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Database: PDB
Entry: 1NQL
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Original site: 1NQL 
HEADER    HORMONE/GROWTH FACTOR RECEPTOR          21-JAN-03   1NQL              
TITLE     STRUCTURE OF THE EXTRACELLULAR DOMAIN OF HUMAN EPIDERMAL GROWTH FACTOR
TITLE    2 (EGF) RECEPTOR IN AN INACTIVE (LOW PH) COMPLEX WITH EGF.             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: EPIDERMAL GROWTH FACTOR RECEPTOR;                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: EXTRACELLULAR DOMAIN;                                      
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: EPIDERMAL GROWTH FACTOR;                                   
COMPND   8 CHAIN: B;                                                            
COMPND   9 SYNONYM: EGF, [CONTAINS: EPIDERMAL GROWTH FACTOR UROGASTRONE, ];     
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 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: VIRUS;                                     
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606;                                                
SOURCE  14 GENE: EGF;                                                           
SOURCE  15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    CELL SURFACE RECEPTOR, TYROSINE KINASE, GLYCOPROTEIN, ENDOSOMAL,      
KEYWDS   2 GROWTH FACTOR, AUTO-INHIBITION, HORMONE-GROWTH FACTOR RECEPTOR       
KEYWDS   3 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.M.FERGUSON,M.A.LEMMON                                               
REVDAT   3   13-JUL-11 1NQL    1       VERSN                                    
REVDAT   2   24-FEB-09 1NQL    1       VERSN                                    
REVDAT   1   11-MAR-03 1NQL    0                                                
JRNL        AUTH   K.M.FERGUSON,M.B.BERGER,J.M.MENDROLA,H.CHO,D.J.LEAHY,        
JRNL        AUTH 2 M.A.LEMMON                                                   
JRNL        TITL   EGF ACTIVATES ITS RECEPTOR BY REMOVING INTERACTIONS THAT     
JRNL        TITL 2 AUTO-INHIBIT ECTODOMAIN DIMERIZATION                         
JRNL        REF    MOL.CELL                      V.  11   507 2003              
JRNL        REFN                   ISSN 1097-2765                               
JRNL        PMID   12620237                                                     
JRNL        DOI    10.1016/S1097-2765(03)00047-9                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.24                                        
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 23435                          
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) : 0.247                           
REMARK   3   R VALUE            (WORKING SET) : 0.241                           
REMARK   3   FREE R VALUE                     : 0.310                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2563                            
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) : 2.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.87                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1600                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3620                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 170                          
REMARK   3   BIN FREE R VALUE                    : 0.4340                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4974                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 176                                     
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 14.79                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.67000                                             
REMARK   3    B22 (A**2) : -3.92000                                             
REMARK   3    B33 (A**2) : 4.87000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.74000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): NULL          
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.911                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.860                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5275 ; 0.014 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7191 ; 1.766 ; 1.991       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   656 ; 8.206 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   819 ; 0.111 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3938 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2137 ; 0.244 ; 0.200       
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):   159 ; 0.181 ; 0.200       
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):    51 ; 0.203 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     7 ; 0.237 ; 0.200       
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):  3265 ; 0.608 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5233 ; 1.206 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2010 ; 2.319 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1958 ; 4.139 ; 4.500       
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 : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : NULL                                          
REMARK   3   ION PROBE RADIUS   : NULL                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1NQL COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-JAN-03.                  
