FMO DATABASE

FMODB ID: ZL9VN

Calculation Name: 4LMX-B-Xray547

Preferred Name:

Target Type:

Ligand Name: 15,16-dihydrobiliverdin | phycoerythrobilin | 5-hydroxylysine

Ligand 3-letter code: DBV | PEB | LYZ

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 4LMX

Chain ID: B

ChEMBL ID:

UniProt ID: U5TBU5

Base Structure: X-ray

Registration Date: 2025-10-04

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	177
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1584121.23385
FMO2-HF: Nuclear repulsion	1517966.716639
FMO2-HF: Total energy	-66154.517211
FMO2-MP2: Total energy	-66341.638382

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.
-86.917	-80.801	18.45	-12.503	-12.059	-0.123

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 : 0.793 / q_NPA : 0.893

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	ASP	-1	-0.767	-0.862	2.559	-50.677	-46.105	2.366	-2.941	-3.997	-0.026
4	A	4	ALA	0	-0.033	-0.004	3.247	6.667	7.404	0.025	-0.219	-0.542	-0.001
5	A	5	PHE	0	0.053	0.008	4.379	4.646	4.810	0.000	-0.022	-0.142	0.000
7	A	7	LYS	1	0.868	0.911	2.971	40.632	41.228	1.066	-0.546	-1.116	0.006
19	A	19	VAL	0	0.011	0.004	4.347	-4.694	-4.622	-0.001	-0.006	-0.065	0.000
23	A	23	ASP	-1	-0.819	-0.912	1.999	-135.132	-135.319	14.997	-8.731	-6.078	-0.102
24	A	24	LEU	0	-0.014	0.001	4.119	-0.629	-0.611	-0.001	-0.019	0.003	0.000
26	A	26	ALA	0	-0.025	-0.016	4.673	3.156	3.194	-0.001	-0.002	-0.034	0.000
27	A	27	LEU	0	0.006	-0.005	4.634	3.038	3.144	-0.001	-0.017	-0.088	0.000
6	A	6	SER	0	0.063	0.027	7.732	1.760	1.760	0.000	0.000	0.000	0.000
8	A	8	VAL	0	0.022	0.013	8.249	2.047	2.047	0.000	0.000	0.000	0.000
9	A	9	ILE	0	-0.027	0.005	10.633	1.950	1.950	0.000	0.000	0.000	0.000
10	A	10	THR	0	-0.028	-0.017	11.103	1.348	1.348	0.000	0.000	0.000	0.000
11	A	11	SER	0	-0.079	-0.018	11.318	0.798	0.798	0.000	0.000	0.000	0.000
12	A	12	ALA	0	0.023	-0.006	13.151	0.974	0.974	0.000	0.000	0.000	0.000
13	A	13	ASP	-1	-0.878	-0.941	12.165	-20.531	-20.531	0.000	0.000	0.000	0.000
14	A	14	GLY	0	-0.002	0.007	15.683	0.526	0.526	0.000	0.000	0.000	0.000
15	A	15	LYS	1	0.868	0.936	12.277	19.805	19.805	0.000	0.000	0.000	0.000
16	A	16	ALA	0	0.027	0.020	12.137	-0.946	-0.946	0.000	0.000	0.000	0.000
17	A	17	ALA	0	0.003	0.003	6.993	-0.733	-0.733	0.000	0.000	0.000	0.000
18	A	18	TYR	0	-0.023	-0.011	8.428	1.520	1.520	0.000	0.000	0.000	0.000
20	A	20	GLY	0	0.044	0.010	6.588	5.382	5.382	0.000	0.000	0.000	0.000
21	A	21	GLY	0	0.010	0.001	7.103	-4.509	-4.509	0.000	0.000	0.000	0.000
22	A	22	ALA	0	0.055	0.016	7.049	-0.183	-0.183	0.000	0.000	0.000	0.000
25	A	25	GLN	0	-0.032	-0.013	7.135	2.645	2.645	0.000	0.000	0.000	0.000
28	A	28	LYS	1	0.877	0.932	7.386	26.972	26.972	0.000	0.000	0.000	0.000
