diff options
Diffstat (limited to 'plip/test/pdb/1xdn.pdb')
| -rw-r--r-- | plip/test/pdb/1xdn.pdb | 5703 |
1 files changed, 0 insertions, 5703 deletions
diff --git a/plip/test/pdb/1xdn.pdb b/plip/test/pdb/1xdn.pdb deleted file mode 100644 index 0c06611..0000000 --- a/plip/test/pdb/1xdn.pdb +++ /dev/null @@ -1,5703 +0,0 @@ -HEADER LIGASE 07-SEP-04 1XDN -TITLE HIGH RESOLUTION CRYSTAL STRUCTURE OF AN EDITOSOME ENZYME FROM -TITLE 2 TRYPANOSOMA BRUCEI: RNA EDITING LIGASE 1 -COMPND MOL_ID: 1; -COMPND 2 MOLECULE: RNA EDITING LIGASE MP52; -COMPND 3 CHAIN: A; -COMPND 4 FRAGMENT: ADENYLATION DOMAIN; -COMPND 5 ENGINEERED: YES -SOURCE MOL_ID: 1; -SOURCE 2 ORGANISM_SCIENTIFIC: TRYPANOSOMA BRUCEI; -SOURCE 3 ORGANISM_TAXID: 5691; -SOURCE 4 GENE: MP52; -SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; -SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; -SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21GOLD DE3; -SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; -SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PSKB3 -KEYWDS RNA EDITING, LIGASE, TRYPANOSOMA BRUCEI, -EXPDTA X-RAY DIFFRACTION -AUTHOR J.DENG,A.SCHNAUFER,R.SALAVATI,K.D.STUART,W.G.HOL -REVDAT 3 10-SEP-14 1XDN 1 JRNL VERSN -REVDAT 2 24-FEB-09 1XDN 1 VERSN -REVDAT 1 07-DEC-04 1XDN 0 -JRNL AUTH J.DENG,A.SCHNAUFER,R.SALAVATI,K.D.STUART,W.G.HOL -JRNL TITL HIGH RESOLUTION CRYSTAL STRUCTURE OF A KEY EDITOSOME ENZYME -JRNL TITL 2 FROM TRYPANOSOMA BRUCEI: RNA EDITING LIGASE 1. -JRNL REF J.MOL.BIOL. V. 343 601 2004 -JRNL REFN ISSN 0022-2836 -JRNL PMID 15465048 -JRNL DOI 10.1016/J.JMB.2004.08.041 -REMARK 2 -REMARK 2 RESOLUTION. 1.20 ANGSTROMS. -REMARK 3 -REMARK 3 REFINEMENT. -REMARK 3 PROGRAM : REFMAC 5.1.24 -REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON -REMARK 3 -REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD -REMARK 3 -REMARK 3 DATA USED IN REFINEMENT. -REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.20 -REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00 -REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL -REMARK 3 COMPLETENESS FOR RANGE (%) : 98.3 -REMARK 3 NUMBER OF REFLECTIONS : 78835 -REMARK 3 -REMARK 3 FIT TO DATA USED IN REFINEMENT. -REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT -REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM -REMARK 3 R VALUE (WORKING + TEST SET) : 0.129 -REMARK 3 R VALUE (WORKING SET) : 0.128 -REMARK 3 FREE R VALUE : 0.148 -REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 -REMARK 3 FREE R VALUE TEST SET COUNT : 4149 -REMARK 3 -REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. -REMARK 3 TOTAL NUMBER OF BINS USED : 20 -REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.20 -REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.23 -REMARK 3 REFLECTION IN BIN (WORKING SET) : 4798 -REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL -REMARK 3 BIN R VALUE (WORKING SET) : 0.1170 -REMARK 3 BIN FREE R VALUE SET COUNT : 260 -REMARK 3 BIN FREE R VALUE : 0.1310 -REMARK 3 -REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. -REMARK 3 PROTEIN ATOMS : 2119 -REMARK 3 NUCLEIC ACID ATOMS : 0 -REMARK 3 HETEROGEN ATOMS : 32 -REMARK 3 SOLVENT ATOMS : 440 -REMARK 3 -REMARK 3 B VALUES. -REMARK 3 FROM WILSON PLOT (A**2) : 7.29 -REMARK 3 MEAN B VALUE (OVERALL, A**2) : 9.40 -REMARK 3 OVERALL ANISOTROPIC B VALUE. -REMARK 3 B11 (A**2) : -0.22000 -REMARK 3 B22 (A**2) : -0.02000 -REMARK 3 B33 (A**2) : 0.28000 -REMARK 3 B12 (A**2) : 0.00000 -REMARK 3 B13 (A**2) : 0.12000 -REMARK 3 B23 (A**2) : 0.00000 -REMARK 3 -REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. -REMARK 3 ESU BASED ON R VALUE (A): 0.034 -REMARK 3 ESU BASED ON FREE R VALUE (A): 0.033 -REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.017 -REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.349 -REMARK 3 -REMARK 3 CORRELATION COEFFICIENTS. -REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.975 -REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.972 -REMARK 3 -REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT -REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2206 ; 0.010 ; 0.021 -REMARK 3 BOND LENGTHS OTHERS (A): 1976 ; 0.002 ; 0.020 -REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2993 ; 1.420 ; 1.978 -REMARK 3 BOND ANGLES OTHERS (DEGREES): 4606 ; 0.784 ; 3.000 -REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 264 ; 5.763 ; 5.000 -REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL -REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL -REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL -REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 320 ; 0.084 ; 0.200 -REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2428 ; 0.011 ; 0.020 -REMARK 3 GENERAL PLANES OTHERS (A): 457 ; 0.017 ; 0.020 -REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 423 ; 0.220 ; 0.200 -REMARK 3 NON-BONDED CONTACTS OTHERS (A): 2349 ; 0.250 ; 0.200 -REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL -REMARK 3 NON-BONDED TORSION OTHERS (A): 1304 ; 0.084 ; 0.200 -REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 304 ; 0.169 ; 0.200 -REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL -REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL -REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL -REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 11 ; 0.119 ; 0.200 -REMARK 3 SYMMETRY VDW OTHERS (A): 38 ; 0.217 ; 0.200 -REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 36 ; 0.177 ; 0.200 -REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL -REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL -REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL -REMARK 3 -REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT -REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1319 ; 1.192 ; 1.500 -REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL -REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2128 ; 1.915 ; 2.000 -REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL -REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 887 ; 2.829 ; 3.000 -REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL -REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 865 ; 4.258 ; 4.500 -REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL -REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL -REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL -REMARK 3 -REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT -REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL -REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL -REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL -REMARK 3 -REMARK 3 NCS RESTRAINTS STATISTICS -REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL -REMARK 3 -REMARK 3 TLS DETAILS -REMARK 3 NUMBER OF TLS GROUPS : NULL -REMARK 3 -REMARK 3 BULK SOLVENT MODELLING. -REMARK 3 METHOD USED : BABINET MODEL WITH MASK -REMARK 3 PARAMETERS FOR MASK CALCULATION -REMARK 3 VDW PROBE RADIUS : 1.40 -REMARK 3 ION PROBE RADIUS : 0.80 -REMARK 3 SHRINKAGE RADIUS : 0.80 -REMARK 3 -REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING -REMARK 3 POSITIONS -REMARK 4 -REMARK 4 1XDN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 -REMARK 100 -REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-SEP-04. -REMARK 100 THE RCSB ID CODE IS RCSB030242. -REMARK 200 -REMARK 200 EXPERIMENTAL DETAILS -REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION -REMARK 200 DATE OF DATA COLLECTION : 15-DEC-03 -REMARK 200 TEMPERATURE (KELVIN) : 100 -REMARK 200 PH : 7.5 -REMARK 200 NUMBER OF CRYSTALS USED : 1 -REMARK 200 -REMARK 200 SYNCHROTRON (Y/N) : Y -REMARK 200 RADIATION SOURCE : APS -REMARK 200 BEAMLINE : 19-ID -REMARK 200 X-RAY GENERATOR MODEL : NULL -REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M -REMARK 200 WAVELENGTH OR RANGE (A) : 0.97885, 0.97899, 0.96112 -REMARK 200 MONOCHROMATOR : NULL -REMARK 200 OPTICS : NULL -REMARK 200 -REMARK 200 DETECTOR TYPE : CCD -REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4 -REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 -REMARK 200 DATA SCALING SOFTWARE : SCALEPACK -REMARK 200 -REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 95711 -REMARK 200 RESOLUTION RANGE HIGH (A) : 1.100 -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 (%) : 86.8 -REMARK 200 DATA REDUNDANCY : NULL -REMARK 200 R MERGE (I) : 0.06400 -REMARK 200 R SYM (I) : 0.06400 -REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 33.8000 -REMARK 200 -REMARK 200 IN THE HIGHEST RESOLUTION SHELL. -REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.10 -REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL -REMARK 200 COMPLETENESS FOR SHELL (%) : 86.8 -REMARK 200 DATA REDUNDANCY IN SHELL : NULL -REMARK 200 R MERGE FOR SHELL (I) : 0.06400 -REMARK 200 R SYM FOR SHELL (I) : 0.06400 -REMARK 200 <I/SIGMA(I)> FOR SHELL : 33.800 -REMARK 200 -REMARK 200 DIFFRACTION PROTOCOL: MAD -REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD -REMARK 200 SOFTWARE USED: SOLVE -REMARK 200 STARTING MODEL: NULL -REMARK 200 -REMARK 200 REMARK: NULL -REMARK 280 -REMARK 280 CRYSTAL -REMARK 280 SOLVENT CONTENT, VS (%): 45.80 -REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30 -REMARK 280 -REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, MAGNESIUM CHLORIDE, TRIS, -REMARK 280 ATP, PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K -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 29.28950 -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 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 GLY A 48 -REMARK 465 HIS A 49 -REMARK 465 MET A 50 -REMARK 465 ASP A 51 -REMARK 465 LYS A 317 -REMARK 465 HIS A 318 -REMARK 465 PRO A 319 -REMARK 465 GLY A 320 -REMARK 465 LYS A 321 -REMARK 465 GLN A 322 -REMARK 465 LYS A 323 -REMARK 465 GLU A 324 -REMARK 480 -REMARK 480 ZERO OCCUPANCY ATOM -REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO -REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS -REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME; -REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): -REMARK 480 M RES C SSEQI ATOMS -REMARK 480 GLU A 278 CD OE1 OE2 -REMARK 500 -REMARK 500 GEOMETRY AND STEREOCHEMISTRY -REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT -REMARK 500 -REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. -REMARK 500 -REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE -REMARK 500 OE1 GLU A 278 O HOH A 677 2.08 -REMARK 500 -REMARK 500 REMARK: NULL -REMARK 500 -REMARK 500 GEOMETRY AND STEREOCHEMISTRY -REMARK 500 SUBTOPIC: TORSION ANGLES -REMARK 500 -REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: -REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; -REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). -REMARK 500 -REMARK 500 STANDARD TABLE: -REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) -REMARK 500 -REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- -REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 -REMARK 500 -REMARK 500 M RES CSSEQI PSI PHI -REMARK 500 TYR A 165 96.21 -160.96 -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 MG A 502 MG -REMARK 620 N RES CSSEQI ATOM -REMARK 620 1 ATP A 501 O1G -REMARK 620 2 ATP A 501 O2B 86.6 -REMARK 620 3 HOH A 528 O 177.6 94.7 -REMARK 620 4 HOH A 514 O 89.5 173.3 89.4 -REMARK 620 5 HOH A 530 O 90.8 95.6 87.1 89.9 -REMARK 620 6 HOH A 520 O 96.9 90.2 85.1 84.9 170.6 -REMARK 620 N 1 2 3 4 5 -REMARK 800 -REMARK 800 SITE -REMARK 800 SITE_IDENTIFIER: AC1 -REMARK 800 EVIDENCE_CODE: SOFTWARE -REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 502 -REMARK 800 -REMARK 800 SITE_IDENTIFIER: AC2 -REMARK 800 EVIDENCE_CODE: SOFTWARE -REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP A 501 -DBREF 1XDN A 51 324 GB 11067037 AAG27062 51 324 -SEQADV 1XDN GLY A 48 GB 11067037 CLONING ARTIFACT -SEQADV 1XDN HIS A 49 GB 11067037 CLONING ARTIFACT -SEQADV 1XDN MET A 50 GB 11067037 CLONING ARTIFACT -SEQADV 1XDN MSE A 115 GB 11067037 MET 115 MODIFIED RESIDUE -SEQADV 1XDN MSE A 263 GB 11067037 MET 263 MODIFIED RESIDUE -SEQADV 1XDN MSE A 314 GB 11067037 MET 314 MODIFIED RESIDUE -SEQRES 1 A 277 GLY HIS MET ASP GLN SER ASP PHE SER PRO TYR ILE GLU -SEQRES 2 A 277 ILE ASP LEU PRO SER GLU SER ARG ILE GLN SER LEU HIS -SEQRES 3 A 277 LYS SER GLY LEU ALA ALA GLN GLU TRP VAL ALA CYS GLU -SEQRES 4 A 277 LYS VAL HIS GLY THR ASN PHE GLY ILE TYR LEU ILE ASN -SEQRES 5 A 277 GLN GLY ASP HIS GLU VAL VAL ARG PHE ALA LYS ARG SER -SEQRES 6 A 277 GLY ILE MSE ASP PRO ASN GLU ASN PHE PHE GLY TYR HIS -SEQRES 7 A 277 ILE LEU ILE ASP GLU PHE THR ALA GLN ILE ARG ILE LEU -SEQRES 8 A 277 ASN ASP LEU LEU LYS GLN LYS TYR GLY LEU SER ARG VAL -SEQRES 9 A 277 GLY ARG LEU VAL LEU ASN GLY GLU LEU PHE GLY ALA LYS -SEQRES 10 A 277 TYR LYS HIS PRO LEU VAL PRO LYS SER GLU LYS TRP CYS -SEQRES 11 A 277 THR LEU PRO ASN GLY LYS LYS PHE PRO ILE ALA GLY VAL -SEQRES 12 A 277 GLN ILE GLN ARG GLU PRO PHE PRO GLN TYR SER PRO GLU -SEQRES 13 A 277 LEU HIS PHE PHE ALA PHE ASP ILE LYS TYR SER VAL SER -SEQRES 14 A 277 GLY ALA GLU GLU ASP PHE VAL LEU LEU GLY TYR ASP GLU -SEQRES 15 A 277 PHE VAL GLU PHE SER SER LYS VAL PRO ASN LEU LEU TYR -SEQRES 16 A 277 ALA ARG ALA LEU VAL ARG GLY THR LEU ASP GLU CYS LEU -SEQRES 17 A 277 ALA PHE ASP VAL GLU ASN PHE MSE THR PRO LEU PRO ALA -SEQRES 18 A 277 LEU LEU GLY LEU GLY ASN TYR PRO LEU GLU GLY ASN LEU -SEQRES 19 A 277 ALA GLU GLY VAL VAL ILE ARG HIS VAL ARG ARG GLY ASP -SEQRES 20 A 277 PRO ALA VAL GLU LYS HIS ASN VAL SER THR ILE ILE LYS -SEQRES 21 A 277 LEU ARG CYS SER SER PHE MSE GLU LEU LYS HIS PRO GLY -SEQRES 22 A 277 LYS GLN LYS GLU -MODRES 1XDN MSE A 115 MET SELENOMETHIONINE -MODRES 1XDN MSE A 263 MET SELENOMETHIONINE -MODRES 1XDN MSE A 314 MET SELENOMETHIONINE -HET MSE A 115 8 -HET MSE A 263 8 -HET MSE A 314 10 -HET MG A 502 1 -HET ATP A 501 31 -HETNAM MSE SELENOMETHIONINE -HETNAM MG MAGNESIUM ION -HETNAM ATP ADENOSINE-5'-TRIPHOSPHATE -FORMUL 1 MSE 3(C5 H11 N O2 SE) -FORMUL 2 MG MG 2+ -FORMUL 3 ATP C10 H16 N5 O13 P3 -FORMUL 4 HOH *440(H2 O) -HELIX 1 1 SER A 65 SER A 75 1 11 -HELIX 2 2 GLY A 76 GLN A 80 5 5 -HELIX 3 3 GLY A 123 ILE A 126 5 4 -HELIX 4 4 LEU A 127 GLY A 147 1 21 -HELIX 5 5 ALA A 188 VAL A 190 5 3 -HELIX 6 6 ALA A 218 GLU A 220 5 3 -HELIX 7 7 GLY A 226 LYS A 236 1 11 -HELIX 8 8 THR A 250 ALA A 256 1 7 -HELIX 9 9 ASP A 258 PHE A 262 5 5 -HELIX 10 10 PRO A 265 LEU A 270 1 6 -HELIX 11 11 ASP A 294 LYS A 299 1 6 -HELIX 12 12 CYS A 310 LEU A 316 1 7 -SHEET 1 A 4 VAL A 247 GLY A 249 0 -SHEET 2 A 4 TRP A 82 LYS A 87 -1 N TRP A 82 O GLY A 249 -SHEET 3 A 4 GLY A 284 HIS A 289 -1 O VAL A 286 N CYS A 85 -SHEET 4 A 4 ILE A 305 ARG A 309 -1 O ILE A 306 N ILE A 287 -SHEET 1 B 6 GLY A 113 ILE A 114 0 -SHEET 2 B 6 HIS A 103 LYS A 110 -1 N LYS A 110 O GLY A 113 -SHEET 3 B 6 THR A 91 GLN A 100 -1 N GLN A 100 O HIS A 103 -SHEET 4 B 6 ARG A 153 LYS A 164 -1 O LEU A 160 N THR A 91 -SHEET 5 B 6 SER A 201 SER A 214 -1 O LYS A 212 N VAL A 155 -SHEET 6 B 6 PHE A 222 LEU A 224 -1 O VAL A 223 N TYR A 213 -SHEET 1 C 6 GLY A 113 ILE A 114 0 -SHEET 2 C 6 HIS A 103 LYS A 110 -1 N LYS A 110 O GLY A 113 -SHEET 3 C 6 THR A 91 GLN A 100 -1 N GLN A 100 O HIS A 103 -SHEET 4 C 6 ARG A 153 LYS A 164 -1 O LEU A 160 N THR A 91 -SHEET 5 C 6 SER A 201 SER A 214 -1 O LYS A 212 N VAL A 155 -SHEET 6 C 6 LEU A 241 TYR A 242 1 O LEU A 241 N ALA A 208 -SHEET 1 D 2 TRP A 176 THR A 178 0 -SHEET 2 D 2 LYS A 184 PRO A 186 -1 O PHE A 185 N CYS A 177 -LINK C ILE A 114 N MSE A 115 1555 1555 1.33 -LINK C MSE A 115 N ASP A 116 1555 1555 1.33 -LINK C PHE A 262 N MSE A 263 1555 1555 1.33 -LINK C MSE A 263 N THR A 264 1555 1555 1.32 -LINK C PHE A 313 N MSE A 314 1555 1555 1.33 -LINK C MSE A 314 N GLU A 315 1555 1555 1.33 -LINK MG MG A 502 O1G ATP A 501 1555 1555 2.09 -LINK MG MG A 502 O2B ATP A 501 1555 1555 2.06 -LINK MG MG A 502 O HOH A 528 1555 1555 2.13 -LINK MG MG A 502 O HOH A 514 1555 1555 2.07 -LINK MG MG A 502 O HOH A 530 1555 1555 2.04 -LINK MG MG A 502 O HOH A 520 1555 1555 2.11 -CISPEP 1 PHE A 197 PRO A 198 0 -7.28 -SITE 1 AC1 5 ATP A 501 HOH A 514 HOH A 520 HOH A 528 -SITE 2 AC1 5 HOH A 530 -SITE 1 AC2 27 TYR A 58 ILE A 59 GLU A 60 ILE A 61 -SITE 2 AC2 27 GLU A 86 LYS A 87 VAL A 88 ASN A 92 -SITE 3 AC2 27 ARG A 111 GLU A 159 PHE A 209 VAL A 286 -SITE 4 AC2 27 LYS A 307 ARG A 309 MG A 502 HOH A 514 -SITE 5 AC2 27 HOH A 520 HOH A 528 HOH A 530 HOH A 536 -SITE 6 AC2 27 HOH A 587 HOH A 634 HOH A 650 HOH A 777 -SITE 7 AC2 27 HOH A 829 HOH A 871 HOH A 886 -CRYST1 44.911 58.579 52.984 90.00 100.23 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 0.022266 0.000000 0.004018 0.00000 -SCALE2 0.000000 0.017071 0.000000 0.00000 -SCALE3 0.000000 0.000000 0.019179 0.00000 -ATOM 1 N GLN A 52 42.237 16.800 35.823 1.00 12.04 N -ANISOU 1 N GLN A 52 1764 1519 1290 -51 85 8 N -ATOM 2 CA GLN A 52 41.667 17.015 34.477 1.00 10.21 C -ANISOU 2 CA GLN A 52 1684 1030 1163 45 63 174 C -ATOM 3 C GLN A 52 40.148 17.010 34.446 1.00 10.33 C -ANISOU 3 C GLN A 52 1788 1017 1117 104 129 163 C -ATOM 4 O GLN A 52 39.564 17.006 33.382 1.00 9.88 O -ANISOU 4 O GLN A 52 1826 876 1049 292 181 182 O -ATOM 5 CB GLN A 52 42.228 15.967 33.522 1.00 9.36 C -ANISOU 5 CB GLN A 52 1554 833 1170 72 15 146 C -ATOM 6 CG GLN A 52 43.734 16.095 33.352 1.00 9.40 C -ANISOU 6 CG GLN A 52 1581 771 1218 86 -200 237 C -ATOM 7 CD GLN A 52 44.170 17.346 32.622 1.00 8.47 C -ANISOU 7 CD GLN A 52 1399 689 1130 22 -142 158 C -ATOM 8 OE1 GLN A 52 45.312 17.791 32.785 1.00 12.47 O -ANISOU 8 OE1 GLN A 52 1745 1079 1911 -88 -491 288 O -ATOM 9 NE2 GLN A 52 43.296 17.915 31.849 1.00 8.79 N -ANISOU 9 NE2 GLN A 52 1234 1041 1063 15 -69 506 N -ATOM 10 N SER A 53 39.488 17.025 35.604 1.00 11.01 N -ANISOU 10 N SER A 53 1803 1212 1166 179 187 226 N -ATOM 11 CA SER A 53 38.026 16.949 35.611 1.00 12.75 C -ANISOU 11 CA SER A 53 1863 1569 1413 117 173 171 C -ATOM 12 C SER A 53 37.340 18.091 34.862 1.00 12.38 C -ANISOU 12 C SER A 53 1797 1573 1333 176 171 119 C -ATOM 13 O SER A 53 36.209 17.937 34.426 1.00 14.69 O -ANISOU 13 O SER A 53 2013 1898 1670 142 240 202 O -ATOM 14 CB SER A 53 37.462 16.890 37.026 1.00 13.59 C -ANISOU 14 CB SER A 53 1919 1711 1532 147 222 282 C -ATOM 15 OG SER A 53 37.854 18.006 37.781 1.00 17.90 O -ANISOU 15 OG SER A 53 2616 2299 1887 226 311 383 O -ATOM 16 N ASP A 54 38.012 19.228 34.730 1.00 11.65 N -ANISOU 16 N ASP A 54 1724 1454 1246 264 152 134 N -ATOM 17 CA ASP A 54 37.455 20.341 33.968 1.00 11.85 C -ANISOU 17 CA ASP A 54 1767 1455 1278 249 117 178 C -ATOM 18 C ASP A 54 37.742 20.271 32.474 1.00 10.23 C -ANISOU 18 C ASP A 54 1562 1275 1050 292 187 237 C -ATOM 19 O ASP A 54 37.168 21.045 31.722 1.00 11.10 O -ANISOU 19 O ASP A 54 1719 1326 1173 448 195 446 O -ATOM 20 CB ASP A 54 37.947 21.667 34.531 1.00 13.04 C -ANISOU 20 CB ASP A 54 1995 1543 1413 294 64 201 C -ATOM 21 CG ASP A 54 37.464 21.907 35.937 1.00 16.08 C -ANISOU 21 CG ASP A 54 2341 1811 1956 415 -6 115 C -ATOM 22 OD1 ASP A 54 36.280 21.638 36.211 1.00 19.99 O -ANISOU 22 OD1 ASP A 54 3244 2206 2145 740 396 -50 O -ATOM 23 OD2 ASP A 54 38.207 22.360 36.811 1.00 21.76 O -ANISOU 23 OD2 ASP A 54 3388 2268 2612 735 2 -249 O -ATOM 24 N PHE A 55 38.617 19.367 32.044 1.00 9.13 N -ANISOU 24 N PHE A 55 1451 1102 915 233 164 264 N -ATOM 25 CA PHE A 55 38.972 19.219 30.642 1.00 8.35 C -ANISOU 25 CA PHE A 55 1276 990 906 119 108 255 C -ATOM 26 C PHE A 55 37.915 18.485 29.848 1.00 8.87 C -ANISOU 26 C PHE A 55 1313 994 1061 61 120 286 C -ATOM 27 O PHE A 55 37.392 17.475 30.303 1.00 10.67 O -ANISOU 27 O PHE A 55 1623 1170 1260 -158 142 415 O -ATOM 28 CB PHE A 55 40.300 18.470 30.543 1.00 8.52 C -ANISOU 28 CB PHE A 55 1252 1126 858 129 47 237 C -ATOM 29 CG PHE A 55 40.730 18.127 29.138 1.00 7.26 C -ANISOU 29 CG PHE A 55 1080 883 793 155 55 228 C -ATOM 30 CD1 PHE A 55 41.050 19.110 28.229 1.00 7.47 C -ANISOU 30 CD1 PHE A 55 1050 928 859 -63 -52 233 C -ATOM 31 CD2 PHE A 55 40.847 16.803 28.753 1.00 8.45 C -ANISOU 31 CD2 PHE A 55 1262 862 1085 80 -70 130 C -ATOM 32 CE1 PHE A 55 41.470 18.763 26.957 1.00 8.40 C -ANISOU 32 CE1 PHE A 55 1229 1056 906 -61 20 249 C -ATOM 33 CE2 PHE A 55 41.266 16.455 27.495 1.00 8.90 C -ANISOU 33 CE2 PHE A 55 1324 977 1079 50 -63 -24 C -ATOM 34 CZ PHE A 55 41.584 17.426 26.589 1.00 9.37 C -ANISOU 34 CZ PHE A 55 1038 1362 1158 -23 -149 95 C -ATOM 35 N SER A 56 37.615 18.984 28.653 1.00 8.47 N -ANISOU 35 N SER A 56 1233 979 1006 32 116 228 N -ATOM 36 CA SER A 56 36.702 18.341 27.727 1.00 8.75 C -ANISOU 36 CA SER A 56 1231 1019 1072 38 57 197 C -ATOM 37 C SER A 56 37.409 18.135 26.390 1.00 8.22 C -ANISOU 37 C SER A 56 1168 944 1009 47 69 195 C -ATOM 38 O SER A 56 37.676 19.116 25.681 1.00 8.56 O -ANISOU 38 O SER A 56 1332 879 1041 91 107 301 O -ATOM 39 CB SER A 56 35.476 19.231 27.540 1.00 9.47 C -ANISOU 39 CB SER A 56 1297 1149 1149 85 42 121 C -ATOM 40 OG SER A 56 34.454 18.554 26.839 1.00 11.56 O -ANISOU 40 OG SER A 56 1305 1468 1617 -23 -67 121 O -ATOM 41 N PRO A 57 37.729 16.888 26.033 1.00 8.33 N -ANISOU 41 N PRO A 57 1272 890 1002 32 116 228 N -ATOM 42 CA PRO A 57 38.409 16.649 24.754 1.00 8.76 C -ANISOU 42 CA PRO A 57 1200 1016 1111 46 70 126 C -ATOM 43 C PRO A 57 37.622 17.191 23.585 1.00 8.53 C -ANISOU 43 C PRO A 57 1115 1087 1037 -2 90 120 C -ATOM 44 O PRO A 57 36.400 17.105 23.551 1.00 10.15 O -ANISOU 44 O PRO A 57 1192 1471 1192 -149 81 282 O -ATOM 45 CB PRO A 57 38.525 15.124 24.677 1.00 9.69 C -ANISOU 45 CB PRO A 57 1335 1102 1242 80 109 130 C -ATOM 46 CG PRO A 57 38.403 14.640 26.059 1.00 11.00 C -ANISOU 46 CG PRO A 57 1529 1180 1471 -88 159 137 C -ATOM 47 CD PRO A 57 37.508 15.628 26.772 1.00 9.30 C -ANISOU 47 CD PRO A 57 1414 924 1193 -51 111 240 C -ATOM 48 N TYR A 58 38.339 17.747 22.619 1.00 7.67 N -ANISOU 48 N TYR A 58 1033 891 988 31 36 154 N -ATOM 49 CA TYR A 58 37.722 18.174 21.383 1.00 8.58 C -ANISOU 49 CA TYR A 58 1188 996 1074 55 -4 48 C -ATOM 50 C TYR A 58 37.720 16.916 20.539 1.00 10.08 C -ANISOU 50 C TYR A 58 1394 1110 1326 65 -88 72 C -ATOM 51 O TYR A 58 37.954 15.802 21.051 1.00 12.68 O -ANISOU 51 O TYR A 58 1913 1264 1641 93 -65 79 O -ATOM 52 CB TYR A 58 38.459 19.389 20.783 1.00 7.74 C -ANISOU 52 CB TYR A 58 1048 922 971 4 19 108 C -ATOM 53 CG TYR A 58 37.649 20.058 19.693 1.00 7.14 C -ANISOU 53 CG TYR A 58 861 917 932 -6 51 201 C -ATOM 54 CD1 TYR A 58 36.490 20.749 19.989 1.00 7.63 C -ANISOU 54 CD1 TYR A 58 917 1131 849 48 144 55 C -ATOM 55 CD2 TYR A 58 38.011 19.951 18.354 1.00 7.35 C -ANISOU 55 CD2 TYR A 58 888 932 972 137 181 246 C -ATOM 56 CE1 TYR A 58 35.725 21.321 18.986 1.00 6.97 C -ANISOU 56 CE1 TYR A 58 857 814 975 105 84 107 C -ATOM 57 CE2 TYR A 58 37.237 20.520 17.348 1.00 7.25 C -ANISOU 57 CE2 TYR A 58 889 973 892 200 133 157 C -ATOM 58 CZ TYR A 58 36.095 21.188 17.671 1.00 6.13 C -ANISOU 58 CZ TYR A 58 822 864 641 39 -21 125 C -ATOM 59 OH TYR A 58 35.360 21.745 16.658 1.00 7.63 O -ANISOU 59 OH TYR A 58 905 1039 954 192 126 112 O -ATOM 60 N ILE A 59 37.333 17.049 19.295 1.00 12.35 N -ANISOU 60 N ILE A 59 1858 1391 1442 67 -54 19 N -ATOM 61 CA ILE A 59 37.115 15.901 18.448 1.00 12.48 C -ANISOU 61 CA ILE A 59 1815 1511 1414 -18 3 -5 C -ATOM 62 C ILE A 59 38.089 15.820 17.302 1.00 11.76 C -ANISOU 62 C ILE A 59 1818 1340 1310 -112 39 106 C -ATOM 63 O ILE A 59 38.750 16.803 16.917 1.00 13.39 O -ANISOU 63 O ILE A 59 2188 1365 1534 -381 75 175 O -ATOM 64 CB ILE A 59 35.694 15.926 17.889 1.00 13.52 C -ANISOU 64 CB ILE A 59 1835 1762 1541 -39 108 14 C -ATOM 65 CG1 ILE A 59 35.445 17.222 17.112 1.00 15.44 C -ANISOU 65 CG1 ILE A 59 1949 2069 1846 73 0 -114 C -ATOM 66 CG2 ILE A 59 34.704 15.759 19.016 1.00 15.64 C -ANISOU 66 CG2 ILE A 59 2034 2173 1734 -60 181 -9 C -ATOM 67 CD1 ILE A 59 34.256 17.154 16.212 1.00 17.64 C -ANISOU 67 CD1 ILE A 59 2133 2466 2102 160 -11 -39 C -ATOM 68 N GLU A 60 38.180 14.611 16.777 1.00 10.67 N -ANISOU 68 N GLU A 60 1639 1280 1133 -23 -37 88 N -ATOM 69 CA GLU A 60 38.661 14.409 15.428 1.00 10.55 C -ANISOU 69 CA GLU A 60 1532 1315 1163 56 -49 68 C -ATOM 70 C GLU A 60 37.481 14.459 14.452 1.00 8.69 C -ANISOU 70 C GLU A 60 1216 1143 942 52 12 -16 C -ATOM 71 O GLU A 60 36.332 14.278 14.839 1.00 10.07 O -ANISOU 71 O GLU A 60 1502 1442 879 -96 30 -26 O -ATOM 72 CB GLU A 60 39.495 13.129 15.350 1.00 12.80 C -ANISOU 72 CB GLU A 60 1738 1695 1428 183 12 58 C -ATOM 73 CG GLU A 60 40.798 13.316 16.137 1.00 17.70 C -ANISOU 73 CG GLU A 60 2231 2365 2126 151 23 142 C -ATOM 74 CD GLU A 60 41.613 12.057 16.350 1.00 21.64 C -ANISOU 74 CD GLU A 60 2708 3021 2493 302 -110 170 C -ATOM 75 OE1 GLU A 60 41.570 11.155 15.484 1.00 23.57 O -ANISOU 75 OE1 GLU A 60 3086 2940 2929 615 207 -9 O -ATOM 76 OE2 GLU A 60 42.308 11.976 17.395 1.00 25.13 O -ANISOU 76 OE2 GLU A 60 3159 3620 2769 347 -86 501 O -ATOM 77 N ILE A 61 37.793 14.733 13.206 1.00 6.90 N -ANISOU 77 N ILE A 61 935 872 813 2 -41 -38 N -ATOM 78 CA ILE A 61 36.779 14.950 12.200 1.00 7.13 C -ANISOU 78 CA ILE A 61 905 956 846 47 -10 -79 C -ATOM 79 C ILE A 61 37.084 14.056 11.030 1.00 7.33 C -ANISOU 79 C ILE A 61 914 895 976 45 11 -111 C -ATOM 80 O ILE A 61 38.219 13.998 10.572 1.00 8.79 O -ANISOU 80 O ILE A 61 909 1355 1074 35 25 -277 O -ATOM 81 CB ILE A 61 36.757 16.443 11.793 1.00 6.83 C -ANISOU 81 CB ILE A 61 872 907 815 11 2 -39 C -ATOM 82 CG1 ILE A 61 36.419 17.333 12.993 1.00 6.74 C -ANISOU 82 CG1 ILE A 61 894 785 881 -42 -61 65 C -ATOM 83 CG2 ILE A 61 35.749 16.663 10.695 1.00 6.97 C -ANISOU 83 CG2 ILE A 61 825 1030 791 13 -1 -137 C -ATOM 84 CD1 ILE A 61 36.548 18.813 12.744 1.00 7.60 C -ANISOU 84 CD1 ILE A 61 801 979 1105 37 -192 19 C -ATOM 85 N ASP A 62 36.066 13.372 10.530 1.00 6.96 N -ANISOU 85 N ASP A 62 879 847 917 63 -2 -113 N -ATOM 86 CA ASP A 62 36.254 12.425 9.448 1.00 7.34 C -ANISOU 86 CA ASP A 62 1021 854 911 87 -4 -129 C -ATOM 87 C ASP A 62 36.040 13.011 8.060 1.00 6.96 C -ANISOU 87 C ASP A 62 928 814 901 54 -13 -187 C -ATOM 88 O ASP A 62 35.232 13.916 7.872 1.00 6.52 O -ANISOU 88 O ASP A 62 908 660 910 138 9 -84 O -ATOM 89 CB ASP A 62 35.294 11.244 9.583 1.00 8.39 C -ANISOU 89 CB ASP A 62 1213 924 1048 72 -53 -65 C -ATOM 90 CG ASP A 62 35.411 10.521 10.881 1.00 11.97 C -ANISOU 90 CG ASP A 62 1683 1327 1535 27 30 -2 C -ATOM 91 OD1 ASP A 62 36.506 10.494 11.474 1.00 15.65 O -ANISOU 91 OD1 ASP A 62 2210 1886 1848 225 -149 466 O -ATOM 92 OD2 ASP A 62 34.418 9.952 11.370 1.00 17.75 O -ANISOU 92 OD2 ASP A 62 2414 2056 2271 -23 11 498 O -ATOM 93 N LEU A 63 36.758 12.454 7.084 1.00 6.71 N -ANISOU 93 N LEU A 63 874 717 956 136 -25 -252 N -ATOM 94 CA LEU A 63 36.396 12.571 5.682 1.00 6.81 C -ANISOU 94 CA LEU A 63 904 778 905 69 43 -222 C -ATOM 95 C LEU A 63 35.017 11.951 5.504 1.00 7.10 C -ANISOU 95 C LEU A 63 931 775 990 53 -5 -271 C -ATOM 96 O LEU A 63 34.647 11.040 6.252 1.00 7.91 O -ANISOU 96 O LEU A 63 1014 903 1085 -4 -28 -172 O -ATOM 97 CB LEU A 63 37.396 11.824 4.813 1.00 7.22 C -ANISOU 97 CB LEU A 63 943 739 1059 109 54 -290 C -ATOM 98 CG LEU A 63 38.828 12.357 4.856 1.00 7.73 C -ANISOU 98 CG LEU A 63 976 923 1038 116 32 -262 C -ATOM 99 CD1 LEU A 63 39.771 11.385 4.148 1.00 8.36 C -ANISOU 99 CD1 LEU A 63 942 1034 1198 124 181 -250 C -ATOM 100 CD2 LEU A 63 38.933 13.737 4.253 1.00 8.58 C -ANISOU 100 CD2 LEU A 63 1048 1104 1109 136 157 -380 C -ATOM 101 N PRO A 64 34.242 12.400 4.526 1.00 7.30 N -ANISOU 101 N PRO A 64 878 898 996 37 15 -243 N -ATOM 102 CA PRO A 64 32.886 11.862 4.349 1.00 7.38 C -ANISOU 102 CA PRO A 64 910 874 1018 0 44 -191 C -ATOM 103 C PRO A 64 32.877 10.416 3.868 1.00 7.74 C -ANISOU 103 C PRO A 64 968 851 1122 11 81 -205 C -ATOM 104 O PRO A 64 33.404 10.094 2.797 1.00 8.70 O -ANISOU 104 O PRO A 64 1187 984 1135 -21 85 -296 O -ATOM 105 CB PRO A 64 32.270 12.793 3.299 1.00 8.12 C -ANISOU 105 CB PRO A 64 1011 975 1099 38 3 -211 C -ATOM 106 CG PRO A 64 33.462 13.342 2.535 1.00 7.13 C -ANISOU 106 CG PRO A 64 901 882 923 108 -19 -170 C -ATOM 107 CD PRO A 64 34.540 13.481 3.572 1.00 7.55 C -ANISOU 107 CD PRO A 64 975 909 984 19 39 -240 C -ATOM 108 N SER A 65 32.257 9.546 4.658 1.00 8.35 N -ANISOU 108 N SER A 65 1040 960 1170 -13 147 -170 N -ATOM 109 CA SER A 65 32.130 8.131 4.315 1.00 8.84 C -ANISOU 109 CA SER A 65 1063 976 1317 41 117 -168 C -ATOM 110 C SER A 65 30.817 7.862 3.590 1.00 8.60 C -ANISOU 110 C SER A 65 1095 888 1282 56 135 -174 C -ATOM 111 O SER A 65 29.878 8.664 3.639 1.00 8.27 O -ANISOU 111 O SER A 65 1084 748 1309 52 143 -317 O -ATOM 112 CB SER A 65 32.191 7.250 5.568 1.00 9.54 C -ANISOU 112 CB SER A 65 1118 1109 1394 36 100 -117 C -ATOM 113 OG SER A 65 31.018 7.423 6.342 1.00 10.43 O -ANISOU 113 OG SER A 65 1032 1304 1625 177 169 -41 O -ATOM 114 N GLU A 66 30.748 6.713 2.924 1.00 9.13 N -ANISOU 114 N GLU A 66 1150 896 1421 100 219 -236 N -ATOM 115 CA GLU A 66 29.508 6.316 2.271 1.00 10.14 C -ANISOU 115 CA GLU A 66 1322 1114 1416 20 180 -273 C -ATOM 116 C GLU A 66 28.356 6.255 3.260 1.00 9.39 C -ANISOU 116 C GLU A 66 1243 968 1354 -10 174 -287 C -ATOM 117 O GLU A 66 27.277 6.760 2.981 1.00 9.78 O -ANISOU 117 O GLU A 66 1233 1039 1443 -76 161 -393 O -ATOM 118 CB GLU A 66 29.642 4.957 1.552 1.00 11.33 C -ANISOU 118 CB GLU A 66 1516 1287 1500 47 250 -342 C -ATOM 119 CG GLU A 66 28.306 4.414 1.019 1.00 15.93 C -ANISOU 119 CG GLU A 66 2181 1857 2012 -25 131 -304 C -ATOM 120 CD GLU A 66 28.433 3.123 0.242 1.00 20.49 C -ANISOU 120 CD GLU A 66 2698 2536 2548 23 78 -291 C -ATOM 121 OE1 GLU A 66 28.933 2.141 0.821 1.00 23.61 O -ANISOU 121 OE1 GLU A 66 3389 2405 3173 62 213 -304 O -ATOM 122 OE2 GLU A 66 28.019 3.089 -0.939 1.00 25.25 O -ANISOU 122 OE2 GLU A 66 3394 3150 3050 -68 119 -533 O -ATOM 123 N SER A 67 28.585 5.632 4.407 1.00 9.14 N -ANISOU 123 N SER A 67 1199 902 1370 32 172 -273 N -ATOM 124 CA SER A 67 27.500 5.447 5.369 1.00 10.01 C -ANISOU 124 CA SER A 67 1291 1065 1444 45 173 -145 C -ATOM 125 C SER A 67 27.067 6.771 5.976 1.00 8.81 C -ANISOU 125 C SER A 67 1186 902 1256 79 189 -212 C -ATOM 126 O SER A 67 25.882 6.991 6.211 1.00 9.60 O -ANISOU 126 O SER A 67 1155 969 1524 19 204 -237 O -ATOM 127 CB SER A 67 27.874 4.458 6.473 1.00 11.61 C -ANISOU 127 CB SER A 67 1512 1255 1643 68 210 -99 C -ATOM 128 OG SER A 67 28.977 4.872 7.232 1.00 14.26 O -ANISOU 128 OG SER A 67 1889 1507 2023 157 282 -11 O -ATOM 129 N ARG A 68 28.017 7.667 6.221 1.00 8.58 N -ANISOU 129 N ARG A 68 1052 960 1244 56 157 -229 N -ATOM 130 CA ARG A 68 27.693 8.974 6.785 1.00 8.32 C -ANISOU 130 CA ARG A 68 1039 947 1175 48 105 -202 C -ATOM 131 C ARG A 68 26.824 9.757 5.813 1.00 8.01 C -ANISOU 131 C ARG A 68 1022 890 1132 28 105 -216 C -ATOM 132 O ARG A 68 25.796 10.325 6.203 1.00 7.98 O -ANISOU 132 O ARG A 68 872 844 1316 15 198 -303 O -ATOM 133 CB ARG A 68 28.955 9.785 7.107 1.00 8.65 C -ANISOU 133 CB ARG A 68 1069 1018 1196 81 30 -168 C -ATOM 134 CG ARG A 68 28.649 11.128 7.782 1.00 8.97 C -ANISOU 134 CG ARG A 68 1110 907 1392 50 -97 -146 C -ATOM 135 CD ARG A 68 28.366 10.995 9.266 1.00 9.86 C -ANISOU 135 CD ARG A 68 1105 1188 1452 -60 226 -276 C -ATOM 136 NE ARG A 68 29.617 10.789 9.969 1.00 9.23 N -ANISOU 136 NE ARG A 68 1213 1036 1255 -109 225 -175 N -ATOM 137 CZ ARG A 68 30.474 11.757 10.265 1.00 8.88 C -ANISOU 137 CZ ARG A 68 1105 1141 1126 -174 125 -158 C -ATOM 138 NH1 ARG A 68 30.148 13.034 10.076 1.00 9.14 N -ANISOU 138 NH1 ARG A 68 1127 1073 1272 -131 62 -183 N -ATOM 139 NH2 ARG A 68 31.642 11.441 10.803 1.00 9.93 N -ANISOU 139 NH2 ARG A 68 1215 1068 1488 -27 36 -227 N -ATOM 140 N ILE A 69 27.229 9.824 4.555 1.00 7.72 N -ANISOU 140 N ILE A 69 885 910 1135 4 115 -207 N -ATOM 141 CA ILE A 69 26.494 10.586 3.566 1.00 7.90 C -ANISOU 141 CA ILE A 69 959 925 1115 37 72 -232 C -ATOM 142 C ILE A 69 25.093 10.004 3.380 1.00 8.35 C -ANISOU 142 C ILE A 69 1007 994 1170 19 23 -233 C -ATOM 143 O ILE A 69 24.116 10.740 3.335 1.00 8.77 O -ANISOU 143 O ILE A 69 989 1068 1272 37 -30 -256 O -ATOM 144 CB ILE A 69 27.280 10.669 2.238 1.00 8.29 C -ANISOU 144 CB ILE A 69 1035 986 1127 77 115 -182 C -ATOM 145 CG1 ILE A 69 28.568 11.485 2.415 1.00 8.01 C -ANISOU 145 CG1 ILE A 69 952 904 1187 184 213 -180 C -ATOM 146 CG2 ILE A 69 26.414 11.244 1.119 1.00 9.03 C -ANISOU 146 CG2 ILE A 69 1110 1183 1137 45 155 -331 C -ATOM 147 CD1 ILE A 69 28.371 12.938 2.863 1.00 8.71 C -ANISOU 147 CD1 ILE A 69 1037 1033 1238 55 266 -114 C -ATOM 148 N GLN A 70 24.978 8.687 3.301 1.00 9.03 N -ANISOU 148 N GLN A 70 1023 1088 1319 -11 57 -267 N -ATOM 149 CA GLN A 70 23.663 8.065 3.154 1.00 9.97 C -ANISOU 149 CA GLN A 70 1134 1229 1422 -84 36 -257 C -ATOM 150 C GLN A 70 22.760 8.408 4.337 1.00 9.86 C -ANISOU 150 C GLN A 70 1054 1190 1500 -57 46 -275 C -ATOM 151 O GLN A 70 21.590 8.713 4.159 1.00 10.39 O -ANISOU 151 O GLN A 70 953 1295 1697 -79 -36 -383 O -ATOM 152 CB GLN A 70 23.802 6.548 3.000 1.00 11.39 C -ANISOU 152 CB GLN A 70 1280 1362 1685 -84 87 -323 C -ATOM 153 CG GLN A 70 24.345 6.122 1.634 1.00 15.15 C -ANISOU 153 CG GLN A 70 1770 1919 2066 -29 81 -381 C -ATOM 154 CD GLN A 70 24.586 4.613 1.506 1.00 19.50 C -ANISOU 154 CD GLN A 70 2491 2463 2452 25 124 -470 C -ATOM 155 OE1 GLN A 70 24.649 4.085 0.390 1.00 25.55 O -ANISOU 155 OE1 GLN A 70 3245 3184 3279 -6 196 -531 O -ATOM 156 NE2 GLN A 70 24.751 3.927 2.639 1.00 21.99 N -ANISOU 156 NE2 GLN A 70 2791 2398 3164 107 233 -469 N -ATOM 157 N SER A 71 23.313 8.370 5.539 1.00 9.16 N -ANISOU 157 N SER A 71 1011 1038 1428 -29 128 -209 N -ATOM 158 CA SER A 71 22.538 8.672 6.737 1.00 9.41 C -ANISOU 158 CA SER A 71 1085 1087 1401 -121 143 -168 C -ATOM 159 C SER A 71 22.139 10.142 6.811 1.00 8.82 C -ANISOU 159 C SER A 71 972 1048 1328 -68 153 -190 C -ATOM 160 O SER A 71 21.038 10.469 7.249 1.00 9.42 O -ANISOU 160 O SER A 71 864 1183 1533 -135 238 -254 O -ATOM 161 CB SER A 71 23.330 8.303 7.980 1.00 10.04 C -ANISOU 161 CB SER A 71 1320 1116 1378 -43 252 -113 C -ATOM 162 OG SER A 71 23.470 6.912 8.117 1.00 14.22 O -ANISOU 162 OG SER A 71 1888 1464 2049 -85 255 -11 O -ATOM 163 N LEU A 72 23.025 11.035 6.393 1.00 7.98 N -ANISOU 163 N LEU A 72 853 960 1218 -38 152 -203 N -ATOM 164 CA LEU A 72 22.700 12.454 6.385 1.00 7.91 C -ANISOU 164 CA LEU A 72 876 981 1146 13 111 -173 C -ATOM 165 C LEU A 72 21.559 12.750 5.425 1.00 8.47 C -ANISOU 165 C LEU A 72 940 1035 1241 20 65 -209 C -ATOM 166 O LEU A 72 20.677 13.537 5.738 1.00 9.08 O -ANISOU 166 O LEU A 72 859 1217 1372 134 55 -196 O -ATOM 167 CB LEU A 72 23.937 13.291 6.066 1.00 7.31 C -ANISOU 167 CB LEU A 72 877 883 1017 -7 164 -205 C -ATOM 168 CG LEU A 72 24.961 13.356 7.203 1.00 7.27 C -ANISOU 168 CG LEU A 72 782 970 1010 81 147 -122 C -ATOM 169 CD1 LEU A 72 26.247 13.996 6.730 1.00 7.32 C -ANISOU 169 CD1 LEU A 72 919 833 1030 -2 79 -179 C -ATOM 170 CD2 LEU A 72 24.421 14.102 8.419 1.00 7.53 C -ANISOU 170 CD2 LEU A 72 963 910 985 26 119 -72 C -ATOM 171 N HIS A 73 21.531 12.080 4.287 1.00 9.11 N -ANISOU 171 N HIS A 73 936 1192 1333 26 18 -163 N -ATOM 172 CA HIS A 73 20.392 12.239 3.387 1.00 10.66 C -ANISOU 172 CA HIS A 73 1139 1424 1487 -5 -56 -122 C -ATOM 173 C HIS A 73 19.112 11.631 3.938 1.00 11.06 C -ANISOU 173 C HIS A 73 1124 1461 1617 -29 -60 -150 C -ATOM 174 O HIS A 73 18.081 12.290 3.955 1.00 11.72 O -ANISOU 174 O HIS A 73 1038 1612 1801 16 -126 -182 O -ATOM 175 CB HIS A 73 20.711 11.686 2.016 1.00 11.39 C -ANISOU 175 CB HIS A 73 1278 1573 1474 15 -116 -152 C -ATOM 