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Database: PDB
Entry: 2V67
LinkDB: 2V67
Original site: 2V67 
ANISOU 3973  CD  LYS D 244    11235   8551   7762  -1561   -108    759       C  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
HEADER    HYDROLASE/DNA                           09-APR-00   1ESG              
TITLE     RESTRICTION ENDONUCLEASE BAMHI BOUND TO A NON-SPECIFIC DNA.           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DNA (5'-D(*TP*GP*GP*AP*TP*TP*CP*A)-3');                    
COMPND   3 CHAIN: C;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: DNA (5'-D(*TP*GP*AP*AP*TP*CP*CP*A)-3');                    
COMPND   7 CHAIN: D;                                                            
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 3;                                                           
COMPND  10 MOLECULE: TYPE II RESTRICTION ENZYME BAMHI;                          
COMPND  11 CHAIN: A, B;                                                         
COMPND  12 SYNONYM: ENDONUCLEASE BAMHI, R.BAMHI, TYPE II SITE-                  
COMPND  13 SPECIFIC DEOXYRIBONUCLEASE;                                          
COMPND  14 EC: 3.1.21.4;                                                        
COMPND  15 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 SYNTHETIC: YES;                                                      
SOURCE   3 OTHER_DETAILS: PHOSPHORAMITE SYNTHESIS;                              
SOURCE   4 MOL_ID: 2;                                                           
SOURCE   5 SYNTHETIC: YES;                                                      
SOURCE   6 OTHER_DETAILS: PHOSPHORAMITE SYNTHESIS;                              
SOURCE   7 MOL_ID: 3;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: BACILLUS AMYLOLIQUEFACIENS;                     
SOURCE   9 ORGANISM_TAXID: 1390;                                                
SOURCE  10 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  11 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    NON-SPECIFIC DNA-PROTEIN COMPLEX., HYDROLASE/DNA COMPLEX              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.VIADIU,A.K.AGGARWAL                                                 
REVDAT   3   24-FEB-09 1ESG    1       VERSN                                    
REVDAT   2   01-APR-03 1ESG    1       JRNL                                     
REVDAT   1   31-MAY-00 1ESG    0                                                
JRNL        AUTH   H.VIADIU,A.K.AGGARWAL                                        
JRNL        TITL   STRUCTURE OF BAMHI BOUND TO NONSPECIFIC DNA: A               
JRNL        TITL 2 MODEL FOR DNA SLIDING.                                       
JRNL        REF    MOL.CELL                      V.   5   889 2000              
JRNL        REFN                   ISSN 1097-2765                               
JRNL        PMID   10882125                                                     
JRNL        DOI    10.1016/S1097-2765(00)80329-9                                
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   H.VIADIU,R.KUCERA,I.SCHILDKRAUT,A.K.AGGARWAL                 
REMARK   1  TITL   A STEP TOWARDS UNDERSTANDING PROTEIN-DNA                     
REMARK   1  TITL 2 SPECIFICITY: CRYSTALLIZATION OF THE RESTRICTION              
REMARK   1  TITL 3 ENDONUCLEASE BAMHI WITH A NON-SPECIFIC DNA                   
REMARK   1  REF    TO BE PUBLISHED                            2000              
REMARK   1  REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : PROTEIN: ENGH & HUBER, DNA: PARKINSON ET        
REMARK   3                      AL.                                             
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 92.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 51166                          
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 SET) : 0.191                           
REMARK   3   FREE R VALUE                     : 0.230                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2574                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3414                                    
REMARK   3   NUCLEIC ACID ATOMS       : 322                                     
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 572                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.48                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1ESG COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-APR-00.                  
REMARK 100 THE RCSB ID CODE IS RCSB010853.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-JUL-98; 15-AUG-98; 15-AUG-      
REMARK 200                                   98                                 
REMARK 200  TEMPERATURE           (KELVIN) : 110; 110; 110                      
REMARK 200  PH                             : 4.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 3                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N; Y; Y                            
REMARK 200  RADIATION SOURCE               : ROTATING ANODE; CHESS; CHESS       
REMARK 200  BEAMLINE                       : NULL; A1; A1                       
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU; NULL; NULL                 
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; NULL; NULL                      
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418; 0.9100; 0.9100             
REMARK 200  MONOCHROMATOR                  : NULL; NULL; NULL                   
REMARK 200  OPTICS                         : NULL; NULL; NULL                   
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE; CCD; CCD              
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS; MACSCIENCE;          
REMARK 200                                   MACSCIENCE                         
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 53008                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 10.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.1                               
REMARK 200  DATA REDUNDANCY                : 4.400                              
REMARK 200  R MERGE                    (I) : 0.05700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 20.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.97                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 85.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.28400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; NULL; NULL                  
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.56                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.20                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% MPD, 10 MM SODIUM ACETATE (PH        
REMARK 280  4.8), 5 MM CACL2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE        
REMARK 280  20K                                                                 
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       57.40000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       33.20000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       45.55000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       33.20000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       57.40000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       45.55000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: A PROTEIN DIMER WITH A DOUBLE STRANDED DNA.                  
