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Entry: 5U8Q
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HEADER    TRANSFERASE                             14-DEC-16   5U8Q              
TITLE     STRUCTURE OF THE ECTODOMAIN OF THE HUMAN TYPE 1 INSULIN-LIKE GROWTH   
TITLE    2 FACTOR RECEPTOR IN COMPLEX WITH IGF-I                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INSULIN-LIKE GROWTH FACTOR 1 RECEPTOR;                     
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: INSULIN-LIKE GROWTH FACTOR I RECEPTOR,IGF-I RECEPTOR;       
COMPND   5 EC: 2.7.10.1;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 OTHER_DETAILS: A17DELTA-BETA CONSTRUCT, SEE WHITTEN ET AL., J. MOL.  
COMPND   9 BIOL., V394, PP878-92 (2009).;                                       
COMPND  10 MOL_ID: 2;                                                           
COMPND  11 MOLECULE: INSULIN-LIKE GROWTH FACTOR I;                              
COMPND  12 CHAIN: B;                                                            
COMPND  13 SYNONYM: IGF-I,MECHANO GROWTH FACTOR,MGF,SOMATOMEDIN-C;              
COMPND  14 ENGINEERED: YES;                                                     
COMPND  15 OTHER_DETAILS: MATURE IGF-1;                                         
COMPND  16 MOL_ID: 3;                                                           
COMPND  17 MOLECULE: FV 24-60 HEAVY CHAIN;                                      
COMPND  18 CHAIN: H;                                                            
COMPND  19 ENGINEERED: YES;                                                     
COMPND  20 OTHER_DETAILS: HEAVY CHAIN VARIABLE DOMAIN (RESIDUES 1-118) OF MAB   
COMPND  21 24-60, INCLUDING ADDITIONAL GLY-THR AT THE N TERMINUS AND GLU-ASN-   
COMPND  22 LEU-TYR-PHE-GLN AT C TERMINUS.;                                      
COMPND  23 MOL_ID: 4;                                                           
COMPND  24 MOLECULE: FV 24-60 LIGHT CHAIN;                                      
COMPND  25 CHAIN: L;                                                            
COMPND  26 ENGINEERED: YES;                                                     
COMPND  27 OTHER_DETAILS: LIGHT CHAIN VARIABLE DOMAIN (RESIDUES 1-107) OF MAB   
COMPND  28 24-60, INCLUDING ADDITIONAL GLY AT THE N TERMINUS.                   
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: IGF1R;                                                         
SOURCE   6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: LEC8;                                   
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: FIII;                                 
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: FIII-IGFR.ECD;                            
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: IGF1, IBP1;                                                    
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  18 MOL_ID: 3;                                                           
SOURCE  19 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  20 ORGANISM_TAXID: 10090;                                               
SOURCE  21 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  22 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  23 EXPRESSION_SYSTEM_VECTOR_TYPE: PGPHFT;                               
SOURCE  24 EXPRESSION_SYSTEM_PLASMID: PGPHFT-SUMO-SCFV;                         
SOURCE  25 MOL_ID: 4;                                                           
SOURCE  26 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  27 ORGANISM_TAXID: 10090;                                               
SOURCE  28 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  29 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  30 EXPRESSION_SYSTEM_VECTOR_TYPE: PGPHFT;                               
SOURCE  31 EXPRESSION_SYSTEM_PLASMID: PGPHFT-SUMO-SCFV                          
KEYWDS    RECEPTOR TYROSINE KINASE, TYPE 1 INSULIN-LIKE GROWTH FACTOR RECEPTOR, 
KEYWDS   2 INSULIN-LIKE GROWTH-FACTOR I, TRANSFERASE                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.LAWRENCE,Y.XU                                                       
REVDAT   3   29-JUL-20 5U8Q    1       COMPND REMARK HETNAM SSBOND              
REVDAT   3 2                   1       LINK   SITE   ATOM                       
REVDAT   2   14-MAR-18 5U8Q    1       JRNL                                     
REVDAT   1   28-FEB-18 5U8Q    0                                                
JRNL        AUTH   Y.XU,G.K.KONG,J.G.MENTING,M.B.MARGETTS,C.A.DELAINE,          
JRNL        AUTH 2 L.M.JENKIN,V.V.KISELYOV,P.DE MEYTS,B.E.FORBES,M.C.LAWRENCE   
JRNL        TITL   HOW LIGAND BINDS TO THE TYPE 1 INSULIN-LIKE GROWTH FACTOR    
JRNL        TITL 2 RECEPTOR.                                                    
JRNL        REF    NAT COMMUN                    V.   9   821 2018              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        PMID   29483580                                                     
JRNL        DOI    10.1038/S41467-018-03219-7                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.27 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.11.1-2575_1692                              
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2           
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.27                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 22.17                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.326                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 32110                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.262                           
REMARK   3   R VALUE            (WORKING SET) : 0.260                           
REMARK   3   FREE R VALUE                     : 0.303                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.746                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1524                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 22.1730 -  7.1985    1.00     2995   144  0.2519 0.2993        
REMARK   3     2  7.1985 -  5.7464    1.00     2879   136  0.2707 0.3350        
REMARK   3     3  5.7464 -  5.0297    1.00     2827   141  0.2156 0.2547        
REMARK   3     4  5.0297 -  4.5742    1.00     2804   155  0.2023 0.2358        
REMARK   3     5  4.5742 -  4.2488    1.00     2786   146  0.2224 0.2589        
REMARK   3     6  4.2488 -  3.9999    0.99     2785   141  0.2527 0.3141        
REMARK   3     7  3.9999 -  3.8006    0.99     2751   137  0.2993 0.3401        
REMARK   3     8  3.8006 -  3.6359    0.99     2799   118  0.3274 0.3342        
REMARK   3     9  3.6359 -  3.4965    0.99     2731   149  0.3348 0.3952        
REMARK   3    10  3.4965 -  3.3763    0.99     2736   126  0.3541 0.4154        
REMARK   3    11  3.3763 -  3.2710    0.90     2493   131  0.4146 0.4307        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.543            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 38.905           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 110.9                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 177.8                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.002           8934                                  
REMARK   3   ANGLE     :  0.520          12148                                  
REMARK   3   CHIRALITY :  0.044           1337                                  
REMARK   3   PLANARITY :  0.003           1549                                  
REMARK   3   DIHEDRAL  : 11.595           5364                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 23                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 266 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  26.2422  29.7960 -49.9071              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.5229 T22:   1.9333                                     
REMARK   3      T33:   1.2098 T12:  -0.0328                                     
REMARK   3      T13:   0.2074 T23:  -0.3994                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.2606 L22:   1.1278                                     
REMARK   3      L33:   1.8219 L12:   1.2116                                     
