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Database: PDB
Entry: 6Q4R
LinkDB: 6Q4R
Original site: 6Q4R 
HEADER    HYDROLASE                               06-DEC-18   6Q4R              
TITLE     HIGH-RESOLUTION CRYSTAL STRUCTURE OF ERAP1 WITH BOUND PHOSPHINIC      
TITLE    2 TRANSITION-STATE ANALOGUE INHIBITOR                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ENDOPLASMIC RETICULUM AMINOPEPTIDASE 1,ENDOPLASMIC         
COMPND   3 RETICULUM AMINOPEPTIDASE 1;                                          
COMPND   4 CHAIN: A;                                                            
COMPND   5 SYNONYM: ARTS-1,ADIPOCYTE-DERIVED LEUCINE AMINOPEPTIDASE,A-LAP,      
COMPND   6 AMINOPEPTIDASE PILS,PUROMYCIN-INSENSITIVE LEUCYL-SPECIFIC            
COMPND   7 AMINOPEPTIDASE,PILS-AP,TYPE 1 TUMOR NECROSIS FACTOR RECEPTOR SHEDDING
COMPND   8 AMINOPEPTIDASE REGULATOR,ARTS-1,ADIPOCYTE-DERIVED LEUCINE            
COMPND   9 AMINOPEPTIDASE,A-LAP,AMINOPEPTIDASE PILS,PUROMYCIN-INSENSITIVE       
COMPND  10 LEUCYL-SPECIFIC AMINOPEPTIDASE,PILS-AP,TYPE 1 TUMOR NECROSIS FACTOR  
COMPND  11 RECEPTOR SHEDDING AMINOPEPTIDASE REGULATOR;                          
COMPND  12 EC: 3.4.11.-,3.4.11.-;                                               
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 OTHER_DETAILS: THE EXON 10 LOOP (25 AMINO ACIDS LONG) HAS BEEN       
COMPND  15 REPLACED BY THE TRIPEPTIDE GSG,THE EXON 10 LOOP (25 AMINO ACIDS LONG)
COMPND  16 HAS BEEN REPLACED BY THE TRIPEPTIDE GSG,THE EXON 10 LOOP (25 AMINO   
COMPND  17 ACIDS LONG) HAS BEEN REPLACED BY THE TRIPEPTIDE GSG,THE EXON 10 LOOP 
COMPND  18 (25 AMINO ACIDS LONG) HAS BEEN REPLACED BY THE TRIPEPTIDE GSG        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: ERAP1, APPILS, ARTS1, KIAA0525, UNQ584/PRO1154;                
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: SF9                                     
KEYWDS    ENDOPLASMIC RETICULUM AMINOPEPTIDASE 1, ERAP1, ANTIGEN PRESENTATION,  
KEYWDS   2 HYDROLASE                                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.GIASTAS,M.NEU,P.ROWLAND,E.STRATIKOS                                 
REVDAT   2   29-MAY-19 6Q4R    1       JRNL                                     
REVDAT   1   10-APR-19 6Q4R    0                                                
JRNL        AUTH   P.GIASTAS,M.NEU,P.ROWLAND,E.STRATIKOS                        
JRNL        TITL   HIGH-RESOLUTION CRYSTAL STRUCTURE OF ENDOPLASMIC RETICULUM   
JRNL        TITL 2 AMINOPEPTIDASE 1 WITH BOUND PHOSPHINIC TRANSITION-STATE      
JRNL        TITL 3 ANALOGUE INHIBITOR.                                          
JRNL        REF    ACS MED.CHEM.LETT.            V.  10   708 2019              
JRNL        REFN                   ISSN 1948-5875                               
JRNL        PMID   31097987                                                     
JRNL        DOI    10.1021/ACSMEDCHEMLETT.9B00002                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.11.1_2575: ???)                            
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 : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 91.45                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 130934                         
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) : 0.180                           
REMARK   3   FREE R VALUE                     : 0.213                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.960                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 6495                            
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 91.5986 -  4.9713    0.99     4466   240  0.1711 0.1919        
REMARK   3     2  4.9713 -  3.9458    1.00     4294   209  0.1334 0.1559        
REMARK   3     3  3.9458 -  3.4470    1.00     4219   226  0.1395 0.1646        
REMARK   3     4  3.4470 -  3.1319    1.00     4246   213  0.1507 0.1938        
REMARK   3     5  3.1319 -  2.9074    1.00     4187   231  0.1555 0.1713        
REMARK   3     6  2.9074 -  2.7359    1.00     4203   209  0.1575 0.1924        
REMARK   3     7  2.7359 -  2.5989    1.00     4188   210  0.1580 0.2050        
REMARK   3     8  2.5989 -  2.4858    1.00     4185   206  0.1590 0.2095        
REMARK   3     9  2.4858 -  2.3901    1.00     4162   208  0.1617 0.2065        
REMARK   3    10  2.3901 -  2.3076    1.00     4123   238  0.1601 0.2028        
REMARK   3    11  2.3076 -  2.2354    1.00     4150   230  0.1602 0.1994        
REMARK   3    12  2.2354 -  2.1715    1.00     4178   201  0.1673 0.2143        
REMARK   3    13  2.1715 -  2.1144    1.00     4162   207  0.2029 0.2291        
REMARK   3    14  2.1144 -  2.0628    0.99     4081   220  0.2175 0.2675        
REMARK   3    15  2.0628 -  2.0159    0.99     4172   219  0.2171 0.2408        
REMARK   3    16  2.0159 -  1.9730    0.99     4088   215  0.2241 0.2695        
REMARK   3    17  1.9730 -  1.9335    1.00     4146   202  0.2243 0.2463        
REMARK   3    18  1.9335 -  1.8970    0.99     4114   240  0.2305 0.2744        
REMARK   3    19  1.8970 -  1.8631    1.00     4055   217  0.2366 0.2768        
REMARK   3    20  1.8631 -  1.8315    0.99     4151   216  0.2575 0.2846        
REMARK   3    21  1.8315 -  1.8020    1.00     4086   230  0.2582 0.2883        
REMARK   3    22  1.8020 -  1.7743    0.99     4112   217  0.2695 0.2454        
REMARK   3    23  1.7743 -  1.7482    0.99     4076   210  0.2862 0.3469        
REMARK   3    24  1.7482 -  1.7235    0.98     4089   215  0.2970 0.3412        
REMARK   3    25  1.7235 -  1.7003    1.00     4121   212  0.3077 0.3549        
REMARK   3    26  1.7003 -  1.6782    0.98     4066   230  0.2937 0.3349        
REMARK   3    27  1.6782 -  1.6572    1.00     4094   194  0.2995 0.3270        
REMARK   3    28  1.6572 -  1.6372    0.98     4083   202  0.3058 0.3639        
REMARK   3    29  1.6372 -  1.6182    0.99     4095   218  0.3123 0.3355        
REMARK   3    30  1.6182 -  1.6000    0.99     4047   210  0.3242 0.3354        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
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)     : 0.230            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.470           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
