HEADER TRANSCRIPTION 08-FEB-05 2BJW TITLE PSPF AAA DOMAIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: PSP OPERON TRANSCRIPTIONAL ACTIVATOR; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: AAA DOMAIN, RESIDUES 1-265; COMPND 5 SYNONYM: PSPF, PHAGE SHOCK PROTEIN F; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI; SOURCE 3 ORGANISM_TAXID: 83333; SOURCE 4 STRAIN: K12; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: B834; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET28B PLUS KEYWDS TRANSCRIPTION, AAA, TRANSCRIPTION ACTIVATION, GENE KEYWDS 2 REGULATION, SIGMA54 ACTIVATOR, ENHANCER BINDING PROTEIN, KEYWDS 3 PSPF, ATP-BINDING, DNA- BINDING, TRANSCRIPTION REGULATION, EXPDTA X-RAY DIFFRACTION AUTHOR M.RAPPAS,J.SCHUMACHER,F.BEURON,H.NIWA,P.BORDES, AUTHOR 2 S.WIGNESHWERARAJ,C.A.KEETCH,C.V.ROBINSON,M.BUCK,X.ZHANG REVDAT 2 24-FEB-09 2BJW 1 VERSN REVDAT 1 31-MAR-05 2BJW 0 JRNL AUTH M.RAPPAS,J.SCHUMACHER,F.BEURON,H.NIWA,P.BORDES, JRNL AUTH 2 S.WIGNESHWERARAJ,C.A.KEETCH,C.V.ROBINSON,M.BUCK, JRNL AUTH 3 X.ZHANG JRNL TITL STRUCTURAL INSIGHTS INTO THE ACTIVITY OF JRNL TITL 2 ENHANCER-BINDING PROTEINS JRNL REF SCIENCE V. 307 1972 2005 JRNL REFN ISSN 0036-8075 JRNL PMID 15790859 JRNL DOI 10.1126/SCIENCE.1105932 REMARK 2 REMARK 2 RESOLUTION. 1.75 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 1.1 REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE- REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU, REMARK 3 : READ,RICE,SIMONSON,WARREN REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 100.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.0 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 10000000 REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.5 REMARK 3 NUMBER OF REFLECTIONS : 26860 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING SET) : 0.18041 REMARK 3 FREE R VALUE : 0.20785 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0 REMARK 3 FREE R VALUE TEST SET COUNT : 1410 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 : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.750 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.796 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 80.4 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1614 REMARK 3 BIN R VALUE (WORKING SET) : 0.244 REMARK 3 BIN FREE R VALUE : 0.345 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 BIN FREE R VALUE TEST SET COUNT : 95 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 : 1917 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 196 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.028 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.57 REMARK 3 B22 (A**2) : -0.57 REMARK 3 B33 (A**2) : 0.85 REMARK 3 B12 (A**2) : -0.28 REMARK 3 B13 (A**2) : 0.00 REMARK 3 B23 (A**2) : 0.00 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) : 0.022 REMARK 3 BOND ANGLES (DEGREES) : 1.696 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 5.37 REMARK 3 IMPROPER ANGLES (DEGREES) : NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : 1.38 ; 1.5 REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.443 ; 2.00 REMARK 3 SIDE-CHAIN BOND (A**2) : 3.54 ; 3 REMARK 3 SIDE-CHAIN ANGLE (A**2) : 5.855 ; 4.5 REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED : BABINET MODEL WITH MASK REMARK 3 KSOL : NULL REMARK 3 BSOL : 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 : PROTEIN_REP.PARAM REMARK 3 PARAMETER FILE 2 : NULL REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP REMARK 3 TOPOLOGY FILE 2 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE REMARK 3 RIDING POSITIONS. DISORDERED REGIONS WERE MODELED AS ALANINES. REMARK 4 REMARK 4 2BJW COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-FEB-05. REMARK 100 THE PDBE ID CODE IS EBI-22890. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 16-JUL-04 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 8.00 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SRS REMARK 200 BEAMLINE : PX14.1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.488 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : MIRRORS REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28281 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 95.5 REMARK 200 DATA REDUNDANCY : 5.400 REMARK 200 R MERGE (I) : 0.05000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 33.7000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.81 REMARK 200 COMPLETENESS FOR SHELL (%) : 80.4 REMARK 200 DATA REDUNDANCY IN SHELL : 3.70 REMARK 200 R MERGE FOR SHELL (I) : 0.45000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 3.200 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: PDB ENTRY 2BJV REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 43 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 2.0 M AMMONIUM FORMATE, 0.1 M REMARK 280 HEPES PH 8.0, 10% MPD REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z+2/3 REMARK 290 3555 -X+Y,-X,Z+1/3 REMARK 290 4555 -X,-Y,Z+1/2 REMARK 290 5555 Y,-X+Y,Z+1/6 REMARK 290 6555 X-Y,X,Z+5/6 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 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 26.18467 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 13.09233 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 19.63850 REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 6.54617 REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 32.73083 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 GENERATING THE BIOMOLECULE REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PQS REMARK 350 APPLY THE FOLLOWING TO CHAINS: A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 MET A 1 REMARK 465 ALA A 2 REMARK 465 GLU A 3 REMARK 465 TYR A 4 REMARK 465 LYS A 5 REMARK 465 ASP A 6 REMARK 465 ASN A 7 REMARK 465 LEU A 8 REMARK 465 ALA A 82 REMARK 465 GLY A 83 REMARK 465 ALA A 84 REMARK 465 PHE A 85 REMARK 465 THR A 86 REMARK 465 GLY A 87 REMARK 465 ALA A 88 REMARK 465 GLN A 89 REMARK 465 PRO A 260 REMARK 465 GLU A 261 REMARK 465 ASP A 262 REMARK 465 ALA A 263 REMARK 465 ILE A 264 REMARK 465 ALA A 265 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 LEU A 72 CG CD1 CD2 REMARK 470 LYS A 90 CG CD CE NZ REMARK 470 ARG A 122 CG CD NE CZ NH1 NH2 REMARK 470 ARG A 257 CG CD NE CZ NH1 NH2 REMARK 470 ARG A 258 CG CD NE CZ NH1 NH2 REMARK 470 PRO A 259 CA C O CB CG CD REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 OE1 GLU A 97 - O HOH A 2069 2.18 REMARK 500 OD1 ASP A 172 - O HOH A 2113 2.03 REMARK 500 OE1 GLU A 215 - O HOH A 2155 2.16 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 REMARK 500 O ASP A 167 OD1 ASN A 231 5555 2.01 REMARK 500 OD1 ASN A 231 O ASP A 167 6554 2.01 REMARK 500 REMARK 500 REMARK: NULL 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 MET A 187 CG MET A 187 SD -0.157 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 ARG A 38 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES REMARK 500 ARG A 55 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES REMARK 500 ASP A 107 CB - CG - OD1 ANGL. DEV. = 6.1 DEGREES REMARK 500 ARG A 143 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES REMARK 500 ARG A 143 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES REMARK 500 ASP A 164 CB - CG - OD1 ANGL. DEV. = 5.4 DEGREES REMARK 500 ASP A 172 CB - CG - OD2 ANGL. DEV. = 6.3 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 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ASN A 225 -131.82 50.11 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 2BJV RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF PSPF(1-275) R168A REMARK 900 MUTANT DBREF 2BJW A 1 265 UNP P37344 PSPF_ECOLI 1 265 SEQRES 1 A 265 MET ALA GLU TYR LYS ASP ASN LEU LEU GLY GLU ALA ASN SEQRES 2 A 265 SER PHE LEU GLU VAL LEU GLU GLN VAL SER HIS LEU ALA SEQRES 3 A 265 PRO LEU ASP LYS PRO VAL LEU ILE ILE GLY GLU ARG GLY SEQRES 4 A 265 THR GLY LYS GLU LEU ILE ALA SER ARG LEU HIS TYR LEU SEQRES 5 A 265 SER SER ARG TRP GLN GLY PRO PHE ILE SER LEU ASN CYS SEQRES 6 A 265 ALA ALA LEU ASN GLU ASN LEU LEU ASP SER GLU LEU PHE SEQRES 7 A 265 GLY HIS GLU ALA GLY ALA PHE THR GLY ALA GLN LYS ARG SEQRES 8 A 265 HIS PRO GLY ARG PHE GLU ARG ALA ASP GLY GLY THR LEU SEQRES 9 A 265 PHE LEU ASP GLU LEU ALA THR ALA PRO MET MET VAL GLN SEQRES 10 A 265 GLU LYS LEU LEU ARG VAL ILE GLU TYR GLY GLU LEU GLU SEQRES 11 A 265 ARG VAL GLY GLY SER GLN PRO LEU GLN VAL ASN VAL ARG SEQRES 12 A 265 LEU VAL CYS ALA THR ASN ALA ASP LEU PRO ALA MET VAL SEQRES 13 A 265 ASN GLU GLY THR PHE ARG ALA ASP LEU LEU ASP ARG LEU SEQRES 14 A 265 ALA PHE ASP VAL VAL GLN LEU PRO PRO LEU ARG GLU ARG SEQRES 15 A 265 GLU SER ASP ILE MET LEU MET ALA GLU TYR PHE ALA ILE SEQRES 16 A 265 GLN MET CYS ARG GLU ILE LYS LEU PRO LEU PHE PRO GLY SEQRES 17 A 265 PHE THR GLU ARG ALA ARG GLU THR LEU LEU ASN TYR ARG SEQRES 18 A 265 TRP PRO GLY ASN ILE ARG GLU LEU LYS ASN VAL VAL GLU SEQRES 19 A 265 ARG SER VAL TYR ARG HIS GLY THR SER ASP TYR PRO LEU SEQRES 20 A 265 ASP ASP ILE ILE ILE ASP PRO PHE LYS ARG ARG PRO PRO SEQRES 21 A 265 GLU ASP ALA ILE ALA FORMUL 2 HOH *196(H2 O1) HELIX 1 1 ALA A 12 ALA A 26 1 15 HELIX 2 2 GLY A 41 LEU A 52 1 12 HELIX 3 3 ALA A 66 LEU A 68 5 3 HELIX 4 4 ASN A 69 GLY A 79 1 11 HELIX 5 5 GLY A 94 ALA A 99 1 6 HELIX 6 6 GLU A 108 ALA A 112 5 5 HELIX 7 7 PRO A 113 GLY A 127 1 15 HELIX 8 8 ASP A 151 GLU A 158 1 8 HELIX 9 9 ARG A 162 ALA A 170 1 9 HELIX 10 10 PRO A 178 GLU A 181 5 4 HELIX 11 11 ARG A 182 ILE A 201 1 20 HELIX 12 12 THR A 210 TYR A 220 1 11 HELIX 13 13 GLY A 224 GLY A 241 1 18 SHEET 1 AA 5 PHE A 60 ASN A 64 0 SHEET 2 AA 5 THR A 103 ASP A 107 1 O THR A 103 N ILE A 61 SHEET 3 AA 5 ARG A 143 THR A 148 1 O ARG A 143 N LEU A 104 SHEET 4 AA 5 VAL A 32 ILE A 35 1 O VAL A 32 N CYS A 146 SHEET 5 AA 5 ASP A 172 GLN A 175 1 O ASP A 172 N LEU A 33 SHEET 1 AB 2 GLU A 128 LEU A 129 0 SHEET 2 AB 2 LEU A 138 GLN A 139 -1 O LEU A 138 N LEU A 129 CRYST1 113.695 113.695 39.277 90.00 90.00 120.00 P 65 6 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 0.008795 0.005078 0.000000 0.00000 SCALE2 0.000000 0.010156 0.000000 0.00000 SCALE3 0.000000 0.000000 0.025460 0.00000 ATOM 1 N LEU A 9 31.776 29.918 2.856 1.00 52.23 N ATOM 2 CA LEU A 9 32.562 31.180 2.713 1.00 52.31 C ATOM 3 C LEU A 9 33.068 31.525 4.112 1.00 51.07 C ATOM 4 O LEU A 9 32.644 30.858 5.075 1.00 51.91 O ATOM 5 CB LEU A 9 31.676 32.300 2.170 1.00 52.76 C ATOM 6 CG LEU A 9 31.301 32.268 0.685 1.00 54.99 C ATOM 7 CD1 LEU A 9 30.521 33.536 0.354 1.00 56.38 C ATOM 8 CD2 LEU A 9 32.533 32.121 -0.232 1.00 56.64 C ATOM 9 N GLY A 10 33.974 32.515 4.213 1.00 49.30 N ATOM 10 CA GLY A 10 34.468 33.031 5.494 1.00 47.86 C ATOM 11 C GLY A 10 35.969 32.926 5.697 1.00 45.94 C ATOM 12 O GLY A 10 36.644 32.267 4.908 1.00 47.16 O ATOM 13 N GLU A 11 36.480 33.574 6.749 1.00 42.83 N ATOM 14 CA GLU A 11 37.914 33.667 7.068 1.00 40.61 C ATOM 15 C GLU A 11 38.234 33.392 8.553 1.00 37.26 C ATOM 16 O GLU A 11 39.373 33.565 8.974 1.00 36.55 O ATOM 17 CB GLU A 11 38.445 35.088 6.766 1.00 41.44 C ATOM 18 CG GLU A 11 38.116 35.651 5.394 1.00 44.74 C ATOM 19 CD GLU A 11 38.705 37.049 5.172 1.00 48.66 C ATOM 20 OE1 GLU A 11 38.807 37.866 6.129 1.00 49.96 O ATOM 21 OE2 GLU A 11 39.063 37.345 4.018 1.00 52.40 O ATOM 22 N ALA A 12 37.252 33.010 9.377 1.00 33.84 N ATOM 23 CA ALA A 12 37.577 32.682 10.777 1.00 31.02 C ATOM 24 C ALA A 12 38.607 31.551 10.749 1.00 29.84 C ATOM 25 O ALA A 12 38.592 30.731 9.832 1.00 26.14 O ATOM 26 CB ALA A 12 36.353 32.244 11.569 1.00 31.16 C ATOM 27 N ASN A 13 39.444 31.499 11.771 1.00 28.02 N ATOM 28 CA ASN A 13 40.510 30.498 11.837 1.00 28.91 C ATOM 29 C ASN A 13 39.958 29.085 11.794 1.00 26.59 C ATOM 30 O ASN A 13 40.509 28.257 11.105 1.00 25.67 O ATOM 31 CB ASN A 13 41.361 30.691 13.100 1.00 30.08 C ATOM 32 CG ASN A 13 42.225 31.944 13.024 1.00 34.30 C ATOM 33 OD1 ASN A 13 42.546 32.450 11.914 1.00 39.35 O ATOM 34 ND2 ASN A 13 42.622 32.454 14.202 1.00 37.54 N ATOM 35 N SER A 14 38.851 28.847 12.482 1.00 25.31 N ATOM 36 CA SER A 14 38.206 27.541 12.485 1.00 24.60 C ATOM 37 C SER A 14 37.780 27.151 11.062 1.00 22.88 C ATOM 38 O SER A 14 37.831 25.992 10.750 1.00 20.47 O ATOM 39 CB SER A 14 37.003 27.515 13.392 1.00 24.89 C ATOM 40 OG SER A 14 36.032 28.459 12.956 1.00 25.00 O ATOM 41 N PHE A 15 37.374 28.105 10.224 1.00 22.16 N ATOM 42 CA PHE A 15 37.041 27.788 8.849 1.00 22.95 C ATOM 43 C PHE A 15 38.264 27.580 7.991 1.00 22.03 C ATOM 44 O PHE A 15 38.277 26.699 7.153 1.00 21.50 O ATOM 45 CB PHE A 15 36.137 28.852 8.219 1.00 24.00 C ATOM 46 CG PHE A 15 35.634 28.454 6.871 1.00 28.70 C ATOM 47 CD1 PHE A 15 34.718 27.426 6.747 1.00 30.72 C ATOM 48 CD2 PHE A 15 36.105 29.076 5.730 1.00 34.66 C ATOM 49 CE1 PHE A 15 34.237 27.007 5.463 1.00 35.65 C ATOM 50 CE2 PHE A 15 35.637 28.674 4.453 1.00 35.14 C ATOM 51 CZ PHE A 15 34.710 27.635 4.336 1.00 34.41 C ATOM 52 N LEU A 16 39.305 28.422 8.151 1.00 21.77 N ATOM 53 CA LEU A 16 40.537 28.174 7.433 1.00 22.68 C ATOM 54 C LEU A 16 41.080 26.776 7.755 1.00 22.27 C ATOM 55 O LEU A 16 41.577 26.123 6.866 1.00 22.13 O ATOM 56 CB LEU A 16 41.600 29.246 7.726 1.00 22.75 C ATOM 57 CG LEU A 16 41.123 30.661 7.400 1.00 25.17 C ATOM 58 CD1 LEU A 16 42.279 31.657 7.746 1.00 25.78 C ATOM 59 CD2 LEU A 16 40.680 30.692 5.929 1.00 23.92 C ATOM 60 N GLU A 17 40.977 26.333 9.001 1.00 23.06 N ATOM 61 CA GLU A 17 41.477 25.013 9.387 1.00 23.54 C ATOM 62 C GLU A 17 40.741 23.929 8.600 1.00 22.64 C ATOM 63 O GLU A 17 41.370 22.948 8.177 1.00 21.47 O ATOM 64 CB GLU A 17 41.290 24.777 10.886 1.00 25.23 C ATOM 65 CG GLU A 17 42.107 25.711 11.808 1.00 32.66 C ATOM 66 CD GLU A 17 41.701 25.579 13.293 1.00 42.80 C ATOM 67 OE1 GLU A 17 41.805 24.449 13.829 1.00 47.86 O ATOM 68 OE2 GLU A 17 41.248 26.585 13.934 1.00 48.80 O ATOM 69 N VAL A 18 39.428 24.120 8.382 1.00 20.84 N ATOM 70 CA VAL A 18 38.630 23.213 7.544 1.00 19.88 C ATOM 71 C VAL A 18 39.138 23.181 6.130 1.00 19.24 C ATOM 72 O VAL A 18 39.331 22.123 5.557 1.00 17.77 O ATOM 73 CB VAL A 18 37.104 23.589 7.527 1.00 19.59 C ATOM 74 CG1 VAL A 18 36.371 22.998 6.383 1.00 20.10 C ATOM 75 CG2 VAL A 18 36.439 23.208 8.776 1.00 20.31 C ATOM 76 N LEU A 19 39.400 24.338 5.535 1.00 18.79 N ATOM 77 CA LEU A 19 39.960 24.351 4.194 1.00 19.13 C ATOM 78 C LEU A 19 41.305 23.665 4.070 1.00 20.07 C ATOM 79 O LEU A 19 41.559 22.974 3.082 1.00 20.98 O ATOM 80 CB LEU A 19 40.005 25.795 3.660 1.00 20.52 C ATOM 81 CG LEU A 19 38.661 26.491 3.476 1.00 23.98 C ATOM 82 CD1 LEU A 19 38.855 27.867 2.948 1.00 25.87 C ATOM 83 CD2 LEU A 19 37.710 25.755 2.520 1.00 27.50 C ATOM 84 N GLU A 20 42.155 23.855 5.070 1.00 21.66 N ATOM 85 CA GLU A 20 43.460 23.188 5.107 1.00 22.90 C ATOM 86 C GLU A 20 43.246 21.642 5.185 1.00 22.27 C ATOM 87 O GLU A 20 43.873 20.905 4.444 1.00 21.63 O ATOM 88 CB GLU A 20 44.282 23.734 6.284 1.00 26.47 C ATOM 89 CG GLU A 20 45.580 22.981 6.534 1.00 31.15 C ATOM 90 CD GLU A 20 46.314 23.477 7.794 1.00 42.47 C ATOM 91 OE1 GLU A 20 45.668 23.634 8.875 1.00 47.58 O ATOM 92 OE2 GLU A 20 47.552 23.701 7.716 1.00 46.50 O ATOM 93 N GLN A 21 42.360 21.186 6.062 1.00 20.72 N ATOM 94 CA GLN A 21 42.025 19.781 6.174 1.00 19.94 C ATOM 95 C GLN A 21 41.542 19.214 4.842 1.00 20.36 C ATOM 96 O GLN A 21 42.006 18.171 4.377 1.00 19.28 O ATOM 97 CB GLN A 21 40.910 19.597 7.179 1.00 20.22 C ATOM 98 CG GLN A 21 40.597 18.138 7.397 1.00 22.56 C ATOM 99 CD GLN A 21 39.523 17.948 8.478 1.00 23.41 C ATOM 100 OE1 GLN A 21 38.874 18.882 8.891 1.00 24.59 O ATOM 101 NE2 GLN A 21 39.369 16.732 8.923 1.00 21.33 N ATOM 102 N VAL A 22 40.608 19.936 4.213 1.00 18.27 N ATOM 103 CA VAL A 22 40.085 19.557 2.896 1.00 18.94 C ATOM 104 C VAL A 22 41.157 19.416 1.855 1.00 19.61 C ATOM 105 O VAL A 22 41.132 18.494 1.080 1.00 19.59 O ATOM 106 CB VAL A 22 39.054 20.564 2.405 1.00 18.73 C ATOM 107 CG1 VAL A 22 38.778 20.359 0.944 1.00 20.70 C ATOM 108 CG2 VAL A 22 37.812 20.378 3.203 1.00 20.90 C ATOM 109 N SER A 23 42.157 20.296 1.888 1.00 20.18 N ATOM 110 CA SER A 23 43.257 20.229 0.908 1.00 21.43 C ATOM 111 C SER A 23 44.055 18.938 1.058 