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*** lao ***elNémo ID: 2610161505131593904Job options:ID = 2610161505131593904 JOBID = lao USERID = unknown PRIVAT = 0 NMODES = 5 DQMIN = -100 DQMAX = 100 DQSTEP = 20 DOGRAPHS = on DOPROJMODS = on DORMSD = on NRBL = 0 CUTOFF = 0 CAONLY = 0 Input data for this run:HEADER lao HEADER AMINO-ACID BINDING PROTEIN 25-FEB-93 2LAO TITLE THREE-DIMENSIONAL STRUCTURES OF THE PERIPLASMIC LYSINE-, ARGININE-, TITLE 2 ORNITHINE-BINDING PROTEIN WITH AND WITHOUT A LIGAND COMPND MOL_ID: 1; COMPND 2 MOLECULE: LYSINE, ARGININE, ORNITHINE-BINDING PROTEIN; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SALMONELLA TYPHIMURIUM; SOURCE 3 ORGANISM_TAXID: 602 KEYWDS AMINO-ACID BINDING PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR S.-H.KIM,B.-H.OH,C.-H.KANG REVDAT 5 06-NOV-24 2LAO 1 SEQADV REVDAT 4 29-NOV-17 2LAO 1 HELIX REVDAT 3 24-FEB-09 2LAO 1 VERSN REVDAT 2 01-APR-03 2LAO 1 JRNL REVDAT 1 22-JUN-94 2LAO 0 JRNL AUTH B.H.OH,J.PANDIT,C.H.KANG,K.NIKAIDO,S.GOKCEN,G.F.AMES,S.H.KIM JRNL TITL THREE-DIMENSIONAL STRUCTURES OF THE PERIPLASMIC JRNL TITL 2 LYSINE/ARGININE/ORNITHINE-BINDING PROTEIN WITH AND WITHOUT A JRNL TITL 3 LIGAND. JRNL REF J.BIOL.CHEM. V. 268 11348 1993 JRNL REFN ISSN 0021-9258 JRNL PMID 8496186 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH C.-H.KANG,W.-C.SHIN,Y.YAMAGATA,S.GOKCEN,G.F.-L.AMES,S.-H.KIM REMARK 1 TITL CRYSTAL STRUCTURE OF THE LYSINE-,ARGININE-, REMARK 1 TITL 2 ORNITHINE-BINDING PROTEIN FROM SALMONELLA TYPHIMURIUM AT 2.7 REMARK 1 TITL 3 ANGSTROMS RESOLUTION REMARK 1 REF J.BIOL.CHEM. V. 266 23893 1992 REMARK 1 REFN ISSN 0021-9258 REMARK 2 REMARK 2 RESOLUTION. 1.90 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 6.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000 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 : 22643 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : NULL REMARK 3 FREE R VALUE TEST SET SELECTION : NULL REMARK 3 R VALUE (WORKING SET) : 0.197 REMARK 3 FREE R VALUE : NULL 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 : 1822 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 89 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL 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) : 0.014 REMARK 3 BOND ANGLES (DEGREES) : 2.760 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 2LAO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL. REMARK 100 THE DEPOSITION ID IS D_1000178293. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : NULL REMARK 200 TEMPERATURE (KELVIN) : NULL REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : NULL REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : NULL REMARK 200 RADIATION SOURCE : NULL REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL REMARK 200 WAVELENGTH OR RANGE (A) : NULL REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : NULL REMARK 200 DETECTOR MANUFACTURER : NULL REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL REMARK 200 DATA SCALING SOFTWARE : NULL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL REMARK 200 RESOLUTION RANGE HIGH (A) : NULL REMARK 200 RESOLUTION RANGE LOW (A) : NULL REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : NULL REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : NULL REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: NULL REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL REMARK 200 SOFTWARE USED: X-PLOR REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 55.91 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.79 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: NULL 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 18.12500 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 51.09000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.26000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 51.09000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 18.12500 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 39.26000 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 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 GLN A 4 CG CD OE1 NE2 REMARK 470 LYS A 44 CG CD CE NZ REMARK 470 LYS A 225 CG CD CE NZ REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 HIS A 113 NE2 HIS A 113 CD2 -0.073 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 ARG A 7 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES REMARK 500 TRP A 47 CD1 - CG - CD2 ANGL. DEV. = 6.2 DEGREES REMARK 500 TRP A 47 CE2 - CD2 - CG ANGL. DEV. = -5.7 DEGREES REMARK 500 ARG A 77 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES REMARK 500 TRP A 130 CD1 - CG - CD2 ANGL. DEV. = 5.8 DEGREES REMARK 500 TRP A 130 CE2 - CD2 - CG ANGL. DEV. = -5.6 DEGREES REMARK 500 ARG A 131 NE - CZ - NH1 ANGL. DEV. = 5.7 DEGREES REMARK 500 ARG A 131 NE - CZ - NH2 ANGL. DEV. = -5.1 DEGREES REMARK 500 LYS A 188 CA - CB - CG ANGL. DEV. = 13.2 DEGREES REMARK 500 ARG A 200 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES REMARK 500 TYR A 230 CB - CG - CD2 ANGL. DEV. = -3.8 DEGREES REMARK 500 REMARK 500 REMARK: NULL 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 THR A 12 32.24 -85.04 REMARK 500 SER A 69 51.60 -154.74 REMARK 500 TRP A 130 -51.90 -124.36 REMARK 500 PHE A 169 -49.83 -157.18 REMARK 500 ASP A 193 56.54 -114.35 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 TYR A 178 0.07 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 999 REMARK 999 SEQUENCE REMARK 999 SEQUENCE ADVISORY NOTICE: REMARK 999 DIFFERENCE BETWEEN SWISS-PROT AND PDB SEQUENCE. REMARK 999 REMARK 999 SWISS-PROT ENTRY NAME: ARGT_SALTY REMARK 999 REMARK 999 SWISS-PROT RESIDUE PDB SEQRES REMARK 999 NAME NUMBER NAME CHAIN SEQ/INSERT CODE REMARK 999 VAL 102 ILE 102 REMARK 999 REMARK 999 RESIDUE 102 OF THE LAO PROTEIN IS ISOLEUCINE, BUT WAS REMARK 999 REPORTED AS VALINE IN SWISS-PROT DATA BANK DUE TO REMARK 999 SEQUENCING ERROR (PERSONAL COMMUNICATION). DBREF 2LAO A 1 238 UNP P02911 ARGT_SALTY 23 260 SEQADV 2LAO ILE A 102 UNP P02911 VAL 124 CONFLICT SEQRES 1 A 238 ALA LEU PRO GLN THR VAL ARG ILE GLY THR ASP THR THR SEQRES 2 A 238 TYR ALA PRO PHE SER SER LYS ASP ALA LYS GLY GLU PHE SEQRES 3 A 238 ILE GLY PHE ASP ILE ASP LEU GLY ASN GLU MET CYS LYS SEQRES 4 A 238 ARG MET GLN VAL LYS CYS THR TRP VAL ALA SER ASP PHE SEQRES 5 A 238 ASP ALA LEU ILE PRO SER LEU LYS ALA LYS LYS ILE ASP SEQRES 6 A 238 ALA ILE ILE SER SER LEU SER ILE THR ASP LYS ARG GLN SEQRES 7 A 238 GLN GLU ILE ALA PHE SER ASP LYS LEU TYR ALA ALA ASP SEQRES 8 A 238 SER ARG LEU ILE ALA ALA LYS GLY SER PRO ILE GLN PRO SEQRES 9 A 238 THR LEU GLU SER LEU LYS GLY LYS HIS VAL GLY VAL LEU SEQRES 10 A 238 GLN GLY SER THR GLN GLU ALA TYR ALA ASN ASP ASN TRP SEQRES 11 A 238 ARG THR LYS GLY VAL ASP VAL VAL ALA TYR ALA ASN GLN SEQRES 12 A 238 ASP LEU ILE TYR SER ASP LEU THR ALA GLY ARG LEU ASP SEQRES 13 A 238 ALA ALA LEU GLN ASP GLU VAL ALA ALA SER GLU GLY PHE SEQRES 14 A 238 LEU LYS GLN PRO ALA GLY LYS GLU TYR ALA PHE ALA GLY SEQRES 15 A 238 PRO SER VAL LYS ASP LYS LYS TYR PHE GLY ASP GLY THR SEQRES 16 A 238 GLY VAL GLY LEU ARG LYS ASP ASP THR GLU LEU LYS ALA SEQRES 17 A 238 ALA PHE ASP LYS ALA LEU THR GLU LEU ARG GLN ASP GLY SEQRES 18 A 238 THR TYR ASP LYS MET ALA LYS LYS TYR PHE ASP PHE ASN SEQRES 19 A 238 VAL TYR GLY ASP FORMUL 2 HOH *89(H2 O) HELIX 1 A PHE A 29 MET A 41 1 13 HELIX 2 B LEU A 55 LYS A 60 1 6 HELIX 3 C ASP A 75 GLU A 80 1 6 HELIX 4 D LEU A 106 LEU A 109 1 4 HELIX 5 E THR A 121 ASN A 129 1 9 HELIX 6 F GLN A 143 THR A 151 1 9 HELIX 7 G GLU A 162 GLY A 168 1 7 HELIX 8 H LYS A 188 PHE A 191 1 4 HELIX 9 I THR A 204 GLN A 219 1 16 HELIX 10 J THR A 222 LYS A 228 1 7 SHEET 1 1 5 LYS A 44 ALA A 49 0 SHEET 2 1 5 THR A 5 THR A 10 1 SHEET 3 1 5 ALA A 66 ILE A 67 1 SHEET 4 1 5 VAL A 197 LEU A 199 -1 SHEET 5 1 5 ALA A 82 SER A 84 1 SHEET 1 2 5 ASP A 136 TYR A 140 0 SHEET 2 2 5 HIS A 113 LEU A 117 1 SHEET 3 2 5 ALA A 157 ASP A 161 1 SHEET 4 2 5 SER A 92 ALA A 97 -1 SHEET 5 2 5 TYR A 178 ALA A 181 1 SSBOND 1 CYS A 38 CYS A 45 1555 1555 2.31 CISPEP 1 ALA A 15 PRO A 16 0 -1.71 CRYST1 36.250 78.520 102.180 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 0.027586 0.000000 0.000000 0.00000 SCALE2 0.000000 0.012736 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009787 0.00000 ATOM 1 N ALA A 1 51.436 44.270 10.041 1.00 53.66 N ATOM 2 CA ALA A 1 50.955 44.766 8.768 1.00 53.06 C ATOM 3 C ALA A 1 49.537 45.148 9.133 1.00 53.22 C ATOM 4 O ALA A 1 48.970 44.538 10.055 1.00 55.56 O ATOM 5 CB ALA A 1 50.876 43.697 7.677 1.00 50.98 C ATOM 6 N LEU A 2 48.955 46.154 8.482 1.00 51.61 N ATOM 7 CA LEU A 2 47.580 46.528 8.769 1.00 49.38 C ATOM 8 C LEU A 2 46.572 45.453 8.330 1.00 49.23 C ATOM 9 O LEU A 2 46.822 44.727 7.358 1.00 51.91 O ATOM 10 CB LEU A 2 47.330 47.867 8.085 1.00 45.80 C ATOM 11 CG LEU A 2 47.009 49.054 8.973 1.00 44.31 C ATOM 12 CD1 LEU A 2 47.905 49.032 10.197 1.00 43.56 C ATOM 13 CD2 LEU A 2 47.118 50.330 8.147 1.00 41.91 C ATOM 14 N PRO A 3 45.448 45.232 9.024 1.00 46.73 N ATOM 15 CA PRO A 3 44.455 44.250 8.616 1.00 45.78 C ATOM 16 C PRO A 3 43.961 44.634 7.234 1.00 46.63 C ATOM 17 O PRO A 3 43.939 45.825 6.898 1.00 47.34 O ATOM 18 CB PRO A 3 43.403 44.341 9.691 1.00 46.99 C ATOM 19 CG PRO A 3 44.105 44.975 10.878 1.00 44.71 C ATOM 20 CD PRO A 3 45.004 45.979 10.190 1.00 44.42 C ATOM 21 N GLN A 4 43.568 43.676 6.398 1.00 46.47 N ATOM 22 CA GLN A 4 43.029 44.060 5.087 1.00 46.45 C ATOM 23 C GLN A 4 41.693 44.761 5.297 1.00 45.04 C ATOM 24 O GLN A 4 41.393 45.774 4.661 1.00 45.78 O ATOM 25 CB GLN A 4 42.785 42.846 4.192 1.00 46.63 C ATOM 26 N THR A 5 40.909 44.192 6.215 1.00 42.61 N ATOM 27 CA THR A 5 39.653 44.771 6.594 1.00 40.11 C ATOM 28 C THR A 5 39.717 44.816 8.095 1.00 35.37 C ATOM 29 O THR A 5 40.067 43.791 8.671 1.00 35.94 O ATOM 30 CB THR A 5 38.484 43.884 6.138 1.00 43.37 C ATOM 31 OG1 THR A 5 38.691 43.602 4.741 1.00 47.16 O ATOM 32 CG2 THR A 5 37.113 44.565 6.389 1.00 45.85 C ATOM 33 N VAL A 6 39.468 45.951 8.737 1.00 32.53 N ATOM 34 CA VAL A 6 39.393 46.107 10.193 1.00 29.27 C ATOM 35 C VAL A 6 37.920 45.846 10.630 1.00 28.08 C ATOM 36 O VAL A 6 36.990 46.464 10.072 1.00 24.45 O ATOM 37 CB VAL A 6 39.897 47.581 10.531 1.00 30.89 C ATOM 38 CG1 VAL A 6 39.819 47.928 12.011 1.00 28.80 C ATOM 39 CG2 VAL A 6 41.390 47.680 10.213 1.00 30.39 C ATOM 40 N ARG A 7 37.656 44.914 11.569 1.00 23.76 N ATOM 41 CA ARG A 7 36.323 44.651 12.059 1.00 22.99 C ATOM 42 C ARG A 7 36.256 45.445 13.334 1.00 20.20 C ATOM 43 O ARG A 7 37.074 45.287 14.226 1.00 21.62 O ATOM 44 CB ARG A 7 36.054 43.177 12.407 1.00 26.36 C ATOM 45 CG ARG A 7 36.116 42.175 11.240 1.00 38.28 C ATOM 46 CD ARG A 7 35.565 40.781 11.633 1.00 47.23 C ATOM 47 NE ARG A 7 34.110 40.616 11.435 1.00 55.32 N ATOM 48 CZ ARG A 7 33.263 40.010 12.321 1.00 60.98 C ATOM 49 NH1 ARG A 7 33.642 39.474 13.504 1.00 58.63 N ATOM 50 NH2 ARG A 7 31.957 39.910 12.010 1.00 63.43 N ATOM 51 N ILE A 8 35.312 46.338 13.471 1.00 20.96 N ATOM 52 CA ILE A 8 35.204 47.178 14.635 1.00 22.87 C ATOM 53 C ILE A 8 33.926 46.777 15.348 1.00 22.26 C ATOM 54 O ILE A 8 32.866 46.797 14.708 1.00 23.20 O ATOM 55 CB ILE A 8 35.135 48.680 14.204 1.00 22.87 C ATOM 56 CG1 ILE A 8 36.277 49.011 13.235 1.00 20.30 C ATOM 57 CG2 ILE A 8 35.114 49.516 15.496 1.00 16.27 C ATOM 58 CD1 ILE A 8 36.390 50.441 12.691 1.00 26.69 C ATOM 59 N GLY A 9 33.991 46.442 16.631 1.00 19.88 N ATOM 60 CA GLY A 9 32.823 46.073 17.377 1.00 19.68 C ATOM 61 C GLY A 9 32.317 47.315 18.061 1.00 22.33 C ATOM 62 O GLY A 9 33.102 48.150 18.528 1.00 21.18 O ATOM 63 N THR A 10 30.995 47.414 18.136 1.00 22.30 N ATOM 64 CA THR A 10 30.341 48.509 18.821 1.00 24.40 C ATOM 65 C THR A 10 29.031 47.986 19.406 1.00 25.03 C ATOM 66 O THR A 10 28.469 47.013 18.915 1.00 27.09 O ATOM 67 CB THR A 10 30.144 49.663 17.786 1.00 21.31 C ATOM 68 OG1 THR A 10 29.779 50.822 18.536 1.00 22.42 O ATOM 69 CG2 THR A 10 29.143 49.323 16.709 1.00 20.91 C ATOM 70 N ASP A 11 28.585 48.544 20.515 1.00 25.18 N ATOM 71 CA ASP A 11 27.295 48.270 21.084 1.00 24.50 C ATOM 72 C ASP A 11 26.339 49.337 20.574 1.00 24.99 C ATOM 73 O ASP A 11 26.381 50.481 21.053 1.00 24.16 O ATOM 74 CB ASP A 11 27.398 48.334 22.599 1.00 26.75 C ATOM 75 CG ASP A 11 26.135 47.908 23.337 1.00 32.19 C ATOM 76 OD1 ASP A 11 25.054 47.833 22.743 1.00 40.44 O ATOM 77 OD2 ASP A 11 26.222 47.644 24.528 1.00 35.65 O ATOM 78 N THR A 12 25.357 48.982 19.747 1.00 27.78 N ATOM 79 CA THR A 12 24.471 49.998 19.169 1.00 27.66 C ATOM 80 C THR A 12 23.257 50.446 19.998 1.00 25.82 C ATOM 81 O THR A 12 22.179 50.779 19.515 1.00 25.56 O ATOM 82 CB THR A 12 24.025 49.491 17.779 1.00 29.46 C ATOM 83 OG1 THR A 12 23.332 48.262 17.935 1.00 30.47 O ATOM 84 CG2 THR A 12 25.224 49.323 16.868 1.00 28.48 C ATOM 85 N THR A 13 23.372 50.454 21.297 1.00 25.10 N ATOM 86 CA THR A 13 22.276 50.871 22.099 1.00 26.54 C ATOM 87 C THR A 13 22.679 52.159 22.793 1.00 29.29 C ATOM 88 O THR A 13 22.255 52.337 23.940 1.00 30.00 O ATOM 89 CB THR A 13 21.982 49.740 23.091 1.00 27.43 C ATOM 90 OG1 THR A 13 23.088 49.548 23.976 1.00 29.45 O ATOM 91 CG2 THR A 13 21.676 48.482 22.323 1.00 28.72 C ATOM 92 N TYR A 14 23.525 53.036 22.221 1.00 31.38 N ATOM 93 CA TYR A 14 23.948 54.240 22.921 1.00 32.43 C ATOM 94 C TYR A 14 23.982 55.502 22.064 1.00 30.15 C ATOM 95 O TYR A 14 25.033 56.076 21.740 1.00 27.41 O ATOM 96 CB TYR A 14 25.330 54.040 23.552 1.00 38.74 C ATOM 97 CG TYR A 14 25.618 55.130 24.591 1.00 49.54 C ATOM 98 CD1 TYR A 14 24.592 55.621 25.389 1.00 54.90 C ATOM 99 CD2 TYR A 14 26.887 55.643 24.757 1.00 51.65 C ATOM 100 CE1 TYR A 14 24.815 56.595 26.337 1.00 60.34 C ATOM 101 CE2 TYR A 14 27.123 56.620 25.709 1.00 58.41 C ATOM 102 CZ TYR A 14 26.089 57.090 26.494 1.00 62.02 C ATOM 103 OH TYR A 14 26.315 58.058 27.469 1.00 67.66 O ATOM 104 N ALA A 15 22.795 55.971 21.688 1.00 27.28 N ATOM 105 CA ALA A 15 22.695 57.227 20.989 1.00 28.02 C ATOM 106 C ALA A 15 23.226 58.278 21.957 1.00 27.58 C ATOM 107 O ALA A 15 23.183 58.065 23.171 1.00 29.46 O ATOM 108 CB ALA A 15 21.258 57.510 20.667 1.00 29.77 C ATOM 109 N PRO A 16 23.850 59.369 21.533 1.00 28.98 N ATOM 110 CA PRO A 16 24.140 59.693 20.144 1.00 27.18 C ATOM 111 C PRO A 16 25.448 59.112 19.606 1.00 24.48 C ATOM 112 O PRO A 16 25.915 59.544 18.540 1.00 23.71 O ATOM 113 CB PRO A 16 24.090 61.207 20.176 1.00 28.19 C ATOM 114 CG PRO A 16 24.818 61.508 21.465 1.00 25.75 C ATOM 115 CD PRO A 16 24.188 60.497 22.406 1.00 26.61 C ATOM 116 N PHE A 17 26.082 58.193 20.347 1.00 22.73 N ATOM 117 CA PHE A 17 27.356 57.640 19.911 1.00 23.93 C ATOM 118 C PHE A 17 27.218 56.447 18.970 1.00 24.39 C ATOM 119 O PHE A 17 27.823 56.461 17.890 1.00 22.15 O ATOM 120 CB PHE A 17 28.177 57.248 21.124 1.00 23.16 C ATOM 121 CG PHE A 17 28.417 58.454 21.995 1.00 26.16 C ATOM 122 CD1 PHE A 17 29.240 59.478 21.539 1.00 27.18 C ATOM 123 CD2 PHE A 17 27.821 58.516 23.240 1.00 24.91 C ATOM 124 CE1 PHE A 17 29.459 60.574 22.365 1.00 26.46 C ATOM 125 CE2 PHE A 17 28.042 59.607 24.059 1.00 27.30 C ATOM 126 CZ PHE A 17 28.865 60.632 23.623 1.00 26.28 C ATOM 127 N SER A 18 26.386 55.454 19.282 1.00 24.94 N ATOM 128 CA SER A 18 26.237 54.299 18.425 1.00 24.18 C ATOM 129 C SER A 18 24.802 53.842 18.523 1.00 22.29 C ATOM 130 O SER A 18 24.347 53.532 19.617 1.00 23.79 O ATOM 131 CB SER A 18 27.149 53.172 18.894 1.00 24.21 C ATOM 132 OG SER A 18 27.106 52.129 17.936 1.00 23.83 O ATOM 133 N SER A 19 24.104 53.765 17.417 1.00 24.29 N ATOM 134 CA SER A 19 22.728 53.318 17.344 1.00 28.24 C ATOM 135 C SER A 19 22.502 52.769 15.942 1.00 28.39 C ATOM 136 O SER A 19 23.403 52.798 15.088 1.00 32.39 O ATOM 137 CB SER A 19 21.768 54.477 17.557 1.00 26.55 C ATOM 138 OG SER A 19 21.200 54.164 18.799 1.00 43.12 O ATOM 139 N LYS A 20 21.282 52.295 15.683 1.00 29.46 N ATOM 140 CA LYS A 20 20.855 51.849 14.383 1.00 30.56 C ATOM 141 C LYS A 20 19.678 52.705 13.993 1.00 29.98 C ATOM 142 O LYS A 20 18.898 53.186 14.824 1.00 28.18 O ATOM 143 CB LYS A 20 20.443 50.427 14.445 1.00 34.46 C ATOM 144 CG LYS A 20 21.491 49.702 13.683 1.00 38.60 C ATOM 145 CD LYS A 20 22.086 48.679 14.595 1.00 44.32 C ATOM 146 CE LYS A 20 23.098 47.934 13.734 1.00 48.46 C ATOM 147 NZ LYS A 20 22.465 47.171 12.674 1.00 53.59 N ATOM 148 N ASP A 21 19.637 53.025 12.720 1.00 30.02 N ATOM 149 CA ASP A 21 18.525 53.813 12.242 1.00 33.49 C ATOM 150 C ASP A 21 17.416 52.904 11.690 1.00 34.06 C ATOM 151 O ASP A 21 17.542 51.676 11.704 1.00 32.45 O ATOM 152 CB ASP A 21 19.043 54.780 11.179 1.00 32.36 C ATOM 153 CG ASP A 21 19.485 54.197 9.844 1.00 34.45 C ATOM 154 OD1 ASP A 21 19.440 52.982 9.632 1.00 32.16 O ATOM 155 OD2 ASP A 21 19.876 55.000 8.997 1.00 38.00 O ATOM 156 N ALA A 22 16.388 53.484 11.067 1.00 33.73 N ATOM 157 CA ALA A 22 15.284 52.706 10.539 1.00 34.60 C ATOM 158 C ALA A 22 15.720 51.762 9.435 1.00 36.66 C ATOM 159 O ALA A 22 15.121 50.709 9.267 1.00 39.74 O ATOM 160 CB ALA A 22 14.227 53.644 10.014 1.00 33.09 C ATOM 161 N LYS A 23 16.794 52.051 8.698 1.00 37.50 N ATOM 162 CA LYS A 23 17.296 51.111 7.700 1.00 39.55 C ATOM 163 C LYS A 23 18.187 50.050 8.331 1.00 37.92 C ATOM 164 O LYS A 23 18.575 49.156 7.603 1.00 39.91 O ATOM 165 CB LYS A 23 18.173 51.744 6.636 1.00 44.15 C ATOM 166 CG LYS A 23 17.812 53.137 6.230 1.00 54.74 C ATOM 167 CD LYS A 23 16.474 53.201 5.517 1.00 62.79 C ATOM 168 CE LYS A 23 16.203 54.669 5.222 1.00 69.26 C ATOM 169 NZ LYS A 23 17.248 55.284 4.401 1.00 72.68 N ATOM 170 N GLY A 24 18.525 50.010 9.620 1.00 35.86 N ATOM 171 CA GLY A 24 19.528 49.072 10.118 1.00 34.95 C ATOM 172 C GLY A 24 20.985 49.601 9.967 1.00 34.55 C ATOM 173 O GLY A 24 21.930 48.931 10.388 1.00 34.78 O ATOM 174 N GLU A 25 21.256 50.755 9.339 1.00 32.10 N ATOM 175 CA GLU A 25 22.585 51.339 9.308 1.00 31.38 C ATOM 176 C GLU A 25 23.004 51.740 10.713 1.00 29.23 C ATOM 177 O GLU A 25 22.171 52.113 11.549 1.00 29.37 O ATOM 178 CB GLU A 25 22.650 52.605 8.497 1.00 38.44 C ATOM 179 CG GLU A 25 21.879 52.702 7.191 1.00 50.92 C ATOM 180 CD GLU A 25 22.316 51.820 6.032 1.00 59.37 C ATOM 181 OE1 GLU A 25 23.371 51.175 6.108 1.00 65.27 O ATOM 182 OE2 GLU A 25 21.581 51.802 5.040 1.00 63.56 O ATOM 183 N PHE A 26 24.309 51.695 10.983 1.00 26.77 N ATOM 184 CA PHE A 26 24.902 52.136 12.249 1.00 25.24 C ATOM 185 C PHE A 26 25.002 53.652 12.123 1.00 24.05 C ATOM 186 O PHE A 26 25.452 54.178 11.094 1.00 23.24 O ATOM 187 CB PHE A 26 26.320 51.606 12.431 1.00 25.15 C ATOM 188 CG PHE A 26 26.410 50.119 12.657 1.00 27.52 C ATOM 189 CD1 PHE A 26 26.182 49.242 11.616 1.00 31.09 C ATOM 190 CD2 PHE A 26 26.699 49.662 13.904 1.00 26.17 C ATOM 191 CE1 PHE A 26 26.242 47.900 11.850 1.00 27.74 C ATOM 192 CE2 PHE A 26 26.757 48.312 14.121 1.00 27.63 C ATOM 193 CZ PHE A 26 26.523 47.435 13.101 1.00 25.00 C ATOM 194 N ILE A 27 24.656 54.405 13.124 1.00 21.75 N ATOM 195 CA ILE A 27 24.701 55.846 13.010 1.00 22.54 C ATOM 196 C ILE A 27 25.236 56.355 14.333 1.00 24.64 C ATOM 197 O ILE A 27 25.068 55.683 15.374 1.00 24.41 O ATOM 198 CB ILE A 27 23.266 56.428 12.749 1.00 23.21 C ATOM 199 CG1 ILE A 27 22.280 55.771 13.703 1.00 29.36 C ATOM 200 CG2 ILE A 27 22.846 56.196 11.302 1.00 24.94 C ATOM 201 CD1 ILE A 27 21.002 56.564 13.961 1.00 29.88 C ATOM 202 N GLY A 28 25.826 57.556 14.354 1.00 24.72 N ATOM 203 CA GLY A 28 26.222 58.132 15.630 1.00 23.44 C ATOM 204 C GLY A 28 27.620 58.662 15.554 1.00 21.98 C ATOM 205 O GLY A 28 28.385 58.371 14.619 1.00 23.10 O ATOM 206 N PHE A 29 27.987 59.399 16.576 1.00 22.24 N ATOM 207 CA PHE A 29 29.292 60.080 16.595 1.00 23.61 C ATOM 208 C PHE A 29 30.478 59.108 16.561 1.00 21.23 C ATOM 209 O PHE A 29 31.403 59.333 15.790 1.00 21.92 O ATOM 210 CB PHE A 29 29.381 61.006 17.847 1.00 24.27 C ATOM 211 CG PHE A 29 30.568 61.958 17.771 1.00 23.12 C ATOM 212 CD1 PHE A 29 30.798 62.667 16.600 1.00 22.78 C ATOM 213 CD2 PHE A 29 31.404 62.103 18.869 1.00 27.41 C ATOM 214 CE1 PHE A 29 31.869 63.522 16.516 1.00 21.57 C ATOM 215 CE2 PHE A 29 32.483 62.978 18.773 1.00 26.99 C ATOM 216 CZ PHE A 29 32.709 63.681 17.604 1.00 23.76 C ATOM 217 N ASP A 30 30.473 58.013 17.312 1.00 18.81 N ATOM 218 CA ASP A 30 31.505 56.992 17.229 1.00 19.33 C ATOM 219 C ASP A 30 31.635 56.414 15.832 1.00 18.92 C ATOM 220 O ASP A 30 32.734 56.130 15.340 1.00 18.08 O ATOM 221 CB ASP A 30 31.184 55.846 18.157 1.00 20.25 C ATOM 222 CG ASP A 30 31.614 56.074 19.577 1.00 24.54 C ATOM 223 OD1 ASP A 30 32.154 57.126 19.886 1.00 24.55 O ATOM 224 OD2 ASP A 30 31.421 55.172 20.383 1.00 27.40 O ATOM 225 N ILE A 31 30.489 56.265 15.156 1.00 21.22 N ATOM 226 CA ILE A 31 30.444 55.689 13.814 1.00 23.29 C ATOM 227 C ILE A 31 31.051 56.691 12.842 1.00 23.07 C ATOM 228 O ILE A 31 31.811 56.313 11.948 1.00 22.53 O ATOM 229 CB ILE A 31 28.959 55.336 13.373 1.00 22.95 C ATOM 230 CG1 ILE A 31 28.252 54.488 14.449 1.00 22.68 C ATOM 231 CG2 ILE A 31 28.988 54.664 11.991 1.00 21.73 C ATOM 232 CD1 ILE A 31 28.902 53.175 14.922 1.00 23.55 C ATOM 233 N ASP A 32 30.753 57.982 13.024 1.00 22.79 N ATOM 234 CA ASP A 32 31.297 59.003 12.137 1.00 23.95 C ATOM 235 C ASP A 32 32.788 59.102 12.276 1.00 24.22 C ATOM 236 O ASP A 32 33.483 59.006 11.265 1.00 25.49 O ATOM 237 CB ASP A 32 30.690 60.355 12.434 1.00 23.66 C ATOM 238 CG ASP A 32 29.217 60.406 12.043 1.00 25.99 C ATOM 239 OD1 ASP A 32 28.765 59.721 11.118 1.00 25.39 O ATOM 240 OD2 ASP A 32 28.513 61.146 12.710 1.00 27.51 O ATOM 241 N LEU A 33 33.255 59.228 13.515 1.00 23.55 N ATOM 242 CA LEU A 33 34.674 59.198 13.862 1.00 24.21 C ATOM 243 C LEU A 33 35.360 57.948 13.285 1.00 23.80 C ATOM 244 O LEU A 33 36.374 58.018 12.583 1.00 24.95 O ATOM 245 CB LEU A 33 34.741 59.223 15.365 1.00 21.18 C ATOM 246 CG LEU A 33 35.372 60.353 16.163 1.00 27.23 C ATOM 247 CD1 LEU A 33 35.374 61.688 15.445 1.00 25.15 C ATOM 248 CD2 LEU A 33 34.600 60.396 17.466 1.00 24.00 C ATOM 249 N GLY A 34 34.772 56.772 13.503 1.00 25.04 N ATOM 250 CA GLY A 34 35.295 55.504 13.010 1.00 22.57 C ATOM 251 C GLY A 34 35.419 55.458 11.513 1.00 22.51 C ATOM 252 O GLY A 34 36.499 55.162 10.999 1.00 23.63 O ATOM 253 N ASN A 35 34.375 55.818 10.785 1.00 21.42 N ATOM 254 CA ASN A 35 34.407 55.793 9.342 1.00 23.24 C ATOM 255 C ASN A 35 35.364 56.769 8.727 1.00 23.83 C ATOM 256 O ASN A 35 36.025 56.435 7.742 1.00 27.57 O ATOM 257 CB ASN A 35 33.059 56.085 8.769 1.00 27.69 C ATOM 258 CG ASN A 35 32.077 54.927 8.852 1.00 31.66 C ATOM 259 OD1 ASN A 35 30.886 55.163 9.046 1.00 35.87 O ATOM 260 ND2 ASN A 35 32.465 53.655 8.720 1.00 31.42 N ATOM 261 N GLU A 36 35.449 57.960 9.287 1.00 24.43 N ATOM 262 CA GLU A 36 36.400 58.960 8.841 1.00 26.49 C ATOM 263 C GLU A 36 37.847 58.477 9.044 1.00 26.24 C ATOM 264 O GLU A 36 38.651 58.425 8.103 1.00 25.04 O ATOM 265 CB GLU A 36 36.109 60.232 9.622 1.00 27.33 C ATOM 266 CG GLU A 36 36.847 61.475 9.157 1.00 35.47 C ATOM 267 CD GLU A 36 36.561 61.908 7.733 1.00 39.42 C ATOM 268 OE1 GLU A 36 35.432 61.729 7.255 1.00 44.95 O ATOM 269 OE2 GLU A 36 37.484 62.420 7.104 1.00 41.57 O ATOM 270 N MET A 37 38.196 57.988 10.242 1.00 25.89 N ATOM 271 CA MET A 37 39.523 57.425 10.466 1.00 25.46 C ATOM 272 C MET A 37 39.774 56.306 9.467 1.00 26.94 C ATOM 273 O MET A 37 40.802 56.372 8.794 1.00 28.87 O ATOM 274 CB MET A 37 39.689 56.863 11.861 1.00 22.39 C ATOM 275 CG MET A 37 39.723 57.993 12.859 1.00 21.06 C ATOM 276 SD MET A 37 40.057 57.515 14.554 1.00 25.42 S ATOM 277 CE MET A 37 38.600 56.655 15.053 1.00 24.61 C ATOM 278 N CYS A 38 38.906 55.338 9.198 1.00 27.09 N ATOM 279 CA CYS A 38 39.184 54.297 8.195 1.00 27.94 C ATOM 280 C CYS A 38 39.472 54.852 6.827 1.00 29.04 C ATOM 281 O CYS A 38 40.367 54.354 6.139 1.00 28.15 O ATOM 282 CB CYS A 38 38.029 53.355 8.054 1.00 24.84 C ATOM 283 SG CYS A 38 37.723 52.651 9.686 1.00 29.17 S ATOM 284 N LYS A 39 38.780 55.937 6.485 1.00 31.00 N ATOM 285 CA LYS A 39 38.967 56.650 5.229 1.00 32.46 C ATOM 286 C LYS A 39 40.391 57.169 5.142 1.00 30.54 C ATOM 287 O LYS A 39 41.106 56.889 4.193 1.00 32.08 O ATOM 288 CB LYS A 39 38.034 57.821 5.169 1.00 34.80 C ATOM 289 CG LYS A 39 37.652 58.160 3.774 1.00 41.17 C ATOM 290 CD LYS A 39 37.358 59.648 3.746 1.00 51.23 C ATOM 291 CE LYS A 39 37.053 60.051 2.302 1.00 59.45 C ATOM 292 NZ LYS A 39 38.075 59.565 1.367 1.00 65.90 N ATOM 293 N ARG A 40 40.861 57.894 6.144 1.00 30.78 N ATOM 294 CA ARG A 40 42.207 58.442 6.151 1.00 32.21 C ATOM 295 C ARG A 40 43.284 57.342 6.231 1.00 34.71 C ATOM 296 O ARG A 40 44.386 57.458 5.674 1.00 36.23 O ATOM 297 CB ARG A 40 42.373 59.349 7.328 1.00 32.40 C ATOM 298 CG ARG A 40 41.238 60.284 7.596 1.00 36.74 C ATOM 299 CD ARG A 40 41.468 61.560 6.886 1.00 42.88 C ATOM 300 NE ARG A 40 40.402 62.508 7.176 1.00 45.63 N ATOM 301 CZ ARG A 40 40.643 63.773 7.493 1.00 46.14 C ATOM 302 NH1 ARG A 40 41.889 64.256 7.585 1.00 47.38 N ATOM 303 NH2 ARG A 40 39.599 64.583 7.645 1.00 48.62 N ATOM 304 N MET A 41 42.995 56.241 6.936 1.00 32.89 N ATOM 305 CA MET A 41 43.885 55.106 7.060 1.00 30.91 C ATOM 306 C MET A 41 43.968 54.359 5.772 1.00 32.59 C ATOM 307 O MET A 41 44.935 53.642 5.576 1.00 34.20 O ATOM 308 CB MET A 41 43.404 54.115 8.071 1.00 29.39 C ATOM 309 CG MET A 41 43.586 54.664 9.458 1.00 31.26 C ATOM 310 SD MET A 41 42.516 53.823 10.632 1.00 33.20 S ATOM 311 CE MET A 41 43.076 52.163 10.379 1.00 32.35 C ATOM 312 N GLN A 42 42.942 54.486 4.933 1.00 33.45 N ATOM 313 CA GLN A 42 42.806 53.806 3.670 1.00 34.53 C ATOM 314 C GLN A 42 42.668 52.294 3.828 1.00 35.33 C ATOM 315 O GLN A 42 43.273 51.501 3.111 1.00 37.36 O ATOM 316 CB GLN A 42 43.994 54.180 2.792 1.00 38.86 C ATOM 317 CG GLN A 42 44.012 55.683 2.613 1.00 48.09 C ATOM 318 CD GLN A 42 45.172 56.177 1.784 1.00 55.00 C ATOM 319 OE1 GLN A 42 45.265 55.900 0.589 1.00 60.30 O ATOM 320 NE2 GLN A 42 46.102 56.938 2.337 1.00 60.62 N ATOM 321 N VAL A 43 41.800 51.855 4.735 1.00 34.35 N ATOM 322 CA VAL A 43 41.490 50.443 4.943 1.00 35.59 C ATOM 323 C VAL A 43 39.980 50.290 4.821 1.00 34.54 C ATOM 324 O VAL A 43 39.236 51.268 4.845 1.00 36.23 O ATOM 325 CB VAL A 43 41.842 49.867 6.362 1.00 35.67 C ATOM 326 CG1 VAL A 43 43.338 49.808 6.564 1.00 39.89 C ATOM 327 CG2 VAL A 43 41.238 50.735 7.455 1.00 37.58 C ATOM 328 N LYS A 44 39.502 49.053 4.725 1.00 34.98 N ATOM 329 CA LYS A 44 38.089 48.752 4.731 1.00 33.40 C ATOM 330 C LYS A 44 37.802 48.393 6.171 1.00 33.73 C ATOM 331 O LYS A 44 38.544 47.602 6.748 1.00 33.61 O ATOM 332 CB LYS A 44 37.737 47.528 3.904 1.00 35.05 C ATOM 333 N CYS A 45 36.756 48.964 6.765 1.00 33.53 N ATOM 334 CA CYS A 45 36.335 48.687 8.133 1.00 32.20 C ATOM 335 C CYS A 45 34.963 48.076 8.096 1.00 32.24 C ATOM 336 O CYS A 45 34.186 48.370 7.181 1.00 34.66 O ATOM 337 CB CYS A 45 36.264 49.945 8.926 1.00 32.25 C ATOM 338 SG CYS A 45 37.998 50.445 9.074 1.00 31.91 S ATOM 339 N THR A 46 34.624 47.188 8.991 1.00 28.56 N ATOM 340 CA THR A 46 33.305 46.642 8.963 1.00 29.49 C ATOM 341 C THR A 46 32.851 46.777 10.386 1.00 29.26 C ATOM 342 O THR A 46 33.652 46.510 11.264 1.00 30.59 O ATOM 343 CB THR A 46 33.403 45.197 8.503 1.00 28.25 C ATOM 344 OG1 THR A 46 33.690 45.267 7.113 1.00 33.86 O ATOM 345 CG2 THR A 46 32.128 44.426 8.679 1.00 30.66 C ATOM 346 N TRP A 47 31.617 47.218 10.616 1.00 28.75 N ATOM 347 CA TRP A 47 31.031 47.339 11.931 1.00 26.78 C ATOM 348 C TRP A 47 30.256 46.072 12.300 1.00 27.68 C ATOM 349 O TRP A 47 29.485 45.499 11.511 1.00 25.38 O ATOM 350 CB TRP A 47 30.145 48.540 11.900 1.00 24.94 C ATOM 351 CG TRP A 47 30.946 49.829 11.757 1.00 24.82 C ATOM 352 CD1 TRP A 47 31.060 50.435 10.545 1.00 25.50 C ATOM 353 CD2 TRP A 47 31.513 50.558 12.760 1.00 23.52 C ATOM 354 NE1 TRP A 47 31.691 51.558 10.773 1.00 26.59 N ATOM 355 CE2 TRP A 47 31.976 51.658 12.075 1.00 25.29 C ATOM 356 CE3 TRP A 47 31.707 50.462 14.098 1.00 26.07 C ATOM 357 CZ2 TRP A 47 32.614 52.715 12.674 1.00 23.02 C ATOM 358 CZ3 TRP A 47 32.345 51.518 14.709 1.00 28.11 C ATOM 359 CH2 TRP A 47 32.793 52.631 14.012 1.00 22.83 C ATOM 360 N VAL A 48 30.549 45.632 13.520 1.00 27.45 N ATOM 361 CA VAL A 48 30.024 44.411 14.078 1.00 25.37 C ATOM 362 C VAL A 48 29.273 44.823 15.335 1.00 25.45 C ATOM 363 O VAL A 48 29.848 45.292 16.319 1.00 25.44 O ATOM 364 CB VAL A 48 31.200 43.441 14.424 1.00 26.35 C ATOM 365 CG1 VAL A 48 30.614 42.138 14.905 1.00 28.88 C ATOM 366 CG2 VAL A 48 32.089 43.155 13.231 1.00 22.81 C ATOM 367 N ALA A 49 27.949 44.719 15.342 1.00 26.91 N ATOM 368 CA ALA A 49 27.178 44.960 16.554 1.00 27.12 C ATOM 369 C ALA A 49 27.418 43.895 17.598 1.00 27.72 C ATOM 370 O ALA A 49 27.462 42.695 17.318 1.00 31.78 O ATOM 371 CB ALA A 49 25.683 45.000 16.252 1.00 28.27 C ATOM 372 N SER A 50 27.598 44.328 18.812 1.00 27.89 N ATOM 373 CA SER A 50 27.864 43.427 19.887 1.00 31.54 C ATOM 374 C SER A 50 27.416 44.039 21.194 1.00 30.55 C ATOM 375 O SER A 50 27.288 45.248 21.339 1.00 30.91 O ATOM 376 CB SER A 50 29.365 43.117 19.919 1.00 31.30 C ATOM 377 OG SER A 50 29.702 42.434 21.130 1.00 35.38 O ATOM 378 N ASP A 51 27.146 43.184 22.161 1.00 30.27 N ATOM 379 CA ASP A 51 26.914 43.632 23.493 1.00 34.29 C ATOM 380 C ASP A 51 28.228 44.129 24.073 1.00 33.92 C ATOM 381 O ASP A 51 29.293 43.542 23.882 1.00 35.49 O ATOM 382 CB ASP A 51 26.354 42.473 24.316 1.00 44.83 C ATOM 383 CG ASP A 51 24.947 42.030 23.873 1.00 55.36 C ATOM 384 OD1 ASP A 51 24.130 42.860 23.415 1.00 60.32 O ATOM 385 OD2 ASP A 51 24.668 40.833 23.996 1.00 60.90 O ATOM 386 N PHE A 52 28.158 45.194 24.846 1.00 31.12 N ATOM 387 CA PHE A 52 29.296 45.833 25.434 1.00 30.64 C ATOM 388 C PHE A 52 30.158 44.914 26.233 1.00 31.68 C ATOM 389 O PHE A 52 31.372 45.029 26.157 1.00 33.14 O ATOM 390 CB PHE A 52 28.873 46.951 26.353 1.00 30.75 C ATOM 391 CG PHE A 52 30.013 47.882 26.684 1.00 28.39 C ATOM 392 CD1 PHE A 52 30.305 48.913 25.826 1.00 30.94 C ATOM 393 CD2 PHE A 52 30.740 47.696 27.832 1.00 31.36 C ATOM 394 CE1 PHE A 52 