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Database: PDB
Entry: 4UIP
LinkDB: 4UIP
Original site: 4UIP 
HEADER    TRANSFERASE                             31-MAR-15   4UIP              
TITLE     THE COMPLEX STRUCTURE OF EXTRACELLULAR DOMAIN OF EGFR WITH REPEBODY   
TITLE    2 (RAC1).                                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: EPIDERMAL GROWTH FACTOR RECEPTOR;                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 26-637;                                           
COMPND   5 SYNONYM: PROTO-ONCOGENE C-ERBB-1, RECEPTOR TYROSINE-PROTEIN KINASE E 
COMPND   6 RBB-1;                                                               
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: REPEBODY (RAC1);                                           
COMPND  10 CHAIN: B;                                                            
COMPND  11 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 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: LISTERIA MONOCYTOGENES, SYNTHETIC CONSTRUCT,    
SOURCE  10 EPTATRETUS BURGERI;                                                  
SOURCE  11 ORGANISM_TAXID: 1639, 32630, 7764;                                   
SOURCE  12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  13 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    TRANSFERASE                                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.J.KANG,Y.J.CHA,H.S.CHO,J.J.LEE,H.S.KIM                              
REVDAT   3   15-MAR-17 4UIP    1       SOURCE                                   
REVDAT   2   23-DEC-15 4UIP    1       TITLE  COMPND                            
REVDAT   1   25-NOV-15 4UIP    0                                                
JRNL        AUTH   J.LEE,H.CHOI,M.YUN,Y.KANG,J.JUNG,Y.RYU,T.Y.KIM,Y.CHA,H.CHO,  
JRNL        AUTH 2 J.MIN,C.CHUNG,H.KIM                                          
JRNL        TITL   ENZYMATIC PRENYLATION AND OXIME LIGATION FOR THE SYNTHESIS   
JRNL        TITL 2 OF STABLE AND HOMOGENEOUS PROTEIN-DRUG CONJUGATES FOR        
JRNL        TITL 3 TARGETED THERAPY.                                            
JRNL        REF    ANGEW.CHEM.INT.ED.ENGL.       V.  54 12020 2015              
JRNL        REFN                   ISSN 1433-7851                               
JRNL        PMID   26315561                                                     
JRNL        DOI    10.1002/ANIE.201505964                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.95 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
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) : 2.95                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 53.28                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 23060                          
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) : 0.240                           
REMARK   3   R VALUE            (WORKING SET) : 0.237                           
REMARK   3   FREE R VALUE                     : 0.297                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1238                            
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) : 2.95                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.03                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1522                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.94                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3330                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 74                           
REMARK   3   BIN FREE R VALUE                    : 0.3540                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6583                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 56                                      
REMARK   3   SOLVENT ATOMS            : 41                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 43.40                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.02000                                              
REMARK   3    B22 (A**2) : -0.20000                                             
REMARK   3    B33 (A**2) : 0.17000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.481         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.362         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 19.592        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.892                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.827                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6792 ; 0.013 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  9221 ; 1.853 ; 1.970       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   848 ; 7.743 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   306 ;41.193 ;25.163       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1171 ;17.157 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    35 ;19.464 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1030 ; 0.109 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5118 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN    
REMARK   3  THE INPUT U VALUES REFINED INDIVIDUALLY                             
REMARK   4                                                                      
REMARK   4 4UIP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 31-MAR-15.                  
