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Database: PDB
Entry: 3MDJ
LinkDB: 3MDJ
Original site: 3MDJ 
HEADER    HYDROLASE/HYDROLASE INHIBITOR           30-MAR-10   3MDJ              
TITLE     ER AMINOPEPTIDASE, ERAP1, BOUND TO THE ZINC AMINOPEPTIDASE INHIBITOR, 
TITLE    2 BESTATIN                                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ENDOPLASMIC RETICULUM AMINOPEPTIDASE 1;                    
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 FRAGMENT: UNP RESIDUES 37-939;                                       
COMPND   5 SYNONYM: ADIPOCYTE-DERIVED LEUCINE AMINOPEPTIDASE, A-LAP, ARTS-1,    
COMPND   6 AMINOPEPTIDASE PILS, PUROMYCIN-INSENSITIVE LEUCYL-SPECIFIC           
COMPND   7 AMINOPEPTIDASE, PILS-AP, TYPE 1 TUMOR NECROSIS FACTOR RECEPTOR       
COMPND   8 SHEDDING AMINOPEPTIDASE REGULATOR;                                   
COMPND   9 EC: 3.4.11.-;                                                        
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: ERAP1, APPILS, ARTS1, KIAA0525, UNQ584/PRO1154;                
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: HI5;                                       
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    AMINOPEPTIDASE, ZN BINDING PROTEIN, ER, HYDROLASE-HYDROLASE INHIBITOR 
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.T.NGUYEN,L.J.STERN                                                  
REVDAT   5   08-NOV-17 3MDJ    1       REMARK                                   
REVDAT   4   27-JUL-11 3MDJ    1       MTRIX1 MTRIX2 MTRIX3                     
REVDAT   3   22-JUN-11 3MDJ    1       JRNL                                     
REVDAT   2   06-APR-11 3MDJ    1       SOURCE                                   
REVDAT   1   30-MAR-11 3MDJ    0                                                
JRNL        AUTH   T.T.NGUYEN,S.C.CHANG,I.EVNOUCHIDOU,I.A.YORK,C.ZIKOS,         
JRNL        AUTH 2 K.L.ROCK,A.L.GOLDBERG,E.STRATIKOS,L.J.STERN                  
JRNL        TITL   STRUCTURAL BASIS FOR ANTIGENIC PEPTIDE PRECURSOR PROCESSING  
JRNL        TITL 2 BY THE ENDOPLASMIC RETICULUM AMINOPEPTIDASE ERAP1.           
JRNL        REF    NAT.STRUCT.MOL.BIOL.          V.  18   604 2011              
JRNL        REFN                   ISSN 1545-9993                               
JRNL        PMID   21478864                                                     
JRNL        DOI    10.1038/NSMB.2021                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.95 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.5_2                                         
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) : 2.95                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.11                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 63753                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.202                           
REMARK   3   R VALUE            (WORKING SET) : 0.199                           
REMARK   3   FREE R VALUE                     : 0.264                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.030                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3207                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 38.1089 -  6.3468    1.00     6127   307  0.2026 0.2198        
REMARK   3     2  6.3468 -  5.0413    1.00     6039   360  0.1891 0.2636        
REMARK   3     3  5.0413 -  4.4051    1.00     6074   312  0.1564 0.2157        
REMARK   3     4  4.4051 -  4.0028    1.00     6099   287  0.1634 0.2604        
REMARK   3     5  4.0028 -  3.7162    1.00     6056   325  0.1751 0.2543        
REMARK   3     6  3.7162 -  3.4973    1.00     6057   344  0.1910 0.2675        
REMARK   3     7  3.4973 -  3.3222    1.00     6069   315  0.2150 0.3111        
REMARK   3     8  3.3222 -  3.1777    1.00     6040   306  0.2334 0.3098        
REMARK   3     9  3.1777 -  3.0554    1.00     6061   324  0.2496 0.3221        
REMARK   3    10  3.0554 -  2.9500    0.99     5924   327  0.2763 0.3294        
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              : 0.28                                          
REMARK   3   B_SOL              : 37.86                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.410            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.240           
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) : 13.68800                                             
REMARK   3    B22 (A**2) : -10.04050                                            
REMARK   3    B33 (A**2) : -3.64740                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 8.17210                                              
REMARK   3    B23 (A**2) : 0.00000                                              
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      :  0.005          20662                                  
REMARK   3   ANGLE     :  0.850          27972                                  
REMARK   3   CHIRALITY :  0.055           3159                                  
REMARK   3   PLANARITY :  0.003           3481                                  
REMARK   3   DIHEDRAL  : 22.052          12355                                  
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 34:1000)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -14.1236  52.6348 -16.8763              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0447 T22:   0.0968                                     
REMARK   3      T33:   0.0285 T12:  -0.0090                                     
REMARK   3      T13:  -0.0550 T23:   0.0317                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7390 L22:   0.8007                                     
REMARK   3      L33:   0.8592 L12:  -0.5379                                     
REMARK   3      L13:  -0.6555 L23:   0.4505                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0445 S12:  -0.0011 S13:  -0.0492                       
REMARK   3      S21:   0.0368 S22:  -0.0023 S23:   0.1424                       
REMARK   3      S31:   0.1656 S32:  -0.0907 S33:  -0.0526                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 34:1000)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  30.0089  84.7712 -64.3253              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0194 T22:   0.0516                                     
REMARK   3      T33:   0.0491 T12:   0.0433                                     
REMARK   3      T13:   0.0224 T23:  -0.0176                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7423 L22:   0.7999                                     
REMARK   3      L33:   0.9222 L12:   0.2174                                     
REMARK   3      L13:  -0.1625 L23:  -0.1322                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0762 S12:   0.0507 S13:  -0.0382                       
REMARK   3      S21:  -0.1727 S22:  -0.0274 S23:  -0.2153                       
REMARK   3      S31:   0.0504 S32:   0.0416 S33:  -0.0183                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: (CHAIN C AND RESID 34:1000)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -16.5067 124.9615 -24.5819              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0027 T22:   0.0285                                     
REMARK   3      T33:   0.0904 T12:  -0.0260                                     
REMARK   3      T13:  -0.0879 T23:  -0.0302                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7978 L22:   1.1735                                     
REMARK   3      L33:   0.4903 L12:   0.1939                                     
REMARK   3      L13:  -0.3153 L23:  -0.1806                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0198 S12:  -0.0345 S13:   0.0684                       
REMARK   3      S21:  -0.0976 S22:  -0.0232 S23:   0.2106                       
REMARK   3      S31:  -0.0719 S32:  -0.0221 S33:   0.0587                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 5                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESSEQ 46:141) AND (NOT        
REMARK   3                          ELEMENT H) AND (NOT ELEMENT D)              
REMARK   3     SELECTION          : CHAIN B AND (RESSEQ 46:141) AND (NOT        
REMARK   3                          ELEMENT H) AND (NOT ELEMENT D)              
REMARK   3     ATOM PAIRS NUMBER  : 756                                         
REMARK   3     RMSD               : 1.839                                       
REMARK   3    NCS OPERATOR : 2                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESSEQ 46:141) AND (NOT        
REMARK   3                          ELEMENT H) AND (NOT ELEMENT D)              
REMARK   3     SELECTION          : CHAIN C AND (RESSEQ 46:141) AND (NOT        
REMARK   3                          ELEMENT H) AND (NOT ELEMENT D)              
REMARK   3     ATOM PAIRS NUMBER  : 756                                         
REMARK   3     RMSD               : 0.822                                       
REMARK   3   NCS GROUP : 2                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESSEQ 142:501) AND (NOT       
REMARK   3                          ELEMENT H) AND (NOT ELEMENT D)              
REMARK   3     SELECTION          : CHAIN B AND (RESSEQ 142:501) AND (NOT       
REMARK   3                          ELEMENT H) AND (NOT ELEMENT D)              
REMARK   3     ATOM PAIRS NUMBER  : 2607                                        
REMARK   3     RMSD               : 0.384                                       
REMARK   3    NCS OPERATOR : 2                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESSEQ 142:501) AND (NOT       
REMARK   3                          ELEMENT H) AND (NOT ELEMENT D)              
REMARK   3     SELECTION          : CHAIN C AND (RESSEQ 142:501) AND (NOT       
REMARK   3                          ELEMENT H) AND (NOT ELEMENT D)              
REMARK   3     ATOM PAIRS NUMBER  : 2607                                        
REMARK   3     RMSD               : 0.392                                       
REMARK   3   NCS GROUP : 3                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESSEQ 502:602) AND (NOT       
REMARK   3                          ELEMENT H) AND (NOT ELEMENT D)              
REMARK   3     SELECTION          : CHAIN B AND (RESSEQ 502:602) AND (NOT       
REMARK   3                          ELEMENT H) AND (NOT ELEMENT D)              
REMARK   3     ATOM PAIRS NUMBER  : 701                                         
REMARK   3     RMSD               : 0.395                                       
REMARK   3    NCS OPERATOR : 2                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESSEQ 502:602) AND (NOT       
REMARK   3                          ELEMENT H) AND (NOT ELEMENT D)              
REMARK   3     SELECTION          : CHAIN C AND (RESSEQ 502:602) AND (NOT       
REMARK   3                          ELEMENT H) AND (NOT ELEMENT D)              
REMARK   3     ATOM PAIRS NUMBER  : 701                                         
REMARK   3     RMSD               : 0.618                                       
REMARK   3   NCS GROUP : 4                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESSEQ 603:698) AND (NOT       
REMARK   3                          ELEMENT H) AND (NOT ELEMENT D)              
REMARK   3     SELECTION          : CHAIN B AND (RESSEQ 603:698) AND (NOT       
REMARK   3                          ELEMENT H) AND (NOT ELEMENT D)              
REMARK   3     ATOM PAIRS NUMBER  : 763                                         
REMARK   3     RMSD               : 0.503                                       
REMARK   3    NCS OPERATOR : 2                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESSEQ 603:698) AND (NOT       
REMARK   3                          ELEMENT H) AND (NOT ELEMENT D)              
REMARK   3     SELECTION          : CHAIN C AND (RESSEQ 603:698) AND (NOT       
REMARK   3                          ELEMENT H) AND (NOT ELEMENT D)              
REMARK   3     ATOM PAIRS NUMBER  : 763                                         
REMARK   3     RMSD               : 0.533                                       
REMARK   3   NCS GROUP : 5                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESSEQ 699:934) AND (NOT       
REMARK   3                          ELEMENT H) AND (NOT ELEMENT D)              
REMARK   3     SELECTION          : CHAIN B AND (RESSEQ 699:934) AND (NOT       
REMARK   3                          ELEMENT H) AND (NOT ELEMENT D)              
REMARK   3     ATOM PAIRS NUMBER  : 1798                                        
REMARK   3     RMSD               : 0.747                                       
REMARK   3    NCS OPERATOR : 2                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESSEQ 699:934) AND (NOT       
REMARK   3                          ELEMENT H) AND (NOT ELEMENT D)              
REMARK   3     SELECTION          : CHAIN C AND (RESSEQ 699:934) AND (NOT       
REMARK   3                          ELEMENT H) AND (NOT ELEMENT D)              
REMARK   3     ATOM PAIRS NUMBER  : 1798                                        
REMARK   3     RMSD               : 0.581                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3MDJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-APR-10.                  