176 CG HIS A 73 21.579 12.598 1.224 1.00 12.21 C -ANISOU 176 CG HIS A 73 1297 1759 1583 83 -91 -101 C -ATOM 177 ND1 HIS A 73 21.077 13.656 0.500 1.00 15.54 N -ANISOU 177 ND1 HIS A 73 1835 2168 1901 71 -88 36 N -ATOM 178 CD2 HIS A 73 22.925 12.688 1.132 1.00 15.34 C -ANISOU 178 CD2 HIS A 73 1519 2398 1910 175 72 141 C -ATOM 179 CE1 HIS A 73 22.073 14.308 -0.072 1.00 15.27 C -ANISOU 179 CE1 HIS A 73 1888 2106 1807 10 -22 14 C -ATOM 180 NE2 HIS A 73 23.205 13.744 0.302 1.00 16.00 N -ANISOU 180 NE2 HIS A 73 1822 2420 1836 84 45 153 N -ATOM 181 N LYS A 74 19.190 10.402 4.427 1.00 11.31 N -ANISOU 181 N LYS A 74 1086 1464 1744 -141 37 -145 N -ATOM 182 CA LYS A 74 17.993 9.689 4.878 1.00 12.24 C -ANISOU 182 CA LYS A 74 1281 1570 1798 -131 34 -130 C -ATOM 183 C LYS A 74 17.318 10.385 6.052 1.00 11.98 C -ANISOU 183 C LYS A 74 1172 1529 1848 -100 83 -160 C -ATOM 184 O LYS A 74 16.084 10.418 6.144 1.00 13.11 O -ANISOU 184 O LYS A 74 1020 1757 2203 -117 191 -314 O -ATOM 185 CB LYS A 74 18.335 8.242 5.246 1.00 12.91 C -ANISOU 185 CB LYS A 74 1394 1611 1897 -128 80 -145 C -ATOM 186 CG LYS A 74 17.127 7.395 5.620 1.00 17.37 C -ANISOU 186 CG LYS A 74 2012 2135 2451 -95 49 -125 C -ATOM 187 CD LYS A 74 16.113 7.287 4.476 1.00 22.78 C -ANISOU 187 CD LYS A 74 2845 2894 2915 -59 13 -2 C -ATOM 188 CE LYS A 74 15.121 6.149 4.706 1.00 25.42 C -ANISOU 188 CE LYS A 74 3239 3197 3222 -16 -12 -16 C -ATOM 189 NZ LYS A 74 14.309 5.856 3.497 1.00 28.28 N -ANISOU 189 NZ LYS A 74 3542 3603 3599 90 -46 -41 N -ATOM 190 N SER A 75 18.123 10.938 6.951 1.00 11.07 N -ANISOU 190 N SER A 75 1081 1438 1684 -70 112 -125 N -ATOM 191 CA SER A 75 17.621 11.627 8.128 1.00 11.13 C -ANISOU 191 CA SER A 75 1189 1414 1626 -39 151 -80 C -ATOM 192 C SER A 75 16.975 12.967 7.807 1.00 10.90 C -ANISOU 192 C SER A 75 1076 1392 1673 -5 105 -108 C -ATOM 193 O SER A 75 16.318 13.538 8.663 1.00 12.48 O -ANISOU 193 O SER A 75 1197 1598 1946 39 338 -156 O -ATOM 194 CB SER A 75 18.750 11.878 9.116 1.00 11.16 C -ANISOU 194 CB SER A 75 1209 1384 1648 -4 177 -128 C -ATOM 195 OG SER A 75 19.719 12.744 8.551 1.00 10.33 O -ANISOU 195 OG SER A 75 905 1328 1690 -29 182 -231 O -ATOM 196 N GLY A 76 17.193 13.497 6.610 1.00 10.13 N -ANISOU 196 N GLY A 76 972 1323 1554 -52 19 -131 N -ATOM 197 CA GLY A 76 16.750 14.833 6.275 1.00 10.10 C -ANISOU 197 CA GLY A 76 1028 1288 1520 -39 -5 -61 C -ATOM 198 C GLY A 76 17.766 15.916 6.584 1.00 9.05 C -ANISOU 198 C GLY A 76 888 1173 1375 28 -63 -43 C -ATOM 199 O GLY A 76 17.565 17.064 6.193 1.00 10.10 O -ANISOU 199 O GLY A 76 853 1280 1704 0 -135 -27 O -ATOM 200 N LEU A 77 18.864 15.570 7.261 1.00 8.52 N -ANISOU 200 N LEU A 77 816 1084 1337 3 31 -14 N -ATOM 201 CA LEU A 77 19.818 16.590 7.668 1.00 8.03 C -ANISOU 201 CA LEU A 77 840 1095 1114 -46 -15 -25 C -ATOM 202 C LEU A 77 20.554 17.221 6.488 1.00 7.21 C -ANISOU 202 C LEU A 77 685 1031 1022 39 -18 -62 C -ATOM 203 O LEU A 77 20.877 18.401 6.541 1.00 7.89 O -ANISOU 203 O LEU A 77 765 1107 1124 -38 -36 -9 O -ATOM 204 CB LEU A 77 20.815 16.020 8.660 1.00 8.06 C -ANISOU 204 CB LEU A 77 843 1116 1101 -58 -1 2 C -ATOM 205 CG LEU A 77 20.235 15.696 10.031 1.00 9.09 C -ANISOU 205 CG LEU A 77 935 1227 1289 -72 86 -57 C -ATOM 206 CD1 LEU A 77 21.234 14.940 10.837 1.00 10.45 C -ANISOU 206 CD1 LEU A 77 1064 1530 1375 -90 -37 175 C -ATOM 207 CD2 LEU A 77 19.791 16.934 10.762 1.00 11.72 C -ANISOU 207 CD2 LEU A 77 1549 1543 1360 -101 164 -19 C -ATOM 208 N ALA A 78 20.808 16.462 5.424 1.00 7.83 N -ANISOU 208 N ALA A 78 817 1066 1090 -6 -12 -88 N -ATOM 209 CA ALA A 78 21.581 16.968 4.295 1.00 8.47 C -ANISOU 209 CA ALA A 78 916 1187 1113 -6 -13 -75 C -ATOM 210 C ALA A 78 20.884 18.141 3.614 1.00 8.53 C -ANISOU 210 C ALA A 78 876 1196 1167 -54 -61 -41 C -ATOM 211 O ALA A 78 21.533 19.032 3.088 1.00 9.36 O -ANISOU 211 O ALA A 78 961 1353 1239 45 -147 73 O -ATOM 212 CB ALA A 78 21.839 15.872 3.289 1.00 9.03 C -ANISOU 212 CB ALA A 78 1073 1185 1173 -42 50 -92 C -ATOM 213 N ALA A 79 19.550 18.145 3.630 1.00 9.47 N -ANISOU 213 N ALA A 79 963 1316 1318 13 -138 -8 N -ATOM 214 CA ALA A 79 18.752 19.184 2.970 1.00 10.09 C -ANISOU 214 CA ALA A 79 1107 1387 1338 12 -181 -27 C -ATOM 215 C ALA A 79 18.653 20.471 3.783 1.00 9.92 C -ANISOU 215 C ALA A 79 1024 1407 1337 97 -207 -8 C -ATOM 216 O ALA A 79 18.143 21.473 3.292 1.00 11.33 O -ANISOU 216 O ALA A 79 1244 1529 1528 239 -471 -36 O -ATOM 217 CB ALA A 79 17.360 18.646 2.708 1.00 10.82 C -ANISOU 217 CB ALA A 79 1159 1487 1465 3 -228 -80 C -ATOM 218 N GLN A 80 19.116 20.441 5.033 1.00 9.26 N -ANISOU 218 N GLN A 80 919 1321 1277 88 -152 -99 N -ATOM 219 CA GLN A 80 19.085 21.596 5.919 1.00 9.29 C -ANISOU 219 CA GLN A 80 932 1331 1265 96 -60 -96 C -ATOM 220 C GLN A 80 20.326 22.465 5.664 1.00 9.11 C -ANISOU 220 C GLN A 80 898 1340 1223 144 -36 -101 C -ATOM 221 O GLN A 80 20.956 22.333 4.625 1.00 9.99 O -ANISOU 221 O GLN A 80 1023 1631 1142 8 -77 -160 O -ATOM 222 CB GLN A 80 18.933 21.118 7.359 1.00 9.29 C -ANISOU 222 CB GLN A 80 872 1338 1316 124 -29 -168 C -ATOM 223 CG GLN A 80 17.629 20.324 7.551 1.00 10.26 C -ANISOU 223 CG GLN A 80 959 1496 1443 62 -53 -93 C -ATOM 224 CD GLN A 80 17.451 19.716 8.934 1.00 12.16 C -ANISOU 224 CD GLN A 80 827 2060 1732 -70 -84 -122 C -ATOM 225 OE1 GLN A 80 18.187 20.005 9.855 1.00 12.95 O -ANISOU 225 OE1 GLN A 80 904 2186 1830 -402 -133 92 O -ATOM 226 NE2 GLN A 80 16.436 18.870 9.074 1.00 15.56 N -ANISOU 226 NE2 GLN A 80 1320 2324 2268 -571 -11 -295 N -ATOM 227 N GLU A 81 20.643 23.377 6.573 1.00 8.73 N -ANISOU 227 N GLU A 81 874 1267 1176 127 -36 -73 N -ATOM 228 CA GLU A 81 21.690 24.368 6.333 1.00 8.29 C -ANISOU 228 CA GLU A 81 841 1119 1188 179 -72 -5 C -ATOM 229 C GLU A 81 23.011 23.942 6.965 1.00 6.84 C -ANISOU 229 C GLU A 81 727 896 975 150 -41 -38 C -ATOM 230 O GLU A 81 23.063 23.575 8.143 1.00 6.87 O -ANISOU 230 O GLU A 81 651 964 996 109 1 -78 O -ATOM 231 CB GLU A 81 21.292 25.723 6.915 1.00 9.67 C -ANISOU 231 CB GLU A 81 961 1236 1475 198 -21 7 C -ATOM 232 CG GLU A 81 20.281 26.580 6.168 1.00 13.76 C -ANISOU 232 CG GLU A 81 1438 1782 2008 177 -116 14 C -ATOM 233 CD GLU A 81 20.492 28.042 6.545 1.00 16.85 C -ANISOU 233 CD GLU A 81 2287 1915 2198 278 -58 70 C -ATOM 234 OE1 GLU A 81 21.004 28.826 5.719 1.00 18.18 O -ANISOU 234 OE1 GLU A 81 2294 1824 2790 334 -325 -34 O -ATOM 235 OE2 GLU A 81 20.210 28.388 7.713 1.00 19.24 O -ANISOU 235 OE2 GLU A 81 2620 2215 2476 52 -256 -91 O -ATOM 236 N TRP A 82 24.055 24.069 6.162 1.00 6.78 N -ANISOU 236 N TRP A 82 760 921 893 135 -52 39 N -ATOM 237 CA TRP A 82 25.428 23.727 6.498 1.00 5.64 C -ANISOU 237 CA TRP A 82 657 743 740 114 -92 -8 C -ATOM 238 C TRP A 82 26.323 24.892 6.106 1.00 5.61 C -ANISOU 238 C TRP A 82 721 677 732 96 -87 -28 C -ATOM 239 O TRP A 82 25.987 25.707 5.245 1.00 6.42 O -ANISOU 239 O TRP A 82 772 824 842 91 -149 24 O -ATOM 240 CB TRP A 82 25.861 22.476 5.715 1.00 6.41 C -ANISOU 240 CB TRP A 82 760 795 880 74 -36 0 C -ATOM 241 CG TRP A 82 25.084 21.243 6.054 1.00 6.10 C -ANISOU 241 CG TRP A 82 720 664 931 55 -87 -108 C -ATOM 242 CD1 TRP A 82 23.780 20.996 5.757 1.00 6.25 C -ANISOU 242 CD1 TRP A 82 618 758 997 116 -177 -159 C -ATOM 243 CD2 TRP A 82 25.558 20.090 6.748 1.00 5.81 C -ANISOU 243 CD2 TRP A 82 585 740 881 33 -113 -165 C -ATOM 244 NE1 TRP A 82 23.407 19.771 6.247 1.00 6.29 N -ANISOU 244 NE1 TRP A 82 616 689 1084 -16 -157 -119 N -ATOM 245 CE2 TRP A 82 24.477 19.195 6.865 1.00 6.66 C -ANISOU 245 CE2 TRP A 82 806 715 1006 15 -42 -191 C -ATOM 246 CE3 TRP A 82 26.794 19.722 7.294 1.00 6.08 C -ANISOU 246 CE3 TRP A 82 786 598 925 -41 -13 -162 C -ATOM 247 CZ2 TRP A 82 24.599 17.961 7.483 1.00 7.04 C -ANISOU 247 CZ2 TRP A 82 707 836 1132 -38 -14 -173 C -ATOM 248 CZ3 TRP A 82 26.914 18.497 7.903 1.00 6.38 C -ANISOU 248 CZ3 TRP A 82 818 792 813 61 -142 -89 C -ATOM 249 CH2 TRP A 82 25.832 17.632 7.997 1.00 7.28 C -ANISOU 249 CH2 TRP A 82 945 799 1020 -11 -83 -149 C -ATOM 250 N VAL A 83 27.495 24.938 6.725 1.00 5.50 N -ANISOU 250 N VAL A 83 665 673 749 66 -65 13 N -ATOM 251 CA VAL A 83 28.558 25.853 6.334 1.00 5.35 C -ANISOU 251 CA VAL A 83 696 631 705 69 -79 -53 C -ATOM 252 C VAL A 83 29.852 25.080 6.127 1.00 5.46 C -ANISOU 252 C VAL A 83 716 650 706 92 -81 8 C -ATOM 253 O VAL A 83 30.092 24.049 6.745 1.00 6.18 O -ANISOU 253 O VAL A 83 768 727 852 93 43 117 O -ATOM 254 CB VAL A 83 28.792 26.978 7.383 1.00 5.76 C -ANISOU 254 CB VAL A 83 735 662 788 58 -39 -95 C -ATOM 255 CG1 VAL A 83 27.590 27.932 7.390 1.00 6.61 C -ANISOU 255 CG1 VAL A 83 941 773 794 79 -39 -135 C -ATOM 256 CG2 VAL A 83 29.071 26.406 8.787 1.00 6.54 C -ANISOU 256 CG2 VAL A 83 887 818 780 69 -36 -168 C -ATOM 257 N ALA A 84 30.707 25.624 5.272 1.00 5.43 N -ANISOU 257 N ALA A 84 692 683 687 65 -39 45 N -ATOM 258 CA ALA A 84 32.110 25.240 5.201 1.00 5.06 C -ANISOU 258 CA ALA A 84 614 693 615 92 -26 35 C -ATOM 259 C ALA A 84 32.946 26.392 5.715 1.00 5.11 C -ANISOU 259 C ALA A 84 646 588 705 138 35 21 C -ATOM 260 O ALA A 84 32.764 27.514 5.253 1.00 5.97 O -ANISOU 260 O ALA A 84 801 619 845 87 -127 82 O -ATOM 261 CB ALA A 84 32.527 24.920 3.791 1.00 6.31 C -ANISOU 261 CB ALA A 84 880 760 757 73 0 -17 C -ATOM 262 N CYS A 85 33.852 26.124 6.654 1.00 4.78 N -ANISOU 262 N CYS A 85 661 567 587 84 -13 -15 N -ATOM 263 CA CYS A 85 34.795 27.114 7.154 1.00 4.73 C -ANISOU 263 CA CYS A 85 631 587 578 63 76 12 C -ATOM 264 C CYS A 85 36.205 26.576 6.987 1.00 4.63 C -ANISOU 264 C CYS A 85 641 575 542 51 33 -21 C -ATOM 265 O CYS A 85 36.421 25.390 6.800 1.00 4.76 O -ANISOU 265 O CYS A 85 673 498 637 81 83 -13 O -ATOM 266 CB CYS A 85 34.535 27.427 8.627 1.00 5.52 C -ANISOU 266 CB CYS A 85 751 705 641 81 115 -47 C -ATOM 267 SG CYS A 85 32.869 28.017 9.012 1.00 7.11 S -ANISOU 267 SG CYS A 85 893 934 871 225 141 -45 S -ATOM 268 N GLU A 86 37.190 27.455 7.078 1.00 4.62 N -ANISOU 268 N GLU A 86 605 473 676 15 22 -20 N -ATOM 269 CA GLU A 86 38.571 27.044 6.878 1.00 4.45 C -ANISOU 269 CA GLU A 86 630 558 502 -11 35 36 C -ATOM 270 C GLU A 86 39.020 26.076 7.969 1.00 4.37 C -ANISOU 270 C GLU A 86 609 540 511 -6 46 11 C -ATOM 271 O GLU A 86 38.754 26.297 9.154 1.00 4.85 O -ANISOU 271 O GLU A 86 800 565 476 61 36 21 O -ATOM 272 CB GLU A 86 39.465 28.281 6.845 1.00 5.19 C -ANISOU 272 CB GLU A 86 731 632 606 -46 22 85 C -ATOM 273 CG GLU A 86 40.931 27.959 6.607 1.00 4.98 C -ANISOU 273 CG GLU A 86 687 627 578 -139 48 -4 C -ATOM 274 CD GLU A 86 41.812 29.159 6.344 1.00 6.64 C -ANISOU 274 CD GLU A 86 815 736 971 -14 -16 2 C -ATOM 275 OE1 GLU A 86 41.342 30.314 6.471 1.00 7.94 O -ANISOU 275 OE1 GLU A 86 992 736 1286 -127 99 42 O -ATOM 276 OE2 GLU A 86 43.012 28.933 6.041 1.00 6.62 O -ANISOU 276 OE2 GLU A 86 802 752 959 -115 84 134 O -ATOM 277 N LYS A 87 39.723 25.026 7.552 1.00 3.83 N -ANISOU 277 N LYS A 87 601 433 419 67 40 -9 N -ATOM 278 CA LYS A 87 40.425 24.140 8.472 1.00 3.94 C -ANISOU 278 CA LYS A 87 568 448 478 18 44 8 C -ATOM 279 C LYS A 87 41.850 24.659 8.607 1.00 3.95 C -ANISOU 279 C LYS A 87 554 466 479 23 86 -50 C -ATOM 280 O LYS A 87 42.583 24.714 7.619 1.00 4.64 O -ANISOU 280 O LYS A 87 637 663 460 -4 107 -168 O -ATOM 281 CB LYS A 87 40.406 22.700 7.983 1.00 4.21 C -ANISOU 281 CB LYS A 87 503 526 571 -14 -38 17 C -ATOM 282 CG LYS A 87 40.812 21.716 9.060 1.00 4.82 C -ANISOU 282 CG LYS A 87 656 466 707 53 35 -35 C -ATOM 283 CD LYS A 87 40.599 20.285 8.636 1.00 5.64 C -ANISOU 283 CD LYS A 87 798 543 801 87 -121 -54 C -ATOM 284 CE LYS A 87 40.745 19.292 9.788 1.00 6.04 C -ANISOU 284 CE LYS A 87 1018 427 849 -43 -53 -93 C -ATOM 285 NZ LYS A 87 42.137 19.250 10.300 1.00 6.11 N -ANISOU 285 NZ LYS A 87 888 654 777 170 -43 52 N -ATOM 286 N VAL A 88 42.191 25.106 9.813 1.00 4.11 N -ANISOU 286 N VAL A 88 507 540 514 -46 71 -40 N -ATOM 287 CA VAL A 88 43.484 25.722 10.086 1.00 4.45 C -ANISOU 287 CA VAL A 88 580 547 560 -10 47 -50 C -ATOM 288 C VAL A 88 44.463 24.675 10.618 1.00 3.93 C -ANISOU 288 C VAL A 88 483 537 472 -80 75 -27 C -ATOM 289 O VAL A 88 44.131 23.888 11.506 1.00 4.74 O -ANISOU 289 O VAL A 88 592 592 614 -58 57 6 O -ATOM 290 CB VAL A 88 43.302 26.914 11.068 1.00 4.47 C -ANISOU 290 CB VAL A 88 578 576 542 12 82 -79 C -ATOM 291 CG1 VAL A 88 44.644 27.493 11.514 1.00 5.48 C -ANISOU 291 CG1 VAL A 88 725 675 681 -4 -7 -89 C -ATOM 292 CG2 VAL A 88 42.459 27.975 10.373 1.00 5.25 C -ANISOU 292 CG2 VAL A 88 749 608 637 -15 99 -120 C -ATOM 293 N HIS A 89 45.670 24.687 10.054 1.00 4.36 N -ANISOU 293 N HIS A 89 571 532 553 -29 8 -8 N -ATOM 294 CA HIS A 89 46.730 23.760 10.416 1.00 4.44 C -ANISOU 294 CA HIS A 89 528 573 584 46 59 -93 C -ATOM 295 C HIS A 89 47.626 24.352 11.490 1.00 4.47 C -ANISOU 295 C HIS A 89 555 534 610 36 19 -110 C -ATOM 296 O HIS A 89 48.645 24.992 11.200 1.00 5.45 O -ANISOU 296 O HIS A 89 578 818 674 -134 60 -59 O -ATOM 297 CB HIS A 89 47.539 23.442 9.194 1.00 5.39 C -ANISOU 297 CB HIS A 89 625 734 686 7 -29 -72 C -ATOM 298 CG HIS A 89 48.572 22.385 9.383 1.00 5.84 C -ANISOU 298 CG HIS A 89 683 822 713 77 153 -58 C -ATOM 299 ND1 HIS A 89 48.273 21.121 9.793 1.00 7.90 N -ANISOU 299 ND1 HIS A 89 803 944 1254 199 139 20 N -ATOM 300 CD2 HIS A 89 49.912 22.427 9.275 1.00 9.92 C -ANISOU 300 CD2 HIS A 89 910 824 2033 33 230 73 C -ATOM 301 CE1 HIS A 89 49.367 20.386 9.781 1.00 7.28 C -ANISOU 301 CE1 HIS A 89 772 763 1230 171 290 -8 C -ATOM 302 NE2 HIS A 89 50.363 21.139 9.389 1.00 7.99 N -ANISOU 302 NE2 HIS A 89 863 1003 1169 162 -39 -133 N -ATOM 303 N GLY A 90 47.212 24.171 12.734 1.00 4.84 N -ANISOU 303 N GLY A 90 553 636 650 -38 69 -75 N -ATOM 304 CA GLY A 90 47.977 24.569 13.905 1.00 4.82 C -ANISOU 304 CA GLY A 90 618 568 643 42 67 -55 C -ATOM 305 C GLY A 90 47.968 23.416 14.884 1.00 4.31 C -ANISOU 305 C GLY A 90 547 528 562 8 57 -34 C -ATOM 306 O GLY A 90 48.231 22.268 14.522 1.00 5.30 O -ANISOU 306 O GLY A 90 757 559 695 113 100 -108 O -ATOM 307 N THR A 91 47.650 23.727 16.133 1.00 4.47 N -ANISOU 307 N THR A 91 599 533 564 44 29 -13 N -ATOM 308 CA THR A 91 47.488 22.698 17.144 1.00 5.08 C -ANISOU 308 CA THR A 91 728 552 648 84 71 14 C -ATOM 309 C THR A 91 46.227 23.006 17.947 1.00 4.89 C -ANISOU 309 C THR A 91 691 446 720 54 65 39 C -ATOM 310 O THR A 91 45.848 24.161 18.123 1.00 4.88 O -ANISOU 310 O THR A 91 709 436 707 85 41 53 O -ATOM 311 CB THR A 91 48.776 22.587 17.981 1.00 5.80 C -ANISOU 311 CB THR A 91 754 752 696 103 64 87 C -ATOM 312 OG1 THR A 91 48.738 21.401 18.776 1.00 7.22 O -ANISOU 312 OG1 THR A 91 846 1011 885 136 13 332 O -ATOM 313 CG2 THR A 91 48.947 23.756 18.929 1.00 7.35 C -ANISOU 313 CG2 THR A 91 954 1070 768 148 -66 42 C -ATOM 314 N ASN A 92 45.560 21.960 18.391 1.00 4.91 N -ANISOU 314 N ASN A 92 734 470 662 72 86 -18 N -ATOM 315 CA ASN A 92 44.301 22.113 19.093 1.00 5.14 C -ANISOU 315 CA ASN A 92 700 552 700 56 55 -2 C -ATOM 316 C ASN A 92 44.489 22.853 20.414 1.00 4.84 C -ANISOU 316 C ASN A 92 678 526 635 127 40 52 C -ATOM 317 O ASN A 92 45.438 22.578 21.157 1.00 5.79 O -ANISOU 317 O ASN A 92 832 654 714 211 7 -103 O -ATOM 318 CB ASN A 92 43.702 20.727 19.353 1.00 5.44 C -ANISOU 318 CB ASN A 92 772 533 761 0 5 -12 C -ATOM 319 CG ASN A 92 42.298 20.794 19.874 1.00 6.04 C -ANISOU 319 CG ASN A 92 868 686 738 -32 120 -38 C -ATOM 320 OD1 ASN A 92 42.067 20.782 21.077 1.00 9.32 O -ANISOU 320 OD1 ASN A 92 946 1827 766 -149 64 -114 O -ATOM 321 ND2 ASN A 92 41.350 20.907 18.972 1.00 6.71 N -ANISOU 321 ND2 ASN A 92 808 944 796 -44 -40 39 N -ATOM 322 N PHE A 93 43.585 23.765 20.710 1.00 5.58 N -ANISOU 322 N PHE A 93 811 681 628 196 -43 -54 N -ATOM 323 CA PHE A 93 43.744 24.595 21.888 1.00 6.28 C -ANISOU 323 CA PHE A 93 963 834 588 201 -12 6 C -ATOM 324 C PHE A 93 42.372 24.872 22.491 1.00 6.64 C -ANISOU 324 C PHE A 93 916 1054 553 354 -124 -30 C -ATOM 325 O PHE A 93 41.336 24.938 21.797 1.00 11.84 O -ANISOU 325 O PHE A 93 1389 2306 801 800 -6 -159 O -ATOM 326 CB PHE A 93 44.514 25.854 21.484 1.00 6.74 C -ANISOU 326 CB PHE A 93 1181 717 662 181 14 60 C -ATOM 327 CG PHE A 93 45.044 26.656 22.642 1.00 6.65 C -ANISOU 327 CG PHE A 93 1039 811 674 144 -33 107 C -ATOM 328 CD1 PHE A 93 46.235 26.319 23.260 1.00 8.52 C -ANISOU 328 CD1 PHE A 93 1077 981 1177 179 61 127 C -ATOM 329 CD2 PHE A 93 44.360 27.767 23.113 1.00 6.80 C -ANISOU 329 CD2 PHE A 93 1017 848 718 58 -75 -100 C -ATOM 330 CE1 PHE A 93 46.720 27.067 24.325 1.00 9.10 C -ANISOU 330 CE1 PHE A 93 986 1179 1293 -19 -240 428 C -ATOM 331 CE2 PHE A 93 44.847 28.519 24.178 1.00 8.18 C -ANISOU 331 CE2 PHE A 93 1112 990 1005 -40 -108 -19 C -ATOM 332 CZ PHE A 93 46.031 28.162 24.776 1.00 8.89 C -ANISOU 332 CZ PHE A 93 1195 1203 977 -71 -209 59 C -ATOM 333 N GLY A 94 42.300 24.959 23.791 1.00 5.27 N -ANISOU 333 N GLY A 94 761 787 454 128 -38 -5 N -ATOM 334 CA GLY A 94 41.063 25.306 24.447 1.00 5.53 C -ANISOU 334 CA GLY A 94 839 735 525 136 54 -41 C -ATOM 335 C GLY A 94 41.307 26.336 25.528 1.00 5.32 C -ANISOU 335 C GLY A 94 832 726 463 157 -4 27 C -ATOM 336 O GLY A 94 42.275 26.237 26.289 1.00 6.37 O -ANISOU 336 O GLY A 94 1012 887 520 314 -108 -22 O -ATOM 337 N ILE A 95 40.417 27.313 25.600 1.00 5.38 N -ANISOU 337 N ILE A 95 831 743 470 215 -16 -45 N -ATOM 338 CA ILE A 95 40.413 28.316 26.652 1.00 5.67 C -ANISOU 338 CA ILE A 95 878 759 514 144 -31 -49 C -ATOM 339 C ILE A 95 39.185 28.061 27.513 1.00 6.00 C -ANISOU 339 C ILE A 95 908 870 501 185 32 -118 C -ATOM 340 O ILE A 95 38.057 28.034 27.030 1.00 6.51 O -ANISOU 340 O ILE A 95 971 982 520 142 57 -87 O -ATOM 341 CB ILE A 95 40.343 29.725 26.042 1.00 6.28 C -ANISOU 341 CB ILE A 95 912 740 734 156 -36 -83 C -ATOM 342 CG1 ILE A 95 41.534 29.973 25.112 1.00 7.15 C -ANISOU 342 CG1 ILE A 95 1059 887 768 105 -5 -58 C -ATOM 343 CG2 ILE A 95 40.270 30.771 27.132 1.00 7.90 C -ANISOU 343 CG2 ILE A 95 1078 921 1003 146 51 -35 C -ATOM 344 CD1 ILE A 95 41.367 31.118 24.145 1.00 8.23 C -ANISOU 344 CD1 ILE A 95 1155 1027 945 -26 -29 -41 C -ATOM 345 N TYR A 96 39.433 27.859 28.798 1.00 6.44 N -ANISOU 345 N TYR A 96 1054 884 506 73 7 -16 N -ATOM 346 CA TYR A 96 38.417 27.482 29.757 1.00 7.18 C -ANISOU 346 CA TYR A 96 1004 1052 671 95 9 -50 C -ATOM 347 C TYR A 96 38.202 28.577 30.791 1.00 7.54 C -ANISOU 347 C TYR A 96 1138 1140 585 126 -20 -59 C -ATOM 348 O TYR A 96 39.158 29.130 31.312 1.00 8.77 O -ANISOU 348 O TYR A 96 1302 1394 634 165 23 -220 O -ATOM 349 CB TYR A 96 38.872 26.235 30.517 1.00 7.82 C -ANISOU 349 CB TYR A 96 1133 1156 682 61 108 38 C -ATOM 350 CG TYR A 96 38.843 24.964 29.703 1.00 7.38 C -ANISOU 350 CG TYR A 96 1219 939 644 169 31 143 C -ATOM 351 CD1 TYR A 96 37.934 23.971 29.993 1.00 7.62 C -ANISOU 351 CD1 TYR A 96 1216 947 730 268 123 105 C -ATOM 352 CD2 TYR A 96 39.720 24.749 28.639 1.00 7.58 C -ANISOU 352 CD2 TYR A 96 1165 999 716 78 117 97 C -ATOM 353 CE1 TYR A 96 37.871 22.814 29.270 1.00 8.09 C -ANISOU 353 CE1 TYR A 96 1346 887 838 164 150 155 C -ATOM 354 CE2 TYR A 96 39.659 23.587 27.890 1.00 7.82 C -ANISOU 354 CE2 TYR A 96 1308 852 810 260 124 155 C -ATOM 355 CZ TYR A 96 38.726 22.620 28.218 1.00 7.05 C -ANISOU 355 CZ TYR A 96 1269 792 616 279 107 108 C -ATOM 356 OH TYR A 96 38.628 21.447 27.518 1.00 8.76 O -ANISOU 356 OH TYR A 96 1733 692 902 100 262 234 O -ATOM 357 N LEU A 97 36.940 28.832 31.123 1.00 7.39 N -ANISOU 357 N LEU A 97 1149 1088 570 173 45 -91 N -ATOM 358 CA LEU A 97 36.602 29.617 32.301 1.00 7.48 C -ANISOU 358 CA LEU A 97 1223 1008 609 175 4 -70 C -ATOM 359 C LEU A 97 35.731 28.717 33.170 1.00 8.25 C -ANISOU 359 C LEU A 97 1348 1168 617 225 87 -28 C -ATOM 360 O LEU A 97 34.679 28.249 32.754 1.00 9.30 O -ANISOU 360 O LEU A 97 1550 1407 574 245 261 -4 O -ATOM 361 CB LEU A 97 35.855 30.893 31.933 1.00 8.20 C -ANISOU 361 CB LEU A 97 1342 1028 743 152 -48 -144 C -ATOM 362 CG LEU A 97 35.619 31.870 33.083 1.00 10.44 C -ANISOU 362 CG LEU A 97 1614 1236 1115 233 -57 -79 C -ATOM 363 CD1 LEU A 97 36.893 32.376 33.661 1.00 12.92 C -ANISOU 363 CD1 LEU A 97 1946 1433 1529 294 -138 -168 C -ATOM 364 CD2 LEU A 97 34.813 33.035 32.587 1.00 13.72 C -ANISOU 364 CD2 LEU A 97 2087 1508 1617 353 -156 -163 C -ATOM 365 N ILE A 98 36.192 28.453 34.388 1.00 9.59 N -ANISOU 365 N ILE A 98 1524 1364 753 215 82 15 N -ATOM 366 CA ILE A 98 35.572 27.483 35.291 1.00 11.31 C -ANISOU 366 CA ILE A 98 1691 1593 1013 175 189 56 C -ATOM 367 C ILE A 98 35.063 28.195 36.537 1.00 13.03 C -ANISOU 367 C ILE A 98 1847 1841 1262 152 167 19 C -ATOM 368 O ILE A 98 35.846 28.803 37.223 1.00 13.62 O -ANISOU 368 O ILE A 98 2159 2078 936 297 325 -152 O -ATOM 369 CB ILE A 98 36.626 26.432 35.705 1.00 11.51 C -ANISOU 369 CB ILE A 98 1724 1608 1042 195 168 122 C -ATOM 370 CG1 ILE A 98 37.266 25.760 34.478 1.00 14.23 C -ANISOU 370 CG1 ILE A 98 2031 1808 1564 279 203 247 C -ATOM 371 CG2 ILE A 98 36.041 25.420 36.713 1.00 12.82 C -ANISOU 371 CG2 ILE A 98 1986 1714 1169 119 185 127 C -ATOM 372 CD1 ILE A 98 36.407 24.977 33.692 1.00 17.84 C -ANISOU 372 CD1 ILE A 98 2244 2312 2221 197 219 147 C -ATOM 373 N ASN A 99 33.755 28.126 36.771 1.00 13.87 N -ANISOU 373 N ASN A 99 2019 1912 1336 138 294 21 N -ATOM 374 CA ASN A 99 33.124 28.671 37.963 1.00 15.86 C -ANISOU 374 CA ASN A 99 2175 2108 1742 87 207 28 C -ATOM 375 C ASN A 99 33.287 27.740 39.147 1.00 16.91 C -ANISOU 375 C ASN A 99 2413 2136 1874 25 186 29 C -ATOM 376 O ASN A 99 33.064 26.526 39.060 1.00 18.08 O -ANISOU 376 O ASN A 99 2732 2376 1760 -92 408 138 O -ATOM 377 CB ASN A 99 31.634 28.888 37.739 1.00 16.88 C -ANISOU 377 CB ASN A 99 2298 2218 1898 90 208 -52 C -ATOM 378 CG ASN A 99 30.971 29.502 38.937 1.00 18.71 C -ANISOU 378 CG ASN A 99 2533 2550 2025 154 281 -20 C -ATOM 379 OD1 ASN A 99 30.409 28.800 39.777 1.00 21.30 O -ANISOU 379 OD1 ASN A 99 3158 3203 1732 132 581 -164 O -ATOM 380 ND2 ASN A 99 31.073 30.813 39.052 1.00 20.44 N -ANISOU 380 ND2 ASN A 99 2942 2626 2195 310 362 -681 N -ATOM 381 N GLN A 100 33.694 28.340 40.249 1.00 17.83 N -ANISOU 381 N GLN A 100 2505 2293 1976 19 126 90 N -ATOM 382 CA GLN A 100 33.844 27.655 41.518 1.00 19.07 C -ANISOU 382 CA GLN A 100 2574 2472 2198 29 74 61 C -ATOM 383 C GLN A 100 33.106 28.467 42.579 1.00 19.98 C -ANISOU 383 C GLN A 100 2669 2583 2340 24 63 35 C -ATOM 384 O GLN A 100 33.696 28.935 43.547 1.00 20.42 O -ANISOU 384 O GLN A 100 2748 2732 2276 54 27 -10 O -ATOM 385 CB GLN A 100 35.326 27.532 41.833 1.00 19.00 C -ANISOU 385 CB GLN A 100 2587 2474 2155 53 78 32 C -ATOM 386 CG GLN A 100 36.072 26.694 40.803 1.00 20.95 C -ANISOU 386 CG GLN A 100 2791 2758 2408 79 81 1 C -ATOM 387 CD GLN A 100 37.569 26.712 40.988 1.00 23.06 C -ANISOU 387 CD GLN A 100 3053 3065 2641 9 112 -19 C -ATOM 388 OE1 GLN A 100 38.112 27.582 41.673 1.00 25.81 O -ANISOU 388 OE1 GLN A 100 3315 3407 3082 -64 200 -25 O -ATOM 389 NE2 GLN A 100 38.248 25.753 40.365 1.00 24.14 N -ANISOU 389 NE2 GLN A 100 3146 3221 2803 174 165 27 N -ATOM 390 N GLY A 101 31.803 28.633 42.384 1.00 21.10 N -ANISOU 390 N GLY A 101 2757 2719 2538 36 57 0 N -ATOM 391 CA GLY A 101 30.973 29.381 43.319 1.00 21.76 C -ANISOU 391 CA GLY A 101 2833 2809 2625 44 59 -31 C -ATOM 392 C GLY A 101 31.099 30.883 43.122 1.00 22.45 C -ANISOU 392 C GLY A 101 2950 2860 2719 40 36 -33 C -ATOM 393 O GLY A 101 30.743 31.399 42.061 1.00 22.91 O -ANISOU 393 O GLY A 101 3082 2969 2654 157 68 -92 O -ATOM 394 N ASP A 102 31.617 31.594 44.126 1.00 23.19 N -ANISOU 394 N ASP A 102 3049 2961 2800 21 36 -20 N -ATOM 395 CA ASP A 102 31.788 33.054 44.029 1.00 23.87 C -ANISOU 395 CA ASP A 102 3095 3025 2947 9 24 -19 C -ATOM 396 C ASP A 102 33.144 33.431 43.435 1.00 23.12 C -ANISOU 396 C ASP A 102 3028 2917 2840 11 38 -34 C -ATOM 397 O ASP A 102 33.490 34.611 43.376 1.00 23.97 O -ANISOU 397 O ASP A 102 3166 3004 2935 -3 68 -49 O -ATOM 398 CB ASP A 102 31.616 33.777 45.382 1.00 24.59 C -ANISOU 398 CB ASP A 102 3185 3123 3033 2 25 -19 C -ATOM 399 CG ASP A 102 31.047 32.897 46.460 1.00 27.28 C -ANISOU 399 CG ASP A 102 3476 3507 3382 -11 -57 56 C -ATOM 400 OD1 ASP A 102 29.909 32.403 46.292 1.00 31.96 O -ANISOU 400 OD1 ASP A 102 4029 4123 3988 -34 -130 104 O -ATOM 401 OD2 ASP A 102 31.670 32.656 47.515 1.00 30.79 O -ANISOU 401 OD2 ASP A 102 3993 4047 3659 104 -123 197 O -ATOM 402 N HIS A 103 33.911 32.430 43.012 1.00 22.02 N -ANISOU 402 N HIS A 103 2865 2800 2700 28 -7 -28 N -ATOM 403 CA HIS A 103 35.153 32.661 42.291 1.00 20.90 C -ANISOU 403 CA HIS A 103 2740 2706 2492 38 -29 -86 C -ATOM 404 C HIS A 103 35.204 31.797 41.031 1.00 19.27 C -ANISOU 404 C HIS A 103 2570 2510 2239 60 -42 -119 C -ATOM 405 O HIS A 103 34.331 30.965 40.802 1.00 18.91 O -ANISOU 405 O HIS A 103 2720 2524 1938 150 20 -196 O -ATOM 406 CB HIS A 103 36.371 32.411 43.196 1.00 21.40 C -ANISOU 406 CB HIS A 103 2786 2774 2567 28 -35 -79 C -ATOM 407 CG HIS A 103 36.353 31.089 43.900 1.00 23.28 C -ANISOU 407 CG HIS A 103 3066 3025 2751 53 -78 -34 C -ATOM 408 ND1 HIS A 103 35.549 30.835 44.992 1.00 25.17 N -ANISOU 408 ND1 HIS A 103 3466 3198 2899 42 -53 62 N -ATOM 409 CD2 HIS A 103 37.063 29.958 43.684 1.00 25.49 C -ANISOU 409 CD2 HIS A 103 3390 3289 3002 111 12 -17 C -ATOM 410 CE1 HIS A 103 35.757 29.598 45.410 1.00 25.71 C -ANISOU 410 CE1 HIS A 103 3492 3325 2950 122 -29 10 C -ATOM 411 NE2 HIS A 103 36.668 29.043 44.630 1.00 26.20 N -ANISOU 411 NE2 HIS A 103 3479 3397 3075 103 -51 76 N -ATOM 412 N GLU A 104 36.231 32.023 40.225 1.00 17.29 N -ANISOU 412 N GLU A 104 2383 2336 1848 74 -29 -233 N -ATOM 413 CA GLU A 104 36.398 31.323 38.945 1.00 16.62 C -ANISOU 413 CA GLU A 104 2257 2218 1839 90 -7 -190 C -ATOM 414 C GLU A 104 37.862 31.314 38.534 1.00 16.24 C -ANISOU 414 C GLU A 104 2187 2226 1755 77 -36 -198 C -ATOM 415 O GLU A 104 38.674 32.078 39.031 1.00 16.39 O -ANISOU 415 O GLU A 104 2337 2237 1652 87 -27 -442 O -ATOM 416 CB GLU A 104 35.565 31.995 37.846 1.00 17.03 C -ANISOU 416 CB GLU A 104 2298 2249 1922 92 6 -166 C -ATOM 417 CG GLU A 104 36.061 33.384 37.446 1.00 17.92 C -ANISOU 417 CG GLU A 104 2372 2362 2074 72 51 -111 C -ATOM 418 CD GLU A 104 35.096 34.158 36.557 1.00 20.00 C -ANISOU 418 CD GLU A 104 2535 2592 2472 -48 28 -35 C -ATOM 419 OE1 GLU A 104 33.900 33.789 36.452 1.00 21.44 O -ANISOU 419 OE1 GLU A 104 2613 2826 2708 12 -60 -34 O -ATOM 420 OE2 GLU A 104 35.544 35.162 35.956 1.00 20.94 O -ANISOU 420 OE2 GLU A 104 2816 2544 2596 -100 -83 -143 O -ATOM 421 N VAL A 105 38.184 30.479 37.558 1.00 14.06 N -ANISOU 421 N VAL A 105 1937 2057 1345 130 -42 -297 N -ATOM 422 CA VAL A 105 39.554 30.302 37.113 1.00 13.28 C -ANISOU 422 CA VAL A 105 1858 1907 1281 123 -69 -128 C -ATOM 423 C VAL A 105 39.618 30.150 35.600 1.00 11.33 C -ANISOU 423 C VAL A 105 1701 1623 981 194 -141 -209 C -ATOM 424 O VAL A 105 38.731 29.550 34.994 1.00 11.39 O -ANISOU 424 O VAL A 105 1849 1675 802 163 -178 -157 O -ATOM 425 CB VAL A 105 40.213 29.085 37.794 1.00 13.22 C -ANISOU 425 CB VAL A 105 1964 2112 944 142 -13 -63 C -ATOM 426 CG1 VAL A 105 39.512 27.779 37.517 1.00 16.04 C -ANISOU 426 CG1 VAL A 105 2149 2243 1703 244 49 76 C -ATOM 427 CG2 VAL A 105 41.627 28.999 37.422 1.00 16.84 C -ANISOU 427 CG2 VAL A 105 2254 2283 1859 105 -89 23 C -ATOM 428 N VAL A 106 40.686 30.681 35.023 1.00 10.61 N -ANISOU 428 N VAL A 106 1629 1518 883 138 -224 -226 N -ATOM 429 CA VAL A 106 40.963 30.535 33.590 1.00 10.24 C -ANISOU 429 CA VAL A 106 1483 1483 923 165 -125 -173 C -ATOM 430 C VAL A 106 42.037 29.464 33.416 1.00 10.18 C -ANISOU 430 C VAL A 106 1454 1494 919 197 -153 -180 C -ATOM 431 O VAL A 106 43.063 29.491 34.094 1.00 11.53 O -ANISOU 431 O VAL A 106 1636 1788 957 303 -303 -329 O -ATOM 432 CB VAL A 106 41.450 31.863 32.985 1.00 11.09 C -ANISOU 432 CB VAL A 106 1522 1526 1165 105 -140 -143 C -ATOM 433 CG1 VAL A 106 41.789 31.708 31.521 1.00 11.92 C -ANISOU 433 CG1 VAL A 106 1626 1503 1400 175 18 22 C -ATOM 434 CG2 VAL A 106 40.417 32.966 33.137 1.00 13.07 C -ANISOU 434 CG2 VAL A 106 1903 1608 1455 210 -23 -154 C -ATOM 435 N ARG A 107 41.799 28.513 32.520 1.00 9.45 N -ANISOU 435 N ARG A 107 1402 1393 792 216 -139 -165 N -ATOM 436 CA ARG A 107 42.738 27.431 32.247 1.00 9.04 C -ANISOU 436 CA ARG A 107 1321 1278 835 193 -68 -27 C -ATOM 437 C ARG A 107 42.893 27.256 30.746 1.00 7.69 C -ANISOU 437 C ARG A 107 1225 1013 681 146 -133 -44 C -ATOM 438 O ARG A 107 42.010 27.651 29.969 1.00 7.96 O -ANISOU 438 O ARG A 107 1224 1175 624 301 -169 19 O -ATOM 439 CB ARG A 107 42.226 26.126 32.877 1.00 9.73 C -ANISOU 439 CB ARG A 107 1496 1363 836 306 1 -47 C -ATOM 440 CG ARG A 107 42.115 26.154 34.398 1.00 12.87 C -ANISOU 440 CG ARG A 107 1809 1869 1212 161 53 -34 C -ATOM 441 CD ARG A 107 43.470 26.004 35.041 1.00 15.46 C -ANISOU 441 CD ARG A 107 2199 2174 1500 71 3 -157 C -ATOM 442 NE ARG A 107 43.418 25.960 36.499 1.00 18.29 N -ANISOU 442 NE ARG A 107 2493 2531 1925 18 -82 -80 N -ATOM 443 CZ ARG A 107 43.725 26.971 37.305 1.00 19.33 C -ANISOU 443 CZ ARG A 107 2662 2655 2026 -66 6 -75 C -ATOM 444 NH1 ARG A 107 44.081 28.160 36.812 1.00 21.92 N -ANISOU 444 NH1 ARG A 107 3057 2875 2396 -100 -51 -82 N -ATOM 445 NH2 ARG A 107 43.643 26.809 38.623 1.00 20.68 N -ANISOU 445 NH2 ARG A 107 2914 2876 2065 36 -141 -32 N -ATOM 446 N PHE A 108 44.002 26.642 30.358 1.00 6.72 N -ANISOU 446 N PHE A 108 1096 866 588 170 -125 36 N -ATOM 447 CA PHE A 108 44.342 26.451 28.953 1.00 6.30 C -ANISOU 447 CA PHE A 108 1008 810 575 130 -63 38 C -ATOM 448 C PHE A 108 44.654 24.994 28.698 1.00 6.31 C -ANISOU 448 C PHE A 108 1052 744 598 134 -130 84 C -ATOM 449 O PHE A 108 45.341 24.356 29.500 1.00 7.57 O -ANISOU 449 O PHE A 108 1310 872 693 172 -271 121 O -ATOM 450 CB PHE A 108 45.515 27.347 28.570 1.00 6.86 C -ANISOU 450 CB PHE A 108 1079 825 700 157 -110 45 C -ATOM 451 CG PHE A 108 45.228 28.792 28.811 1.00 6.48 C -ANISOU 451 CG PHE A 108 1128 653 680 140 -63 26 C -ATOM 452 CD1 PHE A 108 44.420 29.487 27.931 1.00 7.32 C -ANISOU 452 CD1 PHE A 108 1199 747 833 114 -84 24 C -ATOM 453 CD2 PHE A 108 45.681 29.445 29.948 1.00 8.00 C -ANISOU 453 CD2 PHE A 108 1321 851 867 92 -101 -43 C -ATOM 454 CE1 PHE A 108 44.107 30.811 28.163 1.00 8.24 C -ANISOU 454 CE1 PHE A 108 1243 770 1118 54 -164 76 C -ATOM 455 CE2 PHE A 108 45.371 30.771 30.170 1.00 9.23 C -ANISOU 455 CE2 PHE A 108 1528 915 1061 -40 -128 -123 C -ATOM 456 CZ PHE A 108 44.577 31.449 29.293 1.00 8.90 C -ANISOU 456 CZ PHE A 108 1483 748 1147 19 4 -16 C -ATOM 457 N ALA A 109 44.159 24.481 27.572 1.00 6.35 N -ANISOU 457 N ALA A 109 1064 717 629 129 -105 38 N -ATOM 458 CA ALA A 109 44.329 23.078 27.230 1.00 6.03 C -ANISOU 458 CA ALA A 109 968 692 631 104 -45 79 C -ATOM 459 C ALA A 109 44.941 22.919 25.860 1.00 5.82 C -ANISOU 459 C ALA A 109 950 677 585 137 -91 46 C -ATOM 460 O ALA A 109 44.664 23.676 24.928 1.00 6.89 O -ANISOU 460 O ALA A 109 1076 874 667 239 -49 83 O -ATOM 461 CB ALA A 109 43.026 22.353 27.254 1.00 6.99 C -ANISOU 461 CB ALA A 109 1095 827 733 103 -25 34 C -ATOM 462 N LYS A 110 45.758 21.876 25.744 1.00 5.87 N -ANISOU 462 N LYS A 110 953 620 657 119 -33 40 N -ATOM 463 CA LYS A 110 46.210 21.340 24.464 1.00 6.05 C -ANISOU 463 CA LYS A 110 900 635 763 72 27 21 C -ATOM 464 C LYS A 110 45.340 20.122 24.132 1.00 5.99 C -ANISOU 464 C LYS A 110 908 652 714 120 43 11 C -ATOM 465 O LYS A 110 44.358 19.851 24.815 1.00 6.73 O -ANISOU 465 O LYS A 110 952 815 787 54 40 -80 O -ATOM 466 CB LYS A 110 47.707 21.005 24.526 1.00 6.39 C -ANISOU 466 CB LYS A 110 897 690 840 19 67 0 C -ATOM 467 CG LYS A 110 48.100 20.021 25.607 1.00 7.59 C -ANISOU 467 CG LYS A 110 1093 788 1003 12 -107 109 C -ATOM 468 CD LYS A 110 49.601 19.769 25.628 1.00 9.27 C -ANISOU 468 CD LYS A 110 1216 949 1357 50 -191 7 C -ATOM 469 CE LYS A 110 49.979 18.842 26.751 1.00 12.58 C -ANISOU 469 CE LYS A 110 1598 1272 1910 88 -263 10 C -ATOM 470 NZ LYS A 110 51.442 18.589 26.775 1.00 14.24 N -ANISOU 470 NZ LYS A 110 1562 1375 2470 197 -760 -12 N -ATOM 471 N ARG A 111 45.694 19.367 23.103 1.00 6.58 N -ANISOU 471 N ARG A 111 958 724 815 10 59 -24 N -ATOM 472 CA ARG A 111 44.888 18.243 22.666 1.00 7.83 C -ANISOU 472 CA ARG A 111 1177 847 949 -36 20 -66 C -ATOM 473 C ARG A 111 44.595 17.264 23.785 1.00 7.77 C -ANISOU 473 C ARG A 111 1163 745 1045 -108 36 -123 C -ATOM 474 O ARG A 111 43.484 16.732 23.888 1.00 8.37 O -ANISOU 474 O ARG A 111 1101 786 1289 -152 35 -90 O -ATOM 475 CB ARG A 111 45.630 17.522 21.531 1.00 8.92 C -ANISOU 475 CB ARG A 111 1412 954 1021 -102 88 -122 C -ATOM 476 CG ARG A 111 45.165 16.130 21.170 1.00 11.40 C -ANISOU 476 CG ARG A 111 1616 1289 1424 -92 -41 14 C -ATOM 477 CD ARG A 111 43.858 16.171 20.472 1.00 12.12 C -ANISOU 477 CD ARG A 111 1537 1409 1656 38 -195 197 C -ATOM 478 NE ARG A 111 43.955 16.802 19.140 1.00 11.82 N -ANISOU 478 NE ARG A 111 1584 1403 1503 -32 -308 37 N -ATOM 479 CZ ARG A 111 42.902 17.211 18.428 1.00 10.37 C -ANISOU 479 CZ ARG A 111 1315 1311 1311 58 -164 148 C -ATOM 480 NH1 ARG A 111 41.679 17.073 18.925 1.00 13.27 N -ANISOU 480 NH1 ARG A 111 1502 1833 1703 12 -209 401 N -ATOM 481 NH2 ARG A 111 43.064 17.777 17.234 1.00 9.71 N -ANISOU 481 NH2 ARG A 111 1174 1305 1210 198 -126 -22 N -ATOM 482 N SER A 112 45.608 17.005 24.597 1.00 7.90 N -ANISOU 482 N SER A 112 1133 706 1162 -88 -19 -11 N -ATOM 483 CA SER A 112 45.563 15.939 25.586 1.00 8.27 C -ANISOU 483 CA SER A 112 1177 729 1233 -55 -1 45 C -ATOM 484 C SER A 112 45.229 16.353 27.002 1.00 7.90 C -ANISOU 484 C SER A 112 1191 668 1142 18 -56 109 C -ATOM 485 O SER A 112 45.206 15.493 27.868 1.00 9.49 O -ANISOU 485 O SER A 112 1664 661 1280 10 -176 232 O -ATOM 486 CB SER A 112 46.897 15.198 25.579 1.00 9.62 C -ANISOU 486 CB SER A 112 1342 807 1503 -14 27 65 C -ATOM 487 OG SER A 112 47.950 16.093 25.876 1.00 12.64 O -ANISOU 487 OG SER A 112 1312 1111 2380 23 -47 164 O -ATOM 488 N GLY A 113 44.960 17.629 27.263 1.00 7.00 N -ANISOU 488 N GLY A 113 1059 627 973 -81 -29 115 N -ATOM 489 CA GLY A 113 44.524 18.021 28.587 1.00 7.15 C -ANISOU 489 CA GLY A 113 1056 752 906 -18 -47 108 C -ATOM 490 C GLY A 113 44.823 19.451 28.915 1.00 6.24 C -ANISOU 490 C GLY A 113 982 619 769 23 -69 183 C -ATOM 491 O GLY A 113 45.505 20.161 28.178 1.00 6.75 O -ANISOU 491 O GLY A 113 1130 571 861 -47 -63 162 O -ATOM 492 N ILE A 114 44.272 19.892 30.039 1.00 6.59 N -ANISOU 492 N ILE A 114 1027 688 789 -28 -36 132 N -ATOM 493 CA ILE A 114 44.609 21.180 30.623 1.00 7.51 C -ANISOU 493 CA ILE A 114 1163 821 866 18 -99 118 C -ATOM 494 C ILE A 114 46.071 21.154 31.085 1.00 7.39 C -ANISOU 494 C ILE A 114 1142 758 905 17 -139 164 C -ATOM 495 O ILE A 114 46.553 20.159 31.643 1.00 8.44 O -ANISOU 495 O ILE A 114 1303 752 1150 73 -276 196 O -ATOM 496 CB ILE A 114 43.634 21.521 31.770 1.00 7.94 C -ANISOU 496 CB ILE A 114 1152 957 904 11 -112 104 C -ATOM 497 CG1 ILE A 114 42.280 21.933 31.182 1.00 9.49 C -ANISOU 497 CG1 ILE A 114 1297 1228 1080 20 -96 -34 C -ATOM 498 CG2 ILE A 114 44.175 22.643 32.645 1.00 9.35 C -ANISOU 498 CG2 ILE A 114 1377 1178 997 66 -127 -30 C -ATOM 499 CD1 ILE A 114 41.160 22.050 32.203 1.00 11.08 C -ANISOU 499 CD1 ILE A 114 1448 1451 1311 -2 27 12 C -HETATM 500 N MSE A 115 46.776 22.249 30.817 1.00 7.12 N -ANISOU 500 N MSE A 115 1183 677 843 35 -174 217 N -HETATM 501 CA MSE A 115 48.197 22.356 31.073 1.00 8.29 C -ANISOU 501 CA MSE A 115 1262 837 1050 0 -121 116 C -HETATM 502 C MSE A 115 48.520 23.012 32.399 1.00 8.40 C -ANISOU 502 C MSE A 115 1280 870 1041 39 -218 196 C -HETATM 503 O MSE A 115 47.846 23.932 32.858 1.00 8.84 O -ANISOU 503 O MSE A 115 1500 950 907 -5 -261 151 O -HETATM 504 CB MSE A 115 48.874 23.164 29.970 1.00 7.80 C -ANISOU 504 CB MSE A 115 1186 