REMARK   3      L13:   0.5625 L23:   0.9176                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0445 S12:   2.7864 S13:  -0.7600                       
REMARK   3      S21:  -0.4098 S22:   0.4533 S23:  -0.3603                       
REMARK   3      S31:   0.3378 S32:   0.6463 S33:  -0.4663                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 267 THROUGH 456 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  18.4690  13.2341   1.4006              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.5183 T22:   0.8510                                     
REMARK   3      T33:   1.2506 T12:   0.0859                                     
REMARK   3      T13:  -0.0529 T23:  -0.1359                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4162 L22:   3.0590                                     
REMARK   3      L33:   2.9909 L12:   1.2821                                     
REMARK   3      L13:  -1.3478 L23:  -1.4117                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1769 S12:  -0.3829 S13:  -0.1550                       
REMARK   3      S21:   0.1511 S22:  -0.0118 S23:  -0.9718                       
REMARK   3      S31:  -0.2033 S32:   0.1161 S33:   0.1402                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 457 THROUGH 575 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   9.5376 -17.8175   6.4361              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   3.1563 T22:   0.8962                                     
REMARK   3      T33:   0.6327 T12:   0.3103                                     
REMARK   3      T13:  -0.0273 T23:   0.0935                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.3406 L22:   3.6635                                     
REMARK   3      L33:   6.0028 L12:   0.1421                                     
REMARK   3      L13:  -1.2333 L23:  -1.0725                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0788 S12:  -0.3620 S13:   1.0261                       
REMARK   3      S21:  -0.0300 S22:   0.3659 S23:   0.5248                       
REMARK   3      S31:  -0.8633 S32:  -0.1547 S33:  -0.2346                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 576 THROUGH 900 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  18.1669 -23.3123 -57.9280              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.8538 T22:   1.5663                                     
REMARK   3      T33:   0.8687 T12:   0.0893                                     
REMARK   3      T13:   0.0942 T23:  -0.0450                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2261 L22:   0.6512                                     
REMARK   3      L33:   2.2604 L12:  -0.3632                                     
REMARK   3      L13:  -0.0031 L23:   3.0208                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3172 S12:  -0.0311 S13:   0.1475                       
REMARK   3      S21:  -0.3379 S22:  -0.0372 S23:  -0.0241                       
REMARK   3      S31:   0.0554 S32:   0.2890 S33:  -0.2995                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 4 THROUGH 21 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.1149  24.6526 -44.9978              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.3705 T22:   1.9866                                     
REMARK   3      T33:   0.5992 T12:  -0.0540                                     
REMARK   3      T13:  -0.0696 T23:  -0.2041                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.5307 L22:   3.6368                                     
REMARK   3      L33:   9.7914 L12:   0.6185                                     
REMARK   3      L13:  -1.0845 L23:  -1.6164                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1542 S12:   2.4226 S13:   0.1153                       
REMARK   3      S21:   0.3533 S22:   1.2402 S23:  -0.5958                       
REMARK   3      S31:  -0.0652 S32:  -0.3302 S33:  -0.7493                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 22 THROUGH 53 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):   2.8838  19.9558 -35.6241              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.2752 T22:   1.2860                                     
REMARK   3      T33:   0.9264 T12:   0.4935                                     
REMARK   3      T13:   0.2642 T23:  -0.1151                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.0633 L22:   4.6026                                     
REMARK   3      L33:   2.7954 L12:   0.5280                                     
REMARK   3      L13:   1.3880 L23:  -2.6857                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.7179 S12:   0.9148 S13:  -1.1791                       
REMARK   3      S21:  -1.4741 S22:  -0.4348 S23:   0.8086                       
REMARK   3      S31:   0.9360 S32:  -0.4378 S33:  -0.1595                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 54 THROUGH 63 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.7378  27.0095 -35.3262              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.9980 T22:   1.5682                                     
REMARK   3      T33:  -0.0647 T12:   0.5210                                     
REMARK   3      T13:  -0.2308 T23:  -0.1712                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5510 L22:   3.2592                                     
REMARK   3      L33:   5.8178 L12:   0.6721                                     
REMARK   3      L13:   1.3888 L23:   4.0178                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2037 S12:  -0.9814 S13:  -0.8864                       
REMARK   3      S21:   1.2693 S22:  -0.1188 S23:   0.2376                       
REMARK   3      S31:   0.2274 S32:   0.9904 S33:  -0.0707                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'H' AND (RESID 1 THROUGH 17 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  14.2524  56.2686 -17.5537              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.9135 T22:   0.8563                                     
REMARK   3      T33:   0.7914 T12:  -0.0781                                     
REMARK   3      T13:  -0.1596 T23:   0.1262                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6717 L22:   4.9088                                     
REMARK   3      L33:   3.7163 L12:  -4.1336                                     
REMARK   3      L13:  -0.8465 L23:   1.5556                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   1.5032 S12:  -0.8674 S13:   0.6975                       
REMARK   3      S21:  -0.9264 S22:  -0.3050 S23:   0.3724                       
REMARK   3      S31:  -0.2197 S32:  -0.3257 S33:  -1.0393                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'H' AND (RESID 18 THROUGH 25 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  17.3624  52.8657 -22.8102              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.0650 T22:   0.9679                                     
REMARK   3      T33:   0.7574 T12:  -0.1597                                     
REMARK   3      T13:   0.0319 T23:  -0.1846                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3073 L22:   7.5665                                     
REMARK   3      L33:   4.3686 L12:   3.6044                                     
REMARK   3      L13:   0.1549 L23:  -1.1821                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -1.3066 S12:  -0.1802 S13:  -0.4419                       
REMARK   3      S21:  -2.0611 S22:  -0.6577 S23:   0.3800                       
REMARK   3      S31:   1.0732 S32:  -1.0259 S33:   1.6228                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'H' AND (RESID 26 THROUGH 51 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  23.1233  46.7007 -15.2555              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.6294 T22:   0.8647                                     
REMARK   3      T33:   0.5161 T12:  -0.4681                                     
REMARK   3      T13:   0.0822 T23:  -0.0198                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6994 L22:   7.6742                                     
