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Database: PDB
Entry: 5MWX
LinkDB: 5MWX
Original site: 5MWX 
HEADER    TRANSFERASE                             20-JAN-17   5MWX              
TITLE     GALECTIN-1 IN COMPLEX WITH LIGAND JB60                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GALECTIN-1;                                                
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: GAL-1,14 KDA LAMININ-BINDING PROTEIN,HLBP14,14 KDA LECTIN,  
COMPND   5 BETA-GALACTOSIDE-BINDING LECTIN L-14-I,GALAPTIN,HBL,HPL,LACTOSE-     
COMPND   6 BINDING LECTIN 1,LECTIN GALACTOSIDE-BINDING SOLUBLE 1,PUTATIVE MAPK- 
COMPND   7 ACTIVATING PROTEIN PM12,S-LAC LECTIN 1;                              
COMPND   8 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: LGALS1;                                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    SUCROSE PHOSPHORYLASE, BISP, BIFIDOBACTERIUM, TRANSFERASE             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.GRIMM,J.BECHOLD                                                     
REVDAT   2   16-OCT-19 5MWX    1       REMARK                                   
REVDAT   1   28-FEB-18 5MWX    0                                                
JRNL        AUTH   C.GRIMM,J.BECHOLD                                            
JRNL        TITL   GALECTIN-1 IN COMPLEX WITH LIGAND JB60                       
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.29 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX DEV_2443                                      
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 : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.29                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.32                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 71171                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.171                           
REMARK   3   R VALUE            (WORKING SET) : 0.169                           
REMARK   3   FREE R VALUE                     : 0.205                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.970                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3540                            
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 40.3387 -  3.7710    1.00     2932   170  0.1728 0.2063        
REMARK   3     2  3.7710 -  2.9935    1.00     2805   144  0.1604 0.1998        
REMARK   3     3  2.9935 -  2.6152    1.00     2766   150  0.1644 0.1900        
REMARK   3     4  2.6152 -  2.3761    1.00     2745   153  0.1551 0.1983        
REMARK   3     5  2.3761 -  2.2058    1.00     2740   154  0.1363 0.1459        
REMARK   3     6  2.2058 -  2.0758    1.00     2701   148  0.1329 0.1925        
REMARK   3     7  2.0758 -  1.9718    1.00     2732   150  0.1265 0.1548        
REMARK   3     8  1.9718 -  1.8860    1.00     2738   123  0.1298 0.1528        
REMARK   3     9  1.8860 -  1.8134    1.00     2738   124  0.1386 0.1902        
REMARK   3    10  1.8134 -  1.7508    1.00     2754   117  0.1477 0.1996        
REMARK   3    11  1.7508 -  1.6960    1.00     2704   135  0.1605 0.1892        
REMARK   3    12  1.6960 -  1.6476    1.00     2707   146  0.1547 0.2226        
REMARK   3    13  1.6476 -  1.6042    1.00     2666   144  0.1570 0.2324        
REMARK   3    14  1.6042 -  1.5650    1.00     2708   142  0.1567 0.1896        
REMARK   3    15  1.5650 -  1.5295    0.99     2654   160  0.1648 0.2293        
REMARK   3    16  1.5295 -  1.4969    1.00     2695   124  0.1978 0.2294        
REMARK   3    17  1.4969 -  1.4670    1.00     2712   136  0.2376 0.2799        
REMARK   3    18  1.4670 -  1.4393    1.00     2651   153  0.2493 0.2908        
REMARK   3    19  1.4393 -  1.4136    1.00     2695   137  0.2726 0.3389        
REMARK   3    20  1.4136 -  1.3896    1.00     2670   131  0.2826 0.3044        
REMARK   3    21  1.3896 -  1.3672    0.99     2701   139  0.3032 0.3281        
REMARK   3    22  1.3672 -  1.3462    0.99     2657   153  0.3171 0.3580        
REMARK   3    23  1.3462 -  1.3264    0.99     2616   156  0.3431 0.3610        
REMARK   3    24  1.3264 -  1.3077    0.97     2591   141  0.3587 0.4045        
REMARK   3    25  1.3077 -  1.2900    0.94     2553   110  0.3743 0.3413        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
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)     : 0.160            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.550           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.85                          
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      :  0.023           2353                                  