REMARK 100 THE DEPOSITION ID IS D_1000058411.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-JUN-08                          
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X29A                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0809                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 63768                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.950                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : 0.16200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.1000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.95                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.06                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.40                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.76500                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER, RESOLVE                                       
REMARK 200 STARTING MODEL: PDB ENTRY 1Z5H                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.98                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 14% PEG 8000, 0.1M BICINE PH 8.5, 1MM    
REMARK 280  GLUTATHIONE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K, PH    
REMARK 280  7.5                                                                 
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000      117.31750            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
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     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     THR A    45                                                      
REMARK 465     ALA A   111                                                      
REMARK 465     GLY A   112                                                      
REMARK 465     GLU A   113                                                      
REMARK 465     HIS A   417                                                      
REMARK 465     PRO A   418                                                      
REMARK 465     VAL A   419                                                      
REMARK 465     SER A   420                                                      
REMARK 465     THR A   421                                                      
REMARK 465     PRO A   422                                                      
REMARK 465     VAL A   423                                                      
REMARK 465     GLU A   424                                                      
REMARK 465     ASN A   425                                                      
REMARK 465     PRO A   426                                                      
REMARK 465     ALA A   427                                                      
REMARK 465     GLN A   428                                                      
REMARK 465     ILE A   429                                                      
REMARK 465     ARG A   430                                                      
REMARK 465     GLU A   431                                                      
REMARK 465     MET A   432                                                      
REMARK 465     PHE A   433                                                      
REMARK 465     CYS A   486                                                      
REMARK 465     PRO A   487                                                      
REMARK 465     THR A   488                                                      
REMARK 465     ASP A   489                                                      
REMARK 465     GLY A   490                                                      
REMARK 465     VAL A   491                                                      
REMARK 465     LYS A   492                                                      
REMARK 465     GLY A   493                                                      
REMARK 465     MET A   494                                                      
REMARK 465     ASP A   495                                                      
REMARK 465     GLY A   496                                                      
REMARK 465     PHE A   497                                                      
REMARK 465     CYS A   498                                                      
REMARK 465     SER A   499                                                      
REMARK 465     ARG A   500                                                      
REMARK 465     SER A   501                                                      
REMARK 465     GLN A   502                                                      
REMARK 465     HIS A   503                                                      
REMARK 465     SER A   504                                                      
REMARK 465     SER A   505                                                      
REMARK 465     SER A   506                                                      
REMARK 465     SER A   507                                                      
REMARK 465     SER A   508                                                      
REMARK 465     HIS A   509                                                      
REMARK 465     TRP A   510                                                      
REMARK 465     HIS A   511                                                      
REMARK 465     GLN A   512                                                      
REMARK 465     GLU A   513                                                      
REMARK 465     ARG A   514                                                      
REMARK 465     GLY A   552                                                      
REMARK 465     SER A   553                                                      
REMARK 465     ASP A   554                                                      
REMARK 465     GLY A   555                                                      
REMARK 465     PHE A   864                                                      
REMARK 465     GLU A   865                                                      
REMARK 465     LEU A   866                                                      
REMARK 465     GLY A   867                                                      
REMARK 465     GLY A   893                                                      
REMARK 465     PHE A   894                                                      
REMARK 465     PHE A   895                                                      
REMARK 465     SER A   896                                                      
REMARK 465     SER A   897                                                      
REMARK 465     LEU A   898                                                      
REMARK 465     LYS A   899                                                      
REMARK 465     GLU A   900                                                      
REMARK 465     ASN A   901                                                      
REMARK 465     GLY A   902                                                      
REMARK 465     SER A   903                                                      
REMARK 465     GLN A   904                                                      
REMARK 465     LEU A   905                                                      
REMARK 465     ARG A   906                                                      
REMARK 465     SER A   935                                                      
REMARK 465     GLU A   936                                                      
REMARK 465     LYS A   937                                                      
REMARK 465     LEU A   938                                                      
REMARK 465     GLU A   939                                                      
REMARK 465     HIS A   940                                                      
REMARK 465     ASP A   941                                                      
REMARK 465     PRO A   942                                                      
REMARK 465     GLU A   943                                                      
REMARK 465     ALA A   944                                                      
REMARK 465     ASP A   945                                                      
REMARK 465     ALA A   946                                                      
REMARK 465     THR A   947                                                      
REMARK 465     GLY A   948                                                      
REMARK 465     LEU A   949                                                      
REMARK 465     GLU A   950                                                      
REMARK 465     ARG A   951                                                      
REMARK 465     MET A   952                                                      
REMARK 465     LEU A   953                                                      
REMARK 465     GLU A   954                                                      
REMARK 465     SER A   955                                                      
REMARK 465     ARG A   956                                                      
REMARK 465     GLY A   957                                                      
REMARK 465     ALA B    37                                                      
REMARK 465     SER B    38                                                      
REMARK 465     PRO B    39                                                      
REMARK 465     LYS B    40                                                      
REMARK 465     ARG B    41                                                      
REMARK 465     SER B    42                                                      
REMARK 465     ASP B    43                                                      
REMARK 465     GLY B    44                                                      
REMARK 465     THR B    45                                                      
REMARK 465     HIS B   417                                                      
REMARK 465     PRO B   418                                                      
REMARK 465     VAL B   419                                                      
REMARK 465     SER B   420                                                      
REMARK 465     THR B   421                                                      
REMARK 465     PRO B   422                                                      
REMARK 465     VAL B   423                                                      
REMARK 465     GLU B   424                                                      
REMARK 465     ASN B   425                                                      
REMARK 465     PRO B   426                                                      
REMARK 465     ALA B   427                                                      
REMARK 465     GLN B   428                                                      
REMARK 465     ILE B   429                                                      
REMARK 465     ARG B   430                                                      
REMARK 465     GLU B   431                                                      
REMARK 465     MET B   432                                                      
REMARK 465     PHE B   433                                                      
REMARK 465     CYS B   486                                                      
REMARK 465     PRO B   487                                                      
REMARK 465     THR B   488                                                      
REMARK 465     ASP B   489                                                      
REMARK 465     GLY B   490                                                      
REMARK 465     VAL B   491                                                      
REMARK 465     LYS B   492                                                      
REMARK 465     GLY B   493                                                      
REMARK 465     MET B   494                                                      
REMARK 465     ASP B   495                                                      
REMARK 465     GLY B   496                                                      
REMARK 465     PHE B   497                                                      
REMARK 465     CYS B   498                                                      
REMARK 465     SER B   499                                                      
REMARK 465     ARG B   500                                                      
REMARK 465     SER B   501                                                      
REMARK 465     GLN B   502                                                      
REMARK 465     HIS B   503                                                      
REMARK 465     SER B   504                                                      
REMARK 465     SER B   505                                                      
REMARK 465     SER B   506                                                      
REMARK 465     SER B   507                                                      
REMARK 465     SER B   508                                                      
REMARK 465     HIS B   509                                                      
REMARK 465     TRP B   510                                                      
REMARK 465     HIS B   511                                                      
REMARK 465     GLN B   512                                                      
REMARK 465     GLU B   513                                                      
REMARK 465     ARG B   514                                                      
REMARK 465     GLY B   552                                                      
REMARK 465     SER B   553                                                      
REMARK 465     ASP B   554                                                      
REMARK 465     GLY B   555                                                      
REMARK 465     PHE B   864                                                      
REMARK 465     GLU B   865                                                      
REMARK 465     LEU B   866                                                      
REMARK 465     GLY B   867                                                      
REMARK 465     GLY B   893                                                      
REMARK 465     PHE B   894                                                      
REMARK 465     PHE B   895                                                      
REMARK 465     SER B   896                                                      
REMARK 465     SER B   897                                                      
REMARK 465     LEU B   898                                                      
REMARK 465     LYS B   899                                                      
REMARK 465     GLU B   900                                                      
REMARK 465     ASN B   901                                                      
REMARK 465     GLY B   902                                                      
REMARK 465     SER B   903                                                      
REMARK 465     GLN B   904                                                      
REMARK 465     LEU B   905                                                      
REMARK 465     ARG B   906                                                      
REMARK 465     SER B   935                                                      
REMARK 465     GLU B   936                                                      
REMARK 465     LYS B   937                                                      
REMARK 465     LEU B   938                                                      
REMARK 465     GLU B   939                                                      
REMARK 465     HIS B   940                                                      
REMARK 465     ASP B   941                                                      
REMARK 465     PRO B   942                                                      
REMARK 465     GLU B   943                                                      
REMARK 465     ALA B   944                                                      
REMARK 465     ASP B   945                                                      
REMARK 465     ALA B   946                                                      
REMARK 465     THR B   947                                                      
REMARK 465     GLY B   948                                                      
REMARK 465     LEU B   949                                                      
REMARK 465     GLU B   950                                                      
REMARK 465     ARG B   951                                                      
REMARK 465     MET B   952                                                      
REMARK 465     LEU B   953                                                      
REMARK 465     GLU B   954                                                      
REMARK 465     SER B   955                                                      
REMARK 465     ARG B   956                                                      
REMARK 465     GLY B   957                                                      
REMARK 465     ALA C    37                                                      
REMARK 465     SER C    38                                                      
REMARK 465     PRO C    39                                                      
REMARK 465     LYS C    40                                                      
REMARK 465     ARG C    41                                                      
REMARK 465     SER C    42                                                      
REMARK 465     ASP C    43                                                      
REMARK 465     GLY C    44                                                      
REMARK 465     THR C    45                                                      
REMARK 465     ALA C   111                                                      
REMARK 465     GLY C   112                                                      
REMARK 465     HIS C   417                                                      
REMARK 465     PRO C   418                                                      
REMARK 465     VAL C   419                                                      
REMARK 465     SER C   420                                                      
REMARK 465     THR C   421                                                      
REMARK 465     PRO C   422                                                      
REMARK 465     VAL C   423                                                      
REMARK 465     GLU C   424                                                      
REMARK 465     ASN C   425                                                      
REMARK 465     PRO C   426                                                      
REMARK 465     ALA C   427                                                      
REMARK 465     GLN C   428                                                      
REMARK 465     ILE C   429                                                      
REMARK 465     ARG C   430                                                      
REMARK 465     GLU C   431                                                      
REMARK 465     MET C   432                                                      
REMARK 465     PHE C   433                                                      
REMARK 465     CYS C   486                                                      
REMARK 465     PRO C   487                                                      
REMARK 465     THR C   488                                                      
REMARK 465     ASP C   489                                                      
REMARK 465     GLY C   490                                                      
REMARK 465     VAL C   491                                                      
REMARK 465     LYS C   492                                                      
REMARK 465     GLY C   493                                                      
REMARK 465     MET C   494                                                      
REMARK 465     ASP C   495                                                      
REMARK 465     GLY C   496                                                      
REMARK 465     PHE C   497                                                      
REMARK 465     CYS C   498                                                      
REMARK 465     SER C   499                                                      
REMARK 465     ARG C   500                                                      
REMARK 465     SER C   501                                                      
REMARK 465     GLN C   502                                                      
REMARK 465     HIS C   503                                                      
REMARK 465     SER C   504                                                      
REMARK 465     SER C   505                                                      
REMARK 465     SER C   506                                                      
REMARK 465     SER C   507                                                      
REMARK 465     SER C   508                                                      
REMARK 465     HIS C   509                                                      
REMARK 465     TRP C   510                                                      
REMARK 465     HIS C   511                                                      
REMARK 465     GLN C   512                                                      
REMARK 465     GLU C   513                                                      
REMARK 465     ARG C   514                                                      
REMARK 465     GLY C   552                                                      
REMARK 465     SER C   553                                                      
REMARK 465     ASP C   554                                                      
REMARK 465     GLY C   555                                                      
REMARK 465     PHE C   864                                                      
REMARK 465     GLU C   865                                                      
REMARK 465     LEU C   866                                                      
REMARK 465     GLY C   867                                                      
REMARK 465     GLY C   893                                                      
REMARK 465     PHE C   894                                                      
REMARK 465     PHE C   895                                                      
REMARK 465     SER C   896                                                      
REMARK 465     SER C   897                                                      
REMARK 465     LEU C   898                                                      
REMARK 465     LYS C   899                                                      
REMARK 465     GLU C   900                                                      
REMARK 465     ASN C   901                                                      
REMARK 465     GLY C   902                                                      
REMARK 465     SER C   903                                                      
REMARK 465     GLN C   904                                                      
REMARK 465     LEU C   905                                                      
REMARK 465     ARG C   906                                                      
REMARK 465     SER C   935                                                      
REMARK 465     GLU C   936                                                      
REMARK 465     LYS C   937                                                      
REMARK 465     LEU C   938                                                      
REMARK 465     GLU C   939                                                      
REMARK 465     HIS C   940                                                      
REMARK 465     ASP C   941                                                      
REMARK 465     PRO C   942                                                      
REMARK 465     GLU C   943                                                      
REMARK 465     ALA C   944                                                      
REMARK 465     ASP C   945                                                      
REMARK 465     ALA C   946                                                      
REMARK 465     THR C   947                                                      
REMARK 465     GLY C   948                                                      
REMARK 465     LEU C   949                                                      
REMARK 465     GLU C   950                                                      
REMARK 465     ARG C   951                                                      
REMARK 465     MET C   952                                                      
REMARK 465     LEU C   953                                                      
REMARK 465     GLU C   954                                                      
REMARK 465     SER C   955                                                      
REMARK 465     ARG C   956                                                      
REMARK 465     GLY C   957                                                      
REMARK 475                                                                      
REMARK 475 ZERO OCCUPANCY RESIDUES                                              
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.             
