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LongText Report for: 2PM8-pdb

Name Class
2PM8-pdb
HEADER    HYDROLASE                               20-APR-07   2PM8              
TITLE     CRYSTAL STRUCTURE OF RECOMBINANT FULL LENGTH HUMAN                    
TITLE    2 BUTYRYLCHOLINESTERASE                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CHOLINESTERASE;                                            
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: ACYLCHOLINE ACYLHYDROLASE, CHOLINE ESTERASE II,             
COMPND   5 BUTYRYLCHOLINE ESTERASE, PSEUDOCHOLINESTERASE;                       
COMPND   6 EC: 3.1.1.8;                                                         
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 GENE: BCHE, CHE1;                                                    
SOURCE   5 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE   6 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER                            
KEYWDS    CHOLINESTERASE, HYDROLASE                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.N.NGAMELUE,K.HOMMA,O.LOCKRIDGE,O.A.ASOJO                            
REVDAT   1   25-SEP-07 2PM8    0                                                
JRNL        AUTH   M.N.NGAMELUE,K.HOMMA,O.LOCKRIDGE,O.A.ASOJO                   
JRNL        TITL   CRYSTALLIZATION AND X-RAY STRUCTURE OF FULL-LENGTH           
JRNL        TITL 2 RECOMBINANT HUMAN BUTYRYLCHOLINESTERASE                      
JRNL        REF    ACTA CRYSTALLOGR.,SECT.F      V.  63   723 2007              
JRNL        REFN                DK ESSN 1744-3091                               
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION. 2.80 ANGSTROMS.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 38439                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.225                           
REMARK   3   R VALUE            (WORKING SET) : 0.222                           
REMARK   3   FREE R VALUE                     : 0.292                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2027                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH           : 2.80                         
REMARK   3   BIN RESOLUTION RANGE LOW            : 2.87                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2638                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 94.08                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3020                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 145                          
REMARK   3   BIN FREE R VALUE                    : 0.3620                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   ALL ATOMS                : 8699                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 56.44                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.36000                                             
REMARK   3    B22 (A**2) : -0.36000                                             
REMARK   3    B33 (A**2) : 0.72000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.980         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.398         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.313         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 15.960        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.911                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.839                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  8843 ; 0.012 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 12003 ; 1.536 ; 1.962       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1056 ; 6.835 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   404 ;35.308 ;24.059       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1416 ;19.668 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    44 ;18.461 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1281 ; 0.100 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6714 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  4385 ; 0.233 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  5956 ; 0.319 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   348 ; 0.205 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    77 ; 0.243 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     7 ; 0.316 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  5371 ; 0.600 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  8502 ; 1.070 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3970 ; 1.230 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3500 ; 2.038 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 0                                 
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 0                                          
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2PM8 COMPLIES WITH FORMAT V. 3.1, 1-AUG-2007                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.                               
REMARK 100 THE RCSB ID CODE IS RCSB042531.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-DEC-2005                        
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 8.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR                      