1.00 20.60 C ATOM 112 O SER A 23 44.503 18.410 0.075 1.00 22.06 O ATOM 113 CB SER A 23 44.210 21.435 1.009 1.00 23.05 C ATOM 114 OG SER A 23 44.984 21.408 2.201 1.00 28.15 O ATOM 115 N HIS A 24 44.192 18.425 2.283 1.00 20.95 N ATOM 116 CA HIS A 24 44.950 17.165 2.537 1.00 20.85 C ATOM 117 C HIS A 24 44.108 15.908 2.272 1.00 20.44 C ATOM 118 O HIS A 24 44.628 14.915 1.764 1.00 19.42 O ATOM 119 CB HIS A 24 45.482 17.164 3.947 1.00 22.43 C ATOM 120 CG HIS A 24 46.467 18.266 4.193 1.00 24.81 C ATOM 121 ND1 HIS A 24 47.661 18.367 3.506 1.00 32.89 N ATOM 122 CD2 HIS A 24 46.423 19.322 5.037 1.00 29.81 C ATOM 123 CE1 HIS A 24 48.301 19.451 3.917 1.00 32.45 C ATOM 124 NE2 HIS A 24 47.576 20.042 4.852 1.00 31.74 N ATOM 125 N LEU A 25 42.794 15.985 2.502 1.00 19.71 N ATOM 126 CA LEU A 25 41.898 14.836 2.308 1.00 18.41 C ATOM 127 C LEU A 25 41.490 14.622 0.866 1.00 17.43 C ATOM 128 O LEU A 25 41.253 13.505 0.452 1.00 16.21 O ATOM 129 CB LEU A 25 40.606 15.001 3.108 1.00 17.81 C ATOM 130 CG LEU A 25 40.614 14.772 4.624 1.00 22.24 C ATOM 131 CD1 LEU A 25 39.337 15.328 5.252 1.00 26.15 C ATOM 132 CD2 LEU A 25 40.730 13.288 4.912 1.00 21.29 C ATOM 133 N ALA A 26 41.354 15.706 0.094 1.00 17.82 N ATOM 134 CA ALA A 26 40.828 15.626 -1.259 1.00 17.97 C ATOM 135 C ALA A 26 41.554 14.565 -2.155 1.00 18.80 C ATOM 136 O ALA A 26 40.889 13.800 -2.822 1.00 17.73 O ATOM 137 CB ALA A 26 40.852 17.054 -1.910 1.00 18.90 C ATOM 138 N PRO A 27 42.884 14.542 -2.171 1.00 19.60 N ATOM 139 CA PRO A 27 43.621 13.594 -3.027 1.00 22.45 C ATOM 140 C PRO A 27 43.459 12.105 -2.688 1.00 22.22 C ATOM 141 O PRO A 27 43.732 11.230 -3.561 1.00 23.72 O ATOM 142 CB PRO A 27 45.067 14.054 -2.860 1.00 22.33 C ATOM 143 CG PRO A 27 44.928 15.517 -2.428 1.00 24.79 C ATOM 144 CD PRO A 27 43.803 15.443 -1.488 1.00 20.33 C ATOM 145 N LEU A 28 43.001 11.791 -1.493 1.00 22.57 N ATOM 146 CA LEU A 28 42.803 10.415 -1.116 1.00 23.00 C ATOM 147 C LEU A 28 41.543 9.845 -1.768 1.00 22.11 C ATOM 148 O LEU A 28 40.591 10.574 -2.072 1.00 23.24 O ATOM 149 CB LEU A 28 42.654 10.320 0.378 1.00 24.11 C ATOM 150 CG LEU A 28 43.719 10.926 1.280 1.00 27.43 C ATOM 151 CD1 LEU A 28 43.206 10.959 2.675 1.00 32.48 C ATOM 152 CD2 LEU A 28 44.914 10.089 1.220 1.00 32.65 C ATOM 153 N ASP A 29 41.484 8.529 -1.884 1.00 21.78 N ATOM 154 CA ASP A 29 40.263 7.861 -2.333 1.00 22.42 C ATOM 155 C ASP A 29 39.313 7.492 -1.210 1.00 22.00 C ATOM 156 O ASP A 29 38.217 6.876 -1.442 1.00 25.25 O ATOM 157 CB ASP A 29 40.627 6.606 -3.132 1.00 24.32 C ATOM 158 CG ASP A 29 41.203 6.924 -4.473 1.00 32.62 C ATOM 159 OD1 ASP A 29 42.477 7.021 -4.569 1.00 41.64 O ATOM 160 OD2 ASP A 29 40.463 7.083 -5.491 1.00 37.89 O ATOM 161 N LYS A 30 39.596 7.954 -0.002 1.00 18.70 N ATOM 162 CA LYS A 30 38.877 7.473 1.160 1.00 16.32 C ATOM 163 C LYS A 30 37.605 8.231 1.333 1.00 15.76 C ATOM 164 O LYS A 30 37.536 9.384 0.951 1.00 16.87 O ATOM 165 CB LYS A 30 39.741 7.778 2.401 1.00 15.34 C ATOM 166 CG LYS A 30 41.072 6.974 2.399 1.00 17.21 C ATOM 167 CD LYS A 30 40.877 5.476 2.711 1.00 21.42 C ATOM 168 CE LYS A 30 42.167 4.777 2.619 1.00 22.32 C ATOM 169 NZ LYS A 30 42.124 3.390 2.264 1.00 20.81 N ATOM 170 N PRO A 31 36.622 7.623 1.941 1.00 17.44 N ATOM 171 CA PRO A 31 35.346 8.346 2.195 1.00 17.17 C ATOM 172 C PRO A 31 35.524 9.456 3.226 1.00 18.98 C ATOM 173 O PRO A 31 36.403 9.348 4.070 1.00 18.32 O ATOM 174 CB PRO A 31 34.431 7.250 2.722 1.00 17.13 C ATOM 175 CG PRO A 31 35.295 6.117 3.040 1.00 20.05 C ATOM 176 CD PRO A 31 36.550 6.211 2.350 1.00 16.38 C ATOM 177 N VAL A 32 34.743 10.519 3.123 1.00 17.48 N ATOM 178 CA VAL A 32 34.819 11.615 4.051 1.00 16.58 C ATOM 179 C VAL A 32 33.431 11.889 4.582 1.00 16.82 C ATOM 180 O VAL A 32 32.445 11.910 3.818 1.00 16.12 O ATOM 181 CB VAL A 32 35.342 12.883 3.319 1.00 17.82 C ATOM 182 CG1 VAL A 32 35.302 14.080 4.238 1.00 20.98 C ATOM 183 CG2 VAL A 32 36.841 12.618 2.859 1.00 19.87 C ATOM 184 N LEU A 33 33.378 12.087 5.892 1.00 15.68 N ATOM 185 CA LEU A 33 32.170 12.475 6.548 1.00 14.33 C ATOM 186 C LEU A 33 32.240 13.924 6.978 1.00 14.17 C ATOM 187 O LEU A 33 33.139 14.302 7.672 1.00 14.76 O ATOM 188 CB LEU A 33 31.961 11.598 7.763 1.00 14.30 C ATOM 189 CG LEU A 33 30.753 11.830 8.622 1.00 15.91 C ATOM 190 CD1 LEU A 33 29.486 11.630 7.789 1.00 15.82 C ATOM 191 CD2 LEU A 33 30.700 11.004 9.857 1.00 18.37 C ATOM 192 N ILE A 34 31.269 14.716 6.535 1.00 13.64 N ATOM 193 CA ILE A 34 31.149 16.122 6.920 1.00 12.17 C ATOM 194 C ILE A 34 30.035 16.266 7.946 1.00 13.79 C ATOM 195 O ILE A 34 28.914 15.867 7.718 1.00 14.82 O ATOM 196 CB ILE A 34 30.882 17.022 5.656 1.00 14.17 C ATOM 197 CG1 ILE A 34 31.880 16.734 4.577 1.00 14.60 C ATOM 198 CG2 ILE A 34 30.839 18.479 6.086 1.00 14.14 C ATOM 199 CD1 ILE A 34 31.543 17.406 3.230 1.00 17.20 C ATOM 200 N ILE A 35 30.351 16.856 9.089 1.00 14.65 N ATOM 201 CA ILE A 35 29.359 17.138 10.122 1.00 14.51 C ATOM 202 C ILE A 35 29.101 18.641 10.143 1.00 15.32 C ATOM 203 O ILE A 35 30.028 19.405 10.232 1.00 16.83 O ATOM 204 CB ILE A 35 29.855 16.696 11.510 1.00 16.92 C ATOM 205 CG1 ILE A 35 30.222 15.210 11.568 1.00 20.55 C ATOM 206 CG2 ILE A 35 28.787 17.033 12.557 1.00 20.16 C ATOM 207 CD1 ILE A 35 29.097 14.327 11.147 1.00 23.37 C ATOM 208 N GLY A 36 27.860 19.033 9.959 1.00 15.01 N ATOM 209 CA GLY A 36 27.533 20.449 10.002 1.00 16.96 C ATOM 210 C GLY A 36 26.072 20.709 9.974 1.00 16.39 C ATOM 211 O GLY A 36 25.271 19.938 9.417 1.00 16.78 O ATOM 212 N GLU A 37 25.699 21.856 10.508 1.00 15.86 N ATOM 213 CA GLU A 37 24.336 22.323 10.484 1.00 15.84 C ATOM 214 C GLU A 37 23.852 22.735 9.089 1.00 15.92 C ATOM 215 O GLU A 37 24.622 22.950 8.149 1.00 15.94 O ATOM 216 CB GLU A 37 24.138 23.493 11.493 1.00 16.04 C ATOM 217 CG GLU A 37 24.354 23.078 12.945 1.00 18.37 C ATOM 218 CD GLU A 37 24.248 24.225 13.924 1.00 22.27 C ATOM 219 OE1 GLU A 37 23.798 25.329 13.547 1.00 17.31 O ATOM 220 OE2 GLU A 37 24.658 24.020 15.070 1.00 19.74 O ATOM 221 N ARG A 38 22.536 22.872 8.951 1.00 17.02 N ATOM 222 CA ARG A 38 22.010 23.419 7.727 1.00 16.76 C ATOM 223 C ARG A 38 22.592 24.807 7.428 1.00 17.03 C ATOM 224 O ARG A 38 22.801 25.622 8.305 1.00 16.12 O ATOM 225 CB ARG A 38 20.478 23.442 7.680 1.00 20.16 C ATOM 226 CG ARG A 38 19.873 24.592 8.173 1.00 21.67 C ATOM 227 CD ARG A 38 18.356 24.605 7.968 1.00 19.89 C ATOM 228 NE ARG A 38 17.751 25.715 8.691 1.00 18.21 N ATOM 229 CZ ARG A 38 17.371 25.665 9.941 1.00 22.75 C ATOM 230 NH1 ARG A 38 17.457 24.549 10.664 1.00 26.34 N ATOM 231 NH2 ARG A 38 16.896 26.775 10.474 1.00 28.19 N ATOM 232 N GLY A 39 22.828 25.055 6.150 1.00 16.50 N ATOM 233 CA GLY A 39 23.347 26.320 5.693 1.00 16.68 C ATOM 234 C GLY A 39 24.801 26.614 6.003 1.00 15.25 C ATOM 235 O GLY A 39 25.225 27.745 5.855 1.00 13.96 O ATOM 236 N THR A 40 25.590 25.596 6.376 1.00 15.08 N ATOM 237 CA THR A 40 27.026 25.751 6.563 1.00 15.89 C ATOM 238 C THR A 40 27.906 25.461 5.365 1.00 16.91 C ATOM 239 O THR A 40 29.109 25.680 5.453 1.00 20.63 O ATOM 240 CB THR A 40 27.525 24.914 7.708 1.00 17.50 C ATOM 241 OG1 THR A 40 27.143 23.529 7.571 1.00 17.28 O ATOM 242 CG2 THR A 40 26.943 25.349 9.018 1.00 16.49 C ATOM 243 N GLY A 41 27.322 24.995 4.278 1.00 19.02 N ATOM 244 CA GLY A 41 28.032 24.814 3.015 1.00 19.58 C ATOM 245 C GLY A 41 28.556 23.412 2.829 1.00 18.47 C ATOM 246 O GLY A 41 29.600 23.178 2.230 1.00 19.04 O ATOM 247 N LYS A 42 27.859 22.429 3.395 1.00 17.01 N ATOM 248 CA LYS A 42 28.348 21.061 3.274 1.00 17.03 C ATOM 249 C LYS A 42 28.560 20.629 1.844 1.00 17.07 C ATOM 250 O LYS A 42 29.579 20.002 1.564 1.00 19.08 O ATOM 251 CB LYS A 42 27.403 20.097 4.018 1.00 17.79 C ATOM 252 CG LYS A 42 27.390 20.450 5.487 1.00 17.74 C ATOM 253 CD LYS A 42 26.833 19.470 6.428 1.00 25.20 C ATOM 254 CE LYS A 42 25.454 19.205 6.123 1.00 24.43 C ATOM 255 NZ LYS A 42 24.593 20.386 6.190 1.00 29.44 N ATOM 256 N GLU A 43 27.605 20.905 0.972 1.00 18.92 N ATOM 257 CA GLU A 43 27.723 20.460 -0.414 1.00 20.14 C ATOM 258 C GLU A 43 28.867 21.199 -1.143 1.00 18.90 C ATOM 259 O GLU A 43 29.517 20.638 -2.013 1.00 17.55 O ATOM 260 CB GLU A 43 26.406 20.620 -1.161 1.00 19.96 C ATOM 261 CG GLU A 43 26.489 20.216 -2.628 1.00 26.10 C ATOM 262 CD GLU A 43 25.102 20.122 -3.278 1.00 35.95 C ATOM 263 OE1 GLU A 43 24.245 20.980 -2.987 1.00 40.82 O ATOM 264 OE2 GLU A 43 24.889 19.221 -4.110 1.00 36.64 O ATOM 265 N LEU A 44 29.128 22.444 -0.766 1.00 18.67 N ATOM 266 CA LEU A 44 30.249 23.181 -1.331 1.00 19.95 C ATOM 267 C LEU A 44 31.597 22.631 -0.902 1.00 19.31 C ATOM 268 O LEU A 44 32.539 22.576 -1.698 1.00 18.33 O ATOM 269 CB LEU A 44 30.134 24.675 -0.997 1.00 22.61 C ATOM 270 CG LEU A 44 28.938 25.403 -1.609 1.00 26.10 C ATOM 271 CD1 LEU A 44 28.848 26.782 -0.996 1.00 30.39 C ATOM 272 CD2 LEU A 44 29.097 25.556 -3.090 1.00 31.46 C ATOM 273 N ILE A 45 31.664 22.127 0.310 1.00 17.13 N ATOM 274 CA ILE A 45 32.858 21.443 0.787 1.00 17.21 C ATOM 275 C ILE A 45 33.012 20.128 0.069 1.00 16.64 C ATOM 276 O ILE A 45 34.130 19.782 -0.363 1.00 15.88 O ATOM 277 CB ILE A 45 32.794 21.244 2.321 1.00 18.01 C ATOM 278 CG1 ILE A 45 32.892 22.594 3.051 1.00 18.53 C ATOM 279 CG2 ILE A 45 33.881 20.302 2.816 1.00 16.73 C ATOM 280 CD1 ILE A 45 34.143 23.388 2.795 1.00 21.80 C ATOM 281 N ALA A 46 31.923 19.402 -0.097 1.00 15.86 N ATOM 282 CA ALA A 46 31.958 18.187 -0.854 1.00 15.96 C ATOM 283 C ALA A 46 32.493 18.443 -2.293 1.00 18.26 C ATOM 284 O ALA A 46 33.327 17.721 -2.752 1.00 17.91 O ATOM 285 CB ALA A 46 30.618 17.569 -0.905 1.00 15.82 C ATOM 286 N SER A 47 31.969 19.454 -2.953 1.00 18.04 N ATOM 287 CA SER A 47 32.406 19.880 -4.283 1.00 19.99 C ATOM 288 C SER A 47 33.918 20.178 -4.328 1.00 21.58 C ATOM 289 O SER A 47 34.625 19.770 -5.230 1.00 22.05 O ATOM 290 CB SER A 47 31.615 21.112 -4.700 1.00 20.88 C ATOM 291 OG SER A 47 31.968 21.444 -6.034 1.00 25.42 O ATOM 292 N ARG A 48 34.409 20.877 -3.332 1.00 21.97 N ATOM 293 CA ARG A 48 35.809 21.204 -3.165 1.00 23.22 C ATOM 294 C ARG A 48 36.674 20.003 -3.034 1.00 23.34 C ATOM 295 O ARG A 48 37.766 19.945 -3.637 1.00 25.95 O ATOM 296 CB ARG A 48 36.011 22.108 -1.931 1.00 24.41 C ATOM 297 CG ARG A 48 37.339 22.873 -1.963 1.00 26.29 C ATOM 298 CD ARG A 48 37.435 23.860 -0.826 1.00 30.92 C ATOM 299 NE ARG A 48 38.762 24.460 -0.708 1.00 34.17 N ATOM 300 CZ ARG A 48 39.048 25.706 -1.078 1.00 39.55 C ATOM 301 NH1 ARG A 48 38.100 26.515 -1.569 1.00 41.42 N ATOM 302 NH2 ARG A 48 40.288 26.170 -0.934 1.00 41.33 N ATOM 303 N LEU A 49 36.234 19.019 -2.274 1.00 22.09 N ATOM 304 CA LEU A 49 36.922 17.741 -2.176 1.00 20.60 C ATOM 305 C LEU A 49 37.044 17.144 -3.599 1.00 21.09 C ATOM 306 O LEU A 49 38.125 16.751 -4.014 1.00 23.02 O ATOM 307 CB LEU A 49 36.206 16.745 -1.244 1.00 20.66 C ATOM 308 CG LEU A 49 36.357 17.099 0.246 1.00 18.02 C ATOM 309 CD1 LEU A 49 35.283 16.401 1.090 1.00 21.06 C ATOM 310 CD2 LEU A 49 37.765 16.694 0.689 1.00 17.27 C ATOM 311 N HIS A 50 35.954 17.136 -4.355 1.00 19.26 N ATOM 312 CA HIS A 50 35.972 16.597 -5.691 1.00 17.79 C ATOM 313 C HIS A 50 36.949 17.327 -6.617 1.00 19.50 C ATOM 314 O HIS A 50 37.825 16.714 -7.211 1.00 17.55 O ATOM 315 CB HIS A 50 34.596 16.671 -6.300 1.00 17.74 C ATOM 316 CG HIS A 50 34.541 16.163 -7.719 1.00 19.13 C ATOM 317 ND1 HIS A 50 34.671 14.832 -8.029 1.00 19.01 N ATOM 318 CD2 HIS A 50 34.401 16.825 -8.901 1.00 21.30 C ATOM 319 CE1 HIS A 50 34.565 14.684 -9.348 1.00 20.11 C ATOM 320 NE2 HIS A 50 34.396 15.878 -9.896 1.00 18.18 N ATOM 321 N TYR A 51 36.831 18.636 -6.647 1.00 18.94 N ATOM 322 CA TYR A 51 37.644 19.429 -7.575 1.00 22.01 C ATOM 323 C TYR A 51 39.107 19.533 -7.202 1.00 21.93 C ATOM 324 O TYR A 51 39.942 19.738 -8.097 1.00 22.36 O ATOM 325 CB TYR A 51 36.991 20.738 -7.829 1.00 22.60 C ATOM 326 CG TYR A 51 35.765 20.503 -8.709 1.00 28.76 C ATOM 327 CD1 TYR A 51 34.462 20.580 -8.171 1.00 29.21 C ATOM 328 CD2 TYR A 51 35.900 20.091 -10.060 1.00 32.29 C ATOM 329 CE1 TYR A 51 33.366 20.308 -8.929 1.00 32.00 C ATOM 330 CE2 TYR A 51 34.795 19.835 -10.838 1.00 32.58 C ATOM 331 CZ TYR A 51 33.519 19.959 -10.269 1.00 35.32 C ATOM 332 OH TYR A 51 32.384 19.692 -11.003 1.00 36.28 O ATOM 333 N LEU A 52 39.452 19.295 -5.945 1.00 21.35 N ATOM 334 CA LEU A 52 40.837 19.188 -5.534 1.00 22.14 C ATOM 335 C LEU A 52 41.398 17.786 -5.588 1.00 22.28 C ATOM 336 O LEU A 52 42.560 17.563 -5.237 1.00 22.26 O ATOM 337 CB LEU A 52 41.047 19.772 -4.131 1.00 22.36 C ATOM 338 CG LEU A 52 40.832 21.269 -3.984 1.00 22.84 C ATOM 339 CD1 LEU A 52 40.903 21.696 -2.551 1.00 21.85 C ATOM 340 CD2 LEU A 52 41.827 22.023 -4.836 1.00 27.00 C ATOM 341 N SER A 53 40.613 16.833 -6.014 1.00 21.63 N ATOM 342 CA SER A 53 41.068 15.447 -6.087 1.00 21.94 C ATOM 343 C SER A 53 41.565 15.127 -7.494 1.00 23.93 C ATOM 344 O SER A 53 41.423 15.934 -8.426 1.00 23.54 O ATOM 345 CB SER A 53 39.935 14.476 -5.693 1.00 21.65 C ATOM 346 OG SER A 53 38.971 14.410 -6.720 1.00 19.53 O ATOM 347 N SER A 54 42.110 13.920 -7.649 1.00 25.71 N ATOM 348 CA SER A 54 42.493 13.416 -8.969 1.00 26.04 C ATOM 349 C SER A 54 41.306 13.096 -9.848 1.00 26.18 C ATOM 350 O SER A 54 41.472 12.933 -11.050 1.00 27.38 O ATOM 351 CB SER A 54 43.386 12.186 -8.815 1.00 26.77 C ATOM 352 OG SER A 54 42.649 11.038 -8.429 1.00 29.39 O ATOM 353 N ARG A 55 40.100 13.046 -9.273 1.00 24.59 N ATOM 354 CA ARG A 55 38.873 12.743 -9.990 1.00 24.82 C ATOM 355 C ARG A 55 38.168 13.955 -10.540 1.00 24.47 C ATOM 356 O ARG A 55 37.035 13.854 -11.064 1.00 22.39 O ATOM 357 CB ARG A 55 37.860 12.068 -9.024 1.00 27.01 C ATOM 358 CG ARG A 55 38.331 10.794 -8.519 1.00 27.15 C ATOM 359 CD ARG A 55 37.447 10.199 -7.483 1.00 26.95 C ATOM 360 NE ARG A 55 37.895 8.859 -7.247 1.00 26.80 N ATOM 361 CZ ARG A 55 37.346 7.770 -7.732 1.00 28.68 C ATOM 362 NH1 ARG A 55 36.200 7.788 -8.432 1.00 23.64 N ATOM 363 NH2 ARG A 55 37.940 6.638 -7.465 1.00 31.21 N ATOM 364 N TRP A 56 38.827 15.103 -10.435 1.00 23.76 N ATOM 365 CA TRP A 56 38.160 16.368 -10.694 1.00 24.21 C ATOM 366 C TRP A 56 37.463 16.495 -12.052 1.00 24.91 C ATOM 367 O TRP A 56 36.493 17.236 -12.163 1.00 24.73 O ATOM 368 CB TRP A 56 39.136 17.508 -10.497 1.00 24.82 C ATOM 369 CG TRP A 56 40.213 17.545 -11.504 1.00 27.24 C ATOM 370 CD1 TRP A 56 41.346 16.818 -11.503 1.00 29.42 C ATOM 371 CD2 TRP A 56 40.252 18.364 -12.678 1.00 31.37 C ATOM 372 NE1 TRP A 56 42.130 17.154 -12.586 1.00 31.51 N ATOM 373 CE2 TRP A 56 41.478 18.102 -13.328 1.00 32.44 C ATOM 374 CE3 TRP A 56 39.388 19.313 -13.236 1.00 34.41 C ATOM 375 CZ2 TRP A 56 41.854 18.737 -14.523 1.00 33.83 C ATOM 376 CZ3 TRP A 56 39.781 19.962 -14.443 1.00 37.50 C ATOM 377 CH2 TRP A 56 40.990 19.654 -15.057 1.00 34.05 C ATOM 378 N GLN A 57 37.933 15.760 -13.065 1.00 25.47 N ATOM 379 CA GLN A 57 37.267 15.742 -14.353 1.00 25.47 C ATOM 380 C GLN A 57 36.127 14.731 -14.459 1.00 26.28 C ATOM 381 O GLN A 57 35.378 14.725 -15.443 1.00 26.09 O ATOM 382 CB GLN A 57 38.318 15.421 -15.417 1.00 26.63 C ATOM 383 CG GLN A 57 39.263 16.554 -15.698 1.00 29.09 C ATOM 384 CD GLN A 57 39.960 16.438 -17.073 1.00 30.83 C ATOM 385 OE1 GLN A 57 39.500 17.005 -18.080 1.00 33.47 O ATOM 386 NE2 GLN A 57 41.009 15.689 -17.110 1.00 27.92 N ATOM 387 N GLY A 58 36.056 13.790 -13.522 1.00 24.89 N ATOM 388 CA GLY A 58 34.860 12.969 -13.375 1.00 25.17 C ATOM 389 C GLY A 58 33.623 13.686 -12.840 1.00 25.42 C ATOM 390 O GLY A 58 33.652 14.867 -12.536 1.00 27.06 O ATOM 391 N PRO A 59 32.507 12.976 -12.755 1.00 24.49 N ATOM 392 CA PRO A 59 31.253 13.599 -12.357 1.00 24.86 C ATOM 393 C PRO A 59 31.164 13.888 -10.859 1.00 24.48 C ATOM 394 O PRO A 59 31.700 13.104 -10.089 1.00 23.98 O ATOM 395 CB PRO A 59 30.210 12.577 -12.771 1.00 24.65 C ATOM 396 CG PRO A 59 30.898 11.262 -12.709 1.00 26.57 C ATOM 397 CD PRO A 59 32.353 11.562 -13.097 1.00 24.81 C ATOM 398 N PHE A 60 30.506 14.982 -10.480 1.00 24.86 N ATOM 399 CA PHE A 60 30.073 15.214 -9.085 1.00 24.40 C ATOM 400 C PHE A 60 28.547 15.075 -8.986 1.00 23.95 C ATOM 401 O PHE A 60 27.810 15.872 -9.526 1.00 22.36 O ATOM 402 CB PHE A 60 30.514 16.590 -8.657 1.00 24.53 C ATOM 403 CG PHE A 60 30.123 16.943 -7.254 1.00 25.01 C ATOM 404 CD1 PHE A 60 