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Database: PDB
Entry: 3RIK
LinkDB: 3RIK
Original site: 3RIK 
HEADER    HYDROLASE/HYDROLASE INHIBITOR           13-APR-11   3RIK              
TITLE     THE ACID BETA-GLUCOSIDASE ACTIVE SITE EXHIBITS PLASTICITY IN BINDING  
TITLE    2 3,4,5,6-TETRAHYDROXYAZEPANE-BASED INHIBITORS: IMPLICATIONS FOR       
TITLE    3 PHARMACOLOGICAL CHAPERONE DESIGN FOR GAUCHER DISEASE                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUCOSYLCERAMIDASE;                                        
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: RESIDUES 40-536;                                           
COMPND   5 SYNONYM: ACID BETA-GLUCOSIDASE, ALGLUCERASE, BETA-GLUCOCEREBROSIDASE,
COMPND   6 D-GLUCOSYL-N-ACYLSPHINGOSINE GLUCOHYDROLASE, IMIGLUCERASE;           
COMPND   7 EC: 3.2.1.45;                                                        
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: GBA, GC, GLUC;                                                 
SOURCE   6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE   7 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 10029                                       
KEYWDS    TIM-BARREL, LYSOSOMAL HYDROLASE, HYDROLASE, GLYCOSYLATION, LYSOSOME,  
KEYWDS   2 HYDROLASE-HYDROLASE INHIBITOR COMPLEX                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.D.ORWIG,R.L.LIEBERMAN                                               
REVDAT   2   05-DEC-12 3RIK    1       LINK   REMARK                            
REVDAT   1   14-MAR-12 3RIK    0                                                
JRNL        AUTH   S.D.ORWIG,Y.L.TAN,N.P.GRIMSTER,Z.YU,E.T.POWERS,J.W.KELLY,    
JRNL        AUTH 2 R.L.LIEBERMAN                                                
JRNL        TITL   BINDING OF 3,4,5,6-TETRAHYDROXYAZEPANES TO THE               
JRNL        TITL 2 ACID-BETA-GLUCOSIDASE ACTIVE SITE: IMPLICATIONS FOR          
JRNL        TITL 3 PHARMACOLOGICAL CHAPERONE DESIGN FOR GAUCHER DISEASE         
JRNL        REF    BIOCHEMISTRY                  V.  50 10647 2011              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   22047104                                                     
JRNL        DOI    10.1021/BI201619Z                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.48 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
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) : 2.48                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.50                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 88126                          
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) : 0.165                           
REMARK   3   R VALUE            (WORKING SET) : 0.162                           
REMARK   3   FREE R VALUE                     : 0.225                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4628                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.48                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.55                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4899                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 71.99                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2330                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 267                          
REMARK   3   BIN FREE R VALUE                    : 0.3430                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 15716                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 254                                     
REMARK   3   SOLVENT ATOMS            : 908                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 27.99                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : -0.01000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.01000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.377         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.254         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.168         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.662         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.955                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.915                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 16428 ; 0.016 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 22426 ; 1.794 ; 1.959       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1984 ; 7.022 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   720 ;38.045 ;23.444       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2516 ;16.292 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    84 ;20.744 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2456 ; 0.113 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 12520 ; 0.009 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
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):  9936 ; 0.220 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 16064 ; 0.411 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  6492 ; 0.397 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  6362 ; 0.707 ; 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 : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
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: HYDROGENS HAVE BEEN USED IF PRESENT IN    
REMARK   3  THE INPUT                                                           
REMARK   4                                                                      
REMARK   4 3RIK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-APR-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB064974.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NOV-07                             
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : 4.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-BM                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 88126                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.480                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.500                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : 2.900                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.12200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: RIGID BODY REFINEMENT        
REMARK 200 SOFTWARE USED: REFMAC                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.10                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.16                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 11-12% PEG 3350, 0.18-0.205 M AMMONIUM   
REMARK 280  SULFATE, AND 0.1 M ACETATE BUFFER, PH 4.6, VAPOR DIFFUSION,         
REMARK 280  HANGING DROP, TEMPERATURE 298.0K                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
