HEADER HYDROLASE/HYDROLASE INHIBITOR 01-MAY-95 1BMA TITLE BENZYL METHYL AMINIMIDE INHIBITOR COMPLEXED TO PORCINE PANCREATIC TITLE 2 ELASTASE COMPND MOL_ID: 1; COMPND 2 MOLECULE: CHYMOTRYPSIN-LIKE ELASTASE FAMILY MEMBER 1; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: ELASTASE-1; COMPND 5 EC: 3.4.21.36 SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SUS SCROFA; SOURCE 3 ORGANISM_COMMON: PIGS,SWINE,WILD BOAR; SOURCE 4 ORGANISM_TAXID: 9823; SOURCE 5 ORGAN: PANCREAS KEYWDS SERINE PROTEASE,METAL-BINDING, PROTEASE, SECRETED, ZYMOGEN, KEYWDS 2 HYDROLASE-HYDROLASE INHIBITOR COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR E.PEISACH,D.CASEBIER,S.L.GALLION,P.FURTH,G.A.PETSKO,J.C.HOGAN JR., AUTHOR 2 D.RINGE REVDAT 4 13-JUL-11 1BMA 1 VERSN REVDAT 3 24-FEB-09 1BMA 1 VERSN REVDAT 2 01-APR-03 1BMA 1 JRNL REVDAT 1 07-DEC-95 1BMA 0 JRNL AUTH E.PEISACH,D.CASEBIER,S.L.GALLION,P.FURTH,G.A.PETSKO, JRNL AUTH 2 J.C.HOGAN JR.,D.RINGE JRNL TITL INTERACTION OF A PEPTIDOMIMETIC AMINIMIDE INHIBITOR WITH JRNL TITL 2 ELASTASE. JRNL REF SCIENCE V. 269 66 1995 JRNL REFN ISSN 0036-8075 JRNL PMID 7604279 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH C.MATTOS,D.A.GIAMMONA,G.A.PETSKO,D.RINGE REMARK 1 TITL STRUCTURAL ANALYSIS OF THE ACTIVE SITE OF PORCINE PANCREATIC REMARK 1 TITL 2 ELASTASE BASED ON THE X-RAY CRYSTAL STRUCTURES OF COMPLEXES REMARK 1 TITL 3 WITH TRIFLUOROACETYL-DIPEPTIDE-ANILIDE INHIBITORS REMARK 1 REF BIOCHEMISTRY V. 34 3193 1995 REMARK 1 REFN ISSN 0006-2960 REMARK 1 REFERENCE 2 REMARK 1 AUTH I.LI DE LA SIERRA,E.PAPAMICHAEL,C.SAKARELOS,J.-L.DIMICOLI, REMARK 1 AUTH 2 T.PRANGE REMARK 1 TITL INTERACTION OF THE PEPTIDE CF3-LEU-ALA-NH-C6H4-CF3 (TFLA) REMARK 1 TITL 2 WITH PORCINE PANCREATIC ELASTASE. X-RAY STUDIES AT 1.8 REMARK 1 TITL 3 ANGSTROMS REMARK 1 REF J.MOL.RECOG. V. 3 36 1990 REMARK 1 REFN ISSN 0952-3499 REMARK 1 REFERENCE 3 REMARK 1 AUTH E.MEYER,G.COLE,R.RADHAKRISHNAN,O.EPP REMARK 1 TITL STRUCTURE OF NATIVE PORCINE PANCREATIC ELASTASE AT 1.65 REMARK 1 TITL 2 ANGSTROMS RESOLUTION REMARK 1 REF ACTA CRYSTALLOGR.,SECT.B V. 44 26 1988 REMARK 1 REFN ISSN 0108-7681 REMARK 1 REFERENCE 4 REMARK 1 AUTH E.MEYER,R.RADHAKRISHNAN,G.COLE,L.G.PRESTA REMARK 1 TITL STRUCTURE OF THE PRODUCT COMPLEX OF ACETYL-ALA-PRO-ALA WITH REMARK 1 TITL 2 PORCINE PANCREATIC ELASTASE AT 1.65 ANGSTROMS RESOLUTION REMARK 1 REF J.MOL.BIOL. V. 189 533 1986 REMARK 1 REFN ISSN 0022-2836 REMARK 1 REFERENCE 5 REMARK 1 AUTH D.L.HUGHES,L.C.DIECKER,L.C.BIETH,J.-L.DIMICOLI REMARK 1 TITL CRYSTALLOGRAPHIC STUDY OF THE BINDING OF A TRI-FLUOROACETYL REMARK 1 TITL 2 DIPEPTIDE ANILIDE INHIBITOR WITH ELASTASE REMARK 1 REF J.MOL.BIOL. V. 162 645 1982 REMARK 1 REFN ISSN 0022-2836 REMARK 1 REFERENCE 6 REMARK 1 AUTH J.-L.DIMICOLI,A.RENAUD,J.BIETH REMARK 1 TITL THE INDIRECT MECHANISM OF ACTION OF THE TRIFLUOROACETYL REMARK 1 TITL 2 PEPTIDES ON ELASTASE REMARK 1 REF EUR.J.BIOCHEM. V. 107 423 1980 REMARK 1 REFN ISSN 0014-2956 REMARK 1 REFERENCE 7 REMARK 1 AUTH L.SAWYER,C.M.SHOTTON,J.W.CAMPBELL,P.L.WENDELL,H.MUIRHEAD, REMARK 1 AUTH 2 H.C.WATSON,R.DIAMOND,R.C.LADNER REMARK 1 TITL THE ATOMIC STRUCTURE OF CRYSTALLINE PORCINE PANCREATIC REMARK 1 TITL 2 ELASTASE AT 2.5 ANGSTROMS RESOLUTION. COMPARISONS WITH THE REMARK 1 TITL 3 STRUCTURE OF ALPHA-CHYMOTRYPSIN REMARK 1 REF J.MOL.BIOL. V. 118 137 1978 REMARK 1 REFN ISSN 0022-2836 REMARK 2 REMARK 2 RESOLUTION. 1.80 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.1 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) : 10.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 58.7 REMARK 3 NUMBER OF REFLECTIONS : 44505 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) : 0.192 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 : 43 REMARK 3 SOLVENT ATOMS : 134 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.50 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) : 0.015 REMARK 3 BOND ANGLES (DEGREES) : 2.70 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 26.80 REMARK 3 IMPROPER ANGLES (DEGREES) : 1.01 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 1BMA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 20-MAY-94 REMARK 200 TEMPERATURE (KELVIN) : NULL REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : NULL REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : N REMARK 200 RADIATION SOURCE : NULL REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.5148 REMARK 200 MONOCHROMATOR : NI FILTER REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : NULL REMARK 200 DETECTOR MANUFACTURER : SIEMENS REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : NULL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39545 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800 REMARK 200 RESOLUTION RANGE LOW (A) : 10.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 58.7 REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : 0.06300 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 3.1 REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 43.84 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: THE INHIBITOR WAS SOAKED INTO THE REMARK 280 GROWN CRYSTALS USING A 4 MM STOCK SOLUTION OF THE INHIBITOR IN REMARK 280 10% ACETONITRILE. 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 26.08000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 37.76000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 28.84000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 37.76000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.08000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 28.84000 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 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 60 NE2 HIS A 60 CD2 -0.073 REMARK 500 HIS A 75 NE2 HIS A 75 CD2 -0.070 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 27 CD1 - CG - CD2 ANGL. DEV. = 6.1 DEGREES REMARK 500 TRP A 27 CE2 - CD2 - CG ANGL. DEV. = -5.9 DEGREES REMARK 500 ARG A 36 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES REMARK 500 TRP A 41 CD1 - CG - CD2 ANGL. DEV. = 7.3 DEGREES REMARK 500 TRP A 41 CE2 - CD2 - CG ANGL. DEV. = -6.1 DEGREES REMARK 500 ARG A 51 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES REMARK 500 TRP A 54 CD1 - CG - CD2 ANGL. DEV. = 5.5 DEGREES REMARK 500 TRP A 54 CE2 - CD2 - CG ANGL. DEV. = -5.3 DEGREES REMARK 500 ARG A 64 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES REMARK 500 TRP A 98 CD1 - CG - CD2 ANGL. DEV. = 5.0 DEGREES REMARK 500 TRP A 98 CE2 - CD2 - CG ANGL. DEV. = -5.1 DEGREES REMARK 500 TRP A 147 CD1 - CG - CD2 ANGL. DEV. = 6.3 DEGREES REMARK 500 TRP A 147 CE2 - CD2 - CG ANGL. DEV. = -5.5 DEGREES REMARK 500 ARG A 151 CA - CB - CG ANGL. DEV. = 14.0 DEGREES REMARK 500 ARG A 151 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES REMARK 500 TRP A 179 CD1 - CG - CD2 ANGL. DEV. = 6.3 DEGREES REMARK 500 TRP A 179 CE2 - CD2 - CG ANGL. DEV. = -5.3 DEGREES REMARK 500 ARG A 226 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES REMARK 500 ARG A 240 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES REMARK 500 TRP A 247 CD1 - CG - CD2 ANGL. DEV. = 6.2 DEGREES REMARK 500 TRP A 247 CE2 - CD2 - CG ANGL. DEV. = -5.1 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 HIS A 75 -55.40 -129.50 REMARK 500 TYR A 178 -113.73 -104.95 REMARK 500 SER A 203 135.31 -37.60 REMARK 500 SER A 222 -56.81 -120.48 REMARK 500 REMARK 500 REMARK: NULL REMARK 600 REMARK 600 HETEROGEN REMARK 600 NOTE THAT SUBCOMPONENT MBH IS REFERRED TO AS MBA IN THE PAPER REMARK 600 CITED IN THE JRNL RECORDS ABOVE. REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A 280 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLU A 84 OE2 REMARK 620 2 GLN A 79 O 93.3 REMARK 620 3 HOH A 355 O 84.6 90.9 REMARK 620 4 ASN A 81 OD1 83.2 93.3 167.3 REMARK 620 5 GLU A 74 OE1 94.5 163.5 104.3 73.2 REMARK 620 6 ASN A 76 O 169.8 87.8 105.6 86.5 82.0 REMARK 620 7 GLU A 74 OE2 95.9 150.8 62.5 115.3 42.2 88.0 REMARK 620 N 1 2 3 4 5 6 REMARK 630 REMARK 630 MOLECULE TYPE: NULL REMARK 630 MOLECULE NAME: (1R)-1-BENZYL-1-METHYL-1-(2-{[4-(1-METHYLETHYL) REMARK 630 PHENYL]AMINO}-2-OXOETHYL)-2-{(2S)-4-METHYL-2-[(TRIFLUOROACETYL) REMARK 630 AMINO]PENTANOYL}DIAZANIUM REMARK 630 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 630 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 630 REMARK 630 M RES C SSSEQI REMARK 630 0QH A 256 REMARK 630 SOURCE: NULL REMARK 630 TAXONOMY: NULL REMARK 630 SUBCOMP: TFA LEU MBH ISO REMARK 630 DETAILS: NULL REMARK 700 REMARK 700 SHEET REMARK 700 THE SHEETS PRESENTED AS *S1* AND *S2* IN SHEET RECORDS REMARK 700 BELOW ARE ACTUALLY TWO SIX-STRANDED BETA-BARRELS. THIS IS REMARK 700 REPRESENTED BY TWO SEVEN-STRANDED SHEETS IN WHICH THE FIRST REMARK 700 AND LAST STRANDS OF EACH SHEET ARE IDENTICAL. REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 280 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 290 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0QH A 256 REMARK 800 REMARK 800 SITE_IDENTIFIER: CAT REMARK 800 EVIDENCE_CODE: AUTHOR REMARK 800 SITE_DESCRIPTION: CATALYTIC TRIAD REMARK 999 REMARK 999 SEQUENCE REMARK 999 THE RESIDUE NUMBERING SCHEME FOR THE PROTEIN IS SEQUENTIAL REMARK 999 STARTING WITH VAL A 16 AND ENDING WITH ASN A 255. REMARK 999 REMARK 999 THE IDENTITY OF ASN A 81 AGREES WITH THE SEQUENCES OF REMARK 999 SEVERAL OTHER ELASTASE STRUCTURES. THE AUTHORS, THEREFORE, REMARK 999 BELIEVE IT TO BE CORRECT. DBREF 1BMA A 16 255 UNP P00772 CELA1_PIG 27 266 SEQADV 1BMA ASN A 81 UNP P00772 ASP 92 CONFLICT SEQRES 1 A 240 VAL VAL GLY GLY THR GLU ALA GLN ARG ASN SER TRP PRO SEQRES 2 A 240 SER GLN ILE SER LEU GLN TYR ARG SER GLY SER SER TRP SEQRES 3 A 240 ALA HIS THR CYS GLY GLY THR LEU ILE ARG GLN ASN TRP SEQRES 4 A 240 VAL MET THR ALA ALA HIS CYS VAL ASP ARG GLU LEU THR SEQRES 5 A 240 PHE ARG VAL VAL VAL GLY GLU HIS ASN LEU ASN GLN ASN SEQRES 6 A 240 ASN GLY THR GLU GLN TYR VAL GLY VAL GLN LYS ILE VAL SEQRES 7 A 240 VAL HIS PRO TYR TRP ASN THR ASP ASP VAL ALA ALA GLY SEQRES 8 A 240 TYR ASP ILE ALA LEU LEU ARG LEU ALA GLN SER VAL THR SEQRES 9 A 240 LEU ASN SER TYR VAL GLN LEU GLY VAL LEU PRO ARG ALA SEQRES 10 A 240 GLY THR ILE LEU ALA ASN ASN SER PRO CYS TYR ILE THR SEQRES 11 A 240 GLY TRP GLY LEU THR ARG THR ASN GLY GLN LEU ALA GLN SEQRES 12 A 240 THR LEU GLN GLN ALA TYR LEU PRO THR VAL ASP TYR ALA SEQRES 13 A 240 ILE CYS SER SER SER SER TYR TRP GLY SER THR VAL LYS SEQRES 14 A 240 ASN SER MET VAL CYS ALA GLY GLY ASP GLY VAL ARG SER SEQRES 15 A 240 GLY CYS GLN GLY ASP SER GLY GLY PRO LEU HIS CYS LEU SEQRES 16 A 240 VAL ASN GLY GLN TYR ALA VAL HIS GLY VAL THR SER PHE SEQRES 17 A 240 VAL SER ARG LEU GLY CYS ASN VAL THR ARG LYS PRO THR SEQRES 18 A 240 VAL PHE THR ARG VAL SER ALA TYR ILE SER TRP ILE ASN SEQRES 19 A 240 ASN VAL ILE ALA SER ASN HET CA A 280 1 HET SO4 A 290 5 HET 0QH A 256 37 HETNAM CA CALCIUM ION HETNAM SO4 SULFATE ION HETNAM 0QH (1R)-1-BENZYL-1-METHYL-1-(2-{[4-(1-METHYLETHYL) HETNAM 2 0QH PHENYL]AMINO}-2-OXOETHYL)-2-{(2S)-4-METHYL-2- HETNAM 3 0QH [(TRIFLUOROACETYL)AMINO]PENTANOYL}DIAZANIUM FORMUL 2 CA CA 2+ FORMUL 3 SO4 O4 S 2- FORMUL 4 0QH C27 H36 F3 N4 O3 1+ FORMUL 5 HOH *134(H2 O) HELIX 1 H1 ASP A 169 SER A 175 1 7 HELIX 2 H2 TYR A 244 ASN A 255 1 12 SHEET 1 S1 7 SER A 29 SER A 37 0 SHEET 2 S1 7 SER A 40 ILE A 50 -1 SHEET 3 S1 7 ASN A 53 ALA A 59 -1 SHEET 4 S1 7 ASP A 108 GLN A 116 -1 SHEET 5 S1 7 GLU A 84 HIS A 95 -1 SHEET 6 S1 7 PHE A 68 GLY A 73 -1 SHEET 7 S1 7 SER A 29 SER A 37 -1 SHEET 1 S2 7 ASN A 139 THR A 150 0 SHEET 2 S2 7 GLY A 154 VAL A 168 -1 SHEET 3 S2 7 SER A 186 VAL A 195 -1 SHEET 4 S2 7 ASN A 230 VAL A 241 -1 SHEET 5 S2 7 HIS A 218 VAL A 224 -1 SHEET 6 S2 7 SER A 203 CYS A 209 -1 SHEET 7 S2 7 SER A 140 THR A 150 -1 SHEET 1 S3 3 GLY A 154 ALA A 157 0 SHEET 2 S3 3 TRP A 147 LEU A 149 -1 SHEET 3 S3 3 GLN A 200 ASP A 202 -1 SSBOND 1 CYS A 45 CYS A 61 1555 1555 2.02 SSBOND 2 CYS A 142 CYS A 209 1555 1555 2.01 SSBOND 3 CYS A 173 CYS A 189 1555 1555 2.01 SSBOND 4 CYS A 199 CYS A 229 1555 1555 2.01 LINK CA CA A 280 OE2 GLU A 84 1555 1555 2.51 LINK CA CA A 280 O GLN A 79 1555 1555 2.37 LINK CA CA A 280 O HOH A 355 1555 1555 2.53 LINK CA CA A 280 OD1 ASN A 81 1555 1555 2.52 LINK CA CA A 280 OE1 GLU A 74 1555 1555 2.50 LINK CA CA A 280 O ASN A 76 1555 1555 2.37 LINK CA CA A 280 OE2 GLU A 74 1555 1555 3.09 SITE 1 AC1 6 GLU A 74 ASN A 76 GLN A 79 ASN A 81 SITE 2 AC1 6 GLU A 84 HOH A 355 SITE 1 AC2 5 GLY A 133 ARG A 151 ARG A 240 HOH A 340 SITE 2 AC2 5 HOH A 345 SITE 1 AC3 17 GLU A 65 LEU A 66 THR A 67 VAL A 103 SITE 2 AC3 17 THR A 152 THR A 182 CYS A 199 GLN A 200 SITE 3 AC3 17 SER A 203 THR A 221 SER A 222 PHE A 223 SITE 4 AC3 17 VAL A 224 SER A 225 ARG A 226 GLY A 228 SITE 5 AC3 17 CYS A 229 SITE 1 CAT 3 ASP A 108 HIS A 60 SER A 203 CRYST1 52.160 57.680 75.520 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 0.019172 0.000000 0.000000 0.00000 SCALE2 0.000000 0.017337 0.000000 0.00000 SCALE3 0.000000 0.000000 0.013242 0.00000 ATOM 1 N VAL A 16 41.593 32.726 35.179 1.00 5.92 N ATOM 2 CA VAL A 16 40.667 33.462 36.045 1.00 5.90 C ATOM 3 C VAL A 16 39.544 34.005 35.167 1.00 9.05 C ATOM 4 O VAL A 16 39.830 34.764 34.220 1.00 10.48 O ATOM 5 CB VAL A 16 41.446 34.646 36.763 1.00 3.34 C ATOM 6 CG1 VAL A 16 40.479 35.497 37.575 1.00 5.02 C ATOM 7 CG2 VAL A 16 42.485 34.116 37.761 1.00 7.03 C ATOM 8 N VAL A 17 38.276 33.667 35.460 1.00 9.38 N ATOM 9 CA VAL A 17 37.124 34.221 34.774 1.00 8.32 C ATOM 10 C VAL A 17 36.701 35.486 35.515 1.00 10.66 C ATOM 11 O VAL A 17 36.731 35.504 36.741 1.00 10.27 O ATOM 12 CB VAL A 17 35.956 33.225 34.766 1.00 6.81 C ATOM 13 CG1 VAL A 17 34.839 33.738 33.857 1.00 6.95 C ATOM 14 CG2 VAL A 17 36.405 31.908 34.179 1.00 7.97 C ATOM 15 N GLY A 18 36.334 36.574 34.832 1.00 9.48 N ATOM 16 CA GLY A 18 35.822 37.755 35.533 1.00 10.87 C ATOM 17 C GLY A 18 36.915 38.523 36.270 1.00 12.24 C ATOM 18 O GLY A 18 36.678 39.227 37.249 1.00 14.40 O ATOM 19 N GLY A 19 38.145 38.374 35.824 1.00 12.48 N ATOM 20 CA GLY A 19 39.268 39.043 36.456 1.00 14.94 C ATOM 21 C GLY A 19 39.626 40.361 35.784 1.00 16.65 C ATOM 22 O GLY A 19 38.950 40.814 34.852 1.00 18.12 O ATOM 23 N THR A 20 40.656 41.023 36.329 1.00 17.53 N ATOM 24 CA THR A 20 41.215 42.247 35.786 1.00 18.60 C ATOM 25 C THR A 20 42.711 42.021 35.745 1.00 18.76 C ATOM 26 O THR A 20 43.229 41.126 36.410 1.00 18.06 O ATOM 27 CB THR A 20 40.854 43.488 36.671 1.00 18.53 C ATOM 28 OG1 THR A 20 41.161 43.234 38.028 1.00 21.90 O ATOM 29 CG2 THR A 20 39.362 43.783 36.615 1.00 20.28 C ATOM 30 N GLU A 21 43.465 42.806 34.977 1.00 17.36 N ATOM 31 CA GLU A 21 44.865 42.555 34.859 1.00 16.71 C ATOM 32 C GLU A 21 45.574 42.977 36.145 1.00 17.00 C ATOM 33 O GLU A 21 45.219 44.002 36.718 1.00 16.14 O ATOM 34 CB GLU A 21 45.362 43.317 33.667 1.00 20.43 C ATOM 35 CG GLU A 21 46.829 43.020 33.446 1.00 24.72 C ATOM 36 CD GLU A 21 47.475 43.832 32.343 1.00 30.35 C ATOM 37 OE1 GLU A 21 46.815 44.064 31.332 1.00 32.22 O ATOM 38 OE2 GLU A 21 48.640 44.213 32.503 1.00 34.58 O ATOM 39 N ALA A 22 46.507 42.201 36.690 1.00 13.57 N ATOM 40 CA ALA A 22 47.254 42.613 37.877 1.00 16.53 C ATOM 41 C ALA A 22 48.413 43.574 37.541 1.00 19.25 C ATOM 42 O ALA A 22 48.936 43.546 36.410 1.00 19.34 O ATOM 43 CB ALA A 22 47.850 41.387 38.565 1.00 12.65 C ATOM 44 N GLN A 23 48.800 44.479 38.475 1.00 22.53 N ATOM 45 CA GLN A 23 50.009 45.296 38.310 1.00 26.37 C ATOM 46 C GLN A 23 51.263 44.409 38.378 1.00 27.67 C ATOM 47 O GLN A 23 51.187 43.347 38.997 1.00 23.66 O ATOM 48 CB GLN A 23 50.168 46.320 39.400 1.00 31.17 C ATOM 49 CG GLN A 23 49.159 47.429 39.421 1.00 42.19 C ATOM 50 CD GLN A 23 49.687 48.673 40.142 1.00 49.58 C ATOM 51 OE1 GLN A 23 50.904 48.913 40.285 1.00 52.36 O ATOM 52 NE2 GLN A 23 48.727 49.492 40.591 1.00 51.67 N ATOM 53 N ARG A 24 52.431 44.788 37.800 1.00 29.51 N ATOM 54 CA ARG A 24 53.641 43.953 37.789 1.00 30.30 C ATOM 55 C ARG A 24 54.183 43.386 39.081 