REMARK 100 THE RCSB ID CODE IS RCSB018115.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-SEP-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CHESS                              
REMARK 200  BEAMLINE                       : F1                                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.94                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26060                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.0                               
REMARK 200  DATA REDUNDANCY                : 3.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.04800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 50.00                    
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.90                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.34000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1M6B                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 66.05                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.62                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG3400,AMMONIUM SULFATE, MAGNESIUM      
REMARK 280  SULFATE, SODIUM CITRATE, PH 5.0, VAPOR DIFFUSION, HANGING DROP,     
REMARK 280  TEMPERATURE 297K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       59.58500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       51.83000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       59.58500            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       51.83000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     LEU A     1                                                      
REMARK 465     GLU A     2                                                      
REMARK 465     ASN A   615                                                      
REMARK 465     GLY A   616                                                      
REMARK 465     PRO A   617                                                      
REMARK 465     LYS A   618                                                      
REMARK 465     HIS A   619                                                      
REMARK 465     HIS A   620                                                      
REMARK 465     HIS A   621                                                      
REMARK 465     HIS A   622                                                      
REMARK 465     HIS A   623                                                      
REMARK 465     HIS A   624                                                      
REMARK 465     ASN B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     GLU B    51                                                      
REMARK 465     LEU B    52                                                      
REMARK 465     ARG B    53                                                      
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     GLU A   3    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 105    CG   CD   CE   NZ                                   
REMARK 470     LYS A 109    CG   CD   CE   NZ                                   
REMARK 470     LYS A 270    CG   CD   CE   NZ                                   
REMARK 470     ARG A 273    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 285    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP A 290    CG   OD1  OD2                                       
REMARK 470     GLU A 293    CG   CD   OE1  OE2                                  
REMARK 470     MET A 294    CG   SD   CE                                        
REMARK 470     GLU A 295    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 297    CG   OD1  OD2                                       
REMARK 470     LYS A 303    CG   CD   CE   NZ                                   
REMARK 470     GLU A 320    CG   CD   OE1  OE2                                  
REMARK 470     PHE A 321    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS A 322    CG   CD   CE   NZ                                   
REMARK 470     ASP A 323    CG   OD1  OD2                                       
REMARK 470     LYS A 375    CG   CD   CE   NZ                                   
