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Database: PDB
Entry: 3U88
LinkDB: 3U88
Original site: 3U88 
HEADER    TRANSCRIPTION                           16-OCT-11   3U88              
TITLE     CRYSTAL STRUCTURE OF HUMAN MENIN IN COMPLEX WITH MLL1 AND LEDGF       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MENIN;                                                     
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE 2A;                     
COMPND   7 CHAIN: M, N;                                                         
COMPND   8 SYNONYM: LYSINE N-METHYLTRANSFERASE 2A,ALL-1,CXXC-TYPE ZINC FINGER   
COMPND   9 PROTEIN 7,MYELOID/LYMPHOID OR MIXED-LINEAGE LEUKEMIA,MYELOID/LYMPHOID
COMPND  10 OR MIXED-LINEAGE LEUKEMIA PROTEIN 1,TRITHORAX-LIKE PROTEIN,ZINC      
COMPND  11 FINGER PROTEIN HRX;                                                  
COMPND  12 EC: 2.1.1.43;                                                        
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 MOL_ID: 3;                                                           
COMPND  15 MOLECULE: LENS EPITHELIUM-DERIVED GROWTH FACTOR;                     
COMPND  16 CHAIN: C, D;                                                         
COMPND  17 SYNONYM: CLL-ASSOCIATED ANTIGEN KW-7,DENSE FINE SPECKLES 70 KDA      
COMPND  18 PROTEIN,DFS 70,TRANSCRIPTIONAL COACTIVATOR P75/P52;                  
COMPND  19 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: MEN1, SCG2;                                                    
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606;                                                
SOURCE  14 GENE: KMT2A, ALL1, CXXC7, HRX, HTRX, MLL, MLL1, TRX1;                
SOURCE  15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  17 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  18 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  19 MOL_ID: 3;                                                           
SOURCE  20 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  21 ORGANISM_COMMON: HUMAN;                                              
SOURCE  22 ORGANISM_TAXID: 9606;                                                
SOURCE  23 GENE: PSIP1, DFS70, LEDGF, PSIP2;                                    
SOURCE  24 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  25 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  26 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  27 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID                               
KEYWDS    MENIN, MEN1, MLL, JUND, LEDGF, TPR, TRANSCRIPTION                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.HUANG,B.WAN,M.LEI                                                   
REVDAT   3   21-JUN-17 3U88    1       DBREF                                    
REVDAT   2   07-MAR-12 3U88    1       JRNL                                     
REVDAT   1   15-FEB-12 3U88    0                                                
JRNL        AUTH   J.HUANG,B.GURUNG,B.WAN,S.MATKAR,N.A.VENIAMINOVA,K.WAN,       
JRNL        AUTH 2 J.L.MERCHANT,X.HUA,M.LEI                                     
JRNL        TITL   THE SAME POCKET IN MENIN BINDS BOTH MLL AND JUND BUT HAS     
JRNL        TITL 2 OPPOSITE EFFECTS ON TRANSCRIPTION.                           
JRNL        REF    NATURE                        V. 482   542 2012              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   22327296                                                     
JRNL        DOI    10.1038/NATURE10806                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.7_650                                       
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 : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.65                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 50106                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.205                           
REMARK   3   R VALUE            (WORKING SET) : 0.202                           
REMARK   3   FREE R VALUE                     : 0.233                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.070                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 5048                            
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 48.6608 -  9.3036    0.99     1676   188  0.2294 0.2177        
REMARK   3     2  9.3036 -  7.3929    1.00     1599   151  0.1652 0.1976        
REMARK   3     3  7.3929 -  6.4608    1.00     1545   174  0.1981 0.2160        
REMARK   3     4  6.4608 -  5.8712    1.00     1544   162  0.2281 0.2816        
REMARK   3     5  5.8712 -  5.4510    1.00     1511   189  0.2268 0.2597        
REMARK   3     6  5.4510 -  5.1300    1.00     1501   186  0.2247 0.2247        
REMARK   3     7  5.1300 -  4.8733    1.00     1548   145  0.1992 0.2259        
REMARK   3     8  4.8733 -  4.6613    1.00     1518   155  0.1761 0.1922        
REMARK   3     9  4.6613 -  4.4820    1.00     1492   180  0.1578 0.1830        
REMARK   3    10  4.4820 -  4.3275    1.00     1474   205  0.1658 0.2009        
REMARK   3    11  4.3275 -  4.1922    1.00     1472   197  0.1695 0.1946        
REMARK   3    12  4.1922 -  4.0725    1.00     1504   156  0.1765 0.2000        
REMARK   3    13  4.0725 -  3.9653    1.00     1482   180  0.1914 0.2292        
REMARK   3    14  3.9653 -  3.8686    1.00     1510   158  0.1835 0.2270        
REMARK   3    15  3.8686 -  3.7807    1.00     1479   170  0.1959 0.2410        
REMARK   3    16  3.7807 -  3.7003    1.00     1501   151  0.2090 0.2373        
REMARK   3    17  3.7003 -  3.6263    1.00     1472   179  0.2042 0.2558        
REMARK   3    18  3.6263 -  3.5579    1.00     1503   157  0.2088 0.2693        
REMARK   3    19  3.5579 -  3.4943    1.00     1477   174  0.2201 0.2458        
REMARK   3    20  3.4943 -  3.4351    1.00     1481   172  0.2019 0.2422        
REMARK   3    21  3.4351 -  3.3797    1.00     1481   171  0.2240 0.2851        
REMARK   3    22  3.3797 -  3.3277    1.00     1478   164  0.2135 0.2599        
REMARK   3    23  3.3277 -  3.2788    1.00     1498   158  0.2199 0.2542        
REMARK   3    24  3.2788 -  3.2326    1.00     1479   158  0.2324 0.3137        
REMARK   3    25  3.2326 -  3.1889    1.00     1454   179  0.2341 0.3261        
REMARK   3    26  3.1889 -  3.1475    1.00     1502   163  0.2233 0.2656        
REMARK   3    27  3.1475 -  3.1082    1.00     1501   132  0.2286 0.2499        
REMARK   3    28  3.1082 -  3.0708    1.00     1457   175  0.2381 0.2595        
REMARK   3    29  3.0708 -  3.0351    1.00     1459   172  0.2586 0.3503        
REMARK   3    30  3.0351 -  3.0010    0.96     1460   147  0.2915 0.3504        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.10                                          
REMARK   3   SHRINKAGE RADIUS   : 0.83                                          
REMARK   3   K_SOL              : 0.34                                          
REMARK   3   B_SOL              : 49.05                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.420            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.260           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 75.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 77.45                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.38080                                             
REMARK   3    B22 (A**2) : -1.38080                                             
REMARK   3    B33 (A**2) : 2.76160                                              
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  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      :  0.006          10039                                  
REMARK   3   ANGLE     :  1.093          13600                                  
REMARK   3   CHIRALITY :  0.070           1521                                  
REMARK   3   PLANARITY :  0.004           1727                                  
REMARK   3   DIHEDRAL  : 17.493           3680                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
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 3U88 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-OCT-11.                  