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                                                                      
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       45.77650            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5                                           
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: MONOMERIC                         
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                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
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                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
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                                                                      
REMARK 350 BIOMOLECULE: 5                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 13380 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 68820 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -427.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
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 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           DISTANCE          
REMARK 500   O    HOH C   805     O    HOH C   813              1.92            
REMARK 500   O    HOH C   601     O    HOH C   685              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),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    TRP A 184   CE2   TRP A 184   CD2     0.080                       
REMARK 500    HIS A 255   CG    HIS A 255   CD2     0.054                       
REMARK 500    HIS A 290   CG    HIS A 290   CD2     0.055                       
REMARK 500    TRP A 291   CE2   TRP A 291   CD2     0.082                       
REMARK 500    TRP A 381   CE2   TRP A 381   CD2     0.073                       
REMARK 500    HIS B 145   CG    HIS B 145   CD2     0.074                       
REMARK 500    TRP B 184   CE2   TRP B 184   CD2     0.087                       
REMARK 500    HIS B 206   CG    HIS B 206   CD2     0.064                       
REMARK 500    HIS B 273   CG    HIS B 273   CD2     0.056                       
REMARK 500    TRP B 291   CE2   TRP B 291   CD2     0.085                       
REMARK 500    HIS B 311   CG    HIS B 311   CD2     0.060                       
REMARK 500    HIS B 328   CG    HIS B 328   CD2     0.064                       
REMARK 500    TRP B 348   CE2   TRP B 348   CD2     0.077                       
REMARK 500    TRP B 378   CE2   TRP B 378   CD2     0.077                       
REMARK 500    TRP B 393   CE2   TRP B 393   CD2     0.076                       
REMARK 500    TRP C 184   CE2   TRP C 184   CD2     0.074                       
REMARK 500    TRP C 291   CE2   TRP C 291   CD2     0.079                       
REMARK 500    TRP C 348   CE2   TRP C 348   CD2     0.098                       
REMARK 500    HIS D 145   CG    HIS D 145   CD2     0.068                       
REMARK 500    TRP D 184   CE2   TRP D 184   CD2     0.078                       
REMARK 500    HIS D 273   CG    HIS D 273   CD2     0.059                       
REMARK 500    TRP D 291   CE2   TRP D 291   CD2     0.076                       
REMARK 500    HIS D 328   CG    HIS D 328   CD2     0.076                       
REMARK 500    TRP D 348   CE2   TRP D 348   CD2     0.096                       
REMARK 500    TRP D 378   CE2   TRP D 378   CD2     0.082                       
REMARK 500    TRP D 393   CE2   TRP D 393   CD2     0.090                       
REMARK 500    HIS D 419   CG    HIS D 419   CD2     0.059                       
REMARK 500    HIS D 451   CG    HIS D 451   CD2     0.056                       
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 NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU A 286   CA  -  CB  -  CG  ANGL. DEV. =  14.3 DEGREES          
REMARK 500    ARG A 433   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500    ASP A 467   CB  -  CG  -  OD2 ANGL. DEV. =  -5.6 DEGREES          
REMARK 500    ILE B   5   CG1 -  CB  -  CG2 ANGL. DEV. = -14.8 DEGREES          
REMARK 500    PRO B 319   C   -  N   -  CA  ANGL. DEV. =  19.7 DEGREES          
REMARK 500    PRO B 319   C   -  N   -  CD  ANGL. DEV. = -15.4 DEGREES          
REMARK 500    ARG C 433   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.3 DEGREES          
REMARK 500    ARG D 285   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 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    ASN A  19     -155.95   -145.57                                   
REMARK 500    ALA A  33      154.44    -41.91                                   
REMARK 500    PHE A  75     -143.93   -120.55                                   
REMARK 500    ALA A 124     -159.48     73.18                                   
REMARK 500    PHE A 128       45.61    -89.29                                   
REMARK 500    ALA A 136       66.52   -153.71                                   
REMARK 500    ASP A 141       64.32   -106.31                                   
REMARK 500    LEU A 156      -72.84   -107.34                                   
REMARK 500    ASN A 192     -159.41   -135.50                                   
REMARK 500    LYS A 224       48.81     74.53                                   
REMARK 500    GLU A 233      138.58   -175.34                                   
REMARK 500    ASP A 263      -63.83   -121.33                                   
REMARK 500    LEU A 281      -81.92     71.15                                   
REMARK 500    ALA A 318     -124.34    -47.91                                   
REMARK 500    THR A 323      -75.92   -117.49                                   
REMARK 500    VAL A 343      -75.91   -130.59                                   
REMARK 500    SER A 345       41.60    105.85                                   
REMARK 500    HIS A 374        8.91     80.56                                   
REMARK 500    TRP A 381     -138.87    -83.21                                   
REMARK 500    VAL A 394      -60.93   -105.54                                   
REMARK 500    PHE A 397      -37.55   -165.35                                   
REMARK 500    ARG B   2      103.91     53.76                                   
REMARK 500    ASN B  19     -157.79   -147.40                                   
REMARK 500    THR B  61       42.64    -93.91                                   
REMARK 500    THR B  63       35.20   -148.14                                   
REMARK 500    PHE B  75     -138.74   -117.62                                   
REMARK 500    ALA B 124     -156.41     68.62                                   
REMARK 500    CYS B 126     -158.53   -135.45                                   