REMARK   3   ANGLE     :  1.653           3204                                  
REMARK   3   CHIRALITY :  0.116            350                                  
REMARK   3   PLANARITY :  0.011            423                                  
REMARK   3   DIHEDRAL  : 22.870            967                                  
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 5MWX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 20-JAN-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200003149.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-MAY-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID30B                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97242                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 S 6M              
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 71546                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.290                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.320                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 6.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.7100                            
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   (%): 48.20                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.5 M AMMONIUM SULFATE, PH 7.5, VAPOR    
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 298K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       21.63000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       55.62500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       29.12500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       55.62500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       21.63000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       29.12500            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1560 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 12350 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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   O    HOH B   393     O    HOH B   398              1.86            
REMARK 500   O    ASP A   134     O    HOH A   301              2.03            
REMARK 500   O    HOH B   315     O    HOH B   341              2.08            
REMARK 500   OE1  GLN B    93     O    HOH B   301              2.09            
REMARK 500   O    HOH B   335     O    HOH B   374              2.09            
REMARK 500   O    HOH A   366     O    HOH A   389              2.12            
REMARK 500   NAE  WYD A   202     O    HOH A   302              2.16            
REMARK 500   OE2  GLU A    22     O    HOH A   303              2.18            
REMARK 500   OE2  GLU B   105     O    HOH B   302              2.18            
REMARK 500   O    HOH B   347     O    HOH B   385              2.19            
REMARK 500   O    HOH B   302     O    HOH B   397              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500  HH12  ARG A    20     OD2  ASP A    26     4555     1.47            
REMARK 500   O    HOH A   378     O    HOH B   367     1565     1.99            
REMARK 500   OE1  GLN A    93     CAN  WYD B   202     3655     2.19            
REMARK 500   O    HOH B   335     O    HOH B   349     4445     2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU A  71   CB    GLU A  71   CG     -0.116                       
REMARK 500    GLU A  74   CG    GLU A  74   CD      0.096                       
REMARK 500    VAL A  76   CB    VAL A  76   CG2    -0.140                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A  73   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A  50       82.75   -163.12                                   
REMARK 500    PHE A  77       78.38   -152.04                                   
REMARK 500    PRO A  78       50.88    -91.36                                   
REMARK 500    ASP A 125       54.82    -92.88                                   
REMARK 500    PRO B  78       48.61    -94.24                                   
REMARK 500    ASP B 125       47.45    -89.25                                   
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 BME A 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue WYD A 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue WYD B 202                 
DBREF  5MWX A    2   134  UNP    P09382   LEG1_HUMAN       3    135             
DBREF  5MWX B    2   134  UNP    P09382   LEG1_HUMAN       3    135             
SEQRES   1 A  133  CYS GLY LEU VAL ALA SER ASN LEU ASN LEU LYS PRO GLY          
SEQRES   2 A  133  GLU CME LEU ARG VAL ARG GLY GLU VAL ALA PRO ASP ALA          
SEQRES   3 A  133  LYS SER PHE VAL LEU ASN LEU GLY LYS ASP SER ASN ASN          