REMARK   3      L33:   1.1612 L12:  -1.4434                                     
REMARK   3      L13:   1.8486 L23:  -2.4342                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.8147 S12:  -0.0277 S13:  -0.3639                       
REMARK   3      S21:  -1.5201 S22:  -0.4592 S23:  -0.9171                       
REMARK   3      S31:  -1.6260 S32:   1.2952 S33:  -0.4423                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'H' AND (RESID 52 THROUGH 57 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  22.8618  37.7850 -27.5044              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.7950 T22:  -0.3944                                     
REMARK   3      T33:   1.2726 T12:  -0.1854                                     
REMARK   3      T13:   0.4656 T23:  -0.5481                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1923 L22:   5.1658                                     
REMARK   3      L33:   4.6433 L12:   3.2655                                     
REMARK   3      L13:   1.0646 L23:   2.7439                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2780 S12:   0.1157 S13:  -0.8475                       
REMARK   3      S21:  -0.2136 S22:  -0.5280 S23:   0.3948                       
REMARK   3      S31:   0.3216 S32:  -0.2768 S33:   0.1540                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'H' AND (RESID 58 THROUGH 64 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  16.1251  37.6775 -12.2212              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.9664 T22:   1.0713                                     
REMARK   3      T33:   1.0725 T12:  -0.3543                                     
REMARK   3      T13:   0.2643 T23:  -0.0603                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.7189 L22:   4.4793                                     
REMARK   3      L33:   5.1569 L12:  -5.0545                                     
REMARK   3      L13:  -5.4165 L23:   4.8014                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   1.4069 S12:  -1.1826 S13:  -0.4936                       
REMARK   3      S21:   2.4772 S22:  -1.1705 S23:   1.5452                       
REMARK   3      S31:   1.0675 S32:  -0.5601 S33:  -0.2916                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN 'H' AND (RESID 65 THROUGH 73 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  13.2238  42.6397 -19.8967              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.8135 T22:   1.0737                                     
REMARK   3      T33:   0.9585 T12:  -0.5169                                     
REMARK   3      T13:   0.0228 T23:  -0.2303                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.8013 L22:   9.5350                                     
REMARK   3      L33:   1.7270 L12:  -6.4989                                     
REMARK   3      L13:  -2.6344 L23:   3.9999                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -2.6408 S12:   0.2376 S13:  -0.7784                       
REMARK   3      S21:   0.0033 S22:  -0.9192 S23:   1.5499                       
REMARK   3      S31:   0.1896 S32:  -1.3349 S33:   3.4452                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN 'H' AND (RESID 74 THROUGH 83 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  16.1334  48.2377 -25.2920              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.7408 T22:   1.5901                                     
REMARK   3      T33:   0.7766 T12:   0.1165                                     
REMARK   3      T13:  -0.2439 T23:  -0.2291                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.3355 L22:   6.3639                                     
REMARK   3      L33:   3.7665 L12:  -5.7067                                     
REMARK   3      L13:  -4.6134 L23:   4.8862                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.9919 S12:   2.5027 S13:  -1.3902                       
REMARK   3      S21:  -1.6193 S22:  -0.8424 S23:  -0.4851                       
REMARK   3      S31:   1.7631 S32:  -4.7007 S33:   1.5671                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: CHAIN 'H' AND (RESID 84 THROUGH 91 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):   6.3357  48.3619  -8.0278              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.3733 T22:   1.6384                                     
REMARK   3      T33:   0.7500 T12:  -0.1227                                     
REMARK   3      T13:   0.3952 T23:   0.0789                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.1189 L22:   1.9942                                     
REMARK   3      L33:   3.9388 L12:  -4.2213                                     
REMARK   3      L13:   2.9334 L23:   2.3046                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.8092 S12:  -2.2625 S13:  -0.5482                       
REMARK   3      S21:   1.0764 S22:   1.0328 S23:   0.5500                       
REMARK   3      S31:  -1.2219 S32:  -0.8777 S33:  -0.9789                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: CHAIN 'H' AND (RESID 92 THROUGH 97 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  19.3830  52.1430 -12.5903              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.5734 T22:   0.9408                                     
REMARK   3      T33:   0.6182 T12:   0.2028                                     
REMARK   3      T13:  -0.4087 T23:  -0.0656                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.2068 L22:   8.8534                                     
REMARK   3      L33:   2.7131 L12:  -0.2652                                     
REMARK   3      L13:  -1.1545 L23:   4.7955                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2992 S12:  -1.5905 S13:   1.8708                       
REMARK   3      S21:   0.8961 S22:  -0.4202 S23:   0.8846                       
REMARK   3      S31:  -0.9588 S32:  -1.0692 S33:   0.3519                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: CHAIN 'H' AND (RESID 98 THROUGH 118 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  23.5483  50.1994 -14.6840              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.1175 T22:   0.9980                                     
REMARK   3      T33:   1.0333 T12:  -0.4748                                     
REMARK   3      T13:   0.1117 T23:  -0.1121                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7559 L22:   1.6890                                     
REMARK   3      L33:   8.9295 L12:   1.5762                                     
REMARK   3      L13:  -2.0190 L23:   0.8110                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.8787 S12:   1.6152 S13:  -0.2114                       
REMARK   3      S21:  -1.3639 S22:   0.7353 S23:  -0.4737                       
REMARK   3      S31:   0.5307 S32:   0.2341 S33:   0.1440                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: CHAIN 'L' AND (RESID 1 THROUGH 13 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  29.9289  46.8462   4.4989              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.4985 T22:   1.0525                                     
REMARK   3      T33:   1.0995 T12:  -0.0692                                     
REMARK   3      T13:   0.2332 T23:   0.2400                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5999 L22:   4.8021                                     
REMARK   3      L33:   7.3758 L12:  -0.9142                                     
REMARK   3      L13:   0.5218 L23:   3.6802                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.7890 S12:  -0.8627 S13:   1.5352                       
REMARK   3      S21:   2.6321 S22:   0.1582 S23:   0.9830                       
REMARK   3      S31:  -0.9587 S32:  -0.2458 S33:  -0.9090                       
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    SELECTION: CHAIN 'L' AND (RESID 14 THROUGH 38 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  35.7746  45.9406  -0.6679              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.0018 T22:   0.9847                                     
