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Database: PDB
Entry: 1YY9
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Original site: 1YY9 
HEADER    IMMUNE SYSTEM/TRANSFERASE               24-FEB-05   1YY9              
TITLE     STRUCTURE OF THE EXTRACELLULAR DOMAIN OF THE EPIDERMAL GROWTH FACTOR  
TITLE    2 RECEPTOR IN COMPLEX WITH THE FAB FRAGMENT OF CETUXIMAB/ERBITUX/IMC-  
TITLE    3 C225                                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: EPIDERMAL GROWTH FACTOR RECEPTOR;                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 25-642;                                       
COMPND   5 SYNONYM: RECEPTOR TYROSINE-PROTEIN KINASE ERBB-1;                    
COMPND   6 EC: 2.7.10.1;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: CETUXIMAB FAB LIGHT CHAIN;                                 
COMPND  10 CHAIN: C;                                                            
COMPND  11 ENGINEERED: YES;                                                     
COMPND  12 MOL_ID: 3;                                                           
COMPND  13 MOLECULE: CETUXIMAB FAB HEAVY CHAIN;                                 
COMPND  14 CHAIN: D;                                                            
COMPND  15 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: EGFR, ERBB1;                                                   
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_ATCC_NUMBER: SF9;                                  
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: MUS MUSCULUS, HOMO SAPIENS;                     
SOURCE  13 ORGANISM_COMMON: HOUSE MOUSE, HUMAN;                                 
SOURCE  14 ORGANISM_TAXID: 10090,9606;                                          
SOURCE  15 STRAIN: ,;                                                           
SOURCE  16 EXPRESSION_SYSTEM: MUS MUSCULUS;                                     
SOURCE  17 EXPRESSION_SYSTEM_COMMON: HOUSE MOUSE;                               
SOURCE  18 EXPRESSION_SYSTEM_TAXID: 10090;                                      
SOURCE  19 EXPRESSION_SYSTEM_STRAIN: SP2/0-AG15;                                
SOURCE  20 EXPRESSION_SYSTEM_ATCC_NUMBER: CRL-1581;                             
SOURCE  21 EXPRESSION_SYSTEM_CELL: MOUSE MYELOMA CELL LINE;                     
SOURCE  22 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  23 EXPRESSION_SYSTEM_PLASMID: PDHL2;                                    
SOURCE  24 MOL_ID: 3;                                                           
SOURCE  25 ORGANISM_SCIENTIFIC: MUS MUSCULUS, HOMO SAPIENS;                     
SOURCE  26 ORGANISM_COMMON: HOUSE MOUSE, HUMAN;                                 
SOURCE  27 ORGANISM_TAXID: 10090,9606;                                          
SOURCE  28 STRAIN: ,;                                                           
SOURCE  29 EXPRESSION_SYSTEM: MUS MUSCULUS;                                     
SOURCE  30 EXPRESSION_SYSTEM_COMMON: HOUSE MOUSE;                               
SOURCE  31 EXPRESSION_SYSTEM_TAXID: 10090;                                      
SOURCE  32 EXPRESSION_SYSTEM_STRAIN: SP2/0-AG15;                                
SOURCE  33 EXPRESSION_SYSTEM_ATCC_NUMBER: CRL-1581;                             
SOURCE  34 EXPRESSION_SYSTEM_CELL: MOUSE MYELOMA CELL LINE;                     
SOURCE  35 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  36 EXPRESSION_SYSTEM_PLASMID: PDHL2                                     
KEYWDS    CELL SURFACE RECEPTOR; TYROSINE KINASE; GLYCOPROTEIN;                 
KEYWDS   2 ANTIGEN:ANTIBODY COMPLEX; FAB FRAGMENT; ANTITUMOR; DRUG, IMMUNE      
KEYWDS   3 SYSTEM-TRANSFERASE COMPLEX                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.LI,K.R.SCHMITZ,P.D.JEFFREY,J.J.W.WILTZIUS,P.KUSSIE,K.M.FERGUSON     
REVDAT   4   13-JUL-11 1YY9    1       VERSN                                    
REVDAT   3   31-MAR-10 1YY9    1       COMPND                                   
REVDAT   2   24-FEB-09 1YY9    1       VERSN                                    
REVDAT   1   26-APR-05 1YY9    0                                                
JRNL        AUTH   S.LI,K.R.SCHMITZ,P.D.JEFFREY,J.J.W.WILTZIUS,P.KUSSIE,        
JRNL        AUTH 2 K.M.FERGUSON                                                 
JRNL        TITL   STRUCTURAL BASIS FOR INHIBITION OF THE EPIDERMAL GROWTH      
JRNL        TITL 2 FACTOR RECEPTOR BY CETUXIMAB                                 
JRNL        REF    CANCER CELL                   V.   7   301 2005              
JRNL        REFN                   ISSN 1535-6108                               
JRNL        PMID   15837620                                                     
JRNL        DOI    10.1016/J.CCR.2005.03.003                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2                                           
