HEADER    ANTIBIOTIC                              09-JUN-04   1TKQ              
TITLE     SOLUTION STRUCTURE OF A LINKED UNSYMMETRIC GRAMICIDIN IN A MEMBRANE-  
TITLE    2 ISOELECTRICAL SOLVENTS MIXTURE IN THE PRESENCE OF CSCL               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MINI-GRAMICIDIN A;                                         
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: GRAMICIDIN A;                                              
COMPND   7 CHAIN: B;                                                            
COMPND   8 SYNONYM: VALYL GRAMICIDIN;                                           
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 SYNTHETIC: YES;                                                      
SOURCE   3 ORGANISM_SCIENTIFIC: BREVIBACILLUS BREVIS;                           
SOURCE   4 ORGANISM_TAXID: 1393;                                                
SOURCE   5 MOL_ID: 2;                                                           
SOURCE   6 SYNTHETIC: YES;                                                      
SOURCE   7 ORGANISM_SCIENTIFIC: BREVIBACILLUS BREVIS;                           
SOURCE   8 ORGANISM_TAXID: 1393                                                 
KEYWDS    GRAMICIDIN, ANTIFUNGAL, ANTIBACTERIAL, ANTIBIOTIC, MEMBRANE ION       
KEYWDS   2 CHANNEL, LINEAR GRAMICIDIN                                           
EXPDTA    SOLUTION NMR                                                          
MDLTYP    MINIMIZED AVERAGE                                                     
AUTHOR    X.XIE,L.AL-MOMANI,D.BOCKELMANN,C.GRIESINGER,U.KOERT                   
REVDAT   6   25-SEP-19 1TKQ    1       REMARK LINK   ATOM                       
REVDAT   5   27-JUL-11 1TKQ    1       ATOM   HET    HETATM LINK                
REVDAT   5 2                   1       REMARK                                   
REVDAT   4   13-JUL-11 1TKQ    1       VERSN                                    
REVDAT   3   24-FEB-09 1TKQ    1       VERSN                                    
REVDAT   2   12-APR-05 1TKQ    1       JRNL                                     
REVDAT   1   13-JUL-04 1TKQ    0                                                
JRNL        AUTH   X.XIE,L.AL-MOMANI,P.REISS,C.GRIESINGER,U.KOERT               
JRNL        TITL   AN ASYMMETRIC ION CHANNEL DERIVED FROM GRAMICIDIN A.         
JRNL        TITL 2 SYNTHESIS, FUNCTION AND NMR STRUCTURE.                       
JRNL        REF    FEBS J.                       V. 272   975 2005              
JRNL        REFN                   ISSN 1742-464X                               
JRNL        PMID   15691331                                                     
JRNL        DOI    10.1111/J.1742-4658.2004.04531.X                             
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   R.R.KETCHEM,W.HU,T.A.CROSS                                   
REMARK   1  TITL   HIGH-RESOLUTION CONFORMATION OF GRAMICIDIN A IN A LIPID      
REMARK   1  TITL 2 BILAYER BY SOLID-STATE NMR                                   
REMARK   1  REF    SCIENCE                       V. 261  1457 1993              
REMARK   1  REFN                   ISSN 0036-8075                               
REMARK   1  PMID   7690158                                                      
REMARK   1  DOI    10.1126/SCIENCE.7690158                                      
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   Y.CHEN,A.TUCKER,B.A.WALLACE                                  
REMARK   1  TITL   SOLUTION STRUCTURE OF A PARALLEL LEFT-HANDED DOUBLE-HELICAL  
REMARK   1  TITL 2 GRAMICIDIN-A DETERMINED BY 2D 1H NMR                         
REMARK   1  REF    J.MOL.BIOL.                   V. 264   757 1996              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1  PMID   8980684                                                      
REMARK   1  DOI    10.1006/JMBI.1996.0675                                       
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   H.-D.ARNDT,D.BOCKELMANN,A.KNOLL,S.LAMBERTH,C.GRIESINGER,     
REMARK   1  AUTH 2 U.KOERT                                                      
REMARK   1  TITL   CATION CONTROL IN FUNCTIONAL HELICAL PROGRAMMING: STRUCTURES 
REMARK   1  TITL 2 OF A D,L-PEPTIDE ION CHANNEL                                 
REMARK   1  REF    ANGEW.CHEM.INT.ED.ENGL.       V.  41  4062 2002              
REMARK   1  REFN                   ISSN 1433-7851                               
REMARK   1  PMID   12412082                                                     
REMARK   1  DOI    10.1002/1521-3773(20021104)41:21<4062::AID-ANIE4062>3.0.CO;2 
REMARK   1  DOI  2 -U                                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION. NOT APPLICABLE.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : SYBYL/DYANA 6.8                                      
REMARK   3   AUTHORS     : GUENTERT                                             
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON 160 NOE-      
REMARK   3  DERIVED DISTANCE CONSTRAINTS, 39 DIHEDRAL ANGLE RESTRAINTS, AND     
REMARK   3  40 DISTANCE RESTRAINTS FROM HYDROGEN BONDS                          
REMARK   4                                                                      
REMARK   4 1TKQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-JUN-04.                  
REMARK 100 THE DEPOSITION ID IS D_1000022727.                                   
REMARK 210                                                                      
REMARK 210 EXPERIMENTAL DETAILS                                                 
REMARK 210  EXPERIMENT TYPE                : NMR                                
REMARK 210  TEMPERATURE           (KELVIN) : 293                                
REMARK 210  PH                             : NULL                               
REMARK 210  IONIC STRENGTH                 : NULL                               
REMARK 210  PRESSURE                       : NULL                               
REMARK 210  SAMPLE CONTENTS                : 3MM SATURATED WITH CSCL            
REMARK 210                                                                      
REMARK 210  NMR EXPERIMENTS CONDUCTED      : DQF-COSY; 2D NOESY                 
REMARK 210  SPECTROMETER FIELD STRENGTH    : 800 MHZ                            
REMARK 210  SPECTROMETER MODEL             : AVANCE                             
REMARK 210  SPECTROMETER MANUFACTURER      : BRUKER                             
REMARK 210                                                                      
REMARK 210  STRUCTURE DETERMINATION.                                            
REMARK 210   SOFTWARE USED                 : SYBYL/DYANA 6.8                    
REMARK 210   METHOD USED                   : SIMULATED ANNEALING                
REMARK 210                                                                      
REMARK 210 CONFORMERS, NUMBER CALCULATED   : 50                                 
REMARK 210 CONFORMERS, NUMBER SUBMITTED    : 1                                  
REMARK 210 CONFORMERS, SELECTION CRITERIA  : MINIMIZED AVERAGE STRUCTURE OF     
REMARK 210                                   11 STRUCTURES WITH THE LOWEST      
REMARK 210                                   TARGET FUNCTION                    
REMARK 210                                                                      
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1                   
REMARK 210                                                                      
REMARK 210 REMARK: VARIABLE TEMPERATURE EXPERIMENTS WERE PERFORMED TO HAVE      
REMARK 210  THE TEMPERATURE DEPENDENCE OF NH CHEMICAL SHIFTS, THEREFORE         
REMARK 210  PROVIDE EVIDENCE FOR HYDROGEN BONDING.                              
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 760 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 2810 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 6.0 KCAL/MOL                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 GRAMICIDIN IS A HETEROGENEOUS MIXTURE OF SEVERAL COMPOUNDS           
REMARK 400 INCLUDING GRAMICIDIN A, B AND C WHICH ARE OBTAINED FROM              
REMARK 400 BACILLUS BREVIS AND CALLED COLLECTIVELY GRAMICIDIN D                 
REMARK 400 HERE, MODIFIDED GRAMICIDIN A IS REPRESENTED BY TWO SEQUENCES (SEQRES 
REMARK 400 AND ONE HET (SIN)                                                    
REMARK 400                                                                      
REMARK 400 THE MINI-GRAMICIDIN A - GRAMICIDIN A DIMER IS POLYPEPTIDE, A MEMBER  
REMARK 400 OF ANTIBIOTIC CLASS.                                                 
REMARK 400                                                                      
REMARK 400  GROUP: 1                                                            
REMARK 400   NAME: MINI-GRAMICIDIN A - GRAMICIDIN A DIMER                       
REMARK 400   CHAIN: A, B                                                        
REMARK 400   COMPONENT_1: PEPTIDE LIKE POLYMER                                  
REMARK 400   COMPONENT_2: PEPTIDE LIKE POLYMER                                  
REMARK 400   COMPONENT_3: RESIDUE SIN                                           
REMARK 400   DESCRIPTION: THE N-TERMINI OF THE TWO PEPTIDES, EACH A TRUNCATED   
REMARK 400                GRAMICIDIN A, WERE LINKED BY A SUCCINIC ACID IN A     
REMARK 400                HEAD-TO-HEAD MANNER.                                  
