HEADER TRANSFERASE 12-JAN-09 3FTD TITLE CRYSTAL STRUCTURE OF A. AEOLICUS KSGA AT 1.44-ANGSTROM TITLE 2 RESOLUTION COMPND MOL_ID: 1; COMPND 2 MOLECULE: DIMETHYLADENOSINE TRANSFERASE; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: S-ADENOSYLMETHIONINE-6-N', N'-ADENOSYL(RRNA) COMPND 5 DIMETHYLTRANSFERASE, 16S RRNA DIMETHYLASE, HIGH LEVEL COMPND 6 KASUGAMYCIN RESISTANCE PROTEIN KSGA, KASUGAMYCIN COMPND 7 DIMETHYLTRANSFERASE; COMPND 8 EC: 2.1.1.-; COMPND 9 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: AQUIFEX AEOLICUS VF5; SOURCE 3 ORGANISM_TAXID: 224324; SOURCE 4 STRAIN: VF5; SOURCE 5 GENE: AQ_1816, KSGA; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21-CODONPLUS(DE3)-RIL; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_VECTOR: PDONR221; SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PBA1939 KEYWDS KSGA, ROSSMANN-LIKE FOLD, RNA METHYLTRANSFERASE, MTASE, KEYWDS 2 ANTIBIOTIC RESISTANCE, METHYLTRANSFERASE, RNA-BINDING, RRNA KEYWDS 3 PROCESSING, S-ADENOSYL-L-METHIONINE, TRANSFERASE EXPDTA X-RAY DIFFRACTION AUTHOR C.TU,X.JI REVDAT 1 24-MAR-09 3FTD 0 JRNL AUTH C.TU,J.E.TROPEA,B.P.AUSTIN,D.L.COURT,D.S.WAUGH,X.JI JRNL TITL STRUCTURAL BASIS FOR BINDING OF RNA AND COFACTOR JRNL TITL 2 BY A KSGA METHYLTRANSFERASE. JRNL REF STRUCTURE V. 17 374 2009 JRNL REFN ISSN 0969-2126 JRNL PMID 19278652 JRNL DOI 10.1016/J.STR.2009.01.010 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 1.44 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE- REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO, REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH, REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER REMARK 3 : ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : ENGH & HUBER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.44 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.69 REMARK 3 MIN(FOBS/SIGMA_FOBS) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 94.5 REMARK 3 NUMBER OF REFLECTIONS : 37676 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.161 REMARK 3 R VALUE (WORKING SET) : 0.159 REMARK 3 FREE R VALUE : 0.200 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.310 REMARK 3 FREE R VALUE TEST SET COUNT : 2000 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 28.6972 - 3.4740 1.00 2885 162 0.1619 0.1853 REMARK 3 2 3.4740 - 2.7581 1.00 2751 153 0.1565 0.1600 REMARK 3 3 2.7581 - 2.4097 1.00 2721 153 0.1627 0.2048 REMARK 3 4 2.4097 - 2.1895 1.00 2701 152 0.1469 0.1958 REMARK 3 5 2.1895 - 2.0326 1.00 2698 152 0.1322 0.1814 REMARK 3 6 2.0326 - 1.9128 1.00 2672 149 0.1305 0.1891 REMARK 3 7 1.9128 - 1.8170 1.00 2678 150 0.1319 0.1970 REMARK 3 8 1.8170 - 1.7379 0.99 2645 149 0.1416 0.2523 REMARK 3 9 1.7379 - 1.6710 0.99 2635 147 0.1457 0.1909 REMARK 3 10 1.6710 - 1.6134 0.97 2580 145 0.1530 0.2433 REMARK 3 11 1.6134 - 1.5629 0.94 2530 141 0.1660 0.2438 REMARK 3 12 1.5629 - 1.5182 0.89 2360 133 0.1857 0.2428 REMARK 3 13 1.5182 - 1.4783 0.79 2083 117 0.2195 0.2727 REMARK 3 14 1.4783 - 1.4400 0.66 1737 97 0.2929 0.3355 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : 0.38 REMARK 3 B_SOL : 50.04 REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.170 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 14.90 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.00 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.76000 REMARK 3 B22 (A**2) : 0.00000 REMARK 3 B33 (A**2) : 0.00000 REMARK 3 B12 (A**2) : -0.74000 REMARK 3 B13 (A**2) : 1.50000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.005 NULL REMARK 3 ANGLE : NULL NULL REMARK 3 CHIRALITY : NULL NULL REMARK 3 PLANARITY : NULL NULL REMARK 3 DIHEDRAL : 14.495 NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 3FTD COMPLIES WITH FORMAT V. 3.20, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-JAN-09. REMARK 100 THE RCSB ID CODE IS RCSB051018. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 13-MAR-08 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 6.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 22-BM REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000 REMARK 200 MONOCHROMATOR : SI(111) ROSENBAUM-ROCK DOUBLE REMARK 200 CRYSTAL REMARK 200 OPTICS : MIRRORS REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38594 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.440 REMARK 200 RESOLUTION RANGE LOW (A) : 30.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.0 REMARK 200 DATA REDUNDANCY : 6.900 REMARK 200 R MERGE (I) : 0.06800 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 24.6000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.44 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.48 REMARK 200 COMPLETENESS FOR SHELL (%) : 66.0 REMARK 200 DATA REDUNDANCY IN SHELL : 2.70 REMARK 200 R MERGE FOR SHELL (I) : 0.44600 REMARK 200 R SYM FOR SHELL (I) : 0.49300 REMARK 200 FOR SHELL : 1.900 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: PDB ENTRY 3FTC REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 35.31 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.90 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG MME 5000, 0.1 M BIS-TRIS, REMARK 280 PH 6.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 292K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 21.54350 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 43.80900 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 28.69150 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 43.80900 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 21.54350 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 28.69150 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 300 REMARK: THE BIOLOGICAL ASSEMBLY CORRESPONDS TO THE CONTENT OF REMARK 300 THE ASYMMETRIC UNIT. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 SER A 0 REMARK 465 MET A 1 REMARK 465 VAL A 2 REMARK 465 ARG A 3 REMARK 465 LEU A 4 REMARK 465 LYS A 5 REMARK 465 LYS A 6 REMARK 465 GLY A 247 REMARK 465 GLU A 248 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 PRO A 52 31.88 -75.68 REMARK 500 ASN A 182 92.06 -160.08 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1QYR RELATED DB: PDB REMARK 900 LIGAND-FREE E. COLI KSGA REMARK 900 RELATED ID: 1ZQ9 RELATED DB: PDB REMARK 900 H. SAPIENS DIM1 IN COMPLEX WITH SAM REMARK 900 RELATED ID: 1G38 RELATED DB: PDB REMARK 900 M.TAQI IN COMPLEX WITH DNA AND COFACTOR ANALOG NEA REMARK 900 RELATED ID: 3FTC RELATED DB: PDB REMARK 900 LIGAND-FREE A. AEOLICUS KSGA (KSGA2) REMARK 900 RELATED ID: 3FTE RELATED DB: PDB REMARK 900 A. AEOLICUS KSGA IN COMPLEX WITH RNA (KSGA-RNA) REMARK 900 RELATED ID: 3FTF RELATED DB: PDB REMARK 900 A. AEOLICUS KSGA IN COMPLEX WITH RNA AND SAH (KSGA-RNA-SAH) DBREF 3FTD A 1 248 UNP O67680 KSGA_AQUAE 1 248 SEQADV 3FTD SER A 0 UNP O67680 EXPRESSION TAG SEQRES 1 A 249 SER MET VAL ARG LEU LYS LYS SER PHE GLY GLN HIS LEU SEQRES 2 A 249 LEU VAL SER GLU GLY VAL LEU LYS LYS ILE ALA GLU GLU SEQRES 3 A 249 LEU ASN ILE GLU GLU GLY ASN THR VAL VAL GLU VAL GLY SEQRES 4 A 249 GLY GLY THR GLY ASN LEU THR LYS VAL LEU LEU GLN HIS SEQRES 5 A 249 PRO LEU LYS LYS LEU TYR VAL ILE GLU LEU ASP ARG GLU SEQRES 6 A 249 MET VAL GLU ASN LEU LYS SER ILE GLY ASP GLU ARG LEU SEQRES 7 A 249 GLU VAL ILE ASN GLU ASP ALA SER LYS PHE PRO PHE CYS SEQRES 8 A 249 SER LEU GLY LYS GLU LEU LYS VAL VAL GLY ASN LEU PRO SEQRES 9 A 249 TYR ASN VAL ALA SER LEU ILE ILE GLU ASN THR VAL TYR SEQRES 10 A 249 ASN LYS ASP CYS VAL PRO LEU ALA VAL PHE MET VAL GLN SEQRES 11 A 249 LYS GLU VAL ALA GLU LYS LEU GLN GLY LYS LYS ASP THR SEQRES 12 A 249 GLY TRP LEU SER VAL PHE VAL ARG THR PHE TYR ASP VAL SEQRES 13 A 249 ASN TYR VAL MET THR VAL PRO PRO ARG PHE PHE VAL PRO SEQRES 14 A 249 PRO PRO LYS VAL GLN SER ALA VAL ILE LYS LEU VAL LYS SEQRES 15 A 249 ASN GLU LYS PHE PRO VAL LYS ASP LEU LYS ASN TYR LYS SEQRES 16 A 249 LYS PHE LEU THR LYS ILE PHE GLN ASN ARG ARG LYS VAL SEQRES 17 A 249 LEU ARG LYS LYS ILE PRO GLU GLU LEU LEU LYS GLU ALA SEQRES 18 A 249 GLY ILE ASN PRO ASP ALA ARG VAL GLU GLN LEU SER LEU SEQRES 19 A 249 GLU ASP PHE PHE LYS LEU TYR ARG LEU ILE GLU ASP SER SEQRES 20 A 249 GLY GLU FORMUL 2 HOH *277(H2 O) HELIX 1 1 SER A 15 LEU A 26 1 12 HELIX 2 2 GLY A 40 LEU A 49 1 10 HELIX 3 3 ASP A 62 LYS A 70 1 9 HELIX 4 4 PRO A 88 LEU A 92 5 5 HELIX 5 5 VAL A 106 ASN A 117 1 12 HELIX 6 6 LYS A 118 VAL A 121 5 4 HELIX 7 7 LYS A 130 GLY A 138 1 9 HELIX 8 8 GLY A 143 PHE A 152 1 10 HELIX 9 9 PRO A 162 ARG A 164 5 3 HELIX 10 10 ASP A 189 GLN A 202 1 14 HELIX 11 11 VAL A 207 LYS A 211 5 5 HELIX 12 12 PRO A 213 ALA A 220 1 8 HELIX 13 13 ARG A 227 LEU A 231 5 5 HELIX 14 14 SER A 232 ASP A 245 1 14 SHEET 1 A 2 LEU A 13 VAL A 14 0 SHEET 2 A 2 PHE A 166 VAL A 167 -1 O VAL A 167 N LEU A 13 SHEET 1 B 7 LEU A 77 ILE A 80 0 SHEET 2 B 7 LYS A 55 ILE A 59 1 N VAL A 58 O ILE A 80 SHEET 3 B 7 THR A 33 GLY A 38 1 N GLU A 36 O TYR A 57 SHEET 4 B 7 LEU A 96 ASN A 101 1 O LYS A 97 N VAL A 35 SHEET 5 B 7 LEU A 123 GLN A 129 1 O VAL A 125 N VAL A 98 SHEET 6 B 7 SER A 174 LYS A 181 -1 O LEU A 179 N ALA A 124 SHEET 7 B 7 TYR A 153 VAL A 161 -1 N ASP A 154 O VAL A 180 SSBOND 1 CYS A 90 CYS A 120 1555 1555 2.03 CISPEP 1 VAL A 167 PRO A 168 0 -1.44 CRYST1 43.087 57.383 87.618 90.00 90.00 90.00 P 21 21 21 4 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.023209 0.000000 0.000000 0.00000 SCALE2 0.000000 0.017427 0.000000 0.00000 SCALE3 0.000000 0.000000 0.011413 0.00000 ATOM 1 N SER A 7 -14.558 2.038 -0.680 1.00 47.97 N ANISOU 1 N SER A 7 5871 6439 5914 275 -608 479 N ATOM 2 CA SER A 7 -14.131 0.680 -0.355 1.00 46.76 C ANISOU 2 CA SER A 7 5808 6194 5763 222 -737 430 C ATOM 3 C SER A 7 -12.787 0.645 0.369 1.00 42.55 C ANISOU 3 C SER A 7 5059 5661 5447 31 -743 693 C ATOM 4 O SER A 7 -12.480 1.534 1.167 1.00 43.86 O ANISOU 4 O SER A 7 5137 5955 5570 297 -588 666 O ATOM 5 CB SER A 7 -14.083 -0.192 -1.611 1.00 48.71 C ANISOU 5 CB SER A 7 6105 6511 5891 207 -852 56 C ATOM 6 OG SER A 7 -15.350 -0.773 -1.867 1.00 49.90 O ANISOU 6 OG SER A 7 6217 6736 6004 113 -988 -53 O ATOM 7 N PHE A 8 -11.990 -0.384 0.085 1.00 37.48 N ANISOU 7 N PHE A 8 4607 4683 4949 -595 -667 1027 N ATOM 8 CA PHE A 8 -10.743 -0.614 0.819 1.00 31.28 C ANISOU 8 CA PHE A 8 3849 3720 4316 -848 -549 1191 C ATOM 9 C PHE A 8 -9.510 -0.081 0.092 1.00 31.36 C ANISOU 9 C PHE A 8 4014 3906 3994 -1269 -647 1248 C ATOM 10 O PHE A 8 -9.610 0.458 -1.011 1.00 34.39 O ANISOU 10 O PHE A 8 4730 4320 4014 -1314 -980 1359 O ATOM 11 CB PHE A 8 -10.569 -2.102 1.144 1.00 27.11 C ANISOU 11 CB PHE A 8 3568 2737 3996 -802 -199 650 C ATOM 12 CG PHE A 8 -11.723 -2.691 1.899 1.00 26.26 C ANISOU 12 CG PHE A 8 3260 2934 3782 -736 207 457 C ATOM 13 CD1 PHE A 8 -12.119 -2.150 3.111 1.00 27.34 C ANISOU 13 CD1 PHE A 8 3386 3150 3851 -284 539 312 C ATOM 14 CD2 PHE A 8 -12.406 -3.792 1.405 1.00 28.54 C ANISOU 14 CD2 PHE A 8 3935 3200 3706 -1150 728 256 C ATOM 15 CE1 PHE A 8 -13.183 -2.689 3.819 1.00 27.91 C ANISOU 15 CE1 PHE A 8 3415 3378 3812 -526 910 134 C ATOM 16 CE2 PHE A 8 -13.474 -4.342 2.104 1.00 29.05 C ANISOU 16 CE2 PHE A 8 4202 3302 3533 -1210 1023 86 C ATOM 17 CZ PHE A 8 -13.865 -3.791 3.314 1.00 29.00 C ANISOU 17 CZ PHE A 8 4018 3321 3678 -543 1035 -108 C ATOM 18 N GLY A 9 -8.348 -0.228 0.723 1.00 26.97 N ANISOU 18 N GLY A 9 3341 3348 3556 -1143 -367 1372 N ATOM 19 CA GLY A 9 -7.111 0.301 0.174 1.00 26.97 C ANISOU 19 CA GLY A 9 3280 3810 3156 -996 8 1158 C ATOM 20 C GLY A 9 -7.088 1.817 0.076 1.00 25.42 C ANISOU 20 C GLY A 9 2985 3721 2952 -870 75 554 C ATOM 21 O GLY A 9 -6.379 2.378 -0.755 1.00 26.71 O ANISOU 21 O GLY A 9 3428 3820 2898 -1105 155 509 O ATOM 22 N GLN A 10 -7.848 2.484 0.936 1.00 24.86 N ANISOU 22 N GLN A 10 2702 3696 3048 -576 -91 184 N ATOM 23 CA GLN A 10 -7.956 3.939 0.900 1.00 25.89 C ANISOU 23 CA GLN A 10 3156 3743 2935 -133 28 -68 C ATOM 24 C GLN A 10 -6.682 4.666 1.335 1.00 22.51 C ANISOU 24 C GLN A 10 2893 3092 2565 -35 341 192 C ATOM 25 O GLN A 10 -6.426 5.796 0.899 1.00 22.77 O ANISOU 25 O GLN A 10 3420 2891 2339 -252 232 353 O ATOM 26 CB GLN A 10 -9.117 4.391 1.790 1.00 29.14 C ANISOU 26 CB GLN A 10 3467 4335 3267 -55 -56 -612 C ATOM 27 CG GLN A 10 -10.456 3.792 1.410 1.00 34.83 C ANISOU 27 CG GLN A 10 4632 4878 3724 82 -16 -591 C ATOM 28 CD GLN A 10 -11.081 4.486 0.222 1.00 41.83 C ANISOU 28 CD GLN A 10 6229 5472 4190 -327 56 -605 C ATOM 29 OE1 GLN A 10 -11.592 3.838 -0.691 1.00 45.72 O ANISOU 29 OE1 GLN A 10 6939 6014 4419 -290 168 -419 O ATOM 30 NE2 GLN A 10 -11.041 5.815 0.224 1.00 44.09 N ANISOU 30 NE2 GLN A 10 6704 5642 4403 -430 151 -577 N ATOM 31 N HIS A 11 -5.905 4.038 2.219 1.00 22.69 N ANISOU 31 N HIS A 11 3060 3099 2462 -206 814 37 N ATOM 32 CA HIS A 11 -4.734 4.687 2.808 1.00 23.94 C ANISOU 32 CA HIS A 11 2874 3758 2464 38 880 79 C ATOM 33 C HIS A 11 -3.439 3.928 2.555 1.00 23.14 C ANISOU 33 C HIS A 11 2831 3559 2402 -276 782 188 C ATOM 34 O HIS A 11 -2.360 4.516 2.540 1.00 25.40 O ANISOU 34 O HIS A 11 2922 3919 2809 -275 371 -109 O ATOM 35 CB HIS A 11 -4.922 4.852 4.316 1.00 27.29 C ANISOU 35 CB HIS A 11 3362 4241 2764 182 949 -107 C ATOM 36 CG HIS A 11 -6.270 5.374 4.698 1.00 31.95 C ANISOU 36 CG HIS A 11 4058 4876 3206 261 825 -241 C ATOM 37 ND1 HIS A 11 -7.252 4.568 5.238 1.00 35.10 N ANISOU 37 ND1 HIS A 11 4579 5307 3448 682 755 -255 N ATOM 38 CD2 HIS A 11 -6.806 6.612 4.607 1.00 31.73 C ANISOU 38 CD2 HIS A 11 4100 4767 3189 537 784 -468 C ATOM 39 CE1 HIS A 11 -8.332 5.293 5.466 1.00 34.21 C ANISOU 39 CE1 HIS A 11 4401 5167 3430 831 851 -420 C ATOM 40 NE2 HIS A 11 -8.090 6.536 5.089 1.00 33.01 N ANISOU 40 NE2 HIS A 11 4259 4932 3350 705 820 -621 N ATOM 41 N LEU A 12 -3.545 2.622 2.360 1.00 20.64 N ANISOU 41 N LEU A 12 2345 3231 2266 -529 342 166 N ATOM 42 CA LEU A 12 -2.369 1.790 2.184 1.00 20.73 C ANISOU 42 CA LEU A 12 2361 3121 2392 -443 -194 274 C ATOM 43 C LEU A 12 -2.683 0.639 1.246 1.00 21.56 C ANISOU 43 C LEU A 12 2620 3143 2429 -338 -184 137 C ATOM 44 O LEU A 12 -3.722 -0.007 1.375 1.00 23.07 O ANISOU 44 O LEU A 12 2574 3554 2635 -656 61 19 O ATOM 45 CB LEU A 12 -1.899 1.243 3.539 1.00 25.04 C ANISOU 45 CB LEU A 12 2983 3788 2743 203 -575 387 C ATOM 46 CG LEU A 12 -0.811 0.167 3.536 1.00 26.98 C ANISOU 46 CG LEU A 12 3628 3671 2950 176 -945 504 C ATOM 47 CD1 LEU A 12 0.513 0.745 3.044 1.00 26.68 C ANISOU 47 CD1 LEU A 12 3518 3679 2939 37 -1252 762 C ATOM 48 CD2 LEU A 12 -0.656 -0.442 4.930 1.00 26.73 C ANISOU 48 CD2 LEU A 12 3872 3239 3045 232 -905 456 C ATOM 49 N LEU A 13 -1.783 0.393 0.300 1.00 18.75 N ANISOU 49 N LEU A 13 2499 2363 2260 44 9 391 N ATOM 50 CA LEU A 13 -1.876 -0.780 -0.558 1.00 20.90 C ANISOU 50 CA LEU A 13 2982 2743 2215 297 -65 704 C ATOM 51 C LEU A 13 -0.673 -1.676 -0.306 1.00 21.63 C ANISOU 51 C LEU A 13 3024 2545 2649 562 -196 798 C ATOM 52 O LEU A 13 0.469 -1.210 -0.318 1.00 23.02 O ANISOU 52 O LEU A 13 3492 2347 2906 282 60 658 O ATOM 53 CB LEU A 13 -1.944 -0.379 -2.034 1.00 22.07 C ANISOU 53 CB LEU A 13 3377 2911 2097 -272 251 895 C ATOM 54 CG LEU A 13 -3.266 0.271 -2.426 1.00 25.20 C ANISOU 54 CG LEU A 13 3906 3338 2331 -257 145 794 C ATOM 55 CD1 LEU A 13 -3.225 0.744 -3.858 1.00 26.68 C ANISOU 55 CD1 LEU A 13 4048 3794 2293 21 -61 730 C ATOM 56 CD2 LEU A 13 -4.428 -0.691 -2.211 1.00 29.25 C ANISOU 56 CD2 LEU A 13 4686 3800 2625 -528 185 600 C ATOM 57 N VAL A 14 -0.944 -2.954 -0.063 1.00 21.19 N ANISOU 57 N VAL A 14 2874 2563 2614 466 -253 669 N ATOM 58 CA VAL A 14 0.097 -3.956 0.095 1.00 20.60 C ANISOU 58 CA VAL A 14 3028 2357 2442 -238 -262 592 C ATOM 59 C VAL A 14 -0.058 -5.021 -0.984 1.00 21.92 C ANISOU 59 C VAL A 14 3280 2611 2436 -345 -583 479 C ATOM 60 O VAL A 14 -1.163 -5.509 -1.236 1.00 23.78 O ANISOU 60 O VAL A 14 3712 2844 2479 -106 -869 -50 O ATOM 61 CB VAL A 14 0.022 -4.641 1.472 1.00 19.97 C ANISOU 61 CB VAL A 14 3228 2034 2326 -54 -439 536 C ATOM 62 CG1 VAL A 14 1.124 -5.662 1.597 1.00 22.98 C ANISOU 62 CG1 VAL A 14 3632 2592 2507 51 -434 701 C ATOM 63 CG2 VAL A 14 0.098 -3.607 2.599 1.00 20.75 C ANISOU 63 CG2 VAL A 14 3044 2647 2192 -46 -211 666 C ATOM 64 N SER A 15 1.046 -5.377 -1.625 1.00 22.92 N ANISOU 64 N SER A 15 3542 2633 2532 -571 -492 290 N ATOM 65 CA SER A 15 1.036 -6.433 -2.626 1.00 27.80 C ANISOU 65 CA SER A 15 4463 3198 2901 -792 -433 -61 C ATOM 66 C SER A 15 0.265 -7.664 -2.132 1.00 28.59 C ANISOU 66 C SER A 15 5100 3043 2719 -1083 -819 -202 C ATOM 67 O SER A 15 0.492 -8.149 -1.023 1.00 26.35 O ANISOU 67 O SER A 15 4918 2542 2551 -929 -845 -170 O ATOM 68 CB SER A 15 2.471 -6.802 -3.000 1.00 31.23 C ANISOU 68 CB SER A 15 4923 3744 3197 -596 -153 -303 C ATOM 69 OG SER A 15 2.525 -8.078 -3.597 1.00 36.12 O ANISOU 69 OG SER A 15 5571 4515 3637 -512 117 -171 O ATOM 70 N GLU A 16 -0.648 -8.165 -2.959 1.00 31.19 N ANISOU 70 N GLU A 16 5937 3268 2645 -1924 -892 -117 N ATOM 71 CA GLU A 16 -1.490 -9.298 -2.572 1.00 33.76 C ANISOU 71 CA GLU A 16 6390 3839 2598 -1959 -882 -34 C ATOM 72 C GLU A 16 -0.685 -10.548 -2.243 1.00 32.04 C ANISOU 72 C GLU A 16 6376 3779 2019 -2086 -507 -3 C ATOM 73 O GLU A 16 -1.081 -11.349 -1.390 1.00 32.78 O ANISOU 73 O GLU A 16 6708 3718 2026 -2044 -444 192 O ATOM 74 CB GLU A 16 -2.509 -9.605 -3.670 1.00 40.56 C ANISOU 74 CB GLU A 16 7107 4887 3416 -1587 -717 255 C ATOM 75 CG GLU A 16 -3.720 -8.688 -3.643 1.00 47.37 C ANISOU 75 CG GLU A 16 7990 5952 4054 -1309 -81 515 C ATOM 76 CD GLU A 16 -4.569 -8.896 -2.404 1.00 51.82 C ANISOU 76 CD GLU A 16 8654 6495 4540 -1146 434 857 C ATOM 77 OE1 GLU A 16 -4.578 -10.030 -1.876 1.00 53.63 O ANISOU 77 OE1 GLU A 16 8922 6693 4759 -897 666 1174 O ATOM 78 OE2 GLU A 16 -5.226 -7.928 -1.960 1.00 52.87 O ANISOU 78 OE2 GLU A 16 8721 6656 4708 -1510 565 808 O ATOM 79 N GLY A 17 0.443 -10.715 -2.923 1.00 31.64 N ANISOU 79 N GLY A 17 6389 3792 1841 -1547 35 -88 N ATOM 80 CA GLY A 17 1.295 -11.866 -2.694 1.00 30.92 C ANISOU 80 CA GLY A 17 6365 3753 1627 -1032 477 85 C ATOM 81 C GLY A 17 1.825 -11.869 -1.280 1.00 28.11 C ANISOU 81 C GLY A 17 6272 3117 1292 -876 675 19 C ATOM 82 O GLY A 17 1.953 -12.923 -0.654 1.00 29.16 O ANISOU 82 O GLY A 17 6569 3285 1225 -842 1040 -185 O ATOM 83 N VAL A 18 2.128 -10.680 -0.769 1.00 23.87 N ANISOU 83 N VAL A 18 5195 2775 1100 -933 682 -64 N ATOM 84 CA VAL A 18 2.630 -10.543 0.588 1.00 20.52 C ANISOU 84 CA VAL A 18 3947 2616 1233 -645 774 -100 C ATOM 85 C VAL A 18 1.536 -10.878 1.597 1.00 19.79 C ANISOU 85 C VAL A 18 3526 2558 1435 -241 656 -262 C ATOM 86 O VAL A 18 1.773 -11.617 2.555 1.00 17.65 O ANISOU 86 O VAL A 18 2747 2529 1429 -35 404 -92 O ATOM 87 CB VAL A 18 3.206 -9.133 0.844 1.00 18.48 C ANISOU 87 CB VAL A 18 2964 2547 1509 -757 1063 -235 C ATOM 88 CG1 VAL A 18 3.520 -8.943 2.326 1.00 20.22 C ANISOU 88 CG1 VAL A 18 3197 2529 1954 19 869 -365 C ATOM 89 CG2 VAL A 18 4.444 -8.902 -0.025 1.00 21.22 C ANISOU 89 CG2 VAL A 18 3038 3004 2020 -395 861 -304 C ATOM 90 N LEU A 19 0.330 -10.360 1.376 1.00 17.72 N ANISOU 90 N LEU A 19 2935 2445 1350 -657 761 -206 N ATOM 91 CA LEU A 19 -0.772 -10.686 2.271 1.00 17.71 C ANISOU 91 CA LEU A 19 2669 2438 1622 -490 452 24 C ATOM 92 C LEU A 19 -1.046 -12.188 2.273 1.00 20.12 C ANISOU 92 C LEU A 19 3231 2697 1716 -240 186 -64 C ATOM 93 O LEU A 19 -1.277 -12.779 3.326 1.00 19.55 O ANISOU 93 O LEU A 19 2664 2928 1833 12 143 -129 O ATOM 94 CB LEU A 19 -2.037 -9.908 1.907 1.00 19.71 C ANISOU 94 CB LEU A 19 2749 2640 2097 -302 41 361 C ATOM 95 CG LEU A 19 -1.919 -8.379 1.965 1.00 20.68 C ANISOU 95 CG LEU A 19 2841 2561 2454 -245 1 352 C ATOM 96 CD1 LEU A 19 -3.242 -7.729 1.607 1.00 21.44 C ANISOU 96 CD1 LEU A 19 2942 2686 2516 128 5 756 C ATOM 97 CD2 LEU A 19 -1.446 -7.918 3.342 1.00 21.77 C ANISOU 97 CD2 LEU A 19 3047 2676 2546 -498 140 285 C ATOM 98 N LYS A 20 -1.018 -12.810 1.098 1.00 20.41 N ANISOU 98 N LYS A 20 3510 2423 1821 -590 -32 -72 N ATOM 99 CA LYS A 20 -1.275 -14.243 1.016 1.00 22.93 C ANISOU 99 CA LYS A 20 4011 2642 2059 -1070 -211 -1 C ATOM 100 C LYS A 20 -0.242 -15.059 1.778 1.00 23.19 C ANISOU 100 C LYS A 20 4359 2612 1839 -984 136 10 C ATOM 101 O LYS A 20 -0.581 -16.070 2.397 1.00 24.15 O ANISOU 101 O LYS A 20 4648 2451 2074 -921 46 327 O ATOM 102 CB LYS A 20 -1.349 -14.703 -0.440 1.00 30.04 C ANISOU 102 CB LYS A 20 5181 3579 2654 -1063 -293 -25 C ATOM 103 CG LYS A 20 -2.605 -14.237 -1.141 1.00 34.84 C ANISOU 103 CG LYS A 20 6021 4100 3115 -1053 -736 37 C ATOM 104 CD LYS A 20 -2.826 -14.983 -2.442 1.00 41.22 C ANISOU 104 CD LYS A 20 6942 4995 3723 -823 -1017 32 C ATOM 105 CE LYS A 20 -4.213 -14.697 -2.979 1.00 45.13 C ANISOU 105 CE LYS A 20 7441 5510 4195 -705 -1090 -115 C ATOM 106 NZ LYS A 20 -4.556 -13.254 -2.819 1.00 47.26 N ANISOU 106 NZ LYS A 20 7683 5869 4402 -793 -1167 -305 N ATOM 107 N LYS A 21 1.014 -14.625 1.728 1.00 22.91 N ANISOU 107 N LYS A 21 4201 2747 1756 -483 394 -160 N ATOM 108 CA LYS A 21 2.087 -15.320 2.429 1.00 23.01 C ANISOU 108 CA LYS A 21 3814 3070 1856 -94 733 -240 C ATOM 109 C LYS A 21 1.890 -15.178 3.930 1.00 20.06 C ANISOU 109 C LYS A 21 3285 2657 1678 -69 381 -380 C ATOM 110 O LYS A 21 2.099 -16.121 4.693 1.00 19.96 O ANISOU 110 O LYS A 21 3176 2549 1857 -82 516 -225 O ATOM 111 CB LYS A 21 3.453 -14.752 2.030 1.00 24.21 C ANISOU 111 CB LYS A 21 3710 3222 2267 15 866 -222 C ATOM 112 CG LYS A 21 4.618 -15.338 2.819 1.00 29.39 C ANISOU 112 CG LYS A 21 4616 3605 2944 19 797 -671 C ATOM 113 CD LYS A 21 4.837 -16.808 2.488 1.00 31.15 C ANISOU 113 CD LYS A 21 5066 3436 3331 262 226 -981 C ATOM 114 CE LYS A 21 5.982 -17.404 3.306 1.00 32.52 C ANISOU 114 CE LYS A 21 5438 3441 3477 245 69 -912 C ATOM 115 NZ LYS A 21 6.384 -18.760 2.823 1.00 33.03 N ANISOU 115 NZ LYS A 21 5297 3707 3544 -25 103 -1037 N ATOM 116 N ILE A 22 1.482 -13.988 4.347 1.00 17.31 N ANISOU 116 N ILE A 22 2743 2257 1576 54 282 -580 N ATOM 117 CA ILE A 22 1.195 -13.745 5.752 1.00 16.53 C ANISOU 117 CA ILE A 22 2406 2222 1652 97 74 -380 C ATOM 118 C ILE A 22 0.094 -14.683 6.233 1.00 15.99 C ANISOU 118 C ILE A 22 2040 2352 1682 133 -200 -115 C ATOM 119 O ILE A 22 0.235 -15.335 7.281 1.00 16.17 O ANISOU 119 O ILE A 22 2339 2217 1586 43 -107 7 O ATOM 120 CB ILE A 22 0.809 -12.280 6.004 1.00 15.72 C ANISOU 120 CB ILE A 22 2203 2053 1715 -95 121 -426 C ATOM 121 CG1 ILE A 22 2.045 -11.384 5.861 1.00 15.95 C ANISOU 121 CG1 ILE A 22 2134 1993 1930 -311 3 -479 C ATOM 122 CG2 ILE A 22 0.161 -12.120 7.377 1.00 17.06 C ANISOU 122 CG2 ILE A 22 2147 2508 1824 198 -204 -135 C ATOM 123 CD1 ILE A 22 1.732 -9.899 5.772 1.00 16.80 C ANISOU 123 CD1 ILE A 22 2541 1999 1843 7 -237 92 C ATOM 124 N ALA A 23 -0.993 -14.771 5.466 1.00 15.75 N ANISOU 124 N ALA A 23 1835 2311 1836 9 -174 -172 N ATOM 125 CA ALA A 23 -2.097 -15.652 5.842 1.00 17.00 C ANISOU 125 CA ALA A 23 1935 2561 1960 -222 -98 241 C ATOM 126 C ALA A 23 -1.658 -17.113 5.875 1.00 17.25 C ANISOU 126 C ALA A 23 2655 2093 1804 -339 226 -73 C ATOM 127 O ALA A 23 -2.084 -17.878 6.752 1.00 16.92 O ANISOU 127 O ALA A 23 2706 2075 1647 -222 443 -71 O ATOM 128 CB ALA A 23 -3.297 -15.464 4.899 1.00 17.91 C ANISOU 128 CB ALA A 23 2169 2885 1751 -149 -276 622 C ATOM 129 N AGLU A 24 -0.803 -17.493 4.926 0.50 19.94 N ANISOU 129 N AGLU A 24 3535 2173 1868 -165 47 -133 N ATOM 130 N BGLU A 24 -0.811 -17.501 4.925 0.50 19.64 N ANISOU 130 N BGLU A 24 3536 2150 1775 -187 30 -163 N ATOM 131 CA AGLU A 24 -0.287 -18.859 4.851 0.50 22.19 C ANISOU 131 CA AGLU A 24 3766 2663 2002 -169 372 -268 C ATOM 132 CA BGLU A 24 -0.299 -18.867 4.872 0.50 21.60 C ANISOU 132 CA BGLU A 24 3761 2624 1821 -228 352 -332 C ATOM 133 C AGLU A 24 0.553 -19.230 6.077 0.50 20.67 C ANISOU 133 C AGLU A 24 3307 2498 2049 -180 311 -278 C ATOM 134 C BGLU A 24 0.522 -19.222 6.112 0.50 20.39 C ANISOU 134 C BGLU A 24 3316 2483 1948 -249 307 -278 C ATOM 135 O AGLU A 24 0.514 -20.371 6.542 0.50 21.11 O ANISOU 135 O AGLU A 24 3270 2581 2167 -140 406 -436 O ATOM 136 O BGLU A 24 0.444 -20.344 6.617 0.50 20.73 O ANISOU 136 O BGLU A 24 3257 2573 2045 -303 437 -384 O ATOM 137 CB AGLU A 24 0.523 -19.058 3.564 0.50 26.31 C ANISOU 137 CB AGLU A 24 4470 3273 2253 -243 409 -217 C ATOM 138 CB BGLU A 24 0.534 -19.078 3.610 0.50 25.10 C ANISOU 138 CB BGLU A 24 4421 3194 1920 -325 350 -391 C ATOM 139 CG AGLU A 24 1.184 -20.424 3.452 0.50 31.00 C ANISOU 139 CG AGLU A 24 5162 3975 2640 57 362 -89 C ATOM 140 CG BGLU A 24 -0.291 -19.183 2.347 0.50 29.23 C ANISOU 140 CG BGLU A 24 5091 3863 2149 -7 320 -324 C ATOM 141 CD AGLU A 24 1.705 -20.711 2.056 0.50 35.26 C ANISOU 141 CD AGLU A 24 5839 4486 3070 252 221 128 C ATOM 142 CD BGLU A 24 0.551 -19.028 1.099 0.50 33.19 C ANISOU 142 CD BGLU A 24 5910 4326 2375 284 353 -297 C ATOM 143 OE1AGLU A 24 1.218 -20.078 1.096 0.50 37.07 O ANISOU 143 OE1AGLU A 24 6096 4804 3183 131 -42 117 O ATOM 144 OE1BGLU A 24 1.787 -18.897 1.234 0.50 34.07 O ANISOU 144 OE1BGLU A 24 6142 4313 2490 222 182 -123 O ATOM 145 OE2AGLU A 24 2.599 -21.573 1.917 0.50 36.55 O ANISOU 145 OE2AGLU A 24 5920 4678 3288 428 359 123 O ATOM 146 OE2BGLU A 24 -0.020 -19.031 -0.012 0.50 35.20 O ANISOU 146 OE2BGLU A 24 6337 4681 2354 584 463 -445 O ATOM 147 N GLU A 25 1.304 -18.264 6.601 1.00 17.69 N ANISOU 147 N GLU A 25 2539 2280 1902 -204 308 -354 N ATOM 148 CA GLU A 25 2.133 -18.490 7.789 1.00 17.88 C ANISOU 148 CA GLU A 25 2413 2241 2140 16 57 -360 C ATOM 149 C GLU A 25 1.300 -18.771 9.037 1.00 15.67 C ANISOU 149 C GLU A 25 1866 1923 2164 349 -152 -289 C ATOM 150 O GLU A 25 1.795 -19.357 10.007 1.00 17.05 O ANISOU 150 O GLU A 25 1781 2255 2439 445 -213 187 O ATOM 151 CB GLU A 25 3.086 -17.314 8.042 1.00 20.61 C ANISOU 151 CB GLU A 25 2718 2735 2376 -289 271 -369 C ATOM 152 CG GLU A 25 4.278 -17.251 7.093 1.00 27.85 C ANISOU 152 CG GLU A 25 3894 3713 2974 30 474 -26 C ATOM 153 CD GLU A 25 5.138 -18.514 7.122 1.00 32.44 C ANISOU 153 CD GLU A 25 4534 4473 3318 154 758 -216 C ATOM 154 OE1 GLU A 25 5.358 -19.080 8.215 1.00 34.27 O ANISOU 154 OE1 GLU A 25 4762 4714 3542 507 607 -186 O ATOM 155 OE2 GLU A 25 5.607 -18.937 6.045 1.00 35.40 O ANISOU 155 OE2 GLU A 25 5030 4939 3481 118 743 -382 O ATOM 156 N LEU A 26 0.040 -18.353 9.017 1.00 14.67 N ANISOU 156 N LEU A 26 1763 1780 2030 245 89 -183 N ATOM 157 CA LEU A 26 -0.845 -18.566 10.155 1.00 14.58 C ANISOU 157 CA LEU A 26 1958 1775 1806 540 339 -220 C ATOM 158 C LEU A 26 -1.322 -20.001 10.251 1.00 12.75 C ANISOU 158 C LEU A 26 1630 1481 1732 -14 244 -278 C ATOM 159 O LEU A 26 -1.872 -20.410 11.281 1.00 14.88 O ANISOU 159 O LEU A 26 2154 1865 1633 -40 172 -67 O ATOM 160 CB LEU A 26 -2.069 -17.665 10.068 1.00 14.70 C ANISOU 160 CB LEU A 26 1933 1978 1672 986 -317 -310 C ATOM 161 CG LEU A 26 -1.888 -16.201 10.426 1.00 14.91 C ANISOU 161 CG LEU A 26 2099 2008 1556 697 -401 -521 C ATOM 162 CD1 LEU A 26 -3.171 -15.464 10.123 1.00 18.98 C ANISOU 162 CD1 LEU A 26 2842 2370 2000 1288 -658 -246 C ATOM 163 CD2 LEU A 26 -1.506 -16.045 11.909 1.00 15.59 C ANISOU 163 CD2 LEU A 26 2174 2466 1281 120 -267 -277 C ATOM 164 N ASN A 27 -1.139 -20.756 9.171 1.00 14.29 N ANISOU 164 N ASN A 27 1824 1583 2023 24 -220 -460 N ATOM 165 CA ASN A 27 -1.592 -22.142 9.119 1.00 15.25 C ANISOU 165 CA ASN A 27 2375 1235 2181 341 -376 -449 C ATOM 166 C ASN A 27 -3.046 -22.291 9.567 1.00 16.13 C ANISOU 166 C ASN A 27 2520 1360 2248 178 -212 -246 C ATOM 167 O ASN A 27 -3.353 -23.077 10.463 1.00 16.99 O ANISOU 167 O ASN A 27 2678 1400 2375 -288 -359 161 O ATOM 168 CB ASN A 27 -0.688 -23.029 9.977 1.00 19.76 C ANISOU 168 CB ASN A 27 3144 1693 2670 739 -105 -519 C ATOM 169 CG ASN A 27 -0.994 -24.498 9.807 1.00 26.71 C ANISOU 169 CG ASN A 27 4285 2742 3122 763 20 -57 C ATOM 170 OD1 ASN A 27 -1.294 -24.956 8.702 1.00 30.82 O ANISOU 170 OD1 ASN A 27 5150 3271 3289 710 524 185 O ATOM 171 ND2 ASN A 27 -0.925 -25.250 10.904 1.00 29.36 N ANISOU 171 ND2 ASN A 27 4630 3143 3381 1255 -573 285 N ATOM 172 N AILE A 28 -3.938 -21.536 8.937 0.50 14.09 N ANISOU 172 N AILE A 28 1764 1442 2148 97 -319 -430 N ATOM 173 N BILE A 28 -3.939 -21.533 8.938 0.50 15.00 N ANISOU 173 N BILE A 28 1811 1614 2272 104 -190 -419 N ATOM 174 CA AILE A 28 -5.333 -21.497 9.355 0.50 13.00 C ANISOU 174 CA AILE A 28 1649 1107 2182 86 -666 -202 C ATOM 175 CA BILE A 28 -5.342 -21.511 9.337 0.50 15.31 C ANISOU 175 CA BILE A 28 1852 1550 2415 49 -398 -257 C ATOM 176 C AILE A 28 -6.055 -22.803 9.063 0.50 16.16 C ANISOU 176 C AILE A 28 2512 1364 2261 -212 -665 -223 C ATOM 177 C BILE A 28 -6.032 -22.842 9.074 0.50 17.33 C ANISOU 177 C BILE A 28 2535 1603 2446 -216 -522 -307 C ATOM 178 O AILE A 28 -6.056 -23.294 7.935 0.50 18.45 O ANISOU 178 O AILE A 28 2981 1635 2393 -297 -814 -159 O ATOM 179 O BILE A 28 -6.026 -23.351 7.953 0.50 19.06 O ANISOU 179 O BILE A 28 2910 1782 2548 -258 -689 -245 O ATOM 180 CB AILE A 28 -6.087 -20.335 8.690 0.50 13.03 C ANISOU 180 CB AILE A 28 1663 1081 2204 158 -825 116 C ATOM 181 CB BILE A 28 -6.124 -20.394 8.615 0.50 17.63 C ANISOU 181 CB BILE A 28 2205 1913 2581 62 -341 -13 C ATOM 182 CG1AILE A 28 -5.440 -19.003 9.078 0.50 12.23 C ANISOU 182 CG1AILE A 28 1814 536 2294 -82 -908 -57 C ATOM 183 CG1BILE A 28 -5.488 -19.031 8.891 0.50 19.84 C ANISOU 183 CG1BILE A 28 2889 1885 2763 -180 -203 -101 C ATOM 184 CG2AILE A 28 -7.556 -20.364 9.088 0.50 16.14 C ANISOU 184 CG2AILE A 28 2189 1653 2288 503 -536 181 C ATOM 185 CG2BILE A 28 -7.582 -20.400 9.056 0.50 19.13 C ANISOU 185 CG2BILE A 28 2351 2275 2643 452 -143 50 C ATOM 186 CD1AILE A 28 -5.892 -17.836 8.237 0.50 9.37 C ANISOU 186 CD1AILE A 28 1257 51 2251 -190 -1104 30 C ATOM 187 CD1BILE A 28 -5.518 -18.639 10.345 0.50 21.32 C ANISOU 187 CD1BILE A 28 3269 1938 2894 -302 93 -28 C ATOM 188 N AGLU A 29 -6.671 -23.359 10.098 0.50 16.59 N ANISOU 188 N AGLU A 29 2781 1309 2213 -199 -570 -350 N ATOM 189 N BGLU A 29 -6.627 -23.403 10.120 0.50 17.78 N ANISOU 189 N BGLU A 29 2818 1521 2414 -227 -499 -494 N ATOM 190 CA AGLU A 29 -7.349 -24.638 9.987 0.50 17.96 C ANISOU 190 CA AGLU A 29 2929 1455 2440 -238 -344 -15 C ATOM 191 CA BGLU A 29 -7.331 -24.671 10.006 0.50 19.75 C ANISOU 191 CA BGLU A 29 3049 1819 2635 -242 -298 -227 C ATOM 192 C AGLU A 29 -8.759 -24.530 10.545 0.50 16.90 C ANISOU 192 C AGLU A 29 2627 1416 2376 -639 -494 126 C ATOM 193 C BGLU A 29 -8.748 -24.539 10.547 0.50 17.47 C ANISOU 193 C BGLU A 29 2630 1541 2466 -631 -464 91 C ATOM 194 O AGLU A 29 -9.085 -23.569 11.245 0.50 16.75 O ANISOU 194 O AGLU A 29 2614 1573 2175 -781 -433 -170 O ATOM 195 O BGLU A 29 -9.070 -23.567 11.234 0.50 16.97 O ANISOU 195 O BGLU A 29 2545 1643 2258 -702 -372 -68 O ATOM 196 CB AGLU A 29 -6.556 -25.713 10.731 0.50 18.78 C ANISOU 196 CB AGLU A 29 3226 1208 2699 -321 -278 341 C ATOM 197 CB BGLU A 29 -6.572 -25.776 10.748 0.50 23.37 C ANISOU 197 CB BGLU A 29 3684 2189 3004 -139 -244 -140 C ATOM 198 CG AGLU A 29 -5.175 -25.954 10.141 0.50 20.77 C ANISOU 198 CG AGLU A 29 3490 1454 2946 -139 -239 731 C ATOM 199 CG BGLU A 29 -6.541 -25.622 12.259 0.50 28.59 C ANISOU 199 CG BGLU A 29 4435 3070 3356 280 -276 -22 C ATOM 200 CD AGLU A 29 -4.354 -26.944 10.942 0.50 26.70 C ANISOU 200 CD AGLU A 29 4715 2200 3227 39 -206 663 C ATOM 201 CD BGLU A 29 -5.731 -26.715 12.937 0.50 35.55 C ANISOU 201 CD BGLU A 29 5581 4188 3737 988 -230 -22 C ATOM 202 OE1AGLU A 29 -4.362 -26.862 12.190 0.50 28.71 O ANISOU 202 OE1AGLU A 29 5034 2515 3359 -119 -22 681 O ATOM 203 OE1BGLU A 29 -4.970 -27.414 12.233 0.50 38.43 O ANISOU 203 OE1BGLU A 29 6211 4356 4034 1242 -102 103 O ATOM 204 OE2AGLU A 29 -3.693 -27.802 10.322 0.50 30.43 O ANISOU 204 OE2AGLU A 29 5555 2583 3424 123 -410 596 O ATOM 205 OE2BGLU A 29 -5.857 -26.879 14.170 0.50 38.05 O ANISOU 205 OE2BGLU A 29 5755 4960 3742 1565 -555 166 O ATOM 206 N GLU A 30 -9.592 -25.511 10.211 1.00 17.76 N ANISOU 206 N GLU A 30 2604 1586 2555 -659 -520 596 N ATOM 207 CA GLU A 30 -10.956 -25.575 10.713 1.00 17.21 C ANISOU 207 CA GLU A 30 2349 1325 2862 -820 -690 246 C ATOM 208 C GLU A 30 -11.031 -25.347 12.221 1.00 17.96 C ANISOU 208 C GLU A 30 2654 1485 2682 -215 -684 171 C ATOM 209 O GLU A 30 -10.291 -25.964 12.994 1.00 18.47 O ANISOU 209 O GLU A 30 2801 1848 2367 -233 -631 350 O ATOM 210 CB GLU A 30 -11.548 -26.947 