HEADER HYDROLASE 27-JUL-05 2AH2 TITLE TRYPANOSOMA CRUZI TRANS-SIALIDASE IN COMPLEX WITH 2,3- TITLE 2 DIFLUOROSIALIC ACID (COVALENT INTERMEDIATE) COMPND MOL_ID: 1; COMPND 2 MOLECULE: TRANS-SIALIDASE; COMPND 3 CHAIN: A; COMPND 4 EC: 3.2.1.18; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: TRYPANOSOMA CRUZI; SOURCE 3 ORGANISM_COMMON: PROTOZOA; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_COMMON: BACTERIA; SOURCE 6 EXPRESSION_SYSTEM_STRAIN: TOP10F'; SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PTRCHISA KEYWDS TRANSGLYCOSIDASE, COVALENT INTERMEDIATE, TRYPANOSOMA CRUZI, KEYWDS 2 SIALIC ACID EXPDTA X-RAY DIFFRACTION AUTHOR M.F.AMAYA,A.G.WATTS,I.DAMAGER,A.WEHENKEL,T.NGUYEN, AUTHOR 2 A.BUSCHIAZZO,G.PARIS,A.C.FRASCH,S.G.WITHERS,P.M.ALZARI REVDAT 1 23-AUG-05 2AH2 0 SPRSDE 23-AUG-05 2AH2 1S0K JRNL AUTH M.F.AMAYA,A.G.WATTS,I.DAMAGER,A.WEHENKEL,T.NGUYEN, JRNL AUTH 2 A.BUSCHIAZZO,G.PARIS,A.C.FRASCH,S.G.WITHERS, JRNL AUTH 3 P.M.ALZARI JRNL TITL STRUCTURAL INSIGHTS INTO THE CATALYTIC MECHANISM JRNL TITL 2 OF TRYPANOSOMA CRUZI TRANS-SIALIDASE JRNL REF STRUCTURE V. 12 775 2004 JRNL REFN ASTM STRUE6 UK ISSN 0969-2126 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 1.60 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.2.0003 REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON REMARK 3 REMARK 3 REFINEMENT TARGET : ENGH & HUBER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.40 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 89.3 REMARK 3 NUMBER OF REFLECTIONS : 82504 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 + TEST SET) : 0.099 REMARK 3 R VALUE (WORKING SET) : 0.099 REMARK 3 FREE R VALUE : 0.152 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 4134 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH : 1.60 REMARK 3 BIN RESOLUTION RANGE LOW : 1.64 REMARK 3 REFLECTION IN BIN (WORKING SET) : 5424 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 83.63 REMARK 3 BIN R VALUE (WORKING SET) : 0.1030 REMARK 3 BIN FREE R VALUE SET COUNT : 274 REMARK 3 BIN FREE R VALUE : 0.2220 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 ALL ATOMS : 5871 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.98 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.83000 REMARK 3 B22 (A**2) : -0.50000 REMARK 3 B33 (A**2) : 0.41000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 1.16000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.080 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.070 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.039 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.382 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.984 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.968 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5147 ; 0.019 ; 0.021 REMARK 3 BOND LENGTHS OTHERS (A): 4579 ; 0.001 ; 0.020 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7004 ; 1.768 ; 1.937 REMARK 3 BOND ANGLES OTHERS (DEGREES): 10667 ; 0.898 ; 3.000 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 652 ; 7.185 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 220 ;33.744 ;23.636 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 847 ;12.851 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 32 ;17.281 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 767 ; 0.119 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5799 ; 0.009 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 1069 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 922 ; 0.227 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 4789 ; 0.201 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2578 ; 0.179 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): 3149 ; 0.084 ; 0.200 REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 611 ; 0.207 ; 0.200 REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 16 ; 0.228 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): 62 ; 0.271 ; 0.200 REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 44 ; 0.381 ; 0.200 REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 4043 ; 2.187 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1314 ; 0.655 ; 1.500 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5150 ; 2.657 ; 2.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2336 ; 4.305 ; 3.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1854 ; 5.514 ; 4.500 REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): 11879 ; 2.413 ;20.000 REMARK 3 SPHERICITY; FREE ATOMS (A**2): 852 ;26.686 ;12.500 REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 9599 ; 6.919 ;12.500 REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 0 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 0 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : BABINET MODEL WITH MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.20 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE REMARK 3 RIDING POSITIONS REMARK 4 REMARK 4 2AH2 COMPLIES WITH FORMAT V. 3.0, 1-DEC-2006 REMARK 4 REMARK 4 THIS IS THE REMEDIATED VERSION OF THIS PDB ENTRY. REMARK 4 REMEDIATED DATA FILE REVISION 3.101 (2007-05-29) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB. REMARK 100 THE RCSB ID CODE IS RCSB033885. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 16-APR-2003 REMARK 200 TEMPERATURE (KELVIN) : 110.0 REMARK 200 PH : 7.50 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ESRF REMARK 200 BEAMLINE : ID14-1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.934 REMARK 200 MONOCHROMATOR : DIAMOND (111), LAUE GEOMETRY, REMARK 200 150 MICRONS THIN REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : HKL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 82813 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600 REMARK 200 RESOLUTION RANGE LOW (A) : 28.400 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 89.2 REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : 0.04200 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : NULL REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.63 REMARK 200 COMPLETENESS FOR SHELL (%) : 83.8 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.20100 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS REMARK 200 SOFTWARE USED: AMORE REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 51.60 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, TRIS-HCL, ISOPROPANOL, PH REMARK 280 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,1/2+Y,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 64.34500 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT REMARK 300 WHICH CONSISTS OF 1 CHAIN(S). SEE REMARK 350 FOR REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S). REMARK 350 REMARK 350 GENERATING THE BIOMOLECULE REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 APPLY THE FOLLOWING TO CHAINS: A 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 -13 REMARK 465 GLY A -12 REMARK 465 GLY A -11 REMARK 465 SER A -10 REMARK 465 HIS A -9 REMARK 465 HIS A -8 REMARK 465 HIS A -7 REMARK 465 HIS A -6 REMARK 465 HIS A -5 REMARK 465 HIS A -4 REMARK 465 GLY A -3 REMARK 465 MET A -2 REMARK 465 ALA A -1 REMARK 465 SER A 0 REMARK 465 ASP A 400 REMARK 465 PRO A 401 REMARK 465 ALA A 402 REMARK 465 ALA A 403 REMARK 465 SER A 404 REMARK 465 SER A 405 REMARK 465 SER A 406 REMARK 465 GLU A 407 REMARK 465 ARG A 408 REMARK 465 ASP A 634 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 MET A 633 CB CG SD CE 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 REMARK 500 NZ LYS A 215 O HOH 863 1.77 REMARK 500 O HOH 227 O HOH 827 1.80 REMARK 500 O HOH 326 O HOH 859 1.86 REMARK 500 OE2 GLU A 576 O HOH 596 1.89 REMARK 500 O HOH 384 O HOH 825 1.89 REMARK 500 OD2 ASP A 59 O HOH 955 2.02 REMARK 500 O HOH 499 O HOH 920 2.05 REMARK 500 OG SER A 394 O HOH 757 2.10 REMARK 500 O HOH 496 O HOH 761 2.10 REMARK 500 O HOH 666 O HOH 879 2.12 REMARK 500 O HOH 245 O HOH 869 2.13 REMARK 500 O HOH 466 O HOH 680 2.14 REMARK 500 O HOH 576 O HOH 738 2.16 REMARK 500 O HOH 369 O HOH 858 2.17 REMARK 500 O HOH 449 O HOH 682 2.17 REMARK 500 O HOH 355 O HOH 732 2.18 REMARK 500 O HOH 530 O HOH 741 2.19 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 O HOH 17 O HOH 873 1556 1.40 REMARK 500 O HOH 201 O HOH 954 1554 1.86 REMARK 500 O HOH 362 O HOH 806 2555 2.03 REMARK 500 O HOH 92 O HOH 753 1556 2.10 REMARK 500 O HOH 209 O HOH 431 2555 2.15 REMARK 500 O HOH 718 O HOH 869 2545 2.17 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3) REMARK 500 REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 ILE A 49 CG1 ILE A 49 CD1 -0.143 REMARK 500 LYS A 102 CD LYS A 102 CE -0.186 REMARK 500 LYS A 105 CG LYS A 105 CD -0.125 REMARK 500 MET A 259 CB MET A 259 CG -0.132 REMARK 500 VAL A 420 CB VAL A 420 CG1 -0.132 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 LYS A 12 CD - CE - NZ ANGL. DEV. = 14.9 DEGREES REMARK 500 ARG A 117 CB - CG - CD ANGL. DEV. = 10.8 DEGREES REMARK 500 MET A 259 CB - CG - SD ANGL. DEV. = 16.8 DEGREES REMARK 525 REMARK 525 SOLVENT REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH 753 DISTANCE = 5.09 ANGSTROMS REMARK 525 HOH 818 DISTANCE = 5.39 ANGSTROMS REMARK 600 REMARK 600 HETEROGEN REMARK 600 THE COVALENT SIALO-TYROSINE ADDUCT IS THE PRODUCT OF THE REMARK 600 REACTION OF 2,3-DIFLUOROSIALIC ACID WITH THE ENZYME REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 2AGS RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF TRYPANOSOMA RANGELI SIALIDASE IN REMARK 900 INCOMPLEX WITH 2-KETO-3-DEOXY-D-GLYCERO-D-GALACTO-2,3_ REMARK 900 DIFLUORO-NONONIC ACID (2,3-DIFLUORO-KDN) REMARK 900 RELATED ID: 2A75 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF TRYPANOSOMA RANGELI SIALIDASE IN REMARK 900 COMPLEX WITH 2,3- DIFLUOROSIALIC ACID (COVALENT REMARK 900 INTERMEDIATE) REMARK 999 REMARK 999 SEQUENCE REMARK 999 AUTHORS INDICATE THAT THE SEQUENCE IN THE DATABASE IS REMARK 999 INCORRECT DBREF 2AH2 A 1 634 UNP Q26966 Q26966_TRYCR 2 635 SEQADV 2AH2 MET A -13 UNP Q26966 CLONING ARTIFACT SEQADV 2AH2 GLY A -12 UNP Q26966 CLONING ARTIFACT SEQADV 2AH2 GLY A -11 UNP Q26966 CLONING ARTIFACT SEQADV 2AH2 SER A -10 UNP Q26966 CLONING ARTIFACT SEQADV 2AH2 HIS A -9 UNP Q26966 HIS TAG SEQADV 2AH2 HIS A -8 UNP Q26966 HIS TAG SEQADV 2AH2 HIS A -7 UNP Q26966 HIS TAG SEQADV 2AH2 HIS A -6 UNP Q26966 HIS TAG SEQADV 2AH2 HIS A -5 UNP Q26966 HIS TAG SEQADV 2AH2 HIS A -4 UNP Q26966 HIS TAG SEQADV 2AH2 GLY A -3 UNP Q26966 CLONING ARTIFACT SEQADV 2AH2 MET A -2 UNP Q26966 CLONING ARTIFACT SEQADV 2AH2 ALA A -1 UNP Q26966 CLONING ARTIFACT SEQADV 2AH2 SER A 0 UNP Q26966 CLONING ARTIFACT SEQADV 2AH2 PHE A 58 UNP Q26966 ASN 59 ENGINEERED SEQADV 2AH2 THR A 262 UNP Q26966 SER 263 SEE REMARK 999 SEQADV 2AH2 HIS A 476 UNP Q26966 ARG 477 SEE REMARK 999 SEQADV 2AH2 LEU A 484 UNP Q26966 VAL 485 SEE REMARK 999 SEQADV 2AH2 LYS A 495 UNP Q26966 SER 496 ENGINEERED SEQADV 2AH2 GLY A 496 UNP Q26966 VAL 497 ENGINEERED SEQADV 2AH2 LYS A 520 UNP Q26966 GLU 521 ENGINEERED SEQADV 2AH2 VAL A 558 UNP Q26966 GLU 559 SEE REMARK 999 SEQADV 2AH2 GLY A 593 UNP Q26966 ASP 594 ENGINEERED SEQADV 2AH2 ASP A 597 UNP Q26966 ILE 598 ENGINEERED SEQADV 2AH2 ARG A 599 UNP Q26966 HIS 600 ENGINEERED SEQRES 1 A 648 MET GLY GLY SER HIS HIS HIS HIS HIS HIS GLY MET ALA SEQRES 2 A 648 SER LEU ALA PRO GLY SER SER ARG VAL GLU LEU PHE LYS SEQRES 3 A 648 ARG GLN SER SER LYS VAL PRO PHE GLU LYS ASP GLY LYS SEQRES 4 A 648 VAL THR GLU ARG VAL VAL HIS SER PHE ARG LEU PRO ALA SEQRES 5 A 648 LEU VAL ASN VAL ASP GLY VAL MET VAL ALA ILE ALA ASP SEQRES 6 A 648 ALA ARG TYR GLU THR SER PHE ASP ASN SER LEU ILE ASP SEQRES 7 A 648 THR VAL ALA LYS TYR SER VAL ASP ASP GLY GLU THR TRP SEQRES 8 A 648 GLU THR GLN ILE ALA ILE LYS ASN SER ARG ALA SER SER SEQRES 9 A 648 VAL SER ARG VAL VAL ASP PRO THR VAL ILE VAL LYS GLY SEQRES 10 A 648 ASN LYS LEU TYR VAL LEU VAL GLY SER TYR ASN SER SER SEQRES 11 A 648 ARG SER TYR TRP THR SER HIS GLY ASP ALA ARG ASP TRP SEQRES 12 A 648 ASP ILE LEU LEU ALA VAL GLY GLU VAL THR LYS SER THR SEQRES 13 A 648 ALA GLY GLY LYS ILE THR ALA SER ILE LYS TRP GLY SER SEQRES 14 A 648 PRO VAL SER LEU LYS GLU PHE PHE PRO ALA GLU MET GLU SEQRES 15 A 648 GLY MET HIS THR ASN GLN PHE LEU GLY GLY ALA GLY VAL SEQRES 16 A 648 ALA ILE VAL ALA SER ASN GLY ASN LEU VAL TYR PRO VAL SEQRES 17 A 648 GLN VAL THR ASN LYS LYS LYS GLN VAL PHE SER LYS ILE SEQRES 18 A 648 PHE TYR SER GLU ASP GLU GLY LYS THR TRP LYS PHE GLY SEQRES 19 A 648 LYS GLY ARG SER ALA PHE GLY CYS SER GLU PRO VAL ALA SEQRES 20 A 648 LEU GLU TRP GLU GLY LYS LEU ILE ILE ASN THR ARG VAL SEQRES 21 A 648 ASP TYR ARG ARG ARG LEU VAL TYR GLU SER SER ASP MET SEQRES 22 A 648 GLY ASN THR TRP LEU GLU ALA VAL GLY THR LEU SER ARG SEQRES 23 A 648 VAL TRP GLY PRO SER PRO LYS SER ASN GLN PRO GLY SER SEQRES 24 A 648 GLN SER SER PHE THR ALA VAL THR ILE GLU GLY MET ARG SEQRES 25 A 648 VAL MET LEU PHE THR HIS PRO LEU ASN PHE LYS GLY ARG SEQRES 26 A 648 TRP LEU ARG ASP ARG LEU ASN LEU TRP LEU THR ASP ASN SEQRES 27 A 648 GLN ARG ILE TYR ASN VAL GLY GLN VAL SER ILE GLY ASP SEQRES 28 A 648 GLU ASN SER ALA TYR SER SER VAL LEU TYR LYS ASP ASP SEQRES 29 A 648 LYS LEU TYR CYS LEU HIS GLU ILE ASN SER ASN GLU VAL SEQRES 30 A 648 TYR SER LEU VAL PHE ALA ARG LEU VAL GLY GLU LEU ARG SEQRES 31 A 648 ILE ILE LYS SER VAL LEU GLN SER TRP LYS ASN TRP ASP SEQRES 32 A 648 SER HIS LEU SER SER ILE CYS THR PRO ALA ASP PRO ALA SEQRES 33 A 648 ALA SER SER SER GLU ARG GLY CYS GLY PRO ALA VAL THR SEQRES 34 A 648 THR VAL GLY LEU VAL GLY PHE LEU SER HIS SER ALA THR SEQRES 35 A 648 LYS THR GLU TRP GLU ASP ALA TYR ARG CYS VAL ASN ALA SEQRES 36 A 648 SER THR ALA ASN ALA GLU ARG VAL PRO ASN GLY LEU LYS SEQRES 37 A 648 PHE ALA GLY VAL GLY GLY GLY ALA LEU TRP PRO VAL SER SEQRES 38 A 648 GLN GLN GLY GLN ASN GLN ARG TYR HIS PHE ALA ASN HIS SEQRES 39 A 648 ALA PHE THR LEU VAL ALA SER VAL THR ILE HIS GLU VAL SEQRES 40 A 648 PRO LYS GLY ALA SER PRO LEU LEU GLY ALA SER LEU ASP SEQRES 41 A 648 SER SER GLY GLY LYS LYS LEU LEU GLY LEU SER TYR ASP SEQRES 42 A 648 LYS ARG HIS GLN TRP GLN PRO ILE TYR GLY SER THR PRO SEQRES 43 A 648 VAL THR PRO THR GLY SER TRP GLU MET GLY LYS ARG TYR SEQRES 44 A 648 HIS VAL VAL LEU THR MET ALA ASN LYS ILE GLY SER VAL SEQRES 45 A 648 TYR ILE ASP GLY GLU PRO LEU GLU GLY SER GLY GLN THR SEQRES 46 A 648 VAL VAL PRO ASP GLU ARG THR PRO ASP ILE SER HIS PHE SEQRES 47 A 648 TYR VAL GLY GLY TYR LYS ARG SER GLY MET PRO THR ASP SEQRES 48 A 648 SER ARG VAL THR VAL ASN ASN VAL LEU LEU TYR ASN ARG SEQRES 49 A 648 GLN LEU ASN ALA GLU GLU ILE ARG THR LEU PHE LEU SER SEQRES 50 A 648 GLN ASP LEU ILE GLY THR GLU ALA HIS MET ASP HET CL 1001 1 HET FSI A 700 21 HET GOL 1800 6 HET GOL 1801 6 HET GOL 1802 6 HET IPA 1903 4 HETNAM CL CHLORIDE ION HETNAM FSI 5-(ACETYLAMINO)-2,6-ANHYDRO-3,5-DIDEOXY-3- HETNAM 2 FSI FLUORONONONIC ACID HETNAM GOL GLYCEROL HETNAM IPA ISOPROPYL ALCOHOL HETSYN FSI 3-FLUOROSIALIC ACID FORMUL 2 CL CL 1- FORMUL 3 FSI C11 H18 F N O8 FORMUL 4 GOL 3(C3 H8 O3) FORMUL 7 IPA C3 H8 O FORMUL 8 HOH *850(H2 O) HELIX 1 1 TYR A 119 HIS A 123 5 5 HELIX 2 2 THR A 142 LYS A 146 5 5 HELIX 3 3 LYS A 160 PHE A 163 5 4 HELIX 4 4 LEU A 371 ILE A 395 1 25 HELIX 5 5 SER A 467 GLY A 470 5 4 HELIX 6 6 TYR A 475 ASN A 479 5 5 HELIX 7 7 ASN A 613 SER A 623 1 11 HELIX 8 8 THR A 629 MET A 633 5 5 SHEET 1 A 4 SER A 6 PHE A 11 0 SHEET 2 A 4 VAL A 363 ARG A 370 -1 O ARG A 370 N SER A 6 SHEET 3 A 4 LYS A 351 SER A 360 -1 N CYS A 354 O ALA A 369 SHEET 4 A 4 SER A 343 LYS A 348 -1 N LYS A 348 O LYS A 351 SHEET 1 B 2 LYS A 17 LYS A 22 0 SHEET 2 B 2 LYS A 25 VAL A 30 -1 O ARG A 29 N VAL A 18 SHEET 1 C 4 SER A 33 VAL A 42 0 SHEET 2 C 4 VAL A 45 ARG A 53 -1 O VAL A 45 N VAL A 42 SHEET 3 C 4 ILE A 63 SER A 70 -1 O LYS A 68 N ALA A 48 SHEET 4 C 4 GLU A 78 ILE A 83 -1 O GLN A 80 N ALA A 67 SHEET 1 D 3 THR A 148 TRP A 153 0 SHEET 2 D 3 TRP A 129 SER A 141 -1 N THR A 139 O SER A 150 SHEET 3 D 3 VAL A 157 SER A 158 -1 O VAL A 157 N LEU A 133 SHEET 1 E 5 THR A 148 TRP A 153 0 SHEET 2 E 5 TRP A 129 SER A 141 -1 N THR A 139 O SER A 150 SHEET 3 E 5 LYS A 105 TYR A 113 -1 N VAL A 110 O LEU A 132 SHEET 4 E 5 ARG A 93 LYS A 102 -1 N ILE A 100 O TYR A 107 SHEET 5 E 5 GLY A 180 VAL A 181 1 O GLY A 180 N VAL A 99 SHEET 1 F 4 GLU A 166 MET A 167 0 SHEET 2 F 4 MET A 170 GLY A 177 -1 O MET A 170 N MET A 167 SHEET 3 F 4 LEU A 190 ASN A 198 -1 O THR A 197 N ASN A 173 SHEET 4 F 4 ILE A 183 VAL A 184 -1 N ILE A 183 O VAL A 191 SHEET 1 G 5 GLU A 166 MET A 167 0 SHEET 2 G 5 MET A 170 GLY A 177 -1 O MET A 170 N MET A 167 SHEET 3 G 5 LEU A 190 ASN A 198 -1 O THR A 197 N ASN A 173 SHEET 4 G 5 VAL A 203 SER A 210 -1 O PHE A 204 N VAL A 196 SHEET 5 G 5 LYS A 218 PHE A 219 -1 O LYS A 218 N TYR A 209 SHEET 1 H 4 SER A 229 TRP A 236 0 SHEET 2 H 4 LYS A 239 ARG A 245 -1 O ASN A 243 N VAL A 232 SHEET 3 H 4 VAL A 253 SER A 256 -1 O SER A 256 N LEU A 240 SHEET 4 H 4 LEU A 264 GLU A 265 -1 O LEU A 264 N GLU A 255 SHEET 1 I 4 PHE A 289 ILE A 294 0 SHEET 2 I 4 MET A 297 PRO A 305 -1 O VAL A 299 N VAL A 292 SHEET 3 I 4 LEU A 317 THR A 322 -1 O THR A 322 N MET A 300 SHEET 4 I 4 ILE A 327 GLN A 332 -1 O TYR A 328 N LEU A 321 SHEET 1 J 7 ALA A 446 VAL A 449 0 SHEET 2 J 7 GLY A 452 PHE A 455 -1 O LYS A 454 N GLU A 447 SHEET 3 J 7 VAL A 600 TYR A 608 -1 O VAL A 600 N PHE A 455 SHEET 4 J 7 ALA A 481 ILE A 490 -1 N THR A 483 O TYR A 608 SHEET 5 J 7 ARG A 544 ALA A 552 -1 O VAL A 547 N ALA A 486 SHEET 6 J 7 ILE A 555 ILE A 560 -1 O TYR A 559 N VAL A 548 SHEET 7 J 7 GLU A 563 PRO A 564 -1 O GLU A 563 N ILE A 560 SHEET 1 K13 TRP A 524 TYR A 528 0 SHEET 2 K13 LYS A 512 ASP A 519 -1 N SER A 517 O GLN A 525 SHEET 3 K13 ALA A 497 SER A 504 -1 N LEU A 501 O LEU A 516 SHEET 4 K13 HIS A 583 VAL A 586 -1 O HIS A 583 N SER A 504 SHEET 5 K13 GLY A 461 PRO A 465 -1 N TRP A 464 O PHE A 584 SHEET 6 K13 ALA A 441 ALA A 444 -1 N SER A 442 O LEU A 463 SHEET 7 K13 GLU A 431 ASP A 434 -1 N TRP A 432 O ALA A 441 SHEET 8 K13 LEU A 419 ALA A 427 -1 N SER A 426 O GLU A 433 SHEET 9 K13 VAL A 600 TYR A 608 -1 O LEU A 607 N VAL A 420 SHEET 10 K13 ALA A 481 ILE A 490 -1 N THR A 483 O TYR A 608 SHEET 11 K13 ARG A 544 ALA A 552 -1 O VAL A 547 N ALA A 486 SHEET 12 K13 ILE A 555 ILE A 560 -1 O TYR A 559 N VAL A 548 SHEET 13 K13 GLN A 570 THR A 571 -1 O GLN A 570 N GLY A 556 SSBOND 1 CYS A 396 CYS A 410 LINK OH TYR A 342 C2 FSI A 700 CRYST1 54.149 128.690 54.298 90.00 108.74 90.00 P 1 21 1 2 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 0.018468 0.000000 0.006265 0.00000 SCALE2 0.000000 0.007771 0.000000 0.00000 SCALE3 0.000000 0.000000 0.019448 0.00000 ATOM 1 N LEU A 1 -16.259 -4.308 -2.565 1.00 17.08 N ANISOU 1 N LEU A 1 1383 7 372 2631 2475 -437 N ATOM 2 CA LEU A 1 -16.571 -5.027 -1.287 1.00 18.68 C ANISOU 2 CA LEU A 1 1801 -81 80 2763 2533 -264 C ATOM 3 C LEU A 1 -16.583 -6.520 -1.695 1.00 20.37 C ANISOU 3 C LEU A 1 2186 -47 26 2959 2593 -329 C ATOM 4 O LEU A 1 -17.196 -6.820 -2.731 1.00 20.82 O ANISOU 4 O LEU A 1 2211 -247 182 3227 2472 -596 O ATOM 5 CB LEU A 1 -17.939 -4.538 -0.772 1.00 18.53 C ANISOU 5 CB LEU A 1 1839 19 200 2605 2596 -279 C ATOM 6 CG LEU A 1 -18.349 -5.037 0.604 1.00 16.94 C ANISOU 6 CG LEU A 1 1459 -52 319 2680 2295 -393 C ATOM 7 CD1 LEU A 1 -17.262 -4.830 1.702 1.00 14.78 C ANISOU 7 CD1 LEU A 1 1469 51 6 1926 2218 -749 C ATOM 8 CD2 LEU A 1 -19.659 -4.483 1.029 1.00 18.42 C ANISOU 8 CD2 LEU A 1 1832 -87 -39 2509 2656 -195 C ATOM 9 N ALA A 2 -15.858 -7.396 -0.960 1.00 19.54 N ANISOU 9 N ALA A 2 2175 -42 -29 2794 2455 -128 N ATOM 10 CA ALA A 2 -15.661 -8.792 -1.333 1.00 20.09 C ANISOU 10 CA ALA A 2 2198 -145 -274 2819 2615 -192 C ATOM 11 C ALA A 2 -16.950 -9.600 -1.306 1.00 21.43 C ANISOU 11 C ALA A 2 2292 -242 -400 2938 2911 -50 C ATOM 12 O ALA A 2 -17.889 -9.259 -0.620 1.00 20.83 O ANISOU 12 O ALA A 2 2161 -337 -698 2879 2875 -192 O ATOM 13 CB ALA A 2 -14.614 -9.492 -0.414 1.00 20.94 C ANISOU 13 CB ALA A 2 2296 -30 -291 2907 2752 -65 C ATOM 14 N PRO A 3 -16.949 -10.736 -1.988 1.00 22.64 N ANISOU 14 N PRO A 3 2388 -371 -466 3036 3177 -137 N ATOM 15 CA PRO A 3 -18.104 -11.673 -1.917 1.00 23.01 C ANISOU 15 CA PRO A 3 2545 -340 -397 3006 3189 -119 C ATOM 16 C PRO A 3 -18.282 -12.161 -0.531 1.00 21.80 C ANISOU 16 C PRO A 3 2362 -253 -404 2880 3042 -292 C ATOM 17 O PRO A 3 -17.311 -12.525 0.115 1.00 23.25 O ANISOU 17 O PRO A 3 2369 -364 -496 2832 3630 -359 O ATOM 18 CB PRO A 3 -17.710 -12.845 -2.820 1.00 24.63 C ANISOU 18 CB PRO A 3 2820 -276 -357 3243 3292 -95 C ATOM 19 CG PRO A 3 -16.406 -12.561 -3.308 1.00 24.76 C ANISOU 19 CG PRO A 3 2537 -88 -449 3106 3761 -166 C ATOM 20 CD PRO A 3 -15.917 -11.211 -2.904 1.00 23.89 C ANISOU 20 CD PRO A 3 2543 -321 -407 3101 3430 -166 C ATOM 21 N GLY A 4 -19.509 -12.125 -0.058 1.00 19.99 N ANISOU 21 N GLY A 4 2041 -253 -412 2747 2807 -388 N ATOM 22 CA GLY A 4 -19.820 -12.510 1.281 1.00 18.40 C ANISOU 22 CA GLY A 4 1727 -159 -281 2640 2623 -325 C ATOM 23 C GLY A 4 -19.924 -11.346 2.218 1.00 16.86 C ANISOU 23 C GLY A 4 1632 -294 -317 2431 2342 -305 C ATOM 24 O GLY A 4 -20.544 -11.453 3.278 1.00 18.03 O ANISOU 24 O GLY A 4 1899 -501 -486 2440 2512 -104 O ATOM 25 N SER A 5 -19.360 -10.210 1.832 1.00 15.42 N ANISOU 25 N SER A 5 1324 -252 -338 2387 2146 -281 N ATOM 26 CA SER A 5 -19.399 -9.033 2.677 1.00 15.16 C ANISOU 26 CA SER A 5 1365 -115 -208 2271 2124 -333 C ATOM 27 C SER A 5 -20.630 -8.177 2.366 1.00 13.73 C ANISOU 27 C SER A 5 1169 -78 -280 2109 1936 -431 C ATOM 28 O SER A 5 -21.294 -8.309 1.332 1.00 17.00 O ANISOU 28 O SER A 5 1758 35 -396 2684 2017 -379 O ATOM 29 CB SER A 5 -18.131 -8.246 2.501 1.00 14.54 C ANISOU 29 CB SER A 5 1161 -63 -124 2369 1991 -287 C ATOM 30 OG SER A 5 -16.994 -9.038 2.767 1.00 14.71 O ANISOU 30 OG SER A 5 1139 47 -18 2632 1816 -424 O ATOM 31 N SER A 6 -20.967 -7.305 3.296 1.00 13.74 N ANISOU 31 N SER A 6 1115 -51 -217 2031 2072 -403 N ATOM 32 CA SER A 6 -22.155 -6.487 3.159 1.00 13.24 C ANISOU 32 CA SER A 6 1048 -83 -82 1915 2066 -357 C ATOM 33 C SER A 6 -22.007 -5.237 3.991 1.00 11.61 C ANISOU 33 C SER A 6 923 -115 -53 1687 1800 -425 C ATOM 34 O SER A 6 -21.108 -5.146 4.851 1.00 12.97 O ANISOU 34 O SER A 6 1115 -156 -177 1926 1887 -566 O ATOM 35 CB SER A 6 -23.404 -7.294 3.620 1.00 14.88 C ANISOU 35 CB SER A 6 1327 -152 18 2030 2297 -419 C ATOM 36 OG SER A 6 -23.274 -7.666 4.978 1.00 16.98 O ANISOU 36 OG SER A 6 1809 -502 383 2157 2483 251 O ATOM 37 N ARG A 7 -22.877 -4.265 3.736 1.00 12.27 N ANISOU 37 N ARG A 7 956 -159 -35 1856 1851 -305 N ATOM 38 CA ARG A 7 -22.841 -3.005 4.460 1.00 12.90 C ANISOU 38 CA ARG A 7 1199 -159 -8 1853 1847 -334 C ATOM 39 C ARG A 7 -24.175 -2.334 4.617 1.00 11.73 C ANISOU 39 C ARG A 7 1071 -165 58 1705 1678 -434 C ATOM 40 O ARG A 7 -25.148 -2.677 3.921 1.00 12.69 O ANISOU 40 O ARG A 7 944 -466 -219 2046 1829 -520 O ATOM 41 CB ARG A 7 -21.844 -1.994 3.824 1.00 12.79 C ANISOU 41 CB ARG A 7 1176 74 84 1884 1797 -185 C ATOM 42 CG ARG A 7 -22.422 -1.328 2.600 1.00 12.19 C ANISOU 42 CG ARG A 7 1405 -308 232 1685 1539 -204 C ATOM 43 CD ARG A 7 -21.357 -0.590 1.848 1.00 12.40 C ANISOU 43 CD ARG A 7 1386 -322 -121 1949 1378 -341 C ATOM 44 NE ARG A 7 -21.927 0.380 0.910 1.00 12.27 N ANISOU 44 NE ARG A 7 1064 26 -102 1797 1799 -306 N ATOM 45 CZ ARG A 7 -21.188 1.165 0.117 1.00 12.12 C ANISOU 45 CZ ARG A 7 1461 -165 240 1701 1443 -532 C ATOM 46 NH1 ARG A 7 -19.866 1.062 0.103 1.00 12.47 N ANISOU 46 NH1 ARG A 7 924 -386 132 2472 1340 -225 N ATOM 47 NH2 ARG A 7 -21.776 2.050 -0.687 1.00 13.04 N ANISOU 47 NH2 ARG A 7 1242 -188 242 2187 1525 -440 N ATOM 48 N VAL A 8 -24.200 -1.383 5.546 1.00 12.79 N ANISOU 48 N VAL A 8 1161 25 82 1917 1779 -468 N ATOM 49 CA VAL A 8 -25.275 -0.450 5.719 1.00 12.81 C ANISOU 49 CA VAL A 8 1110 -69 24 1945 1813 -372 C ATOM 50 C VAL A 8 -24.752 0.985 5.736 1.00 13.02 C ANISOU 50 C VAL A 8 1072 -40 50 1889 1986 -338 C ATOM 51 O VAL A 8 -23.591 1.214 6.046 1.00 12.48 O ANISOU 51 O VAL A 8 888 -20 77 1872 1978 -406 O ATOM 52 CB VAL A 8 -26.084 -0.736 7.025 1.00 12.26 C ANISOU 52 CB VAL A 8 1085 -55 180 1859 1711 -344 C ATOM 53 CG1 VAL A 8 -26.587 -2.139 6.979 1.00 14.96 C ANISOU 53 CG1 VAL A 8 1632 -67 275 2249 1801 167 C ATOM 54 CG2 VAL A 8 -25.279 -0.478 8.243 1.00 14.67 C ANISOU 54 CG2 VAL A 8 1506 -409 75 2316 1752 -160 C ATOM 55 N AGLU A 9 -25.612 1.934 5.395 0.50 13.30 N ANISOU 55 N AGLU A 9 1014 -67 50 1980 2057 -437 N ATOM 56 N BGLU A 9 -25.637 1.940 5.478 0.50 13.63 N ANISOU 56 N BGLU A 9 1040 -33 68 2035 2104 -429 N ATOM 57 CA AGLU A 9 -25.336 3.342 5.621 0.50 13.78 C ANISOU 57 CA AGLU A 9 1070 -41 126 2018 2145 -405 C ATOM 58 CA BGLU A 9 -25.314 3.360 5.594 0.50 14.20 C ANISOU 58 CA BGLU A 9 1097 -14 134 2114 2181 -411 C ATOM 59 C AGLU A 9 -25.671 3.562 7.084 0.50 13.38 C ANISOU 59 C AGLU A 9 968 -44 120 2027 2089 -328 C ATOM 60 C BGLU A 9 -25.627 3.801 7.032 0.50 13.62 C ANISOU 60 C BGLU A 9 999 -35 125 2068 2106 -379 C ATOM 61 O AGLU A 9 -26.856 3.529 7.481 0.50 13.91 O ANISOU 61 O AGLU A 9 1022 -4 263 1970 2291 -86 O ATOM 62 O BGLU A 9 -26.731 4.266 7.340 0.50 14.82 O ANISOU 62 O BGLU A 9 1044 -28 107 2223 2362 -497 O ATOM 63 CB AGLU A 9 -26.210 4.216 4.736 0.50 14.16 C ANISOU 63 CB AGLU A 9 1135 -16 179 2061 2183 -441 C ATOM 64 CB BGLU A 9 -26.114 4.183 4.584 0.50 14.78 C ANISOU 64 CB BGLU A 9 1172 -14 190 2216 2227 -436 C ATOM 65 CG AGLU A 9 -25.772 5.666 4.655 0.50 14.38 C ANISOU 65 CG AGLU A 9 1103 -73 155 2116 2244 -316 C ATOM 66 CG BGLU A 9 -25.497 5.539 4.285 0.50 15.47 C ANISOU 66 CG BGLU A 9 1250 29 180 2254 2372 -282 C ATOM 67 CD AGLU A 9 -26.581 6.463 3.637 0.50 16.15 C ANISOU 67 CD AGLU A 9 1329 -122 113 2291 2516 -528 C ATOM 68 CD BGLU A 9 -26.437 6.523 3.592 0.50 17.24 C ANISOU 68 CD BGLU A 9 1286 20 213 2673 2589 -358 C ATOM 69 OE1AGLU A 9 -27.392 5.814 2.869 0.50 20.67 O ANISOU 69 OE1AGLU A 9 2389 -181 155 2462 3002 -1255 O ATOM 70 OE1BGLU A 9 -27.683 6.534 3.936 0.50 21.80 O ANISOU 70 OE1BGLU A 9 1837 420 132 3529 2916 324 O ATOM 71 OE2AGLU A 9 -26.451 7.735 3.613 0.50 10.72 O ANISOU 71 OE2AGLU A 9 679 -362 85 1325 2066 -251 O ATOM 72 OE2BGLU A 9 -25.940 7.288 2.696 0.50 18.74 O ANISOU 72 OE2BGLU A 9 1578 223 671 3096 2445 -385 O ATOM 73 N LEU A 10 -24.622 3.681 7.909 1.00 13.78 N ANISOU 73 N LEU A 10 1007 -98 91 2144 2081 -340 N ATOM 74 CA LEU A 10 -24.793 3.852 9.353 1.00 13.54 C ANISOU 74 CA LEU A 10 1067 -91 76 2071 2006 -307 C ATOM 75 C LEU A 10 -24.993 5.315 9.790 1.00 13.56 C ANISOU 75 C LEU A 10 1120 37 216 2091 1939 -298 C ATOM 76 O LEU A 10 -25.873 5.625 10.594 1.00 14.34 O ANISOU 76 O LEU A 10 1077 144 30 2132 2240 -148 O ATOM 77 CB LEU A 10 -23.625 3.209 10.114 1.00 13.84 C ANISOU 77 CB LEU A 10 1174 10 -38 2170 1914 -219 C ATOM 78 CG LEU A 10 -23.648 3.352 11.627 1.00 12.30 C ANISOU 78 CG LEU A 10 1036 -70 -3 1960 1677 -290 C ATOM 79 CD1 LEU A 10 -24.909 2.688 12.189 1.00 16.71 C ANISOU 79 CD1 LEU A 10 1761 71 94 2639 1947 16 C ATOM 80 CD2 LEU A 10 -22.444 2.722 12.228 1.00 13.90 C ANISOU 80 CD2 LEU A 10 1336 5 -77 2082 1860 -31 C ATOM 81 N PHE A 11 -24.099 6.196 9.317 1.00 12.51 N ANISOU 81 N PHE A 11 944 -18 263 2144 1664 -350 N ATOM 82 CA PHE A 11 -24.225 7.616 9.557 1.00 13.05 C ANISOU 82 CA PHE A 11 1103 -50 228 2029 1827 -250 C ATOM 83 C PHE A 11 -24.701 8.189 8.224 1.00 12.82 C ANISOU 83 C PHE A 11 1036 -21 259 2047 1787 -240 C ATOM 84 O PHE A 11 -23.904 8.357 7.311 1.00 12.68 O ANISOU 84 O PHE A 11 1136 31 253 1803 1878 -344 O ATOM 85 CB PHE A 11 -22.892 8.245 9.987 1.00 12.85 C ANISOU 85 CB PHE A 11 1190 -23 218 2011 1680 -167 C ATOM 86 CG PHE A 11 -22.331 7.773 11.342 1.00 11.52 C ANISOU 86 CG PHE A 11 1100 -284 94 1583 1691 -150 C ATOM 87 CD1 PHE A 11 -22.266 8.629 12.414 1.00 12.11 C ANISOU 87 CD1 PHE A 11 1370 27 512 1701 1528 -225 C ATOM 88 CD2 PHE A 11 -21.727 6.529 11.454 1.00 11.80 C ANISOU 88 CD2 PHE A 11 1188 -57 582 1832 1460 -295 C ATOM 89 CE1 PHE A 11 -21.678 8.248 13.605 1.00 11.92 C ANISOU 89 CE1 PHE A 11 1569 -107 361 1617 1343 -143 C ATOM 90 CE2 PHE A 11 -21.104 6.109 12.649 1.00 10.60 C ANISOU 90 CE2 PHE A 11 1087 -15 521 1803 1136 -11 C ATOM 91 CZ PHE A 11 -21.089 6.998 13.734 1.00 12.14 C ANISOU 91 CZ PHE A 11 1174 -62 230 1797 1641 12 C ATOM 92 N ALYS A 12 -26.010 8.448 8.107 0.50 13.09 N ANISOU 92 N ALYS A 12 1022 -37 252 2059 1892 -299 N ATOM 93 N BLYS A 12 -25.999 8.526 8.160 0.50 12.81 N ANISOU 93 N BLYS A 12 1046 50 247 1983 1837 -247 N ATOM 94 CA ALYS A 12 -26.608 8.778 6.817 0.50 14.19 C ANISOU 94 CA ALYS A 12 1128 -138 219 2229 2032 -312 C ATOM 95 CA BLYS A 12 -26.704 8.767 6.902 0.50 14.09 C ANISOU 95 CA BLYS A 12 1211 4 200 2148 1993 -235 C ATOM 96 C ALYS A 12 -26.689 10.270 6.670 0.50 13.51 C ANISOU 96 C ALYS A 12 984 85 188 2174 1972 -334 C ATOM 97 C BLYS A 12 -26.778 10.271 6.628 0.50 13.26 C ANISOU 97 C BLYS A 12 1029 158 176 2094 1913 -293 C ATOM 98 O ALYS A 12 -27.337 10.961 7.467 0.50 14.69 O ANISOU 98 O ALYS A 12 1210 50 258 2305 2064 -228 O ATOM 99 O BLYS A 12 -27.550 10.982 7.294 0.50 13.79 O ANISOU 99 O BLYS A 12 1323 152 127 2080 1833 -199 O ATOM 100 CB ALYS A 12 -28.027 8.200 6.685 0.50 14.12 C ANISOU 100 CB ALYS A 12 1022 -168 233 2295 2047 -390 C ATOM 101 CB BLYS A 12 -28.157 8.180 6.966 0.50 13.39 C ANISOU 101 CB BLYS A 12 1030 22 282 2118 1938 -290 C ATOM 102 CG ALYS A 12 -28.077 6.713 6.803 0.50 15.79 C ANISOU 102 CG ALYS A 12 1361 -247 225 2492 2146 -479 C ATOM 103 CG BLYS A 12 -28.336 6.795 7.705 0.50 15.71 C ANISOU 103 CG BLYS A 12 1577 81 27 2199 2190 -176 C ATOM 104 CD ALYS A 12 -29.549 6.231 6.848 0.50 17.27 C ANISOU 104 CD ALYS A 12 1594 -323 82 2556 2411 -221 C ATOM 105 CD BLYS A 12 -29.831 6.471 8.101 0.50 17.74 C ANISOU 105 CD BLYS A 12 1846 -51 65 2490 2402 26 C ATOM 106 CE ALYS A 12 -29.674 4.870 7.547 0.50 18.99 C ANISOU 106 CE ALYS A 12 1638 -408 440 3063 2515 -163 C ATOM 107 CE BLYS A 12 -30.442 7.608 9.017 0.50 22.60 C ANISOU 107 CE BLYS A 12 2523 -134 -108 3109 2954 146 C ATOM 108 NZ ALYS A 12 -31.102 4.465 7.654 0.50 21.79 N ANISOU 108 NZ ALYS A 12 2222 -530 212 3291 2765 -316 N ATOM 109 NZ BLYS A 12 -31.906 7.860 9.293 0.50 21.81 N ANISOU 109 NZ BLYS A 12 2271 -66 359 3240 2772 -162 N ATOM 110 N ARG A 13 -26.020 10.762 5.640 1.00 13.38 N ANISOU 110 N ARG A 13 1054 199 197 2122 1906 -264 N ATOM 111 CA ARG A 13 -26.009 12.156 5.310 1.00 13.93 C ANISOU 111 CA ARG A 13 1136 222 148 2167 1989 -299 C ATOM 112 C ARG A 13 -27.443 12.648 5.114 1.00 14.28 C ANISOU 112 C ARG A 13 1135 175 231 2346 1943 -376 C ATOM 113 O ARG A 13 -28.274 12.007 4.496 1.00 14.02 O ANISOU 113 O ARG A 13 1097 89 261 2357 1871 -517 O ATOM 114 CB ARG A 13 -25.231 12.436 4.019 1.00 13.77 C ANISOU 114 CB ARG A 13 1247 65 54 1935 2049 -447 C ATOM 115 CG ARG A 13 -25.775 11.710 2.785 1.00 14.02 C ANISOU 115 CG ARG A 13 1132 324 95 2076 2119 -586 C ATOM 116 CD ARG A 13 -24.720 11.502 1.677 1.00 15.41 C ANISOU 116 CD ARG A 13 1588 99 268 2179 2086 -302 C ATOM 117 NE ARG A 13 -25.057 10.443 0.766 1.00 13.96 N ANISOU 117 NE ARG A 13 1505 221 18 1980 1818 -44 N ATOM 118 CZ ARG A 13 -24.210 9.815 -0.039 1.00 16.16 C ANISOU 118 CZ ARG A 13 1321 168 -154 2685 2132 -311 C ATOM 119 NH1 ARG A 13 -22.926 10.079 -0.019 1.00 14.08 N ANISOU 119 NH1 ARG A 13 893 253 270 2397 2057 -391 N ATOM 120 NH2 ARG A 13 -24.639 8.822 -0.809 1.00 15.55 N ANISOU 120 NH2 ARG A 13 1304 113 -286 2245 2358 -651 N ATOM 121 N GLN A 14 -27.664 13.857 5.591 1.00 15.23 N ANISOU 121 N GLN A 14 1203 290 243 2367 2214 -303 N ATOM 122 CA GLN A 14 -28.955 14.562 5.454 1.00 15.64 C ANISOU 122 CA GLN A 14 1172 276 339 2547 2222 -300 C ATOM 123 C GLN A 14 -30.193 13.791 5.972 1.00 16.00 C ANISOU 123 C GLN A 14 1016 254 423 2663 2400 -259 C ATOM 124 O GLN A 14 -31.341 13.998 5.519 1.00 17.73 O ANISOU 124 O GLN A 14 928 320 625 3106 2702 -469 O ATOM 125 CB GLN A 14 -29.099 14.930 3.991 1.00 16.62 C ANISOU 125 CB GLN A 14 1336 426 291 2694 2282 -298 C ATOM 126 CG GLN A 14 -28.105 15.956 3.570 1.00 17.52 C ANISOU 126 CG GLN A 14 1543 457 561 2876 2237 -461 C ATOM 127 CD GLN A 14 -28.147 16.281 2.112 1.00 20.00 C ANISOU 127 CD GLN A 14 1956 338 179 3054 2586 -402 C ATOM 128 OE1 GLN A 14 -28.242 15.393 1.270 1.00 26.39 O ANISOU 128 OE1 GLN A 14 2573 10 -146 4095 3358 -614 O ATOM 129 NE2 GLN A 14 -28.071 17.573 1.801 1.00 26.68 N ANISOU 129 NE2 GLN A 14 2798 335 638 3838 3499 -971 N ATOM 130 N SER A 15 -29.942 12.934 6.952 1.00 15.98 N ANISOU 130 N SER A 15 1155 97 449 2700 2214 -126 N ATOM 131 CA SER A 15 -30.951 12.040 7.448 1.00 16.59 C ANISOU 131 CA SER A 15 1245 36 330 2671 2386 -165 C ATOM 132 C SER A 15 -30.756 11.709 8.905 1.00 16.29 C ANISOU 132 C SER A 15 1173 45 260 2644 2372 -177 C ATOM 133 O SER A 15 -31.631 11.967 9.724 1.00 18.29 O ANISOU 133 O SER A 15 1319 75 143 2984 2647 -95 O ATOM 134 CB SER A 15 -30.942 10.744 6.628 1.00 16.55 C ANISOU 134 CB SER A 15 1313 175 334 2621 2353 -230 C ATOM 135 OG SER A 15 -31.915 9.799 7.101 1.00 20.18 O ANISOU 135 OG SER A 15 1844 -65 391 2837 2985 -235 O ATOM 136 N SER A 16 -29.612 11.144 9.260 1.00 16.86 N ANISOU 136 N SER A 16 1294 175 208 2606 2504 20 N ATOM 137 CA SER A 16 -29.374 10.786 10.647 1.00 16.08 C ANISOU 137 CA SER A 16 1298 81 193 2618 2190 22 C ATOM 138 C SER A 16 -29.365 12.036 11.512 1.00 16.69 C ANISOU 138 C SER A 16 1531 114 248 2614 2196 0 C ATOM 139 O SER A 16 -28.752 13.032 11.174 1.00 16.27 O ANISOU 139 O SER A 16 1734 124 324 2508 1937 -43 O ATOM 140 CB SER A 16 -28.053 10.035 10.860 1.00 16.27 C ANISOU 140 CB SER A 16 1520 272 331 2454 2205 -11 C ATOM 141 OG SER A 16 -28.000 8.795 10.182 1.00 16.81 O ANISOU 141 OG SER A 16 1305 119 173 3011 2071 -47 O ATOM 142 N LYS A 17 -29.985 11.928 12.685 1.00 15.83 N ANISOU 142 N LYS A 17 1364 -32 370 2638 2011 177 N ATOM 143 CA LYS A 17 -30.046 13.006 13.633 1.00 16.24 C ANISOU 143 CA LYS A 17 1441 161 317 2718 2008 -64 C ATOM 144 C LYS A 17 -29.120 12.700 14.807 1.00 14.96 C ANISOU 144 C LYS A 17 1286 313 345 2508 1887 -104 C ATOM 145 O LYS A 17 -28.880 11.518 15.162 1.00 15.54 O ANISOU 145 O LYS A 17 1237 279 415 2667 1997 -253 O ATOM 146 CB LYS A 17 -31.478 13.202 14.137 1.00 16.61 C ANISOU 146 CB LYS A 17 1570 178 306 2795 1946 -118 C ATOM 147 CG LYS A 17 -32.413 13.694 13.058 1.00 17.47 C ANISOU 147 CG LYS A 17 1437 102 171 3096 2102 -223 C ATOM 148 CD LYS A 17 -33.805 13.802 13.622 1.00 20.80 C ANISOU 148 CD LYS A 17 1813 253 425 3555 2534 -218 C ATOM 149 CE LYS A 17 -34.800 14.256 12.561 1.00 21.93 C ANISOU 149 CE LYS A 17 1955 307 298 3997 2380 -276 C ATOM 150 NZ LYS A 17 -36.211 14.248 13.107 1.00 25.16 N ANISOU 150 NZ LYS A 17 1803 18 471 4725 3032 -190 N ATOM 151 N VAL A 18 -28.650 13.761 15.423 1.00 15.65 N ANISOU 151 N VAL A 18 1345 321 456 2592 2009 -241 N ATOM 152 CA VAL A 18 -27.857 13.703 16.658 1.00 15.55 C ANISOU 152 CA VAL A 18 1474 305 270 2537 1897 -116 C ATOM 153 C VAL A 18 -28.407 14.715 17.693 1.00 16.23 C ANISOU 153 C VAL A 18 1627 250 213 2500 2037 -23 C ATOM 154 O VAL A 18 -29.130 15.642 17.339 1.00 16.23 O ANISOU 154 O VAL A 18 1584 363 69 2288 2295 177 O ATOM 155 CB VAL A 18 -26.373 14.031 16.357 1.00 15.67 C ANISOU 155 CB VAL A 18 1477 332 254 2508 1967 -231 C ATOM 156 CG1 VAL A 18 -25.801 13.086 15.371 1.00 14.22 C ANISOU 156 CG1 VAL A 18 1259 330 333 2787 1355 -290 C ATOM 157 CG2 VAL A 18 -26.200 15.426 15.876 1.00 16.16 C ANISOU 157 CG2 VAL A 18 1457 523 189 2612 2070 -88 C ATOM 158 N PRO A 19 -28.167 14.464 18.977 1.00 17.34 N ANISOU 158 N PRO A 19 1881 315 94 2625 2081 175 N ATOM 159 CA PRO A 19 -28.647 15.370 20.035 1.00 18.21 C ANISOU 159 CA PRO A 19 1901 250 56 2712 2303 166 C ATOM 160 C PRO A 19 -27.788 16.642 20.142 1.00 18.90 C ANISOU 160 C PRO A 19 1934 226 57 2844 2402 205 C ATOM 161 O PRO A 19 -26.782 16.672 20.867 1.00 19.83 O ANISOU 161 O PRO A 19 1828 167 54 2909 2795 145 O ATOM 162 CB PRO A 19 -28.547 14.502 21.297 1.00 18.27 C ANISOU 162 CB PRO A 19 1796 270 35 2842 2303 316 C ATOM 163 CG PRO A 19 -27.476 13.510 21.003 1.00 18.32 C ANISOU 163 CG PRO A 19 1832 281 199 2895 2235 186 C ATOM 164 CD PRO A 19 -27.604 13.210 19.524 1.00 17.05 C ANISOU 164 CD PRO A 19 1777 305 40 2613 2086 284 C ATOM 165 N PHE A 20 -28.208 17.667 19.405 1.00 20.03 N ANISOU 165 N PHE A 20 1959 294 -86 2917 2732 258 N ATOM 166 CA PHE A 20 -27.532 18.935 19.381 1.00 20.36 C ANISOU 166 CA PHE A 20 2087 261 1 2968 2678 230 C ATOM 167 C PHE A 20 -27.868 19.765 20.624 1.00 21.61 C ANISOU 167 C PHE A 20 2219 263 -152 3126 2865 228 C ATOM 168 O PHE A 20 -29.022 20.150 20.843 1.00 21.50 O ANISOU 168 O PHE A 20 1810 388 -133 3548 2811 408 O ATOM 169 CB PHE A 20 -27.895 19.691 18.095 1.00 20.64 C ANISOU 169 CB PHE A 20 2135 315 0 2908 2799 158 C ATOM 170 CG PHE A 20 -27.311 21.072 18.020 1.00 20.27 C ANISOU 170 CG PHE A 20 2190 279 -112 2832 2679 180 C ATOM 171 CD1 PHE A 20 -25.994 21.245 17.677 1.00 21.07 C ANISOU 171 CD1 PHE A 20 2053 144 -283 2897 3052 268 C ATOM 172 CD2 PHE A 20 -28.098 22.205 18.240 1.00 22.13 C ANISOU 172 CD2 PHE A 20 2555 151 18 2641 3210 252 C ATOM 173 CE1 PHE A 20 -25.432 22.512 17.578 1.00 20.47 C ANISOU 173 CE1 PHE A 20 2046 357 -200 2434 3297 233 C ATOM 174 CE2 PHE A 20 -27.546 23.471 18.132 1.00 22.83 C ANISOU 174 CE2 PHE A 20 2637 318 -313 2676 3360 293 C ATOM 175 CZ PHE A 20 -26.208 23.635 17.799 1.00 20.02 C ANISOU 175 CZ PHE A 20 1905 278 -112 2520 3180 -135 C ATOM 176 N GLU A 21 -26.845 20.097 21.423 1.00 21.60 N ANISOU 176 N GLU A 21 2208 209 -191 3163 2836 254 N ATOM 177 CA GLU A 21 -27.044 20.855 22.646 1.00 23.87 C ANISOU 177 CA GLU A 21 2677 182 -306 3199 3190 257 C ATOM 178 C GLU A 21 -26.606 22.297 22.465 1.00 24.80 C ANISOU 178 C GLU A 21 2873 187 -332 3282 3266 480 C ATOM 179 O GLU A 21 -25.485 22.540 22.016 1.00 24.02 O ANISOU 179 O GLU A 21 2521 214 -345 3019 3585 567 O ATOM 180 CB GLU A 21 -26.185 20.228 23.707 1.00 24.47 C ANISOU 180 CB GLU A 21 2973 36 -434 3335 2990 241 C ATOM 181 CG GLU A 21 -26.420 20.689 25.116 1.00 26.61 C ANISOU 181 CG GLU A 21 3062 229 -358 3748 3300 165 C ATOM 182 CD GLU A 21 -25.118 20.525 25.902 1.00 28.97 C ANISOU 182 CD GLU A 21 3600 110 -647 3751 3654 -226 C ATOM 183 OE1 GLU A 21 -24.405 19.416 25.863 1.00 29.83 O ANISOU 183 OE1 GLU A 21 4033 375 -492 3892 3408 -648 O ATOM 184 OE2 GLU A 21 -24.782 21.551 26.495 1.00 38.78 O ANISOU 184 OE2 GLU A 21 5020 65 -1360 4308 5403 -483 O ATOM 185 N LYS A 22 -27.462 23.262 22.800 1.00 25.80 N ANISOU 185 N LYS A 22 2951 312 -335 3393 3458 609 N ATOM 186 CA LYS A 22 -27.033 24.634 22.817 1.00 27.01 C ANISOU 186 CA LYS A 22 3223 377 -436 3468 3569 619 C ATOM 187 C LYS A 22 -27.839 25.396 23.828 1.00 28.60 C ANISOU 187 C LYS A 22 3349 367 -588 3737 3779 689 C ATOM 188 O LYS A 22 -29.047 25.240 23.847 1.00 29.20 O ANISOU 188 O LYS A 22 3445 599 -853 3755 3893 863 O ATOM 189 CB LYS A 22 -27.250 25.266 21.448 1.00 28.27 C ANISOU 189 CB LYS A 22 3459 339 -377 3537 3742 559 C ATOM 190 CG LYS A 22 -26.628 26.665 21.285 1.00 28.25 C ANISOU 190 CG LYS A 22 3444 451 -350 3438 3850 631 C ATOM 191 CD LYS A 22 -26.915 27.242 19.907 1.00 28.37 C ANISOU 191 CD LYS A 22 3730 459 -331 3357 3691 656 C ATOM 192 CE LYS A 22 -26.240 28.643 19.781 1.00 30.73 C ANISOU 192 CE LYS A 22 4118 437 -158 3555 4001 591 C ATOM 193 NZ LYS A 22 -26.015 29.096 18.409 1.00 33.75 N ANISOU 193 NZ LYS A 22 4591 206 -137 3906 4323 536 N ATOM 194 N ASP A 23 -27.158 26.195 24.641 1.00 30.22 N ANISOU 194 N ASP A 23 3536 438 -616 3944 4000 784 N ATOM 195 CA ASP A 23 -27.814 27.033 25.655 1.00 31.83 C ANISOU 195 CA ASP A 23 3839 335 -469 4099 4154 626 C ATOM 196 C ASP A 23 -28.742 26.178 26.535 1.00 32.89 C ANISOU 196 C ASP A 23 3915 302 -395 4282 4299 648 C ATOM 197 O ASP A 23 -29.860 26.595 26.909 1.00 34.04 O ANISOU 197 O ASP A 23 4116 240 -657 4444 4372 699 O ATOM 198 CB ASP A 23 -28.577 28.162 24.967 1.00 32.41 C ANISOU 198 CB ASP A 23 3875 481 -452 4110 4328 717 C ATOM 199 CG ASP A 23 -27.678 29.089 24.182 1.00 35.00 C ANISOU 199 CG ASP A 23 4454 584 -638 4240 4604 638 C ATOM 200 OD1 ASP A 23 -28.159 29.592 23.128 1.00 40.55 O ANISOU 200 OD1 ASP A 23 5875 802 -402 4387 5143 907 O ATOM 201 OD2 ASP A 23 -26.486 29.359 24.521 1.00 37.30 O ANISOU 201 OD2 ASP A 23 4376 285 -792 4522 5274 684 O ATOM 202 N GLY A 24 -28.274 24.981 26.852 1.00 33.26 N ANISOU 202 N GLY A 24 4034 183 -283 4274 4326 534 N ATOM 203 CA GLY A 24 -28.996 24.076 27.730 1.00 33.65 C ANISOU 203 CA GLY A 24 4035 155 -251 4397 4351 513 C ATOM 204 C GLY A 24 -30.205 23.376 27.141 1.00 33.89 C ANISOU 204 C GLY A 24 4035 92 -177 4442 4398 480 C ATOM 205 O GLY A 24 -30.939 22.697 27.864 1.00 36.56 O ANISOU 205 O GLY A 24 4413 -7 -13 4774 4703 483 O ATOM 206 N LYS A 25 -30.468 23.554 25.862 1.00 33.52 N ANISOU 206 N LYS A 25 3933 148 -253 4423 4379 523 N ATOM 207 CA LYS A 25 -31.575 22.876 25.209 1.00 32.44 C ANISOU 207 CA LYS A 25 3802 147 -300 4243 4279 473 C ATOM 208 C LYS A 25 -30.917 21.829 24.315 1.00 30.78 C ANISOU 208 C LYS A 25 3559 84 -337 4044 4092 530 C ATOM 209 O LYS A 25 -29.891 22.114 23.712 1.00 29.39 O ANISOU 209 O LYS A 25 3149 165 -525 3857 4161 691 O ATOM 210 CB LYS A 25 -32.360 23.901 24.385 1.00 32.97 C ANISOU 210 CB LYS A 25 3861 105 -339 4282 4381 430 C ATOM 211 CG LYS A 25 -33.331 23.294 23.349 1.00 36.02 C ANISOU 211 CG LYS A 25 4394 284 -240 4554 4736 359 C ATOM 212 CD LYS A 25 -34.323 24.272 22.757 1.00 38.54 C ANISOU 212 CD LYS A 25 4717 214 -141 4806 5120 317 C ATOM 213 CE LYS A 25 -33.635 25.367 21.898 1.00 43.78 C ANISOU 213 CE LYS A 25 5356 128 -137 5377 5898 273 C ATOM 214 NZ LYS A 25 -33.642 26.770 22.549 1.00 48.38 N ANISOU 214 NZ LYS A 25 6082 102 -290 5826 6472 216 N ATOM 215 N VAL A 26 -31.470 20.621 24.283 1.00 28.71 N ANISOU 215 N VAL A 26 3105 80 -289 3917 3885 609 N ATOM 216 CA VAL A 26 -31.052 19.579 23.341 1.00 27.54 C ANISOU 216 CA VAL A 26 2915 111 -221 3913 3637 568 C ATOM 217 C VAL A 26 -32.167 19.352 22.344 1.00 26.77 C ANISOU 217 C VAL A 26 2716 163 -226 3921 3534 546 C ATOM 218 O VAL A 26 -33.355 19.230 22.703 1.00 26.94 O ANISOU 218 O VAL A 26 2460 63 -249 4180 3593 678 O ATOM 219 CB VAL A 26 -30.745 18.260 24.063 1.00 27.19 C ANISOU 219 CB VAL A 26 2776 91 -250 3925 3629 548 C ATOM 220 CG1 VAL A 26 -30.301 17.166 23.085 1.00 28.22 C ANISOU 220 CG1 VAL A 26 2979 130 55 3978 3765 666 C ATOM 221 CG2 VAL A 26 -29.691 18.475 25.131 1.00 30.68 C ANISOU 221 CG2 VAL A 26 3284 -21 -131 4352 4021 466 C ATOM 222 N THR A 27 -31.791 19.309 21.084 1.00 25.00 N ANISOU 222 N THR A 27 2508 308 -222 3741 3249 434 N ATOM 223 CA THR A 27 -32.694 19.079 19.976 1.00 25.89 C ANISOU 223 CA THR A 27 2693 324 -133 3745 3398 353 C ATOM 224 C THR A 27 -32.095 18.023 19.020 1.00 24.92 C ANISOU 224 C THR A 27 2543 305 -58 3665 3258 294 C ATOM 225 O THR A 27 -30.895 18.091 18.700 1.00 24.71 O ANISOU 225 O THR A 27 2117 274 144 3845 3426 548 O ATOM 226 CB THR A 27 -32.762 20.376 19.215 1.00 27.00 C ANISOU 226 CB THR A 27 2978 437 -325 3747 3532 100 C ATOM 227 OG1 THR A 27 -33.211 21.414 20.103 1.00 31.74 O ANISOU 227 OG1 THR A 27 3350 535 -425 4512 4195 12 O ATOM 228 CG2 THR A 27 -33.828 20.281 18.181 1.00 31.47 