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Database: PDB
Entry: 3LNT
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Original site: 3LNT 
HEADER    ISOMERASE                               03-FEB-10   3LNT              
TITLE     CRYSTAL STRUCTURE OF PHOSPHOGLYCEROMUTASE FROM BURKHOLDERIA           
TITLE    2 PSEUDOMALLEI 1710B WITH BOUND MALONIC ACID                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 2,3-BISPHOSPHOGLYCERATE-DEPENDENT PHOSPHOGLYCERATE MUTASE; 
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: PHOSPHOGLYCEROMUTASE, PGAM, BPG-DEPENDENT PGAM, DPGM;       
COMPND   5 EC: 5.4.2.1;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BURKHOLDERIA PSEUDOMALLEI;                      
SOURCE   3 ORGANISM_TAXID: 320372;                                              
SOURCE   4 STRAIN: 1710B;                                                       
SOURCE   5 GENE: GPMA, BURPS1710B_0662;                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    MUTASE, PHOSPHOGLYCERYLMUTASE, SEATTLE STRUCTURAL GENOMICS CENTER FOR 
KEYWDS   2 INFECTIOUS DISEASE, SSGCID, GLYCOLYSIS, ISOMERASE                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE (SSGCID)    
REVDAT   2   05-OCT-11 3LNT    1       JRNL   VERSN                             
REVDAT   1   09-FEB-10 3LNT    0                                                
JRNL        AUTH   D.R.DAVIES,B.L.STAKER,J.A.ABENDROTH,T.E.EDWARDS,R.HARTLEY,   
JRNL        AUTH 2 J.LEONARD,H.KIM,A.L.RYCHEL,S.N.HEWITT,P.J.MYLER,L.J.STEWART  
JRNL        TITL   AN ENSEMBLE OF STRUCTURES OF BURKHOLDERIA PSEUDOMALLEI       
JRNL        TITL 2 2,3-BISPHOSPHOGLYCERATE-DEPENDENT PHOSPHOGLYCERATE MUTASE.   
JRNL        REF    ACTA CRYSTALLOGR.,SECT.F      V.  67  1044 2011              
JRNL        REFN                   ESSN 1744-3091                               
JRNL        PMID   21904048                                                     
JRNL        DOI    10.1107/S1744309111030405                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0104                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.34                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 49078                          
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) : 0.172                           
REMARK   3   R VALUE            (WORKING SET) : 0.170                           
REMARK   3   FREE R VALUE                     : 0.196                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2481                            
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) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.15                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3405                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.89                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2220                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 189                          
REMARK   3   BIN FREE R VALUE                    : 0.2510                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3765                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 27                                      
REMARK   3   SOLVENT ATOMS            : 256                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 33.37                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 27.65                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.02000                                              
REMARK   3    B22 (A**2) : 0.02000                                              
REMARK   3    B33 (A**2) : -0.02000                                             
REMARK   3    B12 (A**2) : 0.01000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.134         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.124         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.083         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.918         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.960                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.948                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3928 ; 0.015 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5355 ; 1.385 ; 1.963       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   486 ; 6.179 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   187 ;35.936 ;23.476       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   644 ;13.217 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    34 ;19.039 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   585 ; 0.092 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3038 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
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):  2387 ; 0.738 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3850 ; 1.324 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1541 ; 2.179 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1498 ; 3.483 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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  : 10                                         
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A    87                          