REMARK 100 THE PDBE ID CODE IS EBI-63515.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 93.15                              
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : BL-1A                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 23060                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.950                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 3.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 2.000                              
REMARK 200  R MERGE                    (I) : 0.17000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: PDB ENTRY 4J4L                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.30                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.88                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 2 21 21                        
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,Y+1/2,-Z+1/2                                         
REMARK 290       4555   -X,-Y+1/2,Z+1/2                                         
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        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       44.17000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       94.60500            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       44.17000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       94.60500            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
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     HIS A   614                                                      
REMARK 465     HIS A   615                                                      
REMARK 465     HIS A   616                                                      
REMARK 465     HIS A   617                                                      
REMARK 465     HIS A   618                                                      
REMARK 465     HIS A   619                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLU B     2                                                      
REMARK 465     THR B     3                                                      
REMARK 465     ILE B     4                                                      
REMARK 465     THR B     5                                                      
REMARK 465     LEU B   244                                                      
REMARK 465     GLU B   245                                                      
REMARK 465     HIS B   246                                                      
REMARK 465     HIS B   247                                                      
REMARK 465     HIS B   248                                                      
REMARK 465     HIS B   249                                                      
REMARK 465     HIS B   250                                                      
REMARK 465     HIS B   251                                                      
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   SG   CYS A   600     SG   CYS A   612              0.72            
REMARK 500   SG   CYS A   558     SG   CYS A   567              1.00            
REMARK 500   SG   CYS B   198     SG   CYS B   241              1.05            
REMARK 500   O    VAL A   505     O    CYS A   511              1.16            
REMARK 500   SG   CYS A   287     SG   CYS A   302              1.26            
REMARK 500   O    PRO A   130     ND2  ASN A   158              1.29            
REMARK 500   OE1  GLU A   296     NZ   LYS A   303              1.33            
REMARK 500   CB   CYS A   534     SG   CYS A   547              1.67            
REMARK 500   CB   CYS A   600     SG   CYS A   612              1.67            
REMARK 500   O    PRO A   607     O    GLY A   608              1.79            
REMARK 500   O    CYS A   486     NH2  ARG A   503              1.81            
REMARK 500   NH2  ARG A   523     O    GLN A   541              1.88            
REMARK 500   OE1  GLU A   489     OG   SER A   501              1.91            
REMARK 500   OE1  GLU A   293     O    HOH A  2013              2.06            
REMARK 500   O    SER B   118     O    ALA B   142              2.08            