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 44979                          
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) : 0.242                           
REMARK   3   R VALUE            (WORKING SET) : 0.239                           
REMARK   3   FREE R VALUE                     : 0.289                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2352                            
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) : 2.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.67                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3074                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 92.17                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3390                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 165                          
REMARK   3   BIN FREE R VALUE                    : 0.4080                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7910                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 259                                     
REMARK   3   SOLVENT ATOMS            : 56                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 33.70                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.54000                                              
REMARK   3    B22 (A**2) : 0.81000                                              
REMARK   3    B33 (A**2) : -3.00000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -1.49000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.523         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.329         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.291         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 30.672        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.923                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.895                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  8368 ; 0.015 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 11425 ; 1.680 ; 1.986       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1041 ; 7.724 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   339 ;38.684 ;24.867       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1311 ;19.830 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    34 ;20.734 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1316 ; 0.109 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6190 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  3584 ; 0.241 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  5620 ; 0.319 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   282 ; 0.152 ; 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):    30 ; 0.203 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     6 ; 0.118 ; 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):  5286 ; 0.625 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  8373 ; 1.046 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3416 ; 1.618 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3013 ; 2.562 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  8629 ; 1.140 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):    72 ; 5.854 ; 3.000       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  8068 ; 1.528 ; 3.000       
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   : 1.20                                          
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 1YY9 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-MAR-05.                  
REMARK 100 THE RCSB ID CODE IS RCSB032063.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CHESS                              
REMARK 200  BEAMLINE                       : A1                                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.976                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 47467                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.500                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : 0.06000                            
REMARK 200  R SYM                      (I) : 0.06000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.69                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.85000                            
REMARK 200  R SYM FOR SHELL            (I) : 0.85000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1NQL AND 1YY8                              
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 64.40                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.48                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3450, AMMONIUM SULFATE, PH 7.5,      
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 300K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       35.43050            