SEQRES   4 A  133  LEU CYS LEU HIS PHE ASN PRO ARG PHE ASN ALA HIS GLY          
SEQRES   5 A  133  ASP ALA ASN THR ILE VAL CYS ASN SER LYS ASP GLY GLY          
SEQRES   6 A  133  ALA TRP GLY THR GLU GLN ARG GLU ALA VAL PHE PRO PHE          
SEQRES   7 A  133  GLN PRO GLY SER VAL ALA GLU VAL CME ILE THR PHE ASP          
SEQRES   8 A  133  GLN ALA ASN LEU THR VAL LYS LEU PRO ASP GLY TYR GLU          
SEQRES   9 A  133  PHE LYS PHE PRO ASN ARG LEU ASN LEU GLU ALA ILE ASN          
SEQRES  10 A  133  TYR MET ALA ALA ASP GLY ASP PHE LYS ILE LYS CME VAL          
SEQRES  11 A  133  ALA PHE ASP                                                  
SEQRES   1 B  133  CYS GLY LEU VAL ALA SER ASN LEU ASN LEU LYS PRO GLY          
SEQRES   2 B  133  GLU CME LEU ARG VAL ARG GLY GLU VAL ALA PRO ASP ALA          
SEQRES   3 B  133  LYS SER PHE VAL LEU ASN LEU GLY LYS ASP SER ASN ASN          
SEQRES   4 B  133  LEU CYS LEU HIS PHE ASN PRO ARG PHE ASN ALA HIS GLY          
SEQRES   5 B  133  ASP ALA ASN THR ILE VAL CYS ASN SER LYS ASP GLY GLY          
SEQRES   6 B  133  ALA TRP GLY THR GLU GLN ARG GLU ALA VAL PHE PRO PHE          
SEQRES   7 B  133  GLN PRO GLY SER VAL ALA GLU VAL CME ILE THR PHE ASP          
SEQRES   8 B  133  GLN ALA ASN LEU THR VAL LYS LEU PRO ASP GLY TYR GLU          
SEQRES   9 B  133  PHE LYS PHE PRO ASN ARG LEU ASN LEU GLU ALA ILE ASN          
SEQRES  10 B  133  TYR MET ALA ALA ASP GLY ASP PHE LYS ILE LYS CME VAL          
SEQRES  11 B  133  ALA PHE ASP                                                  
MODRES 5MWX CME A   16  CYS  MODIFIED RESIDUE                                   
MODRES 5MWX CME A   88  CYS  MODIFIED RESIDUE                                   
MODRES 5MWX CME A  130  CYS  MODIFIED RESIDUE                                   
MODRES 5MWX CME B   16  CYS  MODIFIED RESIDUE                                   
MODRES 5MWX CME B   88  CYS  MODIFIED RESIDUE                                   
MODRES 5MWX CME B  130  CYS  MODIFIED RESIDUE                                   
HET    CME  A  16      19                                                       
HET    CME  A  88      19                                                       
HET    CME  A 130      19                                                       
HET    CME  B  16      19                                                       
HET    CME  B  88      19                                                       
HET    CME  B 130      19                                                       
HET    BME  A 201       8                                                       
HET    WYD  A 202      46                                                       
HET    SO4  B 201       5                                                       
HET    WYD  B 202      46                                                       
HETNAM     CME S,S-(2-HYDROXYETHYL)THIOCYSTEINE                                 
HETNAM     BME BETA-MERCAPTOETHANOL                                             
HETNAM     WYD ~{N}-[(2~{R},3~{R},4~{R},5~{S},6~{R})-5-[(2~{S},3~{R},           
HETNAM   2 WYD  4~{S},5~{S},6~{R})-4-[[1-[[3-(3-AZANYLPROP-1-YNYL)              
HETNAM   3 WYD  PHENYL]METHYL]-1,2,3-TRIAZOL-4-YL]METHOXY]-6-                   
HETNAM   4 WYD  (HYDROXYMETHYL)-3,5-BIS(OXIDANYL)OXAN-2-YL]OXY-6-               
HETNAM   5 WYD  (HYDROXYMETHYL)-4-OXIDANYL-2-PROPOXY-OXAN-3-                    
HETNAM   6 WYD  YL]ETHANAMIDE                                                   
HETNAM     SO4 SULFATE ION                                                      
FORMUL   1  CME    6(C5 H11 N O3 S2)                                            
FORMUL   3  BME    C2 H6 O S                                                    
FORMUL   4  WYD    2(C30 H43 N5 O11)                                            
FORMUL   5  SO4    O4 S 2-                                                      
FORMUL   7  HOH   *191(H2 O)                                                    
HELIX    1 AA1 PRO B  101  GLY B  103  5                                   3    
SHEET    1 AA112 ALA A  67  TRP A  68  0                                        
SHEET    2 AA112 ASP A  54  ASP A  64 -1  N  ASP A  64   O  ALA A  67           
SHEET    3 AA112 ASN A  40  ALA A  51 -1  N  ARG A  48   O  THR A  57           
SHEET    4 AA112 PHE A  30  ASP A  37 -1  N  LEU A  32   O  PHE A  45           
SHEET    5 AA112 ILE A 117  GLY A 124 -1  O  ASP A 123   N  VAL A  31           
SHEET    6 AA112 VAL A   5  LEU A  11 -1  N  ALA A   6   O  MET A 120           
SHEET    7 AA112 VAL B   5  LEU B  11 -1  O  SER B   7   N  VAL A   5           
SHEET    8 AA112 ILE B 117  GLY B 124 -1  O  MET B 120   N  ALA B   6           
SHEET    9 AA112 PHE B  30  ASP B  37 -1  N  ASN B  33   O  ALA B 121           