875 901 -3 -126 83 C -HETATM 505 CG MSE A 115 48.793 22.478 28.625 1.00 8.90 C -ANISOU 505 CG MSE A 115 1353 866 1163 7 -156 71 C -HETATM 506 SE MSE A 115 49.632 23.417 27.200 1.00 17.41 SE -ANISOU 506 SE MSE A 115 2266 2266 2082 -182 -41 -104 SE -HETATM 507 CE MSE A 115 48.262 24.733 26.890 1.00 11.29 C -ANISOU 507 CE MSE A 115 1773 1180 1335 -96 -228 -8 C -ATOM 508 N ASP A 116 49.598 22.540 33.015 1.00 9.01 N -ANISOU 508 N ASP A 116 1344 948 1130 -31 -280 185 N -ATOM 509 CA ASP A 116 50.231 23.259 34.090 1.00 9.89 C -ANISOU 509 CA ASP A 116 1403 1146 1209 -7 -295 171 C -ATOM 510 C ASP A 116 50.637 24.634 33.566 1.00 9.78 C -ANISOU 510 C ASP A 116 1349 1139 1225 -59 -264 131 C -ATOM 511 O ASP A 116 51.114 24.729 32.441 1.00 9.32 O -ANISOU 511 O ASP A 116 1394 1026 1118 -127 -354 120 O -ATOM 512 CB ASP A 116 51.465 22.494 34.566 1.00 11.31 C -ANISOU 512 CB ASP A 116 1570 1310 1416 2 -366 195 C -ATOM 513 CG ASP A 116 52.129 23.152 35.737 1.00 13.59 C -ANISOU 513 CG ASP A 116 1801 1706 1653 -130 -608 413 C -ATOM 514 OD1 ASP A 116 51.845 22.754 36.883 1.00 20.03 O -ANISOU 514 OD1 ASP A 116 2852 2685 2072 -560 -759 331 O -ATOM 515 OD2 ASP A 116 52.931 24.074 35.589 1.00 15.04 O -ANISOU 515 OD2 ASP A 116 2185 1753 1774 -199 -935 570 O -ATOM 516 N PRO A 117 50.465 25.691 34.358 1.00 10.22 N -ANISOU 516 N PRO A 117 1374 1209 1298 -45 -151 98 N -ATOM 517 CA PRO A 117 50.810 27.039 33.876 1.00 10.37 C -ANISOU 517 CA PRO A 117 1395 1216 1326 -18 -128 69 C -ATOM 518 C PRO A 117 52.275 27.245 33.468 1.00 9.46 C -ANISOU 518 C PRO A 117 1317 1104 1173 23 -148 67 C -ATOM 519 O PRO A 117 52.540 28.195 32.739 1.00 9.81 O -ANISOU 519 O PRO A 117 1408 1051 1266 -46 -232 89 O -ATOM 520 CB PRO A 117 50.448 27.940 35.058 1.00 11.62 C -ANISOU 520 CB PRO A 117 1566 1358 1488 -33 -83 39 C -ATOM 521 CG PRO A 117 49.481 27.171 35.833 1.00 13.84 C -ANISOU 521 CG PRO A 117 1807 1703 1746 -62 62 -65 C -ATOM 522 CD PRO A 117 49.874 25.734 35.707 1.00 11.98 C -ANISOU 522 CD PRO A 117 1586 1435 1529 -109 -97 18 C -ATOM 523 N ASN A 118 53.195 26.393 33.919 1.00 9.45 N -ANISOU 523 N ASN A 118 1312 1114 1165 30 -177 43 N -ATOM 524 CA ASN A 118 54.593 26.514 33.522 1.00 9.90 C -ANISOU 524 CA ASN A 118 1295 1170 1294 33 -160 -22 C -ATOM 525 C ASN A 118 55.027 25.540 32.428 1.00 9.61 C -ANISOU 525 C ASN A 118 1301 1142 1209 30 -168 -15 C -ATOM 526 O ASN A 118 56.213 25.429 32.133 1.00 10.66 O -ANISOU 526 O ASN A 118 1317 1237 1494 14 -215 -137 O -ATOM 527 CB ASN A 118 55.507 26.458 34.742 1.00 10.36 C -ANISOU 527 CB ASN A 118 1356 1255 1324 6 -170 -58 C -ATOM 528 CG ASN A 118 55.484 27.751 35.500 1.00 10.77 C -ANISOU 528 CG ASN A 118 1359 1314 1417 -31 -189 -126 C -ATOM 529 OD1 ASN A 118 55.715 28.815 34.928 1.00 11.74 O -ANISOU 529 OD1 ASN A 118 1549 1372 1537 -56 -292 -165 O -ATOM 530 ND2 ASN A 118 55.193 27.678 36.782 1.00 14.19 N -ANISOU 530 ND2 ASN A 118 2041 1776 1575 -131 -208 -85 N -ATOM 531 N GLU A 119 54.072 24.886 31.777 1.00 9.56 N -ANISOU 531 N GLU A 119 1305 1096 1232 70 -218 67 N -ATOM 532 CA GLU A 119 54.397 24.127 30.576 1.00 9.62 C -ANISOU 532 CA GLU A 119 1324 1112 1217 34 -174 41 C -ATOM 533 C GLU A 119 54.558 25.080 29.396 1.00 9.60 C -ANISOU 533 C GLU A 119 1399 1140 1105 -2 -252 21 C -ATOM 534 O GLU A 119 53.618 25.777 29.030 1.00 9.90 O -ANISOU 534 O GLU A 119 1516 1026 1220 169 -330 92 O -ATOM 535 CB GLU A 119 53.327 23.082 30.240 1.00 9.78 C -ANISOU 535 CB GLU A 119 1368 1032 1316 21 -189 81 C -ATOM 536 CG GLU A 119 53.690 22.332 28.961 1.00 11.09 C -ANISOU 536 CG GLU A 119 1547 1189 1476 30 -171 36 C -ATOM 537 CD GLU A 119 52.706 21.276 28.511 1.00 13.12 C -ANISOU 537 CD GLU A 119 1683 1301 2000 120 -169 -93 C -ATOM 538 OE1 GLU A 119 51.808 20.897 29.276 1.00 14.30 O -ANISOU 538 OE1 GLU A 119 1718 1426 2287 14 -238 -427 O -ATOM 539 OE2 GLU A 119 52.853 20.804 27.364 1.00 15.19 O -ANISOU 539 OE2 GLU A 119 1982 1604 2185 -105 -388 -312 O -ATOM 540 N ASN A 120 55.758 25.116 28.828 1.00 10.23 N -ANISOU 540 N ASN A 120 1458 1229 1199 19 -289 104 N -ATOM 541 CA ASN A 120 56.008 25.849 27.595 1.00 10.98 C -ANISOU 541 CA ASN A 120 1625 1311 1234 -89 -218 -5 C -ATOM 542 C ASN A 120 55.334 25.101 26.450 1.00 10.52 C -ANISOU 542 C ASN A 120 1609 1201 1187 -54 -267 -53 C -ATOM 543 O ASN A 120 55.632 23.941 26.216 1.00 12.07 O -ANISOU 543 O ASN A 120 1951 1157 1478 35 -513 18 O -ATOM 544 CB ASN A 120 57.513 25.976 27.344 1.00 12.40 C -ANISOU 544 CB ASN A 120 1845 1569 1297 -192 -232 -42 C -ATOM 545 CG ASN A 120 57.836 26.798 26.106 1.00 15.27 C -ANISOU 545 CG ASN A 120 2290 1660 1850 -515 -100 -140 C -ATOM 546 OD1 ASN A 120 57.098 27.713 25.741 1.00 18.02 O -ANISOU 546 OD1 ASN A 120 3199 1912 1736 -1134 -166 141 O -ATOM 547 ND2 ASN A 120 58.960 26.488 25.473 1.00 18.47 N -ANISOU 547 ND2 ASN A 120 3396 1889 1731 -739 358 -170 N -ATOM 548 N PHE A 121 54.407 25.762 25.768 1.00 9.08 N -ANISOU 548 N PHE A 121 1445 1050 952 -63 -299 -48 N -ATOM 549 CA PHE A 121 53.654 25.159 24.671 1.00 8.11 C -ANISOU 549 CA PHE A 121 1257 894 928 -28 -159 -59 C -ATOM 550 C PHE A 121 53.513 26.178 23.546 1.00 7.15 C -ANISOU 550 C PHE A 121 1087 763 865 -29 -161 -4 C -ATOM 551 O PHE A 121 52.587 26.996 23.509 1.00 6.94 O -ANISOU 551 O PHE A 121 1061 757 816 -10 -128 -61 O -ATOM 552 CB PHE A 121 52.304 24.691 25.182 1.00 8.53 C -ANISOU 552 CB PHE A 121 1438 963 838 -65 -184 7 C -ATOM 553 CG PHE A 121 51.474 23.991 24.154 1.00 8.50 C -ANISOU 553 CG PHE A 121 1332 990 905 -161 -91 52 C -ATOM 554 CD1 PHE A 121 51.737 22.680 23.811 1.00 9.26 C -ANISOU 554 CD1 PHE A 121 1504 1016 997 -113 -195 16 C -ATOM 555 CD2 PHE A 121 50.403 24.632 23.549 1.00 9.28 C -ANISOU 555 CD2 PHE A 121 1341 1258 924 -138 -80 -78 C -ATOM 556 CE1 PHE A 121 50.958 22.022 22.872 1.00 10.37 C -ANISOU 556 CE1 PHE A 121 1700 1118 1121 -251 -19 14 C -ATOM 557 CE2 PHE A 121 49.628 23.973 22.610 1.00 9.99 C -ANISOU 557 CE2 PHE A 121 1330 1573 891 -188 -24 224 C -ATOM 558 CZ PHE A 121 49.902 22.665 22.287 1.00 9.82 C -ANISOU 558 CZ PHE A 121 1436 1347 946 -442 -64 108 C -ATOM 559 N PHE A 122 54.482 26.143 22.648 1.00 7.02 N -ANISOU 559 N PHE A 122 980 781 903 39 -144 -4 N -ATOM 560 CA PHE A 122 54.491 26.952 21.442 1.00 6.44 C -ANISOU 560 CA PHE A 122 859 776 810 -23 -41 -4 C -ATOM 561 C PHE A 122 54.350 28.445 21.728 1.00 6.81 C -ANISOU 561 C PHE A 122 938 794 856 -47 -58 33 C -ATOM 562 O PHE A 122 53.843 29.191 20.903 1.00 8.01 O -ANISOU 562 O PHE A 122 1213 878 951 118 -74 32 O -ATOM 563 CB PHE A 122 53.418 26.473 20.464 1.00 6.74 C -ANISOU 563 CB PHE A 122 877 865 818 -22 4 -38 C -ATOM 564 CG PHE A 122 53.603 25.052 20.018 1.00 6.82 C -ANISOU 564 CG PHE A 122 936 826 829 -57 -104 33 C -ATOM 565 CD1 PHE A 122 54.737 24.670 19.311 1.00 7.27 C -ANISOU 565 CD1 PHE A 122 1075 716 968 -57 -78 63 C -ATOM 566 CD2 PHE A 122 52.630 24.099 20.257 1.00 8.48 C -ANISOU 566 CD2 PHE A 122 1029 991 1199 -26 71 -118 C -ATOM 567 CE1 PHE A 122 54.907 23.372 18.890 1.00 7.87 C -ANISOU 567 CE1 PHE A 122 1179 790 1019 -38 -25 19 C -ATOM 568 CE2 PHE A 122 52.785 22.808 19.810 1.00 10.47 C -ANISOU 568 CE2 PHE A 122 1376 950 1652 -214 -9 -157 C -ATOM 569 CZ PHE A 122 53.922 22.441 19.119 1.00 10.24 C -ANISOU 569 CZ PHE A 122 1459 862 1566 -27 -24 -141 C -ATOM 570 N GLY A 123 54.840 28.891 22.883 1.00 7.31 N -ANISOU 570 N GLY A 123 961 809 1004 -57 -71 -37 N -ATOM 571 CA GLY A 123 54.855 30.307 23.196 1.00 7.80 C -ANISOU 571 CA GLY A 123 1016 818 1127 -43 -83 -16 C -ATOM 572 C GLY A 123 53.510 30.920 23.516 1.00 7.05 C -ANISOU 572 C GLY A 123 979 760 938 -36 -92 29 C -ATOM 573 O GLY A 123 53.404 32.151 23.519 1.00 7.63 O -ANISOU 573 O GLY A 123 1031 715 1151 18 2 -8 O -ATOM 574 N TYR A 124 52.490 30.105 23.815 1.00 6.43 N -ANISOU 574 N TYR A 124 929 674 840 -29 -55 48 N -ATOM 575 CA TYR A 124 51.128 30.639 23.913 1.00 6.80 C -ANISOU 575 CA TYR A 124 916 715 952 -16 -115 11 C -ATOM 576 C TYR A 124 50.976 31.628 25.049 1.00 6.70 C -ANISOU 576 C TYR A 124 786 742 1017 0 -150 57 C -ATOM 577 O TYR A 124 50.046 32.412 25.055 1.00 7.01 O -ANISOU 577 O TYR A 124 802 685 1173 61 -211 56 O -ATOM 578 CB TYR A 124 50.072 29.528 24.050 1.00 6.55 C -ANISOU 578 CB TYR A 124 830 812 845 -53 -166 0 C -ATOM 579 CG TYR A 124 49.862 29.041 25.461 1.00 6.11 C -ANISOU 579 CG TYR A 124 815 719 785 -49 -209 -86 C -ATOM 580 CD1 TYR A 124 48.870 29.605 26.262 1.00 6.80 C -ANISOU 580 CD1 TYR A 124 983 822 775 2 -208 91 C -ATOM 581 CD2 TYR A 124 50.652 28.044 26.000 1.00 7.29 C -ANISOU 581 CD2 TYR A 124 918 944 905 -74 -64 -139 C -ATOM 582 CE1 TYR A 124 48.669 29.184 27.555 1.00 7.32 C -ANISOU 582 CE1 TYR A 124 1030 953 797 117 -29 1 C -ATOM 583 CE2 TYR A 124 50.466 27.618 27.301 1.00 7.63 C -ANISOU 583 CE2 TYR A 124 1199 831 866 41 -40 -48 C -ATOM 584 CZ TYR A 124 49.465 28.182 28.072 1.00 7.32 C -ANISOU 584 CZ TYR A 124 1251 838 689 75 -91 -31 C -ATOM 585 OH TYR A 124 49.280 27.772 29.363 1.00 8.99 O -ANISOU 585 OH TYR A 124 1456 1263 697 235 71 135 O -ATOM 586 N HIS A 125 51.896 31.605 26.006 1.00 6.71 N -ANISOU 586 N HIS A 125 855 718 976 67 -214 -16 N -ATOM 587 CA HIS A 125 51.852 32.570 27.082 1.00 7.27 C -ANISOU 587 CA HIS A 125 940 784 1036 52 -207 4 C -ATOM 588 C HIS A 125 51.810 34.008 26.575 1.00 7.37 C -ANISOU 588 C HIS A 125 905 760 1135 132 -266 3 C -ATOM 589 O HIS A 125 51.269 34.862 27.273 1.00 8.57 O -ANISOU 589 O HIS A 125 1174 723 1359 257 -356 -177 O -ATOM 590 CB HIS A 125 53.024 32.380 28.042 1.00 7.59 C -ANISOU 590 CB HIS A 125 953 816 1115 36 -236 18 C -ATOM 591 CG HIS A 125 52.969 31.081 28.758 1.00 8.71 C -ANISOU 591 CG HIS A 125 1107 980 1222 0 -479 -14 C -ATOM 592 ND1 HIS A 125 53.320 29.901 28.148 1.00 11.90 N -ANISOU 592 ND1 HIS A 125 1581 1075 1866 -32 -717 17 N -ATOM 593 CD2 HIS A 125 52.537 30.761 29.998 1.00 10.43 C -ANISOU 593 CD2 HIS A 125 1104 1159 1698 14 -377 149 C -ATOM 594 CE1 HIS A 125 53.158 28.910 29.000 1.00 12.50 C -ANISOU 594 CE1 HIS A 125 1522 1178 2047 -160 -732 367 C -ATOM 595 NE2 HIS A 125 52.671 29.400 30.127 1.00 12.18 N -ANISOU 595 NE2 HIS A 125 1337 1373 1918 -66 -615 578 N -ATOM 596 N ILE A 126 52.356 34.278 25.382 1.00 7.71 N -ANISOU 596 N ILE A 126 948 707 1274 63 -198 25 N -ATOM 597 CA ILE A 126 52.320 35.625 24.794 1.00 8.53 C -ANISOU 597 CA ILE A 126 1029 816 1394 66 -184 31 C -ATOM 598 C ILE A 126 50.874 36.118 24.576 1.00 8.32 C -ANISOU 598 C ILE A 126 998 819 1340 63 -152 7 C -ATOM 599 O ILE A 126 50.637 37.332 24.518 1.00 9.73 O -ANISOU 599 O ILE A 126 1189 719 1789 111 -251 107 O -ATOM 600 CB ILE A 126 53.146 35.657 23.465 1.00 9.65 C -ANISOU 600 CB ILE A 126 1071 968 1627 72 -83 139 C -ATOM 601 CG1 ILE A 126 53.564 37.078 23.095 1.00 11.74 C -ANISOU 601 CG1 ILE A 126 1441 1243 1773 -11 -133 146 C -ATOM 602 CG2 ILE A 126 52.395 35.082 22.302 1.00 9.93 C -ANISOU 602 CG2 ILE A 126 1023 1032 1716 106 67 101 C -ATOM 603 CD1 ILE A 126 54.772 37.552 23.802 1.00 14.30 C -ANISOU 603 CD1 ILE A 126 1835 1573 2023 -89 -68 83 C -ATOM 604 N LEU A 127 49.921 35.189 24.475 1.00 7.45 N -ANISOU 604 N LEU A 127 926 724 1179 67 -155 6 N -ATOM 605 CA LEU A 127 48.520 35.512 24.242 1.00 7.51 C -ANISOU 605 CA LEU A 127 939 857 1055 91 -144 28 C -ATOM 606 C LEU A 127 47.636 35.413 25.480 1.00 6.84 C -ANISOU 606 C LEU A 127 929 714 956 146 -193 -54 C -ATOM 607 O LEU A 127 46.453 35.712 25.390 1.00 7.31 O -ANISOU 607 O LEU A 127 833 933 1010 191 -167 -118 O -ATOM 608 CB LEU A 127 47.952 34.592 23.156 1.00 7.28 C -ANISOU 608 CB LEU A 127 859 897 1007 102 -86 4 C -ATOM 609 CG LEU A 127 48.616 34.673 21.772 1.00 10.63 C -ANISOU 609 CG LEU A 127 1348 1481 1210 -121 11 -9 C -ATOM 610 CD1 LEU A 127 48.038 33.668 20.808 1.00 10.49 C -ANISOU 610 CD1 LEU A 127 1246 1538 1202 160 101 -137 C -ATOM 611 CD2 LEU A 127 48.526 36.045 21.200 1.00 13.35 C -ANISOU 611 CD2 LEU A 127 1808 1736 1526 -102 -75 -43 C -ATOM 612 N ILE A 128 48.170 35.035 26.636 1.00 7.46 N -ANISOU 612 N ILE A 128 891 910 1033 118 -214 -59 N -ATOM 613 CA ILE A 128 47.315 34.801 27.794 1.00 7.64 C -ANISOU 613 CA ILE A 128 976 954 971 210 -222 -80 C -ATOM 614 C ILE A 128 46.564 36.036 28.244 1.00 8.00 C -ANISOU 614 C ILE A 128 989 1011 1039 159 -273 -98 C -ATOM 615 O ILE A 128 45.395 35.946 28.622 1.00 7.90 O -ANISOU 615 O ILE A 128 997 1094 908 240 -250 -167 O -ATOM 616 CB ILE A 128 48.113 34.172 28.965 1.00 8.29 C -ANISOU 616 CB ILE A 128 1085 1020 1042 149 -259 -97 C -ATOM 617 CG1 ILE A 128 48.359 32.704 28.654 1.00 8.88 C -ANISOU 617 CG1 ILE A 128 1093 1176 1104 191 -140 -73 C -ATOM 618 CG2 ILE A 128 47.378 34.331 30.296 1.00 9.36 C -ANISOU 618 CG2 ILE A 128 1269 1199 1087 307 -284 -19 C -ATOM 619 CD1 ILE A 128 49.231 31.997 29.681 1.00 8.97 C -ANISOU 619 CD1 ILE A 128 1293 1079 1035 171 -103 43 C -ATOM 620 N ASP A 129 47.204 37.195 28.238 1.00 8.51 N -ANISOU 620 N ASP A 129 1065 979 1186 173 -246 -178 N -ATOM 621 CA ASP A 129 46.471 38.393 28.669 1.00 9.49 C -ANISOU 621 CA ASP A 129 1216 1110 1277 95 -210 -226 C -ATOM 622 C ASP A 129 45.258 38.658 27.759 1.00 8.91 C -ANISOU 622 C ASP A 129 1109 965 1310 76 -162 -190 C -ATOM 623 O ASP A 129 44.168 38.989 28.229 1.00 9.24 O -ANISOU 623 O ASP A 129 1142 1033 1334 216 -274 -194 O -ATOM 624 CB ASP A 129 47.372 39.622 28.706 1.00 10.89 C -ANISOU 624 CB ASP A 129 1350 1246 1540 131 -243 -271 C -ATOM 625 CG ASP A 129 48.340 39.610 29.856 1.00 13.80 C -ANISOU 625 CG ASP A 129 1765 1539 1939 -72 -300 -297 C -ATOM 626 OD1 ASP A 129 48.138 38.856 30.823 1.00 17.48 O -ANISOU 626 OD1 ASP A 129 2298 2462 1882 75 -831 -619 O -ATOM 627 OD2 ASP A 129 49.323 40.366 29.856 1.00 19.74 O -ANISOU 627 OD2 ASP A 129 2156 2426 2917 -246 -730 -406 O -ATOM 628 N GLU A 130 45.460 38.513 26.457 1.00 8.36 N -ANISOU 628 N GLU A 130 1054 862 1258 134 -223 -119 N -ATOM 629 CA GLU A 130 44.391 38.671 25.493 1.00 8.11 C -ANISOU 629 CA GLU A 130 1077 823 1180 123 -166 -90 C -ATOM 630 C GLU A 130 43.299 37.622 25.713 1.00 6.96 C -ANISOU 630 C GLU A 130 964 745 935 196 -173 -89 C -ATOM 631 O GLU A 130 42.112 37.961 25.784 1.00 7.16 O -ANISOU 631 O GLU A 130 953 685 1081 219 -218 -151 O -ATOM 632 CB GLU A 130 44.946 38.571 24.087 1.00 9.64 C -ANISOU 632 CB GLU A 130 1219 1093 1348 53 -205 22 C -ATOM 633 CG GLU A 130 43.852 38.614 23.055 1.00 12.17 C -ANISOU 633 CG GLU A 130 1539 1551 1531 -64 -179 -47 C -ATOM 634 CD GLU A 130 44.363 38.888 21.677 1.00 16.53 C -ANISOU 634 CD GLU A 130 2292 2116 1870 -211 -112 -106 C -ATOM 635 OE1 GLU A 130 44.823 40.028 21.454 1.00 19.73 O -ANISOU 635 OE1 GLU A 130 3007 2243 2244 -301 -73 -327 O -ATOM 636 OE2 GLU A 130 44.281 37.973 20.824 1.00 18.71 O -ANISOU 636 OE2 GLU A 130 2725 2564 1820 -166 159 -199 O -ATOM 637 N PHE A 131 43.693 36.354 25.829 1.00 6.20 N -ANISOU 637 N PHE A 131 896 665 793 197 -145 -90 N -ATOM 638 CA PHE A 131 42.727 35.280 26.009 1.00 5.86 C -ANISOU 638 CA PHE A 131 870 677 677 177 -147 -72 C -ATOM 639 C PHE A 131 41.898 35.505 27.276 1.00 5.65 C -ANISOU 639 C PHE A 131 843 640 663 188 -192 -106 C -ATOM 640 O PHE A 131 40.712 35.194 27.325 1.00 6.76 O -ANISOU 640 O PHE A 131 904 878 785 228 -167 -86 O -ATOM 641 CB PHE A 131 43.431 33.935 26.173 1.00 5.88 C -ANISOU 641 CB PHE A 131 886 617 731 112 -192 -87 C -ATOM 642 CG PHE A 131 44.124 33.394 24.936 1.00 5.82 C -ANISOU 642 CG PHE A 131 884 676 648 129 -144 -69 C -ATOM 643 CD1 PHE A 131 43.766 33.773 23.652 1.00 5.97 C -ANISOU 643 CD1 PHE A 131 925 647 695 190 -185 -179 C -ATOM 644 CD2 PHE A 131 45.111 32.440 25.076 1.00 6.62 C -ANISOU 644 CD2 PHE A 131 1031 731 752 162 -166 6 C -ATOM 645 CE1 PHE A 131 44.392 33.211 22.560 1.00 7.02 C -ANISOU 645 CE1 PHE A 131 1134 828 703 174 -102 -112 C -ATOM 646 CE2 PHE A 131 45.734 31.866 23.994 1.00 7.07 C -ANISOU 646 CE2 PHE A 131 1047 823 814 187 -83 -50 C -ATOM 647 CZ PHE A 131 45.371 32.243 22.729 1.00 7.47 C -ANISOU 647 CZ PHE A 131 1197 917 724 144 -2 -183 C -ATOM 648 N THR A 132 42.555 35.965 28.331 1.00 6.76 N -ANISOU 648 N THR A 132 960 878 728 187 -155 -114 N -ATOM 649 CA THR A 132 41.902 36.153 29.618 1.00 7.15 C -ANISOU 649 CA THR A 132 1094 899 721 206 -179 -158 C -ATOM 650 C THR A 132 40.857 37.266 29.519 1.00 7.41 C -ANISOU 650 C THR A 132 1059 935 819 165 -203 -147 C -ATOM 651 O THR A 132 39.728 37.098 29.968 1.00 8.18 O -ANISOU 651 O THR A 132 1248 984 876 277 -210 -246 O -ATOM 652 CB THR A 132 42.961 36.466 30.671 1.00 8.08 C -ANISOU 652 CB THR A 132 1141 1079 850 244 -220 -171 C -ATOM 653 OG1 THR A 132 43.837 35.319 30.799 1.00 9.23 O -ANISOU 653 OG1 THR A 132 1307 1342 856 523 -286 -180 O -ATOM 654 CG2 THR A 132 42.317 36.703 32.045 1.00 9.02 C -ANISOU 654 CG2 THR A 132 1287 1356 784 270 -256 -156 C -ATOM 655 N ALA A 133 41.215 38.379 28.891 1.00 7.29 N -ANISOU 655 N ALA A 133 1005 873 889 205 -189 -176 N -ATOM 656 CA ALA A 133 40.238 39.447 28.691 1.00 7.46 C -ANISOU 656 CA ALA A 133 1002 897 936 180 -166 -165 C -ATOM 657 C ALA A 133 39.079 38.962 27.828 1.00 7.25 C -ANISOU 657 C ALA A 133 975 857 921 206 -173 -169 C -ATOM 658 O ALA A 133 37.913 39.251 28.110 1.00 7.60 O -ANISOU 658 O ALA A 133 1081 884 922 300 -187 -268 O -ATOM 659 CB ALA A 133 40.884 40.648 28.056 1.00 8.36 C -ANISOU 659 CB ALA A 133 1050 952 1173 154 -172 -236 C -ATOM 660 N GLN A 134 39.407 38.205 26.784 1.00 6.26 N -ANISOU 660 N GLN A 134 889 744 744 221 -140 -144 N -ATOM 661 CA GLN A 134 38.394 37.702 25.859 1.00 6.28 C -ANISOU 661 CA GLN A 134 834 761 790 164 -141 -104 C -ATOM 662 C GLN A 134 37.407 36.738 26.509 1.00 6.27 C -ANISOU 662 C GLN A 134 882 710 787 216 -118 -178 C -ATOM 663 O GLN A 134 36.205 36.841 26.290 1.00 6.30 O -ANISOU 663 O GLN A 134 886 793 713 171 -68 -167 O -ATOM 664 CB GLN A 134 39.060 37.054 24.649 1.00 6.43 C -ANISOU 664 CB GLN A 134 851 778 812 245 -121 -28 C -ATOM 665 CG GLN A 134 39.747 38.048 23.740 1.00 6.42 C -ANISOU 665 CG GLN A 134 898 704 834 196 -187 -53 C -ATOM 666 CD GLN A 134 40.540 37.383 22.629 1.00 6.15 C -ANISOU 666 CD GLN A 134 920 693 722 168 -105 -215 C -ATOM 667 OE1 GLN A 134 41.037 36.266 22.794 1.00 7.30 O -ANISOU 667 OE1 GLN A 134 1214 788 771 261 -54 -43 O -ATOM 668 NE2 GLN A 134 40.687 38.079 21.495 1.00 7.31 N -ANISOU 668 NE2 GLN A 134 1181 854 741 91 -107 -76 N -ATOM 669 N ILE A 135 37.909 35.763 27.259 1.00 6.39 N -ANISOU 669 N ILE A 135 927 746 754 201 -143 -81 N -ATOM 670 CA ILE A 135 37.024 34.747 27.817 1.00 6.48 C -ANISOU 670 CA ILE A 135 928 745 789 213 -63 -106 C -ATOM 671 C ILE A 135 36.096 35.353 28.876 1.00 6.64 C -ANISOU 671 C ILE A 135 973 734 812 144 -53 -153 C -ATOM 672 O ILE A 135 34.943 34.951 28.996 1.00 7.17 O -ANISOU 672 O ILE A 135 1074 838 812 201 -87 -119 O -ATOM 673 CB ILE A 135 37.833 33.529 28.330 1.00 6.63 C -ANISOU 673 CB ILE A 135 941 827 750 214 -46 -90 C -ATOM 674 CG1 ILE A 135 36.926 32.298 28.454 1.00 7.79 C -ANISOU 674 CG1 ILE A 135 1223 840 897 233 9 -145 C -ATOM 675 CG2 ILE A 135 38.523 33.819 29.643 1.00 7.36 C -ANISOU 675 CG2 ILE A 135 1010 890 897 182 -125 43 C -ATOM 676 CD1 ILE A 135 36.492 31.699 27.135 1.00 7.75 C -ANISOU 676 CD1 ILE A 135 1172 896 874 106 10 -30 C -ATOM 677 N ARG A 136 36.579 36.351 29.603 1.00 7.16 N -ANISOU 677 N ARG A 136 1005 894 818 181 -69 -149 N -ATOM 678 CA ARG A 136 35.733 37.068 30.557 1.00 7.70 C -ANISOU 678 CA ARG A 136 1073 1010 843 162 -15 -197 C -ATOM 679 C ARG A 136 34.602 37.809 29.868 1.00 7.78 C -ANISOU 679 C ARG A 136 1041 1032 883 139 23 -233 C -ATOM 680 O ARG A 136 33.452 37.779 30.320 1.00 8.74 O -ANISOU 680 O ARG A 136 1147 1162 1009 246 -11 -256 O -ATOM 681 CB ARG A 136 36.586 38.024 31.387 1.00 8.82 C -ANISOU 681 CB ARG A 136 1204 1176 971 161 -33 -161 C -ATOM 682 CG ARG A 136 37.486 37.287 32.364 1.00 11.28 C -ANISOU 682 CG ARG A 136 1388 1542 1353 60 -16 -210 C -ATOM 683 CD ARG A 136 38.308 38.210 33.240 1.00 16.68 C -ANISOU 683 CD ARG A 136 2165 2152 2019 94 -75 -203 C -ATOM 684 NE ARG A 136 39.379 37.515 33.958 1.00 19.66 N -ANISOU 684 NE ARG A 136 2454 2804 2211 114 -80 -241 N -ATOM 685 CZ ARG A 136 39.225 36.603 34.933 1.00 25.21 C -ANISOU 685 CZ ARG A 136 3076 3376 3126 43 -45 -129 C -ATOM 686 NH1 ARG A 136 38.026 36.220 35.366 1.00 26.61 N -ANISOU 686 NH1 ARG A 136 3299 3547 3261 -68 -26 -162 N -ATOM 687 NH2 ARG A 136 40.308 36.055 35.490 1.00 27.27 N -ANISOU 687 NH2 ARG A 136 3340 3615 3404 139 -1 -91 N -ATOM 688 N ILE A 137 34.923 38.447 28.753 1.00 7.28 N -ANISOU 688 N ILE A 137 1010 884 871 235 -35 -225 N -ATOM 689 CA ILE A 137 33.910 39.150 27.977 1.00 7.52 C -ANISOU 689 CA ILE A 137 976 918 962 252 -71 -209 C -ATOM 690 C ILE A 137 32.882 38.165 27.436 1.00 7.82 C -ANISOU 690 C ILE A 137 994 1041 935 257 -59 -268 C -ATOM 691 O ILE A 137 31.678 38.419 27.509 1.00 8.16 O -ANISOU 691 O ILE A 137 1065 1029 1004 364 -125 -241 O -ATOM 692 CB ILE A 137 34.570 39.969 26.861 1.00 7.44 C -ANISOU 692 CB ILE A 137 930 857 1039 268 -161 -280 C -ATOM 693 CG1 ILE A 137 35.288 41.175 27.473 1.00 8.23 C -ANISOU 693 CG1 ILE A 137 1182 868 1075 232 -274 -215 C -ATOM 694 CG2 ILE A 137 33.541 40.430 25.819 1.00 8.01 C -ANISOU 694 CG2 ILE A 137 1162 855 1025 149 -190 -232 C -ATOM 695 CD1 ILE A 137 36.288 41.802 26.581 1.00 8.69 C -ANISOU 695 CD1 ILE A 137 1260 737 1303 135 -376 -266 C -ATOM 696 N LEU A 138 33.341 37.031 26.914 1.00 7.13 N -ANISOU 696 N LEU A 138 948 865 896 207 -40 -198 N -ATOM 697 CA LEU A 138 32.428 36.052 26.362 1.00 6.77 C -ANISOU 697 CA LEU A 138 882 899 790 199 -22 -162 C -ATOM 698 C LEU A 138 31.484 35.537 27.444 1.00 7.24 C -ANISOU 698 C LEU A 138 942 974 834 213 -39 -209 C -ATOM 699 O LEU A 138 30.280 35.402 27.221 1.00 7.64 O -ANISOU 699 O LEU A 138 965 1126 809 239 27 -263 O -ATOM 700 CB LEU A 138 33.222 34.901 25.751 1.00 6.43 C -ANISOU 700 CB LEU A 138 858 899 685 199 -45 -123 C -ATOM 701 CG LEU A 138 32.372 33.769 25.143 1.00 6.81 C -ANISOU 701 CG LEU A 138 927 879 780 159 40 -161 C -ATOM 702 CD1 LEU A 138 31.374 34.259 24.092 1.00 7.37 C -ANISOU 702 CD1 LEU A 138 979 930 891 145 -84 -103 C -ATOM 703 CD2 LEU A 138 33.283 32.694 24.548 1.00 7.04 C -ANISOU 703 CD2 LEU A 138 1021 887 766 116 54 -197 C -ATOM 704 N ASN A 139 32.022 35.227 28.615 1.00 7.69 N -ANISOU 704 N ASN A 139 990 1016 913 249 29 -185 N -ATOM 705 CA ASN A 139 31.179 34.725 29.696 1.00 8.88 C -ANISOU 705 CA ASN A 139 1173 1186 1012 204 22 -88 C -ATOM 706 C ASN A 139 30.121 35.733 30.110 1.00 8.26 C -ANISOU 706 C ASN A 139 1054 1174 907 167 58 -117 C -ATOM 707 O ASN A 139 28.970 35.381 30.359 1.00 8.97 O -ANISOU 707 O ASN A 139 1168 1339 899 215 50 -140 O -ATOM 708 CB ASN A 139 32.006 34.325 30.910 1.00 10.53 C -ANISOU 708 CB ASN A 139 1375 1394 1229 271 51 -31 C -ATOM 709 CG ASN A 139 31.258 33.343 31.811 1.00 13.85 C -ANISOU 709 CG ASN A 139 1751 2062 1449 361 64 100 C -ATOM 710 OD1 ASN A 139 30.800 32.294 31.358 1.00 20.46 O -ANISOU 710 OD1 ASN A 139 2758 2619 2394 123 682 542 O -ATOM 711 ND2 ASN A 139 31.112 33.694 33.074 1.00 20.27 N -ANISOU 711 ND2 ASN A 139 2291 3187 2224 553 121 220 N -ATOM 712 N ASP A 140 30.510 36.993 30.192 1.00 8.25 N -ANISOU 712 N ASP A 140 1059 1174 902 242 64 -140 N -ATOM 713 CA ASP A 140 29.551 38.021 30.568 1.00 8.96 C -ANISOU 713 CA ASP A 140 1146 1155 1100 170 37 -180 C -ATOM 714 C ASP A 140 28.439 38.145 29.539 1.00 9.09 C -ANISOU 714 C ASP A 140 1122 1216 1112 171 1 -166 C -ATOM 715 O ASP A 140 27.270 38.315 29.896 1.00 9.58 O -ANISOU 715 O ASP A 140 1123 1333 1183 271 5 -355 O -ATOM 716 CB ASP A 140 30.250 39.360 30.716 1.00 9.99 C -ANISOU 716 CB ASP A 140 1231 1293 1269 160 -25 -140 C -ATOM 717 CG ASP A 140 30.991 39.498 32.014 1.00 13.07 C -ANISOU 717 CG ASP A 140 1784 1496 1686 106 -52 -50 C -ATOM 718 OD1 ASP A 140 30.782 38.718 32.969 1.00 15.69 O -ANISOU 718 OD1 ASP A 140 2163 2109 1690 34 -249 -128 O -ATOM 719 OD2 ASP A 140 31.827 40.389 32.153 1.00 17.33 O -ANISOU 719 OD2 ASP A 140 2204 1925 2455 -190 -365 -325 O -ATOM 720 N LEU A 141 28.796 38.069 28.259 1.00 8.34 N -ANISOU 720 N LEU A 141 1011 1180 977 292 -12 -217 N -ATOM 721 CA LEU A 141 27.812 38.139 27.185 1.00 8.76 C -ANISOU 721 CA LEU A 141 1087 1213 1026 243 -19 -161 C -ATOM 722 C LEU A 141 26.823 37.001 27.301 1.00 8.61 C -ANISOU 722 C LEU A 141 1060 1255 953 263 -37 -178 C -ATOM 723 O LEU A 141 25.617 37.197 27.147 1.00 9.66 O -ANISOU 723 O LEU A 141 1096 1453 1121 378 -44 -343 O -ATOM 724 CB LEU A 141 28.499 38.093 25.821 1.00 9.23 C -ANISOU 724 CB LEU A 141 1102 1335 1069 219 -157 -126 C -ATOM 725 CG LEU A 141 29.283 39.331 25.386 1.00 11.63 C -ANISOU 725 CG LEU A 141 1490 1619 1306 209 -148 -50 C -ATOM 726 CD1 LEU A 141 30.194 39.025 24.181 1.00 13.38 C -ANISOU 726 CD1 LEU A 141 1771 1829 1482 -32 -113 175 C -ATOM 727 CD2 LEU A 141 28.340 40.495 25.079 1.00 15.02 C -ANISOU 727 CD2 LEU A 141 1973 1769 1965 147 -42 -3 C -ATOM 728 N LEU A 142 27.332 35.794 27.521 1.00 7.77 N -ANISOU 728 N LEU A 142 962 1149 841 285 42 -217 N -ATOM 729 CA LEU A 142 26.488 34.618 27.594 1.00 8.97 C -ANISOU 729 CA LEU A 142 1106 1236 1066 155 -4 -128 C -ATOM 730 C LEU A 142 25.557 34.697 28.794 1.00 8.89 C -ANISOU 730 C LEU A 142 1069 1265 1042 94 39 -117 C -ATOM 731 O LEU A 142 24.374 34.409 28.687 1.00 9.44 O -ANISOU 731 O LEU A 142 987 1395 1203 191 74 -190 O -ATOM 732 CB LEU A 142 27.364 33.370 27.690 1.00 9.17 C -ANISOU 732 CB LEU A 142 1106 1201 1176 162 110 -143 C -ATOM 733 CG LEU A 142 28.029 32.967 26.382 1.00 12.44 C -ANISOU 733 CG LEU A 142 1544 1584 1596 100 50 -30 C -ATOM 734 CD1 LEU A 142 29.111 31.926 26.614 1.00 13.30 C -ANISOU 734 CD1 LEU A 142 1611 1711 1729 164 142 -6 C -ATOM 735 CD2 LEU A 142 27.012 32.481 25.363 1.00 14.86 C -ANISOU 735 CD2 LEU A 142 1864 1925 1855 106 53 -209 C -ATOM 736 N LYS A 143 26.086 35.071 29.945 1.00 8.72 N -ANISOU 736 N LYS A 143 961 1298 1051 96 37 -152 N -ATOM 737 CA LYS A 143 25.247 35.179 31.129 1.00 9.43 C -ANISOU 737 CA LYS A 143 1066 1342 1175 61 92 -77 C -ATOM 738 C LYS A 143 24.135 36.190 30.945 1.00 9.12 C -ANISOU 738 C LYS A 143 984 1354 1128 68 80 -143 C -ATOM 739 O LYS A 143 22.986 35.947 31.315 1.00 9.79 O -ANISOU 739 O LYS A 143 988 1465 1265 111 167 -130 O -ATOM 740 CB LYS A 143 26.070 35.573 32.358 1.00 10.87 C -ANISOU 740 CB LYS A 143 1179 1619 1331 89 93 -91 C -ATOM 741 CG LYS A 143 26.927 34.449 32.895 1.00 12.50 C -ANISOU 741 CG LYS A 143 1533 1824 1388 50 20 -26 C -ATOM 742 CD LYS A 143 27.774 34.808 34.134 1.00 17.01 C -ANISOU 742 CD LYS A 143 2088 2316 2057 95 -169 48 C -ATOM 743 CE LYS A 143 27.219 35.909 35.031 1.00 20.35 C -ANISOU 743 CE LYS A 143 2584 2720 2428 4 -127 -29 C -ATOM 744 NZ LYS A 143 28.290 36.404 35.958 1.00 22.49 N -ANISOU 744 NZ LYS A 143 2937 2991 2614 -99 -245 -156 N -ATOM 745 N GLN A 144 24.477 37.338 30.380 1.00 9.33 N -ANISOU 745 N GLN A 144 1043 1271 1229 176 127 -218 N -ATOM 746 CA GLN A 144 23.484 38.386 30.173 1.00 9.90 C -ANISOU 746 CA GLN A 144 1155 1292 1312 188 87 -184 C -ATOM 747 C GLN A 144 22.413 37.949 29.185 1.00 9.92 C -ANISOU 747 C GLN A 144 1078 1385 1304 201 103 -194 C -ATOM 748 O GLN A 144 21.219 38.112 29.441 1.00 10.62 O -ANISOU 748 O GLN A 144 1012 1630 1392 317 161 -325 O -ATOM 749 CB GLN A 144 24.165 39.648 29.681 1.00 11.12 C -ANISOU 749 CB GLN A 144 1309 1399 1515 184 52 -207 C -ATOM 750 CG GLN A 144 23.252 40.863 29.651 1.00 16.66 C -ANISOU 750 CG GLN A 144 2012 2066 2250 86 28 -87 C -ATOM 751 CD GLN A 144 23.946 42.124 29.165 1.00 22.47 C -ANISOU 751 CD GLN A 144 2699 2831 3005 195 227 -4 C -ATOM 752 OE1 GLN A 144 25.029 42.061 28.571 1.00 28.37 O -ANISOU 752 OE1 GLN A 144 3389 3601 3789 163 316 46 O -ATOM 753 NE2 GLN A 144 23.322 43.274 29.408 1.00 27.03 N -ANISOU 753 NE2 GLN A 144 3252 3437 3579 208 129 27 N -ATOM 754 N LYS A 145 22.831 37.399 28.051 1.00 9.15 N -ANISOU 754 N LYS A 145 1060 1301 1112 139 66 -192 N -ATOM 755 CA LYS A 145 21.873 37.049 27.008 1.00 9.55 C -ANISOU 755 CA LYS A 145 1132 1332 1164 156 23 -43 C -ATOM 756 C LYS A 145 20.959 35.892 27.422 1.00 9.49 C -ANISOU 756 C LYS A 145 1164 1314 1124 123 -50 11 C -ATOM 757 O LYS A 145 19.757 35.942 27.177 1.00 10.14 O -ANISOU 757 O LYS A 145 1206 1380 1266 194 -106 81 O -ATOM 758 CB LYS A 145 22.595 36.735 25.699 1.00 10.92 C -ANISOU 758 CB LYS A 145 1366 1550 1233 111 15 -53 C -ATOM 759 CG LYS A 145 23.169 37.962 25.020 1.00 14.73 C -ANISOU 759 CG LYS A 145 1803 1985 1809 121 59 -49 C -ATOM 760 CD LYS A 145 22.061 38.815 24.385 1.00 20.01 C -ANISOU 760 CD LYS A 145 2493 2593 2517 78 122 65 C -ATOM 761 CE LYS A 145 22.383 39.270 22.975 1.00 23.04 C -ANISOU 761 CE LYS A 145 2886 2963 2905 20 2 32 C -ATOM 762 NZ LYS A 145 21.226 39.984 22.373 1.00 24.54 N -ANISOU 762 NZ LYS A 145 2974 3091 3259 -4 -10 42 N -ATOM 763 N TYR A 146 21.526 34.871 28.057 1.00 9.20 N -ANISOU 763 N TYR A 146 1065 1160 1268 145 -77 31 N -ATOM 764 CA TYR A 146 20.797 33.655 28.402 1.00 9.85 C -ANISOU 764 CA TYR A 146 1162 1262 1318 78 -141 36 C -ATOM 765 C TYR A 146 20.220 33.676 29.806 1.00 9.54 C -ANISOU 765 C TYR A 146 1083 1241 1298 17 -142 61 C -ATOM 766 O TYR A 146 19.592 32.711 30.224 1.00 10.17 O -ANISOU 766 O TYR A 146 1163 1369 1332 -73 -249 166 O -ATOM 767 CB TYR A 146 21.712 32.449 28.204 1.00 10.46 C -ANISOU 767 CB TYR A 146 1155 1331 1489 169 -223 65 C -ATOM 768 CG TYR A 146 21.706 32.017 26.793 1.00 12.50 C -ANISOU 768 CG TYR A 146 1508 1450 1789 250 -298 58 C -ATOM 769 CD1 TYR A 146 20.689 31.196 26.327 1.00 13.87 C -ANISOU 769 CD1 TYR A 146 1512 1755 2003 297 -288 -340 C -ATOM 770 CD2 TYR A 146 22.652 32.468 25.904 1.00 13.89 C -ANISOU 770 CD2 TYR A 146 1901 1620 1755 152 -200 -78 C -ATOM 771 CE1 TYR A 146 20.622 30.791 25.045 1.00 17.29 C -ANISOU 771 CE1 TYR A 146 2256 2171 2139 317 -319 -203 C -ATOM 772 CE2 TYR A 146 22.596 32.067 24.577 1.00 16.58 C -ANISOU 772 CE2 TYR A 146 2421 2007 1870 169 -257 -30 C -ATOM 773 CZ TYR A 146 21.550 31.230 24.158 1.00 14.69 C -ANISOU 773 CZ TYR A 146 2195 1796 1590 302 -330 -265 C -ATOM 774 OH TYR A 146 21.427 30.773 22.869 1.00 20.44 O -ANISOU 774 OH TYR A 146 2925 2664 2178 500 -350 -390 O -ATOM 775 N GLY A 147 20.382 34.783 30.533 1.00 9.87 N -ANISOU 775 N GLY A 147 1170 1332 1247 64 -39 -27 N -ATOM 776 CA GLY A 147 19.760 34.911 31.843 1.00 11.72 C -ANISOU 776 CA GLY A 147 1381 1589 1482 -21 -11 32 C -ATOM 777 C GLY A 147 20.317 33.930 32.860 1.00 11.96 C -ANISOU 777 C GLY A 147 1387 1678 1479 -32 12 105 C -ATOM 778 O GLY A 147 19.573 33.338 33.645 1.00 14.02 O -ANISOU 778 O GLY A 147 1488 2116 1723 13 -9 351 O -ATOM 779 N LEU A 148 21.634 33.755 32.833 1.00 12.33 N -ANISOU 779 N LEU A 148 1481 1704 1498 45 -57 124 N -ATOM 780 CA LEU A 148 22.315 32.805 33.699 1.00 13.21 C -ANISOU 780 CA LEU A 148 1637 1783 1598 -7 -45 92 C -ATOM 781 C LEU A 148 23.043 33.542 34.822 1.00 13.34 C -ANISOU 781 C LEU A 148 1670 1912 1485 37 0 46 C -ATOM 782 O LEU A 148 23.757 34.504 34.578 1.00 14.39 O -ANISOU 782 O LEU A 148 1863 2164 1440 -70 -52 115 O -ATOM 783 CB LEU A 148 23.308 32.007 32.874 1.00 13.24 C -ANISOU 783 CB LEU A 148 1638 1742 1649 25 -128 39 C -ATOM 784 CG LEU A 148 22.738 31.345 31.623 1.00 13.77 C -ANISOU 784 CG LEU A 148 1783 1740 1707 5 -232 88 C -ATOM 785 CD1 LEU A 148 23.872 30.706 30.851 1.00 14.42 C -ANISOU 785 CD1 LEU A 148 1950 1766 1763 55 -258 36 C -ATOM 786 CD2 LEU A 148 21.679 30.327 31.985 1.00 15.46 C -ANISOU 786 CD2 LEU A 148 1824 1926 2123 94 -174 100 C -ATOM 787 N SER A 149 22.851 33.110 36.065 1.00 14.64 N -ANISOU 787 N SER A 149 1824 2091 1644 28 56 8 N -ATOM 788 CA SER A 149 23.582 33.722 37.180 1.00 15.91 C -ANISOU 788 CA SER A 149 2025 2193 1824 68 71 -74 C -ATOM 789 C SER A 149 25.016 33.220 37.239 1.00 15.74 C -ANISOU 789 C SER A 149 2026 2166 1786 69 28 -75 C -ATOM 790 O SER A 149 25.906 33.933 37.695 1.00 16.72 O -ANISOU 790 O SER A 149 2079 2355 1917 137 31 -236 O -ATOM 791 CB SER A 149 22.890 33.453 38.519 1.00 16.52 C -ANISOU 791 CB SER A 149 2113 2315 1849 68 114 -58 C -ATOM 792 OG SER A 149 22.665 32.072 38.720 1.00 20.31 O -ANISOU 792 OG SER A 149 2682 2906 2129 130 392 -4 O -ATOM 793 N ARG A 150 25.221 31.999 36.748 1.00 15.50 N -ANISOU 793 N ARG A 150 2008 2188 1694 145 47 -118 N -ATOM 794 CA ARG A 150 26.490 31.295 36.843 1.00 16.14 C -ANISOU 794 CA ARG A 150 2073 2187 1872 90 25 -114 C -ATOM 795 C ARG A 150 26.639 30.363 35.652 1.00 14.93 C -ANISOU 795 C ARG A 150 1872 2105 1695 84 72 -179 C -ATOM 796 O ARG A 150 25.674 29.747 35.218 1.00 15.33 O -ANISOU 796 O ARG A 150 1783 2254 1786 95 161 -213 O -ATOM 797 CB ARG A 150 26.466 30.468 38.126 1.00 17.63 C -ANISOU 797 CB ARG A 150 2311 2338 2049 141 2 -95 C -ATOM 798 CG ARG A 150 27.762 29.931 38.658 1.00 21.93 C -ANISOU 798 CG ARG A 150 2832 2766 2733 47 51 -66 C -ATOM 799 CD ARG A 150 27.513 28.940 39.794 1.00 25.74 C -ANISOU 799 CD ARG A 150 3312 3255 3210 4 4 -1 C -ATOM 800 NE ARG A 150 26.772 27.784 39.287 1.00 29.19 N -ANISOU 800 NE ARG A 150 3770 3599 3719 -18 2 -7 N -ATOM 801 CZ ARG A 150 27.311 26.636 38.869 1.00 31.21 C -ANISOU 801 CZ ARG A 150 3973 3915 3969 5 46 -27 C -ATOM 802 NH1 ARG A 150 28.625 26.420 38.917 1.00 31.45 N -ANISOU 802 NH1 ARG A 150 4035 3979 3934 -26 88 18 N -ATOM 803 NH2 ARG A 150 26.515 25.677 38.414 1.00 32.28 N -ANISOU 803 NH2 ARG A 150 4139 4069 4056 -20 2 -57 N -ATOM 804 N VAL A 151 27.867 30.218 35.170 1.00 13.94 N -ANISOU 804 N VAL A 151 1731 1999 1564 72 105 -211 N -ATOM 805 CA VAL A 151 28.190 29.245 34.131 1.00 13.24 C -ANISOU 805 CA VAL A 151 1730 1830 1470 106 103 -81 C -ATOM 806 C VAL A 151 29.282 28.382 34.721 1.00 13.11 C -ANISOU 806 C VAL A 151 1733 1840 1406 121 192 -9 C -ATOM 807 O VAL A 151 30.386 28.861 34.915 1.00 14.71 O -ANISOU 807 O VAL A 151 1880 2189 1517 141 157 201 O -ATOM 808 CB VAL A 151 28.658 29.931 32.811 1.00 13.33 C -ANISOU 808 CB VAL A 151 1712 1843 1508 109 82 -70 C -ATOM 809 CG1 VAL A 151 29.171 28.898 31.808 1.00 13.35 C -ANISOU 809 CG1 VAL A 151 1903 1807 1361 209 172 37 C -ATOM 810 CG2 VAL A 151 27.533 30.745 32.208 1.00 14.29 C -ANISOU 810 CG2 VAL A 151 1816 1950 1661 101 68 -50 C -ATOM 811 N GLY A 152 28.970 27.123 35.014 1.00 12.98 N -ANISOU 811 N GLY A 152 1688 1855 1388 117 296 7 N -ATOM 812 CA GLY A 152 29.930 26.217 35.624 1.00 12.76 C -ANISOU 812 CA GLY A 152 1703 1827 1317 102 274 67 C -ATOM 813 C GLY A 152 31.217 26.079 34.810 1.00 11.91 C -ANISOU 813 C GLY A 152 1698 1717 1111 128 329 113 C -ATOM 814 O GLY A 152 32.314 26.148 35.350 1.00 12.35 O -ANISOU 814 O GLY A 152 1866 1862 964 235 418 190 O -ATOM 815 N ARG A 153 31.089 25.903 33.500 1.00 10.91 N -ANISOU 815 N ARG A 153 1489 1655 1001 146 369 130 N -ATOM 816 CA ARG A 153 32.245 25.756 32.624 1.00 9.81 C -ANISOU 816 CA ARG A 153 1337 1372 1016 114 299 99 C -ATOM 817 C ARG A 153 31.927 26.335 31.268 1.00 8.79 C -ANISOU 817 C ARG A 153 1242 1240 858 82 201 80 C -ATOM 818 O ARG A 153 30.934 25.977 30.666 1.00 9.93 O -ANISOU 818 O ARG A 153 1416 1430 926 -10 346 203 O -ATOM 819 CB ARG A 153 32.551 24.291 32.430 1.00 11.43 C -ANISOU 819 CB ARG A 153 1428 1533 1382 118 258 118 C -ATOM 820 CG ARG A 153 33.448 23.672 33.433 1.00 14.18 C -ANISOU 820 CG ARG A 153 1884 1923 1579 59 242 113 C -ATOM 821 CD ARG A 153 34.202 22.494 32.854 1.00 15.21 C -ANISOU 821 CD ARG A 153 1975 1883 1922 325 -67 34 C -ATOM 822 NE ARG A 153 33.289 21.370 32.815 1.00 14.87 N -ANISOU 822 NE ARG A 153 2082 1743 1823 422 -38 100 N -ATOM 823 CZ ARG A 153 33.487 20.223 32.189 1.00 14.70 C -ANISOU 823 CZ ARG A 153 2101 1803 1680 306 16 40 C -ATOM 824 NH1 ARG A 153 34.570 