REMARK 500    ALA B 136       67.58   -150.27                                   
REMARK 500    ASP B 140       19.71     57.86                                   
REMARK 500    ASN B 146       32.16    -93.57                                   
REMARK 500    LEU B 156      -72.05   -109.11                                   
REMARK 500    GLU B 233      140.14   -179.05                                   
REMARK 500    ASP B 263      -70.59   -120.68                                   
REMARK 500    LEU B 281      -78.94     71.39                                   
REMARK 500    LEU B 286        0.72    -62.88                                   
REMARK 500    ALA B 318     -161.67    -61.52                                   
REMARK 500    PRO B 319      143.32    -27.67                                   
REMARK 500    THR B 323      -78.24   -126.29                                   
REMARK 500    SER B 345       33.70     94.09                                   
REMARK 500    PHE B 347      -57.20    158.58                                   
REMARK 500    TRP B 348      -76.65     66.82                                   
REMARK 500    GLN B 350      151.96    -47.17                                   
REMARK 500    HIS B 374        5.87     80.64                                   
REMARK 500    TRP B 381     -144.20    -90.07                                   
REMARK 500    ASN B 382      124.39    -39.24                                   
REMARK 500    ASN C  19     -159.69   -152.35                                   
REMARK 500    PHE C  75     -141.55   -124.47                                   
REMARK 500    ALA C 124     -151.80     78.30                                   
REMARK 500    PHE C 128       46.94    -97.30                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      81 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 CYS A  342     VAL A  343                  -48.46                    
REMARK 500 PHE B  347     TRP B  348                   39.31                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    ARG B   2        21.1      L          L   OUTSIDE RANGE           
REMARK 500    PHE B 347        18.2      L          L   OUTSIDE RANGE           
REMARK 500    VAL C 343        22.2      L          L   OUTSIDE RANGE           
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 C 814        DISTANCE =  5.41 ANGSTROMS                       
REMARK 525    HOH C 815        DISTANCE =  6.05 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 508                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 509                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 510                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 511                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3RI B 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 508                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 509                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 510                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 508                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 509                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 510                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3RI D 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 508                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 509                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3RIL   RELATED DB: PDB                                   
DBREF  3RIK A    1   497  UNP    P04062   GLCM_HUMAN      40    536             
DBREF  3RIK B    1   497  UNP    P04062   GLCM_HUMAN      40    536             
DBREF  3RIK C    1   497  UNP    P04062   GLCM_HUMAN      40    536             
DBREF  3RIK D    1   497  UNP    P04062   GLCM_HUMAN      40    536             
SEQADV 3RIK HIS A  495  UNP  P04062    ARG   534 VARIANT                        
SEQADV 3RIK HIS B  495  UNP  P04062    ARG   534 VARIANT                        
SEQADV 3RIK HIS C  495  UNP  P04062    ARG   534 VARIANT                        
SEQADV 3RIK HIS D  495  UNP  P04062    ARG   534 VARIANT                        
SEQRES   1 A  497  ALA ARG PRO CYS ILE PRO LYS SER PHE GLY TYR SER SER          
SEQRES   2 A  497  VAL VAL CYS VAL CYS ASN ALA THR TYR CYS ASP SER PHE          
SEQRES   3 A  497  ASP PRO PRO THR PHE PRO ALA LEU GLY THR PHE SER ARG          
SEQRES   4 A  497  TYR GLU SER THR ARG SER GLY ARG ARG MET GLU LEU SER          
SEQRES   5 A  497  MET GLY PRO ILE GLN ALA ASN HIS THR GLY THR GLY LEU          
SEQRES   6 A  497  LEU LEU THR LEU GLN PRO GLU GLN LYS PHE GLN LYS VAL          
SEQRES   7 A  497  LYS GLY PHE GLY GLY ALA MET THR ASP ALA ALA ALA LEU          
SEQRES   8 A  497  ASN ILE LEU ALA LEU SER PRO PRO ALA GLN ASN LEU LEU          
SEQRES   9 A  497  LEU LYS SER TYR PHE SER GLU GLU GLY ILE GLY TYR ASN          
SEQRES  10 A  497  ILE ILE ARG VAL PRO MET ALA SER CYS ASP PHE SER ILE          
SEQRES  11 A  497  ARG THR TYR THR TYR ALA ASP THR PRO ASP ASP PHE GLN          
SEQRES  12 A  497  LEU HIS ASN PHE SER LEU PRO GLU GLU ASP THR LYS LEU          
SEQRES  13 A  497  LYS ILE PRO LEU ILE HIS ARG ALA LEU GLN LEU ALA GLN          
SEQRES  14 A  497  ARG PRO VAL SER LEU LEU ALA SER PRO TRP THR SER PRO          
SEQRES  15 A  497  THR TRP LEU LYS THR ASN GLY ALA VAL ASN GLY LYS GLY          
SEQRES  16 A  497  SER LEU LYS GLY GLN PRO GLY ASP ILE TYR HIS GLN THR          
SEQRES  17 A  497  TRP ALA ARG TYR PHE VAL LYS PHE LEU ASP ALA TYR ALA          
SEQRES  18 A  497  GLU HIS LYS LEU GLN PHE TRP ALA VAL THR ALA GLU ASN          
SEQRES  19 A  497  GLU PRO SER ALA GLY LEU LEU SER GLY TYR PRO PHE GLN          
SEQRES  20 A  497  CYS LEU GLY PHE THR PRO GLU HIS GLN ARG ASP PHE ILE          
SEQRES  21 A  497  ALA ARG ASP LEU GLY PRO THR LEU ALA ASN SER THR HIS          
SEQRES  22 A  497  HIS ASN VAL ARG LEU LEU MET LEU ASP ASP GLN ARG LEU          
SEQRES  23 A  497  LEU LEU PRO HIS TRP ALA LYS VAL VAL LEU THR ASP PRO          
SEQRES  24 A  497  GLU ALA ALA LYS TYR VAL HIS GLY ILE ALA VAL HIS TRP          
SEQRES  25 A  497  TYR LEU ASP PHE LEU ALA PRO ALA LYS ALA THR LEU GLY          
SEQRES  26 A  497  GLU THR HIS ARG LEU PHE PRO ASN THR MET LEU PHE ALA          
SEQRES  27 A  497  SER GLU ALA CYS VAL GLY SER LYS PHE TRP GLU GLN SER          
SEQRES  28 A  497  VAL ARG LEU GLY SER TRP ASP ARG GLY MET GLN TYR SER          
SEQRES  29 A  497  HIS SER ILE ILE THR ASN LEU LEU TYR HIS VAL VAL GLY          
SEQRES  30 A  497  TRP THR ASP TRP ASN LEU ALA LEU ASN PRO GLU GLY GLY          
SEQRES  31 A  497  PRO ASN TRP VAL ARG ASN PHE VAL ASP SER PRO ILE ILE          
