Repository: marrink-lab/vermouth-martinize (language: python)

Issue:
Eunit flag Broken
Someone messed up when implementing #422. The lines below are actually non-sense because they overwrite the e-unit criterion. 

https://github.com/marrink-lab/vermouth-martinize/blob/aa53b3e3ca734032518bd56b3b8dad0831653612/bin/martinize2#L737-L741


Discussion / hints:
@pckroon I'd prefer we get rid of one of the flags either `rb_region` or `rb_unit` and for the reminaing flag we accepts either the keywords `chain`, `molecule`, `all` or a resid region
That sounds like a reasonable solution. It makes the argparse part a bit more complicated due to argument validation, but not too much I think
well the rb_region flag already takes both keywords and also resid lists at the moment
@pckroon This is actually a bit more complicated than I thought: What should happen when we have one molecule consisting of two chains and define a resid region? Should the EN be formed between the chains or not?

Fix patch:
diff --git a/bin/martinize2 b/bin/martinize2
index 8dfc7991..38361eb0 100755
--- a/bin/martinize2
+++ b/bin/martinize2
@@ -442,14 +442,11 @@ def entry():
                           type=lambda x: x.split(','), default=None,
                           help='Comma separated list of bead names for elastic bonds')
     rb_group.add_argument('-eunit', dest='rb_unit', default='molecule',
-                          choices=['chain', 'molecule', 'all'],
                           help=('Establish what is the structural unit for the '
                                 'elastic network. Bonds are only created within'
-                                ' a unit.'))
-    rb_group.add_argument('-region', dest='rb_region', default='molecule',
-                          help=('Apply rubber bands only within the specified regions. '
-                                'The format is <start_resid_1>:<end_resid_1>, <start_resid_2>:<end_resid_2>...'
-                                'Start and end resids are included'))
+                                ' a unit. Options are molecule, chain, all, or a'
+                                'specified region defined by resids, with following'
+                                'format: <start_resid_1>:<end_resid_1>, <start_resid_2>:<end_resid_2>...'))
     go_group = parser.add_argument_group('Virtual site based GoMartini')
     go_group.add_argument('-govs-includes', action='store_true', default=False,
                           help='Write include statements to use Vitrual Site Go Martini.')
@@ -731,19 +728,14 @@ def entry():
         elif args.rb_unit == 'chain':
             domain_criterion = vermouth.processors.apply_rubber_band.same_chain
         else:
-            message = 'Unknown value for -eunit: "{}".'.format(args.rb_unit)
-            LOGGER.critical(message)
-            raise ValueError(message)
-        if args.rb_region == 'molecule':
-            domain_criterion = vermouth.processors.apply_rubber_band.always_true
-        else:
-            regions = [tuple([int(i) for i in apair.split(':')]) for apair in args.rb_region.split(',')]
+            regions = [tuple([int(i) for i in apair.split(':')]) for apair in args.rb_unit.split(',')]
             if any(len(region) != 2 for region in regions):
-                message = 'Unknown value for -region: "{}".'.format(args.rb_region)
+                message = 'Faulty resid interval for elastic network unit: "{}".'.format(args.rb_unit)
                 LOGGER.critical(message)
                 raise ValueError(message)
             else:
                 domain_criterion = vermouth.processors.apply_rubber_band.make_same_region_criterion(regions)
+
         if args.rb_selection is not None:
             selector = functools.partial(
                 selectors.proto_select_attribute_in,


Test patch:
diff --git a/vermouth/tests/data/integration_tests/tier-1/EN_chain/README b/vermouth/tests/data/integration_tests/tier-1/EN_chain/README
new file mode 100644
index 00000000..279c8ca8
--- /dev/null
+++ b/vermouth/tests/data/integration_tests/tier-1/EN_chain/README
@@ -0,0 +1,11 @@
+### DETAILS: 
+
+# Human Insulin HOMRO dimer
+# 2 chains which are connected by disulphide bridge
+
+### TEST: 
+
+# the test checks -eunit flag
+# with setting chain; no EN
+# bond should be formed between
+# the two chains
diff --git a/vermouth/tests/data/integration_tests/tier-1/EN_chain/aa.pdb b/vermouth/tests/data/integration_tests/tier-1/EN_chain/aa.pdb
new file mode 100644
index 00000000..8f960de1
--- /dev/null
+++ b/vermouth/tests/data/integration_tests/tier-1/EN_chain/aa.pdb
@@ -0,0 +1,788 @@
+HEADER    HORMONE                                 01-JUL-09   3I40              
+TITLE     HUMAN INSULIN                                                         
+COMPND    MOL_ID: 1;                                                            
+COMPND   2 MOLECULE: INSULIN A CHAIN;                                           
+COMPND   3 CHAIN: A;                                                            
+COMPND   4 ENGINEERED: YES;                                                     
+COMPND   5 MOL_ID: 2;                                                           
+COMPND   6 MOLECULE: INSULIN B CHAIN;                                           
+COMPND   7 CHAIN: B;                                                            
+COMPND   8 ENGINEERED: YES                                                      
+SOURCE    MOL_ID: 1;                                                            
+SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
+SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
+SOURCE   4 ORGANISM_TAXID: 9606;                                                
+SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
+SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
+SOURCE   7 MOL_ID: 2;                                                           
+SOURCE   8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
+SOURCE   9 ORGANISM_COMMON: HUMAN;                                              
+SOURCE  10 ORGANISM_TAXID: 9606;                                                
+SOURCE  11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
+SOURCE  12 EXPRESSION_SYSTEM_TAXID: 562                                         
+KEYWDS    INSULIN, CARBOHYDRATE METABOLISM, CLEAVAGE ON PAIR OF BASIC RESIDUES, 
+KEYWDS   2 DIABETES MELLITUS, DISEASE MUTATION, DISULFIDE BOND, GLUCOSE         
+KEYWDS   3 METABOLISM, HORMONE, PHARMACEUTICAL, SECRETED                        
+EXPDTA    X-RAY DIFFRACTION                                                     
+AUTHOR    V.I.TIMOFEEV,V.V.BEZUGLOV,K.A.MIROSHNIKOV,R.N.CHUPROV-NETOCHIN,       
+AUTHOR   2 I.P.KURANOVA                                                         
+REVDAT   2   05-MAY-10 3I40    1       JRNL                                     
+REVDAT   1   05-JAN-10 3I40    0                                                
+JRNL        AUTH   V.I.TIMOFEEV,R.N.CHUPROV-NETOCHIN,V.R.SAMIGINA,              
+JRNL        AUTH 2 V.V.BEZUGLOV,K.A.MIROSHNIKOV,I.P.KURANOVA                    
+JRNL        TITL   X-RAY INVESTIGATION OF GENE-ENGINEERED HUMAN INSULIN         
+JRNL        TITL 2 CRYSTALLIZED FROM A SOLUTION CONTAINING POLYSIALIC ACID.     
+JRNL        REF    ACTA CRYSTALLOGR.,SECT.F      V.  66   259 2010              
+JRNL        REFN                   ESSN 1744-3091                               
+JRNL        PMID   20208155                                                     
+JRNL        DOI    10.1107/S1744309110000461                                    
+REMARK   2                                                                      
+REMARK   2 RESOLUTION.    1.85 ANGSTROMS.                                       
+REMARK   3                                                                      
+REMARK   3 REFINEMENT.                                                          
+REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
+REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
+REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
+REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
+REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
+REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
+REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
+REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
+REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
+REMARK   3               : ZWART                                                
+REMARK   3                                                                      
+REMARK   3    REFINEMENT TARGET : ML                                            
+REMARK   3                                                                      
+REMARK   3  DATA USED IN REFINEMENT.                                            
+REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85                           
+REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 31.52                          
+REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
+REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.1                           
+REMARK   3   NUMBER OF REFLECTIONS             : 6640                           
+REMARK   3                                                                      
+REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
+REMARK   3   R VALUE     (WORKING + TEST SET) : 0.202                           
+REMARK   3   R VALUE            (WORKING SET) : 0.200                           
+REMARK   3   FREE R VALUE                     : 0.228                           
+REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.760                           
+REMARK   3   FREE R VALUE TEST SET COUNT      : 316                             
+REMARK   3                                                                      
+REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
+REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
+REMARK   3     1 31.5295 -  2.3309    1.00     3219   154  0.1910 0.2145        
+REMARK   3     2  2.3309 -  1.8501    0.99     3105   162  0.2301 0.2627        
+REMARK   3                                                                      
+REMARK   3  BULK SOLVENT MODELLING.                                             
+REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
+REMARK   3   SOLVENT RADIUS     : 1.11                                          
+REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
+REMARK   3   K_SOL              : 0.35                                          
+REMARK   3   B_SOL              : 47.05                                         
+REMARK   3                                                                      
+REMARK   3  ERROR ESTIMATES.                                                    
+REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.240            
+REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.930           
+REMARK   3                                                                      
+REMARK   3  B VALUES.                                                           
+REMARK   3   FROM WILSON PLOT           (A**2) : 24.04                          
+REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 30.30                          
+REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
+REMARK   3    B11 (A**2) : NULL                                                 
+REMARK   3    B22 (A**2) : NULL                                                 
+REMARK   3    B33 (A**2) : NULL                                                 
+REMARK   3    B12 (A**2) : NULL                                                 
+REMARK   3    B13 (A**2) : NULL                                                 
+REMARK   3    B23 (A**2) : NULL                                                 
+REMARK   3                                                                      
+REMARK   3  TWINNING INFORMATION.                                               
+REMARK   3   FRACTION: NULL                                                     
+REMARK   3   OPERATOR: NULL                                                     
+REMARK   3                                                                      
+REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
+REMARK   3                 RMSD          COUNT                                  
+REMARK   3   BOND      :  0.005            423                                  
+REMARK   3   ANGLE     :  0.760            569                                  
+REMARK   3   CHIRALITY :  0.068             62                                  
+REMARK   3   PLANARITY :  0.002             73                                  
+REMARK   3   DIHEDRAL  : 17.205            141                                  
+REMARK   3                                                                      
+REMARK   3  TLS DETAILS                                                         
+REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
+REMARK   3                                                                      
+REMARK   3  NCS DETAILS                                                         
+REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
+REMARK   3                                                                      
+REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
+REMARK   4                                                                      
+REMARK   4 3I40 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
+REMARK 100                                                                      
+REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-JUL-09.                  
+REMARK 100 THE RCSB ID CODE IS RCSB053935.                                      
+REMARK 200                                                                      
+REMARK 200 EXPERIMENTAL DETAILS                                                 
+REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
+REMARK 200  DATE OF DATA COLLECTION        : 10-MAR-09                          
+REMARK 200  TEMPERATURE           (KELVIN) : 100                                
+REMARK 200  PH                             : NULL                               
+REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
+REMARK 200                                                                      
+REMARK 200  SYNCHROTRON              (Y/N) : N                                  
+REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
+REMARK 200  BEAMLINE                       : NULL                               
+REMARK 200  X-RAY GENERATOR MODEL          : BRUKER AXS MICROSTAR               
+REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
+REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
+REMARK 200  MONOCHROMATOR                  : NULL                               
+REMARK 200  OPTICS                         : NULL                               
+REMARK 200                                                                      
+REMARK 200  DETECTOR TYPE                  : CCD                                
+REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM                     
+REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
+REMARK 200  DATA SCALING SOFTWARE          : NULL                               
+REMARK 200                                                                      
+REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 6677                               
+REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.850                              
+REMARK 200  RESOLUTION RANGE LOW       (A) : 54.636                             
+REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
+REMARK 200                                                                      
+REMARK 200 OVERALL.                                                             
+REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
+REMARK 200  DATA REDUNDANCY                : NULL                               
+REMARK 200  R MERGE                    (I) : NULL                               
+REMARK 200  R SYM                      (I) : NULL                               
+REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
+REMARK 200                                                                      
+REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
+REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
+REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
+REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
+REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
+REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
+REMARK 200  R SYM FOR SHELL            (I) : NULL                               
+REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
+REMARK 200                                                                      
+REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
+REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
+REMARK 200 SOFTWARE USED: NULL                                                  
+REMARK 200 STARTING MODEL: PDB ENTRY 2G4M                                       
+REMARK 200                                                                      
+REMARK 200 REMARK: NULL                                                         
+REMARK 280                                                                      
+REMARK 280 CRYSTAL                                                              
+REMARK 280 SOLVENT CONTENT, VS   (%): 62.90                                     
+REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.31                     
+REMARK 280                                                                      
+REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
+REMARK 290                                                                      
+REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
+REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 21 3                           
+REMARK 290                                                                      
+REMARK 290      SYMOP   SYMMETRY                                                
+REMARK 290     NNNMMM   OPERATOR                                                
+REMARK 290       1555   X,Y,Z                                                   
+REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
+REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
+REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
+REMARK 290       5555   Z,X,Y                                                   
+REMARK 290       6555   Z+1/2,-X+1/2,-Y                                         
+REMARK 290       7555   -Z+1/2,-X,Y+1/2                                         
+REMARK 290       8555   -Z,X+1/2,-Y+1/2                                         
+REMARK 290       9555   Y,Z,X                                                   
+REMARK 290      10555   -Y,Z+1/2,-X+1/2                                         
+REMARK 290      11555   Y+1/2,-Z+1/2,-X                                         
+REMARK 290      12555   -Y+1/2,-Z,X+1/2                                         
+REMARK 290      13555   X+1/2,Y+1/2,Z+1/2                                       
+REMARK 290      14555   -X,-Y+1/2,Z                                             
+REMARK 290      15555   -X+1/2,Y,-Z                                             
+REMARK 290      16555   X,-Y,-Z+1/2                                             
+REMARK 290      17555   Z+1/2,X+1/2,Y+1/2                                       
+REMARK 290      18555   Z,-X,-Y+1/2                                             
+REMARK 290      19555   -Z,-X+1/2,Y                                             
+REMARK 290      20555   -Z+1/2,X,-Y                                             
+REMARK 290      21555   Y+1/2,Z+1/2,X+1/2                                       
+REMARK 290      22555   -Y+1/2,Z,-X                                             
+REMARK 290      23555   Y,-Z,-X+1/2                                             
+REMARK 290      24555   -Y,-Z+1/2,X                                             
+REMARK 290                                                                      
+REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
+REMARK 290           MMM -> TRANSLATION VECTOR                                  
+REMARK 290                                                                      
+REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
+REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
+REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
+REMARK 290 RELATED MOLECULES.                                                   
+REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
+REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
+REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
+REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       38.61000            
+REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
+REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       38.61000            
+REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
+REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       38.61000            
+REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       38.61000            
+REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       38.61000            
+REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       38.61000            
+REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
+REMARK 290   SMTRY1   5  0.000000  0.000000  1.000000        0.00000            
+REMARK 290   SMTRY2   5  1.000000  0.000000  0.000000        0.00000            
+REMARK 290   SMTRY3   5  0.000000  1.000000  0.000000        0.00000            
+REMARK 290   SMTRY1   6  0.000000  0.000000  1.000000       38.61000            
+REMARK 290   SMTRY2   6 -1.000000  0.000000  0.000000       38.61000            
+REMARK 290   SMTRY3   6  0.000000 -1.000000  0.000000        0.00000            
+REMARK 290   SMTRY1   7  0.000000  0.000000 -1.000000       38.61000            
+REMARK 290   SMTRY2   7 -1.000000  0.000000  0.000000        0.00000            
+REMARK 290   SMTRY3   7  0.000000  1.000000  0.000000       38.61000            
+REMARK 290   SMTRY1   8  0.000000  0.000000 -1.000000        0.00000            
+REMARK 290   SMTRY2   8  1.000000  0.000000  0.000000       38.61000            
+REMARK 290   SMTRY3   8  0.000000 -1.000000  0.000000       38.61000            
+REMARK 290   SMTRY1   9  0.000000  1.000000  0.000000        0.00000            
+REMARK 290   SMTRY2   9  0.000000  0.000000  1.000000        0.00000            
+REMARK 290   SMTRY3   9  1.000000  0.000000  0.000000        0.00000            
+REMARK 290   SMTRY1  10  0.000000 -1.000000  0.000000        0.00000            
+REMARK 290   SMTRY2  10  0.000000  0.000000  1.000000       38.61000            
+REMARK 290   SMTRY3  10 -1.000000  0.000000  0.000000       38.61000            
+REMARK 290   SMTRY1  11  0.000000  1.000000  0.000000       38.61000            
+REMARK 290   SMTRY2  11  0.000000  0.000000 -1.000000       38.61000            
+REMARK 290   SMTRY3  11 -1.000000  0.000000  0.000000        0.00000            
+REMARK 290   SMTRY1  12  0.000000 -1.000000  0.000000       38.61000            
+REMARK 290   SMTRY2  12  0.000000  0.000000 -1.000000        0.00000            
+REMARK 290   SMTRY3  12  1.000000  0.000000  0.000000       38.61000            
+REMARK 290   SMTRY1  13  1.000000  0.000000  0.000000       38.61000            
+REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       38.61000            
+REMARK 290   SMTRY3  13  0.000000  0.000000  1.000000       38.61000            
+REMARK 290   SMTRY1  14 -1.000000  0.000000  0.000000        0.00000            
+REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000       38.61000            
+REMARK 290   SMTRY3  14  0.000000  0.000000  1.000000        0.00000            
+REMARK 290   SMTRY1  15 -1.000000  0.000000  0.000000       38.61000            
+REMARK 290   SMTRY2  15  0.000000  1.000000  0.000000        0.00000            
+REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000        0.00000            
+REMARK 290   SMTRY1  16  1.000000  0.000000  0.000000        0.00000            
+REMARK 290   SMTRY2  16  0.000000 -1.000000  0.000000        0.00000            
+REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       38.61000            
+REMARK 290   SMTRY1  17  0.000000  0.000000  1.000000       38.61000            
+REMARK 290   SMTRY2  17  1.000000  0.000000  0.000000       38.61000            
+REMARK 290   SMTRY3  17  0.000000  1.000000  0.000000       38.61000            
+REMARK 290   SMTRY1  18  0.000000  0.000000  1.000000        0.00000            
+REMARK 290   SMTRY2  18 -1.000000  0.000000  0.000000        0.00000            
+REMARK 290   SMTRY3  18  0.000000 -1.000000  0.000000       38.61000            
+REMARK 290   SMTRY1  19  0.000000  0.000000 -1.000000        0.00000            
+REMARK 290   SMTRY2  19 -1.000000  0.000000  0.000000       38.61000            
+REMARK 290   SMTRY3  19  0.000000  1.000000  0.000000        0.00000            
+REMARK 290   SMTRY1  20  0.000000  0.000000 -1.000000       38.61000            
+REMARK 290   SMTRY2  20  1.000000  0.000000  0.000000        0.00000            
+REMARK 290   SMTRY3  20  0.000000 -1.000000  0.000000        0.00000            
+REMARK 290   SMTRY1  21  0.000000  1.000000  0.000000       38.61000            
+REMARK 290   SMTRY2  21  0.000000  0.000000  1.000000       38.61000            
+REMARK 290   SMTRY3  21  1.000000  0.000000  0.000000       38.61000            
+REMARK 290   SMTRY1  22  0.000000 -1.000000  0.000000       38.61000            
+REMARK 290   SMTRY2  22  0.000000  0.000000  1.000000        0.00000            
+REMARK 290   SMTRY3  22 -1.000000  0.000000  0.000000        0.00000            
+REMARK 290   SMTRY1  23  0.000000  1.000000  0.000000        0.00000            
+REMARK 290   SMTRY2  23  0.000000  0.000000 -1.000000        0.00000            
+REMARK 290   SMTRY3  23 -1.000000  0.000000  0.000000       38.61000            
+REMARK 290   SMTRY1  24  0.000000 -1.000000  0.000000        0.00000            
+REMARK 290   SMTRY2  24  0.000000  0.000000 -1.000000       38.61000            
+REMARK 290   SMTRY3  24  1.000000  0.000000  0.000000        0.00000            
+REMARK 290                                                                      
+REMARK 290 REMARK: NULL                                                         
+REMARK 300                                                                      
+REMARK 300 BIOMOLECULE: 1                                                       
+REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
+REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
+REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
+REMARK 300 BURIED SURFACE AREA.                                                 
+REMARK 350                                                                      
+REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
+REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
+REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
+REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
+REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
+REMARK 350                                                                      
+REMARK 350 BIOMOLECULE: 1                                                       
+REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
+REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
+REMARK 350 SOFTWARE USED: PISA                                                  
+REMARK 350 TOTAL BURIED SURFACE AREA: 1520 ANGSTROM**2                          
+REMARK 350 SURFACE AREA OF THE COMPLEX: 3380 ANGSTROM**2                        
+REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 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 900                                                                      
+REMARK 900 RELATED ENTRIES                                                      
+REMARK 900 RELATED ID: 3I3Z   RELATED DB: PDB                                   
+REMARK 999                                                                      
+REMARK 999 SEQUENCE                                                             
+REMARK 999 THE CONFLICT OF THE SEQUENCE MAY DUE TO ARTIFACT.                    
+DBREF  3I40 A    1    21  UNP    P01308   INS_HUMAN       90    110             
+DBREF  3I40 B    1    30  UNP    P01308   INS_HUMAN       25     54             
+SEQADV 3I40 ALA B   30  UNP  P01308    THR    54 SEE REMARK 999                 