REMARK 100 THE DEPOSITION ID IS D_1000068429.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-MAR-11                          
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               : APS                                
REMARK 200  BEAMLINE                       : 21-ID-D                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97872                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 100.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 12.30                              
REMARK 200  R MERGE                    (I) : 0.11300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 22.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 67.96                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.84                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6 M AMMONIUM SULFATE, PH 7.0, VAPOR    
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 277K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
REMARK 290       7555   Y,X,-Z+1/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+2/3                                          
REMARK 290      10555   -Y,-X,-Z+5/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+1/6                                            
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       79.47233            
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      158.94467            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      119.20850            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      198.68083            
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       39.73617            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       79.47233            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000      158.94467            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000      198.68083            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000      119.20850            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       39.73617            
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: 6640 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 26520 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, M, 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 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6390 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 26260 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -38.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, N, D                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER A     1                                                      
REMARK 465     PRO A    71                                                      
REMARK 465     PRO A    72                                                      
REMARK 465     GLY A   386                                                      
REMARK 465     GLU A   387                                                      
REMARK 465     GLU A   388                                                      
REMARK 465     ARG A   389                                                      
REMARK 465     PRO A   390                                                      
REMARK 465     GLY A   391                                                      
REMARK 465     GLU A   392                                                      
REMARK 465     GLN A   393                                                      
REMARK 465     SER A   394                                                      
REMARK 465     GLN A   395                                                      
REMARK 465     GLY A   396                                                      
REMARK 465     THR A   397                                                      
REMARK 465     GLN A   398                                                      
REMARK 465     SER A   399                                                      
REMARK 465     GLN A   400                                                      
REMARK 465     GLY A   401                                                      
REMARK 465     GLY A   520                                                      
REMARK 465     THR A   521                                                      
REMARK 465     VAL A   522                                                      
REMARK 465     ALA A   523                                                      
REMARK 465     GLY A   524                                                      
REMARK 465     THR A   525                                                      
REMARK 465     ALA A   526                                                      
REMARK 465     ARG A   527                                                      
REMARK 465     GLY A   528                                                      
REMARK 465     PRO A   529                                                      
REMARK 465     GLU A   530                                                      
REMARK 465     GLY A   531                                                      
REMARK 465     GLY A   532                                                      
REMARK 465     SER A   533                                                      
REMARK 465     THR A   534                                                      
REMARK 465     ALA A   535                                                      
REMARK 465     GLN A   536                                                      
REMARK 465     VAL A   537                                                      
REMARK 465     PRO A   538                                                      
REMARK 465     ALA A   539                                                      
REMARK 465     PRO A   540                                                      
REMARK 465     THR A   541                                                      
REMARK 465     ALA A   542                                                      
REMARK 465     SER A   543                                                      
REMARK 465     PRO A   544                                                      
REMARK 465     PRO A   545                                                      
REMARK 465     PRO A   546                                                      
REMARK 465     GLN A   584                                                      
REMARK 465     VAL A   585                                                      
REMARK 465     GLN A   586                                                      
REMARK 465     MET A   587                                                      
REMARK 465     LYS A   588                                                      
REMARK 465     LYS A   589                                                      
REMARK 465     GLN A   590                                                      
REMARK 465     LYS A   591                                                      
REMARK 465     VAL A   592                                                      
REMARK 465     SER A   593                                                      
REMARK 465     THR A   594                                                      
REMARK 465     PRO A   595                                                      
REMARK 465     SER A   596                                                      
REMARK 465     ASP A   597                                                      
REMARK 465     TYR A   598                                                      
REMARK 465     THR A   599                                                      
REMARK 465     LEU A   600                                                      