10.381 1.00 20.11 C ANISOU 210 CB GLU A 30 2546 1628 3465 -861 -181 502 C ATOM 211 CG GLU A 30 -13.036 -27.018 10.551 1.00 24.43 C ANISOU 211 CG GLU A 30 2592 2752 3937 -362 -344 387 C ATOM 212 CD GLU A 30 -13.766 -26.332 9.415 1.00 28.64 C ANISOU 212 CD GLU A 30 3003 3567 4310 50 167 497 C ATOM 213 OE1 GLU A 30 -13.371 -26.538 8.244 1.00 31.59 O ANISOU 213 OE1 GLU A 30 3206 4278 4519 -109 268 244 O ATOM 214 OE2 GLU A 30 -14.731 -25.590 9.689 1.00 31.84 O ANISOU 214 OE2 GLU A 30 3507 4006 4585 492 317 447 O ATOM 215 N GLY A 31 -11.933 -24.466 12.639 1.00 17.70 N ANISOU 215 N GLY A 31 2805 1261 2658 -559 -803 2 N ATOM 216 CA GLY A 31 -12.129 -24.194 14.052 1.00 17.62 C ANISOU 216 CA GLY A 31 2537 1639 2517 -656 -977 7 C ATOM 217 C GLY A 31 -11.279 -23.072 14.627 1.00 15.34 C ANISOU 217 C GLY A 31 1994 1425 2409 -504 -779 85 C ATOM 218 O GLY A 31 -11.510 -22.655 15.763 1.00 19.38 O ANISOU 218 O GLY A 31 2764 1920 2679 -569 -495 66 O ATOM 219 N ASN A 32 -10.307 -22.579 13.855 1.00 14.66 N ANISOU 219 N ASN A 32 2000 1524 2043 -435 -699 -50 N ATOM 220 CA ASN A 32 -9.398 -21.529 14.323 1.00 14.76 C ANISOU 220 CA ASN A 32 2018 1490 2099 -513 -671 -96 C ATOM 221 C ASN A 32 -10.094 -20.196 14.540 1.00 12.75 C ANISOU 221 C ASN A 32 1540 1216 2086 -381 -698 138 C ATOM 222 O ASN A 32 -10.968 -19.794 13.765 1.00 14.57 O ANISOU 222 O ASN A 32 1755 1549 2231 -378 -803 147 O ATOM 223 CB ASN A 32 -8.266 -21.273 13.322 1.00 14.13 C ANISOU 223 CB ASN A 32 1469 1566 2334 -281 -340 -360 C ATOM 224 CG ASN A 32 -7.133 -22.271 13.420 1.00 16.76 C ANISOU 224 CG ASN A 32 1863 2069 2433 -416 -485 -397 C ATOM 225 OD1 ASN A 32 -6.153 -22.151 12.688 1.00 17.92 O ANISOU 225 OD1 ASN A 32 2237 2100 2470 -351 -310 -527 O ATOM 226 ND2 ASN A 32 -7.255 -23.263 14.309 1.00 19.02 N ANISOU 226 ND2 ASN A 32 2689 2007 2528 -368 -237 -275 N ATOM 227 N THR A 33 -9.686 -19.497 15.586 1.00 11.59 N ANISOU 227 N THR A 33 1645 833 1923 -378 -322 -58 N ATOM 228 CA THR A 33 -10.090 -18.108 15.776 1.00 12.49 C ANISOU 228 CA THR A 33 1415 1288 2041 -542 -439 427 C ATOM 229 C THR A 33 -8.898 -17.213 15.503 1.00 10.55 C ANISOU 229 C THR A 33 1177 1013 1819 -195 -400 224 C ATOM 230 O THR A 33 -7.813 -17.423 16.048 1.00 11.72 O ANISOU 230 O THR A 33 1113 1147 2190 -186 -547 434 O ATOM 231 CB THR A 33 -10.633 -17.859 17.193 1.00 15.07 C ANISOU 231 CB THR A 33 1334 2046 2343 -611 -256 -43 C ATOM 232 OG1 THR A 33 -11.811 -18.649 17.393 1.00 18.35 O ANISOU 232 OG1 THR A 33 1791 2603 2575 -707 -110 153 O ATOM 233 CG2 THR A 33 -10.969 -16.387 17.400 1.00 17.34 C ANISOU 233 CG2 THR A 33 1831 2180 2577 -131 -312 -45 C ATOM 234 N VAL A 34 -9.099 -16.232 14.639 1.00 9.67 N ANISOU 234 N VAL A 34 1220 812 1641 -183 -133 -33 N ATOM 235 CA VAL A 34 -8.024 -15.344 14.241 1.00 9.43 C ANISOU 235 CA VAL A 34 1211 789 1580 -13 -363 150 C ATOM 236 C VAL A 34 -8.356 -13.927 14.699 1.00 8.99 C ANISOU 236 C VAL A 34 1223 742 1449 74 -439 211 C ATOM 237 O VAL A 34 -9.507 -13.516 14.643 1.00 9.97 O ANISOU 237 O VAL A 34 1020 1027 1738 18 -315 19 O ATOM 238 CB VAL A 34 -7.826 -15.374 12.717 1.00 11.04 C ANISOU 238 CB VAL A 34 1374 1274 1546 188 -193 -140 C ATOM 239 CG1 VAL A 34 -6.787 -14.343 12.283 1.00 11.82 C ANISOU 239 CG1 VAL A 34 1213 1858 1420 -382 -79 191 C ATOM 240 CG2 VAL A 34 -7.415 -16.771 12.279 1.00 12.76 C ANISOU 240 CG2 VAL A 34 1931 1324 1590 -117 -104 -583 C ATOM 241 N VAL A 35 -7.350 -13.209 15.183 1.00 9.28 N ANISOU 241 N VAL A 35 1284 812 1427 -285 -164 -138 N ATOM 242 CA VAL A 35 -7.496 -11.825 15.627 1.00 10.85 C ANISOU 242 CA VAL A 35 1333 1329 1458 -321 91 -59 C ATOM 243 C VAL A 35 -6.571 -10.950 14.792 1.00 8.58 C ANISOU 243 C VAL A 35 643 1189 1426 107 77 75 C ATOM 244 O VAL A 35 -5.352 -11.105 14.835 1.00 10.04 O ANISOU 244 O VAL A 35 765 1197 1851 119 64 -99 O ATOM 245 CB VAL A 35 -7.127 -11.664 17.121 1.00 10.56 C ANISOU 245 CB VAL A 35 1618 915 1478 -290 128 168 C ATOM 246 CG1 VAL A 35 -7.285 -10.217 17.549 1.00 12.57 C ANISOU 246 CG1 VAL A 35 1622 1287 1865 -188 -86 138 C ATOM 247 CG2 VAL A 35 -7.976 -12.590 18.003 1.00 10.99 C ANISOU 247 CG2 VAL A 35 1628 1137 1408 260 404 503 C ATOM 248 N GLU A 36 -7.158 -10.062 14.006 1.00 8.29 N ANISOU 248 N GLU A 36 583 1194 1371 -252 -8 293 N ATOM 249 CA GLU A 36 -6.410 -9.220 13.090 1.00 9.31 C ANISOU 249 CA GLU A 36 913 1134 1489 -8 -297 85 C ATOM 250 C GLU A 36 -6.266 -7.830 13.691 1.00 9.22 C ANISOU 250 C GLU A 36 938 806 1758 -3 -23 -28 C ATOM 251 O GLU A 36 -7.250 -7.244 14.161 1.00 10.96 O ANISOU 251 O GLU A 36 1004 1267 1890 238 13 -232 O ATOM 252 CB GLU A 36 -7.123 -9.159 11.738 1.00 11.25 C ANISOU 252 CB GLU A 36 1537 1137 1599 -84 -98 -69 C ATOM 253 CG GLU A 36 -6.485 -8.242 10.727 1.00 13.64 C ANISOU 253 CG GLU A 36 1616 1619 1946 205 -486 -10 C ATOM 254 CD GLU A 36 -7.344 -8.083 9.487 1.00 17.80 C ANISOU 254 CD GLU A 36 2079 2228 2455 -128 -389 77 C ATOM 255 OE1 GLU A 36 -8.382 -8.777 9.383 1.00 19.15 O ANISOU 255 OE1 GLU A 36 2028 2525 2721 -3 -102 206 O ATOM 256 OE2 GLU A 36 -6.984 -7.277 8.611 1.00 20.97 O ANISOU 256 OE2 GLU A 36 2804 2465 2699 356 -336 83 O ATOM 257 N VAL A 37 -5.035 -7.322 13.694 1.00 9.88 N ANISOU 257 N VAL A 37 1052 964 1735 -390 -6 105 N ATOM 258 CA VAL A 37 -4.732 -6.007 14.234 1.00 13.33 C ANISOU 258 CA VAL A 37 1580 1426 2058 -576 -133 -220 C ATOM 259 C VAL A 37 -3.912 -5.196 13.208 1.00 15.70 C ANISOU 259 C VAL A 37 1952 1467 2545 -756 -39 -9 C ATOM 260 O VAL A 37 -3.536 -5.713 12.159 1.00 17.96 O ANISOU 260 O VAL A 37 2154 2137 2533 -556 238 401 O ATOM 261 CB VAL A 37 -3.944 -6.138 15.560 1.00 12.46 C ANISOU 261 CB VAL A 37 1278 1545 1909 -464 310 11 C ATOM 262 CG1 VAL A 37 -4.706 -7.010 16.564 1.00 14.67 C ANISOU 262 CG1 VAL A 37 1780 2040 1752 -88 551 160 C ATOM 263 CG2 VAL A 37 -2.582 -6.737 15.308 1.00 14.89 C ANISOU 263 CG2 VAL A 37 1492 1896 2267 -673 189 -391 C ATOM 264 N GLY A 38 -3.645 -3.926 13.489 1.00 17.18 N ANISOU 264 N GLY A 38 1835 1734 2956 -900 278 522 N ATOM 265 CA GLY A 38 -2.787 -3.150 12.598 1.00 18.09 C ANISOU 265 CA GLY A 38 1854 1956 3063 -250 256 552 C ATOM 266 C GLY A 38 -3.484 -2.487 11.414 1.00 20.38 C ANISOU 266 C GLY A 38 2082 2478 3182 441 305 93 C ATOM 267 O GLY A 38 -4.681 -2.197 11.468 1.00 24.38 O ANISOU 267 O GLY A 38 2260 3534 3466 363 88 -297 O ATOM 268 N GLY A 39 -2.735 -2.249 10.338 1.00 18.02 N ANISOU 268 N GLY A 39 1914 1841 3091 23 -226 74 N ATOM 269 CA GLY A 39 -3.231 -1.463 9.219 1.00 18.94 C ANISOU 269 CA GLY A 39 2135 1918 3141 273 -395 316 C ATOM 270 C GLY A 39 -3.614 -2.235 7.969 1.00 19.08 C ANISOU 270 C GLY A 39 2306 2046 2898 400 -370 228 C ATOM 271 O GLY A 39 -3.319 -3.426 7.842 1.00 22.25 O ANISOU 271 O GLY A 39 3075 2386 2992 400 -300 217 O ATOM 272 N GLY A 40 -4.271 -1.545 7.038 1.00 19.20 N ANISOU 272 N GLY A 40 2093 2418 2781 -49 -723 141 N ATOM 273 CA GLY A 40 -4.729 -2.152 5.798 1.00 17.70 C ANISOU 273 CA GLY A 40 1916 2404 2403 -744 -599 477 C ATOM 274 C GLY A 40 -5.680 -3.309 6.040 1.00 20.04 C ANISOU 274 C GLY A 40 2767 2355 2489 -737 -428 474 C ATOM 275 O GLY A 40 -5.673 -4.299 5.296 1.00 20.31 O ANISOU 275 O GLY A 40 2849 2496 2372 -675 -241 533 O ATOM 276 N THR A 41 -6.513 -3.186 7.073 1.00 20.14 N ANISOU 276 N THR A 41 2687 2408 2554 -639 -341 609 N ATOM 277 CA THR A 41 -7.363 -4.306 7.489 1.00 20.11 C ANISOU 277 CA THR A 41 2675 2536 2430 -532 -235 516 C ATOM 278 C THR A 41 -8.417 -4.700 6.459 1.00 21.06 C ANISOU 278 C THR A 41 2840 2801 2361 -121 -342 251 C ATOM 279 O THR A 41 -8.847 -5.843 6.432 1.00 22.02 O ANISOU 279 O THR A 41 3394 2663 2310 83 -333 261 O ATOM 280 CB THR A 41 -8.037 -4.079 8.870 1.00 19.89 C ANISOU 280 CB THR A 41 2652 2405 2497 -422 -324 295 C ATOM 281 OG1 THR A 41 -8.774 -2.851 8.853 1.00 22.77 O ANISOU 281 OG1 THR A 41 3198 2616 2837 -106 -159 -328 O ATOM 282 CG2 THR A 41 -6.996 -4.046 9.979 1.00 21.06 C ANISOU 282 CG2 THR A 41 2692 2814 2494 -1344 -156 317 C ATOM 283 N GLY A 42 -8.829 -3.771 5.601 1.00 19.02 N ANISOU 283 N GLY A 42 2257 2714 2254 -311 -617 214 N ATOM 284 CA GLY A 42 -9.783 -4.126 4.564 1.00 18.41 C ANISOU 284 CA GLY A 42 2284 2529 2179 106 -809 371 C ATOM 285 C GLY A 42 -9.297 -5.265 3.679 1.00 17.66 C ANISOU 285 C GLY A 42 2263 2263 2184 -514 -495 403 C ATOM 286 O GLY A 42 -9.928 -6.331 3.599 1.00 17.28 O ANISOU 286 O GLY A 42 2189 1998 2379 -456 -336 401 O ATOM 287 N ASN A 43 -8.155 -5.059 3.025 1.00 18.38 N ANISOU 287 N ASN A 43 2756 2292 1934 -133 -251 612 N ATOM 288 CA ASN A 43 -7.627 -6.061 2.097 1.00 19.86 C ANISOU 288 CA ASN A 43 2883 2713 1949 -542 -374 672 C ATOM 289 C ASN A 43 -7.086 -7.320 2.764 1.00 17.80 C ANISOU 289 C ASN A 43 2553 2460 1750 -674 -497 559 C ATOM 290 O ASN A 43 -7.228 -8.417 2.231 1.00 19.14 O ANISOU 290 O ASN A 43 3181 2421 1669 -589 -304 230 O ATOM 291 CB ASN A 43 -6.594 -5.450 1.150 1.00 23.98 C ANISOU 291 CB ASN A 43 3740 3001 2368 -604 -160 1163 C ATOM 292 CG ASN A 43 -7.236 -4.561 0.099 1.00 28.81 C ANISOU 292 CG ASN A 43 4429 3850 2665 -665 -210 1387 C ATOM 293 OD1 ASN A 43 -8.316 -4.871 -0.412 1.00 31.46 O ANISOU 293 OD1 ASN A 43 5000 4081 2870 -937 -269 1764 O ATOM 294 ND2 ASN A 43 -6.584 -3.451 -0.225 1.00 30.54 N ANISOU 294 ND2 ASN A 43 4741 4041 2821 -627 -16 1355 N ATOM 295 N LEU A 44 -6.473 -7.173 3.930 1.00 16.91 N ANISOU 295 N LEU A 44 2528 2322 1573 -635 -478 608 N ATOM 296 CA LEU A 44 -6.018 -8.352 4.667 1.00 13.75 C ANISOU 296 CA LEU A 44 2070 1851 1302 -304 -706 809 C ATOM 297 C LEU A 44 -7.201 -9.203 5.122 1.00 11.47 C ANISOU 297 C LEU A 44 1702 1293 1363 -238 -467 522 C ATOM 298 O LEU A 44 -7.143 -10.436 5.106 1.00 13.33 O ANISOU 298 O LEU A 44 1917 1375 1772 -214 -442 412 O ATOM 299 CB LEU A 44 -5.163 -7.952 5.874 1.00 13.99 C ANISOU 299 CB LEU A 44 2498 1783 1033 -460 -882 713 C ATOM 300 CG LEU A 44 -4.640 -9.093 6.746 1.00 15.58 C ANISOU 300 CG LEU A 44 2439 2159 1319 -343 -902 615 C ATOM 301 CD1 LEU A 44 -3.881 -10.114 5.905 1.00 18.06 C ANISOU 301 CD1 LEU A 44 3091 2168 1602 -219 -469 786 C ATOM 302 CD2 LEU A 44 -3.750 -8.538 7.845 1.00 17.45 C ANISOU 302 CD2 LEU A 44 2820 2393 1415 -730 -1044 370 C ATOM 303 N THR A 45 -8.275 -8.539 5.534 1.00 12.42 N ANISOU 303 N THR A 45 1525 1674 1518 -164 -379 576 N ATOM 304 CA THR A 45 -9.465 -9.242 5.995 1.00 12.37 C ANISOU 304 CA THR A 45 1381 1663 1653 -240 -520 154 C ATOM 305 C THR A 45 -10.017 -10.106 4.868 1.00 14.30 C ANISOU 305 C THR A 45 1811 1803 1818 -180 -477 89 C ATOM 306 O THR A 45 -10.374 -11.252 5.090 1.00 14.12 O ANISOU 306 O THR A 45 1853 1623 1886 -244 -334 -122 O ATOM 307 CB THR A 45 -10.551 -8.258 6.493 1.00 13.90 C ANISOU 307 CB THR A 45 1614 2099 1567 -176 -503 99 C ATOM 308 OG1 THR A 45 -10.074 -7.575 7.659 1.00 16.38 O ANISOU 308 OG1 THR A 45 2180 2409 1635 303 -729 -201 O ATOM 309 CG2 THR A 45 -11.835 -8.992 6.840 1.00 16.54 C ANISOU 309 CG2 THR A 45 2079 2416 1789 89 -232 491 C ATOM 310 N LYS A 46 -10.066 -9.566 3.655 1.00 15.36 N ANISOU 310 N LYS A 46 2261 1552 2023 -345 -1034 21 N ATOM 311 CA LYS A 46 -10.576 -10.332 2.527 1.00 16.47 C ANISOU 311 CA LYS A 46 2676 1519 2062 -289 -1073 130 C ATOM 312 C LYS A 46 -9.709 -11.559 2.253 1.00 16.47 C ANISOU 312 C LYS A 46 2579 1790 1889 -274 -889 -3 C ATOM 313 O LYS A 46 -10.223 -12.625 1.917 1.00 19.17 O ANISOU 313 O LYS A 46 3200 1734 2350 -281 -915 -377 O ATOM 314 CB LYS A 46 -10.712 -9.455 1.276 1.00 19.61 C ANISOU 314 CB LYS A 46 3449 1950 2052 -2 -1303 361 C ATOM 315 CG LYS A 46 -11.754 -8.350 1.413 1.00 24.45 C ANISOU 315 CG LYS A 46 4277 2510 2503 -262 -1269 744 C ATOM 316 CD LYS A 46 -11.702 -7.369 0.243 1.00 28.25 C ANISOU 316 CD LYS A 46 4673 3394 2665 346 -1505 832 C ATOM 317 CE LYS A 46 -12.110 -8.020 -1.069 1.00 32.68 C ANISOU 317 CE LYS A 46 5265 3974 3176 47 -1037 770 C ATOM 318 NZ LYS A 46 -12.179 -7.023 -2.176 1.00 34.61 N ANISOU 318 NZ LYS A 46 5642 4002 3505 -93 -710 624 N ATOM 319 N VAL A 47 -8.399 -11.423 2.418 1.00 14.46 N ANISOU 319 N VAL A 47 2362 1792 1340 -156 -512 231 N ATOM 320 CA VAL A 47 -7.514 -12.568 2.220 1.00 16.37 C ANISOU 320 CA VAL A 47 2533 2165 1519 22 -683 417 C ATOM 321 C VAL A 47 -7.723 -13.630 3.308 1.00 15.34 C ANISOU 321 C VAL A 47 2149 2116 1563 -184 -441 261 C ATOM 322 O VAL A 47 -7.821 -14.824 3.008 1.00 15.32 O ANISOU 322 O VAL A 47 2360 1981 1478 -351 -336 50 O ATOM 323 CB VAL A 47 -6.030 -12.145 2.162 1.00 17.60 C ANISOU 323 CB VAL A 47 2787 2069 1830 -174 -266 617 C ATOM 324 CG1 VAL A 47 -5.116 -13.364 2.224 1.00 20.80 C ANISOU 324 CG1 VAL A 47 3101 2798 2004 -504 -124 721 C ATOM 325 CG2 VAL A 47 -5.771 -11.356 0.901 1.00 18.23 C ANISOU 325 CG2 VAL A 47 2979 2232 1713 601 -463 566 C ATOM 326 N LEU A 48 -7.814 -13.193 4.561 1.00 14.74 N ANISOU 326 N LEU A 48 2048 1982 1569 -596 -144 186 N ATOM 327 CA LEU A 48 -8.000 -14.125 5.674 1.00 13.17 C ANISOU 327 CA LEU A 48 2198 1489 1315 -613 -479 -133 C ATOM 328 C LEU A 48 -9.291 -14.922 5.561 1.00 14.18 C ANISOU 328 C LEU A 48 2295 1578 1512 -492 -478 -278 C ATOM 329 O LEU A 48 -9.323 -16.104 5.909 1.00 14.41 O ANISOU 329 O LEU A 48 2127 1598 1750 -336 -665 -235 O ATOM 330 CB LEU A 48 -7.954 -13.393 7.022 1.00 12.37 C ANISOU 330 CB LEU A 48 2043 1495 1159 -412 -675 -299 C ATOM 331 CG LEU A 48 -6.602 -12.781 7.372 1.00 11.80 C ANISOU 331 CG LEU A 48 2013 1131 1337 -4 -521 -225 C ATOM 332 CD1 LEU A 48 -6.760 -11.856 8.558 1.00 12.60 C ANISOU 332 CD1 LEU A 48 1868 1704 1215 95 -181 -1 C ATOM 333 CD2 LEU A 48 -5.599 -13.877 7.665 1.00 14.27 C ANISOU 333 CD2 LEU A 48 2221 1500 1698 171 -64 -492 C ATOM 334 N LEU A 49 -10.347 -14.282 5.064 1.00 13.07 N ANISOU 334 N LEU A 49 2061 1469 1433 -488 -620 -16 N ATOM 335 CA LEU A 49 -11.648 -14.931 4.960 1.00 15.65 C ANISOU 335 CA LEU A 49 2591 1800 1554 -175 -431 -345 C ATOM 336 C LEU A 49 -11.696 -15.985 3.855 1.00 15.26 C ANISOU 336 C LEU A 49 2303 1845 1648 -82 -854 -460 C ATOM 337 O LEU A 49 -12.661 -16.730 3.758 1.00 17.47 O ANISOU 337 O LEU A 49 2729 1927 1980 -535 -736 -367 O ATOM 338 CB LEU A 49 -12.764 -13.901 4.774 1.00 15.10 C ANISOU 338 CB LEU A 49 2271 1780 1686 -518 -329 -330 C ATOM 339 CG LEU A 49 -13.036 -13.050 6.016 1.00 13.77 C ANISOU 339 CG LEU A 49 1984 1476 1772 -279 -115 -138 C ATOM 340 CD1 LEU A 49 -13.976 -11.913 5.681 1.00 16.27 C ANISOU 340 CD1 LEU A 49 2092 1994 2094 -167 -600 5 C ATOM 341 CD2 LEU A 49 -13.592 -13.893 7.168 1.00 15.92 C ANISOU 341 CD2 LEU A 49 2640 1961 1445 -362 -535 -152 C ATOM 342 N GLN A 50 -10.645 -16.060 3.043 1.00 15.16 N ANISOU 342 N GLN A 50 2431 1899 1427 -188 -436 -500 N ATOM 343 CA GLN A 50 -10.518 -17.150 2.072 1.00 16.29 C ANISOU 343 CA GLN A 50 2677 2043 1468 -113 -482 -264 C ATOM 344 C GLN A 50 -10.034 -18.450 2.722 1.00 17.69 C ANISOU 344 C GLN A 50 3170 2003 1546 -283 -316 -267 C ATOM 345 O GLN A 50 -9.934 -19.483 2.065 1.00 21.56 O ANISOU 345 O GLN A 50 4505 2292 1393 -28 -342 -518 O ATOM 346 CB GLN A 50 -9.582 -16.749 0.935 1.00 16.46 C ANISOU 346 CB GLN A 50 2587 2068 1598 -172 -534 -419 C ATOM 347 CG GLN A 50 -10.106 -15.579 0.131 1.00 19.44 C ANISOU 347 CG GLN A 50 3012 2433 1941 172 -587 -199 C ATOM 348 CD GLN A 50 -9.163 -15.143 -0.964 1.00 23.64 C ANISOU 348 CD GLN A 50 3621 2983 2377 -43 -324 -528 C ATOM 349 OE1 GLN A 50 -8.599 -15.968 -1.683 1.00 25.75 O ANISOU 349 OE1 GLN A 50 3876 3072 2835 -478 279 -472 O ATOM 350 NE2 GLN A 50 -9.003 -13.839 -1.114 1.00 26.13 N ANISOU 350 NE2 GLN A 50 4073 3415 2437 -651 -673 -711 N ATOM 351 N HIS A 51 -9.737 -18.391 4.014 1.00 16.21 N ANISOU 351 N HIS A 51 2543 1984 1632 -414 -380 -29 N ATOM 352 CA HIS A 51 -9.270 -19.559 4.762 1.00 14.94 C ANISOU 352 CA HIS A 51 2104 1616 1957 -566 -600 -191 C ATOM 353 C HIS A 51 -10.351 -20.094 5.702 1.00 15.16 C ANISOU 353 C HIS A 51 2126 1704 1930 -329 -553 -14 C ATOM 354 O HIS A 51 -11.273 -19.368 6.069 1.00 16.27 O ANISOU 354 O HIS A 51 2276 2155 1751 -329 -411 -81 O ATOM 355 CB HIS A 51 -8.008 -19.194 5.537 1.00 16.60 C ANISOU 355 CB HIS A 51 2145 1991 2168 -51 -425 -44 C ATOM 356 CG HIS A 51 -6.845 -18.868 4.655 1.00 15.98 C ANISOU 356 CG HIS A 51 2135 1745 2191 -246 -27 31 C ATOM 357 ND1 HIS A 51 -5.813 -19.755 4.435 1.00 19.97 N ANISOU 357 ND1 HIS A 51 2770 2185 2633 -241 -58 271 N ATOM 358 CD2 HIS A 51 -6.570 -17.770 3.912 1.00 17.41 C ANISOU 358 CD2 HIS A 51 2068 2135 2410 -707 -210 254 C ATOM 359 CE1 HIS A 51 -4.941 -19.207 3.601 1.00 20.43 C ANISOU 359 CE1 HIS A 51 2936 2066 2758 -453 -42 550 C ATOM 360 NE2 HIS A 51 -5.377 -18.009 3.269 1.00 20.47 N ANISOU 360 NE2 HIS A 51 2954 2113 2709 -586 -339 259 N ATOM 361 N PRO A 52 -10.232 -21.369 6.106 1.00 17.56 N ANISOU 361 N PRO A 52 2648 1690 2331 -115 -96 -466 N ATOM 362 CA PRO A 52 -11.291 -22.059 6.856 1.00 19.37 C ANISOU 362 CA PRO A 52 3289 1665 2403 41 72 -446 C ATOM 363 C PRO A 52 -11.420 -21.676 8.332 1.00 16.53 C ANISOU 363 C PRO A 52 2741 1235 2302 -56 -204 -231 C ATOM 364 O PRO A 52 -11.789 -22.539 9.134 1.00 18.96 O ANISOU 364 O PRO A 52 3241 1364 2596 -384 -464 -169 O ATOM 365 CB PRO A 52 -10.878 -23.537 6.771 1.00 23.27 C ANISOU 365 CB PRO A 52 4811 1562 2468 -274 334 -799 C ATOM 366 CG PRO A 52 -9.771 -23.603 5.793 1.00 23.62 C ANISOU 366 CG PRO A 52 4428 2008 2536 -245 211 -822 C ATOM 367 CD PRO A 52 -9.133 -22.278 5.739 1.00 20.66 C ANISOU 367 CD PRO A 52 3863 1627 2360 -4 -61 -686 C ATOM 368 N LEU A 53 -11.118 -20.433 8.695 1.00 14.42 N ANISOU 368 N LEU A 53 2210 1254 2014 -20 -476 -319 N ATOM 369 CA LEU A 53 -11.276 -19.997 10.080 1.00 13.41 C ANISOU 369 CA LEU A 53 2120 1210 1762 -288 -697 3 C ATOM 370 C LEU A 53 -12.738 -20.066 10.538 1.00 13.67 C ANISOU 370 C LEU A 53 2031 1263 1899 -425 -849 65 C ATOM 371 O LEU A 53 -13.658 -20.017 9.719 1.00 15.10 O ANISOU 371 O LEU A 53 2309 1405 2023 -150 -996 162 O ATOM 372 CB LEU A 53 -10.685 -18.596 10.282 1.00 13.94 C ANISOU 372 CB LEU A 53 2024 1509 1761 -324 -558 10 C ATOM 373 CG LEU A 53 -11.161 -17.472 9.357 1.00 12.67 C ANISOU 373 CG LEU A 53 1725 1427 1662 -241 -338 49 C ATOM 374 CD1 LEU A 53 -12.505 -16.918 9.801 1.00 13.35 C ANISOU 374 CD1 LEU A 53 2068 1375 1627 -227 -243 -89 C ATOM 375 CD2 LEU A 53 -10.125 -16.361 9.337 1.00 13.84 C ANISOU 375 CD2 LEU A 53 1584 1641 2032 -275 -206 375 C ATOM 376 N ALYS A 54 -12.938 -20.185 11.847 0.50 14.40 N ANISOU 376 N ALYS A 54 2150 1268 2051 -615 -404 -20 N ATOM 377 N BLYS A 54 -12.939 -20.187 11.847 0.50 14.48 N ANISOU 377 N BLYS A 54 2128 1279 2094 -458 -336 3 N ATOM 378 CA ALYS A 54 -14.274 -20.230 12.430 0.50 15.04 C ANISOU 378 CA ALYS A 54 2119 1488 2105 -547 -438 -4 C ATOM 379 CA BLYS A 54 -14.277 -20.228 12.426 0.50 15.31 C ANISOU 379 CA BLYS A 54 2164 1448 2205 -173 -240 63 C ATOM 380 C ALYS A 54 -14.766 -18.820 12.726 0.50 14.25 C ANISOU 380 C ALYS A 54 1781 1412 2219 -384 -561 188 C ATOM 381 C BLYS A 54 -14.765 -18.815 12.713 0.50 14.25 C ANISOU 381 C BLYS A 54 1768 1390 2255 -208 -496 233 C ATOM 382 O ALYS A 54 -15.943 -18.500 12.544 0.50 14.66 O ANISOU 382 O ALYS A 54 1670 1510 2390 -127 -690 190 O ATOM 383 O BLYS A 54 -15.937 -18.489 12.514 0.50 14.41 O ANISOU 383 O BLYS A 54 1599 1464 2411 81 -681 261 O ATOM 384 CB ALYS A 54 -14.253 -21.057 13.721 0.50 16.60 C ANISOU 384 CB ALYS A 54 2180 1946 2178 -397 -385 337 C ATOM 385 CB BLYS A 54 -14.268 -21.052 13.720 0.50 17.10 C ANISOU 385 CB BLYS A 54 2338 1773 2383 260 -24 352 C ATOM 386 CG ALYS A 54 -15.414 -20.785 14.666 0.50 20.22 C ANISOU 386 CG ALYS A 54 2788 2616 2277 -708 -504 436 C ATOM 387 CG BLYS A 54 -15.555 -20.970 14.532 0.50 21.45 C ANISOU 387 CG BLYS A 54 3160 2368 2621 63 -101 469 C ATOM 388 CD ALYS A 54 -15.236 -21.516 15.989 0.50 23.49 C ANISOU 388 CD ALYS A 54 3327 3204 2393 -1146 -431 419 C ATOM 389 CD BLYS A 54 -15.497 -21.852 15.774 0.50 24.75 C ANISOU 389 CD BLYS A 54 3546 3044 2812 80 -104 387 C ATOM 390 CE ALYS A 54 -16.434 -21.296 16.902 0.50 25.96 C ANISOU 390 CE ALYS A 54 3836 3632 2395 -1210 -391 588 C ATOM 391 CE BLYS A 54 -14.510 -21.313 16.802 0.50 26.35 C ANISOU 391 CE BLYS A 54 3655 3401 2956 398 -160 363 C ATOM 392 NZ ALYS A 54 -16.258 -21.921 18.240 0.50 27.68 N ANISOU 392 NZ ALYS A 54 4198 3932 2384 -1467 -428 789 N ATOM 393 NZ BLYS A 54 -14.589 -22.057 18.090 0.50 27.33 N ANISOU 393 NZ BLYS A 54 3738 3520 3125 952 -402 286 N ATOM 394 N LYS A 55 -13.845 -17.975 13.171 1.00 13.57 N ANISOU 394 N LYS A 55 1777 1201 2178 -628 -690 125 N ATOM 395 CA LYS A 55 -14.180 -16.637 13.610 1.00 12.12 C ANISOU 395 CA LYS A 55 1576 1005 2022 -703 -422 503 C ATOM 396 C LYS A 55 -12.979 -15.721 13.347 1.00 10.29 C ANISOU 396 C LYS A 55 1009 979 1920 -597 -468 357 C ATOM 397 O LYS A 55 -11.832 -16.097 13.582 1.00 11.22 O ANISOU 397 O LYS A 55 1058 995 2210 -153 -441 72 O ATOM 398 CB LYS A 55 -14.496 -16.681 15.109 1.00 14.07 C ANISOU 398 CB LYS A 55 1797 1299 2247 -581 -228 204 C ATOM 399 CG LYS A 55 -14.869 -15.356 15.742 1.00 16.44 C ANISOU 399 CG LYS A 55 1996 1561 2687 -145 2 140 C ATOM 400 CD LYS A 55 -16.327 -15.031 15.524 1.00 18.17 C ANISOU 400 CD LYS A 55 2402 1532 2968 -2 44 -106 C ATOM 401 CE LYS A 55 -16.703 -13.791 16.305 1.00 20.09 C ANISOU 401 CE LYS A 55 2606 1822 3203 -391 -29 -342 C ATOM 402 NZ LYS A 55 -18.121 -13.430 16.107 1.00 20.73 N ANISOU 402 NZ LYS A 55 2385 2139 3350 40 102 -68 N ATOM 403 N LEU A 56 -13.254 -14.525 12.842 1.00 10.92 N ANISOU 403 N LEU A 56 1508 916 1724 -525 -396 484 N ATOM 404 CA LEU A 56 -12.223 -13.523 12.612 1.00 9.97 C ANISOU 404 CA LEU A 56 1579 568 1639 -201 -400 249 C ATOM 405 C LEU A 56 -12.618 -12.241 13.320 1.00 10.30 C ANISOU 405 C LEU A 56 1237 961 1715 -76 -485 -5 C ATOM 406 O LEU A 56 -13.641 -11.640 12.986 1.00 11.51 O ANISOU 406 O LEU A 56 1247 1259 1867 -5 -546 -63 O ATOM 407 CB LEU A 56 -12.045 -13.246 11.108 1.00 10.45 C ANISOU 407 CB LEU A 56 1218 989 1763 -324 -436 568 C ATOM 408 CG LEU A 56 -11.069 -12.111 10.753 1.00 11.33 C ANISOU 408 CG LEU A 56 1199 1154 1952 -299 -273 569 C ATOM 409 CD1 LEU A 56 -9.667 -12.427 11.248 1.00 12.76 C ANISOU 409 CD1 LEU A 56 857 1766 2224 -214 -218 33 C ATOM 410 CD2 LEU A 56 -11.028 -11.831 9.257 1.00 14.19 C ANISOU 410 CD2 LEU A 56 1550 1745 2097 88 -563 391 C ATOM 411 N TYR A 57 -11.834 -11.850 14.322 1.00 10.79 N ANISOU 411 N TYR A 57 972 1464 1661 -218 -274 78 N ATOM 412 CA TYR A 57 -12.013 -10.567 14.981 1.00 10.75 C ANISOU 412 CA TYR A 57 806 1724 1553 -27 13 147 C ATOM 413 C TYR A 57 -11.055 -9.588 14.333 1.00 9.61 C ANISOU 413 C TYR A 57 630 1314 1706 -2 -142 227 C ATOM 414 O TYR A 57 -9.882 -9.913 14.139 1.00 11.75 O ANISOU 414 O TYR A 57 795 1553 2115 -50 -116 66 O ATOM 415 CB TYR A 57 -11.649 -10.658 16.457 1.00 12.01 C ANISOU 415 CB TYR A 57 1072 1900 1589 0 -88 52 C ATOM 416 CG TYR A 57 -12.595 -11.485 17.284 1.00 11.75 C ANISOU 416 CG TYR A 57 1119 1953 1392 -291 -116 -70 C ATOM 417 CD1 TYR A 57 -13.832 -10.982 17.662 1.00 12.98 C ANISOU 417 CD1 TYR A 57 1045 2406 1478 -397 141 206 C ATOM 418 CD2 TYR A 57 -12.244 -12.764 17.705 1.00 12.91 C ANISOU 418 CD2 TYR A 57 1391 1995 1517 -594 174 238 C ATOM 419 CE1 TYR A 57 -14.695 -11.726 18.437 1.00 15.59 C ANISOU 419 CE1 TYR A 57 1471 2863 1588 -309 375 412 C ATOM 420 CE2 TYR A 57 -13.102 -13.523 18.469 1.00 14.76 C ANISOU 420 CE2 TYR A 57 1723 2457 1425 -631 37 203 C ATOM 421 CZ TYR A 57 -14.328 -12.998 18.835 1.00 15.91 C ANISOU 421 CZ TYR A 57 1790 2597 1658 -355 184 359 C ATOM 422 OH TYR A 57 -15.181 -13.749 19.597 1.00 20.82 O ANISOU 422 OH TYR A 57 2898 2913 2098 -258 87 383 O ATOM 423 N VAL A 58 -11.549 -8.401 14.001 1.00 9.79 N ANISOU 423 N VAL A 58 1181 1122 1415 -239 -10 156 N ATOM 424 CA VAL A 58 -10.685 -7.332 13.546 1.00 9.11 C ANISOU 424 CA VAL A 58 879 1127 1455 323 -256 103 C ATOM 425 C VAL A 58 -10.734 -6.193 14.552 1.00 9.98 C ANISOU 425 C VAL A 58 817 1269 1703 65 98 -63 C ATOM 426 O VAL A 58 -11.804 -5.654 14.835 1.00 12.13 O ANISOU 426 O VAL A 58 882 1664 2061 54 117 -371 O ATOM 427 CB VAL A 58 -11.090 -6.819 12.150 1.00 11.66 C ANISOU 427 CB VAL A 58 1455 1486 1487 139 -262 11 C ATOM 428 CG1 VAL A 58 -10.110 -5.746 11.682 1.00 14.04 C ANISOU 428 CG1 VAL A 58 1482 1782 2068 -328 233 387 C ATOM 429 CG2 VAL A 58 -11.152 -7.964 11.149 1.00 13.43 C ANISOU 429 CG2 VAL A 58 1783 1820 1499 205 -578 -380 C ATOM 430 N AILE A 59 -9.577 -5.827 15.108 0.50 7.98 N ANISOU 430 N AILE A 59 737 776 1516 -37 49 -84 N ATOM 431 N BILE A 59 -9.573 -5.873 15.115 0.50 10.05 N ANISOU 431 N BILE A 59 1033 1116 1667 50 74 -370 N ATOM 432 CA AILE A 59 -9.516 -4.776 16.122 0.50 9.19 C ANISOU 432 CA AILE A 59 1069 839 1584 79 -322 -16 C ATOM 433 CA BILE A 59 -9.453 -4.779 16.054 0.50 12.42 C ANISOU 433 CA BILE A 59 1595 1275 1848 97 -195 -532 C ATOM 434 C AILE A 59 -8.989 -3.472 15.517 0.50 10.55 C ANISOU 434 C AILE A 59 977 1088 1941 -234 3 -70 C ATOM 435 C BILE A 59 -9.068 -3.558 15.246 0.50 12.12 C ANISOU 435 C BILE A 59 1647 1029 1927 -24 169 -438 C ATOM 436 O AILE A 59 -7.793 -3.327 15.261 0.50 12.98 O ANISOU 436 O AILE A 59 890 1662 2380 -63 27 81 O ATOM 437 O BILE A 59 -8.044 -3.559 14.551 0.50 12.16 O ANISOU 437 O BILE A 59 1704 1126 1787 158 277 -348 O ATOM 438 CB AILE A 59 -8.652 -5.185 17.345 0.50 10.31 C ANISOU 438 CB AILE A 59 1282 1099 1535 331 -347 105 C ATOM 439 CB BILE A 59 -8.375 -5.056 17.117 0.50 15.73 C ANISOU 439 CB BILE A 59 1868 1960 2147 19 -415 -740 C ATOM 440 CG1AILE A 59 -9.009 -6.595 17.828 0.50 9.95 C ANISOU 440 CG1AILE A 59 1177 1244 1359 922 -422 205 C ATOM 441 CG1BILE A 59 -8.571 -6.444 17.732 0.50 17.49 C ANISOU 441 CG1BILE A 59 2056 2310 2279 -259 -234 -658 C ATOM 442 CG2AILE A 59 -8.820 -4.181 18.471 0.50 12.36 C ANISOU 442 CG2AILE A 59 1793 1144 1759 -212 -365 171 C ATOM 443 CG2BILE A 59 -8.396 -3.980 18.185 0.50 16.03 C ANISOU 443 CG2BILE A 59 1729 2134 2227 195 -251 -794 C ATOM 444 CD1AILE A 59 -8.143 -7.076 18.983 0.50 9.99 C ANISOU 444 CD1AILE A 59 1784 736 1276 695 -650 157 C ATOM 445 CD1BILE A 59 -9.976 -6.711 18.205 0.50 18.92 C ANISOU 445 CD1BILE A 59 2366 2425 2397 -356 -23 -577 C ATOM 446 N GLU A 60 -9.900 -2.526 15.306 1.00 12.19 N ANISOU 446 N GLU A 60 1684 951 1994 -42 86 -360 N ATOM 447 CA GLU A 60 -9.652 -1.348 14.490 1.00 14.81 C ANISOU 447 CA GLU A 60 2385 1069 2170 -93 194 -61 C ATOM 448 C GLU A 60 -10.237 -0.094 15.134 1.00 13.82 C ANISOU 448 C GLU A 60 1861 1126 2263 44 428 159 C ATOM 449 O GLU A 60 -11.417 -0.066 15.464 1.00 14.53 O ANISOU 449 O GLU A 60 1692 1490 2337 -3 658 -28 O ATOM 450 CB GLU A 60 -10.292 -1.574 13.115 1.00 18.26 C ANISOU 450 CB GLU A 60 3099 1664 2174 431 262 172 C ATOM 451 CG GLU A 60 -10.340 -0.352 12.230 1.00 24.25 C ANISOU 451 CG GLU A 60 3636 2822 2756 733 599 320 C ATOM 452 CD GLU A 60 -8.984 0.012 11.693 1.00 28.06 C ANISOU 452 CD GLU A 60 3824 3641 3194 1380 1266 287 C ATOM 453 OE1 GLU A 60 -8.338 -0.860 11.077 1.00 30.86 O ANISOU 453 OE1 GLU A 60 4308 3974 3442 1460 1759 89 O ATOM 454 OE2 GLU A 60 -8.562 1.170 11.884 1.00 31.92 O ANISOU 454 OE2 GLU A 60 4040 4448 3637 1368 1385 203 O ATOM 455 N LEU A 61 -9.415 0.940 15.292 1.00 14.02 N ANISOU 455 N LEU A 61 1985 1094 2245 86 -75 99 N ATOM 456 CA LEU A 61 -9.861 2.210 15.869 1.00 13.47 C ANISOU 456 CA LEU A 61 1739 1149 2227 -110 -448 -35 C ATOM 457 C LEU A 61 -10.540 3.138 14.859 1.00 12.38 C ANISOU 457 C LEU A 61 1218 1319 2167 -113 -193 181 C ATOM 458 O LEU A 61 -11.382 3.951 15.233 1.00 13.69 O ANISOU 458 O LEU A 61 1440 1358 2402 292 -124 -107 O ATOM 459 CB LEU A 61 -8.682 2.961 16.505 1.00 15.51 C ANISOU 459 CB LEU A 61 1806 1561 2525 -194 -972 107 C ATOM 460 CG LEU A 61 -8.151 2.429 17.839 1.00 17.70 C ANISOU 460 CG LEU A 61 2017 2109 2596 -340 -863 459 C ATOM 461 CD1 LEU A 61 -6.956 3.250 18.333 1.00 20.05 C ANISOU 461 CD1 LEU A 61 2375 2368 2873 -607 -761 605 C ATOM 462 CD2 LEU A 61 -9.264 2.394 18.891 1.00 20.12 C ANISOU 462 CD2 LEU A 61 2808 2338 2497 26 -780 457 C ATOM 463 N ASP A 62 -10.161 3.037 13.588 1.00 13.34 N ANISOU 463 N ASP A 62 1428 1611 2027 28 -308 173 N ATOM 464 CA ASP A 62 -10.691 3.937 12.549 1.00 12.75 C ANISOU 464 CA ASP A 62 1171 1809 1863 157 -215 352 C ATOM 465 C ASP A 62 -12.162 3.625 12.283 1.00 13.63 C ANISOU 465 C ASP A 62 1338 2053 1788 -152 30 99 C ATOM 466 O ASP A 62 -12.476 2.571 11.736 1.00 14.52 O ANISOU 466 O ASP A 62 1632 1831 2051 -365 139 -240 O ATOM 467 CB ASP A 62 -9.867 3.756 11.265 1.00 16.33 C ANISOU 467 CB ASP A 62 1849 2399 1957 -316 416 602 C ATOM 468 CG ASP A 62 -10.349 4.612 10.099 1.00 20.49 C ANISOU 468 CG ASP A 62 2505 3083 2195 -296 615 564 C ATOM 469 OD1 ASP A 62 -11.496 5.121 10.104 1.00 19.80 O ANISOU 469 OD1 ASP A 62 2339 3052 2130 -441 148 600 O ATOM 470 OD2 ASP A 62 -9.554 4.752 9.141 1.00 24.72 O ANISOU 470 OD2 ASP A 62 3369 3608 2413 243 398 869 O ATOM 471 N ARG A 63 -13.055 4.539 12.652 1.00 12.04 N ANISOU 471 N ARG A 63 1387 1535 1653 -28 -69 252 N ATOM 472 CA ARG A 63 -14.495 4.278 12.589 1.00 12.64 C ANISOU 472 CA ARG A 63 1689 1476 1638 129 11 36 C ATOM 473 C ARG A 63 -15.057 4.263 11.172 1.00 14.68 C ANISOU 473 C ARG A 63 1791 1856 1928 195 -245 128 C ATOM 474 O ARG A 63 -16.076 3.621 10.915 1.00 16.78 O ANISOU 474 O ARG A 63 2190 1986 2198 103 -612 237 O ATOM 475 CB ARG A 63 -15.265 5.250 13.485 1.00 13.49 C ANISOU 475 CB ARG A 63 1835 1454 1836 222 140 428 C ATOM 476 CG ARG A 63 -14.963 4.990 14.950 1.00 14.69 C ANISOU 476 CG ARG A 63 2207 1451 1924 119 369 297 C ATOM 477 CD ARG A 63 -15.736 5.883 15.908 1.00 15.67 C ANISOU 477 CD ARG A 63 2200 1660 2093 -21 225 141 C ATOM 478 NE ARG A 63 -15.327 5.567 17.275 1.00 17.00 N ANISOU 478 NE ARG A 63 1797 2394 2265 -142 378 184 N ATOM 479 CZ ARG A 63 -15.659 6.265 18.353 1.00 18.26 C ANISOU 479 CZ ARG A 63 2062 2237 2638 -396 273 -21 C ATOM 480 NH1 ARG A 63 -16.432 7.339 18.247 1.00 19.06 N ANISOU 480 NH1 ARG A 63 2213 1995 3034 -301 524 32 N ATOM 481 NH2 ARG A 63 -15.214 5.876 19.542 1.00 19.71 N ANISOU 481 NH2 ARG A 63 2533 2394 2559 -662 444 -32 N ATOM 482 N GLU A 64 -14.389 4.949 10.254 1.00 15.71 N ANISOU 482 N GLU A 64 2402 1642 1924 394 -346 332 N ATOM 483 CA GLU A 64 -14.748 4.850 8.845 1.00 17.85 C ANISOU 483 CA GLU A 64 2672 2054 2053 190 -434 396 C ATOM 484 C GLU A 64 -14.407 3.447 8.342 1.00 16.52 C ANISOU 484 C GLU A 64 2455 1721 2099 119 -590 175 C ATOM 485 O GLU A 64 -15.192 2.822 7.616 1.00 18.31 O ANISOU 485 O GLU A 64 2615 2204 2138 5 -714 83 O ATOM 486 CB GLU A 64 -13.998 5.890 8.014 1.00 22.25 C ANISOU 486 CB GLU A 64 3201 2990 2261 -223 -24 475 C ATOM 487 CG GLU A 64 -14.342 5.832 6.535 1.00 29.05 C ANISOU 487 CG GLU A 64 4453 3864 2720 -91 -301 692 C ATOM 488 CD GLU A 64 -13.522 6.805 5.697 1.00 34.91 C ANISOU 488 CD GLU A 64 5477 4644 3140 -209 -653 804 C ATOM 489 OE1 GLU A 64 -12.317 6.973 5.981 1.00 36.17 O ANISOU 489 OE1 GLU A 64 5635 4691 3415 -396 -682 784 O ATOM 490 OE2 GLU A 64 -14.082 7.401 4.753 1.00 38.52 O ANISOU 490 OE2 GLU A 64 6165 5232 3236 -256 -683 668 O ATOM 491 N MET A 65 -13.228 2.958 8.723 1.00 15.27 N ANISOU 491 N MET A 65 2292 1435 2074 158 -197 245 N ATOM 492 CA MET A 65 -12.832 1.600 8.356 1.00 15.50 C ANISOU 492 CA MET A 65 2235 1730 1924 513 -9 50 C ATOM 493 C MET A 65 -13.757 0.557 8.982 1.00 15.18 C ANISOU 493 C MET A 65 1867 1813 2087 198 -63 27 C ATOM 494 O MET A 65 -14.096 -0.436 8.346 1.00 16.50 O ANISOU 494 O MET A 65 1905 2043 2318 -214 -176 -136 O ATOM 495 CB MET A 65 -11.385 1.316 8.755 1.00 15.88 C ANISOU 495 CB MET A 65 1899 2130 2002 764 -145 -152 C ATOM 496 CG MET A 65 -10.913 -0.085 8.365 1.00 22.62 C ANISOU 496 CG MET A 65 2972 3277 2345 446 -289 -742 C ATOM 497 SD MET A 65 -10.798 -0.336 6.580 1.00 31.66 S ANISOU 497 SD MET A 65 4064 4860 3103 185 -225 -622 S ATOM 498 CE MET A 65 -9.385 0.703 6.206 1.00 35.44 C ANISOU 498 CE MET A 65 4984 5137 3343 -171 37 -790 C ATOM 499 N VAL A 66 -14.166 0.784 10.229 1.00 13.53 N ANISOU 499 N VAL A 66 1613 1483 2042 -37 -61 140 N ATOM 500 CA VAL A 66 -15.126 -0.109 10.870 1.00 14.91 C ANISOU 500 CA VAL A 66 1706 1751 2206 -46 -284 70 C ATOM 501 C VAL A 66 -16.395 -0.198 10.022 1.00 16.41 C ANISOU 501 C VAL A 66 2092 1992 2148 -84 -739 -11 C ATOM 502 O VAL A 66 -16.902 -1.294 9.748 1.00 16.75 O ANISOU 502 O VAL A 66 