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      :  0.006           7601                                  
REMARK   3   ANGLE     :  0.850          10299                                  
REMARK   3   CHIRALITY :  0.052           1154                                  
REMARK   3   PLANARITY :  0.005           1278                                  
REMARK   3   DIHEDRAL  : 12.217           4608                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 45 THROUGH 452 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):-619.6880 377.3836 444.9767              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2256 T22:   0.1593                                     
REMARK   3      T33:   0.1300 T12:   0.0493                                     
REMARK   3      T13:   0.0017 T23:  -0.0046                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7331 L22:   0.6786                                     
REMARK   3      L33:   1.0321 L12:  -0.2968                                     
REMARK   3      L13:   0.2826 L23:  -0.4502                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1420 S12:   0.1507 S13:  -0.0155                       
REMARK   3      S21:  -0.2322 S22:  -0.0796 S23:   0.0148                       
REMARK   3      S31:   0.1329 S32:   0.0259 S33:  -0.0441                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 453 THROUGH 669 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):-601.5766 367.5593 475.2995              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1330 T22:   0.1584                                     
REMARK   3      T33:   0.1836 T12:   0.0001                                     
REMARK   3      T13:  -0.0096 T23:   0.0145                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6692 L22:   0.4450                                     
REMARK   3      L33:   0.5462 L12:  -0.2982                                     
REMARK   3      L13:   0.3946 L23:  -0.1770                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0356 S12:  -0.0143 S13:  -0.0005                       
REMARK   3      S21:  -0.0344 S22:  -0.0429 S23:  -0.0665                       
REMARK   3      S31:   0.0117 S32:   0.0015 S33:   0.0070                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 670 THROUGH 937 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):-627.3101 386.7351 475.5869              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1161 T22:   0.1706                                     
REMARK   3      T33:   0.1524 T12:   0.0000                                     
REMARK   3      T13:   0.0122 T23:  -0.0028                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4569 L22:   1.0179                                     
REMARK   3      L33:   0.1811 L12:   0.0581                                     
REMARK   3      L13:   0.0478 L23:  -0.1348                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0098 S12:  -0.0539 S13:   0.0677                       
REMARK   3      S21:   0.0155 S22:   0.0335 S23:   0.1232                       
REMARK   3      S31:  -0.0338 S32:  -0.0468 S33:  -0.0212                       
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 6Q4R COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 07-DEC-18.                  
REMARK 100 THE DEPOSITION ID IS D_1200013300.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-JUN-18                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PETRA III, EMBL C/O DESY           
REMARK 200  BEAMLINE                       : P13 (MX1)                          
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.987                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 130971                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 91.450                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 5.600                              
REMARK 200  R MERGE                    (I) : 0.11720                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.9500                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 2YD0                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.45                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM DL-MALIC ACID, BIS-TRIS           
REMARK 280  PROPANE, PH 7.0, 25% PEG 1500, VAPOR DIFFUSION, SITTING DROP,       
REMARK 280  TEMPERATURE 289K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 2 21 21                        
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+1/2,-Z+1/2                                         
REMARK 290       4555   -X,-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       58.33450            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       73.63350            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       58.33450            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       73.63350            
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 10170 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 32520 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 96.0 KCAL/MOL                         
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 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 A1907  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     MET A     1                                                      
REMARK 465     VAL A     2                                                      
REMARK 465     PHE A     3                                                      
REMARK 465     LEU A     4                                                      
REMARK 465     PRO A     5                                                      
REMARK 465     LEU A     6                                                      
REMARK 465     LYS A     7                                                      
REMARK 465     TRP A     8                                                      
REMARK 465     SER A     9                                                      
REMARK 465     LEU A    10                                                      
REMARK 465     ALA A    11                                                      
REMARK 465     THR A    12                                                      