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: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, 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 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     VAL A   210                                                      
REMARK 465     GLU A   211                                                      
REMARK 465     ASN A   212                                                      
REMARK 465     LYS A   213                                                      
REMARK 465     LYS B   213                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    LYS B   200     O    HOH B   224              1.88            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    ASN B 187   CG    ASN B 187   OD1     1.269                       
REMARK 500    ASN B 187   CG    ASN B 187   ND2     0.221                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASN B 187   OD1 -  CG  -  ND2 ANGL. DEV. = -87.1 DEGREES          
REMARK 500    ASN B 187   CB  -  CG  -  OD1 ANGL. DEV. =  24.5 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS A  87      -88.71   -124.27                                   
REMARK 500    ASN A 187       40.73    -76.85                                   
REMARK 500    ASP A 196       44.42   -152.55                                   
REMARK 500    LYS A 207     -168.33   -116.94                                   
REMARK 500    ASP A 208       37.75   -174.97                                   
REMARK 500    GLU B 101       60.34   -102.61                                   
REMARK 500    ASN B 102      132.04     14.57                                   
REMARK 500    SER B 103      -22.28     99.27                                   
REMARK 500    LYS B 193     -100.81    -69.80                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH C 424        DISTANCE =  5.10 ANGSTROMS                       
REMARK 525    HOH B 443        DISTANCE =  7.24 ANGSTROMS                       
REMARK 525    HOH B 461        DISTANCE =  5.86 ANGSTROMS                       
REMARK 525    HOH B 467        DISTANCE =  5.22 ANGSTROMS                       
REMARK 525    HOH B 470        DISTANCE =  5.07 ANGSTROMS                       
REMARK 525    HOH A 472        DISTANCE =  6.58 ANGSTROMS                       
REMARK 525    HOH B 474        DISTANCE =  8.29 ANGSTROMS                       
REMARK 525    HOH A 486        DISTANCE =  5.91 ANGSTROMS                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1BAM   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2BAM   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3BAM   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1BHM   RELATED DB: PDB                                   
DBREF  1ESG A    1   213  UNP    P23940   T2BA_BACAM       1    213             
DBREF  1ESG B    1   213  UNP    P23940   T2BA_BACAM       1    213             
DBREF  1ESG C    1     8  PDB    1ESG     1ESG             1      8             
DBREF  1ESG D    1     8  PDB    1ESG     1ESG             1      8             
SEQRES   1 C    8   DT  DG  DG  DA  DT  DT  DC  DA                              
SEQRES   1 D    8   DT  DG  DA  DA  DT  DC  DC  DA                              
SEQRES   1 A  213  MET GLU VAL GLU LYS GLU PHE ILE THR ASP GLU ALA LYS          
SEQRES   2 A  213  GLU LEU LEU SER LYS ASP LYS LEU ILE GLN GLN ALA TYR          
SEQRES   3 A  213  ASN GLU VAL LYS THR SER ILE CYS SER PRO ILE TRP PRO          
SEQRES   4 A  213  ALA THR SER LYS THR PHE THR ILE ASN ASN THR GLU LYS          
SEQRES   5 A  213  ASN CYS ASN GLY VAL VAL PRO ILE LYS GLU LEU CYS TYR          
SEQRES   6 A  213  THR LEU LEU GLU ASP THR TYR ASN TRP TYR ARG GLU LYS          
SEQRES   7 A  213  PRO LEU ASP ILE LEU LYS LEU GLU LYS LYS LYS GLY GLY          
SEQRES   8 A  213  PRO ILE ASP VAL TYR LYS GLU PHE ILE GLU ASN SER GLU          