SHEET   10 AA112 ASN B  40  ALA B  51 -1  O  PHE B  45   N  LEU B  32           
SHEET   11 AA112 ASP B  54  ASP B  64 -1  O  THR B  57   N  ARG B  48           
SHEET   12 AA112 ALA B  67  TRP B  68 -1  O  ALA B  67   N  ASP B  64           
SHEET    1 AA212 GLN A  72  ARG A  73  0                                        
SHEET    2 AA212 ASP A  54  ASP A  64 -1  N  CYS A  60   O  GLN A  72           
SHEET    3 AA212 ASN A  40  ALA A  51 -1  N  ARG A  48   O  THR A  57           
SHEET    4 AA212 PHE A  30  ASP A  37 -1  N  LEU A  32   O  PHE A  45           
SHEET    5 AA212 ILE A 117  GLY A 124 -1  O  ASP A 123   N  VAL A  31           
SHEET    6 AA212 VAL A   5  LEU A  11 -1  N  ALA A   6   O  MET A 120           
SHEET    7 AA212 VAL B   5  LEU B  11 -1  O  SER B   7   N  VAL A   5           
SHEET    8 AA212 ILE B 117  GLY B 124 -1  O  MET B 120   N  ALA B   6           
SHEET    9 AA212 PHE B  30  ASP B  37 -1  N  ASN B  33   O  ALA B 121           
SHEET   10 AA212 ASN B  40  ALA B  51 -1  O  PHE B  45   N  LEU B  32           
SHEET   11 AA212 ASP B  54  ASP B  64 -1  O  THR B  57   N  ARG B  48           
SHEET   12 AA212 GLN B  72  ARG B  73 -1  O  GLN B  72   N  CYS B  60           
SHEET    1 AA310 GLU A 105  PRO A 109  0                                        
SHEET    2 AA310 ASN A  95  LYS A  99 -1  N  LEU A  96   O  PHE A 108           
SHEET    3 AA310 SER A  83  PHE A  91 -1  N  THR A  90   O  THR A  97           
SHEET    4 AA310 LEU A  17  VAL A  23 -1  N  LEU A  17   O  ILE A  89           
SHEET    5 AA310 PHE A 126  PHE A 133 -1  O  LYS A 129   N  ARG A  20           
SHEET    6 AA310 PHE B 126  ASP B 134 -1  O  PHE B 133   N  LYS A 129           
SHEET    7 AA310 CME B  16  VAL B  23 -1  N  GLU B  22   O  LYS B 127           
SHEET    8 AA310 SER B  83  PHE B  91 -1  O  SER B  83   N  VAL B  23           
SHEET    9 AA310 ASN B  95  LYS B  99 -1  O  LYS B  99   N  CME B  88           
SHEET   10 AA310 GLU B 105  PRO B 109 -1  O  PHE B 108   N  LEU B  96           
LINK         C   GLU A  15                 N   CME A  16     1555   1555  1.33  
LINK         C   CME A  16                 N   LEU A  17     1555   1555  1.33  
LINK         C   VAL A  87                 N   CME A  88     1555   1555  1.32  
LINK         C   CME A  88                 N   ILE A  89     1555   1555  1.32  
LINK         C   LYS A 129                 N   CME A 130     1555   1555  1.31  
LINK         C   CME A 130                 N  AVAL A 131     1555   1555  1.34  
LINK         C   CME A 130                 N  BVAL A 131     1555   1555  1.33  
LINK         C   GLU B  15                 N   CME B  16     1555   1555  1.34  
LINK         C   CME B  16                 N   LEU B  17     1555   1555  1.31  
LINK         C   VAL B  87                 N   CME B  88     1555   1555  1.33  
LINK         C   CME B  88                 N   ILE B  89     1555   1555  1.31  
LINK         C   LYS B 129                 N   CME B 130     1555   1555  1.32  
LINK         C   CME B 130                 N  AVAL B 131     1555   1555  1.31  
LINK         C   CME B 130                 N  BVAL B 131     1555   1555  1.32  
LINK         OE1 GLN A  93                 NAA WYD B 202     1555   3655  1.30  
SITE     1 AC1  7 LYS A  36  LEU A 114  GLU A 115  ALA A 116                    
SITE     2 AC1  7 HOH A 341  HOH A 382  LYS B  28                               
SITE     1 AC2 14 SER A  29  HIS A  44  ASN A  46  ARG A  48                    
SITE     2 AC2 14 HIS A  52  ASN A  61  GLU A  71  ARG A  73                    
SITE     3 AC2 14 ASP A 123  GLY A 124  ASP A 125  HOH A 302                    
SITE     4 AC2 14 HOH A 349  THR B  70                                          
SITE     1 AC3  9 PRO A 101  ASP A 102  ASN B  10  LYS B  12                    
SITE     2 AC3  9 HOH B 317  HOH B 318  HOH B 321  HOH B 332                    
SITE     3 AC3  9 HOH B 343                                                     
SITE     1 AC4 15 GLN A  72  GLN A  93  ASN A 113  HIS B  44                    
SITE     2 AC4 15 ASN B  46  ARG B  48  HIS B  52  ASN B  61                    
SITE     3 AC4 15 GLU B  71  ARG B  73  ASP B 123  GLY B 124                    
SITE     4 AC4 15 HOH B 303  HOH B 307  HOH B 367                               
CRYST1   43.260   58.250  111.250  90.00  90.00  90.00 P 21 21 21    8          
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      0.023116  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.017167  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008989        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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