20.005 31.461 1.00 14.98 N -ANISOU 824 NH1 ARG A 153 1979 1849 1861 239 57 91 N -ATOM 825 NH2 ARG A 153 32.560 19.289 32.289 1.00 14.65 N -ANISOU 825 NH2 ARG A 153 2059 1712 1793 272 153 67 N -ATOM 826 N LEU A 154 32.793 27.225 30.811 1.00 7.68 N -ANISOU 826 N LEU A 154 1164 1036 716 58 180 57 N -ATOM 827 CA LEU A 154 32.731 27.797 29.465 1.00 7.08 C -ANISOU 827 CA LEU A 154 1099 1005 585 109 158 17 C -ATOM 828 C LEU A 154 33.976 27.334 28.740 1.00 6.84 C -ANISOU 828 C LEU A 154 1046 991 560 64 156 22 C -ATOM 829 O LEU A 154 35.084 27.477 29.252 1.00 7.39 O -ANISOU 829 O LEU A 154 1105 1165 536 156 189 -99 O -ATOM 830 CB LEU A 154 32.725 29.319 29.560 1.00 7.50 C -ANISOU 830 CB LEU A 154 1193 1014 642 62 211 70 C -ATOM 831 CG LEU A 154 32.873 30.090 28.246 1.00 7.93 C -ANISOU 831 CG LEU A 154 1275 1002 733 134 177 36 C -ATOM 832 CD1 LEU A 154 31.716 29.780 27.296 1.00 8.71 C -ANISOU 832 CD1 LEU A 154 1378 1074 855 158 133 103 C -ATOM 833 CD2 LEU A 154 32.968 31.599 28.534 1.00 9.02 C -ANISOU 833 CD2 LEU A 154 1334 1079 1014 83 79 42 C -ATOM 834 N VAL A 155 33.809 26.791 27.538 1.00 6.03 N -ANISOU 834 N VAL A 155 930 890 471 125 197 24 N -ATOM 835 CA VAL A 155 34.926 26.255 26.773 1.00 5.89 C -ANISOU 835 CA VAL A 155 844 881 511 53 151 63 C -ATOM 836 C VAL A 155 34.917 26.873 25.374 1.00 5.54 C -ANISOU 836 C VAL A 155 771 862 469 94 192 30 C -ATOM 837 O VAL A 155 33.995 26.650 24.604 1.00 6.53 O -ANISOU 837 O VAL A 155 772 1128 581 91 130 125 O -ATOM 838 CB VAL A 155 34.909 24.716 26.680 1.00 6.76 C -ANISOU 838 CB VAL A 155 1029 904 635 98 80 85 C -ATOM 839 CG1 VAL A 155 36.202 24.222 26.039 1.00 8.10 C -ANISOU 839 CG1 VAL A 155 1260 1126 692 236 151 96 C -ATOM 840 CG2 VAL A 155 34.719 24.094 28.047 1.00 7.70 C -ANISOU 840 CG2 VAL A 155 1085 1000 838 60 212 118 C -ATOM 841 N LEU A 156 35.971 27.620 25.072 1.00 5.42 N -ANISOU 841 N LEU A 156 750 814 493 44 114 54 N -ATOM 842 CA LEU A 156 36.210 28.228 23.773 1.00 4.94 C -ANISOU 842 CA LEU A 156 694 710 470 54 90 4 C -ATOM 843 C LEU A 156 37.316 27.429 23.090 1.00 4.52 C -ANISOU 843 C LEU A 156 641 635 439 99 4 26 C -ATOM 844 O LEU A 156 38.484 27.506 23.490 1.00 5.44 O -ANISOU 844 O LEU A 156 829 710 526 139 -5 -70 O -ATOM 845 CB LEU A 156 36.607 29.690 23.974 1.00 5.60 C -ANISOU 845 CB LEU A 156 732 807 588 108 78 56 C -ATOM 846 CG LEU A 156 37.126 30.467 22.762 1.00 5.93 C -ANISOU 846 CG LEU A 156 792 804 653 67 130 -111 C -ATOM 847 CD1 LEU A 156 36.117 30.508 21.646 1.00 7.16 C -ANISOU 847 CD1 LEU A 156 1129 980 611 -82 57 124 C -ATOM 848 CD2 LEU A 156 37.515 31.885 23.179 1.00 6.76 C -ANISOU 848 CD2 LEU A 156 1002 755 809 31 63 -128 C -ATOM 849 N ASN A 157 36.939 26.585 22.137 1.00 4.47 N -ANISOU 849 N ASN A 157 588 651 458 59 74 -15 N -ATOM 850 CA ASN A 157 37.900 25.754 21.439 1.00 4.44 C -ANISOU 850 CA ASN A 157 649 568 466 68 66 19 C -ATOM 851 C ASN A 157 38.314 26.397 20.134 1.00 4.28 C -ANISOU 851 C ASN A 157 649 544 430 64 25 -33 C -ATOM 852 O ASN A 157 37.515 27.024 19.426 1.00 5.13 O -ANISOU 852 O ASN A 157 635 718 595 144 84 12 O -ATOM 853 CB ASN A 157 37.338 24.354 21.156 1.00 5.45 C -ANISOU 853 CB ASN A 157 838 690 542 19 110 61 C -ATOM 854 CG ASN A 157 37.386 23.438 22.362 1.00 6.41 C -ANISOU 854 CG ASN A 157 1076 641 718 47 147 9 C -ATOM 855 OD1 ASN A 157 36.355 23.029 22.888 1.00 7.57 O -ANISOU 855 OD1 ASN A 157 1211 775 888 -13 142 212 O -ATOM 856 ND2 ASN A 157 38.584 23.089 22.788 1.00 7.23 N -ANISOU 856 ND2 ASN A 157 1130 693 921 124 26 144 N -ATOM 857 N GLY A 158 39.575 26.223 19.792 1.00 4.11 N -ANISOU 857 N GLY A 158 596 505 459 92 13 -1 N -ATOM 858 CA GLY A 158 40.106 26.724 18.551 1.00 4.46 C -ANISOU 858 CA GLY A 158 607 560 525 70 49 -53 C -ATOM 859 C GLY A 158 41.468 26.157 18.254 1.00 4.13 C -ANISOU 859 C GLY A 158 592 458 519 46 -2 43 C -ATOM 860 O GLY A 158 41.892 25.186 18.866 1.00 5.49 O -ANISOU 860 O GLY A 158 703 948 434 193 135 64 O -ATOM 861 N GLU A 159 42.113 26.744 17.262 1.00 4.62 N -ANISOU 861 N GLU A 159 601 447 705 77 76 -1 N -ATOM 862 CA GLU A 159 43.398 26.297 16.776 1.00 4.24 C -ANISOU 862 CA GLU A 159 521 473 617 19 106 -54 C -ATOM 863 C GLU A 159 44.436 27.375 17.118 1.00 4.08 C -ANISOU 863 C GLU A 159 533 388 628 50 146 -15 C -ATOM 864 O GLU A 159 44.274 28.539 16.738 1.00 5.04 O -ANISOU 864 O GLU A 159 601 484 831 34 94 18 O -ATOM 865 CB GLU A 159 43.357 26.097 15.255 1.00 4.81 C -ANISOU 865 CB GLU A 159 608 458 759 22 37 -64 C -ATOM 866 CG GLU A 159 44.491 25.209 14.746 1.00 4.82 C -ANISOU 866 CG GLU A 159 643 598 590 53 78 -68 C -ATOM 867 CD GLU A 159 44.255 23.724 14.943 1.00 5.04 C -ANISOU 867 CD GLU A 159 680 574 660 41 189 -167 C -ATOM 868 OE1 GLU A 159 43.231 23.336 15.565 1.00 5.75 O -ANISOU 868 OE1 GLU A 159 692 603 889 22 190 -110 O -ATOM 869 OE2 GLU A 159 45.100 22.944 14.442 1.00 5.39 O -ANISOU 869 OE2 GLU A 159 708 557 779 73 78 -146 O -ATOM 870 N LEU A 160 45.512 26.994 17.809 1.00 4.36 N -ANISOU 870 N LEU A 160 617 444 595 14 61 48 N -ATOM 871 CA LEU A 160 46.659 27.846 18.004 1.00 4.34 C -ANISOU 871 CA LEU A 160 646 474 529 10 -1 -35 C -ATOM 872 C LEU A 160 47.510 27.688 16.759 1.00 4.36 C -ANISOU 872 C LEU A 160 527 468 662 -37 14 -10 C -ATOM 873 O LEU A 160 47.818 26.562 16.386 1.00 4.99 O -ANISOU 873 O LEU A 160 679 511 706 17 47 -114 O -ATOM 874 CB LEU A 160 47.418 27.418 19.261 1.00 5.25 C -ANISOU 874 CB LEU A 160 761 590 640 16 31 4 C -ATOM 875 CG LEU A 160 48.573 28.325 19.641 1.00 6.13 C -ANISOU 875 CG LEU A 160 848 750 728 3 -78 -76 C -ATOM 876 CD1 LEU A 160 48.077 29.633 20.255 1.00 8.44 C -ANISOU 876 CD1 LEU A 160 1196 963 1045 -34 -281 -68 C -ATOM 877 CD2 LEU A 160 49.487 27.609 20.622 1.00 7.53 C -ANISOU 877 CD2 LEU A 160 1092 875 892 -22 -164 -154 C -ATOM 878 N PHE A 161 47.880 28.783 16.109 1.00 4.43 N -ANISOU 878 N PHE A 161 603 521 558 5 28 -149 N -ATOM 879 CA PHE A 161 48.520 28.686 14.803 1.00 4.57 C -ANISOU 879 CA PHE A 161 602 566 566 12 17 -40 C -ATOM 880 C PHE A 161 49.470 29.848 14.572 1.00 4.40 C -ANISOU 880 C PHE A 161 571 552 548 28 60 -34 C -ATOM 881 O PHE A 161 49.467 30.843 15.289 1.00 4.89 O -ANISOU 881 O PHE A 161 646 602 609 -47 114 -74 O -ATOM 882 CB PHE A 161 47.470 28.598 13.676 1.00 4.76 C -ANISOU 882 CB PHE A 161 667 588 553 -1 40 -51 C -ATOM 883 CG PHE A 161 46.759 29.892 13.374 1.00 4.71 C -ANISOU 883 CG PHE A 161 629 684 473 -64 10 -4 C -ATOM 884 CD1 PHE A 161 47.172 30.694 12.326 1.00 6.14 C -ANISOU 884 CD1 PHE A 161 857 955 518 168 153 82 C -ATOM 885 CD2 PHE A 161 45.676 30.319 14.130 1.00 4.51 C -ANISOU 885 CD2 PHE A 161 592 533 588 -57 98 -51 C -ATOM 886 CE1 PHE A 161 46.505 31.868 12.005 1.00 7.13 C -ANISOU 886 CE1 PHE A 161 983 1035 690 129 206 296 C -ATOM 887 CE2 PHE A 161 45.016 31.493 13.827 1.00 5.32 C -ANISOU 887 CE2 PHE A 161 623 728 668 -45 61 -27 C -ATOM 888 CZ PHE A 161 45.428 32.269 12.761 1.00 5.93 C -ANISOU 888 CZ PHE A 161 730 841 680 78 154 115 C -ATOM 889 N GLY A 162 50.253 29.706 13.517 1.00 4.75 N -ANISOU 889 N GLY A 162 647 605 553 -16 38 29 N -ATOM 890 CA GLY A 162 51.142 30.763 13.090 1.00 5.04 C -ANISOU 890 CA GLY A 162 632 658 621 33 47 85 C -ATOM 891 C GLY A 162 52.583 30.559 13.483 1.00 4.90 C -ANISOU 891 C GLY A 162 648 627 585 25 15 114 C -ATOM 892 O GLY A 162 53.076 29.439 13.562 1.00 5.37 O -ANISOU 892 O GLY A 162 680 515 842 35 28 127 O -ATOM 893 N ALA A 163 53.268 31.674 13.690 1.00 5.47 N -ANISOU 893 N ALA A 163 700 617 761 -9 -7 127 N -ATOM 894 CA ALA A 163 54.698 31.727 13.990 1.00 6.11 C -ANISOU 894 CA ALA A 163 717 737 866 -35 -10 135 C -ATOM 895 C ALA A 163 55.544 31.086 12.892 1.00 5.70 C -ANISOU 895 C ALA A 163 679 682 804 -53 -18 178 C -ATOM 896 O ALA A 163 56.596 30.512 13.144 1.00 6.58 O -ANISOU 896 O ALA A 163 714 741 1042 -18 -114 115 O -ATOM 897 CB ALA A 163 54.994 31.162 15.378 1.00 6.60 C -ANISOU 897 CB ALA A 163 802 891 813 -75 3 24 C -ATOM 898 N LYS A 164 55.104 31.241 11.644 1.00 5.70 N -ANISOU 898 N LYS A 164 629 742 791 -30 -11 209 N -ATOM 899 CA LYS A 164 55.882 30.826 10.477 1.00 6.12 C -ANISOU 899 CA LYS A 164 711 720 891 9 32 161 C -ATOM 900 C LYS A 164 55.351 31.544 9.254 1.00 5.51 C -ANISOU 900 C LYS A 164 669 626 799 -22 106 192 C -ATOM 901 O LYS A 164 54.186 31.405 8.917 1.00 5.81 O -ANISOU 901 O LYS A 164 650 751 804 -45 166 160 O -ATOM 902 CB LYS A 164 55.801 29.314 10.266 1.00 6.71 C -ANISOU 902 CB LYS A 164 799 785 964 54 35 254 C -ATOM 903 CG LYS A 164 56.576 28.818 9.031 1.00 8.60 C -ANISOU 903 CG LYS A 164 1063 914 1290 66 70 271 C -ATOM 904 CD LYS A 164 56.468 27.308 8.790 1.00 11.35 C -ANISOU 904 CD LYS A 164 1538 1267 1506 200 122 93 C -ATOM 905 CE LYS A 164 57.221 26.868 7.551 1.00 14.30 C -ANISOU 905 CE LYS A 164 1933 1537 1962 203 -61 -38 C -ATOM 906 NZ LYS A 164 57.214 25.386 7.381 1.00 16.78 N -ANISOU 906 NZ LYS A 164 2171 1767 2436 232 -95 -166 N -ATOM 907 N TYR A 165 56.218 32.278 8.563 1.00 6.02 N -ANISOU 907 N TYR A 165 663 736 889 -31 35 268 N -ATOM 908 CA TYR A 165 55.830 32.906 7.305 1.00 5.96 C -ANISOU 908 CA TYR A 165 734 726 801 -17 7 152 C -ATOM 909 C TYR A 165 57.102 33.250 6.543 1.00 6.16 C -ANISOU 909 C TYR A 165 887 649 801 -42 22 213 C -ATOM 910 O TYR A 165 57.720 34.292 6.779 1.00 7.12 O -ANISOU 910 O TYR A 165 954 806 943 -230 -39 231 O -ATOM 911 CB TYR A 165 54.962 34.144 7.528 1.00 6.32 C -ANISOU 911 CB TYR A 165 846 764 788 39 44 145 C -ATOM 912 CG TYR A 165 54.187 34.508 6.293 1.00 5.81 C -ANISOU 912 CG TYR A 165 769 643 794 58 80 213 C -ATOM 913 CD1 TYR A 165 52.976 33.902 6.023 1.00 6.02 C -ANISOU 913 CD1 TYR A 165 749 703 832 15 179 279 C -ATOM 914 CD2 TYR A 165 54.674 35.425 5.367 1.00 6.39 C -ANISOU 914 CD2 TYR A 165 747 712 968 -35 -21 247 C -ATOM 915 CE1 TYR A 165 52.254 34.211 4.892 1.00 6.30 C -ANISOU 915 CE1 TYR A 165 702 675 1015 -74 43 277 C -ATOM 916 CE2 TYR A 165 53.964 35.734 4.239 1.00 6.21 C -ANISOU 916 CE2 TYR A 165 759 672 927 -80 82 304 C -ATOM 917 CZ TYR A 165 52.745 35.134 4.002 1.00 5.60 C -ANISOU 917 CZ TYR A 165 644 633 848 -12 78 226 C -ATOM 918 OH TYR A 165 52.013 35.422 2.871 1.00 6.88 O -ANISOU 918 OH TYR A 165 829 908 878 -91 -65 297 O -ATOM 919 N LYS A 166 57.500 32.377 5.633 1.00 6.45 N -ANISOU 919 N LYS A 166 761 759 928 -76 108 200 N -ATOM 920 CA LYS A 166 58.833 32.445 5.045 1.00 7.62 C -ANISOU 920 CA LYS A 166 933 886 1074 41 129 201 C -ATOM 921 C LYS A 166 58.873 33.338 3.812 1.00 7.29 C -ANISOU 921 C LYS A 166 978 812 979 -1 210 260 C -ATOM 922 O LYS A 166 59.074 32.889 2.688 1.00 9.59 O -ANISOU 922 O LYS A 166 1551 965 1125 30 115 298 O -ATOM 923 CB LYS A 166 59.318 31.032 4.731 1.00 8.54 C -ANISOU 923 CB LYS A 166 909 1028 1306 36 225 258 C -ATOM 924 CG LYS A 166 59.532 30.172 5.967 1.00 13.17 C -ANISOU 924 CG LYS A 166 1520 1573 1910 63 142 116 C -ATOM 925 CD LYS A 166 59.994 28.757 5.625 1.00 17.90 C -ANISOU 925 CD LYS A 166 2249 2161 2388 74 66 127 C -ATOM 926 CE LYS A 166 61.454 28.711 5.216 1.00 21.76 C -ANISOU 926 CE LYS A 166 2737 2642 2885 121 94 51 C -ATOM 927 NZ LYS A 166 61.883 27.319 4.891 1.00 23.52 N -ANISOU 927 NZ LYS A 166 3019 2798 3119 86 119 -51 N -ATOM 928 N HIS A 167 58.687 34.626 4.037 1.00 7.89 N -ANISOU 928 N HIS A 167 1184 851 961 9 253 225 N -ATOM 929 CA HIS A 167 58.818 35.647 2.997 1.00 7.31 C -ANISOU 929 CA HIS A 167 1034 818 923 -32 187 256 C -ATOM 930 C HIS A 167 59.863 36.638 3.462 1.00 7.93 C -ANISOU 930 C HIS A 167 1085 939 989 -21 214 388 C -ATOM 931 O HIS A 167 59.816 37.080 4.607 1.00 8.60 O -ANISOU 931 O HIS A 167 1139 981 1147 -67 136 377 O -ATOM 932 CB HIS A 167 57.490 36.361 2.794 1.00 7.32 C -ANISOU 932 CB HIS A 167 1035 818 929 -134 214 211 C -ATOM 933 CG HIS A 167 57.449 37.225 1.580 1.00 6.97 C -ANISOU 933 CG HIS A 167 879 745 1023 -144 143 267 C -ATOM 934 ND1 HIS A 167 58.188 38.380 1.463 1.00 7.93 N -ANISOU 934 ND1 HIS A 167 985 873 1153 -74 64 265 N -ATOM 935 CD2 HIS A 167 56.758 37.086 0.425 1.00 7.78 C -ANISOU 935 CD2 HIS A 167 1016 832 1106 -148 162 121 C -ATOM 936 CE1 HIS A 167 57.937 38.921 0.287 1.00 7.91 C -ANISOU 936 CE1 HIS A 167 1056 1004 945 -117 -27 411 C -ATOM 937 NE2 HIS A 167 57.070 38.164 -0.360 1.00 8.24 N -ANISOU 937 NE2 HIS A 167 1179 888 1064 90 139 235 N -ATOM 938 N PRO A 168 60.808 37.014 2.593 1.00 8.59 N -ANISOU 938 N PRO A 168 1069 1039 1155 33 151 261 N -ATOM 939 CA PRO A 168 61.913 37.873 3.023 1.00 9.49 C -ANISOU 939 CA PRO A 168 1120 1213 1270 -59 72 328 C -ATOM 940 C PRO A 168 61.504 39.276 3.476 1.00 9.50 C -ANISOU 940 C PRO A 168 1107 1176 1324 -107 41 308 C -ATOM 941 O PRO A 168 62.281 39.949 4.142 1.00 11.25 O -ANISOU 941 O PRO A 168 1228 1334 1710 -148 -108 373 O -ATOM 942 CB PRO A 168 62.822 37.933 1.786 1.00 10.48 C -ANISOU 942 CB PRO A 168 1134 1331 1515 -6 169 256 C -ATOM 943 CG PRO A 168 61.959 37.576 0.672 1.00 10.90 C -ANISOU 943 CG PRO A 168 1285 1432 1422 -1 235 241 C -ATOM 944 CD PRO A 168 60.958 36.589 1.193 1.00 9.10 C -ANISOU 944 CD PRO A 168 1085 1192 1181 23 245 253 C -ATOM 945 N LEU A 169 60.311 39.734 3.120 1.00 8.31 N -ANISOU 945 N LEU A 169 1007 1020 1128 -84 45 311 N -ATOM 946 CA LEU A 169 59.836 41.040 3.570 1.00 8.41 C -ANISOU 946 CA LEU A 169 1103 975 1116 -104 24 186 C -ATOM 947 C LEU A 169 59.017 40.970 4.856 1.00 8.86 C -ANISOU 947 C LEU A 169 1270 970 1126 -66 -4 177 C -ATOM 948 O LEU A 169 58.486 41.987 5.300 1.00 10.19 O -ANISOU 948 O LEU A 169 1600 1081 1190 13 52 228 O -ATOM 949 CB LEU A 169 59.023 41.723 2.467 1.00 8.31 C -ANISOU 949 CB LEU A 169 1075 925 1156 -191 31 248 C -ATOM 950 CG LEU A 169 59.792 41.953 1.178 1.00 8.27 C -ANISOU 950 CG LEU A 169 974 959 1208 -93 164 302 C -ATOM 951 CD1 LEU A 169 58.910 42.692 0.185 1.00 7.88 C -ANISOU 951 CD1 LEU A 169 1003 912 1079 -132 127 289 C -ATOM 952 CD2 LEU A 169 61.095 42.704 1.371 1.00 9.21 C -ANISOU 952 CD2 LEU A 169 1136 1133 1228 -129 64 442 C -ATOM 953 N VAL A 170 58.907 39.776 5.443 1.00 8.07 N -ANISOU 953 N VAL A 170 1082 960 1021 -120 51 216 N -ATOM 954 CA VAL A 170 58.132 39.565 6.643 1.00 8.21 C -ANISOU 954 CA VAL A 170 1062 1044 1013 -71 71 174 C -ATOM 955 C VAL A 170 59.086 39.053 7.713 1.00 8.68 C -ANISOU 955 C VAL A 170 1150 1094 1054 -206 36 182 C -ATOM 956 O VAL A 170 59.393 37.872 7.771 1.00 8.96 O -ANISOU 956 O VAL A 170 1062 1212 1131 -11 49 233 O -ATOM 957 CB VAL A 170 57.001 38.572 6.386 1.00 7.62 C -ANISOU 957 CB VAL A 170 1017 952 925 -62 77 162 C -ATOM 958 CG1 VAL A 170 56.176 38.354 7.649 1.00 8.07 C -ANISOU 958 CG1 VAL A 170 1034 1152 880 -45 67 191 C -ATOM 959 CG2 VAL A 170 56.118 39.071 5.248 1.00 6.96 C -ANISOU 959 CG2 VAL A 170 989 871 784 -95 177 191 C -ATOM 960 N PRO A 171 59.616 39.942 8.543 1.00 9.76 N -ANISOU 960 N PRO A 171 1319 1254 1135 -285 -42 217 N -ATOM 961 CA PRO A 171 60.525 39.500 9.599 1.00 10.36 C -ANISOU 961 CA PRO A 171 1326 1357 1250 -253 -15 182 C -ATOM 962 C PRO A 171 59.898 38.469 10.522 1.00 9.70 C -ANISOU 962 C PRO A 171 1218 1289 1178 -285 -15 214 C -ATOM 963 O PRO A 171 58.702 38.505 10.796 1.00 9.84 O -ANISOU 963 O PRO A 171 1263 1355 1120 -304 -4 243 O -ATOM 964 CB PRO A 171 60.825 40.794 10.357 1.00 11.81 C -ANISOU 964 CB PRO A 171 1562 1527 1398 -282 -59 168 C -ATOM 965 CG PRO A 171 60.617 41.873 9.351 1.00 12.29 C -ANISOU 965 CG PRO A 171 1581 1571 1516 -243 -32 132 C -ATOM 966 CD PRO A 171 59.460 41.410 8.533 1.00 10.90 C -ANISOU 966 CD PRO A 171 1542 1391 1207 -302 -98 155 C -ATOM 967 N LYS A 172 60.722 37.567 11.011 1.00 10.05 N -ANISOU 967 N LYS A 172 1211 1369 1238 -219 36 184 N -ATOM 968 CA LYS A 172 60.276 36.701 12.083 1.00 10.08 C -ANISOU 968 CA LYS A 172 1298 1304 1228 -161 -14 150 C -ATOM 969 C LYS A 172 59.886 37.539 13.303 1.00 9.08 C -ANISOU 969 C LYS A 172 1208 1138 1102 -205 -127 136 C -ATOM 970 O LYS A 172 60.333 38.681 13.476 1.00 9.92 O -ANISOU 970 O LYS A 172 1337 1244 1186 -376 -140 145 O -ATOM 971 CB LYS A 172 61.338 35.656 12.436 1.00 11.58 C -ANISOU 971 CB LYS A 172 1419 1519 1461 -83 -16 86 C -ATOM 972 CG LYS A 172 61.605 34.672 11.313 1.00 13.66 C -ANISOU 972 CG LYS A 172 1667 1910 1611 -50 55 93 C -ATOM 973 CD LYS A 172 62.384 33.454 11.751 1.00 16.99 C -ANISOU 973 CD LYS A 172 2151 2189 2116 -22 21 -48 C -ATOM 974 CE LYS A 172 61.490 32.415 12.416 1.00 18.27 C -ANISOU 974 CE LYS A 172 2336 2281 2325 24 -18 52 C -ATOM 975 NZ LYS A 172 62.228 31.163 12.739 1.00 19.99 N -ANISOU 975 NZ LYS A 172 2623 2455 2516 164 -130 50 N -ATOM 976 N SER A 173 59.056 36.964 14.160 1.00 8.96 N -ANISOU 976 N SER A 173 1220 1022 1159 -217 -67 162 N -ATOM 977 CA SER A 173 58.606 37.657 15.345 1.00 8.59 C -ANISOU 977 CA SER A 173 1136 996 1128 -180 -82 96 C -ATOM 978 C SER A 173 59.796 38.051 16.215 1.00 9.29 C -ANISOU 978 C SER A 173 1226 1070 1232 -177 -96 86 C -ATOM 979 O SER A 173 60.725 37.274 16.402 1.00 9.80 O -ANISOU 979 O SER A 173 1264 1198 1261 -247 -149 81 O -ATOM 980 CB SER A 173 57.679 36.765 16.168 1.00 7.98 C -ANISOU 980 CB SER A 173 1160 910 961 -178 -54 179 C -ATOM 981 OG SER A 173 57.270 37.437 17.349 1.00 8.75 O -ANISOU 981 OG SER A 173 1260 970 1094 -256 -75 21 O -ATOM 982 N GLU A 174 59.717 39.252 16.769 1.00 9.37 N -ANISOU 982 N GLU A 174 1262 1078 1220 -296 -149 77 N -ATOM 983 CA GLU A 174 60.665 39.738 17.763 1.00 10.66 C -ANISOU 983 CA GLU A 174 1340 1259 1449 -274 -118 6 C -ATOM 984 C GLU A 174 60.154 39.528 19.185 1.00 9.97 C -ANISOU 984 C GLU A 174 1334 1146 1308 -259 -147 -69 C -ATOM 985 O GLU A 174 60.818 39.925 20.144 1.00 11.45 O -ANISOU 985 O GLU A 174 1467 1367 1515 -431 -241 -130 O -ATOM 986 CB GLU A 174 60.946 41.223 17.529 1.00 11.75 C -ANISOU 986 CB GLU A 174 1588 1340 1536 -333 -44 5 C -ATOM 987 CG GLU A 174 61.622 41.529 16.198 1.00 16.35 C -ANISOU 987 CG GLU A 174 2128 2017 2063 -375 48 3 C -ATOM 988 CD GLU A 174 61.910 43.012 16.009 1.00 21.99 C -ANISOU 988 CD GLU A 174 2906 2668 2779 -248 189 10 C -ATOM 989 OE1 GLU A 174 61.347 43.838 16.756 1.00 26.41 O -ANISOU 989 OE1 GLU A 174 3593 2929 3512 -240 175 31 O -ATOM 990 OE2 GLU A 174 62.695 43.358 15.107 1.00 27.62 O -ANISOU 990 OE2 GLU A 174 3570 3365 3560 -280 200 46 O -ATOM 991 N LYS A 175 58.978 38.921 19.336 1.00 9.11 N -ANISOU 991 N LYS A 175 1238 1008 1212 -187 -154 -66 N -ATOM 992 CA LYS A 175 58.359 38.796 20.649 1.00 8.62 C -ANISOU 992 CA LYS A 175 1194 899 1182 -125 -104 -114 C -ATOM 993 C LYS A 175 58.905 37.613 21.426 1.00 8.33 C -ANISOU 993 C LYS A 175 1180 841 1141 -130 -90 -85 C -ATOM 994 O LYS A 175 59.348 36.621 20.854 1.00 8.34 O -ANISOU 994 O LYS A 175 1153 866 1147 -84 -22 -167 O -ATOM 995 CB LYS A 175 56.859 38.630 20.501 1.00 9.28 C -ANISOU 995 CB LYS A 175 1230 1063 1231 -48 -101 -69 C -ATOM 996 CG LYS A 175 56.179 39.782 19.789 1.00 10.49 C -ANISOU 996 CG LYS A 175 1389 1160 1436 -1 -103 -180 C -ATOM 997 CD LYS A 175 54.665 39.649 19.821 1.00 11.91 C -ANISOU 997 CD LYS A 175 1483 1343 1697 122 -116 -116 C -ATOM 998 CE LYS A 175 54.007 40.621 18.865 1.00 13.49 C -ANISOU 998 CE LYS A 175 1601 1555 1967 176 -258 -97 C -ATOM 999 NZ LYS A 175 52.540 40.684 19.055 1.00 16.30 N -ANISOU 999 NZ LYS A 175 1865 1758 2569 0 -205 48 N -ATOM 1000 N TRP A 176 58.847 37.730 22.746 1.00 9.09 N -ANISOU 1000 N TRP A 176 1273 1028 1152 -24 -68 -58 N -ATOM 1001 CA TRP A 176 59.259 36.679 23.672 1.00 9.48 C -ANISOU 1001 CA TRP A 176 1332 1088 1182 0 -35 -77 C -ATOM 1002 C TRP A 176 58.151 36.516 24.683 1.00 10.05 C -ANISOU 1002 C TRP A 176 1382 1161 1274 88 31 -59 C -ATOM 1003 O TRP A 176 57.694 37.516 25.237 1.00 12.24 O -ANISOU 1003 O TRP A 176 1872 1241 1538 135 274 -132 O -ATOM 1004 CB TRP A 176 60.541 37.066 24.438 1.00 10.67 C -ANISOU 1004 CB TRP A 176 1502 1283 1268 -6 -136 -68 C -ATOM 1005 CG TRP A 176 61.766 37.066 23.591 1.00 11.13 C -ANISOU 1005 CG TRP A 176 1315 1499 1415 -256 -227 -10 C -ATOM 1006 CD1 TRP A 176 62.057 37.928 22.581 1.00 13.43 C -ANISOU 1006 CD1 TRP A 176 1516 1798 1786 -272 -181 81 C -ATOM 1007 CD2 TRP A 176 62.882 36.163 23.670 1.00 11.31 C -ANISOU 1007 CD2 TRP A 176 1281 1656 1358 -350 -266 -121 C -ATOM 1008 NE1 TRP A 176 63.266 37.607 22.013 1.00 13.19 N -ANISOU 1008 NE1 TRP A 176 1509 1817 1685 -366 -157 93 N -ATOM 1009 CE2 TRP A 176 63.796 36.533 22.664 1.00 12.63 C -ANISOU 1009 CE2 TRP A 176 1320 1818 1661 -385 -218 -101 C -ATOM 1010 CE3 TRP A 176 63.206 35.080 24.494 1.00 11.02 C -ANISOU 1010 CE3 TRP A 176 1441 1362 1381 -283 -220 -180 C -ATOM 1011 CZ2 TRP A 176 65.006 35.866 22.458 1.00 13.38 C -ANISOU 1011 CZ2 TRP A 176 1392 1902 1788 -395 -113 -37 C -ATOM 1012 CZ3 TRP A 176 64.418 34.420 24.289 1.00 12.37 C -ANISOU 1012 CZ3 TRP A 176 1537 1717 1446 -141 -131 6 C -ATOM 1013 CH2 TRP A 176 65.288 34.808 23.271 1.00 12.86 C -ANISOU 1013 CH2 TRP A 176 1412 1772 1701 -267 -287 -177 C -ATOM 1014 N CYS A 177 57.725 35.287 24.942 1.00 9.33 N -ANISOU 1014 N CYS A 177 1180 1215 1147 69 -9 -8 N -ATOM 1015 CA CYS A 177 56.742 35.045 25.977 1.00 9.81 C -ANISOU 1015 CA CYS A 177 1175 1345 1206 49 -20 16 C -ATOM 1016 C CYS A 177 57.442 34.914 27.313 1.00 9.02 C -ANISOU 1016 C CYS A 177 1052 1284 1091 22 16 17 C -ATOM 1017 O CYS A 177 58.643 34.669 27.369 1.00 9.54 O -ANISOU 1017 O CYS A 177 956 1593 1075 47 -54 -14 O -ATOM 1018 CB CYS A 177 55.923 33.792 25.691 1.00 10.49 C -ANISOU 1018 CB CYS A 177 1255 1573 1155 -3 -100 27 C -ATOM 1019 SG CYS A 177 56.801 32.236 25.857 1.00 10.78 S -ANISOU 1019 SG CYS A 177 1369 1318 1409 -182 -142 -110 S -ATOM 1020 N THR A 178 56.672 35.069 28.383 1.00 9.38 N -ANISOU 1020 N THR A 178 1097 1301 1165 -1 63 -42 N -ATOM 1021 CA THR A 178 57.155 34.888 29.741 1.00 9.89 C -ANISOU 1021 CA THR A 178 1221 1279 1256 -35 121 -81 C -ATOM 1022 C THR A 178 56.216 33.958 30.490 1.00 9.84 C -ANISOU 1022 C THR A 178 1174 1273 1289 -30 127 -110 C -ATOM 1023 O THR A 178 55.011 34.197 30.549 1.00 10.99 O -ANISOU 1023 O THR A 178 1106 1445 1622 24 244 45 O -ATOM 1024 CB THR A 178 57.227 36.230 30.487 1.00 10.65 C -ANISOU 1024 CB THR A 178 1306 1421 1317 -146 178 -66 C -ATOM 1025 OG1 THR A 178 58.014 37.179 29.745 1.00 11.94 O -ANISOU 1025 OG1 THR A 178 1802 1358 1376 -145 375 -228 O -ATOM 1026 CG2 THR A 178 57.939 36.057 31.839 1.00 12.01 C -ANISOU 1026 CG2 THR A 178 1629 1471 1461 -86 168 -230 C -ATOM 1027 N LEU A 179 56.772 32.922 31.084 1.00 8.75 N -ANISOU 1027 N LEU A 179 1054 1171 1099 -121 -3 -103 N -ATOM 1028 CA LEU A 179 55.991 31.987 31.881 1.00 9.26 C -ANISOU 1028 CA LEU A 179 1250 1101 1165 -86 -25 -104 C -ATOM 1029 C LEU A 179 55.845 32.517 33.308 1.00 9.40 C -ANISOU 1029 C LEU A 179 1274 1138 1159 -94 -6 -171 C -ATOM 1030 O LEU A 179 56.611 33.385 33.730 1.00 9.19 O -ANISOU 1030 O LEU A 179 1328 1171 990 -216 24 -195 O -ATOM 1031 CB LEU A 179 56.675 30.630 31.928 1.00 9.62 C -ANISOU 1031 CB LEU A 179 1301 1134 1219 -78 -63 -174 C -ATOM 1032 CG LEU A 179 56.414 29.728 30.721 1.00 11.13 C -ANISOU 1032 CG LEU A 179 1568 1287 1371 -55 92 -170 C -ATOM 1033 CD1 LEU A 179 56.749 30.366 29.381 1.00 11.24 C -ANISOU 1033 CD1 LEU A 179 1577 1393 1298 66 -207 -300 C -ATOM 1034 CD2 LEU A 179 57.190 28.440 30.918 1.00 12.55 C -ANISOU 1034 CD2 LEU A 179 1823 1410 1532 65 -19 -231 C -ATOM 1035 N PRO A 180 54.898 31.992 34.086 1.00 9.92 N -ANISOU 1035 N PRO A 180 1348 1237 1183 -113 14 -125 N -ATOM 1036 CA PRO A 180 54.786 32.402 35.494 1.00 10.79 C -ANISOU 1036 CA PRO A 180 1468 1324 1306 -119 71 -133 C -ATOM 1037 C PRO A 180 56.083 32.269 36.295 1.00 11.11 C -ANISOU 1037 C PRO A 180 1592 1357 1271 -92 67 -132 C -ATOM 1038 O PRO A 180 56.319 33.083 37.190 1.00 11.48 O -ANISOU 1038 O PRO A 180 1761 1439 1161 -198 54 -332 O -ATOM 1039 CB PRO A 180 53.667 31.500 36.028 1.00 11.43 C -ANISOU 1039 CB PRO A 180 1556 1376 1408 -102 55 -63 C -ATOM 1040 CG PRO A 180 52.839 31.206 34.832 1.00 11.55 C -ANISOU 1040 CG PRO A 180 1542 1312 1533 -139 8 -53 C -ATOM 1041 CD PRO A 180 53.804 31.074 33.705 1.00 10.31 C -ANISOU 1041 CD PRO A 180 1294 1310 1311 -97 -64 -75 C -ATOM 1042 N ASN A 181 56.930 31.302 35.960 1.00 10.92 N -ANISOU 1042 N ASN A 181 1551 1350 1248 -87 -15 -148 N -ATOM 1043 CA ASN A 181 58.205 31.123 36.646 1.00 11.37 C -ANISOU 1043 CA ASN A 181 1569 1427 1324 -58 -79 -87 C -ATOM 1044 C ASN A 181 59.325 32.040 36.119 1.00 11.03 C -ANISOU 1044 C ASN A 181 1519 1407 1265 -66 -74 -122 C -ATOM 1045 O ASN A 181 60.452 31.953 36.582 1.00 12.35 O -ANISOU 1045 O ASN A 181 1571 1815 1304 -115 -241 -93 O -ATOM 1046 CB ASN A 181 58.634 29.655 36.612 1.00 11.75 C -ANISOU 1046 CB ASN A 181 1614 1461 1387 -62 -165 -47 C -ATOM 1047 CG ASN A 181 58.904 29.142 35.203 1.00 10.83 C -ANISOU 1047 CG ASN A 181 1428 1193 1493 -23 -190 23 C -ATOM 1048 OD1 ASN A 181 59.071 29.921 34.272 1.00 12.14 O -ANISOU 1048 OD1 ASN A 181 1874 1320 1415 83 -236 -134 O -ATOM 1049 ND2 ASN A 181 58.969 27.823 35.058 1.00 12.88 N -ANISOU 1049 ND2 ASN A 181 1529 1429 1936 141 -568 7 N -ATOM 1050 N GLY A 182 59.030 32.911 35.162 1.00 10.28 N -ANISOU 1050 N GLY A 182 1466 1274 1165 -57 -60 -173 N -ATOM 1051 CA GLY A 182 59.985 33.905 34.694 1.00 10.11 C -ANISOU 1051 CA GLY A 182 1342 1371 1127 -101 -56 -80 C -ATOM 1052 C GLY A 182 60.754 33.509 33.451 1.00 9.60 C -ANISOU 1052 C GLY A 182 1331 1263 1051 -125 -84 -53 C -ATOM 1053 O GLY A 182 61.374 34.354 32.791 1.00 9.78 O -ANISOU 1053 O GLY A 182 1278 1344 1094 -90 10 -68 O -ATOM 1054 N LYS A 183 60.711 32.230 33.112 1.00 9.62 N -ANISOU 1054 N LYS A 183 1234 1297 1121 -12 -81 -14 N -ATOM 1055 CA LYS A 183 61.376 31.783 31.902 1.00 9.57 C -ANISOU 1055 CA LYS A 183 1235 1276 1123 20 -49 -41 C -ATOM 1056 C LYS A 183 60.736 32.417 30.680 1.00 8.58 C -ANISOU 1056 C LYS A 183 1079 1275 906 34 -56 -139 C -ATOM 1057 O LYS A 183 59.523 32.581 30.626 1.00 9.50 O -ANISOU 1057 O LYS A 183 957 1557 1096 29 -122 -80 O -ATOM 1058 CB LYS A 183 61.303 30.273 31.785 1.00 10.30 C -ANISOU 1058 CB LYS A 183 1389 1315 1207 82 -44 12 C -ATOM 1059 CG LYS A 183 62.144 29.538 32.810 1.00 13.57 C -ANISOU 1059 CG LYS A 183 1752 1608 1795 96 -112 47 C -ATOM 1060 CD LYS A 183 62.013 28.037 32.637 1.00 17.46 C -ANISOU 1060 CD LYS A 183 2411 1959 2261 0 -43 95 C -ATOM 1061 CE LYS A 183 62.956 27.266 33.540 1.00 22.00 C -ANISOU 1061 CE LYS A 183 2900 2625 2832 39 -45 41 C -ATOM 1062 NZ LYS A 183 64.337 27.208 32.978 1.00 24.90 N -ANISOU 1062 NZ LYS A 183 3282 2902 3277 -40 -216 62 N -ATOM 1063 N LYS A 184 61.571 32.749 29.709 1.00 8.60 N -ANISOU 1063 N LYS A 184 983 1259 1023 110 -52 -105 N -ATOM 1064 CA LYS A 184 61.136 33.377 28.473 1.00 8.66 C -ANISOU 1064 CA LYS A 184 1091 1179 1020 87 -50 -117 C -ATOM 1065 C LYS A 184 61.575 32.560 27.281 1.00 8.38 C -ANISOU 1065 C LYS A 184 1025 1245 913 102 -57 -188 C -ATOM 1066 O LYS A 184 62.631 31.926 27.296 1.00 9.52 O -ANISOU 1066 O LYS A 184 1046 1500 1070 250 -238 -237 O -ATOM 1067 CB LYS A 184 61.710 34.789 28.341 1.00 8.92 C -ANISOU 1067 CB LYS A 184 1126 1255 1006 -17 -35 -77 C -ATOM 1068 CG LYS A 184 61.308 35.698 29.483 1.00 10.62 C -ANISOU 1068 CG LYS A 184 1419 1331 1285 -56 -19 -182 C -ATOM 1069 CD LYS A 184 61.877 37.106 29.313 1.00 13.78 C -ANISOU 1069 CD LYS A 184 1817 1683 1733 -46 110 -215 C -ATOM 1070 CE LYS A 184 61.080 37.915 28.293 1.00 17.14 C -ANISOU 1070 CE LYS A 184 2327 2051 2135 -17 82 -163 C -ATOM 1071 NZ LYS A 184 61.607 39.295 28.096 1.00 20.06 N -ANISOU 1071 NZ LYS A 184 2561 2442 2617 12 -6 -160 N -ATOM 1072 N PHE A 185 60.745 32.571 26.244 1.00 7.65 N -ANISOU 1072 N PHE A 185 928 1078 899 53 -120 -179 N -ATOM 1073 CA PHE A 185 61.039 31.869 25.000 1.00 8.19 C -ANISOU 1073 CA PHE A 185 1040 1107 963 61 -49 -187 C -ATOM 1074 C PHE A 185 60.693 32.752 23.829 1.00 8.06 C -ANISOU 1074 C PHE A 185 978 1114 967 34 -100 -185 C -ATOM 1075 O PHE A 185 59.695 33.465 23.851 1.00 8.20 O -ANISOU 1075 O PHE A 185 987 1186 940 93 -79 -169 O -ATOM 1076 CB PHE A 185 60.245 30.564 24.923 1.00 8.36 C -ANISOU 1076 CB PHE A 185 1177 1107 892 122 -43 -116 C -ATOM 1077 CG PHE A 185 60.611 29.603 25.989 1.00 9.35 C -ANISOU 1077 CG PHE A 185 1334 1074 1142 155 -74 -53 C -ATOM 1078 CD1 PHE A 185 61.731 28.800 25.850 1.00 12.05 C -ANISOU 1078 CD1 PHE A 185 1795 1418 1362 286 1 76 C -ATOM 1079 CD2 PHE A 185 59.883 29.542 27.163 1.00 9.99 C -ANISOU 1079 CD2 PHE A 185 1411 1195 1189 108 -194 22 C -ATOM 1080 CE1 PHE A 185 62.118 27.957 26.868 1.00 13.62 C -ANISOU 1080 CE1 PHE A 185 1848 1383 1942 307 -130 21 C -ATOM 1081 CE2 PHE A 185 60.264 28.693 28.170 1.00 11.92 C -ANISOU 1081 CE2 PHE A 185 1797 1458 1272 -24 -198 114 C -ATOM 1082 CZ PHE A 185 61.374 27.891 28.012 1.00 13.60 C -ANISOU 1082 CZ PHE A 185 1973 1559 1633 17 -239 75 C -ATOM 1083 N PRO A 186 61.501 32.693 22.782 1.00 7.82 N -ANISOU 1083 N PRO A 186 842 1064 1063 -13 -52 -89 N -ATOM 1084 CA PRO A 186 61.248 33.531 21.613 1.00 8.41 C -ANISOU 1084 CA PRO A 186 963 1130 1102 -82 -3 -62 C -ATOM 1085 C PRO A 186 60.178 32.945 20.712 1.00 7.33 C -ANISOU 1085 C PRO A 186 851 918 1014 -71 19 -69 C -ATOM 1086 O PRO A 186 60.206 31.761 20.386 1.00 7.40 O -ANISOU 1086 O PRO A 186 937 850 1022 -34 6 -39 O -ATOM 1087 CB PRO A 186 62.593 33.522 20.894 1.00 9.15 C -ANISOU 1087 CB PRO A 186 1021 1241 1214 -119 14 11 C -ATOM 1088 CG PRO A 186 63.220 32.206 21.259 1.00 8.98 C -ANISOU 1088 CG PRO A 186 960 1309 1140 -43 103 -50 C -ATOM 1089 CD PRO A 186 62.744 31.906 22.644 1.00 8.65 C -ANISOU 1089 CD PRO A 186 953 1252 1082 7 -50 -31 C -ATOM 1090 N ILE A 187 59.264 33.792 20.266 1.00 6.81 N -ANISOU 1090 N ILE A 187 847 806 934 -89 -4 -4 N -ATOM 1091 CA ILE A 187 58.280 33.354 19.295 1.00 6.79 C -ANISOU 1091 CA ILE A 187 836 779 965 -71 25 1 C -ATOM 1092 C ILE A 187 58.974 32.954 17.982 1.00 6.34 C -ANISOU 1092 C ILE A 187 752 840 815 -75 -27 63 C -ATOM 1093 O ILE A 187 58.506 32.054 17.290 1.00 6.69 O -ANISOU 1093 O ILE A 187 807 809 923 -78 -28 -23 O -ATOM 1094 CB ILE A 187 57.169 34.405 19.097 1.00 7.03 C -ANISOU 1094 CB ILE A 187 843 883 944 -40 13 -16 C -ATOM 1095 CG1 ILE A 187 56.434 34.667 20.428 1.00 7.54 C -ANISOU 1095 CG1 ILE A 187 967 885 1010 3 12 -13 C -ATOM 1096 CG2 ILE A 187 56.193 33.962 18.009 1.00 7.55 C -ANISOU 1096 CG2 ILE A 187 872 838 1156 45 76 76 C -ATOM 1097 CD1 ILE A 187 55.840 33.452 21.069 1.00 9.05 C -ANISOU 1097 CD1 ILE A 187 1080 1092 1265 -26 240 5 C -ATOM 1098 N ALA A 188 60.127 33.556 17.691 1.00 7.53 N -ANISOU 1098 N ALA A 188 971 909 980 -128 35 -22 N -ATOM 1099 CA ALA A 188 60.921 33.179 16.522 1.00 8.17 C -ANISOU 1099 CA ALA A 188 949 1138 1017 -129 74 -41 C -ATOM 1100 C ALA A 188 61.402 31.735 16.570 1.00 8.28 C -ANISOU 1100 C ALA A 188 886 1217 1043 -92 66 -56 C -ATOM 1101 O ALA A 188 61.772 31.197 15.532 1.00 9.78 O -ANISOU 1101 O ALA A 188 1077 1470 1168 -47 221 -243 O -ATOM 1102 CB ALA A 188 62.115 34.128 16.355 1.00 8.80 C -ANISOU 1102 CB ALA A 188 1029 1296 1018 -187 121 -16 C -ATOM 1103 N GLY A 189 61.413 31.108 17.746 1.00 8.00 N -ANISOU 1103 N GLY A 189 875 1086 1078 -32 24 -134 N -ATOM 1104 CA GLY A 189 61.808 29.720 17.888 1.00 8.74 C -ANISOU 1104 CA GLY A 189 1003 1123 1195 47 0 -96 C -ATOM 1105 C GLY A 189 60.657 28.726 17.836 1.00 8.25 C -ANISOU 1105 C GLY A 189 985 964 1183 63 -34 -53 C -ATOM 1106 O GLY A 189 60.901 27.524 17.876 1.00 10.20 O -ANISOU 1106 O GLY A 189 1201 1047 1626 185 -55 -17 O -ATOM 1107 N VAL A 190 59.416 29.208 17.734 1.00 7.28 N -ANISOU 1107 N VAL A 190 861 812 1092 11 -10 -32 N -ATOM 1108 CA VAL A 190 58.238 28.347 17.741 1.00 7.25 C -ANISOU 1108 CA VAL A 190 921 799 1034 -8 -42 36 C -ATOM 1109 C VAL A 190 57.976 27.745 16.364 1.00 7.08 C -ANISOU 1109 C VAL A 190 853 784 1054 20 -1 74 C -ATOM 1110 O VAL A 190 57.885 28.473 15.381 1.00 8.08 O -ANISOU 1110 O VAL A 190 1170 873 1024 -92 11 78 O -ATOM 1111 CB VAL A 190 57.010 29.141 18.207 1.00 7.51 C -ANISOU 1111 CB VAL A 190 963 853 1036 0 0 42 C -ATOM 1112 CG1 VAL A 190 55.741 28.341 18.012 1.00 7.69 C -ANISOU 1112 CG1 VAL A 190 1020 857 1045 -140 -23 -74 C -ATOM 1113 CG2 VAL A 190 57.199 29.557 19.653 1.00 8.66 C -ANISOU 1113 CG2 VAL A 190 1078 857 1353 -35 45 -24 C -ATOM 1114 N GLN A 191 57.850 26.421 16.301 1.00 7.44 N -ANISOU 1114 N GLN A 191 913 821 1090 34 -96 6 N -ATOM 1115 CA GLN A 191 57.515 25.714 15.066 1.00 7.88 C -ANISOU 1115 CA GLN A 191 887 946 1160 98 -59 -64 C -ATOM 1116 C GLN A 191 56.373 24.749 15.330 1.00 7.28 C -ANISOU 1116 C GLN A 191 881 770 1116 88 -99 -8 C -ATOM 1117 O GLN A 191 56.584 23.603 15.702 1.00 8.57 O -ANISOU 1117 O GLN A 191 970 940 1346 227 -139 121 O -ATOM 1118 CB GLN A 191 58.726 24.959 14.498 1.00 9.67 C -ANISOU 1118 CB GLN A 191 1011 1229 1432 32 -21 -135 C -ATOM 1119 CG GLN A 191 58.470 24.328 13.147 1.00 14.30 C -ANISOU 1119 CG GLN A 191 1650 1903 1880 28 13 -95 C -ATOM 1120 CD GLN A 191 59.644 23.508 12.631 1.00 19.11 C -ANISOU 1120 CD GLN A 191 2157 2401 2703 -58 216 30 C -ATOM 1121 OE1 GLN A 191 60.633 24.062 12.157 1.00 23.71 O -ANISOU 1121 OE1 GLN A 191 2504 3157 3347 127 394 101 O -ATOM 1122 NE2 GLN A 191 59.527 22.185 12.715 1.00 21.06 N -ANISOU 1122 NE2 GLN A 191 2317 2561 3122 130 352 -23 N -ATOM 1123 N ILE A 192 55.157 25.220 15.121 1.00 6.59 N -ANISOU 1123 N ILE A 192 722 748 1035 81 -87 43 N -ATOM 1124 CA ILE A 192 53.983 24.394 15.377 1.00 7.18 C -ANISOU 1124 CA ILE A 192 829 891 1006 8 -56 38 C -ATOM 1125 C ILE A 192 53.882 23.270 14.339 1.00 7.76 C -ANISOU 1125 C ILE A 192 916 885 1144 -39 -82 25 C -ATOM 1126 O ILE A 192 53.562 22.133 14.671 1.00 9.03 O -ANISOU 1126 O ILE A 192 1095 907 1429 -59 -75 12 O -ATOM 1127 CB ILE A 192 52.688 25.238 15.411 1.00 6.69 C -ANISOU 1127 CB ILE A 192 768 853 918 0 -49 -13 C -ATOM 1128 CG1 ILE A 192 52.782 26.330 16.483 1.00 7.20 C -ANISOU 1128 CG1 ILE A 192 773 943 1017 32 -53 -31 C -ATOM 1129 CG2 ILE A 192 51.467 24.354 15.695 1.00 8.38 C -ANISOU 1129 CG2 ILE A 192 822 1139 1221 -93 2 -130 C -ATOM 1130 CD1 ILE A 192 51.634 27.319 16.449 1.00 7.82 C -ANISOU 1130 CD1 ILE A 192 893 1031 1045 114 -36 -37 C -ATOM 1131 N GLN A 193 54.155 23.613 13.088 1.00 8.10 N -ANISOU 1131 N GLN A 193 1018 952 1106 24 -99 -72 N -ATOM 1132 CA GLN A 193 54.092 22.689 11.962 1.00 9.58 C -ANISOU 1132 CA GLN A 193 1084 1303 1251 -15 -55 -141 C -ATOM 1133 C GLN A 193 55.272 22.871 11.018 1.00 10.17 C -ANISOU 1133 C GLN A 193 1165 1350 1347 51 -9 -148 C -ATOM 1134 O GLN A 193 55.763 23.979 10.814 1.00 11.67 O -ANISOU 1134 O GLN A 193 1375 1560 1496 86 18 -181 O -ATOM 1135 CB GLN A 193 52.793 22.896 11.171 1.00 10.78 C -ANISOU 1135 CB GLN A 193 1266 1476 1353 80 -118 -184 C -ATOM 1136 CG GLN A 193 51.536 22.656 11.979 1.00 11.65 C -ANISOU 1136 CG GLN A 193 1276 1571 1580 177 -47 -289 C -ATOM 1137 CD GLN A 193 51.367 21.212 12.385 1.00 11.12 C -ANISOU 1137 CD GLN A 193 990 1603 1629 122 61 -326 C -ATOM 1138 OE1 GLN A 193 52.082 20.337 11.902 1.00 11.75 O -ANISOU 1138 OE1 GLN A 193 1116 1549 1800 275 141 -635 O -ATOM 1139 NE2 GLN A 193 50.408 20.949 13.253 1.00 13.04 N -ANISOU 1139 NE2 GLN A 193 1184 1894 1875 -29 117 -559 N -ATOM 1140 N ARG A 194 55.689 21.765 10.397 1.00 11.17 N -ANISOU 1140 N ARG A 194 1283 1476 1484 144 36 -158 N -ATOM 1141 CA ARG A 194 56.844 21.758 9.498 1.00 13.29 C -ANISOU 1141 CA ARG A 194 1517 1807 1725 159 65 -84 C -ATOM 1142 C ARG A 194 56.466 21.932 8.031 1.00 13.03 C -ANISOU 1142 C ARG A 194 1436 1843 1669 120 75 -97 C -ATOM 1143 O ARG A 194 57.320 22.208 7.199 1.00 14.34 O -ANISOU 1143 O ARG A 194 1500 2120 1827 220 247 -178 O -ATOM 1144 CB ARG A 194 57.678 20.472 9.673 1.00 14.11 C -ANISOU 1144 CB ARG A 194 1570 1941 1849 177 50 -14 C -ATOM 1145 CG ARG A 194 