C ANISOU 228 CG2 THR A 27 3662 379 -225 4384 3910 64 C ATOM 229 N GLU A 28 -32.911 17.073 18.591 1.00 22.67 N ANISOU 229 N GLU A 28 2153 257 229 3385 3075 288 N ATOM 230 CA GLU A 28 -32.514 16.097 17.573 1.00 21.78 C ANISOU 230 CA GLU A 28 2091 273 199 3255 2928 113 C ATOM 231 C GLU A 28 -32.362 16.792 16.246 1.00 21.43 C ANISOU 231 C GLU A 28 1903 352 340 3208 3032 -15 C ATOM 232 O GLU A 28 -33.350 17.260 15.652 1.00 24.57 O ANISOU 232 O GLU A 28 1890 705 521 3843 3602 94 O ATOM 233 CB GLU A 28 -33.536 14.981 17.470 1.00 22.43 C ANISOU 233 CB GLU A 28 2145 271 294 3364 3013 76 C ATOM 234 CG GLU A 28 -33.521 14.087 18.671 1.00 24.49 C ANISOU 234 CG GLU A 28 2417 107 198 3605 3283 276 C ATOM 235 CD GLU A 28 -32.307 13.202 18.752 1.00 26.21 C ANISOU 235 CD GLU A 28 2672 -31 245 3895 3390 -183 C ATOM 236 OE1 GLU A 28 -31.657 13.217 19.808 1.00 29.62 O ANISOU 236 OE1 GLU A 28 3221 318 426 4150 3881 -353 O ATOM 237 OE2 GLU A 28 -32.018 12.473 17.778 1.00 26.46 O ANISOU 237 OE2 GLU A 28 2908 394 489 4164 2980 439 O ATOM 238 N ARG A 29 -31.142 16.863 15.764 1.00 19.31 N ANISOU 238 N ARG A 29 1735 386 310 2918 2684 164 N ATOM 239 CA ARG A 29 -30.837 17.708 14.601 1.00 18.75 C ANISOU 239 CA ARG A 29 1691 379 219 2773 2657 5 C ATOM 240 C ARG A 29 -30.246 16.878 13.498 1.00 18.18 C ANISOU 240 C ARG A 29 1689 221 338 2734 2484 -20 C ATOM 241 O ARG A 29 -29.327 16.104 13.741 1.00 17.49 O ANISOU 241 O ARG A 29 1578 419 266 2584 2480 -46 O ATOM 242 CB ARG A 29 -29.850 18.781 15.058 1.00 19.38 C ANISOU 242 CB ARG A 29 1793 413 148 2734 2833 204 C ATOM 243 CG ARG A 29 -29.382 19.707 13.992 1.00 19.07 C ANISOU 243 CG ARG A 29 1694 465 219 2933 2617 -73 C ATOM 244 CD ARG A 29 -28.516 20.828 14.464 1.00 18.68 C ANISOU 244 CD ARG A 29 1649 352 -35 2728 2719 227 C ATOM 245 NE ARG A 29 -28.132 21.690 13.354 1.00 18.59 N ANISOU 245 NE ARG A 29 1389 406 163 2457 3216 -195 N ATOM 246 CZ ARG A 29 -27.447 22.813 13.495 1.00 20.85 C ANISOU 246 CZ ARG A 29 2078 379 293 2710 3132 89 C ATOM 247 NH1 ARG A 29 -27.011 23.232 14.697 1.00 21.63 N ANISOU 247 NH1 ARG A 29 2106 495 459 2418 3693 45 N ATOM 248 NH2 ARG A 29 -27.198 23.533 12.429 1.00 20.87 N ANISOU 248 NH2 ARG A 29 2111 606 395 2786 3031 277 N ATOM 249 N VAL A 30 -30.777 17.028 12.290 1.00 18.17 N ANISOU 249 N VAL A 30 1866 325 333 2714 2324 -62 N ATOM 250 CA VAL A 30 -30.273 16.331 11.094 1.00 17.87 C ANISOU 250 CA VAL A 30 1792 277 362 2661 2336 -114 C ATOM 251 C VAL A 30 -28.902 16.879 10.735 1.00 16.58 C ANISOU 251 C VAL A 30 1661 244 349 2406 2230 -204 C ATOM 252 O VAL A 30 -28.674 18.069 10.835 1.00 19.46 O ANISOU 252 O VAL A 30 1768 167 257 2641 2982 86 O ATOM 253 CB VAL A 30 -31.222 16.551 9.886 1.00 18.11 C ANISOU 253 CB VAL A 30 1720 287 362 3060 2101 -181 C ATOM 254 CG1 VAL A 30 -30.676 15.837 8.662 1.00 20.11 C ANISOU 254 CG1 VAL A 30 2048 515 205 3245 2346 -266 C ATOM 255 CG2 VAL A 30 -32.628 16.013 10.146 1.00 21.85 C ANISOU 255 CG2 VAL A 30 2578 269 471 3328 2395 -340 C ATOM 256 N VAL A 31 -28.001 15.996 10.340 1.00 16.22 N ANISOU 256 N VAL A 31 1544 312 343 2325 2291 -229 N ATOM 257 CA VAL A 31 -26.625 16.338 10.031 1.00 15.37 C ANISOU 257 CA VAL A 31 1551 337 384 2117 2170 -208 C ATOM 258 C VAL A 31 -26.404 16.243 8.504 1.00 16.00 C ANISOU 258 C VAL A 31 1658 360 307 2136 2286 -233 C ATOM 259 O VAL A 31 -26.766 15.261 7.891 1.00 15.57 O ANISOU 259 O VAL A 31 1450 317 452 2102 2364 -226 O ATOM 260 CB VAL A 31 -25.696 15.349 10.766 1.00 15.05 C ANISOU 260 CB VAL A 31 1523 318 344 1909 2285 -252 C ATOM 261 CG1 VAL A 31 -24.207 15.620 10.412 1.00 16.22 C ANISOU 261 CG1 VAL A 31 1417 419 450 2327 2418 -136 C ATOM 262 CG2 VAL A 31 -25.881 15.474 12.250 1.00 16.14 C ANISOU 262 CG2 VAL A 31 1868 269 622 2080 2182 -167 C ATOM 263 N HIS A 32 -25.755 17.245 7.916 1.00 14.49 N ANISOU 263 N HIS A 32 1395 396 377 2108 2001 -252 N ATOM 264 CA HIS A 32 -25.490 17.236 6.490 1.00 14.65 C ANISOU 264 CA HIS A 32 1472 328 244 2077 2016 -201 C ATOM 265 C HIS A 32 -24.551 16.116 6.101 1.00 13.78 C ANISOU 265 C HIS A 32 1384 333 253 1978 1874 -283 C ATOM 266 O HIS A 32 -24.841 15.326 5.227 1.00 13.90 O ANISOU 266 O HIS A 32 1214 390 239 2108 1957 -467 O ATOM 267 CB HIS A 32 -24.900 18.581 6.066 1.00 16.16 C ANISOU 267 CB HIS A 32 1531 330 260 2335 2273 -160 C ATOM 268 CG HIS A 32 -24.590 18.711 4.595 1.00 15.36 C ANISOU 268 CG HIS A 32 1563 455 230 2305 1968 -138 C ATOM 269 ND1 HIS A 32 -23.440 18.207 4.011 1.00 14.92 N ANISOU 269 ND1 HIS A 32 1596 315 92 2374 1698 159 N ATOM 270 CD2 HIS A 32 -25.263 19.347 3.608 1.00 17.34 C ANISOU 270 CD2 HIS A 32 1725 853 316 2703 2158 -235 C ATOM 271 CE1 HIS A 32 -23.434 18.525 2.725 1.00 15.42 C ANISOU 271 CE1 HIS A 32 1381 327 241 2657 1820 281 C ATOM 272 NE2 HIS A 32 -24.528 19.225 2.460 1.00 15.97 N ANISOU 272 NE2 HIS A 32 1707 692 551 2486 1875 -118 N ATOM 273 N SER A 33 -23.410 16.092 6.741 1.00 12.78 N ANISOU 273 N SER A 33 1244 170 147 1931 1681 -192 N ATOM 274 CA SER A 33 -22.316 15.165 6.426 1.00 12.48 C ANISOU 274 CA SER A 33 1279 137 220 1826 1636 -173 C ATOM 275 C SER A 33 -21.649 14.585 7.652 1.00 11.07 C ANISOU 275 C SER A 33 1093 138 117 1682 1430 -172 C ATOM 276 O SER A 33 -21.417 15.284 8.653 1.00 12.39 O ANISOU 276 O SER A 33 1289 417 216 1988 1426 -207 O ATOM 277 CB SER A 33 -21.261 15.866 5.581 1.00 11.59 C ANISOU 277 CB SER A 33 1213 -42 223 1577 1614 -221 C ATOM 278 OG SER A 33 -21.668 16.097 4.242 1.00 14.05 O ANISOU 278 OG SER A 33 1557 55 286 2273 1507 -529 O ATOM 279 N PHE A 34 -21.257 13.309 7.523 1.00 12.35 N ANISOU 279 N PHE A 34 1291 79 263 1935 1465 -207 N ATOM 280 CA PHE A 34 -20.475 12.596 8.517 1.00 11.18 C ANISOU 280 CA PHE A 34 996 90 252 1867 1383 -213 C ATOM 281 C PHE A 34 -19.154 12.201 7.884 1.00 11.69 C ANISOU 281 C PHE A 34 1174 42 112 1935 1330 -139 C ATOM 282 O PHE A 34 -19.128 11.671 6.763 1.00 11.84 O ANISOU 282 O PHE A 34 809 68 127 1935 1753 -122 O ATOM 283 CB PHE A 34 -21.211 11.344 8.996 1.00 12.14 C ANISOU 283 CB PHE A 34 1127 206 446 2038 1448 -179 C ATOM 284 CG PHE A 34 -22.493 11.645 9.711 1.00 11.80 C ANISOU 284 CG PHE A 34 1099 176 361 2110 1273 -253 C ATOM 285 CD1 PHE A 34 -23.717 11.656 9.012 1.00 12.86 C ANISOU 285 CD1 PHE A 34 1154 349 473 2212 1519 -275 C ATOM 286 CD2 PHE A 34 -22.481 11.909 11.072 1.00 12.88 C ANISOU 286 CD2 PHE A 34 1330 144 342 1697 1864 -286 C ATOM 287 CE1 PHE A 34 -24.910 11.945 9.703 1.00 12.71 C ANISOU 287 CE1 PHE A 34 1346 32 -30 1809 1672 -73 C ATOM 288 CE2 PHE A 34 -23.650 12.181 11.779 1.00 13.40 C ANISOU 288 CE2 PHE A 34 1576 359 319 1943 1569 -138 C ATOM 289 CZ PHE A 34 -24.864 12.173 11.087 1.00 12.27 C ANISOU 289 CZ PHE A 34 935 361 217 2198 1530 -332 C ATOM 290 N ARG A 35 -18.071 12.561 8.578 1.00 11.76 N ANISOU 290 N ARG A 35 1103 0 176 1959 1406 -126 N ATOM 291 CA ARG A 35 -16.722 12.339 8.095 1.00 10.66 C ANISOU 291 CA ARG A 35 1080 72 145 1762 1208 -187 C ATOM 292 C ARG A 35 -15.849 11.815 9.246 1.00 10.81 C ANISOU 292 C ARG A 35 1144 56 263 1673 1289 -207 C ATOM 293 O ARG A 35 -16.282 11.722 10.366 1.00 11.17 O ANISOU 293 O ARG A 35 1126 -104 226 1729 1389 -169 O ATOM 294 CB ARG A 35 -16.115 13.601 7.486 1.00 11.34 C ANISOU 294 CB ARG A 35 1238 177 -60 1899 1168 -288 C ATOM 295 CG ARG A 35 -16.785 14.065 6.143 1.00 11.60 C ANISOU 295 CG ARG A 35 1368 -18 237 1680 1357 -81 C ATOM 296 CD ARG A 35 -15.800 14.830 5.288 1.00 11.26 C ANISOU 296 CD ARG A 35 1098 156 240 1722 1457 120 C ATOM 297 NE ARG A 35 -14.689 13.946 4.930 1.00 10.16 N ANISOU 297 NE ARG A 35 1077 -17 -182 1378 1403 -306 N ATOM 298 CZ ARG A 35 -13.521 14.297 4.436 1.00 13.85 C ANISOU 298 CZ ARG A 35 1507 -133 1 1613 2140 -43 C ATOM 299 NH1 ARG A 35 -12.617 13.342 4.177 1.00 13.81 N ANISOU 299 NH1 ARG A 35 1554 -269 68 1556 2134 173 N ATOM 300 NH2 ARG A 35 -13.237 15.560 4.172 1.00 15.98 N ANISOU 300 NH2 ARG A 35 1609 207 272 2005 2455 133 N ATOM 301 N LEU A 36 -14.607 11.492 8.928 1.00 10.47 N ANISOU 301 N LEU A 36 993 57 296 1696 1289 -209 N ATOM 302 CA LEU A 36 -13.621 11.239 9.974 1.00 9.92 C ANISOU 302 CA LEU A 36 1033 64 186 1586 1148 -194 C ATOM 303 C LEU A 36 -13.928 9.979 10.815 1.00 9.46 C ANISOU 303 C LEU A 36 1069 -30 103 1376 1147 -248 C ATOM 304 O LEU A 36 -13.879 10.012 12.053 1.00 9.18 O ANISOU 304 O LEU A 36 1092 -205 67 1361 1034 -161 O ATOM 305 CB LEU A 36 -13.393 12.471 10.853 1.00 11.12 C ANISOU 305 CB LEU A 36 1184 0 223 1507 1532 -130 C ATOM 306 CG LEU A 36 -12.325 13.505 10.413 1.00 9.18 C ANISOU 306 CG LEU A 36 946 159 30 1365 1177 -94 C ATOM 307 CD1 LEU A 36 -10.947 12.985 10.538 1.00 10.15 C ANISOU 307 CD1 LEU A 36 764 -48 296 1767 1325 -292 C ATOM 308 CD2 LEU A 36 -12.625 13.936 8.949 1.00 10.23 C ANISOU 308 CD2 LEU A 36 932 -108 -119 1845 1109 -326 C ATOM 309 N PRO A 37 -14.174 8.858 10.150 1.00 9.85 N ANISOU 309 N PRO A 37 1001 91 214 1410 1330 -255 N ATOM 310 CA PRO A 37 -14.524 7.627 10.864 1.00 9.97 C ANISOU 310 CA PRO A 37 973 1 217 1542 1271 -173 C ATOM 311 C PRO A 37 -13.380 7.129 11.737 1.00 9.07 C ANISOU 311 C PRO A 37 734 -100 285 1616 1095 -197 C ATOM 312 O PRO A 37 -12.233 7.086 11.331 1.00 9.81 O ANISOU 312 O PRO A 37 907 -5 230 1554 1266 -173 O ATOM 313 CB PRO A 37 -14.753 6.623 9.731 1.00 10.74 C ANISOU 313 CB PRO A 37 1098 -99 95 1626 1357 -147 C ATOM 314 CG PRO A 37 -13.953 7.145 8.555 1.00 10.52 C ANISOU 314 CG PRO A 37 952 2 66 1664 1380 -496 C ATOM 315 CD PRO A 37 -14.100 8.655 8.680 1.00 9.05 C ANISOU 315 CD PRO A 37 799 41 327 1409 1230 -375 C ATOM 316 N ALA A 38 -13.755 6.651 12.917 1.00 9.01 N ANISOU 316 N ALA A 38 773 -171 352 1673 975 -128 N ATOM 317 CA ALA A 38 -12.869 5.912 13.841 1.00 10.00 C ANISOU 317 CA ALA A 38 868 -77 352 1577 1355 -51 C ATOM 318 C ALA A 38 -13.718 4.826 14.474 1.00 10.12 C ANISOU 318 C ALA A 38 982 22 386 1699 1161 -54 C ATOM 319 O ALA A 38 -14.710 5.134 15.099 1.00 12.04 O ANISOU 319 O ALA A 38 1014 30 394 1974 1584 235 O ATOM 320 CB ALA A 38 -12.278 6.851 14.878 1.00 10.43 C ANISOU 320 CB ALA A 38 1156 76 365 1581 1222 3 C ATOM 321 N LEU A 39 -13.340 3.565 14.268 1.00 8.75 N ANISOU 321 N LEU A 39 827 -121 307 1453 1045 -152 N ATOM 322 CA LEU A 39 -14.116 2.417 14.741 1.00 10.20 C ANISOU 322 CA LEU A 39 1061 -84 307 1490 1322 -96 C ATOM 323 C LEU A 39 -13.305 1.538 15.662 1.00 10.33 C ANISOU 323 C LEU A 39 1218 -128 348 1568 1139 -149 C ATOM 324 O LEU A 39 -12.255 1.028 15.268 1.00 10.34 O ANISOU 324 O LEU A 39 1407 -111 359 1474 1045 -327 O ATOM 325 CB LEU A 39 -14.585 1.601 13.539 1.00 10.76 C ANISOU 325 CB LEU A 39 1119 -152 291 1713 1255 5 C ATOM 326 CG LEU A 39 -15.468 0.369 13.826 1.00 11.85 C ANISOU 326 CG LEU A 39 1323 -221 276 1679 1500 97 C ATOM 327 CD1 LEU A 39 -16.776 0.738 14.375 1.00 13.23 C ANISOU 327 CD1 LEU A 39 1358 -270 169 1946 1721 130 C ATOM 328 CD2 LEU A 39 -15.646 -0.508 12.592 1.00 11.69 C ANISOU 328 CD2 LEU A 39 1363 24 457 1585 1490 -54 C ATOM 329 N VAL A 40 -13.774 1.389 16.894 1.00 10.51 N ANISOU 329 N VAL A 40 1003 6 377 1629 1359 7 N ATOM 330 CA VAL A 40 -12.991 0.711 17.932 1.00 10.23 C ANISOU 330 CA VAL A 40 1152 -32 497 1563 1170 -204 C ATOM 331 C VAL A 40 -13.847 -0.272 18.729 1.00 11.55 C ANISOU 331 C VAL A 40 1244 120 425 1792 1352 -136 C ATOM 332 O VAL A 40 -15.088 -0.231 18.682 1.00 11.21 O ANISOU 332 O VAL A 40 1148 -131 433 1836 1274 -422 O ATOM 333 CB VAL A 40 -12.337 1.720 18.917 1.00 10.75 C ANISOU 333 CB VAL A 40 1294 -1 535 1631 1159 -61 C ATOM 334 CG1 VAL A 40 -11.375 2.655 18.198 1.00 11.50 C ANISOU 334 CG1 VAL A 40 1640 -171 319 1842 886 -350 C ATOM 335 CG2 VAL A 40 -13.391 2.557 19.645 1.00 9.89 C ANISOU 335 CG2 VAL A 40 1316 -37 239 1721 721 -540 C ATOM 336 N ASN A 41 -13.136 -1.124 19.471 1.00 11.69 N ANISOU 336 N ASN A 41 1428 3 472 1703 1309 -143 N ATOM 337 CA ASN A 41 -13.753 -2.009 20.440 1.00 12.26 C ANISOU 337 CA ASN A 41 1408 -37 513 1817 1431 -136 C ATOM 338 C ASN A 41 -13.328 -1.577 21.813 1.00 13.23 C ANISOU 338 C ASN A 41 1637 -60 371 1769 1621 -121 C ATOM 339 O ASN A 41 -12.123 -1.627 22.126 1.00 13.40 O ANISOU 339 O ASN A 41 1404 74 504 1950 1736 -271 O ATOM 340 CB ASN A 41 -13.277 -3.427 20.182 1.00 12.42 C ANISOU 340 CB ASN A 41 1542 -258 486 1871 1306 -128 C ATOM 341 CG ASN A 41 -13.751 -4.417 21.206 1.00 12.64 C ANISOU 341 CG ASN A 41 1666 8 471 1748 1387 -174 C ATOM 342 OD1 ASN A 41 -14.785 -4.222 21.847 1.00 17.35 O ANISOU 342 OD1 ASN A 41 2937 -359 574 1670 1984 317 O ATOM 343 ND2 ASN A 41 -13.025 -5.522 21.320 1.00 19.78 N ANISOU 343 ND2 ASN A 41 2983 -62 672 1967 2565 23 N ATOM 344 N VAL A 42 -14.290 -1.231 22.667 1.00 13.26 N ANISOU 344 N VAL A 42 1682 -57 290 1696 1657 -178 N ATOM 345 CA VAL A 42 -13.996 -0.914 24.061 1.00 15.10 C ANISOU 345 CA VAL A 42 1899 88 295 2127 1710 -164 C ATOM 346 C VAL A 42 -14.577 -2.009 24.932 1.00 17.05 C ANISOU 346 C VAL A 42 2190 141 239 2416 1873 -12 C ATOM 347 O VAL A 42 -15.751 -1.998 25.247 1.00 16.00 O ANISOU 347 O VAL A 42 2036 -30 301 2595 1445 -172 O ATOM 348 CB VAL A 42 -14.584 0.423 24.483 1.00 16.67 C ANISOU 348 CB VAL A 42 2329 26 52 2278 1725 -115 C ATOM 349 CG1 VAL A 42 -14.089 0.770 25.890 1.00 17.07 C ANISOU 349 CG1 VAL A 42 2173 104 -145 2607 1705 -253 C ATOM 350 CG2 VAL A 42 -14.212 1.461 23.539 1.00 19.18 C ANISOU 350 CG2 VAL A 42 2501 132 49 2418 2367 -211 C ATOM 351 N ASP A 43 -13.730 -3.013 25.212 1.00 18.10 N ANISOU 351 N ASP A 43 2432 137 521 2528 1913 -25 N ATOM 352 CA ASP A 43 -14.070 -4.080 26.159 1.00 18.94 C ANISOU 352 CA ASP A 43 2643 33 416 2577 1973 36 C ATOM 353 C ASP A 43 -15.393 -4.738 25.785 1.00 18.84 C ANISOU 353 C ASP A 43 2531 0 581 2649 1978 152 C ATOM 354 O ASP A 43 -16.206 -5.073 26.658 1.00 23.32 O ANISOU 354 O ASP A 43 3419 153 674 3283 2155 223 O ATOM 355 CB ASP A 43 -14.173 -3.401 27.521 1.00 20.78 C ANISOU 355 CB ASP A 43 3013 -1 287 2837 2043 47 C ATOM 356 CG ASP A 43 -14.097 -4.336 28.685 1.00 24.55 C ANISOU 356 CG ASP A 43 3334 198 333 3410 2582 178 C ATOM 357 OD1 ASP A 43 -13.477 -5.436 28.609 1.00 25.51 O ANISOU 357 OD1 ASP A 43 3489 359 734 3068 3135 -312 O ATOM 358 OD2 ASP A 43 -14.642 -3.971 29.783 1.00 30.71 O ANISOU 358 OD2 ASP A 43 4518 326 297 4978 2171 329 O ATOM 359 N GLY A 44 -15.635 -4.862 24.476 1.00 16.64 N ANISOU 359 N GLY A 44 2468 -74 579 2346 1509 70 N ATOM 360 CA GLY A 44 -16.775 -5.552 23.975 1.00 16.81 C ANISOU 360 CA GLY A 44 2357 -342 530 2329 1701 117 C ATOM 361 C GLY A 44 -17.882 -4.708 23.378 1.00 17.91 C ANISOU 361 C GLY A 44 2423 -548 447 2489 1891 -13 C ATOM 362 O GLY A 44 -18.816 -5.223 22.750 1.00 21.53 O ANISOU 362 O GLY A 44 2870 -884 355 2955 2352 92 O ATOM 363 N VAL A 45 -17.796 -3.398 23.583 1.00 16.06 N ANISOU 363 N VAL A 45 2135 -529 542 2272 1694 259 N ATOM 364 CA VAL A 45 -18.726 -2.445 23.019 1.00 15.51 C ANISOU 364 CA VAL A 45 1801 -465 471 2377 1714 63 C ATOM 365 C VAL A 45 -18.078 -1.788 21.800 1.00 14.11 C ANISOU 365 C VAL A 45 1653 -339 404 2188 1517 39 C ATOM 366 O VAL A 45 -16.954 -1.249 21.865 1.00 14.80 O ANISOU 366 O VAL A 45 1722 -571 525 2485 1413 -226 O ATOM 367 CB VAL A 45 -19.070 -1.371 24.016 1.00 15.92 C ANISOU 367 CB VAL A 45 1716 -498 522 2545 1786 264 C ATOM 368 CG1 VAL A 45 -20.082 -0.396 23.430 1.00 16.64 C ANISOU 368 CG1 VAL A 45 1866 -330 470 2743 1709 262 C ATOM 369 CG2 VAL A 45 -19.621 -2.002 25.325 1.00 17.70 C ANISOU 369 CG2 VAL A 45 2271 -422 767 2672 1780 91 C ATOM 370 N MET A 46 -18.719 -1.942 20.662 1.00 14.74 N ANISOU 370 N MET A 46 1611 -262 406 2173 1814 -155 N ATOM 371 CA MET A 46 -18.231 -1.368 19.411 1.00 14.93 C ANISOU 371 CA MET A 46 1652 -281 197 2270 1748 -114 C ATOM 372 C MET A 46 -18.603 0.136 19.455 1.00 14.37 C ANISOU 372 C MET A 46 1473 -240 420 2229 1755 29 C ATOM 373 O MET A 46 -19.714 0.503 19.817 1.00 14.59 O ANISOU 373 O MET A 46 1301 -414 493 2279 1961 -15 O ATOM 374 CB MET A 46 -18.902 -2.119 18.252 1.00 15.84 C ANISOU 374 CB MET A 46 1661 -333 372 2711 1646 -94 C ATOM 375 CG MET A 46 -18.382 -1.799 16.909 1.00 18.67 C ANISOU 375 CG MET A 46 2234 -248 259 2653 2204 -276 C ATOM 376 SD MET A 46 -19.153 -2.901 15.693 1.00 22.00 S ANISOU 376 SD MET A 46 2724 -72 -501 3350 2282 -804 S ATOM 377 CE MET A 46 -18.364 -4.474 15.900 1.00 19.63 C ANISOU 377 CE MET A 46 1665 -295 119 2947 2845 -737 C ATOM 378 N VAL A 47 -17.642 1.013 19.157 1.00 12.38 N ANISOU 378 N VAL A 47 1158 -124 401 1908 1637 -69 N ATOM 379 CA VAL A 47 -17.897 2.440 19.172 1.00 12.11 C ANISOU 379 CA VAL A 47 1291 -221 244 1869 1442 53 C ATOM 380 C VAL A 47 -17.407 3.048 17.875 1.00 12.01 C ANISOU 380 C VAL A 47 1214 -185 308 1885 1464 0 C ATOM 381 O VAL A 47 -16.290 2.771 17.467 1.00 12.80 O ANISOU 381 O VAL A 47 1187 -296 485 2067 1608 99 O ATOM 382 CB VAL A 47 -17.218 3.134 20.368 1.00 11.82 C ANISOU 382 CB VAL A 47 1232 -144 291 1859 1397 -1 C ATOM 383 CG1 VAL A 47 -17.569 4.574 20.396 1.00 14.57 C ANISOU 383 CG1 VAL A 47 1792 -325 144 2027 1714 -172 C ATOM 384 CG2 VAL A 47 -17.603 2.467 21.693 1.00 13.47 C ANISOU 384 CG2 VAL A 47 1535 -95 251 1907 1675 10 C ATOM 385 N ALA A 48 -18.269 3.841 17.238 1.00 11.15 N ANISOU 385 N ALA A 48 1058 -169 239 1683 1494 59 N ATOM 386 CA ALA A 48 -17.959 4.553 16.027 1.00 11.21 C ANISOU 386 CA ALA A 48 1250 -129 33 1694 1312 5 C ATOM 387 C ALA A 48 -17.992 6.047 16.344 1.00 11.62 C ANISOU 387 C ALA A 48 1275 -9 78 1726 1410 60 C ATOM 388 O ALA A 48 -19.029 6.604 16.777 1.00 12.90 O ANISOU 388 O ALA A 48 1296 149 -136 2002 1600 91 O ATOM 389 CB ALA A 48 -18.980 4.244 14.941 1.00 9.68 C ANISOU 389 CB ALA A 48 1150 -268 -157 1438 1088 -251 C ATOM 390 N AILE A 49 -16.848 6.689 16.115 0.72 10.14 N ANISOU 390 N AILE A 49 840 -42 44 1652 1358 2 N ATOM 391 N BILE A 49 -16.849 6.696 16.156 0.28 11.63 N ANISOU 391 N BILE A 49 1259 5 24 1766 1391 19 N ATOM 392 CA AILE A 49 -16.669 8.103 16.365 0.72 10.98 C ANISOU 392 CA AILE A 49 1152 -102 103 1674 1343 70 C ATOM 393 CA BILE A 49 -16.747 8.129 16.350 0.28 12.23 C ANISOU 393 CA BILE A 49 1452 -3 22 1824 1371 26 C ATOM 394 C AILE A 49 -16.443 8.789 15.004 0.72 11.45 C ANISOU 394 C AILE A 49 1188 13 73 1699 1462 60 C ATOM 395 C BILE A 49 -16.493 8.777 14.997 0.28 12.03 C ANISOU 395 C BILE A 49 1390 19 24 1741 1437 35 C ATOM 396 O AILE A 49 -15.849 8.186 14.067 0.72 11.96 O ANISOU 396 O AILE A 49 1304 159 -39 1699 1540 238 O ATOM 397 O BILE A 49 -15.914 8.163 14.082 0.28 12.24 O ANISOU 397 O BILE A 49 1438 77 -20 1732 1479 101 O ATOM 398 CB AILE A 49 -15.513 8.295 17.396 0.72 10.86 C ANISOU 398 CB AILE A 49 997 -159 140 1757 1373 243 C ATOM 399 CB BILE A 49 -15.658 8.466 17.404 0.28 12.34 C ANISOU 399 CB BILE A 49 1497 -3 73 1865 1326 64 C ATOM 400 CG1AILE A 49 -16.067 8.087 18.854 0.72 14.33 C ANISOU 400 CG1AILE A 49 1785 -766 876 2187 1470 -130 C ATOM 401 CG1BILE A 49 -15.729 9.922 17.876 0.28 12.73 C ANISOU 401 CG1BILE A 49 1634 59 -4 2023 1177 -14 C ATOM 402 CG2AILE A 49 -14.854 9.638 17.266 0.72 10.27 C ANISOU 402 CG2AILE A 49 918 -231 28 1405 1578 9 C ATOM 403 CG2BILE A 49 -14.312 8.159 16.899 0.28 13.81 C ANISOU 403 CG2BILE A 49 1832 -52 187 2078 1336 -7 C ATOM 404 CD1AILE A 49 -15.091 7.609 19.688 0.72 18.74 C ANISOU 404 CD1AILE A 49 2067 -446 494 2248 2803 4 C ATOM 405 CD1BILE A 49 -15.550 10.058 19.426 0.28 14.98 C ANISOU 405 CD1BILE A 49 1902 64 -46 2232 1557 -100 C ATOM 406 N ALA A 50 -16.976 10.003 14.866 1.00 11.50 N ANISOU 406 N ALA A 50 1321 -55 -100 1620 1426 89 N ATOM 407 CA ALA A 50 -16.923 10.730 13.643 1.00 11.61 C ANISOU 407 CA ALA A 50 1324 -5 106 1625 1461 -7 C ATOM 408 C ALA A 50 -17.153 12.211 13.839 1.00 10.89 C ANISOU 408 C ALA A 50 1243 50 130 1622 1270 2 C ATOM 409 O ALA A 50 -17.638 12.664 14.860 1.00 11.29 O ANISOU 409 O ALA A 50 1359 90 175 1775 1155 -24 O ATOM 410 CB ALA A 50 -17.934 10.177 12.687 1.00 11.75 C ANISOU 410 CB ALA A 50 1377 -92 149 1569 1519 -30 C ATOM 411 N ASP A 51 -16.895 12.969 12.786 1.00 11.46 N ANISOU 411 N ASP A 51 1331 25 332 1586 1435 41 N ATOM 412 CA ASP A 51 -17.421 14.334 12.691 1.00 11.52 C ANISOU 412 CA ASP A 51 1241 50 176 1650 1486 -157 C ATOM 413 C ASP A 51 -18.880 14.317 12.308 1.00 12.11 C ANISOU 413 C ASP A 51 1457 44 210 1563 1578 -100 C ATOM 414 O ASP A 51 -19.230 13.640 11.369 1.00 12.11 O ANISOU 414 O ASP A 51 1498 197 242 1684 1417 -289 O ATOM 415 CB ASP A 51 -16.807 15.039 11.519 1.00 11.86 C ANISOU 415 CB ASP A 51 1327 19 335 1818 1361 -203 C ATOM 416 CG ASP A 51 -15.393 15.574 11.697 1.00 10.58 C ANISOU 416 CG ASP A 51 1349 -197 459 1703 965 -324 C ATOM 417 OD1 ASP A 51 -14.698 15.440 12.727 1.00 11.47 O ANISOU 417 OD1 ASP A 51 1317 43 66 2073 967 -346 O ATOM 418 OD2 ASP A 51 -14.942 16.262 10.705 1.00 11.25 O ANISOU 418 OD2 ASP A 51 1202 88 235 1723 1348 43 O ATOM 419 N ALA A 52 -19.677 15.136 12.979 1.00 12.17 N ANISOU 419 N ALA A 52 1240 135 91 1707 1674 -109 N ATOM 420 CA ALA A 52 -21.035 15.516 12.607 1.00 12.05 C ANISOU 420 CA ALA A 52 1214 126 186 1771 1590 -143 C ATOM 421 C ALA A 52 -20.936 16.944 12.099 1.00 12.52 C ANISOU 421 C ALA A 52 1210 177 110 1800 1746 -233 C ATOM 422 O ALA A 52 -20.885 17.910 12.881 1.00 13.47 O ANISOU 422 O ALA A 52 1454 290 304 1748 1917 -124 O ATOM 423 CB ALA A 52 -22.002 15.425 13.849 1.00 10.71 C ANISOU 423 CB ALA A 52 771 51 197 1756 1542 -225 C ATOM 424 N ARG A 53 -20.897 17.027 10.764 1.00 11.42 N ANISOU 424 N ARG A 53 1229 172 276 1599 1512 -87 N ATOM 425 CA ARG A 53 -20.830 18.317 10.061 1.00 13.14 C ANISOU 425 CA ARG A 53 1389 179 227 1827 1777 -132 C ATOM 426 C ARG A 53 -22.268 18.746 9.751 1.00 14.29 C ANISOU 426 C ARG A 53 1488 251 131 1909 2031 -163 C ATOM 427 O ARG A 53 -22.897 18.325 8.786 1.00 13.91 O ANISOU 427 O ARG A 53 1208 518 28 2054 2023 -466 O ATOM 428 CB ARG A 53 -19.941 18.236 8.823 1.00 13.88 C ANISOU 428 CB ARG A 53 1420 80 201 1810 2044 -21 C ATOM 429 CG ARG A 53 -18.556 17.644 9.086 1.00 12.53 C ANISOU 429 CG ARG A 53 1347 -53 522 1963 1452 -305 C ATOM 430 CD ARG A 53 -17.534 17.945 8.029 1.00 13.79 C ANISOU 430 CD ARG A 53 1680 111 479 1690 1869 -346 C ATOM 431 NE ARG A 53 -16.222 17.386 8.393 1.00 13.66 N ANISOU 431 NE ARG A 53 1307 318 349 1826 2055 -51 N ATOM 432 CZ ARG A 53 -15.117 17.615 7.708 1.00 14.91 C ANISOU 432 CZ ARG A 53 1975 439 554 1795 1892 102 C ATOM 433 NH1 ARG A 53 -15.191 18.260 6.534 1.00 15.65 N ANISOU 433 NH1 ARG A 53 2532 114 127 1795 1617 103 N ATOM 434 NH2 ARG A 53 -13.969 17.129 8.144 1.00 14.60 N ANISOU 434 NH2 ARG A 53 1829 66 204 2148 1569 66 N ATOM 435 N TYR A 54 -22.783 19.583 10.635 1.00 15.04 N ANISOU 435 N TYR A 54 1523 159 85 2088 2102 -27 N ATOM 436 CA TYR A 54 -24.210 19.867 10.683 1.00 15.43 C ANISOU 436 CA TYR A 54 1649 329 143 2132 2080 -194 C ATOM 437 C TYR A 54 -24.748 20.467 9.414 1.00 16.82 C ANISOU 437 C TYR A 54 1844 316 268 2192 2352 -103 C ATOM 438 O TYR A 54 -25.835 20.079 8.960 1.00 16.66 O ANISOU 438 O TYR A 54 1833 230 128 2303 2191 -167 O ATOM 439 CB TYR A 54 -24.529 20.782 11.840 1.00 15.15 C ANISOU 439 CB TYR A 54 1463 382 239 2096 2196 -115 C ATOM 440 CG TYR A 54 -24.474 20.118 13.169 1.00 14.34 C ANISOU 440 CG TYR A 54 1662 343 -118 2001 1785 84 C ATOM 441 CD1 TYR A 54 -23.403 20.343 14.028 1.00 13.77 C ANISOU 441 CD1 TYR A 54 1581 49 89 1604 2045 -144 C ATOM 442 CD2 TYR A 54 -25.459 19.239 13.583 1.00 14.45 C ANISOU 442 CD2 TYR A 54 1486 273 244 2146 1857 27 C ATOM 443 CE1 TYR A 54 -23.345 19.749 15.242 1.00 14.89 C ANISOU 443 CE1 TYR A 54 1334 250 70 2210 2113 362 C ATOM 444 CE2 TYR A 54 -25.419 18.638 14.852 1.00 14.87 C ANISOU 444 CE2 TYR A 54 1403 351 34 2376 1869 -59 C ATOM 445 CZ TYR A 54 -24.358 18.882 15.656 1.00 14.95 C ANISOU 445 CZ TYR A 54 1523 248 285 1967 2191 -143 C ATOM 446 OH TYR A 54 -24.265 18.342 16.904 1.00 15.84 O ANISOU 446 OH TYR A 54 1740 112 51 2401 1877 126 O ATOM 447 N GLU A 55 -24.028 21.442 8.876 1.00 17.40 N ANISOU 447 N GLU A 55 1835 438 337 2253 2520 -70 N ATOM 448 CA GLU A 55 -24.564 22.335 7.830 1.00 18.10 C ANISOU 448 CA GLU A 55 2125 440 335 2314 2437 -90 C ATOM 449 C GLU A 55 -24.012 22.132 6.413 1.00 18.75 C ANISOU 449 C GLU A 55 2324 618 406 2459 2339 -191 C ATOM 450 O GLU A 55 -24.693 22.447 5.418 1.00 18.66 O ANISOU 450 O GLU A 55 2122 704 495 2744 2223 -240 O ATOM 451 CB GLU A 55 -24.390 23.799 8.291 1.00 19.17 C ANISOU 451 CB GLU A 55 2403 418 442 2277 2602 -88 C ATOM 452 CG GLU A 55 -25.236 24.085 9.478 1.00 20.01 C ANISOU 452 CG GLU A 55 2662 432 212 2064 2876 11 C ATOM 453 CD GLU A 55 -24.977 25.434 10.135 1.00 26.84 C ANISOU 453 CD GLU A 55 3132 161 403 3295 3770 65 C ATOM 454 OE1 GLU A 55 -24.067 26.138 9.632 1.00 36.72 O ANISOU 454 OE1 GLU A 55 4530 -409 838 4124 5298 777 O ATOM 455 OE2 GLU A 55 -25.643 25.787 11.181 1.00 34.69 O ANISOU 455 OE2 GLU A 55 4142 167 400 4066 4971 457 O ATOM 456 N THR A 56 -22.792 21.612 6.322 1.00 17.28 N ANISOU 456 N THR A 56 2066 371 396 2378 2121 -183 N ATOM 457 CA THR A 56 -22.074 21.466 5.087 1.00 17.92 C ANISOU 457 CA THR A 56 2183 369 261 2312 2313 -124 C ATOM 458 C THR A 56 -20.917 20.563 5.343 1.00 17.19 C ANISOU 458 C THR A 56 2016 312 313 2340 2173 -181 C ATOM 459 O THR A 56 -20.510 20.412 6.493 1.00 17.10 O ANISOU 459 O THR A 56 1973 579 266 2376 2148 -306 O ATOM 460 CB THR A 56 -21.552 22.833 4.604 1.00 18.38 C ANISOU 460 CB THR A 56 2258 517 438 2475 2251 -159 C ATOM 461 OG1 THR A 56 -20.657 22.668 3.505 1.00 23.06 O ANISOU 461 OG1 THR A 56 2953 559 643 2848 2958 -33 O ATOM 462 CG2 THR A 56 -20.768 23.540 5.661 1.00 19.36 C ANISOU 462 CG2 THR A 56 2523 494 205 2172 2661 -17 C ATOM 463 N SER A 57 -20.366 19.969 4.275 1.00 16.65 N ANISOU 463 N SER A 57 1931 295 197 2312 2081 -211 N ATOM 464 CA SER A 57 -19.125 19.179 4.435 1.00 17.70 C ANISOU 464 CA SER A 57 2019 239 220 2420 2284 -75 C ATOM 465 C SER A 57 -17.885 20.000 4.481 1.00 18.43 C ANISOU 465 C SER A 57 2170 233 231 2440 2391 -94 C ATOM 466 O SER A 57 -16.820 19.468 4.699 1.00 18.49 O ANISOU 466 O SER A 57 2036 380 351 2325 2663 -117 O ATOM 467 CB SER A 57 -18.990 18.142 3.321 1.00 17.37 C ANISOU 467 CB SER A 57 1846 270 264 2565 2185 -122 C ATOM 468 OG SER A 57 -18.950 18.819 2.048 1.00 17.73 O ANISOU 468 OG SER A 57 2072 104 -17 2628 2035 -41 O ATOM 469 N APHE A 58 -18.015 21.292 4.211 0.65 18.89 N ANISOU 469 N APHE A 58 2134 140 205 2379 2662 -38 N ATOM 470 N BPHE A 58 -17.940 21.300 4.251 0.35 19.52 N ANISOU 470 N BPHE A 58 2268 186 201 2560 2587 -75 N ATOM 471 CA APHE A 58 -16.871 22.187 4.225 0.65 19.25 C ANISOU 471 CA APHE A 58 2171 89 192 2529 2615 -14 C ATOM 472 CA BPHE A 58 -16.686 22.068 4.211 0.35 20.40 C ANISOU 472 CA BPHE A 58 2383 141 196 2756 2610 -51 C ATOM 473 C APHE A 58 -16.163 22.005 5.546 0.65 19.64 C ANISOU 473 C APHE A 58 2231 30 185 2626 2604 -10 C ATOM 474 C BPHE A 58 -15.900 21.924 5.533 0.35 20.78 C ANISOU 474 C BPHE A 58 2432 73 182 2840 2624 -49 C ATOM 475 O APHE A 58 -16.770 21.859 6.607 0.65 19.44 O ANISOU 475 O APHE A 58 2189 -31 130 2537 2661 -8 O ATOM 476 O BPHE A 58 -16.495 21.935 6.609 0.35 20.21 O ANISOU 476 O BPHE A 58 2273 3 161 2769 2635 -78 O ATOM 477 CB APHE A 58 -17.281 23.650 4.035 0.65 18.89 C ANISOU 477 CB APHE A 58 2164 56 210 2380 2633 -40 C ATOM 478 CB BPHE A 58 -16.969 23.538 3.856 0.35 20.85 C ANISOU 478 CB BPHE A 58 2472 174 204 2829 2620 -96 C ATOM 479 CG APHE A 58 -16.110 24.610 3.963 0.65 19.37 C ANISOU 479 CG APHE A 58 2212 117 224 2368 2780 77 C ATOM 480 CG BPHE A 58 -17.391 23.761 2.412 0.35 20.48 C ANISOU 480 CG BPHE A 58 2484 337 349 2735 2562 -71 C ATOM 481 CD1APHE A 58 -15.186 24.505 2.969 0.65 20.57 C ANISOU 481 CD1APHE A 58 2497 58 108 2402 2914 70 C ATOM 482 CD1BPHE A 58 -18.213 24.811 2.084 0.35 22.51 C ANISOU 482 CD1BPHE A 58 2631 219 209 3160 2760 -74 C ATOM 483 CD2APHE A 58 -15.975 25.628 4.873 0.65 18.97 C ANISOU 483 CD2APHE A 58 1936 151 481 2418 2851 -415 C ATOM 484 CD2BPHE A 58 -16.986 22.903 1.396 0.35 23.74 C ANISOU 484 CD2BPHE A 58 2868 297 419 3380 2772 -129 C ATOM 485 CE1APHE A 58 -14.126 25.391 2.902 0.65 20.03 C ANISOU 485 CE1APHE A 58 2466 12 244 2283 2862 99 C ATOM 486 CE1BPHE A 58 -18.581 25.034 0.763 0.35 22.09 C ANISOU 486 CE1BPHE A 58 2591 365 294 3202 2600 -260 C ATOM 487 CE2APHE A 58 -14.938 26.519 4.782 0.65 19.25 C ANISOU 487 CE2APHE A 58 2159 257 419 2505 2650 -365 C ATOM 488 CE2BPHE A 58 -17.362 23.124 0.074 0.35 22.89 C ANISOU 488 CE2BPHE A 58 2783 259 289 3206 2708 -239 C ATOM 489 CZ APHE A 58 -14.024 26.399 3.797 0.65 19.96 C ANISOU 489 CZ APHE A 58 2208 53 249 2650 2725 -204 C ATOM 490 CZ BPHE A 58 -18.173 24.191 -0.223 0.35 22.11 C ANISOU 490 CZ BPHE A 58 2639 357 299 3089 2673 -243 C ATOM 491 N AASP A 59 -14.839 21.942 5.462 0.60 20.11 N ANISOU 491 N AASP A 59 2327 -17 275 2758 2554 51 N ATOM 492 N BASP A 59 -14.577 21.727 5.468 0.40 21.57 N ANISOU 492 N BASP A 59 2585 -36 233 2939 2669 38 N ATOM 493 CA AASP A 59 -14.018 21.514 6.626 0.60 20.94 C ANISOU 493 CA AASP A 59 2560 11 311 2669 2726 51 C ATOM 494 CA BASP A 59 -13.819 21.454 6.710 0.40 22.00 C ANISOU 494 CA BASP A 59 2736 -18 264 2888 2732 21 C ATOM 495 C AASP A 59 -14.209 22.519 7.741 0.60 21.50 C ANISOU 495 C AASP A 59 2681 32 328 2738 2748 94 C ATOM 496 C BASP A 59 -14.006 22.540 7.775 0.40 22.37 C ANISOU 496 C BASP A 59 2834 -7 285 2872 2791 89 C ATOM 497 O AASP A 59 -14.270 22.189 8.901 0.60 21.32 O ANISOU 497 O AASP A 59 2878 -46 584 2366 2854 207 O ATOM 498 O BASP A 59 -13.883 22.263 8.964 0.40 21.85 O ANISOU 498 O BASP A 59 2848 -142 420 2648 2803 173 O ATOM 499 CB AASP A 59 -12.518 21.468 6.295 0.60 20.02 C ANISOU 499 CB AASP A 59 2371 124 362 2654 2581 138 C ATOM 500 CB BASP A 59 -12.329 21.233 6.419 0.40 22.12 C ANISOU 500 CB BASP A 59 2728 -5 291 3007 2670 72 C ATOM 501 CG AASP A 59 -12.103 20.289 5.362 0.60 20.53 C ANISOU 501 CG AASP A 59 2614 41 395 2363 2821 376 C ATOM 502 CG BASP A 59 -11.984 19.754 6.183 0.40 22.93 C ANISOU 502 CG BASP A 59 2839 -4 344 3264 2609 70 C ATOM 503 OD1AASP A 59 -12.787 19.199 5.256 0.60 16.99 O ANISOU 503 OD1AASP A 59 1410 507 661 2514 2529 689 O ATOM 504 OD1BASP A 59 -11.704 19.371 5.021 0.40 27.07 O ANISOU 504 OD1BASP A 59 3452 238 660 3861 2970 87 O ATOM 505 OD2AASP A 59 -11.017 20.383 4.704 0.60 20.56 O ANISOU 505 OD2AASP A 59 2988 82 578 1612 3212 578 O ATOM 506 OD2BASP A 59 -11.982 18.894 7.091 0.40 21.08 O ANISOU 506 OD2BASP A 59 2743 -376 920 3625 1641 386 O ATOM 507 N ASN A 60 -14.264 23.776 7.361 1.00 22.70 N ANISOU 507 N ASN A 60 3050 -78 353 2742 2829 103 N ATOM 508 CA ASN A 60 -14.249 24.889 8.311 1.00 22.78 C ANISOU 508 CA ASN A 60 2967 -26 380 2808 2880 113 C ATOM 509 C ASN A 60 -15.666 25.414 8.527 1.00 23.10 C ANISOU 509 C ASN A 60 3024 -104 502 2729 3022 86 C ATOM 510 O ASN A 60 -16.037 26.506 8.082 1.00 24.71 O ANISOU 510 O ASN A 60 3493 -155 624 2628 3267 37 O ATOM 511 CB ASN A 60 -13.286 25.940 7.766 1.00 23.33 C ANISOU 511 CB ASN A 60 2986 -35 415 2877 2998 196 C ATOM 512 CG ASN A 60 -11.919 25.345 7.298 1.00 23.72 C ANISOU 512 CG ASN A 60 3043 78 667 3101 2868 190 C ATOM 513 OD1 ASN A 60 -11.435 25.646 6.179 1.00 29.43 O ANISOU 513 OD1 ASN A 60 3537 414 946 4634 3009 416 O ATOM 514 ND2 ASN A 60 -11.289 24.546 8.142 1.00 22.42 N ANISOU 514 ND2 ASN A 60 3113 201 1056 2727 2678 382 N ATOM 515 N SER A 61 -16.484 24.567 9.166 1.00 22.40 N ANISOU 515 N SER A 61 2942 -146 519 2840 2729 225 N ATOM 516 CA SER A 61 -17.923 24.795 9.391 1.00 20.45 C ANISOU 516 CA SER A 61 2597 18 433 2550 2622 82 C ATOM 517 C SER A 61 -18.313 24.176 10.784 1.00 18.04 C ANISOU 517 C SER A 61 2309 41 497 2323 2219 134 C ATOM 518 O SER A 61 -17.464 23.667 11.492 1.00 19.27 O ANISOU 518 O SER A 61 2517 -203 421 2241 2562 574 O ATOM 519 CB SER A 61 -18.735 24.093 8.284 1.00 19.92 C ANISOU 519 CB SER A 61 2668 146 466 2569 2331 -48 C ATOM 520 OG SER A 61 -18.724 22.662 8.392 1.00 20.75 O ANISOU 520 OG SER A 61 2339 96 749 2643 2901 -61 O ATOM 521 N LEU A 62 -19.589 24.200 11.152 1.00 17.45 N ANISOU 521 N LEU A 62 2042 240 357 2344 2243 27 N ATOM 522 CA LEU A 62 -20.045 23.780 12.489 1.00 17.12 C ANISOU 522 CA LEU A 62 1928 278 187 2241 2335 54 C ATOM 523 C LEU A 62 -19.975 22.255 12.631 1.00 16.05 C ANISOU 523 C LEU A 62 1828 322 166 2078 2191 23 C ATOM 524 O LEU A 62 -20.637 21.538 11.922 1.00 15.25 O ANISOU 524 O LEU A 62 1527 755 232 1943 2321 -204 O ATOM 525 CB LEU A 62 -21.469 24.287 12.787 1.00 17.56 C ANISOU 525 CB LEU A 62 2061 283 79 2416 2195 -68 C ATOM 526 CG LEU A 62 -21.971 24.106 14.234 1.00 16.65 C ANISOU 526 CG LEU A 62 1644 241 80 2315 2365 -17 C ATOM 527 CD1 LEU A 62 -21.414 25.180 15.181 1.00 16.37 C ANISOU 527 CD1 LEU A 62 1275 -43 123 2273 2669 -563 C ATOM 528 CD2 LEU A 62 -23.483 24.140 14.305 1.00 20.59 C ANISOU 528 CD2 LEU A 62 2065 380 -5 2856 2902 -137 C ATOM 529 N ILE A 63 -19.182 21.782 13.576 1.00 14.84 N ANISOU 529 N ILE A 63 1608 378 160 1926 2105 67 N ATOM 530 CA ILE A 63 -18.916 20.350 13.716 1.00 14.48 C ANISOU 530 CA ILE A 63 1550 232 81 1936 2014 130 C ATOM 531 C ILE A 63 -18.837 19.986 15.174 1.00 12.73 C ANISOU 531 C ILE A 63 1339 324 162 1641 1858 118 C ATOM 532 O ILE A 63 -18.126 20.652 15.957 1.00 13.34 O ANISOU 532 O ILE A 63 1386 208 220 1581 2099 135 O ATOM 533 CB ILE A 63 -17.573 19.913 13.041 1.00 13.54 C ANISOU 533 CB ILE A 63 1274 217 119 1973 1895 101 C ATOM 534 CG1 ILE A 63 -17.512 20.338 11.565 1.00 13.72 C ANISOU 534 CG1 ILE A 63 1485 284 70 2072 1655 295 C ATOM 535 CG2 ILE A 63 -17.391 18.441 13.150 1.00 13.59 C ANISOU 535 CG2 ILE A 63 1503 124 319 1892 1768 145 C ATOM 536 CD1 ILE A 63 -16.178 20.149 10.890 1.00 15.05 C ANISOU 536 CD1 ILE A 63 1470 15 -39 2219 2026 -96 C ATOM 537 N ASP A 64 -19.567 18.937 15.551 1.00 13.64 N ANISOU 537 N ASP A 64 1471 393 42 1810 1902 162 N ATOM 538 CA ASP A 64 -19.418 18.295 16.868 1.00 12.94 C ANISOU 538 CA ASP A 64 1406 223 74 1833 1676 54 C ATOM 539 C ASP A 64 -18.922 16.866 16.605 1.00 12.74 C ANISOU 539 C ASP A 64 1469 120 49 1739 1632 22 C ATOM 540 O ASP A 64 -19.109 16.331 15.533 1.00 12.51 O ANISOU 540 O ASP A 64 1318 148 123 2009 1426 -200 O ATOM 541 CB ASP A 64 -20.766 18.124 17.554 1.00 12.87 C ANISOU 541 CB ASP A 64 1441 228 126 1750 1696 146 C ATOM 542 CG ASP A 64 -21.283 19.372 18.243 1.00 14.14 C ANISOU 542 CG ASP A 64 1514 250 126 1878 1981 158 C ATOM 543 OD1 ASP A 64 -20.523 20.374 18.491 1.00 14.14 O ANISOU 543 OD1 ASP A 64 1487 143 -251 1773 2111 33 O ATOM 544 OD2 ASP A 64 -22.506 19.378 18.607 1.00 17.05 O ANISOU 544 OD2 ASP A 64 1628 385 115 2116 2731 314 O ATOM 545 N THR A 65 -18.301 16.235 17.590 1.00 11.50 N ANISOU 545 N THR A 65 1356 -13 4 1751 1260 -93 N ATOM 546 CA THR A 65 -17.868 14.824 17.470 1.00 10.96 C ANISOU 546 CA THR A 65 1241 -12 47 1607 1314 68 C ATOM 547 C THR A 65 -19.011 13.937 17.932 1.00 12.73 C ANISOU 547 C THR A 65 1488 2 69 1841 1508 -12 C ATOM 548 O THR A 65 -19.430 14.034 19.084 1.00 13.25 O ANISOU 548 O THR A 65 1488 -166 21 2039 1507 -118 O ATOM 549 CB THR A 65 -16.657 14.560 18.369 1.00 11.44 C ANISOU 549 CB THR A 65 1442 26 54 1598 1304 240 C ATOM 550 OG1 THR A 65 -15.578 15.440 18.021 1.00 12.24 O ANISOU 550 OG1 THR A 65 1046 -39 -37 1846 1757 103 O ATOM 551 CG2 THR A 65 -16.188 13.147 18.176 1.00 11.19 C ANISOU 551 CG2 THR A 65 1394 -28 101 1799 1057 -22 C ATOM 552 N VAL A 66 -19.497 13.080 17.048 1.00 11.74 N ANISOU 552 N VAL A 66 1357 -58 18 1694 1407 20 N ATOM 553 CA VAL A 66 -20.583 12.126 17.344 1.00 11.62 C ANISOU 553 CA VAL A 66 1189 -74 69 1765 1460 -46 C ATOM 554 C VAL A 66 -19.987 10.762 17.654 1.00 11.98 C ANISOU 554 C VAL A 66 1203 -153 188 1806 1543 -11 C ATOM 555 O VAL A 66 -18.944 10.401 17.107 1.00 11.84 O ANISOU 555 O VAL A 66 1133 -85 282 1770 1595 -99 O ATOM 556 CB VAL A 66 -21.582 12.055 16.108 1.00 12.20 C ANISOU 556 CB VAL A 66 1181 -96 207 1798 1656 -80 C ATOM 557 CG1 VAL A 66 -20.875 11.711 14.834 1.00 13.31 C ANISOU 557 CG1 VAL A 66 1411 1 223 2094 1551 -67 C ATOM 558 CG2 VAL A 66 -22.768 11.135 16.307 1.00 16.13 C ANISOU 558 CG2 VAL A 66 1734 -88 219 2368 2023 33 C ATOM 559 N ALA A 67 -20.696 10.000 18.507 1.00 12.03 N ANISOU 559 N ALA A 67 992 -110 139 2004 1574 42 N ATOM 560 CA ALA A 67 -20.445 8.610 18.765 1.00 12.09 C ANISOU 560 CA ALA A 67 1156 -181 137 1824 1611 -13 C ATOM 561 C ALA A 67 -21.727 7.820 18.590 1.00 12.94 C ANISOU 561 C ALA A 67 1162 -109 240 1875 1876 167 C ATOM 562 O ALA A 67 -22.838 8.221 19.039 1.00 14.43 O ANISOU 562 O ALA A 67 1381 117 180 2213 1889 292 O ATOM 563 CB ALA A 67 -19.933 8.411 20.177 1.00 13.32 C ANISOU 563 CB ALA A 67 1301 -129 13 1978 1782 114 C ATOM 564 N LYS A 68 -21.571 6.667 17.979 1.00 12.43 N ANISOU 564 N LYS A 68 1042 -144 232 2030 1648 106 N ATOM 565 CA LYS A 68 -22.609 5.613 18.020 1.00 12.37 C ANISOU 565 CA LYS A 68 1099 -263 180 1862 1739 79 C ATOM 566 C LYS A 68 -21.969 4.405 18.649 1.00 13.36 C ANISOU 566 C LYS A 68 1188 -354 212 1985 1900 113 C ATOM 567 O LYS A 68 -20.789 4.121 18.409 1.00 14.14 O ANISOU 567 O LYS A 68 1197 -390 539 2048 2127 161 O ATOM 568 CB LYS A 68 -23.135 5.282 16.617 1.00 13.38 C ANISOU 568 CB LYS A 68 1227 -196 149 2101 1755 91 C ATOM 569 CG LYS A 68 -24.005 6.367 15.967 1.00 13.45 C ANISOU 569 CG LYS A 68 1117 -181 118 2184 1809 163 C ATOM 570 CD LYS A 68 -24.498 5.927 14.607 1.00 14.21 C ANISOU 570 CD LYS A 68 1436 -145 -4 2057 1903 126 C ATOM 571 CE LYS A 68 -25.370 6.964 13.947 1.00 13.95 C ANISOU 571 CE LYS A 68 1690 162 175 2113 1497 -89 C ATOM 572 NZ LYS A 68 -26.760 6.908 14.581 1.00 16.94 N ANISOU 572 NZ LYS A 68 1704 152 98 2662 2068 197 N ATOM 573 N TYR A 69 -22.734 3.671 19.426 1.00 13.57 N ANISOU 573 N TYR A 69 994 -378 379 2231 1928 182 N ATOM 574 CA TYR A 69 -22.168 2.495 20.078 1.00 14.56 C ANISOU 574 CA TYR A 69 1293 -311 256 2213 2025 204 C ATOM 575 C TYR A 69 -23.129 1.328 20.042 1.00 14.49 C ANISOU 575 C TYR A 69 1336 -363 280 2319 1849 181 C ATOM 576 O TYR A 69 -24.352 1.526 20.020 1.00 15.60 O ANISOU 576 O TYR A 69 1268 -391 275 2482 2176 237 O ATOM 577 CB TYR A 69 -21.637 2.790 21.482 1.00 16.76 C ANISOU 577 CB TYR A 69 1393 -264 216 2786 2187 250 C ATOM 578 CG TYR A 69 -22.677 3.263 22.466 1.00 17.12 C ANISOU 578 CG TYR A 69 1508 -239 187 2923 2072 51 C ATOM 579 CD1 TYR A 69 -22.936 4.581 22.648 1.00 18.23 C ANISOU 579 CD1 TYR A 69 1653 -253 24 3147 2123 133 C ATOM 580 CD2 TYR A 69 -23.395 2.345 23.237 1.00 19.19 C ANISOU 580 CD2 TYR A 69 1585 -265 176 3396 2307 -32 C ATOM 581 CE1 TYR A 69 -23.888 4.999 23.598 1.00 21.68 C ANISOU 581 CE1 TYR A 69 2009 32 200 3377 2851 164 C ATOM 582 CE2 TYR A 69 -24.339 2.745 24.133 1.00 20.26 C ANISOU 582 CE2 TYR A 69 1741 -49 36 3402 2553 155 C ATOM 583 CZ TYR A 69 -24.588 4.068 24.311 1.00 19.91 C ANISOU 583 CZ TYR A 69 1373 45 14 3619 2570 390 C ATOM 584 OH TYR A 69 -25.570 4.450 25.239 1.00 24.85 O ANISOU 584 OH TYR A 69 2085 -92 -173 4680 2674 503 O ATOM 585 N SER A 70 -22.572 0.139 19.957 1.00 14.90 N ANISOU 585 N SER A 70 1525 -382 534 2299 1834 205 N ATOM 586 CA SER A 70 -23.378 -1.093 19.842 1.00 15.62 C ANISOU 586 CA SER A 70 1538 -375 391 2230 2166 113 C ATOM 587 C SER A 70 -22.869 -2.197 20.761 1.00 16.94 C ANISOU 587 C SER A 70 1718 -272 419 2379 2337 259 C ATOM 588 O SER A 70 -21.677 -2.410 20.859 1.00 16.68 O ANISOU 588 O SER A 70 1420 -317 876 2421 2495 192 O ATOM 589 CB SER A 70 -23.329 -1.579 18.422 1.00 16.04 C ANISOU 589 CB SER A 70 1574 -297 339 2236 2284 292 C ATOM 590 OG SER A 70 -23.975 -2.832 18.250 1.00 17.40 O ANISOU 590 OG SER A 70 1658 -918 402 2376 2576 -269 O ATOM 591 N VAL A 71 -23.780 -2.895 21.424 1.00 17.89 N ANISOU 591 N VAL A 71 1934 -257 484 2287 2576 224 N ATOM 592 CA VAL A 71 -23.438 -4.091 22.153 1.00 20.00 C ANISOU 592 CA VAL A 71 2253 -263 481 2666 2677 272 C ATOM 593 C VAL A 71 -23.753 -5.391 21.416 1.00 20.15 C ANISOU 593 C VAL A 71 2480 -182 550 2447 2726 350 C ATOM 594 O VAL A 71 -23.563 -6.478 22.015 1.00 22.81 O ANISOU 594 O VAL A 71 2919 -166 731 2991 2756 587 O ATOM 595 CB VAL A 71 -24.138 -4.156 23.508 1.00 22.04 C ANISOU 595 CB VAL A 71 2620 -61 350 2942 2812 217 C ATOM 596 CG1 VAL A 71 -23.693 -3.013 24.321 1.00 24.11 C ANISOU 596 CG1 VAL A 71 2968 -256 316 3251 2942 106 C ATOM 597 CG2 VAL A 71 -25.672 -4.169 23.311 1.00 21.43 C ANISOU 597 CG2 VAL A 71 2479 -330 360 2911 2751 441 C ATOM 598 N ASP A 72 -24.235 -5.311 20.175 1.00 20.43 N ANISOU 598 N ASP A 72 2344 -272 578 2487 2930 318 N ATOM 599 CA ASP A 72 -24.566 -6.478 19.407 1.00 21.50 C ANISOU 599 CA ASP A 72 2455 -269 467 2673 3040 194 C ATOM 600 C ASP A 72 -23.870 -6.562 18.066 1.00 22.86 C ANISOU 600 C ASP A 72 2745 -306 367 2749 3189 85 C ATOM 601 O ASP A 72 -24.452 -7.005 17.048 1.00 23.15 O ANISOU 601 O ASP A 72 3123 -605 395 2717 2955 41 O ATOM 602 CB ASP A 72 -26.081 -6.589 19.278 1.00 23.51 C ANISOU 602 CB ASP A 72 2570 -341 468 2831 3531 159 C ATOM 603 CG ASP A 72 -26.713 -5.374 18.646 1.00 22.27 C ANISOU 603 CG ASP A 72 1868 -79 611 2733 3858 233 C ATOM 604 OD1 ASP A 72 -26.008 -4.534 18.027 1.00 24.15 O ANISOU 604 OD1 ASP A 72 2230 -441 530 2361 4584 205 O ATOM 605 OD2 ASP A 72 -27.954 -5.178 18.709 1.00 28.80 O ANISOU 605 OD2 ASP A 72 2111 -435 883 3127 5703 542 O ATOM 606 N ASP A 73 -22.615 -6.124 18.083 1.00 22.76 N ANISOU 606 N ASP A 73 2744 -455 347 2914 2988 211 N ATOM 607 CA ASP A 73 -21.779 -6.089 16.880 1.00 23.48 C ANISOU 607 CA ASP A 73 2802 -328 234 3020 3096 82 C ATOM 608 C ASP A 73 -22.432 -5.424 15.700 1.00 23.20 C ANISOU 608 C ASP A 73 2870 -388 137 2993 2949 -32 C ATOM 609 O ASP A 73 -22.288 -5.875 14.580 1.00 25.75 O ANISOU 609 O ASP A 73 3296 -292 265 3190 3298 -52 O ATOM 610 CB ASP A 73 -21.269 -7.462 16.544 1.00 24.11 C ANISOU 610 CB ASP A 73 2917 -334 346 3149 3092 52 C ATOM 611 CG ASP A 73 -20.438 -8.033 17.665 1.00 26.96 C ANISOU 611 CG ASP A 73 3127 -261 353 3609 3505 -35 C ATOM 612 OD1 ASP A 73 -19.512 -7.324 18.174 1.00 27.62 O ANISOU 612 OD1 ASP A 73 3460 -368 678 3910 3125 -418 O ATOM 613 OD2 ASP A 73 -20.681 -9.152 18.119 1.00 32.46 O ANISOU 613 OD2 ASP A 73 3643 -169 637 4342 4347 -36 O ATOM 614 N GLY A 74 -23.125 -4.336 15.969 1.00 23.32 N ANISOU 614 N GLY A 74 2913 -342 16 2938 3007 -183 N ATOM 615 CA GLY A 74 -23.463 -3.397 14.944 1.00 23.37 C ANISOU 615 CA GLY A 74 2980 -258 -126 2994 2906 -367 C ATOM 616 C GLY A 74 -24.798 -3.650 14.332 1.00 25.37 C ANISOU 616 C GLY A 74 3247 -189 -111 3251 3138 -439 C ATOM 617 O GLY A 74 -25.095 -3.105 13.267 1.00 27.34 O ANISOU 617 O GLY A 74 3667 -110 -300 3520 3198 -649 O ATOM 618 N GLU A 75 -25.581 -4.498 14.974 1.00 25.17 N ANISOU 618 N GLU A 75 3020 -324 -208 3226 3318 -605 N ATOM 619 CA GLU A 75 -26.941 -4.682 14.552 1.00 28.05 C ANISOU 619 CA GLU A 75 3351 -199 -128 3667 3638 -552 C ATOM 620 C GLU A 75 -27.757 -3.509 14.996 1.00 27.31 C ANISOU 620 C GLU A 75 3240 -178 -120 3557 3578 -657 C ATOM 621 O GLU A 75 -28.588 -3.029 14.217 1.00 30.33 O ANISOU 621 O GLU A 75 3802 -120 -205 3866 3854 -890 O ATOM 622 CB GLU A 75 -27.523 -6.007 15.064 1.00 29.14 C ANISOU 622 CB GLU A 75 3334 -325 -60 3888 3849 -547 C ATOM 623 CG GLU A 75 -28.315 -6.720 13.978 1.00 36.34 C ANISOU 623 CG GLU A 75 4582 -100 -72 4612 4613 -369 C ATOM 624 CD GLU A 75 -27.433 -7.290 12.864 1.00 43.25 C ANISOU 624 CD GLU A 75 5583 -69 174 5327 5521 -559 C ATOM 