REMARK 500   C    VAL A   505     O    CYS A   511              2.11            
REMARK 500   NH2  ARG B    67     O    HOH B  2002              2.12            
REMARK 500   NE2  GLN B    97     O    HOH B  2003              2.14            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    GLU A   3   N   -  CA  -  C   ANGL. DEV. = -16.3 DEGREES          
REMARK 500    CYS A 502   CB  -  CA  -  C   ANGL. DEV. =   8.8 DEGREES          
REMARK 500    CYS A 515   CA  -  CB  -  SG  ANGL. DEV. =   7.2 DEGREES          
REMARK 500    LEU A 517   N   -  CA  -  C   ANGL. DEV. =  16.8 DEGREES          
REMARK 500    CYS A 547   CA  -  CB  -  SG  ANGL. DEV. =  11.3 DEGREES          
REMARK 500    CYS A 571   CA  -  CB  -  SG  ANGL. DEV. = -11.6 DEGREES          
REMARK 500    CYS A 596   CA  -  CB  -  SG  ANGL. DEV. = -11.9 DEGREES          
REMARK 500    CYS A 612   CA  -  CB  -  SG  ANGL. DEV. =   9.1 DEGREES          
REMARK 500    ARG B 164   NE  -  CZ  -  NH2 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    PRO B 199   C   -  N   -  CD  ANGL. DEV. =  18.4 DEGREES          
REMARK 500    PRO B 242   C   -  N   -  CD  ANGL. DEV. =  14.1 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    SER A  11       50.99   -149.77                                   
REMARK 500    LYS A  13     -120.46     59.15                                   
REMARK 500    LEU A  52       41.27    -95.24                                   
REMARK 500    ASN A 134      -15.81     82.86                                   
REMARK 500    SER A 153       76.61   -119.87                                   
REMARK 500    ASP A 167      121.64    -34.18                                   
REMARK 500    THR A 187       11.56   -143.50                                   
REMARK 500    LYS A 188      -52.59   -128.81                                   
REMARK 500    LYS A 229      -81.56    -97.92                                   
REMARK 500    TYR A 251      -14.13     73.17                                   
REMARK 500    ALA A 289       -8.61    -57.53                                   
REMARK 500    GLU A 306      -23.33     90.51                                   
REMARK 500    ILE A 327      108.45    -57.52                                   
REMARK 500    GLN A 411      -52.41   -123.22                                   
REMARK 500    TYR A 447      -13.17     89.92                                   
REMARK 500    PRO A 488       10.29    -64.56                                   
REMARK 500    ASN A 504      -85.29   -106.57                                   
REMARK 500    ARG A 507      -74.54    -92.07                                   
REMARK 500    CYS A 511      -67.54   -102.26                                   
REMARK 500    VAL A 512     -126.60   -127.17                                   
REMARK 500    ASN A 516       85.08    -66.95                                   
REMARK 500    ASN A 544     -168.58   -125.37                                   
REMARK 500    ASN A 554       32.33    -94.80                                   
REMARK 500    HIS A 560      -90.24   -119.73                                   
REMARK 500    ASN B  74     -164.88   -108.06                                   
REMARK 500    ASN B  96     -153.03   -115.27                                   
REMARK 500    GLU B 119       34.02   -147.68                                   
REMARK 500    GLN B 121       62.12   -109.30                                   
REMARK 500    LEU B 133       54.93    -99.82                                   
REMARK 500    ASN B 144     -159.52   -106.07                                   
REMARK 500    ASN B 168     -161.91   -121.40                                   
REMARK 500    ALA B 223       78.24   -158.67                                   
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 ASN A  274     TYR A  275                 -145.74                    
REMARK 500 ASP A  290     SER A  291                 -149.64                    
REMARK 500 VAL A  512     ASP A  513                  -36.72                    
REMARK 500 GLU A  521     PRO A  522                  142.02                    
