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Database: PDB
Entry: 5B4X
LinkDB: 5B4X
Original site: 5B4X 
HEADER    SIGNALING PROTEIN/ENDOCYTOSIS           20-APR-16   5B4X              
TITLE     CRYSTAL STRUCTURE OF THE APOER2 ECTODOMAIN IN COMPLEX WITH THE REELIN 
TITLE    2 R56 FRAGMENT                                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: REELIN;                                                    
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 1948-2662;                                    
COMPND   5 SYNONYM: REELER PROTEIN;                                             
COMPND   6 EC: 3.4.21.-;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: LOW DENSITY LIPOPROTEIN RECEPTOR-RELATED PROTEIN 8,        
COMPND  10 APOLIPOPROTEIN E RECEPTOR, ISOFORM CRA_E;                            
COMPND  11 CHAIN: B, D;                                                         
COMPND  12 FRAGMENT: APOER2 ECTODOMAIN (UNP RESIDUES 42-607);                   
COMPND  13 SYNONYM: LRP-8,APOLIPOPROTEIN E RECEPTOR 2;                          
COMPND  14 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: RELN, RL;                                                      
SOURCE   6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: LRP8, HCG_33395;                                               
SOURCE  13 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 10029                                       
KEYWDS    SIGNAL TRANSDUCTION, MEMBRANE PROTEIN, SIGNALING PROTEIN-ENDOCYTOSIS  
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.YASUI,H.HIRAI,K.YAMASHITA,J.TAKAGI,T.NOGI                           
REVDAT   1   26-APR-17 5B4X    0                                                
JRNL        AUTH   H.HIRAI,N.YASUI,K.YAMASHITA,S.TABATA,M.YAMAMOTO,J.TAKAGI,    
JRNL        AUTH 2 T.NOGI                                                       
JRNL        TITL   CRYSTAL STRUCTURE OF THE ECTODOMAIN FROM A LDLR CLOSE        
JRNL        TITL 2 HOMOLOGUE IN COMPLEX WITH ITS PHYSIOLOGICAL LIGAND.          
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0029                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.52                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 63926                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : FREE R-VALUE                    
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.203                           
REMARK   3   R VALUE            (WORKING SET) : 0.200                           
REMARK   3   FREE R VALUE                     : 0.255                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3467                            
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) : 3.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.28                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4736                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.0                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2600                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 261                          
REMARK   3   BIN FREE R VALUE                    : 0.3100                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 18806                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 86                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 99.77                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.07000                                              
REMARK   3    B22 (A**2) : 2.07000                                              
REMARK   3    B33 (A**2) : -6.70000                                             
REMARK   3    B12 (A**2) : 2.07000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.451         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.342         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 20.108        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.928                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.891                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 19507 ; 0.006 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 26425 ; 1.178 ; 1.950       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  2369 ; 6.942 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   945 ;36.446 ;24.159       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  3055 ;16.674 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   120 ;15.215 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2809 ; 0.082 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 15046 ; 0.004 ; 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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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 : NULL                                                 
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 5B4X COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-APR-16.                  
REMARK 100 THE DEPOSITION ID IS D_1300000495.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-OCT-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : BL-5A                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97904                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 67441                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.520                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 14.80                              
REMARK 200  R MERGE                    (I) : 0.13900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.28                     
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: SAD                          
REMARK 200 SOFTWARE USED: AUTOSHARP                                             
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 65.70                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.59                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 11-12.5%(WT./VOL.) PEG 3350 200-250MM    
REMARK 280  SODIUM THIOCYANATE, 20MM HEPES-NA (PH 7.5), VAPOR DIFFUSION,        
REMARK 280  HANGING DROP, TEMPERATURE 293K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/6                                            
REMARK 290       6555   X-Y,X,Z+5/6                                             
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      113.22667            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       56.61333            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       84.92000            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       28.30667            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      141.53333            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3840 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 55860 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -61.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3320 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 56600 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A  1946                                                      
REMARK 465     ARG A  1947                                                      
REMARK 465     ASP A  1948                                                      
REMARK 465     GLY A  1949                                                      
REMARK 465     ASN A  1950                                                      
REMARK 465     ASN A  1951                                                      
REMARK 465     LEU A  1952                                                      
REMARK 465     ASN A  1953                                                      
REMARK 465     SER A  2063                                                      
REMARK 465     SER A  2064                                                      
REMARK 465     LEU A  2065                                                      
REMARK 465     VAL A  2066                                                      
REMARK 465     SER A  2067                                                      
REMARK 465     PHE A  2669                                                      
REMARK 465     GLN A  2670                                                      
REMARK 465     SER B    40                                                      
REMARK 465     GLY B    41                                                      
REMARK 465     PRO B    42                                                      
REMARK 465     ALA B    43                                                      
REMARK 465     LYS B   123                                                      
REMARK 465     GLN B   124                                                      
REMARK 465     VAL B   125                                                      
REMARK 465     CYS B   126                                                      
REMARK 465     PRO B   127                                                      
REMARK 465     ALA B   128                                                      
REMARK 465     GLU B   129                                                      
REMARK 465     LYS B   130                                                      
REMARK 465     LEU B   131                                                      
REMARK 465     SER B   132                                                      
REMARK 465     CYS B   133                                                      
REMARK 465     GLY B   134                                                      
REMARK 465     PRO B   135                                                      
REMARK 465     THR B   136                                                      
REMARK 465     SER B   137                                                      
REMARK 465     HIS B   138                                                      
REMARK 465     LYS B   139                                                      
REMARK 465     CYS B   140                                                      
REMARK 465     VAL B   141                                                      
REMARK 465     PRO B   142                                                      
REMARK 465     ALA B   143                                                      
REMARK 465     SER B   144                                                      
REMARK 465     TRP B   145                                                      
REMARK 465     ARG B   146                                                      
REMARK 465     CYS B   147                                                      
REMARK 465     ASP B   148                                                      
REMARK 465     GLY B   149                                                      
REMARK 465     GLU B   150                                                      
REMARK 465     LYS B   151                                                      
REMARK 465     ASP B   152                                                      
REMARK 465     CYS B   153                                                      
REMARK 465     GLU B   154                                                      
REMARK 465     GLY B   155                                                      
REMARK 465     GLY B   156                                                      
REMARK 465     ALA B   157                                                      
REMARK 465     ASP B   158                                                      
REMARK 465     GLU B   159                                                      
REMARK 465     ALA B   160                                                      
REMARK 465     GLY B   161                                                      
REMARK 465     CYS B   162                                                      
REMARK 465     ALA B   163                                                      
REMARK 465     THR B   164                                                      
REMARK 465     SER B   165                                                      
REMARK 465     LEU B   166                                                      
REMARK 465     GLY B   167                                                      
REMARK 465     THR B   168                                                      
REMARK 465     CYS B   169                                                      
REMARK 465     ARG B   170                                                      
REMARK 465     GLY B   171                                                      
REMARK 465     ASP B   172                                                      
