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Database: PDB
Entry: 5HCE
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HEADER    IMMUNE SYSTEM                           04-JAN-16   5HCE              
TITLE     TERNARY COMPLEX OF HUMAN COMPLEMENT C5 WITH ORNITHODOROS MOUBATA OMCI 
TITLE    2 AND RHIPICEPHALUS APPENDICULATUS RACI1                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: COMPLEMENT C5;                                             
COMPND   3 CHAIN: B;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 19-674;                                       
COMPND   5 SYNONYM: C3 AND PZP-LIKE ALPHA-2-MACROGLOBULIN DOMAIN-CONTAINING     
COMPND   6 PROTEIN 4;                                                           
COMPND   7 OTHER_DETAILS: CHAINS A AND B ARE THE PRODUCT OF A SINGLE GENE THAT  
COMPND   8 IS PROCESSED INTO TWO CHAINS THAT REMAIN COVALENTLY LINKED VIA A     
COMPND   9 DISULPHIDE.;                                                         
COMPND  10 MOL_ID: 2;                                                           
COMPND  11 MOLECULE: COMPLEMENT C5;                                             
COMPND  12 CHAIN: A;                                                            
COMPND  13 FRAGMENT: UNP RESIDUES 679-1676;                                     
COMPND  14 SYNONYM: C3 AND PZP-LIKE ALPHA-2-MACROGLOBULIN DOMAIN-CONTAINING     
COMPND  15 PROTEIN 4;                                                           
COMPND  16 OTHER_DETAILS: CHAINS A AND B ARE THE PRODUCT OF A SINGLE GENE THAT  
COMPND  17 IS PROCESSED INTO TWO CHAINS THAT REMAIN COVALENTLY LINKED VIA A     
COMPND  18 DISULPHIDE.;                                                         
COMPND  19 MOL_ID: 3;                                                           
COMPND  20 MOLECULE: COMPLEMENT INHIBITOR;                                      
COMPND  21 CHAIN: C;                                                            
COMPND  22 FRAGMENT: UNP RESIDUES 19-168;                                       
COMPND  23 ENGINEERED: YES;                                                     
COMPND  24 MUTATION: YES;                                                       
COMPND  25 MOL_ID: 4;                                                           
COMPND  26 MOLECULE: RHIPICEPHALUS APPENDICULATUS RACI1;                        
COMPND  27 CHAIN: D;                                                            
COMPND  28 ENGINEERED: YES;                                                     
COMPND  29 OTHER_DETAILS: FIRST 3 RESIDUES ARE THE REMNANT OF THE HISTIDINE-TAG.
COMPND  30 MATURE SEQUENCE BEGINS EEVK.                                         
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 MOL_ID: 2;                                                           
SOURCE   6 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   7 ORGANISM_COMMON: HUMAN;                                              
SOURCE   8 ORGANISM_TAXID: 9606;                                                
SOURCE   9 MOL_ID: 3;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: ORNITHODOROS MOUBATA;                           
SOURCE  11 ORGANISM_COMMON: SOFT TICK;                                          
SOURCE  12 ORGANISM_TAXID: 6938;                                                
SOURCE  13 GENE: CI;                                                            
SOURCE  14 EXPRESSION_SYSTEM: KLUYVEROMYCES LACTIS;                             
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 28985;                                      
SOURCE  16 MOL_ID: 4;                                                           
SOURCE  17 ORGANISM_SCIENTIFIC: RHIPICEPHALUS APPENDICULATUS;                   
SOURCE  18 ORGANISM_TAXID: 34631;                                               
SOURCE  19 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12;                            
SOURCE  20 EXPRESSION_SYSTEM_TAXID: 83333;                                      
SOURCE  21 EXPRESSION_SYSTEM_VARIANT: SHUFFLE T7;                               
SOURCE  22 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  23 EXPRESSION_SYSTEM_PLASMID: PET-M14                                   
KEYWDS    COMPLEMENT, INFLAMMATION, INHIBITOR, TICK, IMMUNE SYSTEM              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.M.JORE,S.JOHNSON,S.M.LEA                                            
REVDAT   4   17-JAN-18 5HCE    1       REMARK                                   
REVDAT   3   18-MAY-16 5HCE    1       JRNL                                     
REVDAT   2   06-APR-16 5HCE    1       JRNL                                     
REVDAT   1   30-MAR-16 5HCE    0                                                
JRNL        AUTH   M.M.JORE,S.JOHNSON,D.SHEPPARD,N.M.BARBER,Y.I.LI,M.A.NUNN,    
JRNL        AUTH 2 H.ELMLUND,S.M.LEA                                            
JRNL        TITL   STRUCTURAL BASIS FOR THERAPEUTIC INHIBITION OF COMPLEMENT    
JRNL        TITL 2 C5.                                                          
JRNL        REF    NAT.STRUCT.MOL.BIOL.          V.  23   378 2016              
JRNL        REFN                   ESSN 1545-9985                               
JRNL        PMID   27018802                                                     
JRNL        DOI    10.1038/NSMB.3196                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.12 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.10_2155: ???)                              
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) : 3.12                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 74.40                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 55783                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.268                           
REMARK   3   R VALUE            (WORKING SET) : 0.267                           
REMARK   3   FREE R VALUE                     : 0.281                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.940                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2754                            
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 74.4241 -  8.4651    0.98     2834   154  0.1880 0.1948        
REMARK   3     2  8.4651 -  6.7204    0.99     2714   155  0.2128 0.2349        
REMARK   3     3  6.7204 -  5.8713    1.00     2697   147  0.2373 0.2662        
REMARK   3     4  5.8713 -  5.3346    1.00     2705   148  0.2205 0.2544        
REMARK   3     5  5.3346 -  4.9523    0.99     2660   161  0.2149 0.2052        
REMARK   3     6  4.9523 -  4.6604    1.00     2672   134  0.2110 0.2369        
REMARK   3     7  4.6604 -  4.4270    1.00     2667   125  0.2237 0.2300        
REMARK   3     8  4.4270 -  4.2343    0.99     2662   128  0.2379 0.2833        
REMARK   3     9  4.2343 -  4.0714    1.00     2669   125  0.2761 0.3075        
REMARK   3    10  4.0714 -  3.9309    0.99     2644   135  0.2817 0.2789        
REMARK   3    11  3.9309 -  3.8080    0.98     2589   140  0.3314 0.3435        
REMARK   3    12  3.8080 -  3.6991    0.99     2646   140  0.3183 0.3505        
REMARK   3    13  3.6991 -  3.6017    0.98     2599   120  0.3553 0.3499        