REMARK 500 LEU A  609     GLU A  610                   42.08                    
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 Poly-Saccharide residues NAG      
REMARK 800  A1616 through NAG A1617 bound to ASN A 328                          
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: Binding site for Mono-Saccharide NAG A1614 bound   
REMARK 800  to ASN A 420                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: Binding site for Mono-Saccharide NAG A1615 bound   
REMARK 800  to ASN A 504                                                        
DBREF  4UIP A    2   613  UNP    P00533   EGFR_HUMAN      26    637             
DBREF  4UIP B    2    66  UNP    E0ACT6   E0ACT6_LISMN    33     97             
DBREF  4UIP B   67   151  PDB    4UIP     4UIP            67    151             
DBREF  4UIP B  152   243  UNP    Q4G1L3   Q4G1L3_EPTBU   141    232             
SEQADV 4UIP HIS A  614  UNP  P00533              EXPRESSION TAG                 
SEQADV 4UIP HIS A  615  UNP  P00533              EXPRESSION TAG                 
SEQADV 4UIP HIS A  616  UNP  P00533              EXPRESSION TAG                 
SEQADV 4UIP HIS A  617  UNP  P00533              EXPRESSION TAG                 
SEQADV 4UIP HIS A  618  UNP  P00533              EXPRESSION TAG                 
SEQADV 4UIP HIS A  619  UNP  P00533              EXPRESSION TAG                 
SEQADV 4UIP MET B    1  UNP  E0ACT6              EXPRESSION TAG                 
SEQADV 4UIP ALA B   25  UNP  E0ACT6    ASP    56 CONFLICT                       
SEQADV 4UIP LEU B  244  UNP  Q4G1L3              EXPRESSION TAG                 
SEQADV 4UIP GLU B  245  UNP  Q4G1L3              EXPRESSION TAG                 
SEQADV 4UIP HIS B  246  UNP  Q4G1L3              EXPRESSION TAG                 
SEQADV 4UIP HIS B  247  UNP  Q4G1L3              EXPRESSION TAG                 
SEQADV 4UIP HIS B  248  UNP  Q4G1L3              EXPRESSION TAG                 
SEQADV 4UIP HIS B  249  UNP  Q4G1L3              EXPRESSION TAG                 
SEQADV 4UIP HIS B  250  UNP  Q4G1L3              EXPRESSION TAG                 
SEQADV 4UIP HIS B  251  UNP  Q4G1L3              EXPRESSION TAG                 
SEQRES   1 A  618  GLU GLU LYS LYS VAL CYS GLN GLY THR SER ASN LYS LEU          
SEQRES   2 A  618  THR GLN LEU GLY THR PHE GLU ASP HIS PHE LEU SER LEU          
SEQRES   3 A  618  GLN ARG MET PHE ASN ASN CYS GLU VAL VAL LEU GLY ASN          
SEQRES   4 A  618  LEU GLU ILE THR TYR VAL GLN ARG ASN TYR ASP LEU SER          
SEQRES   5 A  618  PHE LEU LYS THR ILE GLN GLU VAL ALA GLY TYR VAL LEU          
SEQRES   6 A  618  ILE ALA LEU ASN THR VAL GLU ARG ILE PRO LEU GLU ASN          
SEQRES   7 A  618  LEU GLN ILE ILE ARG GLY ASN MET TYR TYR GLU ASN SER          
SEQRES   8 A  618  TYR ALA LEU ALA VAL LEU SER ASN TYR ASP ALA ASN LYS          
SEQRES   9 A  618  THR GLY LEU LYS GLU LEU PRO MET ARG ASN LEU GLN GLU          
SEQRES  10 A  618  ILE LEU HIS GLY ALA VAL ARG PHE SER ASN ASN PRO ALA          
SEQRES  11 A  618  LEU CYS ASN VAL GLU SER ILE GLN TRP ARG ASP ILE VAL          
SEQRES  12 A  618  SER SER ASP PHE LEU SER ASN MET SER MET ASP PHE GLN          
SEQRES  13 A  618  ASN HIS LEU GLY SER CYS GLN LYS CYS ASP PRO SER CYS          
SEQRES  14 A  618  PRO ASN GLY SER CYS TRP GLY ALA GLY GLU GLU ASN CYS          
SEQRES  15 A  618  GLN LYS LEU THR LYS ILE ILE CYS ALA GLN GLN CYS SER          
SEQRES  16 A  618  GLY ARG CYS ARG GLY LYS SER PRO SER ASP CYS CYS HIS          
SEQRES  17 A  618  ASN GLN CYS ALA ALA GLY CYS THR GLY PRO ARG GLU SER          
SEQRES  18 A  618  ASP CYS LEU VAL CYS ARG LYS PHE ARG ASP GLU ALA THR          
SEQRES  19 A  618  CYS LYS ASP THR CYS PRO PRO LEU MET LEU TYR ASN PRO          
SEQRES  20 A  618  THR THR TYR GLN MET ASP VAL ASN PRO GLU GLY LYS TYR          
SEQRES  21 A  618  SER PHE GLY ALA THR CYS VAL LYS LYS CYS PRO ARG ASN          
SEQRES  22 A  618  TYR VAL VAL THR ASP HIS GLY SER CYS VAL ARG ALA CYS          
SEQRES  23 A  618  GLY ALA ASP SER TYR GLU MET GLU GLU ASP GLY VAL ARG          
SEQRES  24 A  618  LYS CYS LYS LYS CYS GLU GLY PRO CYS ARG LYS VAL CYS          
SEQRES  25 A  618  ASN GLY ILE GLY ILE GLY GLU PHE LYS ASP SER LEU SER          