REMARK 465     MET A    13                                                      
REMARK 465     SER A    14                                                      
REMARK 465     PHE A    15                                                      
REMARK 465     LEU A    16                                                      
REMARK 465     LEU A    17                                                      
REMARK 465     SER A    18                                                      
REMARK 465     SER A    19                                                      
REMARK 465     LEU A    20                                                      
REMARK 465     LEU A    21                                                      
REMARK 465     ALA A    22                                                      
REMARK 465     LEU A    23                                                      
REMARK 465     LEU A    24                                                      
REMARK 465     THR A    25                                                      
REMARK 465     VAL A    26                                                      
REMARK 465     SER A    27                                                      
REMARK 465     THR A    28                                                      
REMARK 465     PRO A    29                                                      
REMARK 465     SER A    30                                                      
REMARK 465     TRP A    31                                                      
REMARK 465     CYS A    32                                                      
REMARK 465     GLN A    33                                                      
REMARK 465     SER A    34                                                      
REMARK 465     THR A    35                                                      
REMARK 465     GLU A    36                                                      
REMARK 465     ALA A    37                                                      
REMARK 465     SER A    38                                                      
REMARK 465     PRO A    39                                                      
REMARK 465     LYS A    40                                                      
REMARK 465     ARG A    41                                                      
REMARK 465     SER A    42                                                      
REMARK 465     ASP A    43                                                      
REMARK 465     GLY A    44                                                      
REMARK 465     GLY A   110                                                      
REMARK 465     ALA A   111                                                      
REMARK 465     GLY A   112                                                      
REMARK 465     GLU A   113                                                      
REMARK 465     GLY A   511                                                      
REMARK 465     SER A   512                                                      
REMARK 465     GLY A   513                                                      
REMARK 465     GLY A   514                                                      
REMARK 465     SER A   553                                                      
REMARK 465     ASP A   554                                                      
REMARK 465     GLY A   555                                                      
REMARK 465     ALA A   556                                                      
REMARK 465     PRO A   557                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A 114    CG   CD   NE   CZ   NH1  NH2                        
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     ILE A  711   CA   CB   CG1  CG2  CD1                             
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A  1225     O    HOH A  1568              1.99            
REMARK 500   O    HOH A  1756     O    HOH A  1893              1.99            
REMARK 500   O    HOH A  1908     O    HOH A  1912              2.00            
REMARK 500   O    HOH A  1789     O    HOH A  1820              2.00            
REMARK 500   O    HOH A  1555     O    HOH A  1830              2.03            
REMARK 500   O    HOH A  1337     O    HOH A  1673              2.05            
REMARK 500   O    HOH A  1240     O    HOH A  1461              2.09            
REMARK 500   O    HOH A  1766     O    HOH A  1857              2.11            
REMARK 500   O    HOH A  1587     O    HOH A  1716              2.13            
REMARK 500   O    HOH A  1709     O    HOH A  1806              2.14            
REMARK 500   O    HOH A  1409     O    HOH A  1485              2.14            
REMARK 500   NZ   LYS A   223     O    HOH A  1105              2.17            
REMARK 500   O    HOH A  1139     O    HOH A  1833              2.18            
REMARK 500   O    HOH A  1544     O    HOH A  1712              2.18            
REMARK 500   O    HOH A  1435     O    HOH A  1699              2.18            
REMARK 500   OG   SER A   343     O    HOH A  1106              2.19            
REMARK 500   O    HOH A  1531     O    HOH A  1559              2.19            
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    THR A 158     -158.12    -95.69                                   
REMARK 500    SER A 316     -167.11    -79.77                                   
REMARK 500    ASN A 362      -61.23    -90.02                                   
REMARK 500    GLU A 424      -54.41   -135.71                                   
REMARK 500    SER A 453      146.04     90.90                                   
REMARK 500    ASN A 601       71.15     68.47                                   
REMARK 500    ASP A 614     -128.67     64.43                                   
REMARK 500    MET A 692       40.68   -140.01                                   
REMARK 500    GLU A 865      135.13     89.78                                   
REMARK 500    SER A 883       28.74   -149.63                                   
REMARK 500    LYS A 899     -122.15     49.65                                   
REMARK 500    ASN A 901       40.29   -100.42                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A1909        DISTANCE =  5.81 ANGSTROMS                       