REMARK 465     SER A   601                                                      
REMARK 465     PHE A   602                                                      
REMARK 465     LEU A   603                                                      
REMARK 465     LYS A   604                                                      
REMARK 465     ARG A   605                                                      
REMARK 465     GLN A   606                                                      
REMARK 465     ARG A   607                                                      
REMARK 465     LYS A   608                                                      
REMARK 465     GLY A   609                                                      
REMARK 465     LEU A   610                                                      
REMARK 465     SER B     1                                                      
REMARK 465     GLU B   387                                                      
REMARK 465     GLU B   388                                                      
REMARK 465     ARG B   389                                                      
REMARK 465     PRO B   390                                                      
REMARK 465     GLY B   391                                                      
REMARK 465     GLU B   392                                                      
REMARK 465     GLN B   393                                                      
REMARK 465     SER B   394                                                      
REMARK 465     GLN B   395                                                      
REMARK 465     GLY B   396                                                      
REMARK 465     THR B   397                                                      
REMARK 465     GLN B   398                                                      
REMARK 465     SER B   399                                                      
REMARK 465     THR B   521                                                      
REMARK 465     VAL B   522                                                      
REMARK 465     ALA B   523                                                      
REMARK 465     GLY B   524                                                      
REMARK 465     THR B   525                                                      
REMARK 465     ALA B   526                                                      
REMARK 465     ARG B   527                                                      
REMARK 465     GLY B   528                                                      
REMARK 465     PRO B   529                                                      
REMARK 465     GLU B   530                                                      
REMARK 465     GLY B   531                                                      
REMARK 465     GLY B   532                                                      
REMARK 465     SER B   533                                                      
REMARK 465     THR B   534                                                      
REMARK 465     ALA B   535                                                      
REMARK 465     GLN B   536                                                      
REMARK 465     VAL B   537                                                      
REMARK 465     PRO B   538                                                      
REMARK 465     ALA B   539                                                      
REMARK 465     PRO B   540                                                      
REMARK 465     THR B   541                                                      
REMARK 465     ALA B   542                                                      
REMARK 465     SER B   543                                                      
REMARK 465     SER B   583                                                      
REMARK 465     GLN B   584                                                      
REMARK 465     VAL B   585                                                      
REMARK 465     GLN B   586                                                      
REMARK 465     MET B   587                                                      
REMARK 465     LYS B   588                                                      
REMARK 465     LYS B   589                                                      
REMARK 465     GLN B   590                                                      
REMARK 465     LYS B   591                                                      
REMARK 465     VAL B   592                                                      
REMARK 465     SER B   593                                                      
REMARK 465     THR B   594                                                      
REMARK 465     PRO B   595                                                      
REMARK 465     SER B   596                                                      
REMARK 465     ASP B   597                                                      
REMARK 465     TYR B   598                                                      
REMARK 465     THR B   599                                                      
REMARK 465     LEU B   600                                                      
REMARK 465     SER B   601                                                      
REMARK 465     PHE B   602                                                      
REMARK 465     LEU B   603                                                      
REMARK 465     LYS B   604                                                      
REMARK 465     ARG B   605                                                      
REMARK 465     GLN B   606                                                      
REMARK 465     ARG B   607                                                      
REMARK 465     LYS B   608                                                      
REMARK 465     GLY B   609                                                      
REMARK 465     LEU B   610                                                      
REMARK 465     SER M     5                                                      
REMARK 465     SER M   136                                                      
REMARK 465     GLY M   137                                                      
REMARK 465     GLY M   138                                                      
REMARK 465     GLY M   139                                                      
REMARK 465     GLY M   140                                                      
REMARK 465     GLY M   141                                                      
REMARK 465     SER M   142                                                      
REMARK 465     GLY M   143                                                      
REMARK 465     GLU M   144                                                      
REMARK 465     ASP M   145                                                      
REMARK 465     GLU M   146                                                      
REMARK 465     GLN M   147                                                      
REMARK 465     PHE M   148                                                      
REMARK 465     LEU M   149                                                      
REMARK 465     GLY M   150                                                      
REMARK 465     PHE M   151                                                      
REMARK 465     GLY M   152                                                      
REMARK 465     SER M   153                                                      
REMARK 465     SER C   347                                                      