1.00 31.38 C ATOM 56 O ARG A 24 54.587 42.235 39.151 1.00 34.00 O ATOM 57 CB ARG A 24 54.840 44.668 37.206 1.00 30.16 C ATOM 58 CG ARG A 24 54.679 44.883 35.770 1.00 28.35 C ATOM 59 CD ARG A 24 55.881 45.609 35.209 1.00 27.43 C ATOM 60 NE ARG A 24 55.515 45.740 33.820 1.00 28.29 N ATOM 61 CZ ARG A 24 55.724 44.756 32.944 1.00 28.28 C ATOM 62 NH1 ARG A 24 56.320 43.610 33.293 1.00 27.96 N ATOM 63 NH2 ARG A 24 55.172 44.852 31.736 1.00 28.73 N ATOM 64 N ASN A 25 54.279 44.201 40.117 1.00 32.39 N ATOM 65 CA ASN A 25 54.869 43.760 41.380 1.00 33.61 C ATOM 66 C ASN A 25 53.824 43.580 42.473 1.00 31.97 C ATOM 67 O ASN A 25 54.141 43.602 43.671 1.00 29.55 O ATOM 68 CB ASN A 25 55.929 44.795 41.809 1.00 37.80 C ATOM 69 CG ASN A 25 55.409 46.225 41.994 1.00 40.56 C ATOM 70 OD1 ASN A 25 54.300 46.613 41.600 1.00 42.11 O ATOM 71 ND2 ASN A 25 56.249 47.031 42.633 1.00 44.06 N ATOM 72 N SER A 26 52.568 43.425 42.030 1.00 28.95 N ATOM 73 CA SER A 26 51.480 43.244 42.956 1.00 27.48 C ATOM 74 C SER A 26 51.550 41.881 43.640 1.00 24.98 C ATOM 75 O SER A 26 51.345 41.838 44.862 1.00 24.86 O ATOM 76 CB SER A 26 50.145 43.400 42.220 1.00 29.77 C ATOM 77 OG SER A 26 49.576 44.692 42.384 1.00 32.18 O ATOM 78 N TRP A 27 51.894 40.773 42.943 1.00 19.00 N ATOM 79 CA TRP A 27 51.827 39.462 43.577 1.00 15.63 C ATOM 80 C TRP A 27 53.117 38.694 43.339 1.00 13.92 C ATOM 81 O TRP A 27 53.144 37.728 42.595 1.00 12.13 O ATOM 82 CB TRP A 27 50.596 38.703 43.019 1.00 11.96 C ATOM 83 CG TRP A 27 49.263 39.463 43.147 1.00 11.14 C ATOM 84 CD1 TRP A 27 48.655 40.009 42.035 1.00 11.57 C ATOM 85 CD2 TRP A 27 48.540 39.681 44.301 1.00 13.48 C ATOM 86 NE1 TRP A 27 47.556 40.562 42.482 1.00 10.27 N ATOM 87 CE2 TRP A 27 47.439 40.401 43.808 1.00 10.92 C ATOM 88 CE3 TRP A 27 48.623 39.397 45.681 1.00 13.18 C ATOM 89 CZ2 TRP A 27 46.423 40.836 44.680 1.00 10.34 C ATOM 90 CZ3 TRP A 27 47.605 39.840 46.538 1.00 11.90 C ATOM 91 CH2 TRP A 27 46.513 40.551 46.040 1.00 10.77 C ATOM 92 N PRO A 28 54.229 39.090 43.951 1.00 11.86 N ATOM 93 CA PRO A 28 55.548 38.663 43.566 1.00 12.64 C ATOM 94 C PRO A 28 55.962 37.263 44.017 1.00 11.81 C ATOM 95 O PRO A 28 57.054 36.803 43.660 1.00 11.52 O ATOM 96 CB PRO A 28 56.413 39.809 44.089 1.00 14.52 C ATOM 97 CG PRO A 28 55.730 40.196 45.376 1.00 12.82 C ATOM 98 CD PRO A 28 54.281 40.117 44.984 1.00 11.25 C ATOM 99 N SER A 29 55.096 36.568 44.781 1.00 9.76 N ATOM 100 CA SER A 29 55.334 35.159 45.098 1.00 9.96 C ATOM 101 C SER A 29 54.674 34.231 44.069 1.00 9.91 C ATOM 102 O SER A 29 54.900 33.017 44.093 1.00 9.94 O ATOM 103 CB SER A 29 54.789 34.832 46.503 1.00 8.62 C ATOM 104 OG SER A 29 53.364 34.849 46.566 1.00 12.43 O ATOM 105 N GLN A 30 53.845 34.765 43.154 1.00 8.00 N ATOM 106 CA GLN A 30 53.241 33.980 42.087 1.00 8.57 C ATOM 107 C GLN A 30 54.294 33.417 41.123 1.00 10.02 C ATOM 108 O GLN A 30 55.207 34.132 40.697 1.00 10.78 O ATOM 109 CB GLN A 30 52.264 34.846 41.275 1.00 10.17 C ATOM 110 CG GLN A 30 51.653 34.201 40.027 1.00 8.01 C ATOM 111 CD GLN A 30 50.507 33.288 40.306 1.00 9.07 C ATOM 112 OE1 GLN A 30 49.469 33.711 40.810 1.00 10.33 O ATOM 113 NE2 GLN A 30 50.621 32.014 39.953 1.00 10.31 N ATOM 114 N ILE A 31 54.210 32.116 40.793 1.00 8.92 N ATOM 115 CA ILE A 31 55.088 31.545 39.777 1.00 6.99 C ATOM 116 C ILE A 31 54.240 30.889 38.673 1.00 7.32 C ATOM 117 O ILE A 31 53.032 30.629 38.858 1.00 6.13 O ATOM 118 CB ILE A 31 56.136 30.486 40.429 1.00 9.28 C ATOM 119 CG1 ILE A 31 55.501 29.162 40.903 1.00 7.00 C ATOM 120 CG2 ILE A 31 56.814 31.169 41.627 1.00 8.47 C ATOM 121 CD1 ILE A 31 55.220 28.102 39.818 1.00 8.11 C ATOM 122 N SER A 32 54.850 30.664 37.482 1.00 8.48 N ATOM 123 CA SER A 32 54.240 29.916 36.392 1.00 9.14 C ATOM 124 C SER A 32 54.994 28.595 36.331 1.00 7.06 C ATOM 125 O SER A 32 56.212 28.571 36.246 1.00 8.01 O ATOM 126 CB SER A 32 54.410 30.660 35.057 1.00 9.53 C ATOM 127 OG SER A 32 54.099 29.861 33.919 1.00 10.59 O ATOM 128 N LEU A 33 54.275 27.494 36.373 1.00 9.59 N ATOM 129 CA LEU A 33 54.858 26.166 36.265 1.00 9.76 C ATOM 130 C LEU A 33 54.588 25.764 34.825 1.00 10.03 C ATOM 131 O LEU A 33 53.451 25.728 34.380 1.00 8.61 O ATOM 132 CB LEU A 33 54.176 25.127 37.197 1.00 10.56 C ATOM 133 CG LEU A 33 54.678 23.658 37.079 1.00 9.91 C ATOM 134 CD1 LEU A 33 56.085 23.543 37.617 1.00 7.64 C ATOM 135 CD2 LEU A 33 53.734 22.732 37.820 1.00 12.30 C ATOM 136 N GLN A 34 55.645 25.383 34.129 1.00 12.13 N ATOM 137 CA GLN A 34 55.609 25.150 32.694 1.00 13.18 C ATOM 138 C GLN A 34 56.151 23.795 32.353 1.00 11.91 C ATOM 139 O GLN A 34 57.055 23.357 33.054 1.00 13.44 O ATOM 140 CB GLN A 34 56.479 26.194 31.955 1.00 12.93 C ATOM 141 CG GLN A 34 55.982 27.572 32.291 1.00 12.27 C ATOM 142 CD GLN A 34 56.605 28.671 31.492 1.00 13.36 C ATOM 143 OE1 GLN A 34 57.616 28.521 30.808 1.00 13.40 O ATOM 144 NE2 GLN A 34 55.926 29.794 31.626 1.00 11.34 N ATOM 145 N TYR A 35 55.675 23.147 31.306 1.00 11.44 N ATOM 146 CA TYR A 35 56.313 21.907 30.895 1.00 14.14 C ATOM 147 C TYR A 35 56.852 22.024 29.466 1.00 14.38 C ATOM 148 O TYR A 35 56.391 22.859 28.695 1.00 13.75 O ATOM 149 CB TYR A 35 55.327 20.761 30.987 1.00 13.02 C ATOM 150 CG TYR A 35 54.128 20.842 30.062 1.00 19.19 C ATOM 151 CD1 TYR A 35 53.089 21.733 30.324 1.00 20.94 C ATOM 152 CD2 TYR A 35 54.087 20.023 28.922 1.00 22.45 C ATOM 153 CE1 TYR A 35 52.006 21.816 29.452 1.00 23.87 C ATOM 154 CE2 TYR A 35 52.999 20.103 28.049 1.00 22.05 C ATOM 155 CZ TYR A 35 51.964 20.998 28.321 1.00 24.06 C ATOM 156 OH TYR A 35 50.865 21.061 27.476 1.00 25.35 O ATOM 157 N ARG A 36 57.832 21.217 29.075 1.00 16.04 N ATOM 158 CA ARG A 36 58.391 21.298 27.740 1.00 19.73 C ATOM 159 C ARG A 36 57.462 20.582 26.795 1.00 22.34 C ATOM 160 O ARG A 36 56.908 19.520 27.036 1.00 22.37 O ATOM 161 CB ARG A 36 59.757 20.698 27.755 1.00 21.39 C ATOM 162 CG ARG A 36 60.578 21.142 26.575 1.00 24.73 C ATOM 163 CD ARG A 36 62.004 20.688 26.765 1.00 30.91 C ATOM 164 NE ARG A 36 62.103 19.297 27.236 1.00 38.05 N ATOM 165 CZ ARG A 36 61.826 18.166 26.523 1.00 39.47 C ATOM 166 NH1 ARG A 36 61.391 18.177 25.242 1.00 43.28 N ATOM 167 NH2 ARG A 36 62.026 16.974 27.092 1.00 37.49 N ATOM 168 N SER A 37 57.147 21.355 25.786 1.00 25.25 N ATOM 169 CA SER A 37 56.184 20.971 24.794 1.00 32.58 C ATOM 170 C SER A 37 56.928 21.157 23.477 1.00 37.49 C ATOM 171 O SER A 37 57.067 22.276 22.947 1.00 38.55 O ATOM 172 CB SER A 37 55.010 21.909 24.986 1.00 34.35 C ATOM 173 OG SER A 37 53.918 21.576 24.154 1.00 39.18 O ATOM 174 N GLY A 38 57.490 20.028 23.009 1.00 39.31 N ATOM 175 CA GLY A 38 58.282 19.988 21.792 1.00 40.50 C ATOM 176 C GLY A 38 59.594 20.740 21.968 1.00 42.41 C ATOM 177 O GLY A 38 60.516 20.339 22.693 1.00 42.97 O ATOM 178 N SER A 39 59.595 21.879 21.277 1.00 42.87 N ATOM 179 CA SER A 39 60.731 22.796 21.262 1.00 44.46 C ATOM 180 C SER A 39 60.594 23.962 22.239 1.00 43.55 C ATOM 181 O SER A 39 61.551 24.647 22.607 1.00 45.39 O ATOM 182 CB SER A 39 60.874 23.321 19.850 1.00 47.58 C ATOM 183 OG SER A 39 59.583 23.585 19.282 1.00 51.23 O ATOM 184 N SER A 40 59.345 24.174 22.644 1.00 41.15 N ATOM 185 CA SER A 40 58.971 25.266 23.518 1.00 38.12 C ATOM 186 C SER A 40 58.493 24.800 24.901 1.00 33.55 C ATOM 187 O SER A 40 58.634 23.624 25.245 1.00 32.42 O ATOM 188 CB SER A 40 57.905 26.050 22.768 1.00 40.19 C ATOM 189 OG SER A 40 56.915 25.159 22.253 1.00 45.65 O ATOM 190 N TRP A 41 57.967 25.752 25.687 1.00 27.38 N ATOM 191 CA TRP A 41 57.496 25.523 27.043 1.00 22.42 C ATOM 192 C TRP A 41 56.114 26.091 27.135 1.00 19.86 C ATOM 193 O TRP A 41 55.904 27.195 26.677 1.00 21.58 O ATOM 194 CB TRP A 41 58.348 26.242 28.014 1.00 22.39 C ATOM 195 CG TRP A 41 59.743 25.673 28.140 1.00 23.61 C ATOM 196 CD1 TRP A 41 60.790 26.138 27.371 1.00 22.48 C ATOM 197 CD2 TRP A 41 60.106 24.685 29.028 1.00 24.55 C ATOM 198 NE1 TRP A 41 61.828 25.437 27.779 1.00 25.26 N ATOM 199 CE2 TRP A 41 61.481 24.564 28.756 1.00 25.15 C ATOM 200 CE3 TRP A 41 59.498 23.894 30.019 1.00 24.05 C ATOM 201 CZ2 TRP A 41 62.247 23.644 29.482 1.00 24.19 C ATOM 202 CZ3 TRP A 41 60.279 22.981 30.736 1.00 21.92 C ATOM 203 CH2 TRP A 41 61.635 22.859 30.471 1.00 23.76 C ATOM 204 N ALA A 42 55.153 25.389 27.704 1.00 16.35 N ATOM 205 CA ALA A 42 53.776 25.840 27.824 1.00 15.04 C ATOM 206 C ALA A 42 53.388 25.995 29.315 1.00 14.44 C ATOM 207 O ALA A 42 53.767 25.155 30.145 1.00 13.83 O ATOM 208 CB ALA A 42 52.825 24.815 27.202 1.00 13.91 C ATOM 209 N HIS A 43 52.632 27.039 29.679 1.00 11.49 N ATOM 210 CA HIS A 43 52.146 27.185 31.048 1.00 12.37 C ATOM 211 C HIS A 43 51.090 26.108 31.347 1.00 10.74 C ATOM 212 O HIS A 43 50.169 25.878 30.566 1.00 11.37 O ATOM 213 CB HIS A 43 51.548 28.584 31.205 1.00 12.11 C ATOM 214 CG HIS A 43 50.789 28.830 32.491 1.00 11.84 C ATOM 215 ND1 HIS A 43 51.312 29.320 33.609 1.00 11.21 N ATOM 216 CD2 HIS A 43 49.454 28.549 32.701 1.00 12.94 C ATOM 217 CE1 HIS A 43 50.340 29.340 34.491 1.00 12.11 C ATOM 218 NE2 HIS A 43 49.227 28.879 33.948 1.00 10.55 N ATOM 219 N THR A 44 51.215 25.400 32.464 1.00 9.11 N ATOM 220 CA THR A 44 50.175 24.476 32.872 1.00 9.74 C ATOM 221 C THR A 44 49.510 24.819 34.228 1.00 7.13 C ATOM 222 O THR A 44 48.329 24.556 34.440 1.00 7.38 O ATOM 223 CB THR A 44 50.822 23.066 32.851 1.00 10.48 C ATOM 224 OG1 THR A 44 49.727 22.191 32.998 1.00 14.23 O ATOM 225 CG2 THR A 44 51.867 22.787 33.920 1.00 12.75 C ATOM 226 N CYS A 45 50.235 25.490 35.116 1.00 6.51 N ATOM 227 CA CYS A 45 49.773 25.700 36.485 1.00 6.29 C ATOM 228 C CYS A 45 50.423 26.923 37.125 1.00 5.70 C ATOM 229 O CYS A 45 51.443 27.401 36.620 1.00 4.80 O ATOM 230 CB CYS A 45 50.122 24.446 37.382 1.00 8.42 C ATOM 231 SG CYS A 45 48.919 23.107 37.188 1.00 10.15 S ATOM 232 N GLY A 46 49.794 27.434 38.193 1.00 6.07 N ATOM 233 CA GLY A 46 50.444 28.450 38.978 1.00 7.86 C ATOM 234 C GLY A 46 51.105 27.748 40.178 1.00 10.78 C ATOM 235 O GLY A 46 51.065 26.510 40.318 1.00 11.22 O ATOM 236 N GLY A 47 51.711 28.548 41.043 1.00 6.54 N ATOM 237 CA GLY A 47 52.285 28.063 42.289 1.00 6.80 C ATOM 238 C GLY A 47 52.661 29.272 43.136 1.00 7.93 C ATOM 239 O GLY A 47 52.493 30.423 42.702 1.00 9.16 O ATOM 240 N THR A 48 53.219 29.016 44.305 1.00 7.69 N ATOM 241 CA THR A 48 53.681 30.047 45.215 1.00 8.22 C ATOM 242 C THR A 48 55.117 29.798 45.606 1.00 9.03 C ATOM 243 O THR A 48 55.466 28.710 46.049 1.00 10.78 O ATOM 244 CB THR A 48 52.811 30.066 46.470 1.00 10.32 C ATOM 245 OG1 THR A 48 51.476 30.319 46.073 1.00 9.40 O ATOM 246 CG2 THR A 48 53.206 31.179 47.448 1.00 9.14 C ATOM 247 N LEU A 49 56.018 30.767 45.471 1.00 9.93 N ATOM 248 CA LEU A 49 57.386 30.650 45.934 1.00 10.04 C ATOM 249 C LEU A 49 57.389 30.698 47.474 1.00 10.76 C ATOM 250 O LEU A 49 56.894 31.661 48.042 1.00 9.70 O ATOM 251 CB LEU A 49 58.216 31.805 45.323 1.00 9.80 C ATOM 252 CG LEU A 49 59.709 31.758 45.631 1.00 12.10 C ATOM 253 CD1 LEU A 49 60.337 30.629 44.818 1.00 10.75 C ATOM 254 CD2 LEU A 49 60.348 33.111 45.320 1.00 12.86 C ATOM 255 N ILE A 50 57.843 29.663 48.187 1.00 10.28 N ATOM 256 CA ILE A 50 57.774 29.700 49.641 1.00 11.21 C ATOM 257 C ILE A 50 59.150 29.768 50.263 1.00 10.60 C ATOM 258 O ILE A 50 59.280 30.150 51.428 1.00 11.17 O ATOM 259 CB ILE A 50 57.008 28.470 50.241 1.00 10.84 C ATOM 260 CG1 ILE A 50 57.635 27.146 49.819 1.00 12.83 C ATOM 261 CG2 ILE A 50 55.545 28.694 49.943 1.00 8.94 C ATOM 262 CD1 ILE A 50 56.887 25.953 50.437 1.00 19.56 C ATOM 263 N ARG A 51 60.179 29.331 49.538 1.00 11.39 N ATOM 264 CA ARG A 51 61.572 29.479 49.921 1.00 14.84 C ATOM 265 C ARG A 51 62.311 29.843 48.642 1.00 14.15 C ATOM 266 O ARG A 51 61.754 29.654 47.574 1.00 15.83 O ATOM 267 CB ARG A 51 62.252 28.189 50.447 1.00 15.49 C ATOM 268 CG ARG A 51 61.749 27.603 51.730 1.00 20.57 C ATOM 269 CD ARG A 51 61.836 28.700 52.749 1.00 26.75 C ATOM 270 NE ARG A 51 61.483 28.198 54.067 1.00 36.70 N ATOM 271 CZ ARG A 51 60.229 28.103 54.521 1.00 40.23 C ATOM 272 NH1 ARG A 51 59.155 28.467 53.810 1.00 44.96 N ATOM 273 NH2 ARG A 51 60.048 27.549 55.715 1.00 45.37 N ATOM 274 N GLN A 52 63.559 30.313 48.677 1.00 14.77 N ATOM 275 CA GLN A 52 64.315 30.613 47.475 1.00 17.69 C ATOM 276 C GLN A 52 64.508 29.415 46.557 1.00 17.94 C ATOM 277 O GLN A 52 64.717 29.568 45.362 1.00 16.30 O ATOM 278 CB GLN A 52 65.684 31.156 47.836 1.00 22.60 C ATOM 279 CG GLN A 52 65.565 32.611 48.259 1.00 31.18 C ATOM 280 CD GLN A 52 66.887 33.323 48.580 1.00 38.73 C ATOM 281 OE1 GLN A 52 67.126 33.760 49.719 1.00 43.53 O ATOM 282 NE2 GLN A 52 67.782 33.472 47.599 1.00 39.25 N ATOM 283 N ASN A 53 64.408 28.203 47.090 1.00 15.33 N ATOM 284 CA ASN A 53 64.510 27.011 46.265 1.00 16.68 C ATOM 285 C ASN A 53 63.330 26.053 46.454 1.00 14.98 C ATOM 286 O ASN A 53 63.459 24.884 46.119 1.00 13.92 O ATOM 287 CB ASN A 53 65.830 26.296 46.572 1.00 17.35 C ATOM 288 CG ASN A 53 66.052 25.916 48.036 1.00 18.96 C ATOM 289 OD1 ASN A 53 66.934 25.116 48.326 1.00 24.48 O ATOM 290 ND2 ASN A 53 65.351 26.389 49.059 1.00 19.62 N ATOM 291 N TRP A 54 62.187 26.485 47.000 1.00 11.60 N ATOM 292 CA TRP A 54 61.013 25.626 47.134 1.00 11.68 C ATOM 293 C TRP A 54 59.781 26.386 46.654 1.00 10.70 C ATOM 294 O TRP A 54 59.648 27.594 46.913 1.00 11.59 O ATOM 295 CB TRP A 54 60.775 25.158 48.617 1.00 11.66 C ATOM 296 CG TRP A 54 61.683 24.023 49.131 1.00 14.01 C ATOM 297 CD1 TRP A 54 62.831 24.286 49.837 1.00 16.95 C ATOM 298 CD2 TRP A 54 61.487 22.654 48.953 1.00 16.32 C ATOM 299 NE1 TRP A 54 63.376 23.106 50.101 1.00 17.14 N ATOM 300 CE2 TRP A 54 62.619 22.108 49.598 1.00 16.55 C ATOM 301 CE3 TRP A 54 60.541 21.809 48.355 1.00 14.98 C ATOM 302 CZ2 TRP A 54 62.823 20.732 49.657 1.00 14.78 C ATOM 303 CZ3 TRP A 54 60.753 20.430 48.420 1.00 18.60 C ATOM 304 CH2 TRP A 54 61.880 19.901 49.063 1.00 16.24 C ATOM 305 N VAL A 55 58.943 25.673 45.877 1.00 9.81 N ATOM 306 CA VAL A 55 57.666 26.154 45.334 1.00 10.27 C ATOM 307 C VAL A 55 56.517 25.268 45.825 1.00 10.57 C ATOM 308 O VAL A 55 56.636 24.045 45.875 1.00 11.53 O ATOM 309 CB VAL A 55 57.697 26.160 43.748 1.00 11.35 C ATOM 310 CG1 VAL A 55 56.318 26.081 43.062 1.00 11.56 C ATOM 311 CG2 VAL A 55 58.243 27.503 43.327 1.00 10.32 C ATOM 312 N MET A 56 55.386 25.846 46.219 1.00 8.66 N ATOM 313 CA MET A 56 54.227 25.076 46.603 1.00 7.44 C ATOM 314 C MET A 56 53.219 25.081 45.458 1.00 10.16 C ATOM 315 O MET A 56 52.927 26.154 44.924 1.00 9.25 O ATOM 316 CB MET A 56 53.670 25.703 47.875 1.00 9.29 C ATOM 317 CG MET A 56 52.377 25.079 48.372 1.00 10.71 C ATOM 318 SD MET A 56 51.700 25.886 49.852 1.00 13.02 S ATOM 319 CE MET A 56 51.288 27.566 49.430 1.00 9.38 C ATOM 320 N THR A 57 52.628 23.952 45.055 1.00 8.68 N ATOM 321 CA THR A 57 51.655 23.921 43.955 1.00 6.91 C ATOM 322 C THR A 57 50.646 22.812 44.262 1.00 7.86 C ATOM 323 O THR A 57 50.679 22.256 45.374 1.00 7.97 O ATOM 324 CB THR A 57 52.436 23.702 42.597 1.00 5.11 C ATOM 325 OG1 THR A 57 51.496 23.956 41.567 1.00 5.03 O ATOM 326 CG2 THR A 57 52.996 22.303 42.379 1.00 5.45 C ATOM 327 N ALA A 58 49.721 22.481 43.359 1.00 8.02 N ATOM 328 CA ALA A 58 48.786 21.380 43.583 1.00 8.76 C ATOM 329 C ALA A 58 49.418 20.058 43.095 1.00 10.42 C ATOM 330 O ALA A 58 50.202 20.041 42.128 1.00 8.70 O ATOM 331 CB ALA A 58 47.485 21.629 42.817 1.00 7.33 C ATOM 332 N ALA A 59 49.157 18.938 43.792 1.00 9.16 N ATOM 333 CA ALA A 59 49.627 17.641 43.341 1.00 8.74 C ATOM 334 C ALA A 59 49.083 17.230 41.957 1.00 9.94 C ATOM 335 O ALA A 59 49.797 16.613 41.149 1.00 9.40 O ATOM 336 CB ALA A 59 49.212 16.591 44.328 1.00 9.97 C ATOM 337 N HIS A 60 47.853 17.606 41.585 1.00 9.12 N ATOM 338 CA HIS A 60 47.349 17.225 40.272 1.00 10.21 C ATOM 339 C HIS A 60 48.119 17.919 39.140 1.00 9.84 C ATOM 340 O HIS A 60 48.018 17.452 38.006 1.00 10.59 O ATOM 341 CB HIS A 60 45.823 17.534 40.124 1.00 9.52 C ATOM 342 CG HIS A 60 45.355 18.977 39.952 1.00 12.03 C ATOM 343 ND1 HIS A 60 44.765 19.764 40.861 1.00 13.28 N ATOM 344 CD2 HIS A 60 45.448 19.698 38.779 1.00 11.66 C ATOM 345 CE1 HIS A 60 44.505 20.915 