REMARK 525    HOH A1910        DISTANCE =  5.88 ANGSTROMS                       
REMARK 525    HOH A1911        DISTANCE =  6.01 ANGSTROMS                       
REMARK 525    HOH A1912        DISTANCE =  6.11 ANGSTROMS                       
REMARK 525    HOH A1913        DISTANCE =  6.16 ANGSTROMS                       
REMARK 525    HOH A1914        DISTANCE =  7.01 ANGSTROMS                       
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                              NA A1045  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER A 316   OG                                                     
REMARK 620 2 HOH A1401   O   151.1                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1008  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 353   NE2                                                    
REMARK 620 2 HIS A 357   NE2 103.1                                              
REMARK 620 3 GLU A 376   OE1 115.1 104.3                                        
REMARK 620 4 HJ5 A1009   O13 106.1 131.0  97.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A1046  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 431   OE2                                                    
REMARK 620 2 HOH A1600   O   112.4                                              
REMARK 620 3 HOH A1853   O   102.0 110.3                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A1044  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER A 870   OG                                                     
REMARK 620 2 HOH A1489   O    61.8                                              
REMARK 620 N                    1                                               
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 1007                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1008                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HJ5 A 1009                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue B3P A 1010                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 1011                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 1012                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 1013                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 1014                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 1015                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 1016                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 1017                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 1018                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 1019                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 1020                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 1021                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 1022                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 1023                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 1024                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 1025                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 1026                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 1027                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 1028                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 1029                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 1030                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 1031                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 1032                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 1033                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 1034                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 1035                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 1036                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 1037                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 1038                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 1039                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 1040                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MLT A 1041                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue P6G A 1042                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PG4 A 1043                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 1044                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 1045                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 1046                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  1003 through BMA A 1005 bound to ASN A 70                           
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  1001 through NAG A 1002 bound to ASN A 154                          
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 1006        
REMARK 800  bound to ASN A 414                                                  
DBREF  6Q4R A    1   485  UNP    Q9NZ08   ERAP1_HUMAN      1    485             
DBREF  6Q4R A  514   937  UNP    Q9NZ08   ERAP1_HUMAN    514    937             
SEQADV 6Q4R GLY A  511  UNP  Q9NZ08              LINKER                         
SEQADV 6Q4R SER A  512  UNP  Q9NZ08              LINKER                         
SEQADV 6Q4R GLY A  513  UNP  Q9NZ08              LINKER                         
SEQRES   1 A  912  MET VAL PHE LEU PRO LEU LYS TRP SER LEU ALA THR MET          
SEQRES   2 A  912  SER PHE LEU LEU SER SER LEU LEU ALA LEU LEU THR VAL          
SEQRES   3 A  912  SER THR PRO SER TRP CYS GLN SER THR GLU ALA SER PRO          
SEQRES   4 A  912  LYS ARG SER ASP GLY THR PRO PHE PRO TRP ASN LYS ILE          
SEQRES   5 A  912  ARG LEU PRO GLU TYR VAL ILE PRO VAL HIS TYR ASP LEU          
SEQRES   6 A  912  LEU ILE HIS ALA ASN LEU THR THR LEU THR PHE TRP GLY          
SEQRES   7 A  912  THR THR LYS VAL GLU ILE THR ALA SER GLN PRO THR SER          
SEQRES   8 A  912  THR ILE ILE LEU HIS SER HIS HIS LEU GLN ILE SER ARG          
SEQRES   9 A  912  ALA THR LEU ARG LYS GLY ALA GLY GLU ARG LEU SER GLU          