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    TRP A  15   CE2 -  CD2 -  CG  ANGL. DEV. =  -4.9 DEGREES          
REMARK 500    TRP B   9   CE2 -  CD2 -  CG  ANGL. DEV. =  -4.9 DEGREES          
REMARK 500    TRP B  11   CE2 -  CD2 -  CG  ANGL. DEV. =  -4.9 DEGREES          
REMARK 500    TRP B  13   CE2 -  CD2 -  CG  ANGL. DEV. =  -4.9 DEGREES          
REMARK 500    TRP B  15   CE2 -  CD2 -  CG  ANGL. DEV. =  -4.9 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1TK2   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF GRAMICIDIN S COMPLEXED WITH ALKALINE            
REMARK 900 PROTEINASE SAVINASE                                                  
REMARK 900 RELATED ID: 2XDC   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF GRAMICIDIN A FROM CRYSTALS GROWN IN A LIPID     
REMARK 900 CUBIC PHASE.                                                         
REMARK 900 RELATED ID: 1AV2   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF GRAMICIDIN A COMPLEXED WITH CESIUM CHLORIDE     
REMARK 900 RELATED ID: 1BDW   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF GRAMICIDIN A FROM BACILLUS BREVIS               
REMARK 900 RELATED ID: 1C4D   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF GRAMICIDIN A COMPLEXED WITH CESIUM CHLORIDE     
REMARK 900 RELATED ID: 1GMK   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF GRAMICIDIN A COMPLRXED WITH POTASSIUM           
REMARK 900 THIOCYANATE                                                          
REMARK 900 RELATED ID: 1GRM   RELATED DB: PDB                                   
REMARK 900 SOLUTION STRUCTURE OF THE GRAMICIDIN A                               
REMARK 900 RELATED ID: 1JNO   RELATED DB: PDB                                   
REMARK 900 SOLUTION STRUCTURE OF GRAMICIDIN A IN SODIUM DODECYL SULFATE         
REMARK 900 MICELLES                                                             
REMARK 900 RELATED ID: 1KQE   RELATED DB: PDB                                   
REMARK 900 SOLUTION STRUCTURE OF A LINKED SHORTENED GRAMICIDIN A IN BENZENE/    
REMARK 900 ACETONE 10:1                                                         
REMARK 900 RELATED ID: 1MAG   RELATED DB: PDB                                   
REMARK 900 SOLID STATE NMR STRUCTURE OF GRAMICIDIN A IN HYDRATED DMPC BILAYERS, 
REMARK 900 RELATED ID: 1MIC   RELATED DB: PDB                                   
REMARK 900 SOLUTION STRUCTURE OF GRAMICIDIN A IN METHANOL IN THE PRESENCE OF    
REMARK 900 CACL                                                                 
REMARK 900 RELATED ID: 1NG8   RELATED DB: PDB                                   
REMARK 900 SOLUTION STRUCTURE OF GRAMICIDIN A (W15G) IN SODIUM DODECYL SULFATE  
REMARK 900 MICELLES                                                             
REMARK 900 RELATED ID: 1NRM   RELATED DB: PDB                                   
REMARK 900 SOLUTION STRUCTURE OF GRAMICIDIN A IN DODECYL PHOSPHOCHOLINE         
REMARK 900 MICELLES                                                             
REMARK 900 RELATED ID: 1NRU   RELATED DB: PDB                                   
REMARK 900 SOLUTION STRUCTURE OF GRAMICIDIN A IN DODECYL PHOSPHOCHOLINE         
REMARK 900 MICELLES IN THE PRESENCE OF EXCESS NA+                               
REMARK 900 RELATED ID: 1NT5   RELATED DB: PDB                                   
REMARK 900 SOLUTION STRUCTURE OF GRAMICIDIN A (V1F) IN SODIUM DODECYL SULFATE   
REMARK 900 MICELLES                                                             
REMARK 900 RELATED ID: 1JO3   RELATED DB: PDB                                   
REMARK 900 SOLUTION STRUCTURE OF GRAMICIDIN B IN SODIUM DODECYL SULFATE         
REMARK 900 MICELLES                                                             
REMARK 900 RELATED ID: 1JO4   RELATED DB: PDB                                   
REMARK 900 SOLUTION STRUCTURE OF GRAMICIDIN C IN SODIUM DODECYL SULFATE         
REMARK 900 MICELLES                                                             
REMARK 900 RELATED ID: 1NT6   RELATED DB: PDB                                   
REMARK 900 SOLUTION STRUCTURE OF F1-GRAMICIDIN C IN SODIUM DODECYL SULFATE      
REMARK 900 MICELLES                                                             
REMARK 900 RELATED ID: 1W5U   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF GRAMICIDIN D IN ETHANOL                         
REMARK 900 RELATED ID: 2IZQ   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF GRAMICIDIN D COMPLEX WITH KI IN METHANOL        
REMARK 900 RELATED ID: 3L8L   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF GRAMICIDIN D COMPLEX WITH NAI                   
REMARK 900 RELATED ID: 1AL4   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF GRAMICIDIN D IN N-PROPANOL                      
REMARK 900 RELATED ID: 1ALX   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF GRAMICIDIN D IN METHANOL                        
REMARK 900 RELATED ID: 1ALZ   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF GRAMICIDIN D IN ETHANOL                         
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 BOTH OF THE C-TERMINI HAVE ETHANOLAMINE ATTACHED WITH                
REMARK 999 THE CAPPING GROUP T-BUTYLDIPHENYLSILYL, WHICH WAS APPLIED            
REMARK 999 TO ENHANCE THE SOLUBILITY AND STABILITY OF THE STRUCTURE             
REMARK 999 IN ORGANIC SOLVENTS. OWING TO AMBIGUITY IN RESONANCE                 
REMARK 999 ASSIGNMENT OF THE TERMINI AND THEREFORE A LACK OF ENOUGH             
REMARK 999 NOE CONSTRAINTS, THE T-BUTYLDIPHENYLSILYL TERMINI WERE               
REMARK 999 OMITTED IN THE STRUCTURE CALCULATION.                                
DBREF  1TKQ A    5    15  NOR    NOR00243 NOR00243         5     15             
DBREF  1TKQ B    1    15  NOR    NOR00243 NOR00243         1     15             
SEQRES   1 A   11  ALA DVA VAL DVA TRP DLE TRP DLE TRP DLE TRP                  
SEQRES   1 B   15  VAL GLY ALA DLE ALA DVA VAL DVA TRP DLE TRP DLE TRP          
SEQRES   2 B   15  DLE TRP                                                      
HET    DVA  A   6      15                                                       
HET    DVA  A   8      15                                                       
HET    DLE  A  10      19                                                       
HET    DLE  A  12      19                                                       
HET    DLE  A  14      19                                                       
HET    DLE  B   4      19                                                       
HET    DVA  B   6      15                                                       
HET    DVA  B   8      15                                                       
HET    DLE  B  10      19                                                       
HET    DLE  B  12      19                                                       
HET    DLE  B  14      19                                                       
HET    SIN  B 101       8                                                       
HETNAM     DVA D-VALINE                                                         
HETNAM     DLE D-LEUCINE                                                        
HETNAM     SIN SUCCINIC ACID                                                    
FORMUL   1  DVA    4(C5 H11 N O2)                                               
FORMUL   1  DLE    7(C6 H13 N O2)                                               
FORMUL   3  SIN    C4 H6 O4                                                     
SHEET    1  AA 3 DLE A  12  TRP A  15  0                                        
SHEET    2  AA 3 DVA A   6  TRP A   9  1  O  DVA A   6   N  TRP A  13           
SHEET    3  AA 3 GLY B   2  TRP B  15 -1  O  ALA B   3   N  VAL A   7           
LINK         C   ALA A   5                 N   DVA A   6     1555   1555  1.36  
LINK         C   DVA A   6                 N   VAL A   7     1555   1555  1.35  
LINK         C   VAL A   7                 N   DVA A   8     1555   1555  1.36  
LINK         C   DVA A   8                 N   TRP A   9     1555   1555  1.36  
LINK         C   TRP A   9                 N   DLE A  10     1555   1555  1.36  
LINK         C   DLE A  10                 N   TRP A  11     1555   1555  1.36  
LINK         C   TRP A  11                 N   DLE A  12     1555   1555  1.36  
LINK         C   DLE A  12                 N   TRP A  13     1555   1555  1.36  
LINK         C   TRP A  13                 N   DLE A  14     1555   1555  1.36  
LINK         C   DLE A  14                 N   TRP A  15     1555   1555  1.35  
LINK         C   ALA B   3                 N   DLE B   4     1555   1555  1.35  
LINK         C   DLE B   4                 N   ALA B   5     1555   1555  1.35  
LINK         C   ALA B   5                 N   DVA B   6     1555   1555  1.36  
LINK         C   DVA B   6                 N   VAL B   7     1555   1555  1.35  
LINK         C   VAL B   7                 N   DVA B   8     1555   1555  1.35  
LINK         C   DVA B   8                 N   TRP B   9     1555   1555  1.36  
LINK         C   TRP B   9                 N   DLE B  10     1555   1555  1.35  
LINK         C   DLE B  10                 N   TRP B  11     1555   1555  1.36  
LINK         C   TRP B  11                 N   DLE B  12     1555   1555  1.35  
LINK         C   DLE B  12                 N   TRP B  13     1555   1555  1.35  
LINK         C   TRP B  13                 N   DLE B  14     1555   1555  1.35  
LINK         C   DLE B  14                 N   TRP B  15     1555   1555  1.35  
