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Database: PDB
Entry: 2NT0
LinkDB: 2NT0
Original site: 2NT0 
HEADER    HYDROLASE                               06-NOV-06   2NT0              
TITLE     ACID-BETA-GLUCOSIDASE LOW PH, GLYCEROL BOUND                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUCOSYLCERAMIDASE;                                        
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: BETA-GLUCOCEREBROSIDASE, ACID BETA-GLUCOSIDASE, D-GLUCOSYL- 
COMPND   5 N-ACYLSPHINGOSINE GLUCOHYDROLASE, ALGLUCERASE, IMIGLUCERASE;         
COMPND   6 EC: 3.2.1.45;                                                        
COMPND   7 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;                                                           
SOURCE   6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE   7 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE   9 EXPRESSION_SYSTEM_ORGAN: OVARY                                       
KEYWDS    CEREZYME, GLUCOCEREBROSIDASE, GLUCOSYLCERAMIDE, HYDROLYSIS, GAUCHER   
KEYWDS   2 DISEASE, HYDROLASE                                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.L.LIEBERMAN,G.A.PETSKO,D.RINGE                                      
REVDAT   3   13-JUL-11 2NT0    1       VERSN                                    
REVDAT   2   24-FEB-09 2NT0    1       VERSN                                    
REVDAT   1   26-DEC-06 2NT0    0                                                
JRNL        AUTH   R.L.LIEBERMAN,B.A.WUSTMAN,P.HUERTAS,A.C.POWE,C.W.PINE,       
JRNL        AUTH 2 R.KHANNA,M.G.SCHLOSSMACHER,D.RINGE,G.A.PETSKO                
JRNL        TITL   STRUCTURE OF ACID BETA-GLUCOSIDASE WITH PHARMACOLOGICAL      
JRNL        TITL 2 CHAPERONE PROVIDES INSIGHT INTO GAUCHER DISEASE.             
JRNL        REF    NAT.CHEM.BIOL.                V.   3   101 2007              
JRNL        REFN                   ISSN 1552-4450                               
JRNL        PMID   17187079                                                     
JRNL        DOI    10.1038/NCHEMBIO850                                          
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  TITL   STRUCTURE OF ACID-BETA-GLUCOSIDASE WITH PHARMACOLOGICAL      
REMARK   1  TITL 2 CHAPERONE PROVIDES INSIGHT INTO GAUCHER DISEASE              
REMARK   1  REF    NAT.CHEM.BIOL.                             2006              
REMARK   1  REFN                   ESSN 1552-4469                               
REMARK   1  DOI    10.1038/NCHEMBIO850                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.79 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) : 1.79                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 84.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 220955                         
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) : 0.181                           
REMARK   3   R VALUE            (WORKING SET) : 0.179                           
REMARK   3   FREE R VALUE                     : 0.215                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 11117                           
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) : 1.79                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.83                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 11696                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 63.17                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2690                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 588                          
REMARK   3   BIN FREE R VALUE                    : 0.3170                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 15720                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 248                                     
REMARK   3   SOLVENT ATOMS            : 1710                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 24.35                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 24.35                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.15000                                              
REMARK   3    B22 (A**2) : -1.24000                                             
REMARK   3    B33 (A**2) : -1.15000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.33000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.123         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.121         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.076         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.437         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.963                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.946                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 16525 ; 0.017 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 22584 ; 1.585 ; 1.958       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1984 ; 6.833 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   720 ;36.931 ;23.444       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2516 ;14.367 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    84 ;18.413 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2416 ; 0.115 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 12536 ; 0.008 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  8643 ; 0.219 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A): 11086 ; 0.308 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  1673 ; 0.197 ; 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):    67 ; 0.200 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    26 ; 0.165 ; 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): 10191 ; 1.011 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 16072 ; 1.530 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  7184 ; 2.485 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  6328 ; 3.622 ; 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: NULL                                      
REMARK   4                                                                      
REMARK   4 2NT0 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-NOV-06.                  