57.071 19.206 9.083 1.00 17.66 C -ANISOU 1145 CG ARG A 194 1999 2383 2325 193 45 -40 C -ATOM 1146 CD ARG A 194 57.966 17.967 9.177 1.00 22.86 C -ANISOU 1146 CD ARG A 194 2759 2952 2975 100 54 56 C -ATOM 1147 NE ARG A 194 57.202 16.731 9.392 1.00 27.76 N -ANISOU 1147 NE ARG A 194 3536 3453 3557 50 -42 -22 N -ATOM 1148 CZ ARG A 194 57.309 15.588 8.694 1.00 31.28 C -ANISOU 1148 CZ ARG A 194 3975 3979 3929 6 67 2 C -ATOM 1149 NH1 ARG A 194 58.161 15.453 7.678 1.00 32.04 N -ANISOU 1149 NH1 ARG A 194 3948 4145 4081 46 128 -8 N -ATOM 1150 NH2 ARG A 194 56.545 14.550 9.026 1.00 32.86 N -ANISOU 1150 NH2 ARG A 194 4212 4141 4132 -9 37 10 N -ATOM 1151 N GLU A 195 55.187 21.791 7.705 1.00 12.96 N -ANISOU 1151 N GLU A 195 1448 1801 1673 151 48 -153 N -ATOM 1152 CA GLU A 195 54.752 21.763 6.308 1.00 12.58 C -ANISOU 1152 CA GLU A 195 1469 1709 1600 144 76 -162 C -ATOM 1153 C GLU A 195 54.992 23.114 5.627 1.00 12.65 C -ANISOU 1153 C GLU A 195 1423 1738 1645 151 59 -200 C -ATOM 1154 O GLU A 195 54.856 24.154 6.269 1.00 13.06 O -ANISOU 1154 O GLU A 195 1416 1812 1731 192 106 -295 O -ATOM 1155 CB GLU A 195 53.264 21.376 6.230 1.00 13.24 C -ANISOU 1155 CB GLU A 195 1509 1824 1695 148 20 -140 C -ATOM 1156 CG GLU A 195 52.976 19.888 6.413 1.00 14.44 C -ANISOU 1156 CG GLU A 195 1736 1978 1771 188 23 -200 C -ATOM 1157 CD GLU A 195 53.127 19.383 7.843 1.00 14.99 C -ANISOU 1157 CD GLU A 195 1873 1823 1999 469 -36 -236 C -ATOM 1158 OE1 GLU A 195 52.953 20.162 8.801 1.00 12.97 O -ANISOU 1158 OE1 GLU A 195 1088 1974 1866 630 99 -450 O -ATOM 1159 OE2 GLU A 195 53.432 18.181 8.019 1.00 19.96 O -ANISOU 1159 OE2 GLU A 195 2880 2217 2486 414 2 -248 O -ATOM 1160 N PRO A 196 55.345 23.106 4.341 1.00 12.25 N -ANISOU 1160 N PRO A 196 1387 1621 1646 187 141 -186 N -ATOM 1161 CA PRO A 196 55.574 24.356 3.609 1.00 12.41 C -ANISOU 1161 CA PRO A 196 1444 1639 1630 65 155 -162 C -ATOM 1162 C PRO A 196 54.308 25.168 3.340 1.00 11.65 C -ANISOU 1162 C PRO A 196 1363 1466 1597 46 209 -184 C -ATOM 1163 O PRO A 196 54.395 26.354 3.020 1.00 12.10 O -ANISOU 1163 O PRO A 196 1332 1488 1777 -45 273 -297 O -ATOM 1164 CB PRO A 196 56.231 23.887 2.306 1.00 12.98 C -ANISOU 1164 CB PRO A 196 1444 1783 1705 145 186 -109 C -ATOM 1165 CG PRO A 196 55.740 22.533 2.143 1.00 13.34 C -ANISOU 1165 CG PRO A 196 1551 1870 1645 162 244 -172 C -ATOM 1166 CD PRO A 196 55.660 21.930 3.510 1.00 12.89 C -ANISOU 1166 CD PRO A 196 1470 1761 1665 164 131 -238 C -ATOM 1167 N PHE A 197 53.147 24.531 3.435 1.00 9.92 N -ANISOU 1167 N PHE A 197 1181 1241 1345 -39 208 -185 N -ATOM 1168 CA PHE A 197 51.881 25.253 3.394 1.00 9.07 C -ANISOU 1168 CA PHE A 197 1136 1027 1282 -30 163 -112 C -ATOM 1169 C PHE A 197 50.873 24.447 4.181 1.00 7.91 C -ANISOU 1169 C PHE A 197 1066 757 1180 -74 204 -81 C -ATOM 1170 O PHE A 197 51.018 23.235 4.296 1.00 9.46 O -ANISOU 1170 O PHE A 197 1252 812 1527 62 233 -190 O -ATOM 1171 CB PHE A 197 51.379 25.511 1.964 1.00 9.75 C -ANISOU 1171 CB PHE A 197 1189 1218 1296 -101 229 -141 C -ATOM 1172 CG PHE A 197 51.202 24.272 1.149 1.00 11.77 C -ANISOU 1172 CG PHE A 197 1430 1410 1631 42 39 -125 C -ATOM 1173 CD1 PHE A 197 52.269 23.754 0.420 1.00 13.98 C -ANISOU 1173 CD1 PHE A 197 1712 1789 1810 86 25 -224 C -ATOM 1174 CD2 PHE A 197 49.981 23.609 1.102 1.00 13.21 C -ANISOU 1174 CD2 PHE A 197 1785 1456 1775 -104 1 -81 C -ATOM 1175 CE1 PHE A 197 52.124 22.598 -0.331 1.00 16.01 C -ANISOU 1175 CE1 PHE A 197 1953 2040 2088 10 78 -231 C -ATOM 1176 CE2 PHE A 197 49.833 22.430 0.354 1.00 14.91 C -ANISOU 1176 CE2 PHE A 197 1802 1812 2049 -73 -41 -149 C -ATOM 1177 CZ PHE A 197 50.907 21.937 -0.355 1.00 16.01 C -ANISOU 1177 CZ PHE A 197 2001 1864 2215 -54 -76 -249 C -ATOM 1178 N PRO A 198 49.845 25.095 4.718 1.00 7.29 N -ANISOU 1178 N PRO A 198 950 768 1050 -36 221 -68 N -ATOM 1179 CA PRO A 198 49.670 26.554 4.747 1.00 6.26 C -ANISOU 1179 CA PRO A 198 869 713 795 -6 127 12 C -ATOM 1180 C PRO A 198 50.622 27.252 5.713 1.00 6.09 C -ANISOU 1180 C PRO A 198 850 723 737 36 119 80 C -ATOM 1181 O PRO A 198 50.997 26.681 6.721 1.00 7.17 O -ANISOU 1181 O PRO A 198 1090 728 905 -52 20 148 O -ATOM 1182 CB PRO A 198 48.226 26.708 5.243 1.00 6.74 C -ANISOU 1182 CB PRO A 198 891 837 833 -28 82 -63 C -ATOM 1183 CG PRO A 198 47.954 25.465 6.021 1.00 7.79 C -ANISOU 1183 CG PRO A 198 892 949 1118 -59 68 19 C -ATOM 1184 CD PRO A 198 48.739 24.384 5.377 1.00 7.64 C -ANISOU 1184 CD PRO A 198 969 918 1016 -175 168 42 C -ATOM 1185 N GLN A 199 50.972 28.488 5.391 1.00 5.41 N -ANISOU 1185 N GLN A 199 802 577 674 15 96 22 N -ATOM 1186 CA GLN A 199 51.658 29.403 6.300 1.00 5.67 C -ANISOU 1186 CA GLN A 199 753 615 785 3 66 41 C -ATOM 1187 C GLN A 199 50.791 30.633 6.469 1.00 5.08 C -ANISOU 1187 C GLN A 199 759 493 676 60 31 80 C -ATOM 1188 O GLN A 199 50.200 31.127 5.517 1.00 5.98 O -ANISOU 1188 O GLN A 199 1021 605 645 174 55 59 O -ATOM 1189 CB GLN A 199 53.018 29.827 5.745 1.00 6.20 C -ANISOU 1189 CB GLN A 199 812 641 902 10 78 32 C -ATOM 1190 CG GLN A 199 54.002 28.675 5.642 1.00 7.22 C -ANISOU 1190 CG GLN A 199 832 734 1178 31 166 3 C -ATOM 1191 CD GLN A 199 55.349 29.134 5.155 1.00 7.10 C -ANISOU 1191 CD GLN A 199 752 658 1287 -100 101 46 C -ATOM 1192 OE1 GLN A 199 55.901 30.088 5.675 1.00 9.06 O -ANISOU 1192 OE1 GLN A 199 884 956 1601 -185 186 102 O -ATOM 1193 NE2 GLN A 199 55.899 28.437 4.178 1.00 10.88 N -ANISOU 1193 NE2 GLN A 199 1206 1192 1732 -79 588 -227 N -ATOM 1194 N TYR A 200 50.723 31.116 7.706 1.00 4.83 N -ANISOU 1194 N TYR A 200 659 602 572 -12 -22 47 N -ATOM 1195 CA TYR A 200 49.723 32.110 8.070 1.00 4.98 C -ANISOU 1195 CA TYR A 200 633 633 625 58 9 61 C -ATOM 1196 C TYR A 200 50.260 33.483 8.471 1.00 5.10 C -ANISOU 1196 C TYR A 200 699 611 625 42 37 104 C -ATOM 1197 O TYR A 200 49.697 34.490 8.068 1.00 5.80 O -ANISOU 1197 O TYR A 200 764 586 852 54 -3 108 O -ATOM 1198 CB TYR A 200 48.867 31.566 9.201 1.00 5.07 C -ANISOU 1198 CB TYR A 200 664 706 555 -23 130 -4 C -ATOM 1199 CG TYR A 200 48.158 30.263 8.874 1.00 5.20 C -ANISOU 1199 CG TYR A 200 628 726 618 25 128 2 C -ATOM 1200 CD1 TYR A 200 47.099 30.234 7.982 1.00 5.47 C -ANISOU 1200 CD1 TYR A 200 703 652 723 53 -33 93 C -ATOM 1201 CD2 TYR A 200 48.538 29.067 9.467 1.00 5.29 C -ANISOU 1201 CD2 TYR A 200 655 708 645 -68 56 101 C -ATOM 1202 CE1 TYR A 200 46.418 29.067 7.719 1.00 5.52 C -ANISOU 1202 CE1 TYR A 200 582 776 738 -30 -89 8 C -ATOM 1203 CE2 TYR A 200 47.871 27.884 9.190 1.00 5.58 C -ANISOU 1203 CE2 TYR A 200 726 685 706 27 94 65 C -ATOM 1204 CZ TYR A 200 46.804 27.898 8.329 1.00 4.50 C -ANISOU 1204 CZ TYR A 200 614 581 513 38 72 -2 C -ATOM 1205 OH TYR A 200 46.142 26.725 8.111 1.00 5.39 O -ANISOU 1205 OH TYR A 200 724 591 731 -112 83 48 O -ATOM 1206 N SER A 201 51.298 33.515 9.306 1.00 4.77 N -ANISOU 1206 N SER A 201 643 546 620 17 24 62 N -ATOM 1207 CA SER A 201 51.721 34.757 9.955 1.00 5.39 C -ANISOU 1207 CA SER A 201 725 588 732 9 41 85 C -ATOM 1208 C SER A 201 53.006 34.492 10.711 1.00 4.93 C -ANISOU 1208 C SER A 201 658 602 612 -6 39 77 C -ATOM 1209 O SER A 201 53.189 33.385 11.219 1.00 5.48 O -ANISOU 1209 O SER A 201 744 615 723 27 -9 134 O -ATOM 1210 CB SER A 201 50.667 35.177 10.985 1.00 5.85 C -ANISOU 1210 CB SER A 201 733 668 822 9 34 51 C -ATOM 1211 OG SER A 201 51.086 36.309 11.740 1.00 6.39 O -ANISOU 1211 OG SER A 201 882 608 938 -25 -30 -48 O -ATOM 1212 N PRO A 202 53.862 35.498 10.862 1.00 5.41 N -ANISOU 1212 N PRO A 202 710 641 702 -42 -6 128 N -ATOM 1213 CA PRO A 202 55.037 35.345 11.730 1.00 5.85 C -ANISOU 1213 CA PRO A 202 718 715 788 -44 -5 81 C -ATOM 1214 C PRO A 202 54.701 35.376 13.218 1.00 5.55 C -ANISOU 1214 C PRO A 202 656 663 789 -111 -2 100 C -ATOM 1215 O PRO A 202 55.540 35.009 14.025 1.00 6.38 O -ANISOU 1215 O PRO A 202 789 808 824 -21 -35 102 O -ATOM 1216 CB PRO A 202 55.898 36.566 11.370 1.00 6.63 C -ANISOU 1216 CB PRO A 202 805 929 783 -179 53 123 C -ATOM 1217 CG PRO A 202 54.889 37.605 10.975 1.00 6.82 C -ANISOU 1217 CG PRO A 202 930 869 790 -191 113 70 C -ATOM 1218 CD PRO A 202 53.841 36.826 10.220 1.00 5.90 C -ANISOU 1218 CD PRO A 202 832 614 796 -19 40 193 C -ATOM 1219 N GLU A 203 53.502 35.841 13.570 1.00 5.46 N -ANISOU 1219 N GLU A 203 663 628 782 -52 -10 54 N -ATOM 1220 CA GLU A 203 53.075 35.906 14.956 1.00 5.75 C -ANISOU 1220 CA GLU A 203 820 613 752 -23 -2 -54 C -ATOM 1221 C GLU A 203 52.170 34.727 15.276 1.00 5.55 C -ANISOU 1221 C GLU A 203 783 602 722 -30 42 -23 C -ATOM 1222 O GLU A 203 51.694 34.022 14.379 1.00 5.62 O -ANISOU 1222 O GLU A 203 803 661 668 -54 39 -15 O -ATOM 1223 CB GLU A 203 52.371 37.224 15.280 1.00 6.31 C -ANISOU 1223 CB GLU A 203 878 629 890 -68 1 -5 C -ATOM 1224 CG GLU A 203 53.195 38.455 14.941 1.00 7.90 C -ANISOU 1224 CG GLU A 203 1103 725 1173 -67 81 -21 C -ATOM 1225 CD GLU A 203 54.517 38.574 15.686 1.00 8.63 C -ANISOU 1225 CD GLU A 203 1371 722 1183 -265 187 88 C -ATOM 1226 OE1 GLU A 203 54.694 37.962 16.768 1.00 9.23 O -ANISOU 1226 OE1 GLU A 203 1170 1008 1329 -330 67 -50 O -ATOM 1227 OE2 GLU A 203 55.377 39.339 15.190 1.00 11.13 O -ANISOU 1227 OE2 GLU A 203 1495 1177 1556 -398 -68 111 O -ATOM 1228 N LEU A 204 51.972 34.504 16.566 1.00 5.75 N -ANISOU 1228 N LEU A 204 784 700 698 -106 -20 8 N -ATOM 1229 CA LEU A 204 51.072 33.479 17.067 1.00 5.76 C -ANISOU 1229 CA LEU A 204 878 656 654 -74 33 -11 C -ATOM 1230 C LEU A 204 49.646 34.014 17.117 1.00 5.52 C -ANISOU 1230 C LEU A 204 824 557 716 -86 87 -16 C -ATOM 1231 O LEU A 204 49.429 35.159 17.501 1.00 6.90 O -ANISOU 1231 O LEU A 204 952 531 1136 -70 109 -180 O -ATOM 1232 CB LEU A 204 51.513 33.090 18.467 1.00 6.79 C -ANISOU 1232 CB LEU A 204 1020 771 789 44 34 25 C -ATOM 1233 CG LEU A 204 51.116 31.737 19.020 1.00 8.61 C -ANISOU 1233 CG LEU A 204 1078 1049 1141 -46 -66 29 C -ATOM 1234 CD1 LEU A 204 51.774 30.615 18.238 1.00 9.26 C -ANISOU 1234 CD1 LEU A 204 1531 760 1226 101 -294 -48 C -ATOM 1235 CD2 LEU A 204 51.459 31.643 20.510 1.00 9.50 C -ANISOU 1235 CD2 LEU A 204 1379 1104 1123 122 69 130 C -ATOM 1236 N HIS A 205 48.695 33.158 16.793 1.00 5.11 N -ANISOU 1236 N HIS A 205 731 545 663 -50 45 -41 N -ATOM 1237 CA HIS A 205 47.291 33.522 16.787 1.00 5.66 C -ANISOU 1237 CA HIS A 205 818 609 723 -33 25 -24 C -ATOM 1238 C HIS A 205 46.425 32.369 17.241 1.00 4.95 C -ANISOU 1238 C HIS A 205 724 568 587 -11 62 -27 C -ATOM 1239 O HIS A 205 46.871 31.225 17.327 1.00 5.39 O -ANISOU 1239 O HIS A 205 785 546 717 20 119 -15 O -ATOM 1240 CB HIS A 205 46.887 33.921 15.380 1.00 6.33 C -ANISOU 1240 CB HIS A 205 779 761 863 -56 60 95 C -ATOM 1241 CG HIS A 205 47.627 35.099 14.856 1.00 8.15 C -ANISOU 1241 CG HIS A 205 998 951 1147 -34 77 113 C -ATOM 1242 ND1 HIS A 205 48.615 35.010 13.900 1.00 10.97 N -ANISOU 1242 ND1 HIS A 205 1467 1461 1238 -181 77 393 N -ATOM 1243 CD2 HIS A 205 47.579 36.399 15.216 1.00 11.21 C -ANISOU 1243 CD2 HIS A 205 1874 925 1460 -46 487 126 C -ATOM 1244 CE1 HIS A 205 49.079 36.218 13.632 1.00 8.85 C -ANISOU 1244 CE1 HIS A 205 1290 1067 1004 -240 25 257 C -ATOM 1245 NE2 HIS A 205 48.467 37.079 14.416 1.00 11.87 N -ANISOU 1245 NE2 HIS A 205 1734 1250 1523 -247 173 160 N -ATOM 1246 N PHE A 206 45.160 32.676 17.484 1.00 5.04 N -ANISOU 1246 N PHE A 206 697 452 764 -4 73 -46 N -ATOM 1247 CA PHE A 206 44.154 31.697 17.883 1.00 4.86 C -ANISOU 1247 CA PHE A 206 752 496 597 -2 39 -59 C -ATOM 1248 C PHE A 206 42.938 31.843 16.978 1.00 4.41 C -ANISOU 1248 C PHE A 206 753 409 513 53 94 -84 C -ATOM 1249 O PHE A 206 42.390 32.925 16.839 1.00 6.04 O -ANISOU 1249 O PHE A 206 1042 526 726 79 -134 -99 O -ATOM 1250 CB PHE A 206 43.759 31.933 19.333 1.00 5.01 C -ANISOU 1250 CB PHE A 206 793 588 520 80 -39 -8 C -ATOM 1251 CG PHE A 206 42.633 31.062 19.820 1.00 4.47 C -ANISOU 1251 CG PHE A 206 723 549 425 -15 25 -18 C -ATOM 1252 CD1 PHE A 206 42.840 29.719 20.106 1.00 4.98 C -ANISOU 1252 CD1 PHE A 206 627 606 657 71 -42 -27 C -ATOM 1253 CD2 PHE A 206 41.372 31.589 20.036 1.00 5.40 C -ANISOU 1253 CD2 PHE A 206 892 562 596 144 118 44 C -ATOM 1254 CE1 PHE A 206 41.810 28.920 20.558 1.00 5.46 C -ANISOU 1254 CE1 PHE A 206 843 475 754 -39 1 -24 C -ATOM 1255 CE2 PHE A 206 40.348 30.783 20.509 1.00 5.26 C -ANISOU 1255 CE2 PHE A 206 886 546 566 114 170 30 C -ATOM 1256 CZ PHE A 206 40.565 29.466 20.778 1.00 5.67 C -ANISOU 1256 CZ PHE A 206 827 687 638 51 78 -79 C -ATOM 1257 N PHE A 207 42.541 30.735 16.374 1.00 4.19 N -ANISOU 1257 N PHE A 207 607 384 598 29 58 -29 N -ATOM 1258 CA PHE A 207 41.389 30.696 15.463 1.00 4.08 C -ANISOU 1258 CA PHE A 207 590 409 550 -5 47 -2 C -ATOM 1259 C PHE A 207 40.259 29.956 16.165 1.00 4.08 C -ANISOU 1259 C PHE A 207 556 441 552 16 59 -43 C -ATOM 1260 O PHE A 207 40.292 28.732 16.295 1.00 5.03 O -ANISOU 1260 O PHE A 207 733 468 708 -10 225 -17 O -ATOM 1261 CB PHE A 207 41.810 29.967 14.194 1.00 4.91 C -ANISOU 1261 CB PHE A 207 612 654 599 9 20 -47 C -ATOM 1262 CG PHE A 207 40.757 29.813 13.145 1.00 5.26 C -ANISOU 1262 CG PHE A 207 752 740 506 18 187 -110 C -ATOM 1263 CD1 PHE A 207 40.491 30.805 12.229 1.00 7.36 C -ANISOU 1263 CD1 PHE A 207 947 962 888 199 -58 -90 C -ATOM 1264 CD2 PHE A 207 40.125 28.596 12.994 1.00 7.78 C -ANISOU 1264 CD2 PHE A 207 916 1065 975 -110 -61 -338 C -ATOM 1265 CE1 PHE A 207 39.559 30.566 11.189 1.00 8.93 C -ANISOU 1265 CE1 PHE A 207 1081 1269 1040 375 49 -88 C -ATOM 1266 CE2 PHE A 207 39.228 28.365 11.985 1.00 9.30 C -ANISOU 1266 CE2 PHE A 207 963 1381 1190 -121 125 -586 C -ATOM 1267 CZ PHE A 207 38.957 29.326 11.076 1.00 9.56 C -ANISOU 1267 CZ PHE A 207 875 1660 1098 196 -18 -460 C -ATOM 1268 N ALA A 208 39.259 30.682 16.646 1.00 4.06 N -ANISOU 1268 N ALA A 208 570 382 589 58 101 2 N -ATOM 1269 CA ALA A 208 38.159 30.053 17.365 1.00 4.22 C -ANISOU 1269 CA ALA A 208 588 539 476 26 29 -20 C -ATOM 1270 C ALA A 208 37.280 29.262 16.420 1.00 4.03 C -ANISOU 1270 C ALA A 208 570 499 460 84 102 -26 C -ATOM 1271 O ALA A 208 36.950 29.759 15.341 1.00 4.52 O -ANISOU 1271 O ALA A 208 644 561 510 -1 64 -28 O -ATOM 1272 CB ALA A 208 37.314 31.116 18.066 1.00 4.33 C -ANISOU 1272 CB ALA A 208 633 482 527 100 43 -123 C -ATOM 1273 N PHE A 209 36.832 28.086 16.847 1.00 4.13 N -ANISOU 1273 N PHE A 209 617 508 443 78 -25 -84 N -ATOM 1274 CA PHE A 209 35.917 27.299 16.032 1.00 4.29 C -ANISOU 1274 CA PHE A 209 586 581 462 17 34 -46 C -ATOM 1275 C PHE A 209 34.767 26.643 16.799 1.00 4.92 C -ANISOU 1275 C PHE A 209 693 558 617 6 15 -26 C -ATOM 1276 O PHE A 209 33.910 26.054 16.175 1.00 5.88 O -ANISOU 1276 O PHE A 209 763 864 606 -210 -42 -73 O -ATOM 1277 CB PHE A 209 36.650 26.307 15.114 1.00 5.20 C -ANISOU 1277 CB PHE A 209 703 638 634 19 13 -128 C -ATOM 1278 CG PHE A 209 37.642 25.401 15.804 1.00 4.47 C -ANISOU 1278 CG PHE A 209 617 513 566 30 24 -87 C -ATOM 1279 CD1 PHE A 209 38.946 25.329 15.351 1.00 5.09 C -ANISOU 1279 CD1 PHE A 209 815 471 646 7 -46 -174 C -ATOM 1280 CD2 PHE A 209 37.277 24.589 16.871 1.00 5.60 C -ANISOU 1280 CD2 PHE A 209 755 557 814 69 158 -84 C -ATOM 1281 CE1 PHE A 209 39.860 24.487 15.961 1.00 5.54 C -ANISOU 1281 CE1 PHE A 209 707 515 881 -13 86 -144 C -ATOM 1282 CE2 PHE A 209 38.197 23.770 17.490 1.00 5.62 C -ANISOU 1282 CE2 PHE A 209 985 516 633 175 184 14 C -ATOM 1283 CZ PHE A 209 39.485 23.718 17.036 1.00 5.35 C -ANISOU 1283 CZ PHE A 209 915 433 683 71 -48 -239 C -ATOM 1284 N ASP A 210 34.671 26.790 18.117 1.00 4.48 N -ANISOU 1284 N ASP A 210 549 637 515 12 62 7 N -ATOM 1285 CA ASP A 210 33.506 26.278 18.829 1.00 4.54 C -ANISOU 1285 CA ASP A 210 596 600 527 27 61 -7 C -ATOM 1286 C ASP A 210 33.416 26.939 20.186 1.00 4.87 C -ANISOU 1286 C ASP A 210 653 694 503 70 47 -10 C -ATOM 1287 O ASP A 210 34.434 27.243 20.807 1.00 5.37 O -ANISOU 1287 O ASP A 210 615 793 632 47 77 -29 O -ATOM 1288 CB ASP A 210 33.563 24.747 18.986 1.00 5.40 C -ANISOU 1288 CB ASP A 210 715 677 661 2 109 -21 C -ATOM 1289 CG ASP A 210 32.703 24.004 17.990 1.00 6.24 C -ANISOU 1289 CG ASP A 210 583 801 985 123 122 -210 C -ATOM 1290 OD1 ASP A 210 31.539 24.400 17.804 1.00 8.24 O -ANISOU 1290 OD1 ASP A 210 765 893 1472 -7 91 -371 O -ATOM 1291 OD2 ASP A 210 33.146 22.998 17.399 1.00 7.53 O -ANISOU 1291 OD2 ASP A 210 822 935 1103 170 -36 -200 O -ATOM 1292 N ILE A 211 32.185 27.142 20.640 1.00 4.68 N -ANISOU 1292 N ILE A 211 494 709 574 20 76 -43 N -ATOM 1293 CA ILE A 211 31.895 27.621 21.985 1.00 5.50 C -ANISOU 1293 CA ILE A 211 690 796 601 -3 81 26 C -ATOM 1294 C ILE A 211 30.826 26.724 22.591 1.00 5.81 C -ANISOU 1294 C ILE A 211 682 784 738 17 96 57 C -ATOM 1295 O ILE A 211 29.774 26.520 21.974 1.00 6.36 O -ANISOU 1295 O ILE A 211 686 929 798 -64 110 155 O -ATOM 1296 CB ILE A 211 31.389 29.070 21.984 1.00 5.68 C -ANISOU 1296 CB ILE A 211 729 788 640 59 81 2 C -ATOM 1297 CG1 ILE A 211 32.478 30.027 21.508 1.00 6.23 C -ANISOU 1297 CG1 ILE A 211 851 820 696 43 77 66 C -ATOM 1298 CG2 ILE A 211 30.879 29.474 23.380 1.00 6.65 C -ANISOU 1298 CG2 ILE A 211 873 898 755 35 70 -42 C -ATOM 1299 CD1 ILE A 211 31.979 31.393 21.132 1.00 7.18 C -ANISOU 1299 CD1 ILE A 211 1059 911 758 -42 34 19 C -ATOM 1300 N LYS A 212 31.084 26.194 23.778 1.00 6.06 N -ANISOU 1300 N LYS A 212 656 883 764 11 150 122 N -ATOM 1301 CA LYS A 212 30.056 25.499 24.530 1.00 6.73 C -ANISOU 1301 CA LYS A 212 762 970 823 -1 170 84 C -ATOM 1302 C LYS A 212 30.102 25.925 25.984 1.00 7.26 C -ANISOU 1302 C LYS A 212 826 1055 877 0 238 164 C -ATOM 1303 O LYS A 212 31.136 26.343 26.501 1.00 7.49 O -ANISOU 1303 O LYS A 212 904 1076 865 44 284 100 O -ATOM 1304 CB LYS A 212 30.178 23.980 24.388 1.00 7.13 C -ANISOU 1304 CB LYS A 212 814 981 913 -70 204 74 C -ATOM 1305 CG LYS A 212 31.438 23.374 24.971 1.00 7.54 C -ANISOU 1305 CG LYS A 212 824 948 1091 5 263 160 C -ATOM 1306 CD LYS A 212 31.516 21.876 24.687 1.00 8.44 C -ANISOU 1306 CD LYS A 212 1024 1066 1115 130 92 148 C -ATOM 1307 CE LYS A 212 32.681 21.200 25.387 1.00 9.61 C -ANISOU 1307 CE LYS A 212 1172 1261 1218 142 169 51 C -ATOM 1308 NZ LYS A 212 32.762 19.757 25.023 1.00 10.24 N -ANISOU 1308 NZ LYS A 212 1316 1018 1556 263 -5 -120 N -ATOM 1309 N TYR A 213 28.964 25.807 26.652 1.00 8.18 N -ANISOU 1309 N TYR A 213 950 1287 868 33 244 140 N -ATOM 1310 CA TYR A 213 28.863 26.173 28.048 1.00 9.10 C -ANISOU 1310 CA TYR A 213 1137 1331 987 9 203 137 C -ATOM 1311 C TYR A 213 28.010 25.152 28.799 1.00 9.79 C -ANISOU 1311 C TYR A 213 1193 1497 1029 -11 272 182 C -ATOM 1312 O TYR A 213 27.052 24.616 28.258 1.00 10.39 O -ANISOU 1312 O TYR A 213 1205 1694 1046 -56 421 310 O -ATOM 1313 CB TYR A 213 28.288 27.585 28.209 1.00 9.99 C -ANISOU 1313 CB TYR A 213 1322 1393 1079 26 194 140 C -ATOM 1314 CG TYR A 213 26.865 27.751 27.724 1.00 10.25 C -ANISOU 1314 CG TYR A 213 1316 1469 1110 94 365 30 C -ATOM 1315 CD1 TYR A 213 25.784 27.595 28.598 1.00 12.01 C -ANISOU 1315 CD1 TYR A 213 1411 1916 1233 186 314 35 C -ATOM 1316 CD2 TYR A 213 26.593 28.052 26.397 1.00 12.38 C -ANISOU 1316 CD2 TYR A 213 1510 1827 1366 219 423 145 C -ATOM 1317 CE1 TYR A 213 24.475 27.742 28.155 1.00 11.74 C -ANISOU 1317 CE1 TYR A 213 1310 1834 1316 213 377 -34 C -ATOM 1318 CE2 TYR A 213 25.287 28.190 25.946 1.00 12.74 C -ANISOU 1318 CE2 TYR A 213 1591 1979 1270 304 288 78 C -ATOM 1319 CZ TYR A 213 24.232 28.035 26.833 1.00 13.36 C -ANISOU 1319 CZ TYR A 213 1434 2099 1541 234 205 80 C -ATOM 1320 OH TYR A 213 22.926 28.175 26.413 1.00 14.73 O -ANISOU 1320 OH TYR A 213 1467 2497 1633 505 218 -86 O -ATOM 1321 N SER A 214 28.401 24.861 30.028 1.00 10.36 N -ANISOU 1321 N SER A 214 1241 1563 1129 -2 314 240 N -ATOM 1322 CA SER A 214 27.632 23.989 30.905 1.00 11.23 C -ANISOU 1322 CA SER A 214 1409 1606 1251 11 347 179 C -ATOM 1323 C SER A 214 27.269 24.780 32.140 1.00 12.45 C -ANISOU 1323 C SER A 214 1561 1725 1444 64 321 174 C -ATOM 1324 O SER A 214 28.138 25.188 32.900 1.00 12.05 O -ANISOU 1324 O SER A 214 1614 1909 1054 115 608 223 O -ATOM 1325 CB SER A 214 28.446 22.771 31.309 1.00 11.65 C -ANISOU 1325 CB SER A 214 1579 1571 1273 35 305 207 C -ATOM 1326 OG SER A 214 27.737 22.044 32.291 1.00 13.02 O -ANISOU 1326 OG SER A 214 1768 1748 1429 7 533 519 O -ATOM 1327 N VAL A 215 25.977 25.012 32.330 1.00 12.94 N -ANISOU 1327 N VAL A 215 1610 1779 1526 35 396 152 N -ATOM 1328 CA VAL A 215 25.506 25.806 33.460 1.00 14.76 C -ANISOU 1328 CA VAL A 215 1880 1959 1769 27 296 61 C -ATOM 1329 C VAL A 215 25.888 25.132 34.784 1.00 14.82 C -ANISOU 1329 C VAL A 215 1866 2042 1724 17 416 61 C -ATOM 1330 O VAL A 215 26.523 25.743 35.618 1.00 14.66 O -ANISOU 1330 O VAL A 215 1894 2255 1420 -1 794 84 O -ATOM 1331 CB VAL A 215 23.993 26.079 33.344 1.00 15.29 C -ANISOU 1331 CB VAL A 215 1881 2040 1888 26 335 36 C -ATOM 1332 CG1 VAL A 215 23.483 26.864 34.552 1.00 17.03 C -ANISOU 1332 CG1 VAL A 215 2138 2239 2093 42 310 -36 C -ATOM 1333 CG2 VAL A 215 23.682 26.820 32.027 1.00 17.22 C -ANISOU 1333 CG2 VAL A 215 2122 2151 2267 44 251 -4 C -ATOM 1334 N SER A 216 25.588 23.846 34.916 1.00 15.58 N -ANISOU 1334 N SER A 216 2032 2081 1806 28 328 62 N -ATOM 1335 CA SER A 216 25.933 23.085 36.117 1.00 16.20 C -ANISOU 1335 CA SER A 216 2132 2148 1873 -3 233 91 C -ATOM 1336 C SER A 216 27.445 22.859 36.224 1.00 16.26 C -ANISOU 1336 C SER A 216 2168 2221 1786 0 241 118 C -ATOM 1337 O SER A 216 27.991 22.721 37.320 1.00 17.40 O -ANISOU 1337 O SER A 216 2345 2574 1689 56 383 151 O -ATOM 1338 CB SER A 216 25.210 21.737 36.095 1.00 16.70 C -ANISOU 1338 CB SER A 216 2213 2217 1914 -19 232 114 C -ATOM 1339 OG SER A 216 25.802 20.883 35.133 1.00 17.35 O -ANISOU 1339 OG SER A 216 2395 2111 2084 -78 485 294 O -ATOM 1340 N GLY A 217 28.118 22.834 35.072 1.00 15.37 N -ANISOU 1340 N GLY A 217 2087 2054 1696 13 247 146 N -ATOM 1341 CA GLY A 217 29.517 22.458 34.985 1.00 15.34 C -ANISOU 1341 CA GLY A 217 2075 1979 1774 -9 122 106 C -ATOM 1342 C GLY A 217 29.713 21.020 34.546 1.00 15.78 C -ANISOU 1342 C GLY A 217 2099 2051 1845 35 90 109 C -ATOM 1343 O GLY A 217 30.794 20.661 34.108 1.00 15.70 O -ANISOU 1343 O GLY A 217 2068 2073 1821 125 168 119 O -ATOM 1344 N ALA A 218 28.673 20.197 34.662 1.00 15.24 N -ANISOU 1344 N ALA A 218 2079 1971 1739 26 123 124 N -ATOM 1345 CA ALA A 218 28.756 18.795 34.282 1.00 15.76 C -ANISOU 1345 CA ALA A 218 2100 1968 1919 28 95 122 C -ATOM 1346 C ALA A 218 28.910 18.623 32.775 1.00 15.52 C -ANISOU 1346 C ALA A 218 2117 1890 1890 35 115 164 C -ATOM 1347 O ALA A 218 28.307 19.363 31.989 1.00 14.57 O -ANISOU 1347 O ALA A 218 2080 1706 1749 47 236 375 O -ATOM 1348 CB ALA A 218 27.532 18.046 34.772 1.00 16.73 C -ANISOU 1348 CB ALA A 218 2222 2101 2030 6 121 142 C -ATOM 1349 N GLU A 219 29.705 17.632 32.382 1.00 16.12 N -ANISOU 1349 N GLU A 219 2184 1953 1987 10 71 142 N -ATOM 1350 CA GLU A 219 29.967 17.343 30.976 1.00 16.67 C -ANISOU 1350 CA GLU A 219 2212 1992 2130 -16 96 109 C -ATOM 1351 C GLU A 219 28.684 17.103 30.180 1.00 16.86 C -ANISOU 1351 C GLU A 219 2215 2028 2163 -51 113 123 C -ATOM 1352 O GLU A 219 28.535 17.568 29.050 1.00 16.76 O -ANISOU 1352 O GLU A 219 2216 2005 2147 -158 175 163 O -ATOM 1353 CB GLU A 219 30.864 16.105 30.858 1.00 17.27 C -ANISOU 1353 CB GLU A 219 2278 2053 2229 15 86 85 C -ATOM 1354 CG GLU A 219 31.492 15.913 29.484 1.00 19.58 C -ANISOU 1354 CG GLU A 219 2592 2342 2506 7 189 106 C -ATOM 1355 CD GLU A 219 32.713 16.793 29.232 1.00 21.43 C -ANISOU 1355 CD GLU A 219 2802 2528 2811 -19 195 102 C -ATOM 1356 OE1 GLU A 219 33.159 17.537 30.130 1.00 22.59 O -ANISOU 1356 OE1 GLU A 219 2847 2614 3122 -201 481 273 O -ATOM 1357 OE2 GLU A 219 33.250 16.717 28.122 1.00 23.75 O -ANISOU 1357 OE2 GLU A 219 3102 2903 3016 -455 361 381 O -ATOM 1358 N GLU A 220 27.748 16.376 30.781 1.00 17.05 N -ANISOU 1358 N GLU A 220 2271 2002 2203 -69 88 168 N -ATOM 1359 CA GLU A 220 26.516 16.008 30.093 1.00 17.61 C -ANISOU 1359 CA GLU A 220 2290 2124 2277 -56 92 131 C -ATOM 1360 C GLU A 220 25.578 17.197 29.861 1.00 16.92 C -ANISOU 1360 C GLU A 220 2208 2027 2194 -83 98 161 C -ATOM 1361 O GLU A 220 24.645 17.093 29.075 1.00 17.81 O -ANISOU 1361 O GLU A 220 2386 2074 2304 -142 96 173 O -ATOM 1362 CB GLU A 220 25.789 14.888 30.836 1.00 18.53 C -ANISOU 1362 CB GLU A 220 2410 2217 2410 -75 77 145 C -ATOM 1363 CG GLU A 220 25.267 15.282 32.208 1.00 20.37 C -ANISOU 1363 CG GLU A 220 2725 2393 2620 -105 144 168 C -ATOM 1364 CD GLU A 220 26.232 14.956 33.338 1.00 21.82 C -ANISOU 1364 CD GLU A 220 2966 2493 2830 -199 158 273 C -ATOM 1365 OE1 GLU A 220 27.466 14.945 33.101 1.00 21.37 O -ANISOU 1365 OE1 GLU A 220 3203 2100 2814 -438 237 401 O -ATOM 1366 OE2 GLU A 220 25.751 14.718 34.478 1.00 24.13 O -ANISOU 1366 OE2 GLU A 220 3424 2741 3001 -387 309 312 O -ATOM 1367 N ASP A 221 25.822 18.311 30.545 1.00 15.84 N -ANISOU 1367 N ASP A 221 2030 1948 2040 -94 159 201 N -ATOM 1368 CA ASP A 221 24.996 19.506 30.399 1.00 15.23 C -ANISOU 1368 CA ASP A 221 1894 1932 1960 -101 216 197 C -ATOM 1369 C ASP A 221 25.567 20.556 29.458 1.00 13.46 C -ANISOU 1369 C ASP A 221 1608 1759 1747 -67 299 254 C -ATOM 1370 O ASP A 221 25.019 21.653 29.374 1.00 13.72 O -ANISOU 1370 O ASP A 221 1529 1835 1847 -51 501 451 O -ATOM 1371 CB ASP A 221 24.778 20.149 31.765 1.00 15.70 C -ANISOU 1371 CB ASP A 221 1984 1982 1996 -150 227 234 C -ATOM 1372 CG ASP A 221 23.989 19.274 32.694 1.00 18.25 C -ANISOU 1372 CG ASP A 221 2274 2354 2303 -316 366 303 C -ATOM 1373 OD1 ASP A 221 23.201 18.448 32.193 1.00 21.13 O -ANISOU 1373 OD1 ASP A 221 2593 3022 2412 -563 810 636 O -ATOM 1374 OD2 ASP A 221 24.108 19.355 33.929 1.00 20.61 O -ANISOU 1374 OD2 ASP A 221 2596 2687 2548 -511 824 453 O -ATOM 1375 N PHE A 222 26.648 20.252 28.748 1.00 12.34 N -ANISOU 1375 N PHE A 222 1465 1604 1619 1 257 248 N -ATOM 1376 CA PHE A 222 27.171 21.223 27.800 1.00 11.54 C -ANISOU 1376 CA PHE A 222 1389 1545 1448 -46 207 161 C -ATOM 1377 C PHE A 222 26.120 21.547 26.740 1.00 11.30 C -ANISOU 1377 C PHE A 222 1265 1523 1505 -46 188 127 C -ATOM 1378 O PHE A 222 25.434 20.654 26.228 1.00 12.86 O -ANISOU 1378 O PHE A 222 1406 1615 1865 -130 165 246 O -ATOM 1379 CB PHE A 222 28.449 20.714 27.121 1.00 11.73 C -ANISOU 1379 CB PHE A 222 1349 1633 1474 -13 251 132 C -ATOM 1380 CG PHE A 222 29.716 21.066 27.861 1.00 11.00 C -ANISOU 1380 CG PHE A 222 1312 1566 1301 23 239 218 C -ATOM 1381 CD1 PHE A 222 30.053 22.388 28.100 1.00 9.98 C -ANISOU 1381 CD1 PHE A 222 1219 1410 1161 -1 301 211 C -ATOM 1382 CD2 PHE A 222 30.572 20.075 28.318 1.00 11.24 C -ANISOU 1382 CD2 PHE A 222 1369 1552 1348 -15 240 215 C -ATOM 1383 CE1 PHE A 222 31.214 22.716 28.773 1.00 10.17 C -ANISOU 1383 CE1 PHE A 222 1341 1468 1052 -67 240 164 C -ATOM 1384 CE2 PHE A 222 31.740 20.408 28.987 1.00 11.02 C -ANISOU 1384 CE2 PHE A 222 1312 1576 1297 88 159 219 C -ATOM 1385 CZ PHE A 222 32.055 21.727 29.212 1.00 10.77 C -ANISOU 1385 CZ PHE A 222 1205 1547 1339 -65 302 251 C -ATOM 1386 N VAL A 223 26.035 22.828 26.411 1.00 10.43 N -ANISOU 1386 N VAL A 223 1093 1485 1383 -66 249 165 N -ATOM 1387 CA VAL A 223 25.230 23.347 25.315 1.00 10.08 C -ANISOU 1387 CA VAL A 223 1057 1479 1292 -35 236 89 C -ATOM 1388 C VAL A 223 26.205 23.972 24.318 1.00 8.82 C -ANISOU 1388 C VAL A 223 825 1318 1205 -42 219 105 C -ATOM 1389 O VAL A 223 26.967 24.855 24.669 1.00 8.59 O -ANISOU 1389 O VAL A 223 961 1268 1033 -49 276 3 O -ATOM 1390 CB VAL A 223 24.244 24.414 25.819 1.00 10.69 C -ANISOU 1390 CB VAL A 223 1151 1599 1309 18 273 103 C -ATOM 1391 CG1 VAL A 223 23.513 25.057 24.660 1.00 11.99 C -ANISOU 1391 CG1 VAL A 223 1264 1722 1569 124 257 122 C -ATOM 1392 CG2 VAL A 223 23.257 23.799 26.816 1.00 12.04 C -ANISOU 1392 CG2 VAL A 223 1234 1875 1463 67 365 110 C -ATOM 1393 N LEU A 224 26.168 23.493 23.088 1.00 8.70 N -ANISOU 1393 N LEU A 224 911 1156 1235 -75 226 72 N -ATOM 1394 CA LEU A 224 27.019 23.989 22.026 1.00 8.23 C -ANISOU 1394 CA LEU A 224 922 1110 1093 -52 157 32 C -ATOM 1395 C LEU A 224 26.317 25.098 21.264 1.00 7.49 C -ANISOU 1395 C LEU A 224 799 1026 1019 -19 129 -16 C -ATOM 1396 O LEU A 224 25.157 24.945 20.894 1.00 8.97 O -ANISOU 1396 O LEU A 224 810 1261 1337 -102 60 -2 O -ATOM 1397 CB LEU A 224 27.327 22.825 21.093 1.00 9.17 C -ANISOU 1397 CB LEU A 224 1020 1219 1242 -78 202 6 C -ATOM 1398 CG LEU A 224 28.348 23.056 19.987 1.00 9.77 C -ANISOU 1398 CG LEU A 224 1242 1286 1180 -7 96 -21 C -ATOM 1399 CD1 LEU A 224 29.725 23.376 20.537 1.00 9.18 C -ANISOU 1399 CD1 LEU A 224 998 1208 1283 -89 234 -76 C -ATOM 1400 CD2 LEU A 224 28.410 21.834 19.078 1.00 10.60 C -ANISOU 1400 CD2 LEU A 224 1195 1360 1470 -114 122 -291 C -ATOM 1401 N LEU A 225 26.994 26.218 21.040 1.00 7.19 N -ANISOU 1401 N LEU A 225 804 1023 902 4 79 -6 N -ATOM 1402 CA LEU A 225 26.421 27.253 20.188 1.00 7.00 C -ANISOU 1402 CA LEU A 225 748 955 956 38 77 -16 C -ATOM 1403 C LEU A 225 26.317 26.770 18.758 1.00 6.71 C -ANISOU 1403 C LEU A 225 713 865 968 51 13 -16 C -ATOM 1404 O LEU A 225 27.252 26.178 18.231 1.00 7.13 O -ANISOU 1404 O LEU A 225 790 883 1037 105 -20 -117 O -ATOM 1405 CB LEU A 225 27.243 28.549 20.247 1.00 6.82 C -ANISOU 1405 CB LEU A 225 754 971 867 9 54 -99 C -ATOM 1406 CG LEU A 225 27.296 29.274 21.595 1.00 8.80 C -ANISOU 1406 CG LEU A 225 1091 1242 1010 29 90 -98 C -ATOM 1407 CD1 LEU A 225 27.938 30.630 21.427 1.00 8.14 C -ANISOU 1407 CD1 LEU A 225 974 1011 1105 176 -40 -235 C -ATOM 1408 CD2 LEU A 225 25.946 29.449 22.241 1.00 10.97 C -ANISOU 1408 CD2 LEU A 225 1444 1491 1230 -76 111 -200 C -ATOM 1409 N GLY A 226 25.175 27.033 18.133 1.00 7.08 N -ANISOU 1409 N GLY A 226 746 929 1014 54 24 -67 N -ATOM 1410 CA GLY A 226 25.039 26.869 16.704 1.00 6.86 C -ANISOU 1410 CA GLY A 226 773 837 996 84 -25 -108 C -ATOM 1411 C GLY A 226 25.896 27.870 15.955 1.00 6.61 C -ANISOU 1411 C GLY A 226 685 807 1019 70 -25 -145 C -ATOM 1412 O GLY A 226 26.406 28.821 16.539 1.00 7.19 O -ANISOU 1412 O GLY A 226 854 761 1113 -37 -9 -210 O -ATOM 1413 N TYR A 227 26.044 27.687 14.646 1.00 6.91 N -ANISOU 1413 N TYR A 227 781 835 1007 -33 29 -166 N -ATOM 1414 CA TYR A 227 26.919 28.543 13.853 1.00 7.24 C -ANISOU 1414 CA TYR A 227 769 958 1024 2 74 -213 C -ATOM 1415 C TYR A 227 26.574 30.023 13.980 1.00 6.76 C -ANISOU 1415 C TYR A 227 751 954 861 -7 98 -228 C -ATOM 1416 O TYR A 227 27.445 30.851 14.203 1.00 6.25 O -ANISOU 1416 O TYR A 227 736 877 761 -117 102 -198 O -ATOM 1417 CB TYR A 227 26.930 28.122 12.352 1.00 7.91 C -ANISOU 1417 CB TYR A 227 861 1032 1113 -74 180 -343 C -ATOM 1418 CG TYR A 227 27.696 29.136 11.473 1.00 9.15 C -ANISOU 1418 CG TYR A 227 1058 1128 1291 -125 128 -539 C -ATOM 1419 CD1 TYR A 227 29.083 29.141 11.432 1.00 10.29 C -ANISOU 1419 CD1 TYR A 227 1215 1089 1604 45 -1 -336 C -ATOM 1420 CD2 TYR A 227 27.011 30.140 10.784 1.00 10.53 C -ANISOU 1420 CD2 TYR A 227 1443 1373 1183 -160 158 -149 C -ATOM 1421 CE1 TYR A 227 29.782 30.112 10.719 1.00 8.22 C -ANISOU 1421 CE1 TYR A 227 1129 903 1091 -52 312 -114 C -ATOM 1422 CE2 TYR A 227 27.690 31.107 10.066 1.00 10.52 C -ANISOU 1422 CE2 TYR A 227 1357 1311 1328 185 -27 104 C -ATOM 1423 CZ TYR A 227 29.078 31.065 10.038 1.00 9.31 C -ANISOU 1423 CZ TYR A 227 1053 1274 1209 247 -15 -230 C -ATOM 1424 OH TYR A 227 29.796 32.020 9.359 1.00 10.28 O -ANISOU 1424 OH TYR A 227 1245 1307 1352 49 93 37 O -ATOM 1425 N ASP A 228 25.310 30.366 13.791 1.00 7.22 N -ANISOU 1425 N ASP A 228 775 939 1026 2 -40 -155 N -ATOM 1426 CA ASP A 228 24.946 31.778 13.815 1.00 7.96 C -ANISOU 1426 CA ASP A 228 918 1043 1064 19 -35 -98 C -ATOM 1427 C ASP A 228 25.205 32.398 15.177 1.00 7.24 C -ANISOU 1427 C ASP A 228 826 895 1027 105 -23 -120 C -ATOM 1428 O ASP A 228 25.679 33.525 15.246 1.00 7.82 O -ANISOU 1428 O ASP A 228 1041 880 1050 120 -20 -95 O -ATOM 1429 CB ASP A 228 23.484 31.992 13.407 1.00 9.17 C -ANISOU 1429 CB ASP A 228 1005 1185 1294 -15 -193 -47 C -ATOM 1430 CG ASP A 228 23.252 31.843 11.931 1.00 11.34 C -ANISOU 1430 CG ASP A 228 1204 1629 1476 -18 -180 3 C -ATOM 1431 OD1 ASP A 228 24.163 32.145 11.128 1.00 13.40 O -ANISOU 1431 OD1 ASP A 228 1646 2215 1228 -106 -400 -120 O -ATOM 1432 OD2 ASP A 228 22.162 31.439 11.489 1.00 14.93 O -ANISOU 1432 OD2 ASP A 228 1601 2246 1824 -170 -564 99 O -ATOM 1433 N GLU A 229 24.890 31.673 16.250 1.00 7.21 N -ANISOU 1433 N GLU A 229 805 883 1052 77 32 -179 N -ATOM 1434 CA GLU A 229 25.155 32.179 17.590 1.00 7.44 C -ANISOU 1434 CA GLU A 229 923 941 961 50 117 -130 C -ATOM 1435 C GLU A 229 26.655 32.275 17.870 1.00 6.13 C -ANISOU 1435 C GLU A 229 752 789 786 21 157 -132 C -ATOM 1436 O GLU A 229 27.114 33.219 18.502 1.00 6.44 O -ANISOU 1436 O GLU A 229 846 792 805 69 112 -158 O -ATOM 1437 CB GLU A 229 24.560 31.264 18.656 1.00 9.08 C -ANISOU 1437 CB GLU A 229 1083 1342 1025 33 303 -238 C -ATOM 1438 CG GLU A 229 23.087 30.921 18.670 1.00 13.85 C -ANISOU 1438 CG GLU A 229 1646 1902 1712 61 145 -88 C -ATOM 1439 CD GLU A 229 22.817 29.847 19.722 1.00 18.14 C -ANISOU 1439 CD GLU A 229 2025 2446 2420 225 300 -57 C -ATOM 1440 OE1 GLU A 229 23.134 28.620 19.554 1.00 17.67 O -ANISOU 1440 OE1 GLU A 229 1535 2741 2436 732 602 284 O -ATOM 1441 OE2 GLU A 229 22.359 30.263 20.782 1.00 22.73 O -ANISOU 1441 OE2 GLU A 229 2889 2959 2786 523 158 -336 O -ATOM 1442 N PHE A 230 27.411 31.281 17.400 1.00 5.77 N -ANISOU 1442 N PHE A 230 699 681 809 31 64 -138 N -ATOM 1443 CA PHE A 230 28.858 31.280 17.530 1.00 5.97 C -ANISOU 1443 CA PHE A 230 728 777 761 48 81 -86 C -ATOM 1444 C PHE A 230 29.440 32.551 16.899 1.00 5.37 C -ANISOU 1444 C PHE A 230 630 704 706 6 39 -128 C -ATOM 1445 O PHE A 230 30.287 33.219 17.494 1.00 5.87 O -ANISOU 1445 O PHE A 230 689 773 768 13 52 -114 O -ATOM 1446 CB PHE A 230 29.439 30.020 16.878 1.00 5.88 C -ANISOU 1446 CB PHE A 230 759 748 724 26 127 -112 C -ATOM 1447 CG PHE A 230 30.927 30.071 16.714 1.00 5.41 C -ANISOU 1447 CG PHE A 230 652 690 711 23 127 -60 C -ATOM 1448 CD1 PHE A 230 31.768 29.788 17.779 1.00 5.23 C -ANISOU 1448 CD1 PHE A 230 796 610 580 66 126 -76 C -ATOM 1449 CD2 PHE A 230 31.489 30.414 15.503 1.00 6.29 C -ANISOU 1449 CD2 PHE A 230 903 894 591 80 18 -87 C -ATOM 1450 CE1 PHE A 230 33.141 29.846 17.624 1.00 6.07 C -ANISOU 1450 CE1 PHE A 230 772 760 773 106 69 0 C -ATOM 1451 CE2 PHE A 230 32.870 30.471 15.352 1.00 6.24 C -ANISOU 1451 CE2 PHE A 230 656 826 885 95 190 56 C -ATOM 1452 CZ PHE A 230 33.691 30.207 16.413 1.00 6.03 C -ANISOU 1452 CZ PHE A 230 665 687 935 152 174 -128 C -ATOM 1453 N VAL A 231 29.005 32.874 15.692 1.00 6.02 N -ANISOU 1453 N VAL A 231 806 762 719 -4 18 -141 N -ATOM 1454 CA VAL A 231 29.494 34.075 15.026 1.00 7.26 C -ANISOU 1454 CA VAL A 231 1051 875 831 -33 -40 -105 C -ATOM 1455 C VAL A 231 29.042 35.345 15.750 1.00 7.15 C -ANISOU 1455 C VAL A 231 1009 897 810 -23 -114 -78 C -ATOM 1456 O VAL A 231 29.809 36.292 15.914 1.00 7.68 O -ANISOU 1456 O VAL A 231 1107 844 966 -57 -163 -41 O -ATOM 1457 CB VAL A 231 29.039 34.095 13.559 1.00 8.59 C -ANISOU 1457 CB VAL A 231 1406 921 936 -21 42 -85 C -ATOM 1458 CG1 VAL A 231 29.184 35.478 12.942 1.00 9.90 C -ANISOU 1458 CG1 VAL A 231 1427 1171 1160 1 -20 -138 C -ATOM 1459 CG2 VAL A 231 29.770 33.030 12.771 1.00 9.96 C -ANISOU 1459 CG2 VAL A 231 1572 1152 1060 -63 84 -111 C -ATOM 1460 N GLU A 232 27.795 35.382 16.192 1.00 7.19 N -ANISOU 1460 N GLU A 232 990 841 898 84 -148 -100 N -ATOM 1461 CA GLU A 232 27.276 36.556 16.891 1.00 8.30 C -ANISOU 1461 CA GLU A 232 1180 962 1011 122 -125 -113 C -ATOM 1462 C GLU A 232 28.099 36.848 18.136 1.00 7.68 C -ANISOU 1462 C GLU A 232 1124 837 957 129 -136 -107 C -ATOM 1463 O GLU A 232 28.558 37.970 18.328 1.00 9.16 O -ANISOU 1463 O GLU A 232 1647 850 