HEADER LYASE 20-NOV-09 3KS3 TITLE HIGH RESOLUTION STRUCTURE OF HUMAN CARBONIC ANHYDRASE II AT TITLE 2 0.9 A COMPND MOL_ID: 1; COMPND 2 MOLECULE: CARBONIC ANHYDRASE 2; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: CARBONIC ANHYDRASE II, CA-II, CARBONATE COMPND 5 DEHYDRATASE II, CARBONIC ANHYDRASE C, CAC; COMPND 6 EC: 4.2.1.1; COMPND 7 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: CA2; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 KEYWDS HIGH RESOLUTION, CARBONIC ANHYDRASE, SHORT HYDROGEN BOND EXPDTA X-RAY DIFFRACTION AUTHOR B.S.AVVARU REVDAT 1 26-JAN-10 3KS3 0 JRNL AUTH B.S.AVVARU,C.U.KIM,K.H.SIPPEL,S.M.GRUNER, JRNL AUTH 2 M.AGBANDJE-MCKENNA,D.N.SILVERMAN,R.MCKENNA JRNL TITL A SHORT, STRONG HYDROGEN BOND IN THE ACTIVE SITE OF JRNL TITL 2 HUMAN CARBONIC ANHYDRASE II. JRNL REF BIOCHEMISTRY V. 49 249 2010 JRNL REFN ISSN 0006-2960 JRNL PMID 20000378 JRNL DOI 10.1021/BI902007B REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 0.90 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.5_2) 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 : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 0.90 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.83 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.050 REMARK 3 COMPLETENESS FOR RANGE (%) : 88.4 REMARK 3 NUMBER OF REFLECTIONS : 158090 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.138 REMARK 3 R VALUE (WORKING SET) : 0.138 REMARK 3 FREE R VALUE : 0.145 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.220 REMARK 3 FREE R VALUE TEST SET COUNT : 1935 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 19.8377 - 1.9392 0.96 17265 212 0.1521 0.1601 REMARK 3 2 1.9392 - 1.5394 0.96 17013 212 0.1127 0.1159 REMARK 3 3 1.5394 - 1.3448 0.96 16888 203 0.1040 0.1119 REMARK 3 4 1.3448 - 1.2219 0.97 17153 204 0.0959 0.1008 REMARK 3 5 1.2219 - 1.1343 0.94 16651 203 0.0943 0.1058 REMARK 3 6 1.1343 - 1.0675 0.92 16170 210 0.0980 0.1022 REMARK 3 7 1.0675 - 1.0140 0.89 15663 200 0.1137 0.1138 REMARK 3 8 1.0140 - 0.9699 0.83 14619 175 0.1359 0.1442 REMARK 3 9 0.9699 - 0.9325 0.75 13233 166 0.1723 0.1922 REMARK 3 10 0.9325 - 0.9003 0.65 11500 150 0.2244 0.2359 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 : 0.41 REMARK 3 B_SOL : 60.48 REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.140 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 11.040 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 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 : 0.009 2216 REMARK 3 ANGLE : 1.392 3018 REMARK 3 CHIRALITY : 0.099 311 REMARK 3 PLANARITY : 0.008 397 REMARK 3 DIHEDRAL : 19.152 816 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 3KS3 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-DEC-09. REMARK 100 THE RCSB ID CODE IS RCSB056377. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 14-FEB-09 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : CHESS REMARK 200 BEAMLINE : A1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9772 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 164840 REMARK 200 RESOLUTION RANGE HIGH (A) : 0.900 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 92.3 REMARK 200 DATA REDUNDANCY : 6.100 REMARK 200 R MERGE (I) : 0.07800 REMARK 200 R SYM (I) : 0.07800 REMARK 200 FOR THE DATA SET : 25.0000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 0.90 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 0.92 REMARK 200 COMPLETENESS FOR SHELL (%) : 92.3 REMARK 200 DATA REDUNDANCY IN SHELL : 2.80 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.58000 REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: SHELXS REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 41.27 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.09 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: NULL REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,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 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 20.67950 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 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 MET A 1 REMARK 465 SER A 2 REMARK 465 HIS A 3 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 ARG A 27 55.42 -143.93 REMARK 500 GLU A 106 -61.49 -93.14 REMARK 500 LYS A 111 -3.75 74.09 REMARK 500 PHE A 176 66.50 -152.38 REMARK 500 ASN A 244 47.38 -93.87 REMARK 500 LYS A 252 -139.46 54.18 REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN A 262 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HOH A 402 O REMARK 620 2 HIS A 119 ND1 118.0 REMARK 620 3 HIS A 94 NE2 110.8 113.6 REMARK 620 4 HIS A 96 NE2 108.2 99.5 105.1 REMARK 620 5 HOH A 707 O 62.6 78.5 87.3 167.0 REMARK 620 N 1 2 3 4 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 262 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 304 DBREF 3KS3 A 1 261 UNP P00918 CAH2_HUMAN 1 260 SEQRES 1 A 260 MET SER HIS HIS TRP GLY TYR GLY LYS HIS ASN GLY PRO SEQRES 2 A 260 GLU HIS TRP HIS LYS ASP PHE PRO ILE ALA LYS GLY GLU SEQRES 3 A 260 ARG GLN SER PRO VAL ASP ILE ASP THR HIS THR ALA LYS SEQRES 4 A 260 TYR ASP PRO SER LEU LYS PRO LEU SER VAL SER TYR ASP SEQRES 5 A 260 GLN ALA THR SER LEU ARG ILE LEU ASN ASN GLY HIS ALA SEQRES 6 A 260 PHE ASN VAL GLU PHE ASP ASP SER GLN ASP LYS ALA VAL SEQRES 7 A 260 LEU LYS GLY GLY PRO LEU ASP GLY THR TYR ARG LEU ILE SEQRES 8 A 260 GLN PHE HIS PHE HIS TRP GLY SER LEU ASP GLY GLN GLY SEQRES 9 A 260 SER GLU HIS THR VAL ASP LYS LYS LYS TYR ALA ALA GLU SEQRES 10 A 260 LEU HIS LEU VAL HIS TRP ASN THR LYS TYR GLY ASP PHE SEQRES 11 A 260 GLY LYS ALA VAL GLN GLN PRO ASP GLY LEU ALA VAL LEU SEQRES 12 A 260 GLY ILE PHE LEU LYS VAL GLY SER ALA LYS PRO GLY LEU SEQRES 13 A 260 GLN LYS VAL VAL ASP VAL LEU ASP SER ILE LYS THR LYS SEQRES 14 A 260 GLY LYS SER ALA ASP PHE THR ASN PHE ASP PRO ARG GLY SEQRES 15 A 260 LEU LEU PRO GLU SER LEU ASP TYR TRP THR TYR PRO GLY SEQRES 16 A 260 SER LEU THR THR PRO PRO LEU LEU GLU CYS VAL THR TRP SEQRES 17 A 260 ILE VAL LEU LYS GLU PRO ILE SER VAL SER SER GLU GLN SEQRES 18 A 260 VAL LEU LYS PHE ARG LYS LEU ASN PHE ASN GLY GLU GLY SEQRES 19 A 260 GLU PRO GLU GLU LEU MET VAL ASP ASN TRP ARG PRO ALA SEQRES 20 A 260 GLN PRO LEU LYS ASN ARG GLN ILE LYS ALA SER PHE LYS HET ZN A 262 1 HET GOL A 304 6 HETNAM ZN ZINC ION HETNAM GOL GLYCEROL FORMUL 2 ZN ZN 2+ FORMUL 3 GOL C3 H8 O3 FORMUL 4 HOH *481(H2 O) HELIX 1 1 GLY A 12 ASP A 19 5 8 HELIX 2 2 PHE A 20 GLY A 25 5 6 HELIX 3 3 LYS A 127 GLY A 129 5 3 HELIX 4 4 ASP A 130 VAL A 135 1 6 HELIX 5 5 LYS A 154 GLY A 156 5 3 HELIX 6 6 LEU A 157 LEU A 164 1 8 HELIX 7 7 ASP A 165 LYS A 168 5 4 HELIX 8 8 ASP A 180 LEU A 185 5 6 HELIX 9 9 SER A 219 ARG A 227 1 9 SHEET 1 A 2 ASP A 32 ILE A 33 0 SHEET 2 A 2 THR A 108 VAL A 109 1 O THR A 108 N ILE A 33 SHEET 1 B10 LYS A 39 TYR A 40 0 SHEET 2 B10 LYS A 257 ALA A 258 1 O ALA A 258 N LYS A 39 SHEET 3 B10 TYR A 191 GLY A 196 -1 N THR A 193 O LYS A 257 SHEET 4 B10 VAL A 207 LEU A 212 -1 O VAL A 207 N GLY A 196 SHEET 5 B10 LEU A 141 VAL A 150 1 N GLY A 145 O LEU A 212 SHEET 6 B10 ALA A 116 ASN A 124 -1 N LEU A 118 O ILE A 146 SHEET 7 B10 TYR A 88 TRP A 97 -1 N HIS A 94 O HIS A 119 SHEET 8 B10 PHE A 66 PHE A 70 -1 N VAL A 68 O PHE A 93 SHEET 9 B10 SER A 56 ASN A 61 -1 N LEU A 57 O GLU A 69 SHEET 10 B10 SER A 173 ASP A 175 -1 O ALA A 174 N ILE A 59 SHEET 1 C 6 LEU A 47 SER A 50 0 SHEET 2 C 6 VAL A 78 GLY A 81 -1 O LYS A 80 N SER A 48 SHEET 3 C 6 TYR A 88 TRP A 97 -1 O TYR A 88 N LEU A 79 SHEET 4 C 6 ALA A 116 ASN A 124 -1 O HIS A 119 N HIS A 94 SHEET 5 C 6 LEU A 141 VAL A 150 -1 O ILE A 146 N LEU A 118 SHEET 6 C 6 ILE A 216 VAL A 218 1 O ILE A 216 N PHE A 147 LINK ZN ZN A 262 O HOH A 402 1555 1555 1.90 LINK ND1 HIS A 119 ZN ZN A 262 1555 1555 2.02 LINK NE2 HIS A 94 ZN ZN A 262 1555 1555 2.03 LINK NE2 HIS A 96 ZN ZN A 262 1555 1555 2.04 LINK ZN ZN A 262 O HOH A 707 1555 1555 2.57 CISPEP 1 SER A 29 PRO A 30 0 -2.73 CISPEP 2 PRO A 201 PRO A 202 0 15.04 SITE 1 AC1 5 HIS A 94 HIS A 96 HIS A 119 HOH A 402 SITE 2 AC1 5 HOH A 707 SITE 1 AC2 8 TYR A 7 ASP A 243 TRP A 245 HOH A 316 SITE 2 AC2 8 HOH A 451 HOH A 608 HOH A 651 HOH A 666 CRYST1 42.354 41.359 72.308 90.00 104.42 90.00 P 1 21 1 2 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.023611 0.000000 0.006071 0.00000 SCALE2 0.000000 0.024179 0.000000 0.00000 SCALE3 0.000000 0.000000 0.014280 0.00000 ATOM 1 N HIS A 4 11.137 -0.211 8.321 1.00 29.07 N ANISOU 1 N HIS A 4 2036 5689 3319 -786 1256 55 N ATOM 2 CA HIS A 4 9.914 0.333 8.875 1.00 24.50 C ANISOU 2 CA HIS A 4 2595 3802 2912 -700 1125 333 C ATOM 3 C HIS A 4 9.177 -0.776 9.621 1.00 19.06 C ANISOU 3 C HIS A 4 2084 2816 2340 -554 920 -141 C ATOM 4 O HIS A 4 9.351 -1.961 9.325 1.00 19.45 O ANISOU 4 O HIS A 4 2352 2925 2114 -247 861 -286 O ATOM 5 CB AHIS A 4 9.096 0.896 7.708 0.43 28.88 C ANISOU 5 CB AHIS A 4 4012 3813 3148 -85 1105 649 C ATOM 6 CB BHIS A 4 9.012 0.956 7.806 0.57 26.45 C ANISOU 6 CB BHIS A 4 2922 4158 2969 -689 995 634 C ATOM 7 CG AHIS A 4 7.748 1.413 8.086 0.43 29.33 C ANISOU 7 CG AHIS A 4 3962 4125 3057 32 501 968 C ATOM 8 CG BHIS A 4 9.203 2.433 7.642 0.57 34.20 C ANISOU 8 CG BHIS A 4 5600 3748 3646 -12 -276 -76 C ATOM 9 ND1AHIS A 4 7.507 2.746 8.340 0.43 30.10 N ANISOU 9 ND1AHIS A 4 3936 4112 3391 387 454 1429 N ATOM 10 ND1BHIS A 4 9.998 3.178 8.486 0.57 39.32 N ANISOU 10 ND1BHIS A 4 7181 3494 4265 420 -1178 -491 N ATOM 11 CD2AHIS A 4 6.558 0.782 8.216 0.43 30.25 C ANISOU 11 CD2AHIS A 4 4006 4635 2853 -148 147 1145 C ATOM 12 CD2BHIS A 4 8.684 3.306 6.746 0.57 36.87 C ANISOU 12 CD2BHIS A 4 6663 3174 4171 1131 -872 -683 C ATOM 13 CE1AHIS A 4 6.228 2.910 8.628 0.43 31.94 C ANISOU 13 CE1AHIS A 4 3972 4827 3338 535 353 1496 C ATOM 14 CE1BHIS A 4 9.974 4.444 8.107 0.57 42.75 C ANISOU 14 CE1BHIS A 4 7859 3666 4717 -64 -1336 -317 C ATOM 15 NE2AHIS A 4 5.632 1.733 8.563 0.43 31.98 N ANISOU 15 NE2AHIS A 4 4060 5464 2629 -109 733 733 N ATOM 16 NE2BHIS A 4 9.182 4.549 7.055 0.57 41.34 N ANISOU 16 NE2BHIS A 4 7465 3553 4689 169 -1230 -225 N ATOM 17 N TRP A 5 8.374 -0.399 10.608 1.00 16.79 N ANISOU 17 N TRP A 5 1750 2437 2193 -665 790 -159 N ATOM 18 CA TRP A 5 7.687 -1.379 11.435 1.00 12.54 C ANISOU 18 CA TRP A 5 1262 1736 1766 -300 378 -142 C ATOM 19 C TRP A 5 6.679 -2.184 10.619 1.00 11.47 C ANISOU 19 C TRP A 5 1244 1607 1506 -133 304 -88 C ATOM 20 O TRP A 5 6.156 -1.715 9.605 1.00 12.72 O ANISOU 20 O TRP A 5 1525 1734 1575 -232 311 73 O ATOM 21 CB TRP A 5 6.994 -0.684 12.613 1.00 10.89 C ANISOU 21 CB TRP A 5 1083 1537 1519 -239 114 -88 C ATOM 22 CG TRP A 5 5.832 0.177 12.221 1.00 10.21 C ANISOU 22 CG TRP A 5 1187 1444 1248 -213 143 24 C ATOM 23 CD1 TRP A 5 5.846 1.500 11.913 1.00 11.95 C ANISOU 23 CD1 TRP A 5 1510 1606 1423 -240 274 219 C ATOM 24 CD2 TRP A 5 4.461 -0.240 12.131 1.00 9.54 C ANISOU 24 CD2 TRP A 5 1142 1446 1039 -75 62 7 C ATOM 25 NE1 TRP A 5 4.581 1.938 11.610 1.00 12.28 N ANISOU 25 NE1 TRP A 5 1697 1573 1395 33 333 290 N ATOM 26 CE2 TRP A 5 3.705 0.888 11.750 1.00 10.68 C ANISOU 26 CE2 TRP A 5 1339 1598 1121 112 98 133 C ATOM 27 CE3 TRP A 5 3.800 -1.455 12.365 1.00 9.51 C ANISOU 27 CE3 TRP A 5 1115 1462 1038 -184 40 -182 C ATOM 28 CZ2 TRP A 5 2.319 0.832 11.585 1.00 12.02 C ANISOU 28 CZ2 TRP A 5 1428 2002 1138 183 -20 -24 C ATOM 29 CZ3 TRP A 5 2.422 -1.510 12.194 1.00 10.51 C ANISOU 29 CZ3 TRP A 5 1120 1794 1079 -131 -16 -377 C ATOM 30 CH2 TRP A 5 1.700 -0.374 11.800 1.00 11.55 C ANISOU 30 CH2 TRP A 5 1144 2134 1110 41 -79 -257 C ATOM 31 N GLY A 6 6.377 -3.386 11.094 1.00 10.25 N ANISOU 31 N GLY A 6 1177 1367 1352 -31 228 -156 N ATOM 32 CA GLY A 6 5.348 -4.213 10.492 1.00 10.08 C ANISOU 32 CA GLY A 6 1240 1388 1202 -32 176 -121 C ATOM 33 C GLY A 6 5.010 -5.382 11.393 1.00 9.32 C ANISOU 33 C GLY A 6 1085 1338 1119 45 202 -149 C ATOM 34 O GLY A 6 5.032 -5.261 12.621 1.00 9.98 O ANISOU 34 O GLY A 6 1130 1603 1058 85 94 -162 O ATOM 35 N TYR A 7 4.718 -6.522 10.767 1.00 9.61 N ANISOU 35 N TYR A 7 1135 1261 1256 59 248 -95 N ATOM 36 CA TYR A 7 4.306 -7.707 11.498 1.00 10.95 C ANISOU 36 CA TYR A 7 1225 1228 1709 102 340 -64 C ATOM 37 C TYR A 7 5.159 -8.917 11.107 1.00 14.47 C ANISOU 37 C TYR A 7 1433 1412 2654 297 693 102 C ATOM 38 O TYR A 7 4.787 -10.044 11.370 1.00 18.57 O ANISOU 38 O TYR A 7 1783 1468 3804 403 1112 446 O ATOM 39 CB TYR A 7 2.825 -8.010 11.255 1.00 9.98 C ANISOU 39 CB TYR A 7 1222 1163 1407 -24 249 -169 C ATOM 40 CG TYR A 7 1.914 -6.925 11.798 1.00 8.34 C ANISOU 40 CG TYR A 7 1007 1057 1104 -104 75 -151 C ATOM 41 CD1 TYR A 7 1.525 -6.920 13.133 1.00 7.71 C ANISOU 41 CD1 TYR A 7 917 982 1030 -95 -13 -43 C ATOM 42 CD2 TYR A 7 1.470 -5.886 10.987 1.00 8.34 C ANISOU 42 CD2 TYR A 7 1095 1060 1013 -150 107 -88 C ATOM 43 CE1 TYR A 7 0.688 -5.926 13.641 1.00 7.32 C ANISOU 43 CE1 TYR A 7 870 981 928 -102 -45 17 C ATOM 44 CE2 TYR A 7 0.633 -4.910 11.476 1.00 8.17 C ANISOU 44 CE2 TYR A 7 1046 1155 902 -141 -8 -20 C ATOM 45 CZ TYR A 7 0.254 -4.924 12.810 1.00 7.46 C ANISOU 45 CZ TYR A 7 878 1063 892 -111 -51 -23 C ATOM 46 OH TYR A 7 -0.586 -3.927 13.248 1.00 7.71 O ANISOU 46 OH TYR A 7 999 1041 890 -1 -65 18 O ATOM 47 N GLY A 8 6.305 -8.674 10.484 1.00 14.48 N ANISOU 47 N GLY A 8 1526 1659 2316 286 680 -149 N ATOM 48 CA GLY A 8 7.239 -9.748 10.142 1.00 17.39 C ANISOU 48 CA GLY A 8 1935 2062 2610 514 890 75 C ATOM 49 C GLY A 8 8.200 -10.100 11.275 1.00 20.14 C ANISOU 49 C GLY A 8 2246 2252 3155 801 803 363 C ATOM 50 O GLY A 8 8.211 -9.445 12.323 1.00 21.39 O ANISOU 50 O GLY A 8 2015 3319 2791 693 760 427 O ATOM 51 N LYS A 9 9.028 -11.119 11.061 1.00 22.08 N ANISOU 51 N LYS A 9 2120 2077 4194 648 634 457 N ATOM 52 CA LYS A 9 9.954 -11.594 12.095 1.00 25.03 C ANISOU 52 CA LYS A 9 2488 2556 4468 843 704 850 C ATOM 53 C LYS A 9 10.960 -10.519 12.443 1.00 24.62 C ANISOU 53 C LYS A 9 2416 3590 3347 479 850 658 C ATOM 54 O LYS A 9 11.416 -10.400 13.584 1.00 25.93 O ANISOU 54 O LYS A 9 2815 3931 3107 1124 696 791 O ATOM 55 CB LYS A 9 10.724 -12.831 11.628 1.00 30.14 C ANISOU 55 CB LYS A 9 2643 3157 5653 1276 746 1297 C ATOM 56 CG LYS A 9 11.823 -13.277 12.597 1.00 38.12 C ANISOU 56 CG LYS A 9 3423 3990 7071 1543 -497 1432 C ATOM 57 CD LYS A 9 12.680 -14.383 12.006 1.00 46.54 C ANISOU 57 CD LYS A 9 5384 3775 8524 1647 -1999 935 C ATOM 58 CE LYS A 9 11.817 -15.446 11.346 1.00 60.94 C ANISOU 58 CE LYS A 9 8220 4869 10066 1289 -3015 -152 C ATOM 59 NZ LYS A 9 12.586 -16.673 11.003 1.00 71.57 N ANISOU 59 NZ LYS A 9 10562 5737 10895 2935 -4889 -903 N ATOM 60 N HIS A 10 11.317 -9.735 11.439 1.00 19.24 N ANISOU 60 N HIS A 10 2124 2364 2824 996 1042 278 N ATOM 61 CA HIS A 10 12.382 -8.790 11.624 1.00 18.76 C ANISOU 61 CA HIS A 10 1967 2586 2575 952 935 48 C ATOM 62 C HIS A 10 11.888 -7.391 11.978 1.00 17.03 C ANISOU 62 C HIS A 10 1729 2543 2200 782 678 -29 C ATOM 63 O HIS A 10 12.689 -6.551 12.371 1.00 18.92 O ANISOU 63 O HIS A 10 1670 3222 2295 944 224 -498 O ATOM 64 CB HIS A 10 13.271 -8.804 10.381 1.00 20.42 C ANISOU 64 CB HIS A 10 2024 2956 2778 760 1032 -425 C ATOM 65 CG HIS A 10 13.780 -10.170 10.042 1.00 22.18 C ANISOU 65 CG HIS A 10 2410 2855 3164 721 1250 -235 C ATOM 66 ND1 HIS A 10 14.780 -10.783 10.762 1.00 23.21 N ANISOU 66 ND1 HIS A 10 2736 2855 3227 698 1457 354 N ATOM 67 CD2 HIS A 10 13.412 -11.054 9.084 1.00 24.83 C ANISOU 67 CD2 HIS A 10 2843 2992 3599 887 1353 -492 C ATOM 68 CE1 HIS A 10 15.025 -11.976 10.249 1.00 24.23 C ANISOU 68 CE1 HIS A 10 2774 2593 3841 614 1536 478 C ATOM 69 NE2 HIS A 10 14.204 -12.167 9.231 1.00 26.97 N ANISOU 69 NE2 HIS A 10 3225 2757 4266 865 1296 -318 N ATOM 70 N ASN A 11 10.576 -7.141 11.884 1.00 14.80 N ANISOU 70 N ASN A 11 1613 2159 1851 591 688 120 N ATOM 71 CA ASN A 11 10.056 -5.799 12.146 1.00 13.51 C ANISOU 71 CA ASN A 11 1329 2217 1587 457 452 -98 C ATOM 72 C ASN A 11 8.751 -5.778 12.946 1.00 12.37 C ANISOU 72 C ASN A 11 1089 2211 1401 372 275 -105 C ATOM 73 O ASN A 11 8.093 -4.745 13.032 1.00 12.42 O ANISOU 73 O ASN A 11 1210 2182 1326 354 288 -40 O ATOM 74 CB ASN A 11 9.881 -5.013 10.851 1.00 12.32 C ANISOU 74 CB ASN A 11 1257 1868 1558 279 436 -140 C ATOM 75 CG ASN A 11 8.797 -5.582 9.959 1.00 12.47 C ANISOU 75 CG ASN A 11 1408 1831 1500 187 441 -139 C ATOM 76 OD1 ASN A 11 8.205 -6.618 10.249 1.00 14.06 O ANISOU 76 OD1 ASN A 11 1583 2181 1579 -129 390 -22 O ATOM 77 ND2 ASN A 11 8.503 -4.873 8.884 1.00 14.96 N ANISOU 77 ND2 ASN A 11 1808 2300 1575 91 387 20 N ATOM 78 N GLY A 12 8.416 -6.916 13.547 1.00 12.34 N ANISOU 78 N GLY A 12 1157 2172 1361 351 248 -132 N ATOM 79 CA GLY A 12 7.144 -7.084 14.238 1.00 12.50 C ANISOU 79 CA GLY A 12 1255 2203 1292 226 298 -167 C ATOM 80 C GLY A 12 7.102 -6.512 15.635 1.00 10.25 C ANISOU 80 C GLY A 12 980 1784 1132 280 103 2 C ATOM 81 O GLY A 12 8.034 -5.834 16.074 1.00 10.47 O ANISOU 81 O GLY A 12 960 1879 1139 242 96 70 O ATOM 82 N PRO A 13 6.016 -6.800 16.354 1.00 9.46 N ANISOU 82 N PRO A 13 1042 1433 1119 131 120 -99 N ATOM 83 CA PRO A 13 5.754 -6.166 17.649 1.00 9.27 C ANISOU 83 CA PRO A 13 1064 1317 1141 11 173 -28 C ATOM 84 C PRO A 13 6.902 -6.197 18.645 1.00 9.01 C ANISOU 84 C PRO A 13 1104 1217 1104 42 111 -38 C ATOM 85 O PRO A 13 7.002 -5.253 19.435 1.00 9.54 O ANISOU 85 O PRO A 13 1008 1423 1195 -25 94 -119 O ATOM 86 CB PRO A 13 4.545 -6.956 18.159 1.00 10.10 C ANISOU 86 CB PRO A 13 1218 1373 1248 -170 234 -96 C ATOM 87 CG PRO A 13 3.771 -7.254 16.900 1.00 10.59 C ANISOU 87 CG PRO A 13 1203 1520 1299 -112 200 -206 C ATOM 88 CD PRO A 13 4.839 -7.552 15.863 1.00 10.48 C ANISOU 88 CD PRO A 13 1153 1572 1258 45 182 -205 C ATOM 89 N GLU A 14 7.726 -7.235 18.655 1.00 10.64 N ANISOU 89 N GLU A 14 1472 1290 1280 179 -86 46 N ATOM 90 CA GLU A 14 8.812 -7.315 19.621 1.00 12.18 C ANISOU 90 CA GLU A 14 1767 1337 1523 317 -268 116 C ATOM 91 C GLU A 14 9.963 -6.337 19.315 1.00 10.80 C ANISOU 91 C GLU A 14 1358 1365 1381 489 -233 -8 C ATOM 92 O GLU A 14 10.862 -6.130 20.146 1.00 12.51 O ANISOU 92 O GLU A 14 1626 1680 1448 497 -375 5 O ATOM 93 CB GLU A 14 9.300 -8.751 19.690 1.00 14.83 C ANISOU 93 CB GLU A 14 2066 1441 2128 464 -331 136 C ATOM 94 CG AGLU A 14 10.064 -9.201 18.436 0.57 14.93 C ANISOU 94 CG AGLU A 14 1565 1768 2340 582 -654 58 C ATOM 95 CG BGLU A 14 8.201 -9.746 20.056 0.43 13.90 C ANISOU 95 CG BGLU A 14 2025 1135 2122 378 -560 -32 C ATOM 96 CD AGLU A 14 9.246 -9.770 17.252 0.57 19.09 C ANISOU 96 CD AGLU A 14 2770 2167 2318 1264 -666 -88 C ATOM 97 CD BGLU A 14 7.303 -9.268 21.190 0.43 14.20 C ANISOU 97 CD BGLU A 14 2225 1129 2039 361 -308 197 C ATOM 98 OE1AGLU A 14 8.091 -9.339 16.949 0.57 17.04 O ANISOU 98 OE1AGLU A 14 2597 1642 2236 1024 -1017 -871 O ATOM 99 OE1BGLU A 14 7.849 -8.873 22.244 0.43 15.21 O ANISOU 99 OE1BGLU A 14 1724 2137 1917 -253 -54 507 O ATOM 100 OE2AGLU A 14 9.835 -10.641 16.564 0.57 15.98 O ANISOU 100 OE2AGLU A 14 2136 1431 2503 342 -713 -40 O ATOM 101 OE2BGLU A 14 6.054 -9.303 21.037 0.43 14.90 O ANISOU 101 OE2BGLU A 14 2312 1423 1925 966 -539 -251 O ATOM 102 N HIS A 15 9.932 -5.741 18.122 1.00 10.16 N ANISOU 102 N HIS A 15 1063 1471 1327 392 -96 -61 N ATOM 103 CA HIS A 15 10.939 -4.770 17.703 1.00 9.93 C ANISOU 103 CA HIS A 15 950 1528 1295 373 -64 -61 C ATOM 104 C HIS A 15 10.483 -3.316 17.850 1.00 9.54 C ANISOU 104 C HIS A 15 770 1567 1286 239 -27 -78 C ATOM 105 O HIS A 15 11.314 -2.408 17.787 1.00 9.89 O ANISOU 105 O HIS A 15 738 1616 1404 201 1 -64 O ATOM 106 CB HIS A 15 11.300 -4.975 16.236 1.00 11.06 C ANISOU 106 CB HIS A 15 967 1817 1419 489 -135 -148 C ATOM 107 CG HIS A 15 12.007 -6.258 15.968 1.00 13.33 C ANISOU 107 CG HIS A 15 1292 2159 1613 702 -124 -332 C ATOM 108 ND1 HIS A 15 13.371 -6.389 16.108 1.00 16.98 N ANISOU 108 ND1 HIS A 15 1495 2930 2028 1181 -277 -699 N ATOM 109 CD2 HIS A 15 11.539 -7.465 15.581 1.00 15.91 C ANISOU 109 CD2 HIS A 15 2045 2082 1918 987 -124 -438 C ATOM 110 CE1 HIS A 15 13.711 -7.628 15.816 1.00 20.43 C ANISOU 110 CE1 HIS A 15 2158 3100 2503 1578 -328 -906 C ATOM 111 NE2 HIS A 15 12.623 -8.301 15.491 1.00 19.02 N ANISOU 111 NE2 HIS A 15 2299 2567 2361 1304 76 -606 N ATOM 112 N TRP A 16 9.169 -3.093 18.002 1.00 8.79 N ANISOU 112 N TRP A 16 838 1355 1146 151 -42 -78 N ATOM 113 CA TRP A 16 8.637 -1.741 17.901 1.00 8.31 C ANISOU 113 CA TRP A 16 662 1338 1158 139 -30 -119 C ATOM 114 C TRP A 16 9.229 -0.773 18.932 1.00 8.28 C ANISOU 114 C TRP A 16 602 1341 1203 140 -80 -71 C ATOM 115 O TRP A 16 9.340 0.425 18.656 1.00 9.06 O ANISOU 115 O TRP A 16 790 1344 1308 40 -149 -74 O ATOM 116 CB TRP A 16 7.097 -1.760 18.009 1.00 7.97 C ANISOU 116 CB TRP A 16 653 1311 1064 66 -39 -101 C ATOM 117 CG TRP A 16 6.408 -2.469 16.882 1.00 7.75 C ANISOU 117 CG TRP A 16 689 1250 1005 73 -59 -92 C ATOM 118 CD1 TRP A 16 6.950 -2.946 15.717 1.00 8.48 C ANISOU 118 CD1 TRP A 16 807 1412 1004 145 64 -117 C ATOM 119 CD2 TRP A 16 4.998 -2.743 16.813 1.00 7.29 C ANISOU 119 CD2 TRP A 16 788 1018 966 45 -17 -26 C ATOM 120 NE1 TRP A 16 5.967 -3.497 14.931 1.00 8.49 N ANISOU 120 NE1 TRP A 16 839 1437 951 69 4 -161 N ATOM 121 CE2 TRP A 16 4.761 -3.396 15.588 1.00 7.45 C ANISOU 121 CE2 TRP A 16 792 1150 887 62 31 -57 C ATOM 122 CE3 TRP A 16 3.921 -2.520 17.687 1.00 7.56 C ANISOU 122 CE3 TRP A 16 808 1046 1017 57 28 -53 C ATOM 123 CZ2 TRP A 16 3.487 -3.819 15.194 1.00 7.76 C ANISOU 123 CZ2 TRP A 16 885 1134 928 -18 -61 -84 C ATOM 124 CZ3 TRP A 16 2.668 -2.937 17.293 1.00 7.63 C ANISOU 124 CZ3 TRP A 16 805 1074 1019 -31 -14 -40 C ATOM 125 CH2 TRP A 16 2.453 -3.573 16.075 1.00 7.82 C ANISOU 125 CH2 TRP A 16 800 1176 994 -19 1 -57 C ATOM 126 N HIS A 17 9.573 -1.287 20.114 1.00 8.52 N ANISOU 126 N HIS A 17 674 1423 1139 78 -58 -116 N ATOM 127 CA HIS A 17 10.073 -0.436 21.168 1.00 9.10 C ANISOU 127 CA HIS A 17 767 1506 1185 47 -88 -66 C ATOM 128 C HIS A 17 11.341 0.341 20.789 1.00 9.65 C ANISOU 128 C HIS A 17 624 1736 1307 -22 -149 -68 C ATOM 129 O HIS A 17 11.612 1.375 21.389 1.00 10.67 O ANISOU 129 O HIS A 17 789 1811 1456 -112 -77 -161 O ATOM 130 CB HIS A 17 10.339 -1.246 22.435 1.00 9.70 C ANISOU 130 CB HIS A 17 808 1631 1246 150 -79 21 C ATOM 131 CG HIS A 17 11.555 -2.117 22.337 1.00 10.41 C ANISOU 131 CG HIS A 17 841 1827 1287 181 -134 157 C ATOM 132 ND1 HIS A 17 12.768 -1.775 22.899 1.00 12.52 N ANISOU 132 ND1 HIS A 17 902 2422 1432 168 -199 171 N ATOM 133 CD2 HIS A 17 11.734 -3.296 21.711 1.00 11.49 C ANISOU 133 CD2 HIS A 17 1138 1841 1384 404 -3 212 C ATOM 134 CE1 HIS A 17 13.640 -2.724 22.628 1.00 13.52 C ANISOU 134 CE1 HIS A 17 1046 2633 1459 473 -114 251 C ATOM 135 NE2 HIS A 17 13.047 -3.658 21.910 1.00 12.59 N ANISOU 135 NE2 HIS A 17 1150 2181 1454 474 3 412 N ATOM 136 N LYS A 18 12.109 -0.152 19.821 1.00 10.09 N ANISOU 136 N LYS A 18 657 1804 1372 -13 -83 15 N ATOM 137 CA LYS A 18 13.344 0.545 19.460 1.00 11.33 C ANISOU 137 CA LYS A 18 604 2068 1632 -25 -56 170 C ATOM 138 C LYS A 18 13.077 1.912 18.838 1.00 12.70 C ANISOU 138 C LYS A 18 662 2067 2098 -142 -189 321 C ATOM 139 O LYS A 18 13.762 2.883 19.122 1.00 17.81 O ANISOU 139 O LYS A 18 1421 2402 2942 -692 -789 801 O ATOM 140 CB LYS A 18 14.201 -0.339 18.553 1.00 11.78 C ANISOU 140 CB LYS A 18 625 2236 1616 130 -36 276 C ATOM 141 CG LYS A 18 14.806 -1.534 19.292 1.00 13.39 C ANISOU 141 CG LYS A 18 1030 2466 1591 496 -62 223 C ATOM 142 CD LYS A 18 15.550 -2.488 18.360 1.00 13.42 C ANISOU 142 CD LYS A 18 977 2445 1677 558 21 323 C ATOM 143 CE LYS A 18 14.570 -3.415 17.679 1.00 13.13 C ANISOU 143 CE LYS A 18 1106 2216 1667 519 112 336 C ATOM 144 NZ LYS A 18 15.237 -4.248 16.641 1.00 13.70 N ANISOU 144 NZ LYS A 18 997 2546 1661 722 52 345 N ATOM 145 N ASP A 19 12.067 1.989 17.987 1.00 11.87 N ANISOU 145 N ASP A 19 747 2102 1662 10 60 228 N ATOM 146 CA ASP A 19 11.667 3.269 17.410 1.00 12.20 C ANISOU 146 CA ASP A 19 888 2109 1640 12 129 239 C ATOM 147 C ASP A 19 10.603 3.984 18.242 1.00 10.87 C ANISOU 147 C ASP A 19 801 1572 1757 -127 125 166 C ATOM 148 O ASP A 19 10.495 5.204 18.153 1.00 12.90 O ANISOU 148 O ASP A 19 1178 1591 2130 -297 300 197 O ATOM 149 CB ASP A 19 11.114 3.086 16.002 1.00 14.64 C ANISOU 149 CB ASP A 19 1111 2748 1703 154 94 224 C ATOM 150 CG ASP A 19 12.194 3.010 14.936 1.00 24.86 C ANISOU 150 CG ASP A 19 2037 5043 2368 -395 1038 -550 C ATOM 151 OD1 ASP A 19 13.297 3.575 15.104 1.00 25.01 O ANISOU 151 OD1 ASP A 19 1872 5070 2562 -283 1103 -78 O ATOM 152 OD2 ASP A 19 11.903 2.398 13.897 1.00 37.83 O ANISOU 152 OD2 ASP A 19 3132 7675 3566 -1221 1981 -2526 O ATOM 153 N PHE A 20 9.819 3.222 19.024 1.00 9.73 N ANISOU 153 N PHE A 20 759 1442 1496 -84 -8 43 N ATOM 154 CA PHE A 20 8.679 3.766 19.770 1.00 9.32 C ANISOU 154 CA PHE A 20 793 1323 1424 -114 22 -57 C ATOM 155 C PHE A 20 8.777 3.268 21.203 1.00 9.53 C ANISOU 155 C PHE A 20 792 1410 1419 -91 10 -92 C ATOM 156 O PHE A 20 8.120 2.299 21.578 1.00 9.37 O ANISOU 156 O PHE A 20 901 1314 1346 -44 14 -80 O ATOM 157 CB PHE A 20 7.352 3.324 19.114 1.00 10.08 C ANISOU 157 CB PHE A 20 831 1537 1461 -149 -41 28 C ATOM 158 CG PHE A 20 7.280 3.692 17.656 1.00 10.77 C ANISOU 158 CG PHE A 20 788 1712 1593 -206 -15 198 C ATOM 159 CD1 PHE A 20 6.873 4.962 17.264 1.00 12.63 C ANISOU 159 CD1 PHE A 20 1138 1824 1837 -260 -10 400 C ATOM 160 CD2 PHE A 20 7.660 2.785 16.676 1.00 11.82 C ANISOU 160 CD2 PHE A 20 860 2095 1537 -229 75 97 C ATOM 161 CE1 PHE A 20 6.859 5.315 15.925 1.00 13.95 C ANISOU 161 CE1 PHE A 20 1079 2279 1943 -266 -53 633 C ATOM 162 CE2 PHE A 20 7.654 3.141 15.332 1.00 13.32 C ANISOU 162 CE2 PHE A 20 921 2504 1634 -272 -17 248 C ATOM 163 CZ PHE A 20 7.251 4.403 14.965 1.00 14.26 C ANISOU 163 CZ PHE A 20 1038 2533 1848 -411 42 520 C ATOM 164 N PRO A 21 9.609 3.921 22.037 1.00 10.75 N ANISOU 164 N PRO A 21 846 1650 1589 -216 -28 -91 N ATOM 165 CA PRO A 21 9.859 3.384 23.378 1.00 11.20 C ANISOU 165 CA PRO A 21 812 1899 1545 -193 -86 -182 C ATOM 166 C PRO A 21 8.598 3.286 24.257 1.00 9.86 C ANISOU 166 C PRO A 21 775 1625 1346 -144 -206 -189 C ATOM 167 O PRO A 21 8.600 2.524 25.231 1.00 10.71 O ANISOU 167 O PRO A 21 849 1876 1344 -68 -217 -139 O ATOM 168 CB PRO A 21 10.918 4.349 23.971 1.00 13.68 C ANISOU 168 CB PRO A 21 1015 2285 1899 -456 -300 -153 C ATOM 169 CG PRO A 21 10.871 5.541 23.092 1.00 15.93 C ANISOU 169 CG PRO A 21 1733 2203 2116 -751 -352 -167 C ATOM 170 CD PRO A 21 10.551 5.004 21.724 1.00 12.84 C ANISOU 170 CD PRO A 21 1097 1845 1935 -528 -161 -109 C ATOM 171 N AILE A 22 7.566 4.060 23.934 0.90 9.34 N ANISOU 171 N AILE A 22 740 1456 1352 -176 -104 -187 N ATOM 172 N BILE A 22 7.555 4.007 23.868 0.10 8.29 N ANISOU 172 N BILE A 22 516 1447 1188 -383 -325 -233 N ATOM 173 CA AILE A 22 6.286 3.951 24.670 0.90 9.00 C ANISOU 173 CA AILE A 22 831 1319 1268 -135 -48 -187 C ATOM 174 CA BILE A 22 6.273 3.978 24.559 0.10 7.65 C ANISOU 174 CA BILE A 22 649 1315 941 -274 -140 -225 C ATOM 175 C AILE A 22 5.678 2.545 24.545 0.90 8.61 C ANISOU 175 C AILE A 22 821 1318 1130 -17 -122 -148 C ATOM 176 C BILE A 22 5.568 2.626 24.384 0.10 7.74 C ANISOU 176 C BILE A 22 680 1235 1028 -216 72 -73 C ATOM 177 O AILE A 22 4.768 2.193 25.295 0.90 8.92 O ANISOU 177 O AILE A 22 853 1348 1186 -14 -101 -139 O ATOM 178 O BILE A 22 4.481 2.409 24.918 0.10 9.79 O ANISOU 178 O BILE A 22 1015 1622 1081 -282 474 183 O ATOM 179 CB AILE A 22 5.299 5.041 24.226 0.90 9.31 C ANISOU 179 CB AILE A 22 858 1301 1377 -119 -44 -224 C ATOM 180 CB BILE A 22 5.364 5.122 24.064 0.10 6.77 C ANISOU 180 CB BILE A 22 615 1063 893 -312 102 -162 C ATOM 181 CG1AILE A 22 4.233 5.315 25.294 0.90 10.83 C ANISOU 181 CG1AILE A 22 971 1496 1648 0 10 -288 C ATOM 182 CG1BILE A 22 4.244 5.402 25.071 0.10 6.28 C ANISOU 182 CG1BILE A 22 567 967 851 -425 -15 -174 C ATOM 183 CG2AILE A 22 4.645 4.672 22.891 0.90 9.84 C ANISOU 183 CG2AILE A 22 976 1413 1348 -102 -113 -46 C ATOM 184 CG2BILE A 22 4.813 4.808 22.675 0.10 3.87 C ANISOU 184 CG2BILE A 22 106 397 966 -197 11 -193 C ATOM 185 CD1AILE A 22 3.338 6.483 24.959 0.90 13.08 C ANISOU 185 CD1AILE A 22 1258 1498 2216 10 -30 -281 C ATOM 186 CD1BILE A 22 4.744 5.759 26.461 0.10 5.41 C ANISOU 186 CD1BILE A 22 792 340 923 -132 -63 -441 C ATOM 187 N ALA A 23 6.194 1.729 23.622 1.00 8.37 N ANISOU 187 N ALA A 23 794 1242 1145 -38 -101 -110 N ATOM 188 CA ALA A 23 5.760 0.340 23.509 1.00 8.32 C ANISOU 188 CA ALA A 23 804 1205 1151 -6 -87 -122 C ATOM 189 C ALA A 23 5.847 -0.416 24.837 1.00 8.88 C ANISOU 189 C ALA A 23 837 1349 1188 -1 -57 -112 C ATOM 190 O ALA A 23 5.131 -1.404 25.011 1.00 9.46 O ANISOU 190 O ALA A 23 1000 1382 1211 -66 -101 -36 O ATOM 191 CB ALA A 23 6.573 -0.394 22.457 1.00 8.72 C ANISOU 191 CB ALA A 23 761 1300 1252 42 -104 -203 C ATOM 192 N LYS A 24 6.749 0.024 25.725 1.00 9.79 N ANISOU 192 N LYS A 24 895 1617 1208 -49 -85 -79 N ATOM 193 CA LYS A 24 6.930 -0.575 27.047 1.00 10.44 C ANISOU 193 CA LYS A 24 961 1724 1280 44 -212 -19 C ATOM 194 C LYS A 24 6.318 0.307 28.152 1.00 11.00 C ANISOU 194 C LYS A 24 1010 1957 1212 -91 -198 -147 C ATOM 195 O LYS A 24 6.692 0.215 29.315 1.00 13.26 O ANISOU 195 O LYS A 24 1157 2611 1270 14 -277 -200 O ATOM 196 CB LYS A 24 8.411 -0.847 27.336 1.00 12.78 C ANISOU 196 CB LYS A 24 1185 2164 1506 349 -288 -15 C ATOM 197 CG LYS A 24 9.032 -1.868 26.394 1.00 15.08 C ANISOU 197 CG LYS A 24 1350 2548 1833 636 -309 -51 C ATOM 198 CD LYS A 24 10.499 -2.086 26.718 1.00 18.80 C ANISOU 198 CD LYS A 24 1451 3288 2404 828 -314 3 C ATOM 199 CE LYS A 24 11.132 -3.114 25.796 1.00 24.02 C ANISOU 199 CE LYS A 24 2255 3911 2961 1199 -235 -118 C ATOM 200 NZ LYS A 24 10.785 -4.500 26.197 1.00 36.60 N ANISOU 200 NZ LYS A 24 5871 3942 4096 284 929 -901 N ATOM 201 N GLY A 25 5.339 1.127 27.773 1.00 10.50 N ANISOU 201 N GLY A 25 1022 1704 1263 -112 -22 -243 N ATOM 202 CA GLY A 25 4.721 2.084 28.672 1.00 11.52 C ANISOU 202 CA GLY A 25 984 2058 1334 -167 -6 -389 C ATOM 203 C GLY A 25 3.739 1.501 29.663 1.00 10.65 C ANISOU 203 C GLY A 25 898 2001 1147 -59 -158 -246 C ATOM 204 O GLY A 25 3.565 0.277 29.788 1.00 11.25 O ANISOU 204 O GLY A 25 1028 2019 1225 -2 -168 -134 O ATOM 205 N GLU A 26 3.090 2.409 30.383 1.00 10.73 N ANISOU 205 N GLU A 26 928 2148 1001 -42 -220 -343 N ATOM 206 CA GLU A 26 2.237 2.065 31.512 1.00 11.66 C ANISOU 206 CA GLU A 26 1021 2410 999 -107 -274 -336 C ATOM 207 C GLU A 26 0.780 1.777 31.126 1.00 9.91 C ANISOU 207 C GLU A 26 1009 1834 924 -120 -169 -229 C ATOM 208 O GLU A 26 0.015 1.287 31.962 1.00 10.95 O ANISOU 208 O GLU A 26 1226 2091 845 -171 -126 -75 O ATOM 209 CB GLU A 26 2.263 3.179 32.546 1.00 15.01 C ANISOU 209 CB GLU A 26 1257 3085 1360 -377 -327 -751 C ATOM 210 CG GLU A 26 3.623 3.376 33.172 1.00 19.28 C ANISOU 210 CG GLU A 26 1547 3971 1809 -493 -672 -618 C ATOM 211 CD GLU A 26 4.156 2.108 33.816 1.00 24.72 C ANISOU 211 CD GLU A 26 2258 4875 2258 -83 -1097 -267 C ATOM 212 OE1 GLU A 26 3.439 1.503 34.643 1.00 27.73 O ANISOU 212 OE1 GLU A 26 3908 4328 2300 3 -395 -92 O ATOM 213 OE2 GLU A 26 5.289 1.713 33.491 1.00 33.98 O ANISOU 213 OE2 GLU A 26 2907 6909 3092 1370 -796 362 O ATOM 214 N ARG A 27 0.387 2.093 29.899 1.00 8.40 N ANISOU 214 N ARG A 27 980 1356 855 -118 -167 -248 N ATOM 215 CA ARG A 27 -1.011 1.876 29.503 1.00 8.44 C ANISOU 215 CA ARG A 27 927 1349 931 50 -200 -326 C ATOM 216 C ARG A 27 -1.094 1.436 28.045 1.00 7.24 C ANISOU 216 C ARG A 27 782 1128 842 -65 -123 -136 C ATOM 217 O ARG A 27 -1.828 2.016 27.233 1.00 7.82 O ANISOU 217 O ARG A 27 901 1187 882 30 -149 -115 O ATOM 218 CB ARG A 27 -1.934 3.064 29.825 1.00 10.87 C ANISOU 218 CB ARG A 27 1448 1540 1143 313 -180 -378 C ATOM 219 CG ARG A 27 -1.558 4.401 29.220 1.00 12.52 C ANISOU 219 CG ARG A 27 1548 1656 1554 74 -122 -319 C ATOM 220 CD ARG A 27 -2.596 5.517 29.477 1.00 14.52 C ANISOU 220 CD ARG A 27 2073 1885 1558 561 -104 -76 C ATOM 221 NE ARG A 27 -3.738 5.475 28.558 1.00 12.20 N ANISOU 221 NE ARG A 27 1796 1382 1457 145 120 -94 N ATOM 222 CZ ARG A 27 -4.682 6.409 28.503 1.00 11.17 C ANISOU 222 CZ ARG A 27 1581 1353 1310 109 168 -48 C ATOM 223 NH1 ARG A 27 -4.671 7.490 29.293 1.00 13.18 N ANISOU 223 NH1 ARG A 27 1783 1762 1462 113 228 -617 N ATOM 224 NH2 ARG A 27 -5.655 6.243 27.630 1.00 12.32 N ANISOU 224 NH2 ARG A 27 1660 1540 1479 -153 166 -214 N ATOM 225 N GLN A 28 -0.377 0.359 27.738 1.00 6.82 N ANISOU 225 N GLN A 28 823 990 778 -76 -104 -126 N ATOM 226 CA GLN A 28 -0.346 -0.174 26.384 1.00 6.72 C ANISOU 226 CA GLN A 28 784 976 795 -86 -133 -157 C ATOM 227 C GLN A 28 -1.508 -1.150 26.119 1.00 6.33 C ANISOU 227 C GLN A 28 767 893 747 -1 -101 -55 C ATOM 228 O GLN A 28 -2.024 -1.821 27.027 1.00 7.43 O ANISOU 228 O GLN A 28 962 1158 701 -103 -150 -36 O ATOM 229 CB GLN A 28 1.003 -0.859 26.122 1.00 7.14 C ANISOU 229 CB GLN A 28 793 1010 910 11 -83 -93 C ATOM 230 CG GLN A 28 2.143 0.173 26.008 1.00 7.20 C ANISOU 230 CG GLN A 28 740 1034 963 11 -112 -117 C ATOM 231 CD GLN A 28 2.031 0.974 24.733 1.00 6.78 C ANISOU 231 CD GLN A 28 611 1035 929 -30 -116 -120 C ATOM 232 OE1 GLN A 28 2.195 0.428 23.631 1.00 7.42 O ANISOU 232 OE1 GLN A 28 843 1047 929 -82 -8 -134 O ATOM 233 NE2 GLN A 28 1.699 2.260 24.860 1.00 7.38 N ANISOU 233 NE2 GLN A 28 691 1094 1018 -38 -76 -150 N ATOM 234 N SER A 29 -1.872 -1.229 24.851 1.00 6.06 N ANISOU 234 N SER A 29 752 842 710 -15 -132 -88 N ATOM 235 CA SER A 29 -2.937 -2.099 24.371 1.00 5.94 C ANISOU 235 CA SER A 29 741 789 726 0 -47 -65 C ATOM 236 C SER A 29 -2.397 -2.974 23.226 1.00 5.94 C ANISOU 236 C SER A 29 732 833 693 -31 -87 -29 C ATOM 237 O SER A 29 -1.453 -2.603 22.545 1.00 6.85 O ANISOU 237 O SER A 29 861 951 790 -24 -39 -60 O ATOM 238 CB SER A 29 -4.101 -1.241 23.840 1.00 5.91 C ANISOU 238 CB SER A 29 729 801 717 -3 -40 -50 C ATOM 239 OG SER A 29 -4.692 -0.514 24.918 1.00 6.53 O ANISOU 239 OG SER A 29 817 839 826 43 16 -121 O ATOM 240 N PRO A 30 -3.054 -4.107 22.975 1.00 5.95 N ANISOU 240 N PRO A 30 772 786 705 12 -72 -34 N ATOM 241 CA PRO A 30 -4.213 -4.674 23.688 1.00 5.77 C ANISOU 241 CA PRO A 30 747 756 690 -37 -27 29 C ATOM 242 C PRO A 30 -3.782 -5.321 24.989 1.00 6.19 C ANISOU 242 C PRO A 30 760 857 736 11 -20 -28 C ATOM 243 O PRO A 30 -2.605 -5.344 25.353 1.00 6.93 O ANISOU 243 O PRO A 30 869 1026 740 63 -94 17 O ATOM 244 CB PRO A 30 -4.722 -5.716 22.701 1.00 6.23 C ANISOU 244 CB PRO A 30 774 856 738 24 -6 -80 C ATOM 245 CG PRO A 30 -3.437 -6.273 22.106 1.00 6.22 C ANISOU 245 CG PRO A 30 790 847 725 26 -65 -88 C ATOM 246 CD PRO A 30 -2.559 -5.036 21.931 1.00 6.35 C ANISOU 246 CD PRO A 30 818 865 728 18 -27 -81 C ATOM 247 N VAL A 31 -4.774 -5.862 25.709 1.00 6.28 N ANISOU 247 N VAL A 31 859 856 672 65 3 53 N ATOM 248 CA VAL A 31 -4.586 -6.607 26.949 1.00 6.72 C ANISOU 248 CA VAL A 31 933 906 716 84 -13 81 C ATOM 249 C VAL A 31 -5.468 -7.849 26.898 1.00 6.55 C ANISOU 249 C VAL A 31 901 905 681 99 -28 125 C ATOM 250 O VAL A 31 -6.436 -7.926 26.132 1.00 7.11 O ANISOU 250 O VAL A 31 900 978 821 15 -58 175 O ATOM 251 CB VAL A 31 -4.926 -5.767 28.203 1.00 7.21 C ANISOU 251 CB VAL A 31 949 955 835 36 -26 11 C ATOM 252 CG1 VAL A 31 -4.009 -4.547 28.289 1.00 8.10 C ANISOU 252 CG1 VAL A 31 1090 1050 937 -71 33 -99 C ATOM 253 CG2 VAL A 31 -6.411 -5.361 28.234 1.00 7.60 C ANISOU 253 CG2 VAL A 31 935 1010 942 125 103 -6 C ATOM 254 N ASP A 32 -5.128 -8.817 27.754 1.00 6.92 N ANISOU 254 N ASP A 32 936 950 744 63 -3 102 N ATOM 255 CA ASP A 32 -6.035 -9.906 28.059 1.00 7.02 C ANISOU 255 CA ASP A 32 947 935 784 78 -24 105 C ATOM 256 C ASP A 32 -7.093 -9.394 29.053 1.00 7.24 C ANISOU 256 C ASP A 32 1006 1022 722 48 -24 92 C ATOM 257 O ASP A 32 -6.782 -8.723 30.039 1.00 9.03 O ANISOU 257 O ASP A 32 1138 1415 879 -12 -17 -158 O ATOM 258 CB ASP A 32 -5.283 -11.085 28.688 1.00 7.93 C ANISOU 258 CB ASP A 32 1120 976 915 92 -45 225 C ATOM 259 CG ASP A 32 -6.208 -12.247 28.986 1.00 8.46 C ANISOU 259 CG ASP A 32 1269 1036 912 94 -41 268 C ATOM 260 OD1 ASP A 32 -6.885 -12.722 28.051 1.00 8.54 O ANISOU 260 OD1 ASP A 32 1199 1093 953 77 -64 217 O ATOM 261 OD2 ASP A 32 -6.259 -12.666 30.167 1.00 10.97 O ANISOU 261 OD2 ASP A 32 1857 1373 940 -220 -74 311 O ATOM 262 N ILE A 33 -8.340 -9.718 28.750 1.00 7.35 N ANISOU 262 N ILE A 33 1007 1017 768 97 14 93 N ATOM 263 CA ILE A 33 -9.482 -9.397 29.611 1.00 7.48 C ANISOU 263 CA ILE A 33 1019 1038 784 123 49 89 C ATOM 264 C ILE A 33 -9.781 -10.638 30.443 1.00 8.07 C ANISOU 264 C ILE A 33 1155 1077 834 149 93 96 C ATOM 265 O ILE A 33 -10.333 -11.614 29.944 1.00 8.61 O ANISOU 265 O ILE A 33 1247 1105 919 27 92 155 O ATOM 266 CB ILE A 33 -10.680 -8.959 28.780 1.00 8.08 C ANISOU 266 CB ILE A 33 997 1121 950 163 53 121 C ATOM 267 CG1 ILE A 33 -10.319 -7.742 27.920 1.00 8.73 C ANISOU 267 CG1 ILE A 33 1039 1181 1098 57 -137 287 C ATOM 268 CG2 ILE A 33 -11.878 -8.677 29.692 1.00 9.97 C ANISOU 268 CG2 ILE A 33 1127 1555 1104 297 181 89 C ATOM 269 CD1 ILE A 33 -11.358 -7.421 26.837 1.00 10.18 C ANISOU 269 CD1 ILE A 33 973 1576 1319 99 -176 367 C ATOM 270 N AASP A 34 -9.405 -10.582 31.712 0.71 9.00 N ANISOU 270 N AASP A 34 1363 1201 854 196 46 211 N ATOM 271 N BASP A 34 -9.394 -10.570 31.714 0.29 8.44 N ANISOU 271 N BASP A 34 1256 1194 757 236 169 191 N ATOM 272 CA AASP A 34 -9.690 -11.670 32.634 0.71 10.19 C ANISOU 272 CA AASP A 34 1514 1356 1000 289 104 309 C ATOM 273 CA BASP A 34 -9.707 -11.594 32.703 0.29 9.38 C ANISOU 273 CA BASP A 34 1388 1354 822 501 337 375 C ATOM 274 C AASP A 34 -11.096 -11.403 33.199 0.71 10.72 C