+SEQRES   1 A   21  GLY ILE VAL GLU GLN CYS CYS THR SER ILE CYS SER LEU          
+SEQRES   2 A   21  TYR GLN LEU GLU ASN TYR CYS ASN                              
+SEQRES   1 B   30  PHE VAL ASN GLN HIS LEU CYS GLY SER HIS LEU VAL GLU          
+SEQRES   2 B   30  ALA LEU TYR LEU VAL CYS GLY GLU ARG GLY PHE PHE TYR          
+SEQRES   3 B   30  THR PRO LYS ALA                                              
+FORMUL   3  HOH   *35(H2 O)                                                     
+HELIX    1   1 GLY A    1  CYS A    7  1                                   7    
+HELIX    2   2 SER A   12  ASN A   18  1                                   7    
+HELIX    3   3 GLY B    8  GLY B   20  1                                  13    
+HELIX    4   4 GLU B   21  GLY B   23  5                                   3    
+SSBOND   1 CYS A    6    CYS A   11                          1555   1555  2.03  
+SSBOND   2 CYS A    7    CYS B    7                          1555   1555  2.04  
+SSBOND   3 CYS A   20    CYS B   19                          1555   1555  2.04  
+CRYST1   77.220   77.220   77.220  90.00  90.00  90.00 I 21 3       24          
+ORIGX1      1.000000  0.000000  0.000000        0.00000                         
+ORIGX2      0.000000  1.000000  0.000000        0.00000                         
+ORIGX3      0.000000  0.000000  1.000000        0.00000                         
+SCALE1      0.012950  0.000000  0.000000        0.00000                         
+SCALE2      0.000000  0.012950  0.000000        0.00000                         
+SCALE3      0.000000  0.000000  0.012950        0.00000                         
+ATOM      1  N   GLY A   1     -27.279   6.238 -12.314  1.00 45.01           N  
+ATOM      2  CA  GLY A   1     -26.249   6.028 -11.313  1.00 43.47           C  
+ATOM      3  C   GLY A   1     -25.582   4.677 -11.471  1.00 34.37           C  
+ATOM      4  O   GLY A   1     -25.731   4.023 -12.501  1.00 30.09           O  
+ATOM      5  N   ILE A   2     -24.853   4.248 -10.446  1.00 32.71           N  
+ATOM      6  CA  ILE A   2     -24.070   3.023 -10.550  1.00 22.60           C  
+ATOM      7  C   ILE A   2     -24.915   1.786 -10.840  1.00 23.32           C  
+ATOM      8  O   ILE A   2     -24.469   0.865 -11.529  1.00 26.36           O  
+ATOM      9  CB  ILE A   2     -23.208   2.791  -9.302  1.00 28.24           C  
+ATOM     10  CG1 ILE A   2     -22.249   1.620  -9.538  1.00 25.03           C  
+ATOM     11  CG2 ILE A   2     -24.090   2.579  -8.068  1.00 32.70           C  
+ATOM     12  CD1 ILE A   2     -21.209   1.479  -8.457  1.00 30.60           C  
+ATOM     13  N   VAL A   3     -26.137   1.755 -10.324  1.00 27.13           N  
+ATOM     14  CA  VAL A   3     -26.993   0.599 -10.563  1.00 30.10           C  
+ATOM     15  C   VAL A   3     -27.324   0.471 -12.049  1.00 32.71           C  
+ATOM     16  O   VAL A   3     -27.258  -0.617 -12.621  1.00 28.83           O  
+ATOM     17  CB  VAL A   3     -28.284   0.657  -9.740  1.00 30.51           C  
+ATOM     18  CG1 VAL A   3     -29.194  -0.497 -10.127  1.00 35.07           C  
+ATOM     19  CG2 VAL A   3     -27.956   0.613  -8.242  1.00 27.53           C  
+ATOM     20  N   GLU A   4     -27.669   1.596 -12.667  1.00 34.97           N  
+ATOM     21  CA  GLU A   4     -28.001   1.627 -14.086  1.00 31.24           C  
+ATOM     22  C   GLU A   4     -26.797   1.224 -14.927  1.00 32.52           C  
+ATOM     23  O   GLU A   4     -26.933   0.517 -15.924  1.00 31.47           O  
+ATOM     24  CB  GLU A   4     -28.474   3.027 -14.485  1.00 38.19           C  
+ATOM     25  CG  GLU A   4     -29.829   3.420 -13.908  1.00 61.51           C  
+ATOM     26  CD  GLU A   4     -29.832   3.535 -12.387  1.00 66.16           C  
+ATOM     27  OE1 GLU A   4     -28.868   4.094 -11.814  1.00 42.60           O  
+ATOM     28  OE2 GLU A   4     -30.812   3.071 -11.762  1.00 67.86           O  
+ATOM     29  N   GLN A   5     -25.615   1.664 -14.508  1.00 28.29           N  
+ATOM     30  CA  GLN A   5     -24.393   1.410 -15.266  1.00 31.01           C  
+ATOM     31  C   GLN A   5     -23.776   0.028 -15.056  1.00 39.69           C  
+ATOM     32  O   GLN A   5     -23.149  -0.511 -15.967  1.00 26.39           O  
+ATOM     33  CB  GLN A   5     -23.349   2.492 -14.974  1.00 25.23           C  
+ATOM     34  CG  GLN A   5     -23.818   3.887 -15.346  1.00 38.13           C  
+ATOM     35  CD  GLN A   5     -24.535   3.921 -16.693  1.00 53.62           C  
+ATOM     36  OE1 GLN A   5     -24.074   3.334 -17.674  1.00 38.85           O  
+ATOM     37  NE2 GLN A   5     -25.671   4.609 -16.741  1.00 42.57           N  
+ATOM     38  N   CYS A   6     -23.940  -0.551 -13.868  1.00 22.46           N  
+ATOM     39  CA  CYS A   6     -23.214  -1.776 -13.549  1.00 20.37           C  
+ATOM     40  C   CYS A   6     -24.114  -2.963 -13.225  1.00 18.21           C  
+ATOM     41  O   CYS A   6     -23.677  -4.107 -13.293  1.00 21.83           O  
+ATOM     42  CB  CYS A   6     -22.235  -1.524 -12.396  1.00 22.32           C  
+ATOM     43  SG  CYS A   6     -20.756  -0.602 -12.893  1.00 27.82           S  
+ATOM     44  N   CYS A   7     -25.359  -2.685 -12.860  1.00 22.16           N  
+ATOM     45  CA  CYS A   7     -26.307  -3.744 -12.520  1.00 21.25           C  
+ATOM     46  C   CYS A   7     -27.245  -4.032 -13.690  1.00 31.44           C  
+ATOM     47  O   CYS A   7     -27.307  -5.155 -14.190  1.00 24.09           O  
+ATOM     48  CB  CYS A   7     -27.119  -3.351 -11.286  1.00 22.97           C  
+ATOM     49  SG  CYS A   7     -28.355  -4.584 -10.791  1.00 28.27           S  
+ATOM     50  N   THR A   8     -27.967  -3.001 -14.122  1.00 29.15           N  
+ATOM     51  CA  THR A   8     -28.901  -3.121 -15.236  1.00 29.59           C  
+ATOM     52  C   THR A   8     -28.147  -3.334 -16.542  1.00 34.52           C  
+ATOM     53  O   THR A   8     -28.647  -3.986 -17.454  1.00 38.61           O  
+ATOM     54  CB  THR A   8     -29.780  -1.868 -15.371  1.00 31.24           C  
+ATOM     55  OG1 THR A   8     -30.023  -1.303 -14.080  1.00 41.12           O  
+ATOM     56  CG2 THR A   8     -31.100  -2.218 -16.029  1.00 51.07           C  
+ATOM     57  N   SER A   9     -26.948  -2.769 -16.630  1.00 26.15           N  
+ATOM     58  CA  SER A   9     -26.064  -3.019 -17.765  1.00 21.41           C  
+ATOM     59  C   SER A   9     -24.699  -3.529 -17.309  1.00 32.36           C  
+ATOM     60  O   SER A   9     -24.419  -3.594 -16.111  1.00 29.40           O  
+ATOM     61  CB  SER A   9     -25.910  -1.765 -18.626  1.00 32.53           C  
+ATOM     62  OG  SER A   9     -25.465  -0.670 -17.851  1.00 47.07           O  
+ATOM     63  N   ILE A  10     -23.849  -3.891 -18.261  1.00 24.43           N  
+ATOM     64  CA  ILE A  10     -22.562  -4.492 -17.924  1.00 24.22           C  
+ATOM     65  C   ILE A  10     -21.591  -3.454 -17.367  1.00 30.49           C  
+ATOM     66  O   ILE A  10     -21.420  -2.380 -17.934  1.00 26.28           O  
+ATOM     67  CB  ILE A  10     -21.942  -5.216 -19.128  1.00 26.99           C  
+ATOM     68  CG1 ILE A  10     -22.880  -6.328 -19.595  1.00 26.49           C  
+ATOM     69  CG2 ILE A  10     -20.577  -5.790 -18.770  1.00 25.10           C  
+ATOM     70  CD1 ILE A  10     -22.302  -7.179 -20.689  1.00 44.31           C  
+ATOM     71  N   CYS A  11     -20.972  -3.790 -16.240  1.00 28.14           N  
+ATOM     72  CA  CYS A  11     -20.088  -2.876 -15.534  1.00 25.92           C  
+ATOM     73  C   CYS A  11     -18.752  -2.779 -16.258  1.00 36.06           C  
+ATOM     74  O   CYS A  11     -18.491  -3.524 -17.204  1.00 27.25           O  
+ATOM     75  CB  CYS A  11     -19.867  -3.387 -14.106  1.00 23.76           C  
+ATOM     76  SG  CYS A  11     -19.406  -2.114 -12.908  1.00 28.09           S  
+ATOM     77  N   SER A  12     -17.902  -1.865 -15.807  1.00 25.78           N  
+ATOM     78  CA  SER A  12     -16.554  -1.767 -16.349  1.00 22.91           C  
+ATOM     79  C   SER A  12     -15.634  -1.220 -15.281  1.00 19.20           C  
+ATOM     80  O   SER A  12     -16.076  -0.508 -14.375  1.00 18.62           O  
+ATOM     81  CB  SER A  12     -16.530  -0.845 -17.559  1.00 24.50           C  
+ATOM     82  OG  SER A  12     -16.681   0.502 -17.157  1.00 24.75           O  
+ATOM     83  N   LEU A  13     -14.346  -1.528 -15.392  1.00 22.17           N  
+ATOM     84  CA  LEU A  13     -13.378  -1.013 -14.426  1.00 19.72           C  
+ATOM     85  C   LEU A  13     -13.412   0.508 -14.438  1.00 22.22           C  
+ATOM     86  O   LEU A  13     -13.329   1.158 -13.393  1.00 17.29           O  
+ATOM     87  CB  LEU A  13     -11.971  -1.517 -14.751  1.00 19.22           C  
+ATOM     88  CG  LEU A  13     -10.860  -0.998 -13.840  1.00 17.99           C  
+ATOM     89  CD1 LEU A  13     -11.104  -1.386 -12.388  1.00 18.06           C  
+ATOM     90  CD2 LEU A  13      -9.522  -1.530 -14.308  1.00 15.25           C  
+ATOM     91  N   TYR A  14     -13.550   1.075 -15.632  1.00 19.94           N  
+ATOM     92  CA  TYR A  14     -13.559   2.521 -15.774  1.00 22.72           C  
+ATOM     93  C   TYR A  14     -14.638   3.140 -14.893  1.00 22.64           C  
+ATOM     94  O   TYR A  14     -14.391   4.094 -14.152  1.00 25.33           O  
+ATOM     95  CB  TYR A  14     -13.771   2.911 -17.239  0.50 27.81           C  
+ATOM     97  CG  TYR A  14     -13.608   4.388 -17.494  0.50 28.31           C  
+ATOM     99  CD1 TYR A  14     -12.442   4.893 -18.059  0.50 23.25           C  
+ATOM    101  CD2 TYR A  14     -14.614   5.282 -17.153  0.50 28.36           C  
+ATOM    103  CE1 TYR A  14     -12.289   6.252 -18.283  0.50 27.32           C  
+ATOM    105  CE2 TYR A  14     -14.472   6.636 -17.372  0.50 29.32           C  
+ATOM    107  CZ  TYR A  14     -13.311   7.117 -17.938  0.50 29.06           C  
+ATOM    109  OH  TYR A  14     -13.179   8.469 -18.153  0.50 33.01           O  
+ATOM    111  N   GLN A  15     -15.837   2.584 -14.969  1.00 21.27           N  
+ATOM    112  CA  GLN A  15     -16.962   3.129 -14.222  1.00 21.51           C  
+ATOM    113  C   GLN A  15     -16.837   2.882 -12.722  1.00 17.30           C  
+ATOM    114  O   GLN A  15     -17.121   3.764 -11.917  1.00 20.82           O  
+ATOM    115  CB  GLN A  15     -18.275   2.561 -14.758  1.00 25.25           C  
+ATOM    116  CG  GLN A  15     -18.527   2.905 -16.214  1.00 32.75           C  
+ATOM    117  CD  GLN A  15     -19.997   3.039 -16.527  1.00 55.05           C  
+ATOM    118  OE1 GLN A  15     -20.680   3.914 -15.987  1.00 53.01           O  
+ATOM    119  NE2 GLN A  15     -20.497   2.177 -17.410  1.00 50.66           N  
+ATOM    120  N   LEU A  16     -16.399   1.687 -12.346  1.00 15.37           N  
+ATOM    121  CA  LEU A  16     -16.236   1.380 -10.930  1.00 17.02           C  
+ATOM    122  C   LEU A  16     -15.301   2.382 -10.273  1.00 16.55           C  
+ATOM    123  O   LEU A  16     -15.565   2.868  -9.172  1.00 19.70           O  
+ATOM    124  CB  LEU A  16     -15.703  -0.037 -10.742  1.00 24.64           C  
+ATOM    125  CG  LEU A  16     -16.709  -1.151 -11.013  1.00 24.23           C  
+ATOM    126  CD1 LEU A  16     -16.007  -2.496 -11.058  1.00 21.90           C  
+ATOM    127  CD2 LEU A  16     -17.786  -1.124  -9.936  1.00 18.48           C  
+ATOM    128  N   GLU A  17     -14.199   2.703 -10.950  1.00 17.86           N  
+ATOM    129  CA  GLU A  17     -13.219   3.608 -10.365  1.00 19.38           C  
+ATOM    130  C   GLU A  17     -13.763   5.026 -10.180  1.00 18.73           C  
+ATOM    131  O   GLU A  17     -13.259   5.782  -9.351  1.00 22.43           O  
+ATOM    132  CB  GLU A  17     -11.910   3.598 -11.155  1.00 20.40           C  
+ATOM    133  CG  GLU A  17     -11.090   2.343 -10.898  1.00 20.17           C  
+ATOM    134  CD  GLU A  17      -9.623   2.514 -11.240  1.00 22.14           C  
+ATOM    135  OE1 GLU A  17      -9.301   3.347 -12.110  1.00 22.42           O  
+ATOM    136  OE2 GLU A  17      -8.792   1.805 -10.640  1.00 27.73           O  
+ATOM    137  N   ASN A  18     -14.799   5.374 -10.932  1.00 20.29           N  
+ATOM    138  CA  ASN A  18     -15.480   6.657 -10.735  1.00 20.00           C  
+ATOM    139  C   ASN A  18     -16.080   6.766  -9.334  1.00 26.36           C  
+ATOM    140  O   ASN A  18     -16.469   7.849  -8.890  1.00 28.46           O  
+ATOM    141  CB  ASN A  18     -16.587   6.839 -11.774  1.00 21.66           C  
+ATOM    142  CG  ASN A  18     -16.061   7.344 -13.113  1.00 25.89           C  
+ATOM    143  OD1 ASN A  18     -15.007   7.974 -13.180  1.00 32.32           O  
+ATOM    144  ND2 ASN A  18     -16.802   7.070 -14.180  1.00 38.57           N  
+ATOM    145  N   TYR A  19     -16.163   5.640  -8.638  1.00 20.84           N  
+ATOM    146  CA  TYR A  19     -16.803   5.618  -7.327  1.00 18.56           C  
+ATOM    147  C   TYR A  19     -15.822   5.394  -6.180  1.00 23.20           C  
+ATOM    148  O   TYR A  19     -16.223   5.337  -5.018  1.00 27.54           O  
+ATOM    149  CB  TYR A  19     -17.945   4.599  -7.298  1.00 20.89           C  
+ATOM    150  CG  TYR A  19     -19.068   4.966  -8.236  1.00 21.62           C  
+ATOM    151  CD1 TYR A  19     -19.115   4.453  -9.521  1.00 23.43           C  
+ATOM    152  CD2 TYR A  19     -20.066   5.848  -7.844  1.00 26.68           C  
+ATOM    153  CE1 TYR A  19     -20.126   4.796 -10.385  1.00 24.39           C  
+ATOM    154  CE2 TYR A  19     -21.082   6.200  -8.708  1.00 31.02           C  
+ATOM    155  CZ  TYR A  19     -21.104   5.672  -9.979  1.00 28.36           C  
+ATOM    156  OH  TYR A  19     -22.114   6.009 -10.853  1.00 42.08           O  
+ATOM    157  N   CYS A  20     -14.534   5.281  -6.499  1.00 21.90           N  
+ATOM    158  CA  CYS A  20     -13.510   5.251  -5.459  1.00 19.66           C  
+ATOM    159  C   CYS A  20     -13.334   6.645  -4.882  1.00 28.69           C  
+ATOM    160  O   CYS A  20     -13.526   7.639  -5.585  1.00 30.53           O  
+ATOM    161  CB  CYS A  20     -12.169   4.783  -6.021  1.00 22.84           C  
+ATOM    162  SG  CYS A  20     -12.209   3.187  -6.829  1.00 22.45           S  
+ATOM    163  N   ASN A  21     -12.955   6.716  -3.609  1.00 26.51           N  
+ATOM    164  CA  ASN A  21     -12.630   7.993  -2.976  1.00 36.60           C  
+ATOM    165  C   ASN A  21     -11.279   8.511  -3.448  1.00 35.58           C  
+ATOM    166  O   ASN A  21     -10.515   7.790  -4.091  1.00 36.84           O  
+ATOM    167  CB  ASN A  21     -12.615   7.863  -1.450  1.00 34.89           C  
+ATOM    168  CG  ASN A  21     -13.978   7.548  -0.878  1.00 33.46           C  
+ATOM    169  OD1 ASN A  21     -14.107   6.726   0.029  1.00 48.60           O  
+ATOM    170  ND2 ASN A  21     -15.008   8.198  -1.408  1.00 39.53           N  
+ATOM    171  OXT ASN A  21     -10.922   9.659  -3.189  1.00 58.00           O  
+TER     172      ASN A  21                                                      
+ATOM    173  N   PHE B   1     -13.174  -9.740 -13.251  1.00 44.56           N  
+ATOM    174  CA  PHE B   1     -14.387  -9.892 -12.452  1.00 53.84           C  
+ATOM    175  C   PHE B   1     -15.310  -8.684 -12.590  1.00 44.51           C  
+ATOM    176  O   PHE B   1     -16.451  -8.715 -12.133  1.00 40.17           O  
+ATOM    177  CB  PHE B   1     -14.042 -10.126 -10.973  1.00 47.36           C  
+ATOM    178  CG  PHE B   1     -13.222  -9.024 -10.356  1.00 43.05           C  
+ATOM    179  CD1 PHE B   1     -13.816  -8.050  -9.571  1.00 39.13           C  
+ATOM    180  CD2 PHE B   1     -11.854  -8.964 -10.565  1.00 48.11           C  
+ATOM    181  CE1 PHE B   1     -13.059  -7.037  -9.008  1.00 29.34           C  
+ATOM    182  CE2 PHE B   1     -11.093  -7.959 -10.002  1.00 34.97           C  
+ATOM    183  CZ  PHE B   1     -11.696  -6.993  -9.224  1.00 36.24           C  
+ATOM    184  N   VAL B   2     -14.819  -7.623 -13.228  1.00 27.44           N  
+ATOM    185  CA  VAL B   2     -15.568  -6.367 -13.273  1.00 25.65           C  
+ATOM    186  C   VAL B   2     -16.402  -6.197 -14.541  1.00 30.55           C  
+ATOM    187  O   VAL B   2     -17.249  -5.306 -14.628  1.00 30.98           O  
+ATOM    188  CB  VAL B   2     -14.633  -5.163 -13.114  1.00 32.50           C  
+ATOM    189  CG1 VAL B   2     -14.056  -5.139 -11.705  1.00 29.74           C  
+ATOM    190  CG2 VAL B   2     -13.519  -5.227 -14.141  1.00 45.24           C  
+ATOM    191  N   ASN B   3     -16.158  -7.045 -15.528  1.00 28.57           N  
+ATOM    192  CA  ASN B   3     -16.844  -6.904 -16.806  1.00 31.00           C  
+ATOM    193  C   ASN B   3     -18.072  -7.800 -16.928  1.00 29.49           C  
+ATOM    194  O   ASN B   3     -18.115  -8.720 -17.743  1.00 28.57           O  
+ATOM    195  CB  ASN B   3     -15.854  -7.122 -17.946  1.00 31.67           C  
+ATOM    196  CG  ASN B   3     -14.703  -6.139 -17.888  1.00 35.45           C  
+ATOM    197  OD1 ASN B   3     -13.561  -6.507 -17.600  1.00 38.37           O  
+ATOM    198  ND2 ASN B   3     -15.009  -4.871 -18.113  1.00 23.34           N  
+ATOM    199  N   GLN B   4     -19.073  -7.514 -16.099  1.00 31.90           N  
+ATOM    200  CA  GLN B   4     -20.313  -8.287 -16.082  1.00 28.96           C  
+ATOM    201  C   GLN B   4     -21.397  -7.521 -15.328  1.00 23.12           C  
+ATOM    202  O   GLN B   4     -21.154  -6.432 -14.812  1.00 26.67           O  
+ATOM    203  CB  GLN B   4     -20.079  -9.648 -15.425  1.00 33.50           C  
+ATOM    204  CG  GLN B   4     -19.608  -9.556 -13.987  1.00 31.03           C  
+ATOM    205  CD  GLN B   4     -19.344 -10.918 -13.379  1.00 54.72           C  
+ATOM    206  OE1 GLN B   4     -20.210 -11.794 -13.390  1.00 51.79           O  
+ATOM    207  NE2 GLN B   4     -18.144 -11.105 -12.840  1.00 41.70           N  
+ATOM    208  N   HIS B   5     -22.599  -8.080 -15.281  1.00 25.17           N  
+ATOM    209  CA  HIS B   5     -23.666  -7.471 -14.503  1.00 26.87           C  
+ATOM    210  C   HIS B   5     -23.358  -7.685 -13.035  1.00 26.33           C  
+ATOM    211  O   HIS B   5     -23.193  -8.822 -12.595  1.00 25.34           O  
+ATOM    212  CB  HIS B   5     -25.013  -8.109 -14.834  1.00 24.65           C  
+ATOM    213  CG  HIS B   5     -25.462  -7.871 -16.239  1.00 27.43           C  
+ATOM    214  ND1 HIS B   5     -26.235  -6.787 -16.598  1.00 29.87           N  
+ATOM    215  CD2 HIS B   5     -25.241  -8.570 -17.377  1.00 27.84           C  
+ATOM    216  CE1 HIS B   5     -26.478  -6.833 -17.896  1.00 24.52           C  
+ATOM    217  NE2 HIS B   5     -25.885  -7.905 -18.393  1.00 35.03           N  
+ATOM    218  N   LEU B   6     -23.267  -6.592 -12.287  1.00 22.69           N  
+ATOM    219  CA  LEU B   6     -22.974  -6.660 -10.862  1.00 21.06           C  
+ATOM    220  C   LEU B   6     -24.052  -5.932 -10.079  1.00 21.50           C  
+ATOM    221  O   LEU B   6     -24.197  -4.715 -10.194  1.00 22.66           O  
+ATOM    222  CB  LEU B   6     -21.612  -6.034 -10.568  1.00 20.56           C  
+ATOM    223  CG  LEU B   6     -20.418  -6.665 -11.281  1.00 20.16           C  
+ATOM    224  CD1 LEU B   6     -19.190  -5.786 -11.103  1.00 20.54           C  
+ATOM    225  CD2 LEU B   6     -20.155  -8.064 -10.763  1.00 25.22           C  
+ATOM    226  N   CYS B   7     -24.800  -6.679  -9.273  1.00 20.58           N  
+ATOM    227  CA  CYS B   7     -25.899  -6.104  -8.513  1.00 22.46           C  
+ATOM    228  C   CYS B   7     -25.754  -6.421  -7.034  1.00 22.72           C  
+ATOM    229  O   CYS B   7     -25.231  -7.471  -6.665  1.00 21.90           O  
+ATOM    230  CB  CYS B   7     -27.236  -6.664  -9.009  1.00 28.16           C  
+ATOM    231  SG  CYS B   7     -27.554  -6.459 -10.788  1.00 29.45           S  
+ATOM    232  N   GLY B   8     -26.229  -5.514  -6.191  1.00 21.36           N  
+ATOM    233  CA  GLY B   8     -26.233  -5.745  -4.759  1.00 22.98           C  
+ATOM    234  C   GLY B   8     -24.859  -6.051  -4.209  1.00 20.91           C  
+ATOM    235  O   GLY B   8     -23.911  -5.316  -4.465  1.00 23.25           O  
+ATOM    236  N   SER B   9     -24.741  -7.136  -3.447  1.00 18.12           N  
+ATOM    237  CA  SER B   9     -23.484  -7.444  -2.778  1.00 15.90           C  
+ATOM    238  C   SER B   9     -22.360  -7.702  -3.780  1.00 18.45           C  
+ATOM    239  O   SER B   9     -21.183  -7.509  -3.473  1.00 17.21           O  
+ATOM    240  CB  SER B   9     -23.648  -8.663  -1.863  1.00 19.34           C  
+ATOM    241  OG  SER B   9     -23.919  -9.813  -2.638  1.00 20.35           O  
+ATOM    242  N   HIS B  10     -22.730  -8.151  -4.972  1.00 14.91           N  
+ATOM    243  CA  HIS B  10     -21.764  -8.403  -6.039  1.00 17.86           C  
+ATOM    244  C   HIS B  10     -21.093  -7.097  -6.470  1.00 18.59           C  
+ATOM    245  O   HIS B  10     -19.891  -7.055  -6.725  1.00 17.96           O  
+ATOM    246  CB  HIS B  10     -22.471  -9.047  -7.236  1.00 18.56           C  
+ATOM    247  CG  HIS B  10     -23.081 -10.384  -6.933  1.00 23.08           C  
+ATOM    248  ND1 HIS B  10     -23.461 -11.269  -7.919  1.00 27.72           N  
+ATOM    249  CD2 HIS B  10     -23.366 -10.990  -5.755  1.00 23.69           C  
+ATOM    250  CE1 HIS B  10     -23.951 -12.364  -7.363  1.00 29.56           C  
+ATOM    251  NE2 HIS B  10     -23.906 -12.220  -6.050  1.00 22.03           N  
+ATOM    252  N   LEU B  11     -21.886  -6.037  -6.550  1.00 16.34           N  
+ATOM    253  CA  LEU B  11     -21.398  -4.713  -6.938  1.00 16.50           C  
+ATOM    254  C   LEU B  11     -20.523  -4.120  -5.847  1.00 19.44           C  
+ATOM    255  O   LEU B  11     -19.446  -3.585  -6.105  1.00 17.25           O  
+ATOM    256  CB  LEU B  11     -22.588  -3.788  -7.211  1.00 16.97           C  
+ATOM    257  CG  LEU B  11     -22.268  -2.390  -7.735  1.00 22.79           C  
+ATOM    258  CD1 LEU B  11     -21.211  -2.486  -8.812  1.00 17.51           C  
+ATOM    259  CD2 LEU B  11     -23.529  -1.754  -8.277  1.00 22.41           C  
+ATOM    260  N   VAL B  12     -20.990  -4.218  -4.610  1.00 15.40           N  
+ATOM    261  CA  VAL B  12     -20.242  -3.690  -3.490  1.00 13.81           C  
+ATOM    262  C   VAL B  12     -18.902  -4.422  -3.332  1.00 15.23           C  
+ATOM    263  O   VAL B  12     -17.879  -3.825  -2.988  1.00 14.98           O  
+ATOM    264  CB  VAL B  12     -21.096  -3.776  -2.212  1.00 24.43           C  
+ATOM    265  CG1 VAL B  12     -20.252  -3.609  -1.029  1.00 30.29           C  
+ATOM    266  CG2 VAL B  12     -22.169  -2.694  -2.241  1.00 21.29           C  
+ATOM    267  N   GLU B  13     -18.912  -5.721  -3.589  1.00 14.50           N  
+ATOM    268  CA  GLU B  13     -17.695  -6.515  -3.515  1.00 14.19           C  
+ATOM    269  C   GLU B  13     -16.682  -6.056  -4.574  1.00 15.30           C  
+ATOM    270  O   GLU B  13     -15.481  -5.936  -4.304  1.00 16.00           O  
+ATOM    271  CB  GLU B  13     -18.046  -7.986  -3.712  1.00 22.91           C  
+ATOM    272  CG  GLU B  13     -16.884  -8.875  -4.073  1.00 31.68           C  
+ATOM    273  CD  GLU B  13     -17.296 -10.336  -4.139  1.00 35.29           C  
+ATOM    274  OE1 GLU B  13     -17.726 -10.873  -3.092  1.00 24.65           O  
+ATOM    275  OE2 GLU B  13     -17.204 -10.932  -5.236  1.00 35.79           O  
+ATOM    276  N   ALA B  14     -17.166  -5.811  -5.782  1.00 16.94           N  
+ATOM    277  CA  ALA B  14     -16.298  -5.308  -6.856  1.00 19.02           C  
+ATOM    278  C   ALA B  14     -15.701  -3.941  -6.523  1.00 17.95           C  
+ATOM    279  O   ALA B  14     -14.507  -3.704  -6.731  1.00 16.40           O  
+ATOM    280  CB  ALA B  14     -17.065  -5.240  -8.157  1.00 19.13           C  
+ATOM    281  N   LEU B  15     -16.536  -3.036  -6.021  1.00 15.53           N  
+ATOM    282  CA  LEU B  15     -16.066  -1.724  -5.592  1.00 13.58           C  
+ATOM    283  C   LEU B  15     -14.977  -1.846  -4.540  1.00 20.33           C  
+ATOM    284  O   LEU B  15     -13.957  -1.159  -4.594  1.00 17.96           O  
+ATOM    285  CB  LEU B  15     -17.228  -0.890  -5.054  1.00 17.56           C  
+ATOM    286  CG  LEU B  15     -18.132  -0.253  -6.108  1.00 19.95           C  
+ATOM    287  CD1 LEU B  15     -19.434   0.217  -5.476  1.00 19.70           C  
+ATOM    288  CD2 LEU B  15     -17.420   0.908  -6.806  1.00 19.43           C  
+ATOM    289  N   TYR B  16     -15.196  -2.733  -3.580  1.00 16.41           N  
+ATOM    290  CA  TYR B  16     -14.214  -2.982  -2.528  1.00 14.22           C  
+ATOM    291  C   TYR B  16     -12.884  -3.467  -3.093  1.00 18.76           C  
+ATOM    292  O   TYR B  16     -11.823  -2.978  -2.708  1.00 14.92           O  
+ATOM    293  CB  TYR B  16     -14.766  -4.015  -1.551  1.00 13.58           C  
+ATOM    294  CG  TYR B  16     -13.748  -4.582  -0.595  1.00 15.85           C  
+ATOM    295  CD1 TYR B  16     -13.213  -3.811   0.431  1.00 19.91           C  
+ATOM    296  CD2 TYR B  16     -13.338  -5.909  -0.707  1.00 14.31           C  
+ATOM    297  CE1 TYR B  16     -12.290  -4.347   1.318  1.00 18.93           C  
+ATOM    298  CE2 TYR B  16     -12.419  -6.445   0.163  1.00 16.89           C  
+ATOM    299  CZ  TYR B  16     -11.899  -5.665   1.173  1.00 19.03           C  
+ATOM    300  OH  TYR B  16     -10.991  -6.225   2.037  1.00 19.26           O  
+ATOM    301  N   LEU B  17     -12.941  -4.437  -4.002  1.00 17.26           N  
+ATOM    302  CA  LEU B  17     -11.725  -4.998  -4.583  1.00 17.15           C  
+ATOM    303  C   LEU B  17     -10.983  -3.979  -5.439  1.00 20.48           C  
+ATOM    304  O   LEU B  17      -9.751  -3.889  -5.407  1.00 20.37           O  
+ATOM    305  CB  LEU B  17     -12.060  -6.221  -5.428  1.00 16.44           C  
+ATOM    306  CG  LEU B  17     -12.491  -7.468  -4.651  1.00 17.44           C  
+ATOM    307  CD1 LEU B  17     -12.867  -8.590  -5.593  1.00 22.58           C  
+ATOM    308  CD2 LEU B  17     -11.383  -7.898  -3.717  1.00 22.13           C  
+ATOM    309  N   VAL B  18     -11.738  -3.226  -6.224  1.00 18.15           N  
+ATOM    310  CA  VAL B  18     -11.150  -2.270  -7.151  1.00 18.50           C  
+ATOM    311  C   VAL B  18     -10.557  -1.063  -6.431  1.00 22.53           C  
+ATOM    312  O   VAL B  18      -9.454  -0.628  -6.747  1.00 21.63           O  
+ATOM    313  CB  VAL B  18     -12.188  -1.824  -8.207  1.00 19.51           C  
+ATOM    314  CG1 VAL B  18     -11.714  -0.594  -8.955  1.00 28.07           C  
+ATOM    315  CG2 VAL B  18     -12.468  -2.973  -9.165  1.00 23.98           C  
+ATOM    316  N   CYS B  19     -11.268  -0.548  -5.433  1.00 19.45           N  
+ATOM    317  CA  CYS B  19     -10.874   0.709  -4.803  1.00 21.28           C  
+ATOM    318  C   CYS B  19      -9.819   0.588  -3.702  1.00 26.60           C  
+ATOM    319  O   CYS B  19      -9.167   1.576  -3.355  1.00 25.82           O  
+ATOM    320  CB  CYS B  19     -12.102   1.455  -4.285  1.00 20.90           C  
+ATOM    321  SG  CYS B  19     -13.231   1.932  -5.593  1.00 21.21           S  
+ATOM    322  N   GLY B  20      -9.653  -0.608  -3.150  1.00 25.20           N  
+ATOM    323  CA  GLY B  20      -8.606  -0.825  -2.167  1.00 33.63           C  
+ATOM    324  C   GLY B  20      -8.661   0.162  -1.014  1.00 39.29           C  
+ATOM    325  O   GLY B  20      -9.737   0.464  -0.501  1.00 27.87           O  
+ATOM    326  N   GLU B  21      -7.507   0.678  -0.599  1.00 30.38           N  
+ATOM    327  CA  GLU B  21      -7.474   1.534   0.591  1.00 34.13           C  
+ATOM    328  C   GLU B  21      -8.014   2.944   0.351  1.00 23.63           C  
+ATOM    329  O   GLU B  21      -8.123   3.737   1.283  1.00 35.45           O  
+ATOM    330  CB  GLU B  21      -6.075   1.569   1.220  1.00 45.91           C  
+ATOM    331  CG  GLU B  21      -5.015   2.280   0.401  1.00 57.50           C  
+ATOM    332  CD  GLU B  21      -3.631   2.179   1.034  1.00 75.22           C  
+ATOM    333  OE1 GLU B  21      -2.707   2.876   0.563  1.00 79.46           O  
+ATOM    334  OE2 GLU B  21      -3.470   1.401   2.002  1.00 57.31           O  
+ATOM    335  N   ARG B  22      -8.356   3.251  -0.897  1.00 27.41           N  
+ATOM    336  CA  ARG B  22      -9.040   4.498  -1.213  1.00 28.81           C  
+ATOM    337  C   ARG B  22     -10.456   4.461  -0.645  1.00 33.76           C  
+ATOM    338  O   ARG B  22     -11.008   5.480  -0.235  1.00 31.35           O  
+ATOM    339  CB  ARG B  22      -9.130   4.700  -2.726  1.00 30.48           C  
+ATOM    340  CG  ARG B  22      -7.876   5.228  -3.400  1.00 38.41           C  
