-7.736	-7.736	0.000	0.000	0.000	0.000
158	A	158	LYS	1	0.845	0.918	31.472	9.863	9.863	0.000	0.000	0.000	0.000
159	A	159	SER	0	-0.088	-0.059	37.561	0.073	0.073	0.000	0.000	0.000	0.000
160	A	160	LYS	1	0.977	0.979	40.689	7.411	7.411	0.000	0.000	0.000	0.000
161	A	161	VAL	0	-0.024	-0.011	35.346	-0.001	-0.001	0.000	0.000	0.000	0.000
162	A	162	ASN	0	-0.040	-0.038	38.790	-0.185	-0.185	0.000	0.000	0.000	0.000
163	A	163	GLU	-1	-0.910	-0.943	40.552	-6.917	-6.917	0.000	0.000	0.000	0.000
164	A	164	VAL	0	0.015	0.002	39.773	0.008	0.008	0.000	0.000	0.000	0.000
165	A	165	LEU	0	-0.065	-0.045	35.527	-0.101	-0.101	0.000	0.000	0.000	0.000
166	A	166	GLU	-1	-0.851	-0.903	39.723	-7.492	-7.492	0.000	0.000	0.000	0.000
167	A	167	ILE	0	-0.107	-0.048	37.001	-0.126	-0.126	0.000	0.000	0.000	0.000
168	A	168	GLU	-1	-0.890	-0.952	40.210	-7.277	-7.277	0.000	0.000	0.000	0.000
169	A	169	ASP	-1	-0.826	-0.920	40.161	-7.683	-7.683	0.000	0.000	0.000	0.000
170	A	170	ARG	1	0.788	0.876	36.679	8.277	8.277	0.000	0.000	0.000	0.000
171	A	171	PHE	0	-0.075	-0.039	34.596	-0.264	-0.264	0.000	0.000	0.000	0.000
172	A	172	ARG	1	0.910	0.944	31.909	9.750	9.750	0.000	0.000	0.000	0.000
173	A	173	PRO	0	0.017	0.023	33.551	-0.373	-0.373	0.000	0.000	0.000	0.000
174	A	174	GLU	-1	-0.831	-0.895	29.039	-10.225	-10.225	0.000	0.000	0.000	0.000
175	A	175	LEU	0	-0.022	-0.035	24.808	-0.068	-0.068	0.000	0.000	0.000	0.000
176	A	176	LEU	0	0.029	0.028	28.944	0.134	0.134	0.000	0.000	0.000	0.000
177	A	177	ILE	0	-0.011	-0.006	23.477	-0.382	-0.382	0.000	0.000	0.000	0.000
178	A	178	THR	0	0.025	0.025	26.374	0.130	0.130	0.000	0.000	0.000	0.000
179	A	179	VAL	0	-0.017	-0.026	24.040	-0.663	-0.663	0.000	0.000	0.000	0.000
180	A	180	GLY	0	0.052	0.017	24.825	0.582	0.582	0.000	0.000	0.000	0.000
181	A	181	TYR	0	0.009	-0.001	22.214	-0.338	-0.338	0.000	0.000	0.000	0.000
182	A	182	THR	0	0.024	0.000	22.180	0.434	0.434	0.000	0.000	0.000	0.000
183	A	183	ASP	-1	-0.914	-0.953	24.404	-10.858	-10.858	0.000	0.000	0.000	0.000
184	A	184	GLU	-1	-0.910	-0.951	24.720	-11.583	-11.583	0.000	0.000	0.000	0.000
185	A	185	LYS	1	0.899	0.958	21.534	11.590	11.590	0.000	0.000	0.000	0.000
186	A	186	LEU	0	0.001	-0.006	20.614	0.625	0.625	0.000	0.000	0.000	0.000
187	A	187	GLU	-1	-0.870	-0.927	18.640	-16.829	-16.829	0.000	0.000	0.000	0.000
188	A	188	PRO	0	-0.063	-0.026	14.686	-0.004	-0.004	0.000	0.000	0.000	0.000
189	A	189	SER	0	0.015	0.009	16.812	0.424	0.424	0.000	0.000	0.000	0.000
190	A	190	TYR	0	0.040	0.010	17.479	-0.857	-0.857	0.000	0.000	0.000	0.000
191	A	191	ARG	1	0.844	0.908	14.871	17.516	17.516	0.000	0.000	0.000	0.000
192	A	192	LEU	0	0.054	0.040	17.807	0.029	0.029	0.000	0.000	0.000	0.000
193	A	193	PRO	0	0.015	0.013	16.774	-1.194	-1.194	0.000	0.000	0.000	0.000
194	A	194	VAL	0	0.027	-0.004	12.875	0.331	0.331	0.000	0.000	0.000	0.000
195	A	195	ASP	-1	-0.935	-0.982	15.795	-17.334	-17.334	0.000	0.000	0.000	0.000
196	A	196	GLU	-1	-0.968	-0.970	18.675	-12.308	-12.308	0.000	0.000	0.000	0.000
197	A	197	ILE	0	-0.060	-0.034	15.820	0.398	0.398	0.000	0.000	0.000	0.000
198	A	198	ILE	0	-0.091	-0.030	14.561	-0.413	-0.413	0.000	0.000	0.000	0.000
199	A	199	GLU	-1	-0.791	-0.871	19.189	-11.699	-11.699	0.000	0.000	0.000	0.000
200	A	200	LYS	1	0.884	0.931	18.849	15.231	15.231	0.000	0.000	0.000	0.000
201	A	201	ARG	0	-0.074	-0.039	23.178	-0.390	-0.390	0.000	0.000	0.000	0.000

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