REMARK   3    14  3.6017 -  3.5139    1.00     2603   137  0.3402 0.3141        
REMARK   3    15  3.5139 -  3.4340    0.98     2644   132  0.3676 0.4073        
REMARK   3    16  3.4340 -  3.3609    0.99     2594   135  0.3823 0.4231        
REMARK   3    17  3.3609 -  3.2937    0.99     2627   127  0.3809 0.3881        
REMARK   3    18  3.2937 -  3.2315    0.99     2605   144  0.3955 0.4220        
REMARK   3    19  3.2315 -  3.1738    0.99     2616   135  0.4035 0.3925        
REMARK   3    20  3.1738 -  3.1200    0.98     2582   132  0.4257 0.4128        
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)     : 0.490            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.030           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 73.10                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 80.90                          
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          14742                                  
REMARK   3   ANGLE     :  0.746          20009                                  
REMARK   3   CHIRALITY :  0.049           2278                                  
REMARK   3   PLANARITY :  0.005           2546                                  
REMARK   3   DIHEDRAL  : 11.985           8933                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 20 THROUGH 674 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.9945 -27.0579  -5.1183              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6074 T22:   0.7035                                     
REMARK   3      T33:   0.6878 T12:  -0.0090                                     
REMARK   3      T13:  -0.0398 T23:  -0.0106                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8984 L22:   1.3096                                     
REMARK   3      L33:   3.2929 L12:  -0.3968                                     
REMARK   3      L13:   0.9613 L23:  -1.0678                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0347 S12:   0.2251 S13:  -0.2481                       
REMARK   3      S21:  -0.3227 S22:   0.1747 S23:  -0.0546                       
REMARK   3      S31:   0.2775 S32:   0.2034 S33:  -0.1236                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 679 THROUGH 819 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -11.6838 -44.1379  24.8247              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6966 T22:   0.8749                                     
REMARK   3      T33:   0.8862 T12:   0.0579                                     
REMARK   3      T13:  -0.2127 T23:  -0.1050                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5794 L22:   1.3383                                     
REMARK   3      L33:   1.9278 L12:   0.4810                                     
REMARK   3      L13:  -0.9572 L23:  -1.0104                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0576 S12:   0.2915 S13:  -0.5410                       
REMARK   3      S21:  -0.2892 S22:  -0.0763 S23:   0.0559                       
REMARK   3      S31:   0.2116 S32:  -0.3298 S33:   0.0737                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 820 THROUGH 1514 )                
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.4494 -28.2346  52.1564              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5923 T22:   0.5705                                     
REMARK   3      T33:   0.5208 T12:   0.0423                                     
REMARK   3      T13:   0.0435 T23:   0.0178                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1689 L22:   1.4345                                     
REMARK   3      L33:   1.2178 L12:  -0.8768                                     
REMARK   3      L13:  -0.2342 L23:   0.0235                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0586 S12:  -0.0331 S13:   0.0629                       
REMARK   3      S21:   0.0860 S22:  -0.0191 S23:   0.0441                       
REMARK   3      S31:  -0.1768 S32:  -0.0040 S33:  -0.0069                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1515 THROUGH 1676 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  14.0072 -51.4788  81.8833              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.4715 T22:   1.7593                                     
REMARK   3      T33:   0.9544 T12:   0.1503                                     
REMARK   3      T13:  -0.0711 T23:   0.1606                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7938 L22:   4.9244                                     
REMARK   3      L33:   5.1918 L12:  -0.2990                                     
REMARK   3      L13:   1.3606 L23:  -2.0891                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1492 S12:  -1.5521 S13:  -0.4378                       
REMARK   3      S21:   1.5419 S22:  -0.0485 S23:  -0.4212                       
REMARK   3      S31:  -0.2785 S32:  -0.0067 S33:   0.0421                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 23 THROUGH 168 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -15.6199 -16.0223  89.6559              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2671 T22:   0.8229                                     
REMARK   3      T33:   0.5673 T12:   0.2801                                     
REMARK   3      T13:   0.1143 T23:  -0.0525                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.2317 L22:   2.3064                                     
REMARK   3      L33:   5.1526 L12:   1.6149                                     
REMARK   3      L13:  -0.3465 L23:  -0.1821                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2139 S12:  -0.7930 S13:  -0.1429                       
REMARK   3      S21:   0.9167 S22:   0.0429 S23:  -0.0224                       
REMARK   3      S31:  -0.1153 S32:   0.3688 S33:   0.0768                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 14 THROUGH 59 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -31.1000 -10.8195  20.3990              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9606 T22:   1.0867                                     
REMARK   3      T33:   0.7841 T12:   0.2412                                     
REMARK   3      T13:  -0.1800 T23:   0.0860                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9780 L22:   2.3313                                     
REMARK   3      L33:   3.3567 L12:   1.4611                                     
REMARK   3      L13:   0.1530 L23:   0.4727                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3524 S12:   0.6088 S13:   0.1180                       
REMARK   3      S21:  -0.2129 S22:  -0.2295 S23:   0.7428                       
REMARK   3      S31:  -0.7246 S32:  -0.8912 S33:  -0.0493                       
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 5HCE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 05-JAN-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000216815.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-MAY-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 9                                  
