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LongText Report for: 3C6Y-pdb

Name Class
3C6Y-pdb
HEADER    LYASE                                   06-FEB-08   3C6Y              
TITLE     HNL FROM HEVEA BRASILIENSIS TO ATOMIC RESOLUTION                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HYDROXYNITRILASE;                                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: (S)-ACETONE-CYANOHYDRIN LYASE, (S)-HYDROXYNITRILE           
COMPND   5 LYASE, OXYNITRILASE;                                                 
COMPND   6 EC: 4.1.2.37;                                                        
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HEVEA BRASILIENSIS;                             
SOURCE   3 ORGANISM_COMMON: PARA RUBBER TREE;                                   
SOURCE   4 GENE: HNL;                                                           
SOURCE   5 EXPRESSION_SYSTEM: PICHIA PASTORIS;                                  
SOURCE   6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: BHIL-D2                                   
KEYWDS    ATOMIC RESOLUTION, HYDROXYNITRIL LYASE, CATALYSIS,                    
KEYWDS   2 PROTONATION STATE, AB INITIO CALCULATIONS, SUBSTRATE BINDING         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.SCHMIDT                                                             
REVDAT   1   03-JUN-08 3C6Y    0                                                
JRNL        AUTH   A.SCHMIDT,K.GRUBER,C.KRATKY,V.S.LAMZIN                       
JRNL        TITL   ATOMIC RESOLUTION STRUCTURES AND QUANTUM CHEMISTRY           
JRNL        TITL 2 MEET TO REVEAL SUBTLETIES OF HYDROXYNITRILE LYASE            
JRNL        TITL 3 CATALYSIS                                                    
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   J.ZUEGG,K.GRUBER,M.GUGGANIG,U.G.WAGNER,C.KRATKY              
REMARK   1  TITL   THREE-DIMENSIONAL STRUCTURES OF ENZYME-SUBSTRATE             
REMARK   1  TITL 2 COMPLEXES OF THE HYDROXYNITRILE LYASE FROM HEVEA             
REMARK   1  TITL 3 BRASILIENSIS                                                 
REMARK   1  REF    PROTEIN SCI.                  V.   8  1990 1999              
REMARK   1  REFN   ASTM PRCIEI  US ISSN 0961-8368                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   K.GRUBER,M.GUGGANIG,U.G.WAGNER,C.KRATKY                      
REMARK   1  TITL   ATOMIC RESOLUTION CRYSTAL STRUCTURE OF                       
REMARK   1  TITL 2 HYDROXYNITRILE LYASE FROM HEVEA BRASILIENSIS                 
REMARK   1  REF    BIOL.CHEM.                    V. 380   993 1999              
REMARK   1  REFN                GE ISSN 1431-6730                               
REMARK   2                                                                      
REMARK   2 RESOLUTION. 1.25 ANGSTROMS.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : SHELXL-97                                            
REMARK   3   AUTHORS     : G.M.SHELDRICK                                        
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.25                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 15.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 92.5                           
REMARK   3   CROSS-VALIDATION METHOD           : FREE R INITIALLY, FINAL        
REMARK   3                                       REFINEMENT AGAINST ALL         
REMARK   3                                       ADATA                          
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).                         
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : 0.127                  
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.127                  
REMARK   3   FREE R VALUE                  (NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 83123                  
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).                     
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : 0.106                  
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : 64103                  
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS      : 4328                                          
REMARK   3   NUCLEIC ACID ATOMS : 0                                             
REMARK   3   HETEROGEN ATOMS    : 24                                            
REMARK   3   SOLVENT ATOMS      : 550                                           
REMARK   3                                                                      
REMARK   3  MODEL REFINEMENT.                                                   
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : 2552.60                 
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : 2013.38                 
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : 34                      
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : 24616                   
REMARK   3   NUMBER OF RESTRAINTS                     : 30456                   
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.                        
REMARK   3   BOND LENGTHS                         (A) : 0.012                   
REMARK   3   ANGLE DISTANCES                      (A) : 0.028                   
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000                   
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : 0.028                   
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : 0.072                   
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.079                   
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : 0.060                   
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : 0.004                   
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : 0.040                   
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : 0.093                   
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED: NULL                                                  
REMARK   3                                                                      
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER                      
REMARK   3   SPECIAL CASE: NULL                                                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: FULL ANISOTROPIC REFINEMENT APPLIED       
REMARK   4                                                                      
REMARK   4 3C6Y COMPLIES WITH FORMAT V. 3.1, 01-AUG-2007                        
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ.                               
