HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 02-AUG-07 2QTI TITLE CRYSTAL STRUCTURE OF THE UPF0352 PROTEIN SO_2176 FROM TITLE 2 SHEWANELLA ONEIDENSIS. NESG TARGET SOR77. COMPND MOL_ID: 1; COMPND 2 MOLECULE: UPF0352 PROTEIN SO_2176; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SHEWANELLA ONEIDENSIS MR-1; SOURCE 3 ORGANISM_TAXID: 211586; SOURCE 4 STRAIN: MR-1; SOURCE 5 GENE: SO_2176; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)+MAGIC; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET21 KEYWDS Y2176_SHEON, UPF0352, SO_2176, PF07208, NESG, SOR77, KEYWDS 2 STRUCTURAL GENOMICS, PSI-2, PROTEIN STRUCTURE INITIATIVE, KEYWDS 3 NORTHEAST STRUCTURAL GENOMICS CONSORTIUM, UNKNOWN FUNCTION EXPDTA X-RAY DIFFRACTION AUTHOR S.M.VOROBIEV,M.SU,J.SEETHARAMAN,A.P.KUZIN,D.WANG, AUTHOR 2 K.CUNNINGHAM,L.OWENS,M.MAGLAQUI,Y.FANG,R.XIAO,T.B.ACTON, AUTHOR 3 G.T.MONTELIONE,L.TONG,J.F.HUNT,NORTHEAST STRUCTURAL AUTHOR 4 GENOMICS CONSORTIUM (NESG) REVDAT 2 24-FEB-09 2QTI 1 VERSN REVDAT 1 21-AUG-07 2QTI 0 JRNL AUTH S.M.VOROBIEV,M.SU,J.SEETHARAMAN,A.P.KUZIN,D.WANG, JRNL AUTH 2 K.CUNNINGHAM,L.OWENS,M.MAGLAQUI,Y.FANG,R.XIAO, JRNL AUTH 3 T.B.ACTON,G.T.MONTELIONE,L.TONG,J.F.HUNT JRNL TITL CRYSTAL STRUCTURE OF THE UPF0352 PROTEIN SO_2176 JRNL TITL 2 FROM SHEWANELLA ONEIDENSIS. JRNL REF TO BE PUBLISHED JRNL REFN REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 2.30 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 1.1 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) : 2.30 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.32 REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 74338.720 REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000 REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 91.0 REMARK 3 NUMBER OF REFLECTIONS : 6260 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) : 0.223 REMARK 3 FREE R VALUE : 0.232 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.800 REMARK 3 FREE R VALUE TEST SET COUNT : 615 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.009 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 6 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.30 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.44 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 76.40 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 774 REMARK 3 BIN R VALUE (WORKING SET) : 0.2110 REMARK 3 BIN FREE R VALUE : 0.2060 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.70 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 93 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.021 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 498 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 19 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 24.90 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 44.30 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -1.28000 REMARK 3 B22 (A**2) : -1.28000 REMARK 3 B33 (A**2) : 2.56000 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) : 0.28 REMARK 3 ESD FROM SIGMAA (A) : 0.13 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) : 0.17 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.005 REMARK 3 BOND ANGLES (DEGREES) : 1.00 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 16.60 REMARK 3 IMPROPER ANGLES (DEGREES) : 0.72 REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED 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 : 0.40 REMARK 3 BSOL : 60.16 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 : PROTEIN_REP.PARAM REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM REMARK 3 PARAMETER FILE 3 : ION.PARAM REMARK 3 PARAMETER FILE 4 : NULL REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP REMARK 3 TOPOLOGY FILE 2 : WATER.TOP REMARK 3 TOPOLOGY FILE 3 : ION.TOP REMARK 3 TOPOLOGY FILE 4 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE FRIEDEL PAIRS WERE USED FOR REMARK 3 PHASING REMARK 4 REMARK 4 2QTI COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-AUG-07. REMARK 100 THE RCSB ID CODE IS RCSB044035. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 25-JUL-07 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 4.