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Database: PDB
Entry: 2YD0
LinkDB: 2YD0
Original site: 2YD0 
HEADER    HYDROLASE                               17-MAR-11   2YD0              
TITLE     CRYSTAL STRUCTURE OF THE SOLUBLE DOMAIN OF HUMAN ENDOPLASMIC RETICULUM
TITLE    2 AMINOPEPTIDASE 1 ERAP1                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ENDOPLASMIC RETICULUM AMINOPEPTIDASE 1;                    
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: SOLUBLE DOMAIN, RESIDUES 46-940;                           
COMPND   5 SYNONYM: ADIPOCYTE-DERIVED LEUCINE AMINOPEPTIDASE, ARTS-1,           
COMPND   6 AMINOPEPTIDASE PILS, PUROMYCIN-INSENSITIVE LEUCYL-SPECIFIC           
COMPND   7 AMINOPEPTIDASE, TYPE 1 TUMOR NECROSIS FACTOR RECEPTOR SHEDDING       
COMPND   8 AMINOPEPTIDASE REGULATOR, A-LAP, PILS-AP;                            
COMPND   9 EC: 3.4.11.-;                                                        
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 OTHER_DETAILS: GLYCOSYLATION AT RESIDUES ASN70, ASN154, ASN414       
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE   6 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: HIGH FIVE;                              
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  10 EXPRESSION_SYSTEM_VECTOR: PFB-CT10HF-LIC                             
KEYWDS    HYDROLASE, GLYCOPROTEIN, METAL-BINDING, METALLOPROTEASE, PROTEASE,    
KEYWDS   2 ADAPTIVE IMMUNITY                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.VOLLMAR,G.KOCHAN,T.KROJER,E.UGOCHUKWU,J.R.C.MUNIZ,J.RAYNOR,         
AUTHOR   2 A.CHAIKUAD,C.ALLERSTON,F.VON DELFT,C.BOUNTRA,C.H.ARROWSMITH,         
AUTHOR   3 J.WEIGELT,A.EDWARDS,S.KNAPP                                          
REVDAT   5   03-APR-19 2YD0    1       SOURCE                                   
REVDAT   4   27-MAR-19 2YD0    1       LINK                                     
REVDAT   3   24-JAN-18 2YD0    1       JRNL                                     
REVDAT   2   03-OCT-12 2YD0    1       SOURCE JRNL   REMARK VERSN               
REVDAT   1   13-APR-11 2YD0    0                                                
SPRSDE     13-APR-11 2YD0      2XDT                                             
JRNL        AUTH   G.KOCHAN,T.KROJER,D.HARVEY,R.FISCHER,L.CHEN,M.VOLLMAR,       
JRNL        AUTH 2 F.VON DELFT,K.L.KAVANAGH,M.A.BROWN,P.BOWNESS,P.WORDSWORTH,   
JRNL        AUTH 3 B.M.KESSLER,U.OPPERMANN                                      
JRNL        TITL   CRYSTAL STRUCTURES OF THE ENDOPLASMIC RETICULUM              
JRNL        TITL 2 AMINOPEPTIDASE-1 (ERAP1) REVEAL THE MOLECULAR BASIS FOR      
JRNL        TITL 3 N-TERMINAL PEPTIDE TRIMMING.                                 
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 108  7745 2011              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   21508329                                                     
JRNL        DOI    10.1073/PNAS.1101262108                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0110                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.94                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 35800                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.155                           
REMARK   3   R VALUE            (WORKING SET) : 0.152                           
REMARK   3   FREE R VALUE                     : 0.215                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1880                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.76                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2507                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.96                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2100                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 136                          
REMARK   3   BIN FREE R VALUE                    : 0.3060                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6838                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 99                                      
REMARK   3   SOLVENT ATOMS            : 288                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 13.50                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.34000                                             
REMARK   3    B22 (A**2) : -1.34000                                             
REMARK   3    B33 (A**2) : 2.01000                                              
REMARK   3    B12 (A**2) : -0.67000                                             
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.429         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.266         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.173         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 17.944        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.957                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.916                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  7131 ; 0.017 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  4754 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  9680 ; 1.668 ; 1.960       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 11588 ; 1.230 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   858 ; 6.583 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   313 ;35.540 ;24.185       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1198 ;16.085 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    31 ;18.267 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1096 ; 0.092 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7789 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1454 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  4285 ; 2.607 ; 3.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1728 ; 0.714 ; 3.000       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6935 ; 4.285 ; 5.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2846 ; 7.844 ; 8.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2743 ;10.089 ;11.000       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS.                                                          
REMARK   4                                                                      
REMARK   4 2YD0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-MAR-11.                  
