HEADER BIOSYNTHETIC PROTEIN 21-APR-08 3CWI TITLE CRYSTAL STRUCTURE OF THIAMINE BIOSYNTHESIS PROTEIN (THIS) TITLE 2 FROM GEOBACTER METALLIREDUCENS. NORTHEAST STRUCTURAL TITLE 3 GENOMICS CONSORTIUM TARGET GMR137 COMPND MOL_ID: 1; COMPND 2 MOLECULE: THIAMINE-BIOSYNTHESIS PROTEIN THIS; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: GEOBACTER METALLIREDUCENS GS-15; SOURCE 3 ORGANISM_TAXID: 269799; SOURCE 4 STRAIN: GS-15 / DSM 7210; SOURCE 5 ATCC: 53774; SOURCE 6 GENE: THIS, GMET_1567; SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)+MAGIC; SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET21 KEYWDS ALPHA-BETA PROTEIN, STRUCTURAL GENOMICS, PSI-2, PROTEIN KEYWDS 2 STRUCTURE INITIATIVE, NORTHEAST STRUCTURAL GENOMICS KEYWDS 3 CONSORTIUM, NESG, BIOSYNTHETIC PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR F.FOROUHAR,M.ABASHIDZE,J.SEETHARAMAN,L.MAO,H.JANJUA,R.XIAO, AUTHOR 2 M.MAGLAQUI,C.CICCOSANTI,E.L.FOOTE,H.WANG,J.K.EVERETT, AUTHOR 3 T.B.ACTON,G.T.MONTELIONE,L.TONG,J.F.HUNT,NORTHEAST AUTHOR 4 STRUCTURAL GENOMICS CONSORTIUM (NESG) REVDAT 2 24-FEB-09 3CWI 1 VERSN REVDAT 1 06-MAY-08 3CWI 0 JRNL AUTH F.FOROUHAR,M.ABASHIDZE,J.SEETHARAMAN,L.MAO, JRNL AUTH 2 H.JANJUA,R.XIAO,M.MAGLAQUI,C.CICCOSANTI,E.L.FOOTE, JRNL AUTH 3 H.WANG,J.K.EVERETT,T.B.ACTON,G.T.MONTELIONE,L.TONG, JRNL AUTH 4 J.F.HUNT JRNL TITL CRYSTAL STRUCTURE OF THIAMINE BIOSYNTHESIS PROTEIN JRNL TITL 2 (THIS) FROM GEOBACTER METALLIREDUCENS. JRNL REF TO BE PUBLISHED JRNL REFN REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 1.90 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 1.2 REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE- REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU, REMARK 3 : READ,RICE,SIMONSON,WARREN REMARK 3 REMARK 3 REFINEMENT TARGET : ENGH & HUBER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.97 REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 856078.580 REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000 REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 90.7 REMARK 3 NUMBER OF REFLECTIONS : 10382 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING SET) : 0.226 REMARK 3 FREE R VALUE : 0.258 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.200 REMARK 3 FREE R VALUE TEST SET COUNT : 1060 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.008 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 10 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.90 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.97 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 69.40 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 702 REMARK 3 BIN R VALUE (WORKING SET) : 0.2190 REMARK 3 BIN FREE R VALUE : 0.2400 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 11.60 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 92 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.025 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 513 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 45 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 16.00 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.00 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 4.20000 REMARK 3 B22 (A**2) : 4.20000 REMARK 3 B33 (A**2) : -8.40000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.23 REMARK 3 ESD FROM SIGMAA (A) : 0.05 REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00 REMARK 3 REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.31 REMARK 3 ESD FROM C-V SIGMAA (A) : 0.18 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.005 REMARK 3 BOND ANGLES (DEGREES) : 1.10 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 25.60 REMARK 3 IMPROPER ANGLES (DEGREES) : 0.59 REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : OVERALL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED : FLAT MODEL REMARK 3 KSOL : 0.45 REMARK 3 BSOL : 59.01 REMARK 3 REMARK 3 NCS MODEL : NULL REMARK 3 REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL REMARK 3 REMARK 3 PARAMETER FILE 1 : NULL REMARK 3 TOPOLOGY FILE 1 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE FRIEDEL PAIRS WERE USED IN REMARK 3 PHASING REMARK 4 REMARK 4 3CWI COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-APR-08. REMARK 100 THE RCSB ID CODE IS RCSB047297. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 02-APR-08 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 5.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : NSLS REMARK 200 BEAMLINE : X4C REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97908 REMARK 200 MONOCHROMATOR : SI 111 CHANNEL REMARK 200 OPTICS : MIRRORS 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 : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 11436 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900 REMARK 200 RESOLUTION RANGE LOW (A) : 30.