REMARK 100 THE RCSB ID CODE IS RCSB040264.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-SEP-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-B                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 220956                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 84.8                               
REMARK 200  DATA REDUNDANCY                : 2.100                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.06200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.6000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.86                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 71.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.80                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.41700                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: 1OGS MONOMER                                         
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.24                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.17                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1 M AMMONIUM SULFATE  0.17 M             
REMARK 280  GUANIDINIUM HCL 0.02 M KCL 0.1 M ACETATE BUFFER PH 4.5              
REMARK 280  CRYOPROTECTANT INCLUDES 20% GLYCEROL, VAPOR DIFFUSION, HANGING      
REMARK 280  DROP, TEMPERATURE 298K                                              
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       45.87950            
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                                              
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 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   OE1  GLU C   151     O    HOH C  2005              1.32            
REMARK 500   OE1  GLN A    73     O    HOH A   869              1.71            
REMARK 500   O    PHE A   109     O    HOH A   903              1.72            
REMARK 500   O    HOH C  1644     O    HOH C  1990              1.74            
REMARK 500   O    HOH B   609     O    HOH B   913              1.79            
REMARK 500   O7   NAG B   498     O    HOH B   602              1.80            
REMARK 500   O    HOH D   584     O    HOH D   889              1.82            
REMARK 500   O    HOH C  1615     O    HOH C  1929              1.88            
REMARK 500   O3   GOL D   508     O    HOH D   798              1.93            
REMARK 500   O    HOH D   564     O    HOH D   829              1.94            
REMARK 500   O    HOH D   942     O    HOH D   944              1.97            
REMARK 500   CB   SER C   196     O    HOH C  1949              1.97            
REMARK 500   OD1  ASN D   102     O    HOH D   806              2.01            
REMARK 500   CB   ILE D    93     O    HOH D   750              2.01            
REMARK 500   O    HOH C  1627     O    HOH D   900              2.02            
REMARK 500   O    HOH A   562     O    HOH A   804              2.03            
REMARK 500   NH2  ARG C   211     O    HOH C  1872              2.03            
REMARK 500   OE1  GLU C   388     O    HOH C  1776              2.04            
REMARK 500   O    HOH B   757     O    HOH B   865              2.05            
REMARK 500   OE2  GLU B   152     O    HOH B   842              2.05            
REMARK 500   C    PHE A   109     O    HOH A   903              2.07            
REMARK 500   OH   TYR D    11     OE1  GLN D   350              2.07            
REMARK 500   O    HOH B   797     O    HOH B   897              2.07            
REMARK 500   OE1  GLN C    57     O    HOH C  1870              2.08            
REMARK 500   O    HOH C  1759     O    HOH C  1927              2.10            
REMARK 500   ND2  ASN B    19     O5   NAG B   498              2.10            
REMARK 500   CG   ASN B   146     C1   NAG B   499              2.11            
REMARK 500   O    HOH B   926     O    HOH B   963              2.11            
REMARK 500   ND2  ASN B    19     C5   NAG B   498              2.11            
REMARK 500   O    HOH D   702     O    HOH D   916              2.13            
REMARK 500   O    HOH B   757     O    HOH B   948              2.13            
REMARK 500   O    HOH A   722     O    HOH A   814              2.13            
REMARK 500   C1   NAG B   498     O    HOH B   964              2.13            
REMARK 500   SG   CYS C    23     O    HOH C  1989              2.13            
REMARK 500   O    HOH D   665     O    HOH D   875              2.13            
REMARK 500   OD1  ASN C   102     O    HOH C  1813              2.14            
REMARK 500   OD2  ASP A   405     O    HOH A   729              2.14            
REMARK 500   O    HOH D   597     O    HOH D   844              2.14            
REMARK 500   CB   CYS C    23     O    HOH C  1989              2.15            
REMARK 500   OH   TYR B    11     OE1  GLN B   350              2.15            
REMARK 500   OD1  ASN A   146     O    HOH A   835              2.16            