REMARK 100 THE DEPOSITION ID IS D_1290047735.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-JAN-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I03                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9763                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC CCD                           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 37682                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 12.20                              
REMARK 200  R MERGE                    (I) : 0.20000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.85                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 12.50                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.96000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR                          
REMARK 200 SOFTWARE USED: SHARP                                                 
REMARK 200 STARTING MODEL: NONE                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.08                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.08                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.4M KCITRATE, 100 MM CACODYLATE (PH     
REMARK 280  5.7), 170 MM N-DODECYL-BETA-MALTOSIDE                               
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 6 2 2                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   -X,-Y,Z                                                 
REMARK 290       5555   Y,-X+Y,Z                                                
REMARK 290       6555   X-Y,X,Z                                                 
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z                                              
REMARK 290      10555   -Y,-X,-Z                                                
REMARK 290      11555   -X+Y,Y,-Z                                               
REMARK 290      12555   X,X-Y,-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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 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 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   111                                                      
REMARK 465     GLY A   112                                                      
REMARK 465     GLU A   113                                                      
REMARK 465     ARG A   114                                                      
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     SER A   553                                                      
REMARK 465     ASP A   554                                                      
REMARK 465     GLY A   555                                                      
REMARK 465     ALA A   556                                                      
REMARK 465     PRO A   557                                                      
REMARK 465     LYS A   941                                                      
REMARK 465     LYS A   942                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A  51    CE   NZ                                             
REMARK 470     GLN A 101    CD   OE1  NE2                                       
REMARK 470     LYS A 109    CG   CD   CE   NZ                                   
REMARK 470     LEU A 115    CG   CD1  CD2                                       
REMARK 470     LYS A 262    CE   NZ                                             
REMARK 470     GLU A 337    CD   OE1  OE2                                       
REMARK 470     LYS A 338    CD   CE   NZ                                        
REMARK 470     LYS A 395    CD   CE   NZ                                        
REMARK 470     PHE A 401    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU A 409    CG   CD   OE1  OE2                                  
REMARK 470     SER A 453    OG                                                  
REMARK 470     ASP A 558    CG   OD1  OD2                                       
REMARK 470     LYS A 573    CG   CD   CE   NZ                                   
REMARK 470     SER A 574    OG                                                  