30.823 16.398 -6.193 1.00 23.61 C ATOM 405 CD2 PHE A 60 29.026 17.751 -6.990 1.00 24.92 C ATOM 406 CE1 PHE A 60 30.450 16.719 -4.869 1.00 21.76 C ATOM 407 CE2 PHE A 60 28.658 18.062 -5.700 1.00 25.31 C ATOM 408 CZ PHE A 60 29.368 17.506 -4.638 1.00 24.31 C ATOM 409 N ILE A 61 28.089 14.084 -8.225 1.00 24.08 N ATOM 410 CA ILE A 61 26.707 13.725 -8.142 1.00 23.25 C ATOM 411 C ILE A 61 26.306 13.908 -6.659 1.00 23.86 C ATOM 412 O ILE A 61 27.101 13.629 -5.793 1.00 21.41 O ATOM 413 CB ILE A 61 26.495 12.300 -8.560 1.00 23.81 C ATOM 414 CG1 ILE A 61 26.940 12.021 -9.987 1.00 26.20 C ATOM 415 CG2 ILE A 61 25.021 11.925 -8.407 1.00 24.07 C ATOM 416 CD1 ILE A 61 26.341 12.959 -11.050 1.00 28.16 C ATOM 417 N SER A 62 25.091 14.375 -6.430 1.00 23.52 N ATOM 418 CA SER A 62 24.601 14.648 -5.116 1.00 23.92 C ATOM 419 C SER A 62 23.216 14.038 -4.935 1.00 24.72 C ATOM 420 O SER A 62 22.402 13.971 -5.880 1.00 25.22 O ATOM 421 CB SER A 62 24.580 16.153 -5.006 1.00 24.70 C ATOM 422 OG SER A 62 24.042 16.537 -3.778 1.00 33.86 O ATOM 423 N LEU A 63 22.906 13.648 -3.706 1.00 22.27 N ATOM 424 CA LEU A 63 21.604 13.104 -3.355 1.00 23.45 C ATOM 425 C LEU A 63 21.321 13.422 -1.893 1.00 23.27 C ATOM 426 O LEU A 63 22.179 13.231 -1.045 1.00 21.22 O ATOM 427 CB LEU A 63 21.547 11.604 -3.566 1.00 23.64 C ATOM 428 CG LEU A 63 20.206 10.954 -3.167 1.00 25.40 C ATOM 429 CD1 LEU A 63 19.145 11.440 -4.143 1.00 29.88 C ATOM 430 CD2 LEU A 63 20.354 9.466 -3.253 1.00 29.62 C ATOM 431 N ASN A 64 20.120 13.921 -1.614 1.00 21.00 N ATOM 432 CA ASN A 64 19.690 14.143 -0.236 1.00 21.01 C ATOM 433 C ASN A 64 18.878 12.951 0.212 1.00 21.83 C ATOM 434 O ASN A 64 17.767 12.787 -0.258 1.00 22.44 O ATOM 435 CB ASN A 64 18.802 15.358 -0.131 1.00 20.92 C ATOM 436 CG ASN A 64 18.560 15.795 1.331 1.00 22.52 C ATOM 437 OD1 ASN A 64 18.300 14.987 2.198 1.00 25.39 O ATOM 438 ND2 ASN A 64 18.672 17.059 1.583 1.00 28.87 N ATOM 439 N CYS A 65 19.400 12.173 1.157 1.00 21.26 N ATOM 440 CA CYS A 65 18.790 10.935 1.569 1.00 20.66 C ATOM 441 C CYS A 65 17.433 11.193 2.235 1.00 22.51 C ATOM 442 O CYS A 65 16.623 10.318 2.285 1.00 21.24 O ATOM 443 CB CYS A 65 19.670 10.157 2.545 1.00 21.33 C ATOM 444 SG CYS A 65 21.254 9.656 1.817 1.00 23.54 S ATOM 445 N ALA A 66 17.269 12.349 2.855 1.00 23.42 N ATOM 446 CA ALA A 66 16.071 12.650 3.635 1.00 24.52 C ATOM 447 C ALA A 66 14.864 12.882 2.759 1.00 26.54 C ATOM 448 O ALA A 66 13.734 12.766 3.245 1.00 27.54 O ATOM 449 CB ALA A 66 16.307 13.849 4.537 1.00 25.01 C ATOM 450 N ALA A 67 15.085 13.148 1.474 1.00 27.26 N ATOM 451 CA ALA A 67 14.004 13.601 0.595 1.00 28.70 C ATOM 452 C ALA A 67 13.115 12.452 0.100 1.00 30.31 C ATOM 453 O ALA A 67 11.978 12.673 -0.362 1.00 29.69 O ATOM 454 CB ALA A 67 14.629 14.362 -0.579 1.00 28.95 C ATOM 455 N LEU A 68 13.618 11.223 0.196 1.00 30.73 N ATOM 456 CA LEU A 68 12.986 10.073 -0.412 1.00 32.39 C ATOM 457 C LEU A 68 12.617 9.024 0.623 1.00 32.93 C ATOM 458 O LEU A 68 13.380 8.776 1.552 1.00 32.08 O ATOM 459 CB LEU A 68 13.935 9.425 -1.402 1.00 32.08 C ATOM 460 CG LEU A 68 14.404 10.314 -2.559 1.00 35.22 C ATOM 461 CD1 LEU A 68 15.412 9.564 -3.457 1.00 37.72 C ATOM 462 CD2 LEU A 68 13.211 10.776 -3.393 1.00 36.68 C ATOM 463 N ASN A 69 11.455 8.385 0.435 1.00 33.60 N ATOM 464 CA ASN A 69 11.085 7.219 1.216 1.00 34.48 C ATOM 465 C ASN A 69 12.019 6.050 0.945 1.00 35.09 C ATOM 466 O ASN A 69 12.775 6.075 -0.015 1.00 35.46 O ATOM 467 CB ASN A 69 9.638 6.779 0.871 1.00 35.10 C ATOM 468 CG ASN A 69 9.508 6.280 -0.561 1.00 37.14 C ATOM 469 OD1 ASN A 69 9.876 5.134 -0.871 1.00 38.24 O ATOM 470 ND2 ASN A 69 9.022 7.153 -1.449 1.00 41.02 N ATOM 471 N GLU A 70 11.912 5.002 1.746 1.00 34.68 N ATOM 472 CA GLU A 70 12.880 3.899 1.712 1.00 35.58 C ATOM 473 C GLU A 70 13.045 3.201 0.362 1.00 35.80 C ATOM 474 O GLU A 70 14.177 2.940 -0.086 1.00 34.69 O ATOM 475 CB GLU A 70 12.536 2.873 2.793 1.00 35.53 C ATOM 476 CG GLU A 70 13.419 1.631 2.793 1.00 37.74 C ATOM 477 CD GLU A 70 13.358 0.890 4.113 1.00 39.50 C ATOM 478 OE1 GLU A 70 12.468 1.187 4.906 1.00 44.34 O ATOM 479 OE2 GLU A 70 14.189 0.033 4.367 1.00 40.97 O ATOM 480 N ASN A 71 11.933 2.868 -0.287 1.00 35.44 N ATOM 481 CA ASN A 71 12.017 2.169 -1.564 1.00 35.26 C ATOM 482 C ASN A 71 12.555 3.051 -2.668 1.00 32.92 C ATOM 483 O ASN A 71 13.333 2.597 -3.520 1.00 32.15 O ATOM 484 CB ASN A 71 10.632 1.618 -1.942 1.00 37.04 C ATOM 485 CG ASN A 71 10.254 0.408 -1.099 1.00 41.34 C ATOM 486 OD1 ASN A 71 11.118 -0.426 -0.790 1.00 51.60 O ATOM 487 ND2 ASN A 71 8.987 0.313 -0.695 1.00 46.93 N ATOM 488 N LEU A 72 12.139 4.308 -2.666 1.00 30.63 N ATOM 489 CA LEU A 72 12.616 5.281 -3.646 1.00 30.53 C ATOM 490 C LEU A 72 14.104 5.628 -3.388 1.00 28.44 C ATOM 491 O LEU A 72 14.853 5.793 -4.341 1.00 27.32 O ATOM 492 CB LEU A 72 11.786 6.517 -3.649 1.00 30.92 C ATOM 493 N LEU A 73 14.527 5.715 -2.126 1.00 25.77 N ATOM 494 CA LEU A 73 15.950 5.992 -1.864 1.00 24.72 C ATOM 495 C LEU A 73 16.801 4.857 -2.369 1.00 24.35 C ATOM 496 O LEU A 73 17.833 5.073 -2.945 1.00 26.03 O ATOM 497 CB LEU A 73 16.223 6.239 -0.390 1.00 23.49 C ATOM 498 CG LEU A 73 17.680 6.503 -0.032 1.00 21.82 C ATOM 499 CD1 LEU A 73 18.264 7.721 -0.735 1.00 20.73 C ATOM 500 CD2 LEU A 73 17.700 6.702 1.498 1.00 22.51 C ATOM 501 N ASP A 74 16.387 3.638 -2.098 1.00 24.63 N ATOM 502 CA ASP A 74 17.117 2.458 -2.555 1.00 25.76 C ATOM 503 C ASP A 74 17.297 2.393 -4.100 1.00 26.48 C ATOM 504 O ASP A 74 18.385 2.062 -4.622 1.00 25.53 O ATOM 505 CB ASP A 74 16.364 1.235 -2.039 1.00 27.39 C ATOM 506 CG ASP A 74 17.018 -0.040 -2.434 1.00 31.23 C ATOM 507 OD1 ASP A 74 16.730 -0.499 -3.545 1.00 39.98 O ATOM 508 OD2 ASP A 74 17.815 -0.650 -1.703 1.00 37.84 O ATOM 509 N SER A 75 16.218 2.703 -4.821 1.00 26.92 N ATOM 510 CA SER A 75 16.216 2.742 -6.276 1.00 28.05 C ATOM 511 C SER A 75 17.093 3.893 -6.784 1.00 26.85 C ATOM 512 O SER A 75 17.784 3.754 -7.786 1.00 26.88 O ATOM 513 CB SER A 75 14.762 2.960 -6.768 1.00 29.18 C ATOM 514 OG SER A 75 14.058 1.753 -6.718 1.00 34.97 O ATOM 515 N GLU A 76 17.062 5.031 -6.096 1.00 24.99 N ATOM 516 CA GLU A 76 17.749 6.209 -6.548 1.00 25.70 C ATOM 517 C GLU A 76 19.279 6.073 -6.354 1.00 24.27 C ATOM 518 O GLU A 76 20.073 6.524 -7.181 1.00 23.41 O ATOM 519 CB GLU A 76 17.168 7.458 -5.883 1.00 26.77 C ATOM 520 CG GLU A 76 17.524 8.775 -6.562 1.00 31.79 C ATOM 521 CD GLU A 76 17.279 8.807 -8.087 1.00 37.38 C ATOM 522 OE1 GLU A 76 16.277 8.208 -8.567 1.00 37.62 O ATOM 523 OE2 GLU A 76 18.129 9.430 -8.786 1.00 38.16 O ATOM 524 N LEU A 77 19.674 5.367 -5.309 1.00 23.23 N ATOM 525 CA LEU A 77 21.086 5.152 -5.021 1.00 23.10 C ATOM 526 C LEU A 77 21.648 4.004 -5.800 1.00 23.32 C ATOM 527 O LEU A 77 22.704 4.091 -6.383 1.00 22.20 O ATOM 528 CB LEU A 77 21.275 4.797 -3.524 1.00 21.77 C ATOM 529 CG LEU A 77 21.722 5.880 -2.628 1.00 26.59 C ATOM 530 CD1 LEU A 77 21.920 5.235 -1.230 1.00 27.15 C ATOM 531 CD2 LEU A 77 22.996 6.506 -3.179 1.00 26.57 C ATOM 532 N PHE A 78 20.931 2.895 -5.797 1.00 23.59 N ATOM 533 CA PHE A 78 21.493 1.656 -6.333 1.00 24.88 C ATOM 534 C PHE A 78 20.910 1.316 -7.713 1.00 26.82 C ATOM 535 O PHE A 78 21.401 0.392 -8.318 1.00 27.88 O ATOM 536 CB PHE A 78 21.284 0.524 -5.372 1.00 24.59 C ATOM 537 CG PHE A 78 21.788 0.839 -3.973 1.00 23.71 C ATOM 538 CD1 PHE A 78 20.901 0.984 -2.935 1.00 25.86 C ATOM 539 CD2 PHE A 78 23.132 1.003 -3.746 1.00 25.72 C ATOM 540 CE1 PHE A 78 21.350 1.302 -1.667 1.00 25.21 C ATOM 541 CE2 PHE A 78 23.613 1.335 -2.476 1.00 23.42 C ATOM 542 CZ PHE A 78 22.724 1.476 -1.445 1.00 23.32 C ATOM 543 N GLY A 79 19.913 2.086 -8.160 1.00 29.10 N ATOM 544 CA GLY A 79 19.286 1.890 -9.479 1.00 31.53 C ATOM 545 C GLY A 79 18.227 0.788 -9.440 1.00 34.73 C ATOM 546 O GLY A 79 18.058 0.117 -8.428 1.00 32.47 O ATOM 547 N HIS A 80 17.510 0.609 -10.556 1.00 37.29 N ATOM 548 CA HIS A 80 16.593 -0.539 -10.732 1.00 40.84 C ATOM 549 C HIS A 80 16.371 -0.812 -12.233 1.00 42.62 C ATOM 550 O HIS A 80 16.548 0.080 -13.084 1.00 41.41 O ATOM 551 CB HIS A 80 15.244 -0.327 -10.020 1.00 41.21 C ATOM 552 CG HIS A 80 14.426 0.781 -10.600 1.00 44.56 C ATOM 553 ND1 HIS A 80 14.794 2.109 -10.510 1.00 46.76 N ATOM 554 CD2 HIS A 80 13.270 0.760 -11.307 1.00 47.78 C ATOM 555 CE1 HIS A 80 13.892 2.861 -11.117 1.00 47.86 C ATOM 556 NE2 HIS A 80 12.963 2.067 -11.622 1.00 48.85 N ATOM 557 N GLU A 81 16.025 -2.057 -12.543 1.00 45.47 N ATOM 558 CA GLU A 81 15.699 -2.479 -13.916 1.00 47.43 C ATOM 559 C GLU A 81 14.591 -3.502 -13.831 1.00 47.39 C ATOM 560 O GLU A 81 13.546 -3.200 -13.252 1.00 48.24 O ATOM 561 CB GLU A 81 16.927 -3.062 -14.643 1.00 48.34 C ATOM 562 CG GLU A 81 17.725 -4.096 -13.832 1.00 51.75 C ATOM 563 CD GLU A 81 18.932 -4.639 -14.600 1.00 56.59 C ATOM 564 OE1 GLU A 81 19.833 -3.844 -14.914 1.00 59.36 O ATOM 565 OE2 GLU A 81 18.987 -5.859 -14.914 1.00 57.81 O ATOM 566 N LYS A 90 15.420 0.756 -20.832 1.00 47.98 N ATOM 567 CA LYS A 90 15.740 -0.539 -20.235 1.00 47.88 C ATOM 568 C LYS A 90 16.108 -0.478 -18.737 1.00 47.75 C ATOM 569 O LYS A 90 15.951 -1.465 -17.997 1.00 48.53 O ATOM 570 CB LYS A 90 16.862 -1.211 -21.026 1.00 48.33 C ATOM 571 N ARG A 91 16.614 0.667 -18.279 1.00 46.21 N ATOM 572 CA ARG A 91 17.131 0.777 -16.913 1.00 45.00 C ATOM 573 C ARG A 91 17.098 2.208 -16.407 1.00 42.28 C ATOM 574 O ARG A 91 17.265 3.142 -17.197 1.00 40.15 O ATOM 575 CB ARG A 91 18.561 0.261 -16.885 1.00 45.42 C ATOM 576 CG ARG A 91 19.116 0.176 -15.510 1.00 51.34 C ATOM 577 CD ARG A 91 20.083 -0.973 -15.290 1.00 58.44 C ATOM 578 NE ARG A 91 20.142 -1.393 -13.870 1.00 63.15 N ATOM 579 CZ ARG A 91 20.679 -0.667 -12.906 1.00 63.62 C ATOM 580 NH1 ARG A 91 21.182 0.516 -13.185 1.00 64.13 N ATOM 581 NH2 ARG A 91 20.689 -1.109 -11.658 1.00 64.93 N ATOM 582 N HIS A 92 16.875 2.366 -15.088 1.00 39.73 N ATOM 583 CA HIS A 92 17.063 3.636 -14.380 1.00 38.32 C ATOM 584 C HIS A 92 18.347 3.528 -13.540 1.00 34.51 C ATOM 585 O HIS A 92 18.331 2.953 -12.454 1.00 32.57 O ATOM 586 CB HIS A 92 15.878 3.967 -13.450 1.00 39.12 C ATOM 587 CG HIS A 92 16.116 5.155 -12.547 1.00 44.40 C ATOM 588 ND1 HIS A 92 16.264 6.442 -13.027 1.00 49.13 N ATOM 589 CD2 HIS A 92 16.232 5.247 -11.191 1.00 47.93 C ATOM 590 CE1 HIS A 92 16.453 7.273 -12.012 1.00 50.39 C ATOM 591 NE2 HIS A 92 16.437 6.574 -10.889 1.00 49.58 N ATOM 592 N PRO A 93 19.452 4.034 -14.065 1.00 30.57 N ATOM 593 CA PRO A 93 20.716 4.041 -13.327 1.00 29.40 C ATOM 594 C PRO A 93 20.596 4.863 -12.048 1.00 27.76 C ATOM 595 O PRO A 93 19.943 5.926 -12.032 1.00 27.91 O ATOM 596 CB PRO A 93 21.677 4.758 -14.294 1.00 29.94 C ATOM 597 CG PRO A 93 21.069 4.627 -15.563 1.00 29.37 C ATOM 598 CD PRO A 93 19.609 4.689 -15.378 1.00 30.06 C ATOM 599 N GLY A 94 21.252 4.381 -11.008 1.00 25.67 N ATOM 600 CA GLY A 94 21.248 5.057 -9.731 1.00 23.96 C ATOM 601 C GLY A 94 22.412 6.005 -9.651 1.00 23.95 C ATOM 602 O GLY A 94 23.224 6.170 -10.586 1.00 23.54 O ATOM 603 N ARG A 95 22.512 6.675 -8.521 1.00 23.94 N ATOM 604 CA ARG A 95 23.509 7.746 -8.353 1.00 23.41 C ATOM 605 C ARG A 95 24.934 7.236 -8.265 1.00 22.98 C ATOM 606 O ARG A 95 25.884 8.001 -8.649 1.00 23.78 O ATOM 607 CB ARG A 95 23.202 8.598 -7.109 1.00 24.59 C ATOM 608 CG ARG A 95 21.828 9.186 -7.069 1.00 26.81 C ATOM 609 CD ARG A 95 21.670 10.340 -7.907 1.00 30.39 C ATOM 610 NE ARG A 95 20.289 10.786 -7.910 1.00 34.28 N ATOM 611 CZ ARG A 95 19.931 12.042 -7.974 1.00 38.38 C ATOM 612 NH1 ARG A 95 20.828 13.026 -8.092 1.00 38.99 N ATOM 613 NH2 ARG A 95 18.640 12.320 -7.962 1.00 41.95 N ATOM 614 N PHE A 96 25.134 6.008 -7.745 1.00 23.16 N ATOM 615 CA PHE A 96 26.482 5.370 -7.747 1.00 22.78 C ATOM 616 C PHE A 96 26.988 5.133 -9.179 1.00 24.60 C ATOM 617 O PHE A 96 28.136 5.400 -9.530 1.00 23.29 O ATOM 618 CB PHE A 96 26.490 4.049 -7.014 1.00 23.65 C ATOM 619 CG PHE A 96 26.875 4.172 -5.549 1.00 21.08 C ATOM 620 CD1 PHE A 96 25.896 4.113 -4.561 1.00 23.16 C ATOM 621 CD2 PHE A 96 28.195 4.393 -5.166 1.00 22.16 C ATOM 622 CE1 PHE A 96 26.245 4.250 -3.205 1.00 24.67 C ATOM 623 CE2 PHE A 96 28.512 4.531 -3.806 1.00 22.69 C ATOM 624 CZ PHE A 96 27.566 4.439 -2.859 1.00 22.91 C ATOM 625 N GLU A 97 26.094 4.652 -10.019 1.00 25.82 N ATOM 626 CA GLU A 97 26.444 4.502 -11.427 1.00 26.62 C ATOM 627 C GLU A 97 26.752 5.806 -12.101 1.00 26.37 C ATOM 628 O GLU A 97 27.719 5.894 -12.843 1.00 28.82 O ATOM 629 CB GLU A 97 25.276 3.873 -12.143 1.00 27.64 C ATOM 630 CG GLU A 97 25.053 2.469 -11.686 1.00 30.06 C ATOM 631 CD GLU A 97 23.677 1.981 -12.058 1.00 32.58 C ATOM 632 OE1 GLU A 97 23.526 1.711 -13.278 1.00 29.16 O ATOM 633 OE2 GLU A 97 22.780 1.906 -11.148 1.00 32.12 O ATOM 634 N ARG A 98 25.927 6.806 -11.880 1.00 25.23 N ATOM 635 CA ARG A 98 26.115 8.126 -12.429 1.00 26.33 C ATOM 636 C ARG A 98 27.387 8.819 -11.998 1.00 26.48 C ATOM 637 O ARG A 98 27.926 9.686 -12.738 1.00 27.44 O ATOM 638 CB ARG A 98 24.934 8.987 -12.088 1.00 26.28 C ATOM 639 CG ARG A 98 23.641 8.466 -12.800 1.00 30.13 C ATOM 640 CD ARG A 98 22.389 9.218 -12.449 1.00 33.65 C ATOM 641 NE ARG A 98 22.571 10.663 -12.592 1.00 36.85 N ATOM 642 CZ ARG A 98 21.724 11.581 -12.142 1.00 41.69 C ATOM 643 NH1 ARG A 98 20.597 11.232 -11.520 1.00 40.99 N ATOM 644 NH2 ARG A 98 22.009 12.874 -12.306 1.00 46.30 N ATOM 645 N ALA A 99 27.874 8.420 -10.839 1.00 25.46 N ATOM 646 CA ALA A 99 29.129 8.982 -10.268 1.00 25.34 C ATOM 647 C ALA A 99 30.385 8.183 -10.573 1.00 25.67 C ATOM 648 O ALA A 99 31.472 8.439 -10.036 1.00 24.41 O ATOM 649 CB ALA A 99 28.978 9.117 -8.733 1.00 25.80 C ATOM 650 N ASP A 100 30.275 7.167 -11.399 1.00 25.66 N ATOM 651 CA ASP A 100 31.415 6.299 -11.670 1.00 25.64 C ATOM 652 C ASP A 100 32.541 7.148 -12.232 1.00 24.79 C ATOM 653 O ASP A 100 32.294 8.039 -13.065 1.00 24.24 O ATOM 654 CB ASP A 100 31.026 5.204 -12.652 1.00 26.81 C ATOM 655 CG ASP A 100 32.166 4.325 -12.988 1.00 31.58 C ATOM 656 OD1 ASP A 100 32.652 3.541 -12.112 1.00 31.89 O ATOM 657 OD2 ASP A 100 32.656 4.370 -14.152 1.00 39.00 O ATOM 658 N GLY A 101 33.748 6.920 -11.703 1.00 24.78 N ATOM 659 CA GLY A 101 34.940 7.721 -12.002 1.00 25.16 C ATOM 660 C GLY A 101 35.017 9.089 -11.348 1.00 25.12 C ATOM 661 O GLY A 101 35.919 9.899 -11.596 1.00 23.01 O ATOM 662 N GLY A 102 34.018 9.398 -10.501 1.00 23.68 N ATOM 663 CA GLY A 102 33.932 10.689 -9.881 1.00 23.07 C ATOM 664 C GLY A 102 33.548 10.576 -8.412 1.00 20.45 C ATOM 665 O GLY A 102 33.949 9.643 -7.759 1.00 19.81 O ATOM 666 N THR A 103 32.781 11.532 -7.925 1.00 21.24 N ATOM 667 CA THR A 103 32.420 11.601 -6.508 1.00 20.54 C ATOM 668 C THR A 103 30.912 11.665 -6.311 1.00 20.64 C ATOM 669 O THR A 103 30.209 12.369 -7.040 1.00 19.39 O ATOM 670 CB THR A 103 33.073 12.856 -5.916 1.00 21.26 C ATOM 671 OG1 THR A 103 34.501 12.789 -6.069 1.00 21.50 O ATOM 672 CG2 THR A 103 32.881 13.019 -4.432 1.00 21.25 C ATOM 673 N LEU A 104 30.433 10.980 -5.278 1.00 18.98 N ATOM 674 CA LEU A 104 29.039 11.015 -4.891 1.00 18.08 C ATOM 675 C LEU A 104 28.907 11.640 -3.496 1.00 16.46 C ATOM 676 O LEU A 104 29.563 11.128 -2.552 1.00 16.61 O ATOM 677 CB LEU A 104 28.500 9.601 -4.817 1.00 16.48 C ATOM 678 CG LEU A 104 27.047 9.441 -4.374 1.00 18.29 C ATOM 679 CD1 LEU A 104 26.103 10.319 -5.195 1.00 17.88 C ATOM 680 CD2 LEU A 104 26.584 7.993 -4.337 1.00 17.91 C ATOM 681 N PHE A 105 28.044 12.659 -3.384 1.00 15.32 N ATOM 682 CA PHE A 105 27.808 13.335 -2.132 1.00 16.31 C ATOM 683 C PHE A 105 26.424 12.926 -1.636 1.00 16.95 C ATOM 684 O PHE A 105 25.425 13.237 -2.294 1.00 17.52 O ATOM 685 CB PHE A 105 27.857 14.848 -2.336 1.00 17.23 C ATOM 686 CG PHE A 105 27.393 15.658 -1.156 1.00 17.30 C ATOM 687 CD1 PHE A 105 28.002 15.518 0.101 1.00 17.06 C ATOM 688 CD2 PHE A 105 26.351 16.533 -1.257 1.00 17.65 C ATOM 689 CE1 PHE A 105 27.596 16.280 1.180 1.00 20.94 C ATOM 690 CE2 PHE A 105 25.919 17.251 -0.158 1.00 21.57 C ATOM 691 CZ PHE A 105 26.547 17.147 1.038 1.00 19.06 C ATOM 692 N LEU A 106 26.364 12.298 -0.461 1.00 16.60 N ATOM 693 CA LEU A 106 25.097 11.875 0.148 1.00 16.71 C ATOM 694 C LEU A 106 24.824 12.763 1.350 1.00 16.65 C ATOM 695 O LEU A 106 25.510 12.681 2.319 1.00 14.84 O ATOM 696 CB LEU A 106 25.131 10.405 0.575 