SEQRES  10 A  912  GLU PRO LEU GLN VAL LEU GLU HIS PRO ARG GLN GLU GLN          
SEQRES  11 A  912  ILE ALA LEU LEU ALA PRO GLU PRO LEU LEU VAL GLY LEU          
SEQRES  12 A  912  PRO TYR THR VAL VAL ILE HIS TYR ALA GLY ASN LEU SER          
SEQRES  13 A  912  GLU THR PHE HIS GLY PHE TYR LYS SER THR TYR ARG THR          
SEQRES  14 A  912  LYS GLU GLY GLU LEU ARG ILE LEU ALA SER THR GLN PHE          
SEQRES  15 A  912  GLU PRO THR ALA ALA ARG MET ALA PHE PRO CYS PHE ASP          
SEQRES  16 A  912  GLU PRO ALA PHE LYS ALA SER PHE SER ILE LYS ILE ARG          
SEQRES  17 A  912  ARG GLU PRO ARG HIS LEU ALA ILE SER ASN MET PRO LEU          
SEQRES  18 A  912  VAL LYS SER VAL THR VAL ALA GLU GLY LEU ILE GLU ASP          
SEQRES  19 A  912  HIS PHE ASP VAL THR VAL LYS MET SER THR TYR LEU VAL          
SEQRES  20 A  912  ALA PHE ILE ILE SER ASP PHE GLU SER VAL SER LYS ILE          
SEQRES  21 A  912  THR LYS SER GLY VAL LYS VAL SER VAL TYR ALA VAL PRO          
SEQRES  22 A  912  ASP LYS ILE ASN GLN ALA ASP TYR ALA LEU ASP ALA ALA          
SEQRES  23 A  912  VAL THR LEU LEU GLU PHE TYR GLU ASP TYR PHE SER ILE          
SEQRES  24 A  912  PRO TYR PRO LEU PRO LYS GLN ASP LEU ALA ALA ILE PRO          
SEQRES  25 A  912  ASP PHE GLN SER GLY ALA MET GLU ASN TRP GLY LEU THR          
SEQRES  26 A  912  THR TYR ARG GLU SER ALA LEU LEU PHE ASP ALA GLU LYS          
SEQRES  27 A  912  SER SER ALA SER SER LYS LEU GLY ILE THR MET THR VAL          
SEQRES  28 A  912  ALA HIS GLU LEU ALA HIS GLN TRP PHE GLY ASN LEU VAL          
SEQRES  29 A  912  THR MET GLU TRP TRP ASN ASP LEU TRP LEU ASN GLU GLY          
SEQRES  30 A  912  PHE ALA LYS PHE MET GLU PHE VAL SER VAL SER VAL THR          
SEQRES  31 A  912  HIS PRO GLU LEU LYS VAL GLY ASP TYR PHE PHE GLY LYS          
SEQRES  32 A  912  CYS PHE ASP ALA MET GLU VAL ASP ALA LEU ASN SER SER          
SEQRES  33 A  912  HIS PRO VAL SER THR PRO VAL GLU ASN PRO ALA GLN ILE          
SEQRES  34 A  912  ARG GLU MET PHE ASP ASP VAL SER TYR ASP LYS GLY ALA          
SEQRES  35 A  912  CYS ILE LEU ASN MET LEU ARG GLU TYR LEU SER ALA ASP          
SEQRES  36 A  912  ALA PHE LYS SER GLY ILE VAL GLN TYR LEU GLN LYS HIS          
SEQRES  37 A  912  SER TYR LYS ASN THR LYS ASN GLU ASP LEU TRP ASP SER          
SEQRES  38 A  912  MET ALA SER ILE GLY SER GLY GLY VAL ASP VAL LYS THR          
SEQRES  39 A  912  MET MET ASN THR TRP THR LEU GLN LYS GLY PHE PRO LEU          
SEQRES  40 A  912  ILE THR ILE THR VAL ARG GLY ARG ASN VAL HIS MET LYS          
SEQRES  41 A  912  GLN GLU HIS TYR MET LYS GLY SER ASP GLY ALA PRO ASP          
SEQRES  42 A  912  THR GLY TYR LEU TRP HIS VAL PRO LEU THR PHE ILE THR          
SEQRES  43 A  912  SER LYS SER ASP MET VAL HIS ARG PHE LEU LEU LYS THR          
SEQRES  44 A  912  LYS THR ASP VAL LEU ILE LEU PRO GLU GLU VAL GLU TRP          
SEQRES  45 A  912  ILE LYS PHE ASN VAL GLY MET ASN GLY TYR TYR ILE VAL          
SEQRES  46 A  912  HIS TYR GLU ASP ASP GLY TRP ASP SER LEU THR GLY LEU          
SEQRES  47 A  912  LEU LYS GLY THR HIS THR ALA VAL SER SER ASN ASP ARG          
SEQRES  48 A  912  ALA SER LEU ILE ASN ASN ALA PHE GLN LEU VAL SER ILE          
SEQRES  49 A  912  GLY LYS LEU SER ILE GLU LYS ALA LEU ASP LEU SER LEU          
SEQRES  50 A  912  TYR LEU LYS HIS GLU THR GLU ILE MET PRO VAL PHE GLN          
SEQRES  51 A  912  GLY LEU ASN GLU LEU ILE PRO MET TYR LYS LEU MET GLU          
SEQRES  52 A  912  LYS ARG ASP MET ASN GLU VAL GLU THR GLN PHE LYS ALA          
SEQRES  53 A  912  PHE LEU ILE ARG LEU LEU ARG ASP LEU ILE ASP LYS GLN          
SEQRES  54 A  912  THR TRP THR ASP GLU GLY SER VAL SER GLU ARG MET LEU          
SEQRES  55 A  912  ARG SER GLN LEU LEU LEU LEU ALA CYS VAL HIS ASN TYR          
SEQRES  56 A  912  GLN PRO CYS VAL GLN ARG ALA GLU GLY TYR PHE ARG LYS          
SEQRES  57 A  912  TRP LYS GLU SER ASN GLY ASN LEU SER LEU PRO VAL ASP          
SEQRES  58 A  912  VAL THR LEU ALA VAL PHE ALA VAL GLY ALA GLN SER THR          
SEQRES  59 A  912  GLU GLY TRP ASP PHE LEU TYR SER LYS TYR GLN PHE SER          
SEQRES  60 A  912  LEU SER SER THR GLU LYS SER GLN ILE GLU PHE ALA LEU          
SEQRES  61 A  912  CYS ARG THR GLN ASN LYS GLU LYS LEU GLN TRP LEU LEU          
SEQRES  62 A  912  ASP GLU SER PHE LYS GLY ASP LYS ILE LYS THR GLN GLU          
SEQRES  63 A  912  PHE PRO GLN ILE LEU THR LEU ILE GLY ARG ASN PRO VAL          
SEQRES  64 A  912  GLY TYR PRO LEU ALA TRP GLN PHE LEU ARG LYS ASN TRP          
SEQRES  65 A  912  ASN LYS LEU VAL GLN LYS PHE GLU LEU GLY SER SER SER          
SEQRES  66 A  912  ILE ALA HIS MET VAL MET GLY THR THR ASN GLN PHE SER          
SEQRES  67 A  912  THR ARG THR ARG LEU GLU GLU VAL LYS GLY PHE PHE SER          
SEQRES  68 A  912  SER LEU LYS GLU ASN GLY SER GLN LEU ARG CYS VAL GLN          
SEQRES  69 A  912  GLN THR ILE GLU THR ILE GLU GLU ASN ILE GLY TRP MET          
SEQRES  70 A  912  ASP LYS ASN PHE ASP LYS ILE ARG VAL TRP LEU GLN SER          
SEQRES  71 A  912  GLU LYS                                                      
HET    NAG  A1001      14                                                       
HET    NAG  A1002      14                                                       
HET    NAG  A1003      14                                                       
HET    NAG  A1004      14                                                       
HET    BMA  A1005      11                                                       
HET    NAG  A1006      14                                                       
HET    NAG  A1007      14                                                       
HET     ZN  A1008       1                                                       
HET    HJ5  A1009      63                                                       
HET    B3P  A1010      45                                                       
HET    EDO  A1011      10                                                       
HET    EDO  A1012      10                                                       
HET    EDO  A1013      10                                                       
HET    EDO  A1014      10                                                       
HET    EDO  A1015      10                                                       
HET    EDO  A1016      10                                                       