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I02                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97949                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M-F               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XIA2                               
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 56166                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.120                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 94.100                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 4.400                              
REMARK 200  R MERGE                    (I) : 0.11500                            
REMARK 200  R SYM                      (I) : 0.14800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.2000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.12                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.31                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.95300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.400                              
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: 3CU7, 2CM4                                           
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 66.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.70                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG 6K, 0.1 M BICINE PH 9.0, VAPOR   
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 294K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       52.63000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      105.18350            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       70.36250            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      105.18350            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       52.63000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       70.36250            
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 12680 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 83140 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -53.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, A, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLN B    19                                                      
REMARK 465     VAL B   612                                                      
REMARK 465     GLN B   613                                                      
REMARK 465     ARG B   614                                                      
REMARK 465     GLY B   615                                                      
REMARK 465     ALA B   616                                                      
REMARK 465     LYS B   617                                                      
REMARK 465     LYS B   618                                                      
REMARK 465     PRO B   619                                                      
REMARK 465     ASP A   874                                                      
REMARK 465     HIS A   875                                                      
REMARK 465     GLN A   876                                                      
REMARK 465     GLY A   877                                                      
REMARK 465     THR A   878                                                      
REMARK 465     SER A  1389                                                      
REMARK 465     HIS A  1390                                                      
REMARK 465     TYR A  1391                                                      
REMARK 465     ARG A  1392                                                      
REMARK 465     GLY A  1393                                                      
REMARK 465     TYR A  1394                                                      
REMARK 465     GLY A  1395                                                      
REMARK 465     ASN A  1396                                                      
REMARK 465     SER A  1397                                                      
REMARK 465     ASP A  1398                                                      
REMARK 465     TYR A  1399                                                      
REMARK 465     MET C     4                                                      
REMARK 465     ALA C     5                                                      
REMARK 465     SER C     6                                                      
REMARK 465     HIS C     7                                                      
REMARK 465     HIS C     8                                                      
REMARK 465     HIS C     9                                                      
REMARK 465     HIS C    10                                                      
REMARK 465     HIS C    11                                                      
REMARK 465     HIS C    12                                                      
REMARK 465     HIS C    13                                                      
REMARK 465     HIS C    14                                                      
REMARK 465     HIS C    15                                                      
REMARK 465     HIS C    16                                                      
REMARK 465     SER C    17                                                      
REMARK 465     GLY C    18                                                      
REMARK 465     ASP C    19                                                      
REMARK 465     SER C    20                                                      
REMARK 465     GLY D    -1                                                      
REMARK 465     PRO D     0                                                      
REMARK 465     MET D     1                                                      
REMARK 465     GLU D     2                                                      
REMARK 465     GLU D     3                                                      
REMARK 465     VAL D     4                                                      
REMARK 465     LYS D     5                                                      
REMARK 465     THR D     6                                                      
REMARK 465     THR D     7                                                      
REMARK 465     PRO D     8                                                      
REMARK 465     ILE D     9                                                      
REMARK 465     PRO D    10                                                      
REMARK 465     ASN D    11                                                      
REMARK 465     HIS D    12                                                      
REMARK 465     THR D    60                                                      
REMARK 465     THR D    61                                                      
REMARK 465     LYS D    62                                                      
REMARK 465     PRO D    63                                                      
REMARK 465     PRO D    64                                                      
REMARK 465     MET D    65                                                      