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT                
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;                      
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)          
REMARK 475   M RES C  SSEQI                                                     
REMARK 475     GLN C   790                                                      
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     ARG A  114   CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 480     ARG A  127   CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 480     LYS A  798   CB   CG   CD   CE   NZ                              
REMARK 480     LYS A  823   CB   CG   CD   CE   NZ                              
REMARK 480     LYS A  828   CG   CD   CE   NZ                                   
REMARK 480     LEU A  853   CB   CG   CD1  CD2                                  
REMARK 480     LYS A  855   CB   CG   CD   CE   NZ                              
REMARK 480     ASN A  858   CB   CG   OD1  ND2                                  
REMARK 480     LYS A  859   CG   CD   CE   NZ                                   
REMARK 480     GLN A  909   CB   CG   CD   OE1  NE2                             
REMARK 480     GLN A  910   CB   CG   CD   OE1  NE2                             
REMARK 480     ASP B  575   CB   CG   OD1  OD2                                  
REMARK 480     GLN B  790   CB   CG   CD   OE1  NE2                             
REMARK 480     LYS B  798   CB   CG   CD   CE   NZ                              
REMARK 480     ASP B  825   CB   CG   OD1  OD2                                  
REMARK 480     LYS B  826   CB   CG   CD   CE   NZ                              
REMARK 480     ILE B  827   CB   CG1  CG2  CD1                                  
REMARK 480     LYS B  828   CG   CD   CE   NZ                                   
REMARK 480     GLN B  851   CB   CG   CD   OE1  NE2                             
REMARK 480     LYS B  859   CG   CD   CE   NZ                                   
REMARK 480     GLN B  909   CB   CG   CD   OE1  NE2                             
REMARK 480     GLN B  910   CB   CG   CD   OE1  NE2                             
REMARK 480     ARG C  114   CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 480     ARG C  127   CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 480     LYS C  573   CG   CD   CE   NZ                                   
REMARK 480     ASP C  575   CB   CG   OD1  OD2                                  
REMARK 480     GLU C  593   CG   CD   OE1  OE2                                  
REMARK 480     LYS C  798   CB   CG   CD   CE   NZ                              
REMARK 480     LYS C  823   CB   CG   CD   CE   NZ                              
REMARK 480     LYS C  828   CG   CD   CE   NZ                                   
REMARK 480     LYS C  859   CG   CD   CE   NZ                                   
REMARK 480     GLN C  862   CB   CG   CD   OE1  NE2                             
REMARK 480     GLN C  909   CB   CG   CD   OE1  NE2                             
REMARK 480     GLN C  910   CB   CG   CD   OE1  NE2                             
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O4   NAG B  5001     O5   NAG B  5002              1.86            
REMARK 500   ND2  ASN B   154     O5   NAG B  6000              1.93            
REMARK 500   OE1  GLU B   320     N2   BES B  1001              1.93            
REMARK 500   OD1  ASN A   760     O5   NAG A  6001              2.13            
REMARK 500   O4   NAG C  5001     O5   NAG C  5002              2.15            
REMARK 500   O4   NAG C  5002     C2   BMA C  5003              2.18            
REMARK 500   O4   NAG A  5002     C2   BMA A  5003              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PRO A  48       30.76    -83.88                                   
REMARK 500    THR A  90      148.74   -173.25                                   
REMARK 500    THR A 185       34.03   -141.13                                   
REMARK 500    GLU A 229      -78.19    -49.88                                   
REMARK 500    SER A 252     -159.65   -165.28                                   
REMARK 500    ASN A 321      126.01    -39.62                                   
REMARK 500    LEU A 324       72.93   -151.08                                   
REMARK 500    LEU A 332      -43.11   -142.92                                   
REMARK 500    GLU A 337       53.14   -112.75                                   
REMARK 500    SER A 340      174.65    177.16                                   
REMARK 500    TRP A 359      -70.09    -91.62                                   
REMARK 500    ASP A 558       85.28   -161.73                                   
REMARK 500    SER A 574      159.31    -49.19                                   
REMARK 500    ASP A 614     -120.18     51.30                                   
REMARK 500    LYS A 689       34.47    -95.48                                   
REMARK 500    ARG A 708      -65.88    -29.67                                   
REMARK 500    TRP A 716       50.64   -100.40                                   
REMARK 500    PHE A 791       30.07    -91.51                                   
REMARK 500    LEU A 793       33.83     70.57                                   
REMARK 500    GLU A 802      -39.04    -33.61                                   
REMARK 500    ILE A 827      148.18    176.84                                   
REMARK 500    LYS A 828      -97.09   -127.13                                   
REMARK 500    GLU A 831      -32.21   -134.93                                   
REMARK 500    LYS A 855      -74.86    -47.61                                   
REMARK 500    VAL A 908       34.70    -76.99                                   
REMARK 500    VAL B  61      -45.60   -130.42                                   
REMARK 500    GLU B 113      -72.41    -75.07                                   
REMARK 500    GLU B 229      -70.59    -51.01                                   
REMARK 500    SER B 252     -160.30   -171.21                                   
REMARK 500    LEU B 324       80.83   -151.11                                   
REMARK 500    LEU B 332      -35.84   -136.50                                   
REMARK 500    GLU B 337       62.33   -107.47                                   
REMARK 500    SER B 340      169.54    176.41                                   
REMARK 500    TRP B 359      -65.98   -101.27                                   
REMARK 500    TYR B 451      -70.75    -64.00                                   
REMARK 500    LYS B 471     -165.15   -129.77                                   
REMARK 500    ASP B 558       82.69   -160.14                                   
REMARK 500    ASP B 614     -129.88     51.17                                   
REMARK 500    LYS B 689       44.80   -103.43                                   
REMARK 500    TRP B 716       55.63   -103.94                                   
REMARK 500    SER B 792      -72.15   -138.09                                   
REMARK 500    LEU B 793      133.18    -39.89                                   
REMARK 500    ILE B 827      147.36   -177.39                                   
REMARK 500    LYS B 828      -97.64   -126.23                                   
REMARK 500    GLU B 831      -34.58   -134.88                                   
REMARK 500    LYS B 855      -74.14    -49.03                                   
REMARK 500    VAL B 908       39.97    -76.79                                   
REMARK 500    LEU B 933        1.87    -67.84                                   
REMARK 500    VAL C  61      -42.43   -139.00                                   
REMARK 500    ARG C 114      117.23   -164.04                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      68 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1000  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 BES B1001   O2                                                     
REMARK 620 2 HIS B 353   NE2 116.4                                              
REMARK 620 3 GLU B 376   OE1 118.6  86.4                                        
REMARK 620 4 HIS B 357   NE2 114.0  98.2 117.8                                  
REMARK 620 5 GLU B 376   OE2 102.6 135.4  54.9  84.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1000  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 353   NE2                                                    
REMARK 620 2 GLU A 376   OE1  84.5                                              
REMARK 620 3 HIS A 357   NE2  95.5 113.3                                        
REMARK 620 4 BES A1001   O2   99.2 128.3 117.4                                  
REMARK 620 5 GLU A 376   OE2 136.3  56.5  84.4 119.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C1000  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 353   NE2                                                    
REMARK 620 2 GLU C 376   OE1  79.0                                              
REMARK 620 3 HIS C 357   NE2 102.8 102.8                                        
REMARK 620 4 BES C1001   O2  122.0 119.3 122.0                                  
REMARK 620 5 GLU C 376   OE2 131.0  54.6  76.0  96.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1000                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BES A 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 5001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 5002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 5003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 5004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 5005                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 6000                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 6001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 1000                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BES B 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 5001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 5002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 6000                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 1000                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BES C 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 5001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 5002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA C 5003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN C 5004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN C 5005                
