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Database: PDB
Entry: 2RHP
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Original site: 2RHP 
HEADER    CELL ADHESION                           09-OCT-07   2RHP              
TITLE     THE THROMBOSPONDIN-1 POLYMORPHISM ASN700SER ASSOCIATED WITH CORNOARY  
TITLE    2 ARTERY DISEASE CAUSES LOCAL AND LONG-RANGING CHANGES IN PROTEIN      
TITLE    3 STRUCTURE                                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: THROMBOSPONDIN-2;                                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: SIGNATURE DOMAIN;                                          
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 GENE: THBS2, TSP2;                                                   
SOURCE   5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: HIGH 5;                                    
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PCOCO                                     
KEYWDS    EXTRACELLULAR MATRIX, CALCIUM-BINDING, GLYCOSYLATED, JELLY-ROLL, EGF- 
KEYWDS   2 LIKE, LECTIN-LIKE, CELL ADHESION, EGF-LIKE DOMAIN, GLYCOPROTEIN,     
KEYWDS   3 HEPARIN-BINDING                                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.B.CARLSON,J.L.KECK,D.F.MOSHER                                       
REVDAT   6   11-OCT-17 2RHP    1       REMARK                                   
REVDAT   5   13-JUL-11 2RHP    1       VERSN                                    
REVDAT   4   24-FEB-09 2RHP    1       VERSN                                    
REVDAT   3   22-JUL-08 2RHP    1       JRNL                                     
REVDAT   2   15-JUL-08 2RHP    1       LINK                                     
REVDAT   1   27-MAY-08 2RHP    0                                                
JRNL        AUTH   C.B.CARLSON,Y.LIU,J.L.KECK,D.F.MOSHER                        
JRNL        TITL   INFLUENCES OF THE N700S THROMBOSPONDIN-1 POLYMORPHISM ON     
JRNL        TITL 2 PROTEIN STRUCTURE AND STABILITY.                             
JRNL        REF    J.BIOL.CHEM.                  V. 283 20069 2008              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   18499674                                                     
JRNL        DOI    10.1074/JBC.M800223200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.24                                        
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 18868                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.229                           
REMARK   3   R VALUE            (WORKING SET) : 0.227                           
REMARK   3   FREE R VALUE                     : 0.277                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1019                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.98                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1415                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.73                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3010                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 77                           
REMARK   3   BIN FREE R VALUE                    : 0.3560                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4850                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 86                                      
REMARK   3   SOLVENT ATOMS            : 71                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 38.02                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -3.41000                                             
REMARK   3    B22 (A**2) : -1.59000                                             
REMARK   3    B33 (A**2) : 4.99000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.424         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.311         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 15.943        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.906                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.848                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5051 ; 0.006 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6899 ; 1.052 ; 1.942       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   621 ; 6.127 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   295 ;32.959 ;25.763       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   724 ;16.361 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    24 ;14.541 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   703 ; 0.078 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4118 ; 0.002 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2649 ; 0.260 ; 0.300       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  3402 ; 0.330 ; 0.500       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   369 ; 0.203 ; 0.500       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):    94 ; 0.186 ; 0.500       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    50 ; 0.283 ; 0.300       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     4 ; 0.230 ; 0.500       
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):  3120 ; 0.627 ; 2.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4984 ; 1.098 ; 3.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2114 ; 0.498 ; 2.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1915 ; 0.760 ; 3.000       
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 : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 2RHP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-OCT-07.                  
REMARK 100 THE DEPOSITION ID IS D_1000044871.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-NOV-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : BRUKER AXS MICROSTAR               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54                               
REMARK 200  MONOCHROMATOR                  : YALE MIRRORS                       
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : BRUKER SMART 2000                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK, HKL-2000                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 19888                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 80.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : 6.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.13700                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.80                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.37200                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1YO8                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.89                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.23                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG [4000], 0.2M SODIUM ACETATE,     
REMARK 280  0.1M TRIS, PH 8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE       
REMARK 280  298K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       46.94600            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       61.32500            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       77.69050            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       46.94600            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       61.32500            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       77.69050            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       46.94600            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       61.32500            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       77.69050            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       46.94600            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       61.32500            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       77.69050            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A 555       31.39    -93.25                                   
REMARK 500    ASN A 556       75.55     17.78                                   
REMARK 500    PHE A 559      133.11    -29.59                                   
REMARK 500    PHE A 576      162.38    -45.73                                   
REMARK 500    PRO A 578      101.15    -59.32                                   
REMARK 500    VAL A 579      107.30    -27.50                                   
REMARK 500    LEU A 582      -80.26    -60.67                                   
REMARK 500    CYS A 594      -88.34    -66.68                                   
REMARK 500    LEU A 596        8.47     57.19                                   
REMARK 500    VAL A 597     -102.95   -120.82                                   
REMARK 500    PRO A 598     -131.85    -97.74                                   
REMARK 500    ASP A 599       43.22   -166.10                                   
REMARK 500    THR A 604       30.08    -82.57                                   
REMARK 500    SER A 605        0.87     81.70                                   
REMARK 500    LYS A 606     -141.33    -96.74                                   
REMARK 500    VAL A 607      -42.45   -139.81                                   
REMARK 500    ARG A 625       -4.88     82.70                                   
REMARK 500    GLU A 642      113.31     70.53                                   
REMARK 500    ASN A 650       79.98   -169.46                                   
REMARK 500    VAL A 706        3.69    -53.20                                   
REMARK 500    HIS A 714       10.77     46.05                                   
REMARK 500    ASN A 725       76.29   -152.96                                   
REMARK 500    GLN A 728       19.58     59.55                                   
REMARK 500    ASN A 761       80.69   -165.63                                   
REMARK 500    TYR A 767      -93.75    -47.25                                   
REMARK 500    LYS A 769       44.44    -89.58                                   
REMARK 500    ASN A 784       70.58   -168.35                                   
REMARK 500    CYS A 799       49.77    -94.00                                   
REMARK 500    ASP A 802       86.61   -151.86                                   
REMARK 500    ASP A 807      -37.26     80.11                                   
REMARK 500    CYS A 815       61.51   -153.14                                   
REMARK 500    CYS A 838       57.20   -162.33                                   
REMARK 500    ASN A 843       75.00    175.14                                   
REMARK 500    ASP A 856      -39.65    -39.57                                   
REMARK 500    ASN A 861       -0.32     58.92                                   
REMARK 500    SER A 880      115.69    -37.27                                   
REMARK 500    ASN A 881       89.03   -156.09                                   
REMARK 500    GLN A 884       17.93     55.71                                   
REMARK 500    ASP A 908        4.00    -63.98                                   
REMARK 500    ASN A 917       85.59   -165.05                                   
REMARK 500    LEU A 923       24.33    -73.09                                   
REMARK 500    CYS A 932       52.25   -100.59                                   
REMARK 500    ASN A 940       -8.49     69.71                                   
REMARK 500    SER A 955      -25.45   -141.46                                   
REMARK 500    ASP A 968       74.10   -153.23                                   
REMARK 500    LYS A 970     -128.08   -155.33                                   
REMARK 500    THR A 973       -5.58     67.60                                   
REMARK 500    ASN A1017       48.13    -77.71                                   
REMARK 500    ASP A1021      174.50     87.20                                   
REMARK 500    ASP A1022       39.35   -154.39                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      55 RAMACHANDRAN OUTLIERS.                        