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38439                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.250                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.0                               
REMARK 200  DATA REDUNDANCY                : 4.900                              
REMARK 200  R MERGE                    (I) : 0.12900                            
REMARK 200  R SYM                      (I) : 0.11600                            
REMARK 200   FOR THE DATA SET  : 11.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.95                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 82.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.54500                            
REMARK 200  R SYM FOR SHELL            (I) : 0.52900                            
REMARK 200   FOR SHELL         : 1.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 1XLW                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.28                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.10                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULPHATE, PH 8.5, VAPOR         
REMARK 280  DIFFUSION, SITTING DROP                                             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 4 21 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   1/2-Y,1/2+X,Z                                           
REMARK 290       4555   1/2+Y,1/2-X,Z                                           
REMARK 290       5555   1/2-X,1/2+Y,-Z                                          
REMARK 290       6555   1/2+X,1/2-Y,-Z                                          
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-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        0.00000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       75.40150            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       75.40150            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       75.40150            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       75.40150            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       75.40150            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       75.40150            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       75.40150            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       75.40150            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
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 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: TETRAMER                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
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  0.000000 -1.000000  0.000000      -75.40150            
REMARK 350   BIOMT2   2  1.000000  0.000000  0.000000      -75.40150            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
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     GLU A     1                                                      
REMARK 465     ASP A     2                                                      
REMARK 465     ASP A     3                                                      
REMARK 465     GLN A   455                                                      
REMARK 465     ASN A   535                                                      
REMARK 465     ILE A   536                                                      
REMARK 465     ASP A   537                                                      
REMARK 465     GLU A   538                                                      
REMARK 465     ALA A   539                                                      
REMARK 465     GLU A   540                                                      
REMARK 465     TRP A   541                                                      
REMARK 465     GLU A   542                                                      
REMARK 465     TRP A   543                                                      
REMARK 465     LYS A   544                                                      
REMARK 465     ALA A   545                                                      
REMARK 465     GLY A   546                                                      
REMARK 465     PHE A   547                                                      
REMARK 465     HIS A   548                                                      
REMARK 465     ARG A   549                                                      
REMARK 465     TRP A   550                                                      
REMARK 465     ASN A   551                                                      
REMARK 465     ASN A   552                                                      
REMARK 465     TYR A   553                                                      
REMARK 465     MET A   554                                                      
REMARK 465     MET A   555                                                      
REMARK 465     ASP A   556                                                      
REMARK 465     TRP A   557                                                      
REMARK 465     LYS A   558                                                      
REMARK 465     ASN A   559                                                      