31.337 49.778 26.116 1.00 34.23 C ATOM 395 CE2 PHE A 52 31.775 48.563 28.117 1.00 36.40 C ATOM 396 CZ PHE A 52 32.071 49.604 27.261 1.00 33.73 C ATOM 397 N ASP A 53 29.588 44.032 27.035 1.00 35.06 N ATOM 398 CA ASP A 53 30.415 43.124 27.823 1.00 38.09 C ATOM 399 C ASP A 53 31.195 42.050 27.053 1.00 35.30 C ATOM 400 O ASP A 53 32.166 41.494 27.576 1.00 36.86 O ATOM 401 CB ASP A 53 29.522 42.475 28.886 1.00 46.64 C ATOM 402 CG ASP A 53 28.915 43.505 29.848 1.00 56.76 C ATOM 403 OD1 ASP A 53 29.571 44.494 30.231 1.00 58.46 O ATOM 404 OD2 ASP A 53 27.751 43.304 30.199 1.00 63.95 O ATOM 405 N ALA A 54 30.821 41.816 25.794 1.00 29.90 N ATOM 406 CA ALA A 54 31.481 40.869 24.920 1.00 26.94 C ATOM 407 C ALA A 54 32.584 41.509 24.102 1.00 25.31 C ATOM 408 O ALA A 54 33.372 40.854 23.427 1.00 24.11 O ATOM 409 CB ALA A 54 30.489 40.312 23.962 1.00 26.03 C ATOM 410 N LEU A 55 32.683 42.818 24.116 1.00 25.30 N ATOM 411 CA LEU A 55 33.606 43.508 23.247 1.00 24.52 C ATOM 412 C LEU A 55 35.070 43.237 23.568 1.00 24.35 C ATOM 413 O LEU A 55 35.787 42.802 22.667 1.00 25.65 O ATOM 414 CB LEU A 55 33.315 45.005 23.317 1.00 23.85 C ATOM 415 CG LEU A 55 32.058 45.529 22.646 1.00 23.17 C ATOM 416 CD1 LEU A 55 31.862 47.001 23.007 1.00 24.98 C ATOM 417 CD2 LEU A 55 32.161 45.316 21.172 1.00 20.18 C ATOM 418 N ILE A 56 35.568 43.439 24.782 1.00 23.52 N ATOM 419 CA ILE A 56 36.967 43.136 25.067 1.00 28.70 C ATOM 420 C ILE A 56 37.262 41.615 24.914 1.00 29.66 C ATOM 421 O ILE A 56 38.305 41.271 24.327 1.00 29.66 O ATOM 422 CB ILE A 56 37.335 43.667 26.506 1.00 26.92 C ATOM 423 CG1 ILE A 56 37.268 45.196 26.456 1.00 28.12 C ATOM 424 CG2 ILE A 56 38.741 43.195 26.972 1.00 28.91 C ATOM 425 CD1 ILE A 56 37.693 45.929 27.749 1.00 29.58 C ATOM 426 N PRO A 57 36.403 40.669 25.339 1.00 30.13 N ATOM 427 CA PRO A 57 36.528 39.242 24.990 1.00 29.99 C ATOM 428 C PRO A 57 36.675 38.980 23.492 1.00 28.52 C ATOM 429 O PRO A 57 37.614 38.302 23.034 1.00 27.94 O ATOM 430 CB PRO A 57 35.293 38.632 25.612 1.00 27.55 C ATOM 431 CG PRO A 57 35.199 39.401 26.908 1.00 26.27 C ATOM 432 CD PRO A 57 35.392 40.823 26.400 1.00 29.59 C ATOM 433 N SER A 58 35.812 39.603 22.694 1.00 27.40 N ATOM 434 CA SER A 58 35.905 39.444 21.267 1.00 26.97 C ATOM 435 C SER A 58 37.189 40.007 20.684 1.00 24.86 C ATOM 436 O SER A 58 37.716 39.469 19.704 1.00 25.44 O ATOM 437 CB SER A 58 34.729 40.106 20.612 1.00 28.82 C ATOM 438 OG SER A 58 33.578 39.424 21.064 1.00 37.68 O ATOM 439 N LEU A 59 37.700 41.090 21.257 1.00 23.94 N ATOM 440 CA LEU A 59 38.946 41.704 20.803 1.00 25.37 C ATOM 441 C LEU A 59 40.131 40.769 21.069 1.00 21.64 C ATOM 442 O LEU A 59 40.943 40.483 20.197 1.00 21.96 O ATOM 443 CB LEU A 59 39.189 43.067 21.542 1.00 22.72 C ATOM 444 CG LEU A 59 40.411 43.898 21.113 1.00 20.13 C ATOM 445 CD1 LEU A 59 40.255 44.310 19.654 1.00 15.78 C ATOM 446 CD2 LEU A 59 40.565 45.078 22.030 1.00 17.14 C ATOM 447 N LYS A 60 40.179 40.295 22.302 1.00 21.74 N ATOM 448 CA LYS A 60 41.250 39.422 22.739 1.00 25.85 C ATOM 449 C LYS A 60 41.269 38.108 21.965 1.00 27.03 C ATOM 450 O LYS A 60 42.338 37.589 21.634 1.00 27.94 O ATOM 451 CB LYS A 60 41.076 39.198 24.212 1.00 25.47 C ATOM 452 CG LYS A 60 41.257 40.568 24.842 1.00 32.80 C ATOM 453 CD LYS A 60 41.879 40.565 26.204 1.00 37.72 C ATOM 454 CE LYS A 60 40.958 40.221 27.360 1.00 44.08 C ATOM 455 NZ LYS A 60 41.764 40.232 28.576 1.00 48.70 N ATOM 456 N ALA A 61 40.092 37.617 21.577 1.00 24.76 N ATOM 457 CA ALA A 61 39.921 36.383 20.836 1.00 23.52 C ATOM 458 C ALA A 61 40.161 36.522 19.356 1.00 24.61 C ATOM 459 O ALA A 61 40.219 35.537 18.638 1.00 25.71 O ATOM 460 CB ALA A 61 38.514 35.891 21.049 1.00 22.26 C ATOM 461 N LYS A 62 40.292 37.773 18.887 1.00 26.01 N ATOM 462 CA LYS A 62 40.510 38.231 17.507 1.00 24.30 C ATOM 463 C LYS A 62 39.305 38.043 16.619 1.00 22.36 C ATOM 464 O LYS A 62 39.389 37.960 15.386 1.00 23.21 O ATOM 465 CB LYS A 62 41.742 37.542 16.849 1.00 24.82 C ATOM 466 CG LYS A 62 43.001 37.653 17.699 1.00 21.61 C ATOM 467 CD LYS A 62 44.204 37.361 16.864 1.00 24.37 C ATOM 468 CE LYS A 62 45.375 37.589 17.775 1.00 27.28 C ATOM 469 NZ LYS A 62 46.602 37.470 17.007 1.00 28.70 N ATOM 470 N LYS A 63 38.137 38.061 17.265 1.00 23.17 N ATOM 471 CA LYS A 63 36.875 38.091 16.529 1.00 25.14 C ATOM 472 C LYS A 63 36.682 39.475 15.888 1.00 24.80 C ATOM 473 O LYS A 63 36.146 39.589 14.791 1.00 24.72 O ATOM 474 CB LYS A 63 35.727 37.830 17.449 1.00 27.83 C ATOM 475 CG LYS A 63 35.714 36.414 17.964 1.00 34.40 C ATOM 476 CD LYS A 63 34.448 36.316 18.757 1.00 39.81 C ATOM 477 CE LYS A 63 34.412 34.979 19.438 1.00 45.17 C ATOM 478 NZ LYS A 63 33.226 34.927 20.262 1.00 50.73 N ATOM 479 N ILE A 64 37.162 40.537 16.543 1.00 24.42 N ATOM 480 CA ILE A 64 37.142 41.884 15.992 1.00 21.04 C ATOM 481 C ILE A 64 38.573 42.421 16.153 1.00 21.51 C ATOM 482 O ILE A 64 39.375 41.867 16.894 1.00 21.68 O ATOM 483 CB ILE A 64 36.125 42.837 16.752 1.00 19.55 C ATOM 484 CG1 ILE A 64 36.438 42.870 18.224 1.00 16.70 C ATOM 485 CG2 ILE A 64 34.691 42.406 16.467 1.00 16.99 C ATOM 486 CD1 ILE A 64 35.533 43.739 19.065 1.00 18.17 C ATOM 487 N ASP A 65 38.905 43.518 15.474 1.00 21.85 N ATOM 488 CA ASP A 65 40.197 44.181 15.511 1.00 21.61 C ATOM 489 C ASP A 65 40.231 45.478 16.304 1.00 22.87 C ATOM 490 O ASP A 65 41.315 45.953 16.626 1.00 23.73 O ATOM 491 CB ASP A 65 40.656 44.499 14.094 1.00 22.34 C ATOM 492 CG ASP A 65 40.613 43.209 13.310 1.00 23.11 C ATOM 493 OD1 ASP A 65 41.228 42.248 13.784 1.00 23.12 O ATOM 494 OD2 ASP A 65 39.947 43.158 12.279 1.00 22.27 O ATOM 495 N ALA A 66 39.093 46.101 16.584 1.00 20.86 N ATOM 496 CA ALA A 66 39.054 47.357 17.298 1.00 22.68 C ATOM 497 C ALA A 66 37.675 47.459 17.935 1.00 21.91 C ATOM 498 O ALA A 66 36.696 46.837 17.490 1.00 22.83 O ATOM 499 CB ALA A 66 39.252 48.552 16.333 1.00 19.81 C ATOM 500 N ILE A 67 37.619 48.246 18.999 1.00 22.11 N ATOM 501 CA ILE A 67 36.388 48.529 19.686 1.00 21.07 C ATOM 502 C ILE A 67 36.179 50.040 19.604 1.00 21.39 C ATOM 503 O ILE A 67 37.054 50.781 20.091 1.00 21.82 O ATOM 504 CB ILE A 67 36.447 48.135 21.181 1.00 18.22 C ATOM 505 CG1 ILE A 67 36.702 46.631 21.396 1.00 17.83 C ATOM 506 CG2 ILE A 67 35.096 48.584 21.800 1.00 18.97 C ATOM 507 CD1 ILE A 67 36.997 46.280 22.865 1.00 15.01 C ATOM 508 N ILE A 68 35.087 50.536 19.029 1.00 20.85 N ATOM 509 CA ILE A 68 34.771 51.962 19.172 1.00 21.28 C ATOM 510 C ILE A 68 33.327 51.964 19.674 1.00 20.96 C ATOM 511 O ILE A 68 32.345 51.803 18.934 1.00 24.84 O ATOM 512 CB ILE A 68 34.865 52.740 17.850 1.00 19.96 C ATOM 513 CG1 ILE A 68 36.280 52.741 17.254 1.00 18.21 C ATOM 514 CG2 ILE A 68 34.489 54.192 18.151 1.00 20.36 C ATOM 515 CD1 ILE A 68 36.374 53.351 15.796 1.00 13.57 C ATOM 516 N SER A 69 33.212 52.138 20.980 1.00 20.49 N ATOM 517 CA SER A 69 31.941 52.049 21.629 1.00 22.46 C ATOM 518 C SER A 69 31.952 52.862 22.918 1.00 21.40 C ATOM 519 O SER A 69 31.587 52.315 23.971 1.00 21.63 O ATOM 520 CB SER A 69 31.709 50.578 21.864 1.00 20.88 C ATOM 521 OG SER A 69 30.356 50.318 22.194 1.00 29.43 O ATOM 522 N SER A 70 32.366 54.156 22.873 1.00 20.86 N ATOM 523 CA SER A 70 32.486 55.013 24.051 1.00 21.21 C ATOM 524 C SER A 70 33.275 54.348 25.177 1.00 23.56 C ATOM 525 O SER A 70 32.947 54.414 26.381 1.00 25.04 O ATOM 526 CB SER A 70 31.092 55.398 24.560 1.00 19.72 C ATOM 527 OG SER A 70 30.390 56.106 23.572 1.00 26.34 O ATOM 528 N LEU A 71 34.348 53.652 24.806 1.00 24.94 N ATOM 529 CA LEU A 71 35.037 52.838 25.809 1.00 23.19 C ATOM 530 C LEU A 71 36.004 53.734 26.589 1.00 22.46 C ATOM 531 O LEU A 71 36.937 54.261 25.971 1.00 23.19 O ATOM 532 CB LEU A 71 35.715 51.721 25.033 1.00 21.26 C ATOM 533 CG LEU A 71 36.506 50.727 25.833 1.00 24.99 C ATOM 534 CD1 LEU A 71 35.597 49.814 26.604 1.00 22.56 C ATOM 535 CD2 LEU A 71 37.372 49.947 24.859 1.00 25.23 C ATOM 536 N SER A 72 35.890 53.985 27.883 1.00 22.19 N ATOM 537 CA SER A 72 36.771 54.953 28.453 1.00 25.12 C ATOM 538 C SER A 72 38.084 54.304 28.825 1.00 25.51 C ATOM 539 O SER A 72 38.203 53.103 29.115 1.00 24.55 O ATOM 540 CB SER A 72 36.053 55.601 29.627 1.00 24.52 C ATOM 541 OG SER A 72 35.669 54.587 30.511 1.00 31.90 O ATOM 542 N ILE A 73 39.101 55.117 28.689 1.00 26.49 N ATOM 543 CA ILE A 73 40.470 54.719 28.933 1.00 26.87 C ATOM 544 C ILE A 73 40.690 54.700 30.440 1.00 29.92 C ATOM 545 O ILE A 73 41.015 55.743 31.065 1.00 29.79 O ATOM 546 CB ILE A 73 41.426 55.663 28.210 1.00 25.84 C ATOM 547 CG1 ILE A 73 41.078 55.726 26.726 1.00 21.31 C ATOM 548 CG2 ILE A 73 42.876 55.203 28.428 1.00 23.52 C ATOM 549 CD1 ILE A 73 41.572 56.902 25.907 1.00 18.20 C ATOM 550 N THR A 74 40.471 53.554 31.048 1.00 30.75 N ATOM 551 CA THR A 74 40.711 53.444 32.466 1.00 32.96 C ATOM 552 C THR A 74 41.991 52.665 32.670 1.00 35.15 C ATOM 553 O THR A 74 42.387 51.857 31.818 1.00 33.89 O ATOM 554 CB THR A 74 39.512 52.748 33.132 1.00 35.05 C ATOM 555 OG1 THR A 74 39.451 51.386 32.674 1.00 33.36 O ATOM 556 CG2 THR A 74 38.203 53.470 32.799 1.00 35.26 C ATOM 557 N ASP A 75 42.576 52.802 33.847 1.00 37.91 N ATOM 558 CA ASP A 75 43.803 52.109 34.185 1.00 44.06 C ATOM 559 C ASP A 75 43.640 50.587 34.128 1.00 41.17 C ATOM 560 O ASP A 75 44.446 49.853 33.576 1.00 37.60 O ATOM 561 CB ASP A 75 44.229 52.576 35.581 1.00 53.71 C ATOM 562 CG ASP A 75 45.752 52.670 35.706 1.00 65.27 C ATOM 563 OD1 ASP A 75 46.399 51.668 36.067 1.00 68.27 O ATOM 564 OD2 ASP A 75 46.281 53.759 35.428 1.00 70.64 O ATOM 565 N LYS A 76 42.512 50.108 34.626 1.00 41.84 N ATOM 566 CA LYS A 76 42.187 48.690 34.639 1.00 43.86 C ATOM 567 C LYS A 76 42.080 48.161 33.212 1.00 41.18 C ATOM 568 O LYS A 76 42.548 47.056 32.978 1.00 41.31 O ATOM 569 CB LYS A 76 40.870 48.525 35.441 1.00 48.63 C ATOM 570 CG LYS A 76 40.659 47.192 36.134 1.00 57.21 C ATOM 571 CD LYS A 76 40.265 46.116 35.127 1.00 66.97 C ATOM 572 CE LYS A 76 40.928 44.778 35.451 1.00 73.00 C ATOM 573 NZ LYS A 76 40.877 43.911 34.281 1.00 78.73 N ATOM 574 N ARG A 77 41.540 48.876 32.220 1.00 38.06 N ATOM 575 CA ARG A 77 41.508 48.334 30.875 1.00 36.26 C ATOM 576 C ARG A 77 42.874 48.438 30.222 1.00 35.96 C ATOM 577 O ARG A 77 43.198 47.609 29.375 1.00 37.90 O ATOM 578 CB ARG A 77 40.515 49.068 30.011 1.00 35.35 C ATOM 579 CG ARG A 77 39.089 48.813 30.439 1.00 34.61 C ATOM 580 CD ARG A 77 38.111 49.607 29.602 1.00 34.78 C ATOM 581 NE ARG A 77 36.769 49.308 30.075 1.00 33.49 N ATOM 582 CZ ARG A 77 35.823 50.212 30.249 1.00 31.00 C ATOM 583 NH1 ARG A 77 36.006 51.505 30.003 1.00 31.54 N ATOM 584 NH2 ARG A 77 34.660 49.780 30.667 1.00 29.81 N ATOM 585 N GLN A 78 43.687 49.437 30.579 1.00 35.53 N ATOM 586 CA GLN A 78 45.037 49.582 30.046 1.00 36.70 C ATOM 587 C GLN A 78 45.924 48.400 30.439 1.00 38.04 C ATOM 588 O GLN A 78 46.872 48.045 29.757 1.00 37.77 O ATOM 589 CB GLN A 78 45.634 50.892 30.544 1.00 35.00 C ATOM 590 CG GLN A 78 44.883 52.058 29.926 1.00 39.46 C ATOM 591 CD GLN A 78 45.595 53.407 29.869 1.00 42.06 C ATOM 592 OE1 GLN A 78 46.063 53.867 28.838 1.00 46.20 O ATOM 593 NE2 GLN A 78 45.706 54.164 30.928 1.00 41.44 N ATOM 594 N GLN A 79 45.626 47.781 31.569 1.00 41.08 N ATOM 595 CA GLN A 79 46.223 46.534 31.990 1.00 44.98 C ATOM 596 C GLN A 79 45.982 45.448 30.947 1.00 44.86 C ATOM 597 O GLN A 79 46.858 44.607 30.725 1.00 44.97 O ATOM 598 CB GLN A 79 45.610 46.126 33.331 1.00 50.71 C ATOM 599 CG GLN A 79 46.309 46.544 34.634 1.00 60.89 C ATOM 600 CD GLN A 79 46.725 48.011 34.823 1.00 68.88 C ATOM 601 OE1 GLN A 79 46.931 48.805 33.894 1.00 72.10 O ATOM 602 NE2 GLN A 79 46.903 48.436 36.076 1.00 70.81 N ATOM 603 N GLU A 80 44.823 45.449 30.281 1.00 42.79 N ATOM 604 CA GLU A 80 44.464 44.425 29.308 1.00 41.83 C ATOM 605 C GLU A 80 44.664 44.684 27.816 1.00 37.90 C ATOM 606 O GLU A 80 45.034 43.774 27.048 1.00 34.40 O ATOM 607 CB GLU A 80 43.015 44.058 29.438 1.00 48.44 C ATOM 608 CG GLU A 80 42.522 43.631 30.786 1.00 58.67 C ATOM 609 CD GLU A 80 41.411 42.612 30.612 1.00 65.04 C ATOM 610 OE1 GLU A 80 40.376 42.932 30.013 1.00 68.61 O ATOM 611 OE2 GLU A 80 41.610 41.481 31.062 1.00 71.43 O ATOM 612 N ILE A 81 44.349 45.924 27.387 1.00 33.82 N ATOM 613 CA ILE A 81 44.290 46.305 25.975 1.00 29.05 C ATOM 614 C ILE A 81 45.005 47.634 25.848 1.00 25.87 C ATOM 615 O ILE A 81 45.335 48.266 26.851 1.00 27.22 O ATOM 616 CB ILE A 81 42.815 46.514 25.425 1.00 27.37 C ATOM 617 CG1 ILE A 81 42.013 47.565 26.228 1.00 24.66 C ATOM 618 CG2 ILE A 81 42.107 45.176 25.459 1.00 26.45 C ATOM 619 CD1 ILE A 81 40.589 47.834 25.674 1.00 19.13 C ATOM 620 N ALA A 82 45.174 48.032 24.598 1.00 23.21 N ATOM 621 CA ALA A 82 45.763 49.291 24.219 1.00 24.57 C ATOM 622 C ALA A 82 44.634 50.221 23.748 1.00 23.88 C ATOM 623 O ALA A 82 43.543 49.755 23.417 1.00 23.49 O ATOM 624 CB ALA A 82 46.746 49.048 23.087 1.00 22.45 C ATOM 625 N PHE A 83 44.848 51.531 23.717 1.00 24.16 N ATOM 626 CA PHE A 83 43.895 52.530 23.290 1.00 24.86 C ATOM 627 C PHE A 83 44.550 53.497 22.327 1.00 25.24 C ATOM 628 O PHE A 83 45.759 53.792 22.411 1.00 27.16 O ATOM 629 CB PHE A 83 43.389 53.378 24.435 1.00 22.66 C ATOM 630 CG PHE A 83 42.443 52.622 25.323 1.00 24.05 C ATOM 631 CD1 PHE A 83 41.092 52.559 24.961 1.00 22.90 C ATOM 632 CD2 PHE A 83 42.918 52.054 26.490 1.00 22.03 C ATOM 633 CE1 PHE A 83 40.215 51.916 25.810 1.00 21.54 C ATOM 634 CE2 PHE A 83 42.018 51.415 27.319 1.00 23.09 C ATOM 635 CZ PHE A 83 40.681 51.354 26.985 1.00 20.39 C ATOM 636 N SER A 84 43.757 54.017 21.393 1.00 24.28 N ATOM 637 CA SER A 84 44.224 55.118 20.556 1.00 23.81 C ATOM 638 C SER A 84 44.304 56.331 21.478 1.00 22.23 C ATOM 639 O SER A 84 43.955 56.288 22.662 1.00 20.11 O ATOM 640 CB SER A 84 43.224 55.431 19.431 1.00 23.47 C ATOM 641 OG SER A 84 41.974 55.852 19.991 1.00 20.22 O ATOM 642 N ASP A 85 44.685 57.460 20.890 1.00 23.09 N ATOM 643 CA ASP A 85 44.524 58.725 21.567 1.00 23.67 C ATOM 644 C ASP A 85 43.017 58.941 21.802 1.00 25.37 C ATOM 645 O ASP A 85 42.173 58.346 21.126 1.00 25.13 O ATOM 646 CB ASP A 85 45.094 59.806 20.680 1.00 25.96 C ATOM 647 CG ASP A 85 46.604 59.750 20.647 1.00 27.48 C ATOM 648 OD1 ASP A 85 47.232 59.418 21.655 1.00 30.66 O ATOM 649 OD2 ASP A 85 47.153 60.028 19.596 1.00 31.07 O ATOM 650 N LYS A 86 42.678 59.783 22.768 1.00 26.85 N ATOM 651 CA LYS A 86 41.312 60.126 23.118 1.00 26.19 C ATOM 652 C LYS A 86 40.479 60.597 21.934 1.00 24.69 C ATOM 653 O LYS A 86 40.923 61.373 21.085 1.00 24.39 O ATOM 654 CB LYS A 86 41.404 61.199 24.177 1.00 31.85 C ATOM 655 CG LYS A 86 40.071 61.670 24.700 1.00 36.13 C ATOM 656 CD LYS A 86 40.222 62.780 25.710 1.00 34.09 C ATOM 657 CE LYS A 86 40.437 64.086 25.023 1.00 37.70 C ATOM 658 NZ LYS A 86 40.306 65.157 25.999 1.00 40.33 N ATOM 659 N LEU A 87 39.259 60.073 21.847 1.00 25.90 N ATOM 660 CA LEU A 87 38.301 60.486 20.829 1.00 25.00 C ATOM 661 C LEU A 87 37.437 61.650 21.325 1.00 25.78 C ATOM 662 O LEU A 87 37.104 62.551 20.566 1.00 24.26 O ATOM 663 CB LEU A 87 37.443 59.274 20.468 1.00 24.49 C ATOM 664 CG LEU A 87 37.805 58.323 19.299 1.00 28.96 C ATOM 665 CD1 LEU A 87 39.266 58.251 19.009 1.00 25.49 C ATOM 666 CD2 LEU A 87 37.320 56.958 19.670 1.00 23.23 C ATOM 667 N TYR A 88 37.056 61.645 22.600 1.00 25.48 N ATOM 668 CA TYR A 88 36.277 62.681 23.271 1.00 25.06 C ATOM 669 C TYR A 88 36.307 62.335 24.747 1.00 24.27 C ATOM 670 O TYR A 88 36.715 61.222 25.156 1.00 26.64 O ATOM 671 CB TYR A 88 34.793 62.734 22.805 1.00 22.94 C ATOM 672 CG TYR A 88 33.988 61.434 22.694 1.00 17.81 C ATOM 673 CD1 TYR A 88 33.355 60.911 23.795 1.00 16.70 C ATOM 674 CD2 TYR A 88 33.996 60.769 21.477 1.00 20.25 C ATOM 675 CE1 TYR A 88 32.696 59.713 23.662 1.00 18.31 C ATOM 676 CE2 TYR A 88 33.345 59.564 21.341 1.00 21.67 C ATOM 677 CZ TYR A 88 32.709 59.044 22.445 1.00 20.42 C ATOM 678 OH TYR A 88 32.076 57.815 22.326 1.00 21.51 O ATOM 679 N ALA A 89 35.844 63.275 25.557 1.00 24.46 N ATOM 680 CA ALA A 89 35.852 63.130 27.001 1.00 24.18 C ATOM 681 C ALA A 89 34.613 62.406 27.481 1.00 22.89 C ATOM 682 O ALA A 89 33.583 62.443 26.815 1.00 23.12 O ATOM 683 CB ALA A 89 35.873 64.488 27.706 1.00 22.80 C ATOM 684 N ALA A 90 34.675 61.791 28.662 1.00 25.53 N ATOM 685 CA ALA A 90 33.540 61.112 29.280 1.00 25.10 C ATOM 686 C ALA A 90 33.469 61.515 30.751 1.00 24.64 C ATOM 687 O ALA A 90 33.548 60.660 31.647 1.00 23.09 O ATOM 688 CB ALA A 90 33.744 59.614 29.174 1.00 24.32 C ATOM 689 N ASP A 91 33.359 62.834 31.034 1.00 25.08 N ATOM 690 CA ASP A 91 33.363 63.309 32.419 1.00 22.36 C ATOM 691 C ASP A 91 31.942 63.474 32.944 1.00 18.87 C ATOM 692 O ASP A 91 30.966 63.360 32.200 1.00 19.83 O ATOM 693 CB ASP A 91 34.120 64.661 32.518 1.00 26.60 C ATOM 694 CG ASP A 91 35.503 64.672 31.860 1.00 29.42 C ATOM 695 OD1 ASP A 91 36.326 63.804 32.140 1.00 31.75 O ATOM 696 OD2 ASP A 91 35.761 65.557 31.054 1.00 34.12 O ATOM 697 N SER A 92 31.886 63.697 34.245 1.00 21.33 N ATOM 698 CA SER A 92 30.650 63.924 34.973 1.00 24.17 C ATOM 699 C SER A 92 30.468 65.401 35.268 1.00 23.52 C ATOM 700 O SER A 92 31.427 66.164 35.103 1.00 20.68 O ATOM 701 CB SER A 92 30.654 63.175 36.294 1.00 22.66 C ATOM 702 OG SER A 92 30.726 61.798 35.999 1.00 28.83 O ATOM 703 N ARG A 93 29.305 65.838 35.748 1.00 22.24 N ATOM 704 CA ARG A 93 29.080 67.253 35.965 1.00 20.46 C ATOM 705 C ARG A 93 27.852 67.332 36.832 1.00 23.59 C ATOM 706 O ARG A 93 27.012 66.417 36.790 1.00 22.33 O ATOM 707 CB ARG A 93 28.864 67.892 34.617 1.00 16.00 C ATOM 708 CG ARG A 93 29.066 69.356 34.620 1.00 16.88 C ATOM 709 CD ARG A 93 29.311 69.768 33.190 1.00 19.09 C ATOM 710 NE ARG A 93 29.424 71.213 33.202 1.00 25.22 N ATOM 711 CZ ARG A 93 29.382 71.996 32.121 1.00 28.83 C ATOM 712 NH1 ARG A 93 29.240 71.483 30.884 1.00 24.95 N ATOM 713 NH2 ARG A 93 29.403 73.337 32.319 1.00 25.27 N ATOM 714 N LEU A 94 27.799 68.365 37.681 1.00 25.18 N ATOM 715 CA LEU A 94 26.640 68.597 38.551 1.00 25.34 C ATOM 716 C LEU A 94 25.501 69.257 37.772 1.00 25.96 C ATOM 717 O LEU A 94 25.721 70.075 36.866 1.00 22.08 O ATOM 718 CB LEU A 94 27.010 69.488 39.767 1.00 18.99 C ATOM 719 CG LEU A 94 27.972 68.894 40.803 1.00 22.20 C ATOM 720 CD1 LEU A 94 28.351 69.951 41.818 1.00 21.34 C ATOM 721 CD2 LEU A 94 27.299 67.753 41.573 1.00 18.35 C ATOM 722 N ILE A 95 24.263 68.841 38.062 1.00 27.75 N ATOM 723 CA ILE A 95 23.082 69.470 37.493 1.00 27.75 C ATOM 724 C ILE A 95 22.375 70.089 38.690 1.00 25.76 C ATOM 725 O ILE A 95 22.320 69.487 39.765 1.00 21.90 O ATOM 726 CB ILE A 95 22.157 68.429 36.822 1.00 34.05 C ATOM 727 CG1 ILE A 95 22.857 67.766 35.666 1.00 38.17 C ATOM 728 CG2 ILE A 95 20.869 69.106 36.337 1.00 38.38 C ATOM 729 CD1 ILE A 95 23.437 66.455 36.231 1.00 47.36 C ATOM 730 N ALA A 96 21.888 71.318 38.553 1.00 25.56 N ATOM 731 CA ALA A 96 21.119 71.962 39.604 1.00 25.04 C ATOM 732 C ALA A 96 20.100 72.898 38.922 1.00 27.19 C ATOM 733 O ALA A 96 19.977 72.956 37.670 1.00 28.84 O ATOM 734 CB ALA A 96 22.046 72.757 40.522 1.00 18.49 C ATOM 735 N ALA A 97 19.256 73.535 39.737 1.00 27.40 N ATOM 736 CA ALA A 97 18.309 74.533 39.255 1.00 26.76 C ATOM 737 C ALA A 97 19.027 75.675 38.516 1.00 27.91 C ATOM 738 O ALA A 97 20.111 76.105 38.949 1.00 26.56 O ATOM 739 CB ALA A 97 17.551 75.089 40.460 1.00 24.48 C ATOM 740 N LYS A 98 18.474 76.138 37.377 1.00 30.07 N ATOM 741 CA LYS A 98 18.972 77.314 36.671 1.00 31.33 C ATOM 742 C LYS A 98 19.224 78.429 37.648 1.00 31.70 C ATOM 743 O LYS A 98 18.436 78.673 38.569 1.00 31.00 O ATOM 744 CB LYS A 98 17.991 77.845 35.675 1.00 34.69 C ATOM 745 CG LYS A 98 18.407 77.314 34.347 1.00 40.07 C ATOM 746 CD LYS A 98 17.505 77.709 33.207 1.00 45.03 C ATOM 747 CE LYS A 98 17.894 76.716 32.118 1.00 48.62 C ATOM 748 NZ LYS A 98 17.234 77.025 30.861 1.00 56.35 N ATOM 749 N GLY A 99 20.434 78.980 37.521 1.00 32.69 N ATOM 750 CA GLY A 99 20.840 80.091 38.372 1.00 32.59 C ATOM 751 C GLY A 99 21.424 79.705 39.722 1.00 32.75 C ATOM 752 O GLY A 99 21.726 80.610 40.513 1.00 33.80 O ATOM 753 N SER A 100 21.583 78.415 40.030 1.00 32.47 N ATOM 754 CA SER A 100 22.202 77.961 41.263 1.00 32.14 C ATOM 755 C SER A 100 23.647 78.463 41.368 1.00 29.04 C ATOM 756 O SER A 100 24.394 78.347 40.406 1.00 28.24 O ATOM 757 CB SER A 100 22.226 76.423 41.303 1.00 33.68 C ATOM 758 OG SER A 100 22.548 75.994 42.622 1.00 38.84 O ATOM 759 N PRO A 101 24.147 78.951 42.488 1.00 28.58 N ATOM 760 CA PRO A 101 25.537 79.247 42.660 1.00 30.11 C ATOM 761 C PRO A 101 26.407 78.020 42.982 1.00 34.81 C ATOM 762 O PRO A 101 27.605 78.218 43.250 1.00 37.96 O ATOM 763 CB PRO A 101 25.473 80.279 43.727 1.00 30.33 C ATOM 764 CG PRO A 101 24.460 79.665 44.647 1.00 31.12 C ATOM 765 CD PRO A 101 23.380 79.313 43.668 1.00 31.65 C ATOM 766 N ILE A 102 25.855 76.776 42.995 1.00 32.04 N ATOM 767 CA ILE A 102 26.557 75.563 43.373 1.00 29.39 C ATOM 768 C ILE A 102 27.730 75.316 42.439 1.00 27.81 C ATOM 769 O ILE A 102 27.652 75.499 41.225 1.00 24.93 O ATOM 770 CB ILE A 102 25.500 74.410 43.363 1.00 31.79 C ATOM 771 CG1 ILE A 102 25.061 74.159 44.770 1.00 33.42 C ATOM 772 CG2 ILE A 102 26.043 73.074 42.916 1.00 35.69 C ATOM 773 CD1 ILE A 102 23.851 73.203 44.819 1.00 35.80 C ATOM 774 N GLN A 103 28.822 74.833 43.034 1.00 27.21 N ATOM 775 CA GLN A 103 30.043 74.528 42.295 1.00 28.46 C ATOM 776 C GLN A 103 30.497 73.142 42.706 1.00 26.91 C ATOM 777 O GLN A 103 30.218 72.775 43.852 1.00 24.00 O ATOM 778 CB GLN A 103 31.165 75.455 42.659 1.00 29.62 C ATOM 779 CG GLN A 103 31.050 76.734 41.918 1.00 33.09 C ATOM 780 CD GLN A 103 31.303 76.536 40.453 1.00 34.83 C ATOM 781 OE1 GLN A 103 30.564 77.008 39.616 1.00 42.12 O ATOM 782 NE2 GLN A 103 32.373 75.852 40.075 1.00 38.39 N ATOM 783 N PRO A 104 31.270 72.378 41.931 1.00 25.26 N ATOM 784 CA PRO A 104 31.788 71.070 42.399 1.00 27.04 C ATOM 785 C PRO A 104 32.997 71.137 43.335 1.00 29.17 C ATOM 786 O PRO A 104 33.991 70.444 43.102 1.00 31.27 O ATOM 787 CB PRO A 104 32.050 70.292 41.093 1.00 26.80 C ATOM 788 CG PRO A 104 32.396 71.421 40.135 1.00 24.46 C ATOM 789 CD PRO A 104 31.410 72.536 40.490 1.00 22.97 C ATOM 790 N THR A 105 32.929 71.944 44.409 1.00 28.97 N ATOM 791 CA THR A 105 34.031 72.132 45.337 1.00 29.73 C ATOM 792 C THR A 105 33.485 71.718 46.671 1.00 31.28 C ATOM 793 O THR A 105 32.285 71.833 46.930 1.00 31.77 O ATOM 794 CB THR A 105 34.490 73.592 45.464 1.00 30.12 C ATOM 795 OG1 THR A 105 33.390 74.369 45.932 1.00 32.28 O ATOM 796 CG2 THR A 105 34.938 74.140 44.129 1.00 30.02 C ATOM 797 N LEU A 106 34.367 71.392 47.579 1.00 32.24 N ATOM 798 CA LEU A 106 33.933 70.919 48.857 1.00 34.61 C ATOM 799 C LEU A 106 33.353 72.096 49.623 1.00 36.74 C ATOM 800 O LEU A 106 32.409 71.957 50.380 1.00 37.36 O ATOM 801 CB LEU A 106 35.145 70.347 49.500 1.00 38.52 C ATOM 802 CG LEU A 106 34.927 69.480 50.685 1.00 44.52 C ATOM 803 CD1 LEU A 106 34.147 68.230 50.291 1.00 44.97 C ATOM 804 CD2 LEU A 106 36.284 69.137 51.259 1.00 47.76 C ATOM 805 N GLU A 107 33.851 73.289 49.339 1.00 38.81 N ATOM 806 CA GLU A 107 33.475 74.542 49.933 1.00 41.86 C ATOM 807 C GLU A 107 32.032 74.848 49.585 1.00 41.13 C ATOM 808 O GLU A 107 31.189 75.160 50.435 1.00 42.61 O ATOM 809 CB GLU A 107 34.412 75.634 49.401 1.00 49.49 C ATOM 810 CG GLU A 107 35.943 75.327 49.502 1.00 61.04 C ATOM 811 CD GLU A 107 36.600 74.499 48.372 1.00 65.59 C ATOM 812 OE1 GLU A 107 36.521 73.260 48.354 1.00 67.68 O ATOM 813 OE2 GLU A 107 37.200 75.110 47.485 1.00 69.42 O ATOM 814 N SER A 108 31.722 74.671 48.306 1.00 37.58 N ATOM 815 CA SER A 108 30.388 74.945 47.845 1.00 33.65 C ATOM 816 C SER A 108 29.392 73.874 48.260 1.00 34.58 C ATOM 817 O SER A 108 28.265 74.194 48.586 1.00 35.70 O ATOM 818 CB SER A 108 30.506 75.060 46.392 1.00 30.35 C ATOM 819 OG SER A 108 29.310 75.432 45.770 1.00 35.59 O ATOM 820 N LEU A 109 29.762 72.598 48.306 1.00 34.48 N ATOM 821 CA LEU A 109 28.830 71.526 48.547 1.00 31.28 C ATOM 822 C LEU A 109 28.575 71.223 49.989 1.00 34.83 C ATOM 823 O LEU A 109 27.606 70.523 50.296 1.00 36.04 O ATOM 824 CB LEU A 109 29.343 70.305 47.826 1.00 24.40 C ATOM 825 CG LEU A 109 29.209 70.416 46.321 1.00 22.85 C ATOM 826 CD1 LEU A 109 29.876 69.271 45.673 1.00 21.79 C ATOM 827 CD2 LEU A 109 27.746 70.436 45.941 1.00 24.31 C ATOM 828 N LYS A 110 29.341 71.715 50.943 1.00 41.05 N ATOM 829 CA LYS A 110 29.034 71.384 52.315 1.00 46.08 C ATOM 830 C LYS A 110 27.741 72.048 52.714 1.00 45.48 C ATOM 831 O LYS A 110 27.539 73.253 52.601 1.00 46.87 O ATOM 832 CB LYS A 110 30.155 71.830 53.192 1.00 51.89 C ATOM 833 CG LYS A 110 31.163 70.693 53.215 1.00 60.82 C ATOM 834 CD LYS A 110 32.483 71.219 53.733 1.00 67.80 C ATOM 835 CE LYS A 110 33.481 70.097 53.808 1.00 70.29 C ATOM 836 NZ LYS A 110 34.804 70.679 53.854 1.00 74.83 N ATOM 837 N GLY A 111 26.820 71.166 53.045 1.00 46.33 N ATOM 838 CA GLY A 111 25.485 71.560 53.452 1.00 47.54 C ATOM 839 C GLY A 111 24.449 71.057 52.457 1.00 48.27 C ATOM 840 O GLY A 111 23.273 70.831 52.786 1.00 52.21 O ATOM 841 N LYS A 112 24.890 70.824 51.227 1.00 43.87 N ATOM 842 CA LYS A 112 23.997 70.449 50.181 1.00 40.46 C ATOM 843 C LYS A 112 23.743 68.952 50.227 1.00 38.77 C ATOM 844 O LYS A 112 24.366 68.230 51.005 1.00 38.23 O ATOM 845 CB LYS A 112 24.622 70.896 48.887 1.00 42.24 C ATOM 846 CG LYS A 112 24.993 72.370 48.831 1.00 46.54 C ATOM 847 CD LYS A 112 23.848 73.340 48.647 1.00 55.48 C ATOM 848 CE LYS A 112 23.245 73.817 49.967 1.00 66.14 C ATOM 849 NZ LYS A 112 22.052 73.091 50.405 1.00 69.69 N ATOM 850 N HIS A 113 22.770 68.498 49.426 1.00 36.57 N ATOM 851 CA HIS A 113 22.337 67.111 49.331 1.00 33.76 C ATOM 852 C HIS A 113 22.532 66.894 47.855 1.00 31.68 C ATOM 853 O HIS A 113 21.968 67.625 47.034 1.00 27.98 O ATOM 854 CB HIS A 113 20.855 66.903 49.650 1.00 38.14 C ATOM 855 CG HIS A 113 20.525 67.523 51.000 1.00 47.24 C ATOM 856 ND1 HIS A 113 19.903 68.676 51.271 1.00 52.05 N ATOM 857 CD2 HIS A 113 20.978 67.023 52.198 1.00 48.57 C ATOM 858 CE1 HIS A 113 19.991 68.886 52.571 1.00 53.20 C ATOM 859 NE2 HIS A 113 20.646 67.879 53.119 1.00 52.70 N ATOM 860 N VAL A 114 23.400 65.937 47.548 1.00 30.03 N ATOM 861 CA VAL A 114 23.799 65.626 46.196 1.00 27.17 C ATOM 862 C VAL A 114 23.305 64.229 45.923 1.00 26.46 C ATOM 863 O VAL A 114 23.550 63.331 46.719 1.00 28.87 O ATOM 864 CB VAL A 114 25.352 65.684 46.049 1.00 25.43 C ATOM 865 CG1 VAL A 114 25.677 65.539 44.549 1.00 22.72 C ATOM 866 CG2 VAL A 114 25.940 66.993 46.639 1.00 26.37 C ATOM 867 N GLY A 115 22.610 63.976 44.841 1.00 25.66 N ATOM 868 CA GLY A 115 22.147 62.638 44.575 1.00 21.40 C ATOM 869 C GLY A 115 23.080 62.034 43.576 1.00 23.75 C ATOM 870 O GLY A 115 23.619 62.696 42.676 1.00 22.39 O ATOM 871 N VAL A 116 23.227 60.734 43.734 1.00 25.70 N ATOM 872 CA VAL A 116 24.115 59.976 42.892 1.00 26.58 C ATOM 873 C VAL A 116 23.408 58.634 42.615 1.00 28.14 C ATOM 874 O VAL A 116 22.565 58.159 43.401 1.00 28.75 O ATOM 875 CB VAL A 116 25.459 59.955 43.735 1.00 26.53 C ATOM 876 CG1 VAL A 116 25.602 58.742 44.646 1.00 24.45 C ATOM 877 CG2 VAL A 116 26.562 60.139 42.765 1.00 24.04 C ATOM 878 N LEU A 117 23.636 58.026 41.457 1.00 28.86 N ATOM 879 CA LEU A 117 23.089 56.711 41.161 1.00 31.66 C ATOM 880 C LEU A 117 23.867 55.612 41.913 1.00 31.82 C ATOM 881 O LEU A 117 25.091 55.587 41.912 1.00 30.61 O ATOM 882 CB LEU A 117 23.160 56.471 39.699 1.00 28.14 C ATOM 883 CG LEU A 117 22.384 55.288 39.261 1.00 32.32 C ATOM 884 CD1 LEU A 117 20.899 55.526 39.410 1.00 34.58 C ATOM 885 CD2 LEU A 117 22.730 55.052 37.815 1.00 35.77 C ATOM 886 N GLN A 118 23.184 54.673 42.554 1.00 31.91 N ATOM 887 CA GLN A 118 23.904 53.717 43.336 1.00 32.63 C ATOM 888 C GLN A 118 24.692 52.770 42.414 1.00 30.64 C ATOM 889 O GLN A 118 24.251 52.366 41.343 1.00 29.42 O ATOM 890 CB GLN A 118 22.896 53.015 44.166 1.00 33.51 C ATOM 891 CG GLN A 118 23.541 52.352 45.331 1.00 39.19 C ATOM 892 CD GLN A 118 22.563 51.422 45.993 1.00 43.07 C ATOM 893 OE1 GLN A 118 21.787 50.703 45.354 1.00 44.69 O ATOM 894 NE2 GLN A 118 22.598 51.469 47.315 1.00 46.54 N ATOM 895 N GLY A 119 25.906 52.496 42.828 1.00 31.05 N ATOM 896 CA GLY A 119 26.825 51.633 42.136 1.00 33.87 C ATOM 897 C GLY A 119 27.509 52.265 40.919 1.00 36.08 C ATOM 898 O GLY A 119 28.194 51.557 40.161 1.00 35.30 O ATOM 899 N SER A 120 27.342 53.559 40.616 1.00 35.22 N ATOM 900 CA SER A 120 28.044 54.049 39.460 1.00 32.03 C ATOM 901 C SER A 120 29.402 54.666 39.835 1.00 30.69 C ATOM 902 O SER A 120 29.777 54.811 40.999 1.00 29.31 O ATOM 903 CB SER A 120 27.044 55.021 38.739 1.00 34.67 C ATOM 904 OG SER A 120 26.809 56.380 39.126 1.00 29.16 O ATOM 905 N THR A 121 30.178 55.049 38.823 1.00 29.77 N ATOM 906 CA THR A 121 31.469 55.705 38.991 1.00 28.77 C ATOM 907 C THR A 121 31.271 57.019 39.692 1.00 24.99 C ATOM 908 O THR A 121 32.068 57.416 40.517 1.00 29.29 O ATOM 909 CB THR A 121 32.121 55.950 37.635 1.00 28.37 C ATOM 910 OG1 THR A 121 31.144 56.543 36.795 1.00 32.60 O ATOM 911 CG2 THR A 121 32.537 54.668 36.953 1.00 30.32 C ATOM 912 N GLN A 122 30.157 57.705 39.387 1.00 26.57 N ATOM 913 CA GLN A 122 29.813 58.931 40.098 1.00 26.25 C ATOM 914 C GLN A 122 29.701 58.773 41.598 1.00 25.55 C ATOM 915 O GLN A 122 30.231 59.629 42.295 1.00 26.60 O ATOM 916 CB GLN A 122 28.485 59.539 39.577 1.00 22.72 C ATOM 917 CG GLN A 122 28.668 60.156 38.208 1.00 19.38 C ATOM 918 CD GLN A 122 28.647 59.155 37.089 1.00 26.89 C ATOM 919 OE1 GLN A 122 29.062 59.395 35.971 1.00 26.86 O ATOM 920 NE2 GLN A 122 28.080 57.972 37.222 1.00 25.00 N ATOM 921 N GLU A 123 29.150 57.684 42.152 1.00 28.09 N ATOM 922 CA GLU A 123 28.978 57.453 43.593 1.00 27.20 C ATOM 923 C GLU A 123 30.356 57.177 44.117 1.00 25.65 C ATOM 924 O GLU A 123 30.702 57.722 45.157 1.00 25.60 O ATOM 925 CB GLU A 123 28.139 56.234 43.919 1.00 25.46 C ATOM 926 CG GLU A 123 27.972 55.791 45.312 1.00 30.92 C ATOM 927 CD GLU A 123 27.333 54.423 45.426 1.00 32.69 C ATOM 928 OE1 GLU A 123 27.579 53.541 44.619 1.00 35.34 O ATOM 929 