625 OE1 GLU A 75 -26.597 -8.207 13.156 1.00 47.07 O ANISOU 625 OE1 GLU A 75 5555 147 397 6051 6276 -942 O ATOM 626 OE2 GLU A 75 -27.587 -6.837 11.689 1.00 45.61 O ANISOU 626 OE2 GLU A 75 6261 2 136 5444 5624 -1200 O ATOM 627 N THR A 76 -27.589 -3.052 16.235 1.00 24.13 N ANISOU 627 N THR A 76 2723 -387 -159 3215 3227 -665 N ATOM 628 CA THR A 76 -28.242 -1.818 16.649 1.00 22.72 C ANISOU 628 CA THR A 76 2335 -433 59 3193 3102 -382 C ATOM 629 C THR A 76 -27.270 -0.901 17.354 1.00 20.43 C ANISOU 629 C THR A 76 2085 -463 108 2834 2843 -284 C ATOM 630 O THR A 76 -26.267 -1.355 17.891 1.00 18.78 O ANISOU 630 O THR A 76 1738 -539 349 2421 2975 -45 O ATOM 631 CB THR A 76 -29.402 -2.083 17.575 1.00 24.15 C ANISOU 631 CB THR A 76 2384 -532 98 3493 3296 -351 C ATOM 632 OG1 THR A 76 -28.947 -2.530 18.874 1.00 25.88 O ANISOU 632 OG1 THR A 76 2095 -804 279 4033 3705 -9 O ATOM 633 CG2 THR A 76 -30.224 -3.194 17.023 1.00 27.24 C ANISOU 633 CG2 THR A 76 2864 -530 22 3558 3925 -299 C ATOM 634 N TRP A 77 -27.575 0.384 17.284 1.00 16.98 N ANISOU 634 N TRP A 77 1670 -231 224 2412 2370 -245 N ATOM 635 CA TRP A 77 -26.731 1.431 17.826 1.00 17.22 C ANISOU 635 CA TRP A 77 1747 -358 196 2530 2264 -64 C ATOM 636 C TRP A 77 -27.484 2.500 18.576 1.00 16.71 C ANISOU 636 C TRP A 77 1591 -186 264 2669 2089 -55 C ATOM 637 O TRP A 77 -28.588 2.865 18.217 1.00 18.21 O ANISOU 637 O TRP A 77 1463 66 -10 3143 2310 -115 O ATOM 638 CB TRP A 77 -25.984 2.156 16.680 1.00 16.96 C ANISOU 638 CB TRP A 77 1720 -313 275 2482 2239 -134 C ATOM 639 CG TRP A 77 -25.175 1.263 15.734 1.00 15.13 C ANISOU 639 CG TRP A 77 1689 -432 165 2079 1981 -27 C ATOM 640 CD1 TRP A 77 -25.652 0.473 14.750 1.00 15.28 C ANISOU 640 CD1 TRP A 77 1602 -419 127 2327 1873 -241 C ATOM 641 CD2 TRP A 77 -23.766 1.086 15.725 1.00 14.59 C ANISOU 641 CD2 TRP A 77 1524 -450 211 2209 1811 28 C ATOM 642 NE1 TRP A 77 -24.625 -0.170 14.101 1.00 16.98 N ANISOU 642 NE1 TRP A 77 1737 -376 309 2407 2305 -252 N ATOM 643 CE2 TRP A 77 -23.456 0.176 14.704 1.00 15.59 C ANISOU 643 CE2 TRP A 77 1383 -710 139 2138 2400 -168 C ATOM 644 CE3 TRP A 77 -22.720 1.584 16.519 1.00 15.35 C ANISOU 644 CE3 TRP A 77 1546 -462 -27 2263 2021 -55 C ATOM 645 CZ2 TRP A 77 -22.158 -0.211 14.419 1.00 14.77 C ANISOU 645 CZ2 TRP A 77 1513 -369 80 1875 2224 -190 C ATOM 646 CZ3 TRP A 77 -21.392 1.202 16.223 1.00 14.79 C ANISOU 646 CZ3 TRP A 77 1413 -221 215 2073 2131 -52 C ATOM 647 CH2 TRP A 77 -21.136 0.338 15.191 1.00 14.62 C ANISOU 647 CH2 TRP A 77 1443 -577 198 2088 2021 -145 C ATOM 648 N GLU A 78 -26.839 3.036 19.604 1.00 16.48 N ANISOU 648 N GLU A 78 1591 -346 216 2472 2198 54 N ATOM 649 CA GLU A 78 -27.263 4.241 20.292 1.00 17.57 C ANISOU 649 CA GLU A 78 1771 -226 320 2572 2331 162 C ATOM 650 C GLU A 78 -26.356 5.395 19.813 1.00 16.78 C ANISOU 650 C GLU A 78 1588 -121 307 2568 2217 226 C ATOM 651 O GLU A 78 -25.225 5.147 19.376 1.00 16.91 O ANISOU 651 O GLU A 78 1275 68 311 2712 2438 293 O ATOM 652 CB GLU A 78 -27.064 4.073 21.782 1.00 18.08 C ANISOU 652 CB GLU A 78 1943 -365 272 2559 2364 359 C ATOM 653 CG GLU A 78 -27.873 2.963 22.425 1.00 24.73 C ANISOU 653 CG GLU A 78 2918 -233 408 2999 3478 449 C ATOM 654 CD GLU A 78 -29.315 3.299 22.588 1.00 30.97 C ANISOU 654 CD GLU A 78 3536 -514 1048 3463 4767 1077 C ATOM 655 OE1 GLU A 78 -29.701 4.468 22.392 1.00 35.56 O ANISOU 655 OE1 GLU A 78 4009 98 1499 4805 4696 1197 O ATOM 656 OE2 GLU A 78 -30.074 2.368 22.947 1.00 41.36 O ANISOU 656 OE2 GLU A 78 4774 -450 774 5084 5856 1173 O ATOM 657 N THR A 79 -26.840 6.632 19.941 1.00 16.40 N ANISOU 657 N THR A 79 1472 -52 308 2587 2170 209 N ATOM 658 CA THR A 79 -26.190 7.795 19.363 1.00 15.88 C ANISOU 658 CA THR A 79 1432 -65 273 2427 2171 191 C ATOM 659 C THR A 79 -26.081 8.848 20.416 1.00 16.14 C ANISOU 659 C THR A 79 1556 38 280 2542 2032 312 C ATOM 660 O THR A 79 -27.028 9.140 21.147 1.00 18.15 O ANISOU 660 O THR A 79 1606 -120 197 3092 2195 449 O ATOM 661 CB THR A 79 -27.052 8.331 18.190 1.00 16.35 C ANISOU 661 CB THR A 79 1468 61 302 2491 2252 269 C ATOM 662 OG1 THR A 79 -27.255 7.314 17.190 1.00 17.15 O ANISOU 662 OG1 THR A 79 1439 -135 219 2476 2600 284 O ATOM 663 CG2 THR A 79 -26.387 9.477 17.451 1.00 16.82 C ANISOU 663 CG2 THR A 79 1431 202 309 2726 2231 24 C ATOM 664 N GLN A 80 -24.935 9.488 20.433 1.00 15.14 N ANISOU 664 N GLN A 80 1419 87 226 2363 1970 98 N ATOM 665 CA GLN A 80 -24.703 10.628 21.285 1.00 16.69 C ANISOU 665 CA GLN A 80 1830 108 93 2488 2020 116 C ATOM 666 C GLN A 80 -23.721 11.628 20.662 1.00 15.37 C ANISOU 666 C GLN A 80 1597 124 48 2312 1932 101 C ATOM 667 O GLN A 80 -23.097 11.353 19.662 1.00 15.07 O ANISOU 667 O GLN A 80 1299 105 -11 2223 2203 354 O ATOM 668 CB GLN A 80 -24.178 10.132 22.624 1.00 19.20 C ANISOU 668 CB GLN A 80 2292 112 9 2783 2218 19 C ATOM 669 CG GLN A 80 -22.895 9.493 22.579 1.00 20.62 C ANISOU 669 CG GLN A 80 2680 -39 185 2882 2272 158 C ATOM 670 CD GLN A 80 -22.487 8.617 23.799 1.00 20.87 C ANISOU 670 CD GLN A 80 2733 225 144 2821 2373 -27 C ATOM 671 OE1 GLN A 80 -21.522 7.972 23.686 1.00 21.29 O ANISOU 671 OE1 GLN A 80 2528 610 368 2853 2708 -236 O ATOM 672 NE2 GLN A 80 -23.213 8.637 24.910 1.00 23.81 N ANISOU 672 NE2 GLN A 80 2977 -131 202 3432 2634 58 N ATOM 673 N ILE A 81 -23.582 12.793 21.279 1.00 15.14 N ANISOU 673 N ILE A 81 1532 216 34 2300 1921 172 N ATOM 674 CA ILE A 81 -22.486 13.711 20.959 1.00 14.63 C ANISOU 674 CA ILE A 81 1632 88 114 2261 1666 101 C ATOM 675 C ILE A 81 -21.444 13.504 22.015 1.00 14.57 C ANISOU 675 C ILE A 81 1808 62 93 2226 1500 100 C ATOM 676 O ILE A 81 -21.730 13.701 23.188 1.00 15.32 O ANISOU 676 O ILE A 81 1750 217 229 2665 1405 68 O ATOM 677 CB ILE A 81 -22.954 15.184 20.868 1.00 15.51 C ANISOU 677 CB ILE A 81 1840 3 46 2410 1641 124 C ATOM 678 CG1 ILE A 81 -23.846 15.393 19.645 1.00 17.01 C ANISOU 678 CG1 ILE A 81 1873 245 33 2522 2067 26 C ATOM 679 CG2 ILE A 81 -21.762 16.142 20.868 1.00 17.30 C ANISOU 679 CG2 ILE A 81 2013 49 -27 2358 2202 206 C ATOM 680 CD1 ILE A 81 -23.182 15.100 18.310 1.00 18.52 C ANISOU 680 CD1 ILE A 81 2233 80 90 2676 2125 95 C ATOM 681 N ALA A 82 -20.250 13.126 21.604 1.00 13.68 N ANISOU 681 N ALA A 82 1581 92 160 2292 1323 32 N ATOM 682 CA ALA A 82 -19.143 12.870 22.530 1.00 13.18 C ANISOU 682 CA ALA A 82 1669 71 167 1966 1371 127 C ATOM 683 C ALA A 82 -18.482 14.177 22.930 1.00 13.29 C ANISOU 683 C ALA A 82 1676 93 106 2004 1368 116 C ATOM 684 O ALA A 82 -18.046 14.326 24.046 1.00 14.62 O ANISOU 684 O ALA A 82 1989 -70 91 2201 1362 366 O ATOM 685 CB ALA A 82 -18.109 11.986 21.854 1.00 14.11 C ANISOU 685 CB ALA A 82 1891 -5 269 1885 1581 137 C ATOM 686 N ILE A 83 -18.341 15.102 21.965 1.00 12.86 N ANISOU 686 N ILE A 83 1649 88 -7 1757 1479 260 N ATOM 687 CA ILE A 83 -17.629 16.367 22.206 1.00 13.89 C ANISOU 687 CA ILE A 83 1656 110 46 1901 1720 126 C ATOM 688 C ILE A 83 -18.366 17.471 21.462 1.00 14.29 C ANISOU 688 C ILE A 83 1576 159 33 2082 1769 48 C ATOM 689 O ILE A 83 -18.587 17.381 20.213 1.00 13.73 O ANISOU 689 O ILE A 83 1575 430 40 2040 1599 45 O ATOM 690 CB ILE A 83 -16.169 16.334 21.747 1.00 12.99 C ANISOU 690 CB ILE A 83 1609 -20 -30 1799 1526 54 C ATOM 691 CG1 ILE A 83 -15.470 15.100 22.242 1.00 13.59 C ANISOU 691 CG1 ILE A 83 1468 -64 -213 2058 1636 89 C ATOM 692 CG2 ILE A 83 -15.408 17.616 22.265 1.00 13.06 C ANISOU 692 CG2 ILE A 83 1766 68 59 1743 1450 56 C ATOM 693 CD1 ILE A 83 -13.993 14.970 21.688 1.00 14.86 C ANISOU 693 CD1 ILE A 83 1548 45 -33 2087 2010 137 C ATOM 694 N LYS A 84 -18.740 18.499 22.212 1.00 15.81 N ANISOU 694 N LYS A 84 1847 142 -3 2185 1973 28 N ATOM 695 CA LYS A 84 -19.368 19.652 21.588 1.00 16.94 C ANISOU 695 CA LYS A 84 1862 164 -58 2386 2189 147 C ATOM 696 C LYS A 84 -18.330 20.741 21.390 1.00 16.18 C ANISOU 696 C LYS A 84 1895 111 -60 2130 2123 141 C ATOM 697 O LYS A 84 -17.420 20.922 22.192 1.00 18.34 O ANISOU 697 O LYS A 84 2043 257 181 2506 2417 348 O ATOM 698 CB LYS A 84 -20.590 20.134 22.347 1.00 20.17 C ANISOU 698 CB LYS A 84 2377 224 -152 2770 2517 18 C ATOM 699 CG LYS A 84 -20.377 20.996 23.479 1.00 23.16 C ANISOU 699 CG LYS A 84 2401 48 -174 3496 2901 360 C ATOM 700 CD LYS A 84 -21.762 21.505 24.014 1.00 25.71 C ANISOU 700 CD LYS A 84 2786 363 -260 3701 3281 174 C ATOM 701 CE LYS A 84 -21.679 22.013 25.439 1.00 30.77 C ANISOU 701 CE LYS A 84 3546 119 -321 4196 3947 -62 C ATOM 702 NZ LYS A 84 -20.285 22.214 25.988 1.00 35.55 N ANISOU 702 NZ LYS A 84 4096 20 -499 4656 4753 13 N ATOM 703 N ASN A 85 -18.475 21.450 20.286 1.00 15.27 N ANISOU 703 N ASN A 85 1816 158 -160 1960 2025 324 N ATOM 704 CA ASN A 85 -17.620 22.618 20.011 1.00 15.82 C ANISOU 704 CA ASN A 85 1872 104 -206 1914 2222 261 C ATOM 705 C ASN A 85 -17.973 23.776 20.926 1.00 15.86 C ANISOU 705 C ASN A 85 1900 70 -230 1869 2256 227 C ATOM 706 O ASN A 85 -18.910 23.713 21.708 1.00 17.15 O ANISOU 706 O ASN A 85 2172 222 -254 2041 2302 336 O ATOM 707 CB ASN A 85 -17.628 22.994 18.524 1.00 14.62 C ANISOU 707 CB ASN A 85 1702 214 -180 1620 2233 164 C ATOM 708 CG ASN A 85 -18.957 23.492 18.012 1.00 14.81 C ANISOU 708 CG ASN A 85 1937 -61 -57 1518 2169 45 C ATOM 709 OD1 ASN A 85 -19.547 22.890 17.047 1.00 16.27 O ANISOU 709 OD1 ASN A 85 2096 -23 -83 2129 1956 1 O ATOM 710 ND2 ASN A 85 -19.456 24.537 18.618 1.00 13.96 N ANISOU 710 ND2 ASN A 85 1235 204 -78 1530 2536 525 N ATOM 711 N SER A 86 -17.195 24.847 20.813 1.00 17.04 N ANISOU 711 N SER A 86 1976 -20 -336 1939 2557 248 N ATOM 712 CA SER A 86 -17.279 25.993 21.736 1.00 18.51 C ANISOU 712 CA SER A 86 2355 109 -262 2210 2466 283 C ATOM 713 C SER A 86 -18.525 26.803 21.613 1.00 18.94 C ANISOU 713 C SER A 86 2450 143 -313 2218 2529 431 C ATOM 714 O SER A 86 -18.810 27.627 22.496 1.00 21.58 O ANISOU 714 O SER A 86 2959 197 -453 2537 2700 461 O ATOM 715 CB SER A 86 -16.116 26.944 21.465 1.00 17.63 C ANISOU 715 CB SER A 86 2246 149 -272 2016 2437 254 C ATOM 716 OG SER A 86 -16.241 27.529 20.162 1.00 19.29 O ANISOU 716 OG SER A 86 3172 29 -255 1842 2314 -215 O ATOM 717 N ARG A 87 -19.236 26.662 20.490 1.00 18.77 N ANISOU 717 N ARG A 87 2441 116 -164 2130 2558 480 N ATOM 718 CA ARG A 87 -20.435 27.416 20.223 1.00 20.17 C ANISOU 718 CA ARG A 87 2586 178 -170 2279 2796 526 C ATOM 719 C ARG A 87 -20.148 28.925 20.067 1.00 21.09 C ANISOU 719 C ARG A 87 2725 324 -144 2220 3066 549 C ATOM 720 O ARG A 87 -21.061 29.749 20.239 1.00 22.21 O ANISOU 720 O ARG A 87 2916 590 -251 2160 3363 922 O ATOM 721 CB ARG A 87 -21.509 27.142 21.280 1.00 20.56 C ANISOU 721 CB ARG A 87 2533 256 -50 2408 2870 466 C ATOM 722 CG ARG A 87 -21.940 25.687 21.355 1.00 19.21 C ANISOU 722 CG ARG A 87 2260 97 117 2545 2491 470 C ATOM 723 CD ARG A 87 -22.893 25.279 20.290 1.00 17.86 C ANISOU 723 CD ARG A 87 1490 278 -181 2706 2589 348 C ATOM 724 NE ARG A 87 -23.408 23.919 20.498 1.00 18.52 N ANISOU 724 NE ARG A 87 1608 475 -160 2561 2865 496 N ATOM 725 CZ ARG A 87 -22.888 22.798 19.950 1.00 16.73 C ANISOU 725 CZ ARG A 87 1630 446 159 2266 2461 162 C ATOM 726 NH1 ARG A 87 -21.843 22.841 19.148 1.00 18.07 N ANISOU 726 NH1 ARG A 87 1770 408 87 2532 2560 364 N ATOM 727 NH2 ARG A 87 -23.422 21.623 20.194 1.00 17.70 N ANISOU 727 NH2 ARG A 87 1849 153 -114 2365 2508 449 N ATOM 728 N ALA A 88 -18.884 29.286 19.777 1.00 20.78 N ANISOU 728 N ALA A 88 2707 399 -123 2023 3164 631 N ATOM 729 CA ALA A 88 -18.474 30.710 19.710 1.00 20.92 C ANISOU 729 CA ALA A 88 2663 362 -226 2075 3209 456 C ATOM 730 C ALA A 88 -19.036 31.401 18.488 1.00 21.28 C ANISOU 730 C ALA A 88 2871 383 -82 1950 3263 517 C ATOM 731 O ALA A 88 -19.344 32.625 18.523 1.00 23.27 O ANISOU 731 O ALA A 88 3168 487 -232 1912 3761 538 O ATOM 732 CB ALA A 88 -16.997 30.880 19.755 1.00 21.56 C ANISOU 732 CB ALA A 88 2844 275 -280 1967 3380 416 C ATOM 733 N SER A 89 -19.170 30.670 17.392 1.00 19.41 N ANISOU 733 N SER A 89 2498 284 -146 1815 3060 350 N ATOM 734 CA SER A 89 -19.677 31.225 16.156 1.00 20.33 C ANISOU 734 CA SER A 89 2417 481 99 2143 3163 279 C ATOM 735 C SER A 89 -20.379 30.166 15.381 1.00 19.78 C ANISOU 735 C SER A 89 2376 533 163 2062 3077 131 C ATOM 736 O SER A 89 -20.362 28.961 15.750 1.00 20.60 O ANISOU 736 O SER A 89 2417 468 287 2379 3030 155 O ATOM 737 CB SER A 89 -18.547 31.780 15.267 1.00 21.08 C ANISOU 737 CB SER A 89 2604 409 127 2149 3255 345 C ATOM 738 OG SER A 89 -17.911 30.719 14.493 1.00 19.26 O ANISOU 738 OG SER A 89 2494 140 24 1849 2972 503 O ATOM 739 N SER A 90 -20.878 30.553 14.208 1.00 20.60 N ANISOU 739 N SER A 90 2396 581 245 2326 3105 -82 N ATOM 740 CA SER A 90 -21.563 29.618 13.306 1.00 20.36 C ANISOU 740 CA SER A 90 2400 394 251 2321 3013 -100 C ATOM 741 C SER A 90 -20.678 28.552 12.681 1.00 19.81 C ANISOU 741 C SER A 90 2341 353 178 2260 2925 -224 C ATOM 742 O SER A 90 -21.193 27.625 12.025 1.00 20.37 O ANISOU 742 O SER A 90 2332 202 399 2367 3039 -528 O ATOM 743 CB SER A 90 -22.265 30.355 12.173 1.00 22.60 C ANISOU 743 CB SER A 90 2540 465 291 2793 3253 -64 C ATOM 744 OG SER A 90 -21.372 30.995 11.308 1.00 25.09 O ANISOU 744 OG SER A 90 2741 479 724 3285 3507 -591 O ATOM 745 N VAL A 91 -19.361 28.705 12.831 1.00 17.54 N ANISOU 745 N VAL A 91 2052 314 345 2041 2571 -165 N ATOM 746 CA VAL A 91 -18.432 27.735 12.300 1.00 17.29 C ANISOU 746 CA VAL A 91 2152 201 148 2001 2415 -121 C ATOM 747 C VAL A 91 -17.535 27.119 13.351 1.00 15.84 C ANISOU 747 C VAL A 91 1949 272 188 1876 2193 -34 C ATOM 748 O VAL A 91 -16.532 26.472 13.038 1.00 15.86 O ANISOU 748 O VAL A 91 1962 337 44 2000 2062 183 O ATOM 749 CB VAL A 91 -17.565 28.279 11.139 1.00 16.90 C ANISOU 749 CB VAL A 91 2231 160 257 1869 2319 -223 C ATOM 750 CG1 VAL A 91 -18.442 28.773 10.031 1.00 19.07 C ANISOU 750 CG1 VAL A 91 2358 100 352 2232 2652 -190 C ATOM 751 CG2 VAL A 91 -16.584 29.373 11.599 1.00 18.05 C ANISOU 751 CG2 VAL A 91 2456 -74 344 2142 2258 -369 C ATOM 752 N SER A 92 -17.872 27.265 14.617 1.00 16.01 N ANISOU 752 N SER A 92 1797 348 150 2171 2113 -110 N ATOM 753 CA SER A 92 -17.026 26.630 15.638 1.00 15.35 C ANISOU 753 CA SER A 92 1833 421 210 1822 2175 42 C ATOM 754 C SER A 92 -17.056 25.120 15.426 1.00 14.69 C ANISOU 754 C SER A 92 1622 244 -37 1841 2116 -53 C ATOM 755 O SER A 92 -18.040 24.535 14.978 1.00 14.22 O ANISOU 755 O SER A 92 1491 366 170 1663 2249 -127 O ATOM 756 CB SER A 92 -17.527 26.976 17.045 1.00 16.20 C ANISOU 756 CB SER A 92 2074 289 152 2061 2019 122 C ATOM 757 OG SER A 92 -17.534 28.381 17.278 1.00 17.32 O ANISOU 757 OG SER A 92 2289 395 -73 1838 2454 271 O ATOM 758 N ARG A 93 -15.965 24.467 15.774 1.00 14.14 N ANISOU 758 N ARG A 93 1563 249 -30 1801 2007 -60 N ATOM 759 CA ARG A 93 -15.802 23.094 15.436 1.00 13.35 C ANISOU 759 CA ARG A 93 1511 200 137 1574 1986 -61 C ATOM 760 C ARG A 93 -14.772 22.417 16.259 1.00 13.76 C ANISOU 760 C ARG A 93 1566 193 54 1603 2060 -105 C ATOM 761 O ARG A 93 -13.739 23.026 16.605 1.00 14.31 O ANISOU 761 O ARG A 93 1843 334 170 1418 2174 -31 O ATOM 762 CB ARG A 93 -15.435 22.940 13.954 1.00 14.52 C ANISOU 762 CB ARG A 93 1477 172 48 1796 2244 -217 C ATOM 763 CG ARG A 93 -14.268 23.710 13.475 1.00 15.13 C ANISOU 763 CG ARG A 93 1854 317 122 1525 2370 93 C ATOM 764 CD ARG A 93 -14.148 23.712 11.980 1.00 15.19 C ANISOU 764 CD ARG A 93 1729 112 229 1762 2277 171 C ATOM 765 NE ARG A 93 -12.964 24.456 11.544 1.00 18.72 N ANISOU 765 NE ARG A 93 2096 163 187 2049 2965 351 N ATOM 766 CZ ARG A 93 -12.929 25.767 11.372 1.00 19.05 C ANISOU 766 CZ ARG A 93 2410 -19 221 2154 2673 743 C ATOM 767 NH1 ARG A 93 -14.022 26.514 11.554 1.00 18.84 N ANISOU 767 NH1 ARG A 93 2210 60 374 2156 2789 319 N ATOM 768 NH2 ARG A 93 -11.822 26.349 10.951 1.00 19.28 N ANISOU 768 NH2 ARG A 93 2182 73 92 2197 2945 824 N ATOM 769 N VAL A 94 -15.079 21.145 16.581 1.00 12.01 N ANISOU 769 N VAL A 94 1413 139 227 1371 1779 -98 N ATOM 770 CA VAL A 94 -14.051 20.223 17.114 1.00 11.33 C ANISOU 770 CA VAL A 94 1298 201 32 1360 1646 0 C ATOM 771 C VAL A 94 -13.791 19.259 15.950 1.00 12.25 C ANISOU 771 C VAL A 94 1402 202 83 1505 1748 6 C ATOM 772 O VAL A 94 -14.719 18.837 15.266 1.00 13.30 O ANISOU 772 O VAL A 94 1599 255 23 1855 1596 121 O ATOM 773 CB VAL A 94 -14.437 19.545 18.428 1.00 11.16 C ANISOU 773 CB VAL A 94 1392 274 -144 1275 1571 -26 C ATOM 774 CG1 VAL A 94 -14.264 20.446 19.618 1.00 13.42 C ANISOU 774 CG1 VAL A 94 1563 73 -112 1660 1876 264 C ATOM 775 CG2 VAL A 94 -15.814 18.969 18.361 1.00 12.25 C ANISOU 775 CG2 VAL A 94 1477 227 -73 1723 1453 26 C ATOM 776 N VAL A 95 -12.510 19.005 15.692 1.00 12.06 N ANISOU 776 N VAL A 95 1412 281 152 1577 1593 -17 N ATOM 777 CA VAL A 95 -12.077 18.425 14.428 1.00 11.17 C ANISOU 777 CA VAL A 95 1170 184 168 1537 1536 -17 C ATOM 778 C VAL A 95 -11.134 17.257 14.549 1.00 10.39 C ANISOU 778 C VAL A 95 1244 92 117 1321 1380 -50 C ATOM 779 O VAL A 95 -10.309 17.167 15.461 1.00 10.21 O ANISOU 779 O VAL A 95 1150 19 -48 1600 1129 -191 O ATOM 780 CB VAL A 95 -11.429 19.486 13.484 1.00 12.49 C ANISOU 780 CB VAL A 95 1462 297 333 1647 1636 105 C ATOM 781 CG1 VAL A 95 -12.342 20.638 13.202 1.00 14.28 C ANISOU 781 CG1 VAL A 95 1777 293 320 1726 1923 159 C ATOM 782 CG2 VAL A 95 -10.122 19.986 14.041 1.00 13.10 C ANISOU 782 CG2 VAL A 95 1646 107 178 1836 1495 -57 C ATOM 783 N ASP A 96 -11.271 16.360 13.590 1.00 10.08 N ANISOU 783 N ASP A 96 1311 220 -42 1402 1114 -160 N ATOM 784 CA ASP A 96 -10.335 15.252 13.344 1.00 10.02 C ANISOU 784 CA ASP A 96 1210 130 95 1335 1262 -142 C ATOM 785 C ASP A 96 -10.145 14.389 14.575 1.00 10.17 C ANISOU 785 C ASP A 96 1210 83 145 1413 1241 -118 C ATOM 786 O ASP A 96 -9.011 14.170 15.025 1.00 11.29 O ANISOU 786 O ASP A 96 1135 77 195 1657 1498 17 O ATOM 787 CB ASP A 96 -9.012 15.710 12.756 1.00 10.87 C ANISOU 787 CB ASP A 96 1478 264 122 1297 1356 -246 C ATOM 788 CG ASP A 96 -9.134 16.199 11.338 1.00 12.25 C ANISOU 788 CG ASP A 96 1606 46 147 1566 1480 -161 C ATOM 789 OD1 ASP A 96 -8.075 16.351 10.704 1.00 14.61 O ANISOU 789 OD1 ASP A 96 1937 -332 262 1883 1728 194 O ATOM 790 OD2 ASP A 96 -10.272 16.432 10.784 1.00 13.75 O ANISOU 790 OD2 ASP A 96 1910 -50 175 1702 1611 -352 O ATOM 791 N PRO A 97 -11.245 13.894 15.119 1.00 11.38 N ANISOU 791 N PRO A 97 1353 -5 50 1633 1335 -267 N ATOM 792 CA PRO A 97 -11.163 13.146 16.362 1.00 10.82 C ANISOU 792 CA PRO A 97 1390 11 46 1449 1271 -124 C ATOM 793 C PRO A 97 -10.278 11.946 16.194 1.00 11.22 C ANISOU 793 C PRO A 97 1257 74 31 1511 1494 -263 C ATOM 794 O PRO A 97 -10.464 11.166 15.218 1.00 13.31 O ANISOU 794 O PRO A 97 1808 407 55 1675 1572 -449 O ATOM 795 CB PRO A 97 -12.635 12.752 16.645 1.00 10.29 C ANISOU 795 CB PRO A 97 1341 -73 -6 1456 1110 -315 C ATOM 796 CG PRO A 97 -13.359 12.809 15.333 1.00 10.46 C ANISOU 796 CG PRO A 97 1234 80 2 1644 1094 -507 C ATOM 797 CD PRO A 97 -12.628 13.974 14.610 1.00 11.11 C ANISOU 797 CD PRO A 97 1167 191 83 1708 1343 -127 C ATOM 798 N THR A 98 -9.324 11.782 17.105 1.00 9.86 N ANISOU 798 N THR A 98 1342 61 16 1385 1018 -221 N ATOM 799 CA THR A 98 -8.364 10.688 17.046 1.00 9.46 C ANISOU 799 CA THR A 98 1207 -42 99 1287 1099 -210 C ATOM 800 C THR A 98 -8.514 9.891 18.344 1.00 9.79 C ANISOU 800 C THR A 98 1213 1 100 1414 1092 -243 C ATOM 801 O THR A 98 -8.469 10.475 19.439 1.00 10.04 O ANISOU 801 O THR A 98 1326 -6 140 1430 1059 -169 O ATOM 802 CB THR A 98 -6.976 11.255 16.887 1.00 9.50 C ANISOU 802 CB THR A 98 1138 134 56 1308 1163 -173 C ATOM 803 OG1 THR A 98 -6.974 12.160 15.767 1.00 10.70 O ANISOU 803 OG1 THR A 98 1557 10 337 1385 1121 121 O ATOM 804 CG2 THR A 98 -5.977 10.142 16.564 1.00 10.63 C ANISOU 804 CG2 THR A 98 1392 205 237 1415 1229 -303 C ATOM 805 N VAL A 99 -8.704 8.579 18.222 1.00 10.38 N ANISOU 805 N VAL A 99 1401 32 138 1489 1054 -224 N ATOM 806 CA VAL A 99 -9.168 7.769 19.366 1.00 9.76 C ANISOU 806 CA VAL A 99 1190 -24 257 1379 1139 -120 C ATOM 807 C VAL A 99 -8.142 6.775 19.857 1.00 9.33 C ANISOU 807 C VAL A 99 1264 24 270 1445 836 -149 C ATOM 808 O VAL A 99 -7.525 6.098 19.023 1.00 10.26 O ANISOU 808 O VAL A 99 1289 37 378 1598 1011 -147 O ATOM 809 CB VAL A 99 -10.425 6.976 18.920 1.00 10.73 C ANISOU 809 CB VAL A 99 1348 -42 313 1571 1155 -178 C ATOM 810 CG1 VAL A 99 -10.983 6.124 20.053 1.00 13.36 C ANISOU 810 CG1 VAL A 99 1504 -259 164 2058 1510 -232 C ATOM 811 CG2 VAL A 99 -11.496 7.921 18.339 1.00 12.39 C ANISOU 811 CG2 VAL A 99 1424 -10 441 1913 1370 202 C ATOM 812 N ILE A 100 -7.956 6.691 21.184 1.00 9.68 N ANISOU 812 N ILE A 100 1303 36 336 1461 911 -218 N ATOM 813 CA ILE A 100 -7.212 5.575 21.794 1.00 10.33 C ANISOU 813 CA ILE A 100 1425 -46 260 1498 1001 -45 C ATOM 814 C ILE A 100 -8.150 4.897 22.754 1.00 10.71 C ANISOU 814 C ILE A 100 1587 -167 332 1558 924 -142 C ATOM 815 O ILE A 100 -8.879 5.542 23.513 1.00 12.48 O ANISOU 815 O ILE A 100 1651 -148 525 1823 1268 87 O ATOM 816 CB ILE A 100 -5.966 6.054 22.552 1.00 8.81 C ANISOU 816 CB ILE A 100 1270 15 215 1376 698 -196 C ATOM 817 CG1 ILE A 100 -5.007 6.780 21.602 1.00 12.26 C ANISOU 817 CG1 ILE A 100 1470 -91 331 1540 1648 -341 C ATOM 818 CG2 ILE A 100 -5.283 4.909 23.212 1.00 11.33 C ANISOU 818 CG2 ILE A 100 1380 -157 179 1663 1259 -155 C ATOM 819 CD1 ILE A 100 -3.846 7.513 22.276 1.00 12.22 C ANISOU 819 CD1 ILE A 100 1550 -1 279 1720 1370 -214 C ATOM 820 N VAL A 101 -8.119 3.594 22.724 1.00 11.91 N ANISOU 820 N VAL A 101 1770 -173 429 1624 1131 -26 N ATOM 821 CA VAL A 101 -8.834 2.787 23.737 1.00 12.20 C ANISOU 821 CA VAL A 101 1748 -227 554 1767 1118 -126 C ATOM 822 C VAL A 101 -7.858 2.230 24.763 1.00 13.70 C ANISOU 822 C VAL A 101 1899 -348 504 2037 1270 -151 C ATOM 823 O VAL A 101 -6.871 1.627 24.382 1.00 12.39 O ANISOU 823 O VAL A 101 1873 -383 562 2020 815 -369 O ATOM 824 CB VAL A 101 -9.570 1.602 23.094 1.00 12.59 C ANISOU 824 CB VAL A 101 1660 -304 558 2038 1084 -222 C ATOM 825 CG1 VAL A 101 -10.230 0.735 24.143 1.00 12.77 C ANISOU 825 CG1 VAL A 101 1770 -478 433 1878 1201 -424 C ATOM 826 CG2 VAL A 101 -10.581 2.073 22.081 1.00 13.96 C ANISOU 826 CG2 VAL A 101 1621 -373 766 2036 1646 -307 C ATOM 827 N LYS A 102 -8.165 2.418 26.052 1.00 15.26 N ANISOU 827 N LYS A 102 1859 -482 539 2400 1539 -134 N ATOM 828 CA LYS A 102 -7.423 1.769 27.095 1.00 15.95 C ANISOU 828 CA LYS A 102 1835 -383 538 2695 1527 -183 C ATOM 829 C LYS A 102 -8.405 1.308 28.178 1.00 16.80 C ANISOU 829 C LYS A 102 1862 -390 535 3010 1508 -332 C ATOM 830 O LYS A 102 -9.105 2.104 28.720 1.00 16.94 O ANISOU 830 O LYS A 102 1654 -476 780 3961 821 -350 O ATOM 831 CB LYS A 102 -6.321 2.704 27.644 1.00 16.51 C ANISOU 831 CB LYS A 102 1873 -389 565 2746 1651 -166 C ATOM 832 CG LYS A 102 -5.327 2.031 28.512 1.00 18.04 C ANISOU 832 CG LYS A 102 2109 -543 371 2733 2012 -105 C ATOM 833 CD LYS A 102 -4.117 3.045 28.828 1.00 20.00 C ANISOU 833 CD LYS A 102 2720 -190 -70 2906 1973 -395 C ATOM 834 CE LYS A 102 -3.287 2.497 29.717 1.00 19.67 C ANISOU 834 CE LYS A 102 3197 382 -325 2150 2124 -302 C ATOM 835 NZ LYS A 102 -2.139 3.244 30.028 1.00 12.23 N ANISOU 835 NZ LYS A 102 1170 -92 143 1676 1799 -254 N ATOM 836 N GLY A 103 -8.432 -0.005 28.420 1.00 19.44 N ANISOU 836 N GLY A 103 1909 -374 799 3597 1879 -198 N ATOM 837 CA GLY A 103 -9.415 -0.608 29.304 1.00 19.69 C ANISOU 837 CA GLY A 103 1871 -451 844 3557 2050 -165 C ATOM 838 C GLY A 103 -10.831 -0.296 28.824 1.00 19.13 C ANISOU 838 C GLY A 103 1654 -438 818 3649 1965 -256 C ATOM 839 O GLY A 103 -11.176 -0.637 27.666 1.00 21.26 O ANISOU 839 O GLY A 103 1684 -600 1079 4163 2231 -303 O ATOM 840 N ASN A 104 -11.607 0.363 29.674 1.00 19.78 N ANISOU 840 N ASN A 104 1740 -504 999 3767 2007 -221 N ATOM 841 CA ASN A 104 -12.984 0.773 29.314 1.00 19.80 C ANISOU 841 CA ASN A 104 1737 -456 756 3851 1935 81 C ATOM 842 C ASN A 104 -13.118 2.276 28.997 1.00 18.78 C ANISOU 842 C ASN A 104 1629 -321 714 3747 1758 2 C ATOM 843 O ASN A 104 -14.201 2.845 29.048 1.00 20.39 O ANISOU 843 O ASN A 104 1849 -426 638 4055 1843 490 O ATOM 844 CB ASN A 104 -13.953 0.347 30.420 1.00 22.24 C ANISOU 844 CB ASN A 104 1996 -551 717 4354 2101 47 C ATOM 845 CG ASN A 104 -13.955 1.294 31.577 1.00 25.70 C ANISOU 845 CG ASN A 104 2265 -530 699 5187 2311 337 C ATOM 846 OD1 ASN A 104 -12.898 1.825 31.966 1.00 33.91 O ANISOU 846 OD1 ASN A 104 3395 -827 838 6645 2841 500 O ATOM 847 ND2 ASN A 104 -15.130 1.470 32.206 1.00 29.76 N ANISOU 847 ND2 ASN A 104 3037 0 1263 6033 2236 228 N ATOM 848 N LYS A 105 -11.992 2.930 28.660 1.00 18.32 N ANISOU 848 N LYS A 105 1874 -339 824 3417 1669 109 N ATOM 849 CA LYS A 105 -11.969 4.354 28.392 1.00 17.80 C ANISOU 849 CA LYS A 105 1895 -270 518 3115 1750 207 C ATOM 850 C LYS A 105 -11.587 4.595 26.927 1.00 16.79 C ANISOU 850 C LYS A 105 1792 -252 435 2988 1598 204 C ATOM 851 O LYS A 105 -10.752 3.904 26.358 1.00 16.98 O ANISOU 851 O LYS A 105 1662 -389 525 3044 1743 182 O ATOM 852 CB LYS A 105 -10.966 5.080 29.277 1.00 18.93 C ANISOU 852 CB LYS A 105 2336 -108 361 3098 1756 242 C ATOM 853 CG LYS A 105 -11.122 4.852 30.773 1.00 26.40 C ANISOU 853 CG LYS A 105 3498 -66 256 3884 2646 225 C ATOM 854 CD LYS A 105 -11.639 5.924 31.500 1.00 29.49 C ANISOU 854 CD LYS A 105 4289 90 100 3955 2960 262 C ATOM 855 CE LYS A 105 -11.827 5.586 33.053 1.00 26.21 C ANISOU 855 CE LYS A 105 3604 393 -446 4152 2201 426 C ATOM 856 NZ LYS A 105 -10.739 6.322 33.865 1.00 32.97 N ANISOU 856 NZ LYS A 105 4305 766 -324 4702 3517 540 N ATOM 857 N LEU A 106 -12.265 5.565 26.349 1.00 15.91 N ANISOU 857 N LEU A 106 1874 -409 493 2663 1506 338 N ATOM 858 CA LEU A 106 -11.928 6.194 25.058 1.00 15.77 C ANISOU 858 CA LEU A 106 1825 -349 419 2584 1581 134 C ATOM 859 C LEU A 106 -11.292 7.538 25.319 1.00 15.33 C ANISOU 859 C LEU A 106 1818 -266 221 2456 1551 134 C ATOM 860 O LEU A 106 -11.925 8.420 25.907 1.00 18.06 O ANISOU 860 O LEU A 106 1917 -504 76 2889 2053 248 O ATOM 861 CB LEU A 106 -13.232 6.501 24.269 1.00 17.83 C ANISOU 861 CB LEU A 106 2154 -332 568 2671 1949 288 C ATOM 862 CG LEU A 106 -14.082 5.346 23.844 1.00 19.92 C ANISOU 862 CG LEU A 106 2242 -240 221 2966 2358 -43 C ATOM 863 CD1 LEU A 106 -15.538 5.560 24.112 1.00 24.08 C ANISOU 863 CD1 LEU A 106 2788 -521 -28 3225 3136 436 C ATOM 864 CD2 LEU A 106 -13.865 5.117 22.395 1.00 24.11 C ANISOU 864 CD2 LEU A 106 3067 -604 -102 3482 2609 478 C ATOM 865 N TYR A 107 -10.104 7.737 24.777 1.00 13.37 N ANISOU 865 N TYR A 107 1630 -182 145 2225 1222 161 N ATOM 866 CA TYR A 107 -9.427 9.033 24.800 1.00 12.56 C ANISOU 866 CA TYR A 107 1644 -24 190 1958 1167 112 C ATOM 867 C TYR A 107 -9.549 9.595 23.389 1.00 11.41 C ANISOU 867 C TYR A 107 1631 49 135 1700 1001 26 C ATOM 868 O TYR A 107 -9.133 8.951 22.431 1.00 12.93 O ANISOU 868 O TYR A 107 2031 79 275 1857 1023 356 O ATOM 869 CB TYR A 107 -7.953 8.823 25.094 1.00 12.88 C ANISOU 869 CB TYR A 107 1719 190 185 1943 1229 -107 C ATOM 870 CG TYR A 107 -7.728 8.324 26.458 1.00 14.69 C ANISOU 870 CG TYR A 107 1754 78 250 2550 1277 -91 C ATOM 871 CD1 TYR A 107 -7.505 9.208 27.499 1.00 17.46 C ANISOU 871 CD1 TYR A 107 1940 133 453 2954 1738 59 C ATOM 872 CD2 TYR A 107 -7.819 6.943 26.742 1.00 15.79 C ANISOU 872 CD2 TYR A 107 1892 13 805 2992 1112 -283 C ATOM 873 CE1 TYR A 107 -7.357 8.735 28.790 1.00 20.03 C ANISOU 873 CE1 TYR A 107 2309 313 149 3555 1746 -195 C ATOM 874 CE2 TYR A 107 -7.651 6.478 28.051 1.00 19.50 C ANISOU 874 CE2 TYR A 107 2319 104 535 3305 1783 -285 C ATOM 875 CZ TYR A 107 -7.444 7.392 29.047 1.00 16.80 C ANISOU 875 CZ TYR A 107 2133 359 809 3274 974 -223 C ATOM 876 OH TYR A 107 -7.270 6.919 30.349 1.00 23.49 O ANISOU 876 OH TYR A 107 2792 482 812 4489 1642 -690 O ATOM 877 N VAL A 108 -10.192 10.753 23.281 1.00 11.08 N ANISOU 877 N VAL A 108 1618 45 162 1655 937 -18 N ATOM 878 CA VAL A 108 -10.469 11.369 21.978 1.00 11.53 C ANISOU 878 CA VAL A 108 1473 49 125 1681 1225 -29 C ATOM 879 C VAL A 108 -9.796 12.745 21.947 1.00 11.94 C ANISOU 879 C VAL A 108 1586 5 110 1727 1221 46 C ATOM 880 O VAL A 108 -10.069 13.632 22.776 1.00 11.44 O ANISOU 880 O VAL A 108 1409 -137 -44 1782 1154 41 O ATOM 881 CB VAL A 108 -11.970 11.451 21.705 1.00 12.00 C ANISOU 881 CB VAL A 108 1494 62 101 1720 1343 65 C ATOM 882 CG1 VAL A 108 -12.254 12.092 20.372 1.00 12.86 C ANISOU 882 CG1 VAL A 108 1374 3 -245 1919 1591 -38 C ATOM 883 CG2 VAL A 108 -12.586 10.101 21.774 1.00 13.22 C ANISOU 883 CG2 VAL A 108 1344 -6 334 1943 1734 39 C ATOM 884 N LEU A 109 -8.910 12.907 20.969 1.00 10.89 N ANISOU 884 N LEU A 109 1313 72 79 1678 1145 64 N ATOM 885 CA LEU A 109 -8.120 14.097 20.791 1.00 10.22 C ANISOU 885 CA LEU A 109 1266 114 87 1392 1225 -77 C ATOM 886 C LEU A 109 -8.700 14.849 19.597 1.00 11.06 C ANISOU 886 C LEU A 109 1435 41 132 1552 1216 -82 C ATOM 887 O LEU A 109 -8.732 14.316 18.520 1.00 10.43 O ANISOU 887 O LEU A 109 1443 202 187 1519 998 -124 O ATOM 888 CB LEU A 109 -6.652 13.769 20.506 1.00 11.41 C ANISOU 888 CB LEU A 109 1484 11 180 1432 1417 -74 C ATOM 889 CG LEU A 109 -5.717 14.948 20.320 1.00 10.36 C ANISOU 889 CG LEU A 109 1169 117 146 1415 1352 -88 C ATOM 890 CD1 LEU A 109 -5.340 15.556 21.698 1.00 14.31 C ANISOU 890 CD1 LEU A 109 1659 -333 -258 1830 1946 214 C ATOM 891 CD2 LEU A 109 -4.428 14.497 19.658 1.00 10.92 C ANISOU 891 CD2 LEU A 109 1351 77 225 1286 1511 -216 C ATOM 892 N VAL A 110 -9.108 16.099 19.794 1.00 10.13 N ANISOU 892 N VAL A 110 1157 92 70 1515 1177 -68 N ATOM 893 CA VAL A 110 -9.665 16.926 18.723 1.00 10.49 C ANISOU 893 CA VAL A 110 1227 44 66 1567 1190 75 C ATOM 894 C VAL A 110 -9.007 18.314 18.711 1.00 10.54 C ANISOU 894 C VAL A 110 1374 61 92 1411 1218 81 C ATOM 895 O VAL A 110 -8.688 18.881 19.747 1.00 11.92 O ANISOU 895 O VAL A 110 1798 -27 -105 1226 1505 -55 O ATOM 896 CB VAL A 110 -11.187 17.159 18.833 1.00 10.67 C ANISOU 896 CB VAL A 110 1234 141 198 1478 1342 14 C ATOM 897 CG1 VAL A 110 -11.977 15.917 18.477 1.00 10.44 C ANISOU 897 CG1 VAL A 110 1495 -19 313 1673 797 -74 C ATOM 898 CG2 VAL A 110 -11.563 17.623 20.212 1.00 11.43 C ANISOU 898 CG2 VAL A 110 1272 0 -128 1470 1599 -222 C ATOM 899 N GLY A 111 -8.806 18.875 17.519 1.00 11.70 N ANISOU 899 N GLY A 111 1495 176 18 1629 1319 59 N ATOM 900 CA GLY A 111 -8.582 20.299 17.426 1.00 11.64 C ANISOU 900 CA GLY A 111 1391 71 -79 1591 1439 79 C ATOM 901 C GLY A 111 -9.874 21.047 17.718 1.00 12.23 C ANISOU 901 C GLY A 111 1371 55 40 1645 1630 -67 C ATOM 902 O GLY A 111 -10.963 20.494 17.548 1.00 12.55 O ANISOU 902 O GLY A 111 1295 46 85 1519 1954 167 O ATOM 903 N SER A 112 -9.752 22.308 18.098 1.00 12.24 N ANISOU 903 N SER A 112 1298 120 51 1621 1731 -108 N ATOM 904 CA SER A 112 -10.892 23.155 18.307 1.00 12.73 C ANISOU 904 CA SER A 112 1490 158 -12 1652 1692 16 C ATOM 905 C SER A 112 -10.628 24.510 17.671 1.00 13.43 C ANISOU 905 C SER A 112 1493 143 40 1670 1937 -75 C ATOM 906 O SER A 112 -9.551 25.088 17.891 1.00 14.57 O ANISOU 906 O SER A 112 1825 138 252 1482 2228 -270 O ATOM 907 CB SER A 112 -11.171 23.245 19.809 1.00 14.87 C ANISOU 907 CB SER A 112 1742 174 100 1984 1921 66 C ATOM 908 OG SER A 112 -12.328 24.048 20.086 1.00 18.93 O ANISOU 908 OG SER A 112 2213 430 -174 2895 2081 162 O ATOM 909 N TYR A 113 -11.573 24.978 16.849 1.00 12.91 N ANISOU 909 N TYR A 113 1549 40 -3 1516 1838 -72 N ATOM 910 CA TYR A 113 -11.517 26.278 16.183 1.00 13.68 C ANISOU 910 CA TYR A 113 1527 141 35 1664 2006 25 C ATOM 911 C TYR A 113 -12.790 27.051 16.498 1.00 14.48 C ANISOU 911 C TYR A 113 1661 216 -48 1686 2153 200 C ATOM 912 O TYR A 113 -13.863 26.459 16.561 1.00 13.81 O ANISOU 912 O TYR A 113 1364 270 -105 1674 2208 37 O ATOM 913 CB TYR A 113 -11.364 26.119 14.661 1.00 13.47 C ANISOU 913 CB TYR A 113 1674 100 118 1592 1851 20 C ATOM 914 CG TYR A 113 -10.049 25.507 14.338 1.00 12.20 C ANISOU 914 CG TYR A 113 1470 102 112 1464 1700 260 C ATOM 915 CD1 TYR A 113 -9.919 24.120 14.175 1.00 14.03 C ANISOU 915 CD1 TYR A 113 1726 60 142 1637 1967 53 C ATOM 916 CD2 TYR A 113 -8.897 26.295 14.233 1.00 12.60 C ANISOU 916 CD2 TYR A 113 1435 214 303 1232 2120 101 C ATOM 917 CE1 TYR A 113 -8.665 23.524 13.902 1.00 12.17 C ANISOU 917 CE1 TYR A 113 1416 -73 10 1523 1683 -239 C ATOM 918 CE2 TYR A 113 -7.641 25.712 13.912 1.00 12.89 C ANISOU 918 CE2 TYR A 113 1329 -96 -63 1766 1800 -355 C ATOM 919 CZ TYR A 113 -7.536 24.320 13.775 1.00 11.86 C ANISOU 919 CZ TYR A 113 1525 101 -58 1675 1304 268 C ATOM 920 OH TYR A 113 -6.304 23.746 13.547 1.00 12.36 O ANISOU 920 OH TYR A 113 1584 320 -295 1445 1664 -190 O ATOM 921 N ASN A 114 -12.653 28.362 16.740 1.00 13.60 N ANISOU 921 N ASN A 114 1520 253 45 1542 2104 42 N ATOM 922 CA ASN A 114 -13.794 29.171 17.165 1.00 15.95 C ANISOU 922 CA ASN A 114 1926 235 41 1877 2255 146 C ATOM 923 C ASN A 114 -14.505 29.824 15.985 1.00 15.86 C ANISOU 923 C ASN A 114 1925 325 134 1766 2333 149 C ATOM 924 O ASN A 114 -15.741 29.750 15.870 1.00 15.97 O ANISOU 924 O ASN A 114 1801 478 271 1790 2474 39 O ATOM 925 CB ASN A 114 -13.386 30.206 18.191 1.00 15.62 C ANISOU 925 CB ASN A 114 1987 347 109 1776 2170 181 C ATOM 926 CG ASN A 114 -13.151 29.611 19.550 1.00 19.67 C ANISOU 926 CG ASN A 114 2660 165 -124 2320 2492 -41 C ATOM 927 OD1 ASN A 114 -13.743 28.613 19.937 1.00 21.25 O ANISOU 927 OD1 ASN A 114 2986 -191 -147 2738 2350 280 O ATOM 928 ND2 ASN A 114 -12.236 30.193 20.259 1.00 27.94 N ANISOU 928 ND2 ASN A 114 3600 -255 -194 3237 3776 -469 N ATOM 929 N SER A 115 -13.726 30.473 15.114 1.00 16.23 N ANISOU 929 N SER A 115 1840 270 106 1860 2465 313 N ATOM 930 CA SER A 115 -14.324 31.247 14.031 1.00 17.02 C ANISOU 930 CA SER A 115 1991 378 62 1928 2546 206 C ATOM 931 C SER A 115 -13.596 31.270 12.686 1.00 16.29 C ANISOU 931 C SER A 115 1854 415 237 1899 2434 224 C ATOM 932 O SER A 115 -14.080 31.916 11.749 1.00 18.71 O ANISOU 932 O SER A 115 2096 852 243 2184 2828 289 O ATOM 933 CB SER A 115 -14.657 32.692 14.488 1.00 18.04 C ANISOU 933 CB SER A 115 1915 342 112 1954 2984 102 C ATOM 934 OG SER A 115 -13.482 33.471 14.624 1.00 21.18 O ANISOU 934 OG SER A 115 2559 485 -296 2279 3207 541 O ATOM 935 N SER A 116 -12.467 30.587 12.538 1.00 15.26 N ANISOU 935 N SER A 116 1890 468 258 1660 2247 77 N ATOM 936 CA SER A 116 -11.741 30.677 11.288 1.00 16.97 C ANISOU 936 CA SER A 116 2089 418 61 1928 2429 171 C ATOM 937 C SER A 116 -12.527 30.035 10.145 1.00 16.69 C ANISOU 937 C SER A 116 2255 496 133 1802 2283 112 C ATOM 938 O SER A 116 -13.116 28.982 10.351 1.00 16.42 O ANISOU 938 O SER A 116 2072 -183 169 2237 1927 314 O ATOM 939 CB SER A 116 -10.352 30.053 11.394 1.00 18.14 C ANISOU 939 CB SER A 116 2072 387 -44 2410 2411 128 C ATOM 940 OG SER A 116 -9.738 30.117 10.111 1.00 18.77 O ANISOU 940 OG SER A 116 2052 436 34 2474 2605 291 O ATOM 941 N ARG A 117 -12.424 30.557 8.931 1.00 18.13 N ANISOU 941 N ARG A 117 2456 417 217 1941 2491 361 N ATOM 942 CA ARG A 117 -12.985 29.894 7.769 1.00 19.89 C ANISOU 942 CA ARG A 117 2592 448 290 2316 2647 179 C ATOM 943 C ARG A 117 -11.882 29.382 6.853 1.00 19.81 C ANISOU 943 C ARG A 117 2552 413 183 2429 2543 220 C ATOM 944 O ARG A 117 -12.195 28.823 5.797 1.00 22.48 O ANISOU 944 O ARG A 117 2897 359 -65 2907 2736 427 O ATOM 945 CB ARG A 117 -13.991 30.795 6.988 1.00 21.55 C ANISOU 945 CB ARG A 117 2688 623 402 2663 2835 186 C ATOM 946 CG ARG A 117 -15.447 30.635 7.543 1.00 25.34 C ANISOU 946 CG ARG A 117 3085 403 471 3222 3318 47 C ATOM 947 CD ARG A 117 -16.420 31.828 7.652 1.00 29.98 C ANISOU 947 CD ARG A 117 4186 293 247 3483 3722 -117 C ATOM 948 NE ARG A 117 -16.397 32.235 9.038 1.00 35.39 N ANISOU 948 NE ARG A 117 5207 161 413 4442 3797 158 N ATOM 949 CZ ARG A 117 -17.365 32.646 9.865 1.00 30.29 C ANISOU 949 CZ ARG A 117 3842 557 499 3512 4155 -68 C ATOM 950 NH1 ARG A 117 -18.693 32.818 9.593 1.00 30.05 N ANISOU 950 NH1 ARG A 117 3923 786 794 3294 4197 -235 N ATOM 951 NH2 ARG A 117 -16.921 32.954 11.066 1.00 30.22 N ANISOU 951 NH2 ARG A 117 4300 691 673 3843 3336 -27 N ATOM 952 N SER A 118 -10.629 29.453 7.313 1.00 18.02 N ANISOU 952 N SER A 118 2479 301 185 1928 2439 138 N ATOM 953 CA SER A 118 -9.486 29.053 6.492 1.00 16.05 C ANISOU 953 CA SER A 118 2214 368 268 1626 2258 -22 C ATOM 954 C SER A 118 -8.903 27.703 6.942 1.00 14.80 C ANISOU 954 C SER A 118 2074 356 190 1477 2072 -115 C ATOM 955 O SER A 118 -8.918 27.357 8.147 1.00 13.49 O ANISOU 955 O SER A 118 1826 205 289 1399 1899 -252 O ATOM 956 CB SER A 118 -8.374 30.096 6.616 1.00 17.01 C ANISOU 956 CB SER A 118 2404 407 195 1576 2481 119 C ATOM 957 OG SER A 118 -8.843 31.359 6.178 1.00 18.40 O ANISOU 957 OG SER A 118 2466 465 292 1893 2631 -169 O ATOM 958 N ATYR A 119 -8.305 27.022 5.976 0.62 12.67 N ANISOU 958 N ATYR A 119 1841 358 285 1251 1720 -218 N ATOM 959 N BTYR A 119 -8.382 26.951 5.987 0.38 15.00 N ANISOU 959 N BTYR A 119 2091 268 250 1598 2009 -198 N ATOM 960 CA ATYR A 119 -7.620 25.743 6.194 0.62 12.74 C ANISOU 960 CA ATYR A 119 1784 284 88 1212 1841 -58 C ATOM 961 CA BTYR A 119 -7.797 25.652 6.301 0.38 15.30 C ANISOU 961 CA BTYR A 119 2077 190 143 1650 2086 -110 C ATOM 962 C ATYR A 119 -6.531 25.859 7.253 0.62 12.76 C ANISOU 962 C ATYR A 119 1817 287 184 1212 1817 -51 C ATOM 963 C BTYR A 119 -6.589 25.820 7.227 0.38 14.57 C ANISOU 963 C BTYR A 119 1994 214 193 1536 2004 -110 C ATOM 964 O ATYR A 119 -5.785 26.837 7.297 0.62 11.49 O ANISOU 964 O ATYR A 119 1651 194 24 1134 1580 -56 O ATOM 965 O BTYR A 119 -5.832 26.788 7.132 0.38 14.18 O ANISOU 965 O BTYR A 119 1906 188 143 1523 1958 -124 O ATOM 966 CB ATYR A 119 -7.077 25.260 4.848 0.62 12.06 C ANISOU 966 CB ATYR A 119 1665 166 20 1226 1691 -113 C ATOM 967 CB BTYR A 119 -7.442 24.916 5.018 0.38 16.92 C ANISOU 967 CB BTYR A 119 2188 1 106 2061 2178 -212 C ATOM 968 CG ATYR A 119 -6.365 23.936 4.953 0.62 10.19 C ANISOU 968 CG ATYR A 119 1376 320 170 1081 1415 -96 C ATOM 969 CG BTYR A 119 -8.622 24.499 4.144 0.38 18.46 C ANISOU 969 CG BTYR A 119 2292 -165 105 2369 2351 -152 C ATOM 970 CD1ATYR A 119 -7.073 22.770 5.205 0.62 9.27 C ANISOU 970 CD1ATYR A 119 1110 97 -227 721 1689 -87 C ATOM 971 CD1BTYR A 119 -8.761 25.004 2.866 0.38 21.49 C ANISOU 971 CD1BTYR A 119 2514 -366 100 2877 2773 -337 C ATOM 972 CD2ATYR A 119 -4.989 23.853 4.845 0.62 9.79 C ANISOU 972 CD2ATYR A 119 1357 67 95 1150 1212 32 C ATOM 973 CD2BTYR A 119 -9.565 23.575 4.581 0.38 18.39 C ANISOU 973 CD2BTYR A 119 2310 -441 124 2374 2301 -409 C ATOM 974 CE1ATYR A 119 -6.435 21.561 5.325 0.62 10.16 C ANISOU 974 CE1ATYR A 119 1126 217 -124 982 1751 -106 C ATOM 975 CE1BTYR A 119 -9.799 24.626 2.045 0.38 20.90 C ANISOU 975 CE1BTYR A 119 2357 -235 -45 3030 2554 -449 C ATOM 976 CE2ATYR A 119 -4.350 22.648 4.963 0.62 12.62 C ANISOU 976 CE2ATYR A 119 1505 312 -7 1652 1636 -343 C ATOM 977 CE2BTYR A 119 -10.597 23.180 3.764 0.38 18.76 C ANISOU 977 CE2BTYR A 119 2058 -139 32 2640 2428 -483 C ATOM 978 CZ ATYR A 119 -5.061 21.511 5.210 0.62 11.36 C ANISOU 978 CZ ATYR A 119 1359 154 24 1449 1509 -44 C ATOM 979 CZ BTYR A 119 -10.713 23.721 2.493 0.38 18.68 C ANISOU 979 CZ BTYR A 119 2262 -353 80 2481 2355 -253 C ATOM 980 OH ATYR A 119 -4.423 20.301 5.323 0.62 9.20 O ANISOU 980 OH ATYR A 119 921 202 -142 1295 1280 -401 O ATOM 981 OH BTYR A 119 -11.751 23.339 1.641 0.38 20.44 O ANISOU 981 OH BTYR A 119 2382 -442 90 2753 2630 -300 O ATOM 982 N TRP A 120 -6.420 24.863 8.134 1.00 13.33 N ANISOU 982 N TRP A 120 1879 244 174 1340 1844 -182 N ATOM 983 CA TRP A 120 -5.546 25.005 9.283 1.00 13.94 C ANISOU 983 CA TRP A 120 1907 191 148 1450 1940 -86 C ATOM 984 C TRP A 120 -4.092 25.342 8.970 1.00 13.37 C ANISOU 984 C TRP A 120 1870 199 153 1437 1773 7 C ATOM 985 O TRP A 120 -3.527 26.166 9.649 1.00 14.02 O ANISOU 985 O TRP A 120 1962 230 121 1533 1832 194 O ATOM 986 CB TRP A 120 -5.706 23.822 10.229 1.00 13.16 C ANISOU 986 CB TRP A 120 1704 109 295 1613 1680 -113 C ATOM 987 CG TRP A 120 -4.954 22.585 9.809 1.00 11.04 C ANISOU 987 CG TRP A 120 1617 71 243 1237 1340 -342 C ATOM 988 CD1 TRP A 120 -5.223 21.747 8.748 1.00 14.72 C ANISOU 988 CD1 TRP A 120 1995 155 173 1574 2024 33 C ATOM 989 CD2 TRP A 120 -3.796 22.047 10.461 1.00 12.87 C ANISOU 989 CD2 TRP A 120 1807 -57 313 1617 1466 -189 C ATOM 990 NE1 TRP A 120 -4.300 20.715 8.719 1.00 12.66 N ANISOU 990 NE1 TRP A 120 1844 186 140 1353 1610 -335 N ATOM 991 CE2 TRP A 120 -3.419 20.875 9.765 1.00 12.37 C ANISOU 991 CE2 TRP A 120 1635 -100 460 1387 1677 -375 C ATOM 992 CE3 TRP A 120 -3.050 22.431 11.587 1.00 11.54 C ANISOU 992 CE3 TRP A 120 1973 -187 254 1172 1238 -6 C ATOM 993 CZ2 TRP A 120 -2.330 20.115 10.146 1.00 13.13 C ANISOU 993 CZ2 TRP A 120 1883 0 278 1413 1689 -23 C ATOM 994 CZ3 TRP A 120 -1.982 21.655 11.980 1.00 11.72 C ANISOU 994 CZ3 TRP A 120 1733 180 258 1295 1422 -274 C ATOM 995 CH2 TRP A 120 -1.640 20.509 11.274 1.00 12.28 C ANISOU 995 CH2 TRP A 120 1754 37 208 1220 1690 -274 C ATOM 996 N THR A 121 -3.501 24.788 7.910 1.00 14.08 N ANISOU 996 N THR A 121 1948 153 220 1496 1905 118 N ATOM 997 CA THR A 121 -2.107 25.085 7.673 1.00 14.62 C ANISOU 997 CA THR A 121 1989 190 127 1643 1922 -37 C ATOM 998 C THR A 121 -1.901 26.447 7.051 1.00 14.54 C ANISOU 998 C THR A 121 1884 127 256 1655 1983 -7 C ATOM 999 O THR A 121 -0.779 26.867 6.913 1.00 14.68 O ANISOU 999 O THR A 121 1712 144 255 1776 2089 -56 O ATOM 1000 CB THR A 121 -1.388 23.994 6.861 1.00 14.05 C ANISOU 1000 CB THR A 121 1876 180 125 1695 1767 -161 C ATOM 1001 OG1 THR A 121 -1.810 24.050 5.493 1.00 17.04 O ANISOU 1001 OG1 THR A 121 2667 297 -92 1933 1872 -557 O ATOM 1002 CG2 THR A 121 -1.695 22.580 7.394 1.00 14.73 C ANISOU 1002 CG2 THR A 121 1995 39 -36 1651 1948 -248 C ATOM 1003 N SER A 122 -2.964 27.117 6.616 1.00 14.67 N ANISOU 1003 N SER A 122 2085 173 308 1626 1859 6 N ATOM 1004 CA SER A 122 -2.807 28.477 6.098 1.00 15.57 C ANISOU 1004 CA SER A 122 2167 213 265 1697 2051 -12 C ATOM 1005 C SER A 122 -2.739 29.535 7.183 1.00 15.21 C ANISOU 1005 C SER A 122 2181 228 334 1661 1935 49 C ATOM 1006 O SER A 122 -2.429 30.704 6.903 1.00 15.68 O ANISOU 1006 O SER A 122 2503 202 448 1530 1922 -61 O ATOM 1007 CB SER A 122 -3.947 28.811 5.167 1.00 17.08 C ANISOU 1007 CB SER A 122 2383 223 392 1891 2214 51 C ATOM 1008 OG SER A 122 -5.104 29.099 5.871 1.00 19.87 O ANISOU 1008 OG SER A 122 2453 164 383 2235 2858 129 O ATOM 1009 N HIS A 123 -3.058 29.164 8.415 1.00 14.62 N ANISOU 1009 N HIS A 123 2201 291 432 1471 1883 1 N ATOM 1010 CA HIS A 123 -3.120 30.161 9.488 1.00 14.19 C ANISOU 1010 CA HIS A 123 2015 138 249 1475 1899 19 C ATOM 1011 C HIS A 123 -1.697 30.574 9.794 1.00 15.05 C ANISOU 1011 C HIS A 123 2129 63 197 1527 2062 18 C ATOM 1012 O HIS A 123 -0.827 29.747 9.988 1.00 15.57 O ANISOU 1012 O HIS A 123 2036 22 192 1640 2239 80 O ATOM 1013 CB HIS A 123 -3.678 29.595 10.796 1.00 14.02 C ANISOU 1013 CB HIS A 123 2049 227 331 1479 1798 -5 C ATOM 1014 CG HIS A 123 -5.101 29.170 10.764 1.00 15.50 C ANISOU 1014 CG HIS A 123 2149 118 375 1586 2155 -37 C ATOM 1015 ND1 HIS A 123 -5.854 29.014 9.612 1.00 15.88 N ANISOU 1015 ND1 HIS A 123 1568 60 73 1756 2709 103 N ATOM 1016 CD2 HIS A 123 -5.910 28.832 11.792 1.00 11.80 C ANISOU 1016 CD2 HIS A 123 1680 157 219 1483 1317 249 C ATOM 1017 CE1 HIS A 123 -7.063 28.554 9.951 1.00 12.89 C ANISOU 1017 CE1 HIS A 123 1606 97 432 1427 1865 189 C ATOM 1018 NE2 HIS A 123 -7.108 28.430 11.262 1.00 