REMARK   3      T33:   0.8882 T12:  -0.1156                                     
REMARK   3      T13:  -0.0197 T23:   0.1342                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.0776 L22:   3.6083                                     
REMARK   3      L33:   7.3460 L12:  -3.4413                                     
REMARK   3      L13:  -1.3170 L23:  -1.7901                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0577 S12:  -0.2905 S13:  -0.5145                       
REMARK   3      S21:   1.9494 S22:  -0.6686 S23:   0.3983                       
REMARK   3      S31:   1.4530 S32:   0.8663 S33:   0.5489                       
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    SELECTION: CHAIN 'L' AND (RESID 39 THROUGH 67 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  38.0720  51.0897  -8.2668              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.9144 T22:   1.3723                                     
REMARK   3      T33:   0.9332 T12:  -0.3654                                     
REMARK   3      T13:  -0.1030 T23:   0.0981                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4830 L22:   2.5088                                     
REMARK   3      L33:   5.0229 L12:   0.2903                                     
REMARK   3      L13:   0.5650 L23:   3.3312                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3321 S12:  -0.2832 S13:  -0.1620                       
REMARK   3      S21:   0.3587 S22:  -0.2105 S23:  -0.1145                       
REMARK   3      S31:  -2.6113 S32:   0.9942 S33:  -0.2537                       
REMARK   3   TLS GROUP : 21                                                     
REMARK   3    SELECTION: CHAIN 'L' AND (RESID 68 THROUGH 75 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  39.1643  43.5313   1.3355              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.8894 T22:   0.9210                                     
REMARK   3      T33:   1.7116 T12:   0.2571                                     
REMARK   3      T13:   0.2551 T23:   0.0992                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.3958 L22:   6.9976                                     
REMARK   3      L33:   5.1645 L12:   6.6180                                     
REMARK   3      L13:  -5.7135 L23:  -5.9668                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -1.1999 S12:  -1.5964 S13:  -1.6321                       
REMARK   3      S21:   3.4884 S22:  -1.0817 S23:  -3.0362                       
REMARK   3      S31:  -0.0218 S32:  -0.7378 S33:   2.1050                       
REMARK   3   TLS GROUP : 22                                                     
REMARK   3    SELECTION: CHAIN 'L' AND (RESID 76 THROUGH 90 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  35.8422  55.0996  -2.0782              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.1315 T22:   0.9164                                     
REMARK   3      T33:   0.7732 T12:  -0.1853                                     
REMARK   3      T13:   0.0135 T23:   0.0268                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.3002 L22:   9.3462                                     
REMARK   3      L33:   3.9408 L12:  -2.1796                                     
REMARK   3      L13:   1.7672 L23:   4.2134                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2320 S12:  -0.3186 S13:  -0.4992                       
REMARK   3      S21:  -0.1759 S22:   0.1581 S23:  -1.1248                       
REMARK   3      S31:  -0.1750 S32:   1.2022 S33:   0.1646                       
REMARK   3   TLS GROUP : 23                                                     
REMARK   3    SELECTION: CHAIN 'L' AND (RESID 91 THROUGH 107 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  28.8344  46.7011  -2.1176              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.3582 T22:   0.9883                                     
REMARK   3      T33:   0.7206 T12:  -0.4751                                     
REMARK   3      T13:  -0.0292 T23:   0.4204                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.0508 L22:   8.5816                                     
REMARK   3      L33:   1.5368 L12:   3.5345                                     
REMARK   3      L13:  -1.3397 L23:   0.2656                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0502 S12:  -1.0103 S13:  -0.4333                       
REMARK   3      S21:   0.5479 S22:   0.2131 S23:   0.3872                       
REMARK   3      S31:   0.1081 S32:  -0.0888 S33:  -0.5123                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5U8Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-DEC-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000225483.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-AUG-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
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                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 32228                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.270                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY                : 7.200                              
REMARK 200  R MERGE                    (I) : 0.19000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.1000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.27                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.46                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 2.07000                            
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: 5U8R                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 67.94                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.84                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.2 M AMMONIUM SULFATE, 0.1 M            
REMARK 280  IMIDAZOLE-MALATE PH 7.0. IGF-1 WAS INCLUDED BY SOAKING DIRECTLY     
REMARK 280  INTO THE MOTHER CRYSTAL. FOR FULL DETAILS SEE THE PRIMARY           
REMARK 280  CITATION., VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K          
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       44.34500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       98.83000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       44.34500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       98.83000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: OCTAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 21280 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 107620 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, H, L, C, D, E                   
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 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  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     LYS A    36                                                      
REMARK 465     ALA A    37                                                      
REMARK 465     GLU A    38                                                      
REMARK 465     ASP A    39                                                      
REMARK 465     TYR A    40                                                      
REMARK 465     GLY A   154                                                      
REMARK 465     THR A   155                                                      
REMARK 465     MET A   156                                                      
REMARK 465     GLU A   157                                                      
REMARK 465     GLU A   158                                                      
REMARK 465     LYS A   159                                                      
REMARK 465     PRO A   160                                                      
REMARK 465     MET A   161                                                      
REMARK 465     GLY A   190                                                      
REMARK 465     LYS A   191                                                      
REMARK 465     ARG A   192                                                      
REMARK 465     ASP A   645                                                      
REMARK 465     GLY A   646                                                      