+ATOM    341  CD  ARG B  22      -8.072   5.288  -4.922  1.00 44.34           C  
+ATOM    342  NE  ARG B  22      -8.003   3.963  -5.546  1.00 61.53           N  
+ATOM    343  CZ  ARG B  22      -8.246   3.711  -6.833  1.00 56.00           C  
+ATOM    344  NH1 ARG B  22      -8.151   2.467  -7.288  1.00 37.21           N  
+ATOM    345  NH2 ARG B  22      -8.588   4.690  -7.664  1.00 33.73           N  
+ATOM    346  N   GLY B  23     -11.048   3.276  -0.627  1.00 23.72           N  
+ATOM    347  CA  GLY B  23     -12.442   3.151  -0.243  1.00 25.22           C  
+ATOM    348  C   GLY B  23     -13.323   3.633  -1.376  1.00 26.84           C  
+ATOM    349  O   GLY B  23     -12.832   3.954  -2.460  1.00 20.71           O  
+ATOM    350  N   PHE B  24     -14.625   3.700  -1.132  1.00 18.98           N  
+ATOM    351  CA  PHE B  24     -15.558   4.055  -2.188  1.00 17.55           C  
+ATOM    352  C   PHE B  24     -16.875   4.561  -1.614  1.00 23.50           C  
+ATOM    353  O   PHE B  24     -17.092   4.530  -0.402  1.00 24.02           O  
+ATOM    354  CB  PHE B  24     -15.811   2.837  -3.086  1.00 17.36           C  
+ATOM    355  CG  PHE B  24     -16.428   1.661  -2.361  1.00 19.89           C  
+ATOM    356  CD1 PHE B  24     -15.628   0.691  -1.776  1.00 18.48           C  
+ATOM    357  CD2 PHE B  24     -17.811   1.527  -2.269  1.00 22.89           C  
+ATOM    358  CE1 PHE B  24     -16.189  -0.390  -1.107  1.00 21.90           C  
+ATOM    359  CE2 PHE B  24     -18.378   0.446  -1.597  1.00 19.48           C  
+ATOM    360  CZ  PHE B  24     -17.562  -0.513  -1.015  1.00 19.73           C  
+ATOM    361  N   PHE B  25     -17.742   5.048  -2.487  1.00 23.02           N  
+ATOM    362  CA  PHE B  25     -19.108   5.343  -2.088  1.00 26.05           C  
+ATOM    363  C   PHE B  25     -20.081   4.558  -2.948  1.00 29.87           C  
+ATOM    364  O   PHE B  25     -19.912   4.448  -4.158  1.00 25.71           O  
+ATOM    365  CB  PHE B  25     -19.410   6.848  -2.118  1.00 30.50           C  
+ATOM    366  CG  PHE B  25     -19.035   7.523  -3.399  1.00 36.46           C  
+ATOM    367  CD1 PHE B  25     -17.729   7.929  -3.625  1.00 41.85           C  
+ATOM    368  CD2 PHE B  25     -19.989   7.772  -4.374  1.00 47.50           C  
+ATOM    369  CE1 PHE B  25     -17.376   8.562  -4.808  1.00 51.84           C  
+ATOM    370  CE2 PHE B  25     -19.645   8.407  -5.560  1.00 37.96           C  
+ATOM    371  CZ  PHE B  25     -18.336   8.802  -5.778  1.00 47.77           C  
+ATOM    372  N   TYR B  26     -21.090   3.991  -2.301  1.00 26.11           N  
+ATOM    373  CA  TYR B  26     -22.087   3.184  -2.976  1.00 19.37           C  
+ATOM    374  C   TYR B  26     -23.429   3.866  -2.826  1.00 26.37           C  
+ATOM    375  O   TYR B  26     -23.966   3.954  -1.726  1.00 25.08           O  
+ATOM    376  CB  TYR B  26     -22.136   1.795  -2.350  1.00 18.99           C  
+ATOM    377  CG  TYR B  26     -23.255   0.930  -2.876  1.00 21.56           C  
+ATOM    378  CD1 TYR B  26     -24.280   0.506  -2.042  1.00 24.62           C  
+ATOM    379  CD2 TYR B  26     -23.285   0.533  -4.203  1.00 23.44           C  
+ATOM    380  CE1 TYR B  26     -25.304  -0.295  -2.516  1.00 26.30           C  
+ATOM    381  CE2 TYR B  26     -24.304  -0.265  -4.690  1.00 25.09           C  
+ATOM    382  CZ  TYR B  26     -25.313  -0.675  -3.842  1.00 27.86           C  
+ATOM    383  OH  TYR B  26     -26.328  -1.469  -4.320  1.00 29.25           O  
+ATOM    384  N   THR B  27     -23.960   4.365  -3.936  1.00 28.14           N  
+ATOM    385  CA  THR B  27     -25.185   5.147  -3.909  1.00 37.14           C  
+ATOM    386  C   THR B  27     -26.169   4.594  -4.936  1.00 32.53           C  
+ATOM    387  O   THR B  27     -26.193   5.035  -6.082  1.00 36.20           O  
+ATOM    388  CB  THR B  27     -24.889   6.637  -4.188  1.00 36.89           C  
+ATOM    389  OG1 THR B  27     -24.271   6.772  -5.473  1.00 57.47           O  
+ATOM    390  CG2 THR B  27     -23.936   7.182  -3.151  1.00 33.01           C  
+ATOM    391  N   PRO B  28     -26.989   3.620  -4.517  1.00 29.25           N  
+ATOM    392  CA  PRO B  28     -27.893   2.887  -5.411  1.00 32.94           C  
+ATOM    393  C   PRO B  28     -29.081   3.726  -5.872  1.00 32.76           C  
+ATOM    394  O   PRO B  28     -29.671   3.417  -6.908  1.00 36.05           O  
+ATOM    395  CB  PRO B  28     -28.401   1.730  -4.542  1.00 31.48           C  
+ATOM    396  CG  PRO B  28     -27.658   1.813  -3.247  1.00 28.54           C  
+ATOM    397  CD  PRO B  28     -27.128   3.190  -3.118  1.00 34.39           C  
+ATOM    398  N   LYS B  29     -29.436   4.751  -5.105  1.00 34.79           N  
+ATOM    399  CA  LYS B  29     -30.532   5.642  -5.483  1.00 49.07           C  
+ATOM    400  C   LYS B  29     -30.051   6.834  -6.309  1.00 63.70           C  
+ATOM    401  O   LYS B  29     -30.669   7.191  -7.315  1.00 73.47           O  
+ATOM    402  CB  LYS B  29     -31.305   6.122  -4.251  1.00 62.86           C  
+ATOM    403  CG  LYS B  29     -32.706   5.526  -4.105  1.00 74.15           C  
+ATOM    404  CD  LYS B  29     -32.690   4.118  -3.525  1.00 72.32           C  
+ATOM    405  CE  LYS B  29     -32.356   3.061  -4.572  1.00 68.55           C  
+ATOM    406  NZ  LYS B  29     -33.458   2.854  -5.553  1.00 59.40           N  
+ATOM    407  N   ALA B  30     -28.950   7.446  -5.884  1.00 72.05           N  
+ATOM    408  CA  ALA B  30     -28.366   8.568  -6.616  1.00 74.07           C  
+ATOM    409  C   ALA B  30     -27.782   8.115  -7.955  1.00 73.01           C  
+ATOM    410  O   ALA B  30     -27.485   8.928  -8.831  1.00 64.47           O  
+ATOM    411  CB  ALA B  30     -27.302   9.269  -5.772  1.00 56.14           C  
+ATOM    412  OXT ALA B  30     -27.594   6.921  -8.197  1.00 73.19           O  
+TER     413      ALA B  30                                                      
+HETATM  414  O   HOH A  22     -29.500  -7.696 -14.149  1.00 50.68           O  
+HETATM  415  O   HOH A  23     -11.374  10.214 -16.391  1.00 40.62           O  
+HETATM  416  O   HOH A  24     -11.187   9.560 -19.007  1.00 44.09           O  
+HETATM  417  O   HOH A  25     -22.708  -0.422 -18.245  1.00 25.03           O  
+HETATM  418  O   HOH A  26     -17.282   8.923   0.122  1.00 44.14           O  
+HETATM  419  O   HOH A  27     -27.802  -5.289 -20.151  1.00 41.02           O  
+HETATM  420  O   HOH A  28     -13.732   9.674 -11.684  1.00 48.35           O  
+HETATM  421  O   HOH A  29     -26.166   6.685 -14.912  1.00 50.84           O  
+HETATM  422  O   HOH A  30     -30.826  -5.812 -17.868  1.00 54.11           O  
+HETATM  423  O   HOH A  31     -14.803   9.989  -8.715  1.00 62.79           O  
+HETATM  424  O   HOH A  32     -19.609   9.964  -9.626  1.00 46.30           O  
+HETATM  425  O   HOH A  33     -13.690  11.749 -14.300  1.00 49.90           O  
+HETATM  426  O   HOH B  31     -24.729  10.263 -12.014  1.00 61.01           O  
+HETATM  427  O   HOH B  32     -20.724 -10.273 -19.319  1.00 52.72           O  
+HETATM  428  O   HOH B  33     -17.700 -13.422  -2.674  1.00 25.54           O  
+HETATM  429  O   HOH B  34     -28.494  10.301 -14.536  1.00 56.88           O  
+HETATM  430  O   HOH B  35     -24.545   6.027  -8.162  1.00 32.84           O  
+HETATM  431  O   HOH B  36     -27.182  -2.924  -7.024  1.00 27.65           O  
+HETATM  432  O   HOH B  37     -24.782  -9.599  -9.935  1.00 26.60           O  
+HETATM  433  O   HOH B  38     -14.505  -9.421 -15.869  1.00 44.83           O  
+HETATM  434  O   HOH B  39     -28.442  -1.829  -2.831  1.00 43.18           O  
+HETATM  435  O   HOH B  40     -12.046  -0.492  -0.930  1.00 25.29           O  
+HETATM  436  O   HOH B  41     -18.702  -9.557  -7.601  1.00 29.84           O  
+HETATM  437  O   HOH B  42      -8.200  -0.632  -9.134  1.00 32.65           O  
+HETATM  438  O   HOH B  43     -15.277 -10.853  -7.465  1.00 43.14           O  
+HETATM  439  O   HOH B  44     -22.107   4.402  -6.065  1.00 31.09           O  
+HETATM  440  O   HOH B  45      -5.206   0.010  -2.235  1.00 43.01           O  
+HETATM  441  O   HOH B  46     -26.729  -9.715  -6.146  1.00 30.80           O  
+HETATM  442  O   HOH B  47     -27.875   3.972  -9.042  1.00 40.15           O  
+HETATM  443  O   HOH B  48     -20.453  -7.642  -0.550  1.00 34.77           O  
+HETATM  444  O   HOH B  49     -17.760 -10.041  -0.552  1.00 37.12           O  
+HETATM  445  O   HOH B  50     -22.932 -10.505 -16.556  1.00 47.78           O  
+HETATM  446  O   HOH B  51     -28.195   5.830  -2.571  1.00 53.39           O  
+HETATM  447  O   HOH B  52     -17.118 -11.123 -18.586  1.00 52.94           O  
+HETATM  448  O   HOH B  53     -27.581   8.994 -11.659  1.00 53.89           O  
+CONECT   43   76                                                                
+CONECT   49  231                                                                
+CONECT   76   43                                                                
+CONECT  162  321                                                                
+CONECT  231   49                                                                
+CONECT  321  162                                                                
+MASTER      279    0    0    4    0    0    0    6  438    2    6    5          
+END                                                                             
diff --git a/vermouth/tests/data/integration_tests/tier-1/EN_chain/martinize2/cg.pdb b/vermouth/tests/data/integration_tests/tier-1/EN_chain/martinize2/cg.pdb
new file mode 100644
index 00000000..62f92b3f
--- /dev/null
+++ b/vermouth/tests/data/integration_tests/tier-1/EN_chain/martinize2/cg.pdb
@@ -0,0 +1,202 @@
+ATOM      1 BB   GLY A   1     -26.214   5.188 -11.960  1.00  0.00              
+ATOM      2 BB   ILE A   2     -24.579   2.426 -10.878  1.00  0.00              
+ATOM      3 SC1  ILE A   2     -22.689   2.117  -8.841  1.00  0.00              
+ATOM      4 BB   VAL A   3     -26.923   0.510 -11.441  1.00  0.00              
+ATOM      5 SC1  VAL A   3     -28.478   0.258  -9.370  1.00  0.00              
+ATOM      6 BB   GLU A   4     -27.331   1.201 -14.450  1.00  0.00              
+ATOM      7 SC1  GLU A   4     -29.596   3.447 -12.744  1.00  0.00              
+ATOM      8 BB   GLN A   5     -24.204   0.600 -15.231  1.00  0.00              
+ATOM      9 SC1  GLN A   5     -24.318   3.659 -16.384  1.00  0.00              
+ATOM     10 BB   CYS A   6     -23.739  -2.413 -13.484  1.00  0.00              
+ATOM     11 SC1  CYS A   6     -21.159  -0.853 -12.757  1.00  0.00              
+ATOM     12 BB   CYS A   7     -26.566  -3.952 -13.363  1.00  0.00              
+ATOM     13 SC1  CYS A   7     -28.018  -4.248 -10.926  1.00  0.00              
+ATOM     14 BB   THR A   8     -28.416  -3.394 -15.895  1.00  0.00              
+ATOM     15 SC1  THR A   8     -30.273  -1.747 -15.052  1.00  0.00              
+ATOM     16 BB   SER A   9     -25.502  -3.238 -16.879  1.00  0.00              
+ATOM     17 SC1  SER A   9     -25.656  -1.139 -18.183  1.00  0.00              
+ATOM     18 BB   ILE A  10     -22.342  -3.480 -17.891  1.00  0.00              
+ATOM     19 SC1  ILE A  10     -21.925  -6.128 -19.546  1.00  0.00              
+ATOM     20 BB   CYS A  11     -19.547  -3.283 -16.373  1.00  0.00              
+ATOM     21 SC1  CYS A  11     -19.532  -2.461 -13.235  1.00  0.00              
+ATOM     22 BB   SER A  12     -16.557  -1.298 -15.386  1.00  0.00              
+ATOM     23 SC1  SER A  12     -16.616  -0.075 -17.329  1.00  0.00              
+ATOM     24 BB   LEU A  13     -13.622  -0.165 -14.373  1.00  0.00              
+ATOM     25 SC1  LEU A  13     -10.864  -1.358 -13.822  1.00  0.00              
+ATOM     26 BB   TYR A  14     -14.043   2.750 -15.061  1.00  0.00              
+ATOM     27 SC1  TYR A  14     -13.689   3.649 -17.367  1.00  0.00              
+ATOM     28 SC2  TYR A  14     -12.366   5.572 -18.171  1.00  0.00              
+ATOM     29 SC3  TYR A  14     -14.543   5.959 -17.262  1.00  0.00              
+ATOM     30 SC4  TYR A  14     -13.236   7.890 -18.061  1.00  0.00              
+ATOM     31 BB   GLN A  15     -16.690   3.121 -13.399  1.00  0.00              
+ATOM     32 SC1  GLN A  15     -19.688   2.957 -16.205  1.00  0.00              
+ATOM     33 BB   LEU A  16     -15.872   2.123 -10.630  1.00  0.00              
+ATOM     34 SC1  LEU A  16     -16.551  -1.202 -10.687  1.00  0.00              
+ATOM     35 BB   GLU A  17     -13.606   4.333 -10.175  1.00  0.00              
+ATOM     36 SC1  GLU A  17     -10.014   2.704 -11.228  1.00  0.00              
+ATOM     37 BB   ASN A  18     -15.730   6.702  -9.928  1.00  0.00              
+ATOM     38 SC1  ASN A  18     -16.058   7.347 -13.112  1.00  0.00              
+ATOM     39 BB   TYR A  19     -16.247   5.491  -6.728  1.00  0.00              
+ATOM     40 SC1  TYR A  19     -18.506   4.783  -7.767  1.00  0.00              
+ATOM     41 SC2  TYR A  19     -19.620   4.625  -9.953  1.00  0.00              
+ATOM     42 SC3  TYR A  19     -20.574   6.024  -8.276  1.00  0.00              
+ATOM     43 SC4  TYR A  19     -21.681   5.865 -10.478  1.00  0.00              
+ATOM     44 BB   CYS A  20     -13.741   6.276  -5.638  1.00  0.00              
+ATOM     45 SC1  CYS A  20     -12.198   3.622  -6.609  1.00  0.00              
+ATOM     46 BB   ASN A  21     -11.590   8.161  -3.487  1.00  0.00              
+ATOM     47 SC1  ASN A  21     -13.980   7.543  -0.874  1.00  0.00              
+ATOM     48 BB   PHE B  22     -14.889  -9.235 -12.595  1.00  0.00              
+ATOM     49 SC1  PHE B  22     -13.433  -9.308 -10.515  1.00  0.00              
+ATOM     50 SC2  PHE B  22     -12.977  -7.339  -9.231  1.00  0.00              
+ATOM     51 SC3  PHE B  22     -11.466  -8.045  -9.996  1.00  0.00              
+ATOM     52 BB   VAL B  23     -16.057  -6.340 -13.945  1.00  0.00              
+ATOM     53 SC1  VAL B  23     -14.069  -5.176 -12.987  1.00  0.00              
+ATOM     54 BB   ASN B  24     -17.316  -7.678 -16.779  1.00  0.00              
+ATOM     55 SC1  ASN B  24     -14.700  -6.138 -17.874  1.00  0.00              
+ATOM     56 BB   GLN B  25     -20.482  -7.367 -15.543  1.00  0.00              
+ATOM     57 SC1  GLN B  25     -19.481 -10.691 -13.750  1.00  0.00              
+ATOM     58 BB   HIS B  26     -23.181  -8.077 -13.813  1.00  0.00              
+ATOM     59 SC1  HIS B  26     -25.237  -7.990 -15.537  1.00  0.00              
+ATOM     60 SC2  HIS B  26     -25.588  -8.212 -17.924  1.00  0.00              
+ATOM     61 SC3  HIS B  26     -26.347  -6.808 -17.197  1.00  0.00              
+ATOM     62 BB   LEU B  27     -23.652  -5.904 -10.860  1.00  0.00              
+ATOM     63 SC1  LEU B  27     -20.344  -6.637 -10.929  1.00  0.00              
+ATOM     64 BB   CYS B  28     -25.384  -6.729  -7.834  1.00  0.00              
+ATOM     65 SC1  CYS B  28     -27.467  -6.515 -10.303  1.00  0.00              
+ATOM     66 BB   GLY B  29     -25.239  -5.626  -4.921  1.00  0.00              
+ATOM     67 BB   SER B  30     -22.878  -7.441  -3.380  1.00  0.00              
+ATOM     68 SC1  SER B  30     -23.803  -9.320  -2.306  1.00  0.00              
+ATOM     69 BB   HIS B  31     -21.310  -7.648  -6.061  1.00  0.00              
+ATOM     70 SC1  HIS B  31     -22.776  -9.716  -7.085  1.00  0.00              
+ATOM     71 SC2  HIS B  31     -23.657 -11.652  -5.914  1.00  0.00              
+ATOM     72 SC3  HIS B  31     -23.687 -11.774  -7.662  1.00  0.00              
+ATOM     73 BB   LEU B  32     -20.752  -4.590  -6.348  1.00  0.00              
+ATOM     74 SC1  LEU B  32     -22.399  -2.605  -8.009  1.00  0.00              
+ATOM     75 BB   VAL B  33     -19.438  -4.030  -3.597  1.00  0.00              
+ATOM     76 SC1  VAL B  33     -21.172  -3.360  -1.827  1.00  0.00              
+ATOM     77 BB   GLU B  34     -17.129  -6.036  -4.003  1.00  0.00              
+ATOM     78 SC1  GLU B  34     -17.435  -9.930  -4.064  1.00  0.00              
+ATOM     79 BB   ALA B  35     -15.860  -4.659  -6.467  1.00  0.00              
+ATOM     80 SC1  ALA B  35     -17.065  -5.240  -8.157  1.00  0.00              
+ATOM     81 BB   LEU B  36     -15.321  -1.924  -5.174  1.00  0.00              
+ATOM     82 SC1  LEU B  36     -18.053  -0.004  -5.861  1.00  0.00              
+ATOM     83 BB   TYR B  37     -13.465  -3.024  -2.980  1.00  0.00              
+ATOM     84 SC1  TYR B  37     -14.257  -4.298  -1.073  1.00  0.00              
+ATOM     85 SC2  TYR B  37     -12.751  -4.079   0.874  1.00  0.00              
+ATOM     86 SC3  TYR B  37     -12.878  -6.177  -0.272  1.00  0.00              
+ATOM     87 SC4  TYR B  37     -11.380  -5.985   1.667  1.00  0.00              
+ATOM     88 BB   LEU B  38     -11.290  -4.298  -4.867  1.00  0.00              
+ATOM     89 SC1  LEU B  38     -12.200  -7.544  -4.847  1.00  0.00              
+ATOM     90 BB   VAL B  39     -10.668  -1.763  -6.631  1.00  0.00              
+ATOM     91 SC1  VAL B  39     -12.123  -1.797  -8.776  1.00  0.00              
+ATOM     92 BB   CYS B  40     -10.236   0.613  -4.293  1.00  0.00              
+ATOM     93 SC1  CYS B  40     -12.923   1.802  -5.236  1.00  0.00              
+ATOM     94 BB   GLY B  41      -9.225  -0.167  -1.672  1.00  0.00              
+ATOM     95 BB   GLU B  42      -7.795   2.278   0.434  1.00  0.00              
+ATOM     96 SC1  GLU B  42      -4.051   2.070   1.072  1.00  0.00              
+ATOM     97 BB   ARG B  43      -9.760   4.457  -0.715  1.00  0.00              
+ATOM     98 SC1  ARG B  43      -8.359   5.072  -3.683  1.00  0.00              
+ATOM     99 SC2  ARG B  43      -8.247   3.708  -6.833  1.00  0.00              
+ATOM    100 BB   GLY B  44     -12.392   3.528  -1.251  1.00  0.00              
+ATOM    101 BB   PHE B  45     -16.063   4.216  -1.257  1.00  0.00              
+ATOM    102 SC1  PHE B  45     -16.270   1.964  -2.548  1.00  0.00              
+ATOM    103 SC2  PHE B  45     -16.333  -0.086  -1.292  1.00  0.00              
+ATOM    104 SC3  PHE B  45     -18.015   0.557  -1.669  1.00  0.00              
+ATOM    105 BB   PHE B  46     -19.208   4.827  -2.996  1.00  0.00              
+ATOM    106 SC1  PHE B  46     -19.132   7.352  -3.069  1.00  0.00              
+ATOM    107 SC2  PHE B  46     -17.706   8.423  -4.668  1.00  0.00              
+ATOM    108 SC3  PHE B  46     -19.449   8.303  -5.245  1.00  0.00              
+ATOM    109 BB   TYR B  47     -22.683   3.773  -2.397  1.00  0.00              
+ATOM    110 SC1  TYR B  47     -22.696   1.363  -2.613  1.00  0.00              
+ATOM    111 SC2  TYR B  47     -24.792   0.105  -2.279  1.00  0.00              
+ATOM    112 SC3  TYR B  47     -23.794   0.134  -4.447  1.00  0.00              
+ATOM    113 SC4  TYR B  47     -25.893  -1.129  -4.115  1.00  0.00              
+ATOM    114 BB   THR B  48     -25.385   4.788  -4.788  1.00  0.00              
+ATOM    115 SC1  THR B  48     -24.356   6.854  -4.391  1.00  0.00              
+ATOM    116 BB   PRO B  49     -28.449   3.421  -5.725  1.00  0.00              
+ATOM    117 SC1  PRO B  49     -27.729   2.244  -3.636  1.00  0.00              
+ATOM    118 BB   LYS B  50     -30.182   6.135  -6.111  1.00  0.00              
+ATOM    119 SC1  LYS B  50     -32.234   5.255  -3.960  1.00  0.00              
+ATOM    120 SC2  LYS B  50     -32.949   2.950  -5.100  1.00  0.00              
+ATOM    121 BB   ALA B  51     -28.005   7.972  -7.567  1.00  0.00              
+ATOM    122 SC1  ALA B  51     -27.302   9.269  -5.772  1.00  0.00              
+TER     123      ALA B  51 
+CONECT    1    2
+CONECT    2    3    4
+CONECT    4    5    6
+CONECT    6    7    8
+CONECT    8    9   10
+CONECT   10   11   12
+CONECT   11   21
+CONECT   12   13   14
+CONECT   13   16   65
+CONECT   14   15   16
+CONECT   16   17   18
+CONECT   18   19   20
+CONECT   20   21   22
+CONECT   22   23   24
+CONECT   24   25   26
+CONECT   26   27   31
+CONECT   27   28   29
+CONECT   28   29   30
+CONECT   29   30
+CONECT   31   32   33
+CONECT   33   34   35
+CONECT   35   36   37
+CONECT   37   38   39
+CONECT   39   40   44
+CONECT   40   41   42
+CONECT   41   42   43
+CONECT   42   43
+CONECT   44   45   46
+CONECT   45   93
+CONECT   46   47
+CONECT   48   49   52
+CONECT   49   50   51
+CONECT   50   51
+CONECT   52   53   54
+CONECT   54   55   56
+CONECT   56   57   58
+CONECT   58   59   62
+CONECT   59   60   61
+CONECT   60   61
+CONECT   62   63   64
+CONECT   64   65   66
+CONECT   66   67
+CONECT   67   68   69
+CONECT   69   70   73
+CONECT   70   71   72
+CONECT   71   72
+CONECT   73   74   75
+CONECT   75   76   77
+CONECT   77   78   79
+CONECT   79   80   81
+CONECT   81   82   83
+CONECT   83   84   88
+CONECT   84   85   86
+CONECT   85   86   87
+CONECT   86   87
+CONECT   88   89   90
+CONECT   90   91   92
+CONECT   92   93   94
+CONECT   94   95
+CONECT   95   96   97
+CONECT   97   98  100
+CONECT   98   99
+CONECT  100  101
+CONECT  101  102  105
+CONECT  102  103  104
+CONECT  103  104
+CONECT  105  106  109
+CONECT  106  107  108
+CONECT  107  108
+CONECT  109  110  114
+CONECT  110  111  112
+CONECT  111  112  113
+CONECT  112  113
+CONECT  114  115  116
+CONECT  116  117  118
+CONECT  118  119  121
+CONECT  119  120
+CONECT  121  122
+END   
\ No newline at end of file
diff --git a/vermouth/tests/data/integration_tests/tier-1/EN_chain/martinize2/cg.top b/vermouth/tests/data/integration_tests/tier-1/EN_chain/martinize2/cg.top
new file mode 100644
index 00000000..a45ed27a
--- /dev/null
+++ b/vermouth/tests/data/integration_tests/tier-1/EN_chain/martinize2/cg.top
@@ -0,0 +1,9 @@
+
+#include "martini.itp"
+#include "molecule_0.itp"
+
+[ system ]
+Title of the system
+
+[ molecules ]
+molecule_0    1
diff --git a/vermouth/tests/data/integration_tests/tier-1/EN_chain/martinize2/chain_A.ssd b/vermouth/tests/data/integration_tests/tier-1/EN_chain/martinize2/chain_A.ssd
new file mode 100644
index 00000000..23c89214
--- /dev/null
+++ b/vermouth/tests/data/integration_tests/tier-1/EN_chain/martinize2/chain_A.ssd
@@ -0,0 +1,80 @@
+==== Secondary Structure Definition by the program DSSP, CMBI version 2.0                          ==== DATE=2022-09-07        .
+REFERENCE W. KABSCH AND C.SANDER, BIOPOLYMERS 22 (1983) 2577-2637                                                              .
+                                                                                                                               .
+COMPND                                                                                                                         .
+SOURCE                                                                                                                         .
+AUTHOR                                                                                                                         .
+   51  2  0  0  0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN)                .
+  3437.6   ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2)                                                                         .
+   31 60.8   TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(J)  , SAME NUMBER PER 100 RESIDUES                              .
+    0  0.0   TOTAL NUMBER OF HYDROGEN BONDS IN     PARALLEL BRIDGES, SAME NUMBER PER 100 RESIDUES                              .
+    2  3.9   TOTAL NUMBER OF HYDROGEN BONDS IN ANTIPARALLEL BRIDGES, SAME NUMBER PER 100 RESIDUES                              .
+    0  0.0   TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-5), SAME NUMBER PER 100 RESIDUES                              .
+    0  0.0   TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-4), SAME NUMBER PER 100 RESIDUES                              .
+    0  0.0   TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-3), SAME NUMBER PER 100 RESIDUES                              .
+    0  0.0   TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-2), SAME NUMBER PER 100 RESIDUES                              .
+    0  0.0   TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-1), SAME NUMBER PER 100 RESIDUES                              .
+    0  0.0   TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+0), SAME NUMBER PER 100 RESIDUES                              .
+    0  0.0   TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+1), SAME NUMBER PER 100 RESIDUES                              .
+    2  3.9   TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES                              .
+    7 13.7   TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+3), SAME NUMBER PER 100 RESIDUES                              .
+   15 29.4   TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+4), SAME NUMBER PER 100 RESIDUES                              .
+    3  5.9   TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+5), SAME NUMBER PER 100 RESIDUES                              .
+  1  2  3  4  5  6  7  8  9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30     *** HISTOGRAMS OF ***           .
+  1  0  0  0  1  0  0  0  0  0  1  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0    RESIDUES PER ALPHA HELIX         .
+  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0    PARALLEL BRIDGES PER LADDER      .
+  1  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0    ANTIPARALLEL BRIDGES PER LADDER  .
+  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0    LADDERS PER SHEET                .
+  #  RESIDUE AA STRUCTURE BP1 BP2  ACC     N-H-->O    O-->H-N    N-H-->O    O-->H-N    TCO  KAPPA ALPHA  PHI   PSI    X-CA   Y-CA   Z-CA            CHAIN
+    1    1 A G     >        0   0   36      0, 0.0     4,-2.0     0, 0.0     3,-0.3   0.000 360.0 360.0 360.0-165.0  -26.2    6.0  -11.3               
+    2    2 A I  H  >> +     0   0    0     47,-0.5     4,-2.7     1,-0.2     5,-0.5   0.821 360.0  56.2 -60.2 -33.2  -24.1    3.0  -10.6               
+    3    3 A V  I  >>S+     0   0   31     46,-0.3     5,-2.6     2,-0.2     4,-2.1   0.939 109.2  46.0 -64.4 -44.8  -27.0    0.6  -10.6               
+    4    4 A E  I  45S+     0   0   90     -3,-0.3     5,-0.4     3,-0.2    -2,-0.2   0.879 119.7  41.8 -63.1 -38.5  -28.0    1.6  -14.1               
+    5    5 A Q  I  <5S+     0   0   75     -4,-2.0    -2,-0.2     3,-0.1    -1,-0.2   0.796 131.4  18.3 -81.2 -30.8  -24.4    1.4  -15.3               
+    6    6 A C  I  <>S+     0   0    0     -4,-2.7    22,-3.5    -5,-0.2     5,-0.6   0.631 131.0  34.7-120.2 -20.4  -23.2   -1.8  -13.5               
+    7    7 A C  I  <<S+     0   0   29     -4,-2.1    -3,-0.2    -5,-0.5    22,-0.1   0.856 124.8  34.5-100.1 -58.4  -26.3   -3.7  -12.5               
+    8    8 A T  T   <S+     0   0  101     -5,-2.6     2,-0.2    20,-0.1    -4,-0.2   0.807 134.0  25.5 -69.0 -31.3  -28.9   -3.1  -15.2               
+    9    9 A S  T   5S-     0   0   45     -6,-0.5    19,-0.4    -5,-0.4     2,-0.2  -0.787 107.5 -71.2-124.9 174.8  -26.1   -3.0  -17.8               
+   10   10 A I  T   5 -     0   0   99     -2,-0.2    17,-0.2    17,-0.1    -3,-0.1  -0.464  50.8-134.1 -73.5 131.2  -22.6   -4.5  -17.9               
+   11   11 A C      < -     0   0    3     15,-2.2     2,-0.3    -5,-0.6    -5,-0.1  -0.145  17.8-159.7 -75.8 172.7  -20.1   -2.9  -15.5               
+   12   12 A S     >  -     0   0   30     13,-0.1     4,-2.5     1,-0.1     5,-0.2  -0.988  31.0-118.9-151.3 155.1  -16.6   -1.8  -16.3               
+   13   13 A L  H  > S+     0   0   80     -2,-0.3     4,-2.4     1,-0.2     5,-0.2   0.902 114.6  59.2 -58.9 -39.3  -13.4   -1.0  -14.4               
+   14   14 A Y  H  > S+     0   0  180      1,-0.2     4,-0.7     2,-0.2    -1,-0.2   0.930 109.9  40.7 -55.7 -48.2  -13.6    2.5  -15.8               
+   15   15 A Q  H >4 S+     0   0   49      1,-0.2     3,-0.8     2,-0.2     4,-0.3   0.904 111.1  55.7 -71.0 -41.5  -17.0    3.1  -14.2               
+   16   16 A L  H >< S+     0   0    0     -4,-2.5     3,-2.2     1,-0.3     4,-0.2   0.919 103.6  55.6 -56.8 -43.4  -16.2    1.4  -10.9               
+   17   17 A E  H >< S+     0   0   86     -4,-2.4     3,-1.4     1,-0.3    -1,-0.3   0.757  91.5  72.1 -65.9 -21.8  -13.2    3.6  -10.4               
+   18   18 A N  T << S+     0   0   95     -3,-0.8    -1,-0.3    -4,-0.7    -2,-0.2   0.653  99.1  50.7 -61.1 -14.1  -15.5    6.7  -10.7               
+   19   19 A Y  T <  S+     0   0   36     -3,-2.2    28,-2.2    -4,-0.3    -1,-0.2   0.402  84.7 105.4-110.5   1.5  -16.8    5.6   -7.3               