SEQRES  26 A  618  ILE ASN ALA THR ASN ILE LYS HIS PHE LYS ASN CYS THR          
SEQRES  27 A  618  SER ILE SER GLY ASP LEU HIS ILE LEU PRO VAL ALA PHE          
SEQRES  28 A  618  ARG GLY ASP SER PHE THR HIS THR PRO PRO LEU ASP PRO          
SEQRES  29 A  618  GLN GLU LEU ASP ILE LEU LYS THR VAL LYS GLU ILE THR          
SEQRES  30 A  618  GLY PHE LEU LEU ILE GLN ALA TRP PRO GLU ASN ARG THR          
SEQRES  31 A  618  ASP LEU HIS ALA PHE GLU ASN LEU GLU ILE ILE ARG GLY          
SEQRES  32 A  618  ARG THR LYS GLN HIS GLY GLN PHE SER LEU ALA VAL VAL          
SEQRES  33 A  618  SER LEU ASN ILE THR SER LEU GLY LEU ARG SER LEU LYS          
SEQRES  34 A  618  GLU ILE SER ASP GLY ASP VAL ILE ILE SER GLY ASN LYS          
SEQRES  35 A  618  ASN LEU CYS TYR ALA ASN THR ILE ASN TRP LYS LYS LEU          
SEQRES  36 A  618  PHE GLY THR SER GLY GLN LYS THR LYS ILE ILE SER ASN          
SEQRES  37 A  618  ARG GLY GLU ASN SER CYS LYS ALA THR GLY GLN VAL CYS          
SEQRES  38 A  618  HIS ALA LEU CYS SER PRO GLU GLY CYS TRP GLY PRO GLU          
SEQRES  39 A  618  PRO ARG ASP CYS VAL SER CYS ARG ASN VAL SER ARG GLY          
SEQRES  40 A  618  ARG GLU CYS VAL ASP LYS CYS ASN LEU LEU GLU GLY GLU          
SEQRES  41 A  618  PRO ARG GLU PHE VAL GLU ASN SER GLU CYS ILE GLN CYS          
SEQRES  42 A  618  HIS PRO GLU CYS LEU PRO GLN ALA MET ASN ILE THR CYS          
SEQRES  43 A  618  THR GLY ARG GLY PRO ASP ASN CYS ILE GLN CYS ALA HIS          
SEQRES  44 A  618  TYR ILE ASP GLY PRO HIS CYS VAL LYS THR CYS PRO ALA          
SEQRES  45 A  618  GLY VAL MET GLY GLU ASN ASN THR LEU VAL TRP LYS TYR          
SEQRES  46 A  618  ALA ASP ALA GLY HIS VAL CYS HIS LEU CYS HIS PRO ASN          
SEQRES  47 A  618  CYS THR TYR GLY CYS THR GLY PRO GLY LEU GLU GLY CYS          
SEQRES  48 A  618  PRO HIS HIS HIS HIS HIS HIS                                  
SEQRES   1 B  251  MET GLU THR ILE THR VAL SER THR PRO ILE LYS GLN ILE          
SEQRES   2 B  251  PHE PRO ASP ASP ALA PHE ALA GLU THR ILE LYS ALA ASN          
SEQRES   3 B  251  LEU LYS LYS LYS SER VAL THR ASP ALA VAL THR GLN ASN          
SEQRES   4 B  251  GLU LEU ASN SER ILE ASP GLN ILE ILE ALA ASN ASN SER          
SEQRES   5 B  251  ASP ILE LYS SER VAL GLN GLY ILE GLN TYR LEU PRO ASN          
SEQRES   6 B  251  VAL ARG TYR LEU ALA LEU GLY GLY ASN LYS LEU HIS ASP          
SEQRES   7 B  251  ILE SER ALA LEU LYS GLU LEU THR ASN LEU THR TYR LEU          
SEQRES   8 B  251  MET LEU HIS TYR ASN GLN LEU GLN ILE LEU PRO ASN GLY          
SEQRES   9 B  251  VAL PHE ASP LYS LEU THR ASN LEU LYS GLU LEU TYR LEU          
SEQRES  10 B  251  SER GLU ASN GLN LEU GLN SER LEU PRO ASP GLY VAL PHE          
SEQRES  11 B  251  ASP LYS LEU THR ASN LEU THR GLU LEU ASP LEU ALA ARG          
SEQRES  12 B  251  ASN GLN LEU GLN SER LEU PRO LYS GLY VAL PHE ASP LYS          
SEQRES  13 B  251  LEU THR GLN LEU LYS ASP LEU ARG LEU TYR GLN ASN GLN          
SEQRES  14 B  251  LEU LYS SER VAL PRO ASP GLY VAL PHE ASP ARG LEU THR          
SEQRES  15 B  251  SER LEU GLN TYR ILE TRP LEU HIS ASP ASN PRO TRP ASP          
SEQRES  16 B  251  CYS THR CYS PRO GLY ILE ARG TYR LEU SER GLU TRP ILE          
SEQRES  17 B  251  ASN LYS HIS SER GLY VAL VAL ARG ASN SER ALA GLY SER          
SEQRES  18 B  251  VAL ALA PRO ASP SER ALA LYS CYS SER GLY SER GLY LYS          
SEQRES  19 B  251  PRO VAL ARG SER ILE ILE CYS PRO THR LEU GLU HIS HIS          
SEQRES  20 B  251  HIS HIS HIS HIS                                              
MODRES 4UIP ASN A  328  ASN  GLYCOSYLATION SITE                                 
MODRES 4UIP ASN A  420  ASN  GLYCOSYLATION SITE                                 
MODRES 4UIP ASN A  504  ASN  GLYCOSYLATION SITE                                 
HET    NAG  A1614      14                                                       
HET    NAG  A1615      14                                                       
HET    NAG  A1616      14                                                       
HET    NAG  A1617      14                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
FORMUL   3  NAG    4(C8 H15 N O6)                                               
FORMUL   6  HOH   *41(H2 O)                                                     