1.00 16.51 C ATOM 697 CG LEU A 106 25.404 9.361 -0.475 1.00 18.08 C ATOM 698 CD1 LEU A 106 25.340 8.015 0.085 1.00 22.14 C ATOM 699 CD2 LEU A 106 24.408 9.488 -1.585 1.00 22.59 C ATOM 700 N ASP A 107 23.824 13.651 1.251 1.00 15.94 N ATOM 701 CA ASP A 107 23.444 14.548 2.360 1.00 16.99 C ATOM 702 C ASP A 107 22.391 13.923 3.211 1.00 16.28 C ATOM 703 O ASP A 107 21.716 13.004 2.807 1.00 16.88 O ATOM 704 CB ASP A 107 22.929 15.866 1.789 1.00 17.76 C ATOM 705 CG ASP A 107 23.051 17.022 2.695 1.00 20.46 C ATOM 706 OD1 ASP A 107 23.591 16.979 3.839 1.00 19.75 O ATOM 707 OD2 ASP A 107 22.510 18.105 2.300 1.00 25.34 O ATOM 708 N GLU A 108 22.290 14.384 4.443 1.00 16.91 N ATOM 709 CA GLU A 108 21.345 13.881 5.448 1.00 16.81 C ATOM 710 C GLU A 108 21.435 12.380 5.622 1.00 16.46 C ATOM 711 O GLU A 108 20.444 11.705 5.660 1.00 17.74 O ATOM 712 CB GLU A 108 19.915 14.392 5.207 1.00 17.95 C ATOM 713 CG GLU A 108 19.966 15.926 5.182 1.00 18.14 C ATOM 714 CD GLU A 108 18.607 16.617 5.185 1.00 26.49 C ATOM 715 OE1 GLU A 108 17.773 16.291 6.091 1.00 27.78 O ATOM 716 OE2 GLU A 108 18.420 17.500 4.294 1.00 30.60 O ATOM 717 N LEU A 109 22.660 11.909 5.770 1.00 17.50 N ATOM 718 CA LEU A 109 22.926 10.486 5.852 1.00 19.17 C ATOM 719 C LEU A 109 22.188 9.795 6.982 1.00 18.99 C ATOM 720 O LEU A 109 21.809 8.636 6.844 1.00 18.72 O ATOM 721 CB LEU A 109 24.434 10.288 5.997 1.00 19.83 C ATOM 722 CG LEU A 109 24.931 8.842 6.149 1.00 25.18 C ATOM 723 CD1 LEU A 109 24.753 8.113 4.902 1.00 25.51 C ATOM 724 CD2 LEU A 109 26.382 8.909 6.609 1.00 27.08 C ATOM 725 N ALA A 110 22.043 10.462 8.112 1.00 19.48 N ATOM 726 CA ALA A 110 21.392 9.864 9.295 1.00 18.49 C ATOM 727 C ALA A 110 19.997 9.388 9.012 1.00 19.87 C ATOM 728 O ALA A 110 19.468 8.567 9.745 1.00 20.11 O ATOM 729 CB ALA A 110 21.381 10.860 10.444 1.00 20.14 C ATOM 730 N THR A 111 19.344 9.939 7.980 1.00 17.39 N ATOM 731 CA THR A 111 17.994 9.542 7.634 1.00 18.54 C ATOM 732 C THR A 111 17.930 8.325 6.762 1.00 19.01 C ATOM 733 O THR A 111 16.848 7.852 6.444 1.00 20.54 O ATOM 734 CB THR A 111 17.209 10.702 6.913 1.00 19.39 C ATOM 735 OG1 THR A 111 17.805 10.920 5.632 1.00 19.48 O ATOM 736 CG2 THR A 111 17.321 11.981 7.616 1.00 20.59 C ATOM 737 N ALA A 112 19.070 7.761 6.344 1.00 17.47 N ATOM 738 CA ALA A 112 18.999 6.559 5.525 1.00 15.69 C ATOM 739 C ALA A 112 18.514 5.382 6.394 1.00 18.16 C ATOM 740 O ALA A 112 19.008 5.190 7.517 1.00 19.44 O ATOM 741 CB ALA A 112 20.382 6.239 4.958 1.00 16.94 C ATOM 742 N PRO A 113 17.544 4.617 5.925 1.00 20.17 N ATOM 743 CA PRO A 113 17.089 3.464 6.695 1.00 22.05 C ATOM 744 C PRO A 113 18.170 2.396 6.770 1.00 21.26 C ATOM 745 O PRO A 113 19.096 2.305 5.982 1.00 19.00 O ATOM 746 CB PRO A 113 15.893 2.951 5.878 1.00 22.90 C ATOM 747 CG PRO A 113 15.562 4.035 4.999 1.00 24.55 C ATOM 748 CD PRO A 113 16.805 4.761 4.671 1.00 21.45 C ATOM 749 N MET A 114 17.978 1.491 7.729 1.00 22.23 N ATOM 750 CA MET A 114 19.009 0.513 8.057 1.00 23.81 C ATOM 751 C MET A 114 19.277 -0.401 6.884 1.00 23.89 C ATOM 752 O MET A 114 20.424 -0.753 6.638 1.00 24.16 O ATOM 753 CB MET A 114 18.656 -0.201 9.361 1.00 25.18 C ATOM 754 CG MET A 114 18.725 0.834 10.559 1.00 26.58 C ATOM 755 SD MET A 114 20.374 1.082 11.171 1.00 30.74 S ATOM 756 CE MET A 114 20.791 -0.501 11.927 1.00 31.19 C ATOM 757 N MET A 115 18.270 -0.689 6.066 1.00 24.99 N ATOM 758 CA MET A 115 18.499 -1.504 4.863 1.00 24.84 C ATOM 759 C MET A 115 19.460 -0.834 3.899 1.00 23.45 C ATOM 760 O MET A 115 20.356 -1.472 3.343 1.00 23.94 O ATOM 761 CB MET A 115 17.190 -1.752 4.114 1.00 28.09 C ATOM 762 CG MET A 115 17.357 -2.646 2.878 1.00 32.11 C ATOM 763 SD MET A 115 15.877 -2.628 1.888 1.00 47.70 S ATOM 764 CE MET A 115 16.330 -1.069 0.984 1.00 44.93 C ATOM 765 N VAL A 116 19.245 0.455 3.667 1.00 21.87 N ATOM 766 CA VAL A 116 20.085 1.235 2.756 1.00 19.61 C ATOM 767 C VAL A 116 21.519 1.287 3.282 1.00 19.53 C ATOM 768 O VAL A 116 22.492 1.197 2.527 1.00 19.06 O ATOM 769 CB VAL A 116 19.478 2.636 2.529 1.00 20.14 C ATOM 770 CG1 VAL A 116 20.478 3.534 1.771 1.00 19.77 C ATOM 771 CG2 VAL A 116 18.183 2.523 1.780 1.00 20.47 C ATOM 772 N GLN A 117 21.643 1.445 4.599 1.00 18.25 N ATOM 773 CA GLN A 117 22.941 1.548 5.243 1.00 17.02 C ATOM 774 C GLN A 117 23.776 0.271 5.024 1.00 18.32 C ATOM 775 O GLN A 117 24.958 0.322 4.784 1.00 19.74 O ATOM 776 CB GLN A 117 22.754 1.786 6.730 1.00 17.42 C ATOM 777 CG GLN A 117 22.253 3.148 7.109 1.00 15.76 C ATOM 778 CD GLN A 117 22.098 3.305 8.599 1.00 18.56 C ATOM 779 OE1 GLN A 117 22.961 2.892 9.339 1.00 18.53 O ATOM 780 NE2 GLN A 117 21.005 3.937 9.033 1.00 17.87 N ATOM 781 N GLU A 118 23.128 -0.889 5.165 1.00 21.07 N ATOM 782 CA GLU A 118 23.842 -2.163 5.005 1.00 23.04 C ATOM 783 C GLU A 118 24.225 -2.323 3.583 1.00 23.65 C ATOM 784 O GLU A 118 25.373 -2.639 3.308 1.00 25.41 O ATOM 785 CB GLU A 118 23.036 -3.361 5.517 1.00 24.24 C ATOM 786 CG GLU A 118 23.899 -4.657 5.643 1.00 28.12 C ATOM 787 CD GLU A 118 23.891 -5.426 4.368 1.00 30.79 C ATOM 788 OE1 GLU A 118 23.018 -5.120 3.521 1.00 34.42 O ATOM 789 OE2 GLU A 118 24.739 -6.322 4.198 1.00 29.89 O ATOM 790 N LYS A 119 23.345 -1.975 2.661 1.00 24.59 N ATOM 791 CA LYS A 119 23.710 -2.016 1.232 1.00 25.52 C ATOM 792 C LYS A 119 24.820 -1.054 0.845 1.00 24.16 C ATOM 793 O LYS A 119 25.630 -1.328 -0.010 1.00 22.94 O ATOM 794 CB LYS A 119 22.488 -1.772 0.369 1.00 26.75 C ATOM 795 CG LYS A 119 21.460 -2.925 0.434 1.00 32.96 C ATOM 796 CD LYS A 119 20.259 -2.609 -0.449 1.00 37.29 C ATOM 797 CE LYS A 119 20.540 -2.815 -1.929 1.00 39.63 C ATOM 798 NZ LYS A 119 19.212 -2.681 -2.649 1.00 42.77 N ATOM 799 N LEU A 120 24.864 0.087 1.502 1.00 22.73 N ATOM 800 CA LEU A 120 25.861 1.065 1.224 1.00 21.19 C ATOM 801 C LEU A 120 27.239 0.545 1.717 1.00 21.97 C ATOM 802 O LEU A 120 28.246 0.714 1.040 1.00 21.18 O ATOM 803 CB LEU A 120 25.443 2.423 1.908 1.00 21.54 C ATOM 804 CG LEU A 120 26.462 3.509 1.907 1.00 21.10 C ATOM 805 CD1 LEU A 120 26.745 3.937 0.466 1.00 23.06 C ATOM 806 CD2 LEU A 120 25.916 4.771 2.665 1.00 24.55 C ATOM 807 N LEU A 121 27.280 -0.112 2.875 1.00 19.84 N ATOM 808 CA LEU A 121 28.541 -0.596 3.414 1.00 22.18 C ATOM 809 C LEU A 121 29.111 -1.597 2.414 1.00 23.73 C ATOM 810 O LEU A 121 30.324 -1.634 2.130 1.00 25.35 O ATOM 811 CB LEU A 121 28.328 -1.339 4.775 1.00 22.89 C ATOM 812 CG LEU A 121 29.629 -1.882 5.408 1.00 23.88 C ATOM 813 CD1 LEU A 121 30.696 -0.911 5.563 1.00 25.27 C ATOM 814 CD2 LEU A 121 29.327 -2.536 6.778 1.00 26.71 C ATOM 815 N ARG A 122 28.215 -2.372 1.832 1.00 24.98 N ATOM 816 CA ARG A 122 28.647 -3.401 0.870 1.00 26.07 C ATOM 817 C ARG A 122 29.284 -2.767 -0.361 1.00 26.91 C ATOM 818 O ARG A 122 30.313 -3.197 -0.834 1.00 27.72 O ATOM 819 CB ARG A 122 27.491 -4.310 0.482 1.00 24.38 C ATOM 820 N VAL A 123 28.668 -1.711 -0.859 1.00 28.17 N ATOM 821 CA VAL A 123 29.182 -1.033 -2.011 1.00 27.59 C ATOM 822 C VAL A 123 30.567 -0.507 -1.679 1.00 29.57 C ATOM 823 O VAL A 123 31.442 -0.522 -2.541 1.00 30.60 O ATOM 824 CB VAL A 123 28.279 0.109 -2.474 1.00 27.97 C ATOM 825 CG1 VAL A 123 28.882 0.790 -3.636 1.00 29.05 C ATOM 826 CG2 VAL A 123 26.932 -0.399 -2.880 1.00 28.09 C ATOM 827 N ILE A 124 30.760 -0.018 -0.454 1.00 28.31 N ATOM 828 CA ILE A 124 32.023 0.561 -0.035 1.00 29.93 C ATOM 829 C ILE A 124 33.091 -0.510 0.072 1.00 33.03 C ATOM 830 O ILE A 124 34.224 -0.278 -0.326 1.00 33.44 O ATOM 831 CB ILE A 124 31.890 1.264 1.326 1.00 29.36 C ATOM 832 CG1 ILE A 124 30.950 2.457 1.185 1.00 26.52 C ATOM 833 CG2 ILE A 124 33.280 1.761 1.863 1.00 31.70 C ATOM 834 CD1 ILE A 124 30.623 3.071 2.561 1.00 23.67 C ATOM 835 N GLU A 125 32.727 -1.658 0.625 1.00 35.62 N ATOM 836 CA GLU A 125 33.727 -2.686 0.957 1.00 38.15 C ATOM 837 C GLU A 125 34.072 -3.490 -0.290 1.00 39.87 C ATOM 838 O GLU A 125 35.258 -3.729 -0.515 1.00 40.72 O ATOM 839 CB GLU A 125 33.289 -3.562 2.177 1.00 38.89 C ATOM 840 CG GLU A 125 33.045 -2.734 3.466 1.00 39.15 C ATOM 841 CD GLU A 125 33.279 -3.483 4.799 1.00 37.92 C ATOM 842 OE1 GLU A 125 32.661 -4.545 4.958 1.00 36.77 O ATOM 843 OE2 GLU A 125 34.045 -3.000 5.678 1.00 34.14 O ATOM 844 N TYR A 126 33.074 -3.804 -1.129 1.00 41.80 N ATOM 845 CA TYR A 126 33.255 -4.619 -2.356 1.00 43.78 C ATOM 846 C TYR A 126 33.413 -3.839 -3.667 1.00 43.68 C ATOM 847 O TYR A 126 33.977 -4.359 -4.621 1.00 43.76 O ATOM 848 CB TYR A 126 32.100 -5.631 -2.550 1.00 44.36 C ATOM 849 CG TYR A 126 32.087 -6.765 -1.549 1.00 49.86 C ATOM 850 CD1 TYR A 126 30.892 -7.340 -1.146 1.00 55.53 C ATOM 851 CD2 TYR A 126 33.284 -7.255 -0.986 1.00 54.06 C ATOM 852 CE1 TYR A 126 30.879 -8.380 -0.207 1.00 58.49 C ATOM 853 CE2 TYR A 126 33.282 -8.273 -0.057 1.00 56.98 C ATOM 854 CZ TYR A 126 32.078 -8.833 0.330 1.00 58.91 C ATOM 855 OH TYR A 126 32.079 -9.833 1.258 1.00 60.42 O ATOM 856 N GLY A 127 32.906 -2.617 -3.739 1.00 43.41 N ATOM 857 CA GLY A 127 32.986 -1.834 -4.953 1.00 43.06 C ATOM 858 C GLY A 127 32.060 -2.236 -6.091 1.00 43.78 C ATOM 859 O GLY A 127 32.377 -1.965 -7.253 1.00 42.34 O ATOM 860 N GLU A 128 30.921 -2.862 -5.779 1.00 44.20 N ATOM 861 CA GLU A 128 29.933 -3.229 -6.792 1.00 45.40 C ATOM 862 C GLU A 128 28.510 -3.221 -6.278 1.00 46.55 C ATOM 863 O GLU A 128 28.263 -3.451 -5.102 1.00 46.54 O ATOM 864 CB GLU A 128 30.206 -4.625 -7.384 1.00 45.45 C ATOM 865 CG GLU A 128 30.257 -5.753 -6.353 1.00 46.88 C ATOM 866 CD GLU A 128 30.713 -7.074 -6.971 1.00 46.79 C ATOM 867 OE1 GLU A 128 31.884 -7.148 -7.393 1.00 49.85 O ATOM 868 OE2 GLU A 128 29.906 -8.024 -7.059 1.00 46.60 O ATOM 869 N LEU A 129 27.581 -2.998 -7.201 1.00 48.31 N ATOM 870 CA LEU A 129 26.149 -3.019 -6.920 1.00 50.42 C ATOM 871 C LEU A 129 25.660 -4.421 -7.168 1.00 52.45 C ATOM 872 O LEU A 129 26.189 -5.098 -8.023 1.00 52.91 O ATOM 873 CB LEU A 129 25.425 -2.032 -7.843 1.00 49.70 C ATOM 874 CG LEU A 129 25.992 -0.612 -7.818 1.00 49.48 C ATOM 875 CD1 LEU A 129 25.333 0.252 -8.884 1.00 48.99 C ATOM 876 CD2 LEU A 129 25.826 0.012 -6.454 1.00 49.75 C ATOM 877 N GLU A 130 24.671 -4.883 -6.429 1.00 55.42 N ATOM 878 CA GLU A 130 24.101 -6.186 -6.754 1.00 58.24 C ATOM 879 C GLU A 130 23.034 -6.046 -7.832 1.00 59.64 C ATOM 880 O GLU A 130 22.392 -5.007 -7.968 1.00 58.99 O ATOM 881 CB GLU A 130 23.531 -6.876 -5.524 1.00 58.86 C ATOM 882 CG GLU A 130 23.389 -8.378 -5.700 1.00 61.95 C ATOM 883 CD GLU A 130 23.321 -9.117 -4.372 1.00 65.40 C ATOM 884 OE1 GLU A 130 22.704 -8.578 -3.417 1.00 67.79 O ATOM 885 OE2 GLU A 130 23.884 -10.235 -4.285 1.00 67.10 O ATOM 886 N ARG A 131 22.864 -7.104 -8.614 1.00 62.45 N ATOM 887 CA ARG A 131 21.924 -7.069 -9.719 1.00 64.39 C ATOM 888 C ARG A 131 21.114 -8.364 -9.791 1.00 64.81 C ATOM 889 O ARG A 131 21.597 -9.458 -9.430 1.00 65.10 O ATOM 890 CB ARG A 131 22.664 -6.783 -11.042 1.00 65.41 C ATOM 891 CG ARG A 131 22.496 -5.339 -11.604 1.00 69.12 C ATOM 892 CD ARG A 131 22.423 -5.283 -13.148 1.00 74.61 C ATOM 893 NE ARG A 131 22.530 -3.937 -13.732 1.00 78.99 N ATOM 894 CZ ARG A 131 22.635 -3.655 -15.053 1.00 82.09 C ATOM 895 NH1 ARG A 131 22.635 -4.600 -15.991 1.00 81.87 N ATOM 896 NH2 ARG A 131 22.731 -2.390 -15.441 1.00 84.26 N ATOM 897 N VAL A 132 19.866 -8.208 -10.239 1.00 64.81 N ATOM 898 CA VAL A 132 18.957 -9.320 -10.488 1.00 64.84 C ATOM 899 C VAL A 132 18.784 -9.430 -12.018 1.00 63.50 C ATOM 900 O VAL A 132 19.401 -8.676 -12.777 1.00 63.84 O ATOM 901 CB VAL A 132 17.602 -9.088 -9.745 1.00 65.11 C ATOM 902 CG1 VAL A 132 16.788 -10.382 -9.615 1.00 65.99 C ATOM 903 CG2 VAL A 132 17.859 -8.488 -8.360 1.00 65.93 C ATOM 904 N GLY A 133 18.002 -10.407 -12.467 1.00 61.88 N ATOM 905 CA GLY A 133 17.498 -10.427 -13.835 1.00 60.15 C ATOM 906 C GLY A 133 18.440 -10.948 -14.906 1.00 58.16 C ATOM 907 O GLY A 133 18.305 -10.530 -16.083 1.00 58.65 O ATOM 908 N GLY A 134 19.379 -11.830 -14.527 1.00 54.72 N ATOM 909 CA GLY A 134 20.379 -12.333 -15.470 1.00 52.27 C ATOM 910 C GLY A 134 21.563 -11.402 -15.684 1.00 50.11 C ATOM 911 O GLY A 134 22.546 -11.760 -16.299 1.00 46.36 O ATOM 912 N SER A 135 21.457 -10.195 -15.128 1.00 48.65 N ATOM 913 CA SER A 135 22.495 -9.179 -15.235 1.00 48.37 C ATOM 914 C SER A 135 23.624 -9.420 -14.227 1.00 46.67 C ATOM 915 O SER A 135 23.371 -9.717 -13.066 1.00 46.58 O ATOM 916 CB SER A 135 21.889 -7.801 -14.966 1.00 48.78 C ATOM 917 OG SER A 135 20.803 -7.483 -15.838 1.00 49.77 O ATOM 918 N GLN A 136 24.859 -9.262 -14.675 1.00 45.01 N ATOM 919 CA GLN A 136 26.025 -9.358 -13.804 1.00 44.04 C ATOM 920 C GLN A 136 26.077 -8.129 -12.853 1.00 43.00 C ATOM 921 O GLN A 136 25.539 -7.076 -13.197 1.00 40.87 O ATOM 922 CB GLN A 136 27.315 -9.395 -14.654 1.00 44.48 C ATOM 923 CG GLN A 136 27.363 -10.526 -15.707 1.00 44.94 C ATOM 924 CD GLN A 136 27.131 -11.915 -15.113 1.00 45.25 C ATOM 925 OE1 GLN A 136 26.641 -12.816 -15.806 1.00 44.85 O ATOM 926 NE2 GLN A 136 27.505 -12.095 -13.844 1.00 44.35 N ATOM 927 N PRO A 137 26.728 -8.269 -11.690 1.00 42.82 N ATOM 928 CA PRO A 137 26.861 -7.146 -10.748 1.00 42.61 C ATOM 929 C PRO A 137 27.536 -5.987 -11.461 1.00 41.84 C ATOM 930 O PRO A 137 28.396 -6.263 -12.304 1.00 41.00 O ATOM 931 CB PRO A 137 27.765 -7.696 -9.629 1.00 43.12 C ATOM 932 CG PRO A 137 27.633 -9.183 -9.712 1.00 43.54 C ATOM 933 CD PRO A 137 27.398 -9.483 -11.182 1.00 43.12 C ATOM 934 N LEU A 138 27.099 -4.755 -11.185 1.00 40.36 N ATOM 935 CA LEU A 138 27.684 -3.564 -11.775 1.00 39.87 C ATOM 936 C LEU A 138 28.835 -3.070 -10.911 1.00 38.79 C ATOM 937 O LEU A 138 28.695 -2.813 -9.709 1.00 37.35 O ATOM 938 CB LEU A 138 26.652 -2.451 -11.962 1.00 40.34 C ATOM 939 CG LEU A 138 25.657 -2.532 -13.126 1.00 42.99 C ATOM 940 CD1 LEU A 138 24.658 -1.380 -12.968 1.00 44.32 C ATOM 941 CD2 LEU A 138 26.332 -2.487 -14.509 1.00 43.96 C ATOM 942 N GLN A 139 29.989 -2.943 -11.539 1.00 37.63 N ATOM 943 CA GLN A 139 31.182 -2.464 -10.886 1.00 37.70 C ATOM 944 C GLN A 139 31.132 -0.936 -10.807 1.00 36.88 C ATOM 945 O GLN A 139 30.765 -0.280 -11.780 1.00 36.69 O ATOM 946 CB GLN A 139 32.408 -2.907 -11.681 1.00 38.45 C ATOM 947 CG GLN A 139 32.734 -4.342 -11.445 1.00 40.01 C ATOM 948 CD GLN A 139 33.149 -4.608 -10.051 1.00 43.39 C ATOM 949 OE1 GLN A 139 32.785 -5.643 -9.480 1.00 49.69 O ATOM 950 NE2 GLN A 139 33.898 -3.683 -9.464 1.00 47.91 N ATOM 951 N VAL A 140 31.455 -0.360 -9.644 1.00 34.95 N ATOM 952 CA VAL A 140 31.504 1.077 -9.573 1.00 33.56 C ATOM 953 C VAL A 140 32.764 1.524 -8.873 1.00 31.38 C ATOM 954 O VAL A 140 33.303 0.832 -8.006 1.00 30.63 O ATOM 955 CB VAL A 140 30.251 1.683 -8.899 1.00 34.36 C ATOM 956 CG1 VAL A 140 29.049 1.515 -9.820 1.00 36.27 C ATOM 957 CG2 VAL A 140 30.001 1.058 -7.521 1.00 35.25 C ATOM 958 N ASN A 141 33.207 2.703 -9.255 1.00 29.11 N ATOM 959 CA ASN A 141 34.437 3.256 -8.739 1.00 27.59 C ATOM 960 C ASN A 141 34.131 4.710 -8.390 1.00 24.77 C ATOM 961 O ASN A 141 34.213 5.610 -9.235 1.00 22.45 O ATOM 962 CB ASN A 141 35.539 3.185 -9.804 1.00 28.12 C ATOM 963 CG ASN A 141 36.799 3.921 -9.372 1.00 31.56 C ATOM 964 OD1 ASN A 141 37.054 4.101 -8.182 1.00 31.05 O ATOM 965 ND2 ASN A 141 37.593 4.349 -10.348 1.00 36.94 N ATOM 966 N VAL A 142 33.732 4.920 -7.138 1.00 22.63 N ATOM 967 CA VAL A 142 33.131 6.188 -6.716 1.00 21.38 C ATOM 968 C VAL A 142 33.788 6.587 -5.394 1.00 19.24 C ATOM 969 O VAL A 142 33.989 5.766 -4.562 1.00 19.89 O ATOM 970 CB VAL A 142 31.623 6.034 -6.508 1.00 21.91 C ATOM 971 CG1 VAL A 142 31.004 7.234 -5.840 1.00 21.39 C ATOM 972 CG2 VAL A 142 30.898 5.759 -7.838 1.00 24.45 C ATOM 973 N ARG A 143 34.187 7.849 -5.284 1.00 19.34 N ATOM 974 CA ARG A 143 34.710 8.402 -4.049 1.00 18.38 C ATOM 975 C ARG A 143 33.488 8.987 -3.349 1.00 17.88 C ATOM 976 O ARG A 143 32.732 9.798 -3.920 1.00 16.62 O ATOM 977 CB ARG A 143 35.749 9.479 -4.334 1.00 17.93 C ATOM 978 CG ARG A 143 36.558 9.902 -3.065 1.00 16.44 C ATOM 979 CD ARG A 143 35.958 11.005 -2.235 1.00 18.74 C ATOM 980 NE ARG A 143 36.871 11.252 -1.140 1.00 17.18 N ATOM 981 CZ ARG A 143 37.957 12.007 -1.186 1.00 17.34 C ATOM 982 NH1 ARG A 143 38.277 12.782 -2.227 1.00 18.31 N ATOM 983 NH2 ARG A 143 38.743 12.022 -0.092 1.00 18.90 N ATOM 984 N LEU A 144 33.278 8.536 -2.122 1.00 16.41 N ATOM 