ANISOU 274 C AASP A 34 1628 1477 968 415 245 342 C ATOM 275 C BASP A 34 -11.137 -11.336 33.163 0.29 9.49 C ANISOU 275 C BASP A 34 1518 1312 775 580 383 340 C ATOM 276 O AASP A 34 -11.306 -10.483 33.988 0.71 12.35 O ANISOU 276 O AASP A 34 1858 1741 1092 382 258 140 O ATOM 277 O BASP A 34 -11.403 -10.368 33.872 0.29 10.63 O ANISOU 277 O BASP A 34 1936 1332 770 621 612 318 O ATOM 278 CB AASP A 34 -8.623 -11.722 33.715 0.71 12.06 C ANISOU 278 CB AASP A 34 1829 1677 1077 618 65 291 C ATOM 279 CB BASP A 34 -8.733 -11.485 33.877 0.29 9.72 C ANISOU 279 CB BASP A 34 1463 1397 835 599 421 457 C ATOM 280 CG AASP A 34 -8.751 -12.942 34.578 0.71 13.01 C ANISOU 280 CG AASP A 34 1988 1809 1146 589 113 331 C ATOM 281 CG BASP A 34 -8.964 -12.549 34.943 0.29 10.62 C ANISOU 281 CG BASP A 34 1574 1531 930 531 329 597 C ATOM 282 OD1AASP A 34 -9.362 -12.831 35.644 0.71 15.53 O ANISOU 282 OD1AASP A 34 2598 2050 1254 327 606 270 O ATOM 283 OD1BASP A 34 -10.102 -13.039 35.072 0.29 10.35 O ANISOU 283 OD1BASP A 34 1804 1337 792 270 70 571 O ATOM 284 OD2AASP A 34 -8.284 -14.017 34.188 0.71 14.04 O ANISOU 284 OD2AASP A 34 2160 1669 1505 613 257 397 O ATOM 285 OD2BASP A 34 -7.990 -12.903 35.644 0.29 12.48 O ANISOU 285 OD2BASP A 34 1816 1727 1198 -35 6 954 O ATOM 286 N THR A 35 -12.061 -12.179 32.713 1.00 10.54 N ANISOU 286 N THR A 35 1505 1545 955 401 287 436 N ATOM 287 CA THR A 35 -13.476 -11.905 32.951 1.00 11.70 C ANISOU 287 CA THR A 35 1515 1728 1203 513 313 432 C ATOM 288 C THR A 35 -13.850 -12.006 34.405 1.00 12.00 C ANISOU 288 C THR A 35 1798 1563 1199 574 479 460 C ATOM 289 O THR A 35 -14.759 -11.316 34.852 1.00 14.40 O ANISOU 289 O THR A 35 2022 2014 1435 812 606 437 O ATOM 290 CB THR A 35 -14.388 -12.818 32.114 1.00 13.02 C ANISOU 290 CB THR A 35 1533 2001 1413 320 265 422 C ATOM 291 OG1 THR A 35 -14.257 -14.167 32.568 1.00 12.85 O ANISOU 291 OG1 THR A 35 1556 1946 1379 105 277 409 O ATOM 292 CG2 THR A 35 -14.056 -12.714 30.619 1.00 15.37 C ANISOU 292 CG2 THR A 35 2018 2300 1520 382 240 473 C ATOM 293 N HIS A 36 -13.147 -12.851 35.157 1.00 12.44 N ANISOU 293 N HIS A 36 2156 1465 1105 592 582 478 N ATOM 294 CA HIS A 36 -13.474 -13.022 36.559 1.00 14.75 C ANISOU 294 CA HIS A 36 2696 1716 1193 391 582 568 C ATOM 295 C HIS A 36 -12.954 -11.865 37.415 1.00 16.04 C ANISOU 295 C HIS A 36 3096 1929 1071 432 720 404 C ATOM 296 O HIS A 36 -13.562 -11.532 38.421 1.00 18.53 O ANISOU 296 O HIS A 36 2735 3237 1066 877 470 125 O ATOM 297 CB HIS A 36 -13.044 -14.405 37.024 1.00 17.52 C ANISOU 297 CB HIS A 36 3298 1816 1543 470 174 667 C ATOM 298 CG HIS A 36 -13.971 -15.485 36.555 1.00 21.30 C ANISOU 298 CG HIS A 36 4692 1676 1723 341 -688 624 C ATOM 299 ND1 HIS A 36 -13.644 -16.392 35.566 1.00 25.80 N ANISOU 299 ND1 HIS A 36 5949 1980 1873 1002 -1282 483 N ATOM 300 CD2 HIS A 36 -15.252 -15.755 36.905 1.00 24.44 C ANISOU 300 CD2 HIS A 36 5069 1926 2293 -711 -880 544 C ATOM 301 CE1 HIS A 36 -14.673 -17.195 35.354 1.00 29.47 C ANISOU 301 CE1 HIS A 36 6749 1954 2497 700 -1710 338 C ATOM 302 NE2 HIS A 36 -15.660 -16.830 36.154 1.00 29.71 N ANISOU 302 NE2 HIS A 36 6378 2186 2726 -597 -1373 208 N ATOM 303 N THR A 37 -11.886 -11.205 36.962 1.00 14.55 N ANISOU 303 N THR A 37 2663 1531 1334 673 355 321 N ATOM 304 CA THR A 37 -11.278 -10.089 37.687 1.00 17.20 C ANISOU 304 CA THR A 37 3116 1656 1764 858 -86 237 C ATOM 305 C THR A 37 -11.871 -8.725 37.303 1.00 15.37 C ANISOU 305 C THR A 37 3011 1638 1193 979 148 121 C ATOM 306 O THR A 37 -11.793 -7.776 38.068 1.00 16.19 O ANISOU 306 O THR A 37 3017 1781 1353 819 -245 -74 O ATOM 307 CB THR A 37 -9.746 -10.061 37.479 1.00 21.72 C ANISOU 307 CB THR A 37 3070 2060 3123 847 -1126 165 C ATOM 308 OG1 THR A 37 -9.172 -11.268 37.991 1.00 27.98 O ANISOU 308 OG1 THR A 37 3924 2358 4349 1405 -686 640 O ATOM 309 CG2 THR A 37 -9.115 -8.875 38.194 1.00 24.32 C ANISOU 309 CG2 THR A 37 3492 2640 3108 626 -597 -357 C ATOM 310 N ALA A 38 -12.464 -8.625 36.120 1.00 12.49 N ANISOU 310 N ALA A 38 2162 1556 1026 638 235 248 N ATOM 311 CA ALA A 38 -13.110 -7.371 35.724 1.00 12.86 C ANISOU 311 CA ALA A 38 2135 1617 1135 684 413 262 C ATOM 312 C ALA A 38 -14.243 -7.109 36.700 1.00 15.21 C ANISOU 312 C ALA A 38 2331 1905 1541 744 692 387 C ATOM 313 O ALA A 38 -14.927 -8.033 37.118 1.00 20.06 O ANISOU 313 O ALA A 38 3044 2288 2290 494 1380 519 O ATOM 314 CB ALA A 38 -13.631 -7.465 34.312 1.00 12.11 C ANISOU 314 CB ALA A 38 1761 1604 1237 486 127 229 C ATOM 315 N LYS A 39 -14.431 -5.862 37.077 1.00 15.34 N ANISOU 315 N LYS A 39 2342 2164 1323 1155 264 145 N ATOM 316 CA LYS A 39 -15.490 -5.579 38.043 1.00 17.76 C ANISOU 316 CA LYS A 39 2500 2948 1299 1530 154 68 C ATOM 317 C LYS A 39 -16.626 -4.801 37.431 1.00 12.85 C ANISOU 317 C LYS A 39 1904 2106 871 706 109 98 C ATOM 318 O LYS A 39 -16.422 -3.819 36.702 1.00 10.94 O ANISOU 318 O LYS A 39 1316 2028 812 391 -53 95 O ATOM 319 CB LYS A 39 -14.954 -4.821 39.234 1.00 21.97 C ANISOU 319 CB LYS A 39 2407 4157 1785 1871 -396 -469 C ATOM 320 CG LYS A 39 -15.923 -4.712 40.380 1.00 22.92 C ANISOU 320 CG LYS A 39 2666 3986 2056 1600 -349 -589 C ATOM 321 CD LYS A 39 -15.281 -3.877 41.442 1.00 24.36 C ANISOU 321 CD LYS A 39 3233 3753 2269 2032 -656 -648 C ATOM 322 CE LYS A 39 -16.280 -3.339 42.418 1.00 26.92 C ANISOU 322 CE LYS A 39 3103 4237 2890 1789 -653 -697 C ATOM 323 NZ LYS A 39 -16.754 -4.400 43.314 1.00 34.43 N ANISOU 323 NZ LYS A 39 3026 5775 4281 1907 -216 610 N ATOM 324 N TYR A 40 -17.837 -5.249 37.726 1.00 14.23 N ANISOU 324 N TYR A 40 2132 2201 1075 333 545 196 N ATOM 325 CA TYR A 40 -19.017 -4.526 37.333 1.00 13.89 C ANISOU 325 CA TYR A 40 1754 2302 1221 -118 439 70 C ATOM 326 C TYR A 40 -18.994 -3.150 37.973 1.00 13.00 C ANISOU 326 C TYR A 40 1607 2333 1002 371 222 -19 C ATOM 327 O TYR A 40 -18.768 -3.011 39.182 1.00 15.15 O ANISOU 327 O TYR A 40 1900 3019 838 854 112 -21 O ATOM 328 CB TYR A 40 -20.264 -5.286 37.781 1.00 19.61 C ANISOU 328 CB TYR A 40 2152 3722 1577 -958 558 70 C ATOM 329 CG TYR A 40 -21.537 -4.514 37.619 1.00 23.83 C ANISOU 329 CG TYR A 40 1904 5541 1610 -682 591 -11 C ATOM 330 CD1 TYR A 40 -21.944 -4.066 36.373 1.00 22.65 C ANISOU 330 CD1 TYR A 40 1443 5386 1776 -869 464 -26 C ATOM 331 CD2 TYR A 40 -22.357 -4.260 38.705 1.00 32.92 C ANISOU 331 CD2 TYR A 40 2959 7578 1971 383 727 -426 C ATOM 332 CE1 TYR A 40 -23.112 -3.363 36.212 1.00 29.42 C ANISOU 332 CE1 TYR A 40 1316 7601 2261 -259 345 -2 C ATOM 333 CE2 TYR A 40 -23.533 -3.562 38.558 1.00 37.96 C ANISOU 333 CE2 TYR A 40 3181 8780 2462 981 863 -600 C ATOM 334 CZ TYR A 40 -23.909 -3.116 37.311 1.00 38.71 C ANISOU 334 CZ TYR A 40 2435 9551 2722 1201 615 -401 C ATOM 335 OH TYR A 40 -25.085 -2.420 37.177 1.00 52.43 O ANISOU 335 OH TYR A 40 3050 12559 4311 2691 901 365 O ATOM 336 N ASP A 41 -19.251 -2.137 37.156 1.00 12.74 N ANISOU 336 N ASP A 41 1501 2210 1131 459 154 -69 N ATOM 337 CA ASP A 41 -19.276 -0.764 37.617 1.00 15.15 C ANISOU 337 CA ASP A 41 1956 2371 1430 837 -103 -189 C ATOM 338 C ASP A 41 -20.666 -0.199 37.378 1.00 17.86 C ANISOU 338 C ASP A 41 2237 3365 1182 1389 218 178 C ATOM 339 O ASP A 41 -20.998 0.174 36.259 1.00 20.15 O ANISOU 339 O ASP A 41 2076 4422 1157 1630 300 471 O ATOM 340 CB ASP A 41 -18.224 0.060 36.874 1.00 17.64 C ANISOU 340 CB ASP A 41 2372 2269 2061 42 -883 -424 C ATOM 341 CG ASP A 41 -18.105 1.471 37.410 1.00 24.88 C ANISOU 341 CG ASP A 41 4246 2569 2640 138 -1723 -490 C ATOM 342 OD1 ASP A 41 -18.940 1.867 38.247 1.00 34.38 O ANISOU 342 OD1 ASP A 41 6616 4243 2204 1691 -1059 -1406 O ATOM 343 OD2 ASP A 41 -17.172 2.181 36.988 1.00 31.70 O ANISOU 343 OD2 ASP A 41 4758 2864 4423 -1273 -2749 117 O ATOM 344 N PRO A 42 -21.503 -0.158 38.422 1.00 23.71 N ANISOU 344 N PRO A 42 2727 4731 1549 2121 586 652 N ATOM 345 CA PRO A 42 -22.885 0.289 38.187 1.00 27.99 C ANISOU 345 CA PRO A 42 2917 5413 2305 2398 834 1020 C ATOM 346 C PRO A 42 -22.971 1.765 37.804 1.00 29.64 C ANISOU 346 C PRO A 42 3695 5238 2328 2892 818 670 C ATOM 347 O PRO A 42 -24.040 2.218 37.397 1.00 35.06 O ANISOU 347 O PRO A 42 4072 6381 2867 3555 969 1153 O ATOM 348 CB PRO A 42 -23.569 0.028 39.537 1.00 33.67 C ANISOU 348 CB PRO A 42 3573 6391 2830 2901 1183 931 C ATOM 349 CG PRO A 42 -22.454 0.086 40.524 1.00 34.50 C ANISOU 349 CG PRO A 42 4155 6302 2651 2824 1181 23 C ATOM 350 CD PRO A 42 -21.302 -0.584 39.817 1.00 26.59 C ANISOU 350 CD PRO A 42 3477 4707 1920 2421 848 408 C ATOM 351 N SER A 43 -21.879 2.512 37.946 1.00 30.13 N ANISOU 351 N SER A 43 5023 4419 2007 2619 358 -105 N ATOM 352 CA SER A 43 -21.880 3.927 37.571 1.00 35.79 C ANISOU 352 CA SER A 43 7013 4346 2238 2717 333 -270 C ATOM 353 C SER A 43 -21.622 4.161 36.070 1.00 31.77 C ANISOU 353 C SER A 43 5414 4762 1896 3469 426 277 C ATOM 354 O SER A 43 -21.750 5.281 35.576 1.00 32.33 O ANISOU 354 O SER A 43 5478 4786 2019 3281 517 278 O ATOM 355 CB SER A 43 -20.858 4.706 38.398 1.00 40.37 C ANISOU 355 CB SER A 43 7700 4507 3132 2352 -575 -329 C ATOM 356 OG SER A 43 -19.538 4.425 37.972 1.00 42.90 O ANISOU 356 OG SER A 43 8217 5172 2913 1446 -299 -1081 O ATOM 357 N LEU A 44 -21.240 3.118 35.335 1.00 27.47 N ANISOU 357 N LEU A 44 3933 4682 1825 2452 398 154 N ATOM 358 CA LEU A 44 -21.112 3.243 33.887 1.00 24.81 C ANISOU 358 CA LEU A 44 2278 5329 1820 1283 48 273 C ATOM 359 C LEU A 44 -22.490 3.471 33.284 1.00 31.37 C ANISOU 359 C LEU A 44 1828 7551 2540 1239 314 1885 C ATOM 360 O LEU A 44 -23.486 3.028 33.817 1.00 36.74 O ANISOU 360 O LEU A 44 1924 8957 3078 1282 623 2950 O ATOM 361 CB LEU A 44 -20.492 1.990 33.285 1.00 20.77 C ANISOU 361 CB LEU A 44 1693 4503 1696 206 -115 -285 C ATOM 362 CG LEU A 44 -18.997 1.798 33.524 1.00 14.60 C ANISOU 362 CG LEU A 44 1575 2439 1532 -299 -244 -66 C ATOM 363 CD1 LEU A 44 -18.597 0.388 33.136 1.00 16.06 C ANISOU 363 CD1 LEU A 44 2248 2159 1694 -596 61 -308 C ATOM 364 CD2 LEU A 44 -18.161 2.826 32.777 1.00 15.32 C ANISOU 364 CD2 LEU A 44 1974 2153 1693 -354 -401 277 C ATOM 365 N LYS A 45 -22.555 4.168 32.164 1.00 31.98 N ANISOU 365 N LYS A 45 1841 7481 2829 663 -70 1896 N ATOM 366 CA LYS A 45 -23.846 4.428 31.532 1.00 33.65 C ANISOU 366 CA LYS A 45 1946 7534 3303 237 -352 1980 C ATOM 367 C LYS A 45 -23.966 3.615 30.280 1.00 32.47 C ANISOU 367 C LYS A 45 1773 7500 3065 -589 -250 2292 C ATOM 368 O LYS A 45 -22.965 3.167 29.772 1.00 28.29 O ANISOU 368 O LYS A 45 1565 6392 2791 -1084 -347 2346 O ATOM 369 CB LYS A 45 -23.948 5.887 31.163 1.00 36.26 C ANISOU 369 CB LYS A 45 2063 7445 4270 1055 -48 1734 C ATOM 370 CG LYS A 45 -23.894 6.786 32.347 1.00 43.19 C ANISOU 370 CG LYS A 45 3048 8159 5205 687 -1034 723 C ATOM 371 CD LYS A 45 -23.746 8.210 31.907 1.00 48.71 C ANISOU 371 CD LYS A 45 4443 8093 5971 303 -1392 175 C ATOM 372 CE LYS A 45 -23.417 9.089 33.084 1.00 49.54 C ANISOU 372 CE LYS A 45 3841 8593 6390 406 -1466 -207 C ATOM 373 NZ LYS A 45 -23.472 10.518 32.700 1.00 53.57 N ANISOU 373 NZ LYS A 45 4962 8500 6891 -198 -1238 -438 N ATOM 374 N PRO A 46 -25.195 3.436 29.760 1.00 34.18 N ANISOU 374 N PRO A 46 1626 7697 3664 -1021 -97 2018 N ATOM 375 CA PRO A 46 -25.252 2.694 28.502 1.00 29.26 C ANISOU 375 CA PRO A 46 1718 5779 3621 -759 -469 2261 C ATOM 376 C PRO A 46 -24.450 3.408 27.429 1.00 25.09 C ANISOU 376 C PRO A 46 1239 5302 2993 -1068 -685 1794 C ATOM 377 O PRO A 46 -24.366 4.634 27.441 1.00 23.64 O ANISOU 377 O PRO A 46 1113 5331 2540 -451 -296 1686 O ATOM 378 CB PRO A 46 -26.750 2.687 28.159 1.00 29.56 C ANISOU 378 CB PRO A 46 1831 5188 4213 -828 -521 1762 C ATOM 379 CG PRO A 46 -27.315 3.824 28.949 1.00 38.31 C ANISOU 379 CG PRO A 46 2357 7880 4319 -114 -548 1023 C ATOM 380 CD PRO A 46 -26.539 3.791 30.233 1.00 39.24 C ANISOU 380 CD PRO A 46 2115 8471 4322 -477 -393 1829 C ATOM 381 N LEU A 47 -23.866 2.630 26.530 1.00 24.11 N ANISOU 381 N LEU A 47 1677 4171 3313 -1173 -773 1657 N ATOM 382 CA LEU A 47 -23.230 3.205 25.367 1.00 18.77 C ANISOU 382 CA LEU A 47 1304 2362 3465 -615 -720 931 C ATOM 383 C LEU A 47 -24.294 3.841 24.532 1.00 15.97 C ANISOU 383 C LEU A 47 1139 1999 2931 -576 -614 824 C ATOM 384 O LEU A 47 -25.389 3.312 24.424 1.00 18.45 O ANISOU 384 O LEU A 47 1111 2487 3411 -730 -729 1093 O ATOM 385 CB LEU A 47 -22.585 2.120 24.505 1.00 23.10 C ANISOU 385 CB LEU A 47 1824 2470 4484 -519 -412 -52 C ATOM 386 CG LEU A 47 -21.134 1.749 24.688 1.00 27.08 C ANISOU 386 CG LEU A 47 1633 3774 4883 -686 -227 -872 C ATOM 387 CD1 LEU A 47 -20.735 0.836 23.550 1.00 26.73 C ANISOU 387 CD1 LEU A 47 1929 3529 4700 -438 -1082 -1193 C ATOM 388 CD2 LEU A 47 -20.260 3.006 24.736 1.00 23.97 C ANISOU 388 CD2 LEU A 47 1541 3353 4214 -239 -1309 -904 C ATOM 389 N SER A 48 -23.950 4.945 23.897 1.00 11.80 N ANISOU 389 N SER A 48 919 1631 1934 -166 -177 238 N ATOM 390 CA SER A 48 -24.754 5.537 22.847 1.00 11.31 C ANISOU 390 CA SER A 48 969 1725 1602 38 -70 22 C ATOM 391 C SER A 48 -23.953 5.506 21.547 1.00 11.16 C ANISOU 391 C SER A 48 997 1660 1582 -201 15 -119 C ATOM 392 O SER A 48 -22.971 6.234 21.401 1.00 12.07 O ANISOU 392 O SER A 48 1179 1718 1687 -331 145 -237 O ATOM 393 CB SER A 48 -25.129 6.974 23.232 1.00 13.18 C ANISOU 393 CB SER A 48 1350 1861 1796 201 -15 16 C ATOM 394 OG SER A 48 -25.774 7.664 22.184 1.00 15.34 O ANISOU 394 OG SER A 48 1448 2207 2174 332 -32 350 O ATOM 395 N VAL A 49 -24.370 4.652 20.625 1.00 11.97 N ANISOU 395 N VAL A 49 1168 1827 1553 -451 97 -157 N ATOM 396 CA VAL A 49 -23.755 4.544 19.314 1.00 13.05 C ANISOU 396 CA VAL A 49 1451 1835 1674 -535 160 -247 C ATOM 397 C VAL A 49 -24.746 5.146 18.330 1.00 13.64 C ANISOU 397 C VAL A 49 1406 2216 1560 -689 12 -237 C ATOM 398 O VAL A 49 -25.820 4.602 18.130 1.00 17.26 O ANISOU 398 O VAL A 49 1610 3200 1748 -1161 -101 -211 O ATOM 399 CB VAL A 49 -23.480 3.071 18.955 1.00 16.33 C ANISOU 399 CB VAL A 49 2200 1822 2181 -644 557 -331 C ATOM 400 CG1 VAL A 49 -22.745 2.970 17.625 1.00 20.39 C ANISOU 400 CG1 VAL A 49 2815 2433 2500 -1088 1114 -981 C ATOM 401 CG2 VAL A 49 -22.689 2.381 20.062 1.00 17.01 C ANISOU 401 CG2 VAL A 49 1778 1953 2730 -327 149 -92 C ATOM 402 N SER A 50 -24.417 6.296 17.753 1.00 13.59 N ANISOU 402 N SER A 50 1352 2179 1633 -484 -62 -200 N ATOM 403 CA SER A 50 -25.324 7.026 16.872 1.00 14.94 C ANISOU 403 CA SER A 50 1364 2262 2053 -90 -143 -289 C ATOM 404 C SER A 50 -24.709 7.126 15.492 1.00 13.25 C ANISOU 404 C SER A 50 998 2147 1890 -96 -263 -100 C ATOM 405 O SER A 50 -23.980 8.066 15.190 1.00 13.90 O ANISOU 405 O SER A 50 1081 2142 2060 -74 -190 1 O ATOM 406 CB SER A 50 -25.628 8.421 17.427 1.00 23.66 C ANISOU 406 CB SER A 50 3118 3049 2823 669 440 -709 C ATOM 407 OG SER A 50 -26.282 8.338 18.681 1.00 35.83 O ANISOU 407 OG SER A 50 4665 5752 3197 1514 1036 -1056 O ATOM 408 N TYR A 51 -25.017 6.141 14.656 1.00 13.34 N ANISOU 408 N TYR A 51 1104 2093 1870 -43 -207 -125 N ATOM 409 CA TYR A 51 -24.413 6.014 13.338 1.00 13.05 C ANISOU 409 CA TYR A 51 1116 2009 1835 -11 -215 -23 C ATOM 410 C TYR A 51 -25.383 6.258 12.169 1.00 14.15 C ANISOU 410 C TYR A 51 1180 2204 1991 -77 -174 259 C ATOM 411 O TYR A 51 -25.005 6.088 11.011 1.00 15.06 O ANISOU 411 O TYR A 51 1437 2442 1843 11 -289 29 O ATOM 412 CB TYR A 51 -23.797 4.618 13.189 1.00 12.22 C ANISOU 412 CB TYR A 51 1104 1906 1633 -133 -318 -187 C ATOM 413 CG TYR A 51 -22.507 4.335 13.966 1.00 11.18 C ANISOU 413 CG TYR A 51 1069 1734 1445 -168 -215 -95 C ATOM 414 CD1 TYR A 51 -21.766 5.339 14.601 1.00 10.97 C ANISOU 414 CD1 TYR A 51 1069 1531 1568 -198 -276 -15 C ATOM 415 CD2 TYR A 51 -22.013 3.045 14.004 1.00 10.44 C ANISOU 415 CD2 TYR A 51 1004 1693 1269 -236 -93 -282 C ATOM 416 CE1 TYR A 51 -20.563 5.031 15.272 1.00 9.76 C ANISOU 416 CE1 TYR A 51 985 1356 1367 -131 -145 -62 C ATOM 417 CE2 TYR A 51 -20.836 2.727 14.649 1.00 9.61 C ANISOU 417 CE2 TYR A 51 1005 1465 1181 -279 -35 -197 C ATOM 418 CZ TYR A 51 -20.106 3.718 15.281 1.00 9.27 C ANISOU 418 CZ TYR A 51 900 1379 1243 -232 -80 -117 C ATOM 419 OH TYR A 51 -18.938 3.354 15.912 1.00 9.47 O ANISOU 419 OH TYR A 51 983 1303 1314 -165 -116 -123 O ATOM 420 N ASP A 52 -26.620 6.651 12.461 1.00 16.31 N ANISOU 420 N ASP A 52 985 2853 2357 -115 -298 557 N ATOM 421 CA ASP A 52 -27.621 6.854 11.415 1.00 19.17 C ANISOU 421 CA ASP A 52 1117 3267 2900 2 -264 819 C ATOM 422 C ASP A 52 -27.205 7.840 10.308 1.00 17.17 C ANISOU 422 C ASP A 52 1388 2604 2532 30 -384 404 C ATOM 423 O ASP A 52 -27.594 7.676 9.153 1.00 20.00 O ANISOU 423 O ASP A 52 2387 2821 2393 159 -632 384 O ATOM 424 CB ASP A 52 -28.955 7.277 12.038 1.00 27.72 C ANISOU 424 CB ASP A 52 1272 5089 4171 277 -142 1334 C ATOM 425 CG ASP A 52 -28.806 8.453 12.984 1.00 41.49 C ANISOU 425 CG ASP A 52 2981 6897 5885 1533 742 81 C ATOM 426 OD1 ASP A 52 -28.202 8.278 14.069 1.00 43.29 O ANISOU 426 OD1 ASP A 52 2571 9127 4750 1448 880 -683 O ATOM 427 OD2 ASP A 52 -29.295 9.552 12.642 1.00 65.40 O ANISOU 427 OD2 ASP A 52 8088 7719 9043 4243 -154 -1224 O ATOM 428 N GLN A 53 -26.410 8.850 10.650 1.00 16.33 N ANISOU 428 N GLN A 53 1154 2326 2724 269 -201 157 N ATOM 429 CA GLN A 53 -25.990 9.843 9.661 1.00 16.18 C ANISOU 429 CA GLN A 53 1372 1993 2782 310 -215 72 C ATOM 430 C GLN A 53 -24.552 9.646 9.163 1.00 14.53 C ANISOU 430 C GLN A 53 1374 1878 2268 274 -101 -148 C ATOM 431 O GLN A 53 -23.974 10.536 8.543 1.00 15.28 O ANISOU 431 O GLN A 53 1584 1859 2363 171 -72 -60 O ATOM 432 CB GLN A 53 -26.182 11.257 10.210 1.00 20.81 C ANISOU 432 CB GLN A 53 2021 2467 3419 927 333 86 C ATOM 433 CG GLN A 53 -27.644 11.630 10.421 1.00 29.27 C ANISOU 433 CG GLN A 53 2302 4575 4245 1535 328 673 C ATOM 434 CD GLN A 53 -28.424 11.656 9.122 1.00 38.11 C ANISOU 434 CD GLN A 53 2039 7276 5167 895 199 2209 C ATOM 435 OE1 GLN A 53 -29.447 10.984 8.981 1.00 43.97 O ANISOU 435 OE1 GLN A 53 2135 9676 4894 189 221 2514 O ATOM 436 NE2 GLN A 53 -27.934 12.426 8.156 1.00 48.72 N ANISOU 436 NE2 GLN A 53 3685 8141 6686 -125 -450 4580 N ATOM 437 N ALA A 54 -23.981 8.476 9.411 1.00 13.19 N ANISOU 437 N ALA A 54 1176 1749 2086 51 -168 -328 N ATOM 438 CA ALA A 54 -22.617 8.206 8.979 1.00 13.04 C ANISOU 438 CA ALA A 54 1163 1671 2123 46 -170 -458 C ATOM 439 C ALA A 54 -22.437 8.401 7.474 1.00 13.33 C ANISOU 439 C ALA A 54 1060 2054 1949 5 -211 -673 C ATOM 440 O ALA A 54 -23.294 8.018 6.671 1.00 17.12 O ANISOU 440 O ALA A 54 1188 3271 2047 -180 -238 -988 O ATOM 441 CB ALA A 54 -22.212 6.805 9.381 1.00 15.86 C ANISOU 441 CB ALA A 54 1582 1791 2652 197 75 -162 C ATOM 442 N THR A 55 -21.308 8.995 7.102 1.00 11.61 N ANISOU 442 N THR A 55 1074 1556 1782 243 -353 -224 N ATOM 443 CA THR A 55 -20.919 9.195 5.710 1.00 11.66 C ANISOU 443 CA THR A 55 1288 1338 1803 307 -520 151 C ATOM 444 C THR A 55 -19.569 8.555 5.473 1.00 9.14 C ANISOU 444 C THR A 55 1156 1011 1306 139 -351 222 C ATOM 445 O THR A 55 -18.547 9.160 5.753 1.00 9.53 O ANISOU 445 O THR A 55 1227 955 1439 -24 -319 110 O ATOM 446 CB THR A 55 -20.806 10.705 5.325 1.00 15.43 C ANISOU 446 CB THR A 55 1770 1412 2680 284 -610 306 C ATOM 447 OG1 THR A 55 -22.084 11.340 5.405 1.00 18.58 O ANISOU 447 OG1 THR A 55 1818 1600 3642 309 -769 376 O ATOM 448 CG2 THR A 55 -20.262 10.878 3.895 1.00 17.69 C ANISOU 448 CG2 THR A 55 2593 1694 2434 160 -679 609 C ATOM 449 N SER A 56 -19.582 7.335 4.969 1.00 8.89 N ANISOU 449 N SER A 56 1080 1095 1202 7 -311 212 N ATOM 450 CA SER A 56 -18.340 6.708 4.546 1.00 8.63 C ANISOU 450 CA SER A 56 1115 1001 1164 47 -349 151 C ATOM 451 C SER A 56 -17.878 7.357 3.247 1.00 9.08 C ANISOU 451 C SER A 56 1102 1111 1237 68 -324 289 C ATOM 452 O SER A 56 -18.685 7.834 2.467 1.00 10.22 O ANISOU 452 O SER A 56 1212 1316 1354 132 -338 393 O ATOM 453 CB SER A 56 -18.476 5.198 4.384 1.00 9.31 C ANISOU 453 CB SER A 56 1324 1046 1168 -70 -471 181 C ATOM 454 OG SER A 56 -19.326 4.859 3.300 1.00 10.11 O ANISOU 454 OG SER A 56 1445 1138 1257 -227 -553 252 O ATOM 455 N LEU A 57 -16.570 7.367 3.027 1.00 8.75 N ANISOU 455 N LEU A 57 1141 1023 1159 136 -218 186 N ATOM 456 CA LEU A 57 -16.009 8.000 1.843 1.00 9.52 C ANISOU 456 CA LEU A 57 1316 999 1300 152 -88 209 C ATOM 457 C LEU A 57 -15.152 7.072 0.984 1.00 8.64 C ANISOU 457 C LEU A 57 1189 932 1160 82 -196 197 C ATOM 458 O LEU A 57 -15.242 7.104 -0.242 1.00 9.72 O ANISOU 458 O LEU A 57 1295 1243 1156 241 -279 214 O ATOM 459 CB LEU A 57 -15.198 9.234 2.232 1.00 11.43 C ANISOU 459 CB LEU A 57 1678 1037 1627 -54 67 50 C ATOM 460 CG LEU A 57 -16.019 10.402 2.795 1.00 14.16 C ANISOU 460 CG LEU A 57 1962 1258 2161 120 -125 -19 C ATOM 461 CD1 LEU A 57 -15.070 11.482 3.291 1.00 17.62 C ANISOU 461 CD1 LEU A 57 2610 1546 2539 -442 455 -531 C ATOM 462 CD2 LEU A 57 -17.005 10.966 1.763 1.00 17.88 C ANISOU 462 CD2 LEU A 57 2368 1897 2530 504 -154 592 C ATOM 463 N ARG A 58 -14.280 6.290 1.613 1.00 8.25 N ANISOU 463 N ARG A 58 1172 893 1067 108 -160 152 N ATOM 464 CA ARG A 58 -13.195 5.657 0.882 1.00 8.16 C ANISOU 464 CA ARG A 58 1126 944 1031 55 -146 194 C ATOM 465 C ARG A 58 -12.690 4.471 1.694 1.00 7.36 C ANISOU 465 C ARG A 58 1101 935 759 36 -170 120 C ATOM 466 O ARG A 58 -12.851 4.436 2.912 1.00 8.06 O ANISOU 466 O ARG A 58 1269 953 838 173 -119 111 O ATOM 467 CB ARG A 58 -12.066 6.681 0.705 1.00 10.13 C ANISOU 467 CB ARG A 58 1339 1101 1410 10 0 332 C ATOM 468 CG ARG A 58 -10.994 6.305 -0.281 1.00 11.87 C ANISOU 468 CG ARG A 58 1396 1477 1638 -167 48 410 C ATOM 469 CD ARG A 58 -9.929 7.406 -0.410 1.00 13.37 C ANISOU 469 CD ARG A 58 1447 1899 1735 -295 -45 593 C ATOM 470 NE ARG A 58 -9.070 7.430 0.770 1.00 12.67 N ANISOU 470 NE ARG A 58 1413 1701 1700 -220 38 330 N ATOM 471 CZ ARG A 58 -7.765 7.664 0.761 1.00 11.97 C ANISOU 471 CZ ARG A 58 1430 1413 1705 -394 158 297 C ATOM 472 NH1 ARG A 58 -7.132 7.915 -0.372 1.00 13.50 N ANISOU 472 NH1 ARG A 58 1717 1592 1819 -544 345 232 N ATOM 473 NH2 ARG A 58 -7.095 7.613 1.893 1.00 12.00 N ANISOU 473 NH2 ARG A 58 1380 1473 1705 -339 155 352 N ATOM 474 N ILE A 59 -12.062 3.525 1.010 1.00 7.34 N ANISOU 474 N ILE A 59 1058 970 761 74 -131 176 N ATOM 475 CA ILE A 59 -11.379 2.404 1.659 1.00 7.01 C ANISOU 475 CA ILE A 59 976 971 718 55 -89 121 C ATOM 476 C ILE A 59 -9.937 2.407 1.139 1.00 7.10 C ANISOU 476 C ILE A 59 962 987 749 43 -104 161 C ATOM 477 O ILE A 59 -9.695 2.594 -0.059 1.00 8.90 O ANISOU 477 O ILE A 59 1142 1535 705 162 -91 231 O ATOM 478 CB ILE A 59 -12.142 1.080 1.414 1.00 7.76 C ANISOU 478 CB ILE A 59 1130 1017 802 47 -147 96 C ATOM 479 CG1 ILE A 59 -11.577 -0.038 2.300 1.00 7.81 C ANISOU 479 CG1 ILE A 59 1198 923 847 18 -68 112 C ATOM 480 CG2 ILE A 59 -12.161 0.692 -0.066 1.00 8.53 C ANISOU 480 CG2 ILE A 59 1365 1031 844 96 -250 79 C ATOM 481 CD1 ILE A 59 -12.403 -1.320 2.234 1.00 8.66 C ANISOU 481 CD1 ILE A 59 1320 985 986 -55 -158 63 C ATOM 482 N LEU A 60 -8.996 2.240 2.067 1.00 7.01 N ANISOU 482 N LEU A 60 927 933 802 1 -68 149 N ATOM 483 CA LEU A 60 -7.562 2.380 1.783 1.00 7.20 C ANISOU 483 CA LEU A 60 970 904 861 60 -37 203 C ATOM 484 C LEU A 60 -6.795 1.180 2.333 1.00 6.67 C ANISOU 484 C LEU A 60 937 831 768 13 -20 111 C ATOM 485 O LEU A 60 -6.941 0.855 3.509 1.00 7.23 O ANISOU 485 O LEU A 60 1019 984 745 83 -20 196 O ATOM 486 CB LEU A 60 -7.011 3.650 2.464 1.00 7.87 C ANISOU 486 CB LEU A 60 992 915 1082 -32 -20 164 C ATOM 487 CG LEU A 60 -5.497 3.822 2.438 1.00 8.67 C ANISOU 487 CG LEU A 60 1094 1032 1169 -121 -67 155 C ATOM 488 CD1 LEU A 60 -4.969 4.096 1.036 1.00 9.88 C ANISOU 488 CD1 LEU A 60 1239 1262 1252 -161 100 212 C ATOM 489 CD2 LEU A 60 -5.066 4.923 3.396 1.00 9.76 C ANISOU 489 CD2 LEU A 60 1318 1091 1300 -150 -108 35 C ATOM 490 N ASN A 61 -5.950 0.559 1.505 1.00 6.84 N ANISOU 490 N ASN A 61 1015 866 719 18 -20 135 N ATOM 491 CA ASN A 61 -4.944 -0.393 1.998 1.00 6.89 C ANISOU 491 CA ASN A 61 991 875 751 27 -30 92 C ATOM 492 C ASN A 61 -3.697 0.423 2.369 1.00 7.03 C ANISOU 492 C ASN A 61 1033 819 818 24 -4 120 C ATOM 493 O ASN A 61 -3.058 1.002 1.484 1.00 8.04 O ANISOU 493 O ASN A 61 1142 970 944 -35 38 179 O ATOM 494 CB ASN A 61 -4.633 -1.430 0.913 1.00 7.15 C ANISOU 494 CB ASN A 61 1026 884 808 37 3 86 C ATOM 495 CG ASN A 61 -3.571 -2.425 1.341 1.00 7.33 C ANISOU 495 CG ASN A 61 1066 894 824 38 69 95 C ATOM 496 OD1 ASN A 61 -2.728 -2.143 2.204 1.00 7.84 O ANISOU 496 OD1 ASN A 61 1091 944 945 55 -72 19 O ATOM 497 ND2 ASN A 61 -3.603 -3.610 0.731 1.00 8.02 N ANISOU 497 ND2 ASN A 61 1187 962 898 71 69 19 N ATOM 498 N ASN A 62 -3.406 0.529 3.664 1.00 7.33 N ANISOU 498 N ASN A 62 1073 869 841 -32 -54 89 N ATOM 499 CA ASN A 62 -2.286 1.338 4.117 1.00 8.09 C ANISOU 499 CA ASN A 62 1156 947 972 -118 -51 142 C ATOM 500 C ASN A 62 -1.013 0.528 4.361 1.00 8.28 C ANISOU 500 C ASN A 62 1059 1072 1015 -195 -41 132 C ATOM 501 O ASN A 62 -0.042 1.043 4.918 1.00 10.06 O ANISOU 501 O ASN A 62 1205 1317 1299 -266 -183 100 O ATOM 502 CB ASN A 62 -2.656 2.175 5.339 1.00 8.70 C ANISOU 502 CB ASN A 62 1360 897 1048 -133 -142 51 C ATOM 503 CG ASN A 62 -3.033 1.323 6.522 1.00 8.82 C ANISOU 503 CG ASN A 62 1406 973 974 -112 -184 -3 C ATOM 504 OD1 ASN A 62 -2.674 0.152 6.600 1.00 8.51 O ANISOU 504 OD1 ASN A 62 1202 1072 961 -79 -114 131 O ATOM 505 ND2 ASN A 62 -3.796 1.904 7.442 1.00 12.14 N ANISOU 505 ND2 ASN A 62 2057 1233 1321 46 309 -26 N ATOM 506 N GLY A 63 -0.997 -0.734 3.949 1.00 8.26 N ANISOU 506 N GLY A 63 1022 1085 1033 -107 -26 137 N ATOM 507 CA GLY A 63 0.153 -1.594 4.147 1.00 9.11 C ANISOU 507 CA GLY A 63 1084 1206 1170 17 15 166 C ATOM 508 C GLY A 63 0.166 -2.355 5.461 1.00 8.81 C ANISOU 508 C GLY A 63 1070 1043 1234 -34 -135 102 C ATOM 509 O GLY A 63 1.013 -3.227 5.646 1.00 10.01 O ANISOU 509 O GLY A 63 1196 1197 1411 86 -71 108 O ATOM 510 N HIS A 64 -0.739 -2.021 6.380 1.00 8.69 N ANISOU 510 N HIS A 64 1006 1088 1208 -105 -106 262 N ATOM 511 CA HIS A 64 -0.875 -2.732 7.656 1.00 9.30 C ANISOU 511 CA HIS A 64 1025 1273 1235 -196 -147 348 C ATOM 512 C HIS A 64 -2.267 -3.287 7.927 1.00 8.83 C ANISOU 512 C HIS A 64 966 1009 1380 -107 -170 419 C ATOM 513 O HIS A 64 -2.428 -4.190 8.732 1.00 12.21 O ANISOU 513 O HIS A 64 1147 1435 2057 -129 -294 859 O ATOM 514 CB AHIS A 64 -0.237 -2.022 8.875 0.70 12.33 C ANISOU 514 CB AHIS A 64 1437 1874 1375 -412 -266 151 C ATOM 515 CB BHIS A 64 -0.564 -1.758 8.779 0.30 9.12 C ANISOU 515 CB BHIS A 64 806 1593 1067 -383 45 203 C ATOM 516 CG AHIS A 64 -0.690 -0.614 9.119 0.70 14.46 C ANISOU 516 CG AHIS A 64 1878 2153 1465 -122 -402 -80 C ATOM 517 CG BHIS A 64 0.789 -1.128 8.662 0.30 8.75 C ANISOU 517 CG BHIS A 64 822 1690 811 -365 110 45 C ATOM 518 ND1AHIS A 64 -0.060 0.477 8.556 0.70 16.72 N ANISOU 518 ND1AHIS A 64 2268 1809 2275 -355 -505 -325 N ATOM 519 ND1BHIS A 64 0.982 0.208 8.394 0.30 10.25 N ANISOU 519 ND1BHIS A 64 1091 1745 1060 -649 184 -144 N ATOM 520 CD2AHIS A 64 -1.621 -0.111 9.966 0.70 18.27 C ANISOU 520 CD2AHIS A 64 2124 3080 1739 386 -631 -435 C ATOM 521 CD2BHIS A 64 2.017 -1.671 8.796 0.30 9.34 C ANISOU 521 CD2BHIS A 64 740 2075 734 -349 51 -206 C ATOM 522 CE1AHIS A 64 -0.636 1.585 8.986 0.70 20.74 C ANISOU 522 CE1AHIS A 64 2760 2180 2941 -206 -783 -953 C ATOM 523 CE1BHIS A 64 2.279 0.462 8.362 0.30 11.51 C ANISOU 523 CE1BHIS A 64 1100 2131 1142 -831 17 -411 C ATOM 524 NE2AHIS A 64 -1.584 1.257 9.845 0.70 21.69 N ANISOU 524 NE2AHIS A 64 2252 2982 3008 552 -768 -908 N ATOM 525 NE2BHIS A 64 2.930 -0.662 8.607 0.30 11.54 N ANISOU 525 NE2BHIS A 64 970 2462 951 -708 -79 -319 N ATOM 526 N ALA A 65 -3.271 -2.683 7.311 1.00 7.90 N ANISOU 526 N ALA A 65 977 980 1044 -74 -56 249 N ATOM 527 CA ALA A 65 -4.659 -3.100 7.374 1.00 7.55 C ANISOU 527 CA ALA A 65 958 1032 878 -50 -30 135 C ATOM 528 C ALA A 65 -5.354 -2.360 6.217 1.00 7.09 C ANISOU 528 C ALA A 65 1024 851 821 30 -10 40 C ATOM 529 O ALA A 65 -4.710 -1.722 5.378 1.00 8.05 O ANISOU 529 O ALA A 65 1048 1108 902 -81 -52 246 O ATOM 530 CB ALA A 65 -5.308 -2.742 8.730 1.00 9.19 C ANISOU 530 CB ALA A 65 1140 1477 875 0 -14 146 C ATOM 531 N PHE A 66 -6.671 -2.437 6.177 1.00 6.92 N ANISOU 531 N PHE A 66 1026 870 733 80 -11 155 N ATOM 532 CA PHE A 66 -7.455 -1.519 5.351 1.00 6.98 C ANISOU 532 CA PHE A 66 1045 930 676 165 2 144 C ATOM 533 C PHE A 66 -8.361 -0.668 6.245 1.00 6.66 C ANISOU 533 C PHE A 66 1009 887 633 99 -30 103 C ATOM 534 O PHE A 66 -8.977 -1.163 7.196 1.00 7.15 O ANISOU 534 O PHE A 66 1157 866 694 96 80 133 O ATOM 535 CB PHE A 66 -8.273 -2.234 4.251 1.00 7.92 C ANISOU 535 CB PHE A 66 1146 1175 687 209 -59 78 C ATOM 536 CG PHE A 66 -9.319 -3.191 4.751 1.00 7.97 C ANISOU 536 CG PHE A 66 1213 1169 645 170 -205 -28 C ATOM 537 CD1 PHE A 66 -9.032 -4.529 4.894 1.00 8.60 C ANISOU 537 CD1 PHE A 66 1401 1137 730 85 -152 -114 C ATOM 538 CD2 PHE A 66 -10.589 -2.727 5.097 1.00 8.62 C ANISOU 538 CD2 PHE A 66 1095 1388 793 140 -288 1 C ATOM 539 CE1 PHE A 66 -9.988 -5.412 5.380 1.00 9.37 C ANISOU 539 CE1 PHE A 66 1479 1257 825 -52 -178 -239 C ATOM 540 CE2 PHE A 66 -11.549 -3.592 5.571 1.00 9.41 C ANISOU 540 CE2 PHE A 66 1249 1448 878 2 -277 -87 C ATOM 541 CZ PHE A 66 -11.254 -4.933 5.721 1.00 9.60 C ANISOU 541 CZ PHE A 66 1318 1470 860 -151 -277 -223 C ATOM 542 N ASN A 67 -8.427 0.623 5.938 1.00 6.37 N ANISOU 542 N ASN A 67 878 828 715 86 -71 137 N ATOM 543 CA ASN A 67 -9.278 1.538 6.674 1.00 6.60 C ANISOU 543 CA ASN A 67 942 804 763 68 -75 126 C ATOM 544 C ASN A 67 -10.469 1.949 5.821 1.00 6.30 C ANISOU 544 C ASN A 67 946 752 694 37 -83 47 C ATOM 545 O ASN A 67 -10.296 2.377 4.686 1.00 7.09 O ANISOU 545 O ASN A 67 991 1026 677 -1 -57 246 O ATOM 546 CB ASN A 67 -8.534 2.822 7.069 1.00 7.72 C ANISOU 546 CB ASN A 67 1033 944 957 -21 -139 50 C ATOM 547 CG ASN A 67 -7.485 2.613 8.132 1.00 9.33 C ANISOU 547 CG ASN A 67 1158 1156 1230 -140 -309 42 C ATOM 548 OD1 ASN A 67 -7.361 1.543 8.714 1.00 9.54 O ANISOU 548 OD1 ASN A 67 1202 1378 1044 -107 -309 231 O ATOM 549 ND2 ASN A 67 -6.751 3.669 8.422 1.00 12.75 N ANISOU 549 ND2 ASN A 67 1651 1287 1909 -151 -779 -104 N ATOM 550 N VAL A 68 -11.664 1.823 6.399 1.00 6.38 N ANISOU 550 N VAL A 68 953 779 693 56 -104 92 N ATOM 551 CA VAL A 68 -12.879 2.440 5.846 1.00 6.40 C ANISOU 551 CA VAL A 68 917 811 704 96 -89 160 C ATOM 552 C VAL A 68 -13.016 3.792 6.528 1.00 6.35 C ANISOU 552 C VAL A 68 906 829 679 98 -132 97 C ATOM 553 O VAL A 68 -13.168 3.858 7.752 1.00 6.84 O ANISOU 553 O VAL A 68 1094 785 721 112 -109 95 O ATOM 554 CB VAL A 68 -14.119 1.563 6.031 1.00 6.85 C ANISOU 554 CB VAL A 68 937 867 799 13 -122 83 C ATOM 555 CG1 VAL A 68 -15.366 2.347 5.583 1.00 8.31 C ANISOU 555 CG1 VAL A 68 981 1213 964 48 -188 100 C ATOM 556 CG2 VAL A 68 -13.993 0.268 5.261 1.00 8.41 C ANISOU 556 CG2 VAL A 68 1137 1070 989 -134 17 -99 C ATOM 557 N GLU A 69 -12.907 4.862 5.742 1.00 6.97 N ANISOU 557 N GLU A 69 1039 823 784 117 -85 172 N ATOM 558 CA GLU A 69 -12.798 6.219 6.229 1.00 7.13 C ANISOU 558 CA GLU A 69 1043 740 928 114 -96 64 C ATOM 559 C GLU A 69 -14.143 6.932 6.131 1.00 6.92 C ANISOU 559 C GLU A 69 1010 729 892 110 -161 134 C ATOM 560 O GLU A 69 -14.902 6.692 5.184 1.00 8.34 O ANISOU 560 O GLU A 69 1236 911 1020 160 -269 13 O ATOM 561 CB GLU A 69 -11.791 6.978 5.358 1.00 8.70 C ANISOU 561 CB GLU A 69 1202 908 1196 63 54 173 C ATOM 562 CG GLU A 69 -10.397 6.380 5.386 1.00 9.79 C ANISOU 562 CG GLU A 69 1195 1089 1436 94 170 203 C ATOM 563 CD GLU A 69 -9.504 6.933 4.275 1.00 11.28 C ANISOU 563 CD GLU A 69 1267 1198 1822 33 271 389 C ATOM 564 OE1 GLU A 69 -10.007 7.659 3.390 1.00 12.29 O ANISOU 564 OE1 GLU A 69 1506 1423 1740 117 385 519 O ATOM 565 OE2 GLU A 69 -8.310 6.613 4.306 1.00 13.68 O ANISOU 565 OE2 GLU A 69 1204 1597 2396 67 386 624 O ATOM 566 N PHE A 70 -14.403 7.820 7.095 1.00 7.25 N ANISOU 566 N PHE A 70 1015 783 956 66 -106 100 N ATOM 567 CA PHE A 70 -15.649 8.564 7.192 1.00 7.67 C ANISOU 567 CA PHE A 70 1064 775 1076 117 -129 113 C ATOM 568 C PHE A 70 -15.395 10.061 7.147 1.00 8.52 C ANISOU 568 C PHE A 70 1104 792 1342 101 -118 109 C ATOM 569 O PHE A 70 -14.325 10.555 7.510 1.00 9.29 O ANISOU 569 O PHE A 70 1167 844 1520 53 -130 128 O ATOM 570 CB PHE A 70 -16.388 8.197 8.502 1.00 7.77 C ANISOU 570 CB PHE A 70 1056 848 1049 126 -59 49 C ATOM 571 CG PHE A 70 -16.940 6.805 8.479 1.00 7.51 C ANISOU 571 CG PHE A 70 1013 872 969 130 -87 121 C ATOM 572 CD1 PHE A 70 -16.102 5.705 8.675 1.00 7.91 C ANISOU 572 CD1 PHE A 70 1154 805 1048 203 52 218 C ATOM 573 CD2 PHE A 70 -18.272 6.583 8.163 1.00 7.88 C ANISOU 573 CD2 PHE A 70 1040 895 1058 55 -117 187 C ATOM 574 CE1 PHE A 70 -16.609 4.422 8.558 1.00 8.58 C ANISOU 574 CE1 PHE A 70 1211 904 1145 157 114 178 C ATOM 575 CE2 PHE A 70 -18.788 5.293 8.058 1.00 8.69 C ANISOU 575 CE2 PHE A 70 1202 956 1144 -13 -80 131 C ATOM 576 CZ PHE A 70 -17.935 4.204 8.253 1.00 9.00 C ANISOU 576 CZ PHE A 70 1381 877 1164 -12 101 65 C ATOM 577 N ASP A 71 -16.429 10.811 6.745 1.00 9.81 N ANISOU 577 N ASP A 71 1282 797 1646 77 -301 223 N ATOM 578 CA ASP A 71 -16.423 12.269 6.914 1.00 11.39 C ANISOU 578 CA ASP A 71 1455 781 2091 66 -498 272 C ATOM 579 C ASP A 71 -16.590 12.600 8.397 1.00 11.19 C ANISOU 579 C ASP A 71 1315 761 2175 101 -197 99 C ATOM 580 O ASP A 71 -17.643 12.353 9.001 1.00 13.76 O ANISOU 580 O ASP A 71 1312 1371 2546 -47 13 -82 O ATOM 581 CB ASP A 71 -17.566 12.887 6.112 1.00 14.17 C ANISOU 581 CB ASP A 71 2010 939 2435 120 -1034 341 C ATOM 582 CG ASP A 71 -17.717 14.383 6.344 1.00 14.16 C ANISOU 582 CG ASP A 71 1942 936 2500 260 -731 180 C ATOM 583 OD1 ASP A 71 -16.791 15.017 6.882 1.00 13.88 O ANISOU 583 OD1 ASP A 71 1912 900 2461 142 -520 185 O ATOM 584 OD2 ASP A 71 -18.780 14.923 5.970 1.00 16.27 O ANISOU 584 OD2 ASP A 71 2089 1206 2886 204 -819 194 O ATOM 585 N ASP A 72 -15.527 13.131 8.981 1.00 11.08 N ANISOU 585 N ASP A 72 1391 869 1949 -20 -230 159 N ATOM 586 CA ASP A 72 -15.539 13.521 10.389 1.00 11.97 C ANISOU 586 CA ASP A 72 1707 847 1994 -7 -119 118 C ATOM 587 C ASP A 72 -15.448 15.046 10.570 1.00 13.57 C ANISOU 587 C ASP A 72 1918 881 2357 -194 -449 139 C ATOM 588 O ASP A 72 -14.952 15.521 11.587 1.00 16.01 O ANISOU 588 O ASP A 72 2527 990 2568 -161 -608 -45 O ATOM 589 CB ASP A 72 -14.413 12.829 11.151 1.00 11.63 C ANISOU 589 CB ASP A 72 1630 1041 1747 -105 -52 238 C ATOM 590 CG ASP A 72 -13.044 13.279 10.698 1.00 13.07 C ANISOU 590 CG ASP A 72 1671 1680 1616 -156 -86 364 C ATOM 591 OD1 ASP A 72 -12.950 13.950 9.633 1.00 16.41 O ANISOU 591 OD1 ASP A 72 1679 2765 1790 -395 -215 893 O ATOM 592 OD2 ASP A 72 -12.067 12.945 11.403 1.00 13.85 O ANISOU 592 OD2 ASP A 72 1759 2065 1440 -137 -139 370 O ATOM 593 N SER A 73 -15.954 15.789 9.591 1.00 14.12 N ANISOU 593 N SER A 73 1909 924 2533 -9 -396 250 N ATOM 594 CA SER A 73 -15.959 17.252 9.666 1.00 15.75 C ANISOU 594 CA SER A 73 2119 1015 2851 -182 -663 141 C ATOM 595 C SER A 73 -17.247 17.834 10.281 1.00 16.67 C ANISOU 595 C SER A 73 2285 834 3216 -21 -508 -225 C ATOM 596 O SER A 73 -17.402 19.051 10.366 1.00 18.20 O ANISOU 596 O SER A 73 3044 788 3083 131 -382 -104 O ATOM 597 CB SER A 73 -15.695 17.855 8.288 1.00 18.76 C ANISOU 597 CB SER A 73 2607 1593 2926 -474 -672 717 C ATOM 598 OG SER A 73 -16.803 17.658 7.429 1.00 16.62 O ANISOU 598 OG SER A 73 2732 1004 2578 97 -507 398 O ATOM 599 N GLN A 74 -18.160 16.955 10.692 1.00 16.01 N ANISOU 599 N GLN A 74 2221 1140 2722 178 -489 -102 N ATOM 600 CA GLN A 74 -19.358 17.308 11.463 1.00 17.19 C ANISOU 600 CA GLN A 74 2423 1625 2483 590 -425 -45 C ATOM 601 C GLN A 74 -19.700 16.131 12.351 1.00 15.80 C ANISOU 601 C GLN A 74 2037 1658 2308 208 -595 -276 C ATOM 602 O GLN A 74 -19.229 15.042 12.100 1.00 15.46 O ANISOU 602 O GLN A 74 1881 1448 2546 -111 -388 -388 O ATOM 603 CB GLN A 74 -20.555 17.513 10.553 1.00 19.81 C ANISOU 603 CB GLN A 74 2584 2149 2792 764 -610 187 C ATOM 604 CG GLN A 74 -20.463 18.673 9.622 1.00 24.10 C ANISOU 604 CG GLN A 74 2930 3159 3068 819 -643 614 C ATOM 605 CD GLN A 74 -21.731 18.821 8.836 1.00 23.90 C ANISOU 605 CD GLN A 74 2999 3129 2954 728 -671 648 C ATOM 606 OE1 GLN A 74 -21.830 18.367 7.695 1.00 23.46 O ANISOU 606 OE1 GLN A 74 2882 3161 2872 41 -540 569 O ATOM 607 NE2 GLN A 74 -22.726 19.445 9.446 1.00 24.48 N ANISOU 607 NE2 GLN A 74 2741 3418 3141 454 -755 646 N ATOM 608 N ASP A 75 -20.543 16.344 13.358 1.00 20.13 N ANISOU 608 N ASP A 75 2688 2599 2360 146 -275 -412 N ATOM 609 CA ASP A 75 -21.062 15.254 14.182 1.00 21.63 C ANISOU 609 CA ASP A 75 2718 3052 2450 -421 -468 -574 C ATOM 610 C ASP A 75 -22.085 14.438 13.382 1.00 21.93 C ANISOU 610 C ASP A 75 2067 3347 2918 70 -925 -813 C ATOM 611 O ASP A 75 -23.287 14.698 13.454 1.00 35.32 O ANISOU 611 O ASP A 75 2151 7476 3795 -172 -510 -2482 O ATOM 612 CB ASP A 75 -21.737 15.800 15.445 1.00 21.14 C ANISOU 612 CB ASP A 75 2883 2874 2276 142 -586 -186 C ATOM 613 CG ASP A 75 -20.753 16.135 16.555 1.00 22.87 C ANISOU 613 CG ASP A 75 3193 3143 2355 143 -434 -582 C ATOM 614 OD1 ASP A 75 -19.711 15.461 16.662 1.00 34.65 O ANISOU 614 OD1 ASP A 75 2421 7513 3231 262 -637 -1374 O ATOM 615 OD2 ASP A 75 -21.052 17.045 17.353 1.00 28.95 O ANISOU 615 OD2 ASP A 75 4951 3686 2362 -345 357 -1109 O ATOM 616 N LYS A 76 -21.603 13.465 12.617 1.00 18.46 N ANISOU 616 N LYS A 76 2290 1845 2877 165 -1247 -117 N ATOM 617 CA LYS A 76 -22.449 12.585 11.808 1.00 19.21 C ANISOU 617 CA LYS A 76 2518 1692 3090 -25 -1360 49 C ATOM 618 C LYS A 76 -22.592 11.166 12.347 1.00 18.06 C ANISOU 618 C LYS A 76 1718 1739 3405 95 -975 194 C ATOM 619 O LYS A 76 -23.626 10.524 12.187 1.00 22.93 O ANISOU 619 O LYS A 