SEQRES   9 A  213  LEU LYS ARG VAL GLY MET GLU PHE GLU THR GLY ASN ILE          
SEQRES  10 A  213  SER SER ALA HIS ARG SER MET ASN LYS LEU LEU LEU GLY          
SEQRES  11 A  213  LEU LYS HIS GLY GLU ILE ASP LEU ALA ILE ILE LEU MET          
SEQRES  12 A  213  PRO ILE LYS GLN LEU ALA TYR TYR LEU THR ASP ARG VAL          
SEQRES  13 A  213  THR ASN PHE GLU GLU LEU GLU PRO TYR PHE GLU LEU THR          
SEQRES  14 A  213  GLU GLY GLN PRO PHE ILE PHE ILE GLY PHE ASN ALA GLU          
SEQRES  15 A  213  ALA TYR ASN SER ASN VAL PRO LEU ILE PRO LYS GLY SER          
SEQRES  16 A  213  ASP GLY MET SER LYS ARG SER ILE LYS LYS TRP LYS ASP          
SEQRES  17 A  213  LYS VAL GLU ASN LYS                                          
SEQRES   1 B  213  MET GLU VAL GLU LYS GLU PHE ILE THR ASP GLU ALA LYS          
SEQRES   2 B  213  GLU LEU LEU SER LYS ASP LYS LEU ILE GLN GLN ALA TYR          
SEQRES   3 B  213  ASN GLU VAL LYS THR SER ILE CYS SER PRO ILE TRP PRO          
SEQRES   4 B  213  ALA THR SER LYS THR PHE THR ILE ASN ASN THR GLU LYS          
SEQRES   5 B  213  ASN CYS ASN GLY VAL VAL PRO ILE LYS GLU LEU CYS TYR          
SEQRES   6 B  213  THR LEU LEU GLU ASP THR TYR ASN TRP TYR ARG GLU LYS          
SEQRES   7 B  213  PRO LEU ASP ILE LEU LYS LEU GLU LYS LYS LYS GLY GLY          
SEQRES   8 B  213  PRO ILE ASP VAL TYR LYS GLU PHE ILE GLU ASN SER GLU          
SEQRES   9 B  213  LEU LYS ARG VAL GLY MET GLU PHE GLU THR GLY ASN ILE          
SEQRES  10 B  213  SER SER ALA HIS ARG SER MET ASN LYS LEU LEU LEU GLY          
SEQRES  11 B  213  LEU LYS HIS GLY GLU ILE ASP LEU ALA ILE ILE LEU MET          
SEQRES  12 B  213  PRO ILE LYS GLN LEU ALA TYR TYR LEU THR ASP ARG VAL          
SEQRES  13 B  213  THR ASN PHE GLU GLU LEU GLU PRO TYR PHE GLU LEU THR          
SEQRES  14 B  213  GLU GLY GLN PRO PHE ILE PHE ILE GLY PHE ASN ALA GLU          
SEQRES  15 B  213  ALA TYR ASN SER ASN VAL PRO LEU ILE PRO LYS GLY SER          
SEQRES  16 B  213  ASP GLY MET SER LYS ARG SER ILE LYS LYS TRP LYS ASP          
SEQRES  17 B  213  LYS VAL GLU ASN LYS                                          
FORMUL   5  HOH   *579(H2 O)                                                    
HELIX    1   1 THR A    9  ASP A   19  1                                  11    
HELIX    2   2 ASP A   19  SER A   35  1                                  17    
HELIX    3   3 VAL A   57  ASN A   73  1                                  17    
HELIX    4   4 LYS A   78  LEU A   85  1                                   8    
HELIX    5   5 ASN A  116  HIS A  133  1                                  18    
HELIX    6   6 ILE A  145  TYR A  150  1                                   6    
HELIX    7   7 ASN A  158  GLU A  163  1                                   6    
HELIX    8   8 PRO A  164  GLU A  170  5                                   7    
HELIX    9   9 SER A  199  TRP A  206  1                                   8    
HELIX   10  10 THR B    9  ASP B   19  1                                  11    
HELIX   11  11 ASP B   19  SER B   35  1                                  17    
HELIX   12  12 VAL B   57  ASN B   73  1                                  17    
HELIX   13  13 LYS B   78  GLU B   86  1                                   9    
HELIX   14  14 ASN B  116  HIS B  133  1                                  18    
HELIX   15  15 ILE B  145  TYR B  150  1                                   6    
HELIX   16  16 ASN B  158  GLU B  163  1                                   6    
HELIX   17  17 PRO B  164  GLU B  170  5                                   7    
HELIX   18  18 ARG B  201  ASN B  212  1                                  12    
SHEET    1   A 6 GLU A   2  ILE A   8  0                                        
SHEET    2   A 6 PHE A 174  ASN A 180 -1  N  PHE A 176   O  PHE A   7           
SHEET    3   A 6 LEU A 138  PRO A 144  1  O  ALA A 139   N  ILE A 175           