REMARK 470     ASP A 575    CG   OD1  OD2                                       
REMARK 470     GLU A 593    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 615    CG   OD1  OD2                                       
REMARK 470     LYS A 656    CE   NZ                                             
REMARK 470     LYS A 665    CG   CD   CE   NZ                                   
REMARK 470     GLU A 694    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 745    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 753    NZ                                                  
REMARK 470     GLU A 780    OE1  OE2                                            
REMARK 470     LYS A 823    CE   NZ                                             
REMARK 470     LYS A 826    CE   NZ                                             
REMARK 470     LYS A 855    CE   NZ                                             
REMARK 470     LYS A 859    CE   NZ                                             
REMARK 470     LYS A 899    CE   NZ                                             
REMARK 470     GLU A 900    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 938    CG   CD1  CD2                                       
REMARK 470     GLU A 939    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 940    CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A  2052     O    HOH A  2142              1.53            
REMARK 500   O    HOH A  2216     O    HOH A  2236              2.02            
REMARK 500   O    HOH A  2037     O    HOH A  2271              2.14            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP A 284   CB  -  CG  -  OD1 ANGL. DEV. =   6.4 DEGREES          
REMARK 500    ARG A 430   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ARG A 579   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ARG A 188       -3.05    -58.33                                   
REMARK 500    ASN A 277        3.42    -67.34                                   
REMARK 500    SER A 316     -165.98    -74.29                                   
REMARK 500    LEU A 332      -36.04   -132.26                                   
REMARK 500    PHE A 401      -60.18    -19.32                                   
REMARK 500    GLU A 424      -50.32   -136.05                                   
REMARK 500    TYR A 438      -70.92    -70.92                                   
REMARK 500    SER A 453      175.30    -58.69                                   
REMARK 500    ASN A 601       73.08     66.85                                   
REMARK 500    ASP A 614     -138.40     60.34                                   
REMARK 500    MET A 692       39.98   -142.57                                   
REMARK 500    GLU A 865      142.81     76.93                                   
REMARK 500    SER A 883       -3.05   -149.46                                   
REMARK 500    LYS A 899     -120.23     51.54                                   
REMARK 500    ASN A 901       42.10   -100.62                                   
REMARK 500    GLU A 939      -46.37   -135.17                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 LEU A  866     GLY A  867                  -47.28                    
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 A1946  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 376   OE1                                                    
REMARK 620 2 HIS A 353   NE2 112.2                                              
REMARK 620 3 HIS A 357   NE2  99.2  97.9                                        
REMARK 620 4 BES A1950   O2  141.0 106.9  74.8                                  
REMARK 620 5 BES A1950   O3   96.4  94.8 154.4  80.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K A1948   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 295   O                                                      
REMARK 620 2 SER A 298   OG   74.9                                              
REMARK 620 3 SER A 298   OG  134.9  69.4                                        
REMARK 620 4 ASP A 295   OD1  62.5 136.8 149.9                                  
