Validation of helical tilt angles in the solution NMR structure of the Z domain of Staphylococcal protein A by combined analysis of residual dipolar coupling and NOE data

Protein Science

Volumn 13, Issue 2, 2004, Pages 549-554

  Zheng, Deyou ^a,c   Aramini, James M ^a,c   Montelione, Gaetano T ^a,b,c,d  

^a RUTGERS UNIVERSITY   (United States)

^b RUTGERS ROBERT WOOD JOHNSON MEDICAL SCHOOL   (United States)

^c NE Structural Genomics Consortium ^*  (United States)

^d RUTGERS UNIVERSITY   (United States)

Author keywords

Residual dipolar coupling; Structure refinement; Z domain

Indexed keywords

IMMUNOGLOBULIN; STAPHYLOCOCCUS PROTEIN A;

ARTICLE; BACTERIAL VIRULENCE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN STRUCTURE; STAPHYLOCOCCUS AUREUS; VALIDATION PROCESS; X RAY CRYSTALLOGRAPHY;

BINDING SITES; IMMUNOGLOBULIN G; MODELS, MOLECULAR; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SENSITIVITY AND SPECIFICITY; SOLUTIONS; STAPHYLOCOCCAL PROTEIN A; STAPHYLOCOCCUS;

BACTERIA (MICROORGANISMS); STAPHYLOCOCCUS; STAPHYLOCOCCUS AUREUS;

EID: 1642493921     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.03351704     Document Type: Article

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