SHEET    4   A 6 LEU A 105  PHE A 112  1  O  ARG A 107   N  LEU A 138           
SHEET    5   A 6 VAL A  95  ILE A 100 -1  O  VAL A  95   N  MET A 110           
SHEET    6   A 6 TYR A  75  ARG A  76 -1  N  TYR A  75   O  TYR A  96           
SHEET    1   B 2 THR A  46  ASN A  48  0                                        
SHEET    2   B 2 ALA A 183  ASN A 185  1  O  ALA A 183   N  ILE A  47           
SHEET    1   C 6 GLU B   2  ILE B   8  0                                        
SHEET    2   C 6 PHE B 174  ASN B 180 -1  N  PHE B 176   O  PHE B   7           
SHEET    3   C 6 LEU B 138  PRO B 144  1  O  ALA B 139   N  ILE B 175           
SHEET    4   C 6 LEU B 105  PHE B 112  1  O  ARG B 107   N  LEU B 138           
SHEET    5   C 6 VAL B  95  ILE B 100 -1  O  VAL B  95   N  MET B 110           
SHEET    6   C 6 TYR B  75  ARG B  76 -1  N  TYR B  75   O  TYR B  96           
SHEET    1   D 2 THR B  46  ASN B  48  0                                        
SHEET    2   D 2 ALA B 183  ASN B 185  1  O  ALA B 183   N  ILE B  47           
CISPEP   1 TRP A   38    PRO A   39          0        -0.10                     
CISPEP   2 TRP B   38    PRO B   39          0        -0.10                     
CRYST1  114.800   91.100   66.400  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.008711  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010977  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015060        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
HEADER    ION CHANNEL INHIBITOR                   10-APR-06   2CK4              
TITLE     SOLUTION STRUCTURE OF AOSK1                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: POTASSIUM CHANNEL TOXIN ALPHA-KTX 3.7;                     
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: TOXIN OSK1, OSK-1;                                          
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 SYNTHETIC: YES;                                                      
SOURCE   3 ORGANISM_SCIENTIFIC: ORTHOCHIRUS SCROBICULOSUS;                      
SOURCE   4 ORGANISM_COMMON: CENTRAL ASIAN SCORPION;                             
SOURCE   5 ORGANISM_TAXID: 6892                                                 
KEYWDS    ION CHANNEL INHIBITOR, POTASSIUM CHANNEL INHIBITOR, ION               
KEYWDS   2 CHANNEL BLOCKER, IONIC CHANNEL INHIBITOR, OSK1, TOXIN,               
KEYWDS   3 NEUROTOXIN, SCORPIO TOXIN                                            
EXPDTA    SOLUTION NMR                                                          
NUMMDL    20                                                                    
AUTHOR    S.ALPHONSE,S.MOUHAT,J.M.SABATIER,H.DARBON,C.BERNARD                   
REVDAT   2   24-FEB-09 2CK4    1       VERSN                                    
REVDAT   1   15-MAY-07 2CK4    0                                                
JRNL        AUTH   S.ALPHONSE,S.MOUHAT,J.M.SABATIER,H.DARBON,C.BERNARD          
JRNL        TITL   SOLUTION STRUCTURE OF TWO ANALOGUES OF THE OSK1              
JRNL        TITL 2 TOXIN                                                        
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION. NOT APPLICABLE.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : ARIA                                                 
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS, GROSSE-             
REMARK   3                 KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,READ,        
REMARK   3                 RICE,SIMONSON,WARREN                                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: WATER REFINEMENT USING THE OPLSX          
REMARK   3  FORCEFIELD.                                                         
REMARK   4                                                                      
REMARK   4 2CK4 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-APR-06.                  