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5 REMARK 200 DATA REDUNDANCY : 14.500 REMARK 200 R MERGE (I) : 0.07800 REMARK 200 R SYM (I) : 0.06300 REMARK 200 FOR THE DATA SET : 40.7400 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8 REMARK 200 DATA REDUNDANCY IN SHELL : 10.80 REMARK 200 R MERGE FOR SHELL (I) : 0.37000 REMARK 200 R SYM FOR SHELL (I) : 0.32800 REMARK 200 FOR SHELL : 4.540 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD REMARK 200 SOFTWARE USED: SOLVE REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: THE STRUCTURE FACTOR FILE CONTAINS FRIEDEL PAIRS REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 43.52 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN SOLUTION: 10 MM TRIS-HCL PH REMARK 280 7.5, 100 MM NACL, 5 MM DTT. RESERVOIR SOLUTION: 100 MM SODIUM REMARK 280 ACETATE PH 5.0, 18% PEG 8000, 200 MM MAGNESIUM CHLORIDE, VAPOR REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 291K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z+1/2 REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4 REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4 REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4 REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4 REMARK 290 7555 Y,X,-Z REMARK 290 8555 -Y,-X,-Z+1/2 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 44.76850 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 20.48250 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 20.48250 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 67.15275 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 20.48250 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 20.48250 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 22.38425 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 20.48250 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 20.48250 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 67.15275 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 20.48250 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 20.48250 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 22.38425 REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 44.76850 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 300 REMARK: AUTHORS STATE THAT THE MONOMERIC ASSEMBLY OF THE REMARK 300 BIOLOGICAL UNIT THAT IS SHOWN IN REMARK 350 IS PUTATIVE REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 LYS A 70 REMARK 465 LEU A 71 REMARK 465 GLU A 72 REMARK 465 HIS A 73 REMARK 465 HIS A 74 REMARK 465 HIS A 75 REMARK 465 HIS A 76 REMARK 465 HIS A 77 REMARK 465 HIS A 78 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 O HOH A 117 O HOH A 117 7556 2.05 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: GMR137 RELATED DB: TARGETDB DBREF 3CWI A 1 70 UNP Q39VC5 Q39VC5_GEOMG 1 70 SEQADV 3CWI LEU A 71 UNP Q39VC5 EXPRESSION TAG SEQADV 3CWI GLU A 72 UNP Q39VC5 EXPRESSION TAG SEQADV 3CWI HIS A 73 UNP Q39VC5 EXPRESSION TAG SEQADV 3CWI HIS A 74 UNP Q39VC5 EXPRESSION TAG SEQADV 3CWI HIS A 75 UNP Q39VC5 EXPRESSION TAG SEQADV 3CWI HIS A 76 UNP Q39VC5 EXPRESSION TAG SEQADV 3CWI HIS A 77 UNP Q39VC5 EXPRESSION TAG SEQADV 3CWI HIS A 78 UNP Q39VC5 EXPRESSION TAG SEQRES 1 A 78 MSE ASN LEU THR VAL ASN GLY LYS PRO SER THR VAL ASP SEQRES 2 A 78 GLY ALA GLU SER LEU ASN VAL THR GLU LEU LEU SER ALA SEQRES 3 A 78 LEU LYS VAL ALA GLN ALA GLU TYR VAL THR VAL GLU LEU SEQRES 4 A 78 ASN GLY GLU VAL LEU GLU ARG GLU ALA PHE ASP ALA THR SEQRES 5 A 78 THR VAL LYS ASP GLY ASP ALA VAL GLU PHE LEU TYR PHE SEQRES 6 A 78 MSE GLY GLY GLY LYS LEU GLU HIS HIS HIS HIS HIS HIS MODRES 3CWI MSE A 1 MET SELENOMETHIONINE MODRES 3CWI MSE A 66 MET SELENOMETHIONINE HET MSE A 1 8 HET MSE A 66 8 HETNAM MSE SELENOMETHIONINE FORMUL 1 MSE 2(C5 H11 N O2 SE) FORMUL 2 HOH *45(H2 O) HELIX 1 1 VAL A 20 LEU A 27 1 8 HELIX 2 2 GLN A 31 VAL A 35 5 5 HELIX 3 3 GLU A 45 PHE A 49 5 5 SHEET 1 A 5 LYS A 8 THR A 11 0 SHEET 2 A 5 ASN A 2 VAL A 5 -1 N VAL A 5 O LYS A 8 SHEET 3 A 5 ALA A 59 LEU A 63 1 O VAL A 60 N THR A 4 SHEET 4 A 5 THR A 36 LEU A 39 -1 N THR A 36 O LEU A 63 SHEET 5 A 5 GLU A 42 VAL A 43 -1 O GLU A 42 N LEU A 39 SHEET 1 B 2 SER A 17 ASN A 19 0 SHEET 2 B 2 THR A 53 LYS A 55 -1 O VAL A 54 N LEU A 18 LINK C MSE A 1 N ASN A 2 1555 1555 1.33 LINK C PHE A 65 N MSE A 66 1555 1555 1.33 LINK C MSE A 66 N GLY A 67 1555 1555 1.33 CRYST1 40.965 40.965 89.537 90.00 90.00 90.00 P 43 21 2 8 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.024411 0.000000 0.000000 0.00000 SCALE2 0.000000 0.024411 0.000000 0.00000 SCALE3 0.000000 0.000000 0.011169 0.00000 HETATM 1 N MSE A 1 27.129 17.327 45.961 1.00 35.75 N HETATM 2 CA MSE A 1 26.660 17.430 44.546 1.00 31.81 C HETATM 3 C MSE A 1 27.150 16.224 43.749 1.00 22.97 C HETATM 4 O MSE A 1 28.193 15.652 44.059 1.00 26.42 O HETATM 5 CB MSE A 1 27.190 18.720 43.906 1.00 35.29 C HETATM 6 CG MSE A 1 28.706 18.788 43.806 1.00 34.31 C HETATM 7 SE MSE A 1 29.341 20.290 42.743 1.00 54.83 SE HETATM 8 CE MSE A 1 29.303 19.468 40.997 1.00 46.95 C REMARK PdbStat -- REMARK PdbStat -- PDB COORDINATES FOR 3CWI.PDB, MODEL/S 1 3CWI.PDB REMARK PdbStat -- SEQRES 1 A 114 MSE ASN LEU THR VAL ASN GLY LYS PRO SER THR VAL ASP SEQRES 2 A 114 GLY ALA GLU SER LEU ASN VAL THR GLU LEU LEU SER ALA SEQRES 3 A 114 LEU LYS VAL ALA GLN ALA GLU TYR VAL THR VAL GLU LEU SEQRES 4 A 114 ASN GLY GLU VAL LEU GLU ARG GLU ALA PHE ASP ALA THR SEQRES 5 A 114 THR VAL LYS ASP GLY ASP ALA VAL GLU PHE LEU TYR PHE SEQRES 6 A 114 MSE GLY GLY GLY HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 7 A 114 HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 8 A 114 HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 9 A 114 HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH REMARK PdbStat -- REMARK PdbStat -- PDB COORDINATES FOR 3CWI.PDB, MODEL/S 1 3CWI.PDB REMARK PdbStat -- SEQRES 1 A 114 MSE ASN LEU THR VAL ASN GLY LYS PRO SER THR VAL ASP SEQRES 2 A 114 GLY ALA GLU SER LEU ASN VAL THR GLU LEU LEU SER ALA SEQRES 3 A 114 LEU LYS VAL ALA GLN ALA GLU TYR VAL THR VAL GLU LEU SEQRES 4 A 114 ASN GLY GLU VAL LEU GLU ARG GLU ALA PHE ASP ALA THR SEQRES 5 A 114 THR VAL LYS ASP GLY ASP ALA VAL GLU PHE LEU TYR PHE SEQRES 6 A 114 MSE GLY GLY GLY HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 7 A 114 HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 8 A 114 HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 9 A 114 HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH REMARK PdbStat -- REMARK PdbStat -- PDB COORDINATES FOR 3CWI.PDB, MODEL/S 1 3CWI.PDB REMARK PdbStat -- SEQRES 1 A 114 MSE ASN LEU THR VAL ASN GLY LYS PRO SER THR VAL ASP SEQRES 2 A 114 GLY ALA GLU SER LEU ASN VAL THR GLU LEU LEU SER ALA SEQRES 3 A 114 LEU LYS VAL ALA GLN ALA GLU TYR VAL THR VAL GLU LEU SEQRES 4 A 114 ASN GLY GLU VAL LEU GLU ARG GLU ALA PHE ASP ALA THR SEQRES 5 A 114 THR VAL LYS ASP GLY ASP ALA VAL GLU PHE LEU TYR PHE SEQRES 6 A 114 MSE GLY GLY GLY HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 7 A 114 HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 8 A 114 HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 9 A 114 HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH REMARK PdbStat -- REMARK PdbStat -- PDB COORDINATES FOR 3CWI.PDB, MODEL/S 1 3CWI.PDB REMARK PdbStat -- SEQRES 1 A 114 MSE ASN LEU THR VAL ASN GLY LYS PRO SER THR VAL ASP SEQRES 2 A 114 GLY ALA GLU SER LEU ASN VAL THR GLU LEU LEU SER ALA SEQRES 3 A 114 LEU LYS VAL ALA GLN ALA GLU TYR VAL THR VAL GLU LEU SEQRES 4 A 114 ASN GLY GLU VAL LEU GLU ARG GLU ALA PHE ASP ALA THR SEQRES 5 A 114 THR VAL LYS ASP GLY ASP ALA VAL GLU PHE LEU TYR PHE SEQRES 6 A 114 MSE GLY GLY GLY HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 7 A 114 HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 8 A 114 HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 9 A 114 HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH MODEL 1 REMARK CONFORMATION 1 ENERGY 0.0000 REMARK FAMILY or FILE: 3CWI.pdb HETATM 1 N MSE A 1 20.863 21.018 52.555 1.00 35.75 N HETATM 2 CA MSE A 1 20.394 21.121 51.140 1.00 31.81 C HETATM 3 C MSE A 1 20.884 19.915 50.343 1.00 22.97 C HETATM 4 O MSE A 1 21.927 19.343 50.653 1.00 26.42 O HETATM 5 CB MSE A 1 20.924 22.411 50.500 1.00 35.29 C HETATM 6 CG MSE A 1 22.440 22.479 50.400 1.00 34.31 C HETATM 7 SE MSE A 1 23.075 23.981 49.337 1.00 54.83 HETATM 8 CE MSE A 1 23.037 23.159 47.591 1.00 46.95 C HETATM 9 N MSE A 1 22.740 19.690 49.852 1.00 35.75 N HETATM 10 CA MSE A 1 22.271 19.793 48.437 1.00 31.81 C HETATM 11 C MSE A 1 22.761 18.587 47.640 1.00 22.97 C HETATM 12 O MSE A 1 23.804 18.015 47.950 1.00 26.42 O HETATM 13 CB MSE A 1 22.801 21.083 47.797 1.00 35.29 C HETATM 14 CG MSE A 1 24.317 21.151 47.697 1.00 34.31 C HETATM 15 SE MSE A 1 24.952 22.653 46.634 1.00 54.83 HETATM 16 CE MSE A 1 24.914 21.831 44.888 1.00 46.95 C HETATM 17 N MSE A 1 22.903 19.587 48.489 1.00 35.75 N HETATM 18 CA MSE A 1 22.434 19.690 47.074 1.00 31.81 C HETATM 19 C MSE A 1 22.924 18.484 46.277 1.00 22.97 C HETATM 20 O MSE A 1 23.967 17.912 46.587 1.00 26.42 O HETATM 21 CB MSE A 1 22.964 20.980 46.434 1.00 35.29 C HETATM 22 CG MSE A 1 24.480 21.048 46.334 1.00 34.31 C HETATM 23 SE MSE A 1 25.115 22.550 45.271 1.00 54.83 HETATM 24 CE MSE A 1 25.077 21.728 43.525 1.00 46.95 C HETATM 25 N MSE A 1 -5.528 5.174 9.828 1.00 35.75 N HETATM 26 CA MSE A 1 -5.997 5.278 8.413 1.00 31.81 C HETATM 27 C MSE A 1 -5.507 4.072 7.616 1.00 22.97 C HETATM 28 O MSE A 1 -4.464 3.500 7.926 1.00 26.42 O HETATM 29 CB MSE A 1 -5.467 6.567 7.773 1.00 35.29 C HETATM 30 CG MSE A 1 -3.951 6.636 7.673 1.00 34.31 C HETATM 31 SE MSE A 1 -3.316 8.138 6.610 1.00 54.83 HETATM 32 CE MSE A 1 -3.354 7.316 4.864 1.00 46.95 C ATOM 33 N ASN A 2 -6.266 3.691 6.594 1.00 21.16 N ATOM 34 CA ASN A 2 -5.906 2.556 5.761 1.00 22.75 C ATOM 35 C ASN A 2 -5.441 2.995 4.392 1.00 25.63 C ATOM 36 O ASN A 2 -6.014 3.909 3.800 1.00 24.20 O ATOM 37 CB ASN A 2 -7.093 1.605 5.578 1.00 31.93 C ATOM 38 CG ASN A 2 -7.242 0.624 6.723 1.00 37.82 C ATOM 39 OD1 ASN A 2 -8.081 -0.274 6.670 1.00 49.41 O ATOM 40 ND2 ASN A 2 -6.430 0.785 7.761 1.00 32.45 N ATOM 41 N LEU A 3 -4.389 2.363 3.891 1.00 16.69 N ATOM 42 CA LEU A 3 -3.905 2.693 2.559 1.00 23.38 C ATOM 43 C LEU A 3 -3.278 1.457 1.957 1.00 19.96 C ATOM 44 O LEU A 3 -3.068 0.455 2.639 1.00 24.61 O ATOM 45 CB LEU A 3 -2.881 3.832 2.598 1.00 26.44 C ATOM 46 CG LEU A 3 -1.543 3.606 3.297 1.00 30.54 C ATOM 47 CD1 LEU A 3 -0.564 4.704 2.894 1.00 28.29 C ATOM 48 CD2 LEU A 3 -1.745 3.587 4.799 1.00 28.91 C ATOM 49 N THR A 4 -3.011 1.525 0.664 1.00 17.55 N ATOM 50 CA THR A 4 -2.396 0.415 -0.039 1.00 17.35 C ATOM 51 C THR A 4 -0.964 0.849 -0.337 1.00 21.36 C ATOM 52 O THR A 4 -0.740 1.952 -0.835 1.00 19.16 O ATOM 53 CB THR A 4 -3.141 0.131 -1.357 1.00 19.66 C ATOM 54 OG1 THR A 4 -4.536 -0.076 -1.079 1.00 22.76 O ATOM 55 CG2 THR A 4 -2.581 -1.105 -2.027 1.00 18.54 C ATOM 56 N VAL A 5 0.000 -0.000 -0.000 1.00 12.69 N ATOM 57 CA VAL A 5 1.403 0.309 -0.246 1.00 18.11 C ATOM 58 C VAL A 5 1.985 -0.829 -1.074 1.00 20.32 C ATOM 59 O VAL A 5 2.011 -1.979 -0.631 1.00 17.58 O ATOM 60 CB VAL A 5 2.196 0.450 1.084 1.00 24.50 C ATOM 61 CG1 VAL A 5 3.671 0.690 0.793 1.00 24.64 C ATOM 62 CG2 VAL A 5 1.632 1.617 1.900 1.00 18.51 C ATOM 63 N ASN A 6 2.438 -0.500 -2.279 1.00 22.04 N ATOM 64 CA ASN A 6 2.991 -1.491 -3.207 1.00 27.14 C ATOM 65 C ASN A 6 1.996 -2.628 -3.411 1.00 29.17 C ATOM 66 O ASN A 6 2.363 -3.810 -3.419 1.00 23.37 O ATOM 67 CB ASN A 6 4.317 -2.046 -2.694 1.00 31.71 C ATOM 68 CG ASN A 6 5.394 -0.986 -2.626 1.00 34.01 C ATOM 69 OD1 ASN A 6 5.476 -0.119 -3.498 1.00 26.26 O ATOM 70 ND2 ASN A 6 6.240 -1.062 -1.604 1.00 40.99 N ATOM 71 N GLY A 7 0.729 -2.248 -3.554 1.00 22.86 N ATOM 72 CA GLY A 7 -0.335 -3.210 -3.789 1.00 19.51 C ATOM 73 C GLY A 7 -0.869 -3.958 -2.587 1.00 19.75 C ATOM 74 O GLY A 7 -1.851 -4.688 -2.706 1.00 21.20 O ATOM 75 N LYS A 8 -0.251 -3.781 -1.427 1.00 17.70 N ATOM 76 CA LYS A 8 -0.702 -4.501 -0.244 1.00 23.22 C ATOM 77 C LYS A 8 -1.274 -3.623 0.859 1.00 21.33 C ATOM 78 O LYS A 8 -0.886 -2.461 1.013 1.00 18.85 O ATOM 79 CB LYS A 8 0.447 -5.348 0.295 1.00 23.33 C ATOM 80 CG LYS A 8 0.927 -6.401 -0.704 1.00 24.26 C ATOM 81 CD LYS A 8 -0.154 -7.449 -0.969 1.00 24.14 C ATOM 82 CE LYS A 8 0.377 -8.609 -1.805 1.00 20.73 C ATOM 83 NZ LYS A 8 0.739 -8.215 -3.194 1.00 25.42 N ATOM 84 N PRO A 9 -2.216 -4.175 1.643 1.00 22.06 N ATOM 85 CA PRO A 9 -2.857 -3.451 2.738 1.00 20.63 C ATOM 86 C PRO A 9 -1.853 -2.918 3.742 1.00 21.68 C ATOM 87 O PRO A 9 -0.871 -3.581 4.087 1.00 18.74 O ATOM 88 CB PRO A 9 -3.781 -4.494 3.354 1.00 30.38 C ATOM 89 CG PRO A 9 -4.133 -5.354 2.176 1.00 32.78 C ATOM 90 CD PRO A 9 -2.797 -5.521 1.508 1.00 24.61 C ATOM 91 N SER A 10 -2.111 -1.708 4.213 1.00 19.11 N ATOM 92 CA SER A 10 -1.230 -1.074 5.181 1.00 23.06 C ATOM 93 C SER A 10 -2.091 -0.220 6.101 1.00 23.41 C ATOM 94 O SER A 10 -3.199 0.178 5.742 1.00 19.37 O ATOM 95 CB SER A 10 -0.189 -0.227 4.440 1.00 26.52 C ATOM 96 OG SER A 10 0.523 0.627 5.320 1.00 33.36 O ATOM 97 N THR A 11 -1.588 0.042 7.299 1.00 20.37 N ATOM 98 CA THR A 11 -2.324 0.839 8.261 1.00 19.10 C ATOM 99 C THR A 11 -1.394 1.820 8.956 1.00 24.17 C ATOM 100 O THR A 11 -0.205 1.546 9.163 1.00 21.75 O ATOM 101 CB THR A 11 -2.987 -0.064 9.327 1.00 25.15 C ATOM 102 OG1 THR A 11 -3.895 -0.970 8.687 1.00 28.55 O ATOM 103 CG2 THR A 11 -3.746 0.764 10.344 1.00 35.08 C ATOM 104 N VAL A 12 -1.942 2.976 9.296 1.00 25.62 N ATOM 105 CA VAL A 12 -1.191 4.000 9.998 1.00 21.54 C ATOM 106 C VAL A 12 -2.091 4.461 11.127 1.00 23.45 C ATOM 107 O VAL A 12 -3.089 5.147 10.896 1.00 29.97 O ATOM 108 CB VAL A 12 -0.865 5.204 9.086 1.00 28.23 C ATOM 109 CG1 VAL A 12 -0.045 6.226 9.859 1.00 23.35 C ATOM 110 CG2 VAL A 12 -0.098 4.740 7.857 1.00 24.52 C ATOM 111 N ASP A 13 -1.766 4.050 12.347 1.00 22.40 N ATOM 112 CA ASP A 13 -2.563 4.461 13.493 1.00 24.55 C ATOM 113 C ASP A 13 -1.967 5.747 14.040 1.00 27.18 C ATOM 114 O ASP A 13 -0.749 5.864 14.173 1.00 26.85 O ATOM 115 CB ASP A 13 -2.553 3.393 14.591 1.00 28.83 C ATOM 116 CG ASP A 13 -3.130 2.068 14.130 1.00 40.82 C ATOM 117 OD1 ASP A 13 -4.190 2.066 13.457 1.00 41.10 O ATOM 118 OD2 ASP A 13 -2.535 1.020 14.464 1.00 43.57 O ATOM 119 N GLY A 14 -2.827 6.709 14.350 1.00 24.02 N ATOM 120 CA GLY A 14 -2.349 7.966 14.895 1.00 25.62 C ATOM 121 C GLY A 14 -2.365 9.125 13.920 1.00 25.53 C ATOM 122 O GLY A 14 -2.072 10.256 14.309 1.00 32.14 O ATOM 123 N ALA A 15 -2.700 8.862 12.659 1.00 23.62 N ATOM 124 CA ALA A 15 -2.740 9.921 11.650 1.00 26.27 C ATOM 125 C ALA A 15 -3.935 9.784 10.715 1.00 25.93 C ATOM 126 O ALA A 15 -4.301 8.677 10.316 1.00 28.60 O ATOM 127 CB ALA A 15 -1.447 9.921 10.843 1.00 27.32 C ATOM 128 N GLU A 16 -4.541 10.914 10.368 1.00 22.54 N ATOM 129 CA GLU A 16 -5.690 10.927 9.469 1.00 30.73 C ATOM 130 C GLU A 16 -5.207 11.180 8.043 1.00 24.22 C ATOM 131 O GLU A 16 -5.944 10.975 7.076 1.00 36.97 O ATOM 132 CB GLU A 16 -6.675 12.020 9.893 1.00 30.48 C ATOM 133 CG GLU A 16 -7.118 11.910 11.348 1.00 45.11 C ATOM 134 CD GLU A 16 -7.586 10.511 11.696 1.00 52.58 C ATOM 135 OE1 GLU A 16 -8.417 9.959 10.942 1.00 60.27 O ATOM 136 OE2 GLU A 16 -7.134 9.968 12.729 1.00 53.33 O ATOM 137 N SER A 17 -3.960 11.623 7.932 1.00 23.45 N ATOM 138 CA SER A 17 -3.321 11.899 6.655 1.00 24.25 C ATOM 139 C SER A 17 -1.842 12.167 6.910 1.00 20.41 C ATOM 140 O SER A 17 -1.426 12.396 8.048 1.00 22.32 O ATOM 141 CB SER A 17 -3.943 13.125 5.978 1.00 26.08 C ATOM 142 OG SER A 17 -3.526 14.320 6.612 1.00 34.47 O ATOM 143 N LEU A 18 -1.054 12.135 5.843 1.00 21.34 N ATOM 144 CA LEU A 18 0.379 12.378 5.918 1.00 18.46 C ATOM 145 C LEU A 18 0.872 12.878 4.581 1.00 21.29 C ATOM 146 O LEU A 18 0.318 12.518 3.541 1.00 23.31 O ATOM 147 CB LEU A 18 1.130 11.088 6.252 1.00 21.39 C ATOM 148 CG LEU A 18 1.155 10.653 7.714 1.00 22.35 C ATOM 149 CD1 LEU A 18 1.715 9.247 7.813 1.00 34.43 C ATOM 150 CD2 LEU A 18 1.992 11.632 8.525 1.00 37.15 C ATOM 151 N ASN A 19 1.904 13.716 4.594 1.00 17.62 N ATOM 152 CA ASN A 19 2.448 14.194 3.334 1.00 19.00 C ATOM 153 C ASN A 19 3.470 13.138 2.933 1.00 16.18 C ATOM 154 O ASN A 19 3.866 12.300 3.751 1.00 17.40 O ATOM 155 CB ASN A 19 3.098 15.580 3.478 1.00 20.94 C ATOM 156 CG ASN A 19 4.196 15.616 4.520 1.00 27.45 C ATOM 157 OD1 ASN A 19 5.212 14.935 4.400 1.00 16.21 O ATOM 158 ND2 ASN A 19 3.998 16.434 5.551 1.00 33.63 N ATOM 159 N VAL A 20 3.882 13.156 1.676 1.00 17.18 N ATOM 160 CA VAL A 20 4.818 12.161 1.183 1.00 22.32 C ATOM 161 C VAL A 20 6.137 12.132 1.933 1.00 19.58 C ATOM 162 O VAL A 20 6.676 11.059 2.199 1.00 16.67 O ATOM 163 CB VAL A 20 5.075 12.365 -0.315 1.00 19.03 C ATOM 164 CG1 VAL A 20 6.126 11.382 -0.810 1.00 17.68 C ATOM 165 CG2 VAL A 20 3.780 12.180 -1.074 1.00 17.73 C ATOM 166 N THR A 21 6.653 13.309 2.268 1.00 17.05 N ATOM 167 CA THR A 21 7.905 13.393 3.003 1.00 22.85 C ATOM 168 C THR A 21 7.821 12.625 4.315 1.00 20.26 C ATOM 169 O THR A 21 8.719 11.852 4.656 1.00 17.93 O ATOM 170 CB THR A 21 8.267 14.847 3.295 1.00 21.96 C ATOM 171 OG1 THR A 21 8.353 15.562 2.058 1.00 23.66 O ATOM 172 CG2 THR A 21 9.603 14.920 4.020 1.00 29.23 C ATOM 173 N GLU A 22 6.732 12.819 5.048 1.00 20.23 N ATOM 174 CA GLU A 22 6.571 12.125 6.319 1.00 16.48 C ATOM 175 C GLU A 22 6.425 10.621 6.096 1.00 19.72 C