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 A  30  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 590   OD1                                                    
REMARK 620 2 LEU A 591   O    66.9                                              
REMARK 620 3 GLU A 593   OE1 120.7  64.1                                        
REMARK 620 4 ASN A 612   OD1 127.0  76.1  69.0                                  
REMARK 620 5 THR A 613   O    80.7 138.9 156.5 107.1                            
REMARK 620 6 GLY A 616   O   140.2 136.8  72.9  92.6  84.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A  28  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 694   OD1                                                    
REMARK 620 2 ASP A 696   OD1  78.5                                              
REMARK 620 3 ASP A 698   OD1  79.4  76.9                                        
REMARK 620 4 TRP A 700   O    72.1 148.4  86.5                                  
REMARK 620 5 ASP A 718   OD2 169.6  98.4  90.2 108.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A  29  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 696   OD2                                                    
REMARK 620 2 ASP A 698   OD2  77.5                                              
REMARK 620 3 ASP A 718   OD1 125.5 101.0                                        
REMARK 620 4 ASP A 718   OD2  79.1  77.1  48.8                                  
REMARK 620 5 CYS A 720   O    90.2 161.5  74.9  87.1                            
REMARK 620 6 LEU A 723   O    81.0 106.1 145.9 158.6  85.2                      
REMARK 620 7 ASN A 725   OD1 149.6  89.5  83.6 125.0 107.7  76.4                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A  25  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 730   OD1                                                    
REMARK 620 2 ASP A 732   OD1  81.9                                              
REMARK 620 3 ASP A 734   OD1  93.8  65.9                                        
REMARK 620 4 ILE A 736   O    75.5 131.1  73.0                                  
REMARK 620 5 ASP A 741   OD2 161.8 112.4  82.7  86.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A  26  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 732   OD2                                                    
REMARK 620 2 ASP A 734   OD2  78.0                                              
REMARK 620 3 ASP A 741   OD1 128.2 128.9                                        
REMARK 620 4 ASP A 741   OD2  90.7  95.4  49.4                                  
REMARK 620 5 ASP A 743   O    85.2 161.7  67.9  92.0                            
REMARK 620 6 ASN A 746   OD1  85.4  82.8 134.3 176.0  88.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A  27  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 738   O                                                      
REMARK 620 2 ASP A 741   O    95.9                                              
REMARK 620 3 ASP A 744   OD1  76.4  72.5                                        
REMARK 620 4 ASP A 744   OD2  95.2 118.1  51.8                                  
REMARK 620 5 ASP A 751   OD2 145.6  70.7  69.4  66.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A  24  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 743   OD1                                                    
REMARK 620 2 ASP A 745   OD1  71.5                                              
REMARK 620 3 ASP A 747   OD1  77.0  72.6                                        
REMARK 620 4 VAL A 749   O    76.0 141.7  80.8                                  
REMARK 620 5 ASP A 754   OD2 158.3 108.7  82.4  94.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A  23  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 745   OD2                                                    
REMARK 620 2 ASP A 747   OD2  73.2                                              
REMARK 620 3 ASP A 754   OD1 122.7 107.3                                        
REMARK 620 4 ASP A 754   OD2  76.6  76.1  50.2                                  
REMARK 620 5 CYS A 756   O    81.1 154.2  84.9  96.5                            
REMARK 620 6 LEU A 759   O    69.2  97.1 154.9 145.6  74.9                      
REMARK 620 7 ASN A 761   OD1 149.6  95.4  87.5 129.0 107.9  84.8                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A  22  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 766   OD1                                                    
REMARK 620 2 ASP A 768   OD1 106.4                                              
REMARK 620 3 ASP A 770   OD1 101.0  70.3                                        
REMARK 620 4 VAL A 772   O    88.0 164.3 101.2                                  
REMARK 620 5 ASP A 777   OD2 154.6  89.1 103.2  79.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A  21  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 770   OD2                                                    
REMARK 620 2 ASP A 777   OD1 109.0                                              
REMARK 620 3 ASP A 777   OD2  93.1  46.7                                        
REMARK 620 4 CYS A 779   O   168.7  61.9  85.0                                  
REMARK 620 5 VAL A 782   O   107.1 138.4 148.9  79.4                            
REMARK 620 6 ASN A 784   OD1  78.1  83.7 123.7  93.7  84.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A  16  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 789   OD1                                                    
REMARK 620 2 ASP A 791   OD1  84.3                                              
REMARK 620 3 ASN A 793   OD1  96.9  89.9                                        
REMARK 620 4 GLU A 795   O    73.1 155.7  84.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A  20  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 802   OD1                                                    
REMARK 620 2 ASP A 804   OD1  77.5                                              
REMARK 620 3 ASP A 806   OD1  85.4  84.3                                        
REMARK 620 4 VAL A 808   O    86.8 163.3  88.9                                  
REMARK 620 5 ASP A 813   OD2 167.5  91.0  98.2 105.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A  19  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 804   OD2                                                    
REMARK 620 2 ASP A 806   OD2  85.5                                              
REMARK 620 3 ASP A 813   OD1 132.1 100.0                                        
REMARK 620 4 ASP A 813   OD2  83.5  85.8  50.1                                  
REMARK 620 5 CYS A 815   O    85.2 168.7  81.6  86.8                            
REMARK 620 6 VAL A 818   O    75.2 121.5 133.6 143.1  62.0                      
REMARK 620 7 ASN A 820   OD1 142.6 100.1  83.6 133.5  91.2  70.4                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A  18  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 825   OD1                                                    
REMARK 620 2 ASP A 827   OD1  88.5                                              