SEQRES  32 A  497  VAL ASP ILE THR LYS ASP THR PHE TYR LYS GLN PRO MET          
SEQRES  33 A  497  PHE TYR HIS LEU GLY HIS PHE SER LYS PHE ILE PRO GLU          
SEQRES  34 A  497  GLY SER GLN ARG VAL GLY LEU VAL ALA SER GLN LYS ASN          
SEQRES  35 A  497  ASP LEU ASP ALA VAL ALA LEU MET HIS PRO ASP GLY SER          
SEQRES  36 A  497  ALA VAL VAL VAL VAL LEU ASN ARG SER SER LYS ASP VAL          
SEQRES  37 A  497  PRO LEU THR ILE LYS ASP PRO ALA VAL GLY PHE LEU GLU          
SEQRES  38 A  497  THR ILE SER PRO GLY TYR SER ILE HIS THR TYR LEU TRP          
SEQRES  39 A  497  HIS ARG GLN                                                  
SEQRES   1 B  497  ALA ARG PRO CYS ILE PRO LYS SER PHE GLY TYR SER SER          
SEQRES   2 B  497  VAL VAL CYS VAL CYS ASN ALA THR TYR CYS ASP SER PHE          
SEQRES   3 B  497  ASP PRO PRO THR PHE PRO ALA LEU GLY THR PHE SER ARG          
SEQRES   4 B  497  TYR GLU SER THR ARG SER GLY ARG ARG MET GLU LEU SER          
SEQRES   5 B  497  MET GLY PRO ILE GLN ALA ASN HIS THR GLY THR GLY LEU          
SEQRES   6 B  497  LEU LEU THR LEU GLN PRO GLU GLN LYS PHE GLN LYS VAL          
SEQRES   7 B  497  LYS GLY PHE GLY GLY ALA MET THR ASP ALA ALA ALA LEU          
SEQRES   8 B  497  ASN ILE LEU ALA LEU SER PRO PRO ALA GLN ASN LEU LEU          
SEQRES   9 B  497  LEU LYS SER TYR PHE SER GLU GLU GLY ILE GLY TYR ASN          
SEQRES  10 B  497  ILE ILE ARG VAL PRO MET ALA SER CYS ASP PHE SER ILE          
SEQRES  11 B  497  ARG THR TYR THR TYR ALA ASP THR PRO ASP ASP PHE GLN          
SEQRES  12 B  497  LEU HIS ASN PHE SER LEU PRO GLU GLU ASP THR LYS LEU          
SEQRES  13 B  497  LYS ILE PRO LEU ILE HIS ARG ALA LEU GLN LEU ALA GLN          
SEQRES  14 B  497  ARG PRO VAL SER LEU LEU ALA SER PRO TRP THR SER PRO          
SEQRES  15 B  497  THR TRP LEU LYS THR ASN GLY ALA VAL ASN GLY LYS GLY          
SEQRES  16 B  497  SER LEU LYS GLY GLN PRO GLY ASP ILE TYR HIS GLN THR          
SEQRES  17 B  497  TRP ALA ARG TYR PHE VAL LYS PHE LEU ASP ALA TYR ALA          
SEQRES  18 B  497  GLU HIS LYS LEU GLN PHE TRP ALA VAL THR ALA GLU ASN          
SEQRES  19 B  497  GLU PRO SER ALA GLY LEU LEU SER GLY TYR PRO PHE GLN          
SEQRES  20 B  497  CYS LEU GLY PHE THR PRO GLU HIS GLN ARG ASP PHE ILE          
SEQRES  21 B  497  ALA ARG ASP LEU GLY PRO THR LEU ALA ASN SER THR HIS          
SEQRES  22 B  497  HIS ASN VAL ARG LEU LEU MET LEU ASP ASP GLN ARG LEU          
SEQRES  23 B  497  LEU LEU PRO HIS TRP ALA LYS VAL VAL LEU THR ASP PRO          
SEQRES  24 B  497  GLU ALA ALA LYS TYR VAL HIS GLY ILE ALA VAL HIS TRP          
SEQRES  25 B  497  TYR LEU ASP PHE LEU ALA PRO ALA LYS ALA THR LEU GLY          
SEQRES  26 B  497  GLU THR HIS ARG LEU PHE PRO ASN THR MET LEU PHE ALA          
SEQRES  27 B  497  SER GLU ALA CYS VAL GLY SER LYS PHE TRP GLU GLN SER          
SEQRES  28 B  497  VAL ARG LEU GLY SER TRP ASP ARG GLY MET GLN TYR SER          
SEQRES  29 B  497  HIS SER ILE ILE THR ASN LEU LEU TYR HIS VAL VAL GLY          
SEQRES  30 B  497  TRP THR ASP TRP ASN LEU ALA LEU ASN PRO GLU GLY GLY          
SEQRES  31 B  497  PRO ASN TRP VAL ARG ASN PHE VAL ASP SER PRO ILE ILE          
SEQRES  32 B  497  VAL ASP ILE THR LYS ASP THR PHE TYR LYS GLN PRO MET          
SEQRES  33 B  497  PHE TYR HIS LEU GLY HIS PHE SER LYS PHE ILE PRO GLU          
SEQRES  34 B  497  GLY SER GLN ARG VAL GLY LEU VAL ALA SER GLN LYS ASN          
SEQRES  35 B  497  ASP LEU ASP ALA VAL ALA LEU MET HIS PRO ASP GLY SER          
SEQRES  36 B  497  ALA VAL VAL VAL VAL LEU ASN ARG SER SER LYS ASP VAL          
SEQRES  37 B  497  PRO LEU THR ILE LYS ASP PRO ALA VAL GLY PHE LEU GLU          
SEQRES  38 B  497  THR ILE SER PRO GLY TYR SER ILE HIS THR TYR LEU TRP          
SEQRES  39 B  497  HIS ARG GLN                                                  
SEQRES   1 C  497  ALA ARG PRO CYS ILE PRO LYS SER PHE GLY TYR SER SER          
SEQRES   2 C  497  VAL VAL CYS VAL CYS ASN ALA THR TYR CYS ASP SER PHE          
SEQRES   3 C  497  ASP PRO PRO THR PHE PRO ALA LEU GLY THR PHE SER ARG          
SEQRES   4 C  497  TYR GLU SER THR ARG SER GLY ARG ARG MET GLU LEU SER          
SEQRES   5 C  497  MET GLY PRO ILE GLN ALA ASN HIS THR GLY THR GLY LEU          
SEQRES   6 C  497  LEU LEU THR LEU GLN PRO GLU GLN LYS PHE GLN LYS VAL          
SEQRES   7 C  497  LYS GLY PHE GLY GLY ALA MET THR ASP ALA ALA ALA LEU          
SEQRES   8 C  497  ASN ILE LEU ALA LEU SER PRO PRO ALA GLN ASN LEU LEU          
SEQRES   9 C  497  LEU LYS SER TYR PHE SER GLU GLU GLY ILE GLY TYR ASN          
SEQRES  10 C  497  ILE ILE ARG VAL PRO MET ALA SER CYS ASP PHE SER ILE          
SEQRES  11 C  497  ARG THR TYR THR TYR ALA ASP THR PRO ASP ASP PHE GLN          
SEQRES  12 C  497  LEU HIS ASN PHE SER LEU PRO GLU GLU ASP THR LYS LEU          
SEQRES  13 C  497  LYS ILE PRO LEU ILE HIS ARG ALA LEU GLN LEU ALA GLN          
SEQRES  14 C  497  ARG PRO VAL SER LEU LEU ALA SER PRO TRP THR SER PRO          
SEQRES  15 C  497  THR TRP LEU LYS THR ASN GLY ALA VAL ASN GLY LYS GLY          
SEQRES  16 C  497  SER LEU LYS GLY GLN PRO GLY ASP ILE TYR HIS GLN THR          
SEQRES  17 C  497  TRP ALA ARG TYR PHE VAL LYS PHE LEU ASP ALA TYR ALA          
SEQRES  18 C  497  GLU HIS LYS LEU GLN PHE TRP ALA VAL THR ALA GLU ASN          
SEQRES  19 C  497  GLU PRO SER ALA GLY LEU LEU SER GLY TYR PRO PHE GLN          
SEQRES  20 C  497  CYS LEU GLY PHE THR PRO GLU HIS GLN ARG ASP PHE ILE          
SEQRES  21 C  497  ALA ARG ASP LEU GLY PRO THR LEU ALA ASN SER THR HIS          
SEQRES  22 C  497  HIS ASN VAL ARG LEU LEU MET LEU ASP ASP GLN ARG LEU          
SEQRES  23 C  497  LEU LEU PRO HIS TRP ALA LYS VAL VAL LEU THR ASP PRO          
SEQRES  24 C  497  GLU ALA ALA LYS TYR VAL HIS GLY ILE ALA VAL HIS TRP          
SEQRES  25 C  497  TYR LEU ASP PHE LEU ALA PRO ALA LYS ALA THR LEU GLY          
SEQRES  26 C  497  GLU THR HIS ARG LEU PHE PRO ASN THR MET LEU PHE ALA          
SEQRES  27 C  497  SER GLU ALA CYS VAL GLY SER LYS PHE TRP GLU GLN SER          
SEQRES  28 C  497  VAL ARG LEU GLY SER TRP ASP ARG GLY MET GLN TYR SER          
SEQRES  29 C  497  HIS SER ILE ILE THR ASN LEU LEU TYR HIS VAL VAL GLY          
SEQRES  30 C  497  TRP THR ASP TRP ASN LEU ALA LEU ASN PRO GLU GLY GLY          
SEQRES  31 C  497  PRO ASN TRP VAL ARG ASN PHE VAL ASP SER PRO ILE ILE          
SEQRES  32 C  497  VAL ASP ILE THR LYS ASP THR PHE TYR LYS GLN PRO MET          
SEQRES  33 C  497  PHE TYR HIS LEU GLY HIS PHE SER LYS PHE ILE PRO GLU          
SEQRES  34 C  497  GLY SER GLN ARG VAL GLY LEU VAL ALA SER GLN LYS ASN          
SEQRES  35 C  497  ASP LEU ASP ALA VAL ALA LEU MET HIS PRO ASP GLY SER          
SEQRES  36 C  497  ALA VAL VAL VAL VAL LEU ASN ARG SER SER LYS ASP VAL          
SEQRES  37 C  497  PRO LEU THR ILE LYS ASP PRO ALA VAL GLY PHE LEU GLU          
