HEADER    FIMBRIAL PROTEIN                        05-OCT-95   1NIL              
TITLE     A COMPARISON OF NMR SOLUTION STRUCTURES OF THE RECEPTOR BINDING       
TITLE    2 DOMAINS OF PSEUDOMONAS AERUGINOSA PILI STRAINS PAO, KB7, AND PAK:    
TITLE    3 IMPLICATIONS FOR RECEPTOR BINDING AND SYNTHETIC VACCINE DESIGN       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PAK PILIN, TRANS;                                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: FIMBRIAL PROTEIN;                                           
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;                         
SOURCE   3 ORGANISM_TAXID: 287;                                                 
SOURCE   4 STRAIN: K                                                            
KEYWDS    FIMBRIAL PROTEIN                                                      
EXPDTA    SOLUTION NMR                                                          
AUTHOR    A.P.CAMPBELL,C.MCINNES,R.S.HODGES,B.D.SYKES                           
REVDAT   3   29-NOV-17 1NIL    1       REMARK HELIX                             
REVDAT   2   24-FEB-09 1NIL    1       VERSN                                    
REVDAT   1   29-JAN-96 1NIL    0                                                
JRNL        AUTH   A.P.CAMPBELL,C.MCINNES,R.S.HODGES,B.D.SYKES                  
JRNL        TITL   COMPARISON OF NMR SOLUTION STRUCTURES OF THE RECEPTOR        
JRNL        TITL 2 BINDING DOMAINS OF PSEUDOMONAS AERUGINOSA PILI STRAINS PAO,  
JRNL        TITL 3 KB7, AND PAK: IMPLICATIONS FOR RECEPTOR BINDING AND          
JRNL        TITL 4 SYNTHETIC VACCINE DESIGN.                                    
JRNL        REF    BIOCHEMISTRY                  V.  34 16255 1995              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   8845350                                                      
JRNL        DOI    10.1021/BI00050A005                                          
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   C.MCINNES,C.M.KAY,R.S.HODGES,B.D.SYKES                       
REMARK   1  TITL   CONFORMATIONAL DIFFERENCES BETWEEN CIS AND TRANS PROLINE     
REMARK   1  TITL 2 ISOMERS OF A PEPTIDE ANTIGEN REPRESENTING THE RECEPTOR       
REMARK   1  TITL 3 BINDING DOMAIN OF PSEUDOMONAS AERUGINOSA AS STUDIED BY 1H    
REMARK   1  TITL 4 NMR                                                          
REMARK   1  REF    BIOPOLYMERS                   V.  34  1221 1994              
REMARK   1  REFN                   ISSN 0006-3525                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   C.MCINNES,F.D.SOENNICHSEN,C.M.KAY,R.S.HODGES,B.D.SYKES       
REMARK   1  TITL   NMR SOLUTION STRUCTURE AND FLEXIBILITY OF A PEPTIDE ANTIGEN  
REMARK   1  TITL 2 REPRESENTING THE RECEPTOR BINDING DOMAIN OF PSEUDOMONAS      
REMARK   1  TITL 3 AERUGINOSA                                                   
REMARK   1  REF    BIOCHEMISTRY                  V.  32 13432 1993              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   2                                                                      
REMARK   2 RESOLUTION. NOT APPLICABLE.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PEPFLEX II                                           
REMARK   3   AUTHORS     : NULL                                                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1NIL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 100 THE DEPOSITION ID IS D_1000175303.                                   
REMARK 210                                                                      
REMARK 210 EXPERIMENTAL DETAILS                                                 
REMARK 210  EXPERIMENT TYPE                : NMR                                
REMARK 210  TEMPERATURE           (KELVIN) : NULL                               
REMARK 210  PH                             : NULL                               
REMARK 210  IONIC STRENGTH                 : NULL                               
REMARK 210  PRESSURE                       : NULL                               
REMARK 210  SAMPLE CONTENTS                : NULL                               
REMARK 210                                                                      
REMARK 210  NMR EXPERIMENTS CONDUCTED      : NULL                               
REMARK 210  SPECTROMETER FIELD STRENGTH    : NULL                               
REMARK 210  SPECTROMETER MODEL             : NULL                               
REMARK 210  SPECTROMETER MANUFACTURER      : NULL                               
REMARK 210                                                                      
REMARK 210  STRUCTURE DETERMINATION.                                            
REMARK 210   SOFTWARE USED                 : NULL                               
REMARK 210   METHOD USED                   : NULL                               
REMARK 210                                                                      
REMARK 210 CONFORMERS, NUMBER CALCULATED   : NULL                               
