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Database: PDB
Entry: 4XSS
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Original site: 4XSS 
HEADER    HORMONE/HORMONE RECEPTOR                22-JAN-15   4XSS              
TITLE     INSULIN-LIKE GROWTH FACTOR I IN COMPLEX WITH SITE 1 OF A HYBRID       
TITLE    2 INSULIN RECEPTOR / TYPE 1 INSULIN-LIKE GROWTH FACTOR RECEPTOR        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INSULIN-LIKE GROWTH FACTOR I;                              
COMPND   3 CHAIN: B;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 49-118;                                       
COMPND   5 SYNONYM: IGF-I,MECHANO GROWTH FACTOR,MGF,SOMATOMEDIN-C;              
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: INSULIN RECEPTOR;                                          
COMPND   9 CHAIN: E;                                                            
COMPND  10 FRAGMENT: L1-CR, UNP RESIDUES 28-377;                                
COMPND  11 SYNONYM: IR;                                                         
COMPND  12 EC: 2.7.10.1;                                                        
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 MOL_ID: 3;                                                           
COMPND  15 MOLECULE: INSULIN-LIKE GROWTH FACTOR RECEPTOR ALPHA-CT PEPTIDE;      
COMPND  16 CHAIN: F;                                                            
COMPND  17 FRAGMENT: ALPHA-CT PEPTIDE, UNP RESIDUES 691-706;                    
COMPND  18 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: IGF1, IBP1;                                                    
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: INSR;                                                          
SOURCE  13 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE  15 EXPRESSION_SYSTEM_CELL_LINE: LEC 8 MUTANT CHO CELL;                  
SOURCE  16 MOL_ID: 3;                                                           
SOURCE  17 SYNTHETIC: YES;                                                      
SOURCE  18 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  19 ORGANISM_TAXID: 9606;                                                
SOURCE  20 OTHER_DETAILS: CHEMICAL SYNTHESIS                                    
KEYWDS    CELL SURFACE RECEPTOR/IMMUNE SYSTEM, INSULIN RECEPTOR, CT PEPTIDE,    
KEYWDS   2 INSULIN-LIKE GROWTH FACTOR RECEPTOR, HORMONE RECEPTOR-HORMONE-IMMUNE 
KEYWDS   3 SYSTEM COMPLEX, HORMONE-HORMONE RECEPTOR COMPLEX                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.LAWRENCE,G.K.-W.KONG,J.G.MENTING,M.C.LAWRENCE                       
REVDAT   6   27-SEP-23 4XSS    1       HETSYN LINK                              
REVDAT   5   29-JUL-20 4XSS    1       COMPND REMARK HETNAM LINK                
REVDAT   5 2                   1       SITE   ATOM                              
REVDAT   4   08-JAN-20 4XSS    1       REMARK                                   
REVDAT   3   13-SEP-17 4XSS    1       SOURCE JRNL   REMARK                     
REVDAT   2   22-JUL-15 4XSS    1       JRNL                                     
REVDAT   1   10-JUN-15 4XSS    0                                                
JRNL        AUTH   J.G.MENTING,C.F.LAWRENCE,G.K.KONG,M.B.MARGETTS,C.W.WARD,     
JRNL        AUTH 2 M.C.LAWRENCE                                                 
JRNL        TITL   STRUCTURAL CONGRUENCY OF LIGAND BINDING TO THE INSULIN AND   
JRNL        TITL 2 INSULIN/TYPE 1 INSULIN-LIKE GROWTH FACTOR HYBRID RECEPTORS.  