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 SEQUENCE CONFLICT IN UNP ENTRY Q9NZ08 AT THESE POSITIONS             
DBREF  3MDJ A   37   939  UNP    Q9NZ08   ERAP1_HUMAN     37    939             
DBREF  3MDJ B   37   939  UNP    Q9NZ08   ERAP1_HUMAN     37    939             
DBREF  3MDJ C   37   939  UNP    Q9NZ08   ERAP1_HUMAN     37    939             
SEQADV 3MDJ ASP A  346  UNP  Q9NZ08    GLY   346 SEE REMARK 999                 
SEQADV 3MDJ ARG A  514  UNP  Q9NZ08    GLY   514 SEE REMARK 999                 
SEQADV 3MDJ ARG A  528  UNP  Q9NZ08    LYS   528 SEE REMARK 999                 
SEQADV 3MDJ GLU A  730  UNP  Q9NZ08    GLN   730 SEE REMARK 999                 
SEQADV 3MDJ HIS A  940  UNP  Q9NZ08              EXPRESSION TAG                 
SEQADV 3MDJ ASP A  941  UNP  Q9NZ08              EXPRESSION TAG                 
SEQADV 3MDJ PRO A  942  UNP  Q9NZ08              EXPRESSION TAG                 
SEQADV 3MDJ GLU A  943  UNP  Q9NZ08              EXPRESSION TAG                 
SEQADV 3MDJ ALA A  944  UNP  Q9NZ08              EXPRESSION TAG                 
SEQADV 3MDJ ASP A  945  UNP  Q9NZ08              EXPRESSION TAG                 
SEQADV 3MDJ ALA A  946  UNP  Q9NZ08              EXPRESSION TAG                 
SEQADV 3MDJ THR A  947  UNP  Q9NZ08              EXPRESSION TAG                 
SEQADV 3MDJ GLY A  948  UNP  Q9NZ08              EXPRESSION TAG                 
SEQADV 3MDJ LEU A  949  UNP  Q9NZ08              EXPRESSION TAG                 
SEQADV 3MDJ GLU A  950  UNP  Q9NZ08              EXPRESSION TAG                 
SEQADV 3MDJ ARG A  951  UNP  Q9NZ08              EXPRESSION TAG                 
SEQADV 3MDJ MET A  952  UNP  Q9NZ08              EXPRESSION TAG                 
SEQADV 3MDJ LEU A  953  UNP  Q9NZ08              EXPRESSION TAG                 
SEQADV 3MDJ GLU A  954  UNP  Q9NZ08              EXPRESSION TAG                 
SEQADV 3MDJ SER A  955  UNP  Q9NZ08              EXPRESSION TAG                 
SEQADV 3MDJ ARG A  956  UNP  Q9NZ08              EXPRESSION TAG                 
SEQADV 3MDJ GLY A  957  UNP  Q9NZ08              EXPRESSION TAG                 
SEQADV 3MDJ ASP B  346  UNP  Q9NZ08    GLY   346 SEE REMARK 999                 
SEQADV 3MDJ ARG B  514  UNP  Q9NZ08    GLY   514 SEE REMARK 999                 
SEQADV 3MDJ ARG B  528  UNP  Q9NZ08    LYS   528 SEE REMARK 999                 
SEQADV 3MDJ GLU B  730  UNP  Q9NZ08    GLN   730 SEE REMARK 999                 
SEQADV 3MDJ HIS B  940  UNP  Q9NZ08              EXPRESSION TAG                 
SEQADV 3MDJ ASP B  941  UNP  Q9NZ08              EXPRESSION TAG                 
SEQADV 3MDJ PRO B  942  UNP  Q9NZ08              EXPRESSION TAG                 
SEQADV 3MDJ GLU B  943  UNP  Q9NZ08              EXPRESSION TAG                 
SEQADV 3MDJ ALA B  944  UNP  Q9NZ08              EXPRESSION TAG                 
SEQADV 3MDJ ASP B  945  UNP  Q9NZ08              EXPRESSION TAG                 
SEQADV 3MDJ ALA B  946  UNP  Q9NZ08              EXPRESSION TAG                 
SEQADV 3MDJ THR B  947  UNP  Q9NZ08              EXPRESSION TAG                 
SEQADV 3MDJ GLY B  948  UNP  Q9NZ08              EXPRESSION TAG                 
SEQADV 3MDJ LEU B  949  UNP  Q9NZ08              EXPRESSION TAG                 
SEQADV 3MDJ GLU B  950  UNP  Q9NZ08              EXPRESSION TAG                 
SEQADV 3MDJ ARG B  951  UNP  Q9NZ08              EXPRESSION TAG                 
SEQADV 3MDJ MET B  952  UNP  Q9NZ08              EXPRESSION TAG                 
SEQADV 3MDJ LEU B  953  UNP  Q9NZ08              EXPRESSION TAG                 
SEQADV 3MDJ GLU B  954  UNP  Q9NZ08              EXPRESSION TAG                 
SEQADV 3MDJ SER B  955  UNP  Q9NZ08              EXPRESSION TAG                 
SEQADV 3MDJ ARG B  956  UNP  Q9NZ08              EXPRESSION TAG                 
SEQADV 3MDJ GLY B  957  UNP  Q9NZ08              EXPRESSION TAG                 
SEQADV 3MDJ ASP C  346  UNP  Q9NZ08    GLY   346 SEE REMARK 999                 
SEQADV 3MDJ ARG C  514  UNP  Q9NZ08    GLY   514 SEE REMARK 999                 
SEQADV 3MDJ ARG C  528  UNP  Q9NZ08    LYS   528 SEE REMARK 999                 
SEQADV 3MDJ GLU C  730  UNP  Q9NZ08    GLN   730 SEE REMARK 999                 
SEQADV 3MDJ HIS C  940  UNP  Q9NZ08              EXPRESSION TAG                 
SEQADV 3MDJ ASP C  941  UNP  Q9NZ08              EXPRESSION TAG                 
SEQADV 3MDJ PRO C  942  UNP  Q9NZ08              EXPRESSION TAG                 
SEQADV 3MDJ GLU C  943  UNP  Q9NZ08              EXPRESSION TAG                 
SEQADV 3MDJ ALA C  944  UNP  Q9NZ08              EXPRESSION TAG                 
SEQADV 3MDJ ASP C  945  UNP  Q9NZ08              EXPRESSION TAG                 
SEQADV 3MDJ ALA C  946  UNP  Q9NZ08              EXPRESSION TAG                 
SEQADV 3MDJ THR C  947  UNP  Q9NZ08              EXPRESSION TAG                 
SEQADV 3MDJ GLY C  948  UNP  Q9NZ08              EXPRESSION TAG                 
SEQADV 3MDJ LEU C  949  UNP  Q9NZ08              EXPRESSION TAG                 
SEQADV 3MDJ GLU C  950  UNP  Q9NZ08              EXPRESSION TAG                 
SEQADV 3MDJ ARG C  951  UNP  Q9NZ08              EXPRESSION TAG                 
SEQADV 3MDJ MET C  952  UNP  Q9NZ08              EXPRESSION TAG                 
SEQADV 3MDJ LEU C  953  UNP  Q9NZ08              EXPRESSION TAG                 
SEQADV 3MDJ GLU C  954  UNP  Q9NZ08              EXPRESSION TAG                 
SEQADV 3MDJ SER C  955  UNP  Q9NZ08              EXPRESSION TAG                 
SEQADV 3MDJ ARG C  956  UNP  Q9NZ08              EXPRESSION TAG                 
SEQADV 3MDJ GLY C  957  UNP  Q9NZ08              EXPRESSION TAG                 
SEQRES   1 A  921  ALA SER PRO LYS ARG SER ASP GLY THR PRO PHE PRO TRP          
SEQRES   2 A  921  ASN LYS ILE ARG LEU PRO GLU TYR VAL ILE PRO VAL HIS          
SEQRES   3 A  921  TYR ASP LEU LEU ILE HIS ALA ASN LEU THR THR LEU THR          
SEQRES   4 A  921  PHE TRP GLY THR THR LYS VAL GLU ILE THR ALA SER GLN          
SEQRES   5 A  921  PRO THR SER THR ILE ILE LEU HIS SER HIS HIS LEU GLN          
SEQRES   6 A  921  ILE SER ARG ALA THR LEU ARG LYS GLY ALA GLY GLU ARG          
SEQRES   7 A  921  LEU SER GLU GLU PRO LEU GLN VAL LEU GLU HIS PRO ARG          
SEQRES   8 A  921  GLN GLU GLN ILE ALA LEU LEU ALA PRO GLU PRO LEU LEU          
SEQRES   9 A  921  VAL GLY LEU PRO TYR THR VAL VAL ILE HIS TYR ALA GLY          
SEQRES  10 A  921  ASN LEU SER GLU THR PHE HIS GLY PHE TYR LYS SER THR          
SEQRES  11 A  921  TYR ARG THR LYS GLU GLY GLU LEU ARG ILE LEU ALA SER          
SEQRES  12 A  921  THR GLN PHE GLU PRO THR ALA ALA ARG MET ALA PHE PRO          
SEQRES  13 A  921  CYS PHE ASP GLU PRO ALA PHE LYS ALA SER PHE SER ILE          
SEQRES  14 A  921  LYS ILE ARG ARG GLU PRO ARG HIS LEU ALA ILE SER ASN          
SEQRES  15 A  921  MET PRO LEU VAL LYS SER VAL THR VAL ALA GLU GLY LEU          
SEQRES  16 A  921  ILE GLU ASP HIS PHE ASP VAL THR VAL LYS MET SER THR          
SEQRES  17 A  921  TYR LEU VAL ALA PHE ILE ILE SER ASP PHE GLU SER VAL          
SEQRES  18 A  921  SER LYS ILE THR LYS SER GLY VAL LYS VAL SER VAL TYR          
SEQRES  19 A  921  ALA VAL PRO ASP LYS ILE ASN GLN ALA ASP TYR ALA LEU          
SEQRES  20 A  921  ASP ALA ALA VAL THR LEU LEU GLU PHE TYR GLU ASP TYR          
SEQRES  21 A  921  PHE SER ILE PRO TYR PRO LEU PRO LYS GLN ASP LEU ALA          
SEQRES  22 A  921  ALA ILE PRO ASP PHE GLN SER GLY ALA MET GLU ASN TRP          
SEQRES  23 A  921  GLY LEU THR THR TYR ARG GLU SER ALA LEU LEU PHE ASP          
SEQRES  24 A  921  ALA GLU LYS SER SER ALA SER SER LYS LEU ASP ILE THR          
SEQRES  25 A  921  MET THR VAL ALA HIS GLU LEU ALA HIS GLN TRP PHE GLY          
SEQRES  26 A  921  ASN LEU VAL THR MET GLU TRP TRP ASN ASP LEU TRP LEU          
SEQRES  27 A  921  ASN GLU GLY PHE ALA LYS PHE MET GLU PHE VAL SER VAL          
SEQRES  28 A  921  SER VAL THR HIS PRO GLU LEU LYS VAL GLY ASP TYR PHE          
SEQRES  29 A  921  PHE GLY LYS CYS PHE ASP ALA MET GLU VAL ASP ALA LEU          
SEQRES  30 A  921  ASN SER SER HIS PRO VAL SER THR PRO VAL GLU ASN PRO          
SEQRES  31 A  921  ALA GLN ILE ARG GLU MET PHE ASP ASP VAL SER TYR ASP          
SEQRES  32 A  921  LYS GLY ALA CYS ILE LEU ASN MET LEU ARG GLU TYR LEU          
SEQRES  33 A  921  SER ALA ASP ALA PHE LYS SER GLY ILE VAL GLN TYR LEU          
SEQRES  34 A  921  GLN LYS HIS SER TYR LYS ASN THR LYS ASN GLU ASP LEU          
SEQRES  35 A  921  TRP ASP SER MET ALA SER ILE CYS PRO THR ASP GLY VAL          
SEQRES  36 A  921  LYS GLY MET ASP GLY PHE CYS SER ARG SER GLN HIS SER          
SEQRES  37 A  921  SER SER SER SER HIS TRP HIS GLN GLU ARG VAL ASP VAL          
SEQRES  38 A  921  LYS THR MET MET ASN THR TRP THR LEU GLN ARG GLY PHE          
SEQRES  39 A  921  PRO LEU ILE THR ILE THR VAL ARG GLY ARG ASN VAL HIS          
SEQRES  40 A  921  MET LYS GLN GLU HIS TYR MET LYS GLY SER ASP GLY ALA          
SEQRES  41 A  921  PRO ASP THR GLY TYR LEU TRP HIS VAL PRO LEU THR PHE          
SEQRES  42 A  921  ILE THR SER LYS SER ASP MET VAL HIS ARG PHE LEU LEU          
SEQRES  43 A  921  LYS THR LYS THR ASP VAL LEU ILE LEU PRO GLU GLU VAL          
SEQRES  44 A  921  GLU TRP ILE LYS PHE ASN VAL GLY MET ASN GLY TYR TYR          
SEQRES  45 A  921  ILE VAL HIS TYR GLU ASP ASP GLY TRP ASP SER LEU THR          
SEQRES  46 A  921  GLY LEU LEU LYS GLY THR HIS THR ALA VAL SER SER ASN          
SEQRES  47 A  921  ASP ARG ALA SER LEU ILE ASN ASN ALA PHE GLN LEU VAL          
SEQRES  48 A  921  SER ILE GLY LYS LEU SER ILE GLU LYS ALA LEU ASP LEU          
SEQRES  49 A  921  SER LEU TYR LEU LYS HIS GLU THR GLU ILE MET PRO VAL          
SEQRES  50 A  921  PHE GLN GLY LEU ASN GLU LEU ILE PRO MET TYR LYS LEU          