REMARK   3    ORIGIN FOR THE GROUP (A): -28.2611 -23.4626  -7.5301              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0587 T22:   0.0786                                     
REMARK   3      T33:   0.0773 T12:  -0.0003                                     
REMARK   3      T13:   0.0108 T23:  -0.0139                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6547 L22:   0.4551                                     
REMARK   3      L33:   0.6499 L12:   0.0487                                     
REMARK   3      L13:   0.0958 L23:   0.2745                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0121 S12:   0.0967 S13:  -0.0241                       
REMARK   3      S21:  -0.0094 S22:   0.0049 S23:  -0.0242                       
REMARK   3      S31:  -0.0322 S32:   0.0440 S33:  -0.0170                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    88        A   108                          
REMARK   3    ORIGIN FOR THE GROUP (A): -14.9641 -11.7181   9.4300              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0770 T22:   0.1354                                     
REMARK   3      T33:   0.0906 T12:  -0.0380                                     
REMARK   3      T13:  -0.0399 T23:  -0.0461                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8415 L22:   4.4591                                     
REMARK   3      L33:   1.3977 L12:   2.2986                                     
REMARK   3      L13:  -0.9386 L23:  -1.8127                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0370 S12:   0.0032 S13:  -0.1879                       
REMARK   3      S21:   0.3719 S22:   0.0137 S23:  -0.3278                       
REMARK   3      S31:  -0.2079 S32:   0.2260 S33:   0.0234                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   109        A   187                          
REMARK   3    ORIGIN FOR THE GROUP (A): -27.0607 -24.8346   8.7168              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0597 T22:   0.0482                                     
REMARK   3      T33:   0.0746 T12:   0.0081                                     
REMARK   3      T13:   0.0019 T23:   0.0064                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7635 L22:   1.2455                                     
REMARK   3      L33:   1.1273 L12:   0.1334                                     
REMARK   3      L13:   0.0783 L23:   0.8071                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0038 S12:  -0.0577 S13:  -0.0623                       
REMARK   3      S21:   0.0937 S22:   0.0245 S23:  -0.0975                       
REMARK   3      S31:   0.0726 S32:   0.0459 S33:  -0.0283                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   188        A   227                          
REMARK   3    ORIGIN FOR THE GROUP (A): -17.2783 -36.1021  -1.9443              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0309 T22:   0.0593                                     
REMARK   3      T33:   0.1296 T12:   0.0271                                     
REMARK   3      T13:   0.0200 T23:   0.0031                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0219 L22:   0.6306                                     
REMARK   3      L33:   0.7047 L12:  -0.0146                                     
REMARK   3      L13:  -0.1117 L23:   0.0335                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0117 S12:  -0.0428 S13:  -0.1914                       
REMARK   3      S21:  -0.0073 S22:   0.0577 S23:  -0.0144                       
REMARK   3      S31:  -0.0130 S32:   0.1103 S33:  -0.0460                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   228        A   244                          
REMARK   3    ORIGIN FOR THE GROUP (A): -10.4439 -24.7451 -10.9749              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0491 T22:   0.0834                                     
REMARK   3      T33:   0.0961 T12:   0.0261                                     
REMARK   3      T13:   0.0287 T23:  -0.0004                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.0900 L22:   2.1907                                     
REMARK   3      L33:   0.4123 L12:   0.6700                                     
REMARK   3      L13:  -0.0667 L23:   0.9213                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0021 S12:   0.0820 S13:  -0.0077                       
REMARK   3      S21:   0.1420 S22:   0.0275 S23:  -0.0591                       
REMARK   3      S31:   0.0635 S32:   0.0096 S33:  -0.0296                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     1        B    88                          
REMARK   3    ORIGIN FOR THE GROUP (A): -47.2729 -17.9332 -14.4280              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0846 T22:   0.0681                                     
REMARK   3      T33:   0.0507 T12:  -0.0050                                     
REMARK   3      T13:  -0.0126 T23:   0.0181                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7513 L22:   0.4469                                     
REMARK   3      L33:   1.0518 L12:  -0.1667                                     