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : NSLS REMARK 200 BEAMLINE : X25 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97913 REMARK 200 MONOCHROMATOR : GRAPHITE REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 7182 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 12.700 REMARK 200 R MERGE (I) : 0.08000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 41.6000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.4 REMARK 200 DATA REDUNDANCY IN SHELL : 8.00 REMARK 200 R MERGE FOR SHELL (I) : 0.52700 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 4.470 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD REMARK 200 SOFTWARE USED: BNP, RESOLVE 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 (%): 44.38 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.21 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 40% PEG 1000, 0.1M AMMONIUM REMARK 280 PHOSPHATE, 0.1M SODIUM CITRATE PH 4.0, MICROBATCH UNDER OIL, REMARK 280 TEMPERATURE 291.0K 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 31.26400 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 25.28800 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 25.28800 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 46.89600 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 25.28800 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 25.28800 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 15.63200 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 25.28800 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 25.28800 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 46.89600 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 25.28800 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 25.28800 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 15.63200 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 31.26400 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: DIMER BY GEL FILTRATION. THE SECOND PART OF THE REMARK 300 BIOLOGICAL ASSEMBLY IS GENERATED BY Y, X, -Z+1 SYMMETRY OPERATOR. 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: 4180 ANGSTROM**2 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 350 BIOMT1 2 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 62.52800 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 MSE A 1 REMARK 465 ALA A 2 REMARK 465 ILE A 3 REMARK 465 GLN A 4 REMARK 465 SER A 5 REMARK 465 LYS A 6 REMARK 465 TYR A 7 REMARK 465 HIS A 75 REMARK 465 HIS A 76 REMARK 465 HIS A 77 REMARK 465 HIS A 78 REMARK 465 HIS A 79 REMARK 465 HIS A 80 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 ASN A 9 CG OD1 ND2 REMARK 470 GLN A 11 CG CD OE1 NE2 REMARK 470 GLU A 74 CG CD OE1 OE2 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 SER A 51 -39.19 -39.98 REMARK 500 LEU A 73 49.62 -87.27 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH A 115 DISTANCE = 6.77 ANGSTROMS REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: SOR77 RELATED DB: TARGETDB REMARK 900 RELATED ID: 2OTA RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF UPF0352 PROTEIN CPS_2611 FROM REMARK 900 COLWELLIA PSYCHRERYTHRAEA. NESG TARGET CSR4 (HOMOLOG REMARK 900 PROTEIN) REMARK 900 RELATED ID: 2JR2 RELATED DB: PDB REMARK 900 SOLUTION NMR STRUCTURE OF HOMODIMER CPS_2611 FROM COLWELLIA REMARK 900 PSYCHRERYTHRAEA. NESG TARGET CSR4 (HOMOLOG PROTEIN) DBREF 2QTI A 1 72 UNP Q8EF26 Y2176_SHEON 1 72 SEQADV 2QTI LEU A 73 UNP Q8EF26 EXPRESSION TAG SEQADV 2QTI GLU A 74 UNP Q8EF26 EXPRESSION TAG SEQADV 2QTI HIS A 75 UNP Q8EF26 EXPRESSION TAG SEQADV 2QTI HIS A 76 UNP Q8EF26 EXPRESSION TAG SEQADV 2QTI HIS A 77 UNP Q8EF26 EXPRESSION TAG SEQADV 2QTI HIS A 78 UNP Q8EF26 EXPRESSION TAG SEQADV 2QTI HIS A 79 UNP Q8EF26 EXPRESSION TAG SEQADV 2QTI HIS A 80 UNP Q8EF26 EXPRESSION TAG SEQRES 1 A 80 MSE ALA ILE GLN SER LYS TYR SER ASN THR GLN VAL GLU SEQRES 2 A 80 SER LEU ILE ALA GLU ILE LEU VAL VAL LEU GLU LYS HIS SEQRES 3 A 80 LYS ALA PRO THR ASP LEU SER LEU MSE ALA LEU GLY ASN SEQRES 4 A 80 CYS VAL THR HIS LEU LEU GLU ARG LYS VAL PRO SER GLU SEQRES 5 A 80 SER ARG GLN ALA VAL ALA GLU GLN PHE ALA LYS ALA LEU SEQRES 6 A 80 ALA GLN SER VAL LYS SER ASN LEU GLU HIS HIS HIS HIS SEQRES 7 A 80 HIS HIS MODRES 2QTI MSE A 35 MET SELENOMETHIONINE HET MSE A 35 8 HETNAM MSE SELENOMETHIONINE FORMUL 1 MSE C5 H11 N O2 SE FORMUL 2 HOH *19(H2 O) HELIX 1 1 SER A 8 LYS A 27 1 20 HELIX 2 2 PRO A 29 VAL A 49 1 21 HELIX 3 3 PRO A 50 LEU A 73 1 24 LINK C LEU A 34 N MSE A 35 1555 1555 1.32 LINK C MSE A 35 N ALA A 36 1555 1555 1.33 CRYST1 50.576 50.576 62.528 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 0.019772 0.000000 0.000000 0.00000 SCALE2 0.000000 0.019772 0.000000 0.00000 SCALE3 0.000000 0.000000 0.015993 0.00000 REMARK PdbStat -- REMARK PdbStat -- PDB COORDINATES FOR 2QTI.PDB, MODEL/S 1 2QTI.PDB REMARK PdbStat -- SEQRES 1 A 86 SER ASN THR GLN VAL GLU SER LEU ILE ALA GLU ILE LEU SEQRES 2 A 86 VAL VAL LEU GLU LYS HIS LYS ALA PRO THR ASP LEU SER SEQRES 3 A 86 LEU MSE ALA LEU GLY ASN CYS VAL THR HIS LEU LEU GLU SEQRES 4 A 86 ARG LYS VAL PRO SER GLU SER ARG GLN ALA VAL ALA GLU SEQRES 5 A 86 GLN PHE ALA LYS ALA LEU ALA GLN SER VAL LYS SER ASN SEQRES 6 A 86 LEU GLU HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 7 A 86 HOH HOH HOH HOH HOH HOH HOH HOH REMARK PdbStat -- REMARK PdbStat -- PDB COORDINATES FOR 2QTI.PDB, MODEL/S 1 2QTI.PDB REMARK PdbStat -- SEQRES 1 A 86 SER ASN THR GLN VAL GLU SER LEU ILE ALA GLU