1893 2247 2222 -297 -417 -329 O ATOM 503 CB VAL A 66 -15.455 0.359 12.301 1.00 14.90 C ANISOU 503 CB VAL A 66 1780 1572 2308 -147 -137 169 C ATOM 504 CG1 VAL A 66 -16.645 -0.396 12.877 1.00 17.44 C ANISOU 504 CG1 VAL A 66 2004 2134 2486 -311 -90 20 C ATOM 505 CG2 VAL A 66 -14.234 0.197 13.203 1.00 15.90 C ANISOU 505 CG2 VAL A 66 2243 1424 2371 284 -227 94 C ATOM 506 N GLU A 67 -16.897 0.953 9.590 1.00 18.55 N ANISOU 506 N GLU A 67 1845 2748 2453 208 -835 41 N ATOM 507 CA GLU A 67 -18.098 0.978 8.753 1.00 24.14 C ANISOU 507 CA GLU A 67 2501 3657 3012 261 -1155 59 C ATOM 508 C GLU A 67 -17.908 0.162 7.466 1.00 23.90 C ANISOU 508 C GLU A 67 2397 3593 3091 343 -916 -200 C ATOM 509 O GLU A 67 -18.767 -0.643 7.094 1.00 25.99 O ANISOU 509 O GLU A 67 2431 4188 3256 138 -919 -452 O ATOM 510 CB GLU A 67 -18.488 2.424 8.422 1.00 28.66 C ANISOU 510 CB GLU A 67 2968 4423 3498 289 -1490 107 C ATOM 511 CG GLU A 67 -19.707 2.562 7.529 1.00 37.40 C ANISOU 511 CG GLU A 67 4497 5579 4134 -462 -1204 -156 C ATOM 512 CD GLU A 67 -20.992 2.176 8.236 1.00 47.39 C ANISOU 512 CD GLU A 67 6677 6667 4660 -255 -928 -378 C ATOM 513 OE1 GLU A 67 -21.051 2.311 9.479 1.00 52.02 O ANISOU 513 OE1 GLU A 67 8023 6873 4868 109 -816 -521 O ATOM 514 OE2 GLU A 67 -21.944 1.743 7.547 1.00 49.42 O ANISOU 514 OE2 GLU A 67 6723 7072 4981 -714 -785 -463 O ATOM 515 N ASN A 68 -16.785 0.377 6.788 1.00 21.64 N ANISOU 515 N ASN A 68 2513 3005 2703 528 -764 -40 N ATOM 516 CA ASN A 68 -16.480 -0.356 5.558 1.00 22.81 C ANISOU 516 CA ASN A 68 2976 3089 2601 376 -966 -156 C ATOM 517 C ASN A 68 -16.349 -1.873 5.752 1.00 21.07 C ANISOU 517 C ASN A 68 2683 2858 2464 -301 -902 -529 C ATOM 518 O ASN A 68 -16.829 -2.651 4.935 1.00 24.48 O ANISOU 518 O ASN A 68 3256 3446 2598 -385 -873 -718 O ATOM 519 CB ASN A 68 -15.223 0.210 4.893 1.00 24.35 C ANISOU 519 CB ASN A 68 3296 3171 2785 83 -1309 -45 C ATOM 520 CG ASN A 68 -15.400 1.653 4.439 1.00 31.79 C ANISOU 520 CG ASN A 68 4322 4434 3320 306 -924 66 C ATOM 521 OD1 ASN A 68 -16.520 2.120 4.227 1.00 34.15 O ANISOU 521 OD1 ASN A 68 4639 4843 3493 595 -924 429 O ATOM 522 ND2 ASN A 68 -14.289 2.364 4.284 1.00 35.32 N ANISOU 522 ND2 ASN A 68 5194 4789 3435 80 -688 -81 N ATOM 523 N LEU A 69 -15.691 -2.287 6.830 1.00 19.70 N ANISOU 523 N LEU A 69 2770 2472 2242 -208 -673 -293 N ATOM 524 CA LEU A 69 -15.518 -3.703 7.133 1.00 20.21 C ANISOU 524 CA LEU A 69 2790 2316 2571 -428 -551 -408 C ATOM 525 C LEU A 69 -16.854 -4.368 7.398 1.00 23.68 C ANISOU 525 C LEU A 69 2908 2686 3401 -536 -618 -660 C ATOM 526 O LEU A 69 -17.095 -5.495 6.973 1.00 24.90 O ANISOU 526 O LEU A 69 3311 2613 3535 -798 -881 -675 O ATOM 527 CB LEU A 69 -14.628 -3.881 8.365 1.00 18.66 C ANISOU 527 CB LEU A 69 2495 2142 2452 222 -702 -76 C ATOM 528 CG LEU A 69 -13.142 -3.590 8.198 1.00 18.98 C ANISOU 528 CG LEU A 69 2455 2227 2528 11 -326 -201 C ATOM 529 CD1 LEU A 69 -12.470 -3.436 9.566 1.00 18.23 C ANISOU 529 CD1 LEU A 69 2291 2157 2478 -258 -287 105 C ATOM 530 CD2 LEU A 69 -12.486 -4.705 7.380 1.00 23.89 C ANISOU 530 CD2 LEU A 69 3386 2855 2835 326 280 -230 C ATOM 531 N LYS A 70 -17.717 -3.672 8.128 1.00 26.61 N ANISOU 531 N LYS A 70 2831 3210 4067 -1194 -363 -389 N ATOM 532 CA LYS A 70 -19.016 -4.219 8.480 1.00 31.00 C ANISOU 532 CA LYS A 70 3442 3885 4449 -1005 -543 -80 C ATOM 533 C LYS A 70 -19.840 -4.503 7.234 1.00 31.11 C ANISOU 533 C LYS A 70 3000 4072 4747 -352 -1039 190 C ATOM 534 O LYS A 70 -20.832 -5.230 7.300 1.00 33.52 O ANISOU 534 O LYS A 70 2989 4696 5049 -844 -903 242 O ATOM 535 CB LYS A 70 -19.759 -3.288 9.439 1.00 34.06 C ANISOU 535 CB LYS A 70 4279 4284 4377 -918 -340 -169 C ATOM 536 CG LYS A 70 -19.175 -3.292 10.849 1.00 37.61 C ANISOU 536 CG LYS A 70 5196 4500 4591 -759 -114 -91 C ATOM 537 CD LYS A 70 -19.963 -2.401 11.787 1.00 39.75 C ANISOU 537 CD LYS A 70 5617 4712 4774 -785 61 39 C ATOM 538 CE LYS A 70 -19.476 -2.546 13.221 1.00 41.25 C ANISOU 538 CE LYS A 70 6019 4667 4984 -819 21 353 C ATOM 539 NZ LYS A 70 -19.901 -3.841 13.834 1.00 43.25 N ANISOU 539 NZ LYS A 70 6574 4720 5137 -503 56 355 N ATOM 540 N SER A 71 -19.429 -3.932 6.107 1.00 29.28 N ANISOU 540 N SER A 71 3149 3216 4759 377 -1445 562 N ATOM 541 CA SER A 71 -20.148 -4.111 4.851 1.00 30.19 C ANISOU 541 CA SER A 71 3713 3149 4609 951 -1987 574 C ATOM 542 C SER A 71 -19.855 -5.476 4.237 1.00 28.86 C ANISOU 542 C SER A 71 3601 2984 4378 318 -2245 598 C ATOM 543 O SER A 71 -20.561 -5.926 3.334 1.00 32.56 O ANISOU 543 O SER A 71 4458 3366 4547 352 -2345 639 O ATOM 544 CB SER A 71 -19.785 -3.001 3.863 1.00 33.50 C ANISOU 544 CB SER A 71 4455 3481 4791 106 -1715 491 C ATOM 545 OG SER A 71 -18.606 -3.322 3.145 1.00 36.04 O ANISOU 545 OG SER A 71 5128 3589 4976 250 -1687 164 O ATOM 546 N ILE A 72 -18.809 -6.129 4.732 1.00 20.04 N ANISOU 546 N ILE A 72 2538 2538 2538 0 0 0 N ATOM 547 CA ILE A 72 -18.514 -7.505 4.348 1.00 20.04 C ANISOU 547 CA ILE A 72 2538 2538 2538 0 0 0 C ATOM 548 C ILE A 72 -19.514 -8.476 4.965 1.00 20.04 C ANISOU 548 C ILE A 72 2538 2538 2538 0 0 0 C ATOM 549 O ILE A 72 -19.745 -8.460 6.174 1.00 30.00 O ANISOU 549 O ILE A 72 4634 2634 4131 -31 -964 737 O ATOM 550 CB ILE A 72 -17.089 -7.914 4.767 1.00 20.04 C ANISOU 550 CB ILE A 72 2538 2538 2538 0 0 0 C ATOM 551 CG1 ILE A 72 -16.051 -7.082 4.012 1.00 20.04 C ANISOU 551 CG1 ILE A 72 2538 2538 2538 0 0 0 C ATOM 552 CG2 ILE A 72 -16.868 -9.399 4.523 1.00 20.04 C ANISOU 552 CG2 ILE A 72 2538 2538 2538 0 0 0 C ATOM 553 CD1 ILE A 72 -14.624 -7.361 4.429 1.00 20.04 C ANISOU 553 CD1 ILE A 72 2538 2538 2538 0 0 0 C ATOM 554 N GLY A 73 -20.105 -9.321 4.126 1.00 26.66 N ANISOU 554 N GLY A 73 3296 2599 4233 -265 -1245 964 N ATOM 555 CA GLY A 73 -21.251 -10.116 4.527 1.00 29.48 C ANISOU 555 CA GLY A 73 3855 2950 4393 -37 -1151 1264 C ATOM 556 C GLY A 73 -20.886 -11.204 5.517 1.00 29.44 C ANISOU 556 C GLY A 73 3731 3162 4290 14 -1094 1132 C ATOM 557 O GLY A 73 -21.674 -11.544 6.399 1.00 33.49 O ANISOU 557 O GLY A 73 4079 4004 4642 217 -1316 1207 O ATOM 558 N ASP A 74 -19.684 -11.752 5.369 1.00 24.35 N ANISOU 558 N ASP A 74 2793 2654 3802 -233 -1105 469 N ATOM 559 CA ASP A 74 -19.291 -12.951 6.106 1.00 21.86 C ANISOU 559 CA ASP A 74 2723 2326 3254 -156 -968 449 C ATOM 560 C ASP A 74 -19.718 -13.005 7.584 1.00 18.48 C ANISOU 560 C ASP A 74 1830 2297 2894 -363 -744 291 C ATOM 561 O ASP A 74 -19.358 -12.146 8.385 1.00 18.44 O ANISOU 561 O ASP A 74 1972 2170 2863 -7 -931 156 O ATOM 562 CB ASP A 74 -17.778 -13.118 5.983 1.00 20.02 C ANISOU 562 CB ASP A 74 1970 2343 3294 -299 -792 539 C ATOM 563 CG ASP A 74 -17.340 -14.567 6.022 1.00 20.50 C ANISOU 563 CG ASP A 74 2269 2365 3154 -148 -687 505 C ATOM 564 OD1 ASP A 74 -17.655 -15.264 7.007 1.00 20.24 O ANISOU 564 OD1 ASP A 74 2146 2479 3064 93 -434 697 O ATOM 565 OD2 ASP A 74 -16.660 -15.000 5.066 1.00 21.19 O ANISOU 565 OD2 ASP A 74 2359 2627 3065 138 -596 718 O ATOM 566 N GLU A 75 -20.484 -14.032 7.935 1.00 19.57 N ANISOU 566 N GLU A 75 1680 2886 2868 -61 -1176 173 N ATOM 567 CA GLU A 75 -20.975 -14.208 9.299 1.00 20.76 C ANISOU 567 CA GLU A 75 1606 3155 3124 -442 -825 60 C ATOM 568 C GLU A 75 -19.847 -14.481 10.306 1.00 17.63 C ANISOU 568 C GLU A 75 1334 2587 2776 -220 -694 -100 C ATOM 569 O GLU A 75 -20.054 -14.399 11.522 1.00 19.24 O ANISOU 569 O GLU A 75 1650 2919 2739 -287 -662 89 O ATOM 570 CB GLU A 75 -21.994 -15.352 9.328 1.00 27.72 C ANISOU 570 CB GLU A 75 2285 4491 3754 -1434 -309 100 C ATOM 571 CG GLU A 75 -22.864 -15.414 10.566 1.00 37.22 C ANISOU 571 CG GLU A 75 4383 5196 4562 -1857 -214 126 C ATOM 572 CD GLU A 75 -23.874 -16.555 10.502 1.00 44.09 C ANISOU 572 CD GLU A 75 5774 5919 5058 -1812 -137 -2 C ATOM 573 OE1 GLU A 75 -23.781 -17.382 9.567 1.00 47.37 O ANISOU 573 OE1 GLU A 75 6545 6185 5266 -1640 -382 -77 O ATOM 574 OE2 GLU A 75 -24.756 -16.627 11.386 1.00 46.00 O ANISOU 574 OE2 GLU A 75 6108 6130 5239 -1732 229 168 O ATOM 575 N ARG A 76 -18.653 -14.798 9.806 1.00 14.00 N ANISOU 575 N ARG A 76 921 1957 2441 -264 -578 84 N ATOM 576 CA ARG A 76 -17.519 -15.118 10.686 1.00 14.37 C ANISOU 576 CA ARG A 76 1517 1741 2199 -350 -737 -64 C ATOM 577 C ARG A 76 -16.750 -13.896 11.161 1.00 12.71 C ANISOU 577 C ARG A 76 1256 1627 1943 -233 -730 36 C ATOM 578 O ARG A 76 -15.890 -14.003 12.039 1.00 12.51 O ANISOU 578 O ARG A 76 1052 1740 1960 -231 -595 232 O ATOM 579 CB ARG A 76 -16.548 -16.068 9.986 1.00 13.97 C ANISOU 579 CB ARG A 76 1740 1705 1862 -89 -268 -270 C ATOM 580 CG ARG A 76 -17.168 -17.409 9.600 1.00 14.30 C ANISOU 580 CG ARG A 76 2015 1669 1747 -803 -399 -75 C ATOM 581 CD ARG A 76 -16.207 -18.208 8.727 1.00 14.62 C ANISOU 581 CD ARG A 76 2222 1632 1698 -234 -275 -110 C ATOM 582 NE ARG A 76 -15.917 -17.528 7.467 1.00 15.51 N ANISOU 582 NE ARG A 76 2240 1814 1837 -187 -460 -119 N ATOM 583 CZ ARG A 76 -14.854 -17.764 6.704 1.00 13.48 C ANISOU 583 CZ ARG A 76 1786 1598 1738 -143 -653 -447 C ATOM 584 NH1 ARG A 76 -13.952 -18.671 7.058 1.00 15.24 N ANISOU 584 NH1 ARG A 76 2006 1791 1991 77 -431 -544 N ATOM 585 NH2 ARG A 76 -14.693 -17.085 5.578 1.00 14.84 N ANISOU 585 NH2 ARG A 76 2197 1936 1506 -123 -581 -342 N ATOM 586 N LEU A 77 -17.063 -12.748 10.577 1.00 12.61 N ANISOU 586 N LEU A 77 1216 1701 1874 -270 -498 174 N ATOM 587 CA LEU A 77 -16.338 -11.517 10.836 1.00 13.33 C ANISOU 587 CA LEU A 77 1295 1763 2006 -220 -351 252 C ATOM 588 C LEU A 77 -16.994 -10.704 11.949 1.00 12.59 C ANISOU 588 C LEU A 77 1097 1642 2044 -220 -153 88 C ATOM 589 O LEU A 77 -18.201 -10.451 11.919 1.00 15.23 O ANISOU 589 O LEU A 77 1056 2464 2266 66 -96 71 O ATOM 590 CB LEU A 77 -16.268 -10.684 9.558 1.00 14.49 C ANISOU 590 CB LEU A 77 1474 1821 2209 -611 -524 446 C ATOM 591 CG LEU A 77 -15.636 -9.300 9.669 1.00 14.18 C ANISOU 591 CG LEU A 77 1289 1800 2299 -430 -566 706 C ATOM 592 CD1 LEU A 77 -14.192 -9.385 10.156 1.00 14.61 C ANISOU 592 CD1 LEU A 77 1100 2041 2408 -599 -579 959 C ATOM 593 CD2 LEU A 77 -15.703 -8.615 8.322 1.00 17.63 C ANISOU 593 CD2 LEU A 77 2433 2084 2182 -682 -987 694 C ATOM 594 N GLU A 78 -16.194 -10.302 12.933 1.00 12.17 N ANISOU 594 N GLU A 78 1246 1364 2012 -228 -131 124 N ATOM 595 CA GLU A 78 -16.659 -9.398 13.977 1.00 12.84 C ANISOU 595 CA GLU A 78 1067 1731 2081 -20 -397 175 C ATOM 596 C GLU A 78 -15.641 -8.281 14.194 1.00 11.03 C ANISOU 596 C GLU A 78 708 1324 2157 121 -410 70 C ATOM 597 O GLU A 78 -14.455 -8.545 14.408 1.00 12.25 O ANISOU 597 O GLU A 78 810 1272 2571 -23 -210 -2 O ATOM 598 CB GLU A 78 -16.909 -10.137 15.294 1.00 13.46 C ANISOU 598 CB GLU A 78 1355 1856 1902 -132 -212 -79 C ATOM 599 CG GLU A 78 -17.279 -9.171 16.417 1.00 16.39 C ANISOU 599 CG GLU A 78 2023 1975 2228 -113 -189 -704 C ATOM 600 CD GLU A 78 -17.687 -9.852 17.713 1.00 21.28 C ANISOU 600 CD GLU A 78 2751 2802 2531 -77 -142 -661 C ATOM 601 OE1 GLU A 78 -17.705 -11.101 17.775 1.00 23.06 O ANISOU 601 OE1 GLU A 78 2770 3238 2754 59 -251 -483 O ATOM 602 OE2 GLU A 78 -18.000 -9.126 18.681 1.00 26.53 O ANISOU 602 OE2 GLU A 78 3772 3467 2838 -566 232 -397 O ATOM 603 N VAL A 79 -16.106 -7.036 14.141 1.00 12.33 N ANISOU 603 N VAL A 79 1716 997 1972 -254 141 -203 N ATOM 604 CA VAL A 79 -15.209 -5.895 14.270 1.00 10.89 C ANISOU 604 CA VAL A 79 1389 881 1866 75 264 61 C ATOM 605 C VAL A 79 -15.288 -5.300 15.670 1.00 13.09 C ANISOU 605 C VAL A 79 1237 1659 2077 20 109 -298 C ATOM 606 O VAL A 79 -16.376 -5.067 16.210 1.00 16.62 O ANISOU 606 O VAL A 79 1610 2339 2364 -70 -20 -557 O ATOM 607 CB VAL A 79 -15.523 -4.802 13.221 1.00 13.41 C ANISOU 607 CB VAL A 79 1519 1468 2108 -487 -185 279 C ATOM 608 CG1 VAL A 79 -14.467 -3.691 13.258 1.00 13.99 C ANISOU 608 CG1 VAL A 79 1494 1543 2276 222 -109 417 C ATOM 609 CG2 VAL A 79 -15.615 -5.411 11.841 1.00 16.79 C ANISOU 609 CG2 VAL A 79 1859 2302 2216 -465 -366 190 C ATOM 610 N ILE A 80 -14.125 -5.072 16.262 1.00 12.77 N ANISOU 610 N ILE A 80 1228 1727 1897 -36 53 -81 N ATOM 611 CA ILE A 80 -14.056 -4.506 17.598 1.00 13.05 C ANISOU 611 CA ILE A 80 1860 1159 1939 -64 -78 358 C ATOM 612 C ILE A 80 -13.352 -3.164 17.504 1.00 12.56 C ANISOU 612 C ILE A 80 1599 1156 2017 -365 478 213 C ATOM 613 O ILE A 80 -12.199 -3.083 17.076 1.00 12.67 O ANISOU 613 O ILE A 80 1577 1246 1989 206 468 70 O ATOM 614 CB ILE A 80 -13.290 -5.435 18.547 1.00 17.39 C ANISOU 614 CB ILE A 80 2937 1330 2338 -168 -255 351 C ATOM 615 CG1 ILE A 80 -14.056 -6.745 18.723 1.00 20.24 C ANISOU 615 CG1 ILE A 80 3787 1433 2468 12 -378 199 C ATOM 616 CG2 ILE A 80 -13.074 -4.776 19.898 1.00 18.90 C ANISOU 616 CG2 ILE A 80 3319 1517 2343 -493 -249 -1 C ATOM 617 CD1 ILE A 80 -13.344 -7.733 19.595 1.00 23.36 C ANISOU 617 CD1 ILE A 80 4449 1834 2593 -208 -424 18 C ATOM 618 N ASN A 81 -14.058 -2.112 17.900 1.00 13.14 N ANISOU 618 N ASN A 81 1714 1112 2167 150 129 442 N ATOM 619 CA ASN A 81 -13.556 -0.748 17.761 1.00 11.91 C ANISOU 619 CA ASN A 81 1032 1426 2064 246 47 -15 C ATOM 620 C ASN A 81 -12.775 -0.342 18.999 1.00 12.12 C ANISOU 620 C ASN A 81 758 1800 2045 295 108 -411 C ATOM 621 O ASN A 81 -13.217 0.518 19.770 1.00 15.71 O ANISOU 621 O ASN A 81 1432 2571 1964 557 -21 -669 O ATOM 622 CB ASN A 81 -14.740 0.200 17.537 1.00 13.96 C ANISOU 622 CB ASN A 81 1201 1740 2361 291 40 69 C ATOM 623 CG ASN A 81 -14.323 1.630 17.243 1.00 14.96 C ANISOU 623 CG ASN A 81 1556 1955 2173 447 -35 -189 C ATOM 624 OD1 ASN A 81 -15.019 2.558 17.647 1.00 16.53 O ANISOU 624 OD1 ASN A 81 2194 1964 2123 395 382 -390 O ATOM 625 ND2 ASN A 81 -13.221 1.819 16.517 1.00 14.27 N ANISOU 625 ND2 ASN A 81 1723 1718 1979 272 -234 -385 N ATOM 626 N GLU A 82 -11.621 -0.981 19.192 1.00 13.59 N ANISOU 626 N GLU A 82 1208 1573 2381 48 -53 -267 N ATOM 627 CA GLU A 82 -10.751 -0.681 20.323 1.00 14.59 C ANISOU 627 CA GLU A 82 1321 1698 2524 -293 119 -344 C ATOM 628 C GLU A 82 -9.289 -0.693 19.899 1.00 14.06 C ANISOU 628 C GLU A 82 1271 1598 2473 -195 -245 -474 C ATOM 629 O GLU A 82 -8.980 -0.976 18.736 1.00 14.59 O ANISOU 629 O GLU A 82 1314 1802 2426 160 -11 -405 O ATOM 630 CB GLU A 82 -10.995 -1.664 21.472 1.00 18.41 C ANISOU 630 CB GLU A 82 1410 2856 2727 -398 348 106 C ATOM 631 CG GLU A 82 -12.392 -1.550 22.110 1.00 22.40 C ANISOU 631 CG GLU A 82 1948 3479 3081 -131 767 -195 C ATOM 632 CD GLU A 82 -12.663 -0.186 22.773 1.00 26.63 C ANISOU 632 CD GLU A 82 2307 4214 3596 -310 709 -238 C ATOM 633 OE1 GLU A 82 -11.698 0.553 23.063 1.00 30.23 O ANISOU 633 OE1 GLU A 82 3268 4615 3602 -495 410 -284 O ATOM 634 OE2 GLU A 82 -13.853 0.149 23.011 1.00 28.66 O ANISOU 634 OE2 GLU A 82 2506 4497 3884 -481 1013 -340 O ATOM 635 N ASP A 83 -8.410 -0.379 20.850 1.00 14.17 N ANISOU 635 N ASP A 83 909 1880 2593 18 -262 -70 N ATOM 636 CA ASP A 83 -6.978 -0.218 20.621 1.00 12.99 C ANISOU 636 CA ASP A 83 1241 1164 2531 -79 -240 -375 C ATOM 637 C ASP A 83 -6.239 -1.536 20.846 1.00 12.04 C ANISOU 637 C ASP A 83 1357 1134 2084 253 24 -362 C ATOM 638 O ASP A 83 -6.195 -2.050 21.969 1.00 12.85 O ANISOU 638 O ASP A 83 1703 1326 1851 -11 -140 -51 O ATOM 639 CB ASP A 83 -6.456 0.827 21.614 1.00 15.55 C ANISOU 639 CB ASP A 83 1789 1000 3118 -43 -667 -544 C ATOM 640 CG ASP A 83 -5.062 1.306 21.295 1.00 18.23 C ANISOU 640 CG ASP A 83 1786 1428 3710 169 -583 -840 C ATOM 641 OD1 ASP A 83 -4.302 0.574 20.641 1.00 20.16 O ANISOU 641 OD1 ASP A 83 2176 1573 3909 81 -377 -619 O ATOM 642 OD2 ASP A 83 -4.723 2.434 21.722 1.00 22.86 O ANISOU 642 OD2 ASP A 83 2560 1918 4208 47 -500 -918 O ATOM 643 N ALA A 84 -5.662 -2.087 19.780 1.00 13.39 N ANISOU 643 N ALA A 84 1500 1396 2189 80 -67 -440 N ATOM 644 CA ALA A 84 -4.970 -3.368 19.868 1.00 14.80 C ANISOU 644 CA ALA A 84 1950 1596 2076 387 -590 -366 C ATOM 645 C ALA A 84 -3.720 -3.345 20.745 1.00 14.56 C ANISOU 645 C ALA A 84 1963 1350 2216 360 -498 -217 C ATOM 646 O ALA A 84 -3.212 -4.400 21.120 1.00 17.87 O ANISOU 646 O ALA A 84 2496 1825 2469 537 -702 109 O ATOM 647 CB ALA A 84 -4.625 -3.882 18.474 1.00 16.29 C ANISOU 647 CB ALA A 84 2616 1784 1789 237 -205 -651 C ATOM 648 N SER A 85 -3.215 -2.162 21.074 1.00 13.88 N ANISOU 648 N SER A 85 1391 1747 2135 366 65 -201 N ATOM 649 CA SER A 85 -2.029 -2.089 21.919 1.00 15.88 C ANISOU 649 CA SER A 85 1723 1741 2570 239 -57 -509 C ATOM 650 C SER A 85 -2.408 -2.182 23.396 1.00 15.85 C ANISOU 650 C SER A 85 1413 1992 2616 153 18 -487 C ATOM 651 O SER A 85 -1.537 -2.300 24.264 1.00 17.93 O ANISOU 651 O SER A 85 1838 2197 2775 182 -427 -417 O ATOM 652 CB SER A 85 -1.234 -0.811 21.640 1.00 18.51 C ANISOU 652 CB SER A 85 1961 2204 2868 -238 35 -657 C ATOM 653 OG SER A 85 -1.958 0.336 22.033 1.00 21.11 O ANISOU 653 OG SER A 85 2584 2388 3048 -469 -41 -409 O ATOM 654 N LYS A 86 -3.711 -2.136 23.675 1.00 15.92 N ANISOU 654 N LYS A 86 1535 1929 2584 -22 623 -538 N ATOM 655 CA LYS A 86 -4.210 -2.156 25.049 1.00 15.18 C ANISOU 655 CA LYS A 86 1719 1470 2576 -215 498 -316 C ATOM 656 C LYS A 86 -5.259 -3.230 25.311 1.00 15.16 C ANISOU 656 C LYS A 86 1581 1932 2245 -29 96 -77 C ATOM 657 O LYS A 86 -5.567 -3.536 26.464 1.00 19.44 O ANISOU 657 O LYS A 86 3013 2321 2050 -300 -19 -59 O ATOM 658 CB LYS A 86 -4.799 -0.794 25.407 1.00 18.12 C ANISOU 658 CB LYS A 86 2175 1606 3104 -628 757 -867 C ATOM 659 CG LYS A 86 -3.781 0.328 25.331 1.00 23.60 C ANISOU 659 CG LYS A 86 3322 1904 3739 -875 1062 -1046 C ATOM 660 CD LYS A 86 -4.454 1.671 25.506 1.00 27.90 C ANISOU 660 CD LYS A 86 4480 1970 4149 -642 1323 -1130 C ATOM 661 CE LYS A 86 -3.459 2.805 25.347 1.00 33.77 C ANISOU 661 CE LYS A 86 5275 3031 4525 -558 1028 -1209 C ATOM 662 NZ LYS A 86 -4.142 4.115 25.260 1.00 38.54 N ANISOU 662 NZ LYS A 86 6113 3858 4670 -593 816 -1358 N ATOM 663 N PHE A 87 -5.815 -3.797 24.249 1.00 15.56 N ANISOU 663 N PHE A 87 1746 2110 2056 -193 53 -142 N ATOM 664 CA PHE A 87 -6.968 -4.686 24.388 1.00 15.74 C ANISOU 664 CA PHE A 87 1486 2479 2015 -236 -77 64 C ATOM 665 C PHE A 87 -6.612 -6.050 24.988 1.00 15.63 C ANISOU 665 C PHE A 87 1544 2423 1971 196 277 166 C ATOM 666 O PHE A 87 -5.605 -6.649 24.609 1.00 16.67 O ANISOU 666 O PHE A 87 1212 2847 2272 98 478 -172 O ATOM 667 CB PHE A 87 -7.630 -4.877 23.025 1.00 16.57 C ANISOU 667 CB PHE A 87 1651 2632 2012 -583 -144 180 C ATOM 668 CG PHE A 87 -8.955 -5.567 23.092 1.00 16.19 C ANISOU 668 CG PHE A 87 1629 2445 2075 -764 58 410 C ATOM 669 CD1 PHE A 87 -10.101 -4.859 23.419 1.00 17.12 C ANISOU 669 CD1 PHE A 87 1700 2526 2279 -69 66 221 C ATOM 670 CD2 PHE A 87 -9.059 -6.929 22.838 1.00 15.40 C ANISOU 670 CD2 PHE A 87 1632 2163 2054 -701 -30 447 C ATOM 671 CE1 PHE A 87 -11.328 -5.499 23.496 1.00 17.67 C ANISOU 671 CE1 PHE A 87 1562 2726 2423 81 116 174 C ATOM 672 CE2 PHE A 87 -10.279 -7.570 22.905 1.00 16.96 C ANISOU 672 CE2 PHE A 87 1602 2617 2224 -454 96 299 C ATOM 673 CZ PHE A 87 -11.420 -6.855 23.238 1.00 18.11 C ANISOU 673 CZ PHE A 87 1694 2809 2378 -94 -34 109 C ATOM 674 N PRO A 88 -7.443 -6.560 25.915 1.00 14.42 N ANISOU 674 N PRO A 88 1314 2138 2027 460 147 -83 N ATOM 675 CA PRO A 88 -7.168 -7.906 26.446 1.00 15.58 C ANISOU 675 CA PRO A 88 1483 2347 2087 279 -41 -212 C ATOM 676 C PRO A 88 -7.623 -8.997 25.483 1.00 14.43 C ANISOU 676 C PRO A 88 988 2283 2212 -12 -211 -327 C ATOM 677 O PRO A 88 -8.793 -9.410 25.502 1.00 15.24 O ANISOU 677 O PRO A 88 1084 2388 2317 224 -224 -270 O ATOM 678 CB PRO A 88 -8.012 -7.987 27.722 1.00 17.73 C ANISOU 678 CB PRO A 88 2020 2700 2017 344 336 -25 C ATOM 679 CG PRO A 88 -8.890 -6.808 27.730 1.00 18.45 C ANISOU 679 CG PRO A 88 2077 2817 2115 1150 517 -147 C ATOM 680 CD PRO A 88 -8.615 -5.931 26.544 1.00 16.72 C ANISOU 680 CD PRO A 88 1861 2609 1882 741 488 -54 C ATOM 681 N PHE A 89 -6.705 -9.453 24.645 1.00 14.92 N ANISOU 681 N PHE A 89 1513 1917 2239 269 -46 -370 N ATOM 682 CA PHE A 89 -7.041 -10.461 23.654 1.00 14.99 C ANISOU 682 CA PHE A 89 1458 2043 2195 7 35 -145 C ATOM 683 C PHE A 89 -7.733 -11.670 24.275 1.00 14.33 C ANISOU 683 C PHE A 89 1193 2008 2241 210 138 57 C ATOM 684 O PHE A 89 -8.619 -12.260 23.665 1.00 14.29 O ANISOU 684 O PHE A 89 980 2247 2203 -52 149 -179 O ATOM 685 CB PHE A 89 -5.796 -10.931 22.902 1.00 13.92 C ANISOU 685 CB PHE A 89 771 2198 2317 336 489 26 C ATOM 686 CG PHE A 89 -5.104 -9.856 22.102 1.00 17.41 C ANISOU 686 CG PHE A 89 1563 2631 2419 204 361 160 C ATOM 687 CD1 PHE A 89 -5.821 -8.902 21.408 1.00 20.21 C ANISOU 687 CD1 PHE A 89 1936 3173 2568 73 521 385 C ATOM 688 CD2 PHE A 89 -3.724 -9.841 22.011 1.00 18.30 C ANISOU 688 CD2 PHE A 89 1595 2901 2457 -60 75 404 C ATOM 689 CE1 PHE A 89 -5.174 -7.929 20.659 1.00 18.75 C ANISOU 689 CE1 PHE A 89 1423 3075 2626 579 258 639 C ATOM 690 CE2 PHE A 89 -3.066 -8.874 21.254 1.00 18.41 C ANISOU 690 CE2 PHE A 89 1632 3137 2224 201 -244 800 C ATOM 691 CZ PHE A 89 -3.792 -7.915 20.582 1.00 18.85 C ANISOU 691 CZ PHE A 89 1790 2966 2404 655 -64 481 C ATOM 692 N ACYS A 90 -7.335 -12.053 25.480 0.50 15.22 N ANISOU 692 N ACYS A 90 1342 1941 2497 264 -184 10 N ATOM 693 N BCYS A 90 -7.314 -12.031 25.487 0.50 17.03 N ANISOU 693 N BCYS A 90 1663 2312 2494 246 -160 -10 N ATOM 694 CA ACYS A 90 -7.884 -13.274 26.062 0.50 15.27 C ANISOU 694 CA ACYS A 90 1319 1910 2571 719 -383 135 C ATOM 695 CA BCYS A 90 -7.853 -13.203 26.176 0.50 19.35 C ANISOU 695 CA BCYS A 90 2072 2717 2560 609 -370 20 C ATOM 696 C ACYS A 90 -9.352 -13.164 26.493 0.50 16.86 C ANISOU 696 C ACYS A 90 1963 1974 2468 617 -154 31 C ATOM 697 C BCYS A 90 -9.376 -13.185 26.268 0.50 17.19 C ANISOU 697 C BCYS A 90 1812 2531 2186 597 -97 -49 C ATOM 698 O ACYS A 90 -9.932 -14.135 26.975 0.50 18.46 O ANISOU 698 O ACYS A 90 2573 1816 2625 176 -324 11 O ATOM 699 O BCYS A 90 -10.016 -14.234 26.287 0.50 15.42 O ANISOU 699 O BCYS A 90 1274 2724 1860 190 -200 21 O ATOM 700 CB ACYS A 90 -6.996 -13.786 27.197 0.50 15.11 C ANISOU 700 CB ACYS A 90 1127 1932 2679 324 -667 247 C ATOM 701 CB BCYS A 90 -7.241 -13.351 27.578 0.50 23.93 C ANISOU 701 CB BCYS A 90 2940 3187 2963 437 -729 29 C ATOM 702 SG ACYS A 90 -5.333 -14.256 26.633 0.50 15.45 S ANISOU 702 SG ACYS A 90 1055 2132 2682 94 -137 23 S ATOM 703 SG BCYS A 90 -7.617 -12.022 28.762 0.50 28.78 S ANISOU 703 SG BCYS A 90 3948 3678 3306 61 -1008 101 S ATOM 704 N SER A 91 -9.951 -11.989 26.314 1.00 15.95 N ANISOU 704 N SER A 91 1503 2222 2333 680 25 -137 N ATOM 705 CA SER A 91 -11.396 -11.849 26.483 1.00 14.68 C ANISOU 705 CA SER A 91 1176 2043 2357 233 122 -119 C ATOM 706 C SER A 91 -12.166 -12.330 25.254 1.00 15.66 C ANISOU 706 C SER A 91 1371 1816 2761 510 139 -26 C ATOM 707 O SER A 91 -13.394 -12.448 25.295 1.00 17.51 O ANISOU 707 O SER A 91 1427 2004 3221 9 628 -149 O ATOM 708 CB SER A 91 -11.784 -10.407 26.834 1.00 14.89 C ANISOU 708 CB SER A 91 1786 1533 2336 116 369 -81 C ATOM 709 OG SER A 91 -11.621 -9.526 25.732 1.00 15.05 O ANISOU 709 OG SER A 91 1566 1569 2581 148 193 -18 O ATOM 710 N LEU A 92 -11.436 -12.618 24.174 1.00 14.13 N ANISOU 710 N LEU A 92 1312 1591 2464 268 -34 174 N ATOM 711 CA LEU A 92 -12.044 -13.054 22.913 1.00 14.97 C ANISOU 711 CA LEU A 92 1255 1761 2669 -269 -308 184 C ATOM 712 C LEU A 92 -12.130 -14.560 22.776 1.00 18.78 C ANISOU 712 C LEU A 92 1913 2205 3015 -440 -426 175 C ATOM 713 O LEU A 92 -12.948 -15.077 22.009 1.00 24.07 O ANISOU 713 O LEU A 92 3123 2591 3431 -753 -1269 114 O ATOM 714 CB LEU A 92 -11.243 -12.512 21.724 1.00 15.23 C ANISOU 714 CB LEU A 92 1246 2033 2506 149 8 186 C ATOM 715 CG LEU A 92 -11.155 -10.992 21.625 1.00 15.23 C ANISOU 715 CG LEU A 92 1415 2049 2320 303 -1 36 C ATOM 716 CD1 LEU A 92 -10.270 -10.579 20.464 1.00 16.90 C ANISOU 716 CD1 LEU A 92 1917 2263 2241 -48 107 -283 C ATOM 717 CD2 LEU A 92 -12.560 -10.397 21.486 1.00 16.78 C ANISOU 717 CD2 LEU A 92 1406 2681 2287 674 -179 201 C ATOM 718 N GLY A 93 -11.274 -15.268 23.499 1.00 15.28 N ANISOU 718 N GLY A 93 1373 1531 2902 53 166 320 N ATOM 719 CA GLY A 93 -11.203 -16.709 23.362 1.00 16.91 C ANISOU 719 CA GLY A 93 2038 1488 2898 258 12 322 C ATOM 720 C GLY A 93 -9.962 -17.289 23.998 1.00 18.01 C ANISOU 720 C GLY A 93 1753 2200 2889 148 148 546 C ATOM 721 O GLY A 93 -9.037 -16.562 24.354 1.00 17.25 O ANISOU 721 O GLY A 93 1851 1945 2755 256 12 407 O ATOM 722 N LYS A 94 -9.943 -18.610 24.129 1.00 21.98 N ANISOU 722 N LYS A 94 2371 2707 3273 497 189 449 N ATOM 723 CA LYS A 94 -8.880 -19.302 24.844 1.00 23.75 C ANISOU 723 CA LYS A 94 2928 2881 3214 253 238 904 C ATOM 724 C LYS A 94 -7.696 -19.623 23.949 1.00 19.95 C ANISOU 724 C LYS A 94 2014 2601 2963 108 -1 659 C ATOM 725 O LYS A 94 -6.604 -19.899 24.440 1.00 19.65 O ANISOU 725 O LYS A 94 1951 2496 3017 418 -366 699 O ATOM 726 CB LYS A 94 -9.414 -20.602 25.453 1.00 29.35 C ANISOU 726 CB LYS A 94 4225 3359 3567 319 732 1209 C ATOM 727 CG LYS A 94 -10.534 -20.404 26.460 1.00 36.38 C ANISOU 727 CG LYS A 94 5573 4313 3936 706 712 825 C ATOM 728 CD LYS A 94 -9.994 -19.978 27.812 1.00 42.27 C ANISOU 728 CD LYS A 94 6690 5081 4288 812 295 715 C ATOM 729 CE LYS A 94 -9.234 -21.110 28.481 1.00 46.37 C ANISOU 729 CE LYS A 94 7452 5664 4500 680 34 612 C ATOM 730 NZ LYS A 94 -8.883 -20.780 29.895 1.00 48.65 N ANISOU 730 NZ LYS A 94 7822 5951 4712 545 -190 527 N ATOM 731 N GLU A 95 -7.918 -19.601 22.638 1.00 18.98 N ANISOU 731 N GLU A 95 2339 2035 2837 -294 326 186 N ATOM 732 CA GLU A 95 -6.875 -19.948 21.685 1.00 18.00 C ANISOU 732 CA GLU A 95 2485 1700 2653 -443 -42 201 C ATOM 733 C GLU A 95 -7.022 -19.094 20.427 1.00 16.55 C ANISOU 733 C GLU A 95 2242 1988 2057 -392 -580 48 C ATOM 734 O GLU A 95 -7.945 -19.285 19.624 1.00 19.59 O ANISOU 734 O GLU A 95 2416 2262 2765 -262 -828 78 O ATOM 735 CB GLU A 95 -6.941 -21.439 21.336 1.00 22.03 C ANISOU 735 CB GLU A 95 2699 2371 3299 557 -348 261 C ATOM 736 CG GLU A 95 -5.784 -21.917 20.470 1.00 27.56 C ANISOU 736 CG GLU A 95 3322 3147 4000 1259 -237 410 C ATOM 737 CD GLU A 95 -5.743 -23.426 20.319 1.00 39.57 C ANISOU 737 CD GLU A 95 5493 4739 4802 635 427 195 C ATOM 738 OE1 GLU A 95 -6.769 -24.084 20.601 1.00 43.86 O ANISOU 738 OE1 GLU A 95 6331 5186 5148 274 718 172 O ATOM 739 OE2 GLU A 95 -4.682 -23.959 19.919 1.00 43.80 O ANISOU 739 OE2 GLU A 95 6428 5132 5079 511 513 150 O ATOM 740 N LEU A 96 -6.098 -18.156 20.265 1.00 11.99 N ANISOU 740 N LEU A 96 1548 1755 1253 44 -294 -92 N ATOM 741 CA LEU A 96 -6.203 -17.135 19.239 1.00 10.90 C ANISOU 741 CA LEU A 96 994 1959 1186 502 26 -314 C ATOM 742 C LEU A 96 -4.940 -17.067 18.407 1.00 10.33 C ANISOU 742 C LEU A 96 944 1760 1221 175 -472 -9 C ATOM 743 O LEU A 96 -3.830 -17.133 18.942 1.00 14.89 O ANISOU 743 O LEU A 96 1290 2891 1475 72 -536 115 O ATOM 744 CB LEU A 96 -6.421 -15.768 19.893 1.00 13.56 C ANISOU 744 CB LEU A 96 1765 2052 1335 378 163 -635 C ATOM 745 CG LEU A 96 -7.528 -15.655 20.944 1.00 15.25 C ANISOU 745 CG LEU A 96 2060 2168 1566 283 23 -719 C ATOM 746 CD1 LEU A 96 -7.426 -14.321 21.647 1.00 16.91 C ANISOU 746 CD1 LEU A 96 2523 2372 1527 161 78 -966 C ATOM 747 CD2 LEU A 96 -8.886 -15.819 20.295 1.00 14.48 C ANISOU 747 CD2 LEU A 96 1451 2304 1747 206 -246 -313 C ATOM 748 N LYS A 97 -5.108 -16.934 17.102 1.00 8.77 N ANISOU 748 N LYS A 97 781 1133 1418 -410 -276 1 N ATOM 749 CA LYS A 97 -3.975 -16.654 16.240 1.00 9.79 C ANISOU 749 CA LYS A 97 1113 1056 1550 102 -178 129 C ATOM 750 C LYS A 97 -4.002 -15.179 15.867 1.00 10.03 C ANISOU 750 C LYS A 97 1210 1000 1600 100 -346 110 C ATOM 751 O LYS A 97 -4.966 -14.705 15.272 1.00 11.43 O ANISOU 751 O LYS A 97 1162 1299 1879 90 -681 176 O ATOM 752 CB LYS A 97 -4.031 -17.532 14.999 1.00 10.71 C ANISOU 752 CB LYS A 97 1742 1063 1262 196 -102 4 C ATOM 753 CG LYS A 97 -3.838 -19.006 15.298 1.00 13.38 C ANISOU 753 CG LYS A 97 2438 1123 1522 96 -313 -2 C ATOM 754 CD LYS A 97 -3.787 -19.820 14.017 1.00 12.83 C ANISOU 754 CD LYS A 97 2502 806 1565 418 -549 -186 C ATOM 755 CE LYS A 97 -3.308 -21.239 14.279 1.00 12.62 C ANISOU 755 CE LYS A 97 2465 944 1385 414 -395 -183 C ATOM 756 NZ LYS A 97 -3.391 -22.068 13.051 1.00 15.22 N ANISOU 756 NZ LYS A 97 2698 1613 1471 17 -217 -451 N ATOM 757 N VAL A 98 -2.948 -14.455 16.219 1.00 8.88 N ANISOU 757 N VAL A 98 1328 727 1319 -92 -62 184 N ATOM 758 CA VAL A 98 -2.937 -13.007 16.040 1.00 9.72 C ANISOU 758 CA VAL A 98 1156 1150 1387 -331 39 -112 C ATOM 759 C VAL A 98 -2.138 -12.645 14.798 1.00 8.78 C ANISOU 759 C VAL A 98 709 1308 1318 -66 -74 55 C ATOM 760 O VAL A 98 -1.100 -13.226 14.546 1.00 10.28 O ANISOU 760 O VAL A 98 761 1521 1624 249 190 161 O ATOM 761 CB VAL A 98 -2.351 -12.315 17.280 1.00 9.30 C ANISOU 761 CB VAL A 98 925 1337 1270 -36 104 44 C ATOM 762 CG1 VAL A 98 -2.239 -10.809 17.055 1.00 12.11 C ANISOU 762 CG1 VAL A 98 1797 1448 1354 -163 -169 -31 C ATOM 763 CG2 VAL A 98 -3.211 -12.638 18.508 1.00 10.60 C ANISOU 763 CG2 VAL A 98 1373 1551 1104 88 482 -137 C ATOM 764 N VAL A 99 -2.634 -11.694 14.008 1.00 8.97 N ANISOU 764 N VAL A 99 1037 1488 881 79 0 131 N ATOM 765 CA VAL A 99 -1.964 -11.313 12.768 1.00 8.54 C ANISOU 765 CA VAL A 99 1387 931 927 73 -22 161 C ATOM 766 C VAL A 99 -2.116 -9.826 12.501 1.00 8.64 C ANISOU 766 C VAL A 99 1241 1103 938 -73 203 192 C ATOM 767 O VAL A 99 -3.160 -9.239 12.811 1.00 9.95 O ANISOU 767 O VAL A 99 1135 1040 1603 -28 204 99 O ATOM 768 CB VAL A 99 -2.511 -12.135 11.571 1.00 9.80 C ANISOU 768 CB VAL A 99 1017 1545 1162 93 4 -129 C ATOM 769 CG1 VAL A 99 -4.016 -11.894 11.359 1.00 11.69 C ANISOU 769 CG1 VAL A 99 1370 1721 1349 -36 -355 -53 C ATOM 770 CG2 VAL A 99 -1.727 -11.846 10.302 1.00 11.95 C ANISOU 770 CG2 VAL A 99 1872 1571 1095 225 217 -79 C ATOM 771 N GLY A 100 -1.092 -9.208 11.919 1.00 9.72 N ANISOU 771 N GLY A 100 1538 960 1195 8 229 273 N ATOM 772 CA GLY A 100 -1.239 -7.826 11.511 1.00 12.14 C ANISOU 772 CA GLY A 100 1382 1418 1812 -40 202 495 C ATOM 773 C GLY A 100 -0.018 -7.187 10.902 1.00 10.62 C ANISOU 773 C GLY A 100 1147 1221 1666 -27 302 544 C ATOM 774 O GLY A 100 1.114 -7.580 11.196 1.00 12.87 O ANISOU 774 O GLY A 100 1362 1530 1996 280 474 465 O ATOM 775 N ASN A 101 -0.269 -6.220 10.023 1.00 11.29 N ANISOU 775 N ASN A 101 1553 1089 1645 -266 77 373 N ATOM 776 CA ASN A 101 0.743 -5.310 9.505 1.00 13.17 C ANISOU 776 CA ASN A 101 1839 1431 1733 -160 377 461 C ATOM 777 C ASN A 101 0.774 -4.114 10.449 1.00 14.61 C ANISOU 777 C ASN A 101 1817 1503 2230 -143 104 448 C ATOM 778 O ASN A 101 -0.164 -3.322 10.486 1.00 15.35 O ANISOU 778 O ASN A 101 1630 1467 2734 31 -30 170 O ATOM 779 CB ASN A 101 0.359 -4.876 8.087 1.00 17.20 C ANISOU 779 CB ASN A 101 2526 2057 1949 -115 569 651 C ATOM 780 CG ASN A 101 1.365 -3.927 7.461 1.00 22.04 C ANISOU 780 CG ASN A 101 3452 2761 2160 345 751 906 C ATOM 781 OD1 ASN A 101 1.039 -3.191 6.529 1.00 26.79 O ANISOU 781 OD1 ASN A 101 3819 3591 2766 555 698 918 O ATOM 782 ND2 ASN A 101 2.591 -3.942 7.962 1.00 20.61 N ANISOU 782 ND2 ASN A 101 3231 2569 2028 201 811 847 N ATOM 783 N LEU A 102 1.839 -3.986 11.229 1.00 14.23 N ANISOU 783 N LEU A 102 1759 1321 2324 -216 105 266 N ATOM 784 CA LEU A 102 1.824 -3.044 12.344 1.00 13.16 C ANISOU 784 CA LEU A 102 1404 1130 2465 -216 22 265 C ATOM 785 C LEU A 102 2.433 -1.696 11.985 1.00 16.81 C ANISOU 785 C LEU A 102 1880 1566 2940 -191 -199 307 C ATOM 786 O LEU A 102 3.564 -1.628 11.519 1.00 19.72 O ANISOU 786 O LEU A 102 2512 2090 2890 -154 246 458 O ATOM 787 CB LEU A 102 2.559 -3.635 13.553 1.00 15.45 C ANISOU 787 CB LEU A 102 1643 1841 2385 -197 -79 428 C ATOM 788 CG LEU A 102 2.160 -5.049 13.973 1.00 13.75 C ANISOU 788 CG LEU A 102 1378 1759 2086 -140 -182 158 C ATOM 789 CD1 LEU A 102 2.916 -5.445 15.234 1.00 12.80 C ANISOU 789 CD1 LEU A 102 1423 1630 1810 -85 -47 -33 C ATOM 790 CD2 LEU A 102 0.645 -5.133 14.178 1.00 13.33 C ANISOU 790 CD2 LEU A 102 1329 1488 2246 8 177 334 C ATOM 791 N PRO A 103 1.679 -0.613 12.214 1.00 18.38 N ANISOU 791 N PRO A 103 1850 1578 3556 3 -652 563 N ATOM 792 CA PRO A 103 2.218 0.729 11.992 1.00 20.90 C ANISOU 792 CA PRO A 103 2429 1450 4061 19 -576 402 C ATOM 793 C PRO A 103 3.441 0.953 12.876 1.00 20.50 C ANISOU 793 C PRO A 103 2307 1431 4049 -339 -527 644 C ATOM 794 O PRO A 103 3.482 0.454 14.004 1.00 19.55 O ANISOU 794 O PRO A 103 2029 1544 3852 -478 -398 664 O ATOM 795 CB PRO A 103 1.062 1.647 12.409 1.00 23.27 C ANISOU 795 CB PRO A 103 2624 1885 4332 465 -814 