40.306 1.00 12.79 C ATOM 346 NE2 HIS A 60 44.916 20.850 39.061 1.00 13.95 N ATOM 347 N CYS A 61 48.885 18.995 39.406 1.00 7.85 N ATOM 348 CA CYS A 61 49.713 19.651 38.388 1.00 9.63 C ATOM 349 C CYS A 61 50.914 18.793 37.965 1.00 11.75 C ATOM 350 O CYS A 61 51.460 18.975 36.873 1.00 11.07 O ATOM 351 CB CYS A 61 50.279 20.995 38.878 1.00 9.53 C ATOM 352 SG CYS A 61 48.981 22.231 39.006 1.00 9.56 S ATOM 353 N VAL A 62 51.372 17.885 38.838 1.00 11.98 N ATOM 354 CA VAL A 62 52.538 17.079 38.543 1.00 13.47 C ATOM 355 C VAL A 62 52.177 15.599 38.430 1.00 14.50 C ATOM 356 O VAL A 62 53.049 14.733 38.528 1.00 15.98 O ATOM 357 CB VAL A 62 53.637 17.283 39.615 1.00 14.34 C ATOM 358 CG1 VAL A 62 54.198 18.694 39.437 1.00 14.68 C ATOM 359 CG2 VAL A 62 53.117 17.128 41.041 1.00 15.60 C ATOM 360 N ASP A 63 50.899 15.278 38.187 1.00 14.73 N ATOM 361 CA ASP A 63 50.545 13.889 37.961 1.00 19.22 C ATOM 362 C ASP A 63 51.208 13.313 36.716 1.00 20.60 C ATOM 363 O ASP A 63 51.656 12.159 36.748 1.00 22.54 O ATOM 364 CB ASP A 63 49.029 13.724 37.841 1.00 18.62 C ATOM 365 CG ASP A 63 48.279 13.565 39.174 1.00 18.39 C ATOM 366 OD1 ASP A 63 48.843 13.089 40.164 1.00 18.09 O ATOM 367 OD2 ASP A 63 47.100 13.916 39.199 1.00 18.27 O ATOM 368 N ARG A 64 51.318 14.065 35.615 1.00 20.95 N ATOM 369 CA ARG A 64 52.016 13.547 34.448 1.00 21.05 C ATOM 370 C ARG A 64 53.499 13.775 34.581 1.00 20.06 C ATOM 371 O ARG A 64 53.971 14.823 35.033 1.00 22.98 O ATOM 372 CB ARG A 64 51.526 14.202 33.157 1.00 25.12 C ATOM 373 CG ARG A 64 50.231 13.593 32.567 1.00 34.24 C ATOM 374 CD ARG A 64 50.160 12.057 32.234 1.00 44.22 C ATOM 375 NE ARG A 64 51.129 11.521 31.257 1.00 53.66 N ATOM 376 CZ ARG A 64 50.832 11.172 29.978 1.00 57.48 C ATOM 377 NH1 ARG A 64 49.601 11.283 29.442 1.00 58.71 N ATOM 378 NH2 ARG A 64 51.800 10.675 29.203 1.00 57.72 N ATOM 379 N GLU A 65 54.238 12.753 34.165 1.00 17.07 N ATOM 380 CA GLU A 65 55.679 12.742 34.250 1.00 17.82 C ATOM 381 C GLU A 65 56.333 13.452 33.078 1.00 19.64 C ATOM 382 O GLU A 65 56.778 12.820 32.122 1.00 20.83 O ATOM 383 CB GLU A 65 56.143 11.299 34.335 1.00 18.50 C ATOM 384 CG GLU A 65 55.616 10.706 35.633 1.00 20.29 C ATOM 385 CD GLU A 65 56.362 9.473 36.085 1.00 17.04 C ATOM 386 OE1 GLU A 65 57.553 9.583 36.382 1.00 17.50 O ATOM 387 OE2 GLU A 65 55.729 8.427 36.140 1.00 19.42 O ATOM 388 N LEU A 66 56.420 14.785 33.220 1.00 15.92 N ATOM 389 CA LEU A 66 56.848 15.716 32.176 1.00 15.64 C ATOM 390 C LEU A 66 58.095 16.424 32.660 1.00 16.72 C ATOM 391 O LEU A 66 58.454 16.286 33.833 1.00 16.69 O ATOM 392 CB LEU A 66 55.757 16.768 31.946 1.00 17.74 C ATOM 393 CG LEU A 66 54.328 16.332 31.660 1.00 18.78 C ATOM 394 CD1 LEU A 66 53.378 17.487 31.846 1.00 21.80 C ATOM 395 CD2 LEU A 66 54.222 15.831 30.257 1.00 20.48 C ATOM 396 N THR A 67 58.774 17.160 31.774 1.00 13.72 N ATOM 397 CA THR A 67 59.883 18.010 32.146 1.00 15.03 C ATOM 398 C THR A 67 59.310 19.379 32.563 1.00 15.54 C ATOM 399 O THR A 67 58.695 20.086 31.764 1.00 16.15 O ATOM 400 CB THR A 67 60.871 18.249 30.983 1.00 16.91 C ATOM 401 OG1 THR A 67 61.456 17.006 30.642 1.00 19.43 O ATOM 402 CG2 THR A 67 61.986 19.202 31.361 1.00 16.06 C ATOM 403 N PHE A 68 59.563 19.798 33.809 1.00 14.23 N ATOM 404 CA PHE A 68 58.984 21.009 34.356 1.00 12.00 C ATOM 405 C PHE A 68 60.057 22.023 34.658 1.00 11.66 C ATOM 406 O PHE A 68 61.182 21.699 35.038 1.00 12.35 O ATOM 407 CB PHE A 68 58.227 20.727 35.660 1.00 10.94 C ATOM 408 CG PHE A 68 56.966 19.891 35.537 1.00 10.22 C ATOM 409 CD1 PHE A 68 55.824 20.423 34.932 1.00 10.34 C ATOM 410 CD2 PHE A 68 56.952 18.589 36.055 1.00 13.17 C ATOM 411 CE1 PHE A 68 54.669 19.641 34.855 1.00 12.14 C ATOM 412 CE2 PHE A 68 55.785 17.811 35.969 1.00 8.93 C ATOM 413 CZ PHE A 68 54.648 18.339 35.372 1.00 12.34 C ATOM 414 N ARG A 69 59.656 23.281 34.477 1.00 11.68 N ATOM 415 CA ARG A 69 60.474 24.403 34.916 1.00 11.50 C ATOM 416 C ARG A 69 59.529 25.414 35.583 1.00 8.81 C ATOM 417 O ARG A 69 58.320 25.415 35.394 1.00 10.24 O ATOM 418 CB ARG A 69 61.213 25.098 33.743 1.00 11.76 C ATOM 419 CG ARG A 69 60.364 25.979 32.846 1.00 14.86 C ATOM 420 CD ARG A 69 61.293 26.707 31.895 1.00 16.28 C ATOM 421 NE ARG A 69 60.420 27.583 31.120 1.00 19.92 N ATOM 422 CZ ARG A 69 60.875 28.394 30.165 1.00 21.52 C ATOM 423 NH1 ARG A 69 62.162 28.451 29.840 1.00 20.39 N ATOM 424 NH2 ARG A 69 60.016 29.192 29.543 1.00 20.72 N ATOM 425 N VAL A 70 60.129 26.315 36.347 1.00 11.12 N ATOM 426 CA VAL A 70 59.422 27.336 37.099 1.00 10.60 C ATOM 427 C VAL A 70 59.950 28.655 36.558 1.00 9.31 C ATOM 428 O VAL A 70 61.156 28.828 36.334 1.00 10.93 O ATOM 429 CB VAL A 70 59.753 27.097 38.634 1.00 9.18 C ATOM 430 CG1 VAL A 70 59.743 28.373 39.455 1.00 13.34 C ATOM 431 CG2 VAL A 70 58.721 26.109 39.166 1.00 6.24 C ATOM 432 N VAL A 71 58.992 29.549 36.368 1.00 8.89 N ATOM 433 CA VAL A 71 59.338 30.909 36.017 1.00 11.93 C ATOM 434 C VAL A 71 58.852 31.852 37.120 1.00 11.92 C ATOM 435 O VAL A 71 57.655 31.937 37.432 1.00 12.15 O ATOM 436 CB VAL A 71 58.702 31.317 34.647 1.00 14.02 C ATOM 437 CG1 VAL A 71 59.272 32.677 34.251 1.00 10.96 C ATOM 438 CG2 VAL A 71 59.011 30.289 33.563 1.00 13.43 C ATOM 439 N VAL A 72 59.804 32.566 37.744 1.00 13.18 N ATOM 440 CA VAL A 72 59.451 33.594 38.734 1.00 12.34 C ATOM 441 C VAL A 72 59.636 34.991 38.089 1.00 14.36 C ATOM 442 O VAL A 72 60.312 35.152 37.048 1.00 13.27 O ATOM 443 CB VAL A 72 60.327 33.453 40.043 1.00 11.92 C ATOM 444 CG1 VAL A 72 60.168 32.062 40.595 1.00 12.55 C ATOM 445 CG2 VAL A 72 61.794 33.651 39.807 1.00 11.27 C ATOM 446 N GLY A 73 58.974 36.008 38.646 1.00 11.87 N ATOM 447 CA GLY A 73 59.073 37.371 38.121 1.00 14.08 C ATOM 448 C GLY A 73 58.387 37.512 36.773 1.00 15.09 C ATOM 449 O GLY A 73 58.735 38.353 35.952 1.00 13.12 O ATOM 450 N GLU A 74 57.377 36.673 36.557 1.00 14.89 N ATOM 451 CA GLU A 74 56.680 36.658 35.300 1.00 15.18 C ATOM 452 C GLU A 74 55.441 37.519 35.345 1.00 15.13 C ATOM 453 O GLU A 74 54.729 37.580 36.343 1.00 15.30 O ATOM 454 CB GLU A 74 56.305 35.201 34.918 1.00 15.63 C ATOM 455 CG GLU A 74 55.658 34.857 33.578 1.00 14.24 C ATOM 456 CD GLU A 74 56.448 35.409 32.404 1.00 17.13 C ATOM 457 OE1 GLU A 74 56.479 36.597 32.299 1.00 16.38 O ATOM 458 OE2 GLU A 74 57.040 34.708 31.606 1.00 19.38 O ATOM 459 N HIS A 75 55.228 38.237 34.232 1.00 15.92 N ATOM 460 CA HIS A 75 53.987 38.963 34.068 1.00 14.16 C ATOM 461 C HIS A 75 53.300 38.688 32.718 1.00 15.24 C ATOM 462 O HIS A 75 52.114 38.343 32.754 1.00 13.71 O ATOM 463 CB HIS A 75 54.285 40.426 34.247 1.00 16.58 C ATOM 464 CG HIS A 75 53.004 41.234 34.238 1.00 18.47 C ATOM 465 ND1 HIS A 75 52.022 41.152 35.121 1.00 19.99 N ATOM 466 CD2 HIS A 75 52.667 42.159 33.285 1.00 19.29 C ATOM 467 CE1 HIS A 75 51.097 41.991 34.744 1.00 21.94 C ATOM 468 NE2 HIS A 75 51.491 42.588 33.645 1.00 23.35 N ATOM 469 N ASN A 76 53.936 38.875 31.533 1.00 12.62 N ATOM 470 CA ASN A 76 53.282 38.553 30.275 1.00 12.88 C ATOM 471 C ASN A 76 53.830 37.233 29.786 1.00 13.49 C ATOM 472 O ASN A 76 55.021 37.202 29.520 1.00 14.57 O ATOM 473 CB ASN A 76 53.557 39.636 29.227 1.00 14.38 C ATOM 474 CG ASN A 76 52.816 39.356 27.917 1.00 16.99 C ATOM 475 OD1 ASN A 76 52.985 38.314 27.303 1.00 18.07 O ATOM 476 ND2 ASN A 76 51.957 40.205 27.375 1.00 18.06 N ATOM 477 N LEU A 77 53.074 36.138 29.618 1.00 13.10 N ATOM 478 CA LEU A 77 53.654 34.856 29.191 1.00 16.26 C ATOM 479 C LEU A 77 54.349 34.840 27.835 1.00 18.78 C ATOM 480 O LEU A 77 55.335 34.135 27.607 1.00 16.87 O ATOM 481 CB LEU A 77 52.587 33.746 29.171 1.00 12.97 C ATOM 482 CG LEU A 77 52.036 33.309 30.510 1.00 12.19 C ATOM 483 CD1 LEU A 77 50.886 32.342 30.314 1.00 10.63 C ATOM 484 CD2 LEU A 77 53.160 32.685 31.334 1.00 11.40 C ATOM 485 N ASN A 78 53.889 35.718 26.964 1.00 22.18 N ATOM 486 CA ASN A 78 54.380 35.717 25.614 1.00 27.02 C ATOM 487 C ASN A 78 55.407 36.791 25.304 1.00 29.22 C ATOM 488 O ASN A 78 55.888 36.812 24.167 1.00 31.27 O ATOM 489 CB ASN A 78 53.136 35.808 24.724 1.00 30.95 C ATOM 490 CG ASN A 78 52.153 34.665 24.993 1.00 34.09 C ATOM 491 OD1 ASN A 78 51.008 34.856 25.420 1.00 36.04 O ATOM 492 ND2 ASN A 78 52.594 33.422 24.807 1.00 35.73 N ATOM 493 N GLN A 79 55.796 37.686 26.230 1.00 29.09 N ATOM 494 CA GLN A 79 56.730 38.787 25.929 1.00 27.70 C ATOM 495 C GLN A 79 57.879 38.885 26.904 1.00 26.60 C ATOM 496 O GLN A 79 57.615 38.583 28.052 1.00 20.79 O ATOM 497 CB GLN A 79 56.043 40.128 25.981 1.00 31.97 C ATOM 498 CG GLN A 79 55.124 40.432 24.818 1.00 40.38 C ATOM 499 CD GLN A 79 54.257 41.660 25.083 1.00 45.18 C ATOM 500 OE1 GLN A 79 54.605 42.525 25.898 1.00 49.79 O ATOM 501 NE2 GLN A 79 53.099 41.765 24.418 1.00 45.59 N ATOM 502 N ASN A 80 59.125 39.256 26.607 1.00 24.38 N ATOM 503 CA ASN A 80 60.093 39.436 27.672 1.00 26.13 C ATOM 504 C ASN A 80 59.733 40.691 28.492 1.00 24.82 C ATOM 505 O ASN A 80 59.459 41.770 27.975 1.00 24.22 O ATOM 506 CB ASN A 80 61.525 39.577 27.110 1.00 31.06 C ATOM 507 CG ASN A 80 62.609 39.916 28.160 1.00 36.12 C ATOM 508 OD1 ASN A 80 62.814 39.231 29.174 1.00 37.74 O ATOM 509 ND2 ASN A 80 63.332 41.026 27.967 1.00 40.37 N ATOM 510 N ASN A 81 59.733 40.517 29.813 1.00 20.88 N ATOM 511 CA ASN A 81 59.400 41.570 30.751 1.00 20.77 C ATOM 512 C ASN A 81 60.699 42.125 31.344 1.00 18.80 C ATOM 513 O ASN A 81 60.704 43.163 31.979 1.00 19.83 O ATOM 514 CB ASN A 81 58.474 40.983 31.844 1.00 19.80 C ATOM 515 CG ASN A 81 57.062 40.605 31.402 1.00 20.20 C ATOM 516 OD1 ASN A 81 56.685 39.438 31.377 1.00 20.33 O ATOM 517 ND2 ASN A 81 56.187 41.530 31.047 1.00 19.34 N ATOM 518 N GLY A 82 61.862 41.502 31.165 1.00 18.50 N ATOM 519 CA GLY A 82 63.105 41.965 31.737 1.00 17.86 C ATOM 520 C GLY A 82 63.188 41.609 33.213 1.00 19.09 C ATOM 521 O GLY A 82 64.088 42.084 33.890 1.00 20.72 O ATOM 522 N THR A 83 62.286 40.781 33.764 1.00 19.40 N ATOM 523 CA THR A 83 62.275 40.417 35.187 1.00 19.01 C ATOM 524 C THR A 83 62.283 38.924 35.505 1.00 18.98 C ATOM 525 O THR A 83 62.373 38.506 36.664 1.00 19.69 O ATOM 526 CB THR A 83 61.045 41.054 35.821 1.00 16.10 C ATOM 527 OG1 THR A 83 59.922 40.569 35.104 1.00 14.11 O ATOM 528 CG2 THR A 83 61.070 42.588 35.751 1.00 16.91 C ATOM 529 N GLU A 84 62.245 38.082 34.466 1.00 17.88 N ATOM 530 CA GLU A 84 62.045 36.648 34.637 1.00 14.65 C ATOM 531 C GLU A 84 63.292 35.900 35.014 1.00 13.47 C ATOM 532 O GLU A 84 64.387 36.258 34.588 1.00 13.80 O ATOM 533 CB GLU A 84 61.499 35.997 33.363 1.00 12.10 C ATOM 534 CG GLU A 84 60.237 36.570 32.736 1.00 14.64 C ATOM 535 CD GLU A 84 60.445 37.752 31.775 1.00 16.56 C ATOM 536 OE1 GLU A 84 61.402 38.528 31.859 1.00 15.47 O ATOM 537 OE2 GLU A 84 59.621 37.917 30.905 1.00 16.61 O ATOM 538 N GLN A 85 63.147 34.915 35.913 1.00 12.34 N ATOM 539 CA GLN A 85 64.221 33.966 36.198 1.00 12.18 C ATOM 540 C GLN A 85 63.605 32.598 35.922 1.00 13.70 C ATOM 541 O GLN A 85 62.467 32.345 36.316 1.00 13.20 O ATOM 542 CB GLN A 85 64.674 34.008 37.637 1.00 14.90 C ATOM 543 CG GLN A 85 65.380 35.285 38.054 1.00 17.26 C ATOM 544 CD GLN A 85 65.518 35.351 39.570 1.00 20.93 C ATOM 545 OE1 GLN A 85 66.202 34.524 40.171 1.00 22.56 O ATOM 546 NE2 GLN A 85 64.883 36.312 40.242 1.00 20.29 N ATOM 547 N TYR A 86 64.354 31.744 35.217 1.00 14.34 N ATOM 548 CA TYR A 86 63.891 30.436 34.741 1.00 16.35 C ATOM 549 C TYR A 86 64.717 29.364 35.424 1.00 16.89 C ATOM 550 O TYR A 86 65.946 29.361 35.275 1.00 18.78 O ATOM 551 CB TYR A 86 64.096 30.294 33.259 1.00 16.32 C ATOM 552 CG TYR A 86 63.416 31.357 32.429 1.00 19.72 C ATOM 553 CD1 TYR A 86 62.099 31.182 32.060 1.00 18.48 C ATOM 554 CD2 TYR A 86 64.098 32.516 32.052 1.00 20.37 C ATOM 555 CE1 TYR A 86 61.448 32.162 31.315 1.00 20.31 C ATOM 556 CE2 TYR A 86 63.451 33.499 31.301 1.00 19.67 C ATOM 557 CZ TYR A 86 62.128 33.308 30.944 1.00 20.73 C ATOM 558 OH TYR A 86 61.442 34.288 30.249 1.00 27.36 O ATOM 559 N VAL A 87 64.095 28.450 36.183 1.00 15.67 N ATOM 560 CA VAL A 87 64.884 27.451 36.906 1.00 15.58 C ATOM 561 C VAL A 87 64.223 26.079 36.822 1.00 14.33 C ATOM 562 O VAL A 87 63.008 25.999 36.714 1.00 12.05 O ATOM 563 CB VAL A 87 65.089 27.968 38.386 1.00 15.09 C ATOM 564 CG1 VAL A 87 63.770 28.218 39.073 1.00 17.81 C ATOM 565 CG2 VAL A 87 65.878 26.938 39.180 1.00 14.82 C ATOM 566 N GLY A 88 65.029 25.001 36.778 1.00 15.60 N ATOM 567 CA GLY A 88 64.545 23.626 36.675 1.00 15.91 C ATOM 568 C GLY A 88 64.036 23.095 38.002 1.00 15.26 C ATOM 569 O GLY A 88 64.387 23.586 39.078 1.00 13.64 O ATOM 570 N VAL A 89 63.131 22.124 37.918 1.00 14.94 N ATOM 571 CA VAL A 89 62.621 21.446 39.101 1.00 16.34 C ATOM 572 C VAL A 89 63.521 20.237 39.296 1.00 19.56 C ATOM 573 O VAL A 89 63.700 19.406 38.406 1.00 21.89 O ATOM 574 CB VAL A 89 61.175 21.005 38.884 1.00 11.51 C ATOM 575 CG1 VAL A 89 60.647 20.192 40.048 1.00 13.75 C ATOM 576 CG2 VAL A 89 60.328 22.252 38.793 1.00 9.94 C ATOM 577 N GLN A 90 64.189 20.204 40.429 1.00 20.26 N ATOM 578 CA GLN A 90 65.034 19.096 40.765 1.00 22.28 C ATOM 579 C GLN A 90 64.294 17.969 41.535 1.00 24.14 C ATOM 580 O GLN A 90 64.680 16.807 41.382 1.00 25.96 O ATOM 581 CB GLN A 90 66.142 19.683 41.550 1.00 23.58 C ATOM 582 CG GLN A 90 67.113 18.705 42.144 1.00 30.44 C ATOM 583 CD GLN A 90 68.064 19.491 43.008 1.00 33.80 C ATOM 584 OE1 GLN A 90 67.753 19.879 44.134 1.00 36.82 O ATOM 585 NE2 GLN A 90 69.237 19.779 42.454 1.00 36.91 N ATOM 586 N LYS A 91 63.262 18.187 42.371 1.00 20.69 N ATOM 587 CA LYS A 91 62.648 17.102 43.128 1.00 18.40 C ATOM 588 C LYS A 91 61.197 17.458 43.376 1.00 17.81 C ATOM 589 O LYS A 91 60.920 18.610 43.681 1.00 17.02 O ATOM 590 CB LYS A 91 63.404 16.948 44.427 1.00 20.25 C ATOM 591 CG LYS A 91 62.840 15.904 45.357 1.00 26.29 C ATOM 592 CD LYS A 91 63.591 15.895 46.677 1.00 29.77 C ATOM 593 CE LYS A 91 63.339 14.527 47.326 1.00 32.95 C ATOM 594 NZ LYS A 91 64.038 13.442 46.641 1.00 36.98 N ATOM 595 N ILE A 92 60.266 16.514 43.214 1.00 14.26 N ATOM 596 CA ILE A 92 58.838 16.726 43.403 1.00 16.37 C ATOM 597 C ILE A 92 58.401 15.863 44.592 1.00 16.51 C ATOM 598 O ILE A 92 58.598 14.641 44.563 1.00 17.95 O ATOM 599 CB ILE A 92 58.097 16.311 42.112 1.00 15.64 C ATOM 600 CG1 ILE A 92 58.510 17.276 40.968 1.00 16.74 C ATOM 601 CG2 ILE A 92 56.580 16.304 42.348 1.00 14.98 C ATOM 602 CD1 ILE A 92 57.997 16.971 39.532 1.00 20.78 C ATOM 603 N VAL A 93 57.797 16.491 45.617 1.00 13.52 N ATOM 604 CA VAL A 93 57.362 15.804 46.824 1.00 12.48 C ATOM 605 C VAL A 93 55.886 16.028 46.841 1.00 12.62 C ATOM 606 O VAL A 93 55.421 17.117 47.128 1.00 14.90 O ATOM 607 CB VAL A 93 58.034 16.409 48.107 1.00 8.83 C ATOM 608 CG1 VAL A 93 57.629 15.621 49.341 1.00 9.55 C ATOM 609 CG2 VAL A 93 59.555 16.361 47.987 1.00 10.27 C ATOM 610 N VAL A 94 55.103 15.022 46.489 1.00 12.74 N ATOM 611 CA VAL A 94 53.657 15.132 46.518 1.00 13.20 C ATOM 612 C VAL A 94 53.193 14.687 47.910 1.00 14.69 C ATOM 613 O VAL A 94 53.896 13.885 48.542 1.00 12.47 O ATOM 614 CB VAL A 94 53.061 14.222 45.373 1.00 16.43 C ATOM 615 CG1 VAL A 94 51.556 14.174 45.405 1.00 15.01 C ATOM 616 CG2 VAL A 94 53.417 14.836 44.013 1.00 15.46 C ATOM 617 N HIS A 95 52.081 15.208 48.467 1.00 12.87 N ATOM 618 CA HIS A 95 51.562 14.729 49.747 1.00 14.54 C ATOM 619 C HIS A 95 51.364 13.200 49.686 1.00 15.11 C ATOM 620 O HIS A 95 50.773 12.732 48.701 1.00 13.56 O ATOM 621 CB HIS A 95 50.230 15.412 50.049 1.00 13.95 C ATOM 622 CG HIS A 95 49.864 15.175 51.497 1.00 16.11 C ATOM 623 ND1 HIS A 95 49.373 14.062 52.040 1.00 14.83 N ATOM 624 CD2 HIS A 95 50.077 16.080 52.510 1.00 16.56 C ATOM 625 CE1 HIS A 95 49.288 14.251 53.348 1.00 16.92 C ATOM 626 NE2 HIS A 95 49.711 15.458 53.612 1.00 17.35 N ATOM 627 N PRO A 96 51.849 12.377 50.656 1.00 15.94 N ATOM 628 CA PRO A 96 51.682 10.906 50.715 1.00 16.06 C ATOM 629 C PRO A 96 50.288 10.339 50.474 1.00 15.65 C ATOM 630 O PRO A 96 50.147 9.247 49.935 1.00 17.84 O ATOM 631 CB PRO A 96 52.206 10.520 52.097 1.00 16.71 C ATOM 632 CG PRO A 96 53.231 11.588 52.459 1.00 16.31 C ATOM 633 CD PRO A 96 52.671 