REMARK 465     GLU B   173                                                      
REMARK 465     PHE B   174                                                      
REMARK 465     GLN B   175                                                      
REMARK 465     CYS B   176                                                      
REMARK 465     GLY B   177                                                      
REMARK 465     ASP B   178                                                      
REMARK 465     GLY B   179                                                      
REMARK 465     THR B   180                                                      
REMARK 465     CYS B   181                                                      
REMARK 465     VAL B   182                                                      
REMARK 465     LEU B   183                                                      
REMARK 465     ALA B   184                                                      
REMARK 465     ILE B   185                                                      
REMARK 465     LYS B   186                                                      
REMARK 465     HIS B   187                                                      
REMARK 465     CYS B   188                                                      
REMARK 465     ASN B   189                                                      
REMARK 465     GLN B   190                                                      
REMARK 465     GLU B   191                                                      
REMARK 465     GLN B   192                                                      
REMARK 465     ASP B   193                                                      
REMARK 465     CYS B   194                                                      
REMARK 465     PRO B   195                                                      
REMARK 465     ASP B   196                                                      
REMARK 465     GLY B   197                                                      
REMARK 465     SER B   198                                                      
REMARK 465     ASP B   199                                                      
REMARK 465     GLU B   200                                                      
REMARK 465     ALA B   201                                                      
REMARK 465     GLY B   202                                                      
REMARK 465     CYS B   203                                                      
REMARK 465     LEU B   204                                                      
REMARK 465     GLN B   205                                                      
REMARK 465     GLY B   206                                                      
REMARK 465     LEU B   207                                                      
REMARK 465     SER B   608                                                      
REMARK 465     SER B   609                                                      
REMARK 465     GLY C  1946                                                      
REMARK 465     ARG C  1947                                                      
REMARK 465     ASP C  1948                                                      
REMARK 465     GLY C  1949                                                      
REMARK 465     ASN C  1950                                                      
REMARK 465     ASN C  1951                                                      
REMARK 465     LEU C  1952                                                      
REMARK 465     ASN C  1953                                                      
REMARK 465     ASN C  1954                                                      
REMARK 465     SER C  2063                                                      
REMARK 465     SER C  2064                                                      
REMARK 465     LEU C  2065                                                      
REMARK 465     VAL C  2066                                                      
REMARK 465     SER C  2067                                                      
REMARK 465     PHE C  2669                                                      
REMARK 465     GLN C  2670                                                      
REMARK 465     SER D    40                                                      
REMARK 465     GLY D    41                                                      
REMARK 465     PRO D    42                                                      
REMARK 465     ALA D    43                                                      
REMARK 465     LYS D   123                                                      
REMARK 465     GLN D   124                                                      
REMARK 465     VAL D   125                                                      
REMARK 465     CYS D   126                                                      
REMARK 465     PRO D   127                                                      
REMARK 465     ALA D   128                                                      
REMARK 465     GLU D   129                                                      
REMARK 465     LYS D   130                                                      
REMARK 465     LEU D   131                                                      
REMARK 465     SER D   132                                                      
REMARK 465     CYS D   133                                                      
REMARK 465     GLY D   134                                                      
REMARK 465     PRO D   135                                                      
REMARK 465     THR D   136                                                      
REMARK 465     SER D   137                                                      
REMARK 465     HIS D   138                                                      
REMARK 465     LYS D   139                                                      
REMARK 465     CYS D   140                                                      
REMARK 465     VAL D   141                                                      
REMARK 465     PRO D   142                                                      
REMARK 465     ALA D   143                                                      
REMARK 465     SER D   144                                                      
REMARK 465     TRP D   145                                                      
REMARK 465     ARG D   146                                                      
REMARK 465     CYS D   147                                                      
REMARK 465     ASP D   148                                                      
REMARK 465     GLY D   149                                                      
REMARK 465     GLU D   150                                                      
REMARK 465     LYS D   151                                                      
REMARK 465     ASP D   152                                                      
REMARK 465     CYS D   153                                                      
REMARK 465     GLU D   154                                                      
REMARK 465     GLY D   155                                                      
REMARK 465     GLY D   156                                                      
REMARK 465     ALA D   157                                                      
REMARK 465     ASP D   158                                                      
REMARK 465     GLU D   159                                                      
REMARK 465     ALA D   160                                                      
REMARK 465     GLY D   161                                                      
REMARK 465     CYS D   162                                                      
REMARK 465     ALA D   163                                                      
REMARK 465     THR D   164                                                      
REMARK 465     SER D   165                                                      
REMARK 465     LEU D   166                                                      
REMARK 465     GLY D   167                                                      
REMARK 465     THR D   168                                                      
REMARK 465     CYS D   169                                                      
REMARK 465     ARG D   170                                                      
REMARK 465     GLY D   171                                                      
REMARK 465     ASP D   172                                                      
REMARK 465     GLU D   173                                                      
REMARK 465     PHE D   174                                                      
REMARK 465     GLN D   175                                                      
REMARK 465     CYS D   176                                                      
REMARK 465     GLY D   177                                                      
REMARK 465     ASP D   178                                                      
REMARK 465     GLY D   179                                                      
REMARK 465     THR D   180                                                      
REMARK 465     CYS D   181                                                      
REMARK 465     VAL D   182                                                      
REMARK 465     LEU D   183                                                      
REMARK 465     ALA D   184                                                      
REMARK 465     ILE D   185                                                      
REMARK 465     LYS D   186                                                      
REMARK 465     HIS D   187                                                      
REMARK 465     CYS D   188                                                      
REMARK 465     ASN D   189                                                      
REMARK 465     GLN D   190                                                      
REMARK 465     GLU D   191                                                      
REMARK 465     GLN D   192                                                      
REMARK 465     ASP D   193                                                      
REMARK 465     CYS D   194                                                      
REMARK 465     PRO D   195                                                      
REMARK 465     ASP D   196                                                      
REMARK 465     GLY D   197                                                      
REMARK 465     SER D   198                                                      
REMARK 465     ASP D   199                                                      
REMARK 465     GLU D   200                                                      
REMARK 465     ALA D   201                                                      
REMARK 465     GLY D   202                                                      
REMARK 465     CYS D   203                                                      
REMARK 465     LEU D   204                                                      
REMARK 465     GLN D   205                                                      
REMARK 465     GLY D   206                                                      
REMARK 465     LEU D   207                                                      
REMARK 465     SER D   608                                                      
REMARK 465     SER D   609                                                      
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    TRP D   102     OD2  ASP D   105              1.98            
REMARK 500   O    TRP B   102     OD2  ASP B   105              2.08            
REMARK 500   O    SER A  1995     OD2  ASP A  2125              2.10            
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    PHE A1962       -1.04     65.76                                   
REMARK 500    PHE A1964       65.93   -105.48                                   
REMARK 500    CYS A1983       70.27     42.04                                   
REMARK 500    ALA A1990       79.37   -115.29                                   
REMARK 500    ASN A2017     -158.10   -129.97                                   
REMARK 500    SER A2031     -176.42   -175.57                                   
REMARK 500    ASP A2047       58.20   -115.04                                   