REMARK 100 THE PDBE ID CODE IS EBI-28455.                                       
REMARK 210                                                                      
REMARK 210 EXPERIMENTAL DETAILS                                                 
REMARK 210  EXPERIMENT TYPE                : NMR                                
REMARK 210  TEMPERATURE           (KELVIN) : 300.0 ; 300.0 ; 300.0              
REMARK 210  PH                             : 3.5 ; NULL ; NULL                  
REMARK 210  IONIC STRENGTH                 : NULL ; NULL ; NULL                 
REMARK 210  PRESSURE                       : 1.0 ; 1.0 ; 1.0                    
REMARK 210  SAMPLE CONTENTS                : 90%WATER,10%D2O                    
REMARK 210                                                                      
REMARK 210  NMR EXPERIMENTS CONDUCTED      : NOESY ; TOCSY ; COSY               
REMARK 210  SPECTROMETER FIELD STRENGTH    : 500 ; 500 ; 500                    
REMARK 210  SPECTROMETER MODEL             : OTHER ; OTHER ; OTHER              
REMARK 210  SPECTROMETER MANUFACTURER      : BRUKER ; BRUKER ; BRUKER           
REMARK 210                                                                      
REMARK 210  STRUCTURE DETERMINATION.                                            
REMARK 210   SOFTWARE USED                 : NMRVIEW                            
REMARK 210   METHOD USED                   : ARIA                               
REMARK 210                                                                      
REMARK 210 CONFORMERS, NUMBER CALCULATED   : 50                                 
REMARK 210 CONFORMERS, NUMBER SUBMITTED    : 20                                 
REMARK 210 CONFORMERS, SELECTION CRITERIA  : LEAST RESTRAINT VIOLATION          
REMARK 210                                                                      
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 14                  
REMARK 210                                                                      
REMARK 210 REMARK: NONE                                                         
REMARK 215                                                                      
REMARK 215 NMR STUDY                                                            
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION           
REMARK 215 NMR DATA.  PROTEIN DATA BANK CONVENTIONS REQUIRE THAT                
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON              
REMARK 215 THESE RECORDS ARE MEANINGLESS.                                       
REMARK 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, GLU 16 TO LYS                         
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, LYS 20 TO ASP                         
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   HA   ASN A     5  -  HG3  LYS A    32              1.54            
REMARK 500   HB3  CYS A    14  -  HB3  CYS A    33              1.56            
REMARK 500   HB3  CYS A    18  -  HB2  MET A    23              1.57            
REMARK 500   HB3  ARG A    24  -  HA   LYS A    38              1.42            
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 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  4 LYS A   7      104.21    -58.04                                   
REMARK 500  6 ASN A   5       33.43    -81.42                                   
REMARK 500  7 ASN A   5       31.06    -79.76                                   
REMARK 500  8 ILE A  10      142.72   -174.70                                   
REMARK 500  9 ASN A   5       39.90    -83.10                                   
REMARK 500 10 LYS A   7       96.33    -69.29                                   
REMARK 500 11 ASN A   5       45.25    -86.03                                   
REMARK 500 12 CYS A   8       85.07    -66.33                                   
REMARK 500 14 ASN A   5       48.96    -86.66                                   
REMARK 500 15 LYS A   7      102.57    -55.53                                   
REMARK 500 19 CYS A   8       98.46    -58.79                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1SCO   RELATED DB: PDB                                   
REMARK 900  SCORPION TOXIN (OSK1 TOXIN) WITH HIGH                               
REMARK 900  AFFINITY FOR SMALL CONDUCTANCE CA(2+)-                              
REMARK 900  ACTIVATED K+ CHANNEL IN NEUROBLASTOMA-X-                            
REMARK 900  GLUOMA NG 108-15 HYBRID CELLS, NMR, 30                              
REMARK 900  STRUCTURES                                                          
REMARK 900 RELATED ID: 2CK5   RELATED DB: PDB                                   
REMARK 900  SOLUTION STRUCTURE OF DELTA 1-7 AOSK1                               
DBREF  2CK4 A    1    38  UNP    P55896   KAX37_ORTSC      1     38             
SEQADV 2CK4 LYS A   16  UNP  P55896    GLU    16 ENGINEERED MUTATION            
SEQADV 2CK4 ASP A   20  UNP  P55896    LYS    20 ENGINEERED MUTATION            
SEQRES   1 A   38  GLY VAL ILE ILE ASN VAL LYS CYS LYS ILE SER ARG GLN          