REMARK 465     GLN A   560                                                      
REMARK 465     PHE A   561                                                      
REMARK 465     ASN A   562                                                      
REMARK 465     ASP A   563                                                      
REMARK 465     TYR A   564                                                      
REMARK 465     THR A   565                                                      
REMARK 465     SER A   566                                                      
REMARK 465     LYS A   567                                                      
REMARK 465     LYS A   568                                                      
REMARK 465     GLU A   569                                                      
REMARK 465     SER A   570                                                      
REMARK 465     CYS A   571                                                      
REMARK 465     VAL A   572                                                      
REMARK 465     GLY A   573                                                      
REMARK 465     LEU A   574                                                      
REMARK 465     GLU B     1                                                      
REMARK 465     ASP B     2                                                      
REMARK 465     ASP B     3                                                      
REMARK 465     GLN B   455                                                      
REMARK 465     ASN B   535                                                      
REMARK 465     ILE B   536                                                      
REMARK 465     ASP B   537                                                      
REMARK 465     GLU B   538                                                      
REMARK 465     ALA B   539                                                      
REMARK 465     GLU B   540                                                      
REMARK 465     TRP B   541                                                      
REMARK 465     GLU B   542                                                      
REMARK 465     TRP B   543                                                      
REMARK 465     LYS B   544                                                      
REMARK 465     ALA B   545                                                      
REMARK 465     GLY B   546                                                      
REMARK 465     PHE B   547                                                      
REMARK 465     HIS B   548                                                      
REMARK 465     ARG B   549                                                      
REMARK 465     TRP B   550                                                      
REMARK 465     ASN B   551                                                      
REMARK 465     ASN B   552                                                      
REMARK 465     TYR B   553                                                      
REMARK 465     MET B   554                                                      
REMARK 465     MET B   555                                                      
REMARK 465     ASP B   556                                                      
REMARK 465     TRP B   557                                                      
REMARK 465     LYS B   558                                                      
REMARK 465     ASN B   559                                                      
REMARK 465     GLN B   560                                                      
REMARK 465     PHE B   561                                                      
REMARK 465     ASN B   562                                                      
REMARK 465     ASP B   563                                                      
REMARK 465     TYR B   564                                                      
REMARK 465     THR B   565                                                      
REMARK 465     SER B   566                                                      
REMARK 465     LYS B   567                                                      
REMARK 465     LYS B   568                                                      
REMARK 465     GLU B   569                                                      
REMARK 465     SER B   570                                                      
REMARK 465     CYS B   571                                                      
REMARK 465     VAL B   572                                                      
REMARK 465     GLY B   573                                                      
REMARK 465     LEU B   574                                                      
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 B   820     O    HOH B   828              1.29            
REMARK 500   OD1  ASN A   485     C1   NDG A   678              1.39            
REMARK 500   CG   ASN A   485     C1   NDG A   678              1.53            
REMARK 500   NZ   LYS B   103     O    HOH B   827              1.70            
REMARK 500   NH2  ARG A   509     O    HOH A  1038              2.09            
REMARK 500   OE1  GLU B   443     O    HOH B   822              2.16            