17.60 N ANISOU 1018 NE2 HIS A 123 1892 191 174 1617 3176 240 N ATOM 1019 N GLY A 124 -1.466 31.879 9.889 1.00 15.62 N ANISOU 1019 N GLY A 124 2039 4 212 1505 2390 -65 N ATOM 1020 CA GLY A 124 -0.164 32.358 10.272 1.00 15.90 C ANISOU 1020 CA GLY A 124 1981 2 109 1741 2318 -55 C ATOM 1021 C GLY A 124 0.129 32.266 11.770 1.00 15.01 C ANISOU 1021 C GLY A 124 1803 -14 106 1778 2119 -93 C ATOM 1022 O GLY A 124 1.298 32.320 12.192 1.00 17.37 O ANISOU 1022 O GLY A 124 1840 -116 -53 2289 2468 61 O ATOM 1023 N ASP A 125 -0.898 32.075 12.587 1.00 15.28 N ANISOU 1023 N ASP A 125 1754 -15 48 1894 2155 -166 N ATOM 1024 CA ASP A 125 -0.687 31.863 14.025 1.00 15.65 C ANISOU 1024 CA ASP A 125 1988 92 101 1761 2197 -17 C ATOM 1025 C ASP A 125 -1.832 31.046 14.602 1.00 15.48 C ANISOU 1025 C ASP A 125 1863 149 27 1834 2184 -82 C ATOM 1026 O ASP A 125 -2.683 30.593 13.840 1.00 14.91 O ANISOU 1026 O ASP A 125 1736 219 -25 1728 2200 -80 O ATOM 1027 CB ASP A 125 -0.507 33.196 14.725 1.00 17.52 C ANISOU 1027 CB ASP A 125 2098 -111 139 2247 2310 -58 C ATOM 1028 CG ASP A 125 -1.673 34.087 14.582 1.00 19.89 C ANISOU 1028 CG ASP A 125 2762 23 75 1941 2852 271 C ATOM 1029 OD1 ASP A 125 -2.822 33.637 14.667 1.00 18.54 O ANISOU 1029 OD1 ASP A 125 2181 185 -38 1998 2864 83 O ATOM 1030 OD2 ASP A 125 -1.531 35.329 14.413 1.00 27.71 O ANISOU 1030 OD2 ASP A 125 3468 94 248 2182 4878 599 O ATOM 1031 N ALA A 126 -1.808 30.812 15.916 1.00 15.98 N ANISOU 1031 N ALA A 126 2000 180 -41 1969 2100 -1 N ATOM 1032 CA ALA A 126 -2.732 29.931 16.615 1.00 14.92 C ANISOU 1032 CA ALA A 126 1842 210 125 1765 2060 -69 C ATOM 1033 C ALA A 126 -3.863 30.689 17.299 1.00 15.44 C ANISOU 1033 C ALA A 126 2001 277 175 1836 2029 14 C ATOM 1034 O ALA A 126 -4.506 30.163 18.227 1.00 17.54 O ANISOU 1034 O ALA A 126 2265 603 155 2065 2333 -119 O ATOM 1035 CB ALA A 126 -2.007 29.080 17.637 1.00 16.63 C ANISOU 1035 CB ALA A 126 2233 112 149 2035 2050 95 C ATOM 1036 N ARG A 127 -4.189 31.892 16.798 1.00 15.34 N ANISOU 1036 N ARG A 127 2086 185 164 1675 2066 79 N ATOM 1037 CA ARG A 127 -5.206 32.692 17.482 1.00 15.10 C ANISOU 1037 CA ARG A 127 1943 106 92 1655 2138 72 C ATOM 1038 C ARG A 127 -6.543 31.998 17.635 1.00 15.59 C ANISOU 1038 C ARG A 127 1950 158 38 1786 2185 96 C ATOM 1039 O ARG A 127 -7.281 32.285 18.603 1.00 17.44 O ANISOU 1039 O ARG A 127 2440 51 -159 1921 2264 200 O ATOM 1040 CB ARG A 127 -5.399 34.048 16.811 1.00 16.49 C ANISOU 1040 CB ARG A 127 2124 159 -80 1741 2397 166 C ATOM 1041 CG ARG A 127 -6.069 34.019 15.440 1.00 15.38 C ANISOU 1041 CG ARG A 127 2010 -12 -33 1622 2210 -63 C ATOM 1042 CD ARG A 127 -6.186 35.392 14.754 1.00 15.62 C ANISOU 1042 CD ARG A 127 2052 -63 77 1632 2251 -112 C ATOM 1043 NE ARG A 127 -4.855 35.836 14.357 1.00 16.69 N ANISOU 1043 NE ARG A 127 2462 -269 298 1363 2514 362 N ATOM 1044 CZ ARG A 127 -4.603 36.966 13.771 1.00 18.97 C ANISOU 1044 CZ ARG A 127 2464 -158 -320 1945 2798 314 C ATOM 1045 NH1 ARG A 127 -5.590 37.777 13.470 1.00 19.55 N ANISOU 1045 NH1 ARG A 127 2745 -210 -299 2272 2411 293 N ATOM 1046 NH2 ARG A 127 -3.364 37.265 13.429 1.00 23.46 N ANISOU 1046 NH2 ARG A 127 3236 -572 -34 2070 3604 690 N ATOM 1047 N ASP A 128 -6.882 31.143 16.700 1.00 14.65 N ANISOU 1047 N ASP A 128 1868 106 35 1425 2272 107 N ATOM 1048 CA ASP A 128 -8.205 30.486 16.663 1.00 14.57 C ANISOU 1048 CA ASP A 128 1844 78 102 1509 2183 66 C ATOM 1049 C ASP A 128 -8.222 29.047 17.191 1.00 15.44 C ANISOU 1049 C ASP A 128 1843 29 90 1677 2346 34 C ATOM 1050 O ASP A 128 -9.301 28.440 17.224 1.00 17.52 O ANISOU 1050 O ASP A 128 2177 -151 191 1698 2779 75 O ATOM 1051 CB ASP A 128 -8.753 30.506 15.219 1.00 14.81 C ANISOU 1051 CB ASP A 128 1760 131 203 1437 2428 5 C ATOM 1052 CG ASP A 128 -10.211 30.245 15.145 1.00 16.35 C ANISOU 1052 CG ASP A 128 1934 -43 -148 1637 2641 -12 C ATOM 1053 OD1 ASP A 128 -10.986 30.855 15.928 1.00 16.50 O ANISOU 1053 OD1 ASP A 128 1939 64 -88 1936 2392 273 O ATOM 1054 OD2 ASP A 128 -10.670 29.458 14.263 1.00 18.62 O ANISOU 1054 OD2 ASP A 128 1899 -502 173 2129 3045 -102 O ATOM 1055 N TRP A 129 -7.060 28.532 17.613 1.00 13.74 N ANISOU 1055 N TRP A 129 1814 131 76 1390 2016 -116 N ATOM 1056 CA TRP A 129 -6.833 27.095 17.768 1.00 12.81 C ANISOU 1056 CA TRP A 129 1772 104 142 1376 1716 -16 C ATOM 1057 C TRP A 129 -6.704 26.701 19.215 1.00 13.31 C ANISOU 1057 C TRP A 129 1894 77 69 1546 1616 0 C ATOM 1058 O TRP A 129 -6.077 27.393 19.994 1.00 13.73 O ANISOU 1058 O TRP A 129 1965 112 -38 1750 1500 210 O ATOM 1059 CB TRP A 129 -5.569 26.681 17.033 1.00 12.49 C ANISOU 1059 CB TRP A 129 1726 128 182 1448 1568 -243 C ATOM 1060 CG TRP A 129 -4.996 25.335 17.370 1.00 13.16 C ANISOU 1060 CG TRP A 129 1679 139 112 1483 1836 -93 C ATOM 1061 CD1 TRP A 129 -5.310 24.157 16.787 1.00 11.19 C ANISOU 1061 CD1 TRP A 129 1636 206 65 1562 1052 -272 C ATOM 1062 CD2 TRP A 129 -3.935 25.045 18.296 1.00 12.88 C ANISOU 1062 CD2 TRP A 129 1471 138 -191 1536 1887 -76 C ATOM 1063 NE1 TRP A 129 -4.574 23.131 17.318 1.00 11.62 N ANISOU 1063 NE1 TRP A 129 1570 5 14 1534 1308 -28 N ATOM 1064 CE2 TRP A 129 -3.714 23.649 18.248 1.00 11.15 C ANISOU 1064 CE2 TRP A 129 1374 28 -71 1133 1726 -69 C ATOM 1065 CE3 TRP A 129 -3.186 25.802 19.189 1.00 12.44 C ANISOU 1065 CE3 TRP A 129 1565 126 198 1510 1651 20 C ATOM 1066 CZ2 TRP A 129 -2.756 23.032 18.994 1.00 12.01 C ANISOU 1066 CZ2 TRP A 129 1306 56 56 1601 1655 -48 C ATOM 1067 CZ3 TRP A 129 -2.237 25.188 19.931 1.00 13.14 C ANISOU 1067 CZ3 TRP A 129 1600 161 -42 1644 1747 -261 C ATOM 1068 CH2 TRP A 129 -2.031 23.805 19.837 1.00 12.77 C ANISOU 1068 CH2 TRP A 129 1614 163 15 1564 1673 -150 C ATOM 1069 N ASP A 130 -7.241 25.538 19.546 1.00 13.37 N ANISOU 1069 N ASP A 130 1925 86 88 1547 1606 -31 N ATOM 1070 CA ASP A 130 -6.888 24.831 20.825 1.00 12.64 C ANISOU 1070 CA ASP A 130 1733 207 111 1446 1624 -82 C ATOM 1071 C ASP A 130 -6.838 23.339 20.448 1.00 12.73 C ANISOU 1071 C ASP A 130 1716 207 -8 1515 1605 -93 C ATOM 1072 O ASP A 130 -7.260 22.925 19.377 1.00 11.53 O ANISOU 1072 O ASP A 130 1687 75 -30 1327 1367 -27 O ATOM 1073 CB ASP A 130 -7.987 25.090 21.874 1.00 12.61 C ANISOU 1073 CB ASP A 130 1880 322 109 1431 1478 -154 C ATOM 1074 CG ASP A 130 -7.537 24.947 23.303 1.00 14.77 C ANISOU 1074 CG ASP A 130 2161 154 51 1633 1815 109 C ATOM 1075 OD1 ASP A 130 -6.443 24.392 23.556 1.00 14.90 O ANISOU 1075 OD1 ASP A 130 2050 272 -75 1756 1855 167 O ATOM 1076 OD2 ASP A 130 -8.257 25.379 24.239 1.00 18.50 O ANISOU 1076 OD2 ASP A 130 2726 524 -332 2335 1967 9 O ATOM 1077 N ILE A 131 -6.366 22.552 21.385 1.00 11.82 N ANISOU 1077 N ILE A 131 1430 97 62 1427 1631 -132 N ATOM 1078 CA ILE A 131 -6.219 21.096 21.227 1.00 12.18 C ANISOU 1078 CA ILE A 131 1515 232 -31 1607 1505 27 C ATOM 1079 C ILE A 131 -6.772 20.486 22.504 1.00 11.87 C ANISOU 1079 C ILE A 131 1488 221 36 1599 1424 -20 C ATOM 1080 O ILE A 131 -6.337 20.816 23.606 1.00 13.23 O ANISOU 1080 O ILE A 131 1679 70 70 1732 1613 164 O ATOM 1081 CB ILE A 131 -4.739 20.760 20.928 1.00 12.64 C ANISOU 1081 CB ILE A 131 1481 206 -50 1746 1575 -52 C ATOM 1082 CG1 ILE A 131 -4.539 19.274 20.636 1.00 13.82 C ANISOU 1082 CG1 ILE A 131 1737 92 -146 1746 1767 109 C ATOM 1083 CG2 ILE A 131 -3.786 21.229 22.055 1.00 12.71 C ANISOU 1083 CG2 ILE A 131 1623 186 -69 1900 1306 -111 C ATOM 1084 CD1 ILE A 131 -5.149 18.781 19.371 1.00 12.20 C ANISOU 1084 CD1 ILE A 131 1698 0 -30 1312 1625 76 C ATOM 1085 N LEU A 132 -7.765 19.633 22.363 1.00 12.02 N ANISOU 1085 N LEU A 132 1666 34 -60 1704 1194 52 N ATOM 1086 CA LEU A 132 -8.540 19.152 23.470 1.00 12.92 C ANISOU 1086 CA LEU A 132 1710 111 -102 1834 1365 -7 C ATOM 1087 C LEU A 132 -8.540 17.616 23.557 1.00 13.52 C ANISOU 1087 C LEU A 132 1823 31 -119 1896 1417 74 C ATOM 1088 O LEU A 132 -8.549 16.929 22.535 1.00 12.37 O ANISOU 1088 O LEU A 132 1743 -160 -131 1741 1214 -10 O ATOM 1089 CB LEU A 132 -10.000 19.606 23.297 1.00 13.66 C ANISOU 1089 CB LEU A 132 1624 123 -243 1850 1713 262 C ATOM 1090 CG LEU A 132 -10.260 21.090 23.039 1.00 14.30 C ANISOU 1090 CG LEU A 132 1752 207 72 1979 1700 -174 C ATOM 1091 CD1 LEU A 132 -11.773 21.293 22.892 1.00 16.32 C ANISOU 1091 CD1 LEU A 132 2302 312 203 2193 1703 451 C ATOM 1092 CD2 LEU A 132 -9.689 21.929 24.139 1.00 17.80 C ANISOU 1092 CD2 LEU A 132 2141 286 -362 2217 2403 -90 C ATOM 1093 N LEU A 133 -8.598 17.127 24.792 1.00 13.29 N ANISOU 1093 N LEU A 133 1706 109 -83 2010 1332 95 N ATOM 1094 CA LEU A 133 -8.720 15.733 25.102 1.00 13.27 C ANISOU 1094 CA LEU A 133 1615 -30 -20 2100 1325 -9 C ATOM 1095 C LEU A 133 -10.000 15.524 25.869 1.00 13.16 C ANISOU 1095 C LEU A 133 1656 -76 36 2140 1204 45 C ATOM 1096 O LEU A 133 -10.198 16.144 26.878 1.00 13.39 O ANISOU 1096 O LEU A 133 1767 -409 109 2241 1080 83 O ATOM 1097 CB LEU A 133 -7.568 15.246 25.983 1.00 13.71 C ANISOU 1097 CB LEU A 133 1582 18 -125 2205 1420 80 C ATOM 1098 CG LEU A 133 -7.536 13.755 26.196 1.00 13.06 C ANISOU 1098 CG LEU A 133 1555 47 0 2145 1260 18 C ATOM 1099 CD1 LEU A 133 -7.134 13.002 24.943 1.00 16.91 C ANISOU 1099 CD1 LEU A 133 2292 205 -273 2069 2063 -117 C ATOM 1100 CD2 LEU A 133 -6.590 13.457 27.335 1.00 14.71 C ANISOU 1100 CD2 LEU A 133 1658 132 88 2176 1752 -171 C ATOM 1101 N ALA A 134 -10.860 14.642 25.365 1.00 13.03 N ANISOU 1101 N ALA A 134 1645 -262 -48 2113 1192 126 N ATOM 1102 CA ALA A 134 -12.056 14.197 26.091 1.00 14.58 C ANISOU 1102 CA ALA A 134 1758 -242 -43 2339 1441 103 C ATOM 1103 C ALA A 134 -11.967 12.714 26.357 1.00 14.92 C ANISOU 1103 C ALA A 134 1753 -183 -33 2347 1569 198 C ATOM 1104 O ALA A 134 -11.545 11.950 25.489 1.00 14.09 O ANISOU 1104 O ALA A 134 1664 -239 -333 2127 1562 228 O ATOM 1105 CB ALA A 134 -13.328 14.486 25.314 1.00 14.57 C ANISOU 1105 CB ALA A 134 1639 -159 65 2262 1634 165 C ATOM 1106 N VAL A 135 -12.463 12.286 27.521 1.00 16.56 N ANISOU 1106 N VAL A 135 2028 -218 -126 2580 1684 375 N ATOM 1107 CA VAL A 135 -12.432 10.873 27.884 1.00 16.37 C ANISOU 1107 CA VAL A 135 1934 -267 -42 2614 1669 353 C ATOM 1108 C VAL A 135 -13.868 10.372 28.078 1.00 15.74 C ANISOU 1108 C VAL A 135 1804 -376 12 2636 1539 402 C ATOM 1109 O VAL A 135 -14.671 10.978 28.820 1.00 16.10 O ANISOU 1109 O VAL A 135 1969 -447 14 2644 1502 363 O ATOM 1110 CB VAL A 135 -11.628 10.636 29.166 1.00 17.38 C ANISOU 1110 CB VAL A 135 2070 -158 -75 2629 1902 252 C ATOM 1111 CG1 VAL A 135 -11.626 9.142 29.575 1.00 19.05 C ANISOU 1111 CG1 VAL A 135 2498 -175 74 2817 1923 350 C ATOM 1112 CG2 VAL A 135 -10.187 11.149 28.993 1.00 16.40 C ANISOU 1112 CG2 VAL A 135 2021 -212 -109 2632 1577 88 C ATOM 1113 N GLY A 136 -14.181 9.283 27.383 1.00 15.73 N ANISOU 1113 N GLY A 136 1837 -477 191 2698 1441 487 N ATOM 1114 CA GLY A 136 -15.453 8.579 27.541 1.00 17.16 C ANISOU 1114 CA GLY A 136 1889 -370 250 2970 1662 414 C ATOM 1115 C GLY A 136 -15.244 7.273 28.273 1.00 19.14 C ANISOU 1115 C GLY A 136 2056 -343 405 3288 1927 480 C ATOM 1116 O GLY A 136 -14.273 6.532 28.042 1.00 19.50 O ANISOU 1116 O GLY A 136 2087 -329 627 3366 1956 593 O ATOM 1117 N GLU A 137 -16.148 6.980 29.204 1.00 19.47 N ANISOU 1117 N GLU A 137 2130 -399 543 3407 1860 365 N ATOM 1118 CA GLU A 137 -16.032 5.777 29.987 1.00 21.13 C ANISOU 1118 CA GLU A 137 2417 -314 511 3453 2156 278 C ATOM 1119 C GLU A 137 -17.223 4.909 29.645 1.00 20.38 C ANISOU 1119 C GLU A 137 2282 -346 745 3375 2087 191 C ATOM 1120 O GLU A 137 -18.385 5.361 29.700 1.00 19.44 O ANISOU 1120 O GLU A 137 2002 -230 754 3444 1938 237 O ATOM 1121 CB GLU A 137 -15.992 6.102 31.472 1.00 22.35 C ANISOU 1121 CB GLU A 137 2653 -406 633 3568 2271 279 C ATOM 1122 CG GLU A 137 -15.848 4.841 32.307 1.00 23.15 C ANISOU 1122 CG GLU A 137 2736 -305 662 3707 2350 229 C ATOM 1123 CD GLU A 137 -15.546 5.153 33.775 1.00 27.13 C ANISOU 1123 CD GLU A 137 3622 -183 540 4010 2676 228 C ATOM 1124 OE1 GLU A 137 -15.470 6.331 34.153 1.00 35.60 O ANISOU 1124 OE1 GLU A 137 4959 6 15 5263 3302 -202 O ATOM 1125 OE2 GLU A 137 -15.375 4.217 34.548 1.00 36.69 O ANISOU 1125 OE2 GLU A 137 5178 33 643 5344 3415 115 O ATOM 1126 N VAL A 138 -16.935 3.690 29.261 1.00 21.02 N ANISOU 1126 N VAL A 138 2205 -277 723 3550 2229 253 N ATOM 1127 CA VAL A 138 -17.950 2.748 28.833 1.00 23.06 C ANISOU 1127 CA VAL A 138 2519 -279 725 3561 2682 167 C ATOM 1128 C VAL A 138 -18.294 1.814 29.982 1.00 24.46 C ANISOU 1128 C VAL A 138 2602 -387 930 3722 2967 144 C ATOM 1129 O VAL A 138 -17.399 1.141 30.553 1.00 25.33 O ANISOU 1129 O VAL A 138 2518 -369 1456 3752 3355 170 O ATOM 1130 CB VAL A 138 -17.459 1.922 27.682 1.00 22.91 C ANISOU 1130 CB VAL A 138 2498 -342 711 3583 2620 171 C ATOM 1131 CG1 VAL A 138 -18.510 0.959 27.298 1.00 26.59 C ANISOU 1131 CG1 VAL A 138 3039 -307 467 3907 3156 308 C ATOM 1132 CG2 VAL A 138 -17.103 2.834 26.514 1.00 24.13 C ANISOU 1132 CG2 VAL A 138 2907 -12 536 3445 2816 192 C ATOM 1133 N THR A 139 -19.577 1.770 30.332 1.00 25.75 N ANISOU 1133 N THR A 139 2890 -455 947 3904 2990 168 N ATOM 1134 CA THR A 139 -20.077 0.869 31.374 1.00 28.75 C ANISOU 1134 CA THR A 139 3321 -533 794 4125 3475 179 C ATOM 1135 C THR A 139 -21.080 -0.103 30.747 1.00 29.59 C ANISOU 1135 C THR A 139 3363 -669 824 4154 3723 219 C ATOM 1136 O THR A 139 -21.941 0.328 30.002 1.00 28.30 O ANISOU 1136 O THR A 139 3047 -811 901 4094 3611 94 O ATOM 1137 CB THR A 139 -20.763 1.713 32.419 1.00 27.57 C ANISOU 1137 CB THR A 139 3299 -810 892 4060 3114 316 C ATOM 1138 OG1 THR A 139 -19.780 2.533 33.070 1.00 31.67 O ANISOU 1138 OG1 THR A 139 4134 -377 1018 4822 3076 122 O ATOM 1139 CG2 THR A 139 -21.383 0.811 33.504 1.00 29.23 C ANISOU 1139 CG2 THR A 139 3488 -496 861 4360 3258 191 C ATOM 1140 N LYS A 140 -20.953 -1.398 31.043 1.00 33.14 N ANISOU 1140 N LYS A 140 3832 -555 705 4516 4241 68 N ATOM 1141 CA LYS A 140 -21.910 -2.410 30.582 1.00 34.53 C ANISOU 1141 CA LYS A 140 4082 -569 692 4635 4401 194 C ATOM 1142 C LYS A 140 -22.831 -2.791 31.721 1.00 36.92 C ANISOU 1142 C LYS A 140 4327 -638 669 5020 4678 171 C ATOM 1143 O LYS A 140 -22.463 -2.699 32.890 1.00 35.20 O ANISOU 1143 O LYS A 140 4028 -954 1039 4806 4540 248 O ATOM 1144 CB LYS A 140 -21.184 -3.664 30.091 1.00 35.15 C ANISOU 1144 CB LYS A 140 4224 -585 660 4712 4419 130 C ATOM 1145 CG LYS A 140 -20.366 -3.484 28.840 1.00 35.27 C ANISOU 1145 CG LYS A 140 4313 -350 687 4639 4446 234 C ATOM 1146 CD LYS A 140 -19.735 -4.781 28.364 1.00 36.37 C ANISOU 1146 CD LYS A 140 4402 -438 589 4761 4653 224 C ATOM 1147 CE LYS A 140 -18.410 -5.031 29.066 1.00 36.35 C ANISOU 1147 CE LYS A 140 4606 -226 739 4746 4456 342 C ATOM 1148 NZ LYS A 140 -17.731 -6.250 28.541 1.00 35.69 N ANISOU 1148 NZ LYS A 140 4835 -518 1036 4294 4428 666 N ATOM 1149 N SER A 141 -24.048 -3.180 31.345 1.00 38.84 N ANISOU 1149 N SER A 141 4518 -751 678 5273 4964 279 N ATOM 1150 CA SER A 141 -25.086 -3.604 32.310 1.00 41.71 C ANISOU 1150 CA SER A 141 4952 -569 520 5603 5289 256 C ATOM 1151 C SER A 141 -26.083 -4.532 31.642 1.00 42.92 C ANISOU 1151 C SER A 141 5039 -686 469 5772 5496 302 C ATOM 1152 O SER A 141 -25.791 -5.091 30.575 1.00 41.70 O ANISOU 1152 O SER A 141 4783 -936 579 5641 5418 383 O ATOM 1153 CB SER A 141 -25.804 -2.400 32.895 1.00 41.38 C ANISOU 1153 CB SER A 141 4831 -562 580 5644 5245 340 C ATOM 1154 OG SER A 141 -27.047 -2.823 33.445 1.00 46.12 O ANISOU 1154 OG SER A 141 5345 -475 739 6229 5950 123 O ATOM 1155 N THR A 142 -27.241 -4.747 32.279 1.00 46.41 N ANISOU 1155 N THR A 142 5649 -507 317 6150 5834 260 N ATOM 1156 CA THR A 142 -28.252 -5.685 31.716 1.00 47.97 C ANISOU 1156 CA THR A 142 5873 -436 282 6289 6062 257 C ATOM 1157 C THR A 142 -29.736 -5.338 31.971 1.00 49.72 C ANISOU 1157 C THR A 142 6113 -367 263 6482 6295 268 C ATOM 1158 O THR A 142 -30.502 -6.237 32.381 1.00 51.43 O ANISOU 1158 O THR A 142 6390 -438 261 6692 6460 290 O ATOM 1159 CB THR A 142 -28.022 -7.182 32.184 1.00 48.76 C ANISOU 1159 CB THR A 142 6079 -385 269 6324 6121 216 C ATOM 1160 OG1 THR A 142 -28.231 -7.294 33.600 1.00 50.97 O ANISOU 1160 OG1 THR A 142 6405 -610 224 6708 6251 382 O ATOM 1161 CG2 THR A 142 -26.583 -7.686 31.968 1.00 48.69 C ANISOU 1161 CG2 THR A 142 5999 -376 161 6377 6124 255 C ATOM 1162 N ALA A 143 -30.149 -4.093 31.707 1.00 49.81 N ANISOU 1162 N ALA A 143 6159 -295 268 6408 6356 276 N ATOM 1163 CA ALA A 143 -31.587 -3.697 31.723 1.00 49.74 C ANISOU 1163 CA ALA A 143 6187 -306 210 6438 6272 272 C ATOM 1164 C ALA A 143 -32.560 -4.630 30.956 1.00 49.93 C ANISOU 1164 C ALA A 143 6166 -344 192 6519 6285 298 C ATOM 1165 O ALA A 143 -32.332 -4.961 29.794 1.00 49.62 O ANISOU 1165 O ALA A 143 6164 -373 307 6553 6135 322 O ATOM 1166 CB ALA A 143 -31.737 -2.284 31.178 1.00 49.91 C ANISOU 1166 CB ALA A 143 6240 -255 187 6407 6316 256 C ATOM 1167 N GLY A 144 -33.651 -5.046 31.610 1.00 50.24 N ANISOU 1167 N GLY A 144 6199 -347 150 6592 6298 310 N ATOM 1168 CA GLY A 144 -34.681 -5.879 30.948 1.00 49.50 C ANISOU 1168 CA GLY A 144 6106 -339 187 6453 6247 367 C ATOM 1169 C GLY A 144 -34.181 -7.258 30.566 1.00 49.12 C ANISOU 1169 C GLY A 144 6050 -363 207 6423 6190 431 C ATOM 1170 O GLY A 144 -34.695 -7.879 29.634 1.00 48.62 O ANISOU 1170 O GLY A 144 5925 -521 287 6443 6103 561 O ATOM 1171 N GLY A 145 -33.166 -7.725 31.290 1.00 48.98 N ANISOU 1171 N GLY A 145 6025 -303 219 6364 6220 418 N ATOM 1172 CA GLY A 145 -32.537 -9.016 31.025 1.00 48.82 C ANISOU 1172 CA GLY A 145 6002 -258 152 6318 6228 366 C ATOM 1173 C GLY A 145 -31.617 -9.031 29.813 1.00 48.96 C ANISOU 1173 C GLY A 145 5993 -228 131 6288 6321 330 C ATOM 1174 O GLY A 145 -31.135 -10.105 29.418 1.00 50.21 O ANISOU 1174 O GLY A 145 6092 -215 84 6466 6518 385 O ATOM 1175 N LYS A 146 -31.361 -7.858 29.226 1.00 47.85 N ANISOU 1175 N LYS A 146 5787 -296 128 6167 6223 272 N ATOM 1176 CA LYS A 146 -30.565 -7.770 27.988 1.00 46.93 C ANISOU 1176 CA LYS A 146 5689 -326 114 6038 6101 174 C ATOM 1177 C LYS A 146 -29.329 -6.948 28.291 1.00 45.05 C ANISOU 1177 C LYS A 146 5390 -442 150 5788 5939 243 C ATOM 1178 O LYS A 146 -29.406 -6.037 29.143 1.00 44.34 O ANISOU 1178 O LYS A 146 5239 -670 180 5735 5871 292 O ATOM 1179 CB LYS A 146 -31.375 -7.147 26.847 1.00 47.29 C ANISOU 1179 CB LYS A 146 5756 -313 106 6045 6164 115 C ATOM 1180 CG LYS A 146 -32.042 -5.807 27.171 1.00 50.19 C ANISOU 1180 CG LYS A 146 6053 -263 25 6539 6477 -39 C ATOM 1181 CD LYS A 146 -33.367 -5.529 26.381 1.00 50.37 C ANISOU 1181 CD LYS A 146 6132 -218 83 6561 6443 -31 C ATOM 1182 CE LYS A 146 -33.166 -5.488 24.859 1.00 53.00 C ANISOU 1182 CE LYS A 146 6442 -140 107 6983 6711 -159 C ATOM 1183 NZ LYS A 146 -34.476 -5.477 24.096 1.00 54.56 N ANISOU 1183 NZ LYS A 146 6617 -172 141 7077 7036 -234 N ATOM 1184 N ILE A 147 -28.213 -7.265 27.620 1.00 42.92 N ANISOU 1184 N ILE A 147 5077 -397 167 5520 5710 199 N ATOM 1185 CA ILE A 147 -26.966 -6.480 27.780 1.00 41.67 C ANISOU 1185 CA ILE A 147 4899 -416 219 5420 5513 247 C ATOM 1186 C ILE A 147 -27.136 -5.074 27.249 1.00 36.91 C ANISOU 1186 C ILE A 147 4153 -543 348 4967 4902 331 C ATOM 1187 O ILE A 147 -27.635 -4.868 26.150 1.00 35.13 O ANISOU 1187 O ILE A 147 3681 -861 429 4892 4774 750 O ATOM 1188 CB ILE A 147 -25.742 -7.103 27.073 1.00 42.05 C ANISOU 1188 CB ILE A 147 4967 -400 235 5376 5632 186 C ATOM 1189 CG1 ILE A 147 -25.469 -8.525 27.579 1.00 45.59 C ANISOU 1189 CG1 ILE A 147 5586 -328 186 5892 5843 71 C ATOM 1190 CG2 ILE A 147 -24.502 -6.216 27.298 1.00 43.32 C ANISOU 1190 CG2 ILE A 147 5116 -348 259 5577 5763 169 C ATOM 1191 CD1 ILE A 147 -25.224 -8.652 29.111 1.00 47.61 C ANISOU 1191 CD1 ILE A 147 5860 -320 12 6195 6034 71 C ATOM 1192 N THR A 148 -26.730 -4.105 28.045 1.00 32.87 N ANISOU 1192 N THR A 148 3595 -593 417 4532 4362 348 N ATOM 1193 CA THR A 148 -26.729 -2.738 27.596 1.00 31.34 C ANISOU 1193 CA THR A 148 3357 -533 372 4390 4160 201 C ATOM 1194 C THR A 148 -25.411 -2.084 27.909 1.00 29.35 C ANISOU 1194 C THR A 148 3125 -556 613 4177 3849 267 C ATOM 1195 O THR A 148 -24.591 -2.596 28.661 1.00 29.14 O ANISOU 1195 O THR A 148 3265 -827 941 3928 3876 321 O ATOM 1196 CB THR A 148 -27.842 -1.972 28.321 1.00 31.94 C ANISOU 1196 CB THR A 148 3375 -575 324 4512 4248 138 C ATOM 1197 OG1 THR A 148 -27.576 -1.974 29.731 1.00 34.96 O ANISOU 1197 OG1 THR A 148 3593 -469 256 4996 4693 311 O ATOM 1198 CG2 THR A 148 -29.164 -2.686 28.194 1.00 30.95 C ANISOU 1198 CG2 THR A 148 2902 -613 129 4468 4387 -38 C ATOM 1199 N ALA A 149 -25.195 -0.938 27.294 1.00 27.05 N ANISOU 1199 N ALA A 149 2917 -486 506 3880 3479 223 N ATOM 1200 CA ALA A 149 -24.039 -0.117 27.626 1.00 25.19 C ANISOU 1200 CA ALA A 149 2645 -449 509 3836 3087 239 C ATOM 1201 C ALA A 149 -24.408 1.339 27.718 1.00 24.18 C ANISOU 1201 C ALA A 149 2503 -465 469 3816 2867 233 C ATOM 1202 O ALA A 149 -25.408 1.776 27.170 1.00 22.51 O ANISOU 1202 O ALA A 149 2170 -427 656 3902 2479 -23 O ATOM 1203 CB ALA A 149 -22.898 -0.327 26.616 1.00 24.78 C ANISOU 1203 CB ALA A 149 2694 -396 447 3801 2919 309 C ATOM 1204 N SER A 150 -23.582 2.092 28.430 1.00 23.21 N ANISOU 1204 N SER A 150 2357 -504 423 3797 2664 49 N ATOM 1205 CA SER A 150 -23.628 3.535 28.336 1.00 23.36 C ANISOU 1205 CA SER A 150 2298 -509 336 3847 2730 105 C ATOM 1206 C SER A 150 -22.206 4.103 28.300 1.00 21.56 C ANISOU 1206 C SER A 150 2022 -525 453 3627 2542 105 C ATOM 1207 O SER A 150 -21.263 3.446 28.740 1.00 22.02 O ANISOU 1207 O SER A 150 2143 -651 600 3769 2453 157 O ATOM 1208 CB SER A 150 -24.402 4.145 29.485 1.00 25.13 C ANISOU 1208 CB SER A 150 2641 -551 281 4005 2901 42 C ATOM 1209 OG SER A 150 -23.733 3.874 30.687 1.00 29.65 O ANISOU 1209 OG SER A 150 3261 -496 350 4757 3246 323 O ATOM 1210 N ILE A 151 -22.113 5.300 27.757 1.00 19.73 N ANISOU 1210 N ILE A 151 1980 -356 408 3423 2093 -14 N ATOM 1211 CA ILE A 151 -20.882 6.001 27.643 1.00 18.87 C ANISOU 1211 CA ILE A 151 1909 -356 365 3258 2002 165 C ATOM 1212 C ILE A 151 -21.065 7.374 28.205 1.00 20.32 C ANISOU 1212 C ILE A 151 2036 -316 338 3434 2248 222 C ATOM 1213 O ILE A 151 -21.896 8.151 27.732 1.00 21.68 O ANISOU 1213 O ILE A 151 2007 -170 284 3712 2516 291 O ATOM 1214 CB ILE A 151 -20.318 6.070 26.180 1.00 19.32 C ANISOU 1214 CB ILE A 151 2003 -375 270 3215 2120 95 C ATOM 1215 CG1 ILE A 151 -20.297 4.695 25.531 1.00 20.13 C ANISOU 1215 CG1 ILE A 151 1940 -373 256 3559 2148 63 C ATOM 1216 CG2 ILE A 151 -18.936 6.645 26.252 1.00 18.60 C ANISOU 1216 CG2 ILE A 151 1851 -295 437 3142 2072 34 C ATOM 1217 CD1 ILE A 151 -19.659 4.657 24.199 1.00 19.18 C ANISOU 1217 CD1 ILE A 151 1914 -449 -126 3372 2002 271 C ATOM 1218 N LYS A 152 -20.282 7.677 29.229 1.00 21.49 N ANISOU 1218 N LYS A 152 2254 -239 320 3499 2410 291 N ATOM 1219 CA LYS A 152 -20.327 8.963 29.844 1.00 21.69 C ANISOU 1219 CA LYS A 152 2329 -297 166 3426 2486 282 C ATOM 1220 C LYS A 152 -19.081 9.703 29.407 1.00 20.04 C ANISOU 1220 C LYS A 152 2039 -219 144 3336 2237 462 C ATOM 1221 O LYS A 152 -17.935 9.205 29.613 1.00 19.64 O ANISOU 1221 O LYS A 152 1864 -527 49 3530 2066 375 O ATOM 1222 CB LYS A 152 -20.279 8.778 31.368 1.00 23.19 C ANISOU 1222 CB LYS A 152 2709 -233 58 3577 2521 301 C ATOM 1223 CG LYS A 152 -20.394 10.016 32.227 1.00 28.66 C ANISOU 1223 CG LYS A 152 3423 -89 362 3931 3535 128 C ATOM 1224 CD LYS A 152 -21.360 11.035 31.661 1.00 35.76 C ANISOU 1224 CD LYS A 152 4490 218 37 4409 4686 -62 C ATOM 1225 CE LYS A 152 -21.540 12.256 32.593 1.00 38.45 C ANISOU 1225 CE LYS A 152 5028 112 179 4739 4841 -113 C ATOM 1226 NZ LYS A 152 -21.851 13.473 31.767 1.00 41.85 N ANISOU 1226 NZ LYS A 152 5669 435 435 4768 5460 -158 N ATOM 1227 N TRP A 153 -19.296 10.854 28.810 1.00 19.52 N ANISOU 1227 N TRP A 153 1963 -133 -93 3237 2215 505 N ATOM 1228 CA TRP A 153 -18.218 11.702 28.320 1.00 19.86 C ANISOU 1228 CA TRP A 153 2094 -152 -13 3197 2255 353 C ATOM 1229 C TRP A 153 -17.866 12.824 29.295 1.00 20.63 C ANISOU 1229 C TRP A 153 2241 -59 -165 3368 2229 460 C ATOM 1230 O TRP A 153 -18.722 13.581 29.724 1.00 22.17 O ANISOU 1230 O TRP A 153 2495 -104 -480 3598 2331 336 O ATOM 1231 CB TRP A 153 -18.555 12.267 26.953 1.00 19.22 C ANISOU 1231 CB TRP A 153 2114 -29 4 3023 2164 391 C ATOM 1232 CG TRP A 153 -18.616 11.218 25.930 1.00 18.07 C ANISOU 1232 CG TRP A 153 2164 -105 47 2669 2032 277 C ATOM 1233 CD1 TRP A 153 -19.705 10.536 25.520 1.00 17.01 C ANISOU 1233 CD1 TRP A 153 2085 -20 192 2481 1897 485 C ATOM 1234 CD2 TRP A 153 -17.514 10.718 25.174 1.00 17.03 C ANISOU 1234 CD2 TRP A 153 2034 -83 162 2676 1760 251 C ATOM 1235 NE1 TRP A 153 -19.357 9.627 24.549 1.00 16.98 N ANISOU 1235 NE1 TRP A 153 2300 -107 235 2442 1710 319 N ATOM 1236 CE2 TRP A 153 -18.002 9.697 24.337 1.00 16.28 C ANISOU 1236 CE2 TRP A 153 2056 42 446 2419 1710 463 C ATOM 1237 CE3 TRP A 153 -16.146 11.008 25.150 1.00 15.97 C ANISOU 1237 CE3 TRP A 153 1914 -132 306 2664 1490 240 C ATOM 1238 CZ2 TRP A 153 -17.170 8.978 23.446 1.00 16.79 C ANISOU 1238 CZ2 TRP A 153 2163 -58 233 2462 1753 279 C ATOM 1239 CZ3 TRP A 153 -15.321 10.286 24.263 1.00 16.16 C ANISOU 1239 CZ3 TRP A 153 1853 23 101 2604 1682 348 C ATOM 1240 CH2 TRP A 153 -15.850 9.297 23.429 1.00 16.76 C ANISOU 1240 CH2 TRP A 153 2239 89 315 2500 1626 399 C ATOM 1241 N GLY A 154 -16.578 12.932 29.620 1.00 20.33 N ANISOU 1241 N GLY A 154 2323 -95 -213 3350 2049 493 N ATOM 1242 CA GLY A 154 -16.077 14.040 30.397 1.00 20.58 C ANISOU 1242 CA GLY A 154 2330 -183 -125 3276 2210 428 C ATOM 1243 C GLY A 154 -16.022 15.322 29.596 1.00 20.58 C ANISOU 1243 C GLY A 154 2463 -138 -69 3214 2141 363 C ATOM 1244 O GLY A 154 -16.033 15.314 28.360 1.00 19.76 O ANISOU 1244 O GLY A 154 2401 -368 47 3110 1995 399 O ATOM 1245 N SER A 155 -15.929 16.436 30.302 1.00 21.32 N ANISOU 1245 N SER A 155 2757 -51 -68 3209 2132 314 N ATOM 1246 CA SER A 155 -15.734 17.683 29.627 1.00 21.71 C ANISOU 1246 CA SER A 155 2859 -10 -121 3136 2254 279 C ATOM 1247 C SER A 155 -14.283 17.720 29.074 1.00 20.06 C ANISOU 1247 C SER A 155 2481 43 -116 2934 2203 254 C ATOM 1248 O SER A 155 -13.323 17.142 29.662 1.00 20.18 O ANISOU 1248 O SER A 155 2454 54 42 3108 2106 709 O ATOM 1249 CB SER A 155 -16.095 18.852 30.498 1.00 25.08 C ANISOU 1249 CB SER A 155 3396 -93 1 3511 2620 -66 C ATOM 1250 OG SER A 155 -15.154 18.821 31.513 1.00 32.62 O ANISOU 1250 OG SER A 155 4706 -64 -435 4542 3145 -412 O ATOM 1251 N PRO A 156 -14.116 18.318 27.907 1.00 18.72 N ANISOU 1251 N PRO A 156 2308 124 -81 2686 2118 346 N ATOM 1252 CA PRO A 156 -12.790 18.362 27.284 1.00 18.43 C ANISOU 1252 CA PRO A 156 2164 77 -132 2662 2174 270 C ATOM 1253 C PRO A 156 -11.817 19.237 28.023 1.00 18.75 C ANISOU 1253 C PRO A 156 2268 51 -216 2501 2355 348 C ATOM 1254 O PRO A 156 -12.231 20.231 28.654 1.00 20.15 O ANISOU 1254 O PRO A 156 2454 171 -487 2644 2558 359 O ATOM 1255 CB PRO A 156 -13.047 18.920 25.879 1.00 18.58 C ANISOU 1255 CB PRO A 156 2063 -158 -67 2749 2247 209 C ATOM 1256 CG PRO A 156 -14.547 19.001 25.716 1.00 19.46 C ANISOU 1256 CG PRO A 156 2125 267 30 3050 2217 452 C ATOM 1257 CD PRO A 156 -15.140 18.944 27.056 1.00 19.28 C ANISOU 1257 CD PRO A 156 2245 105 -118 2825 2254 436 C ATOM 1258 N VAL A 157 -10.559 18.806 28.033 1.00 17.08 N ANISOU 1258 N VAL A 157 2111 15 -183 2284 2094 342 N ATOM 1259 CA VAL A 157 -9.433 19.505 28.679 1.00 16.93 C ANISOU 1259 CA VAL A 157 2157 -32 -196 2363 1913 253 C ATOM 1260 C VAL A 157 -8.418 19.929 27.626 1.00 15.69 C ANISOU 1260 C VAL A 157 2085 -44 -226 2095 1782 180 C ATOM 1261 O VAL A 157 -8.058 19.157 26.748 1.00 14.64 O ANISOU 1261 O VAL A 157 2111 22 -337 1973 1476 258 O ATOM 1262 CB VAL A 157 -8.742 18.537 29.663 1.00 17.32 C ANISOU 1262 CB VAL A 157 2134 -195 -160 2542 1906 265 C ATOM 1263 CG1 VAL A 157 -7.519 19.161 30.269 1.00 22.02 C ANISOU 1263 CG1 VAL A 157 2812 -92 -251 3189 2364 236 C ATOM 1264 CG2 VAL A 157 -9.718 18.172 30.744 1.00 20.16 C ANISOU 1264 CG2 VAL A 157 2418 -100 -125 3056 2183 121 C ATOM 1265 N SER A 158 -7.967 21.169 27.680 1.00 15.78 N ANISOU 1265 N SER A 158 2140 60 -347 2079 1775 200 N ATOM 1266 CA SER A 158 -6.961 21.655 26.740 1.00 14.68 C ANISOU 1266 CA SER A 158 1807 75 -284 1969 1799 171 C ATOM 1267 C SER A 158 -5.581 21.108 27.097 1.00 13.96 C ANISOU 1267 C SER A 158 1771 25 -268 1890 1641 27 C ATOM 1268 O SER A 158 -5.166 21.169 28.259 1.00 15.26 O ANISOU 1268 O SER A 158 2106 15 -394 2039 1653 -30 O ATOM 1269 CB SER A 158 -6.855 23.160 26.766 1.00 15.50 C ANISOU 1269 CB SER A 158 1923 62 -460 1968 1998 30 C ATOM 1270 OG SER A 158 -5.745 23.614 25.972 1.00 15.25 O ANISOU 1270 OG SER A 158 1453 40 -649 2250 2090 161 O ATOM 1271 N LEU A 159 -4.896 20.582 26.066 1.00 13.29 N ANISOU 1271 N LEU A 159 1685 94 -236 1757 1607 -14 N ATOM 1272 CA LEU A 159 -3.535 20.112 26.186 1.00 13.59 C ANISOU 1272 CA LEU A 159 1631 74 -197 1805 1725 -24 C ATOM 1273 C LEU A 159 -2.520 21.146 25.658 1.00 13.87 C ANISOU 1273 C LEU A 159 1754 -9 -213 1780 1733 41 C ATOM 1274 O LEU A 159 -1.291 20.862 25.548 1.00 13.30 O ANISOU 1274 O LEU A 159 1767 232 -270 1799 1484 12 O ATOM 1275 CB LEU A 159 -3.355 18.789 25.408 1.00 12.65 C ANISOU 1275 CB LEU A 159 1529 -31 -193 1720 1556 -25 C ATOM 1276 CG LEU A 159 -4.321 17.699 25.866 1.00 12.93 C ANISOU 1276 CG LEU A 159 1540 32 -170 1746 1624 -115 C ATOM 1277 CD1 LEU A 159 -3.912 16.399 25.144 1.00 13.57 C ANISOU 1277 CD1 LEU A 159 1796 -148 -73 1756 1603 369 C ATOM 1278 CD2 LEU A 159 -4.338 17.510 27.357 1.00 14.26 C ANISOU 1278 CD2 LEU A 159 1799 153 46 1786 1834 -75 C ATOM 1279 N LYS A 160 -2.981 22.368 25.453 1.00 13.94 N ANISOU 1279 N LYS A 160 1734 114 -211 1877 1683 -27 N ATOM 1280 CA LYS A 160 -2.108 23.406 24.904 1.00 14.70 C ANISOU 1280 CA LYS A 160 1952 91 -166 1834 1798 -72 C ATOM 1281 C LYS A 160 -0.870 23.671 25.758 1.00 14.47 C ANISOU 1281 C LYS A 160 2000 -49 -161 1825 1672 2 C ATOM 1282 O LYS A 160 0.223 23.965 25.218 1.00 13.72 O ANISOU 1282 O LYS A 160 1649 7 -133 1998 1564 -17 O ATOM 1283 CB LYS A 160 -2.905 24.684 24.675 1.00 16.08 C ANISOU 1283 CB LYS A 160 2058 18 -96 2086 1965 51 C ATOM 1284 CG LYS A 160 -2.148 25.657 23.959 1.00 20.24 C ANISOU 1284 CG LYS A 160 2642 213 66 2289 2758 -140 C ATOM 1285 CD LYS A 160 -2.934 26.992 23.806 1.00 20.15 C ANISOU 1285 CD LYS A 160 2662 289 290 2188 2804 -237 C ATOM 1286 CE LYS A 160 -4.213 26.827 23.004 1.00 22.11 C ANISOU 1286 CE LYS A 160 2613 232 271 2226 3558 -754 C ATOM 1287 NZ LYS A 160 -4.733 28.186 22.572 1.00 22.70 N ANISOU 1287 NZ LYS A 160 3136 644 -10 2409 3077 -165 N ATOM 1288 N GLU A 161 -0.991 23.528 27.073 1.00 13.92 N ANISOU 1288 N GLU A 161 1894 -106 -122 1828 1567 -165 N ATOM 1289 CA GLU A 161 0.168 23.761 27.947 1.00 15.98 C ANISOU 1289 CA GLU A 161 2090 -98 -243 2171 1810 -148 C ATOM 1290 C GLU A 161 1.310 22.813 27.665 1.00 15.14 C ANISOU 1290 C GLU A 161 1904 -69 -223 2097 1749 -303 C ATOM 1291 O GLU A 161 2.444 23.056 28.094 1.00 17.58 O ANISOU 1291 O GLU A 161 2194 -15 -195 2317 2166 -335 O ATOM 1292 CB GLU A 161 -0.251 23.623 29.408 1.00 16.30 C ANISOU 1292 CB GLU A 161 2202 -112 -250 2225 1765 -237 C ATOM 1293 CG GLU A 161 -0.675 22.226 29.825 1.00 19.26 C ANISOU 1293 CG GLU A 161 2551 98 -210 2326 2440 -32 C ATOM 1294 CD GLU A 161 -0.991 22.126 31.270 1.00 20.76 C ANISOU 1294 CD GLU A 161 2657 -345 -582 2995 2234 -245 C ATOM 1295 OE1 GLU A 161 -0.112 22.388 32.108 1.00 28.34 O ANISOU 1295 OE1 GLU A 161 4066 -259 -385 4265 2434 -291 O ATOM 1296 OE2 GLU A 161 -2.088 21.734 31.597 1.00 25.13 O ANISOU 1296 OE2 GLU A 161 3055 -336 -932 4240 2252 328 O ATOM 1297 N PHE A 162 1.032 21.704 26.964 1.00 14.01 N ANISOU 1297 N PHE A 162 1890 -119 -181 1936 1496 -297 N ATOM 1298 CA PHE A 162 2.080 20.732 26.641 1.00 13.46 C ANISOU 1298 CA PHE A 162 1723 -25 -129 1808 1580 -189 C ATOM 1299 C PHE A 162 2.762 20.942 25.286 1.00 13.91 C ANISOU 1299 C PHE A 162 1808 -86 -232 1876 1599 -249 C ATOM 1300 O PHE A 162 3.619 20.174 24.906 1.00 14.18 O ANISOU 1300 O PHE A 162 1683 -18 15 1904 1798 -78 O ATOM 1301 CB PHE A 162 1.510 19.318 26.743 1.00 14.15 C ANISOU 1301 CB PHE A 162 1743 20 -257 1800 1832 -275 C ATOM 1302 CG PHE A 162 0.939 19.032 28.107 1.00 12.00 C ANISOU 1302 CG PHE A 162 1769 177 -196 1511 1276 -355 C ATOM 1303 CD1 PHE A 162 -0.396 18.855 28.288 1.00 12.99 C ANISOU 1303 CD1 PHE A 162 1770 -5 53 2036 1128 -423 C ATOM 1304 CD2 PHE A 162 1.764 18.993 29.238 1.00 13.40 C ANISOU 1304 CD2 PHE A 162 1804 99 -11 1758 1528 -75 C ATOM 1305 CE1 PHE A 162 -0.940 18.621 29.548 1.00 13.37 C ANISOU 1305 CE1 PHE A 162 1753 -56 -500 1920 1405 -314 C ATOM 1306 CE2 PHE A 162 1.246 18.811 30.473 1.00 14.31 C ANISOU 1306 CE2 PHE A 162 2121 -190 -405 1684 1632 -246 C ATOM 1307 CZ PHE A 162 -0.097 18.629 30.659 1.00 14.71 C ANISOU 1307 CZ PHE A 162 1584 79 -158 2331 1674 -346 C ATOM 1308 N PHE A 163 2.429 22.028 24.630 1.00 13.32 N ANISOU 1308 N PHE A 163 1684 -73 -248 1688 1687 -293 N ATOM 1309 CA PHE A 163 2.924 22.335 23.305 1.00 13.73 C ANISOU 1309 CA PHE A 163 1749 -141 -234 1683 1783 -106 C ATOM 1310 C PHE A 163 4.028 23.389 23.477 1.00 15.88 C ANISOU 1310 C PHE A 163 2043 -201 -251 1917 2071 -186 C ATOM 1311 O PHE A 163 3.725 24.567 23.793 1.00 16.38 O ANISOU 1311 O PHE A 163 2246 -280 -364 1860 2116 -230 O ATOM 1312 CB PHE A 163 1.763 22.878 22.450 1.00 13.61 C ANISOU 1312 CB PHE A 163 1791 -162 -292 1673 1705 -107 C ATOM 1313 CG PHE A 163 2.041 23.011 20.975 1.00 12.95 C ANISOU 1313 CG PHE A 163 1655 -39 81 1603 1659 -326 C ATOM 1314 CD1 PHE A 163 2.792 22.069 20.311 1.00 11.67 C ANISOU 1314 CD1 PHE A 163 1423 17 96 1694 1315 -105 C ATOM 1315 CD2 PHE A 163 1.470 24.047 20.239 1.00 15.00 C ANISOU 1315 CD2 PHE A 163 1712 -241 202 2073 1914 -116 C ATOM 1316 CE1 PHE A 163 2.994 22.125 18.946 1.00 13.33 C ANISOU 1316 CE1 PHE A 163 1645 -153 82 1551 1868 197 C ATOM 1317 CE2 PHE A 163 1.693 24.120 18.880 1.00 14.66 C ANISOU 1317 CE2 PHE A 163 1696 -302 -97 1855 2017 -198 C ATOM 1318 CZ PHE A 163 2.441 23.163 18.230 1.00 13.06 C ANISOU 1318 CZ PHE A 163 1366 -119 30 1665 1930 76 C ATOM 1319 N PRO A 164 5.291 23.014 23.269 1.00 15.66 N ANISOU 1319 N PRO A 164 1951 -190 -80 1819 2178 -226 N ATOM 1320 CA PRO A 164 6.349 24.006 23.422 1.00 17.23 C ANISOU 1320 CA PRO A 164 2154 -255 -223 2096 2294 -224 C ATOM 1321 C PRO A 164 6.287 25.068 22.341 1.00 16.72 C ANISOU 1321 C PRO A 164 1984 -321 -205 1893 2474 -245 C ATOM 1322 O PRO A 164 5.874 24.785 21.229 1.00 16.15 O ANISOU 1322 O PRO A 164 1880 -500 -206 1796 2457 -223 O ATOM 1323 CB PRO A 164 7.611 23.201 23.274 1.00 17.47 C ANISOU 1323 CB PRO A 164 2168 -269 -78 2073 2395 -293 C ATOM 1324 CG PRO A 164 7.244 22.159 22.285 1.00 18.98 C ANISOU 1324 CG PRO A 164 2303 -240 -196 2288 2618 -132 C ATOM 1325 CD PRO A 164 5.829 21.755 22.740 1.00 17.63 C ANISOU 1325 CD PRO A 164 2137 -305 -22 2306 2253 -214 C ATOM 1326 N ALA A 165 6.753 26.292 22.663 1.00 17.53 N ANISOU 1326 N ALA A 165 2161 -261 -444 2065 2435 -304 N ATOM 1327 CA ALA A 165 6.798 27.387 21.682 1.00 18.06 C ANISOU 1327 CA ALA A 165 2157 -294 -404 2193 2512 -208 C ATOM 1328 C ALA A 165 7.817 27.155 20.549 1.00 18.03 C ANISOU 1328 C ALA A 165 2198 -231 -418 2218 2435 -223 C ATOM 1329 O ALA A 165 7.692 27.707 19.475 1.00 18.31 O ANISOU 1329 O ALA A 165 2212 -374 -503 2075 2671 -566 O ATOM 1330 CB ALA A 165 7.105 28.641 22.358 1.00 19.14 C ANISOU 1330 CB ALA A 165 2394 -208 -448 2488 2387 -6 C ATOM 1331 N GLU A 166 8.857 26.376 20.819 1.00 17.94 N ANISOU 1331 N GLU A 166 2034 -222 -274 2344 2436 -401 N ATOM 1332 CA GLU A 166 9.867 26.078 19.841 1.00 19.21 C ANISOU 1332 CA GLU A 166 2115 -246 -365 2427 2754 -230 C ATOM 1333 C GLU A 166 10.164 24.598 19.795 1.00 18.99 C ANISOU 1333 C GLU A 166 2061 -83 -143 2354 2799 -178 C ATOM 1334 O GLU A 166 10.026 23.891 20.789 1.00 18.22 O ANISOU 1334 O GLU A 166 2186 12 -139 2112 2622 -117 O ATOM 1335 CB GLU A 166 11.169 26.819 20.158 1.00 19.14 C ANISOU 1335 CB GLU A 166 2025 -160 -353 2352 2893 -206 C ATOM 1336 CG GLU A 166 11.056 28.318 20.114 1.00 23.00 C ANISOU 1336 CG GLU A 166 2221 -749 -640 2888 3628 -300 C ATOM 1337 CD GLU A 166 12.370 29.022 20.435 1.00 24.25 C ANISOU 1337 CD GLU A 166 2385 -659 -931 3420 3409 -137 C ATOM 1338 OE1 GLU A 166 13.311 28.951 19.631 1.00 30.57 O ANISOU 1338 OE1 GLU A 166 2576 -1153 -1371 4513 4526 -90 O ATOM 1339 OE2 GLU A 166 12.437 29.670 21.486 1.00 33.44 O ANISOU 1339 OE2 GLU A 166 3447 -1322 -1471 4444 4813 -171 O ATOM 1340 N MET A 167 10.493 24.151 18.595 1.00 18.88 N ANISOU 1340 N MET A 167 2058 -102 -110 2271 2844 -219 N ATOM 1341 CA MET A 167 11.077 22.835 18.316 1.00 20.29 C ANISOU 1341 CA MET A 167 2122 -85 -93 2477 3109 -186 C ATOM 1342 C MET A 167 12.302 23.047 17.432 1.00 23.06 C ANISOU 1342 C MET A 167 2443 9 91 2816 3501 -26 C ATOM 1343 O MET A 167 12.434 24.058 16.805 1.00 27.38 O ANISOU 1343 O MET A 167 2393 252 267 3972 4038 109 O ATOM 1344 CB MET A 167 10.023 21.951 17.635 1.00 19.18 C ANISOU 1344 CB MET A 167 2224 -147 -119 2192 2872 -311 C ATOM 1345 CG MET A 167 8.906 21.589 18.545 1.00 17.59 C ANISOU 1345 CG MET A 167 2040 -102 25 2056 2585 -322 C ATOM 1346 SD MET A 167 7.666 20.559 17.661 1.00 17.23 S ANISOU 1346 SD MET A 167 2271 22 -6 1621 2651 -326 S ATOM 1347 CE MET A 167 6.457 20.212 18.915 1.00 16.83 C ANISOU 1347 CE MET A 167 1964 20 406 2198 2232 -868 C ATOM 1348 N GLU A 168 13.276 22.168 17.482 1.00 25.71 N ANISOU 1348 N GLU A 168 2642 -82 -168 3383 3744 64 N ATOM 1349 CA GLU A 168 14.586 22.511 16.902 1.00 25.05 C ANISOU 1349 CA GLU A 168 2605 -100 -183 3329 3584 -21 C ATOM 1350 C GLU A 168 14.444 23.129 15.528 1.00 25.15 C ANISOU 1350 C GLU A 168 2666 -113 -289 3352 3538 -27 C ATOM 1351 O GLU A 168 13.771 22.577 14.634 1.00 26.57 O ANISOU 1351 O GLU A 168 2785 -72 -390 3710 3601 -46 O ATOM 1352 CB GLU A 168 15.473 21.280 16.833 1.00 27.67 C ANISOU 1352 CB GLU A 168 2850 -76 -188 3718 3944 157 C ATOM 1353 CG GLU A 168 16.864 21.536 16.213 1.00 31.41 C ANISOU 1353 CG GLU A 168 3406 -161 -168 4266 4263 47 C ATOM 1354 CD GLU A 168 17.778 22.539 16.954 1.00 39.85 C ANISOU 1354 CD GLU A 168 4270 -13 177 5671 5197 -191 C ATOM 1355 OE1 GLU A 168 17.667 22.682 18.217 1.00 44.41 O ANISOU 1355 OE1 GLU A 168 4760 548 89 6762 5352 -421 O ATOM 1356 OE2 GLU A 168 18.635 23.169 16.243 1.00 41.63 O ANISOU 1356 OE2 GLU A 168 3973 -137 765 6341 5502 -137 O ATOM 1357 N GLY A 169 15.011 24.307 15.369 1.00 23.29 N ANISOU 1357 N GLY A 169 2404 -288 -211 3245 3200 -208 N ATOM 1358 CA GLY A 169 14.955 25.036 14.123 1.00 23.22 C ANISOU 1358 CA GLY A 169 2496 -168 -233 3058 3269 -184 C ATOM 1359 C GLY A 169 13.666 25.793 13.807 1.00 22.79 C ANISOU 1359 C GLY A 169 2570 -178 -160 3036 3050 -248 C ATOM 1360 O GLY A 169 13.568 26.342 12.672 1.00 25.17 O ANISOU 1360 O GLY A 169 2966 -125 -136 3437 3158 -125 O ATOM 1361 N AMET A 170 12.735 25.905 14.785 0.45 21.60 N ANISOU 1361 N AMET A 170 2451 -235 -220 2828 2926 -222 N ATOM 1362 N BMET A 170 12.681 25.827 14.729 0.55 20.84 N ANISOU 1362 N BMET A 170 2338 -260 -256 2707 2874 -262 N ATOM 1363 CA AMET A 170 11.376 26.322 14.461 0.45 20.57 C ANISOU 1363 CA AMET A 170 2346 -268 -268 2632 2837 -282 C ATOM 1364 CA BMET A 170 11.405 26.435 14.389 0.55 19.31 C ANISOU 1364 CA BMET A 170 2190 -259 -289 2390 2755 -316 C ATOM 1365 C AMET A 170 10.486 26.856 15.570 0.45 19.02 C ANISOU 1365 C AMET A 170 2197 -357 -205 2356 2671 -237 C ATOM 1366 C BMET A 170 10.616 26.999 15.557 0.55 18.47 C ANISOU 1366 C BMET A 170 2143 -344 -213 2216 2657 -229 C ATOM 1367 O AMET A 170 10.501 26.395 16.703 0.45 18.78 O ANISOU 1367 O AMET A 170 2162 -207 -134 2353 2619 -393 O ATOM 1368 O BMET A 170 10.921 26.803 16.720 0.55 19.10 O ANISOU 1368 O BMET A 170 2288 -77 -129 2194 2772 -336 O ATOM 1369 CB AMET A 170 10.652 25.124 13.839 0.45 20.01 C ANISOU 1369 CB AMET A 170 2358 -315 -309 2503 2740 -309 C ATOM 1370 CB BMET A 170 10.513 25.419 13.631 0.55 18.40 C ANISOU 1370 CB BMET A 170 2109 -263 -396 2259 2620 -396 C ATOM 1371 CG AMET A 170 11.577 24.356 12.948 0.45 21.17 C ANISOU 1371 CG AMET A 170 2523 -236 -237 2668 2851 -306 C ATOM 1372 CG BMET A 170 10.266 24.172 14.405 0.55 17.15 C ANISOU 1372 CG BMET A 170 2053 -224 -496 2207 2256 -382 C ATOM 1373 SD AMET A 170 10.754 23.020 12.164 0.45 20.56 S ANISOU 1373 SD AMET A 170 2232 -224 -356 2908 2669 -632 S ATOM 1374 SD BMET A 170 9.197 23.028 13.519 0.55 17.18 S ANISOU 1374 SD BMET A 170 1857 -151 -14 2085 2583 -673 S ATOM 1375 CE AMET A 170 10.627 21.807 13.490 0.45 19.55 C ANISOU 1375 CE AMET A 170 2239 -84 -359 2582 2607 -408 C ATOM 1376 CE BMET A 170 10.287 21.674 13.049 0.55 17.13 C ANISOU 1376 CE BMET A 170 2082 1 -163 1745 2679 -258 C ATOM 1377 N HIS A 171 9.623 27.783 15.187 1.00 18.00 N ANISOU 1377 N HIS A 171 2016 -403 -149 2199 2624 -238 N ATOM 1378 CA HIS A 171 8.588 28.254 16.073 1.00 17.43 C ANISOU 1378 CA HIS A 171 2083 -388 -166 2098 2441 -89 C ATOM 1379 C HIS A 171 7.296 27.503 15.751 1.00 16.35 C ANISOU 1379 C HIS A 171 1943 -432 -88 1910 2358 -137 C ATOM 1380 O HIS A 171 6.877 27.440 14.602 1.00 17.04 O ANISOU 1380 O HIS A 171 1978 -425 -65 1978 2517 -157 O ATOM 1381 CB HIS A 171 8.422 29.727 15.847 1.00 18.93 C ANISOU 1381 CB HIS A 171 2130 -501 -302 2311 2749 -186 C ATOM 1382 CG HIS A 171 9.600 30.484 16.325 1.00 21.35 C ANISOU 1382 CG HIS A 171 2852 -923 -633 2643 2617 -291 C ATOM 1383 ND1 HIS A 171 9.837 30.682 17.667 1.00 23.93 N ANISOU 1383 ND1 HIS A 171 2950 -829 -303 3080 3061 -1182 N ATOM 1384 CD2 HIS A 171 10.675 30.948 15.670 1.00 26.81 C ANISOU 1384 CD2 HIS A 171 3467 -857 -758 3682 3035 -599 C ATOM 1385 CE1 HIS A 171 10.985 31.312 17.803 1.00 26.96 C ANISOU 1385 CE1 HIS A 171 3462 -1059 -534 3526 3253 -547 C ATOM 1386 NE2 HIS A 171 11.508 31.489 16.606 1.00 28.29 N ANISOU 1386 NE2 HIS A 171 3770 -936 -1106 3564 3414 -418 N ATOM 1387 N THR A 172 6.678 26.906 16.768 1.00 15.80 N ANISOU 1387 N THR A 172 1768 -206 -49 1777 2458 -110 N ATOM 1388 CA THR A 172 5.492 26.068 16.537 1.00 14.60 C ANISOU 1388 CA THR A 172 1676 -255 -154 1660 2209 -125 C ATOM 1389 C THR A 172 4.275 26.903 16.337 1.00 13.74 C ANISOU 1389 C THR A 172 1652 -197 -95 1416 2152 -163 C ATOM 1390 O THR A 172 4.213 28.047 16.787 1.00 14.92 O ANISOU 1390 O THR A 172 1684 -223 -210 1475 2507 -159 O ATOM 1391 CB THR A 172 5.219 25.153 17.723 1.00 14.73 C ANISOU 1391 CB THR A 172 1640 -77 18 1701 2255 -82 C ATOM 1392 OG1 THR A 172 5.142 25.931 18.925 1.00 16.21 O ANISOU 1392 OG1 THR A 172 1901 -252 -63 1855 2402 -151 O ATOM 1393 CG2 THR A 172 6.366 24.208 17.967 1.00 16.36 C ANISOU 1393 CG2 THR A 172 1599 -34 -152 2072 2544 -309 C ATOM 1394 N ASN A 173 3.263 26.329 15.684 1.00 12.38 N ANISOU 1394 N ASN A 173 1337 -129 -214 1250 2115 -225 N ATOM 1395 CA ASN A 173 2.049 27.082 15.369 1.00 12.45 C ANISOU 1395 CA ASN A 173 1565 -64 -40 1378 1787 12 C ATOM 1396 C ASN A 173 0.861 26.271 15.921 1.00 12.68 C ANISOU 1396 C ASN A 173 1517 -59 -160 1387 1913 -37 C ATOM 1397 O ASN A 173 0.331 26.631 16.981 1.00 12.99 O ANISOU 1397 O ASN A 173 1671 30 -133 1448 1814 -21 O ATOM 1398 CB ASN A 173 2.035 27.357 13.857 1.00 12.36 C ANISOU 1398 CB ASN A 173 1479 247 -77 1396 1821 -55 C ATOM 1399 CG ASN A 173 0.943 28.205 13.402 1.00 15.42 C ANISOU 1399 CG ASN A 173 2347 122 -193 1481 