ILE LEU SEQRES 2 A 86 VAL VAL LEU GLU LYS HIS LYS ALA PRO THR ASP LEU SER SEQRES 3 A 86 LEU MSE ALA LEU GLY ASN CYS VAL THR HIS LEU LEU GLU SEQRES 4 A 86 ARG LYS VAL PRO SER GLU SER ARG GLN ALA VAL ALA GLU SEQRES 5 A 86 GLN PHE ALA LYS ALA LEU ALA GLN SER VAL LYS SER ASN SEQRES 6 A 86 LEU GLU HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 7 A 86 HOH HOH HOH HOH HOH HOH HOH HOH REMARK PdbStat -- REMARK PdbStat -- PDB COORDINATES FOR 2QTI.PDB, MODEL/S 1 2QTI.PDB REMARK PdbStat -- SEQRES 1 A 86 SER ASN THR GLN VAL GLU SER LEU ILE ALA GLU ILE LEU SEQRES 2 A 86 VAL VAL LEU GLU LYS HIS LYS ALA PRO THR ASP LEU SER SEQRES 3 A 86 LEU MSE ALA LEU GLY ASN CYS VAL THR HIS LEU LEU GLU SEQRES 4 A 86 ARG LYS VAL PRO SER GLU SER ARG GLN ALA VAL ALA GLU SEQRES 5 A 86 GLN PHE ALA LYS ALA LEU ALA GLN SER VAL LYS SER ASN SEQRES 6 A 86 LEU GLU HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 7 A 86 HOH HOH HOH HOH HOH HOH HOH HOH MODEL 1 REMARK CONFORMATION 1 ENERGY 0.0000 REMARK FAMILY or FILE: 2QTI.pdb ATOM 1 N SER A 8 12.731 -11.933 8.444 1.00 61.95 N ATOM 2 CA SER A 8 12.262 -10.561 8.780 1.00 60.83 C ATOM 3 C SER A 8 11.912 -9.826 7.490 1.00 60.70 C ATOM 4 O SER A 8 10.993 -9.008 7.458 1.00 61.70 O ATOM 5 CB SER A 8 13.358 -9.801 9.537 1.00 61.38 C ATOM 6 OG SER A 8 12.896 -8.542 9.998 1.00 59.73 O ATOM 7 N ASN A 9 12.648 -10.130 6.426 1.00 58.18 N ATOM 8 CA ASN A 9 12.413 -9.502 5.132 1.00 56.83 C ATOM 9 C ASN A 9 11.016 -9.843 4.636 1.00 55.92 C ATOM 10 O ASN A 9 10.330 -9.007 4.049 1.00 57.47 O ATOM 11 CB ASN A 9 13.450 -9.977 4.125 1.00 57.57 C ATOM 12 N THR A 10 10.602 -11.081 4.875 1.00 53.87 N ATOM 13 CA THR A 10 9.286 -11.537 4.450 1.00 51.49 C ATOM 14 C THR A 10 8.223 -10.850 5.301 1.00 50.82 C ATOM 15 O THR A 10 7.097 -10.634 4.856 1.00 51.95 O ATOM 16 CB THR A 10 9.158 -13.067 4.602 1.00 51.51 C ATOM 17 OG1 THR A 10 10.297 -13.703 4.007 1.00 51.59 O ATOM 18 CG2 THR A 10 7.899 -13.567 3.911 1.00 45.76 C ATOM 19 N GLN A 11 8.602 -10.505 6.528 1.00 49.84 N ATOM 20 CA GLN A 11 7.710 -9.836 7.464 1.00 47.27 C ATOM 21 C GLN A 11 7.479 -8.402 7.013 1.00 46.06 C ATOM 22 O GLN A 11 6.351 -7.911 7.017 1.00 45.54 O ATOM 23 CB GLN A 11 8.319 -9.850 8.860 1.00 51.26 C ATOM 24 N VAL A 12 8.562 -7.734 6.629 1.00 45.24 N ATOM 25 CA VAL A 12 8.484 -6.358 6.160 1.00 43.82 C ATOM 26 C VAL A 12 7.703 -6.332 4.857 1.00 40.11 C ATOM 27 O VAL A 12 6.746 -5.564 4.700 1.00 39.60 O ATOM 28 CB VAL A 12 9.888 -5.775 5.895 1.00 42.91 C ATOM 29 CG1 VAL A 12 9.770 -4.367 5.345 1.00 45.52 C ATOM 30 CG2 VAL A 12 10.703 -5.782 7.178 1.00 48.30 C ATOM 31 N GLU A 13 8.123 -7.191 3.932 1.00 40.23 N ATOM 32 CA GLU A 13 7.493 -7.297 2.625 1.00 38.44 C ATOM 33 C GLU A 13 5.995 -7.591 2.706 1.00 35.99 C ATOM 34 O GLU A 13 5.217 -7.034 1.934 1.00 39.38 O ATOM 35 CB GLU A 13 8.220 -8.357 1.800 1.00 41.20 C ATOM 36 CG GLU A 13 9.648 -7.939 1.478 1.00 47.84 C ATOM 37 CD GLU A 13 10.472 -9.045 0.847 1.00 55.81 C ATOM 38 OE1 GLU A 13 10.568 -10.138 1.449 1.00 50.80 O ATOM 39 OE2 GLU A 13 11.031 -8.815 -0.248 1.00 62.71 O ATOM 40 N SER A 14 5.592 -8.451 3.641 1.00 34.27 N ATOM 41 CA SER A 14 4.179 -8.777 3.815 1.00 33.98 C ATOM 42 C SER A 14 3.402 -7.552 4.278 1.00 34.25 C ATOM 43 O SER A 14 2.300 -7.299 3.797 1.00 35.81 O ATOM 44 CB SER A 14 4.005 -9.895 4.844 1.00 37.86 C ATOM 45 OG SER A 14 4.519 -11.110 4.346 1.00 38.10 O ATOM 46 N LEU A 15 3.974 -6.807 5.226 1.00 35.28 N ATOM 47 CA LEU A 15 3.340 -5.589 5.740 1.00 35.74 C ATOM 48 C LEU A 15 3.161 -4.618 4.592 1.00 34.65 C ATOM 49 O LEU A 15 2.081 -4.061 4.383 1.00 38.98 O ATOM 50 CB LEU A 15 4.215 -4.912 6.804 1.00 37.56 C ATOM 51 CG LEU A 15 3.865 -5.110 8.276 1.00 38.90 C ATOM 52 CD1 LEU A 15 4.611 -4.069 9.100 1.00 37.35 C ATOM 53 CD2 LEU A 15 2.367 -4.950 8.479 1.00 45.57 C ATOM 54 N ILE A 16 4.248 -4.431 3.850 1.00 34.68 N ATOM 55 CA ILE A 16 4.272 -3.534 2.707 1.00 29.61 C ATOM 56 C ILE A 16 3.203 -3.911 1.688 1.00 31.74 C ATOM 57 O ILE A 16 2.417 -3.067 1.252 1.00 34.92 O ATOM 58 CB ILE A 16 5.663 -3.570 2.038 1.00 29.71 C ATOM 59 CG1 ILE A 16 6.684 -2.889 2.954 1.00 26.53 C ATOM 60 CG2 ILE A 16 5.615 -2.895 0.674 1.00 24.93 C ATOM 61 CD1 ILE A 16 8.120 -3.163 2.580 1.00 30.24 C ATOM 62 N ALA A 17 3.167 -5.186 1.320 1.00 33.01 N ATOM 63 CA ALA A 17 2.194 -5.647 0.339 1.00 32.53 C ATOM 64 C ALA A 17 0.778 -5.343 0.812 1.00 31.36 C ATOM 65 O ALA A 17 -0.053 -4.834 0.058 1.00 33.74 O ATOM 66 CB ALA A 17 2.361 -7.146 0.105 1.00 32.09 C ATOM 67 N GLU A 18 0.516 -5.659 2.075 1.00 32.51 N ATOM 68 CA GLU A 18 -0.792 -5.451 2.655 1.00 34.08 C ATOM 69 C GLU A 18 -1.191 -3.987 2.588 1.00 34.74 C ATOM 70 O GLU A 18 -2.331 -3.658 2.271 1.00 39.65 O ATOM 71 CB GLU A 18 -0.789 -5.936 4.103 1.00 35.30 C ATOM 72 CG GLU A 18 -1.805 -7.007 4.377 1.00 38.04 C ATOM 73 CD GLU A 18 -1.746 -7.499 