REMARK 500    LEU A2069       31.40    -96.56                                   
REMARK 500    SER A2071     -168.95   -109.22                                   
REMARK 500    CYS A2137       17.13     53.37                                   
REMARK 500    HIS A2140       54.18   -111.86                                   
REMARK 500    ASN A2145       12.58     54.20                                   
REMARK 500    PHE A2174       86.28     91.94                                   
REMARK 500    GLN A2177       68.73   -105.31                                   
REMARK 500    LEU A2178       40.05    -92.84                                   
REMARK 500    SER A2180      140.43    -38.87                                   
REMARK 500    SER A2271       54.65    -95.00                                   
REMARK 500    PHE A2328       30.64     81.95                                   
REMARK 500    HIS A2339       54.97   -161.86                                   
REMARK 500    ILE A2358      -36.21   -135.04                                   
REMARK 500    ALA A2385     -111.75   -101.71                                   
REMARK 500    SER A2388      -11.74     71.04                                   
REMARK 500    ASP A2391       49.20    -83.53                                   
REMARK 500    PHE A2436       42.12   -105.88                                   
REMARK 500    SER A2452     -177.77   -176.73                                   
REMARK 500    CYS A2482     -155.20     58.26                                   
REMARK 500    ASP A2484       11.24     56.21                                   
REMARK 500    CYS A2486       28.73     49.87                                   
REMARK 500    HIS A2489       53.32   -108.98                                   
REMARK 500    CYS A2559      -90.51   -126.82                                   
REMARK 500    LEU A2585      -53.19   -126.94                                   
REMARK 500    PRO A2630      -33.30    -35.34                                   
REMARK 500    ASP A2647       35.03    -89.69                                   
REMARK 500    LEU A2660      116.32   -160.36                                   
REMARK 500    SER A2662      172.77    179.79                                   
REMARK 500    ASN B  55       33.00    -95.61                                   
REMARK 500    LEU B  72      -13.33     88.32                                   
REMARK 500    CYS B  85     -157.77    -86.55                                   
REMARK 500    ALA B  86     -169.40    -75.49                                   
REMARK 500    CYS B  92     -179.88    -66.75                                   
REMARK 500    CYS B 104       50.31     71.09                                   
REMARK 500    ALA B 119       39.65    -94.80                                   
REMARK 500    CYS B 121     -107.71   -106.27                                   
REMARK 500    HIS B 219      -92.90   -124.07                                   
REMARK 500    ASP B 240      -72.56    -71.52                                   
REMARK 500    GLN B 258      -93.87   -114.49                                   
REMARK 500    TYR B 266     -162.83   -160.48                                   
REMARK 500    ARG B 299      -40.48     77.42                                   
REMARK 500    MET B 318       79.63     83.46                                   
REMARK 500    ASN B 321       87.98   -161.12                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     128 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 LYS B  434     ILE B  435                  149.11                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A4001  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A1961   O                                                      
REMARK 620 2 ASP A1963   OD1 100.4                                              
REMARK 620 3 ASP A1963   OD2  84.0  44.7                                        
REMARK 620 4 SER A1995   O    87.3  86.9 127.5                                  
REMARK 620 5 ASP A2125   OD1  85.6 166.5 125.2 105.5                            
REMARK 620 6 ASP A2125   OD2 102.7 132.4 173.4  53.6  56.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A4002  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A2173   O                                                      
REMARK 620 2 ASN A2202   O    67.9                                              
REMARK 620 3 ASP A2310   OD1  82.4  97.6                                        
REMARK 620 4 ASP A2310   OD2 119.2  75.8  55.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A4003  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A2327   O                                                      
REMARK 620 2 THR A2351   O   153.5                                              
REMARK 620 3 ASP A2353   O    80.0 104.5                                        
REMARK 620 4 ASP A2474   OD1  74.8 131.1  64.9                                  
REMARK 620 5 ASP A2474   OD2 129.3  77.1  85.1  55.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A4004  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A2522   O                                                      
REMARK 620 2 SER A2549   O   152.9                                              
REMARK 620 3 LEU A2551   O    89.2  91.5                                        
REMARK 620 4 ASP A2657   OD1  79.1 127.2 100.5                                  
REMARK 620 5 ASP A2657   OD2 115.8  88.1  61.9  55.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B5001  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TRP B  63   O                                                      
REMARK 620 2 ASP B  66   OD1  82.5                                              
REMARK 620 3 ASP B  68   O   161.9 113.9                                        
REMARK 620 4 ASP B  70   OD2 109.5 109.1  73.5                                  
REMARK 620 5 ASP B  76   OD2  91.7 161.4  70.3  89.6                            
REMARK 620 6 GLU B  77   OE2  91.2  83.3  83.6 156.8  79.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B5002  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TRP B 102   O                                                      
REMARK 620 2 ASP B 105   OD2  53.0                                              
REMARK 620 3 GLU B 107   O   144.6  98.0                                        
REMARK 620 4 GLU B 109   OE1  85.7 103.8  82.2                                  
REMARK 620 5 ASP B 115   OD2 117.5 165.1  94.6  85.7                            
REMARK 620 6 GLU B 116   OE2 125.4 100.1  74.3 148.5  75.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B5003  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B 209   OE1                                                    
REMARK 620 2 GLU B 209   OE2  56.1                                              
REMARK 620 3 ASP B 223   OD1 100.9 147.3                                        
REMARK 620 4 ASP B 223   OD2  68.8  91.9  56.1                                  
REMARK 620 5 LEU B 224   O   173.6 126.5  79.0 115.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B5004  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 246   OD1                                                    
REMARK 620 2 ASP B 246   OD2  43.5                                              
REMARK 620 3 ILE B 247   O    73.3  62.8                                        
REMARK 620 4 GLU B 249   OE1 140.5 130.3  73.4                                  
REMARK 620 5 ASN B 262   OD1 117.6  74.6  72.5  70.7                            
REMARK 620 6 TYR B 263   O    80.4  64.1 124.1 136.9  77.9                      
REMARK 620 7 TYR B 266   O   139.6 143.8 145.6  72.4  92.4  80.4                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C4001  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR C1961   O                                                      
REMARK 620 2 ASP C1963   OD1 102.0                                              
REMARK 620 3 SER C1995   O    97.8 115.8                                        
REMARK 620 4 ASP C2125   OD1  96.8 123.8 113.2                                  
REMARK 620 5 ASP C2125   OD2  87.6 170.2  59.9  56.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C4002  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C2173   O                                                      
REMARK 620 2 GLU C2175   OE2  88.6                                              
REMARK 620 3 ASN C2202   O    86.6  94.6                                        
REMARK 620 4 ASP C2310   OD1  71.7 159.5  90.0                                  
REMARK 620 5 ASP C2310   OD2 124.6 144.3  76.7  56.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C4003  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C2327   O                                                      
REMARK 620 2 THR C2351   O   145.3                                              
REMARK 620 3 ASP C2353   O    86.3 104.5                                        
REMARK 620 4 ASP C2474   OD1  77.0 136.5  81.7                                  
REMARK 620 5 ASP C2474   OD2 132.1  81.6  89.5  55.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C4004  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN C2522   O                                                      
REMARK 620 2 SER C2549   O   149.3                                              
REMARK 620 3 LEU C2551   O    92.1  95.5                                        
REMARK 620 4 ASP C2657   OD1  80.0 129.7  88.5                                  
REMARK 620 5 ASP C2657   OD2 132.1  78.5  73.6  54.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D5001  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TRP D  63   O                                                      
REMARK 620 2 ASP D  66   OD1  78.1                                              
REMARK 620 3 ASP D  68   O   164.0 117.0                                        
REMARK 620 4 ASP D  70   OD2 105.9 106.3  75.9                                  
REMARK 620 5 ASP D  76   OD2  92.9 166.0  71.3  86.4                            
REMARK 620 6 GLU D  77   OE2  90.0  83.8  86.8 162.5  85.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D5002  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TRP D 102   O                                                      
REMARK 620 2 ASP D 105   OD2  50.1                                              
REMARK 620 3 GLU D 107   O   121.2  85.1                                        
REMARK 620 4 GLU D 109   OE1  74.6 108.3  90.1                                  
REMARK 620 5 ASP D 115   OD2 114.5 156.9 117.4  78.7                            
REMARK 620 6 GLU D 116   OE2 155.2 108.8  60.7 129.5  80.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D5003  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU D 209   OE1                                                    
REMARK 620 2 GLU D 209   OE2  56.3                                              
REMARK 620 3 ASP D 223   OD1  92.7 145.9                                        
REMARK 620 4 ASP D 223   OD2  83.2 101.7  56.5                                  
REMARK 620 5 LEU D 224   O   151.3 139.4  74.6 109.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D5004  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D 246   OD1                                                    
REMARK 620 2 ASP D 246   OD2  44.2                                              
REMARK 620 3 ILE D 247   O    73.8  61.4                                        
REMARK 620 4 GLU D 249   OE1 141.6 133.7  76.9                                  
REMARK 620 5 GLU D 249   OE2 100.6 122.8  66.4  43.9                            
REMARK 620 6 ASN D 262   OD1 113.3  69.1  76.3  82.7 119.0                      
REMARK 620 7 TYR D 263   O    74.4  67.6 128.6 144.0 159.5  80.6                
REMARK 620 8 TYR D 266   O   145.8 149.3 138.0  61.7  87.0  90.9  86.9          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 4001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 4002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 4003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 4004                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 5001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 5002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 5003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 5004                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 4001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 4002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 4003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 4004                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA D 5001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA D 5002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA D 5003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA D 5004                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 4005        