REMARK   3      L13:   0.5398 L23:   0.2309                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0682 S12:   0.0181 S13:   0.0529                       
REMARK   3      S21:  -0.0569 S22:   0.0761 S23:  -0.0079                       
REMARK   3      S31:  -0.0871 S32:  -0.0088 S33:  -0.0078                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    89        B   114                          
REMARK   3    ORIGIN FOR THE GROUP (A): -60.0363 -24.2640 -36.2654              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1598 T22:   0.0744                                     
REMARK   3      T33:   0.0384 T12:  -0.0117                                     
REMARK   3      T13:  -0.0553 T23:   0.0010                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5750 L22:   0.3206                                     
REMARK   3      L33:   2.0071 L12:   0.6912                                     
REMARK   3      L13:  -0.2318 L23:   0.0806                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0612 S12:   0.1124 S13:   0.0661                       
REMARK   3      S21:  -0.0430 S22:   0.0500 S23:   0.0338                       
REMARK   3      S31:  -0.2809 S32:   0.2279 S33:   0.0112                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   115        B   161                          
REMARK   3    ORIGIN FOR THE GROUP (A): -56.1488 -34.3249 -23.2371              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0712 T22:   0.1014                                     
REMARK   3      T33:   0.0688 T12:  -0.0167                                     
REMARK   3      T13:  -0.0643 T23:   0.0125                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3403 L22:   0.9024                                     
REMARK   3      L33:   1.8481 L12:   0.1821                                     
REMARK   3      L13:   0.9401 L23:   1.2007                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2901 S12:   0.0473 S13:  -0.3321                       
REMARK   3      S21:   0.0099 S22:  -0.0734 S23:  -0.0891                       
REMARK   3      S31:   0.1165 S32:  -0.1483 S33:  -0.2168                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   162        B   186                          
REMARK   3    ORIGIN FOR THE GROUP (A): -56.0395 -24.1784  -5.1987              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0275 T22:   0.1322                                     
REMARK   3      T33:   0.0789 T12:   0.0255                                     
REMARK   3      T13:  -0.0152 T23:   0.0450                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0691 L22:   1.6525                                     
REMARK   3      L33:   3.1836 L12:   0.2667                                     
REMARK   3      L13:  -0.2620 L23:   0.0577                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0091 S12:  -0.0043 S13:   0.0303                       
REMARK   3      S21:   0.0077 S22:   0.0323 S23:   0.2171                       
REMARK   3      S31:  -0.0951 S32:  -0.1047 S33:  -0.0413                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   187        B   229                          
REMARK   3    ORIGIN FOR THE GROUP (A): -63.4265 -15.8646 -10.7778              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0368 T22:   0.2196                                     
REMARK   3      T33:   0.1265 T12:   0.0468                                     
REMARK   3      T13:  -0.0257 T23:   0.0947                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6627 L22:   0.4307                                     
REMARK   3      L33:   1.5026 L12:   0.9925                                     
REMARK   3      L13:   1.6834 L23:   0.7516                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2026 S12:   0.0004 S13:   0.2547                       
REMARK   3      S21:  -0.0997 S22:   0.0036 S23:   0.1590                       
REMARK   3      S31:  -0.2103 S32:  -0.2323 S33:   0.1990                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : 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          
REMARK   4                                                                      
REMARK   4 3LNT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-FEB-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB057507.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-DEC-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.00                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-E+ SUPERBRIGHT           
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU SATURN 944+                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 49080                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.340                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.08500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.8800                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.15                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.72100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 67.81                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.82                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.4 M SODIUM MALONATE, PH 7.0. CRYSTAL   