5.803 1.00 40.81 C ATOM 74 OE1 GLU A 18 -0.717 -8.116 6.171 1.00 39.38 O ATOM 75 OE2 GLU A 18 -2.726 -7.264 6.551 1.00 45.00 O ATOM 76 N ILE A 19 -0.249 -3.100 2.892 1.00 37.26 N ATOM 77 CA ILE A 19 -0.534 -1.673 2.836 1.00 32.97 C ATOM 78 C ILE A 19 -0.734 -1.242 1.393 1.00 30.40 C ATOM 79 O ILE A 19 -1.628 -0.461 1.092 1.00 35.05 O ATOM 80 CB ILE A 19 0.610 -0.860 3.449 1.00 35.10 C ATOM 81 CG1 ILE A 19 0.726 -1.188 4.939 1.00 29.80 C ATOM 82 CG2 ILE A 19 0.370 0.624 3.230 1.00 33.01 C ATOM 83 CD1 ILE A 19 2.030 -0.726 5.577 1.00 30.62 C ATOM 84 N LEU A 20 0.086 -1.762 0.488 1.00 33.15 N ATOM 85 CA LEU A 20 -0.037 -1.371 -0.913 1.00 33.94 C ATOM 86 C LEU A 20 -1.364 -1.794 -1.516 1.00 35.58 C ATOM 87 O LEU A 20 -1.940 -1.068 -2.330 1.00 39.84 O ATOM 88 CB LEU A 20 1.120 -1.942 -1.738 1.00 34.16 C ATOM 89 CG LEU A 20 2.490 -1.319 -1.452 1.00 33.91 C ATOM 90 CD1 LEU A 20 3.562 -1.974 -2.344 1.00 27.86 C ATOM 91 CD2 LEU A 20 2.420 0.185 -1.697 1.00 28.13 C ATOM 92 N VAL A 21 -1.845 -2.969 -1.120 1.00 35.54 N ATOM 93 CA VAL A 21 -3.116 -3.470 -1.620 1.00 33.57 C ATOM 94 C VAL A 21 -4.236 -2.537 -1.165 1.00 33.32 C ATOM 95 O VAL A 21 -5.184 -2.286 -1.907 1.00 35.42 O ATOM 96 CB VAL A 21 -3.377 -4.904 -1.113 1.00 36.75 C ATOM 97 CG1 VAL A 21 -4.835 -5.263 -1.267 1.00 29.39 C ATOM 98 CG2 VAL A 21 -2.508 -5.884 -1.900 1.00 37.11 C ATOM 99 N VAL A 22 -4.122 -2.027 0.058 1.00 35.14 N ATOM 100 CA VAL A 22 -5.112 -1.095 0.586 1.00 35.25 C ATOM 101 C VAL A 22 -5.216 0.098 -0.357 1.00 37.22 C ATOM 102 O VAL A 22 -6.312 0.521 -0.717 1.00 39.21 O ATOM 103 CB VAL A 22 -4.715 -0.589 1.996 1.00 36.52 C ATOM 104 CG1 VAL A 22 -5.530 0.657 2.363 1.00 35.93 C ATOM 105 CG2 VAL A 22 -4.949 -1.691 3.017 1.00 30.38 C ATOM 106 N LEU A 23 -4.063 0.631 -0.757 1.00 39.97 N ATOM 107 CA LEU A 23 -4.025 1.772 -1.667 1.00 39.02 C ATOM 108 C LEU A 23 -4.572 1.386 -3.040 1.00 40.21 C ATOM 109 O LEU A 23 -5.333 2.137 -3.647 1.00 40.27 O ATOM 110 CB LEU A 23 -2.591 2.298 -1.810 1.00 36.83 C ATOM 111 CG LEU A 23 -1.897 2.771 -0.529 1.00 36.06 C ATOM 112 CD1 LEU A 23 -0.462 3.168 -0.837 1.00 35.88 C ATOM 113 CD2 LEU A 23 -2.653 3.946 0.072 1.00 28.06 C ATOM 114 N GLU A 24 -4.178 0.211 -3.522 1.00 43.09 N ATOM 115 CA GLU A 24 -4.627 -0.280 -4.819 1.00 47.44 C ATOM 116 C GLU A 24 -6.137 -0.533 -4.838 1.00 46.44 C ATOM 117 O GLU A 24 -6.806 -0.229 -5.822 1.00 47.57 O ATOM 118 CB GLU A 24 -3.848 -1.549 -5.183 1.00 47.70 C ATOM 119 CG GLU A 24 -2.350 -1.287 -5.324 1.00 54.55 C ATOM 120 CD GLU A 24 -1.523 -2.549 -5.503 1.00 56.91 C ATOM 121 OE1 GLU A 24 -1.625 -3.456 -4.650 1.00 68.52 O ATOM 122 OE2 GLU A 24 -0.761 -2.629 -6.491 1.00 69.77 O ATOM 123 N LYS A 25 -6.680 -1.075 -3.753 1.00 47.64 N ATOM 124 CA LYS A 25 -8.119 -1.326 -3.685 1.00 50.04 C ATOM 125 C LYS A 25 -8.936 -0.045 -3.834 1.00 52.38 C ATOM 126 O LYS A 25 -10.035 -0.066 -4.406 1.00 56.84 O ATOM 127 CB LYS A 25 -8.497 -2.003 -2.366 1.00 47.77 C ATOM 128 CG LYS A 25 -8.105 -3.459 -2.274 1.00 53.29 C ATOM 129 CD LYS A 25 -8.874 -4.167 -1.176 1.00 55.72 C ATOM 130 CE LYS A 25 -8.580 -5.653 -1.216 1.00 55.69 C ATOM 131 NZ LYS A 25 -8.734 -6.167 -2.609 1.00 56.85 N ATOM 132 N HIS A 26 -8.420 1.060 -3.302 1.00 52.86 N ATOM 133 CA HIS A 26 -9.097 2.353 -3.402 1.00 52.98 C ATOM 134 C HIS A 26 -8.761 3.049 -4.722 1.00 53.29 C ATOM 135 O HIS A 26 -9.347 4.080 -5.045 1.00 53.79 O ATOM 136 CB HIS A 26 -8.660 3.274 -2.249 1.00 53.22 C ATOM 137 CG HIS A 26 -9.177 2.860 -0.909 1.00 53.57 C ATOM 138 ND1 HIS A 26 -8.865 1.650 -0.329 1.00 52.84 N ATOM 139 CD2 HIS A 26 -9.972 3.508 -0.024 1.00 51.83 C ATOM 140 CE1 HIS A 26 -9.441 1.572 0.856 1.00 44.67 C ATOM 141 NE2 HIS A 26 -10.118 2.685 1.067 1.00 49.31 N ATOM 142 N LYS A 27 -7.796 2.500 -5.457 1.00 54.11 N ATOM 143 CA LYS A 27 -7.361 3.086 -6.714 1.00 54.74 C ATOM 144 C LYS A 27 -6.977 4.522 -6.381 1.00 53.01 C ATOM 145 O LYS A 27 -7.125 5.432 -7.193 1.00 52.56 O ATOM 146 CB LYS A 27 -8.495 3.065 -7.748 1.00 56.29 C ATOM 147 CG LYS A 27 -8.856 1.673 -8.308 1.00 63.00 C ATOM 148 CD LYS A 27 -7.634 0.937 -8.844 1.00 74.40 C ATOM 149 CE LYS A 27 -7.973 -0.530 -9.087 1.00 84.03 C ATOM 150 NZ LYS A 27 -6.817 -1.324 -9.587 1.00 85.68 N ATOM 151 N ALA A 28 -6.514 4.708 -5.154 1.00 51.49 N ATOM 152 CA ALA A 28 -6.127 6.016 -4.680 1.00 48.95 C ATOM 153 C ALA A 28 -4.988 6.607 -5.502 1.00 47.66 C ATOM 154 O ALA A 28 -3.996 5.934 -5.795 1.00 47.88 O ATOM 155 CB ALA A 28 -5.724 5.939 -3.205 1.00 49.16 C ATOM 156 N PRO A 29 -5.119 7.885 -5.898 1.00 45.02 N ATOM 157 CA PRO A 29 -4.096 8.586 -6.685 1.00 44.12 C ATOM 158 C PRO A 29 -2.787 8.639 -5.902 1.00 41.40 C ATOM 159 O PRO A 29 -2.775 8.379 -4.699 1.00 40.78 O ATOM 160 CB PRO A 29 -4.696 9.970 -6.871 1.00 42.12 C ATOM 161 CG PRO A 29 -6.145 9.690 -6.939 1.00 43.60 C ATOM 162 CD PRO A 29 -6.349 