REMARK 500   O    PHE B    21     NH1  ARG B   135              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   NZ   LYS B   528     O2   SO4 A   603     4545     2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3)                  
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    ASP A 304   CB    ASP A 304   CG      0.162                       
REMARK 500    GLU A 352   CG    GLU A 352   CD      0.093                       
REMARK 500    GLU A 352   CD    GLU A 352   OE2     0.081                       
REMARK 500    GLU B 352   CD    GLU B 352   OE2     0.082                       
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    LEU B  49   CA  -  CB  -  CG  ANGL. DEV. =  14.6 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    LYS A   9      -11.14    -47.96                                   
REMARK 500    ARG A  42      128.06    -39.51                                   
REMARK 500    PHE A  43      -26.85     84.91                                   
REMARK 500    ASP A  54     -142.12    -78.71                                   
REMARK 500    ASP A  87      122.91    -33.85                                   
REMARK 500    LEU A  93       82.88    -67.89                                   
REMARK 500    LYS A 103      114.16    -38.13                                   
REMARK 500    LYS A 105     -116.46    118.40                                   
REMARK 500    ASN A 106       60.97   -152.38                                   
REMARK 500    PHE A 118        2.52     58.50                                   
REMARK 500    PHE A 153       24.63   -140.47                                   
REMARK 500    ALA A 162       65.53   -155.13                                   
REMARK 500    SER A 198     -111.98     61.28                                   
REMARK 500    GLU A 255      -59.91   -128.29                                   
REMARK 500    ASN A 256       99.00    -51.31                                   
REMARK 500    VAL A 294       99.75    -64.85                                   
REMARK 500    ASP A 297      -65.47    -99.82                                   
REMARK 500    PHE A 298      -81.19    -66.41                                   
REMARK 500    ASN A 342       12.26    -64.27                                   
REMARK 500    SER A 343       25.71     44.27                                   
REMARK 500    ASP A 379       52.15    -56.57                                   
REMARK 500    GLN A 380      -73.29   -103.78                                   
REMARK 500    ARG A 381      112.02    -32.74                                   
REMARK 500    ASN A 384      -66.75    -29.31                                   
REMARK 500    PHE A 398      -51.43   -131.37                                   
REMARK 500    TRP A 412       31.06    -95.64                                   
REMARK 500    GLU A 422       17.45   -147.06                                   
REMARK 500    PRO A 449        0.34    -63.89                                   
REMARK 500    GLU A 451       90.20    -62.46                                   
REMARK 500    PRO A 480       47.84    -82.79                                   
REMARK 500    GLN A 484      -88.77    -81.32                                   
REMARK 500    ASN A 485       97.60    -43.79                                   
REMARK 500    GLN A 486       99.36    -30.29                                   
REMARK 500    SER A 487     -169.98   -100.05                                   
REMARK 500    THR A 496      -72.54    -73.68                                   
REMARK 500    GLN A 498       62.74     65.57                                   
REMARK 500    GLU A 506       13.03   -144.08                                   
REMARK 500    SER A 507      100.97    172.91                                   
REMARK 500    SER A 524      -62.33   -136.61                                   
REMARK 500    PHE B  21       70.52     33.92                                   
REMARK 500    PHE B  43      -20.52     65.12                                   
REMARK 500    ALA B  58       61.23   -109.52                                   
REMARK 500    ALA B  62     -167.18   -102.67                                   
REMARK 500    MET B  81      -15.48    -48.87                                   
REMARK 500    SER B  89      148.98    168.26                                   
REMARK 500    LEU B  93       76.93    -61.95                                   
REMARK 500    LYS B 105      -69.18    109.53                                   
REMARK 500    ASN B 106       49.80    142.63                                   
REMARK 500    PHE B 118       16.31     57.07                                   
REMARK 500    ALA B 150      -36.52    -36.35                                   
REMARK 500    ASN B 159      108.40    -56.45                                   
REMARK 500    ASN B 181      -50.36   -129.47                                   
REMARK 500    SER B 198     -107.09     24.67                                   
REMARK 500    SER B 215       74.46   -118.62                                   
REMARK 500    LEU B 216       -2.50   -146.74                                   
REMARK 500    CYS B 252       -2.63    -36.67                                   
