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Database: PDB
Entry: 3NMN
LinkDB: 3NMN
Original site: 3NMN 
HEADER    PROTEIN BINDING                         22-JUN-10   3NMN              
TITLE     CRYSTAL STRUCTURE OF PYRABACTIN-BOUND ABSCISIC ACID RECEPTOR PYL1 IN  
TITLE    2 COMPLEX WITH TYPE 2C PROTEIN PHOSPHATASE ABI1                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ABSCISIC ACID RECEPTOR PYL1;                               
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 SYNONYM: PYR1-LIKE PROTEIN 1, ABI1-BINDING PROTEIN 6, REGULATORY     
COMPND   5 COMPONENTS OF ABA RECEPTOR 9;                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: PROTEIN PHOSPHATASE 2C 56;                                 
COMPND   9 CHAIN: B, D;                                                         
COMPND  10 SYNONYM: ATPP2C56, PROTEIN PHOSPHATASE 2C ABI1, PP2C ABI1, PROTEIN   
COMPND  11 ABSCISIC ACID-INSENSITIVE 1;                                         
COMPND  12 EC: 3.1.3.16;                                                        
COMPND  13 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;                           
SOURCE   3 ORGANISM_COMMON: MOUSE-EAR CRESS,THALE-CRESS;                        
SOURCE   4 ORGANISM_TAXID: 3702;                                                
SOURCE   5 GENE: PYL1, RCAR12, AT5G46790, MZA15.21;                             
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR: PLASMID;                                   
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET24A;                                   
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;                           
SOURCE  13 ORGANISM_COMMON: MOUSE-EAR CRESS,THALE-CRESS;                        
SOURCE  14 ORGANISM_TAXID: 3702;                                                
SOURCE  15 GENE: ABI1, AT4G26080, F20B18.190;                                   
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE  19 EXPRESSION_SYSTEM_VECTOR: PLASMID;                                   
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PET24A                                    
KEYWDS    PYL1, PYRABACTIN, PLANT HORMONE RECEPTOR, ABSCISIC ACID SIGNALING,    
KEYWDS   2 PROTEIN BINDING                                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    X.E.ZHOU,K.MELCHER,L.-M.NG,F.-F.SOON,Y.XU,K.M.SUINO-POWELL,A.KOVACH,  
AUTHOR   2 J.LI,E.-L.YONG,H.E.XU                                                
REVDAT   3   06-SEP-23 3NMN    1       REMARK SEQADV LINK                       
REVDAT   2   15-SEP-10 3NMN    1       JRNL                                     
REVDAT   1   25-AUG-10 3NMN    0                                                
JRNL        AUTH   K.MELCHER,Y.XU,L.M.NG,X.E.ZHOU,F.F.SOON,V.CHINNUSAMY,        
JRNL        AUTH 2 K.M.SUINO-POWELL,A.KOVACH,F.S.THAM,S.R.CUTLER,J.LI,E.L.YONG, 
JRNL        AUTH 3 J.K.ZHU,H.E.XU                                               
JRNL        TITL   IDENTIFICATION AND MECHANISM OF ABA RECEPTOR ANTAGONISM.     
JRNL        REF    NAT.STRUCT.MOL.BIOL.          V.  17  1102 2010              
JRNL        REFN                   ISSN 1545-9993                               
JRNL        PMID   20729862                                                     
JRNL        DOI    10.1038/NSMB.1887                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.15 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0072                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.62                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 46283                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.213                           
REMARK   3   R VALUE            (WORKING SET) : 0.210                           
REMARK   3   FREE R VALUE                     : 0.248                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3617                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.15                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.21                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3118                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 90.35                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3110                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 280                          
REMARK   3   BIN FREE R VALUE                    : 0.3470                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6956                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 48                                      
REMARK   3   SOLVENT ATOMS            : 180                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 40.94                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.28000                                              
REMARK   3    B22 (A**2) : 0.11000                                              
REMARK   3    B33 (A**2) : -0.57000                                             
REMARK   3    B12 (A**2) : -1.47000                                             
REMARK   3    B13 (A**2) : -2.38000                                             
REMARK   3    B23 (A**2) : 1.22000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.217         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.171         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 15.115        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.951                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.934                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  7134 ; 0.020 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  4926 ; 0.003 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  9649 ; 1.552 ; 1.960       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 11921 ; 0.909 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   875 ; 4.677 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   332 ;37.280 ;23.253       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1228 ;15.062 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    68 ;20.253 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1076 ; 0.092 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7905 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1487 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  4405 ; 1.869 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1782 ; 0.771 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  7114 ; 3.306 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2729 ; 3.638 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2535 ; 5.425 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2): 12060 ; 2.702 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   184 ;14.877 ; 5.000       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2): 11926 ; 5.583 ; 5.000       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3NMN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-JUL-10.                  