REMARK 800  bound to ASN A 2317                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 4006        
REMARK 800  bound to ASN A 2569                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 5005        
REMARK 800  bound to ASN B 388                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG C 4005        
REMARK 800  bound to ASN C 2569                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG D 5005        
REMARK 800  bound to ASN D 388                                                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5B4Y   RELATED DB: PDB                                   
DBREF  5B4X A 1948  2662  UNP    Q60841   RELN_MOUSE    1948   2662             
DBREF  5B4X B   41   606  UNP    D3DQ39   D3DQ39_HUMAN    42    607             
DBREF  5B4X C 1948  2662  UNP    Q60841   RELN_MOUSE    1948   2662             
DBREF  5B4X D   41   606  UNP    D3DQ39   D3DQ39_HUMAN    42    607             
SEQADV 5B4X GLY A 1946  UNP  Q60841              EXPRESSION TAG                 
SEQADV 5B4X ARG A 1947  UNP  Q60841              EXPRESSION TAG                 
SEQADV 5B4X ALA A 2101  UNP  Q60841    CYS  2101 ENGINEERED MUTATION            
SEQADV 5B4X ARG A 2663  UNP  Q60841              EXPRESSION TAG                 
SEQADV 5B4X LEU A 2664  UNP  Q60841              EXPRESSION TAG                 
SEQADV 5B4X GLU A 2665  UNP  Q60841              EXPRESSION TAG                 
SEQADV 5B4X ASN A 2666  UNP  Q60841              EXPRESSION TAG                 
SEQADV 5B4X LEU A 2667  UNP  Q60841              EXPRESSION TAG                 
SEQADV 5B4X TYR A 2668  UNP  Q60841              EXPRESSION TAG                 
SEQADV 5B4X PHE A 2669  UNP  Q60841              EXPRESSION TAG                 
SEQADV 5B4X GLN A 2670  UNP  Q60841              EXPRESSION TAG                 
SEQADV 5B4X SER B   40  UNP  D3DQ39              EXPRESSION TAG                 
SEQADV 5B4X ALA B  607  UNP  D3DQ39              EXPRESSION TAG                 
SEQADV 5B4X SER B  608  UNP  D3DQ39              EXPRESSION TAG                 
SEQADV 5B4X SER B  609  UNP  D3DQ39              EXPRESSION TAG                 
SEQADV 5B4X GLY C 1946  UNP  Q60841              EXPRESSION TAG                 
SEQADV 5B4X ARG C 1947  UNP  Q60841              EXPRESSION TAG                 
SEQADV 5B4X ALA C 2101  UNP  Q60841    CYS  2101 ENGINEERED MUTATION            
SEQADV 5B4X ARG C 2663  UNP  Q60841              EXPRESSION TAG                 
SEQADV 5B4X LEU C 2664  UNP  Q60841              EXPRESSION TAG                 
SEQADV 5B4X GLU C 2665  UNP  Q60841              EXPRESSION TAG                 
SEQADV 5B4X ASN C 2666  UNP  Q60841              EXPRESSION TAG                 
SEQADV 5B4X LEU C 2667  UNP  Q60841              EXPRESSION TAG                 
SEQADV 5B4X TYR C 2668  UNP  Q60841              EXPRESSION TAG                 
SEQADV 5B4X PHE C 2669  UNP  Q60841              EXPRESSION TAG                 
SEQADV 5B4X GLN C 2670  UNP  Q60841              EXPRESSION TAG                 
SEQADV 5B4X SER D   40  UNP  D3DQ39              EXPRESSION TAG                 
SEQADV 5B4X ALA D  607  UNP  D3DQ39              EXPRESSION TAG                 
SEQADV 5B4X SER D  608  UNP  D3DQ39              EXPRESSION TAG                 
SEQADV 5B4X SER D  609  UNP  D3DQ39              EXPRESSION TAG                 
SEQRES   1 A  725  GLY ARG ASP GLY ASN ASN LEU ASN ASN PRO VAL LEU LEU          
SEQRES   2 A  725  LEU ASP THR PHE ASP PHE GLY PRO ARG GLU ASP ASN TRP          
SEQRES   3 A  725  PHE PHE TYR PRO GLY GLY ASN ILE GLY LEU TYR CYS PRO          
SEQRES   4 A  725  TYR SER SER LYS GLY ALA PRO GLU GLU ASP SER ALA MSE          
SEQRES   5 A  725  VAL PHE VAL SER ASN GLU VAL GLY GLU HIS SER ILE THR          
SEQRES   6 A  725  THR ARG ASP LEU SER VAL ASN GLU ASN THR ILE ILE GLN          
SEQRES   7 A  725  PHE GLU ILE ASN VAL GLY CYS SER THR ASP SER SER SER          
SEQRES   8 A  725  ALA ASP PRO VAL ARG LEU GLU PHE SER ARG ASP PHE GLY          
SEQRES   9 A  725  ALA THR TRP HIS LEU LEU LEU PRO LEU CYS TYR HIS SER          
SEQRES  10 A  725  SER SER LEU VAL SER SER LEU CYS SER THR GLU HIS HIS          
SEQRES  11 A  725  PRO SER SER THR TYR TYR ALA GLY THR THR GLN GLY TRP          
SEQRES  12 A  725  ARG ARG GLU VAL VAL HIS PHE GLY LYS LEU HIS LEU ALA          
SEQRES  13 A  725  GLY SER VAL ARG PHE ARG TRP TYR GLN GLY PHE TYR PRO          
SEQRES  14 A  725  ALA GLY SER GLN PRO VAL THR TRP ALA ILE ASP ASN VAL          
SEQRES  15 A  725  TYR ILE GLY PRO GLN CYS GLU GLU MSE CYS TYR GLY HIS          
SEQRES  16 A  725  GLY SER CYS ILE ASN GLY THR LYS CYS ILE CYS ASP PRO          
SEQRES  17 A  725  GLY TYR SER GLY PRO THR CYS LYS ILE SER THR LYS ASN          
SEQRES  18 A  725  PRO ASP PHE LEU LYS ASP ASP PHE GLU GLY GLN LEU GLU          
SEQRES  19 A  725  SER ASP ARG PHE LEU LEU MSE SER GLY GLY LYS PRO SER          
SEQRES  20 A  725  ARG LYS CYS GLY ILE LEU SER SER GLY ASN ASN LEU PHE          
SEQRES  21 A  725  PHE ASN GLU ASP GLY LEU ARG MSE LEU VAL THR ARG ASP          
SEQRES  22 A  725  LEU ASP LEU SER HIS ALA ARG PHE VAL GLN PHE PHE MSE          
SEQRES  23 A  725  ARG LEU GLY CYS GLY LYS GLY VAL PRO ASP PRO ARG SER          
SEQRES  24 A  725  GLN PRO VAL LEU LEU GLN TYR SER LEU ASN GLY GLY LEU          
SEQRES  25 A  725  SER TRP SER LEU LEU GLN GLU PHE LEU PHE SER ASN SER          
SEQRES  26 A  725  SER ASN VAL GLY ARG TYR ILE ALA LEU GLU MSE PRO LEU          
SEQRES  27 A  725  LYS ALA ARG SER GLY SER THR ARG LEU ARG TRP TRP GLN          
SEQRES  28 A  725  PRO SER GLU ASN GLY HIS PHE TYR SER PRO TRP VAL ILE          
SEQRES  29 A  725  ASP GLN ILE LEU ILE GLY GLY ASN ILE SER GLY ASN THR          
SEQRES  30 A  725  VAL LEU GLU ASP ASP PHE SER THR LEU ASP SER ARG LYS          
SEQRES  31 A  725  TRP LEU LEU HIS PRO GLY GLY THR LYS MSE PRO VAL CYS          
SEQRES  32 A  725  GLY SER THR GLY ASP ALA LEU VAL PHE ILE GLU LYS ALA          
SEQRES  33 A  725  SER THR ARG TYR VAL VAL THR THR ASP ILE ALA VAL ASN          
SEQRES  34 A  725  GLU ASP SER PHE LEU GLN ILE ASP PHE ALA ALA SER CYS          
SEQRES  35 A  725  SER VAL THR ASP SER CYS TYR ALA ILE GLU LEU GLU TYR          
SEQRES  36 A  725  SER VAL ASP LEU GLY LEU SER TRP HIS PRO LEU VAL ARG          
SEQRES  37 A  725  ASP CYS LEU PRO THR ASN VAL GLU CYS SER ARG TYR HIS          
SEQRES  38 A  725  LEU GLN ARG ILE LEU VAL SER ASP THR PHE ASN LYS TRP          
SEQRES  39 A  725  THR ARG ILE THR LEU PRO LEU PRO SER TYR THR ARG SER          
SEQRES  40 A  725  GLN ALA THR ARG PHE ARG TRP HIS GLN PRO ALA PRO PHE          
SEQRES  41 A  725  ASP LYS GLN GLN THR TRP ALA ILE ASP ASN VAL TYR ILE          
SEQRES  42 A  725  GLY ASP GLY CYS LEU ASP MSE CYS SER GLY HIS GLY ARG          
SEQRES  43 A  725  CYS VAL GLN GLY SER CYS VAL CYS ASP GLU GLN TRP GLY          
SEQRES  44 A  725  GLY LEU TYR CYS ASP GLU PRO GLU THR SER LEU PRO THR          
SEQRES  45 A  725  GLN LEU LYS ASP ASN PHE ASN ARG ALA PRO SER ASN GLN          
SEQRES  46 A  725  ASN TRP LEU THR VAL SER GLY GLY LYS LEU SER THR VAL          
SEQRES  47 A  725  CYS GLY ALA VAL ALA SER GLY LEU ALA LEU HIS PHE SER          
SEQRES  48 A  725  GLY GLY CYS SER ARG LEU LEU VAL THR VAL ASP LEU ASN          
SEQRES  49 A  725  LEU THR ASN ALA GLU PHE ILE GLN PHE TYR PHE MSE TYR          
SEQRES  50 A  725  GLY CYS LEU ILE THR PRO SER ASN ARG ASN GLN GLY VAL          
SEQRES  51 A  725  LEU LEU GLU TYR SER VAL ASN GLY GLY ILE THR TRP ASN          
SEQRES  52 A  725  LEU LEU MSE GLU ILE PHE TYR ASP GLN TYR SER LYS PRO          
SEQRES  53 A  725  GLY PHE VAL ASN ILE LEU LEU PRO PRO ASP ALA LYS GLU          
SEQRES  54 A  725  ILE ALA THR ARG PHE ARG TRP TRP GLN PRO ARG HIS ASP          
SEQRES  55 A  725  GLY LEU ASP GLN ASN ASP TRP ALA ILE ASP ASN VAL LEU          
SEQRES  56 A  725  ILE SER ARG LEU GLU ASN LEU TYR PHE GLN                      
SEQRES   1 B  570  SER GLY PRO ALA LYS GLU CYS GLU LYS ASP GLN PHE GLN          
SEQRES   2 B  570  CYS ARG ASN GLU ARG CYS ILE PRO SER VAL TRP ARG CYS          
SEQRES   3 B  570  ASP GLU ASP ASP ASP CYS LEU ASP HIS SER ASP GLU ASP          
SEQRES   4 B  570  ASP CYS PRO LYS LYS THR CYS ALA ASP SER ASP PHE THR          
SEQRES   5 B  570  CYS ASP ASN GLY HIS CYS ILE HIS GLU ARG TRP LYS CYS          
SEQRES   6 B  570  ASP GLY GLU GLU GLU CYS PRO ASP GLY SER ASP GLU SER          
SEQRES   7 B  570  GLU ALA THR CYS THR LYS GLN VAL CYS PRO ALA GLU LYS          
SEQRES   8 B  570  LEU SER CYS GLY PRO THR SER HIS LYS CYS VAL PRO ALA          
SEQRES   9 B  570  SER TRP ARG CYS ASP GLY GLU LYS ASP CYS GLU GLY GLY          
SEQRES  10 B  570  ALA ASP GLU ALA GLY CYS ALA THR SER LEU GLY THR CYS          
SEQRES  11 B  570  ARG GLY ASP GLU PHE GLN CYS GLY ASP GLY THR CYS VAL          
SEQRES  12 B  570  LEU ALA ILE LYS HIS CYS ASN GLN GLU GLN ASP CYS PRO          
SEQRES  13 B  570  ASP GLY SER ASP GLU ALA GLY CYS LEU GLN GLY LEU ASN          
SEQRES  14 B  570  GLU CYS LEU HIS ASN ASN GLY GLY CYS SER HIS ILE CYS          
SEQRES  15 B  570  THR ASP LEU LYS ILE GLY PHE GLU CYS THR CYS PRO ALA          
SEQRES  16 B  570  GLY PHE GLN LEU LEU ASP GLN LYS THR CYS GLY ASP ILE          
SEQRES  17 B  570  ASP GLU CYS LYS ASP PRO ASP ALA CYS SER GLN ILE CYS          
SEQRES  18 B  570  VAL ASN TYR LYS GLY TYR PHE LYS CYS GLU CYS TYR PRO          
SEQRES  19 B  570  GLY TYR GLU MET ASP LEU LEU THR LYS ASN CYS LYS ALA          
SEQRES  20 B  570  ALA ALA GLY LYS SER PRO SER LEU ILE PHE THR ASN ARG          
SEQRES  21 B  570  HIS GLU VAL ARG ARG ILE ASP LEU VAL LYS ARG ASN TYR          
SEQRES  22 B  570  SER ARG LEU ILE PRO MET LEU LYS ASN VAL VAL ALA LEU          
SEQRES  23 B  570  ASP VAL GLU VAL ALA THR ASN ARG ILE TYR TRP CYS ASP          
SEQRES  24 B  570  LEU SER TYR ARG LYS ILE TYR SER ALA TYR MET ASP LYS          
SEQRES  25 B  570  ALA SER ASP PRO LYS GLU GLN GLU VAL LEU ILE ASP GLU          
SEQRES  26 B  570  GLN LEU HIS SER PRO GLU GLY LEU ALA VAL ASP TRP VAL          
SEQRES  27 B  570  HIS LYS HIS ILE TYR TRP THR ASP SER GLY ASN LYS THR          
SEQRES  28 B  570  ILE SER VAL ALA THR VAL ASP GLY GLY ARG ARG ARG THR          
SEQRES  29 B  570  LEU PHE SER ARG ASN LEU SER GLU PRO ARG ALA ILE ALA          
SEQRES  30 B  570  VAL ASP PRO LEU ARG GLY PHE MET TYR TRP SER ASP TRP          
SEQRES  31 B  570  GLY ASP GLN ALA LYS ILE GLU LYS SER GLY LEU ASN GLY          
SEQRES  32 B  570  VAL ASP ARG GLN THR LEU VAL SER ASP ASN ILE GLU TRP          
SEQRES  33 B  570  PRO ASN GLY ILE THR LEU ASP LEU LEU SER GLN ARG LEU          
SEQRES  34 B  570  TYR TRP VAL ASP SER LYS LEU HIS GLN LEU SER SER ILE          
SEQRES  35 B  570  ASP PHE SER GLY GLY ASN ARG LYS THR LEU ILE SER SER          
SEQRES  36 B  570  THR ASP PHE LEU SER HIS PRO PHE GLY ILE ALA VAL PHE          
SEQRES  37 B  570  GLU ASP LYS VAL PHE TRP THR ASP LEU GLU ASN GLU ALA          
SEQRES  38 B  570  ILE PHE SER ALA ASN ARG LEU ASN GLY LEU GLU ILE SER          
SEQRES  39 B  570  ILE LEU ALA GLU ASN LEU ASN ASN PRO HIS ASP ILE VAL          
SEQRES  40 B  570  ILE PHE HIS GLU LEU LYS GLN PRO ARG ALA PRO ASP ALA          
SEQRES  41 B  570  CYS GLU LEU SER VAL GLN PRO ASN GLY GLY CYS GLU TYR          
SEQRES  42 B  570  LEU CYS LEU PRO ALA PRO GLN ILE SER SER HIS SER PRO          
SEQRES  43 B  570  LYS TYR THR CYS ALA CYS PRO ASP THR MET TRP LEU GLY          
SEQRES  44 B  570  PRO ASP MET LYS ARG CYS TYR ARG ALA SER SER                  
SEQRES   1 C  725  GLY ARG ASP GLY ASN ASN LEU ASN ASN PRO VAL LEU LEU          
SEQRES   2 C  725  LEU ASP THR PHE ASP PHE GLY PRO ARG GLU ASP ASN TRP          
SEQRES   3 C  725  PHE PHE TYR PRO GLY GLY ASN ILE GLY LEU TYR CYS PRO          
SEQRES   4 C  725  TYR SER SER LYS GLY ALA PRO GLU GLU ASP SER ALA MSE          
SEQRES   5 C  725  VAL PHE VAL SER ASN GLU VAL GLY GLU HIS SER ILE THR          
SEQRES   6 C  725  THR ARG ASP LEU SER VAL ASN GLU ASN THR ILE ILE GLN          
SEQRES   7 C  725  PHE GLU ILE ASN VAL GLY CYS SER THR ASP SER SER SER          
SEQRES   8 C  725  ALA ASP PRO VAL ARG LEU GLU PHE SER ARG ASP PHE GLY          
SEQRES   9 C  725  ALA THR TRP HIS LEU LEU LEU PRO LEU CYS TYR HIS SER          