REMARK 465     THR A   647                                                      
REMARK 465     ILE A   648                                                      
REMARK 465     ASP A   649                                                      
REMARK 465     ILE A   650                                                      
REMARK 465     GLU A   651                                                      
REMARK 465     GLU A   652                                                      
REMARK 465     VAL A   653                                                      
REMARK 465     THR A   654                                                      
REMARK 465     GLU A   655                                                      
REMARK 465     ASN A   656                                                      
REMARK 465     PRO A   657                                                      
REMARK 465     LYS A   658                                                      
REMARK 465     THR A   659                                                      
REMARK 465     GLU A   660                                                      
REMARK 465     VAL A   661                                                      
REMARK 465     CYS A   662                                                      
REMARK 465     GLY A   663                                                      
REMARK 465     GLY A   664                                                      
REMARK 465     GLU A   665                                                      
REMARK 465     LYS A   666                                                      
REMARK 465     GLY A   667                                                      
REMARK 465     PRO A   668                                                      
REMARK 465     CYS A   669                                                      
REMARK 465     CYS A   670                                                      
REMARK 465     ALA A   671                                                      
REMARK 465     CYS A   672                                                      
REMARK 465     PRO A   673                                                      
REMARK 465     LYS A   674                                                      
REMARK 465     THR A   675                                                      
REMARK 465     GLU A   676                                                      
REMARK 465     ALA A   677                                                      
REMARK 465     GLU A   678                                                      
REMARK 465     LYS A   679                                                      
REMARK 465     GLN A   680                                                      
REMARK 465     ALA A   681                                                      
REMARK 465     GLU A   682                                                      
REMARK 465     LYS A   683                                                      
REMARK 465     GLU A   684                                                      
REMARK 465     GLU A   685                                                      
REMARK 465     ALA A   686                                                      
REMARK 465     GLU A   687                                                      
REMARK 465     TYR A   688                                                      
REMARK 465     GLU A   726                                                      
REMARK 465     ARG A   727                                                      
REMARK 465     LYS A   728                                                      
REMARK 465     ARG A   729                                                      
REMARK 465     ARG A   730                                                      
REMARK 465     ASP A   731                                                      
REMARK 465     VAL A   732                                                      
REMARK 465     MET A   733                                                      
REMARK 465     GLN A   734                                                      
REMARK 465     VAL A   735                                                      
REMARK 465     ALA A   736                                                      
REMARK 465     ASN A   737                                                      
REMARK 465     ALA A   738                                                      
REMARK 465     GLY A   739                                                      
REMARK 465     ASN A   740                                                      
REMARK 465     ASN A   741                                                      
REMARK 465     GLU A   742                                                      
REMARK 465     THR A   743                                                      
REMARK 465     GLU A   744                                                      
REMARK 465     GLU A   901                                                      
REMARK 465     ASN A   902                                                      
REMARK 465     PHE A   903                                                      
REMARK 465     ILE A   904                                                      
REMARK 465     HIS A   905                                                      
REMARK 465     GLY B     1                                                      
REMARK 465     PRO B     2                                                      
REMARK 465     GLU B     3                                                      
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     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     GLY H    -1                                                      
REMARK 465     THR H     0                                                      
REMARK 465     GLU H   119                                                      
REMARK 465     ASN H   120                                                      
REMARK 465     LEU H   121                                                      
REMARK 465     TYR H   122                                                      
REMARK 465     PHE H   123                                                      
REMARK 465     GLN H   124                                                      
REMARK 465     GLY L     0                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     SER A 187    OG                                                  
REMARK 470     THR A 188    OG1  CG2                                            
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 A  11      -85.36     62.26                                   
REMARK 500    GLU A  53     -133.45    -90.86                                   
REMARK 500    ASN A  94       -5.53     64.75                                   
REMARK 500    ARG A 108      -84.11   -118.64                                   
REMARK 500    CYS A 148      -84.00   -122.88                                   
REMARK 500    ASN A 168     -115.79     59.68                                   
REMARK 500    THR A 195     -156.89    -84.81                                   
REMARK 500    ASN A 198       70.34     60.73                                   
REMARK 500    GLU A 199      118.03   -162.77                                   
REMARK 500    HIS A 223     -105.81     58.56                                   
REMARK 500    GLU A 242     -120.69     59.34                                   
REMARK 500    TRP A 244      -23.95   -140.08                                   
REMARK 500    SER A 286      -73.84     56.07                                   
REMARK 500    GLN A 287       72.72    -67.09                                   
REMARK 500    ARG A 335      -75.00    -76.72                                   
REMARK 500    ASN A 338     -135.20    -98.61                                   
REMARK 500    LYS A 373      -72.59    -74.36                                   
REMARK 500    ASN A 374        0.66    -68.12                                   
REMARK 500    LEU A 379     -103.87    -80.88                                   
REMARK 500    LEU A 398       95.52    -69.30                                   
REMARK 500    ASP A 405        4.02    -62.48                                   