REMARK 210 CONFORMERS, NUMBER SUBMITTED    : 1                                  
REMARK 210 CONFORMERS, SELECTION CRITERIA  : NULL                               
REMARK 210                                                                      
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL                
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 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
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   C    SER A   131     H    ASP A   132              1.48            
REMARK 500   C    ACE A   127     H    LYS A   128              1.50            
REMARK 500   C    LYS A   128     H    CYS A   129              1.59            
REMARK 500   O    SER A   131     N    ASP A   132              1.67            
REMARK 500   O    ACE A   127     N    LYS A   128              1.70            
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    ACE A 127   C     LYS A 128   N      -0.304                       
REMARK 500    LYS A 128   N     LYS A 128   CA     -0.347                       
REMARK 500    LYS A 128   CA    LYS A 128   CB     -0.256                       
REMARK 500    LYS A 128   CB    LYS A 128   CG     -0.491                       
REMARK 500    LYS A 128   CG    LYS A 128   CD     -0.360                       
REMARK 500    LYS A 128   CD    LYS A 128   CE     -0.488                       
REMARK 500    LYS A 128   CE    LYS A 128   NZ     -0.456                       
REMARK 500    LYS A 128   CA    LYS A 128   C      -0.266                       
REMARK 500    LYS A 128   C     LYS A 128   O      -0.247                       
REMARK 500    LYS A 128   C     CYS A 129   N      -0.258                       
REMARK 500    CYS A 129   N     CYS A 129   CA     -0.239                       
REMARK 500    CYS A 129   CA    CYS A 129   CB     -0.173                       
REMARK 500    CYS A 129   CB    CYS A 129   SG     -0.193                       
REMARK 500    CYS A 129   C     CYS A 129   O      -0.154                       
REMARK 500    CYS A 129   C     THR A 130   N      -0.162                       
REMARK 500    THR A 130   CA    THR A 130   CB     -0.219                       
REMARK 500    THR A 130   CB    THR A 130   OG1    -0.638                       
REMARK 500    THR A 130   CB    THR A 130   CG2    -0.595                       
REMARK 500    THR A 130   CA    THR A 130   C      -0.177                       
REMARK 500    THR A 130   C     THR A 130   O      -0.184                       
REMARK 500    SER A 131   N     SER A 131   CA     -0.159                       
REMARK 500    SER A 131   CA    SER A 131   CB     -0.362                       
REMARK 500    SER A 131   CB    SER A 131   OG     -1.170                       
REMARK 500    SER A 131   C     SER A 131   O      -0.259                       
REMARK 500    SER A 131   C     ASP A 132   N      -0.296                       
REMARK 500    ASP A 132   N     ASP A 132   CA     -0.133                       
REMARK 500    ASP A 132   CA    ASP A 132   CB     -0.200                       
REMARK 500    ASP A 132   CB    ASP A 132   CG     -0.662                       
REMARK 500    ASP A 132   CG    ASP A 132   OD1    -0.920                       
REMARK 500    ASP A 132   CG    ASP A 132   OD2    -0.860                       
REMARK 500    ASP A 132   CA    ASP A 132   C      -0.213                       
REMARK 500    ASP A 132   C     ASP A 132   O      -0.286                       
REMARK 500    GLN A 133   N     GLN A 133   CA     -0.185                       
REMARK 500    GLN A 133   CA    GLN A 133   CB     -0.469                       
REMARK 500    GLN A 133   CB    GLN A 133   CG     -0.444                       
REMARK 500    GLN A 133   CG    GLN A 133   CD     -0.524                       
REMARK 500    GLN A 133   CD    GLN A 133   OE1    -0.814                       
REMARK 500    GLN A 133   CD    GLN A 133   NE2    -0.927                       
REMARK 500    ASP A 134   CB    ASP A 134   CG     -0.192                       
REMARK 500    ASP A 134   CG    ASP A 134   OD1    -0.705                       
REMARK 500    ASP A 134   CG    ASP A 134   OD2    -0.675                       
REMARK 500    GLU A 135   CG    GLU A 135   CD     -0.138                       
REMARK 500    GLU A 135   CD    GLU A 135   OE1    -0.502                       
REMARK 500    GLU A 135   CD    GLU A 135   OE2    -0.475                       
REMARK 500    GLN A 136   CB    GLN A 136   CG     -0.566                       
REMARK 500    GLN A 136   CG    GLN A 136   CD     -0.258                       
REMARK 500    GLN A 136   CD    GLN A 136   OE1    -0.617                       
REMARK 500    GLN A 136   CD    GLN A 136   NE2    -0.701                       
REMARK 500    PHE A 137   CG    PHE A 137   CD2    -0.662                       
REMARK 500    PHE A 137   CG    PHE A 137   CD1    -0.703                       
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      72 BOND DEVIATIONS.                              
