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Database: PDB
Entry: 3DMS
LinkDB: 3DMS
Original site: 3DMS 
HEADER    OXIDOREDUCTASE                          01-JUL-08   3DMS              
TITLE     1.65A CRYSTAL STRUCTURE OF ISOCITRATE DEHYDROGENASE FROM BURKHOLDERIA 
TITLE    2 PSEUDOMALLEI                                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ISOCITRATE DEHYDROGENASE [NADP];                           
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 1.1.1.42;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BURKHOLDERIA PSEUDOMALLEI;                      
SOURCE   3 ORGANISM_COMMON: PSEUDOMONAS PSEUDOMALLEI;                           
SOURCE   4 ORGANISM_TAXID: 28450;                                               
SOURCE   5 STRAIN: 1710B;                                                       
SOURCE   6 GENE: ICD, BPSL0896;                                                 
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: BG1861RC                                  
KEYWDS    BURKHOLDERIA, PSEUDOMALLEI, ISOCITRATE, DEHYDROGENASE, STRUCTURAL     
KEYWDS   2 GENOMICS, SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE, 
KEYWDS   3 SSGCID, GLYOXYLATE BYPASS, MANGANESE, METAL-BINDING, NADP,           
KEYWDS   4 OXIDOREDUCTASE, TRICARBOXYLIC ACID CYCLE                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE (SSGCID)    
REVDAT   4   30-OCT-13 3DMS    1       REMARK                                   
REVDAT   3   05-OCT-11 3DMS    1       JRNL   VERSN                             
REVDAT   2   24-FEB-09 3DMS    1       VERSN                                    
REVDAT   1   15-JUL-08 3DMS    0                                                
JRNL        AUTH   S.P.YATES,T.E.EDWARDS,C.M.BRYAN,A.J.STEIN,W.C.VAN VOORHIS,   
JRNL        AUTH 2 P.J.MYLER,L.J.STEWART,J.ZHENG,Z.JIA                          
JRNL        TITL   STRUCTURAL BASIS OF THE SUBSTRATE SPECIFICITY OF             
JRNL        TITL 2 BIFUNCTIONAL ISOCITRATE DEHYDROGENASE KINASE/PHOSPHATASE.    
JRNL        REF    BIOCHEMISTRY                  V.  50  8103 2011              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   21870819                                                     
JRNL        DOI    10.1021/BI200809P                                            
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   L.BAUGH,L.A.GALLAGHER,R.PATRAPUVICH,M.C.CLIFTON,             
REMARK   1  AUTH 2 A.S.GARDBERG,T.E.EDWARDS,B.ARMOUR,D.W.BEGLEY,S.H.DIETERICH,  
REMARK   1  AUTH 3 D.M.DRANOW,J.ABENDROTH,J.W.FAIRMAN,D.FOX,B.L.STAKER,I.PHAN,  
REMARK   1  AUTH 4 A.GILLESPIE,R.CHOI,S.NAKAZAWA-HEWITT,M.T.NGUYEN,A.NAPULI,    
REMARK   1  AUTH 5 L.BARRETT,G.W.BUCHKO,R.STACY,P.J.MYLER,L.J.STEWART,C.MANOIL, 
REMARK   1  AUTH 6 W.C.VAN VOORHIS                                              
REMARK   1  TITL   COMBINING FUNCTIONAL AND STRUCTURAL GENOMICS TO SAMPLE THE   
REMARK   1  TITL 2 ESSENTIAL BURKHOLDERIA STRUCTOME.                            