985 CA LEU A 144 32.100 8.939 -1.370 1.00 16.48 C ATOM 986 C LEU A 144 32.357 10.063 -0.362 1.00 15.51 C ATOM 987 O LEU A 144 33.317 10.068 0.400 1.00 14.73 O ATOM 988 CB LEU A 144 31.569 7.739 -0.584 1.00 17.32 C ATOM 989 CG LEU A 144 30.207 7.744 0.062 1.00 20.67 C ATOM 990 CD1 LEU A 144 29.098 7.834 -0.992 1.00 18.83 C ATOM 991 CD2 LEU A 144 30.066 6.475 0.905 1.00 25.00 C ATOM 992 N VAL A 145 31.447 11.034 -0.349 1.00 14.30 N ATOM 993 CA VAL A 145 31.420 12.080 0.675 1.00 14.28 C ATOM 994 C VAL A 145 30.017 12.079 1.239 1.00 13.39 C ATOM 995 O VAL A 145 29.041 12.122 0.480 1.00 14.80 O ATOM 996 CB VAL A 145 31.741 13.469 0.086 1.00 12.80 C ATOM 997 CG1 VAL A 145 31.722 14.514 1.136 1.00 15.32 C ATOM 998 CG2 VAL A 145 33.102 13.411 -0.588 1.00 15.40 C ATOM 999 N CYS A 146 29.875 11.982 2.542 1.00 14.04 N ATOM 1000 CA CYS A 146 28.563 12.071 3.170 1.00 13.22 C ATOM 1001 C CYS A 146 28.513 13.251 4.147 1.00 12.63 C ATOM 1002 O CYS A 146 29.533 13.718 4.644 1.00 13.94 O ATOM 1003 CB CYS A 146 28.245 10.801 3.922 1.00 14.40 C ATOM 1004 SG CYS A 146 28.265 9.296 2.930 1.00 16.41 S ATOM 1005 N ALA A 147 27.306 13.737 4.435 1.00 14.51 N ATOM 1006 CA ALA A 147 27.097 14.780 5.425 1.00 13.68 C ATOM 1007 C ALA A 147 25.920 14.553 6.314 1.00 16.02 C ATOM 1008 O ALA A 147 24.958 13.941 5.907 1.00 14.62 O ATOM 1009 CB ALA A 147 26.925 16.126 4.707 1.00 15.92 C ATOM 1010 N THR A 148 26.022 15.073 7.534 1.00 15.24 N ATOM 1011 CA THR A 148 24.906 15.067 8.491 1.00 17.58 C ATOM 1012 C THR A 148 25.125 16.076 9.612 1.00 19.23 C ATOM 1013 O THR A 148 26.201 16.591 9.769 1.00 17.48 O ATOM 1014 CB THR A 148 24.808 13.648 9.082 1.00 18.66 C ATOM 1015 OG1 THR A 148 23.731 13.575 10.008 1.00 20.90 O ATOM 1016 CG2 THR A 148 26.012 13.375 9.887 1.00 17.56 C ATOM 1017 N ASN A 149 24.061 16.388 10.376 1.00 21.78 N ATOM 1018 CA ASN A 149 24.279 17.037 11.654 1.00 22.85 C ATOM 1019 C ASN A 149 23.858 16.225 12.874 1.00 24.20 C ATOM 1020 O ASN A 149 23.914 16.743 14.005 1.00 25.66 O ATOM 1021 CB ASN A 149 23.590 18.383 11.713 1.00 25.59 C ATOM 1022 CG ASN A 149 24.106 19.247 12.847 1.00 25.33 C ATOM 1023 OD1 ASN A 149 25.341 19.334 13.115 1.00 29.15 O ATOM 1024 ND2 ASN A 149 23.160 19.934 13.526 1.00 34.24 N ATOM 1025 N ALA A 150 23.476 14.959 12.638 1.00 20.80 N ATOM 1026 CA ALA A 150 23.153 14.017 13.686 1.00 21.15 C ATOM 1027 C ALA A 150 24.361 13.616 14.464 1.00 21.46 C ATOM 1028 O ALA A 150 25.488 13.721 13.962 1.00 21.68 O ATOM 1029 CB ALA A 150 22.581 12.797 13.059 1.00 20.27 C ATOM 1030 N ASP A 151 24.115 13.054 15.649 1.00 21.20 N ATOM 1031 CA ASP A 151 25.123 12.431 16.468 1.00 22.30 C ATOM 1032 C ASP A 151 25.138 10.972 16.117 1.00 20.69 C ATOM 1033 O ASP A 151 24.376 10.205 16.637 1.00 20.44 O ATOM 1034 CB ASP A 151 24.754 12.594 17.923 1.00 23.00 C ATOM 1035 CG ASP A 151 25.801 12.095 18.859 1.00 28.53 C ATOM 1036 OD1 ASP A 151 26.621 11.218 18.482 1.00 26.35 O ATOM 1037 OD2 ASP A 151 25.811 12.499 20.041 1.00 33.46 O ATOM 1038 N LEU A 152 25.923 10.612 15.117 1.00 20.81 N ATOM 1039 CA LEU A 152 25.934 9.239 14.616 1.00 18.86 C ATOM 1040 C LEU A 152 26.332 8.221 15.638 1.00 19.90 C ATOM 1041 O LEU A 152 25.715 7.155 15.719 1.00 19.13 O ATOM 1042 CB LEU A 152 26.749 9.137 13.321 1.00 18.26 C ATOM 1043 CG LEU A 152 26.163 9.852 12.098 1.00 17.51 C ATOM 1044 CD1 LEU A 152 27.085 9.694 10.867 1.00 23.24 C ATOM 1045 CD2 LEU A 152 24.796 9.377 11.657 1.00 22.52 C ATOM 1046 N PRO A 153 27.351 8.481 16.444 1.00 21.56 N ATOM 1047 CA PRO A 153 27.646 7.540 17.520 1.00 22.21 C ATOM 1048 C PRO A 153 26.430 7.308 18.440 1.00 20.97 C ATOM 1049 O PRO A 153 26.203 6.192 18.812 1.00 21.29 O ATOM 1050 CB PRO A 153 28.799 8.223 18.269 1.00 23.53 C ATOM 1051 CG PRO A 153 29.446 9.119 17.267 1.00 24.48 C ATOM 1052 CD PRO A 153 28.369 9.562 16.315 1.00 22.51 C ATOM 1053 N ALA A 154 25.648 8.342 18.745 1.00 20.94 N ATOM 1054 CA ALA A 154 24.458 8.187 19.561 1.00 19.88 C ATOM 1055 C ALA A 154 23.424 7.359 18.835 1.00 19.61 C ATOM 1056 O ALA A 154 22.762 6.511 19.432 1.00 22.03 O ATOM 1057 CB ALA A 154 23.898 9.543 19.938 1.00 20.73 C ATOM 1058 N MET A 155 23.312 7.524 17.532 1.00 17.05 N ATOM 1059 CA MET A 155 22.406 6.661 16.802 1.00 18.07 C ATOM 1060 C MET A 155 22.830 5.167 16.762 1.00 17.92 C ATOM 1061 O MET A 155 21.996 4.253 16.766 1.00 18.60 O ATOM 1062 CB MET A 155 22.195 7.215 15.420 1.00 18.04 C ATOM 1063 CG MET A 155 21.563 8.506 15.372 1.00 19.64 C ATOM 1064 SD MET A 155 21.250 9.101 13.687 1.00 20.33 S ATOM 1065 CE MET A 155 19.975 8.061 13.200 1.00 22.33 C ATOM 1066 N VAL A 156 24.127 4.906 16.656 1.00 18.24 N ATOM 1067 CA VAL A 156 24.624 3.548 16.752 1.00 19.54 C ATOM 1068 C VAL A 156 24.105 2.950 18.066 1.00 20.01 C ATOM 1069 O VAL A 156 23.631 1.824 18.110 1.00 20.40 O ATOM 1070 CB VAL A 156 26.105 3.508 16.679 1.00 20.08 C ATOM 1071 CG1 VAL A 156 26.654 2.158 17.060 1.00 22.63 C ATOM 1072 CG2 VAL A 156 26.575 3.949 15.259 1.00 19.64 C ATOM 1073 N ASN A 157 24.226 3.684 19.143 1.00 21.90 N ATOM 1074 CA ASN A 157 23.858 3.136 20.451 1.00 23.41 C ATOM 1075 C ASN A 157 22.389 2.820 20.529 1.00 23.64 C ATOM 1076 O ASN A 157 21.965 1.871 21.196 1.00 23.65 O ATOM 1077 CB ASN A 157 24.192 4.113 21.582 1.00 24.25 C ATOM 1078 CG ASN A 157 25.657 4.188 21.886 1.00 28.23 C ATOM 1079 OD1 ASN A 157 26.446 3.311 21.518 1.00 32.54 O ATOM 1080 ND2 ASN A 157 26.044 5.259 22.560 1.00 30.61 N ATOM 1081 N GLU A 158 21.602 3.623 19.858 1.00 24.13 N ATOM 1082 CA GLU A 158 20.165 3.416 19.820 1.00 26.34 C ATOM 1083 C GLU A 158 19.743 2.338 18.842 1.00 25.75 C ATOM 1084 O GLU A 158 18.605 1.928 18.859 1.00 28.65 O ATOM 1085 CB GLU A 158 19.505 4.721 19.419 1.00 27.64 C ATOM 1086 CG GLU A 158 19.895 5.784 20.399 1.00 34.81 C ATOM 1087 CD GLU A 158 19.019 6.985 20.371 1.00 44.13 C ATOM 1088 OE1 GLU A 158 19.379 7.935 21.127 1.00 51.21 O ATOM 1089 OE2 GLU A 158 18.012 6.978 19.612 1.00 48.19 O ATOM 1090 N GLY A 159 20.623 1.893 17.965 1.00 24.71 N ATOM 1091 CA GLY A 159 20.239 0.885 16.987 1.00 23.82 C ATOM 1092 C GLY A 159 19.691 1.457 15.675 1.00 23.59 C ATOM 1093 O GLY A 159 19.162 0.675 14.837 1.00 24.21 O ATOM 1094 N THR A 160 19.817 2.767 15.477 1.00 21.00 N ATOM 1095 CA THR A 160 19.343 3.479 14.259 1.00 21.01 C ATOM 1096 C THR A 160 20.392 3.837 13.248 1.00 20.49 C ATOM 1097 O THR A 160 20.084 4.384 12.176 1.00 19.62 O ATOM 1098 CB THR A 160 18.566 4.715 14.604 1.00 22.13 C ATOM 1099 OG1 THR A 160 19.315 5.549 15.487 1.00 21.62 O ATOM 1100 CG2 THR A 160 17.367 4.314 15.367 1.00 23.78 C ATOM 1101 N PHE A 161 21.643 3.543 13.531 1.00 17.58 N ATOM 1102 CA PHE A 161 22.700 3.670 12.553 1.00 16.39 C ATOM 1103 C PHE A 161 23.645 2.517 12.748 1.00 17.95 C ATOM 1104 O PHE A 161 23.901 2.082 13.867 1.00 17.88 O ATOM 1105 CB PHE A 161 23.459 5.003 12.660 1.00 16.46 C ATOM 1106 CG PHE A 161 24.161 5.420 11.390 1.00 15.62 C ATOM 1107 CD1 PHE A 161 23.463 6.092 10.374 1.00 15.82 C ATOM 1108 CD2 PHE A 161 25.481 5.103 11.181 1.00 15.53 C ATOM 1109 CE1 PHE A 161 24.097 6.403 9.204 1.00 16.05 C ATOM 1110 CE2 PHE A 161 26.111 5.427 10.037 1.00 16.14 C ATOM 1111 CZ PHE A 161 25.426 6.101 9.030 1.00 18.32 C ATOM 1112 N ARG A 162 24.186 2.014 11.653 1.00 17.19 N ATOM 1113 CA ARG A 162 25.068 0.834 11.697 1.00 18.15 C ATOM 1114 C ARG A 162 26.450 1.192 12.190 1.00 18.36 C ATOM 1115 O ARG A 162 27.108 2.063 11.692 1.00 17.70 O ATOM 1116 CB ARG A 162 25.099 0.113 10.339 1.00 18.66 C ATOM 1117 CG ARG A 162 23.813 -0.538 9.929 1.00 20.50 C ATOM 1118 CD ARG A 162 23.962 -1.478 8.777 1.00 26.36 C ATOM 1119 NE ARG A 162 24.786 -2.637 9.220 1.00 28.65 N ATOM 1120 CZ ARG A 162 24.301 -3.784 9.694 1.00 28.59 C ATOM 1121 NH1 ARG A 162 22.985 -4.071 9.717 1.00 30.30 N ATOM 1122 NH2 ARG A 162 25.148 -4.688 10.113 1.00 28.34 N ATOM 1123 N ALA A 163 26.900 0.490 13.224 1.00 20.18 N ATOM 1124 CA ALA A 163 28.238 0.692 13.754 1.00 19.95 C ATOM 1125 C ALA A 163 29.225 0.316 12.646 1.00 20.80 C ATOM 1126 O ALA A 163 30.230 0.966 12.452 1.00 20.79 O ATOM 1127 CB ALA A 163 28.458 -0.204 14.992 1.00 21.71 C ATOM 1128 N ASP A 164 28.950 -0.749 11.908 1.00 21.20 N ATOM 1129 CA ASP A 164 29.962 -1.174 10.914 1.00 21.73 C ATOM 1130 C ASP A 164 30.127 -0.134 9.830 1.00 21.96 C ATOM 1131 O ASP A 164 31.226 0.223 9.424 1.00 21.87 O ATOM 1132 CB ASP A 164 29.709 -2.578 10.323 1.00 22.17 C ATOM 1133 CG ASP A 164 28.295 -2.862 9.917 1.00 25.74 C ATOM 1134 OD1 ASP A 164 27.412 -1.977 9.801 1.00 23.63 O ATOM 1135 OD2 ASP A 164 27.945 -4.042 9.621 1.00 26.70 O ATOM 1136 N LEU A 165 29.008 0.399 9.367 1.00 19.06 N ATOM 1137 CA LEU A 165 29.066 1.511 8.423 1.00 19.33 C ATOM 1138 C LEU A 165 29.825 2.717 8.906 1.00 20.61 C ATOM 1139 O LEU A 165 30.610 3.305 8.186 1.00 20.87 O ATOM 1140 CB LEU A 165 27.657 1.915 7.999 1.00 17.41 C ATOM 1141 CG LEU A 165 27.587 3.096 7.034 1.00 16.76 C ATOM 1142 CD1 LEU A 165 28.278 2.803 5.786 1.00 19.52 C ATOM 1143 CD2 LEU A 165 26.111 3.373 6.727 1.00 16.63 C ATOM 1144 N LEU A 166 29.574 3.169 10.118 1.00 22.67 N ATOM 1145 CA LEU A 166 30.247 4.341 10.647 1.00 24.40 C ATOM 1146 C LEU A 166 31.741 3.941 10.929 1.00 27.77 C ATOM 1147 O LEU A 166 32.562 4.786 10.786 1.00 32.39 O ATOM 1148 CB LEU A 166 29.553 4.818 11.948 1.00 23.88 C ATOM 1149 CG LEU A 166 30.101 6.065 12.592 1.00 24.69 C ATOM 1150 CD1 LEU A 166 29.857 7.248 11.702 1.00 27.67 C ATOM 1151 CD2 LEU A 166 29.478 6.252 14.012 1.00 22.87 C ATOM 1152 N ASP A 167 32.043 2.667 11.203 1.00 31.54 N ATOM 1153 CA ASP A 167 33.450 2.146 11.401 1.00 33.01 C ATOM 1154 C ASP A 167 34.242 2.308 10.086 1.00 35.23 C ATOM 1155 O ASP A 167 35.471 2.179 10.111 1.00 35.67 O ATOM 1156 CB ASP A 167 33.490 0.614 11.757 1.00 34.39 C ATOM 1157 CG ASP A 167 33.330 0.282 13.286 1.00 33.50 C ATOM 1158 OD1 ASP A 167 33.487 1.206 14.135 1.00 35.45 O ATOM 1159 OD2 ASP A 167 33.000 -0.887 13.704 1.00 34.24 O ATOM 1160 N ARG A 168 33.567 2.562 8.955 1.00 34.84 N ATOM 1161 CA ARG A 168 34.211 2.694 7.636 1.00 36.33 C ATOM 1162 C ARG A 168 34.017 4.076 6.969 1.00 35.56 C ATOM 1163 O ARG A 168 34.970 4.693 6.466 1.00 34.75 O ATOM 1164 CB ARG A 168 33.658 1.592 6.738 1.00 37.24 C ATOM 1165 CG ARG A 168 34.292 1.522 5.377 1.00 42.57 C ATOM 1166 CD ARG A 168 35.757 1.174 5.447 1.00 44.20 C ATOM 1167 NE ARG A 168 36.346 0.867 4.152 1.00 47.25 N ATOM 1168 CZ ARG A 168 36.302 -0.321 3.581 1.00 52.35 C ATOM 1169 NH1 ARG A 168 35.682 -1.347 4.159 1.00 52.33 N ATOM 1170 NH2 ARG A 168 36.884 -0.493 2.403 1.00 56.09 N ATOM 1171 N LEU A 169 32.794 4.610 7.017 1.00 33.49 N ATOM 1172 CA LEU A 169 32.525 5.906 6.420 1.00 34.35 C ATOM 1173 C LEU A 169 33.395 6.971 6.970 1.00 31.44 C ATOM 1174 O LEU A 169 33.830 7.807 6.227 1.00 36.08 O ATOM 1175 CB LEU A 169 31.077 6.436 6.633 1.00 33.19 C ATOM 1176 CG LEU A 169 30.053 5.986 5.650 1.00 35.97 C ATOM 1177 CD1 LEU A 169 28.814 6.717 5.959 1.00 33.93 C ATOM 1178 CD2 LEU A 169 30.539 6.171 4.184 1.00 37.33 C ATOM 1179 N ALA A 170 33.606 6.989 8.275 1.00 30.22 N ATOM 1180 CA ALA A 170 34.281 8.069 8.922 1.00 26.68 C ATOM 1181 C ALA A 170 35.794 7.850 8.926 1.00 26.79 C ATOM 1182 O ALA A 170 36.411 7.957 9.948 1.00 30.20 O ATOM 1183 CB ALA A 170 33.776 8.267 10.336 1.00 29.17 C ATOM 1184 N PHE A 171 36.388 7.649 7.761 1.00 23.99 N ATOM 1185 CA PHE A 171 37.867 7.560 7.675 1.00 22.45 C ATOM 1186 C PHE A 171 38.372 8.803 8.304 1.00 20.14 C ATOM 1187 O PHE A 171 39.253 8.779 9.105 1.00 21.59 O ATOM 1188 CB PHE A 171 38.382 7.463 6.245 1.00 19.93 C ATOM 1189 CG PHE A 171 39.884 7.833 6.077 1.00 18.55 C ATOM 1190 CD1 PHE A 171 40.855 6.928 6.391 1.00 20.84 C ATOM 1191 CD2 PHE A 171 40.285 9.062 5.608 1.00 18.05 C ATOM 1192 CE1 PHE A 171 42.181 7.222 6.217 1.00 14.37 C ATOM 1193 CE2 PHE A 171 41.633 9.369 5.456 1.00 17.24 C ATOM 1194 CZ PHE A 171 42.570 8.417 5.760 1.00 15.71 C ATOM 1195 N ASP A 172 37.822 9.978 7.931 1.00 18.88 N ATOM 1196 CA ASP A 172 38.038 11.140 8.655 1.00 19.18 C ATOM 1197 C ASP A 172 36.798 12.000 8.663 1.00 19.03 C ATOM 1198 O ASP A 172 35.861 11.744 7.875 1.00 17.78 O ATOM 1199 CB ASP A 172 39.250 11.965 8.175 1.00 19.93 C ATOM 1200 CG ASP A 172 40.030 12.561 9.304 1.00 24.68 C ATOM 1201 OD1 ASP A 172 39.453 12.707 10.394 1.00 22.37 O ATOM 1202 OD2 ASP A 172 41.237 12.975 9.213 1.00 27.36 O ATOM 1203 N VAL A 173 36.813 13.011 9.528 1.00 15.35 N ATOM 1204 CA VAL A 173 35.616 13.795 9.736 1.00 15.16 C ATOM 1205 C VAL A 173 35.978 15.258 9.623 1.00 16.77 C ATOM 1206 O VAL A 173 36.921 15.727 10.254 1.00 16.81 O ATOM 1207 CB VAL A 173 35.012 13.518 11.169 1.00 14.52 C ATOM 1208 CG1 VAL A 173 33.851 14.447 11.451 1.00 16.50 C ATOM 1209 CG2 VAL A 173 34.529 12.169 11.310 1.00 13.14 C ATOM 1210 N VAL A 174 35.180 15.990 8.854 1.00 15.36 N ATOM 1211 CA VAL A 174 35.323 17.421 8.650 1.00 15.46 C ATOM 1212 C VAL A 174 34.181 18.056 9.397 1.00 16.22 C ATOM 1213 O VAL A 174 33.003 17.805 9.092 1.00 15.36 O ATOM 1214 CB VAL A 174 35.231 17.758 7.144 1.00 14.97 C ATOM 1215 CG1 VAL A 174 35.386 19.252 6.962 1.00 17.22 C ATOM 1216 CG2 VAL A 174 36.400 17.097 6.369 1.00 17.70 C ATOM 1217 N GLN A 175 34.502 18.838 10.423 1.00 16.97 N ATOM 1218 CA GLN A 175 33.472 19.475 11.222 1.00 17.00 C ATOM 1219 C GLN A 175 33.334 20.941 10.827 1.00 15.57 C ATOM 1220 O GLN A 175 34.276 21.729 11.048 1.00 17.29 O ATOM 1221 CB GLN A 175 33.917 19.448 12.646 1.00 20.16 C ATOM 1222 CG GLN A 175 33.768 18.090 13.187 1.00 26.42 C ATOM 1223 CD GLN A 175 32.584 17.918 14.140 1.00 33.38 C ATOM 1224 OE1 GLN A 175 31.541 18.674 14.106 1.00 34.79 O ATOM 1225 NE2 GLN A 175 32.731 16.885 15.006 1.00 34.53 N ATOM 1226 N LEU A 176 32.214 21.300 10.268 1.00 15.07 N ATOM 1227 CA LEU A 176 32.026 22.703 9.841 1.00 17.17 C ATOM 1228 C LEU A 176 31.493 23.506 11.032 1.00 17.97 C ATOM 1229 O LEU A 176 30.474 23.158 11.630 1.00 18.41 O ATOM 1230 CB LEU A 176 31.033 22.787 8.717 1.00 18.54 C ATOM 1231 CG LEU A 176 31.344 22.102 7.438 1.00 18.46 C ATOM 1232 CD1 LEU A 176 30.397 22.494 6.319 1.00 18.59 C ATOM 1233 CD2 LEU A 176 32.868 22.351 7.095 1.00 22.93 C ATOM 1234 N PRO A 177 32.150 24.606 11.374 1.00 18.23 N ATOM 1235 CA PRO A 177 31.703 25.397 12.517 1.00 18.38 C ATOM 1236 C PRO A 177 30.464 26.203 12.181 1.00 18.57 C ATOM 1237 O PRO A 177 30.390 26.815 11.093 1.00 17.49 O ATOM 1238 CB PRO A 177 32.869 26.337 12.767 1.00 18.62 C ATOM 1239 CG PRO A 177 33.547 26.481 11.440 1.00 19.13 C ATOM 1240 CD PRO A 177 33.372 25.155 10.739 1.00 18.60 C ATOM 1241 N PRO A 178 29.487 26.201 13.061 1.00 17.97 N ATOM 1242 CA PRO A 178 28.291 26.976 12.830 1.00 17.82 C ATOM 1243 C PRO A 178 28.652 28.461 12.903 1.00 16.26 C ATOM 1244 O PRO A 178 29.643 28.852 13.482 1.00 14.70 O ATOM 1245 CB PRO A 178 27.397 26.602 13.989 1.00 18.73 C ATOM 1246 CG PRO A 178 28.357 26.228 15.038 1.00 21.42 C ATOM 1247 CD PRO A 178 29.415 25.484 14.353 1.00 19.54 C ATOM 1248 N LEU A 179 27.857 29.277 12.271 1.00 16.06 N ATOM 1249 CA LEU A 179 28.155 30.693 12.193 1.00 16.41 C ATOM 1250 C LEU A 179 28.246 31.326 13.603 1.00 17.05 C ATOM 1251 O LEU A 179 29.025 32.264 13.849 1.00 18.51 O ATOM 1252 CB LEU A 179 27.055 31.311 11.365 1.00 18.17 C ATOM 1253 CG LEU A 179 27.180 32.733 11.034 1.00 20.42 C ATOM 1254 CD1 LEU A 179 28.595 32.968 10.404 1.00 23.44 C ATOM 1255 CD2 LEU A 179 26.011 33.060 10.083 1.00 22.63 C ATOM 1256 N ARG A 180 27.409 30.877 14.517 1.00 18.38 N ATOM 1257 CA ARG A 180 27.423 31.439 15.876 1.00 20.53 C ATOM 1258 C ARG A 180 28.742 31.229 16.609 1.00 22.91 C ATOM 1259 O ARG A 180 29.017 31.882 17.620 1.00 23.18 O ATOM 1260 CB ARG A 180 26.316 30.880 16.700 1.00 20.08 C ATOM 1261 CG ARG A 180 26.509 29.494 17.224 1.00 21.39 C ATOM 1262 CD ARG A 180 25.318 28.996 17.901 1.00 23.66 C ATOM 1263 NE ARG A 180 24.284 28.667 16.956 1.00 27.08 N ATOM 1264 CZ ARG A 180 24.204 27.495 16.286 1.00 23.90 C ATOM 1265 NH1 ARG A 180 25.057 26.541 16.519 1.00 23.26 N ATOM 1266 NH2 ARG A 180 23.219 27.289 15.440 1.00 22.70 N ATOM 1267 N GLU A 181 29.549 30.280 16.158 1.00 24.32 N ATOM 1268 CA GLU A 181 30.889 30.075 16.740 1.00 26.06 C ATOM 1269 C GLU A 181 31.987 30.800 15.948 1.00 27.37 C ATOM 1270 O GLU A 181 