+   20   20 A C  B <    A   46   0A  14     -3,-1.4    26,-0.3    26,-0.2    25,-0.1  -0.525 360.0 360.0 -73.8 150.2  -13.5    5.3   -5.5               
+   21   21 A N              0   0  140     24,-1.9    -1,-0.1    -2,-0.2    24,-0.1  -0.271 360.0 360.0 -74.3 360.0  -12.6    8.0   -3.0               
+   22        !*             0   0    0      0, 0.0     0, 0.0     0, 0.0     0, 0.0   0.000 360.0 360.0 360.0 360.0    0.0    0.0    0.0
+   23    1 B F              0   0  138      0, 0.0     3,-0.1     0, 0.0    13,-0.1   0.000 360.0 360.0 360.0  -9.3  -14.4   -9.9  -12.5               
+   24    2 B V        +     0   0   12      1,-0.2     2,-1.2    12,-0.1     4,-0.1   0.593 360.0  82.5 -95.9 -12.4  -15.6   -6.4  -13.3               
+   25    3 B N  S    S+     0   0  117    -13,-0.1     2,-0.3   -15,-0.1    -1,-0.2  -0.470  83.1  62.7 -96.5  65.8  -16.8   -6.9  -16.8               
+   26    4 B Q  S    S-     0   0   99     -2,-1.2   -15,-2.2    -3,-0.1     2,-0.5  -0.948  98.4 -59.1-164.7 177.2  -20.3   -8.3  -16.1               
+   27    5 B H        -     0   0  104     -2,-0.3     2,-0.5   -17,-0.2   -20,-0.2  -0.642  53.2-173.4 -72.4 122.5  -23.7   -7.5  -14.5               
+   28    6 B L        +     0   0    8    -22,-3.5     2,-0.3    -2,-0.5   -19,-0.1  -0.963   8.1 169.9-124.9 115.0  -23.0   -6.7  -10.9               
+   29    7 B C    >   -     0   0   54     -2,-0.5     3,-1.8   -22,-0.1     4,-0.2  -0.922  49.3 -26.0-126.0 148.7  -25.9   -6.1   -8.5               
+   30    8 B G  T >> S+     0   0   38     -2,-0.3     4,-2.1     1,-0.3     3,-0.7  -0.246 131.6   3.5  56.5-129.1  -26.2   -5.7   -4.8               
+   31    9 B S  H 3> S+     0   0   90      1,-0.3     4,-2.2     2,-0.2    -1,-0.3   0.781 130.9  60.9 -63.1 -26.7  -23.5   -7.4   -2.8               
+   32   10 B H  H <> S+     0   0  114     -3,-1.8     4,-1.7     2,-0.2    -1,-0.3   0.888 107.5  44.5 -64.4 -40.5  -21.8   -8.4   -6.0               
+   33   11 B L  H <> S+     0   0    1     -3,-0.7     4,-2.5    -4,-0.2    -2,-0.2   0.914 113.3  49.1 -70.2 -45.7  -21.4   -4.7   -6.9               
+   34   12 B V  H  X S+     0   0   50     -4,-2.1     4,-2.3     1,-0.2    -2,-0.2   0.878 109.7  53.0 -63.4 -37.0  -20.2   -3.7   -3.5               
+   35   13 B E  H  X S+     0   0  122     -4,-2.2     4,-2.4    -5,-0.2    -1,-0.2   0.913 109.4  48.6 -64.2 -43.3  -17.7   -6.5   -3.5               
+   36   14 B A  H  X S+     0   0    2     -4,-1.7     4,-2.8     2,-0.2     5,-0.3   0.921 110.4  50.7 -62.2 -45.4  -16.3   -5.3   -6.9               
+   37   15 B L  H  X S+     0   0    0     -4,-2.5     4,-2.7     1,-0.2     5,-0.2   0.916 110.7  50.3 -57.1 -44.2  -16.1   -1.7   -5.6               
+   38   16 B Y  H  X S+     0   0  156     -4,-2.3     4,-1.4     1,-0.2    -2,-0.2   0.923 113.6  43.9 -59.9 -47.1  -14.2   -3.0   -2.5               
+   39   17 B L  H  < S+     0   0   92     -4,-2.4    -2,-0.2     1,-0.2    -1,-0.2   0.897 118.5  43.5 -66.5 -42.1  -11.7   -5.0   -4.6               
+   40   18 B V  H  < S+     0   0   20     -4,-2.8    -2,-0.2    -5,-0.2    -1,-0.2   0.915 116.1  44.6 -71.8 -42.4  -11.2   -2.3   -7.2               
+   41   19 B C  H >< S+     0   0    3     -4,-2.7     3,-1.9    -5,-0.3     4,-0.4   0.687  80.0 175.3 -84.1 -19.4  -10.9    0.7   -4.8               
+   42   20 B G  G ><  -     0   0   44     -4,-1.4     3,-1.4     1,-0.3    -1,-0.2  -0.148  68.8  -7.1  53.5-137.1   -8.6   -0.8   -2.2               
+   43   21 B E  G 3  S+     0   0  206      1,-0.3    -1,-0.3     2,-0.0    -2,-0.1   0.553 126.1  72.4 -75.5  -4.4   -7.5    1.5    0.6               
+   44   22 B R  G <  S-     0   0  120     -3,-1.9    -1,-0.3     1,-0.1    -2,-0.2   0.828  90.7-156.9 -68.8 -33.4   -9.0    4.5   -1.2               
+   45   23 B G    <   -     0   0   24     -3,-1.4   -24,-1.9    -4,-0.4     2,-0.3  -0.256   5.7-129.0  75.4-173.9  -12.4    3.2   -0.2               
+   46   24 B F  B     -A   20   0A  58    -26,-0.3     2,-0.4    -3,-0.1   -26,-0.2  -0.942   4.0-113.2-159.3 172.9  -15.6    4.1   -2.2               
+   47   25 B F        -     0   0   91    -28,-2.2     2,-0.6    -2,-0.3    -2,-0.0  -0.993  19.4-159.4-122.1 136.5  -19.1    5.3   -2.1               
+   48   26 B Y        +     0   0   80     -2,-0.4    -2,-0.0   -46,-0.0   -14,-0.0  -0.951  16.5 169.2-116.9 111.8  -22.1    3.2   -3.0               
+   49   27 B T        +     0   0   46     -2,-0.6   -47,-0.5     1,-0.1   -46,-0.3  -0.802   6.9 172.6-129.3  88.6  -25.2    5.1   -3.9               
+   50   28 B P  S    S+     0   0   46      0, 0.0   -47,-0.1     0, 0.0    -1,-0.1   0.704  83.8  40.4 -72.5 -23.6  -27.9    2.9   -5.4               
+   51   29 B K              0   0  188      1,-0.1    -2,-0.1   -48,-0.1     0, 0.0   0.853 360.0 360.0 -90.6 -44.3  -30.5    5.6   -5.5               
+   52   30 B A              0   0   95    -51,-0.0    -1,-0.1   -49,-0.0    -3,-0.0   0.650 360.0 360.0 -68.5 360.0  -28.4    8.6   -6.6               
diff --git a/vermouth/tests/data/integration_tests/tier-1/EN_chain/martinize2/citation b/vermouth/tests/data/integration_tests/tier-1/EN_chain/martinize2/citation
new file mode 100644
index 00000000..ddb39213
--- /dev/null
+++ b/vermouth/tests/data/integration_tests/tier-1/EN_chain/martinize2/citation
@@ -0,0 +1,1 @@
+Souza, P C T; Alessandri, R; Barnoud, J; Thallmair, S; Faustino, I; Grünewald, F; Patmanidis, I; Abdizadeh, H; Bruininks, B M H; Wassenaar, T A; Kroon, P C; Melcr, J; Nieto, V; Corradi, V; Khan, H M; Domański, J; Javanainen, M; Martinez-Seara, H; Reuter, N; Best, R B; Vattulainen, I; Monticelli, L; Periole, X; Tieleman, D P; de Vries, A H; Marrink, S J;  Nature Methods 2021; 10.1038/s41592-021-01098-3
diff --git a/vermouth/tests/data/integration_tests/tier-1/EN_chain/martinize2/command b/vermouth/tests/data/integration_tests/tier-1/EN_chain/martinize2/command
new file mode 100644
index 00000000..a0cada1d
--- /dev/null
+++ b/vermouth/tests/data/integration_tests/tier-1/EN_chain/martinize2/command
@@ -0,0 +1,1 @@
+martinize2 -f ../aa.pdb -o cg.top -x cg.pdb -dssp dssp -p backbone -ff martini3001 -scfix -cys auto -ignore HOH -elastic -eunit chain
diff --git a/vermouth/tests/data/integration_tests/tier-1/EN_chain/martinize2/molecule_0.itp b/vermouth/tests/data/integration_tests/tier-1/EN_chain/martinize2/molecule_0.itp
new file mode 100644
index 00000000..d7975234
--- /dev/null
+++ b/vermouth/tests/data/integration_tests/tier-1/EN_chain/martinize2/molecule_0.itp
@@ -0,0 +1,825 @@
+; This file was generated using the following command:
+; /coarse/fabian/current-projects/polymer_itp_builder/vermouth_dev/venv_py38/bin/martinize2 -f ../aa.pdb -o cg.top -x cg.pdb -dssp dssp -p backbone -ff martini3001 -scfix -cys auto -ignore HOH -elastic -eunit chain
+; martinize with vermouth 0.7.3.dev30
+; The following sequence of secondary structure 
+; was used for the full system:
+; CHIIIIITTTCCHHHHHTTBCCCSSCCCTHHHHHHHHHHHGGGCBCCCSCC
+
+; Pleas cite the following papers:
+; Souza, P C T; Alessandri, R; Barnoud, J; Thallmair, S; Faustino, I; Grünewald, F; Patmanidis, I; Abdizadeh, H; Bruininks, B M H; Wassenaar, T A; Kroon, P C; Melcr, J; Nieto, V; Corradi, V; Khan, H M; Domański, J; Javanainen, M; Martinez-Seara, H; Reuter, N; Best, R B; Vattulainen, I; Monticelli, L; Periole, X; Tieleman, D P; de Vries, A H; Marrink, S J;  Nature Methods 2021; 10.1038/s41592-021-01098-3
+
+[ moleculetype ]
+molecule_0 1
+
+[ atoms ]
+  1 Q5    1 GLY BB    1    1 
+  2 P2    2 ILE BB    2  0.0 
+  3 SC2   2 ILE SC1   3  0.0 
+  4 SP2   3 VAL BB    4  0.0 
+  5 SC3   3 VAL SC1   5  0.0 
+  6 P2    4 GLU BB    6  0.0 
+  7 Q5n   4 GLU SC1   7 -1.0 
+  8 P2    5 GLN BB    8  0.0 
+  9 P5    5 GLN SC1   9  0.0 
+ 10 P2    6 CYS BB   10  0.0 
+ 11 TC6   6 CYS SC1  11  0.0 
+ 12 P2    7 CYS BB   12  0.0 
+ 13 TC6   7 CYS SC1  13  0.0 
+ 14 P2    8 THR BB   14  0.0 
+ 15 SP1   8 THR SC1  15  0.0 
+ 16 P2    9 SER BB   16  0.0 
+ 17 TP1   9 SER SC1  17  0.0 
+ 18 P2   10 ILE BB   18  0.0 
+ 19 SC2  10 ILE SC1  19  0.0 
+ 20 P2   11 CYS BB   20  0.0 
+ 21 TC6  11 CYS SC1  21  0.0 
+ 22 P2   12 SER BB   22  0.0 
+ 23 TP1  12 SER SC1  23  0.0 
+ 24 P2   13 LEU BB   24  0.0 
+ 25 SC2  13 LEU SC1  25  0.0 
+ 26 P2   14 TYR BB   26  0.0 
+ 27 TC4  14 TYR SC1  27  0.0 
+ 28 TC5  14 TYR SC2  28  0.0 
+ 29 TC5  14 TYR SC3  29  0.0 
+ 30 TN6  14 TYR SC4  30  0.0 
+ 31 P2   15 GLN BB   31  0.0 
+ 32 P5   15 GLN SC1  32  0.0 
+ 33 P2   16 LEU BB   33  0.0 
+ 34 SC2  16 LEU SC1  34  0.0 
+ 35 P2   17 GLU BB   35  0.0 
+ 36 Q5n  17 GLU SC1  36 -1.0 
+ 37 P2   18 ASN BB   37  0.0 
+ 38 SP5  18 ASN SC1  38  0.0 
+ 39 P2   19 TYR BB   39  0.0 
+ 40 TC4  19 TYR SC1  40  0.0 
+ 41 TC5  19 TYR SC2  41  0.0 
+ 42 TC5  19 TYR SC3  42  0.0 
+ 43 TN6  19 TYR SC4  43  0.0 
+ 44 P2   20 CYS BB   44  0.0 
+ 45 TC6  20 CYS SC1  45  0.0 
+ 46 Q5   21 ASN BB   46   -1 
+ 47 SP5  21 ASN SC1  47  0.0 
+ 48 Q5   22 PHE BB   48    1 
+ 49 SC4  22 PHE SC1  49  0.0 
+ 50 TC5  22 PHE SC2  50  0.0 
+ 51 TC5  22 PHE SC3  51  0.0 
+ 52 SP2  23 VAL BB   52  0.0 
+ 53 SC3  23 VAL SC1  53  0.0 
+ 54 P2   24 ASN BB   54  0.0 
+ 55 SP5  24 ASN SC1  55  0.0 
+ 56 P2   25 GLN BB   56  0.0 
+ 57 P5   25 GLN SC1  57  0.0 
+ 58 P2   26 HIS BB   58  0.0 
+ 59 TC4  26 HIS SC1  59  0.0 
+ 60 TN6d 26 HIS SC2  60  0.0 
+ 61 TN5a 26 HIS SC3  61  0.0 
+ 62 P2   27 LEU BB   62  0.0 
+ 63 SC2  27 LEU SC1  63  0.0 
+ 64 P2   28 CYS BB   64  0.0 
+ 65 TC6  28 CYS SC1  65  0.0 
+ 66 SP1  29 GLY BB   66  0.0 
+ 67 P2   30 SER BB   67  0.0 
+ 68 TP1  30 SER SC1  68  0.0 
+ 69 P2   31 HIS BB   69  0.0 
+ 70 TC4  31 HIS SC1  70  0.0 
+ 71 TN6d 31 HIS SC2  71  0.0 
+ 72 TN5a 31 HIS SC3  72  0.0 
+ 73 P2   32 LEU BB   73  0.0 
+ 74 SC2  32 LEU SC1  74  0.0 
+ 75 SP2  33 VAL BB   75  0.0 
+ 76 SC3  33 VAL SC1  76  0.0 
+ 77 P2   34 GLU BB   77  0.0 
+ 78 Q5n  34 GLU SC1  78 -1.0 
+ 79 SP2  35 ALA BB   79  0.0 
+ 80 TC3  35 ALA SC1  80  0.0 
+ 81 P2   36 LEU BB   81  0.0 
+ 82 SC2  36 LEU SC1  82  0.0 
+ 83 P2   37 TYR BB   83  0.0 
+ 84 TC4  37 TYR SC1  84  0.0 
+ 85 TC5  37 TYR SC2  85  0.0 
+ 86 TC5  37 TYR SC3  86  0.0 
+ 87 TN6  37 TYR SC4  87  0.0 
+ 88 P2   38 LEU BB   88  0.0 
+ 89 SC2  38 LEU SC1  89  0.0 
+ 90 SP2  39 VAL BB   90  0.0 
+ 91 SC3  39 VAL SC1  91  0.0 
+ 92 P2   40 CYS BB   92  0.0 
+ 93 TC6  40 CYS SC1  93  0.0 
+ 94 SP1  41 GLY BB   94  0.0 
+ 95 P2   42 GLU BB   95  0.0 
+ 96 Q5n  42 GLU SC1  96 -1.0 
+ 97 P2   43 ARG BB   97  0.0 
+ 98 SC3  43 ARG SC1  98  0.0 
+ 99 SQ3p 43 ARG SC2  99  1.0 
+100 SP1  44 GLY BB  100  0.0 
+101 P2   45 PHE BB  101  0.0 
+102 SC4  45 PHE SC1 102  0.0 
+103 TC5  45 PHE SC2 103  0.0 
+104 TC5  45 PHE SC3 104  0.0 
+105 P2   46 PHE BB  105  0.0 
+106 SC4  46 PHE SC1 106  0.0 
+107 TC5  46 PHE SC2 107  0.0 
+108 TC5  46 PHE SC3 108  0.0 
+109 P2   47 TYR BB  109  0.0 
+110 TC4  47 TYR SC1 110  0.0 
+111 TC5  47 TYR SC2 111  0.0 
+112 TC5  47 TYR SC3 112  0.0 
+113 TN6  47 TYR SC4 113  0.0 
+114 P2   48 THR BB  114  0.0 
+115 SP1  48 THR SC1 115  0.0 
+116 SP2a 49 PRO BB  116  0.0 
+117 SC3  49 PRO SC1 117  0.0 
+118 P2   50 LYS BB  118  0.0 
+119 SC3  50 LYS SC1 119  0.0 
+120 SQ4p 50 LYS SC2 120  1.0 
+121 Q5   51 ALA BB  121   -1 
+122 TC3  51 ALA SC1 122  0.0 
+
+[ position_restraints ]
+#ifdef POSRES
+  1 1 1000 1000 1000
+  2 1 1000 1000 1000
+  4 1 1000 1000 1000
+  6 1 1000 1000 1000
+  8 1 1000 1000 1000
+ 10 1 1000 1000 1000
+ 12 1 1000 1000 1000
+ 14 1 1000 1000 1000
+ 16 1 1000 1000 1000
+ 18 1 1000 1000 1000
+ 20 1 1000 1000 1000
+ 22 1 1000 1000 1000
+ 24 1 1000 1000 1000
+ 26 1 1000 1000 1000
+ 31 1 1000 1000 1000
+ 33 1 1000 1000 1000
+ 35 1 1000 1000 1000
+ 37 1 1000 1000 1000
+ 39 1 1000 1000 1000
+ 44 1 1000 1000 1000
+ 46 1 1000 1000 1000
+ 48 1 1000 1000 1000
+ 52 1 1000 1000 1000
+ 54 1 1000 1000 1000
+ 56 1 1000 1000 1000
+ 58 1 1000 1000 1000
+ 62 1 1000 1000 1000
+ 64 1 1000 1000 1000
+ 66 1 1000 1000 1000
+ 67 1 1000 1000 1000
+ 69 1 1000 1000 1000
+ 73 1 1000 1000 1000
+ 75 1 1000 1000 1000
+ 77 1 1000 1000 1000
+ 79 1 1000 1000 1000
+ 81 1 1000 1000 1000
+ 83 1 1000 1000 1000
+ 88 1 1000 1000 1000
+ 90 1 1000 1000 1000
+ 92 1 1000 1000 1000
+ 94 1 1000 1000 1000
+ 95 1 1000 1000 1000
+ 97 1 1000 1000 1000
+100 1 1000 1000 1000
+101 1 1000 1000 1000
+105 1 1000 1000 1000
+109 1 1000 1000 1000
+114 1 1000 1000 1000
+116 1 1000 1000 1000
+118 1 1000 1000 1000
+121 1 1000 1000 1000
+#endif
+
+[ bonds ]
+; Backbone bonds
+ 14  16 1 0.350 4000
+ 16  18 1 0.350 4000
+ 18  20 1 0.350 4000
+ 20  22 1 0.350 4000
+ 37  39 1 0.350 4000
+ 39  44 1 0.350 4000
+ 44  46 1 0.350 4000
+ 48  52 1 0.350 4000
+ 52  54 1 0.350 4000
+ 54  56 1 0.350 4000
+ 56  58 1 0.350 4000
+ 58  62 1 0.350 4000
+ 62  64 1 0.350 4000
+ 64  66 1 0.350 4000
+100 101 1 0.350 4000
+101 105 1 0.350 4000
+105 109 1 0.350 4000
+109 114 1 0.350 4000
+114 116 1 0.350 4000
+116 118 1 0.350 4000
+118 121 1 0.350 4000
+
+; Rubber band
+  1   6 1 0.4832 500.0
+  1   8 1 0.59829 500.0
+  1  10 1 0.81378 500.0
+  2   8 1 0.47356 500.0
+  2  10 1 0.55601 500.0
+  2  12 1 0.71275 500.0
+  2  14 1 0.85886 500.0
+  2  16 1 0.8304 500.0
+  2  31 1 0.83117 500.0
+  2  33 1 0.87161 500.0
+  4  10 1 0.47804 500.0
+  4  12 1 0.4871 500.0
+  4  14 1 0.61074 500.0
+  4  16 1 0.67557 500.0
+  4  18 1 0.88603 500.0
+  6  12 1 0.53207 500.0
+  6  14 1 0.49367 500.0
+  6  16 1 0.53802 500.0
+  6  18 1 0.76576 500.0
+  8  14 1 0.58417 500.0
+  8  16 1 0.43738 500.0
+  8  18 1 0.5214 500.0
+  8  22 1 0.78801 500.0
+  8  31 1 0.8135 500.0
+ 10  31 1 0.89626 500.0
+ 14  20 1 0.88825 500.0
+ 20  26 1 0.82714 500.0
+ 20  31 1 0.76172 500.0
+ 20  33 1 0.87015 500.0
+ 22  31 1 0.48467 500.0
+ 22  33 1 0.58986 500.0
+ 22  35 1 0.82201 500.0
+ 24  33 1 0.49302 500.0
+ 24  35 1 0.61525 500.0
+ 24  37 1 0.84473 500.0
+ 26  35 1 0.51543 500.0
+ 26  37 1 0.6694 500.0
+ 31  37 1 0.50787 500.0
+ 31  39 1 0.70937 500.0
+ 31  44 1 0.88821 500.0
+ 33  39 1 0.51681 500.0
+ 33  44 1 0.68346 500.0
+ 35  44 1 0.49379 500.0
+ 35  46 1 0.79656 500.0
+ 37  46 1 0.77947 500.0
+ 48  56 1 0.65919 500.0
+ 48  58 1 0.84603 500.0
+ 48  79 1 0.771 500.0
+ 52  58 1 0.73333 500.0
+ 52  62 1 0.8209 500.0
+ 52  79 1 0.76673 500.0
+ 54  62 1 0.88509 500.0
+ 58  69 1 0.79857 500.0
+ 58  73 1 0.85897 500.0
+ 62  67 1 0.76747 500.0
+ 62  69 1 0.56165 500.0
+ 62  73 1 0.55218 500.0
+ 62  75 1 0.86036 500.0
+ 64  69 1 0.45366 500.0
+ 64  73 1 0.53138 500.0
+ 64  75 1 0.77842 500.0
+ 66  73 1 0.4821 500.0
+ 66  75 1 0.61604 500.0
+ 66  77 1 0.81712 500.0
+ 67  75 1 0.48496 500.0
+ 67  77 1 0.59509 500.0
+ 67  79 1 0.81562 500.0
+ 69  77 1 0.49312 500.0
+ 69  79 1 0.62294 500.0
+ 69  81 1 0.83323 500.0
+ 73  79 1 0.48939 500.0
+ 73  81 1 0.61629 500.0
+ 73  83 1 0.81794 500.0
+ 75  81 1 0.48859 500.0
+ 75  83 1 0.60888 500.0
+ 75  88 1 0.82503 500.0
+ 75 105 1 0.88798 500.0
+ 75 109 1 0.85352 500.0
+ 77  83 1 0.48527 500.0
+ 77  88 1 0.6153 500.0
+ 77  90 1 0.81796 500.0
+ 79  88 1 0.48547 500.0
+ 79  90 1 0.59471 500.0
+ 79  92 1 0.80095 500.0
+ 81  90 1 0.48783 500.0
+ 81  92 1 0.57507 500.0
+ 81  94 1 0.72464 500.0
+ 81 100 1 0.73275 500.0
+ 81 101 1 0.73204 500.0
+ 81 105 1 0.80887 500.0
+ 83  92 1 0.50376 500.0
+ 83  94 1 0.52769 500.0
+ 83  95 1 0.84802 500.0
+ 83  97 1 0.86499 500.0
+ 83 100 1 0.6861 500.0
+ 83 101 1 0.78829 500.0
+ 88  94 1 0.56152 500.0
+ 88 100 1 0.86908 500.0
+ 90  95 1 0.86316 500.0
+ 90  97 1 0.86323 500.0
+ 90 100 1 0.77404 500.0
+ 92  97 1 0.52729 500.0
+ 92 100 1 0.47326 500.0
+ 92 101 1 0.74935 500.0
+ 94 100 1 0.48855 500.0
+ 94 101 1 0.81335 500.0
+ 95 101 1 0.86594 500.0
+109 118 1 0.86945 500.0
+109 121 1 0.85247 500.0
+114 121 1 0.49721 500.0
+
+; Side chain bonds
+  6   7 1 0.400 5000
+  8   9 1 0.400 5000
+ 10  11 1 0.341 7500
+ 12  13 1 0.341 7500
+ 16  17 1 0.287 7500
+ 20  21 1 0.341 7500
+ 22  23 1 0.287 7500
+ 24  25 1 0.363 7500
+ 26  27 1 0.325 5000
+ 31  32 1 0.400 5000
+ 33  34 1 0.363 7500
+ 35  36 1 0.400 5000
+ 37  38 1 0.352 5000
+ 39  40 1 0.325 5000
+ 44  45 1 0.341 7500
+ 46  47 1 0.352 5000
+ 48  49 1 0.325 7500
+ 54  55 1 0.352 5000
+ 56  57 1 0.400 5000
+ 58  59 1 0.336 7500
+ 62  63 1 0.363 7500
+ 64  65 1 0.341 7500
+ 67  68 1 0.287 7500
+ 69  70 1 0.336 7500
+ 73  74 1 0.363 7500
+ 77  78 1 0.400 5000
+ 81  82 1 0.363 7500
+ 83  84 1 0.325 5000
+ 88  89 1 0.363 7500
+ 92  93 1 0.341 7500
+ 95  96 1 0.400 5000
+ 97  98 1 0.330 5000
+ 98  99 1 0.380 5000
+101 102 1 0.325 7500
+105 106 1 0.325 7500
+109 110 1 0.325 5000
+116 117 1 0.330 7500
+118 119 1 0.330 5000
+119 120 1 0.360 5000
+
+#ifdef FLEXIBLE
+; Side chain bonds
+  2   3 1 0.341 1000000
+  4   5 1 0.292 1000000
+ 14  15 1 0.305 1000000
+ 18  19 1 0.341 1000000
+ 27  28 1 0.300 1000000
+ 27  29 1 0.300 1000000
+ 28  30 1 0.285 1000000
+ 29  30 1 0.285 1000000
+ 28  29 1 0.300 1000000
+ 40  41 1 0.300 1000000
+ 40  42 1 0.300 1000000
+ 41  43 1 0.285 1000000
+ 42  43 1 0.285 1000000
+ 41  42 1 0.300 1000000
+ 49  50 1 0.340 1000000
+ 49  51 1 0.340 1000000
+ 50  51 1 0.290 1000000
+ 52  53 1 0.292 1000000
+ 59  60 1 0.320 1000000
+ 59  61 1 0.300 1000000
+ 60  61 1 0.270 1000000
+ 70  71 1 0.320 1000000
+ 70  72 1 0.300 1000000
+ 71  72 1 0.270 1000000
+ 75  76 1 0.292 1000000
+ 79  80 1 0.270 1000000
+ 84  85 1 0.300 1000000
+ 84  86 1 0.300 1000000
+ 85  87 1 0.285 1000000
+ 86  87 1 0.285 1000000
+ 85  86 1 0.300 1000000
+ 90  91 1 0.292 1000000
+102 103 1 0.340 1000000
+102 104 1 0.340 1000000
+103 104 1 0.290 1000000
+106 107 1 0.340 1000000
+106 108 1 0.340 1000000
+107 108 1 0.290 1000000
+110 111 1 0.300 1000000
+110 112 1 0.300 1000000
+111 113 1 0.285 1000000
+112 113 1 0.285 1000000
+111 112 1 0.300 1000000
+114 115 1 0.305 1000000
+121 122 1 0.270 1000000
+#endif
+
+[ constraints ]
+ 11  21 1 0.24 ; Disulfide bridge
+ 13  65 1 0.24 ; Disulfide bridge
+ 45  93 1 0.24 ; Disulfide bridge
+
+; Backbone bonds
+  1   2 1 0.33
+  2   4 1 0.310
+  4   6 1 0.310
+  6   8 1 0.310
+  8  10 1 0.310
+ 10  12 1 0.310
+ 12  14 1 0.33
+ 22  24 1 0.33
+ 24  26 1 0.310
+ 26  31 1 0.310
+ 31  33 1 0.310
+ 33  35 1 0.310
+ 35  37 1 0.33
+ 66  67 1 0.33
+ 67  69 1 0.310
+ 69  73 1 0.310
+ 73  75 1 0.310
+ 75  77 1 0.310
+ 77  79 1 0.310
+ 79  81 1 0.310
+ 81  83 1 0.310
+ 83  88 1 0.310
+ 88  90 1 0.310
+ 90  92 1 0.310
+ 92  94 1 0.310
+ 94  95 1 0.310
+ 95  97 1 0.310
+ 97 100 1 0.33
+
+#ifndef FLEXIBLE
+; Side chain bonds
+  2   3 1 0.341
+  4   5 1 0.292
+ 14  15 1 0.305
+ 18  19 1 0.341
+ 27  28 1 0.300
+ 27  29 1 0.300
+ 28  30 1 0.285
+ 29  30 1 0.285
+ 28  29 1 0.300
+ 40  41 1 0.300
+ 40  42 1 0.300
+ 41  43 1 0.285
+ 42  43 1 0.285
+ 41  42 1 0.300
+ 49  50 1 0.340
+ 49  51 1 0.340
+ 50  51 1 0.290
+ 52  53 1 0.292
+ 59  60 1 0.320
+ 59  61 1 0.300
+ 60  61 1 0.270
+ 70  71 1 0.320
+ 70  72 1 0.300
+ 71  72 1 0.270
+ 75  76 1 0.292
+ 79  80 1 0.270
+ 84  85 1 0.300
+ 84  86 1 0.300
+ 85  87 1 0.285
+ 86  87 1 0.285
+ 85  86 1 0.300
+ 90  91 1 0.292
+102 103 1 0.340
+102 104 1 0.340
+103 104 1 0.290
+106 107 1 0.340
+106 108 1 0.340
+107 108 1 0.290
+110 111 1 0.300
+110 112 1 0.300
+111 113 1 0.285
+112 113 1 0.285
+111 112 1 0.300
+114 115 1 0.305
+121 122 1 0.270
+#endif
+
+[ angles ]
+; BBB angles
+  1   2   4 10 127 20
+  2   4   6 2 96 700
+  4   6   8 2 96 700
+  6   8  10 2 96 700
+  8  10  12 2 96 700
+ 10  12  14 10 100 20
+ 12  14  16 10 100 20
+ 20  22  24 10 127 20
+ 22  24  26 10 127 20
+ 24  26  31 2 96 700
+ 26  31  33 2 96 700
+ 31  33  35 2 96 700
+ 33  35  37 10 100 20
+ 35  37  39 10 100 20
+ 64  66  67 10 100 20
+ 66  67  69 10 100 20
+ 67  69  73 2 96 700
+ 69  73  75 2 96 700
+ 73  75  77 2 96 700
+ 75  77  79 2 96 700
+ 77  79  81 2 96 700
+ 79  81  83 2 96 700
+ 81  83  88 2 96 700
+ 83  88  90 2 96 700
+ 88  90  92 2 96 700
+ 90  92  94 2 96 700
+ 92  94  95 2 96 700
+ 94  95  97 2 96 700
+ 95  97 100 10 127 20
+ 97 100 101 10 127 20
+ 37  39  44 10 100 20
+ 39  44  46 10 100 20
+100 101 105 10 127 20
+101 105 109 10 127 20
+109 114 116 10 127 20
+114 116 118 10 127 20
+116 118 121 10 127 20
+ 48  52  54 10 127 20
+ 52  54  56 10 127 20
+ 54  56  58 10 127 20
+ 56  58  62 10 127 20
+ 16  18  20 10 100 20
+ 18  20  22 10 100 20
+ 58  62  64 10 127 20
+ 62  64  66 10 100 20
+105 109 114 10 127 20
+ 14  16  18 10 100 20
+
+; BBS angles regular martini
+  1   2   3 2 100 25
+  2   4   5 2 100 25
+  4   6   7 2 100 25
+  6   8   9 2 100 25
+  8  10  11 2 100 25
+ 10  12  13 2 100 25
+ 12  14  15 2 100 25
+ 14  16  17 2 100 25
+ 16  18  19 2 100 25
+ 18  20  21 2 100 25
+ 20  22  23 2 100 25
+ 22  24  25 2 100 25
+ 24  26  27 2 100 25
+ 26  31  32 2 100 25
+ 31  33  34 2 100 25
+ 33  35  36 2 100 25
+ 35  37  38 2 100 25
+ 37  39  40 2 100 25
+ 39  44  45 2 100 25
+ 44  46  47 2 100 25
+ 48  52  53 2 100 25
+ 52  54  55 2 100 25
+ 54  56  57 2 100 25
+ 56  58  59 2 100 25
+ 58  62  63 2 100 25
+ 62  64  65 2 100 25
+ 66  67  68 2 100 25
+ 67  69  70 2 100 25
+ 69  73  74 2 100 25
+ 73  75  76 2 100 25
+ 75  77  78 2 100 25
+ 77  79  80 2 100 25
+ 79  81  82 2 100 25
+ 81  83  84 2 100 25
+ 83  88  89 2 100 25
+ 88  90  91 2 100 25
+ 90  92  93 2 100 25
+ 94  95  96 2 100 25
+ 95  97  98 2 100 25
+100 101 102 2 100 25
+101 105 106 2 100 25
+105 109 110 2 100 25
+109 114 115 2 100 25
+114 116 117 2 100 25
+116 118 119 2 100 25
+118 121 122 2 100 25
+
+; First SBB regular martini
+ 49  48  52 2 100 25
+
+; SC-BB-BB and BB-BB-SC scFix
+  3   2   4 10 100 15 ; SC-BB-BB
+  5   4   6 10 100 15 ; SC-BB-BB
+  7   6   8 10 100 15 ; SC-BB-BB
+  9   8  10 10 100 15 ; SC-BB-BB
+ 11  10  12 10 100 15 ; SC-BB-BB
+ 13  12  14 10 100 15 ; SC-BB-BB
+ 15  14  16 10 100 15 ; SC-BB-BB
+ 17  16  18 10 100 15 ; SC-BB-BB
+ 19  18  20 10 100 15 ; SC-BB-BB
+ 21  20  22 10 100 15 ; SC-BB-BB
+ 23  22  24 10 100 15 ; SC-BB-BB
+ 25  24  26 10 100 15 ; SC-BB-BB
+ 27  26  31 10 100 15 ; SC-BB-BB
+ 32  31  33 10 100 15 ; SC-BB-BB
+ 34  33  35 10 100 15 ; SC-BB-BB
+ 36  35  37 10 100 15 ; SC-BB-BB
+ 38  37  39 10 100 15 ; SC-BB-BB
+ 40  39  44 10 100 15 ; SC-BB-BB
+ 45  44  46 10 100 15 ; SC-BB-BB
+ 49  48  52 10 100 15 ; SC-BB-BB
+ 53  52  54 10 100 15 ; SC-BB-BB
+ 55  54  56 10 100 15 ; SC-BB-BB
+ 57  56  58 10 100 15 ; SC-BB-BB
+ 59  58  62 10 100 15 ; SC-BB-BB
+ 63  62  64 10 100 15 ; SC-BB-BB
+ 65  64  66 10 100 15 ; SC-BB-BB
+ 68  67  69 10 100 15 ; SC-BB-BB
+ 70  69  73 10 100 15 ; SC-BB-BB
+ 74  73  75 10 100 15 ; SC-BB-BB
+ 76  75  77 10 100 15 ; SC-BB-BB
+ 78  77  79 10 100 15 ; SC-BB-BB
+ 80  79  81 10 100 15 ; SC-BB-BB
+ 82  81  83 10 100 15 ; SC-BB-BB
+ 84  83  88 10 100 15 ; SC-BB-BB
+ 89  88  90 10 100 15 ; SC-BB-BB
+ 91  90  92 10 100 15 ; SC-BB-BB
+ 93  92  94 10 100 15 ; SC-BB-BB
+ 96  95  97 10 100 15 ; SC-BB-BB
+ 98  97 100 10 100 15 ; SC-BB-BB
+102 101 105 10 100 15 ; SC-BB-BB
+106 105 109 10 100 15 ; SC-BB-BB
+110 109 114 10 100 15 ; SC-BB-BB
+115 114 116 10 100 15 ; SC-BB-BB
+117 116 118 10 100 15 ; SC-BB-BB
+119 118 121 10 100 15 ; SC-BB-BB
+  1   2   3 10 100 15 ; BB-BB-SC
+  2   4   5 10 100 15 ; BB-BB-SC
+  4   6   7 10 100 15 ; BB-BB-SC
+  6   8   9 10 100 15 ; BB-BB-SC
+  8  10  11 10 100 15 ; BB-BB-SC
+ 10  12  13 10 100 15 ; BB-BB-SC
+ 12  14  15 10 100 15 ; BB-BB-SC
+ 14  16  17 10 100 15 ; BB-BB-SC
+ 16  18  19 10 100 15 ; BB-BB-SC
+ 18  20  21 10 100 15 ; BB-BB-SC
+ 20  22  23 10 100 15 ; BB-BB-SC
+ 22  24  25 10 100 15 ; BB-BB-SC
+ 24  26  27 10 100 15 ; BB-BB-SC
+ 26  31  32 10 100 15 ; BB-BB-SC
+ 31  33  34 10 100 15 ; BB-BB-SC
+ 33  35  36 10 100 15 ; BB-BB-SC
+ 35  37  38 10 100 15 ; BB-BB-SC
+ 37  39  40 10 100 15 ; BB-BB-SC
+ 39  44  45 10 100 15 ; BB-BB-SC
+ 44  46  47 10 100 15 ; BB-BB-SC
+ 48  52  53 10 100 15 ; BB-BB-SC
+ 52  54  55 10 100 15 ; BB-BB-SC
+ 54  56  57 10 100 15 ; BB-BB-SC
+ 56  58  59 10 100 15 ; BB-BB-SC
+ 58  62  63 10 100 15 ; BB-BB-SC
+ 62  64  65 10 100 15 ; BB-BB-SC
+ 66  67  68 10 100 15 ; BB-BB-SC
+ 67  69  70 10 100 15 ; BB-BB-SC
+ 69  73  74 10 100 15 ; BB-BB-SC
+ 73  75  76 10 100 15 ; BB-BB-SC
+ 75  77  78 10 100 15 ; BB-BB-SC
+ 77  79  80 10 100 15 ; BB-BB-SC
+ 79  81  82 10 100 15 ; BB-BB-SC
+ 81  83  84 10 100 15 ; BB-BB-SC
+ 83  88  89 10 100 15 ; BB-BB-SC
+ 88  90  91 10 100 15 ; BB-BB-SC
+ 90  92  93 10 100 15 ; BB-BB-SC
+ 94  95  96 10 100 15 ; BB-BB-SC
+ 95  97  98 10 100 15 ; BB-BB-SC
+100 101 102 10 100 15 ; BB-BB-SC
+101 105 106 10 100 15 ; BB-BB-SC
+105 109 110 10 100 15 ; BB-BB-SC
+109 114 115 10 100 15 ; BB-BB-SC
+114 116 117 10 100 15 ; BB-BB-SC
+116 118 119 10 100 15 ; BB-BB-SC
+118 121 122 10 100 15 ; BB-BB-SC
+
+; Side chain angles
+ 26  27  28 2 120.000 60.0
+ 26  27  29 2 120.000 60.0
+ 39  40  41 2 120.000 60.0
+ 39  40  42 2 120.000 60.0
+ 48  49  50 2 120.000 50.0
+ 48  49  51 2 120.000 50.0
+ 58  59  60 2 120.000 50.0
+ 58  59  61 2 120.000 50.0
+ 69  70  71 2 120.000 50.0
+ 69  70  72 2 120.000 50.0
+ 83  84  85 2 120.000 60.0
+ 83  84  86 2 120.000 60.0
+ 97  98  99 2 180.000 25.0
+101 102 103 2 120.000 50.0
+101 102 104 2 120.000 50.0
+105 106 107 2 120.000 50.0
+105 106 108 2 120.000 50.0
+109 110 111 2 120.000 60.0
+109 110 112 2 120.000 60.0
+118 119 120 2 180.000 25.0
+
+[ dihedrals ]
+  2   4   6   8 1 -120 400 1
+  4   6   8  10 1 -120 400 1
+  6   8  10  12 1 -120 400 1
+ 24  26  31  33 1 -120 400 1
+ 26  31  33  35 1 -120 400 1
+ 67  69  73  75 1 -120 400 1
+ 69  73  75  77 1 -120 400 1
+ 73  75  77  79 1 -120 400 1
+ 75  77  79  81 1 -120 400 1
+ 77  79  81  83 1 -120 400 1
+ 79  81  83  88 1 -120 400 1
+ 81  83  88  90 1 -120 400 1
+ 83  88  90  92 1 -120 400 1
+ 88  90  92  94 1 -120 400 1
+ 90  92  94  95 1 -120 400 1
+ 92  94  95  97 1 -120 400 1
+
+; SC-BB-BB-SC scFix
+  3   2   4   5 1 -121.9 75 1 ; SC-BB-BB-SC
+  5   4   6   7 1 -139.8 75 1 ; SC-BB-BB-SC
+  7   6   8   9 1 126.7 75 1 ; SC-BB-BB-SC
+  9   8  10  11 1 148.0 75 1 ; SC-BB-BB-SC
+ 11  10  12  13 1 -178.9 75 1 ; SC-BB-BB-SC
+ 13  12  14  15 1 -140.1 75 1 ; SC-BB-BB-SC
+ 15  14  16  17 1 141.7 75 1 ; SC-BB-BB-SC
+ 17  16  18  19 1 60.8 75 1 ; SC-BB-BB-SC
+ 19  18  20  21 1 42.9 75 1 ; SC-BB-BB-SC
+ 21  20  22  23 1 40.4 75 1 ; SC-BB-BB-SC
+ 23  22  24  25 1 63.0 75 1 ; SC-BB-BB-SC
+ 25  24  26  27 1 -99.1 75 1 ; SC-BB-BB-SC
+ 27  26  31  32 1 -144.6 75 1 ; SC-BB-BB-SC
+ 32  31  33  34 1 -133.4 75 1 ; SC-BB-BB-SC
+ 34  33  35  36 1 -151.0 75 1 ; SC-BB-BB-SC
+ 36  35  37  38 1 -119.2 75 1 ; SC-BB-BB-SC
+ 38  37  39  40 1 170.7 75 1 ; SC-BB-BB-SC
+ 40  39  44  45 1 111.2 75 1 ; SC-BB-BB-SC
+ 45  44  46  47 1 64.0 75 1 ; SC-BB-BB-SC
+ 49  48  52  53 1 -152.4 75 1 ; SC-BB-BB-SC
+ 53  52  54  55 1 169.6 75 1 ; SC-BB-BB-SC
+ 55  54  56  57 1 29.6 75 1 ; SC-BB-BB-SC
+ 57  56  58  59 1 51.8 75 1 ; SC-BB-BB-SC
+ 59  58  62  63 1 16.6 75 1 ; SC-BB-BB-SC
+ 63  62  64  65 1 22.2 75 1 ; SC-BB-BB-SC
+ 68  67  69  70 1 -146.5 75 1 ; SC-BB-BB-SC
+ 70  69  73  74 1 -168.2 75 1 ; SC-BB-BB-SC
+ 74  73  75  76 1 -120.4 75 1 ; SC-BB-BB-SC
+ 76  75  77  78 1 -117.0 75 1 ; SC-BB-BB-SC
+ 78  77  79  80 1 -122.0 75 1 ; SC-BB-BB-SC
+ 80  79  81  82 1 -153.2 75 1 ; SC-BB-BB-SC
+ 82  81  83  84 1 -124.4 75 1 ; SC-BB-BB-SC
+ 84  83  88  89 1 -144.2 75 1 ; SC-BB-BB-SC
+ 89  88  90  91 1 -148.1 75 1 ; SC-BB-BB-SC
+ 91  90  92  93 1 -158.9 75 1 ; SC-BB-BB-SC
+ 96  95  97  98 1 -124.4 75 1 ; SC-BB-BB-SC
+102 101 105 106 1 25.9 75 1 ; SC-BB-BB-SC
+106 105 109 110 1 -6.7 75 1 ; SC-BB-BB-SC
+110 109 114 115 1 13.3 75 1 ; SC-BB-BB-SC
+115 114 116 117 1 51.4 75 1 ; SC-BB-BB-SC
+117 116 118 119 1 135.4 75 1 ; SC-BB-BB-SC
+119 118 121 122 1 -159.0 75 1 ; SC-BB-BB-SC
+ 64  66  67  68 1 88.3 75 1 ; BB-BB-BB-SC
+ 65  64  66  67 1 -15.5 75 1 ; SC-BB-BB-BB
+ 92  94  95  96 1 68.7 75 1 ; BB-BB-BB-SC
+ 93  92  94  95 1 95.9 75 1 ; SC-BB-BB-BB
+ 97 100 101 102 1 -9.0 75 1 ; BB-BB-BB-SC
+ 98  97 100 101 1 74.1 75 1 ; SC-BB-BB-BB
+
+[ dihedrals ]
+ 30  28  29  27 2 180.0 50.0
+ 43  41  42  40 2 180.0 50.0
+ 87  85  86  84 2 180.0 50.0
+113 111 112 110 2 180.0 50.0
+
+[ exclusions ]
+ 26  27  28  29  30 
+ 27  28  29  30 
+ 28  29  30 
+ 29  30 
+ 39  40  41  42  43 
+ 40  41  42  43 
+ 41  42  43 
+ 42  43 
+ 48  49  50  51 
+ 49  50  51 
+ 50  51 
+ 58  59  60  61 
+ 59  60  61 
+ 60  61 
+ 69  70  71  72 
+ 70  71  72 
+ 71  72 
+ 83  84  85  86  87 
+ 84  85  86  87 
+ 85  86  87 
+ 86  87 
+101 102 103 104 
+102 103 104 
+103 104 
+105 106 107 108 
+106 107 108 
+107 108 
+109 110 111 112 113 
+110 111 112 113 
+111 112 113 
+112 113 
+
diff --git a/vermouth/tests/data/integration_tests/tier-1/EN_chain/martinize2/screen.output b/vermouth/tests/data/integration_tests/tier-1/EN_chain/martinize2/screen.output
new file mode 100644
index 00000000..efa25786
--- /dev/null
+++ b/vermouth/tests/data/integration_tests/tier-1/EN_chain/martinize2/screen.output
@@ -0,0 +1,27 @@
+    INFO - general - Merging two molecules/chains because there is a CONECT record between atoms 49A-CYS7:SG and 231B-CYS7:SG
+    INFO - general - Read 1 molecules from PDB file ../aa.pdb
+    INFO - step - Guessing the bonds.