983 103 -298 -58 O -ATOM 1464 CB GLU A 232 25.816 36.329 17.257 1.00 9.62 C -ANISOU 1464 CB GLU A 232 1260 1160 1234 235 -137 -197 C -ATOM 1465 CG GLU A 232 25.122 37.393 18.094 1.00 16.37 C -ANISOU 1465 CG GLU A 232 2061 2171 1988 153 -92 -247 C -ATOM 1466 CD GLU A 232 23.752 36.913 18.571 1.00 22.64 C -ANISOU 1466 CD GLU A 232 2843 3210 2546 55 -99 -329 C -ATOM 1467 OE1 GLU A 232 23.463 36.970 19.792 1.00 27.98 O -ANISOU 1467 OE1 GLU A 232 3432 4141 3058 156 -91 -336 O -ATOM 1468 OE2 GLU A 232 22.958 36.454 17.717 1.00 28.26 O -ANISOU 1468 OE2 GLU A 232 3207 4231 3297 115 -204 -369 O -ATOM 1469 N PHE A 233 28.283 35.851 18.984 1.00 6.42 N -ANISOU 1469 N PHE A 233 933 812 693 67 1 -128 N -ATOM 1470 CA PHE A 233 29.073 36.053 20.182 1.00 6.59 C -ANISOU 1470 CA PHE A 233 938 840 724 99 -10 -109 C -ATOM 1471 C PHE A 233 30.542 36.335 19.861 1.00 5.94 C -ANISOU 1471 C PHE A 233 885 740 631 90 -52 -165 C -ATOM 1472 O PHE A 233 31.124 37.248 20.425 1.00 6.73 O -ANISOU 1472 O PHE A 233 974 812 769 35 -100 -228 O -ATOM 1473 CB PHE A 233 28.918 34.851 21.126 1.00 7.35 C -ANISOU 1473 CB PHE A 233 1038 973 779 64 -6 -125 C -ATOM 1474 CG PHE A 233 27.628 34.870 21.910 1.00 8.06 C -ANISOU 1474 CG PHE A 233 1255 1091 714 -18 198 -241 C -ATOM 1475 CD1 PHE A 233 27.508 35.630 23.064 1.00 11.39 C -ANISOU 1475 CD1 PHE A 233 1546 1656 1124 -125 249 -328 C -ATOM 1476 CD2 PHE A 233 26.518 34.163 21.494 1.00 9.90 C -ANISOU 1476 CD2 PHE A 233 1380 1369 1011 -96 332 -302 C -ATOM 1477 CE1 PHE A 233 26.307 35.669 23.781 1.00 11.72 C -ANISOU 1477 CE1 PHE A 233 1753 1731 966 -162 259 -620 C -ATOM 1478 CE2 PHE A 233 25.323 34.204 22.217 1.00 11.98 C -ANISOU 1478 CE2 PHE A 233 1614 1869 1066 -209 223 -414 C -ATOM 1479 CZ PHE A 233 25.219 34.953 23.352 1.00 12.17 C -ANISOU 1479 CZ PHE A 233 1641 1850 1132 -153 336 -408 C -ATOM 1480 N SER A 234 31.141 35.562 18.961 1.00 5.65 N -ANISOU 1480 N SER A 234 790 704 653 -2 -25 -163 N -ATOM 1481 CA SER A 234 32.563 35.737 18.674 1.00 6.07 C -ANISOU 1481 CA SER A 234 829 709 766 48 -15 -100 C -ATOM 1482 C SER A 234 32.854 37.127 18.121 1.00 6.37 C -ANISOU 1482 C SER A 234 809 763 846 21 4 -108 C -ATOM 1483 O SER A 234 33.880 37.712 18.422 1.00 6.95 O -ANISOU 1483 O SER A 234 922 671 1046 -34 1 -102 O -ATOM 1484 CB SER A 234 33.056 34.677 17.690 1.00 6.06 C -ANISOU 1484 CB SER A 234 710 823 768 75 -30 -69 C -ATOM 1485 OG SER A 234 33.032 33.383 18.253 1.00 6.86 O -ANISOU 1485 OG SER A 234 886 681 1037 97 0 -80 O -ATOM 1486 N SER A 235 31.927 37.648 17.327 1.00 6.64 N -ANISOU 1486 N SER A 235 917 808 796 -54 -42 -58 N -ATOM 1487 CA SER A 235 32.088 38.960 16.730 1.00 8.07 C -ANISOU 1487 CA SER A 235 1079 953 1032 -29 -58 61 C -ATOM 1488 C SER A 235 32.074 40.074 17.772 1.00 8.02 C -ANISOU 1488 C SER A 235 1095 840 1112 -14 -143 22 C -ATOM 1489 O SER A 235 32.512 41.179 17.487 1.00 9.81 O -ANISOU 1489 O SER A 235 1516 866 1343 -155 -58 60 O -ATOM 1490 CB SER A 235 30.990 39.214 15.689 1.00 9.11 C -ANISOU 1490 CB SER A 235 1259 1116 1085 -54 -67 108 C -ATOM 1491 OG SER A 235 29.741 39.475 16.288 1.00 11.64 O -ANISOU 1491 OG SER A 235 1518 1472 1432 -129 -382 449 O -ATOM 1492 N LYS A 236 31.562 39.791 18.961 1.00 7.48 N -ANISOU 1492 N LYS A 236 1061 701 1078 116 -173 -45 N -ATOM 1493 CA LYS A 236 31.507 40.755 20.050 1.00 8.33 C -ANISOU 1493 CA LYS A 236 1129 850 1183 139 -124 -103 C -ATOM 1494 C LYS A 236 32.664 40.610 21.030 1.00 7.71 C -ANISOU 1494 C LYS A 236 1111 770 1046 195 -181 -163 C -ATOM 1495 O LYS A 236 32.768 41.369 21.982 1.00 9.97 O -ANISOU 1495 O LYS A 236 1355 1046 1387 390 -242 -485 O -ATOM 1496 CB LYS A 236 30.182 40.620 20.791 1.00 9.18 C -ANISOU 1496 CB LYS A 236 1220 985 1281 209 -146 -88 C -ATOM 1497 CG LYS A 236 28.984 40.959 19.941 1.00 11.90 C -ANISOU 1497 CG LYS A 236 1407 1323 1788 166 -151 -148 C -ATOM 1498 CD LYS A 236 27.680 40.728 20.698 1.00 15.72 C -ANISOU 1498 CD LYS A 236 1878 1944 2149 89 -128 -85 C -ATOM 1499 CE LYS A 236 26.461 40.951 19.825 1.00 18.83 C -ANISOU 1499 CE LYS A 236 2182 2400 2571 75 -50 -68 C -ATOM 1500 NZ LYS A 236 25.221 40.474 20.501 1.00 23.29 N -ANISOU 1500 NZ LYS A 236 2819 2845 3185 -17 138 -65 N -ATOM 1501 N VAL A 237 33.530 39.630 20.824 1.00 7.05 N -ANISOU 1501 N VAL A 237 980 753 944 210 -117 -170 N -ATOM 1502 CA VAL A 237 34.682 39.423 21.688 1.00 7.08 C -ANISOU 1502 CA VAL A 237 1017 783 889 87 -115 -142 C -ATOM 1503 C VAL A 237 35.854 40.128 21.004 1.00 6.95 C -ANISOU 1503 C VAL A 237 1019 715 907 131 -154 -225 C -ATOM 1504 O VAL A 237 36.223 39.774 19.891 1.00 7.15 O -ANISOU 1504 O VAL A 237 1087 660 968 77 -130 -164 O -ATOM 1505 CB VAL A 237 34.966 37.932 21.869 1.00 6.70 C -ANISOU 1505 CB VAL A 237 1010 806 730 94 -117 -190 C -ATOM 1506 CG1 VAL A 237 36.233 37.736 22.678 1.00 7.71 C -ANISOU 1506 CG1 VAL A 237 992 982 956 55 -210 -115 C -ATOM 1507 CG2 VAL A 237 33.807 37.235 22.539 1.00 7.40 C -ANISOU 1507 CG2 VAL A 237 1115 907 788 118 -119 -49 C -ATOM 1508 N PRO A 238 36.429 41.156 21.629 1.00 7.80 N -ANISOU 1508 N PRO A 238 1091 786 1085 85 -68 -213 N -ATOM 1509 CA PRO A 238 37.351 42.034 20.903 1.00 7.31 C -ANISOU 1509 CA PRO A 238 1070 662 1042 97 -80 -209 C -ATOM 1510 C PRO A 238 38.607 41.300 20.442 1.00 7.45 C -ANISOU 1510 C PRO A 238 1099 591 1138 104 -98 -179 C -ATOM 1511 O PRO A 238 39.302 40.676 21.236 1.00 7.80 O -ANISOU 1511 O PRO A 238 1160 727 1074 160 -191 -157 O -ATOM 1512 CB PRO A 238 37.703 43.117 21.945 1.00 8.39 C -ANISOU 1512 CB PRO A 238 1186 758 1244 36 -15 -298 C -ATOM 1513 CG PRO A 238 37.468 42.480 23.263 1.00 9.12 C -ANISOU 1513 CG PRO A 238 1340 954 1172 102 -144 -367 C -ATOM 1514 CD PRO A 238 36.278 41.586 23.033 1.00 8.46 C -ANISOU 1514 CD PRO A 238 1172 929 1111 39 -143 -277 C -ATOM 1515 N ASN A 239 38.887 41.433 19.157 1.00 7.49 N -ANISOU 1515 N ASN A 239 1076 568 1200 79 -66 -14 N -ATOM 1516 CA ASN A 239 40.049 40.850 18.509 1.00 7.61 C -ANISOU 1516 CA ASN A 239 1046 694 1151 -1 0 -62 C -ATOM 1517 C ASN A 239 40.062 39.329 18.476 1.00 6.87 C -ANISOU 1517 C ASN A 239 959 598 1053 24 23 -102 C -ATOM 1518 O ASN A 239 41.108 38.726 18.303 1.00 8.98 O -ANISOU 1518 O ASN A 239 1025 768 1615 25 89 -190 O -ATOM 1519 CB ASN A 239 41.345 41.421 19.100 1.00 8.89 C -ANISOU 1519 CB ASN A 239 1198 797 1380 -42 43 -113 C -ATOM 1520 CG ASN A 239 41.437 42.911 18.908 1.00 10.73 C -ANISOU 1520 CG ASN A 239 1502 1006 1567 -249 35 -202 C -ATOM 1521 OD1 ASN A 239 41.565 43.687 19.874 1.00 13.13 O -ANISOU 1521 OD1 ASN A 239 1800 1159 2029 -227 9 -474 O -ATOM 1522 ND2 ASN A 239 41.310 43.338 17.670 1.00 11.23 N -ANISOU 1522 ND2 ASN A 239 2070 720 1475 -347 367 -280 N -ATOM 1523 N LEU A 240 38.906 38.699 18.628 1.00 6.33 N -ANISOU 1523 N LEU A 240 878 501 1025 71 -67 -31 N -ATOM 1524 CA LEU A 240 38.835 37.260 18.480 1.00 5.88 C -ANISOU 1524 CA LEU A 240 894 555 782 106 -62 -37 C -ATOM 1525 C LEU A 240 38.710 36.909 17.002 1.00 5.94 C -ANISOU 1525 C LEU A 240 834 607 816 81 -42 12 C -ATOM 1526 O LEU A 240 37.755 37.330 16.346 1.00 7.43 O -ANISOU 1526 O LEU A 240 1044 843 934 239 -156 -110 O -ATOM 1527 CB LEU A 240 37.652 36.692 19.242 1.00 6.12 C -ANISOU 1527 CB LEU A 240 888 658 776 79 -37 -25 C -ATOM 1528 CG LEU A 240 37.560 35.165 19.238 1.00 5.58 C -ANISOU 1528 CG LEU A 240 893 485 739 65 -74 -99 C -ATOM 1529 CD1 LEU A 240 38.779 34.527 19.900 1.00 7.37 C -ANISOU 1529 CD1 LEU A 240 975 768 1054 35 -72 86 C -ATOM 1530 CD2 LEU A 240 36.280 34.719 19.917 1.00 7.15 C -ANISOU 1530 CD2 LEU A 240 978 611 1127 72 -28 16 C -ATOM 1531 N LEU A 241 39.662 36.148 16.486 1.00 5.53 N -ANISOU 1531 N LEU A 241 794 592 713 40 -37 -8 N -ATOM 1532 CA LEU A 241 39.554 35.557 15.170 1.00 5.67 C -ANISOU 1532 CA LEU A 241 776 685 691 43 43 69 C -ATOM 1533 C LEU A 241 38.723 34.293 15.250 1.00 5.18 C -ANISOU 1533 C LEU A 241 765 637 565 51 55 37 C -ATOM 1534 O LEU A 241 38.920 33.501 16.165 1.00 5.39 O -ANISOU 1534 O LEU A 241 876 575 593 22 -19 57 O -ATOM 1535 CB LEU A 241 40.940 35.203 14.693 1.00 6.87 C -ANISOU 1535 CB LEU A 241 817 843 949 -35 -47 58 C -ATOM 1536 CG LEU A 241 41.057 34.675 13.300 1.00 10.90 C -ANISOU 1536 CG LEU A 241 1352 1389 1399 81 19 -47 C -ATOM 1537 CD1 LEU A 241 40.632 35.696 12.263 1.00 14.35 C -ANISOU 1537 CD1 LEU A 241 1824 1947 1680 193 133 -15 C -ATOM 1538 CD2 LEU A 241 42.495 34.257 13.101 1.00 12.47 C -ANISOU 1538 CD2 LEU A 241 1443 1703 1589 86 79 -49 C -ATOM 1539 N TYR A 242 37.825 34.094 14.294 1.00 5.77 N -ANISOU 1539 N TYR A 242 833 736 624 -54 3 156 N -ATOM 1540 CA TYR A 242 36.907 32.968 14.366 1.00 6.27 C -ANISOU 1540 CA TYR A 242 875 855 651 -64 19 66 C -ATOM 1541 C TYR A 242 36.560 32.453 12.987 1.00 5.79 C -ANISOU 1541 C TYR A 242 755 889 554 -101 -65 123 C -ATOM 1542 O TYR A 242 36.647 33.158 11.996 1.00 7.52 O -ANISOU 1542 O TYR A 242 1089 1151 615 -161 -42 175 O -ATOM 1543 CB TYR A 242 35.637 33.338 15.167 1.00 6.48 C -ANISOU 1543 CB TYR A 242 831 874 757 -97 -12 19 C -ATOM 1544 CG TYR A 242 34.825 34.445 14.570 1.00 7.39 C -ANISOU 1544 CG TYR A 242 867 980 960 -95 122 44 C -ATOM 1545 CD1 TYR A 242 33.820 34.167 13.660 1.00 8.98 C -ANISOU 1545 CD1 TYR A 242 890 1178 1343 68 10 183 C -ATOM 1546 CD2 TYR A 242 35.068 35.766 14.893 1.00 9.16 C -ANISOU 1546 CD2 TYR A 242 1147 1127 1206 103 98 153 C -ATOM 1547 CE1 TYR A 242 33.080 35.177 13.089 1.00 12.00 C -ANISOU 1547 CE1 TYR A 242 1141 1701 1715 208 8 337 C -ATOM 1548 CE2 TYR A 242 34.326 36.800 14.306 1.00 11.19 C -ANISOU 1548 CE2 TYR A 242 1409 1105 1737 206 165 246 C -ATOM 1549 CZ TYR A 242 33.327 36.485 13.412 1.00 12.73 C -ANISOU 1549 CZ TYR A 242 1420 1690 1726 253 172 427 C -ATOM 1550 OH TYR A 242 32.567 37.453 12.822 1.00 18.33 O -ANISOU 1550 OH TYR A 242 1953 2161 2850 326 117 589 O -ATOM 1551 N ALA A 243 36.145 31.196 12.961 1.00 6.23 N -ANISOU 1551 N ALA A 243 868 935 563 -65 4 -38 N -ATOM 1552 CA ALA A 243 35.753 30.512 11.743 1.00 6.83 C -ANISOU 1552 CA ALA A 243 816 1065 714 -4 -55 -110 C -ATOM 1553 C ALA A 243 34.511 31.147 11.153 1.00 7.34 C -ANISOU 1553 C ALA A 243 868 1194 724 50 0 -114 C -ATOM 1554 O ALA A 243 33.491 31.279 11.815 1.00 9.92 O -ANISOU 1554 O ALA A 243 910 1764 1094 134 -36 -38 O -ATOM 1555 CB ALA A 243 35.491 29.061 12.046 1.00 7.72 C -ANISOU 1555 CB ALA A 243 1067 1178 686 -20 -54 -169 C -ATOM 1556 N ARG A 244 34.626 31.574 9.908 1.00 8.03 N -ANISOU 1556 N ARG A 244 982 1259 807 139 -77 -72 N -ATOM 1557 CA ARG A 244 33.524 32.200 9.191 1.00 9.21 C -ANISOU 1557 CA ARG A 244 1221 1202 1073 147 -112 -109 C -ATOM 1558 C ARG A 244 33.220 31.423 7.931 1.00 7.37 C -ANISOU 1558 C ARG A 244 1040 962 796 100 -114 -100 C -ATOM 1559 O ARG A 244 34.126 30.957 7.237 1.00 7.97 O -ANISOU 1559 O ARG A 244 1006 1246 776 125 -103 0 O -ATOM 1560 CB ARG A 244 33.879 33.637 8.815 1.00 11.88 C -ANISOU 1560 CB ARG A 244 1580 1460 1473 92 -201 -150 C -ATOM 1561 CG ARG A 244 33.823 34.612 9.968 1.00 15.64 C -ANISOU 1561 CG ARG A 244 2068 1988 1886 81 -203 -51 C -ATOM 1562 CD ARG A 244 33.913 36.059 9.546 1.00 21.76 C -ANISOU 1562 CD ARG A 244 2843 2671 2751 19 -88 -57 C -ATOM 1563 NE ARG A 244 32.599 36.600 9.181 1.00 26.84 N -ANISOU 1563 NE ARG A 244 3401 3426 3370 31 -56 34 N -ATOM 1564 CZ ARG A 244 32.152 36.823 7.941 1.00 30.18 C -ANISOU 1564 CZ ARG A 244 3810 3873 3782 32 -8 2 C -ATOM 1565 NH1 ARG A 244 32.899 36.555 6.871 1.00 32.17 N -ANISOU 1565 NH1 ARG A 244 4076 4071 4074 30 25 33 N -ATOM 1566 NH2 ARG A 244 30.929 37.325 7.771 1.00 31.73 N -ANISOU 1566 NH2 ARG A 244 4015 4081 3959 58 31 -1 N -ATOM 1567 N ALA A 245 31.945 31.334 7.605 1.00 7.44 N -ANISOU 1567 N ALA A 245 1024 954 848 236 -44 -94 N -ATOM 1568 CA ALA A 245 31.513 30.532 6.477 1.00 7.08 C -ANISOU 1568 CA ALA A 245 1005 866 816 123 -14 -15 C -ATOM 1569 C ALA A 245 32.079 31.037 5.154 1.00 6.63 C -ANISOU 1569 C ALA A 245 995 769 755 181 -26 21 C -ATOM 1570 O ALA A 245 31.967 32.224 4.830 1.00 8.36 O -ANISOU 1570 O ALA A 245 1456 721 999 207 6 91 O -ATOM 1571 CB ALA A 245 30.004 30.502 6.410 1.00 8.07 C -ANISOU 1571 CB ALA A 245 1065 1088 910 104 3 -27 C -ATOM 1572 N LEU A 246 32.673 30.116 4.412 1.00 6.45 N -ANISOU 1572 N LEU A 246 960 726 761 121 26 68 N -ATOM 1573 CA LEU A 246 33.148 30.319 3.054 1.00 7.16 C -ANISOU 1573 CA LEU A 246 1024 901 795 -13 0 69 C -ATOM 1574 C LEU A 246 32.042 30.063 2.046 1.00 7.96 C -ANISOU 1574 C LEU A 246 1150 1057 815 90 -75 142 C -ATOM 1575 O LEU A 246 32.049 30.613 0.943 1.00 9.70 O -ANISOU 1575 O LEU A 246 1410 1422 850 -58 -185 307 O -ATOM 1576 CB LEU A 246 34.289 29.351 2.786 1.00 7.36 C -ANISOU 1576 CB LEU A 246 1010 971 815 -30 42 53 C -ATOM 1577 CG LEU A 246 35.485 29.487 3.723 1.00 8.34 C -ANISOU 1577 CG LEU A 246 1014 1177 978 -9 122 19 C -ATOM 1578 CD1 LEU A 246 36.319 28.224 3.681 1.00 8.16 C -ANISOU 1578 CD1 LEU A 246 1067 1245 787 126 -40 21 C -ATOM 1579 CD2 LEU A 246 36.327 30.698 3.371 1.00 11.23 C -ANISOU 1579 CD2 LEU A 246 1385 1369 1511 -42 73 21 C -ATOM 1580 N VAL A 247 31.129 29.180 2.418 1.00 7.89 N -ANISOU 1580 N VAL A 247 1071 1121 802 19 -156 58 N -ATOM 1581 CA VAL A 247 29.928 28.863 1.674 1.00 8.60 C -ANISOU 1581 CA VAL A 247 1142 1132 992 39 -112 -31 C -ATOM 1582 C VAL A 247 28.893 28.400 2.690 1.00 7.60 C -ANISOU 1582 C VAL A 247 970 984 932 75 -134 42 C -ATOM 1583 O VAL A 247 29.244 27.873 3.760 1.00 7.67 O -ANISOU 1583 O VAL A 247 1036 966 912 67 -213 120 O -ATOM 1584 CB VAL A 247 30.189 27.794 0.559 1.00 10.09 C -ANISOU 1584 CB VAL A 247 1262 1445 1123 23 -126 -172 C -ATOM 1585 CG1 VAL A 247 30.693 26.520 1.131 1.00 11.96 C -ANISOU 1585 CG1 VAL A 247 1617 1561 1366 -112 -61 -200 C -ATOM 1586 CG2 VAL A 247 28.960 27.559 -0.292 1.00 13.81 C -ANISOU 1586 CG2 VAL A 247 1727 1926 1594 102 -150 -262 C -ATOM 1587 N ARG A 248 27.626 28.610 2.372 1.00 8.03 N -ANISOU 1587 N ARG A 248 1012 1059 980 119 -119 161 N -ATOM 1588 CA ARG A 248 26.515 28.215 3.215 1.00 8.45 C -ANISOU 1588 CA ARG A 248 1042 1101 1066 84 -162 80 C -ATOM 1589 C ARG A 248 25.436 27.690 2.296 1.00 8.57 C -ANISOU 1589 C ARG A 248 1053 1139 1061 81 -186 121 C -ATOM 1590 O ARG A 248 25.138 28.306 1.266 1.00 10.13 O -ANISOU 1590 O ARG A 248 1320 1309 1218 37 -402 327 O -ATOM 1591 CB ARG A 248 26.011 29.411 4.010 1.00 8.73 C -ANISOU 1591 CB ARG A 248 1018 1145 1151 34 -159 67 C -ATOM 1592 CG ARG A 248 24.874 29.107 4.946 1.00 10.20 C -ANISOU 1592 CG ARG A 248 1251 1328 1294 178 -92 -58 C -ATOM 1593 CD ARG A 248 24.629 30.221 5.889 1.00 12.56 C -ANISOU 1593 CD ARG A 248 1517 1713 1540 -16 -9 -161 C -ATOM 1594 NE ARG A 248 23.535 29.925 6.797 1.00 12.40 N -ANISOU 1594 NE ARG A 248 1630 1566 1515 94 -76 -225 N -ATOM 1595 CZ ARG A 248 23.450 30.417 8.019 1.00 12.07 C -ANISOU 1595 CZ ARG A 248 1530 1641 1413 142 -111 -123 C -ATOM 1596 NH1 ARG A 248 24.393 31.211 8.491 1.00 14.93 N -ANISOU 1596 NH1 ARG A 248 1677 2242 1752 -57 -242 -75 N -ATOM 1597 NH2 ARG A 248 22.412 30.111 8.783 1.00 12.80 N -ANISOU 1597 NH2 ARG A 248 1444 1780 1637 160 -101 -117 N -ATOM 1598 N GLY A 249 24.828 26.579 2.659 1.00 7.88 N -ANISOU 1598 N GLY A 249 980 1038 977 71 -189 31 N -ATOM 1599 CA GLY A 249 23.780 25.988 1.840 1.00 8.60 C -ANISOU 1599 CA GLY A 249 1086 1113 1067 34 -142 -25 C -ATOM 1600 C GLY A 249 23.474 24.582 2.289 1.00 8.01 C -ANISOU 1600 C GLY A 249 988 1070 985 55 -110 -53 C -ATOM 1601 O GLY A 249 23.702 24.219 3.439 1.00 8.57 O -ANISOU 1601 O GLY A 249 1084 1180 992 -2 -130 -34 O -ATOM 1602 N THR A 250 22.967 23.762 1.382 1.00 7.92 N -ANISOU 1602 N THR A 250 904 1064 1040 113 -182 -55 N -ATOM 1603 CA THR A 250 22.789 22.362 1.694 1.00 7.64 C -ANISOU 1603 CA THR A 250 839 1072 991 85 -148 -86 C -ATOM 1604 C THR A 250 24.148 21.692 1.883 1.00 7.54 C -ANISOU 1604 C THR A 250 800 1013 1051 85 -114 -81 C -ATOM 1605 O THR A 250 25.204 22.225 1.534 1.00 7.53 O -ANISOU 1605 O THR A 250 842 1033 985 80 -125 -149 O -ATOM 1606 CB THR A 250 22.056 21.631 0.575 1.00 8.61 C -ANISOU 1606 CB THR A 250 928 1197 1144 56 -175 -92 C -ATOM 1607 OG1 THR A 250 22.873 21.700 -0.596 1.00 10.06 O -ANISOU 1607 OG1 THR A 250 1084 1560 1176 79 -216 -90 O -ATOM 1608 CG2 THR A 250 20.701 22.271 0.249 1.00 9.74 C -ANISOU 1608 CG2 THR A 250 1071 1507 1122 80 -162 -48 C -ATOM 1609 N LEU A 251 24.112 20.488 2.417 1.00 7.42 N -ANISOU 1609 N LEU A 251 852 954 1010 55 -52 -65 N -ATOM 1610 CA LEU A 251 25.330 19.708 2.550 1.00 7.45 C -ANISOU 1610 CA LEU A 251 875 971 981 58 -78 -87 C -ATOM 1611 C LEU A 251 26.045 19.600 1.197 1.00 7.52 C -ANISOU 1611 C LEU A 251 903 954 999 9 -114 -131 C -ATOM 1612 O LEU A 251 27.254 19.795 1.101 1.00 7.88 O -ANISOU 1612 O LEU A 251 891 1049 1054 53 -68 -100 O -ATOM 1613 CB LEU A 251 25.009 18.337 3.126 1.00 7.61 C -ANISOU 1613 CB LEU A 251 928 939 1021 60 -125 -107 C -ATOM 1614 CG LEU A 251 26.156 17.332 3.149 1.00 8.20 C -ANISOU 1614 CG LEU A 251 896 1067 1149 61 -15 -134 C -ATOM 1615 CD1 LEU A 251 27.254 17.823 4.081 1.00 9.40 C -ANISOU 1615 CD1 LEU A 251 1059 1254 1256 172 -194 -145 C -ATOM 1616 CD2 LEU A 251 25.619 15.984 3.574 1.00 10.52 C -ANISOU 1616 CD2 LEU A 251 1122 1318 1556 199 96 0 C -ATOM 1617 N ASP A 252 25.303 19.276 0.140 1.00 8.47 N -ANISOU 1617 N ASP A 252 970 1202 1044 -41 -84 -167 N -ATOM 1618 CA ASP A 252 25.914 19.128 -1.173 1.00 9.10 C -ANISOU 1618 CA ASP A 252 1111 1233 1110 12 -85 -146 C -ATOM 1619 C ASP A 252 26.521 20.425 -1.697 1.00 9.20 C -ANISOU 1619 C ASP A 252 1129 1330 1035 55 -37 -175 C -ATOM 1620 O ASP A 252 27.577 20.395 -2.307 1.00 9.74 O -ANISOU 1620 O ASP A 252 1146 1358 1197 -9 -3 -193 O -ATOM 1621 CB ASP A 252 24.906 18.548 -2.167 1.00 10.30 C -ANISOU 1621 CB ASP A 252 1241 1454 1218 -86 -82 -195 C -ATOM 1622 CG ASP A 252 24.785 17.048 -2.057 1.00 11.69 C -ANISOU 1622 CG ASP A 252 1270 1614 1554 -119 -258 -228 C -ATOM 1623 OD1 ASP A 252 25.827 16.360 -1.967 1.00 15.13 O -ANISOU 1623 OD1 ASP A 252 1863 1765 2119 -276 -291 -357 O -ATOM 1624 OD2 ASP A 252 23.678 16.478 -2.067 1.00 16.09 O -ANISOU 1624 OD2 ASP A 252 1735 2014 2363 -329 -178 -403 O -ATOM 1625 N GLU A 253 25.881 21.559 -1.434 1.00 8.69 N -ANISOU 1625 N GLU A 253 1082 1231 986 79 -71 -84 N -ATOM 1626 CA GLU A 253 26.433 22.836 -1.854 1.00 9.60 C -ANISOU 1626 CA GLU A 253 1207 1349 1090 92 -30 -25 C -ATOM 1627 C GLU A 253 27.767 23.097 -1.147 1.00 8.93 C -ANISOU 1627 C GLU A 253 1173 1206 1014 40 -21 -37 C -ATOM 1628 O GLU A 253 28.715 23.593 -1.758 1.00 10.39 O -ANISOU 1628 O GLU A 253 1284 1537 1127 -5 -11 39 O -ATOM 1629 CB GLU A 253 25.425 23.960 -1.627 1.00 9.69 C -ANISOU 1629 CB GLU A 253 1304 1295 1083 118 -75 65 C -ATOM 1630 CG GLU A 253 24.331 23.948 -2.685 1.00 11.84 C -ANISOU 1630 CG GLU A 253 1438 1721 1338 256 -191 48 C -ATOM 1631 CD GLU A 253 23.134 24.814 -2.371 1.00 13.84 C -ANISOU 1631 CD GLU A 253 1830 2115 1313 440 -342 140 C -ATOM 1632 OE1 GLU A 253 22.884 25.175 -1.210 1.00 13.34 O -ANISOU 1632 OE1 GLU A 253 1783 2052 1234 607 -423 -29 O -ATOM 1633 OE2 GLU A 253 22.407 25.124 -3.328 1.00 19.92 O -ANISOU 1633 OE2 GLU A 253 2554 3162 1852 733 -597 100 O -ATOM 1634 N CYS A 254 27.852 22.762 0.136 1.00 7.64 N -ANISOU 1634 N CYS A 254 1012 984 905 79 1 -65 N -ATOM 1635 CA CYS A 254 29.111 22.939 0.864 1.00 7.21 C -ANISOU 1635 CA CYS A 254 909 859 971 37 -10 -91 C -ATOM 1636 C CYS A 254 30.188 21.962 0.385 1.00 7.28 C -ANISOU 1636 C CYS A 254 933 833 1000 47 -8 -179 C -ATOM 1637 O CYS A 254 31.354 22.322 0.265 1.00 7.83 O -ANISOU 1637 O CYS A 254 901 986 1088 -11 0 -243 O -ATOM 1638 CB CYS A 254 28.871 22.790 2.351 1.00 7.70 C -ANISOU 1638 CB CYS A 254 834 982 1110 22 -17 -93 C -ATOM 1639 SG CYS A 254 27.923 24.157 3.070 1.00 7.64 S -ANISOU 1639 SG CYS A 254 996 929 978 35 31 -160 S -ATOM 1640 N LEU A 255 29.793 20.722 0.112 1.00 7.92 N -ANISOU 1640 N LEU A 255 919 879 1211 79 23 -234 N -ATOM 1641 CA LEU A 255 30.706 19.693 -0.386 1.00 8.45 C -ANISOU 1641 CA LEU A 255 997 999 1214 53 26 -231 C -ATOM 1642 C LEU A 255 31.281 20.029 -1.745 1.00 9.28 C -ANISOU 1642 C LEU A 255 1111 1095 1319 38 61 -252 C -ATOM 1643 O LEU A 255 32.314 19.480 -2.101 1.00 11.10 O -ANISOU 1643 O LEU A 255 1134 1461 1619 75 197 -312 O -ATOM 1644 CB LEU A 255 30.007 18.335 -0.438 1.00 8.64 C -ANISOU 1644 CB LEU A 255 1037 943 1302 63 28 -285 C -ATOM 1645 CG LEU A 255 29.841 17.656 0.910 1.00 9.49 C -ANISOU 1645 CG LEU A 255 1165 940 1498 78 29 -242 C -ATOM 1646 CD1 LEU A 255 28.872 16.499 0.750 1.00 10.27 C -ANISOU 1646 CD1 LEU A 255 1119 1110 1672 151 131 -232 C -ATOM 1647 CD2 LEU A 255 31.168 17.175 1.465 1.00 11.05 C -ANISOU 1647 CD2 LEU A 255 1315 1062 1820 -31 -152 -65 C -ATOM 1648 N ALA A 256 30.640 20.922 -2.490 1.00 9.20 N -ANISOU 1648 N ALA A 256 1123 1256 1114 19 89 -258 N -ATOM 1649 CA ALA A 256 31.129 21.362 -3.791 1.00 10.32 C -ANISOU 1649 CA ALA A 256 1265 1444 1210 -50 33 -182 C -ATOM 1650 C ALA A 256 32.193 22.439 -3.700 1.00 10.63 C -ANISOU 1650 C ALA A 256 1286 1567 1185 -94 21 -169 C -ATOM 1651 O ALA A 256 32.742 22.840 -4.719 1.00 12.02 O -ANISOU 1651 O ALA A 256 1438 1939 1191 -245 83 -281 O -ATOM 1652 CB ALA A 256 29.980 21.859 -4.637 1.00 11.40 C -ANISOU 1652 CB ALA A 256 1451 1589 1291 -34 32 -172 C -ATOM 1653 N PHE A 257 32.524 22.896 -2.499 1.00 10.37 N -ANISOU 1653 N PHE A 257 1252 1490 1198 -144 0 -176 N -ATOM 1654 CA PHE A 257 33.544 23.909 -2.344 1.00 10.14 C -ANISOU 1654 CA PHE A 257 1268 1383 1202 -98 1 -156 C -ATOM 1655 C PHE A 257 34.861 23.436 -2.951 1.00 10.83 C -ANISOU 1655 C PHE A 257 1376 1458 1280 -137 -15 -162 C -ATOM 1656 O PHE A 257 35.276 22.305 -2.742 1.00 12.45 O -ANISOU 1656 O PHE A 257 1594 1558 1575 -181 125 -254 O -ATOM 1657 CB PHE A 257 33.740 24.227 -0.868 1.00 10.13 C -ANISOU 1657 CB PHE A 257 1280 1413 1155 -34 -31 -175 C -ATOM 1658 CG PHE A 257 34.707 25.338 -0.625 1.00 9.98 C -ANISOU 1658 CG PHE A 257 1358 1395 1036 -174 39 -160 C -ATOM 1659 CD1 PHE A 257 34.322 26.652 -0.808 1.00 12.51 C -ANISOU 1659 CD1 PHE A 257 1625 1598 1527 -153 59 -147 C -ATOM 1660 CD2 PHE A 257 36.007 25.075 -0.245 1.00 10.29 C -ANISOU 1660 CD2 PHE A 257 1430 1546 932 -129 9 63 C -ATOM 1661 CE1 PHE A 257 35.213 27.684 -0.604 1.00 12.81 C -ANISOU 1661 CE1 PHE A 257 1834 1550 1480 -252 89 -207 C -ATOM 1662 CE2 PHE A 257 36.908 26.105 -0.047 1.00 11.11 C -ANISOU 1662 CE2 PHE A 257 1541 1860 820 -185 72 -136 C -ATOM 1663 CZ PHE A 257 36.514 27.402 -0.225 1.00 11.91 C -ANISOU 1663 CZ PHE A 257 1665 1655 1204 -356 94 -273 C -ATOM 1664 N ASP A 258 35.528 24.336 -3.658 1.00 11.44 N -ANISOU 1664 N ASP A 258 1443 1633 1268 -173 69 -155 N -ATOM 1665 CA ASP A 258 36.758 24.032 -4.383 1.00 12.78 C -ANISOU 1665 CA ASP A 258 1607 1829 1421 -120 72 -70 C -ATOM 1666 C ASP A 258 37.981 24.047 -3.453 1.00 12.12 C -ANISOU 1666 C ASP A 258 1539 1748 1317 -175 52 -115 C -ATOM 1667 O ASP A 258 38.750 25.011 -3.450 1.00 12.95 O -ANISOU 1667 O ASP A 258 1629 1777 1513 -305 -107 80 O -ATOM 1668 CB ASP A 258 36.924 25.048 -5.532 1.00 13.85 C -ANISOU 1668 CB ASP A 258 1696 2126 1440 -85 97 -45 C -ATOM 1669 CG ASP A 258 38.161 24.804 -6.379 1.00 17.35 C -ANISOU 1669 CG ASP A 258 2103 2631 1855 -18 316 103 C -ATOM 1670 OD1 ASP A 258 38.827 23.768 -6.182 1.00 20.95 O -ANISOU 1670 OD1 ASP A 258 2382 3389 2190 390 871 -143 O -ATOM 1671 OD2 ASP A 258 38.524 25.603 -7.274 1.00 22.02 O -ANISOU 1671 OD2 ASP A 258 2564 3638 2162 32 500 247 O -ATOM 1672 N VAL A 259 38.204 22.962 -2.717 1.00 11.97 N -ANISOU 1672 N VAL A 259 1645 1579 1323 -173 130 -199 N -ATOM 1673 CA VAL A 259 39.350 22.899 -1.796 1.00 12.53 C -ANISOU 1673 CA VAL A 259 1838 1551 1370 -74 67 -154 C -ATOM 1674 C VAL A 259 40.679 22.812 -2.502 1.00 11.56 C -ANISOU 1674 C VAL A 259 1758 1505 1128 -86 -7 -256 C -ATOM 1675 O VAL A 259 41.689 23.263 -1.967 1.00 12.04 O -ANISOU 1675 O VAL A 259 1896 1637 1042 -123 -88 -324 O -ATOM 1676 CB VAL A 259 39.329 21.707 -0.794 1.00 13.90 C -ANISOU 1676 CB VAL A 259 2122 1569 1588 -45 180 -182 C -ATOM 1677 CG1 VAL A 259 38.391 21.969 0.354 1.00 15.60 C -ANISOU 1677 CG1 VAL A 259 2280 1861 1783 -87 118 -91 C -ATOM 1678 CG2 VAL A 259 39.043 20.365 -1.501 1.00 13.99 C -ANISOU 1678 CG2 VAL A 259 2242 1436 1636 -25 211 -140 C -ATOM 1679 N GLU A 260 40.696 22.234 -3.701 1.00 11.67 N -ANISOU 1679 N GLU A 260 1721 1561 1151 -126 -55 -297 N -ATOM 1680 CA GLU A 260 41.948 22.057 -4.407 1.00 12.24 C -ANISOU 1680 CA GLU A 260 1701 1660 1289 -42 -13 -309 C -ATOM 1681 C GLU A 260 42.641 23.359 -4.725 1.00 12.16 C -ANISOU 1681 C GLU A 260 1659 1744 1214 -111 -3 -369 C -ATOM 1682 O GLU A 260 43.868 23.377 -4.798 1.00 14.65 O -ANISOU 1682 O GLU A 260 1819 2098 1647 -99 32 -524 O -ATOM 1683 CB GLU A 260 41.725 21.268 -5.692 1.00 12.78 C -ANISOU 1683 CB GLU A 260 1743 1778 1334 -73 -4 -327 C -ATOM 1684 CG GLU A 260 41.405 19.815 -5.443 1.00 14.52 C -ANISOU 1684 CG GLU A 260 2004 2016 1495 73 -26 -420 C -ATOM 1685 CD GLU A 260 42.546 19.114 -4.750 1.00 18.53 C -ANISOU 1685 CD GLU A 260 2630 2213 2195 318 203 -385 C -ATOM 1686 OE1 GLU A 260 43.674 19.108 -5.296 1.00 21.82 O -ANISOU 1686 OE1 GLU A 260 2769 3051 2472 364 109 -214 O -ATOM 1687 OE2 GLU A 260 42.319 18.578 -3.667 1.00 20.59 O -ANISOU 1687 OE2 GLU A 260 3161 2545 2116 628 47 -683 O -ATOM 1688 N ASN A 261 41.874 24.429 -4.914 1.00 11.57 N -ANISOU 1688 N ASN A 261 1674 1723 997 -129 23 -291 N -ATOM 1689 CA ASN A 261 42.413 25.739 -5.259 1.00 12.22 C -ANISOU 1689 CA ASN A 261 1820 1753 1070 -136 49 -160 C -ATOM 1690 C ASN A 261 42.213 26.799 -4.187 1.00 11.42 C -ANISOU 1690 C ASN A 261 1768 1647 922 -176 40 -129 C -ATOM 1691 O ASN A 261 42.382 27.980 -4.433 1.00 13.10 O -ANISOU 1691 O ASN A 261 2321 1814 840 -244 133 6 O -ATOM 1692 CB ASN A 261 41.770 26.235 -6.547 1.00 12.89 C -ANISOU 1692 CB ASN A 261 1898 1914 1085 -131 84 -148 C -ATOM 1693 CG ASN A 261 42.117 25.381 -7.712 1.00 15.89 C -ANISOU 1693 CG ASN A 261 2156 2491 1389 -263 237 -418 C -ATOM 1694 OD1 ASN A 261 43.287 25.262 -8.065 1.00 17.97 O -ANISOU 1694 OD1 ASN A 261 2192 3411 1224 -420 198 -697 O -ATOM 1695 ND2 ASN A 261 41.118 24.742 -8.291 1.00 18.57 N -ANISOU 1695 ND2 ASN A 261 2494 3158 1402 -390 365 -844 N -ATOM 1696 N PHE A 262 41.856 26.378 -2.986 1.00 9.73 N -ANISOU 1696 N PHE A 262 1477 1410 808 -193 39 14 N -ATOM 1697 CA PHE A 262 41.526 27.295 -1.909 1.00 8.47 C -ANISOU 1697 CA PHE A 262 1249 1206 761 -92 -8 17 C -ATOM 1698 C PHE A 262 42.820 27.756 -1.244 1.00 8.66 C -ANISOU 1698 C PHE A 262 1251 1194 844 -107 0 62 C -ATOM 1699 O PHE A 262 43.475 27.009 -0.504 1.00 9.02 O -ANISOU 1699 O PHE A 262 1296 1297 832 -140 -38 72 O -ATOM 1700 CB PHE A 262 40.623 26.577 -0.912 1.00 8.66 C -ANISOU 1700 CB PHE A 262 1248 1160 879 -181 3 100 C -ATOM 1701 CG PHE A 262 40.302 27.344 0.350 1.00 7.88 C -ANISOU 1701 CG PHE A 262 1102 1028 864 -144 -7 34 C -ATOM 1702 CD1 PHE A 262 40.049 28.702 0.346 1.00 8.72 C -ANISOU 1702 CD1 PHE A 262 1250 1171 891 -173 -147 76 C -ATOM 1703 CD2 PHE A 262 40.215 26.663 1.545 1.00 7.66 C -ANISOU 1703 CD2 PHE A 262 936 1163 811 -179 -54 -15 C -ATOM 1704 CE1 PHE A 262 39.750 29.365 1.521 1.00 8.47 C -ANISOU 1704 CE1 PHE A 262 1027 1049 1139 -75 -29 -13 C -ATOM 1705 CE2 PHE A 262 39.907 27.317 2.718 1.00 8.62 C -ANISOU 1705 CE2 PHE A 262 987 1398 887 -126 20 -33 C -ATOM 1706 CZ PHE A 262 39.678 28.680 2.701 1.00 8.68 C -ANISOU 1706 CZ PHE A 262 959 1373 964 -156 78 -101 C -HETATM 1707 N MSE A 263 43.203 28.997 -1.535 1.00 8.52 N -ANISOU 1707 N MSE A 263 1279 1164 794 -104 -23 73 N -HETATM 1708 CA MSE A 263 44.358 29.641 -0.914 1.00 8.76 C -ANISOU 1708 CA MSE A 263 1223 1158 946 -112 29 43 C -HETATM 1709 C MSE A 263 43.950 30.157 0.452 1.00 8.16 C -ANISOU 1709 C MSE A 263 1170 1053 876 -103 10 44 C -HETATM 1710 O MSE A 263 42.915 30.779 0.575 1.00 9.70 O -ANISOU 1710 O MSE A 263 1259 1425 1000 1 -117 31 O -HETATM 1711 CB MSE A 263 44.829 30.801 -1.787 1.00 9.69 C -ANISOU 1711 CB MSE A 263 1313 1313 1054 -177 47 87 C -HETATM 1712 CG MSE A 263 45.232 30.387 -3.190 1.00 12.20 C -ANISOU 1712 CG MSE A 263 1691 1618 1324 -86 113 87 C -HETATM 1713 SE MSE A 263 46.854 29.332 -3.232 1.00 21.92 SE -ANISOU 1713 SE MSE A 263 3432 2715 2180 -234 613 63 SE -HETATM 1714 CE MSE A 263 48.106 30.765 -2.917 1.00 17.85 C -ANISOU 1714 CE MSE A 263 2469 2182 2130 -116 90 -14 C -ATOM 1715 N THR A 264 44.754 29.951 1.483 1.00 7.18 N -ANISOU 1715 N THR A 264 1007 909 808 -143 -21 48 N -ATOM 1716 CA THR A 264 44.310 30.426 2.790 1.00 6.91 C -ANISOU 1716 CA THR A 264 949 825 848 -132 27 24 C -ATOM 1717 C THR A 264 44.162 31.945 2.755 1.00 6.96 C -ANISOU 1717 C THR A 264 948 847 849 -116 -23 73 C -ATOM 1718 O THR A 264 45.069 32.661 2.305 1.00 6.77 O -ANISOU 1718 O THR A 264 920 769 881 -89 59 124 O -ATOM 1719 CB THR A 264 45.199 30.004 3.962 1.00 6.73 C -ANISOU 1719 CB THR A 264 992 752 813 -110 51 39 C -ATOM 1720 OG1 THR A 264 44.766 30.725 5.125 1.00 6.50 O -ANISOU 1720 OG1 THR A 264 953 872 644 -137 99 79 O -ATOM 1721 CG2 THR A 264 46.672 30.316 3.748 1.00 7.14 C -ANISOU 1721 CG2 THR A 264 1165 726 822 25 1 86 C -ATOM 1722 N PRO A 265 43.010 32.460 3.210 1.00 7.37 N -ANISOU 1722 N PRO A 265 917 929 953 -85 60 104 N -ATOM 1723 CA PRO A 265 42.792 33.905 3.288 1.00 7.59 C -ANISOU 1723 CA PRO A 265 927 987 967 -9 -11 86 C -ATOM 1724 C PRO A 265 43.399 34.540 4.522 1.00 6.57 C -ANISOU 1724 C PRO A 265 784 807 902 -2 48 167 C -ATOM 1725 O PRO A 265 43.348 35.776 4.644 1.00 7.40 O -ANISOU 1725 O PRO A 265 1021 787 1002 41 -17 157 O -ATOM 1726 CB PRO A 265 41.271 34.014 3.362 1.00 8.08 C -ANISOU 1726 CB PRO A 265 946 1083 1038 -19 -56 45 C -ATOM 1727 CG PRO A 265 40.877 32.807 4.102 1.00 9.35 C -ANISOU 1727 CG PRO A 265 930 1300 1321 -92 54 126 C -ATOM 1728 CD PRO A 265 41.797 31.718 3.608 1.00 7.90 C -ANISOU 1728 CD PRO A 265 1001 968 1029 -133 60 144 C -ATOM 1729 N LEU A 266 43.947 33.752 5.439 1.00 5.91 N -ANISOU 1729 N LEU A 266 806 670 769 -23 103 151 N -ATOM 1730 CA LEU A 266 44.418 34.304 6.694 1.00 5.83 C -ANISOU 1730 CA LEU A 266 774 653 786 18 97 115 C -ATOM 1731 C LEU A 266 45.612 35.245 6.553 1.00 5.87 C -ANISOU 1731 C LEU A 266 787 633 808 34 106 120 C -ATOM 1732 O LEU A 266 45.612 36.270 7.213 1.00 6.39 O -ANISOU 1732 O LEU A 266 945 664 818 40 101 27 O -ATOM 1733 CB LEU A 266 44.657 33.201 7.723 1.00 6.28 C -ANISOU 1733 CB LEU A 266 828 674 881 -103 106 189 C -ATOM 1734 CG LEU A 266 43.361 32.643 8.324 1.00 7.17 C -ANISOU 1734 CG LEU A 266 966 807 948 18 156 138 C -ATOM 1735 CD1 LEU A 266 43.595 31.367 9.083 1.00 8.53 C -ANISOU 1735 CD1 LEU A 266 1123 961 1156 -95 246 200 C -ATOM 1736 CD2 LEU A 266 42.802 33.658 9.297 1.00 10.46 C -ANISOU 1736 CD2 LEU A 266 1483 1143 1347 60 534 171 C -ATOM 1737 N PRO A 267 46.626 34.954 5.736 1.00 5.91 N -ANISOU 1737 N PRO A 267 776 651 818 4 122 111 N -ATOM 1738 CA PRO A 267 47.726 35.925 5.597 1.00 5.93 C -ANISOU 1738 CA PRO A 267 759 622 872 28 82 103 C -ATOM 1739 C PRO A 267 47.230 37.330 5.280 1.00 6.09 C -ANISOU 1739 C PRO A 267 759 647 908 -2 165 94 C -ATOM 1740 O PRO A 267 47.655 38.291 5.911 1.00 6.71 O -ANISOU 1740 O PRO A 267 795 736 1017 -9 161 59 O -ATOM 1741 CB PRO A 267 48.579 35.342 4.465 1.00 6.05 C -ANISOU 1741 CB PRO A 267 738 661 898 23 74 137 C -ATOM 1742 CG PRO A 267 48.381 33.868 4.607 1.00 5.95 C -ANISOU 1742 CG PRO A 267 850 671 738 63 169 93 C -ATOM 1743 CD PRO A 267 46.923 33.707 5.008 1.00 6.39 C -ANISOU 1743 CD PRO A 267 864 790 772 -12 68 140 C -ATOM 1744 N ALA A 268 46.313 37.467 4.336 1.00 6.50 N -ANISOU 1744 N ALA A 268 801 653 1014 -4 73 164 N -ATOM 1745 CA ALA A 268 45.830 38.794 3.975 1.00 7.31 C -ANISOU 1745 CA ALA A 268 998 754 1023 27 75 171 C -ATOM 1746 C ALA A 268 45.059 39.426 5.135 1.00 7.77 C -ANISOU 1746 C ALA A 268 992 773 1183 66 120 202 C -ATOM 1747 O ALA A 268 45.175 40.622 5.400 1.00 9.40 O -ANISOU 1747 O ALA A 268 1354 780 1438 95 332 143 O -ATOM 1748 CB ALA A 268 44.990 38.739 2.733 1.00 8.84 C -ANISOU 1748 CB ALA A 268 1176 989 1191 38 59 208 C -ATOM 1749 N LEU A 269 44.290 38.632 5.858 1.00 7.70 N -ANISOU 1749 N LEU A 269 970 800 1156 120 195 131 N -ATOM 1750 CA LEU A 269 43.571 39.131 7.021 1.00 8.78 C -ANISOU 1750 CA LEU A 269 1078 959 1299 152 181 68 C -ATOM 1751 C LEU A 269 44.513 39.592 8.129 1.00 8.67 C -ANISOU 1751 C LEU A 269 1061 951 1280 99 223 17 C -ATOM 1752 O LEU A 269 44.162 40.465 8.927 1.00 11.70 O -ANISOU 1752 O LEU A 269 1371 1347 1726 327 232 -242 O -ATOM 1753 CB LEU A 269 42.623 38.051 7.538 1.00 9.17 C -ANISOU 1753 CB LEU A 269 1121 1124 1237 93 282 69 C -ATOM 1754 CG LEU A 269 41.425 37.770 6.620 1.00 14.21 C -ANISOU 1754 CG LEU A 269 1698 1784 1915 62 154 80 C -ATOM 1755 CD1 LEU A 269 40.796 36.430 6.947 1.00 17.01 C -ANISOU 1755 CD1 LEU A 269 1991 2239 2232 -35 98 17 C -ATOM 1756 CD2 LEU A 269 40.384 38.891 6.696 1.00 16.85 C -ANISOU 1756 CD2 LEU A 269 1920 2137 2342 118 56 70 C -ATOM 1757 N LEU A 270 45.702 39.009 8.182 1.00 8.04 N -ANISOU 1757 N LEU A 270 1111 912 1033 147 163 60 N -ATOM 1758 CA LEU A 270 46.694 39.279 9.211 1.00 8.18 C -ANISOU 1758 CA LEU A 270 1119 906 1082 15 115 72 C -ATOM 1759 C LEU A 270 47.805 40.198 8.699 1.00 7.68 C -ANISOU 1759 C LEU A 270 1080 831 1006 86 86 80 C -ATOM 1760 O LEU A 270 48.890 40.216 9.257 1.00 9.64 O -ANISOU 1760 O LEU A 270 1347 998 1315 -116 -43 151 O -ATOM 1761 CB LEU A 270 47.243 37.949 9.719 1.00 7.97 C -ANISOU 1761 CB LEU A 270 1086 936 1005 7 80 75 C -ATOM 1762 CG LEU A 270 46.165 37.027 10.311 1.00 8.11 C -ANISOU 1762 CG LEU A 270 1061 1051 969 -14 114 211 C -ATOM 1763 CD1 LEU A 270 46.769 35.669 10.658 1.00 8.46 C -ANISOU 1763 CD1 LEU A 270 1058 1120 1037 -174 -133 236 C -ATOM 1764 CD2 LEU A 270 45.498 37.651 11.532 1.00 10.32 C -ANISOU 1764 CD2 LEU A 270 1363 1439 1119 2 244 78 C -ATOM 1765 N GLY A 271 47.510 40.991 7.669 1.00 8.18 N -ANISOU 1765 N GLY A 271 1183 904 1021 88 84 76 N -ATOM 1766 CA GLY A 271 48.389 42.078 7.271 1.00 8.56 C -ANISOU 1766 CA GLY A 271 1258 856 1136 -26 93 81 C -ATOM 1767 C GLY A 271 49.392 41.770 6.183 1.00 7.69 C -ANISOU 1767 C GLY A 271 1165 723 1031 -73 82 144 C -ATOM 1768 O GLY A 271 50.221 42.624 5.871 1.00 9.09 O -ANISOU 1768 O GLY A 271 1454 771 1225 -268 201 109 O -ATOM 1769 N LEU A 272 49.310 40.586 5.585 1.00 6.80 N -ANISOU 1769 N LEU A 272 999 714 870 -50 63 154 N -ATOM 1770 CA LEU A 272 50.345 40.113 4.687 1.00 6.41 C -ANISOU 1770 CA LEU A 272 876 673 886 -53 92 155 C -ATOM 1771 C LEU A 272 49.899 40.009 3.248 1.00 6.37 C -ANISOU 1771 C LEU A 272 852 696 871 -55 108 229 C -ATOM 1772 O LEU A 272 50.517 39.307 2.463 1.00 6.70 O -ANISOU 1772 O LEU A 272 1082 658 806 -37 151 298 O -ATOM 1773 CB LEU A 272 50.892 38.781 5.181 1.00 6.24 C -ANISOU 1773 CB LEU A 272 797 668 904 -27 61 214 C -ATOM 1774 CG LEU A 272 51.331 38.756 6.636 1.00 6.83 C -ANISOU 1774 CG LEU A 272 965 794 836 54 27 264 C -ATOM 1775 CD1 LEU A 272 51.709 37.345 7.022 1.00 8.25 C -ANISOU 1775 CD1 LEU A 272 1128 1050 953 78 -103 221 C -ATOM 1776 CD2 LEU A 272 52.459 39.716 6.927 1.00 8.47 C -ANISOU 1776 CD2 LEU A 272 1120 1049 1050 -14 -57 173 C -ATOM 1777 N GLY A 273 48.874 40.756 2.872 1.00 7.25 N -ANISOU 1777 N GLY A 273 960 876 917 -19 75 253 N -ATOM 1778 CA GLY A 273 48.369 40.714 1.508 1.00 8.03 C -ANISOU 1778 CA GLY A 273 955 1100 996 -71 112 187 C -ATOM 1779 C GLY A 273 49.389 41.082 0.439 1.00 7.52 C -ANISOU 1779 C GLY A 273 880 1030 944 -71 62 247 C -ATOM 1780 O GLY A 273 49.311 40.593 -0.678 1.00 8.90 O -ANISOU 1780 O GLY A 273 1077 1319 983 -304 -42 280 O -ATOM 1781 N ASN A 274 