REMARK 500   CA   ALA A   168     O    HOH A   903              2.18            
REMARK 500   OG1  THR A   410     O    HOH A   824              2.18            
REMARK 500   O    HOH B   842     O    HOH C  1685              2.18            
REMARK 500   OD2  ASP B   405     O    HOH B   627              2.18            
REMARK 500   O    HOH C  1895     O    HOH C  1984              2.19            
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 B 480   CA  -  CB  -  CG  ANGL. DEV. =  16.1 DEGREES          
REMARK 500    ARG D  44   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.0 DEGREES          
REMARK 500    VAL D 394   CG1 -  CB  -  CG2 ANGL. DEV. =  10.6 DEGREES          
REMARK 500    ARG D 433   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500    LEU D 480   CA  -  CB  -  CG  ANGL. DEV. =  18.0 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     -159.70   -146.80                                   
REMARK 500    PHE A  75     -139.35   -122.88                                   
REMARK 500    ALA A 124     -154.63     67.74                                   
REMARK 500    ASP A 141       66.06   -106.64                                   
REMARK 500    LEU A 156      -68.68   -103.44                                   
REMARK 500    ASN A 192     -158.83   -125.79                                   
REMARK 500    GLU A 233      136.79    167.72                                   
REMARK 500    ASP A 263      -62.38   -123.57                                   
REMARK 500    LEU A 281      -79.47     68.84                                   
REMARK 500    THR A 323      -76.92   -108.50                                   
REMARK 500    HIS A 374       -3.99     83.56                                   
REMARK 500    TRP A 381     -139.85    -81.70                                   
REMARK 500    VAL A 394      -64.81    -98.17                                   
REMARK 500    PHE A 397      -11.99   -151.19                                   
REMARK 500    VAL A 477      -39.18   -133.93                                   
REMARK 500    THR B  61     -154.55    -80.91                                   
REMARK 500    PHE B  75     -133.02   -116.00                                   
REMARK 500    ALA B 124     -151.67     67.91                                   
REMARK 500    LEU B 156      -70.48   -112.47                                   
REMARK 500    ASN B 192     -166.70   -111.92                                   
REMARK 500    GLU B 233      132.04    167.15                                   
REMARK 500    LEU B 281      -82.27     71.15                                   
REMARK 500    ALA B 318       84.98   -160.21                                   
REMARK 500    PRO B 319      119.04    -35.96                                   
REMARK 500    THR B 323      -76.60   -107.38                                   
REMARK 500    SER B 356      108.59    -53.44                                   
REMARK 500    HIS B 374       -1.06     77.82                                   
REMARK 500    TRP B 381     -140.31    -85.67                                   
REMARK 500    ASN B 396       57.56    -90.60                                   
REMARK 500    ASN C  19     -158.57   -149.24                                   
REMARK 500    PHE C  75     -137.99   -119.85                                   
REMARK 500    ALA C 124     -152.30     72.01                                   
REMARK 500    ASP C 141       59.90   -105.08                                   
REMARK 500    LEU C 156      -64.46   -104.87                                   
REMARK 500    ASN C 192     -157.80   -127.48                                   
REMARK 500    GLU C 233      135.37    165.25                                   
REMARK 500    LEU C 281      -82.75     72.27                                   
REMARK 500    THR C 323      -73.29   -110.09                                   
REMARK 500    LEU C 354      109.68    -54.03                                   
REMARK 500    HIS C 374        0.23     80.68                                   
REMARK 500    TRP C 381     -134.62    -87.70                                   
REMARK 500    VAL C 394      -61.09   -105.07                                   
REMARK 500    ARG C 395      139.11   -171.68                                   
REMARK 500    PHE C 397      -10.90   -149.68                                   
REMARK 500    VAL C 477      -43.39   -130.16                                   
REMARK 500    PHE D  75     -135.27   -126.74                                   
REMARK 500    ALA D 124     -153.31     68.14                                   
REMARK 500    ASN D 192     -169.91   -115.14                                   
REMARK 500    GLU D 233      135.60    170.05                                   
REMARK 500    ASP D 263      -68.90   -123.31                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      54 RAMACHANDRAN OUTLIERS.                        