ATOM 176 O GLU A 22 6.938 9.820 6.879 1.00 17.02 O ATOM 177 CB GLU A 22 5.344 12.652 7.067 1.00 20.61 C ATOM 178 CG GLU A 22 5.420 14.129 7.424 1.00 27.72 C ATOM 179 CD GLU A 22 4.104 14.642 7.972 1.00 38.77 C ATOM 180 OE1 GLU A 22 3.063 14.410 7.315 1.00 31.90 O ATOM 181 OE2 GLU A 22 4.105 15.286 9.043 1.00 42.00 O ATOM 182 N LEU A 23 5.738 10.244 5.018 1.00 15.24 N ATOM 183 CA LEU A 23 5.515 8.834 4.690 1.00 14.64 C ATOM 184 C LEU A 23 6.820 8.094 4.424 1.00 17.75 C ATOM 185 O LEU A 23 7.046 7.001 4.946 1.00 18.50 O ATOM 186 CB LEU A 23 4.618 8.715 3.449 1.00 20.39 C ATOM 187 CG LEU A 23 3.617 7.567 3.360 1.00 23.49 C ATOM 188 CD1 LEU A 23 3.201 7.403 1.914 1.00 20.30 C ATOM 189 CD2 LEU A 23 4.202 6.279 3.890 1.00 36.09 C ATOM 190 N LEU A 24 7.662 8.688 3.585 1.00 19.75 N ATOM 191 CA LEU A 24 8.944 8.090 3.231 1.00 26.34 C ATOM 192 C LEU A 24 9.773 7.837 4.474 1.00 24.42 C ATOM 193 O LEU A 24 10.325 6.750 4.660 1.00 22.88 O ATOM 194 CB LEU A 24 9.718 9.015 2.294 1.00 32.90 C ATOM 195 CG LEU A 24 9.471 8.920 0.787 1.00 34.13 C ATOM 196 CD1 LEU A 24 7.989 8.750 0.486 1.00 47.09 C ATOM 197 CD2 LEU A 24 10.019 10.181 0.137 1.00 20.78 C ATOM 198 N SER A 25 9.854 8.851 5.326 1.00 24.77 N ATOM 199 CA SER A 25 10.617 8.744 6.556 1.00 26.74 C ATOM 200 C SER A 25 10.020 7.716 7.507 1.00 23.57 C ATOM 201 O SER A 25 10.722 6.824 7.992 1.00 36.16 O ATOM 202 CB SER A 25 10.697 10.108 7.245 1.00 27.75 C ATOM 203 OG SER A 25 11.431 10.004 8.452 1.00 43.79 O ATOM 204 N ALA A 26 8.725 7.823 7.774 1.00 23.42 N ATOM 205 CA ALA A 26 8.081 6.879 8.684 1.00 26.78 C ATOM 206 C ALA A 26 8.311 5.434 8.235 1.00 31.02 C ATOM 207 O ALA A 26 8.735 4.597 9.030 1.00 25.58 O ATOM 208 CB ALA A 26 6.592 7.171 8.773 1.00 21.28 C ATOM 209 N LEU A 27 8.025 5.145 6.966 1.00 28.09 N ATOM 210 CA LEU A 27 8.217 3.799 6.432 1.00 32.60 C ATOM 211 C LEU A 27 9.695 3.514 6.206 1.00 34.06 C ATOM 212 O LEU A 27 10.071 2.417 5.778 1.00 43.85 O ATOM 213 CB LEU A 27 7.470 3.627 5.103 1.00 26.54 C ATOM 214 CG LEU A 27 5.948 3.563 5.132 1.00 24.35 C ATOM 215 CD1 LEU A 27 5.418 3.238 3.740 1.00 31.18 C ATOM 216 CD2 LEU A 27 5.513 2.495 6.119 1.00 35.22 C ATOM 217 N LYS A 28 10.526 4.510 6.503 1.00 36.28 N ATOM 218 CA LYS A 28 11.973 4.417 6.318 1.00 42.75 C ATOM 219 C LYS A 28 12.304 3.702 5.019 1.00 37.98 C ATOM 220 O LYS A 28 12.994 2.681 5.007 1.00 36.18 O ATOM 221 CB LYS A 28 12.635 3.709 7.506 1.00 42.54 C ATOM 222 CG LYS A 28 11.993 2.391 7.922 1.00 46.84 C ATOM 223 CD LYS A 28 12.674 1.783 9.153 1.00 54.70 C ATOM 224 CE LYS A 28 12.660 2.730 10.355 1.00 56.61 C ATOM 225 NZ LYS A 28 13.595 3.886 10.171 1.00 65.61 N ATOM 226 N VAL A 29 11.796 4.254 3.923 1.00 33.32 N ATOM 227 CA VAL A 29 12.026 3.691 2.604 1.00 36.04 C ATOM 228 C VAL A 29 13.509 3.757 2.248 1.00 35.72 C ATOM 229 O VAL A 29 14.117 4.823 2.293 1.00 29.43 O ATOM 230 CB VAL A 29 11.222 4.451 1.532 1.00 26.40 C ATOM 231 CG1 VAL A 29 11.432 3.804 0.178 1.00 29.13 C ATOM 232 CG2 VAL A 29 9.747 4.455 1.901 1.00 32.95 C ATOM 233 N ALA A 30 14.082 2.615 1.887 1.00 41.56 N ATOM 234 CA ALA A 30 15.496 2.542 1.536 1.00 41.60 C ATOM 235 C ALA A 30 15.855 3.426 0.350 1.00 46.63 C ATOM 236 O ALA A 30 15.095 3.532 -0.614 1.00 45.18 O ATOM 237 CB ALA A 30 15.879 1.103 1.239 1.00 46.42 C ATOM 238 N GLN A 31 17.024 4.056 0.425 1.00 44.31 N ATOM 239 CA GLN A 31 17.486 4.917 -0.656 1.00 47.50 C ATOM 240 C GLN A 31 16.379 5.864 -1.099 1.00 48.48 C ATOM 241 O GLN A 31 16.120 6.022 -2.292 1.00 45.32 O ATOM 242 CB GLN A 31 17.948 4.052 -1.830 1.00 52.05 C ATOM 243 CG GLN A 31 19.145 3.181 -1.480 1.00 59.71 C ATOM 244 CD GLN A 31 19.524 2.205 -2.579 1.00 65.44 C ATOM 245 OE1 GLN A 31 20.582 1.573 -2.518 1.00 65.92 O ATOM 246 NE2 GLN A 31 18.660 2.066 -3.584 1.00 58.21 N ATOM 247 N ALA A 32 15.726 6.483 -0.122 1.00 44.16 N ATOM 248 CA ALA A 32 14.642 7.417 -0.390 1.00 41.81 C ATOM 249 C ALA A 32 15.106 8.577 -1.261 1.00 42.96 C ATOM 250 O ALA A 32 14.294 9.226 -1.918 1.00 41.87 O ATOM 251 CB ALA A 32 14.079 7.945 0.921 1.00 34.52 C ATOM 252 N GLU A 33 16.411 8.831 -1.267 1.00 46.17 N ATOM 253 CA GLU A 33 16.967 9.924 -2.061 1.00 49.04 C ATOM 254 C GLU A 33 16.675 9.702 -3.536 1.00 49.82 C ATOM 255 O GLU A 33 16.265 10.619 -4.244 1.00 49.48 O ATOM 256 CB GLU A 33 18.481 10.027 -1.855 1.00 53.98 C ATOM 257 CG GLU A 33 18.917 10.100 -0.401 1.00 58.25 C ATOM 258 CD GLU A 33 19.437 8.770 0.118 1.00 65.46 C ATOM 259 OE1 GLU A 33 18.676 7.778 0.101 1.00 57.50 O ATOM 260 OE2 GLU A 33 20.614 8.719 0.543 1.00 64.85 O ATOM 261 N TYR A 34 16.892 8.475 -3.996 1.00 49.68 N ATOM 262 CA TYR A 34 16.643 8.146 -5.386 1.00 51.13 C ATOM 263 C TYR A 34 15.628 7.014 -5.559 1.00 50.67 C ATOM 264 O TYR A 34 15.942 5.931 -6.062 1.00 57.49 O ATOM 265 CB TYR A 34 17.966 7.834 -6.097 1.00 59.80 C ATOM 266 CG TYR A 34 18.692 9.080 -6.584 1.00 66.68 C ATOM 267 CD1 TYR A 34 19.032 10.108 -5.698 1.00 66.32 C ATOM 268 CD2 TYR A 34 18.995 9.254 -7.939 1.00 70.34 C ATOM 269 CE1 TYR A 34 19.652 11.281 -6.148 1.00 70.10 C ATOM 270 CE2 TYR A 34 19.620 10.423 -8.402 1.00 72.07 C ATOM 271 CZ TYR A 34 19.941 11.430 -7.505 1.00 72.37 C ATOM 272 OH TYR A 34 20.545 12.588 -7.953 1.00 66.65 O ATOM 273 N VAL A 35 14.406 7.282 -5.107 1.00 37.50 N ATOM 274 CA VAL A 35 13.289 6.350 -5.221 1.00 31.05 C ATOM 275 C VAL A 35 12.183 7.150 -5.901 1.00 23.68 C ATOM 276 O VAL A 35 12.113 8.366 -5.739 1.00 27.35 O ATOM 277 CB VAL A 35 12.792 5.862 -3.829 1.00 32.85 C ATOM 278 CG1 VAL A 35 12.327 7.039 -2.985 1.00 30.87 C ATOM 279 CG2 VAL A 35 