REMARK 290   SMTRY3   2  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: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, D                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     LEU A     1                                                      
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     GLY C   212                                                      
REMARK 465     ALA C   213                                                      
REMARK 465     SER D   221                                                      
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   2    CG   CD   OE1  OE2                                  
REMARK 470     GLU A   3    CG   CD   OE1  OE2                                  
REMARK 470     LYS A   4    CG   CD   CE   NZ                                   
REMARK 470     GLN A 139    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 180    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 193    CG   CD   OE1  NE2                                  
REMARK 470     GLN A 194    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 221    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 258    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 273    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 300    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 503    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 519    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 521    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 523    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG C  18    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS C 126    CG   CD   CE   NZ                                   
REMARK 470     LYS C 188    CG   CD   CE   NZ                                   
REMARK 470     ARG C 211    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS D 135    CG   CD   CE   NZ                                   
REMARK 470     LYS D 215    CG   CD   CE   NZ                                   
REMARK 470     ARG D 216    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS D 220    CG   CD   CE   NZ                                   
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    GLU A   3       86.92   -163.04                                   
REMARK 500    LYS A   4      129.28    -35.53                                   
REMARK 500    LYS A  13     -125.00     45.16                                   
REMARK 500    LEU A  80      102.07    -56.57                                   
REMARK 500    ASN A  91     -109.04     38.46                                   
REMARK 500    SER A  92       45.12   -140.94                                   
REMARK 500    SER A  99       54.25     38.71                                   
REMARK 500    LEU A 111       69.58   -118.53                                   
REMARK 500    ALA A 123     -166.30   -100.78                                   
REMARK 500    ASN A 134      -40.02     73.94                                   
REMARK 500    LYS A 188      -73.96   -123.33                                   
REMARK 500    ILE A 189        1.56    -59.94                                   
REMARK 500    SER A 196      -70.63    -67.45                                   
REMARK 500    SER A 205       49.69    -95.28                                   
REMARK 500    ASP A 206       37.21   -158.58                                   
REMARK 500    ASN A 210      -35.25    -36.41                                   
REMARK 500    ALA A 213      -76.64    -96.23                                   
REMARK 500    GLU A 221      -12.98    -44.52                                   
REMARK 500    LYS A 229      -96.27   -116.59                                   
REMARK 500    GLN A 252     -169.83   -160.46                                   
REMARK 500    GLU A 258        6.27    -68.85                                   
REMARK 500    ALA A 265       38.53    -96.47                                   
REMARK 500    ASP A 279       10.74    -62.38                                   
REMARK 500    ASP A 290      -19.02     93.03                                   
REMARK 500    ASP A 297       97.17     54.24                                   
REMARK 500    HIS A 334        3.21    -66.68                                   
REMARK 500    ASN A 337        0.87     81.03                                   
REMARK 500    HIS A 409       28.88     49.82                                   
REMARK 500    TYR A 447      -26.84     84.03                                   
REMARK 500    HIS A 483      151.42    -44.67                                   
REMARK 500    PRO A 488       16.72    -66.18                                   
REMARK 500    ASN A 504      -88.93   -117.44                                   
REMARK 500    ARG A 507     -104.83    -75.33                                   
REMARK 500    LEU A 518       -9.07     90.85                                   