OE2 GLU A 123 26.530 54.217 46.313 1.00 37.91 O ATOM 930 N ALA A 124 31.190 56.413 43.410 1.00 26.43 N ATOM 931 CA ALA A 124 32.547 56.210 43.872 1.00 25.89 C ATOM 932 C ALA A 124 33.337 57.500 44.061 1.00 25.12 C ATOM 933 O ALA A 124 33.929 57.758 45.117 1.00 27.75 O ATOM 934 CB ALA A 124 33.258 55.318 42.867 1.00 25.04 C ATOM 935 N TYR A 125 33.262 58.382 43.081 1.00 26.91 N ATOM 936 CA TYR A 125 33.906 59.690 43.126 1.00 27.11 C ATOM 937 C TYR A 125 33.344 60.518 44.262 1.00 27.41 C ATOM 938 O TYR A 125 34.076 61.098 45.067 1.00 27.94 O ATOM 939 CB TYR A 125 33.686 60.421 41.788 1.00 25.84 C ATOM 940 CG TYR A 125 34.249 61.828 41.815 1.00 30.51 C ATOM 941 CD1 TYR A 125 35.582 62.003 41.523 1.00 30.85 C ATOM 942 CD2 TYR A 125 33.463 62.922 42.184 1.00 29.56 C ATOM 943 CE1 TYR A 125 36.149 63.263 41.598 1.00 30.92 C ATOM 944 CE2 TYR A 125 34.032 64.175 42.265 1.00 31.81 C ATOM 945 CZ TYR A 125 35.373 64.330 41.963 1.00 33.27 C ATOM 946 OH TYR A 125 35.965 65.579 41.985 1.00 39.51 O ATOM 947 N ALA A 126 32.005 60.590 44.329 1.00 30.78 N ATOM 948 CA ALA A 126 31.313 61.411 45.314 1.00 30.61 C ATOM 949 C ALA A 126 31.545 60.884 46.715 1.00 30.48 C ATOM 950 O ALA A 126 31.712 61.662 47.659 1.00 32.86 O ATOM 951 CB ALA A 126 29.822 61.408 45.077 1.00 28.35 C ATOM 952 N ASN A 127 31.621 59.575 46.890 1.00 33.11 N ATOM 953 CA ASN A 127 31.834 58.978 48.201 1.00 35.20 C ATOM 954 C ASN A 127 33.234 59.285 48.708 1.00 32.89 C ATOM 955 O ASN A 127 33.368 59.876 49.779 1.00 31.13 O ATOM 956 CB ASN A 127 31.579 57.460 48.110 1.00 38.43 C ATOM 957 CG ASN A 127 30.102 57.023 48.228 1.00 42.80 C ATOM 958 OD1 ASN A 127 29.163 57.763 48.526 1.00 43.05 O ATOM 959 ND2 ASN A 127 29.787 55.772 47.968 1.00 45.07 N ATOM 960 N ASP A 128 34.286 59.051 47.910 1.00 36.51 N ATOM 961 CA ASP A 128 35.668 59.331 48.328 1.00 38.76 C ATOM 962 C ASP A 128 35.996 60.797 48.431 1.00 38.36 C ATOM 963 O ASP A 128 36.659 61.206 49.382 1.00 40.15 O ATOM 964 CB ASP A 128 36.723 58.755 47.372 1.00 42.16 C ATOM 965 CG ASP A 128 36.670 57.253 47.146 1.00 47.95 C ATOM 966 OD1 ASP A 128 36.008 56.549 47.906 1.00 51.93 O ATOM 967 OD2 ASP A 128 37.282 56.772 46.193 1.00 52.59 O ATOM 968 N ASN A 129 35.585 61.612 47.464 1.00 37.40 N ATOM 969 CA ASN A 129 35.921 63.014 47.506 1.00 35.89 C ATOM 970 C ASN A 129 34.988 63.884 48.332 1.00 35.65 C ATOM 971 O ASN A 129 35.417 64.931 48.840 1.00 36.00 O ATOM 972 CB ASN A 129 35.950 63.595 46.118 1.00 39.94 C ATOM 973 CG ASN A 129 36.980 62.997 45.171 1.00 45.15 C ATOM 974 OD1 ASN A 129 36.968 61.811 44.840 1.00 45.54 O ATOM 975 ND2 ASN A 129 37.898 63.783 44.619 1.00 48.71 N ATOM 976 N TRP A 130 33.716 63.515 48.497 1.00 31.59 N ATOM 977 CA TRP A 130 32.786 64.434 49.110 1.00 29.40 C ATOM 978 C TRP A 130 32.089 63.859 50.315 1.00 26.40 C ATOM 979 O TRP A 130 32.113 64.482 51.379 1.00 26.12 O ATOM 980 CB TRP A 130 31.709 64.912 48.076 1.00 29.76 C ATOM 981 CG TRP A 130 32.150 65.756 46.856 1.00 29.58 C ATOM 982 CD1 TRP A 130 33.327 66.474 46.822 1.00 25.67 C ATOM 983 CD2 TRP A 130 31.429 65.875 45.667 1.00 27.95 C ATOM 984 NE1 TRP A 130 33.349 67.009 45.630 1.00 24.93 N ATOM 985 CE2 TRP A 130 32.266 66.677 44.910 1.00 22.81 C ATOM 986 CE3 TRP A 130 30.229 65.405 45.136 1.00 22.91 C ATOM 987 CZ2 TRP A 130 31.921 67.043 43.630 1.00 20.34 C ATOM 988 CZ3 TRP A 130 29.886 65.764 43.854 1.00 19.17 C ATOM 989 CH2 TRP A 130 30.728 66.577 43.108 1.00 22.31 C ATOM 990 N ARG A 131 31.473 62.693 50.258 1.00 26.95 N ATOM 991 CA ARG A 131 30.795 62.166 51.427 1.00 28.43 C ATOM 992 C ARG A 131 31.724 61.940 52.639 1.00 29.82 C ATOM 993 O ARG A 131 31.360 62.311 53.768 1.00 30.29 O ATOM 994 CB ARG A 131 30.121 60.894 51.011 1.00 29.78 C ATOM 995 CG ARG A 131 29.245 60.395 52.128 1.00 33.93 C ATOM 996 CD ARG A 131 28.653 59.117 51.630 1.00 39.22 C ATOM 997 NE ARG A 131 28.843 58.208 52.714 1.00 48.93 N ATOM 998 CZ ARG A 131 29.953 57.489 52.834 1.00 52.88 C ATOM 999 NH1 ARG A 131 30.987 57.493 51.988 1.00 55.17 N ATOM 1000 NH2 ARG A 131 30.066 56.825 53.950 1.00 58.96 N ATOM 1001 N THR A 132 32.963 61.455 52.459 1.00 28.34 N ATOM 1002 CA THR A 132 33.890 61.320 53.572 1.00 28.40 C ATOM 1003 C THR A 132 34.217 62.671 54.225 1.00 30.04 C ATOM 1004 O THR A 132 34.582 62.762 55.404 1.00 29.65 O ATOM 1005 CB THR A 132 35.101 60.612 53.012 1.00 25.39 C ATOM 1006 OG1 THR A 132 35.457 61.277 51.828 1.00 27.84 O ATOM 1007 CG2 THR A 132 34.796 59.179 52.658 1.00 28.36 C ATOM 1008 N LYS A 133 34.035 63.766 53.475 1.00 31.74 N ATOM 1009 CA LYS A 133 34.337 65.080 53.972 1.00 29.76 C ATOM 1010 C LYS A 133 33.077 65.762 54.444 1.00 33.12 C ATOM 1011 O LYS A 133 33.100 66.964 54.685 1.00 37.46 O ATOM 1012 CB LYS A 133 34.977 65.885 52.893 1.00 28.08 C ATOM 1013 CG LYS A 133 36.173 65.222 52.224 1.00 33.22 C ATOM 1014 CD LYS A 133 37.381 65.005 53.124 1.00 34.44 C ATOM 1015 CE LYS A 133 38.529 64.429 52.282 1.00 35.84 C ATOM 1016 NZ LYS A 133 38.232 63.136 51.676 1.00 39.18 N ATOM 1017 N GLY A 134 31.958 65.070 54.637 1.00 35.59 N ATOM 1018 CA GLY A 134 30.771 65.698 55.185 1.00 36.64 C ATOM 1019 C GLY A 134 29.766 66.282 54.194 1.00 38.80 C ATOM 1020 O GLY A 134 28.843 66.999 54.620 1.00 43.50 O ATOM 1021 N VAL A 135 29.882 66.075 52.881 1.00 35.53 N ATOM 1022 CA VAL A 135 28.817 66.486 51.980 1.00 32.75 C ATOM 1023 C VAL A 135 27.764 65.369 52.130 1.00 32.91 C ATOM 1024 O VAL A 135 28.125 64.195 52.280 1.00 28.90 O ATOM 1025 CB VAL A 135 29.366 66.565 50.552 1.00 30.82 C ATOM 1026 CG1 VAL A 135 28.254 66.874 49.550 1.00 26.23 C ATOM 1027 CG2 VAL A 135 30.453 67.636 50.526 1.00 29.63 C ATOM 1028 N ASP A 136 26.457 65.650 52.108 1.00 31.50 N ATOM 1029 CA ASP A 136 25.460 64.611 52.261 1.00 29.93 C ATOM 1030 C ASP A 136 25.180 64.047 50.894 1.00 28.19 C ATOM 1031 O ASP A 136 24.452 64.638 50.094 1.00 27.36 O ATOM 1032 CB ASP A 136 24.196 65.192 52.862 1.00 36.85 C ATOM 1033 CG ASP A 136 23.120 64.128 53.000 1.00 47.29 C ATOM 1034 OD1 ASP A 136 23.406 63.063 53.567 1.00 56.38 O ATOM 1035 OD2 ASP A 136 21.998 64.348 52.533 1.00 50.90 O ATOM 1036 N VAL A 137 25.742 62.889 50.610 1.00 25.72 N ATOM 1037 CA VAL A 137 25.632 62.320 49.284 1.00 27.98 C ATOM 1038 C VAL A 137 24.571 61.257 49.422 1.00 29.98 C ATOM 1039 O VAL A 137 24.693 60.463 50.356 1.00 32.96 O ATOM 1040 CB VAL A 137 26.972 61.692 48.846 1.00 28.60 C ATOM 1041 CG1 VAL A 137 26.780 61.007 47.493 1.00 25.51 C ATOM 1042 CG2 VAL A 137 28.070 62.768 48.763 1.00 26.30 C ATOM 1043 N VAL A 138 23.541 61.207 48.574 1.00 30.11 N ATOM 1044 CA VAL A 138 22.477 60.224 48.700 1.00 28.42 C ATOM 1045 C VAL A 138 22.445 59.349 47.460 1.00 25.79 C ATOM 1046 O VAL A 138 22.356 59.842 46.330 1.00 27.25 O ATOM 1047 CB VAL A 138 21.152 60.980 48.892 1.00 31.36 C ATOM 1048 CG1 VAL A 138 20.015 59.985 49.063 1.00 27.05 C ATOM 1049 CG2 VAL A 138 21.276 61.922 50.095 1.00 30.37 C ATOM 1050 N ALA A 139 22.477 58.035 47.610 1.00 25.66 N ATOM 1051 CA ALA A 139 22.563 57.161 46.463 1.00 27.22 C ATOM 1052 C ALA A 139 21.194 56.612 46.135 1.00 28.49 C ATOM 1053 O ALA A 139 20.464 56.234 47.057 1.00 27.66 O ATOM 1054 CB ALA A 139 23.507 56.043 46.784 1.00 29.67 C ATOM 1055 N TYR A 140 20.853 56.580 44.851 1.00 28.17 N ATOM 1056 CA TYR A 140 19.517 56.246 44.395 1.00 30.32 C ATOM 1057 C TYR A 140 19.542 54.984 43.588 1.00 32.17 C ATOM 1058 O TYR A 140 20.487 54.786 42.825 1.00 31.46 O ATOM 1059 CB TYR A 140 18.932 57.307 43.495 1.00 26.16 C ATOM 1060 CG TYR A 140 18.501 58.534 44.279 1.00 27.65 C ATOM 1061 CD1 TYR A 140 19.437 59.353 44.874 1.00 22.61 C ATOM 1062 CD2 TYR A 140 17.145 58.809 44.415 1.00 27.87 C ATOM 1063 CE1 TYR A 140 19.031 60.442 45.604 1.00 26.23 C ATOM 1064 CE2 TYR A 140 16.736 59.909 45.143 1.00 27.58 C ATOM 1065 CZ TYR A 140 17.691 60.711 45.731 1.00 26.75 C ATOM 1066 OH TYR A 140 17.302 61.801 46.473 1.00 29.74 O ATOM 1067 N ALA A 141 18.518 54.147 43.721 1.00 32.26 N ATOM 1068 CA ALA A 141 18.444 52.917 42.972 1.00 32.78 C ATOM 1069 C ALA A 141 18.136 53.215 41.523 1.00 34.35 C ATOM 1070 O ALA A 141 18.417 52.454 40.593 1.00 37.75 O ATOM 1071 CB ALA A 141 17.336 52.071 43.520 1.00 34.20 C ATOM 1072 N ASN A 142 17.536 54.364 41.279 1.00 37.97 N ATOM 1073 CA ASN A 142 17.039 54.636 39.966 1.00 40.84 C ATOM 1074 C ASN A 142 17.157 56.091 39.569 1.00 42.14 C ATOM 1075 O ASN A 142 16.883 57.002 40.338 1.00 41.10 O ATOM 1076 CB ASN A 142 15.617 54.085 40.016 1.00 45.52 C ATOM 1077 CG ASN A 142 14.604 54.839 39.203 1.00 51.90 C ATOM 1078 OD1 ASN A 142 13.804 55.586 39.757 1.00 57.36 O ATOM 1079 ND2 ASN A 142 14.618 54.753 37.876 1.00 56.52 N ATOM 1080 N GLN A 143 17.534 56.316 38.320 1.00 43.63 N ATOM 1081 CA GLN A 143 17.721 57.640 37.773 1.00 43.98 C ATOM 1082 C GLN A 143 16.468 58.487 37.781 1.00 42.88 C ATOM 1083 O GLN A 143 16.571 59.688 38.025 1.00 40.16 O ATOM 1084 CB GLN A 143 18.255 57.487 36.374 1.00 46.02 C ATOM 1085 CG GLN A 143 18.925 58.722 35.808 1.00 53.59 C ATOM 1086 CD GLN A 143 20.049 59.294 36.671 1.00 58.29 C ATOM 1087 OE1 GLN A 143 21.151 58.747 36.803 1.00 59.14 O ATOM 1088 NE2 GLN A 143 19.745 60.434 37.286 1.00 59.44 N ATOM 1089 N ASP A 144 15.288 57.889 37.580 1.00 43.42 N ATOM 1090 CA ASP A 144 14.015 58.614 37.625 1.00 44.71 C ATOM 1091 C ASP A 144 13.765 59.331 38.923 1.00 41.51 C ATOM 1092 O ASP A 144 13.345 60.489 38.943 1.00 41.53 O ATOM 1093 CB ASP A 144 12.824 57.698 37.420 1.00 50.97 C ATOM 1094 CG ASP A 144 12.773 57.209 35.989 1.00 61.28 C ATOM 1095 OD1 ASP A 144 12.529 58.050 35.118 1.00 65.49 O ATOM 1096 OD2 ASP A 144 12.991 56.012 35.744 1.00 67.00 O ATOM 1097 N LEU A 145 14.039 58.627 40.011 1.00 38.86 N ATOM 1098 CA LEU A 145 13.877 59.173 41.341 1.00 37.24 C ATOM 1099 C LEU A 145 14.858 60.284 41.636 1.00 36.39 C ATOM 1100 O LEU A 145 14.572 61.129 42.482 1.00 35.11 O ATOM 1101 CB LEU A 145 14.072 58.107 42.370 1.00 39.38 C ATOM 1102 CG LEU A 145 12.954 57.880 43.342 1.00 44.38 C ATOM 1103 CD1 LEU A 145 13.418 56.793 44.277 1.00 47.58 C ATOM 1104 CD2 LEU A 145 12.604 59.128 44.135 1.00 45.93 C ATOM 1105 N ILE A 146 16.034 60.284 40.998 1.00 36.09 N ATOM 1106 CA ILE A 146 16.986 61.382 41.185 1.00 34.85 C ATOM 1107 C ILE A 146 16.363 62.637 40.578 1.00 32.19 C ATOM 1108 O ILE A 146 16.255 63.687 41.220 1.00 31.41 O ATOM 1109 CB ILE A 146 18.369 61.105 40.486 1.00 35.11 C ATOM 1110 CG1 ILE A 146 19.077 59.906 41.109 1.00 33.45 C ATOM 1111 CG2 ILE A 146 19.272 62.329 40.655 1.00 35.55 C ATOM 1112 CD1 ILE A 146 20.397 59.488 40.428 1.00 33.93 C ATOM 1113 N TYR A 147 15.916 62.509 39.339 1.00 30.89 N ATOM 1114 CA TYR A 147 15.355 63.630 38.632 1.00 32.92 C ATOM 1115 C TYR A 147 14.110 64.175 39.310 1.00 34.65 C ATOM 1116 O TYR A 147 13.990 65.408 39.458 1.00 33.55 O ATOM 1117 CB TYR A 147 15.105 63.172 37.194 1.00 33.87 C ATOM 1118 CG TYR A 147 16.413 63.044 36.396 1.00 38.00 C ATOM 1119 CD1 TYR A 147 17.543 63.770 36.777 1.00 38.26 C ATOM 1120 CD2 TYR A 147 16.470 62.212 35.285 1.00 36.64 C ATOM 1121 CE1 TYR A 147 18.708 63.669 36.061 1.00 40.53 C ATOM 1122 CE2 TYR A 147 17.638 62.110 34.556 1.00 40.29 C ATOM 1123 CZ TYR A 147 18.753 62.836 34.949 1.00 43.87 C ATOM 1124 OH TYR A 147 19.940 62.739 34.220 1.00 46.04 O ATOM 1125 N SER A 148 13.249 63.309 39.864 1.00 36.65 N ATOM 1126 CA SER A 148 12.058 63.792 40.531 1.00 38.60 C ATOM 1127 C SER A 148 12.418 64.445 41.847 1.00 35.84 C ATOM 1128 O SER A 148 11.841 65.484 42.191 1.00 37.18 O ATOM 1129 CB SER A 148 11.101 62.635 40.729 1.00 40.43 C ATOM 1130 OG SER A 148 11.735 61.543 41.365 1.00 53.00 O ATOM 1131 N ASP A 149 13.392 63.927 42.584 1.00 33.83 N ATOM 1132 CA ASP A 149 13.809 64.602 43.803 1.00 34.74 C ATOM 1133 C ASP A 149 14.453 65.964 43.602 1.00 32.48 C ATOM 1134 O ASP A 149 14.282 66.872 44.426 1.00 31.41 O ATOM 1135 CB ASP A 149 14.767 63.711 44.586 1.00 36.55 C ATOM 1136 CG ASP A 149 14.050 62.649 45.390 1.00 40.35 C ATOM 1137 OD1 ASP A 149 12.943 62.269 45.026 1.00 46.80 O ATOM 1138 OD2 ASP A 149 14.591 62.184 46.379 1.00 39.93 O ATOM 1139 N LEU A 150 15.207 66.114 42.522 1.00 34.15 N ATOM 1140 CA LEU A 150 15.832 67.383 42.139 1.00 35.69 C ATOM 1141 C LEU A 150 14.692 68.331 41.816 1.00 35.93 C ATOM 1142 O LEU A 150 14.601 69.391 42.402 1.00 35.58 O ATOM 1143 CB LEU A 150 16.679 67.221 40.888 1.00 34.65 C ATOM 1144 CG LEU A 150 18.025 67.873 40.700 1.00 32.38 C ATOM 1145 CD1 LEU A 150 18.203 67.883 39.210 1.00 30.24 C ATOM 1146 CD2 LEU A 150 18.147 69.266 41.236 1.00 28.90 C ATOM 1147 N THR A 151 13.797 67.902 40.935 1.00 37.51 N ATOM 1148 CA THR A 151 12.608 68.640 40.549 1.00 40.47 C ATOM 1149 C THR A 151 11.735 69.066 41.723 1.00 40.86 C ATOM 1150 O THR A 151 11.226 70.176 41.768 1.00 43.00 O ATOM 1151 CB THR A 151 11.923 67.703 39.573 1.00 42.92 C ATOM 1152 OG1 THR A 151 12.679 67.879 38.364 1.00 43.87 O ATOM 1153 CG2 THR A 151 10.425 67.880 39.479 1.00 47.99 C ATOM 1154 N ALA A 152 11.600 68.182 42.697 1.00 41.44 N ATOM 1155 CA ALA A 152 10.864 68.407 43.925 1.00 40.44 C ATOM 1156 C ALA A 152 11.619 69.236 44.966 1.00 40.19 C ATOM 1157 O ALA A 152 11.105 69.527 46.057 1.00 40.65 O ATOM 1158 CB ALA A 152 10.516 67.042 44.530 1.00 42.07 C ATOM 1159 N GLY A 153 12.887 69.565 44.715 1.00 37.70 N ATOM 1160 CA GLY A 153 13.627 70.355 45.675 1.00 35.16 C ATOM 1161 C GLY A 153 14.148 69.548 46.835 1.00 37.36 C ATOM 1162 O GLY A 153 14.659 70.135 47.801 1.00 37.11 O ATOM 1163 N ARG A 154 14.070 68.210 46.731 1.00 37.56 N ATOM 1164 CA ARG A 154 14.649 67.326 47.742 1.00 39.45 C ATOM 1165 C ARG A 154 16.173 67.221 47.688 1.00 37.67 C ATOM 1166 O ARG A 154 16.863 66.946 48.682 1.00 38.81 O ATOM 1167 CB ARG A 154 14.111 65.931 47.622 1.00 42.13 C ATOM 1168 CG ARG A 154 12.709 65.762 48.187 1.00 51.79 C ATOM 1169 CD ARG A 154 12.629 64.264 48.411 1.00 61.16 C ATOM 1170 NE ARG A 154 11.376 63.765 48.952 1.00 68.08 N ATOM 1171 CZ ARG A 154 11.082 63.817 50.256 1.00 70.71 C ATOM 1172 NH1 ARG A 154 11.930 64.361 51.148 1.00 71.23 N ATOM 1173 NH2 ARG A 154 9.927 63.279 50.662 1.00 69.69 N ATOM 1174 N LEU A 155 16.725 67.451 46.510 1.00 34.60 N ATOM 1175 CA LEU A 155 18.157 67.401 46.294 1.00 29.78 C ATOM 1176 C LEU A 155 18.587 68.776 45.867 1.00 29.79 C ATOM 1177 O LEU A 155 17.843 69.442 45.147 1.00 29.65 O ATOM 1178 CB LEU A 155 18.543 66.471 45.160 1.00 28.06 C ATOM 1179 CG LEU A 155 18.403 64.983 45.302 1.00 23.62 C ATOM 1180 CD1 LEU A 155 18.676 64.374 43.950 1.00 23.44 C ATOM 1181 CD2 LEU A 155 19.302 64.482 46.397 1.00 21.76 C ATOM 1182 N ASP A 156 19.808 69.162 46.218 1.00 28.30 N ATOM 1183 CA ASP A 156 20.369 70.399 45.704 1.00 29.30 C ATOM 1184 C ASP A 156 21.053 70.233 44.349 1.00 28.38 C ATOM 1185 O ASP A 156 21.110 71.173 43.559 1.00 28.84 O ATOM 1186 CB ASP A 156 21.370 70.949 46.684 1.00 31.82 C ATOM 1187 CG ASP A 156 20.680 71.334 47.969 1.00 34.00 C ATOM 1188 OD1 ASP A 156 19.879 72.255 47.917 1.00 43.10 O ATOM 1189 OD2 ASP A 156 20.919 70.730 49.007 1.00 37.05 O ATOM 1190 N ALA A 157 21.598 69.071 44.038 1.00 25.52 N ATOM 1191 CA ALA A 157 22.319 68.830 42.806 1.00 25.68 C ATOM 1192 C ALA A 157 22.393 67.321 42.633 1.00 25.99 C ATOM 1193 O ALA A 157 22.175 66.528 43.579 1.00 26.52 O ATOM 1194 CB ALA A 157 23.739 69.362 42.887 1.00 21.79 C ATOM 1195 N ALA A 158 22.698 66.940 41.403 1.00 23.79 N ATOM 1196 CA ALA A 158 22.900 65.555 41.074 1.00 24.18 C ATOM 1197 C ALA A 158 24.223 65.464 40.321 1.00 24.34 C ATOM 1198 O ALA A 158 24.493 66.312 39.466 1.00 24.24 O ATOM 1199 CB ALA A 158 21.772 65.081 40.185 1.00 24.98 C ATOM 1200 N LEU A 159 25.098 64.508 40.637 1.00 22.98 N ATOM 1201 CA LEU A 159 26.298 64.325 39.836 1.00 23.30 C ATOM 1202 C LEU A 159 25.955 63.272 38.814 1.00 24.71 C ATOM 1203 O LEU A 159 25.627 62.144 39.193 1.00 25.18 O ATOM 1204 CB LEU A 159 27.495 63.812 40.639 1.00 23.61 C ATOM 1205 CG LEU A 159 28.855 63.629 39.958 1.00 20.40 C ATOM 1206 CD1 LEU A 159 29.343 64.950 39.387 1.00 21.77 C ATOM 1207 CD2 LEU A 159 29.858 63.128 40.990 1.00 21.43 C ATOM 1208 N GLN A 160 26.067 63.600 37.535 1.00 24.83 N ATOM 1209 CA GLN A 160 25.766 62.665 36.482 1.00 27.98 C ATOM 1210 C GLN A 160 26.826 62.717 35.408 1.00 25.67 C ATOM 1211 O GLN A 160 27.653 63.631 35.394 1.00 26.85 O ATOM 1212 CB GLN A 160 24.448 62.996 35.818 1.00 34.39 C ATOM 1213 CG GLN A 160 23.367 61.932 35.935 1.00 43.04 C ATOM 1214 CD GLN A 160 22.552 62.119 37.186 1.00 45.97 C ATOM 1215 OE1 GLN A 160 21.763 63.059 37.242 1.00 51.56 O ATOM 1216 NE2 GLN A 160 22.635 61.260 38.194 1.00 49.40 N ATOM 1217 N ASP A 161 26.809 61.724 34.527 1.00 22.09 N ATOM 1218 CA ASP A 161 27.594 61.743 33.321 1.00 22.81 C ATOM 1219 C ASP A 161 27.153 62.970 32.512 1.00 23.28 C ATOM 1220 O ASP A 161 25.953 63.159 32.287 1.00 23.07 O ATOM 1221 CB ASP A 161 27.346 60.492 32.481 1.00 22.27 C ATOM 1222 CG ASP A 161 28.121 60.556 31.174 1.00 24.14 C ATOM 1223 OD1 ASP A 161 29.340 60.476 31.228 1.00 29.16 O ATOM 1224 OD2 ASP A 161 27.546 60.745 30.102 1.00 25.18 O ATOM 1225 N GLU A 162 28.066 63.765 31.954 1.00 23.48 N ATOM 1226 CA GLU A 162 27.693 65.023 31.302 1.00 25.07 C ATOM 1227 C GLU A 162 26.865 64.836 30.049 1.00 24.42 C ATOM 1228 O GLU A 162 25.794 65.415 29.872 1.00 25.46 O ATOM 1229 CB GLU A 162 28.975 65.797 30.998 1.00 26.53 C ATOM 1230 CG GLU A 162 28.851 67.139 30.275 1.00 27.46 C ATOM 1231 CD GLU A 162 30.203 67.838 30.057 1.00 32.20 C ATOM 1232 OE1 GLU A 162 31.264 67.206 30.093 1.00 26.30 O ATOM 1233 OE2 GLU A 162 30.209 69.046 29.823 1.00 32.72 O ATOM 1234 N VAL A 163 27.290 63.959 29.146 1.00 26.72 N ATOM 1235 CA VAL A 163 26.566 63.784 27.910 1.00 26.27 C ATOM 1236 C VAL A 163 25.229 63.123 28.202 1.00 27.68 C ATOM 1237 O VAL A 163 24.226 63.483 27.596 1.00 27.58 O ATOM 1238 CB VAL A 163 27.395 62.951 26.914 1.00 23.32 C ATOM 1239 CG1 VAL A 163 26.550 62.619 25.697 1.00 27.65 C ATOM 1240 CG2 VAL A 163 28.546 63.784 26.360 1.00 22.99 C ATOM 1241 N ALA A 164 25.171 62.232 29.181 1.00 29.01 N ATOM 1242 CA ALA A 164 23.920 61.571 29.495 1.00 30.47 C ATOM 1243 C ALA A 164 22.904 62.558 30.059 1.00 31.24 C ATOM 1244 O ALA A 164 21.743 62.550 29.652 1.00 34.02 O ATOM 1245 CB ALA A 164 24.171 60.468 30.512 1.00 31.12 C ATOM 1246 N ALA A 165 23.339 63.423 30.966 1.00 29.45 N ATOM 1247 CA ALA A 165 22.520 64.473 31.516 1.00 28.38 C ATOM 1248 C ALA A 165 22.087 65.426 30.424 1.00 29.30 C ATOM 1249 O ALA A 165 20.943 65.882 30.447 1.00 30.70 O ATOM 1250 CB ALA A 165 23.307 65.245 32.523 1.00 27.93 C ATOM 1251 N SER A 166 22.938 65.755 29.452 1.00 30.63 N ATOM 1252 CA SER A 166 22.553 66.654 28.370 1.00 36.41 C ATOM 1253 C SER A 166 21.416 66.101 27.538 1.00 37.00 C ATOM 1254 O SER A 166 20.299 66.629 27.519 1.00 36.47 O ATOM 1255 CB SER A 166 23.704 66.937 27.396 1.00 38.04 C ATOM 1256 OG SER A 166 24.771 67.624 28.026 1.00 48.50 O ATOM 1257 N GLU A 167 21.704 64.937 26.982 1.00 37.70 N ATOM 1258 CA GLU A 167 20.799 64.293 26.066 1.00 41.21 C ATOM 1259 C GLU A 167 19.544 63.875 26.770 1.00 41.75 C ATOM 1260 O GLU A 167 18.433 64.161 26.342 1.00 45.12 O ATOM 1261 CB GLU A 167 21.465 63.076 25.462 1.00 40.64 C ATOM 1262 CG GLU A 167 22.634 63.423 24.581 1.00 40.29 C ATOM 1263 CD GLU A 167 22.221 64.076 23.284 1.00 43.39 C ATOM 1264 OE1 GLU A 167 21.408 63.523 22.561 1.00 46.01 O ATOM 1265 OE2 GLU A 167 22.731 65.132 22.949 1.00 45.39 O ATOM 1266 N GLY A 168 19.689 63.317 27.949 1.00 42.38 N ATOM 1267 CA GLY A 168 18.559 62.705 28.586 1.00 42.68 C ATOM 1268 C GLY A 168 17.832 63.514 29.622 1.00 42.57 C ATOM 1269 O GLY A 168 16.961 62.912 30.254 1.00 49.34 O ATOM 1270 N PHE A 169 18.053 64.779 29.895 1.00 36.50 N ATOM 1271 CA PHE A 169 17.248 65.400 30.923 1.00 33.75 C ATOM 1272 C PHE A 169 17.297 66.849 30.632 1.00 35.55 C ATOM 1273 O PHE A 169 16.216 67.403 30.553 1.00 37.98 O ATOM 1274 CB PHE A 169 17.759 65.202 32.362 1.00 29.05 C ATOM 1275 CG PHE A 169 17.044 66.022 33.444 1.00 29.66 C ATOM 1276 CD1 PHE A 169 15.733 65.766 33.804 1.00 32.55 C ATOM 1277 CD2 PHE A 169 17.698 67.053 34.090 1.00 30.70 C ATOM 1278 CE1 PHE A 169 15.096 66.514 34.791 1.00 31.28 C ATOM 1279 CE2 PHE A 169 17.068 67.797 35.072 1.00 30.25 C ATOM 1280 CZ PHE A 169 15.762 67.529 35.437 1.00 32.27 C ATOM 1281 N LEU A 170 18.429 67.489 30.419 1.00 33.36 N ATOM 1282 CA LEU A 170 18.404 68.918 30.220 1.00 35.06 C ATOM 1283 C LEU A 170 17.789 69.238 28.862 1.00 38.99 C ATOM 1284 O LEU A 170 17.399 70.381 28.618 1.00 40.32 O ATOM 1285 CB LEU A 170 19.829 69.453 30.333 1.00 32.91 C ATOM 1286 CG LEU A 170 20.581 69.234 31.634 1.00 29.70 C ATOM 1287 CD1 LEU A 170 22.011 69.694 31.450 1.00 30.95 C ATOM 1288 CD2 LEU A 170 19.879 69.966 32.762 1.00 32.44 C ATOM 1289 N LYS A 171 17.740 68.249 27.947 1.00 42.16 N ATOM 1290 CA LYS A 171 17.045 68.446 26.691 1.00 45.86 C ATOM 1291 C LYS A 171 15.581 68.028 26.792 1.00 48.66 C ATOM 1292 O LYS A 171 14.744 68.394 25.965 1.00 52.35 O ATOM 1293 CB LYS A 171 17.770 67.665 25.600 1.00 48.18 C ATOM 1294 CG LYS A 171 19.029 68.380 25.088 1.00 50.54 C ATOM 1295 CD LYS A 171 19.712 67.682 23.901 1.00 54.77 C ATOM 1296 CE LYS A 171 20.883 68.580 23.430 1.00 61.28 C ATOM 1297 NZ LYS A 171 21.666 68.067 22.304 1.00 63.50 N ATOM 1298 N GLN A 172 15.187 67.282 27.817 1.00 50.65 N ATOM 1299 CA GLN A 172 13.795 66.889 27.964 1.00 52.39 C ATOM 1300 C GLN A 172 12.988 68.052 28.540 1.00 52.64 C ATOM 1301 O GLN A 172 13.545 68.978 29.149 1.00 50.99 O ATOM 1302 CB GLN A 172 13.646 65.658 28.900 1.00 55.75 C ATOM 1303 CG GLN A 172 14.159 64.289 28.401 1.00 62.41 C ATOM 1304 CD GLN A 172 14.603 64.211 26.936 1.00 67.52 C ATOM 1305 OE1 GLN A 172 13.814 64.217 25.988 1.00 71.65 O ATOM 1306 NE2 GLN A 172 15.890 64.155 26.661 1.00 69.65 N ATOM 1307 N PRO A 173 11.641 68.037 28.440 1.00 54.36 N ATOM 1308 CA PRO A 173 10.769 69.068 28.987 1.00 51.71 C ATOM 1309 C PRO A 173 11.042 69.271 30.458 1.00 48.99 C ATOM 1310 O PRO A 173 11.133 70.386 30.961 1.00 47.14 O ATOM 1311 CB PRO A 173 9.380 68.550 28.695 1.00 54.90 C ATOM 1312 CG PRO A 173 9.544 67.789 27.403 1.00 54.52 C ATOM 1313 CD PRO A 173 10.827 67.046 27.708 1.00 56.54 C ATOM 1314 N ALA A 174 11.220 68.149 31.152 1.00 49.31 N ATOM 1315 CA ALA A 174 11.488 68.185 32.577 1.00 49.18 C ATOM 1316 C ALA A 174 12.764 68.923 32.943 1.00 47.89 C ATOM 1317 O ALA A 174 12.805 69.428 34.062 1.00 50.63 O ATOM 1318 CB ALA A 174 11.601 66.777 33.144 1.00 49.65 C ATOM 1319 N GLY A 175 13.770 69.046 32.073 1.00 43.00 N ATOM 1320 CA GLY A 175 14.986 69.713 32.466 1.00 42.99 C ATOM 1321 C GLY A 175 15.052 71.196 32.126 1.00 42.66 C ATOM 1322 O GLY A 175 16.032 71.843 32.508 1.00 40.22 O ATOM 1323 N LYS A 176 14.044 71.774 31.474 1.00 41.76 N ATOM 1324 CA LYS A 176 14.106 73.151 31.025 1.00 41.82 C ATOM 1325 C LYS A 176 14.480 74.163 32.083 1.00 39.53 C ATOM 1326 O LYS A 176 15.155 75.115 31.721 1.00 39.55 O ATOM 1327 CB LYS A 176 12.778 73.572 30.399 1.00 47.08 C ATOM 1328 CG LYS A 176 11.624 73.398 31.374 1.00 59.61 C ATOM 1329 CD LYS A 176 10.288 73.965 30.905 1.00 67.65 C ATOM 1330 CE LYS A 176 9.170 73.514 31.861 1.00 70.75 C ATOM 1331 NZ LYS A 176 9.429 73.858 33.254 1.00 71.22 N ATOM 1332 N GLU A 177 14.145 73.965 33.353 1.00 36.46 N ATOM 1333 CA GLU A 177 14.540 74.898 34.382 1.00 36.65 C ATOM 1334 C GLU A 177 15.840 74.519 35.080 1.00 33.59 C ATOM 1335 O GLU A 177 16.134 74.997 36.185 1.00 31.58 O ATOM 1336 CB GLU A 177 13.455 74.989 35.424 1.00 43.63 C ATOM 1337 CG GLU A 177 12.030 75.266 34.943 1.00 56.68 C ATOM 1338 CD GLU A 177 11.906 76.500 34.061 1.00 65.19 C ATOM 1339 OE1 GLU A 177 12.230 77.595 34.541 1.00 69.42 O ATOM 1340 OE2 GLU A 177 11.502 76.349 32.899 1.00 68.65 O ATOM 1341 N TYR A 178 16.665 73.656 34.495 1.00 31.38 N ATOM 1342 CA TYR A 178 17.826 73.103 35.164 1.00 30.48 C ATOM 1343 C TYR A 178 19.002 73.290 34.240 1.00 29.53 C ATOM 1344 O TYR A 178 18.823 73.541 33.048 1.00 29.65 O ATOM 1345 CB TYR A 178 17.620 71.593 35.479 1.00 30.58 C ATOM 1346 CG TYR A 178 16.655 71.436 36.638 1.00 30.73 C ATOM 1347 CD1 TYR A 178 17.172 71.491 37.903 1.00 28.73 C ATOM 1348 CD2 TYR A 178 15.275 71.397 36.411 1.00 32.07 C ATOM 1349 CE1 TYR A 178 16.308 71.531 38.960 1.00 31.14 C ATOM 1350 CE2 TYR A 178 14.404 71.435 37.468 1.00 29.30 C ATOM 1351 CZ TYR A 178 14.957 71.521 38.717 1.00 32.25 C ATOM 1352 OH TYR A 178 14.144 71.661 39.804 1.00 41.50 O ATOM 1353 N ALA A 179 20.202 73.203 34.807 1.00 28.09 N ATOM 1354 CA ALA A 179 21.405 73.461 34.063 1.00 23.47 C ATOM 1355 C ALA A 179 22.586 72.867 34.809 1.00 23.07 C ATOM 1356 O ALA A 179 22.558 72.635 36.037 1.00 23.81 O ATOM 1357 CB ALA A 179 21.638 74.960 33.965 1.00 21.72 C ATOM 1358 N PHE A 180 23.656 72.696 34.040 1.00 22.35 N ATOM 1359 CA PHE A 180 24.938 72.287 34.582 1.00 22.60 C ATOM 1360 C PHE A 180 25.425 73.301 35.570 1.00 22.28 C ATOM 1361 O PHE A 180 25.403 74.491 35.262 1.00 23.46 O ATOM 1362 CB PHE A 180 25.907 72.152 33.444 1.00 20.56 C ATOM 1363 CG PHE A 180 25.717 70.858 32.643 1.00 22.45 C ATOM 1364 CD1 PHE A 180 25.479 69.638 33.274 1.00 21.91 C ATOM 1365 CD2 PHE A 180 25.835 70.903 31.273 1.00 24.15 C ATOM 1366 CE1 PHE A 180 25.375 68.501 32.502 1.00 20.55 C ATOM 1367 CE2 PHE A 180 25.726 69.750 30.521 1.00 24.54 C ATOM 1368 CZ PHE A 180 25.498 68.542 31.135 1.00 22.28 C ATOM 1369 N ALA A 181 25.778 72.902 36.773 1.00 21.73 N ATOM 1370 CA ALA A 181 26.304 73.847 37.719 1.00 21.55 C ATOM 1371 C ALA A 181 27.818 73.678 37.793 1.00 23.68 C ATOM 1372 O ALA A 181 28.348 72.715 38.364 1.00 25.81 O ATOM 1373 CB ALA A 181 25.689 73.623 39.100 1.00 20.04 C ATOM 1374 N GLY A 182 28.534 74.661 37.235 1.00 23.85 N ATOM 1375 CA GLY A 182 29.982 74.689 37.241 1.00 21.36 C ATOM 1376 C GLY A 182 30.549 73.870 36.099 1.00 20.47 C ATOM 1377 O GLY A 182 29.806 73.410 35.218 1.00 22.23 O ATOM 1378 N PRO A 183 31.872 73.671 36.051 1.00 17.52 N ATOM 1379 CA PRO A 183 32.506 72.925 34.965 1.00 20.99 C ATOM 1380 C PRO A 183 32.458 71.403 35.215 1.00 22.90 C ATOM 1381 O PRO A 183 32.155 70.939 36.331 1.00 22.89 O ATOM 1382 CB PRO A 183 33.885 73.529 34.942 1.00 21.14 C ATOM 1383 CG PRO A 183 34.138 73.698 36.431 1.00 20.19 C ATOM 1384 CD PRO A 183 32.810 74.204 36.998 1.00 15.38 C ATOM 1385 N SER A 184 32.770 70.571 34.240 1.00 24.95 N ATOM 1386 CA SER A 184 32.754 69.151 34.470 1.00 26.86 C ATOM 1387 C SER A 184 33.867 68.711 35.422 1.00 28.46 C ATOM 1388 O SER A 184 34.854 69.420 35.692 1.00 27.33 O ATOM 1389 CB SER A 184 32.853 68.505 33.131 1.00 25.97 C ATOM 1390 OG SER A 184 34.035 68.996 32.575 1.00 29.65 O ATOM 1391 N VAL A 185 33.636 67.564 36.055 1.00 29.95 N ATOM 1392 CA VAL A 185 34.606 67.026 36.970 1.00 32.49 C ATOM 1393 C VAL A 185 35.400 65.951 36.249 1.00 33.07 C ATOM 1394 O VAL A 185 34.890 64.988 35.681 1.00 31.06 O ATOM 1395 CB VAL A 185 33.834 66.531 38.220 1.00 32.30 C ATOM 1396 CG1 VAL A 185 32.887 65.379 38.001 1.00 38.77 C ATOM 1397 CG2 VAL A 185 34.903 66.083 39.167 1.00 36.53 C ATOM 1398 N LYS A 186 36.679 66.188 36.138 1.00 33.48 N ATOM 1399 CA LYS A 186 37.528 65.252 35.456 1.00 36.63 C ATOM 1400 C LYS A 186 38.279 64.542 36.544 1.00 37.91 C ATOM 1401 O LYS A 186 38.721 65.205 37.482 1.00 42.31 O ATOM 1402 CB LYS A 186 38.501 65.978 34.568 1.00 35.66 C ATOM 1403 CG LYS A 186 37.813 66.853 33.563 1.00 40.27 C ATOM 1404 CD LYS A 186 38.814 67.818 32.942 1.00 47.49 C ATOM 1405 CE LYS A 186 38.255 68.487 31.685 1.00 51.22 C ATOM 1406 NZ LYS A 186 38.311 67.570 30.547 1.00 58.23 N ATOM 1407 N ASP A 187 38.351 63.222 36.475 1.00 38.49 N ATOM 1408 CA ASP A 187 39.171 62.425 37.355 1.00 39.69 C ATOM 1409 C ASP A 187 39.454 61.098 36.669 1.00 39.41 C ATOM 1410 O ASP A 187 38.579 60.231 36.608 1.00 40.44 O ATOM 1411 CB ASP A 187 38.462 62.142 38.658 1.00 43.48 C ATOM 1412 CG ASP A 187 39.494 61.898 39.742 1.00 48.49 C ATOM 1413 OD1 ASP A 187 40.062 60.809 39.814 1.00 49.17 O ATOM 1414 OD2 ASP A 187 39.728 62.829 40.511 1.00 55.78 O ATOM 1415 N LYS A 188 40.661 60.849 36.176 1.00 39.61 N ATOM 1416 CA LYS A 188 41.042 59.621 35.464 1.00 38.22 C ATOM 1417 C LYS A 188 40.791 58.373 36.297 1.00 33.37 C ATOM 1418 O LYS A 188 40.332 57.358 35.793 1.00 33.08 O ATOM 1419 CB LYS A 188 42.514 59.868 35.059 1.00 43.72 C ATOM 1420 CG LYS A 188 43.555 58.808 34.728 1.00 52.15 C ATOM 1421 CD LYS A 188 43.194 57.926 33.548 1.00 60.05 C ATOM 1422 CE LYS A 188 44.354 56.999 33.190 1.00 63.87 C ATOM 1423 NZ LYS A 188 44.124 56.437 31.868 1.00 68.17 N ATOM 1424 N LYS A 189 40.954 58.463 37.602 1.00 32.63 N ATOM 1425 CA LYS A 189 40.719 57.328 38.440 1.00 34.44 C ATOM 1426 C LYS A 189 39.297 56.881 38.397 1.00 36.32 C ATOM 1427 O LYS A 189 39.129 55.676 38.460 1.00 37.87 O ATOM 1428 CB LYS A 189 41.066 57.599 39.895 1.00 37.70 C ATOM 1429 CG LYS A 189 40.566 56.510 40.829 1.00 43.67 C ATOM 1430 CD LYS A 189 41.232 56.406 42.182 1.00 53.87 C ATOM 1431 CE LYS A 189 41.441 57.709 42.946 1.00 55.23 C ATOM 1432 NZ LYS A 189 41.798 57.357 44.312 1.00 58.49 N ATOM 1433 N TYR A 190 38.273 57.736 38.277 1.00 35.91 N ATOM 1434 CA TYR A 190 36.906 57.223 38.345 1.00 32.90 C ATOM 1435 C TYR A 190 36.238 57.254 37.007 1.00 30.44 C ATOM 1436 O TYR A 190 35.425 56.387 36.687 1.00 32.84 O ATOM 1437 CB TYR A 190 36.068 58.027 39.332 1.00 34.31 C ATOM 1438 CG TYR A 190 36.679 58.150 40.727 1.00 34.87 C ATOM 1439 CD1 TYR A 190 37.535 59.200 40.995 1.00 34.45 C ATOM 1440 CD2 TYR A 190 36.410 57.222 41.714 1.00 35.64 C ATOM 1441 CE1 TYR A 190 38.121 59.341 42.230 1.00 33.57 C ATOM 1442 CE2 TYR A 190 36.994 57.359 42.957 1.00 35.41 C ATOM 1443 CZ TYR A 190 37.851 58.413 43.199 1.00 36.41 C ATOM 1444 OH TYR A 190 38.473 58.542 44.433 1.00 41.66 O ATOM 1445 N PHE A 191 36.637 58.225 36.181 1.00 28.03 N ATOM 1446 CA PHE A 191 35.974 58.441 34.901 1.00 27.58 C ATOM 1447 C PHE A 191 36.811 58.041 33.717 1.00 28.09 C ATOM 1448 O PHE A 191 36.280 58.015 32.612 1.00 30.10 O ATOM 1449 CB