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    LYS A 128   CA  -  CB  -  CG  ANGL. DEV. =  28.6 DEGREES          
REMARK 500    LYS A 128   CB  -  CG  -  CD  ANGL. DEV. =  35.0 DEGREES          
REMARK 500    LYS A 128   CG  -  CD  -  CE  ANGL. DEV. =  41.6 DEGREES          
REMARK 500    LYS A 128   CD  -  CE  -  NZ  ANGL. DEV. =  52.3 DEGREES          
REMARK 500    CYS A 129   CB  -  CA  -  C   ANGL. DEV. =   7.6 DEGREES          
REMARK 500    THR A 130   OG1 -  CB  -  CG2 ANGL. DEV. = -17.9 DEGREES          
REMARK 500    THR A 130   CA  -  CB  -  CG2 ANGL. DEV. =  11.5 DEGREES          
REMARK 500    SER A 131   CA  -  CB  -  OG  ANGL. DEV. =  45.9 DEGREES          
REMARK 500    SER A 131   O   -  C   -  N   ANGL. DEV. = -10.1 DEGREES          
REMARK 500    ASP A 132   CA  -  CB  -  CG  ANGL. DEV. =  30.2 DEGREES          
REMARK 500    ASP A 132   OD1 -  CG  -  OD2 ANGL. DEV. = -84.1 DEGREES          
REMARK 500    ASP A 132   CB  -  CG  -  OD1 ANGL. DEV. =  42.6 DEGREES          
REMARK 500    ASP A 132   CB  -  CG  -  OD2 ANGL. DEV. =  41.5 DEGREES          
REMARK 500    GLN A 133   OE1 -  CD  -  NE2 ANGL. DEV. = 102.4 DEGREES          
REMARK 500    GLN A 133   CG  -  CD  -  OE1 ANGL. DEV. =  49.7 DEGREES          
REMARK 500    GLN A 133   CG  -  CD  -  NE2 ANGL. DEV. =  52.5 DEGREES          
REMARK 500    ASP A 134   OD1 -  CG  -  OD2 ANGL. DEV. = -81.7 DEGREES          
REMARK 500    ASP A 134   CB  -  CG  -  OD1 ANGL. DEV. =  42.7 DEGREES          
REMARK 500    ASP A 134   CB  -  CG  -  OD2 ANGL. DEV. =  39.1 DEGREES          
REMARK 500    GLU A 135   OE1 -  CD  -  OE2 ANGL. DEV. = -34.3 DEGREES          
REMARK 500    GLU A 135   CG  -  CD  -  OE1 ANGL. DEV. =  22.1 DEGREES          
REMARK 500    GLU A 135   CG  -  CD  -  OE2 ANGL. DEV. =  12.2 DEGREES          
REMARK 500    GLN A 136   CA  -  CB  -  CG  ANGL. DEV. =  28.5 DEGREES          
REMARK 500    GLN A 136   CB  -  CG  -  CD  ANGL. DEV. =  33.3 DEGREES          
REMARK 500    GLN A 136   OE1 -  CD  -  NE2 ANGL. DEV. = -53.8 DEGREES          
REMARK 500    GLN A 136   CG  -  CD  -  OE1 ANGL. DEV. =  26.2 DEGREES          
REMARK 500    GLN A 136   CG  -  CD  -  NE2 ANGL. DEV. =  27.4 DEGREES          
REMARK 500    PHE A 137   CB  -  CG  -  CD2 ANGL. DEV. =  52.4 DEGREES          
REMARK 500    PHE A 137   CD1 -  CG  -  CD2 ANGL. DEV. = 109.5 DEGREES          
REMARK 500    PHE A 137   CB  -  CG  -  CD1 ANGL. DEV. =  53.7 DEGREES          
REMARK 500    PHE A 137   CG  -  CD1 -  CE1 ANGL. DEV. =  54.5 DEGREES          
REMARK 500    PHE A 137   CG  -  CD2 -  CE2 ANGL. DEV. =  55.1 DEGREES          
REMARK 500    PHE A 137   CD1 -  CE1 -  CZ  ANGL. DEV. =  55.6 DEGREES          
REMARK 500    PHE A 137   CE1 -  CZ  -  CE2 ANGL. DEV. = 111.1 DEGREES          
REMARK 500    PHE A 137   CZ  -  CE2 -  CD2 ANGL. DEV. =  55.3 DEGREES          
REMARK 500    LYS A 140   CB  -  CG  -  CD  ANGL. DEV. =  15.7 DEGREES          
REMARK 500    LYS A 140   CD  -  CE  -  NZ  ANGL. DEV. =  19.8 DEGREES          
REMARK 500    SER A 143   CA  -  CB  -  OG  ANGL. DEV. =  52.9 DEGREES          
REMARK 500    LYS A 144   CA  -  CB  -  CG  ANGL. DEV. =  36.6 DEGREES          
REMARK 500    LYS A 144   CB  -  CG  -  CD  ANGL. DEV. =  34.4 DEGREES          
REMARK 500    LYS A 144   CG  -  CD  -  CE  ANGL. DEV. =  34.5 DEGREES          
REMARK 500    LYS A 144   CD  -  CE  -  NZ  ANGL. DEV. =  26.5 DEGREES          
REMARK 500    LYS A 144   CA  -  C   -  O   ANGL. DEV. =  30.1 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    SER A 131      -76.22    -83.31                                   
REMARK 500    ASP A 132      -72.12   -103.61                                   
REMARK 500    GLN A 133       85.78   -153.08                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1NIM   RELATED DB: PDB                                   
DBREF  1NIL A  128   144  UNP    P02973   FMPA_PSEAE     134    150             
SEQRES   1 A   18  ACE LYS CYS THR SER ASP GLN ASP GLU GLN PHE ILE PRO          
SEQRES   2 A   18  LYS GLY CYS SER LYS                                          
HET    ACE  A 127       6                                                       
HETNAM     ACE ACETYL GROUP                                                     
FORMUL   1  ACE    C2 H4 O                                                      
SSBOND   1 CYS A  129    CYS A  142                          1555   1555  1.24  