168 C ATOM 796 CG PRO A 103 -0.166 0.802 12.275 1.00 23.58 C ANISOU 796 CG PRO A 103 2639 2067 4253 494 -1071 156 C ATOM 797 CD PRO A 103 0.265 -0.588 12.625 1.00 20.29 C ANISOU 797 CD PRO A 103 1763 1933 4013 619 -800 232 C ATOM 798 N TYR A 104 4.423 1.684 12.361 1.00 24.05 N ANISOU 798 N TYR A 104 2892 1909 4336 -868 -506 553 N ATOM 799 CA TYR A 104 5.687 1.879 13.055 1.00 26.63 C ANISOU 799 CA TYR A 104 2623 2727 4768 -1087 -427 466 C ATOM 800 C TYR A 104 5.524 2.361 14.497 1.00 26.00 C ANISOU 800 C TYR A 104 2585 2487 4804 -613 -487 223 C ATOM 801 O TYR A 104 6.245 1.903 15.380 1.00 26.72 O ANISOU 801 O TYR A 104 2209 3085 4858 -368 -563 -53 O ATOM 802 CB TYR A 104 6.579 2.854 12.278 1.00 34.93 C ANISOU 802 CB TYR A 104 4098 3877 5294 -1222 -469 347 C ATOM 803 CG TYR A 104 6.033 4.261 12.238 1.00 43.41 C ANISOU 803 CG TYR A 104 6035 4718 5740 -1216 -532 356 C ATOM 804 CD1 TYR A 104 4.989 4.599 11.383 1.00 47.57 C ANISOU 804 CD1 TYR A 104 6960 5151 5961 -905 -702 410 C ATOM 805 CD2 TYR A 104 6.552 5.253 13.064 1.00 47.56 C ANISOU 805 CD2 TYR A 104 6977 5165 5927 -1046 -544 261 C ATOM 806 CE1 TYR A 104 4.479 5.885 11.347 1.00 50.17 C ANISOU 806 CE1 TYR A 104 7521 5422 6118 -711 -637 387 C ATOM 807 CE2 TYR A 104 6.048 6.543 13.034 1.00 49.95 C ANISOU 807 CE2 TYR A 104 7562 5345 6071 -932 -508 367 C ATOM 808 CZ TYR A 104 5.011 6.851 12.175 1.00 51.49 C ANISOU 808 CZ TYR A 104 7830 5502 6231 -630 -432 428 C ATOM 809 OH TYR A 104 4.507 8.131 12.143 1.00 53.88 O ANISOU 809 OH TYR A 104 8165 5845 6460 -383 -169 387 O ATOM 810 N ASN A 105 4.581 3.271 14.746 1.00 24.97 N ANISOU 810 N ASN A 105 2825 1876 4784 -436 -289 49 N ATOM 811 CA ASN A 105 4.514 3.914 16.061 1.00 24.80 C ANISOU 811 CA ASN A 105 2888 1851 4683 196 -493 -105 C ATOM 812 C ASN A 105 3.711 3.163 17.123 1.00 23.60 C ANISOU 812 C ASN A 105 3032 1482 4453 348 -659 -459 C ATOM 813 O ASN A 105 3.567 3.638 18.252 1.00 29.33 O ANISOU 813 O ASN A 105 4717 1848 4577 -318 -759 -836 O ATOM 814 CB ASN A 105 4.069 5.389 15.957 1.00 26.34 C ANISOU 814 CB ASN A 105 2788 2429 4788 339 -883 -102 C ATOM 815 CG ASN A 105 2.580 5.549 15.679 1.00 29.24 C ANISOU 815 CG ASN A 105 3441 2728 4938 463 -884 232 C ATOM 816 OD1 ASN A 105 1.907 4.610 15.268 1.00 30.91 O ANISOU 816 OD1 ASN A 105 3497 3190 5056 191 -1277 340 O ATOM 817 ND2 ASN A 105 2.064 6.764 15.894 1.00 29.02 N ANISOU 817 ND2 ASN A 105 3249 2884 4891 395 -455 25 N ATOM 818 N VAL A 106 3.187 1.996 16.768 1.00 20.32 N ANISOU 818 N VAL A 106 2128 1324 4268 310 -481 204 N ATOM 819 CA VAL A 106 2.496 1.168 17.744 1.00 19.02 C ANISOU 819 CA VAL A 106 1466 1732 4027 458 -261 2 C ATOM 820 C VAL A 106 2.965 -0.288 17.697 1.00 16.31 C ANISOU 820 C VAL A 106 1406 1466 3322 475 38 -143 C ATOM 821 O VAL A 106 2.510 -1.107 18.487 1.00 16.37 O ANISOU 821 O VAL A 106 1220 1848 3152 340 -137 317 O ATOM 822 CB VAL A 106 0.958 1.215 17.559 1.00 22.44 C ANISOU 822 CB VAL A 106 1893 2152 4478 555 -265 117 C ATOM 823 CG1 VAL A 106 0.438 2.619 17.803 1.00 27.02 C ANISOU 823 CG1 VAL A 106 2479 2929 4857 302 -396 -60 C ATOM 824 CG2 VAL A 106 0.574 0.734 16.168 1.00 23.39 C ANISOU 824 CG2 VAL A 106 1966 2429 4492 -149 -315 121 C ATOM 825 N ALA A 107 3.888 -0.608 16.790 1.00 15.21 N ANISOU 825 N ALA A 107 1497 1411 2871 350 -135 1 N ATOM 826 CA ALA A 107 4.321 -2.000 16.617 1.00 13.63 C ANISOU 826 CA ALA A 107 1259 1379 2538 303 58 -201 C ATOM 827 C ALA A 107 4.814 -2.620 17.924 1.00 12.90 C ANISOU 827 C ALA A 107 974 1302 2623 156 -194 135 C ATOM 828 O ALA A 107 4.381 -3.714 18.303 1.00 13.67 O ANISOU 828 O ALA A 107 1353 1251 2590 -199 264 -40 O ATOM 829 CB ALA A 107 5.387 -2.104 15.536 1.00 14.98 C ANISOU 829 CB ALA A 107 1751 1430 2509 210 15 -217 C ATOM 830 N ASER A 108 5.707 -1.923 18.622 0.50 13.91 N ANISOU 830 N ASER A 108 998 1672 2615 223 -665 482 N ATOM 831 N BSER A 108 5.715 -1.921 18.616 0.50 13.32 N ANISOU 831 N BSER A 108 1088 1395 2577 142 -572 119 N ATOM 832 CA ASER A 108 6.271 -2.460 19.856 0.50 14.75 C ANISOU 832 CA ASER A 108 925 1880 2797 -49 -713 562 C ATOM 833 CA BSER A 108 6.260 -2.424 19.874 0.50 13.40 C ANISOU 833 CA BSER A 108 1086 1319 2686 -91 -517 -109 C ATOM 834 C ASER A 108 5.226 -2.624 20.959 0.50 15.61 C ANISOU 834 C ASER A 108 1209 1965 2755 62 -441 280 C ATOM 835 C BSER A 108 5.155 -2.665 20.895 0.50 12.71 C ANISOU 835 C BSER A 108 1053 1196 2578 100 -175 -570 C ATOM 836 O ASER A 108 5.284 -3.584 21.729 0.50 14.83 O ANISOU 836 O ASER A 108 1093 2014 2528 81 -478 462 O ATOM 837 O BSER A 108 5.116 -3.714 21.539 0.50 12.53 O ANISOU 837 O BSER A 108 1268 1134 2357 57 33 -519 O ATOM 838 CB ASER A 108 7.440 -1.606 20.339 0.50 16.07 C ANISOU 838 CB ASER A 108 1130 2031 2942 -95 -704 917 C ATOM 839 CB BSER A 108 7.301 -1.462 20.448 0.50 15.49 C ANISOU 839 CB BSER A 108 1506 1576 2802 -113 -368 124 C ATOM 840 OG ASER A 108 8.510 -1.675 19.414 0.50 19.66 O ANISOU 840 OG ASER A 108 1752 2563 3152 -391 -427 626 O ATOM 841 OG BSER A 108 7.870 -1.978 21.641 0.50 16.63 O ANISOU 841 OG BSER A 108 1929 1407 2980 178 -135 -202 O ATOM 842 N ALEU A 109 4.274 -1.696 21.037 0.50 16.18 N ANISOU 842 N ALEU A 109 1166 2091 2889 1 -460 83 N ATOM 843 N BLEU A 109 4.255 -1.693 21.030 0.50 12.46 N ANISOU 843 N BLEU A 109 560 1479 2692 146 -298 -592 N ATOM 844 CA ALEU A 109 3.197 -1.807 22.020 0.50 17.04 C ANISOU 844 CA ALEU A 109 1497 1972 3005 -150 -486 -235 C ATOM 845 CA BLEU A 109 3.177 -1.769 22.012 0.50 12.22 C ANISOU 845 CA BLEU A 109 731 1141 2769 224 -387 -853 C ATOM 846 C ALEU A 109 2.295 -3.003 21.733 0.50 13.81 C ANISOU 846 C ALEU A 109 1247 1482 2516 21 -560 -429 C ATOM 847 C BLEU A 109 2.212 -2.925 21.740 0.50 12.02 C ANISOU 847 C BLEU A 109 800 1353 2413 -3 -414 -659 C ATOM 848 O ALEU A 109 1.929 -3.750 22.644 0.50 13.29 O ANISOU 848 O ALEU A 109 1547 1449 2053 412 -456 -555 O ATOM 849 O BLEU A 109 1.730 -3.575 22.670 0.50 13.44 O ANISOU 849 O BLEU A 109 1169 1917 2018 21 2 -686 O ATOM 850 CB ALEU A 109 2.346 -0.535 22.067 0.50 22.00 C ANISOU 850 CB ALEU A 109 2536 2270 3553 -436 -483 -238 C ATOM 851 CB BLEU A 109 2.411 -0.445 22.064 0.50 14.48 C ANISOU 851 CB BLEU A 109 1660 701 3140 291 -465 -908 C ATOM 852 CG ALEU A 109 2.826 0.637 22.922 0.50 26.46 C ANISOU 852 CG ALEU A 109 3053 3044 3955 -720 -406 -90 C ATOM 853 CG BLEU A 109 3.272 0.806 22.228 0.50 16.83 C ANISOU 853 CG BLEU A 109 1958 1195 3241 85 -453 -845 C ATOM 854 CD1ALEU A 109 3.330 0.151 24.275 0.50 25.12 C ANISOU 854 CD1ALEU A 109 2549 3006 3987 -782 -453 -117 C ATOM 855 CD1BLEU A 109 2.422 2.068 22.198 0.50 17.82 C ANISOU 855 CD1BLEU A 109 2674 780 3316 260 -242 -878 C ATOM 856 CD2ALEU A 109 3.896 1.421 22.195 0.50 28.67 C ANISOU 856 CD2ALEU A 109 3661 3096 4133 -1135 -372 -100 C ATOM 857 CD2BLEU A 109 4.039 0.720 23.530 0.50 18.97 C ANISOU 857 CD2BLEU A 109 2398 1578 3230 -290 -1047 -840 C ATOM 858 N ILE A 110 1.932 -3.180 20.466 1.00 12.03 N ANISOU 858 N ILE A 110 897 1194 2480 233 -464 -305 N ATOM 859 CA ILE A 110 1.055 -4.281 20.088 1.00 11.72 C ANISOU 859 CA ILE A 110 1070 1297 2083 189 -383 -464 C ATOM 860 C ILE A 110 1.740 -5.615 20.369 1.00 10.32 C ANISOU 860 C ILE A 110 765 1405 1748 160 -89 -410 C ATOM 861 O ILE A 110 1.120 -6.552 20.881 1.00 11.93 O ANISOU 861 O ILE A 110 1407 1389 1735 55 151 -401 O ATOM 862 CB ILE A 110 0.612 -4.171 18.619 1.00 11.68 C ANISOU 862 CB ILE A 110 1298 1064 2074 334 -293 -178 C ATOM 863 CG1 ILE A 110 -0.313 -2.956 18.454 1.00 12.44 C ANISOU 863 CG1 ILE A 110 957 1708 2059 470 -308 223 C ATOM 864 CG2 ILE A 110 -0.102 -5.443 18.177 1.00 12.88 C ANISOU 864 CG2 ILE A 110 1616 1202 2075 -164 42 -164 C ATOM 865 CD1 ILE A 110 -0.628 -2.598 17.006 1.00 14.48 C ANISOU 865 CD1 ILE A 110 1418 1921 2161 881 -621 163 C ATOM 866 N ILE A 111 3.030 -5.697 20.063 1.00 10.77 N ANISOU 866 N ILE A 111 838 1413 1841 440 -321 -523 N ATOM 867 CA ILE A 111 3.762 -6.934 20.322 1.00 11.32 C ANISOU 867 CA ILE A 111 1009 1496 1795 367 -120 -311 C ATOM 868 C ILE A 111 3.867 -7.202 21.825 1.00 12.14 C ANISOU 868 C ILE A 111 1327 1549 1737 578 -205 -312 C ATOM 869 O ILE A 111 3.645 -8.320 22.274 1.00 11.93 O ANISOU 869 O ILE A 111 1144 1632 1756 320 -105 -321 O ATOM 870 CB ILE A 111 5.130 -6.915 19.652 1.00 11.22 C ANISOU 870 CB ILE A 111 906 1389 1965 641 87 -292 C ATOM 871 CG1 ILE A 111 4.942 -6.952 18.134 1.00 13.63 C ANISOU 871 CG1 ILE A 111 1166 1907 2103 352 305 -8 C ATOM 872 CG2 ILE A 111 5.978 -8.091 20.118 1.00 13.02 C ANISOU 872 CG2 ILE A 111 1505 1377 2064 534 321 -413 C ATOM 873 CD1 ILE A 111 6.203 -6.703 17.339 1.00 16.71 C ANISOU 873 CD1 ILE A 111 1418 2465 2466 375 358 360 C ATOM 874 N GLU A 112 4.179 -6.165 22.596 1.00 10.26 N ANISOU 874 N GLU A 112 1054 1222 1622 331 -156 -298 N ATOM 875 CA GLU A 112 4.190 -6.272 24.047 1.00 11.84 C ANISOU 875 CA GLU A 112 991 1508 2000 49 -321 -243 C ATOM 876 C GLU A 112 2.840 -6.753 24.579 1.00 10.94 C ANISOU 876 C GLU A 112 726 1595 1835 442 -64 -337 C ATOM 877 O GLU A 112 2.784 -7.635 25.429 1.00 13.08 O ANISOU 877 O GLU A 112 1215 1718 2035 61 -171 -246 O ATOM 878 CB GLU A 112 4.526 -4.921 24.668 1.00 14.04 C ANISOU 878 CB GLU A 112 1505 1635 2194 -29 -332 -502 C ATOM 879 CG GLU A 112 4.571 -4.934 26.178 1.00 17.65 C ANISOU 879 CG GLU A 112 2189 2160 2355 -101 -436 -609 C ATOM 880 CD GLU A 112 4.767 -3.549 26.771 1.00 21.77 C ANISOU 880 CD GLU A 112 2808 2724 2738 -325 -488 -645 C ATOM 881 OE1 GLU A 112 5.263 -2.654 26.053 1.00 22.03 O ANISOU 881 OE1 GLU A 112 2850 2471 3049 -478 -587 -980 O ATOM 882 OE2 GLU A 112 4.425 -3.352 27.955 1.00 25.23 O ANISOU 882 OE2 GLU A 112 3237 3462 2885 -477 -596 -799 O ATOM 883 N ASN A 113 1.754 -6.171 24.069 1.00 11.17 N ANISOU 883 N ASN A 113 532 1934 1776 179 -50 -508 N ATOM 884 CA ASN A 113 0.415 -6.547 24.520 1.00 12.47 C ANISOU 884 CA ASN A 113 785 1953 1999 319 -100 -374 C ATOM 885 C ASN A 113 0.097 -8.008 24.191 1.00 13.25 C ANISOU 885 C ASN A 113 1075 2046 1912 58 48 -233 C ATOM 886 O ASN A 113 -0.563 -8.712 24.970 1.00 12.70 O ANISOU 886 O ASN A 113 946 2064 1813 60 193 14 O ATOM 887 CB ASN A 113 -0.631 -5.615 23.913 1.00 12.93 C ANISOU 887 CB ASN A 113 393 2216 2304 105 -123 -196 C ATOM 888 CG ASN A 113 -2.003 -5.795 24.525 1.00 13.29 C ANISOU 888 CG ASN A 113 732 2230 2085 149 328 -146 C ATOM 889 OD1 ASN A 113 -2.141 -5.938 25.740 1.00 15.80 O ANISOU 889 OD1 ASN A 113 1461 2288 2254 184 477 -8 O ATOM 890 ND2 ASN A 113 -3.032 -5.784 23.682 1.00 13.33 N ANISOU 890 ND2 ASN A 113 783 2223 2059 12 1 -87 N ATOM 891 N THR A 114 0.571 -8.463 23.039 1.00 11.91 N ANISOU 891 N THR A 114 1023 1543 1958 -77 -80 -199 N ATOM 892 CA THR A 114 0.409 -9.864 22.660 1.00 10.96 C ANISOU 892 CA THR A 114 1233 1194 1735 28 73 -412 C ATOM 893 C THR A 114 1.059 -10.772 23.701 1.00 12.14 C ANISOU 893 C THR A 114 1523 1272 1815 73 -214 -166 C ATOM 894 O THR A 114 0.467 -11.778 24.111 1.00 12.32 O ANISOU 894 O THR A 114 1477 1504 1697 -109 82 -94 O ATOM 895 CB THR A 114 0.975 -10.129 21.253 1.00 12.56 C ANISOU 895 CB THR A 114 1924 1021 1826 -7 193 -504 C ATOM 896 OG1 THR A 114 0.331 -9.248 20.322 1.00 13.31 O ANISOU 896 OG1 THR A 114 1866 1370 1820 -228 153 -196 O ATOM 897 CG2 THR A 114 0.726 -11.574 20.832 1.00 14.93 C ANISOU 897 CG2 THR A 114 2298 1518 1856 -431 309 -778 C ATOM 898 N VAL A 115 2.258 -10.404 24.158 1.00 11.69 N ANISOU 898 N VAL A 115 1229 1298 1914 377 -242 -130 N ATOM 899 CA VAL A 115 2.948 -11.198 25.176 1.00 11.79 C ANISOU 899 CA VAL A 115 922 1519 2038 -68 -92 -76 C ATOM 900 C VAL A 115 2.159 -11.248 26.487 1.00 11.78 C ANISOU 900 C VAL A 115 934 1500 2041 232 -183 -325 C ATOM 901 O VAL A 115 2.069 -12.304 27.127 1.00 14.08 O ANISOU 901 O VAL A 115 1190 1804 2355 135 -517 -358 O ATOM 902 CB VAL A 115 4.386 -10.694 25.435 1.00 14.36 C ANISOU 902 CB VAL A 115 1312 1789 2354 -90 -158 204 C ATOM 903 CG1 VAL A 115 5.050 -11.507 26.548 1.00 16.99 C ANISOU 903 CG1 VAL A 115 1739 1844 2870 31 -212 255 C ATOM 904 CG2 VAL A 115 5.203 -10.772 24.160 1.00 17.08 C ANISOU 904 CG2 VAL A 115 1812 2174 2502 252 58 440 C ATOM 905 N TYR A 116 1.577 -10.121 26.887 1.00 12.76 N ANISOU 905 N TYR A 116 1308 1662 1877 580 -301 -391 N ATOM 906 CA TYR A 116 0.772 -10.118 28.107 1.00 13.62 C ANISOU 906 CA TYR A 116 1532 1883 1757 427 -188 -931 C ATOM 907 C TYR A 116 -0.385 -11.101 27.981 1.00 13.79 C ANISOU 907 C TYR A 116 1616 2028 1594 423 -49 -512 C ATOM 908 O TYR A 116 -0.898 -11.603 28.991 1.00 17.41 O ANISOU 908 O TYR A 116 2142 2855 1617 -128 -134 -311 O ATOM 909 CB TYR A 116 0.217 -8.726 28.415 1.00 16.50 C ANISOU 909 CB TYR A 116 1527 2589 2151 241 -298 -1206 C ATOM 910 CG TYR A 116 1.226 -7.710 28.884 1.00 20.97 C ANISOU 910 CG TYR A 116 2437 2820 2710 293 -297 -1284 C ATOM 911 CD1 TYR A 116 2.085 -7.984 29.940 1.00 21.86 C ANISOU 911 CD1 TYR A 116 2500 2856 2948 -86 -784 -1788 C ATOM 912 CD2 TYR A 116 1.296 -6.465 28.286 1.00 24.93 C ANISOU 912 CD2 TYR A 116 3236 3179 3054 -25 -185 -1263 C ATOM 913 CE1 TYR A 116 3.001 -7.040 30.379 1.00 22.33 C ANISOU 913 CE1 TYR A 116 2338 2947 3198 -772 -920 -1433 C ATOM 914 CE2 TYR A 116 2.199 -5.522 28.710 1.00 25.63 C ANISOU 914 CE2 TYR A 116 3218 3361 3158 -813 -668 -1416 C ATOM 915 CZ TYR A 116 3.055 -5.815 29.754 1.00 25.59 C ANISOU 915 CZ TYR A 116 3020 3424 3279 -526 -875 -1307 C ATOM 916 OH TYR A 116 3.958 -4.875 30.173 1.00 30.08 O ANISOU 916 OH TYR A 116 3791 3924 3712 -165 -268 -870 O ATOM 917 N ASN A 117 -0.796 -11.359 26.740 1.00 12.12 N ANISOU 917 N ASN A 117 1162 1919 1523 152 -207 -481 N ATOM 918 CA ASN A 117 -1.906 -12.268 26.450 1.00 12.57 C ANISOU 918 CA ASN A 117 1132 1997 1645 577 -217 -191 C ATOM 919 C ASN A 117 -1.446 -13.658 25.994 1.00 12.26 C ANISOU 919 C ASN A 117 1108 2022 1526 246 117 181 C ATOM 920 O ASN A 117 -2.214 -14.415 25.403 1.00 12.79 O ANISOU 920 O ASN A 117 975 2254 1628 6 -440 115 O ATOM 921 CB ASN A 117 -2.811 -11.631 25.393 1.00 12.41 C ANISOU 921 CB ASN A 117 921 1935 1859 450 5 52 C ATOM 922 CG ASN A 117 -3.668 -10.520 25.969 1.00 11.87 C ANISOU 922 CG ASN A 117 738 1796 1976 -40 127 32 C ATOM 923 OD1 ASN A 117 -4.723 -10.783 26.540 1.00 15.59 O ANISOU 923 OD1 ASN A 117 1118 2712 2091 -96 160 -7 O ATOM 924 ND2 ASN A 117 -3.204 -9.278 25.857 1.00 13.14 N ANISOU 924 ND2 ASN A 117 960 1864 2167 -291 -63 -254 N ATOM 925 N LYS A 118 -0.206 -14.005 26.311 1.00 13.21 N ANISOU 925 N LYS A 118 1225 2147 1645 468 -54 41 N ATOM 926 CA LYS A 118 0.390 -15.241 25.804 1.00 12.53 C ANISOU 926 CA LYS A 118 1067 2124 1568 495 -325 -51 C ATOM 927 C LYS A 118 -0.401 -16.505 26.157 1.00 11.87 C ANISOU 927 C LYS A 118 1304 1763 1441 194 -90 10 C ATOM 928 O LYS A 118 -0.339 -17.498 25.433 1.00 14.64 O ANISOU 928 O LYS A 118 1516 2020 2026 155 5 -208 O ATOM 929 CB LYS A 118 1.825 -15.377 26.305 1.00 11.77 C ANISOU 929 CB LYS A 118 1287 1850 1335 391 -345 -304 C ATOM 930 CG LYS A 118 1.922 -15.442 27.812 1.00 15.31 C ANISOU 930 CG LYS A 118 1968 2335 1512 131 -699 -148 C ATOM 931 CD LYS A 118 3.351 -15.575 28.248 1.00 18.55 C ANISOU 931 CD LYS A 118 1890 3339 1817 -88 -893 -292 C ATOM 932 CE LYS A 118 3.467 -15.493 29.766 1.00 21.33 C ANISOU 932 CE LYS A 118 2179 3942 1981 330 -765 21 C ATOM 933 NZ LYS A 118 2.823 -16.635 30.474 1.00 24.65 N ANISOU 933 NZ LYS A 118 2498 4625 2243 427 -350 2 N ATOM 934 N ASP A 119 -1.132 -16.486 27.267 1.00 13.27 N ANISOU 934 N ASP A 119 1293 2370 1377 -265 79 37 N ATOM 935 CA ASP A 119 -1.849 -17.690 27.671 1.00 15.25 C ANISOU 935 CA ASP A 119 1896 2501 1395 -134 152 -209 C ATOM 936 C ASP A 119 -2.912 -18.113 26.657 1.00 15.38 C ANISOU 936 C ASP A 119 1860 2242 1739 -239 221 -159 C ATOM 937 O ASP A 119 -3.358 -19.268 26.650 1.00 17.76 O ANISOU 937 O ASP A 119 2512 2082 2151 -276 -301 423 O ATOM 938 CB ASP A 119 -2.459 -17.522 29.063 1.00 22.17 C ANISOU 938 CB ASP A 119 3087 3503 1833 -618 208 -322 C ATOM 939 CG ASP A 119 -1.407 -17.518 30.152 1.00 31.34 C ANISOU 939 CG ASP A 119 4888 4497 2523 -311 74 -334 C ATOM 940 OD1 ASP A 119 -0.236 -17.863 29.861 1.00 31.18 O ANISOU 940 OD1 ASP A 119 4173 4971 2703 -676 -235 -209 O ATOM 941 OD2 ASP A 119 -1.750 -17.167 31.298 1.00 35.84 O ANISOU 941 OD2 ASP A 119 6318 4566 2732 -9 -268 -635 O ATOM 942 N ACYS A 120 -3.315 -17.182 25.802 0.50 12.06 N ANISOU 942 N ACYS A 120 954 2187 1438 76 89 -148 N ATOM 943 N BCYS A 120 -3.306 -17.180 25.796 0.50 14.15 N ANISOU 943 N BCYS A 120 1386 2408 1580 55 440 -251 N ATOM 944 CA ACYS A 120 -4.331 -17.481 24.801 0.50 11.12 C ANISOU 944 CA ACYS A 120 653 2170 1401 374 -275 38 C ATOM 945 CA BCYS A 120 -4.337 -17.454 24.801 0.50 15.65 C ANISOU 945 CA BCYS A 120 1541 2706 1697 420 297 -143 C ATOM 946 C ACYS A 120 -3.862 -17.158 23.384 0.50 12.18 C ANISOU 946 C ACYS A 120 955 2170 1502 161 -20 -69 C ATOM 947 C BCYS A 120 -3.827 -17.332 23.366 0.50 13.32 C ANISOU 947 C BCYS A 120 1161 2264 1635 271 309 63 C ATOM 948 O ACYS A 120 -4.677 -17.064 22.470 0.50 12.78 O ANISOU 948 O ACYS A 120 816 2407 1632 -19 -279 -342 O ATOM 949 O BCYS A 120 -4.576 -17.565 22.419 0.50 13.28 O ANISOU 949 O BCYS A 120 984 2243 1819 258 103 268 O ATOM 950 CB ACYS A 120 -5.623 -16.725 25.099 0.50 12.31 C ANISOU 950 CB ACYS A 120 885 2177 1612 30 35 152 C ATOM 951 CB BCYS A 120 -5.542 -16.535 25.005 0.50 21.03 C ANISOU 951 CB BCYS A 120 2397 3505 2088 476 420 -192 C ATOM 952 SG ACYS A 120 -5.487 -14.980 24.741 0.50 12.59 S ANISOU 952 SG ACYS A 120 779 1983 2021 326 155 47 S ATOM 953 SG BCYS A 120 -6.245 -16.619 26.659 0.50 26.24 S ANISOU 953 SG BCYS A 120 3237 4145 2587 738 518 -299 S ATOM 954 N VAL A 121 -2.556 -16.974 23.208 1.00 11.54 N ANISOU 954 N VAL A 121 1079 1815 1488 248 162 121 N ATOM 955 CA VAL A 121 -1.986 -16.724 21.881 1.00 10.38 C ANISOU 955 CA VAL A 121 1059 1472 1412 139 117 65 C ATOM 956 C VAL A 121 -0.829 -17.679 21.562 1.00 11.27 C ANISOU 956 C VAL A 121 1259 1767 1256 33 -115 -15 C ATOM 957 O VAL A 121 0.331 -17.392 21.873 1.00 12.99 O ANISOU 957 O VAL A 121 1252 2112 1571 58 -101 -109 O ATOM 958 CB VAL A 121 -1.521 -15.253 21.739 1.00 12.29 C ANISOU 958 CB VAL A 121 1658 1429 1583 74 82 250 C ATOM 959 CG1 VAL A 121 -0.938 -14.990 20.360 1.00 14.15 C ANISOU 959 CG1 VAL A 121 1991 1820 1565 -484 46 87 C ATOM 960 CG2 VAL A 121 -2.673 -14.289 22.015 1.00 10.63 C ANISOU 960 CG2 VAL A 121 1394 1334 1309 294 104 257 C ATOM 961 N PRO A 122 -1.136 -18.819 20.932 1.00 10.55 N ANISOU 961 N PRO A 122 801 1511 1695 72 -115 -36 N ATOM 962 CA PRO A 122 -0.086 -19.802 20.621 1.00 12.06 C ANISOU 962 CA PRO A 122 1298 1443 1839 306 245 -248 C ATOM 963 C PRO A 122 0.739 -19.395 19.402 1.00 9.58 C ANISOU 963 C PRO A 122 738 1299 1602 -52 104 -9 C ATOM 964 O PRO A 122 1.833 -19.917 19.193 1.00 12.61 O ANISOU 964 O PRO A 122 1079 1979 1731 216 -275 219 O ATOM 965 CB PRO A 122 -0.888 -21.065 20.281 1.00 13.78 C ANISOU 965 CB PRO A 122 1600 1452 2182 -18 135 -369 C ATOM 966 CG PRO A 122 -2.211 -20.530 19.797 1.00 16.17 C ANISOU 966 CG PRO A 122 1662 2014 2465 -200 253 -543 C ATOM 967 CD PRO A 122 -2.484 -19.370 20.711 1.00 14.42 C ANISOU 967 CD PRO A 122 1621 1729 2129 -167 17 -401 C ATOM 968 N LEU A 123 0.224 -18.459 18.612 1.00 10.43 N ANISOU 968 N LEU A 123 1281 1310 1372 -50 -14 75 N ATOM 969 CA LEU A 123 0.870 -18.124 17.351 1.00 8.91 C ANISOU 969 CA LEU A 123 1019 1072 1294 35 -298 151 C ATOM 970 C LEU A 123 0.516 -16.706 16.938 1.00 9.44 C ANISOU 970 C LEU A 123 1022 1112 1451 216 -158 229 C ATOM 971 O LEU A 123 -0.646 -16.295 17.018 1.00 10.69 O ANISOU 971 O LEU A 123 1020 1338 1702 198 18 169 O ATOM 972 CB LEU A 123 0.394 -19.088 16.252 1.00 13.10 C ANISOU 972 CB LEU A 123 1878 1681 1418 -130 1 -297 C ATOM 973 CG LEU A 123 1.017 -18.905 14.870 1.00 18.03 C ANISOU 973 CG LEU A 123 2217 2748 1883 -503 -45 -684 C ATOM 974 CD1 LEU A 123 2.498 -19.215 14.926 1.00 21.56 C ANISOU 974 CD1 LEU A 123 2798 3304 2087 -65 -20 -395 C ATOM 975 CD2 LEU A 123 0.320 -19.805 13.864 1.00 21.10 C ANISOU 975 CD2 LEU A 123 2728 3388 1900 -1291 85 -912 C ATOM 976 N ALA A 124 1.514 -15.967 16.477 1.00 9.07 N ANISOU 976 N ALA A 124 1265 932 1248 126 -66 326 N ATOM 977 CA ALA A 124 1.267 -14.649 15.913 1.00 8.70 C ANISOU 977 CA ALA A 124 1046 979 1281 148 -52 -35 C ATOM 978 C ALA A 124 2.152 -14.410 14.711 1.00 9.64 C ANISOU 978 C ALA A 124 963 1237 1462 180 -79 174 C ATOM 979 O ALA A 124 3.292 -14.855 14.677 1.00 11.86 O ANISOU 979 O ALA A 124 1139 1893 1474 369 -125 457 O ATOM 980 CB ALA A 124 1.474 -13.546 16.974 1.00 10.74 C ANISOU 980 CB ALA A 124 1729 1038 1313 -26 -116 -216 C ATOM 981 N VAL A 125 1.608 -13.724 13.711 1.00 8.33 N ANISOU 981 N VAL A 125 680 968 1515 -32 -32 -99 N ATOM 982 CA VAL A 125 2.376 -13.361 12.523 1.00 9.89 C ANISOU 982 CA VAL A 125 1273 860 1623 -102 418 14 C ATOM 983 C VAL A 125 2.263 -11.865 12.323 1.00 9.79 C ANISOU 983 C VAL A 125 1138 916 1665 -214 289 -164 C ATOM 984 O VAL A 125 1.161 -11.345 12.197 1.00 10.90 O ANISOU 984 O VAL A 125 907 1168 2065 3 65 259 O ATOM 985 CB VAL A 125 1.870 -14.099 11.259 1.00 11.47 C ANISOU 985 CB VAL A 125 1577 1161 1617 -274 201 67 C ATOM 986 CG1 VAL A 125 2.624 -13.622 10.017 1.00 13.37 C ANISOU 986 CG1 VAL A 125 1797 1705 1577 -53 211 -7 C ATOM 987 CG2 VAL A 125 2.025 -15.603 11.437 1.00 12.45 C ANISOU 987 CG2 VAL A 125 1920 947 1861 -347 132 -70 C ATOM 988 N PHE A 126 3.397 -11.171 12.315 1.00 10.97 N ANISOU 988 N PHE A 126 1113 1310 1742 -70 278 33 N ATOM 989 CA PHE A 126 3.395 -9.719 12.201 1.00 10.54 C ANISOU 989 CA PHE A 126 1350 1341 1313 37 376 -103 C ATOM 990 C PHE A 126 4.280 -9.247 11.059 1.00 10.87 C ANISOU 990 C PHE A 126 1267 1396 1464 -17 494 174 C ATOM 991 O PHE A 126 5.339 -9.828 10.783 1.00 12.37 O ANISOU 991 O PHE A 126 1333 1529 1838 213 567 64 O ATOM 992 CB PHE A 126 3.911 -9.072 13.486 1.00 11.33 C ANISOU 992 CB PHE A 126 1632 1296 1377 -361 366 -314 C ATOM 993 CG PHE A 126 3.007 -9.251 14.679 1.00 11.46 C ANISOU 993 CG PHE A 126 1350 1389 1613 -126 384 -16 C ATOM 994 CD1 PHE A 126 1.678 -8.848 14.634 1.00 12.17 C ANISOU 994 CD1 PHE A 126 1343 1484 1797 82 647 -65 C ATOM 995 CD2 PHE A 126 3.503 -9.791 15.863 1.00 11.82 C ANISOU 995 CD2 PHE A 126 1444 1447 1599 -58 87 1 C ATOM 996 CE1 PHE A 126 0.855 -8.984 15.746 1.00 11.74 C ANISOU 996 CE1 PHE A 126 1332 1421 1705 126 193 -177 C ATOM 997 CE2 PHE A 126 2.683 -9.941 16.978 1.00 12.73 C ANISOU 997 CE2 PHE A 126 1626 1477 1731 -333 73 22 C ATOM 998 CZ PHE A 126 1.360 -9.534 16.920 1.00 11.81 C ANISOU 998 CZ PHE A 126 1371 1502 1613 -87 -113 -246 C ATOM 999 N MET A 127 3.860 -8.170 10.410 1.00 10.08 N ANISOU 999 N MET A 127 1356 1354 1118 -336 437 292 N ATOM 1000 CA MET A 127 4.755 -7.465 9.503 1.00 11.83 C ANISOU 1000 CA MET A 127 1363 1615 1517 -111 235 431 C ATOM 1001 C MET A 127 5.157 -6.176 10.200 1.00 11.67 C ANISOU 1001 C MET A 127 1098 1528 1805 142 -44 489 C ATOM 1002 O MET A 127 4.297 -5.423 10.675 1.00 12.58 O ANISOU 1002 O MET A 127 1189 1527 2064 74 110 357 O ATOM 1003 CB MET A 127 4.088 -7.205 8.152 1.00 14.29 C ANISOU 1003 CB MET A 127 1951 1764 1713 -70 189 491 C ATOM 1004 CG MET A 127 5.026 -6.553 7.152 1.00 17.09 C ANISOU 1004 CG MET A 127 2254 2411 1827 -70 100 537 C ATOM 1005 SD MET A 127 4.663 -6.939 5.420 1.00 21.13 S ANISOU 1005 SD MET A 127 2956 2848 2224 448 327 347 S ATOM 1006 CE MET A 127 2.965 -6.408 5.268 1.00 20.35 C ANISOU 1006 CE MET A 127 2593 2867 2270 906 319 253 C ATOM 1007 N VAL A 128 6.466 -5.955 10.292 1.00 11.62 N ANISOU 1007 N VAL A 128 1128 1394 1890 -147 0 212 N ATOM 1008 CA VAL A 128 7.044 -4.841 11.026 1.00 12.54 C ANISOU 1008 CA VAL A 128 975 1563 2225 -283 -170 183 C ATOM 1009 C VAL A 128 8.249 -4.321 10.251 1.00 14.02 C ANISOU 1009 C VAL A 128 1035 1735 2555 -452 -74 504 C ATOM 1010 O VAL A 128 8.663 -4.932 9.259 1.00 15.52 O ANISOU 1010 O VAL A 128 1498 1903 2495 -326 140 689 O ATOM 1011 CB VAL A 128 7.505 -5.265 12.448 1.00 13.79 C ANISOU 1011 CB VAL A 128 1204 1758 2275 -158 187 317 C ATOM 1012 CG1 VAL A 128 6.311 -5.658 13.304 1.00 15.01 C ANISOU 1012 CG1 VAL A 128 1665 1976 2060 -104 67 536 C ATOM 1013 CG2 VAL A 128 8.524 -6.400 12.382 1.00 16.72 C ANISOU 1013 CG2 VAL A 128 1444 2454 2453 -40 -177 588 C ATOM 1014 N GLN A 129 8.805 -3.194 10.688 1.00 16.24 N ANISOU 1014 N GLN A 129 1411 1673 3086 -486 181 1085 N ATOM 1015 CA GLN A 129 10.052 -2.700 10.111 1.00 18.32 C ANISOU 1015 CA GLN A 129 1741 1684 3533 -506 31 829 C ATOM 1016 C GLN A 129 11.146 -3.754 10.276 1.00 18.55 C ANISOU 1016 C GLN A 129 1311 2315 3420 -465 226 862 C ATOM 1017 O GLN A 129 11.181 -4.476 11.280 1.00 18.78 O ANISOU 1017 O GLN A 129 1434 2412 3288 -479 341 981 O ATOM 1018 CB GLN A 129 10.481 -1.382 10.766 1.00 22.79 C ANISOU 1018 CB GLN A 129 2412 2022 4222 -345 -288 650 C ATOM 1019 CG GLN A 129 9.543 -0.228 10.488 1.00 26.22 C ANISOU 1019 CG GLN A 129 3152 2033 4775 -458 -928 849 C ATOM 1020 CD GLN A 129 10.093 1.107 10.954 1.00 33.03 C ANISOU 1020 CD GLN A 129 4403 2817 5329 -654 -1212 830 C ATOM 1021 OE1 GLN A 129 9.646 2.162 10.507 1.00 38.03 O ANISOU 1021 OE1 GLN A 129 5140 3643 5666 -959 -771 865 O ATOM 1022 NE2 GLN A 129 11.068 1.068 11.857 1.00 36.41 N ANISOU 1022 NE2 GLN A 129 5348 2962 5521 -1145 -1718 371 N ATOM 1023 N LYS A 130 12.018 -3.856 9.277 1.00 19.47 N ANISOU 1023 N LYS A 130 1250 2668 3479 127 577 807 N ATOM 1024 CA LYS A 130 13.069 -4.867 9.286 1.00 21.31 C ANISOU 1024 CA LYS A 130 1575 3003 3519 -120 641 1016 C ATOM 1025 C LYS A 130 13.902 -4.781 10.557 1.00 21.10 C ANISOU 1025 C LYS A 130 1422 3096 3496 -206 492 1155 C ATOM 1026 O LYS A 130 14.252 -5.801 11.142 1.00 20.60 O ANISOU 1026 O LYS A 130 1594 2785 3445 -131 -174 1342 O ATOM 1027 CB LYS A 130 13.960 -4.742 8.048 1.00 23.35 C ANISOU 1027 CB LYS A 130 1758 3356 3757 374 870 1184 C ATOM 1028 CG LYS A 130 14.981 -5.859 7.899 1.00 26.29 C ANISOU 1028 CG LYS A 130 2188 3962 3836 486 656 1314 C ATOM 1029 CD LYS A 130 15.920 -5.571 6.748 1.00 33.22 C ANISOU 1029 CD LYS A 130 3939 4679 4001 101 393 1347 C ATOM 1030 CE LYS A 130 16.714 -4.293 7.002 1.00 39.59 C ANISOU 1030 CE LYS A 130 5342 5400 4298 -250 578 1225 C ATOM 1031 NZ LYS A 130 17.574 -3.904 5.844 1.00 43.99 N ANISOU 1031 NZ LYS A 130 6347 5843 4524 -241 377 1184 N ATOM 1032 N GLU A 131 14.208 -3.562 10.991 1.00 22.34 N ANISOU 1032 N GLU A 131 1620 3341 3527 -695 21 989 N ATOM 1033 CA GLU A 131 15.005 -3.379 12.199 1.00 25.84 C ANISOU 1033 CA GLU A 131 2695 3274 3846 -1224 -296 703 C ATOM 1034 C GLU A 131 14.325 -3.957 13.444 1.00 23.21 C ANISOU 1034 C GLU A 131 2410 2754 3655 -504 -251 746 C ATOM 1035 O GLU A 131 14.983 -4.578 14.286 1.00 22.03 O ANISOU 1035 O GLU A 131 1912 2813 3643 -687 -547 530 O ATOM 1036 CB GLU A 131 15.350 -1.906 12.420 1.00 31.27 C ANISOU 1036 CB GLU A 131 3766 3839 4276 -1608 -464 941 C ATOM 1037 CG GLU A 131 16.176 -1.676 13.672 1.00 39.64 C ANISOU 1037 CG GLU A 131 5340 5026 4694 -1481 -201 860 C ATOM 1038 CD GLU A 131 17.504 -2.415 13.631 1.00 49.25 C ANISOU 1038 CD GLU A 131 7281 6353 5079 -1152 -187 953 C ATOM 1039 OE1 GLU A 131 18.269 -2.216 12.660 1.00 54.79 O ANISOU 1039 OE1 GLU A 131 8168 7177 5473 -812 -37 835 O ATOM 1040 OE2 GLU A 131 17.785 -3.192 14.570 1.00 51.46 O ANISOU 1040 OE2 GLU A 131 7713 6717 5122 -1185 -503 1107 O ATOM 1041 N VAL A 132 13.018 -3.738 13.567 1.00 20.33 N ANISOU 1041 N VAL A 132 2041 2120 3562 -180 9 692 N ATOM 1042 CA VAL A 132 12.266 -4.279 14.696 1.00 18.86 C ANISOU 1042 CA VAL A 132 1640 2166 3359 250 -222 500 C ATOM 1043 C VAL A 132 12.321 -5.801 14.653 1.00 16.26 C ANISOU 1043 C VAL A 132 1410 1899 2869 -75 -341 309 C ATOM 1044 O VAL A 132 12.536 -6.462 15.673 1.00 16.27 O ANISOU 1044 O VAL A 132 1292 2142 2745 41 -367 378 O ATOM 1045 CB VAL A 132 10.797 -3.790 14.692 1.00 21.96 C ANISOU 1045 CB VAL A 132 2828 2108 3405 500 -694 390 C ATOM 1046 CG1 VAL A 132 9.951 -4.601 15.678 1.00 21.07 C ANISOU 1046 CG1 VAL A 132 2165 2581 3259 614 -836 40 C ATOM 1047 CG2 VAL A 132 10.740 -2.290 15.010 1.00 24.83 C ANISOU 1047 CG2 VAL A 132 3694 2253 3486 361 -1058 382 C ATOM 1048 N ALA A 133 12.145 -6.351 13.457 1.00 15.57 N ANISOU 1048 N ALA A 133 1204 1997 2713 -215 41 145 N ATOM 1049 CA ALA A 133 12.173 -7.802 13.256 1.00 14.17 C ANISOU 1049 CA ALA A 133 1169 1652 2563 -150 -84 -327 C ATOM 1050 C ALA A 133 13.534 -8.403 13.620 1.00 14.27 C ANISOU 1050 C ALA A 133 1204 1684 2533 -2 106 33 C ATOM 1051 O ALA A 133 13.611 -9.448 14.267 1.00 16.16 O ANISOU 1051 O ALA A 133 1629 2229 2280 100 20 393 O ATOM 1052 CB ALA A 133 11.805 -8.144 11.806 1.00 14.21 C ANISOU 1052 CB ALA A 133 1352 1757 2289 -212 -326 -469 C ATOM 1053 N GLU A 134 14.601 -7.740 13.193 1.00 14.61 N ANISOU 1053 N GLU A 134 864 2179 2507 -226 206 168 N ATOM 1054 CA GLU A 134 15.948 -8.217 13.473 1.00 17.71 C ANISOU 1054 CA GLU A 134 1145 2963 2620 -478 177 675 C ATOM 1055 C GLU A 134 16.238 -8.189 14.969 1.00 15.80 C ANISOU 1055 C GLU A 134 1054 2502 2444 -286 54 599 C ATOM 1056 O GLU A 134 16.846 -9.112 15.509 1.00 15.95 O ANISOU 1056 O GLU A 134 988 2590 2482 138 -53 550 O ATOM 1057 CB GLU A 134 16.975 -7.375 12.724 1.00 21.60 C ANISOU 1057 CB GLU A 134 1422 3981 2803 -289 482 878 C ATOM 1058 CG GLU A 134 16.925 -7.535 11.221 1.00 25.75 C ANISOU 1058 CG GLU A 134 1945 4715 3123 -63 924 809 C ATOM 1059 CD GLU A 134 17.934 -6.647 10.509 1.00 32.89 C ANISOU 1059 CD GLU A 134 3198 5645 3654 25 989 518 C ATOM 1060 OE1 GLU A 134 18.242 -5.550 11.025 1.00 37.94 O ANISOU 1060 OE1 GLU A 134 4112 6377 3925 -9 933 577 O ATOM 1061 OE2 GLU A 134 18.416 -7.043 9.432 1.00 33.32 O ANISOU 1061 OE2 GLU A 134 2971 5830 3859 599 1031 178 O ATOM 1062 N LYS A 135 15.804 -7.129 15.645 1.00 16.36 N ANISOU 1062 N LYS A 135 1228 2524 2463 -354 274 662 N ATOM 1063 CA LYS A 135 15.951 -7.071 17.098 1.00 16.79 C ANISOU 1063 CA LYS A 135 1444 2250 2684 -552 284 56 C ATOM 1064 C LYS A 135 15.193 -8.219 17.761 1.00 14.36 C ANISOU 1064 C LYS A 135 916 1965 2573 -446 -59 61 C ATOM 1065 O LYS A 135 15.733 -8.903 18.633 1.00 15.29 O ANISOU 1065 O LYS A 135 933 2375 2500 -69 -97 230 O ATOM 1066 CB LYS A 135 15.465 -5.731 17.645 1.00 18.70 C ANISOU 1066 CB LYS A 135 1819 2058 3225 -561 73 182 C ATOM 1067 CG LYS A 135 16.435 -4.594 17.430 1.00 20.77 C ANISOU 1067 CG LYS A 135 2369 1954 3569 -483 -642 140 C ATOM 1068 CD LYS A 135 15.782 -3.267 17.771 1.00 24.76 C ANISOU 1068 CD LYS A 135 3243 2177 3986 -518 -285 -32 C ATOM 1069 CE LYS A 135 15.418 -3.208 19.247 1.00 31.27 C ANISOU 1069 CE LYS A 135 4914 2483 4483 -528 -204 210 C ATOM 1070 NZ LYS A 135 15.150 -1.814 19.703 1.00 37.63 N ANISOU 1070 NZ LYS A 135 6205 3190 4901 -927 -319 396 N ATOM 1071 N LEU A 136 13.948 -8.439 17.339 1.00 14.33 N ANISOU 1071 N LEU A 136 945 1960 2538 -240 -8 92 N ATOM 1072 CA LEU A 136 13.133 -9.503 17.926 1.00 14.02 C ANISOU 1072 CA LEU A 136 781 2071 2473 1 24 11 C ATOM 1073 C LEU A 136 13.758 -10.884 17.755 1.00 14.73 C ANISOU 1073 C LEU A 136 956 2079 2560 -159 168 208 C ATOM 1074 O LEU A 136 13.713 -11.708 18.660 1.00 15.07 O ANISOU 1074 O LEU A 136 1093 2077 2553 36 181 263 O ATOM 1075 CB LEU A 136 11.715 -9.480 17.351 1.00 13.46 C ANISOU 1075 CB LEU A 136 600 2256 2256 -28 102 176 C ATOM 1076 CG LEU A 136 10.876 -8.274 17.772 1.00 18.06 C ANISOU 1076 CG LEU A 136 1479 3174 2208 185 -87 97 C ATOM 1077 CD1 LEU A 136 9.527 -8.294 17.090 1.00 18.13 C ANISOU 1077 CD1 LEU A 136 1060 3581 2247 162 -203 375 C ATOM 1078 CD2 LEU A 136 10.717 -8.213 19.297 1.00 19.90 C ANISOU 1078 CD2 LEU A 136 2084 3472 2003 454 -112 338 C ATOM 1079 N GLN A 137 14.346 -11.122 16.590 1.00 13.77 N ANISOU 1079 N GLN A 137 801 1888 2542 -176 -16 71 N ATOM 1080 CA GLN A 137 15.017 -12.385 16.314 1.00 15.69 C ANISOU 1080 CA GLN A 137 1067 2177 2715 135 182 149 C ATOM 1081 C GLN A 137 16.210 -12.581 17.249 1.00 15.36 C ANISOU 1081 C GLN A 137 1214 2119 2500 -33 105 173 C ATOM 1082 O GLN A 137 16.490 -13.699 17.682 1.00 17.65 O ANISOU 1082 O GLN A 137 1845 2225 2636 539 62 321 O ATOM 1083 CB GLN A 137 15.446 -12.437 14.851 1.00 18.37 C ANISOU 1083 CB GLN A 137 1545 2523 2911 572 280 -231 C ATOM 1084 CG GLN A 137 16.111 -13.725 14.426 1.00 23.90 C