SEQRES   2 A   38  CYS LEU LYS PRO CYS LYS ASP ALA GLY MET ARG PHE GLY          
SEQRES   3 A   38  LYS CYS MET ASN GLY LYS CYS HIS CYS THR PRO LYS              
HELIX    1   1 SER A   11  ASP A   20  1                                  10    
SHEET    1  AA 3 VAL A   2  ILE A   4  0                                        
SHEET    2  AA 3 LYS A  32  CYS A  35 -1  O  CYS A  33   N  ILE A   4           
SHEET    3  AA 3 LYS A  27  MET A  29 -1  O  LYS A  27   N  HIS A  34           
SSBOND   1 CYS A    8    CYS A   28                          1555   1555  2.02  
SSBOND   2 CYS A   14    CYS A   33                          1555   1555  2.03  
SSBOND   3 CYS A   18    CYS A   35                          1555   1555  2.03  
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1           1          
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      1.000000  0.000000  0.000000        0.00000                         
SCALE2      0.000000  1.000000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  1.000000        0.00000                         
MODEL        1                                                                  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
HEADER    VIRAL PROTEIN                           14-SEP-12   2LYA              
TITLE     STRUCTURE OF HIV-1 MYR(-) MATRIX PROTEIN IN COMPLEX WITH 1,2-         
TITLE    2 DIOCTANOYL-SN-PHOSPHATIDYLCHOLINE                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MATRIX PROTEIN P17;                                        
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: MA, GAG-POL POLYPROTEIN;                                    
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS TYPE 1;            
SOURCE   3 ORGANISM_TAXID: 11698;                                               
SOURCE   4 STRAIN: NEW YORK-5 ISOLATE;                                          
SOURCE   5 GENE: GAG-POL;                                                       
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR: PET-11A                                    
KEYWDS    GAG, MATRIX, PLASMA MEMBRANE, LIPID, VIRAL PROTEIN                    
EXPDTA    SOLUTION NMR                                                          
NUMMDL    20                                                                    
AUTHOR    J.VLACH,J.SAAD                                                        
REVDAT   3   03-APR-13 2LYA    1       JRNL                                     
REVDAT   2   06-MAR-13 2LYA    1       JRNL                                     
REVDAT   1   13-FEB-13 2LYA    0                                                
JRNL        AUTH   J.VLACH,J.S.SAAD                                             
JRNL        TITL   TRIO ENGAGEMENT VIA PLASMA MEMBRANE PHOSPHOLIPIDS AND THE    
JRNL        TITL 2 MYRISTOYL MOIETY GOVERNS HIV-1 MATRIX BINDING TO BILAYERS.   
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 110  3525 2013              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   23401539                                                     
JRNL        DOI    10.1073/PNAS.1216655110                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION. NOT APPLICABLE.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CYANA 2.1                                            
REMARK   3   AUTHORS     : GUNTERT, MUMENTHALER AND WUTHRICH                    
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2LYA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-SEP-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB102983.                                      
REMARK 210                                                                      
REMARK 210 EXPERIMENTAL DETAILS                                                 
REMARK 210  EXPERIMENT TYPE                : NMR                                
REMARK 210  TEMPERATURE           (KELVIN) : 308                                
REMARK 210  PH                             : 5.5                                
REMARK 210  IONIC STRENGTH                 : 50                                 
REMARK 210  PRESSURE                       : AMBIENT                            
REMARK 210  SAMPLE CONTENTS                : 0.4 MM [U-95% 13C] MA, 0.8-1.0     
REMARK 210  MM 1,2-DIOCTANOYL-SN-GLYCERO-3-PHOSPHOCHOLINE, 50 MM SODIUM         
REMARK 210  PHOSPHATE, 2 MM DTT, 90% H2O/10% D2O; 0.4-1.0 MM [U-95% 13C; U-     
REMARK 210  95% 15N] MA, 0.8-1.0 MM 1,2-DIOCTANOYL-SN-GLYCERO-3-                
REMARK 210  PHOSPHOCHOLINE, 50 MM SODIUM PHOSPHATE, 2 MM DTT, 90% H2O/10% D2O   
REMARK 210                                                                      
REMARK 210  NMR EXPERIMENTS CONDUCTED      : 3D 13C-EDITED/13C-FILTERED         
REMARK 210                                   NOESY; 3D HCCH-TOCSY; 2D 1H-13C    
REMARK 210                                   HSQC; 3D HNCA; 3D HN(CO)CA; 3D     
REMARK 210                                   HNCACB; 3D CBCA(CO)NH; 3D 1H-15N   
REMARK 210                                   TOCSY; 3D 1H-15N NOESY; 3D 1H-13C  