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    TRP B 312        24.9      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 498                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 498                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 499                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 498                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 498                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 499                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 499                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 499                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 1591                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 1592                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 508                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 508                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 1593                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 1594                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 1595                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2NSX   RELATED DB: PDB                                   
DBREF  2NT0 A    1   497  UNP    P04062   GLCM_HUMAN      40    536             
DBREF  2NT0 B    1   497  UNP    P04062   GLCM_HUMAN      40    536             
DBREF  2NT0 C    1   497  UNP    P04062   GLCM_HUMAN      40    536             
DBREF  2NT0 D    1   497  UNP    P04062   GLCM_HUMAN      40    536             
SEQADV 2NT0 HIS A  495  UNP  P04062    ARG   534 CONFLICT                       
SEQADV 2NT0 HIS B  495  UNP  P04062    ARG   534 CONFLICT                       
SEQADV 2NT0 HIS C  495  UNP  P04062    ARG   534 CONFLICT                       
SEQADV 2NT0 HIS D  495  UNP  P04062    ARG   534 CONFLICT                       
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 2NT0 ASN A   19  ASN  GLYCOSYLATION SITE                                 
MODRES 2NT0 ASN B   19  ASN  GLYCOSYLATION SITE                                 
MODRES 2NT0 ASN C   19  ASN  GLYCOSYLATION SITE                                 
MODRES 2NT0 ASN D   19  ASN  GLYCOSYLATION SITE                                 
MODRES 2NT0 ASN B  146  ASN  GLYCOSYLATION SITE                                 
MODRES 2NT0 THR D   21  THR  GLYCOSYLATION SITE                                 
HET    NAG  A 498      14                                                       
HET    NAG  B 498      14                                                       
HET    NAG  B 499      14                                                       
HET    NAG  D 498      14                                                       
HET    NAG  C 498      14                                                       
HET    SO4  D 499       5                                                       
HET    SO4  D 500       5                                                       
HET    SO4  B 500       5                                                       
HET    SO4  C 499       5                                                       
HET    SO4  A 499       5                                                       
HET    SO4  B 501       5                                                       
HET    SO4  A 500       5                                                       
HET    SO4  C 500       5                                                       
HET    SO4  A 501       5                                                       
HET    SO4  C 501       5                                                       
HET    SO4  D 501       5                                                       
HET    SO4  A 502       5                                                       
HET    SO4  D 502       5                                                       
HET    SO4  B 502       5                                                       
HET    SO4  B 503       5                                                       
HET    SO4  B 504       5                                                       
HET    SO4  D 503       5                                                       
HET    SO4  B 505       5                                                       
HET    SO4  D 504       5                                                       
HET    SO4  D 505       5                                                       
HET    GOL  C1591       6                                                       
HET    GOL  B 506       6                                                       
HET    GOL  C1592       6                                                       
HET    GOL  D 506       6                                                       
HET    GOL  A 503       6                                                       
HET    GOL  B 507       6                                                       
HET    GOL  D 507       6                                                       
HET    GOL  D 508       6                                                       
HET    GOL  B 508       6                                                       
HET    GOL  A 504       6                                                       