11.659 4.858 -4.001 1.00 25.71 C ATOM 280 N THR A 36 11.340 6.484 -6.682 1.00 23.64 N ATOM 281 CA THR A 36 10.245 7.167 -7.360 1.00 26.20 C ATOM 282 C THR A 36 8.948 6.819 -6.648 1.00 25.02 C ATOM 283 O THR A 36 8.690 5.649 -6.345 1.00 20.81 O ATOM 284 CB THR A 36 10.113 6.727 -8.837 1.00 27.72 C ATOM 285 OG1 THR A 36 11.284 7.116 -9.566 1.00 30.36 O ATOM 286 CG2 THR A 36 8.881 7.361 -9.473 1.00 21.51 C ATOM 287 N VAL A 37 8.125 7.826 -6.384 1.00 18.96 N ATOM 288 CA VAL A 37 6.865 7.583 -5.695 1.00 21.77 C ATOM 289 C VAL A 37 5.648 7.793 -6.578 1.00 19.00 C ATOM 290 O VAL A 37 5.532 8.812 -7.251 1.00 17.31 O ATOM 291 CB VAL A 37 6.721 8.493 -4.456 1.00 21.57 C ATOM 292 CG1 VAL A 37 5.405 8.187 -3.738 1.00 21.36 C ATOM 293 CG2 VAL A 37 7.901 8.279 -3.511 1.00 20.30 C ATOM 294 N GLU A 38 4.746 6.816 -6.573 1.00 19.48 N ATOM 295 CA GLU A 38 3.510 6.913 -7.340 1.00 15.28 C ATOM 296 C GLU A 38 2.348 6.962 -6.362 1.00 20.16 C ATOM 297 O GLU A 38 2.302 6.195 -5.401 1.00 17.35 O ATOM 298 CB GLU A 38 3.337 5.716 -8.282 1.00 22.34 C ATOM 299 CG GLU A 38 3.994 5.895 -9.644 1.00 48.05 C ATOM 300 CD GLU A 38 3.611 4.805 -10.633 1.00 53.76 C ATOM 301 OE1 GLU A 38 2.395 4.608 -10.867 1.00 50.93 O ATOM 302 OE2 GLU A 38 4.525 4.150 -11.180 1.00 59.07 O ATOM 303 N LEU A 39 1.427 7.892 -6.601 1.00 18.07 N ATOM 304 CA LEU A 39 0.252 8.053 -5.755 1.00 23.40 C ATOM 305 C LEU A 39 -0.968 7.952 -6.657 1.00 23.41 C ATOM 306 O LEU A 39 -1.143 8.754 -7.576 1.00 20.08 O ATOM 307 CB LEU A 39 0.280 9.414 -5.051 1.00 20.23 C ATOM 308 CG LEU A 39 -0.958 9.772 -4.228 1.00 22.51 C ATOM 309 CD1 LEU A 39 -1.233 8.675 -3.187 1.00 20.57 C ATOM 310 CD2 LEU A 39 -0.737 11.109 -3.543 1.00 20.87 C ATOM 311 N ASN A 40 -1.798 6.948 -6.393 1.00 20.41 N ATOM 312 CA ASN A 40 -3.004 6.697 -7.175 1.00 22.58 C ATOM 313 C ASN A 40 -2.719 6.621 -8.680 1.00 24.27 C ATOM 314 O ASN A 40 -3.459 7.170 -9.502 1.00 27.16 O ATOM 315 CB ASN A 40 -4.074 7.757 -6.867 1.00 23.11 C ATOM 316 CG ASN A 40 -4.545 7.697 -5.415 1.00 25.27 C ATOM 317 OD1 ASN A 40 -4.499 6.636 -4.786 1.00 15.56 O ATOM 318 ND2 ASN A 40 -5.020 8.823 -4.889 1.00 21.93 N ATOM 319 N GLY A 41 -1.629 5.935 -9.021 1.00 26.12 N ATOM 320 CA GLY A 41 -1.253 5.732 -10.410 1.00 30.94 C ATOM 321 C GLY A 41 -0.554 6.866 -11.122 1.00 34.00 C ATOM 322 O GLY A 41 -0.402 6.841 -12.347 1.00 33.27 O ATOM 323 N GLU A 42 -0.121 7.865 -10.368 1.00 25.86 N ATOM 324 CA GLU A 42 0.561 8.997 -10.968 1.00 28.11 C ATOM 325 C GLU A 42 1.919 9.199 -10.321 1.00 24.74 C ATOM 326 O GLU A 42 2.036 9.211 -9.095 1.00 22.31 O ATOM 327 CB GLU A 42 -0.294 10.241 -10.804 1.00 27.98 C ATOM 328 CG GLU A 42 0.395 11.517 -11.183 1.00 41.76 C ATOM 329 CD GLU A 42 -0.543 12.694 -11.091 1.00 53.11 C ATOM 330 OE1 GLU A 42 -1.318 12.751 -10.110 1.00 54.15 O ATOM 331 OE2 GLU A 42 -0.500 13.562 -11.989 1.00 55.11 O ATOM 332 N VAL A 43 2.946 9.336 -11.150 1.00 22.57 N ATOM 333 CA VAL A 43 4.288 9.553 -10.652 1.00 22.40 C ATOM 334 C VAL A 43 4.360 10.968 -10.095 1.00 26.08 C ATOM 335 O VAL A 43 3.943 11.931 -10.745 1.00 26.75 O ATOM 336 CB VAL A 43 5.344 9.382 -11.770 1.00 18.84 C ATOM 337 CG1 VAL A 43 6.704 9.837 -11.275 1.00 25.92 C ATOM 338 CG2 VAL A 43 5.408 7.924 -12.211 1.00 20.32 C ATOM 339 N LEU A 44 4.881 11.083 -8.880 1.00 18.56 N ATOM 340 CA LEU A 44 4.998 12.373 -8.202 1.00 26.02 C ATOM 341 C LEU A 44 6.353 13.038 -8.387 1.00 24.90 C ATOM 342 O LEU A 44 7.353 12.371 -8.641 1.00 20.24 O ATOM 343 CB LEU A 44 4.760 12.184 -6.702 1.00 24.96 C ATOM 344 CG LEU A 44 3.345 12.090 -6.132 1.00 25.72 C ATOM 345 CD1 LEU A 44 2.433 11.286 -7.029 1.00 41.80 C ATOM 346 CD2 LEU A 44 3.432 11.472 -4.744 1.00 27.07 C ATOM 347 N GLU A 45 6.380 14.359 -8.251 1.00 27.23 N ATOM 348 CA GLU A 45 7.630 15.104 -8.351 1.00 25.95 C ATOM 349 C GLU A 45 8.139 15.326 -6.934 1.00 28.74 C ATOM 350 O GLU A 45 7.406 15.806 -6.067 1.00 23.83 O ATOM 351 CB GLU A 45 7.406 16.445 -9.043 1.00 30.08 C ATOM 352 CG GLU A 45 7.155 16.299 -10.527 1.00 48.45 C ATOM 353 CD GLU A 45 6.991 17.628 -11.233 1.00 64.16 C ATOM 354 OE1 GLU A 45 7.026 17.632 -12.485 1.00 68.70 O ATOM 355 OE2 GLU A 45 6.820 18.663 -10.546 1.00 63.62 O ATOM 356 N ARG A 46 9.395 14.961 -6.707 1.00 26.28 N ATOM 357 CA ARG A 46 10.018 15.094 -5.399 1.00 32.74 C ATOM 358 C ARG A 46 9.863 16.493 -4.802 1.00 30.93 C ATOM 359 O ARG A 46 9.829 16.653 -3.584 1.00 27.39 O ATOM 360 CB ARG A 46 11.500 14.719 -5.507 1.00 33.75 C ATOM 361 CG ARG A 46 12.308 14.855 -4.222 1.00 40.43 C ATOM 362 CD ARG A 46 13.667 14.180 -4.370 1.00 41.90 C ATOM 363 NE ARG A 46 13.517 12.733 -4.502 1.00 49.27 N ATOM 364 CZ ARG A 46 13.149 11.930 -3.508 1.00 49.92 C ATOM 365 NH1 ARG A 46 13.028 10.625 -3.716 1.00 44.82 N ATOM 366 NH2 ARG A 46 12.920 12.431 -2.299 1.00 45.70 N ATOM 367 N GLU A 47 9.755 17.497 -5.665 1.00 29.74 N ATOM 368 CA GLU A 47 9.622 18.890 -5.236 1.00 33.90 C ATOM 369 C GLU A 47 8.317 19.148 -4.478 1.00 33.96 C ATOM 370 O GLU A 47 8.232 20.067 -3.658 1.00 32.17 O ATOM 371 CB GLU A 47 9.680 19.809 -6.458 1.00 42.61 C ATOM 372 CG GLU A 47 10.076 21.244 -6.159 1.00 53.96 C ATOM 373 CD GLU A 47 11.551 21.378 -5.826 1.00 67.88 C ATOM 374 OE1 GLU A 47 11.993 22.506 -5.517 1.00 70.79 O ATOM 375 OE2 GLU A 47 12.269 20.356 -5.876 1.00 72.06 O ATOM 376 N ALA A 48 7.304 18.334 -4.752 1.00 26.39 N ATOM 377 CA ALA A 48 6.003 18.497 -4.118 1.00 31.67 C ATOM 378 C ALA A 48 5.711 17.482 -3.009 1.00 25.41 C ATOM 379 O ALA A 48 4.566 17.348 -2.570 1.00 25.16 O ATOM 380 CB ALA A 48 4.909 18.425 -5.177 1.00 24.01 C ATOM 