12.844 51.797 1.00 16.37 C ATOM 634 N TYR A 97 49.246 11.060 50.904 1.00 12.74 N ATOM 635 CA TYR A 97 47.875 10.656 50.747 1.00 12.92 C ATOM 636 C TYR A 97 47.122 11.114 49.509 1.00 14.08 C ATOM 637 O TYR A 97 45.918 10.844 49.445 1.00 12.62 O ATOM 638 CB TYR A 97 47.086 11.125 51.937 1.00 19.96 C ATOM 639 CG TYR A 97 47.419 10.449 53.244 1.00 24.42 C ATOM 640 CD1 TYR A 97 47.972 9.169 53.262 1.00 29.05 C ATOM 641 CD2 TYR A 97 47.116 11.098 54.441 1.00 28.57 C ATOM 642 CE1 TYR A 97 48.214 8.515 54.478 1.00 30.89 C ATOM 643 CE2 TYR A 97 47.357 10.458 55.662 1.00 31.11 C ATOM 644 CZ TYR A 97 47.899 9.168 55.673 1.00 31.62 C ATOM 645 OH TYR A 97 48.088 8.514 56.878 1.00 33.38 O ATOM 646 N TRP A 98 47.783 11.833 48.568 1.00 13.04 N ATOM 647 CA TRP A 98 47.155 12.347 47.348 1.00 12.00 C ATOM 648 C TRP A 98 46.665 11.184 46.522 1.00 12.60 C ATOM 649 O TRP A 98 47.422 10.250 46.298 1.00 13.84 O ATOM 650 CB TRP A 98 48.157 13.169 46.445 1.00 10.27 C ATOM 651 CG TRP A 98 47.633 13.510 45.018 1.00 9.10 C ATOM 652 CD1 TRP A 98 48.301 13.079 43.898 1.00 9.83 C ATOM 653 CD2 TRP A 98 46.490 14.212 44.682 1.00 8.83 C ATOM 654 NE1 TRP A 98 47.583 13.495 42.864 1.00 7.05 N ATOM 655 CE2 TRP A 98 46.512 14.161 43.285 1.00 8.87 C ATOM 656 CE3 TRP A 98 45.436 14.874 45.319 1.00 9.49 C ATOM 657 CZ2 TRP A 98 45.512 14.741 42.521 1.00 10.25 C ATOM 658 CZ3 TRP A 98 44.425 15.458 44.549 1.00 12.16 C ATOM 659 CH2 TRP A 98 44.462 15.398 43.155 1.00 11.86 C ATOM 660 N ASN A 99 45.457 11.209 46.028 1.00 14.58 N ATOM 661 CA ASN A 99 45.017 10.129 45.157 1.00 16.39 C ATOM 662 C ASN A 99 44.429 10.790 43.941 1.00 14.46 C ATOM 663 O ASN A 99 43.391 11.435 44.072 1.00 14.41 O ATOM 664 CB ASN A 99 43.966 9.302 45.883 1.00 18.94 C ATOM 665 CG ASN A 99 43.326 8.185 45.093 1.00 20.89 C ATOM 666 OD1 ASN A 99 43.688 7.903 43.951 1.00 24.09 O ATOM 667 ND2 ASN A 99 42.336 7.557 45.732 1.00 24.14 N ATOM 668 N THR A 100 45.076 10.624 42.786 1.00 15.80 N ATOM 669 CA THR A 100 44.608 11.181 41.502 1.00 18.40 C ATOM 670 C THR A 100 43.146 10.900 41.123 1.00 19.39 C ATOM 671 O THR A 100 42.462 11.748 40.532 1.00 20.77 O ATOM 672 CB THR A 100 45.432 10.654 40.351 1.00 19.59 C ATOM 673 OG1 THR A 100 46.784 10.591 40.746 1.00 26.80 O ATOM 674 CG2 THR A 100 45.218 11.522 39.143 1.00 22.76 C ATOM 675 N ASP A 101 42.670 9.693 41.471 1.00 20.22 N ATOM 676 CA ASP A 101 41.285 9.239 41.235 1.00 22.75 C ATOM 677 C ASP A 101 40.234 9.804 42.210 1.00 25.03 C ATOM 678 O ASP A 101 39.035 9.498 42.075 1.00 23.02 O ATOM 679 CB ASP A 101 41.132 7.708 41.349 1.00 24.56 C ATOM 680 CG ASP A 101 42.027 6.808 40.511 1.00 28.77 C ATOM 681 OD1 ASP A 101 42.446 7.214 39.420 1.00 29.77 O ATOM 682 OD2 ASP A 101 42.279 5.687 40.975 1.00 31.95 O ATOM 683 N ASP A 102 40.685 10.572 43.235 1.00 23.36 N ATOM 684 CA ASP A 102 39.788 11.180 44.201 1.00 22.91 C ATOM 685 C ASP A 102 40.272 12.575 44.630 1.00 22.59 C ATOM 686 O ASP A 102 40.711 12.725 45.774 1.00 21.87 O ATOM 687 CB ASP A 102 39.715 10.218 45.352 1.00 22.88 C ATOM 688 CG ASP A 102 38.567 10.408 46.325 1.00 26.98 C ATOM 689 OD1 ASP A 102 37.798 11.372 46.219 1.00 22.46 O ATOM 690 OD2 ASP A 102 38.468 9.544 47.203 1.00 28.88 O ATOM 691 N VAL A 103 40.207 13.631 43.770 1.00 20.22 N ATOM 692 CA VAL A 103 40.590 14.990 44.190 1.00 18.18 C ATOM 693 C VAL A 103 39.676 15.478 45.338 1.00 15.07 C ATOM 694 O VAL A 103 40.099 16.273 46.166 1.00 14.46 O ATOM 695 CB VAL A 103 40.533 15.972 42.915 1.00 19.44 C ATOM 696 CG1 VAL A 103 39.125 16.374 42.552 1.00 19.05 C ATOM 697 CG2 VAL A 103 41.252 17.269 43.206 1.00 17.32 C ATOM 698 N ALA A 104 38.442 14.967 45.449 1.00 12.49 N ATOM 699 CA ALA A 104 37.510 15.367 46.482 1.00 13.00 C ATOM 700 C ALA A 104 37.913 14.831 47.846 1.00 11.56 C ATOM 701 O ALA A 104 37.409 15.291 48.867 1.00 11.63 O ATOM 702 CB ALA A 104 36.125 14.865 46.138 1.00 13.61 C ATOM 703 N ALA A 105 38.850 13.880 47.903 1.00 12.38 N ATOM 704 CA ALA A 105 39.424 13.466 49.171 1.00 12.37 C ATOM 705 C ALA A 105 40.428 14.478 49.778 1.00 12.90 C ATOM 706 O ALA A 105 40.738 14.402 50.975 1.00 13.39 O ATOM 707 CB ALA A 105 40.153 12.138 48.997 1.00 12.90 C ATOM 708 N GLY A 106 40.932 15.450 49.004 1.00 11.80 N ATOM 709 CA GLY A 106 41.878 16.431 49.511 1.00 11.28 C ATOM 710 C GLY A 106 43.291 16.009 49.180 1.00 10.14 C ATOM 711 O GLY A 106 43.517 15.221 48.264 1.00 10.55 O ATOM 712 N TYR A 107 44.221 16.539 49.991 1.00 6.45 N ATOM 713 CA TYR A 107 45.660 16.363 49.895 1.00 7.59 C ATOM 714 C TYR A 107 46.191 16.831 48.550 1.00 5.93 C ATOM 715 O TYR A 107 47.220 16.349 48.084 1.00 8.21 O ATOM 716 CB TYR A 107 46.098 14.873 50.119 1.00 10.07 C ATOM 717 CG TYR A 107 45.495 14.301 51.410 1.00 14.76 C ATOM 718 CD1 TYR A 107 45.975 14.689 52.667 1.00 14.99 C ATOM 719 CD2 TYR A 107 44.403 13.430 51.318 1.00 16.34 C ATOM 720 CE1 TYR A 107 45.347 14.211 53.819 1.00 19.58 C ATOM 721 CE2 TYR A 107 43.772 12.941 52.449 1.00 16.99 C ATOM 722 CZ TYR A 107 44.250 13.342 53.691 1.00 21.33 C ATOM 723 OH TYR A 107 43.601 12.881 54.828 1.00 28.40 O ATOM 724 N ASP A 108 45.542 17.824 47.956 1.00 6.59 N ATOM 725 CA ASP A 108 46.017 18.293 46.666 1.00 6.83 C ATOM 726 C ASP A 108 47.061 19.380 46.853 1.00 7.13 C ATOM 727 O ASP A 108 46.795 20.575 46.695 1.00 7.22 O ATOM 728 CB ASP A 108 44.835 18.832 45.808 1.00 5.74 C ATOM 729 CG ASP A 108 45.130 18.984 44.297 1.00 7.46 C ATOM 730 OD1 ASP A 108 46.207 18.606 43.862 1.00 6.32 O ATOM 731 OD2 ASP A 108 44.261 19.453 43.571 1.00 7.77 O ATOM 732 N ILE A 109 48.278 18.894 47.151 1.00 6.43 N ATOM 733 CA ILE A 109 49.434 19.753 47.427 1.00 7.64 C ATOM 734 C ILE A 109 50.714 18.997 47.168 1.00 7.56 C ATOM 735 O ILE A 109 50.848 17.790 47.384 1.00 9.28 O ATOM 736 CB ILE A 109 49.313 20.299 48.927 1.00 8.14 C ATOM 737 CG1 ILE A 109 50.424 21.328 49.224 1.00 8.97 C ATOM 738 CG2 ILE A 109 49.366 19.129 49.951 1.00 6.47 C ATOM 739 CD1 ILE A 109 50.035 22.216 50.449 1.00 10.00 C ATOM 740 N ALA A 110 51.673 19.768 46.661 1.00 7.57 N ATOM 741 CA ALA A 110 52.975 19.254 46.297 1.00 8.22 C ATOM 742 C ALA A 110 54.005 20.354 46.456 1.00 9.78 C ATOM 743 O ALA A 110 53.710 21.540 46.305 1.00 10.61 O ATOM 744 CB ALA A 110 52.957 18.783 44.842 1.00 7.05 C ATOM 745 N LEU A 111 55.214 19.961 46.827 1.00 8.38 N ATOM 746 CA LEU A 111 56.315 20.876 46.979 1.00 11.26 C ATOM 747 C LEU A 111 57.401 20.545 45.961 1.00 11.28 C ATOM 748 O LEU A 111 57.808 19.398 45.844 1.00 11.78 O ATOM 749 CB LEU A 111 56.900 20.778 48.401 1.00 11.52 C ATOM 750 CG LEU A 111 55.944 21.119 49.543 1.00 14.90 C ATOM 751 CD1 LEU A 111 56.650 20.874 50.874 1.00 16.48 C ATOM 752 CD2 LEU A 111 55.506 22.572 49.439 1.00 13.34 C ATOM 753 N LEU A 112 57.916 21.532 45.234 1.00 12.10 N ATOM 754 CA LEU A 112 58.928 21.349 44.211 1.00 11.77 C ATOM 755 C LEU A 112 60.230 21.991 44.671 1.00 13.64 C ATOM 756 O LEU A 112 60.290 23.170 45.037 1.00 10.84 O ATOM 757 CB LEU A 112 58.482 22.015 42.905 1.00 12.17 C ATOM 758 CG LEU A 112 57.063 21.837 42.415 1.00 15.40 C ATOM 759 CD1 LEU A 112 56.876 22.538 41.085 1.00 15.49 C ATOM 760 CD2 LEU A 112 56.775 20.368 42.294 1.00 15.15 C ATOM 761 N ARG A 113 61.283 21.186 44.757 1.00 13.46 N ATOM 762 CA ARG A 113 62.589 21.715 45.050 1.00 15.28 C ATOM 763 C ARG A 113 63.244 22.124 43.733 1.00 16.51 C ATOM 764 O ARG A 113 63.374 21.346 42.790 1.00 15.93 O ATOM 765 CB ARG A 113 63.388 20.649 45.748 1.00 19.45 C ATOM 766 CG ARG A 113 64.692 21.189 46.234 1.00 24.78 C ATOM 767 CD ARG A 113 65.510 19.963 46.464 1.00 35.00 C ATOM 768 NE ARG A 113 66.833 20.308 46.929 1.00 44.46 N ATOM 769 CZ ARG A 113 67.054 20.648 48.211 1.00 50.93 C ATOM 770 NH1 ARG A 113 66.056 20.699 49.111 1.00 53.94 N ATOM 771 NH2 ARG A 113 68.294 20.957 48.614 1.00 52.42 N ATOM 772 N LEU A 114 63.656 23.382 43.675 1.00 14.59 N ATOM 773 CA LEU A 114 64.286 23.948 42.517 1.00 12.96 C ATOM 774 C LEU A 114 65.750 23.621 42.431 1.00 14.45 C ATOM 775 O LEU A 114 66.429 23.426 43.427 1.00 15.35 O ATOM 776 CB LEU A 114 64.085 25.448 42.528 1.00 14.52 C ATOM 777 CG LEU A 114 62.643 25.929 42.734 1.00 13.04 C ATOM 778 CD1 LEU A 114 62.618 27.433 42.664 1.00 13.89 C ATOM 779 CD2 LEU A 114 61.727 25.354 41.681 1.00 15.27 C ATOM 780 N ALA A 115 66.225 23.591 41.180 1.00 15.90 N ATOM 781 CA ALA A 115 67.574 23.190 40.869 1.00 16.86 C ATOM 782 C ALA A 115 68.522 24.228 41.395 1.00 19.93 C ATOM 783 O ALA A 115 69.664 23.887 41.715 1.00 22.92 O ATOM 784 CB ALA A 115 67.763 23.068 39.383 1.00 14.10 C ATOM 785 N GLN A 116 68.097 25.490 41.479 1.00 21.12 N ATOM 786 CA GLN A 116 68.882 26.472 42.201 1.00 24.08 C ATOM 787 C GLN A 116 68.024 27.514 42.898 1.00 20.84 C ATOM 788 O GLN A 116 66.823 27.610 42.679 1.00 18.27 O ATOM 789 CB GLN A 116 69.904 27.171 41.267 1.00 30.47 C ATOM 790 CG GLN A 116 69.588 28.237 40.206 1.00 40.70 C ATOM 791 CD GLN A 116 70.645 29.381 40.178 1.00 48.56 C ATOM 792 OE1 GLN A 116 71.846 29.204 40.474 1.00 51.81 O ATOM 793 NE2 GLN A 116 70.236 30.621 39.855 1.00 50.77 N ATOM 794 N SER A 117 68.648 28.236 43.834 1.00 20.21 N ATOM 795 CA SER A 117 67.993 29.326 44.525 1.00 22.03 C ATOM 796 C SER A 117 67.726 30.546 43.645 1.00 20.51 C ATOM 797 O SER A 117 68.607 30.978 42.906 1.00 21.61 O ATOM 798 CB SER A 117 68.848 29.713 45.693 1.00 23.40 C ATOM 799 OG SER A 117 68.736 28.667 46.645 1.00 29.17 O ATOM 800 N VAL A 118 66.505 31.076 43.634 1.00 18.92 N ATOM 801 CA VAL A 118 66.219 32.272 42.862 1.00 17.04 C ATOM 802 C VAL A 118 66.682 33.466 43.689 1.00 18.16 C ATOM 803 O VAL A 118 66.958 33.359 44.893 1.00 18.57 O ATOM 804 CB VAL A 118 64.691 32.408 42.520 1.00 15.99 C ATOM 805 CG1 VAL A 118 64.306 31.212 41.662 1.00 13.34 C ATOM 806 CG2 VAL A 118 63.798 32.454 43.740 1.00 14.89 C ATOM 807 N THR A 119 66.874 34.578 42.987 1.00 17.98 N ATOM 808 CA THR A 119 67.293 35.837 43.544 1.00 18.88 C ATOM 809 C THR A 119 66.071 36.651 43.921 1.00 18.24 C ATOM 810 O THR A 119 65.197 36.845 43.074 1.00 19.28 O ATOM 811 CB THR A 119 68.136 36.574 42.489 1.00 22.39 C ATOM 812 OG1 THR A 119 69.324 35.787 42.316 1.00 24.41 O ATOM 813 CG2 THR A 119 68.409 38.046 42.866 1.00 23.47 C ATOM 814 N LEU A 120 65.997 37.164 45.156 1.00 17.66 N ATOM 815 CA LEU A 120 64.844 37.945 45.535 1.00 17.16 C ATOM 816 C LEU A 120 65.043 39.410 45.223 1.00 17.89 C ATOM 817 O LEU A 120 66.140 39.954 45.375 1.00 21.02 O ATOM 818 CB LEU A 120 64.553 37.758 47.023 1.00 17.06 C ATOM 819 CG LEU A 120 64.308 36.343 47.568 1.00 19.10 C ATOM 820 CD1 LEU A 120 63.883 36.470 49.023 1.00 18.54 C ATOM 821 CD2 LEU A 120 63.208 35.620 46.823 1.00 18.38 C ATOM 822 N ASN A 121 63.967 40.037 44.751 1.00 17.23 N ATOM 823 CA ASN A 121 63.949 41.455 44.410 1.00 18.56 C ATOM 824 C ASN A 121 62.526 41.982 44.418 1.00 18.33 C ATOM 825 O ASN A 121 61.669 41.268 44.947 1.00 19.10 O ATOM 826 CB ASN A 121 64.608 41.669 43.030 1.00 18.33 C ATOM 827 CG ASN A 121 64.039 40.875 41.875 1.00 18.25 C ATOM 828 OD1 ASN A 121 62.827 40.853 41.666 1.00 19.36 O ATOM 829 ND2 ASN A 121 64.922 40.227 41.111 1.00 18.49 N ATOM 830 N SER A 122 62.109 43.135 43.864 1.00 20.06 N ATOM 831 CA SER A 122 60.701 43.535 44.000 1.00 21.56 C ATOM 832 C SER A 122 59.689 42.720 43.200 1.00 21.71 C ATOM 833 O SER A 122 58.476 42.816 43.410 1.00 23.08 O ATOM 834 CB SER A 122 60.540 44.987 43.627 1.00 25.51 C ATOM 835 OG SER A 122 61.304 45.281 42.466 1.00 35.65 O ATOM 836 N TYR A 123 60.216 41.903 42.277 1.00 19.93 N ATOM 837 CA TYR A 123 59.418 41.039 41.431 1.00 17.77 C ATOM 838 C TYR A 123 59.332 39.622 41.935 1.00 15.04 C ATOM 839 O TYR A 123 58.436 38.902 41.513 1.00 14.16 O ATOM 840 CB TYR A 123 60.006 40.982 40.052 1.00 19.11 C ATOM 841 CG TYR A 123 60.098 42.388 39.530 1.00 21.65 C ATOM 842 CD1 TYR A 123 58.899 43.020 39.158 1.00 25.24 C ATOM 843 CD2 TYR A 123 61.335 43.032 39.445 1.00 21.72 C ATOM 844 CE1 TYR A 123 58.945 44.334 38.689 1.00 25.01 C ATOM 845 CE2 TYR A 123 61.380 44.348 38.971 1.00 22.05 C ATOM 846 CZ TYR A 123 60.184 44.980 38.603 1.00 24.94 C ATOM 847 OH TYR A 123 60.168 46.280 38.139 1.00 26.91 O ATOM 848 N VAL A 124 60.314 39.232 42.751 1.00 14.56 N ATOM 849 CA VAL A 124 60.462 37.886 43.301 1.00 15.79 C ATOM 850 C VAL A 124 60.566 37.920 44.837 1.00 13.33 C ATOM 851 O VAL A 124 61.586 38.272 45.424 1.00 13.49 O ATOM 852 CB VAL A 124 61.736 37.207 42.666 1.00 14.02 C ATOM 853 CG1 VAL A 124 61.857 35.756 43.122 1.00 14.00 C ATOM 854 CG2 VAL A 124 61.628 37.221 41.137 1.00 12.98 C ATOM 855 N GLN A 125 59.480 37.525 45.504 1.00 15.12 N ATOM 856 CA GLN A 125 59.396 37.532 46.964 1.00 14.25 C ATOM 857 C GLN A 125 58.761 36.258 47.480 1.00 14.18 C ATOM 858 O GLN A 125 57.963 35.658 46.781 1.00 12.99 O ATOM 859 CB GLN A 125 58.540 38.710 47.464 1.00 16.30 C ATOM 860 CG GLN A 125 59.202 40.063 47.285 1.00 22.28 C ATOM 861 CD GLN A 125 60.382 40.270 48.215 1.00 27.01 C ATOM 862 OE1 GLN A 125 60.210 40.216 49.432 1.00 32.30 O ATOM 863 NE2 GLN A 125 61.614 40.482 47.752 1.00 30.01 N ATOM 864 N LEU A 126 59.072 35.839 48.699 1.00 12.49 N ATOM 865 CA LEU A 126 58.465 34.650 49.243 1.00 13.35 C ATOM 866 C LEU A 126 57.043 34.954 49.700 1.00 12.59 C ATOM 867 O LEU A 126 56.705 36.045 50.161 1.00 11.18 O ATOM 868 CB LEU A 126 59.297 34.118 50.426 1.00 12.23 C ATOM 869 CG LEU A 126 60.799 33.912 50.317 1.00 13.20 C ATOM 870 CD1 LEU A 126 61.319 33.196 51.553 1.00 14.55 C ATOM 871 CD2 LEU A 126 61.109 33.120 49.080 1.00 15.07 C ATOM 872 N GLY A 127 56.200 33.941 49.540 1.00 11.33 N ATOM 873 CA GLY A 127 54.836 33.975 49.957 1.00 11.54 C ATOM 874 C GLY A 127 54.753 33.786 51.454 1.00 13.23 C ATOM 875 O GLY A 127 55.547 33.052 52.038 1.00 14.89 O ATOM 876 N VAL A 128 53.807 34.474 52.086 1.00 12.47 N ATOM 877 CA VAL A 128 53.651 34.406 53.529 1.00 12.66 C ATOM 878 C VAL A 128 52.649 33.269 53.788 1.00 10.38 C ATOM 879 O VAL A 128 51.526 33.321 53.297 1.00 12.45 O ATOM 880 CB VAL A 128 53.125 35.792 54.025 1.00 12.62 C ATOM 881 CG1 VAL A 128 52.798 35.658 55.512 1.00 16.46 C ATOM 882 CG2 VAL A 128 54.153 36.918 53.813 1.00 12.26 C ATOM 883 N LEU A 129 53.000 32.231 54.574 1.00 12.38 N ATOM 884 CA LEU A 129 52.053 31.181 54.933 1.00 12.53 C ATOM 885 C LEU A 129 51.234 31.506 56.197 1.00 14.42 C ATOM 886 O LEU A 129 51.762 32.177 57.100 1.00 14.93 O ATOM 887 CB LEU A 129 52.850 29.870 55.106 1.00 13.25 C ATOM 888 CG LEU A 129 53.533 29.362 53.833 1.00 14.57 C ATOM 889 CD1 LEU A 129 54.094 28.008 54.108 1.00 16.71 C ATOM 890 CD2 LEU A 129 52.563 29.223 52.681 1.00 14.81 C ATOM 891 N PRO A 130 49.960 31.099 56.339 1.00 12.78 N ATOM 892 CA PRO A 130 49.205 31.212 57.581 1.00 14.50 C ATOM 893 C PRO A 130 49.726 30.305 58.703 1.00 14.51 C ATOM 894 O PRO A 130 50.451 29.329 58.494 1.00 13.22 O ATOM 895 CB PRO A 130 47.772 30.904 57.177 1.00 12.12 C ATOM 896 CG PRO A 130 47.960 29.939 56.033 1.00 13.92 C ATOM 897 CD PRO A 130 49.144 30.506 55.289 1.00 13.35 C ATOM 898 N ARG A 131 49.411 30.670 59.949 1.00 16.06 N ATOM 899 CA ARG A 131 49.723 29.766 61.050 1.00 17.91 C ATOM 900 C ARG A 131 48.784 28.578 60.973 1.00 13.67 C ATOM 901 O ARG A 131 47.649 28.714 60.483 1.00 12.92 O ATOM 902 CB ARG A 131 49.560 30.491 62.409 1.00 25.93 C ATOM 903 CG ARG A 131 50.680 31.554 62.612 1.00 39.42 C ATOM 904 CD ARG A 131 52.152 31.030 62.666 1.00 50.12 C ATOM 905 NE ARG A 131 53.162 32.110 62.659 1.00 60.31 N ATOM 906 CZ ARG A 131 54.278 32.132 63.441 1.00 65.68 C ATOM 907 NH1 ARG A 131 54.577 31.147 64.316 1.00 66.88 N ATOM 908 NH2 ARG A 131 55.123 33.181 63.366 1.00 68.80 N ATOM 909 N ALA A 132 49.280 27.411 61.418 1.00 14.22 N ATOM 910 CA ALA A 132 48.519 26.156 61.393 1.00 14.01 C ATOM 911 C ALA A 132 47.173 26.231 62.081 1.00 15.78 C ATOM 912 O ALA A 132 47.078 26.816 63.162 1.00 14.01 O ATOM 913 CB ALA A 132 49.287 25.045 62.070 1.00 16.06 C ATOM 914 N GLY A 133 46.109 25.699 61.454 1.00 12.42 N ATOM 915 CA GLY A 133 44.789 25.646 62.036 1.00 11.40 C ATOM 916 C GLY A 133 43.905 26.836 61.751 1.00 11.68 C ATOM 917 O GLY A 133 42.712 26.772 