REMARK 620 3 ASP A 829   OD1  89.5  91.1                                        
REMARK 620 4 VAL A 831   O    76.3 156.9  71.8                                  
REMARK 620 5 ASP A 836   OD2 173.5  97.7  92.1  98.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A  17  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 827   OD2                                                    
REMARK 620 2 ASP A 836   OD1 141.5                                              
REMARK 620 3 ASP A 836   OD2  98.0  50.7                                        
REMARK 620 4 CYS A 838   O    78.9  74.6  80.6                                  
REMARK 620 5 VAL A 841   O    65.9 121.3 140.6  61.6                            
REMARK 620 6 ASN A 843   OD1 126.4  82.6 133.0  92.6  63.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A  12  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 848   OD1                                                    
REMARK 620 2 ASP A 850   OD1  84.6                                              
REMARK 620 3 ASP A 852   OD1  97.4  95.2                                        
REMARK 620 4 VAL A 854   O    93.5 172.2  92.6                                  
REMARK 620 5 ASP A 859   OD2 172.2  93.3  90.2  87.6                            
REMARK 620 6 HOH A1229   O    84.9  85.8 177.5  86.5  87.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A  11  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 850   OD2                                                    
REMARK 620 2 ASP A 852   OD2  82.5                                              
REMARK 620 3 ASP A 859   OD1 120.1 114.2                                        
REMARK 620 4 ASP A 859   OD2  88.5  69.8  52.4                                  
REMARK 620 5 ASN A 861   OD1  90.3 170.9  74.2 115.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A  10  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 863   OD1                                                    
REMARK 620 2 ASP A 865   OD1  84.3                                              
REMARK 620 3 ASP A 867   OD1  87.1  85.9                                        
REMARK 620 4 HIS A 869   O    79.3 163.2  89.4                                  
REMARK 620 5 ASP A 874   OD2 171.6  90.3  86.2 105.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A   9  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 865   OD2                                                    
REMARK 620 2 ASP A 867   OD2  79.6                                              
REMARK 620 3 ASP A 874   OD1 146.1  95.9                                        
REMARK 620 4 ASP A 874   OD2  98.5  77.4  48.3                                  
REMARK 620 5 CYS A 876   O    93.3 162.3  80.8  87.7                            
REMARK 620 6 ILE A 879   O    76.4 113.2 134.2 166.6  80.4                      
REMARK 620 7 ASN A 881   OD1 144.9  86.0  66.8 109.5 108.3  80.2                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A   7  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 886   OD1                                                    
REMARK 620 2 ASP A 888   OD1  82.3                                              
REMARK 620 3 ASP A 890   OD1  90.8  80.4                                        
REMARK 620 4 GLN A 892   O    81.6 161.5  90.7                                  
REMARK 620 5 ASP A 897   OD2 161.5 115.2  97.4  81.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A1176  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 888   OD2                                                    
REMARK 620 2 ASP A 890   OD2  63.3                                              
REMARK 620 3 ASP A 897   OD1 118.4 134.4                                        
REMARK 620 4 ASP A 897   OD2  86.3  89.2  48.0                                  
REMARK 620 5 ASP A 899   O    68.8 132.1  71.0  88.5                            
REMARK 620 6 ASN A 902   OD1  76.1  83.4 142.1 162.4  84.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A   8  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 894   O                                                      
REMARK 620 2 ASP A 897   O    86.4                                              
REMARK 620 3 ASP A 900   OD1  82.9  81.4                                        
REMARK 620 4 ASP A 900   OD2 106.1 124.7  48.7                                  
REMARK 620 5 ASP A 907   OD2 168.7  84.3  89.4  74.5                            
REMARK 620 6 HOH A1219   O    78.8  81.9 155.9 152.8 106.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A1174  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 899   OD1                                                    
REMARK 620 2 ASP A 901   OD1  84.9                                              
REMARK 620 3 ASP A 903   OD1  84.7  80.7                                        
REMARK 620 4 VAL A 905   O    74.0 150.3  76.9                                  
REMARK 620 5 ASP A 910   OD2 158.9 113.8  88.7  85.1                            
REMARK 620 6 HOH A1204   O    98.3  97.8 176.5 105.5  89.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A1175  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 901   OD2                                                    
REMARK 620 2 ASP A 903   OD2  68.5                                              
REMARK 620 3 ASP A 910   OD1 130.6 107.2                                        
REMARK 620 4 ASP A 910   OD2  90.8  68.3  47.4                                  
REMARK 620 5 CYS A 912   O    80.1 143.1  78.6  94.0                            
REMARK 620 6 VAL A 915   O    70.2 109.4 142.9 159.5  75.8                      
REMARK 620 7 ASN A 917   OD1 144.3 102.6  85.0 118.9 114.3  81.6                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A   3  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 922   OD1                                                    
REMARK 620 2 ASP A 924   OD1  73.9                                              
REMARK 620 3 ASP A 926   OD1  60.0  76.5                                        
REMARK 620 4 ARG A 928   O    75.3 147.7  80.0                                  
REMARK 620 5 ASP A 930   OD1  83.9  97.6 143.8  88.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A   2  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 935   OD1                                                    
REMARK 620 2 ASP A 937   OD1  90.5                                              
REMARK 620 3 ASP A 939   OD1  81.9  75.9                                        
REMARK 620 4 ILE A 941   O    73.6 148.9  75.6                                  
REMARK 620 5 ASP A 946   OD2 160.9  95.3  81.9  92.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A1173  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 937   OD2                                                    
REMARK 620 2 ASP A 939   OD2  77.6                                              
REMARK 620 3 ASP A 946   OD1 120.4 135.5                                        
REMARK 620 4 ASP A 946   OD2  84.9  92.7  53.6                                  
REMARK 620 5 CYS A 948   O    66.8 143.9  72.1  90.0                            