REMARK 100 THE RCSB ID CODE IS RCSB046418.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-MAR-2005                        
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : EMBL/DESY, HAMBURG                 
REMARK 200  BEAMLINE                       : X11                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.8162                             
REMARK 200  MONOCHROMATOR                  : SI                                 
REMARK 200  OPTICS                         : MIRROR                             
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 83123                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.250                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 15.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 3.500                              
REMARK 200  R MERGE                    (I) : 0.05700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 19.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.25                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.26                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 60.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.54000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 1.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MR/RIGID BODY PLACEMENT      
REMARK 200 SOFTWARE USED: REFMAC (RIGID BODY)                                   
REMARK 200 STARTING MODEL: PDB ENTRY 1QJ4                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.20                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.75                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2% PEG400, 2M AMMONIUM SULPHATE,         
REMARK 280  0.1M HEPES-NA, PH7.5, VAPOR DIFFUSION, HANGING DROP,                
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,1/2+Z                                             
REMARK 290       3555   -X,Y,1/2-Z                                              
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   1/2+X,1/2+Y,Z                                           
REMARK 290       6555   1/2-X,1/2-Y,1/2+Z                                       
REMARK 290       7555   1/2-X,1/2+Y,1/2-Z                                       
REMARK 290       8555   1/2+X,1/2-Y,-Z                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       64.10300            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       64.10300            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       23.62450            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       53.05200            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       23.62450            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       53.05200            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       64.10300            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       23.62450            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       53.05200            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       64.10300            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       23.62450            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       53.05200            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4550 ANGSTROM**2                          
REMARK 350 TOTAL SURFACE AREA FOR THE COMPLEX: 19020 ANGSTROM**2                
REMARK 350 GAIN IN SOLVENT FREE ENERGY: -98 KCAL/MOL                            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000      106.10400            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A3006   LIES ON A SPECIAL POSITION.                         
REMARK 375      HOH A3068   LIES ON A SPECIAL POSITION.                         
REMARK 375      HOH A3138   LIES ON A SPECIAL POSITION.                         
REMARK 375      HOH A3352   LIES ON A SPECIAL POSITION.                         
REMARK 375      HOH A3578   LIES ON A SPECIAL POSITION.                         
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                 
REMARK 465                                                                      
REMARK 465   M RES C  SSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI                             
REMARK 500   O    HOH A  3318     O    HOH A  3401              1.74            
REMARK 500   O    HOH A  3304     O    HOH A  3481              2.07            
REMARK 500   O    HOH A  3469     O    HOH A  3471              2.07            
REMARK 500   O    HOH A  3273     O    HOH A  3315              2.08            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCELIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    HIS A  31   CG  -  ND1 -  CE1 ANGL. DEV. =  11.9 DEGREES          
REMARK 500    HIS A  31   ND1 -  CE1 -  NE2 ANGL. DEV. =  -7.7 DEGREES          
