HEADER LIGASE 27-SEP-99 1D2R TITLE 2.9 A CRYSTAL STRUCTURE OF LIGAND-FREE TRYPTOPHANYL-TRNA TITLE 2 SYNTHETASE: DOMAIN MOVEMENTS FRAGMENT THE ADENINE TITLE 3 NUCLEOTIDE BINDING SITE. COMPND MOL_ID: 1; COMPND 2 MOLECULE: TRYPTOPHANYL TRNA SYNTHETASE; COMPND 3 CHAIN: A, B, C, D, E, F; COMPND 4 SYNONYM: TRPRS; COMPND 5 EC: 6.1.1.2 SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS STEAROTHERMOPHILUS; SOURCE 3 ORGANISM_COMMON: BACTERIA KEYWDS CLASS I TRNA SYNTHETASE, AARS, INDUCED FIT, TRPRS EXPDTA X-RAY DIFFRACTION AUTHOR V.A.ILYIN,C.W.CARTER JR. REVDAT 1 05-APR-00 1D2R 0 JRNL AUTH V.A.ILYIN,B.TEMPLE,G.-P.LI,Y.P.VACHETTE, JRNL AUTH 2 C.W.CARTER JR. JRNL TITL 2.9 A CRYSTAL STRUCTURE OF LIGAND-FREE JRNL TITL 2 TRYPTOPHANYL-TRNA SYNTHETASE: DOMAIN MOVEMENTS JRNL TITL 3 FRAGMENT THE ADENINE NUCLEOTIDE BINDING SITE. JRNL REF PROTEIN SCI. V. 9 218 2000 JRNL REFN ASTM PRCIEI US ISSN 0961-8368 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 2.90 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 0.9 REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE- REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU, REMARK 3 : READ,RICE,SIMONSON,WARREN REMARK 3 REMARK 3 REFINEMENT TARGET : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 OUTLIER CUTOFF HIGH (RMS(ABS(F))) : NULL REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 74.3 REMARK 3 NUMBER OF REFLECTIONS : 38244 REMARK 3 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING SET) : 0.237 REMARK 3 FREE R VALUE : 0.262 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 1929 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 6 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.90 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.08 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 51.20 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4172 REMARK 3 BIN R VALUE (WORKING SET) : 0.3440 REMARK 3 BIN FREE R VALUE : 0.3270 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.60 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 201 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.023 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 15480 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 0 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 45.60 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 49.60 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 9.88000 REMARK 3 B22 (A**2) : -7.04000 REMARK 3 B33 (A**2) : -2.83000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 14.23000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.41 REMARK 3 ESD FROM SIGMAA (A) : 0.520 REMARK 3 LOW RESOLUTION CUTOFF (A) : 10.00 REMARK 3 REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.46 REMARK 3 ESD FROM C-V SIGMAA (A) : 0.57 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.009 REMARK 3 BOND ANGLES (DEGREES) : 1.20 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.70 REMARK 3 IMPROPER ANGLES (DEGREES) : 0.84 REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : 2.10 ; 1.500 REMARK 3 MAIN-CHAIN ANGLE (A**2) : 3.65 ; 2.000 REMARK 3 SIDE-CHAIN BOND (A**2) : 2.77 ; 2.000 REMARK 3 SIDE-CHAIN ANGLE (A**2) : 4.57 ; 2.500 REMARK 3 REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED : FLAT MODEL REMARK 3 KSOL : 0.35 REMARK 3 BSOL : 38.32 REMARK 3 REMARK 3 NCS MODEL : CONSTR 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 : CNS_TOPPAR/PROTEIN_REP.PA REMARK 3 TOPOLOGY FILE 1 : CNS_TOPPAR/PROTEIN.TOP REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1D2R COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-SEP-1999. REMARK 100 THE RCSB ID CODE IS RCSB009741. 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 : 6.80 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : N REMARK 200 RADIATION SOURCE : ROTATING ANODE REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU200H REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418 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 : DENZO REMARK 200 DATA SCALING SOFTWARE : R-AXIS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38244 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900 REMARK 200 RESOLUTION RANGE LOW (A) : 18.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : NULL REMARK 200 DATA REDUNDANCY : 1.800 REMARK 200 R MERGE (I) : 0.09100 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: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL REMARK 200 SOFTWARE USED: RSREF, MICE REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): NULL REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 2.0 M K2HPO4 REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 1/2+X,1/2+Y,Z REMARK 290 4555 1/2-X,1/2+Y,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 113.38000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 45.83000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 113.38000 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 45.83000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2, 3 REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT REMARK 300 WHICH CONSISTS OF 6 CHAIN(S). SEE REMARK 350 FOR REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S). REMARK 350 REMARK 350 GENERATING THE BIOMOLECULE 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 APPLY THE FOLLOWING TO CHAINS: A, D REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMOLECULE: 2 REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, E REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMOLECULE: 3 REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, F REMARK 350 BIOMT1 3 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 3 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000 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),F6.3) REMARK 500 REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 ILE A 45 CB ILE A 45 CA 0.056 REMARK 500 GLU A 233 C GLU A 233 CA 0.068 REMARK 500 PRO B 177 CD PRO B 177 CG 0.099 REMARK 500 VAL B 179 CB VAL B 179 CA 0.080 REMARK 500 GLU B 233 C GLU B 233 CA 0.060 REMARK 500 MET B 322 CE MET B 322 SD -0.070 REMARK 500 MET C 1 CE MET C 1 SD 0.058 REMARK 500 MET C 318 CE MET C 318 SD -0.068 REMARK 500 MET E 1 CE MET E 1 SD 0.057 REMARK 500 MET F 1 CE MET F 1 SD 0.060 REMARK 500 MET F 92 SD MET F 92 CG -0.067 REMARK 500 GLU F 233 C GLU F 233 CA 0.059 REMARK 500 MET F 322 CE MET F 322 SD -0.064 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: ENGH AND HUBER, 1991 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 ALA A 234 CA - C - N ANGL. DEV. =-16.0 DEGREES REMARK 500 ALA A 234 O - C - N ANGL. DEV. = 15.3 DEGREES REMARK 500 GLY B 12 N - CA - C ANGL. DEV. = 8.7 DEGREES REMARK 500 VAL B 179 N - CA - C ANGL. DEV. = 12.9 DEGREES REMARK 500 VAL B 179 CA - C - N ANGL. DEV. = 9.4 DEGREES REMARK 500 VAL B 179 O - C - N ANGL. DEV. =-21.1 DEGREES REMARK 500 ALA B 234 CA - C - N ANGL. DEV. =-15.2 DEGREES REMARK 500 ALA B 234 O - C - N ANGL. DEV. = 14.5 DEGREES REMARK 500 ILE C 176 N - CA - C ANGL. DEV. = -9.0 DEGREES REMARK 500 GLY C 180 N - CA - C ANGL. DEV. =-13.5 DEGREES REMARK 500 ALA C 181 N - CA - C ANGL. DEV. = -7.5 DEGREES REMARK 500 ALA C 234 CA - C - N ANGL. DEV. =-16.1 DEGREES REMARK 500 ALA C 234 O - C - N ANGL. DEV. = 15.1 DEGREES REMARK 500 ALA D 181 N - CA - C ANGL. DEV. = 7.9 DEGREES REMARK 500 ALA D 234 CA - C - N ANGL. DEV. =-16.7 DEGREES REMARK 500 ALA D 234 O - C - N ANGL. DEV. = 15.9 DEGREES REMARK 500 GLY E 180 N - CA - C ANGL. DEV. = -9.0 DEGREES REMARK 500 ALA E 234 CA - C - N ANGL. DEV. =-16.7 DEGREES REMARK 500 ALA E 234 O - C - N ANGL. DEV. = 15.4 DEGREES REMARK 500 GLY F 180 N - CA - C ANGL. DEV. =-14.4 DEGREES REMARK 500 ALA F 234 CA - C - N ANGL. DEV. =-15.7 DEGREES REMARK 500 ALA F 234 O - C - N ANGL. DEV. = 12.7 DEGREES 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 M RES CSSEQI PSI PHI REMARK 500 VAL A 179 47.47 -94.78 REMARK 500 VAL B 179 6.30 62.11 DBREF 1D2R A 1 326 GB 68506 YWBSF 1 326 DBREF 1D2R B 1 326 GB 68506 YWBSF 1 326 DBREF 1D2R C 1 326 GB 68506 YWBSF 1 326 DBREF 1D2R D 1 326 GB 68506 YWBSF 1 326 DBREF 1D2R E 1 326 GB 68506 YWBSF 1 326 DBREF 1D2R F 1 326 GB 68506 YWBSF 1 326 SEQRES 1 A 326 MET LYS THR ILE PHE SER GLY ILE GLN PRO SER GLY VAL SEQRES 2 A 326 ILE THR ILE GLY ASN TYR ILE GLY ALA LEU ARG GLN PHE SEQRES 3 A 326 VAL GLU LEU GLN HIS GLU TYR ASN CYS TYR PHE CYS ILE SEQRES 4 A 326 VAL ASP GLN HIS ALA ILE THR VAL TRP GLN ASP PRO HIS SEQRES 5 A 326 GLU LEU ARG GLN ASN ILE ARG ARG LEU ALA ALA LEU TYR SEQRES 6 A 326 LEU ALA VAL GLY ILE ASP PRO THR GLN ALA THR LEU PHE SEQRES 7 A 326 ILE GLN SER GLU VAL PRO ALA HIS ALA GLN ALA ALA TRP SEQRES 8 A 326 MET LEU GLN CYS ILE VAL TYR ILE GLY GLU LEU GLU ARG SEQRES 9 A 326 MET THR GLN PHE LYS GLU LYS SER ALA GLY ALA ALA ALA SEQRES 10 A 326 ALA ALA ALA GLY LEU LEU THR TYR PRO PRO LEU MET ALA SEQRES 11 A 326 ALA ASP ILE LEU LEU TYR ASN THR ASP ILE VAL PRO VAL SEQRES 12 A 326 GLY GLU ASP GLN LYS GLN HIS ILE GLU LEU THR ARG ASP SEQRES 13 A 326 LEU ALA GLU ARG PHE ASN LYS ARG TYR GLY GLU LEU PHE SEQRES 14 A 326 THR ILE PRO GLU ALA ARG ILE PRO LYS VAL GLY ALA ARG SEQRES 15 A 326 ILE MET SER LEU VAL ASP PRO THR LYS LYS MET SER LYS SEQRES 16 A 326 SER ASP PRO ASN PRO LYS ALA TYR ILE THR LEU LEU ASP SEQRES 17 A 326 ASP ALA LYS THR ILE GLU LYS LYS ILE LYS SER ALA VAL SEQRES 18 A 326 THR ASP SER GLU GLY THR ILE ARG TYR ASP LYS GLU ALA SEQRES 19 A 326 LYS PRO GLY ILE SER ASN LEU LEU ASN ILE TYR SER THR SEQRES 20 A 326 LEU SER GLY GLN SER ILE GLU GLU LEU GLU ARG GLN TYR SEQRES 21 A 326 GLU GLY LYS GLY TYR GLY VAL PHE LYS ALA ASP LEU ALA SEQRES 22 A 326 GLN VAL VAL ILE GLU THR LEU ARG PRO ILE GLN GLU ARG SEQRES 23 A 326 TYR HIS HIS TRP MET GLU SER GLU GLU LEU ASP ARG VAL SEQRES 24 A 326 LEU ASP GLU GLY ALA GLU LYS ALA ASN ARG VAL ALA SER