REMARK 620 N                    1     2     3                                   
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 1946                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 1947                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 1948                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1949                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BES A 1950                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A   
REMARK 800  70 RESIDUES 1941 TO 1944                                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A   
REMARK 800  154 RESIDUES 1942 TO 1945                                           
DBREF  2YD0 A   46   940  UNP    Q9NZ08   ERAP1_HUMAN     46    940             
SEQADV 2YD0 LYS A  941  UNP  Q9NZ08              EXPRESSION TAG                 
SEQADV 2YD0 LYS A  942  UNP  Q9NZ08              EXPRESSION TAG                 
SEQRES   1 A  897  PRO PHE PRO TRP ASN LYS ILE ARG LEU PRO GLU TYR VAL          
SEQRES   2 A  897  ILE PRO VAL HIS TYR ASP LEU LEU ILE HIS ALA ASN LEU          
SEQRES   3 A  897  THR THR LEU THR PHE TRP GLY THR THR LYS VAL GLU ILE          
SEQRES   4 A  897  THR ALA SER GLN PRO THR SER THR ILE ILE LEU HIS SER          
SEQRES   5 A  897  HIS HIS LEU GLN ILE SER ARG ALA THR LEU ARG LYS GLY          
SEQRES   6 A  897  ALA GLY GLU ARG LEU SER GLU GLU PRO LEU GLN VAL LEU          
SEQRES   7 A  897  GLU HIS PRO ARG GLN GLU GLN ILE ALA LEU LEU ALA PRO          
SEQRES   8 A  897  GLU PRO LEU LEU VAL GLY LEU PRO TYR THR VAL VAL ILE          
SEQRES   9 A  897  HIS TYR ALA GLY ASN LEU SER GLU THR PHE HIS GLY PHE          
SEQRES  10 A  897  TYR LYS SER THR TYR ARG THR LYS GLU GLY GLU LEU ARG          
SEQRES  11 A  897  ILE LEU ALA SER THR GLN PHE GLU PRO THR ALA ALA ARG          
SEQRES  12 A  897  MET ALA PHE PRO CYS PHE ASP GLU PRO ALA PHE LYS ALA          
SEQRES  13 A  897  SER PHE SER ILE LYS ILE ARG ARG GLU PRO ARG HIS LEU          
SEQRES  14 A  897  ALA ILE SER ASN MET PRO LEU VAL LYS SER VAL THR VAL          
SEQRES  15 A  897  ALA GLU GLY LEU ILE GLU ASP HIS PHE ASP VAL THR VAL          
SEQRES  16 A  897  LYS MET SER THR TYR LEU VAL ALA PHE ILE ILE SER ASP          
SEQRES  17 A  897  PHE GLU SER VAL SER LYS ILE THR LYS SER GLY VAL LYS          
SEQRES  18 A  897  VAL SER VAL TYR ALA VAL PRO ASP LYS ILE ASN GLN ALA          
SEQRES  19 A  897  ASP TYR ALA LEU ASP ALA ALA VAL THR LEU LEU GLU PHE          
SEQRES  20 A  897  TYR GLU ASP TYR PHE SER ILE PRO TYR PRO LEU PRO LYS          
SEQRES  21 A  897  GLN ASP LEU ALA ALA ILE PRO ASP PHE GLN SER GLY ALA          
SEQRES  22 A  897  MET GLU ASN TRP GLY LEU THR THR TYR ARG GLU SER ALA          
SEQRES  23 A  897  LEU LEU PHE ASP ALA GLU LYS SER SER ALA SER SER LYS          
SEQRES  24 A  897  LEU GLY ILE THR MET THR VAL ALA HIS GLU LEU ALA HIS          
SEQRES  25 A  897  GLN TRP PHE GLY ASN LEU VAL THR MET GLU TRP TRP ASN          
SEQRES  26 A  897  ASP LEU TRP LEU ASN GLU GLY PHE ALA LYS PHE MET GLU          
SEQRES  27 A  897  PHE VAL SER VAL SER VAL THR HIS PRO GLU LEU LYS VAL          
SEQRES  28 A  897  GLY ASP TYR PHE PHE GLY LYS CYS PHE ASP ALA MET GLU          
SEQRES  29 A  897  VAL ASP ALA LEU ASN SER SER HIS PRO VAL SER THR PRO          
SEQRES  30 A  897  VAL GLU ASN PRO ALA GLN ILE ARG GLU MET PHE ASP ASP          
SEQRES  31 A  897  VAL SER TYR ASP LYS GLY ALA CYS ILE LEU ASN MET LEU          
SEQRES  32 A  897  ARG GLU TYR LEU SER ALA ASP ALA PHE LYS SER GLY ILE          
SEQRES  33 A  897  VAL GLN TYR LEU GLN LYS HIS SER TYR LYS ASN THR LYS          
SEQRES  34 A  897  ASN GLU ASP LEU TRP ASP SER MET ALA SER ILE CYS PRO          
SEQRES  35 A  897  THR ASP GLY VAL LYS GLY MET ASP GLY PHE CYS SER ARG          
SEQRES  36 A  897  SER GLN HIS SER SER SER SER SER HIS TRP HIS GLN GLU          
SEQRES  37 A  897  GLY VAL ASP VAL LYS THR MET MET ASN THR TRP THR LEU          
SEQRES  38 A  897  GLN LYS GLY PHE PRO LEU ILE THR ILE THR VAL ARG GLY          
SEQRES  39 A  897  ARG ASN VAL HIS MET LYS GLN GLU HIS TYR MET LYS GLY          