REMARK 465     GLY C   430                                                      
REMARK 465     GLU C   431                                                      
REMARK 465     GLY C   432                                                      
REMARK 465     ASP C   433                                                      
REMARK 465     SER C   434                                                      
REMARK 465     VAL C   435                                                      
REMARK 465     SER N     5                                                      
REMARK 465     GLU N   135                                                      
REMARK 465     SER N   136                                                      
REMARK 465     GLY N   137                                                      
REMARK 465     GLY N   138                                                      
REMARK 465     GLY N   139                                                      
REMARK 465     GLY N   140                                                      
REMARK 465     GLY N   141                                                      
REMARK 465     SER N   142                                                      
REMARK 465     GLY N   143                                                      
REMARK 465     GLU N   144                                                      
REMARK 465     ASP N   145                                                      
REMARK 465     GLU N   146                                                      
REMARK 465     GLN N   147                                                      
REMARK 465     PHE N   148                                                      
REMARK 465     LEU N   149                                                      
REMARK 465     GLY N   150                                                      
REMARK 465     PHE N   151                                                      
REMARK 465     GLY N   152                                                      
REMARK 465     SER N   153                                                      
REMARK 465     SER D   347                                                      
REMARK 465     MET D   348                                                      
REMARK 465     ASP D   349                                                      
REMARK 465     SER D   350                                                      
REMARK 465     ARG D   351                                                      
REMARK 465     LEU D   352                                                      
REMARK 465     LYS D   364                                                      
REMARK 465     ILE D   365                                                      
REMARK 465     ASP D   366                                                      
REMARK 465     ASN D   367                                                      
REMARK 465     LEU D   368                                                      
REMARK 465     ASP D   369                                                      
REMARK 465     ARG D   405                                                      
REMARK 465     PHE D   406                                                      
REMARK 465     LYS D   407                                                      
REMARK 465     VAL D   408                                                      
REMARK 465     SER D   409                                                      
REMARK 465     GLU D   431                                                      
REMARK 465     GLY D   432                                                      
REMARK 465     ASP D   433                                                      
REMARK 465     SER D   434                                                      
REMARK 465     VAL D   435                                                      
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     GLN A 582    CG   CD   OE1  NE2                                  
REMARK 470     SER A 583    OG                                                  
REMARK 470     ASP B  70    CG   OD1  OD2                                       
REMARK 470     GLN B 400    CG   CD   OE1  NE2                                  
REMARK 470     GLN B 582    CG   CD   OE1  NE2                                  
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     LYS C  360   NZ                                                  
REMARK 480     MET C  387   CG   SD   CE                                        
REMARK 480     GLN C  388   CG   CD   OE1  NE2                                  
REMARK 480     GLN C  391   CG   CD   OE1  NE2                                  
REMARK 480     ARG C  405   CZ   NH1  NH2                                       
REMARK 480     GLN C  410   CD   OE1  NE2                                       
REMARK 480     LYS D  360   NZ                                                  
REMARK 480     MET D  387   CG   SD   CE                                        
REMARK 480     GLN D  388   CG   CD   OE1  NE2                                  
REMARK 480     GLN D  391   CG   CD   OE1  NE2                                  
REMARK 480     GLN D  410   CD   OE1  NE2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   NH1  ARG N   130     O3   SO4 N   154              2.07            
REMARK 500   O    SER B   130     OAA  0BR B   612              2.11            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ALA A  49      -39.17   -134.38                                   
REMARK 500    ARG A  52       42.07    -85.09                                   
REMARK 500    SER A  66      142.40   -173.79                                   
REMARK 500    TYR A 106       75.01   -116.93                                   
REMARK 500    ASP A 180       14.25   -151.68                                   
REMARK 500    LYS A 224       17.55     57.01                                   
REMARK 500    ASP A 248     -164.42   -164.59                                   
REMARK 500    ASP A 370      -63.12   -135.79                                   
REMARK 500    VAL A 431      -65.72   -123.41                                   
REMARK 500    VAL A 458     -160.55   -102.39                                   
REMARK 500    ALA A 581      106.71    -57.45                                   
REMARK 500    ALA B  49      -30.86   -133.51                                   
REMARK 500    ARG B  52       43.30    -84.75                                   
REMARK 500    ASN B  57      -73.56    -97.31                                   
REMARK 500    PRO B  71      171.26    -50.43                                   
REMARK 500    ARG B 171       -8.82    -58.17                                   
REMARK 500    SER B 178     -153.55   -111.84                                   
REMARK 500    TRP B 183     -159.63   -156.98                                   
REMARK 500    LYS B 201       36.77    -86.63                                   
REMARK 500    LEU B 223       29.26     49.69                                   
REMARK 500    SER B 226       47.25    -84.39                                   
REMARK 500    PRO B 296      152.76    -48.49                                   
REMARK 500    ASP B 370      -56.69   -142.59                                   
REMARK 500    VAL B 431      -54.95   -129.01                                   
REMARK 500    GLU B 547       53.34   -116.23                                   
REMARK 500    ALA M  11       34.12     71.66                                   
REMARK 500    SER C 382       46.10   -104.35                                   