33.170 30.609 16.239 1.00 27.78 O ATOM 1271 CB GLU A 181 31.189 28.598 16.829 1.00 26.80 C ATOM 1272 CG GLU A 181 30.342 27.841 17.860 1.00 29.66 C ATOM 1273 CD GLU A 181 30.587 26.349 17.812 1.00 34.21 C ATOM 1274 OE1 GLU A 181 31.656 25.926 17.286 1.00 40.17 O ATOM 1275 OE2 GLU A 181 29.717 25.608 18.295 1.00 36.72 O ATOM 1276 N ARG A 182 31.604 31.601 14.949 1.00 26.73 N ATOM 1277 CA ARG A 182 32.523 32.351 14.057 1.00 28.32 C ATOM 1278 C ARG A 182 32.051 33.760 14.013 1.00 28.45 C ATOM 1279 O ARG A 182 31.805 34.327 12.963 1.00 26.10 O ATOM 1280 CB ARG A 182 32.489 31.844 12.604 1.00 29.31 C ATOM 1281 CG ARG A 182 32.886 30.462 12.382 1.00 31.28 C ATOM 1282 CD ARG A 182 32.162 29.797 11.216 1.00 31.86 C ATOM 1283 NE ARG A 182 32.684 30.347 10.012 1.00 37.23 N ATOM 1284 CZ ARG A 182 32.267 30.025 8.823 1.00 36.10 C ATOM 1285 NH1 ARG A 182 31.354 29.075 8.666 1.00 41.58 N ATOM 1286 NH2 ARG A 182 32.802 30.623 7.795 1.00 36.87 N ATOM 1287 N GLU A 183 31.869 34.351 15.188 1.00 31.16 N ATOM 1288 CA GLU A 183 31.329 35.684 15.229 1.00 33.87 C ATOM 1289 C GLU A 183 32.059 36.666 14.310 1.00 33.98 C ATOM 1290 O GLU A 183 31.405 37.520 13.764 1.00 34.96 O ATOM 1291 CB GLU A 183 31.242 36.205 16.666 1.00 35.35 C ATOM 1292 CG GLU A 183 30.165 35.596 17.540 1.00 40.18 C ATOM 1293 CD GLU A 183 30.240 36.147 18.967 1.00 47.42 C ATOM 1294 OE1 GLU A 183 30.261 37.398 19.162 1.00 52.28 O ATOM 1295 OE2 GLU A 183 30.332 35.321 19.909 1.00 54.32 O ATOM 1296 N SER A 184 33.378 36.555 14.093 1.00 33.54 N ATOM 1297 CA SER A 184 34.097 37.436 13.143 1.00 33.86 C ATOM 1298 C SER A 184 33.566 37.382 11.726 1.00 32.69 C ATOM 1299 O SER A 184 33.541 38.349 10.991 1.00 34.46 O ATOM 1300 CB SER A 184 35.601 37.100 13.111 1.00 35.39 C ATOM 1301 OG SER A 184 35.896 35.792 12.603 1.00 37.89 O ATOM 1302 N ASP A 185 33.132 36.220 11.328 1.00 28.15 N ATOM 1303 CA ASP A 185 32.592 36.060 10.035 1.00 26.68 C ATOM 1304 C ASP A 185 31.170 36.610 9.895 1.00 24.57 C ATOM 1305 O ASP A 185 30.735 36.794 8.761 1.00 25.03 O ATOM 1306 CB ASP A 185 32.569 34.588 9.640 1.00 25.69 C ATOM 1307 CG ASP A 185 33.899 34.094 9.087 1.00 29.31 C ATOM 1308 OD1 ASP A 185 34.642 34.889 8.461 1.00 30.42 O ATOM 1309 OD2 ASP A 185 34.240 32.900 9.178 1.00 29.45 O ATOM 1310 N ILE A 186 30.409 36.713 10.995 1.00 22.27 N ATOM 1311 CA ILE A 186 29.026 37.231 10.903 1.00 20.45 C ATOM 1312 C ILE A 186 29.055 38.648 10.261 1.00 18.82 C ATOM 1313 O ILE A 186 28.365 38.858 9.231 1.00 16.13 O ATOM 1314 CB ILE A 186 28.337 37.248 12.214 1.00 18.90 C ATOM 1315 CG1 ILE A 186 28.087 35.790 12.699 1.00 19.29 C ATOM 1316 CG2 ILE A 186 26.975 37.938 12.113 1.00 16.74 C ATOM 1317 CD1 ILE A 186 27.455 35.664 14.086 1.00 21.61 C ATOM 1318 N MET A 187 29.797 39.592 10.841 1.00 19.04 N ATOM 1319 CA MET A 187 29.771 40.963 10.281 1.00 18.49 C ATOM 1320 C MET A 187 30.447 41.045 8.919 1.00 18.70 C ATOM 1321 O MET A 187 29.992 41.805 8.000 1.00 17.84 O ATOM 1322 CB MET A 187 30.313 42.010 11.297 1.00 20.39 C ATOM 1323 CG MET A 187 29.296 42.299 12.425 1.00 16.34 C ATOM 1324 SD MET A 187 27.666 42.485 12.252 1.00 20.94 S ATOM 1325 CE MET A 187 27.729 43.818 10.976 1.00 23.90 C ATOM 1326 N LEU A 188 31.473 40.234 8.694 1.00 19.20 N ATOM 1327 CA LEU A 188 32.122 40.148 7.403 1.00 20.62 C ATOM 1328 C LEU A 188 31.186 39.689 6.289 1.00 18.08 C ATOM 1329 O LEU A 188 31.130 40.286 5.197 1.00 16.17 O ATOM 1330 CB LEU A 188 33.350 39.187 7.448 1.00 22.01 C ATOM 1331 CG LEU A 188 33.993 38.764 6.103 1.00 29.15 C ATOM 1332 CD1 LEU A 188 34.734 39.963 5.482 1.00 33.88 C ATOM 1333 CD2 LEU A 188 34.960 37.557 6.208 1.00 34.92 C ATOM 1334 N MET A 189 30.473 38.587 6.531 1.00 16.13 N ATOM 1335 CA MET A 189 29.614 38.073 5.501 1.00 15.77 C ATOM 1336 C MET A 189 28.339 38.942 5.396 1.00 13.25 C ATOM 1337 O MET A 189 27.785 39.047 4.358 1.00 11.99 O ATOM 1338 CB MET A 189 29.216 36.611 5.750 1.00 17.51 C ATOM 1339 CG MET A 189 30.278 35.612 5.459 1.00 20.96 C ATOM 1340 SD MET A 189 29.524 33.936 6.055 1.00 37.01 S ATOM 1341 CE MET A 189 29.892 34.124 7.671 1.00 35.52 C ATOM 1342 N ALA A 190 27.847 39.509 6.533 1.00 12.02 N ATOM 1343 CA ALA A 190 26.680 40.377 6.511 1.00 10.64 C ATOM 1344 C ALA A 190 26.980 41.548 5.582 1.00 10.98 C ATOM 1345 O ALA A 190 26.150 41.924 4.739 1.00 10.74 O ATOM 1346 CB ALA A 190 26.347 40.899 7.882 1.00 11.52 C ATOM 1347 N GLU A 191 28.147 42.148 5.772 1.00 9.90 N ATOM 1348 CA GLU A 191 28.546 43.276 4.873 1.00 12.64 C ATOM 1349 C GLU A 191 28.573 42.854 3.413 1.00 12.64 C ATOM 1350 O GLU A 191 28.067 43.540 2.540 1.00 11.97 O ATOM 1351 CB GLU A 191 29.885 43.855 5.324 1.00 14.60 C ATOM 1352 CG GLU A 191 30.263 45.068 4.507 1.00 21.00 C ATOM 1353 CD GLU A 191 31.623 45.586 4.912 1.00 32.36 C ATOM 1354 OE1 GLU A 191 32.606 44.813 4.793 1.00 31.85 O ATOM 1355 OE2 GLU A 191 31.659 46.726 5.391 1.00 37.59 O ATOM 1356 N TYR A 192 29.131 41.681 3.133 1.00 11.39 N ATOM 1357 CA TYR A 192 29.246 41.183 1.783 1.00 12.30 C ATOM 1358 C TYR A 192 27.884 40.988 1.131 1.00 11.50 C ATOM 1359 O TYR A 192 27.649 41.442 0.012 1.00 11.37 O ATOM 1360 CB TYR A 192 30.020 39.856 1.808 1.00 12.66 C ATOM 1361 CG TYR A 192 30.078 39.206 0.443 1.00 15.82 C ATOM 1362 CD1 TYR A 192 31.102 39.504 -0.424 1.00 20.50 C ATOM 1363 CD2 TYR A 192 29.142 38.245 0.052 1.00 20.59 C ATOM 1364 CE1 TYR A 192 31.188 38.902 -1.677 1.00 23.14 C ATOM 1365 CE2 TYR A 192 29.204 37.682 -1.227 1.00 22.64 C ATOM 1366 CZ TYR A 192 30.219 38.022 -2.056 1.00 27.70 C ATOM 1367 OH TYR A 192 30.268 37.436 -3.309 1.00 30.79 O ATOM 1368 N PHE A 193 26.965 40.339 1.844 1.00 11.09 N ATOM 1369 CA PHE A 193 25.609 40.151 1.376 1.00 11.30 C ATOM 1370 C PHE A 193 24.818 41.425 1.220 1.00 9.90 C ATOM 1371 O PHE A 193 24.045 41.539 0.237 1.00 12.37 O ATOM 1372 CB PHE A 193 24.841 39.163 2.277 1.00 10.94 C ATOM 1373 CG PHE A 193 25.403 37.751 2.281 1.00 10.91 C ATOM 1374 CD1 PHE A 193 25.443 37.065 3.457 1.00 13.89 C ATOM 1375 CD2 PHE A 193 25.798 37.094 1.128 1.00 14.25 C ATOM 1376 CE1 PHE A 193 25.941 35.778 3.497 1.00 17.11 C ATOM 1377 CE2 PHE A 193 26.342 35.810 1.193 1.00 19.09 C ATOM 1378 CZ PHE A 193 26.397 35.183 2.348 1.00 16.27 C ATOM 1379 N ALA A 194 25.033 42.404 2.095 1.00 10.63 N ATOM 1380 CA ALA A 194 24.326 43.664 2.063 1.00 10.14 C ATOM 1381 C ALA A 194 24.771 44.418 0.802 1.00 10.56 C ATOM 1382 O ALA A 194 23.954 44.972 0.087 1.00 11.98 O ATOM 1383 CB ALA A 194 24.607 44.445 3.269 1.00 9.86 C ATOM 1384 N ILE A 195 26.072 44.432 0.538 1.00 12.45 N ATOM 1385 CA ILE A 195 26.601 45.088 -0.674 1.00 11.53 C ATOM 1386 C ILE A 195 26.019 44.524 -1.968 1.00 12.58 C ATOM 1387 O ILE A 195 25.529 45.256 -2.820 1.00 12.53 O ATOM 1388 CB ILE A 195 28.126 45.093 -0.647 1.00 10.92 C ATOM 1389 CG1 ILE A 195 28.636 46.005 0.461 1.00 12.22 C ATOM 1390 CG2 ILE A 195 28.691 45.440 -2.011 1.00 13.04 C ATOM 1391 CD1 ILE A 195 30.126 45.791 0.789 1.00 12.43 C ATOM 1392 N GLN A 196 25.908 43.201 -2.035 1.00 13.39 N ATOM 1393 CA GLN A 196 25.394 42.550 -3.234 1.00 14.31 C ATOM 1394 C GLN A 196 23.968 42.906 -3.402 1.00 13.23 C ATOM 1395 O GLN A 196 23.526 43.177 -4.514 1.00 14.48 O ATOM 1396 CB GLN A 196 25.399 41.036 -3.048 1.00 16.24 C ATOM 1397 CG GLN A 196 26.641 40.320 -3.109 1.00 22.78 C ATOM 1398 CD GLN A 196 26.385 38.764 -3.399 1.00 31.36 C ATOM 1399 OE1 GLN A 196 25.501 38.024 -2.763 1.00 27.22 O ATOM 1400 NE2 GLN A 196 27.138 38.280 -4.364 1.00 31.71 N ATOM 1401 N MET A 197 23.213 42.964 -2.284 1.00 13.83 N ATOM 1402 CA MET A 197 21.787 43.366 -2.374 1.00 13.04 C ATOM 1403 C MET A 197 21.631 44.819 -2.798 1.00 13.18 C ATOM 1404 O MET A 197 20.714 45.140 -3.516 1.00 13.45 O ATOM 1405 CB MET A 197 21.041 43.090 -1.082 1.00 12.44 C ATOM 1406 CG MET A 197 19.538 43.316 -1.179 1.00 12.90 C ATOM 1407 SD MET A 197 18.833 42.093 -2.347 1.00 14.41 S ATOM 1408 CE MET A 197 17.023 42.593 -2.164 1.00 14.03 C ATOM 1409 N CYS A 198 22.527 45.707 -2.341 1.00 11.96 N ATOM 1410 CA CYS A 198 22.521 47.089 -2.790 1.00 13.20 C ATOM 1411 C CYS A 198 22.658 47.162 -4.289 1.00 12.58 C ATOM 1412 O CYS A 198 21.997 48.023 -4.904 1.00 14.51 O ATOM 1413 CB CYS A 198 23.594 47.922 -2.091 1.00 11.51 C ATOM 1414 SG CYS A 198 23.217 48.219 -0.348 1.00 14.27 S ATOM 1415 N ARG A 199 23.561 46.372 -4.863 1.00 12.16 N ATOM 1416 CA ARG A 199 23.718 46.331 -6.332 1.00 13.93 C ATOM 1417 C ARG A 199 22.451 45.867 -7.023 1.00 16.55 C ATOM 1418 O ARG A 199 21.994 46.474 -8.016 1.00 17.14 O ATOM 1419 CB ARG A 199 24.934 45.500 -6.771 1.00 13.27 C ATOM 1420 CG ARG A 199 26.269 45.994 -6.315 1.00 14.76 C ATOM 1421 CD ARG A 199 26.581 47.451 -6.779 1.00 12.89 C ATOM 1422 NE ARG A 199 26.095 48.441 -5.840 1.00 11.05 N ATOM 1423 CZ ARG A 199 26.712 48.764 -4.700 1.00 12.65 C ATOM 1424 NH1 ARG A 199 27.836 48.172 -4.356 1.00 11.51 N ATOM 1425 NH2 ARG A 199 26.232 49.679 -3.924 1.00 13.41 N ATOM 1426 N GLU A 200 21.852 44.830 -6.454 1.00 16.47 N ATOM 1427 CA GLU A 200 20.619 44.261 -6.996 1.00 19.74 C ATOM 1428 C GLU A 200 19.469 45.267 -7.042 1.00 19.25 C ATOM 1429 O GLU A 200 18.718 45.341 -8.059 1.00 20.10 O ATOM 1430 CB GLU A 200 20.251 42.995 -6.215 1.00 19.95 C ATOM 1431 CG GLU A 200 19.194 42.238 -6.976 1.00 25.20 C ATOM 1432 CD GLU A 200 18.838 40.904 -6.353 1.00 29.04 C ATOM 1433 OE1 GLU A 200 19.698 40.283 -5.714 1.00 20.33 O ATOM 1434 OE2 GLU A 200 17.651 40.498 -6.505 1.00 37.00 O ATOM 1435 N ILE A 201 19.338 46.103 -6.020 1.00 16.69 N ATOM 1436 CA ILE A 201 18.288 47.104 -5.988 1.00 18.08 C ATOM 1437 C ILE A 201 18.710 48.536 -6.344 1.00 17.85 C ATOM 1438 O ILE A 201 17.959 49.476 -6.178 1.00 18.69 O ATOM 1439 CB ILE A 201 17.489 47.076 -4.708 1.00 17.88 C ATOM 1440 CG1 ILE A 201 18.300 47.482 -3.454 1.00 18.58 C ATOM 1441 CG2 ILE A 201 16.927 45.693 -4.532 1.00 18.55 C ATOM 1442 CD1 ILE A 201 17.488 47.590 -2.212 1.00 18.36 C ATOM 1443 N LYS A 202 19.935 48.655 -6.785 1.00 18.54 N ATOM 1444 CA LYS A 202 20.505 49.874 -7.327 1.00 19.35 C ATOM 1445 C LYS A 202 20.655 50.995 -6.325 1.00 18.44 C ATOM 1446 O LYS A 202 20.462 52.204 -6.644 1.00 19.82 O ATOM 1447 CB LYS A 202 19.702 50.330 -8.577 1.00 21.02 C ATOM 1448 CG LYS A 202 19.755 49.355 -9.673 1.00 25.43 C ATOM 1449 CD LYS A 202 19.085 49.890 -10.937 1.00 34.86 C ATOM 1450 CE LYS A 202 19.002 48.816 -12.034 1.00 38.59 C ATOM 1451 NZ LYS A 202 18.241 49.368 -13.234 1.00 43.76 N ATOM 1452 N LEU A 203 20.985 50.672 -5.079 1.00 16.52 N ATOM 1453 CA LEU A 203 21.409 51.670 -4.150 1.00 16.01 C ATOM 1454 C LEU A 203 22.864 52.030 -4.379 1.00 16.56 C ATOM 1455 O LEU A 203 23.687 51.192 -4.679 1.00 14.82 O ATOM 1456 CB LEU A 203 21.226 51.241 -2.691 1.00 16.60 C ATOM 1457 CG LEU A 203 19.801 51.019 -2.225 1.00 19.89 C ATOM 1458 CD1 LEU A 203 19.849 50.301 -0.865 1.00 19.97 C ATOM 1459 CD2 LEU A 203 19.151 52.371 -2.127 1.00 23.83 C ATOM 1460 N PRO A 204 23.176 53.315 -4.275 1.00 16.07 N ATOM 1461 CA PRO A 204 24.542 53.768 -4.573 1.00 15.83 C ATOM 1462 C PRO A 204 25.628 53.266 -3.618 1.00 13.42 C ATOM 1463 O PRO A 204 26.730 53.089 -4.052 1.00 12.26 O ATOM 1464 CB PRO A 204 24.439 55.289 -4.526 1.00 16.09 C ATOM 1465 CG PRO A 204 23.154 55.538 -3.717 1.00 18.25 C ATOM 1466 CD PRO A 204 22.265 54.443 -3.994 1.00 17.47 C ATOM 1467 N LEU A 205 25.311 53.071 -2.335 1.00 14.61 N ATOM 1468 CA LEU A 205 26.274 52.709 -1.339 1.00 15.55 C ATOM 1469 C LEU A 205 25.531 51.943 -0.242 1.00 14.32 C ATOM 1470 O LEU A 205 24.377 52.287 0.080 1.00 16.59 O ATOM 1471 CB LEU A 205 26.859 53.940 -0.679 1.00 17.19 C ATOM 1472 CG LEU A 205 28.252 53.921 -0.042 1.00 22.64 C ATOM 1473 CD1 LEU A 205 29.347 53.492 -0.974 1.00 22.44 C ATOM 1474 CD2 LEU A 205 28.562 55.279 0.520 1.00 29.13 C ATOM 1475 N PHE A 206 26.179 50.941 0.315 1.00 13.05 N ATOM 1476 CA PHE A 206 25.668 50.306 1.528 1.00 13.96 C ATOM 1477 C PHE A 206 25.937 51.259 2.672 1.00 15.16 C ATOM 1478 O PHE A 206 27.088 51.570 2.908 1.00 14.46 O ATOM 1479 CB PHE A 206 26.303 48.930 1.791 1.00 12.99 C ATOM 1480 CG PHE A 206 25.860 48.331 3.101 1.00 13.47 C ATOM 1481 CD1 PHE A 206 24.507 48.236 3.394 1.00 13.29 C ATOM 1482 CD2 PHE A 206 26.778 47.966 4.045 1.00 15.31 C ATOM 1483 CE1 PHE A 206 24.081 47.733 4.586 1.00 16.87 C ATOM 1484 CE2 PHE A 206 26.381 47.509 5.258 1.00 16.51 C ATOM 1485 CZ PHE A 206 25.046 47.389 5.545 1.00 15.00 C ATOM 1486 N PRO A 207 24.908 51.764 3.355 1.00 14.99 N ATOM 1487 CA PRO A 207 25.163 52.779 4.375 1.00 16.26 C ATOM 1488 C PRO A 207 25.621 52.295 5.730 1.00 17.13 C ATOM 1489 O PRO A 207 25.778 53.124 6.621 1.00 16.91 O ATOM 1490 CB PRO A 207 23.846 53.491 4.475 1.00 15.47 C ATOM 1491 CG PRO A 207 22.839 52.432 4.286 1.00 14.70 C ATOM 1492 CD PRO A 207 23.465 51.583 3.165 1.00 16.34 C ATOM 1493 N GLY A 208 25.815 51.007 5.912 1.00 15.55 N ATOM 1494 CA GLY A 208 26.350 50.472 7.145 1.00 15.66 C ATOM 1495 C GLY A 208 25.289 49.910 8.033 1.00 14.12 C ATOM 1496 O GLY A 208 24.075 50.047 7.803 1.00 15.81 O ATOM 1497 N PHE A 209 25.726 49.273 9.080 1.00 14.79 N ATOM 1498 CA PHE A 209 24.846 48.712 10.127 1.00 14.79 C ATOM 1499 C PHE A 209 24.990 49.525 11.406 1.00 14.32 C ATOM 1500 O PHE A 209 26.103 49.790 11.843 1.00 12.22 O ATOM 1501 CB PHE A 209 25.249 47.278 10.475 1.00 15.88 C ATOM 1502 CG PHE A 209 25.116 46.295 9.364 1.00 14.69 C ATOM 1503 CD1 PHE A 209 26.256 45.791 8.734 1.00 16.28 C ATOM 1504 CD2 PHE A 209 23.878 45.788 9.038 1.00 16.51 C ATOM 1505 CE1 PHE A 209 26.121 44.850 7.678 1.00 16.20 C ATOM 1506 CE2 PHE A 209 23.757 44.845 8.006 1.00 16.46 C ATOM 1507 CZ PHE A 209 24.914 44.381 7.366 1.00 13.09 C ATOM 1508 N THR A 210 23.866 49.944 11.987 1.00 13.53 N ATOM 1509 CA THR A 210 23.908 50.560 13.307 1.00 14.65 C ATOM 1510 C THR A 210 24.384 49.596 14.366 1.00 13.65 C ATOM 1511 O THR A 210 24.397 48.390 14.188 1.00 11.82 O ATOM 1512 CB THR A 210 22.529 51.072 13.738 1.00 13.29 C ATOM 1513 OG1 THR A 210 21.627 49.997 13.922 1.00 13.87 O ATOM 1514 CG2 THR A 210 21.896 52.002 12.722 1.00 16.13 C ATOM 1515 N GLU A 211 24.777 50.095 15.541 1.00 13.47 N ATOM 1516 CA GLU A 211 25.131 49.227 16.639 1.00 12.43 C ATOM 1517 C GLU A 211 23.959 48.330 17.062 1.00 13.96 C ATOM 1518 O GLU A 211 24.171 47.167 17.368 1.00 14.36 O ATOM 1519 CB GLU A 211 25.601 50.068 17.817 1.00 12.89 C ATOM 1520 CG GLU A 211 26.200 49.287 18.980 1.00 12.70 C ATOM 1521 CD GLU A 211 27.583 48.691 18.752 1.00 12.97 C ATOM 1522 OE1 GLU A 211 28.186 48.936 17.682 1.00 13.64 O ATOM 1523 OE2 GLU A 211 28.053 47.997 19.666 1.00 14.35 O ATOM 1524 N ARG A 212 22.732 48.847 17.033 1.00 14.33 N ATOM 1525 CA ARG A 212 21.556 47.977 17.323 1.00 15.05 C ATOM 1526 C ARG A 212 21.424 46.806 16.307 1.00 15.09 C ATOM 1527 O ARG A 212 21.186 45.644 16.699 1.00 16.49 O ATOM 1528 CB ARG A 212 20.290 48.811 17.258 1.00 16.96 C ATOM 1529 CG ARG A 212 18.994 48.067 17.457 1.00 21.14 C ATOM 1530 CD ARG A 212 17.744 48.995 17.470 1.00 27.27 C ATOM 1531 NE ARG A 212 16.522 48.192 17.368 1.00 36.43 N ATOM 1532 CZ ARG A 212 15.862 47.940 16.251 1.00 39.86 C ATOM 1533 NH1 ARG A 212 16.251 48.433 15.114 1.00 45.31 N ATOM 1534 NH2 ARG A 212 14.773 47.209 16.273 1.00 45.62 N ATOM 1535 N ALA A 213 21.675 47.103 15.044 1.00 13.16 N ATOM 1536 CA ALA A 213 21.706 46.040 14.030 1.00 14.29 C ATOM 1537 C ALA A 213 22.752 45.016 14.278 1.00 14.47 C ATOM 1538 O ALA A 213 22.538 43.800 14.148 1.00 15.01 O ATOM 1539 CB ALA A 213 21.816 46.639 12.647 1.00 15.30 C ATOM 1540 N ARG A 214 23.940 45.477 14.627 1.00 13.34 N ATOM 1541 CA ARG A 214 25.040 44.578 14.926 1.00 13.42 C ATOM 1542 C ARG A 214 24.738 43.701 16.125 1.00 15.07 C ATOM 1543 O ARG A 214 25.091 42.514 16.160 1.00 15.09 O ATOM 1544 CB ARG A 214 26.344 45.391 15.161 1.00 11.19 C ATOM 1545 CG ARG A 214 26.850 46.095 13.913 1.00 11.20 C ATOM 1546 CD ARG A 214 27.689 47.323 14.159 1.00 9.59 C ATOM 1547 NE ARG A 214 28.203 47.852 12.907 1.00 13.64 N ATOM 1548 CZ ARG A 214 29.260 47.353 12.300 1.00 14.67 C ATOM 1549 NH1 ARG A 214 29.927 46.364 12.849 1.00 15.73 N ATOM 1550 NH2 ARG A 214 29.635 47.843 11.133 1.00 16.56 N ATOM 1551 N GLU A 215 24.085 44.254 17.155 1.00 13.68 N ATOM 1552 CA GLU A 215 23.725 43.478 