REMARK 620 6 ASN A 951   O    70.2  85.3 137.9 154.8  77.4                      
REMARK 620 7 ILE A 954   O   141.0 118.5  74.7 126.0  87.8  75.8                
REMARK 620 8 SER A 955   OG  143.6  68.3  79.2  84.5 147.7 117.6  70.4          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A  13  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A 993   OD1                                                    
REMARK 620 2 ASP A1021   OD1 108.2                                              
REMARK 620 3 ASP A1021   OD2 142.0  48.6                                        
REMARK 620 4 ASP A1023   OD2 133.0 115.9  69.5                                  
REMARK 620 5 SER A1156   O    72.0 112.1  88.8  77.1                            
REMARK 620 6 SER A1156   OG   61.3 168.6 142.5  75.4  70.3                      
REMARK 620 7 HOH A1196   O    78.8  96.7 127.2 110.1 143.9  77.4                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A  14  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A1019   O                                                      
REMARK 620 2 ASP A1021   O    91.1                                              
REMARK 620 3 GLN A1044   OE1 162.3  73.8                                        
REMARK 620 4 ASP A1106   OD1 115.3 135.4  82.3                                  
REMARK 620 5 HOH A1220   O    76.4  80.2 109.0  72.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A  15  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A1022   OD1                                                    
REMARK 620 2 ASP A1023   OD1  71.7                                              
REMARK 620 3 GLN A1047   OE1  88.0  74.2                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 4                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 6                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1173                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 2                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 3                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1174                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1175                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1176                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 7                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 8                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 9                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 10                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 11                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 12                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 13                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 14                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 15                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 16                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 17                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 18                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 19                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 20                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 21                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 22                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 23                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 24                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 25                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 26                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 27                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 28                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 29                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 30                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1YO8   RELATED DB: PDB                                   
DBREF  2RHP A  551  1172  UNP    P35442   TSP2_HUMAN     551   1172             
SEQADV 2RHP SER A  702  UNP  P35442    ASN   702 ENGINEERED                     
SEQRES   1 A  622  ASP GLY CYS LEU SER ASN PRO CYS PHE PRO GLY ALA GLN          
SEQRES   2 A  622  CYS SER SER PHE PRO ASP GLY SER TRP SER CYS GLY PHE          
SEQRES   3 A  622  CYS PRO VAL GLY PHE LEU GLY ASN GLY THR HIS CYS GLU          
SEQRES   4 A  622  ASP LEU ASP GLU CYS ALA LEU VAL PRO ASP ILE CYS PHE          
SEQRES   5 A  622  SER THR SER LYS VAL PRO ARG CYS VAL ASN THR GLN PRO          
SEQRES   6 A  622  GLY PHE HIS CYS LEU PRO CYS PRO PRO ARG TYR ARG GLY          
SEQRES   7 A  622  ASN GLN PRO VAL GLY VAL GLY LEU GLU ALA ALA LYS THR          
SEQRES   8 A  622  GLU LYS GLN VAL CYS GLU PRO GLU ASN PRO CYS LYS ASP          
SEQRES   9 A  622  LYS THR HIS ASN CYS HIS LYS HIS ALA GLU CYS ILE TYR          
SEQRES  10 A  622  LEU GLY HIS PHE SER ASP PRO MET TYR LYS CYS GLU CYS          
SEQRES  11 A  622  GLN THR GLY TYR ALA GLY ASP GLY LEU ILE CYS GLY GLU          
SEQRES  12 A  622  ASP SER ASP LEU ASP GLY TRP PRO SER LEU ASN LEU VAL          
SEQRES  13 A  622  CYS ALA THR ASN ALA THR TYR HIS CYS ILE LYS ASP ASN          
SEQRES  14 A  622  CYS PRO HIS LEU PRO ASN SER GLY GLN GLU ASP PHE ASP          
SEQRES  15 A  622  LYS ASP GLY ILE GLY ASP ALA CYS ASP ASP ASP ASP ASP          
SEQRES  16 A  622  ASN ASP GLY VAL THR ASP GLU LYS ASP ASN CYS GLN LEU          
SEQRES  17 A  622  LEU PHE ASN PRO ARG GLN ALA ASP TYR ASP LYS ASP GLU          
SEQRES  18 A  622  VAL GLY ASP ARG CYS ASP ASN CYS PRO TYR VAL HIS ASN          
SEQRES  19 A  622  PRO ALA GLN ILE ASP THR ASP ASN ASN GLY GLU GLY ASP          
SEQRES  20 A  622  ALA CYS SER VAL ASP ILE ASP GLY ASP ASP VAL PHE ASN          
SEQRES  21 A  622  GLU ARG ASP ASN CYS PRO TYR VAL TYR ASN THR ASP GLN          
SEQRES  22 A  622  ARG ASP THR ASP GLY ASP GLY VAL GLY ASP HIS CYS ASP          
SEQRES  23 A  622  ASN CYS PRO LEU VAL HIS ASN PRO ASP GLN THR ASP VAL          
SEQRES  24 A  622  ASP ASN ASP LEU VAL GLY ASP GLN CYS ASP ASN ASN GLU          
SEQRES  25 A  622  ASP ILE ASP ASP ASP GLY HIS GLN ASN ASN GLN ASP ASN          
SEQRES  26 A  622  CYS PRO TYR ILE SER ASN ALA ASN GLN ALA ASP HIS ASP          
SEQRES  27 A  622  ARG ASP GLY GLN GLY ASP ALA CYS ASP PRO ASP ASP ASP          
SEQRES  28 A  622  ASN ASP GLY VAL PRO ASP ASP ARG ASP ASN CYS ARG LEU          
SEQRES  29 A  622  VAL PHE ASN PRO ASP GLN GLU ASP LEU ASP GLY ASP GLY          
SEQRES  30 A  622  ARG GLY ASP ILE CYS LYS ASP ASP PHE ASP ASN ASP ASN          
SEQRES  31 A  622  ILE PRO ASP ILE ASP ASP VAL CYS PRO GLU ASN ASN ALA          
SEQRES  32 A  622  ILE SER GLU THR ASP PHE ARG ASN PHE GLN MET VAL PRO          
SEQRES  33 A  622  LEU ASP PRO LYS GLY THR THR GLN ILE ASP PRO ASN TRP          
SEQRES  34 A  622  VAL ILE ARG HIS GLN GLY LYS GLU LEU VAL GLN THR ALA          
SEQRES  35 A  622  ASN SER ASP PRO GLY ILE ALA VAL GLY PHE ASP GLU PHE          
SEQRES  36 A  622  GLY SER VAL ASP PHE SER GLY THR PHE TYR VAL ASN THR          