LINK         C4  SIN B 101                 N   VAL B   1     1555   1555  1.35  
LINK         C1  SIN B 101                 N   ALA A   5     1555   1555  1.35  
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                         
ATOM      1  N   ALA A   5       2.073  -3.071   1.467  1.00  0.00           N  
ATOM      2  CA  ALA A   5       1.754  -4.469   1.197  1.00  0.00           C  
ATOM      3  C   ALA A   5       0.696  -4.500   0.116  1.00  0.00           C  
ATOM      4  O   ALA A   5      -0.474  -4.371   0.444  1.00  0.00           O  
ATOM      5  CB  ALA A   5       1.250  -5.099   2.518  1.00  0.00           C  
ATOM      6  H1  ALA A   5       1.312  -2.415   1.463  1.00  0.00           H  
ATOM      7  HA  ALA A   5       2.630  -5.046   0.856  1.00  0.00           H  
ATOM      8  HB1 ALA A   5       0.396  -4.528   2.909  1.00  0.00           H  
ATOM      9  HB2 ALA A   5       0.935  -6.141   2.349  1.00  0.00           H  
ATOM     10  HB3 ALA A   5       2.053  -5.085   3.271  1.00  0.00           H  
HETATM   11  N   DVA A   6       1.082  -4.659  -1.173  1.00  0.00           N  
HETATM   12  CA  DVA A   6       0.085  -4.752  -2.243  1.00  0.00           C  
HETATM   13  CB  DVA A   6      -0.258  -6.249  -2.506  1.00  0.00           C  
HETATM   14  CG1 DVA A   6      -1.455  -6.375  -3.489  1.00  0.00           C  
HETATM   15  CG2 DVA A   6      -0.503  -7.052  -1.198  1.00  0.00           C  
HETATM   16  C   DVA A   6       0.645  -4.064  -3.477  1.00  0.00           C  
HETATM   17  O   DVA A   6       1.303  -4.715  -4.275  1.00  0.00           O  
HETATM   18  HA  DVA A   6      -0.848  -4.244  -1.958  1.00  0.00           H  
HETATM   19  HB  DVA A   6       0.610  -6.731  -2.967  1.00  0.00           H  
HETATM   20 HG11 DVA A   6      -1.224  -5.873  -4.441  1.00  0.00           H  
HETATM   21 HG12 DVA A   6      -1.668  -7.434  -3.704  1.00  0.00           H  
HETATM   22 HG13 DVA A   6      -2.360  -5.916  -3.065  1.00  0.00           H  
HETATM   23 HG21 DVA A   6      -1.279  -6.578  -0.586  1.00  0.00           H  
HETATM   24 HG22 DVA A   6      -0.820  -8.081  -1.429  1.00  0.00           H  
HETATM   25 HG23 DVA A   6       0.419  -7.112  -0.599  1.00  0.00           H  
ATOM     26  N   VAL A   7       0.428  -2.741  -3.668  1.00  0.00           N  
ATOM     27  CA  VAL A   7       1.070  -2.043  -4.789  1.00  0.00           C  
ATOM     28  C   VAL A   7       1.619  -0.721  -4.290  1.00  0.00           C  
ATOM     29  O   VAL A   7       0.831   0.024  -3.731  1.00  0.00           O  
ATOM     30  CB  VAL A   7       0.098  -1.833  -5.986  1.00  0.00           C  
ATOM     31  CG1 VAL A   7       0.884  -1.530  -7.294  1.00  0.00           C  
ATOM     32  CG2 VAL A   7      -0.812  -3.075  -6.199  1.00  0.00           C  
ATOM     33  H   VAL A   7      -0.173  -2.212  -3.058  1.00  0.00           H  
ATOM     34  HA  VAL A   7       1.912  -2.631  -5.166  1.00  0.00           H  
ATOM     35  HB  VAL A   7      -0.553  -0.974  -5.759  1.00  0.00           H  
ATOM     36 HG11 VAL A   7       1.583  -0.695  -7.151  1.00  0.00           H  
ATOM     37 HG12 VAL A   7       1.465  -2.409  -7.611  1.00  0.00           H  
ATOM     38 HG13 VAL A   7       0.188  -1.266  -8.107  1.00  0.00           H  
ATOM     39 HG21 VAL A   7      -1.445  -3.251  -5.316  1.00  0.00           H  
ATOM     40 HG22 VAL A   7      -1.474  -2.921  -7.065  1.00  0.00           H  
ATOM     41 HG23 VAL A   7      -0.201  -3.972  -6.382  1.00  0.00           H  
HETATM   42  N   DVA A   8       2.924  -0.387  -4.438  1.00  0.00           N  
HETATM   43  CA  DVA A   8       3.437   0.868  -3.870  1.00  0.00           C  
HETATM   44  CB  DVA A   8       3.358   2.075  -4.853  1.00  0.00           C  
HETATM   45  CG1 DVA A   8       3.807   3.394  -4.158  1.00  0.00           C  
HETATM   46  CG2 DVA A   8       1.925   2.276  -5.418  1.00  0.00           C  
HETATM   47  C   DVA A   8       4.872   0.665  -3.426  1.00  0.00           C  
HETATM   48  O   DVA A   8       5.620   0.087  -4.200  1.00  0.00           O  
HETATM   49  HA  DVA A   8       2.857   1.126  -2.976  1.00  0.00           H  
HETATM   50  HB  DVA A   8       4.035   1.865  -5.700  1.00  0.00           H  
HETATM   51 HG11 DVA A   8       4.828   3.318  -3.763  1.00  0.00           H  
HETATM   52 HG12 DVA A   8       3.785   4.230  -4.874  1.00  0.00           H  
HETATM   53 HG13 DVA A   8       3.134   3.636  -3.321  1.00  0.00           H  
HETATM   54 HG21 DVA A   8       1.211   2.472  -4.604  1.00  0.00           H  
HETATM   55 HG22 DVA A   8       1.902   3.131  -6.112  1.00  0.00           H  
HETATM   56 HG23 DVA A   8       1.591   1.390  -5.972  1.00  0.00           H  
ATOM     57  N   TRP A   9       5.299   1.108  -2.217  1.00  0.00           N  
ATOM     58  CA  TRP A   9       6.652   0.790  -1.746  1.00  0.00           C  
ATOM     59  C   TRP A   9       6.552  -0.221  -0.625  1.00  0.00           C  
ATOM     60  O   TRP A   9       5.591  -0.142   0.120  1.00  0.00           O  
ATOM     61  CB  TRP A   9       7.427   2.038  -1.251  1.00  0.00           C  
ATOM     62  CG  TRP A   9       7.901   2.964  -2.343  1.00  0.00           C  
ATOM     63  CD1 TRP A   9       7.628   2.958  -3.660  1.00  0.00           C  
ATOM     64  CD2 TRP A   9       8.839   4.120  -2.104  1.00  0.00           C  
ATOM     65  NE1 TRP A   9       8.267   3.939  -4.246  1.00  0.00           N  
ATOM     66  CE2 TRP A   9       9.000   4.651  -3.368  1.00  0.00           C  
ATOM     67  CE3 TRP A   9       9.478   4.653  -0.986  1.00  0.00           C  
ATOM     68  CZ2 TRP A   9       9.820   5.755  -3.600  1.00  0.00           C  
ATOM     69  CZ3 TRP A   9      10.308   5.760  -1.204  1.00  0.00           C  
ATOM     70  CH2 TRP A   9      10.477   6.301  -2.489  1.00  0.00           C  
ATOM     71  H   TRP A   9       4.685   1.585  -1.575  1.00  0.00           H  
ATOM     72  HA  TRP A   9       7.261   0.331  -2.535  1.00  0.00           H  
ATOM     73  HB2 TRP A   9       6.807   2.604  -0.541  1.00  0.00           H  
ATOM     74  HB3 TRP A   9       8.333   1.701  -0.722  1.00  0.00           H  
ATOM     75  HD1 TRP A   9       6.986   2.254  -4.186  1.00  0.00           H  
ATOM     76  HE1 TRP A   9       8.222   4.141  -5.256  1.00  0.00           H  
ATOM     77  HE3 TRP A   9       9.336   4.227   0.001  1.00  0.00           H  
ATOM     78  HZ2 TRP A   9       9.942   6.167  -4.595  1.00  0.00           H  
ATOM     79  HZ3 TRP A   9      10.830   6.207  -0.363  1.00  0.00           H  
ATOM     80  HH2 TRP A   9      11.129   7.159  -2.626  1.00  0.00           H  
HETATM   81  N   DLE A  10       7.511  -1.167  -0.482  1.00  0.00           N  
HETATM   82  CA  DLE A  10       7.391  -2.251   0.497  1.00  0.00           C  
HETATM   83  CB  DLE A  10       8.657  -2.274   1.400  1.00  0.00           C  
HETATM   84  CG  DLE A  10       8.778  -3.532   2.317  1.00  0.00           C  
HETATM   85  CD1 DLE A  10      10.067  -3.427   3.180  1.00  0.00           C  
HETATM   86  CD2 DLE A  10       7.541  -3.720   3.238  1.00  0.00           C  
HETATM   87  C   DLE A  10       7.263  -3.553  -0.262  1.00  0.00           C  
HETATM   88  O   DLE A  10       8.261  -3.976  -0.823  1.00  0.00           O  
HETATM   89  H   DLE A  10       8.315  -1.192  -1.083  1.00  0.00           H  
HETATM   90  HA  DLE A  10       6.517  -2.124   1.146  1.00  0.00           H  
HETATM   91  HB2 DLE A  10       9.548  -2.240   0.753  1.00  0.00           H  
HETATM   92  HB3 DLE A  10       8.656  -1.360   2.015  1.00  0.00           H  
HETATM   93  HG  DLE A  10       8.876  -4.437   1.691  1.00  0.00           H  
HETATM   94 HD11 DLE A  10      10.011  -2.556   3.851  1.00  0.00           H  
HETATM   95 HD12 DLE A  10      10.198  -4.333   3.794  1.00  0.00           H  
HETATM   96 HD13 DLE A  10      10.955  -3.320   2.538  1.00  0.00           H  
HETATM   97 HD21 DLE A  10       7.342  -2.801   3.810  1.00  0.00           H  
HETATM   98 HD22 DLE A  10       6.648  -3.976   2.650  1.00  0.00           H  
HETATM   99 HD23 DLE A  10       7.712  -4.545   3.947  1.00  0.00           H  
ATOM    100  N   TRP A  11       6.085  -4.223  -0.313  1.00  0.00           N  
ATOM    101  CA  TRP A  11       6.024  -5.522  -0.987  1.00  0.00           C  
ATOM    102  C   TRP A  11       4.757  -5.745  -1.788  1.00  0.00           C  
ATOM    103  O   TRP A  11       3.777  -5.038  -1.608  1.00  0.00           O  
ATOM    104  CB  TRP A  11       6.237  -6.670   0.044  1.00  0.00           C  
ATOM    105  CG  TRP A  11       7.583  -7.355   0.006  1.00  0.00           C  
ATOM    106  CD1 TRP A  11       8.366  -7.634  -1.053  1.00  0.00           C  
ATOM    107  CD2 TRP A  11       8.296  -7.896   1.221  1.00  0.00           C  
ATOM    108  NE1 TRP A  11       9.441  -8.262  -0.652  1.00  0.00           N  
ATOM    109  CE2 TRP A  11       9.442  -8.448   0.681  1.00  0.00           C  
ATOM    110  CE3 TRP A  11       8.033  -7.932   2.590  1.00  0.00           C  
ATOM    111  CZ2 TRP A  11      10.394  -9.088   1.474  1.00  0.00           C  
ATOM    112  CZ3 TRP A  11       8.981  -8.573   3.399  1.00  0.00           C  
ATOM    113  CH2 TRP A  11      10.140  -9.145   2.850  1.00  0.00           C  
ATOM    114  H   TRP A  11       5.254  -3.893   0.148  1.00  0.00           H  
ATOM    115  HA  TRP A  11       6.794  -5.545  -1.771  1.00  0.00           H  