LINK         C   ACE A 127                 N   LYS A 128     1555   1555  1.03  
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                         
HETATM    1  C   ACE A 127      -2.510  -4.930   1.600  1.00  0.00           C  
HETATM    2  O   ACE A 127      -2.669  -4.664   2.426  1.00  0.00           O  
HETATM    3  CH3 ACE A 127      -3.392  -5.319   1.027  1.00  0.00           C  
HETATM    4  H1  ACE A 127      -3.653  -5.575   1.071  1.00  0.00           H  
HETATM    5  H2  ACE A 127      -3.462  -5.393   0.590  1.00  0.00           H  
HETATM    6  H3  ACE A 127      -3.771  -5.292   0.976  1.00  0.00           H  
ATOM      7  N   LYS A 128      -1.586  -4.898   1.141  1.00  0.00           N  
ATOM      8  CA  LYS A 128      -0.634  -4.538   1.590  1.00  0.00           C  
ATOM      9  C   LYS A 128      -0.376  -3.369   1.199  1.00  0.00           C  
ATOM     10  O   LYS A 128      -0.372  -3.135   0.245  1.00  0.00           O  
ATOM     11  CB  LYS A 128       0.357  -5.326   1.409  1.00  0.00           C  
ATOM     12  CG  LYS A 128       0.758  -5.982   0.723  1.00  0.00           C  
ATOM     13  CD  LYS A 128       1.627  -6.708   0.470  1.00  0.00           C  
ATOM     14  CE  LYS A 128       2.104  -7.391  -0.118  1.00  0.00           C  
ATOM     15  NZ  LYS A 128       2.778  -8.070  -0.499  1.00  0.00           N  
ATOM     16  H   LYS A 128      -1.574  -5.145   0.454  1.00  0.00           H  
ATOM     17  HA  LYS A 128      -0.824  -4.542   2.398  1.00  0.00           H  
ATOM     18  HB2 LYS A 128       0.772  -5.135   1.498  1.00  0.00           H  
ATOM     19  HB3 LYS A 128       0.430  -5.643   1.763  1.00  0.00           H  
ATOM     20  HG2 LYS A 128       0.486  -5.916   0.684  1.00  0.00           H  
ATOM     21  HG3 LYS A 128       0.668  -5.990   0.428  1.00  0.00           H  
ATOM     22  HD2 LYS A 128       1.900  -6.533   0.708  1.00  0.00           H  
ATOM     23  HD3 LYS A 128       1.655  -6.909   0.500  1.00  0.00           H  
ATOM     24  HE2 LYS A 128       1.917  -7.359  -0.229  1.00  0.00           H  
ATOM     25  HE3 LYS A 128       2.137  -7.421  -0.164  1.00  0.00           H  
ATOM     26  HZ1 LYS A 128       3.047  -8.213  -0.609  1.00  0.00           H  
ATOM     27  HZ2 LYS A 128       2.736  -8.182  -0.761  1.00  0.00           H  
ATOM     28  N   CYS A 129      -0.134  -2.648   1.963  1.00  0.00           N  
ATOM     29  CA  CYS A 129       0.142  -1.481   1.737  1.00  0.00           C  
ATOM     30  C   CYS A 129       1.508  -1.398   1.224  1.00  0.00           C  
ATOM     31  O   CYS A 129       1.720  -1.027   0.238  1.00  0.00           O  
ATOM     32  CB  CYS A 129      -0.188  -0.782   2.847  1.00  0.00           C  
ATOM     33  SG  CYS A 129      -1.759  -0.652   3.214  1.00  0.00           S  
ATOM     34  H   CYS A 129      -0.138  -2.965   2.718  1.00  0.00           H  
ATOM     35  HA  CYS A 129      -0.476  -1.122   1.101  1.00  0.00           H  
ATOM     36  HB2 CYS A 129       0.274  -1.114   3.546  1.00  0.00           H  
ATOM     37  HB3 CYS A 129       0.082   0.033   2.763  1.00  0.00           H  
ATOM     38  N   THR A 130       2.414  -1.764   1.875  1.00  0.00           N  
ATOM     39  CA  THR A 130       3.750  -1.804   1.446  1.00  0.00           C  
ATOM     40  C   THR A 130       4.109  -3.020   0.988  1.00  0.00           C  
ATOM     41  O   THR A 130       4.113  -3.813   1.669  1.00  0.00           O  
ATOM     42  CB  THR A 130       4.550  -1.422   2.410  1.00  0.00           C  
ATOM     43  OG1 THR A 130       4.748  -1.953   2.961  1.00  0.00           O  
ATOM     44  CG2 THR A 130       4.324  -0.794   3.049  1.00  0.00           C  
ATOM     45  H   THR A 130       2.069  -2.039   2.667  1.00  0.00           H  
ATOM     46  HA  THR A 130       3.930  -1.197   0.710  1.00  0.00           H  
ATOM     47  HB  THR A 130       5.219  -1.162   2.221  1.00  0.00           H  
ATOM     48  HG1 THR A 130       4.641  -2.138   3.060  1.00  0.00           H  
ATOM     49 HG21 THR A 130       4.309  -0.625   3.350  1.00  0.00           H  
ATOM     50 HG22 THR A 130       4.203  -0.726   3.252  1.00  0.00           H  
ATOM     51 HG23 THR A 130       4.291  -0.528   3.054  1.00  0.00           H  
ATOM     52  N   SER A 131       4.404  -3.152  -0.174  1.00  0.00           N  
ATOM     53  CA  SER A 131       4.793  -4.256  -0.740  1.00  0.00           C  
