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Database: PDB
Entry: 6AZP
LinkDB: 6AZP
Original site: 6AZP 
HEADER    OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 11-SEP-17   6AZP              
TITLE     A STRUCTURALLY DYNAMIC N-TERMINAL REGION DRIVES FUNCTION OF THE       
TITLE    2 STAPHYLOCOCCAL PEROXIDASE INHIBITOR (SPIN)                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MYELOPEROXIDASE;                                           
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: MPO;                                                        
COMPND   5 EC: 1.11.2.2;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: STAPHYLOCOCCAL PEROXIDASE INHIBITOR;                       
COMPND   9 CHAIN: B;                                                            
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: MPO;                                                           
SOURCE   6 EXPRESSION_SYSTEM: MUS MUSCULUS;                                     
SOURCE   7 EXPRESSION_SYSTEM_COMMON: MOUSE;                                     
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 10090;                                      
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;                          
SOURCE  11 ORGANISM_TAXID: 1280;                                                
SOURCE  12 GENE: SAMEA3448974_01858;                                            
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  15 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)                                  
KEYWDS    MYELOPEROXIDASE, INHIBITOR, COMPLEX, INNATE IMMUNE EVASION,           
KEYWDS   2 OXIDOREDUCTASE-OXIDOREDUCTASE INHIBITOR COMPLEX                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.X.RAMYAR,B.V.GEISBRECHT                                             
REVDAT   4   11-DEC-19 6AZP    1       REMARK                                   
REVDAT   3   28-FEB-18 6AZP    1       JRNL                                     
REVDAT   2   17-JAN-18 6AZP    1       JRNL                                     
REVDAT   1   27-DEC-17 6AZP    0                                                
JRNL        AUTH   N.W.M.DE JONG,N.T.PLOSCARIU,K.X.RAMYAR,B.L.GARCIA,           
JRNL        AUTH 2 A.I.HERRERA,O.PRAKASH,B.B.KATZ,K.G.LEIDAL,W.M.NAUSEEF,       
JRNL        AUTH 3 K.P.M.VAN KESSEL,J.A.G.VAN STRIJP,B.V.GEISBRECHT             
JRNL        TITL   A STRUCTURALLY DYNAMIC N-TERMINAL REGION DRIVES FUNCTION OF  
JRNL        TITL 2 THE STAPHYLOCOCCAL PEROXIDASE INHIBITOR (SPIN).              
JRNL        REF    J. BIOL. CHEM.                V. 293  2260 2018              
JRNL        REFN                   ESSN 1083-351X                               
JRNL        PMID   29306874                                                     
JRNL        DOI    10.1074/JBC.RA117.000134                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.29 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.29                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.96                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 36470                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.182                           
REMARK   3   R VALUE            (WORKING SET) : 0.179                           
REMARK   3   FREE R VALUE                     : 0.229                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.480                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2000                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 38.9636 -  5.5171    0.99     2554   149  0.1698 0.2004        
REMARK   3     2  5.5171 -  4.3810    1.00     2499   145  0.1398 0.1981        
REMARK   3     3  4.3810 -  3.8278    0.99     2482   144  0.1398 0.1943        
REMARK   3     4  3.8278 -  3.4780    0.99     2506   145  0.1630 0.1873        
REMARK   3     5  3.4780 -  3.2289    0.99     2457   143  0.1895 0.2198        
REMARK   3     6  3.2289 -  3.0386    0.99     2501   145  0.2013 0.2728        
REMARK   3     7  3.0386 -  2.8865    0.99     2475   143  0.1937 0.2315        
REMARK   3     8  2.8865 -  2.7609    0.99     2451   142  0.2070 0.2612        
REMARK   3     9  2.7609 -  2.6546    0.99     2451   142  0.2078 0.2635        
REMARK   3    10  2.6546 -  2.5630    0.99     2430   142  0.2062 0.2965        
REMARK   3    11  2.5630 -  2.4829    0.99     2471   143  0.2125 0.2995        
REMARK   3    12  2.4829 -  2.4119    0.99     2457   142  0.2224 0.2636        
REMARK   3    13  2.4119 -  2.3484    0.98     2439   142  0.2395 0.3308        