PHE A 191 35.527 59.959 34.754 1.00 25.48 C ATOM 1450 CG PHE A 191 34.702 60.384 35.980 1.00 28.87 C ATOM 1451 CD1 PHE A 191 33.642 59.605 36.447 1.00 29.58 C ATOM 1452 CD2 PHE A 191 35.067 61.497 36.714 1.00 31.50 C ATOM 1453 CE1 PHE A 191 32.970 59.924 37.616 1.00 29.88 C ATOM 1454 CE2 PHE A 191 34.383 61.813 37.877 1.00 29.97 C ATOM 1455 CZ PHE A 191 33.343 61.030 38.331 1.00 28.86 C ATOM 1456 N GLY A 192 38.095 57.706 33.936 1.00 29.68 N ATOM 1457 CA GLY A 192 39.017 57.394 32.869 1.00 28.78 C ATOM 1458 C GLY A 192 39.520 58.646 32.189 1.00 30.65 C ATOM 1459 O GLY A 192 39.201 59.765 32.601 1.00 34.04 O ATOM 1460 N ASP A 193 40.239 58.488 31.094 1.00 31.76 N ATOM 1461 CA ASP A 193 40.838 59.610 30.409 1.00 32.50 C ATOM 1462 C ASP A 193 40.253 59.838 29.027 1.00 29.25 C ATOM 1463 O ASP A 193 40.959 59.877 28.020 1.00 30.42 O ATOM 1464 CB ASP A 193 42.316 59.339 30.336 1.00 38.58 C ATOM 1465 CG ASP A 193 43.049 60.614 30.645 1.00 46.19 C ATOM 1466 OD1 ASP A 193 43.238 61.400 29.720 1.00 53.39 O ATOM 1467 OD2 ASP A 193 43.397 60.830 31.808 1.00 53.46 O ATOM 1468 N GLY A 194 38.942 60.018 28.969 1.00 26.80 N ATOM 1469 CA GLY A 194 38.248 60.123 27.712 1.00 24.42 C ATOM 1470 C GLY A 194 37.961 58.710 27.240 1.00 22.49 C ATOM 1471 O GLY A 194 38.124 57.746 27.993 1.00 24.37 O ATOM 1472 N THR A 195 37.497 58.570 26.017 1.00 22.30 N ATOM 1473 CA THR A 195 37.226 57.277 25.438 1.00 21.33 C ATOM 1474 C THR A 195 38.231 57.098 24.316 1.00 21.07 C ATOM 1475 O THR A 195 38.734 58.117 23.806 1.00 22.45 O ATOM 1476 CB THR A 195 35.805 57.209 24.857 1.00 22.80 C ATOM 1477 OG1 THR A 195 35.644 58.161 23.809 1.00 23.41 O ATOM 1478 CG2 THR A 195 34.816 57.499 25.935 1.00 21.58 C ATOM 1479 N GLY A 196 38.486 55.890 23.824 1.00 18.48 N ATOM 1480 CA GLY A 196 39.458 55.712 22.769 1.00 17.92 C ATOM 1481 C GLY A 196 39.106 54.471 22.013 1.00 20.22 C ATOM 1482 O GLY A 196 38.196 53.747 22.430 1.00 21.64 O ATOM 1483 N VAL A 197 39.754 54.230 20.874 1.00 19.42 N ATOM 1484 CA VAL A 197 39.555 53.019 20.086 1.00 18.01 C ATOM 1485 C VAL A 197 40.286 51.909 20.897 1.00 20.46 C ATOM 1486 O VAL A 197 41.480 52.058 21.202 1.00 23.59 O ATOM 1487 CB VAL A 197 40.187 53.210 18.679 1.00 18.07 C ATOM 1488 CG1 VAL A 197 39.959 51.979 17.834 1.00 17.87 C ATOM 1489 CG2 VAL A 197 39.570 54.367 17.932 1.00 15.62 C ATOM 1490 N GLY A 198 39.627 50.844 21.351 1.00 17.56 N ATOM 1491 CA GLY A 198 40.253 49.738 22.044 1.00 19.78 C ATOM 1492 C GLY A 198 40.915 48.816 21.018 1.00 21.20 C ATOM 1493 O GLY A 198 40.301 48.397 20.023 1.00 22.04 O ATOM 1494 N LEU A 199 42.159 48.433 21.254 1.00 21.78 N ATOM 1495 CA LEU A 199 42.969 47.687 20.314 1.00 22.17 C ATOM 1496 C LEU A 199 43.762 46.628 21.073 1.00 23.98 C ATOM 1497 O LEU A 199 43.988 46.751 22.277 1.00 24.71 O ATOM 1498 CB LEU A 199 43.941 48.623 19.637 1.00 22.61 C ATOM 1499 CG LEU A 199 43.406 49.707 18.714 1.00 22.72 C ATOM 1500 CD1 LEU A 199 44.409 50.810 18.576 1.00 27.19 C ATOM 1501 CD2 LEU A 199 43.118 49.130 17.348 1.00 22.30 C ATOM 1502 N ARG A 200 44.225 45.551 20.452 1.00 25.67 N ATOM 1503 CA ARG A 200 45.104 44.537 21.071 1.00 25.89 C ATOM 1504 C ARG A 200 46.414 45.197 21.422 1.00 25.55 C ATOM 1505 O ARG A 200 46.944 45.947 20.631 1.00 24.76 O ATOM 1506 CB ARG A 200 45.357 43.384 20.099 1.00 23.94 C ATOM 1507 CG ARG A 200 44.166 42.461 20.266 1.00 24.95 C ATOM 1508 CD ARG A 200 44.157 41.194 19.456 1.00 19.34 C ATOM 1509 NE ARG A 200 44.263 41.512 18.054 1.00 19.21 N ATOM 1510 CZ ARG A 200 43.236 41.564 17.219 1.00 17.70 C ATOM 1511 NH1 ARG A 200 41.978 41.326 17.623 1.00 20.51 N ATOM 1512 NH2 ARG A 200 43.505 41.817 15.943 1.00 17.78 N ATOM 1513 N LYS A 201 47.008 44.916 22.573 1.00 26.35 N ATOM 1514 CA LYS A 201 48.257 45.532 22.976 1.00 29.67 C ATOM 1515 C LYS A 201 49.389 45.363 21.982 1.00 31.19 C ATOM 1516 O LYS A 201 50.249 46.229 21.814 1.00 35.37 O ATOM 1517 CB LYS A 201 48.766 44.935 24.261 1.00 31.47 C ATOM 1518 CG LYS A 201 48.050 45.522 25.450 1.00 37.06 C ATOM 1519 CD LYS A 201 49.179 45.675 26.459 1.00 41.00 C ATOM 1520 CE LYS A 201 48.797 46.461 27.682 1.00 42.96 C ATOM 1521 NZ LYS A 201 47.818 45.707 28.434 1.00 46.14 N ATOM 1522 N ASP A 202 49.324 44.303 21.227 1.00 33.46 N ATOM 1523 CA ASP A 202 50.323 43.894 20.236 1.00 34.40 C ATOM 1524 C ASP A 202 50.182 44.562 18.901 1.00 31.20 C ATOM 1525 O ASP A 202 51.083 44.552 18.089 1.00 28.14 O ATOM 1526 CB ASP A 202 50.245 42.399 20.076 1.00 43.33 C ATOM 1527 CG ASP A 202 48.784 41.874 20.126 1.00 50.29 C ATOM 1528 OD1 ASP A 202 48.205 41.667 21.221 1.00 50.73 O ATOM 1529 OD2 ASP A 202 48.204 41.762 19.057 1.00 54.02 O ATOM 1530 N ASP A 203 49.058 45.201 18.647 1.00 31.82 N ATOM 1531 CA ASP A 203 48.818 45.752 17.334 1.00 32.56 C ATOM 1532 C ASP A 203 49.235 47.195 17.224 1.00 32.96 C ATOM 1533 O ASP A 203 48.433 48.108 16.957 1.00 35.60 O ATOM 1534 CB ASP A 203 47.307 45.559 16.955 1.00 31.03 C ATOM 1535 CG ASP A 203 46.980 44.129 16.565 1.00 33.73 C ATOM 1536 OD1 ASP A 203 47.813 43.234 16.621 1.00 35.90 O ATOM 1537 OD2 ASP A 203 45.870 43.881 16.145 1.00 37.35 O ATOM 1538 N THR A 204 50.554 47.371 17.329 1.00 31.91 N ATOM 1539 CA THR A 204 51.051 48.729 17.302 1.00 30.61 C ATOM 1540 C THR A 204 50.950 49.388 15.942 1.00 28.73 C ATOM 1541 O THR A 204 50.725 50.585 15.959 1.00 32.12 O ATOM 1542 CB THR A 204 52.494 48.717 17.823 1.00 34.36 C ATOM 1543 OG1 THR A 204 53.272 47.817 17.077 1.00 38.51 O ATOM 1544 CG2 THR A 204 52.546 48.213 19.254 1.00 33.65 C ATOM 1545 N GLU A 205 51.050 48.795 14.753 1.00 28.58 N ATOM 1546 CA GLU A 205 50.872 49.538 13.519 1.00 31.15 C ATOM 1547 C GLU A 205 49.431 50.012 13.380 1.00 31.39 C ATOM 1548 O GLU A 205 49.199 51.136 12.917 1.00 28.22 O ATOM 1549 CB GLU A 205 51.187 48.705 12.309 1.00 38.12 C ATOM 1550 CG GLU A 205 52.609 48.196 12.330 1.00 50.85 C ATOM 1551 CD GLU A 205 52.612 46.710 12.023 1.00 58.15 C ATOM 1552 OE1 GLU A 205 52.423 45.913 12.952 1.00 63.64 O ATOM 1553 OE2 GLU A 205 52.753 46.355 10.849 1.00 58.43 O ATOM 1554 N LEU A 206 48.456 49.201 13.824 1.00 28.22 N ATOM 1555 CA LEU A 206 47.058 49.594 13.790 1.00 28.25 C ATOM 1556 C LEU A 206 46.832 50.750 14.755 1.00 26.39 C ATOM 1557 O LEU A 206 46.170 51.707 14.356 1.00 27.53 O ATOM 1558 CB LEU A 206 46.171 48.414 14.156 1.00 27.45 C ATOM 1559 CG LEU A 206 44.659 48.578 13.890 1.00 26.08 C ATOM 1560 CD1 LEU A 206 44.410 48.961 12.433 1.00 22.33 C ATOM 1561 CD2 LEU A 206 43.945 47.288 14.260 1.00 26.81 C ATOM 1562 N LYS A 207 47.376 50.777 15.965 1.00 25.84 N ATOM 1563 CA LYS A 207 47.286 51.974 16.807 1.00 28.59 C ATOM 1564 C LYS A 207 47.874 53.245 16.182 1.00 30.25 C ATOM 1565 O LYS A 207 47.289 54.337 16.297 1.00 30.52 O ATOM 1566 CB LYS A 207 47.979 51.729 18.163 1.00 28.35 C ATOM 1567 CG LYS A 207 47.818 52.937 19.055 1.00 28.53 C ATOM 1568 CD LYS A 207 48.384 52.725 20.430 1.00 30.44 C ATOM 1569 CE LYS A 207 48.926 54.072 20.931 1.00 29.83 C ATOM 1570 NZ LYS A 207 47.913 55.083 21.163 1.00 32.10 N ATOM 1571 N ALA A 208 49.031 53.102 15.521 1.00 28.72 N ATOM 1572 CA ALA A 208 49.702 54.194 14.861 1.00 25.77 C ATOM 1573 C ALA A 208 48.833 54.743 13.754 1.00 24.96 C ATOM 1574 O ALA A 208 48.698 55.946 13.557 1.00 26.74 O ATOM 1575 CB ALA A 208 50.983 53.660 14.293 1.00 26.14 C ATOM 1576 N ALA A 209 48.233 53.839 12.998 1.00 22.79 N ATOM 1577 CA ALA A 209 47.358 54.194 11.911 1.00 23.16 C ATOM 1578 C ALA A 209 46.116 54.922 12.427 1.00 23.12 C ATOM 1579 O ALA A 209 45.804 55.977 11.865 1.00 26.30 O ATOM 1580 CB ALA A 209 46.987 52.917 11.165 1.00 21.83 C ATOM 1581 N PHE A 210 45.415 54.460 13.471 1.00 23.36 N ATOM 1582 CA PHE A 210 44.320 55.207 14.103 1.00 25.09 C ATOM 1583 C PHE A 210 44.797 56.531 14.696 1.00 26.57 C ATOM 1584 O PHE A 210 44.151 57.573 14.496 1.00 29.74 O ATOM 1585 CB PHE A 210 43.644 54.438 15.252 1.00 22.77 C ATOM 1586 CG PHE A 210 42.585 53.479 14.734 1.00 26.37 C ATOM 1587 CD1 PHE A 210 41.393 53.960 14.216 1.00 26.82 C ATOM 1588 CD2 PHE A 210 42.789 52.106 14.784 1.00 26.89 C ATOM 1589 CE1 PHE A 210 40.407 53.089 13.747 1.00 24.90 C ATOM 1590 CE2 PHE A 210 41.796 51.248 14.309 1.00 27.36 C ATOM 1591 CZ PHE A 210 40.601 51.727 13.792 1.00 25.44 C ATOM 1592 N ASP A 211 45.916 56.591 15.410 1.00 26.60 N ATOM 1593 CA ASP A 211 46.385 57.852 15.954 1.00 27.15 C ATOM 1594 C ASP A 211 46.700 58.901 14.895 1.00 27.83 C ATOM 1595 O ASP A 211 46.269 60.060 15.033 1.00 25.90 O ATOM 1596 CB ASP A 211 47.604 57.563 16.833 1.00 26.29 C ATOM 1597 CG ASP A 211 47.248 56.899 18.156 1.00 27.08 C ATOM 1598 OD1 ASP A 211 46.078 56.815 18.527 1.00 27.92 O ATOM 1599 OD2 ASP A 211 48.157 56.468 18.845 1.00 30.51 O ATOM 1600 N LYS A 212 47.368 58.497 13.804 1.00 27.94 N ATOM 1601 CA LYS A 212 47.686 59.410 12.717 1.00 30.60 C ATOM 1602 C LYS A 212 46.407 59.999 12.130 1.00 29.26 C ATOM 1603 O LYS A 212 46.215 61.217 12.118 1.00 29.45 O ATOM 1604 CB LYS A 212 48.485 58.664 11.634 1.00 33.32 C ATOM 1605 CG LYS A 212 48.986 59.537 10.468 1.00 37.77 C ATOM 1606 CD LYS A 212 49.742 58.714 9.444 1.00 39.13 C ATOM 1607 CE LYS A 212 50.388 59.617 8.410 1.00 43.13 C ATOM 1608 NZ LYS A 212 49.574 59.818 7.216 1.00 47.22 N ATOM 1609 N ALA A 213 45.470 59.126 11.786 1.00 28.13 N ATOM 1610 CA ALA A 213 44.211 59.547 11.205 1.00 27.40 C ATOM 1611 C ALA A 213 43.406 60.445 12.136 1.00 26.26 C ATOM 1612 O ALA A 213 42.849 61.447 11.670 1.00 28.53 O ATOM 1613 CB ALA A 213 43.388 58.322 10.855 1.00 28.32 C ATOM 1614 N LEU A 214 43.375 60.189 13.440 1.00 25.81 N ATOM 1615 CA LEU A 214 42.655 61.045 14.338 1.00 25.91 C ATOM 1616 C LEU A 214 43.323 62.430 14.394 1.00 28.72 C ATOM 1617 O LEU A 214 42.605 63.428 14.319 1.00 26.77 O ATOM 1618 CB LEU A 214 42.600 60.399 15.721 1.00 26.10 C ATOM 1619 CG LEU A 214 41.934 61.274 16.818 1.00 28.76 C ATOM 1620 CD1 LEU A 214 40.471 61.526 16.458 1.00 27.22 C ATOM 1621 CD2 LEU A 214 42.075 60.612 18.175 1.00 29.81 C ATOM 1622 N THR A 215 44.650 62.599 14.464 1.00 32.22 N ATOM 1623 CA THR A 215 45.282 63.915 14.485 1.00 33.15 C ATOM 1624 C THR A 215 44.990 64.725 13.241 1.00 32.88 C ATOM 1625 O THR A 215 44.659 65.914 13.334 1.00 33.64 O ATOM 1626 CB THR A 215 46.777 63.768 14.637 1.00 35.14 C ATOM 1627 OG1 THR A 215 46.977 63.006 15.830 1.00 36.30 O ATOM 1628 CG2 THR A 215 47.481 65.136 14.733 1.00 39.33 C ATOM 1629 N GLU A 216 45.062 64.061 12.092 1.00 33.97 N ATOM 1630 CA GLU A 216 44.709 64.652 10.817 1.00 36.33 C ATOM 1631 C GLU A 216 43.304 65.213 10.742 1.00 37.55 C ATOM 1632 O GLU A 216 43.114 66.378 10.357 1.00 36.18 O ATOM 1633 CB GLU A 216 44.838 63.640 9.715 1.00 38.81 C ATOM 1634 CG GLU A 216 46.323 63.407 9.467 1.00 45.03 C ATOM 1635 CD GLU A 216 46.654 62.381 8.399 1.00 48.40 C ATOM 1636 OE1 GLU A 216 45.785 62.005 7.599 1.00 50.92 O ATOM 1637 OE2 GLU A 216 47.813 61.968 8.400 1.00 49.81 O ATOM 1638 N LEU A 217 42.294 64.412 11.110 1.00 35.83 N ATOM 1639 CA LEU A 217 40.945 64.912 11.007 1.00 30.91 C ATOM 1640 C LEU A 217 40.705 65.925 12.089 1.00 30.18 C ATOM 1641 O LEU A 217 39.813 66.752 11.918 1.00 31.92 O ATOM 1642 CB LEU A 217 39.923 63.754 11.065 1.00 30.58 C ATOM 1643 CG LEU A 217 39.727 62.842 12.244 1.00 28.48 C ATOM 1644 CD1 LEU A 217 38.727 63.426 13.192 1.00 29.39 C ATOM 1645 CD2 LEU A 217 39.201 61.494 11.757 1.00 29.04 C ATOM 1646 N ARG A 218 41.427 65.947 13.197 1.00 29.70 N ATOM 1647 CA ARG A 218 41.262 67.026 14.133 1.00 33.81 C ATOM 1648 C ARG A 218 41.871 68.306 13.578 1.00 40.62 C ATOM 1649 O ARG A 218 41.209 69.357 13.590 1.00 42.35 O ATOM 1650 CB ARG A 218 41.929 66.725 15.424 1.00 32.90 C ATOM 1651 CG ARG A 218 40.994 65.910 16.266 1.00 35.75 C ATOM 1652 CD ARG A 218 41.599 65.617 17.624 1.00 38.18 C ATOM 1653 NE ARG A 218 41.860 66.801 18.437 1.00 44.48 N ATOM 1654 CZ ARG A 218 40.880 67.611 18.862 1.00 46.47 C ATOM 1655 NH1 ARG A 218 39.597 67.401 18.560 1.00 45.97 N ATOM 1656 NH2 ARG A 218 41.188 68.612 19.682 1.00 48.56 N ATOM 1657 N GLN A 219 43.091 68.231 13.014 1.00 42.31 N ATOM 1658 CA GLN A 219 43.769 69.400 12.471 1.00 43.39 C ATOM 1659 C GLN A 219 43.092 70.062 11.296 1.00 41.69 C ATOM 1660 O GLN A 219 43.072 71.280 11.257 1.00 45.27 O ATOM 1661 CB GLN A 219 45.181 69.066 12.052 1.00 46.33 C ATOM 1662 CG GLN A 219 46.003 68.925 13.325 1.00 56.61 C ATOM 1663 CD GLN A 219 47.517 68.917 13.106 1.00 63.33 C ATOM 1664 OE1 GLN A 219 48.067 68.178 12.290 1.00 66.58 O ATOM 1665 NE2 GLN A 219 48.285 69.724 13.831 1.00 67.29 N ATOM 1666 N ASP A 220 42.502 69.366 10.344 1.00 39.53 N ATOM 1667 CA ASP A 220 41.816 70.003 9.245 1.00 37.10 C ATOM 1668 C ASP A 220 40.372 70.412 9.564 1.00 38.84 C ATOM 1669 O ASP A 220 39.604 70.748 8.655 1.00 39.32 O ATOM 1670 CB ASP A 220 41.838 69.046 8.062 1.00 39.43 C ATOM 1671 CG ASP A 220 41.018 67.756 8.176 1.00 39.55 C ATOM 1672 OD1 ASP A 220 40.410 67.489 9.203 1.00 41.08 O ATOM 1673 OD2 ASP A 220 40.965 67.017 7.204 1.00 40.34 O ATOM 1674 N GLY A 221 39.901 70.243 10.802 1.00 38.05 N ATOM 1675 CA GLY A 221 38.577 70.714 11.195 1.00 36.83 C ATOM 1676 C GLY A 221 37.430 69.738 11.008 1.00 37.71 C ATOM 1677 O GLY A 221 36.308 70.010 11.440 1.00 36.98 O ATOM 1678 N THR A 222 37.659 68.562 10.420 1.00 36.76 N ATOM 1679 CA THR A 222 36.604 67.568 10.226 1.00 33.27 C ATOM 1680 C THR A 222 36.022 67.180 11.583 1.00 32.25 C ATOM 1681 O THR A 222 34.804 67.056 11.690 1.00 32.95 O ATOM 1682 CB THR A 222 37.185 66.336 9.550 1.00 32.08 C ATOM 1683 OG1 THR A 222 37.892 66.801 8.418 1.00 34.46 O ATOM 1684 CG2 THR A 222 36.151 65.366 9.079 1.00 35.27 C ATOM 1685 N TYR A 223 36.819 67.067 12.654 1.00 29.13 N ATOM 1686 CA TYR A 223 36.321 66.674 13.950 1.00 29.54 C ATOM 1687 C TYR A 223 35.211 67.617 14.397 1.00 33.21 C ATOM 1688 O TYR A 223 34.155 67.150 14.855 1.00 32.57 O ATOM 1689 CB TYR A 223 37.466 66.678 14.974 1.00 26.47 C ATOM 1690 CG TYR A 223 37.078 66.176 16.365 1.00 25.72 C ATOM 1691 CD1 TYR A 223 36.334 66.968 17.222 1.00 21.91 C ATOM 1692 CD2 TYR A 223 37.433 64.904 16.756 1.00 24.71 C ATOM 1693 CE1 TYR A 223 35.940 66.512 18.445 1.00 19.14 C ATOM 1694 CE2 TYR A 223 37.036 64.437 17.987 1.00 19.22 C ATOM 1695 CZ TYR A 223 36.298 65.238 18.798 1.00 19.57 C ATOM 1696 OH TYR A 223 35.900 64.774 20.008 1.00 21.71 O ATOM 1697 N ASP A 224 35.440 68.934 14.241 1.00 34.34 N ATOM 1698 CA ASP A 224 34.455 69.915 14.688 1.00 34.77 C ATOM 1699 C ASP A 224 33.183 69.931 13.894 1.00 31.76 C ATOM 1700 O ASP A 224 32.126 70.049 14.496 1.00 34.43 O ATOM 1701 CB ASP A 224 35.000 71.322 14.664 1.00 38.94 C ATOM 1702 CG ASP A 224 36.136 71.493 15.658 1.00 42.83 C ATOM 1703 OD1 ASP A 224 36.046 71.027 16.803 1.00 42.38 O ATOM 1704 OD2 ASP A 224 37.131 72.099 15.261 1.00 50.46 O ATOM 1705 N LYS A 225 33.277 69.753 12.579 1.00 33.00 N ATOM 1706 CA LYS A 225 32.129 69.658 11.692 1.00 33.66 C ATOM 1707 C LYS A 225 31.342 68.435 12.113 1.00 36.46 C ATOM 1708 O LYS A 225 30.126 68.533 12.293 1.00 40.92 O ATOM 1709 CB LYS A 225 32.525 69.466 10.219 1.00 28.36 C ATOM 1710 N MET A 226 32.014 67.308 12.379 1.00 35.37 N ATOM 1711 CA MET A 226 31.304 66.115 12.768 1.00 33.44 C ATOM 1712 C MET A 226 30.673 66.290 14.121 1.00 30.65 C ATOM 1713 O MET A 226 29.519 65.934 14.278 1.00 29.62 O ATOM 1714 CB MET A 226 32.229 64.897 12.796 1.00 35.25 C ATOM 1715 CG MET A 226 32.679 64.611 11.383 1.00 36.92 C ATOM 1716 SD MET A 226 33.308 62.951 11.068 1.00 42.08 S ATOM 1717 CE MET A 226 34.866 63.120 11.892 1.00 39.96 C ATOM 1718 N ALA A 227 31.368 66.862 15.121 1.00 30.91 N ATOM 1719 CA ALA A 227 30.771 67.002 16.443 1.00 32.81 C ATOM 1720 C ALA A 227 29.532 67.909 16.416 1.00 35.09 C ATOM 1721 O ALA A 227 28.519 67.594 17.072 1.00 34.07 O ATOM 1722 CB ALA A 227 31.813 67.594 17.403 1.00 27.62 C ATOM 1723 N LYS A 228 29.577 68.949 15.589 1.00 37.99 N ATOM 1724 CA LYS A 228 28.497 69.912 15.423 1.00 40.99 C ATOM 1725 C LYS A 228 27.132 69.272 15.191 1.00 39.78 C ATOM 1726 O LYS A 228 26.127 69.807 15.667 1.00 41.62 O ATOM 1727 CB LYS A 228 28.788 70.845 14.267 1.00 44.64 C ATOM 1728 CG LYS A 228 29.347 72.117 14.812 1.00 51.86 C ATOM 1729 CD LYS A 228 28.167 73.035 15.117 1.00 61.78 C ATOM 1730 CE LYS A 228 28.148 74.216 14.126 1.00 68.79 C ATOM 1731 NZ LYS A 228 28.098 73.792 12.727 1.00 71.89 N ATOM 1732 N LYS A 229 27.046 68.083 14.579 1.00 38.61 N ATOM 1733 CA LYS A 229 25.763 67.437 14.356 1.00 37.64 C ATOM 1734 C LYS A 229 25.083 67.009 15.632 1.00 36.27 C ATOM 1735 O LYS A 229 23.860 66.831 15.684 1.00 39.53 O ATOM 1736 CB LYS A 229 25.889 66.187 13.556 1.00 39.70 C ATOM 1737 CG LYS A 229 26.211 66.394 12.109 1.00 46.12 C ATOM 1738 CD LYS A 229 26.362 65.010 11.471 1.00 53.01 C ATOM 1739 CE LYS A 229 25.164 64.082 11.652 1.00 53.53 C ATOM 1740 NZ LYS A 229 25.450 62.859 10.934 1.00 55.47 N ATOM 1741 N TYR A 230 25.854 66.779 16.686 1.00 35.40 N ATOM 1742 CA TYR A 230 25.287 66.159 17.872 1.00 31.38 C ATOM 1743 C TYR A 230 25.414 67.003 19.076 1.00 31.44 C ATOM 1744 O TYR A 230 24.548 66.949 19.943 1.00 30.83 O ATOM 1745 CB TYR A 230 25.961 64.831 18.252 1.00 29.01 C ATOM 1746 CG TYR A 230 26.120 63.881 17.094 1.00 26.63 C ATOM 1747 CD1 TYR A 230 27.139 64.017 16.180 1.00 22.99 C ATOM 1748 CD2 TYR A 230 25.174 62.926 16.944 1.00 28.69 C ATOM 1749 CE1 TYR A 230 27.206 63.179 15.097 1.00 25.81 C ATOM 1750 CE2 TYR A 230 25.233 62.087 15.864 1.00 30.57 C ATOM 1751 CZ TYR A 230 26.238 62.214 14.937 1.00 29.82 C ATOM 1752 OH TYR A 230 26.234 61.355 13.851 1.00 25.77 O ATOM 1753 N PHE A 231 26.496 67.776 19.146 1.00 33.94 N ATOM 1754 CA PHE A 231 26.844 68.424 20.401 1.00 34.98 C ATOM 1755 C PHE A 231 27.007 69.881 20.118 1.00 36.68 C ATOM 1756 O PHE A 231 27.629 70.263 19.133 1.00 37.51 O ATOM 1757 CB PHE A 231 28.171 67.882 20.972 1.00 33.09 C ATOM 1758 CG PHE A 231 28.114 66.370 21.186 1.00 32.29 C ATOM 1759 CD1 PHE A 231 27.253 65.847 22.155 1.00 33.06 C ATOM 1760 CD2 PHE A 231 28.868 65.531 20.374 1.00 29.74 C ATOM 1761 CE1 PHE A 231 27.121 64.479 22.309 1.00 31.05 C ATOM 1762 CE2 PHE A 231 28.732 64.159 20.534 1.00 31.30 C ATOM 1763 CZ PHE A 231 27.864 63.644 21.494 1.00 32.70 C ATOM 1764 N ASP A 232 26.434 70.658 21.013 1.00 40.80 N ATOM 1765 CA ASP A 232 26.546 72.104 20.940 1.00 44.43 C ATOM 1766 C ASP A 232 27.661 72.513 21.882 1.00 43.60 C ATOM 1767 O ASP A 232 27.855 73.707 22.082 1.00 47.96 O ATOM 1768 CB ASP A 232 25.247 72.759 21.370 1.00 51.75 C ATOM 1769 CG ASP A 232 24.743 72.155 22.687 1.00 64.70 C ATOM 1770 OD1 ASP A 232 25.303 72.460 23.753 1.00 69.07 O ATOM 1771 OD2 ASP A 232 23.811 71.333 22.633 1.00 72.80 O ATOM 1772 N PHE A 233 28.351 71.579 22.543 1.00 39.81 N ATOM 1773 CA PHE A 233 29.469 71.937 23.393 1.00 37.52 C ATOM 1774 C PHE A 233 30.768 71.251 22.960 1.00 36.69 C ATOM 1775 O PHE A 233 30.798 70.430 22.031 1.00 37.24 O ATOM 1776 CB PHE A 233 29.155 71.580 24.831 1.00 36.29 C ATOM 1777 CG PHE A 233 29.101 70.098 25.139 1.00 40.98 C ATOM 1778 CD1 PHE A 233 28.035 69.338 24.710 1.00 41.52 C ATOM 1779 CD2 PHE A 233 30.132 69.531 25.872 1.00 40.57 C ATOM 1780 CE1 PHE A 233 28.025 67.999 25.028 1.00 43.27 C ATOM 1781 CE2 PHE A 233 30.100 68.199 26.183 1.00 38.66 C ATOM 1782 CZ PHE A 233 29.047 67.440 25.760 1.00 40.49 C ATOM 1783 N ASN A 234 31.897 71.532 23.597 1.00 34.87 N ATOM 1784 CA ASN A 234 33.141 70.908 23.199 1.00 32.53 C ATOM 1785 C ASN A 234 33.263 69.528 23.815 1.00 29.08 C ATOM 1786 O ASN A 234 33.702 69.362 24.944 1.00 27.19 O ATOM 1787 CB ASN A 234 34.231 71.822 23.624 1.00 33.89 C ATOM 1788 CG ASN A 234 35.607 71.229 23.481 1.00 35.20 C ATOM 1789 OD1 ASN A 234 36.424 71.443 24.357 1.00 37.49 O ATOM 1790 ND2 ASN A 234 36.004 70.467 22.486 1.00 35.73 N ATOM 1791 N VAL A 235 32.736 68.529 23.102 1.00 28.28 N ATOM 1792 CA VAL A 235 32.803 67.135 23.546 1.00 28.29 C ATOM 1793 C VAL A 235 34.224 66.644 23.755 1.00 26.34 C ATOM 1794 O VAL A 235 34.466 65.690 24.488 1.00 26.41 O ATOM 1795 CB VAL A 235 32.252 66.027 22.583 1.00 30.68 C ATOM 1796 CG1 VAL A 235 31.055 65.417 23.285 1.00 29.16 C ATOM 1797 CG2 VAL A 235 32.067 66.526 21.171 1.00 27.96 C ATOM 1798 N TYR A 236 35.167 67.204 23.016 1.00 24.89 N ATOM 1799 CA TYR A 236 36.536 66.773 23.147 1.00 24.60 C ATOM 1800 C TYR A 236 37.096 66.992 24.537 1.00 27.25 C ATOM 1801 O TYR A 236 37.800 66.109 25.026 1.00 24.16 O ATOM 1802 CB TYR A 236 37.346 67.494 22.096 1.00 25.78 C ATOM 1803 CG TYR A 236 38.747 66.920 22.051 1.00 30.12 C ATOM 1804 CD1 TYR A 236 38.992 65.702 21.439 1.00 30.39 C ATOM 1805 CD2 TYR A 236 39.755 67.588 22.702 1.00 32.03 C ATOM 1806 CE1 TYR A 236 40.250 65.145 21.481 1.00 30.54 C ATOM 1807 CE2 TYR A 236 41.006 67.034 22.753 1.00 33.89 C ATOM 1808 CZ TYR A 236 41.245 65.830 22.139 1.00 33.01 C ATOM 1809 OH TYR A 236 42.515 65.310 22.213 1.00 31.57 O ATOM 1810 N GLY A 237 36.744 68.093 25.220 1.00 31.30 N ATOM 1811 CA GLY A 237 37.302 68.436 26.516 1.00 35.43 C ATOM 1812 C GLY A 237 38.654 69.103 26.270 1.00 41.74 C ATOM 1813 O GLY A 237 38.843 69.804 25.266 1.00 42.67 O ATOM 1814 N ASP A 238 39.632 68.814 27.124 1.00 47.86 N ATOM 1815 CA ASP A 238 40.936 69.454 27.040 1.00 53.26 C ATOM 1816 C ASP A 238 41.963 68.498 26.444 1.00 54.11 C ATOM 1817 O ASP A 238 42.103 67.376 26.936 1.00 54.48 O ATOM 1818 CB ASP A 238 41.363 69.897 28.450 1.00 57.29 C ATOM 1819 CG ASP A 238 40.377 70.804 29.190 1.00 61.17 C ATOM 1820 OD1 ASP A 238 39.660 71.580 28.548 1.00 63.34 O ATOM 1821 OD2 ASP A 238 40.333 70.734 30.420 1.00 63.51 O ATOM 1822 OXT ASP A 238 42.606 68.875 25.470 1.00 55.41 O TER 1823 ASP A 238 HETATM 1824 O HOH A 401 35.465 53.833 22.185 1.00 17.40 O HETATM 1825 O HOH A 402 29.833 70.386 37.786 1.00 17.14 O HETATM 1826 O HOH A 403 43.753 45.097 17.757 1.00 22.49 O HETATM 1827 O HOH A 404 24.857 59.467 39.438 1.00 26.25 O HETATM 1828 O HOH A 405 30.130 62.511 29.393 1.00 26.09 O HETATM 1829 O HOH A 406 32.008 64.455 29.050 1.00 27.43 O HETATM 1830 O HOH A 407 22.720 75.246 37.739 1.00 30.15 O HETATM 1831 O HOH A 408 45.727 42.952 24.365 1.00 41.65 O HETATM 1832 O HOH A 409 38.011 62.094 33.829 1.00 30.81 O HETATM 1833 O HOH A 410 33.942 44.685 27.038 1.00 35.76 O HETATM 1834 O HOH A 411 30.964 61.368 26.619 1.00 34.24 O HETATM 1835 O HOH A 412 48.617 46.257 13.995 1.00 40.71 O HETATM 1836 O HOH A 413 38.451 69.665 14.181 1.00 42.41 O HETATM 1837 O HOH A 414 29.069 54.296 21.592 1.00 32.80 O HETATM 1838 O HOH A 415 31.392 60.205 33.382 1.00 26.86 O HETATM 1839 O HOH A 416 41.323 54.851 35.386 1.00 41.30 O HETATM 1840 O HOH A 417 47.615 48.564 19.641 1.00 37.18 O HETATM 1841 O HOH A 418 26.295 58.430 11.683 1.00 28.55 O HETATM 1842 O HOH A 419 43.316 62.914 20.769 1.00 37.49 O HETATM 1843 O HOH A 420 47.487 52.523 24.517 1.00 49.40 O HETATM 1844 O HOH A 421 45.375 57.150 24.655 1.00 34.87 O HETATM 1845 O HOH A 422 28.371 77.698 37.121 1.00 30.46 O HETATM 1846 O HOH A 423 26.976 77.322 39.566 1.00 33.68 O HETATM 1847 O HOH A 424 46.464 56.777 9.347 1.00 38.81 O HETATM 1848 O HOH A 425 24.274 66.742 24.219 1.00 60.46 O HETATM 1849 O HOH A 426 41.517 39.337 13.840 1.00 31.33 O HETATM 1850 O HOH A 427 32.092 73.522 25.975 1.00 39.26 O HETATM 1851 O HOH A 428 32.174 71.055 29.411 1.00 36.89 O HETATM 1852 O HOH A 429 28.265 51.858 22.797 1.00 37.34 O HETATM 1853 O HOH A 430 19.135 72.831 42.485 1.00 32.19 O HETATM 1854 O HOH A 431 40.088 60.905 51.071 1.00 58.03 O HETATM 1855 O HOH A 432 36.600 60.864 30.865 1.00 54.93 O HETATM 1856 O HOH A 433 33.249 52.654 28.984 1.00 52.77 O HETATM 1857 O HOH A 434 25.174 58.031 37.025 1.00 53.10 O HETATM 1858 O HOH A 435 50.756 56.142 17.706 1.00 49.00 O HETATM 1859 O HOH A 436 34.155 69.241 20.631 1.00 43.95 O HETATM 1860 O HOH A 437 38.068 35.985 25.013 1.00 36.44 O HETATM 1861 O HOH A 438 28.659 62.891 54.888 1.00 42.17 O HETATM 1862 O HOH A 439 16.173 71.962 43.010 1.00 58.30 O HETATM 1863 O HOH A 440 20.537 61.013 22.161 1.00 54.84 O HETATM 1864 O HOH A 441 23.386 73.334 31.137 1.00 48.08 O HETATM 1865 O HOH A 442 26.714 56.786 9.479 1.00 37.84 O HETATM 1866 O HOH A 443 34.618 56.366 21.671 1.00 20.82 O HETATM 1867 O HOH A 444 23.376 57.265 17.525 1.00 30.89 O HETATM 1868 O HOH A 445 39.537 32.774 18.658 1.00 33.83 O HETATM 1869 O HOH A 446 43.832 35.533 20.599 1.00 31.85 O HETATM 1870 O HOH A 447 44.860 63.470 18.386 1.00 41.61 O HETATM 1871 O HOH A 448 24.831 59.624 34.475 1.00 46.43 O HETATM 1872 O HOH A 449 14.729 75.822 38.554 1.00 52.02 O HETATM 1873 O HOH A 450 32.697 65.399 26.603 1.00 44.50 O HETATM 1874 O HOH A 451 29.067 59.741 27.892 1.00 80.96 O HETATM 1875 O HOH A 452 49.769 49.147 21.355 1.00 56.15 O HETATM 1876 O HOH A 453 29.928 53.057 42.979 1.00 41.64 O HETATM 1877 O HOH A 454 35.555 67.893 29.949 1.00 60.63 O HETATM 1878 O HOH A 455 29.335 57.762 9.107 1.00 43.67 O HETATM 1879 O HOH A 456 33.451 57.708 32.035 1.00 56.83 O HETATM 1880 O HOH A 457 35.749 67.962 44.659 1.00 56.71 O HETATM 1881 O HOH A 458 26.529 43.202 13.484 1.00 57.44 O HETATM 1882 O HOH A 459 23.037 64.632 20.098 1.00 54.55 O HETATM 1883 O HOH A 460 45.876 61.044 17.590 1.00 36.10 O HETATM 1884 O HOH A 461 24.523 46.012 19.933 1.00 54.36 O HETATM 1885 O HOH A 462 25.740 61.340 53.197 1.00 52.28 O HETATM 1886 O HOH A 463 36.762 70.764 33.847 1.00 58.22 O HETATM 1887 O HOH A 464 51.390 47.806 8.632 1.00 45.48 O HETATM 1888 O HOH A 465 38.419 39.020 12.771 1.00 44.13 O HETATM 1889 O HOH A 466 41.978 33.841 22.360 1.00 42.46 O HETATM 1890 O HOH A 468 27.874 69.775 28.194 1.00 47.01 O HETATM 1891 O HOH A 469 34.097 70.483 27.337 1.00 50.35 O HETATM 1892 O HOH A 470 38.043 67.992 37.950 1.00 54.55 O HETATM 1893 O HOH A 471 27.285 56.399 41.293 1.00 61.41 O HETATM 1894 O HOH A 472 26.088 68.532 53.205 1.00 52.81 O HETATM 1895 O HOH A 473 48.001 56.862 23.019 1.00 46.16 O HETATM 1896 O HOH A 474 50.644 57.453 14.461 1.00 44.32 O HETATM 1897 O HOH A 475 33.393 68.088 28.498 1.00 49.10 O HETATM 1898 O HOH A 476 32.409 60.005 8.702 1.00 53.15 O HETATM 1899 O HOH A 477 37.455 50.266 33.771 1.00 45.82 O HETATM 1900 O HOH A 478 18.104 54.322 36.435 1.00 51.97 O HETATM 1901 O HOH A 479 46.626 40.918 17.224 1.00 54.78 O HETATM 1902 O HOH A 480 18.767 51.454 17.195 1.00 57.45 O HETATM 1903 O HOH A 481 19.698 51.524 19.636 1.00 69.46 O HETATM 1904 O HOH A 482 15.673 55.190 43.166 1.00 54.05 O HETATM 1905 O HOH A 483 46.087 55.034 26.256 1.00 58.68 O HETATM 1906 O HOH A 484 33.070 56.747 50.358 1.00 49.56 O HETATM 1907 O HOH A 485 50.703 42.230 15.789 1.00 53.38 O HETATM 1908 O HOH A 486 23.187 70.734 16.488 1.00 68.53 O HETATM 1909 O HOH A 487 23.338 70.407 19.208 1.00 70.34 O HETATM 1910 O HOH A 488 12.213 72.029 34.341 1.00 58.45 O HETATM 1911 O HOH A 489 41.869 65.388 38.789 1.00 63.29 O HETATM 1912 O HOH A 490 47.266 56.519 4.783 1.00 60.77 O CONECT 283 338 CONECT 338 283 MASTER 315 0 0 10 10 0 0 6 1911 1 2 19 END A second structure was input as follows:HEADER AMINO-ACID BINDING PROTEIN 25-FEB-93 1LST TITLE THREE-DIMENSIONAL STRUCTURES OF THE PERIPLASMIC LYSINE-, ARGININE-, TITLE 2 ORNITHINE-BINDING PROTEIN WITH AND WITHOUT A LIGAND COMPND MOL_ID: 1; COMPND 2 MOLECULE: LYSINE, ARGININE, ORNITHINE-BINDING PROTEIN; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SALMONELLA TYPHIMURIUM; SOURCE 3 ORGANISM_TAXID: 602 KEYWDS AMINO-ACID BINDING PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR S.-H.KIM,B.-H.OH REVDAT 5 23-OCT-24 1LST 1 REMARK SEQADV REVDAT 4 29-NOV-17 1LST 1 HELIX REVDAT 3 24-FEB-09 1LST 1 VERSN REVDAT 2 01-APR-03 1LST 1 JRNL REVDAT 1 22-JUN-94 1LST 0 JRNL AUTH B.H.OH,J.PANDIT,C.H.KANG,K.NIKAIDO,S.GOKCEN,G.F.AMES,S.H.KIM JRNL TITL THREE-DIMENSIONAL STRUCTURES OF THE PERIPLASMIC JRNL TITL 2 LYSINE/ARGININE/ORNITHINE-BINDING PROTEIN WITH AND WITHOUT A JRNL TITL 3 LIGAND. JRNL REF J.BIOL.CHEM. V. 268 11348 1993 JRNL REFN ISSN 0021-9258 JRNL PMID 8496186 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH C.-H.KANG,W.-C.SHIN,Y.YAMAGATA,S.GOKCEN,G.F.-L.AMES,S.-H.KIM REMARK 1 TITL CRYSTAL STRUCTURE OF THE LYSINE-, ARGININE-, REMARK 1 TITL 2 ORNITHINE-BINDING PROTEIN FROM SALMONELLA TYPHIMURIUM AT 2.7 REMARK 1 TITL 3 ANGSTROMS RESOLUTION REMARK 1 REF J.BIOL.CHEM. V. 266 23893 1992 REMARK 1 REFN ISSN 0021-9258 REMARK 2 REMARK 2 RESOLUTION. 1.80 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 6.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000 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 : 23359 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : NULL REMARK 3 FREE R VALUE TEST SET SELECTION : NULL REMARK 3 R VALUE (WORKING SET) : 0.165 REMARK 3 FREE R VALUE : NULL 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 : 1805 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 10 REMARK 3 SOLVENT ATOMS : 199 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL 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) : 0.013 REMARK 3 BOND ANGLES (DEGREES) : 2.540 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 1LST COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL. REMARK 100 THE DEPOSITION ID IS D_1000174820. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : NULL REMARK 200 TEMPERATURE (KELVIN) : NULL REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : NULL REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : NULL REMARK 200 RADIATION SOURCE : NULL REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL REMARK 200 WAVELENGTH OR RANGE (A) : NULL REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : NULL REMARK 200 DETECTOR MANUFACTURER : NULL REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL REMARK 200 DATA SCALING SOFTWARE : NULL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL REMARK 200 RESOLUTION RANGE HIGH (A) : NULL REMARK 200 RESOLUTION RANGE LOW (A) : NULL REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : NULL REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : NULL REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: NULL REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL REMARK 200 SOFTWARE USED: X-PLOR REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 50.67 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: NULL 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 18.89500 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 57.96500 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 29.81500 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 57.96500 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 18.89500 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 29.81500 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 LYS A 239 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 GLN A 4 CG CD OE1 NE2 REMARK 470 LYS A 110 CG CD CE NZ REMARK 470 LYS A 176 CG CD CE NZ REMARK 470 GLU A 177 CG CD OE1 OE2 REMARK 470 LYS A 188 CG CD CE NZ REMARK 470 LYS A 189 CG CD CE NZ REMARK 470 LYS A 228 CG CD CE NZ REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 HIS A 113 NE2 HIS A 113 CD2 -0.075 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 TRP A 47 CD1 - CG - CD2 ANGL. DEV. = 6.3 DEGREES REMARK 500 TRP A 47 CE2 - CD2 - CG ANGL. DEV. = -5.3 DEGREES REMARK 500 ARG A 93 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES REMARK 500 TRP A 130 CD1 - CG - CD2 ANGL. DEV. = 5.3 DEGREES REMARK 500 TRP A 130 CE2 - CD2 - CG ANGL. DEV. = -5.2 DEGREES REMARK 500 TYR A 147 CB - CG - CD2 ANGL. DEV. = -3.8 DEGREES REMARK 500 ARG A 200 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES REMARK 500 ARG A 200 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES REMARK 500 GLY A 237 N - CA - C ANGL. DEV. = -15.8 DEGREES REMARK 500 REMARK 500 REMARK: NULL 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 THR A 12 34.33 -82.50 REMARK 500 SER A 69 47.50 -161.90 REMARK 500 PHE A 169 -58.42 -141.43 REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LYS A 240 REMARK 999 REMARK 999 SEQUENCE REMARK 999 SEQUENCE ADVISORY NOTICE: REMARK 999 DIFFERENCE BETWEEN SWISS-PROT AND PDB SEQUENCE. REMARK 999 REMARK 999 SWISS-PROT ENTRY NAME: ARGT_SALTY REMARK 999 REMARK 999 SWISS-PROT RESIDUE PDB SEQRES REMARK 999 NAME NUMBER NAME CHAIN SEQ/INSERT CODE REMARK 999 VAL 102 ILE 102 REMARK 999 REMARK 999 RESIDUE 102 OF THE LAO PROTEIN IS ISOLEUCINE, BUT WAS REMARK 999 REPORTED AS VALINE IN SWISS-PROT DATA BANK DUE TO REMARK 999 SEQUENCING ERROR (PERSONAL COMMUNICATION). DBREF 1LST A 1 238 UNP P02911 ARGT_SALTY 23 260 SEQADV 1LST ILE A 102 UNP P02911 VAL 124 CONFLICT SEQRES 1 A 239 ALA LEU PRO GLN THR VAL ARG ILE GLY THR ASP THR THR SEQRES 2 A 239 TYR ALA PRO PHE SER SER LYS ASP ALA LYS GLY GLU PHE SEQRES 3 A 239 ILE GLY PHE ASP ILE ASP LEU GLY ASN GLU MET CYS LYS SEQRES 4 A 239 ARG MET GLN VAL LYS CYS THR TRP VAL ALA SER ASP PHE SEQRES 5 A 239 ASP ALA LEU ILE PRO SER LEU LYS ALA LYS LYS ILE ASP SEQRES 6 A 239 ALA ILE ILE SER SER LEU SER ILE THR ASP LYS ARG GLN SEQRES 7 A 239 GLN GLU ILE ALA PHE SER ASP LYS LEU TYR ALA ALA ASP SEQRES 8 A 239 SER ARG LEU ILE ALA ALA LYS GLY SER PRO ILE GLN PRO SEQRES 9 A 239 THR LEU GLU SER LEU LYS GLY LYS HIS VAL GLY VAL LEU SEQRES 10 A 239 GLN GLY SER THR GLN GLU ALA TYR ALA ASN ASP ASN TRP SEQRES 11 A 239 ARG THR LYS GLY VAL ASP VAL VAL ALA TYR ALA ASN GLN SEQRES 12 A 239 ASP LEU ILE TYR SER ASP LEU THR ALA GLY ARG LEU ASP SEQRES 13 A 239 ALA ALA LEU GLN ASP GLU VAL ALA ALA SER GLU GLY PHE SEQRES 14 A 239 LEU LYS GLN PRO ALA GLY LYS GLU TYR ALA PHE ALA GLY SEQRES 15 A 239 PRO SER VAL LYS ASP LYS LYS TYR PHE GLY ASP GLY THR SEQRES 16 A 239 GLY VAL GLY LEU ARG LYS ASP ASP THR GLU LEU LYS ALA SEQRES 17 A 239 ALA PHE ASP LYS ALA LEU THR GLU LEU ARG GLN ASP GLY SEQRES 18 A 239 THR TYR ASP LYS MET ALA LYS LYS TYR PHE ASP PHE ASN SEQRES 19 A 239 VAL TYR GLY ASP LYS HET LYS A 240 10 HETNAM LYS LYSINE FORMUL 2 LYS C6 H15 N2 O2 1+ FORMUL 3 HOH *199(H2 O) HELIX 1 A PHE A 29 MET A 41 1 13 HELIX 2 B LEU A 55 LYS A 60 1 6 HELIX 3 C ASP A 75 GLU A 80 1 6 HELIX 4 D LEU A 106 LEU A 109 1 4 HELIX 5 E THR A 121 ASN A 129 1 9 HELIX 6 F GLN A 143 THR A 151 1 9 HELIX 7 G GLU A 162 GLY A 168 1 7 HELIX 8 H LYS A 188 PHE A 191 1 4 HELIX 9 I THR A 204 GLN A 219 1 16 HELIX 10 J THR A 222 LYS A 228 1 7 SHEET 1 1 5 LYS A 44 ALA A 49 0 SHEET 2 1 5 THR A 5 THR A 10 1 SHEET 3 1 5 ALA A 66 ILE A 67 1 SHEET 4 1 5 VAL A 197 LEU A 199 -1 SHEET 5 1 5 ALA A 82 SER A 84 1 SHEET 1 2 5 ASP A 136 TYR A 140 0 SHEET 2 2 5 HIS A 113 LEU A 117 1 SHEET 3 2 5 ALA A 157 ASP A 161 1 SHEET 4 2 5 SER A 92 ALA A 97 -1 SHEET 5 2 5 TYR A 178 ALA A 181 1 SSBOND 1 CYS A 38 CYS A 45 1555 1555 2.01 CISPEP 1 ALA A 15 PRO A 16 0 4.08 SITE 1 AC1 13 ASP A 11 TYR A 14 PHE A 52 SER A 69 SITE 2 AC1 13 SER A 70 SER A 72 ARG A 77 LEU A 117 SITE 3 AC1 13 SER A 120 THR A 121 GLN A 122 ASP A 161 SITE 4 AC1 13 HOH A 426 CRYST1 37.790 59.630 115.930 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 0.026462 0.000000 0.000000 0.00000 SCALE2 0.000000 0.016770 0.000000 0.00000 SCALE3 0.000000 0.000000 0.008626 0.00000 ATOM 1 N ALA A 1 19.369 88.165 50.553 1.00 70.42 N ATOM 2 CA ALA A 1 20.320 87.836 51.572 1.00 70.30 C ATOM 3 C ALA A 1 20.770 86.371 51.506 1.00 69.35 C ATOM 4 O ALA A 1 20.528 85.561 52.410 1.00 71.17 O ATOM 5 CB ALA A 1 19.690 88.125 52.940 1.00 71.87 C ATOM 6 N LEU A 2 21.436 85.981 50.422 1.00 66.16 N ATOM 7 CA LEU A 2 22.031 84.651 50.374 1.00 62.78 C ATOM 8 C LEU A 2 23.360 84.688 51.130 1.00 60.84 C ATOM 9 O LEU A 2 23.968 85.772 51.171 1.00 61.42 O ATOM 10 CB LEU A 2 22.261 84.256 48.936 1.00 61.89 C ATOM 11 CG LEU A 2 20.995 84.214 48.119 1.00 61.54 C ATOM 12 CD1 LEU A 2 21.370 83.775 46.731 1.00 63.11 C ATOM 13 CD2 LEU A 2 19.973 83.291 48.744 1.00 60.35 C ATOM 14 N PRO A 3 23.839 83.601 51.774 1.00 58.10 N ATOM 15 CA PRO A 3 25.134 83.568 52.431 1.00 55.80 C ATOM 16 C PRO A 3 26.280 83.849 51.469 1.00 54.93 C ATOM 17 O PRO A 3 26.187 83.660 50.257 1.00 55.14 O ATOM 18 CB PRO A 3 25.185 82.187 53.070 1.00 55.72 C ATOM 19 CG PRO A 3 24.273 81.328 52.232 1.00 55.93 C ATOM 20 CD PRO A 3 23.154 82.313 51.918 1.00 56.85 C ATOM 21 N GLN A 4 27.388 84.340 52.019 1.00 54.15 N ATOM 22 CA GLN A 4 28.575 84.609 51.210 1.00 52.13 C ATOM 23 C GLN A 4 29.162 83.296 50.686 1.00 48.91 C ATOM 24 O GLN A 4 29.678 83.204 49.562 1.00 49.37 O ATOM 25 CB GLN A 4 29.640 85.327 52.049 1.00 53.76 C ATOM 26 N THR A 5 29.058 82.290 51.560 1.00 44.14 N ATOM 27 CA THR A 5 29.485 80.947 51.273 1.00 39.74 C ATOM 28 C THR A 5 28.308 80.043 51.545 1.00 35.08 C ATOM 29 O THR A 5 27.744 80.087 52.645 1.00 35.11 O ATOM 30 CB THR A 5 30.655 80.569 52.168 1.00 41.62 C ATOM 31 OG1 THR A 5 31.605 81.608 51.937 1.00 45.01 O ATOM 32 CG2 THR A 5 31.221 79.204 51.899 1.00 41.46 C ATOM 33 N VAL A 6 27.932 79.264 50.545 1.00 27.99 N ATOM 34 CA VAL A 6 26.917 78.248 50.699 1.00 22.61 C ATOM 35 C VAL A 6 27.684 76.946 50.951 1.00 19.55 C ATOM 36 O VAL A 6 28.575 76.581 50.167 1.00 17.86 O ATOM 37 CB VAL A 6 26.111 78.149 49.433 1.00 21.13 C ATOM 38 CG1 VAL A 6 25.082 77.002 49.533 1.00 21.03 C ATOM 39 CG2 VAL A 6 25.418 79.492 49.239 1.00 21.21 C ATOM 40 N ARG A 7 27.377 76.260 52.068 1.00 16.77 N ATOM 41 CA ARG A 7 28.034 75.021 52.461 1.00 13.67 C ATOM 42 C ARG A 7 27.191 73.859 51.930 1.00 12.49 C ATOM 43 O ARG A 7 26.013 73.746 52.260 1.00 12.27 O ATOM 44 CB ARG A 7 28.145 75.014 53.978 1.00 13.68 C ATOM 45 CG ARG A 7 29.102 76.129 54.449 1.00 16.83 C ATOM 46 CD ARG A 7 29.208 76.266 55.973 1.00 16.89 C ATOM 47 NE ARG A 7 29.383 74.994 56.671 1.00 19.15 N ATOM 48 CZ ARG A 7 30.525 74.271 56.714 1.00 17.36 C ATOM 49 NH1 ARG A 7 31.641 74.657 56.110 1.00 18.26 N ATOM 50 NH2 ARG A 7 30.531 73.132 57.392 1.00 18.18 N ATOM 51 N ILE A 8 27.723 73.037 51.037 1.00 12.80 N ATOM 52 CA ILE A 8 26.972 71.972 50.385 1.00 13.14 C ATOM 53 C ILE A 8 27.532 70.640 50.850 1.00 12.18 C ATOM 54 O ILE A 8 28.731 70.367 50.697 1.00 13.88 O ATOM 55 CB ILE A 8 27.107 72.044 48.857 1.00 13.58 C ATOM 56 CG1 ILE A 8 26.758 73.469 48.354 1.00 12.96 C ATOM 57 CG2 ILE A 8 26.182 70.960 48.237 1.00 10.36 C ATOM 58 CD1 ILE A 8 26.953 73.664 46.831 1.00 16.76 C ATOM 59 N GLY A 9 26.660 69.830 51.448 1.00 13.01 N ATOM 60 CA GLY A 9 27.034 68.506 51.902 1.00 12.06 C ATOM 61 C GLY A 9 26.781 67.463 50.813 1.00 12.23 C ATOM 62 O GLY A 9 25.761 67.514 50.109 1.00 12.05 O ATOM 63 N THR A 10 27.685 66.492 50.731 1.00 11.98 N ATOM 64 CA THR A 10 27.561 65.397 49.785 1.00 12.30 C ATOM 65 C THR A 10 28.251 64.170 50.398 1.00 14.49 C ATOM 66 O THR A 10 29.154 64.256 51.256 1.00 15.40 O ATOM 67 CB THR A 10 28.218 65.812 48.419 1.00 12.87 C ATOM 68 OG1 THR A 10 27.768 64.846 47.467 1.00 13.11 O ATOM 69 CG2 THR A 10 29.762 65.873 48.438 1.00 10.92 C ATOM 70 N ASP A 11 27.820 62.992 49.954 1.00 14.06 N ATOM 71 CA ASP A 11 28.395 61.725 50.357 1.00 14.03 C ATOM 72 C ASP A 11 29.184 61.268 49.135 1.00 14.23 C ATOM 73 O ASP A 11 28.656 60.836 48.089 1.00 14.08 O ATOM 74 CB ASP A 11 27.255 60.771 50.704 1.00 15.71 C ATOM 75 CG ASP A 11 27.613 59.292 50.661 1.00 19.66 C ATOM 76 OD1 ASP A 11 28.762 58.923 50.885 1.00 20.02 O ATOM 77 OD2 ASP A 11 26.721 58.508 50.384 1.00 22.49 O ATOM 78 N THR A 12 30.499 61.287 49.334 1.00 13.59 N ATOM 79 CA THR A 12 31.423 61.014 48.244 1.00 13.99 C ATOM 80 C THR A 12 31.681 59.543 47.941 1.00 12.87 C ATOM 81 O THR A 12 32.812 59.189 47.593 1.00 13.41 O ATOM 82 CB THR A 12 32.740 61.783 48.558 1.00 15.70 C ATOM 83 OG1 THR A 12 33.189 61.475 49.874 1.00 20.08 O ATOM 84 CG2 THR A 12 32.496 63.282 48.430 1.00 16.14 C ATOM 85 N THR A 13 30.700 58.648 48.090 1.00 13.58 N ATOM 86 CA THR A 13 30.877 57.241 47.756 1.00 14.59 C ATOM 87 C THR A 13 29.784 56.802 46.783 1.00 13.73 C ATOM 88 O THR A 13 29.242 55.701 46.894 1.00 16.15 O ATOM 89 CB THR A 13 30.857 56.374 49.077 1.00 13.81 C ATOM 90 OG1 THR A 13 29.618 56.565 49.725 1.00 17.43 O ATOM 91 CG2 THR A 13 31.964 56.734 50.023 1.00 15.94 C ATOM 92 N TYR A 14 29.420 57.627 45.812 1.00 12.18 N ATOM 93 CA TYR A 14 28.366 57.268 44.876 1.00 12.77 C ATOM 94 C TYR A 14 28.737 57.721 43.455 1.00 13.11 C ATOM 95 O TYR A 14 28.135 58.617 42.848 1.00 12.17 O ATOM 96 CB TYR A 14 27.111 57.924 45.381 1.00 11.24 C ATOM 97 CG TYR A 14 25.862 57.069 45.335 1.00 12.50 C ATOM 98 CD1 TYR A 14 25.733 55.916 46.102 1.00 10.39 C ATOM 99 CD2 TYR A 14 24.823 57.487 44.534 1.00 12.84 C ATOM 100 CE1 TYR A 14 24.543 55.200 46.079 1.00 9.67 C ATOM 101 CE2 TYR A 14 23.635 56.772 44.500 1.00 12.74 C ATOM 102 CZ TYR A 14 23.500 55.640 45.290 1.00 11.35 C ATOM 103 OH TYR A 14 22.280 54.972 45.275 1.00 9.80 O ATOM 104 N ALA A 15 29.795 57.132 42.904 1.00 13.58 N ATOM 105 CA ALA A 15 30.274 57.509 41.596 1.00 14.97 C ATOM 106 C ALA A 15 29.208 57.078 40.596 1.00 16.67 C ATOM 107 O ALA A 15 28.518 56.092 40.865 1.00 16.91 O ATOM 108 CB ALA A 15 31.582 56.792 41.321 1.00 15.89 C ATOM 109 N PRO A 16 28.957 57.741 39.467 1.00 15.66 N ATOM 110 CA PRO A 16 29.694 58.893 38.985 1.00 14.94 C ATOM 111 C PRO A 16 29.122 60.230 39.485 1.00 14.80 C ATOM 112 O PRO A 16 29.434 61.290 38.915 1.00 15.41 O ATOM 113 CB PRO A 16 29.621 58.689 37.477 1.00 15.39 C ATOM 114 CG PRO A 16 28.186 58.249 37.279 1.00 13.36 C ATOM 115 CD PRO A 16 27.917 57.365 38.509 1.00 15.76 C ATOM 116 N PHE A 17 28.258 60.228 40.511 1.00 12.27 N ATOM 117 CA PHE A 17 27.594 61.443 40.939 1.00 12.81 C ATOM 118 C PHE A 17 28.445 62.177 41.939 1.00 13.41 C ATOM 119 O PHE A 17 28.590 63.397 41.828 1.00 12.53 O ATOM 120 CB PHE A 17 26.195 61.127 41.558 1.00 12.19 C ATOM 121 CG PHE A 17 25.245 60.571 40.485 1.00 12.34 C ATOM 122 CD1 PHE A 17 24.700 61.408 39.503 1.00 13.40 C ATOM 123 CD2 PHE A 17 24.951 59.211 40.455 1.00 14.18 C ATOM 124 CE1 PHE A 17 23.890 60.904 38.498 1.00 14.02 C ATOM 125 CE2 PHE A 17 24.134 58.707 39.442 1.00 15.95 C ATOM 126 CZ PHE A 17 23.615 59.547 38.463 1.00 15.17 C ATOM 127 N SER A 18 29.049 61.467 42.875 1.00 12.58 N ATOM 128 CA SER A 18 29.853 62.117 43.880 1.00 13.67 C ATOM 129 C SER A 18 30.913 61.139 44.354 1.00 15.29 C ATOM 130 O SER A 18 30.573 60.086 44.917 1.00 13.73 O ATOM 131 CB SER A 18 28.945 62.545 45.042 1.00 12.58 C ATOM 132 OG SER A 18 29.709 63.258 46.024 1.00 16.53 O ATOM 133 N SER A 19 32.190 61.443 44.166 1.00 15.16 N ATOM 134 CA SER A 19 33.251 60.616 44.713 1.00 17.72 C ATOM 135 C SER A 19 34.499 61.473 44.852 1.00 17.34 C ATOM 136 O SER A 19 34.429 62.691 44.706 1.00 16.20 O ATOM 137 CB SER A 19 33.539 59.378 43.804 1.00 18.71 C ATOM 138 OG SER A 19 33.959 59.846 42.554 1.00 24.25 O ATOM 139 N LYS A 20 35.631 60.894 45.178 1.00 19.55 N ATOM 140 CA LYS A 20 36.843 61.652 45.331 1.00 23.41 C ATOM 141 C LYS A 20 37.872 61.089 44.386 1.00 23.29 C ATOM 142 O LYS A 20 37.842 59.889 44.092 1.00 23.34 O ATOM 143 CB LYS A 20 37.318 61.563 46.772 1.00 27.28 C ATOM 144 CG LYS A 20 36.533 62.568 47.572 1.00 34.71 C ATOM 145 CD LYS A 20 37.101 62.687 48.960 1.00 43.23 C ATOM 146 CE LYS A 20 36.553 64.005 49.519 1.00 48.76 C ATOM 147 NZ LYS A 20 36.844 64.109 50.946 1.00 54.29 N ATOM 148 N ASP A 21 38.741 61.942 43.832 1.00 22.42 N ATOM 149 CA ASP A 21 39.807 61.438 42.984 1.00 22.71 C ATOM 150 C ASP A 21 41.041 61.051 43.811 1.00 22.97 C ATOM 151 O ASP A 21 41.022 61.128 45.052 1.00 22.19 O ATOM 152 CB ASP A 21 40.151 62.499 41.962 1.00 23.13 C ATOM 153 CG ASP A 21 40.839 63.772 42.441 1.00 25.62 C ATOM 154 OD1 ASP A 21 41.274 63.896 43.586 1.00 22.53 O ATOM 155 OD2 ASP A 21 40.924 64.677 41.624 1.00 29.80 O ATOM 156 N ALA A 22 42.177 60.798 43.158 1.00 24.61 N ATOM 157 CA ALA A 22 43.387 60.368 43.872 1.00 27.45 C ATOM 158 C ALA A 22 43.999 61.375 44.818 1.00 27.64 C ATOM 159 O ALA A 22 44.688 61.008 45.769 1.00 29.14 O ATOM 160 CB ALA A 22 44.492 59.972 42.900 1.00 28.02 C ATOM 161 N LYS A 23 43.782 62.655 44.532 1.00 28.15 N ATOM 162 CA LYS A 23 44.264 63.722 45.407 1.00 29.06 C ATOM 163 C LYS A 23 43.249 64.040 46.499 1.00 28.23 C ATOM 164 O LYS A 23 43.495 64.917 47.326 1.00 28.94 O ATOM 165 CB LYS A 23 44.466 65.030 44.691 1.00 29.98 C ATOM 166 CG LYS A 23 45.208 65.052 43.416 1.00 35.10 C ATOM 167 CD LYS A 23 45.159 66.535 43.073 1.00 39.20 C ATOM 168 CE LYS A 23 45.068 66.758 41.561 1.00 43.11 C ATOM 169 NZ LYS A 23 43.776 66.369 41.013 1.00 44.51 N ATOM 170 N GLY A 24 42.053 63.426 46.488 1.00 28.47 N ATOM 171 CA GLY A 24 41.008 63.732 47.455 1.00 25.86 C ATOM 172 C GLY A 24 40.120 64.902 47.053 1.00 25.48 C ATOM 173 O GLY A 24 39.365 65.410 47.878 1.00 27.67 O ATOM 174 N GLU A 25 40.207 65.415 45.838 1.00 24.71 N ATOM 175 CA GLU A 25 39.284 66.438 45.339 1.00 26.05 C ATOM 176 C GLU A 25 37.935 65.784 45.046 1.00 23.18 C ATOM 177 O GLU A 25 37.872 64.624 44.632 1.00 20.38 O ATOM 178 CB GLU A 25 39.780 67.054 44.036 1.00 31.59 C ATOM 179 CG GLU A 25 41.008 67.936 44.158 1.00 44.09 C ATOM 180 CD GLU A 25 40.614 69.281 44.759 1.00 52.91 C ATOM 181 OE1 GLU A 25 40.081 70.105 44.005 1.00 58.27 O ATOM 182 OE2 GLU A 25 40.810 69.492 45.964 1.00 56.96 O ATOM 183 N PHE A 26 36.854 66.528 45.200 1.00 21.75 N ATOM 184 CA PHE A 26 35.485 66.062 44.986 1.00 20.92 C ATOM 185 C PHE A 26 35.234 66.022 43.480 1.00 19.48 C ATOM 186 O PHE A 26 35.561 66.984 42.770 1.00 18.25 O ATOM 187 CB PHE A 26 34.477 67.036 45.649 1.00 24.79 C ATOM 188 CG PHE A 26 34.385 67.084 47.190 1.00 29.07 C ATOM 189 CD1 PHE A 26 35.380 67.642 47.973 1.00 33.69 C ATOM 190 CD2 PHE A 26 33.259 66.609 47.837 1.00 29.26 C ATOM 191 CE1 PHE A 26 35.249 67.718 49.352 1.00 33.20 C ATOM 192 CE2 PHE A 26 33.133 66.688 49.213 1.00 28.90 C ATOM 193 CZ PHE A 26 34.126 67.240 49.975 1.00 28.69 C ATOM 194 N ILE A 27 34.688 64.940 42.932 1.00 16.45 N ATOM 195 CA ILE A 27 34.430 64.831 41.499 1.00 16.96 C ATOM 196 C ILE A 27 33.089 64.160 41.237 1.00 14.51 C ATOM 197 O ILE A 27 32.580 63.386 42.055 1.00 15.60 O ATOM 198 CB ILE A 27 35.506 63.989 40.747 1.00 16.86 C ATOM 199 CG1 ILE A 27 35.637 62.613 41.374 1.00 17.53 C ATOM 200 CG2 ILE A 27 36.828 64.761 40.737 1.00 19.66 C ATOM 201 CD1 ILE A 27 36.414 61.642 40.490 1.00 18.40 C ATOM 202 N GLY A 28 32.479 64.465 40.102 1.00 13.83 N ATOM 203 CA GLY A 28 31.269 63.777 39.703 1.00 11.75 C ATOM 204 C GLY A 28 30.213 64.728 39.210 1.00 11.35 C ATOM 205 O GLY A 28 30.333 65.946 39.349 1.00 13.79 O ATOM 206 N PHE A 29 29.137 64.194 38.655 1.00 11.84 N ATOM 207 CA PHE A 29 28.093 65.001 38.060 1.00 13.54 C ATOM 208 C PHE A 29 27.417 65.914 39.084 1.00 14.44 C ATOM 209 O PHE A 29 27.101 67.064 38.748 1.00 13.05 O ATOM 210 CB PHE A 29 27.063 64.083 37.414 1.00 13.14 C ATOM 211 CG PHE A 29 26.039 64.822 36.550 1.00 14.71 C ATOM 212 CD1 PHE A 29 26.460 65.723 35.573 1.00 14.38 C ATOM 213 CD2 PHE A 29 24.683 64.565 36.719 1.00 14.14 C ATOM 214 CE1 PHE A 29 25.517 66.345 34.772 1.00 16.25 C ATOM 215 CE2 PHE A 29 23.757 65.195 35.911 1.00 13.34 C ATOM 216 CZ PHE A 29 24.172 66.086 34.942 1.00 13.29 C ATOM 217 N ASP A 30 27.221 65.466 40.340 1.00 13.38 N ATOM 218 CA ASP A 30 26.635 66.320 41.379 1.00 12.86 C ATOM 219 C ASP A 30 27.511 67.511 41.697 1.00 13.37 C ATOM 220 O ASP A 30 26.999 68.623 41.908 1.00 13.05 O ATOM 221 CB ASP A 30 26.411 65.557 42.690 1.00 11.57 C ATOM 222 CG ASP A 30 25.127 64.729 42.730 1.00 13.94 C ATOM 223 OD1 ASP A 30 24.314 64.812 41.819 1.00 13.97 O ATOM 224 OD2 ASP A 30 24.929 64.016 43.707 1.00 16.49 O ATOM 225 N ILE A 31 28.823 67.280 41.663 1.00 11.99 N ATOM 226 CA ILE A 31 29.805 68.335 41.952 1.00 14.45 C ATOM 227 C ILE A 31 29.784 69.322 40.779 1.00 13.87 C ATOM 228 O ILE A 31 29.719 70.542 40.977 1.00 12.98 O ATOM 229 CB ILE A 31 31.268 67.702 42.163 1.00 14.01 C ATOM 230 CG1 ILE A 31 31.210 66.528 43.194 1.00 15.06 C ATOM 231 CG2 ILE A 31 32.265 68.795 42.596 1.00 15.18 C ATOM 232 CD1 ILE A 31 30.700 66.787 44.611 1.00 14.01 C ATOM 233 N ASP A 32 29.751 68.825 39.539 1.00 13.63 N ATOM 234 CA ASP A 32 29.694 69.704 38.375 1.00 15.28 C ATOM 235 C ASP A 32 28.444 70.569 38.353 1.00 16.09 C ATOM 236 O ASP A 32 28.535 71.783 38.079 1.00 14.80 O ATOM 237 CB ASP A 32 29.738 68.903 37.073 1.00 14.01 C ATOM 238 CG ASP A 32 31.059 68.189 36.852 1.00 16.22 C ATOM 239 OD1 ASP A 32 32.064 68.522 37.483 1.00 17.57 O ATOM 240 OD2 ASP A 32 31.091 67.257 36.046 1.00 18.74 O ATOM 241 N LEU A 33 27.276 69.981 38.641 1.00 13.88 N ATOM 242 CA LEU A 33 26.048 70.740 38.701 1.00 14.18 C ATOM 243 C LEU A 33 26.084 71.759 39.839 1.00 15.67 C ATOM 244 O LEU A 33 25.724 72.922 39.600 1.00 15.28 O ATOM 245 CB LEU A 33 24.848 69.822 38.904 1.00 15.52 C ATOM 246 CG LEU A 33 24.379 68.974 37.743 1.00 17.33 C ATOM 247 CD1 LEU A 33 23.395 67.933 38.233 1.00 18.87 C ATOM 248 CD2 LEU A 33 23.715 69.864 36.715 1.00 18.89 C ATOM 249 N GLY A 34 26.518 71.386 41.059 1.00 14.80 N ATOM 250 CA GLY A 34 26.571 72.316 42.187 1.00 14.16 C ATOM 251 C GLY A 34 27.488 73.500 41.864 1.00 15.34 C ATOM 252 O GLY A 34 27.155 74.678 42.078 1.00 14.79 O ATOM 253 N ASN A 35 28.675 73.223 41.342 1.00 15.42 N ATOM 254 CA ASN A 35 29.611 74.294 41.020 1.00 16.13 C ATOM 255 C ASN A 35 29.121 75.217 39.904 1.00 16.43 C ATOM 256 O ASN A 35 29.310 76.432 39.993 1.00 16.00 O ATOM 257 CB ASN A 35 30.944 73.724 40.613 1.00 14.83 C ATOM 258 CG ASN A 35 31.766 73.186 41.771 1.00 16.08 C ATOM 259 OD1 ASN A 35 32.641 72.341 41.565 1.00 20.09 O ATOM 260 ND2 ASN A 35 31.565 73.582 43.014 1.00 15.94 N ATOM 261 N GLU A 36 28.451 74.706 38.886 1.00 16.33 N ATOM 262 CA GLU A 36 27.926 75.554 37.825 1.00 17.55 C ATOM 263 C GLU A 36 26.810 76.438 38.379 1.00 17.27 C ATOM 264 O GLU A 36 26.776 77.651 38.130 1.00 17.87 O ATOM 265 CB GLU A 36 27.391 74.686 36.685 1.00 15.86 C ATOM 266 CG GLU A 36 26.879 75.521 35.526 1.00 16.34 C ATOM 267 CD GLU A 36 27.941 76.370 34.829 1.00 21.93 C ATOM 268 OE1 GLU A 36 29.128 76.029 34.831 1.00 23.71 O ATOM 269 OE2 GLU A 36 27.590 77.399 34.254 1.00 26.13 O ATOM 270 N MET A 37 25.875 75.865 39.175 1.00 16.46 N ATOM 271 CA MET A 37 24.821 76.640 39.826 1.00 16.10 C ATOM 272 C MET A 37 25.429 77.711 40.755 1.00 17.05 C ATOM 273 O MET A 37 25.003 78.873 40.671 1.00 16.31 O ATOM 274 CB MET A 37 23.886 75.737 40.651 1.00 15.80 C ATOM 275 CG MET A 37 22.955 74.926 39.747 1.00 14.66 C ATOM 276 SD MET A 37 21.660 73.972 40.576 1.00 17.97 S ATOM 277 CE MET A 37 22.702 72.738 41.284 1.00 17.59 C ATOM 278 N CYS A 38 26.453 77.414 41.580 1.00 15.99 N ATOM 279 CA CYS A 38 27.073 78.408 42.446 1.00 17.35 C ATOM 280 C CYS A 38 27.647 79.567 41.647 1.00 19.80 C ATOM 281 O CYS A 38 27.463 80.723 42.055 1.00 19.95 O ATOM 282 CB CYS A 38 28.183 77.791 43.266 1.00 17.58 C ATOM 283 SG CYS A 38 27.498 76.595 44.466 1.00 20.66 S ATOM 284 N LYS A 39 28.266 79.256 40.499 1.00 20.84 N ATOM 285 CA LYS A 39 28.826 80.224 39.558 1.00 23.61 C ATOM 286 C LYS A 39 27.707 81.113 39.032 1.00 23.46 C ATOM 287 O LYS A 39 27.840 82.335 39.083 1.00 26.41 O ATOM 288 CB LYS A 39 29.487 79.485 38.409 1.00 26.96 C ATOM 289 CG LYS A 39 30.105 80.357 37.361 1.00 33.91 C ATOM 290 CD LYS A 39 30.240 79.572 36.065 1.00 39.14 C ATOM 291 CE LYS A 39 30.924 80.426 34.986 1.00 46.36 C ATOM 292 NZ LYS A 39 30.187 81.642 34.643 1.00 50.47 N ATOM 293 N ARG A 40 26.583 80.577 38.564 1.00 21.46 N ATOM 294 CA ARG A 40 25.460 81.404 38.148 1.00 22.44 C ATOM 295 C ARG A 40 24.763 82.176 39.264 1.00 26.03 C ATOM 296 O ARG A 40 24.224 83.267 39.026 1.00 24.48 O ATOM 297 CB ARG A 40 24.433 80.557 37.441 1.00 21.95 C ATOM 298 CG ARG A 40 25.156 80.101 36.202 1.00 25.33 C ATOM 299 CD ARG A 40 24.285 79.290 35.319 1.00 27.13 C ATOM 300 NE ARG A 40 25.104 78.716 34.269 1.00 27.40 N ATOM 301 CZ ARG A 40 24.803 78.791 32.975 1.00 25.78 C ATOM 302 NH1 ARG A 40 23.715 79.430 32.563 1.00 24.62 N ATOM 303 NH2 ARG A 40 25.543 78.118 32.100 1.00 23.53 N ATOM 304 N MET A 41 24.775 81.679 40.510 1.00 25.31 N ATOM 305 CA MET A 41 24.197 82.388 41.649 1.00 24.79 C ATOM 306 C MET A 41 25.094 83.495 42.160 1.00 25.18 C ATOM 307 O MET A 41 24.689 84.331 42.957 1.00 25.42 O ATOM 308 CB MET A 41 23.941 81.423 42.794 1.00 23.25 C ATOM 309 CG MET A 41 22.802 80.475 42.470 1.00 26.37 C ATOM 310 SD MET A 41 22.904 78.973 43.501 1.00 30.87 S ATOM 311 CE MET A 41 22.467 79.756 45.013 1.00 26.91 C ATOM 312 N GLN A 42 26.343 83.451 41.737 1.00 26.53 N ATOM 313 CA GLN A 42 27.366 84.382 42.145 1.00 31.02 C ATOM 314 C GLN A 42 27.618 84.334 43.637 1.00 32.09 C ATOM 315 O GLN A 42 27.889 85.346 44.291 1.00 32.25 O ATOM 316 CB GLN A 42 26.996 85.793 41.757 1.00 33.82 C ATOM 317 CG GLN A 42 26.812 85.904 40.277 1.00 39.78 C ATOM 318 CD GLN A 42 26.060 87.187 40.064 1.00 46.97 C ATOM 319 OE1 GLN A 42 24.826 87.239 40.027 1.00 50.83 O ATOM 320 NE2 GLN A 42 26.852 88.264 40.060 1.00 48.94 N ATOM 321 N VAL A 43 27.593 83.099 44.166 1.00 30.80 N ATOM 322 CA VAL A 43 27.932 82.839 45.573 1.00 27.55 C ATOM 323 C VAL A 43 29.195 81.989 45.600 1.00 26.63 C ATOM 324 O VAL A 43 29.573 81.372 44.599 1.00 25.88 O ATOM 325 CB VAL A 43 26.844 82.049 46.340 1.00 26.16 C ATOM 326 CG1 VAL A 43 25.619 82.921 46.482 1.00 27.57 C ATOM 327 CG2 VAL A 43 26.480 80.752 45.611 1.00 25.00 C ATOM 328 N LYS A 44 29.895 81.937 46.714 1.00 26.62 N ATOM 329 CA LYS A 44 31.004 81.025 46.871 1.00 27.88 C ATOM 330 C LYS A 44 30.438 79.747 47.513 1.00 24.71 C ATOM 331 O LYS A 44 29.543 79.849 48.339 1.00 22.37 O ATOM 332 CB LYS A 44 32.040 81.669 47.765 1.00 33.21 C ATOM 333 CG LYS A 44 32.740 82.834 47.097 1.00 41.49 C ATOM 334 CD LYS A 44 33.570 82.271 45.947 1.00 51.18 C ATOM 335 CE LYS A 44 34.670 83.252 45.502 1.00 59.29 C ATOM 336 NZ LYS A 44 34.265 84.063 44.359 1.00 65.84 N ATOM 337 N CYS A 45 30.894 78.540 47.209 1.00 24.02 N ATOM 338 CA CYS A 45 30.320 77.335 47.783 1.00 22.79 C ATOM 339 C CYS A 45 31.423 76.481 48.335 1.00 22.72 C ATOM 340 O CYS A 45 32.483 76.423 47.711 1.00 24.28 O ATOM 341 CB CYS A 45 29.569 76.537 46.723 1.00 19.92 C ATOM 342 SG CYS A 45 28.059 77.354 46.244 1.00 18.17 S ATOM 343 N THR A 46 31.233 75.869 49.489 1.00 19.83 N ATOM 344 CA THR A 46 32.219 74.971 50.048 1.00 21.40 C ATOM 345 C THR A 46 31.590 73.585 50.026 1.00 18.18 C ATOM 346 O THR A 46 30.419 73.484 50.386 1.00 17.31 O ATOM 347 CB THR A 46 32.529 75.375 51.498 1.00 23.78 C ATOM 348 OG1 THR A 46 33.132 76.652 51.367 1.00 32.02 O ATOM 349 CG2 THR A 46 33.411 74.395 52.264 1.00 23.29 C ATOM 350 N TRP A 47 32.293 72.536 49.629 1.00 17.40 N ATOM 351 CA TRP A 47 31.754 71.184 49.673 1.00 17.03 C ATOM 352 C TRP A 47 32.198 70.539 50.983 1.00 15.97 C ATOM 353 O TRP A 47 33.348 70.691 51.382 1.00 14.61 O ATOM 354 CB TRP A 47 32.265 70.358 48.478 1.00 14.83 C ATOM 355 CG TRP A 47 31.567 70.782 47.192 1.00 17.19 C ATOM 356 CD1 TRP A 47 32.109 71.760 46.406 1.00 17.78 C ATOM 357 CD2 TRP A 47 30.363 70.304 46.696 1.00 16.73 C ATOM 358 NE1 TRP A 47 31.242 71.905 45.424 1.00 19.21 N ATOM 359 CE2 TRP A 47 30.201 71.067 45.546 1.00 17.26 C ATOM 360 CE3 TRP A 47 29.404 69.356 47.026 1.00 16.33 C ATOM 361 CZ2 TRP A 47 29.105 70.906 44.721 1.00 16.75 C ATOM 362 CZ3 TRP A 47 28.307 69.184 46.194 1.00 15.15 C ATOM 363 CH2 TRP A 47 28.151 69.955 45.053 1.00 14.86 C ATOM 364 N VAL A 48 31.301 69.807 51.637 1.00 14.31 N ATOM 365 CA VAL A 48 31.547 69.172 52.918 1.00 14.88 C ATOM 366 C VAL A 48 31.165 67.707 52.762 1.00 15.08 C ATOM 367 O VAL A 48 30.000 67.424 52.478 1.00 15.26 O ATOM 368 CB VAL A 48 30.674 69.839 54.024 1.00 15.88 C ATOM 369 CG1 VAL A 48 30.903 69.134 55.351 1.00 16.37 C ATOM 370 CG2 VAL A 48 31.031 71.326 54.172 1.00 16.08 C ATOM 371 N ALA A 49 32.076 66.754 52.960 1.00 15.33 N ATOM 372 CA ALA A 49 31.780 65.334 52.805 1.00 15.13 C ATOM 373 C ALA A 49 31.131 64.845 54.083 1.00 16.05 C ATOM 374 O ALA A 49 31.460 65.309 55.177 1.00 18.52 O ATOM 375 CB ALA A 49 33.060 64.570 52.557 1.00 12.90 C ATOM 376 N SER A 50 30.159 63.965 53.988 1.00 15.69 N ATOM 377 CA SER A 50 29.440 63.431 55.122 1.00 16.86 C ATOM 378 C SER A 50 28.949 62.035 54.757 1.00 17.31 C ATOM 379 O SER A 50 28.798 61.690 53.576 1.00 16.17 O ATOM 380 CB SER A 50 28.287 64.372 55.370 1.00 17.53 C ATOM 381 OG SER A 50 27.241 63.883 56.180 1.00 22.56 O ATOM 382 N ASP A 51 28.760 61.156 55.734 1.00 16.78 N ATOM 383 CA ASP A 51 27.989 59.943 55.490 1.00 16.59 C ATOM 384 C ASP A 51 26.586 60.328 55.053 1.00 14.40 C ATOM 385 O ASP A 51 26.063 61.326 55.564 1.00 12.36 O ATOM 386 CB ASP A 51 27.878 59.113 56.754 1.00 21.14 C ATOM 387 CG ASP A 51 29.142 58.347 57.092 1.00 25.80 C ATOM 388 OD1 ASP A 51 30.075 58.292 56.292 1.00 29.48 O ATOM 389 OD2 ASP A 51 29.171 57.769 58.167 1.00 33.02 O ATOM 390 N PHE A 52 25.972 59.586 54.129 1.00 11.75 N ATOM 391 CA PHE A 52 24.643 59.891 53.654 1.00 11.91 C ATOM 392 C PHE A 52 23.585 60.092 54.745 1.00 13.27 C ATOM 393 O PHE A 52 22.807 61.040 54.670 1.00 13.67 O ATOM 394 CB PHE A 52 24.175 58.787 52.717 1.00 10.43 C ATOM 395 CG PHE A 52 22.891 59.185 51.981 1.00 12.51 C ATOM 396 CD1 PHE A 52 22.945 60.147 50.971 1.00 12.50 C ATOM 397 CD2 PHE A 52 21.675 58.617 52.323 1.00 13.44 C ATOM 398 CE1 PHE A 52 21.795 60.517 50.312 1.00 10.54 C ATOM 399 CE2 PHE A 52 20.526 59.002 51.650 1.00 11.93 C ATOM 400 CZ PHE A 52 20.588 59.935 50.637 1.00 11.81 C ATOM 401 N ASP A 53 23.528 59.261 55.800 1.00 13.50 N ATOM 402 CA ASP A 53 22.498 59.405 56.809 1.00 15.60 C ATOM 403 C ASP A 53 22.722 60.587 57.742 1.00 13.46 C ATOM 404 O ASP A 53 21.829 60.910 58.519 1.00 15.74 O ATOM 405 CB ASP A 53 22.368 58.113 57.657 1.00 18.02 C ATOM 406 CG ASP A 53 23.500 57.786 58.623 1.00 26.91 C ATOM 407 OD1 ASP A 53 24.639 58.281 58.472 1.00 27.66 O ATOM 408 OD2 ASP A 53 23.211 57.007 59.542 1.00 31.85 O ATOM 409 N ALA A 54 23.875 61.237 57.694 1.00 12.65 N ATOM 410 CA ALA A 54 24.105 62.422 58.501 1.00 11.97 C ATOM 411 C ALA A 54 23.709 63.687 57.736 1.00 14.10 C ATOM 412 O ALA A 54 23.638 64.774 58.339 1.00 14.80 O ATOM 413 CB ALA A 54 25.556 62.510 58.828 1.00 12.54 C ATOM 414 N LEU A 55 23.370 63.611 56.439 1.00 11.96 N ATOM 415 CA LEU A 55 23.158 64.823 55.659 1.00 13.03 C ATOM 416 C LEU A 55 21.933 65.638 56.029 1.00 13.06 C ATOM 417 O LEU A 55 22.025 66.849 56.308 1.00 13.09 O ATOM 418 CB LEU A 55 23.121 64.438 54.184 1.00 12.35 C ATOM 419 CG LEU A 55 24.459 64.006 53.531 1.00 13.62 C ATOM 420 CD1 LEU A 55 24.128 63.477 52.167 1.00 14.16 C ATOM 421 CD2 LEU A 55 25.457 65.148 53.364 1.00 14.50 C ATOM 422 N ILE A 56 20.757 65.033 56.105 1.00 13.62 N ATOM 423 CA ILE A 56 19.595 65.811 56.494 1.00 14.39 C ATOM 424 C ILE A 56 19.693 66.289 57.959 1.00 15.09 C ATOM 425 O ILE A 56 19.333 67.447 58.159 1.00 13.54 O ATOM 426 CB ILE A 56 18.338 64.935 56.207 1.00 14.71 C ATOM 427 CG1 ILE A 56 18.150 64.827 54.685 1.00 12.35 C ATOM 428 CG2 ILE A 56 17.095 65.524 56.883 1.00 15.43 C ATOM 429 CD1 ILE A 56 16.983 63.926 54.312 1.00 15.81 C ATOM 430 N PRO A 57 20.164 65.542 59.001 1.00 15.70 N ATOM 431 CA PRO A 57 20.490 66.081 60.317 1.00 15.52 C ATOM 432 C PRO A 57 21.407 67.304 60.274 1.00 14.94 C ATOM 433 O PRO A 57 21.138 68.329 60.913 1.00 15.42 O ATOM 434 CB PRO A 57 21.106 64.893 61.062 1.00 16.18 C ATOM 435 CG PRO A 57 20.410 63.689 60.470 1.00 16.97 C ATOM 436 CD PRO A 57 20.376 64.077 58.999 1.00 16.45 C ATOM 437 N SER A 58 22.511 67.227 59.532 1.00 13.91 N ATOM 438 CA SER A 58 23.414 68.361 59.416 1.00 15.77 C ATOM 439 C SER A 58 22.770 69.597 58.819 1.00 15.91 C ATOM 440 O SER A 58 23.083 70.731 59.250 1.00 17.45 O ATOM 441 CB SER A 58 24.613 68.022 58.558 1.00 15.80 C ATOM 442 OG SER A 58 25.269 67.076 59.351 1.00 21.33 O ATOM 443 N LEU A 59 21.925 69.387 57.811 1.00 13.16 N ATOM 444 CA LEU A 59 21.181 70.483 57.201 1.00 15.01 C ATOM 445 C LEU A 59 20.243 71.160 58.222 1.00 16.11 C ATOM 446 O LEU A 59 20.183 72.394 58.364 1.00 14.31 O ATOM 447 CB LEU A 59 20.331 69.972 55.981 1.00 13.82 C ATOM 448 CG LEU A 59 19.487 71.009 55.208 1.00 12.85 C ATOM 449 CD1 LEU A 59 20.420 71.977 54.535 