ATOM     54  C   SER A 131       6.133  -4.675  -0.678  1.00  0.00           C  
ATOM     55  O   SER A 131       6.469  -5.365  -0.085  1.00  0.00           O  
ATOM     56  CB  SER A 131       4.411  -4.209  -1.837  1.00  0.00           C  
ATOM     57  OG  SER A 131       4.261  -4.256  -2.029  1.00  0.00           O  
ATOM     58  H   SER A 131       4.382  -2.419  -0.643  1.00  0.00           H  
ATOM     59  HA  SER A 131       4.340  -4.848  -0.381  1.00  0.00           H  
ATOM     60  HB2 SER A 131       4.387  -4.089  -2.252  1.00  0.00           H  
ATOM     61  HB3 SER A 131       4.248  -4.274  -2.124  1.00  0.00           H  
ATOM     62  HG  SER A 131       4.147  -4.272  -2.082  1.00  0.00           H  
ATOM     63  N   ASP A 132       6.882  -4.247  -1.258  1.00  0.00           N  
ATOM     64  CA  ASP A 132       8.182  -4.483  -1.141  1.00  0.00           C  
ATOM     65  C   ASP A 132       8.498  -3.367  -0.528  1.00  0.00           C  
ATOM     66  O   ASP A 132       8.683  -3.517   0.384  1.00  0.00           O  
ATOM     67  CB  ASP A 132       8.835  -4.807  -2.260  1.00  0.00           C  
ATOM     68  CG  ASP A 132       9.149  -5.461  -2.705  1.00  0.00           C  
ATOM     69  OD1 ASP A 132       9.185  -5.689  -2.940  1.00  0.00           O  
ATOM     70  OD2 ASP A 132       9.379  -5.759  -2.803  1.00  0.00           O  
ATOM     71  H   ASP A 132       6.488  -3.683  -1.712  1.00  0.00           H  
ATOM     72  HA  ASP A 132       8.432  -5.276  -0.622  1.00  0.00           H  
ATOM     73  HB2 ASP A 132       8.956  -4.672  -2.556  1.00  0.00           H  
ATOM     74  HB3 ASP A 132       9.013  -4.712  -2.511  1.00  0.00           H  
ATOM     75  HD2 ASP A 132       9.499  -5.994  -2.764  1.00  0.00           H  
ATOM     76  N   GLN A 133       8.534  -2.264  -1.013  1.00  0.00           N  
ATOM     77  CA  GLN A 133       8.660  -1.104  -0.501  1.00  0.00           C  
ATOM     78  C   GLN A 133       8.157   0.062  -1.098  1.00  0.00           C  
ATOM     79  O   GLN A 133       8.847   0.648  -1.768  1.00  0.00           O  
ATOM     80  CB  GLN A 133       9.693  -0.911  -0.322  1.00  0.00           C  
ATOM     81  CG  GLN A 133       9.941   0.023   0.153  1.00  0.00           C  
ATOM     82  CD  GLN A 133      10.886   0.216   0.340  1.00  0.00           C  
ATOM     83  OE1 GLN A 133      11.294   0.239   0.443  1.00  0.00           O  
ATOM     84  NE2 GLN A 133      11.252   0.362   0.390  1.00  0.00           N  
ATOM     85  H   GLN A 133       8.361  -2.256  -1.768  1.00  0.00           H  
ATOM     86  HA  GLN A 133       8.323  -1.258   0.177  1.00  0.00           H  
ATOM     87  HB2 GLN A 133       9.959  -1.551  -0.001  1.00  0.00           H  
ATOM     88  HB3 GLN A 133      10.048  -0.870  -0.844  1.00  0.00           H  
ATOM     89  HG2 GLN A 133       9.725   0.180   0.162  1.00  0.00           H  
ATOM     90  HG3 GLN A 133       9.607   0.456   0.378  1.00  0.00           H  
ATOM     91 HE21 GLN A 133      11.227   0.462   0.300  1.00  0.00           H  
ATOM     92 HE22 GLN A 133      11.530   0.364   0.515  1.00  0.00           H  
ATOM     93  N   ASP A 134       6.941   0.369  -0.860  1.00  0.00           N  
ATOM     94  CA  ASP A 134       6.304   1.442  -1.395  1.00  0.00           C  
ATOM     95  C   ASP A 134       5.777   2.302  -0.280  1.00  0.00           C  
ATOM     96  O   ASP A 134       4.622   2.223   0.122  1.00  0.00           O  
ATOM     97  CB  ASP A 134       5.249   1.027  -2.256  1.00  0.00           C  
ATOM     98  CG  ASP A 134       5.728   0.474  -3.356  1.00  0.00           C  
ATOM     99  OD1 ASP A 134       5.990   0.131  -3.687  1.00  0.00           O  
ATOM    100  OD2 ASP A 134       5.828   0.412  -3.918  1.00  0.00           O  
ATOM    101  H   ASP A 134       6.476  -0.213  -0.321  1.00  0.00           H  
ATOM    102  HA  ASP A 134       6.988   1.959  -1.998  1.00  0.00           H  
ATOM    103  HB2 ASP A 134       4.696   0.418  -1.806  1.00  0.00           H  
ATOM    104  HB3 ASP A 134       4.574   1.749  -2.532  1.00  0.00           H  
ATOM    105  HD2 ASP A 134       5.940   0.398  -4.205  1.00  0.00           H  
ATOM    106  N   GLU A 135       6.647   3.146   0.208  1.00  0.00           N  
ATOM    107  CA  GLU A 135       6.313   4.043   1.293  1.00  0.00           C  
ATOM    108  C   GLU A 135       5.441   5.196   0.844  1.00  0.00           C  
ATOM    109  O   GLU A 135       4.413   5.421   1.446  1.00  0.00           O  