SEQRES  40 A  897  SER ASP GLY ALA PRO ASP THR GLY TYR LEU TRP HIS VAL          
SEQRES  41 A  897  PRO LEU THR PHE ILE THR SER LYS SER ASP MET VAL HIS          
SEQRES  42 A  897  ARG PHE LEU LEU LYS THR LYS THR ASP VAL LEU ILE LEU          
SEQRES  43 A  897  PRO GLU GLU VAL GLU TRP ILE LYS PHE ASN VAL GLY MET          
SEQRES  44 A  897  ASN GLY TYR TYR ILE VAL HIS TYR GLU ASP ASP GLY TRP          
SEQRES  45 A  897  ASP SER LEU THR GLY LEU LEU LYS GLY THR HIS THR ALA          
SEQRES  46 A  897  VAL SER SER ASN ASP ARG ALA SER LEU ILE ASN ASN ALA          
SEQRES  47 A  897  PHE GLN LEU VAL SER ILE GLY LYS LEU SER ILE GLU LYS          
SEQRES  48 A  897  ALA LEU ASP LEU SER LEU TYR LEU LYS HIS GLU THR GLU          
SEQRES  49 A  897  ILE MET PRO VAL PHE GLN GLY LEU ASN GLU LEU ILE PRO          
SEQRES  50 A  897  MET TYR LYS LEU MET GLU LYS ARG ASP MET ASN GLU VAL          
SEQRES  51 A  897  GLU THR GLN PHE LYS ALA PHE LEU ILE ARG LEU LEU ARG          
SEQRES  52 A  897  ASP LEU ILE ASP LYS GLN THR TRP THR ASP GLU GLY SER          
SEQRES  53 A  897  VAL SER GLU ARG MET LEU ARG SER GLN LEU LEU LEU LEU          
SEQRES  54 A  897  ALA CYS VAL HIS ASN TYR GLN PRO CYS VAL GLN ARG ALA          
SEQRES  55 A  897  GLU GLY TYR PHE ARG LYS TRP LYS GLU SER ASN GLY ASN          
SEQRES  56 A  897  LEU SER LEU PRO VAL ASP VAL THR LEU ALA VAL PHE ALA          
SEQRES  57 A  897  VAL GLY ALA GLN SER THR GLU GLY TRP ASP PHE LEU TYR          
SEQRES  58 A  897  SER LYS TYR GLN PHE SER LEU SER SER THR GLU LYS SER          
SEQRES  59 A  897  GLN ILE GLU PHE ALA LEU CYS ARG THR GLN ASN LYS GLU          
SEQRES  60 A  897  LYS LEU GLN TRP LEU LEU ASP GLU SER PHE LYS GLY ASP          
SEQRES  61 A  897  LYS ILE LYS THR GLN GLU PHE PRO GLN ILE LEU THR LEU          
SEQRES  62 A  897  ILE GLY ARG ASN PRO VAL GLY TYR PRO LEU ALA TRP GLN          
SEQRES  63 A  897  PHE LEU ARG LYS ASN TRP ASN LYS LEU VAL GLN LYS PHE          
SEQRES  64 A  897  GLU LEU GLY SER SER SER ILE ALA HIS MET VAL MET GLY          
SEQRES  65 A  897  THR THR ASN GLN PHE SER THR ARG THR ARG LEU GLU GLU          
SEQRES  66 A  897  VAL LYS GLY PHE PHE SER SER LEU LYS GLU ASN GLY SER          
SEQRES  67 A  897  GLN LEU ARG CYS VAL GLN GLN THR ILE GLU THR ILE GLU          
SEQRES  68 A  897  GLU ASN ILE GLY TRP MET ASP LYS ASN PHE ASP LYS ILE          
SEQRES  69 A  897  ARG VAL TRP LEU GLN SER GLU LYS LEU GLU ARG LYS LYS          
MODRES 2YD0 ASN A   70  ASN  GLYCOSYLATION SITE                                 
MODRES 2YD0 ASN A  154  ASN  GLYCOSYLATION SITE                                 
MODRES 2YD0 ASN A  414  ASN  GLYCOSYLATION SITE                                 
HET    NAG  A1941      14                                                       
HET    NAG  A1944      14                                                       
HET    NAG  A1942      14                                                       
HET    NAG  A1945      14                                                       
HET    NAG  A1943      14                                                       
HET     ZN  A1946       1                                                       
HET      K  A1947       1                                                       
HET      K  A1948       1                                                       
HET    EDO  A1949       4                                                       
HET    BES  A1950      22                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM      ZN ZINC ION                                                         
HETNAM       K POTASSIUM ION                                                    
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     BES 2-(3-AMINO-2-HYDROXY-4-PHENYL-BUTYRYLAMINO)-4-METHYL-            
HETNAM   2 BES  PENTANOIC ACID                                                  
HETSYN     EDO ETHYLENE GLYCOL                                                  
HETSYN     BES BESTATIN                                                         
FORMUL   2  NAG    5(C8 H15 N O6)                                               