1.00 13.12 C ATOM 450 CD2 LEU A 59 18.657 70.370 54.147 1.00 14.39 C ATOM 451 N LYS A 60 19.481 70.317 58.936 1.00 15.56 N ATOM 452 CA LYS A 60 18.550 70.823 59.897 1.00 17.39 C ATOM 453 C LYS A 60 19.284 71.552 61.026 1.00 18.98 C ATOM 454 O LYS A 60 18.773 72.547 61.542 1.00 21.08 O ATOM 455 CB LYS A 60 17.716 69.643 60.411 1.00 19.24 C ATOM 456 CG LYS A 60 16.648 69.333 59.390 1.00 22.28 C ATOM 457 CD LYS A 60 15.553 68.507 60.008 1.00 27.40 C ATOM 458 CE LYS A 60 16.008 67.108 60.068 1.00 32.24 C ATOM 459 NZ LYS A 60 15.196 66.376 61.019 1.00 38.72 N ATOM 460 N ALA A 61 20.478 71.113 61.401 1.00 16.99 N ATOM 461 CA ALA A 61 21.269 71.769 62.409 1.00 17.96 C ATOM 462 C ALA A 61 22.079 72.959 61.877 1.00 19.24 C ATOM 463 O ALA A 61 22.820 73.568 62.645 1.00 20.79 O ATOM 464 CB ALA A 61 22.206 70.721 63.028 1.00 17.91 C ATOM 465 N LYS A 62 21.984 73.336 60.597 1.00 17.16 N ATOM 466 CA LYS A 62 22.711 74.422 59.944 1.00 18.01 C ATOM 467 C LYS A 62 24.212 74.229 59.890 1.00 18.23 C ATOM 468 O LYS A 62 24.982 75.182 59.760 1.00 18.78 O ATOM 469 CB LYS A 62 22.414 75.809 60.599 1.00 18.97 C ATOM 470 CG LYS A 62 20.913 76.097 60.573 1.00 25.11 C ATOM 471 CD LYS A 62 20.409 77.452 61.052 1.00 30.04 C ATOM 472 CE LYS A 62 20.613 78.455 59.916 1.00 39.70 C ATOM 473 NZ LYS A 62 19.623 79.536 59.905 1.00 43.23 N ATOM 474 N LYS A 63 24.693 72.978 59.911 1.00 16.97 N ATOM 475 CA LYS A 63 26.120 72.720 59.713 1.00 16.78 C ATOM 476 C LYS A 63 26.488 72.809 58.225 1.00 15.68 C ATOM 477 O LYS A 63 27.666 72.964 57.867 1.00 14.77 O ATOM 478 CB LYS A 63 26.504 71.338 60.209 1.00 18.36 C ATOM 479 CG LYS A 63 26.247 71.151 61.696 1.00 22.51 C ATOM 480 CD LYS A 63 26.838 69.793 61.969 1.00 30.66 C ATOM 481 CE LYS A 63 26.525 69.243 63.353 1.00 36.40 C ATOM 482 NZ LYS A 63 27.089 67.894 63.462 1.00 41.53 N ATOM 483 N ILE A 64 25.467 72.647 57.356 1.00 14.72 N ATOM 484 CA ILE A 64 25.567 72.837 55.900 1.00 14.73 C ATOM 485 C ILE A 64 24.283 73.561 55.508 1.00 12.01 C ATOM 486 O ILE A 64 23.317 73.571 56.276 1.00 13.21 O ATOM 487 CB ILE A 64 25.645 71.496 55.068 1.00 14.76 C ATOM 488 CG1 ILE A 64 24.435 70.561 55.372 1.00 14.94 C ATOM 489 CG2 ILE A 64 27.065 70.936 55.286 1.00 12.39 C ATOM 490 CD1 ILE A 64 24.455 69.211 54.607 1.00 14.75 C ATOM 491 N ASP A 65 24.284 74.149 54.322 1.00 12.00 N ATOM 492 CA ASP A 65 23.167 74.917 53.827 1.00 12.56 C ATOM 493 C ASP A 65 22.400 74.219 52.738 1.00 13.45 C ATOM 494 O ASP A 65 21.265 74.609 52.463 1.00 14.51 O ATOM 495 CB ASP A 65 23.642 76.262 53.275 1.00 13.07 C ATOM 496 CG ASP A 65 24.409 77.002 54.358 1.00 15.79 C ATOM 497 OD1 ASP A 65 23.862 77.210 55.444 1.00 17.13 O ATOM 498 OD2 ASP A 65 25.581 77.287 54.152 1.00 15.13 O ATOM 499 N ALA A 66 22.989 73.235 52.068 1.00 11.59 N ATOM 500 CA ALA A 66 22.286 72.545 50.996 1.00 12.81 C ATOM 501 C ALA A 66 22.850 71.120 50.866 1.00 13.10 C ATOM 502 O ALA A 66 23.980 70.848 51.330 1.00 14.16 O ATOM 503 CB ALA A 66 22.487 73.313 49.691 1.00 13.49 C ATOM 504 N ILE A 67 22.070 70.210 50.291 1.00 10.64 N ATOM 505 CA ILE A 67 22.524 68.847 50.071 1.00 10.12 C ATOM 506 C ILE A 67 22.454 68.587 48.578 1.00 10.30 C ATOM 507 O ILE A 67 21.354 68.727 47.995 1.00 10.12 O ATOM 508 CB ILE A 67 21.604 67.792 50.785 1.00 9.37 C ATOM 509 CG1 ILE A 67 21.586 68.012 52.311 1.00 10.67 C ATOM 510 CG2 ILE A 67 22.084 66.360 50.400 1.00 9.02 C ATOM 511 CD1 ILE A 67 20.432 67.252 53.015 1.00 9.32 C ATOM 512 N ILE A 68 23.576 68.161 47.971 1.00 10.81 N ATOM 513 CA ILE A 68 23.506 67.659 46.593 1.00 11.87 C ATOM 514 C ILE A 68 24.241 66.326 46.672 1.00 10.47 C ATOM 515 O ILE A 68 25.461 66.259 46.763 1.00 10.15 O ATOM 516 CB ILE A 68 24.184 68.638 45.563 1.00 11.92 C ATOM 517 CG1 ILE A 68 23.506 70.028 45.653 1.00 11.08 C ATOM 518 CG2 ILE A 68 24.072 68.064 44.138 1.00 10.78 C ATOM 519 CD1 ILE A 68 24.188 71.140 44.837 1.00 14.98 C ATOM 520 N SER A 69 23.460 65.253 46.639 1.00 11.42 N ATOM 521 CA SER A 69 24.009 63.932 46.895 1.00 11.66 C ATOM 522 C SER A 69 23.054 62.867 46.370 1.00 12.07 C ATOM 523 O SER A 69 22.723 61.908 47.071 1.00 10.65 O ATOM 524 CB SER A 69 24.222 63.846 48.444 1.00 12.65 C ATOM 525 OG SER A 69 25.137 62.853 48.894 1.00 13.89 O ATOM 526 N SER A 70 22.558 63.008 45.133 1.00 10.07 N ATOM 527 CA SER A 70 21.556 62.113 44.558 1.00 12.14 C ATOM 528 C SER A 70 20.362 61.928 45.508 1.00 12.36 C ATOM 529 O SER A 70 19.782 60.836 45.626 1.00 11.84 O ATOM 530 CB SER A 70 22.183 60.726 44.214 1.00 12.46 C ATOM 531 OG SER A 70 23.299 60.840 43.325 1.00 16.60 O ATOM 532 N LEU A 71 19.951 63.048 46.148 1.00 10.78 N ATOM 533 CA LEU A 71 18.890 63.012 47.149 1.00 11.72 C ATOM 534 C LEU A 71 17.515 63.002 46.516 1.00 9.81 C ATOM 535 O LEU A 71 17.080 64.015 45.986 1.00 10.65 O ATOM 536 CB LEU A 71 19.023 64.219 48.105 1.00 10.85 C ATOM 537 CG LEU A 71 18.148 64.209 49.365 1.00 11.56 C ATOM 538 CD1 LEU A 71 18.684 63.122 50.333 1.00 11.36 C ATOM 539 CD2 LEU A 71 18.162 65.612 50.032 1.00 12.46 C ATOM 540 N SER A 72 16.839 61.851 46.514 1.00 10.28 N ATOM 541 CA SER A 72 15.519 61.730 45.923 1.00 12.45 C ATOM 542 C SER A 72 14.474 62.576 46.635 1.00 11.94 C ATOM 543 O SER A 72 14.468 62.651 47.860 1.00 10.16 O ATOM 544 CB SER A 72 15.082 60.277 45.947 1.00 12.88 C ATOM 545 OG SER A 72 15.887 59.533 45.035 1.00 11.68 O ATOM 546 N ILE A 73 13.597 63.190 45.837 1.00 11.01 N ATOM 547 CA ILE A 73 12.506 64.043 46.276 1.00 12.13 C ATOM 548 C ILE A 73 11.355 63.111 46.595 1.00 12.81 C ATOM 549 O ILE A 73 10.724 62.535 45.694 1.00 13.61 O ATOM 550 CB ILE A 73 12.086 65.045 45.140 1.00 13.77 C ATOM 551 CG1 ILE A 73 13.307 65.812 44.655 1.00 13.02 C ATOM 552 CG2 ILE A 73 10.977 65.994 45.666 1.00 14.07 C ATOM 553 CD1 ILE A 73 12.991 66.632 43.386 1.00 16.78 C ATOM 554 N THR A 74 11.093 62.887 47.881 1.00 13.53 N ATOM 555 CA THR A 74 10.014 61.970 48.266 1.00 15.54 C ATOM 556 C THR A 74 9.028 62.734 49.126 1.00 15.11 C ATOM 557 O THR A 74 9.398 63.711 49.798 1.00 15.36 O ATOM 558 CB THR A 74 10.543 60.762 49.091 1.00 13.59 C ATOM 559 OG1 THR A 74 11.051 61.291 50.317 1.00 13.52 O ATOM 560 CG2 THR A 74 11.612 59.984 48.367 1.00 11.79 C ATOM 561 N ASP A 75 7.842 62.162 49.224 1.00 16.67 N ATOM 562 CA ASP A 75 6.796 62.703 50.066 1.00 18.44 C ATOM 563 C ASP A 75 7.280 62.782 51.514 1.00 19.54 C ATOM 564 O ASP A 75 7.120 63.818 52.164 1.00 17.68 O ATOM 565 CB ASP A 75 5.598 61.794 49.912 1.00 21.06 C ATOM 566 CG ASP A 75 4.334 62.216 50.649 1.00 28.60 C ATOM 567 OD1 ASP A 75 4.289 63.288 51.267 1.00 30.78 O ATOM 568 OD2 ASP A 75 3.358 61.459 50.578 1.00 35.52 O ATOM 569 N LYS A 76 7.900 61.736 52.064 1.00 19.47 N ATOM 570 CA LYS A 76 8.415 61.780 53.425 1.00 22.01 C ATOM 571 C LYS A 76 9.437 62.873 53.714 1.00 21.79 C ATOM 572 O LYS A 76 9.328 63.635 54.695 1.00 22.62 O ATOM 573 CB LYS A 76 9.049 60.465 53.762 1.00 27.58 C ATOM 574 CG LYS A 76 8.143 59.616 54.576 1.00 37.96 C ATOM 575 CD LYS A 76 9.047 58.558 55.189 1.00 48.05 C ATOM 576 CE LYS A 76 9.989 59.184 56.239 1.00 53.49 C ATOM 577 NZ LYS A 76 10.971 58.203 56.679 1.00 58.64 N ATOM 578 N ARG A 77 10.450 62.971 52.851 1.00 17.49 N ATOM 579 CA ARG A 77 11.429 64.031 53.007 1.00 17.00 C ATOM 580 C ARG A 77 10.864 65.452 52.888 1.00 17.05 C ATOM 581 O ARG A 77 11.345 66.352 53.582 1.00 15.65 O ATOM 582 CB ARG A 77 12.552 63.817 51.981 1.00 14.21 C ATOM 583 CG ARG A 77 13.464 62.697 52.432 1.00 11.45 C ATOM 584 CD ARG A 77 14.380 62.319 51.307 1.00 11.85 C ATOM 585 NE ARG A 77 15.257 61.247 51.724 1.00 11.69 N ATOM 586 CZ ARG A 77 15.997 60.551 50.867 1.00 12.42 C ATOM 587 NH1 ARG A 77 15.956 60.832 49.554 1.00 9.27 N ATOM 588 NH2 ARG A 77 16.797 59.583 51.343 1.00 11.16 N ATOM 589 N GLN A 78 9.827 65.691 52.067 1.00 18.27 N ATOM 590 CA GLN A 78 9.199 67.012 51.945 1.00 21.55 C ATOM 591 C GLN A 78 8.475 67.422 53.213 1.00 22.52 C ATOM 592 O GLN A 78 8.162 68.588 53.394 1.00 23.69 O ATOM 593 CB GLN A 78 8.187 67.051 50.836 1.00 24.03 C ATOM 594 CG GLN A 78 8.922 66.809 49.553 1.00 32.00 C ATOM 595 CD GLN A 78 8.559 67.787 48.467 1.00 36.19 C ATOM 596 OE1 GLN A 78 8.151 67.427 47.374 1.00 37.11 O ATOM 597 NE2 GLN A 78 8.759 69.075 48.662 1.00 39.70 N ATOM 598 N GLN A 79 8.185 66.506 54.129 1.00 22.41 N ATOM 599 CA GLN A 79 7.604 66.888 55.392 1.00 23.83 C ATOM 600 C GLN A 79 8.681 67.558 56.215 1.00 23.58 C ATOM 601 O GLN A 79 8.361 68.346 57.102 1.00 23.97 O ATOM 602 CB GLN A 79 7.079 65.670 56.156 1.00 26.90 C ATOM 603 CG GLN A 79 6.010 64.882 55.387 1.00 36.88 C ATOM 604 CD GLN A 79 5.088 65.761 54.521 1.00 43.88 C ATOM 605 OE1 GLN A 79 4.358 66.638 55.013 1.00 49.04 O ATOM 606 NE2 GLN A 79 5.099 65.621 53.189 1.00 44.00 N ATOM 607 N GLU A 80 9.950 67.259 55.963 1.00 21.03 N ATOM 608 CA GLU A 80 11.026 67.779 56.756 1.00 21.77 C ATOM 609 C GLU A 80 11.855 68.876 56.121 1.00 19.91 C ATOM 610 O GLU A 80 12.323 69.769 56.837 1.00 18.77 O ATOM 611 CB GLU A 80 12.025 66.744 57.095 1.00 27.88 C ATOM 612 CG GLU A 80 11.593 65.406 57.595 1.00 38.59 C ATOM 613 CD GLU A 80 12.837 64.602 57.771 1.00 45.72 C ATOM 614 OE1 GLU A 80 13.284 63.953 56.833 1.00 49.20 O ATOM 615 OE2 GLU A 80 13.394 64.675 58.847 1.00 47.06 O ATOM 616 N ILE A 81 12.135 68.769 54.823 1.00 17.02 N ATOM 617 CA ILE A 81 13.007 69.720 54.149 1.00 15.91 C ATOM 618 C ILE A 81 12.296 70.162 52.874 1.00 15.51 C ATOM 619 O ILE A 81 11.202 69.691 52.568 1.00 16.35 O ATOM 620 CB ILE A 81 14.442 69.099 53.785 1.00 16.52 C ATOM 621 CG1 ILE A 81 14.357 67.883 52.847 1.00 14.80 C ATOM 622 CG2 ILE A 81 15.138 68.710 55.109 1.00 16.41 C ATOM 623 CD1 ILE A 81 15.747 67.483 52.336 1.00 15.73 C ATOM 624 N ALA A 82 12.920 71.093 52.152 1.00 15.01 N ATOM 625 CA ALA A 82 12.446 71.615 50.895 1.00 13.88 C ATOM 626 C ALA A 82 13.429 71.139 49.814 1.00 14.63 C ATOM 627 O ALA A 82 14.595 70.807 50.115 1.00 14.84 O ATOM 628 CB ALA A 82 12.455 73.134 50.921 1.00 14.82 C ATOM 629 N PHE A 83 12.995 71.129 48.548 1.00 13.33 N ATOM 630 CA PHE A 83 13.856 70.719 47.451 1.00 12.95 C ATOM 631 C PHE A 83 13.861 71.720 46.328 1.00 13.68 C ATOM 632 O PHE A 83 12.854 72.375 46.092 1.00 14.28 O ATOM 633 CB PHE A 83 13.416 69.407 46.834 1.00 13.69 C ATOM 634 CG PHE A 83 13.663 68.176 47.703 1.00 15.18 C ATOM 635 CD1 PHE A 83 12.691 67.753 48.620 1.00 17.22 C ATOM 636 CD2 PHE A 83 14.854 67.472 47.567 1.00 14.91 C ATOM 637 CE1 PHE A 83 12.908 66.622 49.401 1.00 14.34 C ATOM 638 CE2 PHE A 83 15.045 66.335 48.359 1.00 13.86 C ATOM 639 CZ PHE A 83 14.084 65.919 49.256 1.00 13.55 C ATOM 640 N SER A 84 14.981 71.893 45.644 1.00 13.64 N ATOM 641 CA SER A 84 14.960 72.575 44.350 1.00 15.86 C ATOM 642 C SER A 84 14.105 71.735 43.370 1.00 16.48 C ATOM 643 O SER A 84 13.671 70.614 43.672 1.00 16.01 O ATOM 644 CB SER A 84 16.385 72.675 43.748 1.00 14.81 C ATOM 645 OG SER A 84 16.880 71.380 43.371 1.00 13.32 O ATOM 646 N ASP A 85 13.914 72.220 42.149 1.00 16.87 N ATOM 647 CA ASP A 85 13.408 71.425 41.042 1.00 15.05 C ATOM 648 C ASP A 85 14.371 70.282 40.754 1.00 13.22 C ATOM 649 O ASP A 85 15.532 70.300 41.177 1.00 15.22 O ATOM 650 CB ASP A 85 13.294 72.284 39.781 1.00 18.93 C ATOM 651 CG ASP A 85 12.210 73.331 39.873 1.00 22.03 C ATOM 652 OD1 ASP A 85 11.168 73.109 40.483 1.00 23.33 O ATOM 653 OD2 ASP A 85 12.414 74.389 39.313 1.00 25.87 O ATOM 654 N LYS A 86 13.906 69.317 39.978 1.00 13.41 N ATOM 655 CA LYS A 86 14.638 68.105 39.675 1.00 12.09 C ATOM 656 C LYS A 86 15.969 68.332 38.993 1.00 11.81 C ATOM 657 O LYS A 86 16.026 69.022 37.983 1.00 14.01 O ATOM 658 CB LYS A 86 13.736 67.226 38.791 1.00 16.15 C ATOM 659 CG LYS A 86 14.355 65.900 38.432 1.00 18.69 C ATOM 660 CD LYS A 86 13.369 64.955 37.769 1.00 21.83 C ATOM 661 CE LYS A 86 13.414 65.061 36.275 1.00 27.12 C ATOM 662 NZ LYS A 86 12.579 64.047 35.639 1.00 31.73 N ATOM 663 N LEU A 87 17.032 67.726 39.486 1.00 10.98 N ATOM 664 CA LEU A 87 18.333 67.722 38.862 1.00 13.40 C ATOM 665 C LEU A 87 18.454 66.560 37.878 1.00 14.45 C ATOM 666 O LEU A 87 19.054 66.754 36.825 1.00 14.60 O ATOM 667 CB LEU A 87 19.431 67.603 39.922 1.00 13.59 C ATOM 668 CG LEU A 87 19.534 68.737 40.990 1.00 18.54 C ATOM 669 CD1 LEU A 87 20.711 68.557 41.963 1.00 15.61 C ATOM 670 CD2 LEU A 87 19.791 70.022 40.264 1.00 17.80 C ATOM 671 N TYR A 88 17.998 65.335 38.163 1.00 13.98 N ATOM 672 CA TYR A 88 18.009 64.216 37.217 1.00 12.75 C ATOM 673 C TYR A 88 17.128 63.102 37.798 1.00 14.78 C ATOM 674 O TYR A 88 16.745 63.160 38.978 1.00 12.59 O ATOM 675 CB TYR A 88 19.450 63.667 36.963 1.00 11.07 C ATOM 676 CG TYR A 88 20.339 63.422 38.173 1.00 13.10 C ATOM 677 CD1 TYR A 88 20.176 62.261 38.919 1.00 11.79 C ATOM 678 CD2 TYR A 88 21.233 64.404 38.573 1.00 11.91 C ATOM 679 CE1 TYR A 88 20.936 62.072 40.038 1.00 12.29 C ATOM 680 CE2 TYR A 88 21.996 64.213 39.696 1.00 11.32 C ATOM 681 CZ TYR A 88 21.853 63.035 40.406 1.00 13.59 C ATOM 682 OH TYR A 88 22.622 62.836 41.529 1.00 13.27 O ATOM 683 N ALA A 89 16.798 62.099 36.997 1.00 12.73 N ATOM 684 CA ALA A 89 15.915 61.020 37.414 1.00 12.74 C ATOM 685 C ALA A 89 16.739 59.973 38.152 1.00 13.92 C ATOM 686 O ALA A 89 17.981 59.921 37.983 1.00 14.89 O ATOM 687 CB ALA A 89 15.286 60.368 36.193 1.00 13.82 C ATOM 688 N ALA A 90 16.113 59.153 38.994 1.00 12.98 N ATOM 689 CA ALA A 90 16.857 58.127 39.672 1.00 14.38 C ATOM 690 C ALA A 90 15.927 56.963 39.971 1.00 17.27 C ATOM 691 O ALA A 90 14.994 57.114 40.785 1.00 21.19 O ATOM 692 CB ALA A 90 17.417 58.676 40.971 1.00 16.51 C ATOM 693 N ASP A 91 16.104 55.829 39.288 1.00 16.38 N ATOM 694 CA ASP A 91 15.370 54.601 39.599 1.00 17.34 C ATOM 695 C ASP A 91 16.224 53.657 40.402 1.00 14.04 C ATOM 696 O ASP A 91 17.445 53.817 40.387 1.00 14.62 O ATOM 697 CB ASP A 91 14.928 53.851 38.348 1.00 20.02 C ATOM 698 CG ASP A 91 13.778 54.594 37.696 1.00 27.36 C ATOM 699 OD1 ASP A 91 12.791 54.913 38.355 1.00 29.05 O ATOM 700 OD2 ASP A 91 13.885 54.889 36.516 1.00 32.83 O ATOM 701 N SER A 92 15.607 52.704 41.102 1.00 13.73 N ATOM 702 CA SER A 92 16.333 51.721 41.900 1.00 15.74 C ATOM 703 C SER A 92 16.404 50.375 41.183 1.00 15.48 C ATOM 704 O SER A 92 15.423 49.988 40.525 1.00 15.22 O ATOM 705 CB SER A 92 15.644 51.510 43.249 1.00 16.39 C ATOM 706 OG SER A 92 15.965 52.590 44.089 1.00 19.55 O ATOM 707 N ARG A 93 17.480 49.615 41.346 1.00 15.48 N ATOM 708 CA ARG A 93 17.554 48.312 40.687 1.00 16.06 C ATOM 709 C ARG A 93 18.504 47.415 41.472 1.00 14.26 C ATOM 710 O ARG A 93 19.489 47.915 42.062 1.00 15.45 O ATOM 711 CB ARG A 93 18.050 48.521 39.243 1.00 13.70 C ATOM 712 CG ARG A 93 17.781 47.300 38.341 1.00 14.80 C ATOM 713 CD ARG A 93 17.838 47.747 36.890 1.00 14.77 C ATOM 714 NE ARG A 93 17.674 46.598 36.019 1.00 17.33 N ATOM 715 CZ ARG A 93 17.890 46.647 34.697 1.00 19.60 C ATOM 716 NH1 ARG A 93 18.279 47.764 34.068 1.00 15.01 N ATOM 717 NH2 ARG A 93 17.716 45.515 34.006 1.00 19.41 N ATOM 718 N LEU A 94 18.222 46.107 41.528 1.00 13.91 N ATOM 719 CA LEU A 94 19.081 45.139 42.217 1.00 13.79 C ATOM 720 C LEU A 94 20.257 44.704 41.360 1.00 14.22 C ATOM 721 O LEU A 94 20.124 44.608 40.120 1.00 15.36 O ATOM 722 CB LEU A 94 18.359 43.857 42.556 1.00 15.68 C ATOM 723 CG LEU A 94 17.668 43.561 43.856 1.00 21.73 C ATOM 724 CD1 LEU A 94 17.294 42.099 43.788 1.00 19.84 C ATOM 725 CD2 LEU A 94 18.545 43.794 45.068 1.00 17.52 C ATOM 726 N ILE A 95 21.408 44.449 41.973 1.00 13.94 N ATOM 727 CA ILE A 95 22.542 43.875 41.271 1.00 16.67 C ATOM 728 C ILE A 95 22.928 42.598 42.017 1.00 20.15 C ATOM 729 O ILE A 95 22.734 42.519 43.238 1.00 19.44 O ATOM 730 CB ILE A 95 23.827 44.742 41.222 1.00 15.58 C ATOM 731 CG1 ILE A 95 24.347 45.136 42.567 1.00 13.02 C ATOM 732 CG2 ILE A 95 23.486 45.902 40.312 1.00 15.37 C ATOM 733 CD1 ILE A 95 25.611 45.998 42.492 1.00 16.40 C ATOM 734 N ALA A 96 23.447 41.594 41.297 1.00 19.82 N ATOM 735 CA ALA A 96 23.864 40.327 41.871 1.00 20.49 C ATOM 736 C ALA A 96 24.893 39.742 40.925 1.00 22.47 C ATOM 737 O ALA A 96 25.236 40.371 39.924 1.00 22.94 O ATOM 738 CB ALA A 96 22.682 39.367 41.968 1.00 20.54 C ATOM 739 N ALA A 97 25.471 38.589 41.246 1.00 23.09 N ATOM 740 CA ALA A 97 26.401 37.881 40.363 1.00 23.45 C ATOM 741 C ALA A 97 25.740 37.511 39.045 1.00 21.88 C ATOM 742 O ALA A 97 24.537 37.230 38.992 1.00 21.95 O ATOM 743 CB ALA A 97 26.890 36.591 41.011 1.00 23.62 C ATOM 744 N LYS A 98 26.520 37.578 37.971 1.00 25.07 N ATOM 745 CA LYS A 98 26.056 37.241 36.636 1.00 29.18 C ATOM 746 C LYS A 98 25.480 35.848 36.650 1.00 30.32 C ATOM 747 O LYS A 98 26.045 34.948 37.271 1.00 30.25 O ATOM 748 CB LYS A 98 27.199 37.261 35.660 1.00 34.17 C ATOM 749 CG LYS A 98 27.249 38.539 34.898 1.00 42.91 C ATOM 750 CD LYS A 98 28.506 38.555 34.065 1.00 48.45 C ATOM 751 CE LYS A 98 28.482 39.762 33.122 1.00 53.89 C ATOM 752 NZ LYS A 98 28.460 41.036 33.825 1.00 56.00 N ATOM 753 N GLY A 99 24.344 35.623 36.029 1.00 31.36 N ATOM 754 CA GLY A 99 23.804 34.280 36.062 1.00 35.05 C ATOM 755 C GLY A 99 22.978 33.982 37.291 1.00 37.36 C ATOM 756 O GLY A 99 22.328 32.930 37.357 1.00 39.51 O ATOM 757 N SER A 100 22.970 34.873 38.281 1.00 36.92 N ATOM 758 CA SER A 100 22.102 34.727 39.436 1.00 37.12 C ATOM 759 C SER A 100 20.631 34.578 39.031 1.00 35.00 C ATOM 760 O SER A 100 20.090 35.342 38.225 1.00 35.00 O ATOM 761 CB SER A 100 22.211 35.945 40.347 1.00 36.99 C ATOM 762 OG SER A 100 21.424 35.743 41.506 1.00 39.62 O ATOM 763 N PRO A 101 19.920 33.628 39.613 1.00 34.20 N ATOM 764 CA PRO A 101 18.474 33.552 39.529 1.00 35.26 C ATOM 765 C PRO A 101 17.745 34.657 40.288 1.00 36.30 C ATOM 766 O PRO A 101 16.527 34.780 40.105 1.00 38.00 O ATOM 767 CB PRO A 101 18.172 32.202 40.061 1.00 36.06 C ATOM 768 CG PRO A 101 19.232 32.098 41.140 1.00 36.24 C ATOM 769 CD PRO A 101 20.473 32.548 40.408 1.00 33.67 C ATOM 770 N ILE A 102 18.434 35.457 41.127 1.00 34.37 N ATOM 771 CA ILE A 102 17.791 36.473 41.946 1.00 31.46 C ATOM 772 C ILE A 102 16.972 37.477 41.131 1.00 30.10 C ATOM 773 O ILE A 102 17.324 37.973 40.062 1.00 28.16 O ATOM 774 CB ILE A 102 18.923 37.133 42.796 1.00 33.20 C ATOM 775 CG1 ILE A 102 19.302 36.165 43.918 1.00 32.21 C ATOM 776 CG2 ILE A 102 18.499 38.493 43.350 1.00 34.21 C ATOM 777 CD1 ILE A 102 20.494 36.636 44.772 1.00 31.44 C ATOM 778 N GLN A 103 15.786 37.693 41.653 1.00 29.15 N ATOM 779 CA GLN A 103 14.824 38.619 41.119 1.00 28.44 C ATOM 780 C GLN A 103 14.467 39.518 42.281 1.00 28.16 C ATOM 781 O GLN A 103 14.573 39.079 43.440 1.00 26.84 O ATOM 782 CB GLN A 103 13.584 37.876 40.646 1.00 30.01 C ATOM 783 CG GLN A 103 13.803 37.153 39.331 1.00 34.02 C ATOM 784 CD GLN A 103 14.153 38.117 38.209 1.00 37.55 C ATOM 785 OE1 GLN A 103 13.428 39.075 37.912 1.00 38.59 O ATOM 786 NE2 GLN A 103 15.303 37.902 37.588 1.00 39.19 N ATOM 787 N PRO A 104 13.999 40.751 42.082 1.00 27.32 N ATOM 788 CA PRO A 104 13.597 41.616 43.190 1.00 28.33 C ATOM 789 C PRO A 104 12.294 41.106 43.823 1.00 29.66 C ATOM 790 O PRO A 104 11.322 41.870 43.867 1.00 31.99 O ATOM 791 CB PRO A 104 13.517 42.999 42.527 1.00 27.69 C ATOM 792 CG PRO A 104 13.048 42.681 41.127 1.00 28.00 C ATOM 793 CD PRO A 104 13.863 41.424 40.791 1.00 25.98 C ATOM 794 N THR A 105 12.152 39.856 44.292 1.00 28.92 N ATOM 795 CA THR A 105 10.885 39.404 44.850 1.00 30.17 C ATOM 796 C THR A 105 11.194 38.724 46.162 1.00 29.27 C ATOM 797 O THR A 105 12.302 38.219 46.370 1.00 28.33 O ATOM 798 CB THR A 105 10.149 38.397 43.926 1.00 31.04 C ATOM 799 OG1 THR A 105 10.956 37.231 43.765 1.00 31.97 O ATOM 800 CG2 THR A 105 9.829 39.036 42.569 1.00 32.94 C ATOM 801 N LEU A 106 10.180 38.613 46.998 1.00 29.84 N ATOM 802 CA LEU A 106 10.348 38.085 48.329 1.00 31.10 C ATOM 803 C LEU A 106 10.741 36.633 48.258 1.00 32.05 C ATOM 804 O LEU A 106 11.660 36.174 48.941 1.00 34.35 O ATOM 805 CB LEU A 106 9.036 38.254 49.092 1.00 33.26 C ATOM 806 CG LEU A 106 8.972 37.908 50.567 1.00 34.33 C ATOM 807 CD1 LEU A 106 9.961 38.788 51.322 1.00 33.53 C ATOM 808 CD2 LEU A 106 7.549 38.098 51.062 1.00 32.40 C ATOM 809 N GLU A 107 10.100 35.953 47.336 1.00 33.53 N ATOM 810 CA GLU A 107 10.282 34.533 47.107 1.00 36.49 C ATOM 811 C GLU A 107 11.704 34.225 46.662 1.00 35.77 C ATOM 812 O GLU A 107 12.313 33.233 47.061 1.00 37.36 O ATOM 813 CB GLU A 107 9.294 34.003 46.044 1.00 41.40 C ATOM 814 CG GLU A 107 8.467 34.955 45.142 1.00 52.22 C ATOM 815 CD GLU A 107 7.584 35.951 45.902 1.00 56.78 C ATOM 816 OE1 GLU A 107 6.724 35.529 46.669 1.00 60.24 O ATOM 817 OE2 GLU A 107 7.832 37.158 45.801 1.00 60.57 O ATOM 818 N SER A 108 12.298 35.103 45.859 1.00 34.44 N ATOM 819 CA SER A 108 13.659 34.952 45.391 1.00 30.99 C ATOM 820 C SER A 108 14.684 35.299 46.468 1.00 28.95 C ATOM 821 O SER A 108 15.764 34.715 46.568 1.00 29.17 O ATOM 822 CB SER A 108 13.749 35.865 44.195 1.00 33.26 C ATOM 823 OG SER A 108 14.908 35.652 43.422 1.00 39.01 O ATOM 824 N LEU A 109 14.362 36.313 47.258 1.00 25.94 N ATOM 825 CA LEU A 109 15.299 36.875 48.196 1.00 23.82 C ATOM 826 C LEU A 109 15.203 36.335 49.598 1.00 24.87 C ATOM 827 O LEU A 109 16.103 36.634 50.397 1.00 23.18 O ATOM 828 CB LEU A 109 15.114 38.401 48.235 1.00 22.80 C ATOM 829 CG LEU A 109 15.460 39.206 46.987 1.00 21.63 C ATOM 830 CD1 LEU A 109 14.928 40.618 47.111 1.00 21.70 C ATOM 831 CD2 LEU A 109 16.969 39.176 46.795 1.00 21.85 C ATOM 832 N LYS A 110 14.130 35.627 49.983 1.00 26.76 N ATOM 833 CA LYS A 110 14.022 35.166 51.367 1.00 27.86 C ATOM 834 C LYS A 110 15.251 34.313 51.688 1.00 29.00 C ATOM 835 O LYS A 110 15.711 33.507 50.861 1.00 30.06 O ATOM 836 CB LYS A 110 12.738 34.359 51.537 1.00 29.94 C ATOM 837 N GLY A 111 15.870 34.628 52.837 1.00 28.34 N ATOM 838 CA GLY A 111 17.119 33.979 53.208 1.00 30.18 C ATOM 839 C GLY A 111 18.386 34.506 52.513 1.00 31.14 C ATOM 840 O GLY A 111 19.492 34.004 52.768 1.00 34.05 O ATOM 841 N LYS A 112 18.331 35.493 51.622 1.00 30.36 N ATOM 842 CA LYS A 112 19.525 36.035 50.987 1.00 28.08 C ATOM 843 C LYS A 112 20.007 37.230 51.815 1.00 24.88 C ATOM 844 O LYS A 112 19.281 37.749 52.669 1.00 24.82 O ATOM 845 CB LYS A 112 19.214 36.507 49.584 1.00 31.78 C ATOM 846 CG LYS A 112 18.724 35.440 48.630 1.00 38.72 C ATOM 847 CD LYS A 112 19.795 34.393 48.480 1.00 44.14 C ATOM 848 CE LYS A 112 19.375 33.381 47.428 1.00 48.51 C ATOM 849 NZ LYS A 112 20.417 32.374 47.283 1.00 51.23 N ATOM 850 N HIS A 113 21.217 37.727 51.577 1.00 21.53 N ATOM 851 CA HIS A 113 21.757 38.839 52.333 1.00 20.75 C ATOM 852 C HIS A 113 21.778 39.920 51.276 1.00 19.77 C ATOM 853 O HIS A 113 22.429 39.719 50.238 1.00 18.46 O ATOM 854 CB HIS A 113 23.171 38.587 52.792 1.00 22.94 C ATOM 855 CG HIS A 113 23.303 37.252 53.470 1.00 27.97 C ATOM 856 ND1 HIS A 113 22.749 36.841 54.598 1.00 28.32 N ATOM 857 CD2 HIS A 113 23.993 36.209 52.910 1.00 31.04 C ATOM 858 CE1 HIS A 113 23.066 35.580 54.729 1.00 31.51 C ATOM 859 NE2 HIS A 113 23.823 35.208 53.718 1.00 32.43 N ATOM 860 N VAL A 114 21.049 41.008 51.519 1.00 19.31 N ATOM 861 CA VAL A 114 20.891 42.133 50.592 1.00 18.24 C ATOM 862 C VAL A 114 21.419 43.404 51.273 1.00 17.31 C ATOM 863 O VAL A 114 20.998 43.744 52.391 1.00 16.61 O ATOM 864 CB VAL A 114 19.403 42.318 50.245 1.00 17.25 C ATOM 865 CG1 VAL A 114 19.244 43.523 49.311 1.00 16.03 C ATOM 866 CG2 VAL A 114 18.857 41.027 49.639 1.00 16.69 C ATOM 867 N GLY A 115 22.350 44.079 50.610 1.00 15.63 N ATOM 868 CA GLY A 115 22.928 45.299 51.164 1.00 15.70 C ATOM 869 C GLY A 115 22.184 46.541 50.675 1.00 16.13 C ATOM 870 O GLY A 115 21.767 46.603 49.499 1.00 14.82 O ATOM 871 N VAL A 116 22.022 47.528 51.577 1.00 14.94 N ATOM 872 CA VAL A 116 21.383 48.805 51.253 1.00 13.71 C ATOM 873 C VAL A 116 22.136 49.860 52.054 1.00 14.75 C ATOM 874 O VAL A 116 22.702 49.628 53.142 1.00 13.48 O ATOM 875 CB VAL A 116 19.844 48.890 51.652 1.00 14.30 C ATOM 876 CG1 VAL A 116 18.995 48.019 50.718 1.00 13.67 C ATOM 877 CG2 VAL A 116 19.663 48.481 53.133 1.00 11.62 C ATOM 878 N LEU A 117 22.160 51.070 51.499 1.00 13.89 N ATOM 879 CA LEU A 117 22.799 52.208 52.165 1.00 12.80 C ATOM 880 C LEU A 117 21.913 52.719 53.297 1.00 11.73 C ATOM 881 O LEU A 117 20.735 53.001 53.090 1.00 12.46 O ATOM 882 CB LEU A 117 23.049 53.324 51.117 1.00 12.14 C ATOM 883 CG LEU A 117 23.605 54.679 51.558 1.00 12.24 C ATOM 884 CD1 LEU A 117 24.995 54.528 52.152 1.00 10.04 C ATOM 885 CD2 LEU A 117 23.657 55.598 50.319 1.00 11.32 C ATOM 886 N GLN A 118 22.488 52.874 54.474 1.00 12.23 N ATOM 887 CA GLN A 118 21.783 53.432 55.619 1.00 15.68 C ATOM 888 C GLN A 118 21.344 54.887 55.306 1.00 14.78 C ATOM 889 O GLN A 118 22.109 55.779 54.879 1.00 15.49 O ATOM 890 CB GLN A 118 22.762 53.329 56.792 1.00 17.88 C ATOM 891 CG GLN A 118 22.419 53.608 58.250 1.00 29.24 C ATOM 892 CD GLN A 118 23.535 53.055 59.156 1.00 33.48 C ATOM 893 OE1 GLN A 118 24.746 53.335 59.050 1.00 37.01 O ATOM 894 NE2 GLN A 118 23.092 52.196 60.054 1.00 36.34 N ATOM 895 N GLY A 119 20.065 55.122 55.493 1.00 14.60 N ATOM 896 CA GLY A 119 19.479 56.436 55.347 1.00 14.17 C ATOM 897 C GLY A 119 18.836 56.598 53.986 1.00 15.08 C ATOM 898 O GLY A 119 18.167 57.616 53.783 1.00 13.84 O ATOM 899 N SER A 120 18.964 55.627 53.054 1.00 14.81 N ATOM 900 CA SER A 120 18.424 55.755 51.710 1.00 13.25 C ATOM 901 C SER A 120 16.974 55.346 51.582 1.00 12.24 C ATOM 902 O SER A 120 16.401 54.647 52.433 1.00 10.20 O ATOM 903 CB SER A 120 19.279 54.928 50.749 1.00 12.04 C ATOM 904 OG SER A 120 19.157 53.536 51.051 1.00 11.99 O ATOM 905 N THR A 121 16.371 55.725 50.464 1.00 10.97 N ATOM 906 CA THR A 121 15.021 55.284 50.134 1.00 11.94 C ATOM 907 C THR A 121 15.048 53.746 49.931 1.00 12.74 C ATOM 908 O THR A 121 14.078 53.065 50.256 1.00 11.85 O ATOM 909 CB THR A 121 14.547 55.953 48.858 1.00 13.02 C ATOM 910 OG1 THR A 121 15.542 55.654 47.892 1.00 13.93 O ATOM 911 CG2 THR A 121 14.376 57.464 48.984 1.00 12.92 C ATOM 912 N GLN A 122 16.164 53.172 49.439 1.00 12.16 N ATOM 913 CA GLN A 122 16.316 51.721 49.293 1.00 11.55 C ATOM 914 C GLN A 122 16.274 51.007 50.641 1.00 12.31 C ATOM 915 O GLN A 122 15.636 49.960 50.725 1.00 12.56 O ATOM 916 CB GLN A 122 17.641 51.381 48.615 1.00 12.22 C ATOM 917 CG GLN A 122 17.719 51.761 47.134 1.00 13.61 C ATOM 918 CD GLN A 122 18.195 53.186 46.864 1.00 17.16 C ATOM 919 OE1 GLN A 122 18.767 53.882 47.714 1.00 14.01 O ATOM 920 NE2 GLN A 122 17.980 53.639 45.647 1.00 15.39 N ATOM 921 N GLU A 123 16.867 51.587 51.699 1.00 11.94 N ATOM 922 CA GLU A 123 16.851 51.009 53.029 1.00 13.92 C ATOM 923 C GLU A 123 15.405 51.015 53.491 1.00 15.82 C ATOM 924 O GLU A 123 14.930 49.973 53.947 1.00 15.54 O ATOM 925 CB GLU A 123 17.659 51.825 54.004 1.00 14.05 C ATOM 926 CG GLU A 123 17.623 51.206 55.394 1.00 17.19 C ATOM 927 CD GLU A 123 18.211 52.081 56.468 1.00 18.73 C ATOM 928 OE1 GLU A 123 18.106 53.282 56.411 1.00 19.48 O ATOM 929 OE2 GLU A 123 18.802 51.568 57.382 1.00 22.75 O ATOM 930 N ALA A 124 14.651 52.114 53.306 1.00 15.72 N ATOM 931 CA ALA A 124 13.240 52.153 53.703 1.00 16.66 C ATOM 932 C ALA A 124 12.406 51.057 53.038 1.00 16.81 C ATOM 933 O ALA A 124 11.669 50.306 53.685 1.00 15.49 O ATOM 934 CB ALA A 124 12.614 53.493 53.328 1.00 17.04 C ATOM 935 N TYR A 125 12.565 50.925 51.713 1.00 16.70 N ATOM 936 CA TYR A 125 11.850 49.955 50.931 1.00 15.84 C ATOM 937 C TYR A 125 12.174 48.546 51.385 1.00 17.62 C ATOM 938 O TYR A 125 11.246 47.755 51.609 1.00 16.98 O ATOM 939 CB TYR A 125 12.221 50.118 49.474 1.00 17.57 C ATOM 940 CG TYR A 125 11.492 49.149 48.556 1.00 18.73 C ATOM 941 CD1 TYR A 125 10.229 49.481 48.108 1.00 21.69 C ATOM 942 CD2 TYR A 125 12.064 47.929 48.209 1.00 21.28 C ATOM 943 CE1 TYR A 125 9.520 48.600 47.317 1.00 21.29 C ATOM 944 CE2 TYR A 125 11.362 47.033 47.428 1.00 21.54 C ATOM 945 CZ TYR A 125 10.100 47.389 46.999 1.00 23.42 C ATOM 946 OH TYR A 125 9.393 46.508 46.234 1.00 25.79 O ATOM 947 N ALA A 126 13.465 48.220 51.477 1.00 16.28 N ATOM 948 CA ALA A 126 13.914 46.867 51.815 1.00 15.86 C ATOM 949 C ALA A 126 13.535 46.530 53.254 1.00 17.88 C ATOM 950 O ALA A 126 13.114 45.409 53.550 1.00 17.60 O ATOM 951 CB ALA A 126 15.429 46.760 51.659 1.00 13.67 C ATOM 952 N ASN A 127 13.584 47.480 54.192 1.00 18.64 N ATOM 953 CA ASN A 127 13.228 47.199 55.570 1.00 19.84 C ATOM 954 C ASN A 127 11.763 46.869 55.683 1.00 21.74 C ATOM 955 O ASN A 127 11.416 45.814 56.233 1.00 23.77 O ATOM 956 CB ASN A 127 13.525 48.374 56.475 1.00 19.02 C ATOM 957 CG ASN A 127 14.962 48.413 56.937 1.00 19.57 C ATOM 958 OD1 ASN A 127 15.363 49.317 57.645 1.00 25.04 O ATOM 959 ND2 ASN A 127 15.883 47.506 56.745 1.00 19.49 N ATOM 960 N ASP A 128 10.894 47.685 55.085 1.00 21.57 N ATOM 961 CA ASP A 128 9.462 47.410 55.168 1.00 21.82 C ATOM 962 C ASP A 128 9.039 46.140 54.433 1.00 22.87 C ATOM 963 O ASP A 128 8.348 45.286 55.000 1.00 23.68 O ATOM 964 CB ASP A 128 8.647 48.592 54.604 1.00 20.12 C ATOM 965 CG ASP A 128 8.786 49.867 55.384 1.00 24.66 C ATOM 966 OD1 ASP A 128 9.309 49.895 56.485 1.00 28.55 O ATOM 967 OD2 ASP A 128 8.374 50.883 54.902 1.00 26.01 O ATOM 968 N ASN A 129 9.544 45.976 53.210 1.00 20.90 N ATOM 969 CA ASN A 129 9.065 44.911 52.351 1.00 21.18 C ATOM 970 C ASN A 129 9.745 43.582 52.418 1.00 19.10 C ATOM 971 O ASN A 129 9.159 42.560 52.058 1.00 19.18 O ATOM 972 CB ASN A 129 9.099 45.360 50.895 1.00 21.98 C ATOM 973 CG ASN A 129 8.154 46.528 50.670 1.00 27.57 C ATOM 974 OD1 ASN A 129 6.949 46.339 50.658 1.00 31.51 O ATOM 975 ND2 ASN A 129 8.549 47.791 50.546 1.00 28.55 N ATOM 976 N TRP A 130 11.009 43.602 52.816 1.00 17.94 N ATOM 977 CA TRP A 130 11.821 42.414 52.753 1.00 17.44 C ATOM 978 C TRP A 130 12.323 42.004 54.124 1.00 19.98 C ATOM 979 O TRP A 130 12.173 40.823 54.479 1.00 20.55 O ATOM 980 CB TRP A 130 13.046 42.618 51.797 1.00 16.76 C ATOM 981 CG TRP A 130 12.731 42.849 50.309 1.00 18.85 C ATOM 982 CD1 TRP A 130 11.505 42.538 49.762 1.00 20.79 C ATOM 983 CD2 TRP A 130 13.589 43.390 49.364 1.00 18.32 C ATOM 984 NE1 TRP A 130 11.582 42.892 