SEQRES 25 A 326 GLU MET VAL ARG LYS MET GLU GLN ALA MET GLY LEU GLY SEQRES 26 A 326 ARG SEQRES 1 B 326 MET LYS THR ILE PHE SER GLY ILE GLN PRO SER GLY VAL SEQRES 2 B 326 ILE THR ILE GLY ASN TYR ILE GLY ALA LEU ARG GLN PHE SEQRES 3 B 326 VAL GLU LEU GLN HIS GLU TYR ASN CYS TYR PHE CYS ILE SEQRES 4 B 326 VAL ASP GLN HIS ALA ILE THR VAL TRP GLN ASP PRO HIS SEQRES 5 B 326 GLU LEU ARG GLN ASN ILE ARG ARG LEU ALA ALA LEU TYR SEQRES 6 B 326 LEU ALA VAL GLY ILE ASP PRO THR GLN ALA THR LEU PHE SEQRES 7 B 326 ILE GLN SER GLU VAL PRO ALA HIS ALA GLN ALA ALA TRP SEQRES 8 B 326 MET LEU GLN CYS ILE VAL TYR ILE GLY GLU LEU GLU ARG SEQRES 9 B 326 MET THR GLN PHE LYS GLU LYS SER ALA GLY ALA ALA ALA SEQRES 10 B 326 ALA ALA ALA GLY LEU LEU THR TYR PRO PRO LEU MET ALA SEQRES 11 B 326 ALA ASP ILE LEU LEU TYR ASN THR ASP ILE VAL PRO VAL SEQRES 12 B 326 GLY GLU ASP GLN LYS GLN HIS ILE GLU LEU THR ARG ASP SEQRES 13 B 326 LEU ALA GLU ARG PHE ASN LYS ARG TYR GLY GLU LEU PHE SEQRES 14 B 326 THR ILE PRO GLU ALA ARG ILE PRO LYS VAL GLY ALA ARG SEQRES 15 B 326 ILE MET SER LEU VAL ASP PRO THR LYS LYS MET SER LYS SEQRES 16 B 326 SER ASP PRO ASN PRO LYS ALA TYR ILE THR LEU LEU ASP SEQRES 17 B 326 ASP ALA LYS THR ILE GLU LYS LYS ILE LYS SER ALA VAL SEQRES 18 B 326 THR ASP SER GLU GLY THR ILE ARG TYR ASP LYS GLU ALA SEQRES 19 B 326 LYS PRO GLY ILE SER ASN LEU LEU ASN ILE TYR SER THR SEQRES 20 B 326 LEU SER GLY GLN SER ILE GLU GLU LEU GLU ARG GLN TYR SEQRES 21 B 326 GLU GLY LYS GLY TYR GLY VAL PHE LYS ALA ASP LEU ALA SEQRES 22 B 326 GLN VAL VAL ILE GLU THR LEU ARG PRO ILE GLN GLU ARG SEQRES 23 B 326 TYR HIS HIS TRP MET GLU SER GLU GLU LEU ASP ARG VAL SEQRES 24 B 326 LEU ASP GLU GLY ALA GLU LYS ALA ASN ARG VAL ALA SER SEQRES 25 B 326 GLU MET VAL ARG LYS MET GLU GLN ALA MET GLY LEU GLY SEQRES 26 B 326 ARG SEQRES 1 C 326 MET LYS THR ILE PHE SER GLY ILE GLN PRO SER GLY VAL SEQRES 2 C 326 ILE THR ILE GLY ASN TYR ILE GLY ALA LEU ARG GLN PHE SEQRES 3 C 326 VAL GLU LEU GLN HIS GLU TYR ASN CYS TYR PHE CYS ILE SEQRES 4 C 326 VAL ASP GLN HIS ALA ILE THR VAL TRP GLN ASP PRO HIS SEQRES 5 C 326 GLU LEU ARG GLN ASN ILE ARG ARG LEU ALA ALA LEU TYR SEQRES 6 C 326 LEU ALA VAL GLY ILE ASP PRO THR GLN ALA THR LEU PHE SEQRES 7 C 326 ILE GLN SER GLU VAL PRO ALA HIS ALA GLN ALA ALA TRP SEQRES 8 C 326 MET LEU GLN CYS ILE VAL TYR ILE GLY GLU LEU GLU ARG SEQRES 9 C 326 MET THR GLN PHE LYS GLU LYS SER ALA GLY ALA ALA ALA SEQRES 10 C 326 ALA ALA ALA GLY LEU LEU THR TYR PRO PRO LEU MET ALA SEQRES 11 C 326 ALA ASP ILE LEU LEU TYR ASN THR ASP ILE VAL PRO VAL SEQRES 12 C 326 GLY GLU ASP GLN LYS GLN HIS ILE GLU LEU THR ARG ASP SEQRES 13 C 326 LEU ALA GLU ARG PHE ASN LYS ARG TYR GLY GLU LEU PHE SEQRES 14 C 326 THR ILE PRO GLU ALA ARG ILE PRO LYS VAL GLY ALA ARG SEQRES 15 C 326 ILE MET SER LEU VAL ASP PRO THR LYS LYS MET SER LYS SEQRES 16 C 326 SER ASP PRO ASN PRO LYS ALA TYR ILE THR LEU LEU ASP SEQRES 17 C 326 ASP ALA LYS THR ILE GLU LYS LYS ILE LYS SER ALA VAL SEQRES 18 C 326 THR ASP SER GLU GLY THR ILE ARG TYR ASP LYS GLU ALA SEQRES 19 C 326 LYS PRO GLY ILE SER ASN LEU LEU ASN ILE TYR SER THR SEQRES 20 C 326 LEU SER GLY GLN SER ILE GLU GLU LEU GLU ARG GLN TYR SEQRES 21 C 326 GLU GLY LYS GLY TYR GLY VAL PHE LYS ALA ASP LEU ALA SEQRES 22 C 326 GLN VAL VAL ILE GLU THR LEU ARG PRO ILE GLN GLU ARG SEQRES 23 C 326 TYR HIS HIS TRP MET GLU SER GLU GLU LEU ASP ARG VAL SEQRES 24 C 326 LEU ASP GLU GLY ALA GLU LYS ALA ASN ARG VAL ALA SER SEQRES 25 C 326 GLU MET VAL ARG LYS MET GLU GLN ALA MET GLY LEU GLY SEQRES 26 C 326 ARG SEQRES 1 D 326 MET LYS THR ILE PHE SER GLY ILE GLN PRO SER GLY VAL SEQRES 2 D 326 ILE THR ILE GLY ASN TYR ILE GLY ALA LEU ARG GLN PHE SEQRES 3 D 326 VAL GLU LEU GLN HIS GLU TYR ASN CYS TYR PHE CYS ILE SEQRES 4 D 326 VAL ASP GLN HIS ALA ILE THR VAL TRP GLN ASP PRO HIS SEQRES 5 D 326 GLU LEU ARG GLN ASN ILE ARG ARG LEU ALA ALA LEU TYR SEQRES 6 D 326 LEU ALA VAL GLY ILE ASP PRO THR GLN ALA THR LEU PHE SEQRES 7 D 326 ILE GLN SER GLU VAL PRO ALA HIS ALA GLN ALA ALA TRP SEQRES 8 D 326 MET LEU GLN CYS ILE VAL TYR ILE GLY GLU LEU GLU ARG SEQRES 9 D 326 MET THR GLN PHE LYS GLU LYS SER ALA GLY ALA ALA ALA SEQRES 10 D 326 ALA ALA ALA GLY LEU LEU THR TYR PRO PRO LEU MET ALA SEQRES 11 D 326 ALA ASP ILE LEU LEU TYR ASN THR ASP ILE VAL PRO VAL SEQRES 12 D 326 GLY GLU ASP GLN LYS GLN HIS ILE GLU LEU THR ARG ASP SEQRES 13 D 326 LEU ALA GLU ARG PHE ASN LYS ARG TYR GLY GLU LEU PHE SEQRES 14 D 326 THR ILE PRO GLU ALA ARG ILE PRO LYS VAL GLY ALA ARG SEQRES 15 D 326 ILE MET SER LEU VAL ASP PRO THR LYS LYS MET SER LYS SEQRES 16 D 326 SER ASP PRO ASN PRO LYS ALA TYR ILE THR LEU LEU ASP SEQRES 17 D 326 ASP ALA LYS THR ILE GLU LYS LYS ILE LYS SER ALA VAL SEQRES 18 D 326 THR ASP SER GLU GLY THR ILE ARG TYR ASP LYS GLU ALA SEQRES 19 D 326 LYS PRO GLY ILE SER ASN LEU LEU ASN ILE TYR SER THR SEQRES 20 D 326 LEU SER GLY GLN SER ILE GLU GLU LEU GLU ARG GLN TYR SEQRES 21 D 326 GLU GLY LYS GLY TYR GLY VAL PHE LYS ALA ASP LEU ALA SEQRES 22 D 326 GLN VAL VAL ILE GLU THR LEU ARG PRO ILE GLN GLU ARG SEQRES 23 D 326 TYR HIS HIS TRP MET GLU SER GLU GLU LEU ASP ARG VAL SEQRES 24 D 326 LEU ASP GLU GLY ALA GLU LYS ALA ASN ARG VAL ALA SER SEQRES 25 D 326 GLU MET VAL ARG LYS MET GLU GLN ALA MET GLY LEU GLY SEQRES 26 D 326 ARG SEQRES 1 E 326 MET LYS THR ILE PHE SER GLY ILE GLN PRO SER GLY VAL SEQRES 2 E 326 ILE THR ILE GLY ASN TYR ILE GLY ALA LEU ARG GLN PHE SEQRES 3 E 326 VAL GLU LEU GLN HIS GLU TYR ASN CYS TYR PHE CYS ILE SEQRES 4 E 326 VAL ASP GLN HIS ALA ILE THR VAL TRP GLN ASP PRO HIS SEQRES 5 E 326 GLU LEU ARG GLN ASN ILE ARG ARG LEU ALA ALA LEU TYR SEQRES 6 E 326 LEU ALA VAL GLY ILE ASP PRO THR GLN ALA THR LEU PHE SEQRES 7 E 326 ILE GLN SER GLU VAL PRO ALA HIS ALA GLN ALA ALA TRP SEQRES 8 E 326 MET LEU GLN CYS ILE VAL TYR ILE GLY GLU LEU GLU ARG SEQRES 9 E 326 MET THR GLN PHE LYS GLU LYS SER ALA GLY ALA ALA ALA SEQRES 10 E 326 ALA ALA ALA GLY LEU LEU THR TYR PRO PRO LEU MET ALA SEQRES 11 E 326 ALA ASP ILE LEU LEU TYR ASN THR ASP ILE VAL PRO VAL SEQRES 12 E 326 GLY GLU ASP GLN LYS GLN HIS ILE GLU LEU THR ARG ASP SEQRES 13 E 326 LEU ALA GLU ARG PHE ASN LYS ARG TYR GLY GLU LEU PHE SEQRES 14 E 326 THR ILE PRO GLU ALA ARG ILE PRO LYS VAL GLY ALA ARG SEQRES 15 E 326 ILE MET SER LEU VAL ASP PRO THR LYS LYS MET SER LYS SEQRES 16 E 326 SER ASP PRO ASN PRO LYS ALA TYR ILE THR LEU LEU ASP SEQRES 17 E 326 ASP ALA LYS THR ILE GLU LYS LYS ILE LYS SER ALA VAL SEQRES 18 E 326 THR ASP SER GLU GLY THR ILE ARG TYR ASP LYS GLU ALA SEQRES 19 E 326 LYS PRO GLY ILE SER ASN LEU LEU ASN ILE TYR SER THR SEQRES 20 E 326 LEU SER GLY GLN SER ILE GLU GLU LEU GLU ARG GLN TYR SEQRES 21 E 326 GLU GLY LYS GLY TYR GLY VAL PHE LYS ALA ASP LEU ALA SEQRES 22 E 326 GLN VAL VAL ILE GLU THR LEU ARG PRO ILE GLN GLU ARG SEQRES 23 E 326 TYR HIS HIS TRP MET GLU SER GLU GLU LEU ASP ARG VAL SEQRES 24 E 326 LEU ASP GLU GLY ALA GLU LYS ALA ASN ARG VAL ALA SER SEQRES 25 E 326 GLU MET VAL ARG LYS MET GLU GLN ALA MET GLY LEU GLY SEQRES 26 E 326 ARG SEQRES 1 F 326 MET LYS THR ILE PHE SER GLY ILE GLN PRO SER GLY VAL SEQRES 2 F 326 ILE THR ILE GLY ASN TYR ILE GLY ALA LEU ARG GLN PHE SEQRES 3 F 326 VAL GLU LEU GLN HIS GLU TYR ASN CYS TYR PHE CYS ILE SEQRES 4 F 326 VAL ASP GLN HIS ALA ILE THR VAL TRP GLN ASP PRO HIS SEQRES 5 F 326 GLU LEU ARG GLN ASN ILE ARG ARG LEU ALA ALA LEU TYR SEQRES 6 F 326 LEU ALA VAL GLY ILE ASP PRO THR GLN ALA THR LEU PHE SEQRES 7 F 326 ILE GLN SER GLU VAL PRO ALA HIS ALA GLN ALA ALA TRP SEQRES 8 F 326 MET LEU GLN CYS ILE VAL TYR ILE GLY GLU LEU GLU ARG SEQRES 9 F 326 MET THR GLN PHE LYS GLU LYS SER ALA GLY ALA ALA ALA SEQRES 10 F 326 ALA ALA ALA GLY LEU LEU THR TYR PRO PRO LEU MET ALA SEQRES 11 F 326 ALA ASP ILE LEU LEU TYR ASN THR ASP ILE VAL PRO VAL SEQRES 12 F 326 GLY GLU ASP GLN LYS GLN HIS ILE GLU LEU THR ARG ASP SEQRES 13 F 326 LEU ALA GLU ARG PHE ASN LYS ARG TYR GLY GLU LEU PHE SEQRES 14 F 326 THR ILE PRO GLU ALA ARG ILE PRO LYS VAL GLY ALA ARG SEQRES 15 F 326 ILE MET SER LEU VAL ASP PRO THR LYS LYS MET SER LYS SEQRES 16 F 326 SER ASP PRO ASN PRO LYS ALA TYR ILE THR LEU LEU ASP SEQRES 17 F 326 ASP ALA LYS THR ILE GLU LYS LYS ILE LYS SER ALA VAL SEQRES 18 F 326 THR ASP SER GLU GLY THR ILE ARG TYR ASP LYS GLU ALA SEQRES 19 F 326 LYS PRO GLY ILE SER ASN LEU LEU ASN ILE TYR SER THR SEQRES 20 F 326 LEU SER GLY GLN SER ILE GLU GLU LEU GLU ARG GLN TYR SEQRES 21 F 326 GLU GLY LYS GLY TYR GLY VAL PHE LYS ALA ASP LEU ALA SEQRES 22 F 326 GLN VAL VAL ILE GLU THR LEU ARG PRO ILE GLN GLU ARG SEQRES 23 F 326 TYR HIS HIS TRP MET GLU SER GLU GLU LEU ASP ARG VAL SEQRES 24 F 326 LEU ASP GLU GLY ALA GLU LYS ALA ASN ARG VAL ALA SER SEQRES 25 F 326 GLU MET VAL ARG LYS MET GLU GLN ALA MET GLY LEU GLY SEQRES 26 F 326 ARG HELIX 1 1 THR A 15 ALA A 22 1 8 HELIX 2 2 ALA A 22 TYR A 33 1 12 HELIX 3 3 HIS A 43 VAL A 47 5 5 HELIX 4 4 ASP A 50 GLY A 69 1 20 HELIX 5 5 SER A 81 VAL A 83 5 3 HELIX 6 6 PRO A 84 CYS A 95 1 12 HELIX 7 7 TYR A 98 ARG A 104 1 7 HELIX 8 8 MET A 105 SER A 112 1 8 HELIX 9 9 ALA A 120 LEU A 135 1 16 HELIX 10 10 GLN A 147 GLY A 166 1 20 HELIX 11 11 ASN A 199 TYR A 203 5 5 HELIX 12 12 ASP A 209 ALA A 220 1 12 HELIX 13 13 LYS A 235 GLY A 250 1 16 HELIX 14 14 SER A 252 TYR A 260 1 9 HELIX 15 15 GLY A 264 GLU A 292 1 29 HELIX 16 16 GLU A 294 GLY A 323 1 30 HELIX 17 17 THR B 15 ALA B 22 1 8 HELIX 18 18 ALA B 22 TYR B 33 1 12 HELIX 19 19 HIS B 43 VAL B 47 5 5 HELIX 20 20 ASP B 50 GLY B 69 1 20 HELIX 21 21 SER B 81 VAL B 83 5 3 HELIX 22 22 PRO B 84 CYS B 95 1 12 HELIX 23 23 TYR B 98 ARG B 104 1 7 HELIX 24 24 MET B 105 SER B 112 1 8 HELIX 25 25 ALA B 120 LEU B 135 1 16 HELIX 26 26 GLN B 147 GLY B 166 1 20 HELIX 27 27 ASN B 199 TYR B 203 5 5 HELIX 28 28 ASP B 209 ALA B 220 1 12 HELIX 29 29 LYS B 235 GLY B 250 1 16 HELIX 30 30 SER B 252 TYR B 260 1 9 HELIX 31 31 GLY B 264 GLU B 292 1 29 HELIX 32 32 GLU B 