HET    EDO  A1017      10                                                       
HET    EDO  A1018      10                                                       
HET    EDO  A1019      10                                                       
HET    EDO  A1020      10                                                       
HET    EDO  A1021      10                                                       
HET    EDO  A1022      10                                                       
HET    EDO  A1023      10                                                       
HET    EDO  A1024      10                                                       
HET    EDO  A1025      10                                                       
HET    EDO  A1026      10                                                       
HET    EDO  A1027      10                                                       
HET    EDO  A1028      10                                                       
HET    EDO  A1029      10                                                       
HET    EDO  A1030      10                                                       
HET    EDO  A1031      10                                                       
HET    EDO  A1032      10                                                       
HET    EDO  A1033      10                                                       
HET    EDO  A1034      10                                                       
HET    EDO  A1035      10                                                       
HET    EDO  A1036      10                                                       
HET    EDO  A1037      10                                                       
HET    EDO  A1038      10                                                       
HET    EDO  A1039      10                                                       
HET    EDO  A1040      10                                                       
HET    MLT  A1041      13                                                       
HET    P6G  A1042      45                                                       
HET    PG4  A1043      31                                                       
HET     NA  A1044       1                                                       
HET     NA  A1045       1                                                       
HET     NA  A1046       1                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     BMA BETA-D-MANNOSE                                                   
HETNAM      ZN ZINC ION                                                         
HETNAM     HJ5 [(1~{R})-1-[[(2~{S})-2-[[(2~{S})-1-AZANIUMYL-1-                  
HETNAM   2 HJ5  OXIDANYLIDENE-3-PHENYL-PROPAN-2-YL]CARBAMOYL]PENT-4-            
HETNAM   3 HJ5  YNYL]-OXIDANYL-PHOSPHORYL]-3-PHENYL-PROPYL]AZANIUM              
HETNAM     B3P 2-[3-(2-HYDROXY-1,1-DIHYDROXYMETHYL-ETHYLAMINO)-                 
HETNAM   2 B3P  PROPYLAMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL                   
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     MLT D-MALATE                                                         
HETNAM     P6G HEXAETHYLENE GLYCOL                                              
HETNAM     PG4 TETRAETHYLENE GLYCOL                                             
HETNAM      NA SODIUM ION                                                       
HETSYN     EDO ETHYLENE GLYCOL                                                  
HETSYN     MLT (2R)-2-HYDROXYBUTANEDIOIC ACID; 2-HYDROXY-SUCCINIC ACID          
HETSYN     P6G POLYETHYLENE GLYCOL PEG400                                       
FORMUL   2  NAG    6(C8 H15 N O6)                                               
FORMUL   3  BMA    C6 H12 O6                                                    
FORMUL   6   ZN    ZN 2+                                                        
FORMUL   7  HJ5    C24 H32 N3 O4 P 2+                                           
FORMUL   8  B3P    C11 H26 N2 O6                                                
FORMUL   9  EDO    30(C2 H6 O2)                                                 
FORMUL  39  MLT    C4 H6 O5                                                     
FORMUL  40  P6G    C12 H26 O7                                                   
FORMUL  41  PG4    C8 H18 O5                                                    
FORMUL  42   NA    3(NA 1+)                                                     
FORMUL  45  HOH   *814(H2 O)                                                    
HELIX    1 AA1 ALA A  186  ALA A  190  5                                   5    
HELIX    2 AA2 SER A  243  VAL A  247  5                                   5    
HELIX    3 AA3 VAL A  272  GLN A  278  5                                   7    
HELIX    4 AA4 ALA A  279  SER A  298  1                                  20    
HELIX    5 AA5 SER A  330  LEU A  332  5                                   3    
HELIX    6 AA6 SER A  340  GLN A  358  1                                  19    
HELIX    7 AA7 TRP A  368  ASP A  371  5                                   4    
HELIX    8 AA8 LEU A  372  HIS A  391  1                                  20    
HELIX    9 AA9 PRO A  392  TYR A  399  5                                   8    
HELIX   10 AB1 PHE A  400  ALA A  412  1                                  13    
HELIX   11 AB2 ASN A  425  MET A  432  1                                   8    
HELIX   12 AB3 ASP A  434  SER A  453  1                                  20    
HELIX   13 AB4 SER A  453  HIS A  468  1                                  16    
HELIX   14 AB5 LYS A  474  SER A  484  1                                  11    
HELIX   15 AB6 ASP A  516  LEU A  526  1                                  11    
HELIX   16 AB7 VAL A  602  ASN A  605  5                                   4    
HELIX   17 AB8 ASP A  615  THR A  627  1                                  13    
HELIX   18 AB9 HIS A  628  VAL A  631  5                                   4    
HELIX   19 AC1 SER A  632  ILE A  649  1                                  18    
HELIX   20 AC2 SER A  653  LEU A  662  1                                  10    
HELIX   21 AC3 TYR A  663  GLU A  667  5                                   5    
HELIX   22 AC4 GLU A  669  LYS A  689  1                                  21    
HELIX   23 AC5 MET A  692  GLN A  714  1                                  23    