+    INFO - general - 1 molecules after guessing bonds
+    INFO - step - Repairing the graph.
+    INFO - general - Applying modification N-ter to residue A-GLY1
+    INFO - general - Applying modification C-ter to residue A-ASN21
+    INFO - general - Applying modification N-ter to residue B-PHE1
+    INFO - general - Applying modification C-ter to residue B-ALA30
+    INFO - step - Dealing with modifications.
+    INFO - general - Identified the modifications ['N-ter', 'N-ter'] on residues ['GLY1', 'GLY1', 'GLY1', 'GLY1']
+    INFO - general - Identified the modifications ['C-ter'] on residues ['ASN21', 'ASN21', 'ASN21']
+    INFO - general - Identified the modifications ['C-ter'] on residues ['ALA30', 'ALA30', 'ALA30']
+    INFO - step - Read input.
+    INFO - step - Creating the graph at the target resolution.
+    INFO - general - Applying modification mapping ('C-ter',)
+    INFO - general - Applying modification mapping ('C-ter',)
+    INFO - general - Applying modification mapping ('N-ter',)
+    INFO - general - Applying modification mapping ('N-ter',)
+    INFO - step - Averaging the coordinates.
+    INFO - step - Applying the links.
+    INFO - step - Placing the charge dummies.
+    INFO - step - Applying position restraints.
+    INFO - step - Setting the rubber bands.
+    INFO - step - Writing output.
+    INFO - general - Please cite: Souza, P C T; Alessandri, R; Barnoud, J; Thallmair, S; Faustino, I; Grünewald, F; Patmanidis, I; Abdizadeh, H; Bruininks, B M H; Wassenaar, T A; Kroon, P C; Melcr, J; Nieto, V; Corradi, V; Khan, H M; Domański, J; Javanainen, M; Martinez-Seara, H; Reuter, N; Best, R B; Vattulainen, I; Monticelli, L; Periole, X; Tieleman, D P; de Vries, A H; Marrink, S J;  Nature Methods 2021; 10.1038/s41592-021-01098-3
+    INFO - general - Zen martini: A martini with no vermouth at all. And no gin, either. -- P.J. O’Rourke
diff --git a/vermouth/tests/data/integration_tests/tier-1/EN_region/README b/vermouth/tests/data/integration_tests/tier-1/EN_region/README
new file mode 100644
index 00000000..7e17aa0d
--- /dev/null
+++ b/vermouth/tests/data/integration_tests/tier-1/EN_region/README
@@ -0,0 +1,13 @@
+### DETAILS: 
+
+# Human Insulin HOMRO dimer
+# 2 chains which are connected by disulphide bridge
+
+### TEST: 
+
+# the test checks -eunit flag
+# with setting region and a
+# residue range
+# elastic bonds should be formed
+# only within the regions within
+# the chains -> old_resids are used
diff --git a/vermouth/tests/data/integration_tests/tier-1/EN_region/aa.pdb b/vermouth/tests/data/integration_tests/tier-1/EN_region/aa.pdb
new file mode 100644
index 00000000..8f960de1
--- /dev/null
+++ b/vermouth/tests/data/integration_tests/tier-1/EN_region/aa.pdb
@@ -0,0 +1,788 @@
+HEADER    HORMONE                                 01-JUL-09   3I40              
+TITLE     HUMAN INSULIN                                                         
+COMPND    MOL_ID: 1;                                                            
+COMPND   2 MOLECULE: INSULIN A CHAIN;                                           
+COMPND   3 CHAIN: A;                                                            
+COMPND   4 ENGINEERED: YES;                                                     
+COMPND   5 MOL_ID: 2;                                                           
+COMPND   6 MOLECULE: INSULIN B CHAIN;                                           
+COMPND   7 CHAIN: B;                                                            
+COMPND   8 ENGINEERED: YES                                                      
+SOURCE    MOL_ID: 1;                                                            
+SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
+SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
+SOURCE   4 ORGANISM_TAXID: 9606;                                                
+SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
+SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
+SOURCE   7 MOL_ID: 2;                                                           
+SOURCE   8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
+SOURCE   9 ORGANISM_COMMON: HUMAN;                                              
+SOURCE  10 ORGANISM_TAXID: 9606;                                                
+SOURCE  11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
+SOURCE  12 EXPRESSION_SYSTEM_TAXID: 562                                         
+KEYWDS    INSULIN, CARBOHYDRATE METABOLISM, CLEAVAGE ON PAIR OF BASIC RESIDUES, 
+KEYWDS   2 DIABETES MELLITUS, DISEASE MUTATION, DISULFIDE BOND, GLUCOSE         
+KEYWDS   3 METABOLISM, HORMONE, PHARMACEUTICAL, SECRETED                        
+EXPDTA    X-RAY DIFFRACTION                                                     
+AUTHOR    V.I.TIMOFEEV,V.V.BEZUGLOV,K.A.MIROSHNIKOV,R.N.CHUPROV-NETOCHIN,       
+AUTHOR   2 I.P.KURANOVA                                                         
+REVDAT   2   05-MAY-10 3I40    1       JRNL                                     
+REVDAT   1   05-JAN-10 3I40    0                                                
+JRNL        AUTH   V.I.TIMOFEEV,R.N.CHUPROV-NETOCHIN,V.R.SAMIGINA,              
+JRNL        AUTH 2 V.V.BEZUGLOV,K.A.MIROSHNIKOV,I.P.KURANOVA                    
+JRNL        TITL   X-RAY INVESTIGATION OF GENE-ENGINEERED HUMAN INSULIN         
+JRNL        TITL 2 CRYSTALLIZED FROM A SOLUTION CONTAINING POLYSIALIC ACID.     
+JRNL        REF    ACTA CRYSTALLOGR.,SECT.F      V.  66   259 2010              
+JRNL        REFN                   ESSN 1744-3091                               
+JRNL        PMID   20208155                                                     
+JRNL        DOI    10.1107/S1744309110000461                                    
+REMARK   2                                                                      
+REMARK   2 RESOLUTION.    1.85 ANGSTROMS.                                       
+REMARK   3                                                                      
+REMARK   3 REFINEMENT.                                                          
+REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
+REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
+REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
+REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
+REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
+REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
+REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
+REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
+REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
+REMARK   3               : ZWART                                                
+REMARK   3                                                                      
+REMARK   3    REFINEMENT TARGET : ML                                            
+REMARK   3                                                                      
+REMARK   3  DATA USED IN REFINEMENT.                                            
+REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85                           
+REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 31.52                          
+REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
+REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.1                           
+REMARK   3   NUMBER OF REFLECTIONS             : 6640                           
+REMARK   3                                                                      
+REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
+REMARK   3   R VALUE     (WORKING + TEST SET) : 0.202                           
+REMARK   3   R VALUE            (WORKING SET) : 0.200                           
+REMARK   3   FREE R VALUE                     : 0.228                           
+REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.760                           
+REMARK   3   FREE R VALUE TEST SET COUNT      : 316                             
+REMARK   3                                                                      
+REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
+REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
+REMARK   3     1 31.5295 -  2.3309    1.00     3219   154  0.1910 0.2145        
+REMARK   3     2  2.3309 -  1.8501    0.99     3105   162  0.2301 0.2627        
+REMARK   3                                                                      
+REMARK   3  BULK SOLVENT MODELLING.                                             
+REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
+REMARK   3   SOLVENT RADIUS     : 1.11                                          
+REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
+REMARK   3   K_SOL              : 0.35                                          
+REMARK   3   B_SOL              : 47.05                                         
+REMARK   3                                                                      
+REMARK   3  ERROR ESTIMATES.                                                    
+REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.240            
+REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.930           
+REMARK   3                                                                      
+REMARK   3  B VALUES.                                                           
+REMARK   3   FROM WILSON PLOT           (A**2) : 24.04                          
+REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 30.30                          
+REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
+REMARK   3    B11 (A**2) : NULL                                                 
+REMARK   3    B22 (A**2) : NULL                                                 
+REMARK   3    B33 (A**2) : NULL                                                 
+REMARK   3    B12 (A**2) : NULL                                                 
+REMARK   3    B13 (A**2) : NULL                                                 
+REMARK   3    B23 (A**2) : NULL                                                 
+REMARK   3                                                                      
+REMARK   3  TWINNING INFORMATION.                                               
+REMARK   3   FRACTION: NULL                                                     
+REMARK   3   OPERATOR: NULL                                                     
+REMARK   3                                                                      
+REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
+REMARK   3                 RMSD          COUNT                                  
+REMARK   3   BOND      :  0.005            423                                  
+REMARK   3   ANGLE     :  0.760            569                                  
+REMARK   3   CHIRALITY :  0.068             62                                  
+REMARK   3   PLANARITY :  0.002             73                                  
+REMARK   3   DIHEDRAL  : 17.205            141                                  
+REMARK   3                                                                      
+REMARK   3  TLS DETAILS                                                         
+REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
+REMARK   3                                                                      
+REMARK   3  NCS DETAILS                                                         
+REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
+REMARK   3                                                                      
+REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
+REMARK   4                                                                      
+REMARK   4 3I40 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
+REMARK 100                                                                      
+REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-JUL-09.                  
+REMARK 100 THE RCSB ID CODE IS RCSB053935.                                      
+REMARK 200                                                                      
+REMARK 200 EXPERIMENTAL DETAILS                                                 
+REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
+REMARK 200  DATE OF DATA COLLECTION        : 10-MAR-09                          
+REMARK 200  TEMPERATURE           (KELVIN) : 100                                
+REMARK 200  PH                             : NULL                               
+REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
+REMARK 200                                                                      
+REMARK 200  SYNCHROTRON              (Y/N) : N                                  
+REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
+REMARK 200  BEAMLINE                       : NULL                               
+REMARK 200  X-RAY GENERATOR MODEL          : BRUKER AXS MICROSTAR               
+REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
+REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
+REMARK 200  MONOCHROMATOR                  : NULL                               
+REMARK 200  OPTICS                         : NULL                               
+REMARK 200                                                                      
+REMARK 200  DETECTOR TYPE                  : CCD                                
+REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM                     
+REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
+REMARK 200  DATA SCALING SOFTWARE          : NULL                               
+REMARK 200                                                                      
+REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 6677                               
+REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.850                              
+REMARK 200  RESOLUTION RANGE LOW       (A) : 54.636                             
+REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
+REMARK 200                                                                      
+REMARK 200 OVERALL.                                                             
+REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
+REMARK 200  DATA REDUNDANCY                : NULL                               
+REMARK 200  R MERGE                    (I) : NULL                               
+REMARK 200  R SYM                      (I) : NULL                               
+REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
+REMARK 200                                                                      
+REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
+REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
+REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
+REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
+REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
+REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
+REMARK 200  R SYM FOR SHELL            (I) : NULL                               
+REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
+REMARK 200                                                                      
+REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
+REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
+REMARK 200 SOFTWARE USED: NULL                                                  
+REMARK 200 STARTING MODEL: PDB ENTRY 2G4M                                       
+REMARK 200                                                                      
+REMARK 200 REMARK: NULL                                                         
+REMARK 280                                                                      
+REMARK 280 CRYSTAL                                                              
+REMARK 280 SOLVENT CONTENT, VS   (%): 62.90                                     
+REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.31                     
+REMARK 280                                                                      
+REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
+REMARK 290                                                                      
+REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
+REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 21 3                           
+REMARK 290                                                                      
+REMARK 290      SYMOP   SYMMETRY                                                
+REMARK 290     NNNMMM   OPERATOR                                                
+REMARK 290       1555   X,Y,Z                                                   
+REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
+REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
+REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
+REMARK 290       5555   Z,X,Y                                                   
+REMARK 290       6555   Z+1/2,-X+1/2,-Y                                         
+REMARK 290       7555   -Z+1/2,-X,Y+1/2                                         
+REMARK 290       8555   -Z,X+1/2,-Y+1/2                                         
+REMARK 290       9555   Y,Z,X                                                   
+REMARK 290      10555   -Y,Z+1/2,-X+1/2                                         
+REMARK 290      11555   Y+1/2,-Z+1/2,-X                                         
+REMARK 290      12555   -Y+1/2,-Z,X+1/2                                         
+REMARK 290      13555   X+1/2,Y+1/2,Z+1/2                                       
+REMARK 290      14555   -X,-Y+1/2,Z                                             
+REMARK 290      15555   -X+1/2,Y,-Z                                             
+REMARK 290      16555   X,-Y,-Z+1/2                                             
+REMARK 290      17555   Z+1/2,X+1/2,Y+1/2                                       
+REMARK 290      18555   Z,-X,-Y+1/2                                             
+REMARK 290      19555   -Z,-X+1/2,Y                                             
+REMARK 290      20555   -Z+1/2,X,-Y                                             
+REMARK 290      21555   Y+1/2,Z+1/2,X+1/2                                       
+REMARK 290      22555   -Y+1/2,Z,-X                                             
+REMARK 290      23555   Y,-Z,-X+1/2                                             
+REMARK 290      24555   -Y,-Z+1/2,X                                             
+REMARK 290                                                                      
+REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
+REMARK 290           MMM -> TRANSLATION VECTOR                                  
+REMARK 290                                                                      
+REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
+REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
+REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
+REMARK 290 RELATED MOLECULES.                                                   
+REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
+REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
+REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
+REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       38.61000            
+REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
+REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       38.61000            
+REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
+REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       38.61000            
+REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       38.61000            
+REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       38.61000            
+REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       38.61000            
+REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
+REMARK 290   SMTRY1   5  0.000000  0.000000  1.000000        0.00000            
+REMARK 290   SMTRY2   5  1.000000  0.000000  0.000000        0.00000            
+REMARK 290   SMTRY3   5  0.000000  1.000000  0.000000        0.00000            
+REMARK 290   SMTRY1   6  0.000000  0.000000  1.000000       38.61000            
+REMARK 290   SMTRY2   6 -1.000000  0.000000  0.000000       38.61000            
+REMARK 290   SMTRY3   6  0.000000 -1.000000  0.000000        0.00000            
+REMARK 290   SMTRY1   7  0.000000  0.000000 -1.000000       38.61000            
+REMARK 290   SMTRY2   7 -1.000000  0.000000  0.000000        0.00000            
+REMARK 290   SMTRY3   7  0.000000  1.000000  0.000000       38.61000            
+REMARK 290   SMTRY1   8  0.000000  0.000000 -1.000000        0.00000            
+REMARK 290   SMTRY2   8  1.000000  0.000000  0.000000       38.61000            
+REMARK 290   SMTRY3   8  0.000000 -1.000000  0.000000       38.61000            
+REMARK 290   SMTRY1   9  0.000000  1.000000  0.000000        0.00000            
+REMARK 290   SMTRY2   9  0.000000  0.000000  1.000000        0.00000            
+REMARK 290   SMTRY3   9  1.000000  0.000000  0.000000        0.00000            
+REMARK 290   SMTRY1  10  0.000000 -1.000000  0.000000        0.00000            
+REMARK 290   SMTRY2  10  0.000000  0.000000  1.000000       38.61000            
+REMARK 290   SMTRY3  10 -1.000000  0.000000  0.000000       38.61000            
+REMARK 290   SMTRY1  11  0.000000  1.000000  0.000000       38.61000            
+REMARK 290   SMTRY2  11  0.000000  0.000000 -1.000000       38.61000            
+REMARK 290   SMTRY3  11 -1.000000  0.000000  0.000000        0.00000            
+REMARK 290   SMTRY1  12  0.000000 -1.000000  0.000000       38.61000            
+REMARK 290   SMTRY2  12  0.000000  0.000000 -1.000000        0.00000            
+REMARK 290   SMTRY3  12  1.000000  0.000000  0.000000       38.61000            
+REMARK 290   SMTRY1  13  1.000000  0.000000  0.000000       38.61000            
+REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       38.61000            
+REMARK 290   SMTRY3  13  0.000000  0.000000  1.000000       38.61000            
+REMARK 290   SMTRY1  14 -1.000000  0.000000  0.000000        0.00000            
+REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000       38.61000            
+REMARK 290   SMTRY3  14  0.000000  0.000000  1.000000        0.00000            
+REMARK 290   SMTRY1  15 -1.000000  0.000000  0.000000       38.61000            
+REMARK 290   SMTRY2  15  0.000000  1.000000  0.000000        0.00000            
+REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000        0.00000            
+REMARK 290   SMTRY1  16  1.000000  0.000000  0.000000        0.00000            
+REMARK 290   SMTRY2  16  0.000000 -1.000000  0.000000        0.00000            
+REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       38.61000            
+REMARK 290   SMTRY1  17  0.000000  0.000000  1.000000       38.61000            
+REMARK 290   SMTRY2  17  1.000000  0.000000  0.000000       38.61000            
+REMARK 290   SMTRY3  17  0.000000  1.000000  0.000000       38.61000            
+REMARK 290   SMTRY1  18  0.000000  0.000000  1.000000        0.00000            
+REMARK 290   SMTRY2  18 -1.000000  0.000000  0.000000        0.00000            
+REMARK 290   SMTRY3  18  0.000000 -1.000000  0.000000       38.61000            
+REMARK 290   SMTRY1  19  0.000000  0.000000 -1.000000        0.00000            
+REMARK 290   SMTRY2  19 -1.000000  0.000000  0.000000       38.61000            
+REMARK 290   SMTRY3  19  0.000000  1.000000  0.000000        0.00000            
+REMARK 290   SMTRY1  20  0.000000  0.000000 -1.000000       38.61000            
+REMARK 290   SMTRY2  20  1.000000  0.000000  0.000000        0.00000            
+REMARK 290   SMTRY3  20  0.000000 -1.000000  0.000000        0.00000            
+REMARK 290   SMTRY1  21  0.000000  1.000000  0.000000       38.61000            
+REMARK 290   SMTRY2  21  0.000000  0.000000  1.000000       38.61000            
+REMARK 290   SMTRY3  21  1.000000  0.000000  0.000000       38.61000            
+REMARK 290   SMTRY1  22  0.000000 -1.000000  0.000000       38.61000            
+REMARK 290   SMTRY2  22  0.000000  0.000000  1.000000        0.00000            
+REMARK 290   SMTRY3  22 -1.000000  0.000000  0.000000        0.00000            
+REMARK 290   SMTRY1  23  0.000000  1.000000  0.000000        0.00000            
+REMARK 290   SMTRY2  23  0.000000  0.000000 -1.000000        0.00000            
+REMARK 290   SMTRY3  23 -1.000000  0.000000  0.000000       38.61000            
+REMARK 290   SMTRY1  24  0.000000 -1.000000  0.000000        0.00000            
+REMARK 290   SMTRY2  24  0.000000  0.000000 -1.000000       38.61000            
+REMARK 290   SMTRY3  24  1.000000  0.000000  0.000000        0.00000            
+REMARK 290                                                                      
+REMARK 290 REMARK: NULL                                                         
+REMARK 300                                                                      
+REMARK 300 BIOMOLECULE: 1                                                       
+REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
+REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
+REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
+REMARK 300 BURIED SURFACE AREA.                                                 
+REMARK 350                                                                      
+REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
+REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
+REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
+REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
+REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
+REMARK 350                                                                      
+REMARK 350 BIOMOLECULE: 1                                                       
+REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
+REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
+REMARK 350 SOFTWARE USED: PISA                                                  
+REMARK 350 TOTAL BURIED SURFACE AREA: 1520 ANGSTROM**2                          
+REMARK 350 SURFACE AREA OF THE COMPLEX: 3380 ANGSTROM**2                        
+REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 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 900                                                                      
+REMARK 900 RELATED ENTRIES                                                      
+REMARK 900 RELATED ID: 3I3Z   RELATED DB: PDB                                   
+REMARK 999                                                                      
+REMARK 999 SEQUENCE                                                             
+REMARK 999 THE CONFLICT OF THE SEQUENCE MAY DUE TO ARTIFACT.                    
+DBREF  3I40 A    1    21  UNP    P01308   INS_HUMAN       90    110             
+DBREF  3I40 B    1    30  UNP    P01308   INS_HUMAN       25     54             
+SEQADV 3I40 ALA B   30  UNP  P01308    THR    54 SEE REMARK 999                 
+SEQRES   1 A   21  GLY ILE VAL GLU GLN CYS CYS THR SER ILE CYS SER LEU          
+SEQRES   2 A   21  TYR GLN LEU GLU ASN TYR CYS ASN                              
+SEQRES   1 B   30  PHE VAL ASN GLN HIS LEU CYS GLY SER HIS LEU VAL GLU          
+SEQRES   2 B   30  ALA LEU TYR LEU VAL CYS GLY GLU ARG GLY PHE PHE TYR          
+SEQRES   3 B   30  THR PRO LYS ALA                                              
+FORMUL   3  HOH   *35(H2 O)                                                     
+HELIX    1   1 GLY A    1  CYS A    7  1                                   7    
+HELIX    2   2 SER A   12  ASN A   18  1                                   7    
+HELIX    3   3 GLY B    8  GLY B   20  1                                  13    
+HELIX    4   4 GLU B   21  GLY B   23  5                                   3    
+SSBOND   1 CYS A    6    CYS A   11                          1555   1555  2.03  
+SSBOND   2 CYS A    7    CYS B    7                          1555   1555  2.04  
+SSBOND   3 CYS A   20    CYS B   19                          1555   1555  2.04  
+CRYST1   77.220   77.220   77.220  90.00  90.00  90.00 I 21 3       24          
+ORIGX1      1.000000  0.000000  0.000000        0.00000                         
+ORIGX2      0.000000  1.000000  0.000000        0.00000                         
+ORIGX3      0.000000  0.000000  1.000000        0.00000                         
+SCALE1      0.012950  0.000000  0.000000        0.00000                         
+SCALE2      0.000000  0.012950  0.000000        0.00000                         