ATOM    116  HB2 TRP A  11       6.090  -6.248   1.050  1.00  0.00           H  
ATOM    117  HB3 TRP A  11       5.487  -7.465  -0.083  1.00  0.00           H  
ATOM    118  HD1 TRP A  11       8.165  -7.398  -2.098  1.00  0.00           H  
ATOM    119  HE1 TRP A  11      10.194  -8.584  -1.279  1.00  0.00           H  
ATOM    120  HE3 TRP A  11       7.137  -7.486   3.007  1.00  0.00           H  
ATOM    121  HZ2 TRP A  11      11.289  -9.521   1.039  1.00  0.00           H  
ATOM    122  HZ3 TRP A  11       8.814  -8.630   4.470  1.00  0.00           H  
ATOM    123  HH2 TRP A  11      10.853  -9.641   3.502  1.00  0.00           H  
HETATM  124  N   DLE A  12       4.793  -6.748  -2.700  1.00  0.00           N  
HETATM  125  CA  DLE A  12       3.739  -6.913  -3.698  1.00  0.00           C  
HETATM  126  CB  DLE A  12       3.365  -8.419  -3.824  1.00  0.00           C  
HETATM  127  CG  DLE A  12       2.223  -8.762  -4.834  1.00  0.00           C  
HETATM  128  CD1 DLE A  12       2.649  -8.593  -6.320  1.00  0.00           C  
HETATM  129  CD2 DLE A  12       1.737 -10.220  -4.595  1.00  0.00           C  
HETATM  130  C   DLE A  12       4.320  -6.336  -4.968  1.00  0.00           C  
HETATM  131  O   DLE A  12       5.296  -6.900  -5.436  1.00  0.00           O  
HETATM  132  H   DLE A  12       5.597  -7.337  -2.803  1.00  0.00           H  
HETATM  133  HA  DLE A  12       2.839  -6.367  -3.402  1.00  0.00           H  
HETATM  134  HB2 DLE A  12       4.261  -9.003  -4.088  1.00  0.00           H  
HETATM  135  HB3 DLE A  12       3.052  -8.732  -2.814  1.00  0.00           H  
HETATM  136  HG  DLE A  12       1.359  -8.102  -4.667  1.00  0.00           H  
HETATM  137 HD11 DLE A  12       3.590  -9.127  -6.518  1.00  0.00           H  
HETATM  138 HD12 DLE A  12       1.876  -8.994  -6.995  1.00  0.00           H  
HETATM  139 HD13 DLE A  12       2.774  -7.533  -6.575  1.00  0.00           H  
HETATM  140 HD21 DLE A  12       1.367 -10.343  -3.565  1.00  0.00           H  
HETATM  141 HD22 DLE A  12       0.914 -10.476  -5.280  1.00  0.00           H  
HETATM  142 HD23 DLE A  12       2.563 -10.929  -4.759  1.00  0.00           H  
ATOM    143  N   TRP A  13       3.776  -5.233  -5.536  1.00  0.00           N  
ATOM    144  CA  TRP A  13       4.360  -4.641  -6.746  1.00  0.00           C  
ATOM    145  C   TRP A  13       4.729  -3.182  -6.548  1.00  0.00           C  
ATOM    146  O   TRP A  13       4.280  -2.549  -5.606  1.00  0.00           O  
ATOM    147  CB  TRP A  13       3.399  -4.796  -7.961  1.00  0.00           C  
ATOM    148  CG  TRP A  13       3.658  -5.958  -8.891  1.00  0.00           C  
ATOM    149  CD1 TRP A  13       4.450  -7.036  -8.745  1.00  0.00           C  
ATOM    150  CD2 TRP A  13       3.014  -6.080 -10.249  1.00  0.00           C  
ATOM    151  NE1 TRP A  13       4.380  -7.782  -9.819  1.00  0.00           N  
ATOM    152  CE2 TRP A  13       3.550  -7.254 -10.740  1.00  0.00           C  
ATOM    153  CE3 TRP A  13       2.107  -5.316 -10.980  1.00  0.00           C  
ATOM    154  CZ2 TRP A  13       3.226  -7.735 -12.008  1.00  0.00           C  
ATOM    155  CZ3 TRP A  13       1.773  -5.784 -12.258  1.00  0.00           C  
ATOM    156  CH2 TRP A  13       2.325  -6.972 -12.764  1.00  0.00           C  
ATOM    157  H   TRP A  13       2.967  -4.793  -5.135  1.00  0.00           H  
ATOM    158  HA  TRP A  13       5.329  -5.102  -6.987  1.00  0.00           H  
ATOM    159  HB2 TRP A  13       2.358  -4.854  -7.609  1.00  0.00           H  
ATOM    160  HB3 TRP A  13       3.480  -3.908  -8.607  1.00  0.00           H  
ATOM    161  HD1 TRP A  13       5.069  -7.284  -7.884  1.00  0.00           H  
ATOM    162  HE1 TRP A  13       4.898  -8.664  -9.948  1.00  0.00           H  
ATOM    163  HE3 TRP A  13       1.684  -4.402 -10.576  1.00  0.00           H  
ATOM    164  HZ2 TRP A  13       3.654  -8.656 -12.387  1.00  0.00           H  
ATOM    165  HZ3 TRP A  13       1.074  -5.218 -12.866  1.00  0.00           H  
ATOM    166  HH2 TRP A  13       2.050  -7.307 -13.759  1.00  0.00           H  
HETATM  167  N   DLE A  14       5.572  -2.625  -7.452  1.00  0.00           N  
HETATM  168  CA  DLE A  14       6.111  -1.280  -7.254  1.00  0.00           C  
HETATM  169  CB  DLE A  14       6.179  -0.531  -8.618  1.00  0.00           C  
HETATM  170  CG  DLE A  14       6.767   0.914  -8.536  1.00  0.00           C  
HETATM  171  CD1 DLE A  14       8.322   0.931  -8.608  1.00  0.00           C  
HETATM  172  CD2 DLE A  14       6.212   1.785  -9.700  1.00  0.00           C  
HETATM  173  C   DLE A  14       7.479  -1.471  -6.640  1.00  0.00           C  
HETATM  174  O   DLE A  14       8.281  -2.144  -7.266  1.00  0.00           O  
HETATM  175  H   DLE A  14       5.940  -3.152  -8.221  1.00  0.00           H  
HETATM  176  HA  DLE A  14       5.463  -0.682  -6.597  1.00  0.00           H  
HETATM  177  HB2 DLE A  14       6.758  -1.116  -9.349  1.00  0.00           H  
HETATM  178  HB3 DLE A  14       5.139  -0.490  -8.982  1.00  0.00           H  
HETATM  179  HG  DLE A  14       6.449   1.381  -7.588  1.00  0.00           H  
HETATM  180 HD11 DLE A  14       8.668   0.503  -9.562  1.00  0.00           H  
HETATM  181 HD12 DLE A  14       8.699   1.963  -8.538  1.00  0.00           H  
HETATM  182 HD13 DLE A  14       8.782   0.359  -7.795  1.00  0.00           H  
HETATM  183 HD21 DLE A  14       5.116   1.867  -9.637  1.00  0.00           H  
HETATM  184 HD22 DLE A  14       6.630   2.803  -9.659  1.00  0.00           H  
HETATM  185 HD23 DLE A  14       6.476   1.337 -10.670  1.00  0.00           H  
ATOM    186  N   TRP A  15       7.783  -0.913  -5.445  1.00  0.00           N  
ATOM    187  CA  TRP A  15       9.114  -1.078  -4.856  1.00  0.00           C  
ATOM    188  C   TRP A  15       8.972  -1.809  -3.544  1.00  0.00           C  
ATOM    189  O   TRP A  15       9.277  -1.276  -2.487  1.00  0.00           O  
ATOM    190  CB  TRP A  15       9.778   0.313  -4.673  1.00  0.00           C  
ATOM    191  CG  TRP A  15      11.230   0.166  -4.308  1.00  0.00           C  
ATOM    192  CD1 TRP A  15      11.806   0.378  -3.113  1.00  0.00           C  
ATOM    193  CD2 TRP A  15      12.320  -0.259  -5.258  1.00  0.00           C  
ATOM    194  NE1 TRP A  15      13.090   0.141  -3.206  1.00  0.00           N  
ATOM    195  CE2 TRP A  15      13.441  -0.239  -4.451  1.00  0.00           C  
ATOM    196  CE3 TRP A  15      12.376  -0.612  -6.605  1.00  0.00           C  
ATOM    197  CZ2 TRP A  15      14.701  -0.576  -4.944  1.00  0.00           C  
ATOM    198  CZ3 TRP A  15      13.636  -0.954  -7.113  1.00  0.00           C  
ATOM    199  CH2 TRP A  15      14.779  -0.937  -6.297  1.00  0.00           C  
ATOM    200  H   TRP A  15       7.097  -0.389  -4.932  1.00  0.00           H  
ATOM    201  HA  TRP A  15       9.780  -1.688  -5.488  1.00  0.00           H  
ATOM    202  HB2 TRP A  15       9.721   0.891  -5.606  1.00  0.00           H  
ATOM    203  HB3 TRP A  15       9.258   0.881  -3.892  1.00  0.00           H  
ATOM    204  HD1 TRP A  15      11.274   0.696  -2.215  1.00  0.00           H  
ATOM    205  HE1 TRP A  15      13.754   0.231  -2.422  1.00  0.00           H  
ATOM    206  HE3 TRP A  15      11.486  -0.618  -7.226  1.00  0.00           H  
ATOM    207  HZ2 TRP A  15      15.578  -0.559  -4.307  1.00  0.00           H  
ATOM    208  HZ3 TRP A  15      13.729  -1.238  -8.157  1.00  0.00           H  
ATOM    209  HH2 TRP A  15      15.741  -1.207  -6.720  1.00  0.00           H  
TER     210      TRP A  15                                                      
ATOM    211  N   VAL B   1       3.353   1.645   2.264  1.00  0.00           N  
ATOM    212  CA  VAL B   1       2.896   2.895   1.659  1.00  0.00           C  
ATOM    213  C   VAL B   1       2.386   2.503   0.287  1.00  0.00           C  
ATOM    214  O   VAL B   1       3.187   2.355  -0.626  1.00  0.00           O  
ATOM    215  CB  VAL B   1       4.018   3.972   1.585  1.00  0.00           C  
ATOM    216  CG1 VAL B   1       3.488   5.266   0.903  1.00  0.00           C  
ATOM    217  CG2 VAL B   1       4.545   4.302   3.009  1.00  0.00           C  
ATOM    218  H1  VAL B   1       4.305   1.374   2.118  1.00  0.00           H  
ATOM    219  HA  VAL B   1       2.086   3.339   2.251  1.00  0.00           H  
ATOM    220  HB  VAL B   1       4.855   3.574   0.985  1.00  0.00           H  
ATOM    221 HG11 VAL B   1       2.645   5.689   1.471  1.00  0.00           H  
ATOM    222 HG12 VAL B   1       4.286   6.022   0.849  1.00  0.00           H  
ATOM    223 HG13 VAL B   1       3.147   5.057  -0.123  1.00  0.00           H  
ATOM    224 HG21 VAL B   1       4.946   3.401   3.498  1.00  0.00           H  
ATOM    225 HG22 VAL B   1       5.352   5.049   2.954  1.00  0.00           H  
ATOM    226 HG23 VAL B   1       3.738   4.708   3.638  1.00  0.00           H  
ATOM    227  N   GLY B   2       1.062   2.296   0.102  1.00  0.00           N  
ATOM    228  CA  GLY B   2       0.608   1.794  -1.190  1.00  0.00           C  
ATOM    229  C   GLY B   2      -0.871   1.507  -1.291  1.00  0.00           C  
ATOM    230  O   GLY B   2      -1.645   1.982  -0.475  1.00  0.00           O  
ATOM    231  H   GLY B   2       0.381   2.433   0.833  1.00  0.00           H  
ATOM    232  HA2 GLY B   2       0.875   2.502  -1.988  1.00  0.00           H  
ATOM    233  HA3 GLY B   2       1.125   0.837  -1.358  1.00  0.00           H  