REMARK 100 THE DEPOSITION ID IS D_1000060018.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5                                
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) : 1.00                               
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 : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 46283                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.150                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.0                               
REMARK 200  DATA REDUNDANCY                : 13.40                              
REMARK 200  R MERGE                    (I) : 0.09800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 49.1000                            
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: PDB ENTRY 3KDJ                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.91                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M AMMONIUM SULPHATE, 0.1M BISTRIS,    
REMARK 280  22% PEG 3350, PH 5.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE    
REMARK 280  293K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1880 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19200 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1810 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19980 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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     GLY A    34                                                      
REMARK 465     LYS A   158                                                      
REMARK 465     GLU A   159                                                      
REMARK 465     GLU A   160                                                      
REMARK 465     GLU A   161                                                      
REMARK 465     GLU A   162                                                      
REMARK 465     GLU A   163                                                      
REMARK 465     ARG A   164                                                      
REMARK 465     ARG A   210                                                      
REMARK 465     ASN A   211                                                      
REMARK 465     GLY B   116                                                      
REMARK 465     SER B   117                                                      
REMARK 465     ARG B   118                                                      
REMARK 465     SER B   119                                                      
REMARK 465     LEU B   120                                                      
REMARK 465     PHE B   121                                                      
REMARK 465     GLU B   122                                                      
REMARK 465     PHE B   123                                                      
REMARK 465     LYS B   124                                                      
REMARK 465     SER B   125                                                      
REMARK 465     SER B   155                                                      
REMARK 465     SER B   156                                                      
REMARK 465     GLY B   157                                                      
REMARK 465     SER B   158                                                      
REMARK 465     MET B   159                                                      
REMARK 465     LEU B   160                                                      
REMARK 465     ASP B   161                                                      
REMARK 465     GLY B   162                                                      
REMARK 465     ARG B   163                                                      
REMARK 465     PHE B   164                                                      
REMARK 465     CYS B   208                                                      
REMARK 465     LYS B   372                                                      
REMARK 465     ASN B   373                                                      
REMARK 465     ALA B   374                                                      
REMARK 465     VAL B   375                                                      
REMARK 465     ALA B   376                                                      
REMARK 465     GLY B   377                                                      