ANISOU 1084 CG GLN A 137 2573 3107 3401 772 -91 -108 C ATOM 1085 CD GLN A 137 16.597 -13.665 12.989 1.00 26.43 C ANISOU 1085 CD GLN A 137 2853 3469 3717 710 -77 -130 C ATOM 1086 OE1 GLN A 137 17.140 -12.650 12.545 1.00 29.18 O ANISOU 1086 OE1 GLN A 137 3074 4087 3923 637 -35 -257 O ATOM 1087 NE2 GLN A 137 16.400 -14.749 12.253 1.00 25.71 N ANISOU 1087 NE2 GLN A 137 2655 3419 3692 341 -364 -463 N ATOM 1088 N GLY A 138 16.906 -11.489 17.558 1.00 14.99 N ANISOU 1088 N GLY A 138 706 2526 2464 74 -35 506 N ATOM 1089 CA GLY A 138 17.921 -11.503 18.598 1.00 16.21 C ANISOU 1089 CA GLY A 138 948 2732 2477 294 -367 464 C ATOM 1090 C GLY A 138 19.300 -11.978 18.160 1.00 18.67 C ANISOU 1090 C GLY A 138 1156 3239 2699 664 -117 293 C ATOM 1091 O GLY A 138 20.172 -12.210 18.996 1.00 22.77 O ANISOU 1091 O GLY A 138 1768 3976 2908 1110 23 -19 O ATOM 1092 N LYS A 139 19.512 -12.118 16.855 1.00 17.98 N ANISOU 1092 N LYS A 139 1091 3075 2663 873 183 60 N ATOM 1093 CA LYS A 139 20.808 -12.566 16.335 1.00 21.91 C ANISOU 1093 CA LYS A 139 1710 3481 3133 824 256 -87 C ATOM 1094 C LYS A 139 21.691 -11.401 15.897 1.00 20.91 C ANISOU 1094 C LYS A 139 1325 3518 3102 302 362 -284 C ATOM 1095 O LYS A 139 22.867 -11.324 16.263 1.00 20.31 O ANISOU 1095 O LYS A 139 1174 3341 3200 -16 77 -156 O ATOM 1096 CB LYS A 139 20.613 -13.532 15.163 1.00 24.67 C ANISOU 1096 CB LYS A 139 2354 3470 3547 1173 318 0 C ATOM 1097 CG LYS A 139 19.856 -14.786 15.525 1.00 27.06 C ANISOU 1097 CG LYS A 139 3149 3259 3874 1484 305 -208 C ATOM 1098 CD LYS A 139 19.647 -15.677 14.317 1.00 30.96 C ANISOU 1098 CD LYS A 139 4097 3429 4237 1730 470 -252 C ATOM 1099 CE LYS A 139 19.146 -17.048 14.744 1.00 36.26 C ANISOU 1099 CE LYS A 139 5328 3949 4498 1063 600 -364 C ATOM 1100 NZ LYS A 139 19.288 -18.053 13.652 1.00 41.73 N ANISOU 1100 NZ LYS A 139 6526 4655 4673 730 496 -306 N ATOM 1101 N LYS A 140 21.127 -10.503 15.098 1.00 21.82 N ANISOU 1101 N LYS A 140 1806 3357 3127 93 447 -213 N ATOM 1102 CA LYS A 140 21.882 -9.377 14.549 1.00 22.51 C ANISOU 1102 CA LYS A 140 1468 3841 3242 -408 199 -107 C ATOM 1103 C LYS A 140 21.771 -8.174 15.474 1.00 20.64 C ANISOU 1103 C LYS A 140 844 3850 3145 -773 276 -192 C ATOM 1104 O LYS A 140 22.530 -7.209 15.361 1.00 23.01 O ANISOU 1104 O LYS A 140 1388 4193 3160 -909 594 -413 O ATOM 1105 CB LYS A 140 21.327 -8.997 13.177 1.00 24.28 C ANISOU 1105 CB LYS A 140 1768 4036 3419 -352 326 194 C ATOM 1106 CG LYS A 140 21.457 -10.078 12.130 1.00 28.04 C ANISOU 1106 CG LYS A 140 2359 4589 3703 259 276 168 C ATOM 1107 CD LYS A 140 20.636 -9.731 10.899 1.00 33.00 C ANISOU 1107 CD LYS A 140 3596 4920 4022 786 517 92 C ATOM 1108 CE LYS A 140 21.218 -10.364 9.651 1.00 36.79 C ANISOU 1108 CE LYS A 140 4460 5041 4476 905 886 124 C ATOM 1109 NZ LYS A 140 22.522 -9.733 9.307 1.00 40.76 N ANISOU 1109 NZ LYS A 140 5653 5071 4760 703 730 269 N ATOM 1110 N ASP A 141 20.803 -8.230 16.380 1.00 20.76 N ANISOU 1110 N ASP A 141 1217 3631 3039 -42 417 157 N ATOM 1111 CA ASP A 141 20.517 -7.113 17.258 1.00 19.80 C ANISOU 1111 CA ASP A 141 1214 3382 2927 -9 337 210 C ATOM 1112 C ASP A 141 19.595 -7.613 18.359 1.00 17.40 C ANISOU 1112 C ASP A 141 1253 2850 2508 -96 188 -132 C ATOM 1113 O ASP A 141 19.143 -8.755 18.325 1.00 16.27 O ANISOU 1113 O ASP A 141 1322 2581 2278 -218 158 -437 O ATOM 1114 CB ASP A 141 19.834 -5.999 16.460 1.00 24.53 C ANISOU 1114 CB ASP A 141 2268 3785 3267 -276 492 625 C ATOM 1115 CG ASP A 141 19.999 -4.628 17.095 1.00 30.74 C ANISOU 1115 CG ASP A 141 3542 4336 3799 -932 476 1016 C ATOM 1116 OD1 ASP A 141 20.480 -4.551 18.247 1.00 33.86 O ANISOU 1116 OD1 ASP A 141 4388 4535 3942 -1408 887 1002 O ATOM 1117 OD2 ASP A 141 19.648 -3.623 16.434 1.00 32.40 O ANISOU 1117 OD2 ASP A 141 3815 4479 4014 -777 279 1106 O ATOM 1118 N THR A 142 19.308 -6.752 19.327 1.00 15.87 N ANISOU 1118 N THR A 142 1177 2749 2103 -390 7 -142 N ATOM 1119 CA THR A 142 18.411 -7.113 20.415 1.00 14.19 C ANISOU 1119 CA THR A 142 1036 2225 2129 -225 12 -127 C ATOM 1120 C THR A 142 17.897 -5.859 21.120 1.00 15.63 C ANISOU 1120 C THR A 142 1465 2206 2268 -284 2 -65 C ATOM 1121 O THR A 142 18.159 -4.730 20.673 1.00 19.02 O ANISOU 1121 O THR A 142 2044 2639 2544 -256 140 -42 O ATOM 1122 CB THR A 142 19.089 -8.098 21.406 1.00 15.88 C ANISOU 1122 CB THR A 142 1232 2442 2358 -441 -10 -28 C ATOM 1123 OG1 THR A 142 18.110 -8.645 22.301 1.00 16.58 O ANISOU 1123 OG1 THR A 142 1289 2473 2537 -412 159 -63 O ATOM 1124 CG2 THR A 142 20.208 -7.416 22.199 1.00 15.08 C ANISOU 1124 CG2 THR A 142 1318 2245 2166 -230 -397 -60 C ATOM 1125 N GLY A 143 17.167 -6.060 22.211 1.00 14.07 N ANISOU 1125 N GLY A 143 1019 2186 2138 -288 -171 -174 N ATOM 1126 CA GLY A 143 16.521 -4.973 22.928 1.00 13.06 C ANISOU 1126 CA GLY A 143 958 1849 2154 -106 37 -169 C ATOM 1127 C GLY A 143 15.661 -5.559 24.028 1.00 11.42 C ANISOU 1127 C GLY A 143 730 1453 2153 -115 75 -299 C ATOM 1128 O GLY A 143 15.501 -6.782 24.093 1.00 12.74 O ANISOU 1128 O GLY A 143 1152 1476 2213 -142 -147 -400 O ATOM 1129 N TRP A 144 15.087 -4.713 24.883 1.00 12.03 N ANISOU 1129 N TRP A 144 728 1699 2144 -6 158 -180 N ATOM 1130 CA TRP A 144 14.290 -5.232 25.988 1.00 10.73 C ANISOU 1130 CA TRP A 144 679 1369 2029 -296 123 -568 C ATOM 1131 C TRP A 144 13.087 -6.018 25.450 1.00 10.55 C ANISOU 1131 C TRP A 144 632 1416 1958 -130 -57 -346 C ATOM 1132 O TRP A 144 12.761 -7.092 25.962 1.00 11.19 O ANISOU 1132 O TRP A 144 1049 1277 1923 38 -144 -61 O ATOM 1133 CB TRP A 144 13.868 -4.120 26.961 1.00 11.68 C ANISOU 1133 CB TRP A 144 714 1290 2434 184 -80 -326 C ATOM 1134 CG TRP A 144 12.656 -3.369 26.538 1.00 15.03 C ANISOU 1134 CG TRP A 144 1323 1330 3058 496 -307 -581 C ATOM 1135 CD1 TRP A 144 12.621 -2.172 25.883 1.00 19.12 C ANISOU 1135 CD1 TRP A 144 1961 2045 3258 1023 -568 -632 C ATOM 1136 CD2 TRP A 144 11.292 -3.764 26.728 1.00 17.06 C ANISOU 1136 CD2 TRP A 144 1475 1482 3525 179 -347 -1149 C ATOM 1137 NE1 TRP A 144 11.319 -1.793 25.661 1.00 22.01 N ANISOU 1137 NE1 TRP A 144 2153 2622 3588 557 -586 -707 N ATOM 1138 CE2 TRP A 144 10.482 -2.756 26.171 1.00 20.76 C ANISOU 1138 CE2 TRP A 144 1851 2276 3761 -17 -494 -1099 C ATOM 1139 CE3 TRP A 144 10.677 -4.869 27.330 1.00 18.94 C ANISOU 1139 CE3 TRP A 144 1290 2011 3893 -193 -301 -1351 C ATOM 1140 CZ2 TRP A 144 9.090 -2.820 26.181 1.00 22.71 C ANISOU 1140 CZ2 TRP A 144 1774 2756 4096 -1 -203 -1160 C ATOM 1141 CZ3 TRP A 144 9.294 -4.935 27.344 1.00 21.75 C ANISOU 1141 CZ3 TRP A 144 1649 2412 4201 135 -239 -1290 C ATOM 1142 CH2 TRP A 144 8.515 -3.916 26.771 1.00 23.00 C ANISOU 1142 CH2 TRP A 144 1892 2672 4172 291 -324 -1349 C ATOM 1143 N LEU A 145 12.448 -5.510 24.396 1.00 11.12 N ANISOU 1143 N LEU A 145 655 1727 1842 194 -420 -639 N ATOM 1144 CA LEU A 145 11.274 -6.201 23.846 1.00 12.54 C ANISOU 1144 CA LEU A 145 976 1628 2160 172 -487 -163 C ATOM 1145 C LEU A 145 11.633 -7.572 23.255 1.00 10.50 C ANISOU 1145 C LEU A 145 629 1108 2252 -64 -65 -42 C ATOM 1146 O LEU A 145 10.898 -8.537 23.398 1.00 11.45 O ANISOU 1146 O LEU A 145 718 1124 2508 -152 -194 -2 O ATOM 1147 CB LEU A 145 10.560 -5.349 22.798 1.00 13.19 C ANISOU 1147 CB LEU A 145 653 1674 2683 282 -685 119 C ATOM 1148 CG LEU A 145 9.292 -5.990 22.236 1.00 14.47 C ANISOU 1148 CG LEU A 145 569 1999 2930 318 -631 56 C ATOM 1149 CD1 LEU A 145 8.220 -6.109 23.323 1.00 16.43 C ANISOU 1149 CD1 LEU A 145 909 2278 3053 237 -120 -510 C ATOM 1150 CD2 LEU A 145 8.780 -5.146 21.092 1.00 16.40 C ANISOU 1150 CD2 LEU A 145 1066 1990 3173 248 -992 171 C ATOM 1151 N SER A 146 12.781 -7.650 22.593 1.00 11.21 N ANISOU 1151 N SER A 146 1037 1412 1807 114 -70 0 N ATOM 1152 CA SER A 146 13.274 -8.915 22.075 1.00 9.96 C ANISOU 1152 CA SER A 146 947 1109 1726 -143 24 90 C ATOM 1153 C SER A 146 13.395 -9.963 23.177 1.00 9.93 C ANISOU 1153 C SER A 146 1004 1277 1489 -277 33 24 C ATOM 1154 O SER A 146 12.963 -11.104 23.011 1.00 10.77 O ANISOU 1154 O SER A 146 1007 1606 1479 -328 57 -17 O ATOM 1155 CB SER A 146 14.650 -8.710 21.439 1.00 11.41 C ANISOU 1155 CB SER A 146 974 1438 1923 65 466 -83 C ATOM 1156 OG SER A 146 15.176 -9.935 20.952 1.00 12.21 O ANISOU 1156 OG SER A 146 1249 1482 1905 23 164 -254 O ATOM 1157 N VAL A 147 14.004 -9.587 24.299 1.00 10.58 N ANISOU 1157 N VAL A 147 946 1436 1635 -65 42 -192 N ATOM 1158 CA VAL A 147 14.171 -10.540 25.402 1.00 9.81 C ANISOU 1158 CA VAL A 147 711 1323 1691 -71 -295 -274 C ATOM 1159 C VAL A 147 12.819 -10.895 26.034 1.00 10.94 C ANISOU 1159 C VAL A 147 935 1249 1973 528 -90 -373 C ATOM 1160 O VAL A 147 12.549 -12.060 26.317 1.00 12.69 O ANISOU 1160 O VAL A 147 1169 1431 2220 358 -28 -567 O ATOM 1161 CB VAL A 147 15.158 -10.016 26.470 1.00 9.79 C ANISOU 1161 CB VAL A 147 727 1359 1632 38 -285 -233 C ATOM 1162 CG1 VAL A 147 15.215 -10.962 27.681 1.00 12.12 C ANISOU 1162 CG1 VAL A 147 1395 1887 1321 382 -515 146 C ATOM 1163 CG2 VAL A 147 16.554 -9.819 25.863 1.00 10.70 C ANISOU 1163 CG2 VAL A 147 881 1363 1819 136 88 -400 C ATOM 1164 N PHE A 148 11.971 -9.888 26.235 1.00 10.70 N ANISOU 1164 N PHE A 148 761 1375 1930 354 -77 -458 N ATOM 1165 CA PHE A 148 10.622 -10.092 26.760 1.00 11.56 C ANISOU 1165 CA PHE A 148 755 1502 2135 307 72 -346 C ATOM 1166 C PHE A 148 9.870 -11.101 25.897 1.00 12.46 C ANISOU 1166 C PHE A 148 824 1802 2106 77 -178 -342 C ATOM 1167 O PHE A 148 9.313 -12.073 26.417 1.00 12.49 O ANISOU 1167 O PHE A 148 1279 1398 2068 -152 -11 -182 O ATOM 1168 CB PHE A 148 9.892 -8.743 26.776 1.00 12.21 C ANISOU 1168 CB PHE A 148 799 1682 2155 551 285 -409 C ATOM 1169 CG PHE A 148 8.592 -8.731 27.536 1.00 13.41 C ANISOU 1169 CG PHE A 148 1262 1514 2318 37 312 -80 C ATOM 1170 CD1 PHE A 148 8.562 -8.959 28.903 1.00 14.58 C ANISOU 1170 CD1 PHE A 148 1343 1738 2458 179 420 86 C ATOM 1171 CD2 PHE A 148 7.399 -8.418 26.884 1.00 13.29 C ANISOU 1171 CD2 PHE A 148 1006 1837 2205 -368 61 53 C ATOM 1172 CE1 PHE A 148 7.362 -8.901 29.605 1.00 16.06 C ANISOU 1172 CE1 PHE A 148 1668 2088 2345 156 98 37 C ATOM 1173 CE2 PHE A 148 6.203 -8.357 27.577 1.00 15.23 C ANISOU 1173 CE2 PHE A 148 1441 1987 2359 -126 -304 -27 C ATOM 1174 CZ PHE A 148 6.178 -8.603 28.938 1.00 13.42 C ANISOU 1174 CZ PHE A 148 1344 1486 2266 84 51 -144 C ATOM 1175 N VAL A 149 9.865 -10.873 24.583 1.00 9.78 N ANISOU 1175 N VAL A 149 779 1125 1811 210 -301 -567 N ATOM 1176 CA VAL A 149 9.182 -11.765 23.642 1.00 8.69 C ANISOU 1176 CA VAL A 149 753 762 1785 151 -331 7 C ATOM 1177 C VAL A 149 9.792 -13.171 23.645 1.00 9.53 C ANISOU 1177 C VAL A 149 707 1187 1727 459 -65 74 C ATOM 1178 O VAL A 149 9.075 -14.171 23.726 1.00 11.02 O ANISOU 1178 O VAL A 149 1160 1155 1872 38 -467 276 O ATOM 1179 CB VAL A 149 9.210 -11.193 22.193 1.00 10.05 C ANISOU 1179 CB VAL A 149 1273 629 1917 187 -356 140 C ATOM 1180 CG1 VAL A 149 8.744 -12.224 21.164 1.00 11.37 C ANISOU 1180 CG1 VAL A 149 1363 952 2003 -187 -90 217 C ATOM 1181 CG2 VAL A 149 8.347 -9.933 22.084 1.00 12.36 C ANISOU 1181 CG2 VAL A 149 1173 1081 2440 63 -519 -126 C ATOM 1182 N ARG A 150 11.117 -13.254 23.529 1.00 10.15 N ANISOU 1182 N ARG A 150 933 1326 1595 693 -67 -176 N ATOM 1183 CA ARG A 150 11.763 -14.556 23.381 1.00 10.94 C ANISOU 1183 CA ARG A 150 834 1660 1660 460 -41 -189 C ATOM 1184 C ARG A 150 11.771 -15.402 24.646 1.00 9.44 C ANISOU 1184 C ARG A 150 649 1222 1713 137 -156 -312 C ATOM 1185 O ARG A 150 12.026 -16.601 24.588 1.00 11.23 O ANISOU 1185 O ARG A 150 1221 1238 1808 525 -237 -129 O ATOM 1186 CB ARG A 150 13.167 -14.404 22.802 1.00 11.62 C ANISOU 1186 CB ARG A 150 902 1849 1664 312 446 8 C ATOM 1187 CG ARG A 150 13.147 -14.121 21.310 1.00 11.76 C ANISOU 1187 CG ARG A 150 1076 1858 1532 -24 -22 -48 C ATOM 1188 CD ARG A 150 14.544 -14.010 20.708 1.00 12.81 C ANISOU 1188 CD ARG A 150 1135 1932 1798 259 103 -441 C ATOM 1189 NE ARG A 150 15.246 -12.825 21.188 1.00 13.26 N ANISOU 1189 NE ARG A 150 1239 1911 1888 56 -217 -183 N ATOM 1190 CZ ARG A 150 16.312 -12.861 21.978 1.00 14.30 C ANISOU 1190 CZ ARG A 150 1786 1661 1985 319 -254 -11 C ATOM 1191 NH1 ARG A 150 16.817 -14.037 22.362 1.00 18.02 N ANISOU 1191 NH1 ARG A 150 2271 2552 2021 598 27 228 N ATOM 1192 NH2 ARG A 150 16.880 -11.725 22.371 1.00 14.78 N ANISOU 1192 NH2 ARG A 150 1789 1645 2180 29 -61 -146 N ATOM 1193 N THR A 151 11.474 -14.790 25.785 1.00 9.97 N ANISOU 1193 N THR A 151 1064 1040 1681 -64 -142 -143 N ATOM 1194 CA THR A 151 11.279 -15.551 27.010 1.00 10.47 C ANISOU 1194 CA THR A 151 1443 916 1617 -46 -392 -382 C ATOM 1195 C THR A 151 10.064 -16.465 26.868 1.00 11.11 C ANISOU 1195 C THR A 151 1574 1100 1544 190 -361 -269 C ATOM 1196 O THR A 151 10.022 -17.543 27.475 1.00 11.13 O ANISOU 1196 O THR A 151 1447 945 1834 69 -392 -45 O ATOM 1197 CB THR A 151 11.095 -14.603 28.226 1.00 10.74 C ANISOU 1197 CB THR A 151 1400 1105 1573 -377 -99 -217 C ATOM 1198 OG1 THR A 151 12.251 -13.777 28.343 1.00 12.07 O ANISOU 1198 OG1 THR A 151 1660 1259 1667 -63 -384 -216 O ATOM 1199 CG2 THR A 151 10.924 -15.382 29.541 1.00 13.44 C ANISOU 1199 CG2 THR A 151 1709 1812 1583 -289 -128 -42 C ATOM 1200 N PHE A 152 9.092 -16.031 26.062 1.00 9.55 N ANISOU 1200 N PHE A 152 1061 1293 1275 79 46 -334 N ATOM 1201 CA PHE A 152 7.823 -16.744 25.921 1.00 9.39 C ANISOU 1201 CA PHE A 152 1040 1358 1168 188 28 -415 C ATOM 1202 C PHE A 152 7.495 -17.279 24.521 1.00 9.97 C ANISOU 1202 C PHE A 152 1028 1215 1543 38 -380 -358 C ATOM 1203 O PHE A 152 6.565 -18.080 24.374 1.00 11.66 O ANISOU 1203 O PHE A 152 1081 1415 1932 -179 -88 -257 O ATOM 1204 CB PHE A 152 6.691 -15.844 26.401 1.00 10.31 C ANISOU 1204 CB PHE A 152 1177 1221 1517 147 -77 -510 C ATOM 1205 CG PHE A 152 6.937 -15.260 27.760 1.00 11.73 C ANISOU 1205 CG PHE A 152 1578 1605 1271 229 80 -384 C ATOM 1206 CD1 PHE A 152 6.813 -16.047 28.901 1.00 13.35 C ANISOU 1206 CD1 PHE A 152 1988 2027 1055 255 240 -209 C ATOM 1207 CD2 PHE A 152 7.317 -13.934 27.904 1.00 12.22 C ANISOU 1207 CD2 PHE A 152 1267 1874 1500 471 6 -380 C ATOM 1208 CE1 PHE A 152 7.040 -15.509 30.162 1.00 14.45 C ANISOU 1208 CE1 PHE A 152 2203 1939 1348 -240 358 -235 C ATOM 1209 CE2 PHE A 152 7.548 -13.396 29.163 1.00 14.18 C ANISOU 1209 CE2 PHE A 152 1669 2175 1542 502 266 -274 C ATOM 1210 CZ PHE A 152 7.413 -14.180 30.286 1.00 15.23 C ANISOU 1210 CZ PHE A 152 1998 2273 1513 85 -76 -541 C ATOM 1211 N TYR A 153 8.228 -16.815 23.506 1.00 10.38 N ANISOU 1211 N TYR A 153 1235 1169 1538 292 -135 -173 N ATOM 1212 CA TYR A 153 7.992 -17.202 22.114 1.00 9.72 C ANISOU 1212 CA TYR A 153 807 1321 1565 283 -207 71 C ATOM 1213 C TYR A 153 9.295 -17.518 21.415 1.00 9.58 C ANISOU 1213 C TYR A 153 833 1346 1460 55 -244 -118 C ATOM 1214 O TYR A 153 10.332 -16.961 21.747 1.00 10.48 O ANISOU 1214 O TYR A 153 987 1440 1555 -126 -215 -475 O ATOM 1215 CB TYR A 153 7.315 -16.066 21.329 1.00 9.87 C ANISOU 1215 CB TYR A 153 863 1129 1756 -1 -72 126 C ATOM 1216 CG TYR A 153 5.877 -15.872 21.720 1.00 8.41 C ANISOU 1216 CG TYR A 153 527 1145 1522 453 211 14 C ATOM 1217 CD1 TYR A 153 5.532 -15.042 22.773 1.00 9.53 C ANISOU 1217 CD1 TYR A 153 1080 1208 1332 634 106 -52 C ATOM 1218 CD2 TYR A 153 4.865 -16.562 21.069 1.00 10.88 C ANISOU 1218 CD2 TYR A 153 740 1699 1692 -171 81 -78 C ATOM 1219 CE1 TYR A 153 4.217 -14.885 23.151 1.00 11.26 C ANISOU 1219 CE1 TYR A 153 1120 1743 1412 165 -211 -186 C ATOM 1220 CE2 TYR A 153 3.541 -16.420 21.440 1.00 11.02 C ANISOU 1220 CE2 TYR A 153 926 1596 1664 243 102 -191 C ATOM 1221 CZ TYR A 153 3.223 -15.578 22.487 1.00 10.65 C ANISOU 1221 CZ TYR A 153 746 1822 1478 241 -104 -365 C ATOM 1222 OH TYR A 153 1.918 -15.414 22.880 1.00 12.43 O ANISOU 1222 OH TYR A 153 862 2224 1635 347 -60 -369 O ATOM 1223 N ASP A 154 9.219 -18.397 20.420 1.00 10.21 N ANISOU 1223 N ASP A 154 965 1394 1518 388 -202 -428 N ATOM 1224 CA ASP A 154 10.281 -18.525 19.436 1.00 11.28 C ANISOU 1224 CA ASP A 154 936 1501 1847 516 -47 -354 C ATOM 1225 C ASP A 154 9.963 -17.561 18.307 1.00 12.81 C ANISOU 1225 C ASP A 154 907 1882 2078 27 -287 -73 C ATOM 1226 O ASP A 154 8.803 -17.415 17.912 1.00 14.55 O ANISOU 1226 O ASP A 154 869 2249 2409 -226 -229 579 O ATOM 1227 CB ASP A 154 10.364 -19.951 18.896 1.00 14.52 C ANISOU 1227 CB ASP A 154 1842 1571 2102 865 348 -269 C ATOM 1228 CG ASP A 154 11.010 -20.902 19.871 1.00 18.80 C ANISOU 1228 CG ASP A 154 2602 1907 2632 885 333 -366 C ATOM 1229 OD1 ASP A 154 11.693 -20.429 20.807 1.00 21.02 O ANISOU 1229 OD1 ASP A 154 2987 2419 2580 607 109 -16 O ATOM 1230 OD2 ASP A 154 10.844 -22.127 19.693 1.00 23.47 O ANISOU 1230 OD2 ASP A 154 3634 2190 3091 242 18 -24 O ATOM 1231 N VAL A 155 10.989 -16.876 17.823 1.00 13.36 N ANISOU 1231 N VAL A 155 1203 1734 2139 -274 185 134 N ATOM 1232 CA VAL A 155 10.827 -15.857 16.796 1.00 13.69 C ANISOU 1232 CA VAL A 155 1012 1840 2347 -13 184 241 C ATOM 1233 C VAL A 155 11.453 -16.329 15.498 1.00 16.21 C ANISOU 1233 C VAL A 155 1207 2418 2531 425 125 303 C ATOM 1234 O VAL A 155 12.650 -16.600 15.430 1.00 20.23 O ANISOU 1234 O VAL A 155 1468 3452 2766 427 -31 428 O ATOM 1235 CB VAL A 155 11.445 -14.507 17.230 1.00 15.43 C ANISOU 1235 CB VAL A 155 1665 1796 2399 -508 -148 250 C ATOM 1236 CG1 VAL A 155 11.361 -13.481 16.099 1.00 18.68 C ANISOU 1236 CG1 VAL A 155 2051 2406 2640 -428 -150 275 C ATOM 1237 CG2 VAL A 155 10.761 -13.985 18.484 1.00 15.67 C ANISOU 1237 CG2 VAL A 155 1818 1857 2277 36 -448 304 C ATOM 1238 N ASN A 156 10.623 -16.426 14.471 1.00 15.01 N ANISOU 1238 N ASN A 156 1244 1980 2478 584 570 54 N ATOM 1239 CA ASN A 156 11.037 -16.913 13.170 1.00 18.59 C ANISOU 1239 CA ASN A 156 2006 2421 2636 399 355 338 C ATOM 1240 C ASN A 156 11.004 -15.757 12.184 1.00 17.15 C ANISOU 1240 C ASN A 156 1524 2519 2473 205 553 614 C ATOM 1241 O ASN A 156 9.980 -15.099 12.044 1.00 18.72 O ANISOU 1241 O ASN A 156 1546 2762 2805 739 705 503 O ATOM 1242 CB ASN A 156 10.074 -18.017 12.719 1.00 22.90 C ANISOU 1242 CB ASN A 156 3150 2502 3048 526 119 170 C ATOM 1243 CG ASN A 156 10.053 -19.205 13.670 1.00 30.44 C ANISOU 1243 CG ASN A 156 4051 3515 4000 751 207 -34 C ATOM 1244 OD1 ASN A 156 10.915 -20.078 13.597 1.00 35.30 O ANISOU 1244 OD1 ASN A 156 4884 4186 4341 880 -56 264 O ATOM 1245 ND2 ASN A 156 9.058 -19.248 14.564 1.00 30.88 N ANISOU 1245 ND2 ASN A 156 3668 3618 4447 293 -92 -225 N ATOM 1246 N TYR A 157 12.127 -15.488 11.526 1.00 18.31 N ANISOU 1246 N TYR A 157 1815 2708 2433 110 877 1194 N ATOM 1247 CA TYR A 157 12.184 -14.440 10.511 1.00 20.39 C ANISOU 1247 CA TYR A 157 1861 2942 2943 554 813 841 C ATOM 1248 C TYR A 157 11.776 -15.068 9.184 1.00 20.02 C ANISOU 1248 C TYR A 157 2259 2674 2673 1215 1167 347 C ATOM 1249 O TYR A 157 12.503 -15.887 8.628 1.00 25.05 O ANISOU 1249 O TYR A 157 3044 3627 2846 1561 1476 236 O ATOM 1250 CB TYR A 157 13.595 -13.852 10.432 1.00 23.01 C ANISOU 1250 CB TYR A 157 1998 3283 3461 151 1083 1081 C ATOM 1251 CG TYR A 157 13.736 -12.621 9.560 1.00 26.11 C ANISOU 1251 CG TYR A 157 2292 3565 4061 477 1237 1053 C ATOM 1252 CD1 TYR A 157 13.860 -12.731 8.179 1.00 27.59 C ANISOU 1252 CD1 TYR A 157 2644 3621 4216 656 1412 1356 C ATOM 1253 CD2 TYR A 157 13.787 -11.350 10.120 1.00 26.72 C ANISOU 1253 CD2 TYR A 157 1970 3837 4343 683 1388 974 C ATOM 1254 CE1 TYR A 157 14.003 -11.607 7.378 1.00 27.98 C ANISOU 1254 CE1 TYR A 157 2401 3725 4502 638 1556 1321 C ATOM 1255 CE2 TYR A 157 13.934 -10.219 9.325 1.00 26.10 C ANISOU 1255 CE2 TYR A 157 1685 3709 4522 603 1300 1223 C ATOM 1256 CZ TYR A 157 14.043 -10.356 7.955 1.00 26.11 C ANISOU 1256 CZ TYR A 157 1925 3401 4594 589 1597 1475 C ATOM 1257 OH TYR A 157 14.193 -9.242 7.153 1.00 28.69 O ANISOU 1257 OH TYR A 157 2513 3515 4873 223 1554 1431 O ATOM 1258 N VAL A 158 10.599 -14.695 8.693 1.00 16.85 N ANISOU 1258 N VAL A 158 1914 2063 2423 778 753 -50 N ATOM 1259 CA VAL A 158 9.999 -15.373 7.545 1.00 20.46 C ANISOU 1259 CA VAL A 158 3066 2414 2291 779 1171 -30 C ATOM 1260 C VAL A 158 10.526 -14.854 6.214 1.00 22.64 C ANISOU 1260 C VAL A 158 3712 2439 2450 1229 1487 54 C ATOM 1261 O VAL A 158 10.987 -15.624 5.362 1.00 26.32 O ANISOU 1261 O VAL A 158 4690 2791 2517 1321 1775 164 O ATOM 1262 CB VAL A 158 8.457 -15.247 7.564 1.00 19.95 C ANISOU 1262 CB VAL A 158 3139 2326 2113 86 1016 20 C ATOM 1263 CG1 VAL A 158 7.852 -15.890 6.311 1.00 20.44 C ANISOU 1263 CG1 VAL A 158 3473 2102 2191 -314 643 57 C ATOM 1264 CG2 VAL A 158 7.891 -15.880 8.846 1.00 20.19 C ANISOU 1264 CG2 VAL A 158 3483 2071 2116 179 1122 35 C ATOM 1265 N MET A 159 10.463 -13.543 6.036 1.00 20.81 N ANISOU 1265 N MET A 159 3232 2170 2503 687 1474 605 N ATOM 1266 CA MET A 159 10.893 -12.944 4.787 1.00 21.64 C ANISOU 1266 CA MET A 159 3072 2468 2680 776 1441 643 C ATOM 1267 C MET A 159 11.093 -11.443 4.923 1.00 20.97 C ANISOU 1267 C MET A 159 2441 2704 2823 471 1750 620 C ATOM 1268 O MET A 159 10.495 -10.791 5.786 1.00 20.02 O ANISOU 1268 O MET A 159 2426 2721 2460 1011 1582 369 O ATOM 1269 CB MET A 159 9.875 -13.232 3.682 1.00 26.15 C ANISOU 1269 CB MET A 159 4208 3002 2723 38 915 232 C ATOM 1270 CG MET A 159 8.485 -12.671 3.946 1.00 31.36 C ANISOU 1270 CG MET A 159 5316 3769 2828 -154 107 -284 C ATOM 1271 SD MET A 159 7.365 -12.885 2.548 1.00 39.13 S ANISOU 1271 SD MET A 159 6838 4716 3313 -609 -431 -130 S ATOM 1272 CE MET A 159 8.075 -11.727 1.385 1.00 41.36 C ANISOU 1272 CE MET A 159 7081 5111 3523 -85 -18 -376 C ATOM 1273 N THR A 160 11.936 -10.906 4.052 1.00 24.04 N ANISOU 1273 N THR A 160 2837 3143 3153 653 1719 1026 N ATOM 1274 CA THR A 160 12.113 -9.470 3.940 1.00 24.36 C ANISOU 1274 CA THR A 160 2775 3027 3453 453 1488 883 C ATOM 1275 C THR A 160 11.098 -8.950 2.939 1.00 23.49 C ANISOU 1275 C THR A 160 3160 2643 3122 603 1192 732 C ATOM 1276 O THR A 160 10.762 -9.648 1.973 1.00 23.45 O ANISOU 1276 O THR A 160 3578 2156 3176 754 1241 552 O ATOM 1277 CB THR A 160 13.542 -9.122 3.473 1.00 27.43 C ANISOU 1277 CB THR A 160 2617 3886 3918 398 1395 802 C ATOM 1278 OG1 THR A 160 14.477 -9.570 4.458 1.00 28.77 O ANISOU 1278 OG1 THR A 160 2458 4270 4202 733 1314 908 O ATOM 1279 CG2 THR A 160 13.705 -7.616 3.271 1.00 28.38 C ANISOU 1279 CG2 THR A 160 2578 4213 3992 85 1514 691 C ATOM 1280 N VAL A 161 10.593 -7.742 3.185 1.00 18.96 N ANISOU 1280 N VAL A 161 2751 1758 2695 603 1005 1064 N ATOM 1281 CA VAL A 161 9.627 -7.106 2.296 1.00 18.84 C ANISOU 1281 CA VAL A 161 2794 1842 2521 670 1297 611 C ATOM 1282 C VAL A 161 10.103 -5.710 1.904 1.00 18.41 C ANISOU 1282 C VAL A 161 2640 1878 2474 261 1202 415 C ATOM 1283 O VAL A 161 9.977 -4.763 2.677 1.00 18.45 O ANISOU 1283 O VAL A 161 2700 1831 2478 443 756 101 O ATOM 1284 CB VAL A 161 8.226 -6.996 2.959 1.00 18.59 C ANISOU 1284 CB VAL A 161 2760 1944 2359 396 924 576 C ATOM 1285 CG1 VAL A 161 7.202 -6.451 1.965 1.00 20.44 C ANISOU 1285 CG1 VAL A 161 3095 2159 2510 306 492 79 C ATOM 1286 CG2 VAL A 161 7.784 -8.345 3.503 1.00 18.50 C ANISOU 1286 CG2 VAL A 161 2937 1946 2144 136 689 336 C ATOM 1287 N PRO A 162 10.656 -5.577 0.696 1.00 19.40 N ANISOU 1287 N PRO A 162 2786 1887 2695 326 1060 716 N ATOM 1288 CA PRO A 162 11.175 -4.282 0.246 1.00 19.50 C ANISOU 1288 CA PRO A 162 2535 1896 2975 -37 1234 619 C ATOM 1289 C PRO A 162 10.075 -3.234 0.166 1.00 19.82 C ANISOU 1289 C PRO A 162 2511 1954 3064 -56 1318 438 C ATOM 1290 O PRO A 162 8.908 -3.586 0.020 1.00 21.27 O ANISOU 1290 O PRO A 162 2726 2171 3183 -158 1423 63 O ATOM 1291 CB PRO A 162 11.688 -4.582 -1.163 1.00 22.23 C ANISOU 1291 CB PRO A 162 3018 2343 3084 404 1617 430 C ATOM 1292 CG PRO A 162 11.917 -6.025 -1.196 1.00 24.73 C ANISOU 1292 CG PRO A 162 4182 2104 3108 -248 1342 419 C ATOM 1293 CD PRO A 162 10.921 -6.650 -0.275 1.00 22.17 C ANISOU 1293 CD PRO A 162 3582 2038 2804 -254 1490 504 C ATOM 1294 N PRO A 163 10.445 -1.951 0.234 1.00 20.26 N ANISOU 1294 N PRO A 163 2215 2375 3108 -300 738 440 N ATOM 1295 CA PRO A 163 9.438 -0.884 0.231 1.00 21.38 C ANISOU 1295 CA PRO A 163 2487 2560 3076 -275 904 355 C ATOM 1296 C PRO A 163 8.468 -0.940 -0.951 1.00 21.73 C ANISOU 1296 C PRO A 163 2991 2601 2662 2 978 509 C ATOM 1297 O PRO A 163 7.327 -0.517 -0.801 1.00 21.87 O ANISOU 1297 O PRO A 163 2814 2789 2705 245 805 230 O ATOM 1298 CB PRO A 163 10.287 0.387 0.169 1.00 22.84 C ANISOU 1298 CB PRO A 163 2703 2522 3450 -899 541 297 C ATOM 1299 CG PRO A 163 11.572 -0.006 0.832 1.00 23.31 C ANISOU 1299 CG PRO A 163 2656 2658 3543 -409 211 101 C ATOM 1300 CD PRO A 163 11.809 -1.430 0.440 1.00 23.11 C ANISOU 1300 CD PRO A 163 2687 2676 3418 -141 174 376 C ATOM 1301 N ARG A 164 8.909 -1.451 -2.097 1.00 23.64 N ANISOU 1301 N ARG A 164 3965 2540 2477 -509 1149 219 N ATOM 1302 CA ARG A 164 8.098 -1.430 -3.315 1.00 28.66 C ANISOU 1302 CA ARG A 164 4844 3391 2653 -867 1261 599 C ATOM 1303 C ARG A 164 6.807 -2.233 -3.216 1.00 29.04 C ANISOU 1303 C ARG A 164 5291 3464 2276 -304 595 566 C ATOM 1304 O ARG A 164 5.905 -2.077 -4.039 1.00 30.88 O ANISOU 1304 O ARG A 164 6202 3501 2028 -399 271 1249 O ATOM 1305 CB ARG A 164 8.902 -1.956 -4.501 1.00 35.89 C ANISOU 1305 CB ARG A 164 5694 4781 3161 -1008 1494 337 C ATOM 1306 CG ARG A 164 9.880 -0.972 -5.099 1.00 43.02 C ANISOU 1306 CG ARG A 164 6741 5663 3941 -540 1434 29 C ATOM 1307 CD ARG A 164 10.691 -1.662 -6.184 1.00 48.01 C ANISOU 1307 CD ARG A 164 7468 6314 4460 -41 1603 -113 C ATOM 1308 NE ARG A 164 11.849 -0.893 -6.619 1.00 51.35 N ANISOU 1308 NE ARG A 164 7863 6760 4888 68 1588 -27 N ATOM 1309 CZ ARG A 164 12.838 -1.407 -7.345 1.00 54.46 C ANISOU 1309 CZ ARG A 164 8337 7066 5287 368 1457 -113 C ATOM 1310 NH1 ARG A 164 12.796 -2.683 -7.691 1.00 57.31 N ANISOU 1310 NH1 ARG A 164 8725 7601 5446 631 1202 -191 N ATOM 1311 NH2 ARG A 164 13.866 -0.661 -7.715 1.00 54.94 N ANISOU 1311 NH2 ARG A 164 8276 7227 5370 488 1733 96 N ATOM 1312 N PHE A 165 6.723 -3.105 -2.223 1.00 23.34 N ANISOU 1312 N PHE A 165 4412 2666 1790 -158 760 236 N ATOM 1313 CA PHE A 165 5.534 -3.926 -2.060 1.00 22.52 C ANISOU 1313 CA PHE A 165 4122 2432 2003 -186 509 66 C ATOM 1314 C PHE A 165 4.428 -3.140 -1.361 1.00 22.21 C ANISOU 1314 C PHE A 165 3833 2358 2245 136 127 21 C ATOM 1315 O PHE A 165 3.326 -3.655 -1.165 1.00 23.63 O ANISOU 1315 O PHE A 165 4066 2376 2536 -188 -612 -251 O ATOM 1316 CB PHE A 165 5.858 -5.225 -1.304 1.00 21.38 C ANISOU 1316 CB PHE A 165 3569 2587 1967 -7 618 -96 C ATOM 1317 CG PHE A 165 6.609 -6.240 -2.131 1.00 23.10 C ANISOU 1317 CG PHE A 165 3632 2788 2355 -701 1145 -551 C ATOM 1318 CD1 PHE A 165 7.988 -6.198 -2.209 1.00 24.58 C ANISOU 1318 CD1 PHE A 165 3701 3171 2466 -117 1769 -511 C ATOM 1319 CD2 PHE A 165 5.932 -7.240 -2.824 1.00 25.58 C ANISOU 1319 CD2 PHE A 165 4096 3232 2391 -190 1753 -806 C ATOM 1320 CE1 PHE A 165 8.685 -7.117 -2.967 1.00 26.08 C ANISOU 1320 CE1 PHE A 165 3894 3257 2757 -195 1881 -812 C ATOM 1321 CE2 PHE A 165 6.626 -8.172 -3.581 1.00 27.64 C ANISOU 1321 CE2 PHE A 165 4160 3584 2757 -159 1757 -753 C ATOM 1322 CZ PHE A 165 8.005 -8.110 -3.652 1.00 28.05 C ANISOU 1322 CZ PHE A 165 4269 3535 2851 -319 1572 -895 C ATOM 1323 N PHE A 166 4.734 -1.894 -0.992 1.00 18.92 N ANISOU 1323 N PHE A 166 3353 1803 2030 567 -59 67 N ATOM 1324 CA PHE A 166 3.768 -0.999 -0.360 1.00 19.00 C ANISOU 1324 CA PHE A 166 2870 2471 1875 573 -316 394 C ATOM 1325 C PHE A 166 3.579 0.286 -1.154 1.00 18.41 C ANISOU 1325 C PHE A 166 2436 2529 2029 709 156 338 C ATOM 1326 O PHE A 166 4.526 0.815 -1.736 1.00 20.98 O ANISOU 1326 O PHE A 166 2308 3197 2464 408 -100 324 O ATOM 1327 CB PHE A 166 4.235 -0.576 1.032 1.00 18.97 C ANISOU 1327 CB PHE A 166 2539 2636 2032 196 -695 443 C ATOM 1328 CG PHE A 166 4.570 -1.710 1.941 1.00 18.43 C ANISOU 1328 CG PHE A 166 2147 2478 2378 176 -381 675 C ATOM 1329 CD1 PHE A 166 3.603 -2.260 2.765 1.00 20.52 C ANISOU 1329 CD1 PHE A 166 2650 2667 2480 260 103 991 C ATOM 1330 CD2 PHE A 166 5.860 -2.211 1.996 1.00 20.24 C ANISOU 1330 CD2 PHE A 166 2457 2759 2474 128 -365 511 C ATOM 1331 CE1 PHE A 166 3.914 -3.296 3.617 1.00 21.72 C ANISOU 1331 CE1 PHE A 166 2718 2829 2705 293 46 1010 C ATOM 1332 CE2 PHE A 166 6.177 -3.238 2.848 1.00 20.08 C ANISOU 1332 CE2 PHE A 166 2489 2603 2535 -80 -106 518 C ATOM 1333 CZ PHE A 166 5.205 -3.788 3.657 1.00 19.62 C ANISOU 1333 CZ PHE A 166 2075 2724 2656 118 -6 593 C ATOM 1334 N VAL A 167 2.359 0.804 -1.147 1.00 18.07 N ANISOU 1334 N VAL A 167 2322 2613 1928 445 -375 442 N ATOM 1335 CA VAL A 167 2.129 2.188 -1.546 1.00 19.69 C ANISOU 1335 CA VAL A 167 2782 2747 1952 518 -455 142 C ATOM 1336 C VAL A 167 1.271 2.880 -0.492 1.00 19.16 C ANISOU 1336 C VAL A 167 2379 2775 2126 357 -571 -105 C ATOM 1337 O VAL A 167 0.173 2.422 -0.191 1.00 18.77 O ANISOU 1337 O VAL A 167 2554 2515 2061 22 -555 167 O ATOM 1338 CB VAL A 167 1.426 2.297 -2.894 1.00 20.86 C ANISOU 1338 CB VAL A 167 3005 2909 2012 579 -468 -21 C ATOM 1339 CG1 VAL A 167 1.435 3.747 -3.362 1.00 17.49 C ANISOU 1339 CG1 VAL A 167 2167 2465 2012 457 -603 -70 C ATOM 1340 CG2 VAL A 167 2.099 1.404 -3.910 1.00 22.37 C ANISOU 1340 CG2 VAL A 167 3533 2995 1971 486 -575 -317 C ATOM 1341 N PRO A 168 1.788 3.967 0.104 1.00 20.73 N ANISOU 1341 N PRO A 168 2878 2511 2487 -361 -184 -242 N ATOM 1342 CA PRO A 168 3.119 4.534 -0.146 1.00 21.21 C ANISOU 1342 CA PRO A 168 2640 2781 2638 -182 -249 -23 C ATOM 1343 C PRO A 168 4.221 3.636 0.410 1.00 20.75 C ANISOU 1343 C PRO A 168 2471 2623 2790 -29 38 180 C ATOM 1344 O PRO A 168 4.003 2.949 1.410 1.00 20.69 O ANISOU 1344 O PRO A 168 2634 2465 2759 281 -4 119 O ATOM 1345 CB PRO A 168 3.102 5.851 0.648 1.00 22.44 C ANISOU 1345 CB PRO A 168 2790 2826 2908 -165 -194 0 C ATOM 1346 CG PRO A 168 1.702 6.016 1.182 1.00 23.54 C ANISOU 1346 CG PRO A 168 3206 2844 2891 -269 39 -322 C ATOM 1347 CD PRO A 168 1.091 4.653 1.205 1.00 20.35 C ANISOU 1347 CD PRO A 168 2840 2230 2660 -352 124 -363 C ATOM 1348 N APRO A 169 5.387 3.615 -0.249 0.50 21.51 N ANISOU 1348 N APRO A 169 2504 2779 2888 -188 -199 365 N ATOM 1349 N BPRO A 169 5.410 3.667 -0.209 0.50 19.61 N ANISOU 1349 N BPRO A 169 2380 2338 2731 -587 -27 656 N ATOM 1350 CA APRO A 169 6.501 2.820 0.274 0.50 21.05 C ANISOU 1350 CA APRO A 169 2278 2745 2972 -92 -402 384 C ATOM 1351 CA BPRO A 169 6.521 2.835 0.261 0.50 19.33 C ANISOU 1351 CA BPRO A 169 2227 2312 2806 -513 -220 666 C ATOM 1352 C APRO A 169 7.010 3.409 1.579 0.50 21.92 C ANISOU 1352 C APRO A 169 2575 2520 3233 -153 -601 520 C ATOM 1353 C BPRO A 169 7.129 3.406 1.534 0.50 21.92 C ANISOU 1353 C BPRO A 169 2786 2373 3167 -546 -625 650 C ATOM 1354 O APRO A 169 7.035 4.633 1.725 0.50 22.47 O ANISOU 1354 O APRO A 169 2673 2388 3474 96 -572 577 O ATOM 1355 O BPRO A 169 7.351 4.615 1.610 0.50 24.06 O ANISOU 1355 O BPRO A 169 3267 2419 3456 -847 -783 630 O ATOM 1356 CB APRO A 169 7.577 2.963 -0.808 0.50 22.74 C ANISOU 1356 CB APRO A 169 2736 2998 2906 35 -485 388 C ATOM 1357 CB BPRO A 169 7.530 2.930 -0.883 0.50 19.75 C ANISOU 1357 CB BPRO A 169 2595 2290 2616 -356 -97 863 C ATOM 1358 CG APRO A 169 6.849 3.387 -2.033 0.50 22.36 C ANISOU 1358 CG APRO A 169 2446 3246 2803 74 -572 332 C ATOM 1359 CG BPRO A 169 7.263 4.261 -1.515 0.50 18.11 C ANISOU 1359 CG BPRO A 169 2140 2308 2433 -588 20 917 C ATOM 1360 CD APRO A 169 5.700 4.214 -1.555 0.50 22.58 C ANISOU 1360 CD APRO A 169 2597 3149 2833 -36 -188 370 C ATOM 1361 CD BPRO A 169 5.807 4.571 -1.303 0.50 19.19 C ANISOU 1361 CD BPRO A 169 2255 2504 2532 -741 98 865 C ATOM 1362 N PRO A 170 7.394 2.549 2.530 1.00 22.33 N ANISOU 1362 N PRO A 170 2631 2646 3207 -184 -887 496 N ATOM 1363 CA PRO A 170 8.070 3.000 3.748 1.00 23.24 C ANISOU 1363 CA PRO A 170 2775 2695 3357 -217 -1063 636 C ATOM 1364 C PRO A 170 9.488 3.433 3.386 1.00 25.32 C ANISOU 1364 C PRO A 170 3135 2852 3632 -90 -1121 930 C ATOM 1365 O PRO A 170 9.963 3.123 2.293 1.00 26.31 O ANISOU 1365 O PRO A 170 3410 3005 3580 -341 -904 1161 O ATOM 1366 CB PRO A 170 8.103 1.732 4.608 1.00 22.18 C ANISOU 1366 CB PRO A 170 2686 2619 3121 -394 -931 767 C ATOM 1367 CG PRO A 170 8.055 0.614 3.611 1.00 22.66 C ANISOU 1367 CG PRO A 170 2857 2608 3145 -237 -954 762 C ATOM 1368 CD PRO A 170 7.087 1.110 2.576 1.00 20.83 C ANISOU 1368 CD PRO A 170 2445 2345 3123 -102 -1042 626 C ATOM 1369 N LYS A 171 10.160 4.135 4.290 1.00 