REMARK 465     ALA D    66                                                      
REMARK 465     PRO D    67                                                      
REMARK 465     GLY D    68                                                      
REMARK 465     ASP D    69                                                      
REMARK 465     ASN D    70                                                      
REMARK 465     LYS D    71                                                      
REMARK 465     ASP D    72                                                      
REMARK 465     ASN D    73                                                      
REMARK 465     LYS D    74                                                      
REMARK 465     GLU D    75                                                      
REMARK 465     GLU D    76                                                      
REMARK 465     GLU D    77                                                      
REMARK 465     SER D    78                                                      
REMARK 465     ASN D    79                                                      
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   NZ   LYS C    77     O    ASP C   167              2.17            
REMARK 500   OG   SER A   743     OD1  ASP A   746              2.17            
REMARK 500   OE2  GLU B   331     OG1  THR B   333              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    CYS A1520   CA  -  CB  -  SG  ANGL. DEV. =   6.9 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN B  97       70.67   -118.37                                   
REMARK 500    ASP B 138       -1.44     69.04                                   
REMARK 500    ASP B 208      -39.00     73.36                                   
REMARK 500    TYR B 256       31.04    -93.91                                   
REMARK 500    ALA B 286       33.99    -97.70                                   
REMARK 500    MET B 287       47.93    -80.13                                   
REMARK 500    SER B 311     -129.22     63.46                                   
REMARK 500    TYR B 312      -66.99     63.62                                   
REMARK 500    TYR B 313      -53.73     64.76                                   
REMARK 500    LEU B 318       -7.82     61.06                                   
REMARK 500    ASN B 320       -1.25     66.52                                   
REMARK 500    LEU B 361       45.34    -80.42                                   
REMARK 500    GLN B 399       13.47     59.63                                   
REMARK 500    ASP B 468      137.51   -176.43                                   
REMARK 500    TRP B 469       44.04   -106.37                                   
REMARK 500    THR B 470     -136.51     66.38                                   
REMARK 500    GLU B 480     -158.09    -76.76                                   
REMARK 500    ASP B 520       57.65   -113.39                                   
REMARK 500    ALA B 521      168.72    178.12                                   
REMARK 500    GLN B 550     -103.56     64.74                                   
REMARK 500    GLU B 628       37.97    -86.34                                   
REMARK 500    VAL A 760      -94.05   -107.96                                   
REMARK 500    ARG A 782      -17.66     66.36                                   
REMARK 500    SER A 880       88.70   -156.43                                   
REMARK 500    SER A 881     -160.05     54.21                                   
REMARK 500    SER A 892     -151.94   -161.53                                   
REMARK 500    TRP A 917        0.48    -63.59                                   
REMARK 500    ASP A 966       41.42    -89.03                                   
REMARK 500    SER A1036     -157.10    -94.49                                   
REMARK 500    PHE A1284     -131.38   -127.23                                   
REMARK 500    SER A1286     -154.94   -128.63                                   
REMARK 500    SER A1310      103.14   -162.45                                   
REMARK 500    HIS A1319       57.52   -102.17                                   
REMARK 500    LEU A1323      -72.07    -63.53                                   
REMARK 500    LEU A1334       44.06   -100.41                                   
REMARK 500    ASN A1343       34.72    -90.65                                   
REMARK 500    GLU A1387      -84.76    -93.44                                   
REMARK 500    SER A1420     -153.01    -96.14                                   
REMARK 500    ASP A1447       32.88    -89.04                                   
REMARK 500    GLU A1521       83.12     56.57                                   
REMARK 500    CYS A1525      -36.03   -138.53                                   
REMARK 500    ALA A1545      -35.15     61.53                                   
REMARK 500    ALA A1560      110.50   -167.19                                   
REMARK 500    ASN A1572     -101.23     58.79                                   
REMARK 500    LEU A1582      -77.60    -89.83                                   
REMARK 500    GLU A1589     -136.93   -104.07                                   
REMARK 500    GLU A1623      176.96     62.98                                   
REMARK 500    ASN A1630      -98.99     54.60                                   
REMARK 500    ASP A1640     -166.86   -125.96                                   
REMARK 500    THR A1653       31.39    -99.53                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      58 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ASP B  468     TRP B  469                 -149.23                    
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     CYS A 2101                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CYS A 2101                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  2102 through NAG A 2103 bound to ASN A 911                          
DBREF  5HCE B   19   674  UNP    P01031   CO5_HUMAN       19    674             
DBREF  5HCE A  679  1676  UNP    P01031   CO5_HUMAN      679   1676             
DBREF  5HCE C   19   168  UNP    Q5YD59   Q5YD59_ORNMO    19    168             
DBREF  5HCE D   -1    79  PDB    5HCE     5HCE            -1     79             
SEQADV 5HCE MET C    4  UNP  Q5YD59              INITIATING METHIONINE          
SEQADV 5HCE ALA C    5  UNP  Q5YD59              EXPRESSION TAG                 
SEQADV 5HCE SER C    6  UNP  Q5YD59              EXPRESSION TAG                 
SEQADV 5HCE HIS C    7  UNP  Q5YD59              EXPRESSION TAG                 
SEQADV 5HCE HIS C    8  UNP  Q5YD59              EXPRESSION TAG                 
SEQADV 5HCE HIS C    9  UNP  Q5YD59              EXPRESSION TAG                 
SEQADV 5HCE HIS C   10  UNP  Q5YD59              EXPRESSION TAG                 
SEQADV 5HCE HIS C   11  UNP  Q5YD59              EXPRESSION TAG                 
SEQADV 5HCE HIS C   12  UNP  Q5YD59              EXPRESSION TAG                 
SEQADV 5HCE HIS C   13  UNP  Q5YD59              EXPRESSION TAG                 