ATOM    234  N   ALA B   3      -1.276   0.715  -2.311  1.00  0.00           N  
ATOM    235  CA  ALA B   3      -2.653   0.240  -2.391  1.00  0.00           C  
ATOM    236  C   ALA B   3      -2.701  -1.169  -1.838  1.00  0.00           C  
ATOM    237  O   ALA B   3      -2.004  -2.018  -2.372  1.00  0.00           O  
ATOM    238  CB  ALA B   3      -3.167   0.246  -3.853  1.00  0.00           C  
ATOM    239  H   ALA B   3      -0.623   0.364  -2.988  1.00  0.00           H  
ATOM    240  HA  ALA B   3      -3.317   0.900  -1.820  1.00  0.00           H  
ATOM    241  HB1 ALA B   3      -2.570  -0.437  -4.473  1.00  0.00           H  
ATOM    242  HB2 ALA B   3      -4.218  -0.080  -3.891  1.00  0.00           H  
ATOM    243  HB3 ALA B   3      -3.093   1.261  -4.271  1.00  0.00           H  
HETATM  244  N   DLE B   4      -3.501  -1.441  -0.781  1.00  0.00           N  
HETATM  245  CA  DLE B   4      -3.591  -2.794  -0.230  1.00  0.00           C  
HETATM  246  CB  DLE B   4      -4.778  -3.542  -0.901  1.00  0.00           C  
HETATM  247  CG  DLE B   4      -5.208  -4.865  -0.191  1.00  0.00           C  
HETATM  248  CD1 DLE B   4      -6.266  -5.615  -1.050  1.00  0.00           C  
HETATM  249  CD2 DLE B   4      -4.015  -5.820   0.073  1.00  0.00           C  
HETATM  250  C   DLE B   4      -3.756  -2.667   1.269  1.00  0.00           C  
HETATM  251  O   DLE B   4      -4.867  -2.417   1.714  1.00  0.00           O  
HETATM  252  H   DLE B   4      -4.064  -0.726  -0.347  1.00  0.00           H  
HETATM  253  HA  DLE B   4      -2.670  -3.360  -0.436  1.00  0.00           H  
HETATM  254  HB2 DLE B   4      -5.646  -2.866  -0.919  1.00  0.00           H  
HETATM  255  HB3 DLE B   4      -4.496  -3.752  -1.946  1.00  0.00           H  
HETATM  256  HG  DLE B   4      -5.669  -4.625   0.782  1.00  0.00           H  
HETATM  257 HD11 DLE B   4      -7.124  -4.969  -1.277  1.00  0.00           H  
HETATM  258 HD12 DLE B   4      -5.825  -5.944  -2.004  1.00  0.00           H  
HETATM  259 HD13 DLE B   4      -6.639  -6.503  -0.515  1.00  0.00           H  
HETATM  260 HD21 DLE B   4      -3.269  -5.373   0.747  1.00  0.00           H  
HETATM  261 HD22 DLE B   4      -4.363  -6.756   0.537  1.00  0.00           H  
HETATM  262 HD23 DLE B   4      -3.542  -6.062  -0.887  1.00  0.00           H  
ATOM    263  N   ALA B   5      -2.673  -2.818   2.068  1.00  0.00           N  
ATOM    264  CA  ALA B   5      -2.804  -2.697   3.518  1.00  0.00           C  
ATOM    265  C   ALA B   5      -1.675  -1.867   4.097  1.00  0.00           C  
ATOM    266  O   ALA B   5      -0.529  -2.243   3.906  1.00  0.00           O  
ATOM    267  CB  ALA B   5      -2.820  -4.118   4.134  1.00  0.00           C  
ATOM    268  H   ALA B   5      -1.762  -3.036   1.703  1.00  0.00           H  
ATOM    269  HA  ALA B   5      -3.760  -2.233   3.794  1.00  0.00           H  
ATOM    270  HB1 ALA B   5      -1.879  -4.641   3.913  1.00  0.00           H  
ATOM    271  HB2 ALA B   5      -2.949  -4.064   5.226  1.00  0.00           H  
ATOM    272  HB3 ALA B   5      -3.652  -4.700   3.707  1.00  0.00           H  
HETATM  273  N   DVA B   6      -1.955  -0.751   4.813  1.00  0.00           N  
HETATM  274  CA  DVA B   6      -0.892   0.004   5.481  1.00  0.00           C  
HETATM  275  CB  DVA B   6      -0.783  -0.480   6.959  1.00  0.00           C  
HETATM  276  CG1 DVA B   6       0.255   0.357   7.760  1.00  0.00           C  
HETATM  277  CG2 DVA B   6      -0.412  -1.987   7.042  1.00  0.00           C  
HETATM  278  C   DVA B   6      -1.222   1.484   5.393  1.00  0.00           C  
HETATM  279  O   DVA B   6      -1.968   1.975   6.227  1.00  0.00           O  
HETATM  280  HA  DVA B   6       0.087  -0.158   5.005  1.00  0.00           H  
HETATM  281  HB  DVA B   6      -1.770  -0.362   7.431  1.00  0.00           H  
HETATM  282 HG11 DVA B   6      -0.040   1.415   7.816  1.00  0.00           H  
HETATM  283 HG12 DVA B   6       0.335  -0.016   8.793  1.00  0.00           H  
HETATM  284 HG13 DVA B   6       1.247   0.293   7.287  1.00  0.00           H  
HETATM  285 HG21 DVA B   6       0.540  -2.178   6.523  1.00  0.00           H  
HETATM  286 HG22 DVA B   6      -0.307  -2.300   8.092  1.00  0.00           H  
HETATM  287 HG23 DVA B   6      -1.195  -2.611   6.588  1.00  0.00           H  
ATOM    288  N   VAL B   7      -0.688   2.222   4.392  1.00  0.00           N  
ATOM    289  CA  VAL B   7      -0.964   3.654   4.273  1.00  0.00           C  
ATOM    290  C   VAL B   7      -1.156   3.957   2.800  1.00  0.00           C  
ATOM    291  O   VAL B   7      -0.383   3.436   2.012  1.00  0.00           O  
ATOM    292  CB  VAL B   7       0.216   4.500   4.838  1.00  0.00           C  
ATOM    293  CG1 VAL B   7      -0.178   5.993   5.014  1.00  0.00           C  
ATOM    294  CG2 VAL B   7       0.733   3.929   6.186  1.00  0.00           C  
ATOM    295  H   VAL B   7      -0.073   1.820   3.705  1.00  0.00           H  
ATOM    296  HA  VAL B   7      -1.884   3.914   4.818  1.00  0.00           H  
ATOM    297  HB  VAL B   7       1.053   4.449   4.123  1.00  0.00           H  
ATOM    298 HG11 VAL B   7      -0.613   6.403   4.093  1.00  0.00           H  
ATOM    299 HG12 VAL B   7      -0.918   6.100   5.817  1.00  0.00           H  
ATOM    300 HG13 VAL B   7       0.705   6.595   5.278  1.00  0.00           H  
ATOM    301 HG21 VAL B   7       1.142   2.916   6.047  1.00  0.00           H  
ATOM    302 HG22 VAL B   7       1.537   4.564   6.591  1.00  0.00           H  
ATOM    303 HG23 VAL B   7      -0.083   3.886   6.922  1.00  0.00           H  
HETATM  304  N   DVA B   8      -2.151   4.769   2.382  1.00  0.00           N  
HETATM  305  CA  DVA B   8      -2.376   5.007   0.953  1.00  0.00           C  
HETATM  306  CB  DVA B   8      -2.074   6.499   0.621  1.00  0.00           C  
HETATM  307  CG1 DVA B   8      -2.538   6.883  -0.813  1.00  0.00           C  
HETATM  308  CG2 DVA B   8      -0.550   6.779   0.756  1.00  0.00           C  
HETATM  309  C   DVA B   8      -3.787   4.574   0.602  1.00  0.00           C  
HETATM  310  O   DVA B   8      -4.711   5.357   0.770  1.00  0.00           O  
HETATM  311  HA  DVA B   8      -1.699   4.422   0.311  1.00  0.00           H  
HETATM  312  HB  DVA B   8      -2.613   7.134   1.344  1.00  0.00           H  
HETATM  313 HG11 DVA B   8      -2.082   6.212  -1.557  1.00  0.00           H  
HETATM  314 HG12 DVA B   8      -3.631   6.826  -0.913  1.00  0.00           H  
HETATM  315 HG13 DVA B   8      -2.239   7.917  -1.046  1.00  0.00           H  
HETATM  316 HG21 DVA B   8      -0.179   6.481   1.746  1.00  0.00           H  
HETATM  317 HG22 DVA B   8       0.017   6.217  -0.003  1.00  0.00           H  
HETATM  318 HG23 DVA B   8      -0.342   7.852   0.621  1.00  0.00           H  
ATOM    319  N   TRP B   9      -3.982   3.328   0.102  1.00  0.00           N  
ATOM    320  CA  TRP B   9      -5.283   2.937  -0.451  1.00  0.00           C  
ATOM    321  C   TRP B   9      -5.671   1.544   0.001  1.00  0.00           C  
ATOM    322  O   TRP B   9      -4.794   0.729   0.239  1.00  0.00           O  
ATOM    323  CB  TRP B   9      -5.212   3.006  -2.005  1.00  0.00           C  
ATOM    324  CG  TRP B   9      -6.236   3.915  -2.628  1.00  0.00           C  
ATOM    325  CD1 TRP B   9      -6.110   5.228  -2.885  1.00  0.00           C  
ATOM    326  CD2 TRP B   9      -7.605   3.501  -3.104  1.00  0.00           C  
ATOM    327  NE1 TRP B   9      -7.203   5.664  -3.458  1.00  0.00           N  
ATOM    328  CE2 TRP B   9      -8.106   4.679  -3.625  1.00  0.00           C  
ATOM    329  CE3 TRP B   9      -8.333   2.313  -3.115  1.00  0.00           C  
ATOM    330  CZ2 TRP B   9      -9.365   4.736  -4.222  1.00  0.00           C  
ATOM    331  CZ3 TRP B   9      -9.601   2.357  -3.711  1.00  0.00           C  
ATOM    332  CH2 TRP B   9     -10.104   3.546  -4.265  1.00  0.00           C  
ATOM    333  H   TRP B   9      -3.229   2.660   0.035  1.00  0.00           H  
ATOM    334  HA  TRP B   9      -6.072   3.615  -0.093  1.00  0.00           H  
ATOM    335  HB2 TRP B   9      -4.218   3.371  -2.310  1.00  0.00           H  
ATOM    336  HB3 TRP B   9      -5.352   2.015  -2.462  1.00  0.00           H  
ATOM    337  HD1 TRP B   9      -5.228   5.825  -2.651  1.00  0.00           H  
ATOM    338  HE1 TRP B   9      -7.353   6.641  -3.754  1.00  0.00           H  
ATOM    339  HE3 TRP B   9      -7.934   1.401  -2.684  1.00  0.00           H  
ATOM    340  HZ2 TRP B   9      -9.751   5.663  -4.633  1.00  0.00           H  
ATOM    341  HZ3 TRP B   9     -10.203   1.454  -3.744  1.00  0.00           H  
ATOM    342  HH2 TRP B   9     -11.084   3.545  -4.732  1.00  0.00           H  
HETATM  343  N   DLE B  10      -6.981   1.235   0.121  1.00  0.00           N  
HETATM  344  CA  DLE B  10      -7.389  -0.060   0.663  1.00  0.00           C  
HETATM  345  CB  DLE B  10      -8.805  -0.443   0.138  1.00  0.00           C  
HETATM  346  CG  DLE B  10      -9.428  -1.703   0.817  1.00  0.00           C  
HETATM  347  CD1 DLE B  10     -10.840  -1.975   0.224  1.00  0.00           C  
HETATM  348  CD2 DLE B  10      -8.534  -2.959   0.642  1.00  0.00           C  
HETATM  349  C   DLE B  10      -7.447   0.024   2.172  1.00  0.00           C  
HETATM  350  O   DLE B  10      -8.300   0.749   2.658  1.00  0.00           O  
HETATM  351  H   DLE B  10      -7.694   1.912  -0.081  1.00  0.00           H  
HETATM  352  HA  DLE B  10      -6.683  -0.841   0.343  1.00  0.00           H  