REMARK 280  TRANSFERRED TO 2.4 M MALONATE, PH 7.0 PLUS 25% (V/V) ETHYLENE       
REMARK 280  GLYCOL FOR CRYOPROTECTION, VAPOR DIFFUSION, SITTING DROP,           
REMARK 280  TEMPERATURE 289K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/6                                            
REMARK 290       6555   X-Y,X,Z+5/6                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       69.11333            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       34.55667            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       51.83500            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       17.27833            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       86.39167            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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   245                                                      
REMARK 465     LYS A   246                                                      
REMARK 465     SER A   247                                                      
REMARK 465     ALA A   248                                                      
REMARK 465     ALA A   249                                                      
REMARK 465     SER B     0                                                      
REMARK 465     ASP B   230                                                      
REMARK 465     GLN B   231                                                      
REMARK 465     GLU B   232                                                      
REMARK 465     ALA B   233                                                      
REMARK 465     ILE B   234                                                      
REMARK 465     ALA B   235                                                      
REMARK 465     LYS B   236                                                      
REMARK 465     ALA B   237                                                      
REMARK 465     GLN B   238                                                      
REMARK 465     ALA B   239                                                      
REMARK 465     ALA B   240                                                      
REMARK 465     VAL B   241                                                      
REMARK 465     ALA B   242                                                      
REMARK 465     GLN B   243                                                      
REMARK 465     GLN B   244                                                      
REMARK 465     GLY B   245                                                      
REMARK 465     LYS B   246                                                      
REMARK 465     SER B   247                                                      
REMARK 465     ALA B   248                                                      
REMARK 465     ALA B   249                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A 108    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  98    CG   CD   CE   NZ                                   
REMARK 470     GLU B 129    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 218    CG   CD   OE1  OE2                                  
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   OE2  GLU B   165     O    HOH B   363              2.15            
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   O    HOH A   375     O    HOH A   387     5555     2.11            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    THR A  21      -60.40   -109.42                                   
REMARK 500    GLU A  87      154.79    -47.91                                   
REMARK 500    SER A 166      -54.60   -126.92                                   
REMARK 500    ALA A 181     -137.79   -147.33                                   
REMARK 500    GLU B  87      153.72    -49.90                                   
REMARK 500    SER B 166      -53.09   -135.49                                   
REMARK 500    ALA B 181     -140.93   -147.64                                   
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                              NA A 250  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 284   O                                                      
REMARK 620 2 HOH A 252   O    97.3                                              
REMARK 620 3 HOH A 259   O   116.5 145.5                                        
REMARK 620 4 HOH A 281   O    96.9 108.6  75.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 250                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MLI A 990                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MLI B 990                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 250                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 251                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 251                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3GW8   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF PHOSPHOGLYCEROMUTASE FROM BURKHOLDERIA          
REMARK 900 PSEUDOMALLEI WITH VANADATE AND GLYCEROL                              