SEQRES  37 A  622  ASP ARG ASP ASP ASP TYR ALA GLY PHE VAL PHE GLY TYR          
SEQRES  38 A  622  GLN SER SER SER ARG PHE TYR VAL VAL MET TRP LYS GLN          
SEQRES  39 A  622  VAL THR GLN THR TYR TRP GLU ASP GLN PRO THR ARG ALA          
SEQRES  40 A  622  TYR GLY TYR SER GLY VAL SER LEU LYS VAL VAL ASN SER          
SEQRES  41 A  622  THR THR GLY THR GLY GLU HIS LEU ARG ASN ALA LEU TRP          
SEQRES  42 A  622  HIS THR GLY ASN THR PRO GLY GLN VAL ARG THR LEU TRP          
SEQRES  43 A  622  HIS ASP PRO ARG ASN ILE GLY TRP LYS ASP TYR THR ALA          
SEQRES  44 A  622  TYR ARG TRP HIS LEU THR HIS ARG PRO LYS THR GLY TYR          
SEQRES  45 A  622  ILE ARG VAL LEU VAL HIS GLU GLY LYS GLN VAL MET ALA          
SEQRES  46 A  622  ASP SER GLY PRO ILE TYR ASP GLN THR TYR ALA GLY GLY          
SEQRES  47 A  622  ARG LEU GLY LEU PHE VAL PHE SER GLN GLU MET VAL TYR          
SEQRES  48 A  622  PHE SER ASP LEU LYS TYR GLU CYS ARG ASP ILE                  
MODRES 2RHP ASN A  710  ASN  GLYCOSYLATION SITE                                 
MODRES 2RHP ASN A 1069  ASN  GLYCOSYLATION SITE                                 
MODRES 2RHP SER A  555  SER  GLYCOSYLATION SITE                                 
HET    NAG  A   1      14                                                       
HET    NAG  A   4      14                                                       
HET    NAG  A   5      14                                                       
HET    NAG  A   6      14                                                       
HET     CA  A1173       1                                                       
HET     CA  A   2       1                                                       
HET     CA  A   3       1                                                       
HET     CA  A1174       1                                                       
HET     CA  A1175       1                                                       
HET     CA  A1176       1                                                       
HET     CA  A   7       1                                                       
HET     CA  A   8       1                                                       
HET     CA  A   9       1                                                       
HET     CA  A  10       1                                                       
HET     CA  A  11       1                                                       
HET     CA  A  12       1                                                       
HET     CA  A  13       1                                                       
HET     CA  A  14       1                                                       
HET     CA  A  15       1                                                       
HET     CA  A  16       1                                                       
HET     CA  A  17       1                                                       
HET     CA  A  18       1                                                       
HET     CA  A  19       1                                                       
HET     CA  A  20       1                                                       
HET     CA  A  21       1                                                       
HET     CA  A  22       1                                                       
HET     CA  A  23       1                                                       
HET     CA  A  24       1                                                       
HET     CA  A  25       1                                                       
HET     CA  A  26       1                                                       
HET     CA  A  27       1                                                       
HET     CA  A  28       1                                                       
HET     CA  A  29       1                                                       
HET     CA  A  30       1                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM      CA CALCIUM ION                                                      
FORMUL   2  NAG    4(C8 H15 N O6)                                               
FORMUL   5   CA    30(CA 2+)                                                    
FORMUL  35  HOH   *71(H2 O)                                                     
HELIX    1   1 ASP A  551  ASN A  556  5                                   6    
HELIX    2   2 LEU A  636  THR A  641  1                                   6    
HELIX    3   3 GLY A  737  ASP A  741  5                                   5    
HELIX    4   4 GLY A  773  ASP A  777  5                                   5    
HELIX    5   5 GLY A  796  SER A  800  5                                   5    
HELIX    6   6 GLY A  832  ASP A  836  5                                   5    
HELIX    7   7 GLN A  870  ASP A  874  5                                   5    
HELIX    8   8 GLY A  893  ASP A  897  5                                   5    
HELIX    9   9 PRO A  906  ASP A  910  5                                   5    
HELIX   10  10 GLY A  929  LYS A  933  5                                   5    
HELIX   11  11 PRO A  942  ASP A  946  5                                   5    
HELIX   12  12 HIS A  983  LYS A  986  5                                   4    
HELIX   13  13 GLY A 1075  HIS A 1084  1                                  10    
SHEET    1   A 2 CYS A 564  SER A 566  0                                        
SHEET    2   A 2 TRP A 572  CYS A 574 -1  O  SER A 573   N  SER A 565           
SHEET    1   B 3 CYS A 610  ASN A 612  0                                        
SHEET    2   B 3 PHE A 617  CYS A 619 -1  O  HIS A 618   N  VAL A 611           
SHEET    3   B 3 VAL A 632  GLY A 633 -1  O  GLY A 633   N  PHE A 617           
SHEET    1   C 2 TYR A 626  GLY A 628  0                                        
SHEET    2   C 2 CYS A 646  PRO A 648 -1  O  GLU A 647   N  ARG A 627           
SHEET    1   D 2 ALA A 663  TYR A 667  0                                        
SHEET    2   D 2 TYR A 676  CYS A 680 -1  O  GLU A 679   N  GLU A 664           
SHEET    1   E 2 TYR A 684  GLY A 686  0                                        
SHEET    2   E 2 CYS A 691  GLU A 693 -1  O  GLY A 692   N  ALA A 685           
SHEET    1   F 7 PHE A 962  PRO A 966  0                                        
SHEET    2   F 7 GLY A 997  PHE A1005 -1  O  VAL A1000   N  GLN A 963           
SHEET    3   F 7 GLY A1148  PHE A1155 -1  O  LEU A1152   N  ALA A 999           
SHEET    4   F 7 TYR A1024  SER A1033 -1  N  TYR A1031   O  ARG A1149           
SHEET    5   F 7 ARG A1036  LYS A1043 -1  O  TYR A1038   N  PHE A1029           
SHEET    6   F 7 GLY A1062  ASN A1069 -1  O  SER A1064   N  MET A1041           
SHEET    7   F 7 VAL A1092  HIS A1097 -1  O  LEU A1095   N  LEU A1065           
SHEET    1   G 7 TRP A 979  ARG A 982  0                                        
SHEET    2   G 7 GLU A 987  GLN A 990 -1  O  GLU A 987   N  ARG A 982           
SHEET    3   G 7 VAL A1160  GLU A1168 -1  O  PHE A1162   N  LEU A 988           
SHEET    4   G 7 VAL A1008  VAL A1016 -1  N  THR A1013   O  SER A1163           