294 GLY B 323 1 30 HELIX 33 33 THR C 15 ALA C 22 1 8 HELIX 34 34 ALA C 22 TYR C 33 1 12 HELIX 35 35 VAL C 40 ILE C 45 1 6 HELIX 36 36 ASP C 50 GLY C 69 1 20 HELIX 37 37 SER C 81 VAL C 83 5 3 HELIX 38 38 PRO C 84 CYS C 95 1 12 HELIX 39 39 TYR C 98 ARG C 104 1 7 HELIX 40 40 MET C 105 SER C 112 1 8 HELIX 41 41 ALA C 120 LEU C 135 1 16 HELIX 42 42 GLN C 147 GLY C 166 1 20 HELIX 43 43 ASN C 199 TYR C 203 5 5 HELIX 44 44 ASP C 209 ALA C 220 1 12 HELIX 45 45 LYS C 235 GLY C 250 1 16 HELIX 46 46 SER C 252 TYR C 260 1 9 HELIX 47 47 GLY C 264 GLU C 292 1 29 HELIX 48 48 GLU C 294 GLY C 323 1 30 HELIX 49 49 THR D 15 ALA D 22 1 8 HELIX 50 50 ALA D 22 TYR D 33 1 12 HELIX 51 51 HIS D 43 VAL D 47 5 5 HELIX 52 52 ASP D 50 GLY D 69 1 20 HELIX 53 53 SER D 81 VAL D 83 5 3 HELIX 54 54 PRO D 84 CYS D 95 1 12 HELIX 55 55 TYR D 98 ARG D 104 1 7 HELIX 56 56 MET D 105 SER D 112 1 8 HELIX 57 57 ALA D 120 LEU D 135 1 16 HELIX 58 58 GLN D 147 GLY D 166 1 20 HELIX 59 59 ASN D 199 TYR D 203 5 5 HELIX 60 60 ASP D 209 ALA D 220 1 12 HELIX 61 61 LYS D 235 GLY D 250 1 16 HELIX 62 62 SER D 252 TYR D 260 1 9 HELIX 63 63 GLY D 264 GLU D 292 1 29 HELIX 64 64 GLU D 294 GLY D 323 1 30 HELIX 65 65 THR E 15 ALA E 22 1 8 HELIX 66 66 ALA E 22 TYR E 33 1 12 HELIX 67 67 VAL E 40 ILE E 45 1 6 HELIX 68 68 ASP E 50 GLY E 69 1 20 HELIX 69 69 SER E 81 VAL E 83 5 3 HELIX 70 70 PRO E 84 CYS E 95 1 12 HELIX 71 71 TYR E 98 ARG E 104 1 7 HELIX 72 72 MET E 105 SER E 112 1 8 HELIX 73 73 ALA E 120 LEU E 135 1 16 HELIX 74 74 GLN E 147 GLY E 166 1 20 HELIX 75 75 ASN E 199 TYR E 203 5 5 HELIX 76 76 ASP E 209 ALA E 220 1 12 HELIX 77 77 LYS E 235 GLY E 250 1 16 HELIX 78 78 SER E 252 TYR E 260 1 9 HELIX 79 79 GLY E 264 GLU E 292 1 29 HELIX 80 80 GLU E 294 GLY E 323 1 30 HELIX 81 81 THR F 15 ALA F 22 1 8 HELIX 82 82 ALA F 22 TYR F 33 1 12 HELIX 83 83 VAL F 40 ILE F 45 1 6 HELIX 84 84 ASP F 50 GLY F 69 1 20 HELIX 85 85 SER F 81 VAL F 83 5 3 HELIX 86 86 PRO F 84 CYS F 95 1 12 HELIX 87 87 TYR F 98 ARG F 104 1 7 HELIX 88 88 MET F 105 SER F 112 1 8 HELIX 89 89 ALA F 120 LEU F 135 1 16 HELIX 90 90 GLN F 147 GLY F 166 1 20 HELIX 91 91 ASN F 199 TYR F 203 5 5 HELIX 92 92 ASP F 209 ALA F 220 1 12 HELIX 93 93 LYS F 235 GLY F 250 1 16 HELIX 94 94 SER F 252 TYR F 260 1 9 HELIX 95 95 GLY F 264 GLU F 292 1 29 HELIX 96 96 GLU F 294 GLY F 323 1 30 SHEET 1 A 3 THR A 3 GLY A 7 0 SHEET 2 A 3 ASN A 34 ILE A 39 1 O ASN A 34 N ILE A 4 SHEET 3 A 3 THR A 76 ILE A 79 1 O THR A 76 N PHE A 37 SHEET 1 B 2 ILE A 140 PRO A 142 0 SHEET 2 B 2 GLU A 173 ARG A 175 1 O GLU A 173 N VAL A 141 SHEET 1 C 3 THR B 3 GLY B 7 0 SHEET 2 C 3 ASN B 34 ILE B 39 1 O ASN B 34 N ILE B 4 SHEET 3 C 3 THR B 76 ILE B 79 1 O THR B 76 N PHE B 37 SHEET 1 D 2 ILE B 140 PRO B 142 0 SHEET 2 D 2 GLU B 173 ARG B 175 1 O GLU B 173 N VAL B 141 SHEET 1 E 3 THR C 3 ILE C 8 0 SHEET 2 E 3 ASN C 34 ILE C 39 1 O ASN C 34 N ILE C 4 SHEET 3 E 3 THR C 76 ILE C 79 1 O THR C 76 N PHE C 37 SHEET 1 F 2 ILE C 140 PRO C 142 0 SHEET 2 F 2 GLU C 173 ARG C 175 1 O GLU C 173 N VAL C 141 SHEET 1 G 3 THR D 3 GLY D 7 0 SHEET 2 G 3 ASN D 34 ILE D 39 1 O ASN D 34 N ILE D 4 SHEET 3 G 3 THR D 76 ILE D 79 1 O THR D 76 N PHE D 37 SHEET 1 H 2 ILE D 140 PRO D 142 0 SHEET 2 H 2 GLU D 173 ARG D 175 1 O GLU D 173 N VAL D 141 SHEET 1 I 3 THR E 3 GLY E 7 0 SHEET 2 I 3 ASN E 34 ILE E 39 1 O ASN E 34 N ILE E 4 SHEET 3 I 3 THR E 76 ILE E 79 1 O THR E 76 N PHE E 37 SHEET 1 J 2 ILE E 140 PRO E 142 0 SHEET 2 J 2 GLU E 173 ARG E 175 1 O GLU E 173 N VAL E 141 SHEET 1 K 3 THR F 3 GLY F 7 0 SHEET 2 K 3 ASN F 34 ILE F 39 1 O ASN F 34 N ILE F 4 SHEET 3 K 3 THR F 76 ILE F 79 1 O THR F 76 N PHE F 37 SHEET 1 L 2 ILE F 140 PRO F 142 0 SHEET 2 L 2 GLU F 173 ARG F 175 1 O GLU F 173 N VAL F 141 CRYST1 226.760 91.660 156.970 90.00 132.66 90.00 C 1 2 1 24 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 0.004410 0.000000 0.004064 0.00000 SCALE2 0.000000 0.010910 0.000000 0.00000 SCALE3 0.000000 0.000000 0.008663 0.00000 ATOM 1 N MET A 1 54.714 13.002 41.939 1.00 66.00 N ATOM 2 CA MET A 1 54.310 12.018 42.992 1.00 65.52 C ATOM 3 C MET A 1 53.609 10.830 42.334 1.00 64.02 C ATOM 4 O MET A 1 53.193 10.914 41.179 1.00 65.65 O ATOM 5 CB MET A 1 53.333 12.666 43.974 1.00 67.11 C ATOM 6 CG MET A 1 53.505 14.158 44.167 1.00 68.71 C ATOM 7 SD MET A 1 52.078 14.883 45.032 1.00 71.63 S ATOM 8 CE MET A 1 50.895 15.119 43.656 1.00 71.58 C ATOM 9 N LYS A 2 53.469 9.731 43.071 1.00 60.09 N ATOM 10 CA LYS A 2 52.791 8.553 42.544 1.00 55.63 C ATOM 11 C LYS A 2 51.289 8.772 42.647 1.00 52.59 C ATOM 12 O LYS A 2 50.833 9.561 43.474 1.00 53.28 O ATOM 13 CB LYS A 2 53.192 7.306 43.330 1.00 54.64 C ATOM 14 CG LYS A 2 54.616 6.878 43.081 1.00 57.48 C ATOM 15 CD LYS A 2 54.997 5.705 43.969 1.00 61.14 C ATOM 16 CE LYS A 2 56.350 5.123 43.566 1.00 64.09 C ATOM 17 NZ LYS A 2 56.309 4.595 42.164 1.00 64.75 N ATOM 18 N THR A 3 50.516 8.088 41.808 1.00 47.53 N ATOM 19 CA THR A 3 49.068 8.248 41.839 1.00 41.01 C ATOM 20 C THR A 3 48.379 7.004 42.365 1.00 38.61 C ATOM 21 O THR A 3 48.702 5.891 41.969 1.00 39.25 O ATOM 22 CB THR A 3 48.516 8.537 40.446 1.00 38.80 C ATOM 23 OG1 THR A 3 49.266 9.597 39.843 1.00 39.28 O ATOM 24 CG2 THR A 3 47.059 8.938 40.535 1.00 36.60 C ATOM 25 N ILE A 4 47.425 7.198 43.260 1.00 35.58 N ATOM 26 CA ILE A 4 46.688 6.082 43.818 1.00 34.67 C ATOM 27 C ILE A 4 45.213 6.204 43.471 1.00 34.08 C ATOM 28 O ILE A 4 44.593 7.228 43.737 1.00 34.77 O ATOM 29 CB ILE A 4 46.836 6.047 45.345 1.00 35.42 C ATOM 30 CG1 ILE A 4 48.292 5.749 45.699 1.00 35.96 C ATOM 31 CG2 ILE A 4 45.875 5.030 45.951 1.00 34.06 C ATOM 32 CD1 ILE A 4 48.578 5.675 47.196 1.00 38.47 C ATOM 33 N PHE A 5 44.652 5.162 42.868 1.00 31.41 N ATOM 34 CA PHE A 5 43.240 5.184 42.510 1.00 28.94 C ATOM 35 C PHE A 5 42.501 4.202 43.415 1.00 27.35 C ATOM 36 O PHE A 5 42.986 3.110 43.676 1.00 27.79 O ATOM 37 CB PHE A 5 43.059 4.808 41.024 1.00 27.85 C ATOM 38 CG PHE A 5 41.628 4.889 40.541 1.00 27.15 C ATOM 39 CD1 PHE A 5 40.715 3.884 40.854 1.00 27.28 C ATOM 40 CD2 PHE A 5 41.174 6.001 39.840 1.00 26.13 C ATOM 41 CE1 PHE A 5 39.369 3.980 40.484 1.00 26.44 C ATOM 42 CE2 PHE A 5 39.825 6.109 39.463 1.00 27.40 C ATOM 43 CZ PHE A 5 38.916 5.094 39.791 1.00 25.00 C ATOM 44 N SER A 6 41.330 4.593 43.897 1.00 25.18 N ATOM 45 CA SER A 6 40.551 3.733 44.762 1.00 24.77 C ATOM 46 C SER A 6 39.068 3.832 44.423 1.00 25.98 C ATOM 47 O SER A 6 38.488 4.915 44.478 1.00 27.64 O ATOM 48 CB SER A 6 40.789 4.134 46.214 1.00 28.32 C ATOM 49 OG SER A 6 39.925 3.449 47.112 1.00 32.67 O ATOM 50 N GLY A 7 38.453 2.707 44.063 1.00 25.62 N ATOM 51 CA GLY A 7 37.035 2.713 43.730 1.00 26.79 C ATOM 52 C GLY A 7 36.180 2.491 44.964 1.00 29.14 C ATOM 53 O GLY A 7 36.515 1.668 45.801 1.00 33.40 O ATOM 54 N ILE A 8 35.070 3.201 45.095 1.00 30.27 N ATOM 55 CA ILE A 8 34.241 3.035 46.277 1.00 34.69 C ATOM 56 C ILE A 8 32.830 2.559 45.886 1.00 35.93 C ATOM 57 O ILE A 8 32.103 3.245 45.180 1.00 38.17 O ATOM 58 CB ILE A 8 34.144 4.382 47.089 1.00 37.17 C ATOM 59 CG1 ILE A 8 35.478 5.132 47.060 1.00 38.79 C ATOM 60 CG2 ILE A 8 33.783 4.105 48.541 1.00 38.90 C ATOM 61 CD1 ILE A 8 36.672 4.373 47.632 1.00 40.71 C ATOM 62 N GLN A 9 32.446 1.381 46.346 1.00 37.16 N ATOM 63 CA GLN A 9 31.138 0.854 46.040 1.00 38.13 C ATOM 64 C GLN A 9 30.080 1.567 46.856 1.00 38.75 C ATOM 65 O GLN A 9 30.155 1.608 48.073 1.00 39.40 O ATOM 66 CB GLN A 9 31.112 -0.629 46.365 1.00 41.70 C ATOM 67 CG GLN A 9 31.378 -1.517 45.191 1.00 47.81 C ATOM 68 CD GLN A 9 30.136 -1.694 44.331 1.00 52.44 C ATOM 69 OE1 GLN A 9 30.146 -2.432 43.342 1.00 56.85 O ATOM 70 NE2 GLN A 9 29.050 -1.021 44.713 1.00 53.97 N ATOM 71 N PRO A 10 29.080 2.151 46.196 1.00 39.52 N ATOM 72 CA PRO A 10 28.019 2.851 46.913 1.00 42.47 C ATOM 73 C PRO A 10 27.088 1.898 47.645 1.00 46.46 C ATOM 74 O PRO A 10 26.326 1.156 47.024 1.00 48.00 O ATOM 75 CB PRO A 10 27.315 3.632 45.807 1.00 40.79 C ATOM 76 CG PRO A 10 27.504 2.758 44.625 1.00 40.60 C ATOM 77 CD PRO A 10 28.953 2.372 44.753 1.00 39.84 C ATOM 78 N SER A 11 27.178 1.918 48.975 1.00 52.10 N ATOM 79 CA SER A 11 26.358 1.077 49.870 1.00 55.57 C ATOM 80 C SER A 11 26.116 1.783 51.219 1.00 57.92 C ATOM 81 O SER A 11 25.617 1.159 52.160 1.00 59.81 O ATOM 82 CB SER A 11 27.043 -0.282 50.117 1.00 53.30 C ATOM 83 OG SER A 11 27.106 -1.054 48.926 1.00 51.75 O ATOM 84 N GLY A 12 26.443 3.081 51.285 1.00 58.57 N ATOM 85 CA GLY A 12 26.265 3.865 52.504 1.00 59.21 C ATOM 86 C GLY A 12 26.527 3.133 53.822 1.00 60.32 C ATOM 87 O GLY A 12 25.867 3.398 54.835 1.00 59.45 O ATOM 88 N VAL A 13 27.493 2.213 53.821 1.00 60.48 N ATOM 89 CA VAL A 13 27.797 1.456 55.027 1.00 57.49 C ATOM 90 C VAL A 13 29.227 0.946 55.073 1.00 55.90 C ATOM 91 O VAL A 13 29.542 -0.125 54.537 1.00 57.37 O ATOM 92 CB VAL A 13 26.849 0.242 55.171 1.00 57.62 C ATOM 93 CG1 VAL A 13 26.932 -0.643 53.921 1.00 59.72 C ATOM 94 CG2 VAL A 13 27.219 -0.558 56.397 1.00 56.70 C ATOM 95 N ILE A 14 30.104 1.715 55.701 1.00 51.97 N ATOM 96 CA ILE A 14 31.484 1.276 55.826 1.00 49.60 C ATOM 97 C ILE A 14 31.756 0.913 57.291 1.00 47.22 C ATOM 98 O ILE A 14 31.530 1.722 58.198 1.00 46.78 O ATOM 99 CB ILE A 14 32.457 2.351 55.305 1.00 48.99 C ATOM 100 CG1 ILE A 14 32.281 3.657 56.052 1.00 50.07 C ATOM 101 CG2 ILE A 14 32.167 2.619 53.835 1.00 48.57 C ATOM 102 CD1 ILE A 14 33.194 4.753 55.533 1.00 53.56 C ATOM 103 N THR A 15 32.210 -0.323 57.512 1.00 44.36 N ATOM 104 CA THR A 15 32.482 -0.845 58.858 1.00 40.05 C ATOM 105 C THR A 15 33.672 -0.230 59.588 1.00 39.10 C ATOM 106 O THR A 15 34.583 0.346 58.979 1.00 36.48 O ATOM 107 CB THR A 15 32.709 -2.368 58.841 1.00 38.53 C ATOM 108 OG1 THR A 15 33.899 -2.659 58.101 1.00 36.48 O ATOM 109 CG2 THR A 15 31.536 -3.088 58.208 1.00 33.79 C ATOM 110 N ILE A 16 33.643 -0.372 60.910 1.00 38.46 N ATOM 111 CA ILE A 16 34.687 0.150 61.776 1.00 37.84 C ATOM 112 C ILE A 16 35.991 -0.544 61.406 1.00 35.70 C ATOM 113 O ILE A 16 37.084 -0.033 61.654 1.00 34.69 O ATOM 114 CB ILE A 16 34.344 -0.107 63.272 1.00 40.05 C ATOM 115 CG1 ILE A 16 35.345 0.608 64.166 1.00 41.61 C ATOM 116 CG2 ILE A 16 34.367 -1.574 63.585 1.00 41.94 C ATOM 117 CD1 ILE A 16 35.034 2.084 64.305 1.00 45.02 C ATOM 118 N GLY A 17 35.855 -1.714 60.794 1.00 34.21 N ATOM 119 CA GLY A 17 37.012 -2.466 60.374 1.00 32.66 C ATOM 120 C GLY A 17 37.623 -1.782 59.179 1.00 33.59 C ATOM 121 O GLY A 17 38.841 -1.693 59.073 1.00 32.49 O ATOM 122 N ASN A 18 36.781 -1.291 58.274 1.00 35.56 N ATOM 123 CA ASN A 18 37.274 -0.582 57.083 1.00 39.18 C ATOM 124 C ASN A 18 37.990 0.693 57.525 1.00 37.74 C ATOM 125 O ASN A 18 39.059 1.023 57.011 1.00 34.90 O ATOM 126 CB ASN A 18 36.110 -0.208 56.145 1.00 44.66 C ATOM 127 CG ASN A 18 35.485 -1.432 55.444 1.00 49.68 C ATOM 128 OD1 ASN A 18 34.281 -1.452 55.146 1.00 50.41 O ATOM 129 ND2 ASN A 18 36.309 -2.447 55.166 1.00 50.98 N ATOM 130 N TYR A 19 37.383 1.404 58.476 1.00 37.34 N ATOM 131 CA TYR A 19 37.955 2.636 59.000 1.00 37.01 C ATOM 132 C TYR A 19 39.319 2.378 59.639 1.00 36.74 C ATOM 133 O TYR A 19 40.253 3.146 59.434 1.00 37.52 O ATOM 134 CB TYR A 19 36.994 3.266 60.019 1.00 37.69 C ATOM 135 CG TYR A 19 37.520 4.535 60.674 1.00 39.00 C ATOM 136 CD1 TYR A 19 38.290 4.484 61.831 1.00 39.38 C ATOM 137 CD2 TYR A 19 37.265 5.781 60.127 1.00 40.96 C ATOM 138 CE1 TYR A 19 38.793 5.635 62.425 1.00 38.49 C ATOM 139 CE2 TYR A 19 37.765 6.941 60.716 1.00 41.64 C ATOM 140 CZ TYR A 19 38.529 6.853 61.864 1.00 39.78 C ATOM 141 OH TYR A 19 39.030 7.988 62.437 1.00 42.88 O ATOM 142 N ILE A 20 39.428 1.296 60.406 1.00 34.69 N ATOM 143 CA ILE A 20 40.674 0.963 61.072 1.00 33.02 C ATOM 144 C ILE A 20 41.672 0.392 60.083 1.00 35.32 C ATOM 145 O ILE A 20 42.857 0.712 60.131 1.00 34.07 O ATOM 146 CB ILE A 20 40.437 -0.068 62.181 1.00 31.69 C ATOM 147 CG1 ILE A 20 39.536 0.523 63.254 1.00 31.13 C ATOM 148 CG2 ILE A 20 41.750 -0.499 62.774 1.00 32.21 C ATOM 149 CD1 ILE A 20 39.258 -0.413 64.386 1.00 31.74 C ATOM 150 N GLY A 21 41.171 -0.436 59.169 1.00 38.51 N ATOM 151 CA GLY A 21 42.012 -1.088 58.181 1.00 39.81 C ATOM 152 C GLY A 21 42.723 -0.247 57.139 1.00 41.60 C ATOM 153 O GLY A 21 43.918 -0.434 56.901 1.00 40.81 O ATOM 154 N ALA A 22 42.007 0.670 56.497 1.00 44.94 N ATOM 155 CA ALA A 22 42.631 1.509 55.466 1.00 46.85 C ATOM 156 C ALA A 22 42.133 2.965 55.441 1.00 46.99 C ATOM 157 O ALA A 22 42.931 3.908 55.375 1.00 46.29 O ATOM 158 CB ALA A 22 42.429 0.870 54.097 1.00 45.26 C ATOM 159 N LEU A 23 40.815 3.134 55.494 1.00 46.52 N ATOM 160 CA LEU A 23 40.193 4.450 55.469 1.00 46.83 C ATOM 161 C LEU A 23 40.958 5.488 56.283 1.00 50.11 C ATOM 162 O LEU A 23 41.336 6.529 55.752 1.00 52.64 O ATOM 163 CB LEU A 23 38.764 4.365 56.008 1.00 45.40 C ATOM 164 CG LEU A 23 37.648 5.122 55.295 1.00 41.78 C ATOM 165 CD1 LEU A 23 38.149 6.457 54.812 1.00 44.06 C ATOM 166 CD2 LEU A 23 37.181 4.302 54.133 1.00 46.39 C ATOM 167 N ARG A 24 41.185 5.207 57.566 1.00 52.42 N ATOM 168 CA ARG A 24 41.879 6.150 58.433 1.00 54.43 C ATOM 169 C ARG A 24 43.290 6.458 57.934 1.00 53.75 C ATOM 170 O ARG A 24 43.787 7.561 58.156 1.00 53.85 O ATOM 171 CB ARG A 24 41.904 5.635 59.881 1.00 57.67 C ATOM 172 CG ARG A 24 42.346 6.686 60.893 1.00 61.13 C ATOM 173 CD ARG A 24 42.340 6.158 62.325 1.00 64.09 C ATOM 174 NE ARG A 24 43.135 4.926 62.442 1.00 67.19 N ATOM 175 CZ ARG A 24 43.540 4.391 63.592 1.00 67.22 C ATOM 176 NH1 ARG A 24 43.229 4.978 64.744 1.00 67.44 N ATOM 177 NH2 ARG A 24 44.256 3.273 63.587 1.00 65.13 N ATOM 178 N GLN A 25 43.884 5.507 57.200 1.00 53.63 N ATOM 179 CA GLN A 25 45.235 5.647 56.634 1.00 55.95 C ATOM 180 C GLN A 25 45.343 6.432 55.321 1.00 56.41 C ATOM 181 O GLN A 25 46.414 6.937 54.992 1.00 57.44 O ATOM 182 CB GLN A 25 45.904 4.279 56.449 1.00 58.31 C ATOM 183 CG GLN A 25 46.473 3.677 57.736 1.00 63.30 C ATOM 184 CD GLN A 25 47.550 4.555 58.401 1.00 67.12 C ATOM 185 OE1 GLN A 25 48.677 4.685 57.901 1.00 68.85 O ATOM 186 NE2 GLN A 25 47.192 5.176 59.524 1.00 68.34 N ATOM 187 N PHE A 26 44.268 6.487 54.540 1.00 56.62 N ATOM 188 CA PHE A 26 44.266 7.292 53.321 1.00 55.73 C ATOM 189 C PHE A 26 44.277 8.762 53.735 1.00 55.55 C ATOM 190 O PHE A 26 44.872 9.599 53.062 1.00 55.28 O ATOM 191 CB PHE A 26 43.008 7.042 52.491 1.00 54.79 C ATOM 192 CG PHE A 26 42.984 5.716 51.814 1.00 53.93 C ATOM 193 CD1 PHE A 26 44.136 5.196 51.239 1.00 53.31 C ATOM 194 CD2 PHE A 26 41.802 4.986 51.737 1.00 54.13 C ATOM 195 CE1 PHE A 26 44.112 3.962 50.595 1.00 53.40 C ATOM 196 CE2 PHE A 26 41.765 3.749 51.093 1.00 53.93 C ATOM 197 CZ PHE A 26 42.923 3.236 50.521 1.00 53.56 C ATOM 198 N VAL A 27 43.607 9.076 54.842 1.00 55.41 N ATOM 199 CA VAL A 27 43.560 10.455 55.326 1.00 55.85 C ATOM 200 C VAL A 27 44.957 11.047 55.492 1.00 57.14 C ATOM 201 O VAL A 27 45.125 12.267 55.492 1.00 56.37 O ATOM 202 CB VAL A 27 42.837 10.567 56.671 1.00 54.48 C ATOM 203 CG1 VAL A 27 42.719 12.023 57.060 1.00 50.90 C ATOM 204 CG2 VAL A 27 41.469 9.929 56.579 1.00 55.55 C ATOM 205 N GLU A 28 45.951 10.177 55.644 1.00 59.13 N ATOM 206 CA GLU A 28 47.338 10.605 55.784 1.00 61.85 C ATOM 207 C GLU A 28 48.036 10.581 54.426 1.00 61.88 C ATOM 208 O GLU A 28 48.704 11.546 54.044 1.00 63.40 O ATOM 209 CB GLU A 28 48.090 9.681 56.734 1.00 66.04 C ATOM 210 CG GLU A 28 48.131 10.131 58.185 1.00 72.47 C ATOM 211 CD GLU A 28 48.961 9.183 59.055 1.00 76.75 C ATOM 212 OE1 GLU A 28 50.158 8.981 58.735 1.00 79.90 O ATOM 213 OE2 GLU A 28 48.417 8.634 60.046 1.00 76.34 O ATOM 214 N LEU A 29 47.869 9.473 53.705 1.00 59.66 N ATOM 215 CA LEU A 29 48.481 9.299 52.397 1.00 57.28 C ATOM 216 C LEU A 29 48.089 10.374 51.396 1.00 55.85 C ATOM 217 O LEU A 29 48.873 10.709 50.502 1.00 55.69 O ATOM 218 CB LEU A 29 48.118 7.928 51.824 1.00 57.82 C ATOM 219 CG LEU A 29 48.666 6.701 52.537 1.00 57.79 C ATOM 220 CD1 LEU A 29 48.173 5.446 51.844 1.00 58.40 C ATOM 221 CD2 LEU A 29 50.173 6.755 52.518 1.00 59.12 C ATOM 222 N GLN A 30 46.884 10.923 51.548 1.00 54.51 N ATOM 223 CA GLN A 30 46.391 11.943 50.623 1.00 54.42 C ATOM 224 C GLN A 30 47.288 13.175 50.476 1.00 55.70 C ATOM 225 O GLN A 30 47.130 13.937 49.526 1.00 56.48 O ATOM 226 CB GLN A 30 44.969 12.381 51.003 1.00 50.38 C ATOM 227 CG GLN A 30 44.853 13.202 52.261 1.00 48.15 C ATOM 228 CD GLN A 30 43.418 13.557 52.587 1.00 48.12 C ATOM 229 OE1 GLN A 30 42.705 14.092 51.750 1.00 48.29 O ATOM 230 NE2 GLN A 30 42.987 13.257 53.808 1.00 49.35 N ATOM 231 N HIS A 31 48.230 13.365 51.396 1.00 56.34 N ATOM 232 CA HIS A 31 49.121 14.507 51.309 1.00 56.66 C ATOM 233 C HIS A 31 50.404 14.201 50.560 1.00 57.23 C ATOM 234 O HIS A 31 50.966 15.082 49.918 1.00 58.86 O ATOM 235 CB HIS A 31 49.465 15.049 52.695 1.00 55.97 C ATOM 236 CG HIS A 31 48.311 15.686 53.397 1.00 56.61 C ATOM 237 ND1 HIS A 31 47.485 14.992 54.250 1.00 56.81 N ATOM 238 CD2 HIS A 31 47.828 16.948 53.346 1.00 56.93 C ATOM 239 CE1 HIS A 31 46.538 15.800 54.695 1.00 56.29 C ATOM 240 NE2 HIS A 31 46.721 16.992 54.161 1.00 56.27 N ATOM 241 N GLU A 32 50.869 12.960 50.642 1.00 58.29 N ATOM 242 CA GLU A 32 52.100 12.562 49.958 1.00 62.55 C ATOM 243 C GLU A 32 51.836 12.115 48.533 1.00 62.07 C ATOM 244 O GLU A 32 52.509 12.543 47.594 1.00 62.92 O ATOM 245 CB GLU A 32 52.793 11.405 50.682 1.00 67.68 C ATOM 246 CG GLU A 32 53.282 11.704 52.096 1.00 75.92 C ATOM 247 CD GLU A 32 54.086 10.538 52.704 1.00 79.18 C ATOM 248 OE1 GLU A 32 54.386 10.573 53.923 1.00 80.61 O ATOM 249 OE2 GLU A 32 54.418 9.591 51.950 1.00 80.96 O ATOM 250 N TYR A 33 50.859 11.230 48.389 1.00 60.85 N ATOM 251 CA TYR A 33 50.487 10.700 47.092 1.00 58.20 C ATOM 252 C TYR A 33 49.371 11.506 46.439 1.00 56.13 C ATOM 253 O TYR A 33 48.820 12.441 47.024 1.00 55.16 O ATOM 254 CB TYR A 33 50.040 9.260 47.252 1.00 59.10 C ATOM 255 CG TYR A 33 51.131 8.342 47.734 1.00 61.68 C ATOM 256 CD1 TYR A 33 52.200 7.999 46.897 1.00 63.51 C ATOM 257 CD2 TYR A 33 51.074 7.770 49.005 1.00 61.80 C ATOM 258 CE1 TYR A 33 53.180 7.101 47.311 1.00 64.61 C ATOM 259 CE2 TYR A 33 52.047 6.873 49.428 1.00 63.81 C ATOM 260 CZ TYR A 33 53.095 6.539 48.575 1.00 64.95 C ATOM 261 OH TYR A 33 54.042 5.621 48.973 1.00 68.34 O ATOM 262 N ASN A 34 49.039 11.137 45.210 1.00 54.02 N ATOM 263 CA ASN A 34 47.977 11.813 44.497 1.00 49.99 C ATOM 264 C ASN A 34 46.782 10.868 44.492 1.00 46.78 C ATOM 265 O ASN A 34 46.689 9.993 43.644 1.00 46.62 O ATOM 266 CB ASN A 34 48.415 12.113 43.078 1.00 52.56 C ATOM 267 CG ASN A 34 47.606 13.215 42.468 1.00 56.87 C ATOM 268 OD1 ASN A 34 46.419 13.043 42.196 1.00 60.03 O ATOM 269 ND2 ASN A 34 48.229 14.374 42.274 1.00 59.45 N ATOM 270 N CYS A 35 45.874 11.063 45.443 1.00 43.36 N ATOM 271 CA CYS A 35 44.713 10.202 45.594 1.00 40.27 C ATOM 272 C CYS A 35 43.462 10.513 44.756 1.00 39.22 C ATOM 273 O CYS A 35 43.069 11.667 44.619 1.00 41.74 O ATOM 274 CB CYS A 35 44.327 10.117 47.088 1.00 39.01 C ATOM 275 SG CYS A 35 45.470 9.114 48.129 1.00 33.91 S ATOM 276 N TYR A 36 42.850 9.465 44.189 1.00 36.75 N ATOM 277 CA TYR A 36 41.611 9.560 43.397 1.00 31.21 C ATOM 278 C TYR A 36 40.593 8.649 44.055 1.00 29.42 C ATOM 279 O TYR A 36 40.783 7.444 44.096 1.00 30.62 O ATOM 280 CB TYR A 36 41.810 9.064 41.961 1.00 29.39 C ATOM 281 CG TYR A 36 42.360 10.083 41.018 1.00 24.64 C ATOM 282 CD1 TYR A 36 43.721 10.129 40.738 1.00 24.48 C ATOM 283 CD2 TYR A 36 41.533 11.035 40.444 1.00 22.04 C ATOM 284 CE1 TYR A 36 44.254 11.101 39.912 1.00 23.97 C ATOM 285 CE2 TYR A 36 42.056 12.016 39.615 1.00 23.85 C ATOM 286 CZ TYR A 36 43.418 12.045 39.356 1.00 24.58 C ATOM 287 OH TYR A 36 43.967 13.029 38.563 1.00 26.44 O ATOM 288 N PHE A 37 39.517 9.221 44.561 1.00 27.43 N ATOM 289 CA PHE A 37 38.477 8.438 45.201 1.00 28.66 C ATOM 290 C PHE A 37 37.266 8.511 44.290 1.00 28.25 C ATOM 291 O PHE A 37 36.626 9.551 44.164 1.00 