REMARK   3    14  2.3484 -  2.2911    0.92     2297   133  0.2632 0.3554        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.270            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.910           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 35.36                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 42.01                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.011           5287                                  
REMARK   3   ANGLE     :  1.136           7160                                  
REMARK   3   CHIRALITY :  0.055            778                                  
REMARK   3   PLANARITY :  0.007            943                                  
REMARK   3   DIHEDRAL  : 15.317           2037                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6AZP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-SEP-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000230048.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-DEC-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-BM                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00                               
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL SI(220)             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 36486                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.291                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 7.700                              
REMARK 200  R MERGE                    (I) : 0.15100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.38                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.10                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: PDB ENTRY 5UZU                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.33                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.88                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% W/V PEG3350, 0.2 M AMMONIUM          
REMARK 280  CITRATE, PH 7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE         
REMARK 280  298.0K                                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
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+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       64.42700            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       46.43800            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       64.42700            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       46.43800            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2520 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 26320 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 11.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH B 210  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH B 213  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     HIS B   103                                                      
REMARK 465     VAL B   104                                                      
REMARK 465     LYS B   105                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O4   NAG A   803     C1   BMA A   804              1.57            
REMARK 500   ND2  ASN A   391     C1   NAG A   805              1.81            
REMARK 500   OD1  ASN A   355     C1   NAG A   802              1.86            
REMARK 500   ND2  ASN A   483     C1   NAG A   801              1.96            
REMARK 500   ND2  ASN A   355     C1   NAG A   802              2.06            
REMARK 500   O    HOH A  1142     O    HOH A  1143              2.07            
REMARK 500   OE2  GLU A   347     O    HOH A   901              2.13            
REMARK 500   O    TYR B   101     O    HOH B   201              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PRO A 168     -168.91    -68.23                                   
REMARK 500    GLU A 169       50.83   -145.43                                   
REMARK 500    GLN A 170       24.81   -163.04                                   
REMARK 500    PHE A 207      -43.96   -130.31                                   
REMARK 500    SER A 208      -22.58   -159.50                                   
REMARK 500    ASN A 220       48.07     39.94                                   
REMARK 500    LEU A 242      140.44    -39.45                                   
REMARK 500    VAL A 276      -60.95     62.23                                   
REMARK 500    THR A 277     -133.93    -76.36                                   
REMARK 500    ASN A 323        9.75     48.31                                   
REMARK 500    ASN A 391       96.09   -163.41                                   