29	A	29	LYS	1	0.926	0.970	9.847	27.216	27.216	0.000	0.000	0.000	0.000
30	A	30	PHE	0	-0.029	-0.007	9.022	1.020	1.020	0.000	0.000	0.000	0.000
31	A	31	VAL	0	0.034	0.036	11.144	1.593	1.593	0.000	0.000	0.000	0.000
32	A	32	SER	0	0.040	0.020	14.136	0.165	0.165	0.000	0.000	0.000	0.000
33	A	33	GLU	-1	-0.814	-0.920	17.414	-14.134	-14.134	0.000	0.000	0.000	0.000
34	A	34	GLY	0	0.057	0.038	14.549	0.245	0.245	0.000	0.000	0.000	0.000
35	A	35	ASN	0	-0.015	-0.018	15.337	-1.637	-1.637	0.000	0.000	0.000	0.000
36	A	36	LYS	1	0.919	0.936	17.294	13.232	13.232	0.000	0.000	0.000	0.000
37	A	37	ARG	1	0.733	0.836	15.043	18.793	18.793	0.000	0.000	0.000	0.000
38	A	38	MET	0	-0.023	-0.008	12.891	-0.681	-0.681	0.000	0.000	0.000	0.000
39	A	39	ASP	-1	-0.891	-0.946	16.706	-14.846	-14.846	0.000	0.000	0.000	0.000
40	A	40	SER	0	-0.023	-0.026	20.380	0.852	0.852	0.000	0.000	0.000	0.000
41	A	41	VAL	0	0.014	0.010	16.028	0.507	0.507	0.000	0.000	0.000	0.000
42	A	42	ASN	0	-0.003	0.002	19.128	0.600	0.600	0.000	0.000	0.000	0.000
43	A	43	ALA	0	-0.015	-0.002	20.347	0.597	0.597	0.000	0.000	0.000	0.000
44	A	44	ILE	0	0.019	0.027	21.115	0.619	0.619	0.000	0.000	0.000	0.000
45	A	45	VAL	0	0.000	-0.016	18.808	0.508	0.508	0.000	0.000	0.000	0.000
46	A	46	SER	0	-0.045	-0.028	22.008	0.349	0.349	0.000	0.000	0.000	0.000
47	A	47	ASN	0	-0.057	-0.036	24.122	0.916	0.916	0.000	0.000	0.000	0.000
48	A	48	ALA	0	0.041	0.033	24.450	0.445	0.445	0.000	0.000	0.000	0.000
49	A	49	SER	0	0.042	0.010	26.575	0.226	0.226	0.000	0.000	0.000	0.000
50	A	50	CYS	0	-0.066	-0.027	29.651	0.254	0.254	0.000	0.000	0.000	0.000
51	A	51	ILE	0	0.054	0.032	27.007	0.278	0.278	0.000	0.000	0.000	0.000
52	A	52	VAL	0	0.006	0.022	28.728	0.270	0.270	0.000	0.000	0.000	0.000
53	A	53	SER	0	-0.020	-0.009	31.453	0.351	0.351	0.000	0.000	0.000	0.000
54	A	54	ASP	-1	-0.899	-0.936	34.572	-8.333	-8.333	0.000	0.000	0.000	0.000
55	A	55	SER	0	-0.001	-0.020	32.935	0.213	0.213	0.000	0.000	0.000	0.000
56	A	56	VAL	0	0.002	-0.012	34.499	0.203	0.203	0.000	0.000	0.000	0.000
57	A	57	SER	0	-0.039	-0.031	37.132	0.314	0.314	0.000	0.000	0.000	0.000
58	A	58	GLY	0	0.033	0.005	38.981	0.240	0.240	0.000	0.000	0.000	0.000
59	A	59	MET	0	-0.038	0.004	38.284	0.193	0.193	0.000	0.000	0.000	0.000
60	A	60	VAL	0	-0.040	-0.029	40.651	0.209	0.209	0.000	0.000	0.000	0.000
61	A	61	CYS	0	-0.061	-0.020	43.227	0.177	0.177	0.000	0.000	0.000	0.000
62	A	62	GLU	-1	-0.776	-0.841	42.530	-7.499	-7.499	0.000	0.000	0.000	0.000
63	A	63	ASN	0	0.005	0.024	44.649	0.288	0.288	0.000	0.000	0.000	0.000
64	A	64	PRO	0	0.076	0.039	45.737	-0.071	-0.071	0.000	0.000	0.000	0.000
65	A	65	SER	0	-0.063	-0.053	47.908	0.008	0.008	0.000	0.000	0.000	0.000
66	A	66	LEU	0	-0.021	-0.020	41.675	-0.017	-0.017	0.000	0.000	0.000	0.000