JRNL        REF    STRUCTURE                     V.  23  1271 2015              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   26027733                                                     
JRNL        DOI    10.1016/J.STR.2015.04.016                                    
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   J.G.MENTING                                                  
REMARK   1  TITL   PROTECTIVE HINGE IN INSULIN OPENS TO ENABLE ITS RECEPTOR     
REMARK   1  TITL 2 ENGAGEMENT                                                   
REMARK   1  REF    PROC.NATL.ACAD.SCI.USA        V. 111 E3395 2014              
REMARK   1  REFN                   ISSN 0027-8424                               
REMARK   1  DOI    10.1073/PNAS.1412897111                                      
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   J.G.MENTING                                                  
REMARK   1  TITL   HOW INSULIN ENGAGES ITS PRIMARY BINDING SITE ON THE INSULIN  
REMARK   1  TITL 2 RECEPTOR                                                     
REMARK   1  REF    NATURE                        V. 493   241 2013              
REMARK   1  REFN                   ISSN 0028-0836                               
REMARK   1  DOI    10.1038/NATURE11781                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.10.2                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.28                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 22377                          
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)  : 0.210                          
REMARK   3   R VALUE            (WORKING SET)  : 0.209                          
REMARK   3   FREE R VALUE                      : 0.229                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.130                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 1147                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 11                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 3.00                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 3.15                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 99.79                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2931                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2777                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2767                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2775                   
REMARK   3   BIN FREE R VALUE                        : 0.2808                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.60                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 164                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2933                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 148                                     
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 92.17                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 129.7                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 19.10080                                             
REMARK   3    B22 (A**2) : 19.10080                                             
REMARK   3    B33 (A**2) : -38.20170                                            
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 COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.721               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.332               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.247               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.346               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.254               
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.925                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.913                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 3177   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 4332   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 1126   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 77     ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 455    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 3177   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 438    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 3419   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.25                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 4.22                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 17.88                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { B|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  142.0555  143.3666   45.7306           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.6476 T22:   -0.7883                                    
REMARK   3     T33:    0.6704 T12:    0.3889                                    
REMARK   3     T13:    0.8037 T23:   -0.0415                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.2478 L22:    8.7352                                    