REMARK 500    GLU A 123   OE1 -  CD  -  OE2 ANGL. DEV. =   9.2 DEGREES          
REMARK 500    ARG A 154   NE  -  CZ  -  NH1 ANGL. DEV. =   4.6 DEGREES          
REMARK 500    ARG A 154   NE  -  CZ  -  NH2 ANGL. DEV. =  -7.4 DEGREES          
REMARK 500    LEU A 178   O   -  C   -  N   ANGL. DEV. = -11.2 DEGREES          
REMARK 500    ASP A 225   CB  -  CG  -  OD1 ANGL. DEV. =  -5.8 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A  80     -114.23     50.31                                   
REMARK 500    LYS A 129     -121.15     62.43                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M=MODEL NUMBER;                               
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A3196        DISTANCE =  5.10 ANGSTROMS                       
REMARK 525    HOH A3254        DISTANCE =  5.52 ANGSTROMS                       
REMARK 525    HOH A3267        DISTANCE =  5.35 ANGSTROMS                       
REMARK 525    HOH A3495        DISTANCE =  7.10 ANGSTROMS                       
REMARK 525    HOH A3537        DISTANCE =  6.63 ANGSTROMS                       
REMARK 525    HOH A3608        DISTANCE =  7.26 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 SITE_DESCRIPTION: SO4 BINDING SITE FOR RESIDUE A 2001                
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 SITE_DESCRIPTION: SO4 BINDING SITE FOR RESIDUE A 2002                
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 SITE_DESCRIPTION: SO4 BINDING SITE FOR RESIDUE A 2003                
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 SITE_DESCRIPTION: SO4 BINDING SITE FOR RESIDUE A 2004                
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 SITE_DESCRIPTION: BME BINDING SITE FOR RESIDUE A 2005                
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 SITE_DESCRIPTION: ACN BINDING SITE FOR RESIDUE A 1001                
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 SITE_DESCRIPTION: PEG BINDING SITE FOR RESIDUE A 1501                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1QJ4   RELATED DB: PDB                                   
REMARK 900 HNL AT ATOMIC RESOLUTION                                             
REMARK 900 RELATED ID: 7YAS   RELATED DB: PDB                                   
REMARK 900 HNL LOW TEMPERATURE NATIVE STRUCTURE                                 
REMARK 900 RELATED ID: 3C6X   RELATED DB: PDB                                   
REMARK 900 HNL FROM HEVEA BRASILIENSIS TO ATOMIC RESOLUTION, NATIVE             
REMARK 900 WITH PEG200                                                          
REMARK 900 RELATED ID: 3C6Z   RELATED DB: PDB                                   
REMARK 900 HNL FROM HEVEA BRASILIENSIS TO ATOMIC RESOLUTION, COMPLEX            
REMARK 900 WITH ISOPROPANOL                                                     
REMARK 900 RELATED ID: 3C70   RELATED DB: PDB                                   
REMARK 900 HNL FROM HEVEA BRASILIENSIS TO ATOMIC RESOLUTION, COMPLEX            
REMARK 900 WITH RHODANIDE (SCN)                                                 
DBREF  3C6Y A    1   257  UNP    P52704   HNL_HEVBR        1    257             
SEQRES   1 A  257  MET ALA PHE ALA HIS PHE VAL LEU ILE HIS THR ILE CYS          
SEQRES   2 A  257  HIS GLY ALA TRP ILE TRP HIS LYS LEU LYS PRO LEU LEU          
SEQRES   3 A  257  GLU ALA LEU GLY HIS LYS VAL THR ALA LEU ASP LEU ALA          
SEQRES   4 A  257  ALA SER GLY VAL ASP PRO ARG GLN ILE GLU GLU ILE GLY          
SEQRES   5 A  257  SER PHE ASP GLU TYR SER GLU PRO LEU LEU THR PHE LEU          
SEQRES   6 A  257  GLU ALA LEU PRO PRO GLY GLU LYS VAL ILE LEU VAL GLY          
SEQRES   7 A  257  GLU SER CYS GLY GLY LEU ASN ILE ALA ILE ALA ALA ASP          
SEQRES   8 A  257  LYS TYR CYS GLU LYS ILE ALA ALA ALA VAL PHE HIS ASN          
SEQRES   9 A  257  SER VAL LEU PRO ASP THR GLU HIS CYS PRO SER TYR VAL          
SEQRES  10 A  257  VAL ASP LYS LEU MET GLU VAL PHE PRO ASP TRP LYS ASP          
SEQRES  11 A  257  THR THR TYR PHE THR TYR THR LYS ASP GLY LYS GLU ILE          
SEQRES  12 A  257  THR GLY LEU LYS LEU GLY PHE THR LEU LEU ARG GLU ASN          
SEQRES  13 A  257  LEU TYR THR LEU CYS GLY PRO GLU GLU TYR GLU LEU ALA          
SEQRES  14 A  257  LYS MET LEU THR ARG LYS GLY SER LEU PHE GLN ASN ILE          
SEQRES  15 A  257  LEU ALA LYS ARG PRO PHE PHE THR LYS GLU GLY TYR GLY          
SEQRES  16 A  257  SER ILE LYS LYS ILE TYR VAL TRP THR ASP GLN ASP GLU          
SEQRES  17 A  257  ILE PHE LEU PRO GLU PHE GLN LEU TRP GLN ILE GLU ASN          
SEQRES  18 A  257  TYR LYS PRO ASP LYS VAL TYR LYS VAL GLU GLY GLY ASP          
SEQRES  19 A  257  HIS LYS LEU GLN LEU THR LYS THR LYS GLU ILE ALA GLU          
SEQRES  20 A  257  ILE LEU GLN GLU VAL ALA ASP THR TYR ASN                      
HET    SO4  A2001       5                                                       