76 2033 2662 4017 -653 -880 358 O ATOM 620 CB LYS A 76 -21.874 12.476 10.404 1.00 22.23 C ANISOU 620 CB LYS A 76 3603 1788 3057 -318 -1329 22 C ATOM 621 CG LYS A 76 -22.115 13.686 9.546 1.00 24.71 C ANISOU 621 CG LYS A 76 4014 1912 3461 90 -676 299 C ATOM 622 CD LYS A 76 -21.552 13.456 8.160 1.00 26.15 C ANISOU 622 CD LYS A 76 4077 2272 3587 -537 -612 268 C ATOM 623 CE LYS A 76 -21.965 14.553 7.211 1.00 27.39 C ANISOU 623 CE LYS A 76 4236 2519 3653 -445 -649 395 C ATOM 624 NZ LYS A 76 -21.568 14.218 5.827 1.00 26.62 N ANISOU 624 NZ LYS A 76 3597 2717 3800 518 -547 751 N ATOM 625 N ALA A 77 -21.514 10.649 12.902 1.00 17.36 N ANISOU 625 N ALA A 77 1940 2111 2544 333 -549 385 N ATOM 626 CA ALA A 77 -21.470 9.298 13.453 1.00 14.00 C ANISOU 626 CA ALA A 77 1462 1891 1965 146 -456 77 C ATOM 627 C ALA A 77 -20.676 9.425 14.735 1.00 12.50 C ANISOU 627 C ALA A 77 1011 1794 1943 52 -426 1 C ATOM 628 O ALA A 77 -19.476 9.668 14.699 1.00 15.44 O ANISOU 628 O ALA A 77 942 2477 2448 -218 -239 -361 O ATOM 629 CB ALA A 77 -20.783 8.356 12.482 1.00 17.35 C ANISOU 629 CB ALA A 77 2030 2525 2038 430 -360 -137 C ATOM 630 N VAL A 78 -21.362 9.318 15.866 1.00 12.29 N ANISOU 630 N VAL A 78 1133 1781 1756 -41 -446 18 N ATOM 631 CA VAL A 78 -20.712 9.610 17.126 1.00 12.72 C ANISOU 631 CA VAL A 78 1525 1452 1858 -168 -499 58 C ATOM 632 C VAL A 78 -20.992 8.543 18.172 1.00 11.66 C ANISOU 632 C VAL A 78 1200 1454 1778 -189 -443 75 C ATOM 633 O VAL A 78 -22.022 7.846 18.171 1.00 13.84 O ANISOU 633 O VAL A 78 1488 1654 2117 -508 -723 351 O ATOM 634 CB VAL A 78 -21.106 10.994 17.682 1.00 16.48 C ANISOU 634 CB VAL A 78 2246 1636 2379 -32 -240 -43 C ATOM 635 CG1 VAL A 78 -20.713 12.109 16.714 1.00 16.28 C ANISOU 635 CG1 VAL A 78 1974 1538 2673 131 -376 66 C ATOM 636 CG2 VAL A 78 -22.581 11.023 17.968 1.00 22.65 C ANISOU 636 CG2 VAL A 78 2855 2940 2811 508 784 222 C ATOM 637 N LEU A 79 -20.026 8.432 19.064 1.00 10.11 N ANISOU 637 N LEU A 79 1160 1192 1488 -89 -153 -59 N ATOM 638 CA LEU A 79 -20.058 7.569 20.211 1.00 9.84 C ANISOU 638 CA LEU A 79 1101 1221 1415 -192 -102 -61 C ATOM 639 C LEU A 79 -20.053 8.445 21.461 1.00 10.31 C ANISOU 639 C LEU A 79 1220 1240 1458 -169 -29 -102 C ATOM 640 O LEU A 79 -19.230 9.369 21.567 1.00 10.96 O ANISOU 640 O LEU A 79 1217 1381 1567 -232 -11 -218 O ATOM 641 CB LEU A 79 -18.823 6.663 20.160 1.00 10.21 C ANISOU 641 CB LEU A 79 1013 1442 1425 -171 -90 27 C ATOM 642 CG LEU A 79 -18.696 5.600 21.239 1.00 11.07 C ANISOU 642 CG LEU A 79 1185 1453 1566 10 114 105 C ATOM 643 CD1 LEU A 79 -19.825 4.594 21.127 1.00 13.13 C ANISOU 643 CD1 LEU A 79 1376 1709 1904 -203 67 365 C ATOM 644 CD2 LEU A 79 -17.338 4.906 21.116 1.00 11.18 C ANISOU 644 CD2 LEU A 79 1245 1525 1479 141 41 8 C ATOM 645 N ALYS A 80 -20.932 8.144 22.406 0.70 10.71 N ANISOU 645 N ALYS A 80 1108 1384 1579 -50 45 -195 N ATOM 646 N BLYS A 80 -20.974 8.144 22.375 0.30 10.72 N ANISOU 646 N BLYS A 80 1174 1381 1519 -242 80 -201 N ATOM 647 CA ALYS A 80 -20.989 8.861 23.671 0.70 12.47 C ANISOU 647 CA ALYS A 80 1549 1420 1768 91 136 -164 C ATOM 648 CA BLYS A 80 -21.160 8.869 23.629 0.30 10.30 C ANISOU 648 CA BLYS A 80 979 1246 1688 -340 77 -198 C ATOM 649 C ALYS A 80 -21.532 7.910 24.740 0.70 11.28 C ANISOU 649 C ALYS A 80 1165 1487 1635 -8 88 -102 C ATOM 650 C BLYS A 80 -21.464 7.878 24.749 0.30 10.24 C ANISOU 650 C BLYS A 80 824 1379 1686 -397 156 -118 C ATOM 651 O ALYS A 80 -21.900 6.761 24.458 0.70 11.19 O ANISOU 651 O ALYS A 80 999 1633 1621 -83 -101 -71 O ATOM 652 O BLYS A 80 -21.602 6.678 24.508 0.30 10.57 O ANISOU 652 O BLYS A 80 985 1420 1609 -476 2 36 O ATOM 653 CB ALYS A 80 -21.870 10.104 23.549 0.70 16.10 C ANISOU 653 CB ALYS A 80 2258 1506 2351 370 233 -161 C ATOM 654 CB BLYS A 80 -22.331 9.844 23.512 0.30 12.02 C ANISOU 654 CB BLYS A 80 1091 1446 2031 -172 36 -184 C ATOM 655 CG ALYS A 80 -23.338 9.776 23.430 0.70 21.94 C ANISOU 655 CG ALYS A 80 2212 2906 3217 831 -338 79 C ATOM 656 CG BLYS A 80 -22.080 11.014 22.593 0.30 13.70 C ANISOU 656 CG BLYS A 80 1008 1560 2636 57 -274 -55 C ATOM 657 CD ALYS A 80 -24.083 10.710 22.492 0.70 30.38 C ANISOU 657 CD ALYS A 80 3691 3512 4341 551 -1430 503 C ATOM 658 CD BLYS A 80 -23.166 12.054 22.761 0.30 21.78 C ANISOU 658 CD BLYS A 80 1818 2497 3960 1114 -841 296 C ATOM 659 CE ALYS A 80 -23.497 12.104 22.455 0.70 31.60 C ANISOU 659 CE ALYS A 80 3564 3345 5097 859 -2053 633 C ATOM 660 CE BLYS A 80 -23.008 13.160 21.747 0.30 27.12 C ANISOU 660 CE BLYS A 80 2731 2851 4721 1218 -1033 860 C ATOM 661 NZ ALYS A 80 -24.304 12.994 21.574 0.70 44.55 N ANISOU 661 NZ ALYS A 80 5624 5138 6164 -26 -2715 2411 N ATOM 662 NZ BLYS A 80 -22.571 12.606 20.445 0.30 26.09 N ANISOU 662 NZ BLYS A 80 2326 2625 4961 515 -641 1254 N ATOM 663 N GLY A 81 -21.562 8.385 25.977 1.00 12.16 N ANISOU 663 N GLY A 81 1439 1440 1743 34 432 -65 N ATOM 664 CA GLY A 81 -22.018 7.571 27.086 1.00 12.54 C ANISOU 664 CA GLY A 81 1455 1485 1826 51 423 91 C ATOM 665 C GLY A 81 -20.996 6.547 27.519 1.00 12.21 C ANISOU 665 C GLY A 81 1316 1350 1974 -5 380 2 C ATOM 666 O GLY A 81 -19.805 6.681 27.237 1.00 11.43 O ANISOU 666 O GLY A 81 1231 1404 1706 -219 334 -201 O ATOM 667 N GLY A 82 -21.458 5.528 28.230 1.00 13.86 N ANISOU 667 N GLY A 82 1340 1487 2439 40 507 278 N ATOM 668 CA GLY A 82 -20.543 4.557 28.793 1.00 14.31 C ANISOU 668 CA GLY A 82 1363 1632 2443 96 459 326 C ATOM 669 C GLY A 82 -19.560 5.232 29.711 1.00 14.85 C ANISOU 669 C GLY A 82 1403 1947 2294 212 654 139 C ATOM 670 O GLY A 82 -19.955 5.990 30.592 1.00 17.16 O ANISOU 670 O GLY A 82 1570 2379 2569 334 821 -137 O ATOM 671 N PRO A 83 -18.263 4.964 29.514 1.00 12.48 N ANISOU 671 N PRO A 83 1341 1458 1941 222 508 133 N ATOM 672 CA PRO A 83 -17.252 5.597 30.352 1.00 13.07 C ANISOU 672 CA PRO A 83 1632 1584 1751 354 318 64 C ATOM 673 C PRO A 83 -16.905 7.013 29.883 1.00 12.69 C ANISOU 673 C PRO A 83 1640 1624 1558 194 234 -59 C ATOM 674 O PRO A 83 -16.116 7.687 30.542 1.00 15.41 O ANISOU 674 O PRO A 83 1844 2317 1695 -264 57 -8 O ATOM 675 CB PRO A 83 -16.049 4.678 30.159 1.00 14.30 C ANISOU 675 CB PRO A 83 1678 1937 1817 595 97 144 C ATOM 676 CG PRO A 83 -16.187 4.185 28.729 1.00 12.35 C ANISOU 676 CG PRO A 83 1273 1609 1809 300 148 88 C ATOM 677 CD PRO A 83 -17.670 4.058 28.502 1.00 11.92 C ANISOU 677 CD PRO A 83 1245 1396 1887 129 370 71 C ATOM 678 N LEU A 84 -17.472 7.441 28.753 1.00 10.95 N ANISOU 678 N LEU A 84 1338 1359 1462 216 313 -136 N ATOM 679 CA LEU A 84 -16.993 8.634 28.071 1.00 10.53 C ANISOU 679 CA LEU A 84 1243 1280 1478 157 183 -212 C ATOM 680 C LEU A 84 -17.635 9.916 28.593 1.00 12.02 C ANISOU 680 C LEU A 84 1464 1360 1741 114 268 -477 C ATOM 681 O LEU A 84 -18.822 9.970 28.884 1.00 13.48 O ANISOU 681 O LEU A 84 1423 1663 2035 245 244 -579 O ATOM 682 CB LEU A 84 -17.287 8.536 26.582 1.00 9.27 C ANISOU 682 CB LEU A 84 1043 1082 1397 53 128 -234 C ATOM 683 CG LEU A 84 -16.726 7.291 25.880 1.00 9.16 C ANISOU 683 CG LEU A 84 1011 1128 1340 70 31 -199 C ATOM 684 CD1 LEU A 84 -17.227 7.239 24.457 1.00 11.04 C ANISOU 684 CD1 LEU A 84 1501 1322 1370 310 -3 -246 C ATOM 685 CD2 LEU A 84 -15.183 7.258 25.933 1.00 9.44 C ANISOU 685 CD2 LEU A 84 1033 1158 1394 66 139 -183 C ATOM 686 N ASP A 85 -16.821 10.957 28.648 1.00 13.38 N ANISOU 686 N ASP A 85 1749 1432 1902 -24 305 -648 N ATOM 687 CA ASP A 85 -17.282 12.319 28.866 1.00 16.61 C ANISOU 687 CA ASP A 85 2575 1430 2305 -46 201 -636 C ATOM 688 C ASP A 85 -17.192 12.997 27.494 1.00 16.75 C ANISOU 688 C ASP A 85 2375 1605 2383 -122 389 -382 C ATOM 689 O ASP A 85 -16.142 12.981 26.829 1.00 22.39 O ANISOU 689 O ASP A 85 3459 2500 2549 761 1429 -152 O ATOM 690 CB ASP A 85 -16.390 13.017 29.887 1.00 25.59 C ANISOU 690 CB ASP A 85 4839 2087 2796 -249 -545 -831 C ATOM 691 CG ASP A 85 -16.568 12.472 31.294 1.00 37.22 C ANISOU 691 CG ASP A 85 5713 5469 2959 -449 -1254 -775 C ATOM 692 OD1 ASP A 85 -17.658 11.935 31.595 1.00 41.32 O ANISOU 692 OD1 ASP A 85 5816 6556 3327 -517 -368 -658 O ATOM 693 OD2 ASP A 85 -15.619 12.587 32.101 1.00 54.12 O ANISOU 693 OD2 ASP A 85 7722 9799 3042 -1694 -1731 -1258 O ATOM 694 N GLY A 86 -18.312 13.551 27.046 1.00 18.95 N ANISOU 694 N GLY A 86 2618 2176 2406 -354 -102 -265 N ATOM 695 CA GLY A 86 -18.346 14.245 25.777 1.00 21.21 C ANISOU 695 CA GLY A 86 3630 2041 2389 -470 79 -413 C ATOM 696 C GLY A 86 -18.651 13.374 24.570 1.00 17.07 C ANISOU 696 C GLY A 86 2661 1499 2326 -426 9 -398 C ATOM 697 O GLY A 86 -19.187 12.276 24.680 1.00 18.39 O ANISOU 697 O GLY A 86 2513 1743 2733 -732 73 -316 O ATOM 698 N THR A 87 -18.289 13.892 23.402 1.00 13.34 N ANISOU 698 N THR A 87 1716 1245 2106 53 20 -517 N ATOM 699 CA THR A 87 -18.715 13.344 22.126 1.00 13.13 C ANISOU 699 CA THR A 87 1310 1552 2126 300 -6 -622 C ATOM 700 C THR A 87 -17.500 12.934 21.323 1.00 10.74 C ANISOU 700 C THR A 87 1061 1031 1987 129 -46 -345 C ATOM 701 O THR A 87 -16.560 13.718 21.191 1.00 11.35 O ANISOU 701 O THR A 87 1253 899 2161 17 73 -216 O ATOM 702 CB THR A 87 -19.481 14.425 21.336 1.00 18.05 C ANISOU 702 CB THR A 87 1774 2660 2425 1156 45 -502 C ATOM 703 OG1 THR A 87 -20.645 14.806 22.075 1.00 19.50 O ANISOU 703 OG1 THR A 87 1780 2685 2943 933 196 -610 O ATOM 704 CG2 THR A 87 -19.885 13.934 19.947 1.00 17.85 C ANISOU 704 CG2 THR A 87 1804 2480 2499 669 -312 -468 C ATOM 705 N TYR A 88 -17.541 11.733 20.773 1.00 9.65 N ANISOU 705 N TYR A 88 986 1020 1662 114 -95 -296 N ATOM 706 CA TYR A 88 -16.427 11.206 19.985 1.00 9.11 C ANISOU 706 CA TYR A 88 976 1016 1468 79 -195 -276 C ATOM 707 C TYR A 88 -16.908 10.863 18.581 1.00 9.16 C ANISOU 707 C TYR A 88 889 1062 1530 80 -264 -199 C ATOM 708 O TYR A 88 -17.841 10.099 18.396 1.00 11.67 O ANISOU 708 O TYR A 88 1263 1411 1761 -223 -334 -142 O ATOM 709 CB TYR A 88 -15.835 9.984 20.654 1.00 9.10 C ANISOU 709 CB TYR A 88 1117 951 1391 127 -238 -316 C ATOM 710 CG TYR A 88 -15.091 10.230 21.952 1.00 8.27 C ANISOU 710 CG TYR A 88 987 824 1332 63 -74 -186 C ATOM 711 CD1 TYR A 88 -15.745 10.598 23.126 1.00 8.47 C ANISOU 711 CD1 TYR A 88 915 984 1321 33 33 -181 C ATOM 712 CD2 TYR A 88 -13.705 10.053 22.011 1.00 8.00 C ANISOU 712 CD2 TYR A 88 1021 834 1183 122 -19 -154 C ATOM 713 CE1 TYR A 88 -15.039 10.787 24.303 1.00 8.68 C ANISOU 713 CE1 TYR A 88 974 1082 1241 0 109 -139 C ATOM 714 CE2 TYR A 88 -12.993 10.215 23.169 1.00 7.73 C ANISOU 714 CE2 TYR A 88 980 807 1151 36 56 -127 C ATOM 715 CZ TYR A 88 -13.658 10.565 24.327 1.00 8.01 C ANISOU 715 CZ TYR A 88 1004 843 1198 -25 35 -182 C ATOM 716 OH TYR A 88 -12.957 10.692 25.497 1.00 8.78 O ANISOU 716 OH TYR A 88 1084 1069 1183 -6 116 -202 O ATOM 717 N ARG A 89 -16.234 11.410 17.585 1.00 8.81 N ANISOU 717 N ARG A 89 975 942 1431 210 -188 -315 N ATOM 718 CA ARG A 89 -16.639 11.286 16.179 1.00 8.96 C ANISOU 718 CA ARG A 89 1092 836 1477 128 -356 -91 C ATOM 719 C ARG A 89 -15.902 10.155 15.481 1.00 7.81 C ANISOU 719 C ARG A 89 1052 823 1093 -25 -236 45 C ATOM 720 O ARG A 89 -14.668 10.045 15.572 1.00 7.73 O ANISOU 720 O ARG A 89 1018 873 1048 -33 -145 -8 O ATOM 721 CB ARG A 89 -16.263 12.548 15.412 1.00 12.45 C ANISOU 721 CB ARG A 89 1632 1045 2052 110 -800 140 C ATOM 722 CG ARG A 89 -17.201 13.634 15.527 1.00 17.94 C ANISOU 722 CG ARG A 89 2525 1556 2734 682 -686 61 C ATOM 723 CD ARG A 89 -16.895 14.670 14.514 1.00 21.02 C ANISOU 723 CD ARG A 89 2504 1915 3568 138 -1026 1220 C ATOM 724 NE ARG A 89 -17.610 15.820 14.969 1.00 21.36 N ANISOU 724 NE ARG A 89 2817 2375 2923 70 -1164 948 N ATOM 725 CZ ARG A 89 -17.316 17.053 14.621 1.00 21.10 C ANISOU 725 CZ ARG A 89 3599 2150 2268 334 -621 519 C ATOM 726 NH1 ARG A 89 -16.351 17.295 13.738 1.00 20.77 N ANISOU 726 NH1 ARG A 89 3762 1679 2453 595 -162 705 N ATOM 727 NH2 ARG A 89 -18.040 18.054 15.096 1.00 25.47 N ANISOU 727 NH2 ARG A 89 3632 3146 2900 150 -489 -704 N ATOM 728 N LEU A 90 -16.662 9.326 14.754 1.00 7.82 N ANISOU 728 N LEU A 90 1083 846 1040 43 -199 -27 N ATOM 729 CA LEU A 90 -16.071 8.244 13.975 1.00 7.67 C ANISOU 729 CA LEU A 90 1089 878 946 -27 -203 44 C ATOM 730 C LEU A 90 -15.217 8.778 12.826 1.00 8.00 C ANISOU 730 C LEU A 90 1166 873 1002 -57 -252 147 C ATOM 731 O LEU A 90 -15.700 9.559 11.997 1.00 9.70 O ANISOU 731 O LEU A 90 1218 1266 1201 -32 -281 387 O ATOM 732 CB LEU A 90 -17.200 7.365 13.419 1.00 8.05 C ANISOU 732 CB LEU A 90 1036 1024 998 -145 -163 -66 C ATOM 733 CG LEU A 90 -16.778 6.159 12.575 1.00 8.95 C ANISOU 733 CG LEU A 90 1270 1101 1029 -261 -128 -59 C ATOM 734 CD1 LEU A 90 -15.991 5.122 13.384 1.00 9.20 C ANISOU 734 CD1 LEU A 90 1387 978 1132 -85 -36 -56 C ATOM 735 CD2 LEU A 90 -18.014 5.528 11.941 1.00 10.30 C ANISOU 735 CD2 LEU A 90 1369 1396 1150 -463 -84 -117 C ATOM 736 N ILE A 91 -13.969 8.320 12.762 1.00 7.19 N ANISOU 736 N ILE A 91 1177 664 892 15 -97 43 N ATOM 737 CA ILE A 91 -13.056 8.681 11.673 1.00 7.17 C ANISOU 737 CA ILE A 91 1180 663 883 -32 -118 40 C ATOM 738 C ILE A 91 -12.778 7.518 10.723 1.00 6.66 C ANISOU 738 C ILE A 91 1076 616 838 -31 -159 83 C ATOM 739 O ILE A 91 -12.734 7.714 9.512 1.00 6.94 O ANISOU 739 O ILE A 91 1170 688 777 68 -129 102 O ATOM 740 CB ILE A 91 -11.746 9.345 12.207 1.00 8.18 C ANISOU 740 CB ILE A 91 1323 797 988 -209 -71 -9 C ATOM 741 CG1 ILE A 91 -10.798 9.685 11.052 1.00 10.76 C ANISOU 741 CG1 ILE A 91 1593 1333 1160 -571 -34 1 C ATOM 742 CG2 ILE A 91 -11.039 8.495 13.272 1.00 8.54 C ANISOU 742 CG2 ILE A 91 1288 900 1056 -157 -210 -29 C ATOM 743 CD1 ILE A 91 -9.624 10.586 11.481 1.00 13.71 C ANISOU 743 CD1 ILE A 91 1809 1814 1587 -899 -26 -82 C ATOM 744 N GLN A 92 -12.619 6.300 11.252 1.00 6.63 N ANISOU 744 N GLN A 92 1159 579 780 2 -139 59 N ATOM 745 CA GLN A 92 -12.370 5.142 10.410 1.00 6.43 C ANISOU 745 CA GLN A 92 976 676 792 44 -82 97 C ATOM 746 C GLN A 92 -12.634 3.884 11.206 1.00 5.85 C ANISOU 746 C GLN A 92 954 625 644 49 -53 18 C ATOM 747 O GLN A 92 -12.618 3.911 12.426 1.00 6.66 O ANISOU 747 O GLN A 92 1202 679 649 42 -82 16 O ATOM 748 CB GLN A 92 -10.933 5.122 9.827 1.00 7.24 C ANISOU 748 CB GLN A 92 960 776 1013 -8 -92 193 C ATOM 749 CG GLN A 92 -9.811 5.294 10.859 1.00 8.46 C ANISOU 749 CG GLN A 92 1098 806 1309 -34 -262 109 C ATOM 750 CD GLN A 92 -9.154 4.019 11.327 1.00 7.96 C ANISOU 750 CD GLN A 92 986 861 1178 28 -178 138 C ATOM 751 OE1 GLN A 92 -9.690 2.918 11.239 1.00 7.90 O ANISOU 751 OE1 GLN A 92 1125 758 1120 58 -230 146 O ATOM 752 NE2 GLN A 92 -7.994 4.193 11.931 1.00 10.78 N ANISOU 752 NE2 GLN A 92 1097 1397 1603 -61 -369 231 N ATOM 753 N PHE A 93 -12.841 2.782 10.490 1.00 5.67 N ANISOU 753 N PHE A 93 883 615 654 65 -68 53 N ATOM 754 CA PHE A 93 -12.721 1.478 11.093 1.00 5.71 C ANISOU 754 CA PHE A 93 860 649 662 25 -59 32 C ATOM 755 C PHE A 93 -11.758 0.609 10.273 1.00 5.47 C ANISOU 755 C PHE A 93 874 646 559 17 -111 65 C ATOM 756 O PHE A 93 -11.544 0.814 9.082 1.00 6.26 O ANISOU 756 O PHE A 93 1036 744 597 104 -77 63 O ATOM 757 CB PHE A 93 -14.066 0.764 11.345 1.00 5.97 C ANISOU 757 CB PHE A 93 885 706 678 33 -118 83 C ATOM 758 CG PHE A 93 -14.818 0.295 10.111 1.00 5.95 C ANISOU 758 CG PHE A 93 849 667 746 45 -90 99 C ATOM 759 CD1 PHE A 93 -14.457 -0.860 9.428 1.00 6.64 C ANISOU 759 CD1 PHE A 93 960 753 811 37 -126 71 C ATOM 760 CD2 PHE A 93 -15.932 1.004 9.657 1.00 6.37 C ANISOU 760 CD2 PHE A 93 878 774 768 47 -71 76 C ATOM 761 CE1 PHE A 93 -15.160 -1.290 8.330 1.00 6.90 C ANISOU 761 CE1 PHE A 93 955 791 874 -17 -179 18 C ATOM 762 CE2 PHE A 93 -16.643 0.566 8.557 1.00 7.01 C ANISOU 762 CE2 PHE A 93 915 891 856 33 -150 98 C ATOM 763 CZ PHE A 93 -16.267 -0.568 7.879 1.00 7.07 C ANISOU 763 CZ PHE A 93 921 880 886 -38 -184 70 C ATOM 764 N HIS A 94 -11.224 -0.404 10.953 1.00 5.61 N ANISOU 764 N HIS A 94 909 658 567 51 -59 22 N ATOM 765 CA HIS A 94 -10.329 -1.383 10.342 1.00 5.74 C ANISOU 765 CA HIS A 94 889 648 643 48 -68 54 C ATOM 766 C HIS A 94 -10.399 -2.656 11.180 1.00 5.45 C ANISOU 766 C HIS A 94 825 691 556 59 -125 24 C ATOM 767 O HIS A 94 -11.026 -2.677 12.251 1.00 6.10 O ANISOU 767 O HIS A 94 1001 714 601 100 -14 52 O ATOM 768 CB HIS A 94 -8.886 -0.855 10.269 1.00 6.22 C ANISOU 768 CB HIS A 94 924 735 703 23 -21 90 C ATOM 769 CG HIS A 94 -8.327 -0.579 11.627 1.00 5.64 C ANISOU 769 CG HIS A 94 791 658 695 10 -40 38 C ATOM 770 ND1 HIS A 94 -8.480 0.619 12.276 1.00 6.13 N ANISOU 770 ND1 HIS A 94 902 681 747 30 -123 65 N ATOM 771 CD2 HIS A 94 -7.692 -1.399 12.502 1.00 5.94 C ANISOU 771 CD2 HIS A 94 807 746 703 51 -28 36 C ATOM 772 CE1 HIS A 94 -7.943 0.536 13.484 1.00 6.19 C ANISOU 772 CE1 HIS A 94 847 714 791 8 -100 -3 C ATOM 773 NE2 HIS A 94 -7.473 -0.688 13.657 1.00 5.87 N ANISOU 773 NE2 HIS A 94 817 704 708 60 -143 63 N ATOM 774 N PHE A 95 -9.737 -3.689 10.696 1.00 5.59 N ANISOU 774 N PHE A 95 859 660 605 15 -76 65 N ATOM 775 CA PHE A 95 -9.686 -4.972 11.358 1.00 5.64 C ANISOU 775 CA PHE A 95 867 617 659 29 -48 55 C ATOM 776 C PHE A 95 -8.219 -5.426 11.550 1.00 5.47 C ANISOU 776 C PHE A 95 843 576 658 82 -77 32 C ATOM 777 O PHE A 95 -7.308 -4.963 10.865 1.00 6.82 O ANISOU 777 O PHE A 95 910 828 851 43 -47 127 O ATOM 778 CB PHE A 95 -10.406 -6.070 10.533 1.00 6.04 C ANISOU 778 CB PHE A 95 859 702 734 34 -118 -23 C ATOM 779 CG PHE A 95 -11.847 -5.781 10.196 1.00 5.98 C ANISOU 779 CG PHE A 95 869 677 725 30 -136 -81 C ATOM 780 CD1 PHE A 95 -12.182 -4.923 9.159 1.00 6.85 C ANISOU 780 CD1 PHE A 95 945 841 815 70 -144 -51 C ATOM 781 CD2 PHE A 95 -12.881 -6.418 10.893 1.00 6.75 C ANISOU 781 CD2 PHE A 95 891 841 833 -40 -118 -100 C ATOM 782 CE1 PHE A 95 -13.516 -4.694 8.818 1.00 7.48 C ANISOU 782 CE1 PHE A 95 965 970 908 115 -261 -51 C ATOM 783 CE2 PHE A 95 -14.205 -6.201 10.545 1.00 7.41 C ANISOU 783 CE2 PHE A 95 948 907 962 -22 -137 -196 C ATOM 784 CZ PHE A 95 -14.520 -5.335 9.512 1.00 7.56 C ANISOU 784 CZ PHE A 95 929 982 962 131 -218 -252 C ATOM 785 N HIS A 96 -8.085 -6.389 12.458 1.00 5.49 N ANISOU 785 N HIS A 96 850 577 660 18 -114 9 N ATOM 786 CA HIS A 96 -6.885 -7.198 12.632 1.00 5.76 C ANISOU 786 CA HIS A 96 832 646 710 97 -32 7 C ATOM 787 C HIS A 96 -7.324 -8.649 12.496 1.00 5.56 C ANISOU 787 C HIS A 96 857 634 622 20 -73 16 C ATOM 788 O HIS A 96 -8.384 -9.008 13.011 1.00 6.50 O ANISOU 788 O HIS A 96 960 718 793 16 -5 -22 O ATOM 789 CB HIS A 96 -6.246 -6.968 14.009 1.00 6.23 C ANISOU 789 CB HIS A 96 926 660 781 41 -143 22 C ATOM 790 CG HIS A 96 -5.957 -5.528 14.281 1.00 5.89 C ANISOU 790 CG HIS A 96 822 701 714 35 -90 -1 C ATOM 791 ND1 HIS A 96 -4.745 -4.942 14.045 1.00 6.98 N ANISOU 791 ND1 HIS A 96 785 764 1102 61 -61 -91 N ATOM 792 CD2 HIS A 96 -6.767 -4.512 14.717 1.00 5.99 C ANISOU 792 CD2 HIS A 96 848 742 687 -72 -110 13 C ATOM 793 CE1 HIS A 96 -4.799 -3.650 14.330 1.00 6.85 C ANISOU 793 CE1 HIS A 96 869 708 1026 117 -20 -90 C ATOM 794 NE2 HIS A 96 -6.012 -3.352 14.742 1.00 6.01 N ANISOU 794 NE2 HIS A 96 774 795 714 60 -119 5 N ATOM 795 N TRP A 97 -6.531 -9.478 11.817 1.00 5.60 N ANISOU 795 N TRP A 97 900 590 638 15 -32 -31 N ATOM 796 CA TRP A 97 -6.938 -10.849 11.587 1.00 5.96 C ANISOU 796 CA TRP A 97 859 663 741 28 21 -21 C ATOM 797 C TRP A 97 -5.727 -11.771 11.468 1.00 5.74 C ANISOU 797 C TRP A 97 952 546 683 12 -8 8 C ATOM 798 O TRP A 97 -4.575 -11.343 11.348 1.00 6.61 O ANISOU 798 O TRP A 97 1008 669 833 58 9 13 O ATOM 799 CB TRP A 97 -7.852 -10.973 10.365 1.00 6.27 C ANISOU 799 CB TRP A 97 890 732 758 -14 -9 -37 C ATOM 800 CG TRP A 97 -7.198 -10.557 9.073 1.00 6.09 C ANISOU 800 CG TRP A 97 876 708 729 33 -72 -72 C ATOM 801 CD1 TRP A 97 -6.525 -11.378 8.200 1.00 6.63 C ANISOU 801 CD1 TRP A 97 1036 755 729 17 23 -61 C ATOM 802 CD2 TRP A 97 -7.146 -9.249 8.513 1.00 5.81 C ANISOU 802 CD2 TRP A 97 865 733 609 -34 -101 -52 C ATOM 803 NE1 TRP A 97 -6.086 -10.658 7.116 1.00 6.86 N ANISOU 803 NE1 TRP A 97 1072 803 733 39 -5 -48 N ATOM 804 CE2 TRP A 97 -6.439 -9.341 7.290 1.00 6.27 C ANISOU 804 CE2 TRP A 97 1000 726 656 19 -67 -51 C ATOM 805 CE3 TRP A 97 -7.629 -7.990 8.919 1.00 6.16 C ANISOU 805 CE3 TRP A 97 924 769 649 55 -124 -35 C ATOM 806 CZ2 TRP A 97 -6.242 -8.232 6.457 1.00 6.51 C ANISOU 806 CZ2 TRP A 97 926 843 705 1 -62 10 C ATOM 807 CZ3 TRP A 97 -7.407 -6.890 8.116 1.00 6.39 C ANISOU 807 CZ3 TRP A 97 946 773 708 22 -87 -1 C ATOM 808 CH2 TRP A 97 -6.724 -7.020 6.892 1.00 6.63 C ANISOU 808 CH2 TRP A 97 992 797 729 14 -84 33 C ATOM 809 N GLY A 98 -6.031 -13.072 11.496 1.00 6.59 N ANISOU 809 N GLY A 98 1020 659 823 42 -29 -54 N ATOM 810 CA GLY A 98 -5.000 -14.092 11.521 1.00 6.99 C ANISOU 810 CA GLY A 98 1071 679 906 68 5 -9 C ATOM 811 C GLY A 98 -4.813 -14.786 10.188 1.00 7.07 C ANISOU 811 C GLY A 98 1125 643 917 -15 -26 -66 C ATOM 812 O GLY A 98 -5.563 -14.613 9.234 1.00 8.13 O ANISOU 812 O GLY A 98 1333 811 943 50 -60 -114 O ATOM 813 N SER A 99 -3.792 -15.642 10.163 1.00 7.77 N ANISOU 813 N SER A 99 1277 695 980 112 43 -129 N ATOM 814 CA SER A 99 -3.582 -16.573 9.058 1.00 8.90 C ANISOU 814 CA SER A 99 1391 787 1204 130 50 -238 C ATOM 815 C SER A 99 -4.448 -17.840 9.201 1.00 9.47 C ANISOU 815 C SER A 99 1408 796 1394 147 -88 -337 C ATOM 816 O SER A 99 -4.599 -18.590 8.232 1.00 11.88 O ANISOU 816 O SER A 99 1870 1075 1568 42 -70 -507 O ATOM 817 CB SER A 99 -2.100 -16.954 8.969 1.00 9.90 C ANISOU 817 CB SER A 99 1430 966 1364 223 169 -273 C ATOM 818 OG SER A 99 -1.623 -17.448 10.200 1.00 9.97 O ANISOU 818 OG SER A 99 1372 889 1528 207 109 -72 O ATOM 819 N LEU A 100 -4.962 -18.092 10.413 1.00 9.82 N ANISOU 819 N LEU A 100 1273 829 1627 12 92 -303 N ATOM 820 CA LEU A 100 -5.727 -19.276 10.824 1.00 11.62 C ANISOU 820 CA LEU A 100 1625 814 1975 96 319 -176 C ATOM 821 C LEU A 100 -6.869 -18.782 11.681 1.00 9.98 C ANISOU 821 C LEU A 100 1370 670 1754 -37 89 -120 C ATOM 822 O LEU A 100 -6.727 -17.758 12.341 1.00 9.70 O ANISOU 822 O LEU A 100 1413 734 1538 -43 63 -98 O ATOM 823 CB LEU A 100 -4.863 -20.185 11.708 1.00 15.26 C ANISOU 823 CB LEU A 100 2252 1248 2299 633 510 32 C ATOM 824 CG LEU A 100 -3.562 -20.642 11.068 1.00 17.12 C ANISOU 824 CG LEU A 100 2190 1815 2500 487 -35 -317 C ATOM 825 CD1 LEU A 100 -2.552 -21.150 12.105 1.00 25.64 C ANISOU 825 CD1 LEU A 100 2898 3579 3265 1539 -485 186 C ATOM 826 CD2 LEU A 100 -3.880 -21.715 10.066 1.00 21.25 C ANISOU 826 CD2 LEU A 100 2934 2273 2867 -29 673 -1100 C ATOM 827 N ASP A 101 -7.968 -19.542 11.743 1.00 10.09 N ANISOU 827 N ASP A 101 1348 733 1754 -73 27 -109 N ATOM 828 CA ASP A 101 -9.127 -19.063 12.489 1.00 10.20 C ANISOU 828 CA ASP A 101 1375 813 1686 -50 13 110 C ATOM 829 C ASP A 101 -8.860 -18.965 13.995 1.00 10.95 C ANISOU 829 C ASP A 101 1592 871 1698 -104 -60 160 C ATOM 830 O ASP A 101 -9.546 -18.229 14.684 1.00 12.81 O ANISOU 830 O ASP A 101 2156 1114 1598 87 272 215 O ATOM 831 CB ASP A 101 -10.342 -19.973 12.265 1.00 11.70 C ANISOU 831 CB ASP A 101 1461 1231 1755 -280 -65 281 C ATOM 832 CG ASP A 101 -10.875 -19.968 10.838 1.00 13.16 C ANISOU 832 CG ASP A 101 1699 1312 1988 -409 -193 232 C ATOM 833 OD1 ASP A 101 -10.462 -19.143 10.012 1.00 12.85 O ANISOU 833 OD1 ASP A 101 1815 1330 1737 -314 0 142 O ATOM 834 OD2 ASP A 101 -11.745 -20.812 10.537 1.00 18.03 O ANISOU 834 OD2 ASP A 101 2294 1906 2651 -1020 -370 100 O ATOM 835 N GLY A 102 -7.862 -19.703 14.492 1.00 11.64 N ANISOU 835 N GLY A 102 1698 873 1850 -341 -314 345 N ATOM 836 CA GLY A 102 -7.547 -19.702 15.914 1.00 13.90 C ANISOU 836 CA GLY A 102 2110 1344 1825 -643 -395 550 C ATOM 837 C GLY A 102 -6.723 -18.528 16.439 1.00 11.43 C ANISOU 837 C GLY A 102 1760 1053 1530 -288 -95 307 C ATOM 838 O GLY A 102 -6.356 -18.531 17.611 1.00 12.32 O ANISOU 838 O GLY A 102 1872 1364 1444 -263 -93 454 O ATOM 839 N GLN A 103 -6.448 -17.530 15.591 1.00 9.23 N ANISOU 839 N GLN A 103 1402 850 1256 -134 34 164 N ATOM 840 CA GLN A 103 -5.744 -16.347 16.044 1.00 8.04 C ANISOU 840 CA GLN A 103 1155 846 1056 -4 47 69 C ATOM 841 C GLN A 103 -6.151 -15.182 15.151 1.00 7.23 C ANISOU 841 C GLN A 103 1019 757 971 -8 27 2 C ATOM 842 O GLN A 103 -6.709 -15.386 14.076 1.00 8.11 O ANISOU 842 O GLN A 103 1286 802 993 -41 7 -45 O ATOM 843 CB GLN A 103 -4.231 -16.566 16.004 1.00 8.57 C ANISOU 843 CB GLN A 103 1205 955 1096 147 85 90 C ATOM 844 CG GLN A 103 -3.696 -16.794 14.595 1.00 9.95 C ANISOU 844 CG GLN A 103 1504 972 1304 259 386 242 C ATOM 845 CD GLN A 103 -2.333 -17.439 14.591 1.00 13.15 C ANISOU 845 CD GLN A 103 1815 1435 1746 613 626 673 C ATOM 846 OE1 GLN A 103 -2.129 -18.421 15.274 1.00 19.36 O ANISOU 846 OE1 GLN A 103 2671 2223 2463 1292 1245 1404 O ATOM 847 NE2 GLN A 103 -1.400 -16.900 13.812 1.00 12.49 N ANISOU 847 NE2 GLN A 103 1499 1622 1622 512 381 612 N ATOM 848 N GLY A 104 -5.856 -13.966 15.613 1.00 7.01 N ANISOU 848 N GLY A 104 1006 782 875 31 39 -41 N ATOM 849 CA GLY A 104 -6.152 -12.783 14.841 1.00 6.65 C ANISOU 849 CA GLY A 104 976 758 791 3 -3 4 C ATOM 850 C GLY A 104 -6.590 -11.591 15.666 1.00 6.23 C ANISOU 850 C GLY A 104 852 776 740 -53 -76 63 C ATOM 851 O GLY A 104 -6.325 -10.461 15.302 1.00 6.99 O ANISOU 851 O GLY A 104 1013 790 851 -34 4 85 O ATOM 852 N SER A 105 -7.274 -11.849 16.802 1.00 6.12 N ANISOU 852 N SER A 105 889 714 722 -38 -34 -44 N ATOM 853 CA SER A 105 -7.657 -10.742 17.639 1.00 6.27 C ANISOU 853 CA SER A 105 937 704 742 -47 -85 0 C ATOM 854 C SER A 105 -6.455 -10.179 18.409 1.00 5.74 C ANISOU 854 C SER A 105 790 669 722 -68 -20 -13 C ATOM 855 O SER A 105 -5.430 -10.850 18.603 1.00 7.06 O ANISOU 855 O SER A 105 983 782 918 28 -132 -48 O ATOM 856 CB SER A 105 -8.804 -11.097 18.599 1.00 6.37 C ANISOU 856 CB SER A 105 880 749 789 -53 -19 18 C ATOM 857 OG SER A 105 -8.435 -12.047 19.584 1.00 7.03 O ANISOU 857 OG SER A 105 1079 744 849 -60 -8 33 O ATOM 858 N GLU A 106 -6.614 -8.932 18.825 1.00 5.92 N ANISOU 858 N GLU A 106 846 694 708 -30 -13 2 N ATOM 859 CA GLU A 106 -5.613 -8.228 19.614 1.00 5.93 C ANISOU 859 CA GLU A 106 822 736 694 -5 -49 18 C ATOM 860 C GLU A 106 -5.938 -8.409 21.115 1.00 5.76 C ANISOU 860 C GLU A 106 835 677 677 5 -97 25 C ATOM 861 O GLU A 106 -5.150 -8.971 21.879 1.00 6.67 O ANISOU 861 O GLU A 106 947 862 727 62 -118 46 O ATOM 862 CB GLU A 106 -5.551 -6.771 19.187 1.00 6.10 C ANISOU 862 CB GLU A 106 886 746 687 -41 -25 5 C ATOM 863 CG GLU A 106 -5.040 -6.648 17.760 1.00 7.23 C ANISOU 863 CG GLU A 106 1188 789 769 -73 135 0 C ATOM 864 CD GLU A 106 -4.398 -5.319 17.460 1.00 6.25 C ANISOU 864 CD GLU A 106 886 804 687 -9 -83 -10 C ATOM 865 OE1 GLU A 106 -5.021 -4.282 17.762 1.00 6.67 O ANISOU 865 OE1 GLU A 106 856 791 887 21 -53 -33 O ATOM 866 OE2 GLU A 106 -3.260 -5.327 16.906 1.00 7.49 O ANISOU 866 OE2 GLU A 106 958 898 988 68 29 -35 O ATOM 867 N HIS A 107 -7.107 -7.929 21.539 1.00 5.95 N ANISOU 867 N HIS A 107 876 720 666 44 -76 48 N ATOM 868 CA HIS A 107 -7.596 -8.326 22.848 1.00 5.91 C ANISOU 868 CA HIS A 107 841 707 697 21 -44 -1 C ATOM 869 C HIS A 107 -7.866 -9.831 22.868 1.00 6.14 C ANISOU 869 C HIS A 107 891 761 680 74 -38 95 C ATOM 870 O HIS A 107 -8.201 -10.440 21.843 1.00 6.42 O ANISOU 870 O HIS A 107 974 751 715 -36 -118 34 O ATOM 871 CB HIS A 107 -8.835 -7.511 23.219 1.00 6.32 C ANISOU 871 CB HIS A 107 913 766 721 -3 26 5 C ATOM 872 CG HIS A 107 -8.546 -6.062 23.387 1.00 5.72 C ANISOU 872 CG HIS A 107 776 794 602 3 -91 -12 C ATOM 873 ND1 HIS A 107 -8.579 -5.160 22.349 1.00 6.17 N ANISOU 873 ND1 HIS A 107 930 742 671 5 -104 -5 N ATOM 874 CD2 HIS A 107 -8.097 -5.355 24.470 1.00 6.07 C ANISOU 874 CD2 HIS A 107 839 812 654 75 -73 -19 C ATOM 875 CE1 HIS A 107 -8.176 -3.972 22.798 1.00 6.27 C ANISOU 875 CE1 HIS A 107 918 754 709 41 -22 -29 C ATOM 876 NE2 HIS A 107 -7.881 -4.053 24.082 1.00 6.26 N ANISOU 876 NE2 HIS A 107 876 795 706 50 -82 -44 N ATOM 877 N THR A 108 -7.729 -10.403 24.053 1.00 6.45 N ANISOU 877 N THR A 108 991 747 711 -30 2 119 N ATOM 878 CA THR A 108 -8.108 -11.773 24.322 1.00 6.79 C ANISOU 878 CA THR A 108 1065 734 780 21 42 145 C ATOM 879 C THR A 108 -9.062 -11.781 25.526 1.00 6.55 C ANISOU 879 C THR A 108 962 829 698 72 -86 108 C ATOM 880 O THR A 108 -9.109 -10.814 26.295 1.00 7.18 O ANISOU 880 O THR A 108 1070 867 793 38 8 84 O ATOM 881 CB THR A 108 -6.872 -12.688 24.530 1.00 7.29 C ANISOU 881 CB THR A 108 1050 868 854 98 -21 114 C ATOM 882 OG1 THR A 108 -6.038 -12.181 25.573 1.00 7.64 O ANISOU 882 OG1 THR A 108 1053 977 874 127 -46 125 O ATOM 883 CG2 THR A 108 -6.069 -12.735 23.247 1.00 8.08 C ANISOU 883 CG2 THR A 108 1122 1021 928 150 79 14 C ATOM 884 N VAL A 109 -9.832 -12.856 25.651 1.00 7.21 N ANISOU 884 N VAL A 109 1061 863 817 -12 22 128 N ATOM 885 CA VAL A 109 -10.827 -12.968 26.736 1.00 7.60 C ANISOU 885 CA VAL A 109 1046 989 852 6 69 187 C ATOM 886 C VAL A 109 -10.507 -14.270 27.467 1.00 7.75 C ANISOU 886 C VAL A 109 1110 976 858 -46 63 149 C ATOM 887 O VAL A 109 -10.628 -15.361 26.897 1.00 8.44 O ANISOU 887 O VAL A 109 1268 926 1011 -23 75 188 O ATOM 888 CB VAL A 109 -12.266 -12.977 26.176 1.00 8.64 C ANISOU 888 CB VAL A 109 1055 1183 1045 12 -41 267 C ATOM 889 CG1 VAL A 109 -13.282 -13.112 27.316 1.00 9.75 C ANISOU 889 CG1 VAL A 109 1068 1425 1214 26 103 359 C ATOM 890 CG2 VAL A 109 -12.537 -11.722 25.365 1.00 9.02 C ANISOU 890 CG2 VAL A 109 1250 1104 1072 65 -50 323 C ATOM 891 N ASP A 110 -10.008 -14.156 28.688 1.00 8.21 N ANISOU 891 N ASP A 110 1294 989 836 79 134 283 N ATOM 892 CA ASP A 110 -9.534 -15.349 29.400 1.00 9.16 C ANISOU 892 CA ASP A 110 1392 1075 1014 134 138 375 C ATOM 893 C ASP A 110 -8.548 -16.147 28.540 1.00 9.23 C ANISOU 893 C ASP A 110 1432 1003 1074 169 136 370 C ATOM 894 O ASP A 110 -8.588 -17.381 28.485 1.00 10.67 O ANISOU 894 O ASP A 110 1646 1090 1317 195 248 407 O ATOM 895 CB ASP A 110 -10.709 -16.215 29.883 1.00 10.35 C ANISOU 895 CB ASP A 110 1566 1164 1202 80 293 423 C ATOM 896 CG ASP A 110 -11.579 -15.489 30.893 1.00 10.89 C ANISOU 896 CG ASP A 110 1584 1345 1207 -14 233 444 C ATOM 897 OD1 ASP A 110 -11.049 -14.598 31.596 1.00 11.00 O ANISOU 897 OD1 ASP A 110 1479 1386 1312 157 237 329 O ATOM 898 OD2 ASP A 110 -12.763 -15.832 30.998 1.00 12.87 O ANISOU 898 OD2 ASP A 110 1565 1981 1343 -24 235 303 O ATOM 899 N LYS A 111 -7.670 -15.386 27.878 1.00 8.76 N ANISOU 899 N LYS A 111 1228 1078 1023 174 40 278 N ATOM 900 CA LYS A 111 -6.609 -15.902 26.992 1.00 9.48 C ANISOU 900 CA LYS A 111 1383 1081 1140 314 116 248 C ATOM 901 C LYS A 111 -7.106 -16.419 25.640 1.00 9.47 C ANISOU 901 C LYS A 111 1549 944 1105 211 149 223 C ATOM 902 O LYS A 111 -6.301 -16.774 24.788 1.00 10.93 O ANISOU 902 O LYS A 111 1705 1202 1247 314 333 149 O ATOM 903 CB LYS A 111 -5.688 -16.910 27.695 1.00 12.36 C ANISOU 903 CB LYS A 111 1751 1440 1507 639 -30 308 C ATOM 904 CG LYS A 111 -4.969 -16.338 28.924 1.00 15.16 C ANISOU 904 CG LYS A 111 2104 1784 1871 793 -387 188 C ATOM 905 CD LYS A 111 -4.095 -15.131 28.572 1.00 19.18 C ANISOU 905 CD LYS A 111 2406 2462 2419 277 -344 -325 C ATOM 906 CE LYS A 111 -3.377 -14.542 29.787 1.00 21.93 C ANISOU 906 CE LYS A 111 2460 3059 2815 523 -964 -183 C ATOM 907 NZ LYS A 111 -2.208 -15.339 30.208 1.00 27.76 N ANISOU 907 NZ LYS A 111 3123 3808 3618 1392 -1085 -165 N ATOM 908 N LYS A 112 -8.420 -16.431 25.417 1.00 9.09 N ANISOU 908 N LYS A 112 1508 868 1079 95 184 184 N ATOM 909 CA LYS A 112 -8.979 -16.849 24.133 1.00 9.74 C ANISOU 909 CA LYS A 112 1545 1016 1141 -84 120 169 C ATOM 910 C LYS A 112 -8.718 -15.797 23.067 1.00 8.14 C ANISOU 910 C LYS A 112 1196 843 1055 5 -47 124 C ATOM 911 O LYS A 112 -9.028 -14.627 23.261 1.00 8.10 O ANISOU 911 O LYS A 112 1240 772 1066 -3 41 41 O ATOM 912 CB LYS A 112 -10.500 -17.054 24.237 1.00 12.41 C ANISOU 912 CB LYS A 112 1717 1549 1451 -593 299 -196 C ATOM 913 CG LYS A 112 -11.174 -17.429 22.899 1.00 14.13 C ANISOU 913 CG LYS A 112 1771 1874 1722 -646 215 -557 C ATOM 914 CD LYS A 112 -12.701 -17.382 22.972 1.00 18.52 C ANISOU 914 CD LYS A 112 2044 3039 1953 35 -139 -240 C ATOM 915 CE LYS A 112 -13.333 -17.592 21.609 1.00 19.77 C ANISOU 915 CE LYS A 112 2652 2720 2139 413 -433 -290 C ATOM 916 NZ LYS A 112 -13.117 -18.954 21.098 1.00 22.73 N ANISOU 916 NZ LYS A 112 3588 2605 2445 616 -502 -78 N ATOM 917 N LYS A 113 -8.180 -16.253 21.934 1.00 8.31 N ANISOU 917 N LYS A 113 1344 830 985 204 63 136 N ATOM 918 CA LYS A 113 -8.005 -15.447 20.729 1.00 8.18 C ANISOU 918 CA LYS A 113 1246 909 953 137 -65 141 C ATOM 919 C LYS A 113 -9.160 -15.712 19.777 1.00 8.36 C ANISOU 919 C LYS A 113 1352 725 1100 33 -54 146 C ATOM 920 O LYS A 113 -9.499 -16.869 19.493 1.00 10.63 O ANISOU 920 O LYS A 113 1805 764 1471 98 -309 103 O ATOM 921 CB LYS A 113 -6.703 -15.823 20.020 1.00 9.24 C ANISOU 921 CB LYS A 113 1318 1207 988 225 -16 79 C ATOM 922 CG LYS A 113 -5.444 -15.480 20.808 1.00 9.74 C ANISOU 922 CG LYS A 113 1213 1334 1155 242 52 109 C ATOM 923 CD LYS A 113 -4.201 -16.035 20.128 1.00 11.26 C ANISOU 923 CD LYS A 113 1280 1334 1663 263 -30 56 C ATOM 924 CE LYS A 113 -2.934 -15.459 20.721 1.00 16.35 C ANISOU 924 CE LYS A 113 1585 2074 2555 154 -693 65 C ATOM 925 NZ LYS A 113 -2.477 -16.267 21.851 1.00 23.96 N ANISOU 925 NZ LYS A 113 3080 2367 3656 377 -2094 -40 N ATOM 926 N TYR A 114 -9.738 -14.633 19.271 1.00 7.23 N ANISOU 926 N TYR A 114 1029 740 979 6 -24 123 N ATOM 927 CA TYR A 114 -10.741 -14.721 18.220 1.00 7.03 C ANISOU 927 CA TYR A 114 966 723 982 -81 -11 76 C ATOM 928 C TYR A 114 -10.059 -14.665 16.843 1.00 6.94 C ANISOU 928 C TYR A 114 1028 631 977 -68 -61 37 C ATOM 929 O TYR A 114 -8.881 -14.338 16.721 1.00 7.81 O ANISOU 929 O TYR A 114 1110 821 1038 -45 11 7 O ATOM 930 CB TYR A 114 -11.796 -13.605 18.384 1.00 6.98 C ANISOU 930 CB TYR A 114 875 754 1024 -9 6 88 C ATOM 931 CG TYR A 114 -12.752 -13.840 19.534 1.00 7.63 C ANISOU 931 CG TYR A 114 1074 786 1040 80 3 138 C ATOM 932 CD1 TYR A 114 -13.962 -14.480 19.306 1.00 8.71 C ANISOU 932 CD1 TYR A 114 1034 955 1319 -58 117 121 C ATOM 933 CD2 TYR A 114 -12.468 -13.416 20.820 1.00 9.16 C ANISOU 933 CD2 TYR A 114 1560 909 1010 192 48 87 C ATOM 934 CE1 TYR A 114 -14.880 -14.689 20.341 1.00 10.83 C ANISOU 934 CE1 TYR A 114 1400 1192 1524 4 372 142 C ATOM 935 CE2 TYR A 114 -13.388 -13.621 21.867 1.00 10.93 C ANISOU 935 CE2 TYR A 114 1669 1298 1186 432 193 92 C ATOM 936 CZ TYR A 114 -14.578 -14.258 21.617 1.00 12.50 C ANISOU 936 CZ TYR A 114 1530 1782 1440 406 382 299 C ATOM 937 OH TYR A 114 -15.454 -14.448 22.667 1.00 17.29 O ANISOU 937 OH TYR A 114 2173 2547 1849 357 936 473 O ATOM 938 N ALA A 115 -10.839 -14.950 15.802 1.00 7.06 N ANISOU 938 N ALA A 115 1011 686 986 -107 -28 18 N ATOM 939 CA ALA A 115 -10.318 -14.966 14.437 1.00 7.06 C ANISOU 939 CA ALA A 115 1019 664 999 -65 -51 -40 C ATOM 940 C ALA A 115 -9.937 -13.568 13.935 1.00 6.87 C ANISOU 940 C ALA A 115 1061 677 871 -10 -61 -16 C ATOM 941 O ALA A 115 -9.088 -13.432 13.042 1.00 7.40 O ANISOU 941 O ALA A 115 1078 720 1013 -33 -2 -41 O ATOM 942 CB ALA A 115 -11.340 -15.603 13.499 1.00 7.96 C ANISOU 942 CB ALA A 115 1074 841 1109 -142 -93 -78 C ATOM 943 N ALA A 116 -10.590 -12.547 14.466 1.00 6.67 N ANISOU 943 N ALA A 116 1018 635 882 -17 -26 -16 N ATOM 944 CA ALA A 116 -10.316 -11.187 14.025 1.00 6.37 C ANISOU 944 CA ALA A 116 982 645 793 -2 -12 -6 C ATOM 945 C ALA A 116 -10.922 -10.234 15.054 1.00 5.96 C ANISOU 945 C ALA A 116 889 648 726 13 -62 118 C ATOM 946 O ALA A 116 -11.649 -10.640 15.971 1.00 6.44 O ANISOU 946 O ALA A 116 938 685 824 -11 -2 13 O ATOM 947 CB ALA A 116 -10.860 -10.929 12.626 1.00 6.65 C ANISOU 947 CB ALA A 116 931 810 785 -57 34 4 C ATOM 948 N GLU A 117 -10.599 -8.952 14.879 1.00 5.88 N ANISOU 948 N GLU A 117 893 601 740 25 -36 -2 N ATOM 949 CA GLU A 117 -11.108 -7.911 15.760 1.00 5.84 C ANISOU 949 CA GLU A 117 902 626 691 34 -19 29 C ATOM 950 C GLU A 117 -11.297 -6.647 14.928 1.00 5.72 C ANISOU 950 C GLU A 117 883 644 646 39 -39 31 C ATOM 951 O GLU A 117 -10.393 -6.229 14.193 1.00 6.95 O ANISOU 951 O GLU A 117 924 828 889 61 44 216 O ATOM 952 CB GLU A 117 -10.128 -7.675 16.910 1.00 6.14 C ANISOU 952 CB GLU A 117 912 720 701 38 -50 65 C ATOM 953 CG GLU A 117 -10.613 -6.685 17.975 1.00 6.34 C ANISOU 953 CG GLU A 117 943 755 712 61 -110 24 C ATOM 954 CD GLU A 117 -9.682 -6.624 19.189 1.00 6.09 C ANISOU 954 CD GLU A 117 846 762 704 19 -7 36 C ATOM 955 OE1 GLU A 117 -9.055 -7.655 19.507 1.00 6.87 O ANISOU 955 OE1 GLU A 117 935 887 788 75 -105 58 O ATOM 956 OE2 GLU A 117 -9.609 -5.543 19.821 1.00 7.02 O ANISOU 956 OE2 GLU A 117 1155 837 677 -3 -138 24 O ATOM 957 N LEU A 118 -12.482 -6.044 15.061 1.00 5.60 N ANISOU 957 N LEU A 118 879 616 634 -18 -80 5 N ATOM 958 CA LEU A 118 -12.865 -4.789 14.427 1.00 5.39 C ANISOU 958 CA LEU A 118 790 612 648 27 -101 36 C ATOM 959 C LEU A 118 -12.646 -3.643 15.396 1.00 5.27 C ANISOU 959 C LEU A 118 830 595 575 76 -61 85 C ATOM 960 O LEU A 118 -13.049 -3.728 16.561 1.00 5.59 O ANISOU 960 O LEU A 118 856 666 603 -22 -30 6 O ATOM 961 CB LEU A 118 -14.363 -4.887 14.053 1.00 6.13 C ANISOU 961 CB LEU A 118 841 754 733 4 -109 -11 C ATOM 962 CG LEU A 118 -15.118 -3.611 13.681 1.00 6.55 C ANISOU 962 CG LEU A 118 815 871 803 26 -215 59 C ATOM 963 CD1 LEU A 118 -14.514 -2.936 12.456 1.00 6.70 C ANISOU 963 CD1 LEU A 118 958 792 797 -40 -158 74 C ATOM 964 CD2 LEU A 118 -16.588 -3.981 13.425 1.00 7.70 C ANISOU 964 CD2 LEU A 118 841 1070 1013 -12 -245 105 C ATOM 965 N HIS A 119 -12.007 -2.579 14.904 1.00 5.23 N ANISOU 965 N HIS A 119 778 621 589 14 -70 2 N ATOM 966 CA HIS A 119 -11.770 -1.354 15.657 1.00 5.23 C ANISOU 966 CA HIS A 119 773 624 