REMARK 465     ASP B   378                                                      
REMARK 465     ALA B   379                                                      
REMARK 465     SER B   380                                                      
REMARK 465     LEU B   381                                                      
REMARK 465     LEU B   382                                                      
REMARK 465     ALA B   383                                                      
REMARK 465     ASP B   384                                                      
REMARK 465     GLU B   385                                                      
REMARK 465     ARG B   386                                                      
REMARK 465     ARG B   387                                                      
REMARK 465     LYS B   388                                                      
REMARK 465     ARG B   425                                                      
REMARK 465     ARG B   426                                                      
REMARK 465     LYS B   427                                                      
REMARK 465     LEU B   428                                                      
REMARK 465     LYS B   429                                                      
REMARK 465     SER B   430                                                      
REMARK 465     LYS B   431                                                      
REMARK 465     PRO B   432                                                      
REMARK 465     LEU B   433                                                      
REMARK 465     ASN B   434                                                      
REMARK 465     GLY C    34                                                      
REMARK 465     LYS C   158                                                      
REMARK 465     GLU C   159                                                      
REMARK 465     GLU C   160                                                      
REMARK 465     GLU C   161                                                      
REMARK 465     GLU C   162                                                      
REMARK 465     GLU C   163                                                      
REMARK 465     GLY D   116                                                      
REMARK 465     SER D   117                                                      
REMARK 465     ARG D   118                                                      
REMARK 465     SER D   119                                                      
REMARK 465     LEU D   120                                                      
REMARK 465     PHE D   121                                                      
REMARK 465     GLU D   122                                                      
REMARK 465     PHE D   123                                                      
REMARK 465     LYS D   124                                                      
REMARK 465     SER D   155                                                      
REMARK 465     SER D   156                                                      
REMARK 465     GLY D   157                                                      
REMARK 465     SER D   158                                                      
REMARK 465     MET D   159                                                      
REMARK 465     LEU D   160                                                      
REMARK 465     ASP D   161                                                      
REMARK 465     GLY D   162                                                      
REMARK 465     ARG D   163                                                      
REMARK 465     PHE D   164                                                      
REMARK 465     VAL D   375                                                      
REMARK 465     ALA D   376                                                      
REMARK 465     GLY D   377                                                      
REMARK 465     ASP D   378                                                      
REMARK 465     ALA D   379                                                      
REMARK 465     SER D   380                                                      
REMARK 465     LEU D   381                                                      