REMARK 500    LYS C 407       22.70    -72.20                                   
REMARK 500    LEU C 428       42.71    -89.67                                   
REMARK 500    PHE N 133      -70.16   -106.24                                   
REMARK 500    MET D 387      -72.67    -62.22                                   
REMARK 500    HIS D 393       56.08    -95.85                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CHD A 611                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CHD B 611                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0BR B 612                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GGB A 613                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0BR A 612                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GGB B 615                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GGB A 614                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLV A 615                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLV A 616                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLV A 617                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLV B 616                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 N 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 M 2                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 618                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 619                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 617                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GGB C 108                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 618                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GGB C 109                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLV C 113                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLV D 114                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 N 154                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 M 154                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3U84   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3U85   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3U86   RELATED DB: PDB                                   
DBREF  3U88 A    2   459  UNP    O00255   MEN1_HUMAN       2    459             
DBREF  3U88 A  520   610  UNP    O00255   MEN1_HUMAN     520    610             
DBREF  3U88 B    2   459  UNP    O00255   MEN1_HUMAN       2    459             
DBREF  3U88 B  520   610  UNP    O00255   MEN1_HUMAN     520    610             
DBREF  3U88 M   36   153  UNP    Q03164   KMT2A_HUMAN    103    153             
DBREF  3U88 C  347   435  UNP    O75475   PSIP1_HUMAN    347    435             
DBREF  3U88 N   36   153  UNP    Q03164   KMT2A_HUMAN    103    153             
DBREF  3U88 D  347   435  UNP    O75475   PSIP1_HUMAN    347    435             
SEQADV 3U88 SER A    1  UNP  O00255              EXPRESSION TAG                 
SEQADV 3U88 SER B    1  UNP  O00255              EXPRESSION TAG                 
SEQADV 3U88 SER M    5  UNP  Q03164              EXPRESSION TAG                 
SEQADV 3U88 ARG M    6  UNP  Q03164              EXPRESSION TAG                 
SEQADV 3U88 TRP M    7  UNP  Q03164              EXPRESSION TAG                 
SEQADV 3U88 ARG M    8  UNP  Q03164              EXPRESSION TAG                 
SEQADV 3U88 PHE M    9  UNP  Q03164              EXPRESSION TAG                 
SEQADV 3U88 PRO M   10  UNP  Q03164              EXPRESSION TAG                 
SEQADV 3U88 ALA M   11  UNP  Q03164              EXPRESSION TAG                 
SEQADV 3U88 ARG M   12  UNP  Q03164              EXPRESSION TAG                 
SEQADV 3U88 PRO M   13  UNP  Q03164              EXPRESSION TAG                 
SEQADV 3U88 GLY M   14  UNP  Q03164              EXPRESSION TAG                 
SEQADV 3U88 THR M   15  UNP  Q03164              EXPRESSION TAG                 
SEQADV 3U88 GLY M   23  UNP  Q03164              EXPRESSION TAG                 
SEQADV 3U88 ARG M   24  UNP  Q03164              EXPRESSION TAG                 
SEQADV 3U88 ARG M   25  UNP  Q03164              EXPRESSION TAG                 
SEQADV 3U88 GLY M   26  UNP  Q03164              EXPRESSION TAG                 
SEQADV 3U88 LEU M   27  UNP  Q03164              EXPRESSION TAG                 
SEQADV 3U88 GLY M   28  UNP  Q03164              EXPRESSION TAG                 
SEQADV 3U88 GLY M   29  UNP  Q03164              EXPRESSION TAG                 
SEQADV 3U88 ALA M   30  UNP  Q03164              EXPRESSION TAG                 
SEQADV 3U88 PRO M   31  UNP  Q03164              EXPRESSION TAG                 
SEQADV 3U88 ARG M   32  UNP  Q03164              EXPRESSION TAG                 
SEQADV 3U88 GLN M   33  UNP  Q03164              EXPRESSION TAG                 
SEQADV 3U88 ARG M   34  UNP  Q03164              EXPRESSION TAG                 
SEQADV 3U88 VAL M   35  UNP  Q03164              EXPRESSION TAG                 
SEQADV 3U88 SER N    5  UNP  Q03164              EXPRESSION TAG                 
SEQADV 3U88 ARG N    6  UNP  Q03164              EXPRESSION TAG                 
SEQADV 3U88 TRP N    7  UNP  Q03164              EXPRESSION TAG                 
SEQADV 3U88 ARG N    8  UNP  Q03164              EXPRESSION TAG                 
SEQADV 3U88 PHE N    9  UNP  Q03164              EXPRESSION TAG                 
SEQADV 3U88 PRO N   10  UNP  Q03164              EXPRESSION TAG                 
SEQADV 3U88 ALA N   11  UNP  Q03164              EXPRESSION TAG                 
SEQADV 3U88 ARG N   12  UNP  Q03164              EXPRESSION TAG                 
SEQADV 3U88 PRO N   13  UNP  Q03164              EXPRESSION TAG                 
SEQADV 3U88 GLY N   14  UNP  Q03164              EXPRESSION TAG                 
SEQADV 3U88 THR N   15  UNP  Q03164              EXPRESSION TAG                 
SEQADV 3U88 GLY N   23  UNP  Q03164              EXPRESSION TAG                 
SEQADV 3U88 ARG N   24  UNP  Q03164              EXPRESSION TAG                 
SEQADV 3U88 ARG N   25  UNP  Q03164              EXPRESSION TAG                 
SEQADV 3U88 GLY N   26  UNP  Q03164              EXPRESSION TAG                 
SEQADV 3U88 LEU N   27  UNP  Q03164              EXPRESSION TAG                 
SEQADV 3U88 GLY N   28  UNP  Q03164              EXPRESSION TAG                 
SEQADV 3U88 GLY N   29  UNP  Q03164              EXPRESSION TAG                 
SEQADV 3U88 ALA N   30  UNP  Q03164              EXPRESSION TAG                 
SEQADV 3U88 PRO N   31  UNP  Q03164              EXPRESSION TAG                 
SEQADV 3U88 ARG N   32  UNP  Q03164              EXPRESSION TAG                 
SEQADV 3U88 GLN N   33  UNP  Q03164              EXPRESSION TAG                 
SEQADV 3U88 ARG N   34  UNP  Q03164              EXPRESSION TAG                 
SEQADV 3U88 VAL N   35  UNP  Q03164              EXPRESSION TAG                 
SEQRES   1 A  550  SER GLY LEU LYS ALA ALA GLN LYS THR LEU PHE PRO LEU          
SEQRES   2 A  550  ARG SER ILE ASP ASP VAL VAL ARG LEU PHE ALA ALA GLU          
SEQRES   3 A  550  LEU GLY ARG GLU GLU PRO ASP LEU VAL LEU LEU SER LEU          
SEQRES   4 A  550  VAL LEU GLY PHE VAL GLU HIS PHE LEU ALA VAL ASN ARG          
SEQRES   5 A  550  VAL ILE PRO THR ASN VAL PRO GLU LEU THR PHE GLN PRO          
SEQRES   6 A  550  SER PRO ALA PRO ASP PRO PRO GLY GLY LEU THR TYR PHE          
SEQRES   7 A  550  PRO VAL ALA ASP LEU SER ILE ILE ALA ALA LEU TYR ALA          
SEQRES   8 A  550  ARG PHE THR ALA GLN ILE ARG GLY ALA VAL ASP LEU SER          