SEQRES  10 C  725  SER SER LEU VAL SER SER LEU CYS SER THR GLU HIS HIS          
SEQRES  11 C  725  PRO SER SER THR TYR TYR ALA GLY THR THR GLN GLY TRP          
SEQRES  12 C  725  ARG ARG GLU VAL VAL HIS PHE GLY LYS LEU HIS LEU ALA          
SEQRES  13 C  725  GLY SER VAL ARG PHE ARG TRP TYR GLN GLY PHE TYR PRO          
SEQRES  14 C  725  ALA GLY SER GLN PRO VAL THR TRP ALA ILE ASP ASN VAL          
SEQRES  15 C  725  TYR ILE GLY PRO GLN CYS GLU GLU MSE CYS TYR GLY HIS          
SEQRES  16 C  725  GLY SER CYS ILE ASN GLY THR LYS CYS ILE CYS ASP PRO          
SEQRES  17 C  725  GLY TYR SER GLY PRO THR CYS LYS ILE SER THR LYS ASN          
SEQRES  18 C  725  PRO ASP PHE LEU LYS ASP ASP PHE GLU GLY GLN LEU GLU          
SEQRES  19 C  725  SER ASP ARG PHE LEU LEU MSE SER GLY GLY LYS PRO SER          
SEQRES  20 C  725  ARG LYS CYS GLY ILE LEU SER SER GLY ASN ASN LEU PHE          
SEQRES  21 C  725  PHE ASN GLU ASP GLY LEU ARG MSE LEU VAL THR ARG ASP          
SEQRES  22 C  725  LEU ASP LEU SER HIS ALA ARG PHE VAL GLN PHE PHE MSE          
SEQRES  23 C  725  ARG LEU GLY CYS GLY LYS GLY VAL PRO ASP PRO ARG SER          
SEQRES  24 C  725  GLN PRO VAL LEU LEU GLN TYR SER LEU ASN GLY GLY LEU          
SEQRES  25 C  725  SER TRP SER LEU LEU GLN GLU PHE LEU PHE SER ASN SER          
SEQRES  26 C  725  SER ASN VAL GLY ARG TYR ILE ALA LEU GLU MSE PRO LEU          
SEQRES  27 C  725  LYS ALA ARG SER GLY SER THR ARG LEU ARG TRP TRP GLN          
SEQRES  28 C  725  PRO SER GLU ASN GLY HIS PHE TYR SER PRO TRP VAL ILE          
SEQRES  29 C  725  ASP GLN ILE LEU ILE GLY GLY ASN ILE SER GLY ASN THR          
SEQRES  30 C  725  VAL LEU GLU ASP ASP PHE SER THR LEU ASP SER ARG LYS          
SEQRES  31 C  725  TRP LEU LEU HIS PRO GLY GLY THR LYS MSE PRO VAL CYS          
SEQRES  32 C  725  GLY SER THR GLY ASP ALA LEU VAL PHE ILE GLU LYS ALA          
SEQRES  33 C  725  SER THR ARG TYR VAL VAL THR THR ASP ILE ALA VAL ASN          
SEQRES  34 C  725  GLU ASP SER PHE LEU GLN ILE ASP PHE ALA ALA SER CYS          
SEQRES  35 C  725  SER VAL THR ASP SER CYS TYR ALA ILE GLU LEU GLU TYR          
SEQRES  36 C  725  SER VAL ASP LEU GLY LEU SER TRP HIS PRO LEU VAL ARG          
SEQRES  37 C  725  ASP CYS LEU PRO THR ASN VAL GLU CYS SER ARG TYR HIS          
SEQRES  38 C  725  LEU GLN ARG ILE LEU VAL SER ASP THR PHE ASN LYS TRP          
SEQRES  39 C  725  THR ARG ILE THR LEU PRO LEU PRO SER TYR THR ARG SER          
SEQRES  40 C  725  GLN ALA THR ARG PHE ARG TRP HIS GLN PRO ALA PRO PHE          
SEQRES  41 C  725  ASP LYS GLN GLN THR TRP ALA ILE ASP ASN VAL TYR ILE          
SEQRES  42 C  725  GLY ASP GLY CYS LEU ASP MSE CYS SER GLY HIS GLY ARG          
SEQRES  43 C  725  CYS VAL GLN GLY SER CYS VAL CYS ASP GLU GLN TRP GLY          
SEQRES  44 C  725  GLY LEU TYR CYS ASP GLU PRO GLU THR SER LEU PRO THR          
SEQRES  45 C  725  GLN LEU LYS ASP ASN PHE ASN ARG ALA PRO SER ASN GLN          
SEQRES  46 C  725  ASN TRP LEU THR VAL SER GLY GLY LYS LEU SER THR VAL          
SEQRES  47 C  725  CYS GLY ALA VAL ALA SER GLY LEU ALA LEU HIS PHE SER          
SEQRES  48 C  725  GLY GLY CYS SER ARG LEU LEU VAL THR VAL ASP LEU ASN          
SEQRES  49 C  725  LEU THR ASN ALA GLU PHE ILE GLN PHE TYR PHE MSE TYR          
SEQRES  50 C  725  GLY CYS LEU ILE THR PRO SER ASN ARG ASN GLN GLY VAL          
SEQRES  51 C  725  LEU LEU GLU TYR SER VAL ASN GLY GLY ILE THR TRP ASN          
SEQRES  52 C  725  LEU LEU MSE GLU ILE PHE TYR ASP GLN TYR SER LYS PRO          
SEQRES  53 C  725  GLY PHE VAL ASN ILE LEU LEU PRO PRO ASP ALA LYS GLU          
SEQRES  54 C  725  ILE ALA THR ARG PHE ARG TRP TRP GLN PRO ARG HIS ASP          
SEQRES  55 C  725  GLY LEU ASP GLN ASN ASP TRP ALA ILE ASP ASN VAL LEU          
SEQRES  56 C  725  ILE SER ARG LEU GLU ASN LEU TYR PHE GLN                      
SEQRES   1 D  570  SER GLY PRO ALA LYS GLU CYS GLU LYS ASP GLN PHE GLN          
SEQRES   2 D  570  CYS ARG ASN GLU ARG CYS ILE PRO SER VAL TRP ARG CYS          
SEQRES   3 D  570  ASP GLU ASP ASP ASP CYS LEU ASP HIS SER ASP GLU ASP          
SEQRES   4 D  570  ASP CYS PRO LYS LYS THR CYS ALA ASP SER ASP PHE THR          
SEQRES   5 D  570  CYS ASP ASN GLY HIS CYS ILE HIS GLU ARG TRP LYS CYS          
SEQRES   6 D  570  ASP GLY GLU GLU GLU CYS PRO ASP GLY SER ASP GLU SER          
SEQRES   7 D  570  GLU ALA THR CYS THR LYS GLN VAL CYS PRO ALA GLU LYS          
SEQRES   8 D  570  LEU SER CYS GLY PRO THR SER HIS LYS CYS VAL PRO ALA          
SEQRES   9 D  570  SER TRP ARG CYS ASP GLY GLU LYS ASP CYS GLU GLY GLY          
SEQRES  10 D  570  ALA ASP GLU ALA GLY CYS ALA THR SER LEU GLY THR CYS          
SEQRES  11 D  570  ARG GLY ASP GLU PHE GLN CYS GLY ASP GLY THR CYS VAL          
SEQRES  12 D  570  LEU ALA ILE LYS HIS CYS ASN GLN GLU GLN ASP CYS PRO          
SEQRES  13 D  570  ASP GLY SER ASP GLU ALA GLY CYS LEU GLN GLY LEU ASN          
SEQRES  14 D  570  GLU CYS LEU HIS ASN ASN GLY GLY CYS SER HIS ILE CYS          
SEQRES  15 D  570  THR ASP LEU LYS ILE GLY PHE GLU CYS THR CYS PRO ALA          
SEQRES  16 D  570  GLY PHE GLN LEU LEU ASP GLN LYS THR CYS GLY ASP ILE          
SEQRES  17 D  570  ASP GLU CYS LYS ASP PRO ASP ALA CYS SER GLN ILE CYS          
SEQRES  18 D  570  VAL ASN TYR LYS GLY TYR PHE LYS CYS GLU CYS TYR PRO          
SEQRES  19 D  570  GLY TYR GLU MET ASP LEU LEU THR LYS ASN CYS LYS ALA          
SEQRES  20 D  570  ALA ALA GLY LYS SER PRO SER LEU ILE PHE THR ASN ARG          
SEQRES  21 D  570  HIS GLU VAL ARG ARG ILE ASP LEU VAL LYS ARG ASN TYR          
SEQRES  22 D  570  SER ARG LEU ILE PRO MET LEU LYS ASN VAL VAL ALA LEU          
SEQRES  23 D  570  ASP VAL GLU VAL ALA THR ASN ARG ILE TYR TRP CYS ASP          
SEQRES  24 D  570  LEU SER TYR ARG LYS ILE TYR SER ALA TYR MET ASP LYS          
SEQRES  25 D  570  ALA SER ASP PRO LYS GLU GLN GLU VAL LEU ILE ASP GLU          
SEQRES  26 D  570  GLN LEU HIS SER PRO GLU GLY LEU ALA VAL ASP TRP VAL          
SEQRES  27 D  570  HIS LYS HIS ILE TYR TRP THR ASP SER GLY ASN LYS THR          
SEQRES  28 D  570  ILE SER VAL ALA THR VAL ASP GLY GLY ARG ARG ARG THR          
SEQRES  29 D  570  LEU PHE SER ARG ASN LEU SER GLU PRO ARG ALA ILE ALA          
SEQRES  30 D  570  VAL ASP PRO LEU ARG GLY PHE MET TYR TRP SER ASP TRP          
SEQRES  31 D  570  GLY ASP GLN ALA LYS ILE GLU LYS SER GLY LEU ASN GLY          
SEQRES  32 D  570  VAL ASP ARG GLN THR LEU VAL SER ASP ASN ILE GLU TRP          
SEQRES  33 D  570  PRO ASN GLY ILE THR LEU ASP LEU LEU SER GLN ARG LEU          
SEQRES  34 D  570  TYR TRP VAL ASP SER LYS LEU HIS GLN LEU SER SER ILE          
SEQRES  35 D  570  ASP PHE SER GLY GLY ASN ARG LYS THR LEU ILE SER SER          
SEQRES  36 D  570  THR ASP PHE LEU SER HIS PRO PHE GLY ILE ALA VAL PHE          
SEQRES  37 D  570  GLU ASP LYS VAL PHE TRP THR ASP LEU GLU ASN GLU ALA          
SEQRES  38 D  570  ILE PHE SER ALA ASN ARG LEU ASN GLY LEU GLU ILE SER          
SEQRES  39 D  570  ILE LEU ALA GLU ASN LEU ASN ASN PRO HIS ASP ILE VAL          
SEQRES  40 D  570  ILE PHE HIS GLU LEU LYS GLN PRO ARG ALA PRO ASP ALA          
SEQRES  41 D  570  CYS GLU LEU SER VAL GLN PRO ASN GLY GLY CYS GLU TYR          
SEQRES  42 D  570  LEU CYS LEU PRO ALA PRO GLN ILE SER SER HIS SER PRO          
SEQRES  43 D  570  LYS TYR THR CYS ALA CYS PRO ASP THR MET TRP LEU GLY          
SEQRES  44 D  570  PRO ASP MET LYS ARG CYS TYR ARG ALA SER SER                  
MODRES 5B4X MSE A 1997  MET  MODIFIED RESIDUE                                   
MODRES 5B4X MSE A 2136  MET  MODIFIED RESIDUE                                   
MODRES 5B4X MSE A 2186  MET  MODIFIED RESIDUE                                   
MODRES 5B4X MSE A 2213  MET  MODIFIED RESIDUE                                   
MODRES 5B4X MSE A 2231  MET  MODIFIED RESIDUE                                   
MODRES 5B4X MSE A 2281  MET  MODIFIED RESIDUE                                   
MODRES 5B4X MSE A 2345  MET  MODIFIED RESIDUE                                   
MODRES 5B4X MSE A 2485  MET  MODIFIED RESIDUE                                   
MODRES 5B4X MSE A 2581  MET  MODIFIED RESIDUE                                   
MODRES 5B4X MSE A 2611  MET  MODIFIED RESIDUE                                   
MODRES 5B4X MSE C 1997  MET  MODIFIED RESIDUE                                   
MODRES 5B4X MSE C 2136  MET  MODIFIED RESIDUE                                   
MODRES 5B4X MSE C 2186  MET  MODIFIED RESIDUE                                   
MODRES 5B4X MSE C 2213  MET  MODIFIED RESIDUE                                   
MODRES 5B4X MSE C 2231  MET  MODIFIED RESIDUE                                   
MODRES 5B4X MSE C 2281  MET  MODIFIED RESIDUE                                   
MODRES 5B4X MSE C 2345  MET  MODIFIED RESIDUE                                   
MODRES 5B4X MSE C 2485  MET  MODIFIED RESIDUE                                   
MODRES 5B4X MSE C 2581  MET  MODIFIED RESIDUE                                   
MODRES 5B4X MSE C 2611  MET  MODIFIED RESIDUE                                   
HET    MSE  A1997       8                                                       
HET    MSE  A2136       8                                                       
HET    MSE  A2186       8                                                       
HET    MSE  A2213       8                                                       
HET    MSE  A2231       8                                                       
HET    MSE  A2281       8                                                       
HET    MSE  A2345       8                                                       
HET    MSE  A2485       8                                                       
HET    MSE  A2581       8                                                       
HET    MSE  A2611       8                                                       
HET    MSE  C1997       8                                                       
HET    MSE  C2136       8                                                       
HET    MSE  C2186       8                                                       
HET    MSE  C2213       8                                                       
HET    MSE  C2231       8                                                       
HET    MSE  C2281       8                                                       
HET    MSE  C2345       8                                                       
HET    MSE  C2485       8                                                       
HET    MSE  C2581       8                                                       
HET    MSE  C2611       8                                                       
HET     CA  A4001       1                                                       
HET     CA  A4002       1                                                       
HET     CA  A4003       1                                                       
HET     CA  A4004       1                                                       
HET    NAG  A4005      14                                                       
HET    NAG  A4006      14                                                       
HET     CA  B5001       1                                                       
HET     CA  B5002       1                                                       
HET     CA  B5003       1                                                       
HET     CA  B5004       1                                                       
HET    NAG  B5005      14                                                       
HET     CA  C4001       1                                                       
HET     CA  C4002       1                                                       
HET     CA  C4003       1                                                       
HET     CA  C4004       1                                                       
HET    NAG  C4005      14                                                       
HET     CA  D5001       1                                                       
HET     CA  D5002       1                                                       
HET     CA  D5003       1                                                       
HET     CA  D5004       1                                                       
HET    NAG  D5005      14                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM      CA CALCIUM ION                                                      
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
FORMUL   1  MSE    20(C5 H11 N O2 SE)                                           
FORMUL   5   CA    16(CA 2+)                                                    