27.21 N ANISOU 1369 N LYS A 171 3234 3078 4025 -548 -1275 941 N ATOM 1370 CA LYS A 171 11.525 4.588 4.034 1.00 30.50 C ANISOU 1370 CA LYS A 171 3277 3718 4592 -585 -888 923 C ATOM 1371 C LYS A 171 12.547 3.478 4.271 1.00 30.30 C ANISOU 1371 C LYS A 171 2924 3908 4678 -506 -589 1213 C ATOM 1372 O LYS A 171 13.700 3.574 3.842 1.00 30.67 O ANISOU 1372 O LYS A 171 2818 4056 4778 -607 -66 1457 O ATOM 1373 CB LYS A 171 11.853 5.801 4.908 1.00 35.25 C ANISOU 1373 CB LYS A 171 4393 4152 4846 -457 -870 740 C ATOM 1374 CG LYS A 171 10.948 7.001 4.645 1.00 38.53 C ANISOU 1374 CG LYS A 171 5227 4474 4937 183 -728 728 C ATOM 1375 CD LYS A 171 10.929 7.353 3.162 1.00 40.47 C ANISOU 1375 CD LYS A 171 5586 4897 4892 770 -949 683 C ATOM 1376 CE LYS A 171 10.025 8.541 2.874 1.00 42.40 C ANISOU 1376 CE LYS A 171 5990 5281 4837 600 -1111 588 C ATOM 1377 NZ LYS A 171 10.174 9.009 1.467 1.00 44.00 N ANISOU 1377 NZ LYS A 171 6184 5680 4854 410 -1157 452 N ATOM 1378 N VAL A 172 12.117 2.430 4.964 1.00 29.96 N ANISOU 1378 N VAL A 172 2832 4005 4546 -268 -894 1240 N ATOM 1379 CA VAL A 172 12.987 1.304 5.285 1.00 29.18 C ANISOU 1379 CA VAL A 172 3001 3743 4340 -709 -588 1389 C ATOM 1380 C VAL A 172 12.307 -0.001 4.885 1.00 25.88 C ANISOU 1380 C VAL A 172 2653 3313 3866 -746 41 1692 C ATOM 1381 O VAL A 172 11.103 -0.033 4.658 1.00 24.69 O ANISOU 1381 O VAL A 172 1995 3497 3888 -478 -435 1949 O ATOM 1382 CB VAL A 172 13.319 1.263 6.793 1.00 31.97 C ANISOU 1382 CB VAL A 172 3442 4124 4581 -719 -383 1222 C ATOM 1383 CG1 VAL A 172 14.109 2.502 7.197 1.00 33.76 C ANISOU 1383 CG1 VAL A 172 3795 4370 4659 -598 -707 748 C ATOM 1384 CG2 VAL A 172 12.045 1.143 7.619 1.00 31.90 C ANISOU 1384 CG2 VAL A 172 3435 4141 4544 -175 -147 1396 C ATOM 1385 N AGLN A 173 13.085 -1.074 4.789 0.50 23.96 N ANISOU 1385 N AGLN A 173 2606 2866 3631 -875 420 1679 N ATOM 1386 N BGLN A 173 13.086 -1.072 4.796 0.50 24.00 N ANISOU 1386 N BGLN A 173 2614 2872 3632 -839 416 1700 N ATOM 1387 CA AGLN A 173 12.527 -2.380 4.461 0.50 24.15 C ANISOU 1387 CA AGLN A 173 2799 2937 3440 -410 640 1472 C ATOM 1388 CA BGLN A 173 12.535 -2.381 4.479 0.50 24.18 C ANISOU 1388 CA BGLN A 173 2801 2946 3440 -341 628 1504 C ATOM 1389 C AGLN A 173 11.695 -2.905 5.622 0.50 21.83 C ANISOU 1389 C AGLN A 173 2673 2534 3087 -592 491 1302 C ATOM 1390 C BGLN A 173 11.664 -2.872 5.625 0.50 22.00 C ANISOU 1390 C BGLN A 173 2737 2538 3081 -574 524 1373 C ATOM 1391 O AGLN A 173 11.925 -2.542 6.776 0.50 20.68 O ANISOU 1391 O AGLN A 173 2515 2534 2806 -626 533 1153 O ATOM 1392 O BGLN A 173 11.840 -2.457 6.771 0.50 21.15 O ANISOU 1392 O BGLN A 173 2705 2537 2793 -654 657 1333 O ATOM 1393 CB AGLN A 173 13.634 -3.377 4.105 0.50 27.50 C ANISOU 1393 CB AGLN A 173 3218 3590 3639 -535 952 1419 C ATOM 1394 CB BGLN A 173 13.657 -3.384 4.213 0.50 27.52 C ANISOU 1394 CB BGLN A 173 3170 3633 3652 -366 874 1408 C ATOM 1395 CG AGLN A 173 14.424 -2.999 2.858 0.50 29.68 C ANISOU 1395 CG AGLN A 173 3378 4161 3738 -595 1140 1530 C ATOM 1396 CG BGLN A 173 14.530 -3.028 3.021 0.50 29.87 C ANISOU 1396 CG BGLN A 173 3292 4278 3778 -281 1002 1457 C ATOM 1397 CD AGLN A 173 14.991 -4.206 2.131 0.50 33.30 C ANISOU 1397 CD AGLN A 173 4067 4763 3822 -493 1119 1615 C ATOM 1398 CD BGLN A 173 15.619 -4.049 2.783 0.50 33.67 C ANISOU 1398 CD BGLN A 173 3888 4998 3905 -96 902 1432 C ATOM 1399 OE1AGLN A 173 15.679 -5.038 2.721 0.50 33.64 O ANISOU 1399 OE1AGLN A 173 4098 4782 3902 -530 1148 1833 O ATOM 1400 OE1BGLN A 173 16.040 -4.746 3.704 0.50 35.47 O ANISOU 1400 OE1BGLN A 173 3965 5516 3993 139 631 1373 O ATOM 1401 NE2AGLN A 173 14.711 -4.298 0.837 0.50 35.64 N ANISOU 1401 NE2AGLN A 173 4406 5205 3930 -288 944 1233 N ATOM 1402 NE2BGLN A 173 16.083 -4.144 1.542 0.50 34.36 N ANISOU 1402 NE2BGLN A 173 3905 5226 3921 92 975 1165 N ATOM 1403 N SER A 174 10.719 -3.750 5.309 1.00 19.97 N ANISOU 1403 N SER A 174 2434 2250 2901 -463 492 1223 N ATOM 1404 CA SER A 174 9.915 -4.395 6.328 1.00 17.56 C ANISOU 1404 CA SER A 174 1855 1890 2924 -249 442 928 C ATOM 1405 C SER A 174 10.277 -5.875 6.361 1.00 17.65 C ANISOU 1405 C SER A 174 1851 2011 2841 -119 691 603 C ATOM 1406 O SER A 174 11.140 -6.344 5.595 1.00 18.15 O ANISOU 1406 O SER A 174 1840 2161 2892 -169 920 580 O ATOM 1407 CB SER A 174 8.422 -4.225 6.030 1.00 19.99 C ANISOU 1407 CB SER A 174 2367 1938 3287 102 -121 601 C ATOM 1408 OG SER A 174 8.022 -2.871 6.181 1.00 23.27 O ANISOU 1408 OG SER A 174 2813 2292 3735 357 -334 259 O ATOM 1409 N ALA A 175 9.624 -6.605 7.252 1.00 16.04 N ANISOU 1409 N ALA A 175 1581 1770 2741 -111 500 524 N ATOM 1410 CA ALA A 175 9.852 -8.036 7.387 1.00 14.09 C ANISOU 1410 CA ALA A 175 1030 1873 2449 118 652 672 C ATOM 1411 C ALA A 175 8.625 -8.687 7.985 1.00 13.04 C ANISOU 1411 C ALA A 175 1195 1581 2176 -13 705 518 C ATOM 1412 O ALA A 175 7.871 -8.056 8.725 1.00 14.78 O ANISOU 1412 O ALA A 175 1492 1799 2322 285 736 228 O ATOM 1413 CB ALA A 175 11.062 -8.304 8.275 1.00 15.55 C ANISOU 1413 CB ALA A 175 1125 2283 2497 180 246 742 C ATOM 1414 N VAL A 176 8.433 -9.959 7.671 1.00 11.71 N ANISOU 1414 N VAL A 176 1387 1350 1711 137 655 502 N ATOM 1415 CA VAL A 176 7.392 -10.740 8.310 1.00 12.13 C ANISOU 1415 CA VAL A 176 1248 1444 1917 117 317 345 C ATOM 1416 C VAL A 176 8.044 -11.665 9.321 1.00 11.83 C ANISOU 1416 C VAL A 176 836 1843 1814 348 424 387 C ATOM 1417 O VAL A 176 9.036 -12.348 9.016 1.00 13.59 O ANISOU 1417 O VAL A 176 1313 1918 1930 419 577 432 O ATOM 1418 CB VAL A 176 6.609 -11.560 7.274 1.00 12.86 C ANISOU 1418 CB VAL A 176 1531 1630 1725 -264 135 301 C ATOM 1419 CG1 VAL A 176 5.601 -12.481 7.956 1.00 14.87 C ANISOU 1419 CG1 VAL A 176 1877 2073 1700 -148 293 172 C ATOM 1420 CG2 VAL A 176 5.914 -10.619 6.302 1.00 15.41 C ANISOU 1420 CG2 VAL A 176 2407 1562 1886 -24 119 397 C ATOM 1421 N ILE A 177 7.504 -11.663 10.539 1.00 12.99 N ANISOU 1421 N ILE A 177 1436 1724 1776 167 185 524 N ATOM 1422 CA ILE A 177 7.995 -12.549 11.584 1.00 14.64 C ANISOU 1422 CA ILE A 177 1500 2150 1913 58 269 257 C ATOM 1423 C ILE A 177 6.860 -13.412 12.104 1.00 11.57 C ANISOU 1423 C ILE A 177 1175 1441 1780 317 167 291 C ATOM 1424 O ILE A 177 5.683 -13.010 12.071 1.00 13.24 O ANISOU 1424 O ILE A 177 1430 1422 2178 264 358 389 O ATOM 1425 CB ILE A 177 8.623 -11.769 12.753 1.00 16.60 C ANISOU 1425 CB ILE A 177 1879 2255 2173 21 370 58 C ATOM 1426 CG1 ILE A 177 7.603 -10.793 13.354 1.00 19.88 C ANISOU 1426 CG1 ILE A 177 2774 2657 2121 -60 167 -430 C ATOM 1427 CG2 ILE A 177 9.855 -11.029 12.284 1.00 19.51 C ANISOU 1427 CG2 ILE A 177 2344 2576 2491 -691 469 254 C ATOM 1428 CD1 ILE A 177 8.108 -10.050 14.553 1.00 20.52 C ANISOU 1428 CD1 ILE A 177 3280 2434 2082 -250 142 -226 C ATOM 1429 N LYS A 178 7.220 -14.596 12.577 1.00 11.57 N ANISOU 1429 N LYS A 178 1435 1497 1461 253 198 413 N ATOM 1430 CA LYS A 178 6.267 -15.525 13.160 1.00 11.79 C ANISOU 1430 CA LYS A 178 1550 1410 1519 133 91 231 C ATOM 1431 C LYS A 178 6.690 -15.854 14.583 1.00 11.54 C ANISOU 1431 C LYS A 178 1040 1744 1600 344 166 373 C ATOM 1432 O LYS A 178 7.828 -16.266 14.833 1.00 14.57 O ANISOU 1432 O LYS A 178 1033 2692 1811 873 318 252 O ATOM 1433 CB LYS A 178 6.166 -16.787 12.301 1.00 12.16 C ANISOU 1433 CB LYS A 178 1711 1187 1721 -309 -131 -356 C ATOM 1434 CG LYS A 178 5.235 -17.873 12.814 1.00 16.93 C ANISOU 1434 CG LYS A 178 2724 1596 2111 -284 -316 -374 C ATOM 1435 CD LYS A 178 5.132 -18.983 11.775 1.00 21.97 C ANISOU 1435 CD LYS A 178 3474 2266 2605 -476 -178 -577 C ATOM 1436 CE LYS A 178 4.140 -20.053 12.170 1.00 28.09 C ANISOU 1436 CE LYS A 178 4560 3040 3070 527 91 -371 C ATOM 1437 NZ LYS A 178 3.978 -21.079 11.089 1.00 33.06 N ANISOU 1437 NZ LYS A 178 5475 3587 3498 970 104 -264 N ATOM 1438 N ALEU A 179 5.772 -15.642 15.516 0.50 9.79 N ANISOU 1438 N ALEU A 179 989 1296 1434 155 127 206 N ATOM 1439 N BLEU A 179 5.755 -15.679 15.512 0.50 9.53 N ANISOU 1439 N BLEU A 179 861 1307 1452 -147 246 173 N ATOM 1440 CA ALEU A 179 6.002 -15.951 16.914 0.50 10.38 C ANISOU 1440 CA ALEU A 179 1246 1226 1469 131 -121 57 C ATOM 1441 CA BLEU A 179 5.989 -15.930 16.926 0.50 10.82 C ANISOU 1441 CA BLEU A 179 1141 1413 1554 -276 -60 -66 C ATOM 1442 C ALEU A 179 5.273 -17.240 17.231 0.50 9.97 C ANISOU 1442 C ALEU A 179 1149 1152 1486 219 -165 -166 C ATOM 1443 C BLEU A 179 5.250 -17.197 17.341 0.50 10.48 C ANISOU 1443 C BLEU A 179 1093 1393 1496 -373 125 7 C ATOM 1444 O ALEU A 179 4.076 -17.366 16.963 0.50 10.29 O ANISOU 1444 O ALEU A 179 1063 1333 1514 310 -346 -179 O ATOM 1445 O BLEU A 179 4.021 -17.264 17.256 0.50 10.81 O ANISOU 1445 O BLEU A 179 972 1713 1420 -747 400 279 O ATOM 1446 CB ALEU A 179 5.461 -14.833 17.806 0.50 10.19 C ANISOU 1446 CB ALEU A 179 1316 1224 1330 35 -235 135 C ATOM 1447 CB BLEU A 179 5.471 -14.758 17.759 0.50 11.41 C ANISOU 1447 CB BLEU A 179 1271 1472 1592 -411 -339 -401 C ATOM 1448 CG ALEU A 179 6.373 -13.628 18.049 0.50 11.20 C ANISOU 1448 CG ALEU A 179 1646 1405 1202 182 -391 356 C ATOM 1449 CG BLEU A 179 5.994 -13.363 17.401 0.50 12.87 C ANISOU 1449 CG BLEU A 179 1556 1745 1586 -591 -508 -711 C ATOM 1450 CD1ALEU A 179 6.725 -12.929 16.740 0.50 12.92 C ANISOU 1450 CD1ALEU A 179 2124 1532 1252 -144 -398 845 C ATOM 1451 CD1BLEU A 179 5.389 -12.307 18.319 0.50 12.84 C ANISOU 1451 CD1BLEU A 179 1803 1557 1517 -654 -631 -805 C ATOM 1452 CD2ALEU A 179 5.714 -12.658 19.016 0.50 9.90 C ANISOU 1452 CD2ALEU A 179 1406 1319 1037 467 -815 4 C ATOM 1453 CD2BLEU A 179 7.515 -13.323 17.459 0.50 13.66 C ANISOU 1453 CD2BLEU A 179 1644 1886 1658 -405 -670 -920 C ATOM 1454 N VAL A 180 5.995 -18.194 17.801 1.00 10.10 N ANISOU 1454 N VAL A 180 1050 1217 1569 237 -31 -117 N ATOM 1455 CA VAL A 180 5.404 -19.464 18.185 1.00 11.78 C ANISOU 1455 CA VAL A 180 1440 1497 1536 186 -176 -135 C ATOM 1456 C VAL A 180 5.602 -19.632 19.669 1.00 9.58 C ANISOU 1456 C VAL A 180 974 1172 1492 -260 108 -24 C ATOM 1457 O VAL A 180 6.725 -19.597 20.155 1.00 10.52 O ANISOU 1457 O VAL A 180 1027 1257 1711 -179 204 -130 O ATOM 1458 CB VAL A 180 6.050 -20.633 17.416 1.00 13.55 C ANISOU 1458 CB VAL A 180 2251 1548 1347 112 127 -162 C ATOM 1459 CG1 VAL A 180 5.531 -21.971 17.916 1.00 16.25 C ANISOU 1459 CG1 VAL A 180 2405 1967 1800 -180 311 -73 C ATOM 1460 CG2 VAL A 180 5.798 -20.458 15.928 1.00 14.77 C ANISOU 1460 CG2 VAL A 180 2333 2127 1149 634 286 -596 C ATOM 1461 N LYS A 181 4.511 -19.793 20.400 1.00 11.19 N ANISOU 1461 N LYS A 181 1206 1655 1390 -79 -162 68 N ATOM 1462 CA LYS A 181 4.618 -19.856 21.844 1.00 10.12 C ANISOU 1462 CA LYS A 181 871 1566 1407 210 -122 220 C ATOM 1463 C LYS A 181 5.578 -20.960 22.290 1.00 10.33 C ANISOU 1463 C LYS A 181 840 1409 1675 -141 -61 107 C ATOM 1464 O LYS A 181 5.492 -22.111 21.834 1.00 12.29 O ANISOU 1464 O LYS A 181 1788 1107 1775 -294 -279 -179 O ATOM 1465 CB LYS A 181 3.251 -20.023 22.498 1.00 15.53 C ANISOU 1465 CB LYS A 181 1526 2620 1752 365 579 346 C ATOM 1466 CG LYS A 181 3.300 -19.897 24.022 1.00 19.33 C ANISOU 1466 CG LYS A 181 2145 3242 1955 743 910 429 C ATOM 1467 CD LYS A 181 1.902 -19.932 24.620 1.00 24.36 C ANISOU 1467 CD LYS A 181 2965 3783 2508 1963 897 -58 C ATOM 1468 CE LYS A 181 1.919 -19.606 26.098 1.00 29.10 C ANISOU 1468 CE LYS A 181 3739 4092 3223 1729 1536 -454 C ATOM 1469 NZ LYS A 181 0.577 -19.833 26.701 1.00 35.32 N ANISOU 1469 NZ LYS A 181 5061 4557 3800 1265 1429 -444 N ATOM 1470 N ASN A 182 6.508 -20.573 23.157 1.00 11.67 N ANISOU 1470 N ASN A 182 908 1562 1961 234 -340 209 N ATOM 1471 CA ASN A 182 7.478 -21.475 23.744 1.00 12.84 C ANISOU 1471 CA ASN A 182 976 1829 2073 36 25 214 C ATOM 1472 C ASN A 182 8.030 -20.834 25.009 1.00 13.31 C ANISOU 1472 C ASN A 182 1096 2016 1943 152 118 96 C ATOM 1473 O ASN A 182 8.993 -20.063 24.957 1.00 13.49 O ANISOU 1473 O ASN A 182 1041 2259 1824 -77 -288 -45 O ATOM 1474 CB ASN A 182 8.610 -21.766 22.756 1.00 15.30 C ANISOU 1474 CB ASN A 182 1469 1866 2476 734 158 253 C ATOM 1475 CG ASN A 182 9.733 -22.578 23.388 1.00 18.10 C ANISOU 1475 CG ASN A 182 1909 2100 2865 739 228 498 C ATOM 1476 OD1 ASN A 182 9.645 -22.964 24.550 1.00 21.46 O ANISOU 1476 OD1 ASN A 182 2583 2346 3222 824 39 558 O ATOM 1477 ND2 ASN A 182 10.793 -22.823 22.635 1.00 21.06 N ANISOU 1477 ND2 ASN A 182 2431 2679 2890 1289 3 349 N ATOM 1478 N GLU A 183 7.402 -21.136 26.144 1.00 14.26 N ANISOU 1478 N GLU A 183 1629 1884 1904 369 131 -242 N ATOM 1479 CA GLU A 183 7.758 -20.477 27.398 1.00 13.59 C ANISOU 1479 CA GLU A 183 1219 1795 2149 370 28 -199 C ATOM 1480 C GLU A 183 8.973 -21.130 28.039 1.00 13.52 C ANISOU 1480 C GLU A 183 1712 1276 2146 237 -228 8 C ATOM 1481 O GLU A 183 8.902 -22.252 28.542 1.00 16.01 O ANISOU 1481 O GLU A 183 2161 1462 2458 81 -380 235 O ATOM 1482 CB GLU A 183 6.573 -20.451 28.363 1.00 18.05 C ANISOU 1482 CB GLU A 183 1509 2510 2837 987 198 558 C ATOM 1483 CG GLU A 183 5.362 -19.715 27.812 1.00 24.72 C ANISOU 1483 CG GLU A 183 2372 3518 3502 303 578 6 C ATOM 1484 CD GLU A 183 4.325 -19.429 28.878 1.00 33.89 C ANISOU 1484 CD GLU A 183 3948 4700 4226 -476 785 -10 C ATOM 1485 OE1 GLU A 183 4.643 -18.695 29.838 1.00 36.57 O ANISOU 1485 OE1 GLU A 183 4814 4732 4348 -682 913 -165 O ATOM 1486 OE2 GLU A 183 3.192 -19.935 28.754 1.00 37.67 O ANISOU 1486 OE2 GLU A 183 3928 5613 4772 -699 726 61 O ATOM 1487 N LYS A 184 10.084 -20.405 28.022 1.00 12.03 N ANISOU 1487 N LYS A 184 1277 1307 1985 -14 -651 -123 N ATOM 1488 CA LYS A 184 11.371 -20.955 28.386 1.00 13.18 C ANISOU 1488 CA LYS A 184 1735 1293 1977 -122 -375 -3 C ATOM 1489 C LYS A 184 11.670 -20.795 29.869 1.00 13.62 C ANISOU 1489 C LYS A 184 1805 1503 1867 -495 -466 -130 C ATOM 1490 O LYS A 184 12.435 -21.568 30.433 1.00 15.03 O ANISOU 1490 O LYS A 184 2236 1457 2016 219 -640 -62 O ATOM 1491 CB LYS A 184 12.470 -20.311 27.541 1.00 12.93 C ANISOU 1491 CB LYS A 184 1664 1343 1905 9 -184 66 C ATOM 1492 CG LYS A 184 12.282 -20.535 26.049 1.00 15.65 C ANISOU 1492 CG LYS A 184 2259 1958 1729 -328 53 -178 C ATOM 1493 CD LYS A 184 13.153 -19.610 25.227 1.00 16.12 C ANISOU 1493 CD LYS A 184 2393 1990 1740 -73 336 -488 C ATOM 1494 CE LYS A 184 12.861 -19.754 23.756 1.00 15.02 C ANISOU 1494 CE LYS A 184 1881 1942 1884 435 144 -248 C ATOM 1495 NZ LYS A 184 11.518 -19.222 23.411 1.00 16.70 N ANISOU 1495 NZ LYS A 184 1941 2158 2246 512 342 49 N ATOM 1496 N PHE A 185 11.057 -19.799 30.502 1.00 15.29 N ANISOU 1496 N PHE A 185 2286 1815 1706 -27 -177 -275 N ATOM 1497 CA PHE A 185 11.305 -19.533 31.917 1.00 15.93 C ANISOU 1497 CA PHE A 185 2150 1821 2080 -334 -114 -173 C ATOM 1498 C PHE A 185 10.003 -19.160 32.614 1.00 16.43 C ANISOU 1498 C PHE A 185 2203 1897 2140 -276 123 53 C ATOM 1499 O PHE A 185 9.172 -18.461 32.038 1.00 18.28 O ANISOU 1499 O PHE A 185 2162 2755 2029 353 -64 -152 O ATOM 1500 CB PHE A 185 12.350 -18.419 32.081 1.00 16.76 C ANISOU 1500 CB PHE A 185 1957 2110 2301 -838 132 -47 C ATOM 1501 CG PHE A 185 13.701 -18.760 31.490 1.00 21.01 C ANISOU 1501 CG PHE A 185 2406 2681 2893 -1011 -97 -533 C ATOM 1502 CD1 PHE A 185 14.601 -19.551 32.189 1.00 23.20 C ANISOU 1502 CD1 PHE A 185 2500 3126 3187 -572 -66 -826 C ATOM 1503 CD2 PHE A 185 14.063 -18.291 30.236 1.00 22.68 C ANISOU 1503 CD2 PHE A 185 2805 2649 3162 -1259 356 -808 C ATOM 1504 CE1 PHE A 185 15.841 -19.861 31.652 1.00 24.62 C ANISOU 1504 CE1 PHE A 185 2383 3489 3481 -531 -182 -719 C ATOM 1505 CE2 PHE A 185 15.296 -18.599 29.689 1.00 23.74 C ANISOU 1505 CE2 PHE A 185 2562 3165 3293 -1396 -178 -879 C ATOM 1506 CZ PHE A 185 16.189 -19.388 30.396 1.00 24.01 C ANISOU 1506 CZ PHE A 185 2089 3578 3455 -1139 -110 -721 C ATOM 1507 N PRO A 186 9.822 -19.625 33.860 1.00 20.80 N ANISOU 1507 N PRO A 186 3260 2013 2627 202 295 350 N ATOM 1508 CA PRO A 186 8.544 -19.458 34.558 1.00 23.75 C ANISOU 1508 CA PRO A 186 4021 2094 2909 150 403 218 C ATOM 1509 C PRO A 186 8.405 -18.089 35.192 1.00 25.59 C ANISOU 1509 C PRO A 186 4515 2092 3116 -104 268 2 C ATOM 1510 O PRO A 186 8.393 -17.990 36.416 1.00 31.39 O ANISOU 1510 O PRO A 186 5843 2775 3308 -204 -60 -180 O ATOM 1511 CB PRO A 186 8.600 -20.509 35.675 1.00 26.13 C ANISOU 1511 CB PRO A 186 4654 2303 2969 482 471 636 C ATOM 1512 CG PRO A 186 9.986 -21.052 35.680 1.00 26.47 C ANISOU 1512 CG PRO A 186 4494 2478 3085 851 67 648 C ATOM 1513 CD PRO A 186 10.820 -20.328 34.682 1.00 23.49 C ANISOU 1513 CD PRO A 186 3882 2267 2774 432 134 761 C ATOM 1514 N VAL A 187 8.301 -17.052 34.374 1.00 23.39 N ANISOU 1514 N VAL A 187 4048 1626 3213 -477 62 168 N ATOM 1515 CA VAL A 187 8.077 -15.706 34.882 1.00 24.15 C ANISOU 1515 CA VAL A 187 4153 1658 3364 -592 -108 -120 C ATOM 1516 C VAL A 187 6.603 -15.529 35.232 1.00 27.19 C ANISOU 1516 C VAL A 187 4151 2424 3756 -881 -227 -142 C ATOM 1517 O VAL A 187 5.730 -15.702 34.382 1.00 31.80 O ANISOU 1517 O VAL A 187 5028 3066 3986 -1165 -415 -30 O ATOM 1518 CB VAL A 187 8.478 -14.646 33.842 1.00 24.19 C ANISOU 1518 CB VAL A 187 4242 1783 3166 -253 -122 18 C ATOM 1519 CG1 VAL A 187 8.085 -13.261 34.326 1.00 25.03 C ANISOU 1519 CG1 VAL A 187 4163 2286 3061 -559 -227 -174 C ATOM 1520 CG2 VAL A 187 9.973 -14.715 33.557 1.00 25.41 C ANISOU 1520 CG2 VAL A 187 4749 1603 3301 713 58 -377 C ATOM 1521 N LYS A 188 6.325 -15.192 36.486 1.00 26.12 N ANISOU 1521 N LYS A 188 3310 2598 4015 -481 348 -184 N ATOM 1522 CA LYS A 188 4.949 -15.044 36.941 1.00 29.73 C ANISOU 1522 CA LYS A 188 3803 3248 4245 -86 150 -62 C ATOM 1523 C LYS A 188 4.439 -13.621 36.743 1.00 27.40 C ANISOU 1523 C LYS A 188 3352 2924 4132 107 158 -26 C ATOM 1524 O LYS A 188 3.339 -13.415 36.233 1.00 28.30 O ANISOU 1524 O LYS A 188 3539 2933 4281 400 -57 -140 O ATOM 1525 CB LYS A 188 4.826 -15.455 38.411 1.00 35.82 C ANISOU 1525 CB LYS A 188 4854 4433 4323 -205 -14 -47 C ATOM 1526 CG LYS A 188 5.781 -14.715 39.350 1.00 40.48 C ANISOU 1526 CG LYS A 188 5852 5162 4365 -460 -45 -7 C ATOM 1527 CD LYS A 188 5.935 -15.438 40.687 1.00 43.70 C ANISOU 1527 CD LYS A 188 6518 5684 4399 -788 211 55 C ATOM 1528 CE LYS A 188 6.991 -14.773 41.565 1.00 44.72 C ANISOU 1528 CE LYS A 188 6848 5744 4399 -895 505 90 C ATOM 1529 NZ LYS A 188 7.210 -15.500 42.856 1.00 44.71 N ANISOU 1529 NZ LYS A 188 6975 5655 4357 -889 810 94 N ATOM 1530 N ASP A 189 5.248 -12.643 37.139 1.00 24.91 N ANISOU 1530 N ASP A 189 3052 2608 3805 -268 589 133 N ATOM 1531 CA ASP A 189 4.842 -11.243 37.109 1.00 23.56 C ANISOU 1531 CA ASP A 189 2680 2781 3491 -415 770 -306 C ATOM 1532 C ASP A 189 5.445 -10.556 35.888 1.00 19.87 C ANISOU 1532 C ASP A 189 2143 2070 3337 -525 517 -189 C ATOM 1533 O ASP A 189 6.569 -10.055 35.933 1.00 18.97 O ANISOU 1533 O ASP A 189 1826 2224 3155 -279 344 -462 O ATOM 1534 CB ASP A 189 5.294 -10.548 38.397 1.00 27.43 C ANISOU 1534 CB ASP A 189 3464 3463 3493 -547 1230 -782 C ATOM 1535 CG ASP A 189 4.675 -9.166 38.577 1.00 31.98 C ANISOU 1535 CG ASP A 189 4247 4256 3648 -431 1450 -962 C ATOM 1536 OD1 ASP A 189 4.226 -8.563 37.576 1.00 29.74 O ANISOU 1536 OD1 ASP A 189 3631 3904 3763 -304 1759 -664 O ATOM 1537 OD2 ASP A 189 4.648 -8.681 39.727 1.00 37.86 O ANISOU 1537 OD2 ASP A 189 5490 5134 3761 -267 1299 -978 O ATOM 1538 N LEU A 190 4.695 -10.545 34.791 1.00 17.90 N ANISOU 1538 N LEU A 190 1655 1844 3302 -377 383 123 N ATOM 1539 CA LEU A 190 5.206 -10.003 33.534 1.00 17.89 C ANISOU 1539 CA LEU A 190 1564 1765 3467 -132 292 28 C ATOM 1540 C LEU A 190 5.533 -8.513 33.618 1.00 18.39 C ANISOU 1540 C LEU A 190 1462 1773 3752 -86 527 -201 C ATOM 1541 O LEU A 190 6.508 -8.053 33.025 1.00 19.20 O ANISOU 1541 O LEU A 190 1466 2058 3768 90 588 152 O ATOM 1542 CB LEU A 190 4.239 -10.271 32.384 1.00 19.70 C ANISOU 1542 CB LEU A 190 2041 2023 3421 112 -634 -416 C ATOM 1543 CG LEU A 190 4.028 -11.725 31.983 1.00 27.22 C ANISOU 1543 CG LEU A 190 3820 2994 3526 395 -1549 -462 C ATOM 1544 CD1 LEU A 190 3.183 -11.802 30.721 1.00 29.59 C ANISOU 1544 CD1 LEU A 190 4580 3131 3529 -9 -1915 -272 C ATOM 1545 CD2 LEU A 190 5.351 -12.384 31.769 1.00 29.43 C ANISOU 1545 CD2 LEU A 190 4286 3464 3430 535 -1352 -1242 C ATOM 1546 N LYS A 191 4.717 -7.761 34.351 1.00 19.75 N ANISOU 1546 N LYS A 191 1670 1763 4071 89 544 -353 N ATOM 1547 CA LYS A 191 4.978 -6.339 34.546 1.00 22.02 C ANISOU 1547 CA LYS A 191 1705 2260 4399 360 721 -426 C ATOM 1548 C LYS A 191 6.288 -6.091 35.290 1.00 21.56 C ANISOU 1548 C LYS A 191 1786 2175 4228 118 975 -268 C ATOM 1549 O LYS A 191 7.036 -5.163 34.967 1.00 22.41 O ANISOU 1549 O LYS A 191 1981 2258 4276 117 1175 -320 O ATOM 1550 CB LYS A 191 3.806 -5.674 35.271 1.00 26.55 C ANISOU 1550 CB LYS A 191 2179 3110 4796 643 537 -654 C ATOM 1551 CG LYS A 191 2.596 -5.462 34.380 1.00 35.24 C ANISOU 1551 CG LYS A 191 4080 4165 5145 668 627 -524 C ATOM 1552 CD LYS A 191 2.905 -4.454 33.278 1.00 41.55 C ANISOU 1552 CD LYS A 191 5286 5113 5387 547 571 -546 C ATOM 1553 CE LYS A 191 1.690 -4.210 32.391 1.00 45.04 C ANISOU 1553 CE LYS A 191 5956 5537 5617 447 523 -682 C ATOM 1554 NZ LYS A 191 0.520 -3.729 33.179 1.00 46.81 N ANISOU 1554 NZ LYS A 191 6330 5719 5737 143 522 -696 N ATOM 1555 N ASN A 192 6.574 -6.928 36.279 1.00 19.57 N ANISOU 1555 N ASN A 192 1700 1873 3862 360 998 -461 N ATOM 1556 CA ASN A 192 7.803 -6.781 37.039 1.00 18.27 C ANISOU 1556 CA ASN A 192 1709 1755 3475 25 638 -868 C ATOM 1557 C ASN A 192 9.018 -7.187 36.209 1.00 16.92 C ANISOU 1557 C ASN A 192 1794 1706 2928 -284 498 -1169 C ATOM 1558 O ASN A 192 10.090 -6.586 36.301 1.00 19.65 O ANISOU 1558 O ASN A 192 2192 2221 3053 -498 689 -1410 O ATOM 1559 CB ASN A 192 7.748 -7.603 38.318 1.00 20.72 C ANISOU 1559 CB ASN A 192 1900 2313 3660 -8 639 -889 C ATOM 1560 CG ASN A 192 8.808 -7.188 39.306 1.00 27.73 C ANISOU 1560 CG ASN A 192 3310 3109 4114 355 672 -762 C ATOM 1561 OD1 ASN A 192 8.868 -6.029 39.714 1.00 31.14 O ANISOU 1561 OD1 ASN A 192 4050 3449 4331 506 438 -897 O ATOM 1562 ND2 ASN A 192 9.658 -8.130 39.694 1.00 28.52 N ANISOU 1562 ND2 ASN A 192 3283 3295 4257 769 1027 -426 N ATOM 1563 N TYR A 193 8.838 -8.210 35.390 1.00 14.88 N ANISOU 1563 N TYR A 193 1556 1497 2601 81 393 -587 N ATOM 1564 CA TYR A 193 9.898 -8.660 34.498 1.00 12.96 C ANISOU 1564 CA TYR A 193 1472 1029 2421 111 601 -684 C ATOM 1565 C TYR A 193 10.214 -7.575 33.481 1.00 13.78 C ANISOU 1565 C TYR A 193 1194 1439 2601 254 235 -483 C ATOM 1566 O TYR A 193 11.371 -7.285 33.213 1.00 14.93 O ANISOU 1566 O TYR A 193 1195 1725 2751 190 446 -239 O ATOM 1567 CB TYR A 193 9.452 -9.936 33.809 1.00 12.67 C ANISOU 1567 CB TYR A 193 1440 1107 2266 282 335 -763 C ATOM 1568 CG TYR A 193 10.489 -10.637 32.977 1.00 13.21 C ANISOU 1568 CG TYR A 193 1611 1294 2114 379 109 -315 C ATOM 1569 CD1 TYR A 193 11.760 -10.891 33.476 1.00 12.37 C ANISOU 1569 CD1 TYR A 193 1330 1334 2034 87 55 -413 C ATOM 1570 CD2 TYR A 193 10.175 -11.100 31.708 1.00 13.12 C ANISOU 1570 CD2 TYR A 193 1526 1570 1889 240 276 -191 C ATOM 1571 CE1 TYR A 193 12.693 -11.562 32.711 1.00 13.52 C ANISOU 1571 CE1 TYR A 193 1100 1869 2166 52 13 -339 C ATOM 1572 CE2 TYR A 193 11.091 -11.772 30.944 1.00 13.21 C ANISOU 1572 CE2 TYR A 193 1183 1710 2123 -189 175 -140 C ATOM 1573 CZ TYR A 193 12.348 -11.998 31.440 1.00 12.99 C ANISOU 1573 CZ TYR A 193 820 1890 2225 -168 -53 -395 C ATOM 1574 OH TYR A 193 13.249 -12.679 30.666 1.00 15.57 O ANISOU 1574 OH TYR A 193 1355 2236 2322 124 182 -431 O ATOM 1575 N LYS A 194 9.174 -6.967 32.923 1.00 15.17 N ANISOU 1575 N LYS A 194 1239 1667 2858 57 81 -272 N ATOM 1576 CA LYS A 194 9.357 -5.835 32.032 1.00 18.64 C ANISOU 1576 CA LYS A 194 1700 1986 3395 355 58 100 C ATOM 1577 C LYS A 194 10.127 -4.683 32.694 1.00 19.94 C ANISOU 1577 C LYS A 194 1820 1959 3795 50 322 52 C ATOM 1578 O LYS A 194 11.003 -4.091 32.064 1.00 19.97 O ANISOU 1578 O LYS A 194 1391 1942 4254 -1 333 212 O ATOM 1579 CB LYS A 194 8.015 -5.338 31.502 1.00 18.15 C ANISOU 1579 CB LYS A 194 1408 2119 3368 444 -632 60 C ATOM 1580 CG LYS A 194 8.121 -3.990 30.803 1.00 18.83 C ANISOU 1580 CG LYS A 194 1808 2173 3173 659 -832 216 C ATOM 1581 CD LYS A 194 6.780 -3.482 30.366 1.00 20.12 C ANISOU 1581 CD LYS A 194 2223 2159 3263 681 -890 305 C ATOM 1582 CE LYS A 194 6.920 -2.096 29.782 1.00 23.80 C ANISOU 1582 CE LYS A 194 2949 2527 3564 175 -1037 58 C ATOM 1583 NZ LYS A 194 5.587 -1.517 29.468 1.00 27.21 N ANISOU 1583 NZ LYS A 194 3785 2856 3697 909 -1296 144 N ATOM 1584 N LYS A 195 9.813 -4.380 33.956 1.00 18.99 N ANISOU 1584 N LYS A 195 1750 1623 3841 462 306 -397 N ATOM 1585 CA LYS A 195 10.526 -3.336 34.712 1.00 18.16 C ANISOU 1585 CA LYS A 195 1579 1795 3525 -199 901 -839 C ATOM 1586 C LYS A 195 12.019 -3.626 34.726 1.00 17.93 C ANISOU 1586 C LYS A 195 1695 1710 3408 -221 736 -708 C ATOM 1587 O LYS A 195 12.849 -2.739 34.521 1.00 19.02 O ANISOU 1587 O LYS A 195 1726 1743 3757 -348 666 -690 O ATOM 1588 CB LYS A 195 10.049 -3.264 36.170 1.00 20.86 C ANISOU 1588 CB LYS A 195 1982 2248 3696 -73 1177 -714 C ATOM 1589 CG LYS A 195 8.741 -2.537 36.406 1.00 25.33 C ANISOU 1589 CG LYS A 195 3174 2720 3728 195 1159 -844 C ATOM 1590 CD LYS A 195 8.523 -2.302 37.899 1.00 26.70 C ANISOU 1590 CD LYS A 195 3544 2920 3679 475 1288 -1062 C ATOM 1591 CE LYS A 195 7.220 -1.584 38.164 1.00 30.99 C ANISOU 1591 CE LYS A 195 4227 3851 3694 714 1142 -1009 C ATOM 1592 NZ LYS A 195 6.948 -1.488 39.624 1.00 34.28 N ANISOU 1592 NZ LYS A 195 4714 4567 3742 806 896 -918 N ATOM 1593 N PHE A 196 12.349 -4.881 34.997 1.00 16.97 N ANISOU 1593 N PHE A 196 1789 1729 2927 -111 651 -720 N ATOM 1594 CA PHE A 196 13.735 -5.308 35.087 1.00 13.88 C ANISOU 1594 CA PHE A 196 1639 1307 2328 -101 551 -467 C ATOM 1595 C PHE A 196 14.421 -5.185 33.728 1.00 13.26 C ANISOU 1595 C PHE A 196 1513 1272 2250 -214 383 -614 C ATOM 1596 O PHE A 196 15.535 -4.660 33.634 1.00 14.03 O ANISOU 1596 O PHE A 196 1640 1496 2193 -184 520 -616 O ATOM 1597 CB PHE A 196 13.802 -6.747 35.609 1.00 14.19 C ANISOU 1597 CB PHE A 196 1820 1664 1907 234 563 -468 C ATOM 1598 CG PHE A 196 15.095 -7.441 35.300 1.00 14.67 C ANISOU 1598 CG PHE A 196 1704 1989 1879 15 338 20 C ATOM 1599 CD1 PHE A 196 16.275 -7.057 35.925 1.00 15.40 C ANISOU 1599 CD1 PHE A 196 1742 2287 1821 -127 207 -120 C ATOM 1600 CD2 PHE A 196 15.130 -8.483 34.384 1.00 15.21 C ANISOU 1600 CD2 PHE A 196 2003 1955 1819 134 427 -225 C ATOM 1601 CE1 PHE A 196 17.470 -7.705 35.629 1.00 16.02 C ANISOU 1601 CE1 PHE A 196 1801 2357 1927 -91 272 -110 C ATOM 1602 CE2 PHE A 196 16.314 -9.132 34.091 1.00 15.60 C ANISOU 1602 CE2 PHE A 196 1957 2129 1839 -52 338 -92 C ATOM 1603 CZ PHE A 196 17.483 -8.749 34.715 1.00 16.69 C ANISOU 1603 CZ PHE A 196 2039 2347 1955 -110 243 70 C ATOM 1604 N LEU A 197 13.762 -5.671 32.674 1.00 12.62 N ANISOU 1604 N LEU A 197 1371 1235 2187 105 58 -449 N ATOM 1605 CA LEU A 197 14.359 -5.646 31.335 1.00 12.57 C ANISOU 1605 CA LEU A 197 1424 1144 2207 -119 -25 -300 C ATOM 1606 C LEU A 197 14.516 -4.223 30.804 1.00 12.27 C ANISOU 1606 C LEU A 197 920 1273 2467 82 -118 -553 C ATOM 1607 O LEU A 197 15.544 -3.876 30.232 1.00 12.99 O ANISOU 1607 O LEU A 197 980 1288 2665 135 458 -467 O ATOM 1608 CB LEU A 197 13.543 -6.483 30.339 1.00 11.70 C ANISOU 1608 CB LEU A 197 1283 1026 2135 -283 -17 -234 C ATOM 1609 CG LEU A 197 13.455 -7.987 30.583 1.00 10.60 C ANISOU 1609 CG LEU A 197 1154 821 2050 -42 -82 -425 C ATOM 1610 CD1 LEU A 197 12.526 -8.640 29.571 1.00 10.68 C ANISOU 1610 CD1 LEU A 197 1382 987 1688 -517 -115 -623 C ATOM 1611 CD2 LEU A 197 14.842 -8.605 30.509 1.00 12.80 C ANISOU 1611 CD2 LEU A 197 1256 1089 2517 315 -61 -256 C ATOM 1612 N ATHR A 198 13.481 -3.407 30.967 0.50 13.66 N ANISOU 1612 N ATHR A 198 1377 1336 2475 410 -91 -452 N ATOM 1613 N BTHR A 198 13.496 -3.396 30.984 0.50 14.20 N ANISOU 1613 N BTHR A 198 1493 1357 2544 291 -131 -516 N ATOM 1614 CA ATHR A 198 13.578 -2.024 30.530 0.50 12.95 C ANISOU 1614 CA ATHR A 198 1212 1274 2433 341 -219 -142 C ATOM 1615 CA BTHR A 198 13.580 -2.023 30.505 0.50 13.77 C ANISOU 1615 CA BTHR A 198 1367 1271 2593 172 -299 -227 C ATOM 1616 C ATHR A 198 14.766 -1.361 31.220 0.50 12.41 C ANISOU 1616 C ATHR A 198 772 1326 2615 551 -138 -51 C ATOM 1617 C BTHR A 198 14.666 -1.239 31.250 0.50 13.39 C ANISOU 1617 C BTHR A 198 1110 1220 2757 76 -245 -208 C ATOM 1618 O ATHR A 198 15.608 -0.735 30.575 0.50 14.43 O ANISOU 1618 O ATHR A 198 1059 1600 2821 400 -105 119 O ATOM 1619 O BTHR A 198 15.335 -0.387 30.666 0.50 16.02 O ANISOU 1619 O BTHR A 198 1738 1232 3114 -266 -216 -242 O ATOM 1620 CB ATHR A 198 12.271 -1.222 30.786 0.50 12.72 C ANISOU 1620 CB ATHR A 198 1086 1495 2251 49 -252 -229 C ATOM 1621 CB BTHR A 198 12.216 -1.302 30.581 0.50 13.83 C ANISOU 1621 CB BTHR A 198 1153 1588 2511 129 -321 -196 C ATOM 1622 OG1ATHR A 198 11.876 -1.331 32.162 0.50 12.66 O ANISOU 1622 OG1ATHR A 198 945 1635 2227 -29 211 -475 O ATOM 1623 OG1BTHR A 198 11.288 -1.961 29.710 0.50 14.54 O ANISOU 1623 OG1BTHR A 198 1127 1678 2718 226 -140 -126 O ATOM 1624 CG2ATHR A 198 11.155 -1.749 29.902 0.50 13.69 C ANISOU 1624 CG2ATHR A 198 1359 1439 2403 -156 -418 -124 C ATOM 1625 CG2BTHR A 198 12.349 0.144 30.144 0.50 13.64 C ANISOU 1625 CG2BTHR A 198 1276 1502 2404 20 -243 -434 C ATOM 1626 N LYS A 199 14.850 -1.538 32.532 1.00 13.66 N ANISOU 1626 N LYS A 199 893 1526 2768 323 -182 -225 N ATOM 1627 CA LYS A 199 15.910 -0.911 33.315 1.00 15.76 C ANISOU 1627 CA LYS A 199 1356 1976 2654 281 -179 -375 C ATOM 1628 C LYS A 199 17.300 -1.350 32.837 1.00 13.64 C ANISOU 1628 C LYS A 199 1366 1464 2352 587 -106 -333 C ATOM 1629 O LYS A 199 18.173 -0.509 32.586 1.00 14.47 O ANISOU 1629 O LYS A 199 1613 1588 2295 157 60 -617 O ATOM 1630 CB LYS A 199 15.728 -1.211 34.807 1.00 17.95 C ANISOU 1630 CB LYS A 199 1393 2432 2994 -217 -216 -943 C ATOM 1631 CG LYS A 199 16.828 -0.663 35.679 1.00 23.93 C ANISOU 1631 CG LYS A 199 2179 3392 3518 -325 -105 -756 C ATOM 1632 CD LYS A 199 16.893 0.845 35.585 1.00 28.85 C ANISOU 1632 CD LYS A 199 2915 4003 4042 -136 -597 -493 C ATOM 1633 CE LYS A 199 18.016 1.398 36.456 1.00 32.57 C ANISOU 1633 CE LYS A 199 3554 4423 4398 -547 -757 -384 C ATOM 1634 NZ LYS A 199 17.989 0.833 37.830 1.00 32.43 N ANISOU 1634 NZ LYS A 199 3297 4562 4463 -287 -891 -231 N ATOM 1635 N ILE A 200 17.521 -2.658 32.698 1.00 12.22 N ANISOU 1635 N ILE A 200 1263 1190 2187 815 78 -439 N ATOM 1636 CA ILE A 200 18.858 -3.147 32.370 1.00 12.41 C ANISOU 1636 CA ILE A 200 1514 1058 2142 518 -51 -392 C ATOM 1637 C ILE A 200 19.264 -2.736 30.946 1.00 11.88 C ANISOU 1637 C ILE A 200 1042 1358 2111 65 -430 -281 C ATOM 1638 O ILE A 200 20.450 -2.637 30.629 1.00 13.14 O ANISOU 1638 O ILE A 200 1192 1621 2178 -202 -91 -240 O ATOM 1639 CB ILE A 200 18.979 -4.683 32.577 1.00 11.34 C ANISOU 1639 CB ILE A 200 1145 1055 2106 564 -144 -164 C ATOM 1640 CG1 ILE A 200 20.457 -5.098 32.670 1.00 13.21 C ANISOU 1640 CG1 ILE A 200 1449 1500 2067 445 -503 142 C ATOM 1641 CG2 ILE A 200 18.258 -5.440 31.478 1.00 11.88 C ANISOU 1641 CG2 ILE A 200 1574 1215 1725 -94 -314 -410 C ATOM 1642 CD1 ILE A 200 20.662 -6.545 33.031 1.00 13.58 C ANISOU 1642 CD1 ILE A 200 1660 1518 1981 250 -288 -93 C ATOM 1643 N PHE A 201 18.276 -2.469 30.099 1.00 12.34 N ANISOU 1643 N PHE A 201 1418 1047 2224 320 -281 44 N ATOM 1644 CA PHE A 201 18.560 -2.013 28.739 1.00 12.52 C ANISOU 1644 CA PHE A 201 1585 1019 2153 -43 -663 137 C ATOM 1645 C PHE A 201 18.731 -0.492 28.606 1.00 15.09 C ANISOU 1645 C PHE A 201 1944 1372 2418 -195 -481 -61 C ATOM 1646 O PHE A 201 19.166 -0.013 27.561 1.00 18.45 O ANISOU 1646 O PHE A 201 2830 1809 2370 -431 -12 -128 O ATOM 1647 CB PHE A 201 17.526 -2.540 27.741 1.00 12.76 C ANISOU 1647 CB PHE A 201 1396 1417 2035 146 -330 -92 C ATOM 1648 CG PHE A 201 17.867 -3.896 27.168 1.00 11.41 C ANISOU 1648 CG PHE A 201 1031 1250 2053 84 -271 -143 C ATOM 1649 CD1 PHE A 201 18.695 -3.999 26.058 1.00 12.79 C ANISOU 1649 CD1 PHE A 201 1060 1789 2008 164 -116 -114 C ATOM 1650 CD2 PHE A 201 17.364 -5.066 27.727 1.00 11.33 C ANISOU 1650 CD2 PHE A 201 1023 1227 2055 462 -274 -316 C ATOM 1651 CE1 PHE A 201 19.023 -5.238 25.514 1.00 11.40 C ANISOU 1651 CE1 PHE A 201 707 1812 1812 18 -42 -242 C ATOM 1652 CE2 PHE A 201 17.691 -6.316 27.177 1.00 11.14 C ANISOU 1652 CE2 PHE A 201 