REMARK   3     L33:    9.6839 L12:   -3.0250                                    
REMARK   3     L13:    1.0867 L23:    1.8913                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0028 S12:    0.5746 S13:   -2.1363                     
REMARK   3     S21:    0.0123 S22:   -0.3574 S23:   -0.2974                     
REMARK   3     S31:    1.2200 S32:    0.1681 S33:    0.3603                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { E|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  128.9346  167.2206   45.9027           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.6828 T22:   -0.6762                                    
REMARK   3     T33:   -0.1839 T12:    0.1434                                    
REMARK   3     T13:    0.3632 T23:    0.0056                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.8517 L22:    2.8659                                    
REMARK   3     L33:    1.1623 L12:   -0.4041                                    
REMARK   3     L13:    0.1295 L23:   -0.0972                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.1630 S12:    0.4817 S13:   -0.4639                     
REMARK   3     S21:   -0.5943 S22:   -0.1575 S23:   -0.4756                     
REMARK   3     S31:    0.3562 S32:    0.2240 S33:    0.3205                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: { F|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  139.6418  148.7233   49.9330           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.3123 T22:   -0.3434                                    
REMARK   3     T33:    1.0836 T12:    0.4428                                    
REMARK   3     T13:    0.6473 T23:   -0.0142                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:   -2.5632 L22:    8.8765                                    
REMARK   3     L33:    0.8881 L12:    0.1672                                    
REMARK   3     L13:    4.3463 L23:   -6.0600                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0726 S12:    0.4225 S13:   -1.5662                     
REMARK   3     S21:    0.3789 S22:   -0.4624 S23:   -0.6519                     
REMARK   3     S31:    0.7470 S32:   -0.4015 S33:    0.3898                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4XSS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-JAN-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000206209.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-FEB-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 10.5                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : AUSTRALIAN SYNCHROTRON             
REMARK 200  BEAMLINE                       : MX2                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9537                             
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL MONOCHROMATOR       
REMARK 200                                   (SI111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 22377                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.280                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 6.300                              
REMARK 200  R MERGE                    (I) : 0.13000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.10                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 2.11000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 3LOH                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 79.87                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 6.11                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.75 M AMMONIUM SULFATE, 0.1 M CAPS      
REMARK 280  -NAOH (PH 10.5), 0.2 M LISO4, VAPOR DIFFUSION, HANGING DROP,        
REMARK 280  TEMPERATURE 298K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2                            
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z                                               
REMARK 290       6555   -X,-X+Y,-Z                                              
REMARK 290       7555   X+2/3,Y+1/3,Z+1/3                                       
REMARK 290       8555   -Y+2/3,X-Y+1/3,Z+1/3                                    
REMARK 290       9555   -X+Y+2/3,-X+1/3,Z+1/3                                   
REMARK 290      10555   Y+2/3,X+1/3,-Z+1/3                                      
REMARK 290      11555   X-Y+2/3,-Y+1/3,-Z+1/3                                   
REMARK 290      12555   -X+2/3,-X+Y+1/3,-Z+1/3                                  
REMARK 290      13555   X+1/3,Y+2/3,Z+2/3                                       
REMARK 290      14555   -Y+1/3,X-Y+2/3,Z+2/3                                    
REMARK 290      15555   -X+Y+1/3,-X+2/3,Z+2/3                                   
REMARK 290      16555   Y+1/3,X+2/3,-Z+2/3                                      
REMARK 290      17555   X-Y+1/3,-Y+2/3,-Z+2/3                                   