REMARK 500    GLU A 519      143.82   -173.63                                   
REMARK 500    GLU A 521      -82.38    -61.62                                   
REMARK 500    CYS A 547      165.51    179.06                                   
REMARK 500    HIS A 560      -93.79   -136.15                                   
REMARK 500    ASN A 580       52.32     39.69                                   
REMARK 500    ASP A 588     -165.71    -71.50                                   
REMARK 500    ARG A 610       19.15    -66.45                                   
REMARK 500    THR C  40      128.81    -37.31                                   
REMARK 500    ALA C  51      -45.98     68.81                                   
REMARK 500    SER C  67      118.65   -173.95                                   
REMARK 500    SER C  77       85.97     17.97                                   
REMARK 500    GLU C 123      -57.68     80.79                                   
REMARK 500    ASN C 152       13.73     97.79                                   
REMARK 500    ALA C 184      -23.63     81.52                                   
REMARK 500    GLU C 187       47.46     91.47                                   
REMARK 500    LYS C 188      -34.71   -156.41                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      60 RAMACHANDRAN OUTLIERS.                        
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    SER C 171        23.3      L          L   OUTSIDE RANGE           
REMARK 500    SER D  15        24.4      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDG A 625                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDG D 881                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 3281                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 3282                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 3283                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 3284                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 3285                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 3286                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 3287                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 3288                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 3289                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 3371                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 3372                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 3891                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 4201                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 4202                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 5041                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 5441                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 5791                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 5792                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1YY8   RELATED DB: PDB                                   
REMARK 900 FAB FRAGMENT FROM THE MONOCLONAL ANTIBODY CETUXIMAB                  
DBREF  1YY9 A    1   618  UNP    P00533   EGFR_HUMAN      25    642             
DBREF  1YY9 C    1   213  PDB    1YY9     1YY9             1    213             
DBREF  1YY9 D    1   221  PDB    1YY9     1YY9             1    221             
SEQADV 1YY9 LYS A  474  UNP  P00533    SER   498 CONFLICT                       
SEQADV 1YY9 ARG A  610  UNP  P00533    GLU   634 CONFLICT                       
SEQADV 1YY9 HIS A  619  UNP  P00533              EXPRESSION TAG                 
SEQADV 1YY9 HIS A  620  UNP  P00533              EXPRESSION TAG                 
SEQADV 1YY9 HIS A  621  UNP  P00533              EXPRESSION TAG                 
SEQADV 1YY9 HIS A  622  UNP  P00533              EXPRESSION TAG                 
SEQADV 1YY9 HIS A  623  UNP  P00533              EXPRESSION TAG                 
SEQADV 1YY9 HIS A  624  UNP  P00533              EXPRESSION TAG                 
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 LYS 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 ARG GLY          
SEQRES  48 A  624  CYS PRO THR ASN GLY PRO LYS HIS HIS HIS HIS HIS HIS          
SEQRES   1 C  213  ASP ILE LEU LEU THR GLN SER PRO VAL ILE LEU SER VAL          
SEQRES   2 C  213  SER PRO GLY GLU ARG VAL SER PHE SER CYS ARG ALA SER          
SEQRES   3 C  213  GLN SER ILE GLY THR ASN ILE HIS TRP TYR GLN GLN ARG          
SEQRES   4 C  213  THR ASN GLY SER PRO ARG LEU LEU ILE LYS TYR ALA SER          
SEQRES   5 C  213  GLU SER ILE SER GLY ILE PRO SER ARG PHE SER GLY SER          
SEQRES   6 C  213  GLY SER GLY THR ASP PHE THR LEU SER ILE ASN SER VAL          
SEQRES   7 C  213  GLU SER GLU ASP ILE ALA ASP TYR TYR CYS GLN GLN ASN          