SEQRES   9 A  550  LEU TYR PRO ARG GLU GLY GLY VAL SER SER ARG GLU LEU          
SEQRES  10 A  550  VAL LYS LYS VAL SER ASP VAL ILE TRP ASN SER LEU SER          
SEQRES  11 A  550  ARG SER TYR PHE LYS ASP ARG ALA HIS ILE GLN SER LEU          
SEQRES  12 A  550  PHE SER PHE ILE THR GLY THR LYS LEU ASP SER SER GLY          
SEQRES  13 A  550  VAL ALA PHE ALA VAL VAL GLY ALA CYS GLN ALA LEU GLY          
SEQRES  14 A  550  LEU ARG ASP VAL HIS LEU ALA LEU SER GLU ASP HIS ALA          
SEQRES  15 A  550  TRP VAL VAL PHE GLY PRO ASN GLY GLU GLN THR ALA GLU          
SEQRES  16 A  550  VAL THR TRP HIS GLY LYS GLY ASN GLU ASP ARG ARG GLY          
SEQRES  17 A  550  GLN THR VAL ASN ALA GLY VAL ALA GLU ARG SER TRP LEU          
SEQRES  18 A  550  TYR LEU LYS GLY SER TYR MET ARG CYS ASP ARG LYS MET          
SEQRES  19 A  550  GLU VAL ALA PHE MET VAL CYS ALA ILE ASN PRO SER ILE          
SEQRES  20 A  550  ASP LEU HIS THR ASP SER LEU GLU LEU LEU GLN LEU GLN          
SEQRES  21 A  550  GLN LYS LEU LEU TRP LEU LEU TYR ASP LEU GLY HIS LEU          
SEQRES  22 A  550  GLU ARG TYR PRO MET ALA LEU GLY ASN LEU ALA ASP LEU          
SEQRES  23 A  550  GLU GLU LEU GLU PRO THR PRO GLY ARG PRO ASP PRO LEU          
SEQRES  24 A  550  THR LEU TYR HIS LYS GLY ILE ALA SER ALA LYS THR TYR          
SEQRES  25 A  550  TYR ARG ASP GLU HIS ILE TYR PRO TYR MET TYR LEU ALA          
SEQRES  26 A  550  GLY TYR HIS CYS ARG ASN ARG ASN VAL ARG GLU ALA LEU          
SEQRES  27 A  550  GLN ALA TRP ALA ASP THR ALA THR VAL ILE GLN ASP TYR          
SEQRES  28 A  550  ASN TYR CYS ARG GLU ASP GLU GLU ILE TYR LYS GLU PHE          
SEQRES  29 A  550  PHE GLU VAL ALA ASN ASP VAL ILE PRO ASN LEU LEU LYS          
SEQRES  30 A  550  GLU ALA ALA SER LEU LEU GLU ALA GLY GLU GLU ARG PRO          
SEQRES  31 A  550  GLY GLU GLN SER GLN GLY THR GLN SER GLN GLY SER ALA          
SEQRES  32 A  550  LEU GLN ASP PRO GLU CYS PHE ALA HIS LEU LEU ARG PHE          
SEQRES  33 A  550  TYR ASP GLY ILE CYS LYS TRP GLU GLU GLY SER PRO THR          
SEQRES  34 A  550  PRO VAL LEU HIS VAL GLY TRP ALA THR PHE LEU VAL GLN          
SEQRES  35 A  550  SER LEU GLY ARG PHE GLU GLY GLN VAL ARG GLN LYS VAL          
SEQRES  36 A  550  ARG ILE VAL SER GLY THR VAL ALA GLY THR ALA ARG GLY          
SEQRES  37 A  550  PRO GLU GLY GLY SER THR ALA GLN VAL PRO ALA PRO THR          
SEQRES  38 A  550  ALA SER PRO PRO PRO GLU GLY PRO VAL LEU THR PHE GLN          
SEQRES  39 A  550  SER GLU LYS MET LYS GLY MET LYS GLU LEU LEU VAL ALA          
SEQRES  40 A  550  THR LYS ILE ASN SER SER ALA ILE LYS LEU GLN LEU THR          
SEQRES  41 A  550  ALA GLN SER GLN VAL GLN MET LYS LYS GLN LYS VAL SER          
SEQRES  42 A  550  THR PRO SER ASP TYR THR LEU SER PHE LEU LYS ARG GLN          
SEQRES  43 A  550  ARG LYS GLY LEU                                              
SEQRES   1 B  550  SER GLY LEU LYS ALA ALA GLN LYS THR LEU PHE PRO LEU          
SEQRES   2 B  550  ARG SER ILE ASP ASP VAL VAL ARG LEU PHE ALA ALA GLU          
SEQRES   3 B  550  LEU GLY ARG GLU GLU PRO ASP LEU VAL LEU LEU SER LEU          
SEQRES   4 B  550  VAL LEU GLY PHE VAL GLU HIS PHE LEU ALA VAL ASN ARG          
SEQRES   5 B  550  VAL ILE PRO THR ASN VAL PRO GLU LEU THR PHE GLN PRO          
SEQRES   6 B  550  SER PRO ALA PRO ASP PRO PRO GLY GLY LEU THR TYR PHE          
SEQRES   7 B  550  PRO VAL ALA ASP LEU SER ILE ILE ALA ALA LEU TYR ALA          
SEQRES   8 B  550  ARG PHE THR ALA GLN ILE ARG GLY ALA VAL ASP LEU SER          
SEQRES   9 B  550  LEU TYR PRO ARG GLU GLY GLY VAL SER SER ARG GLU LEU          
SEQRES  10 B  550  VAL LYS LYS VAL SER ASP VAL ILE TRP ASN SER LEU SER          
SEQRES  11 B  550  ARG SER TYR PHE LYS ASP ARG ALA HIS ILE GLN SER LEU          
SEQRES  12 B  550  PHE SER PHE ILE THR GLY THR LYS LEU ASP SER SER GLY          
SEQRES  13 B  550  VAL ALA PHE ALA VAL VAL GLY ALA CYS GLN ALA LEU GLY          
SEQRES  14 B  550  LEU ARG ASP VAL HIS LEU ALA LEU SER GLU ASP HIS ALA          
SEQRES  15 B  550  TRP VAL VAL PHE GLY PRO ASN GLY GLU GLN THR ALA GLU          
SEQRES  16 B  550  VAL THR TRP HIS GLY LYS GLY ASN GLU ASP ARG ARG GLY          
SEQRES  17 B  550  GLN THR VAL ASN ALA GLY VAL ALA GLU ARG SER TRP LEU          
SEQRES  18 B  550  TYR LEU LYS GLY SER TYR MET ARG CYS ASP ARG LYS MET          
SEQRES  19 B  550  GLU VAL ALA PHE MET VAL CYS ALA ILE ASN PRO SER ILE          
SEQRES  20 B  550  ASP LEU HIS THR ASP SER LEU GLU LEU LEU GLN LEU GLN          
SEQRES  21 B  550  GLN LYS LEU LEU TRP LEU LEU TYR ASP LEU GLY HIS LEU          
SEQRES  22 B  550  GLU ARG TYR PRO MET ALA LEU GLY ASN LEU ALA ASP LEU          
SEQRES  23 B  550  GLU GLU LEU GLU PRO THR PRO GLY ARG PRO ASP PRO LEU          
SEQRES  24 B  550  THR LEU TYR HIS LYS GLY ILE ALA SER ALA LYS THR TYR          
SEQRES  25 B  550  TYR ARG ASP GLU HIS ILE TYR PRO TYR MET TYR LEU ALA          
SEQRES  26 B  550  GLY TYR HIS CYS ARG ASN ARG ASN VAL ARG GLU ALA LEU          
SEQRES  27 B  550  GLN ALA TRP ALA ASP THR ALA THR VAL ILE GLN ASP TYR          
SEQRES  28 B  550  ASN TYR CYS ARG GLU ASP GLU GLU ILE TYR LYS GLU PHE          
SEQRES  29 B  550  PHE GLU VAL ALA ASN ASP VAL ILE PRO ASN LEU LEU LYS          
SEQRES  30 B  550  GLU ALA ALA SER LEU LEU GLU ALA GLY GLU GLU ARG PRO          
SEQRES  31 B  550  GLY GLU GLN SER GLN GLY THR GLN SER GLN GLY SER ALA          
SEQRES  32 B  550  LEU GLN ASP PRO GLU CYS PHE ALA HIS LEU LEU ARG PHE          
SEQRES  33 B  550  TYR ASP GLY ILE CYS LYS TRP GLU GLU GLY SER PRO THR          
SEQRES  34 B  550  PRO VAL LEU HIS VAL GLY TRP ALA THR PHE LEU VAL GLN          
SEQRES  35 B  550  SER LEU GLY ARG PHE GLU GLY GLN VAL ARG GLN LYS VAL          
SEQRES  36 B  550  ARG ILE VAL SER GLY THR VAL ALA GLY THR ALA ARG GLY          
SEQRES  37 B  550  PRO GLU GLY GLY SER THR ALA GLN VAL PRO ALA PRO THR          
SEQRES  38 B  550  ALA SER PRO PRO PRO GLU GLY PRO VAL LEU THR PHE GLN          
SEQRES  39 B  550  SER GLU LYS MET LYS GLY MET LYS GLU LEU LEU VAL ALA          
SEQRES  40 B  550  THR LYS ILE ASN SER SER ALA ILE LYS LEU GLN LEU THR          
SEQRES  41 B  550  ALA GLN SER GLN VAL GLN MET LYS LYS GLN LYS VAL SER          
SEQRES  42 B  550  THR PRO SER ASP TYR THR LEU SER PHE LEU LYS ARG GLN          
SEQRES  43 B  550  ARG LYS GLY LEU                                              
SEQRES   1 M   75  SER ARG TRP ARG PHE PRO ALA ARG PRO GLY THR GLY ARG          
SEQRES   2 M   75  ARG GLY LEU GLY GLY ALA PRO ARG GLN ARG VAL PRO ALA          
SEQRES   3 M   75  LEU LEU ARG VAL GLY PRO GLY PHE ASP ALA ALA LEU GLN          
SEQRES   4 M   75  VAL SER ALA ALA ILE GLY THR ASN LEU ARG ARG PHE ARG          
SEQRES   5 M   75  ALA VAL PHE GLY GLU SER GLY GLY GLY GLY GLY SER GLY          
SEQRES   6 M   75  GLU ASP GLU GLN PHE LEU GLY PHE GLY SER                      
SEQRES   1 C   89  SER MET ASP SER ARG LEU GLN ARG ILE HIS ALA GLU ILE          
SEQRES   2 C   89  LYS ASN SER LEU LYS ILE ASP ASN LEU ASP VAL ASN ARG          
SEQRES   3 C   89  CYS ILE GLU ALA LEU ASP GLU LEU ALA SER LEU GLN VAL          
SEQRES   4 C   89  THR MET GLN GLN ALA GLN LYS HIS THR GLU MET ILE THR          
SEQRES   5 C   89  THR LEU LYS LYS ILE ARG ARG PHE LYS VAL SER GLN VAL          
SEQRES   6 C   89  ILE MET GLU LYS SER THR MET LEU TYR ASN LYS PHE LYS          
SEQRES   7 C   89  ASN MET PHE LEU VAL GLY GLU GLY ASP SER VAL                  
SEQRES   1 N   75  SER ARG TRP ARG PHE PRO ALA ARG PRO GLY THR GLY ARG          
SEQRES   2 N   75  ARG GLY LEU GLY GLY ALA PRO ARG GLN ARG VAL PRO ALA          
SEQRES   3 N   75  LEU LEU ARG VAL GLY PRO GLY PHE ASP ALA ALA LEU GLN          
SEQRES   4 N   75  VAL SER ALA ALA ILE GLY THR ASN LEU ARG ARG PHE ARG          
