HEADER TRANSFERASE 12-SEP-01 1JYK TITLE CATALYTIC MECHANISM OF CTP:PHOSPHOCHOLINE TITLE 2 CYTIDYLYTRANSFERASE FROM STREPTOCOCCUS PNEUMONIAE (LICC) COMPND MOL_ID: 1; COMPND 2 MOLECULE: CTP:PHOSPHOCHOLINE CYTIDYLYTRANSFERASE; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: LICC PROTEIN; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS PNEUMONIAE; SOURCE 3 ORGANISM_TAXID: 1313; SOURCE 4 GENE: LICC; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS LICC, 3D STRUCTURE, CTP:PHOSPHOCHOLINE CYTIDYLYLTRANSFERASE EXPDTA X-RAY DIFFRACTION AUTHOR B.-Y.KWAK,M.YUN,H.-W.PARK REVDAT 3 24-FEB-09 1JYK 1 VERSN REVDAT 2 01-APR-03 1JYK 1 JRNL REVDAT 1 22-FEB-02 1JYK 0 JRNL AUTH B.Y.KWAK,Y.M.ZHANG,M.YUN,R.J.HEATH,C.O.ROCK, JRNL AUTH 2 S.JACKOWSKI,H.W.PARK JRNL TITL STRUCTURE AND MECHANISM OF CTP:PHOSPHOCHOLINE JRNL TITL 2 CYTIDYLYLTRANSFERASE (LICC) FROM STREPTOCOCCUS JRNL TITL 3 PNEUMONIAE. JRNL REF J.BIOL.CHEM. V. 277 4343 2002 JRNL REFN ISSN 0021-9258 JRNL PMID 11706035 JRNL DOI 10.1074/JBC.M109163200 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 1.50 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XTALVIEW REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 NUMBER OF REFLECTIONS : 49170 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) : 0.218 REMARK 3 FREE R VALUE : 0.241 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : NULL REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : NULL REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL REMARK 3 BIN R VALUE (WORKING SET) : NULL REMARK 3 BIN FREE R VALUE : NULL REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 1903 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 237 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 20.60 REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL REMARK 3 ESD FROM SIGMAA (A) : NULL REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL REMARK 3 REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL REMARK 3 ESD FROM C-V SIGMAA (A) : NULL REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.007 REMARK 3 BOND ANGLES (DEGREES) : 1.37 REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL REMARK 3 IMPROPER ANGLES (DEGREES) : NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 REMARK 3 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: NULL REMARK 4 REMARK 4 1JYK COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-SEP-01. REMARK 100 THE RCSB ID CODE IS RCSB014336. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 20-APR-01 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : NSLS REMARK 200 BEAMLINE : X8C REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795, 0.9794 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 54137 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.04800 REMARK 200 FOR THE DATA SET : 36.8000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.55 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6 REMARK 200 DATA REDUNDANCY IN SHELL : 2.79 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: MAD REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD REMARK 200 SOFTWARE USED: SOLVE REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 55.78 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.78 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM CITRATE, AMMONIUM SULFATE, REMARK 280 TARTRATE, PH 7.5, VAPOR DIFFUSION, HANGING DROP AT 291K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 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 21.31000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 61.19000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 31.79500 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 61.19000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 21.31000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 31.79500 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 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 MET A -19 REMARK 465 GLY A -18 REMARK 465 SER A -17 REMARK 465 SER A -16 REMARK 465 HIS A -15 REMARK 465 HIS A -14 REMARK 465 HIS A -13 REMARK 465 HIS A -12 REMARK 465 HIS A -11 REMARK 465 HIS A -10 REMARK 465 SER A -9 REMARK 465 SER A -8 REMARK 465 GLY A -7 REMARK 465 LEU A -6 REMARK 465 VAL A -5 REMARK 465 PRO A -4 REMARK 465 ARG A -3 REMARK 465 GLY A -2 REMARK 465 SER A -1 REMARK 465 HIS A 0 REMARK 465 MET A 1 REMARK 465 LYS A 2 REMARK 465 ASN A 232 REMARK 465 GLU A 233 REMARK 465 ASN A 234 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 ASN A 87 3.99 -66.97 REMARK 500 ASP A 107 32.47 -99.95 REMARK 500 PHE A 186 -28.82 -145.51 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 A1120 DISTANCE = 7.15 ANGSTROMS REMARK 525 HOH A1128 DISTANCE = 5.86 ANGSTROMS REMARK 525 HOH A1141 DISTANCE = 6.95 ANGSTROMS REMARK 525 HOH A1145 DISTANCE = 8.67 ANGSTROMS REMARK 525 HOH A1146 DISTANCE = 8.49 ANGSTROMS REMARK 525 HOH A1148 DISTANCE = 7.68 ANGSTROMS REMARK 525 HOH A1153 DISTANCE = 7.84 ANGSTROMS REMARK 525 HOH A1156 DISTANCE = 5.89 ANGSTROMS REMARK 525 HOH A1160 DISTANCE = 14.84 ANGSTROMS REMARK 525 HOH A1162 DISTANCE = 6.21 ANGSTROMS REMARK 525 HOH A1164 DISTANCE = 7.17 ANGSTROMS REMARK 525 HOH A1165 DISTANCE = 7.75 ANGSTROMS REMARK 525 HOH A1166 DISTANCE = 8.35 ANGSTROMS REMARK 525 HOH A1169 DISTANCE = 8.30 ANGSTROMS REMARK 525 HOH A1170 DISTANCE = 7.04 ANGSTROMS REMARK 525 HOH A1171 DISTANCE = 6.55 ANGSTROMS REMARK 525 HOH A1173 DISTANCE = 11.66 ANGSTROMS REMARK 525 HOH A1231 DISTANCE = 9.11 ANGSTROMS REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1JYL RELATED DB: PDB DBREF 1JYK A 7 234 UNP Q97QE9 Q97QE9_STRPN 2 229 SEQADV 1JYK MET A -19 UNP Q97QE9 EXPRESSION TAG SEQADV 1JYK GLY A -18 UNP Q97QE9 EXPRESSION TAG SEQADV 1JYK SER A -17 UNP Q97QE9 EXPRESSION TAG SEQADV 1JYK SER A -16 UNP Q97QE9 EXPRESSION TAG SEQADV 1JYK HIS A -15 UNP Q97QE9 EXPRESSION TAG SEQADV 1JYK HIS A -14 UNP Q97QE9 EXPRESSION TAG SEQADV 1JYK HIS A -13 UNP Q97QE9 EXPRESSION TAG SEQADV 1JYK HIS A -12 UNP Q97QE9 EXPRESSION TAG SEQADV 1JYK HIS A -11 UNP Q97QE9 EXPRESSION TAG SEQADV 1JYK HIS A -10 UNP Q97QE9 EXPRESSION TAG SEQADV 1JYK SER A -9 UNP Q97QE9 EXPRESSION TAG SEQADV 1JYK SER A -8 UNP Q97QE9 EXPRESSION TAG SEQADV 1JYK GLY A -7 UNP Q97QE9 EXPRESSION TAG SEQADV 1JYK LEU A -6 UNP Q97QE9 EXPRESSION TAG SEQADV 1JYK VAL A -5 UNP Q97QE9 EXPRESSION TAG SEQADV 1JYK PRO A -4 UNP Q97QE9 EXPRESSION TAG SEQADV 1JYK ARG A -3 UNP Q97QE9 EXPRESSION TAG SEQADV 1JYK GLY A -2 UNP Q97QE9 EXPRESSION TAG SEQADV 1JYK SER A -1 UNP Q97QE9 EXPRESSION TAG SEQADV 1JYK HIS A 0 UNP Q97QE9 EXPRESSION TAG SEQADV 1JYK MET A 1 UNP Q97QE9 EXPRESSION TAG SEQADV 1JYK LYS A 2 UNP Q97QE9 EXPRESSION TAG SEQADV 1JYK GLU A 3 UNP Q97QE9 EXPRESSION TAG SEQADV 1JYK ILE A 4 UNP Q97QE9 EXPRESSION TAG SEQADV 1JYK ARG A 5 UNP Q97QE9 EXPRESSION TAG SEQADV 1JYK VAL A 6 UNP Q97QE9 EXPRESSION TAG SEQADV 1JYK LEU A 22 UNP Q97QE9 MET 17 CONFLICT SEQADV 1JYK MSE A 114 UNP Q97QE9 MET 109 CLONING ARTIFACT SEQADV 1JYK MSE A 194 UNP Q97QE9 MET 189 CLONING ARTIFACT SEQRES 1 A 254 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY SEQRES 2 A 254 LEU VAL PRO ARG GLY SER HIS MET LYS GLU ILE ARG VAL SEQRES 3 A 254 LYS ALA ILE ILE LEU ALA ALA GLY LEU GLY THR ARG LEU SEQRES 4 A 254 ARG PRO LEU THR GLU ASN THR PRO LYS ALA LEU VAL GLN SEQRES 5 A 254 VAL ASN GLN LYS PRO LEU ILE GLU TYR GLN ILE GLU PHE SEQRES 6 A 254 LEU LYS GLU LYS GLY ILE ASN ASP ILE ILE ILE ILE VAL SEQRES 7 A 254 GLY TYR LEU LYS GLU GLN PHE ASP TYR LEU LYS GLU LYS SEQRES 8 A 254 TYR GLY VAL ARG LEU VAL PHE ASN ASP LYS TYR ALA ASP SEQRES 9 A 254 TYR ASN ASN PHE TYR SER LEU TYR LEU VAL LYS GLU GLU SEQRES 10 A 254 LEU ALA ASN SER TYR VAL ILE ASP ALA ASP ASN TYR LEU SEQRES 11 A 254 PHE LYS ASN MSE PHE ARG ASN ASP LEU THR ARG SER THR SEQRES 12 A 254 TYR PHE SER VAL TYR ARG GLU ASP CYS THR ASN GLU TRP SEQRES 13 A 254 PHE LEU VAL TYR GLY ASP ASP TYR LYS VAL GLN ASP ILE SEQRES 14 A 254 ILE VAL ASP SER LYS ALA GLY ARG ILE LEU SER GLY VAL SEQRES 15 A 254 SER PHE TRP ASP ALA PRO THR ALA GLU LYS ILE VAL SER SEQRES 16 A 254 PHE ILE ASP LYS ALA TYR VAL SER GLY GLU PHE VAL ASP SEQRES 17 A 254 LEU TYR TRP ASP ASN MSE VAL LYS ASP ASN ILE LYS GLU SEQRES 18 A 254 LEU ASP VAL TYR VAL GLU GLU LEU GLU GLY ASN SER ILE SEQRES 19 A 254 TYR GLU ILE ASP SER VAL GLN ASP TYR ARG LYS LEU GLU SEQRES 20 A 254 GLU ILE LEU LYS ASN GLU ASN MODRES 1JYK MSE A 114 MET SELENOMETHIONINE MODRES 1JYK MSE A 194 MET SELENOMETHIONINE HET MSE A 114 8 HET MSE A 194 8 HETNAM MSE SELENOMETHIONINE FORMUL 1 MSE 2(C5 H11 N O2 SE) FORMUL 2 HOH *237(H2 O) HELIX 1 1 GLY A 16 ARG A 20 5 5 HELIX 2 2 PRO A 27 LEU A 30 5 4 HELIX 3 3 LEU A 38 LYS A 49 1 12 HELIX 4 4 LEU A 61 ASP A 66 5 6 HELIX 5 5 TYR A 67 GLY A 73 1 7 HELIX 6 6 ASN A 87 LEU A 93 1 7 HELIX 7 7 VAL A 94 LEU A 98 5 5 HELIX 8 8 ASP A 166 VAL A 182 1 17 HELIX 9 9 ASP A 192 ASP A 197 1 6 HELIX 10 10 ASN A 198 LEU A 202 5 5 HELIX 11 11 SER A 219 LYS A 231 1 13 SHEET 1 A 7 ARG A 75 PHE A 78 0 SHEET 2 A 7 ILE A 54 VAL A 58 1 N ILE A 56 O ARG A 75 SHEET 3 A 7 LYS A 7 ALA A 12 1 N ALA A 8 O ILE A 55 SHEET 4 A 7 SER A 101 ASP A 105 1 O ILE A 104 N ILE A 9 SHEET 5 A 7 VAL A 162 TRP A 165 -1 O SER A 163 N VAL A 103 SHEET 6 A 7 SER A 122 SER A 126 -1 N THR A 123 O PHE A 164 SHEET 7 A 7 VAL A 204 GLU A 208 1 O GLU A 207 N TYR A 124 SHEET 1 B 2 GLN A 32 VAL A 33 0 SHEET 2 B 2 LYS A 36 PRO A 37 -1 O LYS A 36 N VAL A 33 SHEET 1 C 2 ASN A 108 LEU A 110 0 SHEET 2 C 2 ILE A 214 GLU A 216 -1 O TYR A 215 N TYR A 109 SHEET 1 D 2 TYR A 128 ARG A 129 0 SHEET 2 D 2 GLY A 156 ARG A 157 -1 O GLY A 156 N ARG A 129 SHEET 1 E 2 PHE A 137 TYR A 140 0 SHEET 2 E 2 VAL A 146 ILE A 150 -1 O ILE A 150 N PHE A 137 LINK C ASN A 113 N MSE A 114 1555 1555 1.30 LINK C MSE A 114 N PHE A 115 1555 1555 1.33 LINK C ASN A 193 N MSE A 194 1555 1555 1.32 LINK C MSE A 194 N VAL A 195 1555 1555 1.32 CISPEP 1 ARG A 20 PRO A 21 0 -0.42 CRYST1 42.620 63.590 122.380 90.00 90.00 90.00 P 21 21 21 4 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.023463 0.000000 0.000000 0.00000 SCALE2 0.000000 0.015726 0.000000 0.00000 SCALE3 0.000000 0.000000 0.008171 0.00000 ATOM 1 N GLU A 3 3.631 17.253 17.648 1.00 49.15 N ATOM 2 CA GLU A 3 4.209 17.695 16.339 1.00 48.22 C ATOM 3 C GLU A 3 4.158 16.581 15.322 1.00 48.54 C ATOM 4 O GLU A 3 5.202 15.994 15.015 1.00 48.58 O ATOM 5 CB GLU A 3 5.654 18.161 16.524 1.00 46.85 C ATOM 6 CG GLU A 3 5.941 19.489 15.852 1.00 47.06 C ATOM 7 CD GLU A 3 7.413 19.869 15.859 1.00 48.39 C ATOM 8 OE1 GLU A 3 7.708 21.039 15.539 1.00 48.24 O ATOM 9 OE2 GLU A 3 8.271 19.013 16.178 1.00 48.00 O ATOM 10 N ILE A 4 2.976 16.290 14.819 1.00 48.30 N ATOM 11 CA ILE A 4 2.844 15.224 13.842 1.00 47.26 C ATOM 12 C ILE A 4 3.365 15.648 12.499 1.00 46.31 C ATOM 13 O ILE A 4 2.632 15.918 11.542 1.00 49.04 O ATOM 14 CB ILE A 4 1.406 14.707 13.696 1.00 47.69 C ATOM 15 CG1 ILE A 4 0.625 14.991 14.977 1.00 48.87 C ATOM 16 CG2 ILE A 4 1.438 13.209 13.426 1.00 46.74 C ATOM 17 CD1 ILE A 4 -0.724 14.298 15.041 1.00 49.90 C ATOM 18 N ARG A 5 4.686 15.750 12.486 1.00 43.19 N ATOM 19 CA ARG A 5 5.474 16.063 11.335 1.00 40.15 C ATOM 20 C ARG A 5 6.659 15.221 11.743 1.00 36.33 C ATOM 21 O ARG A 5 7.404 15.587 12.657 1.00 35.22 O ATOM 22 CB ARG A 5 5.899 17.530 11.289 1.00 42.96 C ATOM 23 CG ARG A 5 7.257 17.711 10.597 1.00 45.64 C ATOM 24 CD ARG A 5 7.891 19.044 10.930 1.00 48.17 C ATOM 25 NE ARG A 5 7.857 19.988 9.810 1.00 49.63 N ATOM 26 CZ ARG A 5 6.971 19.970 8.827 1.00 50.18 C ATOM 27 NH1 ARG A 5 6.005 19.049 8.788 1.00 49.84 N ATOM 28 NH2 ARG A 5 7.022 20.889 7.865 1.00 51.03 N ATOM 29 N VAL A 6 6.791 14.060 11.126 1.00 32.06 N ATOM 30 CA VAL A 6 7.915 13.201 11.438 1.00 27.96 C ATOM 31 C VAL A 6 9.114 13.850 10.754 1.00 25.36 C ATOM 32 O VAL A 6 9.060 14.189 9.569 1.00 25.49 O ATOM 33 CB VAL A 6 7.696 11.763 10.900 1.00 27.00 C ATOM 34 CG1 VAL A 6 8.987 10.958 11.005 1.00 25.00 C ATOM 35 CG2 VAL A 6 6.580 11.079 11.696 1.00 25.94 C ATOM 36 N LYS A 7 10.187 14.052 11.506 1.00 22.04 N ATOM 37 CA LYS A 7 11.382 14.667 10.945 1.00 20.61 C ATOM 38 C LYS A 7 12.597 13.862 11.337 1.00 17.40 C ATOM 39 O LYS A 7 12.479 12.781 11.910 1.00 16.79 O ATOM 40 CB LYS A 7 11.544 16.103 11.453 1.00 22.25 C ATOM 41 CG LYS A 7 10.241 16.812 11.756 1.00 25.68 C ATOM 42 CD LYS A 7 10.453 17.991 12.705 1.00 27.40 C ATOM 43 CE LYS A 7 10.394 17.553 14.158 1.00 27.54 C ATOM 44 NZ LYS A 7 9.069 16.975 14.525 1.00 28.90 N ATOM 45 N ALA A 8 13.770 14.393 11.030 1.00 15.96 N ATOM 46 CA ALA A 8 15.007 13.712 11.372 1.00 14.84 C ATOM 47 C ALA A 8 16.103 14.696 11.752 1.00 15.18 C ATOM 48 O ALA A 8 16.236 15.763 11.150 1.00 16.19 O ATOM 49 CB ALA A 8 15.469 12.846 10.207 1.00 14.29 C ATOM 50 N ILE A 9 16.876 14.323 12.762 1.00 14.51 N ATOM 51 CA ILE A 9 17.993 15.121 13.243 1.00 14.49 C ATOM 52 C ILE A 9 19.228 14.251 13.032 1.00 14.01 C ATOM 53 O ILE A 9 19.276 13.114 13.504 1.00 14.31 O ATOM 54 CB ILE A 9 17.850 15.443 14.757 1.00 14.02 C ATOM 55 CG1 ILE A 9 16.676 16.395 14.983 1.00 14.68 C ATOM 56 CG2 ILE A 9 19.141 16.039 15.290 1.00 13.76 C ATOM 57 CD1 ILE A 9 16.067 16.292 16.378 1.00 14.04 C ATOM 58 N ILE A 10 20.211 14.769 12.307 1.00 13.44 N ATOM 59 CA ILE A 10 21.437 14.025 12.054 1.00 13.09 C ATOM 60 C ILE A 10 22.585 14.699 12.799 1.00 14.18 C ATOM 61 O ILE A 10 22.851 15.895 12.617 1.00 13.55 O ATOM 62 CB ILE A 10 21.760 13.956 10.534 1.00 12.03 C ATOM 63 CG1 ILE A 10 20.560 13.375 9.779 1.00 12.82 C ATOM 64 CG2 ILE A 10 23.005 13.103 10.297 1.00 11.59 C ATOM 65 CD1 ILE A 10 20.771 13.243 8.276 1.00 13.01 C ATOM 66 N LEU A 11 23.252 13.931 13.653 1.00 13.57 N ATOM 67 CA LEU A 11 24.361 14.448 14.443 1.00 14.52 C ATOM 68 C LEU A 11 25.663 14.328 13.658 1.00 14.73 C ATOM 69 O LEU A 11 26.225 13.240 13.533 1.00 16.73 O ATOM 70 CB LEU A 11 24.457 13.678 15.765 1.00 14.54 C ATOM 71 CG LEU A 11 23.170 13.612 16.596 1.00 14.83 C ATOM 72 CD1 LEU A 11 23.392 12.726 17.819 1.00 15.74 C ATOM 73 CD2 LEU A 11 22.751 15.007 17.016 1.00 16.42 C ATOM 74 N ALA A 12 26.141 15.456 13.134 1.00 13.99 N ATOM 75 CA ALA A 12 27.359 15.470 12.335 1.00 14.04 C ATOM 76 C ALA A 12 28.332 16.607 12.695 1.00 15.10 C ATOM 77 O ALA A 12 29.081 17.071 11.835 1.00 15.55 O ATOM 78 CB ALA A 12 26.980 15.563 10.848 1.00 13.97 C ATOM 79 N ALA A 13 28.346 17.038 13.955 1.00 15.26 N ATOM 80 CA ALA A 13 29.224 18.137 14.360 1.00 16.23 C ATOM 81 C ALA A 13 30.601 17.759 14.912 1.00 16.55 C ATOM 82 O ALA A 13 31.537 18.557 14.841 1.00 16.82 O ATOM 83 CB ALA A 13 28.497 19.018 15.370 1.00 15.57 C ATOM 84 N GLY A 14 30.721 16.549 15.451 1.00 17.47 N ATOM 85 CA GLY A 14 31.969 16.102 16.057 1.00 17.27 C ATOM 86 C GLY A 14 33.237 16.016 15.226 1.00 19.31 C ATOM 87 O GLY A 14 33.207 16.010 13.994 1.00 19.26 O ATOM 88 N LEU A 15 34.366 15.924 15.924 1.00 19.88 N ATOM 89 CA LEU A 15 35.676 15.839 15.291 1.00 20.69 C ATOM 90 C LEU A 15 35.996 14.490 14.627 1.00 21.79 C ATOM 91 O LEU A 15 36.821 14.430 13.709 1.00 22.15 O ATOM 92 CB LEU A 15 36.764 16.173 16.319 1.00 21.79 C ATOM 93 CG LEU A 15 36.731 17.595 16.888 1.00 24.07 C ATOM 94 CD1 LEU A 15 37.463 17.637 18.218 1.00 24.59 C ATOM 95 CD2 LEU A 15 37.370 18.550 15.906 1.00 24.33 C ATOM 96 N GLY A 16 35.361 13.410 15.086 1.00 20.71 N ATOM 97 CA GLY A 16 35.623 12.103 14.499 1.00 19.96 C ATOM 98 C GLY A 16 37.091 11.716 14.554 1.00 21.22 C ATOM 99 O GLY A 16 37.605 11.035 13.664 1.00 20.74 O ATOM 100 N THR A 17 37.767 12.151 15.612 1.00 21.97 N ATOM 101 CA THR A 17 39.187 11.872 15.813 1.00 23.46 C ATOM 102 C THR A 17 39.573 10.404 15.637 1.00 23.81 C ATOM 103 O THR A 17 40.617 10.097 15.051 1.00 23.82 O ATOM 104 CB THR A 17 39.623 12.316 17.216 1.00 24.89 C ATOM 105 OG1 THR A 17 39.292 13.698 17.396 1.00 26.44 O ATOM 106 CG2 THR A 17 41.119 12.122 17.398 1.00 25.39 C ATOM 107 N ARG A 18 38.737 9.503 16.145 1.00 23.96 N ATOM 108 CA ARG A 18 39.004 8.068 16.052 1.00 25.25 C ATOM 109 C ARG A 18 39.056 7.544 14.609 1.00 24.48 C ATOM 110 O ARG A 18 39.558 6.443 14.362 1.00 23.66 O ATOM 111 CB ARG A 18 37.942 7.288 16.838 1.00 27.60 C ATOM 112 CG ARG A 18 36.584 7.256 16.151 1.00 32.41 C ATOM 113 CD ARG A 18 35.615 6.282 16.811 1.00 37.41 C ATOM 114 NE ARG A 18 34.266 6.250 16.222 1.00 44.05 N ATOM 115 CZ ARG A 18 33.830 6.981 15.189 1.00 47.85 C ATOM 