REMARK 500    CYS A 458      -77.48    -77.73                                   
REMARK 500    SER A 471     -155.66   -119.46                                   
REMARK 500    ASN A 473       -1.15   -149.14                                   
REMARK 500    ASN A 504       81.25    -63.69                                   
REMARK 500    ASP A 509       -0.95   -141.88                                   
REMARK 500    ASP A 512     -144.94     58.06                                   
REMARK 500    SER A 516       36.86    -77.19                                   
REMARK 500    SER A 518      -67.67   -144.75                                   
REMARK 500    GLU A 560       77.76    -67.59                                   
REMARK 500    ASP A 562        5.23    -69.18                                   
REMARK 500    ARG A 565      -79.45   -111.12                                   
REMARK 500    ASP A 586       74.63     56.86                                   
REMARK 500    ASN A 754      -58.85   -124.95                                   
REMARK 500    ASN A 762       82.89     57.32                                   
REMARK 500    GLU A 815     -152.53     61.03                                   
REMARK 500    ASN A 816       57.81   -104.64                                   
REMARK 500    ARG A 865       83.72     56.82                                   
REMARK 500    THR A 898       95.26    -61.90                                   
REMARK 500    GLN B  40       39.38    -95.74                                   
REMARK 500    GLU B  46      -49.49   -133.03                                   
REMARK 500    ARG H  85       56.77     39.40                                   
REMARK 500    SER H  98     -155.50   -158.20                                   
REMARK 500    ASP H 101     -167.57   -163.97                                   
REMARK 500    ASN L  31     -118.97   -127.62                                   
REMARK 500    ALA L  51      -32.39     68.99                                   
REMARK 500    SER L  52      -56.77   -128.92                                   
REMARK 500    SER L  91       11.70   -142.39                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5U8R   RELATED DB: PDB                                   
REMARK 900 THE SAME COMPLEX WITHOUT IGF-I                                       
DBREF  5U8Q A    1   905  UNP    P08069   IGF1R_HUMAN     31    935             
DBREF  5U8Q B    1    70  UNP    P05019   IGF1_HUMAN      49    118             
DBREF  5U8Q H   -1   124  PDB    5U8Q     5U8Q            -1    124             
DBREF  5U8Q L    0   107  PDB    5U8Q     5U8Q             0    107             
SEQADV 5U8Q     A       UNP  P08069    THR   748 DELETION                       
SEQADV 5U8Q     A       UNP  P08069    THR   749 DELETION                       
SEQADV 5U8Q     A       UNP  P08069    MET   750 DELETION                       
SEQADV 5U8Q     A       UNP  P08069    SER   751 DELETION                       
SEQADV 5U8Q     A       UNP  P08069    SER   752 DELETION                       
SEQADV 5U8Q     A       UNP  P08069    ARG   753 DELETION                       
SEQADV 5U8Q     A       UNP  P08069    SER   754 DELETION                       
SEQADV 5U8Q     A       UNP  P08069    ARG   755 DELETION                       
SEQADV 5U8Q     A       UNP  P08069    ASN   756 DELETION                       
SEQADV 5U8Q     A       UNP  P08069    THR   757 DELETION                       
SEQADV 5U8Q     A       UNP  P08069    THR   758 DELETION                       
SEQADV 5U8Q     A       UNP  P08069    ALA   759 DELETION                       
SEQADV 5U8Q     A       UNP  P08069    ALA   760 DELETION                       
SEQADV 5U8Q     A       UNP  P08069    ASP   761 DELETION                       
SEQADV 5U8Q     A       UNP  P08069    THR   762 DELETION                       
SEQADV 5U8Q     A       UNP  P08069    TYR   763 DELETION                       
SEQADV 5U8Q     A       UNP  P08069    ASN   764 DELETION                       
SEQADV 5U8Q     A       UNP  P08069    ILE   765 DELETION                       
SEQADV 5U8Q     A       UNP  P08069    THR   766 DELETION                       
SEQADV 5U8Q     A       UNP  P08069    ASP   767 DELETION                       
SEQADV 5U8Q ALA A  738  UNP  P08069    PRO   768 CONFLICT                       
SEQADV 5U8Q GLY A  739  UNP  P08069    GLU   769 CONFLICT                       
SEQADV 5U8Q ASN A  740  UNP  P08069    GLU   770 CONFLICT                       
SEQADV 5U8Q ASN A  741  UNP  P08069    LEU   771 CONFLICT                       
SEQRES   1 A  885  GLU ILE CYS GLY PRO GLY ILE ASP ILE ARG ASN ASP TYR          
SEQRES   2 A  885  GLN GLN LEU LYS ARG LEU GLU ASN CYS THR VAL ILE GLU          
SEQRES   3 A  885  GLY TYR LEU HIS ILE LEU LEU ILE SER LYS ALA GLU ASP          
SEQRES   4 A  885  TYR ARG SER TYR ARG PHE PRO LYS LEU THR VAL ILE THR          
SEQRES   5 A  885  GLU TYR LEU LEU LEU PHE ARG VAL ALA GLY LEU GLU SER          
SEQRES   6 A  885  LEU GLY ASP LEU PHE PRO ASN LEU THR VAL ILE ARG GLY          
SEQRES   7 A  885  TRP LYS LEU PHE TYR ASN TYR ALA LEU VAL ILE PHE GLU          
SEQRES   8 A  885  MET THR ASN LEU LYS ASP ILE GLY LEU TYR ASN LEU ARG          
SEQRES   9 A  885  ASN ILE THR ARG GLY ALA ILE ARG ILE GLU LYS ASN ALA          
SEQRES  10 A  885  ASP LEU CYS TYR LEU SER THR VAL ASP TRP SER LEU ILE          
SEQRES  11 A  885  LEU ASP ALA VAL SER ASN ASN TYR ILE VAL GLY ASN LYS          
SEQRES  12 A  885  PRO PRO LYS GLU CYS GLY ASP LEU CYS PRO GLY THR MET          
SEQRES  13 A  885  GLU GLU LYS PRO MET CYS GLU LYS THR THR ILE ASN ASN          
SEQRES  14 A  885  GLU TYR ASN TYR ARG CYS TRP THR THR ASN ARG CYS GLN          
SEQRES  15 A  885  LYS MET CYS PRO SER THR CYS GLY LYS ARG ALA CYS THR          
SEQRES  16 A  885  GLU ASN ASN GLU CYS CYS HIS PRO GLU CYS LEU GLY SER          
SEQRES  17 A  885  CYS SER ALA PRO ASP ASN ASP THR ALA CYS VAL ALA CYS          
SEQRES  18 A  885  ARG HIS TYR TYR TYR ALA GLY VAL CYS VAL PRO ALA CYS          
SEQRES  19 A  885  PRO PRO ASN THR TYR ARG PHE GLU GLY TRP ARG CYS VAL          
SEQRES  20 A  885  ASP ARG ASP PHE CYS ALA ASN ILE LEU SER ALA GLU SER          
SEQRES  21 A  885  SER ASP SER GLU GLY PHE VAL ILE HIS ASP GLY GLU CYS          
SEQRES  22 A  885  MET GLN GLU CYS PRO SER GLY PHE ILE ARG ASN GLY SER          
SEQRES  23 A  885  GLN SER MET TYR CYS ILE PRO CYS GLU GLY PRO CYS PRO          
SEQRES  24 A  885  LYS VAL CYS GLU GLU GLU LYS LYS THR LYS THR ILE ASP          
SEQRES  25 A  885  SER VAL THR SER ALA GLN MET LEU GLN GLY CYS THR ILE          
SEQRES  26 A  885  PHE LYS GLY ASN LEU LEU ILE ASN ILE ARG ARG GLY ASN          
SEQRES  27 A  885  ASN ILE ALA SER GLU LEU GLU ASN PHE MET GLY LEU ILE          
SEQRES  28 A  885  GLU VAL VAL THR GLY TYR VAL LYS ILE ARG HIS SER HIS          
SEQRES  29 A  885  ALA LEU VAL SER LEU SER PHE LEU LYS ASN LEU ARG LEU          
SEQRES  30 A  885  ILE LEU GLY GLU GLU GLN LEU GLU GLY ASN TYR SER PHE          
SEQRES  31 A  885  TYR VAL LEU ASP ASN GLN ASN LEU GLN GLN LEU TRP ASP          
SEQRES  32 A  885  TRP ASP HIS ARG ASN LEU THR ILE LYS ALA GLY LYS MET          
SEQRES  33 A  885  TYR PHE ALA PHE ASN PRO LYS LEU CYS VAL SER GLU ILE          
SEQRES  34 A  885  TYR ARG MET GLU GLU VAL THR GLY THR LYS GLY ARG GLN          
SEQRES  35 A  885  SER LYS GLY ASP ILE ASN THR ARG ASN ASN GLY GLU ARG          
SEQRES  36 A  885  ALA SER CYS GLU SER ASP VAL LEU HIS PHE THR SER THR          
SEQRES  37 A  885  THR THR SER LYS ASN ARG ILE ILE ILE THR TRP HIS ARG          
SEQRES  38 A  885  TYR ARG PRO PRO ASP TYR ARG ASP LEU ILE SER PHE THR          
SEQRES  39 A  885  VAL TYR TYR LYS GLU ALA PRO PHE LYS ASN VAL THR GLU          
SEQRES  40 A  885  TYR ASP GLY GLN ASP ALA CYS GLY SER ASN SER TRP ASN          
SEQRES  41 A  885  MET VAL ASP VAL ASP LEU PRO PRO ASN LYS ASP VAL GLU          
SEQRES  42 A  885  PRO GLY ILE LEU LEU HIS GLY LEU LYS PRO TRP THR GLN          
SEQRES  43 A  885  TYR ALA VAL TYR VAL LYS ALA VAL THR LEU THR MET VAL          
SEQRES  44 A  885  GLU ASN ASP HIS ILE ARG GLY ALA LYS SER GLU ILE LEU          
SEQRES  45 A  885  TYR ILE ARG THR ASN ALA SER VAL PRO SER ILE PRO LEU          