SEQRES   5 N   75  ALA VAL PHE GLY GLU SER GLY GLY GLY GLY GLY SER GLY          
SEQRES   6 N   75  GLU ASP GLU GLN PHE LEU GLY PHE GLY SER                      
SEQRES   1 D   89  SER MET ASP SER ARG LEU GLN ARG ILE HIS ALA GLU ILE          
SEQRES   2 D   89  LYS ASN SER LEU LYS ILE ASP ASN LEU ASP VAL ASN ARG          
SEQRES   3 D   89  CYS ILE GLU ALA LEU ASP GLU LEU ALA SER LEU GLN VAL          
SEQRES   4 D   89  THR MET GLN GLN ALA GLN LYS HIS THR GLU MET ILE THR          
SEQRES   5 D   89  THR LEU LYS LYS ILE ARG ARG PHE LYS VAL SER GLN VAL          
SEQRES   6 D   89  ILE MET GLU LYS SER THR MET LEU TYR ASN LYS PHE LYS          
SEQRES   7 D   89  ASN MET PHE LEU VAL GLY GLU GLY ASP SER VAL                  
HET    CHD  A 611      29                                                       
HET    GGB  A 613      12                                                       
HET    0BR  A 612      24                                                       
HET    GGB  A 614      12                                                       
HET    GLV  A 615       5                                                       
HET    GLV  A 616       5                                                       
HET    GLV  A 617       5                                                       
HET    SO4  A 618       5                                                       
HET    SO4  A 619       5                                                       
HET    CHD  B 611      29                                                       
HET    0BR  B 612      24                                                       
HET    GGB  B 615      12                                                       
HET    GLV  B 616       5                                                       
HET    SO4  B 617       5                                                       
HET    SO4  B 618       5                                                       
HET    SO4  M   2       5                                                       
HET    SO4  M 154       5                                                       
HET    GGB  C 108      12                                                       
HET    GGB  C 109      12                                                       
HET    GLV  C 113       5                                                       
HET    SO4  N   1       5                                                       
HET    SO4  N 154       5                                                       
HET    GLV  D 114       5                                                       
HETNAM     CHD CHOLIC ACID                                                      
HETNAM     GGB L-CANAVANINE                                                     
HETNAM     0BR (4BETA,8ALPHA,9R)-6'-METHOXY-10,11-DIHYDROCINCHONAN-9-           
HETNAM   2 0BR  OL                                                              
HETNAM     GLV GLYOXYLIC ACID                                                   
HETNAM     SO4 SULFATE ION                                                      
HETSYN     GGB L-2-AMINO-4-(GUANIDINOOXY)BUTYRIC ACID                           
HETSYN     GLV GLYOXALATE, GLYOXYLATE                                           
FORMUL   7  CHD    2(C24 H40 O5)                                                
FORMUL   8  GGB    5(C5 H12 N4 O3)                                              
FORMUL   9  0BR    2(C20 H26 N2 O2)                                             
FORMUL  11  GLV    6(C2 H2 O3)                                                  
FORMUL  14  SO4    8(O4 S 2-)                                                   
HELIX    1   1 LYS A    4  THR A    9  1                                   6    
HELIX    2   2 SER A   15  ARG A   29  1                                  15    
HELIX    3   3 ASP A   33  ALA A   49  1                                  17    
HELIX    4   4 ASP A   82  GLY A   99  1                                  18    
HELIX    5   5 SER A  114  ASN A  127  1                                  14    
HELIX    6   6 SER A  142  GLY A  149  1                                   8    
HELIX    7   7 ASP A  153  LEU A  168  1                                  16    
HELIX    8   8 GLY A  187  GLU A  191  5                                   5    
HELIX    9   9 VAL A  211  ARG A  218  1                                   8    
HELIX   10  10 TYR A  222  SER A  226  5                                   5    
HELIX   11  11 ASP A  231  ALA A  242  1                                  12    
HELIX   12  12 LEU A  254  LEU A  270  1                                  17    
HELIX   13  13 TYR A  276  GLU A  290  1                                  15    
HELIX   14  14 ASP A  297  TYR A  313  1                                  17    
HELIX   15  15 ILE A  318  ASN A  331  1                                  14    
HELIX   16  16 ASN A  333  GLN A  349  1                                  17    
HELIX   17  17 CYS A  354  GLU A  356  5                                   3    
HELIX   18  18 ASP A  357  ASP A  370  1                                  14    
HELIX   19  19 ASP A  370  ALA A  385  1                                  16    
HELIX   20  20 SER A  402  GLN A  405  5                                   4    
HELIX   21  21 ASP A  406  GLU A  425  1                                  20    
HELIX   22  22 HIS A  433  ARG A  446  1                                  14    
HELIX   23  23 GLU A  448  GLN A  453  1                                   6    
HELIX   24  24 SER A  555  MET A  561  1                                   7    
HELIX   25  25 ASN A  571  THR A  580  1                                  10    
HELIX   26  26 LYS B    4  THR B    9  1                                   6    
HELIX   27  27 SER B   15  ARG B   29  1                                  15    
HELIX   28  28 ASP B   33  VAL B   50  1                                  18    
HELIX   29  29 ASP B   82  GLY B   99  1                                  18    
HELIX   30  30 ASP B  102  TYR B  106  5                                   5    
HELIX   31  31 SER B  114  ASN B  127  1                                  14    
HELIX   32  32 SER B  142  GLY B  149  1                                   8    
HELIX   33  33 ASP B  153  LEU B  168  1                                  16    
HELIX   34  34 GLY B  187  GLU B  191  5                                   5    
HELIX   35  35 VAL B  211  GLU B  217  1                                   7    
HELIX   36  36 SER B  219  SER B  226  5                                   8    
HELIX   37  37 ASP B  231  ALA B  242  1                                  12    
HELIX   38  38 LEU B  254  LEU B  270  1                                  17    
HELIX   39  39 TYR B  276  GLU B  290  1                                  15    
HELIX   40  40 ASP B  297  TYR B  313  1                                  17    
HELIX   41  41 ILE B  318  ASN B  331  1                                  14    
HELIX   42  42 ASN B  333  GLN B  349  1                                  17    
HELIX   43  43 CYS B  354  GLU B  356  5                                   3    
HELIX   44  44 ASP B  357  ASP B  370  1                                  14    
HELIX   45  45 ASP B  370  ALA B  385  1                                  16    
HELIX   46  46 GLY B  401  GLN B  405  5                                   5    
HELIX   47  47 ASP B  406  GLU B  425  1                                  20    
HELIX   48  48 HIS B  433  GLY B  445  1                                  13    
HELIX   49  49 GLU B  448  GLN B  453  1                                   6    
HELIX   50  50 SER B  555  GLY B  560  1                                   6    