116 NH1 ARG A 18 34.618 7.851 14.566 1.00 50.09 N ATOM 117 NH2 ARG A 18 32.578 6.837 14.772 1.00 48.14 N ATOM 118 N LEU A 19 38.548 8.326 13.661 1.00 22.90 N ATOM 119 CA LEU A 19 38.544 7.893 12.272 1.00 22.27 C ATOM 120 C LEU A 19 39.773 8.340 11.503 1.00 23.23 C ATOM 121 O LEU A 19 39.862 8.122 10.296 1.00 22.11 O ATOM 122 CB LEU A 19 37.287 8.396 11.563 1.00 22.62 C ATOM 123 CG LEU A 19 35.960 7.866 12.103 1.00 23.27 C ATOM 124 CD1 LEU A 19 34.818 8.403 11.261 1.00 23.62 C ATOM 125 CD2 LEU A 19 35.968 6.348 12.088 1.00 23.00 C ATOM 126 N ARG A 20 40.722 8.962 12.194 1.00 24.54 N ATOM 127 CA ARG A 20 41.948 9.423 11.543 1.00 26.86 C ATOM 128 C ARG A 20 42.547 8.301 10.688 1.00 25.05 C ATOM 129 O ARG A 20 42.517 7.132 11.077 1.00 25.77 O ATOM 130 CB ARG A 20 42.959 9.888 12.598 1.00 30.81 C ATOM 131 CG ARG A 20 44.282 9.114 12.622 1.00 39.28 C ATOM 132 CD ARG A 20 45.329 9.709 11.659 1.00 43.28 C ATOM 133 NE ARG A 20 45.250 11.168 11.556 1.00 48.87 N ATOM 134 CZ ARG A 20 45.939 11.909 10.687 1.00 49.54 C ATOM 135 NH1 ARG A 20 46.772 11.341 9.830 1.00 51.08 N ATOM 136 NH2 ARG A 20 45.796 13.226 10.680 1.00 49.81 N ATOM 137 N PRO A 21 43.119 8.636 9.516 1.00 23.42 N ATOM 138 CA PRO A 21 43.284 9.941 8.855 1.00 22.05 C ATOM 139 C PRO A 21 42.083 10.461 8.047 1.00 20.71 C ATOM 140 O PRO A 21 42.163 11.522 7.427 1.00 19.82 O ATOM 141 CB PRO A 21 44.473 9.702 7.938 1.00 22.23 C ATOM 142 CG PRO A 21 44.241 8.281 7.477 1.00 22.09 C ATOM 143 CD PRO A 21 43.709 7.553 8.703 1.00 22.48 C ATOM 144 N LEU A 22 40.983 9.718 8.046 1.00 18.85 N ATOM 145 CA LEU A 22 39.802 10.103 7.278 1.00 18.25 C ATOM 146 C LEU A 22 39.213 11.466 7.615 1.00 17.70 C ATOM 147 O LEU A 22 38.645 12.136 6.743 1.00 16.47 O ATOM 148 CB LEU A 22 38.701 9.055 7.450 1.00 16.67 C ATOM 149 CG LEU A 22 39.008 7.643 6.962 1.00 15.96 C ATOM 150 CD1 LEU A 22 37.948 6.692 7.500 1.00 16.25 C ATOM 151 CD2 LEU A 22 39.047 7.625 5.443 1.00 17.50 C ATOM 152 N THR A 23 39.348 11.872 8.872 1.00 17.13 N ATOM 153 CA THR A 23 38.761 13.124 9.329 1.00 16.16 C ATOM 154 C THR A 23 39.720 14.275 9.520 1.00 16.21 C ATOM 155 O THR A 23 39.379 15.264 10.168 1.00 15.61 O ATOM 156 CB THR A 23 38.018 12.907 10.645 1.00 16.42 C ATOM 157 OG1 THR A 23 38.855 12.155 11.533 1.00 15.81 O ATOM 158 CG2 THR A 23 36.722 12.141 10.396 1.00 16.29 C ATOM 159 N GLU A 24 40.918 14.158 8.964 1.00 16.59 N ATOM 160 CA GLU A 24 41.884 15.231 9.098 1.00 20.08 C ATOM 161 C GLU A 24 41.407 16.491 8.361 1.00 19.43 C ATOM 162 O GLU A 24 41.544 17.606 8.871 1.00 18.26 O ATOM 163 CB GLU A 24 43.241 14.786 8.557 1.00 25.00 C ATOM 164 CG GLU A 24 44.231 15.919 8.454 1.00 36.31 C ATOM 165 CD GLU A 24 45.644 15.445 8.219 1.00 41.71 C ATOM 166 OE1 GLU A 24 46.578 16.157 8.653 1.00 46.05 O ATOM 167 OE2 GLU A 24 45.814 14.368 7.603 1.00 45.47 O ATOM 168 N ASN A 25 40.839 16.308 7.170 1.00 18.54 N ATOM 169 CA ASN A 25 40.352 17.429 6.365 1.00 18.09 C ATOM 170 C ASN A 25 38.930 17.220 5.888 1.00 17.79 C ATOM 171 O ASN A 25 38.433 17.984 5.063 1.00 18.53 O ATOM 172 CB ASN A 25 41.237 17.635 5.141 1.00 19.68 C ATOM 173 CG ASN A 25 42.625 18.086 5.503 1.00 22.72 C ATOM 174 OD1 ASN A 25 43.443 17.290 5.969 1.00 26.18 O ATOM 175 ND2 ASN A 25 42.906 19.369 5.295 1.00 22.89 N ATOM 176 N THR A 26 38.280 16.181 6.391 1.00 16.99 N ATOM 177 CA THR A 26 36.911 15.889 5.998 1.00 15.68 C ATOM 178 C THR A 26 36.083 15.535 7.214 1.00 16.16 C ATOM 179 O THR A 26 36.501 14.719 8.033 1.00 17.31 O ATOM 180 CB THR A 26 36.847 14.695 5.040 1.00 13.69 C ATOM 181 OG1 THR A 26 37.688 14.942 3.915 1.00 15.46 O ATOM 182 CG2 THR A 26 35.417 14.463 4.572 1.00 14.44 C ATOM 183 N PRO A 27 34.907 16.166 7.366 1.00 16.59 N ATOM 184 CA PRO A 27 34.082 15.827 8.530 1.00 16.80 C ATOM 185 C PRO A 27 33.631 14.372 8.335 1.00 16.97 C ATOM 186 O PRO A 27 33.413 13.935 7.201 1.00 17.13 O ATOM 187 CB PRO A 27 32.930 16.830 8.462 1.00 17.76 C ATOM 188 CG PRO A 27 32.897 17.283 7.033 1.00 15.07 C ATOM 189 CD PRO A 27 34.294 17.205 6.521 1.00 14.70 C ATOM 190 N LYS A 28 33.495 13.618 9.418 1.00 16.51 N ATOM 191 CA LYS A 28 33.123 12.220 9.268 1.00 16.73 C ATOM 192 C LYS A 28 31.817 11.964 8.516 1.00 15.73 C ATOM 193 O LYS A 28 31.694 10.946 7.835 1.00 15.91 O ATOM 194 CB LYS A 28 33.116 11.515 10.630 1.00 18.46 C ATOM 195 CG LYS A 28 32.016 11.917 11.559 1.00 23.04 C ATOM 196 CD LYS A 28 32.286 11.368 12.947 1.00 27.60 C ATOM 197 CE LYS A 28 31.172 11.749 13.903 1.00 29.94 C ATOM 198 NZ LYS A 28 31.156 10.864 15.094 1.00 32.63 N ATOM 199 N ALA A 29 30.854 12.879 8.614 1.00 14.73 N ATOM 200 CA ALA A 29 29.578 12.701 7.915 1.00 15.15 C ATOM 201 C ALA A 29 29.761 12.785 6.403 1.00 14.52 C ATOM 202 O ALA A 29 28.921 12.300 5.637 1.00 13.74 O ATOM 203 CB ALA A 29 28.564 13.756 8.370 1.00 13.13 C ATOM 204 N LEU A 30 30.862 13.395 5.977 1.00 13.99 N ATOM 205 CA LEU A 30 31.126 13.557 4.551 1.00 15.35 C ATOM 206 C LEU A 30 32.215 12.630 3.995 1.00 15.79 C ATOM 207 O LEU A 30 32.631 12.766 2.841 1.00 14.12 O ATOM 208 CB LEU A 30 31.450 15.025 4.250 1.00 15.50 C ATOM 209 CG LEU A 30 30.306 16.004 4.570 1.00 15.23 C ATOM 210 CD1 LEU A 30 30.726 17.407 4.162 1.00 16.73 C ATOM 211 CD2 LEU A 30 29.022 15.607 3.843 1.00 15.38 C ATOM 212 N VAL A 31 32.678 11.691 4.815 1.00 15.18 N ATOM 213 CA VAL A 31 33.671 10.728 4.359 1.00 14.79 C ATOM 214 C VAL A 31 32.927 9.917 3.289 1.00 15.63 C ATOM 215 O VAL A 31 31.763 9.550 3.473 1.00 15.13 O ATOM 216 CB VAL A 31 34.136 9.812 5.526 1.00 14.83 C ATOM 217 CG1 VAL A 31 34.745 8.526 4.988 1.00 13.43 C ATOM 218 CG2 VAL A 31 35.161 10.548 6.372 1.00 12.99 C ATOM 219 N GLN A 32 33.581 9.651 2.168 1.00 16.30 N ATOM 220 CA GLN A 32 32.923 8.921 1.091 1.00 17.83 C ATOM 221 C GLN A 32 33.139 7.411 1.071 1.00 18.46 C ATOM 222 O GLN A 32 34.262 6.927 1.194 1.00 18.23 O ATOM 223 CB GLN A 32 33.346 9.506 -0.257 1.00 18.96 C ATOM 224 CG GLN A 32 33.265 11.018 -0.307 1.00 20.69 C ATOM 225 CD GLN A 32 33.538 11.577 -1.683 1.00 22.85 C ATOM 226 OE1 GLN A 32 33.494 10.860 -2.682 1.00 25.56 O ATOM 227 NE2 GLN A 32 33.817 12.870 -1.745 1.00 23.38 N ATOM 228 N VAL A 33 32.045 6.672 0.937 1.00 18.74 N ATOM 229 CA VAL A 33 32.107 5.222 0.840 1.00 20.43 C ATOM 230 C VAL A 33 31.461 4.941 -0.504 1.00 20.11 C ATOM 231 O VAL A 33 30.394 5.475 -0.820 1.00 18.10 O ATOM 232 CB VAL A 33 31.348 4.502 1.999 1.00 20.99 C ATOM 233 CG1 VAL A 33 31.900 4.971 3.332 1.00 21.68 C ATOM 234 CG2 VAL A 33 29.857 4.757 1.918 1.00 23.37 C ATOM 235 N ASN A 34 32.128 4.125 -1.310 1.00 21.37 N ATOM 236 CA ASN A 34 31.634 3.823 -2.643 1.00 22.67 C ATOM 237 C ASN A 34 31.421 5.148 -3.369 1.00 22.30 C ATOM 238 O ASN A 34 30.411 5.345 -4.051 1.00 23.38 O ATOM 239 CB ASN A 34 30.322 3.041 -2.583 1.00 25.15 C ATOM 240 CG ASN A 34 30.080 2.214 -3.833 1.00 27.31 C ATOM 241 OD1 ASN A 34 31.002 1.941 -4.598 1.00 29.03 O ATOM 242 ND2 ASN A 34 28.833 1.813 -4.043 1.00 29.55 N ATOM 243 N GLN A 35 32.372 6.061 -3.177 1.00 21.42 N ATOM 244 CA GLN A 35 32.373 7.374 -3.819 1.00 22.06 C ATOM 245 C GLN A 35 31.193 8.290 -3.526 1.00 20.49 C ATOM 246 O GLN A 35 30.839 9.124 -4.359 1.00 20.54 O ATOM 247 CB GLN A 35 32.498 7.205 -5.339 1.00 26.55 C ATOM 248 CG GLN A 35 33.738 6.436 -5.793 1.00 32.26 C ATOM 249 CD GLN A 35 35.045 7.030 -5.259 1.00 38.49 C ATOM 250 OE1 GLN A 35 36.011 6.302 -5.004 1.00 39.73 O ATOM 251 NE2 GLN A 35 35.079 8.356 -5.091 1.00 39.44 N ATOM 252 N LYS A 36 30.593 8.152 -2.349 1.00 19.39 N ATOM 253 CA LYS A 36 29.452 8.986 -1.979 1.00 17.73 C ATOM 254 C LYS A 36 29.499 9.308 -0.485 1.00 16.87 C ATOM 255 O LYS A 36 29.648 8.408 0.334 1.00 16.77 O ATOM 256 CB LYS A 36 28.152 8.250 -2.321 1.00 16.89 C ATOM 257 CG LYS A 36 26.876 9.008 -2.005 1.00 17.19 C ATOM 258 CD LYS A 36 25.674 8.312 -2.635 1.00 17.63 C ATOM 259 CE LYS A 36 24.377 9.016 -2.289 1.00 17.01 C ATOM 260 NZ LYS A 36 24.271 10.308 -3.008 1.00 17.18 N ATOM 261 N PRO A 37 29.394 10.600 -0.113 1.00 16.63 N ATOM 262 CA PRO A 37 29.429 10.971 1.311 1.00 15.76 C ATOM 263 C PRO A 37 28.422 10.166 2.123 1.00 14.96 C ATOM 264 O PRO A 37 27.271 10.006 1.718 1.00 15.23 O ATOM 265 CB PRO A 37 29.097 12.462 1.308 1.00 15.40 C ATOM 266 CG PRO A 37 29.546 12.934 -0.043 1.00 16.29 C ATOM 267 CD PRO A 37 29.256 11.783 -0.982 1.00 16.66 C ATOM 268 N LEU A 38 28.861 9.661 3.270 1.00 15.43 N ATOM 269 CA LEU A 38 28.012 8.854 4.141 1.00 14.55 C ATOM 270 C LEU A 38 26.632 9.441 4.411 1.00 13.30 C ATOM 271 O LEU A 38 25.624 8.745 4.313 1.00 13.71 O ATOM 272 CB LEU A 38 28.705 8.624 5.486 1.00 16.61 C ATOM 273 CG LEU A 38 29.751 7.516 5.574 1.00 18.26 C ATOM 274 CD1 LEU A 38 30.408 7.570 6.944 1.00 19.53 C ATOM 275 CD2 LEU A 38 29.107 6.168 5.347 1.00 17.69 C ATOM 276 N ILE A 39 26.586 10.722 4.764 1.00 12.78 N ATOM 277 CA ILE A 39 25.317 11.358 5.087 1.00 12.73 C ATOM 278 C ILE A 39 24.309 11.369 3.934 1.00 12.74 C ATOM 279 O ILE A 39 23.097 11.384 4.168 1.00 12.79 O ATOM 280 CB ILE A 39 25.543 12.809 5.609 1.00 13.12 C ATOM 281 CG1 ILE A 39 24.295 13.293 6.350 1.00 12.86 C ATOM 282 CG2 ILE A 39 25.903 13.740 4.459 1.00 11.98 C ATOM 283 CD1 ILE A 39 24.555 14.487 7.253 1.00 14.17 C ATOM 284 N GLU A 40 24.796 11.359 2.695 1.00 13.46 N ATOM 285 CA GLU A 40 23.892 11.363 1.546 1.00 13.80 C ATOM 286 C GLU A 40 23.065 10.075 1.481 1.00 13.39 C ATOM 287 O GLU A 40 21.893 10.102 1.113 1.00 13.78 O ATOM 288 CB GLU A 40 24.680 11.562 0.247 1.00 14.71 C ATOM 289 CG GLU A 40 25.156 12.998 0.072 1.00 15.78 C ATOM 290 CD GLU A 40 25.762 13.280 -1.295 1.00 17.85 C ATOM 291 OE1 GLU A 40 25.752 12.385 -2.169 1.00 16.30 O ATOM 292 OE2 GLU A 40 26.251 14.410 -1.490 1.00 18.68 O ATOM 293 N TYR A 41 23.667 8.947 1.841 1.00 13.08 N ATOM 294 CA TYR A 41 22.931 7.688 1.836 1.00 13.13 C ATOM 295 C TYR A 41 21.769 7.789 2.820 1.00 12.45 C ATOM 296 O TYR A 41 20.666 7.332 2.540 1.00 13.45 O ATOM 297 CB TYR A 41 23.835 6.529 2.261 1.00 13.16 C ATOM 298 CG TYR A 41 24.881 6.140 1.243 1.00 13.53 C ATOM 299 CD1 TYR A 41 26.200 6.573 1.373 1.00 12.98 C ATOM 300 CD2 TYR A 41 24.565 5.295 0.174 1.00 14.77 C ATOM 301 CE1 TYR A 41 27.182 6.174 0.471 1.00 14.32 C ATOM 302 CE2 TYR A 41 25.543 4.888 -0.739 1.00 15.29 C ATOM 303 CZ TYR A 41 26.847 5.330 -0.582 1.00 15.22 C ATOM 304 OH TYR A 41 27.821 4.930 -1.464 1.00 15.92 O ATOM 305 N GLN A 42 22.030 8.391 3.977 1.00 12.55 N ATOM 306 CA GLN A 42 21.014 8.546 5.012 1.00 12.04 C ATOM 307 C GLN A 42 19.911 9.508 4.586 1.00 12.43 C ATOM 308 O GLN A 42 18.728 9.194 4.711 1.00 13.34 O ATOM 309 CB GLN A 42 21.653 9.037 6.315 1.00 12.45 C ATOM 310 CG GLN A 42 22.788 8.145 6.827 1.00 14.04 C ATOM 311 CD GLN A 42 23.460 8.709 8.075 1.00 15.99 C ATOM 312 OE1 GLN A 42 23.463 9.922 8.306 1.00 15.93 O ATOM 313 NE2 GLN A 42 24.030 7.827 8.887 1.00 17.31 N ATOM 314 N ILE A 43 20.301 10.683 4.091 1.00 12.68 N ATOM 315 CA ILE A 43 19.341 11.692 3.638 1.00 12.82 C ATOM 316 C ILE A 43 18.409 11.130 2.550 1.00 12.39 C ATOM 317 O ILE A 43 17.196 11.359 2.576 1.00 12.54 O ATOM 318 CB ILE A 43 20.074 12.952 3.083 1.00 12.63 C ATOM 319 CG1 ILE A 43 20.695 13.752 4.235 1.00 11.79 C ATOM 320 CG2 ILE A 43 19.096 13.850 2.340 1.00 13.18 C ATOM 321 CD1 ILE A 43 21.742 14.760 3.786 1.00 12.51 C ATOM 322 N GLU A 44 18.974 10.382 1.606 1.00 12.95 N ATOM 323 CA GLU A 44 18.175 9.811 0.523 1.00 13.87 C ATOM 324 C GLU A 44 17.194 8.751 1.032 1.00 14.44 C ATOM 325 O GLU A 44 16.062 8.676 0.554 1.00 14.27 O ATOM 326 CB GLU A 44 19.097 9.254 -0.566 1.00 13.18 C ATOM 327 CG GLU A 44 19.641 10.370 -1.444 1.00 14.41 C ATOM 328 CD GLU A 44 20.733 9.932 -2.396 1.00 16.78 C ATOM 329 OE1 GLU A 44 21.603 10.771 -2.713 1.00 17.72 O ATOM 330 OE2 GLU A 44 20.726 8.767 -2.837 1.00 16.76 O ATOM 331 N PHE A 45 17.621 7.949 2.007 1.00 14.73 N ATOM 332 CA PHE A 45 16.750 6.929 2.591 1.00 13.58 C ATOM 333 C PHE A 45 15.558 7.629 3.223 1.00 12.94 C ATOM 334 O PHE A 45 14.414 7.208 3.067 1.00 13.41 O ATOM 335 CB PHE A 45 17.491 6.145 3.679 1.00 14.51 C ATOM 336 CG PHE A 45 18.118 4.864 3.198 1.00 16.92 C ATOM 337 CD1 PHE A 45 18.958 4.136 4.036 1.00 17.19 C ATOM 338 CD2 PHE A 45 17.871 4.378 1.916 1.00 16.96 C ATOM 339 CE1 PHE A 45 19.540 2.947 3.607 1.00 17.00 C ATOM 340 CE2 PHE A 45 18.449 3.192 1.481 1.00 17.05 C ATOM 341 CZ PHE A 45 19.285 2.477 2.328 1.00 17.06 C ATOM 342 N LEU A 46 15.842 8.712 3.939 1.00 11.97 N ATOM 343 CA LEU A 46 14.812 9.484 4.617 1.00 12.82 C ATOM 344 C LEU A 46 13.791 10.089 3.661 1.00 13.66 C ATOM 345 O LEU A 46 12.585 9.933 3.849 1.00 13.85 O ATOM 346 CB LEU A 46 15.457 10.603 5.428 1.00 13.78 C ATOM 347 CG LEU A 46 16.143 10.166 6.721 1.00 12.92 C ATOM 348 CD1 LEU A 46 17.159 11.228 7.146 1.00 11.76 C ATOM 349 CD2 LEU A 46 15.086 9.949 7.803 1.00 12.54 C ATOM 350 N LYS A 47 14.279 10.784 2.638 1.00 15.24 N ATOM 351 CA LYS A 47 13.395 11.416 1.668 1.00 16.14 C ATOM 352 C LYS A 47 12.602 10.389 0.867 1.00 17.06 C ATOM 353 O LYS A 47 11.473 10.657 0.456 1.00 18.04 O ATOM 354 CB LYS A 47 14.209 12.322 0.743 1.00 16.63 C ATOM 355 CG LYS A 47 15.020 13.347 1.524 1.00 18.45 C ATOM 356 CD LYS A 47 15.342 14.565 0.695 1.00 20.19 C ATOM 357 CE LYS A 47 14.183 15.531 0.685 1.00 19.11 C ATOM 358 NZ LYS A 47 14.392 16.523 -0.380 1.00 17.18 N ATOM 359 N GLU A 48 13.185 9.215 0.651 1.00 17.71 N ATOM 360 CA GLU A 48 12.493 8.159 -0.082 1.00 20.09 C ATOM 361 C GLU A 48 11.244 7.763 0.694 1.00 19.78 C ATOM 362 O GLU A 48 10.275 7.264 0.117 1.00 19.65 O ATOM 363 CB GLU A 48 13.391 6.933 -0.230 1.00 23.09 C ATOM 364 CG GLU A 48 13.863 6.671 -1.646 1.00 32.24 C ATOM 365 CD GLU A 48 15.288 6.151 -1.690 1.00 35.74 C ATOM 366 OE1 GLU A 48 15.540 5.055 -1.142 1.00 36.09 O ATOM 367 OE2 GLU A 48 16.153 6.843 -2.273 1.00 38.07 O ATOM 368 N LYS A 49 11.280 7.988 2.007 1.00 18.63 N ATOM 369 CA LYS A 49 10.168 7.646 2.887 1.00 18.16 C ATOM 370 C LYS A 49 9.282 8.829 3.239 1.00 18.69 C ATOM 371 O LYS A 49 8.373 8.710 4.066 1.00 19.45 O ATOM 372 CB LYS A 49 10.701 7.013 4.168 1.00 18.93 C ATOM 373 CG LYS A 49 11.410 5.706 3.932 1.00 19.84 C ATOM 374 CD LYS A 49 10.414 4.618 3.625 1.00 23.34 C ATOM 375 CE LYS A 49 11.080 3.419 2.988 1.00 24.51 C ATOM 376 NZ LYS A 49 10.063 2.387 2.655 1.00 28.69 N ATOM 377 N GLY A 50 9.549 9.976 2.623 1.00 17.80 N ATOM 378 CA GLY A 50 8.736 11.144 2.891 1.00 18.04 C ATOM 379 C GLY A 50 9.140 11.967 4.098 1.00 18.37 C ATOM 380 O GLY A 50 8.420 12.893 4.485 1.00 19.73 O ATOM 381 N ILE A 51 10.275 11.644 4.705 1.00 16.38 N ATOM 382 CA ILE A 51 10.738 12.408 5.855 1.00 16.03 C ATOM 383 C ILE A 51 11.664 13.472 5.281 1.00 16.63 C ATOM 384 O ILE A 51 12.880 13.303 5.212 1.00 16.54 O ATOM 385 CB ILE A 51 11.469 11.504 6.864 1.00 16.14 C ATOM 386 CG1 ILE A 51 10.535 10.365 7.296 1.00 14.44 C ATOM 387 CG2 ILE A 51 11.888 12.318 8.082 1.00 14.80 C ATOM 388 CD1 ILE A 51 11.251 9.125 7.763 1.00 15.05 C ATOM 389 N ASN A 52 11.055 14.575 4.865 1.00 17.35 N ATOM 390 CA ASN A 52 11.773 15.666 4.227 1.00 18.65 C ATOM 391 C ASN A 52 12.176 16.836 5.104 1.00 19.19 C ATOM 392 O ASN A 52 12.821 17.769 4.630 1.00 20.15 O ATOM 393 CB ASN A 52 10.952 16.154 3.044 1.00 19.64 C ATOM 394 CG ASN A 52 10.577 15.024 2.123 1.00 20.84 C ATOM 395 OD1 ASN A 52 11.348 14.078 1.953 1.00 22.73 O ATOM 396 ND2 ASN A 52 9.387 15.100 1.529 1.00 22.28 N ATOM 397 N ASP A 53 11.787 16.798 6.375 1.00 19.11 N ATOM 398 CA ASP A 53 12.169 17.847 7.307 1.00 19.05 C ATOM 399 C ASP A 53 13.398 17.287 8.003 1.00 18.25 C ATOM 400 O ASP A 53 13.292 16.572 9.005 1.00 18.66 O ATOM 401 CB ASP A 53 11.060 18.115 8.319 1.00 20.54 C ATOM 402 CG ASP A 53 11.422 19.210 9.298 1.00 24.60 C ATOM 403 OD1 ASP A 53 12.543 19.757 9.208 1.00 26.54 O ATOM 404 OD2 ASP A 53 10.587 19.528 10.168 1.00 27.76 O ATOM 405 N ILE A 54 14.561 17.615 7.450 1.00 16.52 N ATOM 406 CA ILE A 54 15.833 17.129 7.960 1.00 15.29 C ATOM 407 C ILE A 54 16.734 18.247 8.478 1.00 15.87 C ATOM 408 O ILE A 54 17.016 19.223 7.776 1.00 15.78 O ATOM 409 CB ILE A 54 16.564 16.327 6.853 1.00 13.91 C ATOM 410 CG1 ILE A 54 15.678 15.156 6.412 1.00 13.52 C ATOM 411 CG2 ILE A 54 17.928 15.841 7.347 1.00 14.29 C ATOM 412 CD1 ILE A 54 16.064 14.576 5.082 1.00 12.45 C ATOM 413 N ILE A 55 17.174 18.089 9.723 1.00 15.18 N ATOM 414 CA ILE A 55 18.044 19.052 10.383 1.00 15.67 C ATOM 415 C ILE A 55 19.386 18.384 10.659 1.00 16.38 C ATOM 416 O ILE A 55 19.443 17.296 11.239 1.00 