SEQADV 5HCE HIS C   14  UNP  Q5YD59              EXPRESSION TAG                 
SEQADV 5HCE HIS C   15  UNP  Q5YD59              EXPRESSION TAG                 
SEQADV 5HCE HIS C   16  UNP  Q5YD59              EXPRESSION TAG                 
SEQADV 5HCE SER C   17  UNP  Q5YD59              EXPRESSION TAG                 
SEQADV 5HCE GLY C   18  UNP  Q5YD59              EXPRESSION TAG                 
SEQADV 5HCE GLN C   78  UNP  Q5YD59    ASN    78 ENGINEERED MUTATION            
SEQADV 5HCE GLN C  102  UNP  Q5YD59    ASN   102 ENGINEERED MUTATION            
SEQRES   1 B  656  GLN GLU GLN THR TYR VAL ILE SER ALA PRO LYS ILE PHE          
SEQRES   2 B  656  ARG VAL GLY ALA SER GLU ASN ILE VAL ILE GLN VAL TYR          
SEQRES   3 B  656  GLY TYR THR GLU ALA PHE ASP ALA THR ILE SER ILE LYS          
SEQRES   4 B  656  SER TYR PRO ASP LYS LYS PHE SER TYR SER SER GLY HIS          
SEQRES   5 B  656  VAL HIS LEU SER SER GLU ASN LYS PHE GLN ASN SER ALA          
SEQRES   6 B  656  ILE LEU THR ILE GLN PRO LYS GLN LEU PRO GLY GLY GLN          
SEQRES   7 B  656  ASN PRO VAL SER TYR VAL TYR LEU GLU VAL VAL SER LYS          
SEQRES   8 B  656  HIS PHE SER LYS SER LYS ARG MET PRO ILE THR TYR ASP          
SEQRES   9 B  656  ASN GLY PHE LEU PHE ILE HIS THR ASP LYS PRO VAL TYR          
SEQRES  10 B  656  THR PRO ASP GLN SER VAL LYS VAL ARG VAL TYR SER LEU          
SEQRES  11 B  656  ASN ASP ASP LEU LYS PRO ALA LYS ARG GLU THR VAL LEU          
SEQRES  12 B  656  THR PHE ILE ASP PRO GLU GLY SER GLU VAL ASP MET VAL          
SEQRES  13 B  656  GLU GLU ILE ASP HIS ILE GLY ILE ILE SER PHE PRO ASP          
SEQRES  14 B  656  PHE LYS ILE PRO SER ASN PRO ARG TYR GLY MET TRP THR          
SEQRES  15 B  656  ILE LYS ALA LYS TYR LYS GLU ASP PHE SER THR THR GLY          
SEQRES  16 B  656  THR ALA TYR PHE GLU VAL LYS GLU TYR VAL LEU PRO HIS          
SEQRES  17 B  656  PHE SER VAL SER ILE GLU PRO GLU TYR ASN PHE ILE GLY          
SEQRES  18 B  656  TYR LYS ASN PHE LYS ASN PHE GLU ILE THR ILE LYS ALA          
SEQRES  19 B  656  ARG TYR PHE TYR ASN LYS VAL VAL THR GLU ALA ASP VAL          
SEQRES  20 B  656  TYR ILE THR PHE GLY ILE ARG GLU ASP LEU LYS ASP ASP          
SEQRES  21 B  656  GLN LYS GLU MET MET GLN THR ALA MET GLN ASN THR MET          
SEQRES  22 B  656  LEU ILE ASN GLY ILE ALA GLN VAL THR PHE ASP SER GLU          
SEQRES  23 B  656  THR ALA VAL LYS GLU LEU SER TYR TYR SER LEU GLU ASP          
SEQRES  24 B  656  LEU ASN ASN LYS TYR LEU TYR ILE ALA VAL THR VAL ILE          
SEQRES  25 B  656  GLU SER THR GLY GLY PHE SER GLU GLU ALA GLU ILE PRO          
SEQRES  26 B  656  GLY ILE LYS TYR VAL LEU SER PRO TYR LYS LEU ASN LEU          
SEQRES  27 B  656  VAL ALA THR PRO LEU PHE LEU LYS PRO GLY ILE PRO TYR          
SEQRES  28 B  656  PRO ILE LYS VAL GLN VAL LYS ASP SER LEU ASP GLN LEU          
SEQRES  29 B  656  VAL GLY GLY VAL PRO VAL THR LEU ASN ALA GLN THR ILE          
SEQRES  30 B  656  ASP VAL ASN GLN GLU THR SER ASP LEU ASP PRO SER LYS          
SEQRES  31 B  656  SER VAL THR ARG VAL ASP ASP GLY VAL ALA SER PHE VAL          
SEQRES  32 B  656  LEU ASN LEU PRO SER GLY VAL THR VAL LEU GLU PHE ASN          
SEQRES  33 B  656  VAL LYS THR ASP ALA PRO ASP LEU PRO GLU GLU ASN GLN          
SEQRES  34 B  656  ALA ARG GLU GLY TYR ARG ALA ILE ALA TYR SER SER LEU          
SEQRES  35 B  656  SER GLN SER TYR LEU TYR ILE ASP TRP THR ASP ASN HIS          
SEQRES  36 B  656  LYS ALA LEU LEU VAL GLY GLU HIS LEU ASN ILE ILE VAL          
SEQRES  37 B  656  THR PRO LYS SER PRO TYR ILE ASP LYS ILE THR HIS TYR          
SEQRES  38 B  656  ASN TYR LEU ILE LEU SER LYS GLY LYS ILE ILE HIS PHE          
SEQRES  39 B  656  GLY THR ARG GLU LYS PHE SER ASP ALA SER TYR GLN SER          
SEQRES  40 B  656  ILE ASN ILE PRO VAL THR GLN ASN MET VAL PRO SER SER          
SEQRES  41 B  656  ARG LEU LEU VAL TYR TYR ILE VAL THR GLY GLU GLN THR          
SEQRES  42 B  656  ALA GLU LEU VAL SER ASP SER VAL TRP LEU ASN ILE GLU          
SEQRES  43 B  656  GLU LYS CYS GLY ASN GLN LEU GLN VAL HIS LEU SER PRO          
SEQRES  44 B  656  ASP ALA ASP ALA TYR SER PRO GLY GLN THR VAL SER LEU          
SEQRES  45 B  656  ASN MET ALA THR GLY MET ASP SER TRP VAL ALA LEU ALA          
SEQRES  46 B  656  ALA VAL ASP SER ALA VAL TYR GLY VAL GLN ARG GLY ALA          
SEQRES  47 B  656  LYS LYS PRO LEU GLU ARG VAL PHE GLN PHE LEU GLU LYS          
SEQRES  48 B  656  SER ASP LEU GLY CYS GLY ALA GLY GLY GLY LEU ASN ASN          
SEQRES  49 B  656  ALA ASN VAL PHE HIS LEU ALA GLY LEU THR PHE LEU THR          
SEQRES  50 B  656  ASN ALA ASN ALA ASP ASP SER GLN GLU ASN ASP GLU PRO          
SEQRES  51 B  656  CYS LYS GLU ILE LEU ARG                                      
SEQRES   1 A  998  LEU GLN LYS LYS ILE GLU GLU ILE ALA ALA LYS TYR LYS          
SEQRES   2 A  998  HIS SER VAL VAL LYS LYS CYS CYS TYR ASP GLY ALA CYS          
SEQRES   3 A  998  VAL ASN ASN ASP GLU THR CYS GLU GLN ARG ALA ALA ARG          
SEQRES   4 A  998  ILE SER LEU GLY PRO ARG CYS ILE LYS ALA PHE THR GLU          
SEQRES   5 A  998  CYS CYS VAL VAL ALA SER GLN LEU ARG ALA ASN ILE SER          
SEQRES   6 A  998  HIS LYS ASP MET GLN LEU GLY ARG LEU HIS MET LYS THR          
SEQRES   7 A  998  LEU LEU PRO VAL SER LYS PRO GLU ILE ARG SER TYR PHE          
SEQRES   8 A  998  PRO GLU SER TRP LEU TRP GLU VAL HIS LEU VAL PRO ARG          
SEQRES   9 A  998  ARG LYS GLN LEU GLN PHE ALA LEU PRO ASP SER LEU THR          
SEQRES  10 A  998  THR TRP GLU ILE GLN GLY VAL GLY ILE SER ASN THR GLY          
SEQRES  11 A  998  ILE CYS VAL ALA ASP THR VAL LYS ALA LYS VAL PHE LYS          
SEQRES  12 A  998  ASP VAL PHE LEU GLU MET ASN ILE PRO TYR SER VAL VAL          
SEQRES  13 A  998  ARG GLY GLU GLN ILE GLN LEU LYS GLY THR VAL TYR ASN          
SEQRES  14 A  998  TYR ARG THR SER GLY MET GLN PHE CYS VAL LYS MET SER          
SEQRES  15 A  998  ALA VAL GLU GLY ILE CYS THR SER GLU SER PRO VAL ILE          
SEQRES  16 A  998  ASP HIS GLN GLY THR LYS SER SER LYS CYS VAL ARG GLN          
SEQRES  17 A  998  LYS VAL GLU GLY SER SER SER HIS LEU VAL THR PHE THR          
SEQRES  18 A  998  VAL LEU PRO LEU GLU ILE GLY LEU HIS ASN ILE ASN PHE          
SEQRES  19 A  998  SER LEU GLU THR TRP PHE GLY LYS GLU ILE LEU VAL LYS          
SEQRES  20 A  998  THR LEU ARG VAL VAL PRO GLU GLY VAL LYS ARG GLU SER          
SEQRES  21 A  998  TYR SER GLY VAL THR LEU ASP PRO ARG GLY ILE TYR GLY          
SEQRES  22 A  998  THR ILE SER ARG ARG LYS GLU PHE PRO TYR ARG ILE PRO          
SEQRES  23 A  998  LEU ASP LEU VAL PRO LYS THR GLU ILE LYS ARG ILE LEU          
SEQRES  24 A  998  SER VAL LYS GLY LEU LEU VAL GLY GLU ILE LEU SER ALA          
SEQRES  25 A  998  VAL LEU SER GLN GLU GLY ILE ASN ILE LEU THR HIS LEU          
SEQRES  26 A  998  PRO LYS GLY SER ALA GLU ALA GLU LEU MET SER VAL VAL          
SEQRES  27 A  998  PRO VAL PHE TYR VAL PHE HIS TYR LEU GLU THR GLY ASN          
SEQRES  28 A  998  HIS TRP ASN ILE PHE HIS SER ASP PRO LEU ILE GLU LYS          
SEQRES  29 A  998  GLN LYS LEU LYS LYS LYS LEU LYS GLU GLY MET LEU SER          
SEQRES  30 A  998  ILE MET SER TYR ARG ASN ALA ASP TYR SER TYR SER VAL          
SEQRES  31 A  998  TRP LYS GLY GLY SER ALA SER THR TRP LEU THR ALA PHE          