REMARK 900 RELATED ID: 3GP3   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF PHOSPHOGLYCEROMUTASE FROM BURKHOLDERIA          
REMARK 900 PSEUDOMALLEI WITH 2-PHOSPHOSERINE                                    
REMARK 900 RELATED ID: 3GP5   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF PHOSPHOGLYCEROMUTASE FROM BURKHOLDERIA          
REMARK 900 PSEUDOMALLEI WITH 3-PHOSPHOGLYCERIC ACID AND VANADATE                
REMARK 900 RELATED ID: 3FDZ   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF PHOSPHOGLYCEROMUTASE FROM BURKHOLDERIA          
REMARK 900 PSEUDOMALLEI 1710B WITH BOUND 2,3-DIPHOSPHOGLYCERIC ACID             
REMARK 900 AND 3-PHOSPHOGLYCERIC ACID                                           
REMARK 900 RELATED ID: 3EZN   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF PHOSPHOGLYCEROMUTASE FROM BURKHOLDERIA          
REMARK 900 PSEUDOMALLEI 1710B                                                   
REMARK 900 RELATED ID: BUPSA.00114.A   RELATED DB: TARGETDB                     
DBREF  3LNT A    1   249  UNP    Q3JWH7   GPMA_BURP1       1    249             
DBREF  3LNT B    1   249  UNP    Q3JWH7   GPMA_BURP1       1    249             
SEQADV 3LNT SER A    0  UNP  Q3JWH7              EXPRESSION TAG                 
SEQADV 3LNT SER B    0  UNP  Q3JWH7              EXPRESSION TAG                 
SEQRES   1 A  250  SER MET TYR LYS LEU VAL LEU ILE ARG HIS GLY GLU SER          
SEQRES   2 A  250  THR TRP ASN LYS GLU ASN ARG PHE THR GLY TRP VAL ASP          
SEQRES   3 A  250  VAL ASP LEU THR GLU GLN GLY ASN ARG GLU ALA ARG GLN          
SEQRES   4 A  250  ALA GLY GLN LEU LEU LYS GLU ALA GLY TYR THR PHE ASP          
SEQRES   5 A  250  ILE ALA TYR THR SER VAL LEU LYS ARG ALA ILE ARG THR          
SEQRES   6 A  250  LEU TRP HIS VAL GLN ASP GLN MET ASP LEU MET TYR VAL          
SEQRES   7 A  250  PRO VAL VAL HIS SER TRP ARG LEU ASN GLU ARG HIS TYR          
SEQRES   8 A  250  GLY ALA LEU SER GLY LEU ASN LYS ALA GLU THR ALA ALA          
SEQRES   9 A  250  LYS TYR GLY ASP GLU GLN VAL LEU VAL TRP ARG ARG SER          
SEQRES  10 A  250  TYR ASP THR PRO PRO PRO ALA LEU GLU PRO GLY ASP GLU          
SEQRES  11 A  250  ARG ALA PRO TYR ALA ASP PRO ARG TYR ALA LYS VAL PRO          
SEQRES  12 A  250  ARG GLU GLN LEU PRO LEU THR GLU CYS LEU LYS ASP THR          
SEQRES  13 A  250  VAL ALA ARG VAL LEU PRO LEU TRP ASN GLU SER ILE ALA          
SEQRES  14 A  250  PRO ALA VAL LYS ALA GLY LYS GLN VAL LEU ILE ALA ALA          
SEQRES  15 A  250  HIS GLY ASN SER LEU ARG ALA LEU ILE LYS TYR LEU ASP          
SEQRES  16 A  250  GLY ILE SER ASP ALA ASP ILE VAL GLY LEU ASN ILE PRO          
SEQRES  17 A  250  ASN GLY VAL PRO LEU VAL TYR GLU LEU ASP GLU SER LEU          
SEQRES  18 A  250  THR PRO ILE ARG HIS TYR TYR LEU GLY ASP GLN GLU ALA          
SEQRES  19 A  250  ILE ALA LYS ALA GLN ALA ALA VAL ALA GLN GLN GLY LYS          
SEQRES  20 A  250  SER ALA ALA                                                  
SEQRES   1 B  250  SER MET TYR LYS LEU VAL LEU ILE ARG HIS GLY GLU SER          
SEQRES   2 B  250  THR TRP ASN LYS GLU ASN ARG PHE THR GLY TRP VAL ASP          
SEQRES   3 B  250  VAL ASP LEU THR GLU GLN GLY ASN ARG GLU ALA ARG GLN          
SEQRES   4 B  250  ALA GLY GLN LEU LEU LYS GLU ALA GLY TYR THR PHE ASP          
SEQRES   5 B  250  ILE ALA TYR THR SER VAL LEU LYS ARG ALA ILE ARG THR          
SEQRES   6 B  250  LEU TRP HIS VAL GLN ASP GLN MET ASP LEU MET TYR VAL          
SEQRES   7 B  250  PRO VAL VAL HIS SER TRP ARG LEU ASN GLU ARG HIS TYR          
SEQRES   8 B  250  GLY ALA LEU SER GLY LEU ASN LYS ALA GLU THR ALA ALA          
SEQRES   9 B  250  LYS TYR GLY ASP GLU GLN VAL LEU VAL TRP ARG ARG SER          
SEQRES  10 B  250  TYR ASP THR PRO PRO PRO ALA LEU GLU PRO GLY ASP GLU          
SEQRES  11 B  250  ARG ALA PRO TYR ALA ASP PRO ARG TYR ALA LYS VAL PRO          
SEQRES  12 B  250  ARG GLU GLN LEU PRO LEU THR GLU CYS LEU LYS ASP THR          
SEQRES  13 B  250  VAL ALA ARG VAL LEU PRO LEU TRP ASN GLU SER ILE ALA          
SEQRES  14 B  250  PRO ALA VAL LYS ALA GLY LYS GLN VAL LEU ILE ALA ALA          
SEQRES  15 B  250  HIS GLY ASN SER LEU ARG ALA LEU ILE LYS TYR LEU ASP          
SEQRES  16 B  250  GLY ILE SER ASP ALA ASP ILE VAL GLY LEU ASN ILE PRO          
SEQRES  17 B  250  ASN GLY VAL PRO LEU VAL TYR GLU LEU ASP GLU SER LEU          
SEQRES  18 B  250  THR PRO ILE ARG HIS TYR TYR LEU GLY ASP GLN GLU ALA          
SEQRES  19 B  250  ILE ALA LYS ALA GLN ALA ALA VAL ALA GLN GLN GLY LYS          
SEQRES  20 B  250  SER ALA ALA                                                  
HET     NA  A 250       1                                                       
HET    MLI  A 990       7                                                       
HET    EDO  A 251       4                                                       
HET    MLI  B 990       7                                                       
HET    EDO  B 250       4                                                       
HET    EDO  B 251       4                                                       
HETNAM      NA SODIUM ION                                                       
HETNAM     MLI MALONATE ION                                                     