REMARK 470     LYS A 407    CG   CD   CE   NZ                                   
REMARK 470     LYS A 443    CG   CD   CE   NZ                                   
REMARK 470     LYS A 454    CG   CD   CE   NZ                                   
REMARK 470     LYS A 455    CG   CD   CE   NZ                                   
REMARK 470     GLN A 462    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 463    CG   CD   CE   NZ                                   
REMARK 470     GLU A 472    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 476    CG   CD   CE   NZ                                   
REMARK 470     ARG A 497    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR A 614    OG1  CG2                                            
REMARK 470     LYS B  48    CG   CD   CE   NZ                                   
REMARK 470     TRP B  50    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP B  50    CZ3  CH2                                            
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     GLU A    3                                                       
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     LYS A    4   N    CA   C    O    CB                              
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   CA   LYS A     4     N    LYS A     5              1.53            
REMARK 500   C    LYS A     4     CA   LYS A     5              1.67            
REMARK 500   O    LYS A     4     N    LYS A     5              1.69            
REMARK 500   SD   MET A   576     O3   NAG A  5791              2.15            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    LYS A   4   CB    LYS A   4   CG     -0.255                       
REMARK 500    LYS A   4   C     LYS A   5   N      -0.816                       
REMARK 500    GLU A  90   CD    GLU A  90   OE2     0.074                       
REMARK 500    MET A 244   CG    MET A 244   SD      0.199                       
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    LYS A   4   CA  -  CB  -  CG  ANGL. DEV. =  22.2 DEGREES          
REMARK 500    LYS A   4   CB  -  CG  -  CD  ANGL. DEV. = -28.1 DEGREES          
REMARK 500    LYS A   4   CA  -  C   -  N   ANGL. DEV. = -34.2 DEGREES          
REMARK 500    LYS A   4   O   -  C   -  N   ANGL. DEV. =  28.1 DEGREES          
REMARK 500    LYS A   5   C   -  N   -  CA  ANGL. DEV. = -19.2 DEGREES          
REMARK 500    ASP A  22   CB  -  CG  -  OD2 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ASP A 102   CB  -  CG  -  OD2 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ASP A 142   CB  -  CG  -  OD2 ANGL. DEV. =   7.2 DEGREES          
REMARK 500    ASP A 206   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ARG A 231   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500    ASP A 355   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ASP A 434   CB  -  CG  -  OD2 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    CYS A 491   CA  -  CB  -  SG  ANGL. DEV. =   8.1 DEGREES          
REMARK 500    ASP B  11   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 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    LYS A   4     -157.77    129.83                                   
REMARK 500    LYS A   5      124.90     19.47                                   
REMARK 500    LYS A  13     -118.84     27.25                                   
REMARK 500    ASN A  32      116.20    -39.18                                   
REMARK 500    TYR A  45       -1.92     63.96                                   
REMARK 500    LEU A  52       45.46    -99.26                                   
REMARK 500    LEU A  55       -5.56    -50.08                                   
REMARK 500    ASN A  91       -6.45     72.52                                   
REMARK 500    SER A  92      -21.82   -164.37                                   
REMARK 500    SER A  99       81.63     53.30                                   
REMARK 500    ALA A 103       80.76    -64.21                                   
REMARK 500    ASN A 104      -24.26    172.38                                   