SEQRES   8 C  213  ASN ASN TRP PRO THR THR PHE GLY ALA GLY THR LYS LEU          
SEQRES   9 C  213  GLU LEU LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE          
SEQRES  10 C  213  PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA          
SEQRES  11 C  213  SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU          
SEQRES  12 C  213  ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER          
SEQRES  13 C  213  GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS          
SEQRES  14 C  213  ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER          
SEQRES  15 C  213  LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU          
SEQRES  16 C  213  VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER          
SEQRES  17 C  213  PHE ASN ARG GLY ALA                                          
SEQRES   1 D  221  GLN VAL GLN LEU LYS GLN SER GLY PRO GLY LEU VAL GLN          
SEQRES   2 D  221  PRO SER GLN SER LEU SER ILE THR CYS THR VAL SER GLY          
SEQRES   3 D  221  PHE SER LEU THR ASN TYR GLY VAL HIS TRP VAL ARG GLN          
SEQRES   4 D  221  SER PRO GLY LYS GLY LEU GLU TRP LEU GLY VAL ILE TRP          
SEQRES   5 D  221  SER GLY GLY ASN THR ASP TYR ASN THR PRO PHE THR SER          
SEQRES   6 D  221  ARG LEU SER ILE ASN LYS ASP ASN SER LYS SER GLN VAL          
SEQRES   7 D  221  PHE PHE LYS MET ASN SER LEU GLN SER ASN ASP THR ALA          
SEQRES   8 D  221  ILE TYR TYR CYS ALA ARG ALA LEU THR TYR TYR ASP TYR          
SEQRES   9 D  221  GLU PHE ALA TYR TRP GLY GLN GLY THR LEU VAL THR VAL          
SEQRES  10 D  221  SER ALA ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU          
SEQRES  11 D  221  ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA          
SEQRES  12 D  221  LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL          
SEQRES  13 D  221  THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL          
SEQRES  14 D  221  HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR          
SEQRES  15 D  221  SER LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU          
SEQRES  16 D  221  GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO          
SEQRES  17 D  221  SER ASN THR LYS VAL ASP LYS ARG VAL GLU PRO LYS SER          
MODRES 1YY9 ASN A   32  ASN  GLYCOSYLATION SITE                                 
MODRES 1YY9 ASN A  328  ASN  GLYCOSYLATION SITE                                 
MODRES 1YY9 ASN A  337  ASN  GLYCOSYLATION SITE                                 
MODRES 1YY9 ASN A  389  ASN  GLYCOSYLATION SITE                                 
MODRES 1YY9 ASN A  420  ASN  GLYCOSYLATION SITE                                 
MODRES 1YY9 ASN A  504  ASN  GLYCOSYLATION SITE                                 
MODRES 1YY9 ASN A  544  ASN  GLYCOSYLATION SITE                                 
MODRES 1YY9 ASN A  579  ASN  GLYCOSYLATION SITE                                 
MODRES 1YY9 ASN D   88  ASN  GLYCOSYLATION SITE                                 
HET    NDG  A 625      14                                                       
HET    NDG  D 881      14                                                       
HET    NAG  A3281      14                                                       
HET    NAG  A3282      14                                                       
HET    BMA  A3283      11                                                       
HET    MAN  A3284      11                                                       
HET    MAN  A3285      11                                                       
HET    MAN  A3286      11                                                       
HET    MAN  A3287      11                                                       
HET    MAN  A3288      11                                                       
HET    MAN  A3289      11                                                       
HET    NAG  A3371      14                                                       
HET    NAG  A3372      14                                                       
HET    NAG  A3891      14                                                       
HET    NAG  A4201      14                                                       
HET    NAG  A4202      14                                                       
HET    NAG  A5041      14                                                       
HET    NAG  A5441      14                                                       
HET    NAG  A5791      14                                                       
HET    NAG  A5792      14                                                       
HETNAM     NDG 2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE                        
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     BMA BETA-D-MANNOSE                                                   
HETNAM     MAN ALPHA-D-MANNOSE                                                  