REMARK 290      18555   -X+1/3,-X+Y+2/3,-Z+2/3                                  
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000      109.58000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       63.26604            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       40.40667            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000      109.58000            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       63.26604            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       40.40667            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000      109.58000            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       63.26604            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       40.40667            
REMARK 290   SMTRY1  10 -0.500000  0.866025  0.000000      109.58000            
REMARK 290   SMTRY2  10  0.866025  0.500000  0.000000       63.26604            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       40.40667            
REMARK 290   SMTRY1  11  1.000000  0.000000  0.000000      109.58000            
REMARK 290   SMTRY2  11  0.000000 -1.000000  0.000000       63.26604            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       40.40667            
REMARK 290   SMTRY1  12 -0.500000 -0.866025  0.000000      109.58000            
REMARK 290   SMTRY2  12 -0.866025  0.500000  0.000000       63.26604            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       40.40667            
REMARK 290   SMTRY1  13  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000      126.53208            
REMARK 290   SMTRY3  13  0.000000  0.000000  1.000000       80.81333            
REMARK 290   SMTRY1  14 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  14  0.866025 -0.500000  0.000000      126.53208            
REMARK 290   SMTRY3  14  0.000000  0.000000  1.000000       80.81333            
REMARK 290   SMTRY1  15 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  15 -0.866025 -0.500000  0.000000      126.53208            
REMARK 290   SMTRY3  15  0.000000  0.000000  1.000000       80.81333            
REMARK 290   SMTRY1  16 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  16  0.866025  0.500000  0.000000      126.53208            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       80.81333            
REMARK 290   SMTRY1  17  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  17  0.000000 -1.000000  0.000000      126.53208            
REMARK 290   SMTRY3  17  0.000000  0.000000 -1.000000       80.81333            
REMARK 290   SMTRY1  18 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  18 -0.866025  0.500000  0.000000      126.53208            
REMARK 290   SMTRY3  18  0.000000  0.000000 -1.000000       80.81333            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5470 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20110 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 10.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, E, F, A, C                         
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTADECAMERIC              
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 45600 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 107910 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, E, F, A, C                         
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -0.500000 -0.866025  0.000000      328.74000            
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000      189.79813            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   3 -0.866025 -0.500000  0.000000      379.59625            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   4  0.000000  0.000000 -1.000000      121.22000            
REMARK 350   BIOMT1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   5  0.000000 -1.000000  0.000000      379.59625            
REMARK 350   BIOMT3   5  0.000000  0.000000 -1.000000      121.22000            
REMARK 350   BIOMT1   6 -0.500000 -0.866025  0.000000      328.74000            
REMARK 350   BIOMT2   6 -0.866025  0.500000  0.000000      189.79813            
REMARK 350   BIOMT3   6  0.000000  0.000000 -1.000000      121.22000            
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     GLY B     1                                                      
REMARK 465     PRO B     2                                                      
REMARK 465     LYS B    27                                                      
REMARK 465     PRO B    28                                                      
REMARK 465     THR B    29                                                      
REMARK 465     GLY B    30                                                      
REMARK 465     TYR B    31                                                      
REMARK 465     GLY B    32                                                      
REMARK 465     SER B    33                                                      