2031 102 C ATOM 1400 OD1 ASN A 173 0.039 28.545 14.134 1.00 18.91 O ANISOU 1400 OD1 ASN A 173 2488 661 38 1965 2731 76 O ATOM 1401 ND2 ASN A 173 0.993 28.531 12.082 1.00 18.15 N ANISOU 1401 ND2 ASN A 173 2201 514 49 1907 2787 -103 N ATOM 1402 N GLN A 174 0.461 25.190 15.253 1.00 12.14 N ANISOU 1402 N GLN A 174 1537 -121 -312 1343 1730 145 N ATOM 1403 CA GLN A 174 -0.661 24.364 15.697 1.00 11.73 C ANISOU 1403 CA GLN A 174 1428 -29 4 1326 1702 61 C ATOM 1404 C GLN A 174 -0.300 22.871 15.657 1.00 11.79 C ANISOU 1404 C GLN A 174 1384 -24 -69 1292 1804 20 C ATOM 1405 O GLN A 174 0.693 22.476 15.034 1.00 10.96 O ANISOU 1405 O GLN A 174 1054 -27 -160 1252 1857 20 O ATOM 1406 CB GLN A 174 -1.898 24.599 14.824 1.00 11.30 C ANISOU 1406 CB GLN A 174 1243 -21 110 1379 1672 -5 C ATOM 1407 CG GLN A 174 -2.345 26.029 14.830 1.00 13.04 C ANISOU 1407 CG GLN A 174 1568 1 108 1409 1977 198 C ATOM 1408 CD GLN A 174 -3.488 26.381 13.897 1.00 12.57 C ANISOU 1408 CD GLN A 174 1400 56 192 1389 1985 245 C ATOM 1409 OE1 GLN A 174 -3.703 27.623 13.530 1.00 19.22 O ANISOU 1409 OE1 GLN A 174 2635 431 439 1519 3148 350 O ATOM 1410 NE2 GLN A 174 -4.244 25.385 13.517 1.00 9.69 N ANISOU 1410 NE2 GLN A 174 1326 187 69 904 1448 125 N ATOM 1411 N PHE A 175 -1.133 22.018 16.272 1.00 10.80 N ANISOU 1411 N PHE A 175 1299 50 5 1239 1563 15 N ATOM 1412 CA PHE A 175 -1.023 20.577 15.990 1.00 10.30 C ANISOU 1412 CA PHE A 175 1221 -24 18 1225 1465 -57 C ATOM 1413 C PHE A 175 -2.384 19.948 16.151 1.00 10.73 C ANISOU 1413 C PHE A 175 1296 -57 17 1234 1547 -23 C ATOM 1414 O PHE A 175 -3.274 20.523 16.810 1.00 10.63 O ANISOU 1414 O PHE A 175 1366 -253 -18 1155 1517 13 O ATOM 1415 CB PHE A 175 0.034 19.863 16.830 1.00 11.54 C ANISOU 1415 CB PHE A 175 1317 -2 9 1396 1671 96 C ATOM 1416 CG PHE A 175 -0.302 19.608 18.268 1.00 9.12 C ANISOU 1416 CG PHE A 175 1168 -183 -109 970 1326 -117 C ATOM 1417 CD1 PHE A 175 -0.696 18.347 18.654 1.00 9.59 C ANISOU 1417 CD1 PHE A 175 1231 -240 120 1252 1161 -27 C ATOM 1418 CD2 PHE A 175 -0.168 20.579 19.249 1.00 10.99 C ANISOU 1418 CD2 PHE A 175 1237 -64 64 1579 1358 -71 C ATOM 1419 CE1 PHE A 175 -0.918 18.055 19.990 1.00 11.38 C ANISOU 1419 CE1 PHE A 175 1622 23 124 1340 1360 206 C ATOM 1420 CE2 PHE A 175 -0.405 20.282 20.578 1.00 12.44 C ANISOU 1420 CE2 PHE A 175 1478 119 -199 1554 1694 75 C ATOM 1421 CZ PHE A 175 -0.788 19.023 20.949 1.00 12.08 C ANISOU 1421 CZ PHE A 175 1388 20 -36 1867 1331 -3 C ATOM 1422 N LEU A 176 -2.541 18.805 15.494 1.00 9.69 N ANISOU 1422 N LEU A 176 1179 -115 -70 1173 1330 -98 N ATOM 1423 CA LEU A 176 -3.762 18.018 15.472 1.00 11.40 C ANISOU 1423 CA LEU A 176 1443 -58 -44 1387 1498 23 C ATOM 1424 C LEU A 176 -3.419 16.530 15.498 1.00 10.66 C ANISOU 1424 C LEU A 176 1405 -46 -86 1279 1365 -3 C ATOM 1425 O LEU A 176 -2.331 16.129 15.088 1.00 11.20 O ANISOU 1425 O LEU A 176 1483 -135 -101 1381 1391 124 O ATOM 1426 CB LEU A 176 -4.542 18.274 14.191 1.00 10.01 C ANISOU 1426 CB LEU A 176 1203 7 86 1288 1310 32 C ATOM 1427 CG LEU A 176 -5.018 19.723 14.011 1.00 10.27 C ANISOU 1427 CG LEU A 176 1199 177 -42 1643 1057 -124 C ATOM 1428 CD1 LEU A 176 -5.593 19.894 12.610 1.00 12.79 C ANISOU 1428 CD1 LEU A 176 1495 0 103 1895 1468 -91 C ATOM 1429 CD2 LEU A 176 -6.073 20.112 15.039 1.00 11.25 C ANISOU 1429 CD2 LEU A 176 1336 172 89 1499 1438 -443 C ATOM 1430 N GLY A 177 -4.380 15.696 15.916 1.00 10.22 N ANISOU 1430 N GLY A 177 1497 -133 -193 1176 1209 126 N ATOM 1431 CA GLY A 177 -4.247 14.270 15.690 1.00 10.36 C ANISOU 1431 CA GLY A 177 1406 -65 65 1217 1312 94 C ATOM 1432 C GLY A 177 -4.246 13.893 14.204 1.00 10.03 C ANISOU 1432 C GLY A 177 1308 -80 69 1158 1342 167 C ATOM 1433 O GLY A 177 -4.675 14.671 13.337 1.00 10.70 O ANISOU 1433 O GLY A 177 1426 79 230 1181 1455 152 O ATOM 1434 N GLY A 178 -3.775 12.691 13.920 1.00 9.85 N ANISOU 1434 N GLY A 178 1385 93 124 1136 1221 97 N ATOM 1435 CA GLY A 178 -3.806 12.134 12.600 1.00 9.86 C ANISOU 1435 CA GLY A 178 1226 56 106 1386 1132 6 C ATOM 1436 C GLY A 178 -5.051 11.384 12.211 1.00 10.70 C ANISOU 1436 C GLY A 178 1370 6 146 1553 1143 30 C ATOM 1437 O GLY A 178 -5.051 10.739 11.162 1.00 11.02 O ANISOU 1437 O GLY A 178 1367 -154 157 1658 1158 -36 O ATOM 1438 N ALA A 179 -6.116 11.556 13.019 1.00 9.31 N ANISOU 1438 N ALA A 179 1184 163 36 1459 891 -129 N ATOM 1439 CA ALA A 179 -7.433 10.991 12.766 1.00 10.74 C ANISOU 1439 CA ALA A 179 1407 49 165 1561 1110 -78 C ATOM 1440 C ALA A 179 -7.447 9.501 12.965 1.00 9.38 C ANISOU 1440 C ALA A 179 1250 49 136 1307 1007 -291 C ATOM 1441 O ALA A 179 -6.397 8.858 13.147 1.00 9.86 O ANISOU 1441 O ALA A 179 988 143 92 1300 1458 -79 O ATOM 1442 CB ALA A 179 -7.958 11.338 11.407 1.00 10.52 C ANISOU 1442 CB ALA A 179 1597 77 408 1386 1012 -16 C ATOM 1443 N GLY A 180 -8.642 8.922 12.948 1.00 8.86 N ANISOU 1443 N GLY A 180 1157 30 281 1198 1010 -349 N ATOM 1444 CA GLY A 180 -8.736 7.484 13.082 1.00 9.42 C ANISOU 1444 CA GLY A 180 1245 -35 100 1363 971 -215 C ATOM 1445 C GLY A 180 -8.346 7.047 14.476 1.00 8.56 C ANISOU 1445 C GLY A 180 1195 -30 59 1287 769 -315 C ATOM 1446 O GLY A 180 -8.755 7.669 15.461 1.00 9.60 O ANISOU 1446 O GLY A 180 1377 13 37 1386 882 -44 O ATOM 1447 N VAL A 181 -7.567 5.966 14.550 1.00 8.15 N ANISOU 1447 N VAL A 181 1032 -117 -59 1396 668 -218 N ATOM 1448 CA VAL A 181 -7.300 5.284 15.828 1.00 8.70 C ANISOU 1448 CA VAL A 181 1147 71 26 1330 826 -139 C ATOM 1449 C VAL A 181 -5.802 5.191 16.077 1.00 8.29 C ANISOU 1449 C VAL A 181 1093 -36 -25 1313 744 -204 C ATOM 1450 O VAL A 181 -5.032 4.791 15.211 1.00 9.02 O ANISOU 1450 O VAL A 181 992 -118 54 1630 805 -292 O ATOM 1451 CB VAL A 181 -7.929 3.868 15.837 1.00 10.14 C ANISOU 1451 CB VAL A 181 1227 -207 -91 1621 1003 -278 C ATOM 1452 CG1 VAL A 181 -7.864 3.257 17.260 1.00 10.51 C ANISOU 1452 CG1 VAL A 181 1165 40 177 1554 1274 -178 C ATOM 1453 CG2 VAL A 181 -9.344 3.921 15.323 1.00 10.43 C ANISOU 1453 CG2 VAL A 181 1183 -501 -108 1746 1032 -393 C ATOM 1454 N ALA A 182 -5.413 5.652 17.243 1.00 8.99 N ANISOU 1454 N ALA A 182 1158 -3 131 1478 777 -249 N ATOM 1455 CA ALA A 182 -4.034 5.592 17.732 1.00 9.45 C ANISOU 1455 CA ALA A 182 1250 -79 231 1419 921 -212 C ATOM 1456 C ALA A 182 -3.904 4.464 18.753 1.00 10.18 C ANISOU 1456 C ALA A 182 1348 -99 229 1619 898 -122 C ATOM 1457 O ALA A 182 -4.719 3.542 18.725 1.00 10.47 O ANISOU 1457 O ALA A 182 1398 -247 436 1406 1172 -326 O ATOM 1458 CB ALA A 182 -3.619 6.935 18.235 1.00 10.43 C ANISOU 1458 CB ALA A 182 1722 113 392 1335 904 -253 C ATOM 1459 N ILE A 183 -2.848 4.448 19.547 1.00 9.83 N ANISOU 1459 N ILE A 183 1302 -118 110 1318 1112 -202 N ATOM 1460 CA ILE A 183 -2.512 3.267 20.316 1.00 10.64 C ANISOU 1460 CA ILE A 183 1453 -141 119 1666 924 -245 C ATOM 1461 C ILE A 183 -2.132 3.486 21.754 1.00 11.54 C ANISOU 1461 C ILE A 183 1609 -134 67 1644 1129 -266 C ATOM 1462 O ILE A 183 -1.741 4.556 22.160 1.00 10.02 O ANISOU 1462 O ILE A 183 1474 -254 -76 1702 630 -386 O ATOM 1463 CB ILE A 183 -1.348 2.480 19.617 1.00 10.89 C ANISOU 1463 CB ILE A 183 1603 -118 26 1470 1063 -261 C ATOM 1464 CG1 ILE A 183 -0.022 3.228 19.726 1.00 9.76 C ANISOU 1464 CG1 ILE A 183 1382 -148 -177 1515 810 -315 C ATOM 1465 CG2 ILE A 183 -1.743 2.078 18.155 1.00 11.53 C ANISOU 1465 CG2 ILE A 183 1770 -8 24 1816 795 2 C ATOM 1466 CD1 ILE A 183 1.135 2.439 19.178 1.00 12.35 C ANISOU 1466 CD1 ILE A 183 1533 -228 -223 1863 1296 -549 C ATOM 1467 N VAL A 184 -2.225 2.390 22.488 1.00 11.35 N ANISOU 1467 N VAL A 184 1670 -365 279 1667 973 -317 N ATOM 1468 CA VAL A 184 -1.534 2.208 23.752 1.00 11.30 C ANISOU 1468 CA VAL A 184 1567 -225 351 1749 977 -358 C ATOM 1469 C VAL A 184 -0.302 1.342 23.450 1.00 11.79 C ANISOU 1469 C VAL A 184 1713 -90 193 1668 1095 -358 C ATOM 1470 O VAL A 184 -0.403 0.261 22.887 1.00 12.42 O ANISOU 1470 O VAL A 184 1622 -87 141 1614 1482 -331 O ATOM 1471 CB VAL A 184 -2.435 1.424 24.727 1.00 12.88 C ANISOU 1471 CB VAL A 184 1806 -226 295 1946 1139 -263 C ATOM 1472 CG1 VAL A 184 -1.695 1.134 25.984 1.00 15.87 C ANISOU 1472 CG1 VAL A 184 2158 -389 486 2365 1506 -549 C ATOM 1473 CG2 VAL A 184 -3.727 2.172 25.043 1.00 10.98 C ANISOU 1473 CG2 VAL A 184 1468 -316 581 2171 530 -247 C ATOM 1474 N ALA A 185 0.893 1.863 23.749 1.00 10.87 N ANISOU 1474 N ALA A 185 1532 -18 296 1414 1183 -258 N ATOM 1475 CA ALA A 185 2.142 1.134 23.583 1.00 12.06 C ANISOU 1475 CA ALA A 185 1714 46 259 1665 1201 -190 C ATOM 1476 C ALA A 185 2.280 0.033 24.637 1.00 11.90 C ANISOU 1476 C ALA A 185 1714 96 284 1742 1065 -246 C ATOM 1477 O ALA A 185 1.538 0.023 25.645 1.00 11.89 O ANISOU 1477 O ALA A 185 1642 39 361 1777 1098 -315 O ATOM 1478 CB ALA A 185 3.344 2.091 23.708 1.00 12.08 C ANISOU 1478 CB ALA A 185 1740 94 524 1533 1314 -216 C ATOM 1479 N SER A 186 3.276 -0.835 24.439 1.00 11.86 N ANISOU 1479 N SER A 186 1842 142 338 1649 1013 -61 N ATOM 1480 CA SER A 186 3.419 -2.007 25.279 1.00 13.35 C ANISOU 1480 CA SER A 186 2040 233 248 1766 1264 -113 C ATOM 1481 C SER A 186 3.837 -1.626 26.688 1.00 13.26 C ANISOU 1481 C SER A 186 1915 134 240 1739 1384 -105 C ATOM 1482 O SER A 186 3.677 -2.426 27.614 1.00 14.40 O ANISOU 1482 O SER A 186 2155 -49 264 1762 1551 48 O ATOM 1483 CB SER A 186 4.407 -3.039 24.688 1.00 13.86 C ANISOU 1483 CB SER A 186 2125 269 357 1917 1225 -54 C ATOM 1484 OG SER A 186 5.679 -2.423 24.490 1.00 19.30 O ANISOU 1484 OG SER A 186 2747 547 -82 2708 1875 203 O ATOM 1485 N ASN A 187 4.327 -0.407 26.851 1.00 11.48 N ANISOU 1485 N ASN A 187 1350 50 97 1651 1360 -111 N ATOM 1486 CA ASN A 187 4.652 0.115 28.196 1.00 11.51 C ANISOU 1486 CA ASN A 187 1499 57 130 1649 1224 -83 C ATOM 1487 C ASN A 187 3.517 0.888 28.842 1.00 10.52 C ANISOU 1487 C ASN A 187 1377 70 98 1472 1146 -141 C ATOM 1488 O ASN A 187 3.705 1.479 29.925 1.00 12.18 O ANISOU 1488 O ASN A 187 1682 170 67 1746 1200 -188 O ATOM 1489 CB ASN A 187 5.899 0.973 28.176 1.00 12.85 C ANISOU 1489 CB ASN A 187 1470 101 -4 1863 1549 -20 C ATOM 1490 CG ASN A 187 5.756 2.230 27.360 1.00 12.84 C ANISOU 1490 CG ASN A 187 1309 -10 311 2096 1474 22 C ATOM 1491 OD1 ASN A 187 4.674 2.557 26.872 1.00 12.01 O ANISOU 1491 OD1 ASN A 187 1258 -141 -146 1757 1545 -149 O ATOM 1492 ND2 ASN A 187 6.839 3.010 27.291 1.00 18.31 N ANISOU 1492 ND2 ASN A 187 1916 -172 233 2345 2694 -312 N ATOM 1493 N GLY A 188 2.354 0.876 28.190 1.00 10.96 N ANISOU 1493 N GLY A 188 1592 80 206 1471 1099 -146 N ATOM 1494 CA GLY A 188 1.183 1.513 28.665 1.00 10.41 C ANISOU 1494 CA GLY A 188 1346 7 372 1587 1022 -131 C ATOM 1495 C GLY A 188 0.985 2.927 28.117 1.00 11.37 C ANISOU 1495 C GLY A 188 1446 25 423 1679 1191 -68 C ATOM 1496 O GLY A 188 -0.085 3.528 28.275 1.00 11.60 O ANISOU 1496 O GLY A 188 1433 181 500 1721 1252 -277 O ATOM 1497 N ASN A 189 1.998 3.497 27.463 1.00 10.52 N ANISOU 1497 N ASN A 189 1261 -71 278 1668 1067 -61 N ATOM 1498 CA ASN A 189 1.860 4.898 27.079 1.00 10.31 C ANISOU 1498 CA ASN A 189 1306 -127 283 1523 1086 -117 C ATOM 1499 C ASN A 189 0.707 5.070 26.112 1.00 9.72 C ANISOU 1499 C ASN A 189 1162 -59 129 1469 1063 -115 C ATOM 1500 O ASN A 189 0.556 4.274 25.191 1.00 9.48 O ANISOU 1500 O ASN A 189 1426 41 42 1462 711 -525 O ATOM 1501 CB ASN A 189 3.156 5.380 26.382 1.00 10.84 C ANISOU 1501 CB ASN A 189 1271 -257 285 1576 1271 -78 C ATOM 1502 CG ASN A 189 4.318 5.639 27.358 1.00 12.24 C ANISOU 1502 CG ASN A 189 1696 -355 299 1607 1344 -188 C ATOM 1503 OD1 ASN A 189 4.215 5.461 28.558 1.00 11.04 O ANISOU 1503 OD1 ASN A 189 1042 50 447 2017 1135 -409 O ATOM 1504 ND2 ASN A 189 5.450 6.073 26.794 1.00 12.63 N ANISOU 1504 ND2 ASN A 189 1472 -56 430 1902 1424 -276 N ATOM 1505 N LEU A 190 -0.076 6.142 26.265 1.00 9.73 N ANISOU 1505 N LEU A 190 1272 -114 -30 1607 816 -314 N ATOM 1506 CA LEU A 190 -0.975 6.623 25.207 1.00 10.13 C ANISOU 1506 CA LEU A 190 1226 -53 86 1561 1060 -235 C ATOM 1507 C LEU A 190 -0.095 7.290 24.193 1.00 9.21 C ANISOU 1507 C LEU A 190 1176 -105 84 1444 880 -337 C ATOM 1508 O LEU A 190 0.689 8.192 24.539 1.00 10.08 O ANISOU 1508 O LEU A 190 1505 -330 277 1424 899 -234 O ATOM 1509 CB LEU A 190 -1.967 7.603 25.820 1.00 9.84 C ANISOU 1509 CB LEU A 190 1135 -141 163 1542 1061 -253 C ATOM 1510 CG LEU A 190 -2.862 7.059 26.929 1.00 10.89 C ANISOU 1510 CG LEU A 190 1197 -172 -50 1810 1129 -250 C ATOM 1511 CD1 LEU A 190 -3.675 8.236 27.438 1.00 13.63 C ANISOU 1511 CD1 LEU A 190 1551 -182 -127 2158 1469 68 C ATOM 1512 CD2 LEU A 190 -3.802 6.044 26.397 1.00 14.15 C ANISOU 1512 CD2 LEU A 190 1705 -104 18 1944 1726 71 C ATOM 1513 N VAL A 191 -0.210 6.898 22.933 1.00 8.71 N ANISOU 1513 N VAL A 191 1134 -203 36 1325 850 -248 N ATOM 1514 CA VAL A 191 0.614 7.429 21.838 1.00 8.99 C ANISOU 1514 CA VAL A 191 1134 -70 65 1399 880 -252 C ATOM 1515 C VAL A 191 -0.260 7.924 20.704 1.00 8.54 C ANISOU 1515 C VAL A 191 1062 -92 135 1308 872 -178 C ATOM 1516 O VAL A 191 -0.917 7.127 20.047 1.00 10.17 O ANISOU 1516 O VAL A 191 1481 -281 206 1268 1114 -461 O ATOM 1517 CB VAL A 191 1.532 6.374 21.294 1.00 9.93 C ANISOU 1517 CB VAL A 191 1131 119 216 1578 1065 -113 C ATOM 1518 CG1 VAL A 191 2.418 6.926 20.193 1.00 12.63 C ANISOU 1518 CG1 VAL A 191 1772 70 181 1707 1319 -49 C ATOM 1519 CG2 VAL A 191 2.416 5.807 22.418 1.00 10.45 C ANISOU 1519 CG2 VAL A 191 1139 178 156 1622 1209 -12 C ATOM 1520 N TYR A 192 -0.214 9.234 20.470 1.00 9.00 N ANISOU 1520 N TYR A 192 1215 -162 44 1304 898 -289 N ATOM 1521 CA TYR A 192 -0.809 9.861 19.310 1.00 9.53 C ANISOU 1521 CA TYR A 192 1286 -118 112 1240 1094 -205 C ATOM 1522 C TYR A 192 0.328 10.313 18.386 1.00 10.29 C ANISOU 1522 C TYR A 192 1309 -78 159 1388 1212 -182 C ATOM 1523 O TYR A 192 1.142 11.190 18.758 1.00 9.96 O ANISOU 1523 O TYR A 192 1236 -184 4 1311 1235 -93 O ATOM 1524 CB TYR A 192 -1.603 11.118 19.662 1.00 10.56 C ANISOU 1524 CB TYR A 192 1381 -174 115 1509 1119 -166 C ATOM 1525 CG TYR A 192 -2.936 10.895 20.332 1.00 9.35 C ANISOU 1525 CG TYR A 192 1234 31 88 1234 1083 -8 C ATOM 1526 CD1 TYR A 192 -3.149 11.304 21.662 1.00 10.62 C ANISOU 1526 CD1 TYR A 192 1345 -229 234 1609 1079 -304 C ATOM 1527 CD2 TYR A 192 -3.996 10.320 19.646 1.00 10.50 C ANISOU 1527 CD2 TYR A 192 1065 -242 337 1512 1412 -56 C ATOM 1528 CE1 TYR A 192 -4.386 11.115 22.271 1.00 11.50 C ANISOU 1528 CE1 TYR A 192 1338 201 228 1742 1289 -165 C ATOM 1529 CE2 TYR A 192 -5.206 10.166 20.232 1.00 10.60 C ANISOU 1529 CE2 TYR A 192 1326 -273 371 1231 1469 -142 C ATOM 1530 CZ TYR A 192 -5.414 10.550 21.547 1.00 10.42 C ANISOU 1530 CZ TYR A 192 1360 -31 354 1415 1183 15 C ATOM 1531 OH TYR A 192 -6.644 10.383 22.192 1.00 13.17 O ANISOU 1531 OH TYR A 192 1253 -38 476 1960 1789 -36 O ATOM 1532 N PRO A 193 0.343 9.825 17.146 1.00 9.74 N ANISOU 1532 N PRO A 193 1474 -77 104 1165 1061 -314 N ATOM 1533 CA PRO A 193 1.177 10.493 16.145 1.00 10.25 C ANISOU 1533 CA PRO A 193 1470 -76 159 1179 1245 -266 C ATOM 1534 C PRO A 193 0.376 11.743 15.745 1.00 10.58 C ANISOU 1534 C PRO A 193 1462 -51 166 1276 1280 -182 C ATOM 1535 O PRO A 193 -0.846 11.693 15.519 1.00 12.09 O ANISOU 1535 O PRO A 193 1649 -115 237 1295 1648 -327 O ATOM 1536 CB PRO A 193 1.305 9.478 15.018 1.00 10.68 C ANISOU 1536 CB PRO A 193 1681 -102 273 1235 1141 -414 C ATOM 1537 CG PRO A 193 0.018 8.696 15.117 1.00 12.83 C ANISOU 1537 CG PRO A 193 1788 19 -48 1599 1486 -293 C ATOM 1538 CD PRO A 193 -0.418 8.699 16.573 1.00 11.70 C ANISOU 1538 CD PRO A 193 1742 4 291 1478 1223 -342 C ATOM 1539 N VAL A 194 1.046 12.875 15.744 1.00 9.47 N ANISOU 1539 N VAL A 194 1194 -172 108 1123 1280 -189 N ATOM 1540 CA VAL A 194 0.374 14.154 15.452 1.00 9.06 C ANISOU 1540 CA VAL A 194 1181 -109 125 1009 1250 -126 C ATOM 1541 C VAL A 194 1.021 14.870 14.299 1.00 8.47 C ANISOU 1541 C VAL A 194 1070 51 91 1016 1129 -156 C ATOM 1542 O VAL A 194 2.182 14.650 13.984 1.00 8.94 O ANISOU 1542 O VAL A 194 1260 -41 241 1109 1026 -176 O ATOM 1543 CB VAL A 194 0.291 15.043 16.720 1.00 10.35 C ANISOU 1543 CB VAL A 194 1230 -14 93 1384 1317 58 C ATOM 1544 CG1 VAL A 194 -0.516 14.355 17.796 1.00 10.16 C ANISOU 1544 CG1 VAL A 194 1239 -33 179 1385 1234 -193 C ATOM 1545 CG2 VAL A 194 1.688 15.447 17.223 1.00 11.56 C ANISOU 1545 CG2 VAL A 194 1543 49 61 1619 1228 48 C ATOM 1546 N GLN A 195 0.215 15.713 13.641 1.00 9.24 N ANISOU 1546 N GLN A 195 940 88 282 1234 1334 -123 N ATOM 1547 CA GLN A 195 0.672 16.584 12.593 1.00 8.79 C ANISOU 1547 CA GLN A 195 973 117 167 1134 1229 -99 C ATOM 1548 C GLN A 195 0.760 17.981 13.211 1.00 9.75 C ANISOU 1548 C GLN A 195 1116 0 176 1219 1368 -19 C ATOM 1549 O GLN A 195 -0.163 18.447 13.902 1.00 10.53 O ANISOU 1549 O GLN A 195 1324 27 10 1173 1504 261 O ATOM 1550 CB GLN A 195 -0.280 16.536 11.395 1.00 8.79 C ANISOU 1550 CB GLN A 195 1099 164 249 1100 1138 -171 C ATOM 1551 CG GLN A 195 -1.736 16.745 11.741 1.00 9.81 C ANISOU 1551 CG GLN A 195 1324 44 -84 1240 1162 -352 C ATOM 1552 CD GLN A 195 -2.658 16.501 10.545 1.00 8.52 C ANISOU 1552 CD GLN A 195 899 289 205 1005 1330 -200 C ATOM 1553 OE1 GLN A 195 -2.230 16.656 9.382 1.00 11.46 O ANISOU 1553 OE1 GLN A 195 1756 212 157 1582 1015 -54 O ATOM 1554 NE2 GLN A 195 -3.928 16.242 10.815 1.00 13.08 N ANISOU 1554 NE2 GLN A 195 854 -73 11 2148 1967 285 N ATOM 1555 N VAL A 196 1.885 18.630 12.940 1.00 10.27 N ANISOU 1555 N VAL A 196 1291 -82 235 1206 1404 74 N ATOM 1556 CA VAL A 196 2.296 19.917 13.533 1.00 10.15 C ANISOU 1556 CA VAL A 196 1284 -133 97 1226 1345 31 C ATOM 1557 C VAL A 196 2.640 20.899 12.424 1.00 10.76 C ANISOU 1557 C VAL A 196 1402 -94 -38 1255 1429 -12 C ATOM 1558 O VAL A 196 3.213 20.521 11.405 1.00 10.78 O ANISOU 1558 O VAL A 196 1414 -215 -218 1269 1412 -2 O ATOM 1559 CB VAL A 196 3.527 19.702 14.481 1.00 10.76 C ANISOU 1559 CB VAL A 196 1314 -223 75 1229 1543 73 C ATOM 1560 CG1 VAL A 196 3.837 20.945 15.309 1.00 12.71 C ANISOU 1560 CG1 VAL A 196 1589 -63 -46 1472 1765 -280 C ATOM 1561 CG2 VAL A 196 3.300 18.534 15.411 1.00 12.05 C ANISOU 1561 CG2 VAL A 196 1022 -76 263 1685 1870 -234 C ATOM 1562 N THR A 197 2.314 22.175 12.653 1.00 11.27 N ANISOU 1562 N THR A 197 1498 -93 151 1284 1499 6 N ATOM 1563 CA THR A 197 2.767 23.244 11.794 1.00 11.04 C ANISOU 1563 CA THR A 197 1513 -79 134 1210 1472 16 C ATOM 1564 C THR A 197 3.703 24.164 12.539 1.00 12.13 C ANISOU 1564 C THR A 197 1637 -50 95 1359 1612 -124 C ATOM 1565 O THR A 197 3.650 24.305 13.785 1.00 12.47 O ANISOU 1565 O THR A 197 1622 -75 158 1382 1735 -211 O ATOM 1566 CB THR A 197 1.612 24.080 11.274 1.00 10.02 C ANISOU 1566 CB THR A 197 1352 -134 200 1189 1265 -198 C ATOM 1567 OG1 THR A 197 0.780 24.473 12.377 1.00 12.01 O ANISOU 1567 OG1 THR A 197 1889 -11 -72 1270 1405 190 O ATOM 1568 CG2 THR A 197 0.789 23.368 10.217 1.00 11.93 C ANISOU 1568 CG2 THR A 197 1449 -1 169 1723 1360 -22 C ATOM 1569 N ASN A 198 4.589 24.813 11.766 1.00 12.46 N ANISOU 1569 N ASN A 198 1764 -262 120 1364 1605 -290 N ATOM 1570 CA ASN A 198 5.407 25.869 12.296 1.00 14.28 C ANISOU 1570 CA ASN A 198 1950 -225 -14 1483 1993 -237 C ATOM 1571 C ASN A 198 4.962 27.204 11.729 1.00 14.58 C ANISOU 1571 C ASN A 198 1979 -157 -5 1469 2089 -305 C ATOM 1572 O ASN A 198 3.988 27.248 10.964 1.00 14.21 O ANISOU 1572 O ASN A 198 1948 -166 146 1330 2118 -406 O ATOM 1573 CB ASN A 198 6.876 25.535 12.058 1.00 13.58 C ANISOU 1573 CB ASN A 198 1791 -172 -44 1412 1958 -293 C ATOM 1574 CG ASN A 198 7.265 25.478 10.599 1.00 14.08 C ANISOU 1574 CG ASN A 198 1600 -575 -139 1488 2261 -53 C ATOM 1575 OD1 ASN A 198 6.603 26.034 9.737 1.00 15.35 O ANISOU 1575 OD1 ASN A 198 1559 -106 570 1741 2532 238 O ATOM 1576 ND2 ASN A 198 8.395 24.793 10.318 1.00 15.19 N ANISOU 1576 ND2 ASN A 198 1494 -227 -204 1702 2575 302 N ATOM 1577 N LYS A 199 5.649 28.279 12.101 1.00 15.95 N ANISOU 1577 N LYS A 199 2077 -166 119 1509 2474 -214 N ATOM 1578 CA LYS A 199 5.245 29.631 11.676 1.00 17.19 C ANISOU 1578 CA LYS A 199 2434 -195 126 1669 2428 -301 C ATOM 1579 C LYS A 199 5.536 29.908 10.189 1.00 17.73 C ANISOU 1579 C LYS A 199 2470 -107 144 1748 2518 -219 C ATOM 1580 O LYS A 199 5.022 30.893 9.614 1.00 19.98 O ANISOU 1580 O LYS A 199 2945 -83 294 1816 2829 -190 O ATOM 1581 CB LYS A 199 5.898 30.674 12.582 1.00 18.84 C ANISOU 1581 CB LYS A 199 2714 -221 129 1692 2753 -274 C ATOM 1582 CG LYS A 199 5.398 30.576 13.987 1.00 19.74 C ANISOU 1582 CG LYS A 199 2973 -314 27 1849 2678 -390 C ATOM 1583 CD LYS A 199 3.964 31.096 14.062 1.00 23.16 C ANISOU 1583 CD LYS A 199 3087 -200 192 2645 3066 -406 C ATOM 1584 CE LYS A 199 3.336 31.123 15.481 1.00 25.77 C ANISOU 1584 CE LYS A 199 3965 -193 43 2135 3692 -446 C ATOM 1585 NZ LYS A 199 3.730 32.257 16.233 1.00 31.68 N ANISOU 1585 NZ LYS A 199 4368 -31 -190 3458 4210 -968 N ATOM 1586 N LYS A 200 6.326 29.038 9.569 1.00 16.54 N ANISOU 1586 N LYS A 200 2244 -308 112 1538 2501 -262 N ATOM 1587 CA LYS A 200 6.553 29.039 8.131 1.00 17.29 C ANISOU 1587 CA LYS A 200 2325 -114 217 1851 2393 -45 C ATOM 1588 C LYS A 200 5.499 28.239 7.361 1.00 15.71 C ANISOU 1588 C LYS A 200 2030 -121 259 1803 2134 -51 C ATOM 1589 O LYS A 200 5.531 28.145 6.105 1.00 16.16 O ANISOU 1589 O LYS A 200 2220 -265 240 1743 2175 284 O ATOM 1590 CB LYS A 200 7.918 28.460 7.839 1.00 18.43 C ANISOU 1590 CB LYS A 200 2405 -252 263 2128 2470 -27 C ATOM 1591 CG LYS A 200 9.015 29.356 8.304 1.00 23.06 C ANISOU 1591 CG LYS A 200 2955 -151 89 2974 2832 14 C ATOM 1592 CD LYS A 200 10.295 28.698 8.100 1.00 28.46 C ANISOU 1592 CD LYS A 200 3503 -148 -1 3660 3648 -167 C ATOM 1593 CE LYS A 200 11.438 29.570 8.532 1.00 34.01 C ANISOU 1593 CE LYS A 200 4031 32 151 4561 4328 20 C ATOM 1594 NZ LYS A 200 12.636 28.748 8.448 1.00 40.06 N ANISOU 1594 NZ LYS A 200 4527 176 334 5479 5215 -48 N ATOM 1595 N LYS A 201 4.522 27.713 8.102 1.00 15.09 N ANISOU 1595 N LYS A 201 1906 -16 323 1543 2281 -5 N ATOM 1596 CA LYS A 201 3.388 26.981 7.565 1.00 14.73 C ANISOU 1596 CA LYS A 201 1982 -16 145 1499 2113 -89 C ATOM 1597 C LYS A 201 3.790 25.619 6.952 1.00 14.80 C ANISOU 1597 C LYS A 201 1849 -4 87 1574 2200 -101 C ATOM 1598 O LYS A 201 3.035 25.036 6.134 1.00 15.47 O ANISOU 1598 O LYS A 201 1964 116 -172 1578 2337 -280 O ATOM 1599 CB LYS A 201 2.525 27.804 6.566 1.00 14.90 C ANISOU 1599 CB LYS A 201 1893 43 112 1638 2129 38 C ATOM 1600 CG LYS A 201 2.138 29.191 7.034 1.00 16.80 C ANISOU 1600 CG LYS A 201 2150 33 282 1953 2279 -165 C ATOM 1601 CD LYS A 201 1.159 29.849 6.083 1.00 16.77 C ANISOU 1601 CD LYS A 201 2451 -5 327 1784 2134 -106 C ATOM 1602 CE LYS A 201 0.738 31.212 6.608 1.00 17.66 C ANISOU 1602 CE LYS A 201 2494 -132 200 2060 2154 -201 C ATOM 1603 NZ LYS A 201 -0.245 31.961 5.714 1.00 21.08 N ANISOU 1603 NZ LYS A 201 3124 314 736 2305 2579 -55 N ATOM 1604 N GLN A 202 4.953 25.117 7.367 1.00 14.03 N ANISOU 1604 N GLN A 202 1669 -116 138 1551 2111 34 N ATOM 1605 CA GLN A 202 5.342 23.768 7.046 1.00 13.67 C ANISOU 1605 CA GLN A 202 1699 -175 184 1573 1922 80 C ATOM 1606 C GLN A 202 4.617 22.808 7.988 1.00 12.71 C ANISOU 1606 C GLN A 202 1618 -133 179 1630 1580 70 C ATOM 1607 O GLN A 202 4.370 23.123 9.155 1.00 13.45 O ANISOU 1607 O GLN A 202 1709 -332 8 1413 1985 311 O ATOM 1608 CB GLN A 202 6.825 23.553 7.193 1.00 14.44 C ANISOU 1608 CB GLN A 202 1736 -259 177 1716 2034 171 C ATOM 1609 CG GLN A 202 7.656 24.462 6.293 1.00 14.70 C ANISOU 1609 CG GLN A 202 1786 -188 530 1895 1905 191 C ATOM 1610 CD GLN A 202 9.148 24.395 6.612 1.00 14.26 C ANISOU 1610 CD GLN A 202 1594 -509 23 1913 1911 53 C ATOM 1611 OE1 GLN A 202 9.578 24.777 7.708 1.00 16.92 O ANISOU 1611 OE1 GLN A 202 2129 -461 -65 2351 1946 -86 O ATOM 1612 NE2 GLN A 202 9.924 23.922 5.655 1.00 19.24 N ANISOU 1612 NE2 GLN A 202 2034 -393 255 2814 2459 -134 N ATOM 1613 N VAL A 203 4.304 21.619 7.464 1.00 11.77 N ANISOU 1613 N VAL A 203 1652 -92 218 1482 1338 -69 N ATOM 1614 CA VAL A 203 3.711 20.545 8.252 1.00 11.43 C ANISOU 1614 CA VAL A 203 1503 -113 103 1508 1329 30 C ATOM 1615 C VAL A 203 4.732 19.399 8.435 1.00 10.01 C ANISOU 1615 C VAL A 203 1329 0 91 1462 1011 -88 C ATOM 1616 O VAL A 203 5.571 19.131 7.594 1.00 11.95 O ANISOU 1616 O VAL A 203 1466 -104 199 1771 1302 -11 O ATOM 1617 CB VAL A 203 2.413 20.021 7.643 1.00 12.54 C ANISOU 1617 CB VAL A 203 1595 -93 3 1804 1363 0 C ATOM 1618 CG1 VAL A 203 2.654 19.261 6.348 1.00 14.02 C ANISOU 1618 CG1 VAL A 203 2130 -36 69 1597 1598 266 C ATOM 1619 CG2 VAL A 203 1.651 19.185 8.668 1.00 13.15 C ANISOU 1619 CG2 VAL A 203 1761 -201 41 1569 1665 -15 C ATOM 1620 N PHE A 204 4.669 18.742 9.587 1.00 10.66 N ANISOU 1620 N PHE A 204 1427 -10 234 1366 1258 175 N ATOM 1621 CA PHE A 204 5.519 17.608 9.899 1.00 9.67 C ANISOU 1621 CA PHE A 204 1325 -2 125 1166 1182 38 C ATOM 1622 C PHE A 204 4.824 16.785 10.967 1.00 9.67 C ANISOU 1622 C PHE A 204 1383 -6 44 1195 1096 -57 C ATOM 1623 O PHE A 204 3.856 17.230 11.592 1.00 11.24 O ANISOU 1623 O PHE A 204 1591 -26 283 1234 1445 237 O ATOM 1624 CB PHE A 204 6.926 18.045 10.345 1.00 10.97 C ANISOU 1624 CB PHE A 204 1574 -94 243 1209 1385 33 C ATOM 1625 CG PHE A 204 6.941 18.995 11.467 1.00 11.20 C ANISOU 1625 CG PHE A 204 1444 -113 296 1279 1533 97 C ATOM 1626 CD1 PHE A 204 7.144 18.560 12.757 1.00 11.25 C ANISOU 1626 CD1 PHE A 204 1387 129 99 1611 1275 -15 C ATOM 1627 CD2 PHE A 204 6.704 20.347 11.259 1.00 12.71 C ANISOU 1627 CD2 PHE A 204 1875 -295 171 1174 1778 -259 C ATOM 1628 CE1 PHE A 204 7.130 19.481 13.827 1.00 11.71 C ANISOU 1628 CE1 PHE A 204 1691 -115 307 1286 1472 0 C ATOM 1629 CE2 PHE A 204 6.659 21.237 12.321 1.00 13.87 C ANISOU 1629 CE2 PHE A 204 2307 -4 301 1338 1624 -330 C ATOM 1630 CZ PHE A 204 6.882 20.817 13.586 1.00 12.84 C ANISOU 1630 CZ PHE A 204 1686 -10 19 1606 1585 -56 C ATOM 1631 N SER A 205 5.305 15.572 11.139 1.00 9.03 N ANISOU 1631 N SER A 205 1096 72 183 1192 1141 -191 N ATOM 1632 CA SER A 205 4.764 14.619 12.113 1.00 8.67 C ANISOU 1632 CA SER A 205 1119 80 268 1138 1034 -243 C ATOM 1633 C SER A 205 5.685 14.442 13.331 1.00 9.81 C ANISOU 1633 C SER A 205 1131 27 188 1400 1194 -269 C ATOM 1634 O SER A 205 6.907 14.508 13.231 1.00 10.00 O ANISOU 1634 O SER A 205 1233 42 282 1219 1346 -249 O ATOM 1635 CB SER A 205 4.476 13.266 11.450 1.00 9.11 C ANISOU 1635 CB SER A 205 1136 -218 225 1359 964 -392 C ATOM 1636 OG SER A 205 3.486 13.407 10.422 1.00 9.80 O ANISOU 1636 OG SER A 205 1063 -141 94 1818 841 -384 O ATOM 1637 N LYS A 206 5.042 14.234 14.477 1.00 9.45 N ANISOU 1637 N LYS A 206 967 70 368 1364 1256 -195 N ATOM 1638 CA LYS A 206 5.706 14.009 15.742 1.00 9.96 C ANISOU 1638 CA LYS A 206 1319 -71 181 1283 1182 -169 C ATOM 1639 C LYS A 206 4.947 12.911 16.505 1.00 9.44 C ANISOU 1639 C LYS A 206 1229 -102 81 1196 1161 -152 C ATOM 1640 O LYS A 206 3.809 12.554 16.139 1.00 10.16 O ANISOU 1640 O LYS A 206 1217 -303 112 1311 1332 -169 O ATOM 1641 CB LYS A 206 5.662 15.280 16.613 1.00 10.31 C ANISOU 1641 CB LYS A 206 1354 -130 110 1306 1257 -207 C ATOM 1642 CG LYS A 206 6.275 16.498 16.036 1.00 13.55 C ANISOU 1642 CG LYS A 206 1819 19 148 1640 1689 -293 C ATOM 1643 CD LYS A 206 7.751 16.487 16.143 1.00 14.82 C ANISOU 1643 CD LYS A 206 2025 90 543 1839 1767 -416 C ATOM 1644 CE LYS A 206 8.222 16.852 17.582 1.00 13.04 C ANISOU 1644 CE LYS A 206 1913 202 145 1393 1649 -523 C ATOM 1645 NZ LYS A 206 9.746 16.826 17.665 1.00 12.86 N ANISOU 1645 NZ LYS A 206 1118 -155 -184 2208 1560 -802 N ATOM 1646 N ILE A 207 5.593 12.409 17.554 1.00 9.22 N ANISOU 1646 N ILE A 207 1296 3 118 1073 1133 -141 N ATOM 1647 CA ILE A 207 4.935 11.479 18.482 1.00 9.76 C ANISOU 1647 CA ILE A 207 1365 86 80 1269 1073 -155 C ATOM 1648 C ILE A 207 4.632 12.325 19.752 1.00 9.91 C ANISOU 1648 C ILE A 207 1332 -43 37 1321 1111 -98 C ATOM 1649 O ILE A 207 5.501 13.023 20.300 1.00 10.53 O ANISOU 1649 O ILE A 207 1389 -137 -43 1489 1121 -136 O ATOM 1650 CB ILE A 207 5.892 10.307 18.845 1.00 9.80 C ANISOU 1650 CB ILE A 207 1415 162 -68 1275 1033 -193 C ATOM 1651 CG1 ILE A 207 6.074 9.338 17.675 1.00 12.50 C ANISOU 1651 CG1 ILE A 207 1697 289 98 1654 1397 135 C ATOM 1652 CG2 ILE A 207 5.321 9.592 20.029 1.00 11.18 C ANISOU 1652 CG2 ILE A 207 1779 534 -10 1462 1007 -27 C ATOM 1653 CD1 ILE A 207 4.854 8.847 17.032 1.00 12.71 C ANISOU 1653 CD1 ILE A 207 1742 476 -384 2113 974 -403 C ATOM 1654 N PHE A 208 3.380 12.253 20.191 1.00 10.35 N ANISOU 1654 N PHE A 208 1113 -275 -45 1393 1428 -105 N ATOM 1655 CA PHE A 208 2.823 12.980 21.326 1.00 9.15 C ANISOU 1655 CA PHE A 208 1081 -131 33 1375 1020 -120 C ATOM 1656 C PHE A 208 2.266 11.936 22.279 1.00 9.49 C ANISOU 1656 C PHE A 208 1233 -148 -54 1341 1030 -217 C ATOM 1657 O PHE A 208 1.390 11.156 21.918 1.00 9.76 O ANISOU 1657 O PHE A 208 1207 -146 191 1361 1141 -163 O ATOM 1658 CB PHE A 208 1.762 13.908 20.783 1.00 10.87 C ANISOU 1658 CB PHE A 208 1444 -17 -58 1470 1213 -98 C ATOM 1659 CG PHE A 208 1.061 14.772 21.804 1.00 11.22 C ANISOU 1659 CG PHE A 208 1501 -156 123 1443 1316 36 C ATOM 1660 CD1 PHE A 208 -0.307 14.628 22.041 1.00 9.96 C ANISOU 1660 CD1 PHE A 208 1402 -69 46 1418 963 -398 C ATOM 1661 CD2 PHE A 208 1.752 15.768 22.489 1.00 10.92 C ANISOU 1661 CD2 PHE A 208 1210 65 -158 1673 1265 -197 C ATOM 1662 CE1 PHE A 208 -0.966 15.432 22.934 1.00 13.17 C ANISOU 1662 CE1 PHE A 208 1618 -112 8 1849 1535 152 C ATOM 1663 CE2 PHE A 208 1.063 16.625 23.380 1.00 11.37 C ANISOU 1663 CE2 PHE A 208 1599 -123 -102 1513 1204 -196 C ATOM 1664 CZ PHE A 208 -0.276 16.443 23.611 1.00 11.53 C ANISOU 1664 CZ PHE A 208 1526 163 -19 1485 1367 53 C ATOM 1665 N TYR A 209 2.840 11.832 23.492 1.00 9.89 N ANISOU 1665 N TYR A 209 1253 -317 -146 1345 1160 -423 N ATOM 1666 CA TYR A 209 2.520 10.684 24.325 1.00 9.71 C ANISOU 1666 CA TYR A 209 1225 -169 -81 1408 1054 -265 C ATOM 1667 C TYR A 209 2.345 11.011 25.765 1.00 9.94 C ANISOU 1667 C TYR A 209 1258 -134 -121 1377 1142 -269 C ATOM 1668 O TYR A 209 2.823 12.017 26.230 1.00 10.58 O ANISOU 1668 O TYR A 209 1574 -239 -183 1647 797 -317 O ATOM 1669 CB TYR A 209 3.584 9.589 24.169 1.00 11.15 C ANISOU 1669 CB TYR A 209 1415 -198 -88 1593 1229 -364 C ATOM 1670 CG TYR A 209 4.988 9.929 24.653 1.00 11.61 C ANISOU 1670 CG TYR A 209 1506 -132 -160 1378 1527 -101 C ATOM 1671 CD1 TYR A 209 5.864 10.678 23.881 1.00 12.87 C ANISOU 1671 CD1 TYR A 209 1772 -287 -39 1560 1557 -75 C ATOM 1672 CD2 TYR A 209 5.434 9.507 25.887 1.00 10.97 C ANISOU 1672 CD2 TYR A 209 1114 -6 345 1731 1322 6 C ATOM 1673 CE1 TYR A 209 7.124 10.980 24.350 1.00 13.21 C ANISOU 1673 CE1 TYR A 209 1556 -314 88 1938 1523 -140 C ATOM 1674 CE2 TYR A 209 6.709 9.792 26.356 1.00 12.16 C ANISOU 1674 CE2 TYR A 209 1414 -355 45 2157 1050 -508 C ATOM 1675 CZ TYR A 209 7.553 10.517 25.585 1.00 12.77 C ANISOU 1675 CZ TYR A 209 1113 -340 86 2149 1587 -454 C ATOM 1676 OH TYR A 209 8.833 10.823 26.018 1.00 16.10 O ANISOU 1676 OH TYR A 209 1540 -118 479 2590 1986 -759 O ATOM 1677 N SER A 210 1.688 10.118 26.472 1.00 11.43 N ANISOU 1677 N SER A 210 1513 -78 -157 1537 1291 -143 N ATOM 1678 CA SER A 210 1.432 10.254 27.894 1.00 11.05 C ANISOU 1678 CA SER A 210 1473 -41 -158 1602 1122 -201 C ATOM 1679 C SER A 210 1.763 8.994 28.662 1.00 11.72 C ANISOU 1679 C SER A 210 1513 34 -92 1707 1233 -272 C ATOM 1680 O SER A 210 1.335 7.931 28.318 1.00 12.90 O ANISOU 1680 O SER A 210 1796 -12 -64 1832 1272 -504 O ATOM 1681 CB SER A 210 -0.036 10.611 28.180 1.00 11.63 C ANISOU 1681 CB SER A 210 1437 244 -203 1739 1242 -290 C ATOM 1682 OG SER A 210 -0.240 10.751 29.607 1.00 11.49 O ANISOU 1682 OG SER A 210 1682 172 -378 1850 831 -278 O ATOM 1683 N GLU A 211 2.482 9.173 29.764 1.00 11.75 N ANISOU 1683 N GLU A 211 1738 -64 -55 1637 1086 -320 N ATOM 1684 CA GLU A 211 2.893 8.072 30.647 1.00 12.19 C ANISOU 1684 CA GLU A 211 1631 105 5 1839 1159 -272 C ATOM 1685 C GLU A 211 2.002 7.916 31.872 1.00 13.49 C ANISOU 1685 C GLU A 211 1868 117 75 1923 1331 -280 C ATOM 1686 O GLU A 211 2.240 7.015 32.682 1.00 14.22 O ANISOU 1686 O GLU A 211 2048 83 195 2202 1151 -226 O ATOM 1687 CB GLU A 211 4.313 8.377 31.130 1.00 13.03 C ANISOU 1687 CB GLU A 211 1697 81 154 2027 1227 -425 C ATOM 1688 CG GLU A 211 5.353 8.432 30.001 1.00 14.26 C ANISOU 1688 CG GLU A 211 1787 -93 142 2233 1395 -352 C ATOM 1689 CD GLU A 211 6.736 8.907 30.433 1.00 15.02 C ANISOU 1689 CD GLU A 211 1650 -4 -296 2483 1573 -327 C ATOM 1690 OE1 GLU A 211 6.818 9.658 31.420 1.00 21.41 O ANISOU 1690 OE1 GLU A 211 2559 -437 -233 3694 1882 -273 O ATOM 1691 OE2 GLU A 211 7.732 8.605 29.753 1.00 20.75 O ANISOU 1691 OE2 GLU A 211 1656 -319 -326 3812 2417 -259 O ATOM 1692 N ASP A 212 1.002 8.800 32.018 1.00 13.42 N ANISOU 1692 N ASP A 212 1976 116 -56 1987 1135 -141 N ATOM 1693 CA ASP A 212 0.199 8.899 33.241 1.00 13.97 C ANISOU 1693 CA ASP A 212 1988 50 -63 2022 1298 -126 C ATOM 1694 C ASP A 212 -1.281 9.038 32.932 1.00 13.18 C ANISOU 1694 C ASP A 212 1855 68 5 1861 1289 -44 C ATOM 1695 O ASP A 212 -2.022 9.740 33.597 1.00 13.84 O ANISOU 1695 O ASP A 212 1908 107 -127 2083 1265 -20 O ATOM 1696 CB ASP A 212 0.704 10.080 34.083 1.00 14.19 C ANISOU 1696 CB ASP A 212 2301 -120 -40 2048 1041 -34 C ATOM 1697 CG ASP A 212 0.633 11.430 33.340 1.00 15.60 C ANISOU 1697 CG ASP A 212 2338 -43 187 2079 1509 -445 C ATOM 1698 OD1 ASP A 212 1.193 12.438 33.898 1.00 18.38 O ANISOU 1698 OD1 ASP A 212 2562 -132 138 2458 1963 -53 O ATOM 1699 OD2 ASP A 212 -0.013 11.579 32.250 1.00 13.32 O ANISOU 1699 OD2 ASP A 212 2010 40 171 2086 963 -600 O ATOM 1700 N GLU A 213 -1.722 8.251 31.965 1.00 12.99 N ANISOU 1700 N GLU A 213 1753 209 -42 1897 1285 -34 N ATOM 1701 CA GLU A 213 -3.144 8.067 31.672 1.00 13.88 C ANISOU 1701 CA GLU A 213 1898 185 63 1904 1472 -61 C ATOM 1702 C GLU A 213 -3.745 9.353 31.166 1.00 13.67 C ANISOU 1702 C GLU A 213 1847 179 64 1968 1379 -61 C ATOM 1703 O GLU A 213 -4.965 9.604 31.279 1.00 15.18 O ANISOU 1703 O GLU A 213 1972 189 86 2125 1669 299 O ATOM 1704 CB GLU A 213 -3.907 7.492 32.875 1.00 12.83 C ANISOU 1704 CB GLU A 213 1640 306 315 1885 1347 -95 C ATOM 1705 CG GLU A 213 -3.130 6.478 33.710 1.00 14.69 C ANISOU 1705 CG GLU A 213 2091 304 275 2135 1354 7 C ATOM 1706 CD GLU A 213 -2.506 5.361 32.921 1.00 14.54 C ANISOU 1706 CD GLU A 213 2316 336 576 1654 1552 -222 C ATOM 1707 OE1 GLU A 213 -3.165 4.902 31.954 1.00 16.00 O ANISOU 1707 OE1 GLU A 213 2896 -55 150 1898 1285 15 O ATOM 1708 OE2 GLU A 213 -1.340 4.942 33.306 1.00 17.27 O ANISOU 1708 OE2 GLU A 213 2857 283 572 1814 1891 112 O ATOM 1709 N GLY A 214 -2.917 10.165 30.519 1.00 13.25 N ANISOU 1709 N GLY A 214 1655 193 84 1825 1553 -15 N ATOM 1710 CA GLY A 214 -3.461 11.355 29.869 1.00 13.07 C ANISOU 1710 CA GLY A 214 1835 186 80 1731 1397 -58 C ATOM 1711 C GLY A 214 -3.447 12.648 30.649 1.00 13.77 C ANISOU 1711 C GLY A 214 2044 182 99 1700 1485 -72 C ATOM 1712 O GLY A 214 -3.915 13.703 30.166 1.00 13.86 O ANISOU 1712 O GLY A 214 1855 305 121 1765 1646 258 O ATOM 1713 N LYS A 215 -2.898 12.596 31.846 1.00 14.21 N ANISOU 1713 N LYS A 215 2234 33 57 1640 1525 -100 N ATOM 1714 CA LYS A 215 -2.789 13.811 32.640 1.00 14.75 C ANISOU 1714 CA LYS A 215 2227 -12 -40 1827 1549 -45 C ATOM 1715 C LYS A 215 -1.736 14.812 32.097 1.00 15.54 C ANISOU 1715 C LYS A 215 2257 32 -36 1918 1729 18 C ATOM 1716 O LYS A 215 -2.020 16.042 31.989 1.00 16.91 O ANISOU 1716 O LYS A 215 2327 174 -77 2158 1941 42 O ATOM 1717 CB LYS A 215 -2.532 13.439 34.102 1.00 18.46 C ANISOU 1717 CB LYS A 215 2605 -83 -20 2405 2003 -22 C ATOM 1718 CG LYS A 215 -3.646 12.597 34.721 1.00 27.38 C ANISOU 1718 CG LYS A 215 3508 -43 89 3517 3377 -25 C ATOM 1719 CD LYS A 215 -5.114 12.922 34.148 1.00 34.83 C ANISOU 1719 CD LYS A 215 4283 -217 324 4662 4288 0 C ATOM 1720 CE LYS A 215 -6.222 12.117 34.790 1.00 34.60 C ANISOU 1720 CE LYS A 215 4074 -262 168 4904 4166 -122 C ATOM 1721 NZ LYS A 215 -7.341 12.057 33.799 1.00 39.24 N ANISOU 1721 NZ LYS A 215 4654 -103 -44 5559 4694 -256 N ATOM 1722 N THR A 216 -0.550 14.289 31.739 1.00 14.08 N ANISOU 1722 N THR A 216 1922 -21 60 1800 1626 -59 N ATOM 1723 CA THR A 216 0.468 15.089 31.112 1.00 13.57 C ANISOU 1723 CA THR A 216 1841 -59 -64 1887 1426 -84 C ATOM 1724 C THR A 216 0.980 14.423 29.835 1.00 12.87 C ANISOU 1724 C THR A 216 1662 -32 -53 1816 1412 -163 C ATOM 1725 O THR A 216 0.857 13.213 29.642 1.00 12.02 O ANISOU 1725 O THR A 216 1387 -247 -47 1924 1256 -286 O ATOM 1726 CB THR A 216 1.642 15.379 32.035 1.00 14.27 C ANISOU 1726 CB THR A 216 1911 14 21 2096 1412 -164 C ATOM 1727 OG1 THR A 216 2.344 14.167 32.299 1.00 15.25 O ANISOU 1727 OG1 THR A 216 2219 -58 -22 2298 1275 -345 O ATOM 1728 CG2 THR A 216 1.195 15.883 33.397 1.00 17.18 C ANISOU 1728 CG2 THR A 216 2347 -252 -241 2391 1786 -269 C ATOM 1729 N TRP A 217 1.538 15.275 28.965 1.00 11.93 N ANISOU 1729 N TRP A 217 1493 -192 -130 1708 1331 -193 N ATOM 1730 CA TRP A 217 1.953 14.849 27.632 1.00 11.66 C ANISOU 1730 CA TRP A 217 1566 -113 -75 1551 1311 -127 C ATOM 1731 C TRP A 217 3.322 15.397 27.296 1.00 12.44 C ANISOU 1731 C TRP A 217 1664 -137 -98 1651 1409 -373 C ATOM 1732 O TRP A 217 3.702 16.511 27.725 1.00 14.30 O ANISOU 1732 O TRP A 217 1912 -206 -242 1586 1934 -298 O ATOM 1733 CB TRP A 217 0.902 15.333 26.609 1.00 11.73 C ANISOU 1733 CB TRP A 217 1578 -86 -125 1560 1319 -212 C ATOM 1734 CG TRP A 217 -0.457 14.686 26.816 1.00 11.61 C ANISOU 1734 CG TRP A 217 1636 140 192 1333 1441 -91 C ATOM 1735 CD1 TRP A 217 -1.452 15.026 27.733 1.00 12.48 C ANISOU 1735 CD1 TRP A 217 1576 37 -81 1510 1654 -283 C ATOM 1736 CD2 TRP A 217 -0.930 13.542 26.141 1.00 12.93 C ANISOU 1736 CD2 TRP A 217 1561 213 56 1817 1531 -100 C ATOM 1737 NE1 TRP A 217 -2.493 14.132 27.647 1.00 12.86 N ANISOU 1737 NE1 TRP A 217 1661 -116 -128 1831 1394 -186 N ATOM 1738 CE2 TRP A 217 -2.186 13.217 26.662 1.00 12.00 C ANISOU 1738 CE2 TRP A 217 1470 87 -151 1725 1363 -41 C ATOM 1739 CE3 TRP A 217 -0.422 12.754 25.100 1.00 13.01 C ANISOU 1739 CE3 TRP A 217 1822 179 36 1704 1416 -388 C ATOM 1740 CZ2 TRP A 217 -2.872 12.137 26.231 1.00 10.41 C ANISOU 1740 CZ2 TRP A 217 1298 -192 -55 1714 943 -296 C ATOM 1741 CZ3 TRP A 217 -1.117 11.679 24.691 1.00 10.03 C ANISOU 1741 CZ3 TRP A 217 1230 180 -68 1442 1136 -457 C ATOM 1742 CH2 TRP A 217 -2.317 11.371 25.242 1.00 11.93 C ANISOU 1742 CH2 TRP A 217 1448 -131 2 1539 1544 -164 C ATOM 1743 N LYS A 218 4.019 14.618 26.498 1.00 12.11 N ANISOU 1743 N LYS A 218 1527 -101 -134 1720 1351 -418 N ATOM 1744 CA LYS A 218 5.351 14.915 26.001 1.00 14.17 C ANISOU 1744 CA LYS A 218 1966 -106 -155 1951 1467 -191 C ATOM 1745 C LYS A 218 5.439 14.705 24.509 1.00 12.25 C ANISOU 1745 C LYS A 218 1685 -183 -67 1685 1283 -204 C ATOM 1746 O LYS A 218 4.713 13.906 23.938 1.00 13.49 O ANISOU 1746 O LYS A 218 1793 -457 -13 1815 1516 -252 O ATOM 1747 CB LYS A 218 6.371 13.954 26.679 1.00 15.61 C ANISOU 1747 CB LYS A 218 2081 -28 -213 2306 1545 -214 C ATOM 1748 CG LYS A 218 6.420 13.995 28.181 1.00 20.31 C ANISOU 1748 CG LYS A 218 2779 166 -11 2876 2059 -134 C ATOM 1749 CD LYS A 218 7.380 12.956 28.708 1.00 22.27 C ANISOU 1749 CD LYS A 218 3236 115 -157 3084 2141 56 C ATOM 1750 CE LYS A 218 7.259 12.857 30.193 1.00 27.55 C ANISOU 1750 CE LYS A 218 4002 -75 -100 3405 3059 18 C ATOM 1751 NZ LYS A 218 7.395 14.186 30.814 1.00 38.74 N ANISOU 1751 NZ LYS A 218 5353 -203 -85 4932 4434 -199 N ATOM 1752 N PHE A 219 6.335 15.446 23.867 1.00 12.28 N ANISOU 1752 N PHE A 219 1533 -390 -177 1699 1431 -267 N ATOM 1753 CA PHE A 219 6.696 15.195 22.473 1.00 11.77 C ANISOU 1753 CA PHE A 219 1483 -190 -145 1652 1334 -115 C ATOM 1754 C PHE A 219 7.995 14.436 22.374 1.00 12.05 C ANISOU 1754 C PHE A 219 1540 -113 -102 1675 1361 -221 C ATOM 1755 O PHE A 219 8.974 14.784 23.058 1.00 12.15 O ANISOU 1755 O PHE A 219 1366 -104 -261 1954 1295 -452 O ATOM 1756 CB PHE A 219 6.874 16.517 21.760 1.00 12.29 C ANISOU 1756 CB PHE A 219 1705 -171 -103 1671 1291 -110 C ATOM 1757 CG PHE A 219 5.573 17.160 21.367 1.00 10.79 C ANISOU 1757 CG PHE A 219 1389 -141 116 1473 1234 96 C ATOM 1758 CD1 PHE A 219 4.932 18.030 22.218 1.00 12.15 C ANISOU 1758 CD1 PHE A 219 1929 -92 326 1474 1213 -193 C ATOM 1759 CD2 PHE A 219 4.989 16.880 20.131 1.00 11.15 C ANISOU 1759 CD2 PHE A 219 1270 -108 -10 1686 1277 -319 C ATOM 1760 CE1 PHE A 219 3.711 18.633 21.841 1.00 12.86 C ANISOU 1760 CE1 PHE A 219 1899 240 -1 1596 1391 -173 C ATOM 1761 CE2 PHE A 219 3.789 17.455 19.774 1.00 12.67 C ANISOU 1761 CE2 PHE A 219 1781 -491 -125 1670 1362 -113 C ATOM 1762 CZ PHE A 219 3.156 18.328 20.610 1.00 13.36 C ANISOU 1762 CZ PHE A 219 1623 37 -140 1672 1779 -168 C ATOM 1763 N GLY A 220 8.040 13.420 21.522 1.00 11.42 N ANISOU 1763 N GLY A 220 1307 -116 -114 1752 1277 -220 N ATOM 1764 CA GLY A 220 9.332 12.853 21.199 1.00 12.89 C ANISOU 1764 CA GLY A 220 1639 34 -232 1789 1470 -129 C ATOM 1765 C GLY A 220 10.187 13.923 20.513 1.00 12.53 C ANISOU 1765 C GLY A 220 1408 0 -128 1780 1569 -97 C ATOM 1766 O GLY A 220 9.654 14.797 19.759 1.00 12.07 O ANISOU 1766 O GLY A 220 1336 -70 197 1780 1469 -152 O ATOM 1767 N LYS A 221 11.504 13.859 20.707 1.00 13.95 N ANISOU 1767 N LYS A 221 1597 -212 -175 2050 1653 -178 N ATOM 1768 CA LYS A 221 12.397 14.896 20.166 1.00 15.60 C ANISOU 1768 CA LYS A 221 1731 -223 -113 2340 1855 -199 C ATOM 1769 C LYS A 221 12.527 14.926 18.659 1.00 14.42 C ANISOU 1769 C LYS A 221 1703 -323 -135 2005 1767 -205 C ATOM 1770 O LYS A 221 12.784 15.993 18.096 1.00 17.07 O ANISOU 1770 O LYS A 221 2202 -475 -297 2338 1945 84 O ATOM 1771 CB LYS A 221 13.800 14.749 20.783 1.00 17.30 C ANISOU 1771 CB LYS A 221 1869 -191 -78 2645 2057 -227 C ATOM 1772 CG LYS A 221 13.817 14.995 22.292 1.00 21.80 C ANISOU 1772 CG LYS A 221 2238 -330 -50 3431 2612 -415 C ATOM 1773 CD LYS A 221 15.253 14.849 22.876 1.00 23.75 C ANISOU 1773 CD LYS A 221 2552 -103 -149 4053 2416 -536 C ATOM 1774 CE LYS A 221 15.264 14.534 24.383 1.00 31.09 C ANISOU 1774 CE LYS A 221 3417 70 237 4804 3589 -561 C ATOM 1775 NZ LYS A 221 16.547 13.770 24.809 1.00 32.90 N ANISOU 1775 NZ LYS A 221 3582 58 -46 4970 3946 -1217 N ATOM 1776 N GLY A 222 12.344 13.798 17.982 1.00 12.43 N ANISOU 1776 N GLY A 222 1553 -268 -238 1744 1423 -166 N ATOM 1777 CA GLY A 222 12.522 13.734 16.545 1.00 12.74 C ANISOU 1777 CA GLY A 222 1537 -198 -171 1852 1450 -128 C ATOM 1778 C GLY A 222 11.305 14.083 15.743 1.00 11.69 C ANISOU 1778 C GLY A 222 1365 -141 -185 1791 1284 -47 C ATOM 1779 O GLY A 222 10.260 14.350 16.312 1.00 12.19 O ANISOU 1779 O GLY A 222 1437 -134 -346 2040 1151 -208 O ATOM 1780 N ARG A 223 11.419 14.046 14.408 1.00 11.53 N ANISOU 1780 N ARG A 223 1322 -67 -178 1803 1255 -178 N ATOM 1781 CA ARG A 223 10.275 14.315 13.535 1.00 11.03 C ANISOU 1781 CA ARG A 223 1103 -255 -20 1667 1421 -183 C ATOM 1782 C ARG A 223 10.446 13.710 12.186 1.00 10.89 C ANISOU 1782 C ARG A 223 1084 -242 86 1578 1476 -231 C ATOM 1783 O ARG A 223 11.539 13.275 11.839 1.00 11.36 O ANISOU 1783 O ARG A 223 909 -98 40 2118 1288 -490 O ATOM 1784 CB ARG A 223 10.106 15.809 13.342 1.00 11.11 C ANISOU 1784 CB ARG A 223 1332 -124 33 1617 1270 -222 C ATOM 1785 CG ARG A 223 11.296 16.533 12.659 1.00 11.75 C ANISOU 1785 CG ARG A 223 1349 -399 68 1870 1244 -380 C ATOM 1786 CD ARG A 223 10.924 17.930 12.145 1.00 12.69 C ANISOU 1786 CD ARG A 223 1411 -281 -111 1761 1648 -50 C ATOM 1787 NE ARG A 223 