REMARK 500    PRO A 477      170.10    -58.20                                   
REMARK 500    ARG A 480      -87.01    -98.97                                   
REMARK 500    ASP A 484        5.37    -69.24                                   
REMARK 500    ASN A 514      -46.79    -20.95                                   
REMARK 500    PHE A 532       15.86     58.94                                   
REMARK 500    SER A 534      -39.29    -36.61                                   
REMARK 500    ASN A 623       91.73   -164.29                                   
REMARK 500    ASN A 721        5.92   -165.18                                   
REMARK 500    ARG A 742       36.27    -87.29                                   
REMARK 500    ASP B  65      118.97    -36.87                                   
REMARK 500    LYS B 100      -21.66    113.14                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     NAG A  801                                                       
REMARK 610     NAG A  802                                                       
REMARK 610     BMA A  804                                                       
REMARK 610     NAG A  805                                                       
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 806  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 262   O                                                      
REMARK 620 2 ASP A 262   OD1  72.2                                              
REMARK 620 3 THR A 334   O    74.4 142.4                                        
REMARK 620 4 THR A 334   OG1 129.0 144.4  72.1                                  
REMARK 620 5 PHE A 336   O   110.3  81.7  94.3 109.6                            
REMARK 620 6 ASP A 338   OD1 143.8  74.9 141.3  74.4  79.2                      
REMARK 620 7 SER A 340   OG   85.3  76.2 117.7  77.7 147.5  72.3                
REMARK 620 N                    1     2     3     4     5     6                 
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 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BMA A 804                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NAG A 805                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 806                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  802 through NAG A 803                                               
DBREF  6AZP A  167   743  UNP    P05164   PERM_HUMAN      72    648             
DBREF1 6AZP B   46   105  UNP                  A0A1K8H768_STAAU                 
DBREF2 6AZP B     A0A1K8H768                         43         102             
SEQRES   1 A  577  CYS PRO GLU GLN ASP LYS TYR ARG THR ILE THR GLY MET          
SEQRES   2 A  577  CYS ASN ASN ARG ARG SER PRO THR LEU GLY ALA SER ASN          
SEQRES   3 A  577  ARG ALA PHE VAL ARG TRP LEU PRO ALA GLU TYR GLU ASP          
SEQRES   4 A  577  GLY PHE SER LEU PRO TYR GLY TRP THR PRO GLY VAL LYS          
SEQRES   5 A  577  ARG ASN GLY PHE PRO VAL ALA LEU ALA ARG ALA VAL SER          
SEQRES   6 A  577  ASN GLU ILE VAL ARG PHE PRO THR ASP GLN LEU THR PRO          
SEQRES   7 A  577  ASP GLN GLU ARG SER LEU MET PHE MET GLN TRP GLY GLN          
SEQRES   8 A  577  LEU LEU ASP HIS ASP LEU ASP PHE THR PRO GLU PRO ALA          
SEQRES   9 A  577  ALA ARG ALA SER PHE VAL THR GLY VAL ASN CYS GLU THR          
SEQRES  10 A  577  SER CYS VAL GLN GLN PRO PRO CYS PHE PRO LEU LYS ILE          
SEQRES  11 A  577  PRO PRO ASN ASP PRO ARG ILE LYS ASN GLN ALA ASP CYS          
SEQRES  12 A  577  ILE PRO PHE PHE ARG SER CSO PRO ALA CYS PRO GLY SER          
SEQRES  13 A  577  ASN ILE THR ILE ARG ASN GLN ILE ASN ALA LEU THR SER          
SEQRES  14 A  577  PHE VAL ASP ALA SER MET VAL TYR GLY SER GLU GLU PRO          
SEQRES  15 A  577  LEU ALA ARG ASN LEU ARG ASN MET SER ASN GLN LEU GLY          
SEQRES  16 A  577  LEU LEU ALA VAL ASN GLN ARG PHE GLN ASP ASN GLY ARG          
SEQRES  17 A  577  ALA LEU LEU PRO PHE ASP ASN LEU HIS ASP ASP PRO CYS          
SEQRES  18 A  577  LEU LEU THR ASN ARG SER ALA ARG ILE PRO CYS PHE LEU          
SEQRES  19 A  577  ALA GLY ASP THR ARG SER SER GLU MET PRO GLU LEU THR          
SEQRES  20 A  577  SER MET HIS THR LEU LEU LEU ARG GLU HIS ASN ARG LEU          
SEQRES  21 A  577  ALA THR GLU LEU LYS SER LEU ASN PRO ARG TRP ASP GLY          
SEQRES  22 A  577  GLU ARG LEU TYR GLN GLU ALA ARG LYS ILE VAL GLY ALA          
SEQRES  23 A  577  MET VAL GLN ILE ILE THR TYR ARG ASP TYR LEU PRO LEU          
SEQRES  24 A  577  VAL LEU GLY PRO THR ALA MET ARG LYS TYR LEU PRO THR          
SEQRES  25 A  577  TYR ARG SER TYR ASN ASP SER VAL ASP PRO ARG ILE ALA          
SEQRES  26 A  577  ASN VAL PHE THR ASN ALA PHE ARG TYR GLY HIS THR LEU          