REMARK 465     SER B    34                                                      
REMARK 465     SER B    35                                                      
REMARK 465     ARG B    36                                                      
REMARK 465     ARG B    37                                                      
REMARK 465     ALA B    38                                                      
REMARK 465     PRO B    39                                                      
REMARK 465     GLN B    40                                                      
REMARK 465     LEU B    64                                                      
REMARK 465     LYS B    65                                                      
REMARK 465     PRO B    66                                                      
REMARK 465     ALA B    67                                                      
REMARK 465     LYS B    68                                                      
REMARK 465     SER B    69                                                      
REMARK 465     ALA B    70                                                      
REMARK 465     LYS E   310                                                      
REMARK 465     SER E   311                                                      
REMARK 465     SER E   312                                                      
REMARK 465     SER E   313                                                      
REMARK 465     LEU E   314                                                      
REMARK 465     VAL E   315                                                      
REMARK 465     PRO E   316                                                      
REMARK 465     ARG E   317                                                      
REMARK 465     VAL F   691                                                      
REMARK 465     PHE F   692                                                      
REMARK 465     PRO F   705                                                      
REMARK 465     GLU F   706                                                      
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    ASN E  15      -57.90     66.71                                   
REMARK 500    ASP E  59     -101.89   -101.87                                   
REMARK 500    ASN E  90        5.55     88.10                                   
REMARK 500    GLU E 153       57.87   -112.21                                   
REMARK 500    ASP E 157      112.13    -28.35                                   
REMARK 500    LYS E 197     -131.46     51.75                                   
REMARK 500    ASN E 230      -88.92   -109.04                                   
REMARK 500    ASP E 234       67.28     32.89                                   
REMARK 500    PRO E 244       31.62    -97.87                                   
REMARK 500    TRP E 251      -18.01   -151.43                                   
REMARK 500    LYS E 267      -84.79    -92.69                                   
REMARK 500    SER E 269       77.95     60.99                                   
REMARK 500    ARG E 271     -169.86    -71.85                                   
REMARK 500    GLN E 272       15.45     53.90                                   
REMARK 500    ASN E 298       19.82   -151.02                                   
REMARK 500    LEU E 299       15.74     52.97                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3W11   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3W12   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3W13   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3W14   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4OGA   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4XST   RELATED DB: PDB                                   
DBREF  4XSS B    1    70  UNP    P05019   IGF1_HUMAN      49    118             
DBREF  4XSS E    1   310  UNP    P06213   INSR_HUMAN      28    337             
DBREF  4XSS F  691   706  PDB    4XSS     4XSS           691    706             
SEQADV 4XSS HIS E  144  UNP  P06213    TYR   171 CONFLICT                       
SEQADV 4XSS SER E  311  UNP  P06213              EXPRESSION TAG                 
SEQADV 4XSS SER E  312  UNP  P06213              EXPRESSION TAG                 
SEQADV 4XSS SER E  313  UNP  P06213              EXPRESSION TAG                 
SEQADV 4XSS LEU E  314  UNP  P06213              EXPRESSION TAG                 
SEQADV 4XSS VAL E  315  UNP  P06213              EXPRESSION TAG                 
SEQADV 4XSS PRO E  316  UNP  P06213              EXPRESSION TAG                 
SEQADV 4XSS ARG E  317  UNP  P06213              EXPRESSION TAG                 
SEQRES   1 B   70  GLY PRO GLU THR LEU CYS GLY ALA GLU LEU VAL ASP ALA          
SEQRES   2 B   70  LEU GLN PHE VAL CYS GLY ASP ARG GLY PHE TYR PHE ASN          
SEQRES   3 B   70  LYS PRO THR GLY TYR GLY SER SER SER ARG ARG ALA PRO          
SEQRES   4 B   70  GLN THR GLY ILE VAL ASP GLU CYS CYS PHE ARG SER CYS          