ATOM    110  CB  GLU A 135       7.599   4.512   1.962  1.00  0.00           C  
ATOM    111  CG  GLU A 135       8.363   3.443   2.680  1.00  0.00           C  
ATOM    112  CD  GLU A 135       9.510   3.797   3.355  1.00  0.00           C  
ATOM    113  OE1 GLU A 135      10.256   3.777   3.278  1.00  0.00           O  
ATOM    114  OE2 GLU A 135       9.604   4.133   4.049  1.00  0.00           O  
ATOM    115  H   GLU A 135       7.573   3.129  -0.210  1.00  0.00           H  
ATOM    116  HA  GLU A 135       5.723   3.512   2.027  1.00  0.00           H  
ATOM    117  HB2 GLU A 135       8.221   4.973   1.287  1.00  0.00           H  
ATOM    118  HB3 GLU A 135       7.399   5.268   2.609  1.00  0.00           H  
ATOM    119  HG2 GLU A 135       8.195   2.929   2.732  1.00  0.00           H  
ATOM    120  HG3 GLU A 135       8.243   2.829   2.662  1.00  0.00           H  
ATOM    121  HE2 GLU A 135       9.398   4.158   4.317  1.00  0.00           H  
ATOM    122  N   GLN A 136       5.820   5.894  -0.209  1.00  0.00           N  
ATOM    123  CA  GLN A 136       4.988   6.922  -0.803  1.00  0.00           C  
ATOM    124  C   GLN A 136       3.752   6.424  -1.576  1.00  0.00           C  
ATOM    125  O   GLN A 136       2.846   7.191  -1.772  1.00  0.00           O  
ATOM    126  CB  GLN A 136       5.882   7.797  -1.688  1.00  0.00           C  
ATOM    127  CG  GLN A 136       6.563   8.465  -1.641  1.00  0.00           C  
ATOM    128  CD  GLN A 136       7.285   9.236  -2.306  1.00  0.00           C  
ATOM    129  OE1 GLN A 136       7.333   9.764  -2.624  1.00  0.00           O  
ATOM    130  NE2 GLN A 136       7.859   9.320  -2.532  1.00  0.00           N  
ATOM    131  H   GLN A 136       6.687   5.606  -0.631  1.00  0.00           H  
ATOM    132  HA  GLN A 136       4.595   7.532  -0.011  1.00  0.00           H  
ATOM    133  HB2 GLN A 136       5.977   7.932  -2.039  1.00  0.00           H  
ATOM    134  HB3 GLN A 136       5.954   7.877  -2.093  1.00  0.00           H  
ATOM    135  HG2 GLN A 136       6.561   8.476  -1.291  1.00  0.00           H  
ATOM    136  HG3 GLN A 136       6.531   8.385  -1.431  1.00  0.00           H  
ATOM    137 HE21 GLN A 136       7.985   9.271  -2.503  1.00  0.00           H  
ATOM    138 HE22 GLN A 136       8.130   9.426  -2.717  1.00  0.00           H  
ATOM    139  N   PHE A 137       3.699   5.185  -1.999  1.00  0.00           N  
ATOM    140  CA  PHE A 137       2.569   4.625  -2.734  1.00  0.00           C  
ATOM    141  C   PHE A 137       1.863   3.573  -1.915  1.00  0.00           C  
ATOM    142  O   PHE A 137       2.458   2.665  -1.503  1.00  0.00           O  
ATOM    143  CB  PHE A 137       3.079   4.083  -4.024  1.00  0.00           C  
ATOM    144  CG  PHE A 137       2.011   3.383  -4.848  1.00  0.00           C  
ATOM    145  CD1 PHE A 137       1.535   3.022  -5.172  1.00  0.00           C  
ATOM    146  CD2 PHE A 137       1.447   3.093  -5.191  1.00  0.00           C  
ATOM    147  CE1 PHE A 137       0.508   2.385  -5.824  1.00  0.00           C  
ATOM    148  CE2 PHE A 137       0.420   2.456  -5.842  1.00  0.00           C  
ATOM    149  CZ  PHE A 137      -0.049   2.102  -6.157  1.00  0.00           C  
ATOM    150  H   PHE A 137       4.463   4.631  -1.674  1.00  0.00           H  
ATOM    151  HA  PHE A 137       1.865   5.380  -2.976  1.00  0.00           H  
ATOM    152  HB2 PHE A 137       3.508   4.887  -4.589  1.00  0.00           H  
ATOM    153  HB3 PHE A 137       3.917   3.442  -3.861  1.00  0.00           H  
ATOM    154  HD1 PHE A 137       1.939   3.234  -4.894  1.00  0.00           H  
ATOM    155  HD2 PHE A 137       1.781   3.361  -4.926  1.00  0.00           H  
ATOM    156  HE1 PHE A 137       0.137   2.109  -6.060  1.00  0.00           H  
ATOM    157  HE2 PHE A 137      -0.020   2.235  -6.091  1.00  0.00           H  
ATOM    158  HZ  PHE A 137      -0.851   1.608  -6.654  1.00  0.00           H  
ATOM    159  N   ILE A 138       0.564   3.689  -1.755  1.00  0.00           N  
ATOM    160  CA  ILE A 138      -0.312   2.670  -1.181  1.00  0.00           C  
ATOM    161  C   ILE A 138      -1.324   2.237  -2.276  1.00  0.00           C  
ATOM    162  O   ILE A 138      -1.899   3.089  -2.916  1.00  0.00           O  
ATOM    163  CB  ILE A 138      -0.988   3.082   0.125  1.00  0.00           C  
ATOM    164  CG1 ILE A 138      -1.936   4.269   0.060  1.00  0.00           C  