FORMUL   4  NDG    2(C8 H15 N O6)                                               
FORMUL   6  NAG    11(C8 H15 N O6)                                              
FORMUL   6  BMA    C6 H12 O6                                                    
FORMUL   6  MAN    6(C6 H12 O6)                                                 
FORMUL  13  HOH   *56(H2 O)                                                     
HELIX    1   1 THR A   19  ASN A   32  1                                  14    
HELIX    2   2 LEU A   52  ILE A   58  5                                   7    
HELIX    3   3 ASN A  134  ILE A  138  5                                   5    
HELIX    4   4 GLN A  139  ILE A  143  5                                   5    
HELIX    5   5 PHE A  148  MET A  152  5                                   5    
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 LEU A  348  GLY A  354  1                                   7    
HELIX   12  12 ASP A  355  HIS A  359  5                                   5    
HELIX   13  13 ASP A  364  VAL A  374  5                                  11    
HELIX   14  14 LEU A  393  GLU A  397  5                                   5    
HELIX   15  15 LYS A  407  GLY A  410  5                                   4    
HELIX   16  16 ASN A  452  LEU A  456  5                                   5    
HELIX   17  17 GLY A  471  THR A  478  1                                   8    
HELIX   18  18 GLU A  495  CYS A  499  5                                   5    
HELIX   19  19 GLY A  577  THR A  581  5                                   5    
HELIX   20  20 GLY A  608  CYS A  612  5                                   5    
HELIX   21  21 THR D   61  THR D   64  5                                   4    
HELIX   22  22 ASN D   73  LYS D   75  5                                   3    
HELIX   23  23 GLN D   86  THR D   90  5                                   5    
HELIX   24  24 SER D  162  ALA D  164  5                                   3    
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 5 LEU A  41  THR A  44  0                                        
SHEET    2   B 5 VAL A  65  ALA A  68  1  O  LEU A  66   N  ILE A  43           
SHEET    3   B 5 TYR A  93  LEU A  98  1  O  ALA A  96   N  ILE A  67           
SHEET    4   B 5 ALA A 123  SER A 127  1  O  ARG A 125   N  VAL A  97           
SHEET    5   B 5 SER A 153  MET A 154  1  O  SER A 153   N  VAL A 124           
SHEET    1   C 2 PHE A 230  ARG A 231  0                                        
SHEET    2   C 2 CYS A 236  LYS A 237 -1  O  LYS A 237   N  PHE A 230           
SHEET    1   D 2 MET A 244  ASN A 247  0                                        
SHEET    2   D 2 GLN A 252  VAL A 255 -1  O  GLN A 252   N  ASN A 247           
SHEET    1   E 2 TYR A 261  PHE A 263  0                                        
SHEET    2   E 2 THR A 266  VAL A 268 -1  O  THR A 266   N  PHE A 263           
SHEET    1   F 2 VAL A 276  VAL A 277  0                                        
SHEET    2   F 2 CYS A 283  VAL A 284 -1  O  VAL A 284   N  VAL A 276           
SHEET    1   G 2 SER A 291  GLU A 295  0                                        
SHEET    2   G 2 ARG A 300  LYS A 304 -1  O  LYS A 303   N  TYR A 292           
SHEET    1   H 5 VAL A 312  ASN A 314  0                                        
SHEET    2   H 5 SER A 340  SER A 342  1  O  SER A 342   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  ALA A 415   N  ILE A 383           
SHEET    4   I 5 ASP A 436  SER A 440  1  O  ILE A 438   N  VAL A 416           
SHEET    5   I 5 THR A 464  ILE A 467  1  O  LYS A 465   N  ILE A 439           
SHEET    1   J 2 VAL A 505  SER A 506  0                                        
SHEET    2   J 2 CYS A 511  VAL A 512 -1  O  VAL A 512   N  VAL A 505           
SHEET    1   K 2 GLU A 524  GLU A 527  0                                        
SHEET    2   K 2 GLU A 530  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  HIS A 566   N  ASP A 563           
SHEET    1   M 3 ALA A 573  VAL A 575  0                                        
SHEET    2   M 3 VAL A 583  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 4 LEU C   4  SER C   7  0                                        
SHEET    2   N 4 VAL C  19  ALA C  25 -1  O  ARG C  24   N  THR C   5           
SHEET    3   N 4 ASP C  70  ILE C  75 -1  O  LEU C  73   N  PHE C  21           
SHEET    4   N 4 PHE C  62  GLY C  66 -1  N  SER C  63   O  SER C  74           
SHEET    1   O 6 ILE C  10  VAL C  13  0                                        
SHEET    2   O 6 THR C 102  LEU C 106  1  O  GLU C 105   N  LEU C  11           
SHEET    3   O 6 ASP C  85  GLN C  90 -1  N  TYR C  86   O  THR C 102           
SHEET    4   O 6 ILE C  33  GLN C  38 -1  N  GLN C  38   O  ASP C  85           
SHEET    5   O 6 ARG C  45  LYS C  49 -1  O  LEU C  47   N  TRP C  35           