REMARK 500    ARG B 254     -165.94   -121.80                                   
REMARK 500    GLU B 255      -68.04   -104.92                                   
REMARK 500    ASP B 268      135.68    -36.09                                   
REMARK 500    TYR B 282      -99.39   -118.77                                   
REMARK 500    ILE B 344       92.22    -68.68                                   
REMARK 500    ARG B 347      -47.41    -27.00                                   
REMARK 500    SER B 362      152.06    -46.20                                   
REMARK 500    ASP B 379       32.95    -81.24                                   
REMARK 500    GLN B 380      -83.98    -81.51                                   
REMARK 500    ARG B 381      118.15    -26.45                                   
REMARK 500    ASN B 384      -74.41    -46.55                                   
REMARK 500    PHE B 398      -61.02   -127.31                                   
REMARK 500    LEU B 428      116.90    -39.47                                   
REMARK 500    GLU B 451      102.51    -53.76                                   
REMARK 500    ARG B 452        1.43    -62.43                                   
REMARK 500    PRO B 480       58.61    -93.73                                   
REMARK 500    GLN B 484      -93.09    -93.78                                   
REMARK 500    ASN B 485       94.66    -35.82                                   
REMARK 500    GLN B 486       83.58    -38.96                                   
REMARK 500    THR B 496      -81.78    -74.29                                   
REMARK 500    GLU B 506     -113.91   -124.07                                   
REMARK 500    SER B 507       90.89    -63.11                                   
REMARK 500    THR B 533      -63.57    -17.78                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1XLW   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1VZJ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1XLU   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1P01   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1XLV   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2CEK   RELATED DB: PDB                                   
DBREF  2PM8 A    1   574  UNP    P06276   CHLE_HUMAN      29    602             
DBREF  2PM8 B    1   574  UNP    P06276   CHLE_HUMAN      29    602             
SEQADV 2PM8 GLN A   17  UNP  P06276    ASN    45 CONFLICT                       
SEQADV 2PM8 GLN A  455  UNP  P06276    ASN   483 CONFLICT                       
SEQADV 2PM8 GLN A  481  UNP  P06276    ASN   509 CONFLICT                       
SEQADV 2PM8 GLN A  486  UNP  P06276    ASN   514 CONFLICT                       
SEQADV 2PM8 GLN B   17  UNP  P06276    ASN    45 CONFLICT                       
SEQADV 2PM8 GLN B  455  UNP  P06276    ASN   483 CONFLICT                       
SEQADV 2PM8 GLN B  481  UNP  P06276    ASN   509 CONFLICT                       
SEQADV 2PM8 GLN B  486  UNP  P06276    ASN   514 CONFLICT                       
SEQRES   1 A  574  GLU ASP ASP ILE ILE ILE ALA THR LYS ASN GLY LYS VAL          
SEQRES   2 A  574  ARG GLY MET GLN LEU THR VAL PHE GLY GLY THR VAL THR          
SEQRES   3 A  574  ALA PHE LEU GLY ILE PRO TYR ALA GLN PRO PRO LEU GLY          
SEQRES   4 A  574  ARG LEU ARG PHE LYS LYS PRO GLN SER LEU THR LYS TRP          
SEQRES   5 A  574  SER ASP ILE TRP ASN ALA THR LYS TYR ALA ASN SER CYS          
SEQRES   6 A  574  CYS GLN ASN ILE ASP GLN SER PHE PRO GLY PHE HIS GLY          
SEQRES   7 A  574  SER GLU MET TRP ASN PRO ASN THR ASP LEU SER GLU ASP          
SEQRES   8 A  574  CYS LEU TYR LEU ASN VAL TRP ILE PRO ALA PRO LYS PRO          
SEQRES   9 A  574  LYS ASN ALA THR VAL LEU ILE TRP ILE TYR GLY GLY GLY          
SEQRES  10 A  574  PHE GLN THR GLY THR SER SER LEU HIS VAL TYR ASP GLY          
SEQRES  11 A  574  LYS PHE LEU ALA ARG VAL GLU ARG VAL ILE VAL VAL SER          
SEQRES  12 A  574  MET ASN TYR ARG VAL GLY ALA LEU GLY PHE LEU ALA LEU          
SEQRES  13 A  574  PRO GLY ASN PRO GLU ALA PRO GLY ASN MET GLY LEU PHE          
SEQRES  14 A  574  ASP GLN GLN LEU ALA LEU GLN TRP VAL GLN LYS ASN ILE          
SEQRES  15 A  574  ALA ALA PHE GLY GLY ASN PRO LYS SER VAL THR LEU PHE          
SEQRES  16 A  574  GLY GLU SER ALA GLY ALA ALA SER VAL SER LEU HIS LEU          
SEQRES  17 A  574  LEU SER PRO GLY SER HIS SER LEU PHE THR ARG ALA ILE          
SEQRES  18 A  574  LEU GLN SER GLY SER PHE ASN ALA PRO TRP ALA VAL THR          
SEQRES  19 A  574  SER LEU TYR GLU ALA ARG ASN ARG THR LEU ASN LEU ALA          
SEQRES  20 A  574  LYS LEU THR GLY CYS SER ARG GLU ASN GLU THR GLU ILE          
SEQRES  21 A  574  ILE LYS CYS LEU ARG ASN LYS ASP PRO GLN GLU ILE LEU          
SEQRES  22 A  574  LEU ASN GLU ALA PHE VAL VAL PRO TYR GLY THR PRO LEU          
SEQRES  23 A  574  SER VAL ASN PHE GLY PRO THR VAL ASP GLY ASP PHE LEU          
SEQRES  24 A  574  THR ASP MET PRO ASP ILE LEU LEU GLU LEU GLY GLN PHE          
SEQRES  25 A  574  LYS LYS THR GLN ILE LEU VAL GLY VAL ASN LYS ASP GLU          
SEQRES  26 A  574  GLY THR ALA PHE LEU VAL TYR GLY ALA PRO GLY PHE SER          
SEQRES  27 A  574  LYS ASP ASN ASN SER ILE ILE THR ARG LYS GLU PHE GLN          