48.494 1.00 23.69 N ATOM 985 CE2 TRP A 130 12.798 43.388 48.214 1.00 20.70 C ATOM 986 CE3 TRP A 130 14.880 43.870 49.313 1.00 18.40 C ATOM 987 CZ2 TRP A 130 13.244 43.847 46.987 1.00 16.30 C ATOM 988 CZ3 TRP A 130 15.344 44.321 48.087 1.00 21.34 C ATOM 989 CH2 TRP A 130 14.528 44.327 46.956 1.00 19.28 C ATOM 990 N ARG A 131 12.889 42.905 54.936 1.00 18.42 N ATOM 991 CA ARG A 131 13.462 42.523 56.215 1.00 19.21 C ATOM 992 C ARG A 131 12.389 41.923 57.119 1.00 19.46 C ATOM 993 O ARG A 131 12.659 40.896 57.734 1.00 19.58 O ATOM 994 CB ARG A 131 14.090 43.734 56.898 1.00 19.53 C ATOM 995 CG ARG A 131 14.772 43.426 58.228 1.00 28.62 C ATOM 996 CD ARG A 131 15.296 44.713 58.910 1.00 34.05 C ATOM 997 NE ARG A 131 14.935 44.731 60.332 1.00 41.70 N ATOM 998 CZ ARG A 131 15.601 44.010 61.259 1.00 45.19 C ATOM 999 NH1 ARG A 131 16.648 43.245 60.916 1.00 46.77 N ATOM 1000 NH2 ARG A 131 15.176 43.968 62.530 1.00 46.36 N ATOM 1001 N THR A 132 11.161 42.449 57.131 1.00 18.11 N ATOM 1002 CA THR A 132 10.107 41.951 58.003 1.00 19.57 C ATOM 1003 C THR A 132 9.737 40.510 57.646 1.00 20.83 C ATOM 1004 O THR A 132 9.306 39.743 58.513 1.00 20.00 O ATOM 1005 CB THR A 132 8.848 42.832 57.880 1.00 19.44 C ATOM 1006 OG1 THR A 132 8.580 42.877 56.479 1.00 23.19 O ATOM 1007 CG2 THR A 132 9.017 44.256 58.413 1.00 22.74 C ATOM 1008 N LYS A 133 9.934 40.123 56.382 1.00 19.72 N ATOM 1009 CA LYS A 133 9.536 38.822 55.898 1.00 20.53 C ATOM 1010 C LYS A 133 10.691 37.849 55.853 1.00 21.74 C ATOM 1011 O LYS A 133 10.606 36.808 55.210 1.00 22.84 O ATOM 1012 CB LYS A 133 8.965 38.967 54.529 1.00 21.23 C ATOM 1013 CG LYS A 133 7.830 39.952 54.365 1.00 23.82 C ATOM 1014 CD LYS A 133 6.624 39.521 55.148 1.00 27.50 C ATOM 1015 CE LYS A 133 5.672 40.687 55.149 1.00 31.75 C ATOM 1016 NZ LYS A 133 4.407 40.232 55.679 1.00 39.10 N ATOM 1017 N GLY A 134 11.809 38.140 56.486 1.00 21.87 N ATOM 1018 CA GLY A 134 12.904 37.212 56.579 1.00 22.84 C ATOM 1019 C GLY A 134 14.001 37.353 55.545 1.00 22.89 C ATOM 1020 O GLY A 134 14.765 36.389 55.366 1.00 25.41 O ATOM 1021 N VAL A 135 14.103 38.440 54.794 1.00 20.53 N ATOM 1022 CA VAL A 135 15.261 38.605 53.919 1.00 17.46 C ATOM 1023 C VAL A 135 16.310 39.197 54.840 1.00 18.15 C ATOM 1024 O VAL A 135 15.950 40.031 55.672 1.00 19.12 O ATOM 1025 CB VAL A 135 14.968 39.591 52.791 1.00 18.26 C ATOM 1026 CG1 VAL A 135 16.203 39.823 51.897 1.00 17.09 C ATOM 1027 CG2 VAL A 135 13.783 39.035 52.019 1.00 16.92 C ATOM 1028 N ASP A 136 17.594 38.820 54.759 1.00 17.46 N ATOM 1029 CA ASP A 136 18.611 39.440 55.600 1.00 17.71 C ATOM 1030 C ASP A 136 19.062 40.769 54.968 1.00 16.70 C ATOM 1031 O ASP A 136 20.042 40.813 54.220 1.00 17.96 O ATOM 1032 CB ASP A 136 19.811 38.483 55.759 1.00 19.49 C ATOM 1033 CG ASP A 136 20.934 39.009 56.646 1.00 23.88 C ATOM 1034 OD1 ASP A 136 20.635 39.645 57.658 1.00 24.89 O ATOM 1035 OD2 ASP A 136 22.111 38.799 56.326 1.00 26.01 O ATOM 1036 N VAL A 137 18.398 41.859 55.314 1.00 14.35 N ATOM 1037 CA VAL A 137 18.718 43.175 54.772 1.00 15.33 C ATOM 1038 C VAL A 137 19.762 43.766 55.704 1.00 15.73 C ATOM 1039 O VAL A 137 19.490 43.925 56.897 1.00 17.81 O ATOM 1040 CB VAL A 137 17.429 44.074 54.729 1.00 15.55 C ATOM 1041 CG1 VAL A 137 17.824 45.493 54.291 1.00 18.06 C ATOM 1042 CG2 VAL A 137 16.407 43.548 53.739 1.00 13.38 C ATOM 1043 N VAL A 138 20.918 44.128 55.178 1.00 14.44 N ATOM 1044 CA VAL A 138 22.026 44.652 55.935 1.00 14.78 C ATOM 1045 C VAL A 138 22.225 46.116 55.547 1.00 15.19 C ATOM 1046 O VAL A 138 22.420 46.386 54.358 1.00 16.58 O ATOM 1047 CB VAL A 138 23.288 43.860 55.601 1.00 16.13 C ATOM 1048 CG1 VAL A 138 24.385 44.339 56.540 1.00 18.41 C ATOM 1049 CG2 VAL A 138 23.051 42.334 55.716 1.00 18.05 C ATOM 1050 N ALA A 139 22.223 47.064 56.495 1.00 15.67 N ATOM 1051 CA ALA A 139 22.393 48.491 56.213 1.00 15.40 C ATOM 1052 C ALA A 139 23.857 48.874 56.336 1.00 16.35 C ATOM 1053 O ALA A 139 24.540 48.452 57.278 1.00 18.29 O ATOM 1054 CB ALA A 139 21.581 49.337 57.204 1.00 15.25 C ATOM 1055 N TYR A 140 24.372 49.659 55.392 1.00 16.15 N ATOM 1056 CA TYR A 140 25.787 50.013 55.363 1.00 16.64 C ATOM 1057 C TYR A 140 26.002 51.515 55.487 1.00 16.25 C ATOM 1058 O TYR A 140 25.166 52.290 55.011 1.00 15.77 O ATOM 1059 CB TYR A 140 26.466 49.563 54.046 1.00 15.82 C ATOM 1060 CG TYR A 140 26.721 48.076 53.929 1.00 16.34 C ATOM 1061 CD1 TYR A 140 25.678 47.182 53.727 1.00 16.62 C ATOM 1062 CD2 TYR A 140 28.023 47.626 54.062 1.00 18.35 C ATOM 1063 CE1 TYR A 140 25.948 45.817 53.678 1.00 16.95 C ATOM 1064 CE2 TYR A 140 28.300 46.264 54.008 1.00 17.09 C ATOM 1065 CZ TYR A 140 27.256 45.365 53.830 1.00 18.82 C ATOM 1066 OH TYR A 140 27.542 43.998 53.825 1.00 18.19 O ATOM 1067 N ALA A 141 27.136 51.924 56.059 1.00 14.65 N ATOM 1068 CA ALA A 141 27.472 53.331 56.230 1.00 16.10 C ATOM 1069 C ALA A 141 27.685 54.031 54.886 1.00 16.09 C ATOM 1070 O ALA A 141 27.349 55.218 54.751 1.00 16.52 O ATOM 1071 CB ALA A 141 28.767 53.546 57.026 1.00 15.32 C ATOM 1072 N ASN A 142 28.224 53.340 53.865 1.00 16.14 N ATOM 1073 CA ASN A 142 28.432 53.972 52.554 1.00 16.69 C ATOM 1074 C ASN A 142 28.365 52.898 51.470 1.00 16.56 C ATOM 1075 O ASN A 142 28.449 51.685 51.772 1.00 15.82 O ATOM 1076 CB ASN A 142 29.778 54.680 52.512 1.00 15.79 C ATOM 1077 CG ASN A 142 30.995 53.777 52.526 1.00 17.53 C ATOM 1078 OD1 ASN A 142 31.326 53.075 51.566 1.00 17.61 O ATOM 1079 ND2 ASN A 142 31.699 53.683 53.616 1.00 20.23 N ATOM 1080 N GLN A 143 28.192 53.315 50.209 1.00 15.12 N ATOM 1081 CA GLN A 143 28.013 52.375 49.097 1.00 15.82 C ATOM 1082 C GLN A 143 29.252 51.591 48.674 1.00 17.28 C ATOM 1083 O GLN A 143 29.155 50.451 48.181 1.00 16.72 O ATOM 1084 CB GLN A 143 27.468 53.151 47.912 1.00 14.81 C ATOM 1085 CG GLN A 143 27.029 52.353 46.692 1.00 13.78 C ATOM 1086 CD GLN A 143 25.832 51.437 46.895 1.00 16.22 C ATOM 1087 OE1 GLN A 143 25.746 50.354 46.291 1.00 19.42 O ATOM 1088 NE2 GLN A 143 24.853 51.835 47.681 1.00 10.31 N ATOM 1089 N ASP A 144 30.440 52.143 48.900 1.00 16.99 N ATOM 1090 CA ASP A 144 31.635 51.403 48.548 1.00 20.29 C ATOM 1091 C ASP A 144 31.779 50.153 49.389 1.00 19.66 C ATOM 1092 O ASP A 144 32.178 49.111 48.850 1.00 20.86 O ATOM 1093 CB ASP A 144 32.862 52.256 48.733 1.00 23.50 C ATOM 1094 CG ASP A 144 32.993 53.374 47.700 1.00 27.97 C ATOM 1095 OD1 ASP A 144 32.362 53.320 46.626 1.00 27.11 O ATOM 1096 OD2 ASP A 144 33.740 54.319 48.008 1.00 32.39 O ATOM 1097 N LEU A 145 31.414 50.226 50.678 1.00 19.53 N ATOM 1098 CA LEU A 145 31.400 49.045 51.556 1.00 21.54 C ATOM 1099 C LEU A 145 30.452 47.987 50.999 1.00 20.60 C ATOM 1100 O LEU A 145 30.801 46.802 51.056 1.00 20.94 O ATOM 1101 CB LEU A 145 30.911 49.337 52.980 1.00 21.61 C ATOM 1102 CG LEU A 145 31.816 50.123 53.909 1.00 25.60 C ATOM 1103 CD1 LEU A 145 31.020 50.588 55.177 1.00 24.65 C ATOM 1104 CD2 LEU A 145 33.026 49.253 54.219 1.00 23.98 C ATOM 1105 N ILE A 146 29.314 48.388 50.407 1.00 18.34 N ATOM 1106 CA ILE A 146 28.381 47.426 49.829 1.00 18.85 C ATOM 1107 C ILE A 146 29.023 46.674 48.657 1.00 18.80 C ATOM 1108 O ILE A 146 28.974 45.436 48.577 1.00 18.19 O ATOM 1109 CB ILE A 146 27.107 48.136 49.341 1.00 17.16 C ATOM 1110 CG1 ILE A 146 26.421 48.773 50.531 1.00 14.82 C ATOM 1111 CG2 ILE A 146 26.222 47.159 48.586 1.00 16.06 C ATOM 1112 CD1 ILE A 146 25.040 49.362 50.263 1.00 12.17 C ATOM 1113 N TYR A 147 29.629 47.403 47.724 1.00 17.00 N ATOM 1114 CA TYR A 147 30.289 46.758 46.594 1.00 19.09 C ATOM 1115 C TYR A 147 31.429 45.837 47.059 1.00 19.72 C ATOM 1116 O TYR A 147 31.583 44.723 46.552 1.00 21.91 O ATOM 1117 CB TYR A 147 30.852 47.828 45.648 1.00 17.78 C ATOM 1118 CG TYR A 147 29.827 48.712 44.952 1.00 16.03 C ATOM 1119 CD1 TYR A 147 28.644 48.206 44.452 1.00 16.38 C ATOM 1120 CD2 TYR A 147 30.144 50.047 44.801 1.00 17.92 C ATOM 1121 CE1 TYR A 147 27.762 49.028 43.778 1.00 15.09 C ATOM 1122 CE2 TYR A 147 29.279 50.870 44.122 1.00 15.59 C ATOM 1123 CZ TYR A 147 28.105 50.354 43.625 1.00 15.34 C ATOM 1124 OH TYR A 147 27.262 51.209 42.961 1.00 17.03 O ATOM 1125 N SER A 148 32.203 46.225 48.059 1.00 19.82 N ATOM 1126 CA SER A 148 33.267 45.375 48.545 1.00 23.42 C ATOM 1127 C SER A 148 32.729 44.080 49.125 1.00 23.14 C ATOM 1128 O SER A 148 33.269 43.008 48.844 1.00 23.60 O ATOM 1129 CB SER A 148 34.070 46.057 49.628 1.00 25.53 C ATOM 1130 OG SER A 148 34.473 47.341 49.151 1.00 36.18 O ATOM 1131 N ASP A 149 31.656 44.121 49.896 1.00 22.29 N ATOM 1132 CA ASP A 149 31.142 42.910 50.456 1.00 22.37 C ATOM 1133 C ASP A 149 30.459 42.034 49.443 1.00 23.99 C ATOM 1134 O ASP A 149 30.506 40.804 49.597 1.00 24.17 O ATOM 1135 CB ASP A 149 30.213 43.266 51.574 1.00 23.71 C ATOM 1136 CG ASP A 149 30.951 43.395 52.904 1.00 25.93 C ATOM 1137 OD1 ASP A 149 32.195 43.381 52.948 1.00 24.74 O ATOM 1138 OD2 ASP A 149 30.244 43.480 53.910 1.00 26.28 O ATOM 1139 N LEU A 150 29.879 42.624 48.397 1.00 23.46 N ATOM 1140 CA LEU A 150 29.266 41.847 47.335 1.00 24.51 C ATOM 1141 C LEU A 150 30.373 41.088 46.636 1.00 25.74 C ATOM 1142 O LEU A 150 30.277 39.870 46.574 1.00 26.41 O ATOM 1143 CB LEU A 150 28.531 42.768 46.339 1.00 25.41 C ATOM 1144 CG LEU A 150 27.714 42.107 45.220 1.00 26.97 C ATOM 1145 CD1 LEU A 150 26.389 41.548 45.762 1.00 27.10 C ATOM 1146 CD2 LEU A 150 27.443 43.139 44.145 1.00 27.43 C ATOM 1147 N THR A 151 31.476 41.709 46.228 1.00 24.72 N ATOM 1148 CA THR A 151 32.523 40.983 45.540 1.00 28.20 C ATOM 1149 C THR A 151 33.226 39.991 46.474 1.00 29.98 C ATOM 1150 O THR A 151 33.789 38.986 46.034 1.00 33.26 O ATOM 1151 CB THR A 151 33.489 42.025 44.950 1.00 28.91 C ATOM 1152 OG1 THR A 151 33.936 42.849 46.026 1.00 33.68 O ATOM 1153 CG2 THR A 151 32.831 42.865 43.863 1.00 27.94 C ATOM 1154 N ALA A 152 33.235 40.245 47.783 1.00 30.31 N ATOM 1155 CA ALA A 152 33.755 39.301 48.760 1.00 30.80 C ATOM 1156 C ALA A 152 32.803 38.128 48.950 1.00 29.74 C ATOM 1157 O ALA A 152 33.148 37.173 49.644 1.00 32.44 O ATOM 1158 CB ALA A 152 33.940 39.946 50.137 1.00 29.33 C ATOM 1159 N GLY A 153 31.597 38.123 48.417 1.00 27.40 N ATOM 1160 CA GLY A 153 30.705 37.021 48.624 1.00 27.69 C ATOM 1161 C GLY A 153 30.018 37.124 49.966 1.00 28.43 C ATOM 1162 O GLY A 153 29.395 36.141 50.343 1.00 29.72 O ATOM 1163 N ARG A 154 30.065 38.233 50.728 1.00 26.53 N ATOM 1164 CA ARG A 154 29.287 38.334 51.953 1.00 25.64 C ATOM 1165 C ARG A 154 27.858 38.777 51.661 1.00 25.32 C ATOM 1166 O ARG A 154 26.960 38.610 52.500 1.00 28.40 O ATOM 1167 CB ARG A 154 29.897 39.321 52.898 1.00 28.31 C ATOM 1168 CG ARG A 154 31.315 38.946 53.226 1.00 35.00 C ATOM 1169 CD ARG A 154 31.893 39.919 54.221 1.00 39.39 C ATOM 1170 NE ARG A 154 33.298 39.599 54.362 1.00 46.95 N ATOM 1171 CZ ARG A 154 34.240 40.526 54.568 1.00 50.14 C ATOM 1172 NH1 ARG A 154 33.941 41.827 54.666 1.00 51.66 N ATOM 1173 NH2 ARG A 154 35.514 40.128 54.667 1.00 50.19 N ATOM 1174 N LEU A 155 27.584 39.383 50.494 1.00 21.56 N ATOM 1175 CA LEU A 155 26.221 39.760 50.144 1.00 20.05 C ATOM 1176 C LEU A 155 25.885 38.992 48.877 1.00 19.18 C ATOM 1177 O LEU A 155 26.793 38.673 48.112 1.00 20.42 O ATOM 1178 CB LEU A 155 26.074 41.265 49.836 1.00 19.67 C ATOM 1179 CG LEU A 155 26.313 42.287 50.953 1.00 18.66 C ATOM 1180 CD1 LEU A 155 26.334 43.693 50.349 1.00 16.63 C ATOM 1181 CD2 LEU A 155 25.243 42.157 52.011 1.00 17.17 C ATOM 1182 N ASP A 156 24.603 38.654 48.712 1.00 18.49 N ATOM 1183 CA ASP A 156 24.083 38.007 47.520 1.00 18.80 C ATOM 1184 C ASP A 156 23.567 39.064 46.556 1.00 18.87 C ATOM 1185 O ASP A 156 23.577 38.838 45.338 1.00 19.19 O ATOM 1186 CB ASP A 156 22.915 37.114 47.815 1.00 20.51 C ATOM 1187 CG ASP A 156 23.310 36.024 48.781 1.00 24.98 C ATOM 1188 OD1 ASP A 156 24.138 35.185 48.430 1.00 27.70 O ATOM 1189 OD2 ASP A 156 22.804 36.043 49.893 1.00 22.80 O ATOM 1190 N ALA A 157 23.115 40.215 47.060 1.00 15.84 N ATOM 1191 CA ALA A 157 22.536 41.229 46.203 1.00 14.76 C ATOM 1192 C ALA A 157 22.653 42.613 46.859 1.00 15.68 C ATOM 1193 O ALA A 157 22.907 42.691 48.071 1.00 16.35 O ATOM 1194 CB ALA A 157 21.070 40.901 45.971 1.00 14.33 C ATOM 1195 N ALA A 158 22.515 43.706 46.098 1.00 14.90 N ATOM 1196 CA ALA A 158 22.533 45.063 46.646 1.00 15.50 C ATOM 1197 C ALA A 158 21.502 45.915 45.896 1.00 15.73 C ATOM 1198 O ALA A 158 21.274 45.709 44.685 1.00 17.08 O ATOM 1199 CB ALA A 158 23.916 45.640 46.465 1.00 13.40 C ATOM 1200 N LEU A 159 20.790 46.814 46.585 1.00 14.11 N ATOM 1201 CA LEU A 159 19.777 47.656 45.971 1.00 13.69 C ATOM 1202 C LEU A 159 20.299 49.090 46.135 1.00 14.53 C ATOM 1203 O LEU A 159 20.701 49.497 47.238 1.00 14.36 O ATOM 1204 CB LEU A 159 18.440 47.506 46.699 1.00 13.94 C ATOM 1205 CG LEU A 159 17.207 48.226 46.092 1.00 17.44 C ATOM 1206 CD1 LEU A 159 16.806 47.542 44.771 1.00 15.25 C ATOM 1207 CD2 LEU A 159 16.041 48.194 47.083 1.00 15.10 C ATOM 1208 N GLN A 160 20.307 49.883 45.063 1.00 12.40 N ATOM 1209 CA GLN A 160 20.830 51.250 45.076 1.00 10.85 C ATOM 1210 C GLN A 160 20.286 51.905 43.805 1.00 13.21 C ATOM 1211 O GLN A 160 19.534 51.233 43.057 1.00 13.68 O ATOM 1212 CB GLN A 160 22.372 51.311 45.022 1.00 8.73 C ATOM 1213 CG GLN A 160 23.060 50.621 43.804 1.00 14.16 C ATOM 1214 CD GLN A 160 22.964 49.088 43.911 1.00 16.96 C ATOM 1215 OE1 GLN A 160 23.524 48.516 44.844 1.00 15.94 O ATOM 1216 NE2 GLN A 160 22.240 48.359 43.059 1.00 14.85 N ATOM 1217 N ASP A 161 20.609 53.186 43.527 1.00 11.53 N ATOM 1218 CA ASP A 161 20.179 53.811 42.282 1.00 11.31 C ATOM 1219 C ASP A 161 20.855 53.106 41.095 1.00 12.04 C ATOM 1220 O ASP A 161 22.062 52.818 41.068 1.00 11.40 O ATOM 1221 CB ASP A 161 20.550 55.302 42.271 1.00 10.47 C ATOM 1222 CG ASP A 161 19.799 56.195 43.264 1.00 11.98 C ATOM 1223 OD1 ASP A 161 18.784 55.799 43.855 1.00 12.05 O ATOM 1224 OD2 ASP A 161 20.246 57.326 43.423 1.00 12.18 O ATOM 1225 N GLU A 162 20.023 52.833 40.090 1.00 14.48 N ATOM 1226 CA GLU A 162 20.423 52.147 38.856 1.00 15.08 C ATOM 1227 C GLU A 162 21.681 52.703 38.171 1.00 14.56 C ATOM 1228 O GLU A 162 22.680 51.995 37.968 1.00 13.47 O ATOM 1229 CB GLU A 162 19.228 52.209 37.942 1.00 15.85 C ATOM 1230 CG GLU A 162 19.394 51.353 36.698 1.00 21.89 C ATOM 1231 CD GLU A 162 18.139 51.224 35.830 1.00 24.31 C ATOM 1232 OE1 GLU A 162 17.078 51.734 36.176 1.00 29.90 O ATOM 1233 OE2 GLU A 162 18.219 50.589 34.786 1.00 23.08 O ATOM 1234 N VAL A 163 21.692 54.005 37.847 1.00 14.14 N ATOM 1235 CA VAL A 163 22.849 54.633 37.202 1.00 14.82 C ATOM 1236 C VAL A 163 24.093 54.580 38.072 1.00 14.31 C ATOM 1237 O VAL A 163 25.173 54.397 37.512 1.00 14.70 O ATOM 1238 CB VAL A 163 22.537 56.143 36.795 1.00 13.75 C ATOM 1239 CG1 VAL A 163 23.724 56.734 36.067 1.00 13.53 C ATOM 1240 CG2 VAL A 163 21.329 56.214 35.855 1.00 13.85 C ATOM 1241 N ALA A 164 23.992 54.700 39.406 1.00 13.81 N ATOM 1242 CA ALA A 164 25.195 54.612 40.244 1.00 14.98 C ATOM 1243 C ALA A 164 25.780 53.192 40.118 1.00 14.87 C ATOM 1244 O ALA A 164 26.969 53.025 39.822 1.00 15.21 O ATOM 1245 CB ALA A 164 24.860 54.879 41.721 1.00 12.07 C ATOM 1246 N ALA A 165 24.934 52.150 40.242 1.00 14.71 N ATOM 1247 CA ALA A 165 25.396 50.758 40.102 1.00 15.88 C ATOM 1248 C ALA A 165 26.003 50.506 38.705 1.00 16.74 C ATOM 1249 O ALA A 165 27.097 49.918 38.596 1.00 16.95 O ATOM 1250 CB ALA A 165 24.227 49.765 40.309 1.00 12.94 C ATOM 1251 N SER A 166 25.336 51.010 37.655 1.00 15.95 N ATOM 1252 CA SER A 166 25.784 50.812 36.281 1.00 17.27 C ATOM 1253 C SER A 166 27.144 51.463 36.004 1.00 19.48 C ATOM 1254 O SER A 166 28.156 50.767 35.792 1.00 19.50 O ATOM 1255 CB SER A 166 24.739 51.375 35.332 1.00 19.03 C ATOM 1256 OG SER A 166 25.142 51.015 34.035 1.00 23.36 O ATOM 1257 N GLU A 167 27.197 52.796 36.139 1.00 18.91 N ATOM 1258 CA GLU A 167 28.404 53.529 35.852 1.00 19.74 C ATOM 1259 C GLU A 167 29.476 53.395 36.908 1.00 20.84 C ATOM 1260 O GLU A 167 30.678 53.308 36.609 1.00 20.87 O ATOM 1261 CB GLU A 167 28.038 55.007 35.641 1.00 19.20 C ATOM 1262 CG GLU A 167 27.066 55.237 34.462 1.00 21.93 C ATOM 1263 CD GLU A 167 27.604 54.853 33.072 1.00 25.53 C ATOM 1264 OE1 GLU A 167 28.828 54.760 32.902 1.00 24.17 O ATOM 1265 OE2 GLU A 167 26.790 54.670 32.157 1.00 27.89 O ATOM 1266 N GLY A 168 29.066 53.353 38.172 1.00 19.49 N ATOM 1267 CA GLY A 168 30.013 53.311 39.243 1.00 19.03 C ATOM 1268 C GLY A 168 30.470 51.900 39.495 1.00 20.33 C ATOM 1269 O GLY A 168 31.482 51.787 40.184 1.00 22.17 O ATOM 1270 N PHE A 169 29.864 50.805 39.000 1.00 19.07 N ATOM 1271 CA PHE A 169 30.350 49.482 39.379 1.00 18.99 C ATOM 1272 C PHE A 169 30.319 48.492 38.225 1.00 19.83 C ATOM 1273 O PHE A 169 31.372 47.956 37.858 1.00 19.36 O ATOM 1274 CB PHE A 169 29.506 48.933 40.558 1.00 19.07 C ATOM 1275 CG PHE A 169 29.849 47.537 41.093 1.00 20.32 C ATOM 1276 CD1 PHE A 169 31.074 47.283 41.713 1.00 23.35 C ATOM 1277 CD2 PHE A 169 28.939 46.493 40.931 1.00 21.20 C ATOM 1278 CE1 PHE A 169 31.391 45.999 42.161 1.00 21.23 C ATOM 1279 CE2 PHE A 169 29.265 45.222 41.379 1.00 21.70 C ATOM 1280 CZ PHE A 169 30.488 44.976 41.992 1.00 22.26 C ATOM 1281 N LEU A 170 29.147 48.253 37.636 1.00 20.03 N ATOM 1282 CA LEU A 170 28.984 47.238 36.621 1.00 21.18 C ATOM 1283 C LEU A 170 29.903 47.485 35.441 1.00 23.61 C ATOM 1284 O LEU A 170 30.540 46.531 34.987 1.00 24.04 O ATOM 1285 CB LEU A 170 27.527 47.179 36.138 1.00 19.68 C ATOM 1286 CG LEU A 170 26.517 46.698 37.147 1.00 18.56 C ATOM 1287 CD1 LEU A 170 25.147 46.481 36.520 1.00 15.59 C ATOM 1288 CD2 LEU A 170 27.049 45.384 37.720 1.00 21.12 C ATOM 1289 N LYS A 171 30.047 48.737 35.006 1.00 22.20 N ATOM 1290 CA LYS A 171 30.941 49.071 33.904 1.00 25.73 C ATOM 1291 C LYS A 171 32.386 49.267 34.341 1.00 26.81 C ATOM 1292 O LYS A 171 33.228 49.751 33.577 1.00 30.69 O ATOM 1293 CB LYS A 171 30.421 50.336 33.201 1.00 24.58 C ATOM 1294 CG LYS A 171 29.183 49.910 32.475 1.00 24.86 C ATOM 1295 CD LYS A 171 28.249 51.021 32.071 1.00 30.93 C ATOM 1296 CE LYS A 171 28.841 51.850 30.970 1.00 34.83 C ATOM 1297 NZ LYS A 171 27.768 52.562 30.305 1.00 37.91 N ATOM 1298 N GLN A 172 32.724 48.904 35.574 1.00 28.23 N ATOM 1299 CA GLN A 172 34.076 49.066 36.074 1.00 29.46 C ATOM 1300 C GLN A 172 34.702 47.682 36.167 1.00 30.44 C ATOM 1301 O GLN A 172 33.962 46.693 36.286 1.00 30.39 O ATOM 1302 CB GLN A 172 34.069 49.709 37.458 1.00 30.05 C ATOM 1303 CG GLN A 172 33.449 51.099 37.474 1.00 32.57 C ATOM 1304 CD GLN A 172 34.127 52.065 36.515 1.00 38.17 C ATOM 1305 OE1 GLN A 172 35.359 52.088 36.423 1.00 40.77 O ATOM 1306 NE2 GLN A 172 33.404 52.886 35.752 1.00 38.90 N ATOM 1307 N PRO A 173 36.041 47.553 36.146 1.00 32.74 N ATOM 1308 CA PRO A 173 36.798 46.328 36.428 1.00 33.07 C ATOM 1309 C PRO A 173 36.180 45.405 37.467 1.00 33.42 C ATOM 1310 O PRO A 173 35.834 44.246 37.194 1.00 33.64 O ATOM 1311 CB PRO A 173 38.156 46.852 36.832 1.00 34.18 C ATOM 1312 CG PRO A 173 38.346 47.982 35.846 1.00 34.12 C ATOM 1313 CD PRO A 173 36.968 48.626 35.778 1.00 33.57 C ATOM 1314 N ALA A 174 35.956 46.007 38.646 1.00 33.37 N ATOM 1315 CA ALA A 174 35.352 45.304 39.767 1.00 32.17 C ATOM 1316 C ALA A 174 33.974 44.701 39.513 1.00 31.76 C ATOM 1317 O ALA A 174 33.690 43.673 40.138 1.00 33.51 O ATOM 1318 CB ALA A 174 35.224 46.233 40.952 1.00 31.89 C ATOM 1319 N GLY A 175 33.129 45.210 38.607 1.00 28.86 N ATOM 1320 CA GLY A 175 31.795 44.667 38.448 1.00 27.66 C ATOM 1321 C GLY A 175 31.596 43.768 37.237 1.00 26.90 C ATOM 1322 O GLY A 175 30.459 43.391 36.911 1.00 25.04 O ATOM 1323 N LYS A 176 32.689 43.379 36.593 1.00 27.86 N ATOM 1324 CA LYS A 176 32.641 42.566 35.380 1.00 29.25 C ATOM 1325 C LYS A 176 31.841 41.273 35.511 1.00 29.30 C ATOM 1326 O LYS A 176 31.130 40.865 34.597 1.00 29.81 O ATOM 1327 CB LYS A 176 34.074 42.214 34.948 1.00 29.61 C ATOM 1328 N GLU A 177 31.889 40.641 36.685 1.00 30.78 N ATOM 1329 CA GLU A 177 31.156 39.405 36.935 1.00 31.84 C ATOM 1330 C GLU A 177 29.787 39.611 37.598 1.00 30.91 C ATOM 1331 O GLU A 177 29.226 38.672 38.187 1.00 29.43 O ATOM 1332 CB GLU A 177 32.022 38.497 37.821 1.00 33.49 C ATOM 1333 N TYR A 178 29.229 40.830 37.525 1.00 28.32 N ATOM 1334 CA TYR A 178 27.967 41.126 38.173 1.00 25.23 C ATOM 1335 C TYR A 178 27.083 41.718 37.137 1.00 22.85 C ATOM 1336 O TYR A 178 27.580 42.135 36.097 1.00 24.09 O ATOM 1337 CB TYR A 178 28.151 42.119 39.320 1.00 25.32 C ATOM 1338 CG TYR A 178 28.985 41.462 40.402 1.00 27.25 C ATOM 1339 CD1 TYR A 178 28.376 40.647 41.326 1.00 27.95 C ATOM 1340 CD2 TYR A 178 30.358 41.623 40.394 1.00 27.92 C ATOM 1341 CE1 TYR A 178 29.148 39.961 42.235 1.00 28.46 C ATOM 1342 CE2 TYR A 178 31.132 40.948 41.298 1.00 30.28 C ATOM 1343 CZ TYR A 178 30.515 40.115 42.202 1.00 30.23 C ATOM 1344 OH TYR A 178 31.304 39.396 43.071 1.00 35.82 O ATOM 1345 N ALA A 179 25.795 41.727 37.415 1.00 20.18 N ATOM 1346 CA ALA A 179 24.812 42.263 36.510 1.00 18.12 C ATOM 1347 C ALA A 179 23.586 42.696 37.279 1.00 17.93 C ATOM 1348 O ALA A 179 23.438 42.406 38.462 1.00 20.24 O ATOM 1349 CB ALA A 179 24.368 41.216 35.519 1.00 18.57 C ATOM 1350 N PHE A 180 22.706 43.453 36.652 1.00 18.23 N ATOM 1351 CA PHE A 180 21.406 43.768 37.199 1.00 17.42 C ATOM 1352 C PHE A 180 20.586 42.506 37.322 1.00 18.63 C ATOM 1353 O PHE A 180 20.618 41.606 36.475 1.00 19.37 O ATOM 1354 CB PHE A 180 20.669 44.741 36.305 1.00 15.60 C ATOM 1355 CG PHE A 180 21.206 46.161 36.408 1.00 18.70 C ATOM 1356 CD1 PHE A 180 21.254 46.808 37.645 1.00 17.11 C ATOM 1357 CD2 PHE A 180 21.595 46.849 35.270 1.00 19.39 C ATOM 1358 CE1 PHE A 180 21.686 48.122 37.725 1.00 18.11 C ATOM 1359 CE2 PHE A 180 22.026 48.168 35.365 1.00 20.24 C ATOM 1360 CZ PHE A 180 22.072 48.802 36.589 1.00 18.24 C ATOM 1361 N ALA A 181 19.848 42.391 38.407 1.00 18.55 N ATOM 1362 CA ALA A 181 19.027 41.237 38.635 1.00 18.62 C ATOM 1363 C ALA A 181 17.597 41.713 38.540 1.00 19.63 C ATOM 1364 O ALA A 181 17.034 42.281 39.481 1.00 20.07 O ATOM 1365 CB ALA A 181 19.344 40.672 40.013 1.00 19.88 C ATOM 1366 N GLY A 182 16.971 41.481 37.380 1.00 16.82 N ATOM 1367 CA GLY A 182 15.594 41.905 37.145 1.00 16.34 C ATOM 1368 C GLY A 182 15.531 43.368 36.694 1.00 16.51 C ATOM 1369 O GLY A 182 16.569 44.023 36.597 1.00 16.16 O ATOM 1370 N PRO A 183 14.365 43.901 36.360 1.00 17.59 N ATOM 1371 CA PRO A 183 14.169 45.288 35.936 1.00 19.21 C ATOM 1372 C PRO A 183 14.179 46.275 37.121 1.00 18.05 C ATOM 1373 O PRO A 183 14.200 45.822 38.274 1.00 17.25 O ATOM 1374 CB PRO A 183 12.849 45.224 35.194 1.00 18.25 C ATOM 1375 CG PRO A 183 12.058 44.274 36.072 1.00 18.92 C ATOM 1376 CD PRO A 183 13.088 43.191 36.435 1.00 19.69 C ATOM 1377 N SER A 184 14.149 47.590 36.883 1.00 19.38 N ATOM 1378 CA SER A 184 14.063 48.598 37.930 1.00 21.43 C ATOM 1379 C SER A 184 12.890 48.301 38.842 1.00 23.39 C ATOM 1380 O SER A 184 11.845 47.838 38.355 1.00 25.12 O ATOM 1381 CB SER A 184 13.811 49.967 37.361 1.00 21.05 C ATOM 1382 OG SER A 184 14.721 50.155 36.308 1.00 28.81 O ATOM 1383 N VAL A 185 13.052 48.555 40.140 1.00 24.11 N ATOM 1384 CA VAL A 185 11.978 48.390 41.112 1.00 26.29 C ATOM 1385 C VAL A 185 11.216 49.699 41.115 1.00 27.47 C ATOM 1386 O VAL A 185 11.757 50.745 41.452 1.00 30.03 O ATOM 1387 CB VAL A 185 12.536 48.123 42.525 1.00 25.39 C ATOM 1388 CG1 VAL A 185 11.385 47.916 43.494 1.00 25.20 C ATOM 1389 CG2 VAL A 185 13.455 46.910 42.484 1.00 27.95 C ATOM 1390 N LYS A 186 9.991 49.722 40.675 1.00 30.59 N ATOM 1391 CA LYS A 186 9.220 50.927 40.724 1.00 33.08 C ATOM 1392 C LYS A 186 8.288 50.859 41.920 1.00 33.37 C ATOM 1393 O LYS A 186 7.568 49.872 42.129 1.00 33.46 O ATOM 1394 CB LYS A 186 8.415 51.077 39.446 1.00 36.88 C ATOM 1395 CG LYS A 186 9.224 51.250 38.173 1.00 41.98 C ATOM 1396 CD LYS A 186 10.166 52.454 38.224 1.00 47.15 C ATOM 1397 CE LYS A 186 10.409 53.073 36.841 1.00 50.00 C ATOM 1398 NZ LYS A 186 11.010 52.163 35.876 1.00 53.11 N ATOM 1399 N ASP A 187 8.341 51.891 42.737 1.00 31.42 N ATOM 1400 CA ASP A 187 7.404 52.070 43.811 1.00 31.81 C ATOM 1401 C ASP A 187 7.380 53.560 44.069 1.00 32.75 C ATOM 1402 O ASP A 187 8.287 54.094 44.723 1.00 31.79 O ATOM 1403 CB ASP A 187 7.842 51.368 45.088 1.00 34.45 C ATOM 1404 CG ASP A 187 6.687 51.316 46.062 1.00 37.37 C ATOM 1405 OD1 ASP A 187 6.144 52.357 46.437 1.00 39.15 O ATOM 1406 OD2 ASP A 187 6.323 50.208 46.436 1.00 40.11 O ATOM 1407 N LYS A 188 6.310 54.245 43.666 1.00 33.78 N ATOM 1408 CA LYS A 188 6.215 55.705 43.800 1.00 35.22 C ATOM 1409 C LYS A 188 6.351 56.227 45.233 1.00 33.94 C ATOM 1410 O LYS A 188 7.078 57.203 45.477 1.00 35.67 O ATOM 1411 CB LYS A 188 4.868 56.210 43.240 1.00 36.11 C ATOM 1412 N LYS A 189 5.723 55.508 46.166 1.00 30.42 N ATOM 1413 CA LYS A 189 5.783 55.848 47.573 1.00 30.70 C ATOM 1414 C LYS A 189 7.189 55.900 48.169 1.00 29.63 C ATOM 1415 O LYS A 189 7.511 56.730 49.028 1.00 32.38 O ATOM 1416 CB LYS A 189 5.004 54.840 48.422 1.00 30.74 C ATOM 1417 N TYR A 190 8.039 54.972 47.765 1.00 24.34 N ATOM 1418 CA TYR A 190 9.349 54.935 48.382 1.00 22.04 C ATOM 1419 C TYR A 190 10.423 55.714 47.656 1.00 19.40 C ATOM 1420 O TYR A 190 11.263 56.344 48.302 1.00 18.04 O ATOM 1421 CB TYR A 190 9.831 53.506 48.511 1.00 20.93 C ATOM 1422 CG TYR A 190 9.117 52.793 49.630 1.00 21.83 C ATOM 1423 CD1 TYR A 190 9.597 52.928 50.919 1.00 23.85 C ATOM 1424 CD2 TYR A 190 8.014 52.024 49.345 1.00 22.97 C ATOM 1425 CE1 TYR A 190 8.979 52.258 51.943 1.00 23.42 C ATOM 1426 CE2 TYR A 190 7.397 51.351 50.368 1.00 24.11 C ATOM 1427 CZ TYR A 190 7.887 51.477 51.645 1.00 25.40 C ATOM 1428 OH TYR A 190 7.230 50.811 52.649 1.00 28.69 O ATOM 1429 N PHE A 191 10.391 55.692 46.324 1.00 16.82 N ATOM 1430 CA PHE A 191 11.560 56.156 45.643 1.00 16.61 C ATOM 1431 C PHE A 191 11.444 57.578 45.181 1.00 16.12 C ATOM 1432 O PHE A 191 12.458 58.147 44.759 1.00 18.12 O ATOM 1433 CB PHE A 191 11.853 55.180 44.485 1.00 16.63 C ATOM 1434 CG PHE A 191 12.184 53.779 45.030 1.00 19.23 C ATOM 1435 CD1 PHE A 191 13.245 53.581 45.911 1.00 16.92 C ATOM 1436 CD2 PHE A 191 11.412 52.686 44.646 1.00 21.78 C ATOM 1437 CE1 PHE A 191 13.505 52.305 46.398 1.00 19.39 C ATOM 1438 CE2 PHE A 191 11.682 51.415 45.140 1.00 20.49 C ATOM 1439 CZ PHE A 191 12.731 51.229 46.013 1.00 17.48 C ATOM 1440 N GLY A 192 10.264 58.173 45.255 1.00 16.61 N ATOM 1441 CA GLY A 192 10.106 59.585 44.918 1.00 19.20 C ATOM 1442 C GLY A 192 10.229 59.937 43.437 1.00 21.15 C ATOM 1443 O GLY A 192 10.094 59.049 42.579 1.00 22.09 O ATOM 1444 N ASP A 193 10.520 61.208 43.117 1.00 21.12 N ATOM 1445 CA ASP A 193 10.536 61.644 41.750 1.00 22.43 C ATOM 1446 C ASP A 193 11.793 62.373 41.340 1.00 21.66 C ATOM 1447 O ASP A 193 11.783 63.597 41.266 1.00 23.96 O ATOM 1448 CB ASP A 193 9.329 62.543 41.516 1.00 27.65 C ATOM 1449 CG ASP A 193 8.904 62.712 40.053 1.00 33.07 C ATOM 1450 OD1 ASP A 193 9.442 62.057 39.148 1.00 32.86 O ATOM 1451 OD2 ASP A 193 7.999 63.519 39.832 1.00 37.10 O ATOM 1452 N GLY A 194 12.883 61.686 41.035 1.00 18.70 N ATOM 1453 CA GLY A 194 14.104 62.370 40.663 1.00 14.44 C ATOM 1454 C GLY A 194 14.769 62.897 41.916 1.00 12.79 C ATOM 1455 O GLY A 194 14.264 62.707 43.034 1.00 14.84 O ATOM 1456 N THR A 195 15.927 63.507 41.745 1.00 12.05 N ATOM 1457 CA THR A 195 16.758 64.009 42.836 1.00 12.72 C ATOM 1458 C THR A 195 16.763 65.538 42.822 1.00 13.17 C ATOM 1459 O THR A 195 16.499 66.123 41.750 1.00 14.30 O ATOM 1460 CB THR A 195 18.227 63.507 42.719 1.00 11.09 C ATOM 1461 OG1 THR A 195 18.877 64.097 41.588 1.00 11.70 O ATOM 1462 CG2 THR A 195 18.227 61.967 42.638 1.00 9.71 C ATOM 1463 N GLY A 196 17.030 66.222 43.932 1.00 12.05 N ATOM 1464 CA GLY A 196 17.052 67.677 43.913 1.00 13.22 C ATOM 1465 C GLY A 196 17.981 68.145 45.021 1.00 13.89 C ATOM 1466 O GLY A 196 18.536 67.330 45.778 1.00 12.86 O ATOM 1467 N VAL A 197 18.281 69.447 45.042 1.00 13.21 N ATOM 1468 CA VAL A 197 19.037 70.070 46.124 1.00 12.03 C ATOM 1469 C VAL A 197 18.130 70.087 47.363 1.00 13.39 C ATOM 1470 O VAL A 197 16.997 70.594 47.279 1.00 13.83 O ATOM 1471 CB VAL A 197 19.457 71.556 45.797 1.00 11.87 C ATOM 1472 CG1 VAL A 197 20.420 72.014 46.887 1.00 11.57 C ATOM 1473 CG2 VAL A 197 20.098 71.696 44.429 1.00 9.82 C ATOM 1474 N GLY A 198 18.585 69.505 48.485 1.00 12.85 N ATOM 1475 CA GLY A 198 17.822 69.559 49.734 1.00 11.95 C ATOM 1476 C GLY A 198 18.167 70.851 50.485 1.00 12.04 C ATOM 1477 O GLY A 198 19.342 71.201 50.615 1.00 11.27 O ATOM 1478 N LEU A 199 17.166 71.565 50.981 1.00 11.89 N ATOM 1479 CA LEU A 199 17.340 72.869 51.605 1.00 12.85 C ATOM 1480 C LEU A 199 16.418 72.967 52.797 1.00 11.83 C ATOM 1481 O LEU A 199 15.412 72.262 52.861 1.00 12.21 O ATOM 1482 CB LEU A 199 16.964 73.987 50.616 1.00 14.59 C ATOM 1483 CG LEU A 199 17.778 74.005 49.332 1.00 13.67 C ATOM 1484 CD1 LEU A 199 16.885 74.460 48.228 1.00 17.88 C ATOM 1485 CD2 LEU A 199 19.066 74.773 49.550 1.00 15.96 C ATOM 1486 N ARG A 200 16.732 73.805 53.790 1.00 14.36 N ATOM 1487 CA ARG A 200 15.836 74.056 54.910 1.00 13.83 C ATOM 1488 C ARG A 200 14.561 74.724 54.384 1.00 15.98 C ATOM 1489 O ARG A 200 14.620 75.582 53.484 1.00 15.55 O ATOM 1490 CB ARG A 200 16.518 74.980 55.918 1.00 16.47 C ATOM 1491 CG ARG A 200 17.598 74.309 56.806 1.00 13.92 C ATOM 1492 CD ARG A 200 18.183 75.347 57.768 1.00 15.10 C ATOM 1493 NE ARG A 200 19.022 76.301 57.056 1.00 15.34 N ATOM 1494 CZ ARG A 200 20.307 76.059 56.772 1.00 17.42 C ATOM 1495 NH1 ARG A 200 20.954 74.923 57.101 1.00 16.66 N ATOM 1496 NH2 ARG A 200 20.974 77.011 56.139 1.00 17.24 N ATOM 1497 N LYS A 201 13.386 74.337 54.884 1.00 15.96 N ATOM 1498 CA LYS A 201 12.117 74.919 54.462 1.00 18.27 C ATOM 1499 C LYS A 201 12.008 76.434 54.438 1.00 21.07 C ATOM 1500 O LYS A 201 11.376 77.032 53.570 1.00 21.89 O ATOM 1501 CB LYS A 201 11.029 74.425 55.335 1.00 20.23 C ATOM 1502 CG LYS A 201 10.815 72.938 55.181 1.00 22.19 C ATOM 1503 CD LYS A 201 9.651 72.584 56.081 1.00 26.13 C ATOM 1504 CE LYS A 201 9.012 71.323 55.619 1.00 