16.86 O ATOM 417 CB ILE A 55 17.437 19.533 11.730 1.00 16.78 C ATOM 418 CG1 ILE A 55 16.027 20.094 11.498 1.00 19.48 C ATOM 419 CG2 ILE A 55 18.330 20.591 12.363 1.00 17.16 C ATOM 420 CD1 ILE A 55 15.241 20.364 12.777 1.00 20.98 C ATOM 421 N ILE A 56 20.468 19.023 10.231 1.00 14.90 N ATOM 422 CA ILE A 56 21.791 18.469 10.447 1.00 14.17 C ATOM 423 C ILE A 56 22.594 19.360 11.384 1.00 15.06 C ATOM 424 O ILE A 56 22.738 20.560 11.137 1.00 14.51 O ATOM 425 CB ILE A 56 22.559 18.316 9.118 1.00 13.56 C ATOM 426 CG1 ILE A 56 21.705 17.542 8.114 1.00 13.59 C ATOM 427 CG2 ILE A 56 23.887 17.613 9.359 1.00 12.46 C ATOM 428 CD1 ILE A 56 22.370 17.345 6.775 1.00 14.29 C ATOM 429 N ILE A 57 23.092 18.778 12.471 1.00 14.76 N ATOM 430 CA ILE A 57 23.908 19.518 13.416 1.00 14.68 C ATOM 431 C ILE A 57 25.345 19.475 12.891 1.00 14.66 C ATOM 432 O ILE A 57 25.943 18.404 12.784 1.00 14.61 O ATOM 433 CB ILE A 57 23.871 18.888 14.829 1.00 15.23 C ATOM 434 CG1 ILE A 57 22.423 18.635 15.264 1.00 15.22 C ATOM 435 CG2 ILE A 57 24.580 19.810 15.812 1.00 15.99 C ATOM 436 CD1 ILE A 57 21.503 19.833 15.096 1.00 15.65 C ATOM 437 N VAL A 58 25.892 20.641 12.561 1.00 14.87 N ATOM 438 CA VAL A 58 27.251 20.725 12.039 1.00 14.72 C ATOM 439 C VAL A 58 28.150 21.522 12.976 1.00 15.73 C ATOM 440 O VAL A 58 27.667 22.292 13.813 1.00 17.40 O ATOM 441 CB VAL A 58 27.277 21.383 10.617 1.00 15.02 C ATOM 442 CG1 VAL A 58 26.391 20.595 9.662 1.00 14.78 C ATOM 443 CG2 VAL A 58 26.811 22.841 10.688 1.00 15.20 C ATOM 444 N GLY A 59 29.457 21.327 12.834 1.00 15.00 N ATOM 445 CA GLY A 59 30.414 22.036 13.664 1.00 15.87 C ATOM 446 C GLY A 59 31.779 22.007 13.007 1.00 16.04 C ATOM 447 O GLY A 59 32.192 22.974 12.357 1.00 15.78 O ATOM 448 N TYR A 60 32.470 20.884 13.172 1.00 15.37 N ATOM 449 CA TYR A 60 33.792 20.677 12.598 1.00 15.77 C ATOM 450 C TYR A 60 33.702 20.714 11.065 1.00 16.29 C ATOM 451 O TYR A 60 32.939 19.948 10.471 1.00 15.83 O ATOM 452 CB TYR A 60 34.324 19.320 13.062 1.00 15.14 C ATOM 453 CG TYR A 60 35.674 18.954 12.506 1.00 15.91 C ATOM 454 CD1 TYR A 60 35.846 17.790 11.751 1.00 15.41 C ATOM 455 CD2 TYR A 60 36.788 19.756 12.743 1.00 16.69 C ATOM 456 CE1 TYR A 60 37.092 17.435 11.250 1.00 16.41 C ATOM 457 CE2 TYR A 60 38.039 19.412 12.247 1.00 17.31 C ATOM 458 CZ TYR A 60 38.185 18.251 11.500 1.00 17.54 C ATOM 459 OH TYR A 60 39.419 17.908 10.997 1.00 19.14 O ATOM 460 N LEU A 61 34.475 21.603 10.437 1.00 15.55 N ATOM 461 CA LEU A 61 34.487 21.760 8.972 1.00 16.19 C ATOM 462 C LEU A 61 33.080 21.914 8.376 1.00 15.68 C ATOM 463 O LEU A 61 32.789 21.417 7.280 1.00 15.68 O ATOM 464 CB LEU A 61 35.207 20.570 8.314 1.00 16.45 C ATOM 465 CG LEU A 61 36.632 20.263 8.803 1.00 15.99 C ATOM 466 CD1 LEU A 61 37.157 18.998 8.140 1.00 14.60 C ATOM 467 CD2 LEU A 61 37.541 21.440 8.493 1.00 15.60 C ATOM 468 N LYS A 62 32.222 22.636 9.093 1.00 15.72 N ATOM 469 CA LYS A 62 30.839 22.836 8.679 1.00 16.62 C ATOM 470 C LYS A 62 30.614 23.389 7.274 1.00 16.81 C ATOM 471 O LYS A 62 29.588 23.094 6.650 1.00 15.87 O ATOM 472 CB LYS A 62 30.116 23.720 9.695 1.00 17.37 C ATOM 473 CG LYS A 62 30.575 25.157 9.702 1.00 19.68 C ATOM 474 CD LYS A 62 29.799 25.961 10.733 1.00 23.05 C ATOM 475 CE LYS A 62 30.141 27.431 10.644 1.00 23.61 C ATOM 476 NZ LYS A 62 31.580 27.640 10.936 1.00 25.74 N ATOM 477 N GLU A 63 31.561 24.174 6.766 1.00 16.88 N ATOM 478 CA GLU A 63 31.402 24.756 5.435 1.00 18.64 C ATOM 479 C GLU A 63 31.293 23.708 4.322 1.00 17.14 C ATOM 480 O GLU A 63 30.802 23.997 3.232 1.00 16.97 O ATOM 481 CB GLU A 63 32.547 25.736 5.136 1.00 20.53 C ATOM 482 CG GLU A 63 33.939 25.114 5.126 1.00 26.85 C ATOM 483 CD GLU A 63 34.533 24.928 6.522 1.00 28.74 C ATOM 484 OE1 GLU A 63 33.978 25.478 7.503 1.00 27.99 O ATOM 485 OE2 GLU A 63 35.562 24.224 6.631 1.00 30.83 O ATOM 486 N GLN A 64 31.732 22.485 4.597 1.00 15.37 N ATOM 487 CA GLN A 64 31.649 21.438 3.589 1.00 15.50 C ATOM 488 C GLN A 64 30.225 20.910 3.444 1.00 14.54 C ATOM 489 O GLN A 64 29.908 20.234 2.466 1.00 15.05 O ATOM 490 CB GLN A 64 32.616 20.298 3.927 1.00 15.28 C ATOM 491 CG GLN A 64 34.086 20.712 3.777 1.00 15.04 C ATOM 492 CD GLN A 64 35.062 19.557 3.899 1.00 15.81 C ATOM 493 OE1 GLN A 64 34.776 18.432 3.479 1.00 16.16 O ATOM 494 NE2 GLN A 64 36.230 19.833 4.471 1.00 15.89 N ATOM 495 N PHE A 65 29.365 21.239 4.408 1.00 14.67 N ATOM 496 CA PHE A 65 27.964 20.796 4.396 1.00 14.45 C ATOM 497 C PHE A 65 27.012 21.735 3.642 1.00 14.90 C ATOM 498 O PHE A 65 25.888 21.356 3.320 1.00 16.88 O ATOM 499 CB PHE A 65 27.432 20.668 5.828 1.00 13.38 C ATOM 500 CG PHE A 65 28.025 19.528 6.609 1.00 13.31 C ATOM 501 CD1 PHE A 65 27.353 18.311 6.715 1.00 14.32 C ATOM 502 CD2 PHE A 65 29.246 19.676 7.259 1.00 13.64 C ATOM 503 CE1 PHE A 65 27.892 17.257 7.460 1.00 13.24 C ATOM 504 CE2 PHE A 65 29.791 18.628 8.006 1.00 13.83 C ATOM 505 CZ PHE A 65 29.110 17.418 8.104 1.00 13.35 C ATOM 506 N ASP A 66 27.452 22.957 3.370 1.00 14.98 N ATOM 507 CA ASP A 66 26.599 23.941 2.711 1.00 15.17 C ATOM 508 C ASP A 66 25.840 23.484 1.477 1.00 14.46 C ATOM 509 O ASP A 66 24.641 23.759 1.346 1.00 14.63 O ATOM 510 CB ASP A 66 27.415 25.185 2.377 1.00 18.21 C ATOM 511 CG ASP A 66 27.714 26.023 3.607 1.00 20.95 C ATOM 512 OD1 ASP A 66 26.894 26.025 4.551 1.00 22.67 O ATOM 513 OD2 ASP A 66 28.774 26.678 3.632 1.00 24.80 O ATOM 514 N TYR A 67 26.523 22.790 0.573 1.00 14.54 N ATOM 515 CA TYR A 67 25.890 22.313 -0.661 1.00 14.22 C ATOM 516 C TYR A 67 24.634 21.455 -0.450 1.00 14.03 C ATOM 517 O TYR A 67 23.802 21.340 -1.349 1.00 13.01 O ATOM 518 CB TYR A 67 26.902 21.518 -1.500 1.00 14.12 C ATOM 519 CG TYR A 67 27.084 20.074 -1.058 1.00 13.39 C ATOM 520 CD1 TYR A 67 26.577 19.020 -1.822 1.00 12.62 C ATOM 521 CD2 TYR A 67 27.767 19.766 0.126 1.00 13.05 C ATOM 522 CE1 TYR A 67 26.743 17.691 -1.422 1.00 14.01 C ATOM 523 CE2 TYR A 67 27.939 18.445 0.535 1.00 13.46 C ATOM 524 CZ TYR A 67 27.427 17.412 -0.241 1.00 14.17 C ATOM 525 OH TYR A 67 27.604 16.103 0.165 1.00 15.06 O ATOM 526 N LEU A 68 24.505 20.849 0.732 1.00 13.42 N ATOM 527 CA LEU A 68 23.363 19.990 1.026 1.00 12.33 C ATOM 528 C LEU A 68 22.041 20.737 1.135 1.00 12.10 C ATOM 529 O LEU A 68 20.979 20.151 0.957 1.00 13.24 O ATOM 530 CB LEU A 68 23.615 19.195 2.317 1.00 12.89 C ATOM 531 CG LEU A 68 24.774 18.186 2.300 1.00 11.64 C ATOM 532 CD1 LEU A 68 25.071 17.741 3.729 1.00 13.63 C ATOM 533 CD2 LEU A 68 24.424 16.980 1.422 1.00 9.22 C ATOM 534 N LYS A 69 22.092 22.030 1.423 1.00 13.60 N ATOM 535 CA LYS A 69 20.863 22.796 1.540 1.00 14.31 C ATOM 536 C LYS A 69 20.105 22.849 0.212 1.00 15.48 C ATOM 537 O LYS A 69 18.895 22.599 0.166 1.00 14.62 O ATOM 538 CB LYS A 69 21.174 24.202 2.037 1.00 16.04 C ATOM 539 CG LYS A 69 21.776 24.220 3.425 1.00 17.07 C ATOM 540 CD LYS A 69 21.915 25.640 3.940 1.00 19.92 C ATOM 541 CE LYS A 69 22.980 26.390 3.171 1.00 21.88 C ATOM 542 NZ LYS A 69 23.290 27.701 3.798 1.00 25.43 N ATOM 543 N GLU A 70 20.807 23.155 -0.875 1.00 15.13 N ATOM 544 CA GLU A 70 20.145 23.208 -2.172 1.00 16.49 C ATOM 545 C GLU A 70 20.029 21.813 -2.802 1.00 16.32 C ATOM 546 O GLU A 70 19.173 21.564 -3.652 1.00 16.34 O ATOM 547 CB GLU A 70 20.891 24.172 -3.104 1.00 17.22 C ATOM 548 CG GLU A 70 20.300 25.584 -3.077 1.00 19.76 C ATOM 549 CD GLU A 70 21.134 26.613 -3.829 1.00 19.88 C ATOM 550 OE1 GLU A 70 21.997 26.216 -4.636 1.00 18.79 O ATOM 551 OE2 GLU A 70 20.920 27.822 -3.610 1.00 19.95 O ATOM 552 N LYS A 71 20.883 20.890 -2.379 1.00 16.08 N ATOM 553 CA LYS A 71 20.825 19.548 -2.935 1.00 15.83 C ATOM 554 C LYS A 71 19.666 18.726 -2.381 1.00 15.28 C ATOM 555 O LYS A 71 19.052 17.947 -3.114 1.00 15.19 O ATOM 556 CB LYS A 71 22.134 18.804 -2.678 1.00 15.14 C ATOM 557 CG LYS A 71 22.186 17.426 -3.331 1.00 16.54 C ATOM 558 CD LYS A 71 23.597 16.872 -3.315 1.00 18.52 C ATOM 559 CE LYS A 71 23.630 15.441 -3.811 1.00 20.84 C ATOM 560 NZ LYS A 71 24.988 15.029 -4.242 1.00 22.45 N ATOM 561 N TYR A 72 19.358 18.906 -1.098 1.00 14.03 N ATOM 562 CA TYR A 72 18.289 18.135 -0.458 1.00 14.39 C ATOM 563 C TYR A 72 17.234 18.925 0.307 1.00 14.97 C ATOM 564 O TYR A 72 16.212 18.358 0.706 1.00 16.12 O ATOM 565 CB TYR A 72 18.886 17.103 0.503 1.00 13.13 C ATOM 566 CG TYR A 72 19.792 16.095 -0.146 1.00 12.08 C ATOM 567 CD1 TYR A 72 21.160 16.107 0.108 1.00 12.03 C ATOM 568 CD2 TYR A 72 19.281 15.099 -0.977 1.00 10.76 C ATOM 569 CE1 TYR A 72 21.998 15.148 -0.442 1.00 13.00 C ATOM 570 CE2 TYR A 72 20.116 14.134 -1.533 1.00 12.38 C ATOM 571 CZ TYR A 72 21.472 14.166 -1.255 1.00 11.27 C ATOM 572 OH TYR A 72 22.308 13.201 -1.754 1.00 13.50 O ATOM 573 N GLY A 73 17.476 20.212 0.528 1.00 14.17 N ATOM 574 CA GLY A 73 16.515 21.012 1.263 1.00 14.68 C ATOM 575 C GLY A 73 16.657 20.847 2.768 1.00 16.70 C ATOM 576 O GLY A 73 15.727 21.139 3.526 1.00 17.61 O ATOM 577 N VAL A 74 17.824 20.384 3.214 1.00 16.55 N ATOM 578 CA VAL A 74 18.056 20.198 4.646 1.00 16.60 C ATOM 579 C VAL A 74 18.360 21.521 5.338 1.00 17.85 C ATOM 580 O VAL A 74 18.700 22.516 4.690 1.00 17.50 O ATOM 581 CB VAL A 74 19.238 19.236 4.912 1.00 14.67 C ATOM 582 CG1 VAL A 74 18.986 17.904 4.226 1.00 14.15 C ATOM 583 CG2 VAL A 74 20.542 19.866 4.434 1.00 14.54 C ATOM 584 N ARG A 75 18.222 21.530 6.658 1.00 17.68 N ATOM 585 CA ARG A 75 18.525 22.719 7.440 1.00 20.46 C ATOM 586 C ARG A 75 19.802 22.411 8.210 1.00 18.78 C ATOM 587 O ARG A 75 19.961 21.305 8.726 1.00 20.01 O ATOM 588 CB ARG A 75 17.395 23.025 8.424 1.00 24.05 C ATOM 589 CG ARG A 75 16.212 23.777 7.823 1.00 30.37 C ATOM 590 CD ARG A 75 15.294 24.294 8.924 1.00 35.51 C ATOM 591 NE ARG A 75 14.560 23.213 9.584 1.00 40.39 N ATOM 592 CZ ARG A 75 13.790 23.375 10.657 1.00 42.61 C ATOM 593 NH1 ARG A 75 13.649 24.578 11.195 1.00 44.72 N ATOM 594 NH2 ARG A 75 13.156 22.334 11.187 1.00 42.40 N ATOM 595 N LEU A 76 20.717 23.369 8.277 1.00 16.99 N ATOM 596 CA LEU A 76 21.963 23.159 9.003 1.00 16.83 C ATOM 597 C LEU A 76 21.950 23.990 10.277 1.00 17.65 C ATOM 598 O LEU A 76 21.561 25.157 10.250 1.00 19.03 O ATOM 599 CB LEU A 76 23.169 23.552 8.137 1.00 17.24 C ATOM 600 CG LEU A 76 23.285 22.895 6.751 1.00 17.84 C ATOM 601 CD1 LEU A 76 24.541 23.389 6.044 1.00 16.95 C ATOM 602 CD2 LEU A 76 23.327 21.378 6.897 1.00 17.71 C ATOM 603 N VAL A 77 22.349 23.380 11.391 1.00 16.58 N ATOM 604 CA VAL A 77 22.407 24.076 12.675 1.00 16.99 C ATOM 605 C VAL A 77 23.833 23.978 13.216 1.00 17.96 C ATOM 606 O VAL A 77 24.344 22.882 13.480 1.00 17.86 O ATOM 607 CB VAL A 77 21.417 23.473 13.688 1.00 15.78 C ATOM 608 CG1 VAL A 77 21.523 24.197 15.023 1.00 15.59 C ATOM 609 CG2 VAL A 77 20.010 23.579 13.147 1.00 14.90 C ATOM 610 N PHE A 78 24.472 25.132 13.374 1.00 18.63 N ATOM 611 CA PHE A 78 25.849 25.198 13.847 1.00 19.82 C ATOM 612 C PHE A 78 26.009 25.037 15.352 1.00 19.39 C ATOM 613 O PHE A 78 25.389 25.747 16.133 1.00 20.18 O ATOM 614 CB PHE A 78 26.473 26.529 13.405 1.00 20.34 C ATOM 615 CG PHE A 78 27.904 26.711 13.834 1.00 21.24 C ATOM 616 CD1 PHE A 78 28.379 27.970 14.180 1.00 20.44 C ATOM 617 CD2 PHE A 78 28.778 25.630 13.886 1.00 21.66 C ATOM 618 CE1 PHE A 78 29.703 28.149 14.570 1.00 20.74 C ATOM 619 CE2 PHE A 78 30.107 25.799 14.276 1.00 22.50 C ATOM 620 CZ PHE A 78 30.569 27.060 14.618 1.00 21.57 C ATOM 621 N ASN A 79 26.850 24.089 15.745 1.00 20.23 N ATOM 622 CA ASN A 79 27.144 23.840 17.148 1.00 20.61 C ATOM 623 C ASN A 79 28.594 24.270 17.364 1.00 22.00 C ATOM 624 O ASN A 79 29.526 23.526 17.050 1.00 20.41 O ATOM 625 CB ASN A 79 26.992 22.355 17.478 1.00 20.59 C ATOM 626 CG ASN A 79 27.486 22.020 18.875 1.00 22.13 C ATOM 627 OD1 ASN A 79 27.900 22.905 19.622 1.00 21.37 O ATOM 628 ND2 ASN A 79 27.443 20.739 19.236 1.00 21.17 N ATOM 629 N ASP A 80 28.785 25.473 17.897 1.00 24.07 N ATOM 630 CA ASP A 80 30.132 25.981 18.112 1.00 27.30 C ATOM 631 C ASP A 80 30.869 25.332 19.280 1.00 26.38 C ATOM 632 O ASP A 80 32.063 25.564 19.473 1.00 27.01 O ATOM 633 CB ASP A 80 30.100 27.499 18.285 1.00 31.96 C ATOM 634 CG ASP A 80 29.458 27.921 19.579 1.00 37.17 C ATOM 635 OD1 ASP A 80 30.190 28.356 20.490 1.00 42.87 O ATOM 636 OD2 ASP A 80 28.223 27.822 19.684 1.00 39.97 O ATOM 637 N LYS A 81 30.172 24.516 20.059 1.00 24.47 N ATOM 638 CA LYS A 81 30.819 23.839 21.178 1.00 25.09 C ATOM 639 C LYS A 81 31.127 22.396 20.793 1.00 24.15 C ATOM 640 O LYS A 81 31.415 21.567 21.650 1.00 23.36 O ATOM 641 CB LYS A 81 29.915 23.851 22.416 1.00 25.92 C ATOM 642 CG LYS A 81 29.207 25.171 22.674 1.00 28.80 C ATOM 643 CD LYS A 81 30.172 26.338 22.647 1.00 31.31 C ATOM 644 CE LYS A 81 31.207 26.215 23.743 1.00 33.10 C ATOM 645 NZ LYS A 81 31.057 27.301 24.744 1.00 35.69 N ATOM 646 N TYR A 82 31.072 22.104 19.498 1.00 23.40 N ATOM 647 CA TYR A 82 31.317 20.754 19.016 1.00 24.05 C ATOM 648 C TYR A 82 32.615 20.157 19.543 1.00 25.36 C ATOM 649 O TYR A 82 32.739 18.938 19.681 1.00 25.81 O ATOM 650 CB TYR A 82 31.328 20.740 17.486 1.00 24.07 C ATOM 651 CG TYR A 82 32.558 21.373 16.878 1.00 24.15 C ATOM 652 CD1 TYR A 82 32.549 22.709 16.482 1.00 23.03 C ATOM 653 CD2 TYR A 82 33.727 20.631 16.688 1.00 23.92 C ATOM 654 CE1 TYR A 82 33.670 23.294 15.909 1.00 24.77 C ATOM 655 CE2 TYR A 82 34.858 21.205 16.115 1.00 24.72 C ATOM 656 CZ TYR A 82 34.819 22.537 15.729 1.00 25.77 C ATOM 657 OH TYR A 82 35.926 23.120 15.161 1.00 28.92 O ATOM 658 N ALA A 83 33.583 21.018 19.833 1.00 26.73 N ATOM 659 CA ALA A 83 34.873 20.559 20.328 1.00 28.99 C ATOM 660 C ALA A 83 34.992 20.663 21.843 1.00 29.89 C ATOM 661 O ALA A 83 35.846 20.018 22.445 1.00 32.14 O ATOM 662 CB ALA A 83 35.988 21.352 19.667 1.00 29.25 C ATOM 663 N ASP A 84 34.130 21.468 22.457 1.00 30.37 N ATOM 664 CA ASP A 84 34.164 21.668 23.903 1.00 29.86 C ATOM 665 C ASP A 84 33.248 20.752 24.698 1.00 28.73 C ATOM 666 O ASP A 84 33.676 20.145 25.675 1.00 30.30 O ATOM 667 CB ASP A 84 33.813 23.118 24.233 1.00 32.84 C ATOM 668 CG ASP A 84 34.578 24.103 23.383 1.00 35.07 C ATOM 669 OD1 ASP A 84 33.961 25.078 22.905 1.00 37.25 O ATOM 670 OD2 ASP A 84 35.795 23.897 23.192 1.00 36.61 O ATOM 671 N TYR A 85 31.985 20.673 24.287 1.00 25.66 N ATOM 672 CA TYR A 85 30.995 19.844 24.966 1.00 23.93 C ATOM 673 C TYR A 85 30.733 18.524 24.238 1.00 23.87 C ATOM 674 O TYR A 85 31.026 18.385 23.049 1.00 23.79 O ATOM 675 CB TYR A 85 29.656 20.576 25.073 1.00 22.71 C ATOM 676 CG TYR A 85 29.674 21.963 25.675 1.00 22.57 C ATOM 677 CD1 TYR A 85 30.744 22.417 26.447 1.00 22.68 C ATOM 678 CD2 TYR A 85 28.583 22.808 25.499 1.00 22.81 C ATOM 679 CE1 TYR A 85 30.715 23.686 27.032 1.00 23.56 C ATOM 680 CE2 TYR A 85 28.542 24.069 26.074 1.00 25.10 C ATOM 681 CZ TYR A 85 29.604 24.506 26.839 1.00 25.85 C ATOM 682 OH TYR A 85 29.526 25.764 27.406 1.00 28.56 O ATOM 683 N ASN A 86 30.162 17.566 24.962 1.00 22.96 N ATOM 684 CA ASN A 86 29.813 16.275 24.392 1.00 23.61 C ATOM 685 C ASN A 86 28.541 16.523 23.575 1.00 21.93 C ATOM 686 O ASN A 86 27.982 17.622 23.633 1.00 20.00 O ATOM 687 CB ASN A 86 29.562 15.263 25.505 1.00 28.00 C ATOM 688 CG ASN A 86 29.958 13.857 25.116 1.00 32.07 C ATOM 689 OD1 ASN A 86 29.923 13.493 23.942 1.00 34.29 O ATOM 690 ND2 ASN A 86 30.335 13.053 26.103 1.00 34.01 N ATOM 691 N ASN A 87 28.067 15.518 22.837 1.00 19.50 N ATOM 692 CA ASN A 87 26.902 15.725 21.984 1.00 17.66 C ATOM 693 C ASN A 87 25.542 15.996 22.621 1.00 16.95 C ATOM 694 O ASN A 87 24.540 16.112 21.912 1.00 17.49 O ATOM 695 CB ASN A 87 26.807 14.605 20.927 1.00 17.51 C ATOM 696 CG ASN A 87 26.309 13.283 21.483 1.00 17.52 C ATOM 697 OD1 ASN A 87 25.897 13.174 22.635 1.00 17.88 O ATOM 698 ND2 ASN A 87 26.346 12.260 20.641 1.00 18.29 N ATOM 699 N PHE A 88 25.498 16.112 23.947 1.00 16.86 N ATOM 700 CA PHE A 88 24.248 16.448 24.635 1.00 14.88 C ATOM 701 C PHE A 88 23.854 17.828 24.095 1.00 13.82 C ATOM 702 O PHE A 88 22.684 18.120 23.836 1.00 13.40 O ATOM 703 CB PHE A 88 24.487 16.558 26.154 1.00 16.04 C ATOM 704 CG PHE A 88 23.522 17.491 26.874 1.00 15.48 C ATOM 705 CD1 PHE A 88 23.750 18.865 26.927 1.00 15.72 C ATOM 706 CD2 PHE A 88 22.394 16.989 27.509 1.00 15.27 C ATOM 707 CE1 PHE A 88 22.859 19.720 27.603 1.00 16.94 C ATOM 708 CE2 PHE A 88 21.499 17.836 28.187 1.00 17.31 C ATOM 709 CZ PHE A 88 21.734 19.201 28.233 1.00 15.96 C ATOM 710 N TYR A 89 24.867 18.672 23.926 1.00 14.86 N ATOM 711 CA TYR A 89 24.662 20.032 23.456 1.00 15.98 C ATOM 712 C TYR A 89 24.181 20.103 