30.15 O ATOM 292 CB PHE A 37 38.166 9.009 46.592 1.00 32.37 C ATOM 293 CG PHE A 37 39.291 8.836 47.590 1.00 33.77 C ATOM 294 CD1 PHE A 37 39.420 7.657 48.317 1.00 34.10 C ATOM 295 CD2 PHE A 37 40.248 9.845 47.771 1.00 33.52 C ATOM 296 CE1 PHE A 37 40.491 7.484 49.205 1.00 35.73 C ATOM 297 CE2 PHE A 37 41.320 9.685 48.652 1.00 32.42 C ATOM 298 CZ PHE A 37 41.450 8.506 49.375 1.00 33.05 C ATOM 299 N CYS A 38 36.963 7.396 43.644 1.00 28.36 N ATOM 300 CA CYS A 38 35.862 7.333 42.694 1.00 29.45 C ATOM 301 C CYS A 38 34.693 6.480 43.152 1.00 27.64 C ATOM 302 O CYS A 38 34.852 5.284 43.354 1.00 31.17 O ATOM 303 CB CYS A 38 36.393 6.784 41.366 1.00 31.38 C ATOM 304 SG CYS A 38 35.128 6.570 40.102 1.00 35.84 S ATOM 305 N ILE A 39 33.522 7.088 43.296 1.00 24.96 N ATOM 306 CA ILE A 39 32.326 6.364 43.716 1.00 23.35 C ATOM 307 C ILE A 39 31.721 5.608 42.515 1.00 25.23 C ATOM 308 O ILE A 39 30.810 6.101 41.869 1.00 28.53 O ATOM 309 CB ILE A 39 31.286 7.343 44.275 1.00 21.17 C ATOM 310 CG1 ILE A 39 31.929 8.175 45.375 1.00 21.62 C ATOM 311 CG2 ILE A 39 30.045 6.585 44.763 1.00 20.72 C ATOM 312 CD1 ILE A 39 30.997 9.195 46.023 1.00 22.66 C ATOM 313 N VAL A 40 32.224 4.412 42.226 1.00 24.80 N ATOM 314 CA VAL A 40 31.766 3.614 41.093 1.00 21.80 C ATOM 315 C VAL A 40 30.279 3.262 41.056 1.00 23.24 C ATOM 316 O VAL A 40 29.902 2.136 41.382 1.00 27.66 O ATOM 317 CB VAL A 40 32.580 2.310 41.003 1.00 19.51 C ATOM 318 CG1 VAL A 40 34.008 2.623 40.602 1.00 17.89 C ATOM 319 CG2 VAL A 40 32.572 1.597 42.339 1.00 18.29 C ATOM 320 N ASP A 41 29.427 4.200 40.645 1.00 22.62 N ATOM 321 CA ASP A 41 27.989 3.906 40.583 1.00 21.36 C ATOM 322 C ASP A 41 27.601 3.083 39.345 1.00 21.96 C ATOM 323 O ASP A 41 26.573 2.404 39.345 1.00 20.95 O ATOM 324 CB ASP A 41 27.155 5.201 40.676 1.00 17.57 C ATOM 325 CG ASP A 41 27.463 6.187 39.575 1.00 16.82 C ATOM 326 OD1 ASP A 41 28.590 6.171 39.029 1.00 13.49 O ATOM 327 OD2 ASP A 41 26.573 7.008 39.269 1.00 16.88 O ATOM 328 N GLN A 42 28.434 3.118 38.307 1.00 22.48 N ATOM 329 CA GLN A 42 28.150 2.350 37.104 1.00 24.45 C ATOM 330 C GLN A 42 28.424 0.884 37.354 1.00 26.24 C ATOM 331 O GLN A 42 27.841 0.012 36.713 1.00 27.69 O ATOM 332 CB GLN A 42 28.982 2.851 35.915 1.00 20.94 C ATOM 333 CG GLN A 42 28.528 4.213 35.453 1.00 19.43 C ATOM 334 CD GLN A 42 29.168 4.651 34.169 1.00 20.64 C ATOM 335 OE1 GLN A 42 30.336 5.022 34.133 1.00 19.63 O ATOM 336 NE2 GLN A 42 28.399 4.607 33.088 1.00 25.91 N ATOM 337 N HIS A 43 29.317 0.600 38.291 1.00 27.59 N ATOM 338 CA HIS A 43 29.613 -0.789 38.604 1.00 25.05 C ATOM 339 C HIS A 43 28.482 -1.361 39.435 1.00 25.97 C ATOM 340 O HIS A 43 28.092 -2.503 39.248 1.00 30.34 O ATOM 341 CB HIS A 43 30.926 -0.910 39.357 1.00 18.87 C ATOM 342 CG HIS A 43 32.090 -1.186 38.466 1.00 20.00 C ATOM 343 ND1 HIS A 43 33.198 -0.370 38.402 1.00 21.56 N ATOM 344 CD2 HIS A 43 32.315 -2.188 37.584 1.00 24.05 C ATOM 345 CE1 HIS A 43 34.057 -0.856 37.521 1.00 22.15 C ATOM 346 NE2 HIS A 43 33.546 -1.960 37.010 1.00 23.04 N ATOM 347 N ALA A 44 27.936 -0.546 40.325 1.00 24.61 N ATOM 348 CA ALA A 44 26.864 -0.959 41.210 1.00 26.36 C ATOM 349 C ALA A 44 25.572 -1.269 40.480 1.00 28.35 C ATOM 350 O ALA A 44 24.637 -1.847 41.049 1.00 27.42 O ATOM 351 CB ALA A 44 26.622 0.134 42.236 1.00 27.78 C ATOM 352 N ILE A 45 25.523 -0.861 39.215 1.00 30.32 N ATOM 353 CA ILE A 45 24.334 -1.030 38.371 1.00 29.18 C ATOM 354 C ILE A 45 24.311 -2.411 37.673 1.00 28.79 C ATOM 355 O ILE A 45 23.393 -2.707 36.904 1.00 31.66 O ATOM 356 CB ILE A 45 24.250 0.170 37.322 1.00 27.46 C ATOM 357 CG1 ILE A 45 22.827 0.630 37.163 1.00 28.40 C ATOM 358 CG2 ILE A 45 24.728 -0.228 35.955 1.00 25.86 C ATOM 359 CD1 ILE A 45 22.284 1.268 38.403 1.00 34.04 C ATOM 360 N THR A 46 25.292 -3.266 37.971 1.00 24.96 N ATOM 361 CA THR A 46 25.341 -4.588 37.354 1.00 21.11 C ATOM 362 C THR A 46 24.439 -5.585 38.055 1.00 22.11 C ATOM 363 O THR A 46 24.230 -6.689 37.564 1.00 25.25 O ATOM 364 CB THR A 46 26.766 -5.172 37.297 1.00 15.98 C ATOM 365 OG1 THR A 46 27.268 -5.296 38.615 1.00 12.77 O ATOM 366 CG2 THR A 46 27.693 -4.298 36.493 1.00 13.55 C ATOM 367 N VAL A 47 23.912 -5.198 39.205 1.00 24.36 N ATOM 368 CA VAL A 47 22.999 -6.055 39.967 1.00 29.11 C ATOM 369 C VAL A 47 21.715 -5.274 40.249 1.00 31.10 C ATOM 370 O VAL A 47 21.712 -4.050 40.176 1.00 33.21 O ATOM 371 CB VAL A 47 23.625 -6.502 41.305 1.00 29.87 C ATOM 372 CG1 VAL A 47 24.775 -7.441 41.036 1.00 30.69 C ATOM 373 CG2 VAL A 47 24.117 -5.294 42.092 1.00 32.95 C ATOM 374 N TRP A 48 20.621 -5.956 40.563 1.00 33.76 N ATOM 375 CA TRP A 48 19.388 -5.223 40.803 1.00 36.43 C ATOM 376 C TRP A 48 19.652 -4.133 41.834 1.00 37.77 C ATOM 377 O TRP A 48 20.314 -4.376 42.844 1.00 37.87 O ATOM 378 CB TRP A 48 18.281 -6.158 41.281 1.00 39.25 C ATOM 379 CG TRP A 48 17.008 -5.985 40.508 1.00 45.59 C ATOM 380 CD1 TRP A 48 16.641 -6.616 39.328 1.00 48.54 C ATOM 381 CD2 TRP A 48 15.957 -5.079 40.809 1.00 49.51 C ATOM 382 NE1 TRP A 48 15.419 -6.149 38.892 1.00 47.30 N ATOM 383 CE2 TRP A 48 14.974 -5.207 39.782 1.00 51.28 C ATOM 384 CE3 TRP A 48 15.734 -4.175 41.853 1.00 53.12 C ATOM 385 CZ2 TRP A 48 13.800 -4.441 39.764 1.00 54.50 C ATOM 386 CZ3 TRP A 48 14.562 -3.411 41.840 1.00 58.06 C ATOM 387 CH2 TRP A 48 13.606 -3.554 40.802 1.00 57.38 C ATOM 388 N GLN A 49 19.170 -2.922 41.559 1.00 40.24 N ATOM 389 CA GLN A 49 19.355 -1.772 42.455 1.00 38.93 C ATOM 390 C GLN A 49 18.076 -0.977 42.528 1.00 40.21 C ATOM 391 O GLN A 49 17.291 -0.962 41.588 1.00 43.97 O ATOM 392 CB GLN A 49 20.446 -0.835 41.934 1.00 37.31 C ATOM 393 CG GLN A 49 21.872 -1.335 42.051 1.00 36.95 C ATOM 394 CD GLN A 49 22.390 -1.296 43.469 1.00 35.60 C ATOM 395 OE1 GLN A 49 21.804 -0.653 44.349 1.00 32.90 O ATOM 396 NE2 GLN A 49 23.507 -1.976 43.697 1.00 32.84 N ATOM 397 N ASP A 50 17.857 -0.305 43.645 1.00 41.38 N ATOM 398 CA ASP A 50 16.658 0.516 43.773 1.00 42.07 C ATOM 399 C ASP A 50 17.082 1.924 43.395 1.00 42.96 C ATOM 400 O ASP A 50 17.931 2.516 44.042 1.00 43.75 O ATOM 401 CB ASP A 50 16.121 0.508 45.193 1.00 43.31 C ATOM 402 CG ASP A 50 14.811 1.270 45.318 1.00 46.96 C ATOM 403 OD1 ASP A 50 13.739 0.681 45.063 1.00 48.83 O ATOM 404 OD2 ASP A 50 14.847 2.470 45.662 1.00 50.77 O ATOM 405 N PRO A 51 16.486 2.489 42.338 1.00 45.04 N ATOM 406 CA PRO A 51 16.847 3.841 41.905 1.00 46.25 C ATOM 407 C PRO A 51 17.010 4.851 43.048 1.00 47.44 C ATOM 408 O PRO A 51 18.007 5.572 43.098 1.00 45.37 O ATOM 409 CB PRO A 51 15.710 4.205 40.957 1.00 45.13 C ATOM 410 CG PRO A 51 15.418 2.902 40.315 1.00 45.42 C ATOM 411 CD PRO A 51 15.402 1.953 41.494 1.00 45.13 C ATOM 412 N HIS A 52 16.045 4.888 43.967 1.00 49.80 N ATOM 413 CA HIS A 52 16.106 5.827 45.077 1.00 52.90 C ATOM 414 C HIS A 52 17.263 5.504 46.029 1.00 51.31 C ATOM 415 O HIS A 52 17.973 6.406 46.488 1.00 51.36 O ATOM 416 CB HIS A 52 14.770 5.850 45.826 1.00 58.61 C ATOM 417 CG HIS A 52 14.672 6.946 46.847 1.00 67.33 C ATOM 418 ND1 HIS A 52 14.936 6.749 48.186 1.00 70.83 N ATOM 419 CD2 HIS A 52 14.371 8.263 46.718 1.00 69.22 C ATOM 420 CE1 HIS A 52 14.802 7.892 48.838 1.00 72.35 C ATOM 421 NE2 HIS A 52 14.460 8.827 47.968 1.00 71.38 N ATOM 422 N GLU A 53 17.463 4.220 46.305 1.00 49.51 N ATOM 423 CA GLU A 53 18.534 3.773 47.191 1.00 47.31 C ATOM 424 C GLU A 53 19.898 4.155 46.655 1.00 43.71 C ATOM 425 O GLU A 53 20.626 4.919 47.272 1.00 45.06 O ATOM 426 CB GLU A 53 18.480 2.258 47.345 1.00 51.41 C ATOM 427 CG GLU A 53 17.347 1.762 48.213 1.00 60.24 C ATOM 428 CD GLU A 53 17.846 1.286 49.564 1.00 66.13 C ATOM 429 OE1 GLU A 53 18.639 0.308 49.595 1.00 68.62 O ATOM 430 OE2 GLU A 53 17.448 1.884 50.593 1.00 70.06 O ATOM 431 N LEU A 54 20.237 3.597 45.502 1.00 40.34 N ATOM 432 CA LEU A 54 21.515 3.852 44.869 1.00 36.57 C ATOM 433 C LEU A 54 21.865 5.335 44.887 1.00 38.91 C ATOM 434 O LEU A 54 22.990 5.723 45.215 1.00 39.75 O ATOM 435 CB LEU A 54 21.483 3.358 43.434 1.00 29.32 C ATOM 436 CG LEU A 54 22.756 3.628 42.664 1.00 23.97 C ATOM 437 CD1 LEU A 54 23.953 3.080 43.392 1.00 23.71 C ATOM 438 CD2 LEU A 54 22.610 3.002 41.317 1.00 26.41 C ATOM 439 N ARG A 55 20.893 6.168 44.542 1.00 40.39 N ATOM 440 CA ARG A 55 21.117 7.603 44.509 1.00 41.67 C ATOM 441 C ARG A 55 21.415 8.147 45.905 1.00 40.95 C ATOM 442 O ARG A 55 22.219 9.067 46.079 1.00 40.26 O ATOM 443 CB ARG A 55 19.890 8.301 43.912 1.00 45.43 C ATOM 444 CG ARG A 55 20.130 9.751 43.457 1.00 51.80 C ATOM 445 CD ARG A 55 19.978 9.912 41.934 1.00 56.77 C ATOM 446 NE ARG A 55 18.755 9.272 41.444 1.00 62.36 N ATOM 447 CZ ARG A 55 17.518 9.610 41.809 1.00 65.12 C ATOM 448 NH1 ARG A 55 17.316 10.597 42.677 1.00 66.34 N ATOM 449 NH2 ARG A 55 16.477 8.951 41.304 1.00 67.09 N ATOM 450 N GLN A 56 20.769 7.568 46.905 1.00 40.97 N ATOM 451 CA GLN A 56 20.966 8.004 48.279 1.00 41.69 C ATOM 452 C GLN A 56 22.325 7.569 48.838 1.00 40.44 C ATOM 453 O GLN A 56 22.966 8.316 49.563 1.00 41.86 O ATOM 454 CB GLN A 56 19.837 7.458 49.155 1.00 44.41 C ATOM 455 CG GLN A 56 19.558 8.288 50.388 1.00 50.67 C ATOM 456 CD GLN A 56 19.177 9.722 50.048 1.00 56.40 C ATOM 457 OE1 GLN A 56 19.124 10.587 50.928 1.00 59.30 O ATOM 458 NE2 GLN A 56 18.906 9.981 48.768 1.00 59.57 N ATOM 459 N ASN A 57 22.761 6.362 48.499 1.00 38.92 N ATOM 460 CA ASN A 57 24.037 5.866 48.978 1.00 37.46 C ATOM 461 C ASN A 57 25.207 6.583 48.374 1.00 36.08 C ATOM 462 O ASN A 57 26.277 6.634 48.971 1.00 37.56 O ATOM 463 CB ASN A 57 24.182 4.382 48.694 1.00 40.26 C ATOM 464 CG ASN A 57 23.233 3.563 49.503 1.00 42.32 C ATOM 465 OD1 ASN A 57 23.030 3.829 50.690 1.00 44.60 O ATOM 466 ND2 ASN A 57 22.645 2.554 48.882 1.00 43.11 N ATOM 467 N ILE A 58 25.026 7.117 47.176 1.00 35.26 N ATOM 468 CA ILE A 58 26.115 7.835 46.538 1.00 34.55 C ATOM 469 C ILE A 58 26.411 9.077 47.380 1.00 34.45 C ATOM 470 O ILE A 58 27.574 9.396 47.645 1.00 33.36 O ATOM 471 CB ILE A 58 25.757 8.218 