HET    GOL  C1593       6                                                       
HET    GOL  C1594       6                                                       
HET    GOL  C1595       6                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     SO4 SULFATE ION                                                      
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   5  NAG    5(C8 H15 N O6)                                               
FORMUL  10  SO4    20(O4 S 2-)                                                  
FORMUL  30  GOL    13(C3 H8 O3)                                                 
FORMUL  43  HOH   *1710(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 GLU A  235  LEU A  241  5                                   7    
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 PRO A  319  PHE A  331  1                                  13    
HELIX   14  14 SER A  356  TYR A  373  1                                  18    
HELIX   15  15 ILE A  406  ASP A  409  5                                   4    
HELIX   16  16 GLN A  414  LYS A  425  1                                  12    
HELIX   17  17 THR B   86  ALA B   95  1                                  10    
HELIX   18  18 SER B   97  SER B  110  1                                  14    
HELIX   19  19 PRO B  150  LYS B  155  1                                   6    
HELIX   20  20 LEU B  156  ALA B  168  1                                  13    
HELIX   21  21 PRO B  182  LYS B  186  5                                   5    
HELIX   22  22 ASP B  203  HIS B  223  1                                  21    
HELIX   23  23 GLU B  235  LEU B  241  5                                   7    
HELIX   24  24 THR B  252  ASP B  263  1                                  12    
HELIX   25  25 ASP B  263  ASN B  270  1                                   8    
HELIX   26  26 LEU B  286  LEU B  288  5                                   3    
HELIX   27  27 PRO B  289  THR B  297  1                                   9    
HELIX   28  28 ASP B  298  LYS B  303  1                                   6    
HELIX   29  29 PRO B  319  PHE B  331  1                                  13    
HELIX   30  30 SER B  356  TYR B  373  1                                  18    
HELIX   31  31 ILE B  406  ASP B  409  5                                   4    
HELIX   32  32 GLN B  414  LYS B  425  1                                  12    
HELIX   33  33 THR C   86  ALA C   95  1                                  10    
HELIX   34  34 SER C   97  SER C  110  1                                  14    
HELIX   35  35 PRO C  150  LYS C  155  1                                   6    
HELIX   36  36 LEU C  156  ALA C  168  1                                  13    
HELIX   37  37 PRO C  182  LYS C  186  5                                   5    
HELIX   38  38 ASP C  203  HIS C  223  1                                  21    
HELIX   39  39 GLU C  235  LEU C  241  5                                   7    
HELIX   40  40 THR C  252  ASP C  263  1                                  12    
HELIX   41  41 ASP C  263  ASN C  270  1                                   8    
HELIX   42  42 LEU C  286  LEU C  288  5                                   3    
HELIX   43  43 PRO C  289  THR C  297  1                                   9    
HELIX   44  44 ASP C  298  LYS C  303  1                                   6    
HELIX   45  45 PRO C  319  PHE C  331  1                                  13    
HELIX   46  46 SER C  356  TYR C  373  1                                  18    
HELIX   47  47 ILE C  406  ASP C  409  5                                   4    
HELIX   48  48 GLN C  414  LYS C  425  1                                  12    
HELIX   49  49 THR D   86  ALA D   95  1                                  10    
HELIX   50  50 SER D   97  SER D  110  1                                  14    
HELIX   51  51 PRO D  150  LYS D  155  1                                   6    
HELIX   52  52 LEU D  156  ALA D  168  1                                  13    
HELIX   53  53 PRO D  182  LYS D  186  5                                   5    
HELIX   54  54 ASP D  203  HIS D  223  1                                  21    
HELIX   55  55 GLU D  235  LEU D  241  5                                   7    
HELIX   56  56 THR D  252  ASP D  263  1                                  12    
HELIX   57  57 ASP D  263  SER D  271  1                                   9    
HELIX   58  58 LEU D  286  LEU D  288  5                                   3    
HELIX   59  59 PRO D  289  THR D  297  1                                   9    
HELIX   60  60 ASP D  298  LYS D  303  1                                   6    
HELIX   61  61 PRO D  319  PHE D  331  1                                  13    
HELIX   62  62 SER D  356  TYR D  373  1                                  18    
HELIX   63  63 ILE D  406  ASP D  409  5                                   4    
HELIX   64  64 GLN D  414  LYS D  425  1                                  12    
SHEET    1   A 5 PRO A   6  LYS A   7  0                                        
SHEET    2   A 5 VAL A  15  CYS A  18 -1  O  VAL A  15   N  LYS A   7           
SHEET    3   A 5 THR A 410  LYS A 413 -1  O  PHE A 411   N  CYS A  18           