8.688 -5.817 1.00 44.47 C ATOM 163 N THR A 30 -1.695 8.963 -6.584 1.00 40.50 N ATOM 164 CA THR A 30 -0.402 9.050 -5.935 1.00 42.27 C ATOM 165 C THR A 30 -0.427 10.067 -4.778 1.00 41.35 C ATOM 166 O THR A 30 -0.045 9.749 -3.650 1.00 43.62 O ATOM 167 CB THR A 30 0.689 9.464 -6.944 1.00 40.06 C ATOM 168 OG1 THR A 30 0.744 8.505 -8.012 1.00 44.60 O ATOM 169 CG2 THR A 30 2.057 9.544 -6.239 1.00 42.18 C ATOM 170 N ASP A 31 -0.878 11.284 -5.060 1.00 41.19 N ATOM 171 CA ASP A 31 -0.932 12.336 -4.046 1.00 39.50 C ATOM 172 C ASP A 31 -1.741 11.907 -2.824 1.00 39.91 C ATOM 173 O ASP A 31 -1.355 12.185 -1.686 1.00 40.35 O ATOM 174 CB ASP A 31 -1.519 13.619 -4.651 1.00 38.43 C ATOM 175 CG ASP A 31 -2.917 13.413 -5.213 1.00 47.11 C ATOM 176 OD1 ASP A 31 -3.207 12.308 -5.722 1.00 54.64 O ATOM 177 OD2 ASP A 31 -3.723 14.362 -5.162 1.00 54.19 O ATOM 178 N LEU A 32 -2.859 11.227 -3.061 1.00 39.27 N ATOM 179 CA LEU A 32 -3.704 10.756 -1.971 1.00 38.39 C ATOM 180 C LEU A 32 -2.982 9.674 -1.168 1.00 36.37 C ATOM 181 O LEU A 32 -3.065 9.634 0.059 1.00 38.34 O ATOM 182 CB LEU A 32 -5.013 10.186 -2.518 1.00 37.25 C ATOM 183 CG LEU A 32 -5.876 9.488 -1.458 1.00 42.92 C ATOM 184 CD1 LEU A 32 -6.390 10.507 -0.453 1.00 38.64 C ATOM 185 CD2 LEU A 32 -7.032 8.774 -2.125 1.00 38.43 C ATOM 186 N SER A 33 -2.280 8.796 -1.874 1.00 34.02 N ATOM 187 CA SER A 33 -1.545 7.715 -1.232 1.00 32.16 C ATOM 188 C SER A 33 -0.475 8.284 -0.317 1.00 29.06 C ATOM 189 O SER A 33 -0.336 7.860 0.827 1.00 34.26 O ATOM 190 CB SER A 33 -0.886 6.822 -2.284 1.00 29.79 C ATOM 191 OG SER A 33 -1.863 6.280 -3.144 1.00 37.68 O ATOM 192 N LEU A 34 0.286 9.241 -0.838 1.00 32.20 N ATOM 193 CA LEU A 34 1.352 9.881 -0.071 1.00 33.43 C ATOM 194 C LEU A 34 0.803 10.569 1.169 1.00 34.76 C ATOM 195 O LEU A 34 1.359 10.457 2.255 1.00 37.62 O ATOM 196 CB LEU A 34 2.075 10.910 -0.940 1.00 34.55 C ATOM 197 CG LEU A 34 2.830 10.299 -2.120 1.00 37.64 C ATOM 198 CD1 LEU A 34 3.534 11.395 -2.895 1.00 38.24 C ATOM 199 CD2 LEU A 34 3.829 9.263 -1.600 1.00 31.60 C HETATM 200 N MSE A 35 -0.298 11.280 0.993 1.00 38.86 N HETATM 201 CA MSE A 35 -0.930 11.997 2.086 1.00 42.98 C HETATM 202 C MSE A 35 -1.359 11.023 3.187 1.00 36.58 C HETATM 203 O MSE A 35 -1.175 11.288 4.373 1.00 36.99 O HETATM 204 CB MSE A 35 -2.134 12.748 1.537 1.00 40.46 C HETATM 205 CG MSE A 35 -2.782 13.724 2.485 1.00 56.00 C HETATM 206 SE MSE A 35 -4.345 14.461 1.614 1.00 74.87 HETATM 207 CE MSE A 35 -3.535 14.979 -0.082 1.00 52.97 C ATOM 208 N ALA A 36 -1.934 9.893 2.790 1.00 32.07 N ATOM 209 CA ALA A 36 -2.370 8.900 3.753 1.00 26.27 C ATOM 210 C ALA A 36 -1.152 8.291 4.446 1.00 26.93 C ATOM 211 O ALA A 36 -1.120 8.158 5.679 1.00 30.22 O ATOM 212 CB ALA A 36 -3.167 7.810 3.048 1.00 26.54 C ATOM 213 N LEU A 37 -0.151 7.920 3.649 1.00 27.69 N ATOM 214 CA LEU A 37 1.065 7.318 4.185 1.00 27.00 C ATOM 215 C LEU A 37 1.774 8.280 5.129 1.00 23.64 C ATOM 216 O LEU A 37 2.266 7.881 6.177 1.00 28.08 O ATOM 217 CB LEU A 37 1.993 6.895 3.043 1.00 25.56 C ATOM 218 CG LEU A 37 1.483 5.710 2.205 1.00 28.81 C ATOM 219 CD1 LEU A 37 2.353 5.543 0.949 1.00 26.04 C ATOM 220 CD2 LEU A 37 1.500 4.433 3.046 1.00 20.72 C ATOM 221 N GLY A 38 1.813 9.553 4.762 1.00 27.77 N ATOM 222 CA GLY A 38 2.453 10.537 5.612 1.00 26.64 C ATOM 223 C GLY A 38 1.713 10.659 6.929 1.00 28.37 C ATOM 224 O GLY A 38 2.329 10.727 7.999 1.00 32.91 O ATOM 225 N ASN A 39 0.388 10.686 6.858 1.00 27.58 N ATOM 226 CA ASN A 39 -0.414 10.789 8.070 1.00 26.16 C ATOM 227 C ASN A 39 -0.211 9.572 8.949 1.00 26.18 C ATOM 228 O ASN A 39 -0.254 9.678 10.168 1.00 28.34 O ATOM 229 CB ASN A 39 -1.893 10.946 7.732 1.00 28.31 C ATOM 230 CG ASN A 39 -2.271 12.376 7.472 1.00 31.76 C ATOM 231 OD1 ASN A 39 -2.303 13.189 8.391 1.00 45.95 O ATOM 232 ND2 ASN A 39 -2.553 12.702 6.215 1.00 39.90 N ATOM 233 N CYS A 40 0.011 8.411 8.343 1.00 29.21 N ATOM 234 CA CYS A 40 0.238 7.219 9.149 1.00 28.41 C ATOM 235 C CYS A 40 1.547 7.369 9.934 1.00 28.86 C ATOM 236 O CYS A 40 1.608 7.021 11.105 1.00 33.35 O ATOM 237 CB CYS A 40 0.269 5.964 8.269 1.00 29.46 C ATOM 238 SG CYS A 40 -1.362 5.498 7.645 1.00 30.07 S ATOM 239 N VAL A 41 2.587 7.896 9.294 1.00 30.65 N ATOM 240 CA VAL A 41 3.867 8.103 9.975 1.00 29.07 C ATOM 241 C VAL A 41 3.651 9.120 11.102 1.00 28.62 C ATOM 242 O VAL A 41 4.075 8.912 12.236 1.00 31.62 O ATOM 243 CB VAL A 41 4.961 8.661 9.003 1.00 25.60 C ATOM 244 CG1 VAL A 41 6.296 8.803 9.732 1.00 19.43 C ATOM 245 CG2 VAL A 41 5.116 7.744 7.812 1.00 24.50 C ATOM 246 N THR A 42 2.986 10.223 10.779 1.00 30.71 N ATOM 247 CA THR A 42 2.716 11.253 11.771 1.00 33.90 C ATOM 248 C THR A 42 1.974 10.652 12.967 1.00 37.29 C ATOM 249 O THR A 42 2.342 10.894 14.119 1.00 40.82 O ATOM 250 CB THR A 42 1.879 12.403 11.163 1.00 31.24 C ATOM 251 OG1 THR A 42 2.677 13.128 10.219 1.00 32.47 O ATOM 252 