HETATM  353  HB2 DLE B  10      -9.490   0.401   0.320  1.00  0.00           H  
HETATM  354  HB3 DLE B  10      -8.744  -0.595  -0.951  1.00  0.00           H  
HETATM  355  HG  DLE B  10      -9.558  -1.521   1.898  1.00  0.00           H  
HETATM  356 HD11 DLE B  10     -10.771  -2.189  -0.854  1.00  0.00           H  
HETATM  357 HD12 DLE B  10     -11.311  -2.838   0.721  1.00  0.00           H  
HETATM  358 HD13 DLE B  10     -11.495  -1.101   0.366  1.00  0.00           H  
HETATM  359 HD21 DLE B  10      -8.316  -3.096  -0.425  1.00  0.00           H  
HETATM  360 HD22 DLE B  10      -7.588  -2.861   1.194  1.00  0.00           H  
HETATM  361 HD23 DLE B  10      -9.044  -3.859   1.018  1.00  0.00           H  
ATOM    362  N   TRP B  11      -6.606  -0.708   2.942  1.00  0.00           N  
ATOM    363  CA  TRP B  11      -6.833  -0.807   4.388  1.00  0.00           C  
ATOM    364  C   TRP B  11      -5.737  -0.203   5.247  1.00  0.00           C  
ATOM    365  O   TRP B  11      -4.585  -0.199   4.846  1.00  0.00           O  
ATOM    366  CB  TRP B  11      -6.994  -2.301   4.772  1.00  0.00           C  
ATOM    367  CG  TRP B  11      -7.210  -2.421   6.258  1.00  0.00           C  
ATOM    368  CD1 TRP B  11      -6.345  -2.877   7.180  1.00  0.00           C  
ATOM    369  CD2 TRP B  11      -8.464  -2.017   6.990  1.00  0.00           C  
ATOM    370  NE1 TRP B  11      -6.894  -2.796   8.366  1.00  0.00           N  
ATOM    371  CE2 TRP B  11      -8.139  -2.284   8.307  1.00  0.00           C  
ATOM    372  CE3 TRP B  11      -9.702  -1.494   6.620  1.00  0.00           C  
ATOM    373  CZ2 TRP B  11      -9.030  -2.023   9.347  1.00  0.00           C  
ATOM    374  CZ3 TRP B  11     -10.607  -1.225   7.655  1.00  0.00           C  
ATOM    375  CH2 TRP B  11     -10.276  -1.484   8.997  1.00  0.00           C  
ATOM    376  H   TRP B  11      -5.850  -1.237   2.541  1.00  0.00           H  
ATOM    377  HA  TRP B  11      -7.778  -0.315   4.664  1.00  0.00           H  
ATOM    378  HB2 TRP B  11      -7.851  -2.743   4.239  1.00  0.00           H  
ATOM    379  HB3 TRP B  11      -6.087  -2.856   4.487  1.00  0.00           H  
ATOM    380  HD1 TRP B  11      -5.342  -3.249   6.965  1.00  0.00           H  
ATOM    381  HE1 TRP B  11      -6.431  -3.084   9.243  1.00  0.00           H  
ATOM    382  HE3 TRP B  11      -9.951  -1.306   5.580  1.00  0.00           H  
ATOM    383  HZ2 TRP B  11      -8.767  -2.230  10.379  1.00  0.00           H  
ATOM    384  HZ3 TRP B  11     -11.581  -0.810   7.416  1.00  0.00           H  
ATOM    385  HH2 TRP B  11     -10.998  -1.262   9.777  1.00  0.00           H  
HETATM  386  N   DLE B  12      -6.078   0.296   6.459  1.00  0.00           N  
HETATM  387  CA  DLE B  12      -5.073   0.851   7.368  1.00  0.00           C  
HETATM  388  CB  DLE B  12      -5.292   0.270   8.797  1.00  0.00           C  
HETATM  389  CG  DLE B  12      -4.556   1.026   9.948  1.00  0.00           C  
HETATM  390  CD1 DLE B  12      -4.934   0.396  11.319  1.00  0.00           C  
HETATM  391  CD2 DLE B  12      -3.013   1.014   9.777  1.00  0.00           C  
HETATM  392  C   DLE B  12      -5.260   2.349   7.399  1.00  0.00           C  
HETATM  393  O   DLE B  12      -6.358   2.768   7.725  1.00  0.00           O  
HETATM  394  H   DLE B  12      -7.034   0.348   6.757  1.00  0.00           H  
HETATM  395  HA  DLE B  12      -4.051   0.595   7.054  1.00  0.00           H  
HETATM  396  HB2 DLE B  12      -6.370   0.312   9.023  1.00  0.00           H  
HETATM  397  HB3 DLE B  12      -4.991  -0.789   8.796  1.00  0.00           H  
HETATM  398  HG  DLE B  12      -4.892   2.078   9.971  1.00  0.00           H  
HETATM  399 HD11 DLE B  12      -4.614  -0.656  11.359  1.00  0.00           H  
HETATM  400 HD12 DLE B  12      -4.449   0.940  12.144  1.00  0.00           H  
HETATM  401 HD13 DLE B  12      -6.023   0.436  11.480  1.00  0.00           H  
HETATM  402 HD21 DLE B  12      -2.708   1.541   8.862  1.00  0.00           H  
HETATM  403 HD22 DLE B  12      -2.532   1.523  10.626  1.00  0.00           H  
HETATM  404 HD23 DLE B  12      -2.642  -0.021   9.738  1.00  0.00           H  
ATOM    405  N   TRP B  13      -4.235   3.177   7.093  1.00  0.00           N  
ATOM    406  CA  TRP B  13      -4.381   4.621   7.265  1.00  0.00           C  
ATOM    407  C   TRP B  13      -4.457   5.317   5.924  1.00  0.00           C  
ATOM    408  O   TRP B  13      -3.470   5.854   5.449  1.00  0.00           O  
ATOM    409  CB  TRP B  13      -3.216   5.150   8.139  1.00  0.00           C  
ATOM    410  CG  TRP B  13      -3.525   6.567   8.539  1.00  0.00           C  
ATOM    411  CD1 TRP B  13      -2.994   7.704   8.061  1.00  0.00           C  
ATOM    412  CD2 TRP B  13      -4.543   6.956   9.581  1.00  0.00           C  
ATOM    413  NE1 TRP B  13      -3.548   8.726   8.665  1.00  0.00           N  
ATOM    414  CE2 TRP B  13      -4.470   8.335   9.567  1.00  0.00           C  
ATOM    415  CE3 TRP B  13      -5.410   6.262  10.422  1.00  0.00           C  
ATOM    416  CZ2 TRP B  13      -5.274   9.114  10.398  1.00  0.00           C  
ATOM    417  CZ3 TRP B  13      -6.225   7.033  11.261  1.00  0.00           C  
ATOM    418  CH2 TRP B  13      -6.158   8.436  11.248  1.00  0.00           C  
ATOM    419  H   TRP B  13      -3.352   2.829   6.758  1.00  0.00           H  
ATOM    420  HA  TRP B  13      -5.305   4.874   7.811  1.00  0.00           H  
ATOM    421  HB2 TRP B  13      -3.133   4.540   9.052  1.00  0.00           H  
ATOM    422  HB3 TRP B  13      -2.263   5.080   7.597  1.00  0.00           H  
ATOM    423  HD1 TRP B  13      -2.227   7.757   7.287  1.00  0.00           H  
ATOM    424  HE1 TRP B  13      -3.314   9.711   8.471  1.00  0.00           H  
ATOM    425  HE3 TRP B  13      -5.451   5.178  10.426  1.00  0.00           H  
ATOM    426  HZ2 TRP B  13      -5.215  10.197  10.384  1.00  0.00           H  
ATOM    427  HZ3 TRP B  13      -6.921   6.537  11.930  1.00  0.00           H  
ATOM    428  HH2 TRP B  13      -6.803   9.006  11.909  1.00  0.00           H  
HETATM  429  N   DLE B  14      -5.646   5.339   5.287  1.00  0.00           N  
HETATM  430  CA  DLE B  14      -5.814   6.146   4.079  1.00  0.00           C  
HETATM  431  CB  DLE B  14      -5.920   7.634   4.517  1.00  0.00           C  
HETATM  432  CG  DLE B  14      -6.260   8.644   3.378  1.00  0.00           C  
HETATM  433  CD1 DLE B  14      -6.488  10.057   3.985  1.00  0.00           C  
HETATM  434  CD2 DLE B  14      -5.139   8.719   2.304  1.00  0.00           C  
HETATM  435  C   DLE B  14      -7.086   5.736   3.377  1.00  0.00           C  
HETATM  436  O   DLE B  14      -8.062   5.516   4.075  1.00  0.00           O  
HETATM  437  H   DLE B  14      -6.453   4.872   5.661  1.00  0.00           H  
HETATM  438  HA  DLE B  14      -4.962   5.999   3.403  1.00  0.00           H  
HETATM  439  HB2 DLE B  14      -6.715   7.685   5.279  1.00  0.00           H  
HETATM  440  HB3 DLE B  14      -4.978   7.939   4.999  1.00  0.00           H  
HETATM  441  HG  DLE B  14      -7.200   8.339   2.884  1.00  0.00           H  
HETATM  442 HD11 DLE B  14      -5.572  10.415   4.482  1.00  0.00           H  
HETATM  443 HD12 DLE B  14      -6.762  10.778   3.199  1.00  0.00           H  
HETATM  444 HD13 DLE B  14      -7.302  10.036   4.726  1.00  0.00           H  
HETATM  445 HD21 DLE B  14      -4.174   8.967   2.772  1.00  0.00           H  
HETATM  446 HD22 DLE B  14      -5.036   7.768   1.769  1.00  0.00           H  
HETATM  447 HD23 DLE B  14      -5.375   9.493   1.558  1.00  0.00           H  
ATOM    448  N   TRP B  15      -7.140   5.626   2.032  1.00  0.00           N  
ATOM    449  CA  TRP B  15      -8.424   5.333   1.401  1.00  0.00           C  
ATOM    450  C   TRP B  15      -8.638   3.841   1.416  1.00  0.00           C  
ATOM    451  O   TRP B  15      -8.722   3.205   0.375  1.00  0.00           O  
ATOM    452  CB  TRP B  15      -8.490   5.936  -0.025  1.00  0.00           C  
ATOM    453  CG  TRP B  15      -9.931   5.998  -0.451  1.00  0.00           C  
ATOM    454  CD1 TRP B  15     -10.608   5.130  -1.219  1.00  0.00           C  
ATOM    455  CD2 TRP B  15     -10.896   7.082  -0.049  1.00  0.00           C  
ATOM    456  NE1 TRP B  15     -11.842   5.547  -1.357  1.00  0.00           N  
ATOM    457  CE2 TRP B  15     -12.060   6.694  -0.683  1.00  0.00           C  
ATOM    458  CE3 TRP B  15     -10.820   8.228   0.741  1.00  0.00           C  
ATOM    459  CZ2 TRP B  15     -13.232   7.442  -0.574  1.00  0.00           C  
ATOM    460  CZ3 TRP B  15     -11.994   8.982   0.868  1.00  0.00           C  
ATOM    461  CH2 TRP B  15     -13.179   8.596   0.220  1.00  0.00           C  
ATOM    462  H   TRP B  15      -6.320   5.711   1.454  1.00  0.00           H  
ATOM    463  HA  TRP B  15      -9.241   5.797   1.982  1.00  0.00           H  
ATOM    464  HB2 TRP B  15      -8.090   6.962  -0.022  1.00  0.00           H  
ATOM    465  HB3 TRP B  15      -7.891   5.338  -0.727  1.00  0.00           H  
ATOM    466  HD1 TRP B  15     -10.180   4.224  -1.643  1.00  0.00           H  
ATOM    467  HE1 TRP B  15     -12.562   5.051  -1.903  1.00  0.00           H  
ATOM    468  HE3 TRP B  15      -9.897   8.516   1.233  1.00  0.00           H  
ATOM    469  HZ2 TRP B  15     -14.142   7.139  -1.080  1.00  0.00           H  
ATOM    470  HZ3 TRP B  15     -11.986   9.880   1.479  1.00  0.00           H  