12.060 18.725 11.648 1.00 13.51 N ANISOU 1787 NE ARG A 223 1714 -444 -3 1653 1763 -237 N ATOM 1788 CZ ARG A 223 12.558 18.653 10.421 1.00 14.76 C ANISOU 1788 CZ ARG A 223 1643 -648 292 2198 1766 -129 C ATOM 1789 NH1 ARG A 223 12.026 17.855 9.503 1.00 17.56 N ANISOU 1789 NH1 ARG A 223 1560 -810 244 2704 2407 69 N ATOM 1790 NH2 ARG A 223 13.555 19.447 10.079 1.00 16.84 N ANISOU 1790 NH2 ARG A 223 1885 -832 117 2800 1713 -500 N ATOM 1791 N SER A 224 9.344 13.639 11.423 1.00 10.47 N ANISOU 1791 N SER A 224 1024 -118 138 1576 1378 -221 N ATOM 1792 CA SER A 224 9.383 13.321 10.020 1.00 10.99 C ANISOU 1792 CA SER A 224 1252 -41 37 1406 1515 2 C ATOM 1793 C SER A 224 10.031 14.465 9.221 1.00 12.00 C ANISOU 1793 C SER A 224 1248 -76 38 1673 1637 -25 C ATOM 1794 O SER A 224 10.248 15.567 9.734 1.00 12.35 O ANISOU 1794 O SER A 224 1230 -44 -35 1768 1692 -223 O ATOM 1795 CB SER A 224 7.966 13.164 9.497 1.00 10.77 C ANISOU 1795 CB SER A 224 1331 14 97 1378 1380 -115 C ATOM 1796 OG SER A 224 7.313 14.403 9.437 1.00 9.83 O ANISOU 1796 OG SER A 224 1232 160 229 1385 1116 -235 O ATOM 1797 N ALA A 225 10.174 14.210 7.947 1.00 11.60 N ANISOU 1797 N ALA A 225 1372 -224 -52 1468 1565 147 N ATOM 1798 CA ALA A 225 10.407 15.241 6.943 1.00 12.16 C ANISOU 1798 CA ALA A 225 1516 -136 79 1700 1402 83 C ATOM 1799 C ALA A 225 9.242 16.194 6.919 1.00 10.68 C ANISOU 1799 C ALA A 225 1427 -78 133 1393 1236 67 C ATOM 1800 O ALA A 225 8.108 15.836 7.290 1.00 10.88 O ANISOU 1800 O ALA A 225 1248 -244 129 1606 1278 60 O ATOM 1801 CB ALA A 225 10.578 14.607 5.584 1.00 13.23 C ANISOU 1801 CB ALA A 225 1599 -228 35 1977 1449 100 C ATOM 1802 N PHE A 226 9.511 17.425 6.488 1.00 11.11 N ANISOU 1802 N PHE A 226 1229 -102 268 1436 1556 -77 N ATOM 1803 CA PHE A 226 8.425 18.341 6.177 1.00 11.71 C ANISOU 1803 CA PHE A 226 1379 -127 210 1484 1584 63 C ATOM 1804 C PHE A 226 7.600 17.782 5.038 1.00 10.23 C ANISOU 1804 C PHE A 226 1295 60 252 1363 1228 -94 C ATOM 1805 O PHE A 226 8.117 17.105 4.107 1.00 11.97 O ANISOU 1805 O PHE A 226 1429 34 109 1699 1417 -69 O ATOM 1806 CB PHE A 226 8.943 19.734 5.860 1.00 12.81 C ANISOU 1806 CB PHE A 226 1471 -158 176 1531 1864 -14 C ATOM 1807 CG PHE A 226 9.657 20.398 7.021 1.00 14.53 C ANISOU 1807 CG PHE A 226 1906 -283 502 1562 2053 -101 C ATOM 1808 CD1 PHE A 226 10.968 20.784 6.918 1.00 15.88 C ANISOU 1808 CD1 PHE A 226 1789 -324 155 2281 1965 -227 C ATOM 1809 CD2 PHE A 226 9.001 20.697 8.185 1.00 13.73 C ANISOU 1809 CD2 PHE A 226 1499 -474 -56 1838 1878 -339 C ATOM 1810 CE1 PHE A 226 11.598 21.394 7.966 1.00 17.02 C ANISOU 1810 CE1 PHE A 226 1760 -739 -60 2520 2187 -114 C ATOM 1811 CE2 PHE A 226 9.674 21.282 9.289 1.00 14.29 C ANISOU 1811 CE2 PHE A 226 1701 -702 79 1804 1922 -234 C ATOM 1812 CZ PHE A 226 10.968 21.638 9.135 1.00 17.52 C ANISOU 1812 CZ PHE A 226 1780 -573 -63 2514 2360 -214 C ATOM 1813 N GLY A 227 6.331 18.067 5.129 1.00 11.16 N ANISOU 1813 N GLY A 227 1422 -189 158 1527 1292 -26 N ATOM 1814 CA GLY A 227 5.341 17.614 4.153 1.00 9.11 C ANISOU 1814 CA GLY A 227 1226 -41 302 1317 916 -169 C ATOM 1815 C GLY A 227 4.616 16.342 4.556 1.00 9.27 C ANISOU 1815 C GLY A 227 1251 -114 184 1177 1091 -217 C ATOM 1816 O GLY A 227 3.663 15.961 3.917 1.00 10.79 O ANISOU 1816 O GLY A 227 1248 -36 396 1351 1498 -285 O ATOM 1817 N CYS A 228 5.097 15.689 5.614 1.00 9.58 N ANISOU 1817 N CYS A 228 1301 -71 254 1224 1111 -295 N ATOM 1818 CA CYS A 228 4.462 14.477 6.149 1.00 9.32 C ANISOU 1818 CA CYS A 228 1157 -79 205 1205 1178 -223 C ATOM 1819 C CYS A 228 3.382 14.877 7.131 1.00 10.75 C ANISOU 1819 C CYS A 228 1510 -67 177 1337 1234 -188 C ATOM 1820 O CYS A 228 3.674 15.336 8.212 1.00 10.53 O ANISOU 1820 O CYS A 228 1363 -303 51 1424 1212 -214 O ATOM 1821 CB CYS A 228 5.495 13.591 6.861 1.00 9.44 C ANISOU 1821 CB CYS A 228 1224 -129 320 1293 1069 -303 C ATOM 1822 SG CYS A 228 6.775 12.968 5.786 1.00 12.34 S ANISOU 1822 SG CYS A 228 1347 30 82 1613 1725 -299 S ATOM 1823 N SER A 229 2.135 14.688 6.723 1.00 9.95 N ANISOU 1823 N SER A 229 1262 -108 -58 1373 1145 -7 N ATOM 1824 CA SER A 229 0.976 15.085 7.520 1.00 9.96 C ANISOU 1824 CA SER A 229 1172 -44 228 1363 1248 -148 C ATOM 1825 C SER A 229 0.211 13.844 7.961 1.00 10.71 C ANISOU 1825 C SER A 229 1358 41 184 1388 1322 -104 C ATOM 1826 O SER A 229 0.560 12.705 7.630 1.00 10.84 O ANISOU 1826 O SER A 229 1530 176 117 1211 1376 20 O ATOM 1827 CB SER A 229 0.072 16.039 6.739 1.00 11.43 C ANISOU 1827 CB SER A 229 1374 -136 256 1552 1414 -84 C ATOM 1828 OG SER A 229 -0.506 15.334 5.661 1.00 11.03 O ANISOU 1828 OG SER A 229 1271 104 123 1555 1364 -437 O ATOM 1829 N GLU A 230 -0.846 14.127 8.719 1.00 10.05 N ANISOU 1829 N GLU A 230 1239 161 296 1275 1301 -33 N ATOM 1830 CA GLU A 230 -1.886 13.168 9.125 1.00 9.63 C ANISOU 1830 CA GLU A 230 1125 -4 176 1301 1231 -270 C ATOM 1831 C GLU A 230 -1.319 11.751 9.358 1.00 9.47 C ANISOU 1831 C GLU A 230 1084 13 182 1260 1253 -250 C ATOM 1832 O GLU A 230 -1.696 10.778 8.683 1.00 10.62 O ANISOU 1832 O GLU A 230 1543 -96 6 1276 1216 -230 O ATOM 1833 CB GLU A 230 -2.977 13.114 8.049 1.00 10.80 C ANISOU 1833 CB GLU A 230 1142 201 337 1687 1273 -271 C ATOM 1834 CG GLU A 230 -4.319 12.815 8.679 1.00 12.32 C ANISOU 1834 CG GLU A 230 1330 45 541 1774 1576 -219 C ATOM 1835 CD GLU A 230 -5.518 13.009 7.811 1.00 11.81 C ANISOU 1835 CD GLU A 230 1339 -38 -33 1537 1612 -163 C ATOM 1836 OE1 GLU A 230 -5.424 12.728 6.608 1.00 10.72 O ANISOU 1836 OE1 GLU A 230 1112 -201 414 1707 1254 -389 O ATOM 1837 OE2 GLU A 230 -6.605 13.367 8.387 1.00 15.04 O ANISOU 1837 OE2 GLU A 230 1140 179 -370 2008 2563 -292 O ATOM 1838 N PRO A 231 -0.432 11.604 10.310 1.00 8.40 N ANISOU 1838 N PRO A 231 1216 -136 221 1074 901 -285 N ATOM 1839 CA PRO A 231 0.191 10.288 10.495 1.00 8.01 C ANISOU 1839 CA PRO A 231 1012 -145 117 1105 924 -205 C ATOM 1840 C PRO A 231 -0.709 9.278 11.237 1.00 7.80 C ANISOU 1840 C PRO A 231 1066 -72 135 1035 860 -190 C ATOM 1841 O PRO A 231 -1.598 9.714 12.000 1.00 8.97 O ANISOU 1841 O PRO A 231 1128 -306 111 1365 912 186 O ATOM 1842 CB PRO A 231 1.423 10.627 11.364 1.00 7.21 C ANISOU 1842 CB PRO A 231 1128 -245 242 982 629 -263 C ATOM 1843 CG PRO A 231 0.938 11.850 12.182 1.00 8.08 C ANISOU 1843 CG PRO A 231 965 -189 320 1017 1085 -165 C ATOM 1844 CD PRO A 231 0.103 12.639 11.222 1.00 8.40 C ANISOU 1844 CD PRO A 231 1056 28 328 1123 1011 -237 C ATOM 1845 N VAL A 232 -0.462 7.983 11.030 1.00 7.35 N ANISOU 1845 N VAL A 232 1064 -72 42 959 769 -157 N ATOM 1846 CA VAL A 232 -1.150 6.947 11.736 1.00 7.89 C ANISOU 1846 CA VAL A 232 1204 -69 19 855 938 -171 C ATOM 1847 C VAL A 232 -0.029 5.956 12.152 1.00 8.71 C ANISOU 1847 C VAL A 232 1237 -93 -5 1113 956 -125 C ATOM 1848 O VAL A 232 0.929 5.746 11.388 1.00 9.30 O ANISOU 1848 O VAL A 232 1390 -72 -22 1228 915 -59 O ATOM 1849 CB VAL A 232 -2.262 6.294 10.835 1.00 9.24 C ANISOU 1849 CB VAL A 232 1270 -43 240 1308 931 -125 C ATOM 1850 CG1 VAL A 232 -1.698 5.716 9.532 1.00 9.44 C ANISOU 1850 CG1 VAL A 232 987 -73 120 1398 1200 -249 C ATOM 1851 CG2 VAL A 232 -3.073 5.287 11.601 1.00 7.87 C ANISOU 1851 CG2 VAL A 232 1202 -57 260 885 903 -285 C ATOM 1852 N ALA A 233 -0.120 5.400 13.369 1.00 8.73 N ANISOU 1852 N ALA A 233 1256 -70 222 1074 984 -153 N ATOM 1853 CA ALA A 233 0.934 4.602 13.927 1.00 8.48 C ANISOU 1853 CA ALA A 233 1280 -4 103 1011 932 -239 C ATOM 1854 C ALA A 233 0.432 3.349 14.581 1.00 9.84 C ANISOU 1854 C ALA A 233 1279 -6 84 1395 1063 -299 C ATOM 1855 O ALA A 233 -0.648 3.295 15.112 1.00 9.65 O ANISOU 1855 O ALA A 233 1188 139 333 1482 996 -427 O ATOM 1856 CB ALA A 233 1.725 5.427 14.936 1.00 10.51 C ANISOU 1856 CB ALA A 233 1388 44 256 1331 1271 -502 C ATOM 1857 N LEU A 234 1.307 2.363 14.594 1.00 9.62 N ANISOU 1857 N LEU A 234 1257 18 -19 1382 1014 -105 N ATOM 1858 CA LEU A 234 1.143 1.141 15.343 1.00 9.74 C ANISOU 1858 CA LEU A 234 1193 -82 42 1346 1158 -168 C ATOM 1859 C LEU A 234 2.485 0.748 15.990 1.00 10.07 C ANISOU 1859 C LEU A 234 1233 3 93 1364 1227 -194 C ATOM 1860 O LEU A 234 3.519 1.301 15.643 1.00 9.38 O ANISOU 1860 O LEU A 234 1044 -27 258 1229 1289 -334 O ATOM 1861 CB LEU A 234 0.575 0.046 14.442 1.00 8.66 C ANISOU 1861 CB LEU A 234 1021 -65 56 1299 969 -237 C ATOM 1862 CG LEU A 234 1.367 -0.408 13.210 1.00 8.33 C ANISOU 1862 CG LEU A 234 907 -292 174 1337 920 -208 C ATOM 1863 CD1 LEU A 234 2.576 -1.268 13.522 1.00 9.90 C ANISOU 1863 CD1 LEU A 234 973 143 271 1578 1207 -7 C ATOM 1864 CD2 LEU A 234 0.459 -1.152 12.279 1.00 10.53 C ANISOU 1864 CD2 LEU A 234 1275 -225 96 1485 1241 -236 C ATOM 1865 N GLU A 235 2.471 -0.208 16.916 1.00 10.22 N ANISOU 1865 N GLU A 235 1145 152 167 1559 1176 -97 N ATOM 1866 CA GLU A 235 3.688 -0.763 17.465 1.00 10.94 C ANISOU 1866 CA GLU A 235 1353 149 231 1571 1231 -119 C ATOM 1867 C GLU A 235 3.942 -2.141 16.868 1.00 11.83 C ANISOU 1867 C GLU A 235 1431 43 235 1706 1357 -103 C ATOM 1868 O GLU A 235 3.026 -2.996 16.843 1.00 12.93 O ANISOU 1868 O GLU A 235 1260 -52 342 1543 2108 -60 O ATOM 1869 CB GLU A 235 3.559 -0.848 19.014 1.00 11.48 C ANISOU 1869 CB GLU A 235 1222 344 270 1780 1360 -281 C ATOM 1870 CG GLU A 235 4.855 -1.341 19.653 1.00 13.71 C ANISOU 1870 CG GLU A 235 1571 527 202 2376 1260 -212 C ATOM 1871 CD GLU A 235 4.761 -1.556 21.164 1.00 15.93 C ANISOU 1871 CD GLU A 235 1982 535 518 2448 1619 -196 C ATOM 1872 OE1 GLU A 235 5.560 -2.342 21.724 1.00 22.33 O ANISOU 1872 OE1 GLU A 235 3081 895 725 3335 2066 -570 O ATOM 1873 OE2 GLU A 235 3.971 -0.967 21.773 1.00 17.87 O ANISOU 1873 OE2 GLU A 235 2566 956 281 2764 1459 -239 O ATOM 1874 N TRP A 236 5.198 -2.407 16.474 1.00 10.47 N ANISOU 1874 N TRP A 236 1317 -2 160 1400 1262 -208 N ATOM 1875 CA TRP A 236 5.566 -3.636 15.822 1.00 10.94 C ANISOU 1875 CA TRP A 236 1533 115 161 1416 1205 -175 C ATOM 1876 C TRP A 236 6.953 -3.993 16.324 1.00 12.37 C ANISOU 1876 C TRP A 236 1654 207 95 1505 1538 -133 C ATOM 1877 O TRP A 236 7.918 -3.255 16.146 1.00 12.38 O ANISOU 1877 O TRP A 236 1720 174 98 1335 1646 -212 O ATOM 1878 CB TRP A 236 5.611 -3.414 14.315 1.00 9.42 C ANISOU 1878 CB TRP A 236 1195 130 162 1315 1068 -284 C ATOM 1879 CG TRP A 236 5.982 -4.666 13.538 1.00 9.18 C ANISOU 1879 CG TRP A 236 1155 -100 258 1264 1068 -140 C ATOM 1880 CD1 TRP A 236 7.206 -5.039 13.102 1.00 12.36 C ANISOU 1880 CD1 TRP A 236 1743 228 80 1495 1456 41 C ATOM 1881 CD2 TRP A 236 5.090 -5.710 13.135 1.00 8.95 C ANISOU 1881 CD2 TRP A 236 1244 67 113 1159 997 -243 C ATOM 1882 NE1 TRP A 236 7.138 -6.229 12.420 1.00 11.51 N ANISOU 1882 NE1 TRP A 236 1582 163 178 1321 1467 -90 N ATOM 1883 CE2 TRP A 236 5.842 -6.657 12.426 1.00 9.67 C ANISOU 1883 CE2 TRP A 236 1557 -43 309 1209 907 -192 C ATOM 1884 CE3 TRP A 236 3.705 -5.904 13.243 1.00 11.08 C ANISOU 1884 CE3 TRP A 236 1775 34 209 1434 998 -144 C ATOM 1885 CZ2 TRP A 236 5.266 -7.781 11.870 1.00 10.80 C ANISOU 1885 CZ2 TRP A 236 1526 342 108 1371 1205 -89 C ATOM 1886 CZ3 TRP A 236 3.143 -6.989 12.650 1.00 10.81 C ANISOU 1886 CZ3 TRP A 236 1395 81 141 1634 1078 -82 C ATOM 1887 CH2 TRP A 236 3.921 -7.928 11.998 1.00 11.58 C ANISOU 1887 CH2 TRP A 236 1719 98 103 1318 1360 -81 C ATOM 1888 N GLU A 237 7.050 -5.124 16.980 1.00 12.85 N ANISOU 1888 N GLU A 237 1803 85 205 1366 1714 -316 N ATOM 1889 CA GLU A 237 8.356 -5.635 17.430 1.00 14.77 C ANISOU 1889 CA GLU A 237 2114 211 159 1717 1778 -448 C ATOM 1890 C GLU A 237 9.197 -4.565 18.153 1.00 15.69 C ANISOU 1890 C GLU A 237 2086 285 292 1854 2020 -593 C ATOM 1891 O GLU A 237 10.366 -4.373 17.859 1.00 18.60 O ANISOU 1891 O GLU A 237 2488 315 276 1974 2603 -848 O ATOM 1892 CB GLU A 237 9.097 -6.262 16.258 1.00 15.50 C ANISOU 1892 CB GLU A 237 2082 425 253 1754 2052 -470 C ATOM 1893 CG GLU A 237 8.305 -7.451 15.755 1.00 18.05 C ANISOU 1893 CG GLU A 237 2507 394 121 2184 2166 -338 C ATOM 1894 CD GLU A 237 8.905 -8.187 14.574 1.00 22.24 C ANISOU 1894 CD GLU A 237 2854 118 -5 2862 2731 -307 C ATOM 1895 OE1 GLU A 237 9.960 -7.721 14.035 1.00 27.49 O ANISOU 1895 OE1 GLU A 237 2810 214 -340 4455 3179 286 O ATOM 1896 OE2 GLU A 237 8.293 -9.243 14.177 1.00 26.33 O ANISOU 1896 OE2 GLU A 237 3929 84 -666 2541 3535 -530 O ATOM 1897 N GLY A 238 8.541 -3.848 19.049 1.00 16.05 N ANISOU 1897 N GLY A 238 2529 227 240 1789 1778 -924 N ATOM 1898 CA GLY A 238 9.207 -2.923 19.924 1.00 16.07 C ANISOU 1898 CA GLY A 238 2573 153 154 1844 1689 -877 C ATOM 1899 C GLY A 238 9.390 -1.541 19.382 1.00 16.12 C ANISOU 1899 C GLY A 238 2492 -30 -83 1679 1951 -906 C ATOM 1900 O GLY A 238 9.857 -0.665 20.075 1.00 19.43 O ANISOU 1900 O GLY A 238 3068 -102 -191 2361 1953 -1465 O ATOM 1901 N LYS A 239 8.900 -1.309 18.182 1.00 14.07 N ANISOU 1901 N LYS A 239 1952 13 -21 1658 1735 -759 N ATOM 1902 CA LYS A 239 9.086 -0.019 17.550 1.00 15.17 C ANISOU 1902 CA LYS A 239 1981 156 -6 1811 1969 -493 C ATOM 1903 C LYS A 239 7.754 0.564 17.192 1.00 12.64 C ANISOU 1903 C LYS A 239 1645 18 26 1514 1642 -492 C ATOM 1904 O LYS A 239 6.839 -0.156 16.856 1.00 13.31 O ANISOU 1904 O LYS A 239 1675 -38 -258 1396 1985 -625 O ATOM 1905 CB LYS A 239 9.899 -0.146 16.262 1.00 16.47 C ANISOU 1905 CB LYS A 239 1935 201 11 1883 2439 -434 C ATOM 1906 CG LYS A 239 11.268 -0.832 16.409 1.00 20.81 C ANISOU 1906 CG LYS A 239 2368 311 -265 2808 2731 -463 C ATOM 1907 CD LYS A 239 11.774 -1.063 14.996 1.00 24.43 C ANISOU 1907 CD LYS A 239 2960 480 -166 3242 3080 -325 C ATOM 1908 CE LYS A 239 10.942 -2.171 14.207 1.00 33.93 C ANISOU 1908 CE LYS A 239 4323 765 -494 4379 4189 84 C ATOM 1909 NZ LYS A 239 11.835 -3.095 13.294 1.00 35.43 N ANISOU 1909 NZ LYS A 239 4480 690 -435 4491 4488 -149 N ATOM 1910 N LEU A 240 7.665 1.888 17.171 1.00 10.86 N ANISOU 1910 N LEU A 240 1415 61 -12 1392 1316 -495 N ATOM 1911 CA LEU A 240 6.543 2.563 16.495 1.00 10.62 C ANISOU 1911 CA LEU A 240 1522 42 275 1261 1250 -293 C ATOM 1912 C LEU A 240 6.794 2.602 14.990 1.00 11.14 C ANISOU 1912 C LEU A 240 1466 -3 157 1505 1261 -336 C ATOM 1913 O LEU A 240 7.879 2.948 14.537 1.00 11.19 O ANISOU 1913 O LEU A 240 1397 -210 183 1924 927 -452 O ATOM 1914 CB LEU A 240 6.471 3.967 17.061 1.00 11.10 C ANISOU 1914 CB LEU A 240 1344 137 194 1311 1560 -174 C ATOM 1915 CG LEU A 240 6.137 4.102 18.526 1.00 11.82 C ANISOU 1915 CG LEU A 240 1855 -81 -16 1294 1342 -320 C ATOM 1916 CD1 LEU A 240 6.208 5.532 18.995 1.00 14.78 C ANISOU 1916 CD1 LEU A 240 1886 86 -103 1883 1844 -163 C ATOM 1917 CD2 LEU A 240 4.765 3.471 18.858 1.00 12.90 C ANISOU 1917 CD2 LEU A 240 1902 -292 199 1478 1519 -207 C ATOM 1918 N ILE A 241 5.776 2.255 14.228 1.00 9.78 N ANISOU 1918 N ILE A 241 1359 -56 275 1290 1064 -350 N ATOM 1919 CA ILE A 241 5.780 2.378 12.774 1.00 9.86 C ANISOU 1919 CA ILE A 241 1415 65 254 1309 1023 -307 C ATOM 1920 C ILE A 241 4.791 3.481 12.479 1.00 8.91 C ANISOU 1920 C ILE A 241 1136 48 344 1440 808 -268 C ATOM 1921 O ILE A 241 3.625 3.366 12.780 1.00 9.60 O ANISOU 1921 O ILE A 241 1153 -9 87 1537 957 -218 O ATOM 1922 CB ILE A 241 5.426 1.044 12.044 1.00 8.85 C ANISOU 1922 CB ILE A 241 1406 174 228 1173 783 -459 C ATOM 1923 CG1 ILE A 241 6.400 -0.085 12.479 1.00 12.78 C ANISOU 1923 CG1 ILE A 241 2267 30 322 1245 1342 -228 C ATOM 1924 CG2 ILE A 241 5.507 1.299 10.534 1.00 8.98 C ANISOU 1924 CG2 ILE A 241 814 -3 183 1622 975 -337 C ATOM 1925 CD1 ILE A 241 6.262 -1.454 11.723 1.00 16.36 C ANISOU 1925 CD1 ILE A 241 2254 -22 401 2224 1736 -212 C ATOM 1926 N ILE A 242 5.308 4.589 11.941 1.00 8.23 N ANISOU 1926 N ILE A 242 1043 -75 272 1230 853 -378 N ATOM 1927 CA ILE A 242 4.552 5.802 11.782 1.00 8.99 C ANISOU 1927 CA ILE A 242 1117 40 126 1320 976 -259 C ATOM 1928 C ILE A 242 4.404 6.034 10.272 1.00 8.09 C ANISOU 1928 C ILE A 242 942 -2 79 1180 948 -271 C ATOM 1929 O ILE A 242 5.393 6.276 9.524 1.00 7.93 O ANISOU 1929 O ILE A 242 878 -176 194 1390 744 -195 O ATOM 1930 CB ILE A 242 5.294 6.976 12.410 1.00 9.37 C ANISOU 1930 CB ILE A 242 1139 25 102 1526 894 -228 C ATOM 1931 CG1 ILE A 242 5.669 6.705 13.882 1.00 11.83 C ANISOU 1931 CG1 ILE A 242 1819 -150 251 1632 1043 -428 C ATOM 1932 CG2 ILE A 242 4.515 8.240 12.326 1.00 11.20 C ANISOU 1932 CG2 ILE A 242 1756 -222 -54 1572 926 -349 C ATOM 1933 CD1 ILE A 242 7.049 7.158 14.290 1.00 13.42 C ANISOU 1933 CD1 ILE A 242 1796 200 226 1918 1385 -402 C ATOM 1934 N ASN A 243 3.159 5.942 9.807 1.00 7.85 N ANISOU 1934 N ASN A 243 861 -75 200 1258 863 -441 N ATOM 1935 CA ASN A 243 2.814 5.885 8.354 1.00 8.62 C ANISOU 1935 CA ASN A 243 1143 -39 79 1279 850 -185 C ATOM 1936 C ASN A 243 2.167 7.192 8.009 1.00 8.51 C ANISOU 1936 C ASN A 243 986 -113 0 1371 876 -297 C ATOM 1937 O ASN A 243 1.142 7.542 8.567 1.00 9.80 O ANISOU 1937 O ASN A 243 1099 -15 259 1241 1384 -136 O ATOM 1938 CB ASN A 243 1.865 4.684 8.207 1.00 8.40 C ANISOU 1938 CB ASN A 243 989 4 227 1201 1000 -301 C ATOM 1939 CG ASN A 243 1.568 4.289 6.775 1.00 9.51 C ANISOU 1939 CG ASN A 243 1120 -55 31 1301 1191 -205 C ATOM 1940 OD1 ASN A 243 1.550 5.149 5.886 1.00 9.57 O ANISOU 1940 OD1 ASN A 243 1095 -184 221 1192 1346 -501 O ATOM 1941 ND2 ASN A 243 1.324 2.974 6.540 1.00 10.05 N ANISOU 1941 ND2 ASN A 243 951 -147 167 1041 1824 -97 N ATOM 1942 N THR A 244 2.823 7.966 7.144 1.00 8.08 N ANISOU 1942 N THR A 244 889 35 91 1366 815 -151 N ATOM 1943 CA THR A 244 2.460 9.371 6.925 1.00 8.68 C ANISOU 1943 CA THR A 244 1121 -19 211 1232 942 -183 C ATOM 1944 C THR A 244 1.837 9.648 5.567 1.00 8.13 C ANISOU 1944 C THR A 244 845 80 85 1279 965 -143 C ATOM 1945 O THR A 244 2.145 8.984 4.565 1.00 9.46 O ANISOU 1945 O THR A 244 1163 212 -31 1255 1175 -27 O ATOM 1946 CB THR A 244 3.632 10.354 7.106 1.00 8.83 C ANISOU 1946 CB THR A 244 1156 111 173 1203 993 -193 C ATOM 1947 OG1 THR A 244 4.571 10.237 6.041 1.00 9.78 O ANISOU 1947 OG1 THR A 244 1208 99 270 1392 1113 -234 O ATOM 1948 CG2 THR A 244 4.365 10.125 8.380 1.00 9.66 C ANISOU 1948 CG2 THR A 244 1358 65 28 1206 1104 -259 C ATOM 1949 N ARG A 245 0.921 10.631 5.558 1.00 9.08 N ANISOU 1949 N ARG A 245 1086 85 264 1377 984 -32 N ATOM 1950 CA ARG A 245 0.352 11.165 4.341 1.00 8.83 C ANISOU 1950 CA ARG A 245 1033 62 248 1336 983 -126 C ATOM 1951 C ARG A 245 1.333 12.190 3.787 1.00 8.88 C ANISOU 1951 C ARG A 245 1018 55 167 1391 963 -194 C ATOM 1952 O ARG A 245 1.813 13.055 4.500 1.00 10.34 O ANISOU 1952 O ARG A 245 1201 -255 160 1532 1196 -131 O ATOM 1953 CB ARG A 245 -0.952 11.854 4.705 1.00 9.29 C ANISOU 1953 CB ARG A 245 1214 12 294 1226 1089 -191 C ATOM 1954 CG ARG A 245 -1.621 12.714 3.606 1.00 8.56 C ANISOU 1954 CG ARG A 245 941 -126 184 1238 1072 -130 C ATOM 1955 CD ARG A 245 -2.937 13.221 4.028 1.00 8.30 C ANISOU 1955 CD ARG A 245 1102 223 167 1057 993 -190 C ATOM 1956 NE ARG A 245 -3.518 14.115 3.075 1.00 10.25 N ANISOU 1956 NE ARG A 245 1298 383 558 1695 900 94 N ATOM 1957 CZ ARG A 245 -4.750 14.530 3.145 1.00 12.21 C ANISOU 1957 CZ ARG A 245 1463 99 395 1406 1769 45 C ATOM 1958 NH1 ARG A 245 -5.559 14.101 4.071 1.00 12.15 N ANISOU 1958 NH1 ARG A 245 1555 475 383 1608 1451 -217 N ATOM 1959 NH2 ARG A 245 -5.184 15.388 2.273 1.00 12.02 N ANISOU 1959 NH2 ARG A 245 1167 226 348 1782 1617 -4 N ATOM 1960 N VAL A 246 1.556 12.157 2.463 1.00 9.92 N ANISOU 1960 N VAL A 246 1353 83 229 1364 1052 -94 N ATOM 1961 CA VAL A 246 2.317 13.200 1.776 1.00 9.55 C ANISOU 1961 CA VAL A 246 1204 22 297 1379 1042 -265 C ATOM 1962 C VAL A 246 1.519 13.556 0.525 1.00 9.78 C ANISOU 1962 C VAL A 246 1303 3 255 1302 1108 -247 C ATOM 1963 O VAL A 246 1.459 12.804 -0.413 1.00 11.08 O ANISOU 1963 O VAL A 246 1634 54 332 1509 1066 -374 O ATOM 1964 CB VAL A 246 3.715 12.740 1.403 1.00 11.14 C ANISOU 1964 CB VAL A 246 1557 -115 334 1597 1079 -147 C ATOM 1965 CG1 VAL A 246 4.547 13.947 0.883 1.00 13.93 C ANISOU 1965 CG1 VAL A 246 1744 -98 178 1903 1643 130 C ATOM 1966 CG2 VAL A 246 4.405 12.134 2.570 1.00 12.73 C ANISOU 1966 CG2 VAL A 246 1503 146 107 1694 1639 -119 C ATOM 1967 N ASP A 247 0.900 14.720 0.532 1.00 10.90 N ANISOU 1967 N ASP A 247 1456 52 209 1516 1170 -264 N ATOM 1968 CA ASP A 247 0.140 15.145 -0.631 1.00 10.15 C ANISOU 1968 CA ASP A 247 1117 -35 223 1531 1208 -405 C ATOM 1969 C ASP A 247 1.081 15.232 -1.831 1.00 10.33 C ANISOU 1969 C ASP A 247 1135 -3 257 1587 1201 -291 C ATOM 1970 O ASP A 247 2.204 15.742 -1.735 1.00 10.28 O ANISOU 1970 O ASP A 247 1036 -53 292 1772 1096 -410 O ATOM 1971 CB ASP A 247 -0.516 16.479 -0.403 1.00 10.79 C ANISOU 1971 CB ASP A 247 1287 0 240 1709 1104 -366 C ATOM 1972 CG ASP A 247 -1.671 16.419 0.570 1.00 10.56 C ANISOU 1972 CG ASP A 247 828 -16 93 1645 1540 -490 C ATOM 1973 OD1 ASP A 247 -1.988 17.492 1.171 1.00 13.93 O ANISOU 1973 OD1 ASP A 247 1555 279 -90 1804 1932 -285 O ATOM 1974 OD2 ASP A 247 -2.326 15.356 0.771 1.00 10.53 O ANISOU 1974 OD2 ASP A 247 1218 -180 507 1583 1200 -250 O ATOM 1975 N TYR A 248 0.659 14.696 -2.959 1.00 10.98 N ANISOU 1975 N TYR A 248 1411 64 355 1522 1237 -171 N ATOM 1976 CA TYR A 248 1.384 14.795 -4.221 1.00 11.91 C ANISOU 1976 CA TYR A 248 1405 55 445 1615 1502 -97 C ATOM 1977 C TYR A 248 2.679 13.981 -4.296 1.00 12.17 C ANISOU 1977 C TYR A 248 1396 9 509 1785 1443 16 C ATOM 1978 O TYR A 248 3.491 14.205 -5.172 1.00 14.25 O ANISOU 1978 O TYR A 248 1717 60 529 1812 1884 57 O ATOM 1979 CB TYR A 248 1.607 16.266 -4.612 1.00 11.21 C ANISOU 1979 CB TYR A 248 1371 -217 554 1436 1450 -18 C ATOM 1980 CG TYR A 248 0.382 17.119 -4.506 1.00 13.43 C ANISOU 1980 CG TYR A 248 1959 -5 597 1644 1497 107 C ATOM 1981 CD1 TYR A 248 0.217 17.983 -3.471 1.00 16.10 C ANISOU 1981 CD1 TYR A 248 2165 79 509 1758 2194 19 C ATOM 1982 CD2 TYR A 248 -0.643 17.013 -5.433 1.00 15.14 C ANISOU 1982 CD2 TYR A 248 2144 177 517 1696 1911 -29 C ATOM 1983 CE1 TYR A 248 -0.940 18.733 -3.311 1.00 15.73 C ANISOU 1983 CE1 TYR A 248 2241 268 600 1411 2323 -92 C ATOM 1984 CE2 TYR A 248 -1.774 17.784 -5.338 1.00 15.71 C ANISOU 1984 CE2 TYR A 248 2003 -114 565 1626 2340 98 C ATOM 1985 CZ TYR A 248 -1.944 18.632 -4.251 1.00 16.28 C ANISOU 1985 CZ TYR A 248 1810 92 588 1687 2687 -98 C ATOM 1986 OH TYR A 248 -3.097 19.394 -4.128 1.00 18.81 O ANISOU 1986 OH TYR A 248 2690 446 772 1581 2874 250 O ATOM 1987 N ARG A 249 2.840 13.040 -3.364 1.00 11.68 N ANISOU 1987 N ARG A 249 1390 -170 529 1563 1484 15 N ATOM 1988 CA ARG A 249 4.028 12.194 -3.291 1.00 11.44 C ANISOU 1988 CA ARG A 249 1359 -108 281 1697 1288 -193 C ATOM 1989 C ARG A 249 3.669 10.855 -2.699 1.00 11.12 C ANISOU 1989 C ARG A 249 1302 -107 186 1621 1299 -307 C ATOM 1990 O ARG A 249 2.571 10.636 -2.151 1.00 11.03 O ANISOU 1990 O ARG A 249 1281 -61 292 1634 1275 -259 O ATOM 1991 CB ARG A 249 5.114 12.808 -2.415 1.00 12.77 C ANISOU 1991 CB ARG A 249 1522 -224 380 1768 1562 -90 C ATOM 1992 CG ARG A 249 5.552 14.208 -2.681 1.00 15.37 C ANISOU 1992 CG ARG A 249 1708 -214 630 2031 2100 74 C ATOM 1993 CD ARG A 249 6.508 14.320 -3.798 1.00 21.45 C ANISOU 1993 CD ARG A 249 2796 -459 609 2284 3070 317 C ATOM 1994 NE ARG A 249 7.019 15.698 -3.889 1.00 23.40 N ANISOU 1994 NE ARG A 249 2852 -733 703 2359 3680 587 N ATOM 1995 CZ ARG A 249 6.409 16.718 -4.508 1.00 26.96 C ANISOU 1995 CZ ARG A 249 3600 -898 834 2659 3983 298 C ATOM 1996 NH1 ARG A 249 5.245 16.588 -5.158 1.00 27.62 N ANISOU 1996 NH1 ARG A 249 3537 -280 1311 3097 3859 339 N ATOM 1997 NH2 ARG A 249 7.007 17.915 -4.479 1.00 31.82 N ANISOU 1997 NH2 ARG A 249 4297 -667 868 3051 4742 436 N ATOM 1998 N ARG A 250 4.624 9.931 -2.755 1.00 10.81 N ANISOU 1998 N ARG A 250 1313 -99 82 1581 1210 -97 N ATOM 1999 CA ARG A 250 4.457 8.631 -2.115 1.00 10.61 C ANISOU 1999 CA ARG A 250 1238 -157 134 1618 1173 -210 C ATOM 2000 C ARG A 250 4.505 8.733 -0.586 1.00 10.41 C ANISOU 2000 C ARG A 250 1287 -190 122 1474 1194 -226 C ATOM 2001 O ARG A 250 5.180 9.559 -0.035 1.00 11.50 O ANISOU 2001 O ARG A 250 1599 -345 237 1475 1293 -159 O ATOM 2002 CB ARG A 250 5.538 7.664 -2.638 1.00 9.84 C ANISOU 2002 CB ARG A 250 1038 -63 86 1747 952 -294 C ATOM 2003 CG ARG A 250 5.452 7.498 -4.182 1.00 11.19 C ANISOU 2003 CG ARG A 250 1419 -85 -259 1609 1221 -207 C ATOM 2004 CD ARG A 250 6.443 6.500 -4.813 1.00 12.98 C ANISOU 2004 CD ARG A 250 1230 142 131 1980 1719 -48 C ATOM 2005 NE ARG A 250 5.986 5.201 -4.551 1.00 16.41 N ANISOU 2005 NE ARG A 250 1697 250 -85 2427 2111 -267 N ATOM 2006 CZ ARG A 250 4.918 4.636 -5.147 1.00 12.82 C ANISOU 2006 CZ ARG A 250 1329 388 -347 1911 1629 -664 C ATOM 2007 NH1 ARG A 250 4.518 3.534 -4.666 1.00 15.52 N ANISOU 2007 NH1 ARG A 250 1804 -4 84 2432 1658 -280 N ATOM 2008 NH2 ARG A 250 4.369 5.095 -6.262 1.00 16.62 N ANISOU 2008 NH2 ARG A 250 2146 175 525 2171 1997 -399 N ATOM 2009 N ARG A 251 3.732 7.909 0.097 1.00 10.32 N ANISOU 2009 N ARG A 251 1264 -222 260 1548 1109 -264 N ATOM 2010 CA ARG A 251 3.721 7.906 1.540 1.00 9.10 C ANISOU 2010 CA ARG A 251 1021 -98 212 1411 1024 -244 C ATOM 2011 C ARG A 251 5.047 7.454 2.156 1.00 9.25 C ANISOU 2011 C ARG A 251 1180 -113 214 1191 1141 -253 C ATOM 2012 O ARG A 251 5.564 6.381 1.830 1.00 10.01 O ANISOU 2012 O ARG A 251 1015 -24 -101 1358 1429 -320 O ATOM 2013 CB ARG A 251 2.622 6.980 2.061 1.00 8.95 C ANISOU 2013 CB ARG A 251 914 -182 228 1375 1108 -480 C ATOM 2014 CG ARG A 251 1.221 7.370 1.726 1.00 8.45 C ANISOU 2014 CG ARG A 251 635 -250 120 1516 1058 -245 C ATOM 2015 CD ARG A 251 0.205 6.460 2.343 1.00 8.47 C ANISOU 2015 CD ARG A 251 829 -70 350 1280 1109 -339 C ATOM 2016 NE ARG A 251 0.126 6.472 3.816 1.00 9.01 N ANISOU 2016 NE ARG A 251 1303 -116 305 1281 837 -71 N ATOM 2017 CZ ARG A 251 -0.686 7.247 4.532 1.00 9.99 C ANISOU 2017 CZ ARG A 251 1303 -194 143 1318 1176 -397 C ATOM 2018 NH1 ARG A 251 -1.488 8.149 3.956 1.00 9.38 N ANISOU 2018 NH1 ARG A 251 1346 51 120 1028 1190 26 N ATOM 2019 NH2 ARG A 251 -0.704 7.146 5.851 1.00 9.11 N ANISOU 2019 NH2 ARG A 251 963 170 153 1305 1192 -474 N ATOM 2020 N LEU A 252 5.577 8.272 3.056 1.00 9.84 N ANISOU 2020 N LEU A 252 1402 -17 88 1090 1245 -246 N ATOM 2021 CA LEU A 252 6.753 7.954 3.843 1.00 9.19 C ANISOU 2021 CA LEU A 252 1143 27 146 1027 1321 -225 C ATOM 2022 C LEU A 252 6.343 7.265 5.132 1.00 8.97 C ANISOU 2022 C LEU A 252 978 72 65 1175 1254 -154 C ATOM 2023 O LEU A 252 5.369 7.632 5.766 1.00 9.75 O ANISOU 2023 O LEU A 252 891 122 171 1558 1255 -20 O ATOM 2024 CB LEU A 252 7.604 9.201 4.169 1.00 8.96 C ANISOU 2024 CB LEU A 252 1117 -128 -25 1240 1044 -296 C ATOM 2025 CG LEU A 252 8.151 9.951 2.923 1.00 12.36 C ANISOU 2025 CG LEU A 252 1718 -44 193 1171 1804 193 C ATOM 2026 CD1 LEU A 252 8.889 11.153 3.330 1.00 13.75 C ANISOU 2026 CD1 LEU A 252 1924 -398 -3 1675 1622 370 C ATOM 2027 CD2 LEU A 252 9.035 9.077 2.116 1.00 19.76 C ANISOU 2027 CD2 LEU A 252 2975 -247 70 1772 2758 388 C ATOM 2028 N VAL A 253 7.127 6.234 5.504 1.00 9.13 N ANISOU 2028 N VAL A 253 946 50 -31 1242 1282 -131 N ATOM 2029 CA VAL A 253 6.918 5.472 6.711 1.00 8.08 C ANISOU 2029 CA VAL A 253 909 48 109 1121 1038 -246 C ATOM 2030 C VAL A 253 8.195 5.496 7.497 1.00 7.67 C ANISOU 2030 C VAL A 253 909 78 22 1199 805 -226 C ATOM 2031 O VAL A 253 9.284 5.308 6.922 1.00 8.34 O ANISOU 2031 O VAL A 253 1006 145 222 1320 840 -142 O ATOM 2032 CB VAL A 253 6.501 4.022 6.399 1.00 7.61 C ANISOU 2032 CB VAL A 253 1030 71 -43 1214 646 -470 C ATOM 2033 CG1 VAL A 253 6.266 3.262 7.666 1.00 9.67 C ANISOU 2033 CG1 VAL A 253 1253 -84 -82 1338 1081 -379 C ATOM 2034 CG2 VAL A 253 5.241 4.038 5.528 1.00 8.88 C ANISOU 2034 CG2 VAL A 253 1044 -84 -197 1343 987 -131 C ATOM 2035 N TYR A 254 8.077 5.682 8.817 1.00 8.82 N ANISOU 2035 N TYR A 254 810 90 -13 1493 1048 -113 N ATOM 2036 CA TYR A 254 9.209 5.755 9.698 1.00 8.33 C ANISOU 2036 CA TYR A 254 993 122 61 1228 942 -203 C ATOM 2037 C TYR A 254 9.111 4.736 10.825 1.00 8.94 C ANISOU 2037 C TYR A 254 1009 13 146 1372 1015 -126 C ATOM 2038 O TYR A 254 8.019 4.308 11.177 1.00 11.04 O ANISOU 2038 O TYR A 254 1154 28 391 1594 1446 3 O ATOM 2039 CB TYR A 254 9.275 7.136 10.316 1.00 9.25 C ANISOU 2039 CB TYR A 254 879 7 86 1344 1290 -585 C ATOM 2040 CG TYR A 254 9.525 8.228 9.309 1.00 9.62 C ANISOU 2040 CG TYR A 254 1114 -130 -236 1068 1473 -80 C ATOM 2041 CD1 TYR A 254 8.480 8.883 8.702 1.00 13.47 C ANISOU 2041 CD1 TYR A 254 1553 -45 -113 1825 1739 -177 C ATOM 2042 CD2 TYR A 254 10.821 8.672 9.029 1.00 10.11 C ANISOU 2042 CD2 TYR A 254 1155 7 -300 1407 1277 -207 C ATOM 2043 CE1 TYR A 254 8.683 9.924 7.798 1.00 10.88 C ANISOU 2043 CE1 TYR A 254 1383 84 -77 1284 1463 -311 C ATOM 2044 CE2 TYR A 254 11.039 9.720 8.176 1.00 9.78 C ANISOU 2044 CE2 TYR A 254 970 -151 177 1446 1299 -443 C ATOM 2045 CZ TYR A 254 9.951 10.318 7.499 1.00 10.16 C ANISOU 2045 CZ TYR A 254 1162 1 84 1352 1346 -286 C ATOM 2046 OH TYR A 254 10.190 11.392 6.666 1.00 12.60 O ANISOU 2046 OH TYR A 254 1535 -38 169 1525 1725 -117 O ATOM 2047 N GLU A 255 10.270 4.383 11.399 1.00 9.54 N ANISOU 2047 N GLU A 255 1014 -12 56 1353 1258 -106 N ATOM 2048 CA GLU A 255 10.304 3.603 12.624 1.00 11.06 C ANISOU 2048 CA GLU A 255 1435 0 3 1481 1285 -322 C ATOM 2049 C GLU A 255 10.967 4.415 13.722 1.00 9.43 C ANISOU 2049 C GLU A 255 1083 -221 1 1414 1082 -478 C ATOM 2050 O GLU A 255 11.862 5.176 13.466 1.00 10.25 O ANISOU 2050 O GLU A 255 1410 -409 -9 1707 776 -651 O ATOM 2051 CB GLU A 255 11.134 2.310 12.419 1.00 12.12 C ANISOU 2051 CB GLU A 255 1753 28 -47 1383 1468 -457 C ATOM 2052 CG GLU A 255 10.458 1.447 11.366 1.00 18.44 C ANISOU 2052 CG GLU A 255 2724 -171 -138 1933 2346 -250 C ATOM 2053 CD GLU A 255 11.149 0.131 11.077 1.00 21.73 C ANISOU 2053 CD GLU A 255 2867 133 -273 2610 2779 -374 C ATOM 2054 OE1 GLU A 255 10.364 -0.807 10.559 1.00 26.26 O ANISOU 2054 OE1 GLU A 255 3691 253 -1216 3685 2599 -862 O ATOM 2055 OE2 GLU A 255 12.409 0.021 11.394 1.00 26.61 O ANISOU 2055 OE2 GLU A 255 3353 1132 -837 3212 3544 -148 O ATOM 2056 N SER A 256 10.520 4.199 14.950 1.00 9.45 N ANISOU 2056 N SER A 256 1001 -206 -98 1554 1034 -487 N ATOM 2057 CA SER A 256 11.134 4.826 16.120 1.00 10.76 C ANISOU 2057 CA SER A 256 1357 -31 -48 1616 1114 -492 C ATOM 2058 C SER A 256 11.091 3.853 17.292 1.00 12.79 C ANISOU 2058 C SER A 256 1632 -87 -31 1897 1327 -435 C ATOM 2059 O SER A 256 9.997 3.382 17.671 1.00 12.28 O ANISOU 2059 O SER A 256 1398 -185 65 2020 1247 -841 O ATOM 2060 CB SER A 256 10.432 6.142 16.503 1.00 11.88 C ANISOU 2060 CB SER A 256 1464 -231 -102 1806 1242 -466 C ATOM 2061 OG SER A 256 11.077 6.614 17.686 1.00 10.71 O ANISOU 2061 OG SER A 256 1291 -68 1 1822 954 -387 O ATOM 2062 N SER A 257 12.268 3.550 17.852 1.00 13.14 N ANISOU 2062 N SER A 257 1947 -105 59 1852 1190 -386 N ATOM 2063 CA SER A 257 12.407 2.629 18.987 1.00 14.89 C ANISOU 2063 CA SER A 257 2081 -16 20 2102 1474 -464 C ATOM 2064 C SER A 257 12.377 3.325 20.310 1.00 14.71 C ANISOU 2064 C SER A 257 1948 -87 165 2073 1566 -422 C ATOM 2065 O SER A 257 12.474 2.687 21.364 1.00 16.75 O ANISOU 2065 O SER A 257 2713 -175 261 2251 1397 -352 O ATOM 2066 CB SER A 257 13.757 1.881 18.827 1.00 16.40 C ANISOU 2066 CB SER A 257 2510 340 -9 2312 1408 -400 C ATOM 2067 OG SER A 257 13.804 1.153 17.594 1.00 23.76 O ANISOU 2067 OG SER A 257 3292 595 209 2911 2822 -206 O ATOM 2068 N ASP A 258 12.275 4.658 20.286 1.00 14.77 N ANISOU 2068 N ASP A 258 1940 -228 -147 2153 1517 -464 N ATOM 2069 CA ASP A 258 12.496 5.438 21.503 1.00 15.15 C ANISOU 2069 CA ASP A 258 1892 -272 -143 2406 1457 -375 C ATOM 2070 C ASP A 258 11.422 6.523 21.673 1.00 14.34 C ANISOU 2070 C ASP A 258 1828 -340 -156 2234 1384 -385 C ATOM 2071 O ASP A 258 11.686 7.696 22.012 1.00 15.48 O ANISOU 2071 O ASP A 258 1903 -473 -19 2463 1515 -483 O ATOM 2072 CB ASP A 258 13.934 5.968 21.553 1.00 15.26 C ANISOU 2072 CB ASP A 258 1805 -109 6 2574 1416 -460 C ATOM 2073 CG ASP A 258 14.302 6.811 20.368 1.00 15.38 C ANISOU 2073 CG ASP A 258 1698 -81 125 2163 1981 -105 C ATOM 2074 OD1 ASP A 258 13.385 7.077 19.543 1.00 14.24 O ANISOU 2074 OD1 ASP A 258 1647 -199 -113 2170 1591 -727 O ATOM 2075 OD2 ASP A 258 15.456 7.286 20.241 1.00 15.94 O ANISOU 2075 OD2 ASP A 258 1296 -84 78 2977 1781 -28 O ATOM 2076 N MET A 259 10.171 6.132 21.415 1.00 13.68 N ANISOU 2076 N MET A 259 1489 -612 -226 2320 1388 -314 N ATOM 2077 CA MET A 259 9.040 7.025 21.647 1.00 14.41 C ANISOU 2077 CA MET A 259 1758 -561 -388 2466 1251 -141 C ATOM 2078 C MET A 259 9.172 8.345 20.891 1.00 14.82 C ANISOU 2078 C MET A 259 1693 -525 -509 2450 1485 -122 C ATOM 2079 O MET A 259 8.811 9.394 21.359 1.00 16.71 O ANISOU 2079 O MET A 259 2240 -533 -655 2810 1296 317 O ATOM 2080 CB MET A 259 8.890 7.299 23.157 1.00 17.49 C ANISOU 2080 CB MET A 259 2143 -627 -373 2919 1582 -249 C ATOM 2081 CG MET A 259 7.744 6.955 23.861 1.00 17.98 C ANISOU 2081 CG MET A 259 2159 -438 -389 3047 1626 90 C ATOM 2082 SD MET A 259 6.223 6.281 23.270 1.00 15.69 S ANISOU 2082 SD MET A 259 1779 -321 -88 2477 1703 0 S ATOM 2083 CE MET A 259 6.505 4.587 23.355 1.00 21.25 C ANISOU 2083 CE MET A 259 2634 160 191 2844 2594 355 C ATOM 2084 N GLY A 260 9.698 8.256 19.674 1.00 13.38 N ANISOU 2084 N GLY A 260 1571 -476 -378 2335 1176 148 N ATOM 2085 CA GLY A 260 9.789 9.392 18.771 1.00 12.84 C ANISOU 2085 CA GLY A 260 1460 -257 -313 2120 1297 -94 C ATOM 2086 C GLY A 260 10.991 10.273 18.954 1.00 11.92 C ANISOU 2086 C GLY A 260 1334 -105 -231 1929 1266 -29 C ATOM 2087 O GLY A 260 11.069 11.292 18.304 1.00 12.03 O ANISOU 2087 O GLY A 260 1351 -61 -183 1752 1465 -135 O ATOM 2088 N ASN A 261 11.948 9.897 19.807 1.00 11.97 N ANISOU 2088 N ASN A 261 1469 0 -151 1949 1130 -106 N ATOM 2089 CA ASN A 261 13.187 10.687 19.913 1.00 12.14 C ANISOU 2089 CA ASN A 261 1474 -101 -137 1859 1277 -226 C ATOM 2090 C ASN A 261 14.018 10.574 18.653 1.00 12.56 C ANISOU 2090 C ASN A 261 1360 -196 -113 1789 1622 -106 C ATOM 2091 O ASN A 261 14.618 11.589 18.231 1.00 14.49 O ANISOU 2091 O ASN A 261 1737 -178 -201 1898 1870 -77 O ATOM 2092 CB ASN A 261 13.996 10.343 21.144 1.00 14.31 C ANISOU 2092 CB ASN A 261 1579 -199 -170 2270 1584 -286 C ATOM 2093 CG ASN A 261 13.363 10.818 22.400 1.00 16.10 C ANISOU 2093 CG ASN A 261 1899 146 -342 2590 1628 -437 C ATOM 2094 OD1 ASN A 261 12.384 11.636 22.397 1.00 16.43 O ANISOU 2094 OD1 ASN A 261 1815 366 -80 2571 1855 -637 O ATOM 2095 ND2 ASN A 261 13.986 10.433 23.521 1.00 21.16 N ANISOU 2095 ND2 ASN A 261 3283 -171 -272 3313 1441 -872 N ATOM 2096 N ATHR A 262 13.990 9.398 17.995 0.50 11.61 N ANISOU 2096 N ATHR A 262 1384 -321 -127 1638 1389 -139 N ATOM 2097 N BTHR A 262 14.001 9.382 18.015 0.50 11.47 N ANISOU 2097 N BTHR A 262 1364 -289 -110 1689 1302 -218 N ATOM 2098 CA ATHR A 262 14.734 9.214 16.776 0.50 12.03 C ANISOU 2098 CA ATHR A 262 1398 -239 -140 1708 1462 -212 C ATOM 2099 CA BTHR A 262 14.777 9.100 16.827 0.50 11.47 C ANISOU 2099 CA BTHR A 262 1318 -211 -121 1718 1321 -309 C ATOM 2100 C ATHR A 262 13.891 8.471 15.753 0.50 12.04 C ANISOU 2100 C ATHR A 262 1456 -282 -104 1695 1421 -218 C ATOM 2101 C BTHR A 262 13.786 8.546 15.795 0.50 11.73 C ANISOU 2101 C BTHR A 262 1409 -263 -120 1719 1327 -303 C ATOM 2102 O ATHR A 262 13.315 7.400 16.025 0.50 11.80 O ANISOU 2102 O ATHR A 262 1383 -312 21 1875 1223 -173 O ATOM 2103 O BTHR A 262 12.943 7.703 16.134 0.50 11.53 O ANISOU 2103 O BTHR A 262 1399 -221 -107 1880 1102 -498 O ATOM 2104 CB ATHR A 262 16.067 8.489 17.001 0.50 11.28 C ANISOU 2104 CB ATHR A 262 1276 -276 -46 1612 1395 -155 C ATOM 2105 CB BTHR A 262 15.894 8.036 17.091 0.50 10.76 C ANISOU 2105 CB BTHR A 262 1155 -252 20 1707 1224 -309 C ATOM 2106 OG1ATHR A 262 15.848 7.233 17.640 0.50 15.95 O ANISOU 2106 OG1ATHR A 262 1935 -439 -262 2013 2113 -422 O ATOM 2107 OG1BTHR A 262 16.677 8.353 18.264 0.50 10.29 O ANISOU 2107 OG1BTHR A 262 748 -294 -164 1603 1559 -708 O ATOM 2108 CG2ATHR A 262 16.960 9.250 17.956 0.50 11.85 C ANISOU 2108 CG2ATHR A 262 1195 -161 -140 1515 1792 -151 C ATOM 2109 CG2BTHR A 262 16.901 7.967 15.938 0.50 11.87 C ANISOU 2109 CG2BTHR A 262 1494 -201 -68 1870 1143 -370 C ATOM 2110 N TRP A 263 13.869 9.048 14.555 1.00 11.45 N ANISOU 2110 N TRP A 263 1347 -313 -32 1730 1272 -233 N ATOM 2111 CA TRP A 263 13.042 8.572 13.458 1.00 11.61 C ANISOU 2111 CA TRP A 263 1382 -206 -154 1735 1294 -147 C ATOM 2112 C TRP A 263 13.936 8.094 12.354 1.00 12.86 C ANISOU 2112 C TRP A 263 1491 -133 -98 1870 1523 -135 C ATOM 2113 O TRP A 263 14.850 8.824 11.939 1.00 14.39 O ANISOU 2113 O TRP A 263 1730 -208 -226 1876 1862 306 O ATOM 2114 CB TRP A 263 12.164 9.666 12.927 1.00 12.33 C ANISOU 2114 CB TRP A 263 1666 -218 -170 1692 1326 -43 C ATOM 2115 CG TRP A 263 11.098 10.174 13.834 1.00 10.80 C ANISOU 2115 CG TRP A 263 1402 -93 -199 1635 1065 36 C ATOM 2116 CD1 TRP A 263 11.191 10.520 15.183 1.00 10.66 C ANISOU 2116 CD1 TRP A 263 1484 155 -248 1778 787 -95 C ATOM 2117 CD2 TRP A 263 9.736 10.412 13.474 1.00 10.58 C ANISOU 2117 CD2 TRP A 263 1564 83 -62 1509 944 103 C ATOM 2118 NE1 TRP A 263 9.985 10.987 15.634 1.00 13.07 N ANISOU 2118 NE1 TRP A 263 1880 84 -337 1828 1257 14 N ATOM 2119 CE2 TRP A 263 9.058 10.866 14.630 1.00 10.99 C ANISOU 2119 CE2 TRP A 263 1261 -131 105 1831 1082 -65 C ATOM 2120 CE3 TRP A 263 9.000 10.207 12.315 1.00 11.70 C ANISOU 2120 CE3 TRP A 263 1647 -159 -18 1539 1257 88 C ATOM 2121 CZ2 TRP A 263 7.718 11.222 14.593 1.00 11.67 C ANISOU 2121 CZ2 TRP A 263 1801 130 28 1544 1087 189 C ATOM 2122 CZ3 TRP A 263 7.657 10.520 12.301 1.00 13.08 C ANISOU 2122 CZ3 TRP A 263 1855 29 18 1802 1312 89 C ATOM 2123 CH2 TRP A 263 7.041 11.027 13.419 1.00 12.51 C ANISOU 2123 CH2 TRP A 263 1994 49 55 1486 1274 60 C ATOM 2124 N ALEU A 264 13.658 6.891 11.876 0.50 12.38 N ANISOU 2124 N ALEU A 264 1423 -131 -36 1824 1455 -182 N ATOM 2125 N BLEU A 264 13.723 6.871 11.891 0.50 11.50 N ANISOU 2125 N BLEU A 264 1247 -210 -87 1719 1403 -195 N ATOM 2126 CA ALEU A 264 14.404 6.286 10.776 0.50 11.95 C ANISOU 2126 CA ALEU A 264 1409 -55 -76 1706 1424 -196 C ATOM 2127 CA BLEU A 264 14.460 6.386 10.715 0.50 11.06 C ANISOU 2127 CA BLEU A 264 1224 -129 -133 1587 1391 -214 C ATOM 2128 C ALEU A 264 13.427 5.923 9.664 0.50 10.58 C ANISOU 2128 C ALEU A 264 1261 -74 -58 1555 1201 -187 C ATOM 2129 C BLEU A 264 13.472 5.921 9.665 0.50 10.03 C ANISOU 2129 C BLEU A 264 1161 -116 -103 1473 1174 -200 C ATOM 2130 O ALEU A 264 12.437 5.230 9.920 0.50 10.90 O ANISOU 2130 O ALEU A 264 1123 -57 -83 1734 1282 -20 O ATOM 2131 O BLEU A 264 12.541 5.161 9.961 0.50 10.28 O ANISOU 2131 O BLEU A 264 1048 -99 -183 1653 1203 -69 O ATOM 2132 CB ALEU A 264 15.091 5.025 11.281 0.50 12.58 C ANISOU 2132 CB ALEU A 264 1468 22 -100 1878 1433 -289 C ATOM 2133 CB BLEU A 264 15.418 5.262 11.069 0.50 11.85 C ANISOU 2133 CB BLEU A 264 1297 -85 -204 1685 1520 -332 C ATOM 2134 CG ALEU A 264 15.999 4.291 10.299 0.50 15.06 C ANISOU 2134 CG ALEU A 264 1943 40 114 2091 1688 -219 C ATOM 2135 CG BLEU A 264 16.451 5.485 12.171 0.50 15.44 C ANISOU 2135 CG BLEU A 264 1561 -96 -85 2079 2226 -435 C ATOM 2136 CD1ALEU A 264 17.121 5.208 9.799 0.50 17.61 C ANISOU 2136 CD1ALEU A 264 1997 286 243 2566 2125 -332 C ATOM 2137 CD1BLEU A 264 17.198 4.163 12.394 0.50 18.63 C ANISOU 2137 CD1BLEU A 264 1793 -293 -75 2443 2843 -510 C ATOM 2138 CD2ALEU A 264 16.543 3.040 11.044 0.50 16.16 C ANISOU 2138 CD2ALEU A 264 2066 221 36 2242 1829 -235 C ATOM 2139 CD2BLEU A 264 17.403 6.560 11.772 0.50 20.56 C ANISOU 2139 CD2BLEU A 264 2281 3 118 2782 2748 -659 C ATOM 2140 N GLU A 265 13.660 6.380 8.440 1.00 9.94 N ANISOU 2140 N GLU A 265 1156 -114 -120 1512 1106 -180 N ATOM 2141 CA GLU A 265 12.749 6.004 7.360 1.00 10.78 C ANISOU 2141 CA GLU A 265 1109 -79 -62 1687 1297 -197 C ATOM 2142 C GLU A 265 12.816 4.482 7.132 1.00 10.25 C ANISOU 2142 C GLU A 265 1058 -97 -58 1614 1223 -258 C ATOM 2143 O GLU A 265 13.911 3.911 7.021 1.00 10.93 O ANISOU 2143 O GLU A 265 893 -313 -221 1682 1578 -562 O ATOM 2144 CB GLU A 265 13.110 6.722 6.077 1.00 10.90 C ANISOU 2144 CB GLU A 265 1237 -54 -172 1677 1227 -178 C ATOM 2145 CG GLU A 265 12.017 6.511 5.042 1.00 11.20 C ANISOU 2145 CG GLU A 265 1213 -94 311 1996 1046 -389 C ATOM 2146 CD GLU A 265 12.285 7.056 3.653 1.00 11.77 C ANISOU 2146 CD GLU A 265 1146 -452 29 2006 1319 17 C ATOM 2147 OE1 GLU A 265 13.236 7.866 3.465 1.00 14.59 O ANISOU 2147 OE1 GLU A 265 1345 -803 533 2747 1448 -241 O ATOM 2148 OE2 GLU A 265 11.464 6.699 2.754 1.00 13.11 O ANISOU 2148 OE2 GLU A 265 1348 -375 112 2045 1587 -507 O ATOM 2149 N ALA A 266 11.670 3.843 7.031 1.00 9.97 N ANISOU 2149 N ALA A 266 1018 -8 -75 1525 1242 -215 N ATOM 2150 CA ALA A 266 11.509 2.402 6.895 1.00 9.74 C ANISOU 2150 CA ALA A 266 1131 -33 -24 1386 1182 -129 C ATOM 2151 C ALA A 266 11.729 1.971 5.434 1.00 9.44 C ANISOU 2151 C ALA A 266 1110 -91 -124 1278 1197 -48 C ATOM 2152 O ALA A 266 10.874 1.332 4.754 1.00 9.71 O ANISOU 2152 O ALA A 266 1196 -89 -207 1297 1195 -226 O ATOM 2153 CB ALA A 266 10.167 1.975 7.410 1.00 9.60 C ANISOU 2153 CB ALA A 266 979 -121 0 1535 1133 -360 C ATOM 2154 N VAL A 267 12.921 2.343 4.934 1.00 10.54 N ANISOU 2154 N VAL A 267 1311 -144 -216 1399 1293 89 N ATOM 2155 CA VAL A 267 13.215 2.070 3.527 1.00 11.00 C ANISOU 2155 CA VAL A 267 1426 -40 -93 1456 1298 98 C ATOM 2156 C VAL A 267 13.244 0.585 3.119 1.00 10.50 C ANISOU 2156 C VAL A 267 1246 10 -70 1471 1273 94 C ATOM 2157 O VAL A 267 13.051 0.274 1.930 1.00 12.71 O ANISOU 2157 O VAL A 267 1652 -10 -136 1731 1444 -68 O ATOM 2158 CB VAL A 267 14.555 2.759 3.088 1.00 13.30 C ANISOU 2158 CB VAL A 267 1796 47 35 1658 1599 283 C ATOM 2159 CG1 VAL A 267 14.426 4.233 3.294 1.00 16.97 C ANISOU 2159 CG1 VAL A 267 2259 -304 -181 2008 2178 590 C ATOM 2160 CG2 VAL A 267 15.727 2.224 3.852 1.00 13.80 C ANISOU 2160 CG2 VAL A 267 1673 -88 -53 2253 1314 538 C ATOM 2161 N GLY A 268 13.533 -0.293 4.068 1.00 10.44 N ANISOU 2161 N GLY A 268 1499 6 -89 1326 1139 -7 N ATOM 2162 CA GLY A 268 13.672 -1.696 3.782 1.00 10.33 C ANISOU 2162 CA GLY A 268 1263 98 90 1361 1298 -60 C ATOM 2163 C GLY A 268 12.363 -2.480 3.847 1.00 10.58 C ANISOU 2163 C GLY A 268 1443 0 127 1299 1279 -14 C ATOM 2164 O GLY A 268 12.376 -3.673 3.678 1.00 11.50 O ANISOU 2164 O GLY A 268 1437 146 29 1511 1421 117 O ATOM 2165 N THR A 269 11.247 -1.782 4.120 1.00 8.74 N ANISOU 2165 N THR A 269 1054 27 185 1165 1099 -189 N ATOM 2166 CA THR A 269 9.963 -2.441 4.349 1.00 8.63 C ANISOU 2166 CA THR A 269 1107 21 109 1180 990 -146 C ATOM 2167 C THR A 269 8.822 -1.728 3.721 1.00 9.43 C ANISOU 2167 C THR A 269 1160 18 -46 1293 1127 -263 C ATOM 2168 O THR A 269 8.389 -2.147 2.656 1.00 11.46 O ANISOU 2168 O THR A 269 1674 155 -93 1788 891 -296 O ATOM 2169 CB THR A 269 9.687 -2.641 5.842 1.00 9.80 C ANISOU 2169 CB THR A 269 1296 -147 8 1236 1189 -249 C ATOM 2170 OG1 THR A 269 9.864 -1.437 6.561 1.00 9.97 O ANISOU 2170 OG1 THR A 269 1198 -143 -220 1512 1076 -272 O ATOM 2171 CG2 THR A 269 10.598 -3.707 6.445 1.00 11.08 C ANISOU 2171 CG2 THR A 269 1066 -285 -40 1682 1462 -231 C ATOM 2172 N LEU A 270 8.342 -0.667 4.360 1.00 8.52 N ANISOU 2172 N LEU A 270 1042 66 -64 1355 839 -329 N ATOM 2173 CA LEU A 270 7.077 -0.067 3.937 1.00 7.82 C ANISOU 2173 CA LEU A 270 958 -16 -41 1099 913 -259 C ATOM 2174 C LEU A 270 7.149 1.337 3.371 1.00 8.39 C ANISOU 2174 C LEU A 270 928 -209 19 1306 952 -226 C ATOM 2175 O LEU A 270 6.157 1.799 2.812 1.00 8.97 O ANISOU 2175 O LEU A 270 989 -187 92 1404 1013 -192 O