REMARK 500    LYS A 105       37.90     76.49                                   
REMARK 500    MET A 113       47.52    -89.32                                   
REMARK 500    ALA A 123     -169.28   -106.78                                   
REMARK 500    ASN A 128       71.83     48.32                                   
REMARK 500    PRO A 130        5.44    -65.99                                   
REMARK 500    ASN A 134      -44.48     68.46                                   
REMARK 500    GLU A 136      -46.67    -25.37                                   
REMARK 500    ILE A 138      151.63    -49.01                                   
REMARK 500    SER A 162       42.09    -76.72                                   
REMARK 500    SER A 169       41.19    -79.20                                   
REMARK 500    ASN A 172       37.79     31.33                                   
REMARK 500    LYS A 188      -44.21   -156.93                                   
REMARK 500    CYS A 191     -142.23    173.00                                   
REMARK 500    GLN A 193      -39.32    -37.81                                   
REMARK 500    SER A 196       47.27   -100.93                                   
REMARK 500    ASP A 206        2.47    -65.25                                   
REMARK 500    LYS A 229      -84.05   -124.23                                   
REMARK 500    GLU A 233     -118.58     62.16                                   
REMARK 500    TYR A 261     -173.18    -67.47                                   
REMARK 500    ARG A 273     -108.27     21.54                                   
REMARK 500    TYR A 292      106.57   -178.04                                   
REMARK 500    MET A 294     -169.52   -120.48                                   
REMARK 500    ASP A 297       90.97     65.89                                   
REMARK 500    CYS A 309      126.49    -38.30                                   
REMARK 500    ARG A 310      114.89    -35.86                                   
REMARK 500    ASN A 314      -82.66    -47.01                                   
REMARK 500    HIS A 334       13.63    -62.32                                   
REMARK 500    LYS A 336      -80.54    -68.65                                   
REMARK 500    ASN A 337       35.67    -85.42                                   
REMARK 500    PRO A 349      -39.10    -34.77                                   
REMARK 500    TRP A 386      138.11    172.10                                   
REMARK 500    ASN A 389      -19.33    -44.84                                   
REMARK 500    LEU A 393       46.68    -85.56                                   
REMARK 500    HIS A 409       11.04     50.53                                   
REMARK 500    GLN A 411      -30.94   -144.08                                   
REMARK 500    LYS A 443        8.11    -63.01                                   
REMARK 500    TRP A 453      -32.94    -31.09                                   
REMARK 500    LYS A 465       59.99   -149.84                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      68 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLU A  521     PRO A  522                  149.23                    
REMARK 500 GLU A  578     ASN A  579                 -135.10                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    ASN A 579        18.6      L          L   OUTSIDE RANGE           
REMARK 500    ASN A 580        19.4      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     NAG A  625                                                       
REMARK 610     NAG A 4202                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 625                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 3281                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 3282                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 3283                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 3371                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 3372                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 3373                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 4201                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 4202                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 5041                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 5441                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 5442                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 5791                