SEQRES  38 C  497  THR ILE SER PRO GLY TYR SER ILE HIS THR TYR LEU TRP          
SEQRES  39 C  497  HIS ARG GLN                                                  
SEQRES   1 D  497  ALA ARG PRO CYS ILE PRO LYS SER PHE GLY TYR SER SER          
SEQRES   2 D  497  VAL VAL CYS VAL CYS ASN ALA THR TYR CYS ASP SER PHE          
SEQRES   3 D  497  ASP PRO PRO THR PHE PRO ALA LEU GLY THR PHE SER ARG          
SEQRES   4 D  497  TYR GLU SER THR ARG SER GLY ARG ARG MET GLU LEU SER          
SEQRES   5 D  497  MET GLY PRO ILE GLN ALA ASN HIS THR GLY THR GLY LEU          
SEQRES   6 D  497  LEU LEU THR LEU GLN PRO GLU GLN LYS PHE GLN LYS VAL          
SEQRES   7 D  497  LYS GLY PHE GLY GLY ALA MET THR ASP ALA ALA ALA LEU          
SEQRES   8 D  497  ASN ILE LEU ALA LEU SER PRO PRO ALA GLN ASN LEU LEU          
SEQRES   9 D  497  LEU LYS SER TYR PHE SER GLU GLU GLY ILE GLY TYR ASN          
SEQRES  10 D  497  ILE ILE ARG VAL PRO MET ALA SER CYS ASP PHE SER ILE          
SEQRES  11 D  497  ARG THR TYR THR TYR ALA ASP THR PRO ASP ASP PHE GLN          
SEQRES  12 D  497  LEU HIS ASN PHE SER LEU PRO GLU GLU ASP THR LYS LEU          
SEQRES  13 D  497  LYS ILE PRO LEU ILE HIS ARG ALA LEU GLN LEU ALA GLN          
SEQRES  14 D  497  ARG PRO VAL SER LEU LEU ALA SER PRO TRP THR SER PRO          
SEQRES  15 D  497  THR TRP LEU LYS THR ASN GLY ALA VAL ASN GLY LYS GLY          
SEQRES  16 D  497  SER LEU LYS GLY GLN PRO GLY ASP ILE TYR HIS GLN THR          
SEQRES  17 D  497  TRP ALA ARG TYR PHE VAL LYS PHE LEU ASP ALA TYR ALA          
SEQRES  18 D  497  GLU HIS LYS LEU GLN PHE TRP ALA VAL THR ALA GLU ASN          
SEQRES  19 D  497  GLU PRO SER ALA GLY LEU LEU SER GLY TYR PRO PHE GLN          
SEQRES  20 D  497  CYS LEU GLY PHE THR PRO GLU HIS GLN ARG ASP PHE ILE          
SEQRES  21 D  497  ALA ARG ASP LEU GLY PRO THR LEU ALA ASN SER THR HIS          
SEQRES  22 D  497  HIS ASN VAL ARG LEU LEU MET LEU ASP ASP GLN ARG LEU          
SEQRES  23 D  497  LEU LEU PRO HIS TRP ALA LYS VAL VAL LEU THR ASP PRO          
SEQRES  24 D  497  GLU ALA ALA LYS TYR VAL HIS GLY ILE ALA VAL HIS TRP          
SEQRES  25 D  497  TYR LEU ASP PHE LEU ALA PRO ALA LYS ALA THR LEU GLY          
SEQRES  26 D  497  GLU THR HIS ARG LEU PHE PRO ASN THR MET LEU PHE ALA          
SEQRES  27 D  497  SER GLU ALA CYS VAL GLY SER LYS PHE TRP GLU GLN SER          
SEQRES  28 D  497  VAL ARG LEU GLY SER TRP ASP ARG GLY MET GLN TYR SER          
SEQRES  29 D  497  HIS SER ILE ILE THR ASN LEU LEU TYR HIS VAL VAL GLY          
SEQRES  30 D  497  TRP THR ASP TRP ASN LEU ALA LEU ASN PRO GLU GLY GLY          
SEQRES  31 D  497  PRO ASN TRP VAL ARG ASN PHE VAL ASP SER PRO ILE ILE          
SEQRES  32 D  497  VAL ASP ILE THR LYS ASP THR PHE TYR LYS GLN PRO MET          
SEQRES  33 D  497  PHE TYR HIS LEU GLY HIS PHE SER LYS PHE ILE PRO GLU          
SEQRES  34 D  497  GLY SER GLN ARG VAL GLY LEU VAL ALA SER GLN LYS ASN          
SEQRES  35 D  497  ASP LEU ASP ALA VAL ALA LEU MET HIS PRO ASP GLY SER          
SEQRES  36 D  497  ALA VAL VAL VAL VAL LEU ASN ARG SER SER LYS ASP VAL          
SEQRES  37 D  497  PRO LEU THR ILE LYS ASP PRO ALA VAL GLY PHE LEU GLU          
SEQRES  38 D  497  THR ILE SER PRO GLY TYR SER ILE HIS THR TYR LEU TRP          
SEQRES  39 D  497  HIS ARG GLN                                                  
MODRES 3RIK ASN A   19  ASN  GLYCOSYLATION SITE                                 
MODRES 3RIK ASN B   19  ASN  GLYCOSYLATION SITE                                 
MODRES 3RIK ASN D   19  ASN  GLYCOSYLATION SITE                                 
MODRES 3RIK ASN C   19  ASN  GLYCOSYLATION SITE                                 
HET    SO4  A 501       5                                                       
HET    SO4  A 502       5                                                       
HET    SO4  A 503       5                                                       
HET    SO4  A 504       5                                                       
HET    SO4  A 505       5                                                       
HET    SO4  A 506       5                                                       
HET    SO4  A 507       5                                                       
HET    SO4  A 508       5                                                       
HET    SO4  A 509       5                                                       
HET    SO4  A 510       5                                                       
HET    NAG  A 511      14                                                       
HET    3RI  B 501      14                                                       
HET    SO4  B 502       5                                                       
HET    SO4  B 503       5                                                       
HET    SO4  B 504       5                                                       
HET    SO4  B 505       5                                                       
HET    SO4  B 506       5                                                       
HET    SO4  B 507       5                                                       
HET    SO4  B 508       5                                                       
HET    SO4  B 509       5                                                       
HET    NAG  B 510      14                                                       
HET    SO4  C 501       5                                                       
HET    SO4  C 502       5                                                       
HET    SO4  C 503       5                                                       
HET    SO4  C 504       5                                                       
HET    SO4  C 505       5                                                       
HET    SO4  C 506       5                                                       
HET    SO4  C 507       5                                                       
HET    SO4  C 508       5                                                       
HET    SO4  C 509       5                                                       
HET    NAG  C 510      14                                                       
HET    3RI  D 501      14                                                       
HET    SO4  D 502       5                                                       
HET    SO4  D 503       5                                                       
HET    SO4  D 504       5                                                       
HET    SO4  D 505       5                                                       
HET    SO4  D 506       5                                                       
HET    SO4  D 507       5                                                       
HET    SO4  D 508       5                                                       