FORMUL   5   ZN    ZN 2+                                                        
FORMUL   6    K    2(K 1+)                                                      
FORMUL   8  EDO    C2 H6 O2                                                     
FORMUL   9  BES    C16 H24 N2 O4                                                
FORMUL  10  HOH   *288(H2 O)                                                    
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  ASP A  371  5                                   4    
HELIX    8   8 LEU A  372  HIS A  391  1                                  20    
HELIX    9   9 PRO A  392  ASP A  398  5                                   7    
HELIX   10  10 TYR A  399  ALA A  412  1                                  14    
HELIX   11  11 ASN A  425  MET A  432  1                                   8    
HELIX   12  12 ASP A  434  LEU A  452  1                                  19    
HELIX   13  13 SER A  453  SER A  469  1                                  17    
HELIX   14  14 LYS A  474  SER A  484  1                                  11    
HELIX   15  15 ASP A  516  LEU A  526  1                                  11    
HELIX   16  16 VAL A  602  ASN A  605  5                                   4    
HELIX   17  17 ASP A  615  THR A  627  1                                  13    
HELIX   18  18 HIS A  628  VAL A  631  5                                   4    
HELIX   19  19 SER A  632  SER A  648  1                                  17    
HELIX   20  20 SER A  653  LEU A  662  1                                  10    
HELIX   21  21 TYR A  663  GLU A  667  5                                   5    
HELIX   22  22 GLU A  669  LYS A  689  1                                  21    
HELIX   23  23 MET A  692  LYS A  713  1                                  22    
HELIX   24  24 SER A  721  HIS A  738  1                                  18    
HELIX   25  25 TYR A  740  SER A  757  1                                  18    
HELIX   26  26 PRO A  764  ASP A  766  5                                   3    
HELIX   27  27 VAL A  767  ALA A  776  1                                  10    
HELIX   28  28 SER A  778  GLN A  790  1                                  13    
HELIX   29  29 SER A  794  CYS A  806  1                                  13    
HELIX   30  30 ASN A  810  GLY A  824  1                                  15    
HELIX   31  31 LYS A  828  GLN A  830  5                                   3    
HELIX   32  32 GLU A  831  ARG A  841  1                                  11    
HELIX   33  33 GLY A  845  ASN A  856  1                                  12    
HELIX   34  34 ASN A  856  GLU A  865  1                                  10    
HELIX   35  35 SER A  868  ASN A  880  1                                  13    
HELIX   36  36 THR A  884  LEU A  898  1                                  15    
HELIX   37  37 LYS A  899  GLY A  902  5                                   4    
HELIX   38  38 LEU A  905  GLU A  936  1                                  32    
SHEET    1  AA 8 SER A 116  PRO A 119  0                                        
SHEET    2  AA 8 GLN A 101  LYS A 109 -1  O  LEU A 107   N  GLU A 118           
SHEET    3  AA 8 TYR A 145  ASN A 154 -1  O  THR A 146   N  ARG A 108           
SHEET    4  AA 8 THR A  75  ALA A  86 -1  O  PHE A  76   N  GLY A 153           
SHEET    5  AA 8 VAL A  58  ASN A  70 -1  O  ILE A  59   N  THR A  85           
SHEET    6  AA 8 SER A 202  ARG A 209  1  O  SER A 202   N  TYR A  63           
SHEET    7  AA 8 LEU A 231  PHE A 236 -1  O  ILE A 232   N  ARG A 209           
SHEET    8  AA 8 LEU A 221  ALA A 228 -1  N  VAL A 222   O  HIS A 235           
SHEET    1  AB 3 THR A  90  HIS A  96  0                                        
SHEET    2  AB 3 GLN A 130  LEU A 139 -1  O  ILE A 131   N  LEU A  95           
SHEET    3  AB 3 GLN A 121  HIS A 125 -1  O  GLN A 121   N  LEU A 134           
SHEET    1  AC 2 GLY A 161  ARG A 168  0                                        
SHEET    2  AC 2 LEU A 174  GLN A 181 -1  O  ARG A 175   N  TYR A 167           
SHEET    1  AD 2 LEU A 214  SER A 217  0                                        