SHEET    5   G 7 TYR A1110  HIS A1116 -1  O  LEU A1114   N  PHE A1010           
SHEET    6   G 7 TYR A1122  GLU A1129 -1  O  HIS A1128   N  ARG A1111           
SHEET    7   G 7 GLN A1132  ASP A1136 -1  O  GLN A1132   N  GLU A1129           
SHEET    1   H 7 TRP A 979  ARG A 982  0                                        
SHEET    2   H 7 GLU A 987  GLN A 990 -1  O  GLU A 987   N  ARG A 982           
SHEET    3   H 7 VAL A1160  GLU A1168 -1  O  PHE A1162   N  LEU A 988           
SHEET    4   H 7 VAL A1008  VAL A1016 -1  N  THR A1013   O  SER A1163           
SHEET    5   H 7 TYR A1110  HIS A1116 -1  O  LEU A1114   N  PHE A1010           
SHEET    6   H 7 TYR A1122  GLU A1129 -1  O  HIS A1128   N  ARG A1111           
SHEET    7   H 7 ILE A1140  TYR A1141 -1  O  ILE A1140   N  ILE A1123           
SHEET    1   I 2 GLN A1047  THR A1048  0                                        
SHEET    2   I 2 TYR A1058  GLY A1059 -1  O  GLY A1059   N  GLN A1047           
SSBOND   1 CYS A  553    CYS A  564                          1555   1555  2.04  
SSBOND   2 CYS A  558    CYS A  574                          1555   1555  2.04  
SSBOND   3 CYS A  577    CYS A  588                          1555   1555  2.02  
SSBOND   4 CYS A  594    CYS A  610                          1555   1555  2.03  
SSBOND   5 CYS A  601    CYS A  619                          1555   1555  2.03  
SSBOND   6 CYS A  622    CYS A  646                          1555   1555  2.02  
SSBOND   7 CYS A  652    CYS A  665                          1555   1555  2.04  
SSBOND   8 CYS A  659    CYS A  678                          1555   1555  2.03  
SSBOND   9 CYS A  680    CYS A  691                          1555   1555  2.04  
SSBOND  10 CYS A  707    CYS A  715                          1555   1555  2.04  
SSBOND  11 CYS A  720    CYS A  740                          1555   1555  2.04  
SSBOND  12 CYS A  756    CYS A  776                          1555   1555  2.03  
SSBOND  13 CYS A  779    CYS A  799                          1555   1555  2.04  
SSBOND  14 CYS A  815    CYS A  835                          1555   1555  2.02  
SSBOND  15 CYS A  838    CYS A  858                          1555   1555  2.02  
SSBOND  16 CYS A  876    CYS A  896                          1555   1555  2.05  
SSBOND  17 CYS A  912    CYS A  932                          1555   1555  2.05  
SSBOND  18 CYS A  948    CYS A 1169                          1555   1555  2.05  
LINK         OD1 ASP A 590                CA    CA A  30     1555   1555  2.55  
LINK         O   LEU A 591                CA    CA A  30     1555   1555  2.39  
LINK         OE1 GLU A 593                CA    CA A  30     1555   1555  2.64  
LINK         OD1 ASN A 612                CA    CA A  30     1555   1555  2.91  
LINK         O   THR A 613                CA    CA A  30     1555   1555  2.35  
LINK         O   GLY A 616                CA    CA A  30     1555   1555  2.32  
LINK         OD1 ASP A 694                CA    CA A  28     1555   1555  2.59  
LINK         OD1 ASP A 696                CA    CA A  28     1555   1555  2.20  
LINK         OD2 ASP A 696                CA    CA A  29     1555   1555  2.29  
LINK         OD1 ASP A 698                CA    CA A  28     1555   1555  2.42  
LINK         OD2 ASP A 698                CA    CA A  29     1555   1555  2.33  
LINK         O   TRP A 700                CA    CA A  28     1555   1555  2.15  
LINK         ND2 ASN A 710                 C1  NAG A   1     1555   1555  1.45  
LINK         OD1 ASP A 718                CA    CA A  29     1555   1555  2.76  
LINK         OD2 ASP A 718                CA    CA A  29     1555   1555  2.50  
LINK         OD2 ASP A 718                CA    CA A  28     1555   1555  2.21  
LINK         O   CYS A 720                CA    CA A  29     1555   1555  2.13  
LINK         O   LEU A 723                CA    CA A  29     1555   1555  2.42  
LINK         OD1 ASN A 725                CA    CA A  29     1555   1555  2.40  
LINK         OD1 ASP A 730                CA    CA A  25     1555   1555  2.28  
LINK         OD1 ASP A 732                CA    CA A  25     1555   1555  2.67  
LINK         OD2 ASP A 732                CA    CA A  26     1555   1555  2.18  
LINK         OD1 ASP A 734                CA    CA A  25     1555   1555  2.88  
LINK         OD2 ASP A 734                CA    CA A  26     1555   1555  2.25  
LINK         O   ILE A 736                CA    CA A  25     1555   1555  2.21  
LINK         O   ASP A 738                CA    CA A  27     1555   1555  2.37  
LINK         O   ASP A 741                CA    CA A  27     1555   1555  2.52  
LINK         OD1 ASP A 741                CA    CA A  26     1555   1555  2.73  
LINK         OD2 ASP A 741                CA    CA A  26     1555   1555  2.53  
LINK         OD2 ASP A 741                CA    CA A  25     1555   1555  2.16  
LINK         O   ASP A 743                CA    CA A  26     1555   1555  2.52  
LINK         OD1 ASP A 743                CA    CA A  24     1555   1555  2.33  
LINK         OD1 ASP A 744                CA    CA A  27     1555   1555  2.45  
LINK         OD2 ASP A 744                CA    CA A  27     1555   1555  2.55  
LINK         OD1 ASP A 745                CA    CA A  24     1555   1555  2.27  
LINK         OD2 ASP A 745                CA    CA A  23     1555   1555  2.55  
LINK         OD1 ASN A 746                CA    CA A  26     1555   1555  2.41  
LINK         OD1 ASP A 747                CA    CA A  24     1555   1555  2.91  
LINK         OD2 ASP A 747                CA    CA A  23     1555   1555  2.50  
LINK         O   VAL A 749                CA    CA A  24     1555   1555  2.57  
LINK         OD2 ASP A 751                CA    CA A  27     1555   1555  2.80  
LINK         OD1 ASP A 754                CA    CA A  23     1555   1555  2.75  
LINK         OD2 ASP A 754                CA    CA A  23     1555   1555  2.37  
LINK         OD2 ASP A 754                CA    CA A  24     1555   1555  2.37  
LINK         O   CYS A 756                CA    CA A  23     1555   1555  2.56  
LINK         O   LEU A 759                CA    CA A  23     1555   1555  2.18  
LINK         OD1 ASN A 761                CA    CA A  23     1555   1555  2.13  
LINK         OD1 ASP A 766                CA    CA A  22     1555   1555  2.23  
LINK         OD1 ASP A 768                CA    CA A  22     1555   1555  2.66  
LINK         OD1 ASP A 770                CA    CA A  22     1555   1555  2.33  
LINK         OD2 ASP A 770                CA    CA A  21     1555   1555  2.49  
LINK         O   VAL A 772                CA    CA A  22     1555   1555  2.60  
LINK         OD1 ASP A 777                CA    CA A  21     1555   1555  2.95  
LINK         OD2 ASP A 777                CA    CA A  21     1555   1555  2.48  
LINK         OD2 ASP A 777                CA    CA A  22     1555   1555  2.43  
LINK         O   CYS A 779                CA    CA A  21     1555   1555  2.44  
LINK         O   VAL A 782                CA    CA A  21     1555   1555  2.10  
LINK         OD1 ASN A 784                CA    CA A  21     1555   1555  2.20  