SEQRES  51 A  921  MET GLU LYS ARG ASP MET ASN GLU VAL GLU THR GLN PHE          
SEQRES  52 A  921  LYS ALA PHE LEU ILE ARG LEU LEU ARG ASP LEU ILE ASP          
SEQRES  53 A  921  LYS GLN THR TRP THR ASP GLU GLY SER VAL SER GLU ARG          
SEQRES  54 A  921  MET LEU ARG SER GLU LEU LEU LEU LEU ALA CYS VAL HIS          
SEQRES  55 A  921  ASN TYR GLN PRO CYS VAL GLN ARG ALA GLU GLY TYR PHE          
SEQRES  56 A  921  ARG LYS TRP LYS GLU SER ASN GLY ASN LEU SER LEU PRO          
SEQRES  57 A  921  VAL ASP VAL THR LEU ALA VAL PHE ALA VAL GLY ALA GLN          
SEQRES  58 A  921  SER THR GLU GLY TRP ASP PHE LEU TYR SER LYS TYR GLN          
SEQRES  59 A  921  PHE SER LEU SER SER THR GLU LYS SER GLN ILE GLU PHE          
SEQRES  60 A  921  ALA LEU CYS ARG THR GLN ASN LYS GLU LYS LEU GLN TRP          
SEQRES  61 A  921  LEU LEU ASP GLU SER PHE LYS GLY ASP LYS ILE LYS THR          
SEQRES  62 A  921  GLN GLU PHE PRO GLN ILE LEU THR LEU ILE GLY ARG ASN          
SEQRES  63 A  921  PRO VAL GLY TYR PRO LEU ALA TRP GLN PHE LEU ARG LYS          
SEQRES  64 A  921  ASN TRP ASN LYS LEU VAL GLN LYS PHE GLU LEU GLY SER          
SEQRES  65 A  921  SER SER ILE ALA HIS MET VAL MET GLY THR THR ASN GLN          
SEQRES  66 A  921  PHE SER THR ARG THR ARG LEU GLU GLU VAL LYS GLY PHE          
SEQRES  67 A  921  PHE SER SER LEU LYS GLU ASN GLY SER GLN LEU ARG CYS          
SEQRES  68 A  921  VAL GLN GLN THR ILE GLU THR ILE GLU GLU ASN ILE GLY          
SEQRES  69 A  921  TRP MET ASP LYS ASN PHE ASP LYS ILE ARG VAL TRP LEU          
SEQRES  70 A  921  GLN SER GLU LYS LEU GLU HIS ASP PRO GLU ALA ASP ALA          
SEQRES  71 A  921  THR GLY LEU GLU ARG MET LEU GLU SER ARG GLY                  
SEQRES   1 B  921  ALA SER PRO LYS ARG SER ASP GLY THR PRO PHE PRO TRP          
SEQRES   2 B  921  ASN LYS ILE ARG LEU PRO GLU TYR VAL ILE PRO VAL HIS          
SEQRES   3 B  921  TYR ASP LEU LEU ILE HIS ALA ASN LEU THR THR LEU THR          
SEQRES   4 B  921  PHE TRP GLY THR THR LYS VAL GLU ILE THR ALA SER GLN          
SEQRES   5 B  921  PRO THR SER THR ILE ILE LEU HIS SER HIS HIS LEU GLN          
SEQRES   6 B  921  ILE SER ARG ALA THR LEU ARG LYS GLY ALA GLY GLU ARG          
SEQRES   7 B  921  LEU SER GLU GLU PRO LEU GLN VAL LEU GLU HIS PRO ARG          
SEQRES   8 B  921  GLN GLU GLN ILE ALA LEU LEU ALA PRO GLU PRO LEU LEU          
SEQRES   9 B  921  VAL GLY LEU PRO TYR THR VAL VAL ILE HIS TYR ALA GLY          
SEQRES  10 B  921  ASN LEU SER GLU THR PHE HIS GLY PHE TYR LYS SER THR          
SEQRES  11 B  921  TYR ARG THR LYS GLU GLY GLU LEU ARG ILE LEU ALA SER          
SEQRES  12 B  921  THR GLN PHE GLU PRO THR ALA ALA ARG MET ALA PHE PRO          
SEQRES  13 B  921  CYS PHE ASP GLU PRO ALA PHE LYS ALA SER PHE SER ILE          
SEQRES  14 B  921  LYS ILE ARG ARG GLU PRO ARG HIS LEU ALA ILE SER ASN          
SEQRES  15 B  921  MET PRO LEU VAL LYS SER VAL THR VAL ALA GLU GLY LEU          
SEQRES  16 B  921  ILE GLU ASP HIS PHE ASP VAL THR VAL LYS MET SER THR          
SEQRES  17 B  921  TYR LEU VAL ALA PHE ILE ILE SER ASP PHE GLU SER VAL          
SEQRES  18 B  921  SER LYS ILE THR LYS SER GLY VAL LYS VAL SER VAL TYR          
SEQRES  19 B  921  ALA VAL PRO ASP LYS ILE ASN GLN ALA ASP TYR ALA LEU          
SEQRES  20 B  921  ASP ALA ALA VAL THR LEU LEU GLU PHE TYR GLU ASP TYR          
SEQRES  21 B  921  PHE SER ILE PRO TYR PRO LEU PRO LYS GLN ASP LEU ALA          
SEQRES  22 B  921  ALA ILE PRO ASP PHE GLN SER GLY ALA MET GLU ASN TRP          
SEQRES  23 B  921  GLY LEU THR THR TYR ARG GLU SER ALA LEU LEU PHE ASP          
SEQRES  24 B  921  ALA GLU LYS SER SER ALA SER SER LYS LEU ASP ILE THR          
SEQRES  25 B  921  MET THR VAL ALA HIS GLU LEU ALA HIS GLN TRP PHE GLY          
SEQRES  26 B  921  ASN LEU VAL THR MET GLU TRP TRP ASN ASP LEU TRP LEU          
SEQRES  27 B  921  ASN GLU GLY PHE ALA LYS PHE MET GLU PHE VAL SER VAL          
SEQRES  28 B  921  SER VAL THR HIS PRO GLU LEU LYS VAL GLY ASP TYR PHE          
SEQRES  29 B  921  PHE GLY LYS CYS PHE ASP ALA MET GLU VAL ASP ALA LEU          
SEQRES  30 B  921  ASN SER SER HIS PRO VAL SER THR PRO VAL GLU ASN PRO          
SEQRES  31 B  921  ALA GLN ILE ARG GLU MET PHE ASP ASP VAL SER TYR ASP          
SEQRES  32 B  921  LYS GLY ALA CYS ILE LEU ASN MET LEU ARG GLU TYR LEU          
SEQRES  33 B  921  SER ALA ASP ALA PHE LYS SER GLY ILE VAL GLN TYR LEU          
SEQRES  34 B  921  GLN LYS HIS SER TYR LYS ASN THR LYS ASN GLU ASP LEU          
SEQRES  35 B  921  TRP ASP SER MET ALA SER ILE CYS PRO THR ASP GLY VAL          
SEQRES  36 B  921  LYS GLY MET ASP GLY PHE CYS SER ARG SER GLN HIS SER          
SEQRES  37 B  921  SER SER SER SER HIS TRP HIS GLN GLU ARG VAL ASP VAL          
SEQRES  38 B  921  LYS THR MET MET ASN THR TRP THR LEU GLN ARG GLY PHE          
SEQRES  39 B  921  PRO LEU ILE THR ILE THR VAL ARG GLY ARG ASN VAL HIS          
SEQRES  40 B  921  MET LYS GLN GLU HIS TYR MET LYS GLY SER ASP GLY ALA          
SEQRES  41 B  921  PRO ASP THR GLY TYR LEU TRP HIS VAL PRO LEU THR PHE          
SEQRES  42 B  921  ILE THR SER LYS SER ASP MET VAL HIS ARG PHE LEU LEU          
SEQRES  43 B  921  LYS THR LYS THR ASP VAL LEU ILE LEU PRO GLU GLU VAL          
SEQRES  44 B  921  GLU TRP ILE LYS PHE ASN VAL GLY MET ASN GLY TYR TYR          
SEQRES  45 B  921  ILE VAL HIS TYR GLU ASP ASP GLY TRP ASP SER LEU THR          
SEQRES  46 B  921  GLY LEU LEU LYS GLY THR HIS THR ALA VAL SER SER ASN          
SEQRES  47 B  921  ASP ARG ALA SER LEU ILE ASN ASN ALA PHE GLN LEU VAL          
SEQRES  48 B  921  SER ILE GLY LYS LEU SER ILE GLU LYS ALA LEU ASP LEU          
SEQRES  49 B  921  SER LEU TYR LEU LYS HIS GLU THR GLU ILE MET PRO VAL          
SEQRES  50 B  921  PHE GLN GLY LEU ASN GLU LEU ILE PRO MET TYR LYS LEU          
SEQRES  51 B  921  MET GLU LYS ARG ASP MET ASN GLU VAL GLU THR GLN PHE          
SEQRES  52 B  921  LYS ALA PHE LEU ILE ARG LEU LEU ARG ASP LEU ILE ASP          
SEQRES  53 B  921  LYS GLN THR TRP THR ASP GLU GLY SER VAL SER GLU ARG          
SEQRES  54 B  921  MET LEU ARG SER GLU LEU LEU LEU LEU ALA CYS VAL HIS          
SEQRES  55 B  921  ASN TYR GLN PRO CYS VAL GLN ARG ALA GLU GLY TYR PHE          
SEQRES  56 B  921  ARG LYS TRP LYS GLU SER ASN GLY ASN LEU SER LEU PRO          
SEQRES  57 B  921  VAL ASP VAL THR LEU ALA VAL PHE ALA VAL GLY ALA GLN          
SEQRES  58 B  921  SER THR GLU GLY TRP ASP PHE LEU TYR SER LYS TYR GLN          
SEQRES  59 B  921  PHE SER LEU SER SER THR GLU LYS SER GLN ILE GLU PHE          
SEQRES  60 B  921  ALA LEU CYS ARG THR GLN ASN LYS GLU LYS LEU GLN TRP          
SEQRES  61 B  921  LEU LEU ASP GLU SER PHE LYS GLY ASP LYS ILE LYS THR          
SEQRES  62 B  921  GLN GLU PHE PRO GLN ILE LEU THR LEU ILE GLY ARG ASN          
SEQRES  63 B  921  PRO VAL GLY TYR PRO LEU ALA TRP GLN PHE LEU ARG LYS          
SEQRES  64 B  921  ASN TRP ASN LYS LEU VAL GLN LYS PHE GLU LEU GLY SER          
SEQRES  65 B  921  SER SER ILE ALA HIS MET VAL MET GLY THR THR ASN GLN          
SEQRES  66 B  921  PHE SER THR ARG THR ARG LEU GLU GLU VAL LYS GLY PHE          
SEQRES  67 B  921  PHE SER SER LEU LYS GLU ASN GLY SER GLN LEU ARG CYS          
SEQRES  68 B  921  VAL GLN GLN THR ILE GLU THR ILE GLU GLU ASN ILE GLY          
SEQRES  69 B  921  TRP MET ASP LYS ASN PHE ASP LYS ILE ARG VAL TRP LEU          
SEQRES  70 B  921  GLN SER GLU LYS LEU GLU HIS ASP PRO GLU ALA ASP ALA          
SEQRES  71 B  921  THR GLY LEU GLU ARG MET LEU GLU SER ARG GLY                  
SEQRES   1 C  921  ALA SER PRO LYS ARG SER ASP GLY THR PRO PHE PRO TRP          
SEQRES   2 C  921  ASN LYS ILE ARG LEU PRO GLU TYR VAL ILE PRO VAL HIS          
SEQRES   3 C  921  TYR ASP LEU LEU ILE HIS ALA ASN LEU THR THR LEU THR          
SEQRES   4 C  921  PHE TRP GLY THR THR LYS VAL GLU ILE THR ALA SER GLN          
SEQRES   5 C  921  PRO THR SER THR ILE ILE LEU HIS SER HIS HIS LEU GLN          
SEQRES   6 C  921  ILE SER ARG ALA THR LEU ARG LYS GLY ALA GLY GLU ARG          
SEQRES   7 C  921  LEU SER GLU GLU PRO LEU GLN VAL LEU GLU HIS PRO ARG          
SEQRES   8 C  921  GLN GLU GLN ILE ALA LEU LEU ALA PRO GLU PRO LEU LEU          
SEQRES   9 C  921  VAL GLY LEU PRO TYR THR VAL VAL ILE HIS TYR ALA GLY          
SEQRES  10 C  921  ASN LEU SER GLU THR PHE HIS GLY PHE TYR LYS SER THR          
SEQRES  11 C  921  TYR ARG THR LYS GLU GLY GLU LEU ARG ILE LEU ALA SER          
SEQRES  12 C  921  THR GLN PHE GLU PRO THR ALA ALA ARG MET ALA PHE PRO          
SEQRES  13 C  921  CYS PHE ASP GLU PRO ALA PHE LYS ALA SER PHE SER ILE          
SEQRES  14 C  921  LYS ILE ARG ARG GLU PRO ARG HIS LEU ALA ILE SER ASN          
SEQRES  15 C  921  MET PRO LEU VAL LYS SER VAL THR VAL ALA GLU GLY LEU          
SEQRES  16 C  921  ILE GLU ASP HIS PHE ASP VAL THR VAL LYS MET SER THR          
SEQRES  17 C  921  TYR LEU VAL ALA PHE ILE ILE SER ASP PHE GLU SER VAL          
SEQRES  18 C  921  SER LYS ILE THR LYS SER GLY VAL LYS VAL SER VAL TYR          
SEQRES  19 C  921  ALA VAL PRO ASP LYS ILE ASN GLN ALA ASP TYR ALA LEU          
SEQRES  20 C  921  ASP ALA ALA VAL THR LEU LEU GLU PHE TYR GLU ASP TYR          
SEQRES  21 C  921  PHE SER ILE PRO TYR PRO LEU PRO LYS GLN ASP LEU ALA          
SEQRES  22 C  921  ALA ILE PRO ASP PHE GLN SER GLY ALA MET GLU ASN TRP          
SEQRES  23 C  921  GLY LEU THR THR TYR ARG GLU SER ALA LEU LEU PHE ASP          
SEQRES  24 C  921  ALA GLU LYS SER SER ALA SER SER LYS LEU ASP ILE THR          
SEQRES  25 C  921  MET THR VAL ALA HIS GLU LEU ALA HIS GLN TRP PHE GLY          
SEQRES  26 C  921  ASN LEU VAL THR MET GLU TRP TRP ASN ASP LEU TRP LEU          
SEQRES  27 C  921  ASN GLU GLY PHE ALA LYS PHE MET GLU PHE VAL SER VAL          
SEQRES  28 C  921  SER VAL THR HIS PRO GLU LEU LYS VAL GLY ASP TYR PHE          
SEQRES  29 C  921  PHE GLY LYS CYS PHE ASP ALA MET GLU VAL ASP ALA LEU          
SEQRES  30 C  921  ASN SER SER HIS PRO VAL SER THR PRO VAL GLU ASN PRO          
SEQRES  31 C  921  ALA GLN ILE ARG GLU MET PHE ASP ASP VAL SER TYR ASP          
SEQRES  32 C  921  LYS GLY ALA CYS ILE LEU ASN MET LEU ARG GLU TYR LEU          
SEQRES  33 C  921  SER ALA ASP ALA PHE LYS SER GLY ILE VAL GLN TYR LEU          
SEQRES  34 C  921  GLN LYS HIS SER TYR LYS ASN THR LYS ASN GLU ASP LEU          