SEQRES  46 A  885  ASP VAL LEU SER ALA SER ASN SER SER SER GLN LEU ILE          
SEQRES  47 A  885  VAL LYS TRP ASN PRO PRO SER LEU PRO ASN GLY ASN LEU          
SEQRES  48 A  885  SER TYR TYR ILE VAL ARG TRP GLN ARG GLN PRO GLN ASP          
SEQRES  49 A  885  GLY TYR LEU TYR ARG HIS ASN TYR CYS SER LYS ASP LYS          
SEQRES  50 A  885  ILE PRO ILE ARG LYS TYR ALA ASP GLY THR ILE ASP ILE          
SEQRES  51 A  885  GLU GLU VAL THR GLU ASN PRO LYS THR GLU VAL CYS GLY          
SEQRES  52 A  885  GLY GLU LYS GLY PRO CYS CYS ALA CYS PRO LYS THR GLU          
SEQRES  53 A  885  ALA GLU LYS GLN ALA GLU LYS GLU GLU ALA GLU TYR ARG          
SEQRES  54 A  885  LYS VAL PHE GLU ASN PHE LEU HIS ASN SER ILE PHE VAL          
SEQRES  55 A  885  PRO ARG PRO GLU ARG LYS ARG ARG ASP VAL MET GLN VAL          
SEQRES  56 A  885  ALA ASN ALA GLY ASN ASN GLU THR GLU TYR PRO PHE PHE          
SEQRES  57 A  885  GLU SER ARG VAL ASP ASN LYS GLU ARG THR VAL ILE SER          
SEQRES  58 A  885  ASN LEU ARG PRO PHE THR LEU TYR ARG ILE ASP ILE HIS          
SEQRES  59 A  885  SER CYS ASN HIS GLU ALA GLU LYS LEU GLY CYS SER ALA          
SEQRES  60 A  885  SER ASN PHE VAL PHE ALA ARG THR MET PRO ALA GLU GLY          
SEQRES  61 A  885  ALA ASP ASP ILE PRO GLY PRO VAL THR TRP GLU PRO ARG          
SEQRES  62 A  885  PRO GLU ASN SER ILE PHE LEU LYS TRP PRO GLU PRO GLU          
SEQRES  63 A  885  ASN PRO ASN GLY LEU ILE LEU MET TYR GLU ILE LYS TYR          
SEQRES  64 A  885  GLY SER GLN VAL GLU ASP GLN ARG GLU CYS VAL SER ARG          
SEQRES  65 A  885  GLN GLU TYR ARG LYS TYR GLY GLY ALA LYS LEU ASN ARG          
SEQRES  66 A  885  LEU ASN PRO GLY ASN TYR THR ALA ARG ILE GLN ALA THR          
SEQRES  67 A  885  SER LEU SER GLY ASN GLY SER TRP THR ASP PRO VAL PHE          
SEQRES  68 A  885  PHE TYR VAL GLN ALA LYS THR GLY TYR GLU ASN PHE ILE          
SEQRES  69 A  885  HIS                                                          
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 H  126  GLY THR GLN VAL GLN LEU GLN GLN SER GLY PRO ASP VAL          
SEQRES   2 H  126  VAL ARG PRO GLY VAL SER VAL LYS ILE SER CYS LYS GLY          
SEQRES   3 H  126  SER GLY TYR THR PHE THR ASP TYR ALA ILE HIS TRP VAL          
SEQRES   4 H  126  LYS GLN SER HIS ALA LYS SER LEU GLU TRP ILE GLY VAL          
SEQRES   5 H  126  ILE SER THR TYR ASN GLY ASN THR LYS TYR ASN GLN LYS          
SEQRES   6 H  126  PHE LYS GLY LYS ALA ALA ILE THR VAL ASP LYS SER SER          
SEQRES   7 H  126  SER THR ALA TYR LEU GLU LEU ALA ARG LEU THR SER GLU          
SEQRES   8 H  126  ASP SER ALA ILE TYR TYR CYS ALA SER TYR GLY ASP LEU          
SEQRES   9 H  126  TYR VAL MET ASP TYR TRP GLY GLN GLY THR SER VAL THR          
SEQRES  10 H  126  VAL SER SER GLU ASN LEU TYR PHE GLN                          
SEQRES   1 L  108  GLY ASP ILE VAL LEU THR GLN SER PRO ALA THR LEU SER          
SEQRES   2 L  108  VAL THR PRO GLY ASP SER VAL SER LEU SER CYS ARG ALA          
SEQRES   3 L  108  SER GLN THR ILE SER ASN ASN LEU HIS TRP TYR GLN GLN          
SEQRES   4 L  108  LYS SER HIS GLU SER PRO ARG LEU LEU ILE LYS TYR ALA          
SEQRES   5 L  108  SER GLN SER ILE SER GLY ILE PRO SER ARG PHE SER GLY          
SEQRES   6 L  108  SER GLY SER GLY THR ASP PHE THR LEU SER ILE ASN SER          
SEQRES   7 L  108  VAL GLU THR GLU ASP PHE GLY MET TYR PHE CYS GLN GLN          
SEQRES   8 L  108  SER ASN SER TRP PRO ARG THR PHE GLY ALA GLY THR LYS          
SEQRES   9 L  108  LEU GLU LEU LYS                                              
HET    NAG  C   1      14                                                       
HET    NAG  C   2      14                                                       
HET    NAG  D   1      14                                                       
HET    NAG  D   2      14                                                       
HET    MAN  D   3      11                                                       
HET    MAN  D   4      11                                                       
HET    NAG  E   1      14                                                       
HET    NAG  E   2      14                                                       
HET    SO4  A1001       5                                                       
HET    SO4  A1002       5                                                       
HET    MLT  A1003       9                                                       
HET    NAG  A1004      14                                                       
HET    NAG  A1007      14                                                       
HET    NAG  A1012      14                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     MAN ALPHA-D-MANNOPYRANOSE                                            
HETNAM     SO4 SULFATE ION                                                      
HETNAM     MLT D-MALATE                                                         
HETSYN     MLT (2R)-2-HYDROXYBUTANEDIOIC ACID; 2-HYDROXY-SUCCINIC ACID          
FORMUL   5  NAG    9(C8 H15 N O6)                                               
FORMUL   6  MAN    2(C6 H12 O6)                                                 
FORMUL   8  SO4    2(O4 S 2-)                                                   
FORMUL  10  MLT    C4 H6 O5                                                     
HELIX    1 AA1 TYR A   13  GLU A   20  5                                   8    
HELIX    2 AA2 SER A   65  LEU A   69  5                                   5    
HELIX    3 AA3 PRO A  144  CYS A  148  5                                   5    
HELIX    4 AA4 ARG A  249  ALA A  253  1                                   5    
HELIX    5 AA5 THR A  315  GLN A  321  5                                   7    
HELIX    6 AA6 ILE A  340  MET A  348  1                                   9    
HELIX    7 AA7 GLY A  349  ILE A  351  5                                   3    
HELIX    8 AA8 CYS A  425  GLY A  437  1                                  13    
HELIX    9 AA9 ASP A  624  ARG A  629  5                                   6    
HELIX   10 AB1 LYS A  690  PHE A  701  1                                  12    
HELIX   11 AB2 ARG A  852  GLY A  859  1                                   8    
HELIX   12 AB3 GLY B    7  GLY B   19  1                                  13    
HELIX   13 AB4 ILE B   43  CYS B   48  1                                   6    
HELIX   14 AB5 ASP B   53  MET B   59  1                                   7    
HELIX   15 AB6 THR H   28  TYR H   32  5                                   5    
HELIX   16 AB7 GLN H   62  LYS H   65  5                                   4    
HELIX   17 AB8 THR H   87  SER H   91  5                                   5    
HELIX   18 AB9 LYS L   49  GLN L   53  5                                   5    
SHEET    1 AA1 5 ILE A   2  CYS A   3  0                                        
SHEET    2 AA1 5 VAL A  24  ILE A  25  1  O  VAL A  24   N  CYS A   3           
SHEET    3 AA1 5 VAL A  50  ILE A  51  1  O  VAL A  50   N  ILE A  25           
SHEET    4 AA1 5 VAL A  75  ILE A  76  1  O  VAL A  75   N  ILE A  51           
SHEET    5 AA1 5 ASN A 105  ILE A 106  1  O  ASN A 105   N  ILE A  76           
SHEET    1 AA2 6 ILE A   7  ARG A  10  0                                        
SHEET    2 AA2 6 LEU A  29  ILE A  34  1  O  HIS A  30   N  ILE A   9           
SHEET    3 AA2 6 LEU A  55  VAL A  60  1  O  LEU A  56   N  LEU A  29           
SHEET    4 AA2 6 TYR A  85  PHE A  90  1  O  VAL A  88   N  LEU A  57           
SHEET    5 AA2 6 ALA A 110  GLU A 114  1  O  ALA A 110   N  ALA A  86           
SHEET    6 AA2 6 TYR A 138  VAL A 140  1  O  TYR A 138   N  ILE A 113           
SHEET    1 AA3 2 LYS A 164  ILE A 167  0                                        
SHEET    2 AA3 2 GLU A 170  TYR A 173 -1  O  GLU A 170   N  ILE A 167           
SHEET    1 AA4 2 CYS A 205  CYS A 209  0                                        
SHEET    2 AA4 2 CYS A 218  CYS A 221 -1  O  ALA A 220   N  LEU A 206           
SHEET    1 AA5 2 TYR A 224  TYR A 226  0                                        
SHEET    2 AA5 2 VAL A 229  VAL A 231 -1  O  VAL A 229   N  TYR A 226           
SHEET    1 AA6 4 ARG A 245  ASP A 248  0                                        
SHEET    2 AA6 4 THR A 238  PHE A 241 -1  N  TYR A 239   O  VAL A 247           