SEQRES  27 A  577  ILE GLN PRO PHE MET PHE ARG LEU ASP ASN ARG TYR GLN          
SEQRES  28 A  577  PRO MET GLU PRO ASN PRO ARG VAL PRO LEU SER ARG VAL          
SEQRES  29 A  577  PHE PHE ALA SER TRP ARG VAL VAL LEU GLU GLY GLY ILE          
SEQRES  30 A  577  ASP PRO ILE LEU ARG GLY LEU MET ALA THR PRO ALA LYS          
SEQRES  31 A  577  LEU ASN ARG GLN ASN GLN ILE ALA VAL ASP GLU ILE ARG          
SEQRES  32 A  577  GLU ARG LEU PHE GLU GLN VAL MET ARG ILE GLY LEU ASP          
SEQRES  33 A  577  LEU PRO ALA LEU ASN MET GLN ARG SER ARG ASP HIS GLY          
SEQRES  34 A  577  LEU PRO GLY TYR ASN ALA TRP ARG ARG PHE CYS GLY LEU          
SEQRES  35 A  577  PRO GLN PRO GLU THR VAL GLY GLN LEU GLY THR VAL LEU          
SEQRES  36 A  577  ARG ASN LEU LYS LEU ALA ARG LYS LEU MET GLU GLN TYR          
SEQRES  37 A  577  GLY THR PRO ASN ASN ILE ASP ILE TRP MET GLY GLY VAL          
SEQRES  38 A  577  SER GLU PRO LEU LYS ARG LYS GLY ARG VAL GLY PRO LEU          
SEQRES  39 A  577  LEU ALA CYS ILE ILE GLY THR GLN PHE ARG LYS LEU ARG          
SEQRES  40 A  577  ASP GLY ASP ARG PHE TRP TRP GLU ASN GLU GLY VAL PHE          
SEQRES  41 A  577  SER MET GLN GLN ARG GLN ALA LEU ALA GLN ILE SER LEU          
SEQRES  42 A  577  PRO ARG ILE ILE CYS ASP ASN THR GLY ILE THR THR VAL          
SEQRES  43 A  577  SER LYS ASN ASN ILE PHE MET SER ASN SER TYR PRO ARG          
SEQRES  44 A  577  ASP PHE VAL ASN CYS SER THR LEU PRO ALA LEU ASN LEU          
SEQRES  45 A  577  ALA SER TRP ARG GLU                                          
SEQRES   1 B   60  ALA ASN PHE LEU GLU HIS GLU LEU SER TYR ILE ASP VAL          
SEQRES   2 B   60  LEU LEU ASP LYS ASN ALA ASP GLN ALA THR LYS ASP ASN          
SEQRES   3 B   60  LEU ARG SER TYR PHE ALA ASP LYS GLY LEU HIS SER ILE          
SEQRES   4 B   60  LYS ASP ILE ILE ASN LYS ALA LYS GLN ASP GLY PHE ASP          
SEQRES   5 B   60  VAL SER LYS TYR GLU HIS VAL LYS                              
MODRES 6AZP CSO A  316  CYS  MODIFIED RESIDUE                                   
HET    CSO  A 316       7                                                       
HET    NAG  A 801      14                                                       
HET    NAG  A 802      14                                                       
HET    NAG  A 803      14                                                       
HET    BMA  A 804      11                                                       
HET    NAG  A 805      14                                                       
HET     CA  A 806       1                                                       
HETNAM     CSO S-HYDROXYCYSTEINE                                                
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     BMA BETA-D-MANNOSE                                                   
HETNAM      CA CALCIUM ION                                                      
FORMUL   1  CSO    C3 H7 N O3 S                                                 
FORMUL   3  NAG    4(C8 H15 N O6)                                               
FORMUL   5  BMA    C6 H12 O6                                                    
FORMUL   7   CA    CA 2+                                                        
FORMUL   8  HOH   *282(H2 O)                                                    
HELIX    1 AA1 LEU A  226  VAL A  235  1                                  10    
HELIX    2 AA2 PRO A  238  LEU A  242  5                                   5    
HELIX    3 AA3 LEU A  250  ASP A  264  1                                  15    
HELIX    4 AA4 ALA A  270  PHE A  275  5                                   6    
HELIX    5 AA5 ALA A  339  GLY A  344  1                                   6    
HELIX    6 AA6 GLU A  346  LEU A  353  1                                   8    
HELIX    7 AA7 PRO A  386  ASN A  391  5                                   6    
HELIX    8 AA8 MET A  409  ASN A  434  1                                  26    
HELIX    9 AA9 ASP A  438  ASP A  461  1                                  24    
HELIX   10 AB1 ASP A  461  LEU A  476  1                                  16    
HELIX   11 AB2 ALA A  491  PHE A  498  1                                   8    
HELIX   12 AB3 ARG A  499  ILE A  505  5                                   7    
HELIX   13 AB4 SER A  528  VAL A  530  5                                   3    
HELIX   14 AB5 ALA A  533  GLU A  540  1                                   8    
HELIX   15 AB6 ILE A  543  THR A  553  1                                  11    
HELIX   16 AB7 VAL A  565  GLU A  570  1                                   6    
HELIX   17 AB8 PHE A  573  MET A  577  5                                   5    