22.005 1.00 16.95 C ATOM 713 O TYR A 89 23.462 21.029 21.626 1.00 17.55 O ATOM 714 CB TYR A 89 25.951 20.838 23.641 1.00 16.61 C ATOM 715 CG TYR A 89 25.754 22.317 23.450 1.00 17.06 C ATOM 716 CD1 TYR A 89 24.919 23.050 24.297 1.00 18.48 C ATOM 717 CD2 TYR A 89 26.358 22.977 22.384 1.00 19.23 C ATOM 718 CE1 TYR A 89 24.689 24.412 24.078 1.00 20.29 C ATOM 719 CE2 TYR A 89 26.137 24.332 22.154 1.00 20.60 C ATOM 720 CZ TYR A 89 25.304 25.044 23.001 1.00 21.41 C ATOM 721 OH TYR A 89 25.086 26.382 22.757 1.00 22.40 O ATOM 722 N SER A 90 24.576 19.132 21.192 1.00 16.01 N ATOM 723 CA SER A 90 24.133 19.106 19.808 1.00 15.27 C ATOM 724 C SER A 90 22.616 18.959 19.803 1.00 15.29 C ATOM 725 O SER A 90 21.914 19.635 19.054 1.00 15.27 O ATOM 726 CB SER A 90 24.774 17.936 19.077 1.00 15.12 C ATOM 727 OG SER A 90 26.100 18.258 18.697 1.00 18.08 O ATOM 728 N LEU A 91 22.106 18.068 20.646 1.00 15.27 N ATOM 729 CA LEU A 91 20.669 17.874 20.729 1.00 16.81 C ATOM 730 C LEU A 91 20.016 19.061 21.444 1.00 17.84 C ATOM 731 O LEU A 91 18.879 19.423 21.130 1.00 18.51 O ATOM 732 CB LEU A 91 20.336 16.573 21.465 1.00 18.07 C ATOM 733 CG LEU A 91 18.851 16.182 21.463 1.00 20.42 C ATOM 734 CD1 LEU A 91 18.328 16.081 20.036 1.00 21.48 C ATOM 735 CD2 LEU A 91 18.680 14.856 22.178 1.00 20.89 C ATOM 736 N TYR A 92 20.722 19.661 22.404 1.00 17.94 N ATOM 737 CA TYR A 92 20.176 20.817 23.123 1.00 17.54 C ATOM 738 C TYR A 92 19.768 21.920 22.141 1.00 17.35 C ATOM 739 O TYR A 92 18.684 22.502 22.257 1.00 17.08 O ATOM 740 CB TYR A 92 21.197 21.396 24.110 1.00 17.81 C ATOM 741 CG TYR A 92 20.662 22.619 24.821 1.00 19.07 C ATOM 742 CD1 TYR A 92 19.800 22.488 25.912 1.00 21.71 C ATOM 743 CD2 TYR A 92 20.931 23.904 24.347 1.00 19.81 C ATOM 744 CE1 TYR A 92 19.206 23.602 26.515 1.00 22.38 C ATOM 745 CE2 TYR A 92 20.342 25.033 24.939 1.00 21.82 C ATOM 746 CZ TYR A 92 19.475 24.871 26.023 1.00 24.08 C ATOM 747 OH TYR A 92 18.863 25.968 26.609 1.00 25.77 O ATOM 748 N LEU A 93 20.642 22.186 21.169 1.00 16.50 N ATOM 749 CA LEU A 93 20.407 23.221 20.165 1.00 16.79 C ATOM 750 C LEU A 93 19.116 23.041 19.365 1.00 16.74 C ATOM 751 O LEU A 93 18.579 24.009 18.837 1.00 17.80 O ATOM 752 CB LEU A 93 21.606 23.301 19.216 1.00 15.70 C ATOM 753 CG LEU A 93 22.898 23.773 19.892 1.00 15.87 C ATOM 754 CD1 LEU A 93 24.094 23.472 19.002 1.00 16.56 C ATOM 755 CD2 LEU A 93 22.805 25.265 20.182 1.00 15.97 C ATOM 756 N VAL A 94 18.612 21.814 19.278 1.00 16.06 N ATOM 757 CA VAL A 94 17.373 21.562 18.542 1.00 16.61 C ATOM 758 C VAL A 94 16.364 20.807 19.403 1.00 16.50 C ATOM 759 O VAL A 94 15.486 20.114 18.887 1.00 16.31 O ATOM 760 CB VAL A 94 17.643 20.741 17.245 1.00 16.27 C ATOM 761 CG1 VAL A 94 18.423 21.585 16.251 1.00 16.00 C ATOM 762 CG2 VAL A 94 18.416 19.467 17.576 1.00 15.96 C ATOM 763 N LYS A 95 16.472 20.971 20.719 1.00 17.34 N ATOM 764 CA LYS A 95 15.593 20.266 21.639 1.00 16.63 C ATOM 765 C LYS A 95 14.110 20.394 21.338 1.00 17.24 C ATOM 766 O LYS A 95 13.360 19.431 21.498 1.00 17.34 O ATOM 767 CB LYS A 95 15.868 20.702 23.083 1.00 17.37 C ATOM 768 CG LYS A 95 15.499 22.141 23.411 1.00 17.59 C ATOM 769 CD LYS A 95 16.153 22.557 24.724 1.00 18.43 C ATOM 770 CE LYS A 95 15.793 23.982 25.106 1.00 17.96 C ATOM 771 NZ LYS A 95 14.499 24.031 25.825 1.00 19.38 N ATOM 772 N GLU A 96 13.676 21.563 20.891 1.00 18.25 N ATOM 773 CA GLU A 96 12.258 21.740 20.609 1.00 20.42 C ATOM 774 C GLU A 96 11.812 21.023 19.331 1.00 20.26 C ATOM 775 O GLU A 96 10.628 20.996 19.006 1.00 22.04 O ATOM 776 CB GLU A 96 11.920 23.233 20.542 1.00 23.26 C ATOM 777 CG GLU A 96 12.375 24.037 21.783 1.00 30.07 C ATOM 778 CD GLU A 96 11.838 23.490 23.118 1.00 33.17 C ATOM 779 OE1 GLU A 96 10.746 22.883 23.136 1.00 34.55 O ATOM 780 OE2 GLU A 96 12.509 23.670 24.158 1.00 34.79 O ATOM 781 N GLU A 97 12.761 20.426 18.619 1.00 20.04 N ATOM 782 CA GLU A 97 12.461 19.702 17.386 1.00 20.14 C ATOM 783 C GLU A 97 12.445 18.195 17.625 1.00 20.15 C ATOM 784 O GLU A 97 12.167 17.419 16.714 1.00 19.96 O ATOM 785 CB GLU A 97 13.519 20.017 16.330 1.00 21.22 C ATOM 786 CG GLU A 97 13.700 21.494 16.062 1.00 25.92 C ATOM 787 CD GLU A 97 12.766 22.001 14.980 1.00 29.27 C ATOM 788 OE1 GLU A 97 11.954 21.203 14.463 1.00 31.02 O ATOM 789 OE2 GLU A 97 12.847 23.200 14.640 1.00 33.52 O ATOM 790 N LEU A 98 12.744 17.783 18.851 1.00 19.82 N ATOM 791 CA LEU A 98 12.803 16.365 19.176 1.00 19.59 C ATOM 792 C LEU A 98 11.519 15.569 18.952 1.00 19.70 C ATOM 793 O LEU A 98 11.571 14.422 18.494 1.00 20.48 O ATOM 794 CB LEU A 98 13.274 16.180 20.620 1.00 18.76 C ATOM 795 CG LEU A 98 13.658 14.749 21.016 1.00 18.30 C ATOM 796 CD1 LEU A 98 14.702 14.182 20.057 1.00 17.53 C ATOM 797 CD2 LEU A 98 14.196 14.767 22.434 1.00 17.07 C ATOM 798 N ALA A 99 10.376 16.167 19.272 1.00 20.19 N ATOM 799 CA ALA A 99 9.086 15.493 19.122 1.00 20.06 C ATOM 800 C ALA A 99 8.845 14.909 17.733 1.00 19.70 C ATOM 801 O ALA A 99 8.901 15.622 16.731 1.00 19.70 O ATOM 802 CB ALA A 99 7.956 16.449 19.482 1.00 21.87 C ATOM 803 N ASN A 100 8.564 13.607 17.695 1.00 19.24 N ATOM 804 CA ASN A 100 8.300 12.891 16.453 1.00 19.93 C ATOM 805 C ASN A 100 9.465 12.977 15.488 1.00 19.80 C ATOM 806 O ASN A 100 9.285 13.102 14.274 1.00 20.25 O ATOM 807 CB ASN A 100 7.039 13.440 15.802 1.00 21.74 C ATOM 808 CG ASN A 100 5.802 13.123 16.606 1.00 24.06 C ATOM 809 OD1 ASN A 100 5.617 11.989 17.051 1.00 25.06 O ATOM 810 ND2 ASN A 100 4.953 14.122 16.810 1.00 25.96 N ATOM 811 N SER A 101 10.669 12.887 16.037 1.00 19.06 N ATOM 812 CA SER A 101 11.869 12.972 15.231 1.00 18.44 C ATOM 813 C SER A 101 12.817 11.790 15.397 1.00 16.93 C ATOM 814 O SER A 101 12.893 11.169 16.462 1.00 16.65 O ATOM 815 CB SER A 101 12.609 14.265 15.573 1.00 19.80 C ATOM 816 OG SER A 101 13.890 14.299 14.972 1.00 23.68 O ATOM 817 N TYR A 102 13.521 11.470 14.316 1.00 16.25 N ATOM 818 CA TYR A 102 14.525 10.416 14.335 1.00 14.97 C ATOM 819 C TYR A 102 15.800 11.150 14.728 1.00 15.46 C ATOM 820 O TYR A 102 15.956 12.331 14.410 1.00 16.04 O ATOM 821 CB TYR A 102 14.749 9.828 12.935 1.00 14.93 C ATOM 822 CG TYR A 102 13.758 8.772 12.529 1.00 13.35 C ATOM 823 CD1 TYR A 102 13.977 7.425 12.829 1.00 13.00 C ATOM 824 CD2 TYR A 102 12.582 9.120 11.867 1.00 13.15 C ATOM 825 CE1 TYR A 102 13.037 6.453 12.478 1.00 13.70 C ATOM 826 CE2 TYR A 102 11.640 8.157 11.514 1.00 13.13 C ATOM 827 CZ TYR A 102 11.872 6.830 11.824 1.00 13.63 C ATOM 828 OH TYR A 102 10.925 5.896 11.491 1.00 15.59 O ATOM 829 N VAL A 103 16.695 10.469 15.431 1.00 14.04 N ATOM 830 CA VAL A 103 17.983 11.043 15.794 1.00 13.53 C ATOM 831 C VAL A 103 18.927 10.036 15.160 1.00 13.84 C ATOM 832 O VAL A 103 18.856 8.845 15.460 1.00 13.71 O ATOM 833 CB VAL A 103 18.201 11.106 17.328 1.00 14.06 C ATOM 834 CG1 VAL A 103 19.631 11.560 17.634 1.00 11.41 C ATOM 835 CG2 VAL A 103 17.197 12.075 17.949 1.00 12.66 C ATOM 836 N ILE A 104 19.808 10.512 14.292 1.00 13.42 N ATOM 837 CA ILE A 104 20.715 9.638 13.569 1.00 12.76 C ATOM 838 C ILE A 104 22.180 10.025 13.679 1.00 13.98 C ATOM 839 O ILE A 104 22.529 11.194 13.529 1.00 13.64 O ATOM 840 CB ILE A 104 20.324 9.630 12.077 1.00 13.51 C ATOM 841 CG1 ILE A 104 18.874 9.167 11.944 1.00 14.19 C ATOM 842 CG2 ILE A 104 21.280 8.756 11.270 1.00 13.69 C ATOM 843 CD1 ILE A 104 18.102 9.888 10.864 1.00 16.48 C ATOM 844 N ASP A 105 23.033 9.040 13.941 1.00 14.25 N ATOM 845 CA ASP A 105 24.469 9.284 14.021 1.00 17.16 C ATOM 846 C ASP A 105 24.938 9.294 12.572 1.00 18.30 C ATOM 847 O ASP A 105 24.548 8.430 11.789 1.00 17.20 O ATOM 848 CB ASP A 105 25.180 8.157 14.771 1.00 19.75 C ATOM 849 CG ASP A 105 24.961 8.213 16.277 1.00 22.18 C ATOM 850 OD1 ASP A 105 24.420 9.218 16.791 1.00 23.05 O ATOM 851 OD2 ASP A 105 25.342 7.230 16.950 1.00 25.37 O ATOM 852 N ALA A 106 25.781 10.261 12.220 1.00 19.99 N ATOM 853 CA ALA A 106 26.259 10.385 10.849 1.00 20.90 C ATOM 854 C ALA A 106 27.407 9.466 10.442 1.00 22.10 C ATOM 855 O ALA A 106 27.757 9.417 9.262 1.00 24.65 O ATOM 856 CB ALA A 106 26.643 11.840 10.570 1.00 22.20 C ATOM 857 N ASP A 107 27.995 8.738 11.388 1.00 21.59 N ATOM 858 CA ASP A 107 29.109 7.853 11.050 1.00 22.86 C ATOM 859 C ASP A 107 28.747 6.376 10.892 1.00 22.19 C ATOM 860 O ASP A 107 29.551 5.490 11.194 1.00 24.09 O ATOM 861 CB ASP A 107 30.229 7.990 12.079 1.00 25.28 C ATOM 862 CG ASP A 107 29.720 7.944 13.499 1.00 28.13 C ATOM 863 OD1 ASP A 107 28.591 7.457 13.722 1.00 29.34 O ATOM 864 OD2 ASP A 107 30.460 8.400 14.394 1.00 30.33 O ATOM 865 N ASN A 108 27.537 6.115 10.418 1.00 19.85 N ATOM 866 CA ASN A 108 27.082 4.754 10.196 1.00 18.32 C ATOM 867 C ASN A 108 26.637 4.618 8.752 1.00 17.71 C ATOM 868 O ASN A 108 26.116 5.566 8.163 1.00 19.03 O ATOM 869 CB ASN A 108 25.889 4.428 11.094 1.00 18.87 C ATOM 870 CG ASN A 108 26.289 4.199 12.535 1.00 20.93 C ATOM 871 OD1 ASN A 108 27.409 3.776 12.819 1.00 23.95 O ATOM 872 ND2 ASN A 108 25.376 4.485 13.456 1.00 20.60 N ATOM 873 N TYR A 109 26.853 3.446 8.178 1.00 16.78 N ATOM 874 CA TYR A 109 26.402 3.187 6.825 1.00 16.64 C ATOM 875 C TYR A 109 25.185 2.276 6.986 1.00 17.64 C ATOM 876 O TYR A 109 25.274 1.214 7.611 1.00 17.22 O ATOM 877 CB TYR A 109 27.479 2.475 6.010 1.00 14.57 C ATOM 878 CG TYR A 109 27.021 2.145 4.608 1.00 16.55 C ATOM 879 CD1 TYR A 109 26.499 0.886 4.299 1.00 16.49 C ATOM 880 CD2 TYR A 109 27.085 3.101 3.594 1.00 16.73 C ATOM 881 CE1 TYR A 109 26.052 0.588 3.015 1.00 16.29 C ATOM 882 CE2 TYR A 109 26.641 2.815 2.308 1.00 17.24 C ATOM 883 CZ TYR A 109 26.127 1.558 2.026 1.00 17.90 C ATOM 884 OH TYR A 109 25.704 1.272 0.750 1.00 19.09 O ATOM 885 N LEU A 110 24.051 2.688 6.434 1.00 17.82 N ATOM 886 CA LEU A 110 22.829 1.899 6.546 1.00 17.85 C ATOM 887 C LEU A 110 22.617 0.988 5.341 1.00 18.91 C ATOM 888 O LEU A 110 22.382 1.466 4.230 1.00 19.58 O ATOM 889 CB LEU A 110 21.622 2.833 6.716 1.00 17.70 C ATOM 890 CG LEU A 110 21.806 3.950 7.752 1.00 17.38 C ATOM 891 CD1 LEU A 110 20.644 4.908 7.700 1.00 17.70 C ATOM 892 CD2 LEU A 110 21.932 3.346 9.134 1.00 17.78 C ATOM 893 N PHE A 111 22.705 -0.321 5.560 1.00 19.37 N ATOM 894 CA PHE A 111 22.505 -1.283 4.480 1.00 20.20 C ATOM 895 C PHE A 111 21.026 -1.458 4.146 1.00 21.45 C ATOM 896 O PHE A 111 20.678 -1.885 3.050 1.00 23.83 O ATOM 897 CB PHE A 111 23.105 -2.639 4.855 1.00 18.93 C ATOM 898 CG PHE A 111 24.565 -2.760 4.538 1.00 18.57 C ATOM 899 CD1 PHE A 111 24.986 -3.127 3.261 1.00 18.90 C ATOM 900 CD2 PHE A 111 25.524 -2.487 5.509 1.00 18.78 C ATOM 901 CE1 PHE A 111 26.345 -3.219 2.957 1.00 19.09 C ATOM 902 CE2 PHE A 111 26.879 -2.576 5.215 1.00 18.89 C ATOM 903 CZ PHE A 111 27.291 -2.943 3.936 1.00 18.83 C ATOM 904 N LYS A 112 20.154 -1.126 5.092 1.00 21.80 N ATOM 905 CA LYS A 112 18.722 -1.263 4.880 1.00 22.14 C ATOM 906 C LYS A 112 17.983 -0.008 5.319 1.00 21.12 C ATOM 907 O LYS A 112 18.410 0.654 6.270 1.00 20.32 O ATOM 908 CB LYS A 112 18.197 -2.469 5.664 1.00 26.24 C ATOM 909 CG LYS A 112 18.714 -3.811 5.159 1.00 31.61 C ATOM 910 CD LYS A 112 17.573 -4.764 4.831 1.00 36.43 C ATOM 911 CE LYS A 112 17.146 -5.557 6.057 1.00 39.80 C ATOM 912 NZ LYS A 112 15.923 -6.380 5.805 1.00 42.51 N ATOM 913 N ASN A 113 16.889 0.315 4.619 1.00 18.90 N ATOM 914 CA ASN A 113 16.066 1.480 4.952 1.00 18.23 C ATOM 915 C ASN A 113 14.935 1.143 5.927 1.00 17.16 C ATOM 916 O ASN A 113 13.839 0.710 5.606 1.00 17.73 O ATOM 917 CB ASN A 113 15.483 2.158 3.723 1.00 16.25 C ATOM 918 CG ASN A 113 14.925 3.535 4.050 1.00 17.33 C ATOM 919 OD1 ASN A 113 14.889 3.942 5.218 1.00 15.69 O ATOM 920 ND2 ASN A 113 14.490 4.258 3.025 1.00 16.26 N HETATM 921 N MSE A 114 15.320 1.427 7.137 1.00 18.17 N HETATM 922 CA MSE A 114 14.745 1.313 8.457 1.00 19.18 C HETATM 923 C MSE A 114 13.661 2.351 8.744 1.00 18.58 C HETATM 924 O MSE A 114 12.759 2.133 9.559 1.00 17.57 O HETATM 925 CB MSE A 114 15.963 1.707 9.111 1.00 26.55 C HETATM 926 CG MSE A 114 16.228 2.045 10.404 1.00 26.01 C HETATM 927 SE MSE A 114 17.833 2.388 9.699 1.00 32.25 SE HETATM 928 CE MSE A 114 18.645 0.518 9.942 1.00 28.10 C ATOM 929 N PHE A 115 13.834 3.516 8.129 1.00 16.69 N ATOM 930 CA PHE A 115 12.957 4.648 8.350 1.00 15.51 C ATOM 931 C PHE A 115 11.533 4.500 7.868 1.00 16.07 C ATOM 932 O PHE A 115 11.280 3.982 6.782 1.00 16.11 O ATOM 933 CB PHE A 115 13.585 5.899 7.732 1.00 14.14 C ATOM 934 CG PHE A 115 14.984 6.158 8.205 1.00 14.56 C ATOM 935 CD1 PHE A 115 15.242 6.402 9.558 1.00 15.26 C ATOM 936 CD2 PHE A 115 16.053 6.133 7.312 1.00 14.15 C ATOM 937 CE1 PHE A 115 16.548 6.615 10.013 1.00 15.41 C ATOM 938 CE2 PHE A 115 17.366 6.344 7.754 1.00 15.32 C ATOM 939 CZ PHE A 115 17.613 6.586 9.109 1.00 15.61 C ATOM 940 N ARG A 116 10.602 4.950 8.699 1.00 17.42 N ATOM 941 CA ARG A 116 9.187 4.930 8.348 1.00 19.82 C ATOM 942 C ARG A 116 8.512 6.153 8.946 1.00 19.47 C ATOM 943 O ARG A 116 8.948 6.675 9.978 1.00 17.49 O ATOM 944 CB ARG A 116 8.478 3.663 8.841 1.00 22.18 C ATOM 945 CG ARG A 116 9.243 2.799 9.811 1.00 28.38 C ATOM 946 CD ARG A 116 8.653 1.392 9.854 1.00 30.13 C ATOM 947 NE ARG A 116 7.256 1.365 9.419 1.00 35.85 N ATOM 948 CZ ARG A 116 6.779 0.578 8.452 1.00 37.11 C ATOM 949 NH1 ARG A 116 7.586 -0.256 7.806 1.00 37.35 N ATOM 950 NH2 ARG A 116 5.491 0.630 8.122 1.00 37.44 N ATOM 951 N ASN A 117 7.446 6.613 8.293 1.00 19.73 N ATOM 952 CA ASN A 117 6.728 7.783 8.781 1.00 21.73 C ATOM 953 C ASN A 117 5.450 7.437 9.553 1.00 21.01 C ATOM 954 O ASN A 117 4.612 8.305 9.789 1.00 21.58 O ATOM 955 CB ASN A 117 6.419 8.745 7.616 1.00 21.57 C ATOM 956 CG ASN A 117 5.407 8.180 6.619 1.00 22.20 C ATOM 957 OD1 ASN A 117 5.021 7.014 6.682 1.00 23.01 O ATOM 958 ND2 ASN A 117 4.974 9.025 5.689 1.00 23.21 N ATOM 959 N ASP A 118 5.321 6.182 9.975 1.00 20.72 N ATOM 960 CA ASP A 118 4.134 5.758 10.707 1.00 21.88 C ATOM 961 C ASP A 118 4.413 5.206 12.113 1.00 22.22 C ATOM 962 O ASP A 118 3.557 4.554 12.711 1.00 21.55 O ATOM 963 CB ASP A 118 3.379 4.720 9.884 1.00 21.53 C ATOM 964 CG ASP A 118 4.213 3.495 9.606 1.00 23.71 C ATOM 965 OD1 ASP A 118 5.408 3.488 9.981 1.00 23.78 O ATOM 966 OD2 ASP A 118 3.672 2.538 9.017 1.00 24.85 O ATOM 967 N LEU A 119 5.606 5.469 12.639 1.00 23.94 N ATOM 968 CA LEU A 119 5.968 5.007 13.978 1.00 25.03 C ATOM 969 C LEU A 119 5.123 5.760 14.996 1.00 26.23 C ATOM 970 O LEU A 119 4.954 6.975 14.881 1.00 27.36 O ATOM 971 CB LEU A 119 7.443 5.279 14.252 1.00 26.00 C ATOM 972 CG LEU A 119 8.343 4.060 14.415 1.00 28.46 C ATOM 973 CD1 LEU A 119 8.213 3.152 13.202 1.00 29.43 C ATOM 974 CD2 LEU A 119 9.779 4.526 14.586 1.00 29.06 C ATOM 975 N THR A 120 4.602 5.049 15.993 1.00 25.87 N ATOM 976 CA THR A 120 3.757 5.679 17.003 1.00 25.61 C ATOM 977 C THR A 120 4.330 5.661 18.413 1.00 23.87 C ATOM 978 O THR A 120 3.658 6.068 19.362 1.00 25.59 O ATOM 979 CB THR A 120 2.362 5.026 17.049 1.00 26.26 C ATOM 980 OG1 THR A 120 2.498 3.626 17.313 1.00 29.35 O ATOM 981 CG2 THR A 120 1.641 5.223 15.725 1.00 27.79 C ATOM 982 N ARG A 121 5.561 5.194 18.560 1.00 21.14 N ATOM 983 CA ARG A 121 6.176 5.150 19.876 1.00 18.63 C ATOM 984 C ARG A 121 7.680 5.291 19.760 1.00 17.16 C ATOM 985 O ARG A 121 8.262 4.957 18.726 1.00 16.09 O ATOM 986 CB ARG A 121 5.826 3.840 20.587 1.00 19.14 C ATOM 987 CG ARG A 121 6.538 2.632 20.031 1.00 19.47 C ATOM 988 CD ARG A 121 5.763 1.362 20.334 1.00 22.34 C ATOM 989 NE ARG A 121 6.573 0.167 20.109 1.00 24.25 N ATOM 990 CZ ARG A 121 6.272 -1.037 20.586 1.00 25.41 C ATOM 991 NH1 ARG A 121 5.181 -1.208 21.316 1.00 25.52 N ATOM 992 NH2 ARG A 121 7.067 -2.068 20.340 1.00 27.10 N ATOM 993 N SER A 122 8.303 5.799 20.823 1.00 17.25 N ATOM 994 CA SER A 122 9.750 5.990 20.853 1.00 16.57 C ATOM 995 C SER A 122 10.410 4.635 20.628 1.00 17.00 C ATOM 996 O SER A 122 10.048 3.640 21.273 1.00 16.04 O ATOM 997 CB SER A 122 10.173 6.592 22.192 1.00 16.91 C ATOM 998 OG SER A 122 9.528 7.837 22.384 1.00 17.64 O ATOM 999 N THR A 123 11.383 4.605 19.722 1.00 15.08 N ATOM 1000 CA THR A 123 12.043 3.359 19.362 1.00 15.47 C ATOM 1001 C THR A 123 13.549 3.458 19.174 1.00 15.76 C ATOM 1002 O THR A 123 14.065 4.457 18.662 1.00 15.28 O ATOM 1003 CB THR A 123 11.464 2.815 18.028 1.00 15.29 C ATOM 1004 OG1 THR A 123 10.048 2.662 18.145 1.00 17.70 O ATOM 1005 CG2 THR A 123 12.091 1.485 17.660 1.00 15.55 C ATOM 1006 N TYR A 124 14.243 2.407 19.594 1.00 14.41 N ATOM 1007 CA TYR A 124 15.676 2.304 19.405 1.00 14.02 C ATOM 1008 