HET    NAG  D 509      14                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     3RI (3S,4R,5R,6S)-1-(2-HYDROXYETHYL)AZEPANE-3,4,5,6-TETROL           
FORMUL   5  SO4    34(O4 S 2-)                                                  
FORMUL  15  NAG    4(C8 H15 N O6)                                               
FORMUL  16  3RI    2(C8 H17 N O5)                                               
FORMUL  45  HOH   *908(H2 O)                                                    
HELIX    1   1 THR A   86  ALA A   95  1                                  10    
HELIX    2   2 SER A   97  SER A  110  1                                  14    
HELIX    3   3 PRO A  150  LYS A  155  1                                   6    
HELIX    4   4 LEU A  156  ALA A  168  1                                  13    
HELIX    5   5 PRO A  182  LYS A  186  5                                   5    
HELIX    6   6 ASP A  203  HIS A  223  1                                  21    
HELIX    7   7 SER A  237  LEU A  241  5                                   5    
HELIX    8   8 THR A  252  ASP A  263  1                                  12    
HELIX    9   9 ASP A  263  ASN A  270  1                                   8    
HELIX   10  10 LEU A  286  LEU A  288  5                                   3    
HELIX   11  11 PRO A  289  THR A  297  1                                   9    
HELIX   12  12 ASP A  298  LYS A  303  1                                   6    
HELIX   13  13 LEU A  314  ALA A  318  5                                   5    
HELIX   14  14 THR A  323  PHE A  331  1                                   9    
HELIX   15  15 SER A  356  TYR A  373  1                                  18    
HELIX   16  16 ILE A  406  ASP A  409  5                                   4    
HELIX   17  17 GLN A  414  LYS A  425  1                                  12    
HELIX   18  18 THR B   86  ALA B   95  1                                  10    
HELIX   19  19 SER B   97  SER B  110  1                                  14    
HELIX   20  20 PRO B  150  LYS B  155  1                                   6    
HELIX   21  21 LEU B  156  ALA B  168  1                                  13    
HELIX   22  22 PRO B  182  LYS B  186  5                                   5    
HELIX   23  23 ASP B  203  HIS B  223  1                                  21    
HELIX   24  24 GLU B  235  LEU B  241  5                                   7    
HELIX   25  25 THR B  252  ASP B  263  1                                  12    
HELIX   26  26 ASP B  263  ASN B  270  1                                   8    
HELIX   27  27 LEU B  286  LEU B  288  5                                   3    
HELIX   28  28 PRO B  289  THR B  297  1                                   9    
HELIX   29  29 ASP B  298  LYS B  303  1                                   6    
HELIX   30  30 THR B  323  PHE B  331  1                                   9    
HELIX   31  31 SER B  356  TYR B  373  1                                  18    
HELIX   32  32 ILE B  406  ASP B  409  5                                   4    
HELIX   33  33 GLN B  414  LYS B  425  1                                  12    
HELIX   34  34 THR C   86  ALA C   95  1                                  10    
HELIX   35  35 SER C   97  SER C  110  1                                  14    
HELIX   36  36 PRO C  150  LYS C  155  1                                   6    
HELIX   37  37 LEU C  156  ALA C  168  1                                  13    
HELIX   38  38 PRO C  182  LYS C  186  5                                   5    
HELIX   39  39 ASP C  203  HIS C  223  1                                  21    
HELIX   40  40 SER C  237  LEU C  241  5                                   5    
HELIX   41  41 THR C  252  ASP C  263  1                                  12    
HELIX   42  42 ASP C  263  ASN C  270  1                                   8    
HELIX   43  43 LEU C  286  LEU C  288  5                                   3    
HELIX   44  44 PRO C  289  THR C  297  1                                   9    
HELIX   45  45 ASP C  298  LYS C  303  1                                   6    
HELIX   46  46 LEU C  314  ALA C  318  5                                   5    
HELIX   47  47 PRO C  319  ALA C  322  5                                   4    
HELIX   48  48 THR C  323  PHE C  331  1                                   9    
HELIX   49  49 SER C  356  TYR C  373  1                                  18    
HELIX   50  50 ILE C  406  LYS C  408  5                                   3    
HELIX   51  51 GLN C  414  LYS C  425  1                                  12    
HELIX   52  52 THR D   86  ALA D   95  1                                  10    
HELIX   53  53 SER D   97  SER D  110  1                                  14    
HELIX   54  54 PRO D  150  LYS D  155  1                                   6    
HELIX   55  55 LEU D  156  ALA D  168  1                                  13    
HELIX   56  56 PRO D  182  LYS D  186  5                                   5    
HELIX   57  57 ASP D  203  HIS D  223  1                                  21    
HELIX   58  58 SER D  237  LEU D  241  5                                   5    
HELIX   59  59 THR D  252  ASP D  263  1                                  12    
HELIX   60  60 ASP D  263  ASN D  270  1                                   8    
HELIX   61  61 LEU D  286  LEU D  288  5                                   3    
HELIX   62  62 PRO D  289  THR D  297  1                                   9    
HELIX   63  63 ASP D  298  LYS D  303  1                                   6    
HELIX   64  64 THR D  323  PHE D  331  1                                   9    
HELIX   65  65 SER D  356  TYR D  373  1                                  18    
HELIX   66  66 ILE D  406  ASP D  409  5                                   4    
HELIX   67  67 GLN D  414  LYS D  425  1                                  12    
SHEET    1   A 4 PRO A   6  LYS A   7  0                                        
SHEET    2   A 4 VAL A  15  CYS A  18 -1  O  VAL A  15   N  LYS A   7           
SHEET    3   A 4 THR A 410  LYS A 413 -1  O  PHE A 411   N  CYS A  18           
SHEET    4   A 4 ILE A 402  ASP A 405 -1  N  ASP A 405   O  THR A 410           
SHEET    1   B 9 GLU A  50  PRO A  55  0                                        
SHEET    2   B 9 THR A  36  THR A  43 -1  N  ARG A  39   O  SER A  52           
SHEET    3   B 9 SER A 488  TRP A 494 -1  O  LEU A 493   N  SER A  38           
SHEET    4   B 9 ALA A 456  ASN A 462 -1  N  VAL A 458   O  TYR A 492           
SHEET    5   B 9 LEU A 444  MET A 450 -1  N  ASP A 445   O  LEU A 461           
SHEET    6   B 9 GLN A 432  ALA A 438 -1  N  GLN A 432   O  MET A 450           