592 27 -60 -3 C ATOM 967 C HIS A 119 -12.476 -0.188 14.962 1.00 5.16 C ANISOU 967 C HIS A 119 803 554 604 34 -135 17 C ATOM 968 O HIS A 119 -12.107 0.175 13.843 1.00 6.11 O ANISOU 968 O HIS A 119 955 755 611 106 -29 79 O ATOM 969 CB HIS A 119 -10.277 -1.025 15.754 1.00 5.46 C ANISOU 969 CB HIS A 119 692 687 696 15 -108 29 C ATOM 970 CG HIS A 119 -9.561 -1.995 16.627 1.00 5.50 C ANISOU 970 CG HIS A 119 716 721 653 73 -125 -64 C ATOM 971 ND1 HIS A 119 -8.183 -2.179 16.617 1.00 5.96 N ANISOU 971 ND1 HIS A 119 924 690 652 31 -125 -24 N ATOM 972 CD2 HIS A 119 -10.070 -2.844 17.569 1.00 5.67 C ANISOU 972 CD2 HIS A 119 820 733 601 29 -118 32 C ATOM 973 CE1 HIS A 119 -7.903 -3.111 17.520 1.00 5.93 C ANISOU 973 CE1 HIS A 119 833 768 651 -7 -102 -7 C ATOM 974 NE2 HIS A 119 -9.018 -3.531 18.108 1.00 6.15 N ANISOU 974 NE2 HIS A 119 853 834 648 49 -157 39 N ATOM 975 N LEU A 120 -13.485 0.383 15.627 1.00 5.59 N ANISOU 975 N LEU A 120 842 597 686 2 -97 17 N ATOM 976 CA LEU A 120 -14.152 1.605 15.181 1.00 5.72 C ANISOU 976 CA LEU A 120 837 656 682 63 -100 -28 C ATOM 977 C LEU A 120 -13.533 2.754 15.984 1.00 5.25 C ANISOU 977 C LEU A 120 783 590 620 72 -93 52 C ATOM 978 O LEU A 120 -13.653 2.806 17.210 1.00 5.87 O ANISOU 978 O LEU A 120 863 703 664 -13 -101 31 O ATOM 979 CB LEU A 120 -15.677 1.509 15.395 1.00 6.49 C ANISOU 979 CB LEU A 120 757 813 896 34 -150 -49 C ATOM 980 CG LEU A 120 -16.359 0.439 14.526 1.00 7.23 C ANISOU 980 CG LEU A 120 982 853 913 -123 -146 -50 C ATOM 981 CD1 LEU A 120 -17.179 -0.487 15.379 1.00 10.89 C ANISOU 981 CD1 LEU A 120 1848 1123 1168 -639 157 -77 C ATOM 982 CD2 LEU A 120 -17.206 1.094 13.450 1.00 8.87 C ANISOU 982 CD2 LEU A 120 973 1312 1085 9 -351 -125 C ATOM 983 N VAL A 121 -12.824 3.622 15.273 1.00 5.94 N ANISOU 983 N VAL A 121 916 669 671 -58 -70 -2 N ATOM 984 CA VAL A 121 -11.977 4.636 15.904 1.00 5.84 C ANISOU 984 CA VAL A 121 897 649 672 0 -36 49 C ATOM 985 C VAL A 121 -12.668 5.994 15.903 1.00 5.96 C ANISOU 985 C VAL A 121 863 664 738 -30 -43 24 C ATOM 986 O VAL A 121 -13.110 6.460 14.850 1.00 6.93 O ANISOU 986 O VAL A 121 1143 740 750 94 -128 18 O ATOM 987 CB VAL A 121 -10.625 4.740 15.126 1.00 6.65 C ANISOU 987 CB VAL A 121 917 745 865 -47 3 6 C ATOM 988 CG1 VAL A 121 -9.715 5.782 15.770 1.00 7.40 C ANISOU 988 CG1 VAL A 121 911 906 994 -112 30 -20 C ATOM 989 CG2 VAL A 121 -9.918 3.383 15.066 1.00 7.27 C ANISOU 989 CG2 VAL A 121 960 800 1004 19 69 -17 C ATOM 990 N HIS A 122 -12.745 6.612 17.086 1.00 6.02 N ANISOU 990 N HIS A 122 896 600 790 -13 -97 -53 N ATOM 991 CA HIS A 122 -13.449 7.886 17.254 1.00 6.39 C ANISOU 991 CA HIS A 122 888 676 864 0 -60 -46 C ATOM 992 C HIS A 122 -12.546 8.862 18.021 1.00 6.22 C ANISOU 992 C HIS A 122 810 699 852 5 -89 -78 C ATOM 993 O HIS A 122 -11.802 8.440 18.910 1.00 7.10 O ANISOU 993 O HIS A 122 1066 728 903 -91 -208 59 O ATOM 994 CB HIS A 122 -14.741 7.709 18.095 1.00 6.51 C ANISOU 994 CB HIS A 122 827 706 942 20 -46 -48 C ATOM 995 CG HIS A 122 -15.631 6.574 17.675 1.00 6.45 C ANISOU 995 CG HIS A 122 777 730 943 52 -67 -45 C ATOM 996 ND1 HIS A 122 -15.321 5.266 17.941 1.00 6.92 N ANISOU 996 ND1 HIS A 122 850 738 1043 10 -53 -29 N ATOM 997 CD2 HIS A 122 -16.835 6.548 17.048 1.00 7.22 C ANISOU 997 CD2 HIS A 122 910 859 975 15 -60 15 C ATOM 998 CE1 HIS A 122 -16.310 4.490 17.505 1.00 7.00 C ANISOU 998 CE1 HIS A 122 773 834 1051 -6 1 -64 C ATOM 999 NE2 HIS A 122 -17.246 5.238 16.953 1.00 7.64 N ANISOU 999 NE2 HIS A 122 883 940 1079 -84 -79 -75 N ATOM 1000 N TRP A 123 -12.645 10.157 17.704 1.00 6.55 N ANISOU 1000 N TRP A 123 888 653 947 15 -69 -114 N ATOM 1001 CA TRP A 123 -11.852 11.163 18.404 1.00 6.66 C ANISOU 1001 CA TRP A 123 896 653 983 -39 -71 -82 C ATOM 1002 C TRP A 123 -12.761 12.178 19.126 1.00 6.99 C ANISOU 1002 C TRP A 123 987 631 1039 -53 -82 -56 C ATOM 1003 O TRP A 123 -13.853 12.522 18.669 1.00 7.72 O ANISOU 1003 O TRP A 123 958 779 1197 63 -154 -120 O ATOM 1004 CB TRP A 123 -10.834 11.847 17.467 1.00 8.10 C ANISOU 1004 CB TRP A 123 1039 980 1059 -145 -55 -100 C ATOM 1005 CG TRP A 123 -11.422 12.497 16.251 1.00 8.43 C ANISOU 1005 CG TRP A 123 1324 785 1095 -213 -29 -59 C ATOM 1006 CD1 TRP A 123 -11.640 11.907 15.045 1.00 8.96 C ANISOU 1006 CD1 TRP A 123 1463 812 1131 -143 -79 -79 C ATOM 1007 CD2 TRP A 123 -11.853 13.857 16.121 1.00 9.31 C ANISOU 1007 CD2 TRP A 123 1587 739 1212 -229 -24 -27 C ATOM 1008 NE1 TRP A 123 -12.197 12.797 14.170 1.00 9.83 N ANISOU 1008 NE1 TRP A 123 1764 781 1191 -144 -149 -15 N ATOM 1009 CE2 TRP A 123 -12.323 14.010 14.804 1.00 10.41 C ANISOU 1009 CE2 TRP A 123 1991 703 1261 -210 -163 -60 C ATOM 1010 CE3 TRP A 123 -11.869 14.962 16.979 1.00 10.30 C ANISOU 1010 CE3 TRP A 123 1815 788 1311 -300 84 -80 C ATOM 1011 CZ2 TRP A 123 -12.829 15.212 14.329 1.00 12.14 C ANISOU 1011 CZ2 TRP A 123 2433 738 1440 -177 -133 22 C ATOM 1012 CZ3 TRP A 123 -12.368 16.162 16.493 1.00 11.90 C ANISOU 1012 CZ3 TRP A 123 2337 752 1434 -247 219 -92 C ATOM 1013 CH2 TRP A 123 -12.838 16.275 15.190 1.00 12.29 C ANISOU 1013 CH2 TRP A 123 2412 750 1508 -152 1 27 C ATOM 1014 N ASN A 124 -12.231 12.663 20.244 1.00 7.31 N ANISOU 1014 N ASN A 124 991 706 1080 26 -154 -161 N ATOM 1015 CA ASN A 124 -12.955 13.550 21.147 1.00 7.57 C ANISOU 1015 CA ASN A 124 1089 680 1106 24 -63 -217 C ATOM 1016 C ASN A 124 -13.059 14.936 20.528 1.00 8.20 C ANISOU 1016 C ASN A 124 1151 735 1230 62 -123 -199 C ATOM 1017 O ASN A 124 -12.046 15.590 20.291 1.00 8.21 O ANISOU 1017 O ASN A 124 1182 691 1247 33 -58 -224 O ATOM 1018 CB ASN A 124 -12.178 13.600 22.456 1.00 8.27 C ANISOU 1018 CB ASN A 124 1217 840 1084 0 1 -156 C ATOM 1019 CG ASN A 124 -12.943 14.248 23.572 1.00 8.70 C ANISOU 1019 CG ASN A 124 1317 827 1162 -39 117 -178 C ATOM 1020 OD1 ASN A 124 -13.768 15.137 23.352 1.00 9.50 O ANISOU 1020 OD1 ASN A 124 1289 983 1336 45 146 -253 O ATOM 1021 ND2 ASN A 124 -12.661 13.815 24.786 1.00 10.01 N ANISOU 1021 ND2 ASN A 124 1545 1066 1191 41 155 -194 N ATOM 1022 N THR A 125 -14.286 15.400 20.279 1.00 9.00 N ANISOU 1022 N THR A 125 1211 815 1395 179 -183 -209 N ATOM 1023 CA THR A 125 -14.482 16.642 19.552 1.00 10.48 C ANISOU 1023 CA THR A 125 1367 884 1730 219 -294 -105 C ATOM 1024 C THR A 125 -13.945 17.855 20.296 1.00 10.36 C ANISOU 1024 C THR A 125 1351 799 1787 140 -144 -76 C ATOM 1025 O THR A 125 -13.730 18.890 19.684 1.00 11.49 O ANISOU 1025 O THR A 125 1423 956 1986 98 -95 70 O ATOM 1026 CB THR A 125 -15.959 16.852 19.158 1.00 13.73 C ANISOU 1026 CB THR A 125 1644 1327 2246 286 -683 -70 C ATOM 1027 OG1 THR A 125 -16.752 16.890 20.343 1.00 15.21 O ANISOU 1027 OG1 THR A 125 1470 1337 2971 351 -222 -337 O ATOM 1028 CG2 THR A 125 -16.435 15.722 18.227 1.00 15.34 C ANISOU 1028 CG2 THR A 125 2014 1544 2269 150 -967 -90 C ATOM 1029 N LYS A 127 -13.723 17.743 21.604 1.00 10.23 N ANISOU 1029 N LYS A 127 1424 791 1672 79 43 -336 N ATOM 1030 CA LYS A 127 -13.175 18.885 22.332 1.00 11.92 C ANISOU 1030 CA LYS A 127 1697 1042 1788 -125 282 -571 C ATOM 1031 C LYS A 127 -11.740 19.242 21.887 1.00 10.36 C ANISOU 1031 C LYS A 127 1569 716 1651 9 88 -363 C ATOM 1032 O LYS A 127 -11.285 20.336 22.186 1.00 12.73 O ANISOU 1032 O LYS A 127 1954 803 2078 -205 352 -593 O ATOM 1033 CB LYS A 127 -13.277 18.694 23.833 1.00 14.74 C ANISOU 1033 CB LYS A 127 2079 1638 1882 -468 267 -605 C ATOM 1034 CG LYS A 127 -12.249 17.805 24.457 1.00 15.72 C ANISOU 1034 CG LYS A 127 2259 1809 1905 -475 116 -588 C ATOM 1035 CD LYS A 127 -12.691 17.552 25.890 1.00 21.27 C ANISOU 1035 CD LYS A 127 2703 2973 2406 -638 -11 -385 C ATOM 1036 CE LYS A 127 -11.574 17.075 26.765 1.00 31.47 C ANISOU 1036 CE LYS A 127 2887 4535 4536 -673 -950 608 C ATOM 1037 NZ LYS A 127 -11.334 15.626 26.601 1.00 56.82 N ANISOU 1037 NZ LYS A 127 7548 5314 8728 372 -2475 1953 N ATOM 1038 N TYR A 128 -11.067 18.335 21.172 1.00 8.78 N ANISOU 1038 N TYR A 128 1374 710 1251 -7 -23 -190 N ATOM 1039 CA TYR A 128 -9.718 18.580 20.677 1.00 9.06 C ANISOU 1039 CA TYR A 128 1362 813 1266 -90 -62 -174 C ATOM 1040 C TYR A 128 -9.645 18.996 19.215 1.00 9.36 C ANISOU 1040 C TYR A 128 1398 822 1335 -104 -26 -151 C ATOM 1041 O TYR A 128 -8.553 19.232 18.699 1.00 10.35 O ANISOU 1041 O TYR A 128 1456 1033 1442 -26 65 -70 O ATOM 1042 CB TYR A 128 -8.798 17.397 20.971 1.00 9.41 C ANISOU 1042 CB TYR A 128 1411 799 1366 -41 -42 -180 C ATOM 1043 CG TYR A 128 -8.753 17.072 22.442 1.00 9.11 C ANISOU 1043 CG TYR A 128 1216 892 1354 38 -97 -206 C ATOM 1044 CD1 TYR A 128 -8.384 18.042 23.375 1.00 10.31 C ANISOU 1044 CD1 TYR A 128 1501 1033 1384 0 -222 -245 C ATOM 1045 CD2 TYR A 128 -9.086 15.814 22.916 1.00 8.86 C ANISOU 1045 CD2 TYR A 128 1174 943 1248 125 -71 -156 C ATOM 1046 CE1 TYR A 128 -8.362 17.756 24.733 1.00 10.86 C ANISOU 1046 CE1 TYR A 128 1743 1065 1319 105 -254 -301 C ATOM 1047 CE2 TYR A 128 -9.071 15.516 24.266 1.00 9.46 C ANISOU 1047 CE2 TYR A 128 1359 1025 1211 201 -69 -220 C ATOM 1048 CZ TYR A 128 -8.693 16.492 25.174 1.00 10.74 C ANISOU 1048 CZ TYR A 128 1729 1097 1255 235 -133 -253 C ATOM 1049 OH TYR A 128 -8.668 16.253 26.532 1.00 12.65 O ANISOU 1049 OH TYR A 128 2182 1417 1207 288 -103 -391 O ATOM 1050 N GLY A 129 -10.789 19.096 18.538 1.00 9.30 N ANISOU 1050 N GLY A 129 1437 828 1269 -75 -36 -73 N ATOM 1051 CA GLY A 129 -10.807 19.772 17.238 1.00 10.17 C ANISOU 1051 CA GLY A 129 1658 865 1342 53 100 90 C ATOM 1052 C GLY A 129 -10.438 18.939 16.015 1.00 10.02 C ANISOU 1052 C GLY A 129 1689 870 1248 26 -95 155 C ATOM 1053 O GLY A 129 -11.074 19.070 14.971 1.00 10.97 O ANISOU 1053 O GLY A 129 1864 930 1375 77 -227 224 O ATOM 1054 N AASP A 130 -9.334 18.176 16.101 0.62 10.45 N ANISOU 1054 N AASP A 130 1681 985 1303 204 28 132 N ATOM 1055 N BASP A 130 -9.494 18.030 16.151 0.38 9.67 N ANISOU 1055 N BASP A 130 1737 840 1098 127 41 118 N ATOM 1056 CA AASP A 130 -8.854 17.305 15.008 0.62 10.17 C ANISOU 1056 CA AASP A 130 1781 940 1143 164 -89 135 C ATOM 1057 CA BASP A 130 -9.335 17.040 15.108 0.38 9.54 C ANISOU 1057 CA BASP A 130 1822 784 1020 -19 111 151 C ATOM 1058 C AASP A 130 -8.167 16.036 15.562 0.62 9.40 C ANISOU 1058 C AASP A 130 1624 917 1032 136 -130 45 C ATOM 1059 C BASP A 130 -8.548 15.883 15.659 0.38 9.11 C ANISOU 1059 C BASP A 130 1725 799 938 -12 62 2 C ATOM 1060 O AASP A 130 -7.647 16.045 16.693 0.62 7.83 O ANISOU 1060 O AASP A 130 1038 897 1042 11 -45 11 O ATOM 1061 O BASP A 130 -8.236 15.852 16.835 0.38 7.04 O ANISOU 1061 O BASP A 130 995 766 915 -87 67 86 O ATOM 1062 CB AASP A 130 -7.985 18.061 13.965 0.62 10.64 C ANISOU 1062 CB AASP A 130 1630 1183 1229 299 -104 235 C ATOM 1063 CB BASP A 130 -8.674 17.634 13.855 0.38 10.72 C ANISOU 1063 CB BASP A 130 1938 1076 1058 -107 153 256 C ATOM 1064 CG AASP A 130 -6.584 18.444 14.471 0.62 11.40 C ANISOU 1064 CG AASP A 130 1644 1136 1550 292 -154 182 C ATOM 1065 CG BASP A 130 -7.294 18.195 14.122 0.38 10.67 C ANISOU 1065 CG BASP A 130 1891 902 1262 38 186 363 C ATOM 1066 OD1AASP A 130 -5.761 17.551 14.731 0.62 11.73 O ANISOU 1066 OD1AASP A 130 1764 1179 1512 243 -206 253 O ATOM 1067 OD1BASP A 130 -6.748 18.907 13.245 0.38 12.03 O ANISOU 1067 OD1BASP A 130 2341 939 1290 -229 475 202 O ATOM 1068 OD2AASP A 130 -6.283 19.652 14.534 0.62 13.72 O ANISOU 1068 OD2AASP A 130 1759 1138 2316 207 -175 529 O ATOM 1069 OD2BASP A 130 -6.751 17.922 15.214 0.38 11.72 O ANISOU 1069 OD2BASP A 130 1763 1256 1434 -33 96 428 O ATOM 1070 N PHE A 131 -8.226 14.942 14.790 1.00 10.29 N ANISOU 1070 N PHE A 131 1976 945 987 215 11 44 N ATOM 1071 CA PHE A 131 -7.645 13.679 15.201 1.00 9.19 C ANISOU 1071 CA PHE A 131 1642 898 951 147 -103 -15 C ATOM 1072 C PHE A 131 -6.185 13.840 15.650 1.00 8.73 C ANISOU 1072 C PHE A 131 1581 822 915 -113 1 3 C ATOM 1073 O PHE A 131 -5.765 13.251 16.646 1.00 8.63 O ANISOU 1073 O PHE A 131 1480 871 926 -136 29 -5 O ATOM 1074 CB PHE A 131 -7.772 12.681 14.057 1.00 9.48 C ANISOU 1074 CB PHE A 131 1585 1005 1013 62 -111 -123 C ATOM 1075 CG PHE A 131 -7.175 11.338 14.345 1.00 9.17 C ANISOU 1075 CG PHE A 131 1461 925 1098 -58 -8 -197 C ATOM 1076 CD1 PHE A 131 -7.902 10.352 14.999 1.00 9.76 C ANISOU 1076 CD1 PHE A 131 1556 1006 1147 -205 -112 -143 C ATOM 1077 CD2 PHE A 131 -5.875 11.034 13.959 1.00 11.23 C ANISOU 1077 CD2 PHE A 131 1633 1205 1429 116 177 -198 C ATOM 1078 CE1 PHE A 131 -7.352 9.109 15.263 1.00 11.48 C ANISOU 1078 CE1 PHE A 131 1918 1066 1377 -199 -110 -221 C ATOM 1079 CE2 PHE A 131 -5.325 9.789 14.222 1.00 13.29 C ANISOU 1079 CE2 PHE A 131 1906 1416 1729 346 268 -140 C ATOM 1080 CZ PHE A 131 -6.064 8.832 14.884 1.00 12.69 C ANISOU 1080 CZ PHE A 131 2037 1231 1555 129 -25 -216 C ATOM 1081 N GLY A 132 -5.401 14.611 14.892 1.00 9.93 N ANISOU 1081 N GLY A 132 1754 1006 1013 -177 128 14 N ATOM 1082 CA GLY A 132 -3.995 14.780 15.217 1.00 10.81 C ANISOU 1082 CA GLY A 132 1697 1221 1191 -377 277 36 C ATOM 1083 C GLY A 132 -3.746 15.404 16.581 1.00 9.96 C ANISOU 1083 C GLY A 132 1536 1037 1212 -291 260 70 C ATOM 1084 O GLY A 132 -2.781 15.067 17.277 1.00 10.83 O ANISOU 1084 O GLY A 132 1480 1231 1404 -164 130 -93 O ATOM 1085 N ALYS A 133 -4.608 16.342 16.977 0.65 9.61 N ANISOU 1085 N ALYS A 133 1521 944 1186 -283 189 60 N ATOM 1086 N BLYS A 133 -4.618 16.328 16.968 0.35 9.45 N ANISOU 1086 N BLYS A 133 1503 925 1163 -285 208 61 N ATOM 1087 CA ALYS A 133 -4.522 16.912 18.318 0.65 9.33 C ANISOU 1087 CA ALYS A 133 1401 958 1186 -213 122 29 C ATOM 1088 CA BLYS A 133 -4.533 16.910 18.295 0.35 9.21 C ANISOU 1088 CA BLYS A 133 1384 949 1168 -218 129 24 C ATOM 1089 C ALYS A 133 -5.049 15.914 19.360 0.65 8.17 C ANISOU 1089 C ALYS A 133 1206 882 1014 -205 47 -58 C ATOM 1090 C BLYS A 133 -5.054 15.925 19.350 0.35 8.10 C ANISOU 1090 C BLYS A 133 1192 876 1010 -213 52 -56 C ATOM 1091 O ALYS A 133 -4.506 15.803 20.456 0.65 9.03 O ANISOU 1091 O ALYS A 133 1271 1119 1039 -330 -19 -83 O ATOM 1092 O BLYS A 133 -4.502 15.833 20.445 0.35 8.88 O ANISOU 1092 O BLYS A 133 1240 1112 1022 -329 -2 -86 O ATOM 1093 CB ALYS A 133 -5.300 18.220 18.398 0.65 11.10 C ANISOU 1093 CB ALYS A 133 1626 976 1617 -180 78 55 C ATOM 1094 CB BLYS A 133 -5.318 18.213 18.362 0.35 11.05 C ANISOU 1094 CB BLYS A 133 1621 982 1596 -171 96 60 C ATOM 1095 CG ALYS A 133 -4.628 19.354 17.671 0.65 17.31 C ANISOU 1095 CG ALYS A 133 2091 1484 3002 -338 -202 683 C ATOM 1096 CG BLYS A 133 -5.240 18.868 19.715 0.35 17.11 C ANISOU 1096 CG BLYS A 133 2080 1476 2945 -348 -181 679 C ATOM 1097 CD ALYS A 133 -3.354 19.811 18.379 0.65 29.76 C ANISOU 1097 CD ALYS A 133 3162 3064 5082 -1520 -1656 1451 C ATOM 1098 CD BLYS A 133 -3.855 19.405 19.989 0.35 29.61 C ANISOU 1098 CD BLYS A 133 3150 3062 5039 -1511 -1651 1441 C ATOM 1099 CE ALYS A 133 -3.624 20.977 19.315 0.65 42.51 C ANISOU 1099 CE ALYS A 133 6142 3875 6136 -1771 -3536 1223 C ATOM 1100 CE BLYS A 133 -3.808 20.067 21.342 0.35 42.52 C ANISOU 1100 CE BLYS A 133 6145 3875 6137 -1772 -3536 1225 C ATOM 1101 NZ ALYS A 133 -4.213 22.121 18.587 0.65 49.04 N ANISOU 1101 NZ ALYS A 133 8670 3435 6530 -2322 -2467 1649 N ATOM 1102 NZ BLYS A 133 -4.971 20.963 21.545 0.35 49.04 N ANISOU 1102 NZ BLYS A 133 8669 3434 6529 -2322 -2466 1649 N ATOM 1103 N ALA A 134 -6.121 15.192 19.016 1.00 8.06 N ANISOU 1103 N ALA A 134 1282 822 960 -280 29 -25 N ATOM 1104 CA ALA A 134 -6.716 14.260 19.965 1.00 7.55 C ANISOU 1104 CA ALA A 134 1103 890 875 -248 -23 -20 C ATOM 1105 C ALA A 134 -5.738 13.177 20.405 1.00 7.51 C ANISOU 1105 C ALA A 134 1029 935 888 -258 10 -10 C ATOM 1106 O ALA A 134 -5.739 12.788 21.569 1.00 8.10 O ANISOU 1106 O ALA A 134 1035 1159 884 -133 -28 49 O ATOM 1107 CB ALA A 134 -7.979 13.653 19.367 1.00 7.97 C ANISOU 1107 CB ALA A 134 1122 951 956 -164 -98 -12 C ATOM 1108 N VAL A 135 -4.907 12.660 19.485 1.00 7.98 N ANISOU 1108 N VAL A 135 1147 947 938 -252 37 18 N ATOM 1109 CA VAL A 135 -3.999 11.566 19.857 1.00 8.24 C ANISOU 1109 CA VAL A 135 1212 942 979 -141 60 26 C ATOM 1110 C VAL A 135 -2.915 11.988 20.830 1.00 8.49 C ANISOU 1110 C VAL A 135 1089 1111 1027 -154 131 30 C ATOM 1111 O VAL A 135 -2.224 11.131 21.388 1.00 9.29 O ANISOU 1111 O VAL A 135 1122 1245 1163 -62 12 92 O ATOM 1112 CB VAL A 135 -3.375 10.831 18.664 1.00 9.10 C ANISOU 1112 CB VAL A 135 1270 1105 1084 -204 133 -29 C ATOM 1113 CG1 VAL A 135 -4.445 10.179 17.796 1.00 10.21 C ANISOU 1113 CG1 VAL A 135 1499 1178 1204 -266 29 -98 C ATOM 1114 CG2 VAL A 135 -2.470 11.752 17.845 1.00 9.30 C ANISOU 1114 CG2 VAL A 135 1320 1048 1166 -106 278 6 C ATOM 1115 N GLN A 136 -2.771 13.300 21.039 1.00 8.33 N ANISOU 1115 N GLN A 136 1027 1077 1059 -216 76 -35 N ATOM 1116 CA GLN A 136 -1.820 13.835 22.018 1.00 9.39 C ANISOU 1116 CA GLN A 136 1137 1286 1144 -298 8 -18 C ATOM 1117 C GLN A 136 -2.410 13.993 23.416 1.00 8.96 C ANISOU 1117 C GLN A 136 1103 1260 1042 -252 -83 -29 C ATOM 1118 O GLN A 136 -1.742 14.529 24.306 1.00 10.96 O ANISOU 1118 O GLN A 136 1344 1639 1181 -424 -127 -183 O ATOM 1119 CB GLN A 136 -1.266 15.178 21.522 1.00 11.54 C ANISOU 1119 CB GLN A 136 1408 1612 1364 -640 195 -74 C ATOM 1120 CG AGLN A 136 -0.698 15.077 20.131 0.50 9.56 C ANISOU 1120 CG AGLN A 136 924 1378 1330 -431 11 74 C ATOM 1121 CG BGLN A 136 -0.291 15.063 20.335 0.50 12.88 C ANISOU 1121 CG BGLN A 136 1589 1745 1560 -702 311 7 C ATOM 1122 CD AGLN A 136 -0.133 16.408 19.657 0.50 10.83 C ANISOU 1122 CD AGLN A 136 1149 1380 1586 -490 142 186 C ATOM 1123 CD BGLN A 136 0.993 14.348 20.695 0.50 16.47 C ANISOU 1123 CD BGLN A 136 2091 1701 2467 -547 64 18 C ATOM 1124 OE1AGLN A 136 0.747 16.989 20.286 0.50 14.51 O ANISOU 1124 OE1AGLN A 136 1759 1860 1893 -1076 -157 497 O ATOM 1125 OE1BGLN A 136 1.351 13.348 20.078 0.50 21.62 O ANISOU 1125 OE1BGLN A 136 2702 1253 4258 -699 1440 -304 O ATOM 1126 NE2AGLN A 136 -0.657 16.896 18.545 0.50 11.48 N ANISOU 1126 NE2AGLN A 136 1181 1472 1711 -400 169 247 N ATOM 1127 NE2BGLN A 136 1.696 14.861 21.701 0.50 28.06 N ANISOU 1127 NE2BGLN A 136 4426 3793 2442 328 -1589 74 N ATOM 1128 N GLN A 137 -3.638 13.507 23.611 1.00 8.32 N ANISOU 1128 N GLN A 137 1056 1174 930 -166 -43 -53 N ATOM 1129 CA GLN A 137 -4.355 13.684 24.875 1.00 7.98 C ANISOU 1129 CA GLN A 137 1085 1068 880 -100 -76 -105 C ATOM 1130 C GLN A 137 -4.712 12.341 25.487 1.00 7.77 C ANISOU 1130 C GLN A 137 1035 1117 799 -48 -87 -115 C ATOM 1131 O GLN A 137 -5.054 11.415 24.757 1.00 8.06 O ANISOU 1131 O GLN A 137 1186 1067 810 -42 -54 -69 O ATOM 1132 CB GLN A 137 -5.661 14.474 24.683 1.00 8.99 C ANISOU 1132 CB GLN A 137 1202 1181 1035 -14 -100 -28 C ATOM 1133 CG GLN A 137 -5.602 15.650 23.752 1.00 11.20 C ANISOU 1133 CG GLN A 137 1765 1234 1255 -7 23 32 C ATOM 1134 CD GLN A 137 -4.536 16.635 24.075 1.00 12.37 C ANISOU 1134 CD GLN A 137 1958 1305 1438 -121 92 -92 C ATOM 1135 OE1 GLN A 137 -3.929 17.219 23.158 1.00 15.86 O ANISOU 1135 OE1 GLN A 137 2540 1824 1661 -394 382 48 O ATOM 1136 NE2 GLN A 137 -4.299 16.859 25.351 1.00 11.43 N ANISOU 1136 NE2 GLN A 137 1670 1117 1556 -208 -20 -290 N ATOM 1137 N PRO A 138 -4.741 12.238 26.822 1.00 8.48 N ANISOU 1137 N PRO A 138 1101 1320 802 -95 -105 -105 N ATOM 1138 CA PRO A 138 -4.999 10.931 27.433 1.00 9.38 C ANISOU 1138 CA PRO A 138 1244 1464 858 -79 -120 62 C ATOM 1139 C PRO A 138 -6.426 10.430 27.211 1.00 9.26 C ANISOU 1139 C PRO A 138 1052 1379 1087 -73 -60 147 C ATOM 1140 O PRO A 138 -6.646 9.230 27.278 1.00 12.33 O ANISOU 1140 O PRO A 138 1280 1483 1923 -89 -87 397 O ATOM 1141 CB PRO A 138 -4.738 11.173 28.921 1.00 12.91 C ANISOU 1141 CB PRO A 138 1919 1945 1040 -223 -285 45 C ATOM 1142 CG PRO A 138 -4.765 12.659 29.085 1.00 20.35 C ANISOU 1142 CG PRO A 138 4159 2338 1235 -1010 320 -164 C ATOM 1143 CD PRO A 138 -4.266 13.220 27.799 1.00 11.87 C ANISOU 1143 CD PRO A 138 1772 1767 969 -528 -210 -271 C ATOM 1144 N ASP A 139 -7.360 11.348 26.945 1.00 8.64 N ANISOU 1144 N ASP A 139 1103 1329 853 -125 -14 -68 N ATOM 1145 CA ASP A 139 -8.762 11.020 26.633 1.00 8.94 C ANISOU 1145 CA ASP A 139 1003 1493 902 -96 9 -55 C ATOM 1146 C ASP A 139 -9.112 11.465 25.215 1.00 7.74 C ANISOU 1146 C ASP A 139 946 1109 885 -142 -13 -37 C ATOM 1147 O ASP A 139 -10.223 11.890 24.920 1.00 8.78 O ANISOU 1147 O ASP A 139 1085 1171 1080 -32 67 -1 O ATOM 1148 CB ASP A 139 -9.718 11.640 27.657 1.00 10.47 C ANISOU 1148 CB ASP A 139 1215 1654 1107 -51 140 -183 C ATOM 1149 CG ASP A 139 -9.641 13.134 27.708 1.00 11.08 C ANISOU 1149 CG ASP A 139 1300 1721 1187 85 65 -242 C ATOM 1150 OD1 ASP A 139 -8.724 13.720 27.093 1.00 11.01 O ANISOU 1150 OD1 ASP A 139 1520 1415 1250 50 87 -270 O ATOM 1151 OD2 ASP A 139 -10.506 13.723 28.381 1.00 14.33 O ANISOU 1151 OD2 ASP A 139 1941 2077 1428 239 450 -502 O ATOM 1152 N GLY A 140 -8.144 11.336 24.298 1.00 7.06 N ANISOU 1152 N GLY A 140 985 882 816 -92 -35 -46 N ATOM 1153 CA GLY A 140 -8.355 11.817 22.946 1.00 7.37 C ANISOU 1153 CA GLY A 140 1034 896 868 -129 -65 -76 C ATOM 1154 C GLY A 140 -9.212 10.916 22.055 1.00 6.23 C ANISOU 1154 C GLY A 140 775 728 864 -72 5 -60 C ATOM 1155 O GLY A 140 -9.901 11.417 21.176 1.00 6.86 O ANISOU 1155 O GLY A 140 962 720 925 0 -93 -59 O ATOM 1156 N LEU A 141 -9.082 9.600 22.222 1.00 6.27 N ANISOU 1156 N LEU A 141 817 704 863 -29 -37 -5 N ATOM 1157 CA LEU A 141 -9.770 8.640 21.357 1.00 6.25 C ANISOU 1157 CA LEU A 141 829 697 849 -44 -15 -48 C ATOM 1158 C LEU A 141 -10.643 7.710 22.169 1.00 5.78 C ANISOU 1158 C LEU A 141 793 646 757 45 -88 -90 C ATOM 1159 O LEU A 141 -10.365 7.410 23.332 1.00 6.59 O ANISOU 1159 O LEU A 141 904 793 807 -82 -119 -18 O ATOM 1160 CB LEU A 141 -8.775 7.771 20.564 1.00 6.96 C ANISOU 1160 CB LEU A 141 933 796 914 -20 99 -22 C ATOM 1161 CG LEU A 141 -7.873 8.437 19.547 1.00 9.41 C ANISOU 1161 CG LEU A 141 1435 921 1221 261 477 184 C ATOM 1162 CD1 LEU A 141 -7.152 7.362 18.729 1.00 8.39 C ANISOU 1162 CD1 LEU A 141 1085 987 1115 211 196 20 C ATOM 1163 CD2 LEU A 141 -8.511 9.478 18.664 1.00 11.63 C ANISOU 1163 CD2 LEU A 141 1904 1070 1443 326 614 234 C ATOM 1164 N ALA A 142 -11.681 7.201 21.500 1.00 6.22 N ANISOU 1164 N ALA A 142 873 695 796 -23 -31 -53 N ATOM 1165 CA ALA A 142 -12.480 6.088 22.003 1.00 6.65 C ANISOU 1165 CA ALA A 142 875 754 899 -64 -25 -39 C ATOM 1166 C ALA A 142 -12.526 5.070 20.887 1.00 6.16 C ANISOU 1166 C ALA A 142 878 687 777 -114 -87 18 C ATOM 1167 O ALA A 142 -12.930 5.403 19.766 1.00 6.50 O ANISOU 1167 O ALA A 142 1041 691 737 -29 -162 37 O ATOM 1168 CB ALA A 142 -13.899 6.547 22.402 1.00 7.50 C ANISOU 1168 CB ALA A 142 901 886 1061 -81 69 -71 C ATOM 1169 N VAL A 143 -12.087 3.845 21.172 1.00 6.14 N ANISOU 1169 N VAL A 143 898 702 734 -38 -144 4 N ATOM 1170 CA VAL A 143 -12.099 2.788 20.181 1.00 5.93 C ANISOU 1170 CA VAL A 143 868 693 694 29 -79 5 C ATOM 1171 C VAL A 143 -13.070 1.705 20.653 1.00 5.82 C ANISOU 1171 C VAL A 143 922 650 639 45 -59 12 C ATOM 1172 O VAL A 143 -12.940 1.190 21.765 1.00 6.49 O ANISOU 1172 O VAL A 143 1024 794 650 -35 -67 38 O ATOM 1173 CB VAL A 143 -10.709 2.216 19.851 1.00 6.63 C ANISOU 1173 CB VAL A 143 851 887 780 77 -111 3 C ATOM 1174 CG1 VAL A 143 -10.811 1.184 18.753 1.00 7.54 C ANISOU 1174 CG1 VAL A 143 1031 1020 816 219 -143 -73 C ATOM 1175 CG2 VAL A 143 -9.751 3.348 19.422 1.00 7.64 C ANISOU 1175 CG2 VAL A 143 859 1118 925 -22 -34 80 C ATOM 1176 N LEU A 144 -14.064 1.430 19.806 1.00 6.05 N ANISOU 1176 N LEU A 144 950 711 637 19 -112 -28 N ATOM 1177 CA LEU A 144 -15.004 0.348 20.014 1.00 6.06 C ANISOU 1177 CA LEU A 144 794 800 708 -58 -61 27 C ATOM 1178 C LEU A 144 -14.428 -0.894 19.342 1.00 6.03 C ANISOU 1178 C LEU A 144 909 711 672 -143 -27 -6 C ATOM 1179 O LEU A 144 -14.233 -0.904 18.126 1.00 7.06 O ANISOU 1179 O LEU A 144 1254 786 643 -36 56 23 O ATOM 1180 CB LEU A 144 -16.343 0.782 19.430 1.00 7.93 C ANISOU 1180 CB LEU A 144 947 1153 915 -11 -62 125 C ATOM 1181 CG LEU A 144 -17.527 -0.163 19.621 1.00 9.30 C ANISOU 1181 CG LEU A 144 1005 1205 1322 -134 -52 97 C ATOM 1182 CD1 LEU A 144 -17.799 -0.424 21.084 1.00 12.21 C ANISOU 1182 CD1 LEU A 144 1266 1840 1535 -328 -30 488 C ATOM 1183 CD2 LEU A 144 -18.766 0.415 18.956 1.00 11.07 C ANISOU 1183 CD2 LEU A 144 1022 1794 1392 -2 -141 75 C ATOM 1184 N GLY A 145 -14.137 -1.905 20.158 1.00 5.96 N ANISOU 1184 N GLY A 145 885 728 651 -84 -23 -30 N ATOM 1185 CA GLY A 145 -13.577 -3.153 19.675 1.00 6.15 C ANISOU 1185 CA GLY A 145 841 765 731 -79 -16 -42 C ATOM 1186 C GLY A 145 -14.633 -4.252 19.683 1.00 5.75 C ANISOU 1186 C GLY A 145 796 726 662 -39 -30 -17 C ATOM 1187 O GLY A 145 -15.366 -4.403 20.670 1.00 6.93 O ANISOU 1187 O GLY A 145 1016 889 726 -171 64 -38 O ATOM 1188 N ILE A 146 -14.672 -5.001 18.590 1.00 5.72 N ANISOU 1188 N ILE A 146 855 661 656 -72 -83 -29 N ATOM 1189 CA ILE A 146 -15.681 -6.052 18.395 1.00 5.73 C ANISOU 1189 CA ILE A 146 802 645 732 6 -40 -7 C ATOM 1190 C ILE A 146 -14.962 -7.295 17.884 1.00 5.58 C ANISOU 1190 C ILE A 146 743 670 707 -22 -94 15 C ATOM 1191 O ILE A 146 -14.240 -7.235 16.889 1.00 6.56 O ANISOU 1191 O ILE A 146 946 708 837 -70 56 -17 O ATOM 1192 CB ILE A 146 -16.777 -5.585 17.412 1.00 6.65 C ANISOU 1192 CB ILE A 146 796 774 956 -81 -127 6 C ATOM 1193 CG1 ILE A 146 -17.419 -4.284 17.925 1.00 8.07 C ANISOU 1193 CG1 ILE A 146 1012 944 1110 144 -175 -12 C ATOM 1194 CG2 ILE A 146 -17.818 -6.682 17.225 1.00 8.50 C ANISOU 1194 CG2 ILE A 146 923 935 1373 -100 -369 12 C ATOM 1195 CD1 ILE A 146 -18.484 -3.686 17.040 1.00 7.88 C ANISOU 1195 CD1 ILE A 146 957 934 1104 44 -154 78 C ATOM 1196 N PHE A 147 -15.143 -8.407 18.574 1.00 5.82 N ANISOU 1196 N PHE A 147 856 630 726 13 -42 6 N ATOM 1197 CA PHE A 147 -14.526 -9.657 18.164 1.00 6.09 C ANISOU 1197 CA PHE A 147 921 625 769 -3 -73 0 C ATOM 1198 C PHE A 147 -15.305 -10.296 17.009 1.00 6.43 C ANISOU 1198 C PHE A 147 927 681 835 -95 -16 -9 C ATOM 1199 O PHE A 147 -16.526 -10.173 16.926 1.00 7.26 O ANISOU 1199 O PHE A 147 943 881 933 -44 -72 -105 O ATOM 1200 CB PHE A 147 -14.533 -10.631 19.346 1.00 6.34 C ANISOU 1200 CB PHE A 147 938 634 836 -48 -78 42 C ATOM 1201 CG PHE A 147 -13.681 -10.171 20.493 1.00 6.33 C ANISOU 1201 CG PHE A 147 961 634 809 -10 -81 106 C ATOM 1202 CD1 PHE A 147 -12.308 -9.996 20.321 1.00 6.78 C ANISOU 1202 CD1 PHE A 147 944 778 853 -49 -73 -2 C ATOM 1203 CD2 PHE A 147 -14.231 -9.902 21.742 1.00 6.66 C ANISOU 1203 CD2 PHE A 147 911 770 851 -20 -71 114 C ATOM 1204 CE1 PHE A 147 -11.497 -9.591 21.373 1.00 7.00 C ANISOU 1204 CE1 PHE A 147 945 856 858 -46 -106 2 C ATOM 1205 CE2 PHE A 147 -13.434 -9.507 22.797 1.00 7.35 C ANISOU 1205 CE2 PHE A 147 1064 906 824 -22 -36 95 C ATOM 1206 CZ PHE A 147 -12.057 -9.345 22.615 1.00 7.17 C ANISOU 1206 CZ PHE A 147 991 899 834 -66 -137 52 C ATOM 1207 N LEU A 148 -14.558 -10.996 16.145 1.00 6.44 N ANISOU 1207 N LEU A 148 962 690 795 -142 -20 -14 N ATOM 1208 CA LEU A 148 -15.125 -11.797 15.058 1.00 6.56 C ANISOU 1208 CA LEU A 148 971 746 777 -61 -57 -80 C ATOM 1209 C LEU A 148 -14.792 -13.255 15.280 1.00 6.65 C ANISOU 1209 C LEU A 148 1019 669 838 -82 -39 -7 C ATOM 1210 O LEU A 148 -13.626 -13.610 15.504 1.00 7.85 O ANISOU 1210 O LEU A 148 1144 775 1064 -58 -35 27 O ATOM 1211 CB LEU A 148 -14.556 -11.379 13.693 1.00 6.94 C ANISOU 1211 CB LEU A 148 1138 704 793 -109 -73 -49 C ATOM 1212 CG LEU A 148 -15.108 -10.121 13.029 1.00 7.12 C ANISOU 1212 CG LEU A 148 1147 685 874 -78 -104 6 C ATOM 1213 CD1 LEU A 148 -14.882 -8.873 13.861 1.00 8.18 C ANISOU 1213 CD1 LEU A 148 1441 716 950 -135 -131 -69 C ATOM 1214 CD2 LEU A 148 -14.495 -9.944 11.654 1.00 8.25 C ANISOU 1214 CD2 LEU A 148 1225 1006 902 -188 -108 31 C ATOM 1215 N LYS A 149 -15.816 -14.104 15.200 1.00 7.49 N ANISOU 1215 N LYS A 149 1111 657 1079 -153 -124 -10 N ATOM 1216 CA LYS A 149 -15.621 -15.554 15.155 1.00 8.40 C ANISOU 1216 CA LYS A 149 1259 734 1200 -143 -252 3 C ATOM 1217 C LYS A 149 -16.132 -16.053 13.803 1.00 8.54 C ANISOU 1217 C LYS A 149 1259 790 1198 -16 -233 -85 C ATOM 1218 O LYS A 149 -16.944 -15.402 13.146 1.00 9.76 O ANISOU 1218 O LYS A 149 1505 1088 1116 204 -282 -168 O ATOM 1219 CB LYS A 149 -16.356 -16.248 16.301 1.00 10.05 C ANISOU 1219 CB LYS A 149 1570 990 1257 -256 -246 135 C ATOM 1220 CG LYS A 149 -17.875 -16.107 16.263 1.00 12.72 C ANISOU 1220 CG LYS A 149 1666 1535 1632 -314 -26 394 C ATOM 1221 CD LYS A 149 -18.526 -16.833 17.442 1.00 19.76 C ANISOU 1221 CD LYS A 149 2340 2720 2449 -532 259 1018 C ATOM 1222 CE LYS A 149 -20.038 -16.742 17.392 1.00 27.64 C ANISOU 1222 CE LYS A 149 2569 4550 3383 -1480 98 1234 C ATOM 1223 NZ LYS A 149 -20.662 -17.418 18.562 1.00 38.39 N ANISOU 1223 NZ LYS A 149 4187 5774 4625 -2083 1261 1572 N ATOM 1224 N VAL A 150 -15.630 -17.201 13.380 1.00 9.56 N ANISOU 1224 N VAL A 150 1491 860 1282 -6 -298 -154 N ATOM 1225 CA VAL A 150 -16.020 -17.799 12.107 1.00 9.66 C ANISOU 1225 CA VAL A 150 1431 888 1353 -37 -258 -237 C ATOM 1226 C VAL A 150 -17.210 -18.731 12.307 1.00 9.85 C ANISOU 1226 C VAL A 150 1460 862 1419 -107 -287 -24 C ATOM 1227 O VAL A 150 -17.147 -19.674 13.095 1.00 11.67 O ANISOU 1227 O VAL A 150 1819 1082 1533 -222 -363 114 O ATOM 1228 CB VAL A 150 -14.828 -18.543 11.472 1.00 10.34 C ANISOU 1228 CB VAL A 150 1411 1031 1486 47 -304 -250 C ATOM 1229 CG1 VAL A 150 -15.269 -19.316 10.234 1.00 12.41 C ANISOU 1229 CG1 VAL A 150 1775 1428 1513 157 -272 -391 C ATOM 1230 CG2 VAL A 150 -13.740 -17.544 11.136 1.00 11.62 C ANISOU 1230 CG2 VAL A 150 1449 1203 1763 4 -238 -67 C ATOM 1231 N GLY A 151 -18.272 -18.470 11.558 1.00 10.16 N ANISOU 1231 N GLY A 151 1499 996 1364 -268 -267 -67 N ATOM 1232 CA GLY A 151 -19.482 -19.287 11.590 1.00 11.21 C ANISOU 1232 CA GLY A 151 1536 1282 1440 -501 -295 165 C ATOM 1233 C GLY A 151 -20.365 -18.843 10.443 1.00 10.38 C ANISOU 1233 C GLY A 151 1528 1066 1352 -320 -216 32 C ATOM 1234 O GLY A 151 -19.988 -18.955 9.281 1.00 10.63 O ANISOU 1234 O GLY A 151 1526 1231 1282 -248 -170 -41 O ATOM 1235 N ASER A 152 -21.541 -18.324 10.775 0.57 10.61 N ANISOU 1235 N ASER A 152 1476 1160 1397 -323 -123 -29 N ATOM 1236 N BSER A 152 -21.540 -18.316 10.763 0.43 10.69 N ANISOU 1236 N BSER A 152 1508 1087 1468 -337 -127 62 N ATOM 1237 CA ASER A 152 -22.428 -17.750 9.773 0.57 10.74 C ANISOU 1237 CA ASER A 152 1410 1234 1436 -240 -8 -126 C ATOM 1238 CA BSER A 152 -22.424 -17.788 9.733 0.43 11.72 C ANISOU 1238 CA BSER A 152 1356 1409 1689 -428 -243 106 C ATOM 1239 C ASER A 152 -21.823 -16.475 9.198 0.57 9.84 C ANISOU 1239 C ASER A 152 1364 1153 1220 -287 -211 -210 C ATOM 1240 C BSER A 152 -21.922 -16.433 9.234 0.43 10.43 C ANISOU 1240 C BSER A 152 1578 1048 1338 -266 -213 -81 C ATOM 1241 O ASER A 152 -21.015 -15.808 9.847 0.57 10.33 O ANISOU 1241 O ASER A 152 1599 1163 1162 -213 -255 -300 O ATOM 1242 O BSER A 152 -21.299 -15.667 9.976 0.43 9.46 O ANISOU 1242 O BSER A 152 1194 1218 1184 -194 -203 -102 O ATOM 1243 CB ASER A 152 -23.789 -17.437 10.399 0.57 13.34 C ANISOU 1243 CB ASER A 152 1470 1590 2010 -207 167 138 C ATOM 1244 CB BSER A 152 -23.853 -17.656 10.264 0.43 14.09 C ANISOU 1244 CB BSER A 152 1457 1829 2068 -340 -168 -216 C ATOM 1245 OG ASER A 152 -24.404 -18.619 10.882 0.57 16.36 O ANISOU 1245 OG ASER A 152 1638 2205 2372 -186 317 718 O ATOM 1246 OG BSER A 152 -23.934 -16.649 11.254 0.43 16.66 O ANISOU 1246 OG BSER A 152 1907 2490 1933 -481 -57 -340 O ATOM 1247 N ALA A 153 -22.203 -16.145 7.970 1.00 10.11 N ANISOU 1247 N ALA A 153 1463 1096 1282 -235 -279 -146 N ATOM 1248 CA ALA A 153 -21.795 -14.894 7.351 1.00 10.07 C ANISOU 1248 CA ALA A 153 1463 1108 1254 -185 -146 -142 C ATOM 1249 C ALA A 153 -22.430 -13.693 8.051 1.00 9.67 C ANISOU 1249 C ALA A 153 1278 1110 1287 -181 -105 -92 C ATOM 1250 O ALA A 153 -23.548 -13.762 8.572 1.00 10.80 O ANISOU 1250 O ALA A 153 1298 1201 1602 -225 9 -156 O ATOM 1251 CB ALA A 153 -22.169 -14.879 5.884 1.00 11.71 C ANISOU 1251 CB ALA A 153 1688 1435 1327 -294 -166 -143 C ATOM 1252 N LYS A 154 -21.701 -12.573 8.017 1.00 9.27 N ANISOU 1252 N LYS A 154 1209 1059 1256 -57 -115 -48 N ATOM 1253 CA LYS A 154 -22.223 -11.284 8.468 1.00 9.74 C ANISOU 1253 CA LYS A 154 1246 1112 1343 -98 -88 -6 C ATOM 1254 C LYS A 154 -22.672 -10.521 7.232 1.00 9.48 C ANISOU 1254 C LYS A 154 1084 1102 1416 -82 -126 -36 C ATOM 1255 O LYS A 154 -21.846 -10.050 6.454 1.00 9.40 O ANISOU 1255 O LYS A 154 1079 1130 1364 -110 -180 33 O ATOM 1256 CB LYS A 154 -21.137 -10.499 9.206 1.00 10.17 C ANISOU 1256 CB LYS A 154 1453 1071 1342 -155 -259 7 C ATOM 1257 CG LYS A 154 -21.644 -9.270 9.954 1.00 11.48 C ANISOU 1257 CG LYS A 154 1827 1162 1374 -132 -197 -56 C ATOM 1258 CD LYS A 154 -22.511 -9.630 11.142 1.00 13.09 C ANISOU 1258 CD LYS A 154 2312 1209 1453 -3 16 -13 C ATOM 1259 CE LYS A 154 -22.656 -8.453 12.080 1.00 14.39 C ANISOU 1259 CE LYS A 154 2440 1442 1584 51 153 62 C ATOM 1260 NZ LYS A 154 -23.564 -8.788 13.199 1.00 16.32 N ANISOU 1260 NZ LYS A 154 2195 2176 1828 170 107 4 N ATOM 1261 N PRO A 155 -23.988 -10.406 7.006 1.00 10.52 N ANISOU 1261 N PRO A 155 1072 1306 1619 -138 -158 79 N ATOM 1262 CA PRO A 155 -24.406 -9.793 5.736 1.00 11.55 C ANISOU 1262 CA PRO A 155 1002 1662 1725 -228 -304 150 C ATOM 1263 C PRO A 155 -23.875 -8.367 5.544 1.00 11.06 C ANISOU 1263 C PRO A 155 982 1636 1585 -127 -258 223 C ATOM 1264 O PRO A 155 -23.493 -7.995 4.434 1.00 12.38 O ANISOU 1264 O PRO A 155 1185 1865 1651 -116 -210 426 O ATOM 1265 CB PRO A 155 -25.941 -9.827 5.834 1.00 14.06 C ANISOU 1265 CB PRO A 155 1029 2183 2129 -255 -314 297 C ATOM 1266 CG PRO A 155 -26.226 -10.979 6.753 1.00 16.47 C ANISOU 1266 CG PRO A 155 1324 2662 2272 -418 -326 619 C ATOM 1267 CD PRO A 155 -25.132 -10.938 7.779 1.00 12.83 C ANISOU 1267 CD PRO A 155 1126 1766 1984 -322 -203 283 C ATOM 1268 N GLY A 156 -23.831 -7.603 6.637 1.00 10.77 N ANISOU 1268 N GLY A 156 1085 1287 1719 -44 -168 273 N ATOM 1269 CA GLY A 156 -23.386 -6.222 6.593 1.00 11.31 C ANISOU 1269 CA GLY A 156 1209 1300 1787 -55 -82 302 C ATOM 1270 C GLY A 156 -21.905 -6.029 6.319 1.00 11.10 C ANISOU 1270 C GLY A 156 1185 1164 1867 -74 -102 207 C ATOM 1271 O GLY A 156 -21.461 -4.912 6.097 1.00 13.24 O ANISOU 1271 O GLY A 156 1341 1096 2594 -35 -36 337 O ATOM 1272 N LEU A 157 -21.136 -7.117 6.358 1.00 9.63 N ANISOU 1272 N LEU A 157 1120 1073 1465 -65 -127 -2 N ATOM 1273 CA LEU A 157 -19.711 -7.083 6.033 1.00 9.35 C ANISOU 1273 CA LEU A 157 1065 1150 1339 -194 -171 -45 C ATOM 1274 C LEU A 157 -19.451 -7.313 4.546 1.00 9.17 C ANISOU 1274 C LEU A 157 1175 1047 1262 -198 -193 1 C ATOM 1275 O LEU A 157 -18.375 -7.001 4.047 1.00 9.42 O ANISOU 1275 O LEU A 157 1231 1133 1217 -273 -151 -26 O ATOM 1276 CB LEU A 157 -18.967 -8.140 6.861 1.00 9.45 C ANISOU 1276 CB LEU A 157 966 1254 1371 -134 -218 -40 C ATOM 1277 CG LEU A 157 -17.446 -8.244 6.684 1.00 10.00 C ANISOU 1277 CG LEU A 157 1043 1267 1489 -152 -298 -86 C ATOM 1278 CD1 LEU A 157 -16.743 -6.931 7.085 1.00 10.99 C ANISOU 1278 CD1 LEU A 157 1331 1382 1464 -465 -378 -95 C ATOM 1279 CD2 LEU A 157 -16.915 -9.422 7.492 1.00 10.83 C ANISOU 1279 CD2 LEU A 157 1178 1356 1583 31 -311 -65 C ATOM 1280 N GLN A 158 -20.420 -7.871 3.817 1.00 9.72 N ANISOU 1280 N GLN A 158 1163 1194 1336 -305 -339 6 N ATOM 1281 CA GLN A 158 -20.107 -8.341 2.473 1.00 10.49 C ANISOU 1281 CA GLN A 158 1331 1269 1386 -409 -349 -112 C ATOM 1282 C GLN A 158 -19.663 -7.218 1.528 1.00 10.09 C ANISOU 1282 C GLN A 158 1325 1204 1304 -246 -369 -99 C ATOM 1283 O GLN A 158 -18.801 -7.431 0.691 1.00 10.41 O ANISOU 1283 O GLN A 158 1296 1343 1317 -313 -284 -149 O ATOM 1284 CB GLN A 158 -21.262 -9.159 1.891 1.00 11.15 C ANISOU 1284 CB GLN A 158 1287 1290 1659 -265 -477 -171 C ATOM 1285 CG GLN A 158 -20.869 -9.881 0.623 1.00 11.36 C ANISOU 1285 CG GLN A 158 1493 1318 1505 -295 -489 -113 C ATOM 1286 CD GLN A 158 -19.750 -10.883 0.825 1.00 10.84 C ANISOU 1286 CD GLN A 158 1463 1303 1354 -220 -366 -119 C ATOM 1287 OE1 GLN A 158 -19.604 -11.484 1.903 1.00 10.54 O ANISOU 1287 OE1 GLN A 158 1561 1227 1216 -7 -278 -135 O ATOM 1288 NE2 GLN A 158 -18.965 -11.098 -0.223 1.00 13.15 N ANISOU 1288 NE2 GLN A 158 1731 1784 1481 -363 -182 -292 N ATOM 1289 N LYS A 159 -20.256 -6.029 1.657 1.00 10.35 N ANISOU 1289 N LYS A 159 1190 1345 1396 -221 -444 28 N ATOM 1290 CA LYS A 159 -19.849 -4.927 0.784 1.00 10.92 C ANISOU 1290 CA LYS A 159 1311 1258 1578 -185 -479 48 C ATOM 1291 C LYS A 159 -18.356 -4.580 0.975 1.00 9.98 C ANISOU 1291 C LYS A 159 1356 1194 1242 -234 -306 -4 C ATOM 1292 O LYS A 159 -17.677 -4.201 0.009 1.00 11.02 O ANISOU 1292 O LYS A 159 1471 1497 1221 -361 -223 26 O ATOM 1293 CB LYS A 159 -20.723 -3.695 1.009 1.00 14.79 C ANISOU 1293 CB LYS A 159 1647 1582 2389 77 -626 12 C ATOM 1294 CG LYS A 159 -22.117 -3.839 0.394 1.00 22.86 C ANISOU 1294 CG LYS A 159 2048 2752 3887 636 -1259 -212 C ATOM 1295 CD LYS A 159 -22.862 -2.505 0.224 1.00 31.20 C ANISOU 1295 CD LYS A 159 3155 3716 4982 1508 -1075 -696 C ATOM 1296 CE LYS A 159 -22.703 -1.555 1.414 1.00 39.70 C ANISOU 1296 CE LYS A 159 6495 3540 5051 1556 -555 -657 C ATOM 1297 NZ LYS A 159 -23.619 -0.360 1.353 1.00 31.57 N ANISOU 1297 NZ LYS A 159 5288 2814 3894 447 725 -173 N ATOM 1298 N VAL A 160 -17.864 -4.702 2.201 1.00 9.09 N ANISOU 1298 N VAL A 160 1193 1060 1203 -177 -280 -45 N ATOM 1299 CA VAL A 160 -16.434 -4.519 2.465 1.00 8.95 C ANISOU 1299 CA VAL A 160 1106 1126 1167 -171 -218 -87 C ATOM 1300 C VAL A 160 -15.630 -5.619 1.763 1.00 8.89 C ANISOU 1300 C VAL A 160 1193 1076 1109 -225 -191 -117 C ATOM 1301 O VAL A 160 -14.674 -5.349 1.040 1.00 