SHEET    3 AA6 4 GLU A 272  MET A 274  1  O  CYS A 273   N  ARG A 240           
SHEET    4 AA6 4 VAL A 267  HIS A 269 -1  N  HIS A 269   O  GLU A 272           
SHEET    1 AA7 2 ILE A 282  ARG A 283  0                                        
SHEET    2 AA7 2 CYS A 291  ILE A 292 -1  O  ILE A 292   N  ILE A 282           
SHEET    1 AA8 4 CYS A 302  ILE A 311  0                                        
SHEET    2 AA8 4 ILE A 325  ILE A 332  1  O  LEU A 331   N  ILE A 311           
SHEET    3 AA8 4 VAL A 353  VAL A 354  1  O  VAL A 353   N  PHE A 326           
SHEET    4 AA8 4 LEU A 377  ILE A 378  1  O  LEU A 377   N  VAL A 354           
SHEET    1 AA9 5 CYS A 302  ILE A 311  0                                        
SHEET    2 AA9 5 ILE A 325  ILE A 332  1  O  LEU A 331   N  ILE A 311           
SHEET    3 AA9 5 VAL A 358  ARG A 361  1  O  LYS A 359   N  ILE A 332           
SHEET    4 AA9 5 TYR A 388  LEU A 393  1  O  SER A 389   N  VAL A 358           
SHEET    5 AA9 5 LYS A 415  ALA A 419  1  O  TYR A 417   N  VAL A 392           
SHEET    1 AB1 2 ASP A 461  LEU A 463  0                                        
SHEET    2 AB1 2 ALA A 567  SER A 569  1  O  LYS A 568   N  ASP A 461           
SHEET    1 AB2 3 PHE A 465  THR A 470  0                                        
SHEET    2 AB2 3 ILE A 475  TRP A 479 -1  O  THR A 478   N  THR A 466           
SHEET    3 AB2 3 GLY A 535  LEU A 538 -1  O  LEU A 538   N  ILE A 475           
SHEET    1 AB3 4 ASN A 520  VAL A 522  0                                        
SHEET    2 AB3 4 LEU A 490  GLU A 499 -1  N  VAL A 495   O  VAL A 522           
SHEET    3 AB3 4 GLN A 546  LEU A 556 -1  O  VAL A 554   N  SER A 492           
SHEET    4 AB3 4 LEU A 572  ARG A 575 -1  O  ILE A 574   N  TYR A 547           
SHEET    1 AB4 3 LEU A 585  ALA A 590  0                                        
SHEET    2 AB4 3 GLN A 596  ASN A 602 -1  O  ASN A 602   N  LEU A 585           
SHEET    3 AB4 3 ARG A 757  SER A 761 -1  O  ILE A 760   N  LEU A 597           
SHEET    1 AB5 4 PHE A 747  VAL A 752  0                                        
SHEET    2 AB5 4 LEU A 611  ARG A 620 -1  N  TYR A 614   O  VAL A 752           
SHEET    3 AB5 4 LEU A 768  ASN A 777 -1  O  ASP A 772   N  ARG A 617           
SHEET    4 AB5 4 VAL A 791  ARG A 794 -1  O  VAL A 791   N  ILE A 771           
SHEET    1 AB6 3 THR A 809  ARG A 813  0                                        
SHEET    2 AB6 3 SER A 817  LYS A 821 -1  O  LYS A 821   N  THR A 809           
SHEET    3 AB6 3 GLY A 860  LEU A 863 -1  O  LEU A 863   N  ILE A 818           
SHEET    1 AB7 4 GLN A 846  SER A 851  0                                        
SHEET    2 AB7 4 ILE A 832  GLY A 840 -1  N  TYR A 835   O  VAL A 850           
SHEET    3 AB7 4 GLY A 869  SER A 879 -1  O  ARG A 874   N  LYS A 838           
SHEET    4 AB7 4 VAL A 890  VAL A 894 -1  O  VAL A 890   N  ALA A 873           
SHEET    1 AB8 4 GLN H   3  GLN H   6  0                                        
SHEET    2 AB8 4 VAL H  18  SER H  25 -1  O  LYS H  23   N  GLN H   5           
SHEET    3 AB8 4 THR H  78  LEU H  83 -1  O  LEU H  83   N  VAL H  18           
SHEET    4 AB8 4 ALA H  68  ASP H  73 -1  N  ALA H  69   O  GLU H  82           
SHEET    1 AB9 6 ASP H  10  VAL H  12  0                                        
SHEET    2 AB9 6 THR H 112  VAL H 116  1  O  SER H 113   N  ASP H  10           
SHEET    3 AB9 6 ILE H  93  SER H  98 -1  N  TYR H  94   O  THR H 112           
SHEET    4 AB9 6 ILE H  34  GLN H  39 -1  N  HIS H  35   O  ALA H  97           
SHEET    5 AB9 6 GLU H  46  ILE H  51 -1  O  GLU H  46   N  LYS H  38           
SHEET    6 AB9 6 THR H  58  TYR H  60 -1  O  LYS H  59   N  VAL H  50           
SHEET    1 AC1 4 ASP H  10  VAL H  12  0                                        
SHEET    2 AC1 4 THR H 112  VAL H 116  1  O  SER H 113   N  ASP H  10           
SHEET    3 AC1 4 ILE H  93  SER H  98 -1  N  TYR H  94   O  THR H 112           
SHEET    4 AC1 4 TYR H 107  TRP H 108 -1  O  TYR H 107   N  SER H  98           
SHEET    1 AC2 3 LEU L   4  THR L   5  0                                        
SHEET    2 AC2 3 VAL L  19  ILE L  29 -1  O  ARG L  24   N  THR L   5           
SHEET    3 AC2 3 PHE L  62  ILE L  75 -1  O  LEU L  73   N  LEU L  21           
SHEET    1 AC3 5 THR L  10  VAL L  13  0                                        
SHEET    2 AC3 5 THR L 102  LEU L 106  1  O  GLU L 105   N  VAL L  13           
SHEET    3 AC3 5 MET L  85  GLN L  90 -1  N  TYR L  86   O  THR L 102           
SHEET    4 AC3 5 LEU L  33  GLN L  38 -1  N  HIS L  34   O  GLN L  89           
SHEET    5 AC3 5 ARG L  45  ILE L  48 -1  O  ARG L  45   N  GLN L  37           
SHEET    1 AC4 4 THR L  10  VAL L  13  0                                        
SHEET    2 AC4 4 THR L 102  LEU L 106  1  O  GLU L 105   N  VAL L  13           
SHEET    3 AC4 4 MET L  85  GLN L  90 -1  N  TYR L  86   O  THR L 102           
SHEET    4 AC4 4 THR L  97  PHE L  98 -1  O  THR L  97   N  GLN L  90           
SSBOND   1 CYS A    3    CYS A   22                          1555   1555  2.03  
SSBOND   2 CYS A  120    CYS A  148                          1555   1555  2.03  
SSBOND   3 CYS A  152    CYS A  175                          1555   1555  2.03  
SSBOND   4 CYS A  162    CYS A  181                          1555   1555  2.03  
SSBOND   5 CYS A  185    CYS A  194                          1555   1555  2.03  
SSBOND   6 CYS A  189    CYS A  200                          1555   1555  2.03  
SSBOND   7 CYS A  201    CYS A  209                          1555   1555  2.03  
SSBOND   8 CYS A  205    CYS A  218                          1555   1555  2.03  
SSBOND   9 CYS A  221    CYS A  230                          1555   1555  2.03  
SSBOND  10 CYS A  234    CYS A  246                          1555   1555  2.03  
SSBOND  11 CYS A  252    CYS A  273                          1555   1555  2.03  
SSBOND  12 CYS A  277    CYS A  291                          1555   1555  2.03  
SSBOND  13 CYS A  294    CYS A  298                          1555   1555  2.03  
SSBOND  14 CYS A  302    CYS A  323                          1555   1555  2.03  
SSBOND  15 CYS A  425    CYS A  458                          1555   1555  2.03  
SSBOND  16 CYS A  514    CYS A  514                          1555   2555  2.03  
SSBOND  17 CYS A  633    CYS A  849                          1555   1555  2.03  
SSBOND  18 CYS A  776    CYS A  785                          1555   1555  2.04  
SSBOND  19 CYS B    6    CYS B   48                          1555   1555  2.03  
SSBOND  20 CYS B   18    CYS B   61                          1555   1555  2.03  
SSBOND  21 CYS B   47    CYS B   52                          1555   1555  2.03  
SSBOND  22 CYS H   22    CYS H   96                          1555   1555  2.03  
SSBOND  23 CYS L   23    CYS L   88                          1555   1555  2.03  
LINK         ND2 ASN A  21                 C1  NAG A1004     1555   1555  1.44  
LINK         ND2 ASN A 105                 C1  NAG C   1     1555   1555  1.44  
LINK         ND2 ASN A 504                 C1  NAG A1007     1555   1555  1.44  
LINK         ND2 ASN A 577                 C1  NAG D   1     1555   1555  1.44  
LINK         ND2 ASN A 870                 C1  NAG A1012     1555   1555  1.44  
LINK         ND2 ASN A 883                 C1  NAG E   1     1555   1555  1.44  
LINK         O4  NAG C   1                 C1  NAG C   2     1555   1555  1.44  
LINK         O4  NAG D   1                 C1  NAG D   2     1555   1555  1.44  
LINK         O4  NAG D   2                 C1  MAN D   3     1555   1555  1.44  
LINK         O4  MAN D   3                 C1  MAN D   4     1555   1555  1.45  
LINK         O4  NAG E   1                 C1  NAG E   2     1555   1555  1.44  
CISPEP   1 GLY A    4    PRO A    5          0        -0.32                     
CISPEP   2 TRP L   94    PRO L   95          0        -1.43                     
CRYST1   88.690  197.660  117.650  90.00  90.00  90.00 P 21 21 2     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      0.011275  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005059  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008500        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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