REMARK   1  REF    PLOS ONE                      V.   8 53851 2013              
REMARK   1  REFN                   ESSN 1932-6203                               
REMARK   1  PMID   23382856                                                     
REMARK   1  DOI    10.1371/JOURNAL.PONE.0053851                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.65 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
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) : 1.65                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.69                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 47920                          
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) : 0.206                           
REMARK   3   R VALUE            (WORKING SET) : 0.205                           
REMARK   3   FREE R VALUE                     : 0.234                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2427                            
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) : 1.65                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.69                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3346                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.09                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3460                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 154                          
REMARK   3   BIN FREE R VALUE                    : 0.4200                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3211                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 262                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.23                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.12000                                              
REMARK   3    B22 (A**2) : -0.04000                                             
REMARK   3    B33 (A**2) : -0.14000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.07000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.115         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.110         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.081         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.353         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.944                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3348 ; 0.007 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4540 ; 1.013 ; 1.970       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   431 ; 5.468 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   144 ;35.799 ;24.861       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   610 ;12.559 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    17 ;13.271 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   506 ; 0.070 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2511 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1548 ; 0.179 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2336 ; 0.301 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   221 ; 0.101 ; 0.200       
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):    93 ; 0.152 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    15 ; 0.106 ; 0.200       
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):  2158 ; 0.515 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3377 ; 0.804 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1365 ; 1.292 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1155 ; 2.072 ; 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):  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  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
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 3DMS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-JUL-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB048232.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-APR-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-D                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00                               
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL MONOCHROMATOR       
REMARK 200  OPTICS                         : ADJUSTABLE FOCUSING MIRRORS        
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL                                
REMARK 200  DATA SCALING SOFTWARE          : DTREK                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 47920                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.650                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.680                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 3.350                              
REMARK 200  R MERGE                    (I) : 0.04300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.71                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.79                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.28600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.45                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, 2M POTASSIUM FORMATE, PH   
