HEADER PROTEIN FIBRIL 08-APR-18 6G8C TITLE CRYSTAL STRUCTURE OF THE AMYLOID-LIKE IYQYGG SEGMENT FROM THE R1 TITLE 2 REPEAT OF THE E. COLI BIOFILM-ASSOCIATED CSGA CURLI PROTEIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: MAJOR CURLIN SUBUNIT; COMPND 3 CHAIN: B; COMPND 4 FRAGMENT: AMYLOID SPINE SEGMENT IYQYGG FROM CSGA (RESIDUES 47-52) COMPND 5 SECRETED BY E. COLI; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 SYNTHETIC: YES; SOURCE 3 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI K-12; SOURCE 4 ORGANISM_TAXID: 83333; SOURCE 5 OTHER_DETAILS: IYQYGG FROM CSGA, SYNTHESIZED KEYWDS BACTERIAL STERIC-ZIPPER CROSS-BETA AMYLOID FIBRIL FROM E. COLI, KEYWDS 2 PROTEIN FIBRIL EXPDTA X-RAY DIFFRACTION AUTHOR M.LANDAU,S.PEROV REVDAT 1 24-APR-19 6G8C 0 JRNL AUTH S.PEROV,N.SALINAS,O.LIDOR,N.GOLAN,E.TAYEB-FLIGELMAN, JRNL AUTH 2 D.WILLBOLD,M.LANDAU JRNL TITL BIOFILM-RELATED CURLI CSGA SHARES STERIC ZIPPER STRUCTURES JRNL TITL 2 AND INHIBITORS OF PATHOLOGICAL HUMAN AMYLOIDS JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 1.65 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.65 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.14 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 97.3 REMARK 3 NUMBER OF REFLECTIONS : 489 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING + TEST SET) : 0.148 REMARK 3 R VALUE (WORKING SET) : 0.145 REMARK 3 FREE R VALUE : 0.178 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.100 REMARK 3 FREE R VALUE TEST SET COUNT : 55 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 50 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 2 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 19.06 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 11.97 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -1.17000 REMARK 3 B22 (A**2) : -0.81000 REMARK 3 B33 (A**2) : 1.69000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.28000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.108 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.100 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.056 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.799 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA REMARK 3 BOND LENGTH (A) : NULL ; NULL REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL REMARK 3 REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL REMARK 3 REMARK 3 NON-BONDED CONTACT RESTRAINTS. REMARK 3 SINGLE TORSION (A) : NULL ; NULL REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL REMARK 3 REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS. REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL REMARK 3 PLANAR (DEGREES) : NULL ; NULL REMARK 3 STAGGERED (DEGREES) : NULL ; NULL REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING REMARK 3 POSITIONS U VALUES : REFINED INDIVIDUALLY REMARK 4 REMARK 4 6G8C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 09-APR-18. REMARK 100 THE DEPOSITION ID IS D_1200009568. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 02-MAY-16 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : PETRA III, EMBL C/O DESY REMARK 200 BEAMLINE : P14 (MX2) REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9763 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 545 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.650 REMARK 200 RESOLUTION RANGE LOW (A) : 19.140 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.3 REMARK 200 DATA REDUNDANCY : 5.231 REMARK 200 R MERGE (I) : 0.09900 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 8.6600 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.85 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 5.90 REMARK 200 R MERGE FOR SHELL (I) : 0.32600 