50.370 41.913 0.763 1.00 6.68 N -ANISOU 1781 N ASN A 274 871 807 858 -25 60 330 N -ATOM 1782 CA ASN A 274 51.383 42.282 -0.214 1.00 6.38 C -ANISOU 1782 CA ASN A 274 882 715 826 -13 69 291 C -ATOM 1783 C ASN A 274 52.530 41.290 -0.329 1.00 6.49 C -ANISOU 1783 C ASN A 274 903 770 790 -34 51 334 C -ATOM 1784 O ASN A 274 53.406 41.491 -1.159 1.00 7.21 O -ANISOU 1784 O ASN A 274 959 790 989 70 199 484 O -ATOM 1785 CB ASN A 274 51.951 43.678 0.087 1.00 7.01 C -ANISOU 1785 CB ASN A 274 920 817 926 4 20 321 C -ATOM 1786 CG ASN A 274 51.003 44.792 -0.247 1.00 7.28 C -ANISOU 1786 CG ASN A 274 1064 720 980 136 231 257 C -ATOM 1787 OD1 ASN A 274 50.859 45.761 0.518 1.00 10.65 O -ANISOU 1787 OD1 ASN A 274 1612 1077 1359 172 241 277 O -ATOM 1788 ND2 ASN A 274 50.366 44.679 -1.370 1.00 6.71 N -ANISOU 1788 ND2 ASN A 274 1030 732 784 323 151 454 N -ATOM 1789 N TYR A 275 52.517 40.230 0.484 1.00 6.57 N -ANISOU 1789 N TYR A 275 873 763 858 6 99 314 N -ATOM 1790 CA TYR A 275 53.658 39.312 0.603 1.00 6.85 C -ANISOU 1790 CA TYR A 275 876 810 915 -10 59 235 C -ATOM 1791 C TYR A 275 53.219 37.871 0.374 1.00 7.10 C -ANISOU 1791 C TYR A 275 962 809 925 6 19 286 C -ATOM 1792 O TYR A 275 53.327 37.019 1.241 1.00 7.10 O -ANISOU 1792 O TYR A 275 911 759 1026 -27 103 498 O -ATOM 1793 CB TYR A 275 54.326 39.476 1.969 1.00 7.13 C -ANISOU 1793 CB TYR A 275 867 821 1020 57 -29 283 C -ATOM 1794 CG TYR A 275 54.532 40.920 2.333 1.00 6.92 C -ANISOU 1794 CG TYR A 275 854 877 898 40 33 253 C -ATOM 1795 CD1 TYR A 275 55.316 41.748 1.547 1.00 7.46 C -ANISOU 1795 CD1 TYR A 275 908 934 990 0 145 160 C -ATOM 1796 CD2 TYR A 275 53.901 41.481 3.431 1.00 8.72 C -ANISOU 1796 CD2 TYR A 275 1039 1011 1260 -31 237 191 C -ATOM 1797 CE1 TYR A 275 55.484 43.092 1.850 1.00 8.44 C -ANISOU 1797 CE1 TYR A 275 994 998 1213 -58 137 198 C -ATOM 1798 CE2 TYR A 275 54.064 42.814 3.748 1.00 9.37 C -ANISOU 1798 CE2 TYR A 275 1229 1078 1252 -33 223 80 C -ATOM 1799 CZ TYR A 275 54.847 43.629 2.946 1.00 8.80 C -ANISOU 1799 CZ TYR A 275 983 930 1430 -13 116 133 C -ATOM 1800 OH TYR A 275 54.991 44.950 3.266 1.00 10.72 O -ANISOU 1800 OH TYR A 275 1292 1126 1653 -119 188 -21 O -ATOM 1801 N PRO A 276 52.701 37.587 -0.810 1.00 8.66 N -ANISOU 1801 N PRO A 276 1367 845 1076 -37 -106 266 N -ATOM 1802 CA PRO A 276 52.164 36.251 -1.076 1.00 9.32 C -ANISOU 1802 CA PRO A 276 1360 994 1187 -47 -50 132 C -ATOM 1803 C PRO A 276 53.257 35.193 -1.120 1.00 9.09 C -ANISOU 1803 C PRO A 276 1271 944 1236 -111 96 244 C -ATOM 1804 O PRO A 276 54.396 35.470 -1.514 1.00 10.10 O -ANISOU 1804 O PRO A 276 1508 961 1369 -188 273 251 O -ATOM 1805 CB PRO A 276 51.504 36.421 -2.443 1.00 10.84 C -ANISOU 1805 CB PRO A 276 1614 1152 1352 -82 -186 140 C -ATOM 1806 CG PRO A 276 52.224 37.542 -3.065 1.00 11.09 C -ANISOU 1806 CG PRO A 276 1828 1148 1238 51 -132 240 C -ATOM 1807 CD PRO A 276 52.552 38.479 -1.975 1.00 9.53 C -ANISOU 1807 CD PRO A 276 1623 930 1068 23 -169 289 C -ATOM 1808 N LEU A 277 52.884 33.977 -0.732 1.00 8.45 N -ANISOU 1808 N LEU A 277 1198 821 1189 -52 118 231 N -ATOM 1809 CA LEU A 277 53.727 32.800 -0.875 1.00 8.89 C -ANISOU 1809 CA LEU A 277 1155 987 1235 -29 155 126 C -ATOM 1810 C LEU A 277 53.105 31.902 -1.932 1.00 9.49 C -ANISOU 1810 C LEU A 277 1334 1094 1177 -68 312 94 C -ATOM 1811 O LEU A 277 51.918 31.569 -1.880 1.00 9.55 O -ANISOU 1811 O LEU A 277 1419 1206 1003 -134 169 -73 O -ATOM 1812 CB LEU A 277 53.835 32.055 0.448 1.00 8.57 C -ANISOU 1812 CB LEU A 277 1119 846 1290 -23 65 135 C -ATOM 1813 CG LEU A 277 54.541 32.810 1.576 1.00 10.34 C -ANISOU 1813 CG LEU A 277 1351 972 1603 30 -32 67 C -ATOM 1814 CD1 LEU A 277 54.434 32.070 2.892 1.00 11.22 C -ANISOU 1814 CD1 LEU A 277 1531 1200 1532 246 -261 125 C -ATOM 1815 CD2 LEU A 277 55.994 33.045 1.225 1.00 13.04 C -ANISOU 1815 CD2 LEU A 277 1588 1441 1922 5 -32 122 C -ATOM 1816 N GLU A 278 53.900 31.515 -2.919 1.00 11.82 N -ANISOU 1816 N GLU A 278 1593 1455 1442 -194 396 -12 N -ATOM 1817 CA GLU A 278 53.408 30.657 -3.991 1.00 13.14 C -ANISOU 1817 CA GLU A 278 1798 1636 1559 -141 323 -31 C -ATOM 1818 C GLU A 278 52.920 29.330 -3.423 1.00 12.74 C -ANISOU 1818 C GLU A 278 1734 1631 1474 -127 401 -93 C -ATOM 1819 O GLU A 278 53.570 28.743 -2.584 1.00 13.72 O -ANISOU 1819 O GLU A 278 1802 1518 1892 -63 433 -301 O -ATOM 1820 CB GLU A 278 54.493 30.364 -5.029 1.00 15.03 C -ANISOU 1820 CB GLU A 278 2023 1914 1773 -125 290 -53 C -ATOM 1821 CG GLU A 278 54.884 31.546 -5.895 1.00 19.81 C -ANISOU 1821 CG GLU A 278 2597 2473 2456 -142 170 -20 C -ATOM 1822 CD GLU A 278 56.106 32.291 -5.398 0.00 25.21 C -ANISOU 1822 CD GLU A 278 3296 3137 3144 -184 -40 88 C -ATOM 1823 OE1 GLU A 278 56.755 31.833 -4.429 0.00 30.12 O -ANISOU 1823 OE1 GLU A 278 3857 3678 3907 -226 -135 76 O -ATOM 1824 OE2 GLU A 278 56.425 33.341 -5.991 0.00 28.28 O -ANISOU 1824 OE2 GLU A 278 3638 3349 3755 -449 42 153 O -ATOM 1825 N GLY A 279 51.776 28.881 -3.905 1.00 12.54 N -ANISOU 1825 N GLY A 279 1746 1653 1366 -79 327 -127 N -ATOM 1826 CA GLY A 279 51.238 27.597 -3.527 1.00 11.69 C -ANISOU 1826 CA GLY A 279 1632 1468 1340 -95 282 -126 C -ATOM 1827 C GLY A 279 50.755 27.516 -2.090 1.00 9.81 C -ANISOU 1827 C GLY A 279 1374 1235 1117 -85 299 -122 C -ATOM 1828 O GLY A 279 50.645 26.419 -1.557 1.00 10.54 O -ANISOU 1828 O GLY A 279 1528 1166 1310 -89 463 -164 O -ATOM 1829 N ASN A 280 50.441 28.653 -1.468 1.00 8.20 N -ANISOU 1829 N ASN A 280 1244 997 872 -113 323 -50 N -ATOM 1830 CA ASN A 280 50.025 28.690 -0.077 1.00 7.34 C -ANISOU 1830 CA ASN A 280 1063 960 764 -108 179 -2 C -ATOM 1831 C ASN A 280 48.545 28.329 0.098 1.00 6.50 C -ANISOU 1831 C ASN A 280 1005 792 670 -123 166 -41 C -ATOM 1832 O ASN A 280 47.701 29.134 0.514 1.00 7.06 O -ANISOU 1832 O ASN A 280 1085 822 773 -106 158 -48 O -ATOM 1833 CB ASN A 280 50.338 30.049 0.517 1.00 6.94 C -ANISOU 1833 CB ASN A 280 968 824 844 -191 215 96 C -ATOM 1834 CG ASN A 280 50.291 30.041 2.034 1.00 6.68 C -ANISOU 1834 CG ASN A 280 965 841 730 -113 192 171 C -ATOM 1835 OD1 ASN A 280 50.340 28.986 2.656 1.00 7.71 O -ANISOU 1835 OD1 ASN A 280 1374 782 774 -110 200 80 O -ATOM 1836 ND2 ASN A 280 50.208 31.212 2.632 1.00 6.70 N -ANISOU 1836 ND2 ASN A 280 935 686 925 -29 210 22 N -ATOM 1837 N LEU A 281 48.253 27.077 -0.217 1.00 7.21 N -ANISOU 1837 N LEU A 281 1115 858 766 -140 163 -38 N -ATOM 1838 CA LEU A 281 46.922 26.508 -0.091 1.00 7.12 C -ANISOU 1838 CA LEU A 281 1040 897 766 -189 88 -3 C -ATOM 1839 C LEU A 281 46.557 26.279 1.364 1.00 6.89 C -ANISOU 1839 C LEU A 281 925 926 765 -188 88 12 C -ATOM 1840 O LEU A 281 47.396 25.904 2.183 1.00 7.27 O -ANISOU 1840 O LEU A 281 979 1122 659 -108 99 7 O -ATOM 1841 CB LEU A 281 46.860 25.180 -0.831 1.00 8.36 C -ANISOU 1841 CB LEU A 281 1229 1017 931 -218 140 -7 C -ATOM 1842 CG LEU A 281 46.948 25.287 -2.354 1.00 9.69 C -ANISOU 1842 CG LEU A 281 1411 1308 961 -205 169 -103 C -ATOM 1843 CD1 LEU A 281 47.295 23.940 -2.941 1.00 12.76 C -ANISOU 1843 CD1 LEU A 281 1976 1548 1323 -106 58 -154 C -ATOM 1844 CD2 LEU A 281 45.634 25.787 -2.931 1.00 11.18 C -ANISOU 1844 CD2 LEU A 281 1612 1586 1047 -210 -42 -118 C -ATOM 1845 N ALA A 282 45.292 26.530 1.675 1.00 6.55 N -ANISOU 1845 N ALA A 282 851 878 760 -156 67 86 N -ATOM 1846 CA ALA A 282 44.723 26.126 2.941 1.00 6.25 C -ANISOU 1846 CA ALA A 282 855 832 686 -99 63 -25 C -ATOM 1847 C ALA A 282 44.790 24.620 3.094 1.00 5.72 C -ANISOU 1847 C ALA A 282 739 837 596 -86 116 -33 C -ATOM 1848 O ALA A 282 44.795 23.870 2.119 1.00 6.98 O -ANISOU 1848 O ALA A 282 1111 919 619 -131 216 -60 O -ATOM 1849 CB ALA A 282 43.296 26.593 3.022 1.00 6.29 C -ANISOU 1849 CB ALA A 282 864 859 665 -137 -21 5 C -ATOM 1850 N GLU A 283 44.789 24.160 4.337 1.00 5.17 N -ANISOU 1850 N GLU A 283 790 651 521 -98 98 -104 N -ATOM 1851 CA GLU A 283 44.709 22.726 4.588 1.00 5.70 C -ANISOU 1851 CA GLU A 283 759 716 689 -11 84 -19 C -ATOM 1852 C GLU A 283 43.454 22.121 3.961 1.00 5.30 C -ANISOU 1852 C GLU A 283 730 719 565 2 97 -108 C -ATOM 1853 O GLU A 283 43.499 21.039 3.369 1.00 6.26 O -ANISOU 1853 O GLU A 283 843 847 687 18 81 -279 O -ATOM 1854 CB GLU A 283 44.744 22.461 6.094 1.00 5.69 C -ANISOU 1854 CB GLU A 283 777 770 613 -11 74 -85 C -ATOM 1855 CG GLU A 283 44.480 21.017 6.455 1.00 6.55 C -ANISOU 1855 CG GLU A 283 1049 775 662 -43 77 -8 C -ATOM 1856 CD GLU A 283 44.361 20.745 7.929 1.00 6.26 C -ANISOU 1856 CD GLU A 283 970 518 887 10 129 38 C -ATOM 1857 OE1 GLU A 283 44.705 21.602 8.755 1.00 6.99 O -ANISOU 1857 OE1 GLU A 283 1106 757 791 -150 -25 -26 O -ATOM 1858 OE2 GLU A 283 43.885 19.638 8.249 1.00 8.17 O -ANISOU 1858 OE2 GLU A 283 1540 695 867 -82 326 -66 O -ATOM 1859 N GLY A 284 42.330 22.809 4.168 1.00 4.94 N -ANISOU 1859 N GLY A 284 649 608 619 -35 96 -116 N -ATOM 1860 CA GLY A 284 41.047 22.356 3.684 1.00 5.27 C -ANISOU 1860 CA GLY A 284 727 681 591 -35 109 -150 C -ATOM 1861 C GLY A 284 39.944 23.098 4.382 1.00 4.70 C -ANISOU 1861 C GLY A 284 656 638 490 -34 20 -111 C -ATOM 1862 O GLY A 284 40.120 24.239 4.774 1.00 4.81 O -ANISOU 1862 O GLY A 284 750 555 522 -55 37 -107 O -ATOM 1863 N VAL A 285 38.804 22.427 4.504 1.00 4.57 N -ANISOU 1863 N VAL A 285 598 605 531 -4 76 -78 N -ATOM 1864 CA VAL A 285 37.627 22.982 5.159 1.00 4.56 C -ANISOU 1864 CA VAL A 285 604 577 552 17 31 -61 C -ATOM 1865 C VAL A 285 37.010 21.981 6.115 1.00 4.61 C -ANISOU 1865 C VAL A 285 582 544 626 21 31 -54 C -ATOM 1866 O VAL A 285 37.176 20.763 5.970 1.00 4.93 O -ANISOU 1866 O VAL A 285 734 517 621 15 199 -86 O -ATOM 1867 CB VAL A 285 36.548 23.462 4.151 1.00 5.04 C -ANISOU 1867 CB VAL A 285 692 639 583 32 12 -37 C -ATOM 1868 CG1 VAL A 285 37.097 24.614 3.321 1.00 6.08 C -ANISOU 1868 CG1 VAL A 285 837 743 730 41 -48 -42 C -ATOM 1869 CG2 VAL A 285 36.023 22.333 3.287 1.00 6.32 C -ANISOU 1869 CG2 VAL A 285 838 785 776 -29 -42 -181 C -ATOM 1870 N VAL A 286 36.294 22.520 7.097 1.00 3.98 N -ANISOU 1870 N VAL A 286 549 429 535 5 56 -69 N -ATOM 1871 CA VAL A 286 35.398 21.760 7.949 1.00 4.31 C -ANISOU 1871 CA VAL A 286 604 488 545 47 80 14 C -ATOM 1872 C VAL A 286 33.979 22.163 7.581 1.00 4.45 C -ANISOU 1872 C VAL A 286 608 485 595 50 62 -11 C -ATOM 1873 O VAL A 286 33.669 23.355 7.470 1.00 5.08 O -ANISOU 1873 O VAL A 286 636 488 803 90 14 20 O -ATOM 1874 CB VAL A 286 35.682 22.050 9.432 1.00 4.84 C -ANISOU 1874 CB VAL A 286 672 576 591 44 70 -25 C -ATOM 1875 CG1 VAL A 286 34.632 21.442 10.340 1.00 5.51 C -ANISOU 1875 CG1 VAL A 286 781 728 584 57 40 13 C -ATOM 1876 CG2 VAL A 286 37.072 21.519 9.801 1.00 5.34 C -ANISOU 1876 CG2 VAL A 286 669 679 680 -47 48 -54 C -ATOM 1877 N ILE A 287 33.134 21.156 7.363 1.00 4.90 N -ANISOU 1877 N ILE A 287 627 522 711 73 35 -3 N -ATOM 1878 CA ILE A 287 31.742 21.361 6.970 1.00 4.88 C -ANISOU 1878 CA ILE A 287 591 517 745 60 7 30 C -ATOM 1879 C ILE A 287 30.880 20.861 8.110 1.00 4.87 C -ANISOU 1879 C ILE A 287 507 577 765 65 12 27 C -ATOM 1880 O ILE A 287 31.066 19.749 8.613 1.00 5.64 O -ANISOU 1880 O ILE A 287 644 597 901 81 108 112 O -ATOM 1881 CB ILE A 287 31.454 20.612 5.658 1.00 5.65 C -ANISOU 1881 CB ILE A 287 729 612 803 69 -56 -36 C -ATOM 1882 CG1 ILE A 287 32.210 21.311 4.513 1.00 6.69 C -ANISOU 1882 CG1 ILE A 287 856 819 864 23 -30 1 C -ATOM 1883 CG2 ILE A 287 29.966 20.532 5.390 1.00 6.65 C -ANISOU 1883 CG2 ILE A 287 797 924 803 -30 -40 -60 C -ATOM 1884 CD1 ILE A 287 32.283 20.504 3.229 1.00 7.77 C -ANISOU 1884 CD1 ILE A 287 1042 1004 904 20 36 -109 C -ATOM 1885 N ARG A 288 29.924 21.684 8.530 1.00 5.30 N -ANISOU 1885 N ARG A 288 594 612 808 69 118 120 N -ATOM 1886 CA ARG A 288 29.090 21.339 9.667 1.00 5.35 C -ANISOU 1886 CA ARG A 288 596 634 801 59 21 37 C -ATOM 1887 C ARG A 288 27.683 21.900 9.508 1.00 5.13 C -ANISOU 1887 C ARG A 288 566 602 778 98 1 -13 C -ATOM 1888 O ARG A 288 27.473 22.935 8.895 1.00 5.59 O -ANISOU 1888 O ARG A 288 591 651 880 89 10 13 O -ATOM 1889 CB ARG A 288 29.703 21.830 10.978 1.00 6.21 C -ANISOU 1889 CB ARG A 288 610 887 860 88 75 87 C -ATOM 1890 CG ARG A 288 29.902 23.331 11.047 1.00 7.15 C -ANISOU 1890 CG ARG A 288 779 1019 916 -37 -33 -4 C -ATOM 1891 CD ARG A 288 30.782 23.711 12.205 1.00 8.37 C -ANISOU 1891 CD ARG A 288 916 1228 1034 -116 -48 -76 C -ATOM 1892 NE ARG A 288 30.097 23.543 13.479 1.00 7.60 N -ANISOU 1892 NE ARG A 288 719 1260 908 -209 -26 -49 N -ATOM 1893 CZ ARG A 288 30.712 23.360 14.638 1.00 7.30 C -ANISOU 1893 CZ ARG A 288 750 1067 955 -106 -133 -66 C -ATOM 1894 NH1 ARG A 288 32.034 23.243 14.700 1.00 7.77 N -ANISOU 1894 NH1 ARG A 288 822 1167 963 132 -108 -255 N -ATOM 1895 NH2 ARG A 288 30.000 23.243 15.750 1.00 7.40 N -ANISOU 1895 NH2 ARG A 288 723 1166 922 106 -81 -25 N -ATOM 1896 N HIS A 289 26.735 21.216 10.119 1.00 5.36 N -ANISOU 1896 N HIS A 289 601 640 797 97 -49 -5 N -ATOM 1897 CA HIS A 289 25.347 21.661 10.166 1.00 4.88 C -ANISOU 1897 CA HIS A 289 544 606 702 104 1 -30 C -ATOM 1898 C HIS A 289 25.287 22.902 11.031 1.00 5.22 C -ANISOU 1898 C HIS A 289 515 648 820 76 -19 -83 C -ATOM 1899 O HIS A 289 25.900 22.941 12.095 1.00 5.93 O -ANISOU 1899 O HIS A 289 588 809 854 38 -21 -78 O -ATOM 1900 CB HIS A 289 24.492 20.531 10.767 1.00 5.71 C -ANISOU 1900 CB HIS A 289 653 593 923 58 33 10 C -ATOM 1901 CG HIS A 289 23.022 20.736 10.654 1.00 6.16 C -ANISOU 1901 CG HIS A 289 694 750 896 72 73 -124 C -ATOM 1902 ND1 HIS A 289 22.381 21.815 11.195 1.00 7.90 N -ANISOU 1902 ND1 HIS A 289 669 824 1507 -105 71 -227 N -ATOM 1903 CD2 HIS A 289 22.054 19.930 10.165 1.00 8.97 C -ANISOU 1903 CD2 HIS A 289 920 882 1604 45 13 -171 C -ATOM 1904 CE1 HIS A 289 21.091 21.723 10.938 1.00 7.86 C -ANISOU 1904 CE1 HIS A 289 712 691 1580 95 91 -188 C -ATOM 1905 NE2 HIS A 289 20.866 20.595 10.304 1.00 8.11 N -ANISOU 1905 NE2 HIS A 289 660 1114 1305 87 0 -65 N -ATOM 1906 N VAL A 290 24.521 23.905 10.630 1.00 5.87 N -ANISOU 1906 N VAL A 290 638 731 857 67 -3 -142 N -ATOM 1907 CA VAL A 290 24.488 25.142 11.390 1.00 6.53 C -ANISOU 1907 CA VAL A 290 749 698 1034 38 69 -115 C -ATOM 1908 C VAL A 290 23.858 25.000 12.770 1.00 6.52 C -ANISOU 1908 C VAL A 290 709 676 1089 72 53 -88 C -ATOM 1909 O VAL A 290 24.050 25.878 13.606 1.00 6.88 O -ANISOU 1909 O VAL A 290 777 710 1124 9 71 -223 O -ATOM 1910 CB VAL A 290 23.836 26.310 10.618 1.00 7.79 C -ANISOU 1910 CB VAL A 290 973 774 1212 113 133 -35 C -ATOM 1911 CG1 VAL A 290 24.584 26.591 9.329 1.00 8.54 C -ANISOU 1911 CG1 VAL A 290 1124 887 1234 139 117 13 C -ATOM 1912 CG2 VAL A 290 22.356 26.089 10.409 1.00 8.74 C -ANISOU 1912 CG2 VAL A 290 1078 1006 1236 210 101 -29 C -ATOM 1913 N ARG A 291 23.121 23.919 13.011 1.00 6.70 N -ANISOU 1913 N ARG A 291 714 823 1007 32 78 -97 N -ATOM 1914 CA ARG A 291 22.558 23.636 14.325 1.00 7.46 C -ANISOU 1914 CA ARG A 291 743 961 1131 26 172 -87 C -ATOM 1915 C ARG A 291 23.140 22.375 14.932 1.00 7.30 C -ANISOU 1915 C ARG A 291 767 914 1093 20 167 -117 C -ATOM 1916 O ARG A 291 22.545 21.780 15.815 1.00 8.31 O -ANISOU 1916 O ARG A 291 843 1082 1232 40 338 -28 O -ATOM 1917 CB ARG A 291 21.029 23.594 14.277 1.00 8.90 C -ANISOU 1917 CB ARG A 291 913 1153 1314 54 207 -77 C -ATOM 1918 CG ARG A 291 20.465 24.959 13.915 1.00 13.01 C -ANISOU 1918 CG ARG A 291 1252 1805 1886 215 283 154 C -ATOM 1919 CD ARG A 291 20.653 26.061 14.968 1.00 19.77 C -ANISOU 1919 CD ARG A 291 2372 2489 2648 43 122 103 C -ATOM 1920 NE ARG A 291 19.893 25.853 16.209 1.00 23.69 N -ANISOU 1920 NE ARG A 291 2943 2992 3064 114 176 -75 N -ATOM 1921 CZ ARG A 291 19.894 26.689 17.259 1.00 27.86 C -ANISOU 1921 CZ ARG A 291 3511 3546 3527 -68 111 -20 C -ATOM 1922 NH1 ARG A 291 20.636 27.794 17.257 1.00 29.34 N -ANISOU 1922 NH1 ARG A 291 3791 3645 3711 -37 157 -35 N -ATOM 1923 NH2 ARG A 291 19.166 26.403 18.335 1.00 29.81 N -ANISOU 1923 NH2 ARG A 291 3798 3779 3749 -44 94 7 N -ATOM 1924 N ARG A 292 24.344 22.007 14.512 1.00 7.26 N -ANISOU 1924 N ARG A 292 815 924 1018 51 171 -129 N -ATOM 1925 CA ARG A 292 25.083 20.949 15.190 1.00 7.74 C -ANISOU 1925 CA ARG A 292 875 1062 1005 48 118 -45 C -ATOM 1926 C ARG A 292 25.039 21.172 16.702 1.00 8.11 C -ANISOU 1926 C ARG A 292 915 1060 1105 60 158 -87 C -ATOM 1927 O ARG A 292 25.284 22.279 17.190 1.00 8.45 O -ANISOU 1927 O ARG A 292 991 1207 1010 3 275 -197 O -ATOM 1928 CB ARG A 292 26.533 20.932 14.719 1.00 7.31 C -ANISOU 1928 CB ARG A 292 823 1004 947 98 181 -148 C -ATOM 1929 CG ARG A 292 27.425 20.000 15.474 1.00 9.06 C -ANISOU 1929 CG ARG A 292 990 1369 1081 314 127 -18 C -ATOM 1930 CD ARG A 292 28.706 19.723 14.710 1.00 9.52 C -ANISOU 1930 CD ARG A 292 925 1522 1167 422 95 81 C -ATOM 1931 NE ARG A 292 29.514 18.683 15.360 1.00 13.46 N -ANISOU 1931 NE ARG A 292 1248 2296 1569 459 461 -50 N -ATOM 1932 CZ ARG A 292 30.316 18.903 16.352 1.00 13.64 C -ANISOU 1932 CZ ARG A 292 1240 2210 1732 376 465 -97 C -ATOM 1933 NH1 ARG A 292 30.499 20.135 16.795 1.00 15.43 N -ANISOU 1933 NH1 ARG A 292 1683 2119 2059 288 -64 -170 N -ATOM 1934 NH2 ARG A 292 30.976 17.893 16.905 1.00 12.06 N -ANISOU 1934 NH2 ARG A 292 1453 1560 1568 468 31 151 N -ATOM 1935 N GLY A 293 24.719 20.120 17.436 1.00 9.14 N -ANISOU 1935 N GLY A 293 1071 1290 1111 10 171 -62 N -ATOM 1936 CA GLY A 293 24.597 20.200 18.880 1.00 9.93 C -ANISOU 1936 CA GLY A 293 1212 1387 1173 -53 105 -31 C -ATOM 1937 C GLY A 293 23.178 20.390 19.386 1.00 10.47 C -ANISOU 1937 C GLY A 293 1341 1486 1152 -54 266 -102 C -ATOM 1938 O GLY A 293 22.904 20.105 20.557 1.00 12.86 O -ANISOU 1938 O GLY A 293 1734 1975 1176 -71 361 -10 O -ATOM 1939 N ASP A 294 22.271 20.868 18.544 1.00 10.45 N -ANISOU 1939 N ASP A 294 1297 1434 1239 1 352 -141 N -ATOM 1940 CA ASP A 294 20.880 21.052 18.953 1.00 11.81 C -ANISOU 1940 CA ASP A 294 1447 1553 1488 44 292 -139 C -ATOM 1941 C ASP A 294 20.230 19.687 19.098 1.00 11.76 C -ANISOU 1941 C ASP A 294 1419 1612 1434 14 350 -132 C -ATOM 1942 O ASP A 294 20.431 18.826 18.249 1.00 10.49 O -ANISOU 1942 O ASP A 294 1186 1361 1438 36 360 -201 O -ATOM 1943 CB ASP A 294 20.135 21.853 17.899 1.00 12.62 C -ANISOU 1943 CB ASP A 294 1463 1577 1752 118 316 -138 C -ATOM 1944 CG ASP A 294 18.711 22.155 18.305 1.00 16.43 C -ANISOU 1944 CG ASP A 294 1910 1905 2425 184 255 -129 C -ATOM 1945 OD1 ASP A 294 18.454 23.275 18.779 1.00 23.07 O -ANISOU 1945 OD1 ASP A 294 2654 2742 3369 331 492 -263 O -ATOM 1946 OD2 ASP A 294 17.794 21.334 18.205 1.00 20.46 O -ANISOU 1946 OD2 ASP A 294 1908 2522 3341 411 538 32 O -ATOM 1947 N PRO A 295 19.465 19.452 20.170 1.00 13.04 N -ANISOU 1947 N PRO A 295 1646 1729 1579 -45 314 -117 N -ATOM 1948 CA PRO A 295 18.816 18.148 20.347 1.00 13.41 C -ANISOU 1948 CA PRO A 295 1655 1787 1653 -56 298 -57 C -ATOM 1949 C PRO A 295 18.017 17.647 19.148 1.00 12.36 C -ANISOU 1949 C PRO A 295 1440 1669 1585 -45 394 -25 C -ATOM 1950 O PRO A 295 18.015 16.451 18.918 1.00 12.76 O -ANISOU 1950 O PRO A 295 1504 1556 1788 0 502 -101 O -ATOM 1951 CB PRO A 295 17.896 18.370 21.551 1.00 14.58 C -ANISOU 1951 CB PRO A 295 1835 2001 1702 -59 290 -64 C -ATOM 1952 CG PRO A 295 18.516 19.459 22.304 1.00 15.54 C -ANISOU 1952 CG PRO A 295 2001 2045 1857 -23 236 -48 C -ATOM 1953 CD PRO A 295 19.209 20.343 21.320 1.00 14.11 C -ANISOU 1953 CD PRO A 295 1791 1926 1643 -63 305 -109 C -ATOM 1954 N ALA A 296 17.338 18.515 18.414 1.00 12.24 N -ANISOU 1954 N ALA A 296 1357 1626 1664 126 386 -95 N -ATOM 1955 CA ALA A 296 16.563 18.083 17.260 1.00 12.75 C -ANISOU 1955 CA ALA A 296 1489 1645 1708 76 165 -37 C -ATOM 1956 C ALA A 296 17.464 17.609 16.115 1.00 12.44 C -ANISOU 1956 C ALA A 296 1454 1599 1671 89 150 -73 C -ATOM 1957 O ALA A 296 17.038 16.817 15.286 1.00 14.64 O -ANISOU 1957 O ALA A 296 1550 1993 2020 -89 86 -103 O -ATOM 1958 CB ALA A 296 15.620 19.183 16.774 1.00 14.02 C -ANISOU 1958 CB ALA A 296 1638 1813 1875 114 74 -12 C -ATOM 1959 N VAL A 297 18.696 18.101 16.050 1.00 11.35 N -ANISOU 1959 N VAL A 297 1373 1411 1525 62 201 -129 N -ATOM 1960 CA VAL A 297 19.686 17.573 15.102 1.00 11.37 C -ANISOU 1960 CA VAL A 297 1414 1489 1417 -34 187 -137 C -ATOM 1961 C VAL A 297 20.300 16.291 15.638 1.00 10.85 C -ANISOU 1961 C VAL A 297 1226 1405 1490 -5 215 -158 C -ATOM 1962 O VAL A 297 20.427 15.294 14.932 1.00 11.02 O -ANISOU 1962 O VAL A 297 1231 1415 1539 25 238 -377 O -ATOM 1963 CB VAL A 297 20.802 18.600 14.840 1.00 12.26 C -ANISOU 1963 CB VAL A 297 1549 1636 1471 -98 225 -123 C -ATOM 1964 CG1 VAL A 297 22.001 17.964 14.107 1.00 12.81 C -ANISOU 1964 CG1 VAL A 297 1645 1715 1505 -225 159 -151 C -ATOM 1965 CG2 VAL A 297 20.248 19.746 14.046 1.00 14.27 C -ANISOU 1965 CG2 VAL A 297 1875 1780 1767 -74 9 -216 C -ATOM 1966 N GLU A 298 20.707 16.327 16.889 1.00 11.35 N -ANISOU 1966 N GLU A 298 1321 1416 1575 67 123 -88 N -ATOM 1967 CA GLU A 298 21.426 15.211 17.495 1.00 12.68 C -ANISOU 1967 CA GLU A 298 1542 1538 1736 90 31 -45 C -ATOM 1968 C GLU A 298 20.585 13.956 17.631 1.00 12.10 C -ANISOU 1968 C GLU A 298 1511 1463 1620 126 49 -31 C -ATOM 1969 O GLU A 298 21.129 12.866 17.694 1.00 12.22 O -ANISOU 1969 O GLU A 298 1590 1419 1633 286 -3 52 O -ATOM 1970 CB GLU A 298 21.936 15.613 18.882 1.00 13.76 C -ANISOU 1970 CB GLU A 298 1685 1670 1872 125 -44 -43 C -ATOM 1971 CG GLU A 298 22.959 16.729 18.859 1.00 15.90 C -ANISOU 1971 CG GLU A 298 1931 1884 2225 144 -25 -112 C -ATOM 1972 CD GLU A 298 24.120 16.391 17.957 1.00 17.80 C -ANISOU 1972 CD GLU A 298 2176 2078 2509 75 61 -165 C -ATOM 1973 OE1 GLU A 298 24.715 15.318 18.185 1.00 17.49 O -ANISOU 1973 OE1 GLU A 298 2065 2077 2503 33 232 148 O -ATOM 1974 OE2 GLU A 298 24.419 17.155 16.998 1.00 18.24 O -ANISOU 1974 OE2 GLU A 298 2038 2099 2791 397 -167 -375 O -ATOM 1975 N LYS A 299 19.264 14.103 17.649 1.00 12.00 N -ANISOU 1975 N LYS A 299 1512 1459 1588 39 103 31 N -ATOM 1976 CA LYS A 299 18.387 12.960 17.831 1.00 11.96 C -ANISOU 1976 CA LYS A 299 1481 1481 1580 6 153 67 C -ATOM 1977 C LYS A 299 18.562 11.933 16.722 1.00 11.04 C -ANISOU 1977 C LYS A 299 1355 1393 1447 -12 187 138 C -ATOM 1978 O LYS A 299 18.241 10.778 16.910 1.00 11.87 O -ANISOU 1978 O LYS A 299 1637 1345 1527 -123 335 269 O -ATOM 1979 CB LYS A 299 16.916 13.406 17.924 1.00 13.12 C -ANISOU 1979 CB LYS A 299 1549 1671 1765 -64 245 36 C -ATOM 1980 CG LYS A 299 16.315 13.879 16.622 1.00 14.63 C -ANISOU 1980 CG LYS A 299 1541 1976 2042 61 264 1 C -ATOM 1981 CD LYS A 299 14.823 14.207 16.734 1.00 18.08 C -ANISOU 1981 CD LYS A 299 1921 2520 2428 66 187 2 C -ATOM 1982 CE LYS A 299 14.305 14.851 15.448 1.00 20.05 C -ANISOU 1982 CE LYS A 299 2020 2933 2665 162 44 -155 C -ATOM 1983 NZ LYS A 299 12.830 15.127 15.487 1.00 22.97 N -ANISOU 1983 NZ LYS A 299 2148 3365 3213 147 163 -107 N -ATOM 1984 N HIS A 300 19.021 12.354 15.549 1.00 9.79 N -ANISOU 1984 N HIS A 300 1164 1164 1390 32 207 228 N -ATOM 1985 CA HIS A 300 19.188 11.434 14.433 1.00 8.95 C -ANISOU 1985 CA HIS A 300 1064 1146 1191 17 129 175 C -ATOM 1986 C HIS A 300 20.392 10.511 14.561 1.00 8.41 C -ANISOU 1986 C HIS A 300 1057 977 1160 22 200 164 C -ATOM 1987 O HIS A 300 20.546 9.589 13.774 1.00 9.88 O -ANISOU 1987 O HIS A 300 1229 1194 1330 96 138 66 O -ATOM 1988 CB HIS A 300 19.297 12.219 13.143 1.00 9.44 C -ANISOU 1988 CB HIS A 300 1107 1190 1288 -24 90 138 C -ATOM 1989 CG HIS A 300 18.084 13.033 12.848 1.00 9.82 C -ANISOU 1989 CG HIS A 300 986 1301 1444 102 73 79 C -ATOM 1990 ND1 HIS A 300 17.022 12.550 12.117 1.00 13.98 N -ANISOU 1990 ND1 HIS A 300 1361 1772 2176 115 -79 40 N -ATOM 1991 CD2 HIS A 300 17.739 14.283 13.236 1.00 13.47 C -ANISOU 1991 CD2 HIS A 300 1501 1526 2089 151 -257 -39 C -ATOM 1992 CE1 HIS A 300 16.102 13.489 12.018 1.00 13.24 C -ANISOU 1992 CE1 HIS A 300 1391 1656 1981 284 -190 -4 C -ATOM 1993 NE2 HIS A 300 16.508 14.548 12.692 1.00 13.57 N -ANISOU 1993 NE2 HIS A 300 1337 1706 2113 419 -221 -144 N -ATOM 1994 N ASN A 301 21.261 10.773 15.525 1.00 8.92 N -ANISOU 1994 N ASN A 301 1128 1026 1234 4 212 102 N -ATOM 1995 CA ASN A 301 22.418 9.916 15.780 1.00 8.79 C -ANISOU 1995 CA ASN A 301 1095 1064 1179 18 179 101 C -ATOM 1996 C ASN A 301 23.349 9.811 14.570 1.00 8.93 C -ANISOU 1996 C ASN A 301 1132 1020 1240 -10 221 65 C -ATOM 1997 O ASN A 301 23.896 8.747 14.298 1.00 9.88 O -ANISOU 1997 O ASN A 301 1418 996 1340 47 459 125 O -ATOM 1998 CB ASN A 301 21.966 8.525 16.227 1.00 9.31 C -ANISOU 1998 CB ASN A 301 1165 1148 1221 4 176 154 C -ATOM 1999 CG ASN A 301 23.099 7.680 16.756 1.00 10.16 C -ANISOU 1999 CG ASN A 301 1264 1316 1278 -2 43 140 C -ATOM 2000 OD1 ASN A 301 23.968 8.160 17.495 1.00 11.85 O -ANISOU 2000 OD1 ASN A 301 1491 1601 1410 46 -34 294 O -ATOM 2001 ND2 ASN A 301 23.075 6.396 16.413 1.00 11.13 N -ANISOU 2001 ND2 ASN A 301 1404 1403 1419 94 194 341 N -ATOM 2002 N VAL A 302 23.537 10.932 13.878 1.00 8.78 N -ANISOU 2002 N VAL A 302 1128 1019 1189 -77 281 34 N -ATOM 2003 CA VAL A 302 24.481 11.024 12.775 1.00 9.58 C -ANISOU 2003 CA VAL A 302 1207 1099 1330 -85 261 44 C -ATOM 2004 C VAL A 302 25.357 12.247 12.994 1.00 8.39 C -ANISOU 2004 C VAL A 302 1068 932 1185 -110 264 90 C -ATOM 2005 O VAL A 302 24.862 13.374 13.199 1.00 9.60 O -ANISOU 2005 O VAL A 302 1085 920 1643 -99 364 94 O -ATOM 2006 CB VAL A 302 23.778 11.098 11.420 1.00 10.12 C -ANISOU 2006 CB VAL A 302 1218 1189 1436 -351 296 27 C -ATOM 2007 CG1 VAL A 302 22.907 12.263 11.285 1.00 16.11 C -ANISOU 2007 CG1 VAL A 302 1962 2211 1947 -70 180 23 C -ATOM 2008 CG2 VAL A 302 24.795 11.046 10.295 1.00 11.28 C -ANISOU 2008 CG2 VAL A 302 1498 1377 1409 -256 300 -11 C -ATOM 2009 N SER A 303 26.668 12.049 12.975 1.00 8.16 N -ANISOU 2009 N SER A 303 1027 877 1194 -11 209 87 N -ATOM 2010 CA SER A 303 27.566 13.173 13.179 1.00 7.82 C -ANISOU 2010 CA SER A 303 1009 900 1062 -1 135 75 C -ATOM 2011 C SER A 303 27.408 14.210 12.060 1.00 6.73 C -ANISOU 2011 C SER A 303 829 814 914 -11 149 37 C -ATOM 2012 O SER A 303 27.357 13.875 10.881 1.00 7.09 O -ANISOU 2012 O SER A 303 929 837 926 -70 244 -79 O -ATOM 2013 CB SER A 303 29.006 12.687 13.260 1.00 9.01 C -ANISOU 2013 CB SER A 303 1086 1075 1262 30 36 165 C -ATOM 2014 OG SER A 303 29.881 13.779 13.215 1.00 10.60 O -ANISOU 2014 OG SER A 303 1138 1203 1686 -43 -114 141 O -ATOM 2015 N THR A 304 27.349 15.471 12.457 1.00 6.52 N -ANISOU 2015 N THR A 304 812 734 930 -28 104 -4 N -ATOM 2016 CA THR A 304 27.143 16.556 11.494 1.00 7.00 C -ANISOU 2016 CA THR A 304 764 771 1124 -11 110 65 C -ATOM 2017 C THR A 304 28.367 17.437 11.337 1.00 5.94 C -ANISOU 2017 C THR A 304 716 681 859 -46 54 69 C -ATOM 2018 O THR A 304 28.245 18.641 11.132 1.00 6.73 O -ANISOU 2018 O THR A 304 734 685 1136 45 32 4 O -ATOM 2019 CB THR A 304 25.940 17.380 11.818 1.00 9.22 C -ANISOU 2019 CB THR A 304 943 1038 1519 -2 255 62 C -ATOM 2020 OG1 THR A 304 26.086 17.865 13.140 1.00 11.87 O -ANISOU 2020 OG1 THR A 304 974 1315 2218 -180 748 -234 O -ATOM 2021 CG2 THR A 304 24.658 16.565 11.778 1.00 11.20 C -ANISOU 2021 CG2 THR A 304 1056 1230 1968 61 95 73 C -ATOM 2022 N ILE A 305 29.539 16.822 11.373 1.00 5.67 N -ANISOU 2022 N ILE A 305 685 618 851 55 101 28 N -ATOM 2023 CA ILE A 305 30.775 17.524 11.063 1.00 5.33 C -ANISOU 2023 CA ILE A 305 725 570 731 26 115 60 C -ATOM 2024 C ILE A 305 31.656 16.609 10.238 1.00 5.43 C -ANISOU 2024 C ILE A 305 726 558 778 12 68 34 C -ATOM 2025 O ILE A 305 31.798 15.420 10.545 1.00 5.98 O -ANISOU 2025 O ILE A 305 929 568 772 78 211 -23 O -ATOM 2026 CB ILE A 305 31.451 18.050 12.354 1.00 5.68 C -ANISOU 2026 CB ILE A 305 762 605 791 5 160 -7 C -ATOM 2027 CG1 ILE A 305 32.569 19.040 12.052 1.00 5.86 C -ANISOU 2027 CG1 ILE A 305 700 738 788 61 89 -92 C -ATOM 2028 CG2 ILE A 305 31.916 16.920 13.274 1.00 6.65 C -ANISOU 2028 CG2 ILE A 305 823 802 901 -17 150 68 C -ATOM 2029 CD1 ILE A 305 32.917 19.887 13.254 1.00 7.12 C -ANISOU 2029 CD1 ILE A 305 879 875 951 -151 206 -76 C -ATOM 2030 N ILE A 306 32.219 17.161 9.169 1.00 5.17 N -ANISOU 2030 N ILE A 306 626 620 716 84 66 60 N -ATOM 2031 CA ILE A 306 33.111 16.423 8.276 1.00 5.81 C -ANISOU 2031 CA ILE A 306 751 749 705 -60 23 -127 C -ATOM 2032 C ILE A 306 34.209 17.376 7.816 1.00 5.02 C -ANISOU 2032 C ILE A 306 630 584 692 30 32 -108 C -ATOM 2033 O ILE A 306 34.140 18.584 8.040 1.00 5.64 O -ANISOU 2033 O ILE A 306 681 595 865 31 136 -101 O -ATOM 2034 CB ILE A 306 32.398 15.812 7.056 1.00 7.65 C -ANISOU 2034 CB ILE A 306 925 1139 841 -140 76 -55 C -ATOM 2035 CG1 ILE A 306 31.693 16.886 6.281 1.00 9.32 C -ANISOU 2035 CG1 ILE A 306 1033 1166 1339 -97 149 -209 C -ATOM 2036 CG2 ILE A 306 31.446 14.687 7.431 1.00 9.83 C -ANISOU 2036 CG2 ILE A 306 1238 1345 1149 -142 -59 -171 C -ATOM 2037 CD1 ILE A 306 31.159 16.426 4.941 1.00 11.43 C -ANISOU 2037 CD1 ILE A 306 1436 1496 1412 99 -115 -75 C -ATOM 2038 N LYS A 307 35.231 16.835 7.169 1.00 5.32 N -ANISOU 2038 N LYS A 307 666 593 761 25 185 -87 N -ATOM 2039 CA LYS A 307 36.295 17.661 6.612 1.00 5.83 C -ANISOU 2039 CA LYS A 307 783 655 777 -5 174 -50 C -ATOM 2040 C LYS A 307 36.569 17.255 5.173 1.00 5.53 C -ANISOU 2040 C LYS A 307 761 546 794 59 200 -95 C -ATOM 2041 O LYS A 307 36.283 16.131 4.755 1.00 6.58 O -ANISOU 2041 O LYS A 307 974 660 866 -56 297 -190 O -ATOM 2042 CB LYS A 307 37.584 17.519 7.428 1.00 6.65 C -ANISOU 2042 CB LYS A 307 845 799 881 -95 113 -139 C -ATOM 2043 CG LYS A 307 38.237 16.162 7.232 1.00 7.79 C -ANISOU 2043 CG LYS A 307 971 909 1080 9 68 -157 C -ATOM 2044 CD LYS A 307 39.383 15.905 8.181 1.00 8.29 C -ANISOU 2044 CD LYS A 307 1108 875 1166 95 28 -331 C -ATOM 2045 CE LYS A 307 39.971 14.529 7.957 1.00 8.40 C -ANISOU 2045 CE LYS A 307 951 1046 1195 139 70 -429 C -ATOM 2046 NZ LYS A 307 40.613 14.028 9.188 1.00 9.13 N -ANISOU 2046 NZ LYS A 307 1192 1128 1145 35 -98 -387 N -ATOM 2047 N LEU A 308 37.139 18.196 4.427 1.00 5.82 N -ANISOU 2047 N LEU A 308 851 586 774 -55 214 -182 N -ATOM 2048 CA LEU A 308 37.752 17.954 3.130 1.00 6.00 C -ANISOU 2048 CA LEU A 308 874 673 732 0 205 -191 C -ATOM 2049 C LEU A 308 39.129 18.587 3.165 1.00 6.06 C -ANISOU 2049 C LEU A 308 831 656 814 -45 152 -165 C -ATOM 2050 O LEU A 308 39.283 19.699 3.664 1.00 7.15 O -ANISOU 2050 O LEU A 308 912 616 1187 -86 271 -268 O -ATOM 2051 CB LEU A 308 36.969 18.622 2.011 1.00 7.02 C -ANISOU 2051 CB LEU A 308 1012 734 921 -10 178 -226 C -ATOM 2052 CG LEU A 308 35.516 18.234 1.803 1.00 7.68 C -ANISOU 2052 CG LEU A 308 919 958 1041 41 82 -168 C -ATOM 2053 CD1 LEU A 308 34.886 19.114 0.754 1.00 9.04 C -ANISOU 2053 CD1 LEU A 308 1067 1035 1329 202 20 -152 C -ATOM 2054 CD2 LEU A 308 35.368 16.778 1.413 1.00 8.18 C -ANISOU 2054 CD2 LEU A 308 845 1030 1232 -27 26 -127 C -ATOM 2055 N ARG A 309 40.132 17.898 2.636 1.00 5.98 N -ANISOU 2055 N ARG A 309 807 696 765 -60 151 -174 N -ATOM 2056 CA ARG A 309 41.481 18.443 2.547 1.00 6.61 C -ANISOU 2056 CA ARG A 309 873 827 810 -83 94 -216 C -ATOM 2057 C ARG A 309 41.906 18.560 1.114 1.00 7.19 C -ANISOU 2057 C ARG A 309 957 889 885 -181 131 -220 C -ATOM 2058 O ARG A 309 41.480 17.790 0.243 1.00 8.20 O -ANISOU 2058 O ARG A 309 1059 1144 911 -337 222 -407 O -ATOM 2059 CB ARG A 309 42.493 17.607 3.309 1.00 7.76 C -ANISOU 2059 CB ARG A 309 907 993 1048 -61 124 -192 C -ATOM 2060 CG ARG A 309 42.378 17.774 4.797 1.00 8.42 C -ANISOU 2060 CG ARG A 309 1038 1090 1070 20 -26 -150 C -ATOM 2061 CD ARG A 309 43.117 16.728 5.552 1.00 11.67 C -ANISOU 2061 CD ARG A 309 1737 1481 1213 158 1 -330 C -ATOM 2062 NE ARG A 309 43.581 17.189 6.854 1.00 10.69 N -ANISOU 2062 NE ARG A 309 1510 1323 1226 80 55 -77 N -ATOM 2063 CZ ARG A 309 43.845 16.373 7.856 1.00 9.43 C -ANISOU 2063 CZ ARG A 309 1289 1012 1281 184 135 -89 C -ATOM 2064 NH1 ARG A 309 43.625 15.061 7.751 1.00 11.12 N -ANISOU 2064 NH1 ARG A 309 1469 1252 1502 -18 175 -165 N -ATOM 2065 NH2 ARG A 309 44.341 16.863 8.970 1.00 9.97 N -ANISOU 2065 NH2 ARG A 309 1390 1106 1289 22 78 -97 N -ATOM 2066 N CYS A 310 42.770 19.524 0.828 1.00 7.77 N -ANISOU 2066 N CYS A 310 903 1046 1003 -195 144 -203 N -ATOM 2067 CA CYS A 310 43.314 19.567 -0.523 1.00 8.99 C -ANISOU 2067 CA CYS A 310 1041 1195 1178 -147 222 -124 C -ATOM 2068 C CYS A 310 44.339 18.455 -0.711 1.00 9.35 C -ANISOU 2068 C CYS A 310 1097 1235 1218 -106 213 -139 C -ATOM 2069 O CYS A 310 45.044 18.057 0.208 1.00 9.61 O -ANISOU 2069 O CYS A 310 1144 1295 1212 32 415 -268 O -ATOM 2070 CB CYS A 310 43.857 20.929 -0.918 1.00 10.03 C -ANISOU 2070 CB CYS A 310 1125 1254 1431 -148 349 -75 C -ATOM 2071 SG CYS A 310 45.369 21.434 -0.112 1.00 11.95 S -ANISOU 2071 SG CYS A 310 1529 1428 1582 -198 264 -290 S -ATOM 2072 N SER A 311 44.400 17.953 -1.933 1.00 10.32 N -ANISOU 2072 N SER A 311 1274 1380 1266 -102 143 -204 N -ATOM 2073 CA SER A 311 45.300 16.868 -2.266 1.00 11.85 C -ANISOU 2073 CA SER A 311 1534 1567 1400 13 76 -245 C -ATOM 2074 C SER A 311 46.750 17.269 -2.058 1.00 11.66 C -ANISOU 2074 C SER A 311 1530 1565 1334 77 145 -320 C -ATOM 2075 O SER A 311 47.546 16.462 -1.609 1.00 12.98 O -ANISOU 2075 O SER A 311 1654 1729 1545 183 139 -502 O -ATOM 2076 CB SER A 311 45.065 16.404 -3.709 1.00 12.27 C -ANISOU 2076 CB SER A 311 1654 1588 1418 -59 50 -297 C -ATOM 2077 OG SER A 311 45.466 17.394 -4.643 1.00 16.04 O -ANISOU 2077 OG SER A 311 2340 2212 1541 45 62 -368 O -ATOM 2078 N SER A 312 47.073 18.521 -2.352 1.00 12.23 N -ANISOU 2078 N SER A 312 1457 1748 1441 49 187 -243 N -ATOM 2079 CA SER A 312 48.435 19.024 -2.196 1.00 13.57 C -ANISOU 2079 CA SER A 312 1621 1845 1688 -5 111 -191 C -ATOM 2080 C SER A 312 48.900 18.887 -0.744 1.00 12.78 C -ANISOU 2080 C SER A 312 1442 1772 1641 25 93 -280 C -ATOM 2081 O SER A 312 50.044 18.513 -0.483 1.00 14.18 O -ANISOU 2081 O SER A 312 1457 2023 1905 27 23 -469 O -ATOM 2082 CB SER A 312 48.512 20.482 -2.665 1.00 14.03 C -ANISOU 2082 CB SER A 312 1693 1921 1714 -106 112 -114 C -ATOM 2083 OG SER A 312 48.261 20.581 -4.059 1.00 18.53 O -ANISOU 2083 OG SER A 312 2285 2419 2337 -165 154 -13 O -ATOM 2084 N PHE A 313 48.006 19.197 0.198 1.00 12.15 N -ANISOU 2084 N PHE A 313 1458 1664 1491 22 62 -372 N -ATOM 2085 CA PHE A 313 48.311 19.067 1.617 1.00 12.15 C -ANISOU 2085 CA PHE A 313 1537 1541 1537 65 -4 -271 C -ATOM 2086 C PHE A 313 48.464 17.610 2.025 1.00 12.90 C -ANISOU 2086 C PHE A 313 1628 1645 1626 176 -14 -278 C -ATOM 2087 O PHE A 313 49.384 17.264 2.757 1.00 13.39 O -ANISOU 2087 O PHE A 313 1850 1563 1672 439 -47 -429 O -ATOM 2088 CB PHE A 313 47.228 19.736 2.465 1.00 11.67 C -ANISOU 2088 CB PHE A 313 1508 1444 1479 160 -43 -327 C -ATOM 2089 CG PHE A 313 47.461 19.608 3.946 1.00 11.86 C -ANISOU 2089 CG PHE A 313 1459 1552 1494 251 -178 -303 C -ATOM 2090 CD1 PHE A 313 48.280 20.508 4.614 1.00 13.24 C -ANISOU 2090 CD1 PHE A 313 2056 1296 1678 299 -307 -354 C -ATOM 2091 CD2 PHE A 313 46.865 18.594 4.661 1.00 12.34 C -ANISOU 2091 CD2 PHE A 313 1542 1726 1421 341 -149 -342 C -ATOM 2092 CE1 PHE A 313 48.513 20.373 5.976 1.00 14.12 C -ANISOU 2092 CE1 PHE A 313 2008 1601 1756 194 -358 -421 C -ATOM 2093 CE2 PHE A 313 47.089 18.456 6.020 1.00 13.24 C -ANISOU 2093 CE2 PHE A 313 1587 1752 1689 305 -50 -142 C -ATOM 2094 CZ PHE A 313 47.902 19.359 6.681 1.00 14.42 C -ANISOU 2094 CZ PHE A 313 1947 1899 1633 341 -207 -233 C -HETATM 2095 N MSE A 314 47.546 16.767 1.565 1.00 14.30 N -ANISOU 2095 N MSE A 314 1894 1740 1797 96 7 -207 N -HETATM 2096 CA MSE A 314 47.574 15.344 1.906 1.00 17.04 C -ANISOU 2096 CA MSE A 314 2258 2058 2159 98 -1 -125 C -HETATM 2097 C MSE A 314 48.876 14.697 1.427 1.00 18.17 C -ANISOU 2097 C MSE A 314 2373 2169 2361 104 -47 -110 C -HETATM 2098 O MSE A 314 49.415 13.826 2.101 1.00 19.59 O -ANISOU 2098 O MSE A 314 2667 2301 2474 258 -150 -133 O -HETATM 2099 CB MSE