18.322 1.00 17.03 C ATOM 1553 C GLU A 215 22.742 42.380 17.917 1.00 19.31 C ATOM 1554 O GLU A 215 22.841 41.234 18.410 1.00 21.95 O ATOM 1555 CB GLU A 215 23.072 44.407 19.377 1.00 18.38 C ATOM 1556 CG GLU A 215 24.128 45.195 20.146 1.00 21.96 C ATOM 1557 CD GLU A 215 23.565 46.082 21.304 1.00 31.29 C ATOM 1558 OE1 GLU A 215 22.442 45.785 21.801 1.00 37.64 O ATOM 1559 OE2 GLU A 215 24.204 47.085 21.707 1.00 27.29 O ATOM 1560 N THR A 216 21.822 42.728 17.021 1.00 20.02 N ATOM 1561 CA THR A 216 20.769 41.802 16.581 1.00 20.74 C ATOM 1562 C THR A 216 21.463 40.678 15.814 1.00 19.92 C ATOM 1563 O THR A 216 21.200 39.461 16.053 1.00 21.70 O ATOM 1564 CB THR A 216 19.764 42.557 15.709 1.00 20.51 C ATOM 1565 OG1 THR A 216 19.088 43.610 16.450 1.00 23.09 O ATOM 1566 CG2 THR A 216 18.623 41.646 15.217 1.00 21.30 C ATOM 1567 N LEU A 217 22.374 41.057 14.910 1.00 19.13 N ATOM 1568 CA LEU A 217 23.127 40.081 14.094 1.00 18.75 C ATOM 1569 C LEU A 217 23.977 39.149 14.977 1.00 20.46 C ATOM 1570 O LEU A 217 24.054 37.929 14.734 1.00 23.27 O ATOM 1571 CB LEU A 217 24.025 40.750 13.059 1.00 19.39 C ATOM 1572 CG LEU A 217 23.222 41.453 11.951 1.00 16.89 C ATOM 1573 CD1 LEU A 217 24.177 42.328 11.208 1.00 18.16 C ATOM 1574 CD2 LEU A 217 22.567 40.424 10.978 1.00 21.78 C ATOM 1575 N LEU A 218 24.686 39.710 15.950 1.00 18.04 N ATOM 1576 CA LEU A 218 25.672 38.960 16.708 1.00 19.80 C ATOM 1577 C LEU A 218 25.015 38.170 17.845 1.00 20.53 C ATOM 1578 O LEU A 218 25.585 37.214 18.302 1.00 23.70 O ATOM 1579 CB LEU A 218 26.752 39.905 17.258 1.00 18.85 C ATOM 1580 CG LEU A 218 27.615 40.556 16.183 1.00 18.82 C ATOM 1581 CD1 LEU A 218 28.501 41.606 16.741 1.00 22.31 C ATOM 1582 CD2 LEU A 218 28.429 39.564 15.454 1.00 24.74 C ATOM 1583 N ASN A 219 23.826 38.571 18.270 1.00 21.20 N ATOM 1584 CA ASN A 219 23.143 37.893 19.378 1.00 23.09 C ATOM 1585 C ASN A 219 22.336 36.704 18.850 1.00 21.93 C ATOM 1586 O ASN A 219 21.994 35.782 19.613 1.00 21.47 O ATOM 1587 CB ASN A 219 22.206 38.833 20.121 1.00 23.94 C ATOM 1588 CG ASN A 219 22.954 39.759 21.081 1.00 29.35 C ATOM 1589 OD1 ASN A 219 24.145 39.526 21.401 1.00 33.55 O ATOM 1590 ND2 ASN A 219 22.282 40.855 21.500 1.00 33.84 N ATOM 1591 N TYR A 220 21.949 36.743 17.582 1.00 18.63 N ATOM 1592 CA TYR A 220 21.075 35.690 17.052 1.00 18.85 C ATOM 1593 C TYR A 220 21.845 34.387 16.840 1.00 18.94 C ATOM 1594 O TYR A 220 23.001 34.445 16.500 1.00 17.72 O ATOM 1595 CB TYR A 220 20.440 36.180 15.712 1.00 18.91 C ATOM 1596 CG TYR A 220 19.481 35.220 15.085 1.00 15.04 C ATOM 1597 CD1 TYR A 220 18.406 34.711 15.751 1.00 16.27 C ATOM 1598 CD2 TYR A 220 19.627 34.833 13.749 1.00 14.52 C ATOM 1599 CE1 TYR A 220 17.511 33.805 15.157 1.00 18.55 C ATOM 1600 CE2 TYR A 220 18.751 33.965 13.139 1.00 13.86 C ATOM 1601 CZ TYR A 220 17.666 33.418 13.853 1.00 16.45 C ATOM 1602 OH TYR A 220 16.762 32.526 13.239 1.00 16.22 O ATOM 1603 N ARG A 221 21.185 33.207 17.025 1.00 17.54 N ATOM 1604 CA ARG A 221 21.879 31.938 16.896 1.00 18.86 C ATOM 1605 C ARG A 221 22.118 31.402 15.496 1.00 17.08 C ATOM 1606 O ARG A 221 22.881 30.423 15.369 1.00 19.05 O ATOM 1607 CB ARG A 221 21.158 30.846 17.733 1.00 20.47 C ATOM 1608 CG ARG A 221 21.602 30.680 19.136 1.00 28.95 C ATOM 1609 CD ARG A 221 21.390 29.183 19.606 1.00 36.43 C ATOM 1610 NE ARG A 221 22.448 28.713 20.528 1.00 41.00 N ATOM 1611 CZ ARG A 221 23.068 27.531 20.446 1.00 45.46 C ATOM 1612 NH1 ARG A 221 22.789 26.652 19.484 1.00 45.69 N ATOM 1613 NH2 ARG A 221 23.991 27.219 21.346 1.00 51.39 N ATOM 1614 N TRP A 222 21.469 31.965 14.474 1.00 14.41 N ATOM 1615 CA TRP A 222 21.596 31.552 13.069 1.00 13.07 C ATOM 1616 C TRP A 222 21.444 30.019 12.908 1.00 14.04 C ATOM 1617 O TRP A 222 22.367 29.351 12.531 1.00 15.40 O ATOM 1618 CB TRP A 222 22.977 32.001 12.509 1.00 14.43 C ATOM 1619 CG TRP A 222 23.089 33.528 12.571 1.00 16.60 C ATOM 1620 CD1 TRP A 222 23.824 34.257 13.430 1.00 17.02 C ATOM 1621 CD2 TRP A 222 22.329 34.445 11.786 1.00 18.09 C ATOM 1622 NE1 TRP A 222 23.593 35.599 13.209 1.00 14.85 N ATOM 1623 CE2 TRP A 222 22.646 35.736 12.226 1.00 16.02 C ATOM 1624 CE3 TRP A 222 21.391 34.307 10.755 1.00 15.01 C ATOM 1625 CZ2 TRP A 222 22.074 36.848 11.653 1.00 13.44 C ATOM 1626 CZ3 TRP A 222 20.785 35.418 10.228 1.00 17.11 C ATOM 1627 CH2 TRP A 222 21.133 36.692 10.699 1.00 16.43 C ATOM 1628 N PRO A 223 20.301 29.477 13.251 1.00 15.16 N ATOM 1629 CA PRO A 223 20.069 28.050 13.044 1.00 15.95 C ATOM 1630 C PRO A 223 20.243 27.652 11.595 1.00 17.72 C ATOM 1631 O PRO A 223 20.570 26.483 11.257 1.00 18.02 O ATOM 1632 CB PRO A 223 18.645 27.887 13.490 1.00 16.77 C ATOM 1633 CG PRO A 223 18.025 29.220 13.487 1.00 17.61 C ATOM 1634 CD PRO A 223 19.128 30.131 13.834 1.00 15.07 C ATOM 1635 N GLY A 224 20.033 28.614 10.690 1.00 15.93 N ATOM 1636 CA GLY A 224 20.253 28.343 9.290 1.00 16.28 C ATOM 1637 C GLY A 224 21.529 28.884 8.719 1.00 15.15 C ATOM 1638 O GLY A 224 21.731 28.881 7.497 1.00 15.84 O ATOM 1639 N ASN A 225 22.415 29.309 9.601 1.00 15.50 N ATOM 1640 CA ASN A 225 23.766 29.641 9.295 1.00 16.55 C ATOM 1641 C ASN A 225 23.907 30.608 8.087 1.00 18.75 C ATOM 1642 O ASN A 225 23.245 31.622 8.088 1.00 18.27 O ATOM 1643 CB ASN A 225 24.614 28.330 9.246 1.00 16.09 C ATOM 1644 CG ASN A 225 24.677 27.705 10.580 1.00 15.73 C ATOM 1645 OD1 ASN A 225 25.484 28.123 11.443 1.00 16.66 O ATOM 1646 ND2 ASN A 225 23.808 26.687 10.812 1.00 14.71 N ATOM 1647 N ILE A 226 24.768 30.347 7.118 1.00 20.10 N ATOM 1648 CA ILE A 226 25.013 31.304 6.017 1.00 20.76 C ATOM 1649 C ILE A 226 23.870 31.564 5.093 1.00 20.82 C ATOM 1650 O ILE A 226 23.643 32.716 4.738 1.00 19.50 O ATOM 1651 CB ILE A 226 26.208 30.822 5.105 1.00 21.96 C ATOM 1652 CG1 ILE A 226 27.382 30.378 5.914 1.00 25.36 C ATOM 1653 CG2 ILE A 226 26.584 31.819 4.117 1.00 24.69 C ATOM 1654 CD1 ILE A 226 27.850 31.270 6.880 1.00 31.70 C ATOM 1655 N ARG A 227 23.120 30.533 4.707 1.00 18.40 N ATOM 1656 CA ARG A 227 21.955 30.685 3.896 1.00 19.01 C ATOM 1657 C ARG A 227 20.992 31.664 4.593 1.00 17.95 C ATOM 1658 O ARG A 227 20.443 32.535 3.941 1.00 17.32 O ATOM 1659 CB ARG A 227 21.255 29.339 3.630 1.00 20.66 C ATOM 1660 CG ARG A 227 19.861 29.486 2.947 1.00 23.69 C ATOM 1661 CD ARG A 227 18.964 28.171 2.850 1.00 24.86 C ATOM 1662 NE ARG A 227 19.516 27.182 1.873 1.00 25.70 N ATOM 1663 CZ ARG A 227 20.184 26.058 2.225 1.00 25.32 C ATOM 1664 NH1 ARG A 227 20.366 25.757 3.519 1.00 23.38 N ATOM 1665 NH2 ARG A 227 20.663 25.224 1.290 1.00 25.74 N ATOM 1666 N GLU A 228 20.735 31.428 5.891 1.00 15.87 N ATOM 1667 CA GLU A 228 19.843 32.277 6.668 1.00 15.87 C ATOM 1668 C GLU A 228 20.398 33.684 6.757 1.00 14.79 C ATOM 1669 O GLU A 228 19.620 34.643 6.594 1.00 15.62 O ATOM 1670 CB GLU A 228 19.585 31.742 8.065 1.00 14.80 C ATOM 1671 CG GLU A 228 18.481 32.482 8.797 1.00 15.52 C ATOM 1672 CD GLU A 228 18.208 31.930 10.195 1.00 14.89 C ATOM 1673 OE1 GLU A 228 19.119 31.323 10.785 1.00 17.36 O ATOM 1674 OE2 GLU A 228 17.083 32.223 10.694 1.00 16.97 O ATOM 1675 N LEU A 229 21.682 33.820 6.998 1.00 14.38 N ATOM 1676 CA LEU A 229 22.260 35.181 7.061 1.00 14.59 C ATOM 1677 C LEU A 229 22.040 35.930 5.781 1.00 13.07 C ATOM 1678 O LEU A 229 21.675 37.133 5.794 1.00 13.50 O ATOM 1679 CB LEU A 229 23.758 35.122 7.452 1.00 14.37 C ATOM 1680 CG LEU A 229 24.544 36.404 7.537 1.00 13.98 C ATOM 1681 CD1 LEU A 229 24.030 37.297 8.615 1.00 14.81 C ATOM 1682 CD2 LEU A 229 26.021 36.154 7.688 1.00 16.84 C ATOM 1683 N LYS A 230 22.306 35.290 4.649 1.00 12.14 N ATOM 1684 CA LYS A 230 22.113 35.957 3.376 1.00 12.65 C ATOM 1685 C LYS A 230 20.657 36.422 3.218 1.00 12.34 C ATOM 1686 O LYS A 230 20.403 37.579 2.928 1.00 12.55 O ATOM 1687 CB LYS A 230 22.486 35.023 2.215 1.00 13.90 C ATOM 1688 CG LYS A 230 22.284 35.660 0.815 1.00 15.14 C ATOM 1689 CD LYS A 230 22.890 34.836 -0.273 1.00 21.74 C ATOM 1690 CE LYS A 230 22.646 35.409 -1.642 1.00 24.07 C ATOM 1691 NZ LYS A 230 23.313 34.609 -2.694 1.00 28.62 N ATOM 1692 N ASN A 231 19.707 35.545 3.552 1.00 12.70 N ATOM 1693 CA ASN A 231 18.298 35.862 3.409 1.00 14.76 C ATOM 1694 C ASN A 231 17.892 37.049 4.292 1.00 12.36 C ATOM 1695 O ASN A 231 17.248 37.995 3.817 1.00 14.52 O ATOM 1696 CB ASN A 231 17.417 34.639 3.736 1.00 16.28 C ATOM 1697 CG ASN A 231 17.683 33.513 2.823 1.00 24.01 C ATOM 1698 OD1 ASN A 231 17.772 32.304 3.227 1.00 34.50 O ATOM 1699 ND2 ASN A 231 17.923 33.858 1.567 1.00 25.92 N ATOM 1700 N VAL A 232 18.257 36.992 5.553 1.00 12.49 N ATOM 1701 CA VAL A 232 17.954 38.044 6.542 1.00 12.19 C ATOM 1702 C VAL A 232 18.519 39.379 6.087 1.00 12.81 C ATOM 1703 O VAL A 232 17.832 40.378 6.071 1.00 13.17 O ATOM 1704 CB VAL A 232 18.501 37.702 7.905 1.00 13.08 C ATOM 1705 CG1 VAL A 232 18.407 38.893 8.833 1.00 13.02 C ATOM 1706 CG2 VAL A 232 17.681 36.480 8.484 1.00 16.11 C ATOM 1707 N VAL A 233 19.774 39.374 5.680 1.00 11.08 N ATOM 1708 CA VAL A 233 20.450 40.611 5.252 1.00 11.23 C ATOM 1709 C VAL A 233 19.833 41.202 3.962 1.00 10.72 C ATOM 1710 O VAL A 233 19.597 42.420 3.870 1.00 10.63 O ATOM 1711 CB VAL A 233 21.954 40.431 5.140 1.00 11.21 C ATOM 1712 CG1 VAL A 233 22.579 41.680 4.455 1.00 11.88 C ATOM 1713 CG2 VAL A 233 22.548 40.244 6.552 1.00 10.05 C ATOM 1714 N GLU A 234 19.542 40.357 2.968 1.00 11.27 N ATOM 1715 CA GLU A 234 18.898 40.813 1.739 1.00 11.19 C ATOM 1716 C GLU A 234 17.535 41.472 2.022 1.00 11.46 C ATOM 1717 O GLU A 234 17.246 42.512 1.484 1.00 12.84 O ATOM 1718 CB GLU A 234 18.787 39.737 0.656 1.00 12.15 C ATOM 1719 CG GLU A 234 20.115 39.216 0.172 1.00 13.01 C ATOM 1720 CD GLU A 234 20.036 38.440 -1.115 1.00 22.63 C ATOM 1721 OE1 GLU A 234 18.924 37.944 -1.436 1.00 21.70 O ATOM 1722 OE2 GLU A 234 21.069 38.356 -1.802 1.00 20.48 O ATOM 1723 N ARG A 235 16.752 40.820 2.822 1.00 12.16 N ATOM 1724 CA ARG A 235 15.425 41.345 3.161 1.00 13.81 C ATOM 1725 C ARG A 235 15.573 42.653 3.911 1.00 12.95 C ATOM 1726 O ARG A 235 14.826 43.565 3.669 1.00 13.97 O ATOM 1727 CB ARG A 235 14.624 40.360 3.981 1.00 15.62 C ATOM 1728 CG ARG A 235 13.340 40.953 4.429 1.00 16.46 C ATOM 1729 CD ARG A 235 12.471 39.930 5.210 1.00 18.94 C ATOM 1730 NE ARG A 235 13.270 39.148 6.175 1.00 20.29 N ATOM 1731 CZ ARG A 235 13.578 37.862 5.987 1.00 19.45 C ATOM 1732 NH1 ARG A 235 13.128 37.223 4.932 1.00 21.14 N ATOM 1733 NH2 ARG A 235 14.259 37.182 6.888 1.00 19.72 N ATOM 1734 N SER A 236 16.510 42.686 4.853 1.00 12.97 N ATOM 1735 CA SER A 236 16.715 43.865 5.662 1.00 11.56 C ATOM 1736 C SER A 236 17.100 45.052 4.808 1.00 12.38 C ATOM 1737 O SER A 236 16.629 46.179 5.015 1.00 13.57 O ATOM 1738 CB SER A 236 17.777 43.600 6.717 1.00 11.47 C ATOM 1739 OG SER A 236 17.312 42.562 7.611 1.00 14.36 O ATOM 1740 N VAL A 237 18.037 44.845 3.881 1.00 12.20 N ATOM 1741 CA VAL A 237 18.462 45.930 2.945 1.00 10.69 C ATOM 1742 C VAL A 237 17.288 46.431 2.126 1.00 12.81 C ATOM 1743 O VAL A 237 17.149 47.636 1.916 1.00 14.19 O ATOM 1744 CB VAL A 237 19.603 45.481 2.040 1.00 11.20 C ATOM 1745 CG1 VAL A 237 19.922 46.482 0.950 1.00 12.89 C ATOM 1746 CG2 VAL A 237 20.864 45.320 2.936 1.00 13.17 C ATOM 1747 N TYR A 238 16.514 45.505 1.559 1.00 14.47 N ATOM 1748 CA TYR A 238 15.326 45.829 0.730 1.00 14.33 C ATOM 1749 C TYR A 238 14.286 46.659 1.531 1.00 14.68 C ATOM 1750 O TYR A 238 13.832 47.718 1.059 1.00 14.57 O ATOM 1751 CB TYR A 238 14.728 44.531 0.213 1.00 15.40 C ATOM 1752 CG TYR A 238 13.297 44.722 -0.228 1.00 14.40 C ATOM 1753 CD1 TYR A 238 13.041 45.471 -1.354 1.00 19.40 C ATOM 1754 CD2 TYR A 238 12.219 44.222 0.483 1.00 15.13 C ATOM 1755 CE1 TYR A 238 11.743 45.682 -1.769 1.00 19.04 C ATOM 1756 CE2 TYR A 238 10.912 44.505 0.060 1.00 15.64 C ATOM 1757 CZ TYR A 238 10.738 45.212 -1.069 1.00 17.98 C ATOM 1758 OH TYR A 238 9.457 45.463 -1.544 1.00 24.71 O ATOM 1759 N ARG A 239 13.982 46.252 2.734 1.00 15.44 N ATOM 1760 CA ARG A 239 13.021 46.981 3.589 1.00 16.57 C ATOM 1761 C ARG A 239 13.522 48.344 3.998 1.00 16.25 C ATOM 1762 O ARG A 239 12.700 49.289 4.100 1.00 17.14 O ATOM 1763 CB ARG A 239 12.683 46.186 4.848 1.00 16.63 C ATOM 1764 CG ARG A 239 11.896 44.901 4.600 1.00 19.21 C ATOM 1765 CD ARG A 239 10.927 44.646 5.727 1.00 27.27 C ATOM 1766 NE ARG A 239 10.234 43.364 5.613 1.00 26.60 N ATOM 1767 CZ ARG A 239 9.633 42.783 6.612 1.00 29.90 C ATOM 1768 NH1 ARG A 239 9.578 43.371 7.820 1.00 27.83 N ATOM 1769 NH2 ARG A 239 9.090 41.609 6.421 1.00 28.82 N ATOM 1770 N HIS A 240 14.828 48.471 4.199 1.00 16.01 N ATOM 1771 CA HIS A 240 15.482 49.743 4.513 1.00 17.34 C ATOM 1772 C HIS A 240 15.409 50.663 3.315 1.00 17.64 C ATOM 1773 O HIS A 240 14.908 51.799 3.444 1.00 19.19 O ATOM 1774 CB HIS A 240 16.909 49.499 4.979 1.00 17.17 C ATOM 1775 CG HIS A 240 17.667 50.731 5.410 1.00 15.94 C ATOM 1776 ND1 HIS A 240 17.306 51.474 6.524 1.00 19.05 N ATOM 1777 CD2 HIS A 240 18.772 51.324 4.895 1.00 19.64 C ATOM 1778 CE1 HIS A 240 18.177 52.459 6.672 1.00 22.94 C ATOM 1779 NE2 HIS A 240 19.086 52.381 5.714 1.00 17.02 N ATOM 1780 N GLY A 241 15.942 50.210 2.190 1.00 17.12 N ATOM 1781 CA GLY A 241 15.712 50.772 0.880 1.00 17.92 C ATOM 1782 C GLY A 241 16.300 52.146 0.659 1.00 17.86 C ATOM 1783 O GLY A 241 15.826 52.890 -0.201 1.00 18.58 O ATOM 1784 N THR A 242 17.311 52.520 1.431 1.00 17.13 N ATOM 1785 CA THR A 242 17.961 53.794 1.239 1.00 17.88 C ATOM 1786 C THR A 242 19.413 53.781 1.614 1.00 19.84 C ATOM 1787 O THR A 242 19.834 52.962 2.447 1.00 18.89 O ATOM 1788 CB THR A 242 17.212 54.892 2.039 1.00 19.21 C ATOM 1789 OG1 THR A 242 17.833 56.149 1.831 1.00 19.93 O ATOM 1790 CG2 THR A 242 17.316 54.665 3.522 1.00 19.58 C ATOM 1791 N SER A 243 20.193 54.666 0.969 1.00 18.99 N ATOM 1792 CA SER A 243 21.592 54.870 1.324 1.00 17.50 C ATOM 1793 C SER A 243 21.820 56.094 2.215 1.00 20.75 C ATOM 1794 O SER A 243 22.981 56.376 2.593 1.00 17.93 O ATOM 1795 CB SER A 243 22.428 55.048 0.051 1.00 18.51 C ATOM 1796 OG SER A 243 22.469 53.882 -0.808 1.00 18.74 O ATOM 1797 N ASP A 244 20.734 56.758 2.621 1.00 22.12 N ATOM 1798 CA ASP A 244 20.844 58.069 3.286 1.00 24.05 C ATOM 1799 C ASP A 244 21.143 57.917 4.756 1.00 26.16 C ATOM 1800 O ASP A 244 21.671 58.857 5.411 1.00 25.31 O ATOM 1801 CB ASP A 244 19.543 58.864 3.130 1.00 25.84 C ATOM 1802 CG ASP A 244 19.304 59.365 1.744 1.00 27.72 C ATOM 1803 OD1 ASP A 244 20.240 59.469 0.945 1.00 34.38 O ATOM 1804 OD2 ASP A 244 18.178 59.719 1.375 1.00 35.81 O ATOM 1805 N TYR A 245 20.797 56.763 5.320 1.00 24.77 N ATOM 1806 CA TYR A 245 21.161 56.492 6.704 1.00 25.72 C ATOM 1807 C TYR A 245 21.388 55.015 6.995 1.00 22.07 C ATOM 1808 O TYR A 245 20.952 54.203 6.197 1.00 20.79 O ATOM 1809 CB TYR A 245 20.140 57.068 7.662 1.00 26.97 C ATOM 1810 CG TYR A 245 18.747 56.836 7.351 1.00 31.59 C ATOM 1811 CD1 TYR A 245 18.095 55.714 7.872 1.00 37.71 C ATOM 1812 CD2 TYR A 245 18.008 57.761 6.620 1.00 35.06 C ATOM 1813 CE1 TYR A 245 16.730 55.465 7.628 1.00 38.76 C ATOM 1814 CE2 TYR A 245 16.645 57.518 6.339 1.00 40.21 C ATOM 1815 CZ TYR A 245 16.012 56.348 6.859 1.00 41.18 C ATOM 1816 OH TYR A 245 14.672 56.075 6.645 1.00 41.42 O ATOM 1817 N PRO A 246 22.125 54.694 8.050 1.00 21.55 N ATOM 1818 CA PRO A 246 22.549 53.301 8.294 1.00 20.67 C ATOM 1819 C PRO A 246 21.356 52.353 8.541 1.00 18.86 C ATOM 1820 O PRO A 246 20.302 52.752 9.051 1.00 17.94 O ATOM 1821 CB PRO A 246 23.465 53.382 9.515 1.00 21.89 C ATOM 1822 CG PRO A 246 23.114 54.701 10.140 1.00 25.24 C ATOM 1823 CD PRO A 246 22.727 55.633 9.034 1.00 23.52 C ATOM 1824 N LEU A 247 21.537 51.093 8.169 1.00 17.67 N ATOM 1825 CA LEU A 247 20.516 50.086 8.343 1.00 16.60 C ATOM 1826 C LEU A 247 20.432 49.718 9.814 1.00 16.13 C ATOM 1827 O LEU A 247 21.435 49.307 10.434 1.00 14.38 O ATOM 1828 CB LEU A 247 20.885 48.887 7.464 1.00 17.75 C ATOM 1829 CG LEU A 247 19.923 47.702 7.436 1.00 22.71 C ATOM 1830 CD1 LEU A 247 20.431 46.735 6.348 1.00 23.80 C ATOM 1831 CD2 LEU A 247 19.842 46.991 8.729 1.00 25.42 C ATOM 1832 N ASP A 248 19.249 49.887 10.399 1.00 15.51 N ATOM 1833 CA ASP A 248 19.008 49.673 11.828 1.00 16.63 C ATOM 1834 C ASP A 248 18.144 48.433 12.147 1.00 17.10 C ATOM 1835 O ASP A 248 18.338 47.785 13.160 1.00 18.29 O ATOM 