+SCALE3      0.000000  0.000000  0.012950        0.00000                         
+ATOM      1  N   GLY A   1     -27.279   6.238 -12.314  1.00 45.01           N  
+ATOM      2  CA  GLY A   1     -26.249   6.028 -11.313  1.00 43.47           C  
+ATOM      3  C   GLY A   1     -25.582   4.677 -11.471  1.00 34.37           C  
+ATOM      4  O   GLY A   1     -25.731   4.023 -12.501  1.00 30.09           O  
+ATOM      5  N   ILE A   2     -24.853   4.248 -10.446  1.00 32.71           N  
+ATOM      6  CA  ILE A   2     -24.070   3.023 -10.550  1.00 22.60           C  
+ATOM      7  C   ILE A   2     -24.915   1.786 -10.840  1.00 23.32           C  
+ATOM      8  O   ILE A   2     -24.469   0.865 -11.529  1.00 26.36           O  
+ATOM      9  CB  ILE A   2     -23.208   2.791  -9.302  1.00 28.24           C  
+ATOM     10  CG1 ILE A   2     -22.249   1.620  -9.538  1.00 25.03           C  
+ATOM     11  CG2 ILE A   2     -24.090   2.579  -8.068  1.00 32.70           C  
+ATOM     12  CD1 ILE A   2     -21.209   1.479  -8.457  1.00 30.60           C  
+ATOM     13  N   VAL A   3     -26.137   1.755 -10.324  1.00 27.13           N  
+ATOM     14  CA  VAL A   3     -26.993   0.599 -10.563  1.00 30.10           C  
+ATOM     15  C   VAL A   3     -27.324   0.471 -12.049  1.00 32.71           C  
+ATOM     16  O   VAL A   3     -27.258  -0.617 -12.621  1.00 28.83           O  
+ATOM     17  CB  VAL A   3     -28.284   0.657  -9.740  1.00 30.51           C  
+ATOM     18  CG1 VAL A   3     -29.194  -0.497 -10.127  1.00 35.07           C  
+ATOM     19  CG2 VAL A   3     -27.956   0.613  -8.242  1.00 27.53           C  
+ATOM     20  N   GLU A   4     -27.669   1.596 -12.667  1.00 34.97           N  
+ATOM     21  CA  GLU A   4     -28.001   1.627 -14.086  1.00 31.24           C  
+ATOM     22  C   GLU A   4     -26.797   1.224 -14.927  1.00 32.52           C  
+ATOM     23  O   GLU A   4     -26.933   0.517 -15.924  1.00 31.47           O  
+ATOM     24  CB  GLU A   4     -28.474   3.027 -14.485  1.00 38.19           C  
+ATOM     25  CG  GLU A   4     -29.829   3.420 -13.908  1.00 61.51           C  
+ATOM     26  CD  GLU A   4     -29.832   3.535 -12.387  1.00 66.16           C  
+ATOM     27  OE1 GLU A   4     -28.868   4.094 -11.814  1.00 42.60           O  
+ATOM     28  OE2 GLU A   4     -30.812   3.071 -11.762  1.00 67.86           O  
+ATOM     29  N   GLN A   5     -25.615   1.664 -14.508  1.00 28.29           N  
+ATOM     30  CA  GLN A   5     -24.393   1.410 -15.266  1.00 31.01           C  
+ATOM     31  C   GLN A   5     -23.776   0.028 -15.056  1.00 39.69           C  
+ATOM     32  O   GLN A   5     -23.149  -0.511 -15.967  1.00 26.39           O  
+ATOM     33  CB  GLN A   5     -23.349   2.492 -14.974  1.00 25.23           C  
+ATOM     34  CG  GLN A   5     -23.818   3.887 -15.346  1.00 38.13           C  
+ATOM     35  CD  GLN A   5     -24.535   3.921 -16.693  1.00 53.62           C  
+ATOM     36  OE1 GLN A   5     -24.074   3.334 -17.674  1.00 38.85           O  
+ATOM     37  NE2 GLN A   5     -25.671   4.609 -16.741  1.00 42.57           N  
+ATOM     38  N   CYS A   6     -23.940  -0.551 -13.868  1.00 22.46           N  
+ATOM     39  CA  CYS A   6     -23.214  -1.776 -13.549  1.00 20.37           C  
+ATOM     40  C   CYS A   6     -24.114  -2.963 -13.225  1.00 18.21           C  
+ATOM     41  O   CYS A   6     -23.677  -4.107 -13.293  1.00 21.83           O  
+ATOM     42  CB  CYS A   6     -22.235  -1.524 -12.396  1.00 22.32           C  
+ATOM     43  SG  CYS A   6     -20.756  -0.602 -12.893  1.00 27.82           S  
+ATOM     44  N   CYS A   7     -25.359  -2.685 -12.860  1.00 22.16           N  
+ATOM     45  CA  CYS A   7     -26.307  -3.744 -12.520  1.00 21.25           C  
+ATOM     46  C   CYS A   7     -27.245  -4.032 -13.690  1.00 31.44           C  
+ATOM     47  O   CYS A   7     -27.307  -5.155 -14.190  1.00 24.09           O  
+ATOM     48  CB  CYS A   7     -27.119  -3.351 -11.286  1.00 22.97           C  
+ATOM     49  SG  CYS A   7     -28.355  -4.584 -10.791  1.00 28.27           S  
+ATOM     50  N   THR A   8     -27.967  -3.001 -14.122  1.00 29.15           N  
+ATOM     51  CA  THR A   8     -28.901  -3.121 -15.236  1.00 29.59           C  
+ATOM     52  C   THR A   8     -28.147  -3.334 -16.542  1.00 34.52           C  
+ATOM     53  O   THR A   8     -28.647  -3.986 -17.454  1.00 38.61           O  
+ATOM     54  CB  THR A   8     -29.780  -1.868 -15.371  1.00 31.24           C  
+ATOM     55  OG1 THR A   8     -30.023  -1.303 -14.080  1.00 41.12           O  
+ATOM     56  CG2 THR A   8     -31.100  -2.218 -16.029  1.00 51.07           C  
+ATOM     57  N   SER A   9     -26.948  -2.769 -16.630  1.00 26.15           N  
+ATOM     58  CA  SER A   9     -26.064  -3.019 -17.765  1.00 21.41           C  
+ATOM     59  C   SER A   9     -24.699  -3.529 -17.309  1.00 32.36           C  
+ATOM     60  O   SER A   9     -24.419  -3.594 -16.111  1.00 29.40           O  
+ATOM     61  CB  SER A   9     -25.910  -1.765 -18.626  1.00 32.53           C  
+ATOM     62  OG  SER A   9     -25.465  -0.670 -17.851  1.00 47.07           O  
+ATOM     63  N   ILE A  10     -23.849  -3.891 -18.261  1.00 24.43           N  
+ATOM     64  CA  ILE A  10     -22.562  -4.492 -17.924  1.00 24.22           C  
+ATOM     65  C   ILE A  10     -21.591  -3.454 -17.367  1.00 30.49           C  
+ATOM     66  O   ILE A  10     -21.420  -2.380 -17.934  1.00 26.28           O  
+ATOM     67  CB  ILE A  10     -21.942  -5.216 -19.128  1.00 26.99           C  
+ATOM     68  CG1 ILE A  10     -22.880  -6.328 -19.595  1.00 26.49           C  
+ATOM     69  CG2 ILE A  10     -20.577  -5.790 -18.770  1.00 25.10           C  
+ATOM     70  CD1 ILE A  10     -22.302  -7.179 -20.689  1.00 44.31           C  
+ATOM     71  N   CYS A  11     -20.972  -3.790 -16.240  1.00 28.14           N  
+ATOM     72  CA  CYS A  11     -20.088  -2.876 -15.534  1.00 25.92           C  
+ATOM     73  C   CYS A  11     -18.752  -2.779 -16.258  1.00 36.06           C  
+ATOM     74  O   CYS A  11     -18.491  -3.524 -17.204  1.00 27.25           O  
+ATOM     75  CB  CYS A  11     -19.867  -3.387 -14.106  1.00 23.76           C  
+ATOM     76  SG  CYS A  11     -19.406  -2.114 -12.908  1.00 28.09           S  
+ATOM     77  N   SER A  12     -17.902  -1.865 -15.807  1.00 25.78           N  
+ATOM     78  CA  SER A  12     -16.554  -1.767 -16.349  1.00 22.91           C  
+ATOM     79  C   SER A  12     -15.634  -1.220 -15.281  1.00 19.20           C  
+ATOM     80  O   SER A  12     -16.076  -0.508 -14.375  1.00 18.62           O  
+ATOM     81  CB  SER A  12     -16.530  -0.845 -17.559  1.00 24.50           C  
+ATOM     82  OG  SER A  12     -16.681   0.502 -17.157  1.00 24.75           O  
+ATOM     83  N   LEU A  13     -14.346  -1.528 -15.392  1.00 22.17           N  
+ATOM     84  CA  LEU A  13     -13.378  -1.013 -14.426  1.00 19.72           C  
+ATOM     85  C   LEU A  13     -13.412   0.508 -14.438  1.00 22.22           C  
+ATOM     86  O   LEU A  13     -13.329   1.158 -13.393  1.00 17.29           O  
+ATOM     87  CB  LEU A  13     -11.971  -1.517 -14.751  1.00 19.22           C  
+ATOM     88  CG  LEU A  13     -10.860  -0.998 -13.840  1.00 17.99           C  
+ATOM     89  CD1 LEU A  13     -11.104  -1.386 -12.388  1.00 18.06           C  
+ATOM     90  CD2 LEU A  13      -9.522  -1.530 -14.308  1.00 15.25           C  
+ATOM     91  N   TYR A  14     -13.550   1.075 -15.632  1.00 19.94           N  
+ATOM     92  CA  TYR A  14     -13.559   2.521 -15.774  1.00 22.72           C  
+ATOM     93  C   TYR A  14     -14.638   3.140 -14.893  1.00 22.64           C  
+ATOM     94  O   TYR A  14     -14.391   4.094 -14.152  1.00 25.33           O  
+ATOM     95  CB  TYR A  14     -13.771   2.911 -17.239  0.50 27.81           C  
+ATOM     97  CG  TYR A  14     -13.608   4.388 -17.494  0.50 28.31           C  
+ATOM     99  CD1 TYR A  14     -12.442   4.893 -18.059  0.50 23.25           C  
+ATOM    101  CD2 TYR A  14     -14.614   5.282 -17.153  0.50 28.36           C  
+ATOM    103  CE1 TYR A  14     -12.289   6.252 -18.283  0.50 27.32           C  
+ATOM    105  CE2 TYR A  14     -14.472   6.636 -17.372  0.50 29.32           C  
+ATOM    107  CZ  TYR A  14     -13.311   7.117 -17.938  0.50 29.06           C  
+ATOM    109  OH  TYR A  14     -13.179   8.469 -18.153  0.50 33.01           O  
+ATOM    111  N   GLN A  15     -15.837   2.584 -14.969  1.00 21.27           N  
+ATOM    112  CA  GLN A  15     -16.962   3.129 -14.222  1.00 21.51           C  
+ATOM    113  C   GLN A  15     -16.837   2.882 -12.722  1.00 17.30           C  
+ATOM    114  O   GLN A  15     -17.121   3.764 -11.917  1.00 20.82           O  
+ATOM    115  CB  GLN A  15     -18.275   2.561 -14.758  1.00 25.25           C  
+ATOM    116  CG  GLN A  15     -18.527   2.905 -16.214  1.00 32.75           C  
+ATOM    117  CD  GLN A  15     -19.997   3.039 -16.527  1.00 55.05           C  
+ATOM    118  OE1 GLN A  15     -20.680   3.914 -15.987  1.00 53.01           O  
+ATOM    119  NE2 GLN A  15     -20.497   2.177 -17.410  1.00 50.66           N  
+ATOM    120  N   LEU A  16     -16.399   1.687 -12.346  1.00 15.37           N  
+ATOM    121  CA  LEU A  16     -16.236   1.380 -10.930  1.00 17.02           C  
+ATOM    122  C   LEU A  16     -15.301   2.382 -10.273  1.00 16.55           C  
+ATOM    123  O   LEU A  16     -15.565   2.868  -9.172  1.00 19.70           O  
+ATOM    124  CB  LEU A  16     -15.703  -0.037 -10.742  1.00 24.64           C  
+ATOM    125  CG  LEU A  16     -16.709  -1.151 -11.013  1.00 24.23           C  
+ATOM    126  CD1 LEU A  16     -16.007  -2.496 -11.058  1.00 21.90           C  
+ATOM    127  CD2 LEU A  16     -17.786  -1.124  -9.936  1.00 18.48           C  
+ATOM    128  N   GLU A  17     -14.199   2.703 -10.950  1.00 17.86           N  
+ATOM    129  CA  GLU A  17     -13.219   3.608 -10.365  1.00 19.38           C  
+ATOM    130  C   GLU A  17     -13.763   5.026 -10.180  1.00 18.73           C  
+ATOM    131  O   GLU A  17     -13.259   5.782  -9.351  1.00 22.43           O  
+ATOM    132  CB  GLU A  17     -11.910   3.598 -11.155  1.00 20.40           C  
+ATOM    133  CG  GLU A  17     -11.090   2.343 -10.898  1.00 20.17           C  
+ATOM    134  CD  GLU A  17      -9.623   2.514 -11.240  1.00 22.14           C  
+ATOM    135  OE1 GLU A  17      -9.301   3.347 -12.110  1.00 22.42           O  
+ATOM    136  OE2 GLU A  17      -8.792   1.805 -10.640  1.00 27.73           O  
+ATOM    137  N   ASN A  18     -14.799   5.374 -10.932  1.00 20.29           N  
+ATOM    138  CA  ASN A  18     -15.480   6.657 -10.735  1.00 20.00           C  
+ATOM    139  C   ASN A  18     -16.080   6.766  -9.334  1.00 26.36           C  
+ATOM    140  O   ASN A  18     -16.469   7.849  -8.890  1.00 28.46           O  
+ATOM    141  CB  ASN A  18     -16.587   6.839 -11.774  1.00 21.66           C  
+ATOM    142  CG  ASN A  18     -16.061   7.344 -13.113  1.00 25.89           C  
+ATOM    143  OD1 ASN A  18     -15.007   7.974 -13.180  1.00 32.32           O  
+ATOM    144  ND2 ASN A  18     -16.802   7.070 -14.180  1.00 38.57           N  
+ATOM    145  N   TYR A  19     -16.163   5.640  -8.638  1.00 20.84           N  
+ATOM    146  CA  TYR A  19     -16.803   5.618  -7.327  1.00 18.56           C  
+ATOM    147  C   TYR A  19     -15.822   5.394  -6.180  1.00 23.20           C  
+ATOM    148  O   TYR A  19     -16.223   5.337  -5.018  1.00 27.54           O  
+ATOM    149  CB  TYR A  19     -17.945   4.599  -7.298  1.00 20.89           C  
+ATOM    150  CG  TYR A  19     -19.068   4.966  -8.236  1.00 21.62           C  
+ATOM    151  CD1 TYR A  19     -19.115   4.453  -9.521  1.00 23.43           C  
+ATOM    152  CD2 TYR A  19     -20.066   5.848  -7.844  1.00 26.68           C  
+ATOM    153  CE1 TYR A  19     -20.126   4.796 -10.385  1.00 24.39           C  
+ATOM    154  CE2 TYR A  19     -21.082   6.200  -8.708  1.00 31.02           C  
+ATOM    155  CZ  TYR A  19     -21.104   5.672  -9.979  1.00 28.36           C  
+ATOM    156  OH  TYR A  19     -22.114   6.009 -10.853  1.00 42.08           O  
+ATOM    157  N   CYS A  20     -14.534   5.281  -6.499  1.00 21.90           N  
+ATOM    158  CA  CYS A  20     -13.510   5.251  -5.459  1.00 19.66           C  
+ATOM    159  C   CYS A  20     -13.334   6.645  -4.882  1.00 28.69           C  
+ATOM    160  O   CYS A  20     -13.526   7.639  -5.585  1.00 30.53           O  
+ATOM    161  CB  CYS A  20     -12.169   4.783  -6.021  1.00 22.84           C  
+ATOM    162  SG  CYS A  20     -12.209   3.187  -6.829  1.00 22.45           S  
+ATOM    163  N   ASN A  21     -12.955   6.716  -3.609  1.00 26.51           N  
+ATOM    164  CA  ASN A  21     -12.630   7.993  -2.976  1.00 36.60           C  
+ATOM    165  C   ASN A  21     -11.279   8.511  -3.448  1.00 35.58           C  
+ATOM    166  O   ASN A  21     -10.515   7.790  -4.091  1.00 36.84           O  
+ATOM    167  CB  ASN A  21     -12.615   7.863  -1.450  1.00 34.89           C  
+ATOM    168  CG  ASN A  21     -13.978   7.548  -0.878  1.00 33.46           C  
+ATOM    169  OD1 ASN A  21     -14.107   6.726   0.029  1.00 48.60           O  
+ATOM    170  ND2 ASN A  21     -15.008   8.198  -1.408  1.00 39.53           N  
+ATOM    171  OXT ASN A  21     -10.922   9.659  -3.189  1.00 58.00           O  
+TER     172      ASN A  21                                                      
+ATOM    173  N   PHE B   1     -13.174  -9.740 -13.251  1.00 44.56           N  
+ATOM    174  CA  PHE B   1     -14.387  -9.892 -12.452  1.00 53.84           C  
+ATOM    175  C   PHE B   1     -15.310  -8.684 -12.590  1.00 44.51           C  
+ATOM    176  O   PHE B   1     -16.451  -8.715 -12.133  1.00 40.17           O  
+ATOM    177  CB  PHE B   1     -14.042 -10.126 -10.973  1.00 47.36           C  
+ATOM    178  CG  PHE B   1     -13.222  -9.024 -10.356  1.00 43.05           C  
+ATOM    179  CD1 PHE B   1     -13.816  -8.050  -9.571  1.00 39.13           C  
+ATOM    180  CD2 PHE B   1     -11.854  -8.964 -10.565  1.00 48.11           C  
+ATOM    181  CE1 PHE B   1     -13.059  -7.037  -9.008  1.00 29.34           C  
+ATOM    182  CE2 PHE B   1     -11.093  -7.959 -10.002  1.00 34.97           C  
+ATOM    183  CZ  PHE B   1     -11.696  -6.993  -9.224  1.00 36.24           C  
+ATOM    184  N   VAL B   2     -14.819  -7.623 -13.228  1.00 27.44           N  
+ATOM    185  CA  VAL B   2     -15.568  -6.367 -13.273  1.00 25.65           C  
+ATOM    186  C   VAL B   2     -16.402  -6.197 -14.541  1.00 30.55           C  
+ATOM    187  O   VAL B   2     -17.249  -5.306 -14.628  1.00 30.98           O  
+ATOM    188  CB  VAL B   2     -14.633  -5.163 -13.114  1.00 32.50           C  
+ATOM    189  CG1 VAL B   2     -14.056  -5.139 -11.705  1.00 29.74           C  
+ATOM    190  CG2 VAL B   2     -13.519  -5.227 -14.141  1.00 45.24           C  
+ATOM    191  N   ASN B   3     -16.158  -7.045 -15.528  1.00 28.57           N  
+ATOM    192  CA  ASN B   3     -16.844  -6.904 -16.806  1.00 31.00           C  
+ATOM    193  C   ASN B   3     -18.072  -7.800 -16.928  1.00 29.49           C  
+ATOM    194  O   ASN B   3     -18.115  -8.720 -17.743  1.00 28.57           O  
+ATOM    195  CB  ASN B   3     -15.854  -7.122 -17.946  1.00 31.67           C  
+ATOM    196  CG  ASN B   3     -14.703  -6.139 -17.888  1.00 35.45           C  
+ATOM    197  OD1 ASN B   3     -13.561  -6.507 -17.600  1.00 38.37           O  
+ATOM    198  ND2 ASN B   3     -15.009  -4.871 -18.113  1.00 23.34           N  
+ATOM    199  N   GLN B   4     -19.073  -7.514 -16.099  1.00 31.90           N  
+ATOM    200  CA  GLN B   4     -20.313  -8.287 -16.082  1.00 28.96           C  
+ATOM    201  C   GLN B   4     -21.397  -7.521 -15.328  1.00 23.12           C  
+ATOM    202  O   GLN B   4     -21.154  -6.432 -14.812  1.00 26.67           O  
+ATOM    203  CB  GLN B   4     -20.079  -9.648 -15.425  1.00 33.50           C  
+ATOM    204  CG  GLN B   4     -19.608  -9.556 -13.987  1.00 31.03           C  
+ATOM    205  CD  GLN B   4     -19.344 -10.918 -13.379  1.00 54.72           C  
+ATOM    206  OE1 GLN B   4     -20.210 -11.794 -13.390  1.00 51.79           O  
+ATOM    207  NE2 GLN B   4     -18.144 -11.105 -12.840  1.00 41.70           N  
+ATOM    208  N   HIS B   5     -22.599  -8.080 -15.281  1.00 25.17           N  
+ATOM    209  CA  HIS B   5     -23.666  -7.471 -14.503  1.00 26.87           C  
+ATOM    210  C   HIS B   5     -23.358  -7.685 -13.035  1.00 26.33           C  
+ATOM    211  O   HIS B   5     -23.193  -8.822 -12.595  1.00 25.34           O  
+ATOM    212  CB  HIS B   5     -25.013  -8.109 -14.834  1.00 24.65           C  
+ATOM    213  CG  HIS B   5     -25.462  -7.871 -16.239  1.00 27.43           C  
+ATOM    214  ND1 HIS B   5     -26.235  -6.787 -16.598  1.00 29.87           N  
+ATOM    215  CD2 HIS B   5     -25.241  -8.570 -17.377  1.00 27.84           C  
+ATOM    216  CE1 HIS B   5     -26.478  -6.833 -17.896  1.00 24.52           C  
+ATOM    217  NE2 HIS B   5     -25.885  -7.905 -18.393  1.00 35.03           N  
+ATOM    218  N   LEU B   6     -23.267  -6.592 -12.287  1.00 22.69           N  
+ATOM    219  CA  LEU B   6     -22.974  -6.660 -10.862  1.00 21.06           C  
+ATOM    220  C   LEU B   6     -24.052  -5.932 -10.079  1.00 21.50           C  
+ATOM    221  O   LEU B   6     -24.197  -4.715 -10.194  1.00 22.66           O  
+ATOM    222  CB  LEU B   6     -21.612  -6.034 -10.568  1.00 20.56           C  
+ATOM    223  CG  LEU B   6     -20.418  -6.665 -11.281  1.00 20.16           C  
+ATOM    224  CD1 LEU B   6     -19.190  -5.786 -11.103  1.00 20.54           C  
+ATOM    225  CD2 LEU B   6     -20.155  -8.064 -10.763  1.00 25.22           C  
+ATOM    226  N   CYS B   7     -24.800  -6.679  -9.273  1.00 20.58           N  
+ATOM    227  CA  CYS B   7     -25.899  -6.104  -8.513  1.00 22.46           C  
+ATOM    228  C   CYS B   7     -25.754  -6.421  -7.034  1.00 22.72           C  
+ATOM    229  O   CYS B   7     -25.231  -7.471  -6.665  1.00 21.90           O  
+ATOM    230  CB  CYS B   7     -27.236  -6.664  -9.009  1.00 28.16           C  
+ATOM    231  SG  CYS B   7     -27.554  -6.459 -10.788  1.00 29.45           S  
+ATOM    232  N   GLY B   8     -26.229  -5.514  -6.191  1.00 21.36           N  
+ATOM    233  CA  GLY B   8     -26.233  -5.745  -4.759  1.00 22.98           C  
+ATOM    234  C   GLY B   8     -24.859  -6.051  -4.209  1.00 20.91           C  
+ATOM    235  O   GLY B   8     -23.911  -5.316  -4.465  1.00 23.25           O  
+ATOM    236  N   SER B   9     -24.741  -7.136  -3.447  1.00 18.12           N  
+ATOM    237  CA  SER B   9     -23.484  -7.444  -2.778  1.00 15.90           C  
+ATOM    238  C   SER B   9     -22.360  -7.702  -3.780  1.00 18.45           C  
+ATOM    239  O   SER B   9     -21.183  -7.509  -3.473  1.00 17.21           O  
+ATOM    240  CB  SER B   9     -23.648  -8.663  -1.863  1.00 19.34           C  
+ATOM    241  OG  SER B   9     -23.919  -9.813  -2.638  1.00 20.35           O  
+ATOM    242  N   HIS B  10     -22.730  -8.151  -4.972  1.00 14.91           N  
+ATOM    243  CA  HIS B  10     -21.764  -8.403  -6.039  1.00 17.86           C  
+ATOM    244  C   HIS B  10     -21.093  -7.097  -6.470  1.00 18.59           C  
+ATOM    245  O   HIS B  10     -19.891  -7.055  -6.725  1.00 17.96           O  
+ATOM    246  CB  HIS B  10     -22.471  -9.047  -7.236  1.00 18.56           C  
+ATOM    247  CG  HIS B  10     -23.081 -10.384  -6.933  1.00 23.08           C  
+ATOM    248  ND1 HIS B  10     -23.461 -11.269  -7.919  1.00 27.72           N  
+ATOM    249  CD2 HIS B  10     -23.366 -10.990  -5.755  1.00 23.69           C  
+ATOM    250  CE1 HIS B  10     -23.951 -12.364  -7.363  1.00 29.56           C  
+ATOM    251  NE2 HIS B  10     -23.906 -12.220  -6.050  1.00 22.03           N  
+ATOM    252  N   LEU B  11     -21.886  -6.037  -6.550  1.00 16.34           N  
+ATOM    253  CA  LEU B  11     -21.398  -4.713  -6.938  1.00 16.50           C  
+ATOM    254  C   LEU B  11     -20.523  -4.120  -5.847  1.00 19.44           C  
+ATOM    255  O   LEU B  11     -19.446  -3.585  -6.105  1.00 17.25           O  
+ATOM    256  CB  LEU B  11     -22.588  -3.788  -7.211  1.00 16.97           C  
+ATOM    257  CG  LEU B  11     -22.268  -2.390  -7.735  1.00 22.79           C  
+ATOM    258  CD1 LEU B  11     -21.211  -2.486  -8.812  1.00 17.51           C  
+ATOM    259  CD2 LEU B  11     -23.529  -1.754  -8.277  1.00 22.41           C  
+ATOM    260  N   VAL B  12     -20.990  -4.218  -4.610  1.00 15.40           N  
+ATOM    261  CA  VAL B  12     -20.242  -3.690  -3.490  1.00 13.81           C  
+ATOM    262  C   VAL B  12     -18.902  -4.422  -3.332  1.00 15.23           C  
+ATOM    263  O   VAL B  12     -17.879  -3.825  -2.988  1.00 14.98           O  
+ATOM    264  CB  VAL B  12     -21.096  -3.776  -2.212  1.00 24.43           C  
+ATOM    265  CG1 VAL B  12     -20.252  -3.609  -1.029  1.00 30.29           C  
+ATOM    266  CG2 VAL B  12     -22.169  -2.694  -2.241  1.00 21.29           C  
+ATOM    267  N   GLU B  13     -18.912  -5.721  -3.589  1.00 14.50           N  
+ATOM    268  CA  GLU B  13     -17.695  -6.515  -3.515  1.00 14.19           C  
+ATOM    269  C   GLU B  13     -16.682  -6.056  -4.574  1.00 15.30           C  
+ATOM    270  O   GLU B  13     -15.481  -5.936  -4.304  1.00 16.00           O  
+ATOM    271  CB  GLU B  13     -18.046  -7.986  -3.712  1.00 22.91           C  
+ATOM    272  CG  GLU B  13     -16.884  -8.875  -4.073  1.00 31.68           C  
+ATOM    273  CD  GLU B  13     -17.296 -10.336  -4.139  1.00 35.29           C  
+ATOM    274  OE1 GLU B  13     -17.726 -10.873  -3.092  1.00 24.65           O  
+ATOM    275  OE2 GLU B  13     -17.204 -10.932  -5.236  1.00 35.79           O  
+ATOM    276  N   ALA B  14     -17.166  -5.811  -5.782  1.00 16.94           N  
+ATOM    277  CA  ALA B  14     -16.298  -5.308  -6.856  1.00 19.02           C  
+ATOM    278  C   ALA B  14     -15.701  -3.941  -6.523  1.00 17.95           C  
+ATOM    279  O   ALA B  14     -14.507  -3.704  -6.731  1.00 16.40           O  
+ATOM    280  CB  ALA B  14     -17.065  -5.240  -8.157  1.00 19.13           C  
+ATOM    281  N   LEU B  15     -16.536  -3.036  -6.021  1.00 15.53           N  
+ATOM    282  CA  LEU B  15     -16.066  -1.724  -5.592  1.00 13.58           C  
+ATOM    283  C   LEU B  15     -14.977  -1.846  -4.540  1.00 20.33           C  
+ATOM    284  O   LEU B  15     -13.957  -1.159  -4.594  1.00 17.96           O  
+ATOM    285  CB  LEU B  15     -17.228  -0.890  -5.054  1.00 17.56           C  
+ATOM    286  CG  LEU B  15     -18.132  -0.253  -6.108  1.00 19.95           C  
+ATOM    287  CD1 LEU B  15     -19.434   0.217  -5.476  1.00 19.70           C  
+ATOM    288  CD2 LEU B  15     -17.420   0.908  -6.806  1.00 19.43           C  
+ATOM    289  N   TYR B  16     -15.196  -2.733  -3.580  1.00 16.41           N  
+ATOM    290  CA  TYR B  16     -14.214  -2.982  -2.528  1.00 14.22           C  
+ATOM    291  C   TYR B  16     -12.884  -3.467  -3.093  1.00 18.76           C  
+ATOM    292  O   TYR B  16     -11.823  -2.978  -2.708  1.00 14.92           O  
+ATOM    293  CB  TYR B  16     -14.766  -4.015  -1.551  1.00 13.58           C  
+ATOM    294  CG  TYR B  16     -13.748  -4.582  -0.595  1.00 15.85           C  
+ATOM    295  CD1 TYR B  16     -13.213  -3.811   0.431  1.00 19.91           C  
+ATOM    296  CD2 TYR B  16     -13.338  -5.909  -0.707  1.00 14.31           C  
+ATOM    297  CE1 TYR B  16     -12.290  -4.347   1.318  1.00 18.93           C  
+ATOM    298  CE2 TYR B  16     -12.419  -6.445   0.163  1.00 16.89           C  
+ATOM    299  CZ  TYR B  16     -11.899  -5.665   1.173  1.00 19.03           C  
+ATOM    300  OH  TYR B  16     -10.991  -6.225   2.037  1.00 19.26           O  
+ATOM    301  N   LEU B  17     -12.941  -4.437  -4.002  1.00 17.26           N  
+ATOM    302  CA  LEU B  17     -11.725  -4.998  -4.583  1.00 17.15           C  
+ATOM    303  C   LEU B  17     -10.983  -3.979  -5.439  1.00 20.48           C  
+ATOM    304  O   LEU B  17      -9.751  -3.889  -5.407  1.00 20.37           O  
+ATOM    305  CB  LEU B  17     -12.060  -6.221  -5.428  1.00 16.44           C  
+ATOM    306  CG  LEU B  17     -12.491  -7.468  -4.651  1.00 17.44           C  
+ATOM    307  CD1 LEU B  17     -12.867  -8.590  -5.593  1.00 22.58           C  
+ATOM    308  CD2 LEU B  17     -11.383  -7.898  -3.717  1.00 22.13           C  
+ATOM    309  N   VAL B  18     -11.738  -3.226  -6.224  1.00 18.15           N  
+ATOM    310  CA  VAL B  18     -11.150  -2.270  -7.151  1.00 18.50           C  
+ATOM    311  C   VAL B  18     -10.557  -1.063  -6.431  1.00 22.53           C  
+ATOM    312  O   VAL B  18      -9.454  -0.628  -6.747  1.00 21.63           O  
+ATOM    313  CB  VAL B  18     -12.188  -1.824  -8.207  1.00 19.51           C  
+ATOM    314  CG1 VAL B  18     -11.714  -0.594  -8.955  1.00 28.07           C  
+ATOM    315  CG2 VAL B  18     -12.468  -2.973  -9.165  1.00 23.98           C  
+ATOM    316  N   CYS B  19     -11.268  -0.548  -5.433  1.00 19.45           N  
+ATOM    317  CA  CYS B  19     -10.874   0.709  -4.803  1.00 21.28           C  
+ATOM    318  C   CYS B  19      -9.819   0.588  -3.702  1.00 26.60           C  
+ATOM    319  O   CYS B  19      -9.167   1.576  -3.355  1.00 25.82           O  
+ATOM    320  CB  CYS B  19     -12.102   1.455  -4.285  1.00 20.90           C  
+ATOM    321  SG  CYS B  19     -13.231   1.932  -5.593  1.00 21.21           S  
+ATOM    322  N   GLY B  20      -9.653  -0.608  -3.150  1.00 25.20           N  
+ATOM    323  CA  GLY B  20      -8.606  -0.825  -2.167  1.00 33.63           C  
+ATOM    324  C   GLY B  20      -8.661   0.162  -1.014  1.00 39.29           C  
+ATOM    325  O   GLY B  20      -9.737   0.464  -0.501  1.00 27.87           O  
+ATOM    326  N   GLU B  21      -7.507   0.678  -0.599  1.00 30.38           N  
+ATOM    327  CA  GLU B  21      -7.474   1.534   0.591  1.00 34.13           C  
+ATOM    328  C   GLU B  21      -8.014   2.944   0.351  1.00 23.63           C  
+ATOM    329  O   GLU B  21      -8.123   3.737   1.283  1.00 35.45           O  
+ATOM    330  CB  GLU B  21      -6.075   1.569   1.220  1.00 45.91           C  
+ATOM    331  CG  GLU B  21      -5.015   2.280   0.401  1.00 57.50           C  
+ATOM    332  CD  GLU B  21      -3.631   2.179   1.034  1.00 75.22           C  
+ATOM    333  OE1 GLU B  21      -2.707   2.876   0.563  1.00 79.46           O  
+ATOM    334  OE2 GLU B  21      -3.470   1.401   2.002  1.00 57.31           O  
+ATOM    335  N   ARG B  22      -8.356   3.251  -0.897  1.00 27.41           N  
+ATOM    336  CA  ARG B  22      -9.040   4.498  -1.213  1.00 28.81           C  
+ATOM    337  C   ARG B  22     -10.456   4.461  -0.645  1.00 33.76           C  
+ATOM    338  O   ARG B  22     -11.008   5.480  -0.235  1.00 31.35           O  
+ATOM    339  CB  ARG B  22      -9.130   4.700  -2.726  1.00 30.48           C  
+ATOM    340  CG  ARG B  22      -7.876   5.228  -3.400  1.00 38.41           C  
+ATOM    341  CD  ARG B  22      -8.072   5.288  -4.922  1.00 44.34           C  
+ATOM    342  NE  ARG B  22      -8.003   3.963  -5.546  1.00 61.53           N  
+ATOM    343  CZ  ARG B  22      -8.246   3.711  -6.833  1.00 56.00           C  
+ATOM    344  NH1 ARG B  22      -8.151   2.467  -7.288  1.00 37.21           N  
+ATOM    345  NH2 ARG B  22      -8.588   4.690  -7.664  1.00 33.73           N  
+ATOM    346  N   GLY B  23     -11.048   3.276  -0.627  1.00 23.72           N  
+ATOM    347  CA  GLY B  23     -12.442   3.151  -0.243  1.00 25.22           C  
+ATOM    348  C   GLY B  23     -13.323   3.633  -1.376  1.00 26.84           C  
+ATOM    349  O   GLY B  23     -12.832   3.954  -2.460  1.00 20.71           O  
+ATOM    350  N   PHE B  24     -14.625   3.700  -1.132  1.00 18.98           N  
+ATOM    351  CA  PHE B  24     -15.558   4.055  -2.188  1.00 17.55           C  
+ATOM    352  C   PHE B  24     -16.875   4.561  -1.614  1.00 23.50           C  
+ATOM    353  O   PHE B  24     -17.092   4.530  -0.402  1.00 24.02           O  
+ATOM    354  CB  PHE B  24     -15.811   2.837  -3.086  1.00 17.36           C  
+ATOM    355  CG  PHE B  24     -16.428   1.661  -2.361  1.00 19.89           C  
+ATOM    356  CD1 PHE B  24     -15.628   0.691  -1.776  1.00 18.48           C  