62.027 1.00 12.16 O ATOM 918 N THR A 134 44.469 27.938 61.230 1.00 12.27 N ATOM 919 CA THR A 134 43.715 29.150 60.918 1.00 12.85 C ATOM 920 C THR A 134 42.583 28.894 59.957 1.00 11.47 C ATOM 921 O THR A 134 42.803 28.385 58.867 1.00 11.69 O ATOM 922 CB THR A 134 44.648 30.227 60.295 1.00 13.66 C ATOM 923 OG1 THR A 134 45.687 30.503 61.219 1.00 17.97 O ATOM 924 CG2 THR A 134 43.926 31.533 60.032 1.00 17.08 C ATOM 925 N ILE A 135 41.384 29.252 60.348 1.00 9.47 N ATOM 926 CA ILE A 135 40.189 29.186 59.540 1.00 10.97 C ATOM 927 C ILE A 135 39.715 30.642 59.371 1.00 14.31 C ATOM 928 O ILE A 135 39.593 31.399 60.338 1.00 14.95 O ATOM 929 CB ILE A 135 39.094 28.352 60.262 1.00 11.95 C ATOM 930 CG1 ILE A 135 39.633 26.968 60.584 1.00 14.79 C ATOM 931 CG2 ILE A 135 37.824 28.320 59.428 1.00 14.04 C ATOM 932 CD1 ILE A 135 39.932 26.005 59.446 1.00 18.18 C ATOM 933 N LEU A 136 39.430 31.092 58.150 1.00 15.33 N ATOM 934 CA LEU A 136 38.900 32.423 57.908 1.00 15.29 C ATOM 935 C LEU A 136 37.394 32.465 58.111 1.00 16.06 C ATOM 936 O LEU A 136 36.653 31.499 57.870 1.00 15.28 O ATOM 937 CB LEU A 136 39.216 32.880 56.461 1.00 16.04 C ATOM 938 CG LEU A 136 40.704 32.930 56.113 1.00 18.11 C ATOM 939 CD1 LEU A 136 40.897 33.096 54.617 1.00 21.51 C ATOM 940 CD2 LEU A 136 41.353 34.040 56.921 1.00 19.80 C ATOM 941 N ALA A 137 36.917 33.627 58.553 1.00 16.01 N ATOM 942 CA ALA A 137 35.481 33.798 58.649 1.00 17.87 C ATOM 943 C ALA A 137 34.844 33.866 57.247 1.00 18.01 C ATOM 944 O ALA A 137 35.507 34.108 56.239 1.00 16.27 O ATOM 945 CB ALA A 137 35.174 35.088 59.415 1.00 18.28 C ATOM 946 N ASN A 138 33.532 33.622 57.203 1.00 18.60 N ATOM 947 CA ASN A 138 32.733 33.695 56.001 1.00 18.18 C ATOM 948 C ASN A 138 32.894 35.101 55.484 1.00 19.27 C ATOM 949 O ASN A 138 32.994 36.085 56.229 1.00 17.88 O ATOM 950 CB ASN A 138 31.262 33.470 56.276 1.00 17.20 C ATOM 951 CG ASN A 138 30.433 33.247 55.024 1.00 20.09 C ATOM 952 OD1 ASN A 138 30.676 32.313 54.261 1.00 19.28 O ATOM 953 ND2 ASN A 138 29.436 34.094 54.767 1.00 20.96 N ATOM 954 N ASN A 139 32.995 35.108 54.165 1.00 18.73 N ATOM 955 CA ASN A 139 33.154 36.302 53.365 1.00 20.28 C ATOM 956 C ASN A 139 34.413 37.113 53.609 1.00 19.05 C ATOM 957 O ASN A 139 34.368 38.332 53.490 1.00 19.23 O ATOM 958 CB ASN A 139 31.929 37.170 53.556 1.00 25.51 C ATOM 959 CG ASN A 139 31.584 37.807 52.234 1.00 34.05 C ATOM 960 OD1 ASN A 139 30.958 37.179 51.377 1.00 40.16 O ATOM 961 ND2 ASN A 139 32.015 39.048 52.015 1.00 40.04 N ATOM 962 N SER A 140 35.543 36.481 53.963 1.00 15.70 N ATOM 963 CA SER A 140 36.798 37.186 54.122 1.00 14.52 C ATOM 964 C SER A 140 37.315 37.619 52.773 1.00 15.11 C ATOM 965 O SER A 140 37.031 36.951 51.785 1.00 14.47 O ATOM 966 CB SER A 140 37.867 36.321 54.772 1.00 16.20 C ATOM 967 OG SER A 140 37.468 36.086 56.112 1.00 18.16 O ATOM 968 N PRO A 141 38.003 38.759 52.678 1.00 14.63 N ATOM 969 CA PRO A 141 38.577 39.279 51.444 1.00 13.41 C ATOM 970 C PRO A 141 39.807 38.525 51.000 1.00 10.55 C ATOM 971 O PRO A 141 40.833 38.470 51.675 1.00 11.01 O ATOM 972 CB PRO A 141 38.831 40.740 51.769 1.00 14.54 C ATOM 973 CG PRO A 141 39.189 40.734 53.232 1.00 15.28 C ATOM 974 CD PRO A 141 38.095 39.783 53.731 1.00 16.40 C ATOM 975 N CYS A 142 39.669 37.908 49.826 1.00 11.19 N ATOM 976 CA CYS A 142 40.765 37.156 49.211 1.00 10.27 C ATOM 977 C CYS A 142 40.805 37.452 47.732 1.00 10.86 C ATOM 978 O CYS A 142 39.767 37.785 47.149 1.00 12.76 O ATOM 979 CB CYS A 142 40.548 35.673 49.362 1.00 12.32 C ATOM 980 SG CYS A 142 40.395 35.106 51.066 1.00 11.55 S ATOM 981 N TYR A 143 41.991 37.399 47.132 1.00 9.25 N ATOM 982 CA TYR A 143 42.160 37.538 45.699 1.00 7.77 C ATOM 983 C TYR A 143 42.678 36.232 45.103 1.00 9.84 C ATOM 984 O TYR A 143 43.627 35.658 45.663 1.00 9.61 O ATOM 985 CB TYR A 143 43.191 38.602 45.349 1.00 8.46 C ATOM 986 CG TYR A 143 42.556 39.960 45.490 1.00 15.49 C ATOM 987 CD1 TYR A 143 42.505 40.616 46.728 1.00 20.51 C ATOM 988 CD2 TYR A 143 41.972 40.533 44.365 1.00 18.94 C ATOM 989 CE1 TYR A 143 41.852 41.855 46.833 1.00 22.21 C ATOM 990 CE2 TYR A 143 41.327 41.768 44.467 1.00 25.19 C ATOM 991 CZ TYR A 143 41.275 42.414 45.699 1.00 25.16 C ATOM 992 OH TYR A 143 40.644 43.636 45.777 1.00 31.74 O ATOM 993 N ILE A 144 42.116 35.757 43.968 1.00 8.83 N ATOM 994 CA ILE A 144 42.751 34.637 43.247 1.00 8.16 C ATOM 995 C ILE A 144 43.617 35.210 42.158 1.00 8.94 C ATOM 996 O ILE A 144 43.264 36.216 41.529 1.00 9.58 O ATOM 997 CB ILE A 144 41.669 33.658 42.648 1.00 7.84 C ATOM 998 CG1 ILE A 144 42.414 32.453 42.000 1.00 9.60 C ATOM 999 CG2 ILE A 144 40.755 34.349 41.648 1.00 5.35 C ATOM 1000 CD1 ILE A 144 41.552 31.284 41.473 1.00 6.07 C ATOM 1001 N THR A 145 44.789 34.652 41.924 1.00 7.93 N ATOM 1002 CA THR A 145 45.569 35.137 40.804 1.00 7.74 C ATOM 1003 C THR A 145 45.991 34.012 39.845 1.00 10.60 C ATOM 1004 O THR A 145 46.172 32.873 40.276 1.00 9.17 O ATOM 1005 CB THR A 145 46.858 35.918 41.281 1.00 5.71 C ATOM 1006 OG1 THR A 145 47.622 35.116 42.173 1.00 5.47 O ATOM 1007 CG2 THR A 145 46.444 37.275 41.846 1.00 8.19 C ATOM 1008 N GLY A 146 46.149 34.299 38.540 1.00 8.12 N ATOM 1009 CA GLY A 146 46.676 33.295 37.629 1.00 9.19 C ATOM 1010 C GLY A 146 46.537 33.671 36.155 1.00 9.69 C ATOM 1011 O GLY A 146 45.903 34.677 35.803 1.00 8.92 O ATOM 1012 N TRP A 147 47.140 32.807 35.319 1.00 7.68 N ATOM 1013 CA TRP A 147 47.144 32.956 33.862 1.00 7.80 C ATOM 1014 C TRP A 147 46.212 31.971 33.164 1.00 9.38 C ATOM 1015 O TRP A 147 46.263 31.821 31.952 1.00 11.53 O ATOM 1016 CB TRP A 147 48.558 32.739 33.306 1.00 8.48 C ATOM 1017 CG TRP A 147 49.620 33.790 33.632 1.00 9.39 C ATOM 1018 CD1 TRP A 147 49.780 34.882 32.834 1.00 10.04 C ATOM 1019 CD2 TRP A 147 50.541 33.740 34.652 1.00 10.02 C ATOM 1020 NE1 TRP A 147 50.813 35.519 33.335 1.00 8.45 N ATOM 1021 CE2 TRP A 147 51.303 34.896 34.408 1.00 9.41 C ATOM 1022 CE3 TRP A 147 50.865 32.913 35.729 1.00 7.37 C ATOM 1023 CZ2 TRP A 147 52.386 35.235 35.229 1.00 11.23 C ATOM 1024 CZ3 TRP A 147 51.953 33.253 36.548 1.00 7.18 C ATOM 1025 CH2 TRP A 147 52.716 34.408 36.308 1.00 8.91 C ATOM 1026 N GLY A 148 45.346 31.299 33.929 1.00 9.69 N ATOM 1027 CA GLY A 148 44.410 30.330 33.395 1.00 7.88 C ATOM 1028 C GLY A 148 43.335 30.928 32.510 1.00 9.49 C ATOM 1029 O GLY A 148 43.270 32.144 32.321 1.00 10.20 O ATOM 1030 N LEU A 149 42.438 30.060 32.037 1.00 7.76 N ATOM 1031 CA LEU A 149 41.387 30.425 31.092 1.00 7.74 C ATOM 1032 C LEU A 149 40.533 31.537 31.615 1.00 8.88 C ATOM 1033 O LEU A 149 40.138 31.552 32.795 1.00 9.52 O ATOM 1034 CB LEU A 149 40.429 29.279 30.782 1.00 7.94 C ATOM 1035 CG LEU A 149 40.950 27.945 30.363 1.00 9.90 C ATOM 1036 CD1 LEU A 149 39.772 27.102 29.900 1.00 12.79 C ATOM 1037 CD2 LEU A 149 42.009 28.104 29.318 1.00 10.28 C ATOM 1038 N THR A 150 40.270 32.468 30.710 1.00 8.87 N ATOM 1039 CA THR A 150 39.468 33.607 31.094 1.00 10.03 C ATOM 1040 C THR A 150 37.977 33.426 30.858 1.00 10.87 C ATOM 1041 O THR A 150 37.150 34.270 31.235 1.00 10.66 O ATOM 1042 CB THR A 150 40.028 34.863 30.362 1.00 10.23 C ATOM 1043 OG1 THR A 150 39.856 34.692 28.967 1.00 14.19 O ATOM 1044 CG2 THR A 150 41.491 35.069 30.621 1.00 9.13 C ATOM 1045 N ARG A 151 37.589 32.297 30.250 1.00 11.55 N ATOM 1046 CA ARG A 151 36.199 31.916 30.057 1.00 12.27 C ATOM 1047 C ARG A 151 36.241 30.399 30.140 1.00 10.58 C ATOM 1048 O ARG A 151 37.274 29.796 29.839 1.00 11.78 O ATOM 1049 CB ARG A 151 35.622 32.208 28.642 1.00 19.17 C ATOM 1050 CG ARG A 151 35.542 33.557 27.934 1.00 26.69 C ATOM 1051 CD ARG A 151 34.361 34.465 28.283 1.00 34.03 C ATOM 1052 NE ARG A 151 33.052 33.811 28.152 1.00 39.13 N ATOM 1053 CZ ARG A 151 32.061 34.233 27.333 1.00 39.58 C ATOM 1054 NH1 ARG A 151 32.169 35.307 26.524 1.00 40.73 N ATOM 1055 NH2 ARG A 151 30.897 33.581 27.372 1.00 38.69 N ATOM 1056 N THR A 152 35.125 29.758 30.488 1.00 11.92 N ATOM 1057 CA THR A 152 34.967 28.299 30.424 1.00 12.16 C ATOM 1058 C THR A 152 35.237 27.895 28.963 1.00 14.05 C ATOM 1059 O THR A 152 34.671 28.486 28.039 1.00 14.86 O ATOM 1060 CB THR A 152 33.536 27.922 30.815 1.00 9.41 C ATOM 1061 OG1 THR A 152 33.409 28.313 32.174 1.00 14.56 O ATOM 1062 CG2 THR A 152 33.199 26.458 30.680 1.00 11.59 C ATOM 1063 N ASN A 153 36.126 26.926 28.749 1.00 14.23 N ATOM 1064 CA ASN A 153 36.538 26.475 27.424 1.00 14.96 C ATOM 1065 C ASN A 153 37.083 27.596 26.559 1.00 14.95 C ATOM 1066 O ASN A 153 36.934 27.509 25.339 1.00 15.11 O ATOM 1067 CB ASN A 153 35.370 25.809 26.676 1.00 19.04 C ATOM 1068 CG ASN A 153 34.910 24.544 27.381 1.00 23.80 C ATOM 1069 OD1 ASN A 153 35.706 23.653 27.729 1.00 24.64 O ATOM 1070 ND2 ASN A 153 33.596 24.510 27.614 1.00 25.16 N ATOM 1071 N GLY A 154 37.682 28.633 27.180 1.00 13.63 N ATOM 1072 CA GLY A 154 38.293 29.745 26.469 1.00 11.62 C ATOM 1073 C GLY A 154 39.772 29.503 26.257 1.00 13.55 C ATOM 1074 O GLY A 154 40.259 28.392 25.990 1.00 15.18 O ATOM 1075 N GLN A 155 40.527 30.570 26.353 1.00 14.43 N ATOM 1076 CA GLN A 155 41.966 30.447 26.288 1.00 15.79 C ATOM 1077 C GLN A 155 42.712 31.081 27.468 1.00 13.66 C ATOM 1078 O GLN A 155 42.148 31.866 28.224 1.00 10.24 O ATOM 1079 CB GLN A 155 42.494 31.050 24.978 1.00 21.59 C ATOM 1080 CG GLN A 155 42.034 32.419 24.521 1.00 29.39 C ATOM 1081 CD GLN A 155 42.764 32.889 23.260 1.00 34.23 C ATOM 1082 OE1 GLN A 155 43.277 32.111 22.451 1.00 36.53 O ATOM 1083 NE2 GLN A 155 42.853 34.200 23.067 1.00 36.81 N ATOM 1084 N LEU A 156 43.990 30.734 27.655 1.00 14.13 N ATOM 1085 CA LEU A 156 44.836 31.289 28.717 1.00 14.79 C ATOM 1086 C LEU A 156 44.989 32.798 28.626 1.00 16.90 C ATOM 1087 O LEU A 156 44.858 33.409 27.550 1.00 16.83 O ATOM 1088 CB LEU A 156 46.234 30.698 28.671 1.00 15.94 C ATOM 1089 CG LEU A 156 46.337 29.193 28.964 1.00 19.73 C ATOM 1090 CD1 LEU A 156 47.807 28.814 28.724 1.00 20.30 C ATOM 1091 CD2 LEU A 156 45.865 28.823 30.392 1.00 16.92 C ATOM 1092 N ALA A 157 45.223 33.437 29.764 1.00 15.33 N ATOM 1093 CA ALA A 157 45.495 34.858 29.753 1.00 15.51 C ATOM 1094 C ALA A 157 46.947 35.040 29.333 1.00 16.07 C ATOM 1095 O ALA A 157 47.813 34.194 29.633 1.00 17.90 O ATOM 1096 CB ALA A 157 45.296 35.403 31.140 1.00 12.82 C ATOM 1097 N GLN A 158 47.257 36.120 28.610 1.00 15.47 N ATOM 1098 CA GLN A 158 48.664 36.437 28.362 1.00 17.41 C ATOM 1099 C GLN A 158 49.301 37.143 29.552 1.00 13.63 C ATOM 1100 O GLN A 158 50.479 36.973 29.807 1.00 14.94 O ATOM 1101 CB GLN A 158 48.861 37.368 27.215 1.00 24.31 C ATOM 1102 CG GLN A 158 48.408 36.857 25.859 1.00 36.06 C ATOM 1103 CD GLN A 158 48.489 37.906 24.729 1.00 42.49 C ATOM 1104 OE1 GLN A 158 47.839 37.725 23.689 1.00 46.00 O ATOM 1105 NE2 GLN A 158 49.244 39.021 24.843 1.00 44.51 N ATOM 1106 N THR A 159 48.564 37.994 30.273 1.00 14.16 N ATOM 1107 CA THR A 159 49.082 38.719 31.431 1.00 13.59 C ATOM 1108 C THR A 159 48.386 38.250 32.721 1.00 12.30 C ATOM 1109 O THR A 159 47.212 37.843 32.687 1.00 13.30 O ATOM 1110 CB THR A 159 48.863 40.238 31.206 1.00 14.21 C ATOM 1111 OG1 THR A 159 47.474 40.482 31.134 1.00 16.33 O ATOM 1112 CG2 THR A 159 49.479 40.707 29.901 1.00 15.33 C ATOM 1113 N LEU A 160 49.072 38.369 33.880 1.00 11.84 N ATOM 1114 CA LEU A 160 48.496 37.890 35.143 1.00 12.23 C ATOM 1115 C LEU A 160 47.179 38.597 35.455 1.00 11.95 C ATOM 1116 O LEU A 160 47.063 39.809 35.272 1.00 12.78 O ATOM 1117 CB LEU A 160 49.509 38.104 36.293 1.00 11.08 C ATOM 1118 CG LEU A 160 49.146 37.580 37.676 1.00 10.58 C ATOM 1119 CD1 LEU A 160 49.052 36.061 37.608 1.00 8.70 C ATOM 1120 CD2 LEU A 160 50.203 37.943 38.681 1.00 10.14 C ATOM 1121 N GLN A 161 46.164 37.806 35.817 1.00 8.13 N ATOM 1122 CA GLN A 161 44.839 38.318 36.151 1.00 9.83 C ATOM 1123 C GLN A 161 44.583 38.159 37.638 1.00 10.91 C ATOM 1124 O GLN A 161 45.180 37.282 38.280 1.00 11.00 O ATOM 1125 CB GLN A 161 43.691 37.548 35.461 1.00 10.26 C ATOM 1126 CG GLN A 161 43.752 37.452 33.946 1.00 12.31 C ATOM 1127 CD GLN A 161 43.575 38.796 33.267 1.00 13.11 C ATOM 1128 OE1 GLN A 161 42.483 39.358 33.324 1.00 15.12 O ATOM 1129 NE2 GLN A 161 44.620 39.310 32.628 1.00 15.95 N ATOM 1130 N GLN A 162 43.699 38.982 38.181 1.00 10.49 N ATOM 1131 CA GLN A 162 43.262 38.785 39.556 1.00 13.38 C ATOM 1132 C GLN A 162 41.767 39.000 39.660 1.00 12.98 C ATOM 1133 O GLN A 162 41.156 39.715 38.864 1.00 13.63 O ATOM 1134 CB GLN A 162 43.981 39.738 40.506 1.00 14.26 C ATOM 1135 CG GLN A 162 43.684 41.172 40.198 1.00 18.96 C ATOM 1136 CD GLN A 162 44.422 42.100 41.114 1.00 17.04 C ATOM 1137 OE1 GLN A 162 45.636 42.113 41.175 1.00 18.54 O ATOM 1138 NE2 GLN A 162 43.661 42.902 41.825 1.00 19.42 N ATOM 1139 N ALA A 163 41.127 38.327 40.599 1.00 13.23 N ATOM 1140 CA ALA A 163 39.695 38.494 40.792 1.00 13.22 C ATOM 1141 C ALA A 163 39.435 38.497 42.288 1.00 11.36 C ATOM 1142 O ALA A 163 40.101 37.777 43.036 1.00 11.21 O ATOM 1143 CB ALA A 163 38.880 37.350 40.176 1.00 14.42 C ATOM 1144 N TYR A 164 38.474 39.311 42.731 1.00 11.67 N ATOM 1145 CA TYR A 164 38.141 39.408 44.130 1.00 11.56 C ATOM 1146 C TYR A 164 37.231 38.243 44.395 1.00 10.80 C ATOM 1147 O TYR A 164 36.176 38.123 43.775 1.00 12.70 O ATOM 1148 CB TYR A 164 37.448 40.710 44.359 1.00 12.54 C ATOM 1149 CG TYR A 164 37.040 40.933 45.788 1.00 13.95 C ATOM 1150 CD1 TYR A 164 38.014 41.027 46.791 1.00 17.97 C ATOM 1151 CD2 TYR A 164 35.687 41.029 46.070 1.00 16.75 C ATOM 1152 CE1 TYR A 164 37.615 41.220 48.101 1.00 18.03 C ATOM 1153 CE2 TYR A 164 35.281 41.224 47.391 1.00 21.27 C ATOM 1154 CZ TYR A 164 36.248 41.318 48.402 1.00 22.57 C ATOM 1155 OH TYR A 164 35.833 41.496 49.724 1.00 26.64 O ATOM 1156 N LEU A 165 37.643 37.397 45.335 1.00 9.07 N ATOM 1157 CA LEU A 165 36.957 36.131 45.560 1.00 10.37 C ATOM 1158 C LEU A 165 36.810 35.914 47.063 1.00 11.29 C ATOM 1159 O LEU A 165 37.644 35.248 47.661 1.00 11.27 O ATOM 1160 CB LEU A 165 37.787 34.976 44.930 1.00 12.38 C ATOM 1161 CG LEU A 165 37.093 33.893 44.101 1.00 11.95 C ATOM 1162 CD1 LEU A 165 36.540 34.532 42.852 1.00 9.43 C ATOM 1163 CD2 LEU A 165 38.062 32.782 43.751 1.00 8.65 C ATOM 1164 N PRO A 166 35.818 36.492 47.729 1.00 11.82 N ATOM 1165 CA PRO A 166 35.583 36.361 49.163 1.00 13.01 C ATOM 1166 C PRO A 166 35.260 34.957 49.614 1.00 13.63 C ATOM 1167 O PRO A 166 34.616 34.224 48.863 1.00 12.83 O ATOM 1168 CB PRO A 166 34.462 37.318 49.422 1.00 15.56 C ATOM 1169 CG PRO A 166 33.694 37.392 48.119 1.00 16.69 C ATOM 1170 CD PRO A 166 34.823 37.368 47.118 1.00 14.04 C ATOM 1171 N THR A 167 35.620 34.550 50.821 1.00 14.28 N ATOM 1172 CA THR A 167 35.421 33.166 51.166 1.00 12.03 C ATOM 1173 C THR A 167 33.984 32.783 51.463 1.00 13.99 C ATOM 1174 O THR A 167 33.121 33.622 51.727 1.00 13.60 O ATOM 1175 CB THR A 167 36.327 32.814 52.346 1.00 14.28 C ATOM 1176 OG1 THR A 167 35.813 33.542 53.453 1.00 12.69 O ATOM 1177 CG2 THR A 167 37.805 33.108 52.083 1.00 14.31 C ATOM 1178 N VAL A 168 33.710 31.477 51.351 1.00 12.25 N ATOM 1179 CA VAL A 168 32.398 30.889 51.637 1.00 13.80 C ATOM 1180 C VAL A 168 32.787 29.872 52.697 1.00 16.47 C ATOM 1181 O VAL A 168 33.563 28.951 52.386 1.00 16.50 O ATOM 1182 CB VAL A 168 31.794 30.139 50.415 1.00 11.38 C ATOM 1183 CG1 VAL A 168 30.432 29.638 50.754 1.00 12.27 C ATOM 1184 CG2 VAL A 168 31.689 31.048 49.222 1.00 14.01 C ATOM 1185 N ASP A 169 32.285 29.980 53.941 1.00 16.38 N ATOM 1186 CA ASP A 169 32.769 29.053 54.947 1.00 18.65 C ATOM 1187 C ASP A 169 32.266 27.632 54.746 1.00 17.74 C ATOM 1188 O ASP A 169 31.359 27.388 53.953 1.00 17.72 O ATOM 1189 CB ASP A 169 32.409 29.582 56.344 1.00 19.48 C ATOM 1190 CG ASP A 169 30.968 29.641 56.817 1.00 24.59 C ATOM 1191 OD1 ASP A 169 30.079 29.046 56.217 1.00 26.31 O ATOM 1192 OD2 ASP A 169 30.738 30.291 57.834 1.00 24.58 O ATOM 1193 N TYR A 170 32.844 26.713 55.507 1.00 18.85 N ATOM 1194 CA TYR A 170 32.610 25.308 55.315 1.00 19.40 C ATOM 1195 C TYR A 170 31.175 24.909 55.488 1.00 20.05 C ATOM 1196 O TYR A 170 30.680 24.097 54.705 1.00 18.83 O ATOM 1197 CB TYR A 170 33.506 24.536 