SHEET    6   O 6 GLU C  53  SER C  54 -1  O  GLU C  53   N  LYS C  49           
SHEET    1   P 4 ILE C  10  VAL C  13  0                                        
SHEET    2   P 4 THR C 102  LEU C 106  1  O  GLU C 105   N  LEU C  11           
SHEET    3   P 4 ASP C  85  GLN C  90 -1  N  TYR C  86   O  THR C 102           
SHEET    4   P 4 THR C  97  PHE C  98 -1  O  THR C  97   N  GLN C  90           
SHEET    1   Q 4 SER C 114  PHE C 118  0                                        
SHEET    2   Q 4 THR C 129  PHE C 139 -1  O  ASN C 137   N  SER C 114           
SHEET    3   Q 4 TYR C 173  SER C 182 -1  O  LEU C 179   N  VAL C 132           
SHEET    4   Q 4 SER C 159  VAL C 163 -1  N  GLN C 160   O  THR C 178           
SHEET    1   R 4 ALA C 153  LEU C 154  0                                        
SHEET    2   R 4 LYS C 145  VAL C 150 -1  N  VAL C 150   O  ALA C 153           
SHEET    3   R 4 TYR C 192  THR C 197 -1  O  ALA C 193   N  LYS C 149           
SHEET    4   R 4 VAL C 205  LYS C 207 -1  O  LYS C 207   N  CYS C 194           
SHEET    1   S 4 GLN D   3  SER D   7  0                                        
SHEET    2   S 4 LEU D  18  SER D  25 -1  O  THR D  21   N  SER D   7           
SHEET    3   S 4 GLN D  77  MET D  82 -1  O  VAL D  78   N  CYS D  22           
SHEET    4   S 4 LEU D  67  ASP D  72 -1  N  SER D  68   O  LYS D  81           
SHEET    1   T 6 LEU D  11  VAL D  12  0                                        
SHEET    2   T 6 THR D 113  VAL D 117  1  O  THR D 116   N  VAL D  12           
SHEET    3   T 6 ALA D  91  ALA D  98 -1  N  ALA D  91   O  VAL D 115           
SHEET    4   T 6 VAL D  34  SER D  40 -1  N  VAL D  37   O  TYR D  94           
SHEET    5   T 6 GLY D  44  ILE D  51 -1  O  GLU D  46   N  ARG D  38           
SHEET    6   T 6 THR D  57  TYR D  59 -1  O  ASP D  58   N  VAL D  50           
SHEET    1   U 4 LEU D  11  VAL D  12  0                                        
SHEET    2   U 4 THR D 113  VAL D 117  1  O  THR D 116   N  VAL D  12           
SHEET    3   U 4 ALA D  91  ALA D  98 -1  N  ALA D  91   O  VAL D 115           
SHEET    4   U 4 PHE D 106  TRP D 109 -1  O  TYR D 108   N  ARG D  97           
SHEET    1   V 4 SER D 126  LEU D 130  0                                        
SHEET    2   V 4 ALA D 142  TYR D 151 -1  O  LEU D 147   N  PHE D 128           
SHEET    3   V 4 TYR D 182  VAL D 190 -1  O  TYR D 182   N  TYR D 151           
SHEET    4   V 4 VAL D 169  THR D 171 -1  N  HIS D 170   O  VAL D 187           
SHEET    1   W 4 SER D 126  LEU D 130  0                                        
SHEET    2   W 4 ALA D 142  TYR D 151 -1  O  LEU D 147   N  PHE D 128           
SHEET    3   W 4 TYR D 182  VAL D 190 -1  O  TYR D 182   N  TYR D 151           
SHEET    4   W 4 VAL D 175  LEU D 176 -1  N  VAL D 175   O  SER D 183           
SHEET    1   X 3 THR D 157  TRP D 160  0                                        
SHEET    2   X 3 ILE D 201  HIS D 206 -1  O  ASN D 205   N  THR D 157           
SHEET    3   X 3 THR D 211  ARG D 216 -1  O  LYS D 215   N  CYS D 202           
SSBOND   1 CYS A    7    CYS A   34                          1555   1555  2.10  
SSBOND   2 CYS A  133    CYS A  163                          1555   1555  2.06  
SSBOND   3 CYS A  166    CYS A  175                          1555   1555  2.05  
SSBOND   4 CYS A  170    CYS A  183                          1555   1555  2.09  
SSBOND   5 CYS A  191    CYS A  199                          1555   1555  1.97  
SSBOND   6 CYS A  195    CYS A  207                          1555   1555  2.04  
SSBOND   7 CYS A  208    CYS A  216                          1555   1555  2.05  
SSBOND   8 CYS A  212    CYS A  224                          1555   1555  2.05  
SSBOND   9 CYS A  227    CYS A  236                          1555   1555  2.04  
SSBOND  10 CYS A  240    CYS A  267                          1555   1555  2.04  
SSBOND  11 CYS A  271    CYS A  283                          1555   1555  2.08  
SSBOND  12 CYS A  287    CYS A  302                          1555   1555  2.05  
SSBOND  13 CYS A  305    CYS A  309                          1555   1555  2.09  
SSBOND  14 CYS A  313    CYS A  338                          1555   1555  2.03  
SSBOND  15 CYS A  446    CYS A  475                          1555   1555  2.07  
SSBOND  16 CYS A  482    CYS A  491                          1555   1555  2.04  
SSBOND  17 CYS A  486    CYS A  499                          1555   1555  2.03  
SSBOND  18 CYS A  502    CYS A  511                          1555   1555  2.04  
SSBOND  19 CYS A  515    CYS A  531                          1555   1555  2.08  
SSBOND  20 CYS A  534    CYS A  547                          1555   1555  2.06  
SSBOND  21 CYS A  538    CYS A  555                          1555   1555  2.04  
SSBOND  22 CYS A  558    CYS A  567                          1555   1555  2.03  
SSBOND  23 CYS A  571    CYS A  593                          1555   1555  2.05  