67	A	67	ILE	0	-0.015	-0.007	44.032	-0.123	-0.123	0.000	0.000	0.000	0.000
68	A	68	ALA	0	0.030	0.031	45.922	0.100	0.100	0.000	0.000	0.000	0.000
69	A	69	PRO	0	0.025	-0.012	48.228	-0.126	-0.126	0.000	0.000	0.000	0.000
70	A	70	ASN	0	-0.048	-0.028	48.023	0.043	0.043	0.000	0.000	0.000	0.000
71	A	71	GLY	0	0.047	0.059	46.037	-0.080	-0.080	0.000	0.000	0.000	0.000
72	A	72	GLY	0	0.002	-0.010	41.871	-0.085	-0.085	0.000	0.000	0.000	0.000
73	A	73	VAL	0	-0.008	-0.024	38.745	-0.169	-0.169	0.000	0.000	0.000	0.000
74	A	74	TYR	0	0.018	0.034	41.383	0.041	0.041	0.000	0.000	0.000	0.000
75	A	75	THR	0	-0.018	-0.029	43.492	-0.110	-0.110	0.000	0.000	0.000	0.000
76	A	76	ASN	0	0.065	0.013	40.202	-0.172	-0.172	0.000	0.000	0.000	0.000
77	A	77	ARG	1	0.962	0.990	39.029	7.444	7.444	0.000	0.000	0.000	0.000
78	A	78	LYS	1	0.891	0.948	37.814	7.238	7.238	0.000	0.000	0.000	0.000
79	A	79	MET	0	0.040	0.034	37.590	-0.260	-0.260	0.000	0.000	0.000	0.000
80	A	80	ALA	0	0.002	0.001	35.136	-0.235	-0.235	0.000	0.000	0.000	0.000
81	A	81	ALA	0	-0.021	-0.006	33.329	-0.328	-0.328	0.000	0.000	0.000	0.000
82	A	82	CYS	0	0.038	0.018	32.646	-0.235	-0.235	0.000	0.000	0.000	0.000
83	A	83	LEU	0	-0.006	0.003	32.723	-0.259	-0.259	0.000	0.000	0.000	0.000
84	A	84	ARG	1	0.867	0.908	28.464	9.841	9.841	0.000	0.000	0.000	0.000
85	A	85	ASP	-1	-0.761	-0.844	28.099	-10.673	-10.673	0.000	0.000	0.000	0.000
86	A	86	ALA	0	0.027	0.017	28.119	-0.358	-0.358	0.000	0.000	0.000	0.000
87	A	87	GLU	-1	-0.818	-0.902	25.238	-12.540	-12.540	0.000	0.000	0.000	0.000
88	A	88	ILE	0	-0.034	-0.016	23.422	-0.660	-0.660	0.000	0.000	0.000	0.000
89	A	89	ILE	0	0.037	0.016	23.205	-0.671	-0.671	0.000	0.000	0.000	0.000
90	A	90	LEU	0	-0.015	0.000	23.911	-0.502	-0.502	0.000	0.000	0.000	0.000
91	A	91	ARG	1	0.820	0.892	20.246	13.273	13.273	0.000	0.000	0.000	0.000
92	A	92	TYR	0	0.063	0.039	18.167	-1.261	-1.261	0.000	0.000	0.000	0.000
93	A	93	VAL	0	0.002	0.017	19.554	-0.713	-0.713	0.000	0.000	0.000	0.000
94	A	94	SER	0	-0.074	-0.053	19.202	-0.615	-0.615	0.000	0.000	0.000	0.000
95	A	95	TYR	0	0.059	0.006	11.645	-1.597	-1.597	0.000	0.000	0.000	0.000
96	A	96	SER	0	-0.015	0.003	15.548	-1.119	-1.119	0.000	0.000	0.000	0.000
97	A	97	LEU	0	-0.028	-0.008	17.267	-0.517	-0.517	0.000	0.000	0.000	0.000
98	A	98	LEU	0	-0.050	-0.019	11.583	-0.379	-0.379	0.000	0.000	0.000	0.000
99	A	99	SER	0	-0.068	-0.053	12.402	-1.389	-1.389	0.000	0.000	0.000	0.000
100	A	100	GLY	0	-0.017	-0.005	13.421	-0.874	-0.874	0.000	0.000	0.000	0.000
101	A	101	ASP	-1	-0.853	-0.892	14.540	-19.052	-19.052	0.000	0.000	0.000	0.000
102	A	102	SER	0	0.013	-0.031	17.569	-0.200	-0.200	0.000	0.000	0.000	0.000
103	A	103	SER	0	-0.069	-0.048	15.998	0.467	0.467	0.000	0.000	0.000	0.000
104	A	104	VAL	0	0.013	-0.005	14.080	0.561	0.561	0.000	0.000	0.000	0.000