ATOM 2176 CB LEU A 270 6.097 -0.071 5.111 1.00 9.68 C ANISOU 2176 CB LEU A 270 1090 -174 18 1299 1289 -170 C ATOM 2177 CG LEU A 270 5.841 -1.397 5.813 1.00 9.46 C ANISOU 2177 CG LEU A 270 899 -142 248 1514 1180 -282 C ATOM 2178 CD1 LEU A 270 4.901 -1.205 6.948 1.00 10.64 C ANISOU 2178 CD1 LEU A 270 977 69 204 1926 1138 -361 C ATOM 2179 CD2 LEU A 270 5.312 -2.419 4.817 1.00 12.30 C ANISOU 2179 CD2 LEU A 270 1395 -101 112 1586 1692 -198 C ATOM 2180 N SER A 271 8.249 2.068 3.608 1.00 7.92 N ANISOU 2180 N SER A 271 846 -122 45 1329 833 -359 N ATOM 2181 CA SER A 271 8.290 3.414 3.099 1.00 8.18 C ANISOU 2181 CA SER A 271 1057 -109 -18 1255 793 -196 C ATOM 2182 C SER A 271 8.260 3.461 1.596 1.00 8.34 C ANISOU 2182 C SER A 271 993 -123 32 1343 833 -157 C ATOM 2183 O SER A 271 8.913 2.662 0.924 1.00 9.17 O ANISOU 2183 O SER A 271 1064 -48 58 1536 882 -125 O ATOM 2184 CB SER A 271 9.480 4.196 3.608 1.00 8.75 C ANISOU 2184 CB SER A 271 1135 -90 83 1370 817 -352 C ATOM 2185 OG SER A 271 9.255 5.559 3.436 1.00 8.95 O ANISOU 2185 OG SER A 271 1287 -8 -25 1031 1082 -565 O ATOM 2186 N ARG A 272 7.456 4.382 1.089 1.00 8.47 N ANISOU 2186 N ARG A 272 791 -38 4 1623 802 -132 N ATOM 2187 CA ARG A 272 7.328 4.641 -0.348 1.00 9.52 C ANISOU 2187 CA ARG A 272 1141 -111 69 1584 889 -162 C ATOM 2188 C ARG A 272 6.599 3.552 -1.120 1.00 8.69 C ANISOU 2188 C ARG A 272 764 2 124 1573 965 -155 C ATOM 2189 O ARG A 272 6.464 3.607 -2.363 1.00 10.61 O ANISOU 2189 O ARG A 272 1756 -40 219 1533 740 -248 O ATOM 2190 CB ARG A 272 8.627 5.031 -1.027 1.00 10.61 C ANISOU 2190 CB ARG A 272 1199 -80 -49 1657 1173 -271 C ATOM 2191 CG ARG A 272 9.356 6.138 -0.260 1.00 12.69 C ANISOU 2191 CG ARG A 272 1332 -521 -200 1902 1585 -99 C ATOM 2192 CD ARG A 272 10.591 6.687 -0.929 1.00 17.15 C ANISOU 2192 CD ARG A 272 2257 -575 -9 2417 1843 -89 C ATOM 2193 NE ARG A 272 11.407 7.413 0.028 1.00 18.00 N ANISOU 2193 NE ARG A 272 2430 -670 309 2650 1757 -70 N ATOM 2194 CZ ARG A 272 11.842 8.673 -0.125 1.00 22.46 C ANISOU 2194 CZ ARG A 272 3204 -454 427 2988 2340 -219 C ATOM 2195 NH1 ARG A 272 12.567 9.233 0.838 1.00 23.96 N ANISOU 2195 NH1 ARG A 272 3408 -1049 296 3326 2367 -6 N ATOM 2196 NH2 ARG A 272 11.565 9.401 -1.229 1.00 27.88 N ANISOU 2196 NH2 ARG A 272 4314 -861 544 3557 2721 -227 N ATOM 2197 N VAL A 273 6.059 2.584 -0.407 1.00 8.93 N ANISOU 2197 N VAL A 273 1008 -64 105 1520 864 -287 N ATOM 2198 CA VAL A 273 5.266 1.536 -1.044 1.00 8.59 C ANISOU 2198 CA VAL A 273 878 0 -40 1403 982 -302 C ATOM 2199 C VAL A 273 3.945 2.093 -1.602 1.00 9.37 C ANISOU 2199 C VAL A 273 977 90 -77 1479 1102 -323 C ATOM 2200 O VAL A 273 3.555 1.805 -2.745 1.00 11.45 O ANISOU 2200 O VAL A 273 1066 62 -140 1997 1288 -148 O ATOM 2201 CB VAL A 273 5.016 0.381 -0.078 1.00 7.94 C ANISOU 2201 CB VAL A 273 809 -62 -140 1418 787 -395 C ATOM 2202 CG1 VAL A 273 3.924 -0.568 -0.614 1.00 9.63 C ANISOU 2202 CG1 VAL A 273 1160 -151 -161 1528 969 -152 C ATOM 2203 CG2 VAL A 273 6.319 -0.334 0.188 1.00 10.29 C ANISOU 2203 CG2 VAL A 273 1340 255 0 1283 1286 -328 C ATOM 2204 N TRP A 274 3.247 2.869 -0.795 1.00 8.58 N ANISOU 2204 N TRP A 274 791 123 -47 1314 1155 -270 N ATOM 2205 CA TRP A 274 1.889 3.266 -1.155 1.00 8.88 C ANISOU 2205 CA TRP A 274 990 -12 70 1402 982 -354 C ATOM 2206 C TRP A 274 1.820 4.640 -1.749 1.00 9.50 C ANISOU 2206 C TRP A 274 1151 7 -26 1384 1072 -226 C ATOM 2207 O TRP A 274 2.236 5.632 -1.142 1.00 10.09 O ANISOU 2207 O TRP A 274 1294 -105 185 1407 1131 -224 O ATOM 2208 CB TRP A 274 0.977 3.176 0.074 1.00 10.22 C ANISOU 2208 CB TRP A 274 1055 -59 97 1552 1276 -139 C ATOM 2209 CG TRP A 274 0.723 1.753 0.507 1.00 9.24 C ANISOU 2209 CG TRP A 274 1048 -143 80 1333 1127 -168 C ATOM 2210 CD1 TRP A 274 0.052 0.797 -0.184 1.00 9.07 C ANISOU 2210 CD1 TRP A 274 1016 -164 265 1355 1075 -215 C ATOM 2211 CD2 TRP A 274 1.197 1.128 1.710 1.00 8.89 C ANISOU 2211 CD2 TRP A 274 790 -7 118 1274 1313 -308 C ATOM 2212 NE1 TRP A 274 0.037 -0.366 0.519 1.00 9.76 N ANISOU 2212 NE1 TRP A 274 1179 -425 10 1361 1169 -46 N ATOM 2213 CE2 TRP A 274 0.703 -0.189 1.711 1.00 10.42 C ANISOU 2213 CE2 TRP A 274 1083 35 -19 1544 1331 -268 C ATOM 2214 CE3 TRP A 274 1.916 1.581 2.838 1.00 9.90 C ANISOU 2214 CE3 TRP A 274 1314 -72 33 1121 1326 -99 C ATOM 2215 CZ2 TRP A 274 0.987 -1.098 2.735 1.00 9.74 C ANISOU 2215 CZ2 TRP A 274 855 -455 84 1491 1355 -338 C ATOM 2216 CZ3 TRP A 274 2.153 0.685 3.883 1.00 9.38 C ANISOU 2216 CZ3 TRP A 274 935 -286 65 1380 1250 -394 C ATOM 2217 CH2 TRP A 274 1.710 -0.644 3.795 1.00 11.14 C ANISOU 2217 CH2 TRP A 274 1502 -65 255 1396 1333 -259 C ATOM 2218 N GLY A 275 1.270 4.717 -2.962 1.00 10.44 N ANISOU 2218 N GLY A 275 1222 -10 112 1520 1224 -396 N ATOM 2219 CA GLY A 275 1.083 5.999 -3.645 1.00 10.37 C ANISOU 2219 CA GLY A 275 1220 -6 149 1522 1198 -195 C ATOM 2220 C GLY A 275 -0.344 6.499 -3.581 1.00 9.38 C ANISOU 2220 C GLY A 275 1156 -8 124 1441 965 -91 C ATOM 2221 O GLY A 275 -1.269 5.685 -3.556 1.00 10.86 O ANISOU 2221 O GLY A 275 1173 -58 265 1598 1356 -226 O ATOM 2222 N PRO A 276 -0.540 7.816 -3.532 1.00 10.08 N ANISOU 2222 N PRO A 276 1100 -19 267 1509 1221 -126 N ATOM 2223 CA PRO A 276 -1.879 8.371 -3.311 1.00 10.14 C ANISOU 2223 CA PRO A 276 1065 76 273 1653 1132 -250 C ATOM 2224 C PRO A 276 -2.796 8.401 -4.545 1.00 10.02 C ANISOU 2224 C PRO A 276 1049 141 347 1719 1038 -257 C ATOM 2225 O PRO A 276 -3.968 8.736 -4.403 1.00 12.15 O ANISOU 2225 O PRO A 276 1164 87 224 2009 1439 -212 O ATOM 2226 CB PRO A 276 -1.587 9.772 -2.840 1.00 11.76 C ANISOU 2226 CB PRO A 276 1193 180 405 1688 1587 -88 C ATOM 2227 CG PRO A 276 -0.299 10.155 -3.533 1.00 11.52 C ANISOU 2227 CG PRO A 276 1246 79 261 1739 1392 31 C ATOM 2228 CD PRO A 276 0.502 8.856 -3.464 1.00 11.03 C ANISOU 2228 CD PRO A 276 1059 27 310 1750 1379 -133 C ATOM 2229 N SER A 277 -2.239 8.111 -5.728 1.00 9.96 N ANISOU 2229 N SER A 277 891 243 406 1875 1018 -331 N ATOM 2230 CA SER A 277 -3.014 8.073 -6.963 1.00 10.76 C ANISOU 2230 CA SER A 277 1236 33 215 1817 1034 -282 C ATOM 2231 C SER A 277 -2.159 7.345 -7.971 1.00 10.56 C ANISOU 2231 C SER A 277 1189 116 214 1806 1017 -220 C ATOM 2232 O SER A 277 -1.004 7.052 -7.660 1.00 11.21 O ANISOU 2232 O SER A 277 1098 131 336 1881 1277 -186 O ATOM 2233 CB SER A 277 -3.264 9.490 -7.485 1.00 10.58 C ANISOU 2233 CB SER A 277 1324 50 154 1778 918 -303 C ATOM 2234 OG SER A 277 -2.059 10.168 -7.858 1.00 12.01 O ANISOU 2234 OG SER A 277 1169 12 587 1987 1405 -352 O ATOM 2235 N PRO A 278 -2.697 6.998 -9.138 1.00 11.94 N ANISOU 2235 N PRO A 278 1357 24 -23 1992 1187 -261 N ATOM 2236 CA PRO A 278 -1.914 6.257 -10.115 1.00 12.80 C ANISOU 2236 CA PRO A 278 1482 60 51 2148 1231 -274 C ATOM 2237 C PRO A 278 -0.541 6.767 -10.380 1.00 13.47 C ANISOU 2237 C PRO A 278 1741 80 46 2166 1211 -131 C ATOM 2238 O PRO A 278 0.427 5.968 -10.379 1.00 14.69 O ANISOU 2238 O PRO A 278 1646 258 159 2393 1543 19 O ATOM 2239 CB PRO A 278 -2.834 6.173 -11.345 1.00 13.43 C ANISOU 2239 CB PRO A 278 1555 -64 -143 2273 1274 -225 C ATOM 2240 CG PRO A 278 -4.209 6.139 -10.700 1.00 14.12 C ANISOU 2240 CG PRO A 278 1608 -146 -134 2418 1339 -262 C ATOM 2241 CD PRO A 278 -4.125 7.064 -9.489 1.00 12.40 C ANISOU 2241 CD PRO A 278 1456 137 -13 2251 1002 -268 C ATOM 2242 N LYS A 279 -0.425 8.072 -10.502 1.00 14.76 N ANISOU 2242 N LYS A 279 1720 225 168 2295 1591 -187 N ATOM 2243 CA LYS A 279 0.856 8.709 -10.741 1.00 14.85 C ANISOU 2243 CA LYS A 279 1715 13 232 2194 1731 -60 C ATOM 2244 C LYS A 279 1.472 9.385 -9.540 1.00 13.88 C ANISOU 2244 C LYS A 279 1516 86 326 2158 1599 -148 C ATOM 2245 O LYS A 279 2.426 10.143 -9.664 1.00 15.38 O ANISOU 2245 O LYS A 279 1511 73 408 2282 2051 -39 O ATOM 2246 CB LYS A 279 0.720 9.700 -11.913 1.00 16.82 C ANISOU 2246 CB LYS A 279 1921 38 342 2495 1973 -129 C ATOM 2247 CG LYS A 279 0.398 9.008 -13.258 1.00 20.81 C ANISOU 2247 CG LYS A 279 2722 -104 290 2903 2280 243 C ATOM 2248 CD LYS A 279 1.352 7.806 -13.447 1.00 27.13 C ANISOU 2248 CD LYS A 279 4016 -8 -369 3537 2755 105 C ATOM 2249 CE LYS A 279 1.521 7.293 -14.810 1.00 31.17 C ANISOU 2249 CE LYS A 279 4260 383 142 4171 3412 270 C ATOM 2250 NZ LYS A 279 2.766 6.379 -14.755 1.00 32.58 N ANISOU 2250 NZ LYS A 279 4355 596 -193 4448 3573 622 N ATOM 2251 N SER A 280 0.901 9.134 -8.370 1.00 13.17 N ANISOU 2251 N SER A 280 1455 -17 310 2049 1497 -112 N ATOM 2252 CA SER A 280 1.391 9.690 -7.104 1.00 13.51 C ANISOU 2252 CA SER A 280 1598 28 239 2030 1505 -139 C ATOM 2253 C SER A 280 1.595 11.193 -7.174 1.00 14.87 C ANISOU 2253 C SER A 280 1790 27 188 2279 1579 -135 C ATOM 2254 O SER A 280 2.544 11.725 -6.635 1.00 15.31 O ANISOU 2254 O SER A 280 1787 101 253 2293 1733 -408 O ATOM 2255 CB SER A 280 2.634 8.953 -6.653 1.00 12.81 C ANISOU 2255 CB SER A 280 1321 -112 337 2116 1428 -262 C ATOM 2256 OG SER A 280 2.379 7.605 -6.308 1.00 14.13 O ANISOU 2256 OG SER A 280 1397 100 480 2238 1733 -558 O ATOM 2257 N ASN A 281 0.610 11.877 -7.755 1.00 13.20 N ANISOU 2257 N ASN A 281 1752 104 242 2097 1165 -50 N ATOM 2258 CA ASN A 281 0.653 13.306 -8.008 1.00 13.89 C ANISOU 2258 CA ASN A 281 1829 142 229 2053 1394 48 C ATOM 2259 C ASN A 281 -0.631 14.038 -7.631 1.00 13.39 C ANISOU 2259 C ASN A 281 1828 177 315 1917 1342 46 C ATOM 2260 O ASN A 281 -0.898 15.117 -8.173 1.00 14.48 O ANISOU 2260 O ASN A 281 1907 83 486 1973 1621 110 O ATOM 2261 CB ASN A 281 0.996 13.564 -9.480 1.00 14.48 C ANISOU 2261 CB ASN A 281 1826 198 255 2149 1524 171 C ATOM 2262 CG ASN A 281 -0.039 13.089 -10.422 1.00 15.97 C ANISOU 2262 CG ASN A 281 2265 249 437 2287 1515 205 C ATOM 2263 OD1 ASN A 281 -1.013 12.379 -10.043 1.00 16.26 O ANISOU 2263 OD1 ASN A 281 1758 195 301 3004 1413 -142 O ATOM 2264 ND2 ASN A 281 0.088 13.573 -11.694 1.00 20.84 N ANISOU 2264 ND2 ASN A 281 2724 2 592 3095 2096 350 N ATOM 2265 N GLN A 282 -1.360 13.447 -6.682 1.00 12.84 N ANISOU 2265 N GLN A 282 1651 94 280 1936 1288 -65 N ATOM 2266 CA GLN A 282 -2.610 13.976 -6.194 1.00 11.69 C ANISOU 2266 CA GLN A 282 1529 45 247 1778 1134 -102 C ATOM 2267 C GLN A 282 -2.579 14.006 -4.687 1.00 10.43 C ANISOU 2267 C GLN A 282 1308 191 367 1624 1030 -53 C ATOM 2268 O GLN A 282 -1.669 13.411 -4.087 1.00 10.35 O ANISOU 2268 O GLN A 282 1292 276 365 1687 953 -258 O ATOM 2269 CB GLN A 282 -3.785 13.065 -6.683 1.00 10.72 C ANISOU 2269 CB GLN A 282 1329 -63 153 1630 1112 -195 C ATOM 2270 CG GLN A 282 -3.799 12.857 -8.162 1.00 11.83 C ANISOU 2270 CG GLN A 282 1591 66 410 1880 1024 -227 C ATOM 2271 CD GLN A 282 -4.204 14.099 -8.955 1.00 13.50 C ANISOU 2271 CD GLN A 282 2020 251 112 2064 1045 29 C ATOM 2272 OE1 GLN A 282 -4.989 14.924 -8.457 1.00 14.10 O ANISOU 2272 OE1 GLN A 282 1503 264 430 2199 1655 -179 O ATOM 2273 NE2 GLN A 282 -3.645 14.267 -10.157 1.00 18.49 N ANISOU 2273 NE2 GLN A 282 2689 65 660 3177 1160 -242 N ATOM 2274 N PRO A 283 -3.535 14.674 -4.059 1.00 10.51 N ANISOU 2274 N PRO A 283 1490 124 336 1451 1049 -184 N ATOM 2275 CA PRO A 283 -3.641 14.633 -2.601 1.00 11.06 C ANISOU 2275 CA PRO A 283 1325 80 297 1647 1230 -188 C ATOM 2276 C PRO A 283 -3.695 13.217 -2.042 1.00 10.62 C ANISOU 2276 C PRO A 283 1339 35 220 1399 1297 -279 C ATOM 2277 O PRO A 283 -4.226 12.312 -2.678 1.00 11.82 O ANISOU 2277 O PRO A 283 1520 149 213 1460 1509 -159 O ATOM 2278 CB PRO A 283 -4.934 15.391 -2.317 1.00 11.09 C ANISOU 2278 CB PRO A 283 1547 207 137 1699 965 -384 C ATOM 2279 CG PRO A 283 -5.082 16.358 -3.532 1.00 11.94 C ANISOU 2279 CG PRO A 283 1546 242 67 1624 1365 -250 C ATOM 2280 CD PRO A 283 -4.586 15.542 -4.643 1.00 11.55 C ANISOU 2280 CD PRO A 283 1572 247 207 1728 1086 -207 C ATOM 2281 N GLY A 284 -3.150 13.096 -0.845 1.00 10.65 N ANISOU 2281 N GLY A 284 1133 -175 208 1526 1387 -289 N ATOM 2282 CA GLY A 284 -3.182 11.877 -0.081 1.00 10.12 C ANISOU 2282 CA GLY A 284 1131 -31 292 1412 1302 -250 C ATOM 2283 C GLY A 284 -4.456 11.721 0.756 1.00 11.14 C ANISOU 2283 C GLY A 284 1263 -93 193 1553 1416 -251 C ATOM 2284 O GLY A 284 -5.462 12.374 0.534 1.00 10.63 O ANISOU 2284 O GLY A 284 1195 -49 194 1445 1397 -258 O ATOM 2285 N SER A 285 -4.393 10.905 1.780 1.00 9.77 N ANISOU 2285 N SER A 285 1218 -136 302 1329 1165 -246 N ATOM 2286 CA SER A 285 -5.568 10.554 2.590 1.00 9.69 C ANISOU 2286 CA SER A 285 1150 -51 298 1445 1086 -193 C ATOM 2287 C SER A 285 -5.161 10.121 3.991 1.00 9.97 C ANISOU 2287 C SER A 285 1255 -101 259 1273 1257 -117 C ATOM 2288 O SER A 285 -4.017 9.779 4.251 1.00 10.47 O ANISOU 2288 O SER A 285 1257 26 109 1298 1422 -48 O ATOM 2289 CB SER A 285 -6.335 9.405 1.927 1.00 10.69 C ANISOU 2289 CB SER A 285 1215 -91 329 1494 1351 -82 C ATOM 2290 OG SER A 285 -7.587 9.148 2.537 1.00 10.83 O ANISOU 2290 OG SER A 285 1069 -196 431 1796 1250 -178 O ATOM 2291 N GLN A 286 -6.151 10.188 4.860 1.00 8.71 N ANISOU 2291 N GLN A 286 1129 6 214 1316 865 -85 N ATOM 2292 CA GLN A 286 -6.164 9.455 6.133 1.00 9.76 C ANISOU 2292 CA GLN A 286 1375 -23 267 1261 1069 -61 C ATOM 2293 C GLN A 286 -6.193 7.958 5.783 1.00 8.46 C ANISOU 2293 C GLN A 286 1195 -32 59 1176 842 -106 C ATOM 2294 O GLN A 286 -6.746 7.568 4.777 1.00 9.61 O ANISOU 2294 O GLN A 286 1075 -125 78 1537 1037 -417 O ATOM 2295 CB GLN A 286 -7.377 9.865 6.934 1.00 8.89 C ANISOU 2295 CB GLN A 286 1225 -21 278 1217 934 -95 C ATOM 2296 CG GLN A 286 -7.618 9.132 8.265 1.00 9.18 C ANISOU 2296 CG GLN A 286 985 22 307 1212 1290 -171 C ATOM 2297 CD GLN A 286 -8.308 7.805 8.076 1.00 9.37 C ANISOU 2297 CD GLN A 286 1329 -123 -45 1075 1155 62 C ATOM 2298 OE1 GLN A 286 -8.925 7.570 7.025 1.00 10.06 O ANISOU 2298 OE1 GLN A 286 1077 -429 21 1623 1121 -181 O ATOM 2299 NE2 GLN A 286 -8.117 6.891 9.029 1.00 8.34 N ANISOU 2299 NE2 GLN A 286 1135 -253 195 1418 615 -466 N ATOM 2300 N SER A 287 -5.556 7.153 6.626 1.00 8.71 N ANISOU 2300 N SER A 287 933 -41 17 1324 1050 -333 N ATOM 2301 CA SER A 287 -5.451 5.735 6.474 1.00 8.62 C ANISOU 2301 CA SER A 287 970 -54 107 1239 1064 -280 C ATOM 2302 C SER A 287 -5.685 5.018 7.807 1.00 7.58 C ANISOU 2302 C SER A 287 889 -67 77 1092 898 -279 C ATOM 2303 O SER A 287 -5.155 5.450 8.831 1.00 8.88 O ANISOU 2303 O SER A 287 784 -114 123 1504 1084 -367 O ATOM 2304 CB SER A 287 -4.040 5.369 5.993 1.00 9.59 C ANISOU 2304 CB SER A 287 1145 -93 -167 1265 1235 -212 C ATOM 2305 OG SER A 287 -3.872 5.690 4.625 1.00 9.92 O ANISOU 2305 OG SER A 287 1238 -166 70 1600 931 -121 O ATOM 2306 N SER A 288 -6.385 3.875 7.776 1.00 7.97 N ANISOU 2306 N SER A 288 949 -195 196 1241 838 -428 N ATOM 2307 CA SER A 288 -6.391 2.947 8.904 1.00 7.56 C ANISOU 2307 CA SER A 288 878 -46 211 1055 938 -251 C ATOM 2308 C SER A 288 -5.122 2.120 8.851 1.00 8.12 C ANISOU 2308 C SER A 288 841 -144 198 1326 919 -218 C ATOM 2309 O SER A 288 -4.738 1.644 7.794 1.00 9.45 O ANISOU 2309 O SER A 288 1140 -5 256 1401 1048 -465 O ATOM 2310 CB SER A 288 -7.629 2.050 8.866 1.00 8.58 C ANISOU 2310 CB SER A 288 946 -77 137 1167 1147 -175 C ATOM 2311 OG SER A 288 -7.802 1.283 10.048 1.00 9.22 O ANISOU 2311 OG SER A 288 932 -42 343 1310 1261 -200 O ATOM 2312 N PHE A 289 -4.445 1.977 9.996 1.00 8.46 N ANISOU 2312 N PHE A 289 916 -77 292 1330 968 -244 N ATOM 2313 CA PHE A 289 -3.195 1.213 10.020 1.00 8.60 C ANISOU 2313 CA PHE A 289 1028 -104 174 1207 1031 -160 C ATOM 2314 C PHE A 289 -3.102 0.616 11.409 1.00 8.50 C ANISOU 2314 C PHE A 289 1047 -131 146 1207 974 -241 C ATOM 2315 O PHE A 289 -2.788 1.296 12.403 1.00 10.37 O ANISOU 2315 O PHE A 289 1352 -330 263 1466 1120 -129 O ATOM 2316 CB PHE A 289 -2.010 2.180 9.698 1.00 8.50 C ANISOU 2316 CB PHE A 289 928 -19 206 1327 973 -190 C ATOM 2317 CG PHE A 289 -0.670 1.521 9.564 1.00 9.21 C ANISOU 2317 CG PHE A 289 1029 -123 150 1381 1088 -106 C ATOM 2318 CD1 PHE A 289 -0.438 0.436 8.747 1.00 9.32 C ANISOU 2318 CD1 PHE A 289 1020 -170 180 1587 933 -455 C ATOM 2319 CD2 PHE A 289 0.409 2.084 10.197 1.00 9.55 C ANISOU 2319 CD2 PHE A 289 1224 150 83 1358 1045 -488 C ATOM 2320 CE1 PHE A 289 0.870 -0.097 8.595 1.00 9.35 C ANISOU 2320 CE1 PHE A 289 1194 -250 99 1324 1033 -422 C ATOM 2321 CE2 PHE A 289 1.665 1.542 10.087 1.00 8.73 C ANISOU 2321 CE2 PHE A 289 881 -138 -11 1363 1070 -388 C ATOM 2322 CZ PHE A 289 1.906 0.478 9.279 1.00 8.54 C ANISOU 2322 CZ PHE A 289 1033 -203 -112 1357 853 -204 C ATOM 2323 N THR A 290 -3.370 -0.676 11.480 1.00 7.81 N ANISOU 2323 N THR A 290 1106 -70 116 1028 832 -315 N ATOM 2324 CA THR A 290 -3.449 -1.379 12.755 1.00 8.12 C ANISOU 2324 CA THR A 290 936 -178 162 1090 1058 -357 C ATOM 2325 C THR A 290 -2.664 -2.683 12.733 1.00 8.10 C ANISOU 2325 C THR A 290 1093 -132 29 1161 824 -425 C ATOM 2326 O THR A 290 -2.511 -3.336 11.701 1.00 8.85 O ANISOU 2326 O THR A 290 1000 -122 -12 1431 929 -378 O ATOM 2327 CB THR A 290 -4.922 -1.692 13.090 1.00 10.36 C ANISOU 2327 CB THR A 290 1254 -89 237 1413 1266 -421 C ATOM 2328 OG1 THR A 290 -5.467 -2.405 12.003 1.00 9.24 O ANISOU 2328 OG1 THR A 290 880 -14 243 1267 1362 -470 O ATOM 2329 CG2 THR A 290 -5.745 -0.475 13.343 1.00 10.43 C ANISOU 2329 CG2 THR A 290 1095 -149 167 1883 985 -257 C ATOM 2330 N ALA A 291 -2.188 -3.069 13.924 1.00 8.73 N ANISOU 2330 N ALA A 291 1124 -212 94 1179 1014 -506 N ATOM 2331 CA ALA A 291 -1.617 -4.359 14.154 1.00 8.82 C ANISOU 2331 CA ALA A 291 1196 -130 223 1143 1009 -343 C ATOM 2332 C ALA A 291 -2.655 -5.229 14.856 1.00 9.52 C ANISOU 2332 C ALA A 291 1160 1 173 1313 1143 -239 C ATOM 2333 O ALA A 291 -3.283 -4.801 15.855 1.00 11.35 O ANISOU 2333 O ALA A 291 1746 -215 285 1296 1271 104 O ATOM 2334 CB ALA A 291 -0.405 -4.218 15.029 1.00 10.85 C ANISOU 2334 CB ALA A 291 1588 -149 310 1420 1113 -399 C ATOM 2335 N VAL A 292 -2.820 -6.446 14.347 1.00 10.09 N ANISOU 2335 N VAL A 292 1342 -19 286 1339 1150 -185 N ATOM 2336 CA VAL A 292 -3.803 -7.417 14.840 1.00 10.39 C ANISOU 2336 CA VAL A 292 1298 -134 199 1325 1323 -248 C ATOM 2337 C VAL A 292 -3.156 -8.794 14.818 1.00 11.24 C ANISOU 2337 C VAL A 292 1535 -100 186 1442 1291 -159 C ATOM 2338 O VAL A 292 -2.138 -9.004 14.147 1.00 12.30 O ANISOU 2338 O VAL A 292 1764 -36 384 1563 1345 -121 O ATOM 2339 CB VAL A 292 -5.070 -7.421 14.011 1.00 12.26 C ANISOU 2339 CB VAL A 292 1561 -275 60 1457 1639 -210 C ATOM 2340 CG1 VAL A 292 -5.766 -6.038 14.062 1.00 12.94 C ANISOU 2340 CG1 VAL A 292 1234 -636 6 1583 2099 -167 C ATOM 2341 CG2 VAL A 292 -4.784 -7.793 12.559 1.00 13.53 C ANISOU 2341 CG2 VAL A 292 1606 -203 178 1825 1707 -508 C ATOM 2342 N THR A 293 -3.770 -9.731 15.532 1.00 11.32 N ANISOU 2342 N THR A 293 1713 -169 263 1425 1160 -204 N ATOM 2343 CA THR A 293 -3.291 -11.104 15.505 1.00 11.28 C ANISOU 2343 CA THR A 293 1561 -337 188 1527 1198 -236 C ATOM 2344 C THR A 293 -4.443 -11.949 14.959 1.00 11.41 C ANISOU 2344 C THR A 293 1468 -300 111 1569 1298 -182 C ATOM 2345 O THR A 293 -5.492 -12.069 15.584 1.00 13.17 O ANISOU 2345 O THR A 293 1880 -157 96 1751 1370 -101 O ATOM 2346 CB THR A 293 -2.918 -11.578 16.910 1.00 12.50 C ANISOU 2346 CB THR A 293 1661 -289 137 1812 1275 -221 C ATOM 2347 OG1 THR A 293 -1.819 -10.781 17.410 1.00 13.67 O ANISOU 2347 OG1 THR A 293 1672 -508 230 2158 1362 -308 O ATOM 2348 CG2 THR A 293 -2.375 -13.016 16.795 1.00 13.45 C ANISOU 2348 CG2 THR A 293 2011 -88 598 1891 1206 -379 C ATOM 2349 N ILE A 294 -4.172 -12.597 13.831 1.00 11.75 N ANISOU 2349 N ILE A 294 1691 -309 80 1421 1352 -233 N ATOM 2350 CA ILE A 294 -5.125 -13.440 13.168 1.00 13.10 C ANISOU 2350 CA ILE A 294 1706 -235 93 1586 1684 -204 C ATOM 2351 C ILE A 294 -4.599 -14.829 13.060 1.00 14.28 C ANISOU 2351 C ILE A 294 1901 -181 216 1718 1807 -239 C ATOM 2352 O ILE A 294 -3.557 -15.063 12.502 1.00 14.35 O ANISOU 2352 O ILE A 294 2032 -99 147 1688 1729 -217 O ATOM 2353 CB ILE A 294 -5.442 -12.881 11.734 1.00 12.61 C ANISOU 2353 CB ILE A 294 1742 -139 46 1527 1522 -273 C ATOM 2354 CG1 ILE A 294 -6.064 -11.475 11.842 1.00 12.81 C ANISOU 2354 CG1 ILE A 294 2115 -163 83 1367 1384 13 C ATOM 2355 CG2 ILE A 294 -6.369 -13.835 10.923 1.00 15.16 C ANISOU 2355 CG2 ILE A 294 2003 -258 39 1714 2040 -139 C ATOM 2356 CD1 ILE A 294 -6.232 -10.743 10.537 1.00 13.83 C ANISOU 2356 CD1 ILE A 294 1627 -544 124 1832 1796 -304 C ATOM 2357 N GLU A 295 -5.351 -15.759 13.620 1.00 14.99 N ANISOU 2357 N GLU A 295 1836 -318 224 1671 2186 -285 N ATOM 2358 CA GLU A 295 -4.924 -17.145 13.708 1.00 17.22 C ANISOU 2358 CA GLU A 295 2295 -103 180 1934 2314 -251 C ATOM 2359 C GLU A 295 -3.478 -17.298 14.159 1.00 15.48 C ANISOU 2359 C GLU A 295 2107 -103 268 1719 2054 -226 C ATOM 2360 O GLU A 295 -2.674 -18.091 13.618 1.00 17.30 O ANISOU 2360 O GLU A 295 2627 -117 303 1501 2444 -71 O ATOM 2361 CB GLU A 295 -5.219 -17.922 12.433 1.00 16.37 C ANISOU 2361 CB GLU A 295 2021 106 165 1851 2347 -515 C ATOM 2362 CG GLU A 295 -6.717 -17.932 12.122 1.00 19.62 C ANISOU 2362 CG GLU A 295 2560 -375 26 2173 2721 -270 C ATOM 2363 CD GLU A 295 -7.065 -18.879 11.000 1.00 22.25 C ANISOU 2363 CD GLU A 295 2692 -378 -29 2666 3094 -208 C ATOM 2364 OE1 GLU A 295 -8.219 -19.298 10.996 1.00 29.39 O ANISOU 2364 OE1 GLU A 295 3284 -585 628 3400 4479 -117 O ATOM 2365 OE2 GLU A 295 -6.189 -19.190 10.144 1.00 26.01 O ANISOU 2365 OE2 GLU A 295 3464 -544 -62 3225 3193 203 O ATOM 2366 N GLY A 296 -3.160 -16.552 15.208 1.00 15.64 N ANISOU 2366 N GLY A 296 2170 -128 422 1678 2094 -196 N ATOM 2367 CA GLY A 296 -1.856 -16.682 15.825 1.00 15.80 C ANISOU 2367 CA GLY A 296 2082 -23 364 1946 1971 -218 C ATOM 2368 C GLY A 296 -0.736 -15.867 15.211 1.00 15.57 C ANISOU 2368 C GLY A 296 1899 -65 433 2009 2006 -290 C ATOM 2369 O GLY A 296 0.404 -15.879 15.742 1.00 18.28 O ANISOU 2369 O GLY A 296 2003 -132 732 2489 2452 -364 O ATOM 2370 N AMET A 297 -0.988 -15.201 14.080 0.50 13.75 N ANISOU 2370 N AMET A 297 1799 10 317 1736 1687 -304 N ATOM 2371 N BMET A 297 -1.029 -15.147 14.133 0.50 15.31 N ANISOU 2371 N BMET A 297 1948 11 358 1937 1930 -220 N ATOM 2372 CA AMET A 297 0.068 -14.411 13.440 0.50 13.37 C ANISOU 2372 CA AMET A 297 1791 43 301 1687 1602 -281 C ATOM 2373 CA BMET A 297 0.002 -14.404 13.435 0.50 15.90 C ANISOU 2373 CA BMET A 297 2036 14 296 2030 1975 -161 C ATOM 2374 C AMET A 297 -0.217 -12.921 13.599 0.50 12.85 C ANISOU 2374 C AMET A 297 1782 26 282 1555 1545 -244 C ATOM 2375 C BMET A 297 -0.226 -12.902 13.578 0.50 14.19 C ANISOU 2375 C BMET A 297 1910 11 296 1736 1744 -173 C ATOM 2376 O AMET A 297 -1.294 -12.457 13.269 0.50 11.81 O ANISOU 2376 O AMET A 297 1529 -77 330 1651 1305 -355 O ATOM 2377 O BMET A 297 -1.282 -12.406 13.219 0.50 13.28 O ANISOU 2377 O BMET A 297 1716 -88 354 1819 1507 -242 O ATOM 2378 CB AMET A 297 0.189 -14.707 11.939 0.50 12.54 C ANISOU 2378 CB AMET A 297 1797 68 241 1470 1498 -287 C ATOM 2379 CB BMET A 297 -0.014 -14.767 11.956 0.50 15.81 C ANISOU 2379 CB BMET A 297 2073 23 264 1918 2015 -122 C ATOM 2380 CG AMET A 297 1.459 -14.122 11.277 0.50 12.69 C ANISOU 2380 CG AMET A 297 1601 -40 171 1721 1498 -350 C ATOM 2381 CG BMET A 297 0.283 -16.252 11.690 0.50 19.47 C ANISOU 2381 CG BMET A 297 2386 7 98 2573 2438 -98 C ATOM 2382 SD AMET A 297 1.519 -14.151 9.434 0.50 15.03 S ANISOU 2382 SD AMET A 297 1967 229 180 2129 1613 -615 S ATOM 2383 SD BMET A 297 0.087 -16.744 9.973 0.50 24.59 S ANISOU 2383 SD BMET A 297 2814 99 153 3506 3022 -33 S ATOM 2384 CE AMET A 297 1.414 -15.899 9.136 0.50 14.63 C ANISOU 2384 CE AMET A 297 1482 -94 345 2080 1996 -432 C ATOM 2385 CE BMET A 297 1.134 -15.470 9.252 0.50 21.93 C ANISOU 2385 CE BMET A 297 2504 54 364 3029 2798 -497 C ATOM 2386 N ARG A 298 0.772 -12.198 14.105 1.00 13.35 N ANISOU 2386 N ARG A 298 1808 28 358 1634 1629 -278 N ATOM 2387 CA ARG A 298 0.745 -10.728 14.152 1.00 12.71 C ANISOU 2387 CA ARG A 298 1687 -42 267 1599 1541 -199 C ATOM 2388 C ARG A 298 0.958 -10.185 12.738 1.00 11.60 C ANISOU 2388 C ARG A 298 1514 12 192 1424 1468 -86 C ATOM 2389 O ARG A 298 1.907 -10.533 12.068 1.00 12.33 O ANISOU 2389 O ARG A 298 1513 -23 383 1567 1605 -41 O ATOM 2390 CB ARG A 298 1.790 -10.202 15.117 1.00 14.41 C ANISOU 2390 CB ARG A 298 2015 -23 303 1793 1667 -204 C ATOM 2391 CG ARG A 298 1.551 -8.829 15.545 1.00 16.91 C ANISOU 2391 CG ARG A 298 2460 -17 241 2249 1714 -206 C ATOM 2392 CD ARG A 298 0.504 -8.734 16.505 1.00 20.34 C ANISOU 2392 CD ARG A 298 2801 61 366 2448 2476 -40 C ATOM 2393 NE ARG A 298 0.335 -7.416 17.122 1.00 18.06 N ANISOU 2393 NE ARG A 298 2876 72 324 2339 1646 -162 N ATOM 2394 CZ ARG A 298 -0.753 -7.091 17.841 1.00 19.93 C ANISOU 2394 CZ ARG A 298 3041 -132 126 2223 2308 98 C ATOM 2395 NH1 ARG A 298 -1.757 -7.983 18.006 1.00 16.16 N ANISOU 2395 NH1 ARG A 298 2016 -391 -316 1747 2376 -194 N ATOM 2396 NH2 ARG A 298 -0.840 -5.868 18.403 1.00 21.38 N ANISOU 2396 NH2 ARG A 298 3340 -64 339 2416 2366 131 N ATOM 2397 N VAL A 299 0.049 -9.324 12.307 1.00 10.41 N ANISOU 2397 N VAL A 299 1465 -40 240 1369 1120 -166 N ATOM 2398 CA VAL A 299 0.113 -8.658 11.041 1.00 10.67 C ANISOU 2398 CA VAL A 299 1532 -57 209 1384 1137 -126 C ATOM 2399 C VAL A 299 -0.425 -7.235 11.114 1.00 8.69 C ANISOU 2399 C VAL A 299 1130 -35 151 1299 870 -292 C ATOM 2400 O VAL A 299 -0.985 -6.809 12.114 1.00 8.97 O ANISOU 2400 O VAL A 299 1362 139 251 1306 738 -221 O ATOM 2401 CB VAL A 299 -0.696 -9.448 9.992 1.00 11.40 C ANISOU 2401 CB VAL A 299 1792 -50 318 1384 1154 -138 C ATOM 2402 CG1 VAL A 299 -0.147 -10.868 9.829 1.00 14.38 C ANISOU 2402 CG1 VAL A 299 2062 -28 296 1823 1579 -108 C ATOM 2403 CG2 VAL A 299 -2.217 -9.505 10.348 1.00 12.77 C ANISOU 2403 CG2 VAL A 299 1987 -150 267 1584 1277 -142 C ATOM 2404 N MET A 300 -0.220 -6.507 10.041 1.00 8.93 N ANISOU 2404 N MET A 300 1104 -87 120 1176 1110 -146 N ATOM 2405 CA MET A 300 -0.722 -5.149 9.903 1.00 8.72 C ANISOU 2405 CA MET A 300 1098 -13 71 1249 966 -211 C ATOM 2406 C MET A 300 -1.747 -5.063 8.798 1.00 8.34 C ANISOU 2406 C MET A 300 962 -33 0 1165 1041 -271 C ATOM 2407 O MET A 300 -1.594 -5.702 7.735 1.00 8.43 O ANISOU 2407 O MET A 300 988 -96 118 1376 837 -319 O ATOM 2408 CB MET A 300 0.430 -4.210 9.589 1.00 7.94 C ANISOU 2408 CB MET A 300 1026 -102 172 1218 769 -449 C ATOM 2409 CG MET A 300 1.589 -4.268 10.573 1.00 8.38 C ANISOU 2409 CG MET A 300 909 -41 -121 1320 952 -185 C ATOM 2410 SD MET A 300 2.926 -3.201 10.122 1.00 13.02 S ANISOU 2410 SD MET A 300 1066 -69 -277 1476 2404 -118 S ATOM 2411 CE MET A 300 4.182 -4.378 9.768 1.00 13.49 C ANISOU 2411 CE MET A 300 1393 -35 479 1947 1785 -330 C ATOM 2412 N LEU A 301 -2.780 -4.259 9.048 1.00 7.70 N ANISOU 2412 N LEU A 301 811 -80 85 1143 970 -228 N ATOM 2413 CA LEU A 301 -3.797 -3.996 8.032 1.00 8.77 C ANISOU 2413 CA LEU A 301 1172 -145 -3 1153 1005 -288 C ATOM 2414 C LEU A 301 -3.769 -2.463 7.734 1.00 9.67 C ANISOU 2414 C LEU A 301 1325 -39 74 1210 1139 -172 C ATOM 2415 O LEU A 301 -3.661 -1.638 8.665 1.00 8.65 O ANISOU 2415 O LEU A 301 1076 0 -46 1233 975 -415 O ATOM 2416 CB LEU A 301 -5.187 -4.350 8.584 1.00 9.41 C ANISOU 2416 CB LEU A 301 1282 -231 -44 1232 1062 -160 C ATOM 2417 CG LEU A 301 -5.433 -5.839 8.918 1.00 9.60 C ANISOU 2417 CG LEU A 301 1128 -352 103 1313 1204 -153 C ATOM 2418 CD1 LEU A 301 -6.811 -6.036 9.538 1.00 11.10 C ANISOU 2418 CD1 LEU A 301 1042 -363 -113 1344 1830 -209 C ATOM 2419 CD2 LEU A 301 -5.177 -6.655 7.682 1.00 12.20 C ANISOU 2419 CD2 LEU A 301 1631 -222 -109 1303 1702 -221 C ATOM 2420 N PHE A 302 -3.753 -2.137 6.452 1.00 8.37 N ANISOU 2420 N PHE A 302 1145 -17 67 1109 924 -333 N ATOM 2421 CA PHE A 302 -3.647 -0.761 5.965 1.00 7.62 C ANISOU 2421 CA PHE A 302 920 -63 169 1109 865 -285 C ATOM 2422 C PHE A 302 -4.701 -0.480 4.920 1.00 8.35 C ANISOU 2422 C PHE A 302 924 -114 52 1236 1012 -236 C ATOM 2423 O PHE A 302 -4.858 -1.260 3.976 1.00 9.74 O ANISOU 2423 O PHE A 302 1265 -105 211 1340 1094 -315 O ATOM 2424 CB PHE A 302 -2.257 -0.549 5.333 1.00 7.54 C ANISOU 2424 CB PHE A 302 891 -68 173 1010 961 -283 C ATOM 2425 CG PHE A 302 -2.034 0.801 4.719 1.00 7.65 C ANISOU 2425 CG PHE A 302 585 3 37 1241 1077 -202 C ATOM 2426 CD1 PHE A 302 -1.801 1.927 5.486 1.00 8.92 C ANISOU 2426 CD1 PHE A 302 996 -17 168 1204 1187 -294 C ATOM 2427 CD2 PHE A 302 -2.069 0.920 3.343 1.00 8.37 C ANISOU 2427 CD2 PHE A 302 1293 -169 56 1177 708 -365 C ATOM 2428 CE1 PHE A 302 -1.636 3.176 4.894 1.00 8.80 C ANISOU 2428 CE1 PHE A 302 1153 -120 204 1309 880 -459 C ATOM 2429 CE2 PHE A 302 -1.897 2.130 2.732 1.00 8.80 C ANISOU 2429 CE2 PHE A 302 719 89 155 1259 1365 -295 C ATOM 2430 CZ PHE A 302 -1.679 3.286 3.518 1.00 7.51 C ANISOU 2430 CZ PHE A 302 823 -120 77 1028 1000 -25 C ATOM 2431 N THR A 303 -5.349 0.682 5.030 1.00 7.60 N ANISOU 2431 N THR A 303 849 -35 -35 1142 897 -278 N ATOM 2432 CA THR A 303 -6.254 1.124 3.980 1.00 8.20 C ANISOU 2432 CA THR A 303 955 -9 262 1306 853 -254 C ATOM 2433 C THR A 303 -5.845 2.464 3.381 1.00 9.39 C ANISOU 2433 C THR A 303 1233 28 128 1236 1099 -278 C ATOM 2434 O THR A 303 -5.366 3.370 4.077 1.00 8.89 O ANISOU 2434 O THR A 303 1118 -161 191 1143 1117 -460 O ATOM 2435 CB THR A 303 -7.675 1.274 4.470 1.00 10.41 C ANISOU 2435 CB THR A 303 1425 18 228 1415 1114 -297 C ATOM 2436 OG1 THR A 303 -7.699 2.091 5.655 1.00 9.43 O ANISOU 2436 OG1 THR A 303 785 -60 213 1730 1066 -309 O ATOM 2437 CG2 THR A 303 -8.327 -0.076 4.745 1.00 10.34 C ANISOU 2437 CG2 THR A 303 1021 -141 397 1656 1251 -60 C ATOM 2438 N HIS A 304 -6.163 2.643 2.111 1.00 9.52 N ANISOU 2438 N HIS A 304 1045 7 94 1371 1200 -245 N ATOM 2439 CA HIS A 304 -5.995 3.949 1.427 1.00 9.12 C ANISOU 2439 CA HIS A 304 1008 40 98 1373 1082 -225 C ATOM 2440 C HIS A 304 -6.774 3.900 0.114 1.00 9.43 C ANISOU 2440 C HIS A 304 1092 27 63 1433 1055 -291 C ATOM 2441 O HIS A 304 -6.845 2.865 -0.543 1.00 10.55 O ANISOU 2441 O HIS A 304 1296 -11 108 1635 1075 -113 O ATOM 2442 CB HIS A 304 -4.508 4.193 1.125 1.00 9.34 C ANISOU 2442 CB HIS A 304 826 133 215 1606 1116 -226 C ATOM 2443 CG HIS A 304 -4.190 5.586 0.716 1.00 9.99 C ANISOU 2443 CG HIS A 304 1215 -256 26 1291 1288 -133 C ATOM 2444 ND1 HIS A 304 -3.507 6.479 1.506 1.00 12.41 N ANISOU 2444 ND1 HIS A 304 1302 178 671 1673 1736 -146 N ATOM 2445 CD2 HIS A 304 -4.440 6.227 -0.456 1.00 5.29 C ANISOU 2445 CD2 HIS A 304 622 -70 253 793 595 -316 C ATOM 2446 CE1 HIS A 304 -3.369 7.627 0.850 1.00 7.89 C ANISOU 2446 CE1 HIS A 304 1212 -223 617 988 797 -338 C ATOM 2447 NE2 HIS A 304 -3.940 7.499 -0.339 1.00 13.79 N ANISOU 2447 NE2 HIS A 304 1662 348 328 1815 1760 -27 N ATOM 2448 N PRO A 305 -7.407 5.021 -0.269 1.00 8.19 N ANISOU 2448 N PRO A 305 862 -48 88 1341 909 -536 N ATOM 2449 CA PRO A 305 -8.076 5.050 -1.598 1.00 8.58 C ANISOU 2449 CA PRO A 305 976 -83 214 1490 792 -428 C ATOM 2450 C PRO A 305 -7.061 5.029 -2.725 1.00 8.99 C ANISOU 2450 C PRO A 305 977 -99 132 1527 909 -538 C ATOM 2451 O PRO A 305 -5.944 5.554 -2.603 1.00 8.88 O ANISOU 2451 O PRO A 305 901 -75 227 1626 847 -508 O ATOM 2452 CB PRO A 305 -8.812 6.392 -1.580 1.00 9.26 C ANISOU 2452 CB PRO A 305 939 -144 79 1752 827 -503 C ATOM 2453 CG PRO A 305 -8.034 7.215 -0.622 1.00 9.38 C ANISOU 2453 CG PRO A 305 952 71 300 1471 1139 -507 C ATOM 2454 CD PRO A 305 -7.575 6.279 0.485 1.00 10.34 C ANISOU 2454 CD PRO A 305 1109 1 451 1528 1291 -208 C ATOM 2455 N LEU A 306 -7.437 4.432 -3.844 1.00 8.95 N ANISOU 2455 N LEU A 306 1009 -7 80 1579 813 -463 N ATOM 2456 CA LEU A 306 -6.584 4.515 -5.018 1.00 10.22 C ANISOU 2456 CA LEU A 306 1001 -41 162 1718 1163 -323 C ATOM 2457 C LEU A 306 -6.667 5.833 -5.773 1.00 11.08 C ANISOU 2457 C LEU A 306 1094 17 115 1808 1308 -345 C ATOM 2458 O LEU A 306 -5.720 6.191 -6.450 1.00 12.44 O ANISOU 2458 O LEU A 306 1082 109 238 2083 1561 -272 O ATOM 2459 CB LEU A 306 -6.789 3.347 -5.970 1.00 12.20 C ANISOU 2459 CB LEU A 306 1208 -63 249 1875 1550 -294 C ATOM 2460 CG LEU A 306 -6.463 1.947 -5.462 1.00 11.45 C ANISOU 2460 CG LEU A 306 1294 169 206 1529 1526 -275 C ATOM 2461 CD1 LEU A 306 -6.904 0.912 -6.492 1.00 12.72 C ANISOU 2461 CD1 LEU A 306 1518 21 -160 1316 1996 -266 C ATOM 2462 CD2 LEU A 306 -5.002 1.764 -5.065 1.00 12.15 C ANISOU 2462 CD2 LEU A 306 1309 -42 8 1559 1747 -489 C ATOM 2463 N ASN A 307 -7.803 6.529 -5.711 1.00 10.63 N ANISOU 2463 N ASN A 307 1070 -64 102 1745 1222 -224 N ATOM 2464 CA ASN A 307 -7.872 7.891 -6.226 1.00 11.47 C ANISOU 2464 CA ASN A 307 1337 49 135 1822 1197 -369 C ATOM 2465 C ASN A 307 -7.599 7.949 -7.706 1.00 11.38 C ANISOU 2465 C ASN A 307 1355 -12 161 1830 1138 -206 C ATOM 2466 O ASN A 307 -6.843 8.784 -8.190 1.00 11.98 O ANISOU 2466 O ASN A 307 1388 143 419 2130 1034 -305 O ATOM 2467 CB ASN A 307 -7.000 8.890 -5.433 1.00 10.32 C ANISOU 2467 CB ASN A 307 1030 4 184 1669 1220 -81 C ATOM 2468 CG ASN A 307 -7.398 10.324 -5.656 1.00 10.86 C ANISOU 2468 CG ASN A 307 1137 -52 100 1702 1287 -334 C ATOM 2469 OD1 ASN A 307 -8.521 10.616 -6.186 1.00 11.61 O ANISOU 2469 OD1 ASN A 307 1323 -99 344 2084 1004 -303 O ATOM 2470 ND2 ASN A 307 -6.520 11.250 -5.209 1.00 11.10 N ANISOU 2470 ND2 ASN A 307 1239 -10 238 1788 1188 -324 N ATOM 2471 N PHE A 308 -8.256 7.053 -8.450 1.00 12.50 N ANISOU 2471 N PHE A 308 1568 63 150 1833 1347 -254 N ATOM 2472 CA PHE A 308 -8.160 7.160 -9.919 1.00 13.07 C ANISOU 2472 CA PHE A 308 1690 -2 199 2028 1246 -415 C ATOM 2473 C PHE A 308 -8.692 8.515 -10.438 1.00 13.55 C ANISOU 2473 C PHE A 308 1656 91 341 2159 1333 -254 C ATOM 2474 O PHE A 308 -8.211 9.030 -11.470 1.00 14.91 O ANISOU 2474 O PHE A 308 1755 145 483 2501 1406 -451 O ATOM 2475 CB PHE A 308 -8.914 6.050 -10.666 1.00 14.26 C ANISOU 2475 CB PHE A 308 1890 -33 132 2128 1399 -411 C ATOM 2476 CG PHE A 308 -8.366 4.660 -10.492 1.00 14.45 C ANISOU 2476 CG PHE A 308 1842 -239 -213 2239 1408 -662 C ATOM 2477 CD1 PHE A 308 -8.978 3.600 -11.174 1.00 16.45 C ANISOU 2477 CD1 PHE A 308 2320 18 -56 2235 1696 -531 C ATOM 2478 CD2 PHE A 308 -7.254 4.395 -9.748 1.00 15.09 C ANISOU 2478 CD2 PHE A 308 2135 285 300 2240 1360 -553 C ATOM 2479 CE1 PHE A 308 -8.537 2.340 -11.032 1.00 16.17 C ANISOU 2479 CE1 PHE A 308 2168 -172 -465 2142 1832 -377 C ATOM 2480 CE2 PHE A 308 -6.809 3.139 -9.643 1.00 15.68 C ANISOU 2480 CE2 PHE A 308 2104 41 -80 2159 1692 -743 C ATOM 2481 CZ PHE A 308 -7.415 2.104 -10.307 1.00 16.96 C ANISOU 2481 CZ PHE A 308 2104 53 -30 2140 2196 -440 C ATOM 2482 N LYS A 309 -9.719 9.056 -9.798 1.00 12.79 N ANISOU 2482 N LYS A 309 1606 224 329 2050 1203 -319 N ATOM 2483 CA LYS A 309 -10.348 10.287 -10.245 1.00 13.95 C ANISOU 2483 CA LYS A 309 1839 83 517 2137 1324 -231 C ATOM 2484 C LYS A 309 -9.525 11.510 -9.989 1.00 14.43 C ANISOU 2484 C LYS A 309 1895 206 554 2177 1410 -313 C ATOM 2485 O LYS A 309 -9.615 12.489 -10.757 1.00 17.20 O ANISOU 2485 O LYS A 309 2275 209 946 2354 1904 -204 O ATOM 2486 CB LYS A 309 -11.748 10.439 -9.646 1.00 12.94 C ANISOU 2486 CB LYS A 309 1668 199 501 2024 1224 -447 C ATOM 2487 CG LYS A 309 -12.697 9.319 -10.015 1.00 13.45 C ANISOU 2487 CG LYS A 309 1741 -184 433 2091 1279 -296 C ATOM 2488 CD LYS A 309 -13.982 9.560 -9.228 1.00 15.69 C ANISOU 2488 CD LYS A 309 1854 15 511 2479 1627 -511 C ATOM 2489 CE LYS A 309 -14.967 8.478 -9.329 1.00 16.99 C ANISOU 2489 CE LYS A 309 1971 -381 261 2917 1565 -512 C ATOM 2490 NZ LYS A 309 -16.240 8.771 -8.497 1.00 13.28 N ANISOU 2490 NZ LYS A 309 1371 -295 307 2774 900 -552 N ATOM 2491 N GLY A 310 -8.682 11.488 -8.982 1.00 13.90 N ANISOU 2491 N GLY A 310 1778 119 468 2120 1381 -234 N ATOM 2492 CA GLY A 310 -7.852 12.627 -8.665 1.00 13.79 C ANISOU 2492 CA GLY A 310 1646 66 466 2153 1440 -226 C ATOM 2493 C GLY A 310 -8.482 13.645 -7.734 1.00 12.23 C ANISOU 2493 C GLY A 310 1345 99 337 1885 1414 -269 C ATOM 2494 O GLY A 310 -9.660 13.541 -7.284 1.00 12.64 O ANISOU 2494 O GLY A 310 1192 -64 511 2273 1337 -400 O ATOM 2495 N ARG A 311 -7.659 14.661 -7.450 1.00 13.39 N ANISOU 2495 N ARG A 311 1488 152 576 2057 1541 -96 N ATOM 2496 CA ARG A 311 -7.937 15.672 -6.461 1.00 13.82 C ANISOU 2496 CA ARG A 311 1719 214 565 1969 1564 -224 C ATOM 2497 C ARG A 311 -8.311 14.948 -5.169 1.00 13.81 C ANISOU 2497 C ARG A 311 1564 143 565 1892 1788 -92 C ATOM 2498 O ARG A 311 -7.577 14.049 -4.791 1.00 12.04 O ANISOU 2498 O ARG A 311 1193 128 485 1979 1402 -291 O ATOM 2499 CB ARG A 311 -8.971 16.679 -6.996 1.00 14.62 C ANISOU 2499 CB ARG A 311 1940 377 554 2052 1560 -163 C ATOM 2500 CG ARG A 311 -8.542 17.384 -8.297 1.00 19.72 C ANISOU 2500 CG ARG A 311 2583 268 665 2475 2434 30 C ATOM 2501 CD ARG A 311 -9.527 18.539 -8.693 1.00 22.76 C ANISOU 2501 CD ARG A 311 3229 385 679 3078 2338 -318 C ATOM 2502 NE ARG A 311 -9.558 19.526 -7.608 1.00 32.40 N ANISOU 2502 NE ARG A 311 5095 574 882 3990 3223 -729 N ATOM 2503 CZ ARG A 311 -9.907 20.795 -7.670 1.00 37.62 C ANISOU 2503 CZ ARG A 311 5647 669 506 4871 3772 -669 C ATOM 2504 NH1 ARG A 311 -10.337 21.361 -8.812 1.00 42.01 N ANISOU 2504 NH1 ARG A 311 5943 555 541 5530 4487 -634 N ATOM 2505 NH2 ARG A 311 -9.819 21.531 -6.561 1.00 37.93 N ANISOU 2505 NH2 ARG A 311 5603 711 610 5054 3751 -559 N ATOM 2506 N TRP A 312 -9.361 15.353 -4.474 1.00 12.18 N ANISOU 2506 N TRP A 312 1479 276 349 1652 1494 -149 N ATOM 2507 CA TRP A 312 -9.711 14.738 -3.214 1.00 11.56 C ANISOU 2507 CA TRP A 312 1405 179 484 1582 1406 -348 C ATOM 2508 C TRP A 312 -10.830 13.732 -3.369 1.00 12.20 C ANISOU 2508 C TRP A 312 1472 121 397 1717 1447 -335 C ATOM 2509 O TRP A 312 -11.336 13.227 -2.373 1.00 11.62 O ANISOU 2509 O TRP A 312 1206 182 374 1784 1422 -305 O ATOM 2510 CB TRP A 312 -10.048 15.784 -2.140 1.00 12.31 C ANISOU 2510 CB TRP A 312 1635 117 660 1565 1476 -450 C ATOM 2511 CG TRP A 312 -8.911 16.604 -1.751 1.00 12.50 C ANISOU 2511 CG TRP A 312 1628 -45 472 1753 1368 -375 C ATOM 2512 CD1 TRP A 312 -8.095 16.411 -0.663 1.00 12.61 C ANISOU 2512 CD1 TRP A 312 1715 77 136 1555 1518 -582 C ATOM 2513 CD2 TRP A 312 -8.440 17.779 -2.387 1.00 13.26 C ANISOU 2513 CD2 TRP A 312 1650 122 302 1847 1539 -628 C ATOM 2514 NE1 TRP A 312 -7.127 17.374 -0.621 1.00 12.97 N ANISOU 2514 NE1 TRP A 312 1646 162 407 1587 1694 -343 N ATOM 2515 CE2 TRP A 312 -7.315 18.240 -1.650 1.00 14.84 C ANISOU 2515 CE2 TRP A 312 1990 -352 276 1687 1961 -360 C ATOM 2516 CE3 TRP A 312 -8.872 18.519 -3.461 1.00 15.32 C ANISOU 2516 CE3 TRP A 312 2059 -436 717 1817 1943 -542 C ATOM 2517 CZ2 TRP A 312 -6.589 19.374 -2.007 1.00 16.83 C ANISOU 2517 CZ2 TRP A 312 2168 -15 339 1933 2290 -232 C ATOM 2518 CZ3 TRP A 312 -8.120 19.617 -3.863 1.00 16.48 C ANISOU 2518 CZ3 TRP A 312 2278 -251 574 2123 1859 -751 C ATOM 2519 CH2 TRP A 312 -7.016 20.041 -3.118 1.00 16.18 C ANISOU 2519 CH2 TRP A 312 2161 -772 314 1963 2024 -562 C ATOM 2520 N LEU A 313 -11.246 13.409 -4.607 1.00 11.12 N ANISOU 2520 N LEU A 313 1243 2 481 1669 1314 -363 N ATOM 2521 CA LEU A 313 -12.368 12.489 -4.732 1.00 12.30 C ANISOU 2521 CA LEU A 313 1506 110 275 1745 1421 -343 C ATOM 2522 C LEU A 313 -12.066 11.124 -4.081 1.00 11.10 C ANISOU 2522 C LEU A 313 1295 32 265 1809 1112 -373 C ATOM 2523 O LEU A 313 -12.883 10.587 -3.350 1.00 11.70 O ANISOU 2523 O LEU A 313 1197 -131 298 1996 1250 -406 O ATOM 2524 CB LEU A 313 -12.739 12.347 -6.205 1.00 12.69 C ANISOU 2524 CB LEU A 313 1606 138 267 1803 1410 -371 C ATOM 2525 CG LEU A 313 -13.297 13.637 -6.848 1.00 15.21 C ANISOU 2525 CG LEU A 313 2261 371 400 2112 1405 -403 C ATOM 2526 CD1 LEU A 313 -13.608 13.469 -8.357 1.00 19.02 C ANISOU 2526 CD1 LEU A 313 2599 600 391 2594 2030 -710 C ATOM 2527 CD2 LEU A 313 -14.521 14.091 -6.093 1.00 17.00 C ANISOU 2527 CD2 LEU A 313 2405 486 440 2269 1785 -484 C ATOM 2528 N ARG A 314 -10.912 10.548 -4.399 1.00 10.02 N ANISOU 2528 N ARG A 314 1104 80 310 1764 937 -422 N ATOM 2529 CA ARG A 314 -10.405 9.424 -3.632 1.00 10.10 C ANISOU 2529 CA ARG A 314 1075 38 215 1599 1160 -285 C ATOM 2530 C ARG A 314 -11.364 8.253 -3.602 1.00 10.27 C ANISOU 2530 C ARG A 314 1064 84 238 1680 1159 -327 C ATOM 2531 O ARG A 314 -11.717 7.679 -2.546 1.00 10.89 O ANISOU 2531 O ARG A 314 1023 -162 314 1892 1222 -343 O ATOM 2532 CB ARG A 314 -9.989 9.945 -2.252 1.00 8.82 C ANISOU 2532 CB ARG A 314 1091 -20 227 1427 833 -216 C ATOM 2533 CG ARG A 314 -8.716 10.781 -2.333 1.00 11.09 C ANISOU 2533 CG ARG A 314 1152 92 397 1654 1408 -337 C ATOM 2534 CD ARG A 314 -8.299 11.418 -1.029 1.00 10.40 C ANISOU 2534 CD ARG A 314 1177 211 145 1499 1272 -276 C ATOM 2535 NE ARG A 314 -9.328 12.358 -0.584 1.00 11.12 N ANISOU 2535 NE ARG A 314 1323 22 175 1611 1289 -81 N ATOM 2536 CZ ARG A 314 -9.278 13.076 0.512 1.00 10.62 C ANISOU 2536 CZ ARG A 314 1298 -31 331 1396 1341 -372 C ATOM 2537 NH1 ARG A 314 -8.174 13.089 1.271 1.00 9.94 N ANISOU 2537 NH1 ARG A 314 791 206 -11 1826 1158 -681 N ATOM 2538 NH2 ARG A 314 -10.324 13.828 0.855 1.00 11.08 N ANISOU 2538 NH2 ARG A 314 1314 -41 8 1715 1180 -358 N ATOM 2539 N ASP A 315 -11.672 7.827 -4.830 1.00 10.73 N ANISOU 2539 N ASP A 315 1189 64 336 1698 1190 -430 N ATOM 2540 CA ASP A 315 -12.388 6.576 -5.086 1.00 10.52 C ANISOU 2540 CA ASP A 315 1049 -6 247 1756 1189 -355 C ATOM 2541 C ASP A 315 -11.497 5.373 -4.714 1.00 10.66 C ANISOU 2541 C ASP A 315 1106 -76 223 1790 1153 -302 C ATOM 2542 O ASP A 315 -10.270 5.471 -4.591 1.00 10.97 O ANISOU 2542 O ASP A 315 948 -290 119 1967 1254 -352 O ATOM 2543 CB ASP A 315 -12.735 6.502 -6.583 1.00 11.45 C ANISOU 2543 CB ASP A 315 1198 8 334 1902 1250 -208 C ATOM 2544 CG ASP A 315 -11.539 6.805 -7.437 1.00 12.11 C ANISOU 2544 CG ASP A 315 1319 161 399 1930 1349 -597 C ATOM 2545 OD1 ASP A 315 -10.905 5.869 -7.964 1.00 13.19 O ANISOU 2545 OD1 ASP A 315 1762 163 63 1869 1378 -342 O ATOM 2546 OD2 ASP A 315 -11.095 7.968 -7.529 1.00 13.89 O ANISOU 2546 OD2 ASP A 315 1425 -172 344 2256 1594 -251 O ATOM 2547 N ARG A 316 -12.153 4.229 -4.642 1.00 10.42 N ANISOU 2547 N ARG A 316 982 -109 114 1687 1289 -312 N ATOM 2548 CA ARG A 316 -11.545 2.930 -4.598 1.00 9.57 C ANISOU 2548 CA ARG A 316 945 23 147 1624 1065 -514 C ATOM 2549 C ARG A 316 -10.682 2.665 -3.346 1.00 9.92 C ANISOU 2549 C ARG A 316 1090 -43 158 1646 1033 -466 C ATOM 2550 O ARG A 316 -9.489 2.429 -3.427 1.00 10.55 O ANISOU 2550 O ARG A 316 975 -39 155 1995 1036 -522 O ATOM 2551 CB ARG A 316 -10.802 2.652 -5.891 1.00 10.10 C ANISOU 2551 CB ARG A 316 967 129 69 1775 1094 -548 C ATOM 2552 CG ARG A 316 -11.729 2.584 -7.100 1.00 11.26 C ANISOU 2552 CG ARG A 316 1375 235 36 1669 1233 -439 C ATOM 2553 CD ARG A 316 -10.966 2.368 -8.390 1.00 13.86 C ANISOU 2553 CD ARG A 316 1654 119 -91 2157 1452 -625 C ATOM 2554 NE ARG A 316 -11.839 2.150 -9.516 1.00 16.62 N ANISOU 2554 NE ARG A 316 2107 80 -94 2601 1604 -737 N ATOM 2555 CZ ARG A 316 -12.410 3.117 -10.207 1.00 18.56 C ANISOU 2555 CZ ARG A 316 2401 -92 -12 2617 2032 -1086 C ATOM 2556 NH1 ARG A 316 -12.258 4.386 -9.862 1.00 17.59 N ANISOU 2556 NH1 ARG A 316 2165 -337 188 2435 2081 -1022 N ATOM 2557 NH2 ARG A 316 -13.195 2.815 -11.261 1.00 21.72 N ANISOU 2557 NH2 ARG A 316 3028 -296 -149 3005 2220 -1345 N ATOM 2558 N LEU A 317 -11.368 2.669 -2.212 1.00 9.12 N ANISOU 2558 N LEU A 317 963 -26 155 1505 994 -444 N ATOM 2559 CA LEU A 317 -10.739 2.317 -0.939 1.00 10.04 C ANISOU 2559 CA LEU A 317 1129 -51 217 1586 1098 -406 C ATOM 2560 C LEU A 317 -10.231 0.881 -1.012 1.00 9.57 C ANISOU 2560 C LEU A 317 925 -4 331 1562 1147 -455 C ATOM 2561 O LEU A 317 -11.009 -0.033 -1.166 1.00 10.98 O ANISOU 2561 O LEU A 317 1173 -140 -2 1579 1419 -441 O ATOM 2562 CB LEU A 317 -11.759 2.448 