26.50 C ATOM 1505 NZ LYS A 201 7.810 71.077 56.385 1.00 32.22 N ATOM 1506 N ASP A 202 12.586 77.088 55.430 1.00 20.31 N ATOM 1507 CA ASP A 202 12.556 78.537 55.472 1.00 21.86 C ATOM 1508 C ASP A 202 13.559 79.241 54.547 1.00 22.72 C ATOM 1509 O ASP A 202 13.497 80.471 54.467 1.00 20.37 O ATOM 1510 CB ASP A 202 12.767 78.971 56.922 1.00 21.87 C ATOM 1511 CG ASP A 202 14.065 78.456 57.549 1.00 23.35 C ATOM 1512 OD1 ASP A 202 14.165 77.253 57.795 1.00 23.33 O ATOM 1513 OD2 ASP A 202 14.954 79.264 57.812 1.00 25.54 O ATOM 1514 N ASP A 203 14.471 78.543 53.825 1.00 21.32 N ATOM 1515 CA ASP A 203 15.444 79.205 52.974 1.00 20.39 C ATOM 1516 C ASP A 203 14.922 79.309 51.558 1.00 21.00 C ATOM 1517 O ASP A 203 15.503 78.888 50.556 1.00 17.78 O ATOM 1518 CB ASP A 203 16.781 78.458 52.969 1.00 21.11 C ATOM 1519 CG ASP A 203 17.753 78.861 54.085 1.00 25.82 C ATOM 1520 OD1 ASP A 203 17.469 79.833 54.791 1.00 29.84 O ATOM 1521 OD2 ASP A 203 18.808 78.238 54.261 1.00 24.89 O ATOM 1522 N THR A 204 13.802 80.007 51.474 1.00 21.55 N ATOM 1523 CA THR A 204 13.110 80.117 50.199 1.00 24.55 C ATOM 1524 C THR A 204 13.916 80.975 49.206 1.00 23.35 C ATOM 1525 O THR A 204 13.919 80.724 48.005 1.00 22.02 O ATOM 1526 CB THR A 204 11.689 80.668 50.521 1.00 23.85 C ATOM 1527 OG1 THR A 204 11.837 81.857 51.267 1.00 28.68 O ATOM 1528 CG2 THR A 204 10.901 79.735 51.390 1.00 24.04 C ATOM 1529 N GLU A 205 14.714 81.922 49.707 1.00 23.39 N ATOM 1530 CA GLU A 205 15.517 82.787 48.867 1.00 26.00 C ATOM 1531 C GLU A 205 16.618 81.915 48.244 1.00 25.34 C ATOM 1532 O GLU A 205 16.932 82.021 47.041 1.00 23.31 O ATOM 1533 CB GLU A 205 16.146 83.888 49.699 1.00 30.49 C ATOM 1534 CG GLU A 205 16.616 85.044 48.821 1.00 42.46 C ATOM 1535 CD GLU A 205 17.468 86.131 49.487 1.00 48.31 C ATOM 1536 OE1 GLU A 205 17.263 86.455 50.661 1.00 51.45 O ATOM 1537 OE2 GLU A 205 18.358 86.680 48.828 1.00 50.47 O ATOM 1538 N LEU A 206 17.211 80.993 49.035 1.00 23.35 N ATOM 1539 CA LEU A 206 18.243 80.118 48.497 1.00 20.92 C ATOM 1540 C LEU A 206 17.632 79.135 47.484 1.00 17.88 C ATOM 1541 O LEU A 206 18.240 78.894 46.421 1.00 17.82 O ATOM 1542 CB LEU A 206 18.942 79.396 49.669 1.00 20.06 C ATOM 1543 CG LEU A 206 20.179 78.569 49.325 1.00 21.55 C ATOM 1544 CD1 LEU A 206 21.230 79.407 48.602 1.00 20.00 C ATOM 1545 CD2 LEU A 206 20.751 78.021 50.623 1.00 22.99 C ATOM 1546 N LYS A 207 16.433 78.601 47.746 1.00 15.64 N ATOM 1547 CA LYS A 207 15.794 77.712 46.780 1.00 16.28 C ATOM 1548 C LYS A 207 15.528 78.435 45.452 1.00 19.16 C ATOM 1549 O LYS A 207 15.784 77.872 44.379 1.00 19.39 O ATOM 1550 CB LYS A 207 14.448 77.174 47.302 1.00 15.14 C ATOM 1551 CG LYS A 207 13.613 76.420 46.284 1.00 15.42 C ATOM 1552 CD LYS A 207 12.339 75.906 46.845 1.00 15.46 C ATOM 1553 CE LYS A 207 11.322 75.601 45.725 1.00 20.06 C ATOM 1554 NZ LYS A 207 11.812 74.654 44.717 1.00 16.61 N ATOM 1555 N ALA A 208 15.004 79.664 45.493 1.00 17.85 N ATOM 1556 CA ALA A 208 14.729 80.420 44.303 1.00 16.84 C ATOM 1557 C ALA A 208 15.992 80.648 43.485 1.00 15.81 C ATOM 1558 O ALA A 208 15.924 80.527 42.260 1.00 16.05 O ATOM 1559 CB ALA A 208 14.134 81.739 44.706 1.00 18.34 C ATOM 1560 N ALA A 209 17.140 80.930 44.105 1.00 16.00 N ATOM 1561 CA ALA A 209 18.394 81.118 43.410 1.00 15.91 C ATOM 1562 C ALA A 209 18.892 79.831 42.741 1.00 18.90 C ATOM 1563 O ALA A 209 19.381 79.861 41.588 1.00 16.19 O ATOM 1564 CB ALA A 209 19.438 81.598 44.397 1.00 16.71 C ATOM 1565 N PHE A 210 18.812 78.675 43.455 1.00 16.26 N ATOM 1566 CA PHE A 210 19.185 77.391 42.860 1.00 15.72 C ATOM 1567 C PHE A 210 18.241 77.073 41.702 1.00 13.86 C ATOM 1568 O PHE A 210 18.708 76.635 40.642 1.00 15.63 O ATOM 1569 CB PHE A 210 19.093 76.190 43.861 1.00 14.06 C ATOM 1570 CG PHE A 210 20.340 75.992 44.704 1.00 14.70 C ATOM 1571 CD1 PHE A 210 21.519 75.597 44.084 1.00 12.75 C ATOM 1572 CD2 PHE A 210 20.301 76.214 46.070 1.00 13.04 C ATOM 1573 CE1 PHE A 210 22.666 75.410 44.829 1.00 16.42 C ATOM 1574 CE2 PHE A 210 21.472 76.019 46.793 1.00 13.55 C ATOM 1575 CZ PHE A 210 22.654 75.614 46.197 1.00 13.97 C ATOM 1576 N ASP A 211 16.926 77.278 41.834 1.00 14.80 N ATOM 1577 CA ASP A 211 15.987 76.982 40.737 1.00 15.78 C ATOM 1578 C ASP A 211 16.197 77.815 39.486 1.00 15.86 C ATOM 1579 O ASP A 211 16.146 77.305 38.372 1.00 16.21 O ATOM 1580 CB ASP A 211 14.572 77.164 41.217 1.00 14.46 C ATOM 1581 CG ASP A 211 14.123 76.031 42.141 1.00 18.29 C ATOM 1582 OD1 ASP A 211 14.775 74.997 42.178 1.00 19.33 O ATOM 1583 OD2 ASP A 211 13.116 76.176 42.817 1.00 19.93 O ATOM 1584 N LYS A 212 16.498 79.099 39.657 1.00 15.80 N ATOM 1585 CA LYS A 212 16.771 80.002 38.557 1.00 15.16 C ATOM 1586 C LYS A 212 18.069 79.586 37.868 1.00 14.44 C ATOM 1587 O LYS A 212 18.086 79.430 36.652 1.00 16.26 O ATOM 1588 CB LYS A 212 16.879 81.410 39.114 1.00 17.94 C ATOM 1589 CG LYS A 212 17.252 82.413 38.040 1.00 22.86 C ATOM 1590 CD LYS A 212 17.288 83.809 38.603 1.00 28.27 C ATOM 1591 CE LYS A 212 17.576 84.840 37.504 1.00 31.97 C ATOM 1592 NZ LYS A 212 19.005 84.940 37.226 1.00 35.22 N ATOM 1593 N ALA A 213 19.161 79.317 38.598 1.00 14.79 N ATOM 1594 CA ALA A 213 20.413 78.904 37.989 1.00 14.21 C ATOM 1595 C ALA A 213 20.227 77.566 37.260 1.00 16.10 C ATOM 1596 O ALA A 213 20.762 77.371 36.170 1.00 15.78 O ATOM 1597 CB ALA A 213 21.456 78.725 39.052 1.00 14.47 C ATOM 1598 N LEU A 214 19.444 76.620 37.800 1.00 17.23 N ATOM 1599 CA LEU A 214 19.215 75.340 37.148 1.00 17.40 C ATOM 1600 C LEU A 214 18.471 75.542 35.830 1.00 17.43 C ATOM 1601 O LEU A 214 18.868 74.949 34.826 1.00 16.57 O ATOM 1602 CB LEU A 214 18.396 74.424 38.060 1.00 17.50 C ATOM 1603 CG LEU A 214 18.075 73.031 37.521 1.00 18.28 C ATOM 1604 CD1 LEU A 214 19.361 72.228 37.240 1.00 16.16 C ATOM 1605 CD2 LEU A 214 17.181 72.343 38.542 1.00 18.41 C ATOM 1606 N THR A 215 17.376 76.306 35.797 1.00 18.16 N ATOM 1607 CA THR A 215 16.690 76.652 34.551 1.00 20.51 C ATOM 1608 C THR A 215 17.630 77.239 33.515 1.00 19.00 C ATOM 1609 O THR A 215 17.639 76.763 32.384 1.00 18.86 O ATOM 1610 CB THR A 215 15.588 77.661 34.823 1.00 22.50 C ATOM 1611 OG1 THR A 215 14.710 77.005 35.712 1.00 25.93 O ATOM 1612 CG2 THR A 215 14.786 78.064 33.587 1.00 24.86 C ATOM 1613 N GLU A 216 18.445 78.222 33.903 1.00 20.57 N ATOM 1614 CA GLU A 216 19.391 78.863 32.990 1.00 21.22 C ATOM 1615 C GLU A 216 20.420 77.897 32.435 1.00 19.96 C ATOM 1616 O GLU A 216 20.661 77.908 31.230 1.00 18.44 O ATOM 1617 CB GLU A 216 20.137 80.006 33.685 1.00 21.50 C ATOM 1618 CG GLU A 216 19.101 81.055 34.058 1.00 29.92 C ATOM 1619 CD GLU A 216 19.577 82.280 34.841 1.00 33.39 C ATOM 1620 OE1 GLU A 216 20.739 82.326 35.284 1.00 34.17 O ATOM 1621 OE2 GLU A 216 18.735 83.182 34.996 1.00 36.34 O ATOM 1622 N LEU A 217 21.037 77.024 33.234 1.00 17.53 N ATOM 1623 CA LEU A 217 22.044 76.156 32.672 1.00 16.16 C ATOM 1624 C LEU A 217 21.376 75.044 31.866 1.00 15.95 C ATOM 1625 O LEU A 217 22.025 74.486 30.967 1.00 17.26 O ATOM 1626 CB LEU A 217 22.937 75.638 33.828 1.00 18.28 C ATOM 1627 CG LEU A 217 22.497 74.682 34.932 1.00 18.67 C ATOM 1628 CD1 LEU A 217 22.645 73.271 34.401 1.00 19.98 C ATOM 1629 CD2 LEU A 217 23.392 74.796 36.166 1.00 16.76 C ATOM 1630 N ARG A 218 20.098 74.674 32.092 1.00 15.70 N ATOM 1631 CA ARG A 218 19.438 73.702 31.225 1.00 18.57 C ATOM 1632 C ARG A 218 19.110 74.314 29.854 1.00 20.33 C ATOM 1633 O ARG A 218 19.403 73.786 28.790 1.00 19.43 O ATOM 1634 CB ARG A 218 18.168 73.221 31.874 1.00 18.65 C ATOM 1635 CG ARG A 218 18.478 72.145 32.951 1.00 21.46 C ATOM 1636 CD ARG A 218 17.230 71.440 33.530 1.00 24.00 C ATOM 1637 NE ARG A 218 16.324 70.838 32.541 1.00 24.70 N ATOM 1638 CZ ARG A 218 16.669 69.856 31.688 1.00 30.33 C ATOM 1639 NH1 ARG A 218 17.895 69.314 31.647 1.00 29.28 N ATOM 1640 NH2 ARG A 218 15.737 69.387 30.847 1.00 34.65 N ATOM 1641 N GLN A 219 18.611 75.540 29.926 1.00 22.28 N ATOM 1642 CA GLN A 219 18.189 76.362 28.793 1.00 24.08 C ATOM 1643 C GLN A 219 19.263 76.608 27.755 1.00 21.98 C ATOM 1644 O GLN A 219 19.047 76.459 26.562 1.00 20.92 O ATOM 1645 CB GLN A 219 17.723 77.662 29.371 1.00 28.30 C ATOM 1646 CG GLN A 219 16.593 78.331 28.702 1.00 37.47 C ATOM 1647 CD GLN A 219 15.747 79.103 29.708 1.00 44.32 C ATOM 1648 OE1 GLN A 219 14.617 78.710 30.013 1.00 48.19 O ATOM 1649 NE2 GLN A 219 16.254 80.197 30.271 1.00 46.48 N ATOM 1650 N ASP A 220 20.446 77.001 28.180 1.00 20.54 N ATOM 1651 CA ASP A 220 21.482 77.311 27.235 1.00 18.87 C ATOM 1652 C ASP A 220 22.267 76.104 26.762 1.00 18.04 C ATOM 1653 O ASP A 220 23.288 76.268 26.095 1.00 17.21 O ATOM 1654 CB ASP A 220 22.373 78.365 27.900 1.00 19.23 C ATOM 1655 CG ASP A 220 23.286 77.924 29.050 1.00 23.42 C ATOM 1656 OD1 ASP A 220 23.290 76.753 29.418 1.00 22.80 O ATOM 1657 OD2 ASP A 220 24.011 78.764 29.587 1.00 23.68 O ATOM 1658 N GLY A 221 21.922 74.884 27.187 1.00 19.83 N ATOM 1659 CA GLY A 221 22.672 73.698 26.771 1.00 17.89 C ATOM 1660 C GLY A 221 23.852 73.292 27.659 1.00 17.23 C ATOM 1661 O GLY A 221 24.516 72.274 27.378 1.00 18.00 O ATOM 1662 N THR A 222 24.144 73.993 28.763 1.00 15.57 N ATOM 1663 CA THR A 222 25.243 73.608 29.654 1.00 17.83 C ATOM 1664 C THR A 222 24.951 72.265 30.348 1.00 16.81 C ATOM 1665 O THR A 222 25.877 71.455 30.505 1.00 17.81 O ATOM 1666 CB THR A 222 25.471 74.666 30.740 1.00 17.58 C ATOM 1667 OG1 THR A 222 25.830 75.838 30.025 1.00 21.57 O ATOM 1668 CG2 THR A 222 26.574 74.330 31.733 1.00 20.30 C ATOM 1669 N TYR A 223 23.698 71.997 30.748 1.00 15.87 N ATOM 1670 CA TYR A 223 23.401 70.735 31.418 1.00 17.53 C ATOM 1671 C TYR A 223 23.796 69.556 30.518 1.00 20.13 C ATOM 1672 O TYR A 223 24.437 68.596 30.970 1.00 18.91 O ATOM 1673 CB TYR A 223 21.901 70.660 31.750 1.00 16.67 C ATOM 1674 CG TYR A 223 21.464 69.385 32.495 1.00 17.85 C ATOM 1675 CD1 TYR A 223 21.303 68.191 31.800 1.00 17.60 C ATOM 1676 CD2 TYR A 223 21.205 69.433 33.859 1.00 18.43 C ATOM 1677 CE1 TYR A 223 20.897 67.048 32.457 1.00 18.75 C ATOM 1678 CE2 TYR A 223 20.790 68.298 34.524 1.00 14.29 C ATOM 1679 CZ TYR A 223 20.643 67.119 33.813 1.00 17.21 C ATOM 1680 OH TYR A 223 20.170 65.983 34.441 1.00 18.56 O ATOM 1681 N ASP A 224 23.448 69.636 29.226 1.00 20.65 N ATOM 1682 CA ASP A 224 23.708 68.507 28.362 1.00 22.43 C ATOM 1683 C ASP A 224 25.185 68.404 28.088 1.00 21.52 C ATOM 1684 O ASP A 224 25.675 67.282 28.021 1.00 22.58 O ATOM 1685 CB ASP A 224 22.930 68.659 27.073 1.00 26.30 C ATOM 1686 CG ASP A 224 21.442 68.602 27.320 1.00 30.89 C ATOM 1687 OD1 ASP A 224 20.987 67.677 27.979 1.00 34.40 O ATOM 1688 OD2 ASP A 224 20.728 69.486 26.871 1.00 34.35 O ATOM 1689 N LYS A 225 25.928 69.509 28.005 1.00 21.51 N ATOM 1690 CA LYS A 225 27.358 69.448 27.828 1.00 23.29 C ATOM 1691 C LYS A 225 27.930 68.738 29.029 1.00 23.17 C ATOM 1692 O LYS A 225 28.824 67.907 28.881 1.00 23.90 O ATOM 1693 CB LYS A 225 28.086 70.767 27.860 1.00 29.23 C ATOM 1694 CG LYS A 225 27.651 71.904 27.003 1.00 38.95 C ATOM 1695 CD LYS A 225 28.150 71.824 25.580 1.00 47.14 C ATOM 1696 CE LYS A 225 28.337 73.277 25.114 1.00 53.17 C ATOM 1697 NZ LYS A 225 27.112 74.074 25.160 1.00 57.79 N ATOM 1698 N MET A 226 27.468 69.059 30.243 1.00 22.07 N ATOM 1699 CA MET A 226 28.022 68.430 31.430 1.00 21.54 C ATOM 1700 C MET A 226 27.655 66.942 31.552 1.00 19.88 C ATOM 1701 O MET A 226 28.500 66.098 31.881 1.00 18.59 O ATOM 1702 CB MET A 226 27.548 69.194 32.649 1.00 23.31 C ATOM 1703 CG MET A 226 28.230 70.550 32.806 1.00 27.53 C ATOM 1704 SD MET A 226 27.883 71.352 34.411 1.00 32.33 S ATOM 1705 CE MET A 226 26.130 71.539 34.310 1.00 29.69 C ATOM 1706 N ALA A 227 26.420 66.590 31.220 1.00 18.25 N ATOM 1707 CA ALA A 227 25.955 65.239 31.338 1.00 18.43 C ATOM 1708 C ALA A 227 26.687 64.277 30.394 1.00 22.54 C ATOM 1709 O ALA A 227 27.029 63.135 30.747 1.00 21.24 O ATOM 1710 CB ALA A 227 24.482 65.275 31.058 1.00 15.89 C ATOM 1711 N LYS A 228 27.029 64.784 29.198 1.00 23.50 N ATOM 1712 CA LYS A 228 27.711 63.999 28.170 1.00 23.94 C ATOM 1713 C LYS A 228 29.080 63.569 28.640 1.00 24.45 C ATOM 1714 O LYS A 228 29.615 62.584 28.142 1.00 25.16 O ATOM 1715 CB LYS A 228 27.866 64.820 26.870 1.00 23.59 C ATOM 1716 N LYS A 229 29.690 64.254 29.610 1.00 24.18 N ATOM 1717 CA LYS A 229 30.960 63.804 30.162 1.00 25.19 C ATOM 1718 C LYS A 229 30.834 62.454 30.897 1.00 23.08 C ATOM 1719 O LYS A 229 31.788 61.711 31.078 1.00 24.37 O ATOM 1720 CB LYS A 229 31.440 64.922 31.082 1.00 30.10 C ATOM 1721 CG LYS A 229 32.597 64.696 32.059 1.00 36.86 C ATOM 1722 CD LYS A 229 32.895 66.034 32.699 1.00 42.57 C ATOM 1723 CE LYS A 229 33.867 66.012 33.860 1.00 45.89 C ATOM 1724 NZ LYS A 229 33.758 67.276 34.589 1.00 46.43 N ATOM 1725 N TYR A 230 29.657 62.094 31.358 1.00 21.02 N ATOM 1726 CA TYR A 230 29.476 60.876 32.105 1.00 20.48 C ATOM 1727 C TYR A 230 28.535 59.885 31.436 1.00 22.44 C ATOM 1728 O TYR A 230 28.709 58.678 31.607 1.00 24.84 O ATOM 1729 CB TYR A 230 28.912 61.195 33.486 1.00 18.52 C ATOM 1730 CG TYR A 230 29.725 62.183 34.299 1.00 17.85 C ATOM 1731 CD1 TYR A 230 30.801 61.710 35.018 1.00 17.09 C ATOM 1732 CD2 TYR A 230 29.388 63.536 34.313 1.00 17.11 C ATOM 1733 CE1 TYR A 230 31.559 62.585 35.768 1.00 18.68 C ATOM 1734 CE2 TYR A 230 30.150 64.417 35.067 1.00 15.75 C ATOM 1735 CZ TYR A 230 31.230 63.934 35.786 1.00 17.58 C ATOM 1736 OH TYR A 230 32.031 64.776 36.526 1.00 17.85 O ATOM 1737 N PHE A 231 27.516 60.356 30.705 1.00 22.44 N ATOM 1738 CA PHE A 231 26.392 59.526 30.288 1.00 23.19 C ATOM 1739 C PHE A 231 26.167 59.615 28.800 1.00 25.38 C ATOM 1740 O PHE A 231 26.395 60.675 28.202 1.00 26.25 O ATOM 1741 CB PHE A 231 25.097 59.982 30.979 1.00 20.81 C ATOM 1742 CG PHE A 231 25.253 60.208 32.477 1.00 20.23 C ATOM 1743 CD1 PHE A 231 25.563 59.139 33.325 1.00 17.99 C ATOM 1744 CD2 PHE A 231 25.107 61.493 32.991 1.00 19.03 C ATOM 1745 CE1 PHE A 231 25.724 59.372 34.685 1.00 18.33 C ATOM 1746 CE2 PHE A 231 25.269 61.707 34.356 1.00 19.02 C ATOM 1747 CZ PHE A 231 25.583 60.651 35.203 1.00 18.14 C ATOM 1748 N ASP A 232 25.644 58.553 28.202 1.00 26.45 N ATOM 1749 CA ASP A 232 25.376 58.580 26.786 1.00 29.86 C ATOM 1750 C ASP A 232 23.881 58.378 26.569 1.00 29.52 C ATOM 1751 O ASP A 232 23.413 57.858 25.556 1.00 33.04 O ATOM 1752 CB ASP A 232 26.224 57.482 26.121 1.00 35.81 C ATOM 1753 CG ASP A 232 25.840 56.016 26.319 1.00 42.52 C ATOM 1754 OD1 ASP A 232 25.145 55.657 27.278 1.00 45.70 O ATOM 1755 OD2 ASP A 232 26.239 55.219 25.470 1.00 46.77 O ATOM 1756 N PHE A 233 23.072 58.706 27.562 1.00 26.95 N ATOM 1757 CA PHE A 233 21.623 58.547 27.493 1.00 24.89 C ATOM 1758 C PHE A 233 21.086 59.769 28.248 1.00 25.66 C ATOM 1759 O PHE A 233 21.874 60.454 28.931 1.00 25.02 O ATOM 1760 CB PHE A 233 21.203 57.289 28.214 1.00 26.06 C ATOM 1761 CG PHE A 233 21.709 57.181 29.659 1.00 25.59 C ATOM 1762 CD1 PHE A 233 22.971 56.668 29.901 1.00 24.04 C ATOM 1763 CD2 PHE A 233 20.901 57.611 30.698 1.00 26.12 C ATOM 1764 CE1 PHE A 233 23.425 56.605 31.189 1.00 24.57 C ATOM 1765 CE2 PHE A 233 21.378 57.542 31.980 1.00 23.77 C ATOM 1766 CZ PHE A 233 22.629 57.043 32.214 1.00 24.13 C ATOM 1767 N ASN A 234 19.803 60.091 28.229 1.00 23.98 N ATOM 1768 CA ASN A 234 19.318 61.251 28.936 1.00 26.79 C ATOM 1769 C ASN A 234 19.089 60.976 30.416 1.00 24.88 C ATOM 1770 O ASN A 234 18.129 60.368 30.854 1.00 25.61 O ATOM 1771 CB ASN A 234 18.086 61.702 28.168 1.00 29.07 C ATOM 1772 CG ASN A 234 16.998 62.468 28.898 1.00 32.13 C ATOM 1773 OD1 ASN A 234 15.846 62.027 28.849 1.00 37.05 O ATOM 1774 ND2 ASN A 234 17.160 63.598 29.554 1.00 31.95 N ATOM 1775 N VAL A 235 20.023 61.408 31.258 1.00 23.59 N ATOM 1776 CA VAL A 235 19.968 61.185 32.696 1.00 21.04 C ATOM 1777 C VAL A 235 18.826 61.978 33.326 1.00 20.80 C ATOM 1778 O VAL A 235 18.266 61.613 34.362 1.00 20.04 O ATOM 1779 CB VAL A 235 21.394 61.570 33.244 1.00 20.72 C ATOM 1780 CG1 VAL A 235 21.642 63.072 33.234 1.00 18.46 C ATOM 1781 CG2 VAL A 235 21.534 61.017 34.644 1.00 20.02 C ATOM 1782 N TYR A 236 18.448 63.091 32.718 1.00 19.94 N ATOM 1783 CA TYR A 236 17.432 63.926 33.293 1.00 18.69 C ATOM 1784 C TYR A 236 16.112 63.178 33.339 1.00 22.21 C ATOM 1785 O TYR A 236 15.291 63.424 34.216 1.00 20.62 O ATOM 1786 CB TYR A 236 17.376 65.192 32.443 1.00 17.90 C ATOM 1787 CG TYR A 236 16.414 66.193 33.019 1.00 19.16 C ATOM 1788 CD1 TYR A 236 16.809 66.993 34.083 1.00 19.98 C ATOM 1789 CD2 TYR A 236 15.151 66.275 32.466 1.00 21.14 C ATOM 1790 CE1 TYR A 236 15.918 67.879 34.636 1.00 19.79 C ATOM 1791 CE2 TYR A 236 14.254 67.154 33.016 1.00 23.95 C ATOM 1792 CZ TYR A 236 14.666 67.944 34.076 1.00 23.42 C ATOM 1793 OH TYR A 236 13.799 68.866 34.603 1.00 25.42 O ATOM 1794 N GLY A 237 15.948 62.172 32.474 1.00 26.25 N ATOM 1795 CA GLY A 237 14.670 61.532 32.250 1.00 32.94 C ATOM 1796 C GLY A 237 13.995 62.688 31.559 1.00 40.20 C ATOM 1797 O GLY A 237 14.636 63.388 30.767 1.00 43.31 O ATOM 1798 N ASP A 238 12.752 62.964 31.816 1.00 45.63 N ATOM 1799 CA ASP A 238 12.212 64.269 31.485 1.00 52.36 C ATOM 1800 C ASP A 238 10.887 64.247 32.186 1.00 53.39 C ATOM 1801 O ASP A 238 10.211 63.199 32.157 1.00 56.64 O ATOM 1802 CB ASP A 238 12.039 64.530 29.952 1.00 56.07 C ATOM 1803 CG ASP A 238 12.891 65.767 29.573 1.00 59.73 C ATOM 1804 OD1 ASP A 238 12.474 66.894 29.866 1.00 62.78 O ATOM 1805 OD2 ASP A 238 13.989 65.622 29.023 1.00 60.38 O TER 1806 ASP A 238 HETATM 1807 N LYS A 240 18.663 58.231 45.771 1.00 10.52 N HETATM 1808 CA LYS A 240 18.729 57.446 46.982 1.00 11.60 C HETATM 1809 C LYS A 240 18.141 58.287 48.141 1.00 13.99 C HETATM 1810 O LYS A 240 18.040 57.797 49.267 1.00 10.70 O HETATM 1811 CB LYS A 240 20.183 57.087 47.258 1.00 9.82 C HETATM 1812 CG LYS A 240 21.160 58.248 47.238 1.00 11.18 C HETATM 1813 CD LYS A 240 22.442 57.774 47.856 1.00 10.09 C HETATM 1814 CE LYS A 240 23.521 58.814 47.667 1.00 9.58 C HETATM 1815 NZ LYS A 240 24.756 58.442 48.359 1.00 12.40 N HETATM 1816 OXT LYS A 240 17.791 59.453 47.900 1.00 12.31 O HETATM 1817 O HOH A 401 20.737 65.844 45.608 1.00 11.65 O HETATM 1818 O HOH A 402 18.914 75.522 53.480 1.00 14.83 O HETATM 1819 O HOH A 403 25.554 61.475 44.768 1.00 12.89 O HETATM 1820 O HOH A 404 21.500 53.849 47.639 1.00 14.49 O HETATM 1821 O HOH A 405 27.624 57.479 53.221 1.00 12.10 O HETATM 1822 O HOH A 406 21.320 65.250 42.838 1.00 18.08 O HETATM 1823 O HOH A 407 16.035 44.893 40.162 1.00 17.72 O HETATM 1824 O HOH A 408 20.444 58.223 38.798 1.00 16.71 O HETATM 1825 O HOH A 409 19.500 55.652 38.735 1.00 14.92 O HETATM 1826 O HOH A 410 18.593 60.084 54.950 1.00 33.02 O HETATM 1827 O HOH A 411 15.196 56.939 45.408 1.00 16.25 O HETATM 1828 O HOH A 412 13.917 72.359 57.043 1.00 17.62 O HETATM 1829 O HOH A 413 26.044 76.133 57.248 1.00 18.73 O HETATM 1830 O HOH A 414 20.324 82.206 40.536 1.00 20.65 O HETATM 1831 O HOH A 415 15.980 55.437 43.212 1.00 15.95 O HETATM 1832 O HOH A 416 22.222 51.326 48.601 1.00 13.63 O HETATM 1833 O HOH A 417 30.824 72.791 36.985 1.00 24.79 O HETATM 1834 O HOH A 418 24.789 56.457 55.695 1.00 14.49 O HETATM 1835 O HOH A 419 28.343 53.902 42.879 1.00 21.14 O HETATM 1836 O HOH A 420 20.317 62.110 55.450 1.00 20.32 O HETATM 1837 O HOH A 421 17.534 55.605 36.355 1.00 27.49 O HETATM 1838 O HOH A 422 15.839 50.334 32.985 1.00 30.67 O HETATM 1839 O HOH A 423 27.035 55.907 49.464 1.00 22.31 O HETATM 1840 O HOH A 424 21.443 58.713 41.401 1.00 14.28 O HETATM 1841 O HOH A 425 14.235 70.654 36.584 1.00 19.47 O HETATM 1842 O HOH A 426 26.031 60.562 47.318 1.00 17.08 O HETATM 1843 O HOH A 427 29.074 43.985 34.690 1.00 29.82 O HETATM 1844 O HOH A 428 25.052 37.192 43.631 1.00 26.28 O HETATM 1845 O HOH A 429 34.198 73.228 56.123 1.00 25.00 O HETATM 1846 O HOH A 430 15.555 60.294 54.569 1.00 28.08 O HETATM 1847 O HOH A 431 12.429 69.774 59.943 1.00 32.03 O HETATM 1848 O HOH A 432 14.031 71.636 60.928 1.00 31.21 O HETATM 1849 O HOH A 433 12.794 53.055 40.949 1.00 25.35 O HETATM 1850 O HOH A 434 13.922 76.372 50.806 1.00 26.38 O HETATM 1851 O HOH A 435 18.668 58.982 35.235 1.00 32.12 O HETATM 1852 O HOH A 436 13.284 59.448 38.938 1.00 25.84 O HETATM 1853 O HOH A 437 14.348 48.184 34.092 1.00 22.71 O HETATM 1854 O HOH A 438 20.614 50.656 32.890 1.00 52.50 O HETATM 1855 O HOH A 439 17.306 81.544 51.838 1.00 23.49 O HETATM 1856 O HOH A 440 34.162 71.660 43.839 1.00 61.89 O HETATM 1857 O HOH A 441 14.613 75.158 37.956 1.00 26.11 O HETATM 1858 O HOH A 442 32.034 60.587 40.875 1.00 26.11 O HETATM 1859 O HOH A 443 8.005 58.918 50.812 1.00 29.24 O HETATM 1860 O HOH A 444 22.525 39.150 38.082 1.00 42.28 O HETATM 1861 O HOH A 445 22.062 46.422 59.381 1.00 26.33 O HETATM 1862 O HOH A 446 23.103 44.108 33.967 1.00 30.69 O HETATM 1863 O HOH A 447 10.127 71.366 48.118 1.00 27.98 O HETATM 1864 O HOH A 448 30.476 54.458 44.583 1.00 29.13 O HETATM 1865 O HOH A 449 10.997 70.013 43.449 1.00 29.90 O HETATM 1866 O HOH A 450 31.426 61.090 52.383 1.00 33.65 O HETATM 1867 O HOH A 451 26.657 56.278 58.866 1.00 36.37 O HETATM 1868 O HOH A 452 19.729 67.877 63.318 1.00 34.31 O HETATM 1869 O HOH A 453 34.383 75.970 56.698 1.00 33.59 O HETATM 1870 O HOH A 454 31.504 43.405 56.323 1.00 36.85 O HETATM 1871 O HOH A 455 18.035 41.599 58.665 1.00 40.16 O HETATM 1872 O HOH A 456 34.930 72.646 48.078 1.00 39.83 O HETATM 1873 O HOH A 457 42.243 60.205 40.209 1.00 58.02 O HETATM 1874 O HOH A 458 18.540 46.941 58.291 1.00 51.18 O HETATM 1875 O HOH A 459 17.658 78.672 57.497 1.00 25.69 O HETATM 1876 O HOH A 460 9.510 53.893 41.415 1.00 41.33 O HETATM 1877 O HOH A 461 14.234 59.092 42.677 1.00 25.80 O HETATM 1878 O HOH A 462 17.009 84.376 45.359 1.00 27.32 O HETATM 1879 O HOH A 463 14.559 73.392 35.949 1.00 35.11 O HETATM 1880 O HOH A 464 33.759 66.790 38.552 1.00 19.61 O HETATM 1881 O HOH A 465 21.156 82.707 38.097 1.00 35.45 O HETATM 1882 O HOH A 466 13.512 80.677 40.892 1.00 38.65 O HETATM 1883 O HOH A 467 31.546 77.529 41.312 1.00 36.52 O HETATM 1884 O HOH A 468 19.661 64.247 30.067 1.00 36.60 O HETATM 1885 O HOH A 469 16.093 54.947 55.307 1.00 26.21 O HETATM 1886 O HOH A 470 9.024 70.983 50.828 1.00 37.14 O HETATM 1887 O HOH A 471 15.518 57.668 55.878 1.00 52.71 O HETATM 1888 O HOH A 472 26.675 56.246 29.703 1.00 40.98 O HETATM 1889 O HOH A 473 10.872 57.078 51.027 1.00 41.98 O HETATM 1890 O HOH A 474 45.663 59.393 47.582 1.00 39.96 O HETATM 1891 O HOH A 475 34.660 67.700 53.651 1.00 41.92 O HETATM 1892 O HOH A 476 29.000 61.886 58.372 1.00 50.06 O HETATM 1893 O HOH A 477 26.709 53.835 61.430 1.00 52.48 O HETATM 1894 O HOH A 478 18.195 37.684 37.469 1.00 63.22 O HETATM 1895 O HOH A 479 32.626 78.837 44.772 1.00 55.03 O HETATM 1896 O HOH A 480 11.692 61.934 56.225 1.00 42.19 O HETATM 1897 O HOH A 481 9.871 42.806 46.160 1.00 37.88 O HETATM 1898 O HOH A 482 19.197 80.903 30.053 1.00 40.71 O HETATM 1899 O HOH A 483 12.083 61.541 37.675 1.00 41.72 O HETATM 1900 O HOH A 484 34.508 49.486 46.823 1.00 44.00 O HETATM 1901 O HOH A 485 15.005 39.473 58.296 1.00 26.80 O HETATM 1902 O HOH A 486 11.885 78.688 44.024 1.00 55.51 O HETATM 1903 O HOH A 487 33.071 71.085 38.907 1.00 36.60 O HETATM 1904 O HOH A 488 34.925 59.040 50.600 1.00 49.57 O HETATM 1905 O HOH A 489 14.604 82.870 52.539 1.00 40.32 O HETATM 1906 O HOH A 490 11.562 55.478 40.731 1.00 46.48 O HETATM 1907 O HOH A 491 39.333 65.192 50.608 1.00 46.55 O HETATM 1908 O HOH A 492 21.202 71.475 28.560 1.00 23.75 O HETATM 1909 O HOH A 493 22.569 48.198 31.836 1.00 61.29 O HETATM 1910 O HOH A 494 12.057 59.334 51.917 1.00 21.33 O HETATM 1911 O HOH A 495 27.312 41.739 55.454 1.00 40.78 O HETATM 1912 O HOH A 496 15.777 82.708 34.650 1.00 54.35 O HETATM 1913 O HOH A 497 19.747 84.514 42.094 1.00 41.79 O HETATM 1914 O HOH A 498 30.222 66.251 57.715 1.00 50.79 O HETATM 1915 O HOH A 499 24.312 53.216 32.338 1.00 46.44 O HETATM 1916 O HOH A 500 10.816 45.166 39.080 1.00 61.84 O HETATM 1917 O HOH A 501 11.462 41.392 38.661 1.00 69.31 O HETATM 1918 O HOH A 502 26.987 59.080 60.116 1.00 53.95 O HETATM 1919 O HOH A 503 37.247 69.267 46.501 1.00 48.77 O HETATM 1920 O HOH A 504 33.410 41.008 39.045 1.00 51.78 O HETATM 1921 O HOH A 505 22.884 33.627 51.223 1.00 82.89 O HETATM 1922 O HOH A 506 30.517 58.295 53.126 1.00 33.91 O HETATM 1923 O HOH A 507 29.211 59.302 27.262 1.00 59.36 O HETATM 1924 O HOH A 508 35.206 57.764 47.122 1.00 45.41 O HETATM 1925 O HOH A 510 31.256 55.927 54.926 1.00 45.88 O HETATM 1926 O HOH A 511 24.936 65.029 61.382 1.00 45.67 O HETATM 1927 O HOH A 512 24.045 71.351 24.616 1.00 40.62 O HETATM 1928 O HOH A 513 28.848 79.511 32.700 1.00 66.68 O HETATM 1929 O HOH A 514 10.778 49.369 35.497 1.00 71.73 O HETATM 1930 O HOH A 515 31.495 75.573 36.741 1.00 47.60 O HETATM 1931 O HOH A 516 32.362 56.149 37.979 1.00 65.56 O HETATM 1932 O HOH A 518 10.199 82.014 54.747 1.00 68.92 O HETATM 1933 O HOH A 519 12.498 33.734 55.685 1.00 75.12 O HETATM 1934 O HOH A 521 10.386 65.938 40.058 1.00 41.21 O HETATM 1935 O HOH A 522 35.073 69.632 55.734 1.00 56.00 O HETATM 1936 O HOH A 523 18.078 73.258 26.285 1.00 52.48 O HETATM 1937 O HOH A 525 10.372 68.507 41.343 1.00 49.48 O HETATM 1938 O HOH A 526 10.477 72.771 43.128 1.00 54.90 O HETATM 1939 O HOH A 527 32.700 45.975 33.295 1.00 69.92 O HETATM 1940 O HOH A 528 30.465 67.642 33.386 1.00 52.17 O HETATM 1941 O HOH A 529 33.221 57.269 53.532 1.00 57.41 O HETATM 1942 O HOH A 530 26.715 79.364 55.711 1.00 43.15 O HETATM 1943 O HOH A 531 8.989 62.494 57.511 1.00 55.77 O HETATM 1944 O HOH A 532 16.690 83.789 42.084 1.00 51.30 O HETATM 1945 O HOH A 534 22.644 37.769 35.504 1.00 50.33 O HETATM 1946 O HOH A 535 11.906 79.673 46.532 1.00 67.46 O HETATM 1947 O HOH A 536 18.681 67.285 29.538 1.00 46.08 O HETATM 1948 O HOH A 537 33.528 60.283 38.377 1.00 62.73 O HETATM 1949 O HOH A 538 35.250 68.721 40.281 1.00 41.55 O HETATM 1950 O HOH A 539 25.422 38.848 55.502 1.00 76.30 O HETATM 1951 O HOH A 540 18.881 60.675 57.836 1.00 64.51 O HETATM 1952 O HOH A 541 21.935 53.446 33.828 1.00 41.65 O HETATM 1953 O HOH A 542 6.301 69.146 45.270 1.00 71.23 O HETATM 1954 O HOH A 543 35.902 58.006 40.780 1.00 48.52 O HETATM 1955 O HOH A 544 4.619 52.571 42.030 1.00 57.01 O HETATM 1956 O HOH A 545 24.928 86.674 44.540 1.00 55.46 O HETATM 1957 O HOH A 547 41.364 59.890 47.619 1.00 55.57 O HETATM 1958 O HOH A 548 22.216 60.353 61.294 1.00 64.14 O HETATM 1959 O HOH A 549 39.170 68.238 48.619 1.00 54.79 O HETATM 1960 O HOH A 550 7.243 47.613 44.796 1.00 49.64 O HETATM 1961 O HOH A 551 22.990 51.107 63.150 1.00 51.14 O HETATM 1962 O HOH A 552 11.209 69.870 38.925 1.00 62.38 O HETATM 1963 O HOH A 553 17.759 66.003 63.126 1.00 68.13 O HETATM 1964 O HOH A 554 29.006 57.609 61.421 1.00 64.72 O HETATM 1965 O HOH A 556 11.014 76.486 50.463 1.00 53.04 O HETATM 1966 O HOH A 557 9.202 55.748 53.306 1.00 69.20 O HETATM 1967 O HOH A 558 36.150 71.191 49.958 1.00 74.33 O HETATM 1968 O HOH A 559 24.181 53.706 62.443 1.00 59.43 O HETATM 1969 O HOH A 560 22.272 52.455 30.085 1.00 70.23 O HETATM 1970 O HOH A 561 31.692 55.766 57.446 1.00 79.71 O HETATM 1971 O HOH A 562 23.517 81.987 33.545 1.00 61.21 O HETATM 1972 O HOH A 563 9.798 65.133 37.232 1.00 65.30 O HETATM 1973 O HOH A 564 8.372 47.427 40.593 1.00 62.34 O HETATM 1974 O HOH A 565 18.175 50.730 31.130 1.00 55.50 O HETATM 1975 O HOH A 566 27.288 82.846 34.930 1.00 59.71 O HETATM 1976 O HOH A 567 31.112 80.301 43.026 1.00 56.22 O HETATM 1977 O HOH A 568 26.285 34.959 46.556 1.00 82.53 O HETATM 1978 O HOH A 569 9.350 69.542 45.998 1.00 60.21 O HETATM 1979 O HOH A 570 26.260 44.237 33.765 1.00 54.60 O HETATM 1980 O HOH A 571 28.035 37.591 45.471 1.00 59.76 O HETATM 1981 O HOH A 572 15.888 36.983 34.207 1.00 70.58 O HETATM 1982 O HOH A 573 11.651 61.573 34.720 1.00 56.97 O HETATM 1983 O HOH A 574 29.872 40.658 56.780 1.00 66.67 O HETATM 1984 O HOH A 575 23.653 67.043 63.696 1.00 58.02 O HETATM 1985 O HOH A 576 33.588 50.869 30.583 1.00 81.86 O HETATM 1986 O HOH A 577 34.951 71.489 53.771 1.00 63.75 O HETATM 1987 O HOH A 578 21.744 64.864 28.541 1.00 65.33 O HETATM 1988 O HOH A 579 30.851 74.293 33.168 1.00 68.47 O HETATM 1989 O HOH A 580 34.056 38.948 42.416 1.00 57.72 O HETATM 1990 O HOH A 581 36.353 69.677 43.500 1.00 74.22 O HETATM 1991 O HOH A 583 19.974 51.868 60.533 1.00 65.35 O HETATM 1992 O HOH A 584 19.063 54.687 32.574 1.00 63.67 O HETATM 1993 O HOH A 586 19.686 72.255 23.632 1.00 80.10 O HETATM 1994 O HOH A 587 17.428 71.120 28.598 1.00 56.33 O HETATM 1995 O HOH A 588 24.025 65.098 26.802 1.00 69.83 O HETATM 1996 O HOH A 589 28.887 34.866 37.832 1.00 60.97 O HETATM 1997 O HOH A 590 33.421 51.907 44.640 1.00 72.95 O HETATM 1998 O HOH A 592 30.379 57.471 33.995 1.00 50.35 O HETATM 1999 O HOH A 593 11.878 75.919 34.602 1.00 63.86 O HETATM 2000 O HOH A 594 36.528 43.109 48.768 1.00 67.97 O HETATM 2001 O HOH A 596 14.121 52.483 34.679 1.00 64.64 O HETATM 2002 O HOH A 598 24.287 78.610 57.694 1.00 75.94 O HETATM 2003 O HOH A 599 27.416 81.998 31.423 1.00 68.14 O HETATM 2004 O HOH A 600 9.535 53.378 55.633 1.00 68.15 O HETATM 2005 O HOH A 601 8.626 83.164 57.408 1.00 71.48 O HETATM 2006 O HOH A 602 18.094 58.366 27.054 1.00 57.57 O HETATM 2007 O HOH A 604 25.314 48.605 32.844 1.00 70.80 O HETATM 2008 O HOH A 605 34.778 52.465 54.172 1.00 74.85 O HETATM 2009 O HOH A 606 1.474 40.308 55.070 1.00 62.11 O HETATM 2010 O HOH A 607 32.768 58.845 34.177 1.00 57.07 O HETATM 2011 O HOH A 608 13.564 51.283 57.999 1.00 84.87 O HETATM 2012 O HOH A 611 16.726 58.613 32.906 1.00 62.15 O HETATM 2013 O HOH A 612 25.733 85.149 36.836 1.00 67.75 O HETATM 2014 O HOH A 613 35.911 42.254 41.855 1.00 61.32 O HETATM 2015 O HOH A 615 23.139 34.579 43.264 1.00 85.05 O CONECT 283 342 CONECT 342 283 MASTER 314 0 1 10 10 0 4 6 2014 1 2 19 END If you find results from this site helpful for your research, please cite one of our papers:
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