REMARK 280  7, VAPOR DIFFUSION, TEMPERATURE 289K                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       51.99650            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       31.11900            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       51.99650            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       31.11900            
REMARK 290   SMTRY3   4  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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6790 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 32630 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -43.0 KCAL/MOL                        
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   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
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 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     MET A    -7                                                      
REMARK 465     ALA A    -6                                                      
REMARK 465     HIS A    -5                                                      
REMARK 465     HIS A    -4                                                      
REMARK 465     HIS A    -3                                                      
REMARK 465     HIS A    -2                                                      
REMARK 465     HIS A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     PRO A     2                                                      
REMARK 465     GLY A   110                                                      
REMARK 465     GLY A   111                                                      
REMARK 465     GLY A   112                                                      
REMARK 465     ILE A   113                                                      
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    PHE A  21       -5.30     77.42                                   
REMARK 500    VAL A  98      -59.78     75.32                                   
REMARK 500    THR A 106     -169.10   -109.84                                   
REMARK 500    GLU A 159     -143.69   -138.56                                   
REMARK 500    ASP A 160     -172.57     66.95                                   
REMARK 500    LYS A 232       54.88   -115.77                                   
REMARK 500    THR A 239      -75.24   -119.80                                   
REMARK 500    ASP A 299      -95.35   -138.49                                   
REMARK 500    ALA A 344       68.00     38.43                                   
REMARK 500    TRP A 371       58.87    -90.42                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: BUPSA.00092.A   RELATED DB: TARGETDB                     
DBREF  3DMS A    1   419  UNP    Q63WJ4   Q63WJ4_BURPS     1    419             
SEQADV 3DMS MET A   -7  UNP  Q63WJ4              EXPRESSION TAG                 
SEQADV 3DMS ALA A   -6  UNP  Q63WJ4              EXPRESSION TAG                 
SEQADV 3DMS HIS A   -5  UNP  Q63WJ4              EXPRESSION TAG                 
SEQADV 3DMS HIS A   -4  UNP  Q63WJ4              EXPRESSION TAG                 
SEQADV 3DMS HIS A   -3  UNP  Q63WJ4              EXPRESSION TAG                 
SEQADV 3DMS HIS A   -2  UNP  Q63WJ4              EXPRESSION TAG                 
SEQADV 3DMS HIS A   -1  UNP  Q63WJ4              EXPRESSION TAG                 
SEQADV 3DMS HIS A    0  UNP  Q63WJ4              EXPRESSION TAG                 
SEQRES   1 A  427  MET ALA HIS HIS HIS HIS HIS HIS MET PRO TYR GLN HIS          
SEQRES   2 A  427  ILE LYS VAL PRO GLU GLY GLY ASP LYS ILE THR VAL ASN          
SEQRES   3 A  427  LYS ASP PHE SER LEU ASN VAL SER ASP GLN PRO ILE ILE          
SEQRES   4 A  427  PRO TYR ILE GLU GLY ASP GLY THR GLY PHE ASP ILE THR          
SEQRES   5 A  427  PRO VAL MET ILE LYS VAL VAL ASP ALA ALA VAL GLU LYS          
SEQRES   6 A  427  ALA TYR GLY GLY LYS LYS LYS ILE HIS TRP MET GLU ILE          
SEQRES   7 A  427  TYR ALA GLY GLU LYS ALA THR LYS VAL TYR GLY PRO ASP          
SEQRES   8 A  427  VAL TRP LEU PRO GLU GLU THR LEU GLN VAL LEU LYS GLU          
SEQRES   9 A  427  TYR VAL VAL SER ILE LYS GLY PRO LEU THR THR PRO VAL          
SEQRES  10 A  427  GLY GLY GLY ILE ARG SER LEU ASN VAL ALA LEU ARG GLN          
SEQRES  11 A  427  GLU LEU ASP LEU TYR VAL CYS LEU ARG PRO ILE GLN TYR          
SEQRES  12 A  427  PHE LYS GLY VAL PRO SER PRO VAL ARG GLU PRO GLU LYS          
SEQRES  13 A  427  THR ASN MET VAL ILE PHE ARG GLU ASN SER GLU ASP ILE          
SEQRES  14 A  427  TYR ALA GLY ILE GLU TRP ALA ALA GLU SER GLU GLN ALA          
SEQRES  15 A  427  LYS LYS VAL ILE LYS PHE LEU GLN GLU GLU MET GLY VAL          