C TYR A 124 15.812 1.201 18.365 1.00 15.08 C ATOM 1009 O TYR A 124 15.330 0.089 18.593 1.00 15.71 O ATOM 1010 CB TYR A 124 16.377 1.833 20.679 1.00 14.68 C ATOM 1011 CG TYR A 124 16.817 2.934 21.604 1.00 13.89 C ATOM 1012 CD1 TYR A 124 17.767 3.866 21.211 1.00 13.40 C ATOM 1013 CD2 TYR A 124 16.278 3.042 22.882 1.00 15.55 C ATOM 1014 CE1 TYR A 124 18.172 4.883 22.069 1.00 14.45 C ATOM 1015 CE2 TYR A 124 16.675 4.053 23.748 1.00 15.20 C ATOM 1016 CZ TYR A 124 17.620 4.968 23.336 1.00 14.53 C ATOM 1017 OH TYR A 124 18.017 5.960 24.194 1.00 15.89 O ATOM 1018 N PHE A 125 16.424 1.498 17.221 1.00 14.08 N ATOM 1019 CA PHE A 125 16.642 0.471 16.206 1.00 13.16 C ATOM 1020 C PHE A 125 18.003 -0.087 16.593 1.00 14.02 C ATOM 1021 O PHE A 125 19.026 0.580 16.432 1.00 13.94 O ATOM 1022 CB PHE A 125 16.643 1.100 14.814 1.00 13.36 C ATOM 1023 CG PHE A 125 15.294 1.604 14.403 1.00 13.25 C ATOM 1024 CD1 PHE A 125 14.479 0.851 13.562 1.00 14.59 C ATOM 1025 CD2 PHE A 125 14.810 2.807 14.905 1.00 14.14 C ATOM 1026 CE1 PHE A 125 13.193 1.285 13.227 1.00 14.83 C ATOM 1027 CE2 PHE A 125 13.529 3.252 14.579 1.00 15.19 C ATOM 1028 CZ PHE A 125 12.717 2.486 13.738 1.00 15.47 C ATOM 1029 N SER A 126 17.997 -1.313 17.120 1.00 13.51 N ATOM 1030 CA SER A 126 19.202 -1.950 17.640 1.00 13.32 C ATOM 1031 C SER A 126 19.751 -3.208 16.967 1.00 13.76 C ATOM 1032 O SER A 126 19.010 -4.149 16.683 1.00 15.62 O ATOM 1033 CB SER A 126 18.971 -2.270 19.119 1.00 12.63 C ATOM 1034 OG SER A 126 20.086 -2.936 19.678 1.00 13.39 O ATOM 1035 N VAL A 127 21.061 -3.220 16.734 1.00 14.37 N ATOM 1036 CA VAL A 127 21.720 -4.380 16.153 1.00 16.09 C ATOM 1037 C VAL A 127 22.460 -5.073 17.300 1.00 17.26 C ATOM 1038 O VAL A 127 22.836 -4.429 18.288 1.00 16.25 O ATOM 1039 CB VAL A 127 22.768 -3.995 15.064 1.00 15.85 C ATOM 1040 CG1 VAL A 127 22.068 -3.466 13.812 1.00 14.89 C ATOM 1041 CG2 VAL A 127 23.745 -2.967 15.616 1.00 16.62 C ATOM 1042 N TYR A 128 22.662 -6.381 17.175 1.00 17.94 N ATOM 1043 CA TYR A 128 23.384 -7.135 18.192 1.00 19.28 C ATOM 1044 C TYR A 128 24.879 -7.087 17.868 1.00 20.48 C ATOM 1045 O TYR A 128 25.276 -7.228 16.707 1.00 20.90 O ATOM 1046 CB TYR A 128 22.898 -8.591 18.216 1.00 20.54 C ATOM 1047 CG TYR A 128 23.720 -9.509 19.101 1.00 21.43 C ATOM 1048 CD1 TYR A 128 23.430 -9.645 20.462 1.00 23.20 C ATOM 1049 CD2 TYR A 128 24.785 -10.242 18.579 1.00 22.53 C ATOM 1050 CE1 TYR A 128 24.187 -10.495 21.279 1.00 25.51 C ATOM 1051 CE2 TYR A 128 25.542 -11.090 19.383 1.00 22.88 C ATOM 1052 CZ TYR A 128 25.240 -11.213 20.729 1.00 24.21 C ATOM 1053 OH TYR A 128 25.989 -12.049 21.524 1.00 25.56 O ATOM 1054 N ARG A 129 25.707 -6.881 18.888 1.00 20.32 N ATOM 1055 CA ARG A 129 27.151 -6.823 18.696 1.00 21.20 C ATOM 1056 C ARG A 129 27.893 -7.582 19.790 1.00 23.27 C ATOM 1057 O ARG A 129 27.406 -7.707 20.916 1.00 22.58 O ATOM 1058 CB ARG A 129 27.637 -5.374 18.702 1.00 20.33 C ATOM 1059 CG ARG A 129 27.235 -4.574 17.490 1.00 21.99 C ATOM 1060 CD ARG A 129 27.748 -5.210 16.217 1.00 24.05 C ATOM 1061 NE ARG A 129 27.371 -4.430 15.038 1.00 24.17 N ATOM 1062 CZ ARG A 129 26.495 -4.829 14.117 1.00 26.11 C ATOM 1063 NH1 ARG A 129 25.892 -6.012 14.236 1.00 23.35 N ATOM 1064 NH2 ARG A 129 26.228 -4.048 13.068 1.00 22.84 N ATOM 1065 N GLU A 130 29.081 -8.076 19.444 1.00 25.43 N ATOM 1066 CA GLU A 130 29.941 -8.804 20.374 1.00 26.85 C ATOM 1067 C GLU A 130 31.305 -8.113 20.424 1.00 26.74 C ATOM 1068 O GLU A 130 31.592 -7.245 19.599 1.00 27.31 O ATOM 1069 CB GLU A 130 30.096 -10.253 19.918 1.00 26.71 C ATOM 1070 CG GLU A 130 28.800 -11.029 19.969 1.00 29.35 C ATOM 1071 CD GLU A 130 28.982 -12.503 19.677 1.00 30.27 C ATOM 1072 OE1 GLU A 130 28.139 -13.305 20.135 1.00 30.72 O ATOM 1073 OE2 GLU A 130 29.963 -12.858 18.991 1.00 31.23 O ATOM 1074 N ASP A 131 32.140 -8.490 21.386 1.00 28.11 N ATOM 1075 CA ASP A 131 33.463 -7.881 21.526 1.00 30.50 C ATOM 1076 C ASP A 131 33.296 -6.373 21.535 1.00 29.71 C ATOM 1077 O ASP A 131 34.076 -5.638 20.930 1.00 30.59 O ATOM 1078 CB ASP A 131 34.373 -8.281 20.362 1.00 35.00 C ATOM 1079 CG ASP A 131 34.428 -9.775 20.156 1.00 40.57 C ATOM 1080 OD1 ASP A 131 34.720 -10.498 21.136 1.00 44.85 O ATOM 1081 OD2 ASP A 131 34.175 -10.227 19.017 1.00 44.16 O ATOM 1082 N CYS A 132 32.266 -5.919 22.233 1.00 28.75 N ATOM 1083 CA CYS A 132 31.964 -4.503 22.320 1.00 28.38 C ATOM 1084 C CYS A 132 32.963 -3.714 23.133 1.00 29.65 C ATOM 1085 O CYS A 132 33.686 -4.256 23.965 1.00 29.41 O ATOM 1086 CB CYS A 132 30.578 -4.303 22.923 1.00 25.87 C ATOM 1087 SG CYS A 132 29.269 -4.624 21.774 1.00 24.15 S ATOM 1088 N THR A 133 32.979 -2.414 22.887 1.00 31.66 N ATOM 1089 CA THR A 133 33.865 -1.521 23.599 1.00 34.17 C ATOM 1090 C THR A 133 33.168 -0.184 23.752 1.00 34.09 C ATOM 1091 O THR A 133 32.847 0.477 22.766 1.00 35.76 O ATOM 1092 CB THR A 133 35.182 -1.325 22.833 1.00 35.98 C ATOM 1093 OG1 THR A 133 36.110 -2.346 23.221 1.00 38.20 O ATOM 1094 CG2 THR A 133 35.782 0.044 23.132 1.00 37.40 C ATOM 1095 N ASN A 134 32.912 0.199 24.995 1.00 33.73 N ATOM 1096 CA ASN A 134 32.269 1.472 25.276 1.00 34.22 C ATOM 1097 C ASN A 134 30.865 1.653 24.702 1.00 31.40 C ATOM 1098 O ASN A 134 30.404 2.781 24.551 1.00 32.73 O ATOM 1099 CB ASN A 134 33.158 2.613 24.785 1.00 38.41 C ATOM 1100 CG ASN A 134 34.478 2.670 25.522 1.00 43.54 C ATOM 1101 OD1 ASN A 134 35.522 2.962 24.931 1.00 47.27 O ATOM 1102 ND2 ASN A 134 34.443 2.389 26.824 1.00 44.00 N ATOM 1103 N GLU A 135 30.184 0.563 24.376 1.00 27.33 N ATOM 1104 CA GLU A 135 28.829 0.675 23.849 1.00 23.35 C ATOM 1105 C GLU A 135 27.859 0.677 25.016 1.00 20.89 C ATOM 1106 O GLU A 135 28.240 0.352 26.139 1.00 20.69 O ATOM 1107 CB GLU A 135 28.497 -0.514 22.945 1.00 25.60 C ATOM 1108 CG GLU A 135 29.585 -0.870 21.967 1.00 27.63 C ATOM 1109 CD GLU A 135 29.600 0.057 20.784 1.00 31.04 C ATOM 1110 OE1 GLU A 135 30.585 0.022 20.014 1.00 32.67 O ATOM 1111 OE2 GLU A 135 28.626 0.825 20.624 1.00 32.37 O ATOM 1112 N TRP A 136 26.614 1.055 24.753 1.00 17.94 N ATOM 1113 CA TRP A 136 25.578 1.041 25.780 1.00 17.13 C ATOM 1114 C TRP A 136 24.575 -0.007 25.316 1.00 16.92 C ATOM 1115 O TRP A 136 24.310 -0.133 24.121 1.00 16.31 O ATOM 1116 CB TRP A 136 24.897 2.402 25.913 1.00 17.04 C ATOM 1117 CG TRP A 136 25.717 3.432 26.643 1.00 17.76 C ATOM 1118 CD1 TRP A 136 27.037 3.336 27.009 1.00 17.97 C ATOM 1119 CD2 TRP A 136 25.284 4.734 27.063 1.00 17.09 C ATOM 1120 NE1 TRP A 136 27.448 4.497 27.619 1.00 17.44 N ATOM 1121 CE2 TRP A 136 26.390 5.371 27.667 1.00 18.28 C ATOM 1122 CE3 TRP A 136 24.065 5.422 26.979 1.00 18.03 C ATOM 1123 CZ2 TRP A 136 26.315 6.673 28.189 1.00 18.86 C ATOM 1124 CZ3 TRP A 136 23.991 6.716 27.503 1.00 18.82 C ATOM 1125 CH2 TRP A 136 25.111 7.325 28.099 1.00 18.44 C ATOM 1126 N PHE A 137 24.017 -0.757 26.256 1.00 16.46 N ATOM 1127 CA PHE A 137 23.088 -1.821 25.905 1.00 15.75 C ATOM 1128 C PHE A 137 21.664 -1.631 26.387 1.00 15.54 C ATOM 1129 O PHE A 137 21.407 -0.951 27.385 1.00 15.72 O ATOM 1130 CB PHE A 137 23.633 -3.151 26.417 1.00 14.59 C ATOM 1131 CG PHE A 137 25.042 -3.419 25.996 1.00 14.41 C ATOM 1132 CD1 PHE A 137 25.311 -4.228 24.893 1.00 14.53 C ATOM 1133 CD2 PHE A 137 26.103 -2.837 26.676 1.00 13.21 C ATOM 1134 CE1 PHE A 137 26.624 -4.452 24.471 1.00 14.96 C ATOM 1135 CE2 PHE A 137 27.416 -3.051 26.266 1.00 14.98 C ATOM 1136 CZ PHE A 137 27.678 -3.864 25.155 1.00 15.16 C ATOM 1137 N LEU A 138 20.743 -2.260 25.665 1.00 15.01 N ATOM 1138 CA LEU A 138 19.321 -2.184 25.961 1.00 14.46 C ATOM 1139 C LEU A 138 18.826 -3.389 26.758 1.00 15.36 C ATOM 1140 O LEU A 138 19.017 -4.533 26.348 1.00 14.80 O ATOM 1141 CB LEU A 138 18.535 -2.080 24.647 1.00 14.58 C ATOM 1142 CG LEU A 138 18.822 -0.833 23.800 1.00 13.98 C ATOM 1143 CD1 LEU A 138 18.483 -1.106 22.340 1.00 13.03 C ATOM 1144 CD2 LEU A 138 18.001 0.341 24.330 1.00 13.40 C ATOM 1145 N VAL A 139 18.186 -3.124 27.891 1.00 15.24 N ATOM 1146 CA VAL A 139 17.643 -4.189 28.730 1.00 16.15 C ATOM 1147 C VAL A 139 16.139 -4.248 28.485 1.00 15.50 C ATOM 1148 O VAL A 139 15.430 -3.275 28.741 1.00 16.92 O ATOM 1149 CB VAL A 139 17.895 -3.905 30.228 1.00 15.01 C ATOM 1150 CG1 VAL A 139 17.147 -4.923 31.085 1.00 14.70 C ATOM 1151 CG2 VAL A 139 19.390 -3.941 30.517 1.00 16.82 C ATOM 1152 N TYR A 140 15.644 -5.378 27.993 1.00 15.71 N ATOM 1153 CA TYR A 140 14.216 -5.490 27.720 1.00 16.48 C ATOM 1154 C TYR A 140 13.667 -6.914 27.753 1.00 17.47 C ATOM 1155 O TYR A 140 14.419 -7.889 27.677 1.00 17.50 O ATOM 1156 CB TYR A 140 13.895 -4.854 26.361 1.00 16.04 C ATOM 1157 CG TYR A 140 14.615 -5.493 25.193 1.00 15.90 C ATOM 1158 CD1 TYR A 140 13.972 -6.424 24.373 1.00 16.68 C ATOM 1159 CD2 TYR A 140 15.930 -5.143 24.885 1.00 15.37 C ATOM 1160 CE1 TYR A 140 14.621 -6.992 23.266 1.00 15.86 C ATOM 1161 CE2 TYR A 140 16.589 -5.703 23.782 1.00 17.01 C ATOM 1162 CZ TYR A 140 15.924 -6.626 22.976 1.00 16.57 C ATOM 1163 OH TYR A 140 16.559 -7.169 21.880 1.00 16.73 O ATOM 1164 N GLY A 141 12.342 -7.008 27.852 1.00 19.12 N ATOM 1165 CA GLY A 141 11.675 -8.294 27.901 1.00 20.54 C ATOM 1166 C GLY A 141 10.832 -8.601 26.674 1.00 22.53 C ATOM 1167 O GLY A 141 11.116 -8.131 25.573 1.00 21.89 O ATOM 1168 N ASP A 142 9.772 -9.378 26.884 1.00 24.09 N ATOM 1169 CA ASP A 142 8.878 -9.816 25.815 1.00 25.62 C ATOM 1170 C ASP A 142 8.101 -8.732 25.087 1.00 24.90 C ATOM 1171 O ASP A 142 7.696 -8.925 23.940 1.00 24.57 O ATOM 1172 CB ASP A 142 7.886 -10.844 26.364 1.00 30.22 C ATOM 1173 CG ASP A 142 8.572 -12.022 27.031 1.00 34.72 C ATOM 1174 OD1 ASP A 142 7.996 -12.574 27.993 1.00 39.91 O ATOM 1175 OD2 ASP A 142 9.684 -12.398 26.599 1.00 35.53 O ATOM 1176 N ASP A 143 7.877 -7.604 25.750 1.00 23.23 N ATOM 1177 CA ASP A 143 7.133 -6.513 25.138 1.00 21.76 C ATOM 1178 C ASP A 143 8.066 -5.524 24.448 1.00 21.23 C ATOM 1179 O ASP A 143 7.623 -4.489 23.947 1.00 22.63 O ATOM 1180 CB ASP A 143 6.294 -5.787 26.191 1.00 21.79 C ATOM 1181 CG ASP A 143 7.137 -5.178 27.292 1.00 22.12 C ATOM 1182 OD1 ASP A 143 8.361 -5.436 27.341 1.00 23.08 O ATOM 1183 OD2 ASP A 143 6.567 -4.435 28.117 1.00 25.96 O ATOM 1184 N TYR A 144 9.356 -5.849 24.429 1.00 20.17 N ATOM 1185 CA TYR A 144 10.367 -5.001 23.805 1.00 19.63 C ATOM 1186 C TYR A 144 10.496 -3.606 24.421 1.00 19.28 C ATOM 1187 O TYR A 144 11.098 -2.710 23.829 1.00 17.57 O ATOM 1188 CB TYR A 144 10.091 -4.896 22.302 1.00 20.25 C ATOM 1189 CG TYR A 144 10.225 -6.232 21.618 1.00 20.03 C ATOM 1190 CD1 TYR A 144 9.096 -6.982 21.282 1.00 21.29 C ATOM 1191 CD2 TYR A 144 11.484 -6.790 21.379 1.00 19.36 C ATOM 1192 CE1 TYR A 144 9.215 -8.256 20.735 1.00 22.20 C ATOM 1193 CE2 TYR A 144 11.617 -8.064 20.833 1.00 21.34 C ATOM 1194 CZ TYR A 144 10.478 -8.791 20.517 1.00 22.65 C ATOM 1195 OH TYR A 144 10.605 -10.061 19.999 1.00 24.51 O ATOM 1196 N LYS A 145 9.943 -3.423 25.617 1.00 18.72 N ATOM 1197 CA LYS A 145 10.031 -2.134 26.291 1.00 18.28 C ATOM 1198 C LYS A 145 11.349 -2.027 27.056 1.00 17.85 C ATOM 1199 O LYS A 145 11.718 -2.929 27.810 1.00 17.63 O ATOM 1200 CB LYS A 145 8.854 -1.947 27.251 1.00 19.49 C ATOM 1201 CG LYS A 145 8.680 -0.509 27.719 1.00 21.42 C ATOM 1202 CD LYS A 145 7.421 -0.348 28.553 1.00 23.24 C ATOM 1203 CE LYS A 145 7.180 1.109 28.899 1.00 24.06 C ATOM 1204 NZ LYS A 145 8.016 1.540 30.050 1.00 26.36 N ATOM 1205 N VAL A 146 12.057 -0.921 26.855 1.00 16.52 N ATOM 1206 CA VAL A 146 13.336 -0.702 27.515 1.00 16.50 C ATOM 1207 C VAL A 146 13.161 -0.497 29.018 1.00 17.33 C ATOM 1208 O VAL A 146 12.499 0.449 29.462 1.00 17.29 O ATOM 1209 CB VAL A 146 14.068 0.521 26.922 1.00 15.97 C ATOM 1210 CG1 VAL A 146 15.405 0.716 27.623 1.00 14.45 C ATOM 1211 CG2 VAL A 146 14.279 0.317 25.418 1.00 15.01 C ATOM 1212 N GLN A 147 13.758 -1.399 29.791 1.00 17.58 N ATOM 1213 CA GLN A 147 13.682 -1.355 31.245 1.00 19.45 C ATOM 1214 C GLN A 147 14.871 -0.604 31.812 1.00 19.67 C ATOM 1215 O GLN A 147 14.788 -0.001 32.878 1.00 20.23 O ATOM 1216 CB GLN A 147 13.665 -2.777 31.810 1.00 19.87 C ATOM 1217 CG GLN A 147 12.396 -3.542 31.502 1.00 22.10 C ATOM 1218 CD GLN A 147 11.149 -2.775 31.891 1.00 24.06 C ATOM 1219 OE1 GLN A 147 11.158 -2.004 32.848 1.00 28.38 O ATOM 1220 NE2 GLN A 147 10.070 -2.977 31.149 1.00 25.75 N ATOM 1221 N ASP A 148 15.981 -0.647 31.087 1.00 18.74 N ATOM 1222 CA ASP A 148 17.196 0.019 31.515 1.00 18.78 C ATOM 1223 C ASP A 148 18.175 0.077 30.350 1.00 18.22 C ATOM 1224 O ASP A 148 18.001 -0.614 29.340 1.00 18.68 O ATOM 1225 CB ASP A 148 17.826 -0.770 32.666 1.00 19.74 C ATOM 1226 CG ASP A 148 18.694 0.091 33.560 1.00 21.49 C ATOM 1227 OD1 ASP A 148 18.877 1.291 33.259 1.00 21.65 O ATOM 1228 OD2 ASP A 148 19.196 -0.440 34.573 1.00 21.72 O ATOM 1229 N ILE A 149 19.191 0.919 30.488 1.00 16.92 N ATOM 1230 CA ILE A 149 20.241 1.034 29.489 1.00 16.35 C ATOM 1231 C ILE A 149 21.504 0.926 30.322 1.00 17.31 C ATOM 1232 O ILE A 149 21.705 1.694 31.261 1.00 19.64 O ATOM 1233 CB ILE A 149 20.196 2.383 28.742 1.00 15.23 C ATOM 1234 CG1 ILE A 149 18.998 2.400 27.784 1.00 14.24 C ATOM 1235 CG2 ILE A 149 21.496 2.590 27.968 1.00 13.89 C ATOM 1236 CD1 ILE A 149 18.562 3.787 27.354 1.00 14.75 C ATOM 1237 N ILE A 150 22.354 -0.031 29.988 1.00 17.04 N ATOM 1238 CA ILE A 150 23.555 -0.252 30.768 1.00 17.70 C ATOM 1239 C ILE A 150 24.827 -0.218 29.942 1.00 19.09 C ATOM 1240 O ILE A 150 24.782 -0.236 28.707 1.00 18.00 O ATOM 1241 CB ILE A 150 23.468 -1.612 31.482 1.00 18.11 C ATOM 1242 CG1 ILE A 150 23.373 -2.735 30.449 1.00 17.48 C ATOM 1243 CG2 ILE A 150 22.242 -1.650 32.371 1.00 17.53 C ATOM 1244 CD1 ILE A 150 23.531 -4.105 31.029 1.00 20.13 C ATOM 1245 N VAL A 151 25.963 -0.178 30.634 1.00 19.45 N ATOM 1246 CA VAL A 151 27.257 -0.151 29.973 1.00 20.96 C ATOM 1247 C VAL A 151 28.079 -1.404 30.285 1.00 21.67 C ATOM 1248 O VAL A 151 29.059 -1.694 29.599 1.00 21.44 O ATOM 1249 CB VAL A 151 28.075 1.088 30.400 1.00 20.93 C ATOM 1250 CG1 VAL A 151 27.170 2.308 30.485 1.00 21.01 C ATOM 1251 CG2 VAL A 151 28.749 0.829 31.735 1.00 20.36 C ATOM 1252 N ASP A 152 27.664 -2.150 31.305 1.00 22.34 N ATOM 1253 CA ASP A 152 28.388 -3.347 31.728 1.00 23.82 C ATOM 1254 C ASP A 152 28.195 -4.624 30.901 1.00 24.32 C ATOM 1255 O ASP A 152 27.566 -5.589 31.360 1.00 24.24 O ATOM 1256 CB ASP A 152 28.065 -3.654 33.196 1.00 25.98 C ATOM 1257 CG ASP A 152 29.084 -4.590 33.838 1.00 27.59 C ATOM 1258 OD1 ASP A 152 30.109 -4.909 33.198 1.00 27.15 O ATOM 1259 OD2 ASP A 152 28.854 -5.009 34.993 1.00 28.96 O ATOM 1260 N SER A 153 28.744 -4.634 29.692 1.00 22.54 N ATOM 1261 CA SER A 153 28.673 -5.812 28.842 1.00 21.64 C ATOM 1262 C SER A 153 29.591 -5.686 27.644 1.00 22.46 C ATOM 1263 O SER A 153 29.939 -4.582 27.228 1.00 22.71 O ATOM 1264 CB SER A 153 27.249 -6.068 28.359 1.00 19.94 C ATOM 1265 OG SER A 153 27.175 -7.352 27.756 1.00 20.89 O ATOM 1266 N LYS A 154 29.987 -6.833 27.100 1.00 23.20 N ATOM 1267 CA LYS A 154 30.852 -6.882 25.931 1.00 23.11 C ATOM 1268 C LYS A 154 30.054 -7.402 24.745 1.00 21.53 C ATOM 1269 O LYS A 154 30.573 -7.494 23.634 1.00 21.48 O ATOM 1270 CB LYS A 154 32.039 -7.805 26.188 1.00 26.13 C ATOM 1271 CG LYS A 154 32.810 -7.471 27.451 1.00 31.45 C ATOM 1272 CD LYS A 154 34.305 -7.545 27.219 1.00 36.81 C ATOM 1273 CE LYS A 154 35.062 -6.766 28.282 1.00 40.46 C ATOM 1274 NZ LYS A 154 36.541 -6.878 28.103 1.00 44.36 N ATOM 1275 N ALA A 155 28.788 -7.739 24.988 1.00 19.80 N ATOM 1276 CA ALA A 155 27.918 -8.259 23.940 1.00 18.91 C ATOM 1277 C ALA A 155 26.457 -7.977 24.246 1.00 18.55 C ATOM 1278 O ALA A 155 26.052 -7.950 25.407 1.00 18.44 O ATOM 1279 CB ALA A 155 28.129 -9.763 23.780 1.00 17.74 C ATOM 1280 N GLY A 156 25.666 -7.776 23.198 1.00 17.69 N ATOM 1281 CA GLY A 156 24.252 -7.511 23.381 1.00 16.62 C ATOM 1282 C GLY A 156 23.681 -6.548 22.354 1.00 16.87 C ATOM 1283 O GLY A 156 24.350 -6.193 21.382 1.00 16.63 O ATOM 1284 N ARG A 157 22.431 -6.144 22.575 1.00 15.42 N ATOM 1285 CA ARG A 157 21.733 -5.202 21.708 1.00 15.67 C ATOM 1286 C ARG A 157 22.159 -3.803 22.144 1.00 16.38 C ATOM 1287 O ARG A 157 21.841 -3.345 23.242 1.00 16.82 O ATOM 1288 CB ARG A 157 20.223 -5.373 21.857 1.00 14.42 C ATOM 1289 CG ARG A 157 19.691 -6.668 21.255 1.00 14.97 C ATOM 1290 CD ARG A 157 19.531 -6.519 19.759 1.00 17.27 C ATOM 1291 NE ARG A 157 19.213 -7.788 19.122 1.00 18.10 N ATOM 1292 CZ ARG A 157 18.911 -7.926 17.836 1.00 19.67 C ATOM 1293 