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   3   NA    NA 1+                                                        
FORMUL   4  MLI    2(C3 H2 O4 2-)                                               
FORMUL   5  EDO    3(C2 H6 O2)                                                  
FORMUL   9  HOH   *256(H2 O)                                                    
HELIX    1   1 SER A   12  GLU A   17  1                                   6    
HELIX    2   2 THR A   29  ALA A   46  1                                  18    
HELIX    3   3 LEU A   58  ASP A   73  1                                  16    
HELIX    4   4 TRP A   83  ASN A   86  5                                   4    
HELIX    5   5 TYR A   90  SER A   94  5                                   5    
HELIX    6   6 ASN A   97  GLY A  106  1                                  10    
HELIX    7   7 GLY A  106  SER A  116  1                                  11    
HELIX    8   8 ASP A  135  ALA A  139  5                                   5    
HELIX    9   9 PRO A  142  LEU A  146  5                                   5    
HELIX   10  10 CYS A  151  SER A  166  1                                  16    
HELIX   11  11 SER A  166  ALA A  173  1                                   8    
HELIX   12  12 HIS A  182  ASP A  194  1                                  13    
HELIX   13  13 ASP A  200  LEU A  204  5                                   5    
HELIX   14  14 ASP A  230  GLN A  244  1                                  15    
HELIX   15  15 SER B   12  GLU B   17  1                                   6    
HELIX   16  16 THR B   29  ALA B   46  1                                  18    
HELIX   17  17 LEU B   58  ASP B   73  1                                  16    
HELIX   18  18 TRP B   83  ASN B   86  5                                   4    
HELIX   19  19 TYR B   90  SER B   94  5                                   5    
HELIX   20  20 ASN B   97  GLY B  106  1                                  10    
HELIX   21  21 GLY B  106  SER B  116  1                                  11    
HELIX   22  22 ASP B  135  ALA B  139  5                                   5    
HELIX   23  23 PRO B  142  LEU B  146  5                                   5    
HELIX   24  24 CYS B  151  LEU B  160  1                                  10    
HELIX   25  25 LEU B  160  SER B  166  1                                   7    
HELIX   26  26 SER B  166  ALA B  173  1                                   8    
HELIX   27  27 HIS B  182  ASP B  194  1                                  13    
HELIX   28  28 SER B  197  VAL B  202  1                                   6    
SHEET    1   A 6 VAL A  79  HIS A  81  0                                        
SHEET    2   A 6 ILE A  52  THR A  55  1  N  THR A  55   O  VAL A  80           
SHEET    3   A 6 VAL A 177  ALA A 181  1  O  LEU A 178   N  TYR A  54           
SHEET    4   A 6 TYR A   2  ARG A   8  1  N  ILE A   7   O  ALA A 181           
SHEET    5   A 6 LEU A 212  LEU A 216 -1  O  TYR A 214   N  LEU A   4           
SHEET    6   A 6 PRO A 222  TYR A 227 -1  O  ILE A 223   N  GLU A 215           
SHEET    1   B 6 VAL B  79  HIS B  81  0                                        
SHEET    2   B 6 ILE B  52  THR B  55  1  N  THR B  55   O  VAL B  80           
SHEET    3   B 6 VAL B 177  ALA B 181  1  O  LEU B 178   N  TYR B  54           
SHEET    4   B 6 TYR B   2  ARG B   8  1  N  ILE B   7   O  ALA B 181           
SHEET    5   B 6 LEU B 212  LEU B 216 -1  O  LEU B 212   N  LEU B   6           
SHEET    6   B 6 PRO B 222  TYR B 227 -1  O  TYR B 226   N  VAL B 213           
LINK        NA    NA A 250                 O   HOH A 284     1555   1555  2.65  
LINK        NA    NA A 250                 O   HOH A 252     1555   1555  2.68  
LINK        NA    NA A 250                 O   HOH A 259     1555   1555  2.75  
LINK        NA    NA A 250                 O   HOH A 281     1555   1555  3.11  
SITE     1 AC1  4 TRP A  23  HOH A 252  HOH A 259  HOH A 284                    
SITE     1 AC2 13 ARG A   8  HIS A   9  ASN A  15  ARG A  19                    
SITE     2 AC2 13 THR A  21  GLY A  22  GLU A  87  TYR A  90                    
SITE     3 AC2 13 HOH A 255  HOH A 268  HOH A 300  HOH A 304                    
SITE     4 AC2 13 HOH A 360                                                     
SITE     1 AC3 12 ARG B   8  HIS B   9  ASN B  15  ARG B  19                    
SITE     2 AC3 12 THR B  21  GLY B  22  GLU B  87  TYR B  90                    
SITE     3 AC3 12 HOH B 273  HOH B 322  HOH B 327  HOH B 359                    
SITE     1 AC4  4 EDO A 251  ARG B  63  TRP B  66  HIS B  67                    
SITE     1 AC5  3 ARG A  63  HIS A  67  EDO B 250                               
SITE     1 AC6  6 VAL A  79  HOH A 260  PRO B  78  VAL B  79                    
SITE     2 AC6  6 ARG B 115  HOH B 289                                          
CRYST1  119.620  119.620  103.670  90.00  90.00 120.00 P 65         12          
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      0.008360  0.004827  0.000000        0.00000                         
SCALE2      0.000000  0.009653  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009646        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system