LINK         OD1 ASP A 789                CA    CA A  16     1555   1555  2.27  
LINK         OD1 ASP A 791                CA    CA A  16     1555   1555  2.06  
LINK         OD1 ASN A 793                CA    CA A  16     1555   1555  2.68  
LINK         O   GLU A 795                CA    CA A  16     1555   1555  2.22  
LINK         OD1 ASP A 802                CA    CA A  20     1555   1555  2.32  
LINK         OD1 ASP A 804                CA    CA A  20     1555   1555  2.21  
LINK         OD2 ASP A 804                CA    CA A  19     1555   1555  2.17  
LINK         OD1 ASP A 806                CA    CA A  20     1555   1555  2.23  
LINK         OD2 ASP A 806                CA    CA A  19     1555   1555  2.15  
LINK         O   VAL A 808                CA    CA A  20     1555   1555  2.21  
LINK         OD1 ASP A 813                CA    CA A  19     1555   1555  2.70  
LINK         OD2 ASP A 813                CA    CA A  20     1555   1555  2.14  
LINK         OD2 ASP A 813                CA    CA A  19     1555   1555  2.49  
LINK         O   CYS A 815                CA    CA A  19     1555   1555  2.97  
LINK         O   VAL A 818                CA    CA A  19     1555   1555  2.39  
LINK         OD1 ASN A 820                CA    CA A  19     1555   1555  2.29  
LINK         OD1 ASP A 825                CA    CA A  18     1555   1555  2.59  
LINK         OD1 ASP A 827                CA    CA A  18     1555   1555  2.10  
LINK         OD2 ASP A 827                CA    CA A  17     1555   1555  2.49  
LINK         OD1 ASP A 829                CA    CA A  18     1555   1555  2.52  
LINK         O   VAL A 831                CA    CA A  18     1555   1555  2.46  
LINK         OD1 ASP A 836                CA    CA A  17     1555   1555  2.80  
LINK         OD2 ASP A 836                CA    CA A  18     1555   1555  2.65  
LINK         OD2 ASP A 836                CA    CA A  17     1555   1555  2.08  
LINK         O   CYS A 838                CA    CA A  17     1555   1555  2.63  
LINK         O   VAL A 841                CA    CA A  17     1555   1555  2.53  
LINK         OD1 ASN A 843                CA    CA A  17     1555   1555  2.62  
LINK         OD1 ASP A 848                CA    CA A  12     1555   1555  2.23  
LINK         OD1 ASP A 850                CA    CA A  12     1555   1555  2.35  
LINK         OD2 ASP A 850                CA    CA A  11     1555   1555  2.54  
LINK         OD1 ASP A 852                CA    CA A  12     1555   1555  2.36  
LINK         OD2 ASP A 852                CA    CA A  11     1555   1555  2.39  
LINK         O   VAL A 854                CA    CA A  12     1555   1555  2.23  
LINK         OD1 ASP A 859                CA    CA A  11     1555   1555  2.25  
LINK         OD2 ASP A 859                CA    CA A  12     1555   1555  2.08  
LINK         OD2 ASP A 859                CA    CA A  11     1555   1555  2.66  
LINK         OD1 ASN A 861                CA    CA A  11     1555   1555  2.25  
LINK         OD1 ASP A 863                CA    CA A  10     1555   1555  2.20  
LINK         OD1 ASP A 865                CA    CA A  10     1555   1555  2.18  
LINK         OD2 ASP A 865                CA    CA A   9     1555   1555  2.26  
LINK         OD1 ASP A 867                CA    CA A  10     1555   1555  2.46  
LINK         OD2 ASP A 867                CA    CA A   9     1555   1555  2.29  
LINK         O   HIS A 869                CA    CA A  10     1555   1555  2.34  
LINK         OD1 ASP A 874                CA    CA A   9     1555   1555  2.90  
LINK         OD2 ASP A 874                CA    CA A  10     1555   1555  2.38  
LINK         OD2 ASP A 874                CA    CA A   9     1555   1555  2.25  
LINK         O   CYS A 876                CA    CA A   9     1555   1555  2.40  
LINK         O   ILE A 879                CA    CA A   9     1555   1555  2.35  
LINK         OD1 ASN A 881                CA    CA A   9     1555   1555  2.32  
LINK         OD1 ASP A 886                CA    CA A   7     1555   1555  2.25  
LINK         OD1 ASP A 888                CA    CA A   7     1555   1555  2.32  
LINK         OD2 ASP A 888                CA    CA A1176     1555   1555  2.72  
LINK         OD1 ASP A 890                CA    CA A   7     1555   1555  2.26  
LINK         OD2 ASP A 890                CA    CA A1176     1555   1555  2.31  
LINK         O   GLN A 892                CA    CA A   7     1555   1555  2.28  
LINK         O   ASP A 894                CA    CA A   8     1555   1555  2.38  
LINK         O   ASP A 897                CA    CA A   8     1555   1555  2.06  
LINK         OD1 ASP A 897                CA    CA A1176     1555   1555  2.87  
LINK         OD2 ASP A 897                CA    CA A   7     1555   1555  2.59  
LINK         OD2 ASP A 897                CA    CA A1176     1555   1555  2.40  
LINK         O   ASP A 899                CA    CA A1176     1555   1555  2.42  
LINK         OD1 ASP A 899                CA    CA A1174     1555   1555  2.30  
LINK         OD1 ASP A 900                CA    CA A   8     1555   1555  2.44  
LINK         OD2 ASP A 900                CA    CA A   8     1555   1555  2.81  
LINK         OD1 ASP A 901                CA    CA A1174     1555   1555  2.34  
LINK         OD2 ASP A 901                CA    CA A1175     1555   1555  2.49  
LINK         OD1 ASN A 902                CA    CA A1176     1555   1555  2.65  
LINK         OD1 ASP A 903                CA    CA A1174     1555   1555  2.38  
LINK         OD2 ASP A 903                CA    CA A1175     1555   1555  2.11  
LINK         O   VAL A 905                CA    CA A1174     1555   1555  2.39  
LINK         OD2 ASP A 907                CA    CA A   8     1555   1555  2.20  
LINK         OD1 ASP A 910                CA    CA A1175     1555   1555  2.72  
LINK         OD2 ASP A 910                CA    CA A1175     1555   1555  2.74  
LINK         OD2 ASP A 910                CA    CA A1174     1555   1555  2.27  
LINK         O   CYS A 912                CA    CA A1175     1555   1555  2.43  
LINK         O   VAL A 915                CA    CA A1175     1555   1555  2.56  
LINK         OD1 ASN A 917                CA    CA A1175     1555   1555  2.40  
LINK         OD1 ASP A 922                CA    CA A   3     1555   1555  2.60  
LINK         OD1 ASP A 924                CA    CA A   3     1555   1555  2.35  
LINK         OD1 ASP A 926                CA    CA A   3     1555   1555  2.28  
LINK         O   ARG A 928                CA    CA A   3     1555   1555  2.38  
LINK         OD1 ASP A 930                CA    CA A   3     1555   1555  2.37  
LINK         OD1 ASP A 935                CA    CA A   2     1555   1555  2.22  
LINK         OD1 ASP A 937                CA    CA A   2     1555   1555  2.10  
LINK         OD2 ASP A 937                CA    CA A1173     1555   1555  2.48  
LINK         OD1 ASP A 939                CA    CA A   2     1555   1555  2.71  
LINK         OD2 ASP A 939                CA    CA A1173     1555   1555  2.26  
LINK         O   ILE A 941                CA    CA A   2     1555   1555  2.33  