45.088 1.00 33.73 C ATOM 472 CG1 ILE A 58 25.456 6.944 44.288 1.00 30.28 C ATOM 473 CG2 ILE A 58 26.926 8.958 44.439 1.00 30.87 C ATOM 474 CD1 ILE A 58 25.099 7.181 42.836 1.00 29.14 C ATOM 475 N ARG A 59 25.363 9.759 47.836 1.00 34.08 N ATOM 476 CA ARG A 59 25.573 10.938 48.666 1.00 36.14 C ATOM 477 C ARG A 59 26.172 10.581 50.019 1.00 35.91 C ATOM 478 O ARG A 59 27.102 11.243 50.490 1.00 35.75 O ATOM 479 CB ARG A 59 24.265 11.688 48.862 1.00 36.97 C ATOM 480 CG ARG A 59 23.760 12.363 47.603 1.00 41.75 C ATOM 481 CD ARG A 59 22.585 13.243 47.941 1.00 44.33 C ATOM 482 NE ARG A 59 22.986 14.236 48.926 1.00 47.67 N ATOM 483 CZ ARG A 59 23.589 15.380 48.624 1.00 48.64 C ATOM 484 NH1 ARG A 59 23.841 15.671 47.353 1.00 47.51 N ATOM 485 NH2 ARG A 59 23.963 16.218 49.592 1.00 49.92 N ATOM 486 N ARG A 60 25.622 9.540 50.640 1.00 36.13 N ATOM 487 CA ARG A 60 26.106 9.062 51.926 1.00 34.37 C ATOM 488 C ARG A 60 27.596 8.727 51.877 1.00 32.27 C ATOM 489 O ARG A 60 28.385 9.216 52.675 1.00 33.02 O ATOM 490 CB ARG A 60 25.322 7.829 52.361 1.00 34.94 C ATOM 491 CG ARG A 60 24.157 8.156 53.244 1.00 40.59 C ATOM 492 CD ARG A 60 23.655 6.921 53.954 1.00 45.94 C ATOM 493 NE ARG A 60 22.624 6.228 53.199 1.00 51.03 N ATOM 494 CZ ARG A 60 21.362 6.636 53.102 1.00 54.73 C ATOM 495 NH1 ARG A 60 20.973 7.743 53.721 1.00 55.24 N ATOM 496 NH2 ARG A 60 20.483 5.932 52.390 1.00 56.95 N ATOM 497 N LEU A 61 27.978 7.903 50.918 1.00 30.35 N ATOM 498 CA LEU A 61 29.357 7.500 50.774 1.00 29.91 C ATOM 499 C LEU A 61 30.282 8.685 50.611 1.00 29.49 C ATOM 500 O LEU A 61 31.322 8.761 51.260 1.00 28.08 O ATOM 501 CB LEU A 61 29.487 6.540 49.589 1.00 29.93 C ATOM 502 CG LEU A 61 30.834 5.828 49.473 1.00 30.34 C ATOM 503 CD1 LEU A 61 31.112 5.040 50.746 1.00 26.23 C ATOM 504 CD2 LEU A 61 30.821 4.924 48.262 1.00 30.06 C ATOM 505 N ALA A 62 29.908 9.612 49.737 1.00 33.54 N ATOM 506 CA ALA A 62 30.722 10.816 49.510 1.00 34.40 C ATOM 507 C ALA A 62 30.788 11.641 50.797 1.00 32.77 C ATOM 508 O ALA A 62 31.850 12.133 51.175 1.00 32.63 O ATOM 509 CB ALA A 62 30.125 11.663 48.396 1.00 34.65 C ATOM 510 N ALA A 63 29.647 11.787 51.465 1.00 30.34 N ATOM 511 CA ALA A 63 29.598 12.536 52.715 1.00 30.98 C ATOM 512 C ALA A 63 30.434 11.846 53.801 1.00 31.74 C ATOM 513 O ALA A 63 31.217 12.493 54.489 1.00 31.46 O ATOM 514 CB ALA A 63 28.151 12.677 53.180 1.00 29.16 C ATOM 515 N LEU A 64 30.266 10.533 53.939 1.00 31.15 N ATOM 516 CA LEU A 64 30.983 9.771 54.938 1.00 27.42 C ATOM 517 C LEU A 64 32.492 9.753 54.693 1.00 27.08 C ATOM 518 O LEU A 64 33.275 9.669 55.638 1.00 28.09 O ATOM 519 CB LEU A 64 30.456 8.353 54.970 1.00 27.85 C ATOM 520 CG LEU A 64 30.191 7.818 56.366 1.00 29.35 C ATOM 521 CD1 LEU A 64 29.539 6.455 56.235 1.00 31.34 C ATOM 522 CD2 LEU A 64 31.501 7.728 57.155 1.00 29.17 C ATOM 523 N TYR A 65 32.905 9.825 53.434 1.00 24.81 N ATOM 524 CA TYR A 65 34.322 9.826 53.122 1.00 26.05 C ATOM 525 C TYR A 65 34.951 11.152 53.494 1.00 28.35 C ATOM 526 O TYR A 65 36.108 11.224 53.933 1.00 26.92 O ATOM 527 CB TYR A 65 34.547 9.549 51.641 1.00 24.15 C ATOM 528 CG TYR A 65 35.149 8.202 51.381 1.00 22.02 C ATOM 529 CD1 TYR A 65 34.460 7.052 51.727 1.00 22.40 C ATOM 530 CD2 TYR A 65 36.417 8.077 50.817 1.00 19.66 C ATOM 531 CE1 TYR A 65 35.010 5.805 51.530 1.00 24.97 C ATOM 532 CE2 TYR A 65 36.982 6.838 50.605 1.00 21.08 C ATOM 533 CZ TYR A 65 36.276 5.700 50.967 1.00 25.40 C ATOM 534 OH TYR A 65 36.838 4.455 50.779 1.00 27.50 O ATOM 535 N LEU A 66 34.184 12.216 53.304 1.00 31.68 N ATOM 536 CA LEU A 66 34.655 13.557 53.646 1.00 32.75 C ATOM 537 C LEU A 66 34.755 13.632 55.162 1.00 32.60 C ATOM 538 O LEU A 66 35.741 14.130 55.694 1.00 34.44 O ATOM 539 CB LEU A 66 33.676 14.632 53.120 1.00 31.58 C ATOM 540 CG LEU A 66 33.723 15.008 51.629 1.00 23.77 C ATOM 541 CD1 LEU A 66 32.556 15.882 51.334 1.00 22.64 C ATOM 542 CD2 LEU A 66 35.020 15.695 51.294 1.00 17.60 C ATOM 543 N ALA A 67 33.739 13.104 55.842 1.00 31.17 N ATOM 544 CA ALA A 67 33.691 13.092 57.302 1.00 30.40 C ATOM 545 C ALA A 67 34.881 12.364 57.918 1.00 30.51 C ATOM 546 O ALA A 67 35.415 12.809 58.922 1.00 30.84 O ATOM 547 CB ALA A 67 32.384 12.455 57.780 1.00 31.03 C ATOM 548 N VAL A 68 35.293 11.250 57.322 1.00 30.67 N ATOM 549 CA VAL A 68 36.420 10.502 57.845 1.00 29.88 C ATOM 550 C VAL A 68 37.681 11.350 57.787 1.00 29.75 C ATOM 551 O VAL A 68 38.612 11.135 58.547 1.00 30.97 O ATOM 552 CB VAL A 68 36.620 9.210 57.054 1.00 30.01 C ATOM 553 CG1 VAL A 68 37.970 8.611 57.353 1.00 29.77 C ATOM 554 CG2 VAL A 68 35.515 8.230 57.412 1.00 31.54 C ATOM 555 N GLY A 69 37.709 12.324 56.891 1.00 30.77 N ATOM 556 CA GLY A 69 38.881 13.164 56.793 1.00 34.07 C ATOM 557 C GLY A 69 39.464 13.378 55.407 1.00 37.76 C ATOM 558 O GLY A 69 40.510 14.009 55.266 1.00 39.69 O ATOM 559 N ILE A 70 38.818 12.865 54.368 1.00 39.94 N ATOM 560 CA ILE A 70 39.355 13.065 53.026 1.00 40.10 C ATOM 561 C ILE A 70 39.296 14.568 52.699 1.00 40.77 C ATOM 562 O ILE A 70 38.258 15.213 52.883 1.00 38.44 O ATOM 563 CB ILE A 70 38.558 12.257 51.975 1.00 38.97 C ATOM 564 CG1 ILE A 70 38.645 10.772 52.290 1.00 36.79 C ATOM 565 CG2 ILE A 70 39.150 12.494 50.596 1.00 37.92 C ATOM 566 CD1 ILE A 70 40.048 10.212 52.119 1.00 33.26 C ATOM 567 N ASP A 71 40.416 15.118 52.236 1.00 40.99 N ATOM 568 CA ASP A 71 40.505 16.536 51.904 1.00 43.49 C ATOM 569 C ASP A 71 40.142 16.754 50.437 1.00 44.45 C ATOM 570 O ASP A 71 40.928 16.427 49.549 1.00 46.20 O ATOM 571 CB ASP A 71 41.934 17.044 52.151 1.00 47.30 C ATOM 572 CG ASP A 71 42.019 18.564 52.229 1.00 47.91 C ATOM 573 OD1 ASP A 71 41.457 19.241 51.343 1.00 48.51 O ATOM 574 OD2 ASP A 71 42.658 19.069 53.177 1.00 48.56 O ATOM 575 N PRO A 72 38.962 17.336 50.162 1.00 43.74 N ATOM 576 CA PRO A 72 38.528 17.577 48.787 1.00 43.77 C ATOM 577 C PRO A 72 39.444 18.454 47.956 1.00 45.02 C ATOM 578 O PRO A 72 39.270 18.555 46.746 1.00 47.90 O ATOM 579 CB PRO A 72 37.147 18.184 48.968 1.00 40.14 C ATOM 580 CG PRO A 72 37.318 18.954 50.207 1.00 42.65 C ATOM 581 CD PRO A 72 38.033 17.973 51.103 1.00 44.22 C ATOM 582 N THR A 73 40.424 19.086 48.580 1.00 45.52 N ATOM 583 CA THR A 73 41.320 19.945 47.814 1.00 46.85 C ATOM 584 C THR A 73 42.652 19.258 47.606 1.00 46.10 C ATOM 585 O THR A 73 43.396 19.578 46.689 1.00 44.52 O ATOM 586 CB THR A 73 41.564 21.273 48.545 1.00 48.44 C ATOM 587 OG1 THR A 73 42.483 21.049 49.621 1.00 52.06 O ATOM 588 CG2 THR A 73 40.250 21.825 49.106 1.00 48.33 C ATOM 589 N GLN A 74 42.936 18.303 48.476 1.00 47.28 N ATOM 590 CA GLN A 74 44.178 17.562 48.416 1.00 48.94 C ATOM 591 C GLN A 74 43.997 16.317 47.536 1.00 47.07 C ATOM 592 O GLN A 74 44.929 15.866 46.860 1.00 45.81 O ATOM 593 CB GLN A 74 44.591 17.172 49.841 1.00 53.50 C ATOM 594 CG GLN A 74 46.051 16.797 50.011 1.00 59.99 C ATOM 595 CD GLN A 74 46.990 17.953 49.731 1.00 62.55 C ATOM 596 OE1 GLN A 74 47.019 18.489 48.626 1.00 64.81 O ATOM 597 NE2 GLN A 74 47.760 18.349 50.740 1.00 66.57 N ATOM 598 N ALA A 75 42.781 15.777 47.556 1.00 46.01 N ATOM 599 CA ALA A 75 42.414 14.587 46.784 1.00 43.39 C ATOM 600 C ALA A 75 41.243 14.871 45.824 1.00 40.79 C ATOM 601 O ALA A 75 40.636 15.944 45.857 1.00 40.63 O ATOM 602 CB ALA A 75 42.034 13.452 47.736 1.00 43.19 C ATOM 603 N THR A 76 40.930 13.902 44.968 1.00 36.11 N ATOM 604 CA THR A 76 39.843 14.065 44.026 1.00 30.79 C ATOM 605 C THR A 76 38.764 13.065 44.353 1.00 27.59 C ATOM 606 O THR A 76 38.992 11.867 44.283 1.00 28.69 O ATOM 607 CB THR A 76 40.326 13.829 42.600 1.00 31.02 C ATOM 608 OG1 THR A 76 41.533 14.570 42.358 1.00 33.09 O ATOM 609 CG2 THR A 76 39.273 14.281 41.619 1.00 30.83 C ATOM 610 N LEU A 77 37.604 13.560 44.757 1.00 25.43 N ATOM 611 CA LEU A 77 36.490 12.682 45.109 1.00 25.22 C ATOM 612 C LEU A 77 35.393 12.947 44.101 1.00 26.59 C ATOM 613 O LEU A 77 34.843 14.045 44.071 1.00 30.85 O ATOM 614 CB LEU A 77 35.963 13.005 46.509 1.00 23.90 C ATOM 615 CG LEU A 77 34.707 12.262 46.956 1.00 23.52 C ATOM 616 CD1 LEU A 77 35.046 10.794 47.110 1.00 26.65 C ATOM 617 CD2 LEU A 77 34.186 12.820 48.254 1.00 22.65 C ATOM 618 N PHE A 78 35.056 11.955 43.281 1.00 26.07 N ATOM 619 CA PHE A 78 34.031 12.154 42.255 1.00 24.06 C ATOM 620 C PHE A 78 33.192 10.941 41.980 1.00 22.57 C ATOM 621 O PHE A 78 33.610 9.833 42.255 1.00 24.86 O ATOM 622 CB PHE A 78 34.684 12.555 40.945 1.00 22.17 C ATOM 623 CG PHE A 78 35.462 11.452 40.300 1.00 18.30 C ATOM 624 CD1 PHE A 78 36.645 11.001 40.852 1.00 15.79 C ATOM 625 CD2 PHE A 78 35.032 10.899 39.103 1.00 20.92 C ATOM 626 CE1 PHE A 78 37.398 10.023 40.214 1.00 17.51 C ATOM 627 CE2 PHE A 78 35.776 9.916 38.451 1.00 21.12 C ATOM 628 CZ PHE A 78 36.959 9.481 39.006 1.00 19.63 C ATOM 629 N ILE A 79 32.016 11.166 41.410 1.00 21.02 N ATOM 630 CA ILE A 79 31.118 10.081 41.058 1.00 20.46 C ATOM 631 C ILE A 79 31.475 9.577 39.647 1.00 22.96 C ATOM 632 O ILE A 79 31.542 10.354 38.713 1.00 25.29 O ATOM 633 CB ILE A 79 29.691 10.565 41.077 1.00 17.66 C ATOM 634 CG1 ILE A 79 29.358 11.087 42.466 1.00 16.13 C ATOM 635 CG2 ILE A 79 28.777 9.450 40.632 1.00 16.61 C ATOM 636 CD1 ILE A 79 28.006 11.757 42.575 1.00 20.58 C ATOM 637 N GLN A 80 31.718 8.279 39.505 1.00 24.05 N ATOM 638 CA GLN A 80 32.112 7.678 38.228 1.00 23.58 C ATOM 639 C GLN A 80 31.312 8.094 36.991 1.00 23.64 C ATOM 640 O GLN A 80 31.891 8.573 36.017 1.00 23.50 O ATOM 641 CB GLN A 80 32.067 6.160 38.346 1.00 22.36 C ATOM 642 CG GLN A 80 32.491 5.397 37.114 1.00 20.48 C ATOM 643 CD GLN A 80 32.360 3.890 37.329 1.00 21.39 C ATOM 644 OE1 GLN A 80 31.361 3.420 37.892 1.00 13.96 O ATOM 645 NE2 GLN A 80 33.357 3.130 36.870 1.00 16.22 N ATOM 646 N SER A 81 29.993 7.896 37.021 1.00 22.28 N ATOM 647 CA SER A 81 29.131 8.226 35.890 1.00 20.20 C ATOM 648 C SER A 81 29.167 9.676 35.421 1.00 23.22 C ATOM 649 O SER A 81 28.710 9.972 34.308 1.00 27.76 O ATOM 650 CB SER A 81 27.692 