REMARK 210                                   NOESY; 2D 1H-15N HSQC              
REMARK 210  SPECTROMETER FIELD STRENGTH    : 700 MHZ                            
REMARK 210  SPECTROMETER MODEL             : AVANCE II                          
REMARK 210  SPECTROMETER MANUFACTURER      : BRUKER                             
REMARK 210                                                                      
REMARK 210  STRUCTURE DETERMINATION.                                            
REMARK 210   SOFTWARE USED                 : CYANA 2.1, TOPSPIN, NMRPIPE,       
REMARK 210                                   CCPN_ANALYSIS                      
REMARK 210   METHOD USED                   : SIMULATED ANNEALING, TORSION       
REMARK 210                                   ANGLE DYNAMICS                     
REMARK 210                                                                      
REMARK 210 CONFORMERS, NUMBER CALCULATED   : 100                                
REMARK 210 CONFORMERS, NUMBER SUBMITTED    : 20                                 
REMARK 210 CONFORMERS, SELECTION CRITERIA  : STRUCTURES WITH THE LOWEST ENERGY  
REMARK 210                                                                      
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1                   
REMARK 210                                                                      
REMARK 210 REMARK: NULL                                                         
REMARK 215                                                                      
REMARK 215 NMR STUDY                                                            
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION           
REMARK 215 NMR DATA.  PROTEIN DATA BANK CONVENTIONS REQUIRE THAT                
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON              
REMARK 215 THESE RECORDS ARE MEANINGLESS.                                       
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 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. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;                   
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                            
REMARK 465   MODELS 1-20                                                        
REMARK 465     RES C SSSEQI                                                     
REMARK 465     HIS A   133                                                      
REMARK 465     HIS A   134                                                      
REMARK 465     HIS A   135                                                      
REMARK 465     HIS A   136                                                      
REMARK 465     HIS A   137                                                      
REMARK 465     HIS A   138                                                      
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  1 SER A   6       79.42   -164.09                                   
REMARK 500  1 SER A   9     -171.37    -66.88                                   
REMARK 500  1 GLN A 116       34.28   -158.47                                   
REMARK 500  1 ALA A 119       50.16    -94.37                                   
REMARK 500  1 ALA A 120       56.29   -146.96                                   
REMARK 500  1 ASP A 121       26.99   -145.12                                   
REMARK 500  1 VAL A 128      142.23   -171.02                                   
REMARK 500  1 ASN A 131       56.99   -141.28                                   
REMARK 500  2 ALA A   3       47.21   -105.36                                   
REMARK 500  2 ARG A   4       94.49     57.75                                   
REMARK 500  2 SER A   9     -171.38    -69.21                                   
REMARK 500  2 GLN A  90      -72.39    -99.10                                   
REMARK 500  2 ARG A  91      -36.01   -179.07                                   
REMARK 500  2 ALA A 118      -43.73   -171.82                                   
REMARK 500  2 ASP A 121       70.11   -109.60                                   
REMARK 500  3 ALA A   3      176.54     61.43                                   
REMARK 500  3 ALA A   5      -46.30   -141.74                                   
REMARK 500  3 THR A  70       31.40    -95.49                                   
REMARK 500  3 SER A  72     -178.44    -63.83                                   
REMARK 500  3 GLN A  90      -73.69    -92.57                                   
REMARK 500  3 ARG A  91      -35.33   -179.28                                   
REMARK 500  3 ASP A  93       64.06   -114.93                                   
REMARK 500  3 ALA A 115       26.55   -143.86                                   
REMARK 500  3 GLN A 116      -70.03   -123.13                                   
REMARK 500  3 ALA A 118      -44.23   -176.51                                   
REMARK 500  3 ASN A 131      167.98     61.95                                   
REMARK 500  4 ALA A   3      -42.98   -155.81                                   
