Properties

Disulfide bonds

Other bonds (neither disulfide, covalent nor hydrogen bonds, e.g. Zinc–sulphur bond)

Non-standard residues

Sequence alignments

• Entity_assembly_ID (NMR): A vs Auth_asym_ID (model): A

--------10--------20----
VXXXXLCXPGCTXXGGGXNCXFCX
||||||||||||||||||||||||
VXXXXLCXPGCTXXGGGXNCXFCX

Chain assignments

Content subtype: combined_19619_2mh5.nef

Assigned chemical shifts

1. Saveframe: assigned_chem_shift_list_1
   • Status: Error
   • Sequence coverage of experimental data
     • Entity_assembly_ID: A, Chain length: 24, Sequence coverage: 100.0%

     --------10--------20----
     VXXXXLCXPGCTXXGGGXNCXFCX
     ||||||||||||||||||||||||
     VXXXXLCXPGCTXXGGGXNCXFCX
     

   • Total number of assignments
     • ¹H chemical shifts: 106
     • ¹³C chemical shifts: 40
   • Completeness of assignments
     • Entity_assemble_ID: A
       • Excluded Comp_ID in statistics

         Comp_index_ID	Comp_ID
         4	5CW
         8	DBB
         24	TEE

       • All atoms

         Atom group	# of target shifts	# of assigned shifts	Completeness (%)
         1H chemical shifts	91	80	87.9
         13C chemical shifts	71	30	42.3

       • Backbone atoms

         Atom group	# of target shifts	# of assigned shifts	Completeness (%)
         1H chemical shifts	42	38	90.5
         13C chemical shifts	38	9	23.7

       • Side chain atoms

         Atom group	# of target shifts	# of assigned shifts	Completeness (%)
         1H chemical shifts	49	42	85.7
         13C chemical shifts	33	21	63.6

       • Methyl group atoms

         Atom group	# of target shifts	# of assigned shifts	Completeness (%)
         1H chemical shifts	10	7	70.0
         13C chemical shifts	10	6	60.0

       • Aromatic group atoms

         Atom group	# of target shifts	# of assigned shifts	Completeness (%)
         1H chemical shifts	5	4	80.0
         13C chemical shifts	5	4	80.0

   • Redox state of CYS
     • A:7:CYS, CA: None ppm, CB: 38.745 ppm
       • Redox_state (pred. by CS): oxidized
       • Disulfide_bond (coordinates): False, Other_bond (coordinates): False
     • A:11:CYS, CA: None ppm, CB: 38.733 ppm
       • Redox_state (pred. by CS): oxidized
       • Disulfide_bond (coordinates): False, Other_bond (coordinates): False
     • A:20:CYS, CA: 57.59 ppm, CB: None ppm
       • Redox_state (pred. by CS): oxidized 51.0%, reduced 49.0%
       • Disulfide_bond (coordinates): False, Other_bond (coordinates): False
     • A:23:CYS, CA: None ppm, CB: 33.962 ppm
       • Redox_state (pred. by CS): oxidized 76.7%, reduced 23.3%
       • Disulfide_bond (coordinates): False, Other_bond (coordinates): False
   • Peptide bond of PRO
     • A:9:PRO, CB: None ppm, CG: 28.22 ppm
       • Peptide_bond (pred. by CS): trans
       • Peptide_bond (coordinates): trans
   • Rotameric state of ILE , LEU, and VAL
     • A:1:VAL, CG1: 20.543 ppm, CG2: 20.796 ppm
       • Rotameric_state (pred. by CS): gauche+ 48.3%, trans 26.4%, gauche- 25.3%
       • Rotameric_state (coordinates): gauche+
     • A:6:LEU, CD1: 24.1 ppm, CD2: 24.654 ppm
       • Rotameric_state (pred. by CS): gauche+ 55.5%, trans 44.5%, gauche- 0.0%
       • Rotameric_state (coordinates): trans
   • Histogram of normalized assigned chemical shifts
   • Random coil index and derived parameters (S² and NMR RMSD)
     • Chain_ID: A

Covalent bonds

1. Saveframe: assembly
   • Status: OK

Distance restraints

1. Saveframe: CNS/XPLOR_distance_constraints_3
   • Status: OK
   • Experiment type: noe
   • Sequence coverage of experimental data
     • Entity_assembly_ID: A, Chain length: 24, Sequence coverage: 37.5%
   • Total number of restraints: 42
     • Intra-residue restraints, i = j : 30
     • Long range restraints, | i - j | >= 5 : 12
   • Weight of restraints: 1.0 (42)
     • Intra-residue restraints, i = j : 1.0 (30)
     • Long range restraints, | i - j | >= 5 : 1.0 (12)
   • Potential type of restraints: square-well-parabolic (42)
     • Intra-residue restraints, i = j : square-well-parabolic (30)
     • Long range restraints, | i - j | >= 5 : square-well-parabolic (12)
   • Range of distance target values: 1.66, 4.75 (Å)
   • Histogram of distance target values
   • Distance restraints per residue
     • Chain_ID: A
     • Chain_ID: B
       None
   • Distance restraints on contact map

Dihedral angle restraints

1. Saveframe: CNS/XPLOR_dihedral_2
   • Status: OK
   • Experiment type: .
   • Sequence coverage of experimental data
     • Entity_assembly_ID: A, Chain length: 24, Sequence coverage: 66.7%

     --------10--------20----
     VXXXXLCXPGCTXXGGGXNCXFCX
     ||  ||| |||||||||||     
     VX..XLC.PGCTXXGGGXN     
     --------10---------     
     

   • Total number of restraints: 21
     • Psi angle constraints: 8
     • Phi angle constraints: 13
   • Total number of restraints per polymer type: 21
     • Protein: 21
   • Weight of restraints: 1.0 (21)
     • Psi angle constraints: 1.0 (8)
     • Phi angle constraints: 1.0 (13)
   • Potential type of restraints: square-well-parabolic (21)
     • Psi angle constraints: square-well-parabolic (8)
     • Phi angle constraints: square-well-parabolic (13)
   • Plot of Phi-Psi angle restraints
   • Dihedral angle restraints per residue
     • Chain_ID: A