SEQRES  35 C  921  TRP ASP SER MET ALA SER ILE CYS PRO THR ASP GLY VAL          
SEQRES  36 C  921  LYS GLY MET ASP GLY PHE CYS SER ARG SER GLN HIS SER          
SEQRES  37 C  921  SER SER SER SER HIS TRP HIS GLN GLU ARG VAL ASP VAL          
SEQRES  38 C  921  LYS THR MET MET ASN THR TRP THR LEU GLN ARG GLY PHE          
SEQRES  39 C  921  PRO LEU ILE THR ILE THR VAL ARG GLY ARG ASN VAL HIS          
SEQRES  40 C  921  MET LYS GLN GLU HIS TYR MET LYS GLY SER ASP GLY ALA          
SEQRES  41 C  921  PRO ASP THR GLY TYR LEU TRP HIS VAL PRO LEU THR PHE          
SEQRES  42 C  921  ILE THR SER LYS SER ASP MET VAL HIS ARG PHE LEU LEU          
SEQRES  43 C  921  LYS THR LYS THR ASP VAL LEU ILE LEU PRO GLU GLU VAL          
SEQRES  44 C  921  GLU TRP ILE LYS PHE ASN VAL GLY MET ASN GLY TYR TYR          
SEQRES  45 C  921  ILE VAL HIS TYR GLU ASP ASP GLY TRP ASP SER LEU THR          
SEQRES  46 C  921  GLY LEU LEU LYS GLY THR HIS THR ALA VAL SER SER ASN          
SEQRES  47 C  921  ASP ARG ALA SER LEU ILE ASN ASN ALA PHE GLN LEU VAL          
SEQRES  48 C  921  SER ILE GLY LYS LEU SER ILE GLU LYS ALA LEU ASP LEU          
SEQRES  49 C  921  SER LEU TYR LEU LYS HIS GLU THR GLU ILE MET PRO VAL          
SEQRES  50 C  921  PHE GLN GLY LEU ASN GLU LEU ILE PRO MET TYR LYS LEU          
SEQRES  51 C  921  MET GLU LYS ARG ASP MET ASN GLU VAL GLU THR GLN PHE          
SEQRES  52 C  921  LYS ALA PHE LEU ILE ARG LEU LEU ARG ASP LEU ILE ASP          
SEQRES  53 C  921  LYS GLN THR TRP THR ASP GLU GLY SER VAL SER GLU ARG          
SEQRES  54 C  921  MET LEU ARG SER GLU LEU LEU LEU LEU ALA CYS VAL HIS          
SEQRES  55 C  921  ASN TYR GLN PRO CYS VAL GLN ARG ALA GLU GLY TYR PHE          
SEQRES  56 C  921  ARG LYS TRP LYS GLU SER ASN GLY ASN LEU SER LEU PRO          
SEQRES  57 C  921  VAL ASP VAL THR LEU ALA VAL PHE ALA VAL GLY ALA GLN          
SEQRES  58 C  921  SER THR GLU GLY TRP ASP PHE LEU TYR SER LYS TYR GLN          
SEQRES  59 C  921  PHE SER LEU SER SER THR GLU LYS SER GLN ILE GLU PHE          
SEQRES  60 C  921  ALA LEU CYS ARG THR GLN ASN LYS GLU LYS LEU GLN TRP          
SEQRES  61 C  921  LEU LEU ASP GLU SER PHE LYS GLY ASP LYS ILE LYS THR          
SEQRES  62 C  921  GLN GLU PHE PRO GLN ILE LEU THR LEU ILE GLY ARG ASN          
SEQRES  63 C  921  PRO VAL GLY TYR PRO LEU ALA TRP GLN PHE LEU ARG LYS          
SEQRES  64 C  921  ASN TRP ASN LYS LEU VAL GLN LYS PHE GLU LEU GLY SER          
SEQRES  65 C  921  SER SER ILE ALA HIS MET VAL MET GLY THR THR ASN GLN          
SEQRES  66 C  921  PHE SER THR ARG THR ARG LEU GLU GLU VAL LYS GLY PHE          
SEQRES  67 C  921  PHE SER SER LEU LYS GLU ASN GLY SER GLN LEU ARG CYS          
SEQRES  68 C  921  VAL GLN GLN THR ILE GLU THR ILE GLU GLU ASN ILE GLY          
SEQRES  69 C  921  TRP MET ASP LYS ASN PHE ASP LYS ILE ARG VAL TRP LEU          
SEQRES  70 C  921  GLN SER GLU LYS LEU GLU HIS ASP PRO GLU ALA ASP ALA          
SEQRES  71 C  921  THR GLY LEU GLU ARG MET LEU GLU SER ARG GLY                  
MODRES 3MDJ ASN A   70  ASN  GLYCOSYLATION SITE                                 
MODRES 3MDJ ASN A  760  ASN  GLYCOSYLATION SITE                                 
MODRES 3MDJ ASN A  154  ASN  GLYCOSYLATION SITE                                 
MODRES 3MDJ ASN B  154  ASN  GLYCOSYLATION SITE                                 
MODRES 3MDJ ASN C   70  ASN  GLYCOSYLATION SITE                                 
MODRES 3MDJ ASN B   70  ASN  GLYCOSYLATION SITE                                 
HET     ZN  A1000       1                                                       
HET    BES  A1001      22                                                       
HET    NAG  A5001      14                                                       
HET    NAG  A5002      14                                                       
HET    BMA  A5003      11                                                       
HET    MAN  A5004      11                                                       
HET    MAN  A5005      11                                                       
HET    NAG  A6000      14                                                       
HET    NAG  A6001      14                                                       
HET     ZN  B1000       1                                                       
HET    BES  B1001      22                                                       
HET    NAG  B5001      14                                                       
HET    NAG  B5002      14                                                       
HET    NAG  B6000      14                                                       
HET     ZN  C1000       1                                                       
HET    BES  C1001      22                                                       
HET    NAG  C5001      14                                                       
HET    NAG  C5002      14                                                       
HET    BMA  C5003      11                                                       
HET    MAN  C5004      11                                                       
HET    MAN  C5005      11                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     BES 2-(3-AMINO-2-HYDROXY-4-PHENYL-BUTYRYLAMINO)-4-METHYL-            
HETNAM   2 BES  PENTANOIC ACID                                                  
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     BMA BETA-D-MANNOSE                                                   
HETNAM     MAN ALPHA-D-MANNOSE                                                  
HETSYN     BES BESTATIN                                                         
FORMUL   4   ZN    3(ZN 2+)                                                     
FORMUL   5  BES    3(C16 H24 N2 O4)                                             
FORMUL   6  NAG    9(C8 H15 N O6)                                               
FORMUL   6  BMA    2(C6 H12 O6)                                                 
FORMUL   6  MAN    4(C6 H12 O6)                                                 
HELIX    1   1 ALA A  186  PHE A  191  1                                   6    
HELIX    2   2 SER A  243  VAL A  247  5                                   5    
HELIX    3   3 LYS A  275  GLN A  278  5                                   4    
HELIX    4   4 ALA A  279  PHE A  297  1                                  19    
HELIX    5   5 SER A  330  LEU A  332  5                                   3    
HELIX    6   6 SER A  340  HIS A  357  1                                  18    
HELIX    7   7 TRP A  368  ASN A  370  5                                   3    
HELIX    8   8 ASP A  371  HIS A  391  1                                  21    
HELIX    9   9 PRO A  392  LYS A  395  5                                   4    
HELIX   10  10 VAL A  396  ALA A  412  1                                  17    
HELIX   11  11 ASP A  434  LEU A  452  1                                  19    
HELIX   12  12 SER A  453  SER A  469  1                                  17    
HELIX   13  13 LYS A  474  ALA A  483  1                                  10    
HELIX   14  14 ASP A  516  LEU A  526  1                                  11    
HELIX   15  15 VAL A  602  ASN A  605  5                                   4    
HELIX   16  16 ASP A  615  THR A  627  1                                  13    
HELIX   17  17 HIS A  628  VAL A  631  5                                   4    
HELIX   18  18 SER A  632  ILE A  649  1                                  18    
HELIX   19  19 SER A  653  LEU A  662  1                                  10    
HELIX   20  20 TYR A  663  GLU A  667  5                                   5    
HELIX   21  21 GLU A  669  GLU A  688  1                                  20    
HELIX   22  22 MET A  692  GLN A  714  1                                  23    
HELIX   23  23 SER A  721  HIS A  738  1                                  18    
HELIX   24  24 TYR A  740  GLU A  756  1                                  17    
HELIX   25  25 PRO A  764  ALA A  776  1                                  13    
HELIX   26  26 SER A  778  TYR A  789  1                                  12    
HELIX   27  27 SER A  795  ARG A  807  1                                  13    
HELIX   28  28 ASN A  810  SER A  821  1                                  12    
HELIX   29  29 GLU A  831  GLY A  840  1                                  10    
HELIX   30  30 GLY A  845  ASN A  856  1                                  12    
HELIX   31  31 ASN A  856  GLN A  862  1                                   7    
HELIX   32  32 ILE A  871  ASN A  880  1                                  10    
HELIX   33  33 THR A  884  LYS A  892  1                                   9    
HELIX   34  34 VAL A  908  LEU A  933  1                                  26    
HELIX   35  35 ALA B  186  ALA B  190  5                                   5    
HELIX   36  36 SER B  243  VAL B  247  5                                   5    
HELIX   37  37 VAL B  272  GLN B  278  5                                   7    
HELIX   38  38 ALA B  279  SER B  298  1                                  20    
HELIX   39  39 SER B  330  LEU B  332  5                                   3    
HELIX   40  40 SER B  340  HIS B  357  1                                  18    
HELIX   41  41 TRP B  368  ASN B  370  5                                   3    
HELIX   42  42 ASP B  371  HIS B  391  1                                  21    
HELIX   43  43 PRO B  392  LYS B  395  5                                   4    
HELIX   44  44 VAL B  396  ALA B  412  1                                  17    
HELIX   45  45 ASP B  434  LEU B  452  1                                  19    
HELIX   46  46 SER B  453  SER B  469  1                                  17    
HELIX   47  47 LYS B  474  ALA B  483  1                                  10    
HELIX   48  48 ASP B  516  LEU B  526  1                                  11    
HELIX   49  49 VAL B  602  ASN B  605  5                                   4    
HELIX   50  50 ASP B  615  HIS B  628  1                                  14    
HELIX   51  51 THR B  629  VAL B  631  5                                   3    