ATOM    471  HH2 TRP B  15     -14.072   9.203   0.336  1.00  0.00           H  
TER     472      TRP B  15                                                      
HETATM  473  C1  SIN B 101       3.342  -2.692   1.727  1.00  0.00           C  
HETATM  474  O1  SIN B 101       4.275  -3.479   1.733  1.00  0.00           O  
HETATM  475  C2  SIN B 101       3.599  -1.231   1.976  1.00  0.00           C  
HETATM  476  C3  SIN B 101       2.854  -0.599   3.185  1.00  0.00           C  
HETATM  477  C4  SIN B 101       2.449   0.810   2.825  1.00  0.00           C  
HETATM  478  O3  SIN B 101       1.295   1.148   3.023  1.00  0.00           O  
HETATM  479  H21 SIN B 101       4.674  -1.069   2.136  1.00  0.00           H  
HETATM  480  H31 SIN B 101       3.479  -0.592   4.092  1.00  0.00           H  
CONECT    1  473                                                                
CONECT    3   11                                                                
CONECT   11    3   12                                                           
CONECT   12   11   13   16   18                                                 
CONECT   13   12   14   15   19                                                 
CONECT   14   13   20   21   22                                                 
CONECT   15   13   23   24   25                                                 
CONECT   16   12   17   26                                                      
CONECT   17   16                                                                
CONECT   18   12                                                                
CONECT   19   13                                                                
CONECT   20   14                                                                
CONECT   21   14                                                                
CONECT   22   14                                                                
CONECT   23   15                                                                
CONECT   24   15                                                                
CONECT   25   15                                                                
CONECT   26   16                                                                
CONECT   28   42                                                                
CONECT   42   28   43                                                           
CONECT   43   42   44   47   49                                                 
CONECT   44   43   45   46   50                                                 
CONECT   45   44   51   52   53                                                 
CONECT   46   44   54   55   56                                                 
CONECT   47   43   48   57                                                      
CONECT   48   47                                                                
CONECT   49   43                                                                
CONECT   50   44                                                                
CONECT   51   45                                                                
CONECT   52   45                                                                
CONECT   53   45                                                                
CONECT   54   46                                                                
CONECT   55   46                                                                
CONECT   56   46                                                                
CONECT   57   47                                                                
CONECT   59   81                                                                
CONECT   81   59   82   89                                                      
CONECT   82   81   83   87   90                                                 
CONECT   83   82   84   91   92                                                 
CONECT   84   83   85   86   93                                                 
CONECT   85   84   94   95   96                                                 
CONECT   86   84   97   98   99                                                 
CONECT   87   82   88  100                                                      
CONECT   88   87                                                                
CONECT   89   81                                                                
CONECT   90   82                                                                
CONECT   91   83                                                                
CONECT   92   83                                                                
CONECT   93   84                                                                
CONECT   94   85                                                                
CONECT   95   85                                                                
CONECT   96   85                                                                
CONECT   97   86                                                                
CONECT   98   86                                                                
CONECT   99   86                                                                
CONECT  100   87                                                                
CONECT  102  124                                                                
CONECT  124  102  125  132                                                      
CONECT  125  124  126  130  133                                                 
CONECT  126  125  127  134  135                                                 
CONECT  127  126  128  129  136                                                 
CONECT  128  127  137  138  139                                                 
CONECT  129  127  140  141  142                                                 
CONECT  130  125  131  143                                                      
CONECT  131  130                                                                
CONECT  132  124                                                                
CONECT  133  125                                                                
CONECT  134  126                                                                
CONECT  135  126                                                                
CONECT  136  127                                                                
CONECT  137  128                                                                
CONECT  138  128                                                                
CONECT  139  128                                                                
CONECT  140  129                                                                
CONECT  141  129                                                                
CONECT  142  129                                                                
CONECT  143  130                                                                
CONECT  145  167                                                                
CONECT  167  145  168  175                                                      
CONECT  168  167  169  173  176                                                 
CONECT  169  168  170  177  178                                                 
CONECT  170  169  171  172  179                                                 
CONECT  171  170  180  181  182                                                 
CONECT  172  170  183  184  185                                                 
CONECT  173  168  174  186                                                      
CONECT  174  173                                                                
CONECT  175  167                                                                
CONECT  176  168                                                                
CONECT  177  169                                                                
CONECT  178  169                                                                
CONECT  179  170                                                                
CONECT  180  171                                                                
CONECT  181  171                                                                
CONECT  182  171                                                                
CONECT  183  172                                                                
CONECT  184  172                                                                
CONECT  185  172                                                                
CONECT  186  173                                                                
CONECT  211  477                                                                
CONECT  236  244                                                                
CONECT  244  236  245  252                                                      
CONECT  245  244  246  250  253                                                 
CONECT  246  245  247  254  255                                                 
CONECT  247  246  248  249  256                                                 
CONECT  248  247  257  258  259                                                 
CONECT  249  247  260  261  262                                                 
CONECT  250  245  251  263                                                      
CONECT  251  250                                                                