REMARK 465     LEU D   382                                                      
REMARK 465     ALA D   383                                                      
REMARK 465     ASP D   384                                                      
REMARK 465     GLU D   385                                                      
REMARK 465     ARG D   386                                                      
REMARK 465     ARG D   387                                                      
REMARK 465     LYS D   388                                                      
REMARK 465     ARG D   425                                                      
REMARK 465     ARG D   426                                                      
REMARK 465     LYS D   427                                                      
REMARK 465     LEU D   428                                                      
REMARK 465     LYS D   429                                                      
REMARK 465     SER D   430                                                      
REMARK 465     LYS D   431                                                      
REMARK 465     PRO D   432                                                      
REMARK 465     LEU D   433                                                      
REMARK 465     ASN D   434                                                      
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   ND2  ASN C    54     O    GLU D   389     1455     2.16            
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    CYS A 104   CB    CYS A 104   SG     -0.149                       
REMARK 500    CYS B 259   CB    CYS B 259   SG     -0.157                       
REMARK 500    CYS D 259   CB    CYS D 259   SG     -0.136                       
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  54     -165.07     53.70                                   
REMARK 500    MET A 100       74.56   -117.67                                   
REMARK 500    HIS A 142     -176.52   -177.76                                   
REMARK 500    LEU A 144       68.08   -115.28                                   
REMARK 500    ARG B 137       42.51    -98.57                                   
REMARK 500    ARG B 150       50.80     33.15                                   
REMARK 500    GLN B 153      -72.52    -28.74                                   
REMARK 500    PRO B 166       17.59    -62.50                                   
REMARK 500    GLN B 167      -30.18   -145.35                                   
REMARK 500    LYS B 204       79.23     48.52                                   
REMARK 500    ARG B 268       75.47   -105.10                                   
REMARK 500    TRP B 300       77.31   -152.33                                   
REMARK 500    LEU C  52      -82.26    -89.96                                   
REMARK 500    ASN C  54     -147.87   -125.12                                   
REMARK 500    PHE C  88       -1.47     72.08                                   
REMARK 500    ASP C  97       33.22    -95.68                                   
REMARK 500    LEU C 126       97.11   -160.66                                   
REMARK 500    ASN C 209       48.29    -79.72                                   
REMARK 500    LEU D 152       42.37    -88.63                                   
REMARK 500    ARG D 191      -33.08   -131.86                                   
REMARK 500    LYS D 204       65.42     61.35                                   
REMARK 500    TRP D 300       81.61   -159.62                                   
REMARK 500    VAL D 308      -63.78    -91.96                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 998  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B  55   O                                                      
REMARK 620 2 ASP B 177   OD2 133.4                                              
REMARK 620 3 ASP B 347   OD1  89.4  75.3                                        
REMARK 620 4 ASP B 413   OD1  91.9 134.2 118.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 999  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 177   OD2                                                    
REMARK 620 2 ASP B 261   OD1 113.9                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG D 998  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D 177   OD2                                                    