SHEET    4   A 5 ILE A 402  ASP A 405 -1  N  ASP A 405   O  THR A 410           
SHEET    5   A 5 ALA A 384  LEU A 385  1  N  LEU A 385   O  VAL A 404           
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  PHE A  75   O  ARG A 433           
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  LEU A 480   N  ILE A 472           
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  VAL A 121           
SHEET    4   C 9 ALA A 229  THR A 231  1  O  THR A 231   N  ALA A 176           
SHEET    5   C 9 ARG A 277  GLN A 284  1  O  ARG A 277   N  VAL A 230           
SHEET    6   C 9 GLY A 307  TYR A 313  1  O  ALA A 309   N  MET A 280           
SHEET    7   C 9 MET A 335  CYS A 342  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  82   O  ASP A 380           
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  GLU B  41   O  GLU B  50           
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  VAL B 458   O  TYR B 492           
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  VAL B 434   O  ALA B 448           
SHEET    7   E 9 LEU B  65  LYS B  77 -1  N  PHE B  75   O  ARG B 433           
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  CYS C  18 -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  PHE C  37   O  GLY C  54           
SHEET    3   H 9 SER C 488  TRP C 494 -1  O  THR C 491   N  TYR C  40           
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  PHE C  75   O  ARG C 433           
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  THR C 231   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 GLY C 307  TYR C 313  1  O  ALA C 309   N  MET C 280           
SHEET    7   I 9 MET C 335  CYS C 342  1  O  PHE C 337   N  VAL C 310           
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  ASP D 405   O  THR D 410           
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  VAL D 458   O  TYR D 492           
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  GLN D 432   O  MET D 450           
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  THR D 231   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  ALA D 309   N  MET D 280           
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  2.04  
SSBOND   2 CYS A   18    CYS A   23                          1555   1555  2.04  
SSBOND   3 CYS B    4    CYS B   16                          1555   1555  2.04  
SSBOND   4 CYS B   18    CYS B   23                          1555   1555  2.05  
SSBOND   5 CYS C    4    CYS C   16                          1555   1555  2.04  
SSBOND   6 CYS C   18    CYS C   23                          1555   1555  2.04  
SSBOND   7 CYS D    4    CYS D   16                          1555   1555  2.04  
SSBOND   8 CYS D   18    CYS D   23                          1555   1555  2.05  
LINK         ND2 ASN A  19                 C1  NAG A 498     1555   1555  1.45  
LINK         ND2 ASN B  19                 C6  NAG B 498     1555   1555  1.33  
LINK         ND2 ASN C  19                 C1  NAG C 498     1555   1555  2.25  
LINK         ND2 ASN D  19                 C1  NAG D 498     1555   1555  1.46  
LINK         OD1 ASN B 146                 C1  NAG B 499     1555   1555  1.35  
LINK         OD1 ASN B 146                 O5  NAG B 499     1555   1555  1.15  
LINK         OG1 THR D  21                 C8  NAG D 498     1555   1555  1.34  
CISPEP   1 LEU A  288    PRO A  289          0         3.04                     
CISPEP   2 GLY A  390    PRO A  391          0         1.04                     
CISPEP   3 GLY B   62    THR B   63          0       -17.71                     
CISPEP   4 LEU B  288    PRO B  289          0         2.03                     
CISPEP   5 GLY B  390    PRO B  391          0         1.97                     
CISPEP   6 LEU C  288    PRO C  289          0         2.26                     
CISPEP   7 GLY C  390    PRO C  391          0         1.53                     
CISPEP   8 LEU D  288    PRO D  289          0         2.13                     
CISPEP   9 GLY D  390    PRO D  391          0         2.64                     
SITE     1 AC1  6 ILE A   5  ASN A  19  HOH A 546  HOH A 716                    
SITE     2 AC1  6 HOH A 744  HOH A 816                                          
SITE     1 AC2  8 ASN B  19  TYR B  22  HOH B 602  HOH B 617                    
SITE     2 AC2  8 HOH B 720  HOH B 822  HOH B 937  HOH B 964                    
SITE     1 AC3  6 THR B 138  ASN B 146  HOH B 652  HOH B 934                    
SITE     2 AC3  6 SER C  97  PRO C  98                                          
SITE     1 AC4  5 ASN D  19  THR D  21  HOH D 590  HOH D 687                    
SITE     2 AC4  5 HOH D 942                                                     
SITE     1 AC5 11 ILE C   5  ASN C  19  THR C  21  HOH C1611                    
SITE     2 AC5 11 HOH C1895  HOH C1896  HOH C1902  HOH C1934                    
SITE     3 AC5 11 HOH C1968  HOH C1982  HOH C1984                               
SITE     1 AC6 10 SER C 242  TYR D  11  SER D  12  ARG D 353                    
SITE     2 AC6 10 SER D 356  TRP D 357  ASP D 358  HOH D 550                    
SITE     3 AC6 10 HOH D 770  HOH D 830                                          
SITE     1 AC7  7 LYS D  79  TRP D 228  ARG D 277  HIS D 306                    