SEQRES  32 A  998  ALA LEU ARG VAL LEU GLY GLN VAL ASN LYS TYR VAL GLU          
SEQRES  33 A  998  GLN ASN GLN ASN SER ILE CYS ASN SER LEU LEU TRP LEU          
SEQRES  34 A  998  VAL GLU ASN TYR GLN LEU ASP ASN GLY SER PHE LYS GLU          
SEQRES  35 A  998  ASN SER GLN TYR GLN PRO ILE LYS LEU GLN GLY THR LEU          
SEQRES  36 A  998  PRO VAL GLU ALA ARG GLU ASN SER LEU TYR LEU THR ALA          
SEQRES  37 A  998  PHE THR VAL ILE GLY ILE ARG LYS ALA PHE ASP ILE CYS          
SEQRES  38 A  998  PRO LEU VAL LYS ILE ASP THR ALA LEU ILE LYS ALA ASP          
SEQRES  39 A  998  ASN PHE LEU LEU GLU ASN THR LEU PRO ALA GLN SER THR          
SEQRES  40 A  998  PHE THR LEU ALA ILE SER ALA TYR ALA LEU SER LEU GLY          
SEQRES  41 A  998  ASP LYS THR HIS PRO GLN PHE ARG SER ILE VAL SER ALA          
SEQRES  42 A  998  LEU LYS ARG GLU ALA LEU VAL LYS GLY ASN PRO PRO ILE          
SEQRES  43 A  998  TYR ARG PHE TRP LYS ASP ASN LEU GLN HIS LYS ASP SER          
SEQRES  44 A  998  SER VAL PRO ASN THR GLY THR ALA ARG MET VAL GLU THR          
SEQRES  45 A  998  THR ALA TYR ALA LEU LEU THR SER LEU ASN LEU LYS ASP          
SEQRES  46 A  998  ILE ASN TYR VAL ASN PRO VAL ILE LYS TRP LEU SER GLU          
SEQRES  47 A  998  GLU GLN ARG TYR GLY GLY GLY PHE TYR SER THR GLN ASP          
SEQRES  48 A  998  THR ILE ASN ALA ILE GLU GLY LEU THR GLU TYR SER LEU          
SEQRES  49 A  998  LEU VAL LYS GLN LEU ARG LEU SER MET ASP ILE ASP VAL          
SEQRES  50 A  998  SER TYR LYS HIS LYS GLY ALA LEU HIS ASN TYR LYS MET          
SEQRES  51 A  998  THR ASP LYS ASN PHE LEU GLY ARG PRO VAL GLU VAL LEU          
SEQRES  52 A  998  LEU ASN ASP ASP LEU ILE VAL SER THR GLY PHE GLY SER          
SEQRES  53 A  998  GLY LEU ALA THR VAL HIS VAL THR THR VAL VAL HIS LYS          
SEQRES  54 A  998  THR SER THR SER GLU GLU VAL CYS SER PHE TYR LEU LYS          
SEQRES  55 A  998  ILE ASP THR GLN ASP ILE GLU ALA SER HIS TYR ARG GLY          
SEQRES  56 A  998  TYR GLY ASN SER ASP TYR LYS ARG ILE VAL ALA CYS ALA          
SEQRES  57 A  998  SER TYR LYS PRO SER ARG GLU GLU SER SER SER GLY SER          
SEQRES  58 A  998  SER HIS ALA VAL MET ASP ILE SER LEU PRO THR GLY ILE          
SEQRES  59 A  998  SER ALA ASN GLU GLU ASP LEU LYS ALA LEU VAL GLU GLY          
SEQRES  60 A  998  VAL ASP GLN LEU PHE THR ASP TYR GLN ILE LYS ASP GLY          
SEQRES  61 A  998  HIS VAL ILE LEU GLN LEU ASN SER ILE PRO SER SER ASP          
SEQRES  62 A  998  PHE LEU CYS VAL ARG PHE ARG ILE PHE GLU LEU PHE GLU          
SEQRES  63 A  998  VAL GLY PHE LEU SER PRO ALA THR PHE THR VAL TYR GLU          
SEQRES  64 A  998  TYR HIS ARG PRO ASP LYS GLN CYS THR MET PHE TYR SER          
SEQRES  65 A  998  THR SER ASN ILE LYS ILE GLN LYS VAL CYS GLU GLY ALA          
SEQRES  66 A  998  ALA CYS LYS CYS VAL GLU ALA ASP CYS GLY GLN MET GLN          
SEQRES  67 A  998  GLU GLU LEU ASP LEU THR ILE SER ALA GLU THR ARG LYS          
SEQRES  68 A  998  GLN THR ALA CYS LYS PRO GLU ILE ALA TYR ALA TYR LYS          
SEQRES  69 A  998  VAL SER ILE THR SER ILE THR VAL GLU ASN VAL PHE VAL          
SEQRES  70 A  998  LYS TYR LYS ALA THR LEU LEU ASP ILE TYR LYS THR GLY          
SEQRES  71 A  998  GLU ALA VAL ALA GLU LYS ASP SER GLU ILE THR PHE ILE          
SEQRES  72 A  998  LYS LYS VAL THR CYS THR ASN ALA GLU LEU VAL LYS GLY          
SEQRES  73 A  998  ARG GLN TYR LEU ILE MET GLY LYS GLU ALA LEU GLN ILE          
SEQRES  74 A  998  LYS TYR ASN PHE SER PHE ARG TYR ILE TYR PRO LEU ASP          
SEQRES  75 A  998  SER LEU THR TRP ILE GLU TYR TRP PRO ARG ASP THR THR          
SEQRES  76 A  998  CYS SER SER CYS GLN ALA PHE LEU ALA ASN LEU ASP GLU          
SEQRES  77 A  998  PHE ALA GLU ASP ILE PHE LEU ASN GLY CYS                      
SEQRES   1 C  165  MET ALA SER HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS          
SEQRES   2 C  165  SER GLY ASP SER GLU SER ASP CYS THR GLY SER GLU PRO          
SEQRES   3 C  165  VAL ASP ALA PHE GLN ALA PHE SER GLU GLY LYS GLU ALA          
SEQRES   4 C  165  TYR VAL LEU VAL ARG SER THR ASP PRO LYS ALA ARG ASP          
SEQRES   5 C  165  CYS LEU LYS GLY GLU PRO ALA GLY GLU LYS GLN ASP ASN          
SEQRES   6 C  165  THR LEU PRO VAL MET MET THR PHE LYS GLN GLY THR ASP          
SEQRES   7 C  165  TRP ALA SER THR ASP TRP THR PHE THR LEU ASP GLY ALA          
SEQRES   8 C  165  LYS VAL THR ALA THR LEU GLY GLN LEU THR GLN ASN ARG          
SEQRES   9 C  165  GLU VAL VAL TYR ASP SER GLN SER HIS HIS CYS HIS VAL          
SEQRES  10 C  165  ASP LYS VAL GLU LYS GLU VAL PRO ASP TYR GLU MET TRP          
SEQRES  11 C  165  MET LEU ASP ALA GLY GLY LEU GLU VAL GLU VAL GLU CYS          
SEQRES  12 C  165  CYS ARG GLN LYS LEU GLU GLU LEU ALA SER GLY ARG ASN          
SEQRES  13 C  165  GLN MET TYR PRO HIS LEU LYS ASP CYS                          
SEQRES   1 D   81  GLY PRO MET GLU GLU VAL LYS THR THR PRO ILE PRO ASN          
SEQRES   2 D   81  HIS GLN CYS VAL ASN ALA THR CYS GLU ARG LYS LEU ASP          
SEQRES   3 D   81  ALA LEU GLY ASN ALA VAL ILE THR LYS CYS PRO GLN GLY          
SEQRES   4 D   81  CYS LEU CYS VAL VAL ARG GLY ALA SER ASN ILE VAL PRO          
SEQRES   5 D   81  ALA ASN GLY THR CYS PHE GLN LEU ALA THR THR LYS PRO          
SEQRES   6 D   81  PRO MET ALA PRO GLY ASP ASN LYS ASP ASN LYS GLU GLU          
SEQRES   7 D   81  GLU SER ASN                                                  
HET    CYS  A2101       6                                                       
HET    NAG  A2102      14                                                       
HET    NAG  A2103      14                                                       
HETNAM     CYS CYSTEINE                                                         
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
FORMUL   5  CYS    C3 H7 N O2 S                                                 
FORMUL   6  NAG    2(C8 H15 N O6)                                               
HELIX    1 AA1 GLN B   88  LEU B   92  5                                   5    
HELIX    2 AA2 ASP B  302  VAL B  307  1                                   6    
HELIX    3 AA3 TYR B  492  ILE B  496  5                                   5    
HELIX    4 AA4 THR B  531  VAL B  535  5                                   5    
HELIX    5 AA5 ALA B  608  GLY B  611  5                                   4    
HELIX    6 AA6 ARG B  622  GLU B  628  1                                   7    
HELIX    7 AA7 ASN B  641  ALA B  649  1                                   9    
HELIX    8 AA8 GLN A  680  TYR A  690  1                                  11    
HELIX    9 AA9 LYS A  696  ALA A  703  1                                   8    
HELIX   10 AB1 THR A  710  ALA A  716  1                                   7    
HELIX   11 AB2 GLY A  721  ARG A  739  1                                  19    
HELIX   12 AB3 SER A  743  LEU A  758  1                                  16    
HELIX   13 AB4 VAL A  984  SER A  993  1                                  10    
HELIX   14 AB5 SER A 1007  SER A 1014  1                                   8    
HELIX   15 AB6 VAL A 1015  GLY A 1028  1                                  14    
HELIX   16 AB7 HIS A 1030  PHE A 1034  5                                   5    