0.183 1.00 9.73 C ANISOU 2562 CB LEU A 317 1046 123 133 1590 1061 -421 C ATOM 2563 CG LEU A 317 -11.196 2.241 1.596 1.00 9.35 C ANISOU 2563 CG LEU A 317 1179 175 103 1296 1077 -386 C ATOM 2564 CD1 LEU A 317 -10.223 3.338 1.948 1.00 12.21 C ANISOU 2564 CD1 LEU A 317 1290 46 221 1811 1536 -504 C ATOM 2565 CD2 LEU A 317 -12.348 2.122 2.551 1.00 11.87 C ANISOU 2565 CD2 LEU A 317 1780 -172 91 1490 1238 -347 C ATOM 2566 N ASN A 318 -8.913 0.698 -0.825 1.00 10.54 N ANISOU 2566 N ASN A 318 871 -167 265 1679 1454 -527 N ATOM 2567 CA ASN A 318 -8.282 -0.620 -0.827 1.00 10.14 C ANISOU 2567 CA ASN A 318 883 -60 360 1674 1296 -401 C ATOM 2568 C ASN A 318 -7.687 -0.977 0.520 1.00 9.48 C ANISOU 2568 C ASN A 318 863 -54 215 1605 1133 -427 C ATOM 2569 O ASN A 318 -7.204 -0.127 1.261 1.00 10.37 O ANISOU 2569 O ASN A 318 1153 25 402 1588 1198 -624 O ATOM 2570 CB ASN A 318 -7.208 -0.738 -1.942 1.00 11.56 C ANISOU 2570 CB ASN A 318 1120 -2 619 1973 1296 -464 C ATOM 2571 CG ASN A 318 -7.788 -1.106 -3.243 1.00 14.16 C ANISOU 2571 CG ASN A 318 1447 133 369 2350 1583 -345 C ATOM 2572 OD1 ASN A 318 -8.667 -0.353 -3.828 1.00 19.88 O ANISOU 2572 OD1 ASN A 318 2309 385 773 3153 2090 -503 O ATOM 2573 ND2 ASN A 318 -7.406 -2.201 -3.716 1.00 11.43 N ANISOU 2573 ND2 ASN A 318 1513 500 414 1770 1057 -732 N ATOM 2574 N LEU A 319 -7.707 -2.284 0.775 1.00 8.17 N ANISOU 2574 N LEU A 319 918 -108 240 1264 919 -641 N ATOM 2575 CA LEU A 319 -7.180 -2.912 2.003 1.00 8.22 C ANISOU 2575 CA LEU A 319 931 -128 211 1327 864 -305 C ATOM 2576 C LEU A 319 -5.977 -3.761 1.675 1.00 8.03 C ANISOU 2576 C LEU A 319 982 -169 134 1291 775 -406 C ATOM 2577 O LEU A 319 -5.964 -4.508 0.654 1.00 10.32 O ANISOU 2577 O LEU A 319 1253 -115 64 1494 1172 -270 O ATOM 2578 CB LEU A 319 -8.292 -3.835 2.581 1.00 8.93 C ANISOU 2578 CB LEU A 319 975 -81 228 1325 1091 -191 C ATOM 2579 CG LEU A 319 -7.906 -4.600 3.844 1.00 9.78 C ANISOU 2579 CG LEU A 319 914 150 282 1577 1224 -397 C ATOM 2580 CD1 LEU A 319 -7.544 -3.742 5.011 1.00 12.40 C ANISOU 2580 CD1 LEU A 319 1001 -63 199 1771 1937 46 C ATOM 2581 CD2 LEU A 319 -9.080 -5.483 4.209 1.00 11.22 C ANISOU 2581 CD2 LEU A 319 1366 -159 238 1655 1240 -383 C ATOM 2582 N TRP A 320 -4.953 -3.603 2.515 1.00 7.44 N ANISOU 2582 N TRP A 320 870 -184 125 1293 664 -421 N ATOM 2583 CA TRP A 320 -3.680 -4.248 2.380 1.00 8.02 C ANISOU 2583 CA TRP A 320 950 -93 48 1235 860 -170 C ATOM 2584 C TRP A 320 -3.348 -5.001 3.646 1.00 8.81 C ANISOU 2584 C TRP A 320 1132 -102 92 1207 1006 -120 C ATOM 2585 O TRP A 320 -3.658 -4.557 4.776 1.00 9.54 O ANISOU 2585 O TRP A 320 965 -11 109 1314 1342 -92 O ATOM 2586 CB TRP A 320 -2.550 -3.178 2.165 1.00 8.52 C ANISOU 2586 CB TRP A 320 1059 -216 120 1313 863 -146 C ATOM 2587 CG TRP A 320 -2.774 -2.376 0.927 1.00 9.62 C ANISOU 2587 CG TRP A 320 1020 -215 236 1451 1181 -17 C ATOM 2588 CD1 TRP A 320 -3.571 -1.264 0.777 1.00 10.23 C ANISOU 2588 CD1 TRP A 320 1300 -214 368 1606 978 -47 C ATOM 2589 CD2 TRP A 320 -2.247 -2.688 -0.343 1.00 9.59 C ANISOU 2589 CD2 TRP A 320 1048 -204 273 1265 1330 -545 C ATOM 2590 NE1 TRP A 320 -3.553 -0.862 -0.543 1.00 11.15 N ANISOU 2590 NE1 TRP A 320 1268 -172 164 1744 1223 -232 N ATOM 2591 CE2 TRP A 320 -2.743 -1.729 -1.254 1.00 8.51 C ANISOU 2591 CE2 TRP A 320 919 -225 211 1406 906 -444 C ATOM 2592 CE3 TRP A 320 -1.352 -3.668 -0.812 1.00 9.64 C ANISOU 2592 CE3 TRP A 320 1369 -148 -46 1286 1008 -23 C ATOM 2593 CZ2 TRP A 320 -2.360 -1.723 -2.588 1.00 11.56 C ANISOU 2593 CZ2 TRP A 320 1323 -270 90 1818 1248 -304 C ATOM 2594 CZ3 TRP A 320 -0.979 -3.658 -2.119 1.00 10.52 C ANISOU 2594 CZ3 TRP A 320 1213 -353 -35 1548 1236 -82 C ATOM 2595 CH2 TRP A 320 -1.478 -2.697 -3.003 1.00 11.52 C ANISOU 2595 CH2 TRP A 320 1429 -292 180 1625 1320 28 C ATOM 2596 N LEU A 321 -2.616 -6.095 3.461 1.00 8.99 N ANISOU 2596 N LEU A 321 1225 -60 107 1261 928 -132 N ATOM 2597 CA LEU A 321 -2.179 -6.987 4.574 1.00 8.45 C ANISOU 2597 CA LEU A 321 1029 -112 222 1127 1053 -189 C ATOM 2598 C LEU A 321 -0.656 -7.114 4.507 1.00 9.24 C ANISOU 2598 C LEU A 321 1103 -73 195 1358 1050 -194 C ATOM 2599 O LEU A 321 -0.122 -7.461 3.440 1.00 9.17 O ANISOU 2599 O LEU A 321 994 -25 181 1367 1123 -171 O ATOM 2600 CB LEU A 321 -2.819 -8.379 4.307 1.00 9.07 C ANISOU 2600 CB LEU A 321 1048 -230 318 1249 1148 -45 C ATOM 2601 CG LEU A 321 -2.374 -9.541 5.130 1.00 9.45 C ANISOU 2601 CG LEU A 321 1185 48 141 1267 1138 -264 C ATOM 2602 CD1 LEU A 321 -2.767 -9.377 6.601 1.00 11.26 C ANISOU 2602 CD1 LEU A 321 1854 -423 -83 1346 1077 -77 C ATOM 2603 CD2 LEU A 321 -2.875 -10.832 4.565 1.00 9.49 C ANISOU 2603 CD2 LEU A 321 1201 67 434 1244 1159 -33 C ATOM 2604 N THR A 322 0.070 -6.945 5.620 1.00 7.89 N ANISOU 2604 N THR A 322 933 63 168 1174 891 -232 N ATOM 2605 CA THR A 322 1.486 -7.191 5.541 1.00 8.05 C ANISOU 2605 CA THR A 322 913 -80 193 1282 862 -229 C ATOM 2606 C THR A 322 1.983 -7.754 6.854 1.00 8.43 C ANISOU 2606 C THR A 322 843 22 83 1421 939 -223 C ATOM 2607 O THR A 322 1.499 -7.391 7.931 1.00 10.42 O ANISOU 2607 O THR A 322 1307 28 22 1620 1032 -326 O ATOM 2608 CB THR A 322 2.264 -5.879 5.170 1.00 9.29 C ANISOU 2608 CB THR A 322 1202 -34 184 1327 997 -358 C ATOM 2609 OG1 THR A 322 3.666 -6.111 5.227 1.00 8.78 O ANISOU 2609 OG1 THR A 322 676 -224 176 1620 1040 -405 O ATOM 2610 CG2 THR A 322 1.987 -4.722 6.173 1.00 10.29 C ANISOU 2610 CG2 THR A 322 1040 -216 337 1627 1240 -173 C ATOM 2611 N ASP A 323 2.994 -8.594 6.758 1.00 9.59 N ANISOU 2611 N ASP A 323 1199 181 129 1349 1093 -73 N ATOM 2612 CA ASP A 323 3.782 -9.055 7.912 1.00 9.46 C ANISOU 2612 CA ASP A 323 1032 64 17 1530 1031 -169 C ATOM 2613 C ASP A 323 5.106 -8.351 8.065 1.00 9.95 C ANISOU 2613 C ASP A 323 1264 82 -34 1388 1128 -27 C ATOM 2614 O ASP A 323 6.010 -8.878 8.725 1.00 10.85 O ANISOU 2614 O ASP A 323 1305 279 49 1374 1444 -267 O ATOM 2615 CB ASP A 323 4.053 -10.581 7.848 1.00 9.24 C ANISOU 2615 CB ASP A 323 1066 93 -63 1512 933 -114 C ATOM 2616 CG ASP A 323 4.917 -10.947 6.687 1.00 9.04 C ANISOU 2616 CG ASP A 323 962 119 -23 1527 944 -264 C ATOM 2617 OD1 ASP A 323 5.431 -12.108 6.640 1.00 10.87 O ANISOU 2617 OD1 ASP A 323 1415 282 27 1522 1191 -435 O ATOM 2618 OD2 ASP A 323 5.182 -10.074 5.780 1.00 9.79 O ANISOU 2618 OD2 ASP A 323 1086 -28 162 1435 1198 -359 O ATOM 2619 N ASN A 324 5.188 -7.145 7.503 1.00 9.61 N ANISOU 2619 N ASN A 324 1188 136 123 1322 1138 -167 N ATOM 2620 CA ASN A 324 6.439 -6.386 7.465 1.00 9.99 C ANISOU 2620 CA ASN A 324 1191 9 79 1499 1105 -211 C ATOM 2621 C ASN A 324 7.501 -6.949 6.527 1.00 10.09 C ANISOU 2621 C ASN A 324 1169 4 75 1518 1146 -218 C ATOM 2622 O ASN A 324 8.645 -6.476 6.538 1.00 11.18 O ANISOU 2622 O ASN A 324 982 -271 -93 2088 1176 20 O ATOM 2623 CB ASN A 324 7.001 -6.185 8.905 1.00 10.29 C ANISOU 2623 CB ASN A 324 1410 61 55 1446 1052 -265 C ATOM 2624 CG ASN A 324 7.826 -4.890 9.044 1.00 12.16 C ANISOU 2624 CG ASN A 324 1411 -127 9 1994 1214 -206 C ATOM 2625 OD1 ASN A 324 8.908 -4.853 9.712 1.00 14.92 O ANISOU 2625 OD1 ASN A 324 1816 -408 113 2811 1041 -774 O ATOM 2626 ND2 ASN A 324 7.345 -3.867 8.451 1.00 7.94 N ANISOU 2626 ND2 ASN A 324 1039 -273 0 1259 715 -400 N ATOM 2627 N GLN A 325 7.094 -7.869 5.656 1.00 10.55 N ANISOU 2627 N GLN A 325 863 -70 -8 1975 1168 -175 N ATOM 2628 CA GLN A 325 7.933 -8.464 4.645 1.00 10.12 C ANISOU 2628 CA GLN A 325 1217 -41 -63 1668 959 -215 C ATOM 2629 C GLN A 325 7.169 -8.479 3.309 1.00 9.65 C ANISOU 2629 C GLN A 325 1243 -24 -69 1407 1016 -182 C ATOM 2630 O GLN A 325 7.528 -7.729 2.362 1.00 11.41 O ANISOU 2630 O GLN A 325 1423 -246 -100 1832 1079 -294 O ATOM 2631 CB GLN A 325 8.364 -9.897 5.070 1.00 9.67 C ANISOU 2631 CB GLN A 325 1003 112 29 1840 831 -175 C ATOM 2632 CG GLN A 325 8.864 -10.022 6.507 1.00 11.19 C ANISOU 2632 CG GLN A 325 1356 154 117 1790 1105 -508 C ATOM 2633 CD GLN A 325 9.333 -11.411 6.851 1.00 11.39 C ANISOU 2633 CD GLN A 325 1343 110 -82 1737 1245 -184 C ATOM 2634 OE1 GLN A 325 10.529 -11.616 7.155 1.00 12.97 O ANISOU 2634 OE1 GLN A 325 1308 222 -301 1991 1627 -184 O ATOM 2635 NE2 GLN A 325 8.429 -12.372 6.793 1.00 11.37 N ANISOU 2635 NE2 GLN A 325 1448 16 38 1552 1318 -131 N ATOM 2636 N ARG A 326 6.111 -9.296 3.268 1.00 8.82 N ANISOU 2636 N ARG A 326 1224 -180 113 1185 943 -88 N ATOM 2637 CA ARG A 326 5.216 -9.426 2.136 1.00 9.06 C ANISOU 2637 CA ARG A 326 1206 -181 -30 1189 1046 -165 C ATOM 2638 C ARG A 326 4.094 -8.423 2.269 1.00 9.30 C ANISOU 2638 C ARG A 326 1215 -223 -58 1291 1027 -98 C ATOM 2639 O ARG A 326 3.711 -8.051 3.386 1.00 9.84 O ANISOU 2639 O ARG A 326 1252 -241 191 1444 1041 -189 O ATOM 2640 CB ARG A 326 4.672 -10.840 2.047 1.00 11.69 C ANISOU 2640 CB ARG A 326 1461 -97 12 1560 1418 -204 C ATOM 2641 CG ARG A 326 5.760 -11.929 2.057 1.00 9.74 C ANISOU 2641 CG ARG A 326 1330 -183 -40 1292 1078 69 C ATOM 2642 CD ARG A 326 5.708 -12.749 3.319 1.00 11.76 C ANISOU 2642 CD ARG A 326 1355 68 98 1577 1533 -54 C ATOM 2643 NE ARG A 326 6.921 -13.522 3.448 1.00 12.48 N ANISOU 2643 NE ARG A 326 1560 -38 61 1452 1727 -168 N ATOM 2644 CZ ARG A 326 7.067 -14.542 4.239 1.00 11.73 C ANISOU 2644 CZ ARG A 326 1339 -230 191 1765 1350 -190 C ATOM 2645 NH1 ARG A 326 6.129 -14.862 5.133 1.00 13.06 N ANISOU 2645 NH1 ARG A 326 1422 508 279 1936 1601 27 N ATOM 2646 NH2 ARG A 326 8.200 -15.194 4.203 1.00 11.54 N ANISOU 2646 NH2 ARG A 326 1435 -391 119 1584 1365 77 N ATOM 2647 N ILE A 327 3.584 -7.952 1.137 1.00 9.44 N ANISOU 2647 N ILE A 327 1227 -171 -130 1325 1032 -74 N ATOM 2648 CA ILE A 327 2.560 -6.952 1.117 1.00 8.71 C ANISOU 2648 CA ILE A 327 1111 -220 5 1238 959 -261 C ATOM 2649 C ILE A 327 1.502 -7.365 0.110 1.00 8.98 C ANISOU 2649 C ILE A 327 1027 -63 66 1436 949 -184 C ATOM 2650 O ILE A 327 1.746 -7.361 -1.087 1.00 9.40 O ANISOU 2650 O ILE A 327 932 -93 154 1789 849 -365 O ATOM 2651 CB ILE A 327 3.142 -5.571 0.819 1.00 9.08 C ANISOU 2651 CB ILE A 327 1068 -219 48 1323 1057 -202 C ATOM 2652 CG1 ILE A 327 4.238 -5.133 1.820 1.00 9.84 C ANISOU 2652 CG1 ILE A 327 1225 -368 -160 1203 1308 -57 C ATOM 2653 CG2 ILE A 327 1.989 -4.533 0.760 1.00 10.13 C ANISOU 2653 CG2 ILE A 327 1318 -110 -190 1433 1097 -273 C ATOM 2654 CD1 ILE A 327 4.966 -3.927 1.329 1.00 11.31 C ANISOU 2654 CD1 ILE A 327 1385 -386 48 1784 1126 -539 C ATOM 2655 N TYR A 328 0.330 -7.700 0.631 1.00 9.15 N ANISOU 2655 N TYR A 328 1024 -31 160 1441 1012 -260 N ATOM 2656 CA TYR A 328 -0.750 -8.332 -0.111 1.00 9.04 C ANISOU 2656 CA TYR A 328 996 -159 64 1311 1124 -206 C ATOM 2657 C TYR A 328 -1.913 -7.357 -0.265 1.00 8.92 C ANISOU 2657 C TYR A 328 1150 -111 20 1297 941 -293 C ATOM 2658 O TYR A 328 -2.390 -6.772 0.710 1.00 9.75 O ANISOU 2658 O TYR A 328 1161 33 91 1530 1011 -132 O ATOM 2659 CB TYR A 328 -1.259 -9.590 0.647 1.00 10.27 C ANISOU 2659 CB TYR A 328 1177 25 159 1602 1122 -292 C ATOM 2660 CG TYR A 328 -2.336 -10.321 -0.155 1.00 9.87 C ANISOU 2660 CG TYR A 328 955 44 154 1510 1284 -266 C ATOM 2661 CD1 TYR A 328 -2.027 -11.096 -1.238 1.00 10.12 C ANISOU 2661 CD1 TYR A 328 823 -233 8 1631 1391 -425 C ATOM 2662 CD2 TYR A 328 -3.676 -10.174 0.156 1.00 11.20 C ANISOU 2662 CD2 TYR A 328 1130 134 183 1772 1351 -504 C ATOM 2663 CE1 TYR A 328 -3.023 -11.694 -1.974 1.00 11.64 C ANISOU 2663 CE1 TYR A 328 1178 -213 11 1854 1390 -691 C ATOM 2664 CE2 TYR A 328 -4.676 -10.765 -0.583 1.00 11.89 C ANISOU 2664 CE2 TYR A 328 1182 -134 38 1847 1488 -312 C ATOM 2665 CZ TYR A 328 -4.337 -11.542 -1.619 1.00 11.99 C ANISOU 2665 CZ TYR A 328 1505 -423 -127 1837 1211 -270 C ATOM 2666 OH TYR A 328 -5.366 -12.113 -2.366 1.00 13.59 O ANISOU 2666 OH TYR A 328 1342 -341 -92 2141 1678 -741 O ATOM 2667 N ASN A 329 -2.415 -7.202 -1.489 1.00 10.90 N ANISOU 2667 N ASN A 329 1221 -81 113 1592 1326 -343 N ATOM 2668 CA ASN A 329 -3.612 -6.412 -1.752 1.00 10.83 C ANISOU 2668 CA ASN A 329 1223 -113 160 1535 1354 -300 C ATOM 2669 C ASN A 329 -4.845 -7.271 -1.564 1.00 10.51 C ANISOU 2669 C ASN A 329 1183 -122 64 1505 1305 -367 C ATOM 2670 O ASN A 329 -5.119 -8.174 -2.359 1.00 11.51 O ANISOU 2670 O ASN A 329 1375 -116 -84 1822 1174 -450 O ATOM 2671 CB ASN A 329 -3.620 -5.873 -3.154 1.00 13.04 C ANISOU 2671 CB ASN A 329 1300 -235 128 1824 1828 -371 C ATOM 2672 CG ASN A 329 -4.868 -5.099 -3.428 1.00 14.83 C ANISOU 2672 CG ASN A 329 1884 285 122 2144 1605 -568 C ATOM 2673 OD1 ASN A 329 -5.244 -4.243 -2.666 1.00 24.34 O ANISOU 2673 OD1 ASN A 329 2555 888 -199 3547 3145 -871 O ATOM 2674 ND2 ASN A 329 -5.461 -5.328 -4.544 1.00 26.84 N ANISOU 2674 ND2 ASN A 329 3474 963 -307 3669 3052 -1423 N ATOM 2675 N VAL A 330 -5.533 -7.050 -0.437 1.00 10.41 N ANISOU 2675 N VAL A 330 1222 -50 26 1406 1326 -414 N ATOM 2676 CA VAL A 330 -6.732 -7.815 -0.126 1.00 10.47 C ANISOU 2676 CA VAL A 330 1027 -70 64 1487 1462 -280 C ATOM 2677 C VAL A 330 -7.830 -7.477 -1.153 1.00 11.27 C ANISOU 2677 C VAL A 330 1065 -193 31 1566 1650 -247 C ATOM 2678 O VAL A 330 -8.557 -8.351 -1.651 1.00 12.92 O ANISOU 2678 O VAL A 330 1129 -184 -171 1774 2004 -342 O ATOM 2679 CB VAL A 330 -7.217 -7.559 1.289 1.00 10.37 C ANISOU 2679 CB VAL A 330 963 -98 58 1284 1691 -328 C ATOM 2680 CG1 VAL A 330 -8.427 -8.384 1.541 1.00 11.92 C ANISOU 2680 CG1 VAL A 330 1188 -9 148 1577 1762 -321 C ATOM 2681 CG2 VAL A 330 -6.165 -7.961 2.275 1.00 11.01 C ANISOU 2681 CG2 VAL A 330 1206 -2 -5 1445 1533 37 C ATOM 2682 N GLY A 331 -7.930 -6.194 -1.468 1.00 12.00 N ANISOU 2682 N GLY A 331 1265 -122 -39 1622 1670 -368 N ATOM 2683 CA GLY A 331 -8.789 -5.706 -2.540 1.00 11.70 C ANISOU 2683 CA GLY A 331 1239 46 10 1660 1544 -437 C ATOM 2684 C GLY A 331 -9.543 -4.456 -2.159 1.00 11.35 C ANISOU 2684 C GLY A 331 1271 -70 -1 1613 1428 -411 C ATOM 2685 O GLY A 331 -9.216 -3.793 -1.157 1.00 11.38 O ANISOU 2685 O GLY A 331 1344 -97 115 1650 1327 -672 O ATOM 2686 N GLN A 332 -10.563 -4.175 -2.954 1.00 10.53 N ANISOU 2686 N GLN A 332 1136 -31 -48 1703 1160 -489 N ATOM 2687 CA GLN A 332 -11.328 -2.934 -2.846 1.00 10.98 C ANISOU 2687 CA GLN A 332 1122 -184 38 1761 1287 -492 C ATOM 2688 C GLN A 332 -12.487 -3.149 -1.844 1.00 10.75 C ANISOU 2688 C GLN A 332 1009 -43 24 1761 1311 -438 C ATOM 2689 O GLN A 332 -13.354 -4.045 -2.050 1.00 13.02 O ANISOU 2689 O GLN A 332 1266 -460 102 1962 1717 -217 O ATOM 2690 CB GLN A 332 -11.878 -2.539 -4.190 1.00 10.54 C ANISOU 2690 CB GLN A 332 942 -126 114 1931 1129 -556 C ATOM 2691 CG GLN A 332 -12.621 -1.225 -4.155 1.00 10.41 C ANISOU 2691 CG GLN A 332 1182 -178 30 1718 1053 -722 C ATOM 2692 CD GLN A 332 -13.158 -0.783 -5.499 1.00 12.35 C ANISOU 2692 CD GLN A 332 1444 -81 182 2135 1110 -383 C ATOM 2693 OE1 GLN A 332 -12.416 -0.718 -6.488 1.00 15.63 O ANISOU 2693 OE1 GLN A 332 1752 304 478 2671 1515 -95 O ATOM 2694 NE2 GLN A 332 -14.402 -0.386 -5.514 1.00 14.24 N ANISOU 2694 NE2 GLN A 332 1267 95 -256 2609 1532 18 N ATOM 2695 N VAL A 333 -12.473 -2.338 -0.788 1.00 11.52 N ANISOU 2695 N VAL A 333 1025 -34 56 1782 1566 -409 N ATOM 2696 CA VAL A 333 -13.493 -2.410 0.267 1.00 10.91 C ANISOU 2696 CA VAL A 333 1019 -92 121 1655 1470 -366 C ATOM 2697 C VAL A 333 -14.730 -1.614 -0.197 1.00 11.67 C ANISOU 2697 C VAL A 333 1086 -70 114 1756 1589 -338 C ATOM 2698 O VAL A 333 -15.846 -2.006 0.054 1.00 12.93 O ANISOU 2698 O VAL A 333 1083 -272 210 1905 1923 -484 O ATOM 2699 CB VAL A 333 -12.968 -1.846 1.581 1.00 12.32 C ANISOU 2699 CB VAL A 333 1295 -5 255 1907 1479 -234 C ATOM 2700 CG1 VAL A 333 -14.065 -1.642 2.611 1.00 12.87 C ANISOU 2700 CG1 VAL A 333 1205 -92 179 1974 1710 -369 C ATOM 2701 CG2 VAL A 333 -11.871 -2.770 2.125 1.00 13.66 C ANISOU 2701 CG2 VAL A 333 1358 297 337 2226 1604 -292 C ATOM 2702 N SER A 334 -14.512 -0.470 -0.849 1.00 10.85 N ANISOU 2702 N SER A 334 849 -160 213 1649 1625 -596 N ATOM 2703 CA SER A 334 -15.612 0.356 -1.318 1.00 10.96 C ANISOU 2703 CA SER A 334 920 -64 59 1560 1683 -322 C ATOM 2704 C SER A 334 -16.253 -0.324 -2.522 1.00 11.21 C ANISOU 2704 C SER A 334 999 -12 7 1593 1665 -507 C ATOM 2705 O SER A 334 -15.747 -1.351 -3.012 1.00 12.43 O ANISOU 2705 O SER A 334 986 -42 -120 1871 1865 -572 O ATOM 2706 CB SER A 334 -15.106 1.747 -1.677 1.00 11.56 C ANISOU 2706 CB SER A 334 862 -122 75 1649 1880 -386 C ATOM 2707 OG SER A 334 -14.171 1.728 -2.726 1.00 10.26 O ANISOU 2707 OG SER A 334 928 -6 199 1814 1156 -361 O ATOM 2708 N ILE A 335 -17.333 0.236 -3.036 1.00 12.40 N ANISOU 2708 N ILE A 335 1061 -246 -51 1868 1781 -430 N ATOM 2709 CA ILE A 335 -18.096 -0.406 -4.104 1.00 13.28 C ANISOU 2709 CA ILE A 335 1205 -197 -33 2020 1817 -342 C ATOM 2710 C ILE A 335 -18.035 0.428 -5.362 1.00 13.28 C ANISOU 2710 C ILE A 335 1267 -193 -155 2031 1746 -450 C ATOM 2711 O ILE A 335 -18.337 1.638 -5.361 1.00 13.91 O ANISOU 2711 O ILE A 335 1397 -64 -285 1907 1982 -429 O ATOM 2712 CB ILE A 335 -19.575 -0.609 -3.652 1.00 13.54 C ANISOU 2712 CB ILE A 335 1383 -234 -123 2131 1631 -423 C ATOM 2713 CG1 ILE A 335 -19.609 -1.620 -2.489 1.00 14.01 C ANISOU 2713 CG1 ILE A 335 1585 -136 100 1998 1740 -38 C ATOM 2714 CG2 ILE A 335 -20.403 -1.114 -4.764 1.00 13.76 C ANISOU 2714 CG2 ILE A 335 1462 -465 56 2034 1733 -492 C ATOM 2715 CD1 ILE A 335 -20.993 -1.865 -1.906 1.00 14.17 C ANISOU 2715 CD1 ILE A 335 1111 -351 45 2389 1885 -242 C ATOM 2716 N GLY A 336 -17.686 -0.211 -6.467 1.00 14.08 N ANISOU 2716 N GLY A 336 1300 -100 -129 2016 2034 -350 N ATOM 2717 CA GLY A 336 -17.620 0.445 -7.734 1.00 15.02 C ANISOU 2717 CA GLY A 336 1474 -94 -18 2295 1937 -404 C ATOM 2718 C GLY A 336 -16.672 1.621 -7.755 1.00 14.23 C ANISOU 2718 C GLY A 336 1494 -208 78 2243 1667 -239 C ATOM 2719 O GLY A 336 -15.576 1.613 -7.134 1.00 12.89 O ANISOU 2719 O GLY A 336 1080 -139 146 2470 1346 -607 O ATOM 2720 N ASP A 337 -17.115 2.695 -8.373 1.00 14.32 N ANISOU 2720 N ASP A 337 1570 -41 86 2422 1448 -500 N ATOM 2721 CA ASP A 337 -16.266 3.884 -8.502 1.00 14.80 C ANISOU 2721 CA ASP A 337 1685 -82 280 2374 1564 -454 C ATOM 2722 C ASP A 337 -16.657 4.973 -7.509 1.00 14.79 C ANISOU 2722 C ASP A 337 1645 -165 254 2249 1723 -388 C ATOM 2723 O ASP A 337 -16.322 6.133 -7.716 1.00 14.99 O ANISOU 2723 O ASP A 337 1811 -225 247 2225 1659 -255 O ATOM 2724 CB ASP A 337 -16.269 4.429 -9.937 1.00 18.08 C ANISOU 2724 CB ASP A 337 2276 -153 237 2683 1908 -473 C ATOM 2725 CG ASP A 337 -17.569 5.070 -10.314 1.00 21.79 C ANISOU 2725 CG ASP A 337 3059 8 846 3416 1803 -526 C ATOM 2726 OD1 ASP A 337 -18.597 4.920 -9.636 1.00 23.36 O ANISOU 2726 OD1 ASP A 337 3241 8 1012 3765 1867 -1064 O ATOM 2727 OD2 ASP A 337 -17.634 5.811 -11.320 1.00 31.48 O ANISOU 2727 OD2 ASP A 337 4578 574 1530 4922 2459 -1514 O ATOM 2728 N GLU A 338 -17.349 4.632 -6.423 1.00 13.76 N ANISOU 2728 N GLU A 338 1337 -95 293 2190 1700 -393 N ATOM 2729 CA GLU A 338 -17.768 5.662 -5.492 1.00 12.54 C ANISOU 2729 CA GLU A 338 1352 -110 211 1974 1436 -357 C ATOM 2730 C GLU A 338 -16.554 6.303 -4.861 1.00 12.43 C ANISOU 2730 C GLU A 338 1081 116 294 2065 1574 -312 C ATOM 2731 O GLU A 338 -15.497 5.679 -4.715 1.00 13.09 O ANISOU 2731 O GLU A 338 1106 301 301 2325 1540 -610 O ATOM 2732 CB GLU A 338 -18.673 5.100 -4.368 1.00 12.98 C ANISOU 2732 CB GLU A 338 1288 -95 127 1999 1642 -333 C ATOM 2733 CG GLU A 338 -17.957 4.170 -3.381 1.00 13.10 C ANISOU 2733 CG GLU A 338 1472 -93 132 1823 1681 -318 C ATOM 2734 CD GLU A 338 -18.893 3.376 -2.497 1.00 11.82 C ANISOU 2734 CD GLU A 338 948 -49 112 1843 1700 -244 C ATOM 2735 OE1 GLU A 338 -18.385 2.507 -1.739 1.00 12.91 O ANISOU 2735 OE1 GLU A 338 1028 -54 365 2138 1739 -317 O ATOM 2736 OE2 GLU A 338 -20.127 3.625 -2.484 1.00 13.42 O ANISOU 2736 OE2 GLU A 338 894 -131 53 2241 1961 -304 O ATOM 2737 N ASN A 339 -16.718 7.557 -4.442 1.00 11.00 N ANISOU 2737 N ASN A 339 1072 2 187 1821 1287 -488 N ATOM 2738 CA ASN A 339 -15.694 8.313 -3.728 1.00 11.88 C ANISOU 2738 CA ASN A 339 1269 40 282 1958 1284 -330 C ATOM 2739 C ASN A 339 -15.678 7.846 -2.270 1.00 11.20 C ANISOU 2739 C ASN A 339 1266 61 295 1753 1236 -298 C ATOM 2740 O ASN A 339 -16.718 7.816 -1.620 1.00 11.35 O ANISOU 2740 O ASN A 339 1137 132 324 1961 1214 -287 O ATOM 2741 CB ASN A 339 -15.971 9.799 -3.813 1.00 11.17 C ANISOU 2741 CB ASN A 339 1336 37 266 1888 1020 -407 C ATOM 2742 CG ASN A 339 -16.084 10.297 -5.240 1.00 10.95 C ANISOU 2742 CG ASN A 339 1129 158 423 2059 971 -247 C ATOM 2743 OD1 ASN A 339 -15.361 9.826 -6.128 1.00 13.31 O ANISOU 2743 OD1 ASN A 339 1305 -8 528 2472 1279 -354 O ATOM 2744 ND2 ASN A 339 -17.030 11.228 -5.474 1.00 13.37 N ANISOU 2744 ND2 ASN A 339 1584 413 376 1775 1719 -944 N ATOM 2745 N SER A 340 -14.500 7.497 -1.764 1.00 11.75 N ANISOU 2745 N SER A 340 1217 107 402 1780 1467 -210 N ATOM 2746 CA SER A 340 -14.412 6.789 -0.500 1.00 10.83 C ANISOU 2746 CA SER A 340 1178 48 223 1727 1208 -411 C ATOM 2747 C SER A 340 -13.026 6.983 0.150 1.00 10.22 C ANISOU 2747 C SER A 340 989 56 343 1597 1295 -367 C ATOM 2748 O SER A 340 -12.157 6.097 0.065 1.00 10.48 O ANISOU 2748 O SER A 340 1018 155 281 1678 1283 -473 O ATOM 2749 CB SER A 340 -14.687 5.298 -0.700 1.00 12.80 C ANISOU 2749 CB SER A 340 1474 77 396 1920 1467 -363 C ATOM 2750 OG SER A 340 -13.792 4.741 -1.702 1.00 12.54 O ANISOU 2750 OG SER A 340 1838 58 -4 1785 1140 -438 O ATOM 2751 N ALA A 341 -12.855 8.129 0.812 1.00 9.00 N ANISOU 2751 N ALA A 341 912 115 229 1561 944 -307 N ATOM 2752 CA ALA A 341 -11.518 8.536 1.241 1.00 10.02 C ANISOU 2752 CA ALA A 341 981 -9 104 1626 1200 -379 C ATOM 2753 C ALA A 341 -11.142 7.986 2.631 1.00 9.51 C ANISOU 2753 C ALA A 341 975 -32 133 1545 1091 -319 C ATOM 2754 O ALA A 341 -10.277 7.111 2.729 1.00 11.31 O ANISOU 2754 O ALA A 341 1343 273 151 1897 1056 -774 O ATOM 2755 CB ALA A 341 -11.373 10.046 1.242 1.00 9.82 C ANISOU 2755 CB ALA A 341 1026 -139 235 1733 970 -318 C ATOM 2756 N TYR A 342 -11.731 8.500 3.710 1.00 9.18 N ANISOU 2756 N TYR A 342 984 0 180 1463 1039 -377 N ATOM 2757 CA TYR A 342 -11.263 8.159 5.038 1.00 8.81 C ANISOU 2757 CA TYR A 342 883 -4 164 1400 1062 -324 C ATOM 2758 C TYR A 342 -11.943 6.864 5.528 1.00 8.96 C ANISOU 2758 C TYR A 342 970 -2 219 1347 1087 -435 C ATOM 2759 O TYR A 342 -13.057 6.537 5.139 1.00 8.99 O ANISOU 2759 O TYR A 342 720 -128 165 1703 989 -550 O ATOM 2760 CB TYR A 342 -11.546 9.281 5.982 1.00 9.19 C ANISOU 2760 CB TYR A 342 1044 59 268 1396 1049 -405 C ATOM 2761 CG TYR A 342 -10.696 10.554 5.895 1.00 9.13 C ANISOU 2761 CG TYR A 342 998 -66 276 1547 921 -187 C ATOM 2762 CD1 TYR A 342 -10.011 10.942 4.738 1.00 10.96 C ANISOU 2762 CD1 TYR A 342 1025 -3 172 1863 1277 -392 C ATOM 2763 CD2 TYR A 342 -10.570 11.349 7.030 1.00 11.68 C ANISOU 2763 CD2 TYR A 342 1261 -224 261 1740 1435 -398 C ATOM 2764 CE1 TYR A 342 -9.288 12.132 4.707 1.00 10.59 C ANISOU 2764 CE1 TYR A 342 1015 -3 303 2053 956 -422 C ATOM 2765 CE2 TYR A 342 -9.881 12.504 7.025 1.00 10.12 C ANISOU 2765 CE2 TYR A 342 1381 -252 199 1426 1034 -740 C ATOM 2766 CZ TYR A 342 -9.228 12.922 5.847 1.00 11.66 C ANISOU 2766 CZ TYR A 342 1437 -54 150 1507 1483 -444 C ATOM 2767 OH TYR A 342 -8.461 14.077 5.887 1.00 13.69 O ANISOU 2767 OH TYR A 342 2011 74 345 1425 1764 -494 O ATOM 2768 N SER A 343 -11.263 6.122 6.409 1.00 9.98 N ANISOU 2768 N SER A 343 1156 5 224 1478 1156 -363 N ATOM 2769 CA SER A 343 -11.673 4.777 6.757 1.00 9.12 C ANISOU 2769 CA SER A 343 1035 -105 215 1326 1102 -271 C ATOM 2770 C SER A 343 -11.122 4.307 8.080 1.00 8.48 C ANISOU 2770 C SER A 343 887 -123 198 1329 1006 -315 C ATOM 2771 O SER A 343 -10.136 4.827 8.570 1.00 9.77 O ANISOU 2771 O SER A 343 935 -105 279 1424 1352 -373 O ATOM 2772 CB SER A 343 -11.206 3.801 5.666 1.00 10.28 C ANISOU 2772 CB SER A 343 1286 -41 215 1415 1206 -139 C ATOM 2773 OG SER A 343 -9.803 3.709 5.567 1.00 10.00 O ANISOU 2773 OG SER A 343 1041 317 7 1546 1210 -346 O ATOM 2774 N SER A 344 -11.749 3.272 8.632 1.00 7.63 N ANISOU 2774 N SER A 344 761 -205 207 1249 888 -446 N ATOM 2775 CA SER A 344 -11.302 2.679 9.886 1.00 9.33 C ANISOU 2775 CA SER A 344 1177 -76 231 1279 1086 -235 C ATOM 2776 C SER A 344 -11.674 1.211 9.896 1.00 9.55 C ANISOU 2776 C SER A 344 971 -232 180 1292 1362 -292 C ATOM 2777 O SER A 344 -12.844 0.855 9.748 1.00 9.84 O ANISOU 2777 O SER A 344 1055 -256 169 1431 1250 -273 O ATOM 2778 CB SER A 344 -11.926 3.401 11.094 1.00 10.03 C ANISOU 2778 CB SER A 344 1163 -85 189 1492 1154 -246 C ATOM 2779 OG SER A 344 -11.321 3.013 12.323 1.00 9.15 O ANISOU 2779 OG SER A 344 1037 34 163 1427 1010 -441 O ATOM 2780 N VAL A 345 -10.649 0.372 10.119 1.00 9.49 N ANISOU 2780 N VAL A 345 1145 -162 260 1276 1182 -325 N ATOM 2781 CA VAL A 345 -10.845 -1.072 10.113 1.00 9.22 C ANISOU 2781 CA VAL A 345 1108 -185 131 1272 1121 -240 C ATOM 2782 C VAL A 345 -10.697 -1.614 11.510 1.00 9.22 C ANISOU 2782 C VAL A 345 1068 -216 152 1286 1149 -239 C ATOM 2783 O VAL A 345 -9.742 -1.277 12.221 1.00 9.41 O ANISOU 2783 O VAL A 345 892 -207 152 1541 1139 -280 O ATOM 2784 CB VAL A 345 -9.806 -1.776 9.223 1.00 9.21 C ANISOU 2784 CB VAL A 345 1154 -79 35 1281 1061 -106 C ATOM 2785 CG1 VAL A 345 -9.918 -3.262 9.330 1.00 11.28 C ANISOU 2785 CG1 VAL A 345 1097 -218 24 1593 1594 -163 C ATOM 2786 CG2 VAL A 345 -9.979 -1.349 7.759 1.00 10.29 C ANISOU 2786 CG2 VAL A 345 1243 -192 110 1609 1056 -73 C ATOM 2787 N LEU A 346 -11.657 -2.455 11.914 1.00 9.86 N ANISOU 2787 N LEU A 346 1164 -238 275 1450 1133 -258 N ATOM 2788 CA LEU A 346 -11.656 -3.052 13.254 1.00 10.86 C ANISOU 2788 CA LEU A 346 1374 -254 185 1547 1205 -245 C ATOM 2789 C LEU A 346 -11.707 -4.554 13.155 1.00 10.73 C ANISOU 2789 C LEU A 346 1314 -258 109 1448 1312 -203 C ATOM 2790 O LEU A 346 -12.512 -5.101 12.440 1.00 10.47 O ANISOU 2790 O LEU A 346 1334 -335 214 1499 1144 -303 O ATOM 2791 CB LEU A 346 -12.881 -2.588 14.055 1.00 11.27 C ANISOU 2791 CB LEU A 346 1493 -210 188 1490 1298 -366 C ATOM 2792 CG LEU A 346 -13.210 -3.268 15.390 1.00 10.83 C ANISOU 2792 CG LEU A 346 1448 -271 89 1637 1030 -198 C ATOM 2793 CD1 LEU A 346 -12.089 -2.951 16.392 1.00 13.16 C ANISOU 2793 CD1 LEU A 346 1823 -141 165 1883 1293 -115 C ATOM 2794 CD2 LEU A 346 -14.543 -2.782 15.912 1.00 11.92 C ANISOU 2794 CD2 LEU A 346 1484 -336 301 2018 1027 -186 C ATOM 2795 N TYR A 347 -10.894 -5.226 13.954 1.00 10.53 N ANISOU 2795 N TYR A 347 1319 -316 122 1447 1233 -326 N ATOM 2796 CA TYR A 347 -10.895 -6.678 14.099 1.00 11.58 C ANISOU 2796 CA TYR A 347 1514 -293 85 1504 1379 -215 C ATOM 2797 C TYR A 347 -11.295 -6.993 15.504 1.00 12.41 C ANISOU 2797 C TYR A 347 1723 -272 98 1559 1430 -222 C ATOM 2798 O TYR A 347 -10.567 -6.653 16.436 1.00 12.99 O ANISOU 2798 O TYR A 347 2006 -567 290 1653 1274 -388 O ATOM 2799 CB TYR A 347 -9.506 -7.279 13.781 1.00 12.41 C ANISOU 2799 CB TYR A 347 1624 -103 290 1688 1403 -199 C ATOM 2800 CG TYR A 347 -9.430 -8.780 13.776 1.00 11.78 C ANISOU 2800 CG TYR A 347 1586 -261 267 1550 1339 -343 C ATOM 2801 CD1 TYR A 347 -10.305 -9.561 13.013 1.00 12.12 C ANISOU 2801 CD1 TYR A 347 1489 -142 466 1457 1659 -36 C ATOM 2802 CD2 TYR A 347 -8.518 -9.449 14.590 1.00 13.50 C ANISOU 2802 CD2 TYR A 347 1771 -201 534 1589 1769 -87 C ATOM 2803 CE1 TYR A 347 -10.220 -10.934 13.016 1.00 14.89 C ANISOU 2803 CE1 TYR A 347 2020 -163 412 1800 1837 234 C ATOM 2804 CE2 TYR A 347 -8.420 -10.807 14.593 1.00 15.02 C ANISOU 2804 CE2 TYR A 347 2016 100 407 1916 1771 59 C ATOM 2805 CZ TYR A 347 -9.269 -11.560 13.807 1.00 14.05 C ANISOU 2805 CZ TYR A 347 2303 -175 261 1627 1407 35 C ATOM 2806 OH TYR A 347 -9.146 -12.934 13.824 1.00 15.65 O ANISOU 2806 OH TYR A 347 2446 450 511 1852 1647 81 O ATOM 2807 N LYS A 348 -12.474 -7.589 15.668 1.00 12.68 N ANISOU 2807 N LYS A 348 1600 -299 139 1838 1378 -214 N ATOM 2808 CA LYS A 348 -13.067 -7.829 16.980 1.00 13.67 C ANISOU 2808 CA LYS A 348 1778 -317 141 1816 1597 -47 C ATOM 2809 C LYS A 348 -13.704 -9.170 17.035 1.00 13.56 C ANISOU 2809 C LYS A 348 1821 -326 96 1780 1548 -1 C ATOM 2810 O LYS A 348 -14.542 -9.467 16.218 1.00 12.85 O ANISOU 2810 O LYS A 348 1905 -470 135 1700 1277 -190 O ATOM 2811 CB LYS A 348 -14.080 -6.760 17.324 1.00 13.40 C ANISOU 2811 CB LYS A 348 1726 -340 231 1840 1523 3 C ATOM 2812 CG LYS A 348 -14.866 -6.996 18.590 1.00 14.30 C ANISOU 2812 CG LYS A 348 1725 -253 44 1999 1706 -17 C ATOM 2813 CD LYS A 348 -16.037 -6.013 18.727 1.00 16.02 C ANISOU 2813 CD LYS A 348 1905 -298 194 2241 1940 151 C ATOM 2814 CE LYS A 348 -16.872 -6.320 20.003 1.00 18.73 C ANISOU 2814 CE LYS A 348 2405 -129 368 2719 1993 117 C ATOM 2815 NZ LYS A 348 -17.640 -7.649 19.942 1.00 19.49 N ANISOU 2815 NZ LYS A 348 2490 -487 833 2604 2312 286 N ATOM 2816 N ASP A 349 -13.299 -9.985 18.002 1.00 13.87 N ANISOU 2816 N ASP A 349 1995 -360 142 1715 1559 -144 N ATOM 2817 CA ASP A 349 -13.898 -11.310 18.200 1.00 15.36 C ANISOU 2817 CA ASP A 349 2123 -243 276 1890 1820 92 C ATOM 2818 C ASP A 349 -13.910 -12.132 16.888 1.00 15.56 C ANISOU 2818 C ASP A 349 2142 -443 243 1898 1870 -59 C ATOM 2819 O ASP A 349 -14.897 -12.766 16.490 1.00 15.70 O ANISOU 2819 O ASP A 349 2026 -661 243 2210 1729 147 O ATOM 2820 CB ASP A 349 -15.242 -11.198 18.882 1.00 16.51 C ANISOU 2820 CB ASP A 349 2370 -570 457 1917 1986 133 C ATOM 2821 CG ASP A 349 -15.136 -10.572 20.270 1.00 19.34 C ANISOU 2821 CG ASP A 349 2625 -105 633 2668 2056 445 C ATOM 2822 OD1 ASP A 349 -14.295 -11.010 21.120 1.00 25.83 O ANISOU 2822 OD1 ASP A 349 3890 -292 -217 3864 2057 158 O ATOM 2823 OD2 ASP A 349 -15.858 -9.637 20.614 1.00 26.32 O ANISOU 2823 OD2 ASP A 349 4493 1 889 2909 2596 900 O ATOM 2824 N ASP A 350 -12.749 -12.095 16.219 1.00 14.32 N ANISOU 2824 N ASP A 350 2132 -209 280 1679 1630 46 N ATOM 2825 CA ASP A 350 -12.529 -12.821 14.974 1.00 14.73 C ANISOU 2825 CA ASP A 350 2118 -274 363 1620 1858 27 C ATOM 2826 C ASP A 350 -13.537 -12.455 13.902 1.00 15.46 C ANISOU 2826 C ASP A 350 2087 -272 340 1711 2075 -97 C ATOM 2827 O ASP A 350 -13.891 -13.270 13.040 1.00 16.26 O ANISOU 2827 O ASP A 350 2307 -268 495 1547 2322 139 O ATOM 2828 CB ASP A 350 -12.497 -14.313 15.176 1.00 16.29 C ANISOU 2828 CB ASP A 350 2453 33 239 1802 1932 -16 C ATOM 2829 CG ASP A 350 -11.941 -15.020 13.975 1.00 17.31 C ANISOU 2829 CG ASP A 350 2828 -22 312 1837 1912 71 C ATOM 2830 OD1 ASP A 350 -12.433 -16.138 13.692 1.00 24.85 O ANISOU 2830 OD1 ASP A 350 4209 -260 -66 2384 2845 553 O ATOM 2831 OD2 ASP A 350 -11.007 -14.519 13.287 1.00 19.98 O ANISOU 2831 OD2 ASP A 350 3138 25 180 1946 2505 275 O ATOM 2832 N LYS A 351 -13.939 -11.183 13.916 1.00 13.05 N ANISOU 2832 N LYS A 351 1749 -276 374 1341 1866 -166 N ATOM 2833 CA LYS A 351 -14.761 -10.623 12.787 1.00 13.20 C ANISOU 2833 CA LYS A 351 1712 -329 299 1541 1760 -297 C ATOM 2834 C LYS A 351 -14.129 -9.306 12.347 1.00 12.92 C ANISOU 2834 C LYS A 351 1595 -385 255 1603 1710 -190 C ATOM 2835 O LYS A 351 -13.613 -8.572 13.213 1.00 13.39 O ANISOU 2835 O LYS A 351 1549 -490 375 1719 1817 -107 O ATOM 2836 CB LYS A 351 -16.200 -10.414 13.219 1.00 15.62 C ANISOU 2836 CB LYS A 351 2213 -339 253 1741 1979 -348 C ATOM 2837 CG LYS A 351 -16.974 -11.730 13.546 1.00 18.50 C ANISOU 2837 CG LYS A 351 2482 -426 716 2391 2154 -548 C ATOM 2838 CD LYS A 351 -17.770 -12.325 12.472 1.00 27.89 C ANISOU 2838 CD LYS A 351 4032 -517 691 3172 3390 -160 C ATOM 2839 CE LYS A 351 -18.519 -13.565 12.947 1.00 29.11 C ANISOU 2839 CE LYS A 351 3983 -406 724 3393 3684 -388 C ATOM 2840 NZ LYS A 351 -17.593 -14.366 13.809 1.00 37.46 N ANISOU 2840 NZ LYS A 351 5144 -728 733 4396 4690 -364 N ATOM 2841 N LEU A 352 -14.190 -9.008 11.046 1.00 11.73 N ANISOU 2841 N LEU A 352 1412 -445 145 1327 1716 -154 N ATOM 2842 CA LEU A 352 -13.522 -7.813 10.485 1.00 11.07 C ANISOU 2842 CA LEU A 352 1242 -321 184 1516 1445 -165 C ATOM 2843 C LEU A 352 -14.600 -6.835 10.009 1.00 9.39 C ANISOU 2843 C LEU A 352 1022 -371 149 1214 1331 -220 C ATOM 2844 O LEU A 352 -15.601 -7.240 9.365 1.00 12.14 O ANISOU 2844 O LEU A 352 1029 -437 146 1791 1793 -250 O ATOM 2845 CB LEU A 352 -12.589 -8.215 9.351 1.00 10.63 C ANISOU 2845 CB LEU A 352 1143 -251 15 1503 1393 -406 C ATOM 2846 CG LEU A 352 -11.583 -7.191 8.860 1.00 10.67 C ANISOU 2846 CG LEU A 352 1429 -354 124 1501 1122 -161 C ATOM 2847 CD1 LEU A 352 -10.543 -6.898 10.008 1.00 10.84 C ANISOU 2847 CD1 LEU A 352 1367 -298 319 1561 1189 -123 C ATOM 2848 CD2 LEU A 352 -10.867 -7.706 7.634 1.00 13.30 C ANISOU 2848 CD2 LEU A 352 1622 -329 -16 1947 1484 -317 C ATOM 2849 N TYR A 353 -14.400 -5.554 10.314 1.00 10.28 N ANISOU 2849 N TYR A 353 914 -371 340 1411 1581 -102 N ATOM 2850 CA TYR A 353 -15.356 -4.513 10.032 1.00 10.91 C ANISOU 2850 CA TYR A 353 1084 -218 219 1443 1616 -4 C ATOM 2851 C TYR A 353 -14.640 -3.294 9.465 1.00 10.64 C ANISOU 2851 C TYR A 353 1078 -159 269 1350 1612 -127 C ATOM 2852 O TYR A 353 -13.477 -3.054 9.772 1.00 11.16 O ANISOU 2852 O TYR A 353 998 -184 442 1420 1821 -316 O ATOM 2853 CB TYR A 353 -16.071 -4.062 11.317 1.00 12.11 C ANISOU 2853 CB TYR A 353 1239 -322 352 1716 1645 -10 C ATOM 2854 CG TYR A 353 -16.724 -5.177 12.073 1.00 12.23 C ANISOU 2854 CG TYR A 353 1269 -107 97 1773 1604 151 C ATOM 2855 CD1 TYR A 353 -16.028 -5.861 13.061 1.00 15.19 C ANISOU 2855 CD1 TYR A 353 1776 -233 248 2118 1876 -201 C ATOM 2856 CD2 TYR A 353 -18.032 -5.565 11.814 1.00 13.92 C ANISOU 2856 CD2 TYR A 353 1310 -55 354 2208 1767 247 C ATOM 2857 CE1 TYR A 353 -16.637 -6.864 13.833 1.00 14.11 C ANISOU 2857 CE1 TYR A 353 1345 -462 537 2039 1977 -83 C ATOM 2858 CE2 TYR A 353 -18.629 -6.556 12.550 1.00 14.86 C ANISOU 2858 CE2 TYR A 353 1351 -209 497 1987 2306 86 C ATOM 2859 CZ TYR A 353 -17.919 -7.215 13.548 1.00 15.22 C ANISOU 2859 CZ TYR A 353 1394 -465 621 2150 2236 127 C ATOM 2860 OH TYR A 353 -18.569 -8.161 14.317 1.00 17.16 O ANISOU 2860 OH TYR A 353 1431 -647 628 2363 2726 245 O ATOM 2861 N CYS A 354 -15.365 -2.477 8.704 1.00 10.91 N ANISOU 2861 N CYS A 354 1126 -200 291 1582 1435 -213 N ATOM 2862 CA CYS A 354 -14.828 -1.221 8.229 1.00 10.34 C ANISOU 2862 CA CYS A 354 1072 -180 190 1451 1404 -212 C ATOM 2863 C CYS A 354 -15.898 -0.168 8.254 1.00 11.35 C ANISOU 2863 C CYS A 354 1062 -221 199 1651 1597 -178 C ATOM 2864 O CYS A 354 -16.973 -0.396 7.735 1.00 12.38 O ANISOU 2864 O CYS A 354 1071 -95 259 1908 1722 -559 O ATOM 2865 CB CYS A 354 -14.258 -1.340 6.848 1.00 10.54 C ANISOU 2865 CB CYS A 354 986 -146 154 1561 1458 -249 C ATOM 2866 SG CYS A 354 -13.445 0.180 6.250 1.00 11.28 S ANISOU 2866 SG CYS A 354 1238 -103 251 1813 1235 -306 S ATOM 2867 N LEU A 355 -15.590 0.970 8.886 1.00 10.63 N ANISOU 2867 N LEU A 355 810 -183 194 1622 1606 -221 N ATOM 2868 CA LEU A 355 -16.446 2.155 8.815 1.00 9.96 C ANISOU 2868 CA LEU A 355 910 -184 212 1506 1366 -223 C ATOM 2869 C LEU A 355 -15.675 3.109 7.876 1.00 9.91 C ANISOU 2869 C LEU A 355 854 -122 249 1540 1370 -266 C ATOM 2870 O LEU A 355 -14.549 3.481 8.162 1.00 10.10 O ANISOU 2870 O LEU A 355 964 -158 316 1607 1267 -484 O ATOM 2871 CB LEU A 355 -16.504 2.794 10.195 1.00 11.00 C ANISOU 2871 CB LEU A 355 868 -136 73 1818 1490 -216 C ATOM 2872 CG LEU A 355 -17.433 4.024 10.408 1.00 11.31 C ANISOU 2872 CG LEU A 355 921 -248 -3 1731 1645 -242 C ATOM 2873 CD1 LEU A 355 -18.901 3.684 10.256 1.00 11.85 C ANISOU 2873 CD1 LEU A 355 911 -165 -150 2075 1516 -366 C ATOM 2874 CD2 LEU A 355 -17.119 4.704 11.754 1.00 11.41 C ANISOU 2874 CD2 LEU A 355 1042 -263 169 1923 1369 -129 C ATOM 2875 N HIS A 356 -16.305 3.543 6.788 1.00 9.16 N ANISOU 2875 N HIS A 356 859 -191 324 1542 1079 -563 N ATOM 2876 CA HIS A 356 -15.671 4.433 5.859 1.00 8.96 C ANISOU 2876 CA HIS A 356 871 -234 163 1438 1096 -474 C ATOM 2877 C HIS A 356 -16.595 5.410 5.186 1.00 10.44 C ANISOU 2877 C HIS A 356 988 -89 143 1550 1427 -263 C ATOM 2878 O HIS A 356 -17.824 5.217 5.126 1.00 10.43 O ANISOU 2878 O HIS A 356 913 -169 119 1709 1340 -221 O ATOM 2879 CB HIS A 356 -14.849 3.644 4.810 1.00 8.68 C ANISOU 2879 CB HIS A 356 815 -85 188 1378 1104 -539 C ATOM 2880 CG HIS A 356 -15.633 2.923 3.762 1.00 9.40 C ANISOU 2880 CG HIS A 356 1103 -384 85 1413 1054 -427 C ATOM 2881 ND1 HIS A 356 -16.091 3.560 2.625 1.00 11.15 N ANISOU 2881 ND1 HIS A 356 1198 -145 -27 1735 1302 -456 N ATOM 2882 CD2 HIS A 356 -15.890 1.591 3.578 1.00 9.66 C ANISOU 2882 CD2 HIS A 356 993 -56 367 1496 1179 -723 C ATOM 2883 CE1 HIS A 356 -16.708 2.655 1.844 1.00 10.55 C ANISOU 2883 CE1 HIS A 356 1085 -265 237 1669 1254 -259 C ATOM 2884 NE2 HIS A 356 -16.620 1.464 2.414 1.00 10.81 N ANISOU 2884 NE2 HIS A 356 1097 -222 563 1821 1187 -795 N ATOM 2885 N GLU A 357 -15.984 6.449 4.618 1.00 10.07 N ANISOU 2885 N GLU A 357 1072 -61 301 1475 1278 -296 N ATOM 2886 CA GLU A 357 -16.743 7.486 3.951 1.00 10.60 C ANISOU 2886 CA GLU A 357 1095 19 209 1589 1342 -157 C ATOM 2887 C GLU A 357 -17.238 7.022 2.592 1.00 10.36 C ANISOU 2887 C GLU A 357 945 -9 181 1699 1290 -205 C ATOM 2888 O GLU A 357 -16.560 6.266 1.890 1.00 11.04 O ANISOU 2888 O GLU A 357 1067 61 121 1644 1483 -370 O ATOM 2889 CB GLU A 357 -15.848 8.695 3.748 1.00 10.87 C ANISOU 2889 CB GLU A 357 1128 -156 253 1638 1363 -402 C ATOM 2890 CG GLU A 357 -15.480 9.403 5.072 1.00 9.89 C ANISOU 2890 CG GLU A 357 986 -176 -35 1295 1476 -293 C ATOM 2891 CD GLU A 357 -14.548 10.566 4.928 1.00 9.41 C ANISOU 2891 CD GLU A 357 1047 176 321 1353 1174 -151 C ATOM 2892 OE1 GLU A 357 -14.461 11.329 5.935 1.00 10.79 O ANISOU 2892 OE1 GLU A 357 1416 -176 97 1238 1445 103 O ATOM 2893 OE2 GLU A 357 -13.899 10.691 3.846 1.00 12.07 O ANISOU 2893 OE2 GLU A 357 1179 79 376 1788 1619 -104 O ATOM 2894 N ILE A 358 -18.383 7.557 2.189 1.00 10.65 N ANISOU 2894 N ILE A 358 1013 146 183 1715 1318 -192 N ATOM 2895 CA ILE A 358 -18.826 7.620 0.808 1.00 11.88 C ANISOU 2895 CA ILE A 358 1218 44 154 1732 1563 -225 C ATOM 2896 C ILE A 358 -19.262 9.050 0.559 1.00 11.90 C ANISOU 2896 C ILE A 358 1149 161 179 1920 1452 -361 C ATOM 2897 O ILE A 358 -19.885 9.684 1.414 1.00 12.05 O ANISOU 2897 O ILE A 358 1326 160 221 1796 1454 -385 O ATOM 2898 CB ILE A 358 -19.936 6.588 0.501 1.00 11.52 C ANISOU 2898 CB ILE A 358 1084 45 70 1864 1428 -360 C ATOM 2899 CG1 ILE A 358 -21.148 6.803 1.368 1.00 12.98 C ANISOU 2899 CG1 ILE A 358 1236 -83 156 1783 1911 -258 C ATOM 2900 CG2 ILE A 358 -19.394 5.181 0.671 1.00 12.48 C ANISOU 2900 CG2 ILE A 358 1238 -2 352 1558 1946 -365 C ATOM 2901 CD1 ILE A 358 -22.432 6.062 0.871 1.00 12.98 C ANISOU 2901 CD1 ILE A 358 1223 -210 76 2012 1696 -292 C ATOM 2902 N ASN A 359 -18.838 9.576 -0.586 1.00 10.98 N ANISOU 2902 N ASN A 359 1179 94 287 1877 1115 -428 N ATOM 2903 CA ASN A 359 -19.028 10.981 -0.948 1.00 11.87 C ANISOU 2903 CA ASN A 359 1264 167 248 1851 1395 -404 C ATOM 2904 C ASN A 359 -19.670 11.119 -2.320 1.00 13.22 C ANISOU 2904 C ASN A 359 1463 272 308 2127 1432 -385 C ATOM 2905 O ASN A 359 -19.076 10.713 -3.340 1.00 12.81 O ANISOU 2905 O ASN A 359 1302 270 510 2328 1238 -491 O ATOM 2906 CB ASN A 359 -17.648 11.669 -0.908 1.00 12.47 C ANISOU 2906 CB ASN A 359 1304 12 178 1930 1502 -304 C ATOM 2907 CG ASN A 359 -17.575 13.020 -1.655 1.00 12.83 C ANISOU 2907 CG ASN A 359 1416 58 322 2022 1434 -428 C ATOM 2908 OD1 ASN A 359 -16.420 13.492 -2.010 1.00 16.68 O ANISOU 2908 OD1 ASN A 359 1709 -156 743 2450 2178 -487 O ATOM 2909 ND2 ASN A 359 -18.689 13.671 -1.829 1.00 9.62 N ANISOU 2909 ND2 ASN A 359 757 231 244 1458 1438 -117 N ATOM 2910 N SER A 360 -20.875 11.703 -2.333 1.00 13.25 N ANISOU 2910 N SER A 360 1381 168 332 2216 1436 -299 N ATOM 2911 CA SER A 360 -21.484 12.100 -3.612 1.00 14.13 C ANISOU 2911 CA SER A 360 1518 200 321 2247 1602 -495 C ATOM 2912 C SER A 360 -21.749 13.577 -3.541 1.00 15.27 C ANISOU 2912 C SER A 360 1702 37 244 2443 1656 -502 C ATOM 2913 O SER A 360 -22.462 14.024 -2.642 1.00 14.82 O ANISOU 2913 O SER A 360 1538 192 402 2480 1611 -552 O ATOM 2914 CB SER A 360 -22.783 11.291 -3.889 1.00 15.17 C ANISOU 2914 CB SER A 360 1596 263 228 2386 1781 -402 C ATOM 2915 OG SER A 360 -22.508 9.914 -4.213 1.00 17.27 O ANISOU 2915 OG SER A 360 1900 517 254 2462 2200 -957 O ATOM 2916 N ASN A 361 -21.201 14.341 -4.496 1.00 16.03 N ANISOU 2916 N ASN A 361 1846 132 228 2519 1723 -474 N ATOM 2917 CA ASN A 361 -21.410 15.783 -4.525 1.00 16.17 C ANISOU 2917 CA ASN A 361 1852 131 362 2422 1870 -385 C ATOM 2918 C ASN A 361 -21.042 16.520 -3.234 1.00 14.71 C ANISOU 2918 C ASN A 361 1546 229 302 2236 1806 -326 C ATOM 2919 O ASN A 361 -21.686 17.495 -2.817 1.00 15.65 O ANISOU 2919 O ASN A 361 1693 355 608 2222 2030 -481 O ATOM 2920 CB ASN A 361 -22.833 16.034 -4.947 1.00 18.10 C ANISOU 2920 CB ASN A 361 2066 120 296 2691 2121 -409 C ATOM 2921 CG ASN A 361 -23.140 15.322 -6.282 1.00 23.24 C ANISOU 2921 CG ASN A 361 2781 70 218 3199 2850 -375 C ATOM 2922 OD1 ASN A 361 -22.380 15.495 -7.228 1.00 30.99 O ANISOU 2922 OD1 ASN A 361 4066 357 448 4326 3382 -382 O ATOM 2923 ND2 ASN A 361 -24.203 14.464 -6.335 1.00 27.69 N ANISOU 2923 ND2 ASN A 361 3352 423 -18 3742 3427 -1749 N ATOM 2924 N GLU A 362 -19.973 16.041 -2.585 1.00 14.91 N ANISOU 2924 N GLU A 362 1582 272 415 2206 1878 -179 N ATOM 2925 CA GLU A 362 -19.526 16.612 -1.335 1.00 14.08 C ANISOU 2925 CA GLU A 362 1447 351 372 2067 1833 -292 C ATOM 2926 C GLU A 362 -20.543 16.556 -0.206 1.00 13.77 C ANISOU 2926 C GLU A 362 1316 356 282 2054 1861 -305 C ATOM 2927 O GLU A 362 -20.600 17.423 0.664 1.00 15.17 O ANISOU 2927 O GLU A 362 1581 370 358 2108 2074 -176 O ATOM 2928 CB GLU A 362 -18.959 18.025 -1.518 1.00 13.92 C ANISOU 2928 CB GLU A 362 1339 355 189 2024 1923 -298 C ATOM 2929 CG GLU A 362 -17.772 18.114 -2.484 1.00 14.56 C ANISOU 2929 CG GLU A 362 1782 406 354 1904 1843 -205 C ATOM 2930 CD GLU A 362 -16.670 17.164 -2.087 1.00 13.89 C ANISOU 2930 CD GLU A 362 1368 70 416 1759 2150 6 C ATOM 2931 OE1 GLU A 362 -16.247 17.243 -0.927 1.00 14.63 O ANISOU 2931 OE1 GLU A 362 1536 268 214 2284 1738 17 O ATOM 2932 OE2 GLU A 362 -16.248 16.335 -2.927 1.00 15.81 O ANISOU 2932 OE2 GLU A 362 1892 592 609 1880 2234 -103 O ATOM 2933 N VAL A 363 -21.318 15.486 -0.225 1.00 13.05 N ANISOU 2933 N VAL A 363 1307 314 302 1950 1702 -343 N ATOM 2934 CA VAL A 363 -22.207 15.126 0.847 1.00 13.93 C ANISOU 2934 CA VAL A 363 1367 258 282 2145 1780 -320 C ATOM 2935 C VAL A 363 -21.748 13.722 1.291 1.00 12.65 C ANISOU 2935 C VAL A 363 1206 269 193 1964 1636 -324 C ATOM 2936 O VAL A 363 -21.743 12.759 0.485 1.00 12.50 O ANISOU 2936 O VAL A 363 998 215 374 1972 1778 -422 O ATOM 2937 CB VAL A 363 -23.694 15.165 0.470 1.00 14.61 C ANISOU 2937 CB VAL A 363 1483 288 274 2195 1871 -317 C ATOM 2938 CG1 VAL A 363 -24.543 15.117 1.700 1.00 15.10 C ANISOU 2938 CG1 VAL A 363 1250 448 478 2324 2163 -301 C ATOM 2939 CG2 VAL A 363 -24.082 16.400 -0.352 1.00 13.66 C ANISOU 2939 CG2 VAL A 363 974 500 623 2355 1858 -422 C ATOM 2940 N TYR A 364 -21.375 13.620 2.581 1.00 11.59 N ANISOU 2940 N TYR A 364 1224 178 75 1741 1439 -254 N ATOM 2941 CA TYR A 364 -20.691 12.454 3.052 1.00 11.40 C ANISOU 2941 CA TYR A 364 1034 141 144 1865 1431 -339 C ATOM 2942 C TYR A 364 -21.506 11.615 4.011 1.00 11.30 C ANISOU 2942 C TYR A 364 971 167 124 1774 1548 -376 C ATOM 2943 O TYR A 364 -22.048 12.159 4.990 1.00 12.48 O ANISOU 2943 O TYR A 364 935 312 190 2090 1714 -184 O ATOM 2944 CB TYR A 364 -19.379 12.856 3.759 1.00 10.91 C ANISOU 2944 CB TYR A 364 858 4 202 1829 1459 -399 C ATOM 2945 CG TYR A 364 -18.325 13.506 2.857 1.00 11.55