7.857 36.204 1.00 17.25 C ATOM 651 OG SER A 81 27.175 8.649 37.232 1.00 17.37 O ATOM 652 N GLU A 82 29.688 10.582 36.252 1.00 22.10 N ATOM 653 CA GLU A 82 29.777 11.997 35.878 1.00 20.15 C ATOM 654 C GLU A 82 31.016 12.282 35.050 1.00 18.95 C ATOM 655 O GLU A 82 31.266 13.424 34.672 1.00 22.83 O ATOM 656 CB GLU A 82 29.759 12.897 37.113 1.00 17.37 C ATOM 657 CG GLU A 82 28.591 12.601 38.024 1.00 20.32 C ATOM 658 CD GLU A 82 28.382 13.656 39.082 1.00 22.35 C ATOM 659 OE1 GLU A 82 29.396 14.217 39.571 1.00 24.34 O ATOM 660 OE2 GLU A 82 27.198 13.899 39.436 1.00 19.83 O ATOM 661 N VAL A 83 31.794 11.242 34.791 1.00 16.31 N ATOM 662 CA VAL A 83 32.973 11.359 33.949 1.00 19.32 C ATOM 663 C VAL A 83 32.760 10.325 32.842 1.00 25.32 C ATOM 664 O VAL A 83 33.078 9.135 33.002 1.00 26.98 O ATOM 665 CB VAL A 83 34.240 11.028 34.702 1.00 17.12 C ATOM 666 CG1 VAL A 83 35.418 11.042 33.758 1.00 14.73 C ATOM 667 CG2 VAL A 83 34.436 12.017 35.806 1.00 19.79 C ATOM 668 N PRO A 84 32.193 10.766 31.704 1.00 26.67 N ATOM 669 CA PRO A 84 31.905 9.919 30.543 1.00 24.49 C ATOM 670 C PRO A 84 33.090 9.110 30.012 1.00 23.56 C ATOM 671 O PRO A 84 32.905 8.022 29.488 1.00 24.97 O ATOM 672 CB PRO A 84 31.389 10.922 29.529 1.00 24.87 C ATOM 673 CG PRO A 84 30.738 11.961 30.395 1.00 23.29 C ATOM 674 CD PRO A 84 31.781 12.155 31.438 1.00 23.64 C ATOM 675 N ALA A 85 34.296 9.647 30.131 1.00 22.01 N ATOM 676 CA ALA A 85 35.481 8.948 29.655 1.00 23.77 C ATOM 677 C ALA A 85 35.520 7.488 30.119 1.00 26.30 C ATOM 678 O ALA A 85 36.040 6.610 29.421 1.00 26.84 O ATOM 679 CB ALA A 85 36.732 9.666 30.123 1.00 24.29 C ATOM 680 N HIS A 86 34.977 7.229 31.305 1.00 26.15 N ATOM 681 CA HIS A 86 34.959 5.880 31.849 1.00 24.82 C ATOM 682 C HIS A 86 34.204 4.922 30.932 1.00 24.64 C ATOM 683 O HIS A 86 34.691 3.832 30.654 1.00 25.25 O ATOM 684 CB HIS A 86 34.326 5.870 33.250 1.00 26.65 C ATOM 685 CG HIS A 86 35.268 6.270 34.357 1.00 26.64 C ATOM 686 ND1 HIS A 86 35.782 7.543 34.491 1.00 25.00 N ATOM 687 CD2 HIS A 86 35.764 5.563 35.399 1.00 25.47 C ATOM 688 CE1 HIS A 86 36.545 7.602 35.565 1.00 20.01 C ATOM 689 NE2 HIS A 86 36.551 6.414 36.135 1.00 24.60 N ATOM 690 N ALA A 87 33.023 5.316 30.458 1.00 24.41 N ATOM 691 CA ALA A 87 32.238 4.450 29.572 1.00 22.99 C ATOM 692 C ALA A 87 32.883 4.363 28.198 1.00 21.99 C ATOM 693 O ALA A 87 32.858 3.322 27.560 1.00 22.73 O ATOM 694 CB ALA A 87 30.820 4.968 29.451 1.00 21.30 C ATOM 695 N GLN A 88 33.463 5.462 27.749 1.00 21.28 N ATOM 696 CA GLN A 88 34.108 5.480 26.457 1.00 23.92 C ATOM 697 C GLN A 88 35.333 4.587 26.427 1.00 24.96 C ATOM 698 O GLN A 88 35.522 3.797 25.504 1.00 28.23 O ATOM 699 CB GLN A 88 34.512 6.901 26.091 1.00 24.38 C ATOM 700 CG GLN A 88 33.356 7.795 25.763 1.00 26.64 C ATOM 701 CD GLN A 88 33.802 9.193 25.489 1.00 28.32 C ATOM 702 OE1 GLN A 88 34.240 9.889 26.393 1.00 29.68 O ATOM 703 NE2 GLN A 88 33.722 9.611 24.231 1.00 31.62 N ATOM 704 N ALA A 89 36.180 4.728 27.435 1.00 26.11 N ATOM 705 CA ALA A 89 37.399 3.932 27.528 1.00 25.05 C ATOM 706 C ALA A 89 37.017 2.468 27.739 1.00 24.44 C ATOM 707 O ALA A 89 37.644 1.572 27.180 1.00 25.18 O ATOM 708 CB ALA A 89 38.256 4.431 28.682 1.00 24.64 C ATOM 709 N ALA A 90 35.981 2.231 28.540 1.00 21.19 N ATOM 710 CA ALA A 90 35.535 0.876 28.804 1.00 19.44 C ATOM 711 C ALA A 90 35.214 0.139 27.516 1.00 21.12 C ATOM 712 O ALA A 90 35.532 -1.039 27.376 1.00 23.69 O ATOM 713 CB ALA A 90 34.319 0.883 29.725 1.00 16.54 C ATOM 714 N TRP A 91 34.584 0.829 26.568 1.00 23.21 N ATOM 715 CA TRP A 91 34.226 0.198 25.304 1.00 19.56 C ATOM 716 C TRP A 91 35.458 -0.133 24.501 1.00 17.38 C ATOM 717 O TRP A 91 35.572 -1.226 23.989 1.00 22.00 O ATOM 718 CB TRP A 91 33.295 1.080 24.460 1.00 19.46 C ATOM 719 CG TRP A 91 33.036 0.480 23.102 1.00 20.86 C ATOM 720 CD1 TRP A 91 33.544 0.906 21.902 1.00 20.45 C ATOM 721 CD2 TRP A 91 32.334 -0.738 22.827 1.00 21.16 C ATOM 722 NE1 TRP A 91 33.215 0.026 20.913 1.00 20.59 N ATOM 723 CE2 TRP A 91 32.479 -1.001 21.449 1.00 22.16 C ATOM 724 CE3 TRP A 91 31.608 -1.642 23.616 1.00 23.60 C ATOM 725 CZ2 TRP A 91 31.918 -2.145 20.834 1.00 21.68 C ATOM 726 CZ3 TRP A 91 31.052 -2.773 23.008 1.00 22.59 C ATOM 727 CH2 TRP A 91 31.216 -3.015 21.634 1.00 22.16 C ATOM 728 N MET A 92 36.386 0.797 24.383 1.00 15.42 N ATOM 729 CA MET A 92 37.577 0.498 23.614 1.00 20.19 C ATOM 730 C MET A 92 38.333 -0.697 24.163 1.00 22.23 C ATOM 731 O MET A 92 38.831 -1.539 23.408 1.00 23.88 O ATOM 732 CB MET A 92 38.505 1.704 23.550 1.00 20.11 C ATOM 733 CG MET A 92 37.911 2.844 22.792 1.00 22.51 C ATOM 734 SD MET A 92 39.092 4.122 22.565 1.00 29.54 S ATOM 735 CE MET A 92 38.546 5.263 23.840 1.00 22.00 C ATOM 736 N LEU A 93 38.434 -0.796 25.481 1.00 24.60 N ATOM 737 CA LEU A 93 39.161 -1.932 26.042 1.00 24.54 C ATOM 738 C LEU A 93 38.393 -3.243 25.805 1.00 25.46 C ATOM 739 O LEU A 93 39.014 -4.281 25.549 1.00 27.96 O ATOM 740 CB LEU A 93 39.453 -1.702 27.534 1.00 20.07 C ATOM 741 CG LEU A 93 40.357 -0.507 27.849 1.00 14.86 C ATOM 742 CD1 LEU A 93 40.508 -0.427 29.336 1.00 16.53 C ATOM 743 CD2 LEU A 93 41.706 -0.607 27.166 1.00 6.94 C ATOM 744 N GLN A 94 37.060 -3.196 25.867 1.00 22.25 N ATOM 745 CA GLN A 94 36.277 -4.395 25.612 1.00 24.96 C ATOM 746 C GLN A 94 36.636 -4.977 24.251 1.00 26.40 C ATOM 747 O GLN A 94 36.465 -6.159 24.018 1.00 30.41 O ATOM 748 CB GLN A 94 34.780 -4.113 25.630 1.00 23.26 C ATOM 749 CG GLN A 94 34.165 -4.106 26.990 1.00 29.51 C ATOM 750 CD GLN A 94 32.661 -4.161 26.932 1.00 34.03 C ATOM 751 OE1 GLN A 94 32.103 -5.058 26.317 1.00 37.66 O ATOM 752 NE2 GLN A 94 31.991 -3.198 27.565 1.00 35.60 N ATOM 753 N CYS A 95 37.146 -4.143 23.361 1.00 26.67 N ATOM 754 CA CYS A 95 37.500 -4.588 22.033 1.00 27.53 C ATOM 755 C CYS A 95 38.853 -5.228 21.942 1.00 28.21 C ATOM 756 O CYS A 95 39.172 -5.846 20.928 1.00 31.36 O ATOM 757 CB CYS A 95 37.413 -3.429 21.032 1.00 27.49 C ATOM 758 SG CYS A 95 35.729 -2.778 20.822 1.00 28.92 S ATOM 759 N ILE A 96 39.676 -5.066 22.969 1.00 28.95 N ATOM 760 CA ILE A 96 41.002 -5.689 22.932 1.00 31.86 C ATOM 761 C ILE A 96 41.121 -6.797 23.968 1.00 32.03 C ATOM 762 O ILE A 96 42.139 -7.474 24.039 1.00 33.31 O ATOM 763 CB ILE A 96 42.150 -4.680 23.162 1.00 33.03 C ATOM 764 CG1 ILE A 96 42.152 -4.214 24.611 1.00 34.12 C ATOM 765 CG2 ILE A 96 41.993 -3.491 22.217 1.00 33.91 C ATOM 766 CD1 ILE A 96 43.273 -3.226 24.911 1.00 37.36 C ATOM 767 N VAL A 97 40.083 -6.989 24.770 1.00 30.90 N ATOM 768 CA VAL A 97 40.127 -8.050 25.750 1.00 32.20 C ATOM 769 C VAL A 97 39.447 -9.257 25.129 1.00 37.82 C ATOM 770 O VAL A 97 38.400 -9.118 24.491 1.00 40.66 O ATOM 771 CB VAL A 97 39.369 -7.676 27.026 1.00 31.70 C ATOM 772 CG1 VAL A 97 37.939 -7.290 26.705 1.00 27.99 C ATOM 773 CG2 VAL A 97 39.390 -8.838 28.007 1.00 30.18 C ATOM 774 N TYR A 98 40.023 -10.445 25.300 1.00 41.36 N ATOM 775 CA TYR A 98 39.434 -11.664 24.726 1.00 42.82 C ATOM 776 C TYR A 98 38.291 -12.211 25.575 1.00 43.86 C ATOM 777 O TYR A 98 38.275 -12.040 26.802 1.00 43.10 O ATOM 778 CB TYR A 98 40.510 -12.734 24.563 1.00 44.04 C ATOM 779 CG TYR A 98 41.682 -12.291 23.714 1.00 45.77 C ATOM 780 CD1 TYR A 98 41.518 -11.989 22.360 1.00 45.44 C ATOM 781 CD2 TYR A 98 42.956 -12.174 24.266 1.00 46.42 C ATOM 782 CE1 TYR A 98 42.595 -11.583 21.576 1.00 45.33 C ATOM 783 CE2 TYR A 98 44.039 -11.767 23.488 1.00 47.91 C ATOM 784 CZ TYR A 98 43.846 -11.473 22.140 1.00 46.52 C ATOM 785 OH TYR A 98 44.903 -11.071 21.360 1.00 48.38 O ATOM 786 N ILE A 99 37.336 -12.881 24.929 1.00 44.30 N ATOM 787 CA ILE A 99 36.185 -13.424 25.655 1.00 44.97 C ATOM 788 C ILE A 99 36.649 -14.397 26.723 1.00 45.34 C ATOM 789 O ILE A 99 36.060 -14.476 27.799 1.00 44.50 O ATOM 790 CB ILE A 99 35.204 -14.158 24.723 1.00 46.03 C ATOM 791 CG1 ILE A 99 34.995 -13.347 23.439 1.00 47.09 C ATOM 792 CG2 ILE A 99 33.864 -14.347 25.435 1.00 43.98 C ATOM 793 CD1 ILE A 99 34.273 -14.106 22.329 1.00 48.97 C ATOM 794 N GLY A 100 37.714 -15.131 26.414 1.00 46.07 N ATOM 795 CA GLY A 100 38.254 -16.078 27.369 1.00 46.94 C ATOM 796 C GLY A 100 38.708 -15.396 28.651 1.00 46.97 C ATOM 797 O GLY A 100 38.371 -15.834 29.757 1.00 47.51 O ATOM 798 N GLU A 101 39.462 -14.310 28.509 1.00 45.69 N ATOM 799 CA GLU A 101 39.954 -13.587 29.672 1.00 47.11 C ATOM 800 C GLU A 101 38.816 -13.132 30.587 1.00 48.00 C ATOM 801 O GLU A 101 38.986 -13.016 31.806 1.00 47.58 O ATOM 802 CB GLU A 101 40.789 -12.383 29.231 1.00 45.74 C ATOM 803 CG GLU A 101 41.978 -12.758 28.381 1.00 46.06 C ATOM 804 CD GLU A 101 42.814 -11.568 27.983 1.00 46.41 C ATOM 805 OE1 GLU A 101 42.312 -10.702 27.243 1.00 46.56 O ATOM 806 OE2 GLU A 101 43.978 -11.489 28.419 1.00 47.62 O ATOM 807 N LEU A 102 37.649 -12.893 30.001 1.00 48.71 N ATOM 808 CA LEU A 102 36.500 -12.453 30.778 1.00 51.92 C ATOM 809 C LEU A 102 35.796 -13.596 31.485 1.00 56.61 C ATOM 810 O LEU A 102 35.510 -13.512 32.686 1.00 55.14 O ATOM 811 CB LEU A 102 35.496 -11.729 29.881 1.00 48.33 C ATOM 812 CG LEU A 102 35.806 -10.301 29.455 1.00 45.17 C ATOM 813 CD1 LEU A 102 34.721 -9.833 28.513 1.00 45.24 C ATOM 814 CD2 LEU A 102 35.884 -9.397 30.666 1.00 41.48 C ATOM 815 N GLU A 103 35.509 -14.657 30.725 1.00 64.22 N ATOM 816 CA GLU A 103 34.811 -15.832 31.253 1.00 71.41 C ATOM 817 C GLU A 103 35.671 -16.627 32.237 1.00 74.08 C ATOM 818 O GLU A 103 35.144 -17.429 33.009 1.00 74.29 O ATOM 819 CB GLU A 103 34.323 -16.750 30.108 1.00 73.28 C ATOM 820 CG GLU A 103 33.285 -16.099 29.164 1.00 78.64 C ATOM 821 CD GLU A 103 32.284 -17.088 28.553 1.00 81.15 C ATOM 822 OE1 GLU A 103 32.726 -18.138 28.025 1.00 83.46 O ATOM 823 OE2 GLU A 103 31.057 -16.802 28.585 1.00 80.50 O ATOM 824 N ARG A 104 36.984 -16.386 32.224 1.00 77.62 N ATOM 825 CA ARG A 104 37.893 -17.092 33.119 1.00 81.44 C ATOM 826 C ARG A 104 38.007 -16.368 34.453 1.00 84.10 C ATOM 827 O ARG A 104 38.491 -16.932 35.427 1.00 