576 1769 1885 194 16 -455 C ATOM 1653 CZ PHE A 201 18.515 -6.399 26.072 1.00 11.33 C ANISOU 1653 CZ PHE A 201 631 1851 1821 -41 77 -293 C ATOM 1654 N GLN A 202 18.396 0.273 29.644 1.00 14.98 N ANISOU 1654 N GLN A 202 1349 1538 2802 -166 -24 189 N ATOM 1655 CA GLN A 202 18.720 1.706 29.646 1.00 16.51 C ANISOU 1655 CA GLN A 202 1319 1522 3431 -81 176 292 C ATOM 1656 C GLN A 202 20.228 1.864 29.508 1.00 15.73 C ANISOU 1656 C GLN A 202 1481 1144 3352 130 -64 255 C ATOM 1657 O GLN A 202 20.984 1.085 30.084 1.00 16.76 O ANISOU 1657 O GLN A 202 1833 1388 3145 -21 -246 -140 O ATOM 1658 CB GLN A 202 18.277 2.373 30.951 1.00 18.09 C ANISOU 1658 CB GLN A 202 1103 1756 4013 11 582 246 C ATOM 1659 CG GLN A 202 16.780 2.401 31.183 1.00 23.77 C ANISOU 1659 CG GLN A 202 2072 2478 4482 61 169 526 C ATOM 1660 CD GLN A 202 16.027 3.019 30.029 1.00 28.27 C ANISOU 1660 CD GLN A 202 2734 3126 4880 379 -106 709 C ATOM 1661 OE1 GLN A 202 16.190 4.203 29.726 1.00 31.99 O ANISOU 1661 OE1 GLN A 202 3747 3333 5074 1118 -133 953 O ATOM 1662 NE2 GLN A 202 15.190 2.220 29.376 1.00 31.36 N ANISOU 1662 NE2 GLN A 202 3015 3865 5035 656 -311 415 N ATOM 1663 N ASN A 203 20.667 2.875 28.761 1.00 18.36 N ANISOU 1663 N ASN A 203 1605 1796 3575 -105 422 130 N ATOM 1664 CA ASN A 203 22.097 3.139 28.610 1.00 20.78 C ANISOU 1664 CA ASN A 203 2092 2143 3659 -352 508 -35 C ATOM 1665 C ASN A 203 22.830 1.880 28.145 1.00 17.20 C ANISOU 1665 C ASN A 203 1329 2049 3154 -82 207 -174 C ATOM 1666 O ASN A 203 23.679 1.332 28.853 1.00 16.86 O ANISOU 1666 O ASN A 203 1649 1820 2936 -213 187 -376 O ATOM 1667 CB ASN A 203 22.675 3.643 29.932 1.00 24.83 C ANISOU 1667 CB ASN A 203 2855 2539 4040 -537 732 -415 C ATOM 1668 CG ASN A 203 22.053 4.956 30.378 1.00 30.38 C ANISOU 1668 CG ASN A 203 3868 3280 4395 -519 694 -402 C ATOM 1669 OD1 ASN A 203 21.998 5.923 29.617 1.00 33.07 O ANISOU 1669 OD1 ASN A 203 4532 3374 4659 -770 584 -415 O ATOM 1670 ND2 ASN A 203 21.589 4.999 31.622 1.00 32.13 N ANISOU 1670 ND2 ASN A 203 3880 3738 4589 -327 692 -582 N ATOM 1671 N ARG A 204 22.499 1.435 26.940 1.00 17.18 N ANISOU 1671 N ARG A 204 1450 2213 2863 -253 128 -81 N ATOM 1672 CA ARG A 204 22.946 0.140 26.443 1.00 17.54 C ANISOU 1672 CA ARG A 204 1537 2439 2686 -283 -14 -198 C ATOM 1673 C ARG A 204 24.461 0.007 26.361 1.00 16.70 C ANISOU 1673 C ARG A 204 1690 2137 2515 -375 106 -156 C ATOM 1674 O ARG A 204 24.986 -1.097 26.437 1.00 17.80 O ANISOU 1674 O ARG A 204 2422 1845 2495 -312 -468 -399 O ATOM 1675 CB ARG A 204 22.328 -0.138 25.073 1.00 23.41 C ANISOU 1675 CB ARG A 204 2440 3567 2887 -278 -365 -438 C ATOM 1676 CG ARG A 204 22.829 0.795 23.989 1.00 30.18 C ANISOU 1676 CG ARG A 204 3687 4618 3162 -277 -558 -477 C ATOM 1677 CD ARG A 204 22.227 0.461 22.639 1.00 36.70 C ANISOU 1677 CD ARG A 204 4895 5491 3556 -26 -76 -379 C ATOM 1678 NE ARG A 204 23.075 0.936 21.549 1.00 42.63 N ANISOU 1678 NE ARG A 204 5984 6265 3946 318 55 -172 N ATOM 1679 CZ ARG A 204 24.179 0.316 21.140 1.00 44.30 C ANISOU 1679 CZ ARG A 204 6075 6542 4215 608 333 41 C ATOM 1680 NH1 ARG A 204 24.574 -0.805 21.733 1.00 44.53 N ANISOU 1680 NH1 ARG A 204 6106 6455 4357 717 273 -4 N ATOM 1681 NH2 ARG A 204 24.890 0.819 20.138 1.00 44.66 N ANISOU 1681 NH2 ARG A 204 5997 6677 4294 536 496 283 N ATOM 1682 N AARG A 205 25.160 1.131 26.212 0.50 16.40 N ANISOU 1682 N AARG A 205 1342 2311 2575 -572 173 163 N ATOM 1683 N BARG A 205 25.157 1.133 26.216 0.50 16.66 N ANISOU 1683 N BARG A 205 1561 2249 2519 -470 225 70 N ATOM 1684 CA AARG A 205 26.613 1.109 26.057 0.50 15.73 C ANISOU 1684 CA AARG A 205 963 2367 2645 -255 196 465 C ATOM 1685 CA BARG A 205 26.610 1.118 26.053 0.50 16.08 C ANISOU 1685 CA BARG A 205 1416 2187 2506 -76 317 232 C ATOM 1686 C AARG A 205 27.353 0.995 27.385 0.50 16.66 C ANISOU 1686 C AARG A 205 1411 2291 2625 -301 20 202 C ATOM 1687 C BARG A 205 27.363 1.070 27.379 0.50 16.20 C ANISOU 1687 C BARG A 205 1478 2087 2588 -86 76 -28 C ATOM 1688 O AARG A 205 28.552 0.736 27.404 0.50 18.57 O ANISOU 1688 O AARG A 205 1845 2504 2706 -235 -93 75 O ATOM 1689 O BARG A 205 28.582 0.937 27.389 0.50 16.46 O ANISOU 1689 O BARG A 205 1514 2031 2707 110 -53 -362 O ATOM 1690 CB AARG A 205 27.097 2.359 25.319 0.50 16.60 C ANISOU 1690 CB AARG A 205 1058 2522 2727 -163 159 563 C ATOM 1691 CB BARG A 205 27.080 2.337 25.254 0.50 17.42 C ANISOU 1691 CB BARG A 205 2087 2146 2386 -22 395 200 C ATOM 1692 CG AARG A 205 26.673 2.442 23.862 0.50 17.15 C ANISOU 1692 CG AARG A 205 1074 2743 2699 -183 139 810 C ATOM 1693 CG BARG A 205 26.520 2.427 23.844 0.50 18.22 C ANISOU 1693 CG BARG A 205 2592 2181 2147 -65 592 367 C ATOM 1694 CD AARG A 205 27.502 3.489 23.143 0.50 19.20 C ANISOU 1694 CD AARG A 205 1141 3222 2931 -615 28 766 C ATOM 1695 CD BARG A 205 27.162 3.575 23.082 0.50 20.49 C ANISOU 1695 CD BARG A 205 3055 2532 2196 -171 614 367 C ATOM 1696 NE AARG A 205 28.916 3.133 23.175 0.50 20.12 N ANISOU 1696 NE AARG A 205 996 3616 3031 -1220 341 609 N ATOM 1697 NE BARG A 205 26.523 3.804 21.790 0.50 20.69 N ANISOU 1697 NE BARG A 205 3309 2530 2021 -187 791 159 N ATOM 1698 CZ AARG A 205 29.911 4.010 23.228 0.50 21.56 C ANISOU 1698 CZ AARG A 205 1211 3799 3179 -1496 201 290 C ATOM 1699 CZ BARG A 205 26.759 3.084 20.698 0.50 22.19 C ANISOU 1699 CZ BARG A 205 3107 3134 2190 196 1171 270 C ATOM 1700 NH1AARG A 205 29.657 5.312 23.259 0.50 22.56 N ANISOU 1700 NH1AARG A 205 1649 3737 3183 -1440 164 -105 N ATOM 1701 NH1BARG A 205 27.616 2.074 20.736 0.50 20.80 N ANISOU 1701 NH1BARG A 205 2728 3028 2144 377 1582 139 N ATOM 1702 NH2AARG A 205 31.165 3.580 23.257 0.50 23.75 N ANISOU 1702 NH2AARG A 205 1506 4239 3276 -1074 220 412 N ATOM 1703 NH2BARG A 205 26.130 3.367 19.567 0.50 23.89 N ANISOU 1703 NH2BARG A 205 3401 3400 2274 586 1151 568 N ATOM 1704 N LYS A 206 26.648 1.203 28.492 1.00 17.86 N ANISOU 1704 N LYS A 206 1721 2364 2699 -345 -101 136 N ATOM 1705 CA LYS A 206 27.284 1.175 29.812 1.00 16.90 C ANISOU 1705 CA LYS A 206 1560 2159 2700 -153 -217 96 C ATOM 1706 C LYS A 206 27.625 -0.246 30.243 1.00 16.35 C ANISOU 1706 C LYS A 206 1580 2223 2408 -347 -167 300 C ATOM 1707 O LYS A 206 26.805 -1.148 30.105 1.00 17.16 O ANISOU 1707 O LYS A 206 1795 2394 2330 -779 -215 54 O ATOM 1708 CB LYS A 206 26.393 1.838 30.866 1.00 24.13 C ANISOU 1708 CB LYS A 206 2677 3023 3467 144 647 -150 C ATOM 1709 CG LYS A 206 26.340 3.355 30.759 1.00 31.89 C ANISOU 1709 CG LYS A 206 4034 4210 3873 436 1134 -388 C ATOM 1710 CD LYS A 206 25.436 3.963 31.819 1.00 36.05 C ANISOU 1710 CD LYS A 206 4661 4903 4132 665 1482 -562 C ATOM 1711 CE LYS A 206 25.835 3.517 33.205 1.00 39.10 C ANISOU 1711 CE LYS A 206 5083 5456 4317 595 1786 -608 C ATOM 1712 NZ LYS A 206 25.231 4.409 34.237 1.00 40.73 N ANISOU 1712 NZ LYS A 206 5152 5815 4509 538 1906 -660 N ATOM 1713 N VAL A 207 28.829 -0.449 30.766 1.00 16.79 N ANISOU 1713 N VAL A 207 1640 2220 2517 43 -262 431 N ATOM 1714 CA VAL A 207 29.188 -1.771 31.276 1.00 14.89 C ANISOU 1714 CA VAL A 207 1270 1980 2407 -122 -326 93 C ATOM 1715 C VAL A 207 28.238 -2.173 32.396 1.00 13.02 C ANISOU 1715 C VAL A 207 1300 1634 2013 -333 -150 -248 C ATOM 1716 O VAL A 207 27.742 -1.328 33.145 1.00 14.76 O ANISOU 1716 O VAL A 207 2054 1815 1739 -201 -113 -279 O ATOM 1717 CB VAL A 207 30.646 -1.851 31.757 1.00 17.65 C ANISOU 1717 CB VAL A 207 1638 2247 2821 -597 -157 -3 C ATOM 1718 CG1 VAL A 207 31.584 -1.667 30.581 1.00 20.10 C ANISOU 1718 CG1 VAL A 207 2227 2311 3097 -446 -35 192 C ATOM 1719 CG2 VAL A 207 30.914 -0.820 32.841 1.00 19.85 C ANISOU 1719 CG2 VAL A 207 1627 2959 2956 -811 -450 75 C ATOM 1720 N LEU A 208 27.980 -3.469 32.500 1.00 11.85 N ANISOU 1720 N LEU A 208 1231 1515 1754 -353 -38 -72 N ATOM 1721 CA LEU A 208 26.939 -3.958 33.391 1.00 13.57 C ANISOU 1721 CA LEU A 208 1635 1727 1793 -595 -23 -627 C ATOM 1722 C LEU A 208 27.197 -3.680 34.875 1.00 13.87 C ANISOU 1722 C LEU A 208 1856 1712 1702 -250 -315 -450 C ATOM 1723 O LEU A 208 26.255 -3.553 35.653 1.00 15.55 O ANISOU 1723 O LEU A 208 2181 2126 1599 137 87 -401 O ATOM 1724 CB LEU A 208 26.681 -5.448 33.151 1.00 14.26 C ANISOU 1724 CB LEU A 208 1772 1834 1810 -165 -35 -576 C ATOM 1725 CG LEU A 208 25.868 -5.737 31.887 1.00 12.79 C ANISOU 1725 CG LEU A 208 1119 2016 1723 158 256 -337 C ATOM 1726 CD1 LEU A 208 26.016 -7.204 31.518 1.00 15.04 C ANISOU 1726 CD1 LEU A 208 2281 1989 1444 193 189 -392 C ATOM 1727 CD2 LEU A 208 24.393 -5.352 32.067 1.00 15.41 C ANISOU 1727 CD2 LEU A 208 1493 2294 2066 133 98 -40 C ATOM 1728 N ARG A 209 28.460 -3.581 35.273 1.00 14.26 N ANISOU 1728 N ARG A 209 1700 2063 1652 -318 -582 -463 N ATOM 1729 CA ARG A 209 28.768 -3.321 36.677 1.00 17.08 C ANISOU 1729 CA ARG A 209 2082 2532 1873 -106 -573 -405 C ATOM 1730 C ARG A 209 28.287 -1.936 37.125 1.00 16.19 C ANISOU 1730 C ARG A 209 2290 2139 1720 -487 -385 -283 C ATOM 1731 O ARG A 209 28.221 -1.653 38.319 1.00 21.07 O ANISOU 1731 O ARG A 209 3299 2829 1875 7 -188 -476 O ATOM 1732 CB ARG A 209 30.262 -3.488 36.957 1.00 20.25 C ANISOU 1732 CB ARG A 209 2046 3239 2408 67 -604 -183 C ATOM 1733 CG ARG A 209 31.145 -2.487 36.239 1.00 24.18 C ANISOU 1733 CG ARG A 209 2125 4030 3031 -784 -743 -10 C ATOM 1734 CD ARG A 209 32.615 -2.686 36.578 1.00 30.85 C ANISOU 1734 CD ARG A 209 3164 4842 3715 -1045 -590 298 C ATOM 1735 NE ARG A 209 33.467 -1.976 35.629 1.00 38.26 N ANISOU 1735 NE ARG A 209 4471 5695 4368 -989 -554 298 N ATOM 1736 CZ ARG A 209 33.711 -0.669 35.680 1.00 42.84 C ANISOU 1736 CZ ARG A 209 5408 6155 4711 -1137 -336 337 C ATOM 1737 NH1 ARG A 209 33.172 0.073 36.639 1.00 44.18 N ANISOU 1737 NH1 ARG A 209 5736 6141 4909 -1066 -374 136 N ATOM 1738 NH2 ARG A 209 34.496 -0.103 34.774 1.00 45.41 N ANISOU 1738 NH2 ARG A 209 5929 6574 4750 -1040 -261 548 N ATOM 1739 N LYS A 210 27.970 -1.069 36.167 1.00 16.04 N ANISOU 1739 N LYS A 210 2345 2068 1681 60 -217 -92 N ATOM 1740 CA LYS A 210 27.435 0.248 36.503 1.00 16.36 C ANISOU 1740 CA LYS A 210 2377 1824 2015 -354 168 -112 C ATOM 1741 C LYS A 210 25.917 0.214 36.632 1.00 18.76 C ANISOU 1741 C LYS A 210 3097 1951 2080 194 261 -388 C ATOM 1742 O LYS A 210 25.302 1.191 37.061 1.00 22.02 O ANISOU 1742 O LYS A 210 4038 2151 2175 610 530 -428 O ATOM 1743 CB LYS A 210 27.842 1.287 35.460 1.00 19.32 C ANISOU 1743 CB LYS A 210 2775 2032 2534 -788 276 -540 C ATOM 1744 CG LYS A 210 29.333 1.540 35.406 1.00 25.15 C ANISOU 1744 CG LYS A 210 3547 2738 3271 -1105 286 -352 C ATOM 1745 CD LYS A 210 29.699 2.343 34.175 1.00 29.42 C ANISOU 1745 CD LYS A 210 3869 3433 3876 -1561 437 -226 C ATOM 1746 CE LYS A 210 31.111 2.895 34.286 1.00 34.49 C ANISOU 1746 CE LYS A 210 4745 4046 4314 -1481 219 -157 C ATOM 1747 NZ LYS A 210 31.470 3.745 33.117 1.00 36.56 N ANISOU 1747 NZ LYS A 210 5311 4057 4520 -1554 187 -13 N ATOM 1748 N LYS A 211 25.322 -0.918 36.263 1.00 16.95 N ANISOU 1748 N LYS A 211 2981 1669 1787 -152 -95 -532 N ATOM 1749 CA LYS A 211 23.865 -1.063 36.240 1.00 16.68 C ANISOU 1749 CA LYS A 211 2595 1983 1760 -45 127 -397 C ATOM 1750 C LYS A 211 23.352 -2.153 37.181 1.00 17.43 C ANISOU 1750 C LYS A 211 2316 2436 1869 22 252 -204 C ATOM 1751 O LYS A 211 22.194 -2.130 37.595 1.00 20.64 O ANISOU 1751 O LYS A 211 2497 3170 2172 750 354 280 O ATOM 1752 CB LYS A 211 23.396 -1.372 34.816 1.00 17.87 C ANISOU 1752 CB LYS A 211 2491 2508 1790 -213 -497 -206 C ATOM 1753 CG LYS A 211 23.654 -0.244 33.833 1.00 21.35 C ANISOU 1753 CG LYS A 211 3388 2769 1954 -11 -632 -212 C ATOM 1754 CD LYS A 211 22.820 -0.399 32.583 1.00 22.50 C ANISOU 1754 CD LYS A 211 3158 2999 2392 -336 -348 -200 C ATOM 1755 CE LYS A 211 23.452 -1.325 31.591 1.00 20.42 C ANISOU 1755 CE LYS A 211 2439 2684 2634 -432 51 -134 C ATOM 1756 NZ LYS A 211 22.789 -1.164 30.273 1.00 15.73 N ANISOU 1756 NZ LYS A 211 1676 1781 2517 -281 -267 -22 N ATOM 1757 N ILE A 212 24.219 -3.112 37.486 1.00 16.83 N ANISOU 1757 N ILE A 212 2202 2280 1910 341 58 6 N ATOM 1758 CA ILE A 212 23.888 -4.231 38.367 1.00 16.39 C ANISOU 1758 CA ILE A 212 2029 2139 2059 -73 -151 -186 C ATOM 1759 C ILE A 212 25.055 -4.410 39.325 1.00 16.03 C ANISOU 1759 C ILE A 212 1677 2415 1999 -216 -92 -264 C ATOM 1760 O ILE A 212 26.212 -4.420 38.888 1.00 16.78 O ANISOU 1760 O ILE A 212 1718 2532 2126 -508 13 -184 O ATOM 1761 CB ILE A 212 23.730 -5.552 37.563 1.00 16.90 C ANISOU 1761 CB ILE A 212 1829 2277 2314 -336 -294 -123 C ATOM 1762 CG1 ILE A 212 22.650 -5.422 36.481 1.00 18.68 C ANISOU 1762 CG1 ILE A 212 2044 2354 2697 -167 92 104 C ATOM 1763 CG2 ILE A 212 23.450 -6.735 38.498 1.00 20.35 C ANISOU 1763 CG2 ILE A 212 2020 3196 2513 -586 -106 -123 C ATOM 1764 CD1 ILE A 212 21.244 -5.337 37.022 1.00 21.47 C ANISOU 1764 CD1 ILE A 212 2621 2471 3065 -375 220 184 C ATOM 1765 N PRO A 213 24.778 -4.548 40.631 1.00 16.37 N ANISOU 1765 N PRO A 213 1754 2563 1900 287 346 9 N ATOM 1766 CA PRO A 213 25.905 -4.713 41.559 1.00 18.00 C ANISOU 1766 CA PRO A 213 2224 2727 1886 318 241 6 C ATOM 1767 C PRO A 213 26.821 -5.870 41.147 1.00 17.74 C ANISOU 1767 C PRO A 213 2121 2515 2103 374 6 -172 C ATOM 1768 O PRO A 213 26.336 -6.958 40.850 1.00 17.24 O ANISOU 1768 O PRO A 213 2092 2241 2217 -10 -243 -166 O ATOM 1769 CB PRO A 213 25.214 -5.031 42.894 1.00 17.97 C ANISOU 1769 CB PRO A 213 2080 2968 1780 425 427 -34 C ATOM 1770 CG PRO A 213 23.883 -4.369 42.788 1.00 20.39 C ANISOU 1770 CG PRO A 213 2343 3510 1893 165 115 45 C ATOM 1771 CD PRO A 213 23.483 -4.489 41.335 1.00 18.98 C ANISOU 1771 CD PRO A 213 2341 3306 1565 305 190 50 C ATOM 1772 N GLU A 214 28.129 -5.629 41.141 1.00 19.11 N ANISOU 1772 N GLU A 214 1782 2937 2539 392 -156 -435 N ATOM 1773 CA GLU A 214 29.111 -6.636 40.715 1.00 22.10 C ANISOU 1773 CA GLU A 214 1860 3412 3122 159 -402 -525 C ATOM 1774 C GLU A 214 28.921 -7.993 41.398 1.00 22.65 C ANISOU 1774 C GLU A 214 2338 3213 3054 253 -435 -187 C ATOM 1775 O GLU A 214 29.095 -9.038 40.773 1.00 23.51 O ANISOU 1775 O GLU A 214 2541 3318 3073 207 -600 56 O ATOM 1776 CB GLU A 214 30.539 -6.129 40.947 1.00 27.89 C ANISOU 1776 CB GLU A 214 2407 4386 3801 461 -122 -653 C ATOM 1777 CG GLU A 214 31.607 -6.936 40.221 1.00 36.16 C ANISOU 1777 CG GLU A 214 4014 5321 4404 246 -61 -772 C ATOM 1778 CD GLU A 214 32.945 -6.211 40.147 1.00 44.82 C ANISOU 1778 CD GLU A 214 5701 6455 4872 16 -92 -961 C ATOM 1779 OE1 GLU A 214 33.213 -5.363 41.023 1.00 47.94 O ANISOU 1779 OE1 GLU A 214 6292 6763 5159 29 -114 -1005 O ATOM 1780 OE2 GLU A 214 33.731 -6.490 39.213 1.00 49.40 O ANISOU 1780 OE2 GLU A 214 6564 7100 5104 -273 -131 -856 O ATOM 1781 N GLU A 215 28.577 -7.963 42.681 1.00 22.00 N ANISOU 1781 N GLU A 215 2876 2821 2660 218 -777 -155 N ATOM 1782 CA GLU A 215 28.299 -9.172 43.455 1.00 26.96 C ANISOU 1782 CA GLU A 215 4034 3371 2837 -394 -749 4 C ATOM 1783 C GLU A 215 27.308 -10.100 42.743 1.00 26.17 C ANISOU 1783 C GLU A 215 4121 3118 2703 -475 -948 294 C ATOM 1784 O GLU A 215 27.533 -11.310 42.646 1.00 26.29 O ANISOU 1784 O GLU A 215 4085 3269 2632 -879 -1406 522 O ATOM 1785 CB GLU A 215 27.761 -8.778 44.836 1.00 33.65 C ANISOU 1785 CB GLU A 215 5627 3990 3167 -268 -558 144 C ATOM 1786 CG GLU A 215 27.418 -9.931 45.757 1.00 40.63 C ANISOU 1786 CG GLU A 215 6784 4949 3703 -47 -259 28 C ATOM 1787 CD GLU A 215 26.762 -9.457 47.046 1.00 46.84 C ANISOU 1787 CD GLU A 215 8011 5555 4231 -33 -185 192 C ATOM 1788 OE1 GLU A 215 26.240 -8.317 47.065 1.00 46.03 O ANISOU 1788 OE1 GLU A 215 8259 4887 4342 583 40 41 O ATOM 1789 OE2 GLU A 215 26.767 -10.221 48.038 1.00 50.34 O ANISOU 1789 OE2 GLU A 215 8506 6169 4449 -385 -353 294 O ATOM 1790 N LEU A 216 26.213 -9.530 42.240 1.00 22.91 N ANISOU 1790 N LEU A 216 3282 2789 2634 32 -1036 385 N ATOM 1791 CA LEU A 216 25.192 -10.326 41.552 1.00 21.84 C ANISOU 1791 CA LEU A 216 2825 2884 2587 156 -534 323 C ATOM 1792 C LEU A 216 25.665 -10.810 40.179 1.00 20.73 C ANISOU 1792 C LEU A 216 2867 2364 2645 -165 -190 180 C ATOM 1793 O LEU A 216 25.351 -11.927 39.767 1.00 21.68 O ANISOU 1793 O LEU A 216 3044 2429 2762 -693 -422 385 O ATOM 1794 CB LEU A 216 23.877 -9.545 41.417 1.00 21.26 C ANISOU 1794 CB LEU A 216 2474 3002 2601 593 -109 163 C ATOM 1795 CG LEU A 216 23.250 -9.028 42.715 1.00 24.08 C ANISOU 1795 CG LEU A 216 3060 3227 2860 618 121 147 C ATOM 1796 CD1 LEU A 216 21.981 -8.265 42.409 1.00 25.15 C ANISOU 1796 CD1 LEU A 216 3066 3514 2975 507 143 260 C ATOM 1797 CD2 LEU A 216 22.964 -10.170 43.687 1.00 26.49 C ANISOU 1797 CD2 LEU A 216 3351 3694 3018 444 277 -89 C ATOM 1798 N LEU A 217 26.406 -9.964 39.465 1.00 19.84 N ANISOU 1798 N LEU A 217 2738 2224 2576 210 -474 132 N ATOM 1799 CA LEU A 217 26.963 -10.349 38.169 1.00 19.41 C ANISOU 1799 CA LEU A 217 2957 1991 2427 -92 -716 117 C ATOM 1800 C LEU A 217 27.907 -11.549 38.293 1.00 21.76 C ANISOU 1800 C LEU A 217 3423 2168 2676 -189 -855 32 C ATOM 1801 O LEU A 217 27.849 -12.481 37.490 1.00 21.54 O ANISOU 1801 O LEU A 217 3600 2030 2554 -359 -391 -102 O ATOM 1802 CB LEU A 217 27.681 -9.164 37.511 1.00 19.44 C ANISOU 1802 CB LEU A 217 2933 2039 2414 -7 -497 134 C ATOM 1803 CG LEU A 217 26.773 -8.006 37.085 1.00 16.09 C ANISOU 1803 CG LEU A 217 2160 1644 2308 9 -446 -129 C ATOM 1804 CD1 LEU A 217 27.600 -6.793 36.651 1.00 17.32 C ANISOU 1804 CD1 LEU A 217 2519 1909 2150 -251 -68 -9 C ATOM 1805 CD2 LEU A 217 25.814 -8.435 35.967 1.00 14.81 C ANISOU 1805 CD2 LEU A 217 1800 1562 2265 200 -703 -139 C ATOM 1806 N LYS A 218 28.772 -11.530 39.303 1.00 24.53 N ANISOU 1806 N LYS A 218 3508 2562 3249 137 -956 42 N ATOM 1807 CA LYS A 218 29.706 -12.630 39.512 1.00 27.12 C ANISOU 1807 CA LYS A 218 3887 2587 3828 451 -857 -136 C ATOM 1808 C LYS A 218 28.963 -13.914 39.852 1.00 27.73 C ANISOU 1808 C LYS A 218 4171 2505 3859 446 -1071 113 C ATOM 1809 O LYS A 218 29.317 -14.993 39.377 1.00 27.97 O ANISOU 1809 O LYS A 218 4366 2153 4107 588 -923 -103 O ATOM 1810 CB LYS A 218 30.701 -12.296 40.620 1.00 29.46 C ANISOU 1810 CB LYS A 218 3663 3176 4354 599 -688 -244 C ATOM 1811 CG LYS A 218 31.784 -11.320 40.209 1.00 35.74 C ANISOU 1811 CG LYS A 218 4551 4215 4812 614 -403 -51 C ATOM 1812 CD LYS A 218 32.620 -10.916 41.414 1.00 40.55 C ANISOU 1812 CD LYS A 218 5239 5080 5088 515 -391 246 C ATOM 1813 CE LYS A 218 33.958 -10.326 41.001 1.00 45.87 C ANISOU 1813 CE LYS A 218 6397 5691 5338 434 -262 654 C ATOM 1814 NZ LYS A 218 33.802 -9.121 40.141 1.00 49.04 N ANISOU 1814 NZ LYS A 218 6901 6143 5588 597 -278 690 N ATOM 1815 N GLU A 219 27.925 -13.791 40.671 1.00 28.32 N ANISOU 1815 N GLU A 219 4355 2612 3793 33 -1195 579 N ATOM 1816 CA GLU A 219 27.111 -14.938 41.051 1.00 30.77 C ANISOU 1816 CA GLU A 219 4676 3134 3881 -107 -1036 775 C ATOM 1817 C GLU A 219 26.409 -15.556 39.843 1.00 28.10 C ANISOU 1817 C GLU A 219 4461 2618 3595 -503 -991 936 C ATOM 1818 O GLU A 219 26.193 -16.773 39.793 1.00 31.00 O ANISOU 1818 O GLU A 219 5164 3038 3576 -580 -1081 760 O ATOM 1819 CB GLU A 219 26.090 -14.523 42.109 1.00 35.57 C ANISOU 1819 CB GLU A 219 5164 4084 4264 -94 -846 776 C ATOM 1820 CG GLU A 219 25.196 -15.643 42.580 1.00 43.27 C ANISOU 1820 CG GLU A 219 6577 5074 4789 -168 -881 545 C ATOM 1821 CD GLU A 219 24.509 -15.315 43.890 1.00 50.30 C ANISOU 1821 CD GLU A 219 7781 5987 5344 -308 -806 387 C ATOM 1822 OE1 GLU A 219 24.603 -14.149 44.337 1.00 51.46 O ANISOU 1822 OE1 GLU A 219 7876 6187 5487 -311 -992 381 O ATOM 1823 OE2 GLU A 219 23.880 -16.225 44.475 1.00 54.33 O ANISOU 1823 OE2 GLU A 219 8546 6473 5622 -399 -803 251 O ATOM 1824 N ALA A 220 26.055 -14.716 38.873 1.00 26.70 N ANISOU 1824 N ALA A 220 3942 2842 3361 -460 -901 823 N ATOM 1825 CA ALA A 220 25.406 -15.183 37.652 1.00 25.81 C ANISOU 1825 CA ALA A 220 3816 2496 3492 -326 -600 642 C ATOM 1826 C ALA A 220 26.429 -15.619 36.602 1.00 27.18 C ANISOU 1826 C ALA A 220 3959 2651 3714 -72 -660 397 C ATOM 1827 O ALA A 220 26.062 -16.042 35.505 1.00 28.82 O ANISOU 1827 O ALA A 220 4163 2980 3805 -73 -527 232 O ATOM 1828 CB ALA A 220 24.501 -14.098 37.086 1.00 24.98 C ANISOU 1828 CB ALA A 220 3576 2566 3348 -62 -327 793 C ATOM 1829 N GLY A 221 27.710 -15.503 36.936 1.00 25.19 N ANISOU 1829 N GLY A 221 3452 2383 3735 401 -693 336 N ATOM 1830 CA GLY A 221 28.767 -15.895 36.023 1.00 26.26 C ANISOU 1830 CA GLY A 221 3837 2591 3548 57 -676 351 C ATOM 1831 C GLY A 221 28.931 -14.940 34.856 1.00 27.34 C ANISOU 1831 C GLY A 221 4278 2736 3372 601 -819 38 C ATOM 1832 O GLY A 221 29.366 -15.332 33.773 1.00 29.34 O ANISOU 1832 O GLY A 221 4801 2893 3451 862 -744 -200 O ATOM 1833 N ILE A 222 28.592 -13.677 35.083 1.00 23.93 N ANISOU 1833 N ILE A 222 3421 2576 3095 378 -1010 -182 N ATOM 1834 CA ILE A 222 28.672 -12.666 34.043 1.00 22.46 C ANISOU 1834 CA ILE A 222 3018 2499 3014 462 -810 -370 C ATOM 1835 C ILE A 222 29.860 -11.740 34.278 1.00 21.77 C ANISOU 1835 C ILE A 222 2853 2521 2895 775 -686 -92 C ATOM 1836 O ILE A 222 30.104 -11.293 35.401 1.00 23.73 O ANISOU 1836 O ILE A 222 3273 2910 2832 498 -1026 -11 O ATOM 1837 CB ILE A 222 27.369 -11.844 33.992 1.00 21.79 C ANISOU 1837 CB ILE A 222 2773 2593 2912 202 -763 -306 C ATOM 1838 CG1 ILE A 222 26.178 -12.770 33.759 1.00 20.77 C ANISOU 1838 CG1 ILE A 222 2490 2473 2927 6 -360 -90 C ATOM 1839 CG2 ILE A 222 27.445 -10.750 32.925 1.00 21.45 C ANISOU 1839 CG2 ILE A 222 2844 2369 2937 559 -872 -271 C ATOM 1840 CD1 ILE A 222 24.849 -12.101 33.981 1.00 18.95 C ANISOU 1840 CD1 ILE A 222 1809 2536 2853 276 -214 518 C ATOM 1841 N ASN A 223 30.605 -11.467 33.214 1.00 21.87 N ANISOU 1841 N ASN A 223 2826 2490 2994 486 -518 39 N ATOM 1842 CA ASN A 223 31.719 -10.533 33.276 1.00 22.85 C ANISOU 1842 CA ASN A 223 2804 2972 2903 635 -350 -181 C ATOM 1843 C ASN A 223 31.196 -9.141 33.614 1.00 22.06 C ANISOU 1843 C ASN A 223 2739 3107 2533 655 -561 -248 C ATOM 1844 O ASN A 223 30.356 -8.604 32.895 1.00 20.19 O ANISOU 1844 O ASN A 223 2360 2786 2524 478 -278 -261 O ATOM 1845 CB ASN A 223 32.459 -10.533 31.934 1.00 25.60 C ANISOU 1845 CB ASN A 223 2858 3559 3307 765 -94 -283 C ATOM 1846 CG ASN A 223 33.726 -9.709 31.961 1.00 28.78 C ANISOU 1846 CG ASN A 223 3005 4238 3690 1300 125 -349 C ATOM 1847 OD1 ASN A 223 33.856 -8.769 32.741 1.00 28.70 O ANISOU 1847 OD1 ASN A 223 2380 4449 4073 937 59 -445 O ATOM 1848 ND2 ASN A 223 34.674 -10.062 31.104 1.00 32.27 N ANISOU 1848 ND2 ASN A 223 3857 4759 3643 1218 332 -257 N ATOM 1849 N PRO A 224 31.674 -8.554 34.722 1.00 22.64 N ANISOU 1849 N PRO A 224 2908 3467 2225 1042 -938 -210 N ATOM 1850 CA PRO A 224 31.193 -7.223 35.120 1.00 22.44 C ANISOU 1850 CA PRO A 224 3257 3240 2027 448 -888 -300 C ATOM 1851 C PRO A 224 31.397 -6.162 34.035 1.00 18.22 C ANISOU 1851 C PRO A 224 1770 2752 2399 12 -414 -303 C ATOM 1852 O PRO A 224 30.720 -5.133 34.055 1.00 19.16 O ANISOU 1852 O PRO A 224 1699 2926 2652 -20 -375 -474 O ATOM 1853 CB PRO A 224 32.046 -6.895 36.354 1.00 24.94 C ANISOU 1853 CB PRO A 224 4065 3530 1880 496 -1452 -148 C ATOM 1854 CG PRO A 224 32.442 -8.224 36.894 1.00 27.12 C ANISOU 1854 CG PRO A 224 4498 3649 2155 358 -1182 92 C ATOM 1855 CD PRO A 224 32.617 -9.119 35.703 1.00 25.93 C ANISOU 1855 CD PRO A 224 3889 3745 2217 516 -1150 28 C ATOM 1856 N ASP A 225 32.309 -6.414 33.100 1.00 18.00 N ANISOU 1856 N ASP A 225 1219 3109 2511 180 -275 -236 N ATOM 1857 CA ASP A 225 32.586 -5.459 32.033 1.00 21.25 C ANISOU 1857 CA ASP A 225 1394 3770 2910 -99 -233 -343 C ATOM 1858 C ASP A 225 31.860 -5.799 30.731 1.00 17.91 C ANISOU 1858 C ASP A 225 1148 3079 2577 103 64 -519 C ATOM 1859 O ASP A 225 32.037 -5.121 29.715 1.00 19.64 O ANISOU 1859 O ASP A 225 1577 3262 2623 -20 607 -727 O ATOM 1860 CB ASP A 225 34.092 -5.336 31.798 1.00 27.21 C ANISOU 1860 CB ASP A 225 1949 4877 3512 -179 -256 -730 C ATOM 1861 CG ASP A 225 34.788 -4.567 32.910 1.00 35.52 C ANISOU 1861 CG ASP A 225 3330 5791 4372 -137 -665 -1041 C ATOM 1862 OD1 ASP A 225 34.160 -3.651 33.486 1.00 36.40 O ANISOU 1862 OD1 ASP A 225 3424 5786 4619 -447 -729 -1176 O ATOM 1863 OD2 ASP A 225 35.959 -4.876 33.211 1.00 42.51 O ANISOU 1863 OD2 ASP A 225 5004 6398 4749 -89 -813 -973 O ATOM 1864 N ALA A 226 31.042 -6.846 30.762 1.00 14.67 N ANISOU 1864 N ALA A 226 1043 2199 2331 302 -116 -783 N ATOM 1865 CA ALA A 226 30.168 -7.141 29.635 1.00 14.97 C ANISOU 1865 CA ALA A 226 1308 2213 2167 498 53 -372 C ATOM 1866 C ALA A 226 29.094 -6.061 29.524 1.00 14.32 C ANISOU 1866 C ALA A 226 1228 2286 1927 437 82 -209 C ATOM 1867 O ALA A 226 28.869 -5.288 30.463 1.00 13.09 O ANISOU 1867 O ALA A 226 1078 2143 1751 272 79 -190 O ATOM 1868 CB ALA A 226 29.521 -8.513 29.797 1.00 15.41 C ANISOU 1868 CB ALA A 226 1635 1948 2269 41 454 15 C ATOM 1869 N ARG A 227 28.454 -6.000 28.362 1.00 12.90 N ANISOU 1869 N ARG A 227 1020 2290 1589 407 -228 119 N ATOM 1870 CA ARG A 227 27.348 -5.079 28.130 1.00 11.72 C ANISOU 1870 CA ARG A 227 923 1748 1781 -165 -320 79 C ATOM 1871 C ARG A 227 26.071 -5.857 27.888 1.00 11.02 C ANISOU 1871 C ARG A 227 955 1635 1594 -93 -40 -20 C ATOM 1872 O ARG A 227 26.113 -7.040 27.538 1.00 12.32 O ANISOU 1872 O ARG A 227 1112 1851 1718 2 -16 -304 O ATOM 1873 CB ARG A 227 27.653 -4.147 26.960 1.00 13.11 C ANISOU 1873 CB ARG A 227 970 2065 1945 -399 -194 102 C ATOM 1874 CG ARG A 227 28.642 -3.050 27.323 1.00 14.25 C ANISOU 1874 CG ARG A 227 783 2384 2247 -724 125 205 C ATOM 1875 CD ARG A 227 29.202 -2.374 26.083 1.00 16.81 C ANISOU 1875 CD ARG A 227 1436 2397 2554 -1036 417 141 C ATOM 1876 NE ARG A 227 30.043 -1.222 26.401 1.00 17.94 N ANISOU 1876 NE ARG A 227 1496 2428 2891 -255 270 123 N ATOM 1877 CZ ARG A 227 31.368 -1.263 26.516 1.00 18.05 C ANISOU 1877 CZ ARG A 227 1417 2140 3298 -279 372 -399 C ATOM 1878 NH1 ARG A 227 32.017 -2.408 26.344 1.00 20.32 N ANISOU 1878 NH1 ARG A 227 2133 2057 3528 47 672 -809 N ATOM 1879 NH2 ARG A 227 32.046 -0.155 26.800 1.00 21.63 N ANISOU 1879 NH2 ARG A 227 1980 2700 3538 -864 447 -190 N ATOM 1880 N VAL A 228 24.937 -5.196 28.094 1.00 9.59 N ANISOU 1880 N VAL A 228 585 1461 1595 -81 43 -145 N ATOM 1881 CA VAL A 228 23.644 -5.880 28.096 1.00 8.92 C ANISOU 1881 CA VAL A 228 536 1281 1569 -33 146 -75 C ATOM 1882 C VAL A 228 23.344 -6.675 26.816 1.00 9.43 C ANISOU 1882 C VAL A 228 858 1230 1492 -9 179 -4 C ATOM 1883 O VAL A 228 22.716 -7.736 26.870 1.00 10.20 O ANISOU 1883 O VAL A 228 967 1384 1524 48 -57 -86 O ATOM 1884 CB VAL A 228 22.474 -4.898 28.424 1.00 9.78 C ANISOU 1884 CB VAL A 228 545 1573 1598 59 358 -161 C ATOM 1885 CG1 VAL A 228 22.250 -3.873 27.295 1.00 10.60 C ANISOU 1885 CG1 VAL A 228 905 1587 1536 -157 -163 180 C ATOM 1886 CG2 VAL A 228 21.198 -5.669 28.721 1.00 12.07 C ANISOU 1886 CG2 VAL A 228 667 2102 1817 83 415 -362 C ATOM 1887 N GLU A 229 23.764 -6.159 25.668 1.00 10.46 N ANISOU 1887 N GLU A 229 1026 1699 1249 -167 136 -227 N ATOM 1888 CA GLU A 229 23.439 -6.801 24.392 1.00 11.96 C ANISOU 1888 CA GLU A 229 1551 1433 1558 45 196 -1 C ATOM 1889 C GLU A 229 24.159 -8.134 24.167 1.00 11.52 C ANISOU 1889 C GLU A 229 1323 1598 1453 -77 -86 -63 C ATOM 1890 O GLU A 229 23.830 -8.864 23.228 1.00 13.79 O ANISOU 1890 O GLU A 229 1710 2054 1475 -181 -61 -229 O ATOM 1891 CB GLU A 229 23.660 -5.832 23.218 1.00 16.33 C ANISOU 1891 CB GLU A 229 1965 1849 2390 -162 77 -113 C ATOM 1892 CG GLU A 229 22.620 -4.712 23.176 1.00 19.20 C ANISOU 1892 CG GLU A 229 2162 2165 2968 436 251 29 C ATOM 1893 CD GLU A 229 22.858 -3.700 22.067 1.00 28.31 C ANISOU 1893 CD GLU A 229 3458 3538 3759 787 581 192 C ATOM 1894 OE1 GLU A 229 23.834 -3.861 21.300 1.00 34.03 O ANISOU 1894 OE1 GLU A 229 4237 4511 4179 788 835 889 O ATOM 1895 OE2 GLU A 229 22.062 -2.739 21.955 1.00 29.04 O ANISOU 1895 OE2 GLU A 229 3437 3623 3974 546 364 136 O ATOM 1896 N GLN A 230 25.117 -8.460 25.035 1.00 11.46 N ANISOU 1896 N GLN A 230 1171 1569 1613 50 -29 137 N ATOM 1897 CA GLN A 230 25.835 -9.729 24.933 1.00 10.69 C ANISOU 1897 CA GLN A 230 491 1614 1955 -1 43 205 C ATOM 1898 C GLN A 230 25.281 -10.812 25.862 1.00 12.91 C ANISOU 1898 C GLN A 230 978 1902 2022 276 194 -16 C ATOM 1899 O GLN A 230 25.752 -11.949 25.841 1.00 14.40 O ANISOU 1899 O GLN A 230 1311 1909 2249 323 304 -166 O ATOM 1900 CB GLN A 230 27.334 -9.529 25.181 1.00 13.06 C ANISOU 1900 CB GLN A 230 1039 1692 2229 455 516 200 C ATOM 1901 CG GLN A 230 28.110 -9.108 23.929 1.00 12.83 C ANISOU 1901 CG GLN A 230 1126 1453 2293 -109 680 -141 C ATOM 1902 CD GLN A 230 27.771 -7.701 23.473 1.00 16.06 C ANISOU 1902 CD GLN A 230 1474 2373 2255 -137 303 -152 C ATOM 1903 OE1 GLN A 230 28.128 -6.721 24.128 1.00 16.34 O ANISOU 1903 OE1 GLN A 230 1126 2834 2248 120 127 -91 O ATOM 1904 NE2 GLN A 230 27.076 -7.595 22.342 1.00 17.46 N ANISOU 1904 NE2 GLN A 230 1544 2779 2310 -71 511 -258 N ATOM 1905 N LEU A 231 24.289 -10.468 26.678 1.00 12.07 N ANISOU 1905 N LEU A 231 1086 1638 1862 41 166 -153 N ATOM 1906 CA LEU A 231 23.725 -11.448 27.605 1.00 12.25 C ANISOU 1906 CA LEU A 231 1408 1512 1734 -230 -72 -369 C ATOM 1907 C LEU A 231 22.820 -12.447 26.882 1.00 13.22 C ANISOU 1907 C LEU A 231 1659 1543 1818 -493 -1 -657 C ATOM 1908 O LEU A 231 22.178 -12.110 25.887 1.00 14.80 O ANISOU 1908 O LEU A 231 1622 2144 1856 -218 -330 -209 O ATOM 1909 CB LEU A 231 22.921 -10.755 28.705 1.00 12.11 C ANISOU 1909 CB LEU A 231 1508 1421 1670 -12 -332 -218 C ATOM 1910 CG LEU A 231 23.698 -9.825 29.637 1.00 12.80 C ANISOU 1910 CG LEU A 231 1043 2019 1799 358 -427 -222 C ATOM 1911 CD1 LEU A 231 22.749 -9.329 30.723 1.00 14.20 C ANISOU 1911 CD1 LEU A 231 1413 2180 1801 584 233 -509 C ATOM 1912 CD2 LEU A 231 24.912 -10.530 30.246 1.00 14.87 C ANISOU 1912 CD2 LEU A 231 1690 1838 2121 174 -662 -121 C ATOM 1913 N SER A 232 22.762 -13.667 27.403 1.00 13.96 N ANISOU 1913 N SER A 232 1533 1544 2227 -480 -20 -436 N ATOM 1914 CA SER A 232 21.870 -14.699 26.886 1.00 14.22 C ANISOU 1914 CA SER A 232 1549 1471 2381 -237 -292 -264 C ATOM 1915 C SER A 232 20.537 -14.653 27.623 1.00 13.57 C ANISOU 1915 C SER A 232 1405 1360 2388 -97 -385 -450 C ATOM 1916 O SER A 232 20.432 -14.018 28.658 1.00 13.13 O ANISOU 1916 O SER A 232 1470 1412 2106 97 -264 -349 O ATOM 1917 CB SER A 232 22.497 -16.066 27.123 1.00 16.57 C ANISOU 1917 CB SER A 232 2213 1698 2382 258 -268 249 C ATOM 1918 OG SER A 232 22.485 -16.378 28.507 1.00 17.05 O ANISOU 1918 OG SER A 232 2247 1816 2415 8 -90 -195 O ATOM 1919 N ALEU A 233 19.512 -15.313 27.089 0.50 13.27 N ANISOU 1919 N ALEU A 233 1289 1301 2450 -230 -399 -348 N ATOM 1920 N BLEU A 233 19.536 -15.348 27.090 0.50 14.99 N ANISOU 1920 N BLEU A 233 1703 1373 2617 -202 -339 -446 N ATOM 1921 CA ALEU A 233 18.235 -15.377 27.800 0.50 13.39 C ANISOU 1921 CA ALEU A 233 1056 1689 2340 -385 -504 -387 C ATOM 1922 CA BLEU A 233 18.227 -15.426 27.733 0.50 16.90 C ANISOU 1922 CA BLEU A 233 1934 1803 2683 -252 -416 -574 C ATOM 1923 C ALEU A 233 18.445 -15.921 29.207 0.50 14.55 C ANISOU 1923 C ALEU A 233 1252 1777 2499 -330 -374 -384 C ATOM 1924 C BLEU A 233 18.320 -16.028 29.140 0.50 16.85 C ANISOU 1924 C BLEU A 233 1954 2003 2443 -105 -387 -705 C ATOM 1925 O ALEU A 233 17.925 -15.375 30.185 0.50 14.07 O ANISOU 1925 O ALEU A 233 1098 1542 2704 -420 -144 -420 O ATOM 1926 O BLEU A 233 17.600 -15.614 30.053 0.50 17.33 O ANISOU 1926 O BLEU A 233 2252 2149 2184 -89 -256 -1302 O ATOM 1927 CB ALEU A 233 17.227 -16.260 27.067 0.50 13.28 C ANISOU 1927 CB ALEU A 233 1315 1710 2019 -78 -357 -565 C ATOM 1928 CB BLEU A 233 17.264 -16.241 26.868 0.50 19.63 C ANISOU 1928 CB BLEU A 233 2581 1865 3012 -302 -357 -571 C ATOM 1929 CG ALEU A 233 16.670 -15.779 25.732 0.50 10.85 C ANISOU 1929 CG ALEU A 233 1302 1262 1557 343 -547 -832 C ATOM 1930 CG BLEU A 233 15.776 -16.113 27.169 0.50 21.10 C ANISOU 1930 CG BLEU A 233 3121 1641 3254 -335 -362 -525 C ATOM 1931 CD1ALEU A 233 15.670 -16.805 25.212 0.50 12.33 C ANISOU 1931 CD1ALEU A 233 1530 1489 1666 505 -635 -912 C ATOM 1932 CD1BLEU A 233 15.374 -14.655 27.224 0.50 20.83 C ANISOU 1932 CD1BLEU A 233 3213 1359 3342 245 -32 -806 C ATOM 1933 CD2ALEU A 233 16.029 -14.405 25.859 0.50 10.29 C ANISOU 1933 CD2ALEU A 233 1740 768 1402 71 -796 -681 C ATOM 1934 CD2BLEU A 233 14.969 -16.855 26.113 0.50 21.35 C ANISOU 1934 CD2BLEU A 233 2956 1867 3288 -1017 -518 -265 C ATOM 1935 N GLU A 234 19.207 -17.005 29.306 1.00 15.75 N ANISOU 1935 N GLU A 234 1795 1792 2397 35 -573 -305 N ATOM 1936 CA GLU A 234 19.461 -17.625 30.607 1.00 17.55 C ANISOU 1936 CA GLU A 234 1952 2108 2607 -154 -740 -18 C ATOM 1937 C GLU A 234 20.046 -16.604 31.589 1.00 15.84 C ANISOU 1937 C GLU A 234 1826 1963 2229 -603 -386 -77 C ATOM 1938 O GLU A 234 19.664 -16.578 32.764 1.00 16.71 O ANISOU 1938 O GLU A 234 2031 2155 2161 -496 -10 -134 O ATOM 1939 CB GLU A 234 20.384 -18.842 30.464 1.00 21.97 C ANISOU 1939 CB GLU A 234 3277 2107 2962 524 -914 487 C ATOM 1940 CG GLU A 234 20.634 -19.589 31.766 1.00 31.92 C ANISOU 1940 CG GLU A 234 5064 3290 3772 1275 -725 216 C ATOM 1941 CD GLU A 234 21.813 -20.551 31.686 1.00 41.46 C ANISOU 1941 CD GLU A 234 6737 4757 4258 1415 -573 219 C ATOM 1942 OE1 GLU A 234 22.437 -20.657 30.605 1.00 43.75 O ANISOU 1942 OE1 GLU A 234 7081 5165 4377 1754 -366 -62 O ATOM 1943 OE2 GLU A 234 22.120 -21.195 32.713 1.00 45.14 O ANISOU 1943 OE2 GLU A 234 7363 5319 4468 1249 -699 382 O ATOM 1944 N ASP A 235 20.957 -15.758 31.105 1.00 12.91 N ANISOU 1944 N ASP A 235 1245 1471 2189 -485 -252 -29 N ATOM 1945 CA ASP A 235 21.530 -14.692 31.935 1.00 12.83 C ANISOU 1945 CA ASP A 235 1461 1477 1934 -289 -277 89 C ATOM 1946 C ASP A 235 20.457 -13.766 32.485 1.00 12.38 C ANISOU 1946 C ASP A 235 1371 1724 1606 160 -208 10 C ATOM 1947 O ASP A 235 20.489 -13.379 33.660 1.00 13.14 O ANISOU 1947 O ASP A 235 1679 2033 1281 -126 -50 -307 O ATOM 1948 CB ASP A 235 22.526 -13.843 31.145 1.00 12.82 C ANISOU 1948 CB ASP A 235 1203 1597 2068 -47 -149 -239 C ATOM 1949 CG ASP A 235 23.770 -14.608 30.753 1.00 16.90 C ANISOU 1949 CG ASP A 235 1856 2289 2273 276 -299 -10 C ATOM 1950 OD1 ASP A 235 24.152 -15.556 31.481 1.00 19.31 O ANISOU 1950 OD1 ASP A 235 2067 2785 2485 264 -404 185 O ATOM 1951 OD2 ASP A 235 24.384 -14.244 29.727 1.00 18.79 O ANISOU 1951 OD2 ASP A 235 2068 2784 2287 -70 182 102 O ATOM 1952 N PHE A 236 19.528 -13.363 31.628 1.00 10.91 N ANISOU 1952 N PHE A 236 1277 1307 1558 44 -139 211 N ATOM 1953 CA PHE A 236 18.483 -12.441 32.062 1.00 11.39 C ANISOU 1953 CA PHE A 236 1274 1722 1329 292 38 46 C ATOM 1954 C PHE A 236 17.624 -13.068 33.139 1.00 12.64 C ANISOU 1954 C PHE A 236 1522 1618 1662 -84 -232 95 C ATOM 1955 O PHE A 236 17.265 -12.408 34.109 1.00 15.04 O ANISOU 1955 O PHE A 236 1799 2281 1635 -426 19 14 O ATOM 1956 CB PHE A 236 17.618 -11.989 30.883 1.00 11.57 C ANISOU 1956 CB PHE A 236 1192 1779 1424 205 -28 -6 C ATOM 1957 CG PHE A 236 18.298 -11.001 29.980 1.00 11.16 C ANISOU 1957 CG PHE A 236 1100 1649 1490 268 -21 -64 C ATOM 1958 CD1 PHE A 236 18.482 -9.681 30.382 1.00 12.13 C ANISOU 1958 CD1 PHE A 236 1176 1805 1628 -28 222 115 C ATOM 1959 CD2 PHE A 236 18.750 -11.388 28.734 1.00 10.91 C ANISOU 1959 CD2 PHE A 236 855 1836 1452 340 -2 34 C ATOM 1960 CE1 PHE A 236 19.105 -8.764 29.549 1.00 11.49 C ANISOU 1960 CE1 PHE A 236 1091 1658 1615 64 298 123 C ATOM 1961 CE2 PHE A 236 19.372 -10.484 27.895 1.00 12.02 C ANISOU 1961 CE2 PHE A 236 1184 1872 1509 272 20 165 C ATOM 1962 CZ PHE A 236 19.558 -9.171 28.302 1.00 12.71 C ANISOU 1962 CZ PHE A 236 1267 1856 1704 293 -66 -155 C ATOM 1963 N PHE A 237 17.284 -14.342 32.979 1.00 13.46 N ANISOU 1963 N PHE A 237 1574 1741 1796 -460 39 -76 N ATOM 1964 CA PHE A 237 16.408 -14.961 33.956 1.00 14.98 C ANISOU 1964 CA PHE A 237 1743 2024 1924 -1311 -61 -50 C ATOM 1965 C PHE A 237 17.114 -15.147 35.292 1.00 14.03 C ANISOU 1965 C PHE A 237 1525 2094 1712 -383 219 -26 C ATOM 1966 O PHE A 237 16.539 -14.876 36.352 1.00 15.72 O ANISOU 1966 O PHE A 237 2023 2434 1516 -528 322 -103 O ATOM 1967 CB PHE A 237 15.864 -16.297 33.476 1.00 19.53 C ANISOU 1967 CB PHE A 237 2961 2533 1926 -1995 73 -187 C ATOM 1968 CG PHE A 237 14.957 -16.941 34.473 1.00 24.31 C ANISOU 1968 CG PHE A 237 3777 3384 2073 -2361 -15 -286 C ATOM 1969 CD1 PHE A 237 13.697 -16.418 34.712 1.00 24.98 C ANISOU 1969 CD1 PHE A 237 3591 3779 2118 -2394 -260 -541 C ATOM 1970 CD2 PHE A 237 15.376 -18.042 35.208 1.00 26.58 C ANISOU 1970 CD2 PHE A 237 4511 3343 2243 -1904 19 -358 C ATOM 1971 CE1 PHE A 237 12.858 -17.000 35.638 1.00 27.23 C ANISOU 1971 CE1 PHE A 237 3874 4196 2273 -2349 -62 -452 C ATOM 1972 CE2 PHE A 237 14.540 -18.623 36.138 1.00 28.81 C ANISOU 1972 CE2 PHE A 237 4517 3936 2493 -1937 -9 -459 C ATOM 1973 CZ PHE A 237 13.282 -18.103 36.352 1.00 27.67 C ANISOU 1973 CZ PHE A 237 4001 4078 2433 -1980 266 -415 C ATOM 1974 N LYS A 238 18.362 -15.608 35.247 1.00 16.22 N ANISOU 1974 N LYS A 238 1860 2213 2088 -481 88 -3 N ATOM 1975 CA LYS A 238 19.097 -15.812 36.489 1.00 17.45 C ANISOU 1975 CA LYS A 238 1827 2567 2234 43 -149 -8 C ATOM 1976 C LYS A 238 19.331 -14.485 37.214 1.00 14.68 C ANISOU 1976 C LYS A 238 1633 1994 1951 -334 -207 128 C ATOM 1977 O LYS A 238 19.202 -14.414 38.433 1.00 17.66 O ANISOU 1977 O LYS A 238 2016 2702 1990 -491 24 -179 O ATOM 1978 CB LYS A 238 20.391 -16.597 36.277 1.00 23.86 C ANISOU 1978 CB LYS A 238 2933 3506 2624 48 -190 0 C ATOM 1979 CG LYS A 238 21.442 -15.917 35.444 1.00 32.40 C ANISOU 1979 CG LYS A 238 4364 4604 3343 718 -295 -89 C ATOM 1980 CD LYS A 238 22.631 -16.860 35.270 1.00 36.92 C ANISOU 1980 CD LYS A 238 4763 5495 3770 1151 -446 -141 C ATOM 1981 CE LYS A 238 23.519 -16.449 34.109 1.00 36.73 C ANISOU 1981 CE LYS A 238 4396 5716 3843 1198 -454 -121 C ATOM 1982 NZ LYS A 238 24.262 -17.610 33.558 1.00 40.14 N ANISOU 1982 NZ LYS A 238 4916 6244 4091 959 -463 -172 N ATOM 1983 N ALEU A 239 19.667 -13.435 36.466 0.50 12.60 N ANISOU 1983 N ALEU A 239 1185 1700 1901 -289 -203 69 N ATOM 1984 N BLEU A 239 19.632 -13.433 36.458 0.50 14.41 N ANISOU 1984 N BLEU A 239 1749 1711 2012 -308 -240 288 N ATOM 1985 CA ALEU A 239 19.802 -12.112 37.070 0.50 12.32 C ANISOU 1985 CA ALEU A 239 1432 1551 1695 -225 70 -147 C ATOM 1986 CA BLEU A 239 19.816 -12.117 37.057 0.50 15.37 C ANISOU 1986 CA BLEU A 239 2234 1665 1939 -374 -27 220 C ATOM 1987 C ALEU A 239 18.479 -11.687 37.683 0.50 14.08 C ANISOU 1987 C ALEU A 239 1717 1827 1803 -405 104 53 C ATOM 1988 C BLEU A 239 18.502 -11.580 37.625 0.50 15.45 C ANISOU 1988 C BLEU A 239 1985 1961 1921 -707 109 -70 C ATOM 1989 O ALEU A 239 18.431 -11.254 38.833 0.50 14.91 O ANISOU 1989 O ALEU A 239 1933 2014 1716 -340 148 373 O ATOM 1990 O BLEU A 239 18.484 -10.960 38.686 0.50 15.53 O ANISOU 1990 O BLEU A 239 1964 2118 1818 -1001 211 -381 O ATOM 1991 CB ALEU A 239 20.258 -11.064 36.050 0.50 11.27 C ANISOU 1991 CB ALEU A 239 1006 1729 1544 -255 -82 -306 C ATOM 1992 CB BLEU A 239 20.405 -11.131 36.048 0.50 17.63 C ANISOU 1992 CB BLEU A 239 2764 1921 2013 -162 -245 562 C ATOM 1993 CG ALEU A 239 21.732 -11.093 35.654 0.50 9.57 C ANISOU 1993 CG ALEU A 239 593 1470 1570 -266 -300 -231 C ATOM 1994 CG BLEU A 239 20.969 -9.862 36.678 0.50 18.57 C ANISOU 1994 CG BLEU A 239 3074 1728 2252 46 -290 911 C ATOM 1995 CD1ALEU A 239 22.005 -10.036 34.595 0.50 10.34 C ANISOU 1995 CD1ALEU A 239 961 1208 1758 -394 -145 -127 C ATOM 1996 CD1BLEU A 239 22.024 -10.201 37.726 0.50 18.64 C ANISOU 1996 CD1BLEU A 239 3049 1719 2312 -328 -275 734 C ATOM 1997 CD2ALEU A 239 22.611 -10.897 36.880 0.50 11.53 C ANISOU 1997 CD2ALEU A 239 850 1705 1824 -457 -361 -243 C ATOM 1998 CD2BLEU A 239 21.539 -8.947 35.605 0.50 17.32 C ANISOU 1998 CD2BLEU A 239 2758 1509 2311 164 -302 1241 C ATOM 1999 N TYR A 240 17.406 -11.816 36.910 1.00 14.14 N ANISOU 1999 N TYR A 240 1535 2033 1803 -206 243 32 N ATOM 2000 CA TYR A 240 16.086 -11.428 37.383 1.00 14.00 C ANISOU 2000 CA TYR A 240 1389 2140 1788 -88 -32 -29 C ATOM 2001 C TYR A 240 15.783 -12.089 38.720 1.00 15.37 C ANISOU 2001 C TYR A 240 1631 2480 1726 58 74 73 C ATOM 2002 O TYR A 240 15.330 -11.432 39.658 1.00 18.01 O ANISOU 2002 O TYR A 240 2162 3214 1464 -130 439 -122 O ATOM 2003 CB TYR A 240 15.023 -11.817 36.360 1.00 13.18 C ANISOU 2003 CB TYR A 240 1222 2020 1764 -413 -173 23 C ATOM 2004 CG TYR A 240 13.610 -11.491 36.785 1.00 15.27 C ANISOU 2004 CG TYR A 240 1489 2215 2098 -104 192 -19 C ATOM 2005 CD1 TYR A 240 13.215 -10.177 37.002 1.00 16.11 C ANISOU 2005 CD1 TYR A 240 2080 2110 1929 491 648 -319 C ATOM 2006 CD2 TYR A 240 12.665 -12.493 36.948 1.00 17.33 C ANISOU 2006 CD2 TYR A 240 1612 2559 2413 -58 528 -57 C ATOM 2007 CE1 TYR A 240 11.922 -9.864 37.383 1.00 17.74 C ANISOU 2007 CE1 TYR A 240 2106 2485 2147 356 314 -502 C ATOM 2008 CE2 TYR A 240 11.368 -12.190 37.334 1.00 18.10 C ANISOU 2008 CE2 TYR A 240 1505 2648 2721 113 152 -455 C ATOM 2009 CZ TYR A 240 11.003 -10.878 37.545 1.00 19.46 C ANISOU 2009 CZ TYR A 240 1592 3161 2641 257 472 -380 C ATOM 2010 OH TYR A 240 9.718 -10.593 37.914 1.00 21.69 O ANISOU 2010 OH TYR A 240 1553 3640 3046 108 686 -204 O ATOM 2011 N AARG A 241 16.046 -13.389 38.807 0.50 15.74 N ANISOU 2011 N AARG A 241 1630 2560 1790 -278 133 248 N ATOM 2012 N BARG A 241 16.034 -13.392 38.808 0.50 15.61 N ANISOU 2012 N BARG A 241 1570 2483 1878 -274 104 283 N ATOM 2013 CA AARG A 241 15.798 -14.135 40.038 0.50 18.56 C ANISOU 2013 CA AARG A 241 2451 2765 1834 -351 142 51 C ATOM 2014 CA BARG A 241 15.789 -14.128 40.047 0.50 18.34 C ANISOU 2014 CA BARG A 241 2344 2605 2019 -290 109 112 C ATOM 2015 C AARG A 241 16.693 -13.675 41.187 0.50 19.01 C ANISOU 2015 C AARG A 241 2447 2958 1815 -133 54 31 C ATOM 2016 C BARG A 241 16.690 -13.664 41.189 0.50 18.88 C ANISOU 2016 C BARG A 241 2382 2885 1904 -94 33 60 C ATOM 2017 O AARG A 241 16.242 -13.571 42.331 0.50 21.11 O ANISOU 2017 O AARG A 241 2857 3218 1943 -144 44 81 O ATOM 2018 O BARG A 241 16.242 -13.549 42.334 0.50 20.99 O ANISOU 2018 O BARG A 241 2809 3142 2021 -111 19 90 O ATOM 2019 CB AARG A 241 15.966 -15.636 39.801 0.50 22.05 C ANISOU 2019 CB AARG A 241 3110 3233 2034 -676 140 -121 C ATOM 2020 CB BARG A 241 15.946 -15.633 39.827 0.50 21.59 C ANISOU 2020 CB BARG A 241 2888 2914 2400 -536 96 -2 C ATOM 2021 CG AARG A 241 14.851 -16.245 38.966 0.50 25.77 C ANISOU 2021 CG AARG A 241 3640 3897 2253 -809 207 -282 C ATOM 2022 CG BARG A 241 14.656 -16.346 39.445 0.50 24.89 C ANISOU 2022 CG BARG A 241 3238 3404 2814 -656 182 -63 C ATOM 2023 CD AARG A 241 13.492 -15.872 39.539 0.50 29.82 C ANISOU 2023 CD AARG A 241 4119 4537 2671 -879 197 -294 C ATOM 2024 CD BARG A 241 13.600 -16.195 40.539 0.50 26.89 C ANISOU 2024 CD BARG A 241 3400 3552 3265 -908 49 -225 C ATOM 2025 NE AARG A 241 12.391 -16.536 38.847 0.50 33.06 N ANISOU 2025 NE AARG A 241 4705 4903 2953 -1011 294 -226 N ATOM 2026 NE BARG A 241 12.630 -15.147 40.237 0.50 28.47 N ANISOU 2026 NE BARG A 241 3531 3645 3639 -1149 -73 -729 N ATOM 2027 CZ AARG A 241 11.960 -17.762 39.131 0.50 34.50 C ANISOU 2027 CZ AARG A 241 4947 5031 3128 -880 254 -124 C ATOM 2028 CZ BARG A 241 11.771 -14.647 41.119 0.50 28.71 C ANISOU 2028 CZ BARG A 241 3493 3757 3658 -892 -121 -550 C ATOM 2029 NH1AARG A 241 12.541 -18.468 40.091 0.50 35.19 N ANISOU 2029 NH1AARG A 241 4904 5266 3198 -976 148 -86 N ATOM 2030 NH1BARG A 241 11.771 -15.086 42.370 0.50 27.23 N ANISOU 2030 NH1BARG A 241 3006 3567 3772 -724 -182 -170 N ATOM 2031 NH2AARG A 241 10.951 -18.283 38.448 0.50 34.79 N ANISOU 2031 NH2AARG A 241 5068 5007 3144 -807 127 -156 N ATOM 2032 NH2BARG A 241 10.921 -13.697 40.755 0.50 30.32 N ANISOU 2032 NH2BARG A 241 3850 4019 3649 -595 -326 -476 N ATOM 2033 N LEU A 242 17.957 -13.400 40.882 1.00 19.40 N ANISOU 2033 N LEU A 242 2748 2798 1824 -615 -83 51 N ATOM 2034 CA LEU A 242 18.907 -12.949 41.894 1.00 20.28 C ANISOU 2034 CA LEU A 242 3028 2796 1881 -647 46 271 C ATOM 2035 C LEU A 242 18.484 -11.617 42.470 1.00 23.08 C ANISOU 2035 C LEU A 242 3539 3124 2104 -493 -46 103 C ATOM 2036 O LEU A 242 18.584 -11.383 43.673 1.00 25.41 O ANISOU 2036 O LEU A 242 4040 3376 2239 -560 -478 41 O ATOM 2037 CB LEU A 242 20.308 -12.809 41.304 1.00 20.91 C ANISOU 2037 CB LEU A 242 2749 3068 2126 -296 -55 64 C ATOM 2038 CG LEU A 242 21.079 -14.107 41.086 1.00 24.03 C ANISOU 2038 CG LEU A 242 3276 3345 2507 -219 -135 -80 C ATOM 2039 CD1 LEU A 242 22.357 -13.825 40.323 1.00 26.58 C ANISOU 2039 CD1 LEU A 242 3732 3647 2718 -209 6 -67 C ATOM 2040 CD2 LEU A 242 21.377 -14.759 42.418 1.00 24.76 C ANISOU 2040 CD2 LEU A 242 3353 3443 2610 -420 69 -71 C ATOM 2041 N ILE A 243 18.028 -10.733 41.595 1.00 21.99 N ANISOU 2041 N ILE A 243 3216 2929 2207 -651 174 -452 N ATOM 2042 CA ILE A 243 17.612 -9.409 42.013 1.00 27.27 C ANISOU 2042 CA ILE A 243 3921 3573 2865 -716 213 -672 C ATOM 2043 C ILE A 243 16.291 -9.453 42.779 1.00 28.91 C ANISOU 2043 C ILE A 243 4156 3931 2896 -797 670 -961 C ATOM 2044 O ILE A 243 16.086 -8.690 43.722 1.00 30.78 O ANISOU 2044 O ILE A 243 4575 4157 2961 -1270 920 -1192 O ATOM 2045 CB ILE A 243 17.527 -8.467 40.805 1.00 29.42 C ANISOU 2045 CB ILE A 243 4210 3667 3300 11 214 -884 C ATOM 2046 CG1 ILE A 243 18.942 -8.143 40.314 1.00 27.34 C ANISOU 2046 CG1 ILE A 243 3310 3652 3425 -242 133 -964 C ATOM 2047 CG2 ILE A 243 16.784 -7.201 41.174 1.00 31.75 C ANISOU 2047 CG2 ILE A 243 4715 3869 3480 533 289 -1069 C ATOM 2048 CD1 ILE A 243 18.999 -7.564 38.931 1.00 28.68 C ANISOU 2048 CD1 ILE A 243 3377 3943 3575 -565 5 -914 C ATOM 2049 N GLU A 244 15.402 -10.361 42.387 1.00 28.98 N ANISOU 2049 N GLU A 244 4007 4159 2842 -779 801 -828 N ATOM 2050 CA GLU A 244 14.115 -10.501 43.067 1.00 31.76 C ANISOU 2050 CA GLU A 244 4140 4837 3088 -653 957 -761 C ATOM 2051 C GLU A 244 14.264 -11.137 44.445 1.00 32.64 C ANISOU 2051 C GLU A 244 4207 4985 3210 -743 1159 -594 C ATOM 2052 O GLU A 244 13.495 -10.842 45.358 1.00 34.69 O ANISOU 2052 O GLU A 244 4315 5573 3290 -561 1366 -546 O ATOM 2053 CB GLU A 244 13.134 -11.309 42.218 1.00 34.48 C ANISOU 2053 CB GLU A 244 4441 5326 3334 -359 838 -660 C ATOM 2054 CG GLU A 244 12.568 -10.535 41.046 1.00 38.13 C ANISOU 2054 CG GLU A 244 5027 5752 3708 113 604 -537 C ATOM 2055 CD GLU A 244 11.778 -9.318 41.487 1.00 42.19 C ANISOU 2055 CD GLU A 244 5624 6345 4058 99 510 -432 C ATOM 2056 OE1 GLU A 244 10.818 -9.487 42.270 1.00 44.95 O ANISOU 2056 OE1 GLU A 244 5946 6736 4394 106 361 -409 O ATOM 2057 OE2 GLU A 244 12.111 -8.194 41.049 1.00 42.24 O ANISOU 2057 OE2 GLU A 244 5657 6290 4100 43 459 -279 O ATOM 2058 N ASP A 245 15.256 -12.006 44.595 1.00 33.11 N ANISOU 2058 N ASP A 245 4406 4777 3396 -747 1009 -720 N ATOM 2059 CA ASP A 245 15.480 -12.680 45.871 1.00 36.99 C ANISOU 2059 CA ASP A 245 5247 5120 3687 -745 598 -893 C ATOM 2060 C ASP A 245 16.250 -11.811 46.860 1.00 39.87 C ANISOU 2060 C ASP A 245 5796 5580 3773 -928 151 -1058 C ATOM 2061 O ASP A 245 16.376 -12.166 48.030 1.00 43.28 O ANISOU 2061 O ASP A 245 6483 5997 3963 -1070 129 -798 O ATOM 2062 CB ASP A 245 16.223 -14.000 45.664 1.00 39.07 C ANISOU 2062 CB ASP A 245 5673 5145 4026 -338 778 -930 C ATOM 2063 CG ASP A 245 15.394 -15.023 44.915 1.00 43.47 C ANISOU 2063 CG ASP A 245 6308 5740 4469 -154 804 -867 C ATOM 2064 OD1 ASP A 245 14.149 -14.916 44.947 1.00 44.07 O ANISOU 2064 OD1 ASP A 245 6142 5928 4672 -337 616 -988 O ATOM 2065 OD2 ASP A 245 15.987 -15.934 44.297 1.00 46.38 O ANISOU 2065 OD2 ASP A 245 7059 5984 4579 98 898 -709 O ATOM 2066 N SER A 246 16.766 -10.679 46.392 1.00 39.01 N ANISOU 2066 N SER A 246 5582 5368 3871 -1152 -188 -1438 N ATOM 2067 CA SER A 246 17.559 -9.796 47.244 1.00 42.33 C ANISOU 2067 CA SER A 246 5990 5779 4314 -997 -369 -1477 C ATOM 2068 C SER A 246 16.677 -8.942 48.148 1.00 45.55 C ANISOU 2068 C SER A 246 6777 5979 4548 -754 -596 -1616 C ATOM 2069 O SER A 246 17.147 -8.389 49.147 1.00 47.75 O ANISOU 2069 O SER A 246 7263 6145 4732 -782 -917 -1545 O ATOM 2070 CB SER A 246 18.463 -8.896 46.401 1.00 42.71 C ANISOU 2070 CB SER A 246 5682 5960 4583 -1011 -239 -1385 C ATOM 2071 OG SER A 246 19.381 -9.659 45.639 1.00 43.63 O ANISOU 2071 OG SER A 246 5587 6202 4787 -893 -86 -1301 O TER 2072 SER A 246 HETATM 2073 O HOH A 249 19.151 7.388 29.491 1.00 47.24 O HETATM 2074 O HOH A 250 18.728 2.776 23.618 1.00 48.88 O HETATM 2075 O HOH A 251 23.948 -18.587 29.263 1.00 41.68 O HETATM 2076 O HOH A 252 9.382 -13.583 44.513 1.00 43.33 O HETATM 2077 O HOH A 253 -1.700 -12.196 35.771 1.00 44.36 O HETATM 2078 O HOH A 254 23.117 -13.205 46.267 1.00 49.27 O HETATM 2079 O HOH A 255 0.168 -0.659 8.806 1.00 41.78 O HETATM 2080 O HOH A 256 0.619 -12.063 37.454 1.00 48.77 O HETATM 2081 O HOH A 257 16.149 2.518 24.657 1.00 22.76 O HETATM 2082 O HOH A 258 -9.537 -24.075 20.936 1.00 22.77 O HETATM 2083 O HOH A 259 34.993 -5.234 35.854 1.00 22.91 O HETATM 2084 O HOH A 260 -16.236 -7.052 -0.029 1.00 22.01 O HETATM 2085 O HOH A 261 0.563 -5.502 -6.945 1.00 22.01 O HETATM 2086 O HOH A 262 29.819 -18.123 39.794 1.00 22.01 O HETATM 2087 O HOH A 263 17.912 -9.541 8.767 1.00 22.01 O HETATM 2088 O HOH A 264 -6.644 -26.463 21.459 1.00 22.01 O HETATM 2089 O HOH A 265 -18.445 -18.779 16.376 1.00 22.01 O HETATM 2090 O HOH A 266 24.056 4.854 18.665 1.00 22.01 O HETATM 2091 O HOH A 267 -5.360 3.534 15.334 1.00 22.01 O HETATM 2092 O HOH A 268 21.444 -16.228 18.531 1.00 22.01 O HETATM 2093 O HOH A 269 23.699 3.871 22.138 1.00 22.01 O HETATM 2094 O HOH A 270 -2.181 -28.103 12.631 1.00 22.01 O HETATM 2095 O HOH A 271 -16.038 -15.471 22.964 1.00 22.01 O HETATM 2096 O HOH A 272 -5.115 -14.955 -6.066 1.00 22.01 O HETATM 2097 O HOH A 273 19.484 -15.578 45.505 1.00 22.01 O HETATM 2098 O HOH A 274 15.145 -17.152 9.157 1.00 22.01 O HETATM 2099 O HOH A 275 24.954 -2.370 28.782 1.00 13.47 O HETATM 2100 O HOH A 276 13.827 -5.269 20.985 1.00 12.63 O HETATM 2101 O HOH A 277 -7.561 -1.610 3.488 1.00 12.64 O HETATM 2102 O HOH A 278 15.763 -1.792 24.296 1.00 17.10 O HETATM 2103 O HOH A 279 -1.537 -14.303 29.329 1.00 17.92 O HETATM 2104 O HOH A 280 29.895 -7.228 26.150 1.00 14.18 O HETATM 2105 O HOH A 281 13.153 -3.065 22.651 1.00 18.24 O HETATM 2106 O HOH A 282 18.433 -10.895 14.409 1.00 16.76 O HETATM 2107 O HOH A 283 24.975 -3.429 24.940 1.00 14.80 O HETATM 2108 O HOH A 284 24.312 -6.584 13.391 1.00 16.23 O HETATM 2109 O HOH A 285 19.026 1.455 20.439 1.00 22.01 O HETATM 2110 O HOH A 286 0.026 8.439 2.976 1.00 22.01 O HETATM 2111 O HOH A 287 17.370 -11.788 7.165 1.00 22.01 O HETATM 2112 O HOH A 288 -2.962 -5.531 9.492 1.00 17.05 O HETATM 2113 O HOH A 289 -3.305 -20.194 6.573 1.00 19.83 O HETATM 2114 O HOH A 290 20.067 -18.787 26.976 1.00 16.91 O HETATM 2115 O HOH A 291 -13.919 -23.354 10.837 1.00 20.04 O HETATM 2116 O HOH A 292 21.254 -9.611 25.230 1.00 18.47 O HETATM 2117 O HOH A 293 4.945 -22.794 26.101 1.00 20.15 O HETATM 2118 O HOH A 294 -11.801 4.756 17.752 1.00 17.26 O HETATM 2119 O HOH A 295 31.489 -4.999 26.912 1.00 17.90 O HETATM 2120 O HOH A 296 19.441 -10.652 23.709 1.00 21.64 O HETATM 2121 O HOH A 297 13.662 -17.366 18.835 1.00 18.85 O HETATM 2122 O HOH A 298 -7.382 2.943 -3.178 1.00 23.19 O HETATM 2123 O HOH A 299 26.159 -4.915 20.795 1.00 20.07 O HETATM 2124 O HOH A 300 27.381 -4.137 23.393 1.00 21.66 O HETATM 2125 O HOH A 301 27.400 -13.077 23.954 1.00 21.46 O HETATM 2126 O HOH A 302 30.713 2.126 30.772 1.00 23.85 O HETATM 2127 O HOH A 303 7.724 -1.837 12.910 1.00 25.78 O HETATM 2128 O HOH A 304 24.680 4.241 26.839 1.00 25.26 O HETATM 2129 O HOH A 305 -16.386 -12.416 21.500 1.00 28.54 O HETATM 2130 O HOH A 306 -6.522 0.609 15.081 1.00 23.63 O HETATM 2131 O HOH A 307 -19.097 -12.734 13.467 1.00 23.24 O HETATM 2132 O HOH A 308 6.940 -23.653 30.081 1.00 24.78 O HETATM 2133 O HOH A 309 -16.483 -2.407 19.223 1.00 24.69 O HETATM 2134 O HOH A 310 -3.961 -21.025 23.895 1.00 31.30 O HETATM 2135 O HOH A 311 17.564 -3.953 36.185 1.00 24.16 O HETATM 2136 O HOH A 312 -6.060 1.326 3.591 1.00 23.03 O HETATM 2137 O HOH A 313 30.154 3.832 19.826 1.00 22.63 O HETATM 2138 O HOH A 314 -8.692 -28.134 12.856 1.00 28.17 O HETATM 2139 O HOH A 315 8.066 -12.922 38.298 1.00 27.72 O HETATM 2140 O HOH A 316 12.150 -5.006 18.660 1.00 22.90 O HETATM 2141 O HOH A 317 30.145 -12.120 30.210 1.00 25.81 O HETATM 2142 O HOH A 318 -4.025 -6.856 27.438 1.00 23.49 O HETATM 2143 O HOH A 319 11.797 -0.878 -3.228 1.00 27.58 O HETATM 2144 O HOH A 320 -1.055 -23.864 14.010 1.00 26.52 O HETATM 2145 O HOH A 321 -7.656 -8.429 -0.552 1.00 28.93 O HETATM 2146 O HOH A 322 -17.215 -9.794 21.025 1.00 26.66 O HETATM 2147 O HOH A 323 9.447 -15.051 38.401 1.00 31.50 O HETATM 2148 O HOH A 324 -14.337 -14.560 1.045 1.00 32.62 O HETATM 2149 O HOH A 325 13.969 -1.372 9.024 1.00 28.34 O HETATM 2150 O HOH A 326 5.555 1.263 -4.070 1.00 33.16 O HETATM 2151 O HOH A 327 -5.662 -22.497 5.421 1.00 23.54 O HETATM 2152 O HOH A 328 -18.295 7.892 16.149 1.00 26.50 O HETATM 2153 O HOH A 329 1.933 -8.613 35.195 1.00 33.32 O HETATM 2154 O HOH A 330 19.837 -2.247 35.879 1.00 24.56 O HETATM 2155 O HOH A 331 19.491 -2.941 22.468 1.00 28.65 O HETATM 2156 O HOH A 332 -12.718 -12.839 0.607 1.00 26.50 O HETATM 2157 O HOH A 333 -14.730 -11.892 28.249 1.00 26.67 O HETATM 2158 O HOH A 334 6.532 -2.549 33.862 1.00 29.59 O HETATM 2159 O HOH A 335 15.422 -16.247 17.243 1.00 26.68 O HETATM 2160 O HOH A 336 5.997 -0.975 11.033 1.00 27.82 O HETATM 2161 O HOH A 337 -16.145 -13.515 2.682 1.00 26.97 O HETATM 2162 O HOH A 338 23.629 -12.236 23.360 1.00 30.40 O HETATM 2163 O HOH A 339 -3.621 -4.651 3.671 1.00 30.02 O HETATM 2164 O HOH A 340 -4.401 -24.602 14.326 1.00 33.10 O HETATM 2165 O HOH A 341 -15.789 -1.463 22.988 1.00 38.70 O HETATM 2166 O HOH A 342 20.066 -16.909 24.430 1.00 32.18 O HETATM 2167 O HOH A 343 -7.836 -20.781 17.277 1.00 28.29 O HETATM 2168 O HOH A 344 -21.810 -15.772 5.931 1.00 25.37 O HETATM 2169 O HOH A 345 -8.145 -1.984 -2.484 1.00 39.86 O HETATM 2170 O HOH A 346 6.766 0.815 17.876 1.00 30.98 O HETATM 2171 O HOH A 347 -10.792 4.706 6.503 1.00 33.50 O HETATM 2172 O HOH A 348 -4.868 1.339 6.474 1.00 26.47 O HETATM 2173 O HOH A 349 1.889 -22.453 18.071 1.00 32.44 O HETATM 2174 O HOH A 350 14.275 -17.470 11.783 1.00 28.87 O HETATM 2175 O HOH A 351 -12.469 -29.070 7.579 1.00 26.62 O HETATM 2176 O HOH A 352 23.350 -10.525 21.520 1.00 35.31 O HETATM 2177 O HOH A 353 10.947 -1.727 21.741 1.00 30.27 O HETATM 2178 O HOH A 354 15.863 -17.073 21.949 1.00 30.20 O HETATM 2179 O HOH A 355 11.846 -5.750 38.811 1.00 39.17 O HETATM 2180 O HOH A 356 -18.997 -7.837 10.971 1.00 29.59 O HETATM 2181 O HOH A 357 -6.427 -1.057 17.233 1.00 29.16 O HETATM 2182 O HOH A 358 -9.412 1.364 3.276 1.00 33.85 O HETATM 2183 O HOH A 359 6.412 -1.930 23.955 1.00 27.17 O HETATM 2184 O HOH A 360 -6.701 -0.718 9.037 1.00 30.47 O HETATM 2185 O HOH A 361 -9.145 0.636 23.451 1.00 27.34 O HETATM 2186 O HOH A 362 9.138 -0.653 6.839 1.00 32.44 O HETATM 2187 O HOH A 363 -14.520 -16.026 20.189 1.00 35.62 O HETATM 2188 O HOH A 364 -6.132 -17.660 -0.464 1.00 34.47 O HETATM 2189 O HOH A 365 19.726 -14.824 23.111 1.00 41.92 O HETATM 2190 O HOH A 366 -14.496 -11.291 2.062 1.00 29.41 O HETATM 2191 O HOH A 367 5.113 4.001 -5.135 1.00 28.07 O HETATM 2192 O HOH A 368 27.140 7.179 22.356 1.00 33.92 O HETATM 2193 O HOH A 369 26.131 3.377 38.430 1.00 31.80 O HETATM 2194 O HOH A 370 1.520 -2.225 25.315 1.00 31.97 O HETATM 2195 O HOH A 371 -6.814 -16.269 -3.602 1.00 38.72 O HETATM 2196 O HOH A 372 34.859 -1.487 24.688 1.00 32.91 O HETATM 2197 O HOH A 373 8.283 0.100 14.839 1.00 27.56 O HETATM 2198 O HOH A 374 -19.755 -11.732 19.224 1.00 33.62 O HETATM 2199 O HOH A 375 7.360 7.178 1.107 1.00 38.14 O HETATM 2200 O HOH A 376 -18.161 3.010 12.722 1.00 30.51 O HETATM 2201 O HOH A 377 16.854 5.678 32.090 1.00 37.70 O HETATM 2202 O HOH A 378 20.912 -11.440 21.478 1.00 31.83 O HETATM 2203 O HOH A 379 1.693 -11.260 35.072 1.00 30.77 O HETATM 2204 O HOH A 380 15.996 -0.918 5.508 1.00 34.86 O HETATM 2205 O HOH A 381 29.461 -15.569 27.404 1.00 45.79 O HETATM 2206 O HOH A 382 -10.515 -19.428 21.032 1.00 30.43 O HETATM 2207 O HOH A 383 -6.032 -20.006 27.202 1.00 31.18 O HETATM 2208 O HOH A 384 13.996 -4.400 38.371 1.00 32.21 O HETATM 2209 O HOH A 385 30.815 2.681 27.208 1.00 38.36 O HETATM 2210 O HOH A 386 -16.770 9.185 20.626 1.00 39.48 O HETATM 2211 O HOH A 387 -8.688 -24.137 16.664 1.00 40.51 O HETATM 2212 O HOH A 388 -1.372 5.042 21.285 1.00 36.80 O HETATM 2213 O HOH A 389 -17.745 -6.364 18.459 1.00 34.14 O HETATM 2214 O HOH A 390 18.925 -13.066 24.535 1.00 38.21 O HETATM 2215 O HOH A 391 15.247 -17.167 14.572 1.00 37.42 O HETATM 2216 O HOH A 392 6.354 -24.483 21.088 1.00 33.88 O HETATM 2217 O HOH A 393 -17.783 -20.444 11.507 1.00 30.03 O HETATM 2218 O HOH A 394 8.839 -9.502 -0.263 1.00 36.18 O HETATM 2219 O HOH A 395 15.039 0.201 27.649 1.00 36.43 O HETATM 2220 O HOH A 396 12.949 0.767 -10.500 1.00 30.34 O HETATM 2221 O HOH A 397 -5.428 -2.480 15.166 1.00 37.90 O HETATM 2222 O HOH A 398 17.616 -18.760 38.849 1.00 39.83 O HETATM 2223 O HOH A 399 -4.943 -2.269 2.053 1.00 35.60 O HETATM 2224 O HOH A 400 18.734 4.981 28.010 1.00 42.37 O HETATM 2225 O HOH A 401 -18.113 -17.736 13.883 1.00 43.41 O HETATM 2226 O HOH A 402 -7.402 -19.769 0.113 1.00 35.85 O HETATM 2227 O HOH A 403 -3.709 4.468 19.795 1.00 39.64 O HETATM 2228 O HOH A 404 11.145 -2.557 18.930 1.00 28.80 O HETATM 2229 O HOH A 405 21.651 2.785 33.545 1.00 33.29 O HETATM 2230 O HOH A 406 -5.239 -10.380 29.316 1.00 39.33 O HETATM 2231 O HOH A 407 31.961 -13.110 36.488 1.00 35.76 O HETATM 2232 O HOH A 408 -1.748 -4.272 5.584 1.00 33.66 O HETATM 2233 O HOH A 409 -0.688 4.879 4.808 1.00 38.75 O HETATM 2234 O HOH A 410 -3.846 -5.289 -1.417 1.00 39.04 O HETATM 2235 O HOH A 411 -0.775 4.190 14.962 1.00 40.67 O HETATM 2236 O HOH A 412 22.842 -5.882 19.529 1.00 40.76 O HETATM 2237 O HOH A 413 20.637 3.218 25.415 1.00 34.38 O HETATM 2238 O HOH A 414 10.661 1.466 14.456 1.00 41.27 O HETATM 2239 O HOH A 415 -0.820 -22.557 16.797 1.00 33.20 O HETATM 2240 O HOH A 416 7.913 1.710 -5.200 1.00 34.40 O HETATM 2241 O HOH A 417 4.046 2.228 9.210 1.00 46.56 O HETATM 2242 O HOH A 418 20.029 -12.874 45.492 1.00 38.00 O HETATM 2243 O HOH A 419 -15.639 -9.464 0.245 1.00 39.46 O HETATM 2244 O HOH A 420 10.037 1.712 -3.356 1.00 49.05 O HETATM 2245 O HOH A 421 -14.150 -18.084 18.515 1.00 33.95 O HETATM 2246 O HOH A 422 3.110 -23.095 15.044 1.00 45.11 O HETATM 2247 O HOH A 423 -11.384 -21.214 18.175 1.00 31.86 O HETATM 2248 O HOH A 424 -12.639 -19.875 23.724 1.00 35.23 O HETATM 2249 O HOH A 425 13.679 -19.691 16.989 1.00 43.51 O HETATM 2250 O HOH A 426 14.431 -4.940 -3.160 1.00 33.35 O HETATM 2251 O HOH A 427 6.288 -21.671 31.982 1.00 42.43 O HETATM 2252 O HOH A 428 -8.259 3.168 24.029 1.00 38.11 O HETATM 2253 O HOH A 429 -17.386 2.048 15.578 1.00 36.97 O HETATM 2254 O HOH A 430 12.662 1.436 26.941 1.00 42.06 O HETATM 2255 O HOH A 431 -14.325 -17.356 1.672 1.00 33.97 O HETATM 2256 O HOH A 432 8.385 1.628 8.083 1.00 44.12 O HETATM 2257 O HOH A 433 27.211 -14.139 29.781 1.00 44.84 O HETATM 2258 O HOH A 434 17.415 -11.865 9.962 1.00 41.98 O HETATM 2259 O HOH A 435 -5.316 -22.189 17.152 1.00 36.97 O HETATM 2260 O HOH A 436 -3.096 0.264 17.938 1.00 38.12 O HETATM 2261 O HOH A 437 5.018 -2.903 8.282 1.00 44.80 O HETATM 2262 O HOH A 438 22.802 -19.816 27.265 1.00 39.88 O HETATM 2263 O HOH A 439 -11.728 2.294 5.000 1.00 38.76 O HETATM 2264 O HOH A 440 34.218 -3.444 29.218 1.00 44.33 O HETATM 2265 O HOH A 441 7.963 -18.512 39.145 1.00 48.64 O HETATM 2266 O HOH A 442 -2.915 -17.233 1.625 1.00 41.42 O HETATM 2267 O HOH A 443 -1.451 -6.556 -5.221 1.00 37.96 O HETATM 2268 O HOH A 444 26.425 -16.797 30.857 1.00 40.54 O HETATM 2269 O HOH A 445 13.609 -15.561 4.200 1.00 43.64 O HETATM 2270 O HOH A 446 29.167 -17.688 29.835 1.00 35.92 O HETATM 2271 O HOH A 447 -16.089 -21.781 9.241 1.00 43.96 O HETATM 2272 O HOH A 448 23.942 -5.307 16.616 1.00 37.76 O HETATM 2273 O HOH A 449 4.015 3.207 4.323 1.00 39.61 O HETATM 2274 O HOH A 450 15.337 -6.585 -0.939 1.00 46.80 O HETATM 2275 O HOH A 451 -2.813 -21.984 4.623 1.00 37.44 O HETATM 2276 O HOH A 452 -14.324 -24.511 6.605 1.00 39.98 O HETATM 2277 O HOH A 453 -19.661 -15.439 17.152 1.00 29.96 O HETATM 2278 O HOH A 454 5.453 4.752 19.972 1.00 44.97 O HETATM 2279 O HOH A 455 12.053 -6.710 43.463 1.00 46.18 O HETATM 2280 O HOH A 456 -19.016 6.268 13.974 1.00 36.02 O HETATM 2281 O HOH A 457 -3.063 2.542 14.485 1.00 38.84 O HETATM 2282 O HOH A 458 2.948 -15.520 -1.475 1.00 46.53 O HETATM 2283 O HOH A 459 -10.788 -13.890 29.828 1.00 35.93 O HETATM 2284 O HOH A 460 -4.259 -2.689 28.825 1.00 47.19 O HETATM 2285 O HOH A 461 9.069 4.547 6.840 1.00 42.79 O HETATM 2286 O HOH A 462 5.237 1.160 19.677 1.00 30.78 O HETATM 2287 O HOH A 463 20.265 0.521 34.024 1.00 39.67 O HETATM 2288 O HOH A 464 34.979 -1.891 27.170 1.00 39.90 O HETATM 2289 O HOH A 465 -2.963 5.855 23.346 1.00 42.24 O HETATM 2290 O HOH A 466 -3.401 -3.816 0.817 1.00 40.48 O HETATM 2291 O HOH A 467 -19.511 -17.120 6.177 1.00 38.48 O HETATM 2292 O HOH A 468 19.407 -16.992 39.867 1.00 35.91 O HETATM 2293 O HOH A 469 -2.068 7.149 1.954 1.00 34.39 O HETATM 2294 O HOH A 470 -1.410 -20.092 24.325 1.00 42.40 O HETATM 2295 O HOH A 471 -18.916 -9.250 1.142 1.00 44.04 O HETATM 2296 O HOH A 472 -0.434 -22.677 5.564 1.00 42.34 O HETATM 2297 O HOH A 473 -20.180 1.141 12.010 1.00 44.90 O HETATM 2298 O HOH A 474 -2.569 -27.273 7.772 1.00 44.03 O HETATM 2299 O HOH A 475 22.511 -8.620 19.863 1.00 43.67 O HETATM 2300 O HOH A 476 -12.449 -17.683 20.507 1.00 44.49 O HETATM 2301 O HOH A 477 -13.106 -24.172 17.548 1.00 38.64 O HETATM 2302 O HOH A 478 4.238 -7.693 -6.501 1.00 41.36 O HETATM 2303 O HOH A 479 1.882 -2.421 -3.615 1.00 40.35 O HETATM 2304 O HOH A 480 3.541 -9.839 -4.891 1.00 42.98 O HETATM 2305 O HOH A 481 -16.830 -17.082 2.568 1.00 38.87 O HETATM 2306 O HOH A 482 6.827 -4.717 40.688 1.00 39.28 O HETATM 2307 O HOH A 483 5.266 -24.619 15.543 1.00 42.05 O HETATM 2308 O HOH A 484 18.396 -17.576 42.227 1.00 45.64 O HETATM 2309 O HOH A 485 -2.458 -24.046 18.560 1.00 44.06 O HETATM 2310 O HOH A 486 -10.051 2.242 -3.064 1.00 39.70 O HETATM 2311 O HOH A 487 2.068 -23.388 12.644 1.00 44.90 O HETATM 2312 O HOH A 488 -0.633 1.572 23.999 1.00 44.12 O HETATM 2313 O HOH A 489 4.335 -1.585 32.222 1.00 36.19 O HETATM 2314 O HOH A 490 18.277 3.756 34.251 1.00 45.77 O HETATM 2315 O HOH A 491 36.187 -7.660 33.842 1.00 45.28 O HETATM 2316 O HOH A 492 19.000 -19.201 34.190 1.00 47.07 O HETATM 2317 O HOH A 493 31.725 -15.222 37.955 1.00 48.97 O HETATM 2318 O HOH A 494 19.890 -15.125 20.370 1.00 47.22 O HETATM 2319 O HOH A 495 35.003 3.348 35.410 1.00 44.81 O HETATM 2320 O HOH A 496 18.115 -22.213 33.596 1.00 45.94 O HETATM 2321 O HOH A 497 18.023 -1.099 23.185 1.00 43.43 O HETATM 2322 O HOH A 498 -2.725 -4.193 -3.807 1.00 44.82 O HETATM 2323 O HOH A 499 -2.849 -0.436 14.554 1.00 44.38 O HETATM 2324 O HOH A 500 -15.194 4.910 2.848 1.00 50.05 O HETATM 2325 O HOH A 501 -4.312 -13.483 29.499 1.00 48.25 O HETATM 2326 O HOH A 502 18.426 0.625 25.167 1.00 45.65 O HETATM 2327 O HOH A 503 9.421 1.511 18.665 1.00 42.43 O HETATM 2328 O HOH A 504 6.545 -0.213 26.843 1.00 37.95 O HETATM 2329 O HOH A 505 -20.543 -17.800 12.148 1.00 46.62 O HETATM 2330 O HOH A 506 5.578 -22.935 12.951 1.00 46.29 O HETATM 2331 O HOH A 507 21.270 0.645 38.171 1.00 40.54 O HETATM 2332 O HOH A 508 15.983 0.643 -8.461 1.00 44.78 O HETATM 2333 O HOH A 509 3.416 -16.080 33.164 1.00 46.54 O HETATM 2334 O HOH A 510 9.270 -22.075 15.938 1.00 38.07 O HETATM 2335 O HOH A 511 -21.405 -1.024 7.216 1.00 44.88 O HETATM 2336 O HOH A 512 -5.714 -5.511 29.290 1.00 47.47 O HETATM 2337 O HOH A 513 16.623 4.191 26.485 1.00 39.02 O HETATM 2338 O HOH A 514 -19.964 -19.673 9.930 1.00 48.25 O HETATM 2339 O HOH A 515 9.013 -0.275 28.464 1.00 42.05 O HETATM 2340 O HOH A 516 -16.640 -18.162 18.056 1.00 43.41 O HETATM 2341 O HOH A 517 -10.591 7.933 4.072 1.00 47.41 O HETATM 2342 O HOH A 518 6.434 -18.777 31.785 1.00 48.27 O HETATM 2343 O HOH A 519 -6.069 -11.236 -3.886 1.00 49.54 O HETATM 2344 O HOH A 520 2.365 -22.612 8.279 1.00 45.17 O HETATM 2345 O HOH A 521 -4.761 -18.107 -2.980 1.00 48.54 O HETATM 2346 O HOH A 522 -25.452 -19.826 8.066 1.00 49.21 O HETATM 2347 O HOH A 523 -19.027 -7.459 8.446 1.00 39.94 O HETATM 2348 O HOH A 524 0.342 -15.225 31.148 1.00 48.25 O HETATM 2349 O HOH A 525 -0.636 -11.182 31.842 1.00 45.66 O CONECT 702 952 CONECT 952 702 MASTER 256 0 0 14 9 0 0 6 2348 1 2 20 END