HET    SO4  A2002       5                                                       
HET    SO4  A2003       5                                                       
HET    SO4  A2004       5                                                       
HET    BME  A2005       4                                                       
HET    ACN  A1001       8                                                       
HET    PEG  A1501       7                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     BME BETA-MERCAPTOETHANOL                                             
HETNAM     ACN ACETONE                                                          
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
FORMUL   2  SO4    4(O4 S 2-)                                                   
FORMUL   6  BME    C2 H6 O S                                                    
FORMUL   7  ACN    C3 H6 O                                                      
FORMUL   8  PEG    C4 H10 O3                                                    
FORMUL   9  HOH   *534(H2 O)                                                    
HELIX    1   1 GLY A   15  HIS A   20  5                                   6    
HELIX    2   2 LYS A   21  LEU A   29  1                                   9    
HELIX    3   3 GLN A   47  ILE A   51  5                                   5    
HELIX    4   4 SER A   53  SER A   58  1                                   6    
HELIX    5   5 SER A   58  ALA A   67  1                                  10    
HELIX    6   6 CYS A   81  CYS A   94  1                                  14    
HELIX    7   7 SER A  115  PHE A  125  1                                  11    
HELIX    8   8 GLY A  149  LEU A  157  1                                   9    
HELIX    9   9 GLY A  162  THR A  173  1                                  12    
HELIX   10  10 PHE A  179  ARG A  186  1                                   8    
HELIX   11  11 GLY A  193  ILE A  197  5                                   5    
HELIX   12  12 LEU A  211  TYR A  222  1                                  12    
HELIX   13  13 LYS A  236  LYS A  241  1                                   6    
HELIX   14  14 LYS A  241  TYR A  256  1                                  16    
SHEET    1   A 6 LYS A  32  LEU A  36  0                                        
SHEET    2   A 6 HIS A   5  ILE A   9  1  N  LEU A   8   O  THR A  34           
SHEET    3   A 6 VAL A  74  SER A  80  1  O  VAL A  77   N  ILE A   9           
SHEET    4   A 6 ILE A  97  SER A 105  1  O  VAL A 101   N  LEU A  76           
SHEET    5   A 6 LYS A 199  TRP A 203  1  O  VAL A 202   N  PHE A 102           
SHEET    6   A 6 LYS A 226  LYS A 229  1  O  LYS A 226   N  TYR A 201           
SHEET    1   B 3 THR A 132  LYS A 138  0                                        
SHEET    2   B 3 LYS A 141  LYS A 147 -1  O  ILE A 143   N  TYR A 136           
SHEET    3   B 3 GLY A 176  SER A 177 -1  O  GLY A 176   N  LEU A 146           
LINK         SG BCYS A  94                 S2 BBME A2005   1555   1555    2.11  
SITE     1 AC1  9 LYS A  23  LYS A 170  HOH A3019  HOH A3134                    
SITE     2 AC1  9 HOH A3172  HOH A3249  HOH A3444  HOH A3495                    
SITE     3 AC1  9 HOH A3530                                                     
SITE     1 AC2 11 THR A 137  LYS A 138  ASP A 139  GLY A 140                    
SITE     2 AC2 11 GLY A 232  GLY A 233  LYS A 241  HOH A3224                    
SITE     3 AC2 11 HOH A3236  HOH A3340  HOH A3380                               
SITE     1 AC3  8 LYS A 141  ASN A 181  LYS A 185  HOH A3115                    
SITE     2 AC3  8 HOH A3128  HOH A3142  HOH A3421  HOH A3488                    
SITE     1 AC4  5 THR A 110  GLY A 195  TYR A 222  HOH A3257                    
SITE     2 AC4  5 HOH A3471                                                     
SITE     1 AC5  4 CYS A  94  GLU A  95  GLU A 192  HOH A3356                    
SITE     1 AC6  8 THR A  11  ILE A  12  SER A  80  TRP A 128                    
SITE     2 AC6  8 LEU A 148  LEU A 157  HIS A 235  HOH A3050                    
SITE     1 AC7  7 GLN A  47  LYS A 147  ARG A 174  LYS A 175                    
SITE     2 AC7  7 HOH A3149  HOH A3324  HOH A3455                               
CRYST1   47.249  106.104  128.206  90.00  90.00  90.00 C 2 2 21      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.021164  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009425  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007800        0.00000                         
END                                                                             

Send your questions or comments to :
Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
For technical information about these pages see:
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