9.97 O ANISOU 1301 O VAL A 160 1288 1192 1307 -185 -34 -81 O ATOM 1302 CB VAL A 160 -16.160 -4.504 3.976 1.00 9.48 C ANISOU 1302 CB VAL A 160 1179 1173 1251 -137 -262 -155 C ATOM 1303 CG1 VAL A 160 -14.668 -4.475 4.257 1.00 10.92 C ANISOU 1303 CG1 VAL A 160 1173 1543 1432 -215 -349 -121 C ATOM 1304 CG2 VAL A 160 -16.849 -3.325 4.646 1.00 11.06 C ANISOU 1304 CG2 VAL A 160 1562 1291 1350 87 -256 -258 C ATOM 1305 N VAL A 161 -16.018 -6.869 1.990 1.00 9.30 N ANISOU 1305 N VAL A 161 1320 1073 1141 -156 -141 -172 N ATOM 1306 CA VAL A 161 -15.307 -7.996 1.402 1.00 11.11 C ANISOU 1306 CA VAL A 161 1759 1147 1317 -14 71 -92 C ATOM 1307 C VAL A 161 -15.174 -7.868 -0.111 1.00 10.90 C ANISOU 1307 C VAL A 161 1746 1150 1248 -264 3 -226 C ATOM 1308 O VAL A 161 -14.130 -8.150 -0.704 1.00 12.26 O ANISOU 1308 O VAL A 161 1945 1348 1367 -254 255 -282 O ATOM 1309 CB VAL A 161 -16.054 -9.329 1.762 1.00 13.81 C ANISOU 1309 CB VAL A 161 2324 1207 1716 66 160 -48 C ATOM 1310 CG1 VAL A 161 -15.567 -10.489 0.912 1.00 14.25 C ANISOU 1310 CG1 VAL A 161 2182 1334 1897 -113 -307 -164 C ATOM 1311 CG2 VAL A 161 -15.898 -9.618 3.253 1.00 15.68 C ANISOU 1311 CG2 VAL A 161 2647 1451 1857 126 316 155 C ATOM 1312 N ASP A 162 -16.252 -7.440 -0.748 1.00 11.79 N ANISOU 1312 N ASP A 162 1873 1390 1216 -516 -204 -200 N ATOM 1313 CA ASP A 162 -16.250 -7.444 -2.196 1.00 14.42 C ANISOU 1313 CA ASP A 162 2164 1942 1373 -759 -265 -250 C ATOM 1314 C ASP A 162 -15.449 -6.330 -2.855 1.00 14.15 C ANISOU 1314 C ASP A 162 2415 1725 1237 -646 8 -251 C ATOM 1315 O ASP A 162 -15.174 -6.414 -4.042 1.00 19.05 O ANISOU 1315 O ASP A 162 3291 2828 1119 -1170 232 -458 O ATOM 1316 CB ASP A 162 -17.666 -7.464 -2.716 1.00 17.72 C ANISOU 1316 CB ASP A 162 2155 2844 1734 -718 -380 -149 C ATOM 1317 CG ASP A 162 -18.287 -8.842 -2.629 1.00 18.48 C ANISOU 1317 CG ASP A 162 1985 3001 2035 -792 -444 -470 C ATOM 1318 OD1 ASP A 162 -17.544 -9.853 -2.713 1.00 20.22 O ANISOU 1318 OD1 ASP A 162 2293 3020 2371 -602 33 212 O ATOM 1319 OD2 ASP A 162 -19.500 -8.903 -2.440 1.00 19.56 O ANISOU 1319 OD2 ASP A 162 2111 3138 2184 -719 -108 -417 O ATOM 1320 N VAL A 163 -15.069 -5.295 -2.107 1.00 10.96 N ANISOU 1320 N VAL A 163 1574 1406 1185 -308 -328 -95 N ATOM 1321 CA VAL A 163 -14.231 -4.244 -2.660 1.00 11.27 C ANISOU 1321 CA VAL A 163 1557 1462 1264 -169 -298 58 C ATOM 1322 C VAL A 163 -12.734 -4.551 -2.480 1.00 10.62 C ANISOU 1322 C VAL A 163 1543 1396 1096 -160 -202 -20 C ATOM 1323 O VAL A 163 -11.879 -3.858 -3.036 1.00 10.96 O ANISOU 1323 O VAL A 163 1549 1491 1124 -178 -8 42 O ATOM 1324 CB VAL A 163 -14.608 -2.857 -2.062 1.00 12.57 C ANISOU 1324 CB VAL A 163 1698 1399 1677 -123 -355 148 C ATOM 1325 CG1 VAL A 163 -14.042 -2.687 -0.678 1.00 14.09 C ANISOU 1325 CG1 VAL A 163 2194 1445 1715 -288 186 -119 C ATOM 1326 CG2 VAL A 163 -14.153 -1.715 -2.951 1.00 15.60 C ANISOU 1326 CG2 VAL A 163 2293 1647 1986 -15 -182 433 C ATOM 1327 N LEU A 164 -12.406 -5.575 -1.683 1.00 10.65 N ANISOU 1327 N LEU A 164 1626 1371 1049 -120 -187 -34 N ATOM 1328 CA LEU A 164 -11.006 -5.807 -1.342 1.00 10.50 C ANISOU 1328 CA LEU A 164 1557 1298 1136 -106 -57 -43 C ATOM 1329 C LEU A 164 -10.125 -6.123 -2.558 1.00 12.11 C ANISOU 1329 C LEU A 164 1988 1382 1230 -217 232 -180 C ATOM 1330 O LEU A 164 -8.947 -5.770 -2.562 1.00 11.63 O ANISOU 1330 O LEU A 164 1815 1453 1151 6 127 56 O ATOM 1331 CB LEU A 164 -10.857 -6.874 -0.265 1.00 10.53 C ANISOU 1331 CB LEU A 164 1594 1202 1203 39 21 8 C ATOM 1332 CG LEU A 164 -11.531 -6.535 1.077 1.00 9.95 C ANISOU 1332 CG LEU A 164 1422 1117 1240 34 -113 40 C ATOM 1333 CD1 LEU A 164 -11.305 -7.661 2.077 1.00 11.44 C ANISOU 1333 CD1 LEU A 164 1599 1327 1420 28 -61 272 C ATOM 1334 CD2 LEU A 164 -11.066 -5.190 1.643 1.00 10.12 C ANISOU 1334 CD2 LEU A 164 1323 1245 1279 87 -230 -92 C ATOM 1335 N ASP A 165 -10.691 -6.757 -3.580 1.00 14.21 N ANISOU 1335 N ASP A 165 2279 1748 1373 -43 148 -465 N ATOM 1336 CA ASP A 165 -9.941 -7.042 -4.804 1.00 18.23 C ANISOU 1336 CA ASP A 165 3034 2162 1731 -437 429 -603 C ATOM 1337 C ASP A 165 -9.396 -5.776 -5.453 1.00 15.68 C ANISOU 1337 C ASP A 165 2442 2067 1448 -134 377 -363 C ATOM 1338 O ASP A 165 -8.412 -5.832 -6.194 1.00 19.97 O ANISOU 1338 O ASP A 165 2869 2760 1960 170 1026 -74 O ATOM 1339 CB ASP A 165 -10.824 -7.783 -5.813 1.00 29.99 C ANISOU 1339 CB ASP A 165 4818 3389 3187 -1760 450 -1410 C ATOM 1340 CG ASP A 165 -10.883 -9.272 -5.555 1.00 42.64 C ANISOU 1340 CG ASP A 165 6836 3563 5805 -1518 -1455 -1132 C ATOM 1341 OD1 ASP A 165 -10.015 -9.792 -4.822 1.00 50.04 O ANISOU 1341 OD1 ASP A 165 6080 6095 6837 -820 -1228 321 O ATOM 1342 OD2 ASP A 165 -11.797 -9.924 -6.099 1.00 56.48 O ANISOU 1342 OD2 ASP A 165 9051 3985 8424 -3269 -2970 -574 O ATOM 1343 N SER A 166 -10.057 -4.646 -5.230 1.00 12.95 N ANISOU 1343 N SER A 166 1793 2070 1059 -186 -219 -138 N ATOM 1344 CA SER A 166 -9.646 -3.395 -5.849 1.00 12.63 C ANISOU 1344 CA SER A 166 1587 2140 1073 -135 -262 151 C ATOM 1345 C SER A 166 -8.601 -2.621 -5.059 1.00 11.28 C ANISOU 1345 C SER A 166 1600 1761 923 33 -111 137 C ATOM 1346 O SER A 166 -8.077 -1.621 -5.547 1.00 12.46 O ANISOU 1346 O SER A 166 1701 1997 1038 -89 -228 386 O ATOM 1347 CB SER A 166 -10.859 -2.510 -6.126 1.00 14.61 C ANISOU 1347 CB SER A 166 1546 2418 1588 -81 -228 276 C ATOM 1348 OG SER A 166 -11.420 -2.009 -4.936 1.00 15.65 O ANISOU 1348 OG SER A 166 2019 2204 1723 185 -255 196 O ATOM 1349 N ILE A 167 -8.306 -3.079 -3.839 1.00 9.29 N ANISOU 1349 N ILE A 167 1239 1471 820 92 -137 67 N ATOM 1350 CA ILE A 167 -7.297 -2.458 -2.999 1.00 8.58 C ANISOU 1350 CA ILE A 167 1162 1174 923 34 -71 57 C ATOM 1351 C ILE A 167 -6.307 -3.519 -2.492 1.00 7.91 C ANISOU 1351 C ILE A 167 1130 1022 852 -47 -4 24 C ATOM 1352 O ILE A 167 -5.906 -3.524 -1.331 1.00 8.21 O ANISOU 1352 O ILE A 167 1233 1057 828 66 -8 7 O ATOM 1353 CB ILE A 167 -7.919 -1.630 -1.831 1.00 8.96 C ANISOU 1353 CB ILE A 167 1288 1107 1009 153 -9 95 C ATOM 1354 CG1 ILE A 167 -8.793 -2.491 -0.908 1.00 9.41 C ANISOU 1354 CG1 ILE A 167 1296 1318 962 76 37 -18 C ATOM 1355 CG2 ILE A 167 -8.715 -0.436 -2.400 1.00 10.20 C ANISOU 1355 CG2 ILE A 167 1391 1227 1257 230 -47 139 C ATOM 1356 CD1 ILE A 167 -8.863 -1.944 0.489 1.00 10.30 C ANISOU 1356 CD1 ILE A 167 1426 1434 1055 -73 41 -119 C ATOM 1357 N LYS A 168 -5.892 -4.405 -3.394 1.00 8.79 N ANISOU 1357 N LYS A 168 1233 1178 930 30 17 9 N ATOM 1358 CA LYS A 168 -5.108 -5.547 -2.967 1.00 8.63 C ANISOU 1358 CA LYS A 168 1190 1124 964 39 12 -108 C ATOM 1359 C LYS A 168 -3.796 -5.159 -2.287 1.00 8.10 C ANISOU 1359 C LYS A 168 1251 969 860 50 53 -8 C ATOM 1360 O LYS A 168 -3.354 -5.833 -1.355 1.00 8.45 O ANISOU 1360 O LYS A 168 1286 989 933 29 -41 84 O ATOM 1361 CB LYS A 168 -4.831 -6.481 -4.161 1.00 10.06 C ANISOU 1361 CB LYS A 168 1375 1260 1187 94 -91 -253 C ATOM 1362 CG LYS A 168 -4.077 -7.746 -3.778 1.00 12.00 C ANISOU 1362 CG LYS A 168 1848 1209 1502 164 -80 -300 C ATOM 1363 CD LYS A 168 -3.888 -8.638 -4.997 1.00 17.08 C ANISOU 1363 CD LYS A 168 2982 1490 2018 407 -171 -662 C ATOM 1364 CE LYS A 168 -3.093 -9.881 -4.685 1.00 20.75 C ANISOU 1364 CE LYS A 168 3347 1834 2704 708 37 -667 C ATOM 1365 NZ LYS A 168 -2.899 -10.710 -5.902 1.00 31.34 N ANISOU 1365 NZ LYS A 168 4925 3552 3430 2059 -184 -1333 N ATOM 1366 N THR A 169 -3.157 -4.118 -2.812 1.00 8.56 N ANISOU 1366 N THR A 169 1259 1048 946 5 102 106 N ATOM 1367 CA THR A 169 -1.807 -3.766 -2.436 1.00 8.46 C ANISOU 1367 CA THR A 169 1206 1065 944 8 179 84 C ATOM 1368 C THR A 169 -1.732 -2.400 -1.748 1.00 8.04 C ANISOU 1368 C THR A 169 1102 1035 917 -1 147 148 C ATOM 1369 O THR A 169 -2.613 -1.541 -1.885 1.00 8.48 O ANISOU 1369 O THR A 169 1178 997 1048 33 122 150 O ATOM 1370 CB THR A 169 -0.873 -3.811 -3.673 1.00 9.31 C ANISOU 1370 CB THR A 169 1314 1198 1024 76 200 126 C ATOM 1371 OG1 THR A 169 -1.461 -3.039 -4.723 1.00 10.15 O ANISOU 1371 OG1 THR A 169 1486 1398 973 176 238 198 O ATOM 1372 CG2 THR A 169 -0.688 -5.239 -4.143 1.00 11.31 C ANISOU 1372 CG2 THR A 169 1747 1259 1291 246 531 117 C ATOM 1373 N LYS A 170 -0.654 -2.236 -0.995 1.00 8.82 N ANISOU 1373 N LYS A 170 1169 1118 1064 70 89 64 N ATOM 1374 CA LYS A 170 -0.375 -1.040 -0.235 1.00 9.07 C ANISOU 1374 CA LYS A 170 1208 1088 1149 -44 117 98 C ATOM 1375 C LYS A 170 -0.462 0.219 -1.077 1.00 8.74 C ANISOU 1375 C LYS A 170 1123 1108 1089 -44 129 130 C ATOM 1376 O LYS A 170 0.137 0.304 -2.160 1.00 10.37 O ANISOU 1376 O LYS A 170 1443 1372 1125 -93 342 130 O ATOM 1377 CB LYS A 170 1.024 -1.154 0.389 1.00 10.52 C ANISOU 1377 CB LYS A 170 1336 1285 1375 -89 -28 201 C ATOM 1378 CG LYS A 170 1.464 0.064 1.181 1.00 12.01 C ANISOU 1378 CG LYS A 170 1439 1405 1719 -244 -185 223 C ATOM 1379 CD LYS A 170 2.742 -0.186 1.957 1.00 18.60 C ANISOU 1379 CD LYS A 170 1955 2286 2828 -17 -663 -10 C ATOM 1380 CE LYS A 170 3.799 -0.840 1.110 1.00 39.49 C ANISOU 1380 CE LYS A 170 3936 5990 5077 2456 -211 -981 C ATOM 1381 NZ LYS A 170 4.058 0.006 -0.061 1.00 68.03 N ANISOU 1381 NZ LYS A 170 7418 11431 7000 3631 1672 -1422 N ATOM 1382 N GLY A 171 -1.206 1.193 -0.577 1.00 8.98 N ANISOU 1382 N GLY A 171 1173 1018 1221 -33 157 105 N ATOM 1383 CA GLY A 171 -1.334 2.472 -1.232 1.00 10.06 C ANISOU 1383 CA GLY A 171 1390 1091 1342 -98 83 267 C ATOM 1384 C GLY A 171 -2.543 2.587 -2.144 1.00 9.95 C ANISOU 1384 C GLY A 171 1350 1067 1362 -89 89 306 C ATOM 1385 O GLY A 171 -2.829 3.683 -2.634 1.00 12.32 O ANISOU 1385 O GLY A 171 1935 1106 1639 -65 -15 369 O ATOM 1386 N LYS A 172 -3.236 1.487 -2.418 1.00 9.12 N ANISOU 1386 N LYS A 172 1124 1129 1211 62 139 342 N ATOM 1387 CA LYS A 172 -4.434 1.530 -3.237 1.00 9.33 C ANISOU 1387 CA LYS A 172 1160 1299 1084 84 154 298 C ATOM 1388 C LYS A 172 -5.641 1.942 -2.384 1.00 8.81 C ANISOU 1388 C LYS A 172 1152 1284 912 166 95 289 C ATOM 1389 O LYS A 172 -5.818 1.468 -1.272 1.00 8.50 O ANISOU 1389 O LYS A 172 1207 1218 804 97 48 271 O ATOM 1390 CB LYS A 172 -4.700 0.179 -3.891 1.00 10.53 C ANISOU 1390 CB LYS A 172 1226 1537 1241 105 136 71 C ATOM 1391 CG LYS A 172 -3.692 -0.211 -4.966 1.00 14.76 C ANISOU 1391 CG LYS A 172 1437 2504 1667 358 95 -311 C ATOM 1392 CD LYS A 172 -4.249 -1.257 -5.930 1.00 21.98 C ANISOU 1392 CD LYS A 172 2338 3637 2376 564 135 -1030 C ATOM 1393 CE LYS A 172 -3.378 -1.400 -7.172 1.00 26.82 C ANISOU 1393 CE LYS A 172 2930 4006 3255 -411 463 -989 C ATOM 1394 NZ LYS A 172 -3.072 -0.090 -7.813 1.00 33.42 N ANISOU 1394 NZ LYS A 172 3328 4706 4665 -8 273 411 N ATOM 1395 N SER A 173 -6.472 2.788 -2.969 1.00 10.54 N ANISOU 1395 N SER A 173 1298 1718 987 339 136 502 N ATOM 1396 CA SER A 173 -7.739 3.181 -2.379 1.00 10.52 C ANISOU 1396 CA SER A 173 1304 1744 950 413 39 317 C ATOM 1397 C SER A 173 -8.858 3.051 -3.407 1.00 10.32 C ANISOU 1397 C SER A 173 1446 1615 858 487 -40 265 C ATOM 1398 O SER A 173 -8.615 2.985 -4.618 1.00 11.74 O ANISOU 1398 O SER A 173 1636 2029 795 551 62 326 O ATOM 1399 CB SER A 173 -7.690 4.607 -1.827 1.00 12.18 C ANISOU 1399 CB SER A 173 1562 1880 1184 439 -125 175 C ATOM 1400 OG SER A 173 -7.511 5.559 -2.869 1.00 13.82 O ANISOU 1400 OG SER A 173 2071 1769 1411 235 -228 224 O ATOM 1401 N ALA A 174 -10.085 3.040 -2.902 1.00 10.43 N ANISOU 1401 N ALA A 174 1427 1679 858 465 -115 190 N ATOM 1402 CA ALA A 174 -11.268 3.003 -3.742 1.00 10.97 C ANISOU 1402 CA ALA A 174 1519 1706 945 440 -146 99 C ATOM 1403 C ALA A 174 -12.382 3.796 -3.091 1.00 10.02 C ANISOU 1403 C ALA A 174 1351 1626 829 373 -159 217 C ATOM 1404 O ALA A 174 -12.488 3.871 -1.872 1.00 9.32 O ANISOU 1404 O ALA A 174 1306 1452 784 282 -138 231 O ATOM 1405 CB ALA A 174 -11.715 1.578 -3.964 1.00 12.60 C ANISOU 1405 CB ALA A 174 1695 1757 1336 274 -46 -7 C ATOM 1406 N ASP A 175 -13.229 4.384 -3.918 1.00 11.93 N ANISOU 1406 N ASP A 175 1550 2008 973 564 -162 236 N ATOM 1407 CA ASP A 175 -14.417 5.036 -3.414 1.00 13.55 C ANISOU 1407 CA ASP A 175 1489 2332 1327 698 -367 220 C ATOM 1408 C ASP A 175 -15.229 4.024 -2.599 1.00 12.16 C ANISOU 1408 C ASP A 175 1301 1853 1468 452 -362 -192 C ATOM 1409 O ASP A 175 -15.333 2.851 -2.976 1.00 14.44 O ANISOU 1409 O ASP A 175 1662 2039 1785 476 -338 -593 O ATOM 1410 CB ASP A 175 -15.254 5.544 -4.597 1.00 19.66 C ANISOU 1410 CB ASP A 175 2245 3070 2156 1127 -637 635 C ATOM 1411 CG ASP A 175 -14.602 6.729 -5.329 1.00 29.70 C ANISOU 1411 CG ASP A 175 4534 3662 3089 -191 -1573 1468 C ATOM 1412 OD1 ASP A 175 -13.977 7.584 -4.662 1.00 34.26 O ANISOU 1412 OD1 ASP A 175 4827 4335 3854 -569 -1970 1055 O ATOM 1413 OD2 ASP A 175 -14.736 6.823 -6.574 1.00 35.15 O ANISOU 1413 OD2 ASP A 175 4868 5240 3249 -1740 -1674 2022 O ATOM 1414 N PHE A 176 -15.804 4.471 -1.485 1.00 10.78 N ANISOU 1414 N PHE A 176 1124 1581 1389 226 -297 -32 N ATOM 1415 CA PHE A 176 -16.560 3.561 -0.628 1.00 10.37 C ANISOU 1415 CA PHE A 176 1132 1283 1525 134 -311 -45 C ATOM 1416 C PHE A 176 -17.622 4.345 0.119 1.00 9.65 C ANISOU 1416 C PHE A 176 1116 1206 1346 71 -453 -1 C ATOM 1417 O PHE A 176 -17.581 4.497 1.319 1.00 13.55 O ANISOU 1417 O PHE A 176 1803 2015 1328 783 -713 -349 O ATOM 1418 CB PHE A 176 -15.631 2.761 0.314 1.00 10.69 C ANISOU 1418 CB PHE A 176 1127 1149 1786 76 -324 -53 C ATOM 1419 CG PHE A 176 -16.255 1.487 0.830 1.00 10.47 C ANISOU 1419 CG PHE A 176 1131 1133 1716 81 -235 -108 C ATOM 1420 CD1 PHE A 176 -16.468 0.415 -0.016 1.00 12.22 C ANISOU 1420 CD1 PHE A 176 1850 1127 1665 -95 121 -89 C ATOM 1421 CD2 PHE A 176 -16.625 1.355 2.155 1.00 10.83 C ANISOU 1421 CD2 PHE A 176 1184 1341 1591 107 -410 -125 C ATOM 1422 CE1 PHE A 176 -17.048 -0.760 0.445 1.00 12.74 C ANISOU 1422 CE1 PHE A 176 1901 1292 1646 -255 147 -127 C ATOM 1423 CE2 PHE A 176 -17.190 0.170 2.629 1.00 10.97 C ANISOU 1423 CE2 PHE A 176 1161 1466 1542 65 -269 -46 C ATOM 1424 CZ PHE A 176 -17.412 -0.880 1.767 1.00 11.17 C ANISOU 1424 CZ PHE A 176 1200 1430 1615 -52 -145 -53 C ATOM 1425 N THR A 177 -18.582 4.857 -0.635 1.00 9.83 N ANISOU 1425 N THR A 177 1220 1345 1170 142 -155 297 N ATOM 1426 CA THR A 177 -19.643 5.672 -0.086 1.00 9.31 C ANISOU 1426 CA THR A 177 1055 1249 1234 113 -198 431 C ATOM 1427 C THR A 177 -20.856 4.840 0.325 1.00 8.53 C ANISOU 1427 C THR A 177 1109 1154 977 -2 -225 345 C ATOM 1428 O THR A 177 -21.046 3.709 -0.131 1.00 9.56 O ANISOU 1428 O THR A 177 1454 1213 967 -40 -165 257 O ATOM 1429 CB THR A 177 -20.043 6.779 -1.092 1.00 11.46 C ANISOU 1429 CB THR A 177 1341 1545 1467 112 -227 704 C ATOM 1430 OG1 THR A 177 -20.350 6.198 -2.361 1.00 13.96 O ANISOU 1430 OG1 THR A 177 2304 1841 1160 723 -40 573 O ATOM 1431 CG2 THR A 177 -18.915 7.812 -1.248 1.00 15.85 C ANISOU 1431 CG2 THR A 177 1730 1890 2401 -181 -99 1273 C ATOM 1432 N ASN A 178 -21.673 5.425 1.198 1.00 8.73 N ANISOU 1432 N ASN A 178 1033 1279 1006 -42 -157 340 N ATOM 1433 CA ASN A 178 -22.957 4.858 1.594 1.00 9.55 C ANISOU 1433 CA ASN A 178 1110 1360 1157 -157 -267 416 C ATOM 1434 C ASN A 178 -22.862 3.520 2.319 1.00 10.02 C ANISOU 1434 C ASN A 178 1207 1344 1258 -157 -283 451 C ATOM 1435 O ASN A 178 -23.798 2.737 2.289 1.00 13.94 O ANISOU 1435 O ASN A 178 1429 1754 2114 -426 -543 916 O ATOM 1436 CB ASN A 178 -23.916 4.779 0.405 1.00 10.14 C ANISOU 1436 CB ASN A 178 1210 1335 1307 -98 -380 419 C ATOM 1437 CG ASN A 178 -24.074 6.105 -0.252 1.00 10.94 C ANISOU 1437 CG ASN A 178 1392 1446 1317 -34 -366 401 C ATOM 1438 OD1 ASN A 178 -23.532 6.347 -1.338 1.00 12.66 O ANISOU 1438 OD1 ASN A 178 1566 1926 1320 -105 -300 557 O ATOM 1439 ND2 ASN A 178 -24.760 7.008 0.402 1.00 11.53 N ANISOU 1439 ND2 ASN A 178 1251 1505 1626 116 -273 453 N ATOM 1440 N PHE A 179 -21.747 3.261 2.993 1.00 8.68 N ANISOU 1440 N PHE A 179 1280 1152 865 -108 -217 269 N ATOM 1441 CA PHE A 179 -21.632 2.071 3.814 1.00 8.85 C ANISOU 1441 CA PHE A 179 1264 1188 910 -95 -222 294 C ATOM 1442 C PHE A 179 -22.129 2.346 5.224 1.00 8.73 C ANISOU 1442 C PHE A 179 1256 1173 890 -142 -248 242 C ATOM 1443 O PHE A 179 -21.746 3.349 5.836 1.00 9.92 O ANISOU 1443 O PHE A 179 1537 1310 922 -243 -186 177 O ATOM 1444 CB PHE A 179 -20.182 1.564 3.876 1.00 9.58 C ANISOU 1444 CB PHE A 179 1382 1214 1043 29 -88 336 C ATOM 1445 CG PHE A 179 -20.055 0.331 4.723 1.00 8.95 C ANISOU 1445 CG PHE A 179 1201 1147 1052 -41 -170 241 C ATOM 1446 CD1 PHE A 179 -20.437 -0.898 4.213 1.00 10.07 C ANISOU 1446 CD1 PHE A 179 1456 1217 1153 -29 -213 202 C ATOM 1447 CD2 PHE A 179 -19.642 0.407 6.050 1.00 8.67 C ANISOU 1447 CD2 PHE A 179 1034 1220 1039 -45 -192 320 C ATOM 1448 CE1 PHE A 179 -20.401 -2.039 4.991 1.00 10.28 C ANISOU 1448 CE1 PHE A 179 1479 1215 1209 -50 -90 221 C ATOM 1449 CE2 PHE A 179 -19.602 -0.746 6.832 1.00 8.63 C ANISOU 1449 CE2 PHE A 179 967 1231 1080 -36 -93 288 C ATOM 1450 CZ PHE A 179 -19.984 -1.962 6.300 1.00 9.30 C ANISOU 1450 CZ PHE A 179 1122 1248 1165 -14 -52 283 C ATOM 1451 N ASP A 180 -22.974 1.458 5.728 1.00 8.77 N ANISOU 1451 N ASP A 180 1051 1352 929 -52 -230 220 N ATOM 1452 CA ASP A 180 -23.605 1.642 7.034 1.00 9.30 C ANISOU 1452 CA ASP A 180 1087 1438 1007 -33 -146 178 C ATOM 1453 C ASP A 180 -22.912 0.777 8.095 1.00 8.18 C ANISOU 1453 C ASP A 180 996 1135 976 -40 -39 164 C ATOM 1454 O ASP A 180 -23.102 -0.448 8.120 1.00 9.03 O ANISOU 1454 O ASP A 180 1169 1197 1063 -57 -61 85 O ATOM 1455 CB ASP A 180 -25.077 1.241 6.940 1.00 11.25 C ANISOU 1455 CB ASP A 180 1118 1850 1305 -27 -142 167 C ATOM 1456 CG ASP A 180 -25.870 1.625 8.171 1.00 12.99 C ANISOU 1456 CG ASP A 180 1115 2311 1511 67 -26 3 C ATOM 1457 OD1 ASP A 180 -25.288 1.876 9.247 1.00 11.05 O ANISOU 1457 OD1 ASP A 180 1193 1654 1351 142 47 185 O ATOM 1458 OD2 ASP A 180 -27.100 1.665 8.041 1.00 21.63 O ANISOU 1458 OD2 ASP A 180 1039 5109 2071 121 -26 -734 O ATOM 1459 N PRO A 181 -22.123 1.389 8.995 1.00 8.30 N ANISOU 1459 N PRO A 181 1054 1155 945 15 -87 149 N ATOM 1460 CA PRO A 181 -21.399 0.569 9.977 1.00 8.31 C ANISOU 1460 CA PRO A 181 952 1236 969 24 -105 223 C ATOM 1461 C PRO A 181 -22.318 -0.077 11.027 1.00 8.55 C ANISOU 1461 C PRO A 181 1021 1300 930 -17 -92 206 C ATOM 1462 O PRO A 181 -21.845 -0.939 11.772 1.00 9.04 O ANISOU 1462 O PRO A 181 1141 1270 1022 -1 -146 226 O ATOM 1463 CB PRO A 181 -20.405 1.564 10.599 1.00 9.23 C ANISOU 1463 CB PRO A 181 1025 1346 1137 -102 -126 97 C ATOM 1464 CG PRO A 181 -21.089 2.905 10.424 1.00 9.72 C ANISOU 1464 CG PRO A 181 1231 1328 1135 -26 -167 51 C ATOM 1465 CD PRO A 181 -21.806 2.822 9.108 1.00 9.30 C ANISOU 1465 CD PRO A 181 1305 1138 1091 -153 -179 110 C ATOM 1466 N ARG A 182 -23.587 0.321 11.092 1.00 8.76 N ANISOU 1466 N ARG A 182 984 1325 1019 11 -21 172 N ATOM 1467 CA ARG A 182 -24.512 -0.365 12.003 1.00 9.11 C ANISOU 1467 CA ARG A 182 1049 1295 1118 -40 4 178 C ATOM 1468 C ARG A 182 -24.614 -1.853 11.692 1.00 9.26 C ANISOU 1468 C ARG A 182 1015 1368 1133 -55 -141 174 C ATOM 1469 O ARG A 182 -24.923 -2.656 12.581 1.00 10.46 O ANISOU 1469 O ARG A 182 1305 1395 1276 -113 11 320 O ATOM 1470 CB ARG A 182 -25.893 0.288 11.992 1.00 10.01 C ANISOU 1470 CB ARG A 182 1123 1335 1344 -41 142 140 C ATOM 1471 CG ARG A 182 -25.863 1.692 12.553 1.00 11.23 C ANISOU 1471 CG ARG A 182 1367 1419 1481 39 219 56 C ATOM 1472 CD ARG A 182 -27.197 2.381 12.468 1.00 12.58 C ANISOU 1472 CD ARG A 182 1502 1556 1723 229 360 241 C ATOM 1473 NE ARG A 182 -27.544 2.635 11.083 1.00 13.60 N ANISOU 1473 NE ARG A 182 1410 1864 1894 225 318 382 N ATOM 1474 CZ ARG A 182 -28.603 3.341 10.708 1.00 16.76 C ANISOU 1474 CZ ARG A 182 1563 2451 2354 493 266 403 C ATOM 1475 NH1 ARG A 182 -29.420 3.851 11.622 1.00 22.15 N ANISOU 1475 NH1 ARG A 182 1915 3535 2968 899 635 -68 N ATOM 1476 NH2 ARG A 182 -28.852 3.539 9.419 1.00 22.21 N ANISOU 1476 NH2 ARG A 182 2376 3476 2588 1134 53 856 N ATOM 1477 N GLY A 183 -24.365 -2.235 10.431 1.00 9.35 N ANISOU 1477 N GLY A 183 1087 1337 1127 -60 -256 140 N ATOM 1478 CA GLY A 183 -24.412 -3.627 10.040 1.00 10.28 C ANISOU 1478 CA GLY A 183 1331 1346 1230 -66 -358 112 C ATOM 1479 C GLY A 183 -23.256 -4.488 10.536 1.00 10.01 C ANISOU 1479 C GLY A 183 1204 1294 1307 -31 -277 132 C ATOM 1480 O GLY A 183 -23.232 -5.684 10.253 1.00 11.46 O ANISOU 1480 O GLY A 183 1578 1194 1584 -76 -369 90 O ATOM 1481 N LEU A 184 -22.310 -3.892 11.277 1.00 8.87 N ANISOU 1481 N LEU A 184 1084 1206 1080 -44 -231 194 N ATOM 1482 CA LEU A 184 -21.183 -4.630 11.844 1.00 9.02 C ANISOU 1482 CA LEU A 184 1175 1140 1112 6 -189 183 C ATOM 1483 C LEU A 184 -21.322 -4.854 13.348 1.00 9.13 C ANISOU 1483 C LEU A 184 1209 1147 1113 -93 -213 251 C ATOM 1484 O LEU A 184 -20.439 -5.453 13.953 1.00 10.37 O ANISOU 1484 O LEU A 184 1348 1352 1239 77 -163 373 O ATOM 1485 CB LEU A 184 -19.879 -3.896 11.549 1.00 9.19 C ANISOU 1485 CB LEU A 184 1199 1175 1120 -17 -160 225 C ATOM 1486 CG LEU A 184 -19.550 -3.729 10.062 1.00 10.81 C ANISOU 1486 CG LEU A 184 1430 1443 1234 88 -161 296 C ATOM 1487 CD1 LEU A 184 -18.281 -2.920 9.887 1.00 12.55 C ANISOU 1487 CD1 LEU A 184 1356 2002 1411 -87 -218 640 C ATOM 1488 CD2 LEU A 184 -19.451 -5.063 9.343 1.00 14.09 C ANISOU 1488 CD2 LEU A 184 2198 1618 1540 307 208 105 C ATOM 1489 N LEU A 185 -22.404 -4.360 13.965 1.00 9.53 N ANISOU 1489 N LEU A 185 1280 1225 1116 -27 -147 264 N ATOM 1490 CA LEU A 185 -22.557 -4.437 15.409 1.00 9.88 C ANISOU 1490 CA LEU A 185 1269 1301 1182 -247 -224 265 C ATOM 1491 C LEU A 185 -23.262 -5.739 15.813 1.00 12.08 C ANISOU 1491 C LEU A 185 1860 1425 1304 -522 -450 428 C ATOM 1492 O LEU A 185 -24.101 -6.243 15.085 1.00 17.60 O ANISOU 1492 O LEU A 185 2896 1954 1839 -1313 -1300 920 O ATOM 1493 CB LEU A 185 -23.369 -3.234 15.908 1.00 10.17 C ANISOU 1493 CB LEU A 185 1144 1462 1256 -185 -142 168 C ATOM 1494 CG LEU A 185 -22.836 -1.847 15.542 1.00 10.42 C ANISOU 1494 CG LEU A 185 1036 1369 1556 -42 -326 151 C ATOM 1495 CD1 LEU A 185 -23.765 -0.749 16.023 1.00 12.55 C ANISOU 1495 CD1 LEU A 185 1506 1677 1585 262 -92 43 C ATOM 1496 CD2 LEU A 185 -21.430 -1.656 16.101 1.00 13.01 C ANISOU 1496 CD2 LEU A 185 1408 1449 2086 -105 -800 247 C ATOM 1497 N PRO A 186 -22.924 -6.295 16.978 1.00 9.84 N ANISOU 1497 N PRO A 186 1276 1321 1144 -215 -184 280 N ATOM 1498 CA PRO A 186 -23.713 -7.405 17.539 1.00 10.21 C ANISOU 1498 CA PRO A 186 1216 1329 1334 -153 -109 318 C ATOM 1499 C PRO A 186 -25.010 -6.860 18.164 1.00 10.12 C ANISOU 1499 C PRO A 186 1057 1330 1458 -208 -303 302 C ATOM 1500 O PRO A 186 -25.242 -5.649 18.219 1.00 11.01 O ANISOU 1500 O PRO A 186 913 1339 1932 -101 -352 381 O ATOM 1501 CB PRO A 186 -22.773 -7.967 18.598 1.00 9.86 C ANISOU 1501 CB PRO A 186 1166 1289 1293 -10 -13 287 C ATOM 1502 CG PRO A 186 -22.067 -6.747 19.106 1.00 9.33 C ANISOU 1502 CG PRO A 186 1092 1299 1152 114 -40 185 C ATOM 1503 CD PRO A 186 -21.832 -5.880 17.876 1.00 8.85 C ANISOU 1503 CD PRO A 186 1091 1218 1055 12 -116 166 C ATOM 1504 N GLU A 187 -25.845 -7.767 18.659 1.00 11.05 N ANISOU 1504 N GLU A 187 1278 1506 1412 -427 -201 329 N ATOM 1505 CA GLU A 187 -27.105 -7.382 19.287 1.00 11.57 C ANISOU 1505 CA GLU A 187 1103 1636 1656 -418 -340 312 C ATOM 1506 C GLU A 187 -26.907 -6.584 20.580 1.00 10.29 C ANISOU 1506 C GLU A 187 832 1524 1554 -183 -245 280 C ATOM 1507 O GLU A 187 -27.543 -5.543 20.785 1.00 12.01 O ANISOU 1507 O GLU A 187 1027 1755 1782 69 -165 287 O ATOM 1508 CB GLU A 187 -27.901 -8.664 19.567 1.00 14.31 C ANISOU 1508 CB GLU A 187 1265 1763 2409 -582 -421 338 C ATOM 1509 CG GLU A 187 -29.145 -8.504 20.400 1.00 20.19 C ANISOU 1509 CG GLU A 187 1693 2566 3411 -395 148 616 C ATOM 1510 CD GLU A 187 -29.717 -9.842 20.828 1.00 22.63 C ANISOU 1510 CD GLU A 187 2179 2582 3838 -228 688 539 C ATOM 1511 OE1 GLU A 187 -29.494 -10.836 20.108 1.00 25.15 O ANISOU 1511 OE1 GLU A 187 1850 3383 4325 -1125 235 -768 O ATOM 1512 OE2 GLU A 187 -30.389 -9.886 21.877 1.00 28.50 O ANISOU 1512 OE2 GLU A 187 3375 3207 4246 -106 1770 988 O ATOM 1513 N SER A 188 -26.048 -7.103 21.452 1.00 9.72 N ANISOU 1513 N SER A 188 841 1479 1374 -181 -201 106 N ATOM 1514 CA SER A 188 -25.814 -6.499 22.757 1.00 9.66 C ANISOU 1514 CA SER A 188 1050 1273 1350 -181 -127 85 C ATOM 1515 C SER A 188 -24.666 -5.493 22.727 1.00 9.24 C ANISOU 1515 C SER A 188 829 1393 1288 -114 -90 35 C ATOM 1516 O SER A 188 -23.647 -5.734 22.087 1.00 10.72 O ANISOU 1516 O SER A 188 912 1830 1332 -186 -32 -193 O ATOM 1517 CB SER A 188 -25.452 -7.590 23.774 1.00 10.95 C ANISOU 1517 CB SER A 188 1371 1437 1353 -230 -226 177 C ATOM 1518 OG SER A 188 -25.166 -7.028 25.041 1.00 11.80 O ANISOU 1518 OG SER A 188 1313 1787 1382 -241 -192 184 O ATOM 1519 N LEU A 189 -24.835 -4.409 23.468 1.00 9.19 N ANISOU 1519 N LEU A 189 889 1273 1330 -164 -197 40 N ATOM 1520 CA LEU A 189 -23.763 -3.442 23.688 1.00 10.20 C ANISOU 1520 CA LEU A 189 1114 1293 1470 -176 -286 67 C ATOM 1521 C LEU A 189 -23.085 -3.599 25.059 1.00 9.83 C ANISOU 1521 C LEU A 189 886 1481 1367 -159 -186 17 C ATOM 1522 O LEU A 189 -22.388 -2.691 25.495 1.00 12.10 O ANISOU 1522 O LEU A 189 1375 1823 1397 -491 -239 27 O ATOM 1523 CB LEU A 189 -24.283 -2.013 23.510 1.00 12.24 C ANISOU 1523 CB LEU A 189 1299 1414 1939 -155 -377 173 C ATOM 1524 CG LEU A 189 -24.758 -1.640 22.102 1.00 13.74 C ANISOU 1524 CG LEU A 189 1158 1746 2315 -149 -583 520 C ATOM 1525 CD1 LEU A 189 -25.237 -0.199 22.065 1.00 16.98 C ANISOU 1525 CD1 LEU A 189 1830 1754 2866 -143 -634 785 C ATOM 1526 CD2 LEU A 189 -23.684 -1.881 21.062 1.00 15.84 C ANISOU 1526 CD2 LEU A 189 1204 2633 2180 -242 -560 819 C ATOM 1527 N ASP A 190 -23.259 -4.739 25.731 1.00 9.15 N ANISOU 1527 N ASP A 190 793 1516 1167 -57 -37 -73 N ATOM 1528 CA ASP A 190 -22.490 -4.988 26.953 1.00 9.24 C ANISOU 1528 CA ASP A 190 814 1590 1105 -176 56 -54 C ATOM 1529 C ASP A 190 -20.988 -4.922 26.633 1.00 8.12 C ANISOU 1529 C ASP A 190 792 1355 938 -127 19 -31 C ATOM 1530 O ASP A 190 -20.555 -5.435 25.595 1.00 8.74 O ANISOU 1530 O ASP A 190 901 1454 966 -148 -7 -121 O ATOM 1531 CB ASP A 190 -22.819 -6.381 27.509 1.00 11.62 C ANISOU 1531 CB ASP A 190 990 2047 1379 -422 123 299 C ATOM 1532 CG ASP A 190 -24.229 -6.499 28.133 1.00 15.56 C ANISOU 1532 CG ASP A 190 950 3152 1810 -708 151 241 C ATOM 1533 OD1 ASP A 190 -24.894 -5.478 28.365 1.00 18.84 O ANISOU 1533 OD1 ASP A 190 1172 3875 2109 -417 583 -349 O ATOM 1534 OD2 ASP A 190 -24.621 -7.641 28.410 1.00 19.45 O ANISOU 1534 OD2 ASP A 190 1429 3607 2353 -1068 226 648 O ATOM 1535 N TYR A 191 -20.215 -4.352 27.547 1.00 7.88 N ANISOU 1535 N TYR A 191 796 1330 867 -116 33 6 N ATOM 1536 CA TYR A 191 -18.803 -4.095 27.235 1.00 7.74 C ANISOU 1536 CA TYR A 191 824 1318 799 -171 -23 81 C ATOM 1537 C TYR A 191 -17.922 -4.138 28.473 1.00 7.38 C ANISOU 1537 C TYR A 191 863 1188 755 -95 -12 49 C ATOM 1538 O TYR A 191 -18.365 -4.019 29.620 1.00 8.00 O ANISOU 1538 O TYR A 191 867 1417 756 -84 46 22 O ATOM 1539 CB TYR A 191 -18.639 -2.726 26.528 1.00 8.36 C ANISOU 1539 CB TYR A 191 992 1375 810 -120 -28 124 C ATOM 1540 CG TYR A 191 -19.035 -1.538 27.385 1.00 8.39 C ANISOU 1540 CG TYR A 191 1031 1296 860 -202 -92 189 C ATOM 1541 CD1 TYR A 191 -18.118 -0.925 28.238 1.00 8.90 C ANISOU 1541 CD1 TYR A 191 1014 1373 993 -244 -70 153 C ATOM 1542 CD2 TYR A 191 -20.319 -1.012 27.324 1.00 8.71 C ANISOU 1542 CD2 TYR A 191 1055 1242 1013 -143 -107 189 C ATOM 1543 CE1 TYR A 191 -18.487 0.138 29.046 1.00 9.47 C ANISOU 1543 CE1 TYR A 191 1249 1267 1082 -295 -198 132 C ATOM 1544 CE2 TYR A 191 -20.703 0.061 28.120 1.00 9.25 C ANISOU 1544 CE2 TYR A 191 1154 1264 1098 -156 -128 182 C ATOM 1545 CZ TYR A 191 -19.773 0.631 28.979 1.00 9.60 C ANISOU 1545 CZ TYR A 191 1285 1244 1117 -188 -160 119 C ATOM 1546 OH TYR A 191 -20.101 1.678 29.810 1.00 11.04 O ANISOU 1546 OH TYR A 191 1491 1417 1287 -208 -196 14 O ATOM 1547 N TRP A 192 -16.628 -4.272 28.177 1.00 6.96 N ANISOU 1547 N TRP A 192 856 1110 679 -78 -15 60 N ATOM 1548 CA TRP A 192 -15.545 -3.994 29.114 1.00 6.78 C ANISOU 1548 CA TRP A 192 822 1040 715 -59 35 61 C ATOM 1549 C TRP A 192 -14.841 -2.698 28.697 1.00 6.65 C ANISOU 1549 C TRP A 192 808 1063 655 -56 -33 -9 C ATOM 1550 O TRP A 192 -14.777 -2.385 27.506 1.00 7.89 O ANISOU 1550 O TRP A 192 1111 1286 599 -343 -17 1 O ATOM 1551 CB TRP A 192 -14.509 -5.119 29.119 1.00 7.70 C ANISOU 1551 CB TRP A 192 882 1148 896 19 20 18 C ATOM 1552 CG TRP A 192 -15.018 -6.462 29.530 1.00 7.55 C ANISOU 1552 CG TRP A 192 874 1076 917 78 -27 71 C ATOM 1553 CD1 TRP A 192 -15.257 -6.892 30.805 1.00 8.46 C ANISOU 1553 CD1 TRP A 192 1057 1135 1024 60 -29 177 C ATOM 1554 CD2 TRP A 192 -15.276 -7.579 28.675 1.00 7.88 C ANISOU 1554 CD2 TRP A 192 823 1103 1068 40 -68 14 C ATOM 1555 NE1 TRP A 192 -15.671 -8.204 30.796 1.00 9.30 N ANISOU 1555 NE1 TRP A 192 1250 1120 1166 50 -58 222 N ATOM 1556 CE2 TRP A 192 -15.684 -8.647 29.498 1.00 8.90 C ANISOU 1556 CE2 TRP A 192 1127 1029 1224 104 -90 103 C ATOM 1557 CE3 TRP A 192 -15.187 -7.788 27.295 1.00 8.90 C ANISOU 1557 CE3 TRP A 192 840 1368 1172 0 -111 -145 C ATOM 1558 CZ2 TRP A 192 -15.999 -9.902 28.980 1.00 9.74 C ANISOU 1558 CZ2 TRP A 192 1153 1077 1472 133 -139 8 C ATOM 1559 CZ3 TRP A 192 -15.484 -9.035 26.789 1.00 10.21 C ANISOU 1559 CZ3 TRP A 192 1034 1446 1398 -60 -142 -292 C ATOM 1560 CH2 TRP A 192 -15.892 -10.074 27.626 1.00 10.24 C ANISOU 1560 CH2 TRP A 192 1011 1312 1567 94 -177 -227 C ATOM 1561 N THR A 193 -14.289 -1.969 29.663 1.00 6.44 N ANISOU 1561 N THR A 193 787 1052 607 -63 -19 18 N ATOM 1562 CA THR A 193 -13.570 -0.746 29.342 1.00 6.23 C ANISOU 1562 CA THR A 193 767 996 605 -34 2 -13 C ATOM 1563 C THR A 193 -12.329 -0.579 30.208 1.00 6.22 C ANISOU 1563 C THR A 193 783 973 607 17 -10 -24 C ATOM 1564 O THR A 193 -12.303 -0.963 31.379 1.00 7.34 O ANISOU 1564 O THR A 193 883 1261 645 -56 -96 32 O ATOM 1565 CB THR A 193 -14.518 0.494 29.456 1.00 6.96 C ANISOU 1565 CB THR A 193 864 1022 758 6 -16 -21 C ATOM 1566 OG1 THR A 193 -13.837 1.676 29.038 1.00 7.46 O ANISOU 1566 OG1 THR A 193 947 1031 858 27 -8 -33 O ATOM 1567 CG2 THR A 193 -15.041 0.700 30.856 1.00 7.81 C ANISOU 1567 CG2 THR A 193 915 1197 857 73 112 -64 C ATOM 1568 N TYR A 194 -11.297 0.027 29.611 1.00 6.48 N ANISOU 1568 N TYR A 194 800 1030 633 12 -108 -46 N ATOM 1569 CA TYR A 194 -10.066 0.323 30.331 1.00 6.45 C ANISOU 1569 CA TYR A 194 775 1041 634 43 -76 -29 C ATOM 1570 C TYR A 194 -9.300 1.394 29.529 1.00 6.26 C ANISOU 1570 C TYR A 194 794 970 613 74 -78 -58 C ATOM 1571 O TYR A 194 -9.524 1.561 28.330 1.00 6.64 O ANISOU 1571 O TYR A 194 874 1054 595 -24 -148 -37 O ATOM 1572 CB TYR A 194 -9.230 -0.965 30.525 1.00 6.72 C ANISOU 1572 CB TYR A 194 856 1040 658 50 -85 -20 C ATOM 1573 CG TYR A 194 -8.533 -1.426 29.259 1.00 6.62 C ANISOU 1573 CG TYR A 194 850 997 669 42 -88 27 C ATOM 1574 CD1 TYR A 194 -9.211 -2.142 28.283 1.00 6.38 C ANISOU 1574 CD1 TYR A 194 759 926 739 62 -87 13 C ATOM 1575 CD2 TYR A 194 -7.204 -1.071 29.017 1.00 6.72 C ANISOU 1575 CD2 TYR A 194 822 986 744 -4 -122 -47 C ATOM 1576 CE1 TYR A 194 -8.578 -2.507 27.075 1.00 6.19 C ANISOU 1576 CE1 TYR A 194 768 875 710 40 -77 8 C ATOM 1577 CE2 TYR A 194 -6.565 -1.414 27.832 1.00 6.64 C ANISOU 1577 CE2 TYR A 194 786 992 744 -8 -73 -39 C ATOM 1578 CZ TYR A 194 -7.249 -2.114 26.863 1.00 6.44 C ANISOU 1578 CZ TYR A 194 841 902 703 27 -82 -5 C ATOM 1579 OH TYR A 194 -6.583 -2.419 25.694 1.00 6.56 O ANISOU 1579 OH TYR A 194 809 931 754 -51 12 -75 O ATOM 1580 N PRO A 195 -8.351 2.082 30.195 1.00 6.44 N ANISOU 1580 N PRO A 195 760 1061 626 9 -56 -124 N ATOM 1581 CA PRO A 195 -7.524 3.083 29.506 1.00 6.49 C ANISOU 1581 CA PRO A 195 806 937 722 13 -48 -162 C ATOM 1582 C PRO A 195 -6.315 2.411 28.832 1.00 6.09 C ANISOU 1582 C PRO A 195 713 920 680 -10 -120 -106 C ATOM 1583 O PRO A 195 -5.587 1.650 29.488 1.00 6.97 O ANISOU 1583 O PRO A 195 824 1154 672 76 -96 -33 O ATOM 1584 CB PRO A 195 -7.054 4.006 30.640 1.00 7.68 C ANISOU 1584 CB PRO A 195 968 1120 831 -48 -42 -238 C ATOM 1585 CG PRO A 195 -7.013 3.109 31.846 1.00 8.37 C ANISOU 1585 CG PRO A 195 1034 1343 802 -158 6 -299 C ATOM 1586 CD PRO A 195 -8.167 2.115 31.653 1.00 8.04 C ANISOU 1586 CD PRO A 195 953 1369 732 -115 -56 -203 C ATOM 1587 N GLY A 196 -6.085 2.727 27.570 1.00 5.98 N ANISOU 1587 N GLY A 196 739 877 655 9 -65 -87 N ATOM 1588 CA GLY A 196 -4.968 2.100 26.852 1.00 6.34 C ANISOU 1588 CA GLY A 196 804 868 738 35 -2 -50 C ATOM 1589 C GLY A 196 -4.410 2.982 25.755 1.00 5.95 C ANISOU 1589 C GLY A 196 695 779 787 7 -76 -79 C ATOM 1590 O GLY A 196 -4.344 4.218 25.874 1.00 6.64 O ANISOU 1590 O GLY A 196 826 845 853 -57 -17 -88 O ATOM 1591 N SER A 197 -4.011 2.317 24.678 1.00 6.08 N ANISOU 1591 N SER A 197 772 811 728 -41 -23 -72 N ATOM 1592 CA SER A 197 -3.190 2.956 23.645 1.00 6.33 C ANISOU 1592 CA SER A 197 749 838 818 -17 -15 -5 C ATOM 1593 C SER A 197 -3.643 2.554 22.262 1.00 5.85 C ANISOU 1593 C SER A 197 693 753 777 48 5 -55 C ATOM 1594 O SER A 197 -4.419 1.608 22.075 1.00 6.21 O ANISOU 1594 O SER A 197 745 841 776 -43 -71 -58 O ATOM 1595 CB SER A 197 -1.685 2.550 23.806 1.00 6.59 C ANISOU 1595 CB SER A 197 739 901 864 -12 -91 -80 C ATOM 1596 OG SER A 197 -1.465 1.211 23.386 1.00 6.50 O ANISOU 1596 OG SER A 197 804 866 800 -18 -25 -39 O ATOM 1597 N LEU A 198 -3.113 3.251 21.256 1.00 6.30 N ANISOU 1597 N LEU A 198 796 836 760 -7 26 -56 N ATOM 1598 CA LEU A 198 -3.113 2.715 19.903 1.00 6.51 C ANISOU 1598 CA LEU A 198 803 917 754 -30 44 -34 C ATOM 1599 C LEU A 198 -2.377 1.367 19.907 1.00 6.10 C ANISOU 1599 C LEU A 198 700 902 716 -34 20 -69 C ATOM 1600 O LEU A 198 -1.389 1.194 20.633 1.00 6.88 O ANISOU 1600 O LEU A 198 778 1000 836 -19 -60 -144 O ATOM 1601 CB LEU A 198 -2.358 3.642 18.938 1.00 7.72 C ANISOU 1601 CB LEU A 198 1092 919 924 -32 61 43 C ATOM 1602 CG LEU A 198 -2.695 5.128 18.956 1.00 11.31 C ANISOU 1602 CG LEU A 198 1656 1175 1466 211 358 378 C ATOM 1603 CD1 LEU A 198 -1.841 5.857 17.909 1.00 11.87 C ANISOU 1603 CD1 LEU A 198 1828 1186 1498 -154 232 202 C ATOM 1604 CD2 LEU A 198 -4.138 5.362 18.703 1.00 13.71 C ANISOU 1604 CD2 LEU A 198 1682 1729 1798 454 496 719 C ATOM 1605 N THR A 199 -2.820 0.431 19.065 1.00 6.39 N ANISOU 1605 N THR A 199 763 862 802 2 -18 -66 N ATOM 1606 CA THR A 199 -2.135 -0.856 18.992 1.00 6.27 C ANISOU 1606 CA THR A 199 755 853 773 24 -63 -77 C ATOM 1607 C THR A 199 -1.124 -0.949 17.837 1.00 6.29 C ANISOU 1607 C THR A 199 709 868 812 -29 -76 -94 C ATOM 1608 O THR A 199 -0.501 -1.993 17.662 1.00 6.94 O ANISOU 1608 O THR A 199 787 918 931 15 -40 -49 O ATOM 1609 CB THR A 199 -3.103 -2.044 18.910 1.00 6.02 C ANISOU 1609 CB THR A 199 745 862 681 -37 -70 -48 C ATOM 1610 OG1 THR A 199 -3.726 -2.049 17.640 1.00 6.53 O ANISOU 1610 OG1 THR A 199 855 897 730 -49 -107 37 O ATOM 1611 CG2 THR A 199 -4.143 -2.005 20.053 1.00 7.15 C ANISOU 1611 CG2 THR A 199 855 1056 806 -55 89 4 C ATOM 1612 N THR A 200 -0.987 0.145 17.083 1.00 6.78 N ANISOU 1612 N THR A 200 753 927 898 -44 30 -81 N ATOM 1613 CA THR A 200 0.051 0.273 16.058 1.00 7.07 C ANISOU 1613 CA THR A 200 773 1011 900 -82 18 -101 C ATOM 1614 C THR A 200 0.897 1.502 16.407 1.00 7.14 C ANISOU 1614 C THR A 200 815 1021 878 -34 39 -44 C ATOM 1615 O THR A 200 0.417 2.459 17.001 1.00 7.46 O ANISOU 1615 O THR A 200 893 968 976 -165 26 -72 O ATOM 1616 CB THR A 200 -0.550 0.470 14.664 1.00 7.90 C ANISOU 1616 CB THR A 200 912 1071 1021 -120 -59 -2 C ATOM 1617 OG1 THR A 200 -1.554 1.505 14.727 1.00 9.15 O ANISOU 1617 OG1 THR A 200 1142 1126 1209 -9 -255 83 O ATOM 1618 CG2 THR A 200 -1.180 -0.807 14.187 1.00 8.61 C ANISOU 1618 CG2 THR A 200 1095 1136 1040 -78 -86 -108 C ATOM 1619 N PRO A 201 2.180 1.492 15.977 1.00 7.80 N ANISOU 1619 N PRO A 201 852 1139 973 -84 12 -55 N ATOM 1620 CA PRO A 201 2.995 2.715 16.076 1.00 8.12 C ANISOU 1620 CA PRO A 201 797 1249 1041 -163 73 5 C ATOM 1621 C PRO A 201 2.210 3.907 15.524 1.00 8.63 C ANISOU 1621 C PRO A 201 1024 1249 1009 -178 83 22 C ATOM 1622 O PRO A 201 1.596 3.798 14.463 1.00 9.80 O ANISOU 1622 O PRO A 201 1220 1475 1028 -169 -76 57 O ATOM 1623 CB PRO A 201 4.231 2.359 15.240 1.00 9.63 C ANISOU 1623 CB PRO A 201 933 1489 1236 -219 162 -173 C ATOM 1624 CG PRO A 201 4.377 0.890 15.474 1.00 9.41 C ANISOU 1624 CG PRO A 201 847 1526 1204 -65 47 -191 C ATOM 1625 CD PRO A 201 2.957 0.376 15.399 1.00 8.26 C ANISOU 1625 CD PRO A 201 767 1269 1102 -23 38 -159 C ATOM 1626 N PRO A 202 2.221 5.044 16.239 1.00 8.86 N ANISOU 1626 N PRO A 202 1120 1220 1026 -179 57 115 N ATOM 1627 CA PRO A 202 3.125 5.412 17.337 1.00 8.64 C ANISOU 1627 CA PRO A 202 1042 1186 1054 -282 70 -23 C ATOM 1628 C PRO A 202 2.724 4.963 18.756 1.00 7.80 C ANISOU 1628 C PRO A 202 851 1074 1040 -141 7 -50 C ATOM 1629 O PRO A 202 3.369 5.400 19.702 1.00 8.57 O ANISOU 1629 O PRO A 202 1003 1149 1106 -243 60 -58 O ATOM 1630 CB PRO A 202 3.153 6.938 17.239 1.00 10.95 C ANISOU 1630 CB PRO A 202 1584 1185 1392 -276 171 42 C ATOM 1631 CG PRO A 202 1.813 7.293 16.716 1.00 11.91 C ANISOU 1631 CG PRO A 202 1780 1186 1558 -147 31 86 C ATOM 1632 CD PRO A 202 1.500 6.220 15.711 1.00 10.92 C ANISOU 1632 CD PRO A 202 1592 1252 1305 -34 -17 156 C ATOM 1633 N LEU A 203 1.698 4.120 18.902 1.00 7.18 N ANISOU 1633 N LEU A 203 833 948 947 -65 22 -35 N ATOM 1634 CA LEU A 203 1.421 3.469 20.193 1.00 7.06 C ANISOU 1634 CA LEU A 203 812 917 953 -47 -26 -88 C ATOM 1635 C LEU A 203 1.047 4.472 21.286 1.00 7.00 C ANISOU 1635 C LEU A 203 736 957 967 -59 -22 -39 C ATOM 1636 O LEU A 203 1.201 4.214 22.479 1.00 7.50 O ANISOU 1636 O LEU A 203 883 977 991 -38 -29 -126 O ATOM 1637 CB LEU A 203 2.563 2.540 20.641 1.00 7.16 C ANISOU 1637 CB LEU A 203 754 1022 946 -11 -22 -114 C ATOM 1638 CG LEU A 203 2.914 1.421 19.668 1.00 7.31 C ANISOU 1638 CG LEU A 203 722 1073 980 47 -33 -125 C ATOM 1639 CD1 LEU A 203 4.220 0.737 20.133 1.00 8.41 C ANISOU 1639 CD1 LEU A 203 872 1125 1200 47 -89 -148 C ATOM 1640 CD2 LEU A 203 1.819 0.391 19.542 1.00 7.88 C ANISOU 1640 CD2 LEU A 203 822 1098 1075 44 -91 -167 C ATOM 1641 N LEU A 204 0.468 5.605 20.885 1.00 7.54 N ANISOU 1641 N LEU A 204 879 922 1064 -34 71 -56 N ATOM 1642 CA LEU A 204 0.197 6.693 21.808 1.00 7.88 C ANISOU 1642 CA LEU A 204 923 905 1166 -94 104 -48 C ATOM 1643 C LEU A 204 -0.880 6.270 22.833 1.00 7.07 C ANISOU 1643 C LEU A 204 791 842 1055 -3 0 -133 C ATOM 1644 O LEU A 204 -1.860 5.584 22.496 1.00 7.42 O ANISOU 1644 O LEU A 204 918 898 1002 -54 -9 -125 O ATOM 1645 CB LEU A 204 -0.258 7.940 21.048 1.00 8.68 C ANISOU 1645 CB LEU A 204 1012 921 1365 -34 204 63 C ATOM 1646 CG LEU A 204 0.828 8.539 20.150 1.00 10.48 C ANISOU 1646 CG LEU A 204 1138 1132 1712 12 290 253 C ATOM 1647 CD1 LEU A 204 0.244 9.610 19.259 1.00 11.75 C ANISOU 1647 CD1 LEU A 204 1494 1172 1798 172 609 399 C ATOM 1648 CD2 LEU A 204 1.967 9.101 21.007 1.00 13.51 C ANISOU 1648 CD2 LEU A 204 1291 1568 2275 -477 145 270 C ATOM 1649 N GLU A 205 -0.691 6.732 24.065 1.00 7.59 N ANISOU 1649 N GLU A 205 799 993 1090 -64 -9 -138 N ATOM 1650 CA GLU A 205 -1.541 6.363 25.197 1.00 7.20 C ANISOU 1650 CA GLU A 205 771 958 1005 -60 -68 -183 C ATOM 1651 C GLU A 205 -2.711 7.335 25.352 1.00 7.17 C ANISOU 1651 C GLU A 205 789 916 1020 -40 -71 -196 C ATOM 1652 O GLU A 205 -2.820 8.091 26.312 1.00 8.84 O ANISOU 1652 O GLU A 205 1054 1278 1026 152 -158 -288 O ATOM 1653 CB GLU A 205 -0.666 6.209 26.445 1.00 7.96 C ANISOU 1653 CB GLU A 205 875 1083 1065 -13 -168 -183 C ATOM 1654 CG GLU A 205 0.242 4.990 26.306 1.00 8.34 C ANISOU 1654 CG GLU A 205 899 1173 1097 13 -177 -179 C ATOM 1655 CD GLU A 205 1.180 4.722 27.475 1.00 8.81 C ANISOU 1655 CD GLU A 205 909 1274 1166 2 -210 -220 C ATOM 1656 OE1 GLU A 205 1.506 5.669 28.212 1.00 10.48 O ANISOU 1656 OE1 GLU A 205 1121 1491 1372 16 -389 -443 O ATOM 1657 OE2 GLU A 205 1.586 3.540 27.610 1.00 8.71 O ANISOU 1657 OE2 GLU A 205 909 1313 1087 33 -167 -125 O ATOM 1658 N CYS A 206 -3.615 7.245 24.384 1.00 6.73 N ANISOU 1658 N CYS A 206 790 811 955 -43 -76 -88 N ATOM 1659 CA CYS A 206 -4.660 8.237 24.189 1.00 6.84 C ANISOU 1659 CA CYS A 206 852 816 930 -111 -70 -99 C ATOM 1660 C CYS A 206 -6.055 7.620 24.070 1.00 6.66 C ANISOU 1660 C CYS A 206 789 803 939 -36 -66 -72 C ATOM 1661 O CYS A 206 -6.979 8.340 23.714 1.00 8.01 O ANISOU 1661 O CYS A 206 909 873 1263 14 -201 2 O ATOM 1662 CB CYS A 206 -4.383 9.089 22.941 1.00 8.01 C ANISOU 1662 CB CYS A 206 1096 929 1019 -74 63 -36 C ATOM 1663 SG CYS A 206 -4.346 8.102 21.402 1.00 8.26 S ANISOU 1663 SG CYS A 206 1356 909 875 -5 -32 -20 S ATOM 1664 N VAL A 207 -6.193 6.320 24.349 1.00 6.39 N ANISOU 1664 N VAL A 207 732 739 957 -30 4 -31 N ATOM 1665 CA VAL A 207 -7.434 5.605 24.007 1.00 6.19 C ANISOU 1665 CA VAL A 207 713 744 893 -45 -58 -9 C ATOM 1666 C VAL A 207 -8.217 5.155 25.243 1.00 6.60 C ANISOU 1666 C VAL A 207 810 818 879 23 -118 -4 C ATOM 1667 O VAL A 207 -7.661 4.495 26.116 1.00 7.63 O ANISOU 1667 O VAL A 207 822 1074 1003 -10 -118 143 O ATOM 1668 CB VAL A 207 -7.144 4.350 23.147 1.00 6.42 C ANISOU 1668 CB VAL A 207 680 814 944 -54 -53 -45 C ATOM 1669 CG1 VAL A 207 -8.445 3.625 22.791 1.00 6.67 C ANISOU 1669 CG1 VAL A 207 794 843 898 -60 -117 -30 C ATOM 1670 CG2 VAL A 207 -6.369 4.719 21.880 1.00 7.22 C ANISOU 1670 CG2 VAL A 207 783 991 969 42 61 4 C ATOM 1671 N THR A 208 -9.519 5.476 25.265 1.00 6.29 N ANISOU 1671 N THR A 208 817 807 764 -6 -47 -37 N ATOM 1672 CA THR A 208 -10.476 4.745 26.121 1.00 6.28 C ANISOU 1672 CA THR A 208 811 764 809 -64 11 -49 C ATOM 1673 C THR A 208 -10.994 3.579 25.274 1.00 6.00 C ANISOU 1673 C THR A 208 780 778 722 -21 -11 7 C ATOM 1674 O THR A 208 -11.676 3.779 24.272 1.00 6.42 O ANISOU 1674 O THR A 208 877 838 724 -12 -203 -11 O ATOM 1675 CB THR A 208 -11.634 5.631 26.576 1.00 7.10 C ANISOU 1675 CB THR A 208 851 889 956 -29 19 -132 C ATOM 1676 OG1 THR A 208 -11.124 6.753 27.307 1.00 7.96 O ANISOU 1676 OG1 THR A 208 1079 917 1030 -23 25 -174 O ATOM 1677 CG2 THR A 208 -12.573 4.826 27.463 1.00 8.05 C ANISOU 1677 CG2 THR A 208 907 1086 1065 -84 111 -112 C ATOM 1678 N TRP A 209 -10.631 2.365 25.691 1.00 5.83 N ANISOU 1678 N TRP A 209 762 781 673 6 -40 -11 N ATOM 1679 CA TRP A 209 -11.087 1.169 25.001 1.00 5.55 C ANISOU 1679 CA TRP A 209 744 738 626 -28 -100 -15 C ATOM 1680 C TRP A 209 -12.446 0.734 25.520 1.00 5.56 C ANISOU 1680 C TRP A 209 774 737 602 16 -44 3 C ATOM 1681 O TRP A 209 -12.675 0.696 26.731 1.00 6.38 O ANISOU 1681 O TRP A 209 837 960 628 -42 -61 -31 O ATOM 1682 CB TRP A 209 -10.065 0.018 25.218 1.00 6.01 C ANISOU 1682 CB TRP A 209 802 820 660 32 -116 19 C ATOM 1683 CG TRP A 209 -8.916 0.123 24.259 1.00 5.96 C ANISOU 1683 CG TRP A 209 743 765 758 45 -132 0 C ATOM 1684 CD1 TRP A 209 -7.702 0.718 24.467 1.00 6.94 C ANISOU 1684 CD1 TRP A 209 833 902 904 35 -89 -6 C ATOM 1685 CD2 TRP A 209 -8.947 -0.288 22.899 1.00 5.97 C ANISOU 1685 CD2 TRP A 209 741 737 789 53 -65 -6 C ATOM 1686 NE1 TRP A 209 -6.964 0.698 23.300 1.00 6.88 N ANISOU 1686 NE1 TRP A 209 715 936 962 37 -55 -5 N ATOM 1687 CE2 TRP A 209 -7.706 0.081 22.322 1.00 6.63 C ANISOU 1687 CE2 TRP A 209 794 832 893 54 -62 9 C ATOM 1688 CE3 TRP A 209 -9.895 -0.945 22.105 1.00 6.08 C ANISOU 1688 CE3 TRP A 209 803 769 740 27 -78 -33 C ATOM 1689 CZ2 TRP A 209 -7.397 -0.196 20.986 1.00 7.30 C ANISOU 1689 CZ2 TRP A 209 881 1018 874 146 111 -14 C ATOM 1690 CZ3 TRP A 209 -9.592 -1.217 20.793 1.00 6.99 C ANISOU 1690 CZ3 TRP A 209 1058 866 733 57 -54 -57 C ATOM 1691 CH2 TRP A 209 -8.354 -0.846 20.245 1.00 7.25 C ANISOU 1691 CH2 TRP A 209 1125 806 825 151 57 -50 C ATOM 1692 N ILE A 210 -13.329 0.388 24.579 1.00 5.62 N ANISOU 1692 N ILE A 210 760 744 632 -22 -47 8 N ATOM 1693 CA ILE A 210 -14.659 -0.156 24.878 1.00 5.78 C ANISOU 1693 CA ILE A 210 701 790 707 -82 -23 12 C ATOM 1694 C ILE A 210 -14.747 -1.423 24.034 1.00 5.82 C ANISOU 1694 C ILE A 210 696 815 701 -16 -28 24 C ATOM 1695 O ILE A 210 -14.863 -1.334 22.820 1.00 6.47 O ANISOU 1695 O ILE A 210 1062 803 592 3 -70 6 O ATOM 1696 CB ILE A 210 -15.754 0.871 24.530 1.00 6.58 C ANISOU 1696 CB ILE A 210 758 851 893 -19 -16 -43 C ATOM 1697 CG1 ILE A 210 -15.539 2.151 25.348 1.00 8.04 C ANISOU 1697 CG1 ILE A 210 954 906 1194 87 -46 -196 C ATOM 1698 CG2 ILE A 210 -17.129 0.253 24.748 1.00 7.38 C ANISOU 1698 CG2 ILE A 210 724 1046 1033 -43 -25 14 C ATOM 1699 CD1 ILE A 210 -16.371 3.335 24.891 1.00 9.30 C ANISOU 1699 CD1 ILE A 210 1092 954 1489 198 -191 -144 C ATOM 1700 N VAL A 211 -14.650 -2.584 24.684 1.00 5.67 N ANISOU 1700 N VAL A 211 753 740 662 -21 -66 40 N ATOM 1701 CA VAL A 211 -14.592 -3.863 23.997 1.00 5.82 C ANISOU 1701 CA VAL A 211 807 738 669 -71 -26 29 C ATOM 1702 C VAL A 211 -15.906 -4.599 24.255 1.00 6.03 C ANISOU 1702 C VAL A 211 824 803 665 -49 -34 52 C ATOM 1703 O VAL A 211 -16.240 -4.893 25.399 1.00 6.73 O ANISOU 1703 O VAL A 211 844 1063 648 -132 20 45 O ATOM 1704 CB VAL A 211 -13.380 -4.709 24.457 1.00 6.30 C ANISOU 1704 CB VAL A 211 799 784 809 -61 -21 24 C ATOM 1705 CG1 VAL A 211 -13.374 -6.050 23.756 1.00 7.42 C ANISOU 1705 CG1 VAL A 211 987 863 967 27 -17 0 C ATOM 1706 CG2 VAL A 211 -12.083 -3.950 24.187 1.00 7.32 C ANISOU 1706 CG2 VAL A 211 874 874 1035 -12 -1 113 C ATOM 1707 N LEU A 212 -16.658 -4.863 23.192 1.00 6.59 N ANISOU 1707 N LEU A 212 811 1004 688 -122 3 43 N ATOM 1708 CA LEU A 212 -17.950 -5.531 23.351 1.00 6.87 C ANISOU 1708 CA LEU A 212 795 1016 799 -199 -32 -28 C ATOM 1709 C LEU A 212 -17.770 -6.993 23.723 1.00 7.02 C ANISOU 1709 C LEU A 212 852 996 818 -146 -91 15 C ATOM 1710 O LEU A 212 -16.911 -7.693 23.190 1.00 7.57 O ANISOU 1710 O LEU A 212 914 1048 916 -117 -48 5 O ATOM 1711 CB LEU A 212 -18.784 -5.392 22.078 1.00 7.30 C ANISOU 1711 CB LEU A 212 830 1089 854 -108 -104 -6 C ATOM 1712 CG LEU A 212 -19.164 -3.983 21.648 1.00 7.97 C ANISOU 1712 CG LEU A 212 938 1101 988 -6 -129 25 C ATOM 1713 CD1 LEU A 212 -20.196 -4.049 20.511 1.00 10.06 C ANISOU 1713 CD1 LEU A 212 1086 1505 1230 -41 -350 120 C ATOM 1714 CD2 LEU A 212 -19.717 -3.160 22.790 1.00 9.18 C ANISOU 1714 CD2 LEU A 212 1090 1271 1127 71 25 14 C ATOM 1715 N LYS A 213 -18.621 -7.471 24.633 1.00 7.52 N ANISOU 1715 N LYS A 213 896 1107 855 -215 -70 74 N ATOM 1716 CA LYS A 213 -18.595 -8.867 25.030 1.00 8.38 C ANISOU 1716 CA LYS A 213 1074 1189 922 -293 -171 269 C ATOM 1717 C LYS A 213 -19.063 -9.822 23.941 1.00 7.95 C ANISOU 1717 C LYS A 213 952 1066 1002 -175 -106 189 C ATOM 1718 O LYS A 213 -18.539 -10.928 23.812 1.00 9.65 O ANISOU 1718 O LYS A 213 1140 1148 1378 -68 -256 223 O ATOM 1719 CB LYS A 213 -19.415 -9.078 26.302 1.00 11.93 C ANISOU 1719 CB LYS A 213 1641 1703 1190 -737 -71 309 C ATOM 1720 CG LYS A 213 -19.534 -10.529 26.730 1.00 17.54 C ANISOU 1720 CG LYS A 213 2791 2117 1755 -1060 -122 749 C ATOM 1721 CD LYS A 213 -20.067 -10.663 28.141 1.00 23.74 C ANISOU 1721 CD LYS A 213 3495 2772 2754 -658 334 669 C ATOM 1722 CE LYS A 213 -21.262 -9.748 28.390 1.00 33.36 C ANISOU 1722 CE LYS A 213 3791 4203 4680 -68 106 -767 C ATOM 1723 NZ LYS A 213 -22.556 -10.308 27.908 1.00 34.23 N ANISOU 1723 NZ LYS A 213 4214 3245 5546 203 -477 -1182 N ATOM 1724 N AGLU A 214 -20.092 -9.435 23.198 0.51 7.50 N ANISOU 1724 N AGLU A 214 887 1059 905 -157 -50 83 N ATOM 1725 N BGLU A 214 -20.085 -9.433 23.181 0.49 7.30 N ANISOU 1725 N BGLU A 214 840 1048 886 -153 -37 71 N ATOM 1726 CA AGLU A 214 -20.689 -10.330 22.226 0.51 7.78 C ANISOU 1726 CA AGLU A 214 908 1075 972 -188 -30 64 C ATOM 1727 CA BGLU A 214 -20.644 -10.323 22.173 0.49 7.70 C ANISOU 1727 CA BGLU A 214 848 1072 1005 -144 -70 55 C ATOM 1728 C AGLU A 214 -19.924 -10.241 20.913 0.51 7.10 C ANISOU 1728 C AGLU A 214 878 930 891 -169 -99 86 C ATOM 1729 C BGLU A 214 -19.895 -10.208 20.850 0.49 7.46 C ANISOU 1729 C BGLU A 214 883 1031 919 -137 -77 57 C ATOM 1730 O AGLU A 214 -19.816 -9.157 20.352 0.51 7.22 O ANISOU 1730 O AGLU A 214 817 979 945 -124 -46 156 O ATOM 1731 O BGLU A 214 -19.892 -9.139 20.242 0.49 7.86 O ANISOU 1731 O BGLU A 214 937 1070 978 -69 -41 140 O ATOM 1732 CB AGLU A 214 -22.143 -9.924 21.990 0.51 8.54 C ANISOU 1732 CB AGLU A 214 949 1165 1130 -207 -52 -46 C ATOM 1733 CB BGLU A 214 -22.136 -10.026 21.940 0.49 8.90 C ANISOU 1733 CB BGLU A 214 888 1206 1287 -170 -178 51 C ATOM 1734 CG AGLU A 214 -22.901 -10.863 21.064 0.51 9.93 C ANISOU 1734 CG AGLU A 214 1050 1299 1422 -411 -56 -105 C ATOM 1735 CG BGLU A 214 -22.768 -10.961 20.905 0.49 11.27 C ANISOU 1735 CG BGLU A 214 1102 1317 1862 -79 -474 -164 C ATOM 1736 CD AGLU A 214 -24.279 -10.335 20.689 0.51 11.56 C ANISOU 1736 CD AGLU A 214 1176 1521 1694 -322 -313 -172 C ATOM 1737 CD BGLU A 214 -24.295 -10.862 20.815 0.49 12.45 C ANISOU 1737 CD BGLU A 214 1082 1384 2265 -301 -541 -18 C ATOM 1738 OE1AGLU A 214 -24.956 -9.776 21.575 0.51 12.46 O ANISOU 1738 OE1AGLU A 214 1249 1425 2062 -158 -250 -386 O ATOM 1739 OE1BGLU A 214 -24.886 -9.836 21.208 0.49 10.95 O ANISOU 1739 OE1BGLU A 214 906 1508 1748 -182 -381 202 O ATOM 1740 OE2AGLU A 214 -24.686 -10.478 19.514 0.51 13.51 O ANISOU 1740 OE2AGLU A 214 1682 1819 1631 -426 -337 72 O ATOM 1741 OE2BGLU A 214 -24.904 -11.822 20.322 0.49 15.73 O ANISOU 1741 OE2BGLU A 214 1494 1380 3103 -370 -895 -52 O ATOM 1742 N APRO A 215 -19.405 -11.368 20.398 0.51 7.88 N ANISOU 1742 N APRO A 215 1146 917 933 -86 -4 59 N ATOM 1743 N BPRO A 215 -19.274 -11.306 20.391 0.49 7.55 N ANISOU 1743 N BPRO A 215 940 960 970 -164 -42 43 N ATOM 1744 CA APRO A 215 -18.759 -11.276 19.086 0.51 7.77 C ANISOU 1744 CA APRO A 215 1061 940 950 -83 -13 -2 C ATOM 1745 CA BPRO A 215 -18.653 -11.327 19.065 0.49 7.65 C ANISOU 1745 CA BPRO A 215 885 1038 986 -91 -51 -33 C ATOM 1746 C APRO A 215 -19.782 -11.178 17.976 0.51 7.76 C ANISOU 1746 C APRO A 215 1055 944 949 -276 -70 -43 C ATOM 1747 C BPRO A 215 -19.694 -11.343 17.950 0.49 7.91 C ANISOU 1747 C BPRO A 215 862 1179 964 -114 -76 -6 C ATOM 1748 O APRO A 215 -20.964 -11.431 18.193 0.51 9.88 O ANISOU 1748 O APRO A 215 1155 1499 1100 -435 -98 99 O ATOM 1749 O BPRO A 215 -20.823 -11.816 18.146 0.49 9.17 O ANISOU 1749 O BPRO A 215 1094 1406 984 -430 -140 -68 O ATOM 1750 CB APRO A 215 -18.020 -12.611 18.967 0.51 8.30 C ANISOU 1750 CB APRO A 215 1098 925 1132 -153 -11 -132 C ATOM 1751 CB BPRO A 215 -17.857 -12.645 19.065 0.49 8.71 C ANISOU 1751 CB BPRO A 215 1098 1068 1144 57 -60 -51 C ATOM 1752 CG APRO A 215 -18.831 -13.563 19.783 0.51 8.36 C ANISOU 1752 CG APRO A 215 1125 888 1165 -168 -55 -85 C ATOM 1753 CG BPRO A 215 -17.839 -13.114 20.489 0.49 10.46 C ANISOU 1753 CG BPRO A 215 1603 1183 1188 243 175 71 C ATOM 1754 CD APRO A 215 -19.408 -12.745 20.923 0.51 8.97 C ANISOU 1754 CD APRO A 215 1378 887 1144 -108 96 37 C ATOM 1755 CD BPRO A 215 -19.096 -12.586 21.098 0.49 9.08 C ANISOU 1755 CD BPRO A 215 1339 987 1126 -72 81 95 C ATOM 1756 N ILE A 216 -19.311 -10.827 16.787 1.00 7.83 N ANISOU 1756 N ILE A 216 1071 1011 893 -85 -40 -109 N ATOM 1757 CA ILE A 216 -20.077 -11.045 15.584 1.00 7.59 C ANISOU 1757 CA ILE A 216 1000 960 925 -80 -112 -133 C ATOM 1758 C ILE A 216 -19.538 -12.297 14.890 1.00 7.87 C ANISOU 1758 C ILE A 216 1033 893 1065 -108 -204 -99 C ATOM 1759 O ILE A 216 -18.380 -12.666 15.057 1.00 9.06 O ANISOU 1759 O ILE A 216 1089 1061 1292 -85 -104 -223 O ATOM 1760 CB ILE A 216 -20.074 -9.827 14.638 1.00 8.06 C ANISOU 1760 CB ILE A 216 1045 1002 1017 -32 -77 -89 C ATOM 1761 CG1 ILE A 216 -18.665 -9.478 14.125 1.00 8.48 C ANISOU 1761 CG1 ILE A 216 1088 1090 1045 -61 -95 73 C ATOM 1762 CG2 ILE A 216 -20.748 -8.627 15.320 1.00 8.94 C ANISOU 1762 CG2 ILE A 216 1174 1074 1151 93 -32 -185 C ATOM 1763 CD1 ILE A 216 -18.661 -8.494 12.970 1.00 10.67 C ANISOU 1763 CD1 ILE A 216 1560 1290 1203 -122 67 146 C ATOM 1764 N ASER A 217 -20.404 -12.978 14.152 0.82 8.87 N ANISOU 1764 N ASER A 217 1166 985 1220 -14 -228 -171 N ATOM 1765 N BSER A 217 -20.398 -12.914 14.093 0.18 8.11 N ANISOU 1765 N BSER A 217 1203 727 1151 -203 -258 -73 N ATOM 1766 CA ASER A 217 -19.988 -14.101 13.322 0.82 9.58 C ANISOU 1766 CA ASER A 217 1330 1010 1299 -88 -299 -211 C ATOM 1767 CA BSER A 217 -20.031 -14.075 13.308 0.18 8.65 C ANISOU 1767 CA BSER A 217 1551 691 1045 -267 -128 17 C ATOM 1768 C ASER A 217 -19.807 -13.652 11.890 0.82 8.99 C ANISOU 1768 C ASER A 217 1302 980 1133 -3 -261 -139 C ATOM 1769 C BSER A 217 -19.825 -13.667 11.855 0.18 8.38 C ANISOU 1769 C BSER A 217 1263 917 1003 -76 -358 33 C ATOM 1770 O ASER A 217 -20.653 -12.919 11.358 0.82 9.72 O ANISOU 1770 O ASER A 217 1269 1156 1267 -62 -179 -3 O ATOM 1771 O BSER A 217 -20.643 -12.944 11.280 0.18 11.09 O ANISOU 1771 O BSER A 217 2148 1329 738 757 -383 -372 O ATOM 1772 CB ASER A 217 -21.037 -15.221 13.355 0.82 13.91 C ANISOU 1772 CB ASER A 217 2271 1178 1835 -543 96 -106 C ATOM 1773 CB BSER A 217 -21.128 -15.139 13.416 0.18 9.58 C ANISOU 1773 CB BSER A 217 1968 659 1013 -424 185 -84 C ATOM 1774 OG ASER A 217 -21.147 -15.813 14.631 0.82 18.37 O ANISOU 1774 OG ASER A 217 2494 2314 2171 -790 -284 386 O ATOM 1775 OG BSER A 217 -20.794 -16.305 12.689 0.18 8.17 O ANISOU 1775 OG BSER A 217 1326 538 1239 -82 -121 -30 O ATOM 1776 N VAL A 218 -18.717 -14.122 11.275 1.00 8.56 N ANISOU 1776 N VAL A 218 1303 869 1079 -89 -313 -143 N ATOM 1777 CA VAL A 218 -18.445 -13.933 9.857 1.00 8.50 C ANISOU 1777 CA VAL A 218 1225 867 1140 -121 -238 -113 C ATOM 1778 C VAL A 218 -18.190 -15.314 9.251 1.00 8.28 C ANISOU 1778 C VAL A 218 1196 854 1095 -108 -234 -102 C ATOM 1779 O VAL A 218 -17.839 -16.249 9.963 1.00 8.98 O ANISOU 1779 O VAL A 218 1403 844 1163 -80 -271 -131 O ATOM 1780 CB VAL A 218 -17.233 -13.004 9.616 1.00 9.55 C ANISOU 1780 CB VAL A 218 1263 839 1528 -168 -275 -113 C ATOM 1781 CG1 VAL A 218 -17.465 -11.657 10.292 1.00 10.18 C ANISOU 1781 CG1 VAL A 218 1578 827 1464 -145 -260 -126 C ATOM 1782 CG2 VAL A 218 -15.948 -13.634 10.116 1.00 10.90 C ANISOU 1782 CG2 VAL A 218 1272 1016 1853 -117 -388 -164 C ATOM 1783 N SER A 219 -18.342 -15.459 7.942 1.00 8.53 N ANISOU 1783 N SER A 219 1278 836 1128 -144 -194 -125 N ATOM 1784 CA SER A 219 -18.141 -16.781 7.365 1.00 8.86 C ANISOU 1784 CA SER A 219 1336 802 1228 -115 -153 -186 C ATOM 1785 C SER A 219 -16.653 -17.033 7.050 1.00 8.62 C ANISOU 1785 C SER A 219 1304 729 1240 -119 -150 -58 C ATOM 1786 O SER A 219 -15.848 -16.100 6.919 1.00 8.64 O ANISOU 1786 O SER A 219 1282 767 1234 -143 -210 -39 O ATOM 1787 CB SER A 219 -18.969 -16.942 6.101 1.00 9.39 C ANISOU 1787 CB SER A 219 1360 917 1289 -223 -149 -198 C ATOM 1788 OG SER A 219 -18.482 -16.057 5.113 1.00 9.36 O ANISOU 1788 OG SER A 219 1270 995 1290 -158 -182 -81 O ATOM 1789 N SER A 220 -16.328 -18.303 6.872 1.00 9.25 N ANISOU 1789 N SER A 220 1315 779 1419 -122 -139 -22 N ATOM 1790 CA SER A 220 -14.995 -18.677 6.442 1.00 9.74 C ANISOU 1790 CA SER A 220 1289 840 1571 -52 -207 55 C ATOM 1791 C SER A 220 -14.631 -17.983 5.126 1.00 9.68 C ANISOU 1791 C SER A 220 1251 907 1519 -30 -176 -53 C ATOM 1792 O SER A 220 -13.509 -17.531 4.942 1.00 10.80 O ANISOU 1792 O SER A 220 1288 1091 1725 -57 -122 109 O ATOM 1793 CB SER A 220 -14.871 -20.198 6.334 1.00 12.50 C ANISOU 1793 CB SER A 220 1768 1024 1959 -26 -129 -50 C ATOM 1794 OG SER A 220 -15.885 -20.768 5.510 1.00 15.67 O ANISOU 1794 OG SER A 220 2441 1314 2198 -256 -199 -210 O ATOM 1795 N GLU A 221 -15.594 -17.860 4.218 1.00 9.54 N ANISOU 1795 N GLU A 221 1336 923 1365 1 -104 -168 N ATOM 1796 CA GLU A 221 -15.304 -17.222 2.939 1.00 10.07 C ANISOU 1796 CA GLU A 221 1374 1083 1368 86 -136 -186 C ATOM 1797 C GLU A 221 -14.979 -15.739 3.106 1.00 9.67 C ANISOU 1797 C GLU A 221 1354 1060 1260 68 -58 -74 C ATOM 1798 O GLU A 221 -14.138 -15.183 2.394 1.00 10.78 O ANISOU 1798 O GLU A 221 1475 1253 1370 58 76 -85 O ATOM 1799 CB GLU A 221 -16.460 -17.387 1.950 1.00 12.49 C ANISOU 1799 CB GLU A 221 1787 1401 1557 123 -336 -394 C ATOM 1800 CG GLU A 221 -16.688 -18.817 1.475 1.00 14.93 C ANISOU 1800 CG GLU A 221 2120 1626 1926 57 -505 -623 C ATOM 1801 CD GLU A 221 -17.587 -19.627 2.390 1.00 17.66 C ANISOU 1801 CD GLU A 221 2991 1446 2275 -306 -404 -539 C ATOM 1802 OE1 GLU A 221 -18.105 -19.097 3.386 1.00 14.24 O ANISOU 1802 OE1 GLU A 221 1957 1428 2028 -191 -511 -190 O ATOM 1803 OE2 GLU A 221 -17.806 -20.820 2.097 1.00 24.86 O ANISOU 1803 OE2 GLU A 221 4267 1789 3388 -975 -252 -999 O ATOM 1804 N GLN A 222 -15.667 -15.078 4.032 1.00 8.76 N ANISOU 1804 N GLN A 222 1234 902 1194 12 -183 -89 N ATOM 1805 CA GLN A 222 -15.400 -13.666 4.283 1.00 8.57 C ANISOU 1805 CA GLN A 222 1208 921 1129 -43 -71 -8 C ATOM 1806 C GLN A 222 -13.976 -13.447 4.825 1.00 8.53 C ANISOU 1806 C GLN A 222 1152 973 1115 -26 -93 74 C ATOM 1807 O GLN A 222 -13.238 -12.594 4.324 1.00 9.21 O ANISOU 1807 O GLN A 222 1250 1092 1159 -66 -71 106 O ATOM 1808 CB GLN A 222 -16.465 -13.071 5.216 1.00 8.14 C ANISOU 1808 CB GLN A 222 1152 909 1032 -87 -164 -61 C ATOM 1809 CG GLN A 222 -17.804 -12.952 4.529 1.00 8.40 C ANISOU 1809 CG GLN A 222 1151 985 1056 -105 -136 -87 C ATOM 1810 CD GLN A 222 -18.919 -12.418 5.426 1.00 8.25 C ANISOU 1810 CD GLN A 222 1208 843 1082 -82 -189 -40 C ATOM 1811 OE1 GLN A 222 -19.036 -12.782 6.604 1.00 8.76 O ANISOU 1811 OE1 GLN A 222 1286 953 1089 -53 -124 -73 O ATOM 1812 NE2 GLN A 222 -19.765 -11.564 4.854 1.00 9.18 N ANISOU 1812 NE2 GLN A 222 1172 1062 1255 -55 -166 15 N ATOM 1813 N VAL A 223 -13.573 -14.235 5.824 1.00 9.09 N ANISOU 1813 N VAL A 223 1216 1022 1214 -70 -140 134 N ATOM 1814 CA VAL A 223 -12.227 -14.045 6.373 1.00 10.05 C ANISOU 1814 CA VAL A 223 1181 1324 1312 -135 -222 161 C ATOM 1815 C VAL A 223 -11.153 -14.492 5.356 1.00 9.54 C ANISOU 1815 C VAL A 223 1182 1092 1351 -76 -139 146 C ATOM 1816 O VAL A 223 -10.077 -13.905 5.300 1.00 9.80 O ANISOU 1816 O VAL A 223 1176 1198 1349 -132 -100 154 O ATOM 1817 CB VAL A 223 -12.060 -14.675 7.775 1.00 13.21 C ANISOU 1817 CB VAL A 223 1489 1806 1725 -338 -513 487 C ATOM 1818 CG1 VAL A 223 -12.044 -16.188 7.705 1.00 15.21 C ANISOU 1818 CG1 VAL A 223 1752 1848 2181 -456 -584 684 C ATOM 1819 CG2 VAL A 223 -10.807 -14.135 8.459 1.00 17.43 C ANISOU 1819 CG2 VAL A 223 2435 2192 1996 -563 -1065 500 C ATOM 1820 N LEU A 224 -11.450 -15.499 4.534 1.00 10.23 N ANISOU 1820 N LEU A 224 1285 1098 1503 -66 -124 82 N ATOM 1821 CA LEU A 224 -10.503 -15.903 3.505 1.00 11.50 C ANISOU 1821 CA LEU A 224 1465 1221 1682 -32 53 -77 C ATOM 1822 C LEU A 224 -10.192 -14.742 2.561 1.00 10.71 C ANISOU 1822 C LEU A 224 1301 1208 1561 -18 102 -91 C ATOM 1823 O LEU A 224 -9.066 -14.599 2.097 1.00 11.59 O ANISOU 1823 O LEU A 224 1321 1459 1624 -76 182 -149 O ATOM 1824 CB LEU A 224 -11.003 -17.144 2.756 1.00 14.19 C ANISOU 1824 CB LEU A 224 1923 1306 2163 -183 64 -242 C ATOM 1825 CG LEU A 224 -10.834 -18.453 3.543 1.00 18.00 C ANISOU 1825 CG LEU A 224 2636 1398 2806 254 23 -197 C ATOM 1826 CD1 LEU A 224 -11.694 -19.565 2.966 1.00 21.35 C ANISOU 1826 CD1 LEU A 224 3421 1538 3152 -118 25 24 C ATOM 1827 CD2 LEU A 224 -9.368 -18.871 3.611 1.00 20.49 C ANISOU 1827 CD2 LEU A 224 2734 2005 3045 736 435 -313 C ATOM 1828 N LYS A 225 -11.185 -13.899 2.287 1.00 9.97 N ANISOU 1828 N LYS A 225 1195 1283 1312 -127 -67 -38 N ATOM 1829 CA LYS A 225 -10.955 -12.748 1.431 1.00 10.22 C ANISOU 1829 CA LYS A 225 1190 1493 1201 -144 -139 82 C ATOM 1830 C LYS A 225 -10.076 -11.684 2.098 1.00 8.80 C ANISOU 1830 C LYS A 225 1120 1175 1047 45 -46 92 C ATOM 1831 O LYS A 225 -9.262 -11.063 1.429 1.00 9.57 O ANISOU 1831 O LYS A 225 1215 1349 1074 -89 -22 69 O ATOM 1832 CB LYS A 225 -12.282 -12.220 0.897 1.00 12.29 C ANISOU 1832 CB LYS A 225 1272 1945 1452 -214 -383 363 C ATOM 1833 CG LYS A 225 -12.838 -13.226 -0.141 1.00 16.31 C ANISOU 1833 CG LYS A 225 1830 2557 1810 -578 -559 283 C ATOM 1834 CD LYS A 225 -14.174 -12.877 -0.781 1.00 20.05 C ANISOU 1834 CD LYS A 225 1908 3362 2349 -544 -734 -81 C ATOM 1835 CE LYS A 225 -14.571 -13.923 -1.835 1.00 24.56 C ANISOU 1835 CE LYS A 225 2402 4112 2818 -202 -1030 -615 C ATOM 1836 NZ LYS A 225 -15.715 -13.487 -2.662 1.00 24.39 N ANISOU 1836 NZ LYS A 225 2589 3433 3247 -100 -1175 -793 N ATOM 1837 N PHE A 226 -10.202 -11.502 3.414 1.00 8.24 N ANISOU 1837 N PHE A 226 1072 1036 1025 19 9 68 N ATOM 1838 CA PHE A 226 -9.261 -10.624 4.115 1.00 8.08 C ANISOU 1838 CA PHE A 226 1037 1075 959 53 2 31 C ATOM 1839 C PHE A 226 -7.816 -11.118 3.870 1.00 7.60 C ANISOU 1839 C PHE A 226 1085 945 856 55 85 30 C ATOM 1840 O PHE A 226 -6.903 -10.319 3.689 1.00 8.19 O ANISOU 1840 O PHE A 226 1156 1009 947 29 38 -56 O ATOM 1841 CB PHE A 226 -9.489 -10.653 5.638 1.00 8.20 C ANISOU 1841 CB PHE A 226 1115 958 1044 88 83 -12 C ATOM 1842 CG PHE A 226 -10.673 -9.861 6.177 1.00 8.53 C ANISOU 1842 CG PHE A 226 1027 927 1286 -92 65 -253 C ATOM 1843 CD1 PHE A 226 -11.741 -9.416 5.415 1.00 12.23 C ANISOU 1843 CD1 PHE A 226 1522 1643 1482 589 320 192 C ATOM 1844 CD2 PHE A 226 -10.725 -9.646 7.564 1.00 12.44 C ANISOU 1844 CD2 PHE A 226 1273 1919 1533 -27 66 -727 C ATOM 1845 CE1 PHE A 226 -12.803 -8.717 6.018 1.00 12.80 C ANISOU 1845 CE1 PHE A 226 1490 1611 1761 461 334 32 C ATOM 1846 CE2 PHE A 226 -11.760 -8.949 8.147 1.00 14.37 C ANISOU 1846 CE2 PHE A 226 1201 2459 1801 16 -61 -1107 C ATOM 1847 CZ PHE A 226 -12.787 -8.470 7.371 1.00 12.58 C ANISOU 1847 CZ PHE A 226 1161 1743 1876 -51 54 -820 C ATOM 1848 N ARG A 227 -7.632 -12.438 3.904 1.00 7.80 N ANISOU 1848 N ARG A 227 1074 972 916 34 19 32 N ATOM 1849 CA ARG A 227 -6.306 -13.050 3.842 1.00 8.35 C ANISOU 1849 CA ARG A 227 1161 987 1023 85 21 46 C ATOM 1850 C ARG A 227 -5.689 -13.029 2.443 1.00 8.48 C ANISOU 1850 C ARG A 227 1177 960 1086 38 8 -29 C ATOM 1851 O ARG A 227 -4.553 -13.456 2.272 1.00 9.92 O ANISOU 1851 O ARG A 227 1299 1307 1164 187 90 15 O ATOM 1852 CB ARG A 227 -6.361 -14.479 4.381 1.00 8.71 C ANISOU 1852 CB ARG A 227 1266 987 1055 81 4 38 C ATOM 1853 CG ARG A 227 -6.792 -14.597 5.828 1.00 8.80 C ANISOU 1853 CG ARG A 227 1314 965 1064 4 -73 53 C ATOM 1854 CD ARG A 227 -6.798 -16.050 6.268 1.00 10.67 C ANISOU 1854 CD ARG A 227 1820 1060 1175 40 -36 131 C ATOM 1855 NE ARG A 227 -7.306 -16.187 7.625 1.00 9.72 N ANISOU 1855 NE ARG A 227 1599 927 1167 -110 -235 62 N ATOM 1856 CZ ARG A 227 -8.142 -17.134 8.031 1.00 11.43 C ANISOU 1856 CZ ARG A 227 1785 1226 1333 -415 -260 -26 C ATOM 1857 NH1 ARG A 227 -8.554 -18.076 7.188 1.00 14.64 N ANISOU 1857 NH1 ARG A 227 2227 1523 1812 -637 -228 -399 N ATOM 1858 NH2 ARG A 227 -8.574 -17.127 9.280 1.00 12.66 N ANISOU 1858 NH2 ARG A 227 1989 1398 1422 -474 30 36 N ATOM 1859 N LYS A 228 -6.438 -12.558 1.444 1.00 8.12 N ANISOU 1859 N LYS A 228 1181 975 931 -42 48 -115 N ATOM 1860 CA LYS A 228 -5.908 -12.378 0.087 1.00 8.90 C ANISOU 1860 CA LYS A 228 1257 1144 981 -44 26 -217 C ATOM 1861 C LYS A 228 -5.288 -11.004 -0.133 1.00 8.56 C ANISOU 1861 C LYS A 228 1382 1052 817 38 32 -128 C ATOM 1862 O LYS A 228 -4.643 -10.785 -1.154 1.00 9.89 O ANISOU 1862 O LYS A 228 1651 1226 882 -15 194 -157 O ATOM 1863 CB LYS A 228 -7.001 -12.612 -0.954 1.00 11.53 C ANISOU 1863 CB LYS A 228 1648 1527 1208 -266 -72 -233 C ATOM 1864 CG LYS A 228 -7.458 -14.050 -1.047 1.00 15.73 C ANISOU 1864 CG LYS A 228 2123 2017 1836 -804 -139 -534 C ATOM 1865 CD LYS A 228 -8.671 -14.215 -1.966 1.00 22.99 C ANISOU 1865 CD LYS A 228 2687 3364 2686 -1032 -799 -635 C ATOM 1866 CE LYS A 228 -8.455 -13.613 -3.344 1.00 37.99 C ANISOU 1866 CE LYS A 228 5593 4902 3939 191 -1976 361 C ATOM 1867 NZ LYS A 228 -9.617 -13.885 -4.243 1.00 55.02 N ANISOU 1867 NZ LYS A 228 9083 6395 5427 237 -3792 -643 N ATOM 1868 N LEU A 229 -5.509 -10.073 0.797 1.00 7.75 N ANISOU 1868 N LEU A 229 1179 934 833 10 -13 -114 N ATOM 1869 CA LEU A 229 -4.867 -8.774 0.713 1.00 7.66 C ANISOU 1869 CA LEU A 229 1151 899 862 43 35 -17 C ATOM 1870 C LEU A 229 -3.345 -8.935 0.813 1.00 7.53 C ANISOU 1870 C LEU A 229 1211 851 800 72 41 -45 C ATOM 1871 O LEU A 229 -2.832 -9.980 1.244 1.00 8.08 O ANISOU 1871 O LEU A 229 1272 900 899 81 64 -8 O ATOM 1872 CB LEU A 229 -5.383 -7.873 1.841 1.00 7.86 C ANISOU 1872 CB LEU A 229 1131 951 904 81 22 -88 C ATOM 1873 CG LEU A 229 -6.813 -7.370 1.625 1.00 8.25 C ANISOU 1873 CG LEU A 229 1136 1082 917 59 -1 -21 C ATOM 1874 CD1 LEU A 229 -7.364 -6.832 2.937 1.00 8.93 C ANISOU 1874 CD1 LEU A 229 1167 1233 993 119 -27 -243 C ATOM 1875 CD2 LEU A 229 -6.845 -6.310 0.538 1.00 11.04 C ANISOU 1875 CD2 LEU A 229 1496 1457 1244 268 119 285 C ATOM 1876 N ASN A 230 -2.635 -7.877 0.427 1.00 7.70 N ANISOU 1876 N ASN A 230 1128 918 881 61 82 -16 N ATOM 1877 CA ASN A 230 -1.176 -7.864 0.454 1.00 7.84 C ANISOU 1877 CA ASN A 230 1122 934 923 58 123 15 C ATOM 1878 C ASN A 230 -0.655 -6.711 1.327 1.00 7.55 C ANISOU 1878 C ASN A 230 1036 917 916 112 171 29 C ATOM 1879 O ASN A 230 -1.166 -5.595 1.288 1.00 8.52 O ANISOU 1879 O ASN A 230 1217 970 1049 114 56 -20 O ATOM 1880 CB ASN A 230 -0.577 -7.620 -0.948 1.00 8.90 C ANISOU 1880 CB ASN A 230 1257 1169 957 107 176 -17 C ATOM 1881 CG ASN A 230 -0.664 -8.786 -1.930 1.00 10.20 C ANISOU 1881 CG ASN A 230 1602 1268 1008 160 204 -144 C ATOM 1882 OD1 ASN A 230 -0.169 -8.640 -3.043 1.00 12.60 O ANISOU 1882 OD1 ASN A 230 2251 1448 1087 245 406 -78 O ATOM 1883 ND2 ASN A 230 -1.250 -9.919 -1.552 1.00 10.57 N ANISOU 1883 ND2 ASN A 230 1634 1190 1191 130 216 -280 N ATOM 1884 N PHE A 231 0.409 -7.001 2.084 1.00 8.00 N ANISOU 1884 N PHE A 231 1109 1000 930 81 137 37 N ATOM 1885 CA PHE A 231 1.171 -5.959 2.778 1.00 8.22 C ANISOU 1885 CA PHE A 231 1050 1057 1015 -28 33 56 C ATOM 1886 C PHE A 231 1.982 -5.085 1.794 1.00 9.07 C ANISOU 1886 C PHE A 231 1252 1168 1027 -100 35 67 C ATOM 1887 O PHE A 231 2.202 -3.906 2.037 1.00 10.52 O ANISOU 1887 O PHE A 231 1574 1211 1213 -287 76 139 O ATOM 1888 CB PHE A 231 2.181 -6.580 3.751 1.00 8.62 C ANISOU 1888 CB PHE A 231 1101 1133 1043 -36 20 96 C ATOM 1889 CG PHE A 231 1.606 -7.178 5.028 1.00 8.24 C ANISOU 1889 CG PHE A 231 1112 1029 988 -42 -15 61 C ATOM 1890 CD1 PHE A 231 0.863 -6.406 5.923 1.00 8.81 C ANISOU 1890 CD1 PHE A 231 1295 1107 944 -34 23 22 C ATOM 1891 CD2 PHE A 231 1.934 -8.469 5.405 1.00 8.87 C ANISOU 1891 CD2 PHE A 231 1188 1096 1084 20 3 9 C ATOM 1892 CE1 PHE A 231 0.430 -6.923 7.142 1.00 9.15 C ANISOU 1892 CE1 PHE A 231 1348 1111 1020 -60 0 -10 C ATOM 1893 CE2 PHE A 231 1.503 -8.992 6.621 1.00 9.21 C ANISOU 1893 CE2 PHE A 231 1279 1128 1090 -3 -56 85 C ATOM 1894 CZ PHE A 231 0.755 -8.221 7.492 1.00 8.75 C ANISOU 1894 CZ PHE A 231 1163 1185 977 -94 -71 42 C ATOM 1895 N ASN A 232 2.499 -5.719 0.741 1.00 9.69 N ANISOU 1895 N ASN A 232 1164 1397 1122 -17 136 137 N ATOM 1896 CA ASN A 232 3.370 -5.076 -0.240 1.00 10.14 C ANISOU 1896 CA ASN A 232 1173 1462 1219 41 179 260 C ATOM 1897 C ASN A 232 2.602 -4.173 -1.194 1.00 9.77 C ANISOU 1897 C ASN A 232 1157 1397 1159 130 156 205 C ATOM 1898 O ASN A 232 1.390 -4.284 -1.362 1.00 9.60 O ANISOU 1898 O ASN A 232 1177 1323 1147 169 128 82 O ATOM 1899 CB ASN A 232 4.083 -6.160 -1.041 1.00 11.26 C ANISOU 1899 CB ASN A 232 1181 1700 1397 264 289 336 C ATOM 1900 CG ASN A 232 3.101 -7.106 -1.670 1.00 11.47 C ANISOU 1900 CG ASN A 232 1350 1650 1356 437 342 65 C ATOM 1901 OD1 ASN A 232 2.569 -7.985 -0.989 1.00 11.52 O ANISOU 1901 OD1 ASN A 232 1380 1589 1407 401 341 51 O ATOM 1902 ND2 ASN A 232 2.785 -6.895 -2.942 1.00 13.97 N ANISOU 1902 ND2 ASN A 232 2032 1906 1371 717 337 -64 N ATOM 1903 N GLY A 233 3.363 -3.312 -1.872 1.00 11.33 N ANISOU 1903 N GLY A 233 1302 1747 1254 21 211 438 N ATOM 1904 CA GLY A 233 2.842 -2.535 -2.979 1.00 11.29 C ANISOU 1904 CA GLY A 233 1442 1620 1226 176 281 466 C ATOM 1905 C GLY A 233 2.835 -3.321 -4.280 1.00 11.52 C ANISOU 1905 C GLY A 233 1474 1665 1240 402 323 357 C ATOM 1906 O GLY A 233 3.466 -4.362 -4.407 1.00 14.90 O ANISOU 1906 O GLY A 233 2255 2007 1399 927 662 521 O ATOM 1907 N GLU A 234 2.083 -2.813 -5.250 1.00 10.98 N ANISOU 1907 N GLU A 234 1509 1490 1172 179 311 258 N ATOM 1908 CA GLU A 234 2.028 -3.412 -6.572 1.00 11.99 C ANISOU 1908 CA GLU A 234 1786 1540 1228 310 382 196 C ATOM 1909 C GLU A 234 3.431 -3.473 -7.194 1.00 13.70 C ANISOU 1909 C GLU A 234 2101 1816 1289 570 556 339 C ATOM 1910 O GLU A 234 4.192 -2.518 -7.122 1.00 15.10 O ANISOU 1910 O GLU A 234 1765 2498 1474 275 486 368 O ATOM 1911 CB GLU A 234 1.077 -2.606 -7.464 1.00 13.07 C ANISOU 1911 CB GLU A 234 1776 1874 1317 -11 95 155 C ATOM 1912 CG GLU A 234 0.835 -3.199 -8.833 1.00 17.06 C ANISOU 1912 CG GLU A 234 2345 2638 1500 -752 163 62 C ATOM 1913 CD GLU A 234 -0.023 -2.308 -9.706 1.00 22.71 C ANISOU 1913 CD GLU A 234 2995 4094 1539 -4 -137 269 C ATOM 1914 OE1 GLU A 234 -0.396 -1.189 -9.272 1.00 25.27 O ANISOU 1914 OE1 GLU A 234 3953 3831 1817 243 46 564 O ATOM 1915 OE2 GLU A 234 -0.318 -2.733 -10.831 1.00 24.59 O ANISOU 1915 OE2 GLU A 234 3760 4049 1533 -551 -409 351 O ATOM 1916 N GLY A 235 3.757 -4.608 -7.789 1.00 17.64 N ANISOU 1916 N GLY A 235 2897 2252 1552 1186 826 249 N ATOM 1917 CA GLY A 235 5.041 -4.763 -8.450 1.00 20.94 C ANISOU 1917 CA GLY A 235 3072 2937 1946 1530 1035 508 C ATOM 1918 C GLY A 235 6.144 -5.204 -7.509 1.00 21.68 C ANISOU 1918 C GLY A 235 2891 3455 1890 1643 1146 629 C ATOM 1919 O GLY A 235 7.307 -5.319 -7.915 1.00 28.91 O ANISOU 1919 O GLY A 235 3019 6110 1856 1923 1216 989 O ATOM 1920 N GLU A 236 5.771 -5.466 -6.256 1.00 21.80 N ANISOU 1920 N GLU A 236 2522 3642 2117 1746 1057 1032 N ATOM 1921 CA GLU A 236 6.697 -5.997 -5.271 1.00 21.61 C ANISOU 1921 CA GLU A 236 2076 3782 2354 1349 986 1405 C ATOM 1922 C GLU A 236 6.350 -7.448 -4.966 1.00 22.11 C ANISOU 1922 C GLU A 236 2297 3837 2268 1245 1085 1307 C ATOM 1923 O GLU A 236 5.242 -7.906 -5.262 1.00 22.39 O ANISOU 1923 O GLU A 236 2632 3498 2377 1309 930 621 O ATOM 1924 CB GLU A 236 6.617 -5.182 -3.978 1.00 21.98 C ANISOU 1924 CB GLU A 236 1902 3764 2685 775 769 1475 C ATOM 1925 CG GLU A 236 6.946 -3.719 -4.175 1.00 24.34 C ANISOU 1925 CG GLU A 236 2160 3809 3281 657 980 1495 C ATOM 1926 CD GLU A 236 6.746 -2.904 -2.918 1.00 28.41 C ANISOU 1926 CD GLU A 236 3033 4138 3624 -534 1113 1145 C ATOM 1927 OE1 GLU A 236 6.238 -3.460 -1.925 1.00 23.35 O ANISOU 1927 OE1 GLU A 236 1801 3883 3188 -63 573 1132 O ATOM 1928 OE2 GLU A 236 7.111 -1.708 -2.928 1.00 38.58 O ANISOU 1928 OE2 GLU A 236 5761 4716 4180 -1850 1498 1245 O ATOM 1929 N PRO A 237 7.295 -8.183 -4.353 1.00 24.03 N ANISOU 1929 N PRO A 237 2248 3956 2927 1455 1242 1729 N ATOM 1930 CA PRO A 237 7.024 -9.583 -4.013 1.00 21.94 C ANISOU 1930 CA PRO A 237 2184 3504 2648 1438 1134 1186 C ATOM 1931 C PRO A 237 5.805 -9.708 -3.093 1.00 18.42 C ANISOU 1931 C PRO A 237 2066 2931 2001 1063 867 732 C ATOM 1932 O PRO A 237 5.648 -8.920 -2.154 1.00 18.12 O ANISOU 1932 O PRO A 237 1897 2895 2094 708 814 550 O ATOM 1933 CB PRO A 237 8.312 -10.032 -3.305 1.00 22.96 C ANISOU 1933 CB PRO A 237 2204 3274 3246 1198 973 1430 C ATOM 1934 CG PRO A 237 9.372 -9.135 -3.886 1.00 26.75 C ANISOU 1934 CG PRO A 237 2409 3819 3936 1235 970 2271 C ATOM 1935 CD PRO A 237 8.686 -7.809 -4.028 1.00 27.09 C ANISOU 1935 CD PRO A 237 2450 3980 3863 1372 946 2475 C ATOM 1936 N GLU A 238 4.950 -10.681 -3.389 1.00 18.27 N ANISOU 1936 N GLU A 238 2075 2965 1901 1193 697 210 N ATOM 1937 CA GLU A 238 3.697 -10.821 -2.653 1.00 16.53 C ANISOU 1937 CA GLU A 238 1849 2636 1794 1051 367 -303 C ATOM 1938 C GLU A 238 3.896 -11.325 -1.235 1.00 13.01 C ANISOU 1938 C GLU A 238 1524 1780 1637 577 391 -178 C ATOM 1939 O GLU A 238 4.481 -12.383 -1.018 1.00 13.68 O ANISOU 1939 O GLU A 238 1560 1865 1772 617 348 -162 O ATOM 1940 CB GLU A 238 2.701 -11.737 -3.387 1.00 19.83 C ANISOU 1940 CB GLU A 238 2031 3312 2190 1209 -23 -973 C ATOM 1941 CG GLU A 238 1.341 -11.798 -2.669 1.00 20.50 C ANISOU 1941 CG GLU A 238 2376 2950 2463 621 107 -1220 C ATOM 1942 CD GLU A 238 0.272 -12.624 -3.369 1.00 23.99 C ANISOU 1942 CD GLU A 238 2588 3316 3213 401 109 -1857 C ATOM 1943 OE1 GLU A 238 0.605 -13.710 -3.890 1.00 32.56 O ANISOU 1943 OE1 GLU A 238 2996 4197 5179 962 -656 -3193 O ATOM 1944 OE2 GLU A 238 -0.911 -12.198 -3.366 1.00 17.97 O ANISOU 1944 OE2 GLU A 238 2525 2187 2118 67 202 -983 O ATOM 1945 N GLU A 239 3.393 -10.554 -0.277 1.00 11.89 N ANISOU 1945 N GLU A 239 1441 1588 1487 325 437 24 N ATOM 1946 CA GLU A 239 3.378 -10.938 1.122 1.00 11.52 C ANISOU 1946 CA GLU A 239 1248 1540 1591 70 303 62 C ATOM 1947 C GLU A 239 1.939 -10.796 1.596 1.00 9.41 C ANISOU 1947 C GLU A 239 1160 1096 1321 176 300 23 C ATOM 1948 O GLU A 239 1.431 -9.688 1.679 1.00 10.58 O ANISOU 1948 O GLU A 239 1437 998 1585 146 393 18 O ATOM 1949 CB GLU A 239 4.228 -9.995 1.975 1.00 17.70 C ANISOU 1949 CB GLU A 239 1836 2474 2414 -637 76 -74 C ATOM 1950 CG GLU A 239 5.650 -9.761 1.545 1.00 25.86 C ANISOU 1950 CG GLU A 239 1938 3498 4390 -582 -31 -1266 C ATOM 1951 CD GLU A 239 6.301 -8.627 2.330 1.00 38.56 C ANISOU 1951 CD GLU A 239 3887 4207 6559 -1963 -1160 -1402 C ATOM 1952 OE1 GLU A 239 6.981 -8.906 3.341 1.00 52.32 O ANISOU 1952 OE1 GLU A 239 8027 5193 6660 -2644 -2456 -1421 O ATOM 1953 OE2 GLU A 239 6.130 -7.447 1.947 1.00 43.68 O ANISOU 1953 OE2 GLU A 239 4881 4052 7665 -2520 -661 -1267 O ATOM 1954 N LEU A 240 1.294 -11.911 1.895 1.00 8.48 N ANISOU 1954 N LEU A 240 1200 961 1060 209 237 -20 N ATOM 1955 CA LEU A 240 -0.116 -11.849 2.279 1.00 8.36 C ANISOU 1955 CA LEU A 240 1157 1013 1008 219 216 -14 C ATOM 1956 C LEU A 240 -0.282 -11.054 3.572 1.00 7.78 C ANISOU 1956 C LEU A 240 1099 982 875 114 93 76 C ATOM 1957 O LEU A 240 0.459 -11.233 4.546 1.00 8.41 O ANISOU 1957 O LEU A 240 1133 1062 1000 147 68 28 O ATOM 1958 CB LEU A 240 -0.686 -13.246 2.471 1.00 9.03 C ANISOU 1958 CB LEU A 240 1186 1025 1219 168 177 -84 C ATOM 1959 CG LEU A 240 -0.724 -14.141 1.240 1.00 10.70 C ANISOU 1959 CG LEU A 240 1234 1263 1567 160 -51 -342 C ATOM 1960 CD1 LEU A 240 -1.288 -15.483 1.630 1.00 12.87 C ANISOU 1960 CD1 LEU A 240 1744 1184 1961 156 -161 -282 C ATOM 1961 CD2 LEU A 240 -1.538 -13.510 0.141 1.00 13.11 C ANISOU 1961 CD2 LEU A 240 1934 1538 1509 260 -26 -373 C ATOM 1962 N MET A 241 -1.310 -10.208 3.588 1.00 7.70 N ANISOU 1962 N MET A 241 1118 993 814 173 109 16 N ATOM 1963 CA MET A 241 -1.679 -9.437 4.779 1.00 7.63 C ANISOU 1963 CA MET A 241 1173 939 785 136 167 -21 C ATOM 1964 C MET A 241 -2.493 -10.353 5.712 1.00 7.23 C ANISOU 1964 C MET A 241 1108 888 750 44 47 -50 C ATOM 1965 O MET A 241 -3.710 -10.498 5.582 1.00 7.99 O ANISOU 1965 O MET A 241 1131 1064 842 84 -4 -13 O ATOM 1966 CB MET A 241 -2.510 -8.223 4.365 1.00 7.91 C ANISOU 1966 CB MET A 241 1228 910 869 147 185 4 C ATOM 1967 CG MET A 241 -2.860 -7.303 5.555 1.00 8.07 C ANISOU 1967 CG MET A 241 1247 883 935 93 204 -58 C ATOM 1968 SD MET A 241 -3.830 -5.849 5.086 1.00 8.50 S ANISOU 1968 SD MET A 241 1353 775 1102 92 209 -5 S ATOM 1969 CE MET A 241 -2.550 -4.821 4.365 1.00 9.64 C ANISOU 1969 CE MET A 241 1271 1075 1318 -30 274 145 C ATOM 1970 N VAL A 242 -1.745 -10.995 6.611 1.00 7.03 N ANISOU 1970 N VAL A 242 1079 865 728 61 54 -14 N ATOM 1971 CA VAL A 242 -2.282 -11.883 7.639 1.00 6.93 C ANISOU 1971 CA VAL A 242 1055 788 789 23 40 -22 C ATOM 1972 C VAL