HELIX   18 AB9 ASP A  582  HIS A  594  1                                  13    
HELIX   19 AC1 GLY A  598  GLY A  607  1                                  10    
HELIX   20 AC2 THR A  613  ARG A  622  1                                  10    
HELIX   21 AC3 ASN A  623  GLY A  635  1                                  13    
HELIX   22 AC4 THR A  636  ILE A  640  5                                   5    
HELIX   23 AC5 ASP A  641  GLU A  649  1                                   9    
HELIX   24 AC6 GLY A  658  GLY A  675  1                                  18    
HELIX   25 AC7 SER A  687  ALA A  695  1                                   9    
HELIX   26 AC8 SER A  698  THR A  707  1                                  10    
HELIX   27 AC9 SER A  731  LEU A  733  5                                   3    
HELIX   28 AD1 ASN A  737  ARG A  742  5                                   6    
HELIX   29 AD2 HIS B   51  LEU B   60  1                                  10    
HELIX   30 AD3 ASP B   65  ASP B   78  1                                  14    
HELIX   31 AD4 SER B   83  ASP B   94  1                                  12    
SHEET    1 AA1 2 ARG A 193  ALA A 194  0                                        
SHEET    2 AA1 2 ILE A 330  ASN A 331 -1  O  ASN A 331   N  ARG A 193           
SHEET    1 AA2 2 PRO A 244  SER A 249  0                                        
SHEET    2 AA2 2 PRO A 554  LYS A 556 -1  O  ALA A 555   N  ASP A 245           
SHEET    1 AA3 2 LEU A 294  LYS A 295  0                                        
SHEET    2 AA3 2 CYS A 309  ILE A 310 -1  O  ILE A 310   N  LEU A 294           
SHEET    1 AA4 2 GLN A 370  ASP A 371  0                                        
SHEET    2 AA4 2 ARG A 374  ALA A 375 -1  O  ARG A 374   N  ASP A 371           
SHEET    1 AA5 2 PHE A 508  PHE A 510  0                                        
SHEET    2 AA5 2 ARG A 524  PRO A 526 -1  O  VAL A 525   N  MET A 509           
SHEET    1 AA6 2 THR A 711  SER A 713  0                                        
SHEET    2 AA6 2 PHE A 727  ASN A 729 -1  O  VAL A 728   N  VAL A 712           
SSBOND   1 CYS A  167    CYS A  180                          1555   1555  1.99  
SSBOND   2 CYS A  281    CYS A  291                          1555   1555  2.02  
SSBOND   3 CYS A  285    CYS A  309                          1555   1555  2.04  
SSBOND   4 CYS A  387    CYS A  398                          1555   1555  2.08  
SSBOND   5 CYS A  606    CYS A  663                          1555   1555  2.05  
SSBOND   6 CYS A  704    CYS A  730                          1555   1555  2.05  
LINK         O   ASP A 262                CA    CA A 806     1555   1555  2.25  
LINK         OD1 ASP A 262                CA    CA A 806     1555   1555  2.26  
LINK         C   SER A 315                 N   CSO A 316     1555   1555  1.32  
LINK         C   CSO A 316                 N   PRO A 317     1555   1555  1.33  
LINK         O   THR A 334                CA    CA A 806     1555   1555  2.32  
LINK         OG1 THR A 334                CA    CA A 806     1555   1555  2.46  
LINK         O   PHE A 336                CA    CA A 806     1555   1555  2.29  
LINK         OD1 ASP A 338                CA    CA A 806     1555   1555  2.46  
LINK         OG  SER A 340                CA    CA A 806     1555   1555  1.96  
LINK         O4  NAG A 802                 C1  NAG A 803     1555   1555  1.42  
CISPEP   1 PRO A  289    PRO A  290          0         1.33                     
CISPEP   2 GLU A  520    PRO A  521          0         6.71                     
CISPEP   3 ASN A  715    ASN A  716          0         8.23                     
CISPEP   4 TYR A  723    PRO A  724          0         6.80                     
SITE     1 AC1  2 ARG A 480  ASN A 483                                          
SITE     1 AC2  2 GLN A 692  NAG A 803                                          
SITE     1 AC3  2 ASN A 391  TRP A 535                                          
SITE     1 AC4  5 ASP A 262  THR A 334  PHE A 336  ASP A 338                    
SITE     2 AC4  5 SER A 340                                                     
SITE     1 AC5  8 ASN A 355  ASN A 358  ALA A 364  VAL A 365                    
SITE     2 AC5  8 GLN A 367  BMA A 804  HOH A 906  HIS B  51                    
CRYST1  128.854   92.876   80.460  90.00 119.91  90.00 C 1 2 1       4          
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      0.007761  0.000000  0.004464        0.00000                         
SCALE2      0.000000  0.010767  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014338        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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