HELIX   24 AC6 SER A  721  HIS A  738  1                                  18    
HELIX   25 AC7 TYR A  740  SER A  757  1                                  18    
HELIX   26 AC8 PRO A  764  ALA A  776  1                                  13    
HELIX   27 AC9 SER A  778  GLN A  790  1                                  13    
HELIX   28 AD1 SER A  794  CYS A  806  1                                  13    
HELIX   29 AD2 ASN A  810  GLY A  824  1                                  15    
HELIX   30 AD3 LYS A  828  GLN A  830  5                                   3    
HELIX   31 AD4 GLU A  831  ASN A  842  1                                  12    
HELIX   32 AD5 GLY A  845  ASN A  856  1                                  12    
HELIX   33 AD6 ASN A  856  GLU A  865  1                                  10    
HELIX   34 AD7 SER A  868  ASN A  880  1                                  13    
HELIX   35 AD8 THR A  884  SER A  897  1                                  14    
HELIX   36 AD9 LEU A  898  GLY A  902  5                                   5    
HELIX   37 AE1 LEU A  905  LYS A  937  1                                  33    
SHEET    1 AA1 8 SER A 116  PRO A 119  0                                        
SHEET    2 AA1 8 GLN A 101  LYS A 109 -1  N  LEU A 107   O  GLU A 118           
SHEET    3 AA1 8 TYR A 145  ASN A 154 -1  O  THR A 146   N  ARG A 108           
SHEET    4 AA1 8 THR A  75  ALA A  86 -1  N  THR A  80   O  ILE A 149           
SHEET    5 AA1 8 VAL A  58  ASN A  70 -1  N  ASN A  70   O  THR A  75           
SHEET    6 AA1 8 SER A 202  ARG A 209  1  O  SER A 204   N  LEU A  65           
SHEET    7 AA1 8 LEU A 231  PHE A 236 -1  O  ASP A 234   N  ILE A 207           
SHEET    8 AA1 8 LEU A 221  ALA A 228 -1  N  LYS A 223   O  HIS A 235           
SHEET    1 AA2 3 THR A  92  HIS A  96  0                                        
SHEET    2 AA2 3 GLN A 130  LEU A 134 -1  O  LEU A 133   N  ILE A  93           
SHEET    3 AA2 3 GLN A 121  HIS A 125 -1  N  LEU A 123   O  ALA A 132           
SHEET    1 AA3 2 GLY A 161  ARG A 168  0                                        
SHEET    2 AA3 2 LEU A 174  GLN A 181 -1  O  ARG A 175   N  TYR A 167           
SHEET    1 AA4 2 LEU A 214  SER A 217  0                                        
SHEET    2 AA4 2 PHE A 249  SER A 252 -1  O  SER A 252   N  LEU A 214           
SHEET    1 AA5 5 GLU A 255  ILE A 260  0                                        
SHEET    2 AA5 5 LYS A 266  ALA A 271 -1  O  VAL A 267   N  LYS A 259           
SHEET    3 AA5 5 LYS A 305  ILE A 311  1  O  LEU A 308   N  TYR A 270           
SHEET    4 AA5 5 LEU A 324  ARG A 328  1  O  TYR A 327   N  ILE A 311           
SHEET    5 AA5 5 ALA A 318  MET A 319 -1  N  MET A 319   O  THR A 326           
SHEET    1 AA6 2 VAL A 364  MET A 366  0                                        
SHEET    2 AA6 2 LYS A 471  THR A 473  1  O  THR A 473   N  THR A 365           
SHEET    1 AA7 4 THR A 586  ILE A 590  0                                        
SHEET    2 AA7 4 ASN A 541  HIS A 548 -1  N  VAL A 542   O  LEU A 589           
SHEET    3 AA7 4 PRO A 531  ARG A 538 -1  N  LEU A 532   O  GLU A 547           
SHEET    4 AA7 4 ILE A 609  TYR A 612  1  O  HIS A 611   N  ILE A 535           
SHEET    1 AA8 3 SER A 574  LEU A 582  0                                        
SHEET    2 AA8 3 VAL A 565  THR A 571 -1  N  VAL A 565   O  LEU A 582           
SHEET    3 AA8 3 ILE A 598  PHE A 600 -1  O  LYS A 599   N  ILE A 570           
SSBOND   1 CYS A  404    CYS A  443                          1555   1555  2.04  
SSBOND   2 CYS A  736    CYS A  743                          1555   1555  2.07  
LINK         ND2 ASN A  70                 C1  NAG A1003     1555   1555  1.44  
LINK         ND2 ASN A 154                 C1  NAG A1001     1555   1555  1.45  
LINK         OG ASER A 316                NA    NA A1045     1555   1555  2.94  
LINK         NE2 HIS A 353                ZN    ZN A1008     1555   1555  2.03  
LINK         NE2 HIS A 357                ZN    ZN A1008     1555   1555  2.07  
LINK         OE1 GLU A 376                ZN    ZN A1008     1555   1555  1.94  
LINK         ND2 ASN A 414                 C1  NAG A1006     1555   1555  1.44  
LINK         OE2 GLU A 431                NA    NA A1046     1555   1555  2.83  
LINK         ND2 ASN A 760                 C1  NAG A1007     1555   1555  1.45  
LINK         OG  SER A 870                NA    NA A1044     1555   1555  3.00  
LINK         O4  NAG A1001                 C1  NAG A1002     1555   1555  1.44  
LINK         O4  NAG A1003                 C1  NAG A1004     1555   1555  1.44  
LINK         O4  NAG A1004                 C1  BMA A1005     1555   1555  1.44  
LINK        ZN    ZN A1008                 O13 HJ5 A1009     1555   1555  1.91  
LINK        NA    NA A1044                 O   HOH A1489     1555   1555  3.02  
LINK        NA    NA A1045                 O   HOH A1401     1555   1555  2.85  
LINK        NA    NA A1046                 O   HOH A1600     1555   1555  2.93  
LINK        NA    NA A1046                 O   HOH A1853     1555   1555  2.75  
CISPEP   1 GLU A  183    PRO A  184          0         1.77                     
SITE     1 AC1  5 LYS A 338  ASN A 760  SER A 762  HOH A1111                    
SITE     2 AC1  5 HOH A1620                                                     
SITE     1 AC2  4 HIS A 353  HIS A 357  GLU A 376  HJ5 A1009                    
SITE     1 AC3 17 GLU A 183  SER A 316  GLY A 317  ALA A 318                    
SITE     2 AC3 17 GLU A 320  HIS A 353  GLU A 354  HIS A 357                    
SITE     3 AC3 17 GLU A 376  PHE A 433  TYR A 438   ZN A1008                    
SITE     4 AC3 17 EDO A1030  EDO A1034   NA A1044  HOH A1257                    
SITE     5 AC3 17 HOH A1638                                                     
SITE     1 AC4 19 PHE A 405  ASP A 406  GLU A 409  LYS A 551                    
SITE     2 AC4 19 ASN A 641  SER A 648  GLN A 675  ASN A 678                    
SITE     3 AC4 19 GLU A 679  PRO A 682  TRP A 921  HOH A1136                    
SITE     4 AC4 19 HOH A1221  HOH A1325  HOH A1423  HOH A1433                    
SITE     5 AC4 19 HOH A1529  HOH A1580  HOH A1639                               
SITE     1 AC5  6 GLU A 129  THR A 185  PRO A 426  ARG A 430                    