381 N PHE A 49 6.736 16.771 -2.558 1.00 23.73 N ATOM 382 CA PHE A 49 6.559 15.778 -1.507 1.00 25.13 C ATOM 383 C PHE A 49 5.996 16.369 -0.214 1.00 24.45 C ATOM 384 O PHE A 49 5.194 15.725 0.461 1.00 20.50 O ATOM 385 CB PHE A 49 7.886 15.066 -1.221 1.00 26.20 C ATOM 386 CG PHE A 49 8.218 13.965 -2.195 1.00 25.49 C ATOM 387 CD1 PHE A 49 7.476 13.789 -3.358 1.00 23.95 C ATOM 388 CD2 PHE A 49 9.284 13.105 -1.949 1.00 23.19 C ATOM 389 CE1 PHE A 49 7.793 12.777 -4.267 1.00 20.80 C ATOM 390 CE2 PHE A 49 9.612 12.088 -2.851 1.00 25.15 C ATOM 391 CZ PHE A 49 8.860 11.928 -4.010 1.00 19.78 C ATOM 392 N ASP A 50 6.394 17.591 0.135 1.00 22.77 N ATOM 393 CA ASP A 50 5.883 18.195 1.363 1.00 28.80 C ATOM 394 C ASP A 50 4.415 18.598 1.270 1.00 24.30 C ATOM 395 O ASP A 50 3.709 18.619 2.283 1.00 28.82 O ATOM 396 CB ASP A 50 6.696 19.433 1.764 1.00 31.15 C ATOM 397 CG ASP A 50 8.120 19.101 2.154 1.00 39.15 C ATOM 398 OD1 ASP A 50 8.343 18.077 2.839 1.00 36.95 O ATOM 399 OD2 ASP A 50 9.026 19.882 1.784 1.00 38.24 O ATOM 400 N ALA A 51 3.957 18.919 0.063 1.00 15.60 N ATOM 401 CA ALA A 51 2.573 19.350 -0.140 1.00 27.59 C ATOM 402 C ALA A 51 1.591 18.236 -0.502 1.00 20.42 C ATOM 403 O ALA A 51 0.400 18.324 -0.200 1.00 23.02 O ATOM 404 CB ALA A 51 2.528 20.438 -1.208 1.00 27.36 C ATOM 405 N THR A 52 2.096 17.194 -1.146 1.00 20.71 N ATOM 406 CA THR A 52 1.265 16.076 -1.557 1.00 22.31 C ATOM 407 C THR A 52 0.850 15.261 -0.340 1.00 21.37 C ATOM 408 O THR A 52 1.688 14.843 0.464 1.00 19.23 O ATOM 409 CB THR A 52 2.021 15.194 -2.564 1.00 21.31 C ATOM 410 OG1 THR A 52 2.482 16.010 -3.647 1.00 22.10 O ATOM 411 CG2 THR A 52 1.113 14.107 -3.116 1.00 19.73 C ATOM 412 N THR A 53 -0.448 15.024 -0.210 1.00 16.25 N ATOM 413 CA THR A 53 -0.953 14.292 0.939 1.00 23.06 C ATOM 414 C THR A 53 -1.595 12.951 0.605 1.00 21.25 C ATOM 415 O THR A 53 -2.301 12.809 -0.393 1.00 19.71 O ATOM 416 CB THR A 53 -1.976 15.149 1.700 1.00 30.39 C ATOM 417 OG1 THR A 53 -1.478 16.491 1.807 1.00 36.34 O ATOM 418 CG2 THR A 53 -2.193 14.593 3.094 1.00 34.63 C ATOM 419 N VAL A 54 -1.336 11.973 1.464 1.00 19.99 N ATOM 420 CA VAL A 54 -1.881 10.635 1.316 1.00 19.11 C ATOM 421 C VAL A 54 -2.968 10.475 2.361 1.00 19.68 C ATOM 422 O VAL A 54 -2.733 10.711 3.544 1.00 25.12 O ATOM 423 CB VAL A 54 -0.793 9.567 1.541 1.00 27.27 C ATOM 424 CG1 VAL A 54 -1.371 8.184 1.295 1.00 28.60 C ATOM 425 CG2 VAL A 54 0.391 9.831 0.615 1.00 23.74 C ATOM 426 N LYS A 55 -4.165 10.091 1.926 1.00 21.08 N ATOM 427 CA LYS A 55 -5.282 9.927 2.853 1.00 23.18 C ATOM 428 C LYS A 55 -5.806 8.494 2.863 1.00 27.77 C ATOM 429 O LYS A 55 -5.349 7.652 2.093 1.00 17.73 O ATOM 430 CB LYS A 55 -6.407 10.893 2.471 1.00 25.46 C ATOM 431 CG LYS A 55 -5.951 12.348 2.386 1.00 33.13 C ATOM 432 CD LYS A 55 -7.081 13.274 1.952 1.00 41.39 C ATOM 433 CE LYS A 55 -6.601 14.719 1.843 1.00 36.77 C ATOM 434 NZ LYS A 55 -7.696 15.636 1.441 1.00 38.58 N ATOM 435 N ASP A 56 -6.756 8.223 3.754 1.00 22.33 N ATOM 436 CA ASP A 56 -7.342 6.886 3.852 1.00 23.42 C ATOM 437 C ASP A 56 -7.810 6.421 2.474 1.00 20.84 C ATOM 438 O ASP A 56 -8.478 7.160 1.750 1.00 17.31 O ATOM 439 CB ASP A 56 -8.534 6.899 4.817 1.00 27.23 C ATOM 440 CG ASP A 56 -9.183 5.532 4.963 1.00 33.89 C ATOM 441 OD1 ASP A 56 -8.655 4.689 5.718 1.00 33.14 O ATOM 442 OD2 ASP A 56 -10.221 5.295 4.307 1.00 38.40 O ATOM 443 N GLY A 57 -7.447 5.198 2.106 1.00 18.47 N ATOM 444 CA GLY A 57 -7.860 4.666 0.824 1.00 20.58 C ATOM 445 C GLY A 57 -6.940 4.930 -0.358 1.00 20.17 C ATOM 446 O GLY A 57 -7.154 4.365 -1.422 1.00 20.40 O ATOM 447 N ASP A 58 -5.923 5.775 -0.191 1.00 19.19 N ATOM 448 CA ASP A 58 -5.007 6.070 -1.295 1.00 19.06 C ATOM 449 C ASP A 58 -4.049 4.900 -1.554 1.00 19.04 C ATOM 450 O ASP A 58 -3.809 4.080 -0.667 1.00 17.86 O ATOM 451 CB ASP A 58 -4.199 7.341 -1.002 1.00 12.23 C ATOM 452 CG ASP A 58 -5.001 8.616 -1.213 1.00 27.04 C ATOM 453 OD1 ASP A 58 -6.067 8.559 -1.868 1.00 20.56 O ATOM 454 OD2 ASP A 58 -4.553 9.695 -0.743 1.00 22.61 O ATOM 455 N ALA A 59 -3.512 4.830 -2.770 1.00 13.91 N ATOM 456 CA ALA A 59 -2.583 3.764 -3.148 1.00 14.86 C ATOM 457 C ALA A 59 -1.220 4.358 -3.479 1.00 16.27 C ATOM 458 O ALA A 59 -1.089 5.140 -4.415 1.00 17.21 O ATOM 459 CB ALA A 59 -3.116 3.007 -4.351 1.00 19.15 C ATOM 460 N VAL A 60 -0.207 3.986 -2.711 1.00 13.33 N ATOM 461 CA VAL A 60 1.127 4.497 -2.954 1.00 15.58 C ATOM 462 C VAL A 60 2.055 3.381 -3.398 1.00 18.65 C ATOM 463 O VAL A 60 1.943 2.235 -2.944 1.00 16.30 O ATOM 464 CB VAL A 60 1.689 5.185 -1.690 1.00 18.37 C ATOM 465 CG1 VAL A 60 0.771 6.329 -1.283 1.00 21.97 C ATOM 466 CG2 VAL A 60 1.801 4.185 -0.547 1.00 27.41 C ATOM 467 N GLU A 61 2.967 3.712 -4.303 1.00 18.36 N ATOM 468 CA GLU A 61 3.921 2.728 -4.808 1.00 21.77 C ATOM 469 C GLU A 61 5.333 3.299 -4.763 1.00 20.67 C ATOM 470 O GLU A 61 5.555 4.465 -5.079 1.00 16.74 O ATOM 471 CB GLU A 61 3.578 2.367 -6.250 1.00 22.06 C ATOM 472 CG GLU A 61 2.187 1.815 -6.453 1.00 34.74 C ATOM 473 CD GLU A 61 1.819 1.752 -7.923 1.00 43.85 C ATOM 474 OE1 GLU A 61 1.577 2.823 -8.526 1.00 55.98 O ATOM 475 OE2 GLU A 61 1.785 0.639 -8.479 1.00 48.20 O ATOM 476 N PHE A 62 6.279 2.464 -4.362 1.00 17.32 N ATOM 477 CA PHE A 62 7.669 2.870 -4.295 1.00 22.80 C ATOM 478 C PHE A 62 8.433 2.082 -5.347 1.00 21.95 C ATOM 479 O PHE A 62 8.492 0.853 -5.293 1.00 24.36 O ATOM 480 CB PHE A 62 8.230 2.608 -2.897 1.00 17.51 C ATOM 481 CG PHE A 62 7.512 3.362 -1.815 1.00 23.43 C ATOM 482 CD1 PHE A 62 7.451 4.747 -1.844 1.00 18.91 C ATOM 483 CD2 PHE A 62 6.869 2.688 -0.784 1.00 25.84 