NH1 ARG A 157 18.882 -6.869 17.032 1.00 16.20 N ATOM 1294 NH2 ARG A 157 18.628 -9.130 17.355 1.00 19.01 N ATOM 1295 N ILE A 158 22.886 -3.123 21.272 1.00 16.00 N ATOM 1296 CA ILE A 158 23.406 -1.802 21.593 1.00 15.42 C ATOM 1297 C ILE A 158 22.611 -0.634 21.027 1.00 14.76 C ATOM 1298 O ILE A 158 21.759 -0.801 20.153 1.00 13.92 O ATOM 1299 CB ILE A 158 24.869 -1.673 21.079 1.00 14.31 C ATOM 1300 CG1 ILE A 158 24.898 -1.832 19.551 1.00 14.48 C ATOM 1301 CG2 ILE A 158 25.742 -2.755 21.704 1.00 13.16 C ATOM 1302 CD1 ILE A 158 26.156 -1.326 18.894 1.00 15.35 C ATOM 1303 N LEU A 159 22.875 0.551 21.570 1.00 15.37 N ATOM 1304 CA LEU A 159 22.272 1.779 21.056 1.00 15.35 C ATOM 1305 C LEU A 159 23.100 1.868 19.773 1.00 14.94 C ATOM 1306 O LEU A 159 24.331 1.967 19.830 1.00 14.58 O ATOM 1307 CB LEU A 159 22.570 2.953 21.992 1.00 13.91 C ATOM 1308 CG LEU A 159 21.455 3.216 23.005 1.00 13.17 C ATOM 1309 CD1 LEU A 159 21.295 1.986 23.883 1.00 14.26 C ATOM 1310 CD2 LEU A 159 21.781 4.441 23.846 1.00 13.29 C ATOM 1311 N SER A 160 22.432 1.807 18.628 1.00 15.42 N ATOM 1312 CA SER A 160 23.129 1.768 17.348 1.00 15.02 C ATOM 1313 C SER A 160 23.232 3.018 16.482 1.00 15.93 C ATOM 1314 O SER A 160 23.816 2.961 15.401 1.00 15.99 O ATOM 1315 CB SER A 160 22.534 0.633 16.511 1.00 16.24 C ATOM 1316 OG SER A 160 22.333 -0.519 17.314 1.00 16.35 O ATOM 1317 N GLY A 161 22.670 4.132 16.925 1.00 15.21 N ATOM 1318 CA GLY A 161 22.775 5.333 16.116 1.00 16.04 C ATOM 1319 C GLY A 161 21.531 5.720 15.346 1.00 16.22 C ATOM 1320 O GLY A 161 21.565 6.654 14.543 1.00 16.81 O ATOM 1321 N VAL A 162 20.440 4.987 15.553 1.00 15.05 N ATOM 1322 CA VAL A 162 19.171 5.306 14.909 1.00 13.55 C ATOM 1323 C VAL A 162 18.087 5.090 15.956 1.00 13.78 C ATOM 1324 O VAL A 162 17.965 4.002 16.527 1.00 13.31 O ATOM 1325 CB VAL A 162 18.870 4.406 13.669 1.00 14.02 C ATOM 1326 CG1 VAL A 162 17.543 4.825 13.039 1.00 13.58 C ATOM 1327 CG2 VAL A 162 19.995 4.515 12.644 1.00 14.27 C ATOM 1328 N SER A 163 17.322 6.140 16.227 1.00 12.61 N ATOM 1329 CA SER A 163 16.245 6.073 17.204 1.00 13.44 C ATOM 1330 C SER A 163 15.157 7.068 16.816 1.00 13.86 C ATOM 1331 O SER A 163 15.415 8.016 16.074 1.00 15.04 O ATOM 1332 CB SER A 163 16.778 6.389 18.613 1.00 14.19 C ATOM 1333 OG SER A 163 17.329 7.698 18.705 1.00 13.16 O ATOM 1334 N PHE A 164 13.942 6.841 17.302 1.00 13.85 N ATOM 1335 CA PHE A 164 12.814 7.723 17.022 1.00 14.24 C ATOM 1336 C PHE A 164 12.145 8.082 18.342 1.00 14.81 C ATOM 1337 O PHE A 164 12.052 7.246 19.239 1.00 14.50 O ATOM 1338 CB PHE A 164 11.803 7.034 16.106 1.00 15.47 C ATOM 1339 CG PHE A 164 10.541 7.823 15.901 1.00 15.90 C ATOM 1340 CD1 PHE A 164 10.485 8.839 14.942 1.00 16.82 C ATOM 1341 CD2 PHE A 164 9.412 7.570 16.677 1.00 14.88 C ATOM 1342 CE1 PHE A 164 9.324 9.592 14.761 1.00 14.75 C ATOM 1343 CE2 PHE A 164 8.248 8.316 16.505 1.00 15.36 C ATOM 1344 CZ PHE A 164 8.204 9.330 15.546 1.00 16.18 C ATOM 1345 N TRP A 165 11.674 9.317 18.456 1.00 14.94 N ATOM 1346 CA TRP A 165 11.046 9.769 19.692 1.00 15.71 C ATOM 1347 C TRP A 165 9.682 10.387 19.467 1.00 16.32 C ATOM 1348 O TRP A 165 9.544 11.298 18.646 1.00 16.19 O ATOM 1349 CB TRP A 165 11.982 10.759 20.387 1.00 13.69 C ATOM 1350 CG TRP A 165 13.305 10.133 20.563 1.00 14.46 C ATOM 1351 CD1 TRP A 165 14.366 10.195 19.702 1.00 14.42 C ATOM 1352 CD2 TRP A 165 13.655 9.179 21.572 1.00 15.08 C ATOM 1353 NE1 TRP A 165 15.349 9.319 20.104 1.00 15.33 N ATOM 1354 CE2 TRP A 165 14.942 8.684 21.248 1.00 14.54 C ATOM 1355 CE3 TRP A 165 13.004 8.680 22.711 1.00 14.94 C ATOM 1356 CZ2 TRP A 165 15.588 7.715 22.027 1.00 15.68 C ATOM 1357 CZ3 TRP A 165 13.645 7.725 23.484 1.00 13.86 C ATOM 1358 CH2 TRP A 165 14.928 7.251 23.137 1.00 14.53 C ATOM 1359 N ASP A 166 8.675 9.886 20.181 1.00 16.54 N ATOM 1360 CA ASP A 166 7.330 10.433 20.050 1.00 18.46 C ATOM 1361 C ASP A 166 7.216 11.722 20.870 1.00 18.62 C ATOM 1362 O ASP A 166 8.118 12.056 21.648 1.00 17.86 O ATOM 1363 CB ASP A 166 6.262 9.411 20.475 1.00 19.83 C ATOM 1364 CG ASP A 166 6.418 8.956 21.907 1.00 19.80 C ATOM 1365 OD1 ASP A 166 6.811 9.769 22.760 1.00 19.78 O ATOM 1366 OD2 ASP A 166 6.145 7.771 22.179 1.00 22.58 O ATOM 1367 N ALA A 167 6.117 12.451 20.679 1.00 19.24 N ATOM 1368 CA ALA A 167 5.901 13.727 21.359 1.00 20.26 C ATOM 1369 C ALA A 167 5.894 13.644 22.890 1.00 21.58 C ATOM 1370 O ALA A 167 6.593 14.401 23.561 1.00 21.78 O ATOM 1371 CB ALA A 167 4.617 14.364 20.851 1.00 18.93 C ATOM 1372 N PRO A 168 5.086 12.742 23.466 1.00 22.12 N ATOM 1373 CA PRO A 168 5.075 12.650 24.928 1.00 22.10 C ATOM 1374 C PRO A 168 6.460 12.366 25.515 1.00 21.75 C ATOM 1375 O PRO A 168 6.836 12.939 26.542 1.00 22.48 O ATOM 1376 CB PRO A 168 4.094 11.515 25.211 1.00 22.70 C ATOM 1377 CG PRO A 168 3.241 11.436 23.995 1.00 22.99 C ATOM 1378 CD PRO A 168 4.127 11.810 22.851 1.00 22.42 C ATOM 1379 N THR A 169 7.215 11.479 24.866 1.00 20.15 N ATOM 1380 CA THR A 169 8.551 11.126 25.346 1.00 18.89 C ATOM 1381 C THR A 169 9.525 12.293 25.189 1.00 18.19 C ATOM 1382 O THR A 169 10.297 12.594 26.105 1.00 17.50 O ATOM 1383 CB THR A 169 9.123 9.900 24.595 1.00 18.09 C ATOM 1384 OG1 THR A 169 8.163 8.839 24.601 1.00 18.64 O ATOM 1385 CG2 THR A 169 10.398 9.414 25.268 1.00 16.89 C ATOM 1386 N ALA A 170 9.479 12.946 24.028 1.00 17.84 N ATOM 1387 CA ALA A 170 10.355 14.081 23.738 1.00 18.15 C ATOM 1388 C ALA A 170 10.133 15.213 24.741 1.00 18.41 C ATOM 1389 O ALA A 170 11.077 15.906 25.140 1.00 18.17 O ATOM 1390 CB ALA A 170 10.096 14.584 22.321 1.00 16.78 C ATOM 1391 N GLU A 171 8.878 15.399 25.140 1.00 19.79 N ATOM 1392 CA GLU A 171 8.532 16.446 26.089 1.00 21.53 C ATOM 1393 C GLU A 171 9.256 16.190 27.407 1.00 21.70 C ATOM 1394 O GLU A 171 9.838 17.100 27.995 1.00 22.26 O ATOM 1395 CB GLU A 171 7.024 16.466 26.307 1.00 24.62 C ATOM 1396 CG GLU A 171 6.540 17.661 27.083 1.00 32.25 C ATOM 1397 CD GLU A 171 5.077 17.548 27.455 1.00 37.81 C ATOM 1398 OE1 GLU A 171 4.660 16.457 27.899 1.00 41.39 O ATOM 1399 OE2 GLU A 171 4.344 18.548 27.302 1.00 40.64 O ATOM 1400 N LYS A 172 9.231 14.943 27.865 1.00 21.32 N ATOM 1401 CA LYS A 172 9.903 14.588 29.109 1.00 21.36 C ATOM 1402 C LYS A 172 11.405 14.781 28.961 1.00 18.96 C ATOM 1403 O LYS A 172 12.059 15.326 29.846 1.00 19.03 O ATOM 1404 CB LYS A 172 9.608 13.132 29.483 1.00 23.45 C ATOM 1405 CG LYS A 172 8.169 12.893 29.908 1.00 27.07 C ATOM 1406 CD LYS A 172 8.006 11.532 30.561 1.00 30.43 C ATOM 1407 CE LYS A 172 7.088 11.613 31.764 1.00 31.32 C ATOM 1408 NZ LYS A 172 6.667 10.263 32.220 1.00 32.39 N ATOM 1409 N ILE A 173 11.953 14.330 27.840 1.00 17.23 N ATOM 1410 CA ILE A 173 13.383 14.461 27.608 1.00 16.82 C ATOM 1411 C ILE A 173 13.831 15.934 27.564 1.00 16.88 C ATOM 1412 O ILE A 173 14.912 16.268 28.050 1.00 16.01 O ATOM 1413 CB ILE A 173 13.790 13.739 26.301 1.00 15.98 C ATOM 1414 CG1 ILE A 173 13.725 12.228 26.520 1.00 13.86 C ATOM 1415 CG2 ILE A 173 15.201 14.145 25.872 1.00 13.79 C ATOM 1416 CD1 ILE A 173 13.682 11.414 25.230 1.00 15.73 C ATOM 1417 N VAL A 174 13.008 16.815 26.997 1.00 16.95 N ATOM 1418 CA VAL A 174 13.387 18.225 26.923 1.00 18.08 C ATOM 1419 C VAL A 174 13.483 18.809 28.333 1.00 18.41 C ATOM 1420 O VAL A 174 14.377 19.605 28.628 1.00 17.77 O ATOM 1421 CB VAL A 174 12.381 19.055 26.083 1.00 18.28 C ATOM 1422 CG1 VAL A 174 12.668 20.546 26.245 1.00 18.11 C ATOM 1423 CG2 VAL A 174 12.481 18.661 24.607 1.00 18.32 C ATOM 1424 N SER A 175 12.568 18.404 29.204 1.00 19.02 N ATOM 1425 CA SER A 175 12.593 18.892 30.574 1.00 19.83 C ATOM 1426 C SER A 175 13.878 18.410 31.259 1.00 18.71 C ATOM 1427 O SER A 175 14.492 19.144 32.042 1.00 17.39 O ATOM 1428 CB SER A 175 11.354 18.405 31.329 1.00 19.95 C ATOM 1429 OG SER A 175 11.517 17.070 31.770 1.00 23.70 O ATOM 1430 N PHE A 176 14.291 17.181 30.957 1.00 19.00 N ATOM 1431 CA PHE A 176 15.517 16.631 31.531 1.00 18.50 C ATOM 1432 C PHE A 176 16.712 17.389 30.960 1.00 17.77 C ATOM 1433 O PHE A 176 17.704 17.633 31.655 1.00 17.34 O ATOM 1434 CB PHE A 176 15.665 15.142 31.188 1.00 17.97 C ATOM 1435 CG PHE A 176 14.545 14.283 31.696 1.00 19.90 C ATOM 1436 CD1 PHE A 176 14.179 13.128 31.011 1.00 20.17 C ATOM 1437 CD2 PHE A 176 13.847 14.626 32.853 1.00 20.74 C ATOM 1438 CE1 PHE A 176 13.132 12.324 31.468 1.00 20.54 C ATOM 1439 CE2 PHE A 176 12.800 13.832 33.318 1.00 20.66 C ATOM 1440 CZ PHE A 176 12.441 12.678 32.622 1.00 22.03 C ATOM 1441 N ILE A 177 16.610 17.754 29.686 1.00 17.79 N ATOM 1442 CA ILE A 177 17.674 18.487 29.011 1.00 16.73 C ATOM 1443 C ILE A 177 17.814 19.875 29.636 1.00 16.01 C ATOM 1444 O ILE A 177 18.924 20.307 29.957 1.00 15.96 O ATOM 1445 CB ILE A 177 17.375 18.637 27.498 1.00 16.62 C ATOM 1446 CG1 ILE A 177 17.655 17.308 26.781 1.00 14.74 C ATOM 1447 CG2 ILE A 177 18.203 19.780 26.911 1.00 13.84 C ATOM 1448 CD1 ILE A 177 17.174 17.262 25.339 1.00 15.16 C ATOM 1449 N ASP A 178 16.682 20.557 29.805 1.00 16.58 N ATOM 1450 CA ASP A 178 16.676 21.898 30.391 1.00 16.90 C ATOM 1451 C ASP A 178 17.350 21.844 31.749 1.00 17.23 C ATOM 1452 O ASP A 178 18.257 22.621 32.033 1.00 17.59 O ATOM 1453 CB ASP A 178 15.248 22.409 30.571 1.00 17.05 C ATOM 1454 CG ASP A 178 14.582 22.765 29.257 1.00 16.94 C ATOM 1455 OD1 ASP A 178 13.338 22.823 29.233 1.00 18.14 O ATOM 1456 OD2 ASP A 178 15.294 22.984 28.254 1.00 19.41 O ATOM 1457 N LYS A 179 16.905 20.907 32.580 1.00 17.86 N ATOM 1458 CA LYS A 179 17.457 20.740 33.923 1.00 18.61 C ATOM 1459 C LYS A 179 18.957 20.479 33.934 1.00 17.76 C ATOM 1460 O LYS A 179 19.683 21.071 34.729 1.00 17.97 O ATOM 1461 CB LYS A 179 16.738 19.601 34.660 1.00 20.44 C ATOM 1462 CG LYS A 179 17.281 19.315 36.063 1.00 23.01 C ATOM 1463 CD LYS A 179 16.665 18.046 36.649 1.00 25.44 C ATOM 1464 CE LYS A 179 15.238 18.288 37.148 1.00 27.16 C ATOM 1465 NZ LYS A 179 14.833 17.322 38.214 1.00 29.68 N ATOM 1466 N ALA A 180 19.429 19.593 33.060 1.00 16.61 N ATOM 1467 CA ALA A 180 20.851 19.282 33.013 1.00 15.53 C ATOM 1468 C ALA A 180 21.682 20.481 32.567 1.00 16.10 C ATOM 1469 O ALA A 180 22.740 20.762 33.138 1.00 15.92 O ATOM 1470 CB ALA A 180 21.095 18.101 32.077 1.00 16.34 C ATOM 1471 N TYR A 181 21.201 21.187 31.547 1.00 16.61 N ATOM 1472 CA TYR A 181 21.911 22.343 31.007 1.00 16.83 C ATOM 1473 C TYR A 181 22.069 23.473 32.027 1.00 18.07 C ATOM 1474 O TYR A 181 23.060 24.205 32.005 1.00 17.89 O ATOM 1475 CB TYR A 181 21.175 22.866 29.773 1.00 16.18 C ATOM 1476 CG TYR A 181 21.924 23.923 28.984 1.00 16.91 C ATOM 1477 CD1 TYR A 181 23.210 23.681 28.495 1.00 17.75 C ATOM 1478 CD2 TYR A 181 21.334 25.159 28.702 1.00 17.08 C ATOM 1479 CE1 TYR A 181 23.892 24.644 27.742 1.00 17.92 C ATOM 1480 CE2 TYR A 181 22.004 26.127 27.951 1.00 17.02 C ATOM 1481 CZ TYR A 181 23.281 25.864 27.472 1.00 18.20 C ATOM 1482 OH TYR A 181 23.947 26.806 26.718 1.00 18.98 O ATOM 1483 N VAL A 182 21.099 23.608 32.924 1.00 19.16 N ATOM 1484 CA VAL A 182 21.153 24.673 33.923 1.00 22.29 C ATOM 1485 C VAL A 182 21.559 24.249 35.331 1.00 21.76 C ATOM 1486 O VAL A 182 21.402 25.024 36.277 1.00 20.97 O ATOM 1487 CB VAL A 182 19.805 25.384 34.032 1.00 24.06 C ATOM 1488 CG1 VAL A 182 19.614 26.294 32.845 1.00 29.85 C ATOM 1489 CG2 VAL A 182 18.692 24.374 34.112 1.00 27.22 C ATOM 1490 N SER A 183 22.076 23.030 35.468 1.00 20.30 N ATOM 1491 CA SER A 183 22.486 22.517 36.767 1.00 19.89 C ATOM 1492 C SER A 183 23.984 22.253 36.823 1.00 21.22 C ATOM 1493 O SER A 183 24.478 21.640 37.770 1.00 20.97 O ATOM 1494 CB SER A 183 21.714 21.237 37.085 1.00 18.22 C ATOM 1495 OG SER A 183 20.339 21.521 37.268 1.00 20.96 O ATOM 1496 N GLY A 184 24.702 22.722 35.803 1.00 22.93 N ATOM 1497 CA GLY A 184 26.143 22.541 35.749 1.00 24.77 C ATOM 1498 C GLY A 184 26.571 21.087 35.676 1.00 27.18 C ATOM 1499 O GLY A 184 27.645 20.731 36.153 1.00 28.18 O ATOM 1500 N GLU A 185 25.732 20.248 35.073 1.00 28.91 N ATOM 1501 CA GLU A 185 26.019 18.819 34.939 1.00 30.50 C ATOM 1502 C GLU A 185 25.656 18.360 33.531 1.00 29.11 C ATOM 1503 O GLU A 185 24.785 17.504 33.365 1.00 31.19 O ATOM 1504 CB GLU A 185 25.197 18.023 35.968 1.00 34.03 C ATOM 1505 CG GLU A 185 24.017 18.803 36.574 1.00 37.45 C ATOM 1506 CD GLU A 185 23.186 18.000 37.583 1.00 38.48 C ATOM 1507 OE1 GLU A 185 21.938 18.031 37.488 1.00 37.69 O ATOM 1508 OE2 GLU A 185 23.774 17.348 38.473 1.00 39.32 O ATOM 1509 N PHE A 186 26.323 18.915 32.519 1.00 24.92 N ATOM 1510 CA PHE A 186 26.003 18.554 31.138 1.00 22.11 C ATOM 1511 C PHE A 186 27.163 18.514 30.137 1.00 20.45 C ATOM 1512 O PHE A 186 27.111 17.765 29.169 1.00 19.39 O ATOM 1513 CB PHE A 186 24.937 19.517 30.593 1.00 19.61 C ATOM 1514 CG PHE A 186 25.480 20.884 30.250 1.00 20.00 C ATOM 1515 CD1 PHE A 186 25.539 21.885 31.216 1.00 18.32 C ATOM 1516 CD2 PHE A 186 25.999 21.147 28.980 1.00 19.06 C ATOM 1517 CE1 PHE A 186 26.110 23.119 30.928 1.00 18.25 C ATOM 1518 CE2 PHE A 186 26.574 22.381 28.681 1.00 18.45 C ATOM 1519 CZ PHE A 186 26.629 23.369 29.661 1.00 18.07 C ATOM 1520 N VAL A 187 28.197 19.317 30.360 1.00 20.95 N ATOM 1521 CA VAL A 187 29.314 19.397 29.417 1.00 20.68 C ATOM 1522 C VAL A 187 29.895 18.087 28.902 1.00 20.92 C ATOM 1523 O VAL A 187 30.282 18.005 27.741 1.00 20.85 O ATOM 1524 CB VAL A 187 30.480 20.268 29.974 1.00 21.54 C ATOM 1525 CG1 VAL A 187 29.985 21.684 30.229 1.00 22.61 C ATOM 1526 CG2 VAL A 187 31.049 19.662 31.252 1.00 23.00 C ATOM 1527 N ASP A 188 29.951 17.060 29.743 1.00 21.70 N ATOM 1528 CA ASP A 188 30.521 15.785 29.317 1.00 23.53 C ATOM 1529 C ASP A 188 29.481 14.739 28.929 1.00 21.53 C ATOM 1530 O ASP A 188 29.834 13.634 28.522 1.00 22.65 O ATOM 1531 CB ASP A 188 31.421 15.219 30.424 1.00 29.27 C ATOM 1532 CG ASP A 188 32.572 16.145 30.771 1.00 34.78 C ATOM 1533 OD1 ASP A 188 32.655 16.582 31.940 1.00 39.39 O ATOM 1534 OD2 ASP A 188 33.393 16.435 29.875 1.00 38.26 O ATOM 1535 N LEU A 189 28.206 15.093 29.030 1.00 19.19 N ATOM 1536 CA LEU A 189 27.127 14.164 28.720 1.00 18.61 C ATOM 1537 C LEU A 189 26.849 13.931 27.246 1.00 18.26 C ATOM 1538 O LEU A 189 27.072 14.800 26.396 1.00 17.08 O ATOM 1539 CB LEU A 189 25.817 14.631 29.366 1.00 18.26 C ATOM 1540 CG LEU A 189 25.665 14.730 30.889 1.00 18.31 C ATOM 1541 CD1 LEU A 189 24.243 15.149 31.210 1.00 18.72 C ATOM 1542 CD2 LEU A 189 25.983 13.408 31.546 1.00 17.75 C ATOM 1543 N TYR A 190 26.356 12.733 26.958 1.00 18.29 N ATOM 1544 CA TYR A 190 25.950 12.377 25.608 1.00 18.51 C ATOM 1545 C TYR A 190 24.464 12.671 25.678 1.00 17.59 C ATOM 1546 O TYR A 190 23.890 12.645 26.772 1.00 16.52 O ATOM 1547 CB TYR A 190 26.125 10.882 25.348 1.00 19.93 C ATOM 1548 CG TYR A 190 27.544 10.396 25.407 1.00 23.59 C ATOM 1549 CD1 TYR A 190 27.996 9.651 26.494 1.00 26.25 C ATOM 1550 CD2 TYR A 190 28.424 10.632 24.357 1.00 25.96 C ATOM 1551 CE1 TYR A 190 29.290 9.146 26.533 1.00 28.69 C ATOM 1552 CE2 TYR A 190 29.721 10.132 24.384 1.00 29.77 C ATOM 1553 CZ TYR A 190 30.146 9.387 25.474 1.00 30.49 C ATOM 1554 OH TYR A 190 31.419 8.864 25.498 1.00 33.42 O ATOM 1555 N TRP A 191 23.830 12.949 24.543 1.00 16.12 N ATOM 1556 CA TRP A 191 22.402 13.208 24.576 1.00 16.20 C ATOM 1557 C TRP A 191 21.692 11.954 25.116 1.00 17.24 C ATOM 1558 O TRP A 191 20.635 12.041 25.750 1.00 16.78 O ATOM 1559 CB TRP A 191 21.887 13.583 23.176 1.00 16.82 C ATOM 1560 CG TRP A 191 21.653 12.423 22.246 1.00 17.34 C ATOM 1561 CD1 TRP A 191 22.534 11.910 21.335 1.00 16.61 C ATOM 1562 CD2 TRP A 191 20.453 11.637 22.133 1.00 17.98 C ATOM 1563 NE1 TRP A 191 21.955 10.862 20.658 1.00 17.19 N ATOM 1564 CE2 TRP A 191 20.681 10.671 21.128 1.00 17.78 C ATOM 1565 CE3 TRP A 191 19.205 11.662 22.781 1.00 17.94 C ATOM 1566 CZ2 TRP A 191 19.705 9.735 20.752 1.00 16.89 C ATOM 1567 CZ3 TRP A 191 18.236 10.728 22.411 1.00 16.56 C ATOM 1568 CH2 TRP A 191 18.494 9.779 21.405 1.00 18.16 C ATOM 1569 N ASP A 192 22.297 10.790 24.884 1.00 16.91 N ATOM 1570 CA ASP A 192 21.733 9.522 25.340 1.00 16.93 C ATOM 1571 C ASP A 192 21.586 9.442 26.854 1.00 16.64 C ATOM 1572 O ASP A 192 20.687 8.766 27.361 1.00 16.82 O ATOM 1573 CB ASP A 192 22.605 8.366 24.871 1.00 17.82 C ATOM 1574 CG ASP A 192 22.837 8.396 23.393 1.00 19.08 C ATOM 1575 OD1 ASP A 192 22.028 7.791 22.659 1.00 20.22 O ATOM 1576 OD2 ASP A 192 23.822 9.035 22.967 1.00 22.20 O ATOM 1577 N ASN A 193 22.473 10.119 27.574 1.00 16.83 N ATOM 1578 CA ASN A 193 22.406 10.103 29.027 1.00 