FORMUL   9  NAG    5(C8 H15 N O6)                                               
HELIX    1 AA1 CYS A 2133  GLY A 2139  5                                   7    
HELIX    2 AA2 PRO A 2282  ARG A 2286  5                                   5    
HELIX    3 AA3 PRO A 2447  ARG A 2451  5                                   5    
HELIX    4 AA4 LEU A 2483  GLY A 2488  5                                   6    
HELIX    5 AA5 ASN A 2590  GLY A 2594  5                                   5    
HELIX    6 AA6 PRO A 2629  LYS A 2633  5                                   5    
HELIX    7 AA7 VAL B   62  ARG B   64  5                                   3    
HELIX    8 AA8 HIS B   74  ASP B   78  5                                   5    
HELIX    9 AA9 GLY B  113  SER B  117  5                                   5    
HELIX   10 AB1 LEU B  211  GLY B  215  5                                   5    
HELIX   11 AB2 ASP B  248  ASP B  252  5                                   5    
HELIX   12 AB3 ASP B  350  ALA B  352  5                                   3    
HELIX   13 AB4 ASP B  354  GLN B  358  5                                   5    
HELIX   14 AB5 HIS B  549  GLN B  553  5                                   5    
HELIX   15 AB6 GLN B  565  CYS B  570  5                                   6    
HELIX   16 AB7 CYS C 2133  GLY C 2139  5                                   7    
HELIX   17 AB8 PRO C 2282  ARG C 2286  5                                   5    
HELIX   18 AB9 PRO C 2447  ARG C 2451  5                                   5    
HELIX   19 AC1 LEU C 2483  GLY C 2488  5                                   6    
HELIX   20 AC2 ASN C 2590  GLY C 2594  5                                   5    
HELIX   21 AC3 PRO C 2629  LYS C 2633  5                                   5    
HELIX   22 AC4 VAL D   62  ARG D   64  5                                   3    
HELIX   23 AC5 HIS D   99  LYS D  103  5                                   5    
HELIX   24 AC6 GLY D  113  SER D  117  5                                   5    
HELIX   25 AC7 HIS D  212  CYS D  217  5                                   6    
HELIX   26 AC8 ASP D  354  GLN D  358  5                                   5    
HELIX   27 AC9 HIS D  549  GLN D  553  5                                   5    
HELIX   28 AD1 ASP D  558  SER D  563  1                                   6    
HELIX   29 AD2 GLN D  565  CYS D  570  5                                   6    
SHEET    1 AA1 3 LEU A1959  ASP A1960  0                                        
SHEET    2 AA1 3 TRP A2122  PRO A2131 -1  O  VAL A2127   N  ASP A1960           
SHEET    3 AA1 3 MSE A1997  PHE A1999 -1  N  MSE A1997   O  ILE A2124           
SHEET    1 AA2 4 LEU A1959  ASP A1960  0                                        
SHEET    2 AA2 4 TRP A2122  PRO A2131 -1  O  VAL A2127   N  ASP A1960           
SHEET    3 AA2 4 THR A2020  VAL A2028 -1  N  GLU A2025   O  ASP A2125           
SHEET    4 AA2 4 ARG A2089  HIS A2094 -1  O  GLU A2091   N  PHE A2024           
SHEET    1 AA3 5 TRP A1971  PHE A1973  0                                        
SHEET    2 AA3 5 GLY A2005  THR A2011 -1  O  THR A2010   N  PHE A1973           
SHEET    3 AA3 5 GLY A2102  TYR A2113 -1  O  TYR A2113   N  GLY A2005           
SHEET    4 AA3 5 SER A2035  SER A2045 -1  N  GLU A2043   O  ARG A2107           
SHEET    5 AA3 5 HIS A2053  LEU A2054 -1  O  HIS A2053   N  PHE A2044           
SHEET    1 AA4 4 LEU A2014  VAL A2016  0                                        
SHEET    2 AA4 4 GLY A2102  TYR A2113 -1  O  GLY A2102   N  VAL A2016           
SHEET    3 AA4 4 SER A2035  SER A2045 -1  N  GLU A2043   O  ARG A2107           
SHEET    4 AA4 4 THR A2079  ALA A2082 -1  O  TYR A2080   N  VAL A2040           
SHEET    1 AA5 2 GLY A2141  ILE A2144  0                                        
SHEET    2 AA5 2 LYS A2148  CYS A2151 -1  O  LYS A2148   N  ILE A2144           
SHEET    1 AA6 2 TYR A2155  SER A2156  0                                        
SHEET    2 AA6 2 ILE A2162  SER A2163 -1  O  ILE A2162   N  SER A2156           
SHEET    1 AA7 4 LEU A2170  ASP A2172  0                                        
SHEET    2 AA7 4 TRP A2307  GLY A2315 -1  O  ILE A2314   N  LEU A2170           
SHEET    3 AA7 4 ASN A2203  PHE A2206 -1  N  LEU A2204   O  ILE A2309           
SHEET    4 AA7 4 LYS A2190  SER A2192 -1  N  LYS A2190   O  PHE A2205           
SHEET    1 AA8 4 LEU A2170  ASP A2172  0                                        
SHEET    2 AA8 4 TRP A2307  GLY A2315 -1  O  ILE A2314   N  LEU A2170           
SHEET    3 AA8 4 PHE A2226  ARG A2232 -1  N  GLN A2228   O  LEU A2313           
SHEET    4 AA8 4 ARG A2275  GLU A2280 -1  O  ILE A2277   N  PHE A2229           
SHEET    1 AA9 5 PHE A2183  SER A2187  0                                        
SHEET    2 AA9 5 MSE A2213  THR A2216 -1  O  VAL A2215   N  LEU A2185           
SHEET    3 AA9 5 ARG A2291  TRP A2295 -1  O  LEU A2292   N  THR A2216           
SHEET    4 AA9 5 VAL A2247  SER A2252 -1  N  GLN A2250   O  ARG A2293           
SHEET    5 AA9 5 TRP A2259  PHE A2265 -1  O  LEU A2262   N  LEU A2249           
SHEET    1 AB1 4 VAL A2323  ASP A2326  0                                        
SHEET    2 AB1 4 TRP A2471  GLY A2479 -1  O  ILE A2478   N  LEU A2324           
SHEET    3 AB1 4 ALA A2354  PHE A2357 -1  N  PHE A2357   O  TRP A2471           
SHEET    4 AB1 4 THR A2343  MSE A2345 -1  N  THR A2343   O  VAL A2356           
SHEET    1 AB2 4 VAL A2323  ASP A2326  0                                        
SHEET    2 AB2 4 TRP A2471  GLY A2479 -1  O  ILE A2478   N  LEU A2324           
SHEET    3 AB2 4 PHE A2378  ALA A2384 -1  N  GLN A2380   O  TYR A2477           
SHEET    4 AB2 4 THR A2440  PRO A2445 -1  O  LEU A2444   N  LEU A2379           
SHEET    1 AB3 4 ARG A2364  VAL A2367  0                                        
SHEET    2 AB3 4 SER A2452  GLN A2461 -1  O  GLN A2461   N  ARG A2364           
SHEET    3 AB3 4 ALA A2395  SER A2401 -1  N  GLU A2399   O  ARG A2458           
SHEET    4 AB3 4 HIS A2409  PRO A2410 -1  O  HIS A2409   N  TYR A2400           
SHEET    1 AB4 4 ILE A2371  VAL A2373  0                                        
SHEET    2 AB4 4 SER A2452  GLN A2461 -1  O  THR A2455   N  ILE A2371           
SHEET    3 AB4 4 ALA A2395  SER A2401 -1  N  GLU A2399   O  ARG A2458           
SHEET    4 AB4 4 LEU A2431  VAL A2432 -1  O  LEU A2431   N  ILE A2396           
SHEET    1 AB5 2 GLY A2490  VAL A2493  0                                        
SHEET    2 AB5 2 SER A2496  CYS A2499 -1  O  VAL A2498   N  ARG A2491           
SHEET    1 AB6 2 TRP A2503  GLY A2504  0                                        
SHEET    2 AB6 2 GLU A2510  PRO A2511 -1  O  GLU A2510   N  GLY A2504           
SHEET    1 AB7 4 LEU A2519  ASP A2521  0                                        
SHEET    2 AB7 4 TRP A2654  SER A2662 -1  O  ILE A2661   N  LEU A2519           
SHEET    3 AB7 4 ALA A2552  PHE A2555 -1  N  LEU A2553   O  ILE A2656           
SHEET    4 AB7 4 GLY A2538  SER A2541 -1  N  LYS A2539   O  HIS A2554           
SHEET    1 AB8 4 LEU A2519  ASP A2521  0                                        
SHEET    2 AB8 4 TRP A2654  SER A2662 -1  O  ILE A2661   N  LEU A2519           
SHEET    3 AB8 4 PHE A2575  TYR A2582 -1  N  TYR A2579   O  ASP A2657           
SHEET    4 AB8 4 GLY A2622  LEU A2627 -1  O  ILE A2626   N  ILE A2576           
SHEET    1 AB9 5 THR A2534  SER A2536  0                                        
SHEET    2 AB9 5 LEU A2562  VAL A2564 -1  O  LEU A2562   N  SER A2536           
SHEET    3 AB9 5 ARG A2638  TRP A2642 -1  O  TRP A2641   N  LEU A2563           
SHEET    4 AB9 5 VAL A2595  SER A2600 -1  N  LEU A2596   O  TRP A2642           
SHEET    5 AB9 5 TRP A2607  ILE A2613 -1  O  MSE A2611   N  LEU A2597           
SHEET    1 AC1 2 GLN B  50  GLN B  52  0                                        
SHEET    2 AC1 2 CYS B  58  PRO B  60 -1  O  ILE B  59   N  PHE B  51           
SHEET    1 AC2 2 ASP B  89  THR B  91  0                                        
SHEET    2 AC2 2 CYS B  97  HIS B  99 -1  O  ILE B  98   N  PHE B  90           
SHEET    1 AC3 2 ILE B 220  THR B 222  0                                        
SHEET    2 AC3 2 GLU B 229  THR B 231 -1  O  GLU B 229   N  THR B 222           
SHEET    1 AC4 2 LEU B 238  LEU B 239  0                                        
SHEET    2 AC4 2 CYS B 244  GLY B 245 -1  O  GLY B 245   N  LEU B 238           
SHEET    1 AC5 2 ILE B 259  TYR B 263  0                                        
SHEET    2 AC5 2 TYR B 266  GLU B 270 -1  O  LYS B 268   N  VAL B 261           
SHEET    1 AC6 2 TYR B 275  MET B 277  0                                        
SHEET    2 AC6 2 CYS B 284  ALA B 286 -1  O  LYS B 285   N  GLU B 276           
SHEET    1 AC7 7 GLU B 359  ILE B 362  0                                        
SHEET    2 AC7 7 LYS B 343  TYR B 348 -1  N  ILE B 344   O  LEU B 361           
SHEET    3 AC7 7 ARG B 333  ASP B 338 -1  N  ILE B 334   O  ALA B 347           
SHEET    4 AC7 7 TYR B 312  GLU B 328 -1  N  ASP B 326   O  TYR B 335           
SHEET    5 AC7 7 ARG B 299  ASP B 306 -1  N  ARG B 304   O  SER B 313           
SHEET    6 AC7 7 SER B 293  THR B 297 -1  N  LEU B 294   O  ILE B 305           
SHEET    7 AC7 7 ILE B 545  PHE B 548 -1  O  VAL B 546   N  ILE B 295           
SHEET    1 AC8 4 GLY B 371  ASP B 375  0                                        
SHEET    2 AC8 4 HIS B 380  ASP B 385 -1  O  HIS B 380   N  ASP B 375           
SHEET    3 AC8 4 THR B 390  THR B 395 -1  O  SER B 392   N  TRP B 383           
SHEET    4 AC8 4 ARG B 401  PHE B 405 -1  O  LEU B 404   N  ILE B 391           
SHEET    1 AC9 4 PRO B 412  ASP B 418  0                                        
SHEET    2 AC9 4 PHE B 423  ASP B 428 -1  O  TYR B 425   N  ALA B 416           
SHEET    3 AC9 4 LYS B 434  GLY B 439 -1  O  SER B 438   N  MET B 424           
SHEET    4 AC9 4 GLN B 446  VAL B 449 -1  O  GLN B 446   N  LYS B 437           
SHEET    1 AD1 4 THR B 460  ASP B 462  0                                        
SHEET    2 AD1 4 ARG B 467  ASP B 472 -1  O  ARG B 467   N  ASP B 462           
SHEET    3 AD1 4 GLN B 477  ASP B 482 -1  O  ILE B 481   N  LEU B 468           
SHEET    4 AD1 4 LYS B 489  ILE B 492 -1  O  ILE B 492   N  LEU B 478           
SHEET    1 AD2 4 PRO B 501  PHE B 507  0                                        
SHEET    2 AD2 4 LYS B 510  ASP B 515 -1  O  PHE B 512   N  ALA B 505           
SHEET    3 AD2 4 ALA B 520  ASN B 525 -1  O  ALA B 524   N  VAL B 511           
SHEET    4 AD2 4 SER B 533  ALA B 536 -1  O  ALA B 536   N  ILE B 521           
SHEET    1 AD3 2 LEU B 573  PRO B 576  0                                        
SHEET    2 AD3 2 TYR B 587  ALA B 590 -1  O  THR B 588   N  LEU B 575           
SHEET    1 AD4 2 TRP B 596  LEU B 597  0                                        
SHEET    2 AD4 2 CYS B 604  TYR B 605 -1  O  TYR B 605   N  TRP B 596           
SHEET    1 AD5 5 TRP C1971  PHE C1973  0                                        
SHEET    2 AD5 5 GLY C2005  THR C2011 -1  O  THR C2010   N  PHE C1972           
SHEET    3 AD5 5 GLY C2102  TYR C2113 -1  O  TYR C2113   N  GLY C2005           
SHEET    4 AD5 5 SER C2035  SER C2045 -1  N  ARG C2041   O  TYR C2109           
SHEET    5 AD5 5 HIS C2053  LEU C2054 -1  O  HIS C2053   N  PHE C2044           
SHEET    1 AD6 4 LEU C2014  VAL C2016  0                                        
SHEET    2 AD6 4 GLY C2102  TYR C2113 -1  O  GLY C2102   N  VAL C2016           
SHEET    3 AD6 4 SER C2035  SER C2045 -1  N  ARG C2041   O  TYR C2109           
SHEET    4 AD6 4 THR C2079  ALA C2082 -1  O  TYR C2080   N  VAL C2040           
SHEET    1 AD7 5 ASN C1978  GLY C1980  0                                        
SHEET    2 AD7 5 ALA C1996  PHE C1999 -1  O  ALA C1996   N  GLY C1980           
SHEET    3 AD7 5 TRP C2122  PRO C2131 -1  O  TRP C2122   N  PHE C1999           
SHEET    4 AD7 5 THR C2020  ILE C2026 -1  N  GLU C2025   O  ASP C2125           
SHEET    5 AD7 5 ARG C2089  GLU C2091 -1  O  GLU C2091   N  PHE C2024           
SHEET    1 AD8 2 GLY C2141  ILE C2144  0                                        
SHEET    2 AD8 2 LYS C2148  CYS C2151 -1  O  LYS C2148   N  ILE C2144           
SHEET    1 AD9 4 LEU C2170  ASP C2172  0                                        
SHEET    2 AD9 4 TRP C2307  GLY C2315 -1  O  ILE C2314   N  LEU C2170           
SHEET    3 AD9 4 ASN C2203  PHE C2206 -1  N  LEU C2204   O  ILE C2309           
SHEET    4 AD9 4 LYS C2190  SER C2192 -1  N  LYS C2190   O  PHE C2205           