SEQRES   5 B   70  ASP LEU ARG ARG LEU GLU MET TYR CYS ALA PRO LEU LYS          
SEQRES   6 B   70  PRO ALA LYS SER ALA                                          
SEQRES   1 E  317  HIS LEU TYR PRO GLY GLU VAL CYS PRO GLY MET ASP ILE          
SEQRES   2 E  317  ARG ASN ASN LEU THR ARG LEU HIS GLU LEU GLU ASN CYS          
SEQRES   3 E  317  SER VAL ILE GLU GLY HIS LEU GLN ILE LEU LEU MET PHE          
SEQRES   4 E  317  LYS THR ARG PRO GLU ASP PHE ARG ASP LEU SER PHE PRO          
SEQRES   5 E  317  LYS LEU ILE MET ILE THR ASP TYR LEU LEU LEU PHE ARG          
SEQRES   6 E  317  VAL TYR GLY LEU GLU SER LEU LYS ASP LEU PHE PRO ASN          
SEQRES   7 E  317  LEU THR VAL ILE ARG GLY SER ARG LEU PHE PHE ASN TYR          
SEQRES   8 E  317  ALA LEU VAL ILE PHE GLU MET VAL HIS LEU LYS GLU LEU          
SEQRES   9 E  317  GLY LEU TYR ASN LEU MET ASN ILE THR ARG GLY SER VAL          
SEQRES  10 E  317  ARG ILE GLU LYS ASN ASN GLU LEU CYS TYR LEU ALA THR          
SEQRES  11 E  317  ILE ASP TRP SER ARG ILE LEU ASP SER VAL GLU ASP ASN          
SEQRES  12 E  317  HIS ILE VAL LEU ASN LYS ASP ASP ASN GLU GLU CYS GLY          
SEQRES  13 E  317  ASP ILE CYS PRO GLY THR ALA LYS GLY LYS THR ASN CYS          
SEQRES  14 E  317  PRO ALA THR VAL ILE ASN GLY GLN PHE VAL GLU ARG CYS          
SEQRES  15 E  317  TRP THR HIS SER HIS CYS GLN LYS VAL CYS PRO THR ILE          
SEQRES  16 E  317  CYS LYS SER HIS GLY CYS THR ALA GLU GLY LEU CYS CYS          
SEQRES  17 E  317  HIS SER GLU CYS LEU GLY ASN CYS SER GLN PRO ASP ASP          
SEQRES  18 E  317  PRO THR LYS CYS VAL ALA CYS ARG ASN PHE TYR LEU ASP          
SEQRES  19 E  317  GLY ARG CYS VAL GLU THR CYS PRO PRO PRO TYR TYR HIS          
SEQRES  20 E  317  PHE GLN ASP TRP ARG CYS VAL ASN PHE SER PHE CYS GLN          
SEQRES  21 E  317  ASP LEU HIS HIS LYS CYS LYS ASN SER ARG ARG GLN GLY          
SEQRES  22 E  317  CYS HIS GLN TYR VAL ILE HIS ASN ASN LYS CYS ILE PRO          
SEQRES  23 E  317  GLU CYS PRO SER GLY TYR THR MET ASN SER SER ASN LEU          
SEQRES  24 E  317  LEU CYS THR PRO CYS LEU GLY PRO CYS PRO LYS SER SER          
SEQRES  25 E  317  SER LEU VAL PRO ARG                                          
SEQRES   1 F   16  VAL PHE GLU ASN PHE LEU HIS ASN SER ILE PHE VAL PRO          
SEQRES   2 F   16  ARG PRO GLU                                                  
HET    NAG  A   1      14                                                       
HET    NAG  A   2      14                                                       
HET    BMA  A   3      11                                                       
HET    FUC  A   4      10                                                       
HET    NAG  C   1      14                                                       
HET    NAG  C   2      14                                                       
HET    FUC  C   3      10                                                       
HET    SO4  E 401       5                                                       
HET    NAG  E 402      14                                                       
HET    NAG  E 407      14                                                       
HET    NAG  E 408      14                                                       
HET    NAG  E 412      14                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     BMA BETA-D-MANNOPYRANOSE                                             
HETNAM     FUC ALPHA-L-FUCOPYRANOSE                                             
HETNAM     SO4 SULFATE ION                                                      
HETSYN     NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-           
HETSYN   2 NAG  D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-          
HETSYN   3 NAG  2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE                         
HETSYN     BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE                               
HETSYN     FUC ALPHA-L-FUCOSE; 6-DEOXY-ALPHA-L-GALACTOPYRANOSE; L-              
HETSYN   2 FUC  FUCOSE; FUCOSE                                                  
FORMUL   4  NAG    8(C8 H15 N O6)                                               
FORMUL   4  BMA    C6 H12 O6                                                    
FORMUL   4  FUC    2(C6 H12 O5)                                                 
FORMUL   6  SO4    O4 S 2-                                                      
HELIX    1 AA1 CYS B    6  GLY B   19  1                                  14    
HELIX    2 AA2 ASP B   20  GLY B   22  5                                   3    
HELIX    3 AA3 GLY B   42  CYS B   48  1                                   7    
HELIX    4 AA4 ASP B   53  GLU B   58  1                                   6    
HELIX    5 AA5 MET B   59  CYS B   61  5                                   3    
HELIX    6 AA6 LEU E   17  GLU E   24  5                                   8    
HELIX    7 AA7 ARG E   42  ARG E   47  5                                   6    