SHEET    7   B 9 LEU A  65  LYS A  77 -1  N  THR A  68   O  VAL A 437           
SHEET    8   B 9 VAL A 468  ASP A 474  1  O  LYS A 473   N  LEU A  69           
SHEET    9   B 9 GLY A 478  SER A 484 -1  O  SER A 484   N  VAL A 468           
SHEET    1   C 9 GLY A  80  ALA A  84  0                                        
SHEET    2   C 9 ILE A 118  MET A 123  1  O  ARG A 120   N  GLY A  83           
SHEET    3   C 9 SER A 173  PRO A 178  1  O  LEU A 175   N  ILE A 119           
SHEET    4   C 9 ALA A 229  THR A 231  1  O  ALA A 229   N  ALA A 176           
SHEET    5   C 9 ARG A 277  GLN A 284  1  O  LEU A 279   N  VAL A 230           
SHEET    6   C 9 VAL A 305  HIS A 311  1  O  ALA A 309   N  MET A 280           
SHEET    7   C 9 MET A 335  GLU A 340  1  O  MET A 335   N  ILE A 308           
SHEET    8   C 9 VAL A 375  ASN A 382  1  O  VAL A 376   N  LEU A 336           
SHEET    9   C 9 GLY A  80  ALA A  84  1  N  GLY A  80   O  TRP A 378           
SHEET    1   D 4 PRO B   6  LYS B   7  0                                        
SHEET    2   D 4 VAL B  15  CYS B  18 -1  O  VAL B  15   N  LYS B   7           
SHEET    3   D 4 THR B 410  LYS B 413 -1  O  PHE B 411   N  CYS B  18           
SHEET    4   D 4 ILE B 402  ASP B 405 -1  N  ASP B 405   O  THR B 410           
SHEET    1   E 9 GLU B  50  PRO B  55  0                                        
SHEET    2   E 9 THR B  36  THR B  43 -1  N  ARG B  39   O  SER B  52           
SHEET    3   E 9 SER B 488  TRP B 494 -1  O  LEU B 493   N  SER B  38           
SHEET    4   E 9 ALA B 456  ASN B 462 -1  N  ALA B 456   O  TRP B 494           
SHEET    5   E 9 LEU B 444  MET B 450 -1  N  ASP B 445   O  LEU B 461           
SHEET    6   E 9 GLN B 432  ALA B 438 -1  N  GLN B 432   O  MET B 450           
SHEET    7   E 9 LEU B  66  LYS B  77 -1  N  THR B  68   O  VAL B 437           
SHEET    8   E 9 VAL B 468  ASP B 474  1  O  LYS B 473   N  LEU B  69           
SHEET    9   E 9 GLY B 478  SER B 484 -1  O  GLY B 478   N  ASP B 474           
SHEET    1   F 9 GLY B  80  ALA B  84  0                                        
SHEET    2   F 9 ILE B 118  MET B 123  1  O  ARG B 120   N  GLY B  83           
SHEET    3   F 9 SER B 173  PRO B 178  1  O  LEU B 175   N  VAL B 121           
SHEET    4   F 9 ALA B 229  THR B 231  1  O  THR B 231   N  ALA B 176           
SHEET    5   F 9 ARG B 277  GLN B 284  1  O  LEU B 279   N  VAL B 230           
SHEET    6   F 9 GLY B 307  TYR B 313  1  O  ALA B 309   N  MET B 280           
SHEET    7   F 9 MET B 335  CYS B 342  1  O  MET B 335   N  ILE B 308           
SHEET    8   F 9 VAL B 375  ASN B 382  1  O  VAL B 376   N  LEU B 336           
SHEET    9   F 9 GLY B  80  ALA B  84  1  N  GLY B  82   O  ASP B 380           
SHEET    1   G 4 PRO C   6  LYS C   7  0                                        
SHEET    2   G 4 VAL C  15  ASN C  19 -1  O  VAL C  15   N  LYS C   7           
SHEET    3   G 4 THR C 410  LYS C 413 -1  O  PHE C 411   N  CYS C  18           
SHEET    4   G 4 ILE C 402  ASP C 405 -1  N  ASP C 405   O  THR C 410           
SHEET    1   H 9 GLU C  50  PRO C  55  0                                        
SHEET    2   H 9 THR C  36  THR C  43 -1  N  ARG C  39   O  SER C  52           
SHEET    3   H 9 SER C 488  TRP C 494 -1  O  LEU C 493   N  SER C  38           
SHEET    4   H 9 ALA C 456  ASN C 462 -1  N  VAL C 458   O  TYR C 492           
SHEET    5   H 9 LEU C 444  MET C 450 -1  N  ASP C 445   O  LEU C 461           
SHEET    6   H 9 GLN C 432  ALA C 438 -1  N  GLN C 432   O  MET C 450           
SHEET    7   H 9 LEU C  65  LYS C  77 -1  N  THR C  68   O  VAL C 437           
SHEET    8   H 9 VAL C 468  ASP C 474  1  O  LYS C 473   N  LEU C  69           
SHEET    9   H 9 GLY C 478  SER C 484 -1  O  LEU C 480   N  ILE C 472           
SHEET    1   I 9 GLY C  80  ALA C  84  0                                        
SHEET    2   I 9 ILE C 118  MET C 123  1  O  ARG C 120   N  GLY C  83           
SHEET    3   I 9 SER C 173  PRO C 178  1  O  LEU C 175   N  VAL C 121           
SHEET    4   I 9 ALA C 229  THR C 231  1  O  ALA C 229   N  ALA C 176           
SHEET    5   I 9 ARG C 277  GLN C 284  1  O  LEU C 279   N  VAL C 230           
SHEET    6   I 9 VAL C 305  HIS C 311  1  O  ALA C 309   N  MET C 280           
SHEET    7   I 9 MET C 335  GLU C 340  1  O  MET C 335   N  ILE C 308           
SHEET    8   I 9 VAL C 375  ASN C 382  1  O  VAL C 376   N  LEU C 336           
SHEET    9   I 9 GLY C  80  ALA C  84  1  N  GLY C  82   O  ASP C 380           
SHEET    1   J 4 PRO D   6  LYS D   7  0                                        
SHEET    2   J 4 VAL D  15  CYS D  18 -1  O  VAL D  15   N  LYS D   7           
SHEET    3   J 4 THR D 410  LYS D 413 -1  O  PHE D 411   N  CYS D  18           
SHEET    4   J 4 ILE D 402  ASP D 405 -1  N  ILE D 403   O  TYR D 412           
SHEET    1   K 9 GLU D  50  PRO D  55  0                                        
SHEET    2   K 9 THR D  36  THR D  43 -1  N  ARG D  39   O  SER D  52           
SHEET    3   K 9 SER D 488  TRP D 494 -1  O  LEU D 493   N  SER D  38           
SHEET    4   K 9 ALA D 456  ASN D 462 -1  N  ALA D 456   O  TRP D 494           
SHEET    5   K 9 LEU D 444  MET D 450 -1  N  ASP D 445   O  LEU D 461           
SHEET    6   K 9 GLN D 432  ALA D 438 -1  N  VAL D 434   O  ALA D 448           
SHEET    7   K 9 LEU D  65  LYS D  77 -1  N  THR D  68   O  VAL D 437           
SHEET    8   K 9 VAL D 468  ASP D 474  1  O  LYS D 473   N  LEU D  69           
SHEET    9   K 9 GLY D 478  SER D 484 -1  O  GLY D 478   N  ASP D 474           
SHEET    1   L 9 GLY D  80  ALA D  84  0                                        
SHEET    2   L 9 ILE D 118  MET D 123  1  O  ARG D 120   N  GLY D  83           
SHEET    3   L 9 SER D 173  PRO D 178  1  O  LEU D 175   N  VAL D 121           
SHEET    4   L 9 ALA D 229  THR D 231  1  O  ALA D 229   N  ALA D 176           
SHEET    5   L 9 ARG D 277  GLN D 284  1  O  LEU D 279   N  VAL D 230           
SHEET    6   L 9 GLY D 307  TYR D 313  1  O  HIS D 311   N  ASP D 283           
SHEET    7   L 9 MET D 335  CYS D 342  1  O  PHE D 337   N  VAL D 310           
SHEET    8   L 9 VAL D 375  ASN D 382  1  O  VAL D 376   N  LEU D 336           
SHEET    9   L 9 GLY D  80  ALA D  84  1  N  GLY D  82   O  ASP D 380           
SSBOND   1 CYS A    4    CYS A   16                          1555   1555  2.10  
SSBOND   2 CYS A   18    CYS A   23                          1555   1555  2.21  
SSBOND   3 CYS B    4    CYS B   16                          1555   1555  2.13  
SSBOND   4 CYS B   18    CYS B   23                          1555   1555  2.24  
SSBOND   5 CYS C    4    CYS C   16                          1555   1555  2.12  
SSBOND   6 CYS C   18    CYS C   23                          1555   1555  2.23  