SHEET    1 AE1 4 LEU C2170  ASP C2172  0                                        
SHEET    2 AE1 4 TRP C2307  GLY C2315 -1  O  ILE C2314   N  LEU C2170           
SHEET    3 AE1 4 PHE C2226  LEU C2233 -1  N  PHE C2230   O  ASP C2310           
SHEET    4 AE1 4 ARG C2275  GLU C2280 -1  O  ILE C2277   N  PHE C2229           
SHEET    1 AE2 5 LEU C2185  SER C2187  0                                        
SHEET    2 AE2 5 MSE C2213  VAL C2215 -1  O  VAL C2215   N  LEU C2185           
SHEET    3 AE2 5 ARG C2291  TRP C2295 -1  O  TRP C2294   N  LEU C2214           
SHEET    4 AE2 5 VAL C2247  SER C2252 -1  N  LEU C2248   O  TRP C2295           
SHEET    5 AE2 5 TRP C2259  PHE C2265 -1  O  PHE C2265   N  VAL C2247           
SHEET    1 AE3 4 LEU C2324  ASP C2326  0                                        
SHEET    2 AE3 4 TRP C2471  GLY C2479 -1  O  ILE C2478   N  LEU C2324           
SHEET    3 AE3 4 ALA C2354  PHE C2357 -1  N  PHE C2357   O  TRP C2471           
SHEET    4 AE3 4 GLY C2342  MSE C2345 -1  N  THR C2343   O  VAL C2356           
SHEET    1 AE4 4 LEU C2324  ASP C2326  0                                        
SHEET    2 AE4 4 TRP C2471  GLY C2479 -1  O  ILE C2478   N  LEU C2324           
SHEET    3 AE4 4 PHE C2378  ALA C2384 -1  N  GLN C2380   O  TYR C2477           
SHEET    4 AE4 4 THR C2440  PRO C2445 -1  O  THR C2440   N  PHE C2383           
SHEET    1 AE5 5 TRP C2336  LEU C2338  0                                        
SHEET    2 AE5 5 TYR C2365  THR C2368 -1  O  VAL C2367   N  LEU C2338           
SHEET    3 AE5 5 ARG C2456  HIS C2460 -1  O  PHE C2457   N  THR C2368           
SHEET    4 AE5 5 ALA C2395  SER C2401 -1  N  GLU C2397   O  HIS C2460           
SHEET    5 AE5 5 HIS C2409  PRO C2410 -1  O  HIS C2409   N  TYR C2400           
SHEET    1 AE6 5 TRP C2336  LEU C2338  0                                        
SHEET    2 AE6 5 TYR C2365  THR C2368 -1  O  VAL C2367   N  LEU C2338           
SHEET    3 AE6 5 ARG C2456  HIS C2460 -1  O  PHE C2457   N  THR C2368           
SHEET    4 AE6 5 ALA C2395  SER C2401 -1  N  GLU C2397   O  HIS C2460           
SHEET    5 AE6 5 LEU C2431  VAL C2432 -1  O  LEU C2431   N  ILE C2396           
SHEET    1 AE7 2 GLY C2490  VAL C2493  0                                        
SHEET    2 AE7 2 SER C2496  CYS C2499 -1  O  VAL C2498   N  ARG C2491           
SHEET    1 AE8 2 TRP C2503  GLY C2504  0                                        
SHEET    2 AE8 2 GLU C2510  PRO C2511 -1  O  GLU C2510   N  GLY C2504           
SHEET    1 AE9 4 LEU C2519  ASP C2521  0                                        
SHEET    2 AE9 4 TRP C2654  SER C2662 -1  O  ILE C2661   N  LEU C2519           
SHEET    3 AE9 4 ALA C2552  PHE C2555 -1  N  PHE C2555   O  TRP C2654           
SHEET    4 AE9 4 GLY C2538  SER C2541 -1  N  LYS C2539   O  HIS C2554           
SHEET    1 AF1 4 LEU C2519  ASP C2521  0                                        
SHEET    2 AF1 4 TRP C2654  SER C2662 -1  O  ILE C2661   N  LEU C2519           
SHEET    3 AF1 4 PHE C2575  TYR C2582 -1  N  TYR C2579   O  ASP C2657           
SHEET    4 AF1 4 GLY C2622  LEU C2627 -1  O  ILE C2626   N  ILE C2576           
SHEET    1 AF2 5 TRP C2532  SER C2536  0                                        
SHEET    2 AF2 5 LEU C2562  THR C2565 -1  O  LEU C2562   N  SER C2536           
SHEET    3 AF2 5 ARG C2638  TRP C2642 -1  O  PHE C2639   N  THR C2565           
SHEET    4 AF2 5 VAL C2595  SER C2600 -1  N  SER C2600   O  ARG C2638           
SHEET    5 AF2 5 TRP C2607  ILE C2613 -1  O  MSE C2611   N  LEU C2597           
SHEET    1 AF3 2 GLN D  50  GLN D  52  0                                        
SHEET    2 AF3 2 CYS D  58  PRO D  60 -1  O  ILE D  59   N  PHE D  51           
SHEET    1 AF4 2 PHE D  90  THR D  91  0                                        
SHEET    2 AF4 2 CYS D  97  ILE D  98 -1  O  ILE D  98   N  PHE D  90           
SHEET    1 AF5 2 ILE D 220  THR D 222  0                                        
SHEET    2 AF5 2 GLU D 229  THR D 231 -1  O  THR D 231   N  ILE D 220           
SHEET    1 AF6 2 LEU D 238  LEU D 239  0                                        
SHEET    2 AF6 2 CYS D 244  GLY D 245 -1  O  GLY D 245   N  LEU D 238           
SHEET    1 AF7 2 ILE D 259  ASN D 262  0                                        
SHEET    2 AF7 2 PHE D 267  GLU D 270 -1  O  LYS D 268   N  VAL D 261           
SHEET    1 AF8 2 TYR D 275  GLU D 276  0                                        
SHEET    2 AF8 2 LYS D 285  ALA D 286 -1  O  LYS D 285   N  GLU D 276           
SHEET    1 AF9 4 ASN D 311  ILE D 316  0                                        
SHEET    2 AF9 4 VAL D 302  ASP D 306 -1  N  VAL D 302   O  ILE D 316           
SHEET    3 AF9 4 SER D 293  THR D 297 -1  N  PHE D 296   O  ARG D 303           
SHEET    4 AF9 4 ILE D 545  PHE D 548 -1  O  VAL D 546   N  ILE D 295           
SHEET    1 AG1 4 VAL D 322  GLU D 328  0                                        
SHEET    2 AG1 4 ARG D 333  ASP D 338 -1  O  TYR D 335   N  ASP D 326           
SHEET    3 AG1 4 LYS D 343  TYR D 348 -1  O  TYR D 345   N  TRP D 336           
SHEET    4 AG1 4 GLU D 359  ILE D 362 -1  O  LEU D 361   N  ILE D 344           
SHEET    1 AG2 4 GLY D 371  ASP D 375  0                                        
SHEET    2 AG2 4 HIS D 380  ASP D 385 -1  O  TYR D 382   N  ALA D 373           
SHEET    3 AG2 4 THR D 390  THR D 395 -1  O  SER D 392   N  TRP D 383           
SHEET    4 AG2 4 ARG D 401  PHE D 405 -1  O  ARG D 402   N  VAL D 393           
SHEET    1 AG3 4 PRO D 412  ASP D 418  0                                        
SHEET    2 AG3 4 PHE D 423  ASP D 428 -1  O  PHE D 423   N  ASP D 418           
SHEET    3 AG3 4 LYS D 434  GLY D 439 -1  O  SER D 438   N  MET D 424           
SHEET    4 AG3 4 GLN D 446  VAL D 449 -1  O  LEU D 448   N  ILE D 435           
SHEET    1 AG4 4 PRO D 456  ASP D 462  0                                        
SHEET    2 AG4 4 ARG D 467  ASP D 472 -1  O  TYR D 469   N  THR D 460           
SHEET    3 AG4 4 GLN D 477  ASP D 482 -1  O  ILE D 481   N  LEU D 468           
SHEET    4 AG4 4 LYS D 489  ILE D 492 -1  O  LYS D 489   N  SER D 480           
SHEET    1 AG5 4 PRO D 501  PHE D 507  0                                        
SHEET    2 AG5 4 LYS D 510  ASP D 515 -1  O  PHE D 512   N  ALA D 505           
SHEET    3 AG5 4 ALA D 520  ASN D 525 -1  O  ALA D 524   N  VAL D 511           
SHEET    4 AG5 4 SER D 533  ALA D 536 -1  O  SER D 533   N  SER D 523           
SHEET    1 AG6 2 LEU D 573  PRO D 576  0                                        
SHEET    2 AG6 2 TYR D 587  ALA D 590 -1  O  THR D 588   N  LEU D 575           
SHEET    1 AG7 2 TRP D 596  LEU D 597  0                                        
SHEET    2 AG7 2 CYS D 604  TYR D 605 -1  O  TYR D 605   N  TRP D 596           
SSBOND   1 CYS A 1983    CYS A 2030                          1555   1555  2.04  
SSBOND   2 CYS A 2059    CYS A 2070                          1555   1555  2.04  
SSBOND   3 CYS A 2133    CYS A 2143                          1555   1555  2.04  
SSBOND   4 CYS A 2137    CYS A 2149                          1555   1555  2.04  
SSBOND   5 CYS A 2151    CYS A 2160                          1555   1555  2.04  
SSBOND   6 CYS A 2195    CYS A 2235                          1555   1555  2.03  
SSBOND   7 CYS A 2348    CYS A 2387                          1555   1555  2.04  
SSBOND   8 CYS A 2393    CYS A 2559                          1555   1555  2.05  
SSBOND   9 CYS A 2415    CYS A 2422                          1555   1555  2.05  
SSBOND  10 CYS A 2482    CYS A 2492                          1555   1555  2.05  
SSBOND  11 CYS A 2486    CYS A 2497                          1555   1555  2.06  
SSBOND  12 CYS A 2499    CYS A 2508                          1555   1555  2.07  
SSBOND  13 CYS A 2544    CYS A 2584                          1555   1555  2.04  
SSBOND  14 CYS B   46    CYS B   58                          1555   1555  2.05  
SSBOND  15 CYS B   53    CYS B   71                          1555   1555  2.04  
SSBOND  16 CYS B   65    CYS B   80                          1555   1555  2.03  
SSBOND  17 CYS B   85    CYS B   97                          1555   1555  2.03  
SSBOND  18 CYS B   92    CYS B  110                          1555   1555  2.04  
SSBOND  19 CYS B  104    CYS B  121                          1555   1555  2.04  
SSBOND  20 CYS B  210    CYS B  221                          1555   1555  2.03  
SSBOND  21 CYS B  217    CYS B  230                          1555   1555  2.03  
SSBOND  22 CYS B  232    CYS B  244                          1555   1555  2.04  
SSBOND  23 CYS B  250    CYS B  260                          1555   1555  2.05  
SSBOND  24 CYS B  256    CYS B  269                          1555   1555  2.04  
SSBOND  25 CYS B  271    CYS B  284                          1555   1555  2.06  
SSBOND  26 CYS B  560    CYS B  574                          1555   1555  2.06  
SSBOND  27 CYS B  570    CYS B  589                          1555   1555  2.03  
SSBOND  28 CYS B  591    CYS B  604                          1555   1555  2.06  
SSBOND  29 CYS C 1983    CYS C 2030                          1555   1555  2.03  
SSBOND  30 CYS C 2059    CYS C 2070                          1555   1555  2.02  
SSBOND  31 CYS C 2133    CYS C 2143                          1555   1555  2.03  
SSBOND  32 CYS C 2137    CYS C 2149                          1555   1555  2.03  
SSBOND  33 CYS C 2151    CYS C 2160                          1555   1555  2.04  
SSBOND  34 CYS C 2195    CYS C 2235                          1555   1555  2.03  
SSBOND  35 CYS C 2348    CYS C 2387                          1555   1555  2.04  
SSBOND  36 CYS C 2393    CYS C 2559                          1555   1555  2.05  
SSBOND  37 CYS C 2415    CYS C 2422                          1555   1555  2.02  
SSBOND  38 CYS C 2482    CYS C 2492                          1555   1555  2.06  
SSBOND  39 CYS C 2486    CYS C 2497                          1555   1555  2.05  
SSBOND  40 CYS C 2499    CYS C 2508                          1555   1555  2.07  
SSBOND  41 CYS C 2544    CYS C 2584                          1555   1555  2.04  
SSBOND  42 CYS D   46    CYS D   58                          1555   1555  2.04  
SSBOND  43 CYS D   53    CYS D   71                          1555   1555  2.03  
SSBOND  44 CYS D   65    CYS D   80                          1555   1555  2.04  
SSBOND  45 CYS D   85    CYS D   97                          1555   1555  2.03  
SSBOND  46 CYS D   92    CYS D  110                          1555   1555  2.04  
SSBOND  47 CYS D  104    CYS D  121                          1555   1555  2.04  
SSBOND  48 CYS D  210    CYS D  221                          1555   1555  2.04  
SSBOND  49 CYS D  217    CYS D  230                          1555   1555  2.03  
SSBOND  50 CYS D  232    CYS D  244                          1555   1555  2.03  
SSBOND  51 CYS D  250    CYS D  260                          1555   1555  2.05  
SSBOND  52 CYS D  256    CYS D  269                          1555   1555  2.04  
SSBOND  53 CYS D  271    CYS D  284                          1555   1555  2.05  
SSBOND  54 CYS D  560    CYS D  574                          1555   1555  2.05  
SSBOND  55 CYS D  570    CYS D  589                          1555   1555  2.02  
SSBOND  56 CYS D  591    CYS D  604                          1555   1555  2.06  
LINK         O   THR A1961                CA    CA A4001     1555   1555  2.32  
LINK         OD1 ASP A1963                CA    CA A4001     1555   1555  2.32  
LINK         OD2 ASP A1963                CA    CA A4001     1555   1555  3.12  
LINK         O   SER A1995                CA    CA A4001     1555   1555  2.33  
LINK         C   ALA A1996                 N   MSE A1997     1555   1555  1.34  
LINK         C   MSE A1997                 N   VAL A1998     1555   1555  1.33  
LINK         OD1 ASP A2125                CA    CA A4001     1555   1555  2.33  
LINK         OD2 ASP A2125                CA    CA A4001     1555   1555  2.32  
LINK         C   GLU A2135                 N   MSE A2136     1555   1555  1.34  
LINK         C   MSE A2136                 N   CYS A2137     1555   1555  1.34  
LINK         O   ASP A2173                CA    CA A4002     1555   1555  2.34  
LINK         C   LEU A2185                 N   MSE A2186     1555   1555  1.33  
LINK         C   MSE A2186                 N   SER A2187     1555   1555  1.33  
LINK         O   ASN A2202                CA    CA A4002     1555   1555  2.32  
LINK         C   ARG A2212                 N   MSE A2213     1555   1555  1.33  
LINK         C   MSE A2213                 N   LEU A2214     1555   1555  1.33  