SITE     2 AC7  7 HOH D 650  HOH D 749  HOH D 876                               
SITE     1 AC8  9 SER A 242  TYR B  11  SER B  12  ARG B 353                    
SITE     2 AC8  9 SER B 356  TRP B 357  ASP B 358  HOH B 848                    
SITE     3 AC8  9 HOH B 899                                                     
SITE     1 AC9  7 TYR C  11  SER C  12  ARG C 353  SER C 356                    
SITE     2 AC9  7 TRP C 357  ASP C 358  HOH C1863                               
SITE     1 BC1  7 TYR A  11  SER A  12  ARG A 353  SER A 356                    
SITE     2 BC1  7 TRP A 357  ASP A 358  HOH A 813                               
SITE     1 BC2  6 LYS B  79  TRP B 228  ARG B 277  HIS B 306                    
SITE     2 BC2  6 HOH B 669  HOH B 755                                          
SITE     1 BC3  5 LYS A  79  TRP A 228  ARG A 277  HIS A 306                    
SITE     2 BC3  5 HOH A 735                                                     
SITE     1 BC4  5 LYS C  79  TRP C 228  ARG C 277  HIS C 306                    
SITE     2 BC4  5 HOH C1782                                                     
SITE     1 BC5  4 ARG A  44  SER A  45  HOH A 643  HOH A 908                    
SITE     1 BC6  3 ARG C  44  SER C  45  HOH C1762                               
SITE     1 BC7  6 PRO D  29  GLU D 111  GLN D 169  ARG D 170                    
SITE     2 BC7  6 HOH D 607  HOH D 790                                          
SITE     1 BC8  2 ARG A  44  TYR A 487                                          
SITE     1 BC9  7 GLY D 193  LYS D 194  SER D 242  GLY D 243                    
SITE     2 BC9  7 HOH D 689  HOH D 727  HOH D 925                               
SITE     1 CC1  4 LYS B 321  ARG B 329  ARG C 329  LEU C 330                    
SITE     1 CC2  4 ARG B  44  SER B 465  TYR B 487  HOH B 941                    
SITE     1 CC3  6 GLY B 193  LYS B 194  SER B 242  GLY B 243                    
SITE     2 CC3  6 HOH B 603  HOH B 655                                          
SITE     1 CC4  3 ARG D  44  SER D  45  HOH D 539                               
SITE     1 CC5  3 ARG B  44  SER B  45  HOH B 597                               
SITE     1 CC6  3 ARG A 329  LYS D 321  ARG D 329                               
SITE     1 CC7  3 ARG D  44  TYR D 487  HOH D 939                               
SITE     1 CC8  4 PHE C  75  HIS C 328  HIS C 374  HOH C1622                    
SITE     1 CC9 11 ASP B 127  PHE B 128  TRP B 179  ASN B 234                    
SITE     2 CC9 11 GLU B 235  PHE B 246  TYR B 313  GLU B 340                    
SITE     3 CC9 11 TRP B 381  ASN B 396  HOH B 868                               
SITE     1 DC1  9 ASP C 127  PHE C 128  TRP C 179  ASN C 234                    
SITE     2 DC1  9 GLU C 235  TYR C 313  GLU C 340  TRP C 381                    
SITE     3 DC1  9 PHE C 397                                                     
SITE     1 DC2 11 ASP D 127  PHE D 128  TRP D 179  ASN D 234                    
SITE     2 DC2 11 GLU D 235  PHE D 246  TYR D 313  GLU D 340                    
SITE     3 DC2 11 TRP D 381  ASN D 396  HOH D 880                               
SITE     1 DC3 10 ASP A 127  PHE A 128  TRP A 179  ASN A 234                    
SITE     2 DC3 10 GLU A 235  TYR A 313  GLU A 340  TRP A 381                    
SITE     3 DC3 10 PHE A 397  HOH A 833                                          
SITE     1 DC4  9 PRO B 391  ASN B 392  ARG B 395  PHE B 397                    
SITE     2 DC4  9 HOH B 577  HOH B 598  VAL C 394  ARG C 395                    
SITE     3 DC4  9 HOH C1742                                                     
SITE     1 DC5  7 ARG D   2  ASP D  24  SER D  25  PHE D  26                    
SITE     2 DC5  7 ARG D  48  GOL D 508  HOH D 583                               
SITE     1 DC6  9 PRO D   3  CYS D   4  ARG D  48  MET D  49                    
SITE     2 DC6  9 GLU D  50  GOL D 507  HOH D 555  HOH D 667                    
SITE     3 DC6  9 HOH D 798                                                     
SITE     1 DC7  7 ASP B  24  SER B  25  PHE B  26  ARG B  48                    
SITE     2 DC7  7 MET B  49  HOH B 574  HOH B 592                               
SITE     1 DC8  9 ASP A  24  SER A  25  PHE A  26  ARG A  48                    
SITE     2 DC8  9 MET A  49  TYR A 418  HOH A 644  HOH A 760                    
SITE     3 DC8  9 HOH A 842                                                     
SITE     1 DC9  8 ARG C   2  ASP C  24  SER C  25  PHE C  26                    
SITE     2 DC9  8 ARG C  48  MET C  49  HOH C1774  HOH C1866                    
SITE     1 EC1  6 PRO C 289  LYS C 293  GOL C1595  HOH C1801                    
SITE     2 EC1  6 HOH C1889  PRO D 319                                          
SITE     1 EC2  3 HIS C 290  LYS C 293  GOL C1594                               
CRYST1  107.941   91.759  152.810  90.00 110.96  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      0.009264  0.000000  0.003549        0.00000                         
SCALE2      0.000000  0.010898  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007008        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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