SEQRES  16 A  427  LYS LYS ILE ARG PHE PRO GLN THR SER GLY ILE GLY ILE          
SEQRES  17 A  427  LYS PRO VAL SER LYS GLU GLY THR GLU ARG LEU VAL ARG          
SEQRES  18 A  427  LYS ALA ILE GLN TYR ALA ILE ASP ASN ASP ARG LYS SER          
SEQRES  19 A  427  VAL THR LEU VAL HIS LYS GLY ASN ILE MET LYS PHE THR          
SEQRES  20 A  427  GLU GLY ALA PHE ARG ASP ALA GLY TYR ALA LEU ALA GLN          
SEQRES  21 A  427  LYS GLU PHE GLY ALA GLU LEU ILE ASP GLY GLY PRO TRP          
SEQRES  22 A  427  MET LYS PHE LYS ASN PRO LYS THR GLY ASN GLU ILE VAL          
SEQRES  23 A  427  VAL LYS ASP SER ILE ALA ASP ALA PHE LEU GLN GLN ILE          
SEQRES  24 A  427  LEU LEU ARG PRO ALA GLU TYR ASP VAL ILE ALA THR LEU          
SEQRES  25 A  427  ASN LEU ASN GLY ASP TYR ILE SER ASP ALA LEU ALA ALA          
SEQRES  26 A  427  GLN VAL GLY GLY ILE GLY ILE ALA PRO GLY ALA ASN LEU          
SEQRES  27 A  427  SER ASP SER VAL ALA MET PHE GLU ALA THR HIS GLY THR          
SEQRES  28 A  427  ALA PRO LYS TYR ALA GLY LYS ASP TYR VAL ASN PRO GLY          
SEQRES  29 A  427  SER GLU ILE LEU SER ALA GLU MET MET LEU ARG HIS LEU          
SEQRES  30 A  427  GLY TRP THR GLU ALA ALA ASP VAL ILE ILE SER ALA MET          
SEQRES  31 A  427  GLU LYS SER ILE LYS GLN LYS ARG VAL THR TYR ASP PHE          
SEQRES  32 A  427  ALA ARG LEU MET GLU GLY ALA THR GLN VAL SER CYS SER          
SEQRES  33 A  427  GLY PHE GLY GLN VAL LEU ILE GLU ASN MET GLU                  
FORMUL   2  HOH   *262(H2 O)                                                    
HELIX    1   1 THR A   39  GLY A   60  1                                  22    
HELIX    2   2 GLY A   73  GLY A   81  1                                   9    
HELIX    3   3 PRO A   87  TYR A   97  1                                  11    
HELIX    4   4 SER A  115  LEU A  124  1                                  10    
HELIX    5   5 GLU A  145  THR A  149  5                                   5    
HELIX    6   6 GLU A  159  GLY A  164  5                                   6    
HELIX    7   7 SER A  171  GLU A  184  1                                  14    
HELIX    8   8 PHE A  192  SER A  196  5                                   5    
HELIX    9   9 SER A  204  ASN A  222  1                                  19    
HELIX   10  10 THR A  239  GLY A  256  1                                  18    
HELIX   11  11 ALA A  284  ARG A  294  1                                  11    
HELIX   12  12 PRO A  295  TYR A  298  5                                   4    
HELIX   13  13 LEU A  304  VAL A  319  1                                  16    
HELIX   14  14 ALA A  344  ALA A  348  5                                   5    
HELIX   15  15 PRO A  355  LEU A  369  1                                  15    
HELIX   16  16 TRP A  371  LYS A  389  1                                  19    
HELIX   17  17 THR A  392  ARG A  397  1                                   6    
HELIX   18  18 SER A  406  ASN A  417  1                                  12    
SHEET    1   A 2 THR A  16  VAL A  17  0                                        
SHEET    2   A 2 LEU A  23  ASN A  24 -1  O  ASN A  24   N  THR A  16           
SHEET    1   B12 HIS A  66  GLU A  69  0                                        
SHEET    2   B12 ILE A  30  ILE A  34  1  N  ILE A  31   O  MET A  68           
SHEET    3   B12 VAL A  99  LYS A 102  1  O  ILE A 101   N  ILE A  34           
SHEET    4   B12 ALA A 335  ALA A 339  1  O  PHE A 337   N  SER A 100           
SHEET    5   B12 PRO A 326  LEU A 330 -1  N  ASN A 329   O  MET A 336           
SHEET    6   B12 VAL A 128  ILE A 133 -1  N  LEU A 130   O  ALA A 328           
SHEET    7   B12 MET A 151  GLU A 156 -1  O  MET A 151   N  ILE A 133           
SHEET    8   B12 VAL A 300  THR A 303  1  O  ILE A 301   N  PHE A 154           
SHEET    9   B12 SER A 226  HIS A 231  1  N  THR A 228   O  ALA A 302           
SHEET   10   B12 GLU A 276  ILE A 283  1  O  LYS A 280   N  LEU A 229           
SHEET   11   B12 MET A 266  LYS A 269 -1  N  PHE A 268   O  ILE A 277           
SHEET   12   B12 GLU A 258  LEU A 259 -1  N  GLU A 258   O  LYS A 267           
SHEET    1   C 2 GLU A 166  TRP A 167  0                                        
SHEET    2   C 2 ILE A 198  GLY A 199 -1  O  ILE A 198   N  TRP A 167           
SHEET    1   D 2 ARG A 390  VAL A 391  0                                        
SHEET    2   D 2 THR A 403  GLN A 404  1  O  THR A 403   N  VAL A 391           
CISPEP   1 GLY A  263    PRO A  264          0         5.58                     
CRYST1  103.993   62.238   70.998  90.00 118.52  90.00 C 1 2 1       4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.009616  0.000000  0.005226        0.00000                         
SCALE2      0.000000  0.016067  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016031        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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