LINK         C   PHE A2230                 N   MSE A2231     1555   1555  1.33  
LINK         C   MSE A2231                 N   ARG A2232     1555   1555  1.33  
LINK         C   GLU A2280                 N   MSE A2281     1555   1555  1.34  
LINK         C   MSE A2281                 N   PRO A2282     1555   1555  1.35  
LINK         OD1 ASP A2310                CA    CA A4002     1555   1555  2.32  
LINK         OD2 ASP A2310                CA    CA A4002     1555   1555  2.33  
LINK         ND2 ASN A2317                 C1  NAG A4005     1555   1555  1.45  
LINK         O   ASP A2327                CA    CA A4003     1555   1555  2.34  
LINK         C   LYS A2344                 N   MSE A2345     1555   1555  1.33  
LINK         C   MSE A2345                 N   PRO A2346     1555   1555  1.35  
LINK         O   THR A2351                CA    CA A4003     1555   1555  2.34  
LINK         O   ASP A2353                CA    CA A4003     1555   1555  2.33  
LINK         OD1 ASP A2474                CA    CA A4003     1555   1555  2.34  
LINK         OD2 ASP A2474                CA    CA A4003     1555   1555  2.34  
LINK         C   ASP A2484                 N   MSE A2485     1555   1555  1.34  
LINK         C   MSE A2485                 N   CYS A2486     1555   1555  1.33  
LINK         O   ASN A2522                CA    CA A4004     1555   1555  2.34  
LINK         O   SER A2549                CA    CA A4004     1555   1555  2.32  
LINK         O   LEU A2551                CA    CA A4004     1555   1555  2.33  
LINK         ND2 ASN A2569                 C1  NAG A4006     1555   1555  1.45  
LINK         C   PHE A2580                 N   MSE A2581     1555   1555  1.33  
LINK         C   MSE A2581                 N   TYR A2582     1555   1555  1.33  
LINK         C   LEU A2610                 N   MSE A2611     1555   1555  1.33  
LINK         C   MSE A2611                 N   GLU A2612     1555   1555  1.34  
LINK         OD1 ASP A2657                CA    CA A4004     1555   1555  2.34  
LINK         OD2 ASP A2657                CA    CA A4004     1555   1555  2.33  
LINK         O   TRP B  63                CA    CA B5001     1555   1555  2.31  
LINK         OD1 ASP B  66                CA    CA B5001     1555   1555  2.32  
LINK         O   ASP B  68                CA    CA B5001     1555   1555  2.30  
LINK         OD2 ASP B  70                CA    CA B5001     1555   1555  2.31  
LINK         OD2 ASP B  76                CA    CA B5001     1555   1555  2.33  
LINK         OE2 GLU B  77                CA    CA B5001     1555   1555  2.32  
LINK         O   TRP B 102                CA    CA B5002     1555   1555  2.32  
LINK         OD2 ASP B 105                CA    CA B5002     1555   1555  2.33  
LINK         O   GLU B 107                CA    CA B5002     1555   1555  2.32  
LINK         OE1 GLU B 109                CA    CA B5002     1555   1555  2.33  
LINK         OD2 ASP B 115                CA    CA B5002     1555   1555  2.33  
LINK         OE2 GLU B 116                CA    CA B5002     1555   1555  2.33  
LINK         OE1 GLU B 209                CA    CA B5003     1555   1555  2.32  
LINK         OE2 GLU B 209                CA    CA B5003     1555   1555  2.33  
LINK         OD1 ASP B 223                CA    CA B5003     1555   1555  2.33  
LINK         OD2 ASP B 223                CA    CA B5003     1555   1555  2.32  
LINK         O   LEU B 224                CA    CA B5003     1555   1555  2.33  
LINK         OD1 ASP B 246                CA    CA B5004     1555   1555  2.32  
LINK         OD2 ASP B 246                CA    CA B5004     1555   1555  3.18  
LINK         O   ILE B 247                CA    CA B5004     1555   1555  2.33  
LINK         OE1 GLU B 249                CA    CA B5004     1555   1555  2.32  
LINK         OD1 ASN B 262                CA    CA B5004     1555   1555  2.33  
LINK         O   TYR B 263                CA    CA B5004     1555   1555  2.33  
LINK         O   TYR B 266                CA    CA B5004     1555   1555  2.34  
LINK         ND2 ASN B 388                 C1  NAG B5005     1555   1555  1.46  
LINK         O   THR C1961                CA    CA C4001     1555   1555  2.32  
LINK         OD1 ASP C1963                CA    CA C4001     1555   1555  2.32  
LINK         O   SER C1995                CA    CA C4001     1555   1555  2.33  
LINK         C   ALA C1996                 N   MSE C1997     1555   1555  1.34  
LINK         C   MSE C1997                 N   VAL C1998     1555   1555  1.33  
LINK         OD1 ASP C2125                CA    CA C4001     1555   1555  2.33  
LINK         OD2 ASP C2125                CA    CA C4001     1555   1555  2.32  
LINK         C   GLU C2135                 N   MSE C2136     1555   1555  1.34  
LINK         C   MSE C2136                 N   CYS C2137     1555   1555  1.33  
LINK         O   ASP C2173                CA    CA C4002     1555   1555  2.33  
LINK         OE2 GLU C2175                CA    CA C4002     1555   1555  2.32  
LINK         C   LEU C2185                 N   MSE C2186     1555   1555  1.33  
LINK         C   MSE C2186                 N   SER C2187     1555   1555  1.33  
LINK         O   ASN C2202                CA    CA C4002     1555   1555  2.32  
LINK         C   ARG C2212                 N   MSE C2213     1555   1555  1.33  
LINK         C   MSE C2213                 N   LEU C2214     1555   1555  1.33  
LINK         C   PHE C2230                 N   MSE C2231     1555   1555  1.33  
LINK         C   MSE C2231                 N   ARG C2232     1555   1555  1.33  
LINK         C   GLU C2280                 N   MSE C2281     1555   1555  1.33  
LINK         C   MSE C2281                 N   PRO C2282     1555   1555  1.36  
LINK         OD1 ASP C2310                CA    CA C4002     1555   1555  2.32  
LINK         OD2 ASP C2310                CA    CA C4002     1555   1555  2.33  
LINK         O   ASP C2327                CA    CA C4003     1555   1555  2.33  
LINK         C   LYS C2344                 N   MSE C2345     1555   1555  1.33  
LINK         C   MSE C2345                 N   PRO C2346     1555   1555  1.35  
LINK         O   THR C2351                CA    CA C4003     1555   1555  2.34  
LINK         O   ASP C2353                CA    CA C4003     1555   1555  2.33  
LINK         OD1 ASP C2474                CA    CA C4003     1555   1555  2.35  
LINK         OD2 ASP C2474                CA    CA C4003     1555   1555  2.33  
LINK         C   ASP C2484                 N   MSE C2485     1555   1555  1.33  
LINK         C   MSE C2485                 N   CYS C2486     1555   1555  1.33  
LINK         O   ASN C2522                CA    CA C4004     1555   1555  2.35  
LINK         O   SER C2549                CA    CA C4004     1555   1555  2.33  
LINK         O   LEU C2551                CA    CA C4004     1555   1555  2.33  
LINK         ND2 ASN C2569                 C1  NAG C4005     1555   1555  1.45  
LINK         C   PHE C2580                 N   MSE C2581     1555   1555  1.33  
LINK         C   MSE C2581                 N   TYR C2582     1555   1555  1.34  
LINK         C   LEU C2610                 N   MSE C2611     1555   1555  1.33  
LINK         C   MSE C2611                 N   GLU C2612     1555   1555  1.33  
LINK         OD1 ASP C2657                CA    CA C4004     1555   1555  2.35  
LINK         OD2 ASP C2657                CA    CA C4004     1555   1555  2.34  
LINK         O   TRP D  63                CA    CA D5001     1555   1555  2.32  
LINK         OD1 ASP D  66                CA    CA D5001     1555   1555  2.32  
LINK         O   ASP D  68                CA    CA D5001     1555   1555  2.32  
LINK         OD2 ASP D  70                CA    CA D5001     1555   1555  2.31  
LINK         OD2 ASP D  76                CA    CA D5001     1555   1555  2.32  
LINK         OE2 GLU D  77                CA    CA D5001     1555   1555  2.32  
LINK         O   TRP D 102                CA    CA D5002     1555   1555  2.34  
LINK         OD2 ASP D 105                CA    CA D5002     1555   1555  2.32  
LINK         O   GLU D 107                CA    CA D5002     1555   1555  2.33  
LINK         OE1 GLU D 109                CA    CA D5002     1555   1555  2.33  
LINK         OD2 ASP D 115                CA    CA D5002     1555   1555  2.33  
LINK         OE2 GLU D 116                CA    CA D5002     1555   1555  2.34  
LINK         OE1 GLU D 209                CA    CA D5003     1555   1555  2.32  
LINK         OE2 GLU D 209                CA    CA D5003     1555   1555  2.32  
LINK         OD1 ASP D 223                CA    CA D5003     1555   1555  2.32  
LINK         OD2 ASP D 223                CA    CA D5003     1555   1555  2.32  
LINK         O   LEU D 224                CA    CA D5003     1555   1555  2.33  
LINK         OD1 ASP D 246                CA    CA D5004     1555   1555  2.33  
LINK         OD2 ASP D 246                CA    CA D5004     1555   1555  3.14  
LINK         O   ILE D 247                CA    CA D5004     1555   1555  2.41  
LINK         OE1 GLU D 249                CA    CA D5004     1555   1555  2.33  
LINK         OE2 GLU D 249                CA    CA D5004     1555   1555  3.15  
LINK         OD1 ASN D 262                CA    CA D5004     1555   1555  2.33  
LINK         O   TYR D 263                CA    CA D5004     1555   1555  2.33  
LINK         O   TYR D 266                CA    CA D5004     1555   1555  2.33  
LINK         ND2 ASN D 388                 C1  NAG D5005     1555   1555  1.47  
CISPEP   1 ALA A 2463    PRO A 2464          0        -1.18                     
CISPEP   2 ALA C 2463    PRO C 2464          0        -4.24                     
SITE     1 AC1  5 THR A1961  ASP A1963  ASP A1994  SER A1995                    
SITE     2 AC1  5 ASP A2125                                                     
SITE     1 AC2  3 ASP A2173  ASN A2202  ASP A2310                               
SITE     1 AC3  5 ASP A2327  THR A2351  ASP A2353  ASP A2474                    
SITE     2 AC3  5 ASN A2475                                                     
SITE     1 AC4  4 ASN A2522  SER A2549  LEU A2551  ASP A2657                    
SITE     1 AC5  6 TRP B  63  ASP B  66  ASP B  68  ASP B  70                    
SITE     2 AC5  6 ASP B  76  GLU B  77                                          
SITE     1 AC6  6 TRP B 102  ASP B 105  GLU B 107  GLU B 109                    
SITE     2 AC6  6 ASP B 115  GLU B 116                                          
SITE     1 AC7  3 GLU B 209  ASP B 223  LEU B 224                               
SITE     1 AC8  7 ASP B 246  ILE B 247  GLU B 249  ASN B 262                    
SITE     2 AC8  7 TYR B 263  GLY B 265  TYR B 266                               
SITE     1 AC9  5 THR C1961  ASP C1963  ASP C1994  SER C1995                    
SITE     2 AC9  5 ASP C2125                                                     
SITE     1 AD1  4 ASP C2173  GLU C2175  ASN C2202  ASP C2310                    
SITE     1 AD2  4 ASP C2327  THR C2351  ASP C2353  ASP C2474                    
SITE     1 AD3  4 ASN C2522  SER C2549  LEU C2551  ASP C2657                    
SITE     1 AD4  6 TRP D  63  ASP D  66  ASP D  68  ASP D  70                    
SITE     2 AD4  6 ASP D  76  GLU D  77                                          
SITE     1 AD5  6 TRP D 102  ASP D 105  GLU D 107  GLU D 109                    
SITE     2 AD5  6 ASP D 115  GLU D 116                                          
SITE     1 AD6  3 GLU D 209  ASP D 223  LEU D 224                               
SITE     1 AD7  6 ASP D 246  ILE D 247  GLU D 249  ASN D 262                    
SITE     2 AD7  6 TYR D 263  TYR D 266                                          
SITE     1 AD8  4 ASP A2168  HIS A2223  ASN A2317  SER A2319                    
SITE     1 AD9  5 PRO A2511  LEU A2515  ASN A2569  THR A2571                    
SITE     2 AD9  5 ASN A2572                                                     
SITE     1 AE1  3 GLN B 365  HIS B 367  ASN B 388                               
SITE     1 AE2  3 PRO C2511  LEU C2515  ASN C2569                               
SITE     1 AE3  3 GLN D 365  HIS D 367  ASN D 388                               
CRYST1  205.951  205.951  169.840  90.00  90.00 120.00 P 65         12          
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      0.004856  0.002803  0.000000        0.00000                         
SCALE2      0.000000  0.005607  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005888        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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