+ATOM    357  CD2 PHE B  24     -17.811   1.527  -2.269  1.00 22.89           C  
+ATOM    358  CE1 PHE B  24     -16.189  -0.390  -1.107  1.00 21.90           C  
+ATOM    359  CE2 PHE B  24     -18.378   0.446  -1.597  1.00 19.48           C  
+ATOM    360  CZ  PHE B  24     -17.562  -0.513  -1.015  1.00 19.73           C  
+ATOM    361  N   PHE B  25     -17.742   5.048  -2.487  1.00 23.02           N  
+ATOM    362  CA  PHE B  25     -19.108   5.343  -2.088  1.00 26.05           C  
+ATOM    363  C   PHE B  25     -20.081   4.558  -2.948  1.00 29.87           C  
+ATOM    364  O   PHE B  25     -19.912   4.448  -4.158  1.00 25.71           O  
+ATOM    365  CB  PHE B  25     -19.410   6.848  -2.118  1.00 30.50           C  
+ATOM    366  CG  PHE B  25     -19.035   7.523  -3.399  1.00 36.46           C  
+ATOM    367  CD1 PHE B  25     -17.729   7.929  -3.625  1.00 41.85           C  
+ATOM    368  CD2 PHE B  25     -19.989   7.772  -4.374  1.00 47.50           C  
+ATOM    369  CE1 PHE B  25     -17.376   8.562  -4.808  1.00 51.84           C  
+ATOM    370  CE2 PHE B  25     -19.645   8.407  -5.560  1.00 37.96           C  
+ATOM    371  CZ  PHE B  25     -18.336   8.802  -5.778  1.00 47.77           C  
+ATOM    372  N   TYR B  26     -21.090   3.991  -2.301  1.00 26.11           N  
+ATOM    373  CA  TYR B  26     -22.087   3.184  -2.976  1.00 19.37           C  
+ATOM    374  C   TYR B  26     -23.429   3.866  -2.826  1.00 26.37           C  
+ATOM    375  O   TYR B  26     -23.966   3.954  -1.726  1.00 25.08           O  
+ATOM    376  CB  TYR B  26     -22.136   1.795  -2.350  1.00 18.99           C  
+ATOM    377  CG  TYR B  26     -23.255   0.930  -2.876  1.00 21.56           C  
+ATOM    378  CD1 TYR B  26     -24.280   0.506  -2.042  1.00 24.62           C  
+ATOM    379  CD2 TYR B  26     -23.285   0.533  -4.203  1.00 23.44           C  
+ATOM    380  CE1 TYR B  26     -25.304  -0.295  -2.516  1.00 26.30           C  
+ATOM    381  CE2 TYR B  26     -24.304  -0.265  -4.690  1.00 25.09           C  
+ATOM    382  CZ  TYR B  26     -25.313  -0.675  -3.842  1.00 27.86           C  
+ATOM    383  OH  TYR B  26     -26.328  -1.469  -4.320  1.00 29.25           O  
+ATOM    384  N   THR B  27     -23.960   4.365  -3.936  1.00 28.14           N  
+ATOM    385  CA  THR B  27     -25.185   5.147  -3.909  1.00 37.14           C  
+ATOM    386  C   THR B  27     -26.169   4.594  -4.936  1.00 32.53           C  
+ATOM    387  O   THR B  27     -26.193   5.035  -6.082  1.00 36.20           O  
+ATOM    388  CB  THR B  27     -24.889   6.637  -4.188  1.00 36.89           C  
+ATOM    389  OG1 THR B  27     -24.271   6.772  -5.473  1.00 57.47           O  
+ATOM    390  CG2 THR B  27     -23.936   7.182  -3.151  1.00 33.01           C  
+ATOM    391  N   PRO B  28     -26.989   3.620  -4.517  1.00 29.25           N  
+ATOM    392  CA  PRO B  28     -27.893   2.887  -5.411  1.00 32.94           C  
+ATOM    393  C   PRO B  28     -29.081   3.726  -5.872  1.00 32.76           C  
+ATOM    394  O   PRO B  28     -29.671   3.417  -6.908  1.00 36.05           O  
+ATOM    395  CB  PRO B  28     -28.401   1.730  -4.542  1.00 31.48           C  
+ATOM    396  CG  PRO B  28     -27.658   1.813  -3.247  1.00 28.54           C  
+ATOM    397  CD  PRO B  28     -27.128   3.190  -3.118  1.00 34.39           C  
+ATOM    398  N   LYS B  29     -29.436   4.751  -5.105  1.00 34.79           N  
+ATOM    399  CA  LYS B  29     -30.532   5.642  -5.483  1.00 49.07           C  
+ATOM    400  C   LYS B  29     -30.051   6.834  -6.309  1.00 63.70           C  
+ATOM    401  O   LYS B  29     -30.669   7.191  -7.315  1.00 73.47           O  
+ATOM    402  CB  LYS B  29     -31.305   6.122  -4.251  1.00 62.86           C  
+ATOM    403  CG  LYS B  29     -32.706   5.526  -4.105  1.00 74.15           C  
+ATOM    404  CD  LYS B  29     -32.690   4.118  -3.525  1.00 72.32           C  
+ATOM    405  CE  LYS B  29     -32.356   3.061  -4.572  1.00 68.55           C  
+ATOM    406  NZ  LYS B  29     -33.458   2.854  -5.553  1.00 59.40           N  
+ATOM    407  N   ALA B  30     -28.950   7.446  -5.884  1.00 72.05           N  
+ATOM    408  CA  ALA B  30     -28.366   8.568  -6.616  1.00 74.07           C  
+ATOM    409  C   ALA B  30     -27.782   8.115  -7.955  1.00 73.01           C  
+ATOM    410  O   ALA B  30     -27.485   8.928  -8.831  1.00 64.47           O  
+ATOM    411  CB  ALA B  30     -27.302   9.269  -5.772  1.00 56.14           C  
+ATOM    412  OXT ALA B  30     -27.594   6.921  -8.197  1.00 73.19           O  
+TER     413      ALA B  30                                                      
+HETATM  414  O   HOH A  22     -29.500  -7.696 -14.149  1.00 50.68           O  
+HETATM  415  O   HOH A  23     -11.374  10.214 -16.391  1.00 40.62           O  
+HETATM  416  O   HOH A  24     -11.187   9.560 -19.007  1.00 44.09           O  
+HETATM  417  O   HOH A  25     -22.708  -0.422 -18.245  1.00 25.03           O  
+HETATM  418  O   HOH A  26     -17.282   8.923   0.122  1.00 44.14           O  
+HETATM  419  O   HOH A  27     -27.802  -5.289 -20.151  1.00 41.02           O  
+HETATM  420  O   HOH A  28     -13.732   9.674 -11.684  1.00 48.35           O  
+HETATM  421  O   HOH A  29     -26.166   6.685 -14.912  1.00 50.84           O  
+HETATM  422  O   HOH A  30     -30.826  -5.812 -17.868  1.00 54.11           O  
+HETATM  423  O   HOH A  31     -14.803   9.989  -8.715  1.00 62.79           O  
+HETATM  424  O   HOH A  32     -19.609   9.964  -9.626  1.00 46.30           O  
+HETATM  425  O   HOH A  33     -13.690  11.749 -14.300  1.00 49.90           O  
+HETATM  426  O   HOH B  31     -24.729  10.263 -12.014  1.00 61.01           O  
+HETATM  427  O   HOH B  32     -20.724 -10.273 -19.319  1.00 52.72           O  
+HETATM  428  O   HOH B  33     -17.700 -13.422  -2.674  1.00 25.54           O  
+HETATM  429  O   HOH B  34     -28.494  10.301 -14.536  1.00 56.88           O  
+HETATM  430  O   HOH B  35     -24.545   6.027  -8.162  1.00 32.84           O  
+HETATM  431  O   HOH B  36     -27.182  -2.924  -7.024  1.00 27.65           O  
+HETATM  432  O   HOH B  37     -24.782  -9.599  -9.935  1.00 26.60           O  
+HETATM  433  O   HOH B  38     -14.505  -9.421 -15.869  1.00 44.83           O  
+HETATM  434  O   HOH B  39     -28.442  -1.829  -2.831  1.00 43.18           O  
+HETATM  435  O   HOH B  40     -12.046  -0.492  -0.930  1.00 25.29           O  
+HETATM  436  O   HOH B  41     -18.702  -9.557  -7.601  1.00 29.84           O  
+HETATM  437  O   HOH B  42      -8.200  -0.632  -9.134  1.00 32.65           O  
+HETATM  438  O   HOH B  43     -15.277 -10.853  -7.465  1.00 43.14           O  
+HETATM  439  O   HOH B  44     -22.107   4.402  -6.065  1.00 31.09           O  
+HETATM  440  O   HOH B  45      -5.206   0.010  -2.235  1.00 43.01           O  
+HETATM  441  O   HOH B  46     -26.729  -9.715  -6.146  1.00 30.80           O  
+HETATM  442  O   HOH B  47     -27.875   3.972  -9.042  1.00 40.15           O  
+HETATM  443  O   HOH B  48     -20.453  -7.642  -0.550  1.00 34.77           O  
+HETATM  444  O   HOH B  49     -17.760 -10.041  -0.552  1.00 37.12           O  
+HETATM  445  O   HOH B  50     -22.932 -10.505 -16.556  1.00 47.78           O  
+HETATM  446  O   HOH B  51     -28.195   5.830  -2.571  1.00 53.39           O  
+HETATM  447  O   HOH B  52     -17.118 -11.123 -18.586  1.00 52.94           O  
+HETATM  448  O   HOH B  53     -27.581   8.994 -11.659  1.00 53.89           O  
+CONECT   43   76                                                                
+CONECT   49  231                                                                
+CONECT   76   43                                                                
+CONECT  162  321                                                                
+CONECT  231   49                                                                
+CONECT  321  162                                                                
+MASTER      279    0    0    4    0    0    0    6  438    2    6    5          
+END                                                                             
diff --git a/vermouth/tests/data/integration_tests/tier-1/EN_region/martinize2/cg.pdb b/vermouth/tests/data/integration_tests/tier-1/EN_region/martinize2/cg.pdb
new file mode 100644
index 00000000..62f92b3f
--- /dev/null
+++ b/vermouth/tests/data/integration_tests/tier-1/EN_region/martinize2/cg.pdb
@@ -0,0 +1,202 @@
+ATOM      1 BB   GLY A   1     -26.214   5.188 -11.960  1.00  0.00              
+ATOM      2 BB   ILE A   2     -24.579   2.426 -10.878  1.00  0.00              
+ATOM      3 SC1  ILE A   2     -22.689   2.117  -8.841  1.00  0.00              
+ATOM      4 BB   VAL A   3     -26.923   0.510 -11.441  1.00  0.00              
+ATOM      5 SC1  VAL A   3     -28.478   0.258  -9.370  1.00  0.00              
+ATOM      6 BB   GLU A   4     -27.331   1.201 -14.450  1.00  0.00              
+ATOM      7 SC1  GLU A   4     -29.596   3.447 -12.744  1.00  0.00              
+ATOM      8 BB   GLN A   5     -24.204   0.600 -15.231  1.00  0.00              
+ATOM      9 SC1  GLN A   5     -24.318   3.659 -16.384  1.00  0.00              
+ATOM     10 BB   CYS A   6     -23.739  -2.413 -13.484  1.00  0.00              
+ATOM     11 SC1  CYS A   6     -21.159  -0.853 -12.757  1.00  0.00              
+ATOM     12 BB   CYS A   7     -26.566  -3.952 -13.363  1.00  0.00              
+ATOM     13 SC1  CYS A   7     -28.018  -4.248 -10.926  1.00  0.00              
+ATOM     14 BB   THR A   8     -28.416  -3.394 -15.895  1.00  0.00              
+ATOM     15 SC1  THR A   8     -30.273  -1.747 -15.052  1.00  0.00              
+ATOM     16 BB   SER A   9     -25.502  -3.238 -16.879  1.00  0.00              
+ATOM     17 SC1  SER A   9     -25.656  -1.139 -18.183  1.00  0.00              
+ATOM     18 BB   ILE A  10     -22.342  -3.480 -17.891  1.00  0.00              
+ATOM     19 SC1  ILE A  10     -21.925  -6.128 -19.546  1.00  0.00              
+ATOM     20 BB   CYS A  11     -19.547  -3.283 -16.373  1.00  0.00              
+ATOM     21 SC1  CYS A  11     -19.532  -2.461 -13.235  1.00  0.00              
+ATOM     22 BB   SER A  12     -16.557  -1.298 -15.386  1.00  0.00              
+ATOM     23 SC1  SER A  12     -16.616  -0.075 -17.329  1.00  0.00              
+ATOM     24 BB   LEU A  13     -13.622  -0.165 -14.373  1.00  0.00              
+ATOM     25 SC1  LEU A  13     -10.864  -1.358 -13.822  1.00  0.00              
+ATOM     26 BB   TYR A  14     -14.043   2.750 -15.061  1.00  0.00              
+ATOM     27 SC1  TYR A  14     -13.689   3.649 -17.367  1.00  0.00              
+ATOM     28 SC2  TYR A  14     -12.366   5.572 -18.171  1.00  0.00              
+ATOM     29 SC3  TYR A  14     -14.543   5.959 -17.262  1.00  0.00              
+ATOM     30 SC4  TYR A  14     -13.236   7.890 -18.061  1.00  0.00              
+ATOM     31 BB   GLN A  15     -16.690   3.121 -13.399  1.00  0.00              
+ATOM     32 SC1  GLN A  15     -19.688   2.957 -16.205  1.00  0.00              
+ATOM     33 BB   LEU A  16     -15.872   2.123 -10.630  1.00  0.00              
+ATOM     34 SC1  LEU A  16     -16.551  -1.202 -10.687  1.00  0.00              
+ATOM     35 BB   GLU A  17     -13.606   4.333 -10.175  1.00  0.00              
+ATOM     36 SC1  GLU A  17     -10.014   2.704 -11.228  1.00  0.00              
+ATOM     37 BB   ASN A  18     -15.730   6.702  -9.928  1.00  0.00              
+ATOM     38 SC1  ASN A  18     -16.058   7.347 -13.112  1.00  0.00              
+ATOM     39 BB   TYR A  19     -16.247   5.491  -6.728  1.00  0.00              
+ATOM     40 SC1  TYR A  19     -18.506   4.783  -7.767  1.00  0.00              
+ATOM     41 SC2  TYR A  19     -19.620   4.625  -9.953  1.00  0.00              
+ATOM     42 SC3  TYR A  19     -20.574   6.024  -8.276  1.00  0.00              
+ATOM     43 SC4  TYR A  19     -21.681   5.865 -10.478  1.00  0.00              
+ATOM     44 BB   CYS A  20     -13.741   6.276  -5.638  1.00  0.00              
+ATOM     45 SC1  CYS A  20     -12.198   3.622  -6.609  1.00  0.00              
+ATOM     46 BB   ASN A  21     -11.590   8.161  -3.487  1.00  0.00              
+ATOM     47 SC1  ASN A  21     -13.980   7.543  -0.874  1.00  0.00              
+ATOM     48 BB   PHE B  22     -14.889  -9.235 -12.595  1.00  0.00              
+ATOM     49 SC1  PHE B  22     -13.433  -9.308 -10.515  1.00  0.00              
+ATOM     50 SC2  PHE B  22     -12.977  -7.339  -9.231  1.00  0.00              
+ATOM     51 SC3  PHE B  22     -11.466  -8.045  -9.996  1.00  0.00              
+ATOM     52 BB   VAL B  23     -16.057  -6.340 -13.945  1.00  0.00              
+ATOM     53 SC1  VAL B  23     -14.069  -5.176 -12.987  1.00  0.00              
+ATOM     54 BB   ASN B  24     -17.316  -7.678 -16.779  1.00  0.00              
+ATOM     55 SC1  ASN B  24     -14.700  -6.138 -17.874  1.00  0.00              
+ATOM     56 BB   GLN B  25     -20.482  -7.367 -15.543  1.00  0.00              
+ATOM     57 SC1  GLN B  25     -19.481 -10.691 -13.750  1.00  0.00              
+ATOM     58 BB   HIS B  26     -23.181  -8.077 -13.813  1.00  0.00              
+ATOM     59 SC1  HIS B  26     -25.237  -7.990 -15.537  1.00  0.00              
+ATOM     60 SC2  HIS B  26     -25.588  -8.212 -17.924  1.00  0.00              
+ATOM     61 SC3  HIS B  26     -26.347  -6.808 -17.197  1.00  0.00              
+ATOM     62 BB   LEU B  27     -23.652  -5.904 -10.860  1.00  0.00              
+ATOM     63 SC1  LEU B  27     -20.344  -6.637 -10.929  1.00  0.00              
+ATOM     64 BB   CYS B  28     -25.384  -6.729  -7.834  1.00  0.00              
+ATOM     65 SC1  CYS B  28     -27.467  -6.515 -10.303  1.00  0.00              
+ATOM     66 BB   GLY B  29     -25.239  -5.626  -4.921  1.00  0.00              
+ATOM     67 BB   SER B  30     -22.878  -7.441  -3.380  1.00  0.00              
+ATOM     68 SC1  SER B  30     -23.803  -9.320  -2.306  1.00  0.00              
+ATOM     69 BB   HIS B  31     -21.310  -7.648  -6.061  1.00  0.00              
+ATOM     70 SC1  HIS B  31     -22.776  -9.716  -7.085  1.00  0.00              
+ATOM     71 SC2  HIS B  31     -23.657 -11.652  -5.914  1.00  0.00              
+ATOM     72 SC3  HIS B  31     -23.687 -11.774  -7.662  1.00  0.00              
+ATOM     73 BB   LEU B  32     -20.752  -4.590  -6.348  1.00  0.00              
+ATOM     74 SC1  LEU B  32     -22.399  -2.605  -8.009  1.00  0.00              
+ATOM     75 BB   VAL B  33     -19.438  -4.030  -3.597  1.00  0.00              
+ATOM     76 SC1  VAL B  33     -21.172  -3.360  -1.827  1.00  0.00              
+ATOM     77 BB   GLU B  34     -17.129  -6.036  -4.003  1.00  0.00              
+ATOM     78 SC1  GLU B  34     -17.435  -9.930  -4.064  1.00  0.00              
+ATOM     79 BB   ALA B  35     -15.860  -4.659  -6.467  1.00  0.00              
+ATOM     80 SC1  ALA B  35     -17.065  -5.240  -8.157  1.00  0.00              
+ATOM     81 BB   LEU B  36     -15.321  -1.924  -5.174  1.00  0.00              
+ATOM     82 SC1  LEU B  36     -18.053  -0.004  -5.861  1.00  0.00              
+ATOM     83 BB   TYR B  37     -13.465  -3.024  -2.980  1.00  0.00              
+ATOM     84 SC1  TYR B  37     -14.257  -4.298  -1.073  1.00  0.00              
+ATOM     85 SC2  TYR B  37     -12.751  -4.079   0.874  1.00  0.00              
+ATOM     86 SC3  TYR B  37     -12.878  -6.177  -0.272  1.00  0.00              
+ATOM     87 SC4  TYR B  37     -11.380  -5.985   1.667  1.00  0.00              
+ATOM     88 BB   LEU B  38     -11.290  -4.298  -4.867  1.00  0.00              
+ATOM     89 SC1  LEU B  38     -12.200  -7.544  -4.847  1.00  0.00              
+ATOM     90 BB   VAL B  39     -10.668  -1.763  -6.631  1.00  0.00              
+ATOM     91 SC1  VAL B  39     -12.123  -1.797  -8.776  1.00  0.00              
+ATOM     92 BB   CYS B  40     -10.236   0.613  -4.293  1.00  0.00              
+ATOM     93 SC1  CYS B  40     -12.923   1.802  -5.236  1.00  0.00              
+ATOM     94 BB   GLY B  41      -9.225  -0.167  -1.672  1.00  0.00              
+ATOM     95 BB   GLU B  42      -7.795   2.278   0.434  1.00  0.00              
+ATOM     96 SC1  GLU B  42      -4.051   2.070   1.072  1.00  0.00              
+ATOM     97 BB   ARG B  43      -9.760   4.457  -0.715  1.00  0.00              
+ATOM     98 SC1  ARG B  43      -8.359   5.072  -3.683  1.00  0.00              
+ATOM     99 SC2  ARG B  43      -8.247   3.708  -6.833  1.00  0.00              
+ATOM    100 BB   GLY B  44     -12.392   3.528  -1.251  1.00  0.00              
+ATOM    101 BB   PHE B  45     -16.063   4.216  -1.257  1.00  0.00              
+ATOM    102 SC1  PHE B  45     -16.270   1.964  -2.548  1.00  0.00              
+ATOM    103 SC2  PHE B  45     -16.333  -0.086  -1.292  1.00  0.00              
+ATOM    104 SC3  PHE B  45     -18.015   0.557  -1.669  1.00  0.00              
+ATOM    105 BB   PHE B  46     -19.208   4.827  -2.996  1.00  0.00              
+ATOM    106 SC1  PHE B  46     -19.132   7.352  -3.069  1.00  0.00              
+ATOM    107 SC2  PHE B  46     -17.706   8.423  -4.668  1.00  0.00              
+ATOM    108 SC3  PHE B  46     -19.449   8.303  -5.245  1.00  0.00              
+ATOM    109 BB   TYR B  47     -22.683   3.773  -2.397  1.00  0.00              
+ATOM    110 SC1  TYR B  47     -22.696   1.363  -2.613  1.00  0.00              
+ATOM    111 SC2  TYR B  47     -24.792   0.105  -2.279  1.00  0.00              
+ATOM    112 SC3  TYR B  47     -23.794   0.134  -4.447  1.00  0.00              
+ATOM    113 SC4  TYR B  47     -25.893  -1.129  -4.115  1.00  0.00              
+ATOM    114 BB   THR B  48     -25.385   4.788  -4.788  1.00  0.00              
+ATOM    115 SC1  THR B  48     -24.356   6.854  -4.391  1.00  0.00              
+ATOM    116 BB   PRO B  49     -28.449   3.421  -5.725  1.00  0.00              
+ATOM    117 SC1  PRO B  49     -27.729   2.244  -3.636  1.00  0.00              
+ATOM    118 BB   LYS B  50     -30.182   6.135  -6.111  1.00  0.00              
+ATOM    119 SC1  LYS B  50     -32.234   5.255  -3.960  1.00  0.00              
+ATOM    120 SC2  LYS B  50     -32.949   2.950  -5.100  1.00  0.00              
+ATOM    121 BB   ALA B  51     -28.005   7.972  -7.567  1.00  0.00              
+ATOM    122 SC1  ALA B  51     -27.302   9.269  -5.772  1.00  0.00              
+TER     123      ALA B  51 
+CONECT    1    2
+CONECT    2    3    4
+CONECT    4    5    6
+CONECT    6    7    8
+CONECT    8    9   10
+CONECT   10   11   12
+CONECT   11   21
+CONECT   12   13   14
+CONECT   13   16   65
+CONECT   14   15   16
+CONECT   16   17   18
+CONECT   18   19   20
+CONECT   20   21   22
+CONECT   22   23   24
+CONECT   24   25   26
+CONECT   26   27   31
+CONECT   27   28   29
+CONECT   28   29   30
+CONECT   29   30
+CONECT   31   32   33
+CONECT   33   34   35
+CONECT   35   36   37
+CONECT   37   38   39
+CONECT   39   40   44
+CONECT   40   41   42
+CONECT   41   42   43
+CONECT   42   43
+CONECT   44   45   46
+CONECT   45   93
+CONECT   46   47
+CONECT   48   49   52
+CONECT   49   50   51
+CONECT   50   51
+CONECT   52   53   54
+CONECT   54   55   56
+CONECT   56   57   58
+CONECT   58   59   62
+CONECT   59   60   61
+CONECT   60   61
+CONECT   62   63   64
+CONECT   64   65   66
+CONECT   66   67
+CONECT   67   68   69
+CONECT   69   70   73
+CONECT   70   71   72
+CONECT   71   72
+CONECT   73   74   75
+CONECT   75   76   77
+CONECT   77   78   79
+CONECT   79   80   81
+CONECT   81   82   83
+CONECT   83   84   88
+CONECT   84   85   86
+CONECT   85   86   87
+CONECT   86   87
+CONECT   88   89   90
+CONECT   90   91   92
+CONECT   92   93   94
+CONECT   94   95
+CONECT   95   96   97
+CONECT   97   98  100
+CONECT   98   99
+CONECT  100  101
+CONECT  101  102  105
+CONECT  102  103  104
+CONECT  103  104
+CONECT  105  106  109
+CONECT  106  107  108
+CONECT  107  108
+CONECT  109  110  114
+CONECT  110  111  112
+CONECT  111  112  113
+CONECT  112  113
+CONECT  114  115  116
+CONECT  116  117  118
+CONECT  118  119  121
+CONECT  119  120
+CONECT  121  122
+END   
\ No newline at end of file
diff --git a/vermouth/tests/data/integration_tests/tier-1/EN_region/martinize2/cg.top b/vermouth/tests/data/integration_tests/tier-1/EN_region/martinize2/cg.top
new file mode 100644
index 00000000..a45ed27a
--- /dev/null
+++ b/vermouth/tests/data/integration_tests/tier-1/EN_region/martinize2/cg.top
@@ -0,0 +1,9 @@
+
+#include "martini.itp"
+#include "molecule_0.itp"
+
+[ system ]
+Title of the system
+
+[ molecules ]
+molecule_0    1
diff --git a/vermouth/tests/data/integration_tests/tier-1/EN_region/martinize2/chain_A.ssd b/vermouth/tests/data/integration_tests/tier-1/EN_region/martinize2/chain_A.ssd
new file mode 100644
index 00000000..23c89214
--- /dev/null
+++ b/vermouth/tests/data/integration_tests/tier-1/EN_region/martinize2/chain_A.ssd
@@ -0,0 +1,80 @@
+==== Secondary Structure Definition by the program DSSP, CMBI version 2.0                          ==== DATE=2022-09-07        .
+REFERENCE W. KABSCH AND C.SANDER, BIOPOLYMERS 22 (1983) 2577-2637                                                              .
+                                                                                                                               .
+COMPND                                                                                                                         .
+SOURCE                                                                                                                         .
+AUTHOR                                                                                                                         .
+   51  2  0  0  0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN)                .
+  3437.6   ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2)                                                                         .
+   31 60.8   TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(J)  , SAME NUMBER PER 100 RESIDUES                              .
+    0  0.0   TOTAL NUMBER OF HYDROGEN BONDS IN     PARALLEL BRIDGES, SAME NUMBER PER 100 RESIDUES                              .
+    2  3.9   TOTAL NUMBER OF HYDROGEN BONDS IN ANTIPARALLEL BRIDGES, SAME NUMBER PER 100 RESIDUES                              .
+    0  0.0   TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-5), SAME NUMBER PER 100 RESIDUES                              .
+    0  0.0   TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-4), SAME NUMBER PER 100 RESIDUES                              .
+    0  0.0   TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-3), SAME NUMBER PER 100 RESIDUES                              .
+    0  0.0   TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-2), SAME NUMBER PER 100 RESIDUES                              .
+    0  0.0   TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-1), SAME NUMBER PER 100 RESIDUES                              .
+    0  0.0   TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+0), SAME NUMBER PER 100 RESIDUES                              .
+    0  0.0   TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+1), SAME NUMBER PER 100 RESIDUES                              .
+    2  3.9   TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES                              .
+    7 13.7   TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+3), SAME NUMBER PER 100 RESIDUES                              .
+   15 29.4   TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+4), SAME NUMBER PER 100 RESIDUES                              .
+    3  5.9   TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+5), SAME NUMBER PER 100 RESIDUES                              .
+  1  2  3  4  5  6  7  8  9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30     *** HISTOGRAMS OF ***           .
+  1  0  0  0  1  0  0  0  0  0  1  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0    RESIDUES PER ALPHA HELIX         .
+  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0    PARALLEL BRIDGES PER LADDER      .
+  1  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0    ANTIPARALLEL BRIDGES PER LADDER  .
+  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0  0    LADDERS PER SHEET                .
+  #  RESIDUE AA STRUCTURE BP1 BP2  ACC     N-H-->O    O-->H-N    N-H-->O    O-->H-N    TCO  KAPPA ALPHA  PHI   PSI    X-CA   Y-CA   Z-CA            CHAIN
+    1    1 A G     >        0   0   36      0, 0.0     4,-2.0     0, 0.0     3,-0.3   0.000 360.0 360.0 360.0-165.0  -26.2    6.0  -11.3               
+    2    2 A I  H  >> +     0   0    0     47,-0.5     4,-2.7     1,-0.2     5,-0.5   0.821 360.0  56.2 -60.2 -33.2  -24.1    3.0  -10.6               
+    3    3 A V  I  >>S+     0   0   31     46,-0.3     5,-2.6     2,-0.2     4,-2.1   0.939 109.2  46.0 -64.4 -44.8  -27.0    0.6  -10.6               
+    4    4 A E  I  45S+     0   0   90     -3,-0.3     5,-0.4     3,-0.2    -2,-0.2   0.879 119.7  41.8 -63.1 -38.5  -28.0    1.6  -14.1               
+    5    5 A Q  I  <5S+     0   0   75     -4,-2.0    -2,-0.2     3,-0.1    -1,-0.2   0.796 131.4  18.3 -81.2 -30.8  -24.4    1.4  -15.3               
+    6    6 A C  I  <>S+     0   0    0     -4,-2.7    22,-3.5    -5,-0.2     5,-0.6   0.631 131.0  34.7-120.2 -20.4  -23.2   -1.8  -13.5               
+    7    7 A C  I  <<S+     0   0   29     -4,-2.1    -3,-0.2    -5,-0.5    22,-0.1   0.856 124.8  34.5-100.1 -58.4  -26.3   -3.7  -12.5               
+    8    8 A T  T   <S+     0   0  101     -5,-2.6     2,-0.2    20,-0.1    -4,-0.2   0.807 134.0  25.5 -69.0 -31.3  -28.9   -3.1  -15.2               
+    9    9 A S  T   5S-     0   0   45     -6,-0.5    19,-0.4    -5,-0.4     2,-0.2  -0.787 107.5 -71.2-124.9 174.8  -26.1   -3.0  -17.8               
+   10   10 A I  T   5 -     0   0   99     -2,-0.2    17,-0.2    17,-0.1    -3,-0.1  -0.464  50.8-134.1 -73.5 131.2  -22.6   -4.5  -17.9               
+   11   11 A C      < -     0   0    3     15,-2.2     2,-0.3    -5,-0.6    -5,-0.1  -0.145  17.8-159.7 -75.8 172.7  -20.1   -2.9  -15.5               
+   12   12 A S     >  -     0   0   30     13,-0.1     4,-2.5     1,-0.1     5,-0.2  -0.988  31.0-118.9-151.3 155.1  -16.6   -1.8  -16.3               
+   13   13 A L  H  > S+     0   0   80     -2,-0.3     4,-2.4     1,-0.2     5,-0.2   0.902 114.6  59.2 -58.9 -39.3  -13.4   -1.0  -14.4               
+   14   14 A Y  H  > S+     0   0  180      1,-0.2     4,-0.7     2,-0.2    -1,-0.2   0.930 109.9  40.7 -55.7 -48.2  -13.6    2.5  -15.8               
+   15   15 A Q  H >4 S+     0   0   49      1,-0.2     3,-0.8     2,-0.2     4,-0.3   0.904 111.1  55.7 -71.0 -41.5  -17.0    3.1  -14.2               
+   16   16 A L  H >< S+     0   0    0     -4,-2.5     3,-2.2     1,-0.3     4,-0.2   0.919 103.6  55.6 -56.8 -43.4  -16.2    1.4  -10.9               
+   17   17 A E  H >< S+     0   0   86     -4,-2.4     3,-1.4     1,-0.3    -1,-0.3   0.757  91.5  72.1 -65.9 -21.8  -13.2    3.6  -10.4               
+   18   18 A N  T << S+     0   0   95     -3,-0.8    -1,-0.3    -4,-0.7    -2,-0.2   0.653  99.1  50.7 -61.1 -14.1  -15.5    6.7  -10.7               
+   19   19 A Y  T <  S+     0   0   36     -3,-2.2    28,-2.2    -4,-0.3    -1,-0.2   0.402  84.7 105.4-110.5   1.5  -16.8    5.6   -7.3               
+   20   20 A C  B <    A   46   0A  14     -3,-1.4    26,-0.3    26,-0.2    25,-0.1  -0.525 360.0 360.0 -73.8 150.2  -13.5    5.3   -5.5               
+   21   21 A N              0   0  140     24,-1.9    -1,-0.1    -2,-0.2    24,-0.1  -0.271 360.0 360.0 -74.3 360.0  -12.6    8.0   -3.0               
+   22        !*             0   0    0      0, 0.0     0, 0.0     0, 0.0     0, 0.0   0.000 360.0 360.0 360.0 360.0    0.0    0.0    0.0
+   23    1 B F              0   0  138      0, 0.0     3,-0.1     0, 0.0    13,-0.1   0.000 360.0 360.0 360.0  -9.3  -14.4   -9.9  -12.5               
+   24    2 B V        +     0   0   12      1,-0.2     2,-1.2    12,-0.1     4,-0.1   0.593 360.0  82.5 -95.9 -12.4  -15.6   -6.4  -13.3               
+   25    3 B N  S    S+     0   0  117    -13,-0.1     2,-0.3   -15,-0.1    -1,-0.2  -0.470  83.1  62.7 -96.5  65.8  -16.8   -6.9  -16.8               
+   26    4 B Q  S    S-     0   0   99     -2,-1.2   -15,-2.2    -3,-0.1     2,-0.5  -0.948  98.4 -59.1-164.7 177.2  -20.3   -8.3  -16.1               