CG2 THR A 42 1.433 13.358 12.238 1.00 39.90 C ATOM 253 N HIS A 43 0.944 9.856 12.680 1.00 40.70 N ATOM 254 CA HIS A 43 0.137 9.208 13.714 1.00 39.42 C ATOM 255 C HIS A 43 1.044 8.388 14.631 1.00 39.18 C ATOM 256 O HIS A 43 1.032 8.569 15.846 1.00 39.41 O ATOM 257 CB HIS A 43 -0.895 8.288 13.061 1.00 40.88 C ATOM 258 CG HIS A 43 -1.805 7.602 14.032 1.00 48.85 C ATOM 259 ND1 HIS A 43 -2.973 8.174 14.492 1.00 56.41 N ATOM 260 CD2 HIS A 43 -1.730 6.381 14.613 1.00 51.01 C ATOM 261 CE1 HIS A 43 -3.578 7.334 15.310 1.00 57.92 C ATOM 262 NE2 HIS A 43 -2.847 6.236 15.403 1.00 50.08 N ATOM 263 N LEU A 44 1.827 7.491 14.038 1.00 38.79 N ATOM 264 CA LEU A 44 2.751 6.648 14.790 1.00 40.36 C ATOM 265 C LEU A 44 3.704 7.443 15.669 1.00 40.75 C ATOM 266 O LEU A 44 3.857 7.143 16.849 1.00 41.38 O ATOM 267 CB LEU A 44 3.593 5.799 13.845 1.00 41.41 C ATOM 268 CG LEU A 44 2.896 4.698 13.059 1.00 42.81 C ATOM 269 CD1 LEU A 44 3.925 4.013 12.163 1.00 49.50 C ATOM 270 CD2 LEU A 44 2.268 3.697 14.013 1.00 49.58 C ATOM 271 N LEU A 45 4.360 8.443 15.089 1.00 40.36 N ATOM 272 CA LEU A 45 5.306 9.255 15.845 1.00 40.44 C ATOM 273 C LEU A 45 4.651 9.911 17.044 1.00 41.80 C ATOM 274 O LEU A 45 5.216 9.934 18.131 1.00 45.60 O ATOM 275 CB LEU A 45 5.933 10.333 14.951 1.00 36.65 C ATOM 276 CG LEU A 45 6.888 9.811 13.876 1.00 38.40 C ATOM 277 CD1 LEU A 45 7.634 10.975 13.231 1.00 31.68 C ATOM 278 CD2 LEU A 45 7.877 8.840 14.510 1.00 31.55 C ATOM 279 N GLU A 46 3.454 10.442 16.839 1.00 44.96 N ATOM 280 CA GLU A 46 2.724 11.107 17.907 1.00 47.13 C ATOM 281 C GLU A 46 2.297 10.113 18.975 1.00 47.79 C ATOM 282 O GLU A 46 2.336 10.418 20.167 1.00 49.97 O ATOM 283 CB GLU A 46 1.487 11.807 17.340 1.00 48.07 C ATOM 284 CG GLU A 46 1.788 12.808 16.234 1.00 52.95 C ATOM 285 CD GLU A 46 0.555 13.169 15.423 1.00 68.02 C ATOM 286 OE1 GLU A 46 -0.149 12.244 14.961 1.00 77.72 O ATOM 287 OE2 GLU A 46 0.291 14.374 15.236 1.00 70.85 O ATOM 288 N ARG A 47 1.917 8.914 18.550 1.00 51.61 N ATOM 289 CA ARG A 47 1.445 7.904 19.486 1.00 53.80 C ATOM 290 C ARG A 47 2.494 6.964 20.084 1.00 51.90 C ATOM 291 O ARG A 47 2.243 6.345 21.119 1.00 55.16 O ATOM 292 CB ARG A 47 0.323 7.078 18.836 1.00 54.90 C ATOM 293 CG ARG A 47 -0.325 6.070 19.780 1.00 68.96 C ATOM 294 CD ARG A 47 -1.552 5.383 19.185 1.00 85.62 C ATOM 295 NE ARG A 47 -2.728 6.251 19.145 1.00 99.27 N ATOM 296 CZ ARG A 47 -3.971 5.833 19.382 1.00100.00 C ATOM 297 NH1 ARG A 47 -4.197 4.558 19.678 1.00100.00 N ATOM 298 NH2 ARG A 47 -4.990 6.683 19.323 1.00 98.84 N ATOM 299 N LYS A 48 3.668 6.853 19.473 1.00 49.36 N ATOM 300 CA LYS A 48 4.660 5.944 20.023 1.00 47.45 C ATOM 301 C LYS A 48 6.072 6.487 20.196 1.00 46.43 C ATOM 302 O LYS A 48 6.965 5.770 20.640 1.00 44.00 O ATOM 303 CB LYS A 48 4.688 4.655 19.198 1.00 52.07 C ATOM 304 CG LYS A 48 3.405 3.841 19.320 1.00 53.54 C ATOM 305 CD LYS A 48 3.506 2.508 18.594 1.00 64.71 C ATOM 306 CE LYS A 48 2.250 1.669 18.802 1.00 70.49 C ATOM 307 NZ LYS A 48 2.015 1.348 20.243 1.00 72.30 N ATOM 308 N VAL A 49 6.278 7.751 19.856 1.00 44.87 N ATOM 309 CA VAL A 49 7.593 8.354 20.005 1.00 42.45 C ATOM 310 C VAL A 49 7.517 9.575 20.916 1.00 47.13 C ATOM 311 O VAL A 49 6.713 10.482 20.697 1.00 47.40 O ATOM 312 CB VAL A 49 8.181 8.789 18.640 1.00 39.24 C ATOM 313 CG1 VAL A 49 9.485 9.540 18.848 1.00 32.19 C ATOM 314 CG2 VAL A 49 8.414 7.570 17.763 1.00 36.04 C ATOM 315 N PRO A 50 8.352 9.604 21.964 1.00 50.29 N ATOM 316 CA PRO A 50 8.378 10.723 22.906 1.00 48.83 C ATOM 317 C PRO A 50 8.475 12.058 22.179 1.00 45.35 C ATOM 318 O PRO A 50 9.280 12.229 21.262 1.00 45.33 O ATOM 319 CB PRO A 50 9.614 10.429 23.744 1.00 51.13 C ATOM 320 CG PRO A 50 9.585 8.934 23.823 1.00 56.44 C ATOM 321 CD PRO A 50 9.279 8.540 22.391 1.00 50.95 C ATOM 322 N SER A 51 7.636 12.993 22.597 1.00 44.64 N ATOM 323 CA SER A 51 7.589 14.327 22.020 1.00 44.03 C ATOM 324 C SER A 51 8.963 14.917 21.691 1.00 42.49 C ATOM 325 O SER A 51 9.135 15.576 20.671 1.00 42.56 O ATOM 326 CB SER A 51 6.851 15.259 22.981 1.00 46.94 C ATOM 327 OG SER A 51 7.036 16.611 22.610 1.00 55.97 O ATOM 328 N GLU A 52 9.932 14.676 22.564 1.00 43.01 N ATOM 329 CA GLU A 52 11.289 15.195 22.404 1.00 42.80 C ATOM 330 C GLU A 52 12.112 14.582 21.271 1.00 43.36 C ATOM 331 O GLU A 52 13.089 15.180 20.820 1.00 44.35 O ATOM 332 CB GLU A 52 12.048 15.020 23.724 1.00 44.05 C ATOM 333 CG GLU A 52 11.760 13.686 24.399 1.00 49.31 C ATOM 334 CD GLU A 52 12.662 13.406 25.581 1.00 65.12 C ATOM 335 OE1 GLU A 52 12.522 12.317 26.182 1.00 70.23 O ATOM 336 OE2 GLU A 52 13.510 14.266 25.910 1.00 68.95 O ATOM 337 N SER A 53 11.724 13.398 20.804 1.00 42.28 N ATOM 338 CA SER A 53 12.473 12.730 19.737 1.00 41.19 C ATOM 339 C SER A 53 11.700 12.697 18.419 1.00 40.35 C ATOM 340 O SER A 53 12.261 12.428 17.351 1.00 42.18 O ATOM 341 CB SER A 53 12.795 