105	A	105	LEU	0	-0.017	0.000	17.495	0.549	0.549	0.000	0.000	0.000	0.000
106	A	106	GLU	-1	-0.794	-0.882	20.738	-12.430	-12.430	0.000	0.000	0.000	0.000
107	A	107	ASP	-1	-0.894	-0.957	19.436	-13.982	-13.982	0.000	0.000	0.000	0.000
108	A	108	ARG	1	0.862	0.921	16.597	16.322	16.322	0.000	0.000	0.000	0.000
109	A	109	CYS	0	-0.089	-0.029	20.914	0.297	0.297	0.000	0.000	0.000	0.000
110	A	110	LEU	0	-0.005	0.000	23.571	0.553	0.553	0.000	0.000	0.000	0.000
111	A	111	ASN	0	-0.016	0.012	23.920	0.998	0.998	0.000	0.000	0.000	0.000
112	A	112	GLY	0	0.076	0.049	26.654	-0.026	-0.026	0.000	0.000	0.000	0.000
113	A	113	LEU	0	-0.042	-0.005	27.807	0.354	0.354	0.000	0.000	0.000	0.000
114	A	114	LYS	1	0.829	0.895	30.255	8.865	8.865	0.000	0.000	0.000	0.000
115	A	115	GLU	-1	-0.945	-0.963	33.318	-8.670	-8.670	0.000	0.000	0.000	0.000
116	A	116	THR	0	-0.002	-0.004	31.752	0.243	0.243	0.000	0.000	0.000	0.000
117	A	117	TYR	0	-0.033	-0.054	31.168	0.209	0.209	0.000	0.000	0.000	0.000
118	A	118	ALA	0	-0.007	0.006	35.821	0.256	0.256	0.000	0.000	0.000	0.000
119	A	119	SER	0	-0.077	-0.044	36.864	0.224	0.224	0.000	0.000	0.000	0.000
120	A	120	LEU	0	-0.033	-0.020	35.031	0.157	0.157	0.000	0.000	0.000	0.000
121	A	121	GLY	0	-0.013	0.009	39.252	0.124	0.124	0.000	0.000	0.000	0.000
122	A	122	VAL	0	-0.053	-0.028	36.008	0.112	0.112	0.000	0.000	0.000	0.000
123	A	123	PRO	0	-0.014	-0.008	38.937	-0.058	-0.058	0.000	0.000	0.000	0.000
124	A	124	ALA	0	0.081	0.029	37.623	-0.107	-0.107	0.000	0.000	0.000	0.000
125	A	125	ALA	0	0.014	0.011	38.042	-0.155	-0.155	0.000	0.000	0.000	0.000
126	A	126	GLY	0	0.028	0.007	39.788	-0.040	-0.040	0.000	0.000	0.000	0.000
127	A	127	ASN	0	0.029	0.010	33.565	-0.296	-0.296	0.000	0.000	0.000	0.000
128	A	128	ALA	0	0.037	0.018	34.829	-0.244	-0.244	0.000	0.000	0.000	0.000
129	A	129	ARG	1	0.785	0.856	35.734	7.942	7.942	0.000	0.000	0.000	0.000
130	A	130	THR	0	0.050	0.021	33.112	-0.095	-0.095	0.000	0.000	0.000	0.000
131	A	131	ILE	0	0.003	-0.002	30.230	-0.235	-0.235	0.000	0.000	0.000	0.000
132	A	132	SER	0	-0.061	-0.037	31.935	-0.151	-0.151	0.000	0.000	0.000	0.000
133	A	133	ILE	0	0.028	0.026	34.347	-0.031	-0.031	0.000	0.000	0.000	0.000
134	A	134	MET	0	-0.006	0.022	29.111	-0.257	-0.257	0.000	0.000	0.000	0.000
135	A	135	LYS	1	0.759	0.879	29.552	9.883	9.883	0.000	0.000	0.000	0.000
136	A	136	ALA	0	0.013	0.001	30.613	-0.157	-0.157	0.000	0.000	0.000	0.000
137	A	137	THR	0	-0.014	-0.016	31.005	0.050	0.050	0.000	0.000	0.000	0.000
138	A	138	VAL	0	-0.022	-0.010	25.306	-0.141	-0.141	0.000	0.000	0.000	0.000
139	A	139	ILE	0	0.027	0.009	28.034	-0.215	-0.215	0.000	0.000	0.000	0.000
140	A	140	GLY	0	0.037	0.040	29.723	0.065	0.065	0.000	0.000	0.000	0.000
141	A	141	PHE	0	-0.031	-0.032	27.848	0.103	0.103	0.000	0.000	0.000	0.000