ATOM    165  CG2 ILE A 138       0.084   3.318   1.187  1.00  0.00           C  
ATOM    166  CD1 ILE A 138      -3.402   3.949  -0.200  1.00  0.00           C  
ATOM    167  H   ILE A 138       0.192   4.487  -2.154  1.00  0.00           H  
ATOM    168  HA  ILE A 138       0.305   1.823  -0.931  1.00  0.00           H  
ATOM    169  HB  ILE A 138      -1.580   2.241   0.469  1.00  0.00           H  
ATOM    170 HG12 ILE A 138      -1.752   4.936   0.198  1.00  0.00           H  
ATOM    171 HG13 ILE A 138      -1.746   4.834   0.121  1.00  0.00           H  
ATOM    172 HG21 ILE A 138       0.492   3.653   1.333  1.00  0.00           H  
ATOM    173 HG22 ILE A 138       0.404   3.220   1.459  1.00  0.00           H  
ATOM    174 HG23 ILE A 138       0.209   3.256   1.625  1.00  0.00           H  
ATOM    175 HD11 ILE A 138      -3.806   3.760  -0.074  1.00  0.00           H  
ATOM    176 HD12 ILE A 138      -3.788   3.964  -0.377  1.00  0.00           H  
ATOM    177 HD13 ILE A 138      -3.788   3.884  -0.342  1.00  0.00           H  
ATOM    178  N   PRO A 139      -1.592   0.957  -2.535  1.00  0.00           N  
ATOM    179  CA  PRO A 139      -2.533   0.522  -3.574  1.00  0.00           C  
ATOM    180  C   PRO A 139      -4.031   0.664  -3.213  1.00  0.00           C  
ATOM    181  O   PRO A 139      -4.397   0.976  -2.110  1.00  0.00           O  
ATOM    182  CB  PRO A 139      -2.098  -0.897  -3.773  1.00  0.00           C  
ATOM    183  CG  PRO A 139      -1.591  -1.344  -2.445  1.00  0.00           C  
ATOM    184  CD  PRO A 139      -0.929  -0.133  -1.874  1.00  0.00           C  
ATOM    185  HA  PRO A 139      -2.345   1.070  -4.482  1.00  0.00           H  
ATOM    186  HB2 PRO A 139      -2.713  -1.455  -4.182  1.00  0.00           H  
ATOM    187  HB3 PRO A 139      -1.480  -1.020  -4.455  1.00  0.00           H  
ATOM    188  HG2 PRO A 139      -1.691  -1.966  -2.093  1.00  0.00           H  
ATOM    189  HG3 PRO A 139      -1.647  -1.860  -2.252  1.00  0.00           H  
ATOM    190  HD2 PRO A 139      -0.957  -0.098  -0.906  1.00  0.00           H  
ATOM    191  HD3 PRO A 139       0.048  -0.107  -1.977  1.00  0.00           H  
ATOM    192  N   LYS A 140      -4.890   0.411  -4.176  1.00  0.00           N  
ATOM    193  CA  LYS A 140      -6.346   0.456  -4.006  1.00  0.00           C  
ATOM    194  C   LYS A 140      -6.802  -0.760  -3.224  1.00  0.00           C  
ATOM    195  O   LYS A 140      -6.779  -1.850  -3.712  1.00  0.00           O  
ATOM    196  CB  LYS A 140      -7.000   0.545  -5.369  1.00  0.00           C  
ATOM    197  CG  LYS A 140      -7.935   1.056  -5.584  1.00  0.00           C  
ATOM    198  CD  LYS A 140      -8.577   1.104  -6.746  1.00  0.00           C  
ATOM    199  CE  LYS A 140      -9.710   1.468  -6.881  1.00  0.00           C  
ATOM    200  NZ  LYS A 140     -10.158   1.520  -7.504  1.00  0.00           N  
ATOM    201  H   LYS A 140      -4.462   0.109  -5.022  1.00  0.00           H  
ATOM    202  HA  LYS A 140      -6.606   1.358  -3.466  1.00  0.00           H  
ATOM    203  HB2 LYS A 140      -6.825   0.461  -5.916  1.00  0.00           H  
ATOM    204  HB3 LYS A 140      -6.968   0.323  -5.755  1.00  0.00           H  
ATOM    205  HG2 LYS A 140      -8.007   0.982  -5.165  1.00  0.00           H  
ATOM    206  HG3 LYS A 140      -8.085   1.500  -5.269  1.00  0.00           H  
ATOM    207  HD2 LYS A 140      -8.419   1.076  -7.172  1.00  0.00           H  
ATOM    208  HD3 LYS A 140      -8.343   0.889  -7.133  1.00  0.00           H  
ATOM    209  HE2 LYS A 140      -9.971   1.534  -6.587  1.00  0.00           H  
ATOM    210  HE3 LYS A 140      -9.984   1.645  -6.805  1.00  0.00           H  
ATOM    211  HZ1 LYS A 140     -10.409   1.558  -7.711  1.00  0.00           H  
ATOM    212  HZ2 LYS A 140     -10.173   1.393  -7.658  1.00  0.00           H  
ATOM    213  N   GLY A 141      -7.190  -0.515  -1.995  1.00  0.00           N  
ATOM    214  CA  GLY A 141      -7.522  -1.533  -1.028  1.00  0.00           C  
ATOM    215  C   GLY A 141      -6.684  -1.624   0.200  1.00  0.00           C  
ATOM    216  O   GLY A 141      -6.957  -2.446   0.978  1.00  0.00           O  
ATOM    217  H   GLY A 141      -7.025   0.428  -1.735  1.00  0.00           H  
ATOM    218  HA2 GLY A 141      -8.523  -1.362  -0.690  1.00  0.00           H  
ATOM    219  HA3 GLY A 141      -7.540  -2.481  -1.477  1.00  0.00           H  