11.297 20.168 1.00 39.38 C ATOM 342 OG SER A 53 13.286 11.267 21.495 1.00 40.59 O ATOM 343 N ARG A 54 10.408 12.986 18.510 1.00 40.09 N ATOM 344 CA ARG A 54 9.517 12.960 17.357 1.00 39.16 C ATOM 345 C ARG A 54 10.072 13.618 16.098 1.00 36.79 C ATOM 346 O ARG A 54 10.125 13.002 15.033 1.00 39.74 O ATOM 347 CB ARG A 54 8.190 13.595 17.746 1.00 36.08 C ATOM 348 CG ARG A 54 7.004 12.961 17.072 1.00 42.93 C ATOM 349 CD ARG A 54 5.743 13.293 17.833 1.00 47.51 C ATOM 350 NE ARG A 54 5.676 12.587 19.109 1.00 47.93 N ATOM 351 CZ ARG A 54 4.996 13.030 20.161 1.00 50.57 C ATOM 352 NH1 ARG A 54 4.338 14.177 20.083 1.00 45.11 N ATOM 353 NH2 ARG A 54 4.970 12.331 21.286 1.00 51.33 N ATOM 354 N GLN A 55 10.490 14.868 16.212 1.00 35.46 N ATOM 355 CA GLN A 55 11.036 15.572 15.064 1.00 34.45 C ATOM 356 C GLN A 55 12.268 14.833 14.540 1.00 34.73 C ATOM 357 O GLN A 55 12.434 14.656 13.330 1.00 35.43 O ATOM 358 CB GLN A 55 11.429 16.993 15.460 1.00 35.01 C ATOM 359 CG GLN A 55 11.506 17.956 14.300 1.00 40.35 C ATOM 360 CD GLN A 55 10.128 18.358 13.824 1.00 45.92 C ATOM 361 OE1 GLN A 55 9.276 18.738 14.629 1.00 47.70 O ATOM 362 NE2 GLN A 55 9.899 18.280 12.517 1.00 39.91 N ATOM 363 N ALA A 56 13.131 14.408 15.460 1.00 35.25 N ATOM 364 CA ALA A 56 14.352 13.697 15.089 1.00 31.81 C ATOM 365 C ALA A 56 14.020 12.387 14.359 1.00 28.23 C ATOM 366 O ALA A 56 14.594 12.098 13.312 1.00 26.90 O ATOM 367 CB ALA A 56 15.202 13.421 16.335 1.00 30.98 C ATOM 368 N VAL A 57 13.099 11.594 14.902 1.00 27.94 N ATOM 369 CA VAL A 57 12.733 10.350 14.224 1.00 27.16 C ATOM 370 C VAL A 57 12.121 10.691 12.856 1.00 28.41 C ATOM 371 O VAL A 57 12.384 10.022 11.867 1.00 36.40 O ATOM 372 CB VAL A 57 11.715 9.529 15.038 1.00 28.27 C ATOM 373 CG1 VAL A 57 11.316 8.273 14.262 1.00 30.56 C ATOM 374 CG2 VAL A 57 12.318 9.146 16.390 1.00 26.90 C ATOM 375 N ALA A 58 11.316 11.747 12.804 1.00 30.60 N ATOM 376 CA ALA A 58 10.703 12.165 11.548 1.00 30.01 C ATOM 377 C ALA A 58 11.794 12.491 10.524 1.00 31.26 C ATOM 378 O ALA A 58 11.705 12.091 9.358 1.00 32.18 O ATOM 379 CB ALA A 58 9.814 13.392 11.773 1.00 29.43 C ATOM 380 N GLU A 59 12.825 13.209 10.962 1.00 33.23 N ATOM 381 CA GLU A 59 13.915 13.571 10.059 1.00 33.31 C ATOM 382 C GLU A 59 14.714 12.363 9.575 1.00 30.26 C ATOM 383 O GLU A 59 15.125 12.311 8.415 1.00 33.39 O ATOM 384 CB GLU A 59 14.870 14.574 10.714 1.00 35.63 C ATOM 385 CG GLU A 59 16.225 14.626 10.012 1.00 43.92 C ATOM 386 CD GLU A 59 16.871 15.991 10.049 1.00 61.52 C ATOM 387 OE1 GLU A 59 16.976 16.577 11.149 1.00 70.80 O ATOM 388 OE2 GLU A 59 17.281 16.475 8.971 1.00 69.34 O ATOM 389 N GLN A 60 14.940 11.397 10.456 1.00 32.17 N ATOM 390 CA GLN A 60 15.682 10.204 10.061 1.00 32.04 C ATOM 391 C GLN A 60 14.839 9.394 9.083 1.00 30.94 C ATOM 392 O GLN A 60 15.361 8.768 8.160 1.00 34.17 O ATOM 393 CB GLN A 60 16.034 9.361 11.290 1.00 37.07 C ATOM 394 CG GLN A 60 17.066 10.017 12.212 1.00 37.04 C ATOM 395 CD GLN A 60 18.321 10.439 11.466 1.00 43.81 C ATOM 396 OE1 GLN A 60 18.402 11.548 10.934 1.00 46.41 O ATOM 397 NE2 GLN A 60 19.302 9.546 11.409 1.00 49.90 N ATOM 398 N PHE A 61 13.525 9.415 9.282 1.00 32.10 N ATOM 399 CA PHE A 61 12.630 8.697 8.379 1.00 30.54 C ATOM 400 C PHE A 61 12.795 9.357 7.010 1.00 29.02 C ATOM 401 O PHE A 61 12.926 8.685 5.989 1.00 31.10 O ATOM 402 CB PHE A 61 11.175 8.832 8.841 1.00 31.25 C ATOM 403 CG PHE A 61 10.177 8.222 7.891 1.00 24.95 C ATOM 404 CD1 PHE A 61 9.820 6.879 8.000 1.00 29.01 C ATOM 405 CD2 PHE A 61 9.607 8.982 6.880 1.00 28.59 C ATOM 406 CE1 PHE A 61 8.909 6.308 7.119 1.00 28.10 C ATOM 407 CE2 PHE A 61 8.690 8.420 5.986 1.00 25.50 C ATOM 408 CZ PHE A 61 8.339 7.079 6.107 1.00 28.19 C ATOM 409 N ALA A 62 12.812 10.684 7.012 1.00 29.85 N ATOM 410 CA ALA A 62 12.940 11.456 5.779 1.00 31.88 C ATOM 411 C ALA A 62 14.262 11.209 5.063 1.00 30.76 C ATOM 412 O ALA A 62 14.289 11.046 3.841 1.00 34.20 O ATOM 413 CB ALA A 62 12.781 12.939 6.079 1.00 33.47 C ATOM 414 N LYS A 63 15.354 11.187 5.822 1.00 32.08 N ATOM 415 CA LYS A 63 16.672 10.953 5.242 1.00 31.71 C ATOM 416 C LYS A 63 16.691 9.581 4.587 1.00 31.88 C ATOM 417 O LYS A 63 17.150 9.425 3.454 1.00 36.65 O ATOM 418 CB LYS A 63 17.748 11.012 6.326 1.00 34.37 C ATOM 419 CG LYS A 63 18.123 12.408 6.787 1.00 36.54 C ATOM 420 CD LYS A 63 19.062 13.073 5.804 1.00 60.37 C ATOM 421 CE LYS A 63 19.751 14.277 6.433 1.00 67.06 C ATOM 422 NZ LYS A 63 18.776 15.280 6.947 1.00 75.51 N ATOM 423 N ALA A 64 16.183 8.591 5.313 1.00 32.83 N ATOM 424 CA ALA A 64 16.123 7.220 4.818 1.00 33.36 C ATOM 425 C ALA A 64 15.313 7.194 3.540 1.00 31.60 C ATOM 426 O ALA A 64 15.700 6.574 2.554 1.00 34.69 O ATOM 427 CB ALA A 64 15.485 6.308 5.863 1.00 32.40 C ATOM 428 N LEU A 65 14.181 7.880 3.549 1.00 35.24 N ATOM 429 CA LEU A 65 13.353 7.913 2.355 1.00 34.85 C ATOM 430 C LEU A 65 