SEQRES  28 A  574  GLU GLY LEU LYS ILE PHE PHE PRO GLY VAL SER GLU PHE          
SEQRES  29 A  574  GLY LYS GLU SER ILE LEU PHE HIS TYR THR ASP TRP VAL          
SEQRES  30 A  574  ASP ASP GLN ARG PRO GLU ASN TYR ARG GLU ALA LEU GLY          
SEQRES  31 A  574  ASP VAL VAL GLY ASP TYR ASN PHE ILE CYS PRO ALA LEU          
SEQRES  32 A  574  GLU PHE THR LYS LYS PHE SER GLU TRP GLY ASN ASN ALA          
SEQRES  33 A  574  PHE PHE TYR TYR PHE GLU HIS ARG SER SER LYS LEU PRO          
SEQRES  34 A  574  TRP PRO GLU TRP MET GLY VAL MET HIS GLY TYR GLU ILE          
SEQRES  35 A  574  GLU PHE VAL PHE GLY LEU PRO LEU GLU ARG ARG ASP GLN          
SEQRES  36 A  574  TYR THR LYS ALA GLU GLU ILE LEU SER ARG SER ILE VAL          
SEQRES  37 A  574  LYS ARG TRP ALA ASN PHE ALA LYS TYR GLY ASN PRO GLN          
SEQRES  38 A  574  GLU THR GLN ASN GLN SER THR SER TRP PRO VAL PHE LYS          
SEQRES  39 A  574  SER THR GLU GLN LYS TYR LEU THR LEU ASN THR GLU SER          
SEQRES  40 A  574  THR ARG ILE MET THR LYS LEU ARG ALA GLN GLN CYS ARG          
SEQRES  41 A  574  PHE TRP THR SER PHE PHE PRO LYS VAL LEU GLU MET THR          
SEQRES  42 A  574  GLY ASN ILE ASP GLU ALA GLU TRP GLU TRP LYS ALA GLY          
SEQRES  43 A  574  PHE HIS ARG TRP ASN ASN TYR MET MET ASP TRP LYS ASN          
SEQRES  44 A  574  GLN PHE ASN ASP TYR THR SER LYS LYS GLU SER CYS VAL          
SEQRES  45 A  574  GLY LEU                                                      
SEQRES   1 B  574  GLU ASP ASP ILE ILE ILE ALA THR LYS ASN GLY LYS VAL          
SEQRES   2 B  574  ARG GLY MET GLN LEU THR VAL PHE GLY GLY THR VAL THR          
SEQRES   3 B  574  ALA PHE LEU GLY ILE PRO TYR ALA GLN PRO PRO LEU GLY          
SEQRES   4 B  574  ARG LEU ARG PHE LYS LYS PRO GLN SER LEU THR LYS TRP          
SEQRES   5 B  574  SER ASP ILE TRP ASN ALA THR LYS TYR ALA ASN SER CYS          
SEQRES   6 B  574  CYS GLN ASN ILE ASP GLN SER PHE PRO GLY PHE HIS GLY          
SEQRES   7 B  574  SER GLU MET TRP ASN PRO ASN THR ASP LEU SER GLU ASP          
SEQRES   8 B  574  CYS LEU TYR LEU ASN VAL TRP ILE PRO ALA PRO LYS PRO          
SEQRES   9 B  574  LYS ASN ALA THR VAL LEU ILE TRP ILE TYR GLY GLY GLY          
SEQRES  10 B  574  PHE GLN THR GLY THR SER SER LEU HIS VAL TYR ASP GLY          
SEQRES  11 B  574  LYS PHE LEU ALA ARG VAL GLU ARG VAL ILE VAL VAL SER          
SEQRES  12 B  574  MET ASN TYR ARG VAL GLY ALA LEU GLY PHE LEU ALA LEU          
SEQRES  13 B  574  PRO GLY ASN PRO GLU ALA PRO GLY ASN MET GLY LEU PHE          
SEQRES  14 B  574  ASP GLN GLN LEU ALA LEU GLN TRP VAL GLN LYS ASN ILE          
SEQRES  15 B  574  ALA ALA PHE GLY GLY ASN PRO LYS SER VAL THR LEU PHE          
SEQRES  16 B  574  GLY GLU SER ALA GLY ALA ALA SER VAL SER LEU HIS LEU          
SEQRES  17 B  574  LEU SER PRO GLY SER HIS SER LEU PHE THR ARG ALA ILE          
SEQRES  18 B  574  LEU GLN SER GLY SER PHE ASN ALA PRO TRP ALA VAL THR          
SEQRES  19 B  574  SER LEU TYR GLU ALA ARG ASN ARG THR LEU ASN LEU ALA          
SEQRES  20 B  574  LYS LEU THR GLY CYS SER ARG GLU ASN GLU THR GLU ILE          
SEQRES  21 B  574  ILE LYS CYS LEU ARG ASN LYS ASP PRO GLN GLU ILE LEU          
SEQRES  22 B  574  LEU ASN GLU ALA PHE VAL VAL PRO TYR GLY THR PRO LEU          
SEQRES  23 B  574  SER VAL ASN PHE GLY PRO THR VAL ASP GLY ASP PHE LEU          
SEQRES  24 B  574  THR ASP MET PRO ASP ILE LEU LEU GLU LEU GLY GLN PHE          
SEQRES  25 B  574  LYS LYS THR GLN ILE LEU VAL GLY VAL ASN LYS ASP GLU          
SEQRES  26 B  574  GLY THR ALA PHE LEU VAL TYR GLY ALA PRO GLY PHE SER          
SEQRES  27 B  574  LYS ASP ASN ASN SER ILE ILE THR ARG LYS GLU PHE GLN          
SEQRES  28 B  574  GLU GLY LEU LYS ILE PHE PHE PRO GLY VAL SER GLU PHE          
SEQRES  29 B  574  GLY LYS GLU SER ILE LEU PHE HIS TYR THR ASP TRP VAL          
SEQRES  30 B  574  ASP ASP GLN ARG PRO GLU ASN TYR ARG GLU ALA LEU GLY          
SEQRES  31 B  574  ASP VAL VAL GLY ASP TYR ASN PHE ILE CYS PRO ALA LEU          
SEQRES  32 B  574  GLU PHE THR LYS LYS PHE SER GLU TRP GLY ASN ASN ALA          
SEQRES  33 B  574  PHE PHE TYR TYR PHE GLU HIS ARG SER SER LYS LEU PRO          
SEQRES  34 B  574  TRP PRO GLU TRP MET GLY VAL MET HIS GLY TYR GLU ILE          
SEQRES  35 B  574  GLU PHE VAL PHE GLY LEU PRO LEU GLU ARG ARG ASP GLN          
SEQRES  36 B  574  TYR THR LYS ALA GLU GLU ILE LEU SER ARG SER ILE VAL          
SEQRES  37 B  574  LYS ARG TRP ALA ASN PHE ALA LYS TYR GLY ASN PRO GLN          
SEQRES  38 B  574  GLU THR GLN ASN GLN SER THR SER TRP PRO VAL PHE LYS          
SEQRES  39 B  574  SER THR GLU GLN LYS TYR LEU THR LEU ASN THR GLU SER          
SEQRES  40 B  574  THR ARG ILE MET THR LYS LEU ARG ALA GLN GLN CYS ARG          
SEQRES  41 B  574  PHE TRP THR SER PHE PHE PRO LYS VAL LEU GLU MET THR          
SEQRES  42 B  574  GLY ASN ILE ASP GLU ALA GLU TRP GLU TRP LYS ALA GLY          
SEQRES  43 B  574  PHE HIS ARG TRP ASN ASN TYR MET MET ASP TRP LYS ASN          
SEQRES  44 B  574  GLN PHE ASN ASP TYR THR SER LYS LYS GLU SER CYS VAL          
SEQRES  45 B  574  GLY LEU                                                      
MODRES 2PM8 ASN A   57  ASN  GLYCOSYLATION SITE                                 
MODRES 2PM8 ASN A  106  ASN  GLYCOSYLATION SITE                                 
MODRES 2PM8 ASN A  341  ASN  GLYCOSYLATION SITE                                 