DBREF  1NQL A    1   618  GB     4885199  NP_005219       25    642             
DBREF  1NQL B    1    53  UNP    P01133   EGF_HUMAN      971   1023             
SEQRES   1 A  624  LEU GLU GLU LYS LYS VAL CYS GLN GLY THR SER ASN LYS          
SEQRES   2 A  624  LEU THR GLN LEU GLY THR PHE GLU ASP HIS PHE LEU SER          
SEQRES   3 A  624  LEU GLN ARG MET PHE ASN ASN CYS GLU VAL VAL LEU GLY          
SEQRES   4 A  624  ASN LEU GLU ILE THR TYR VAL GLN ARG ASN TYR ASP LEU          
SEQRES   5 A  624  SER PHE LEU LYS THR ILE GLN GLU VAL ALA GLY TYR VAL          
SEQRES   6 A  624  LEU ILE ALA LEU ASN THR VAL GLU ARG ILE PRO LEU GLU          
SEQRES   7 A  624  ASN LEU GLN ILE ILE ARG GLY ASN MET TYR TYR GLU ASN          
SEQRES   8 A  624  SER TYR ALA LEU ALA VAL LEU SER ASN TYR ASP ALA ASN          
SEQRES   9 A  624  LYS THR GLY LEU LYS GLU LEU PRO MET ARG ASN LEU GLN          
SEQRES  10 A  624  GLU ILE LEU HIS GLY ALA VAL ARG PHE SER ASN ASN PRO          
SEQRES  11 A  624  ALA LEU CYS ASN VAL GLU SER ILE GLN TRP ARG ASP ILE          
SEQRES  12 A  624  VAL SER SER ASP PHE LEU SER ASN MET SER MET ASP PHE          
SEQRES  13 A  624  GLN ASN HIS LEU GLY SER CYS GLN LYS CYS ASP PRO SER          
SEQRES  14 A  624  CYS PRO ASN GLY SER CYS TRP GLY ALA GLY GLU GLU ASN          
SEQRES  15 A  624  CYS GLN LYS LEU THR LYS ILE ILE CYS ALA GLN GLN CYS          
SEQRES  16 A  624  SER GLY ARG CYS ARG GLY LYS SER PRO SER ASP CYS CYS          
SEQRES  17 A  624  HIS ASN GLN CYS ALA ALA GLY CYS THR GLY PRO ARG GLU          
SEQRES  18 A  624  SER ASP CYS LEU VAL CYS ARG LYS PHE ARG ASP GLU ALA          
SEQRES  19 A  624  THR CYS LYS ASP THR CYS PRO PRO LEU MET LEU TYR ASN          
SEQRES  20 A  624  PRO THR THR TYR GLN MET ASP VAL ASN PRO GLU GLY LYS          
SEQRES  21 A  624  TYR SER PHE GLY ALA THR CYS VAL LYS LYS CYS PRO ARG          
SEQRES  22 A  624  ASN TYR VAL VAL THR ASP HIS GLY SER CYS VAL ARG ALA          
SEQRES  23 A  624  CYS GLY ALA ASP SER TYR GLU MET GLU GLU ASP GLY VAL          
SEQRES  24 A  624  ARG LYS CYS LYS LYS CYS GLU GLY PRO CYS ARG LYS VAL          
SEQRES  25 A  624  CYS ASN GLY ILE GLY ILE GLY GLU PHE LYS ASP SER LEU          
SEQRES  26 A  624  SER ILE ASN ALA THR ASN ILE LYS HIS PHE LYS ASN CYS          
SEQRES  27 A  624  THR SER ILE SER GLY ASP LEU HIS ILE LEU PRO VAL ALA          
SEQRES  28 A  624  PHE ARG GLY ASP SER PHE THR HIS THR PRO PRO LEU ASP          
SEQRES  29 A  624  PRO GLN GLU LEU ASP ILE LEU LYS THR VAL LYS GLU ILE          
SEQRES  30 A  624  THR GLY PHE LEU LEU ILE GLN ALA TRP PRO GLU ASN ARG          
SEQRES  31 A  624  THR ASP LEU HIS ALA PHE GLU ASN LEU GLU ILE ILE ARG          
SEQRES  32 A  624  GLY ARG THR LYS GLN HIS GLY GLN PHE SER LEU ALA VAL          
SEQRES  33 A  624  VAL SER LEU ASN ILE THR SER LEU GLY LEU ARG SER LEU          
SEQRES  34 A  624  LYS GLU ILE SER ASP GLY ASP VAL ILE ILE SER GLY ASN          
SEQRES  35 A  624  LYS ASN LEU CYS TYR ALA ASN THR ILE ASN TRP LYS LYS          
SEQRES  36 A  624  LEU PHE GLY THR SER GLY GLN LYS THR LYS ILE ILE SER          
SEQRES  37 A  624  ASN ARG GLY GLU ASN SER CYS LYS ALA THR GLY GLN VAL          
SEQRES  38 A  624  CYS HIS ALA LEU CYS SER PRO GLU GLY CYS TRP GLY PRO          
SEQRES  39 A  624  GLU PRO ARG ASP CYS VAL SER CYS ARG ASN VAL SER ARG          
SEQRES  40 A  624  GLY ARG GLU CYS VAL ASP LYS CYS LYS LEU LEU GLU GLY          
SEQRES  41 A  624  GLU PRO ARG GLU PHE VAL GLU ASN SER GLU CYS ILE GLN          
SEQRES  42 A  624  CYS HIS PRO GLU CYS LEU PRO GLN ALA MET ASN ILE THR          
SEQRES  43 A  624  CYS THR GLY ARG GLY PRO ASP ASN CYS ILE GLN CYS ALA          
SEQRES  44 A  624  HIS TYR ILE ASP GLY PRO HIS CYS VAL LYS THR CYS PRO          