84.66 O ATOM 828 CB ARG A 104 39.286 -17.249 32.487 1.00 82.25 C ATOM 829 CG ARG A 104 40.189 -16.025 32.588 1.00 86.31 C ATOM 830 CD ARG A 104 41.629 -16.309 32.126 1.00 89.78 C ATOM 831 NE ARG A 104 42.619 -15.549 32.899 1.00 94.54 N ATOM 832 CZ ARG A 104 42.768 -14.222 32.876 1.00 95.85 C ATOM 833 NH1 ARG A 104 41.992 -13.471 32.107 1.00 96.32 N ATOM 834 NH2 ARG A 104 43.688 -13.639 33.643 1.00 96.27 N ATOM 835 N MET A 105 37.551 -15.120 34.493 1.00 87.83 N ATOM 836 CA MET A 105 37.595 -14.330 35.717 1.00 91.68 C ATOM 837 C MET A 105 36.847 -15.073 36.814 1.00 97.01 C ATOM 838 O MET A 105 35.642 -15.302 36.695 1.00 97.48 O ATOM 839 CB MET A 105 36.938 -12.971 35.507 1.00 88.72 C ATOM 840 CG MET A 105 37.432 -11.919 36.475 1.00 85.78 C ATOM 841 SD MET A 105 38.792 -10.929 35.762 1.00 83.19 S ATOM 842 CE MET A 105 40.053 -12.179 35.433 1.00 82.23 C ATOM 843 N THR A 106 37.564 -15.441 37.880 1.00103.34 N ATOM 844 CA THR A 106 36.987 -16.183 39.017 1.00108.81 C ATOM 845 C THR A 106 35.896 -15.404 39.763 1.00113.27 C ATOM 846 O THR A 106 35.073 -16.010 40.455 1.00113.96 O ATOM 847 CB THR A 106 38.082 -16.619 40.045 1.00108.13 C ATOM 848 OG1 THR A 106 39.078 -17.412 39.381 1.00108.41 O ATOM 849 CG2 THR A 106 37.459 -17.460 41.158 1.00107.61 C ATOM 850 N GLN A 107 35.897 -14.072 39.643 1.00117.82 N ATOM 851 CA GLN A 107 34.871 -13.241 40.292 1.00121.43 C ATOM 852 C GLN A 107 33.618 -13.360 39.407 1.00123.59 C ATOM 853 O GLN A 107 32.496 -13.072 39.843 1.00123.30 O ATOM 854 CB GLN A 107 35.323 -11.777 40.382 1.00121.56 C ATOM 855 CG GLN A 107 34.415 -10.876 41.236 1.00121.95 C ATOM 856 CD GLN A 107 34.828 -10.812 42.703 1.00122.07 C ATOM 857 OE1 GLN A 107 34.315 -9.990 43.470 1.00121.30 O ATOM 858 NE2 GLN A 107 35.757 -11.679 43.100 1.00122.50 N ATOM 859 N PHE A 108 33.843 -13.779 38.158 1.00125.81 N ATOM 860 CA PHE A 108 32.773 -14.000 37.195 1.00127.97 C ATOM 861 C PHE A 108 32.202 -15.406 37.406 1.00129.93 C ATOM 862 O PHE A 108 31.012 -15.570 37.665 1.00130.41 O ATOM 863 CB PHE A 108 33.279 -13.888 35.750 1.00127.07 C ATOM 864 CG PHE A 108 32.412 -14.633 34.751 1.00126.70 C ATOM 865 CD1 PHE A 108 31.105 -14.224 34.494 1.00126.03 C ATOM 866 CD2 PHE A 108 32.885 -15.780 34.116 1.00125.90 C ATOM 867 CE1 PHE A 108 30.285 -14.944 33.624 1.00124.77 C ATOM 868 CE2 PHE A 108 32.074 -16.508 33.245 1.00124.86 C ATOM 869 CZ PHE A 108 30.771 -16.088 33.001 1.00124.86 C ATOM 870 N LYS A 109 33.061 -16.417 37.289 1.00131.89 N ATOM 871 CA LYS A 109 32.652 -17.813 37.452 1.00133.84 C ATOM 872 C LYS A 109 31.949 -18.075 38.794 1.00135.35 C ATOM 873 O LYS A 109 31.271 -19.096 38.962 1.00135.12 O ATOM 874 CB LYS A 109 33.873 -18.735 37.318 1.00133.46 C ATOM 875 CG LYS A 109 34.700 -18.498 36.056 1.00132.76 C ATOM 876 CD LYS A 109 36.028 -19.257 36.084 1.00132.19 C ATOM 877 CE LYS A 109 35.873 -20.722 35.700 1.00131.47 C ATOM 878 NZ LYS A 109 34.996 -21.490 36.620 1.00130.86 N ATOM 879 N GLU A 110 32.115 -17.151 39.741 1.00137.66 N ATOM 880 CA GLU A 110 31.499 -17.260 41.070 1.00139.60 C ATOM 881 C GLU A 110 29.988 -16.989 41.052 1.00139.49 C ATOM 882 O GLU A 110 29.189 -17.838 41.470 1.00139.13 O ATOM 883 CB GLU A 110 32.178 -16.288 42.061 1.00141.35 C ATOM 884 CG GLU A 110 33.374 -16.860 42.834 1.00142.24 C ATOM 885 CD GLU A 110 33.971 -15.861 43.821 1.00142.65 C ATOM 886 OE1 GLU A 110 34.610 -14.881 43.378 1.00142.25 O ATOM 887 OE2 GLU A 110 33.783 -16.053 45.042 1.00143.18 O ATOM 888 N LYS A 111 29.607 -15.806 40.567 1.00139.13 N ATOM 889 CA LYS A 111 28.200 -15.405 40.506 1.00137.87 C ATOM 890 C LYS A 111 27.463 -15.935 39.268 1.00137.48 C ATOM 891 O LYS A 111 26.232 -15.860 39.204 1.00137.07 O ATOM 892 CB LYS A 111 28.086 -13.873 40.566 1.00136.65 C ATOM 893 CG LYS A 111 28.697 -13.239 41.816 1.00135.15 C ATOM 894 CD LYS A 111 28.347 -11.761 41.908 1.00133.95 C ATOM 895 CE LYS A 111 28.967 -11.113 43.138 1.00132.88 C ATOM 896 NZ LYS A 111 28.531 -9.695 43.308 1.00130.97 N ATOM 897 N SER A 112 28.220 -16.478 38.309 1.00137.11 N ATOM 898 CA SER A 112 27.664 -17.026 37.064 1.00136.39 C ATOM 899 C SER A 112 27.247 -18.488 37.212 1.00135.82 C ATOM 900 O SER A 112 26.800 -19.123 36.253 1.00135.88 O ATOM 901 CB SER A 112 28.679 -16.895 35.910 1.00136.44 C ATOM 902 OG SER A 112 29.816 -17.726 36.078 1.00135.88 O ATOM 903 N ALA A 113 27.394 -19.013 38.425 1.00134.83 N ATOM 904 CA ALA A 113 27.039 -20.396 38.719 1.00133.30 C ATOM 905 C ALA A 113 25.698 -20.490 39.452 1.00132.21 C ATOM 906 O ALA A 113 24.901 -21.388 39.177 1.00132.37 O ATOM 907 CB ALA A 113 28.146 -21.048 39.550 1.00133.08 C ATOM 908 N GLY A 114 25.455 -19.553 40.372 1.00130.59 N ATOM 909 CA GLY A 114 24.217 -19.542 41.143 1.00127.55 C ATOM 910 C GLY A 114 23.119 -18.616 40.636 1.00125.21 C ATOM 911 O GLY A 114 22.748 -17.652 41.316 1.00125.20 O ATOM 912 N ALA A 115 22.608 -18.921 39.441 1.00122.37 N ATOM 913 CA ALA A 115 21.538 -18.153 38.788 1.00118.73 C ATOM 914 C ALA A 115 21.141 -18.748 37.417 1.00115.45 C ATOM 915 O ALA A 115 21.914 -19.490 36.795 1.00115.93 O ATOM 916 CB ALA A 115 21.971 -16.694 38.615 1.00119.15 C ATOM 917 N ALA A 116 19.927 -18.425 36.966 1.00109.85 N ATOM 918 CA ALA A 116 19.420 -18.895 35.678 1.00103.87 C ATOM 919 C ALA A 116 19.934 -17.954 34.587 1.00100.00 C ATOM 920 O ALA A 116 20.465 -18.396 33.565 1.00101.21 O ATOM 921 CB ALA A 116 17.892 -18.908 35.687 1.00103.61 C ATOM 922 N ALA A 117 19.776 -16.651 34.826 1.00 93.40 N ATOM 923 CA ALA A 117 20.224 -15.614 33.897 1.00 84.92 C ATOM 924 C ALA A 117 20.728 -14.379 34.655 1.00 79.75 C ATOM 925 O ALA A 117 19.994 -13.777 35.445 1.00 78.32 O ATOM 926 CB ALA A 117 19.087 -15.226 32.955 1.00 84.96 C ATOM 927 N ALA A 118 21.986 -14.014 34.403 1.00 73.36 N ATOM 928 CA ALA A 118 22.615 -12.854 35.034 1.00 66.21 C ATOM 929 C ALA A 118 22.816 -11.722 34.015 1.00 61.16 C ATOM 930 O ALA A 118 22.862 -11.966 32.807 1.00 59.42 O ATOM 931 CB ALA A 118 23.957 -13.258 35.637 1.00 64.38 C ATOM 932 N ALA A 119 22.923 -10.489 34.507 1.00 55.06 N ATOM 933 CA ALA A 119 23.130 -9.329 33.644 1.00 48.78 C ATOM 934 C ALA A 119 24.463 -9.501 32.950 1.00 44.48 C ATOM 935 O ALA A 119 25.425 -9.966 33.551 1.00 43.90 O ATOM 936 CB ALA A 119 23.148 -8.042 34.464 1.00 47.68 C ATOM 937 N ALA A 120 24.525 -9.125 31.683 1.00 41.00 N ATOM 938 CA ALA A 120 25.764 -9.246 30.936 1.00 39.04 C ATOM 939 C ALA A 120 26.821 -8.374 31.593 1.00 38.42 C ATOM 940 O ALA A 120 28.015 -8.525 31.332 1.00 38.18 O ATOM 941 CB ALA A 120 25.546 -8.811 29.498 1.00 38.12 C ATOM 942 N GLY A 121 26.371 -7.463 32.455 1.00 37.96 N ATOM 943 CA GLY A 121 27.286 -6.567 33.143 1.00 35.58 C ATOM 944 C GLY A 121 28.187 -7.278 34.128 1.00 33.69 C ATOM 945 O GLY A 121 29.290 -6.818 34.418 1.00 32.63 O ATOM 946 N LEU A 122 27.700 -8.405 34.639 1.00 33.98 N ATOM 947 CA LEU A 122 28.438 -9.223 35.589 1.00 32.91 C ATOM 948 C LEU A 122 29.578 -9.944 34.899 1.00 32.78 C ATOM 949 O LEU A 122 30.400 -10.563 35.553 1.00 33.98 O ATOM 950 CB LEU A 122 27.517 -10.255 36.227 1.00 31.17 C ATOM 951 CG LEU A 122 27.254 -10.122 37.717 1.00 30.91 C ATOM 952 CD1 LEU A 122 26.727 -8.748 38.016 1.00 33.24 C ATOM 953 CD2 LEU A 122 26.258 -11.165 38.142 1.00 31.73 C ATOM 954 N LEU A 123 29.625 -9.867 33.578 1.00 34.09 N ATOM 955 CA LEU A 123 30.675 -10.529 32.821 1.00 36.84 C ATOM 956 C LEU A 123 31.508 -9.519 32.074 1.00 37.65 C ATOM 957 O LEU A 123 32.604 -9.825 31.597 1.00 36.29 O ATOM 958 CB LEU A 123 30.067 -11.517 31.815 1.00 40.56 C ATOM 959 CG LEU A 123 30.949 -11.930 30.619 1.00 42.15 C ATOM 960 CD1 LEU A 123 32.082 -12.824 31.087 1.00 42.72 C ATOM 961 CD2 LEU A 123 30.110 -12.658 29.581 1.00 43.37 C ATOM 962 N THR A 124 30.992 -8.304 31.962 1.00 39.54 N ATOM 963 CA THR A 124 31.720 -7.285 31.217 1.00 40.75 C ATOM 964 C THR A 124 32.237 -6.102 32.023 1.00 41.18 C ATOM 965 O THR A 124 32.729 -5.128 31.436 1.00 42.00 O ATOM 966 CB THR A 124 30.858 -6.752 30.065 1.00 40.47 C ATOM 967 OG1 THR A 124 29.607 -6.277 30.588 1.00 41.72 O ATOM 968 CG2 THR A 124 30.601 -7.862 29.068 1.00 40.50 C ATOM 969 N TYR A 125 32.153 -6.182 33.352 1.00 39.56 N ATOM 970 CA TYR A 125 32.641 -5.086 34.182 1.00 37.65 C ATOM 971 C TYR A 125 34.167 -4.976 34.211 1.00 34.56 C ATOM 972 O TYR A 125 34.699 -3.893 34.386 1.00 35.84 O ATOM 973 CB TYR A 125 32.091 -5.188 35.611 1.00 37.31 C ATOM 974 CG TYR A 125 32.680 -6.305 36.423 1.00 39.44 C ATOM 975 CD1 TYR A 125 33.878 -6.147 37.129 1.00 39.86 C ATOM 976 CD2 TYR A 125 32.040 -7.531 36.476 1.00 41.80 C ATOM 977 CE1 TYR A 125 34.419 -7.206 37.874 1.00 41.73 C ATOM 978 CE2 TYR A 125 32.561 -8.592 37.209 1.00 44.70 C ATOM 979 CZ TYR A 125 33.753 -8.430 37.908 1.00 44.24 C ATOM 980 OH TYR A 125 34.251 -9.509 38.611 1.00 43.85 O ATOM 981 N PRO A 126 34.888 -6.085 34.029 1.00 30.49 N ATOM 982 CA PRO A 126 36.342 -5.987 34.052 1.00 29.74 C ATOM 983 C PRO A 126 36.883 -4.890 33.155 1.00 29.15 C ATOM 984 O PRO A 126 37.654 -4.032 33.603 1.00 30.94 O ATOM 985 CB PRO A 126 36.783 -7.364 33.605 1.00 28.01 C ATOM 986 CG PRO A 126 35.775 -8.207 34.287 1.00 31.84 C ATOM 987 CD PRO A 126 34.478 -7.488 33.974 1.00 30.72 C ATOM 988 N PRO A 127 36.493 -4.882 31.878 1.00 26.85 N ATOM 989 CA PRO A 127 37.001 -3.837 30.987 1.00 24.54 C ATOM 990 C PRO A 127 36.707 -2.416 31.516 1.00 22.87 C ATOM 991 O PRO A 127 37.512 -1.500 31.322 1.00 20.48 O ATOM 992 CB PRO A 127 36.293 -4.147 29.675 1.00 24.42 C ATOM 993 CG PRO A 127 36.123 -5.614 29.736 1.00 26.58 C ATOM 994 CD PRO A 127 35.630 -5.811 31.144 1.00 25.47 C ATOM 995 N LEU A 128 35.564 -2.239 32.183 1.00 20.66 N ATOM 996 CA LEU A 128 35.189 -0.936 32.737 1.00 20.78 C ATOM 997 C LEU A 128 36.081 -0.599 33.936 1.00 24.99 C ATOM 998 O LEU A 128 36.550 0.532 34.064 1.00 22.39 O ATOM 999 CB LEU A 128 33.725 -0.942 33.175 1.00 16.78 C ATOM 1000 CG LEU A 128 33.218 0.237 33.994 1.00 11.4