14.140 8.519 1.195 1.00 34.94 C ATOM 431 O LEU A 65 14.191 7.941 0.109 1.00 36.71 O ATOM 432 CB LEU A 65 12.090 8.734 2.597 1.00 36.14 C ATOM 433 CG LEU A 65 11.217 8.889 1.348 1.00 36.00 C ATOM 434 CD1 LEU A 65 10.807 7.498 0.830 1.00 30.47 C ATOM 435 CD2 LEU A 65 9.985 9.735 1.693 1.00 39.39 C ATOM 436 N ALA A 66 14.745 9.682 1.434 1.00 36.72 N ATOM 437 CA ALA A 66 15.524 10.373 0.406 1.00 37.07 C ATOM 438 C ALA A 66 16.643 9.481 -0.127 1.00 37.98 C ATOM 439 O ALA A 66 16.819 9.349 -1.341 1.00 37.71 O ATOM 440 CB ALA A 66 16.111 11.655 0.972 1.00 33.19 C ATOM 441 N GLN A 67 17.397 8.869 0.783 1.00 40.04 N ATOM 442 CA GLN A 67 18.490 7.992 0.375 1.00 42.37 C ATOM 443 C GLN A 67 17.931 6.826 -0.419 1.00 41.08 C ATOM 444 O GLN A 67 18.475 6.443 -1.452 1.00 43.68 O ATOM 445 CB GLN A 67 19.252 7.457 1.591 1.00 43.79 C ATOM 446 CG GLN A 67 20.705 7.914 1.663 1.00 57.26 C ATOM 447 CD GLN A 67 21.435 7.809 0.327 1.00 64.64 C ATOM 448 OE1 GLN A 67 21.481 6.744 -0.296 1.00 65.20 O ATOM 449 NE2 GLN A 67 22.011 8.921 -0.115 1.00 64.30 N ATOM 450 N SER A 68 16.836 6.262 0.069 1.00 40.08 N ATOM 451 CA SER A 68 16.223 5.144 -0.616 1.00 43.88 C ATOM 452 C SER A 68 15.947 5.532 -2.061 1.00 44.81 C ATOM 453 O SER A 68 16.435 4.885 -2.989 1.00 45.03 O ATOM 454 CB SER A 68 14.922 4.746 0.074 1.00 44.69 C ATOM 455 OG SER A 68 14.382 3.582 -0.520 1.00 51.24 O ATOM 456 N VAL A 69 15.174 6.600 -2.247 1.00 44.63 N ATOM 457 CA VAL A 69 14.829 7.075 -3.585 1.00 41.46 C ATOM 458 C VAL A 69 16.067 7.303 -4.447 1.00 45.88 C ATOM 459 O VAL A 69 16.127 6.859 -5.593 1.00 48.81 O ATOM 460 CB VAL A 69 14.033 8.403 -3.527 1.00 40.91 C ATOM 461 CG1 VAL A 69 13.842 8.960 -4.936 1.00 38.31 C ATOM 462 CG2 VAL A 69 12.682 8.176 -2.854 1.00 36.53 C ATOM 463 N LYS A 70 17.049 8.002 -3.891 1.00 46.00 N ATOM 464 CA LYS A 70 18.271 8.302 -4.614 1.00 50.70 C ATOM 465 C LYS A 70 18.911 7.020 -5.134 1.00 55.03 C ATOM 466 O LYS A 70 19.083 6.841 -6.343 1.00 55.29 O ATOM 467 CB LYS A 70 19.239 9.049 -3.699 1.00 49.88 C ATOM 468 CG LYS A 70 20.529 9.479 -4.370 1.00 54.99 C ATOM 469 CD LYS A 70 21.360 10.335 -3.433 1.00 63.85 C ATOM 470 CE LYS A 70 22.668 10.758 -4.076 1.00 71.13 C ATOM 471 NZ LYS A 70 23.447 11.657 -3.179 1.00 75.48 N ATOM 472 N SER A 71 19.250 6.122 -4.217 1.00 58.80 N ATOM 473 CA SER A 71 19.868 4.862 -4.593 1.00 62.96 C ATOM 474 C SER A 71 19.030 4.127 -5.625 1.00 64.85 C ATOM 475 O SER A 71 19.575 3.547 -6.560 1.00 69.08 O ATOM 476 CB SER A 71 20.074 3.982 -3.359 1.00 64.37 C ATOM 477 OG SER A 71 20.960 4.610 -2.444 1.00 66.09 O ATOM 478 N ASN A 72 17.710 4.154 -5.466 1.00 66.85 N ATOM 479 CA ASN A 72 16.830 3.478 -6.412 1.00 70.73 C ATOM 480 C ASN A 72 17.042 4.053 -7.804 1.00 72.49 C ATOM 481 O ASN A 72 16.675 3.439 -8.805 1.00 73.64 O ATOM 482 CB ASN A 72 15.366 3.633 -6.002 1.00 72.80 C ATOM 483 CG ASN A 72 15.059 2.964 -4.675 1.00 81.83 C ATOM 484 OD1 ASN A 72 15.461 1.824 -4.433 1.00 92.21 O ATOM 485 ND2 ASN A 72 14.332 3.665 -3.812 1.00 85.50 N ATOM 486 N LEU A 73 17.631 5.244 -7.854 1.00 74.84 N ATOM 487 CA LEU A 73 17.930 5.901 -9.119 1.00 76.09 C ATOM 488 C LEU A 73 19.298 5.409 -9.578 1.00 77.82 C ATOM 489 O LEU A 73 20.176 6.205 -9.916 1.00 77.19 O ATOM 490 CB LEU A 73 17.957 7.424 -8.945 1.00 75.45 C ATOM 491 CG LEU A 73 16.678 8.219 -9.221 1.00 72.49 C ATOM 492 CD1 LEU A 73 15.521 7.690 -8.397 1.00 71.70 C ATOM 493 CD2 LEU A 73 16.934 9.678 -8.903 1.00 75.03 C ATOM 494 N GLU A 74 19.472 4.090 -9.570 1.00 79.25 N ATOM 495 CA GLU A 74 20.727 3.473 -9.984 1.00 80.43 C ATOM 496 C GLU A 74 20.507 2.487 -11.128 1.00 80.95 C ATOM 497 O GLU A 74 19.333 2.200 -11.457 1.00 44.58 O ATOM 498 CB GLU A 74 21.374 2.763 -8.798 1.00 79.17 C HETATM 499 O HOH A 101 13.523 15.617 17.843 1.00 46.23 O HETATM 500 O HOH A 102 2.757 14.546 0.466 1.00 48.17 O HETATM 501 O HOH A 103 5.176 -6.177 -1.796 1.00 51.91 O HETATM 502 O HOH A 104 13.576 -12.975 3.587 1.00 63.11 O HETATM 503 O HOH A 105 11.682 16.260 11.068 1.00 43.25 O HETATM 504 O HOH A 106 12.600 16.997 27.684 1.00 56.06 O HETATM 505 O HOH A 107 11.757 -16.756 4.190 1.00 51.95 O HETATM 506 O HOH A 108 0.406 14.254 -1.171 1.00 47.87 O HETATM 507 O HOH A 110 21.540 4.996 -12.565 1.00 60.33 O HETATM 508 O HOH A 112 -7.367 12.696 -3.721 1.00 70.79 O HETATM 509 O HOH A 113 -6.208 14.023 7.590 1.00 46.93 O HETATM 510 O HOH A 114 -3.317 16.024 5.737 1.00 58.61 O HETATM 511 O HOH A 115 9.052 -4.398 -4.988 1.00 47.23 O HETATM 512 O HOH A 117 5.340 7.795 23.551 1.00 53.42 O HETATM 513 O HOH A 118 15.653 -11.900 9.424 1.00 54.94 O HETATM 514 O HOH A 119 -9.142 -7.167 -5.328 1.00 52.41 O HETATM 515 O HOH A 120 1.435 4.861 23.041 1.00 51.75 O HETATM 516 O HOH A 121 2.565 -2.406 -7.329 1.00 53.21 O HETATM 517 O HOH A 122 -5.746 8.553 21.178 1.00 50.92 O TER 518 HOH A 122 ENDMDL MASTER END