SEQRES  45 A  624  ALA GLY VAL MET GLY GLU ASN ASN THR LEU VAL TRP LYS          
SEQRES  46 A  624  TYR ALA ASP ALA GLY HIS VAL CYS HIS LEU CYS HIS PRO          
SEQRES  47 A  624  ASN CYS THR TYR GLY CYS THR GLY PRO GLY LEU GLU GLY          
SEQRES  48 A  624  CYS PRO THR ASN GLY PRO LYS HIS HIS HIS HIS HIS HIS          
SEQRES   1 B   53  ASN SER ASP SER GLU CYS PRO LEU SER HIS ASP GLY TYR          
SEQRES   2 B   53  CYS LEU HIS ASP GLY VAL CYS MET TYR ILE GLU ALA LEU          
SEQRES   3 B   53  ASP LYS TYR ALA CYS ASN CYS VAL VAL GLY TYR ILE GLY          
SEQRES   4 B   53  GLU ARG CYS GLN TYR ARG ASP LEU LYS TRP TRP GLU LEU          
SEQRES   5 B   53  ARG                                                          
MODRES 1NQL ASN A  420  ASN  GLYCOSYLATION SITE                                 
MODRES 1NQL ASN A  328  ASN  GLYCOSYLATION SITE                                 
MODRES 1NQL ASN A  337  ASN  GLYCOSYLATION SITE                                 
MODRES 1NQL ASN A  504  ASN  GLYCOSYLATION SITE                                 
MODRES 1NQL ASN A  544  ASN  GLYCOSYLATION SITE                                 
MODRES 1NQL ASN A  579  ASN  GLYCOSYLATION SITE                                 
HET    NAG  A 625      14                                                       
HET    NAG  A3281      14                                                       
HET    NAG  A3282      14                                                       
HET    BMA  A3283      11                                                       
HET    NAG  A3371      14                                                       
HET    NAG  A3372      14                                                       
HET    BMA  A3373      11                                                       
HET    NAG  A4201      14                                                       
HET    NAG  A4202      14                                                       
HET    NAG  A5041      14                                                       
HET    NAG  A5441      14                                                       
HET    NAG  A5442      14                                                       
HET    NAG  A5791      14                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     BMA BETA-D-MANNOSE                                                   
FORMUL   3  NAG    11(C8 H15 N O6)                                              
FORMUL   4  BMA    2(C6 H12 O6)                                                 
HELIX    1   1 THR A   19  ASN A   32  1                                  14    
HELIX    2   2 SER A   53  ILE A   58  5                                   6    
HELIX    3   3 ASN A  134  ILE A  138  5                                   5    
HELIX    4   4 GLN A  139  VAL A  144  1                                   6    
HELIX    5   5 SER A  145  MET A  152  5                                   8    
HELIX    6   6 CYS A  170  SER A  174  5                                   5    
HELIX    7   7 GLY A  179  CYS A  183  5                                   5    
HELIX    8   8 SER A  203  CYS A  207  5                                   5    
HELIX    9   9 ILE A  318  LYS A  322  5                                   5    
HELIX   10  10 ASN A  331  LYS A  336  5                                   6    
HELIX   11  11 PRO A  349  GLY A  354  1                                   6    
HELIX   12  12 ASP A  364  VAL A  374  5                                  11    
HELIX   13  13 LEU A  393  GLU A  397  5                                   5    
HELIX   14  14 LYS A  407  GLY A  410  5                                   4    
HELIX   15  15 ASN A  452  LEU A  456  5                                   5    
HELIX   16  16 GLY A  471  GLY A  479  1                                   9    
HELIX   17  17 GLU A  495  CYS A  499  5                                   5    
SHEET    1   A 5 VAL A   6  CYS A   7  0                                        
SHEET    2   A 5 VAL A  36  VAL A  37  1  O  VAL A  36   N  CYS A   7           
SHEET    3   A 5 GLU A  60  VAL A  61  1  O  GLU A  60   N  VAL A  37           