1836 CB ASP A 248 18.343 50.930 12.390 1.00 17.43 C ATOM 1837 CG ASP A 248 18.196 50.905 13.914 1.00 21.06 C ATOM 1838 OD1 ASP A 248 19.230 50.764 14.642 1.00 18.23 O ATOM 1839 OD2 ASP A 248 17.071 51.043 14.475 1.00 25.65 O ATOM 1840 N ASP A 249 17.229 48.086 11.260 1.00 18.77 N ATOM 1841 CA ASP A 249 16.272 47.014 11.444 1.00 20.89 C ATOM 1842 C ASP A 249 16.647 45.738 10.713 1.00 19.65 C ATOM 1843 O ASP A 249 16.547 45.692 9.493 1.00 19.56 O ATOM 1844 CB ASP A 249 14.913 47.460 10.970 1.00 20.95 C ATOM 1845 CG ASP A 249 14.432 48.698 11.682 1.00 30.44 C ATOM 1846 OD1 ASP A 249 14.234 48.651 12.915 1.00 35.89 O ATOM 1847 OD2 ASP A 249 14.217 49.780 11.087 1.00 38.76 O ATOM 1848 N ILE A 250 17.106 44.741 11.477 1.00 18.67 N ATOM 1849 CA ILE A 250 17.452 43.452 10.918 1.00 18.15 C ATOM 1850 C ILE A 250 16.205 42.575 11.040 1.00 19.03 C ATOM 1851 O ILE A 250 15.737 42.269 12.148 1.00 20.98 O ATOM 1852 CB ILE A 250 18.606 42.833 11.663 1.00 17.63 C ATOM 1853 CG1 ILE A 250 19.846 43.725 11.498 1.00 19.94 C ATOM 1854 CG2 ILE A 250 18.910 41.429 11.195 1.00 19.23 C ATOM 1855 CD1 ILE A 250 20.465 43.747 10.185 1.00 21.35 C ATOM 1856 N ILE A 251 15.706 42.145 9.902 1.00 18.23 N ATOM 1857 CA ILE A 251 14.429 41.439 9.832 1.00 18.28 C ATOM 1858 C ILE A 251 14.686 39.986 9.857 1.00 17.37 C ATOM 1859 O ILE A 251 14.733 39.294 8.798 1.00 19.81 O ATOM 1860 CB ILE A 251 13.709 41.839 8.552 1.00 19.57 C ATOM 1861 CG1 ILE A 251 13.685 43.314 8.356 1.00 21.28 C ATOM 1862 CG2 ILE A 251 12.283 41.265 8.588 1.00 20.05 C ATOM 1863 CD1 ILE A 251 13.072 44.059 9.364 1.00 17.07 C ATOM 1864 N ILE A 252 14.903 39.458 11.073 1.00 17.21 N ATOM 1865 CA ILE A 252 15.153 38.046 11.248 1.00 18.08 C ATOM 1866 C ILE A 252 13.925 37.226 10.872 1.00 18.38 C ATOM 1867 O ILE A 252 14.043 36.218 10.186 1.00 19.26 O ATOM 1868 CB ILE A 252 15.556 37.731 12.664 1.00 19.01 C ATOM 1869 CG1 ILE A 252 16.972 38.317 12.928 1.00 23.54 C ATOM 1870 CG2 ILE A 252 15.616 36.225 12.946 1.00 21.78 C ATOM 1871 CD1 ILE A 252 17.414 38.107 14.240 1.00 28.03 C ATOM 1872 N ASP A 253 12.778 37.683 11.340 1.00 18.21 N ATOM 1873 CA ASP A 253 11.499 36.940 11.163 1.00 19.20 C ATOM 1874 C ASP A 253 10.611 37.682 10.190 1.00 19.67 C ATOM 1875 O ASP A 253 10.033 38.697 10.578 1.00 20.78 O ATOM 1876 CB ASP A 253 10.842 36.791 12.546 1.00 19.15 C ATOM 1877 CG ASP A 253 9.517 36.010 12.488 1.00 21.95 C ATOM 1878 OD1 ASP A 253 9.145 35.573 11.395 1.00 23.06 O ATOM 1879 OD2 ASP A 253 8.843 35.771 13.516 1.00 26.68 O ATOM 1880 N PRO A 254 10.453 37.205 8.933 1.00 20.70 N ATOM 1881 CA PRO A 254 9.666 37.886 7.912 1.00 23.87 C ATOM 1882 C PRO A 254 8.181 37.858 8.191 1.00 25.78 C ATOM 1883 O PRO A 254 7.404 38.579 7.529 1.00 27.89 O ATOM 1884 CB PRO A 254 10.011 37.046 6.646 1.00 23.29 C ATOM 1885 CG PRO A 254 10.371 35.798 7.144 1.00 23.43 C ATOM 1886 CD PRO A 254 11.025 35.968 8.372 1.00 22.86 C ATOM 1887 N PHE A 255 7.772 37.027 9.151 1.00 26.12 N ATOM 1888 CA PHE A 255 6.394 36.942 9.484 1.00 29.12 C ATOM 1889 C PHE A 255 5.948 38.043 10.470 1.00 33.90 C ATOM 1890 O PHE A 255 4.751 38.264 10.630 1.00 35.73 O ATOM 1891 CB PHE A 255 6.045 35.544 9.968 1.00 27.63 C ATOM 1892 CG PHE A 255 6.245 34.471 8.929 1.00 23.03 C ATOM 1893 CD1 PHE A 255 7.398 33.765 8.866 1.00 19.49 C ATOM 1894 CD2 PHE A 255 5.241 34.141 7.989 1.00 24.61 C ATOM 1895 CE1 PHE A 255 7.616 32.822 7.961 1.00 21.82 C ATOM 1896 CE2 PHE A 255 5.443 33.124 7.097 1.00 20.77 C ATOM 1897 CZ PHE A 255 6.583 32.435 7.070 1.00 22.48 C ATOM 1898 N LYS A 256 6.885 38.771 11.074 1.00 38.40 N ATOM 1899 CA LYS A 256 6.495 39.856 11.967 1.00 42.46 C ATOM 1900 C LYS A 256 5.983 41.065 11.141 1.00 46.16 C ATOM 1901 O LYS A 256 6.606 41.451 10.132 1.00 47.67 O ATOM 1902 CB LYS A 256 7.661 40.234 12.899 1.00 42.36 C ATOM 1903 CG LYS A 256 7.838 39.236 14.046 1.00 43.71 C ATOM 1904 CD LYS A 256 8.950 39.654 15.041 1.00 44.66 C ATOM 1905 CE LYS A 256 9.046 38.645 16.204 1.00 45.20 C ATOM 1906 NZ LYS A 256 9.595 37.307 15.775 1.00 44.89 N ATOM 1907 N ARG A 257 4.858 41.645 11.575 1.00 50.26 N ATOM 1908 CA ARG A 257 4.328 42.871 10.969 1.00 52.87 C ATOM 1909 C ARG A 257 5.094 44.092 11.493 1.00 54.80 C ATOM 1910 O ARG A 257 4.608 44.786 12.374 1.00 56.05 O ATOM 1911 CB ARG A 257 2.808 42.990 11.277 1.00 53.14 C ATOM 1912 N ARG A 258 6.292 44.356 10.965 1.00 57.22 N ATOM 1913 CA ARG A 258 7.166 45.414 11.512 1.00 58.61 C ATOM 1914 C ARG A 258 6.855 46.762 10.857 1.00 59.75 C ATOM 1915 O ARG A 258 7.669 47.321 10.118 1.00 60.67 O ATOM 1916 CB ARG A 258 8.652 45.057 11.326 1.00 58.77 C ATOM 1917 N PRO A 259 5.779 47.355 11.023 1.00 60.71 N TER 1918 PRO A 259 HETATM 1919 O HOH A2001 41.400 34.521 9.433 1.00 47.02 O HETATM 1920 O HOH A2002 39.507 33.981 13.518 1.00 43.20 O HETATM 1921 O HOH A2003 37.957 24.082 12.535 1.00 32.83 O HETATM 1922 O HOH A2004 37.875 30.735 14.603 1.00 37.00 O HETATM 1923 O HOH A2005 34.931 28.810 15.275 1.00 50.12 O HETATM 1924 O HOH A2006 42.727 29.429 2.856 1.00 44.23 O HETATM 1925 O HOH A2007 43.255 27.525 4.843 1.00 41.10 O HETATM 1926 O HOH A2008 37.725 17.850 13.355 1.00 50.77 O HETATM 1927 O HOH A2009 45.093 22.584 -2.493 1.00 40.40 O HETATM 1928 O HOH A2010 48.405 12.094 2.494 1.00 33.70 O HETATM 1929 O HOH A2011 40.861 23.323 0.572 1.00 31.75 O HETATM 1930 O HOH A2012 34.073 4.659 -0.398 1.00 35.41 O HETATM 1931 O HOH A2013 48.721 26.157 9.395 1.00 53.96 O HETATM 1932 O HOH A2014 37.297 19.260 11.073 1.00 23.14 O HETATM 1933 O HOH A2015 44.516 19.771 -2.485 1.00 35.65 O HETATM 1934 O HOH A2016 47.059 14.206 1.224 1.00 29.50 O HETATM 1935 O HOH A2017 48.343 16.516 0.514 1.00 47.16 O HETATM 1936 O HOH A2018 48.082 22.635 5.307 1.00 46.41 O HETATM 1937 O HOH A2019 42.165 11.755 -5.760 1.00 38.42 O HETATM 1938 O HOH A2020 45.109 21.057 -6.479 1.00 49.00 O HETATM 1939 O HOH A2021 40.087 11.039 -4.761 1.00 34.49 O HETATM 1940 O HOH A2022 35.375 6.831 -0.973 1.00 23.95 O HETATM 1941 O HOH A2023 31.401 15.773 -15.606 1.00 50.79 O HETATM 1942 O HOH A2024 31.611 9.196 4.040 1.00 43.18 O HETATM 1943 O HOH A2025 27.203 22.664 15.219 1.00 40.18 O HETATM 1944 O HOH A2026 34.034 41.160 -2.437 1.00 50.14 O HETATM 1945 O HOH A2027 30.778 41.749 -7.141 1.00 49.31 O HETATM 1946 O HOH A2028 20.974 22.194 11.101 1.00 29.21 O HETATM 1947 O HOH A2029 18.024 21.655 9.639 1.00 43.56 O HETATM 1948 O HOH A2030 30.258 27.908 6.410 1.00 40.35 O HETATM 1949 O HOH A2031 24.730 23.137 4.039 1.00 39.46 O HETATM 1950 O HOH A2032 24.912 21.928 1.592 1.00 41.91 O HETATM 1951 O HOH A2033 22.017 19.960 -4.925 1.00 48.37 O HETATM 1952 O HOH A2034 33.393 24.689 -3.277 1.00 40.23 O HETATM 1953 O HOH A2035 26.481 23.813 0.262 1.00 38.90 O HETATM 1954 O HOH A2036 27.807 1.917 -14.158 1.00 46.75 O HETATM 1955 O HOH A2037 42.994 18.784 -8.633 1.00 42.98 O HETATM 1956 O HOH A2038 29.737 20.405 -9.950 1.00 37.48 O HETATM 1957 O HOH A2039 44.817 18.917 -4.820 1.00 34.29 O HETATM 1958 O HOH A2040 40.128 13.585 -13.227 1.00 40.24 O HETATM 1959 O HOH A2041 27.901 -7.017 -3.314 1.00 63.61 O HETATM 1960 O HOH A2042 41.691 14.491 -15.221 1.00 49.12 O HETATM 1961 O HOH A2043 32.973 17.403 -13.577 1.00 50.25 O HETATM 1962 O HOH A2044 25.680 17.641 -7.788 1.00 41.18 O HETATM 1963 O HOH A2045 29.492 16.497 -12.757 1.00 42.01 O HETATM 1964 O HOH A2046 23.834 15.616 -8.800 1.00 35.09 O HETATM 1965 O HOH A2047 21.866 16.972 -2.369 1.00 47.74 O HETATM 1966 O HOH A2048 29.203 13.496 16.425 1.00 36.68 O HETATM 1967 O HOH A2049 18.294 14.851 -3.688 1.00 36.86 O HETATM 1968 O HOH A2050 10.024 11.511 0.808 1.00 41.47 O HETATM 1969 O HOH A2051 24.028 -2.633 13.206 1.00 39.58 O HETATM 1970 O HOH A2052 14.250 6.721 3.240 1.00 33.93 O HETATM 1971 O HOH A2053 9.205 2.844 0.778 1.00 46.18 O HETATM 1972 O HOH A2054 9.543 9.956 -1.328 1.00 41.88 O HETATM 1973 O HOH A2055 38.355 3.598 0.448 1.00 37.16 O HETATM 1974 O HOH A2056 12.464 6.159 5.171 1.00 44.31 O HETATM 1975 O HOH A2057 12.230 3.143 6.503 1.00 42.31 O HETATM 1976 O HOH A2058 15.192 -0.303 6.720 1.00 30.60 O HETATM 1977 O HOH A2059 33.767 23.792 14.728 1.00 41.20 O HETATM 1978 O HOH A2060 19.949 8.532 -10.689 1.00 41.86 O HETATM 1979 O HOH A2061 32.188 42.772 -0.823 1.00 32.26 O HETATM 1980 O HOH A2062 28.324 43.071 -5.039 1.00 34.58 O HETATM 1981 O HOH A2063 23.422 38.941 -5.836 1.00 42.12 O HETATM 1982 O HOH A2064 23.386 42.952 -9.205 1.00 45.81 O HETATM 1983 O HOH A2065 14.616 46.570 -8.356 1.00 47.04 O HETATM 1984 O HOH A2066 27.538 55.841 4.157 1.00 42.09 O HETATM 1985 O HOH A2067 24.633 54.495 13.327 1.00 46.13 O HETATM 1986 O HOH A2068 22.395 51.175 20.298 1.00 30.41 O HETATM 1987 O HOH A2069 24.845 1.746 -15.014 1.00 41.73 O HETATM 1988 O HOH A2070 23.700 3.349 -8.968 1.00 29.39 O HETATM 1989 O HOH A2071 16.912 54.314 -4.526 1.00 56.94 O HETATM 1990 O HOH A2072 36.937 12.999 -4.762 1.00 21.65 O HETATM 1991 O HOH A2073 13.098 48.240 7.935 1.00 35.64 O HETATM 1992 O HOH A2074 6.007 32.544 12.735 1.00 44.52 O HETATM 1993 O HOH A2075 12.017 43.193 12.484 1.00 49.61 O HETATM 1994 O HOH A2076 21.734 18.421 -0.430 1.00 44.88 O HETATM 1995 O HOH A2077 22.780 16.966 6.591 1.00 33.89 O HETATM 1996 O HOH A2078 20.417 19.225 3.774 1.00 40.02 O HETATM 1997 O HOH A2079 14.902 6.201 8.259 1.00 43.26 O HETATM 1998 O HOH A2080 15.350 8.902 4.383 1.00 30.27 O HETATM 1999 O HOH A2081 15.649 1.945 9.368 1.00 41.32 O HETATM 2000 O HOH A2082 19.836 -4.631 2.509 1.00 48.37 O HETATM 2001 O HOH A2083 27.025 -4.457 -3.014 1.00 46.77 O HETATM 2002 O HOH A2084 23.766 -2.824 -4.406 1.00 40.36 O HETATM 2003 O HOH A2085 29.050 -14.295 -17.125 1.00 40.28 O HETATM 2004 O HOH A2086 27.153 -15.538 -17.022 1.00 44.57 O HETATM 2005 O HOH A2087 25.152 -9.295 -17.822 1.00 56.30 O HETATM 2006 O HOH A2088 27.627 -12.875 -11.334 1.00 51.08 O HETATM 2007 O HOH A2089 33.794 2.396 -5.606 1.00 36.69 O HETATM 2008 O HOH A2090 36.736 4.764 -3.840 1.00 50.58 O HETATM 2009 O HOH A2091 32.413 4.416 -2.614 1.00 34.63 O HETATM 2010 O HOH A2092 21.301 13.538 8.674 1.00 24.61 O HETATM 2011 O HOH A2093 27.598 20.764 13.837 1.00 34.97 O HETATM 2012 O HOH A2094 27.945 12.481 14.054 1.00 27.50 O HETATM 2013 O HOH A2095 28.357 4.732 19.731 1.00 37.06 O HETATM 2014 O HOH A2096 23.286 0.226 15.904 1.00 26.84 O HETATM 2015 O HOH A2097 28.305 4.946 23.952 1.00 46.94 O HETATM 2016 O HOH A2098 21.669 8.266 23.171 1.00 45.89 O HETATM 2017 O HOH A2099 18.167 7.075 17.114 1.00 41.00 O HETATM 2018 O HOH A2100 17.572 4.525 11.211 1.00 40.43 O HETATM 2019 O HOH A2101 22.278 -4.359 12.532 1.00 37.84 O HETATM 2020 O HOH A2102 30.927 2.610 14.806 1.00 32.17 O HETATM 2021 O HOH A2103 25.252 -1.174 14.839 1.00 40.82 O HETATM 2022 O HOH A2104 26.944 -3.046 12.957 1.00 34.40 O HETATM 2023 O HOH A2105 27.762 -5.876 7.443 1.00 41.17 O HETATM 2024 O HOH A2106 28.511 -6.059 11.280 1.00 42.73 O HETATM 2025 O HOH A2107 33.586 0.976 16.533 1.00 36.20 O HETATM 2026 O HOH A2108 36.322 2.804 12.704 1.00 44.88 O HETATM 2027 O HOH A2109 35.316 4.400 9.808 1.00 45.20 O HETATM 2028 O HOH A2110 33.455 -3.464 12.527 1.00 25.84 O HETATM 2029 O HOH A2111 37.755 3.106 3.052 1.00 34.06 O HETATM 2030 O HOH A2112 37.592 4.486 5.186 1.00 29.47 O HETATM 2031 O HOH A2113 38.385 11.319 11.423 1.00 40.06 O HETATM 2032 O HOH A2114 37.554 13.838 7.536 1.00 34.44 O HETATM 2033 O HOH A2115 37.401 15.690 12.951 1.00 42.11 O HETATM 2034 O HOH A2116 29.689 18.525 15.762 1.00 45.18 O HETATM 2035 O HOH A2117 35.272 16.340 14.778 1.00 31.64 O HETATM 2036 O HOH A2118 36.035 22.507 12.770 1.00 45.53 O HETATM 2037 O HOH A2119 30.377 20.689 13.248 1.00 26.09 O HETATM 2038 O HOH A2120 27.768 23.346 12.019 1.00 23.83 O HETATM 2039 O HOH A2121 20.688 25.045 15.975 1.00 51.30 O HETATM 2040 O HOH A2122 34.049 26.151 16.396 1.00 46.74 O HETATM 2041 O HOH A2123 29.753 23.143 16.755 1.00 46.72 O HETATM 2042 O HOH A2124 27.317 26.295 18.718 1.00 41.20 O HETATM 2043 O HOH A2125 32.509 33.239 17.993 1.00 46.21 O HETATM 2044 O HOH A2126 31.928 39.912 18.992 1.00 55.90 O HETATM 2045 O HOH A2127 31.330 39.944 13.623 1.00 31.51 O HETATM 2046 O HOH A2128 36.313 36.082 10.098 1.00 41.49 O HETATM 2047 O HOH A2129 35.620 34.458 14.903 1.00 53.38 O HETATM 2048 O HOH A2130 32.886 41.762 3.837 1.00 30.84 O HETATM 2049 O HOH A2131 32.493 43.265 1.690 1.00 36.91 O HETATM 2050 O HOH A2132 29.550 48.722 6.907 1.00 42.95 O HETATM 2051 O HOH A2133 30.201 48.728 3.899 1.00 40.84 O HETATM 2052 O HOH A2134 33.024 47.925 7.962 1.00 48.31 O HETATM 2053 O HOH A2135 33.558 45.703 2.155 1.00 46.14 O HETATM 2054 O HOH A2136 29.601 42.090 -1.923 1.00 22.60 O HETATM 2055 O HOH A2137 24.091 41.893 -6.838 1.00 26.90 O HETATM 2056 O HOH A2138 29.410 45.839 -5.456 1.00 21.25 O HETATM 2057 O HOH A2139 23.790 47.658 -9.779 1.00 38.67 O HETATM 2058 O HOH A2140 15.691 41.577 -7.612 1.00 35.16 O HETATM 2059 O HOH A2141 15.970 44.330 -8.338 1.00 39.03 O HETATM 2060 O HOH A2142 21.840 40.189 -4.015 1.00 28.40 O HETATM 2061 O HOH A2143 15.171 49.551 -5.577 1.00 44.44 O HETATM 2062 O HOH A2144 24.005 49.886 -7.077 1.00 19.04 O HETATM 2063 O HOH A2145 29.040 53.412 4.050 1.00 46.10 O HETATM 2064 O HOH A2146 25.589 55.843 6.415 1.00 35.89 O HETATM 2065 O HOH A2147 27.031 52.500 11.366 1.00 37.46 O HETATM 2066 O HOH A2148 28.502 49.955 9.488 1.00 27.80 O HETATM 2067 O HOH A2149 26.884 47.447 21.870 1.00 23.75 O HETATM 2068 O HOH A2150 24.951 53.086 15.579 1.00 21.91 O HETATM 2069 O HOH A2151 22.287 51.771 17.458 1.00 19.96 O HETATM 2070 O HOH A2152 15.240 44.675 14.320 1.00 41.16 O HETATM 2071 O HOH A2153 16.853 45.493 18.955 1.00 48.62 O HETATM 2072 O HOH A2154 32.187 45.275 11.318 1.00 28.25 O HETATM 2073 O HOH A2155 20.840 46.638 20.635 1.00 51.14 O HETATM 2074 O HOH A2156 24.023 50.198 21.878 1.00 53.10 O HETATM 2075 O HOH A2157 19.131 38.999 17.979 1.00 29.63 O HETATM 2076 O HOH A2158 19.563 44.714 19.022 1.00 41.95 O HETATM 2077 O HOH A2159 19.175 41.126 19.869 1.00 49.28 O HETATM 2078 O HOH A2160 25.533 34.521 16.991 1.00 38.12 O HETATM 2079 O HOH A2161 15.119 31.041 14.872 1.00 47.98 O HETATM 2080 O HOH A2162 18.764 33.358 18.914 1.00 26.21 O HETATM 2081 O HOH A2163 25.015 29.384 13.951 1.00 23.33 O HETATM 2082 O HOH A2164 20.488 27.166 17.286 1.00 47.44 O HETATM 2083 O HOH A2165 20.715 24.413 12.867 1.00 26.52 O HETATM 2084 O HOH A2166 21.735 23.104 4.073 1.00 32.21 O HETATM 2085 O HOH A2167 21.312 22.420 0.898 1.00 50.28 O HETATM 2086 O HOH A2168 26.202 34.931 -2.370 1.00 35.37 O HETATM 2087 O HOH A2169 24.129 36.071 -5.084 1.00 57.86 O HETATM 2088 O HOH A2170 19.832 32.333 1.001 1.00 37.94 O HETATM 2089 O HOH A2171 19.432 33.801 -1.070 1.00 49.28 O HETATM 2090 O HOH A2172 23.471 39.018 -0.996 1.00 17.36 O HETATM 2091 O HOH A2173 20.938 36.779 -3.989 1.00 37.20 O HETATM 2092 O HOH A2174 14.397 35.026 6.136 1.00 46.80 O HETATM 2093 O HOH A2175 13.703 48.951 -1.352 1.00 30.19 O HETATM 2094 O HOH A2176 9.863 49.000 4.928 1.00 42.77 O HETATM 2095 O HOH A2177 14.502 52.392 6.982 1.00 37.54 O HETATM 2096 O HOH A2178 12.564 52.439 4.867 1.00 53.27 O HETATM 2097 O HOH A2179 16.472 55.141 -1.908 1.00 55.05 O HETATM 2098 O HOH A2180 14.888 51.151 -2.520 1.00 35.51 O HETATM 2099 O HOH A2181 15.695 58.000 3.382 1.00 63.76 O HETATM 2100 O HOH A2182 16.943 57.237 -0.497 1.00 53.19 O HETATM 2101 O HOH A2183 19.125 56.195 -1.465 1.00 32.65 O HETATM 2102 O HOH A2184 19.514 54.315 10.826 1.00 34.21 O HETATM 2103 O HOH A2185 16.673 50.241 9.130 1.00 25.37 O HETATM 2104 O HOH A2186 19.836 52.546 16.553 1.00 26.84 O HETATM 2105 O HOH A2187 17.948 45.305 14.403 1.00 28.46 O HETATM 2106 O HOH A2188 16.182 51.806 16.943 1.00 38.93 O HETATM 2107 O HOH A2189 15.324 46.884 7.431 1.00 22.09 O HETATM 2108 O HOH A2190 14.766 51.632 12.854 1.00 39.95 O HETATM 2109 O HOH A2191 15.200 33.901 9.429 1.00 28.49 O HETATM 2110 O HOH A2192 12.525 40.007 13.091 1.00 29.83 O HETATM 2111 O HOH A2193 6.334 35.223 13.741 1.00 38.97 O HETATM 2112 O HOH A2194 8.847 32.576 12.193 1.00 45.67 O HETATM 2113 O HOH A2195 12.238 38.636 15.500 1.00 44.48 O HETATM 2114 O HOH A2196 2.528 46.954 13.972 1.00 59.69 O MASTER 372 0 0 13 7 0 0 6 2113 1 0 21 END