A 242 -1.469 -11.663 8.910 1.00 6.63 C ANISOU 1972 C VAL A 242 1020 743 757 75 34 -64 C ATOM 1973 O VAL A 242 -0.321 -11.238 8.867 1.00 7.57 O ANISOU 1973 O VAL A 242 1065 955 857 65 14 -62 O ATOM 1974 CB VAL A 242 -2.227 -13.385 7.233 1.00 7.93 C ANISOU 1974 CB VAL A 242 1207 876 930 34 4 -160 C ATOM 1975 CG1 VAL A 242 -3.136 -13.649 6.043 1.00 8.97 C ANISOU 1975 CG1 VAL A 242 1403 993 1013 -99 -68 -202 C ATOM 1976 CG2 VAL A 242 -0.784 -13.846 6.970 1.00 8.74 C ANISOU 1976 CG2 VAL A 242 1270 946 1104 123 142 -132 C ATOM 1977 N ASP A 243 -2.089 -11.990 10.055 1.00 6.59 N ANISOU 1977 N ASP A 243 1059 727 718 66 -29 -45 N ATOM 1978 CA ASP A 243 -1.413 -11.875 11.337 1.00 6.43 C ANISOU 1978 CA ASP A 243 979 702 762 131 12 -49 C ATOM 1979 C ASP A 243 -0.923 -10.447 11.607 1.00 6.09 C ANISOU 1979 C ASP A 243 892 725 697 87 23 -43 C ATOM 1980 O ASP A 243 0.161 -10.208 12.125 1.00 7.52 O ANISOU 1980 O ASP A 243 995 837 1024 68 -129 -68 O ATOM 1981 CB ASP A 243 -0.336 -12.933 11.530 1.00 7.06 C ANISOU 1981 CB ASP A 243 999 758 926 120 -61 -19 C ATOM 1982 CG ASP A 243 -0.914 -14.330 11.603 1.00 7.58 C ANISOU 1982 CG ASP A 243 1175 747 959 156 -18 -65 C ATOM 1983 OD1 ASP A 243 -1.946 -14.518 12.296 1.00 7.72 O ANISOU 1983 OD1 ASP A 243 1170 789 973 76 49 -10 O ATOM 1984 OD2 ASP A 243 -0.335 -15.244 10.975 1.00 8.93 O ANISOU 1984 OD2 ASP A 243 1352 820 1222 122 196 -121 O ATOM 1985 N ASN A 244 -1.814 -9.493 11.308 1.00 6.08 N ANISOU 1985 N ASN A 244 929 657 724 50 28 -85 N ATOM 1986 CA ASN A 244 -1.557 -8.080 11.549 1.00 5.98 C ANISOU 1986 CA ASN A 244 827 682 763 17 -4 -10 C ATOM 1987 C ASN A 244 -2.107 -7.615 12.913 1.00 5.87 C ANISOU 1987 C ASN A 244 820 728 681 -14 -66 -26 C ATOM 1988 O ASN A 244 -2.757 -6.579 13.014 1.00 7.41 O ANISOU 1988 O ASN A 244 1185 816 814 246 56 26 O ATOM 1989 CB ASN A 244 -2.093 -7.208 10.405 1.00 6.36 C ANISOU 1989 CB ASN A 244 839 793 784 -38 -19 74 C ATOM 1990 CG ASN A 244 -3.588 -7.357 10.205 1.00 7.46 C ANISOU 1990 CG ASN A 244 887 884 1062 -89 -126 202 C ATOM 1991 OD1 ASN A 244 -4.227 -8.249 10.749 1.00 7.34 O ANISOU 1991 OD1 ASN A 244 891 837 1062 -7 -36 217 O ATOM 1992 ND2 ASN A 244 -4.157 -6.428 9.471 1.00 11.68 N ANISOU 1992 ND2 ASN A 244 1243 1488 1708 -289 -430 853 N ATOM 1993 N TRP A 245 -1.804 -8.412 13.940 1.00 6.08 N ANISOU 1993 N TRP A 245 897 774 640 31 -34 -10 N ATOM 1994 CA TRP A 245 -2.245 -8.170 15.313 1.00 5.76 C ANISOU 1994 CA TRP A 245 815 740 632 87 -48 -80 C ATOM 1995 C TRP A 245 -1.043 -8.066 16.240 1.00 5.96 C ANISOU 1995 C TRP A 245 824 767 672 54 -31 -24 C ATOM 1996 O TRP A 245 -0.055 -8.806 16.110 1.00 7.28 O ANISOU 1996 O TRP A 245 969 954 842 134 -114 -66 O ATOM 1997 CB TRP A 245 -3.204 -9.281 15.806 1.00 6.41 C ANISOU 1997 CB TRP A 245 877 800 761 54 -41 -55 C ATOM 1998 CG TRP A 245 -2.727 -10.688 15.618 1.00 6.17 C ANISOU 1998 CG TRP A 245 795 801 750 6 49 8 C ATOM 1999 CD1 TRP A 245 -2.821 -11.428 14.478 1.00 6.45 C ANISOU 1999 CD1 TRP A 245 860 799 792 23 44 -52 C ATOM 2000 CD2 TRP A 245 -2.096 -11.541 16.585 1.00 6.67 C ANISOU 2000 CD2 TRP A 245 884 854 797 20 -5 43 C ATOM 2001 NE1 TRP A 245 -2.301 -12.695 14.663 1.00 7.02 N ANISOU 2001 NE1 TRP A 245 984 812 873 12 54 -23 N ATOM 2002 CE2 TRP A 245 -1.840 -12.778 15.951 1.00 6.87 C ANISOU 2002 CE2 TRP A 245 925 830 855 63 28 43 C ATOM 2003 CE3 TRP A 245 -1.778 -11.397 17.939 1.00 7.44 C ANISOU 2003 CE3 TRP A 245 1033 961 833 46 -11 42 C ATOM 2004 CZ2 TRP A 245 -1.255 -13.850 16.623 1.00 8.50 C ANISOU 2004 CZ2 TRP A 245 1263 934 1034 159 36 123 C ATOM 2005 CZ3 TRP A 245 -1.193 -12.466 18.601 1.00 9.22 C ANISOU 2005 CZ3 TRP A 245 1467 1143 893 237 -7 173 C ATOM 2006 CH2 TRP A 245 -0.931 -13.671 17.941 1.00 9.20 C ANISOU 2006 CH2 TRP A 245 1359 1090 1048 224 -42 213 C ATOM 2007 N ARG A 246 -1.161 -7.146 17.190 1.00 6.19 N ANISOU 2007 N ARG A 246 833 828 689 81 -35 -109 N ATOM 2008 CA ARG A 246 -0.242 -7.036 18.313 1.00 6.37 C ANISOU 2008 CA ARG A 246 794 879 747 28 -36 -73 C ATOM 2009 C ARG A 246 -0.748 -7.942 19.444 1.00 6.48 C ANISOU 2009 C ARG A 246 825 892 745 42 -87 -92 C ATOM 2010 O ARG A 246 -1.933 -7.946 19.742 1.00 7.19 O ANISOU 2010 O ARG A 246 939 1000 792 44 -55 -71 O ATOM 2011 CB ARG A 246 -0.185 -5.588 18.807 1.00 6.57 C ANISOU 2011 CB ARG A 246 797 921 780 12 0 -42 C ATOM 2012 CG ARG A 246 0.923 -5.338 19.824 1.00 6.72 C ANISOU 2012 CG ARG A 246 762 996 793 -21 -67 -91 C ATOM 2013 CD ARG A 246 0.846 -3.955 20.435 1.00 6.78 C ANISOU 2013 CD ARG A 246 699 1093 785 -70 -23 -168 C ATOM 2014 NE ARG A 246 2.080 -3.658 21.162 1.00 7.41 N ANISOU 2014 NE ARG A 246 810 1120 887 -69 -46 -198 N ATOM 2015 CZ ARG A 246 2.277 -2.646 21.989 1.00 7.43 C ANISOU 2015 CZ ARG A 246 756 1186 880 -173 -18 -132 C ATOM 2016 NH1 ARG A 246 1.275 -1.857 22.371 1.00 7.71 N ANISOU 2016 NH1 ARG A 246 898 1085 945 -215 94 -203 N ATOM 2017 NH2 ARG A 246 3.508 -2.432 22.474 1.00 8.56 N ANISOU 2017 NH2 ARG A 246 877 1306 1069 -189 -51 -185 N ATOM 2018 N PRO A 247 0.154 -8.698 20.096 1.00 7.12 N ANISOU 2018 N PRO A 247 863 1027 816 70 -25 -45 N ATOM 2019 CA PRO A 247 -0.298 -9.549 21.205 1.00 7.40 C ANISOU 2019 CA PRO A 247 987 951 875 144 -39 22 C ATOM 2020 C PRO A 247 -0.593 -8.720 22.462 1.00 6.94 C ANISOU 2020 C PRO A 247 883 940 813 90 -98 42 C ATOM 2021 O PRO A 247 -0.265 -7.537 22.579 1.00 7.41 O ANISOU 2021 O PRO A 247 972 1014 829 51 -65 -4 O ATOM 2022 CB PRO A 247 0.899 -10.479 21.436 1.00 8.78 C ANISOU 2022 CB PRO A 247 1149 1113 1075 250 19 130 C ATOM 2023 CG PRO A 247 2.063 -9.648 21.036 1.00 10.53 C ANISOU 2023 CG PRO A 247 1174 1480 1347 199 -94 187 C ATOM 2024 CD PRO A 247 1.597 -8.870 19.821 1.00 8.75 C ANISOU 2024 CD PRO A 247 907 1327 1093 234 -30 72 C ATOM 2025 N ALA A 248 -1.222 -9.386 23.432 1.00 7.56 N ANISOU 2025 N ALA A 248 1022 1017 833 115 -45 1 N ATOM 2026 CA ALA A 248 -1.578 -8.751 24.693 1.00 7.68 C ANISOU 2026 CA ALA A 248 1007 1075 837 110 23 28 C ATOM 2027 C ALA A 248 -0.332 -8.229 25.419 1.00 7.54 C ANISOU 2027 C ALA A 248 946 1090 828 157 -23 63 C ATOM 2028 O ALA A 248 0.710 -8.900 25.488 1.00 8.59 O ANISOU 2028 O ALA A 248 1073 1235 956 228 -105 26 O ATOM 2029 CB ALA A 248 -2.327 -9.734 25.586 1.00 9.02 C ANISOU 2029 CB ALA A 248 1176 1239 1011 -57 105 58 C ATOM 2030 N GLN A 249 -0.490 -7.054 26.011 1.00 7.47 N ANISOU 2030 N GLN A 249 880 1125 834 100 -87 84 N ATOM 2031 CA GLN A 249 0.545 -6.338 26.749 1.00 7.67 C ANISOU 2031 CA GLN A 249 899 1192 822 108 -128 2 C ATOM 2032 C GLN A 249 0.235 -6.345 28.242 1.00 8.04 C ANISOU 2032 C GLN A 249 988 1251 815 193 -106 57 C ATOM 2033 O GLN A 249 -0.899 -6.579 28.644 1.00 8.92 O ANISOU 2033 O GLN A 249 1123 1321 945 88 -1 54 O ATOM 2034 CB GLN A 249 0.607 -4.897 26.239 1.00 8.18 C ANISOU 2034 CB GLN A 249 1017 1194 896 -2 -67 14 C ATOM 2035 CG GLN A 249 0.904 -4.793 24.738 1.00 8.37 C ANISOU 2035 CG GLN A 249 1054 1180 947 -4 -45 -6 C ATOM 2036 CD GLN A 249 2.230 -5.452 24.377 1.00 8.99 C ANISOU 2036 CD GLN A 249 1000 1353 1063 -137 6 -82 C ATOM 2037 OE1 GLN A 249 3.271 -5.123 24.952 1.00 10.87 O ANISOU 2037 OE1 GLN A 249 1015 1883 1232 -219 37 -198 O ATOM 2038 NE2 GLN A 249 2.205 -6.385 23.444 1.00 9.47 N ANISOU 2038 NE2 GLN A 249 1010 1490 1100 -65 4 -51 N ATOM 2039 N PRO A 250 1.241 -6.070 29.086 1.00 9.56 N ANISOU 2039 N PRO A 250 1059 1663 912 311 -212 -58 N ATOM 2040 CA PRO A 250 1.004 -6.130 30.529 1.00 11.13 C ANISOU 2040 CA PRO A 250 1401 1899 929 671 -277 -109 C ATOM 2041 C PRO A 250 -0.053 -5.119 30.984 1.00 9.46 C ANISOU 2041 C PRO A 250 1228 1479 887 403 -194 47 C ATOM 2042 O PRO A 250 -0.035 -3.953 30.604 1.00 9.37 O ANISOU 2042 O PRO A 250 1071 1501 988 285 -141 107 O ATOM 2043 CB PRO A 250 2.376 -5.790 31.117 1.00 14.63 C ANISOU 2043 CB PRO A 250 1566 2661 1332 950 -536 -463 C ATOM 2044 CG PRO A 250 3.364 -6.202 30.052 1.00 15.48 C ANISOU 2044 CG PRO A 250 1376 3021 1485 619 -517 -464 C ATOM 2045 CD PRO A 250 2.664 -5.832 28.762 1.00 13.11 C ANISOU 2045 CD PRO A 250 1014 2641 1324 351 -464 -316 C ATOM 2046 N LEU A 251 -0.938 -5.580 31.866 1.00 9.60 N ANISOU 2046 N LEU A 251 1352 1426 867 247 -116 35 N ATOM 2047 CA LEU A 251 -1.994 -4.722 32.377 1.00 9.37 C ANISOU 2047 CA LEU A 251 1329 1294 937 198 -81 46 C ATOM 2048 C LEU A 251 -1.459 -3.608 33.278 1.00 8.87 C ANISOU 2048 C LEU A 251 1203 1346 821 261 -142 72 C ATOM 2049 O LEU A 251 -2.019 -2.502 33.321 1.00 9.21 O ANISOU 2049 O LEU A 251 1229 1323 949 220 -227 11 O ATOM 2050 CB LEU A 251 -3.037 -5.574 33.120 1.00 11.38 C ANISOU 2050 CB LEU A 251 1609 1472 1243 50 191 27 C ATOM 2051 CG LEU A 251 -4.323 -4.852 33.531 1.00 12.03 C ANISOU 2051 CG LEU A 251 1534 1544 1493 -185 205 -162 C ATOM 2052 CD1 LEU A 251 -5.076 -4.320 32.322 1.00 12.68 C ANISOU 2052 CD1 LEU A 251 1464 1823 1530 -81 -2 -270 C ATOM 2053 CD2 LEU A 251 -5.204 -5.805 34.339 1.00 14.73 C ANISOU 2053 CD2 LEU A 251 1899 1809 1888 -328 466 -135 C ATOM 2054 N LYS A 252 -0.395 -3.899 34.027 1.00 9.66 N ANISOU 2054 N LYS A 252 1248 1578 847 350 -211 -20 N ATOM 2055 CA LYS A 252 0.192 -2.909 34.911 1.00 10.68 C ANISOU 2055 CA LYS A 252 1319 1770 970 422 -239 -118 C ATOM 2056 C LYS A 252 -0.861 -2.330 35.858 1.00 11.17 C ANISOU 2056 C LYS A 252 1505 1761 979 396 -153 -50 C ATOM 2057 O LYS A 252 -1.677 -3.095 36.389 1.00 12.33 O ANISOU 2057 O LYS A 252 1785 1887 1013 271 60 -7 O ATOM 2058 CB LYS A 252 1.004 -1.875 34.142 1.00 12.23 C ANISOU 2058 CB LYS A 252 1315 1968 1366 181 -138 -257 C ATOM 2059 CG LYS A 252 2.125 -2.535 33.343 1.00 16.17 C ANISOU 2059 CG LYS A 252 1510 2748 1888 69 133 -400 C ATOM 2060 CD LYS A 252 3.109 -1.552 32.740 1.00 19.76 C ANISOU 2060 CD LYS A 252 1857 3225 2427 195 421 65 C ATOM 2061 CE LYS A 252 4.310 -2.288 32.169 1.00 23.51 C ANISOU 2061 CE LYS A 252 1864 3872 3197 189 657 42 C ATOM 2062 NZ LYS A 252 5.219 -1.389 31.408 1.00 25.29 N ANISOU 2062 NZ LYS A 252 2041 4040 3528 504 493 822 N ATOM 2063 N ASN A 253 -0.831 -1.025 36.110 1.00 11.09 N ANISOU 2063 N ASN A 253 1347 1798 1070 353 -289 -326 N ATOM 2064 CA ASN A 253 -1.683 -0.437 37.148 1.00 12.84 C ANISOU 2064 CA ASN A 253 1361 2203 1314 228 -347 -469 C ATOM 2065 C ASN A 253 -3.027 -0.024 36.556 1.00 12.09 C ANISOU 2065 C ASN A 253 1271 1999 1324 318 -233 -274 C ATOM 2066 O ASN A 253 -3.338 1.172 36.534 1.00 13.99 O ANISOU 2066 O ASN A 253 1723 2034 1557 495 -95 -289 O ATOM 2067 CB ASN A 253 -0.987 0.755 37.810 1.00 16.24 C ANISOU 2067 CB ASN A 253 1997 2535 1638 172 -482 -807 C ATOM 2068 CG ASN A 253 -1.764 1.296 38.993 1.00 20.54 C ANISOU 2068 CG ASN A 253 2936 2650 2219 192 -32 -1012 C ATOM 2069 OD1 ASN A 253 -1.861 2.509 39.193 1.00 23.16 O ANISOU 2069 OD1 ASN A 253 2747 2805 3246 404 -276 -1644 O ATOM 2070 ND2 ASN A 253 -2.340 0.395 39.781 1.00 24.65 N ANISOU 2070 ND2 ASN A 253 3327 3774 2265 -571 233 -1071 N ATOM 2071 N ARG A 254 -3.785 -1.014 36.040 1.00 10.82 N ANISOU 2071 N ARG A 254 1154 1983 975 243 -198 133 N ATOM 2072 CA ARG A 254 -5.097 -0.775 35.455 1.00 9.38 C ANISOU 2072 CA ARG A 254 1100 1529 936 114 -119 19 C ATOM 2073 C ARG A 254 -6.112 -1.779 35.949 1.00 9.99 C ANISOU 2073 C ARG A 254 1180 1395 1220 135 58 -45 C ATOM 2074 O ARG A 254 -5.781 -2.914 36.292 1.00 13.01 O ANISOU 2074 O ARG A 254 1457 1642 1843 179 399 256 O ATOM 2075 CB ARG A 254 -5.007 -0.793 33.932 1.00 8.78 C ANISOU 2075 CB ARG A 254 1119 1349 868 83 -131 -41 C ATOM 2076 CG ARG A 254 -4.178 0.355 33.392 1.00 8.57 C ANISOU 2076 CG ARG A 254 1169 1248 841 107 -100 -107 C ATOM 2077 CD ARG A 254 -4.070 0.316 31.883 1.00 8.61 C ANISOU 2077 CD ARG A 254 1247 1223 802 209 -73 -115 C ATOM 2078 NE ARG A 254 -3.203 -0.777 31.441 1.00 7.82 N ANISOU 2078 NE ARG A 254 1051 1200 723 166 -149 4 N ATOM 2079 CZ ARG A 254 -2.922 -1.046 30.162 1.00 7.03 C ANISOU 2079 CZ ARG A 254 819 1108 744 -6 -137 -23 C ATOM 2080 NH1 ARG A 254 -3.532 -0.356 29.194 1.00 6.59 N ANISOU 2080 NH1 ARG A 254 829 991 684 44 -159 65 N ATOM 2081 NH2 ARG A 254 -2.083 -2.021 29.842 1.00 7.51 N ANISOU 2081 NH2 ARG A 254 902 1140 814 81 -145 27 N ATOM 2082 N GLN A 255 -7.353 -1.309 35.994 1.00 11.14 N ANISOU 2082 N GLN A 255 1087 1863 1281 51 0 -375 N ATOM 2083 CA GLN A 255 -8.495 -2.162 36.259 1.00 13.50 C ANISOU 2083 CA GLN A 255 1131 2570 1427 -90 -96 -407 C ATOM 2084 C GLN A 255 -9.405 -2.122 35.038 1.00 11.95 C ANISOU 2084 C GLN A 255 1203 1813 1523 82 -311 -240 C ATOM 2085 O GLN A 255 -9.686 -1.058 34.462 1.00 15.93 O ANISOU 2085 O GLN A 255 1940 1688 2425 198 -883 -277 O ATOM 2086 CB GLN A 255 -9.255 -1.719 37.518 1.00 20.87 C ANISOU 2086 CB GLN A 255 1988 3584 2358 140 95 -661 C ATOM 2087 CG GLN A 255 -9.679 -0.255 37.544 1.00 38.11 C ANISOU 2087 CG GLN A 255 5904 4239 4339 1365 1259 -1088 C ATOM 2088 CD GLN A 255 -9.814 0.289 38.964 1.00 44.14 C ANISOU 2088 CD GLN A 255 8379 3325 5067 -1094 2176 -1052 C ATOM 2089 OE1 GLN A 255 -9.663 1.493 39.212 1.00 47.59 O ANISOU 2089 OE1 GLN A 255 10074 3270 4737 -1800 2010 -1701 O ATOM 2090 NE2 GLN A 255 -10.091 -0.603 39.905 1.00 55.28 N ANISOU 2090 NE2 GLN A 255 9148 5547 6307 -4334 2577 -873 N ATOM 2091 N ILE A 256 -9.863 -3.294 34.640 1.00 9.75 N ANISOU 2091 N ILE A 256 1016 1664 1025 40 -60 -18 N ATOM 2092 CA ILE A 256 -10.859 -3.385 33.587 1.00 8.87 C ANISOU 2092 CA ILE A 256 926 1573 871 104 -1 58 C ATOM 2093 C ILE A 256 -12.249 -3.401 34.263 1.00 8.70 C ANISOU 2093 C ILE A 256 955 1522 830 94 65 215 C ATOM 2094 O ILE A 256 -12.471 -4.149 35.221 1.00 9.95 O ANISOU 2094 O ILE A 256 1113 1702 963 194 32 374 O ATOM 2095 CB ILE A 256 -10.646 -4.632 32.744 1.00 9.55 C ANISOU 2095 CB ILE A 256 966 1634 1029 182 -65 -65 C ATOM 2096 CG1 ILE A 256 -9.215 -4.612 32.153 1.00 10.66 C ANISOU 2096 CG1 ILE A 256 1122 1573 1357 168 79 -120 C ATOM 2097 CG2 ILE A 256 -11.706 -4.723 31.650 1.00 10.59 C ANISOU 2097 CG2 ILE A 256 1148 1721 1156 62 -254 -32 C ATOM 2098 CD1 ILE A 256 -8.895 -5.786 31.286 1.00 12.56 C ANISOU 2098 CD1 ILE A 256 1524 1754 1492 96 280 -254 C ATOM 2099 N LYS A 257 -13.148 -2.556 33.766 1.00 8.20 N ANISOU 2099 N LYS A 257 929 1420 766 85 -22 129 N ATOM 2100 CA LYS A 257 -14.510 -2.451 34.302 1.00 8.29 C ANISOU 2100 CA LYS A 257 901 1463 785 76 42 82 C ATOM 2101 C LYS A 257 -15.487 -3.059 33.320 1.00 8.26 C ANISOU 2101 C LYS A 257 963 1433 742 4 -3 146 C ATOM 2102 O LYS A 257 -15.298 -2.988 32.119 1.00 9.51 O ANISOU 2102 O LYS A 257 1234 1732 648 -317 19 84 O ATOM 2103 CB LYS A 257 -14.855 -0.992 34.570 1.00 10.25 C ANISOU 2103 CB LYS A 257 1134 1547 1215 102 48 -125 C ATOM 2104 CG LYS A 257 -13.976 -0.369 35.632 1.00 15.32 C ANISOU 2104 CG LYS A 257 1752 2207 1863 -58 -265 -502 C ATOM 2105 CD LYS A 257 -14.069 -1.123 36.954 1.00 26.85 C ANISOU 2105 CD LYS A 257 3812 3856 2535 769 -1131 -155 C ATOM 2106 CE LYS A 257 -13.501 -0.308 38.107 1.00 38.57 C ANISOU 2106 CE LYS A 257 5758 5653 3244 1173 -1456 -1079 C ATOM 2107 NZ LYS A 257 -13.668 -0.995 39.418 1.00 44.35 N ANISOU 2107 NZ LYS A 257 6904 6059 3888 148 -1823 -951 N ATOM 2108 N ALA A 258 -16.521 -3.698 33.863 1.00 8.92 N ANISOU 2108 N ALA A 258 997 1609 785 -41 78 73 N ATOM 2109 CA ALA A 258 -17.598 -4.282 33.089 1.00 8.48 C ANISOU 2109 CA ALA A 258 940 1396 887 -46 72 27 C ATOM 2110 C ALA A 258 -18.874 -3.457 33.223 1.00 8.45 C ANISOU 2110 C ALA A 258 934 1471 805 -82 106 56 C ATOM 2111 O ALA A 258 -19.214 -2.988 34.310 1.00 9.47 O ANISOU 2111 O ALA A 258 1075 1655 867 17 147 -74 O ATOM 2112 CB ALA A 258 -17.857 -5.721 33.529 1.00 10.71 C ANISOU 2112 CB ALA A 258 1442 1372 1257 -63 122 76 C ATOM 2113 N SER A 259 -19.603 -3.348 32.118 1.00 8.23 N ANISOU 2113 N SER A 259 944 1353 830 -57 56 4 N ATOM 2114 CA SER A 259 -20.882 -2.620 32.111 1.00 8.88 C ANISOU 2114 CA SER A 259 1020 1281 1073 51 30 14 C ATOM 2115 C SER A 259 -22.051 -3.487 32.563 1.00 10.01 C ANISOU 2115 C SER A 259 945 1642 1217 -93 87 -4 C ATOM 2116 O SER A 259 -23.155 -2.982 32.693 1.00 12.87 O ANISOU 2116 O SER A 259 1130 2152 1610 17 256 -47 O ATOM 2117 CB SER A 259 -21.167 -2.113 30.702 1.00 9.65 C ANISOU 2117 CB SER A 259 1182 1340 1147 -12 -55 60 C ATOM 2118 OG SER A 259 -21.589 -3.169 29.856 1.00 9.00 O ANISOU 2118 OG SER A 259 970 1485 967 -70 -7 70 O ATOM 2119 N PHE A 260 -21.794 -4.771 32.790 1.00 10.77 N ANISOU 2119 N PHE A 260 1060 1708 1323 -245 176 153 N ATOM 2120 CA PHE A 260 -22.842 -5.777 32.980 1.00 13.63 C ANISOU 2120 CA PHE A 260 1511 1963 1705 -538 211 352 C ATOM 2121 C PHE A 260 -22.446 -6.683 34.129 1.00 19.45 C ANISOU 2121 C PHE A 260 2286 2990 2113 -1190 -66 1035 C ATOM 2122 O PHE A 260 -21.268 -6.783 34.486 1.00 20.91 O ANISOU 2122 O PHE A 260 2542 3209 2193 -1337 -548 1429 O ATOM 2123 CB PHE A 260 -22.966 -6.602 31.693 1.00 12.73 C ANISOU 2123 CB PHE A 260 1210 1857 1769 -357 -158 187 C ATOM 2124 CG PHE A 260 -21.696 -7.323 31.319 1.00 12.83 C ANISOU 2124 CG PHE A 260 1262 1522 2089 -286 -191 215 C ATOM 2125 CD1 PHE A 260 -20.712 -6.683 30.568 1.00 11.24 C ANISOU 2125 CD1 PHE A 260 1297 1385 1587 -153 -95 -3 C ATOM 2126 CD2 PHE A 260 -21.465 -8.608 31.759 1.00 17.01 C ANISOU 2126 CD2 PHE A 260 1393 1873 3197 -281 -358 870 C ATOM 2127 CE1 PHE A 260 -19.528 -7.337 30.266 1.00 12.93 C ANISOU 2127 CE1 PHE A 260 1278 1538 2094 -76 -250 58 C ATOM 2128 CE2 PHE A 260 -20.291 -9.267 31.444 1.00 19.70 C ANISOU 2128 CE2 PHE A 260 1827 1767 3893 -32 64 821 C ATOM 2129 CZ PHE A 260 -19.326 -8.630 30.696 1.00 18.15 C ANISOU 2129 CZ PHE A 260 1499 1867 3531 98 -156 673 C ATOM 2130 N LYS A 261 -23.442 -7.335 34.714 1.00 27.67 N ANISOU 2130 N LYS A 261 3081 4289 3145 -2026 -275 1998 N ATOM 2131 CA LYS A 261 -23.195 -8.342 35.733 1.00 37.55 C ANISOU 2131 CA LYS A 261 4634 5265 4368 -1784 319 2946 C ATOM 2132 C LYS A 261 -23.215 -9.725 35.101 1.00 41.90 C ANISOU 2132 C LYS A 261 6097 4839 4985 -1000 596 3148 C ATOM 2133 O LYS A 261 -22.337 -10.556 35.348 1.00 46.42 O ANISOU 2133 O LYS A 261 5177 6139 6321 27 637 3075 O ATOM 2134 CB LYS A 261 -24.236 -8.254 36.848 1.00 42.85 C ANISOU 2134 CB LYS A 261 5228 6055 4999 -2149 841 2446 C ATOM 2135 CG LYS A 261 -23.672 -7.751 38.166 1.00 44.56 C ANISOU 2135 CG LYS A 261 4457 6796 5680 -1359 551 531 C ATOM 2136 CD LYS A 261 -24.721 -7.780 39.262 1.00 45.73 C ANISOU 2136 CD LYS A 261 4912 6606 5858 -2216 1069 -74 C ATOM 2137 CE LYS A 261 -25.821 -6.763 39.002 1.00 47.70 C ANISOU 2137 CE LYS A 261 5025 6998 6101 -1835 1588 -709 C ATOM 2138 NZ LYS A 261 -26.992 -6.960 39.903 1.00 48.01 N ANISOU 2138 NZ LYS A 261 5581 6463 6198 -2400 1998 -312 N ATOM 2139 OXT LYS A 261 -24.110 -10.035 34.319 1.00 44.52 O ANISOU 2139 OXT LYS A 261 8041 4206 4667 -118 612 2514 O TER 2140 LYS A 261 HETATM 2141 ZN ZN A 262 -6.745 -1.548 15.342 1.00 5.63 ZN ANISOU 2141 ZN ZN A 262 808 678 652 9 -69 -11 ZN HETATM 2142 C1 GOL A 304 2.334 -10.601 15.533 1.00 17.82 C ANISOU 2142 C1 GOL A 304 2707 2235 1827 368 518 -318 C HETATM 2143 O1 GOL A 304 1.605 -10.862 16.700 1.00 13.85 O ANISOU 2143 O1 GOL A 304 1875 1982 1407 839 -76 48 O HETATM 2144 C2 GOL A 304 1.822 -11.596 14.514 1.00 16.84 C ANISOU 2144 C2 GOL A 304 2681 2189 1529 1108 -99 -25 C HETATM 2145 O2 GOL A 304 2.337 -11.407 13.210 1.00 12.21 O ANISOU 2145 O2 GOL A 304 1410 1622 1607 337 -154 -97 O HETATM 2146 C3 GOL A 304 2.157 -13.008 14.977 1.00 18.03 C ANISOU 2146 C3 GOL A 304 2915 1971 1965 772 -312 -57 C HETATM 2147 O3 GOL A 304 1.501 -13.933 14.145 1.00 24.32 O ANISOU 2147 O3 GOL A 304 4317 2410 2514 1022 -959 -486 O HETATM 2148 O HOH A 126 2.346 -14.228 -1.029 0.62 14.05 O ANISOU 2148 O HOH A 126 1789 1786 1762 612 122 -194 O HETATM 2149 O HOH A 263 -23.978 -3.381 3.903 0.82 25.01 O ANISOU 2149 O HOH A 263 2713 1792 4998 463 93 504 O HETATM 2150 O HOH A 264 -26.026 -3.139 6.723 0.99 32.15 O ANISOU 2150 O HOH A 264 3425 4501 4288 -159 -963 599 O HETATM 2151 O HOH A 265 6.225 -11.201 16.077 0.82 26.80 O ANISOU 2151 O HOH A 265 2651 3928 3604 -729 -835 1185 O HETATM 2152 O HOH A 266 7.178 -3.589 -10.670 0.77 22.19 O ANISOU 2152 O HOH A 266 3272 3397 1761 -981 682 -282 O HETATM 2153 O HOH A 267 -27.449 -5.283 27.689 0.65 24.51 O ANISOU 2153 O HOH A 267 1855 3953 3505 577 -672 -68 O HETATM 2154 O HOH A 268 -19.950 -16.457 21.489 0.68 29.41 O ANISOU 2154 O HOH A 268 3688 3481 4007 -1135 431 518 O HETATM 2155 O HOH A 269 -13.886 14.934 6.555 0.96 30.64 O ANISOU 2155 O HOH A 269 2911 4074 4657 -356 376 90 O HETATM 2156 O HOH A 270 -6.857 -2.016 -8.253 0.84 29.23 O ANISOU 2156 O HOH A 270 4736 4132 2238 78 909 417 O HETATM 2157 O HOH A 271 -5.045 5.447 13.919 1.00 32.99 O ANISOU 2157 O HOH A 271 3831 3993 4712 -695 -405 -721 O HETATM 2158 O HOH A 272 14.733 -10.220 14.500 0.78 28.41 O ANISOU 2158 O HOH A 272 3565 3065 4163 1510 -36 -891 O HETATM 2159 O HOH A 273 15.117 -6.886 12.529 0.57 24.69 O ANISOU 2159 O HOH A 273 1087 3831 4464 -100 -605 -1974 O HETATM 2160 O HOH A 274 -17.690 -8.717 35.242 0.94 27.29 O ANISOU 2160 O HOH A 274 3911 3007 3452 509 600 49 O HETATM 2161 O HOH A 275 -26.057 -6.307 33.888 0.76 30.19 O ANISOU 2161 O HOH A 275 2326 4366 4780 -1137 962 732 O HETATM 2162 O HOH A 276 -10.481 -20.161 7.536 0.46 24.64 O ANISOU 2162 O HOH A 276 4118 3370 1876 -2317 736 -1153 O HETATM 2163 O HOH A 277 12.496 -7.013 -4.732 0.82 26.66 O ANISOU 2163 O HOH A 277 3109 2805 4214 971 747 619 O HETATM 2164 O HOH A 278 0.193 7.561 29.809 0.59 24.51 O ANISOU 2164 O HOH A 278 2633 3111 3569 375 -1228 -1525 O HETATM 2165 O HOH A 279 -3.124 -17.651 31.625 0.73 29.40 O ANISOU 2165 O HOH A 279 3653 4234 3284 -872 -788 90 O HETATM 2166 O HOH A 280 -4.455 -4.674 11.260 0.30 9.94 O ANISOU 2166 O HOH A 280 1252 1170 1353 -122 87 137 O HETATM 2167 O HOH A 281 -26.856 -0.156 3.910 0.92 30.13 O ANISOU 2167 O HOH A 281 3006 4678 3763 -915 -305 -372 O HETATM 2168 O HOH A 282 2.725 -8.660 -6.888 0.77 31.12 O ANISOU 2168 O HOH A 282 4017 4061 3747 6 144 -694 O HETATM 2169 O HOH A 283 1.055 -6.663 -7.569 0.73 27.48 O ANISOU 2169 O HOH A 283 4535 2423 3483 -359 -1162 301 O HETATM 2170 O HOH A 284 -18.872 -20.727 14.991 0.87 26.56 O ANISOU 2170 O HOH A 284 3663 3898 2532 -763 -459 1640 O HETATM 2171 O HOH A 285 -20.954 19.135 13.906 0.73 21.38 O ANISOU 2171 O HOH A 285 3054 1465 3603 279 -134 -227 O HETATM 2172 O HOH A 286 10.180 6.909 15.394 0.75 31.60 O ANISOU 2172 O HOH A 286 3681 4051 4273 -473 -498 299 O HETATM 2173 O HOH A 287 -11.314 1.342 -7.737 0.90 30.45 O ANISOU 2173 O HOH A 287 4466 4454 2648 383 -1028 249 O HETATM 2174 O HOH A 288 -10.416 13.938 8.552 0.60 24.93 O ANISOU 2174 O HOH A 288 3298 3754 2421 -351 954 551 O HETATM 2175 O HOH A 289 12.367 7.002 18.015 0.73 27.53 O ANISOU 2175 O HOH A 289 2807 3229 4423 -1179 -13 744 O HETATM 2176 O HOH A 290 9.401 -9.450 0.449 0.85 26.97 O ANISOU 2176 O HOH A 290 2639 4055 3553 1273 503 569 O HETATM 2177 O HOH A 291 -26.030 8.381 6.437 0.43 24.05 O ANISOU 2177 O HOH A 291 2094 3356 3689 -237 -1486 -280 O HETATM 2178 O HOH A 292 -21.894 -14.210 18.941 0.55 22.46 O ANISOU 2178 O HOH A 292 3624 1770 3141 -1175 631 -9 O HETATM 2179 O HOH A 293 -22.694 20.136 12.290 0.92 28.27 O ANISOU 2179 O HOH A 293 4527 2345 3870 -1067 641 390 O HETATM 2180 O HOH A 294 6.483 -4.687 27.815 0.76 27.83 O ANISOU 2180 O HOH A 294 2951 4281 3343 1112 117 1318 O HETATM 2181 O HOH A 295 6.369 -5.328 32.040 0.69 30.82 O ANISOU 2181 O HOH A 295 3119 4206 4386 -516 -184 -89 O HETATM 2182 O HOH A 296 -16.723 -18.184 20.476 0.75 25.16 O ANISOU 2182 O HOH A 296 2684 3955 2922 -348 1191 -48 O HETATM 2183 O HOH A 297 4.868 11.532 20.373 0.73 31.66 O ANISOU 2183 O HOH A 297 3749 3671 4610 -504 -138 377 O HETATM 2184 O HOH A 298 3.893 0.664 -4.103 0.52 24.03 O ANISOU 2184 O HOH A 298 3306 2857 2968 -827 1532 -476 O HETATM 2185 O HOH A 299 -17.624 -6.899 42.535 0.44 19.85 O ANISOU 2185 O HOH A 299 3156 2853 1534 -103 -45 260 O HETATM 2186 O HOH A 300 10.446 -5.149 -5.599 0.64 26.64 O ANISOU 2186 O HOH A 300 2986 2745 4392 1381 536 527 O HETATM 2187 O HOH A 301 4.746 4.957 10.932 0.64 30.17 O ANISOU 2187 O HOH A 301 4569 2957 3936 1414 645 1182 O HETATM 2188 O HOH A 302 1.092 -18.394 13.171 0.76 26.74 O ANISOU 2188 O HOH A 302 2548 3923 3689 1451 803 556 O HETATM 2189 O HOH A 303 -27.298 -10.610 22.735 0.72 27.72 O ANISOU 2189 O HOH A 303 3447 3413 3674 -797 898 756 O HETATM 2190 O HOH A 305 1.522 13.003 17.657 0.76 28.00 O ANISOU 2190 O HOH A 305 2870 4053 3716 -284 -26 464 O HETATM 2191 O HOH A 306 -5.178 -16.632 32.472 0.59 27.00 O ANISOU 2191 O HOH A 306 3902 3501 2854 480 331 1294 O HETATM 2192 O HOH A 307 9.723 0.122 14.503 0.69 22.19 O ANISOU 2192 O HOH A 307 2632 2316 3484 351 -1560 -494 O HETATM 2193 O HOH A 308 -0.653 -17.369 29.674 0.58 25.23 O ANISOU 2193 O HOH A 308 3371 3556 2657 -398 -872 259 O HETATM 2194 O HOH A 309 -16.644 12.706 34.510 0.67 27.82 O ANISOU 2194 O HOH A 309 3508 3524 3538 -651 565 -1036 O HETATM 2195 O HOH A 310 -12.900 7.207 31.361 0.59 25.12 O ANISOU 2195 O HOH A 310 3084 4126 2335 100 -489 587 O HETATM 2196 O HOH A 311 -0.569 12.450 14.154 0.69 30.46 O ANISOU 2196 O HOH A 311 4243 3712 3619 946 831 -525 O HETATM 2197 O HOH A 312 -4.415 -5.325 -7.960 0.59 24.62 O ANISOU 2197 O HOH A 312 2713 4136 2504 165 22 -1451 O HETATM 2198 O HOH A 313 -12.657 10.014 -5.579 0.86 31.27 O ANISOU 2198 O HOH A 313 3242 4730 3909 -504 -796 202 O HETATM 2199 O HOH A 314 -26.230 -2.360 35.115 0.65 32.43 O ANISOU 2199 O HOH A 314 4197 4665 3458 430 639 150 O HETATM 2200 O HOH A 315 3.434 2.853 0.101 0.49 22.73 O ANISOU 2200 O HOH A 315 2597 2129 3910 -209 166 1485 O HETATM 2201 O HOH A 316 3.984 -12.193 11.492 0.52 23.23 O ANISOU 2201 O HOH A 316 2406 3229 3191 162 673 585 O HETATM 2202 O HOH A 317 -6.487 -19.510 5.588 0.88 29.97 O ANISOU 2202 O HOH A 317 2913 3911 4561 695 632 784 O HETATM 2203 O HOH A 318 -19.986 -8.368 35.938 0.59 26.48 O ANISOU 2203 O HOH A 318 3712 3626 2722 281 -649 1150 O HETATM 2204 O HOH A 319 6.899 -1.173 -7.118 0.45 19.48 O ANISOU 2204 O HOH A 319 2064 1341 3996 157 847 394 O HETATM 2205 O HOH A 320 9.573 -2.169 -6.677 0.63 27.01 O ANISOU 2205 O HOH A 320 3171 3102 3991 985 -22 862 O HETATM 2206 O HOH A 321 1.672 2.339 36.161 0.68 29.83 O ANISOU 2206 O HOH A 321 3567 4640 3129 65 426 -203 O HETATM 2207 O HOH A 322 -15.141 14.910 31.136 0.54 23.21 O ANISOU 2207 O HOH A 322 2477 2657 3683 -116 687 490 O HETATM 2208 O HOH A 323 -26.260 3.221 34.345 0.77 33.78 O ANISOU 2208 O HOH A 323 3445 4530 4859 379 -236 665 O HETATM 2209 O HOH A 324 9.268 7.666 18.309 0.84 28.15 O ANISOU 2209 O HOH A 324 2928 2914 4852 -310 580 184 O HETATM 2210 O HOH A 325 -4.948 -7.883 -8.545 0.87 29.51 O ANISOU 2210 O HOH A 325 3672 3984 3559 -475 226 -403 O HETATM 2211 O HOH A 326 -25.662 11.239 19.657 0.74 25.87 O ANISOU 2211 O HOH A 326 2925 3032 3872 600 -126 121 O HETATM 2212 O HOH A 327 14.791 -7.178 7.770 0.61 29.69 O ANISOU 2212 O HOH A 327 2380 4739 4162 1682 424 544 O HETATM 2213 O HOH A 328 -25.172 20.740 8.900 0.74 33.89 O ANISOU 2213 O HOH A 328 4211 4053 4613 296 -648 480 O HETATM 2214 O HOH A 329 1.703 -9.750 32.141 0.74 28.03 O ANISOU 2214 O HOH A 329 3554 3841 3254 678 -629 340 O HETATM 2215 O HOH A 330 0.251 19.516 17.516 0.79 30.24 O ANISOU 2215 O HOH A 330 3365 3565 4561 -683 280 674 O HETATM 2216 O HOH A 331 -0.405 -20.558 15.104 0.69 29.52 O ANISOU 2216 O HOH A 331 3138 2869 5208 1661 12 -623 O HETATM 2217 O HOH A 332 -0.399 -15.362 27.628 0.76 31.50 O ANISOU 2217 O HOH A 332 3592 3303 5073 1132 -19 322 O HETATM 2218 O HOH A 333 -15.048 11.586 35.735 0.92 34.51 O ANISOU 2218 O HOH A 333 4221 4401 4489 45 138 -851 O HETATM 2219 O HOH A 334 -12.059 0.285 41.608 0.38 21.05 O ANISOU 2219 O HOH A 334 2760 3454 1785 779 68 -569 O HETATM 2220 O HOH A 335 -11.990 -3.400 39.717 0.48 20.62 O ANISOU 2220 O HOH A 335 2662 3510 1663 136 188 437 O HETATM 2221 O HOH A 336 -20.098 -2.137 43.361 0.90 34.67 O ANISOU 2221 O HOH A 336 4323 4932 3916 171 234 -14 O HETATM 2222 O HOH A 337 -20.102 16.996 23.575 0.58 27.83 O ANISOU 2222 O HOH A 337 3200 3111 4265 951 49 -1728 O HETATM 2223 O HOH A 338 8.235 -8.249 -8.128 0.82 32.65 O ANISOU 2223 O HOH A 338 3996 3979 4431 1387 636 -1070 O HETATM 2224 O HOH A 339 -1.613 18.225 16.091 0.70 30.44 O ANISOU 2224 O HOH A 339 3826 3834 3907 -818 901 357 O HETATM 2225 O HOH A 340 -10.580 3.263 37.904 0.50 24.48 O ANISOU 2225 O HOH A 340 3621 2706 2973 -1175 1712 -1368 O HETATM 2226 O HOH A 341 1.252 3.252 5.463 0.59 28.07 O ANISOU 2226 O HOH A 341 3124 2716 4825 -1590 -569 -326 O HETATM 2227 O HOH A 342 -11.095 -23.643 12.250 0.77 21.97 O ANISOU 2227 O HOH A 342 3074 1733 3540 -212 -1290 464 O HETATM 2228 O HOH A 343 -23.361 0.840 34.981 0.74 22.33 O ANISOU 2228 O HOH A 343 1893 4552 2039 1089 260 649 O HETATM 2229 O HOH A 344 -6.995 -20.158 24.186 0.72 22.17 O ANISOU 2229 O HOH A 344 4273 1458 2693 273 -1104 -118 O HETATM 2230 O HOH A 345 -17.165 -8.321 20.521 0.99 7.68 O ANISOU 2230 O HOH A 345 976 1032 908 -109 138 -25 O HETATM 2231 O HOH A 346 -4.850 7.739 5.729 0.82 26.79 O ANISOU 2231 O HOH A 346 3822 3857 2501 -2232 949 -206 O HETATM 2232 O HOH A 347 -16.637 -14.892 28.764 0.89 27.07 O ANISOU 2232 O HOH A 347 2974 4648 2664 692 64 1350 O HETATM 2233 O HOH A 348 -24.309 -7.043 0.575 1.00 27.23 O ANISOU 2233 O HOH A 348 4123 2634 3589 -941 -1371 -109 O HETATM 2234 O HOH A 349 -0.755 -19.827 8.849 0.79 32.89 O ANISOU 2234 O HOH A 349 5030 3082 4387 1914 926 -780 O HETATM 2235 O HOH A 350 -9.208 21.115 23.707 0.62 27.89 O ANISOU 2235 O HOH A 350 3909 2122 4567 -333 -62 -283 O HETATM 2236 O HOH A 351 -9.700 13.361 10.624 0.85 32.12 O ANISOU 2236 O HOH A 351 4134 3643 4427 -558 132 -938 O HETATM 2237 O HOH A 352 1.023 3.447 -5.111 1.00 31.14 O ANISOU 2237 O HOH A 352 5077 2405 4349 227 1402 80 O HETATM 2238 O AHOH A 353 -6.653 6.789 12.156 0.62 32.70 O ANISOU 2238 O AHOH A 353 4482 3118 4822 -1716 -781 -690 O HETATM 2239 O BHOH A 353 -7.068 8.330 10.834 0.38 53.22 O ANISOU 2239 O BHOH A 353 6402 6697 7121 -496 383 49 O HETATM 2240 O HOH A 354 -24.889 -1.662 33.281 0.55 24.35 O ANISOU 2240 O HOH A 354 3170 3483 2601 1607 677 -511 O HETATM 2241 O HOH A 355 -1.806 16.602 12.449 0.80 29.31 O ANISOU 2241 O HOH A 355 4753 2968 3415 895 1612 1410 O HETATM 2242 O HOH A 356 -28.654 5.856 26.012 0.91 32.51 O ANISOU 2242 O HOH A 356 3357 4489 4506 -182 -1569 -555 O HETATM 2243 O HOH A 357 -4.764 -21.716 5.442 0.98 33.28 O ANISOU 2243 O HOH A 357 4017 4169 4460 644 378 -154 O HETATM 2244 O HOH A 358 -27.520 -1.536 8.340 1.00 36.95 O ANISOU 2244 O HOH A 358 4095 5205 4741 140 -142 748 O HETATM 2245 O HOH A 359 -24.097 0.403 28.213 0.63 32.85 O ANISOU 2245 O HOH A 359 4344 4193 3944 -445 367 1067 O HETATM 2246 O HOH A 360 -1.312 -3.911 15.749 0.91 7.08 O ANISOU 2246 O HOH A 360 890 973 827 -89 25 -76 O HETATM 2247 O HOH A 361 1.571 -8.143 -4.972 1.00 37.32 O ANISOU 2247 O HOH A 361 4859 4804 4516 16 751 -456 O HETATM 2248 O HOH A 362 -15.604 -20.149 22.496 0.90 32.50 O ANISOU 2248 O HOH A 362 4038 2776 5534 1330 1279 -89 O HETATM 2249 O HOH A 363 -21.404 -0.261 -1.978 1.00 34.22 O ANISOU 2249 O HOH A 363 4358 4829 3815 796 -60 605 O HETATM 2250 O HOH A 364 -15.359 -10.798 -3.771 1.00 31.51 O ANISOU 2250 O HOH A 364 3038 4110 4822 -428 -552 -587 O HETATM 2251 O HOH A 365 -25.233 -1.175 29.224 0.88 35.05 O ANISOU 2251 O HOH A 365 4241 4524 4553 -930 -945 -12 O HETATM 2252 O HOH A 366 -16.320 17.045 26.552 1.00 35.12 O ANISOU 2252 O HOH A 366 4063 4492 4788 -524 775 -1358 O HETATM 2253 O HOH A 367 -30.134 4.303 27.378 1.00 38.10 O ANISOU 2253 O HOH A 367 4195 5443 4838 -546 -1361 -631 O HETATM 2254 O HOH A 368 -5.579 -13.806 34.269 0.86 33.99 O ANISOU 2254 O HOH A 368 3836 5184 3896 86 -370 1149 O HETATM 2255 O HOH A 369 3.414 3.162 -4.168 1.00 35.01 O ANISOU 2255 O HOH A 369 4738 3778 4788 -488 730 -98 O HETATM 2256 O HOH A 370 -20.261 17.998 3.431 0.98 35.57 O ANISOU 2256 O HOH A 370 4343 4964 4206 405 -907 862 O HETATM 2257 O HOH A 371 -17.896 -14.370 30.936 0.84 32.08 O ANISOU 2257 O HOH A 371 3643 4832 3714 613 -1015 864 O HETATM 2258 O HOH A 372 0.973 10.073 26.985 0.85 34.84 O ANISOU 2258 O HOH A 372 4450 4492 4294 -739 -580 -368 O HETATM 2259 O HOH A 373 -20.610 6.216 32.979 0.70 33.05 O ANISOU 2259 O HOH A 373 3750 4282 4525 -145 513 1085 O HETATM 2260 O HOH A 374 -28.495 -1.292 28.486 0.95 37.93 O ANISOU 2260 O HOH A 374 4412 5033 4968 -266 300 289 O HETATM 2261 O HOH A 375 -3.164 14.959 11.493 0.89 34.40 O ANISOU 2261 O HOH A 375 3606 5445 4019 -39 773 690 O HETATM 2262 O HOH A 376 10.462 5.447 13.151 0.97 37.76 O ANISOU 2262 O HOH A 376 4240 5340 4768 -547 981 1150 O HETATM 2263 O HOH A 377 15.686 -6.202 5.152 0.91 36.45 O ANISOU 2263 O HOH A 377 3700 4820 5327 592 127 625 O HETATM 2264 O HOH A 378 -20.434 -4.743 -3.560 0.74 30.20 O ANISOU 2264 O HOH A 378 3448 4371 3656 -1047 -1644 -554 O HETATM 2265 O HOH A 379 -27.800 -3.939 8.712 1.00 39.35 O ANISOU 2265 O HOH A 379 4045 5658 5247 -135 -398 -575 O HETATM 2266 O HOH A 380 -23.510 -6.944 -2.083 0.92 37.17 O ANISOU 2266 O HOH A 380 3835 4880 5409 -400 -12 -653 O HETATM 2267 O HOH A 381 5.623 -13.730 8.315 0.97 37.90 O ANISOU 2267 O HOH A 381 4383 4993 5025 717 -434 47 O HETATM 2268 O HOH A 382 3.021 6.779 32.198 0.92 32.97 O ANISOU 2268 O HOH A 382 5000 4008 3520 362 -785 -1960 O HETATM 2269 O HOH A 383 1.724 9.312 30.984 0.97 40.62 O ANISOU 2269 O HOH A 383 5362 4878 5194 -531 -494 -1119 O HETATM 2270 O HOH A 384 6.668 1.547 31.675 0.78 36.22 O ANISOU 2270 O HOH A 384 4100 5658 4003 -381 -1399 -358 O HETATM 2271 O HOH A 385 -4.567 -13.420 18.089 0.90 7.53 O ANISOU 2271 O HOH A 385 1085 836 939 87 -85 16 O HETATM 2272 O HOH A 386 -2.631 -18.962 21.884 0.78 34.00 O ANISOU 2272 O HOH A 386 4498 3142 5277 890 -800 1039 O HETATM 2273 O HOH A 387 -14.190 -21.412 0.787 0.81 37.33 O ANISOU 2273 O HOH A 387 4513 4623 5048 1049 1256 -1093 O HETATM 2274 O HOH A 388 -3.590 -11.077 20.982 0.92 7.58 O ANISOU 2274 O HOH A 388 1023 1032 827 179 -82 28 O HETATM 2275 O HOH A 389 -11.184 -5.651 40.995 0.89 36.15 O ANISOU 2275 O HOH A 389 3646 4969 5122 -182 -446 225 O HETATM 2276 O HOH A 390 9.551 8.264 21.368 0.81 35.67 O ANISOU 2276 O HOH A 390 3864 3996 5692 -636 -263 -248 O HETATM 2277 O HOH A 391 -27.157 -12.592 19.840 0.99 36.06 O ANISOU 2277 O HOH A 391 3334 4682 5684 -344 -1438 -836 O HETATM 2278 O HOH A 392 -15.691 -17.866 -1.870 1.00 38.17 O ANISOU 2278 O HOH A 392 4148 5368 4987 453 1118 547 O HETATM 2279 O HOH A 393 -28.249 6.070 15.466 0.71 36.27 O ANISOU 2279 O HOH A 393 3453 4966 5362 -408 -1443 -3 O HETATM 2280 O HOH A 394 1.141 -18.557 28.864 0.95 35.07 O ANISOU 2280 O HOH A 394 3850 4990 4484 -426 -303 1093 O HETATM 2281 O HOH A 395 8.121 -5.000 -0.437 0.75 35.90 O ANISOU 2281 O HOH A 395 4642 4433 4565 393 -542 546 O HETATM 2282 O HOH A 396 -19.260 8.599 -4.142 0.50 28.29 O ANISOU 2282 O HOH A 396 3340 4132 3279 959 -887 1500 O HETATM 2283 O HOH A 397 -2.135 -12.155 22.959 0.89 7.94 O ANISOU 2283 O HOH A 397 1045 972 999 122 -103 85 O HETATM 2284 O HOH A 398 -2.284 19.520 23.883 0.80 35.06 O ANISOU 2284 O HOH A 398 4261 4364 4697 -2626 -861 -245 O HETATM 2285 O HOH A 399 -17.002 18.609 22.296 0.79 35.51 O ANISOU 2285 O HOH A 399 3878 5102 4511 489 -492 -911 O HETATM 2286 O HOH A 400 -14.721 -20.528 27.587 0.92 37.34 O ANISOU 2286 O HOH A 400 4703 5077 4406 -80 1266 236 O HETATM 2287 O HOH A 401 -11.552 8.322 -3.218 1.00 40.44 O ANISOU 2287 O HOH A 401 4876 5372 5118 654 -653 72 O HETATM 2288 O HOH A 402 -5.307 -0.530 16.053 0.87 7.98 O ANISOU 2288 O HOH A 402 1193 854 985 -244 -259 6 O HETATM 2289 O HOH A 403 -25.770 0.157 35.414 0.96 35.67 O ANISOU 2289 O HOH A 403 3552 5666 4334 480 998 653 O HETATM 2290 O HOH A 404 -1.948 -12.388 31.707 1.00 37.74 O ANISOU 2290 O HOH A 404 4293 5550 4497 -268 -813 474 O HETATM 2291 O HOH A 405 4.400 -9.661 7.988 0.97 32.94 O ANISOU 2291 O HOH A 405 3002 4712 4800 -560 -655 296 O HETATM 2292 O HOH A 406 -20.543 2.206 -2.385 0.65 33.83 O ANISOU 2292 O HOH A 406 4429 3907 4519 -648 -198 452 O HETATM 2293 O HOH A 407 11.317 -3.603 7.934 0.84 35.12 O ANISOU 2293 O HOH A 407 3583 4948 4814 -180 662 232 O HETATM 2294 O HOH A 408 3.276 -0.401 36.954 1.00 41.75 O ANISOU 2294 O HOH A 408 4856 5575 5433 -409 -396 -237 O HETATM 2295 O HOH A 409 -21.999 19.478 16.889 1.00 41.36 O ANISOU 2295 O HOH A 409 4835 5222 5657 502 335 313 O HETATM 2296 O HOH A 410 6.714 -7.804 -10.603 0.85 37.02 O ANISOU 2296 O HOH A 410 4462 4984 4619 911 476 -287 O HETATM 2297 O HOH A 411 -10.132 -19.328 27.932 0.65 37.94 O ANISOU 2297 O HOH A 411 4401 4518 5495 -185 -116 155 O HETATM 2298 O HOH A 412 -25.292 -14.571 11.125 1.00 40.50 O ANISOU 2298 O HOH A 412 4648 5111 5631 124 82 98 O HETATM 2299 O HOH A 413 -24.151 -14.350 20.307 1.00 36.38 O ANISOU 2299 O HOH A 413 4563 3598 5660 -462 -297 497 O HETATM 2300 O HOH A 414 -30.888 1.487 5.762 0.90 42.60 O ANISOU 2300 O HOH A 414 4966 5843 5375 314 245 -14 O HETATM 2301 O HOH A 415 6.310 0.052 -1.393 0.79 37.59 O ANISOU 2301 O HOH A 415 4357 4485 5441 -756 194 482 O HETATM 2302 O HOH A 416 -5.635 -17.004 -3.496 0.69 38.47 O ANISOU 2302 O HOH A 416 4675 4496 5447 124 17 -298 O HETATM 2303 O HOH A 417 9.063 2.061 30.114 1.00 41.46 O ANISOU 2303 O HOH A 417 4931 5305 5517 -446 -120 -406 O HETATM 2304 O HOH A 418 9.304 -7.120 24.150 0.91 39.70 O ANISOU 2304 O HOH A 418 4407 5370 5307 491 515 -552 O HETATM 2305 O HOH A 419 -25.264 9.063 26.010 0.98 37.80 O ANISOU 2305 O HOH A 419 4202 5142 5020 569 63 -103 O HETATM 2306 O HOH A 420 5.246 10.002 16.720 0.91 39.15 O ANISOU 2306 O HOH A 420 5014 4881 4980 -431 -95 920 O HETATM 2307 O HOH A 421 -31.235 -12.852 20.764 0.77 36.46 O ANISOU 2307 O HOH A 421 4137 3977 5737 -2097 270 551 O HETATM 2308 O HOH A 422 -1.859 -6.322 -8.128 0.97 40.54 O ANISOU 2308 O HOH A 422 5207 5470 4727 -22 126 51 O HETATM 2309 O HOH A 423 4.509 7.442 13.697 0.92 37.52 O ANISOU 2309 O HOH A 423 4262 5151 4842 886 -68 559 O HETATM 2310 O HOH A 424 4.098 -8.797 33.010 0.98 40.92 O ANISOU 2310 O HOH A 424 4990 5258 5300 503 -465 195 O HETATM 2311 O HOH A 425 -6.524 1.958 -7.755 1.00 40.35 O ANISOU 2311 O HOH A 425 4907 5192 5233 295 194 429 O HETATM 2312 O HOH A 426 -6.020 0.230 40.009 0.92 41.70 O ANISOU 2312 O HOH A 426 5166 5487 5190 -652 26 -821 O HETATM 2313 O HOH A 427 6.727 -2.654 0.379 0.78 41.33 O ANISOU 2313 O HOH A 427 4737 5353 5612 230 312 -183 O HETATM 2314 O HOH A 428 5.153 -13.303 17.273 0.98 39.36 O ANISOU 2314 O HOH A 428 4765 5031 5159 937 -341 458 O HETATM 2315 O HOH A 429 -24.795 -11.057 24.184 0.80 37.28 O ANISOU 2315 O HOH A 429 4505 4732 4927 116 723 -242 O HETATM 2316 O HOH A 430 6.142 8.768 14.795 0.60 40.83 O ANISOU 2316 O HOH A 430 5116 4611 5786 -101 -387 406 O HETATM 2317 O HOH A 431 -28.991 6.490 7.366 0.91 39.14 O ANISOU 2317 O HOH A 431 5252 5181 4439 62 -332 1207 O HETATM 2318 O HOH A 432 9.139 -13.281 16.172 0.94 39.18 O ANISOU 2318 O HOH A 432 4544 4747 5594 -827 321 580 O HETATM 2319 O HOH A 433 -23.150 15.585 18.599 0.97 40.08 O ANISOU 2319 O HOH A 433 4123 5772 5334 489 -160 -235 O HETATM 2320 O HOH A 434 -22.727 12.228 27.208 0.80 37.74 O ANISOU 2320 O HOH A 434 3983 5088 5268 1863 1258 -591 O HETATM 2321 O HOH A 435 -22.079 -15.264 21.320 0.74 40.01 O ANISOU 2321 O HOH A 435 4768 4808 5626 -441 366 154 O HETATM 2322 O HOH A 436 -13.981 17.022 31.227 0.97 40.24 O ANISOU 2322 O HOH A 436 4942 5036 5310 -49 -667 163 O HETATM 2323 O HOH A 437 0.411 15.443 14.088 0.90 41.29 O ANISOU 2323 O HOH A 437 4776 5340 5573 -689 440 711 O HETATM 2324 O HOH A 438 -8.835 -3.675 7.993 0.89 5.88 O ANISOU 2324 O HOH A 438 937 743 553 9 -53 38 O HETATM 2325 O HOH A 439 -17.291 18.624 3.948 1.00 33.04 O ANISOU 2325 O HOH A 439 4104 3360 5089 198 -1271 -1021 O HETATM 2326 O HOH A 440 -21.632 1.048 0.381 0.89 30.32 O ANISOU 2326 O HOH A 440 5099 2533 3889 -1844 723 240 O HETATM 2327 O HOH A 441 4.346 -6.013 34.170 1.00 46.45 O ANISOU 2327 O HOH A 441 5135 6394 6119 362 -755 282 O HETATM 2328 O HOH A 442 -14.264 4.084 33.252 1.00 46.80 O ANISOU 2328 O HOH A 442 6019 6210 5554 675 367 -358 O HETATM 2329 O HOH A 443 -26.329 0.858 25.201 0.97 45.49 O ANISOU 2329 O HOH A 443 4646 5605 7034 -442 -441 -218 O HETATM 2330 O HOH A 444 6.348 -12.168 6.404 0.86 46.87 O ANISOU 2330 O HOH A 444 5171 6279 6356 -1196 -354 300 O HETATM 2331 O HOH A 445 0.452 -15.673 24.262 1.00 46.48 O ANISOU 2331 O HOH A 445 5537 5677 6447 522 -5 827 O HETATM 2332 O HOH A 446 -14.873 -23.664 4.008 1.00 49.61 O ANISOU 2332 O HOH A 446 6491 6078 6283 473 1320 13 O HETATM 2333 O HOH A 447 1.277 -10.272 29.614 1.00 48.88 O ANISOU 2333 O HOH A 447 5292 6919 6363 202 -926 261 O HETATM 2334 O HOH A 448 -26.130 -7.230 15.061 0.69 46.98 O ANISOU 2334 O HOH A 448 5720 6238 5891 -129 -856 -999 O HETATM 2335 O HOH A 449 -19.834 -13.621 24.631 1.00 49.29 O ANISOU 2335 O HOH A 449 6414 5883 6433 133 174 -490 O HETATM 2336 O HOH A 450 -22.233 -13.095 24.039 1.00 49.77 O ANISOU 2336 O HOH A 450 6254 6126 6530 -773 696 325 O HETATM 2337 O HOH A 451 1.309 -16.546 14.821 1.00 49.22 O ANISOU 2337 O HOH A 451 5363 6168 7172 -118 -404 298 O HETATM 2338 O HOH A 452 1.440 5.929 34.231 1.00 48.20 O ANISOU 2338 O HOH A 452 5669 6069 6574 363 -627 -730 O HETATM 2339 O HOH A 453 -13.043 9.906 -1.553 0.99 49.95 O ANISOU 2339 O HOH A 453 5638 6437 6905 303 237 -49 O HETATM 2340 O HOH A 454 -26.567 9.972 23.992 0.83 49.88 O ANISOU 2340 O HOH A 454 5923 6075 6953 100 150 -169 O HETATM 2341 O HOH A 455 -29.299 -1.474 4.943 0.99 51.58 O ANISOU 2341 O HOH A 455 6093 6828 6678 792 -105 550 O HETATM 2342 O HOH A 456 -0.333 -20.458 27.919 1.00 49.66 O ANISOU 2342 O HOH A 456 5650 6543 6675 234 -83 416 O HETATM 2343 O HOH A 457 -8.795 -15.648 33.000 0.98 34.90 O ANISOU 2343 O HOH A 457 4799 4738 3721 736 -986 1532 O HETATM 2344 O HOH A 458 12.521 -6.839 -2.061 1.00 41.25 O ANISOU 2344 O HOH A 458 5483 4863 5327 978 317 -518 O HETATM 2345 O HOH A 459 -13.008 2.220 33.285 0.84 41.28 O ANISOU 2345 O HOH A 459 5184 5662 4840 291 40 760 O HETATM 2346 O HOH A 460 -25.509 8.305 28.390 1.00 43.52 O ANISOU 2346 O HOH A 460 4891 5867 5777 857 766 -169 O HETATM 2347 O HOH A 461 0.182 -3.078 39.420 1.00 45.84 O ANISOU 2347 O HOH A 461 5622 5907 5887 153 135 206 O HETATM 2348 O HOH A 462 -25.866 14.783 8.645 1.00 46.04 O ANISOU 2348 O HOH A 462 5709 5674 6110 6 -450 133 O HETATM 2349 O HOH A 463 -27.351 4.671 6.370 1.00 46.04 O ANISOU 2349 O HOH A 463 5746 5926 5820 10 124 576 O HETATM 2350 O HOH A 464 5.861 -2.698 7.034 1.00 44.95 O ANISOU 2350 O HOH A 464 5649 6028 5401 199 187 12 O HETATM 2351 O HOH A 465 -25.131 -9.906 32.210 1.00 46.10 O ANISOU 2351 O HOH A 465 5058 6085 6373 -611 -324 188 O HETATM 2352 O HOH A 466 -2.059 3.574 11.205 1.00 44.57 O ANISOU 2352 O HOH A 466 5414 5610 5913 341 -455 -295 O HETATM 2353 O HOH A 467 -8.076 -15.407 11.465 0.93 8.55 O ANISOU 2353 O HOH A 467 1150 932 1166 40 77 -141 O HETATM 2354 O HOH A 468 -24.711 -4.438 -2.629 1.00 44.05 O ANISOU 2354 O HOH A 468 5617 5212 5909 -86 618 -183 O HETATM 2355 O HOH A 469 -2.872 12.400 12.650 1.00 45.75 O ANISOU 2355 O HOH A 469 5589 5520 6275 -176 127 213 O HETATM 2356 O HOH A 470 -19.320 14.656 32.807 0.98 46.37 O ANISOU 2356 O HOH A 470 5683 6168 5769 -416 -370 292 O HETATM 2357 O HOH A 471 -28.193 -2.684 10.676 1.00 46.54 O ANISOU 2357 O HOH A 471 5305 6283 6095 -9 -8 -422 O HETATM 2358 O HOH A 472 13.028 -0.029 9.714 1.00 47.89 O ANISOU 2358 O HOH A 472 5447 6532 6217 367 -350 -583 O HETATM 2359 O HOH A 473 8.330 6.857 25.992 1.00 50.65 O ANISOU 2359 O HOH A 473 6092 6693 6458 6 -506 -536 O HETATM 2360 O HOH A 474 -19.235 14.357 9.446 0.83 44.89 O ANISOU 2360 O HOH A 474 5019 5607 6428 321 713 -510 O HETATM 2361 O HOH A 475 -7.586 1.608 37.486 0.85 53.39 O ANISOU 2361 O HOH A 475 6494 6786 7004 569 -300 190 O HETATM 2362 O HOH A 476 4.032 -11.663 23.201 1.00 48.25 O ANISOU 2362 O HOH A 476 5604 6353 6374 890 305 595 O HETATM 2363 O HOH A 477 -12.587 4.662 34.907 1.00 48.36 O ANISOU 2363 O HOH A 477 5713 6396 6264 -55 413 555 O HETATM 2364 O HOH A 478 8.618 -12.242 7.885 1.00 48.89 O ANISOU 2364 O HOH A 478 5990 6005 6582 491 160 -290 O HETATM 2365 O HOH A 479 8.082 8.305 23.403 0.92 48.49 O ANISOU 2365 O HOH A 479 5309 6510 6604 -436 -471 -377 O HETATM 2366 O HOH A 480 6.549 8.712 25.106 1.00 47.68 O ANISOU 2366 O HOH A 480 5859 6116 6141 -539 -441 34 O HETATM 2367 O HOH A 481 -10.847 8.878 25.684 0.87 8.31 O ANISOU 2367 O HOH A 481 1165 1006 986 -85 53 -148 O HETATM 2368 O HOH A 482 3.666 2.902 8.163 1.00 50.28 O ANISOU 2368 O HOH A 482 6157 6695 6251 -140 -334 355 O HETATM 2369 O HOH A 483 3.345 -9.685 24.950 1.00 48.64 O ANISOU 2369 O HOH A 483 5679 6634 6166 85 236 -99 O HETATM 2370 O HOH A 484 5.788 -7.813 31.722 1.00 52.30 O ANISOU 2370 O HOH A 484 6450 6486 6935 58 82 193 O HETATM 2371 O HOH A 485 5.070 9.022 27.380 1.00 51.34 O ANISOU 2371 O HOH A 485 5978 6576 6952 26 -205 -304 O HETATM 2372 O HOH A 486 -18.085 6.480 38.676 0.99 49.33 O ANISOU 2372 O HOH A 486 5940 6316 6487 -300 -895 -33 O HETATM 2373 O HOH A 487 -17.059 -4.141 -4.972 0.96 49.64 O ANISOU 2373 O HOH A 487 6161 6670 6030 666 -360 40 O HETATM 2374 O HOH A 488 -0.949 -17.317 18.052 1.00 29.25 O ANISOU 2374 O HOH A 488 3707 3701 3707 9 1 7 O HETATM 2375 O HOH A 489 -4.049 20.844 15.811 1.00 29.24 O ANISOU 2375 O HOH A 489 3702 3703 3706 -2 -1 -1 O HETATM 2376 O HOH A 490 -15.392 1.154 -5.045 1.00 29.22 O ANISOU 2376 O HOH A 490 3699 3704 3700 4 -5 -11 O HETATM 2377 O AHOH A 491 2.568 -4.168 7.839 0.94 29.11 O ANISOU 2377 O AHOH A 491 3686 3688 3688 3 -7 1 O HETATM 2378 O HOH A 492 -2.619 -8.576 29.257 0.94 9.69 O ANISOU 2378 O HOH A 492 1091 1478 1115 8 -254 195 O HETATM 2379 O HOH A 493 -3.439 -13.106 25.295 0.93 9.48 O ANISOU 2379 O HOH A 493 1179 1327 1096 190 -30 274 O HETATM 2380 O HOH A 494 -21.753 -7.073 23.706 0.90 10.00 O ANISOU 2380 O HOH A 494 898 1423 1477 18 -223 -438 O HETATM 2381 O HOH A 495 -22.128 5.941 4.871 0.88 10.28 O ANISOU 2381 O HOH A 495 1217 1234 1457 -84 -322 150 O HETATM 2382 O HOH A 496 1.067 -1.413 29.549 0.97 11.92 O ANISOU 2382 O HOH A 496 1105 2118 1306 17 -306 437 O HETATM 2383 O HOH A 497 4.745 -4.747 21.086 0.97 10.96 O ANISOU 2383 O HOH A 497 875 1926 1362 154 55 -308 O HETATM 2384 O HOH A 498 0.060 -0.795 -4.638 0.88 9.92 O ANISOU 2384 O HOH A 498 1489 1208 1072 37 289 262 O HETATM 2385 O HOH A 499 -3.770 -15.718 24.488 1.00 11.78 O ANISOU 2385 O HOH A 499 1500 1340 1638 282 170 182 O HETATM 2386 O HOH A 500 -19.449 10.154 9.018 0.87 9.86 O ANISOU 2386 O HOH A 500 1167 1139 1440 63 -204 -33 O HETATM 2387 O HOH A 501 8.489 -3.714 21.202 0.92 10.55 O ANISOU 2387 O HOH A 501 1061 1618 1328 -81 -131 7 O HETATM 2388 O HOH A 502 -12.929 -17.123 16.976 0.80 9.90 O ANISOU 2388 O HOH A 502 1298 1016 1445 -120 -179 80 O HETATM 2389 O HOH A 503 -21.334 8.064 1.997 0.89 11.26 O ANISOU 2389 O HOH A 503 1446 1223 1610 99 -551 141 O HETATM 2390 O HOH A 504 -17.834 19.301 6.184 0.71 8.03 O ANISOU 2390 O HOH A 504 1294 499 1258 -10 -136 -44 O HETATM 2391 O HOH A 505 -13.973 10.534 28.047 0.88 12.01 O ANISOU 2391 O HOH A 505 1502 1679 1384 -128 500 -246 O HETATM 2392 O HOH A 506 -17.941 -20.529 8.166 0.78 10.28 O ANISOU 2392 O HOH A 506 1418 1143 1346 -261 -173 18 O HETATM 2393 O HOH A 507 -2.653 -3.056 11.574 0.91 11.12 O ANISOU 2393 O HOH A 507 1130 1987 1110 130 -137 27 O HETATM 2394 O HOH A 508 -10.453 -18.222 17.270 0.69 9.31 O ANISOU 2394 O HOH A 508 1362 795 1380 -144 -71 67 O HETATM 2395 O HOH A 509 -5.078 0.967 10.008 0.72 10.84 O ANISOU 2395 O HOH A 509 1231 1543 1343 217 -203 123 O HETATM 2396 O HOH A 510 7.529 6.183 21.817 0.90 12.06 O ANISOU 2396 O HOH A 510 984 1549 2050 -91 29 -1 O HETATM 2397 O HOH A 511 -7.569 -8.523 32.734 0.77 10.87 O ANISOU 2397 O HOH A 511 1509 1522 1099 148 -33 -53 O HETATM 2398 O HOH A 512 -4.172 0.781 14.058 0.65 9.64 O ANISOU 2398 O HOH A 512 1002 1263 1396 -99 -175 172 O HETATM 2399 O HOH A 513 -6.978 6.102 6.546 0.93 14.41 O ANISOU 2399 O HOH A 513 1385 1281 2810 -76 -55 -92 O HETATM 2400 O HOH A 514 -24.095 -0.633 4.057 1.00 15.11 O ANISOU 2400 O HOH A 514 2379 1830 1531 -671 -178 -99 O HETATM 2401 O HOH A 515 -18.074 10.754 11.408 0.85 13.86 O ANISOU 2401 O HOH A 515 1489 2130 1648 16 -387 -11 O HETATM 2402 O HOH A 516 5.333 7.229 20.427 0.94 14.19 O ANISOU 2402 O HOH A 516 1308 1458 2623 -395 -447 -27 O HETATM 2403 O HOH A 517 2.263 -13.141 5.284 0.77 11.83 O ANISOU 2403 O HOH A 517 1414 1613 1468 535 -18 -18 O HETATM 2404 O HOH A 518 -16.193 -12.215 24.552 0.86 12.28 O ANISOU 2404 O HOH A 518 1322 1711 1633 380 -224 80 O HETATM 2405 O HOH A 519 3.495 5.188 29.923 0.98 15.50 O ANISOU 2405 O HOH A 519 1631 2011 2249 -6 -970 -441 O HETATM 2406 O HOH A 520 -24.977 -7.620 9.268 0.77 11.75 O ANISOU 2406 O HOH A 520 1383 1524 1558 -167 -207 -55 O HETATM 2407 O HOH A 521 -6.815 -20.159 19.629 0.63 9.88 O ANISOU 2407 O HOH A 521 1642 1039 1074 -283 58 123 O HETATM 2408 O HOH A 522 -13.094 -16.752 26.678 0.71 11.15 O ANISOU 2408 O HOH A 522 1357 1288 1593 -132 310 40 O HETATM 2409 O HOH A 523 -14.464 -16.511 29.047 0.90 15.37 O ANISOU 2409 O HOH A 523 1900 2322 1615 -376 276 409 O HETATM 2410 O HOH A 524 1.059 8.955 24.560 0.73 11.84 O ANISOU 2410 O HOH A 524 1382 1417 1699 -470 -238 -102 O HETATM 2411 O HOH A 525 -16.496 -9.880 33.083 0.91 14.94 O ANISOU 2411 O HOH A 525 1871 1898 1907 506 477 784 O HETATM 2412 O HOH A 526 -20.457 10.969 26.694 0.98 15.41 O ANISOU 2412 O HOH A 526 1776 1522 2557 -88 287 -390 O HETATM 2413 O HOH A 527 4.178 -6.432 7.960 0.82 14.06 O ANISOU 2413 O HOH A 527 1910 2238 1193 357 -47 -42 O HETATM 2414 O HOH A 528 -0.289 -14.110 22.271 0.85 13.60 O ANISOU 2414 O HOH A 528 1385 1491 2290 479 -187 -180 O HETATM 2415 O HOH A 529 -14.639 -18.461 18.813 0.75 12.07 O ANISOU 2415 O HOH A 529 1767 1346 1474 -219 -23 99 O HETATM 2416 O HOH A 530 -26.494 2.907 21.002 0.83 14.96 O ANISOU 2416 O HOH A 530 1522 2124 2039 -856 -396 513 O HETATM 2417 O HOH A 531 -23.357 -2.929 6.921 0.87 14.73 O ANISOU 2417 O HOH A 531 1803 1459 2336 -236 529 -274 O HETATM 2418 O HOH A 532 -9.454 -9.915 -1.118 0.83 15.10 O ANISOU 2418 O HOH A 532 2614 1977 1147 837 224 174 O HETATM 2419 O HOH A 533 -11.999 9.594 3.295 0.67 11.14 O ANISOU 2419 O HOH A 533 1379 1122 1732 -9 87 353 O HETATM 2420 O HOH A 534 -13.381 -18.436 14.652 0.69 10.92 O ANISOU 2420 O HOH A 534 1862 1020 1265 170 -211 42 O HETATM 2421 O HOH A 535 -22.919 -5.856 2.831 0.79 13.01 O ANISOU 2421 O HOH A 535 1257 1645 2041 12 -208 434 O HETATM 2422 O HOH A 536 -0.623 10.964 23.658 0.69 11.77 O ANISOU 2422 O HOH A 536 1551 1444 1478 149 -288 -211 O HETATM 2423 O HOH A 537 -12.136 2.895 31.014 0.89 14.69 O ANISOU 2423 O HOH A 537 1800 1901 1878 8 -513 -736 O HETATM 2424 O HOH A 538 -2.862 6.281 -1.523 0.83 15.53 O ANISOU 2424 O HOH A 538 1355 1037 3509 -338 455 198 O HETATM 2425 O HOH A 539 -23.084 -11.507 14.189 0.94 14.40 O ANISOU 2425 O HOH A 539 1394 1882 2197 48 -226 223 O HETATM 2426 O HOH A 540 -20.050 -16.523 3.035 0.98 19.82 O ANISOU 2426 O HOH A 540 1665 4734 1133 -1150 -422 184 O HETATM 2427 O HOH A 541 -5.193 1.299 17.695 0.81 18.42 O ANISOU 2427 O HOH A 541 2351 1867 2780 1098 -1851 -1272 O HETATM 2428 O HOH A 542 -1.256 -10.931 29.093 0.88 15.77 O ANISOU 2428 O HOH A 542 2104 2211 1677 736 -494 -4 O HETATM 2429 O HOH A 543 4.850 -7.247 22.355 0.79 13.66 O ANISOU 2429 O HOH A 543 1253 1938 2000 110 238 75 O HETATM 2430 O HOH A 544 -16.344 16.136 23.569 0.78 15.92 O ANISOU 2430 O HOH A 544 1395 1033 3622 41 518 -507 O HETATM 2431 O HOH A 545 -3.809 -12.763 -2.878 0.78 15.14 O ANISOU 2431 O HOH A 545 2718 1643 1390 3 596 -452 O HETATM 2432 O HOH A 546 -7.269 -16.691 1.459 0.72 13.21 O ANISOU 2432 O HOH A 546 1376 1379 2263 42 168 -235 O HETATM 2433 O HOH A 547 -9.231 -5.703 36.103 0.78 13.35 O ANISOU 2433 O HOH A 547 1817 1629 1627 231 -34 303 O HETATM 2434 O HOH A 548 13.303 0.347 24.625 1.00 16.81 O ANISOU 2434 O HOH A 548 1450 2833 2105 -53 -285 -325 O HETATM 2435 O HOH A 549 -7.060 -14.729 31.746 0.88 16.52 O ANISOU 2435 O HOH A 549 3211 1629 1436 -144 366 514 O HETATM 2436 O HOH A 550 1.911 -13.865 20.673 0.84 18.11 O ANISOU 2436 O HOH A 550 2102 2300 2480 832 608 846 O HETATM 2437 O HOH A 551 15.371 -2.384 14.541 0.82 16.08 O ANISOU 2437 O HOH A 551 1318 3260 1533 225 144 857 O HETATM 2438 O HOH A 552 4.125 -3.262 26.672 0.90 15.64 O ANISOU 2438 O HOH A 552 2721 1724 1496 -863 -401 80 O HETATM 2439 O HOH A 553 -24.313 8.856 20.284 0.75 13.92 O ANISOU 2439 O HOH A 553 1507 1953 1828 80 142 134 O HETATM 2440 O HOH A 554 -27.112 -3.873 25.213 0.98 16.35 O ANISOU 2440 O HOH A 554 1507 2519 2188 455 396 153 O HETATM 2441 O HOH A 555 2.450 -11.259 9.493 0.74 13.31 O ANISOU 2441 O HOH A 555 1301 1617 2140 110 173 -26 O HETATM 2442 O HOH A 556 -19.550 17.585 6.123 0.67 13.10 O ANISOU 2442 O HOH A 556 1786 1158 2032 103 -270 245 O HETATM 2443 O HOH A 557 -1.362 9.406 28.150 0.77 17.91 O ANISOU 2443 O HOH A 557 1908 2397 2498 311 -830 -1377 O HETATM 2444 O HOH A 558 -4.152 -0.771 11.836 0.67 14.68 O ANISOU 2444 O HOH A 558 2268 1450 1858 453 -975 -329 O HETATM 2445 O HOH A 559 -19.500 -20.717 5.077 0.60 12.23 O ANISOU 2445 O HOH A 559 1794 1181 1674 -65 51 -90 O HETATM 2446 O HOH A 560 -18.684 -12.231 -3.582 0.82 14.01 O ANISOU 2446 O HOH A 560 1545 2136 1643 -316 -216 -281 O HETATM 2447 O HOH A 561 -13.069 8.046 28.891 0.66 13.90 O ANISOU 2447 O HOH A 561 1656 2078 1546 379 422 -123 O HETATM 2448 O HOH A 562 -9.709 -7.850 34.326 0.87 15.34 O ANISOU 2448 O HOH A 562 2008 1793 2029 393 291 257 O HETATM 2449 O HOH A 563 1.895 -15.306 9.505 0.81 17.83 O ANISOU 2449 O HOH A 563 1734 2951 2091 757 767 540 O HETATM 2450 O HOH A 564 -14.918 20.413 17.662 0.66 13.67 O ANISOU 2450 O HOH A 564 2184 1449 1561 -115 -429 97 O HETATM 2451 O HOH A 565 -15.303 19.609 13.129 0.55 12.25 O ANISOU 2451 O HOH A 565 2221 995 1437 162 -536 73 O HETATM 2452 O HOH A 566 -12.176 10.916 5.775 0.71 17.01 O ANISOU 2452 O HOH A 566 1720 1994 2748 -619 905 -593 O HETATM 2453 O HOH A 567 -4.724 -15.814 0.793 0.86 17.78 O ANISOU 2453 O HOH A 567 1437 1559 3758 126 93 -933 O HETATM 2454 O HOH A 568 -6.324 -4.274 -6.352 0.86 17.34 O ANISOU 2454 O HOH A 568 2768 2817 1003 597 101 115 O HETATM 2455 O HOH A 569 -9.828 15.019 12.212 0.90 20.51 O ANISOU 2455 O HOH A 569 3493 3016 1285 1634 -456 -70 O HETATM 2456 O HOH A 570 -6.781 -5.178 37.628 0.65 13.03 O ANISOU 2456 O HOH A 570 1322 1937 1690 141 63 420 O HETATM 2457 O HOH A 571 -22.598 1.345 30.315 0.52 11.52 O ANISOU 2457 O HOH A 571 1161 1641 1575 145 211 69 O HETATM 2458 O HOH A 572 -10.637 8.701 7.825 0.75 15.27 O ANISOU 2458 O HOH A 572 1771 2675 1354 -774 310 -514 O HETATM 2459 O HOH A 573 -4.331 -8.307 31.298 0.61 12.05 O ANISOU 2459 O HOH A 573 1102 2273 1203 -116 -165 -419 O HETATM 2460 O HOH A 574 -0.133 1.300 34.682 0.90 17.43 O ANISOU 2460 O HOH A 574 3720 1911 992 -117 166 -225 O HETATM 2461 O HOH A 575 -1.431 -12.839 27.199 0.83 19.27 O ANISOU 2461 O HOH A 575 2563 1977 2781 578 -1698 -144 O HETATM 2462 O HOH A 576 13.055 -5.700 24.571 0.90 18.65 O ANISOU 2462 O HOH A 576 1868 2697 2519 97 -108 632 O HETATM 2463 O HOH A 577 -13.637 20.212 15.146 0.69 13.53 O ANISOU 2463 O HOH A 577 2303 960 1879 55 -723 96 O HETATM 2464 O HOH A 578 -10.557 -19.434 20.061 0.56 12.64 O ANISOU 2464 O HOH A 578 2259 1021 1522 26 193 147 O HETATM 2465 O HOH A 579 -8.052 -19.245 21.830 0.84 19.15 O ANISOU 2465 O HOH A 579 4221 1112 1941 836 1408 200 O HETATM 2466 O HOH A 580 -17.797 20.191 17.603 0.52 14.91 O ANISOU 2466 O HOH A 580 1838 1862 1965 75 -508 245 O HETATM 2467 O HOH A 581 -20.797 8.668 30.093 0.94 20.55 O ANISOU 2467 O HOH A 581 2549 2442 2817 425 1269 -393 O HETATM 2468 O HOH A 582 -7.438 -8.321 -2.205 0.95 17.51 O ANISOU 2468 O HOH A 582 2224 2302 2125 149 252 205 O HETATM 2469 O HOH A 583 -0.999 3.933 13.792 0.82 18.84 O ANISOU 2469 O HOH A 583 1579 1841 3739 -569 -819 1312 O HETATM 2470 O HOH A 584 -11.288 -15.050 34.294 0.47 11.28 O ANISOU 2470 O HOH A 584 1692 1413 1184 413 71 125 O HETATM 2471 O HOH A 585 11.070 1.363 26.051 0.80 18.01 O ANISOU 2471 O HOH A 585 952 3433 2457 320 -8 734 O HETATM 2472 O HOH A 586 -0.842 -8.374 32.789 0.79 17.62 O ANISOU 2472 O HOH A 586 3165 1688 1841 690 549 354 O HETATM 2473 O HOH A 587 -8.828 0.889 -6.447 0.82 18.62 O ANISOU 2473 O HOH A 587 3718 2243 1113 786 103 138 O HETATM 2474 O HOH A 588 -13.091 13.506 31.965 0.78 19.13 O ANISOU 2474 O HOH A 588 2304 2788 2175 -768 851 -911 O HETATM 2475 O HOH A 589 13.825 2.198 22.843 0.61 13.87 O ANISOU 2475 O HOH A 589 891 2531 1846 -408 -313 -170 O HETATM 2476 O HOH A 590 -9.346 6.085 29.196 0.64 12.28 O ANISOU 2476 O HOH A 590 1428 1582 1655 56 -271 -108 O HETATM 2477 O HOH A 591 -4.710 -11.834 32.271 0.81 15.53 O ANISOU 2477 O HOH A 591 2018 2612 1272 110 -355 111 O HETATM 2478 O HOH A 592 0.329 0.978 -6.660 0.82 21.40 O ANISOU 2478 O HOH A 592 4228 1746 2157 238 1091 872 O HETATM 2479 O HOH A 593 -12.855 3.825 -6.757 0.82 20.27 O ANISOU 2479 O HOH A 593 2882 3761 1058 1063 -174 186 O HETATM 2480 O HOH A 594 -24.759 -9.467 2.014 0.76 17.68 O ANISOU 2480 O HOH A 594 1977 2998 1743 -570 -364 -368 O HETATM 2481 O HOH A 595 15.944 3.615 15.609 0.79 18.81 O ANISOU 2481 O HOH A 595 1374 3899 1874 -748 -16 -355 O HETATM 2482 O HOH A 596 4.217 -2.354 29.106 0.85 22.17 O ANISOU 2482 O HOH A 596 3736 2643 2046 -1410 1122 -822 O HETATM 2483 O HOH A 597 -22.240 -18.317 13.674 0.89 17.82 O ANISOU 2483 O HOH A 597 3003 1902 1867 -281 139 -60 O HETATM 2484 O HOH A 598 -15.714 9.157 -2.046 0.86 18.62 O ANISOU 2484 O HOH A 598 2224 2229 2623 240 226 1440 O HETATM 2485 O HOH A 599 -5.695 2.971 13.322 0.78 20.58 O ANISOU 2485 O HOH A 599 1597 1924 4298 -107 -1006 1023 O HETATM 2486 O HOH A 600 -1.416 4.847 -4.823 0.77 17.88 O ANISOU 2486 O HOH A 600 3074 1753 1968 -437 713 418 O HETATM 2487 O HOH A 601 11.380 -6.985 22.631 0.96 21.80 O ANISOU 2487 O HOH A 601 2608 3843 1833 389 -327 544 O HETATM 2488 O HOH A 602 -0.490 14.068 16.248 0.90 18.99 O ANISOU 2488 O HOH A 602 1959 2583 2672 -146 820 276 O HETATM 2489 O HOH A 603 -8.212 7.691 8.468 0.99 21.30 O ANISOU 2489 O HOH A 603 1948 3764 2379 -13 414 22 O HETATM 2490 O HOH A 604 -11.825 10.970 0.914 0.75 18.67 O ANISOU 2490 O HOH A 604 2412 2513 2169 -485 -127 1078 O HETATM 2491 O HOH A 605 -4.216 4.962 6.996 0.62 14.37 O ANISOU 2491 O HOH A 605 2225 1398 1836 101 94 -45 O HETATM 2492 O HOH A 606 -18.305 -3.543 -2.611 0.68 18.52 O ANISOU 2492 O HOH A 606 3080 2513 1444 -712 -777 396 O HETATM 2493 O HOH A 607 -8.723 -15.334 36.903 0.72 17.84 O ANISOU 2493 O HOH A 607 1973 2157 2647 -247 -286 1250 O HETATM 2494 O HOH A 608 2.790 -12.327 18.594 0.82 16.87 O ANISOU 2494 O HOH A 608 2203 2557 1651 881 116 429 O HETATM 2495 O HOH A 609 -24.116 -0.493 26.426 0.53 14.58 O ANISOU 2495 O HOH A 609 1719 2111 1710 -236 -348 -280 O HETATM 2496 O HOH A 610 -18.940 12.382 13.156 0.63 15.30 O ANISOU 2496 O HOH A 610 1495 1798 2521 284 -647 -499 O HETATM 2497 O HOH A 611 -19.020 3.558 -3.448 0.91 24.50 O ANISOU 2497 O HOH A 611 3913 3653 1743 1924 -992 -349 O HETATM 2498 O HOH A 612 -24.324 -3.405 29.693 0.70 15.61 O ANISOU 2498 O HOH A 612 1036 2838 2058 207 -225 -498 O HETATM 2499 O HOH A 613 -7.221 -9.825 -4.642 1.00 22.31 O ANISOU 2499 O HOH A 613 2730 2770 2979 -20 351 -495 O HETATM 2500 O HOH A 614 -17.438 -16.190 22.031 0.76 20.95 O ANISOU 2500 O HOH A 614 2159 2276 3525 -50 1072 926 O HETATM 2501 O HOH A 615 -10.831 5.117 31.116 0.64 17.24 O ANISOU 2501 O HOH A 615 2633 2369 1547 -1083 87 9 O HETATM 2502 O HOH A 616 -23.434 -11.092 17.172 0.87 23.50 O ANISOU 2502 O HOH A 616 1901 4826 2201 -835 -488 461 O HETATM 2503 O HOH A 617 -6.063 16.894 27.611 0.71 20.94 O ANISOU 2503 O HOH A 617 1669 4785 1503 659 67 -904 O HETATM 2504 O HOH A 618 3.627 -2.990 4.405 0.99 22.13 O ANISOU 2504 O HOH A 618 2592 2949 2869 190 -335 -116 O HETATM 2505 O HOH A 619 16.483 -8.842 11.496 0.66 14.67 O ANISOU 2505 O HOH A 619 1192 2424 1958 21 -205 -1 O HETATM 2506 O HOH A 620 -16.972 -13.943 26.322 0.77 17.28 O ANISOU 2506 O HOH A 620 1786 2660 2118 52 83 628 O HETATM 2507 O HOH A 621 1.270 -11.559 25.033 1.00 25.68 O ANISOU 2507 O HOH A 621 4959 2172 2625 1772 -1678 -512 O HETATM 2508 O HOH A 622 -10.555 16.021 29.560 0.64 19.85 O ANISOU 2508 O HOH A 622 3473 1773 2297 -414 1317 -605 O HETATM 2509 O HOH A 623 -25.730 9.687 13.441 0.97 26.86 O ANISOU 2509 O HOH A 623 3023 3231 3952 -80 -1388 604 O HETATM 2510 O HOH A 624 -1.925 -17.365 25.683 0.88 25.83 O ANISOU 2510 O HOH A 624 3194 3206 3412 1478 -760 463 O HETATM 2511 O HOH A 625 -21.237 -19.556 6.733 0.68 17.65 O ANISOU 2511 O HOH A 625 2685 2340 1680 -395 -28 -315 O HETATM 2512 O HOH A 626 9.994 -4.346 -7.846 0.51 14.02 O ANISOU 2512 O HOH A 626 1551 1647 2131 162 64 -153 O HETATM 2513 O HOH A 627 -5.319 7.410 -2.397 0.39 10.68 O ANISOU 2513 O HOH A 627 1255 1490 1315 -135 335 228 O HETATM 2514 O HOH A 628 -16.599 5.433 -7.824 0.73 20.25 O ANISOU 2514 O HOH A 628 1925 2488 3280 688 -956 -11 O HETATM 2515 O HOH A 629 1.291 -16.144 -2.547 0.76 23.96 O ANISOU 2515 O HOH A 629 2067 2768 4267 814 -448 -70 O HETATM 2516 O HOH A 630 -10.823 20.981 25.120 0.44 11.96 O ANISOU 2516 O HOH A 630 1914 1260 1372 -200 -186 -259 O HETATM 2517 O HOH A 631 -5.555 3.725 -5.683 0.98 28.71 O ANISOU 2517 O HOH A 631 3638 3641 3630 8 6 18 O HETATM 2518 O HOH A 632 -23.432 -0.019 32.453 0.69 16.18 O ANISOU 2518 O HOH A 632 1828 2253 2066 370 500 332 O HETATM 2519 O HOH A 633 -1.602 11.734 26.229 0.76 18.31 O ANISOU 2519 O HOH A 633 2062 2837 2056 196 506 -112 O HETATM 2520 O HOH A 634 -23.463 -13.136 11.387 0.62 14.81 O ANISOU 2520 O HOH A 634 1451 2518 1658 -223 -393 325 O HETATM 2521 O HOH A 635 -12.713 12.669 29.310 0.74 24.51 O ANISOU 2521 O HOH A 635 2288 4265 2758 -1505 1339 -2165 O HETATM 2522 O HOH A 636 1.707 12.441 22.884 0.79 20.81 O ANISOU 2522 O HOH A 636 1786 2257 3865 -373 23 -185 O HETATM 2523 O HOH A 637 -14.098 14.502 27.304 0.99 23.66 O ANISOU 2523 O HOH A 637 4093 2692 2205 -802 1569 -834 O HETATM 2524 O HOH A 638 11.644 -0.214 16.177 0.62 14.89 O ANISOU 2524 O HOH A 638 1638 2261 1759 243 -69 29 O HETATM 2525 O HOH A 639 1.330 -6.160 34.578 0.97 23.69 O ANISOU 2525 O HOH A 639 4321 2931 1748 2141 -575 182 O HETATM 2526 O HOH A 640 -12.894 -8.745 -3.150 0.61 16.19 O ANISOU 2526 O HOH A 640 2544 1834 1772 -360 354 -727 O HETATM 2527 O HOH A 641 -2.280 -4.251 -7.031 0.94 22.83 O ANISOU 2527 O HOH A 641 3427 3383 1863 -1208 -656 232 O HETATM 2528 O HOH A 642 14.037 5.740 19.299 0.94 23.17 O ANISOU 2528 O HOH A 642 1902 2550 4352 -562 46 292 O HETATM 2529 O HOH A 643 12.983 -3.741 13.636 0.78 23.05 O ANISOU 2529 O HOH A 643 1591 4842 2324 -600 249 -120 O HETATM 2530 O HOH A 644 -16.697 14.930 33.365 0.75 21.97 O ANISOU 2530 O HOH A 644 4240 2220 1887 -632 396 -326 O HETATM 2531 O HOH A 645 9.385 2.147 12.235 0.89 22.86 O ANISOU 2531 O HOH A 645 2279 2649 3757 -422 1111 -359 O HETATM 2532 O HOH A 646 -28.129 6.429 21.777 0.75 20.39 O ANISOU 2532 O HOH A 646 1204 2939 3606 97 39 355 O HETATM 2533 O HOH A 647 -12.367 16.586 9.169 0.83 28.27 O ANISOU 2533 O HOH A 647 3368 2732 4642 -960 -131 1437 O HETATM 2534 O HOH A 648 -15.494 -10.346 37.336 0.44 17.84 O ANISOU 2534 O HOH A 648 3143 1897 1738 486 1540 371 O HETATM 2535 O AHOH A 649 -4.676 3.518 10.804 0.59 20.26 O ANISOU 2535 O AHOH A 649 2462 2117 3120 349 -1331 -557 O HETATM 2536 O BHOH A 649 -4.059 5.389 9.731 0.41 40.26 O ANISOU 2536 O BHOH A 649 5457 5461 4379 91 -204 180 O HETATM 2537 O HOH A 650 -25.142 4.761 8.563 0.92 25.17 O ANISOU 2537 O HOH A 650 3241 2936 3387 175 -1171 -882 O HETATM 2538 O HOH A 651 4.938 -10.421 13.868 0.65 20.21 O ANISOU 2538 O HOH A 651 2902 1660 3116 72 -1833 -352 O HETATM 2539 O HOH A 652 -25.712 -10.572 17.735 0.66 18.88 O ANISOU 2539 O HOH A 652 2209 1846 3117 -650 -49 32 O HETATM 2540 O HOH A 653 10.090 -2.499 14.037 0.74 21.24 O ANISOU 2540 O HOH A 653 1810 3086 3174 -240 620 236 O HETATM 2541 O HOH A 654 2.825 -13.455 7.960 0.47 12.60 O ANISOU 2541 O HOH A 654 1301 1818 1666 253 -146 -122 O HETATM 2542 O HOH A 655 7.422 -7.636 -0.434 0.96 22.90 O ANISOU 2542 O HOH A 655 1637 3074 3991 483 145 383 O HETATM 2543 O HOH A 656 -7.308 1.652 35.235 0.81 23.71 O ANISOU 2543 O HOH A 656 2419 2891 3698 1154 1243 946 O HETATM 2544 O HOH A 657 -8.507 -17.369 35.044 0.81 21.49 O ANISOU 2544 O HOH A 657 3223 3033 1908 -434 -15 762 O HETATM 2545 O HOH A 658 -16.526 -15.901 32.671 0.70 17.79 O ANISOU 2545 O HOH A 658 1909 2970 1878 6 235 501 O HETATM 2546 O HOH A 659 -5.803 15.438 12.048 0.86 24.83 O ANISOU 2546 O HOH A 659 3944 3960 1529 832 804 1105 O HETATM 2547 O HOH A 660 -5.176 -9.498 33.660 0.75 21.06 O ANISOU 2547 O HOH A 660 2500 2911 2593 808 -552 -165 O HETATM 2548 O HOH A 661 8.605 -4.595 23.759 0.95 26.15 O ANISOU 2548 O HOH A 661 4391 3825 1718 -1391 -650 303 O HETATM 2549 O HOH A 662 -18.044 -11.904 31.569 0.94 23.28 O ANISOU 2549 O HOH A 662 2447 2597 3802 50 -214 820 O HETATM 2550 O HOH A 663 -13.500 -0.582 -6.105 0.85 21.40 O ANISOU 2550 O HOH A 663 2634 2588 2908 562 -921 -494 O HETATM 2551 O HOH A 664 -13.175 -22.101 8.735 0.59 23.74 O ANISOU 2551 O HOH A 664 3035 2568 3417 -774 -1035 354 O HETATM 2552 O HOH A 665 -20.920 -6.850 -1.972 0.83 23.22 O ANISOU 2552 O HOH A 665 3420 2169 3232 -321 -1692 -618 O HETATM 2553 O HOH A 666 3.206 -14.232 12.098 0.58 23.07 O ANISOU 2553 O HOH A 666 2235 2839 3693 1040 595 921 O HETATM 2554 O HOH A 667 -9.066 -2.440 41.084 0.37 17.84 O ANISOU 2554 O HOH A 667 1624 3788 1365 -324 15 1341 O HETATM 2555 O HOH A 668 -11.144 -11.022 -2.773 0.69 21.69 O ANISOU 2555 O HOH A 668 3704 2521 2017 -249 -138 71 O HETATM 2556 O HOH A 669 -25.464 -9.680 15.346 0.92 22.81 O ANISOU 2556 O HOH A 669 3017 2624 3026 -155 705 -4 O HETATM 2557 O HOH A 670 14.629 0.191 15.141 0.87 24.15 O ANISOU 2557 O HOH A 670 3594 3606 1977 1522 1176 943 O HETATM 2558 O HOH A 671 -9.894 6.323 -4.117 0.99 26.14 O ANISOU 2558 O HOH A 671 3356 3605 2972 361 -839 891 O HETATM 2559 O HOH A 672 5.378 9.248 22.212 0.79 22.43 O ANISOU 2559 O HOH A 672 1463 2478 4580 -457 177 -1252 O HETATM 2560 O HOH A 673 -11.175 1.074 33.612 0.47 16.08 O ANISOU 2560 O HOH A 673 1683 3418 1008 53 -33 114 O HETATM 2561 O HOH A 674 -8.188 7.305 27.791 0.47 14.79 O ANISOU 2561 O HOH A 674 1639 1775 2205 403 -496 -806 O HETATM 2562 O HOH A 675 -27.921 4.543 23.979 0.68 20.05 O ANISOU 2562 O HOH A 675 872 3465 3283 -254 128 307 O HETATM 2563 O HOH A 676 -5.398 2.379 37.774 0.57 19.60 O ANISOU 2563 O HOH A 676 1170 2201 4077 196 75 -1729 O HETATM 2564 O HOH A 677 -3.149 -20.439 6.743 0.47 17.06 O ANISOU 2564 O HOH A 677 3050 1432 1999 325 1104 -408 O HETATM 2565 O HOH A 678 -1.517 3.230 -7.237 0.70 23.52 O ANISOU 2565 O HOH A 678 3509 2735 2692 -261 165 644 O HETATM 2566 O HOH A 679 -13.500 -22.368 11.452 0.53 22.14 O ANISOU 2566 O HOH A 679 3251 1879 3282 -1486 -970 792 O HETATM 2567 O HOH A 680 -18.995 17.797 18.838 0.66 21.45 O ANISOU 2567 O HOH A 680 1671 2379 4099 551 -862 -879 O HETATM 2568 O HOH A 681 -16.787 7.615 -3.957 0.65 24.96 O ANISOU 2568 O HOH A 681 3419 3329 2738 -389 417 495 O HETATM 2569 O HOH A 682 -8.361 -19.631 26.514 0.33 12.77 O ANISOU 2569 O HOH A 682 2431 802 1618 317 -70 -398 O HETATM 2570 O HOH A 683 -16.571 -1.222 39.842 0.58 21.52 O ANISOU 2570 O HOH A 683 3046 2999 2131 -846 -818 588 O HETATM 2571 O HOH A 684 -17.763 5.451 -3.463 0.60 19.24 O ANISOU 2571 O HOH A 684 2599 3025 1688 1323 -732 20 O HETATM 2572 O HOH A 685 -8.119 -21.976 10.314 0.84 24.75 O ANISOU 2572 O HOH A 685 3440 1856 4108 277 -750 -1599 O HETATM 2573 O HOH A 686 -7.162 -8.154 -6.908 0.77 21.62 O ANISOU 2573 O HOH A 686 3262 3132 1819 483 52 -483 O HETATM 2574 O HOH A 687 -3.997 -15.399 -2.049 0.74 21.72 O ANISOU 2574 O HOH A 687 3288 2304 2661 -837 579 -465 O HETATM 2575 O HOH A 688 -19.920 -3.891 41.539 0.92 24.82 O ANISOU 2575 O HOH A 688 3167 4840 1424 -12 298 800 O HETATM 2576 O HOH A 689 -28.586 0.137 6.560 0.72 25.48 O ANISOU 2576 O HOH A 689 1842 4194 3646 297 -604 -1112 O HETATM 2577 O HOH A 690 -12.878 -19.423 26.313 0.70 22.24 O ANISOU 2577 O HOH A 690 3476 1315 3660 -53 2029 -60 O HETATM 2578 O HOH A 691 10.494 -8.693 8.816 1.00 28.24 O ANISOU 2578 O HOH A 691 3463 4067 3201 724 847 -179 O HETATM 2579 O HOH A 692 3.499 10.100 24.032 0.82 21.31 O ANISOU 2579 O HOH A 692 1943 2812 3342 -1115 329 -977 O HETATM 2580 O HOH A 693 -23.405 -18.182 6.299 0.72 22.14 O ANISOU 2580 O HOH A 693 3453 2776 2183 -1661 -676 -688 O HETATM 2581 O HOH A 694 -24.801 12.353 6.300 0.70 21.96 O ANISOU 2581 O HOH A 694 3124 2585 2635 245 -394 556 O HETATM 2582 O HOH A 695 6.569 8.494 18.198 0.83 24.55 O ANISOU 2582 O HOH A 695 2818 2887 3625 -1261 -124 527 O HETATM 2583 O HOH A 696 6.962 -3.403 30.266 0.94 28.75 O ANISOU 2583 O HOH A 696 2711 3858 4357 1210 454 -413 O HETATM 2584 O HOH A 697 -18.201 -2.755 45.283 0.72 25.57 O ANISOU 2584 O HOH A 697 3018 4098 2597 862 -360 -1369 O HETATM 2585 O HOH A 698 -22.975 -15.002 16.479 0.80 29.21 O ANISOU 2585 O HOH A 698 3109 4185 3806 621 597 -872 O HETATM 2586 O HOH A 699 12.001 -6.420 8.204 0.65 24.56 O ANISOU 2586 O HOH A 699 3274 3114 2944 963 1579 334 O HETATM 2587 O HOH A 700 2.786 1.239 -2.094 0.61 24.83 O ANISOU 2587 O HOH A 700 2015 4758 2661 -1027 892 -750 O HETATM 2588 O HOH A 701 -13.973 -8.604 -5.268 0.69 25.82 O ANISOU 2588 O HOH A 701 4307 2604 2901 -400 994 -1080 O HETATM 2589 O HOH A 702 -13.529 -16.633 -0.020 0.90 27.57 O ANISOU 2589 O HOH A 702 3521 4185 2770 -328 488 -1661 O HETATM 2590 O HOH A 703 8.421 -11.256 2.663 0.85 24.97 O ANISOU 2590 O HOH A 703 2845 3685 2956 475 335 -1636 O HETATM 2591 O HOH A 704 8.264 -5.621 -10.268 0.95 26.28 O ANISOU 2591 O HOH A 704 3618 3156 3212 620 1049 159 O HETATM 2592 O HOH A 705 -17.248 -13.856 37.916 0.84 24.59 O ANISOU 2592 O HOH A 705 3039 3143 3160 500 661 713 O HETATM 2593 O HOH A 706 -27.147 -1.167 26.107 0.62 22.79 O ANISOU 2593 O HOH A 706 2884 2688 3086 -76 -1266 -106 O HETATM 2594 O HOH A 707 -7.334 0.632 16.566 0.29 13.03 O ANISOU 2594 O HOH A 707 656 3262 1031 -570 -258 313 O HETATM 2595 O HOH A 708 2.048 -14.851 -5.457 0.56 21.43 O ANISOU 2595 O HOH A 708 2472 3023 2648 1353 -519 -1306 O HETATM 2596 O HOH A 709 8.089 3.227 27.975 0.82 24.90 O ANISOU 2596 O HOH A 709 2872 4195 2395 -527 85 353 O HETATM 2597 O HOH A 710 -16.707 -16.054 -4.095 0.85 28.48 O ANISOU 2597 O HOH A 710 3498 3797 3527 -873 -24 -796 O HETATM 2598 O HOH A 711 -10.482 -12.433 40.216 0.48 13.98 O ANISOU 2598 O HOH A 711 1765 2035 1513 -25 151 483 O HETATM 2599 O HOH A 712 0.955 14.754 24.479 0.61 21.81 O ANISOU 2599 O HOH A 712 1274 4396 2616 -717 -297 250 O HETATM 2600 O HOH A 713 -25.554 -1.456 -0.125 0.79 25.83 O ANISOU 2600 O HOH A 713 3204 3754 2857 -943 -648 1292 O HETATM 2601 O HOH A 714 -13.224 -5.287 -5.814 0.60 25.57 O ANISOU 2601 O HOH A 714 2948 4219 2548 -1481 864 -771 O HETATM 2602 O HOH A 715 6.476 -5.467 6.716 1.00 28.47 O ANISOU 2602 O HOH A 715 2943 5301 2572 -403 732 -15 O HETATM 2603 O HOH A 716 -25.915 -3.551 32.132 0.77 27.78 O ANISOU 2603 O HOH A 716 2022 4421 4114 -713 246 -353 O HETATM 2604 O HOH A 717 -4.565 -1.375 38.156 0.36 20.53 O ANISOU 2604 O HOH A 717 2581 3941 1279 764 573 -73 O HETATM 2605 O HOH A 718 4.822 -12.919 4.490 0.69 25.34 O ANISOU 2605 O HOH A 718 1861 2573 5192 740 520 -1117 O HETATM 2606 O HOH A 719 -25.903 -4.934 13.634 0.45 15.40 O ANISOU 2606 O HOH A 719 1262 2301 2288 -30 -229 744 O HETATM 2607 O HOH A 720 -10.679 -5.606 38.462 0.64 22.64 O ANISOU 2607 O HOH A 720 3532 3293 1776 -693 786 -462 O HETATM 2608 O HOH A 721 5.157 -10.676 18.920 1.00 25.32 O ANISOU 2608 O HOH A 721 2503 3911 3204 222 531 -470 O HETATM 2609 O HOH A 722 0.931 3.391 1.800 0.88 29.86 O ANISOU 2609 O HOH A 722 4474 2752 4120 1034 684 376 O HETATM 2610 O HOH A 723 9.221 -9.882 14.232 0.34 22.35 O ANISOU 2610 O HOH A 723 2750 2647 3094 793 966 -680 O HETATM 2611 O HOH A 724 -20.656 13.781 28.949 0.82 29.59 O ANISOU 2611 O HOH A 724 3300 4440 3502 440 1136 -684 O HETATM 2612 O HOH A 725 -22.892 -9.392 25.447 0.51 16.80 O ANISOU 2612 O HOH A 725 1915 3028 1439 -780 -31 175 O HETATM 2613 O HOH A 726 2.638 -8.985 27.465 0.42 23.92 O ANISOU 2613 O HOH A 726 3345 2309 3434 810 -2468 236 O HETATM 2614 O HOH A 727 -4.921 -18.490 23.416 0.86 26.16 O ANISOU 2614 O HOH A 727 3307 3044 3589 42 526 -1476 O HETATM 2615 O HOH A 728 1.665 8.239 28.182 0.74 26.40 O ANISOU 2615 O HOH A 728 3487 2094 4451 -948 -1373 -579 O HETATM 2616 O HOH A 729 -3.177 17.906 14.265 0.77 26.28 O ANISOU 2616 O HOH A 729 4782 1965 3237 219 1863 784 O HETATM 2617 O HOH A 730 -15.165 -15.869 25.155 0.69 23.96 O ANISOU 2617 O HOH A 730 2732 3659 2713 1482 -659 -802 O HETATM 2618 O HOH A 731 -30.033 -11.018 17.866 0.53 24.52 O ANISOU 2618 O HOH A 731 2666 2379 4271 -1246 -1319 43 O HETATM 2619 O HOH A 732 -2.679 6.242 14.055 0.75 27.40 O ANISOU 2619 O HOH A 732 3073 3931 3407 903 -892 -605 O HETATM 2620 O HOH A 733 5.791 -6.004 24.459 0.72 23.23 O ANISOU 2620 O HOH A 733 2548 2436 3843 -604 -23 -152 O HETATM 2621 O HOH A 734 0.222 -10.001 -5.412 0.65 24.92 O ANISOU 2621 O HOH A 734 3051 4410 2010 -298 733 -907 O HETATM 2622 O HOH A 735 -14.423 -21.262 3.249 0.72 31.93 O ANISOU 2622 O HOH A 735 3537 4593 4001 114 979 -1409 O HETATM 2623 O HOH A 736 -5.981 -18.002 3.444 0.70 24.77 O ANISOU 2623 O HOH A 736 3228 3208 2977 1056 -274 202 O HETATM 2624 O HOH A 737 -26.222 6.451 27.159 0.83 26.46 O ANISOU 2624 O HOH A 737 2078 4002 3972 87 -58 -810 O HETATM 2625 O HOH A 738 -27.646 -7.431 26.100 0.74 21.93 O ANISOU 2625 O HOH A 738 2013 3543 2776 -593 707 92 O HETATM 2626 O HOH A 739 -15.977 -11.996 39.462 0.65 25.92 O ANISOU 2626 O HOH A 739 2682 3026 4138 -820 810 79 O HETATM 2627 O HOH A 740 -5.745 -12.177 -5.026 0.85 26.31 O ANISOU 2627 O HOH A 740 3673 3515 2808 546 -174 -634 O HETATM 2628 O HOH A 741 -26.561 -6.621 30.563 0.85 30.23 O ANISOU 2628 O HOH A 741 2182 5658 3644 8 994 1032 O HETATM 2629 O HOH A 742 0.622 -19.189 10.622 0.49 22.71 O ANISOU 2629 O HOH A 742 3001 1962 3666 1223 -1491 -1106 O HETATM 2630 O HOH A 743 12.420 -0.154 12.248 0.96 30.72 O ANISOU 2630 O HOH A 743 3914 4431 3327 -957 761 107 O CONECT 773 2141 CONECT 794 2141 CONECT 971 2141 CONECT 2141 773 794 971 2288 CONECT 2141 2594 CONECT 2142 2143 2144 CONECT 2143 2142 CONECT 2144 2142 2145 2146 CONECT 2145 2144 CONECT 2146 2144 2147 CONECT 2147 2146 CONECT 2288 2141 CONECT 2594 2141 MASTER 246 0 2 9 18 0 4 6 2629 1 13 20 END