+   27    5 B H        -     0   0  104     -2,-0.3     2,-0.5   -17,-0.2   -20,-0.2  -0.642  53.2-173.4 -72.4 122.5  -23.7   -7.5  -14.5               
+   28    6 B L        +     0   0    8    -22,-3.5     2,-0.3    -2,-0.5   -19,-0.1  -0.963   8.1 169.9-124.9 115.0  -23.0   -6.7  -10.9               
+   29    7 B C    >   -     0   0   54     -2,-0.5     3,-1.8   -22,-0.1     4,-0.2  -0.922  49.3 -26.0-126.0 148.7  -25.9   -6.1   -8.5               
+   30    8 B G  T >> S+     0   0   38     -2,-0.3     4,-2.1     1,-0.3     3,-0.7  -0.246 131.6   3.5  56.5-129.1  -26.2   -5.7   -4.8               
+   31    9 B S  H 3> S+     0   0   90      1,-0.3     4,-2.2     2,-0.2    -1,-0.3   0.781 130.9  60.9 -63.1 -26.7  -23.5   -7.4   -2.8               
+   32   10 B H  H <> S+     0   0  114     -3,-1.8     4,-1.7     2,-0.2    -1,-0.3   0.888 107.5  44.5 -64.4 -40.5  -21.8   -8.4   -6.0               
+   33   11 B L  H <> S+     0   0    1     -3,-0.7     4,-2.5    -4,-0.2    -2,-0.2   0.914 113.3  49.1 -70.2 -45.7  -21.4   -4.7   -6.9               
+   34   12 B V  H  X S+     0   0   50     -4,-2.1     4,-2.3     1,-0.2    -2,-0.2   0.878 109.7  53.0 -63.4 -37.0  -20.2   -3.7   -3.5               
+   35   13 B E  H  X S+     0   0  122     -4,-2.2     4,-2.4    -5,-0.2    -1,-0.2   0.913 109.4  48.6 -64.2 -43.3  -17.7   -6.5   -3.5               
+   36   14 B A  H  X S+     0   0    2     -4,-1.7     4,-2.8     2,-0.2     5,-0.3   0.921 110.4  50.7 -62.2 -45.4  -16.3   -5.3   -6.9               
+   37   15 B L  H  X S+     0   0    0     -4,-2.5     4,-2.7     1,-0.2     5,-0.2   0.916 110.7  50.3 -57.1 -44.2  -16.1   -1.7   -5.6               
+   38   16 B Y  H  X S+     0   0  156     -4,-2.3     4,-1.4     1,-0.2    -2,-0.2   0.923 113.6  43.9 -59.9 -47.1  -14.2   -3.0   -2.5               
+   39   17 B L  H  < S+     0   0   92     -4,-2.4    -2,-0.2     1,-0.2    -1,-0.2   0.897 118.5  43.5 -66.5 -42.1  -11.7   -5.0   -4.6               
+   40   18 B V  H  < S+     0   0   20     -4,-2.8    -2,-0.2    -5,-0.2    -1,-0.2   0.915 116.1  44.6 -71.8 -42.4  -11.2   -2.3   -7.2               
+   41   19 B C  H >< S+     0   0    3     -4,-2.7     3,-1.9    -5,-0.3     4,-0.4   0.687  80.0 175.3 -84.1 -19.4  -10.9    0.7   -4.8               
+   42   20 B G  G ><  -     0   0   44     -4,-1.4     3,-1.4     1,-0.3    -1,-0.2  -0.148  68.8  -7.1  53.5-137.1   -8.6   -0.8   -2.2               
+   43   21 B E  G 3  S+     0   0  206      1,-0.3    -1,-0.3     2,-0.0    -2,-0.1   0.553 126.1  72.4 -75.5  -4.4   -7.5    1.5    0.6               
+   44   22 B R  G <  S-     0   0  120     -3,-1.9    -1,-0.3     1,-0.1    -2,-0.2   0.828  90.7-156.9 -68.8 -33.4   -9.0    4.5   -1.2               
+   45   23 B G    <   -     0   0   24     -3,-1.4   -24,-1.9    -4,-0.4     2,-0.3  -0.256   5.7-129.0  75.4-173.9  -12.4    3.2   -0.2               
+   46   24 B F  B     -A   20   0A  58    -26,-0.3     2,-0.4    -3,-0.1   -26,-0.2  -0.942   4.0-113.2-159.3 172.9  -15.6    4.1   -2.2               
+   47   25 B F        -     0   0   91    -28,-2.2     2,-0.6    -2,-0.3    -2,-0.0  -0.993  19.4-159.4-122.1 136.5  -19.1    5.3   -2.1               
+   48   26 B Y        +     0   0   80     -2,-0.4    -2,-0.0   -46,-0.0   -14,-0.0  -0.951  16.5 169.2-116.9 111.8  -22.1    3.2   -3.0               
+   49   27 B T        +     0   0   46     -2,-0.6   -47,-0.5     1,-0.1   -46,-0.3  -0.802   6.9 172.6-129.3  88.6  -25.2    5.1   -3.9               
+   50   28 B P  S    S+     0   0   46      0, 0.0   -47,-0.1     0, 0.0    -1,-0.1   0.704  83.8  40.4 -72.5 -23.6  -27.9    2.9   -5.4               
+   51   29 B K              0   0  188      1,-0.1    -2,-0.1   -48,-0.1     0, 0.0   0.853 360.0 360.0 -90.6 -44.3  -30.5    5.6   -5.5               
+   52   30 B A              0   0   95    -51,-0.0    -1,-0.1   -49,-0.0    -3,-0.0   0.650 360.0 360.0 -68.5 360.0  -28.4    8.6   -6.6               
diff --git a/vermouth/tests/data/integration_tests/tier-1/EN_region/martinize2/citation b/vermouth/tests/data/integration_tests/tier-1/EN_region/martinize2/citation
new file mode 100644
index 00000000..ddb39213
--- /dev/null
+++ b/vermouth/tests/data/integration_tests/tier-1/EN_region/martinize2/citation
@@ -0,0 +1,1 @@
+Souza, P C T; Alessandri, R; Barnoud, J; Thallmair, S; Faustino, I; Grünewald, F; Patmanidis, I; Abdizadeh, H; Bruininks, B M H; Wassenaar, T A; Kroon, P C; Melcr, J; Nieto, V; Corradi, V; Khan, H M; Domański, J; Javanainen, M; Martinez-Seara, H; Reuter, N; Best, R B; Vattulainen, I; Monticelli, L; Periole, X; Tieleman, D P; de Vries, A H; Marrink, S J;  Nature Methods 2021; 10.1038/s41592-021-01098-3
diff --git a/vermouth/tests/data/integration_tests/tier-1/EN_region/martinize2/command b/vermouth/tests/data/integration_tests/tier-1/EN_region/martinize2/command
new file mode 100644
index 00000000..0d039f13
--- /dev/null
+++ b/vermouth/tests/data/integration_tests/tier-1/EN_region/martinize2/command
@@ -0,0 +1,1 @@
+martinize2 -f ../aa.pdb -o cg.top -x cg.pdb -dssp dssp -p backbone -ff martini3001 -scfix -cys auto -ignore HOH -elastic -eunit 8:18
diff --git a/vermouth/tests/data/integration_tests/tier-1/EN_region/martinize2/molecule_0.itp b/vermouth/tests/data/integration_tests/tier-1/EN_region/martinize2/molecule_0.itp
new file mode 100644
index 00000000..0b3e517e
--- /dev/null
+++ b/vermouth/tests/data/integration_tests/tier-1/EN_region/martinize2/molecule_0.itp
@@ -0,0 +1,755 @@
+; This file was generated using the following command:
+; /coarse/fabian/current-projects/polymer_itp_builder/vermouth_dev/venv_py38/bin/martinize2 -f ../aa.pdb -o cg.top -x cg.pdb -dssp dssp -p backbone -ff martini3001 -scfix -cys auto -ignore HOH -elastic -eunit 8:18
+; martinize with vermouth 0.7.3.dev30
+; The following sequence of secondary structure 
+; was used for the full system:
+; CHIIIIITTTCCHHHHHTTBCCCSSCCCTHHHHHHHHHHHGGGCBCCCSCC
+
+; Pleas cite the following papers:
+; Souza, P C T; Alessandri, R; Barnoud, J; Thallmair, S; Faustino, I; Grünewald, F; Patmanidis, I; Abdizadeh, H; Bruininks, B M H; Wassenaar, T A; Kroon, P C; Melcr, J; Nieto, V; Corradi, V; Khan, H M; Domański, J; Javanainen, M; Martinez-Seara, H; Reuter, N; Best, R B; Vattulainen, I; Monticelli, L; Periole, X; Tieleman, D P; de Vries, A H; Marrink, S J;  Nature Methods 2021; 10.1038/s41592-021-01098-3
+
+[ moleculetype ]
+molecule_0 1
+
+[ atoms ]
+  1 Q5    1 GLY BB    1    1 
+  2 P2    2 ILE BB    2  0.0 
+  3 SC2   2 ILE SC1   3  0.0 
+  4 SP2   3 VAL BB    4  0.0 
+  5 SC3   3 VAL SC1   5  0.0 
+  6 P2    4 GLU BB    6  0.0 
+  7 Q5n   4 GLU SC1   7 -1.0 
+  8 P2    5 GLN BB    8  0.0 
+  9 P5    5 GLN SC1   9  0.0 
+ 10 P2    6 CYS BB   10  0.0 
+ 11 TC6   6 CYS SC1  11  0.0 
+ 12 P2    7 CYS BB   12  0.0 
+ 13 TC6   7 CYS SC1  13  0.0 
+ 14 P2    8 THR BB   14  0.0 
+ 15 SP1   8 THR SC1  15  0.0 
+ 16 P2    9 SER BB   16  0.0 
+ 17 TP1   9 SER SC1  17  0.0 
+ 18 P2   10 ILE BB   18  0.0 
+ 19 SC2  10 ILE SC1  19  0.0 
+ 20 P2   11 CYS BB   20  0.0 
+ 21 TC6  11 CYS SC1  21  0.0 
+ 22 P2   12 SER BB   22  0.0 
+ 23 TP1  12 SER SC1  23  0.0 
+ 24 P2   13 LEU BB   24  0.0 
+ 25 SC2  13 LEU SC1  25  0.0 
+ 26 P2   14 TYR BB   26  0.0 
+ 27 TC4  14 TYR SC1  27  0.0 
+ 28 TC5  14 TYR SC2  28  0.0 
+ 29 TC5  14 TYR SC3  29  0.0 
+ 30 TN6  14 TYR SC4  30  0.0 
+ 31 P2   15 GLN BB   31  0.0 
+ 32 P5   15 GLN SC1  32  0.0 
+ 33 P2   16 LEU BB   33  0.0 
+ 34 SC2  16 LEU SC1  34  0.0 
+ 35 P2   17 GLU BB   35  0.0 
+ 36 Q5n  17 GLU SC1  36 -1.0 
+ 37 P2   18 ASN BB   37  0.0 
+ 38 SP5  18 ASN SC1  38  0.0 
+ 39 P2   19 TYR BB   39  0.0 
+ 40 TC4  19 TYR SC1  40  0.0 
+ 41 TC5  19 TYR SC2  41  0.0 
+ 42 TC5  19 TYR SC3  42  0.0 
+ 43 TN6  19 TYR SC4  43  0.0 
+ 44 P2   20 CYS BB   44  0.0 
+ 45 TC6  20 CYS SC1  45  0.0 
+ 46 Q5   21 ASN BB   46   -1 
+ 47 SP5  21 ASN SC1  47  0.0 
+ 48 Q5   22 PHE BB   48    1 
+ 49 SC4  22 PHE SC1  49  0.0 
+ 50 TC5  22 PHE SC2  50  0.0 
+ 51 TC5  22 PHE SC3  51  0.0 
+ 52 SP2  23 VAL BB   52  0.0 
+ 53 SC3  23 VAL SC1  53  0.0 
+ 54 P2   24 ASN BB   54  0.0 
+ 55 SP5  24 ASN SC1  55  0.0 
+ 56 P2   25 GLN BB   56  0.0 
+ 57 P5   25 GLN SC1  57  0.0 
+ 58 P2   26 HIS BB   58  0.0 
+ 59 TC4  26 HIS SC1  59  0.0 
+ 60 TN6d 26 HIS SC2  60  0.0 
+ 61 TN5a 26 HIS SC3  61  0.0 
+ 62 P2   27 LEU BB   62  0.0 
+ 63 SC2  27 LEU SC1  63  0.0 
+ 64 P2   28 CYS BB   64  0.0 
+ 65 TC6  28 CYS SC1  65  0.0 
+ 66 SP1  29 GLY BB   66  0.0 
+ 67 P2   30 SER BB   67  0.0 
+ 68 TP1  30 SER SC1  68  0.0 
+ 69 P2   31 HIS BB   69  0.0 
+ 70 TC4  31 HIS SC1  70  0.0 
+ 71 TN6d 31 HIS SC2  71  0.0 
+ 72 TN5a 31 HIS SC3  72  0.0 
+ 73 P2   32 LEU BB   73  0.0 
+ 74 SC2  32 LEU SC1  74  0.0 
+ 75 SP2  33 VAL BB   75  0.0 
+ 76 SC3  33 VAL SC1  76  0.0 
+ 77 P2   34 GLU BB   77  0.0 
+ 78 Q5n  34 GLU SC1  78 -1.0 
+ 79 SP2  35 ALA BB   79  0.0 
+ 80 TC3  35 ALA SC1  80  0.0 
+ 81 P2   36 LEU BB   81  0.0 
+ 82 SC2  36 LEU SC1  82  0.0 
+ 83 P2   37 TYR BB   83  0.0 
+ 84 TC4  37 TYR SC1  84  0.0 
+ 85 TC5  37 TYR SC2  85  0.0 
+ 86 TC5  37 TYR SC3  86  0.0 
+ 87 TN6  37 TYR SC4  87  0.0 
+ 88 P2   38 LEU BB   88  0.0 
+ 89 SC2  38 LEU SC1  89  0.0 
+ 90 SP2  39 VAL BB   90  0.0 
+ 91 SC3  39 VAL SC1  91  0.0 
+ 92 P2   40 CYS BB   92  0.0 
+ 93 TC6  40 CYS SC1  93  0.0 
+ 94 SP1  41 GLY BB   94  0.0 
+ 95 P2   42 GLU BB   95  0.0 
+ 96 Q5n  42 GLU SC1  96 -1.0 
+ 97 P2   43 ARG BB   97  0.0 
+ 98 SC3  43 ARG SC1  98  0.0 
+ 99 SQ3p 43 ARG SC2  99  1.0 
+100 SP1  44 GLY BB  100  0.0 
+101 P2   45 PHE BB  101  0.0 
+102 SC4  45 PHE SC1 102  0.0 
+103 TC5  45 PHE SC2 103  0.0 
+104 TC5  45 PHE SC3 104  0.0 
+105 P2   46 PHE BB  105  0.0 
+106 SC4  46 PHE SC1 106  0.0 
+107 TC5  46 PHE SC2 107  0.0 
+108 TC5  46 PHE SC3 108  0.0 
+109 P2   47 TYR BB  109  0.0 
+110 TC4  47 TYR SC1 110  0.0 
+111 TC5  47 TYR SC2 111  0.0 
+112 TC5  47 TYR SC3 112  0.0 
+113 TN6  47 TYR SC4 113  0.0 
+114 P2   48 THR BB  114  0.0 
+115 SP1  48 THR SC1 115  0.0 
+116 SP2a 49 PRO BB  116  0.0 
+117 SC3  49 PRO SC1 117  0.0 
+118 P2   50 LYS BB  118  0.0 
+119 SC3  50 LYS SC1 119  0.0 
+120 SQ4p 50 LYS SC2 120  1.0 
+121 Q5   51 ALA BB  121   -1 
+122 TC3  51 ALA SC1 122  0.0 
+
+[ position_restraints ]
+#ifdef POSRES
+  1 1 1000 1000 1000
+  2 1 1000 1000 1000
+  4 1 1000 1000 1000
+  6 1 1000 1000 1000
+  8 1 1000 1000 1000
+ 10 1 1000 1000 1000
+ 12 1 1000 1000 1000
+ 14 1 1000 1000 1000
+ 16 1 1000 1000 1000
+ 18 1 1000 1000 1000
+ 20 1 1000 1000 1000
+ 22 1 1000 1000 1000
+ 24 1 1000 1000 1000
+ 26 1 1000 1000 1000
+ 31 1 1000 1000 1000
+ 33 1 1000 1000 1000
+ 35 1 1000 1000 1000
+ 37 1 1000 1000 1000
+ 39 1 1000 1000 1000
+ 44 1 1000 1000 1000
+ 46 1 1000 1000 1000
+ 48 1 1000 1000 1000
+ 52 1 1000 1000 1000
+ 54 1 1000 1000 1000
+ 56 1 1000 1000 1000
+ 58 1 1000 1000 1000
+ 62 1 1000 1000 1000
+ 64 1 1000 1000 1000
+ 66 1 1000 1000 1000
+ 67 1 1000 1000 1000
+ 69 1 1000 1000 1000
+ 73 1 1000 1000 1000
+ 75 1 1000 1000 1000
+ 77 1 1000 1000 1000
+ 79 1 1000 1000 1000
+ 81 1 1000 1000 1000
+ 83 1 1000 1000 1000
+ 88 1 1000 1000 1000
+ 90 1 1000 1000 1000
+ 92 1 1000 1000 1000
+ 94 1 1000 1000 1000
+ 95 1 1000 1000 1000
+ 97 1 1000 1000 1000
+100 1 1000 1000 1000
+101 1 1000 1000 1000
+105 1 1000 1000 1000
+109 1 1000 1000 1000
+114 1 1000 1000 1000
+116 1 1000 1000 1000
+118 1 1000 1000 1000
+121 1 1000 1000 1000
+#endif
+
+[ bonds ]
+; Backbone bonds
+ 14  16 1 0.350 4000
+ 16  18 1 0.350 4000
+ 18  20 1 0.350 4000
+ 20  22 1 0.350 4000
+ 37  39 1 0.350 4000
+ 39  44 1 0.350 4000
+ 44  46 1 0.350 4000
+ 48  52 1 0.350 4000
+ 52  54 1 0.350 4000
+ 54  56 1 0.350 4000
+ 56  58 1 0.350 4000
+ 58  62 1 0.350 4000
+ 62  64 1 0.350 4000
+ 64  66 1 0.350 4000
+100 101 1 0.350 4000
+101 105 1 0.350 4000
+105 109 1 0.350 4000
+109 114 1 0.350 4000
+114 116 1 0.350 4000
+116 118 1 0.350 4000
+118 121 1 0.350 4000
+
+; Rubber band
+ 14  20 1 0.88825 500.0
+ 20  26 1 0.82714 500.0
+ 20  31 1 0.76172 500.0
+ 20  33 1 0.87015 500.0
+ 22  31 1 0.48467 500.0
+ 22  33 1 0.58986 500.0
+ 22  35 1 0.82201 500.0
+ 24  33 1 0.49302 500.0
+ 24  35 1 0.61525 500.0
+ 24  37 1 0.84473 500.0
+ 24  90 1 0.84391 500.0
+ 26  35 1 0.51543 500.0
+ 26  37 1 0.6694 500.0
+ 31  37 1 0.50787 500.0
+ 33  79 1 0.79586 500.0
+ 33  81 1 0.68158 500.0
+ 33  90 1 0.76272 500.0
+ 35  81 1 0.81914 500.0
+ 35  90 1 0.76386 500.0
+ 66  73 1 0.4821 500.0
+ 66  75 1 0.61604 500.0
+ 66  77 1 0.81712 500.0
+ 67  75 1 0.48496 500.0
+ 67  77 1 0.59509 500.0
+ 67  79 1 0.81562 500.0
+ 69  77 1 0.49312 500.0
+ 69  79 1 0.62294 500.0
+ 69  81 1 0.83323 500.0
+ 73  79 1 0.48939 500.0
+ 73  81 1 0.61629 500.0
+ 73  83 1 0.81794 500.0
+ 75  81 1 0.48859 500.0
+ 75  83 1 0.60888 500.0
+ 75  88 1 0.82503 500.0
+ 77  83 1 0.48527 500.0
+ 77  88 1 0.6153 500.0
+ 77  90 1 0.81796 500.0
+ 79  88 1 0.48547 500.0
+ 79  90 1 0.59471 500.0
+ 81  90 1 0.48783 500.0
+
+; Side chain bonds
+  6   7 1 0.400 5000
+  8   9 1 0.400 5000
+ 10  11 1 0.341 7500
+ 12  13 1 0.341 7500
+ 16  17 1 0.287 7500
+ 20  21 1 0.341 7500
+ 22  23 1 0.287 7500
+ 24  25 1 0.363 7500
+ 26  27 1 0.325 5000
+ 31  32 1 0.400 5000
+ 33  34 1 0.363 7500
+ 35  36 1 0.400 5000
+ 37  38 1 0.352 5000
+ 39  40 1 0.325 5000
+ 44  45 1 0.341 7500
+ 46  47 1 0.352 5000
+ 48  49 1 0.325 7500
+ 54  55 1 0.352 5000
+ 56  57 1 0.400 5000
+ 58  59 1 0.336 7500
+ 62  63 1 0.363 7500
+ 64  65 1 0.341 7500
+ 67  68 1 0.287 7500
+ 69  70 1 0.336 7500
+ 73  74 1 0.363 7500
+ 77  78 1 0.400 5000
+ 81  82 1 0.363 7500
+ 83  84 1 0.325 5000
+ 88  89 1 0.363 7500
+ 92  93 1 0.341 7500
+ 95  96 1 0.400 5000
+ 97  98 1 0.330 5000
+ 98  99 1 0.380 5000
+101 102 1 0.325 7500
+105 106 1 0.325 7500
+109 110 1 0.325 5000
+116 117 1 0.330 7500
+118 119 1 0.330 5000
+119 120 1 0.360 5000
+
+#ifdef FLEXIBLE
+; Side chain bonds
+  2   3 1 0.341 1000000
+  4   5 1 0.292 1000000
+ 14  15 1 0.305 1000000
+ 18  19 1 0.341 1000000
+ 27  28 1 0.300 1000000
+ 27  29 1 0.300 1000000
+ 28  30 1 0.285 1000000
+ 29  30 1 0.285 1000000
+ 28  29 1 0.300 1000000
+ 40  41 1 0.300 1000000
+ 40  42 1 0.300 1000000
+ 41  43 1 0.285 1000000
+ 42  43 1 0.285 1000000
+ 41  42 1 0.300 1000000
+ 49  50 1 0.340 1000000
+ 49  51 1 0.340 1000000
+ 50  51 1 0.290 1000000
+ 52  53 1 0.292 1000000
+ 59  60 1 0.320 1000000
+ 59  61 1 0.300 1000000
+ 60  61 1 0.270 1000000
+ 70  71 1 0.320 1000000
+ 70  72 1 0.300 1000000
+ 71  72 1 0.270 1000000
+ 75  76 1 0.292 1000000
+ 79  80 1 0.270 1000000
+ 84  85 1 0.300 1000000
+ 84  86 1 0.300 1000000
+ 85  87 1 0.285 1000000
+ 86  87 1 0.285 1000000
+ 85  86 1 0.300 1000000
+ 90  91 1 0.292 1000000
+102 103 1 0.340 1000000
+102 104 1 0.340 1000000
+103 104 1 0.290 1000000
+106 107 1 0.340 1000000
+106 108 1 0.340 1000000
+107 108 1 0.290 1000000
+110 111 1 0.300 1000000
+110 112 1 0.300 1000000
+111 113 1 0.285 1000000
+112 113 1 0.285 1000000
+111 112 1 0.300 1000000
+114 115 1 0.305 1000000
+121 122 1 0.270 1000000
+#endif
+
+[ constraints ]
+ 11  21 1 0.24 ; Disulfide bridge
+ 13  65 1 0.24 ; Disulfide bridge
+ 45  93 1 0.24 ; Disulfide bridge
+
+; Backbone bonds
+  1   2 1 0.33
+  2   4 1 0.310
+  4   6 1 0.310
+  6   8 1 0.310
+  8  10 1 0.310
+ 10  12 1 0.310
+ 12  14 1 0.33
+ 22  24 1 0.33
+ 24  26 1 0.310
+ 26  31 1 0.310
+ 31  33 1 0.310
+ 33  35 1 0.310
+ 35  37 1 0.33
+ 66  67 1 0.33
+ 67  69 1 0.310
+ 69  73 1 0.310
+ 73  75 1 0.310
+ 75  77 1 0.310
+ 77  79 1 0.310
+ 79  81 1 0.310
+ 81  83 1 0.310
+ 83  88 1 0.310
+ 88  90 1 0.310
+ 90  92 1 0.310
+ 92  94 1 0.310
+ 94  95 1 0.310
+ 95  97 1 0.310
+ 97 100 1 0.33
+
+#ifndef FLEXIBLE
+; Side chain bonds
+  2   3 1 0.341
+  4   5 1 0.292
+ 14  15 1 0.305
+ 18  19 1 0.341
+ 27  28 1 0.300
+ 27  29 1 0.300
+ 28  30 1 0.285
+ 29  30 1 0.285
+ 28  29 1 0.300
+ 40  41 1 0.300
+ 40  42 1 0.300
+ 41  43 1 0.285
+ 42  43 1 0.285
+ 41  42 1 0.300
+ 49  50 1 0.340
+ 49  51 1 0.340
+ 50  51 1 0.290
+ 52  53 1 0.292
+ 59  60 1 0.320
+ 59  61 1 0.300
+ 60  61 1 0.270
+ 70  71 1 0.320
+ 70  72 1 0.300
+ 71  72 1 0.270
+ 75  76 1 0.292
+ 79  80 1 0.270
+ 84  85 1 0.300
+ 84  86 1 0.300
+ 85  87 1 0.285
+ 86  87 1 0.285
+ 85  86 1 0.300
+ 90  91 1 0.292
+102 103 1 0.340
+102 104 1 0.340
+103 104 1 0.290
+106 107 1 0.340
+106 108 1 0.340
+107 108 1 0.290
+110 111 1 0.300
+110 112 1 0.300
+111 113 1 0.285
+112 113 1 0.285
+111 112 1 0.300
+114 115 1 0.305
+121 122 1 0.270
+#endif
+
+[ angles ]
+; BBB angles
+  1   2   4 10 127 20
+  2   4   6 2 96 700
+  4   6   8 2 96 700
+  6   8  10 2 96 700
+  8  10  12 2 96 700
+ 10  12  14 10 100 20
+ 12  14  16 10 100 20
+ 20  22  24 10 127 20
+ 22  24  26 10 127 20
+ 24  26  31 2 96 700
+ 26  31  33 2 96 700
+ 31  33  35 2 96 700
+ 33  35  37 10 100 20
+ 35  37  39 10 100 20
+ 64  66  67 10 100 20
+ 66  67  69 10 100 20
+ 67  69  73 2 96 700
+ 69  73  75 2 96 700
+ 73  75  77 2 96 700
+ 75  77  79 2 96 700
+ 77  79  81 2 96 700
+ 79  81  83 2 96 700
+ 81  83  88 2 96 700
+ 83  88  90 2 96 700
+ 88  90  92 2 96 700
+ 90  92  94 2 96 700
+ 92  94  95 2 96 700
+ 94  95  97 2 96 700
+ 95  97 100 10 127 20
+ 97 100 101 10 127 20
+ 37  39  44 10 100 20
+ 39  44  46 10 100 20
+100 101 105 10 127 20
+101 105 109 10 127 20
+109 114 116 10 127 20
+114 116 118 10 127 20
+116 118 121 10 127 20
+ 48  52  54 10 127 20
+ 52  54  56 10 127 20
+ 54  56  58 10 127 20
+ 56  58  62 10 127 20
+ 16  18  20 10 100 20
+ 18  20  22 10 100 20
+ 58  62  64 10 127 20
+ 62  64  66 10 100 20
+105 109 114 10 127 20
+ 14  16  18 10 100 20
+
+; BBS angles regular martini
+  1   2   3 2 100 25
+  2   4   5 2 100 25
+  4   6   7 2 100 25
+  6   8   9 2 100 25
+  8  10  11 2 100 25
+ 10  12  13 2 100 25
+ 12  14  15 2 100 25
+ 14  16  17 2 100 25
+ 16  18  19 2 100 25
+ 18  20  21 2 100 25
+ 20  22  23 2 100 25
+ 22  24  25 2 100 25
+ 24  26  27 2 100 25
+ 26  31  32 2 100 25
+ 31  33  34 2 100 25
+ 33  35  36 2 100 25
+ 35  37  38 2 100 25
+ 37  39  40 2 100 25
+ 39  44  45 2 100 25
+ 44  46  47 2 100 25
+ 48  52  53 2 100 25
+ 52  54  55 2 100 25
+ 54  56  57 2 100 25
+ 56  58  59 2 100 25
+ 58  62  63 2 100 25
+ 62  64  65 2 100 25
+ 66  67  68 2 100 25
+ 67  69  70 2 100 25
+ 69  73  74 2 100 25
+ 73  75  76 2 100 25
+ 75  77  78 2 100 25
+ 77  79  80 2 100 25
+ 79  81  82 2 100 25
+ 81  83  84 2 100 25
+ 83  88  89 2 100 25
+ 88  90  91 2 100 25
+ 90  92  93 2 100 25
+ 94  95  96 2 100 25
+ 95  97  98 2 100 25
+100 101 102 2 100 25
+101 105 106 2 100 25
+105 109 110 2 100 25
+109 114 115 2 100 25
+114 116 117 2 100 25
+116 118 119 2 100 25
+118 121 122 2 100 25
+
+; First SBB regular martini
+ 49  48  52 2 100 25
+
+; SC-BB-BB and BB-BB-SC scFix
+  3   2   4 10 100 15 ; SC-BB-BB
+  5   4   6 10 100 15 ; SC-BB-BB
+  7   6   8 10 100 15 ; SC-BB-BB
+  9   8  10 10 100 15 ; SC-BB-BB
+ 11  10  12 10 100 15 ; SC-BB-BB
+ 13  12  14 10 100 15 ; SC-BB-BB
+ 15  14  16 10 100 15 ; SC-BB-BB
+ 17  16  18 10 100 15 ; SC-BB-BB
+ 19  18  20 10 100 15 ; SC-BB-BB
+ 21  20  22 10 100 15 ; SC-BB-BB
+ 23  22  24 10 100 15 ; SC-BB-BB
+ 25  24  26 10 100 15 ; SC-BB-BB
+ 27  26  31 10 100 15 ; SC-BB-BB
+ 32  31  33 10 100 15 ; SC-BB-BB
+ 34  33  35 10 100 15 ; SC-BB-BB
+ 36  35  37 10 100 15 ; SC-BB-BB
+ 38  37  39 10 100 15 ; SC-BB-BB
+ 40  39  44 10 100 15 ; SC-BB-BB
+ 45  44  46 10 100 15 ; SC-BB-BB
+ 49  48  52 10 100 15 ; SC-BB-BB
+ 53  52  54 10 100 15 ; SC-BB-BB
+ 55  54  56 10 100 15 ; SC-BB-BB
+ 57  56  58 10 100 15 ; SC-BB-BB
+ 59  58  62 10 100 15 ; SC-BB-BB
+ 63  62  64 10 100 15 ; SC-BB-BB
+ 65  64  66 10 100 15 ; SC-BB-BB
+ 68  67  69 10 100 15 ; SC-BB-BB
+ 70  69  73 10 100 15 ; SC-BB-BB
+ 74  73  75 10 100 15 ; SC-BB-BB
+ 76  75  77 10 100 15 ; SC-BB-BB
+ 78  77  79 10 100 15 ; SC-BB-BB
+ 80  79  81 10 100 15 ; SC-BB-BB
+ 82  81  83 10 100 15 ; SC-BB-BB
+ 84  83  88 10 100 15 ; SC-BB-BB
+ 89  88  90 10 100 15 ; SC-BB-BB
+ 91  90  92 10 100 15 ; SC-BB-BB
+ 93  92  94 10 100 15 ; SC-BB-BB
+ 96  95  97 10 100 15 ; SC-BB-BB
+ 98  97 100 10 100 15 ; SC-BB-BB
+102 101 105 10 100 15 ; SC-BB-BB
+106 105 109 10 100 15 ; SC-BB-BB
+110 109 114 10 100 15 ; SC-BB-BB
+115 114 116 10 100 15 ; SC-BB-BB
+117 116 118 10 100 15 ; SC-BB-BB
+119 118 121 10 100 15 ; SC-BB-BB
+  1   2   3 10 100 15 ; BB-BB-SC
+  2   4   5 10 100 15 ; BB-BB-SC
+  4   6   7 10 100 15 ; BB-BB-SC
+  6   8   9 10 100 15 ; BB-BB-SC
+  8  10  11 10 100 15 ; BB-BB-SC
+ 10  12  13 10 100 15 ; BB-BB-SC
+ 12  14  15 10 100 15 ; BB-BB-SC
+ 14  16  17 10 100 15 ; BB-BB-SC
+ 16  18  19 10 100 15 ; BB-BB-SC
+ 18  20  21 10 100 15 ; BB-BB-SC
+ 20  22  23 10 100 15 ; BB-BB-SC
+ 22  24  25 10 100 15 ; BB-BB-SC
+ 24  26  27 10 100 15 ; BB-BB-SC
+ 26  31  32 10 100 15 ; BB-BB-SC
+ 31  33  34 10 100 15 ; BB-BB-SC
+ 33  35  36 10 100 15 ; BB-BB-SC
+ 35  37  38 10 100 15 ; BB-BB-SC
+ 37  39  40 10 100 15 ; BB-BB-SC
+ 39  44  45 10 100 15 ; BB-BB-SC
+ 44  46  47 10 100 15 ; BB-BB-SC
+ 48  52  53 10 100 15 ; BB-BB-SC
+ 52  54  55 10 100 15 ; BB-BB-SC
+ 54  56  57 10 100 15 ; BB-BB-SC
+ 56  58  59 10 100 15 ; BB-BB-SC
+ 58  62  63 10 100 15 ; BB-BB-SC
+ 62  64  65 10 100 15 ; BB-BB-SC
+ 66  67  68 10 100 15 ; BB-BB-SC
+ 67  69  70 10 100 15 ; BB-BB-SC
+ 69  73  74 10 100 15 ; BB-BB-SC
+ 73  75  76 10 100 15 ; BB-BB-SC
+ 75  77  78 10 100 15 ; BB-BB-SC
+ 77  79  80 10 100 15 ; BB-BB-SC
+ 79  81  82 10 100 15 ; BB-BB-SC
+ 81  83  84 10 100 15 ; BB-BB-SC
+ 83  88  89 10 100 15 ; BB-BB-SC
+ 88  90  91 10 100 15 ; BB-BB-SC
+ 90  92  93 10 100 15 ; BB-BB-SC
+ 94  95  96 10 100 15 ; BB-BB-SC
+ 95  97  98 10 100 15 ; BB-BB-SC
+100 101 102 10 100 15 ; BB-BB-SC
+101 105 106 10 100 15 ; BB-BB-SC
+105 109 110 10 100 15 ; BB-BB-SC
+109 114 115 10 100 15 ; BB-BB-SC
+114 116 117 10 100 15 ; BB-BB-SC
+116 118 119 10 100 15 ; BB-BB-SC
+118 121 122 10 100 15 ; BB-BB-SC
+
+; Side chain angles
+ 26  27  28 2 120.000 60.0
+ 26  27  29 2 120.000 60.0
+ 39  40  41 2 120.000 60.0
+ 39  40  42 2 120.000 60.0
+ 48  49  50 2 120.000 50.0
+ 48  49  51 2 120.000 50.0
+ 58  59  60 2 120.000 50.0
+ 58  59  61 2 120.000 50.0
+ 69  70  71 2 120.000 50.0
+ 69  70  72 2 120.000 50.0
+ 83  84  85 2 120.000 60.0
+ 83  84  86 2 120.000 60.0
+ 97  98  99 2 180.000 25.0
+101 102 103 2 120.000 50.0
+101 102 104 2 120.000 50.0
+105 106 107 2 120.000 50.0
+105 106 108 2 120.000 50.0
+109 110 111 2 120.000 60.0
+109 110 112 2 120.000 60.0
+118 119 120 2 180.000 25.0
+
+[ dihedrals ]
+  2   4   6   8 1 -120 400 1
+  4   6   8  10 1 -120 400 1
+  6   8  10  12 1 -120 400 1
+ 24  26  31  33 1 -120 400 1
+ 26  31  33  35 1 -120 400 1
+ 67  69  73  75 1 -120 400 1
+ 69  73  75  77 1 -120 400 1
+ 73  75  77  79 1 -120 400 1
+ 75  77  79  81 1 -120 400 1
+ 77  79  81  83 1 -120 400 1
+ 79  81  83  88 1 -120 400 1
+ 81  83  88  90 1 -120 400 1
+ 83  88  90  92 1 -120 400 1
+ 88  90  92  94 1 -120 400 1
+ 90  92  94  95 1 -120 400 1
+ 92  94  95  97 1 -120 400 1
+
+; SC-BB-BB-SC scFix
+  3   2   4   5 1 -121.9 75 1 ; SC-BB-BB-SC
+  5   4   6   7 1 -139.8 75 1 ; SC-BB-BB-SC
+  7   6   8   9 1 126.7 75 1 ; SC-BB-BB-SC
+  9   8  10  11 1 148.0 75 1 ; SC-BB-BB-SC
+ 11  10  12  13 1 -178.9 75 1 ; SC-BB-BB-SC
+ 13  12  14  15 1 -140.1 75 1 ; SC-BB-BB-SC
+ 15  14  16  17 1 141.7 75 1 ; SC-BB-BB-SC
+ 17  16  18  19 1 60.8 75 1 ; SC-BB-BB-SC
+ 19  18  20  21 1 42.9 75 1 ; SC-BB-BB-SC
+ 21  20  22  23 1 40.4 75 1 ; SC-BB-BB-SC
+ 23  22  24  25 1 63.0 75 1 ; SC-BB-BB-SC
+ 25  24  26  27 1 -99.1 75 1 ; SC-BB-BB-SC
+ 27  26  31  32 1 -144.6 75 1 ; SC-BB-BB-SC
+ 32  31  33  34 1 -133.4 75 1 ; SC-BB-BB-SC
+ 34  33  35  36 1 -151.0 75 1 ; SC-BB-BB-SC
+ 36  35  37  38 1 -119.2 75 1 ; SC-BB-BB-SC
+ 38  37  39  40 1 170.7 75 1 ; SC-BB-BB-SC
+ 40  39  44  45 1 111.2 75 1 ; SC-BB-BB-SC
+ 45  44  46  47 1 64.0 75 1 ; SC-BB-BB-SC
+ 49  48  52  53 1 -152.4 75 1 ; SC-BB-BB-SC
+ 53  52  54  55 1 169.6 75 1 ; SC-BB-BB-SC
+ 55  54  56  57 1 29.6 75 1 ; SC-BB-BB-SC
+ 57  56  58  59 1 51.8 75 1 ; SC-BB-BB-SC
+ 59  58  62  63 1 16.6 75 1 ; SC-BB-BB-SC
+ 63  62  64  65 1 22.2 75 1 ; SC-BB-BB-SC
+ 68  67  69  70 1 -146.5 75 1 ; SC-BB-BB-SC
+ 70  69  73  74 1 -168.2 75 1 ; SC-BB-BB-SC
+ 74  73  75  76 1 -120.4 75 1 ; SC-BB-BB-SC
+ 76  75  77  78 1 -117.0 75 1 ; SC-BB-BB-SC
+ 78  77  79  80 1 -122.0 75 1 ; SC-BB-BB-SC
+ 80  79  81  82 1 -153.2 75 1 ; SC-BB-BB-SC
+ 82  81  83  84 1 -124.4 75 1 ; SC-BB-BB-SC
+ 84  83  88  89 1 -144.2 75 1 ; SC-BB-BB-SC
+ 89  88  90  91 1 -148.1 75 1 ; SC-BB-BB-SC
+ 91  90  92  93 1 -158.9 75 1 ; SC-BB-BB-SC
+ 96  95  97  98 1 -124.4 75 1 ; SC-BB-BB-SC
+102 101 105 106 1 25.9 75 1 ; SC-BB-BB-SC
+106 105 109 110 1 -6.7 75 1 ; SC-BB-BB-SC
+110 109 114 115 1 13.3 75 1 ; SC-BB-BB-SC
+115 114 116 117 1 51.4 75 1 ; SC-BB-BB-SC
+117 116 118 119 1 135.4 75 1 ; SC-BB-BB-SC
+119 118 121 122 1 -159.0 75 1 ; SC-BB-BB-SC
+ 64  66  67  68 1 88.3 75 1 ; BB-BB-BB-SC
+ 65  64  66  67 1 -15.5 75 1 ; SC-BB-BB-BB
+ 92  94  95  96 1 68.7 75 1 ; BB-BB-BB-SC
+ 93  92  94  95 1 95.9 75 1 ; SC-BB-BB-BB
+ 97 100 101 102 1 -9.0 75 1 ; BB-BB-BB-SC
+ 98  97 100 101 1 74.1 75 1 ; SC-BB-BB-BB
+
+[ dihedrals ]
+ 30  28  29  27 2 180.0 50.0
+ 43  41  42  40 2 180.0 50.0
+ 87  85  86  84 2 180.0 50.0
+113 111 112 110 2 180.0 50.0
+
+[ exclusions ]
+ 26  27  28  29  30 
+ 27  28  29  30 
+ 28  29  30 
+ 29  30 
+ 39  40  41  42  43 
+ 40  41  42  43 
+ 41  42  43 
+ 42  43 
+ 48  49  50  51 
+ 49  50  51 
+ 50  51 
+ 58  59  60  61 
+ 59  60  61 
+ 60  61 
+ 69  70  71  72 
+ 70  71  72 
+ 71  72 
+ 83  84  85  86  87 
+ 84  85  86  87 
+ 85  86  87 
+ 86  87 
+101 102 103 104 
+102 103 104 
+103 104 
+105 106 107 108 
+106 107 108 
+107 108 
+109 110 111 112 113 
+110 111 112 113 
+111 112 113 
+112 113 
+
diff --git a/vermouth/tests/data/integration_tests/tier-1/EN_region/martinize2/screen.output b/vermouth/tests/data/integration_tests/tier-1/EN_region/martinize2/screen.output
new file mode 100644
index 00000000..efa25786
--- /dev/null
+++ b/vermouth/tests/data/integration_tests/tier-1/EN_region/martinize2/screen.output
@@ -0,0 +1,27 @@
+    INFO - general - Merging two molecules/chains because there is a CONECT record between atoms 49A-CYS7:SG and 231B-CYS7:SG
+    INFO - general - Read 1 molecules from PDB file ../aa.pdb
+    INFO - step - Guessing the bonds.
+    INFO - general - 1 molecules after guessing bonds
+    INFO - step - Repairing the graph.
+    INFO - general - Applying modification N-ter to residue A-GLY1
+    INFO - general - Applying modification C-ter to residue A-ASN21
+    INFO - general - Applying modification N-ter to residue B-PHE1
+    INFO - general - Applying modification C-ter to residue B-ALA30
+    INFO - step - Dealing with modifications.
+    INFO - general - Identified the modifications ['N-ter', 'N-ter'] on residues ['GLY1', 'GLY1', 'GLY1', 'GLY1']
+    INFO - general - Identified the modifications ['C-ter'] on residues ['ASN21', 'ASN21', 'ASN21']
+    INFO - general - Identified the modifications ['C-ter'] on residues ['ALA30', 'ALA30', 'ALA30']
+    INFO - step - Read input.
+    INFO - step - Creating the graph at the target resolution.
+    INFO - general - Applying modification mapping ('C-ter',)
+    INFO - general - Applying modification mapping ('C-ter',)
+    INFO - general - Applying modification mapping ('N-ter',)
+    INFO - general - Applying modification mapping ('N-ter',)
+    INFO - step - Averaging the coordinates.
+    INFO - step - Applying the links.
+    INFO - step - Placing the charge dummies.
+    INFO - step - Applying position restraints.
+    INFO - step - Setting the rubber bands.
+    INFO - step - Writing output.
+    INFO - general - Please cite: Souza, P C T; Alessandri, R; Barnoud, J; Thallmair, S; Faustino, I; Grünewald, F; Patmanidis, I; Abdizadeh, H; Bruininks, B M H; Wassenaar, T A; Kroon, P C; Melcr, J; Nieto, V; Corradi, V; Khan, H M; Domański, J; Javanainen, M; Martinez-Seara, H; Reuter, N; Best, R B; Vattulainen, I; Monticelli, L; Periole, X; Tieleman, D P; de Vries, A H; Marrink, S J;  Nature Methods 2021; 10.1038/s41592-021-01098-3
+    INFO - general - Zen martini: A martini with no vermouth at all. And no gin, either. -- P.J. O’Rourke
diff --git a/vermouth/tests/integration_tests/test_integration.py b/vermouth/tests/integration_tests/test_integration.py
index c08c2403..92c2a976 100644
--- a/vermouth/tests/integration_tests/test_integration.py
+++ b/vermouth/tests/integration_tests/test_integration.py
@@ -134,7 +134,9 @@ def _interaction_equal(interaction1, interaction2):
     ['tier-1', 'villin'],
     ['tier-1', '3i40'],
     ['tier-1', '6LFO_gap'],
-    ['tier-1', '1mj5']
+    ['tier-1', '1mj5'],
+    ['tier-1', 'EN_chain'],
+    ['tier-1', 'EN_region'],
     # ['tier-2', 'barnase_barstar'],
     # ['tier-2', 'dna'],
     # ['tier-2', 'gpa_dimer'],