17.00 C ATOM 1579 C ASN A 193 21.030 10.510 29.446 1.00 18.02 C ATOM 1580 O ASN A 193 20.583 10.233 30.552 1.00 18.09 O ATOM 1581 CB ASN A 193 23.391 11.084 29.623 1.00 15.75 C ATOM 1582 CG ASN A 193 24.719 10.453 29.898 1.00 15.58 C ATOM 1583 OD1 ASN A 193 25.650 10.569 29.104 1.00 16.55 O ATOM 1584 ND2 ASN A 193 24.823 9.772 31.029 1.00 16.33 N HETATM 1585 N MSE A 194 20.311 11.161 28.558 1.00 20.29 N HETATM 1586 CA MSE A 194 19.032 11.564 29.028 1.00 21.63 C HETATM 1587 C MSE A 194 17.885 10.644 28.963 1.00 20.63 C HETATM 1588 O MSE A 194 16.856 10.852 29.603 1.00 19.76 O HETATM 1589 CB MSE A 194 18.838 12.968 28.581 1.00 25.25 C HETATM 1590 CG MSE A 194 19.073 13.537 29.926 1.00 34.51 C HETATM 1591 SE MSE A 194 19.123 15.197 29.716 1.00 29.13 SE HETATM 1592 CE MSE A 194 21.162 15.191 29.599 1.00 34.88 C ATOM 1593 N VAL A 195 18.139 9.533 28.295 1.00 19.13 N ATOM 1594 CA VAL A 195 17.171 8.491 28.234 1.00 18.21 C ATOM 1595 C VAL A 195 17.690 7.520 29.301 1.00 18.04 C ATOM 1596 O VAL A 195 16.932 7.063 30.157 1.00 18.41 O ATOM 1597 CB VAL A 195 17.176 7.821 26.871 1.00 18.42 C ATOM 1598 CG1 VAL A 195 16.133 6.704 26.843 1.00 15.45 C ATOM 1599 CG2 VAL A 195 16.891 8.858 25.793 1.00 18.15 C ATOM 1600 N LYS A 196 18.989 7.239 29.263 1.00 17.25 N ATOM 1601 CA LYS A 196 19.599 6.308 30.213 1.00 18.07 C ATOM 1602 C LYS A 196 19.407 6.701 31.672 1.00 18.84 C ATOM 1603 O LYS A 196 19.011 5.876 32.496 1.00 19.22 O ATOM 1604 CB LYS A 196 21.098 6.165 29.945 1.00 19.16 C ATOM 1605 CG LYS A 196 21.846 5.380 31.023 1.00 21.11 C ATOM 1606 CD LYS A 196 23.318 5.222 30.671 1.00 25.58 C ATOM 1607 CE LYS A 196 24.057 4.375 31.694 1.00 28.48 C ATOM 1608 NZ LYS A 196 24.249 5.101 32.982 1.00 33.23 N ATOM 1609 N ASP A 197 19.685 7.963 31.983 1.00 18.65 N ATOM 1610 CA ASP A 197 19.588 8.458 33.355 1.00 18.44 C ATOM 1611 C ASP A 197 18.175 8.760 33.854 1.00 18.12 C ATOM 1612 O ASP A 197 17.998 9.137 35.008 1.00 19.65 O ATOM 1613 CB ASP A 197 20.478 9.698 33.512 1.00 16.41 C ATOM 1614 CG ASP A 197 21.958 9.395 33.275 1.00 17.67 C ATOM 1615 OD1 ASP A 197 22.724 10.333 32.974 1.00 19.68 O ATOM 1616 OD2 ASP A 197 22.371 8.218 33.392 1.00 22.50 O ATOM 1617 N ASN A 198 17.173 8.586 32.999 1.00 17.60 N ATOM 1618 CA ASN A 198 15.783 8.847 33.379 1.00 18.29 C ATOM 1619 C ASN A 198 14.871 7.772 32.794 1.00 18.42 C ATOM 1620 O ASN A 198 13.665 7.964 32.684 1.00 18.02 O ATOM 1621 CB ASN A 198 15.339 10.218 32.847 1.00 18.37 C ATOM 1622 CG ASN A 198 16.233 11.353 33.322 1.00 21.09 C ATOM 1623 OD1 ASN A 198 16.061 11.863 34.429 1.00 22.11 O ATOM 1624 ND2 ASN A 198 17.191 11.755 32.485 1.00 18.12 N ATOM 1625 N ILE A 199 15.461 6.640 32.422 1.00 20.07 N ATOM 1626 CA ILE A 199 14.721 5.548 31.797 1.00 21.15 C ATOM 1627 C ILE A 199 13.417 5.152 32.492 1.00 22.26 C ATOM 1628 O ILE A 199 12.426 4.841 31.837 1.00 22.71 O ATOM 1629 CB ILE A 199 15.640 4.308 31.634 1.00 20.12 C ATOM 1630 CG1 ILE A 199 14.979 3.278 30.715 1.00 20.01 C ATOM 1631 CG2 ILE A 199 15.961 3.715 32.994 1.00 20.37 C ATOM 1632 CD1 ILE A 199 14.507 3.844 29.389 1.00 18.95 C ATOM 1633 N LYS A 200 13.415 5.182 33.819 1.00 24.78 N ATOM 1634 CA LYS A 200 12.238 4.821 34.606 1.00 25.94 C ATOM 1635 C LYS A 200 11.042 5.735 34.359 1.00 25.48 C ATOM 1636 O LYS A 200 9.913 5.395 34.712 1.00 25.83 O ATOM 1637 CB LYS A 200 12.587 4.820 36.101 1.00 28.69 C ATOM 1638 CG LYS A 200 14.081 5.025 36.411 1.00 33.34 C ATOM 1639 CD LYS A 200 14.608 6.349 35.846 1.00 34.35 C ATOM 1640 CE LYS A 200 16.125 6.486 35.956 1.00 35.64 C ATOM 1641 NZ LYS A 200 16.888 5.238 35.673 1.00 39.83 N ATOM 1642 N GLU A 201 11.282 6.890 33.747 1.00 25.59 N ATOM 1643 CA GLU A 201 10.208 7.843 33.457 1.00 26.63 C ATOM 1644 C GLU A 201 9.788 7.839 31.992 1.00 24.98 C ATOM 1645 O GLU A 201 8.828 8.513 31.619 1.00 24.64 O ATOM 1646 CB GLU A 201 10.647 9.266 33.802 1.00 29.55 C ATOM 1647 CG GLU A 201 11.396 9.388 35.098 1.00 36.39 C ATOM 1648 CD GLU A 201 10.491 9.173 36.278 1.00 40.39 C ATOM 1649 OE1 GLU A 201 9.315 9.590 36.195 1.00 42.60 O ATOM 1650 OE2 GLU A 201 10.954 8.586 37.281 1.00 44.15 O ATOM 1651 N LEU A 202 10.504 7.089 31.164 1.00 23.32 N ATOM 1652 CA LEU A 202 10.211 7.074 29.743 1.00 21.76 C ATOM 1653 C LEU A 202 9.759 5.734 29.202 1.00 21.90 C ATOM 1654 O LEU A 202 10.129 4.683 29.717 1.00 22.72 O ATOM 1655 CB LEU A 202 11.443 7.546 28.967 1.00 20.96 C ATOM 1656 CG LEU A 202 12.083 8.853 29.447 1.00 21.01 C ATOM 1657 CD1 LEU A 202 13.494 8.988 28.876 1.00 20.95 C ATOM 1658 CD2 LEU A 202 11.206 10.024 29.038 1.00 19.09 C ATOM 1659 N ASP A 203 8.944 5.789 28.155 1.00 21.65 N ATOM 1660 CA ASP A 203 8.442 4.592 27.492 1.00 21.78 C ATOM 1661 C ASP A 203 9.134 4.528 26.132 1.00 21.87 C ATOM 1662 O ASP A 203 8.798 5.290 25.219 1.00 22.40 O ATOM 1663 CB ASP A 203 6.926 4.673 27.298 1.00 22.68 C ATOM 1664 CG ASP A 203 6.164 4.609 28.610 1.00 26.02 C ATOM 1665 OD1 ASP A 203 6.732 4.142 29.620 1.00 27.03 O ATOM 1666 OD2 ASP A 203 4.993 5.030 28.630 1.00 28.81 O ATOM 1667 N VAL A 204 10.110 3.635 26.018 1.00 19.94 N ATOM 1668 CA VAL A 204 10.863 3.460 24.780 1.00 18.92 C ATOM 1669 C VAL A 204 10.885 1.979 24.441 1.00 18.07 C ATOM 1670 O VAL A 204 10.962 1.129 25.327 1.00 17.77 O ATOM 1671 CB VAL A 204 12.319 3.952 24.921 1.00 18.34 C ATOM 1672 CG1 VAL A 204 12.910 4.231 23.532 1.00 16.28 C ATOM 1673 CG2 VAL A 204 12.366 5.193 25.814 1.00 18.47 C ATOM 1674 N TYR A 205 10.830 1.673 23.156 1.00 16.83 N ATOM 1675 CA TYR A 205 10.815 0.292 22.731 1.00 17.56 C ATOM 1676 C TYR A 205 11.979 -0.053 21.832 1.00 17.22 C ATOM 1677 O TYR A 205 12.637 0.828 21.291 1.00 18.61 O ATOM 1678 CB TYR A 205 9.488 -0.001 22.045 1.00 17.87 C ATOM 1679 CG TYR A 205 8.338 0.176 22.992 1.00 20.95 C ATOM 1680 CD1 TYR A 205 7.852 1.445 23.297 1.00 20.66 C ATOM 1681 CD2 TYR A 205 7.757 -0.925 23.623 1.00 22.02 C ATOM 1682 CE1 TYR A 205 6.816 1.612 24.205 1.00 22.57 C ATOM 1683 CE2 TYR A 205 6.723 -0.767 24.532 1.00 22.64 C ATOM 1684 CZ TYR A 205 6.259 0.501 24.816 1.00 23.02 C ATOM 1685 OH TYR A 205 5.224 0.654 25.702 1.00 27.95 O ATOM 1686 N VAL A 206 12.232 -1.347 21.685 1.00 16.26 N ATOM 1687 CA VAL A 206 13.333 -1.820 20.869 1.00 16.23 C ATOM 1688 C VAL A 206 12.863 -2.481 19.578 1.00 17.34 C ATOM 1689 O VAL A 206 11.957 -3.315 19.591 1.00 16.87 O ATOM 1690 CB VAL A 206 14.200 -2.834 21.656 1.00 15.79 C ATOM 1691 CG1 VAL A 206 15.360 -3.320 20.801 1.00 16.04 C ATOM 1692 CG2 VAL A 206 14.727 -2.189 22.925 1.00 16.34 C ATOM 1693 N GLU A 207 13.475 -2.081 18.467 1.00 17.07 N ATOM 1694 CA GLU A 207 13.180 -2.658 17.167 1.00 17.62 C ATOM 1695 C GLU A 207 14.454 -3.414 16.819 1.00 16.99 C ATOM 1696 O GLU A 207 15.461 -2.812 16.459 1.00 16.38 O ATOM 1697 CB GLU A 207 12.912 -1.560 16.142 1.00 21.12 C ATOM 1698 CG GLU A 207 12.744 -2.058 14.709 1.00 26.70 C ATOM 1699 CD GLU A 207 11.469 -2.855 14.497 1.00 30.88 C ATOM 1700 OE1 GLU A 207 10.492 -2.653 15.256 1.00 32.31 O ATOM 1701 OE2 GLU A 207 11.447 -3.687 13.566 1.00 33.82 O ATOM 1702 N GLU A 208 14.412 -4.736 16.959 1.00 16.83 N ATOM 1703 CA GLU A 208 15.569 -5.572 16.689 1.00 17.29 C ATOM 1704 C GLU A 208 15.923 -5.607 15.211 1.00 18.74 C ATOM 1705 O GLU A 208 15.133 -6.056 14.382 1.00 19.71 O ATOM 1706 CB GLU A 208 15.308 -6.986 17.195 1.00 17.36 C ATOM 1707 CG GLU A 208 15.008 -7.041 18.682 1.00 19.88 C ATOM 1708 CD GLU A 208 14.942 -8.460 19.217 1.00 21.92 C ATOM 1709 OE1 GLU A 208 14.490 -9.348 18.466 1.00 22.53 O ATOM 1710 OE2 GLU A 208 15.337 -8.686 20.382 1.00 21.79 O ATOM 1711 N LEU A 209 17.119 -5.127 14.887 1.00 18.55 N ATOM 1712 CA LEU A 209 17.586 -5.098 13.511 1.00 19.31 C ATOM 1713 C LEU A 209 18.463 -6.303 13.201 1.00 20.32 C ATOM 1714 O LEU A 209 19.132 -6.846 14.086 1.00 19.13 O ATOM 1715 CB LEU A 209 18.405 -3.828 13.252 1.00 16.76 C ATOM 1716 CG LEU A 209 17.707 -2.471 13.252 1.00 17.27 C ATOM 1717 CD1 LEU A 209 18.732 -1.380 12.991 1.00 16.84 C ATOM 1718 CD2 LEU A 209 16.637 -2.443 12.181 1.00 17.65 C ATOM 1719 N GLU A 210 18.458 -6.715 11.934 1.00 23.26 N ATOM 1720 CA GLU A 210 19.296 -7.819 11.492 1.00 27.48 C ATOM 1721 C GLU A 210 20.726 -7.301 11.579 1.00 28.28 C ATOM 1722 O GLU A 210 20.991 -6.135 11.287 1.00 27.71 O ATOM 1723 CB GLU A 210 18.955 -8.202 10.056 1.00 32.04 C ATOM 1724 CG GLU A 210 17.520 -8.684 9.895 1.00 42.39 C ATOM 1725 CD GLU A 210 17.062 -8.705 8.447 1.00 48.64 C ATOM 1726 OE1 GLU A 210 17.077 -9.796 7.836 1.00 51.52 O ATOM 1727 OE2 GLU A 210 16.687 -7.632 7.921 1.00 51.47 O ATOM 1728 N GLY A 211 21.637 -8.172 11.991 1.00 29.84 N ATOM 1729 CA GLY A 211 23.033 -7.805 12.161 1.00 31.97 C ATOM 1730 C GLY A 211 23.705 -6.849 11.192 1.00 32.92 C ATOM 1731 O GLY A 211 24.463 -5.982 11.620 1.00 33.65 O ATOM 1732 N ASN A 212 23.439 -6.993 9.899 1.00 33.12 N ATOM 1733 CA ASN A 212 24.075 -6.142 8.895 1.00 34.92 C ATOM 1734 C ASN A 212 23.247 -4.937 8.432 1.00 33.50 C ATOM 1735 O ASN A 212 23.510 -4.374 7.367 1.00 34.76 O ATOM 1736 CB ASN A 212 24.456 -6.993 7.676 1.00 38.78 C ATOM 1737 CG ASN A 212 23.353 -7.955 7.268 1.00 43.28 C ATOM 1738 OD1 ASN A 212 22.164 -7.636 7.367 1.00 45.42 O ATOM 1739 ND2 ASN A 212 23.742 -9.143 6.806 1.00 45.16 N ATOM 1740 N SER A 213 22.266 -4.533 9.227 1.00 29.61 N ATOM 1741 CA SER A 213 21.408 -3.411 8.861 1.00 27.19 C ATOM 1742 C SER A 213 22.131 -2.077 8.975 1.00 25.63 C ATOM 1743 O SER A 213 21.979 -1.198 8.125 1.00 23.25 O ATOM 1744 CB SER A 213 20.166 -3.401 9.749 1.00 27.99 C ATOM 1745 OG SER A 213 19.204 -4.327 9.277 1.00 30.65 O ATOM 1746 N ILE A 214 22.899 -1.930 10.050 1.00 24.78 N ATOM 1747 CA ILE A 214 23.676 -0.722 10.302 1.00 23.79 C ATOM 1748 C ILE A 214 25.128 -1.163 10.377 1.00 23.98 C ATOM 1749 O ILE A 214 25.452 -2.143 11.048 1.00 26.54 O ATOM 1750 CB ILE A 214 23.292 -0.064 11.651 1.00 22.32 C ATOM 1751 CG1 ILE A 214 21.897 0.554 11.559 1.00 23.07 C ATOM 1752 CG2 ILE A 214 24.305 1.005 12.020 1.00 22.17 C ATOM 1753 CD1 ILE A 214 21.294 0.907 12.904 1.00 20.99 C ATOM 1754 N TYR A 215 26.002 -0.462 9.674 1.00 22.01 N ATOM 1755 CA TYR A 215 27.412 -0.802 9.700 1.00 21.52 C ATOM 1756 C TYR A 215 28.138 0.369 10.334 1.00 22.45 C ATOM 1757 O TYR A 215 28.174 1.457 9.770 1.00 22.19 O ATOM 1758 CB TYR A 215 27.930 -1.041 8.289 1.00 21.46 C ATOM 1759 CG TYR A 215 29.365 -1.503 8.238 1.00 22.24 C ATOM 1760 CD1 TYR A 215 29.686 -2.785 7.796 1.00 22.35 C ATOM 1761 CD2 TYR A 215 30.408 -0.648 8.589 1.00 22.43 C ATOM 1762 CE1 TYR A 215 31.011 -3.201 7.701 1.00 23.41 C ATOM 1763 CE2 TYR A 215 31.733 -1.053 8.498 1.00 22.58 C ATOM 1764 CZ TYR A 215 32.027 -2.331 8.051 1.00 23.28 C ATOM 1765 OH TYR A 215 33.336 -2.737 7.938 1.00 25.47 O ATOM 1766 N GLU A 216 28.703 0.138 11.515 1.00 23.42 N ATOM 1767 CA GLU A 216 29.419 1.169 12.255 1.00 24.02 C ATOM 1768 C GLU A 216 30.809 1.428 11.715 1.00 22.25 C ATOM 1769 O GLU A 216 31.562 0.494 11.447 1.00 24.16 O ATOM 1770 CB GLU A 216 29.551 0.770 13.724 1.00 27.03 C ATOM 1771 CG GLU A 216 28.256 0.352 14.373 1.00 34.14 C ATOM 1772 CD GLU A 216 27.831 -1.061 14.000 1.00 38.51 C ATOM 1773 OE1 GLU A 216 28.549 -1.735 13.221 1.00 38.43 O ATOM 1774 OE2 GLU A 216 26.766 -1.494 14.496 1.00 42.50 O ATOM 1775 N ILE A 217 31.145 2.700 11.551 1.00 21.08 N ATOM 1776 CA ILE A 217 32.472 3.073 11.085 1.00 20.78 C ATOM 1777 C ILE A 217 33.135 3.733 12.290 1.00 21.41 C ATOM 1778 O ILE A 217 32.989 4.932 12.517 1.00 21.24 O ATOM 1779 CB ILE A 217 32.401 4.055 9.896 1.00 19.84 C ATOM 1780 CG1 ILE A 217 31.503 3.465 8.803 1.00 19.52 C ATOM 1781 CG2 ILE A 217 33.802 4.309 9.345 1.00 19.34 C ATOM 1782 CD1 ILE A 217 31.552 4.196 7.488 1.00 18.96 C ATOM 1783 N ASP A 218 33.846 2.925 13.071 1.00 21.83 N ATOM 1784 CA ASP A 218 34.502 3.404 14.279 1.00 23.22 C ATOM 1785 C ASP A 218 35.997 3.609 14.116 1.00 21.97 C ATOM 1786 O ASP A 218 36.655 4.100 15.031 1.00 21.87 O ATOM 1787 CB ASP A 218 34.269 2.418 15.432 1.00 27.19 C ATOM 1788 CG ASP A 218 32.828 2.405 15.912 1.00 31.35 C ATOM 1789 OD1 ASP A 218 32.156 3.452 15.801 1.00 33.55 O ATOM 1790 OD2 ASP A 218 32.369 1.345 16.400 1.00 31.63 O ATOM 1791 N SER A 219 36.535 3.219 12.966 1.00 21.05 N ATOM 1792 CA SER A 219 37.964 3.358 12.700 1.00 20.09 C ATOM 1793 C SER A 219 38.177 3.354 11.199 1.00 19.66 C ATOM 1794 O SER A 219 37.273 2.981 10.453 1.00 20.18 O ATOM 1795 CB SER A 219 38.723 2.183 13.309 1.00 19.87 C ATOM 1796 OG SER A 219 38.396 0.976 12.639 1.00 18.97 O ATOM 1797 N VAL A 220 39.361 3.760 10.748 1.00 18.73 N ATOM 1798 CA VAL A 220 39.626 3.755 9.313 1.00 19.26 C ATOM 1799 C VAL A 220 39.632 2.293 8.850 1.00 19.10 C ATOM 1800 O VAL A 220 39.388 1.992 7.688 1.00 19.32 O ATOM 1801 CB VAL A 220 40.972 4.450 8.972 1.00 17.97 C ATOM 1802 CG1 VAL A 220 42.134 3.663 9.537 1.00 18.97 C ATOM 1803 CG2 VAL A 220 41.111 4.597 7.468 1.00 19.22 C ATOM 1804 N GLN A 221 39.888 1.380 9.784 1.00 20.26 N ATOM 1805 CA GLN A 221 39.894 -0.043 9.468 1.00 20.68 C ATOM 1806 C GLN A 221 38.473 -0.475 9.116 1.00 19.49 C ATOM 1807 O GLN A 221 38.265 -1.234 8.166 1.00 18.93 O ATOM 1808 CB GLN A 221 40.401 -0.849 10.661 1.00 24.11 C ATOM 1809 CG GLN A 221 41.920 -0.892 10.768 1.00 28.69 C ATOM 1810 CD GLN A 221 42.524 0.412 11.280 1.00 30.49 C ATOM 1811 OE1 GLN A 221 41.913 1.130 12.080 1.00 29.51 O ATOM 1812 NE2 GLN A 221 43.735 0.720 10.818 1.00 31.46 N ATOM 1813 N ASP A 222 37.501 0.005 9.890 1.00 18.01 N ATOM 1814 CA ASP A 222 36.098 -0.314 9.638 1.00 18.68 C ATOM 1815 C ASP A 222 35.758 0.222 8.257 1.00 18.90 C ATOM 1816 O ASP A 222 35.058 -0.420 7.476 1.00 18.54 O ATOM 1817 CB ASP A 222 35.185 0.371 10.659 1.00 19.86 C ATOM 1818 CG ASP A 222 35.194 -0.312 12.011 1.00 22.12 C ATOM 1819 OD1 ASP A 222 35.703 -1.445 12.112 1.00 22.15 O ATOM 1820 OD2 ASP A 222 34.689 0.294 12.977 1.00 22.41 O ATOM 1821 N TYR A 223 36.260 1.420 7.976 1.00 18.51 N ATOM 1822 CA TYR A 223 36.031 2.087 6.702 1.00 18.08 C ATOM 1823 C TYR A 223 36.590 1.272 5.539 1.00 18.02 C ATOM 1824 O TYR A 223 35.929 1.075 4.522 1.00 18.03 O ATOM 1825 CB TYR A 223 36.685 3.471 6.732 1.00 18.31 C ATOM 1826 CG TYR A 223 36.810 4.111 5.378 1.00 19.01 C ATOM 1827 CD1 TYR A 223 35.731 4.779 4.804 1.00 20.05 C ATOM 1828 CD2 TYR A 223 37.999 4.032 4.658 1.00 19.68 C ATOM 1829 CE1 TYR A 223 35.831 5.353 3.542 1.00 20.77 C ATOM 1830 CE2 TYR A 223 38.111 4.602 3.397 1.00 21.33 C ATOM 1831 CZ TYR A 223 37.020 5.261 2.848 1.00 21.60 C ATOM 1832 OH TYR A 223 37.122 5.827 1.603 1.00 26.51 O ATOM 1833 N ARG A 224 37.822 0.806 5.688 1.00 18.72 N ATOM 1834 CA ARG A 224 38.457 0.021 4.640 1.00 20.25 C ATOM 1835 C ARG A 224 37.697 -1.280 4.370 1.00 20.61 C ATOM 1836 O ARG A 224 37.516 -1.678 3.220 1.00 20.33 O ATOM 1837 CB ARG A 224 39.911 -0.270 5.027 1.00 20.64 C ATOM 1838 CG ARG A 224 40.813 0.932 4.831 1.00 20.52 C ATOM 1839 CD ARG A 224 42.095 0.846 5.636 1.00 19.21 C ATOM 1840 NE ARG A 224 42.841 2.102 5.569 1.00 19.42 N ATOM 1841 CZ ARG A 224 43.875 2.401 6.353 1.00 22.53 C ATOM 1842 NH1 ARG A 224 44.285 1.527 7.270 1.00 20.16 N ATOM 1843 NH2 ARG A 224 44.492 3.572 6.231 1.00 19.75 N ATOM 1844 N LYS A 225 37.248 -1.937 5.432 1.00 21.09 N ATOM 1845 CA LYS A 225 36.507 -3.181 5.284 1.00 22.13 C ATOM 1846 C LYS A 225 35.192 -2.954 4.546 1.00 21.58 C ATOM 1847 O LYS A 225 34.825 -3.734 3.672 1.00 21.37 O ATOM 1848 CB LYS A 225 36.249 -3.798 6.658 1.00 23.86 C ATOM 1849 CG LYS A 225 37.467 -4.516 7.211 1.00 28.40 C ATOM 1850 CD LYS A 225 37.362 -4.788 8.698 1.00 33.10 C ATOM 1851 CE LYS A 225 38.642 -5.439 9.206 1.00 36.49 C ATOM 1852 NZ LYS A 225 38.491 -5.999 10.578 1.00 40.03 N ATOM 1853 N LEU A 226 34.487 -1.881 4.897 1.00 20.74 N ATOM 1854 CA LEU A 226 33.215 -1.559 4.258 1.00 20.38 C ATOM 1855 C LEU A 226 33.407 -1.285 2.772 1.00 21.19 C ATOM 1856 O LEU A 226 32.600 -1.702 1.944 1.00 20.39 O ATOM 1857 CB LEU A 226 32.578 -0.327 4.910 1.00 19.91 C ATOM 1858 CG LEU A 226 31.315 0.207 4.223 1.00 20.08 C ATOM 1859 CD1 LEU A 226 30.227 -0.865 4.234 1.00 19.98 C ATOM 1860 CD2 LEU A 226 30.833 1.465 4.940 1.00 19.99 C ATOM 1861 N GLU A 227 34.474 -0.568 2.440 1.00 21.44 N ATOM 1862 CA GLU A 227 34.752 -0.245 1.051 1.00 23.75 C ATOM 1863 C GLU A 227 34.885 -1.539 0.263 1.00 24.85 C ATOM 1864 O GLU A 227 34.361 -1.659 -0.842 1.00 25.24 O ATOM 1865 CB GLU A 227 36.041 0.577 0.945 1.00 24.04 C ATOM 1866 CG GLU A 227 35.865 2.050 1.310 1.00 26.01 C ATOM 