ATOM    220  N   CYS A 142      -5.705  -0.807   0.400  1.00  0.00           N  
ATOM    221  CA  CYS A 142      -4.920  -0.767   1.584  1.00  0.00           C  
ATOM    222  C   CYS A 142      -5.599  -0.179   2.698  1.00  0.00           C  
ATOM    223  O   CYS A 142      -5.929  -0.777   3.585  1.00  0.00           O  
ATOM    224  CB  CYS A 142      -3.666  -0.162   1.310  1.00  0.00           C  
ATOM    225  SG  CYS A 142      -2.769  -0.132   2.713  1.00  0.00           S  
ATOM    226  H   CYS A 142      -5.561  -0.190  -0.346  1.00  0.00           H  
ATOM    227  HA  CYS A 142      -4.717  -1.682   1.864  1.00  0.00           H  
ATOM    228  HB2 CYS A 142      -3.193  -0.557   0.568  1.00  0.00           H  
ATOM    229  HB3 CYS A 142      -3.751   0.674   0.970  1.00  0.00           H  
ATOM    230  N   SER A 143      -5.818   0.964   2.632  1.00  0.00           N  
ATOM    231  CA  SER A 143      -6.539   1.614   3.568  1.00  0.00           C  
ATOM    232  C   SER A 143      -7.679   1.842   2.968  1.00  0.00           C  
ATOM    233  O   SER A 143      -7.821   2.644   2.387  1.00  0.00           O  
ATOM    234  CB  SER A 143      -5.922   2.682   4.045  1.00  0.00           C  
ATOM    235  OG  SER A 143      -5.631   3.115   4.097  1.00  0.00           O  
ATOM    236  H   SER A 143      -5.500   1.317   1.825  1.00  0.00           H  
ATOM    237  HA  SER A 143      -6.695   1.143   4.379  1.00  0.00           H  
ATOM    238  HB2 SER A 143      -5.971   2.836   4.362  1.00  0.00           H  
ATOM    239  HB3 SER A 143      -5.631   3.004   4.083  1.00  0.00           H  
ATOM    240  HG  SER A 143      -5.503   3.267   4.072  1.00  0.00           H  
ATOM    241  N   LYS A 144      -8.480   1.104   3.102  1.00  0.00           N  
ATOM    242  CA  LYS A 144      -9.591   1.162   2.538  1.00  0.00           C  
ATOM    243  C   LYS A 144     -10.438   1.059   3.283  1.00  0.00           C  
ATOM    244  O   LYS A 144     -10.712   0.765   3.642  1.00  0.00           O  
ATOM    245  CB  LYS A 144      -9.673   0.441   1.673  1.00  0.00           C  
ATOM    246  CG  LYS A 144      -9.937   0.249   0.723  1.00  0.00           C  
ATOM    247  CD  LYS A 144      -9.987  -0.318   0.132  1.00  0.00           C  
ATOM    248  CE  LYS A 144     -10.260  -0.523  -0.840  1.00  0.00           C  
ATOM    249  NZ  LYS A 144     -10.422  -1.053  -1.208  1.00  0.00           N  
ATOM    250  OXT LYS A 144     -10.852   1.340   3.500  1.00  0.00           O  
ATOM    251  H   LYS A 144      -8.242   0.465   3.586  1.00  0.00           H  
ATOM    252  HA  LYS A 144      -9.757   1.827   2.219  1.00  0.00           H  
ATOM    253  HB2 LYS A 144      -9.536   0.311   1.561  1.00  0.00           H  
ATOM    254  HB3 LYS A 144      -9.669   0.163   1.830  1.00  0.00           H  
ATOM    255  HG2 LYS A 144     -10.052   0.351   0.605  1.00  0.00           H  
ATOM    256  HG3 LYS A 144      -9.989   0.437   0.550  1.00  0.00           H  
ATOM    257  HD2 LYS A 144      -9.747  -0.456   0.145  1.00  0.00           H  
ATOM    258  HD3 LYS A 144     -10.049  -0.459   0.418  1.00  0.00           H  
ATOM    259  HE2 LYS A 144     -10.260  -0.337  -0.883  1.00  0.00           H  
ATOM    260  HE3 LYS A 144     -10.342  -0.454  -1.269  1.00  0.00           H  
ATOM    261  HZ1 LYS A 144     -10.521  -1.296  -1.192  1.00  0.00           H  
ATOM    262  HZ2 LYS A 144     -10.183  -1.168  -1.314  1.00  0.00           H  
ATOM    263  HXT LYS A 144     -10.893   1.149   3.463  1.00  0.00           H  
TER     264      LYS A 144                                                      
CONECT    1    2    3    7                                                      
CONECT    2    1                                                                
CONECT    3    1    4    5    6                                                 
CONECT    4    3                                                                
CONECT    5    3                                                                
CONECT    6    3                                                                
CONECT    7    1                                                                
CONECT   33  225                                                                
CONECT  225   33                                                                
MASTER      247    0    1    0    0    0    0    6  135    1    9    2          
END