MODRES 2PM8 ASN B  106  ASN  GLYCOSYLATION SITE                                 
MODRES 2PM8 ASN A  485  ASN  GLYCOSYLATION SITE                                 
HET    NAG  C 781      14                                                       
HET    NAG  C 782      14                                                       
HET    NAG  A 791      14                                                       
HET    NDG  A 678      14                                                       
HET    NAG  A 798      14                                                       
HET    NAG  B 781      14                                                       
HET    NAG  B 791      14                                                       
HET    SO4  A 601       5                                                       
HET    SO4  A 602       5                                                       
HET    SO4  A 603       5                                                       
HET    SO4  A 604       5                                                       
HET    SO4  A 606       5                                                       
HET    SO4  B 601       5                                                       
HET    SO4  B 602       5                                                       
HET    GOL  A 999       6                                                       
HET    GOL  A 774       6                                                       
HET    GOL  A 777       6                                                       
HET    GOL  B 774       6                                                       
HET    GOL  B 777       6                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     NDG 2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE                        
HETNAM     SO4 SULFATE ION                                                      
HETNAM     GOL GLYCEROL                                                         
HETSYN     NAG NAG                                                              
FORMUL   3  NAG    6(C8 H15 N O6)                                               
FORMUL   5  NDG    C8 H15 N O6                                                  
FORMUL   9  SO4    7(O4 S 2-)                                                   
FORMUL  16  GOL    5(C3 H8 O3)                                                  
FORMUL  21  HOH   *94(H2 O)                                                     
HELIX    1   1 PHE A   76  MET A   81  1                                   6    
HELIX    2   2 LEU A  125  ASP A  129  5                                   5    
HELIX    3   3 GLY A  130  ARG A  138  1                                   9    
HELIX    4   4 GLY A  149  LEU A  154  1                                   6    
HELIX    5   5 ASN A  165  ILE A  182  1                                  18    
HELIX    6   6 ALA A  183  PHE A  185  5                                   3    
HELIX    7   7 SER A  198  LEU A  208  1                                  11    
HELIX    8   8 SER A  235  THR A  250  1                                  16    
HELIX    9   9 ASN A  256  ASN A  266  1                                  11    
HELIX   10  10 ASP A  268  ALA A  277  1                                  10    
HELIX   11  11 MET A  302  LEU A  309  1                                   8    
HELIX   12  12 GLY A  326  GLY A  333  5                                   8    
HELIX   13  13 THR A  346  PHE A  358  1                                  13    
HELIX   14  14 SER A  362  THR A  374  1                                  13    
HELIX   15  15 GLU A  383  PHE A  398  1                                  16    
HELIX   16  16 PHE A  398  GLU A  411  1                                  14    
HELIX   17  17 PRO A  431  GLY A  435  5                                   5    
HELIX   18  18 GLU A  441  PHE A  446  1                                   6    
HELIX   19  19 GLY A  447  GLU A  451  5                                   5    
HELIX   20  20 THR A  457  GLY A  478  1                                  22    
HELIX   21  21 ARG A  515  SER A  524  1                                  10    
HELIX   22  22 SER A  524  MET A  532  1                                   9    
HELIX   23  23 LEU B   38  ARG B   42  5                                   5    
HELIX   24  24 PHE B   76  MET B   81  1                                   6    
HELIX   25  25 LEU B  125  ASP B  129  5                                   5    
HELIX   26  26 GLY B  130  ARG B  138  1                                   9    
HELIX   27  27 GLY B  149  LEU B  154  1                                   6    
HELIX   28  28 ASN B  165  ILE B  182  1                                  18    
HELIX   29  29 ALA B  183  PHE B  185  5                                   3    
HELIX   30  30 GLU B  197  LEU B  208  1                                  12    
HELIX   31  31 SER B  210  HIS B  214  5                                   5    
HELIX   32  32 SER B  235  THR B  250  1                                  16    
HELIX   33  33 GLU B  257  ARG B  265  1                                   9    
HELIX   34  34 ASP B  268  ALA B  277  1                                  10    
HELIX   35  35 MET B  302  LEU B  309  1                                   8    