REMARK 500  4 ALA A 119       59.30   -111.87                                   
REMARK 500  4 ALA A 120       64.48   -174.65                                   
REMARK 500  4 ASP A 121       42.71   -173.82                                   
REMARK 500  5 ALA A   3       25.20   -143.59                                   
REMARK 500  5 ARG A   4      -61.44   -124.29                                   
REMARK 500  5 ALA A   5      102.24   -167.96                                   
REMARK 500  5 SER A   9     -171.78    -65.76                                   
REMARK 500  5 THR A  70       30.79    -95.54                                   
REMARK 500  5 GLN A  90      -74.06   -102.46                                   
REMARK 500  5 ARG A  91      -35.18   -179.09                                   
REMARK 500  5 ALA A 115       33.57   -141.13                                   
REMARK 500  5 ALA A 120      -50.90   -165.89                                   
REMARK 500  5 ASN A 125      108.57    -58.77                                   
REMARK 500  6 ALA A 119       44.57    -92.23                                   
REMARK 500  6 ALA A 120     -170.82   -177.75                                   
REMARK 500  6 ASN A 131      128.11   -173.87                                   
REMARK 500  7 ARG A   4       56.47   -152.11                                   
REMARK 500  7 ALA A   5      176.99     62.33                                   
REMARK 500  7 SER A   6      164.13     63.09                                   
REMARK 500  7 VAL A   7      -62.70    -91.18                                   
REMARK 500  7 ALA A 118      -40.55   -172.10                                   
REMARK 500  8 GLN A  90      -74.72    -79.66                                   
REMARK 500  8 ARG A  91       34.51   -179.40                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     134 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PC8 A 300                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 18715   RELATED DB: BMRB                                 
REMARK 900 RELATED ID: 2LYB   RELATED DB: PDB                                   
DBREF  2LYA A    2   132  UNP    P12497   POL_HV1N5        2    132             
SEQADV 2LYA HIS A  133  UNP  P12497              EXPRESSION TAG                 
SEQADV 2LYA HIS A  134  UNP  P12497              EXPRESSION TAG                 
SEQADV 2LYA HIS A  135  UNP  P12497              EXPRESSION TAG                 
SEQADV 2LYA HIS A  136  UNP  P12497              EXPRESSION TAG                 
SEQADV 2LYA HIS A  137  UNP  P12497              EXPRESSION TAG                 
SEQADV 2LYA HIS A  138  UNP  P12497              EXPRESSION TAG                 
SEQRES   1 A  137  GLY ALA ARG ALA SER VAL LEU SER GLY GLY GLU LEU ASP          
SEQRES   2 A  137  LYS TRP GLU LYS ILE ARG LEU ARG PRO GLY GLY LYS LYS          
SEQRES   3 A  137  GLN TYR LYS LEU LYS HIS ILE VAL TRP ALA SER ARG GLU          
SEQRES   4 A  137  LEU GLU ARG PHE ALA VAL ASN PRO GLY LEU LEU GLU THR          
SEQRES   5 A  137  SER GLU GLY CYS ARG GLN ILE LEU GLY GLN LEU GLN PRO          
SEQRES   6 A  137  SER LEU GLN THR GLY SER GLU GLU LEU ARG SER LEU TYR          
SEQRES   7 A  137  ASN THR ILE ALA VAL LEU TYR CYS VAL HIS GLN ARG ILE          
SEQRES   8 A  137  ASP VAL LYS ASP THR LYS GLU ALA LEU ASP LYS ILE GLU          
SEQRES   9 A  137  GLU GLU GLN ASN LYS SER LYS LYS LYS ALA GLN GLN ALA          
SEQRES  10 A  137  ALA ALA ASP THR GLY ASN ASN SER GLN VAL SER GLN ASN          
SEQRES  11 A  137  TYR HIS HIS HIS HIS HIS HIS                                  
HET    PC8  A 300      82                                                       
HETNAM     PC8 1,2-DIOCTANOYL-SN-GLYCERO-3-PHOSPHOCHOLINE                       
FORMUL   2  PC8    C24 H49 N O8 P 1+                                            
HELIX    1   1 SER A    9  ILE A   19  1                                  11    
HELIX    2   2 LYS A   30  GLU A   42  1                                  13    
HELIX    3   3 ARG A   43  ALA A   45  5                                   3    
HELIX    4   4 ASN A   47  GLU A   52  5                                   6    
HELIX    5   5 THR A   53  GLN A   65  1                                  13    
HELIX    6   6 SER A   67  GLY A   71  5                                   5    
HELIX    7   7 SER A   72  GLN A   90  1                                  19    
HELIX    8   8 ASP A   96  ALA A  115  1                                  20    
SITE     1 AC1  3 LEU A  41  PHE A  44  LEU A  64                               
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1           1          
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      1.000000  0.000000  0.000000        0.00000                         
SCALE2      0.000000  1.000000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  1.000000        0.00000                         
MODEL        1                                                                  
(ATOM LINES ARE NOT SHOWN.)

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