SSBOND   7 CYS D    4    CYS D   16                          1555   1555  2.13  
SSBOND   8 CYS D   18    CYS D   23                          1555   1555  2.24  
LINK         ND2 ASN A  19                 C1  NAG A 511     1555   1555  1.42  
LINK         ND2 ASN B  19                 C1  NAG B 510     1555   1555  1.86  
LINK         ND2 ASN D  19                 C1  NAG D 509     1555   1555  1.94  
LINK         ND2 ASN C  19                 C1  NAG C 510     1555   1555  2.12  
CISPEP   1 LEU A  288    PRO A  289          0         2.98                     
CISPEP   2 ALA A  318    PRO A  319          0         5.89                     
CISPEP   3 GLY A  344    SER A  345          0        11.27                     
CISPEP   4 GLY A  390    PRO A  391          0         4.36                     
CISPEP   5 GLY B   62    THR B   63          0       -12.57                     
CISPEP   6 LEU B  288    PRO B  289          0         5.05                     
CISPEP   7 ALA B  318    PRO B  319          0        -1.27                     
CISPEP   8 GLY B  344    SER B  345          0        -3.68                     
CISPEP   9 GLY B  390    PRO B  391          0         8.93                     
CISPEP  10 LEU C  288    PRO C  289          0         8.46                     
CISPEP  11 GLY C  390    PRO C  391          0         4.59                     
CISPEP  12 LEU D  288    PRO D  289          0         3.45                     
CISPEP  13 GLY D  390    PRO D  391          0         5.08                     
SITE     1 AC1  7 TYR A  11  SER A  12  ARG A 353  SER A 356                    
SITE     2 AC1  7 TRP A 357  ASP A 358  HOH A 740                               
SITE     1 AC2  5 LYS A  79  TRP A 228  ARG A 277  HIS A 306                    
SITE     2 AC2  5 HOH A 776                                                     
SITE     1 AC3  5 GLN A 169  ARG A 170  PRO A 428  HIS A 451                    
SITE     2 AC3  5 HOH A 758                                                     
SITE     1 AC4  4 ARG A 329  LEU A 330  LYS D 321  ARG D 329                    
SITE     1 AC5  4 THR A  63  GLY A  64  GLN A 440  LYS C 473                    
SITE     1 AC6  4 ARG A  44  SER A  45  HOH A 712  HOH A 791                    
SITE     1 AC7  3 ARG A  44  SER A 465  TYR A 487                               
SITE     1 AC8  3 GLU A 254  ARG A 257  HOH A 808                               
SITE     1 AC9  7 LYS A 473  HOH A 775  HOH A 801  HOH A 806                    
SITE     2 AC9  7 THR C  63  GLY C  64  GLN C 440                               
SITE     1 BC1  1 ARG A 277                                                     
SITE     1 BC2  6 ILE A   5  ASN A  19  TYR A  22  HOH A 667                    
SITE     2 BC2  6 HOH A 671  HOH A 802                                          
SITE     1 BC3 13 ASP B 127  PHE B 128  TRP B 179  ASN B 234                    
SITE     2 BC3 13 GLU B 235  PHE B 246  GLN B 284  HIS B 311                    
SITE     3 BC3 13 TRP B 312  TYR B 313  GLU B 340  TRP B 381                    
SITE     4 BC3 13 ASN B 396                                                     
SITE     1 BC4  6 TYR B  11  SER B  12  ARG B 353  SER B 356                    
SITE     2 BC4  6 TRP B 357  ASP B 358                                          
SITE     1 BC5  4 LYS B  79  TRP B 228  ARG B 277  HIS B 306                    
SITE     1 BC6  6 GLY B 193  LYS B 194  SER B 242  GLY B 243                    
SITE     2 BC6  6 HOH B 718  HOH B 779                                          
SITE     1 BC7  5 ARG B  44  SER B  45  HOH B 683  HOH B 756                    
SITE     2 BC7  5 HOH B 827                                                     
SITE     1 BC8  3 SER B  45  ARG B  47  HOH B 759                               
SITE     1 BC9  1 ARG B 277                                                     
SITE     1 CC1  5 GLU B 111  ARG B 170  PRO B 428  HIS B 451                    
SITE     2 CC1  5 HOH B 793                                                     
SITE     1 CC2  3 ARG B  44  SER B 465  TYR B 487                               
SITE     1 CC3  3 ILE B   5  ASN B  19  HOH B 661                               
SITE     1 CC4  6 TYR C  11  SER C  12  ARG C 353  SER C 356                    
SITE     2 CC4  6 TRP C 357  ASP C 358                                          
SITE     1 CC5  5 LYS C  79  TRP C 228  ARG C 277  HIS C 306                    
SITE     2 CC5  5 HOH C 744                                                     
SITE     1 CC6  4 LYS B 321  ARG B 329  ARG C 329  LEU C 330                    
SITE     1 CC7  4 ARG C 170  PRO C 428  HIS C 451  HOH C 780                    
SITE     1 CC8  3 ARG C  44  SER C  45  HOH C 700                               
SITE     1 CC9  6 ARG C 285  PRO C 319  ALA C 320  THR C 369                    
SITE     2 CC9  6 HOH C 652  HOH C 778                                          
SITE     1 DC1  3 GLU C 254  ARG C 257  HOH C 819                               
SITE     1 DC2  2 SER C  45  ARG C  47                                          
SITE     1 DC3  3 ARG C  44  SER C 465  TYR C 487                               
SITE     1 DC4  3 ILE C   5  ASN C  19  TYR C  22                               
SITE     1 DC5 11 ASP D 127  PHE D 128  TRP D 179  ASN D 234                    
SITE     2 DC5 11 GLU D 235  PHE D 246  TRP D 312  TYR D 313                    
SITE     3 DC5 11 GLU D 340  TRP D 381  VAL D 398                               
SITE     1 DC6  7 TYR D  11  SER D  12  ARG D 353  SER D 356                    
SITE     2 DC6  7 TRP D 357  ASP D 358  HOH D 812                               
SITE     1 DC7  6 GLY D 193  LYS D 194  SER D 242  GLY D 243                    
SITE     2 DC7  6 HOH D 674  HOH D 701                                          
SITE     1 DC8  4 LYS D  79  TRP D 228  ARG D 277  HIS D 306                    
SITE     1 DC9  5 ARG D  44  SER D  45  HOH D 618  HOH D 671                    
SITE     2 DC9  5 HOH D 753                                                     
SITE     1 EC1  4 THR D  43  SER D  45  ARG D  47  HOH D 749                    
SITE     1 EC2  3 ARG D  44  SER D 465  TYR D 487                               
SITE     1 EC3  1 ARG D 277                                                     
SITE     1 EC4  4 ILE D   5  ASN D  19  HOH D 681  HOH D 804                    
CRYST1  107.980   91.553  152.213  90.00 110.70  90.00 P 1 21 1      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      0.009261  0.000000  0.003499        0.00000                         
SCALE2      0.000000  0.010923  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007023        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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