wwPDB validation report of PDB entry 1ITI

THE NUMBERING SCHEME IN THIS STRUCTURE INCLUDES THE
FOUR-RESIDUE SEQUENCE GLU-ALA-GLU-ALA AT THE N-TERMINUS OF
THE RECOMBINANT PROTEIN WHICH IS NOT PART OF THE NATURAL
HUMAN IL-4; THE NATURAL IL-4 SEQUENCE THEREFORE STARTS AT
RESIDUE 5.
THE TWO POTENTIAL N-LINKED GLYCOSYLATION SITES AT ASN 42
AND ASN 109 IN THE NATURAL SEQUENCE WERE CHANGED TO ASP TO
PREVENT HYPERGLYCOSYLATION IN THE YEAST HOST.

DETAILS OF THE STRUCTURE DETERMINATION AND ALL STRUCTURAL
STATISTICS ARE GIVEN IN THE REFERENCE LISTED ON THE JRNL
RECORDS ABOVE (I.E. AGREEMENT WITH EXPERIMENTAL RESTRAINTS,
DEVIATIONS FROM IDEALITY FOR BOND LENGTHS, ANGLES, PLANES
AND CHIRALITY, NON-BONDED CONTACTS, ATOMIC RMS DIFFERENCES
BETWEEN THE CALCULATED STRUCTURES).

THE STRUCTURES ARE BASED ON A TOTAL OF 2973 EXPERIMENTAL
NMR RESTRAINTS COMPRISING: 2515 INTERPROTON DISTANCE
RESTRAINTS DERIVED FROM NOE MEASUREMENTS; 102
HYDROGEN-BONDING DISTANCE RESTRAINTS FOR 51 HYDROGEN-BONDS
IDENTIFIED ON THE BASIS OF THE NOE AND AMIDE PROTON
EXCHANGE DATA, AS WELL AS THE INITIAL STRUCTURE
CALCULATIONS; AND 130 PHI, 119 PSI, 73 CHI1, 32 CHI2 AND
2 CHI3 TORSION ANGLE RESTRAINTS DERIVED FROM COUPLING
CONSTANTS, NOE DATA, AND 13C SECONDARY CHEMICAL SHIFTS.

THE METHOD USED TO DETERMINE THE STRUCTURES IS THE HYBRID
METRIC MATRIX DISTANCE GEOMETRY-DYNAMICAL SIMULATED
ANNEALING METHOD [NILGES, M., CLORE, G.M. & GRONENBORN,
A.M., FEBS LETT. 229, 317-324 (1988)].

A TOTAL OF 30 STRUCTURES WERE CALCULATED. THE ATOMIC RMS
DISTRIBUTION ABOUT THE MEAN COORDINATE POSITIONS FOR
RESIDUES 8 - 129 IS 0.44 (+/-0.03) ANGSTROMS FOR THE
BACKBONE ATOMS, 0.83 (+/-0.03) ANGSTROMS FOR ALL ATOMS,
AND 0.51 (+/-0.04) ANGSTROMS FOR ALL ATOMS EXCLUDING
DISORDERED SIDE CHAINS. THE N- (RESIDUES 1 - 7) AND C-
(RESIDUES 130 - 133) TERMINAL RESIDUES ARE DISORDERED.

THE COORDINATES OF THE RESTRAINED MINIMIZED STRUCTURE ARE
LISTED FIRST AS MODEL 0. THIS (SA)R RESTRAINED MINIMIZED
MEAN STRUCTURE WAS DERIVED BY AVERAGING THE COORDINATES OF
THE INDIVIDUAL SA STRUCTURES (BEST FITTED TO RESIDUES 8 -
129) AND SUBJECTING THE RESULTING COORDINATES TO RESTRAINED
MINIMIZATION. THE QUANTITY PRESENTED IN THE TEMPERATURE
FACTOR FIELD (COLUMNS 61 - 66) REPRESENTS THE ATOMIC RMS
DEVIATIONS OF THE 30 INDIVIDUAL SA STRUCTURES ABOUT THE
MEAN STRUCTURE. RESIDUES 1 - 7 AND 130 - 133 AT THE N-
AND C-TERMINI, RESPECTIVELY, ARE DISORDERED.

THE HIGH RESOLUTION THREE-DIMENSIONAL SOLUTION STRUCTURE OF HUMAN INTERLEUKIN-4 DETERMINED BY MULTI-DIMENSIONAL HETERONUCLEAR MAGNETIC RESONANCE SPECTROSCOPY

geometric validation package for ligand chemistry in protein x-ray structures
assessment of nmr assigned chemical shifts
geometric validation of nmr ensemble structure
20191225.v01 (using entries in the PDB archive December 25th 2019)
domain identification of nmr ensemble structure
classification of nmr ensemble structure
nmr chemical shift validation and reference correction
random coil index prediction from nmr chemical shifts