56.265 1.00 21.04 C ATOM 1198 CG TYR A 170 33.214 23.051 56.250 1.00 23.14 C ATOM 1199 CD1 TYR A 170 33.602 22.282 55.145 1.00 26.72 C ATOM 1200 CD2 TYR A 170 32.532 22.469 57.332 1.00 26.68 C ATOM 1201 CE1 TYR A 170 33.314 20.920 55.119 1.00 25.93 C ATOM 1202 CE2 TYR A 170 32.241 21.102 57.307 1.00 27.72 C ATOM 1203 CZ TYR A 170 32.645 20.334 56.199 1.00 28.85 C ATOM 1204 OH TYR A 170 32.446 18.960 56.205 1.00 27.20 O ATOM 1205 N ALA A 171 30.485 25.483 56.457 1.00 19.61 N ATOM 1206 CA ALA A 171 29.101 25.118 56.673 1.00 21.92 C ATOM 1207 C ALA A 171 28.224 25.480 55.490 1.00 23.01 C ATOM 1208 O ALA A 171 27.300 24.738 55.163 1.00 24.62 O ATOM 1209 CB ALA A 171 28.552 25.819 57.901 1.00 22.12 C ATOM 1210 N ILE A 172 28.501 26.598 54.811 1.00 22.62 N ATOM 1211 CA ILE A 172 27.740 26.953 53.626 1.00 22.20 C ATOM 1212 C ILE A 172 28.229 26.155 52.417 1.00 21.87 C ATOM 1213 O ILE A 172 27.414 25.602 51.661 1.00 23.60 O ATOM 1214 CB ILE A 172 27.877 28.447 53.367 1.00 23.58 C ATOM 1215 CG1 ILE A 172 27.265 29.244 54.528 1.00 26.43 C ATOM 1216 CG2 ILE A 172 27.127 28.796 52.093 1.00 23.26 C ATOM 1217 CD1 ILE A 172 27.460 30.777 54.480 1.00 29.86 C ATOM 1218 N CYS A 173 29.550 26.023 52.248 1.00 20.25 N ATOM 1219 CA CYS A 173 30.085 25.356 51.077 1.00 19.04 C ATOM 1220 C CYS A 173 29.723 23.876 50.994 1.00 18.75 C ATOM 1221 O CYS A 173 29.491 23.342 49.908 1.00 16.80 O ATOM 1222 CB CYS A 173 31.593 25.525 51.061 1.00 17.25 C ATOM 1223 SG CYS A 173 32.221 25.307 49.374 1.00 14.89 S ATOM 1224 N SER A 174 29.611 23.206 52.138 1.00 18.61 N ATOM 1225 CA SER A 174 29.246 21.819 52.096 1.00 19.62 C ATOM 1226 C SER A 174 27.756 21.616 52.240 1.00 19.20 C ATOM 1227 O SER A 174 27.318 20.478 52.376 1.00 20.88 O ATOM 1228 CB SER A 174 30.015 21.085 53.173 1.00 19.00 C ATOM 1229 OG SER A 174 29.675 21.542 54.466 1.00 23.92 O ATOM 1230 N SER A 175 26.928 22.660 52.158 1.00 19.31 N ATOM 1231 CA SER A 175 25.500 22.463 52.244 1.00 19.81 C ATOM 1232 C SER A 175 25.071 21.940 50.890 1.00 22.90 C ATOM 1233 O SER A 175 25.757 22.156 49.872 1.00 22.99 O ATOM 1234 CB SER A 175 24.782 23.757 52.557 1.00 17.66 C ATOM 1235 OG SER A 175 24.702 24.666 51.472 1.00 22.90 O ATOM 1236 N SER A 176 23.950 21.222 50.843 1.00 25.07 N ATOM 1237 CA SER A 176 23.537 20.574 49.607 1.00 27.40 C ATOM 1238 C SER A 176 23.314 21.487 48.400 1.00 26.86 C ATOM 1239 O SER A 176 23.465 21.041 47.265 1.00 28.07 O ATOM 1240 CB SER A 176 22.275 19.739 49.916 1.00 30.02 C ATOM 1241 OG SER A 176 21.199 20.458 50.511 1.00 36.25 O ATOM 1242 N SER A 177 23.023 22.778 48.556 1.00 27.00 N ATOM 1243 CA SER A 177 22.851 23.663 47.403 1.00 27.03 C ATOM 1244 C SER A 177 24.156 24.169 46.760 1.00 25.15 C ATOM 1245 O SER A 177 24.150 24.736 45.662 1.00 24.45 O ATOM 1246 CB SER A 177 21.947 24.858 47.831 1.00 29.12 C ATOM 1247 OG SER A 177 22.066 25.296 49.188 1.00 35.57 O ATOM 1248 N TYR A 178 25.282 23.972 47.467 1.00 22.58 N ATOM 1249 CA TYR A 178 26.628 24.306 47.009 1.00 19.15 C ATOM 1250 C TYR A 178 27.369 23.040 46.614 1.00 17.43 C ATOM 1251 O TYR A 178 26.943 22.403 45.659 1.00 16.91 O ATOM 1252 CB TYR A 178 27.403 25.033 48.110 1.00 19.85 C ATOM 1253 CG TYR A 178 26.936 26.453 48.295 1.00 19.44 C ATOM 1254 CD1 TYR A 178 25.648 26.697 48.769 1.00 20.35 C ATOM 1255 CD2 TYR A 178 27.804 27.490 47.954 1.00 21.19 C ATOM 1256 CE1 TYR A 178 25.208 28.000 48.907 1.00 23.84 C ATOM 1257 CE2 TYR A 178 27.372 28.796 48.082 1.00 21.78 C ATOM 1258 CZ TYR A 178 26.078 29.036 48.552 1.00 25.26 C ATOM 1259 OH TYR A 178 25.630 30.337 48.640 1.00 29.53 O ATOM 1260 N TRP A 179 28.438 22.590 47.283 1.00 15.81 N ATOM 1261 CA TRP A 179 29.178 21.425 46.843 1.00 14.58 C ATOM 1262 C TRP A 179 28.825 20.158 47.577 1.00 15.60 C ATOM 1263 O TRP A 179 29.259 19.074 47.206 1.00 15.80 O ATOM 1264 CB TRP A 179 30.638 21.704 47.014 1.00 10.68 C ATOM 1265 CG TRP A 179 31.306 22.452 45.874 1.00 13.09 C ATOM 1266 CD1 TRP A 179 31.641 23.789 45.945 1.00 12.92 C ATOM 1267 CD2 TRP A 179 31.699 21.873 44.701 1.00 13.86 C ATOM 1268 NE1 TRP A 179 32.262 24.051 44.808 1.00 12.64 N ATOM 1269 CE2 TRP A 179 32.326 22.956 44.034 1.00 12.99 C ATOM 1270 CE3 TRP A 179 31.605 20.616 44.123 1.00 13.14 C ATOM 1271 CZ2 TRP A 179 32.881 22.776 42.753 1.00 12.21 C ATOM 1272 CZ3 TRP A 179 32.149 20.444 42.847 1.00 15.91 C ATOM 1273 CH2 TRP A 179 32.782 21.503 42.166 1.00 14.09 C ATOM 1274 N GLY A 180 28.074 20.277 48.664 1.00 15.83 N ATOM 1275 CA GLY A 180 27.719 19.125 49.483 1.00 16.58 C ATOM 1276 C GLY A 180 28.944 18.478 50.082 1.00 18.19 C ATOM 1277 O GLY A 180 29.944 19.129 50.416 1.00 18.94 O ATOM 1278 N SER A 181 28.839 17.145 50.120 1.00 19.51 N ATOM 1279 CA SER A 181 29.881 16.222 50.565 1.00 20.26 C ATOM 1280 C SER A 181 31.235 16.299 49.891 1.00 17.73 C ATOM 1281 O SER A 181 32.232 15.824 50.432 1.00 18.28 O ATOM 1282 CB SER A 181 29.466 14.766 50.390 1.00 22.21 C ATOM 1283 OG SER A 181 28.769 14.312 51.523 1.00 28.46 O ATOM 1284 N THR A 182 31.291 16.821 48.682 1.00 16.34 N ATOM 1285 CA THR A 182 32.539 16.864 47.951 1.00 15.15 C ATOM 1286 C THR A 182 33.515 17.765 48.670 1.00 13.10 C ATOM 1287 O THR A 182 34.690 17.421 48.625 1.00 14.50 O ATOM 1288 CB THR A 182 32.200 17.336 46.539 1.00 17.28 C ATOM 1289 OG1 THR A 182 31.377 16.291 46.046 1.00 18.72 O ATOM 1290 CG2 THR A 182 33.375 17.574 45.620 1.00 17.98 C ATOM 1291 N VAL A 183 33.120 18.855 49.356 1.00 11.33 N ATOM 1292 CA VAL A 183 34.165 19.646 50.033 1.00 12.21 C ATOM 1293 C VAL A 183 34.349 19.158 51.448 1.00 12.41 C ATOM 1294 O VAL A 183 33.427 18.725 52.124 1.00 15.19 O ATOM 1295 CB VAL A 183 33.888 21.174 50.102 1.00 14.68 C ATOM 1296 CG1 VAL A 183 33.857 21.630 48.660 1.00 16.16 C ATOM 1297 CG2 VAL A 183 32.628 21.552 50.801 1.00 16.59 C ATOM 1298 N LYS A 184 35.610 19.128 51.798 1.00 11.85 N ATOM 1299 CA LYS A 184 36.046 18.708 53.104 1.00 12.76 C ATOM 1300 C LYS A 184 36.480 19.966 53.849 1.00 14.30 C ATOM 1301 O LYS A 184 36.728 21.024 53.275 1.00 12.58 O ATOM 1302 CB LYS A 184 37.248 17.747 53.006 1.00 10.65 C ATOM 1303 CG LYS A 184 37.052 16.560 52.054 1.00 14.86 C ATOM 1304 CD LYS A 184 35.784 15.804 52.402 1.00 15.58 C ATOM 1305 CE LYS A 184 35.466 14.618 51.488 1.00 18.57 C ATOM 1306 NZ LYS A 184 35.004 15.001 50.158 1.00 16.58 N ATOM 1307 N ASN A 185 36.630 19.812 55.162 1.00 15.07 N ATOM 1308 CA ASN A 185 37.134 20.869 56.020 1.00 17.39 C ATOM 1309 C ASN A 185 38.643 21.147 55.792 1.00 14.69 C ATOM 1310 O ASN A 185 39.116 22.198 56.234 1.00 14.25 O ATOM 1311 CB ASN A 185 36.834 20.492 57.497 1.00 22.38 C ATOM 1312 CG ASN A 185 37.098 21.662 58.459 1.00 29.56 C ATOM 1313 OD1 ASN A 185 37.642 21.428 59.538 1.00 34.55 O ATOM 1314 ND2 ASN A 185 36.810 22.950 58.173 1.00 31.07 N ATOM 1315 N SER A 186 39.416 20.274 55.081 1.00 10.71 N ATOM 1316 CA SER A 186 40.789 20.543 54.657 1.00 9.08 C ATOM 1317 C SER A 186 40.816 21.433 53.386 1.00 8.56 C ATOM 1318 O SER A 186 41.870 21.577 52.757 1.00 8.90 O ATOM 1319 CB SER A 186 41.531 19.237 54.341 1.00 9.04 C ATOM 1320 OG SER A 186 40.846 18.549 53.296 1.00 10.97 O ATOM 1321 N MET A 187 39.692 22.023 52.979 1.00 7.52 N ATOM 1322 CA MET A 187 39.585 22.867 51.804 1.00 10.21 C ATOM 1323 C MET A 187 38.993 24.237 52.154 1.00 12.42 C ATOM 1324 O MET A 187 38.270 24.386 53.138 1.00 11.96 O ATOM 1325 CB MET A 187 38.671 22.216 50.791 1.00 10.94 C ATOM 1326 CG MET A 187 39.204 20.911 50.205 1.00 11.39 C ATOM 1327 SD MET A 187 37.858 20.000 49.438 1.00 10.12 S ATOM 1328 CE MET A 187 38.604 18.454 49.020 1.00 10.58 C ATOM 1329 N VAL A 188 39.304 25.263 51.350 1.00 12.50 N ATOM 1330 CA VAL A 188 38.697 26.598 51.432 1.00 13.07 C ATOM 1331 C VAL A 188 37.879 26.815 50.155 1.00 11.00 C ATOM 1332 O VAL A 188 38.297 26.453 49.077 1.00 13.48 O ATOM 1333 CB VAL A 188 39.768 27.717 51.529 1.00 13.39 C ATOM 1334 CG1 VAL A 188 39.170 29.107 51.572 1.00 13.79 C ATOM 1335 CG2 VAL A 188 40.536 27.482 52.798 1.00 12.84 C ATOM 1336 N CYS A 189 36.697 27.373 50.265 1.00 12.00 N ATOM 1337 CA CYS A 189 35.841 27.710 49.152 1.00 11.22 C ATOM 1338 C CYS A 189 35.862 29.210 49.013 1.00 12.82 C ATOM 1339 O CYS A 189 35.793 29.898 50.024 1.00 11.42 O ATOM 1340 CB CYS A 189 34.411 27.300 49.402 1.00 13.78 C ATOM 1341 SG CYS A 189 34.212 25.515 49.558 1.00 12.57 S ATOM 1342 N ALA A 190 35.977 29.752 47.793 1.00 11.38 N ATOM 1343 CA ALA A 190 35.901 31.199 47.611 1.00 10.48 C ATOM 1344 C ALA A 190 35.139 31.493 46.321 1.00 10.01 C ATOM 1345 O ALA A 190 35.229 30.723 45.356 1.00 10.78 O ATOM 1346 CB ALA A 190 37.304 31.764 47.552 1.00 7.99 C ATOM 1347 N GLY A 191 34.278 32.528 46.318 1.00 9.54 N ATOM 1348 CA GLY A 191 33.535 32.923 45.138 1.00 10.94 C ATOM 1349 C GLY A 191 32.145 32.340 45.049 1.00 11.49 C ATOM 1350 O GLY A 191 31.391 32.402 46.015 1.00 15.03 O ATOM 1351 N GLY A 192 31.795 31.810 43.883 1.00 11.09 N ATOM 1352 CA GLY A 192 30.468 31.222 43.705 1.00 11.75 C ATOM 1353 C GLY A 192 29.407 32.187 43.205 1.00 13.13 C ATOM 1354 O GLY A 192 28.250 31.816 43.138 1.00 12.39 O ATOM 1355 N ASP A 193 29.761 33.422 42.839 1.00 14.59 N ATOM 1356 CA ASP A 193 28.770 34.392 42.363 1.00 16.42 C ATOM 1357 C ASP A 193 28.282 34.182 40.922 1.00 17.95 C ATOM 1358 O ASP A 193 27.339 34.831 40.484 1.00 20.10 O ATOM 1359 CB ASP A 193 29.326 35.854 42.519 1.00 17.13 C ATOM 1360 CG ASP A 193 30.544 36.360 41.725 1.00 19.55 C ATOM 1361 OD1 ASP A 193 31.034 35.665 40.846 1.00 19.13 O ATOM 1362 OD2 ASP A 193 31.043 37.457 41.995 1.00 20.30 O ATOM 1363 N GLY A 194 28.878 33.264 40.170 1.00 17.24 N ATOM 1364 CA GLY A 194 28.495 33.016 38.790 1.00 17.43 C ATOM 1365 C GLY A 194 29.245 33.916 37.820 1.00 18.50 C ATOM 1366 O GLY A 194 29.095 33.748 36.617 1.00 21.56 O ATOM 1367 N VAL A 195 30.084 34.850 38.281 1.00 16.91 N ATOM 1368 CA VAL A 195 30.838 35.793 37.447 1.00 16.26 C ATOM 1369 C VAL A 195 32.346 35.605 37.463 1.00 15.66 C ATOM 1370 O VAL A 195 33.052 35.707 36.457 1.00 15.31 O ATOM 1371 CB VAL A 195 30.553 37.275 37.882 1.00 15.62 C ATOM 1372 CG1 VAL A 195 31.218 38.227 36.885 1.00 12.84 C ATOM 1373 CG2 VAL A 195 29.042 37.511 37.993 1.00 17.52 C ATOM 1374 N ARG A 196 32.829 35.354 38.673 1.00 14.43 N ATOM 1375 CA ARG A 196 34.244 35.333 38.967 1.00 13.75 C ATOM 1376 C ARG A 196 34.619 33.972 39.483 1.00 10.11 C ATOM 1377 O ARG A 196 33.910 33.436 40.322 1.00 11.55 O ATOM 1378 CB ARG A 196 34.598 36.365 40.036 1.00 16.23 C ATOM 1379 CG ARG A 196 34.460 37.700 39.378 1.00 21.25 C ATOM 1380 CD ARG A 196 34.743 38.820 40.316 1.00 20.80 C ATOM 1381 NE ARG A 196 33.700 38.932 41.323 1.00 21.73 N ATOM 1382 CZ ARG A 196 33.610 40.024 42.086 1.00 22.00 C ATOM 1383 NH1 ARG A 196 34.467 41.054 41.927 1.00 20.62 N ATOM 1384 NH2 ARG A 196 32.717 40.033 43.077 1.00 21.75 N ATOM 1385 N SER A 197 35.713 33.421 38.988 1.00 10.11 N ATOM 1386 CA SER A 197 36.198 32.147 39.479 1.00 9.45 C ATOM 1387 C SER A 197 37.592 31.883 39.001 1.00 6.91 C ATOM 1388 O SER A 197 38.159 32.562 38.140 1.00 9.22 O ATOM 1389 CB SER A 197 35.297 31.007 38.996 1.00 12.93 C ATOM 1390 OG SER A 197 35.336 30.935 37.577 1.00 20.65 O ATOM 1391 N GLY A 198 38.160 30.827 39.565 1.00 7.32 N ATOM 1392 CA GLY A 198 39.364 30.208 39.003 1.00 8.03 C ATOM 1393 C GLY A 198 38.972 29.406 37.764 1.00 7.77 C ATOM 1394 O GLY A 198 37.780 29.191 37.521 1.00 11.00 O ATOM 1395 N CYS A 199 39.901 28.961 36.939 1.00 8.22 N ATOM 1396 CA CYS A 199 39.509 28.154 35.759 1.00 8.73 C ATOM 1397 C CYS A 199 40.744 27.340 35.398 1.00 8.78 C ATOM 1398 O CYS A 199 41.796 27.568 35.999 1.00 10.58 O ATOM 1399 CB CYS A 199 39.096 29.056 34.534 1.00 9.70 C ATOM 1400 SG CYS A 199 37.954 28.233 33.374 1.00 10.88 S ATOM 1401 N GLN A 200 40.713 26.389 34.451 1.00 10.41 N ATOM 1402 CA GLN A 200 41.885 25.592 34.095 1.00 9.08 C ATOM 1403 C GLN A 200 43.107 26.415 33.856 1.00 9.28 C ATOM 1404 O GLN A 200 42.942 27.456 33.234 1.00 10.66 O ATOM 1405 CB GLN A 200 41.655 24.810 32.835 1.00 15.06 C ATOM 1406 CG GLN A 200 40.680 23.683 33.098 1.00 23.03 C ATOM 1407 CD GLN A 200 39.292 24.017 32.633 1.00 28.01 C ATOM 1408 OE1 GLN A 200 38.840 23.535 31.590 1.00 34.19 O ATOM 1409 NE2 GLN A 200 38.569 24.812 33.404 1.00 30.17 N ATOM 1410 N GLY A 201 44.286 26.022 34.354 1.00 5.85 N ATOM 1411 CA GLY A 201 45.546 26.785 34.241 1.00 7.92 C ATOM 1412 C GLY A 201 45.821 27.690 35.457 1.00 5.59 C ATOM 1413 O GLY A 201 46.904 28.245 35.569 1.00 8.61 O ATOM 1414 N ASP A 202 44.808 27.926 36.298 1.00 7.47 N ATOM 1415 CA ASP A 202 44.988 28.610 37.575 1.00 6.56 C ATOM 1416 C ASP A 202 45.353 27.604 38.678 1.00 9.54 C ATOM 1417 O ASP A 202 45.887 27.999 39.703 1.00 6.94 O ATOM 1418 CB ASP A 202 43.733 29.345 38.003 1.00 6.07 C ATOM 1419 CG ASP A 202 43.380 30.501 37.103 1.00 4.86 C ATOM 1420 OD1 ASP A 202 44.282 31.198 36.652 1.00 8.85 O ATOM 1421 OD2 ASP A 202 42.199 30.695 36.860 1.00 7.20 O ATOM 1422 N SER A 203 45.120 26.301 38.460 1.00 12.03 N ATOM 1423 CA SER A 203 45.496 25.184 39.340 1.00 11.28 C ATOM 1424 C SER A 203 46.832 25.356 40.015 1.00 8.97 C ATOM 1425 O SER A 203 47.781 25.791 39.370 1.00 7.68 O ATOM 1426 CB SER A 203 45.580 23.890 38.534 1.00 13.93 C ATOM 1427 OG SER A 203 44.314 23.381 38.110 1.00 16.67 O ATOM 1428 N GLY A 204 46.951 25.077 41.300 1.00 7.04 N ATOM 1429 CA GLY A 204 48.247 25.158 41.935 1.00 6.36 C ATOM 1430 C GLY A 204 48.566 26.524 42.502 1.00 7.46 C ATOM 1431 O GLY A 204 49.417 26.631 43.396 1.00 6.58 O ATOM 1432 N GLY A 205 47.878 27.567 41.978 1.00 7.72 N ATOM 1433 CA GLY A 205 48.228 28.922 42.354 1.00 6.49 C ATOM 1434 C GLY A 205 47.653 29.337 43.694 1.00 7.96 C ATOM 1435 O GLY A 205 46.865 28.597 44.306 1.00 9.08 O ATOM 1436 N PRO A 206 48.010 30.549 44.151 1.00 7.38 N ATOM 1437 CA PRO A 206 47.538 31.146 45.403 1.00 6.75 C ATOM 1438 C PRO A 206 46.131 31.751 45.478 1.00 7.46 C ATOM 1439 O PRO A 206 45.570 32.262 44.485 1.00 6.98 O ATOM 1440 CB PRO A 206 48.619 32.164 45.712 1.00 3.94 C ATOM 1441 CG PRO A 206 48.841 32.717 44.308 1.00 7.28 C ATOM 1442 CD PRO A 206 48.937 31.463 43.457 1.00 4.71 C ATOM 1443 N LEU A 207 45.556 31.637 46.682 1.00 6.01 N ATOM 1444 CA LEU A 207 44.400 32.439 47.073 1.00 6.18 C ATOM 1445 C LEU A 207 45.077 33.308 48.157 1.00 7.30 C ATOM 1446 O LEU A 207 45.624 32.791 49.148 1.00 7.76 O ATOM 1447 CB LEU A 207 43.247 31.589 47.693 1.00 5.97 C ATOM 1448 CG LEU A 207 41.992 32.358 48.218 1.00 4.05 C ATOM 1449 CD1 LEU A 207 41.246 33.024 47.068 1.00 6.67 C ATOM 1450 CD2 LEU A 207 41.077 31.399 48.970 1.00 7.99 C ATOM 1451 N HIS A 208 45.156 34.627 47.931 1.00 7.62 N ATOM 1452 CA HIS A 208 45.818 35.576 48.844 1.00 7.94 C ATOM 1453 C HIS A 208 44.728 36.187 49.672 1.00 8.26 C ATOM 1454 O HIS A 208 43.806 36.778 49.103 1.00 8.96 O ATOM 1455 CB HIS A 208 46.483 36.740 48.138 1.00 6.17 C ATOM 1456 CG HIS A 208 47.324 36.319 46.959 1.00 9.32 C ATOM 1457 ND1 HIS A 208 48.604 35.971 46.999 1.00 8.26 N ATOM 1458 CD2 HIS A 208 46.916 36.270 45.636 1.00 10.85 C ATOM 1459 CE1 HIS A 208 49.011 35.724 45.759 1.00 10.58 C ATOM 1460 NE2 HIS A 208 47.979 35.909 44.963 1.00 12.70 N ATOM 1461 N CYS A 209 44.794 36.094 51.003 1.00 10.31 N ATOM 1462 CA CYS A 209 43.768 36.662 51.874 1.00 9.59 C ATOM 1463 C CYS A 209 44.396 37.619 52.867 1.00 10.04 C ATOM 1464 O CYS A 209 45.472 37.361 53.397 1.00 9.32 O ATOM 1465 CB CYS A 209 43.045 35.584 52.653 1.00 10.10 C ATOM 1466 SG CYS A 209 42.199 34.388 51.566 1.00 10.46 S ATOM 1467 N LEU A 210 43.710 38.746 53.064 1.00 12.01 N ATOM 1468 CA LEU A 210 44.150 39.791 53.975 1.00 16.22 C ATOM 1469 C LEU A 210 43.758 39.469 55.432 1.00 16.11 C ATOM 1470 O LEU A 210 42.593 39.391 55.823 1.00 16.56 O ATOM 1471 CB LEU A 210 43.540 41.143 53.518 1.00 18.02 C ATOM 1472 CG LEU A 210 44.065 42.433 54.201 1.00 21.65 C ATOM 1473 CD1 LEU A 210 45.570 42.555 53.951 1.00 22.49 C ATOM 1474 CD2 LEU A 210 43.335 43.663 53.655 1.00 21.54 C ATOM 1475 N VAL A 211 44.793 39.255 56.242 1.00 16.99 N ATOM 1476 CA VAL A 211 44.675 38.906 57.646 1.00 19.04 C