REMARK 620 2 ASP D 261   OD1 114.8                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG D 999  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D 177   OD2                                                    
REMARK 620 2 ASP D 347   OD2 107.3                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PYV A 900                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 998                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 999                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PYV C 900                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 998                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 999                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3KAY   RELATED DB: PDB                                   
REMARK 900 APO PYL1 CRYSTAL STRUCTURE                                           
REMARK 900 RELATED ID: 3NMH   RELATED DB: PDB                                   
REMARK 900 PYRABACTIN BOUND PYL2                                                
REMARK 900 RELATED ID: 3NMP   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3NMT   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3NMV   RELATED DB: PDB                                   
DBREF  3NMN A   36   211  UNP    Q8VZS8   PYL1_ARATH      36    211             
DBREF  3NMN B  117   434  UNP    P49597   P2C56_ARATH    117    434             
DBREF  3NMN C   36   211  UNP    Q8VZS8   PYL1_ARATH      36    211             
DBREF  3NMN D  117   434  UNP    P49597   P2C56_ARATH    117    434             
SEQADV 3NMN GLY A   34  UNP  Q8VZS8              EXPRESSION TAG                 
SEQADV 3NMN SER A   35  UNP  Q8VZS8              EXPRESSION TAG                 
SEQADV 3NMN GLY B  116  UNP  P49597              EXPRESSION TAG                 
SEQADV 3NMN GLY C   34  UNP  Q8VZS8              EXPRESSION TAG                 
SEQADV 3NMN SER C   35  UNP  Q8VZS8              EXPRESSION TAG                 
SEQADV 3NMN GLY D  116  UNP  P49597              EXPRESSION TAG                 
SEQRES   1 A  178  GLY SER GLU PHE THR GLN LEU SER GLN SER ILE ALA GLU          
SEQRES   2 A  178  PHE HIS THR TYR GLN LEU GLY ASN GLY ARG CYS SER SER          
SEQRES   3 A  178  LEU LEU ALA GLN ARG ILE HIS ALA PRO PRO GLU THR VAL          
SEQRES   4 A  178  TRP SER VAL VAL ARG ARG PHE ASP ARG PRO GLN ILE TYR          
SEQRES   5 A  178  LYS HIS PHE ILE LYS SER CYS ASN VAL SER GLU ASP PHE          
SEQRES   6 A  178  GLU MET ARG VAL GLY CYS THR ARG ASP VAL ASN VAL ILE          
SEQRES   7 A  178  SER GLY LEU PRO ALA ASN THR SER ARG GLU ARG LEU ASP          
SEQRES   8 A  178  LEU LEU ASP ASP ASP ARG ARG VAL THR GLY PHE SER ILE          
SEQRES   9 A  178  THR GLY GLY GLU HIS ARG LEU ARG ASN TYR LYS SER VAL          
SEQRES  10 A  178  THR THR VAL HIS ARG PHE GLU LYS GLU GLU GLU GLU GLU          
SEQRES  11 A  178  ARG ILE TRP THR VAL VAL LEU GLU SER TYR VAL VAL ASP          
SEQRES  12 A  178  VAL PRO GLU GLY ASN SER GLU GLU ASP THR ARG LEU PHE          
SEQRES  13 A  178  ALA ASP THR VAL ILE ARG LEU ASN LEU GLN LYS LEU ALA          
SEQRES  14 A  178  SER ILE THR GLU ALA MET ASN ARG ASN                          
SEQRES   1 B  319  GLY SER ARG SER LEU PHE GLU PHE LYS SER VAL PRO LEU          
SEQRES   2 B  319  TYR GLY PHE THR SER ILE CYS GLY ARG ARG PRO GLU MET          
SEQRES   3 B  319  GLU ASP ALA VAL SER THR ILE PRO ARG PHE LEU GLN SER          
SEQRES   4 B  319  SER SER GLY SER MET LEU ASP GLY ARG PHE ASP PRO GLN          
SEQRES   5 B  319  SER ALA ALA HIS PHE PHE GLY VAL TYR ASP GLY HIS GLY          
SEQRES   6 B  319  GLY SER GLN VAL ALA ASN TYR CYS ARG GLU ARG MET HIS          
SEQRES   7 B  319  LEU ALA LEU ALA GLU GLU ILE ALA LYS GLU LYS PRO MET          
SEQRES   8 B  319  LEU CYS ASP GLY ASP THR TRP LEU GLU LYS TRP LYS LYS          
SEQRES   9 B  319  ALA LEU PHE ASN SER PHE LEU ARG VAL ASP SER GLU ILE          
SEQRES  10 B  319  GLU SER VAL ALA PRO GLU THR VAL GLY SER THR SER VAL          
SEQRES  11 B  319  VAL ALA VAL VAL PHE PRO SER HIS ILE PHE VAL ALA ASN          
SEQRES  12 B  319  CYS GLY ASP SER ARG ALA VAL LEU CYS ARG GLY LYS THR          
SEQRES  13 B  319  ALA LEU PRO LEU SER VAL ASP HIS LYS PRO ASP ARG GLU          
SEQRES  14 B  319  ASP GLU ALA ALA ARG ILE GLU ALA ALA GLY GLY LYS VAL          