SHEET    4   A 5 ILE A  82  ILE A  83  1  O  ILE A  82   N  VAL A  61           
SHEET    5   A 5 GLU A 118  ILE A 119  1  O  GLU A 118   N  ILE A  83           
SHEET    1   B 3 GLN A  16  LEU A  17  0                                        
SHEET    2   B 3 LYS B  28  CYS B  33  1  O  CYS B  31   N  GLN A  16           
SHEET    3   B 3 VAL B  19  ILE B  23 -1  N  VAL B  19   O  ASN B  32           
SHEET    1   C 5 LEU A  41  THR A  44  0                                        
SHEET    2   C 5 VAL A  65  ALA A  68  1  O  LEU A  66   N  ILE A  43           
SHEET    3   C 5 TYR A  93  LEU A  98  1  O  ALA A  94   N  VAL A  65           
SHEET    4   C 5 ALA A 123  SER A 127  1  O  ARG A 125   N  VAL A  97           
SHEET    5   C 5 SER A 153  MET A 154  1  O  SER A 153   N  PHE A 126           
SHEET    1   D 2 PHE A 230  ASP A 232  0                                        
SHEET    2   D 2 THR A 235  LYS A 237 -1  O  LYS A 237   N  PHE A 230           
SHEET    1   E 2 MET A 244  TYR A 246  0                                        
SHEET    2   E 2 MET A 253  VAL A 255 -1  O  ASP A 254   N  LEU A 245           
SHEET    1   F 2 TYR A 261  PHE A 263  0                                        
SHEET    2   F 2 THR A 266  VAL A 268 -1  O  THR A 266   N  PHE A 263           
SHEET    1   G 2 VAL A 276  VAL A 277  0                                        
SHEET    2   G 2 CYS A 283  VAL A 284 -1  O  VAL A 284   N  VAL A 276           
SHEET    1   H 5 VAL A 312  CYS A 313  0                                        
SHEET    2   H 5 SER A 340  ILE A 341  1  O  SER A 340   N  CYS A 313           
SHEET    3   H 5 GLU A 376  ILE A 377  1  O  GLU A 376   N  ILE A 341           
SHEET    4   H 5 ILE A 401  ILE A 402  1  O  ILE A 401   N  ILE A 377           
SHEET    5   H 5 GLU A 431  ILE A 432  1  O  GLU A 431   N  ILE A 402           
SHEET    1   I 5 LEU A 345  ILE A 347  0                                        
SHEET    2   I 5 LEU A 381  ILE A 383  1  O  LEU A 382   N  LEU A 345           
SHEET    3   I 5 PHE A 412  VAL A 417  1  O  SER A 413   N  LEU A 381           
SHEET    4   I 5 ASP A 436  SER A 440  1  O  ILE A 438   N  VAL A 416           
SHEET    5   I 5 ILE A 466  ILE A 467  1  O  ILE A 467   N  ILE A 439           
SHEET    1   J 2 VAL A 505  ARG A 507  0                                        
SHEET    2   J 2 GLU A 510  VAL A 512 -1  O  GLU A 510   N  ARG A 507           
SHEET    1   K 2 GLU A 524  VAL A 526  0                                        
SHEET    2   K 2 CYS A 531  GLN A 533 -1  O  ILE A 532   N  PHE A 525           
SHEET    1   L 2 TYR A 561  ASP A 563  0                                        
SHEET    2   L 2 HIS A 566  VAL A 568 -1  O  VAL A 568   N  TYR A 561           
SHEET    1   M 3 ALA A 573  MET A 576  0                                        
SHEET    2   M 3 LEU A 582  ALA A 587 -1  O  VAL A 583   N  VAL A 575           
SHEET    3   M 3 CYS A 593  LEU A 595 -1  O  HIS A 594   N  TYR A 586           
SHEET    1   N 2 SER B   4  GLU B   5  0                                        
SHEET    2   N 2 TYR B  13  CYS B  14 -1  O  CYS B  14   N  SER B   4           
SHEET    1   O 2 TYR B  37  ILE B  38  0                                        
SHEET    2   O 2 TYR B  44  ARG B  45 -1  O  TYR B  44   N  ILE B  38           
SSBOND   1 CYS A    7    CYS A   34                          1555   1555  2.07  
SSBOND   2 CYS A  133    CYS A  163                          1555   1555  2.05  
SSBOND   3 CYS A  166    CYS A  175                          1555   1555  2.03  
SSBOND   4 CYS A  170    CYS A  183                          1555   1555  2.06  
SSBOND   5 CYS A  191    CYS A  199                          1555   1555  2.10  
SSBOND   6 CYS A  195    CYS A  207                          1555   1555  2.03  
SSBOND   7 CYS A  208    CYS A  216                          1555   1555  2.08  
SSBOND   8 CYS A  212    CYS A  224                          1555   1555  2.02  
SSBOND   9 CYS A  227    CYS A  236                          1555   1555  2.03  
SSBOND  10 CYS A  240    CYS A  267                          1555   1555  2.08  
SSBOND  11 CYS A  271    CYS A  283                          1555   1555  2.05  