HELIX   52  52 SER B  632  SER B  648  1                                  17    
HELIX   53  53 SER B  653  LEU B  662  1                                  10    
HELIX   54  54 TYR B  663  GLU B  667  5                                   5    
HELIX   55  55 GLU B  669  GLU B  688  1                                  20    
HELIX   56  56 MET B  692  GLN B  714  1                                  23    
HELIX   57  57 SER B  721  HIS B  738  1                                  18    
HELIX   58  58 TYR B  740  GLU B  756  1                                  17    
HELIX   59  59 PRO B  764  ALA B  776  1                                  13    
HELIX   60  60 SER B  778  PHE B  791  1                                  14    
HELIX   61  61 SER B  795  CYS B  806  1                                  12    
HELIX   62  62 ASN B  810  SER B  821  1                                  12    
HELIX   63  63 GLU B  831  ARG B  841  1                                  11    
HELIX   64  64 GLY B  845  ASN B  856  1                                  12    
HELIX   65  65 ASN B  856  VAL B  861  1                                   6    
HELIX   66  66 ILE B  871  ASN B  880  1                                  10    
HELIX   67  67 ARG B  885  LYS B  892  1                                   8    
HELIX   68  68 VAL B  908  LEU B  933  1                                  26    
HELIX   69  69 ALA C  186  ALA C  190  5                                   5    
HELIX   70  70 SER C  243  VAL C  247  5                                   5    
HELIX   71  71 LYS C  275  GLN C  278  5                                   4    
HELIX   72  72 ALA C  279  SER C  298  1                                  20    
HELIX   73  73 SER C  330  LEU C  332  5                                   3    
HELIX   74  74 SER C  340  HIS C  357  1                                  18    
HELIX   75  75 TRP C  368  ASN C  370  5                                   3    
HELIX   76  76 ASP C  371  HIS C  391  1                                  21    
HELIX   77  77 PRO C  392  LYS C  395  5                                   4    
HELIX   78  78 VAL C  396  ALA C  412  1                                  17    
HELIX   79  79 ASP C  434  LEU C  452  1                                  19    
HELIX   80  80 SER C  453  SER C  469  1                                  17    
HELIX   81  81 LYS C  474  SER C  484  1                                  11    
HELIX   82  82 ASP C  516  LEU C  526  1                                  11    
HELIX   83  83 VAL C  602  ASN C  605  5                                   4    
HELIX   84  84 ASP C  615  HIS C  628  1                                  14    
HELIX   85  85 THR C  629  VAL C  631  5                                   3    
HELIX   86  86 SER C  632  SER C  648  1                                  17    
HELIX   87  87 SER C  653  LEU C  662  1                                  10    
HELIX   88  88 TYR C  663  GLU C  667  5                                   5    
HELIX   89  89 GLU C  669  GLU C  688  1                                  20    
HELIX   90  90 MET C  692  GLN C  714  1                                  23    
HELIX   91  91 SER C  721  HIS C  738  1                                  18    
HELIX   92  92 TYR C  740  GLU C  756  1                                  17    
HELIX   93  93 PRO C  764  ALA C  776  1                                  13    
HELIX   94  94 SER C  778  TYR C  789  1                                  12    
HELIX   95  95 SER C  795  ARG C  807  1                                  13    
HELIX   96  96 ASN C  810  SER C  821  1                                  12    
HELIX   97  97 GLU C  831  GLY C  840  1                                  10    
HELIX   98  98 GLY C  845  ASN C  856  1                                  12    
HELIX   99  99 ASN C  856  GLN C  862  1                                   7    
HELIX  100 100 ILE C  871  ASN C  880  1                                  10    
HELIX  101 101 ARG C  885  LYS C  892  1                                   8    
HELIX  102 102 VAL C  908  LEU C  933  1                                  26    
SHEET    1   A 8 GLU A 117  PRO A 119  0                                        
SHEET    2   A 8 GLN A 101  ARG A 108 -1  N  LEU A 107   O  GLU A 118           
SHEET    3   A 8 PRO A 144  ASN A 154 -1  O  HIS A 150   N  ARG A 104           
SHEET    4   A 8 THR A  75  ALA A  86 -1  N  PHE A  76   O  GLY A 153           
SHEET    5   A 8 VAL A  58  ASN A  70 -1  N  ILE A  59   O  THR A  85           
SHEET    6   A 8 SER A 202  ARG A 209  1  O  LYS A 206   N  LEU A  65           
SHEET    7   A 8 LEU A 231  PHE A 236 -1  O  ASP A 234   N  ILE A 207           
SHEET    8   A 8 LEU A 221  ALA A 228 -1  N  VAL A 222   O  HIS A 235           
SHEET    1   B 3 THR A  92  HIS A  96  0                                        
SHEET    2   B 3 GLN A 130  LEU A 134 -1  O  ILE A 131   N  LEU A  95           
SHEET    3   B 3 GLN A 121  HIS A 125 -1  N  HIS A 125   O  GLN A 130           
SHEET    1   C 2 GLY A 161  ARG A 168  0                                        
SHEET    2   C 2 LEU A 174  GLN A 181 -1  O  ARG A 175   N  TYR A 167           
SHEET    1   D 2 LEU A 214  SER A 217  0                                        
SHEET    2   D 2 PHE A 249  SER A 252 -1  O  ILE A 250   N  ILE A 216           
SHEET    1   E 5 GLU A 255  ILE A 260  0                                        
SHEET    2   E 5 LYS A 266  ALA A 271 -1  O  VAL A 267   N  LYS A 259           
SHEET    3   E 5 LYS A 305  ILE A 311  1  O  LEU A 308   N  SER A 268           
SHEET    4   E 5 LEU A 324  ARG A 328  1  O  TYR A 327   N  ILE A 311           
SHEET    5   E 5 ALA A 318  MET A 319 -1  N  MET A 319   O  THR A 326           
SHEET    1   F 2 VAL A 364  MET A 366  0                                        
SHEET    2   F 2 LYS A 471  THR A 473  1  O  LYS A 471   N  THR A 365           
SHEET    1   G 4 THR A 586  ILE A 590  0                                        
SHEET    2   G 4 ASN A 541  HIS A 548 -1  N  VAL A 542   O  LEU A 589           
SHEET    3   G 4 PRO A 531  ARG A 538 -1  N  THR A 536   O  HIS A 543           
SHEET    4   G 4 ILE A 609  TYR A 612  1  O  HIS A 611   N  ILE A 533           
SHEET    1   H 3 HIS A 578  LEU A 582  0                                        
SHEET    2   H 3 VAL A 565  THR A 571 -1  N  PHE A 569   O  HIS A 578           
SHEET    3   H 3 ILE A 598  PHE A 600 -1  O  LYS A 599   N  ILE A 570           
SHEET    1   I 8 GLU B 118  PRO B 119  0                                        
SHEET    2   I 8 GLN B 101  ARG B 108 -1  N  LEU B 107   O  GLU B 118           
SHEET    3   I 8 TYR B 145  ASN B 154 -1  O  THR B 146   N  ARG B 108           
SHEET    4   I 8 THR B  75  ALA B  86 -1  N  PHE B  76   O  GLY B 153           
SHEET    5   I 8 VAL B  58  ASN B  70 -1  N  ILE B  59   O  THR B  85           
SHEET    6   I 8 SER B 202  ARG B 209  1  O  LYS B 206   N  LEU B  65           
SHEET    7   I 8 LEU B 231  PHE B 236 -1  O  ASP B 234   N  ILE B 207           
SHEET    8   I 8 LEU B 221  ALA B 228 -1  N  VAL B 222   O  HIS B 235           
SHEET    1   J 3 THR B  92  HIS B  96  0                                        
SHEET    2   J 3 GLN B 130  LEU B 134 -1  O  ILE B 131   N  LEU B  95           
SHEET    3   J 3 GLN B 121  HIS B 125 -1  N  LEU B 123   O  ALA B 132           
SHEET    1   K 4 GLY B 161  ARG B 168  0                                        
SHEET    2   K 4 LEU B 174  GLN B 181 -1  O  ARG B 175   N  TYR B 167           
SHEET    3   K 4 PHE B 249  SER B 252 -1  O  ILE B 251   N  ALA B 178           
SHEET    4   K 4 LEU B 214  SER B 217 -1  N  LEU B 214   O  SER B 252           
SHEET    1   L 5 GLU B 255  ILE B 260  0                                        
SHEET    2   L 5 LYS B 266  ALA B 271 -1  O  VAL B 267   N  LYS B 259           
SHEET    3   L 5 LYS B 305  ILE B 311  1  O  LEU B 308   N  SER B 268           
SHEET    4   L 5 LEU B 324  ARG B 328  1  O  THR B 325   N  ALA B 309           
SHEET    5   L 5 ALA B 318  MET B 319 -1  N  MET B 319   O  THR B 326           
SHEET    1   M 2 VAL B 364  MET B 366  0                                        
SHEET    2   M 2 LYS B 471  THR B 473  1  O  THR B 473   N  THR B 365           
SHEET    1   N 4 THR B 586  ILE B 590  0                                        
SHEET    2   N 4 ASN B 541  HIS B 548 -1  N  VAL B 542   O  LEU B 589           
SHEET    3   N 4 PRO B 531  ARG B 538 -1  N  THR B 536   O  HIS B 543           
SHEET    4   N 4 ILE B 609  TYR B 612  1  O  HIS B 611   N  ILE B 535           
SHEET    1   O 3 HIS B 578  LEU B 582  0                                        
SHEET    2   O 3 VAL B 565  THR B 571 -1  N  PHE B 569   O  HIS B 578           
SHEET    3   O 3 ILE B 598  PHE B 600 -1  O  LYS B 599   N  ILE B 570           
SHEET    1   P 8 GLU C 118  PRO C 119  0                                        
SHEET    2   P 8 GLN C 101  ARG C 108 -1  N  LEU C 107   O  GLU C 118           
SHEET    3   P 8 TYR C 145  ASN C 154 -1  O  THR C 146   N  ARG C 108           
SHEET    4   P 8 THR C  75  ALA C  86 -1  N  PHE C  76   O  GLY C 153           
SHEET    5   P 8 VAL C  58  ASN C  70 -1  N  ASP C  64   O  LYS C  81           
SHEET    6   P 8 SER C 202  ARG C 209  1  O  SER C 202   N  TYR C  63           
SHEET    7   P 8 LEU C 231  PHE C 236 -1  O  ASP C 234   N  ILE C 207           
SHEET    8   P 8 LEU C 221  ALA C 228 -1  N  VAL C 222   O  HIS C 235           
SHEET    1   Q 3 THR C  92  HIS C  96  0                                        
SHEET    2   Q 3 GLN C 130  LEU C 134 -1  O  ILE C 131   N  LEU C  95           
SHEET    3   Q 3 GLN C 121  HIS C 125 -1  N  LEU C 123   O  ALA C 132           
SHEET    1   R 2 GLY C 161  ARG C 168  0                                        
SHEET    2   R 2 LEU C 174  GLN C 181 -1  O  GLN C 181   N  GLY C 161           
SHEET    1   S 2 LEU C 214  SER C 217  0                                        
SHEET    2   S 2 PHE C 249  SER C 252 -1  O  ILE C 250   N  ILE C 216           
SHEET    1   T 5 GLU C 255  ILE C 260  0                                        