SEQRES  15 B  319  ILE GLN TRP ASN GLY ALA ARG VAL PHE GLY VAL LEU ALA          
SEQRES  16 B  319  MET SER ARG SER ILE GLY ASP ARG TYR LEU LYS PRO SER          
SEQRES  17 B  319  ILE ILE PRO ASP PRO GLU VAL THR ALA VAL LYS ARG VAL          
SEQRES  18 B  319  LYS GLU ASP ASP CYS LEU ILE LEU ALA SER ASP GLY VAL          
SEQRES  19 B  319  TRP ASP VAL MET THR ASP GLU GLU ALA CYS GLU MET ALA          
SEQRES  20 B  319  ARG LYS ARG ILE LEU LEU TRP HIS LYS LYS ASN ALA VAL          
SEQRES  21 B  319  ALA GLY ASP ALA SER LEU LEU ALA ASP GLU ARG ARG LYS          
SEQRES  22 B  319  GLU GLY LYS ASP PRO ALA ALA MET SER ALA ALA GLU TYR          
SEQRES  23 B  319  LEU SER LYS LEU ALA ILE GLN ARG GLY SER LYS ASP ASN          
SEQRES  24 B  319  ILE SER VAL VAL VAL VAL ASP LEU LYS PRO ARG ARG LYS          
SEQRES  25 B  319  LEU LYS SER LYS PRO LEU ASN                                  
SEQRES   1 C  178  GLY SER GLU PHE THR GLN LEU SER GLN SER ILE ALA GLU          
SEQRES   2 C  178  PHE HIS THR TYR GLN LEU GLY ASN GLY ARG CYS SER SER          
SEQRES   3 C  178  LEU LEU ALA GLN ARG ILE HIS ALA PRO PRO GLU THR VAL          
SEQRES   4 C  178  TRP SER VAL VAL ARG ARG PHE ASP ARG PRO GLN ILE TYR          
SEQRES   5 C  178  LYS HIS PHE ILE LYS SER CYS ASN VAL SER GLU ASP PHE          
SEQRES   6 C  178  GLU MET ARG VAL GLY CYS THR ARG ASP VAL ASN VAL ILE          
SEQRES   7 C  178  SER GLY LEU PRO ALA ASN THR SER ARG GLU ARG LEU ASP          
SEQRES   8 C  178  LEU LEU ASP ASP ASP ARG ARG VAL THR GLY PHE SER ILE          
SEQRES   9 C  178  THR GLY GLY GLU HIS ARG LEU ARG ASN TYR LYS SER VAL          
SEQRES  10 C  178  THR THR VAL HIS ARG PHE GLU LYS GLU GLU GLU GLU GLU          
SEQRES  11 C  178  ARG ILE TRP THR VAL VAL LEU GLU SER TYR VAL VAL ASP          
SEQRES  12 C  178  VAL PRO GLU GLY ASN SER GLU GLU ASP THR ARG LEU PHE          
SEQRES  13 C  178  ALA ASP THR VAL ILE ARG LEU ASN LEU GLN LYS LEU ALA          
SEQRES  14 C  178  SER ILE THR GLU ALA MET ASN ARG ASN                          
SEQRES   1 D  319  GLY SER ARG SER LEU PHE GLU PHE LYS SER VAL PRO LEU          
SEQRES   2 D  319  TYR GLY PHE THR SER ILE CYS GLY ARG ARG PRO GLU MET          
SEQRES   3 D  319  GLU ASP ALA VAL SER THR ILE PRO ARG PHE LEU GLN SER          
SEQRES   4 D  319  SER SER GLY SER MET LEU ASP GLY ARG PHE ASP PRO GLN          
SEQRES   5 D  319  SER ALA ALA HIS PHE PHE GLY VAL TYR ASP GLY HIS GLY          
SEQRES   6 D  319  GLY SER GLN VAL ALA ASN TYR CYS ARG GLU ARG MET HIS          
SEQRES   7 D  319  LEU ALA LEU ALA GLU GLU ILE ALA LYS GLU LYS PRO MET          
SEQRES   8 D  319  LEU CYS ASP GLY ASP THR TRP LEU GLU LYS TRP LYS LYS          
SEQRES   9 D  319  ALA LEU PHE ASN SER PHE LEU ARG VAL ASP SER GLU ILE          
SEQRES  10 D  319  GLU SER VAL ALA PRO GLU THR VAL GLY SER THR SER VAL          
SEQRES  11 D  319  VAL ALA VAL VAL PHE PRO SER HIS ILE PHE VAL ALA ASN          
SEQRES  12 D  319  CYS GLY ASP SER ARG ALA VAL LEU CYS ARG GLY LYS THR          
SEQRES  13 D  319  ALA LEU PRO LEU SER VAL ASP HIS LYS PRO ASP ARG GLU          
SEQRES  14 D  319  ASP GLU ALA ALA ARG ILE GLU ALA ALA GLY GLY LYS VAL          
SEQRES  15 D  319  ILE GLN TRP ASN GLY ALA ARG VAL PHE GLY VAL LEU ALA          
SEQRES  16 D  319  MET SER ARG SER ILE GLY ASP ARG TYR LEU LYS PRO SER          
SEQRES  17 D  319  ILE ILE PRO ASP PRO GLU VAL THR ALA VAL LYS ARG VAL          
SEQRES  18 D  319  LYS GLU ASP ASP CYS LEU ILE LEU ALA SER ASP GLY VAL          
SEQRES  19 D  319  TRP ASP VAL MET THR ASP GLU GLU ALA CYS GLU MET ALA          
SEQRES  20 D  319  ARG LYS ARG ILE LEU LEU TRP HIS LYS LYS ASN ALA VAL          
SEQRES  21 D  319  ALA GLY ASP ALA SER LEU LEU ALA ASP GLU ARG ARG LYS          
SEQRES  22 D  319  GLU GLY LYS ASP PRO ALA ALA MET SER ALA ALA GLU TYR          
SEQRES  23 D  319  LEU SER LYS LEU ALA ILE GLN ARG GLY SER LYS ASP ASN          
SEQRES  24 D  319  ILE SER VAL VAL VAL VAL ASP LEU LYS PRO ARG ARG LYS          
SEQRES  25 D  319  LEU LYS SER LYS PRO LEU ASN                                  
HET    PYV  A 900      22                                                       
HET     MG  B 998       1                                                       
HET     MG  B 999       1                                                       
HET    PYV  C 900      22                                                       