HELIX   17 AB8 ASP A 1037  SER A 1055  1                                  19    
HELIX   18 AB9 ILE A 1056  ARG A 1060  5                                   5    
HELIX   19 AC1 SER A 1075  ASN A 1090  1                                  16    
HELIX   20 AC2 ASN A 1096  TYR A 1111  1                                  16    
HELIX   21 AC3 THR A 1132  ALA A 1155  1                                  24    
HELIX   22 AC4 LEU A 1161  THR A 1179  1                                  19    
HELIX   23 AC5 SER A 1184  LEU A 1197  1                                  14    
HELIX   24 AC6 HIS A 1202  GLU A 1215  1                                  14    
HELIX   25 AC7 THR A 1244  LEU A 1261  1                                  18    
HELIX   26 AC8 ASP A 1263  GLU A 1277  1                                  15    
HELIX   27 AC9 SER A 1286  VAL A 1304  1                                  19    
HELIX   28 AD1 ASN A 1435  GLU A 1444  1                                  10    
HELIX   29 AD2 GLU A 1546  THR A 1551  1                                   6    
HELIX   30 AD3 SER A 1656  LEU A 1673  1                                  18    
HELIX   31 AD4 ASP C   31  PHE C   36  1                                   6    
HELIX   32 AD5 SER C   37  LYS C   40  5                                   4    
HELIX   33 AD6 GLU C  141  SER C  156  1                                  16    
HELIX   34 AD7 TYR C  162  LYS C  166  5                                   5    
SHEET    1 AA1 4 GLN B  80  THR B  86  0                                        
SHEET    2 AA1 4 SER B  36  TYR B  44 -1  N  ILE B  41   O  ASN B  81           
SHEET    3 AA1 4 THR B  22  PRO B  28 -1  N  THR B  22   O  TYR B  44           
SHEET    4 AA1 4 LEU B 651  THR B 655 -1  O  THR B 652   N  ALA B  27           
SHEET    1 AA2 5 PHE B  31  ARG B  32  0                                        
SHEET    2 AA2 5 SER B 112  THR B 120  1  O  PRO B 118   N  PHE B  31           
SHEET    3 AA2 5 TYR B 101  SER B 108 -1  N  VAL B 102   O  MET B 117           
SHEET    4 AA2 5 PHE B  50  SER B  58 -1  N  THR B  53   O  VAL B 107           
SHEET    5 AA2 5 SER B  65  LEU B  73 -1  O  SER B  67   N  ILE B  56           
SHEET    1 AA3 3 PHE B 125  THR B 130  0                                        
SHEET    2 AA3 3 VAL B 143  LEU B 148 -1  O  ARG B 144   N  HIS B 129           
SHEET    3 AA3 3 ILE B 182  SER B 184 -1  O  ILE B 183   N  VAL B 145           
SHEET    1 AA4 5 VAL B 134  TYR B 135  0                                        
SHEET    2 AA4 5 THR B 212  VAL B 219  1  O  GLU B 218   N  TYR B 135           
SHEET    3 AA4 5 GLY B 197  TYR B 205 -1  N  ILE B 201   O  ALA B 215           
SHEET    4 AA4 5 THR B 159  ILE B 164 -1  N  VAL B 160   O  LYS B 204           
SHEET    5 AA4 5 GLU B 170  GLU B 176 -1  O  VAL B 174   N  LEU B 161           
SHEET    1 AA5 2 SER B 140  VAL B 141  0                                        
SHEET    2 AA5 2 PHE B 188  LYS B 189 -1  O  PHE B 188   N  VAL B 141           
SHEET    1 AA6 2 GLU B 221  TYR B 222  0                                        
SHEET    2 AA6 2 GLU A 764  ILE A 765  1  O  ILE A 765   N  GLU B 221           
SHEET    1 AA7 3 PHE B 227  PRO B 233  0                                        
SHEET    2 AA7 3 PHE B 246  TYR B 254 -1  O  LYS B 251   N  SER B 230           
SHEET    3 AA7 3 LYS B 258  VAL B 259 -1  O  LYS B 258   N  TYR B 254           
SHEET    1 AA8 3 PHE B 227  PRO B 233  0                                        
SHEET    2 AA8 3 PHE B 246  TYR B 254 -1  O  LYS B 251   N  SER B 230           
SHEET    3 AA8 3 ILE B 296  PHE B 301 -1  O  VAL B 299   N  ILE B 248           
SHEET    1 AA9 5 PHE B 237  ILE B 238  0                                        
SHEET    2 AA9 5 SER B 337  TYR B 347  1  O  LYS B 346   N  ILE B 238           
SHEET    3 AA9 5 TYR B 322  GLU B 331 -1  N  VAL B 327   O  ALA B 340           
SHEET    4 AA9 5 GLU B 262  ARG B 272 -1  N  ARG B 272   O  TYR B 322           
SHEET    5 AA9 5 GLU B 281  MET B 283 -1  O  GLU B 281   N  ILE B 271           
SHEET    1 AB1 5 PHE B 237  ILE B 238  0                                        
SHEET    2 AB1 5 SER B 337  TYR B 347  1  O  LYS B 346   N  ILE B 238           
SHEET    3 AB1 5 TYR B 322  GLU B 331 -1  N  VAL B 327   O  ALA B 340           
SHEET    4 AB1 5 GLU B 262  ARG B 272 -1  N  ARG B 272   O  TYR B 322           
SHEET    5 AB1 5 ASN B 289  ILE B 293 -1  O  THR B 290   N  VAL B 265           
SHEET    1 AB2 3 LYS B 353  LEU B 356  0                                        
SHEET    2 AB2 3 TYR B 369  LYS B 376 -1  O  LYS B 376   N  LYS B 353           
SHEET    3 AB2 3 VAL B 417  LEU B 422 -1  O  LEU B 422   N  TYR B 369           
SHEET    1 AB3 5 PHE B 362  LEU B 363  0                                        
SHEET    2 AB3 5 ARG B 449  ALA B 456  1  O  ILE B 455   N  LEU B 363           
SHEET    3 AB3 5 VAL B 428  THR B 437 -1  N  VAL B 435   O  GLU B 450           
SHEET    4 AB3 5 PRO B 387  ASP B 396 -1  N  ILE B 395   O  THR B 429           
SHEET    5 AB3 5 THR B 401  ASP B 403 -1  O  SER B 402   N  THR B 394           
SHEET    1 AB4 5 PHE B 362  LEU B 363  0                                        
SHEET    2 AB4 5 ARG B 449  ALA B 456  1  O  ILE B 455   N  LEU B 363           
SHEET    3 AB4 5 VAL B 428  THR B 437 -1  N  VAL B 435   O  GLU B 450           
SHEET    4 AB4 5 PRO B 387  ASP B 396 -1  N  ILE B 395   O  THR B 429           
SHEET    5 AB4 5 SER B 407  VAL B 410 -1  O  SER B 409   N  VAL B 388           
SHEET    1 AB5 3 TYR B 464  ASP B 468  0                                        
SHEET    2 AB5 3 HIS B 481  LYS B 489 -1  O  THR B 487   N  TYR B 466           
SHEET    3 AB5 3 GLN B 524  PRO B 529 -1  O  ILE B 528   N  LEU B 482           
SHEET    1 AB6 4 LYS B 508  GLU B 516  0                                        
SHEET    2 AB6 4 HIS B 498  SER B 505 -1  N  TYR B 499   O  ARG B 515           
SHEET    3 AB6 4 SER B 537  VAL B 546 -1  O  ARG B 539   N  LEU B 504           
SHEET    4 AB6 4 GLU B 553  ASN B 562 -1  O  VAL B 555   N  TYR B 544           
SHEET    1 AB7 3 LEU B 571  SER B 576  0                                        
SHEET    2 AB7 3 THR B 587  THR B 594 -1  O  SER B 589   N  SER B 576           
SHEET    3 AB7 3 ARG A 783  ALA A 789 -1  O  LEU A 786   N  LEU B 590           
SHEET    1 AB8 4 VAL A 777  VAL A 780  0                                        
SHEET    2 AB8 4 SER B 598  ASP B 606 -1  N  SER B 598   O  VAL A 780           
SHEET    3 AB8 4 THR A 795  SER A 805 -1  O  VAL A 802   N  ALA B 601           
SHEET    4 AB8 4 GLY A 808  VAL A 811 -1  O  CYS A 810   N  GLY A 803           
SHEET    1 AB9 4 VAL A 777  VAL A 780  0                                        
SHEET    2 AB9 4 SER B 598  ASP B 606 -1  N  SER B 598   O  VAL A 780           
SHEET    3 AB9 4 THR A 795  SER A 805 -1  O  VAL A 802   N  ALA B 601           
SHEET    4 AB9 4 VAL A 815  VAL A 819 -1  O  VAL A 815   N  ILE A 799           
SHEET    1 AC1 4 VAL A 823  ASN A 828  0                                        
SHEET    2 AC1 4 GLN A 838  ASN A 847 -1  O  TYR A 846   N  PHE A 824           
SHEET    3 AC1 4 SER A 892  PRO A 902 -1  O  PHE A 898   N  LEU A 841           