CONECT  252  244                                                                
CONECT  253  245                                                                
CONECT  254  246                                                                
CONECT  255  246                                                                
CONECT  256  247                                                                
CONECT  257  248                                                                
CONECT  258  248                                                                
CONECT  259  248                                                                
CONECT  260  249                                                                
CONECT  261  249                                                                
CONECT  262  249                                                                
CONECT  263  250                                                                
CONECT  265  273                                                                
CONECT  273  265  274                                                           
CONECT  274  273  275  278  280                                                 
CONECT  275  274  276  277  281                                                 
CONECT  276  275  282  283  284                                                 
CONECT  277  275  285  286  287                                                 
CONECT  278  274  279  288                                                      
CONECT  279  278                                                                
CONECT  280  274                                                                
CONECT  281  275                                                                
CONECT  282  276                                                                
CONECT  283  276                                                                
CONECT  284  276                                                                
CONECT  285  277                                                                
CONECT  286  277                                                                
CONECT  287  277                                                                
CONECT  288  278                                                                
CONECT  290  304                                                                
CONECT  304  290  305                                                           
CONECT  305  304  306  309  311                                                 
CONECT  306  305  307  308  312                                                 
CONECT  307  306  313  314  315                                                 
CONECT  308  306  316  317  318                                                 
CONECT  309  305  310  319                                                      
CONECT  310  309                                                                
CONECT  311  305                                                                
CONECT  312  306                                                                
CONECT  313  307                                                                
CONECT  314  307                                                                
CONECT  315  307                                                                
CONECT  316  308                                                                
CONECT  317  308                                                                
CONECT  318  308                                                                
CONECT  319  309                                                                
CONECT  321  343                                                                
CONECT  343  321  344  351                                                      
CONECT  344  343  345  349  352                                                 
CONECT  345  344  346  353  354                                                 
CONECT  346  345  347  348  355                                                 
CONECT  347  346  356  357  358                                                 
CONECT  348  346  359  360  361                                                 
CONECT  349  344  350  362                                                      
CONECT  350  349                                                                
CONECT  351  343                                                                
CONECT  352  344                                                                
CONECT  353  345                                                                
CONECT  354  345                                                                
CONECT  355  346                                                                
CONECT  356  347                                                                
CONECT  357  347                                                                
CONECT  358  347                                                                
CONECT  359  348                                                                
CONECT  360  348                                                                
CONECT  361  348                                                                
CONECT  362  349                                                                
CONECT  364  386                                                                
CONECT  386  364  387  394                                                      
CONECT  387  386  388  392  395                                                 
CONECT  388  387  389  396  397                                                 
CONECT  389  388  390  391  398                                                 
CONECT  390  389  399  400  401                                                 
CONECT  391  389  402  403  404                                                 
CONECT  392  387  393  405                                                      
CONECT  393  392                                                                
CONECT  394  386                                                                
CONECT  395  387                                                                
CONECT  396  388                                                                
CONECT  397  388                                                                
CONECT  398  389                                                                
CONECT  399  390                                                                
CONECT  400  390                                                                
CONECT  401  390                                                                
CONECT  402  391                                                                
CONECT  403  391                                                                
CONECT  404  391                                                                
CONECT  405  392                                                                
CONECT  407  429                                                                
CONECT  429  407  430  437                                                      
CONECT  430  429  431  435  438                                                 
CONECT  431  430  432  439  440                                                 
CONECT  432  431  433  434  441                                                 
CONECT  433  432  442  443  444                                                 
CONECT  434  432  445  446  447                                                 
CONECT  435  430  436  448                                                      
CONECT  436  435                                                                
CONECT  437  429                                                                
CONECT  438  430                                                                
CONECT  439  431                                                                
CONECT  440  431                                                                
CONECT  441  432                                                                
CONECT  442  433                                                                
CONECT  443  433                                                                
CONECT  444  433                                                                
CONECT  445  434                                                                
CONECT  446  434                                                                
CONECT  447  434                                                                
CONECT  448  435                                                                
CONECT  473    1  474  475                                                      
CONECT  474  473                                                                
CONECT  475  473  476  479                                                      
CONECT  476  475  477  480                                                      
CONECT  477  211  476  478                                                      
CONECT  478  477                                                                
CONECT  479  475                                                                
CONECT  480  476                                                                
MASTER      215    0   12    0    3    0    0    6  242    2  225    3          
END