HET     MG  D 998       1                                                       
HET     MG  D 999       1                                                       
HETNAM     PYV 4-BROMO-N-(PYRIDIN-2-YLMETHYL)NAPHTHALENE-1-SULFONAMIDE          
HETNAM      MG MAGNESIUM ION                                                    
HETSYN     PYV PYRABACTIN                                                       
FORMUL   5  PYV    2(C16 H13 BR N2 O2 S)                                        
FORMUL   6   MG    4(MG 2+)                                                     
FORMUL  11  HOH   *180(H2 O)                                                    
HELIX    1   1 SER A   35  HIS A   48  1                                  14    
HELIX    2   2 PRO A   68  ARG A   77  1                                  10    
HELIX    3   3 ARG A   81  TYR A   85  5                                   5    
HELIX    4   4 SER A  182  ASN A  209  1                                  28    
HELIX    5   5 SER B  182  LYS B  204  1                                  23    
HELIX    6   6 GLY B  210  SER B  234  1                                  25    
HELIX    7   7 ARG B  283  GLY B  294  1                                  12    
HELIX    8   8 ARG B  318  LYS B  321  5                                   4    
HELIX    9   9 SER B  346  ASP B  351  1                                   6    
HELIX   10  10 THR B  354  HIS B  370  1                                  17    
HELIX   11  11 ASP B  392  ARG B  409  1                                  18    
HELIX   12  12 GLU C   36  PHE C   47  1                                  12    
HELIX   13  13 PRO C   68  ARG C   77  1                                  10    
HELIX   14  14 ARG C   81  TYR C   85  5                                   5    
HELIX   15  15 SER C  182  ASN C  209  1                                  28    
HELIX   16  16 ARG D  150  SER D  154  5                                   5    
HELIX   17  17 SER D  182  LYS D  202  1                                  21    
HELIX   18  18 MET D  206  ASP D  209  5                                   4    
HELIX   19  19 GLY D  210  GLU D  233  1                                  24    
HELIX   20  20 ARG D  283  GLY D  294  1                                  12    
HELIX   21  21 ARG D  318  LYS D  321  5                                   4    
HELIX   22  22 SER D  346  ASP D  351  1                                   6    
HELIX   23  23 THR D  354  HIS D  370  1                                  17    
HELIX   24  24 ASP D  392  ARG D  409  1                                  18    
SHEET    1   A 7 ARG A  56  ILE A  65  0                                        
SHEET    2   A 7 TRP A 166  ASP A 176 -1  O  VAL A 175   N  CYS A  57           
SHEET    3   A 7 LYS A 148  PHE A 156 -1  N  LYS A 148   O  VAL A 174           
SHEET    4   A 7 VAL A 132  GLY A 139 -1  N  THR A 133   O  THR A 151           
SHEET    5   A 7 THR A 118  ASP A 127 -1  N  ASP A 127   O  VAL A 132           
SHEET    6   A 7 THR A 105  VAL A 110 -1  N  VAL A 108   O  SER A 119           
SHEET    7   A 7 ILE A  89  ASN A  93 -1  N  ASN A  93   O  ASP A 107           
SHEET    1   B 5 LEU B 128  ILE B 134  0                                        
SHEET    2   B 5 ILE B 415  ASP B 421 -1  O  ASP B 421   N  LEU B 128           
SHEET    3   B 5 ASP B 339  ALA B 345 -1  N  LEU B 342   O  VAL B 420           
SHEET    4   B 5 ARG B 263  ARG B 268 -1  N  VAL B 265   O  ILE B 343           
SHEET    5   B 5 ALA B 272  PRO B 274 -1  O  LEU B 273   N  LEU B 266           
SHEET    1   C 4 ASP B 143  ILE B 148  0                                        
SHEET    2   C 4 HIS B 171  HIS B 179 -1  O  PHE B 172   N  ILE B 148           
SHEET    3   C 4 GLY B 241  SER B 242 -1  O  GLY B 241   N  HIS B 179           
SHEET    4   C 4 ILE B 315  GLY B 316 -1  O  ILE B 315   N  SER B 242           
SHEET    1   D 5 ASP B 143  ILE B 148  0                                        
SHEET    2   D 5 HIS B 171  HIS B 179 -1  O  PHE B 172   N  ILE B 148           
SHEET    3   D 5 SER B 244  VAL B 249 -1  O  ALA B 247   N  PHE B 173           
SHEET    4   D 5 HIS B 253  CYS B 259 -1  O  PHE B 255   N  VAL B 248           
SHEET    5   D 5 GLU B 329  LYS B 334 -1  O  VAL B 333   N  ILE B 254           
SHEET    1   E 2 VAL B 297  GLN B 299  0                                        
