wwPDB validation report of PDB entry 7I1B

THE STRUCTURES ARE BASED ON 2630 INTERPROTON DISTANCE
RESTRAINTS DERIVED FROM NOE MEASUREMENTS; 114 HYDROGEN
BONDING DISTANCE RESTRAINTS FOR 57 HYDROGEN-BONDS
IDENTIFIED ON THE BASIS OF THE NOE AND AMIDE PROTON
EXCHANGE DATA, AS WELL AS THE INITIAL STRUCTURE
CALCULATIONS; 36 DISTANCE RESTRAINTS RELATING TO NH-H2O-CO
BRIDGING HYDROGEN BONDS INVOLVING 7 BOUND WATER MOLECULES
AND IDENTIFIED FROM ROE MEASUREMENTS; AND 152 PHI AND 115
PSI BACKBONE TORSION ANGLE RESTRAINTS AND 99 CHI SIDE CHAIN
TORSION ANGLE RESTRAINTS DERIVED FROM COUPLING CONSTRAINTS
AND NOE DATA. THE LATTER ARE OBTAINED USING THE
CONFORMATIONAL GRID SEARCH PROGRAM "STEREOSEARCH" (M.
NILGES, G. M. CLORE, AND A. M. GRONENBORN (1990)
BIOPOLYMERS 29, 813-822). THE METHOD USED TO DETERMINE THE
STRUCTURES IS THE HYBRID METRIC MATRIX DISTANCE
GEOMETRY-DYNAMICAL SIMULATED ANNEALING METHOD (M. NILGES,
G. M. CLORE, AND A. M. GRONENBORN, (1990) FEBS LETT. 229,
317-324).

THE QUANTITY PRESENTED IN THE B-VALUE FIELD IN THIS
COORDINATE FILE REPRESENTS THE ATOMIC RMS DEVIATION OF THE
INDIVIDUAL STRUCTURES ABOUT THE MEAN COORDINATE POSITIONS.

THE RESTRAINED MINIMIZED AVERAGE STRUCTURE CAN BE FOUND IN
PDB ENTRY 6I1B. IT WAS OBTAINED BY AVERAGING THE
COORDINATES OF THE INDIVIDUAL STRUCTURES AND SUBJECTING THE
RESULTING COORDINATES TO RESTRAINED MINIMIZATION.

HIGH-RESOLUTION THREE-DIMENSIONAL STRUCTURE OF INTERLEUKIN-1 BETA IN SOLUTION BY THREE-AND FOUR-DIMENSIONAL NUCLEAR 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