ATOM 1477 C VAL A 211 45.700 39.779 58.367 1.00 18.36 C ATOM 1478 O VAL A 211 46.889 39.687 58.062 1.00 18.05 O ATOM 1479 CB VAL A 211 45.020 37.417 57.848 1.00 22.08 C ATOM 1480 CG1 VAL A 211 45.077 37.062 59.313 1.00 23.93 C ATOM 1481 CG2 VAL A 211 43.955 36.568 57.209 1.00 22.44 C ATOM 1482 N ASN A 212 45.276 40.627 59.315 1.00 18.74 N ATOM 1483 CA ASN A 212 46.155 41.475 60.132 1.00 19.98 C ATOM 1484 C ASN A 212 47.094 42.352 59.310 1.00 17.73 C ATOM 1485 O ASN A 212 48.302 42.401 59.529 1.00 18.87 O ATOM 1486 CB ASN A 212 47.006 40.618 61.097 1.00 23.71 C ATOM 1487 CG ASN A 212 46.182 39.752 62.055 1.00 29.76 C ATOM 1488 OD1 ASN A 212 46.465 38.561 62.278 1.00 32.63 O ATOM 1489 ND2 ASN A 212 45.134 40.342 62.634 1.00 31.27 N ATOM 1490 N GLY A 213 46.493 42.964 58.294 1.00 14.91 N ATOM 1491 CA GLY A 213 47.178 43.897 57.444 1.00 11.87 C ATOM 1492 C GLY A 213 48.185 43.275 56.525 1.00 14.76 C ATOM 1493 O GLY A 213 48.959 43.999 55.912 1.00 15.07 O ATOM 1494 N GLN A 214 48.179 41.950 56.359 1.00 14.17 N ATOM 1495 CA GLN A 214 49.205 41.263 55.586 1.00 15.43 C ATOM 1496 C GLN A 214 48.533 40.284 54.615 1.00 14.62 C ATOM 1497 O GLN A 214 47.610 39.603 55.041 1.00 14.30 O ATOM 1498 CB GLN A 214 50.066 40.555 56.605 1.00 15.94 C ATOM 1499 CG GLN A 214 51.264 39.860 56.048 1.00 19.80 C ATOM 1500 CD GLN A 214 52.128 39.170 57.107 1.00 20.39 C ATOM 1501 OE1 GLN A 214 53.320 39.473 57.259 1.00 24.35 O ATOM 1502 NE2 GLN A 214 51.558 38.197 57.822 1.00 22.43 N ATOM 1503 N TYR A 215 48.833 40.202 53.315 1.00 14.11 N ATOM 1504 CA TYR A 215 48.265 39.149 52.483 1.00 13.61 C ATOM 1505 C TYR A 215 48.968 37.829 52.723 1.00 12.39 C ATOM 1506 O TYR A 215 50.180 37.793 52.619 1.00 14.64 O ATOM 1507 CB TYR A 215 48.425 39.498 51.061 1.00 14.44 C ATOM 1508 CG TYR A 215 47.258 40.356 50.629 1.00 17.88 C ATOM 1509 CD1 TYR A 215 46.036 39.744 50.371 1.00 16.16 C ATOM 1510 CD2 TYR A 215 47.408 41.735 50.451 1.00 21.97 C ATOM 1511 CE1 TYR A 215 44.961 40.494 49.925 1.00 19.19 C ATOM 1512 CE2 TYR A 215 46.325 42.500 50.006 1.00 24.30 C ATOM 1513 CZ TYR A 215 45.117 41.856 49.746 1.00 24.11 C ATOM 1514 OH TYR A 215 44.033 42.565 49.282 1.00 30.65 O ATOM 1515 N ALA A 216 48.285 36.763 53.100 1.00 11.17 N ATOM 1516 CA ALA A 216 48.944 35.488 53.251 1.00 8.90 C ATOM 1517 C ALA A 216 48.295 34.521 52.289 1.00 9.12 C ATOM 1518 O ALA A 216 47.155 34.705 51.878 1.00 6.94 O ATOM 1519 CB ALA A 216 48.780 34.987 54.667 1.00 9.71 C ATOM 1520 N VAL A 217 49.005 33.475 51.896 1.00 9.17 N ATOM 1521 CA VAL A 217 48.483 32.483 50.937 1.00 9.15 C ATOM 1522 C VAL A 217 47.743 31.400 51.731 1.00 8.85 C ATOM 1523 O VAL A 217 48.356 30.558 52.388 1.00 10.09 O ATOM 1524 CB VAL A 217 49.665 31.869 50.140 1.00 12.18 C ATOM 1525 CG1 VAL A 217 49.106 30.837 49.159 1.00 11.76 C ATOM 1526 CG2 VAL A 217 50.492 32.965 49.462 1.00 10.13 C ATOM 1527 N HIS A 218 46.408 31.436 51.679 1.00 7.84 N ATOM 1528 CA HIS A 218 45.553 30.528 52.425 1.00 7.30 C ATOM 1529 C HIS A 218 45.050 29.356 51.584 1.00 8.46 C ATOM 1530 O HIS A 218 44.526 28.366 52.131 1.00 8.23 O ATOM 1531 CB HIS A 218 44.340 31.284 52.967 1.00 8.92 C ATOM 1532 CG HIS A 218 44.628 32.019 54.279 1.00 10.64 C ATOM 1533 ND1 HIS A 218 44.180 31.691 55.493 1.00 10.75 N ATOM 1534 CD2 HIS A 218 45.483 33.092 54.419 1.00 14.34 C ATOM 1535 CE1 HIS A 218 44.743 32.506 56.359 1.00 14.78 C ATOM 1536 NE2 HIS A 218 45.531 33.354 55.706 1.00 12.41 N ATOM 1537 N GLY A 219 45.180 29.445 50.250 1.00 7.23 N ATOM 1538 CA GLY A 219 44.659 28.367 49.401 1.00 6.28 C ATOM 1539 C GLY A 219 45.628 27.993 48.288 1.00 5.34 C ATOM 1540 O GLY A 219 46.475 28.794 47.905 1.00 6.80 O ATOM 1541 N VAL A 220 45.573 26.746 47.822 1.00 7.32 N ATOM 1542 CA VAL A 220 46.273 26.292 46.615 1.00 5.62 C ATOM 1543 C VAL A 220 45.097 25.897 45.701 1.00 6.97 C ATOM 1544 O VAL A 220 44.303 25.011 46.059 1.00 5.93 O ATOM 1545 CB VAL A 220 47.187 25.074 46.930 1.00 6.49 C ATOM 1546 CG1 VAL A 220 47.723 24.488 45.651 1.00 7.98 C ATOM 1547 CG2 VAL A 220 48.425 25.493 47.714 1.00 7.83 C ATOM 1548 N THR A 221 44.896 26.517 44.525 1.00 6.24 N ATOM 1549 CA THR A 221 43.697 26.257 43.694 1.00 7.32 C ATOM 1550 C THR A 221 43.632 24.790 43.246 1.00 7.97 C ATOM 1551 O THR A 221 44.609 24.220 42.746 1.00 8.36 O ATOM 1552 CB THR A 221 43.699 27.186 42.439 1.00 9.07 C ATOM 1553 OG1 THR A 221 43.998 28.538 42.827 1.00 9.53 O ATOM 1554 CG2 THR A 221 42.359 27.127 41.752 1.00 5.81 C ATOM 1555 N SER A 222 42.478 24.167 43.465 1.00 8.65 N ATOM 1556 CA SER A 222 42.342 22.742 43.256 1.00 9.57 C ATOM 1557 C SER A 222 41.283 22.365 42.225 1.00 9.40 C ATOM 1558 O SER A 222 41.618 21.664 41.264 1.00 11.94 O ATOM 1559 CB SER A 222 42.014 22.028 44.615 1.00 10.44 C ATOM 1560 OG SER A 222 41.964 20.601 44.518 1.00 7.17 O ATOM 1561 N PHE A 223 40.015 22.755 42.350 1.00 8.26 N ATOM 1562 CA PHE A 223 39.055 22.358 41.358 1.00 9.14 C ATOM 1563 C PHE A 223 37.867 23.321 41.302 1.00 10.35 C ATOM 1564 O PHE A 223 37.628 24.147 42.198 1.00 9.64 O ATOM 1565 CB PHE A 223 38.609 20.871 41.646 1.00 11.15 C ATOM 1566 CG PHE A 223 37.853 20.540 42.948 1.00 11.44 C ATOM 1567 CD1 PHE A 223 36.468 20.640 42.988 1.00 10.26 C ATOM 1568 CD2 PHE A 223 38.546 20.139 44.094 1.00 12.61 C ATOM 1569 CE1 PHE A 223 35.764 20.354 44.151 1.00 9.32 C ATOM 1570 CE2 PHE A 223 37.825 19.861 45.254 1.00 9.67 C ATOM 1571 CZ PHE A 223 36.444 19.968 45.285 1.00 9.35 C ATOM 1572 N VAL A 224 37.205 23.238 40.143 1.00 7.66 N ATOM 1573 CA VAL A 224 35.974 23.926 39.837 1.00 8.11 C ATOM 1574 C VAL A 224 34.993 22.874 39.315 1.00 8.11 C ATOM 1575 O VAL A 224 35.315 21.698 39.126 1.00 9.71 O ATOM 1576 CB VAL A 224 36.170 25.046 38.756 1.00 8.31 C ATOM 1577 CG1 VAL A 224 36.999 26.192 39.339 1.00 8.77 C ATOM 1578 CG2 VAL A 224 36.889 24.517 37.531 1.00 10.84 C ATOM 1579 N SER A 225 33.761 23.296 39.101 1.00 10.38 N ATOM 1580 CA SER A 225 32.715 22.444 38.562 1.00 12.28 C ATOM 1581 C SER A 225 33.063 21.936 37.174 1.00 14.77 C ATOM 1582 O SER A 225 33.660 22.645 36.369 1.00 12.00 O ATOM 1583 CB SER A 225 31.448 23.248 38.492 1.00 14.44 C ATOM 1584 OG SER A 225 30.392 22.488 37.935 1.00 13.00 O ATOM 1585 N ARG A 226 32.699 20.687 36.902 1.00 17.12 N ATOM 1586 CA ARG A 226 32.858 20.143 35.565 1.00 18.88 C ATOM 1587 C ARG A 226 31.826 20.845 34.693 1.00 18.19 C ATOM 1588 O ARG A 226 32.024 20.845 33.488 1.00 19.46 O ATOM 1589 CB AARG A 226 32.636 18.611 35.532 0.50 18.28 C ATOM 1590 CB BARG A 226 32.590 18.632 35.482 0.50 18.93 C ATOM 1591 CG AARG A 226 31.274 18.031 35.871 0.50 19.97 C ATOM 1592 CG BARG A 226 31.198 18.143 35.851 0.50 21.01 C ATOM 1593 CD AARG A 226 31.123 16.550 35.440 0.50 21.61 C ATOM 1594 CD BARG A 226 30.827 16.839 35.111 0.50 23.47 C ATOM 1595 NE AARG A 226 29.720 16.126 35.490 0.50 19.41 N ATOM 1596 NE BARG A 226 29.972 15.985 35.932 0.50 20.33 N ATOM 1597 CZ AARG A 226 28.822 16.412 34.535 0.50 19.53 C ATOM 1598 CZ BARG A 226 30.508 15.244 36.903 0.50 19.45 C ATOM 1599 NH1AARG A 226 29.112 17.100 33.426 0.50 18.71 N ATOM 1600 NH1BARG A 226 31.826 15.276 37.111 0.50 22.46 N ATOM 1601 NH2AARG A 226 27.558 16.055 34.720 0.50 20.95 N ATOM 1602 NH2BARG A 226 29.738 14.534 37.714 0.50 11.80 N ATOM 1603 N LEU A 227 30.761 21.462 35.235 1.00 17.41 N ATOM 1604 CA LEU A 227 29.799 22.189 34.417 1.00 18.32 C ATOM 1605 C LEU A 227 30.280 23.526 33.867 1.00 19.58 C ATOM 1606 O LEU A 227 29.765 24.026 32.857 1.00 21.27 O ATOM 1607 CB LEU A 227 28.570 22.446 35.200 1.00 19.76 C ATOM 1608 CG LEU A 227 27.946 21.156 35.747 1.00 24.84 C ATOM 1609 CD1 LEU A 227 26.872 21.537 36.753 1.00 27.60 C ATOM 1610 CD2 LEU A 227 27.428 20.276 34.617 1.00 23.53 C ATOM 1611 N GLY A 228 31.285 24.109 34.509 1.00 16.77 N ATOM 1612 CA GLY A 228 31.799 25.392 34.104 1.00 13.99 C ATOM 1613 C GLY A 228 32.636 25.950 35.224 1.00 10.47 C ATOM 1614 O GLY A 228 32.480 25.567 36.365 1.00 10.66 O ATOM 1615 N CYS A 229 33.551 26.837 34.870 1.00 10.47 N ATOM 1616 CA CYS A 229 34.368 27.501 35.845 1.00 9.12 C ATOM 1617 C CYS A 229 33.579 28.478 36.699 1.00 9.74 C ATOM 1618 O CYS A 229 33.635 28.351 37.904 1.00 11.86 O ATOM 1619 CB CYS A 229 35.461 28.201 35.116 1.00 5.24 C ATOM 1620 SG CYS A 229 36.647 27.064 34.364 1.00 9.50 S ATOM 1621 N ASN A 230 32.806 29.430 36.175 1.00 12.90 N ATOM 1622 CA ASN A 230 32.052 30.403 36.965 1.00 11.67 C ATOM 1623 C ASN A 230 30.624 29.969 37.036 1.00 13.70 C ATOM 1624 O ASN A 230 29.784 30.262 36.200 1.00 18.68 O ATOM 1625 CB ASN A 230 32.150 31.779 36.328 1.00 12.51 C ATOM 1626 CG ASN A 230 31.776 31.810 34.847 1.00 14.26 C ATOM 1627 OD1 ASN A 230 32.319 31.047 34.041 1.00 13.98 O ATOM 1628 ND2 ASN A 230 30.828 32.648 34.433 1.00 14.78 N ATOM 1629 N VAL A 231 30.309 29.176 38.027 1.00 15.22 N ATOM 1630 CA VAL A 231 28.962 28.665 38.205 1.00 17.57 C ATOM 1631 C VAL A 231 28.460 29.105 39.581 1.00 18.17 C ATOM 1632 O VAL A 231 29.160 29.026 40.604 1.00 18.32 O ATOM 1633 CB VAL A 231 29.033 27.119 38.028 1.00 18.26 C ATOM 1634 CG1 VAL A 231 27.718 26.430 38.416 1.00 19.20 C ATOM 1635 CG2 VAL A 231 29.253 26.822 36.552 1.00 18.38 C ATOM 1636 N THR A 232 27.252 29.684 39.547 1.00 19.07 N ATOM 1637 CA THR A 232 26.557 30.130 40.750 1.00 22.11 C ATOM 1638 C THR A 232 26.427 28.953 41.724 1.00 21.83 C ATOM 1639 O THR A 232 26.035 27.833 41.361 1.00 21.80 O ATOM 1640 CB THR A 232 25.152 30.674 40.380 1.00 23.60 C ATOM 1641 OG1 THR A 232 25.324 31.816 39.534 1.00 26.85 O ATOM 1642 CG2 THR A 232 24.377 31.112 41.603 1.00 26.52 C ATOM 1643 N ARG A 233 26.805 29.244 42.976 1.00 20.88 N ATOM 1644 CA ARG A 233 26.821 28.277 44.076 1.00 21.90 C ATOM 1645 C ARG A 233 27.770 27.111 43.913 1.00 19.36 C ATOM 1646 O ARG A 233 27.629 26.100 44.590 1.00 18.62 O ATOM 1647 CB ARG A 233 25.423 27.699 44.343 1.00 25.56 C ATOM 1648 CG ARG A 233 24.583 28.792 44.884 1.00 29.13 C ATOM 1649 CD ARG A 233 23.164 28.370 45.144 1.00 37.78 C ATOM 1650 NE ARG A 233 22.633 29.481 45.910 1.00 47.82 N ATOM 1651 CZ ARG A 233 22.098 30.584 45.350 1.00 53.44 C ATOM 1652 NH1 ARG A 233 21.979 30.739 44.010 1.00 54.84 N ATOM 1653 NH2 ARG A 233 21.777 31.606 46.168 1.00 56.42 N ATOM 1654 N LYS A 234 28.756 27.231 43.015 1.00 16.50 N ATOM 1655 CA LYS A 234 29.833 26.254 42.974 1.00 14.24 C ATOM 1656 C LYS A 234 31.094 27.079 43.073 1.00 12.98 C ATOM 1657 O LYS A 234 31.812 27.264 42.098 1.00 11.14 O ATOM 1658 CB LYS A 234 29.881 25.453 41.686 1.00 13.88 C ATOM 1659 CG LYS A 234 28.765 24.457 41.559 1.00 20.97 C ATOM 1660 CD LYS A 234 29.059 23.243 42.404 1.00 24.77 C ATOM 1661 CE LYS A 234 27.987 22.184 42.249 1.00 31.09 C ATOM 1662 NZ LYS A 234 26.726 22.697 42.765 1.00 35.24 N ATOM 1663 N PRO A 235 31.448 27.607 44.239 1.00 12.98 N ATOM 1664 CA PRO A 235 32.662 28.391 44.392 1.00 11.47 C ATOM 1665 C PRO A 235 33.895 27.618 44.007 1.00 10.04 C ATOM 1666 O PRO A 235 33.837 26.388 43.918 1.00 9.33 O ATOM 1667 CB PRO A 235 32.591 28.818 45.835 1.00 11.41 C ATOM 1668 CG PRO A 235 31.722 27.811 46.523 1.00 13.56 C ATOM 1669 CD PRO A 235 30.701 27.457 45.487 1.00 11.50 C ATOM 1670 N THR A 236 34.982 28.324 43.701 1.00 7.10 N ATOM 1671 CA THR A 236 36.247 27.684 43.400 1.00 7.02 C ATOM 1672 C THR A 236 36.744 27.023 44.699 1.00 8.02 C ATOM 1673 O THR A 236 36.590 27.597 45.793 1.00 7.37 O ATOM 1674 CB THR A 236 37.265 28.728 42.925 1.00 5.25 C ATOM 1675 OG1 THR A 236 36.707 29.407 41.795 1.00 8.21 O ATOM 1676 CG2 THR A 236 38.580 28.104 42.538 1.00 2.88 C ATOM 1677 N VAL A 237 37.346 25.819 44.586 1.00 6.84 N ATOM 1678 CA VAL A 237 37.793 25.077 45.766 1.00 7.14 C ATOM 1679 C VAL A 237 39.310 24.989 45.794 1.00 7.29 C ATOM 1680 O VAL A 237 39.975 24.661 44.795 1.00 7.33 O ATOM 1681 CB VAL A 237 37.184 23.639 45.789 1.00 7.85 C ATOM 1682 CG1 VAL A 237 37.542 22.927 47.128 1.00 8.17 C ATOM 1683 CG2 VAL A 237 35.682 23.721 45.640 1.00 9.59 C ATOM 1684 N PHE A 238 39.836 25.268 47.011 1.00 7.55 N ATOM 1685 CA PHE A 238 41.248 25.374 47.286 1.00 5.97 C ATOM 1686 C PHE A 238 41.704 24.385 48.358 1.00 6.46 C ATOM 1687 O PHE A 238 40.933 24.045 49.248 1.00 8.93 O ATOM 1688 CB PHE A 238 41.577 26.786 47.779 1.00 7.26 C ATOM 1689 CG PHE A 238 41.203 27.888 46.803 1.00 7.68 C ATOM 1690 CD1 PHE A 238 39.888 28.361 46.738 1.00 8.41 C ATOM 1691 CD2 PHE A 238 42.187 28.379 45.927 1.00 5.27 C ATOM 1692 CE1 PHE A 238 39.554 29.319 45.788 1.00 6.40 C ATOM 1693 CE2 PHE A 238 41.836 29.339 44.976 1.00 5.48 C ATOM 1694 CZ PHE A 238 40.528 29.801 44.914 1.00 6.98 C ATOM 1695 N THR A 239 42.930 23.878 48.300 1.00 5.52 N ATOM 1696 CA THR A 239 43.525 23.120 49.397 1.00 6.64 C ATOM 1697 C THR A 239 43.773 24.150 50.507 1.00 7.11 C ATOM 1698 O THR A 239 44.362 25.190 50.204 1.00 7.28 O ATOM 1699 CB THR A 239 44.839 22.513 48.957 1.00 5.02 C ATOM 1700 OG1 THR A 239 44.467 21.693 47.867 1.00 7.25 O ATOM 1701 CG2 THR A 239 45.551 21.690 49.984 1.00 8.52 C ATOM 1702 N ARG A 240 43.355 23.877 51.761 1.00 7.86 N ATOM 1703 CA ARG A 240 43.561 24.827 52.848 1.00 6.80 C ATOM 1704 C ARG A 240 44.978 24.704 53.338 1.00 7.30 C ATOM 1705 O ARG A 240 45.380 23.731 53.990 1.00 10.68 O ATOM 1706 CB ARG A 240 42.520 24.564 53.993 1.00 8.62 C ATOM 1707 CG ARG A 240 42.716 25.564 55.145 1.00 8.87 C ATOM 1708 CD ARG A 240 41.536 25.653 56.067 1.00 8.61 C ATOM 1709 NE ARG A 240 41.221 24.374 56.687 1.00 11.56 N ATOM 1710 CZ ARG A 240 41.903 23.795 57.693 1.00 9.55 C ATOM 1711 NH1 ARG A 240 42.978 24.334 58.250 1.00 8.42 N ATOM 1712 NH2 ARG A 240 41.432 22.638 58.178 1.00 8.69 N ATOM 1713 N VAL A 241 45.804 25.730 53.047 1.00 6.78 N ATOM 1714 CA VAL A 241 47.224 25.673 53.358 1.00 7.67 C ATOM 1715 C VAL A 241 47.477 25.524 54.872 1.00 7.96 C ATOM 1716 O VAL A 241 48.393 24.794 55.248 1.00 7.52 O ATOM 1717 CB VAL A 241 47.932 26.945 52.800 1.00 8.15 C ATOM 1718 CG1 VAL A 241 49.359 27.081 53.289 1.00 5.92 C ATOM 1719 CG2 VAL A 241 47.919 26.850 51.265 1.00 6.16 C ATOM 1720 N SER A 242 46.633 26.129 55.732 1.00 6.90 N ATOM 1721 CA SER A 242 46.862 26.061 57.180 1.00 9.87 C ATOM 1722 C SER A 242 46.687 24.647 57.739 1.00 11.50 C ATOM 1723 O SER A 242 47.135 24.390 58.850 1.00 10.55 O ATOM 1724 CB SER A 242 45.909 27.017 57.926 1.00 6.38 C ATOM 1725 OG SER A 242 44.558 26.626 57.971 1.00 7.15 O ATOM 1726 N ALA A 243 46.080 23.711 56.973 1.00 11.57 N ATOM 1727 CA ALA A 243 45.964 22.335 57.399 1.00 11.12 C ATOM 1728 C ALA A 243 47.248 21.578 57.116 1.00 11.17 C ATOM 1729 O ALA A 243 47.410 20.456 57.591 1.00 13.38 O ATOM 1730 CB ALA A 243 44.809 21.659 56.669 1.00 8.87 C ATOM 1731 N TYR A 244 48.231 22.171 56.442 1.00 8.71 N ATOM 1732 CA TYR A 244 49.429 21.466 56.001 1.00 9.59 C ATOM 1733 C TYR A 244 50.741 22.034 56.457 1.00 9.55 C ATOM 1734 O TYR A 244 51.796 21.637 55.969 1.00 10.53 O ATOM 1735 CB TYR A 244 49.437 21.389 54.445 1.00 9.85 C ATOM 1736 CG TYR A 244 48.266 20.543 53.912 1.00 11.66 C ATOM 1737 CD1 TYR A 244 48.373 19.146 53.905 1.00 11.24 C ATOM 1738 CD2 TYR A 244 47.065 21.160 53.517 1.00 8.56 C ATOM 1739 CE1 TYR A 244 47.283 18.375 53.511 1.00 9.19 C ATOM 1740 CE2 TYR A 244 45.975 20.388 53.133 1.00 6.79 C ATOM 1741 CZ TYR A 244 46.101 19.005 53.137 1.00 8.12 C ATOM 1742 OH TYR A 244 45.004 18.234 52.809 1.00 10.18 O ATOM 1743 N ILE A 245 50.728 22.928 57.441 1.00 11.15 N ATOM 1744 CA ILE A 245 51.951 23.617 57.834 1.00 11.13 C ATOM 1745 C ILE A 245 53.013 22.684 58.391 1.00 10.97 C ATOM 1746 O ILE A 245 54.177 22.828 58.026 1.00 11.37 O ATOM 1747 CB ILE A 245 51.557 24.735 58.842 1.00 9.25 C ATOM 1748 CG1 ILE A 245 50.595 25.722 58.155 1.00 10.37 C ATOM 1749 CG2 ILE A 245 52.831 25.389 59.412 1.00 10.03 C ATOM 1750 CD1 ILE A 245 51.125 26.399 56.881 1.00 11.86 C ATOM 1751 N SER A 246 52.652 21.695 59.223 1.00 12.45 N ATOM 1752 CA SER A 246 53.628 20.737 59.730 1.00 11.85 C ATOM 1753 C SER A 246 54.232 19.877 58.649 1.00 11.14 C ATOM 1754 O SER A 246 55.438 19.646 58.683 1.00 13.26 O ATOM 1755 CB SER A 246 52.986 19.821 60.742 1.00 17.42 C ATOM 1756 OG SER A 246 52.876 