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 3.210 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: IDEAL BETA-STRAND REMARK 200 REMARK 200 REMARK: NEEDLE-LIKE REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): NULL REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: RESERVOIR CONTAINED 0.1 M SODIUM REMARK 280 ACETATE PH 4.6 AND 2.0 M SODIUM FORMATE, VAPOR DIFFUSION, REMARK 280 HANGING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 X+1/2,Y+1/2,Z REMARK 290 4555 -X+1/2,Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 21.08500 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 2.38000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 21.08500 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 2.38000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 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: OCTADECAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350 APPLY THE FOLLOWING TO CHAINS: B REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 -4.76000 REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000 REMARK 350 APPLY THE FOLLOWING TO CHAINS: B REMARK 350 BIOMT1 3 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 3 0.000000 1.000000 0.000000 -9.52000 REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000 REMARK 350 APPLY THE FOLLOWING TO CHAINS: B REMARK 350 BIOMT1 4 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 4 0.000000 1.000000 0.000000 -14.28000 REMARK 350 BIOMT3 4 0.000000 0.000000 1.000000 0.00000 REMARK 350 APPLY THE FOLLOWING TO CHAINS: B REMARK 350 BIOMT1 5 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 5 0.000000 1.000000 0.000000 -19.04000 REMARK 350 BIOMT3 5 0.000000 0.000000 1.000000 0.00000 REMARK 350 APPLY THE FOLLOWING TO CHAINS: B REMARK 350 BIOMT1 6 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 6 0.000000 1.000000 0.000000 4.76000 REMARK 350 BIOMT3 6 0.000000 0.000000 1.000000 0.00000 REMARK 350 APPLY THE FOLLOWING TO CHAINS: B REMARK 350 BIOMT1 7 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 7 0.000000 1.000000 0.000000 9.52000 REMARK 350 BIOMT3 7 0.000000 0.000000 1.000000 0.00000 REMARK 350 APPLY THE FOLLOWING TO CHAINS: B REMARK 350 BIOMT1 8 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 8 0.000000 1.000000 0.000000 14.28000 REMARK 350 BIOMT3 8 0.000000 0.000000 1.000000 0.00000 REMARK 350 APPLY THE FOLLOWING TO CHAINS: B REMARK 350 BIOMT1 9 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 9 0.000000 1.000000 0.000000 19.04000 REMARK 350 BIOMT3 9 0.000000 0.000000 1.000000 0.00000 REMARK 350 APPLY THE FOLLOWING TO CHAINS: B REMARK 350 BIOMT1 10 -1.000000 0.000000 0.000000 21.08500 REMARK 350 BIOMT2 10 0.000000 1.000000 0.000000 2.38000 REMARK 350 BIOMT3 10 0.000000 0.000000 -1.000000 0.00000 REMARK 350 APPLY THE FOLLOWING TO CHAINS: B REMARK 350 BIOMT1 11 -1.000000 0.000000 0.000000 21.08500 REMARK 350 BIOMT2 11 0.000000 1.000000 0.000000 -16.66000 REMARK 350 BIOMT3 11 0.000000 0.000000 -1.000000 0.00000 REMARK 350 APPLY THE FOLLOWING TO CHAINS: B REMARK 350 BIOMT1 12 -1.000000 0.000000 0.000000 21.08500 REMARK 350 BIOMT2 12 0.000000 1.000000 0.000000 -11.90000 REMARK 350 BIOMT3 12 0.000000 0.000000 -1.000000 0.00000 REMARK 350 APPLY THE FOLLOWING TO CHAINS: B REMARK 350 BIOMT1 13 -1.000000 0.000000 0.000000 21.08500 REMARK 350 BIOMT2 13 0.000000 1.000000 0.000000 -7.14000 REMARK 350 BIOMT3 13 0.000000 0.000000 -1.000000 0.00000 REMARK 350 APPLY THE FOLLOWING TO CHAINS: B REMARK 350 BIOMT1 14 -1.000000 0.000000 0.000000 21.08500 REMARK 350 BIOMT2 14 0.000000 1.000000 0.000000 -2.38000 REMARK 350 BIOMT3 14 0.000000 0.000000 -1.000000 0.00000 REMARK 350 APPLY THE FOLLOWING TO CHAINS: B REMARK 350 BIOMT1 15 -1.000000 0.000000 0.000000 21.08500 REMARK 350 