HELIX   51  51 ASN B  571  LEU B  579  1                                   9    
HELIX   52  52 GLY M   23  GLY M   29  1                                   7    
HELIX   53  53 ASP M  113  GLY M  134  1                                  22    
HELIX   54  54 ASP C  349  LEU C  363  1                                  15    
HELIX   55  55 ASP C  369  ALA C  381  1                                  13    
HELIX   56  56 THR C  386  LYS C  392  1                                   7    
HELIX   57  57 HIS C  393  ARG C  404  1                                  12    
HELIX   58  58 SER C  409  LEU C  428  1                                  20    
HELIX   59  59 GLY N   23  GLY N   28  1                                   6    
HELIX   60  60 ASP N  113  PHE N  133  1                                  21    
HELIX   61  61 ARG D  354  SER D  362  1                                   9    
HELIX   62  62 ASN D  371  SER D  382  1                                  12    
HELIX   63  63 THR D  386  GLN D  391  1                                   6    
HELIX   64  64 HIS D  393  ARG D  404  1                                  12    
HELIX   65  65 VAL D  411  GLY D  430  1                                  20    
SHEET    1   A 2 VAL A  53  ILE A  54  0                                        
SHEET    2   A 2 ARG M 107  VAL M 108  1  O  ARG M 107   N  ILE A  54           
SHEET    1   B 2 PHE A  63  PRO A  67  0                                        
SHEET    2   B 2 LEU A  75  PRO A  79 -1  O  THR A  76   N  SER A  66           
SHEET    1   C 4 GLN A 192  ALA A 194  0                                        
SHEET    2   C 4 ALA A 182  PHE A 186 -1  N  VAL A 184   O  ALA A 194           
SHEET    3   C 4 HIS A 174  LEU A 177 -1  N  ALA A 176   O  TRP A 183           
SHEET    4   C 4 MET A 228  ARG A 229 -1  O  MET A 228   N  LEU A 177           
SHEET    1   D 2 THR A 251  SER A 253  0                                        
SHEET    2   D 2 GLN M  33  VAL M  35  1  O  GLN M  33   N  ASP A 252           
SHEET    1   E 2 ARG A 456  VAL A 458  0                                        
SHEET    2   E 2 VAL A 550  THR A 552  1  O  LEU A 551   N  ARG A 456           
SHEET    1   F 2 VAL B  53  ILE B  54  0                                        
SHEET    2   F 2 ARG N 107  VAL N 108  1  O  ARG N 107   N  ILE B  54           
SHEET    1   G 2 PHE B  63  SER B  66  0                                        
SHEET    2   G 2 THR B  76  PRO B  79 -1  O  PHE B  78   N  GLN B  64           
SHEET    1   H 4 GLN B 192  ALA B 194  0                                        
SHEET    2   H 4 ALA B 182  PHE B 186 -1  N  VAL B 184   O  ALA B 194           
SHEET    3   H 4 HIS B 174  LEU B 177 -1  N  HIS B 174   O  VAL B 185           
SHEET    4   H 4 MET B 228  ARG B 229 -1  O  MET B 228   N  LEU B 177           
SHEET    1   I 3 SER B 246  ASP B 248  0                                        
SHEET    2   I 3 THR B 251  SER B 253 -1  O  THR B 251   N  ILE B 247           
SHEET    3   I 3 GLN N  33  VAL N  35  1  O  VAL N  35   N  ASP B 252           
SHEET    1   J 2 ARG B 456  VAL B 458  0                                        
SHEET    2   J 2 VAL B 550  THR B 552  1  O  LEU B 551   N  ARG B 456           
CISPEP   1 PHE A   11    PRO A   12          0        -2.28                     
CISPEP   2 PHE B   11    PRO B   12          0        -4.21                     
CISPEP   3 PRO B   69    ASP B   70          0         2.93                     
CISPEP   4 PRO B   71    PRO B   72          0         3.75                     
CISPEP   5 PRO B   72    GLY B   73          0        -1.28                     
CISPEP   6 GLY B   73    GLY B   74          0        -1.36                     
CISPEP   7 GLU B  109    GLY B  110          0        -2.23                     
CISPEP   8 GLY B  202    ASN B  203          0        -5.45                     
CISPEP   9 PRO B  544    PRO B  545          0        -7.71                     
CISPEP  10 PRO M   13    GLY M   14          0        18.98                     
CISPEP  11 VAL M  108    GLY M  109          0        17.12                     
CISPEP  12 GLY M  109    PRO M  110          0         3.05                     
CISPEP  13 PRO M  110    GLY M  111          0       -10.69                     
CISPEP  14 PRO N   13    GLY N   14          0        18.11                     
CISPEP  15 VAL N  108    GLY N  109          0        18.89                     
CISPEP  16 GLY N  109    PRO N  110          0        18.62                     
SITE     1 AC1  5 SER A 132  TYR A 133  PHE A 134  LYS A 135                    
SITE     2 AC1  5 CHD B 611                                                     
SITE     1 AC2  5 CHD A 611  SER B 132  TYR B 133  PHE B 134                    
SITE     2 AC2  5 LYS B 135                                                     
SITE     1 AC3  6 0BR A 612  TRP B 126  SER B 130  ARG B 131                    
SITE     2 AC3  6 TRP B 198  ASN B 203                                          
SITE     1 AC4  4 TYR A 133  PHE A 134  ARG A 137  LYS A 151                    
SITE     1 AC5  7 TRP A 126  LEU A 129  SER A 130  ARG A 131                    
SITE     2 AC5  7 TRP A 198  ASN A 203  0BR B 612                               
SITE     1 AC6  4 TYR B 133  PHE B 134  ARG B 137  LYS B 151                    
SITE     1 AC7  5 ARG A 108  GLY A 111  VAL A 112  SER A 113                    
SITE     2 AC7  5 ARG A 171                                                     
SITE     1 AC8  5 LYS A 135  ASP A 136  SER A 154  TRP A 198                    
SITE     2 AC8  5 GLY A 200                                                     
SITE     1 AC9  4 GLU A 195  THR A 197  ARG A 206  TYR A 222                    
SITE     1 BC1  5 GLU A 408  ALA A 411  HIS A 412  ARG A 415                    
SITE     2 BC1  5 LEU A 551                                                     
SITE     1 BC2  6 LYS B 135  ASP B 136  SER B 154  TRP B 198                    
SITE     2 BC2  6 GLY B 200  LYS B 201                                          
SITE     1 BC3  5 ARG B 330  GLY N  23  ARG N  24  ARG N  25                    
SITE     2 BC3  5 GLY N  26                                                     
SITE     1 BC4  6 GLY M  14  THR M  15  GLY M  23  ARG M  24                    
SITE     2 BC4  6 ARG M  25  GLY M  26                                          
SITE     1 BC5  3 THR A  56  LYS A 377  ARG A 446                               
SITE     1 BC6  2 ARG A 275  LYS B 310                                          
SITE     1 BC7  4 ARG B 108  GLY B 111  GLY B 169  ARG B 171                    
SITE     1 BC8  2 GGB C 109  ARG C 405                                          
SITE     1 BC9  2 LYS B 377  ARG B 446                                          
SITE     1 CC1  4 GGB C 108  LEU C 363  LYS C 364  ILE C 365                    
SITE     1 CC2  4 ARG A  98  ARG C 404  THR C 417  ASN C 421                    
SITE     1 CC3  2 THR D 417  ASN D 421                                          
SITE     1 CC4  3 GLY B   2  LYS D 424  ARG N 130                               
SITE     1 CC5  5 GLY A   2  LYS C 424  ARG M 130  GLY M 134                    
SITE     2 CC5  5 GLU M 135                                                     
CRYST1  187.990  187.990  238.417  90.00  90.00 120.00 P 61 2 2     24          
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      0.005319  0.003071  0.000000        0.00000                         
SCALE2      0.000000  0.006142  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004194        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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