HELIX    1   1 THR A   19  PHE A   31  1                                  13    
HELIX    2   2 LEU A   52  ILE A   58  5                                   7    
HELIX    3   3 PHE A  148  MET A  152  5                                   5    
HELIX    4   4 CYS A  170  SER A  174  5                                   5    
HELIX    5   5 GLY A  179  ASN A  182  5                                   4    
HELIX    6   6 ILE A  318  LYS A  322  5                                   5    
HELIX    7   7 ILE A  332  LYS A  336  5                                   5    
HELIX    8   8 PRO A  349  GLY A  354  1                                   6    
HELIX    9   9 ASP A  364  VAL A  374  5                                  11    
HELIX   10  10 TYR A  447  ILE A  451  5                                   5    
HELIX   11  11 ASN A  452  LEU A  456  5                                   5    
HELIX   12  12 GLY A  471  THR A  478  1                                   8    
HELIX   13  13 GLU A  578  ASN A  580  5                                   3    
HELIX   14  14 ILE B   10  PHE B   14  1                                   5    
HELIX   15  15 ASP B   16  LEU B   27  1                                  12    
HELIX   16  16 THR B   37  ASN B   42  1                                   6    
HELIX   17  17 GLY B   59  LEU B   63  5                                   5    
HELIX   18  18 ILE B   79  LYS B   83  5                                   5    
HELIX   19  19 ILE B  201  HIS B  211  1                                  11    
HELIX   20  20 ALA B  223  ALA B  227  5                                   5    
HELIX   21  21 VAL B  236  ILE B  239  5                                   4    
SHEET    1  AA 5 VAL A   6  CYS A   7  0                                        
SHEET    2  AA 5 VAL A  36  VAL A  37  1  O  VAL A  36   N  CYS A   7           
SHEET    3  AA 5 GLU A  60  VAL A  61  1  O  GLU A  60   N  VAL A  37           
SHEET    4  AA 5 ILE A  82  ILE A  83  1  O  ILE A  82   N  VAL A  61           
SHEET    5  AA 5 GLU A 118  ILE A 119  1  O  GLU A 118   N  ILE A  83           
SHEET    1  AB 5 LEU A  41  THR A  44  0                                        
SHEET    2  AB 5 VAL A  65  ALA A  68  1  O  LEU A  66   N  ILE A  43           
SHEET    3  AB 5 TYR A  93  LEU A  98  1  O  ALA A  94   N  VAL A  65           
SHEET    4  AB 5 ALA A 123  SER A 127  1  O  ALA A 123   N  ALA A  94           
SHEET    5  AB 5 SER A 153  MET A 154  1  O  SER A 153   N  PHE A 126           
SHEET    1  AC 2 PHE A 230  ARG A 231  0                                        
SHEET    2  AC 2 CYS A 236  LYS A 237 -1  O  LYS A 237   N  PHE A 230           
SHEET    1  AD 2 MET A 244  TYR A 246  0                                        
SHEET    2  AD 2 MET A 253  VAL A 255 -1  O  ASP A 254   N  LEU A 245           
SHEET    1  AE 2 TYR A 261  PHE A 263  0                                        
SHEET    2  AE 2 THR A 266  VAL A 268 -1  O  THR A 266   N  PHE A 263           
SHEET    1  AF 2 VAL A 276  VAL A 277  0                                        
SHEET    2  AF 2 CYS A 283  VAL A 284 -1  O  VAL A 284   N  VAL A 276           
SHEET    1  AG 2 SER A 291  GLU A 296  0                                        
SHEET    2  AG 2 VAL A 299  LYS A 304 -1  O  VAL A 299   N  GLU A 296           
SHEET    1  AH 5 VAL A 312  ASN A 314  0                                        
SHEET    2  AH 5 SER A 340  SER A 342  1  O  SER A 340   N  CYS A 313           
SHEET    3  AH 5 GLU A 376  ILE A 377  1  O  GLU A 376   N  ILE A 341           
SHEET    4  AH 5 ILE A 401  ILE A 402  1  O  ILE A 401   N  ILE A 377           
SHEET    5  AH 5 GLU A 431  ILE A 432  1  O  GLU A 431   N  ILE A 402           
SHEET    1  AI 5 LEU A 345  ILE A 347  0                                        
SHEET    2  AI 5 LEU A 381  ILE A 383  1  O  LEU A 382   N  ILE A 347           
SHEET    3  AI 5 PHE A 412  VAL A 417  1  O  SER A 413   N  LEU A 381           
SHEET    4  AI 5 ASP A 436  SER A 440  1  O  ASP A 436   N  SER A 413           
SHEET    5  AI 5 THR A 464  ILE A 467  1  O  LYS A 465   N  ILE A 439           
SHEET    1  AJ 2 GLU A 524  GLU A 527  0                                        