LINK         OD1 ASP A 946                CA    CA A1173     1555   1555  2.61  
LINK         OD2 ASP A 946                CA    CA A1173     1555   1555  2.19  
LINK         OD2 ASP A 946                CA    CA A   2     1555   1555  2.51  
LINK         O   CYS A 948                CA    CA A1173     1555   1555  2.52  
LINK         O   ASN A 951                CA    CA A1173     1555   1555  2.41  
LINK         O   ILE A 954                CA    CA A1173     1555   1555  2.29  
LINK         OG  SER A 955                CA    CA A1173     1555   1555  2.94  
LINK         OD1 ASN A 993                CA    CA A  13     1555   1555  2.99  
LINK         O   ASP A1019                CA    CA A  14     1555   1555  2.85  
LINK         O   ASP A1021                CA    CA A  14     1555   1555  2.56  
LINK         OD1 ASP A1021                CA    CA A  13     1555   1555  2.85  
LINK         OD2 ASP A1021                CA    CA A  13     1555   1555  2.45  
LINK         OD1 ASP A1022                CA    CA A  15     1555   1555  2.35  
LINK         OD1 ASP A1023                CA    CA A  15     1555   1555  2.42  
LINK         OD2 ASP A1023                CA    CA A  13     1555   1555  2.54  
LINK         OE1 GLN A1044                CA    CA A  14     1555   1555  2.60  
LINK         OE1 GLN A1047                CA    CA A  15     1555   1555  2.46  
LINK         ND2 ASN A1069                 C1  NAG A   4     1555   1555  1.44  
LINK         OD1 ASP A1106                CA    CA A  14     1555   1555  2.72  
LINK         O   SER A1156                CA    CA A  13     1555   1555  2.38  
LINK         OG  SER A1156                CA    CA A  13     1555   1555  2.34  
LINK         O4  NAG A   4                 C1  NAG A   5     1555   1555  1.45  
LINK        CA    CA A1174                 O   HOH A1204     1555   1555  2.46  
LINK        CA    CA A   8                 O   HOH A1219     1555   1555  2.92  
LINK        CA    CA A  12                 O   HOH A1229     1555   1555  2.23  
LINK        CA    CA A  13                 O   HOH A1196     1555   1555  2.74  
LINK        CA    CA A  14                 O   HOH A1220     1555   1555  2.27  
LINK         OG  SER A 555                 C1  NAG A   6     1555   1555  1.44  
CISPEP   1 ASP A  673    PRO A  674          0         0.95                     
CISPEP   2 GLN A 1053    PRO A 1054          0        -1.97                     
SITE     1 AC1  4 ASP A 866  ASN A1069  THR A1071  THR A1144                    
SITE     1 AC2  4 GLY A 552  SER A 555  GLY A 570  TRP A 572                    
SITE     1 AC3  7 ASP A 937  ASP A 939  ASP A 946  CYS A 948                    
SITE     2 AC3  7 ASN A 951  ILE A 954  SER A 955                               
SITE     1 AC4  5 ASP A 935  ASP A 937  ASP A 939  ILE A 941                    
SITE     2 AC4  5 ASP A 946                                                     
SITE     1 AC5  5 ASP A 922  ASP A 924  ASP A 926  ARG A 928                    
SITE     2 AC5  5 ASP A 930                                                     
SITE     1 AC6  5 ASP A 899  ASP A 901  ASP A 903  ASP A 910                    
SITE     2 AC6  5 HOH A1204                                                     
SITE     1 AC7  5 ASP A 901  ASP A 903  ASP A 910  CYS A 912                    
SITE     2 AC7  5 ASN A 917                                                     
SITE     1 AC8  5 ASP A 888  ASP A 890  ASP A 897  ASP A 899                    
SITE     2 AC8  5 ASN A 902                                                     
SITE     1 AC9  5 ASP A 886  ASP A 888  ASP A 890  GLN A 892                    
SITE     2 AC9  5 ASP A 897                                                     
SITE     1 BC1  5 ASP A 894  ASP A 897  ASP A 900  ASP A 907                    
SITE     2 BC1  5 HOH A1219                                                     
SITE     1 BC2  7 ASP A 865  ASP A 867  ASP A 874  CYS A 876                    
SITE     2 BC2  7 ILE A 879  SER A 880  ASN A 881                               
SITE     1 BC3  5 ASP A 863  ASP A 865  ASP A 867  HIS A 869                    
SITE     2 BC3  5 ASP A 874                                                     
SITE     1 BC4  4 ASP A 850  ASP A 852  ASP A 859  ASN A 861                    
SITE     1 BC5  5 ASP A 848  ASP A 850  ASP A 852  ASP A 859                    
SITE     2 BC5  5 HOH A1229                                                     
SITE     1 BC6  5 ASN A 993  ASP A1021  ASP A1023  SER A1156                    
SITE     2 BC6  5 HOH A1196                                                     
SITE     1 BC7  5 ASP A1019  ASP A1021  GLN A1044  ASP A1106                    
SITE     2 BC7  5 HOH A1220                                                     
SITE     1 BC8  4 ASP A1021  ASP A1022  ASP A1023  GLN A1047                    
SITE     1 BC9  4 ASP A 789  ASP A 791  ASN A 793  GLU A 795                    
SITE     1 CC1  5 ASP A 827  ASP A 829  ASP A 836  CYS A 838                    
SITE     2 CC1  5 ASN A 843                                                     
SITE     1 CC2  4 ASP A 825  ASP A 827  ASP A 829  ASP A 836                    
SITE     1 CC3  5 ASP A 804  ASP A 806  ASP A 813  CYS A 815                    
SITE     2 CC3  5 ASN A 820                                                     
SITE     1 CC4  4 ASP A 802  ASP A 804  ASP A 806  ASP A 813                    
SITE     1 CC5  5 ASP A 768  ASP A 770  ASP A 777  CYS A 779                    
SITE     2 CC5  5 ASN A 784                                                     
SITE     1 CC6  4 ASP A 766  ASP A 768  ASP A 770  ASP A 777                    
SITE     1 CC7  6 ASP A 745  ASP A 747  ASP A 754  CYS A 756                    
SITE     2 CC7  6 LEU A 759  ASN A 761                                          
SITE     1 CC8  4 ASP A 743  ASP A 745  ASP A 747  ASP A 754                    
SITE     1 CC9  5 ASP A 730  ASP A 732  ASP A 734  ILE A 736                    
SITE     2 CC9  5 ASP A 741                                                     
SITE     1 DC1  5 ASP A 732  ASP A 734  ASP A 741  ASP A 743                    
SITE     2 DC1  5 ASN A 746                                                     
SITE     1 DC2  4 ASP A 738  ASP A 741  ASP A 744  ASP A 751                    
SITE     1 DC3  5 ASP A 694  ASP A 696  ASP A 698  TRP A 700                    
SITE     2 DC3  5 ASP A 718                                                     
SITE     1 DC4  6 ASP A 696  ASP A 698  ASP A 718  CYS A 720                    
SITE     2 DC4  6 LEU A 723  ASN A 725                                          
SITE     1 DC5  6 ASP A 590  LEU A 591  GLU A 593  ASN A 612                    
SITE     2 DC5  6 THR A 613  GLY A 616                                          
CRYST1   93.892  122.650  155.381  90.00  90.00  90.00 I 2 2 2       8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.010651  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008153  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006436        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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