SITE     2 AC5  6 GLU A 865  HOH A1268                                          
SITE     1 AC6  7 SER A 340  ALA A 341  SER A 342  ARG A 725                    
SITE     2 AC6  7 SER A 729  ASP A 766  EDO A1029                               
SITE     1 AC7  4 MET A 576  VAL A 577  ARG A 854  P6G A1042                    
SITE     1 AC8  4 LEU A 589  ILE A 590  EDO A1028  P6G A1042                    
SITE     1 AC9  9 ARG A 127  GLN A 128  GLU A 129  ARG A 188                    
SITE     2 AC9  9 PRO A 426  EDO A1020  HOH A1248  HOH A1522                    
SITE     3 AC9  9 HOH A1576                                                     
SITE     1 AD1  6 ASN A 154  LEU A 155  SER A 156  PHE A 162                    
SITE     2 AD1  6 MET A 189  HOH A1354                                          
SITE     1 AD2  8 LYS A 899  GLU A 900  GLY A 902  SER A 903                    
SITE     2 AD2  8 GLN A 904  LEU A 905  HOH A1169  HOH A1617                    
SITE     1 AD3  7 ASN A 370  ASP A 371  SER A 420  THR A 421                    
SITE     2 AD3  7 PRO A 422  HOH A1222  HOH A1517                               
SITE     1 AD4  9 PHE A 569  HIS A 578  LEU A 591  PRO A 592                    
SITE     2 AD4  9 THR A 886  GLU A 889  P6G A1042  HOH A1182                    
SITE     3 AD4  9 HOH A1382                                                     
SITE     1 AD5 10 ARG A 188  ASP A 195  TRP A 368  GLU A 424                    
SITE     2 AD5 10 ASN A 425  PRO A 426  ILE A 429  EDO A1015                    
SITE     3 AD5 10 HOH A1114  HOH A1159                                          
SITE     1 AD6  6 THR A 668  GLU A 669  ILE A 670  SER A 723                    
SITE     2 AD6  6 GLU A 724  HOH A1583                                          
SITE     1 AD7  7 THR A 421  VAL A 423  GLN A 428  GLU A 431                    
SITE     2 AD7  7 ARG A 906  HOH A1190  HOH A1374                               
SITE     1 AD8  4 ARG A 540  GLU A 593  GLU A 594  HOH A1240                    
SITE     1 AD9  3 ARG A 746  TYR A 750  HOH A1239                               
SITE     1 AE1  5 GLU A 688  ARG A 690  TYR A 846  HOH A1164                    
SITE     2 AE1  5 HOH A1348                                                     
SITE     1 AE2  6 LEU A  66  HIS A  68  TRP A  77  GLY A  78                    
SITE     2 AE2  6 THR A  79  HOH A1140                                          
SITE     1 AE3  5 LYS A 573  GLU A 593  ARG A 690  THR A 884                    
SITE     2 AE3  5 HOH A1109                                                     
SITE     1 AE4  2 EDO A1014  P6G A1042                                          
SITE     1 AE5  6 SER A 340  SER A 342  LEU A 769  GLN A 800                    
SITE     2 AE5  6 EDO A1012  HOH A1147                                          
SITE     1 AE6  8 PHE A 433  ASP A 434  ASP A 435  TYR A 438                    
SITE     2 AE6  8 SER A 869  HIS A 873  HJ5 A1009  HOH A1612                    
SITE     1 AE7  5 SER A 453  ARG A 854  ASN A 858  PHE A 894                    
SITE     2 AE7  5 HOH A1504                                                     
SITE     1 AE8  5 GLU A 367  LYS A 471  ASN A 472  HOH A1488                    
SITE     2 AE8  5 HOH A1532                                                     
SITE     1 AE9  3 ARG A 690  MET A 922  ASP A 923                               
SITE     1 AF1  5 GLN A 315  GLY A 317  ARG A 328  HJ5 A1009                    
SITE     2 AF1  5 HOH A1565                                                     
SITE     1 AF2  3 LEU A 677  ASN A 678  GLN A 730                               
SITE     1 AF3  6 HIS A  68  ASN A  70  THR A  75  TRP A  77                    
SITE     2 AF3  6 NAG A1003  HOH A1387                                          
SITE     1 AF4  2 TRP A  49  ASN A  50                                          
SITE     1 AF5  6 LYS A 338  LEU A 761  LEU A 763  GLU A 797                    
SITE     2 AF5  6 HOH A1127  HOH A1208                                          
SITE     1 AF6  5 SER A 416  HIS A 417  PRO A 418  ARG A 906                    
SITE     2 AF6  5 HOH A1162                                                     
SITE     1 AF7  3 ASN A 522  GLN A 527  HOH A1398                               
SITE     1 AF8  7 TYR A 684  LYS A 685  LEU A 733  ARG A 807                    
SITE     2 AF8  7 HOH A1102  HOH A1156  HOH A1247                               
SITE     1 AF9 13 PHE A 569  MET A 576  VAL A 577  HIS A 578                    
SITE     2 AF9 13 ARG A 579  GLU A 889  GLY A 893  EDO A1013                    
SITE     3 AF9 13 EDO A1014  EDO A1019  EDO A1028  HOH A1182                    
SITE     4 AF9 13 HOH A1376                                                     
SITE     1 AG1 13 MET A 447  GLU A 450  TYR A 451  PRO A 566                    
SITE     2 AG1 13 LEU A 567  THR A 568  ARG A 579  PHE A 580                    
SITE     3 AG1 13 LEU A 581  ASN A 601  GLY A 606  TYR A 608                    
SITE     4 AG1 13 HOH A1225                                                     
SITE     1 AG2  6 GLN A 315  SER A 868  SER A 869  SER A 870                    
SITE     2 AG2  6 HJ5 A1009  HOH A1489                                          
SITE     1 AG3  4 PHE A 314  GLN A 315  SER A 316  HOH A1401                    
SITE     1 AG4  5 GLU A 431  ARG A 906  CYS A 907  HOH A1600                    
SITE     2 AG4  5 HOH A1853                                                     
SITE     1 AG5  7 HIS A  68  ALA A  69  ASN A  70  GLU A 210                    
SITE     2 AG5  7 EDO A1036  HOH A1286  HOH A1527                               
SITE     1 AG6  6 HIS A  99  GLN A 101  ASN A 154  HOH A1176                    
SITE     2 AG6  6 HOH A1249  HOH A1284                                          
SITE     1 AG7  3 ASN A 414  MET A 550  HOH A1115                               
CRYST1   57.683  116.669  147.267  90.00  90.00  90.00 P 2 21 21     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      0.017336  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008571  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006790        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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