SHEET    2   E 2 ALA B 303  VAL B 305 -1  O  ARG B 304   N  ILE B 298           
SHEET    1   F 7 ARG C  56  ILE C  65  0                                        
SHEET    2   F 7 TRP C 166  ASP C 176 -1  O  GLU C 171   N  LEU C  61           
SHEET    3   F 7 LYS C 148  PHE C 156 -1  N  LYS C 148   O  VAL C 174           
SHEET    4   F 7 VAL C 132  GLY C 139 -1  N  THR C 133   O  THR C 151           
SHEET    5   F 7 THR C 118  ASP C 127 -1  N  ARG C 120   O  THR C 138           
SHEET    6   F 7 THR C 105  VAL C 110 -1  N  VAL C 108   O  SER C 119           
SHEET    7   F 7 ILE C  89  ASN C  93 -1  N  ASN C  93   O  ASP C 107           
SHEET    1   G 5 TYR D 129  ILE D 134  0                                        
SHEET    2   G 5 ILE D 415  ASP D 421 -1  O  VAL D 417   N  THR D 132           
SHEET    3   G 5 ASP D 339  ALA D 345 -1  N  LEU D 344   O  VAL D 418           
SHEET    4   G 5 ARG D 263  ARG D 268 -1  N  VAL D 265   O  ILE D 343           
SHEET    5   G 5 THR D 271  PRO D 274 -1  O  LEU D 273   N  LEU D 266           
SHEET    1   H 4 ASP D 143  ILE D 148  0                                        
SHEET    2   H 4 HIS D 171  HIS D 179 -1  O  PHE D 172   N  ILE D 148           
SHEET    3   H 4 GLY D 241  VAL D 249 -1  O  ALA D 247   N  PHE D 173           
SHEET    4   H 4 ILE D 315  GLY D 316 -1  O  ILE D 315   N  SER D 242           
SHEET    1   I 5 ASP D 143  ILE D 148  0                                        
SHEET    2   I 5 HIS D 171  HIS D 179 -1  O  PHE D 172   N  ILE D 148           
SHEET    3   I 5 GLY D 241  VAL D 249 -1  O  ALA D 247   N  PHE D 173           
SHEET    4   I 5 HIS D 253  CYS D 259 -1  O  ALA D 257   N  VAL D 246           
SHEET    5   I 5 GLU D 329  LYS D 334 -1  O  THR D 331   N  VAL D 256           
SHEET    1   J 2 VAL D 297  GLN D 299  0                                        
SHEET    2   J 2 ALA D 303  VAL D 305 -1  O  ARG D 304   N  ILE D 298           
SSBOND   1 CYS D  267    CYS D  359                          1555   1555  2.11  
LINK         O   HOH B  55                MG    MG B 998     1555   1555  2.70  
LINK         OD2 ASP B 177                MG    MG B 998     1555   1555  2.36  
LINK         OD2 ASP B 177                MG    MG B 999     1555   1555  2.62  
LINK         OD1 ASP B 261                MG    MG B 999     1555   1555  2.69  
LINK         OD1 ASP B 347                MG    MG B 998     1555   1555  2.51  
LINK         OD1 ASP B 413                MG    MG B 998     1555   1555  3.00  
LINK         OD2 ASP D 177                MG    MG D 998     1555   1555  2.58  
LINK         OD2 ASP D 177                MG    MG D 999     1555   1555  2.58  
LINK         OD1 ASP D 261                MG    MG D 998     1555   1555  2.48  
LINK         OD2 ASP D 347                MG    MG D 999     1555   1555  2.44  
CISPEP   1 LYS B  321    PRO B  322          0        -2.93                     
CISPEP   2 LYS D  321    PRO D  322          0        -3.98                     
SITE     1 AC1 10 VAL A 108  ALA A 116  SER A 119  GLU A 121                    
SITE     2 AC1 10 HIS A 142  LEU A 144  TYR A 147  PHE A 189                    
SITE     3 AC1 10 VAL A 193  HOH A 219                                          
SITE     1 AC2  4 HOH B  55  ASP B 177  ASP B 347  ASP B 413                    
SITE     1 AC3  4 ASP B 177  ASP B 261  SER B 262  ASP B 347                    
SITE     1 AC4 12 HOH C   7  ILE C  89  VAL C 108  LEU C 114                    
SITE     2 AC4 12 ALA C 116  SER C 119  GLU C 121  LEU C 144                    
SITE     3 AC4 12 TYR C 147  PHE C 189  VAL C 193  HOH C 214                    
SITE     1 AC5  6 HOH D  57  ASP D 177  ASP D 261  SER D 262                    
SITE     2 AC5  6 SER D 346  ASP D 347                                          
SITE     1 AC6  5 ASP D 177  SER D 346  ASP D 347  GLY D 348                    
SITE     2 AC6  5 ASN D 414                                                     
CRYST1   59.978   66.710   72.598 115.78  95.43 105.60 P 1           2          
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      0.016673  0.004655  0.004355        0.00000                         
SCALE2      0.000000  0.015564  0.008519        0.00000                         
SCALE3      0.000000  0.000000  0.015774        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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