1867 CD GLU A 227 35.136 2.855 0.235 1.00 27.67 C ATOM 1868 OE1 GLU A 227 35.622 3.953 -0.111 1.00 29.13 O ATOM 1869 OE2 GLU A 227 34.081 2.402 -0.261 1.00 28.50 O ATOM 1870 N GLU A 228 35.583 -2.507 0.847 1.00 27.34 N ATOM 1871 CA GLU A 228 35.783 -3.801 0.207 1.00 30.66 C ATOM 1872 C GLU A 228 34.437 -4.484 -0.005 1.00 30.33 C ATOM 1873 O GLU A 228 34.185 -5.084 -1.051 1.00 30.51 O ATOM 1874 CB GLU A 228 36.688 -4.687 1.070 1.00 34.28 C ATOM 1875 CG GLU A 228 37.403 -5.805 0.311 1.00 43.34 C ATOM 1876 CD GLU A 228 37.742 -5.432 -1.134 1.00 48.66 C ATOM 1877 OE1 GLU A 228 38.322 -4.342 -1.353 1.00 50.85 O ATOM 1878 OE2 GLU A 228 37.429 -6.231 -2.050 1.00 51.93 O ATOM 1879 N ILE A 229 33.571 -4.390 0.997 1.00 29.54 N ATOM 1880 CA ILE A 229 32.253 -4.989 0.905 1.00 28.20 C ATOM 1881 C ILE A 229 31.446 -4.312 -0.197 1.00 29.18 C ATOM 1882 O ILE A 229 30.866 -4.981 -1.051 1.00 30.26 O ATOM 1883 CB ILE A 229 31.495 -4.867 2.236 1.00 26.17 C ATOM 1884 CG1 ILE A 229 32.178 -5.732 3.291 1.00 24.19 C ATOM 1885 CG2 ILE A 229 30.048 -5.308 2.060 1.00 25.74 C ATOM 1886 CD1 ILE A 229 31.675 -5.500 4.693 1.00 23.87 C ATOM 1887 N LEU A 230 31.419 -2.985 -0.188 1.00 29.67 N ATOM 1888 CA LEU A 230 30.665 -2.249 -1.194 1.00 32.34 C ATOM 1889 C LEU A 230 31.228 -2.460 -2.607 1.00 35.80 C ATOM 1890 O LEU A 230 30.530 -2.237 -3.597 1.00 37.25 O ATOM 1891 CB LEU A 230 30.621 -0.759 -0.830 1.00 29.66 C ATOM 1892 CG LEU A 230 29.925 -0.437 0.500 1.00 27.34 C ATOM 1893 CD1 LEU A 230 29.695 1.056 0.607 1.00 26.65 C ATOM 1894 CD2 LEU A 230 28.600 -1.183 0.600 1.00 25.09 C ATOM 1895 N LYS A 231 32.482 -2.903 -2.693 1.00 37.91 N ATOM 1896 CA LYS A 231 33.140 -3.178 -3.975 1.00 40.97 C ATOM 1897 C LYS A 231 32.883 -2.147 -5.074 1.00 44.05 C ATOM 1898 O LYS A 231 32.400 -1.037 -4.757 1.00 47.34 O ATOM 1899 CB LYS A 231 32.723 -4.561 -4.481 1.00 39.81 C ATOM 1900 CG LYS A 231 32.751 -5.611 -3.403 1.00 39.28 C ATOM 1901 CD LYS A 231 32.564 -6.998 -3.958 1.00 39.45 C ATOM 1902 CE LYS A 231 31.788 -7.852 -2.978 1.00 39.24 C ATOM 1903 NZ LYS A 231 31.511 -9.201 -3.533 1.00 41.39 N TER 1904 LYS A 231 HETATM 1905 O HOH A1001 8.042 8.922 -0.595 1.00 16.25 O HETATM 1906 O HOH A1002 31.443 18.932 0.493 1.00 14.46 O HETATM 1907 O HOH A1003 19.734 2.421 18.548 1.00 16.09 O HETATM 1908 O HOH A1004 23.296 24.779 -0.833 1.00 18.08 O HETATM 1909 O HOH A1005 19.943 7.718 17.614 1.00 15.02 O HETATM 1910 O HOH A1006 24.603 24.823 34.023 1.00 16.47 O HETATM 1911 O HOH A1007 36.416 10.506 2.052 1.00 16.32 O HETATM 1912 O HOH A1008 26.247 1.928 21.960 1.00 17.84 O HETATM 1913 O HOH A1009 40.665 13.999 5.815 1.00 19.86 O HETATM 1914 O HOH A1010 10.361 -4.970 28.909 1.00 18.62 O HETATM 1915 O HOH A1011 34.624 14.518 11.880 1.00 21.54 O HETATM 1916 O HOH A1012 30.369 19.407 11.132 1.00 18.01 O HETATM 1917 O HOH A1013 14.379 -10.683 28.292 1.00 19.28 O HETATM 1918 O HOH A1014 25.483 6.341 5.495 1.00 17.05 O HETATM 1919 O HOH A1015 24.051 22.059 -3.857 1.00 18.46 O HETATM 1920 O HOH A1016 7.627 8.423 27.404 1.00 22.30 O HETATM 1921 O HOH A1017 20.194 25.930 6.974 1.00 19.81 O HETATM 1922 O HOH A1018 36.931 17.001 2.462 1.00 20.38 O HETATM 1923 O HOH A1019 38.059 11.314 4.219 1.00 18.84 O HETATM 1924 O HOH A1020 10.736 2.254 28.553 1.00 19.75 O HETATM 1925 O HOH A1021 21.498 -7.523 14.905 1.00 24.70 O HETATM 1926 O HOH A1022 16.375 14.570 35.218 1.00 23.77 O HETATM 1927 O HOH A1023 19.347 13.420 33.550 1.00 19.02 O HETATM 1928 O HOH A1024 11.688 -0.064 10.245 1.00 21.50 O HETATM 1929 O HOH A1025 17.506 25.086 22.077 1.00 23.13 O HETATM 1930 O HOH A1026 33.016 14.328 0.815 1.00 20.67 O HETATM 1931 O HOH A1027 22.307 28.712 25.954 1.00 28.80 O HETATM 1932 O HOH A1028 23.412 5.906 12.205 1.00 26.66 O HETATM 1933 O HOH A1029 30.469 15.035 10.611 1.00 22.01 O HETATM 1934 O HOH A1030 30.291 -0.567 27.599 1.00 23.21 O HETATM 1935 O HOH A1031 22.693 6.572 20.225 1.00 23.66 O HETATM 1936 O HOH A1032 19.047 -10.226 20.794 1.00 22.41 O HETATM 1937 O HOH A1033 27.048 18.567 26.580 1.00 25.96 O HETATM 1938 O HOH A1034 28.507 19.516 21.596 1.00 26.97 O HETATM 1939 O HOH A1035 39.371 15.371 13.351 1.00 21.67 O HETATM 1940 O HOH A1036 15.184 24.004 19.933 1.00 28.58 O HETATM 1941 O HOH A1037 9.383 15.564 7.214 1.00 22.22 O HETATM 1942 O HOH A1038 11.439 1.251 6.237 1.00 21.58 O HETATM 1943 O HOH A1039 22.898 27.716 13.291 1.00 29.95 O HETATM 1944 O HOH A1040 8.721 0.387 18.093 1.00 25.23 O HETATM 1945 O HOH A1041 25.048 9.772 20.636 1.00 22.62 O HETATM 1946 O HOH A1042 9.490 5.250 -1.571 1.00 26.22 O HETATM 1947 O HOH A1043 21.944 6.633 -1.874 1.00 23.55 O HETATM 1948 O HOH A1044 12.246 -9.868 23.684 1.00 23.55 O HETATM 1949 O HOH A1045 9.114 19.963 27.976 1.00 42.43 O HETATM 1950 O HOH A1046 34.640 5.907 -1.955 1.00 25.75 O HETATM 1951 O HOH A1047 34.106 16.005 18.666 1.00 33.07 O HETATM 1952 O HOH A1048 40.041 20.505 4.728 1.00 26.88 O HETATM 1953 O HOH A1049 30.775 -11.694 25.786 1.00 26.80 O HETATM 1954 O HOH A1050 31.421 -2.645 11.947 1.00 29.11 O HETATM 1955 O HOH A1051 12.271 22.792 31.868 1.00 32.07 O HETATM 1956 O HOH A1052 29.731 -8.105 16.555 1.00 26.58 O HETATM 1957 O HOH A1053 19.593 28.735 -1.490 1.00 24.64 O HETATM 1958 O HOH A1054 27.140 27.201 26.488 1.00 31.78 O HETATM 1959 O HOH A1055 22.260 2.135 33.818 1.00 32.40 O HETATM 1960 O HOH A1056 36.038 23.480 11.690 1.00 26.68 O HETATM 1961 O HOH A1057 27.520 11.232 14.687 1.00 25.66 O HETATM 1962 O HOH A1058 3.689 11.545 18.956 1.00 37.31 O HETATM 1963 O HOH A1059 24.647 -1.167 0.398 1.00 27.84 O HETATM 1964 O HOH A1060 21.796 3.098 0.187 1.00 23.98 O HETATM 1965 O HOH A1061 41.095 5.240 12.577 1.00 25.77 O HETATM 1966 O HOH A1062 8.603 -9.260 29.949 1.00 25.41 O HETATM 1967 O HOH A1063 34.071 23.918 19.729 1.00 29.99 O HETATM 1968 O HOH A1064 15.977 -1.173 2.487 1.00 32.20 O HETATM 1969 O HOH A1065 27.140 7.818 31.994 1.00 31.95 O HETATM 1970 O HOH A1066 10.487 18.436 21.411 1.00 27.02 O HETATM 1971 O HOH A1067 30.826 -7.682 33.607 1.00 30.85 O HETATM 1972 O HOH A1068 36.810 22.722 4.748 1.00 26.29 O HETATM 1973 O HOH A1069 27.150 -4.827 10.093 1.00 39.19 O HETATM 1974 O HOH A1070 15.424 9.956 -1.706 1.00 30.13 O HETATM 1975 O HOH A1071 22.854 27.617 0.069 1.00 32.95 O HETATM 1976 O HOH A1072 28.906 16.345 32.509 1.00 30.11 O HETATM 1977 O HOH A1073 40.949 20.635 9.956 1.00 36.23 O HETATM 1978 O HOH A1074 26.471 4.898 16.153 1.00 30.28 O HETATM 1979 O HOH A1075 2.778 15.544 24.412 1.00 40.90 O HETATM 1980 O HOH A1076 19.960 3.656 34.109 1.00 31.68 O HETATM 1981 O HOH A1077 5.249 13.893 28.485 1.00 37.03 O HETATM 1982 O HOH A1078 39.352 -1.143 1.050 1.00 33.83 O HETATM 1983 O HOH A1079 6.700 17.119 22.934 1.00 33.65 O HETATM 1984 O HOH A1080 13.610 -2.345 10.731 1.00 35.51 O HETATM 1985 O HOH A1081 7.650 16.994 3.124 1.00 38.59 O HETATM 1986 O HOH A1082 26.232 14.884 35.057 1.00 41.70 O HETATM 1987 O HOH A1083 33.425 25.389 12.477 1.00 30.89 O HETATM 1988 O HOH A1084 17.382 24.632 3.246 1.00 31.28 O HETATM 1989 O HOH A1085 11.387 2.114 31.782 1.00 35.17 O HETATM 1990 O HOH A1086 0.973 3.372 13.032 1.00 29.94 O HETATM 1991 O HOH A1087 27.587 -7.479 11.449 1.00 37.97 O HETATM 1992 O HOH A1088 26.946 5.051 -4.413 1.00 35.58 O HETATM 1993 O HOH A1089 26.518 26.482 9.280 1.00 32.79 O HETATM 1994 O HOH A1090 8.541 3.695 31.819 1.00 35.35 O HETATM 1995 O HOH A1091 14.276 11.077 36.328 1.00 29.80 O HETATM 1996 O HOH A1092 3.032 0.179 22.483 1.00 36.43 O HETATM 1997 O HOH A1093 6.183 11.950 5.818 1.00 39.24 O HETATM 1998 O HOH A1094 23.154 27.421 7.271 1.00 39.54 O HETATM 1999 O HOH A1095 26.118 2.735 34.326 1.00 42.38 O HETATM 2000 O HOH A1096 25.973 -3.150 -1.456 1.00 38.72 O HETATM 2001 O HOH A1097 20.353 16.975 35.522 1.00 40.18 O HETATM 2002 O HOH A1098 30.289 4.873 28.404 1.00 43.69 O HETATM 2003 O HOH A1099 16.635 -5.344 9.787 1.00 33.97 O HETATM 2004 O HOH A1100 28.223 18.279 37.338 1.00 47.60 O HETATM 2005 O HOH A1101 27.230 -3.846 36.617 1.00 49.45 O HETATM 2006 O HOH A1102 29.753 0.417 17.515 1.00 42.46 O HETATM 2007 O HOH A1103 18.843 7.097 -3.773 1.00 36.15 O HETATM 2008 O HOH A1104 7.075 6.297 1.112 1.00 35.40 O HETATM 2009 O HOH A1105 26.750 1.802 -1.886 1.00 37.84 O HETATM 2010 O HOH A1106 6.513 5.902 23.911 1.00 33.11 O HETATM 2011 O HOH A1107 8.143 14.366 34.202 1.00 46.80 O HETATM 2012 O HOH A1108 16.472 25.061 12.328 1.00 35.93 O HETATM 2013 O HOH A1109 33.767 -1.203 27.365 1.00 42.94 O HETATM 2014 O HOH A1110 21.779 8.811 -5.575 1.00 32.56 O HETATM 2015 O HOH A1111 6.124 -0.973 32.303 1.00 41.12 O HETATM 2016 O HOH A1112 25.101 -9.300 14.782 1.00 34.64 O HETATM 2017 O HOH A1113 36.340 25.258 18.128 1.00 43.98 O HETATM 2018 O HOH A1114 12.569 13.575 37.356 1.00 46.87 O HETATM 2019 O HOH A1115 34.237 17.069 22.415 1.00 41.55 O HETATM 2020 O HOH A1116 23.177 15.068 34.422 1.00 42.38 O HETATM 2021 O HOH A1117 9.555 -1.814 18.384 1.00 30.37 O HETATM 2022 O HOH A1118 30.392 11.090 30.114 1.00 45.19 O HETATM 2023 O HOH A1119 34.080 -2.203 18.604 1.00 39.67 O HETATM 2024 O HOH A1120 7.624 -3.348 -0.855 1.00 56.92 O HETATM 2025 O HOH A1121 33.795 0.581 -2.299 1.00 27.54 O HETATM 2026 O HOH A1122 15.451 -10.936 21.831 1.00 43.40 O HETATM 2027 O HOH A1123 15.456 12.221 38.918 1.00 54.39 O HETATM 2028 O HOH A1124 41.005 -0.739 14.484 1.00 46.03 O HETATM 2029 O HOH A1125 31.678 6.734 22.561 1.00 48.85 O HETATM 2030 O HOH A1126 32.456 16.566 11.635 1.00 54.74 O HETATM 2031 O HOH A1127 32.182 -10.721 23.194 1.00 38.93 O HETATM 2032 O HOH A1128 5.300 25.612 18.294 1.00 64.82 O HETATM 2033 O HOH A1129 32.131 11.649 -5.304 1.00 40.05 O HETATM 2034 O HOH A1130 28.508 -0.402 -6.336 1.00 45.84 O HETATM 2035 O HOH A1131 23.697 29.316 -2.386 1.00 44.01 O HETATM 2036 O HOH A1132 38.005 3.475 17.251 1.00 47.02 O HETATM 2037 O HOH A1133 6.550 15.341 5.337 1.00 37.61 O HETATM 2038 O HOH A1134 37.021 -0.443 14.721 1.00 47.81 O HETATM 2039 O HOH A1135 2.842 7.587 21.990 1.00 51.84 O HETATM 2040 O HOH A1136 18.939 7.425 37.205 1.00 40.91 O HETATM 2041 O HOH A1137 3.929 -2.343 26.075 1.00 46.07 O HETATM 2042 O HOH A1138 27.774 2.124 -8.380 1.00 58.35 O HETATM 2043 O HOH A1139 9.244 -11.587 22.613 1.00 43.40 O HETATM 2044 O HOH A1140 15.552 -2.448 8.779 1.00 42.96 O HETATM 2045 O HOH A1141 -1.746 5.909 23.723 1.00 51.73 O HETATM 2046 O HOH A1142 35.928 -6.273 3.911 1.00 39.46 O HETATM 2047 O HOH A1143 15.072 17.764 3.342 1.00 41.27 O HETATM 2048 O HOH A1144 24.358 -7.215 3.105 1.00 63.20 O HETATM 2049 O HOH A1145 1.125 16.308 35.817 1.00 60.97 O HETATM 2050 O HOH A1146 43.716 26.358 14.233 1.00 56.43 O HETATM 2051 O HOH A1147 32.702 -3.501 30.319 1.00 37.78 O HETATM 2052 O HOH A1148 23.809 -6.360 -3.743 1.00 49.58 O HETATM 2053 O HOH A1149 16.124 24.981 17.382 1.00 49.75 O HETATM 2054 O HOH A1150 30.015 3.899 21.074 1.00 48.08 O HETATM 2055 O HOH A1151 31.720 -1.924 15.784 1.00 50.94 O HETATM 2056 O HOH A1152 21.814 29.508 9.248 1.00 51.45 O HETATM 2057 O HOH A1153 39.897 -11.926 -6.842 1.00 44.54 O HETATM 2058 O HOH A1154 41.055 -3.112 6.993 1.00 43.84 O HETATM 2059 O HOH A1155 32.495 -9.497 16.763 1.00 42.02 O HETATM 2060 O HOH A1156 37.576 -10.675 14.226 1.00 49.07 O HETATM 2061 O HOH A1157 37.124 -9.157 7.627 1.00 57.29 O HETATM 2062 O HOH A1158 36.667 28.614 6.086 1.00 52.09 O HETATM 2063 O HOH A1159 24.956 10.938 34.612 1.00 42.27 O HETATM 2064 O HOH A1160 14.951 -15.172 -6.108 1.00 52.82 O HETATM 2065 O HOH A1161 29.805 30.993 17.335 1.00 54.13 O HETATM 2066 O HOH A1162 -0.384 2.493 23.766 1.00 43.47 O HETATM 2067 O HOH A1163 9.274 -3.803 10.660 1.00 40.88 O HETATM 2068 O HOH A1164 7.335 5.497 42.640 1.00 53.79 O HETATM 2069 O HOH A1165 4.372 -6.596 12.331 1.00 54.06 O HETATM 2070 O HOH A1166 -0.486 -5.648 17.087 1.00 47.07 O HETATM 2071 O HOH A1167 43.829 -1.614 7.683 1.00 40.16 O HETATM 2072 O HOH A1168 27.873 10.401 33.587 1.00 43.21 O HETATM 2073 O HOH A1169 36.953 -12.612 -8.793 1.00 63.51 O HETATM 2074 O HOH A1170 25.397 -0.232 38.837 1.00 45.12 O HETATM 2075 O HOH A1171 1.449 -6.976 24.115 1.00 55.67 O HETATM 2076 O HOH A1172 20.037 27.154 22.069 1.00 42.07 O HETATM 2077 O HOH A1173 23.648 7.411 45.064 1.00 62.37 O HETATM 2078 O HOH A1174 33.110 28.782 21.511 1.00 53.28 O HETATM 2079 O HOH A1175 37.922 18.863 25.835 1.00 50.06 O HETATM 2080 O HOH A1176 22.390 14.950 39.305 1.00 53.02 O HETATM 2081 O HOH A1177 20.663 5.158 18.891 1.00 15.11 O HETATM 2082 O HOH A1178 22.388 8.784 18.576 1.00 18.98 O HETATM 2083 O HOH A1179 19.522 7.784 23.376 1.00 18.04 O HETATM 2084 O HOH A1180 26.895 10.687 17.370 1.00 29.01 O HETATM 2085 O HOH A1181 33.245 17.026 1.586 1.00 15.06 O HETATM 2086 O HOH A1182 25.688 26.748 -0.579 1.00 42.87 O HETATM 2087 O HOH A1183 24.349 24.721 -4.148 1.00 25.77 O HETATM 2088 O HOH A1184 37.315 8.267 1.009 1.00 30.16 O HETATM 2089 O HOH A1185 35.237 12.818 1.071 1.00 35.87 O HETATM 2090 O HOH A1186 44.320 12.098 5.840 1.00 43.40 O HETATM 2091 O HOH A1187 7.132 -3.761 30.509 1.00 31.06 O HETATM 2092 O HOH A1188 23.509 4.844 5.112 1.00 26.29 O HETATM 2093 O HOH A1189 23.281 3.207 2.634 1.00 31.82 O HETATM 2094 O HOH A1190 20.654 5.650 0.295 1.00 22.43 O HETATM 2095 O HOH A1191 18.253 5.169 -1.548 1.00 25.24 O HETATM 2096 O HOH A1192 14.302 3.581 0.286 1.00 31.97 O HETATM 2097 O HOH A1193 11.716 3.843 -1.903 1.00 40.24 O HETATM 2098 O HOH A1194 18.582 27.009 5.441 1.00 39.68 O HETATM 2099 O HOH A1195 38.512 19.615 2.142 1.00 28.77 O HETATM 2100 O HOH A1196 18.203 16.146 33.825 1.00 20.87 O HETATM 2101 O HOH A1197 21.934 12.946 33.090 1.00 25.45 O HETATM 2102 O HOH A1198 10.609 -0.704 7.966 1.00 28.09 O HETATM 2103 O HOH A1199 13.988 15.607 36.371 1.00 48.58 O HETATM 2104 O HOH A1200 12.292 17.236 34.808 1.00 36.49 O HETATM 2105 O HOH A1201 13.328 21.216 33.542 1.00 30.18 O HETATM 2106 O HOH A1202 10.220 -0.843 12.125 1.00 40.33 O HETATM 2107 O HOH A1203 19.734 28.510 25.820 1.00 35.66 O HETATM 2108 O HOH A1204 6.704 6.619 3.501 1.00 37.58 O HETATM 2109 O HOH A1205 30.916 -2.506 25.826 1.00 39.16 O HETATM 2110 O HOH A1206 26.773 3.125 18.344 1.00 40.74 O HETATM 2111 O HOH A1207 25.799 1.147 15.502 1.00 36.50 O HETATM 2112 O HOH A1208 23.215 2.737 -2.311 1.00 45.18 O HETATM 2113 O HOH A1209 23.266 5.187 -3.545 1.00 42.97 O HETATM 2114 O HOH A1210 19.997 5.414 -5.301 1.00 47.88 O HETATM 2115 O HOH A1211 12.364 -11.594 26.654 1.00 27.02 O HETATM 2116 O HOH A1212 27.169 29.350 24.930 1.00 42.78 O HETATM 2117 O HOH A1213 26.363 27.559 21.096 1.00 47.05 O HETATM 2118 O HOH A1214 26.237 27.511 18.161 1.00 36.20 O HETATM 2119 O HOH A1215 34.788 25.442 10.513 1.00 38.11 O HETATM 2120 O HOH A1216 35.058 26.376 14.317 1.00 44.66 O HETATM 2121 O HOH A1217 6.907 -8.234 28.731 1.00 37.35 O HETATM 2122 O HOH A1218 8.802 18.914 23.109 1.00 33.00 O HETATM 2123 O HOH A1219 25.556 -6.767 32.733 1.00 21.44 O HETATM 2124 O HOH A1220 11.207 0.721 33.906 1.00 50.45 O HETATM 2125 O HOH A1221 28.562 5.840 -5.772 1.00 38.94 O HETATM 2126 O HOH A1222 27.480 25.029 7.290 1.00 24.77 O HETATM 2127 O HOH A1223 14.717 8.534 37.498 1.00 44.96 O HETATM 2128 O HOH A1224 26.399 -5.493 -0.450 1.00 57.19 O HETATM 2129 O HOH A1225 31.688 1.817 28.868 1.00 49.85 O HETATM 2130 O HOH A1226 12.842 -11.350 19.466 1.00 36.33 O HETATM 2131 O HOH A1227 14.604 20.002 5.495 1.00 31.50 O HETATM 2132 O HOH A1228 4.106 2.609 26.386 1.00 39.57 O HETATM 2133 O HOH A1229 5.307 -4.099 22.664 1.00 35.53 O HETATM 2134 O HOH A1230 29.510 13.097 21.720 1.00 49.45 O HETATM 2135 O HOH A1231 -4.125 22.000 14.920 1.00 48.75 O HETATM 2136 O HOH A1232 5.793 16.015 34.080 1.00 47.94 O HETATM 2137 O HOH A1233 22.584 27.766 23.265 1.00 31.48 O HETATM 2138 O HOH A1234 20.259 1.009 -1.025 1.00 49.42 O HETATM 2139 O HOH A1235 32.924 27.572 8.197 1.00 31.70 O HETATM 2140 O HOH A1236 7.278 7.812 12.300 1.00 47.74 O HETATM 2141 O HOH A1237 32.586 -1.616 20.140 1.00 41.69 O CONECT 915 921 CONECT 921 915 922 CONECT 922 921 923 925 CONECT 923 922 924 929 CONECT 924 923 CONECT 925 922 926 CONECT 926 925 927 CONECT 927 926 928 CONECT 928 927 CONECT 929 923 CONECT 1579 1585 CONECT 1585 1579 1586 CONECT 1586 1585 1587 1589 CONECT 1587 1586 1588 1593 CONECT 1588 1587 CONECT 1589 1586 1590 CONECT 1590 1589 1591 CONECT 1591 1590 1592 CONECT 1592 1591 CONECT 1593 1587 MASTER 284 0 2 11 15 0 0 6 2140 1 20 20 END