HELIX   36  36 ASP B  324  GLY B  333  5                                  10    
HELIX   37  37 THR B  346  PHE B  358  1                                  13    
HELIX   38  38 SER B  362  THR B  374  1                                  13    
HELIX   39  39 GLU B  383  PHE B  398  1                                  16    
HELIX   40  40 PHE B  398  GLU B  411  1                                  14    
HELIX   41  41 PRO B  431  GLY B  435  5                                   5    
HELIX   42  42 GLU B  441  PHE B  446  1                                   6    
HELIX   43  43 GLY B  447  GLU B  451  5                                   5    
HELIX   44  44 THR B  457  GLY B  478  1                                  22    
HELIX   45  45 ARG B  515  SER B  524  1                                  10    
HELIX   46  46 PHE B  526  GLY B  534  1                                   9    
SHEET    1   A 3 ILE A   5  THR A   8  0                                        
SHEET    2   A 3 GLY A  11  ARG A  14 -1  O  VAL A  13   N  ILE A   6           
SHEET    3   A 3 ILE A  55  ASN A  57  1  O  TRP A  56   N  ARG A  14           
SHEET    1   B11 MET A  16  VAL A  20  0                                        
SHEET    2   B11 GLY A  23  PRO A  32 -1  O  GLY A  23   N  VAL A  20           
SHEET    3   B11 TYR A  94  PRO A 100 -1  O  LEU A  95   N  ILE A  31           
SHEET    4   B11 ILE A 140  MET A 144 -1  O  SER A 143   N  ASN A  96           
SHEET    5   B11 ALA A 107  ILE A 113  1  N  TRP A 112   O  VAL A 142           
SHEET    6   B11 GLY A 187  GLU A 197  1  O  PHE A 195   N  ILE A 111           
SHEET    7   B11 ARG A 219  GLN A 223  1  O  ILE A 221   N  LEU A 194           
SHEET    8   B11 ILE A 317  ASN A 322  1  O  LEU A 318   N  LEU A 222           
SHEET    9   B11 ALA A 416  PHE A 421  1  O  PHE A 417   N  ILE A 317           
SHEET   10   B11 LYS A 499  LEU A 503  1  O  LEU A 503   N  TYR A 420           
SHEET   11   B11 ILE A 510  THR A 512 -1  O  MET A 511   N  TYR A 500           
SHEET    1   C 3 ILE B   5  THR B   8  0                                        
SHEET    2   C 3 GLY B  11  ARG B  14 -1  O  VAL B  13   N  ILE B   6           
SHEET    3   C 3 ILE B  55  ASN B  57  1  O  TRP B  56   N  ARG B  14           
SHEET    1   D11 MET B  16  VAL B  20  0                                        
SHEET    2   D11 GLY B  23  PRO B  32 -1  O  VAL B  25   N  LEU B  18           
SHEET    3   D11 TYR B  94  PRO B 100 -1  O  ILE B  99   N  THR B  26           
SHEET    4   D11 ILE B 140  MET B 144 -1  O  SER B 143   N  ASN B  96           
SHEET    5   D11 ALA B 107  ILE B 113  1  N  TRP B 112   O  VAL B 142           
SHEET    6   D11 GLY B 187  GLY B 196  1  O  THR B 193   N  ILE B 111           
SHEET    7   D11 ARG B 219  GLN B 223  1  O  ILE B 221   N  LEU B 194           
SHEET    8   D11 ILE B 317  ASN B 322  1  O  LEU B 318   N  LEU B 222           
SHEET    9   D11 ALA B 416  PHE B 421  1  O  PHE B 417   N  VAL B 319           
SHEET   10   D11 LYS B 499  LEU B 503  1  O  LEU B 503   N  TYR B 420           
SHEET   11   D11 ILE B 510  THR B 512 -1  O  MET B 511   N  TYR B 500           
SSBOND   1 CYS A   65    CYS A   92                        1555   1555    2.04  
SSBOND   2 CYS A  252    CYS A  263                        1555   1555    2.04  
SSBOND   3 CYS A  400    CYS A  519                        1555   1555    2.09  
SSBOND   4 CYS B   65    CYS B   92                        1555   1555    2.04  
SSBOND   5 CYS B  252    CYS B  263                        1555   1555    2.05  
SSBOND   6 CYS B  400    CYS B  519                        1555   1555    2.08  
LINK         ND2 ASN A  57                 C1  NAG A 798   1555   1555    1.45  
LINK         ND2 ASN A 106                 C1  NAG A 791   1555   1555    1.45  
LINK         ND2 ASN A 341                 C1  NAG C 781   1555   1555    1.44  
LINK         ND2 ASN B 106                 C1  NAG B 791   1555   1555    1.46  
LINK         O4  NAG C 781                 C1  NAG C 782   1555   1555    1.45  
LINK         ND2 ASN A 485                 C1  NDG A 678   1555   1555    1.43  
CISPEP   1 ALA A  101    PRO A  102          0         4.11                     
CISPEP   2 PRO A  104    LYS A  105          0        14.70                     
CISPEP   3 ALA B  101    PRO B  102          0         5.90                     
CISPEP   4 PRO B  104    LYS B  105          0        27.05                     
CRYST1  150.803  150.803  142.120  90.00  90.00  90.00 P 4 21 2     16          
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      0.006631  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006631  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007036        0.00000                         
TER    4222      GLY A 534                                                      
TER    8444      GLY B 534                                                      
MASTER      519    0   19   46   28    0    0    6 8699    2  180   90          
END                                                                             

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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.
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