20.618 61.884 1.00 25.47 O ATOM 1757 N TRP A 247 53.436 19.436 57.656 1.00 11.38 N ATOM 1758 CA TRP A 247 53.987 18.615 56.574 1.00 10.46 C ATOM 1759 C TRP A 247 54.981 19.446 55.762 1.00 12.43 C ATOM 1760 O TRP A 247 56.126 19.023 55.545 1.00 10.24 O ATOM 1761 CB TRP A 247 52.812 18.090 55.707 1.00 10.33 C ATOM 1762 CG TRP A 247 53.261 17.313 54.467 1.00 14.12 C ATOM 1763 CD1 TRP A 247 53.714 16.023 54.550 1.00 15.22 C ATOM 1764 CD2 TRP A 247 53.360 17.829 53.179 1.00 14.99 C ATOM 1765 NE1 TRP A 247 54.129 15.729 53.320 1.00 15.11 N ATOM 1766 CE2 TRP A 247 53.946 16.760 52.474 1.00 14.91 C ATOM 1767 CE3 TRP A 247 53.042 19.022 52.516 1.00 15.78 C ATOM 1768 CZ2 TRP A 247 54.234 16.862 51.111 1.00 13.51 C ATOM 1769 CZ3 TRP A 247 53.332 19.115 51.144 1.00 16.23 C ATOM 1770 CH2 TRP A 247 53.922 18.049 50.455 1.00 16.23 C ATOM 1771 N ILE A 248 54.572 20.698 55.405 1.00 13.24 N ATOM 1772 CA ILE A 248 55.437 21.603 54.640 1.00 13.46 C ATOM 1773 C ILE A 248 56.740 21.840 55.356 1.00 13.85 C ATOM 1774 O ILE A 248 57.794 21.685 54.756 1.00 15.18 O ATOM 1775 CB ILE A 248 54.751 22.959 54.394 1.00 11.46 C ATOM 1776 CG1 ILE A 248 53.573 22.727 53.471 1.00 10.52 C ATOM 1777 CG2 ILE A 248 55.735 23.964 53.791 1.00 13.13 C ATOM 1778 CD1 ILE A 248 52.650 23.931 53.358 1.00 13.12 C ATOM 1779 N ASN A 249 56.708 22.167 56.643 1.00 15.66 N ATOM 1780 CA ASN A 249 57.966 22.361 57.335 1.00 18.53 C ATOM 1781 C ASN A 249 58.814 21.119 57.539 1.00 16.43 C ATOM 1782 O ASN A 249 60.031 21.260 57.491 1.00 17.80 O ATOM 1783 CB ASN A 249 57.724 23.020 58.681 1.00 21.46 C ATOM 1784 CG ASN A 249 57.244 24.449 58.519 1.00 22.86 C ATOM 1785 OD1 ASN A 249 56.449 24.895 59.330 1.00 29.97 O ATOM 1786 ND2 ASN A 249 57.638 25.244 57.531 1.00 26.91 N ATOM 1787 N ASN A 250 58.213 19.930 57.696 1.00 16.83 N ATOM 1788 CA ASN A 250 58.941 18.651 57.807 1.00 16.47 C ATOM 1789 C ASN A 250 59.611 18.253 56.486 1.00 16.56 C ATOM 1790 O ASN A 250 60.651 17.609 56.494 1.00 16.74 O ATOM 1791 CB ASN A 250 57.970 17.526 58.243 1.00 13.56 C ATOM 1792 CG ASN A 250 57.466 17.622 59.681 1.00 15.43 C ATOM 1793 OD1 ASN A 250 56.398 17.164 60.074 1.00 18.41 O ATOM 1794 ND2 ASN A 250 58.233 18.199 60.557 1.00 14.31 N ATOM 1795 N VAL A 251 59.059 18.618 55.314 1.00 17.64 N ATOM 1796 CA VAL A 251 59.696 18.335 54.019 1.00 16.18 C ATOM 1797 C VAL A 251 60.857 19.283 53.790 1.00 17.67 C ATOM 1798 O VAL A 251 61.933 18.839 53.397 1.00 18.03 O ATOM 1799 CB VAL A 251 58.690 18.486 52.860 1.00 15.59 C ATOM 1800 CG1 VAL A 251 59.319 18.240 51.489 1.00 12.59 C ATOM 1801 CG2 VAL A 251 57.588 17.488 53.087 1.00 13.13 C ATOM 1802 N ILE A 252 60.702 20.573 54.053 1.00 19.04 N ATOM 1803 CA ILE A 252 61.769 21.530 53.775 1.00 25.61 C ATOM 1804 C ILE A 252 63.003 21.300 54.650 1.00 29.58 C ATOM 1805 O ILE A 252 64.137 21.321 54.168 1.00 31.98 O ATOM 1806 CB ILE A 252 61.160 22.946 53.947 1.00 25.94 C ATOM 1807 CG1 ILE A 252 60.223 23.219 52.786 1.00 26.02 C ATOM 1808 CG2 ILE A 252 62.248 24.007 53.990 1.00 28.18 C ATOM 1809 CD1 ILE A 252 59.431 24.496 53.108 1.00 31.12 C ATOM 1810 N ALA A 253 62.773 21.069 55.941 1.00 33.64 N ATOM 1811 CA ALA A 253 63.826 20.729 56.888 1.00 39.90 C ATOM 1812 C ALA A 253 64.486 19.356 56.643 1.00 44.78 C ATOM 1813 O ALA A 253 65.631 19.154 57.073 1.00 46.42 O ATOM 1814 CB ALA A 253 63.273 20.715 58.302 1.00 37.88 C ATOM 1815 N SER A 254 63.845 18.359 55.999 1.00 48.99 N ATOM 1816 CA SER A 254 64.540 17.101 55.772 1.00 52.68 C ATOM 1817 C SER A 254 65.070 16.922 54.351 1.00 55.19 C ATOM 1818 O SER A 254 65.847 15.987 54.133 1.00 56.64 O ATOM 1819 CB SER A 254 63.621 15.919 56.142 1.00 53.68 C ATOM 1820 OG SER A 254 62.413 15.811 55.394 1.00 55.52 O ATOM 1821 N ASN A 255 64.721 17.786 53.381 1.00 57.18 N ATOM 1822 CA ASN A 255 65.204 17.656 52.004 1.00 59.60 C ATOM 1823 C ASN A 255 66.166 18.765 51.639 1.00 60.68 C ATOM 1824 O ASN A 255 65.878 19.922 51.956 1.00 63.35 O ATOM 1825 CB ASN A 255 64.083 17.715 50.981 1.00 60.00 C ATOM 1826 CG ASN A 255 63.104 16.556 51.026 1.00 60.85 C ATOM 1827 OD1 ASN A 255 63.035 15.771 50.087 1.00 61.78 O ATOM 1828 ND2 ASN A 255 62.301 16.382 52.075 1.00 60.59 N ATOM 1829 OXT ASN A 255 67.187 18.458 51.029 1.00 62.36 O TER 1830 ASN A 255 HETATM 1831 CA CA A 280 57.314 37.378 30.072 1.00 20.84 CA HETATM 1832 S SO4 A 290 43.528 21.842 61.312 1.00 42.65 S HETATM 1833 O1 SO4 A 290 43.862 22.938 60.486 1.00 41.10 O HETATM 1834 O2 SO4 A 290 44.637 20.950 61.397 1.00 43.95 O HETATM 1835 O3 SO4 A 290 42.382 21.153 60.795 1.00 41.19 O HETATM 1836 O4 SO4 A 290 43.258 22.304 62.628 1.00 44.27 O HETATM 1837 C1 0QH A 256 41.149 23.354 37.644 1.00 31.55 C HETATM 1838 C2 0QH A 256 41.347 24.616 38.562 1.00 29.79 C HETATM 1839 O 0QH A 256 40.738 23.466 36.483 1.00 31.48 O HETATM 1840 F1 0QH A 256 41.871 24.392 39.754 1.00 30.45 F HETATM 1841 F2 0QH A 256 42.130 25.537 38.058 1.00 27.87 F HETATM 1842 F3 0QH A 256 40.210 25.231 38.787 1.00 30.74 F HETATM 1843 N 0QH A 256 41.428 22.136 38.149 1.00 32.72 N HETATM 1844 CA 0QH A 256 40.800 20.919 37.702 1.00 35.06 C HETATM 1845 C 0QH A 256 39.307 21.048 37.435 1.00 37.47 C HETATM 1846 O1 0QH A 256 38.514 21.565 38.211 1.00 36.15 O HETATM 1847 CB 0QH A 256 41.100 19.869 38.747 1.00 34.44 C HETATM 1848 CG 0QH A 256 41.280 18.443 38.288 1.00 36.76 C HETATM 1849 CD1 0QH A 256 42.225 18.333 37.087 1.00 36.80 C HETATM 1850 CD2 0QH A 256 41.811 17.676 39.479 1.00 38.25 C HETATM 1851 N1 0QH A 256 37.773 20.686 35.406 1.00 44.05 N HETATM 1852 N2 0QH A 256 39.121 20.568 36.190 1.00 41.52 N HETATM 1853 C3 0QH A 256 37.712 22.117 34.940 1.00 46.64 C HETATM 1854 C11 0QH A 256 36.522 22.554 34.080 1.00 51.49 C HETATM 1855 C21 0QH A 256 35.753 23.641 34.490 1.00 50.39 C HETATM 1856 C31 0QH A 256 34.724 24.077 33.677 1.00 52.00 C HETATM 1857 C4 0QH A 256 34.426 23.461 32.459 1.00 53.48 C HETATM 1858 C5 0QH A 256 35.179 22.373 32.039 1.00 54.08 C HETATM 1859 C6 0QH A 256 36.225 21.923 32.850 1.00 54.40 C HETATM 1860 C1M 0QH A 256 38.160 19.713 34.316 1.00 46.35 C HETATM 1861 CA2 0QH A 256 36.531 20.238 36.106 1.00 42.79 C HETATM 1862 CA1 0QH A 256 36.544 18.892 36.812 1.00 41.97 C HETATM 1863 O2 0QH A 256 36.668 17.792 36.251 1.00 40.89 O HETATM 1864 C12 0QH A 256 36.195 18.351 39.070 1.00 41.34 C HETATM 1865 N11 0QH A 256 36.432 19.241 38.103 1.00 41.27 N HETATM 1866 C22 0QH A 256 36.820 17.094 39.138 1.00 41.18 C HETATM 1867 C32 0QH A 256 36.529 16.229 40.207 1.00 42.70 C HETATM 1868 C41 0QH A 256 35.613 16.613 41.216 1.00 40.91 C HETATM 1869 C51 0QH A 256 35.007 17.872 41.125 1.00 42.28 C HETATM 1870 C61 0QH A 256 35.290 18.723 40.059 1.00 41.35 C HETATM 1871 C1' 0QH A 256 35.273 15.697 42.414 1.00 38.52 C HETATM 1872 C2' 0QH A 256 35.742 14.242 42.251 1.00 36.76 C HETATM 1873 C3' 0QH A 256 33.777 15.691 42.501 1.00 38.27 C HETATM 1874 O HOH A 301 32.882 26.020 39.606 1.00 17.65 O HETATM 1875 O HOH A 302 32.442 29.522 40.356 1.00 21.49 O HETATM 1876 O HOH A 303 31.364 32.109 40.271 1.00 14.39 O HETATM 1877 O HOH A 304 34.013 31.083 41.939 1.00 14.29 O HETATM 1878 O HOH A 305 35.685 27.451 53.086 1.00 14.08 O HETATM 1879 O HOH A 306 35.231 24.442 53.127 1.00 28.89 O HETATM 1880 O HOH A 307 35.490 31.094 55.192 1.00 19.23 O HETATM 1881 O HOH A 308 39.761 29.106 55.841 1.00 14.63 O HETATM 1882 O HOH A 309 53.144 39.621 37.336 1.00 26.14 O HETATM 1883 O HOH A 310 57.464 42.102 35.337 1.00 30.84 O HETATM 1884 O HOH A 311 56.295 39.174 39.811 1.00 21.08 O HETATM 1885 O HOH A 312 45.452 30.812 42.008 1.00 6.92 O HETATM 1886 O HOH A 313 47.449 30.520 39.380 1.00 6.92 O HETATM 1887 O HOH A 314 48.283 30.372 36.744 1.00 10.12 O HETATM 1888 O HOH A 315 50.127 28.060 45.624 1.00 9.45 O HETATM 1889 O HOH A 316 42.549 29.375 56.136 1.00 12.87 O HETATM 1890 O HOH A 317 45.102 28.273 54.960 1.00 9.55 O HETATM 1891 O HOH A 318 41.167 18.810 46.507 1.00 11.18 O HETATM 1892 O HOH A 319 42.862 19.540 48.578 1.00 9.49 O HETATM 1893 O HOH A 320 42.969 19.206 51.337 1.00 13.03 O HETATM 1894 O HOH A 321 57.440 35.699 40.935 1.00 14.74 O HETATM 1895 O HOH A 322 55.936 34.579 38.033 1.00 23.30 O HETATM 1896 O HOH A 323 52.785 39.989 40.333 1.00 25.89 O HETATM 1897 O HOH A 324 33.689 36.733 43.984 1.00 22.09 O HETATM 1898 O HOH A 325 32.752 34.434 42.638 1.00 19.00 O HETATM 1899 O HOH A 326 61.296 18.059 35.669 1.00 30.78 O HETATM 1900 O HOH A 327 60.418 37.615 50.653 1.00 26.97 O HETATM 1901 O HOH A 328 52.092 36.358 50.688 1.00 17.16 O HETATM 1902 O HOH A 329 32.883 31.561 31.264 1.00 23.33 O HETATM 1903 O HOH A 330 43.307 12.818 47.113 1.00 10.74 O HETATM 1904 O HOH A 331 36.720 37.088 32.045 1.00 23.95 O HETATM 1905 O HOH A 332 43.583 34.271 34.093 1.00 8.71 O HETATM 1906 O HOH A 333 64.151 38.662 38.603 1.00 17.67 O HETATM 1907 O HOH A 334 52.858 37.863 46.914 1.00 23.65 O HETATM 1908 O HOH A 335 50.321 18.976 58.535 1.00 26.76 O HETATM 1909 O HOH A 336 40.093 37.345 33.628 1.00 25.03 O HETATM 1910 O HOH A 337 32.158 36.439 33.842 1.00 28.27 O HETATM 1911 O HOH A 338 54.965 37.964 49.272 1.00 44.50 O HETATM 1912 O HOH A 339 48.863 37.454 57.934 1.00 30.43 O HETATM 1913 O HOH A 340 41.448 24.662 62.587 1.00 24.01 O HETATM 1914 O HOH A 341 61.601 23.704 58.048 1.00 33.41 O HETATM 1915 O HOH A 342 66.904 32.764 34.214 1.00 30.56 O HETATM 1916 O HOH A 343 49.238 33.132 26.847 1.00 35.15 O HETATM 1917 O HOH A 344 47.105 44.440 40.996 1.00 20.82 O HETATM 1918 O HOH A 345 47.069 22.275 61.044 1.00 31.32 O HETATM 1919 O HOH A 346 34.646 30.080 59.205 1.00 27.77 O HETATM 1920 O HOH A 347 43.223 10.806 49.056 1.00 30.40 O HETATM 1921 O HOH A 348 67.980 25.297 36.489 1.00 28.90 O HETATM 1922 O HOH A 349 68.279 36.872 47.286 1.00 33.84 O HETATM 1923 O HOH A 350 52.212 27.533 62.384 1.00 28.11 O HETATM 1924 O HOH A 351 57.507 31.607 53.559 1.00 40.44 O HETATM 1925 O HOH A 352 50.195 37.258 48.866 1.00 31.37 O HETATM 1926 O HOH A 353 64.855 31.038 51.212 1.00 39.73 O HETATM 1927 O HOH A 354 48.078 43.679 46.695 1.00 44.90 O HETATM 1928 O HOH A 355 58.415 35.335 29.066 1.00 27.17 O HETATM 1929 O HOH A 356 45.710 38.988 29.308 1.00 38.47 O HETATM 1930 O HOH A 357 51.043 14.003 41.579 1.00 21.25 O HETATM 1931 O HOH A 358 67.908 23.479 45.499 1.00 32.89 O HETATM 1932 O HOH A 359 61.233 13.914 42.154 1.00 33.27 O HETATM 1933 O HOH A 360 36.842 25.273 30.915 1.00 13.93 O HETATM 1934 O HOH A 361 56.471 41.206 37.704 1.00 27.85 O HETATM 1935 O HOH A 362 44.959 29.044 25.226 1.00 33.57 O HETATM 1936 O HOH A 363 38.998 33.020 26.805 1.00 20.64 O HETATM 1937 O HOH A 364 64.429 26.904 30.756 1.00 27.82 O HETATM 1938 O HOH A 365 49.235 16.475 56.392 1.00 29.93 O HETATM 1939 O HOH A 366 44.125 17.192 55.905 1.00 39.61 O HETATM 1940 O HOH A 367 49.797 21.805 60.380 1.00 27.84 O HETATM 1941 O HOH A 368 50.024 19.785 34.563 1.00 30.97 O HETATM 1942 O HOH A 369 46.429 32.844 24.842 1.00 41.62 O HETATM 1943 O HOH A 370 47.931 33.256 60.045 1.00 28.11 O HETATM 1944 O HOH A 371 41.806 45.255 34.043 1.00 30.30 O HETATM 1945 O HOH A 372 63.874 21.873 33.271 1.00 41.07 O HETATM 1946 O HOH A 373 56.782 32.378 30.107 1.00 26.11 O HETATM 1947 O HOH A 374 47.243 34.732 57.808 1.00 23.62 O HETATM 1948 O HOH A 375 37.066 28.697 55.048 1.00 34.12 O HETATM 1949 O HOH A 376 37.249 25.085 56.044 1.00 40.37 O HETATM 1950 O HOH A 377 28.275 17.000 45.695 1.00 37.97 O HETATM 1951 O HOH A 378 42.408 40.137 59.903 1.00 44.03 O HETATM 1952 O HOH A 379 49.251 46.251 34.415 1.00 43.84 O HETATM 1953 O HOH A 380 54.093 37.592 39.323 1.00 34.41 O HETATM 1954 O HOH A 381 48.187 22.582 30.415 1.00 39.01 O HETATM 1955 O HOH A 382 51.483 31.033 26.492 1.00 51.83 O HETATM 1956 O HOH A 383 56.607 12.499 46.037 1.00 23.19 O HETATM 1957 O HOH A 384 55.626 11.776 48.780 1.00 40.69 O HETATM 1958 O HOH A 385 52.534 35.789 59.363 1.00 38.05 O HETATM 1959 O HOH A 386 35.031 27.253 57.241 1.00 29.30 O HETATM 1960 O HOH A 387 32.125 31.879 59.654 1.00 34.45 O HETATM 1961 O HOH A 388 28.198 29.575 58.752 1.00 42.72 O HETATM 1962 O HOH A 389 45.086 35.683 25.607 1.00 31.08 O HETATM 1963 O HOH A 390 32.348 34.623 31.387 1.00 31.83 O HETATM 1964 O HOH A 391 38.765 35.716 59.975 1.00 31.57 O HETATM 1965 O HOH A 392 44.103 41.461 30.834 1.00 49.81 O HETATM 1966 O HOH A 393 41.972 15.911 53.072 1.00 32.93 O HETATM 1967 O HOH A 394 28.002 18.208 53.733 1.00 35.56 O HETATM 1968 O HOH A 395 44.375 23.297 35.373 1.00 22.03 O HETATM 1969 O HOH A 396 30.702 31.211 29.539 1.00 51.18 O HETATM 1970 O HOH A 397 30.494 28.541 32.709 1.00 49.36 O HETATM 1971 O HOH A 398 56.412 21.054 62.131 1.00 43.25 O HETATM 1972 O HOH A 399 44.542 44.447 44.699 1.00 48.81 O HETATM 1973 O HOH A 400 31.898 26.937 58.945 1.00 37.09 O HETATM 1974 O HOH A 401 37.218 41.186 40.473 1.00 38.21 O HETATM 1975 O HOH A 402 26.032 29.330 36.708 1.00 41.30 O HETATM 1976 O HOH A 403 26.133 32.573 45.021 1.00 40.73 O HETATM 1977 O HOH A 404 55.838 42.729 28.694 1.00 41.47 O HETATM 1978 O HOH A 405 42.852 35.753 27.210 1.00 41.44 O HETATM 1979 O HOH A 406 52.225 44.186 55.156 1.00 45.19 O HETATM 1980 O HOH A 407 41.877 18.854 58.058 1.00 45.51 O HETATM 1981 O HOH A 408 26.732 21.589 55.886 1.00 47.70 O HETATM 1982 O HOH A 409 32.690 16.791 53.773 1.00 39.34 O HETATM 1983 O HOH A 410 58.623 17.123 24.197 1.00 44.44 O HETATM 1984 O HOH A 411 65.260 20.092 24.330 1.00 37.78 O HETATM 1985 O HOH A 412 45.751 7.536 49.944 1.00 45.48 O HETATM 1986 O HOH A 413 57.867 17.562 29.038 1.00 39.83 O HETATM 1987 O HOH A 414 28.283 22.782 30.998 1.00 43.50 O HETATM 1988 O HOH A 415 67.326 26.052 33.737 1.00 65.89 O HETATM 1989 O HOH A 416 58.019 14.849 36.117 1.00 20.44 O HETATM 1990 O HOH A 417 51.753 33.322 44.908 1.00 39.55 O HETATM 1991 O HOH A 418 56.671 43.846 45.568 1.00 48.93 O HETATM 1992 O HOH A 419 39.120 23.034 61.598 1.00 42.00 O HETATM 1993 O HOH A 420 41.306 15.026 56.005 1.00 47.08 O HETATM 1994 O HOH A 421 26.653 15.602 48.462 1.00 44.38 O HETATM 1995 O HOH A 422 25.367 17.571 33.210 1.00 40.94 O HETATM 1996 O HOH A 423 42.962 20.877 34.581 1.00 39.92 O HETATM 1997 O HOH A 424 63.325 17.648 23.374 1.00 51.93 O HETATM 1998 O HOH A 425 51.125 42.005 52.466 1.00 33.24 O HETATM 1999 O HOH A 426 44.781 6.738 38.029 1.00 35.75 O HETATM 2000 O HOH A 427 40.801 45.034 42.972 1.00 37.80 O HETATM 2001 O HOH A 428 41.185 41.488 32.038 1.00 41.78 O HETATM 2002 O HOH A 429 50.800 44.806 30.573 1.00 46.30 O HETATM 2003 O HOH A 430 57.885 37.456 52.108 1.00 38.46 O HETATM 2004 O HOH A 431 22.145 21.543 53.132 1.00 41.38 O HETATM 2005 O HOH A 432 41.352 34.096 61.758 1.00 45.89 O HETATM 2006 O HOH A 433 48.397 9.654 43.158 1.00 40.50 O HETATM 2007 O HOH A 434 42.265 45.255 31.328 1.00 40.72 O CONECT 231 352 CONECT 352 231 CONECT 457 1831 CONECT 458 1831 CONECT 472 1831 CONECT 496 1831 CONECT 516 1831 CONECT 537 1831 CONECT 980 1466 CONECT 1223 1341 CONECT 1341 1223 CONECT 1400 1620 CONECT 1466 980 CONECT 1620 1400 CONECT 1831 457 458 472 496 CONECT 1831 516 537 1928 CONECT 1832 1833 1834 1835 1836 CONECT 1833 1832 CONECT 1834 1832 CONECT 1835 1832 CONECT 1836 1832 CONECT 1837 1838 1839 1843 CONECT 1838 1837 1840 1841 1842 CONECT 1839 1837 CONECT 1840 1838 CONECT 1841 1838 CONECT 1842 1838 CONECT 1843 1837 1844 CONECT 1844 1843 1845 1847 CONECT 1845 1844 1846 1852 CONECT 1846 1845 CONECT 1847 1844 1848 CONECT 1848 1847 1849 1850 CONECT 1849 1848 CONECT 1850 1848 CONECT 1851 1852 1853 1860 1861 CONECT 1852 1845 1851 CONECT 1853 1851 1854 CONECT 1854 1853 1855 1859 CONECT 1855 1854 1856 CONECT 1856 1855 1857 CONECT 1857 1856 1858 CONECT 1858 1857 1859 CONECT 1859 1854 1858 CONECT 1860 1851 CONECT 1861 1851 1862 CONECT 1862 1861 1863 1865 CONECT 1863 1862 CONECT 1864 1865 1866 1870 CONECT 1865 1862 1864 CONECT 1866 1864 1867 CONECT 1867 1866 1868 CONECT 1868 1867 1869 1871 CONECT 1869 1868 1870 CONECT 1870 1864 1869 CONECT 1871 1868 1872 1873 CONECT 1872 1871 CONECT 1873 1871 CONECT 1928 1831 MASTER 392 0 3 2 17 0 10 6 1999 1 59 19 END