SHEET    2  AD 2 PHE A 249  SER A 252 -1  O  ILE A 250   N  ILE A 216           
SHEET    1  AE 5 GLU A 255  ILE A 260  0                                        
SHEET    2  AE 5 LYS A 266  ALA A 271 -1  O  VAL A 267   N  LYS A 259           
SHEET    3  AE 5 LYS A 305  ILE A 311  1  O  GLN A 306   N  SER A 268           
SHEET    4  AE 5 LEU A 324  ARG A 328  1  O  THR A 325   N  ALA A 309           
SHEET    5  AE 5 ALA A 318  MET A 319 -1  O  MET A 319   N  THR A 326           
SHEET    1  AF 2 VAL A 364  MET A 366  0                                        
SHEET    2  AF 2 LYS A 471  THR A 473  1  O  LYS A 471   N  THR A 365           
SHEET    1  AG 4 THR A 586  ILE A 590  0                                        
SHEET    2  AG 4 ASN A 541  TYR A 549 -1  O  VAL A 542   N  LEU A 589           
SHEET    3  AG 4 PHE A 530  ARG A 538 -1  O  PHE A 530   N  TYR A 549           
SHEET    4  AG 4 ILE A 609  TYR A 612  1  O  ILE A 609   N  ILE A 533           
SHEET    1  AH 3 HIS A 578  LEU A 582  0                                        
SHEET    2  AH 3 VAL A 565  THR A 571 -1  O  VAL A 565   N  LEU A 582           
SHEET    3  AH 3 ILE A 598  PHE A 600 -1  O  LYS A 599   N  ILE A 570           
SSBOND   1 CYS A  404    CYS A  443                          1555   1555  2.07  
SSBOND   2 CYS A  736    CYS A  743                          1555   1555  2.09  
LINK         ND2 ASN A  70                 C1  NAG A1941     1555   1555  1.41  
LINK         ND2 ASN A 154                 C1  NAG A1942     1555   1555  1.45  
LINK         ND2 ASN A 414                 C1  NAG A1943     1555   1555  1.45  
LINK         O4  NAG A1941                 C1  NAG A1944     1555   1555  1.41  
LINK         O4  NAG A1942                 C1  NAG A1945     1555   1555  1.45  
LINK        ZN    ZN A1946                 OE1 GLU A 376     1555   1555  1.96  
LINK        ZN    ZN A1946                 NE2 HIS A 353     1555   1555  2.11  
LINK        ZN    ZN A1946                 NE2 HIS A 357     1555   1555  2.10  
LINK        ZN    ZN A1946                 O2  BES A1950     1555   1555  1.86  
LINK        ZN    ZN A1946                 O3  BES A1950     1555   1555  1.93  
LINK         K     K A1947                 OE1 GLU A 431     1555   1555  3.41  
LINK         K     K A1948                 O   ASP A 295     1555   1555  2.66  
LINK         K     K A1948                 OG  SER A 298     1555   1555  3.05  
LINK         K     K A1948                 OG  SER A 298     1555  11555  2.97  
LINK         K     K A1948                 OD1 ASP A 295     1555   1555  2.63  
CISPEP   1 GLU A  183    PRO A  184          0        -0.49                     
SITE     1 AC1  4 HIS A 353  HIS A 357  GLU A 376  BES A1950                    
SITE     1 AC2  2 GLU A 431  ARG A 906                                          
SITE     1 AC3  2 ASP A 295  SER A 298                                          
SITE     1 AC4  2 TYR A 451  ARG A 579                                          
SITE     1 AC5 14 GLN A 181  GLU A 183  SER A 316  GLY A 317                    
SITE     2 AC5 14 ALA A 318  MET A 319  GLU A 320  HIS A 353                    
SITE     3 AC5 14 GLU A 354  HIS A 357  GLU A 376  LYS A 380                    
SITE     4 AC5 14 TYR A 438   ZN A1946                                          
SITE     1 AC6 10 HIS A  68  ALA A  69  ASN A  70  GLN A  88                    
SITE     2 AC6 10 HIS A  99  ASN A 154  GLU A 210  GLU A 229                    
SITE     3 AC6 10 ASN A 414  NAG A1945                                          
SITE     1 AC7  6 GLN A  88  HIS A  99  ASN A 154  GLU A 229                    
SITE     2 AC7  6 ASN A 414  NAG A1941                                          
CRYST1  200.948  200.948  114.222  90.00  90.00 120.00 P 6 2 2      12          
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      0.004976  0.002873  0.000000        0.00000                         
SCALE2      0.000000  0.005746  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008755        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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