SHEET    4 AC1 4 ILE A 865  THR A 867 -1  N  CYS A 866   O  LEU A 901           
SHEET    1 AC2 3 VAL A 823  ASN A 828  0                                        
SHEET    2 AC2 3 GLN A 838  ASN A 847 -1  O  TYR A 846   N  PHE A 824           
SHEET    3 AC2 3 VAL A1485  GLY A1486 -1  O  GLY A1486   N  GLN A 838           
SHEET    1 AC3 5 VAL A 833  VAL A 834  0                                        
SHEET    2 AC3 5 GLY A 919  VAL A 930  1  O  VAL A 930   N  VAL A 833           
SHEET    3 AC3 5 GLY A 906  THR A 916 -1  N  HIS A 908   O  LEU A 927           
SHEET    4 AC3 5 MET A 853  MET A 859 -1  N  LYS A 858   O  SER A 913           
SHEET    5 AC3 5 GLN A 886  VAL A 888 -1  O  GLN A 886   N  PHE A 855           
SHEET    1 AC4 4 VAL A 934  LEU A 944  0                                        
SHEET    2 AC4 4 ALA A1357  LYS A1367 -1  O  VAL A1359   N  VAL A 942           
SHEET    3 AC4 4 LYS A 974  LYS A 980 -1  N  SER A 978   O  HIS A1360           
SHEET    4 AC4 4 VAL A1338  GLU A1339 -1  O  VAL A1338   N  LEU A 977           
SHEET    1 AC5 4 ARG A 956  PHE A 959  0                                        
SHEET    2 AC5 4 LEU A1346  THR A1350 -1  O  VAL A1348   N  LYS A 957           
SHEET    3 AC5 4 SER A1310  TYR A1317 -1  N  ASP A1314   O  SER A1349           
SHEET    4 AC5 4 HIS A1324  THR A1329 -1  O  HIS A1324   N  VAL A1315           
SHEET    1 AC6 3 TYR A1225  PHE A1227  0                                        
SHEET    2 AC6 3 LEU A1217  LYS A1219 -1  N  LEU A1217   O  PHE A1227           
SHEET    3 AC6 3 GLY C 139  LEU C 140 -1  O  GLY C 139   N  VAL A1218           
SHEET    1 AC7 4 PHE A1377  GLN A1384  0                                        
SHEET    2 AC7 4 ARG A1401  TYR A1408 -1  O  CYS A1405   N  LYS A1380           
SHEET    3 AC7 4 LEU A1473  GLU A1481 -1  O  PHE A1477   N  ILE A1402           
SHEET    4 AC7 4 ILE A1432  ALA A1434 -1  N  SER A1433   O  PHE A1480           
SHEET    1 AC8 5 ASP A1452  LYS A1456  0                                        
SHEET    2 AC8 5 HIS A1459  LEU A1464 -1  O  GLN A1463   N  ASP A1452           
SHEET    3 AC8 5 ALA A1422  SER A1427 -1  N  ILE A1426   O  VAL A1460           
SHEET    4 AC8 5 ALA A1491  GLU A1497 -1  O  THR A1494   N  ASP A1425           
SHEET    5 AC8 5 ARG A1500  TYR A1509 -1  O  TYR A1509   N  ALA A1491           
SHEET    1 AC9 7 LEU A1625  TYR A1629  0                                        
SHEET    2 AC9 7 SER A1632  PRO A1638 -1  O  ARG A1634   N  ILE A1627           
SHEET    3 AC9 7 GLU A1597  LYS A1603  1  N  THR A1599   O  TYR A1637           
SHEET    4 AC9 7 PHE A1574  THR A1587 -1  N  ALA A1579   O  ILE A1598           
SHEET    5 AC9 7 TYR A1559  GLU A1571 -1  N  THR A1566   O  LYS A1578           
SHEET    6 AC9 7 GLN A1616  GLY A1621 -1  O  TYR A1617   N  VAL A1563           
SHEET    7 AC9 7 TRP A1644  TYR A1647 -1  O  GLU A1646   N  LEU A1618           
SHEET    1 AD1 9 TYR C  43  SER C  48  0                                        
SHEET    2 AD1 9 ASP C  55  PRO C  61 -1  O  GLY C  59   N  TYR C  43           
SHEET    3 AD1 9 THR C  69  GLN C  78 -1  O  THR C  75   N  LYS C  58           
SHEET    4 AD1 9 ASP C  81  ASP C  92 -1  O  THR C  85   N  MET C  74           
SHEET    5 AD1 9 LYS C  95  LEU C 100 -1  O  LYS C  95   N  ASP C  92           
SHEET    6 AD1 9 LEU C 103  ASP C 112 -1  O  ARG C 107   N  VAL C  96           
SHEET    7 AD1 9 CYS C 118  VAL C 123 -1  O  VAL C 120   N  TYR C 111           
SHEET    8 AD1 9 ASP C 129  LEU C 135 -1  O  TRP C 133   N  HIS C 119           
SHEET    9 AD1 9 TYR C  43  SER C  48 -1  N  VAL C  44   O  MET C 134           
SHEET    1 AD2 4 ALA D  29  ILE D  31  0                                        
SHEET    2 AD2 4 CYS D  19  LEU D  23 -1  N  LYS D  22   O  VAL D  30           
SHEET    3 AD2 4 ALA D  51  PHE D  56 -1  O  ALA D  51   N  ARG D  21           
SHEET    4 AD2 4 LEU D  39  VAL D  41 -1  N  VAL D  41   O  THR D  54           
SSBOND   1 CYS B  567    CYS A  810                          1555   1555  2.03  
SSBOND   2 CYS B  634    CYS B  669                          1555   1555  2.03  
SSBOND   3 CYS A  698    CYS A  724                          1555   1555  2.04  
SSBOND   4 CYS A  699    CYS A  731                          1555   1555  2.02  
SSBOND   5 CYS A  704    CYS A 2101                          1555   1555  2.02  
SSBOND   6 CYS A  711    CYS A  732                          1555   1555  2.03  
SSBOND   7 CYS A  856    CYS A  883                          1555   1555  2.04  
SSBOND   8 CYS A  866    CYS A 1527                          1555   1555  2.03  
SSBOND   9 CYS A 1101    CYS A 1159                          1555   1555  2.03  
SSBOND  10 CYS A 1375    CYS A 1505                          1555   1555  2.03  
SSBOND  11 CYS A 1405    CYS A 1474                          1555   1555  2.03  
SSBOND  12 CYS A 1520    CYS A 1525                          1555   1555  2.03  
SSBOND  13 CYS A 1532    CYS A 1606                          1555   1555  2.02  
SSBOND  14 CYS A 1553    CYS A 1676                          1555   1555  2.03  
SSBOND  15 CYS A 1654    CYS A 1657                          1555   1555  2.00  
SSBOND  16 CYS C   24    CYS C  146                          1555   1555  2.03  
SSBOND  17 CYS C   56    CYS C  168                          1555   1555  2.03  
SSBOND  18 CYS C  118    CYS C  147                          1555   1555  2.03  
SSBOND  19 CYS D   14    CYS D   38                          1555   1555  2.03  
SSBOND  20 CYS D   19    CYS D   40                          1555   1555  2.01  
SSBOND  21 CYS D   34    CYS D   55                          1555   1555  2.02  
LINK         ND2 ASN A 911                 C1  NAG A2102     1555   1555  1.42  
LINK         O4  NAG A2102                 C1  NAG A2103     1555   1555  1.44  
CISPEP   1 TYR B   59    PRO B   60          0        -1.69                     
CISPEP   2 HIS B  473    LYS B  474          0         3.61                     
CISPEP   3 VAL B  535    PRO B  536          0        -1.80                     
CISPEP   4 SER B  576    PRO B  577          0         2.46                     
CISPEP   5 GLY A  996    ILE A  997          0        -4.00                     
CISPEP   6 LEU A 1180    PRO A 1181          0         0.48                     
CISPEP   7 ASN A 1221    PRO A 1222          0         3.02                     
CISPEP   8 LYS A 1515    ILE A 1516          0        13.51                     
CISPEP   9 GLU C   28    PRO C   29          0         0.90                     
CISPEP  10 VAL D   49    PRO D   50          0        -7.55                     
SITE     1 AC1  3 TYR A 700  CYS A 704  ARG A 751                               
SITE     1 AC2  5 SER A 860  ASN A 909  ASN A 911  ASN B 398                    
SITE     2 AC2  5 GLU B 400                                                     
CRYST1  105.260  140.725  210.367  90.00  90.00  90.00 P 21 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      0.009500  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007106  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004754        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system