HELIX    8 AA8 ASP E  132  ILE E  136  5                                   5    
HELIX    9 AA9 ASP E  150  ASN E  152  5                                   3    
HELIX   10 AB1 PRO E  193  GLY E  200  5                                   8    
HELIX   11 AB2 PHE E  256  HIS E  264  1                                   9    
HELIX   12 AB3 ASN F  694  PHE F  701  1                                   8    
SHEET    1 AA1 5 GLU E   6  ARG E  14  0                                        
SHEET    2 AA1 5 CYS E  26  MET E  38  1  O  GLU E  30   N  CYS E   8           
SHEET    3 AA1 5 MET E  56  ILE E  57  1  O  MET E  56   N  ILE E  29           
SHEET    4 AA1 5 VAL E  81  ILE E  82  1  O  VAL E  81   N  ILE E  57           
SHEET    5 AA1 5 ASN E 111  ILE E 112  1  O  ASN E 111   N  ILE E  82           
SHEET    1 AA2 6 GLU E   6  ARG E  14  0                                        
SHEET    2 AA2 6 CYS E  26  MET E  38  1  O  GLU E  30   N  CYS E   8           
SHEET    3 AA2 6 LEU E  61  VAL E  66  1  O  LEU E  62   N  LEU E  33           
SHEET    4 AA2 6 TYR E  91  PHE E  96  1  O  VAL E  94   N  LEU E  63           
SHEET    5 AA2 6 SER E 116  ASN E 122  1  O  ARG E 118   N  LEU E  93           
SHEET    6 AA2 6 HIS E 144  ASN E 148  1  O  HIS E 144   N  VAL E 117           
SHEET    1 AA3 2 ALA E 171  ILE E 174  0                                        
SHEET    2 AA3 2 GLN E 177  GLU E 180 -1  O  GLN E 177   N  ILE E 174           
SHEET    1 AA4 2 CYS E 182  THR E 184  0                                        
SHEET    2 AA4 2 HIS E 187  CYS E 188 -1  O  HIS E 187   N  TRP E 183           
SHEET    1 AA5 2 PHE E 231  TYR E 232  0                                        
SHEET    2 AA5 2 CYS E 237  VAL E 238 -1  O  VAL E 238   N  PHE E 231           
SHEET    1 AA6 4 ARG E 252  ASN E 255  0                                        
SHEET    2 AA6 4 TYR E 245  PHE E 248 -1  N  TYR E 246   O  VAL E 254           
SHEET    3 AA6 4 LYS E 283  ILE E 285  1  O  CYS E 284   N  HIS E 247           
SHEET    4 AA6 4 VAL E 278  HIS E 280 -1  N  VAL E 278   O  ILE E 285           
SHEET    1 AA7 2 TYR E 292  MET E 294  0                                        
SHEET    2 AA7 2 CYS E 301  PRO E 303 -1  O  THR E 302   N  THR E 293           
SSBOND   1 CYS B    6    CYS B   48                          1555   1555  2.04  
SSBOND   2 CYS B   18    CYS B   61                          1555   1555  2.05  
SSBOND   3 CYS B   47    CYS B   52                          1555   1555  2.06  
SSBOND   4 CYS E    8    CYS E   26                          1555   1555  2.04  
SSBOND   5 CYS E  126    CYS E  155                          1555   1555  2.04  
SSBOND   6 CYS E  159    CYS E  182                          1555   1555  2.05  
SSBOND   7 CYS E  169    CYS E  188                          1555   1555  2.05  
SSBOND   8 CYS E  192    CYS E  201                          1555   1555  2.04  
SSBOND   9 CYS E  196    CYS E  207                          1555   1555  2.04  
SSBOND  10 CYS E  208    CYS E  216                          1555   1555  2.03  
SSBOND  11 CYS E  212    CYS E  225                          1555   1555  2.01  
SSBOND  12 CYS E  228    CYS E  237                          1555   1555  2.02  
SSBOND  13 CYS E  241    CYS E  253                          1555   1555  2.04  
SSBOND  14 CYS E  259    CYS E  284                          1555   1555  2.04  
SSBOND  15 CYS E  266    CYS E  274                          1555   1555  2.05  
SSBOND  16 CYS E  288    CYS E  301                          1555   1555  2.05  
SSBOND  17 CYS E  304    CYS E  308                          1555   1555  2.05  
LINK         ND2 ASN E  16                 C1  NAG E 402     1555   1555  1.43  
LINK         ND2 ASN E  25                 C1  NAG A   1     1555   1555  1.44  
LINK         ND2 ASN E 111                 C1  NAG E 407     1555   1555  1.44  
LINK         ND2 ASN E 215                 C1  NAG E 408     1555   1555  1.43  
LINK         ND2 ASN E 255                 C1  NAG C   1     1555   1555  1.43  
LINK         ND2 ASN E 295                 C1  NAG E 412     1555   1555  1.44  
LINK         O4  NAG A   1                 C1  NAG A   2     1555   1555  1.43  
LINK         O6  NAG A   1                 C1  FUC A   4     1555   1555  1.41  
LINK         O4  NAG A   2                 C1  BMA A   3     1555   1555  1.43  
LINK         O4  NAG C   1                 C1  NAG C   2     1555   1555  1.43  
LINK         O6  NAG C   1                 C1  FUC C   3     1555   1555  1.41  
CISPEP   1 PRO E  243    PRO E  244          0        10.39                     
CRYST1  219.160  219.160  121.220  90.00  90.00 120.00 H 3 2        18          
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      0.004563  0.002634  0.000000        0.00000                         
SCALE2      0.000000  0.005269  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008249        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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