SSBOND  12 CYS A  287    CYS A  302                          1555   1555  2.06  
SSBOND  13 CYS A  305    CYS A  309                          1555   1555  2.06  
SSBOND  14 CYS A  313    CYS A  338                          1555   1555  2.05  
SSBOND  15 CYS A  446    CYS A  475                          1555   1555  2.08  
SSBOND  16 CYS A  482    CYS A  491                          1555   1555  2.06  
SSBOND  17 CYS A  486    CYS A  499                          1555   1555  2.05  
SSBOND  18 CYS A  502    CYS A  511                          1555   1555  2.05  
SSBOND  19 CYS A  515    CYS A  531                          1555   1555  2.02  
SSBOND  20 CYS A  534    CYS A  547                          1555   1555  2.06  
SSBOND  21 CYS A  538    CYS A  555                          1555   1555  2.07  
SSBOND  22 CYS A  558    CYS A  567                          1555   1555  2.02  
SSBOND  23 CYS A  571    CYS A  593                          1555   1555  2.04  
SSBOND  24 CYS A  596    CYS A  604                          1555   1555  2.04  
SSBOND  25 CYS A  600    CYS A  612                          1555   1555  2.04  
SSBOND  26 CYS B    6    CYS B   20                          1555   1555  2.08  
SSBOND  27 CYS B   14    CYS B   31                          1555   1555  2.04  
SSBOND  28 CYS B   33    CYS B   42                          1555   1555  2.07  
LINK         ND2 ASN A 420                 C1  NAG A4201     1555   1555  1.45  
LINK         ND2 ASN A 328                 C1  NAG A3281     1555   1555  1.43  
LINK         ND2 ASN A 337                 C1  NAG A3371     1555   1555  1.36  
LINK         ND2 ASN A 504                 C1  NAG A5041     1555   1555  1.45  
LINK         ND2 ASN A 544                 C1  NAG A5441     1555   1555  1.44  
LINK         ND2 ASN A 579                 C1  NAG A5791     1555   1555  1.50  
LINK         O4  NAG A3281                 C1  NAG A3282     1555   1555  1.45  
LINK         O4  NAG A3371                 C1  NAG A3372     1555   1555  1.45  
LINK         O4  NAG A5441                 C1  NAG A5442     1555   1555  1.45  
LINK         O4  NAG A3372                 C1  BMA A3373     1555   1555  1.46  
LINK         O4  NAG A3282                 C1  BMA A3283     1555   1555  1.45  
LINK         ND2 ASN A 337                 C2  NAG A3371     1555   1555  2.01  
SITE     1 AC1  3 GLN A  28  ASN A  32  ASN A  33                               
SITE     1 AC2  7 SER A 324  LEU A 325  SER A 326  ASN A 328                    
SITE     2 AC2  7 ASN A 331  THR A 358  NAG A3282                               
SITE     1 AC3  3 ASP A 323  NAG A3281  BMA A3283                               
SITE     1 AC4  2 ASP A 323  NAG A3282                                          
SITE     1 AC5  2 ASN A 337  NAG A3372                                          
SITE     1 AC6  2 NAG A3371  BMA A3373                                          
SITE     1 AC7  1 NAG A3372                                                     
SITE     1 AC8  5 GLU A 388  ASN A 389  ASN A 420  ASN A 444                    
SITE     2 AC8  5 NAG A4202                                                     
SITE     1 AC9  1 NAG A4201                                                     
SITE     1 BC1  3 ARG A 503  ASN A 504  ASP A 513                               
SITE     1 BC2  6 TYR A 101  ALA A 542  ASN A 544  NAG A5442                    
SITE     2 BC2  6 GLU B  24  ALA B  25                                          
SITE     1 BC3  4 TYR A 101  HIS A 594  NAG A5441  ALA B  25                    
SITE     1 BC4  6 PRO A 241  ASN A 256  GLU A 258  MET A 576                    
SITE     2 BC4  6 GLY A 577  ASN A 579                                          
CRYST1  119.170  103.660  101.490  90.00 119.27  90.00 C 1 2 1       4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.008391  0.000000  0.004703        0.00000                         
SCALE2      0.000000  0.009647  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011295        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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