142	A	142	ILE	0	-0.021	-0.009	24.214	0.013	0.013	0.000	0.000	0.000	0.000
143	A	143	THR	0	-0.054	-0.039	27.584	0.095	0.095	0.000	0.000	0.000	0.000
144	A	144	ASN	0	-0.025	-0.010	30.363	0.360	0.360	0.000	0.000	0.000	0.000
145	A	145	ASN	0	0.010	-0.002	32.558	0.558	0.558	0.000	0.000	0.000	0.000
146	A	146	SER	0	-0.025	-0.012	32.508	0.185	0.185	0.000	0.000	0.000	0.000
147	A	147	GLN	0	-0.023	-0.013	34.531	0.062	0.062	0.000	0.000	0.000	0.000
148	A	148	GLN	0	0.034	0.010	36.826	-0.153	-0.153	0.000	0.000	0.000	0.000
149	A	149	LYS	1	0.912	0.955	28.668	10.836	10.836	0.000	0.000	0.000	0.000
150	A	150	LYS	1	0.875	0.952	31.636	9.066	9.066	0.000	0.000	0.000	0.000
151	A	151	LEU	0	0.029	0.016	25.361	-0.163	-0.163	0.000	0.000	0.000	0.000
152	A	152	SER	0	-0.021	-0.006	26.617	0.395	0.395	0.000	0.000	0.000	0.000
153	A	153	THR	0	-0.002	0.004	23.906	-0.377	-0.377	0.000	0.000	0.000	0.000
154	A	154	PRO	0	-0.003	-0.009	24.100	0.471	0.471	0.000	0.000	0.000	0.000
155	A	155	ALA	0	0.006	0.012	27.139	-0.060	-0.060	0.000	0.000	0.000	0.000
156	A	156	GLY	0	0.005	-0.010	28.250	-0.104	-0.104	0.000	0.000	0.000	0.000
157	A	157	ASP	-1	-0.797	-0.863	28.835	-10.826	-10.826	0.000	0.000	0.000	0.000
158	A	158	CYS	0	-0.008	-0.002	25.336	-0.759	-0.759	0.000	0.000	0.000	0.000
159	A	159	SER	0	-0.002	-0.023	26.412	-0.322	-0.322	0.000	0.000	0.000	0.000
160	A	160	ALA	0	0.016	0.026	24.661	0.053	0.053	0.000	0.000	0.000	0.000
161	A	161	LEU	0	0.031	0.013	19.772	-0.139	-0.139	0.000	0.000	0.000	0.000
162	A	162	ALA	0	-0.018	-0.006	23.697	-0.101	-0.101	0.000	0.000	0.000	0.000
163	A	163	SER	0	-0.005	-0.018	26.866	0.356	0.356	0.000	0.000	0.000	0.000
164	A	164	GLU	-1	-0.773	-0.830	19.733	-16.394	-16.394	0.000	0.000	0.000	0.000
165	A	165	VAL	0	0.003	-0.004	22.991	-0.038	-0.038	0.000	0.000	0.000	0.000
166	A	166	GLY	0	0.006	-0.002	24.440	0.255	0.255	0.000	0.000	0.000	0.000
167	A	167	GLY	0	0.060	0.028	26.606	0.295	0.295	0.000	0.000	0.000	0.000
168	A	168	TYR	0	-0.030	-0.039	19.535	0.175	0.175	0.000	0.000	0.000	0.000
169	A	169	PHE	0	0.051	0.006	24.890	0.118	0.118	0.000	0.000	0.000	0.000
170	A	170	ASP	-1	-0.789	-0.857	28.006	-9.864	-9.864	0.000	0.000	0.000	0.000
171	A	171	LYS	1	0.817	0.909	24.159	12.787	12.787	0.000	0.000	0.000	0.000
172	A	172	VAL	0	-0.004	-0.006	26.096	0.191	0.191	0.000	0.000	0.000	0.000
173	A	173	SER	0	-0.038	-0.037	28.360	0.382	0.382	0.000	0.000	0.000	0.000
174	A	174	SER	0	-0.048	-0.045	30.678	0.380	0.380	0.000	0.000	0.000	0.000
175	A	175	ALA	0	-0.014	0.010	28.902	0.188	0.188	0.000	0.000	0.000	0.000
176	A	176	LEU	0	-0.048	-0.031	30.404	0.151	0.151	0.000	0.000	0.000	0.000
177	A	177	ALA	-1	-0.839	-0.887	33.529	-8.206	-8.206	0.000	0.000	0.000	0.000

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