BIOMT2 15 0.000000 1.000000 0.000000 7.14000 REMARK 350 BIOMT3 15 0.000000 0.000000 -1.000000 0.00000 REMARK 350 APPLY THE FOLLOWING TO CHAINS: B REMARK 350 BIOMT1 16 -1.000000 0.000000 0.000000 21.08500 REMARK 350 BIOMT2 16 0.000000 1.000000 0.000000 11.90000 REMARK 350 BIOMT3 16 0.000000 0.000000 -1.000000 0.00000 REMARK 350 APPLY THE FOLLOWING TO CHAINS: B REMARK 350 BIOMT1 17 -1.000000 0.000000 0.000000 21.08500 REMARK 350 BIOMT2 17 0.000000 1.000000 0.000000 16.66000 REMARK 350 BIOMT3 17 0.000000 0.000000 -1.000000 0.00000 REMARK 350 APPLY THE FOLLOWING TO CHAINS: B REMARK 350 BIOMT1 18 -1.000000 0.000000 0.000000 21.08500 REMARK 350 BIOMT2 18 0.000000 1.000000 0.000000 21.42000 REMARK 350 BIOMT3 18 0.000000 0.000000 -1.000000 0.00000 DBREF 6G8C B 1 6 UNP P28307 CSGA_ECOLI 47 52 SEQRES 1 B 6 ILE TYR GLN TYR GLY GLY FORMUL 2 HOH *2(H2 O) CRYST1 42.170 4.760 19.600 90.00 102.43 90.00 C 1 2 1 4 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.023714 0.000000 0.005227 0.00000 SCALE2 0.000000 0.210084 0.000000 0.00000 SCALE3 0.000000 0.000000 0.052245 0.00000 ATOM 1 N ILE B 1 0.331 3.119 4.818 1.00 13.51 N ATOM 2 CA ILE B 1 1.518 3.401 5.677 1.00 11.56 C ATOM 3 C ILE B 1 2.738 2.783 5.018 1.00 12.30 C ATOM 4 O ILE B 1 2.769 1.572 4.754 1.00 11.04 O ATOM 5 CB ILE B 1 1.371 2.848 7.117 1.00 13.95 C ATOM 6 CG1 ILE B 1 0.143 3.457 7.830 1.00 14.63 C ATOM 7 CG2 ILE B 1 2.679 3.032 7.881 1.00 14.90 C ATOM 8 CD1 ILE B 1 -0.194 2.710 9.114 1.00 17.65 C ATOM 9 N TYR B 2 3.722 3.641 4.787 1.00 10.11 N ATOM 10 CA TYR B 2 4.977 3.235 4.137 1.00 10.13 C ATOM 11 C TYR B 2 6.074 3.762 5.018 1.00 9.18 C ATOM 12 O TYR B 2 6.101 4.937 5.258 1.00 8.08 O ATOM 13 CB TYR B 2 5.121 3.877 2.736 1.00 9.44 C ATOM 14 CG TYR B 2 6.473 3.626 2.113 1.00 9.46 C ATOM 15 CD1 TYR B 2 6.670 2.543 1.223 1.00 10.46 C ATOM 16 CD2 TYR B 2 7.583 4.400 2.449 1.00 8.74 C ATOM 17 CE1 TYR B 2 7.892 2.298 0.672 1.00 10.42 C ATOM 18 CE2 TYR B 2 8.852 4.137 1.927 1.00 9.96 C ATOM 19 CZ TYR B 2 9.008 3.100 1.024 1.00 10.11 C ATOM 20 OH TYR B 2 10.247 2.890 0.476 1.00 10.10 O ATOM 21 N GLN B 3 6.982 2.898 5.448 1.00 9.03 N ATOM 22 CA GLN B 3 8.037 3.317 6.301 1.00 8.49 C ATOM 23 C GLN B 3 9.328 2.703 5.782 1.00 8.86 C ATOM 24 O GLN B 3 9.422 1.516 5.589 1.00 8.36 O ATOM 25 CB GLN B 3 7.793 2.850 7.740 1.00 9.24 C ATOM 26 CG GLN B 3 6.533 3.470 8.323 1.00 10.38 C ATOM 27 CD GLN B 3 6.117 2.882 9.623 1.00 12.90 C ATOM 28 OE1 GLN B 3 6.168 1.650 9.811 1.00 11.26 O ATOM 29 NE2 GLN B 3 5.628 3.725 10.486 1.00 8.97 N ATOM 30 N TYR B 4 10.318 3.552 5.642 1.00 8.04 N ATOM 31 CA TYR B 4 11.611 3.142 5.184 1.00 9.34 C ATOM 32 C TYR B 4 12.621 3.699 6.111 1.00 10.51 C ATOM 33 O TYR B 4 12.654 4.914 6.321 1.00 8.33 O ATOM 34 CB TYR B 4 11.871 3.708 3.805 1.00 11.73 C ATOM 35 CG TYR B 4 13.283 3.423 3.242 1.00 9.69 C ATOM 36 CD1 TYR B 4 13.511 2.408 2.296 1.00 14.13 C ATOM 37 CD2 TYR B 4 14.383 4.195 3.646 1.00 9.34 C ATOM 38 CE1 TYR B 4 14.774 2.173 1.744 1.00 14.00 C ATOM 39 CE2 TYR B 4 15.649 3.963 3.112 1.00 12.02 C ATOM 40 CZ TYR B 4 15.838 2.950 2.178 1.00 16.71 C ATOM 41 OH TYR B 4 17.093 2.726 1.668 1.00 17.99 O ATOM 42 N GLY B 5 13.507 2.849 6.614 1.00 11.58 N ATOM 43 CA GLY B 5 14.592 3.301 7.552 1.00 13.42 C ATOM 44 C GLY B 5 15.845 2.640 7.082 1.00 16.22 C ATOM 45 O GLY B 5 15.878 1.406 6.948 1.00 13.61 O ATOM 46 N GLY B 6 16.884 3.431 6.865 1.00 14.58 N ATOM 47 CA GLY B 6 18.224 2.874 6.629 1.00 17.20 C ATOM 48 C GLY B 6 18.935 3.634 5.535 1.00 21.41 C ATOM 49 O GLY B 6 19.993 3.209 5.020 1.00 22.29 O ATOM 50 OXT GLY B 6 18.440 4.695 5.124 1.00 20.56 O TER 51 GLY B 6 HETATM 52 O HOH B 101 18.901 5.322 2.488 1.00 25.00 O HETATM 53 O HOH B 102 1.297 4.326 2.455 1.00 26.07 O MASTER 258 0 0 0 0 0 0 6 52 1 0 1 END