SSBOND  24 CYS A  596    CYS A  604                          1555   1555  2.04  
SSBOND  25 CYS A  600    CYS A  612                          1555   1555  2.05  
SSBOND  26 CYS C   23    CYS C   88                          1555   1555  2.08  
SSBOND  27 CYS C  134    CYS C  194                          1555   1555  2.03  
SSBOND  28 CYS D   22    CYS D   95                          1555   1555  2.16  
SSBOND  29 CYS D  146    CYS D  202                          1555   1555  2.04  
LINK         ND2 ASN A  32                 C1  NDG A 625     1555   1555  1.46  
LINK         ND2 ASN A 328                 C1  NAG A3281     1555   1555  1.45  
LINK         ND2 ASN A 337                 C1  NAG A3371     1555   1555  1.45  
LINK         ND2 ASN A 389                 C1  NAG A3891     1555   1555  1.44  
LINK         ND2 ASN A 420                 C1  NAG A4201     1555   1555  1.44  
LINK         ND2 ASN A 504                 C1  NAG A5041     1555   1555  1.45  
LINK         ND2 ASN A 544                 C1  NAG A5441     1555   1555  1.41  
LINK         ND2 ASN A 579                 C1  NAG A5791     1555   1555  1.45  
LINK         ND2 ASN D  88                 C1  NDG D 881     1555   1555  1.45  
LINK         O4  NAG A3281                 C1  NAG A3282     1555   1555  1.44  
LINK         O4  NAG A3282                 C1  BMA A3283     1555   1555  1.44  
LINK         O3  BMA A3283                 C1  MAN A3285     1555   1555  1.43  
LINK         O6  BMA A3283                 C1  MAN A3284     1555   1555  1.45  
LINK         O3  MAN A3284                 C1  MAN A3289     1555   1555  1.43  
LINK         O6  MAN A3284                 C1  MAN A3287     1555   1555  1.43  
LINK         O3  MAN A3285                 C1  MAN A3286     1555   1555  1.44  
LINK         O2  MAN A3287                 C1  MAN A3288     1555   1555  1.44  
LINK         O4  NAG A3371                 C1  NAG A3372     1555   1555  1.45  
LINK         O4  NAG A4201                 C1  NAG A4202     1555   1555  1.45  
LINK         O4  NAG A5791                 C1  NAG A5792     1555   1555  1.43  
CISPEP   1 SER C    7    PRO C    8          0        -5.79                     
CISPEP   2 TRP C   94    PRO C   95          0        -2.70                     
CISPEP   3 TYR C  140    PRO C  141          0        -1.60                     
CISPEP   4 PHE D  152    PRO D  153          0        -6.37                     
CISPEP   5 GLU D  154    PRO D  155          0        -5.09                     
SITE     1 AC1  2 ASN A  32  ASN A  33                                          
SITE     1 AC2  1 ASN D  88                                                     
SITE     1 AC3  9 SER A 324  LEU A 325  SER A 326  ASN A 328                    
SITE     2 AC3  9 ASN A 331  ASP A 355  THR A 358  THR A 360                    
SITE     3 AC3  9 NAG A3282                                                     
SITE     1 AC4  3 ASP A 323  NAG A3281  BMA A3283                               
SITE     1 AC5  4 ASP A 323  NAG A3282  MAN A3284  MAN A3285                    
SITE     1 AC6  3 BMA A3283  MAN A3287  MAN A3289                               
SITE     1 AC7  2 BMA A3283  MAN A3286                                          
SITE     1 AC8  1 MAN A3285                                                     
SITE     1 AC9  2 MAN A3284  MAN A3288                                          
SITE     1 BC1  1 MAN A3287                                                     
SITE     1 BC2  1 MAN A3284                                                     
SITE     1 BC3  4 LYS A 311  LYS A 336  ASN A 337  NAG A3372                    
SITE     1 BC4  1 NAG A3371                                                     
SITE     1 BC5  2 ASN A 389  HOH A5795                                          
SITE     1 BC6  5 GLU A 388  ASN A 420  THR A 422  ASN A 444                    
SITE     2 BC6  5 NAG A4202                                                     
SITE     1 BC7  2 NAG A4201  HOH A5816                                          
SITE     1 BC8  5 ALA A 484  ARG A 503  ASN A 504  ASP A 513                    
SITE     2 BC8  5 HOH A5805                                                     
SITE     1 BC9  1 ASN A 544                                                     
SITE     1 CC1  4 ASN A 579  ASN A 580  THR A 581  NAG A5792                    
SITE     1 CC2  2 NAG A5791  HOH A5817                                          
CRYST1   77.823   70.861  147.122  90.00 102.48  90.00 P 1 21 1      2          
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      0.012850  0.000000  0.002844        0.00000                         
SCALE2      0.000000  0.014112  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006962        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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