C ATOM 484 CE1 PHE A 62 6.757 5.454 -0.868 1.00 20.41 C ATOM 485 CE2 PHE A 62 6.170 3.386 0.200 1.00 18.12 C ATOM 486 CZ PHE A 62 6.117 4.763 0.154 1.00 20.83 C ATOM 487 N LEU A 63 8.994 2.796 -6.318 1.00 20.82 N ATOM 488 CA LEU A 63 9.729 2.157 -7.403 1.00 19.24 C ATOM 489 C LEU A 63 11.154 2.704 -7.517 1.00 20.61 C ATOM 490 O LEU A 63 11.418 3.862 -7.182 1.00 18.16 O ATOM 491 CB LEU A 63 8.993 2.375 -8.730 1.00 23.91 C ATOM 492 CG LEU A 63 7.461 2.245 -8.764 1.00 27.16 C ATOM 493 CD1 LEU A 63 6.972 2.526 -10.176 1.00 36.46 C ATOM 494 CD2 LEU A 63 7.028 0.865 -8.311 1.00 38.65 C ATOM 495 N TYR A 64 12.069 1.860 -7.993 1.00 17.43 N ATOM 496 CA TYR A 64 13.460 2.264 -8.158 1.00 21.26 C ATOM 497 C TYR A 64 13.915 1.990 -9.582 1.00 22.24 C ATOM 498 O TYR A 64 13.913 0.846 -10.029 1.00 20.64 O ATOM 499 CB TYR A 64 14.375 1.497 -7.201 1.00 22.02 C ATOM 500 CG TYR A 64 14.038 1.653 -5.739 1.00 26.32 C ATOM 501 CD1 TYR A 64 13.079 0.841 -5.131 1.00 35.31 C ATOM 502 CD2 TYR A 64 14.688 2.606 -4.958 1.00 24.40 C ATOM 503 CE1 TYR A 64 12.782 0.971 -3.772 1.00 32.27 C ATOM 504 CE2 TYR A 64 14.401 2.745 -3.609 1.00 29.32 C ATOM 505 CZ TYR A 64 13.448 1.926 -3.023 1.00 35.75 C ATOM 506 OH TYR A 64 13.168 2.070 -1.685 1.00 33.97 O ATOM 507 N PHE A 65 14.310 3.040 -10.290 1.00 25.75 N ATOM 508 CA PHE A 65 14.774 2.889 -11.658 1.00 26.08 C ATOM 509 C PHE A 65 16.294 2.995 -11.753 1.00 33.70 C ATOM 510 O PHE A 65 16.896 3.928 -11.224 1.00 30.75 O ATOM 511 CB PHE A 65 14.126 3.945 -12.549 1.00 26.45 C ATOM 512 CG PHE A 65 12.635 3.820 -12.643 1.00 39.84 C ATOM 513 CD1 PHE A 65 11.826 4.122 -11.551 1.00 30.15 C ATOM 514 CD2 PHE A 65 12.037 3.379 -13.822 1.00 35.47 C ATOM 515 CE1 PHE A 65 10.439 3.984 -11.631 1.00 39.70 C ATOM 516 CE2 PHE A 65 10.655 3.238 -13.914 1.00 33.01 C ATOM 517 CZ PHE A 65 9.852 3.542 -12.814 1.00 30.81 C HETATM 518 N MSE A 66 16.903 2.021 -12.425 1.00 31.33 N HETATM 519 CA MSE A 66 18.350 1.981 -12.627 1.00 39.95 C HETATM 520 C MSE A 66 18.602 1.507 -14.056 1.00 36.53 C HETATM 521 O MSE A 66 17.923 0.599 -14.537 1.00 30.52 O HETATM 522 CB MSE A 66 18.995 1.009 -11.640 1.00 44.60 C HETATM 523 CG MSE A 66 18.720 1.325 -10.184 1.00 67.65 C HETATM 524 SE MSE A 66 18.473 -0.295 -9.162 1.00 98.16 HETATM 525 CE MSE A 66 16.718 -0.758 -9.852 1.00 79.87 C ATOM 526 N GLY A 67 19.572 2.122 -14.731 1.00 38.33 N ATOM 527 CA GLY A 67 19.869 1.742 -16.104 1.00 52.11 C ATOM 528 C GLY A 67 20.555 2.848 -16.885 1.00 59.51 C ATOM 529 O GLY A 67 20.588 3.996 -16.442 1.00 62.56 O ATOM 530 N GLY A 68 21.088 2.514 -18.059 1.00 66.07 N ATOM 531 CA GLY A 68 21.791 3.504 -18.861 1.00 67.98 C ATOM 532 C GLY A 68 20.984 4.227 -19.924 1.00 71.48 C ATOM 533 O GLY A 68 21.247 4.072 -21.118 1.00 71.31 O ATOM 534 N GLY A 69 20.008 5.029 -19.498 1.00 75.34 N ATOM 535 CA GLY A 69 19.193 5.768 -20.447 1.00 74.50 C ATOM 536 C GLY A 69 18.459 6.954 -19.840 1.00 75.80 C ATOM 537 O GLY A 69 18.866 8.108 -20.107 1.00 76.04 O HETATM 538 O HOH A 79 -0.238 0.553 -3.799 1.00 22.18 O HETATM 539 O HOH A 80 -0.149 4.459 -7.173 1.00 28.06 O HETATM 540 O HOH A 81 8.775 10.425 -7.191 1.00 24.80 O HETATM 541 O HOH A 82 2.555 9.629 -14.143 1.00 27.06 O HETATM 542 O HOH A 83 2.463 14.098 -10.248 1.00 30.11 O HETATM 543 O HOH A 84 -6.480 1.757 -0.851 1.00 29.23 O HETATM 544 O HOH A 85 -5.252 -1.474 5.262 1.00 27.51 O HETATM 545 O HOH A 86 15.592 -1.175 -3.695 1.00 47.00 O HETATM 546 O HOH A 87 8.520 18.777 -0.848 1.00 33.04 O HETATM 547 O HOH A 88 -8.575 8.616 8.711 1.00 46.64 O HETATM 548 O HOH A 89 3.913 15.545 -8.132 1.00 31.69 O HETATM 549 O HOH A 90 13.841 5.678 -9.135 1.00 25.45 O HETATM 550 O HOH A 91 -7.128 10.810 -1.992 1.00 31.49 O HETATM 551 O HOH A 92 -4.778 -2.857 0.179 1.00 34.52 O HETATM 552 O HOH A 93 22.815 0.026 -18.011 1.00 47.27 O HETATM 553 O HOH A 94 2.603 -6.494 -3.354 1.00 30.44 O HETATM 554 O HOH A 95 11.417 16.336 -1.604 1.00 34.20 O HETATM 555 O HOH A 96 16.909 7.438 2.236 1.00 39.97 O HETATM 556 O HOH A 97 11.059 14.258 -9.129 1.00 35.67 O HETATM 557 O HOH A 98 21.143 4.046 -12.613 1.00 37.75 O HETATM 558 O HOH A 99 11.224 9.541 -10.786 1.00 40.66 O HETATM 559 O HOH A 100 -1.851 11.432 -7.662 1.00 40.11 O HETATM 560 O HOH A 101 10.851 15.031 0.704 1.00 30.84 O HETATM 561 O HOH A 102 12.377 12.730 8.587 1.00 44.94 O HETATM 562 O HOH A 103 -0.886 14.760 9.668 1.00 60.58 O HETATM 563 O HOH A 104 4.571 18.013 -9.161 1.00 34.65 O HETATM 564 O HOH A 105 -11.928 5.838 2.270 1.00 41.43 O HETATM 565 O HOH A 106 -0.979 15.566 6.034 1.00 34.22 O HETATM 566 O HOH A 107 -10.272 -0.748 8.980 1.00 51.84 O HETATM 567 O HOH A 108 -5.264 10.444 14.261 1.00 38.60 O HETATM 568 O HOH A 109 -1.067 12.413 13.422 1.00 53.24 O HETATM 569 O HOH A 110 -6.709 1.160 1.700 1.00 30.30 O HETATM 570 O HOH A 111 -6.231 -1.336 2.491 1.00 25.53 O HETATM 571 O HOH A 112 -9.680 1.452 2.090 1.00 39.21 O HETATM 572 O HOH A 113 -10.475 2.514 4.378 1.00 45.69 O HETATM 573 O HOH A 114 -6.942 3.977 -4.470 1.00 40.78 O HETATM 574 O HOH A 115 -8.623 7.855 -0.995 1.00 38.46 O HETATM 575 O HOH A 116 -10.744 6.310 -0.743 1.00 47.79 O HETATM 576 O HOH A 117 -5.555 16.361 8.410 1.00 51.05 O HETATM 577 O HOH A 118 7.018 17.458 5.673 1.00 30.02 O HETATM 578 O HOH A 119 8.473 16.625 7.566 1.00 38.78 O HETATM 579 O HOH A 120 1.550 14.756 10.235 1.00 67.65 O HETATM 580 O HOH A 121 3.340 0.447 6.545 1.00 52.92 O HETATM 581 O HOH A 122 -0.799 -0.659 -6.088 1.00 74.20 O HETATM 582 O HOH A 123 -1.012 21.076 1.181 1.00 87.24 O TER 583 HOH A 123 ENDMDL MASTER END