SHEET    2   T 5 LYS C 266  ALA C 271 -1  O  VAL C 267   N  LYS C 259           
SHEET    3   T 5 LYS C 305  ILE C 311  1  O  ALA C 310   N  TYR C 270           
SHEET    4   T 5 LEU C 324  ARG C 328  1  O  TYR C 327   N  ILE C 311           
SHEET    5   T 5 ALA C 318  MET C 319 -1  N  MET C 319   O  THR C 326           
SHEET    1   U 2 VAL C 364  MET C 366  0                                        
SHEET    2   U 2 LYS C 471  THR C 473  1  O  LYS C 471   N  THR C 365           
SHEET    1   V 4 THR C 586  ILE C 590  0                                        
SHEET    2   V 4 ASN C 541  TYR C 549 -1  N  VAL C 542   O  LEU C 589           
SHEET    3   V 4 PHE C 530  ARG C 538 -1  N  ARG C 538   O  ASN C 541           
SHEET    4   V 4 ILE C 609  TYR C 612  1  O  HIS C 611   N  ILE C 535           
SHEET    1   W 3 HIS C 578  LEU C 582  0                                        
SHEET    2   W 3 VAL C 565  THR C 571 -1  N  VAL C 565   O  LEU C 582           
SHEET    3   W 3 ILE C 598  PHE C 600 -1  O  LYS C 599   N  ILE C 570           
SSBOND   1 CYS A  404    CYS A  443                          1555   1555  2.03  
SSBOND   2 CYS A  736    CYS A  743                          1555   1555  2.03  
SSBOND   3 CYS B  404    CYS B  443                          1555   1555  2.03  
SSBOND   4 CYS B  736    CYS B  743                          1555   1555  1.96  
SSBOND   5 CYS C  404    CYS C  443                          1555   1555  2.03  
SSBOND   6 CYS C  736    CYS C  743                          1555   1555  2.04  
LINK         O3  BMA A5003                 C1  MAN A5004     1555   1555  1.37  
LINK         O3  BMA C5003                 C1  MAN C5004     1555   1555  1.38  
LINK         O4  NAG A5002                 C1  BMA A5003     1555   1555  1.42  
LINK         O4  NAG C5002                 C1  BMA C5003     1555   1555  1.42  
LINK         O4  NAG B5001                 C1  NAG B5002     1555   1555  1.45  
LINK         O4  NAG A5001                 C1  NAG A5002     1555   1555  1.47  
LINK         O4  NAG C5001                 C1  NAG C5002     1555   1555  1.48  
LINK         ND2 ASN A  70                 C1  NAG A5001     1555   1555  1.48  
LINK         O6  BMA C5003                 C1  MAN C5005     1555   1555  1.48  
LINK         ND2 ASN A 760                 C1  NAG A6001     1555   1555  1.48  
LINK         ND2 ASN A 154                 C1  NAG A6000     1555   1555  1.48  
LINK         O6  BMA A5003                 C1  MAN A5005     1555   1555  1.49  
LINK         ND2 ASN B 154                 C1  NAG B6000     1555   1555  1.49  
LINK         ND2 ASN C  70                 C1  NAG C5001     1555   1555  1.49  
LINK         ND2 ASN B  70                 C1  NAG B5001     1555   1555  1.50  
LINK        ZN    ZN B1000                 O2  BES B1001     1555   1555  2.08  
LINK         NE2 HIS A 353                ZN    ZN A1000     1555   1555  2.14  
LINK         OE1 GLU A 376                ZN    ZN A1000     1555   1555  2.14  
LINK         NE2 HIS C 353                ZN    ZN C1000     1555   1555  2.15  
LINK         NE2 HIS A 357                ZN    ZN A1000     1555   1555  2.19  
LINK        ZN    ZN A1000                 O2  BES A1001     1555   1555  2.19  
LINK         OE1 GLU C 376                ZN    ZN C1000     1555   1555  2.20  
LINK         NE2 HIS B 353                ZN    ZN B1000     1555   1555  2.20  
LINK         OE1 GLU B 376                ZN    ZN B1000     1555   1555  2.24  
LINK         NE2 HIS C 357                ZN    ZN C1000     1555   1555  2.27  
LINK         NE2 HIS B 357                ZN    ZN B1000     1555   1555  2.30  
LINK        ZN    ZN C1000                 O2  BES C1001     1555   1555  2.40  
LINK         OE2 GLU A 376                ZN    ZN A1000     1555   1555  2.47  
LINK         OE2 GLU B 376                ZN    ZN B1000     1555   1555  2.50  
LINK         OE2 GLU C 376                ZN    ZN C1000     1555   1555  2.54  
CISPEP   1 GLU A  183    PRO A  184          0         2.44                     
CISPEP   2 SER A  316    GLY A  317          0         4.77                     
CISPEP   3 SER A  757    ASN A  758          0        -1.26                     
CISPEP   4 GLU B  183    PRO B  184          0         3.38                     
CISPEP   5 SER B  316    GLY B  317          0         6.79                     
CISPEP   6 SER B  757    ASN B  758          0        -3.32                     
CISPEP   7 GLU C  183    PRO C  184          0         2.56                     
CISPEP   8 SER C  316    GLY C  317          0         6.44                     
CISPEP   9 SER C  757    ASN C  758          0        -3.52                     
SITE     1 AC1  4 HIS A 353  HIS A 357  GLU A 376  BES A1001                    
SITE     1 AC2 12 GLU A 183  GLY A 317  ALA A 318  MET A 319                    
SITE     2 AC2 12 GLU A 320  THR A 350  HIS A 353  GLU A 354                    
SITE     3 AC2 12 HIS A 357  GLU A 376  GLU A 383   ZN A1000                    
SITE     1 AC3  5 HIS A  68  ASN A  70  THR A  73  GLU A 210                    
SITE     2 AC3  5 NAG A5002                                                     
SITE     1 AC4  4 GLY A 230  NAG A5001  BMA A5003  MAN A5005                    
SITE     1 AC5  5 NAG A5002  MAN A5004  MAN A5005  THR B 166                    
SITE     2 AC5  5 ASP B 313                                                     
SITE     1 AC6  2 GLU A 229  BMA A5003                                          
SITE     1 AC7  4 NAG A5002  BMA A5003  GLU B 157  LYS B 164                    
SITE     1 AC8  1 ASN A 154                                                     
SITE     1 AC9  1 ASN A 760                                                     
SITE     1 BC1  4 HIS B 353  HIS B 357  GLU B 376  BES B1001                    
SITE     1 BC2 14 GLN B 181  GLU B 183  SER B 316  GLY B 317                    
SITE     2 BC2 14 ALA B 318  MET B 319  GLU B 320  HIS B 353                    
SITE     3 BC2 14 GLU B 354  HIS B 357  GLU B 376  LYS B 380                    
SITE     4 BC2 14 GLU B 383   ZN B1000                                          
SITE     1 BC3  5 HIS B  68  ASN B  70  THR B  72  GLU B 210                    
SITE     2 BC3  5 NAG B5002                                                     
SITE     1 BC4  1 NAG B5001                                                     
SITE     1 BC5  2 GLN B 101  ASN B 154                                          
SITE     1 BC6  4 HIS C 353  HIS C 357  GLU C 376  BES C1001                    
SITE     1 BC7 12 GLU C 183  SER C 316  GLY C 317  ALA C 318                    
SITE     2 BC7 12 MET C 319  GLU C 320  THR C 350  HIS C 353                    
SITE     3 BC7 12 GLU C 354  GLU C 376  GLU C 383   ZN C1000                    
SITE     1 BC8  5 HIS C  68  ASN C  70  GLU C 210  LEU C 231                    
SITE     2 BC8  5 NAG C5002                                                     
SITE     1 BC9  5 GLU C 229  GLY C 230  NAG C5001  BMA C5003                    
SITE     2 BC9  5 MAN C5005                                                     
SITE     1 CC1  3 NAG C5002  MAN C5004  MAN C5005                               
SITE     1 CC2  2 GLU C 229  BMA C5003                                          
SITE     1 CC3  2 NAG C5002  BMA C5003                                          
CRYST1   71.029  234.635   95.860  90.00 103.59  90.00 P 1 21 1      6          
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      0.014079  0.000000  0.003403        0.00000                         
SCALE2      0.000000  0.004262  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010732        0.00000                         
MTRIX1   1  0.164122  0.733748  0.659300      -39.56080    1                    
MTRIX2   1 -0.491017 -0.518912  0.699738      155.83099    1                    
MTRIX3   1  0.855550 -0.438570  0.275118       12.10640    1                    
MTRIX1   2  0.163489 -0.544208  0.822867       76.97210    1                    
MTRIX2   2  0.695633 -0.527851 -0.487307      118.12200    1                    
MTRIX3   2  0.699547  0.652083  0.292271      -79.83650    1                    
MTRIX1   3  0.172178  0.757168  0.630120      -43.04900    1                    
MTRIX2   3 -0.502981 -0.482425  0.717131      155.07001    1                    
MTRIX3   3  0.846974 -0.440413  0.297778       13.96940    1                    
MTRIX1   4  0.161326 -0.542051  0.824715       76.66960    1                    
MTRIX2   4  0.705216 -0.521276 -0.480563      117.65600    1                    
MTRIX3   4  0.690394  0.659130  0.298168      -80.46050    1                    
MTRIX1   5  0.199735  0.722916  0.661437      -38.49480    1                    
MTRIX2   5 -0.485558 -0.513304  0.707639      157.07300    1                    
MTRIX3   5  0.851081 -0.462506  0.248493       13.12820    1                    
MTRIX1   6  0.211666 -0.533237  0.819058       76.56220    1                    
MTRIX2   6  0.726886 -0.474320 -0.496646      112.46400    1                    
MTRIX3   6  0.653325  0.700485  0.287206      -85.91040    1                    
MTRIX1   7  0.200553  0.749399  0.631015      -43.32870    1                    
MTRIX2   7 -0.477745 -0.487513  0.730815      155.46700    1                    
MTRIX3   7  0.855300 -0.448031  0.260250       12.42990    1                    
MTRIX1   8  0.165070 -0.542775  0.823497       76.50310    1                    
MTRIX2   8  0.714600 -0.509658 -0.479162      116.34300    1                    
MTRIX3   8  0.679779  0.667566  0.303738      -81.44710    1                    
MTRIX1   9  0.212959  0.759499  0.614662      -46.14300    1                    
MTRIX2   9 -0.484244 -0.464351  0.741543      153.83901    1                    
MTRIX3   9  0.848620 -0.455565  0.268895       14.21620    1                    
MTRIX1  10  0.165219 -0.579134  0.798315       81.30410    1                    
MTRIX2  10  0.699512 -0.501802 -0.508800      115.00800    1                    
MTRIX3  10  0.695259  0.642494  0.322204      -77.95330    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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