SHEET    2  AJ 2 GLU A 530  GLN A 533 -1  O  GLU A 530   N  GLU A 527           
SHEET    1  AK 2 TYR A 561  ASP A 563  0                                        
SHEET    2  AK 2 HIS A 566  VAL A 568 -1  O  HIS A 566   N  ASP A 563           
SHEET    1  AL 3 ALA A 573  MET A 576  0                                        
SHEET    2  AL 3 LEU A 582  ALA A 587 -1  O  VAL A 583   N  GLY A 574           
SHEET    3  AL 3 CYS A 593  LEU A 595 -1  O  HIS A 594   N  TYR A 586           
SHEET    1  BA 2 THR B   8  PRO B   9  0                                        
SHEET    2  BA 2 ALA B  35  VAL B  36 -1  O  VAL B  36   N  THR B   8           
SHEET    1  BB 8 GLN B  46  ILE B  48  0                                        
SHEET    2  BB 8 TYR B  68  ALA B  70  1  O  TYR B  68   N  ILE B  47           
SHEET    3  BB 8 TYR B  90  MET B  92  1  O  TYR B  90   N  LEU B  69           
SHEET    4  BB 8 GLU B 114  TYR B 116  1  O  GLU B 114   N  LEU B  91           
SHEET    5  BB 8 GLU B 138  ASP B 140  1  O  GLU B 138   N  LEU B 115           
SHEET    6  BB 8 ASP B 162  ARG B 164  1  O  ASP B 162   N  LEU B 139           
SHEET    7  BB 8 TYR B 186  TRP B 188  1  O  TYR B 186   N  LEU B 163           
SHEET    8  BB 8 VAL B 215  ARG B 216  1  N  ARG B 216   O  ILE B 187           
SSBOND   1 CYS A    7    CYS A   34                          1555   1555  2.00  
SSBOND   2 CYS A  166    CYS A  175                          1555   1555  2.06  
SSBOND   3 CYS A  170    CYS A  183                          1555   1555  2.06  
SSBOND   4 CYS A  191    CYS A  199                          1555   1555  2.05  
SSBOND   5 CYS A  195    CYS A  207                          1555   1555  2.05  
SSBOND   6 CYS A  208    CYS A  216                          1555   1555  1.97  
SSBOND   7 CYS A  212    CYS A  224                          1555   1555  2.06  
SSBOND   8 CYS A  227    CYS A  236                          1555   1555  2.07  
SSBOND   9 CYS A  240    CYS A  267                          1555   1555  2.07  
SSBOND  10 CYS A  271    CYS A  283                          1555   1555  1.48  
SSBOND  11 CYS A  305    CYS A  309                          1555   1555  2.09  
SSBOND  12 CYS A  313    CYS A  338                          1555   1555  2.02  
SSBOND  13 CYS A  446    CYS A  475                          1555   1555  2.11  
SSBOND  14 CYS A  482    CYS A  491                          1555   1555  2.06  
SSBOND  15 CYS A  486    CYS A  499                          1555   1555  2.03  
SSBOND  16 CYS A  502    CYS A  511                          1555   1555  1.89  
SSBOND  17 CYS A  515    CYS A  531                          1555   1555  2.01  
SSBOND  18 CYS A  534    CYS A  547                          1555   1555  2.28  
SSBOND  19 CYS A  538    CYS A  555                          1555   1555  1.91  
SSBOND  20 CYS A  571    CYS A  593                          1555   1555  1.94  
SSBOND  21 CYS A  596    CYS A  604                          1555   1555  1.95  
SSBOND  22 CYS B  196    CYS B  229                          1555   1555  1.99  
LINK         ND2 ASN A 328                 C1  NAG A1616     1555   1555  1.39  
LINK         ND2 ASN A 420                 C1  NAG A1614     1555   1555  1.43  
LINK         ND2 ASN A 504                 C1  NAG A1615     1555   1555  1.49  
LINK         O4  NAG A1616                 C1  NAG A1617     1555   1555  1.45  
CISPEP   1 CYS B  198    PRO B  199          0         9.27                     
SITE     1 AC1  9 ASP A 323  SER A 324  LEU A 325  SER A 326                    
SITE     2 AC1  9 ASN A 328  ASN A 331  ASP A 355  THR A 358                    
SITE     3 AC1  9 THR A 360                                                     
SITE     1 AC2  1 ASN A 420                                                     
SITE     1 AC3  2 ARG A 503  ASN A 504                                          
CRYST1   66.790   88.340  189.210  90.00  90.00  90.00 P 2 21 21     4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.014972  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011320  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005285        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system