A 314 46.334 14.601 1.354 1.00 17.98 C -ANISOU 2099 CB MSE A 314 2364 2138 2328 63 -1 -119 C -HETATM 2100 CG MSE A 314 44.962 15.138 1.866 1.00 22.32 C -ANISOU 2100 CG MSE A 314 2829 2681 2968 -53 59 -131 C -HETATM 2101 SE AMSE A 314 43.366 14.034 1.742 0.50 25.64 SE -ANISOU 2101 SE AMSE A 314 3149 3024 3566 -111 -2 -185 SE -HETATM 2102 SE BMSE A 314 45.570 14.850 3.710 0.50 33.86 SE -ANISOU 2102 SE BMSE A 314 4508 4213 4142 76 207 61 SE -HETATM 2103 CE AMSE A 314 42.742 14.682 0.005 0.50 26.97 C -ANISOU 2103 CE AMSE A 314 3350 3394 3502 39 -10 -76 C -HETATM 2104 CE BMSE A 314 41.560 14.056 2.331 0.50 28.88 C -ANISOU 2104 CE BMSE A 314 3632 3690 3651 -21 182 17 C -ATOM 2105 N GLU A 315 49.404 15.167 0.301 1.00 18.78 N -ANISOU 2105 N GLU A 315 2448 2252 2436 158 -31 -141 N -ATOM 2106 CA GLU A 315 50.629 14.623 -0.282 1.00 20.66 C -ANISOU 2106 CA GLU A 315 2599 2570 2680 92 4 -82 C -ATOM 2107 C GLU A 315 51.880 14.980 0.523 1.00 21.30 C -ANISOU 2107 C GLU A 315 2641 2658 2791 116 0 -120 C -ATOM 2108 O GLU A 315 52.905 14.318 0.386 1.00 22.18 O -ANISOU 2108 O GLU A 315 2650 2752 3024 272 -17 -127 O -ATOM 2109 CB GLU A 315 50.796 15.124 -1.715 1.00 20.60 C -ANISOU 2109 CB GLU A 315 2568 2588 2668 105 40 -100 C -ATOM 2110 CG GLU A 315 49.827 14.509 -2.714 1.00 23.14 C -ANISOU 2110 CG GLU A 315 2931 2910 2949 75 70 -65 C -ATOM 2111 CD GLU A 315 49.696 15.322 -3.992 1.00 26.97 C -ANISOU 2111 CD GLU A 315 3414 3437 3396 -7 85 -55 C -ATOM 2112 OE1 GLU A 315 50.562 16.189 -4.251 1.00 29.88 O -ANISOU 2112 OE1 GLU A 315 3859 3805 3686 -148 165 34 O -ATOM 2113 OE2 GLU A 315 48.725 15.094 -4.744 1.00 30.02 O -ANISOU 2113 OE2 GLU A 315 3830 3943 3633 49 127 -90 O -ATOM 2114 N LEU A 316 51.812 16.028 1.343 1.00 22.13 N -ANISOU 2114 N LEU A 316 2742 2802 2864 86 -37 -89 N -ATOM 2115 CA LEU A 316 52.936 16.402 2.205 1.00 22.92 C -ANISOU 2115 CA LEU A 316 2860 2897 2949 24 -21 -58 C -ATOM 2116 C LEU A 316 53.189 15.335 3.270 1.00 23.60 C -ANISOU 2116 C LEU A 316 2931 2973 3061 2 -20 -27 C -ATOM 2117 O LEU A 316 52.284 14.591 3.657 1.00 25.02 O -ANISOU 2117 O LEU A 316 3079 3150 3274 18 -30 -14 O -ATOM 2118 CB LEU A 316 52.680 17.749 2.881 1.00 22.93 C -ANISOU 2118 CB LEU A 316 2861 2935 2916 -1 -53 -90 C -ATOM 2119 CG LEU A 316 52.494 18.953 1.961 1.00 22.56 C -ANISOU 2119 CG LEU A 316 2833 2867 2872 3 17 -110 C -ATOM 2120 CD1 LEU A 316 52.050 20.171 2.774 1.00 22.84 C -ANISOU 2120 CD1 LEU A 316 2924 2957 2797 -30 -80 -139 C -ATOM 2121 CD2 LEU A 316 53.762 19.249 1.167 1.00 22.88 C -ANISOU 2121 CD2 LEU A 316 2901 2938 2854 28 11 -101 C -TER 2122 LEU A 316 -HETATM 2123 MG MG A 502 45.408 19.600 12.379 1.00 5.17 MG -ANISOU 2123 MG MG A 502 683 555 724 49 -8 -33 MG -HETATM 2124 PG ATP A 501 46.034 17.442 14.649 1.00 8.07 P -ANISOU 2124 PG ATP A 501 1049 858 1156 103 -185 10 P -HETATM 2125 O1G ATP A 501 46.554 18.251 13.486 1.00 6.46 O -ANISOU 2125 O1G ATP A 501 841 780 833 141 -77 -20 O -HETATM 2126 O2G ATP A 501 47.012 16.440 15.214 1.00 9.86 O -ANISOU 2126 O2G ATP A 501 1237 949 1559 287 -271 142 O -HETATM 2127 O3G ATP A 501 45.415 18.289 15.759 1.00 9.14 O -ANISOU 2127 O3G ATP A 501 1443 976 1050 128 34 -44 O -HETATM 2128 PB ATP A 501 44.166 16.669 12.640 1.00 6.53 P -ANISOU 2128 PB ATP A 501 865 579 1035 51 -49 -22 P -HETATM 2129 O1B ATP A 501 44.846 15.767 11.696 1.00 8.60 O -ANISOU 2129 O1B ATP A 501 1217 670 1381 142 -44 -222 O -HETATM 2130 O2B ATP A 501 44.015 18.092 12.214 1.00 5.78 O -ANISOU 2130 O2B ATP A 501 796 521 879 44 -67 -30 O -HETATM 2131 O3B ATP A 501 44.807 16.562 14.092 1.00 7.50 O -ANISOU 2131 O3B ATP A 501 1215 778 855 0 -149 143 O -HETATM 2132 PA ATP A 501 41.441 16.004 12.024 1.00 6.54 P -ANISOU 2132 PA ATP A 501 979 589 915 -10 -107 -103 P -HETATM 2133 O1A ATP A 501 41.868 15.977 10.607 1.00 8.18 O -ANISOU 2133 O1A ATP A 501 1081 1121 905 -142 -154 -199 O -HETATM 2134 O2A ATP A 501 40.573 14.911 12.597 1.00 7.34 O -ANISOU 2134 O2A ATP A 501 1001 528 1259 -15 -22 -31 O -HETATM 2135 O3A ATP A 501 42.720 16.073 13.004 1.00 6.94 O -ANISOU 2135 O3A ATP A 501 1019 658 958 -43 -81 52 O -HETATM 2136 O5' ATP A 501 40.761 17.421 12.230 1.00 6.65 O -ANISOU 2136 O5' ATP A 501 1078 581 868 88 -113 -12 O -HETATM 2137 C5' ATP A 501 40.228 17.831 13.474 1.00 6.42 C -ANISOU 2137 C5' ATP A 501 807 712 917 -12 -29 5 C -HETATM 2138 C4' ATP A 501 41.034 18.978 14.030 1.00 5.20 C -ANISOU 2138 C4' ATP A 501 744 524 707 -14 70 -29 C -HETATM 2139 O4' ATP A 501 41.042 20.083 13.138 1.00 4.96 O -ANISOU 2139 O4' ATP A 501 755 401 727 56 46 -22 O -HETATM 2140 C3' ATP A 501 40.382 19.568 15.268 1.00 5.52 C -ANISOU 2140 C3' ATP A 501 830 602 665 66 100 63 C -HETATM 2141 O3' ATP A 501 40.575 18.803 16.426 1.00 7.48 O -ANISOU 2141 O3' ATP A 501 1253 818 768 122 105 91 O -HETATM 2142 C2' ATP A 501 40.973 20.967 15.342 1.00 4.80 C -ANISOU 2142 C2' ATP A 501 653 589 581 121 53 -44 C -HETATM 2143 O2' ATP A 501 42.117 20.993 16.172 1.00 6.19 O -ANISOU 2143 O2' ATP A 501 800 944 608 84 -83 32 O -HETATM 2144 C1' ATP A 501 41.343 21.265 13.892 1.00 4.22 C -ANISOU 2144 C1' ATP A 501 601 442 560 93 58 -77 C -HETATM 2145 N9 ATP A 501 40.602 22.354 13.240 1.00 3.78 N -ANISOU 2145 N9 ATP A 501 361 535 537 67 30 -5 N -HETATM 2146 C8 ATP A 501 41.171 23.310 12.442 1.00 4.18 C -ANISOU 2146 C8 ATP A 501 562 558 468 -99 72 -5 C -HETATM 2147 N7 ATP A 501 40.249 24.145 11.942 1.00 4.47 N -ANISOU 2147 N7 ATP A 501 576 605 515 -10 48 -5 N -HETATM 2148 C5 ATP A 501 39.058 23.679 12.418 1.00 3.65 C -ANISOU 2148 C5 ATP A 501 505 444 435 33 55 -43 C -HETATM 2149 C6 ATP A 501 37.744 24.121 12.264 1.00 4.22 C -ANISOU 2149 C6 ATP A 501 607 350 644 120 -7 1 C -HETATM 2150 N6 ATP A 501 37.382 25.103 11.430 1.00 5.27 N -ANISOU 2150 N6 ATP A 501 745 524 732 137 -9 -94 N -HETATM 2151 N1 ATP A 501 36.760 23.458 12.935 1.00 4.95 N -ANISOU 2151 N1 ATP A 501 520 746 613 -63 110 -121 N -HETATM 2152 C2 ATP A 501 37.057 22.401 13.740 1.00 4.70 C -ANISOU 2152 C2 ATP A 501 624 581 579 -41 -22 1 C -HETATM 2153 N3 ATP A 501 38.297 21.903 13.909 1.00 4.79 N -ANISOU 2153 N3 ATP A 501 667 555 596 -55 83 -64 N -HETATM 2154 C4 ATP A 501 39.267 22.569 13.244 1.00 3.29 C -ANISOU 2154 C4 ATP A 501 514 379 354 -22 56 -29 C -HETATM 2155 O HOH A 503 44.809 17.970 37.617 1.00 36.08 O -ANISOU 2155 O HOH A 503 4386 5537 3785 -520 -992 -1082 O -HETATM 2156 O HOH A 504 42.954 19.170 36.304 1.00 24.50 O -ANISOU 2156 O HOH A 504 2833 3518 2958 -2 -622 -1395 O -HETATM 2157 O HOH A 505 40.660 20.162 36.149 1.00 27.10 O -ANISOU 2157 O HOH A 505 3805 1890 4602 -257 16 196 O -HETATM 2158 O HOH A 506 44.237 20.691 37.847 1.00 31.69 O -ANISOU 2158 O HOH A 506 3809 4155 4075 198 -499 958 O -HETATM 2159 O HOH A 507 17.460 9.609 1.448 1.00 34.71 O -ANISOU 2159 O HOH A 507 4608 4863 3714 -192 -175 -460 O -HETATM 2160 O HOH A 508 33.710 21.548 35.755 1.00 34.55 O -ANISOU 2160 O HOH A 508 5177 5332 2618 160 -225 101 O -HETATM 2161 O HOH A 509 58.096 33.599 10.856 1.00 10.13 O -ANISOU 2161 O HOH A 509 1082 1042 1723 -139 -196 -17 O -HETATM 2162 O HOH A 510 55.267 27.929 14.039 1.00 7.63 O -ANISOU 2162 O HOH A 510 953 759 1183 -28 38 198 O -HETATM 2163 O HOH A 511 41.922 35.290 18.063 1.00 6.88 O -ANISOU 2163 O HOH A 511 938 678 996 199 -67 -96 O -HETATM 2164 O HOH A 512 58.073 34.302 13.567 1.00 8.10 O -ANISOU 2164 O HOH A 512 801 973 1303 -96 11 107 O -HETATM 2165 O HOH A 513 50.287 27.048 12.279 1.00 8.03 O -ANISOU 2165 O HOH A 513 825 826 1398 -48 156 -300 O -HETATM 2166 O HOH A 514 46.968 20.960 12.454 1.00 5.94 O -ANISOU 2166 O HOH A 514 726 663 867 7 40 -61 O -HETATM 2167 O HOH A 515 35.931 20.580 24.045 1.00 12.46 O -ANISOU 2167 O HOH A 515 1207 1404 2122 -92 -279 833 O -HETATM 2168 O HOH A 516 27.187 24.141 16.304 1.00 7.65 O -ANISOU 2168 O HOH A 516 820 1054 1031 138 -44 -167 O -HETATM 2169 O HOH A 517 39.455 21.182 24.948 1.00 8.14 O -ANISOU 2169 O HOH A 517 1202 1000 890 211 40 119 O -HETATM 2170 O HOH A 518 53.280 36.276 18.496 1.00 7.92 O -ANISOU 2170 O HOH A 518 1150 917 940 -141 -136 -144 O -HETATM 2171 O HOH A 519 61.158 36.077 18.867 1.00 8.92 O -ANISOU 2171 O HOH A 519 1027 1075 1285 -151 -112 101 O -HETATM 2172 O HOH A 520 46.186 19.099 10.482 1.00 6.57 O -ANISOU 2172 O HOH A 520 850 760 883 81 101 -233 O -HETATM 2173 O HOH A 521 30.077 26.561 18.558 1.00 6.94 O -ANISOU 2173 O HOH A 521 729 873 1032 20 12 -4 O -HETATM 2174 O HOH A 522 33.420 13.556 11.668 1.00 7.95 O -ANISOU 2174 O HOH A 522 935 884 1199 134 3 34 O -HETATM 2175 O HOH A 523 27.466 24.688 13.601 1.00 7.89 O -ANISOU 2175 O HOH A 523 897 962 1136 112 -110 -166 O -HETATM 2176 O HOH A 524 57.172 45.969 2.224 1.00 14.78 O -ANISOU 2176 O HOH A 524 1595 1560 2460 -463 604 -55 O -HETATM 2177 O HOH A 525 52.082 29.977 9.907 1.00 6.93 O -ANISOU 2177 O HOH A 525 738 1150 742 -23 52 135 O -HETATM 2178 O HOH A 526 35.850 39.285 16.890 1.00 8.23 O -ANISOU 2178 O HOH A 526 1316 712 1095 172 -99 -30 O -HETATM 2179 O HOH A 527 58.622 31.792 14.517 1.00 7.79 O -ANISOU 2179 O HOH A 527 810 1088 1061 -137 -34 161 O -HETATM 2180 O HOH A 528 44.239 21.032 11.319 1.00 5.59 O -ANISOU 2180 O HOH A 528 709 588 824 106 79 4 O -HETATM 2181 O HOH A 529 23.047 28.449 13.575 1.00 9.59 O -ANISOU 2181 O HOH A 529 883 1043 1717 141 79 -216 O -HETATM 2182 O HOH A 530 44.639 20.395 14.092 1.00 5.86 O -ANISOU 2182 O HOH A 530 773 642 811 34 34 -69 O -HETATM 2183 O HOH A 531 57.423 40.860 16.055 1.00 12.10 O -ANISOU 2183 O HOH A 531 1638 1146 1813 -146 -51 -64 O -HETATM 2184 O HOH A 532 42.580 35.536 20.672 1.00 9.97 O -ANISOU 2184 O HOH A 532 1367 1589 833 600 -127 -187 O -HETATM 2185 O HOH A 533 41.861 14.510 23.280 1.00 10.06 O -ANISOU 2185 O HOH A 533 1393 924 1505 -87 -127 207 O -HETATM 2186 O HOH A 534 58.410 35.573 9.030 1.00 12.96 O -ANISOU 2186 O HOH A 534 2520 1235 1168 -389 -198 159 O -HETATM 2187 O HOH A 535 37.675 41.407 29.946 1.00 9.02 O -ANISOU 2187 O HOH A 535 1505 931 989 160 -126 -352 O -HETATM 2188 O HOH A 536 46.386 19.244 17.947 1.00 9.72 O -ANISOU 2188 O HOH A 536 1343 994 1355 324 -192 -326 O -HETATM 2189 O HOH A 537 33.957 24.389 22.521 1.00 9.05 O -ANISOU 2189 O HOH A 537 1055 1466 915 47 199 108 O -HETATM 2190 O HOH A 538 51.195 26.221 30.174 1.00 11.66 O -ANISOU 2190 O HOH A 538 2295 1123 1011 478 -380 181 O -HETATM 2191 O HOH A 539 36.665 41.930 17.362 1.00 10.20 O -ANISOU 2191 O HOH A 539 1563 923 1389 156 -358 -93 O -HETATM 2192 O HOH A 540 32.690 24.707 9.752 1.00 11.68 O -ANISOU 2192 O HOH A 540 2163 957 1317 146 643 -4 O -HETATM 2193 O HOH A 541 46.038 26.111 32.387 1.00 11.65 O -ANISOU 2193 O HOH A 541 2200 1246 977 631 -426 -152 O -HETATM 2194 O HOH A 542 50.835 38.785 10.605 1.00 12.82 O -ANISOU 2194 O HOH A 542 1363 1021 2485 -104 -227 655 O -HETATM 2195 O HOH A 543 47.253 20.607 20.998 1.00 7.41 O -ANISOU 2195 O HOH A 543 1112 846 856 286 47 69 O -HETATM 2196 O HOH A 544 30.225 18.438 24.882 1.00 19.29 O -ANISOU 2196 O HOH A 544 1980 2601 2748 -454 173 -19 O -HETATM 2197 O HOH A 545 36.676 30.186 7.840 1.00 7.92 O -ANISOU 2197 O HOH A 545 1054 730 1222 199 37 -161 O -HETATM 2198 O HOH A 546 54.547 28.621 26.010 1.00 15.77 O -ANISOU 2198 O HOH A 546 3622 966 1403 -336 -1290 0 O -HETATM 2199 O HOH A 547 23.626 23.992 18.610 1.00 16.59 O -ANISOU 2199 O HOH A 547 1590 1857 2854 -231 342 -1086 O -HETATM 2200 O HOH A 548 24.281 21.253 22.644 1.00 16.66 O -ANISOU 2200 O HOH A 548 2164 2535 1631 -1018 278 -129 O -HETATM 2201 O HOH A 549 41.100 32.482 -0.400 1.00 18.61 O -ANISOU 2201 O HOH A 549 2198 2334 2538 281 -632 745 O -HETATM 2202 O HOH A 550 61.194 35.875 6.823 1.00 18.15 O -ANISOU 2202 O HOH A 550 2126 2545 2223 568 135 331 O -HETATM 2203 O HOH A 551 47.247 31.935 0.640 1.00 8.72 O -ANISOU 2203 O HOH A 551 1243 955 1113 -130 180 167 O -HETATM 2204 O HOH A 552 54.972 40.671 12.879 1.00 13.50 O -ANISOU 2204 O HOH A 552 1909 1159 2060 -135 147 268 O -HETATM 2205 O HOH A 553 41.617 37.400 3.258 1.00 19.94 O -ANISOU 2205 O HOH A 553 2042 1800 3734 -157 -895 900 O -HETATM 2206 O HOH A 554 32.150 10.566 7.405 1.00 10.95 O -ANISOU 2206 O HOH A 554 1188 1779 1193 -186 88 -173 O -HETATM 2207 O HOH A 555 22.644 18.077 0.346 1.00 11.45 O -ANISOU 2207 O HOH A 555 1230 1717 1402 -234 -124 -349 O -HETATM 2208 O HOH A 556 34.011 19.700 22.549 1.00 13.80 O -ANISOU 2208 O HOH A 556 1514 1855 1872 290 52 342 O -HETATM 2209 O HOH A 557 32.974 22.004 21.336 1.00 13.88 O -ANISOU 2209 O HOH A 557 1691 1889 1693 262 53 94 O -HETATM 2210 O HOH A 558 22.426 13.567 14.354 1.00 14.62 O -ANISOU 2210 O HOH A 558 1608 1172 2773 58 1171 94 O -HETATM 2211 O HOH A 559 57.043 40.605 11.123 1.00 13.42 O -ANISOU 2211 O HOH A 559 1666 1380 2051 -368 152 -130 O -HETATM 2212 O HOH A 560 22.846 26.497 21.560 1.00 14.76 O -ANISOU 2212 O HOH A 560 1475 2446 1687 327 299 54 O -HETATM 2213 O HOH A 561 54.395 19.248 11.019 1.00 18.56 O -ANISOU 2213 O HOH A 561 2479 1470 3100 501 293 -315 O -HETATM 2214 O HOH A 562 56.465 34.623 -2.914 1.00 21.44 O -ANISOU 2214 O HOH A 562 2402 1969 3774 -240 981 -22 O -HETATM 2215 O HOH A 563 58.853 41.091 13.616 1.00 17.00 O -ANISOU 2215 O HOH A 563 2137 1617 2705 -196 -68 765 O -HETATM 2216 O HOH A 564 23.463 14.234 -3.586 1.00 27.64 O -ANISOU 2216 O HOH A 564 3858 3156 3488 -563 -689 -919 O -HETATM 2217 O HOH A 565 50.519 43.542 3.186 1.00 10.59 O -ANISOU 2217 O HOH A 565 1406 1059 1557 -150 226 197 O -HETATM 2218 O HOH A 566 41.176 18.078 22.800 1.00 11.00 O -ANISOU 2218 O HOH A 566 1154 1242 1782 49 -68 439 O -HETATM 2219 O HOH A 567 50.137 37.387 27.918 1.00 14.39 O -ANISOU 2219 O HOH A 567 1465 1238 2762 150 -560 -658 O -HETATM 2220 O HOH A 568 32.412 8.815 9.471 1.00 18.92 O -ANISOU 2220 O HOH A 568 3167 1530 2490 -102 286 382 O -HETATM 2221 O HOH A 569 54.697 26.269 11.920 1.00 10.11 O -ANISOU 2221 O HOH A 569 1257 1203 1381 138 4 137 O -HETATM 2222 O HOH A 570 21.011 5.743 14.434 1.00 17.98 O -ANISOU 2222 O HOH A 570 2634 2355 1841 -654 -468 384 O -HETATM 2223 O HOH A 571 42.523 14.177 36.676 1.00 21.25 O -ANISOU 2223 O HOH A 571 3558 2756 1758 1250 353 559 O -HETATM 2224 O HOH A 572 44.619 35.597 17.453 1.00 15.59 O -ANISOU 2224 O HOH A 572 1747 901 3275 176 669 15 O -HETATM 2225 O HOH A 573 34.858 19.666 -3.099 1.00 19.19 O -ANISOU 2225 O HOH A 573 1744 1864 3681 -122 608 -500 O -HETATM 2226 O HOH A 574 41.914 21.004 23.799 1.00 14.88 O -ANISOU 2226 O HOH A 574 1202 3598 853 415 134 244 O -HETATM 2227 O HOH A 575 15.551 17.392 11.850 1.00 16.98 O -ANISOU 2227 O HOH A 575 1992 1850 2609 505 -49 360 O -HETATM 2228 O HOH A 576 63.838 30.155 29.191 1.00 13.60 O -ANISOU 2228 O HOH A 576 1467 1378 2323 112 -458 -17 O -HETATM 2229 O HOH A 577 58.559 24.907 18.682 1.00 13.04 O -ANISOU 2229 O HOH A 577 2065 1317 1570 281 -279 302 O -HETATM 2230 O HOH A 578 48.234 35.299 0.767 1.00 12.38 O -ANISOU 2230 O HOH A 578 1541 1502 1659 -67 73 36 O -HETATM 2231 O HOH A 579 38.917 10.599 7.947 1.00 14.83 O -ANISOU 2231 O HOH A 579 1959 1975 1699 1090 -54 37 O -HETATM 2232 O HOH A 580 38.565 32.821 0.778 1.00 20.24 O -ANISOU 2232 O HOH A 580 2210 2202 3277 47 -556 59 O -HETATM 2233 O HOH A 581 34.182 26.985 -4.302 1.00 25.09 O -ANISOU 2233 O HOH A 581 4209 2850 2472 655 522 427 O -HETATM 2234 O HOH A 582 19.844 17.925 -0.158 1.00 20.36 O -ANISOU 2234 O HOH A 582 1920 3159 2656 69 -350 -621 O -HETATM 2235 O HOH A 583 45.767 35.385 2.173 1.00 8.64 O -ANISOU 2235 O HOH A 583 1221 960 1100 -47 -1 220 O -HETATM 2236 O HOH A 584 50.558 38.912 22.088 1.00 14.41 O -ANISOU 2236 O HOH A 584 2256 1582 1634 329 125 -6 O -HETATM 2237 O HOH A 585 54.110 36.275 27.751 1.00 13.65 O -ANISOU 2237 O HOH A 585 1093 2182 1910 190 -288 -540 O -HETATM 2238 O HOH A 586 56.378 23.928 22.732 1.00 15.42 O -ANISOU 2238 O HOH A 586 1811 2038 2007 644 -58 513 O -HETATM 2239 O HOH A 587 40.913 12.345 11.835 1.00 19.22 O -ANISOU 2239 O HOH A 587 3184 1606 2510 567 174 -372 O -HETATM 2240 O HOH A 588 51.418 37.523 -6.861 1.00 20.80 O -ANISOU 2240 O HOH A 588 2960 1955 2986 -123 -924 320 O -HETATM 2241 O HOH A 589 52.668 40.646 11.267 1.00 25.28 O -ANISOU 2241 O HOH A 589 2432 1558 5615 -323 -1253 -281 O -HETATM 2242 O HOH A 590 29.085 2.121 3.477 1.00 34.85 O -ANISOU 2242 O HOH A 590 4489 4023 4727 -504 68 -610 O -HETATM 2243 O HOH A 591 39.038 31.613 7.222 1.00 11.20 O -ANISOU 2243 O HOH A 591 1262 980 2012 -137 81 130 O -HETATM 2244 O HOH A 592 35.693 8.400 6.469 1.00 16.24 O -ANISOU 2244 O HOH A 592 1834 1312 3025 108 -217 41 O -HETATM 2245 O HOH A 593 57.658 25.838 21.163 1.00 14.54 O -ANISOU 2245 O HOH A 593 1409 1770 2342 190 -242 -273 O -HETATM 2246 O HOH A 594 24.129 4.709 6.271 1.00 21.80 O -ANISOU 2246 O HOH A 594 2581 1758 3942 -439 551 -652 O -HETATM 2247 O HOH A 595 60.720 29.280 21.427 1.00 14.72 O -ANISOU 2247 O HOH A 595 2608 1301 1682 152 -609 -62 O -HETATM 2248 O HOH A 596 37.705 34.223 2.911 1.00 20.54 O -ANISOU 2248 O HOH A 596 2249 2476 3078 463 -77 750 O -HETATM 2249 O HOH A 597 58.920 33.175 -5.180 1.00 21.68 O -ANISOU 2249 O HOH A 597 2110 1639 4487 -411 236 -895 O -HETATM 2250 O HOH A 598 50.548 33.727 1.188 1.00 8.23 O -ANISOU 2250 O HOH A 598 1166 840 1119 20 36 266 O -HETATM 2251 O HOH A 599 40.630 15.011 20.904 1.00 17.50 O -ANISOU 2251 O HOH A 599 2369 2643 1636 576 -617 -183 O -HETATM 2252 O HOH A 600 25.216 35.475 13.354 1.00 17.39 O -ANISOU 2252 O HOH A 600 2807 1752 2047 -5 -643 508 O -HETATM 2253 O HOH A 601 48.564 17.177 23.417 1.00 15.79 O -ANISOU 2253 O HOH A 601 1770 1653 2576 -105 -36 -108 O -HETATM 2254 O HOH A 602 49.882 39.791 16.106 1.00 22.86 O -ANISOU 2254 O HOH A 602 3765 1389 3531 341 486 394 O -HETATM 2255 O HOH A 603 48.221 38.681 25.445 1.00 11.29 O -ANISOU 2255 O HOH A 603 1067 1030 2190 -82 -140 -173 O -HETATM 2256 O HOH A 604 21.741 20.625 -2.803 1.00 19.23 O -ANISOU 2256 O HOH A 604 2083 3302 1922 -56 -193 -513 O -HETATM 2257 O HOH A 605 63.949 36.354 18.812 1.00 14.82 O -ANISOU 2257 O HOH A 605 1212 1955 2462 -194 128 -233 O -HETATM 2258 O HOH A 606 40.519 17.316 38.462 1.00 27.41 O -ANISOU 2258 O HOH A 606 4054 4021 2336 -341 630 274 O -HETATM 2259 O HOH A 607 34.900 33.438 5.438 1.00 21.24 O -ANISOU 2259 O HOH A 607 2459 2421 3188 -418 397 -125 O -HETATM 2260 O HOH A 608 41.275 30.909 -2.808 1.00 20.87 O -ANISOU 2260 O HOH A 608 3104 2138 2687 207 -1551 538 O -HETATM 2261 O HOH A 609 28.469 33.924 8.205 1.00 24.25 O -ANISOU 2261 O HOH A 609 3091 1743 4377 630 -1106 437 O -HETATM 2262 O HOH A 610 52.526 27.199 10.436 1.00 13.00 O -ANISOU 2262 O HOH A 610 1337 1231 2368 -238 80 351 O -HETATM 2263 O HOH A 611 42.200 23.609 0.812 1.00 9.52 O -ANISOU 2263 O HOH A 611 1482 1262 874 -84 94 -187 O -HETATM 2264 O HOH A 612 27.656 9.319 12.658 1.00 15.04 O -ANISOU 2264 O HOH A 612 1796 1022 2895 148 662 188 O -HETATM 2265 O HOH A 613 18.902 24.272 9.246 1.00 16.07 O -ANISOU 2265 O HOH A 613 1228 2242 2636 509 299 -71 O -HETATM 2266 O HOH A 614 41.498 11.681 7.950 1.00 18.55 O -ANISOU 2266 O HOH A 614 2128 1894 3024 583 -438 -1198 O -HETATM 2267 O HOH A 615 22.478 28.245 23.673 1.00 20.84 O -ANISOU 2267 O HOH A 615 3327 2663 1928 1121 -38 -398 O -HETATM 2268 O HOH A 616 50.804 25.462 9.237 1.00 18.30 O -ANISOU 2268 O HOH A 616 2426 2126 2399 -233 194 2 O -HETATM 2269 O HOH A 617 45.489 42.127 25.458 1.00 20.80 O -ANISOU 2269 O HOH A 617 2381 2655 2865 545 -472 -18 O -HETATM 2270 O HOH A 618 41.148 12.471 20.013 1.00 15.50 O -ANISOU 2270 O HOH A 618 2452 1763 1673 517 -596 68 O -HETATM 2271 O HOH A 619 57.813 23.182 29.581 1.00 21.52 O -ANISOU 2271 O HOH A 619 2242 3441 2490 1224 -73 707 O -HETATM 2272 O HOH A 620 48.005 41.266 24.459 1.00 20.52 O -ANISOU 2272 O HOH A 620 2262 1977 3557 173 252 397 O -HETATM 2273 O HOH A 621 63.522 28.681 21.788 1.00 31.85 O -ANISOU 2273 O HOH A 621 4407 2681 5012 1562 34 362 O -HETATM 2274 O HOH A 622 59.384 27.350 22.636 1.00 18.47 O -ANISOU 2274 O HOH A 622 2780 2503 1733 -424 5 -84 O -HETATM 2275 O HOH A 623 49.347 37.793 17.857 1.00 12.90 O -ANISOU 2275 O HOH A 623 2254 951 1696 259 -287 -79 O -HETATM 2276 O HOH A 624 23.354 22.652 33.326 1.00 21.34 O -ANISOU 2276 O HOH A 624 2904 2246 2955 66 557 0 O -HETATM 2277 O HOH A 625 58.073 28.571 2.186 1.00 24.97 O -ANISOU 2277 O HOH A 625 3488 2372 3627 -644 1911 -600 O -HETATM 2278 O HOH A 626 27.350 30.709 0.276 1.00 20.33 O -ANISOU 2278 O HOH A 626 2596 2773 2353 116 -345 1119 O -HETATM 2279 O HOH A 627 51.412 38.126 19.580 1.00 12.82 O -ANISOU 2279 O HOH A 627 1736 1509 1625 452 -35 48 O -HETATM 2280 O AHOH A 628 45.236 31.575 33.709 0.60 15.73 O -ANISOU 2280 O AHOH A 628 2052 2147 1776 140 -192 -109 O -HETATM 2281 O BHOH A 628 46.573 32.468 33.347 0.40 15.50 O -ANISOU 2281 O BHOH A 628 1783 1954 2151 50 -36 120 O -HETATM 2282 O HOH A 629 25.636 34.399 10.900 1.00 25.32 O -ANISOU 2282 O HOH A 629 4450 3090 2078 -986 -83 -248 O -HETATM 2283 O HOH A 630 62.833 39.708 13.130 1.00 25.37 O -ANISOU 2283 O HOH A 630 2155 4479 3006 -1271 -457 723 O -HETATM 2284 O HOH A 631 31.595 6.284 8.704 1.00 20.83 O -ANISOU 2284 O HOH A 631 3294 2376 2243 -245 -318 301 O -HETATM 2285 O HOH A 632 48.053 40.062 21.879 1.00 25.67 O -ANISOU 2285 O HOH A 632 1926 3901 3925 519 -132 -616 O -HETATM 2286 O HOH A 633 45.209 12.625 21.087 1.00 18.80 O -ANISOU 2286 O HOH A 633 2410 2375 2357 -301 722 921 O -HETATM 2287 O HOH A 634 34.021 24.170 12.391 1.00 11.83 O -ANISOU 2287 O HOH A 634 1203 1698 1592 -3 -27 -233 O -HETATM 2288 O HOH A 635 41.173 42.595 22.660 1.00 13.25 O -ANISOU 2288 O HOH A 635 1962 1443 1626 77 -471 -290 O -HETATM 2289 O HOH A 636 15.796 21.601 20.036 1.00 26.90 O -ANISOU 2289 O HOH A 636 2342 3749 4129 602 560 189 O -HETATM 2290 O HOH A 637 32.596 42.014 30.052 1.00 20.53 O -ANISOU 2290 O HOH A 637 2564 2137 3098 42 431 -557 O -HETATM 2291 O HOH A 638 43.911 42.155 23.250 1.00 18.71 O -ANISOU 2291 O HOH A 638 2115 2277 2715 93 -425 -486 O -HETATM 2292 O HOH A 639 47.333 17.062 10.252 1.00 29.87 O -ANISOU 2292 O HOH A 639 4133 3585 3629 1007 -487 -506 O -HETATM 2293 O AHOH A 640 29.272 26.761 15.657 0.50 7.85 O -ANISOU 2293 O AHOH A 640 804 1105 1071 212 -86 67 O -HETATM 2294 O BHOH A 640 30.862 26.742 15.480 0.50 10.13 O -ANISOU 2294 O BHOH A 640 1636 1302 909 -94 -35 0 O -HETATM 2295 O HOH A 641 30.939 41.377 27.960 1.00 17.32 O -ANISOU 2295 O HOH A 641 2391 2306 1881 458 277 -189 O -HETATM 2296 O HOH A 642 37.258 36.211 12.221 1.00 22.48 O -ANISOU 2296 O HOH A 642 4230 2168 2143 358 406 825 O -HETATM 2297 O HOH A 643 31.171 43.189 23.268 1.00 16.97 O -ANISOU 2297 O HOH A 643 2138 1616 2694 427 255 -569 O -HETATM 2298 O HOH A 644 49.519 37.535 0.507 1.00 17.15 O -ANISOU 2298 O HOH A 644 2751 1897 1866 -508 74 -249 O -HETATM 2299 O HOH A 645 63.628 37.693 10.392 1.00 22.43 O -ANISOU 2299 O HOH A 645 1483 3436 3603 -86 474 830 O -HETATM 2300 O HOH A 646 42.725 13.444 5.559 1.00 21.59 O -ANISOU 2300 O HOH A 646 3193 2713 2294 -1075 101 -816 O -HETATM 2301 O HOH A 647 28.516 25.464 -3.798 1.00 23.97 O -ANISOU 2301 O HOH A 647 5325 2131 1650 880 569 781 O -HETATM 2302 O HOH A 648 18.203 15.182 3.312 1.00 15.79 O -ANISOU 2302 O HOH A 648 1398 1979 2620 127 122 -5 O -HETATM 2303 O HOH A 649 34.417 42.956 18.430 1.00 23.30 O -ANISOU 2303 O HOH A 649 1768 2058 5026 41 341 -723 O -HETATM 2304 O HOH A 650 44.203 13.536 10.204 1.00 22.30 O -ANISOU 2304 O HOH A 650 4165 1561 2745 596 -1025 -369 O -HETATM 2305 O HOH A 651 17.174 21.855 0.788 1.00 17.69 O -ANISOU 2305 O HOH A 651 1430 3378 1914 554 -299 229 O -HETATM 2306 O HOH A 652 47.673 33.742 -1.282 1.00 15.96 O -ANISOU 2306 O HOH A 652 2534 1792 1738 -293 379 592 O -HETATM 2307 O HOH A 653 18.650 38.285 26.150 1.00 14.48 O -ANISOU 2307 O HOH A 653 1669 1722 2108 361 -346 -311 O -HETATM 2308 O HOH A 654 44.798 34.387 33.192 1.00 19.47 O -ANISOU 2308 O HOH A 654 2605 3301 1492 1159 -69 -109 O -HETATM 2309 O HOH A 655 38.135 27.725 -3.627 1.00 26.97 O -ANISOU 2309 O HOH A 655 4067 3176 3004 637 -355 155 O -HETATM 2310 O HOH A 656 49.840 39.588 13.347 1.00 26.49 O -ANISOU 2310 O HOH A 656 3803 3237 3025 -685 1057 -227 O -HETATM 2311 O HOH A 657 26.347 32.915 6.934 1.00 20.73 O -ANISOU 2311 O HOH A 657 2432 3554 1889 -892 10 -151 O -HETATM 2312 O HOH A 658 54.753 21.452 25.809 1.00 18.87 O -ANISOU 2312 O HOH A 658 3307 1444 2416 -356 191 -451 O -HETATM 2313 O HOH A 659 20.730 29.028 12.395 1.00 24.49 O -ANISOU 2313 O HOH A 659 2237 4067 3000 638 -14 366 O -HETATM 2314 O HOH A 660 58.881 25.929 32.783 1.00 16.49 O -ANISOU 2314 O HOH A 660 1753 2025 2485 139 -423 -452 O -HETATM 2315 O HOH A 661 61.146 33.326 7.769 1.00 16.44 O -ANISOU 2315 O HOH A 661 1539 2319 2387 39 -84 296 O -HETATM 2316 O HOH A 662 56.836 38.379 27.574 1.00 21.42 O -ANISOU 2316 O HOH A 662 4080 2069 1987 891 600 -298 O -HETATM 2317 O HOH A 663 56.595 43.183 6.890 1.00 24.82 O -ANISOU 2317 O HOH A 663 3859 3356 2214 1140 141 -610 O -HETATM 2318 O HOH A 664 33.125 26.415 13.627 1.00 13.10 O -ANISOU 2318 O HOH A 664 1605 1902 1470 192 -279 -167 O -HETATM 2319 O HOH A 665 19.682 31.699 18.300 1.00 15.89 O -ANISOU 2319 O HOH A 665 1108 3049 1878 177 329 -265 O -HETATM 2320 O HOH A 666 64.236 24.813 26.283 1.00 32.00 O -ANISOU 2320 O HOH A 666 3215 3793 5148 510 -442 -1294 O -HETATM 2321 O HOH A 667 21.980 21.124 24.274 1.00 29.19 O -ANISOU 2321 O HOH A 667 2987 4556 3548 -769 844 -782 O -HETATM 2322 O HOH A 668 26.017 7.441 9.924 1.00 28.06 O -ANISOU 2322 O HOH A 668 3660 4274 2725 1276 395 618 O -HETATM 2323 O HOH A 669 30.036 26.457 13.081 1.00 16.05 O -ANISOU 2323 O HOH A 669 1972 2029 2096 -48 -205 -123 O -HETATM 2324 O AHOH A 670 22.489 32.559 21.370 0.50 24.12 O -ANISOU 2324 O AHOH A 670 2864 3234 3065 -68 35 -127 O -HETATM 2325 O BHOH A 670 22.322 34.197 20.774 0.50 27.00 O -ANISOU 2325 O BHOH A 670 3206 3709 3344 39 15 29 O -HETATM 2326 O AHOH A 671 17.607 24.331 14.881 0.50 28.87 O -ANISOU 2326 O AHOH A 671 3749 3630 3587 34 -20 21 O -HETATM 2327 O BHOH A 671 17.056 25.381 16.221 0.50 26.45 O -ANISOU 2327 O BHOH A 671 3051 3333 3665 176 -158 -455 O -HETATM 2328 O HOH A 672 64.124 25.889 23.919 1.00 33.33 O -ANISOU 2328 O HOH A 672 3352 4636 4674 -750 702 -550 O -HETATM 2329 O HOH A 673 59.251 40.295 26.609 1.00 30.10 O -ANISOU 2329 O HOH A 673 3489 3975 3972 314 -111 -345 O -HETATM 2330 O HOH A 674 58.463 40.260 23.701 1.00 27.18 O -ANISOU 2330 O HOH A 674 5807 2163 2355 312 219 -42 O -HETATM 2331 O HOH A 675 21.011 28.268 28.349 1.00 27.54 O -ANISOU 2331 O HOH A 675 2673 2968 4823 750 -95 -296 O -HETATM 2332 O HOH A 676 20.730 26.426 -0.372 1.00 27.92 O -ANISOU 2332 O HOH A 676 2406 4334 3866 1639 -162 -497 O -HETATM 2333 O HOH A 677 56.911 31.982 -2.357 1.00 28.02 O -ANISOU 2333 O HOH A 677 3186 2080 5377 17 1615 -456 O -HETATM 2334 O HOH A 678 55.340 45.362 5.976 1.00 22.41 O -ANISOU 2334 O HOH A 678 3454 2337 2721 487 -468 -244 O -HETATM 2335 O HOH A 679 59.155 31.943 9.051 1.00 14.23 O -ANISOU 2335 O HOH A 679 1406 1808 2191 191 -199 581 O -HETATM 2336 O HOH A 680 47.542 22.339 36.764 1.00 12.94 O -ANISOU 2336 O HOH A 680 2532 1368 1013 -486 -210 259 O -HETATM 2337 O HOH A 681 20.615 34.137 18.903 1.00 19.88 O -ANISOU 2337 O HOH A 681 1854 2787 2911 161 694 207 O -HETATM 2338 O HOH A 682 37.720 33.632 5.575 1.00 20.92 O -ANISOU 2338 O HOH A 682 2234 2518 3194 643 132 156 O -HETATM 2339 O HOH A 683 57.102 22.010 32.136 1.00 29.76 O -ANISOU 2339 O HOH A 683 4106 3412 3789 652 -437 1029 O -HETATM 2340 O HOH A 684 25.531 7.472 12.589 1.00 16.30 O -ANISOU 2340 O HOH A 684 2239 1742 2210 162 695 191 O -HETATM 2341 O HOH A 685 26.840 27.493 -3.381 1.00 26.93 O -ANISOU 2341 O HOH A 685 4079 3155 2996 1327 -524 748 O -HETATM 2342 O HOH A 686 47.265 25.724 38.339 1.00 38.02 O -ANISOU 2342 O HOH A 686 4618 5516 4311 -234 328 -359 O -HETATM 2343 O HOH A 687 48.345 19.414 34.684 1.00 23.50 O -ANISOU 2343 O HOH A 687 3704 2209 3016 184 -210 769 O -HETATM 2344 O HOH A 688 54.071 25.182 37.709 1.00 21.15 O -ANISOU 2344 O HOH A 688 3177 3029 1828 -962 -470 308 O -HETATM 2345 O HOH A 689 49.889 14.064 26.287 1.00 18.45 O -ANISOU 2345 O HOH A 689 2167 2390 2454 -280 -297 667 O -HETATM 2346 O HOH A 690 14.405 21.937 1.366 1.00 23.86 O -ANISOU 2346 O HOH A 690 2053 4088 2925 749 -104 -315 O -HETATM 2347 O HOH A 691 30.982 14.695 16.103 1.00 25.33 O -ANISOU 2347 O HOH A 691 3608 2517 3500 688 549 903 O -HETATM 2348 O HOH A 692 19.016 15.427 0.720 1.00 19.35 O -ANISOU 2348 O HOH A 692 2239 2787 2323 128 -282 -405 O -HETATM 2349 O HOH A 693 48.273 28.229 31.890 1.00 19.82 O -ANISOU 2349 O HOH A 693 2291 3326 1912 1202 -177 338 O -HETATM 2350 O HOH A 694 58.698 28.969 12.067 1.00 18.35 O -ANISOU 2350 O HOH A 694 1729 2798 2444 655 -226 -336 O -HETATM 2351 O HOH A 695 38.296 30.061 -2.574 1.00 27.20 O -ANISOU 2351 O HOH A 695 4115 3485 2731 214 -411 418 O -HETATM 2352 O HOH A 696 28.439 18.469 -4.005 1.00 24.19 O -ANISOU 2352 O HOH A 696 2615 3177 3397 310 -243 -1128 O -HETATM 2353 O HOH A 697 39.226 10.624 10.659 1.00 19.42 O -ANISOU 2353 O HOH A 697 2611 2357 2408 444 -477 -48 O -HETATM 2354 O HOH A 698 45.996 14.724 30.781 1.00 23.37 O -ANISOU 2354 O HOH A 698 2787 3046 3046 -287 -275 -525 O -HETATM 2355 O HOH A 699 43.794 40.190 30.677 1.00 22.71 O -ANISOU 2355 O HOH A 699 3146 3354 2129 216 -557 -1294 O -HETATM 2356 O HOH A 700 26.837 39.436 32.434 1.00 20.85 O -ANISOU 2356 O HOH A 700 2233 3387 2302 222 215 -1130 O -HETATM 2357 O HOH A 701 36.935 23.003 39.194 1.00 30.47 O -ANISOU 2357 O HOH A 701 3528 4420 3629 -28 230 460 O -HETATM 2358 O HOH A 702 49.563 20.012 16.335 1.00 24.31 O -ANISOU 2358 O HOH A 702 2268 2944 4022 -153 635 -839 O -HETATM 2359 O HOH A 703 45.680 38.737 32.268 1.00 28.30 O -ANISOU 2359 O HOH A 703 3646 4333 2771 126 -648 -975 O -HETATM 2360 O HOH A 704 24.758 27.869 -1.413 1.00 27.20 O -ANISOU 2360 O HOH A 704 4705 3513 2115 443 -665 236 O -HETATM 2361 O HOH A 705 36.976 12.371 18.083 1.00 18.84 O -ANISOU 2361 O HOH A 705 3075 2040 2040 -593 184 205 O -HETATM 2362 O HOH A 706 54.835 19.845 23.846 1.00 30.56 O -ANISOU 2362 O HOH A 706 4479 3059 4071 141 220 -1152 O -HETATM 2363 O HOH A 707 60.141 25.757 30.392 1.00 28.58 O -ANISOU 2363 O HOH A 707 4348 3629 2881 -128 116 343 O -HETATM 2364 O HOH A 708 37.908 38.702 13.871 1.00 26.16 O -ANISOU 2364 O HOH A 708 3973 3242 2722 1067 488 849 O -HETATM 2365 O HOH A 709 64.461 41.681 2.842 1.00 29.89 O -ANISOU 2365 O HOH A 709 3295 4065 3993 -124 185 829 O -HETATM 2366 O HOH A 710 27.225 32.919 4.451 1.00 25.83 O -ANISOU 2366 O HOH A 710 3858 2534 3421 -710 568 300 O -HETATM 2367 O HOH A 711 47.391 15.320 32.554 1.00 23.86 O -ANISOU 2367 O HOH A 711 2417 2505 4142 433 163 -14 O -HETATM 2368 O HOH A 712 58.586 26.092 37.492 1.00 25.83 O -ANISOU 2368 O HOH A 712 3420 2445 3948 277 -493 1137 O -HETATM 2369 O HOH A 713 19.289 21.747 -3.284 1.00 28.20 O -ANISOU 2369 O HOH A 713 2635 4833 3244 985 -574 -266 O -HETATM 2370 O HOH A 714 54.262 34.491 38.300 1.00 17.47 O -ANISOU 2370 O HOH A 714 2304 2076 2257 -300 254 -511 O -HETATM 2371 O HOH A 715 23.873 23.504 30.815 1.00 21.66 O -ANISOU 2371 O HOH A 715 2463 2957 2809 68 1129 608 O -HETATM 2372 O HOH A 716 49.305 31.884 33.285 1.00 24.04 O -ANISOU 2372 O HOH A 716 2986 3706 2441 838 -554 -104 O -HETATM 2373 O HOH A 717 55.037 21.472 21.959 1.00 29.72 O -ANISOU 2373 O HOH A 717 2899 4965 3425 -227 -415 -9 O -HETATM 2374 O HOH A 718 45.360 38.431 -0.899 1.00 28.68 O -ANISOU 2374 O HOH A 718 4495 3142 3259 -965 -24 967 O -HETATM 2375 O HOH A 719 52.996 46.711 2.634 1.00 21.45 O -ANISOU 2375 O HOH A 719 2811 3210 2129 792 -16 80 O -HETATM 2376 O HOH A 720 38.124 33.344 9.407 1.00 25.78 O -ANISOU 2376 O HOH A 720 4268 2946 2580 1744 920 151 O -HETATM 2377 O HOH A 721 38.540 17.840 -4.661 1.00 26.33 O -ANISOU 2377 O HOH A 721 3169 3221 3614 -251 1133 7 O -HETATM 2378 O HOH A 722 42.500 32.397 36.652 1.00 23.34 O -ANISOU 2378 O HOH A 722 3446 3589 1832 -750 -139 -904 O -HETATM 2379 O HOH A 723 31.666 16.565 34.423 1.00 26.59 O -ANISOU 2379 O HOH A 723 4306 2954 2841 493 -364 1163 O -HETATM 2380 O HOH A 724 59.933 18.041 6.476 1.00 19.19 O -ANISOU 2380 O HOH A 724 1196 2488 3606 262 -277 -24 O -HETATM 2381 O HOH A 725 58.583 25.029 4.963 1.00 20.68 O -ANISOU 2381 O HOH A 725 2361 2658 2835 228 -148 -441 O -HETATM 2382 O HOH A 726 28.495 16.946 26.485 1.00 25.96 O -ANISOU 2382 O HOH A 726 3749 2623 3491 -247 711 -46 O -HETATM 2383 O HOH A 727 32.421 30.060 33.667 1.00 20.06 O -ANISOU 2383 O HOH A 727 1940 2772 2906 168 856 -106 O -HETATM 2384 O HOH A 728 20.828 33.320 9.874 1.00 22.09 O -ANISOU 2384 O HOH A 728 2820 3008 2562 476 -318 181 O -HETATM 2385 O HOH A 729 34.245 32.100 0.086 1.00 23.39 O -ANISOU 2385 O HOH A 729 2499 3268 3118 -580 129 1445 O -HETATM 2386 O HOH A 730 33.020 37.179 33.039 1.00 21.61 O -ANISOU 2386 O HOH A 730 3363 3568 1279 322 4 0 O -HETATM 2387 O HOH A 731 60.541 29.003 14.312 1.00 18.50 O -ANISOU 2387 O HOH A 731 1660 2165 3203 238 311 -553 O -HETATM 2388 O HOH A 732 32.460 23.831 37.092 1.00 26.08 O -ANISOU 2388 O HOH A 732 3880 3527 2501 196 217 1237 O -HETATM 2389 O HOH A 733 30.490 34.241 6.083 1.00 22.97 O -ANISOU 2389 O HOH A 733 3601 2136 2990 782 832 220 O -HETATM 2390 O HOH A 734 63.621 40.064 20.176 1.00 27.38 O -ANISOU 2390 O HOH A 734 2469 3791 4141 -780 -410 900 O -HETATM 2391 O HOH A 735 29.836 32.254 35.655 1.00 22.35 O -ANISOU 2391 O HOH A 735 2293 2987 3212 324 -265 -413 O -HETATM 2392 O HOH A 736 33.922 13.330 14.307 1.00 22.64 O -ANISOU 2392 O HOH A 736 3286 3733 1581 -1243 -562 498 O -HETATM 2393 O HOH A 737 34.985 40.551 14.546 1.00 25.02 O -ANISOU 2393 O HOH A 737 3942 2365 3199 -278 -430 520 O -HETATM 2394 O HOH A 738 62.133 41.163 6.507 1.00 24.79 O -ANISOU 2394 O HOH A 738 2458 3782 3177 -653 -91 -709 O -HETATM 2395 O HOH A 739 59.202 30.715 1.121 1.00 18.06 O -ANISOU 2395 O HOH A 739 3086 1484 2289 -547 772 -308 O -HETATM 2396 O HOH A 740 35.784 15.348 30.002 1.00 26.35 O -ANISOU 2396 O HOH A 740 2854 2914 4241 -199 -110 121 O -HETATM 2397 O HOH A 741 53.234 28.474 1.913 1.00 23.22 O -ANISOU 2397 O HOH A 741 2725 2848 3249 -161 -71 71 O -HETATM 2398 O HOH A 742 49.988 33.364 -2.490 1.00 22.74 O -ANISOU 2398 O HOH A 742 2626 2631 3380 -22 367 1317 O -HETATM 2399 O HOH A 743 64.277 40.090 28.362 1.00 38.47 O -ANISOU 2399 O HOH A 743 4745 5198 4672 656 -17 -292 O -HETATM 2400 O HOH A 744 61.877 24.361 7.126 1.00 25.07 O -ANISOU 2400 O HOH A 744 2549 3194 3781 229 -355 -119 O -HETATM 2401 O HOH A 745 28.303 6.259 9.425 1.00 26.35 O -ANISOU 2401 O HOH A 745 2709 3848 3452 -181 275 -401 O -HETATM 2402 O HOH A 746 58.978 20.406 5.604 1.00 26.85 O -ANISOU 2402 O HOH A 746 3295 3615 3291 1028 631 825 O -HETATM 2403 O HOH A 747 49.984 34.014 -4.951 1.00 29.85 O -ANISOU 2403 O HOH A 747 3932 3839 3567 -760 -502 -28 O -HETATM 2404 O HOH A 748 41.775 37.609 0.853 1.00 34.36 O -ANISOU 2404 O HOH A 748 4683 4621 3750 813 -409 668 O -HETATM 2405 O HOH A 749 38.992 36.785 2.816 1.00 26.32 O -ANISOU 2405 O HOH A 749 2609 3109 4281 549 -584 451 O -HETATM 2406 O HOH A 750 41.695 21.224 -9.506 1.00 38.45 O -ANISOU 2406 O HOH A 750 5396 4987 4223 316 200 -928 O -HETATM 2407 O HOH A 751 24.250 12.874 16.797 1.00 23.01 O -ANISOU 2407 O HOH A 751 2669 2423 3648 400 -19 -584 O -HETATM 2408 O HOH A 752 47.586 30.232 33.423 1.00 25.93 O -ANISOU 2408 O HOH A 752 3504 3591 2754 497 -406 -269 O -HETATM 2409 O HOH A 753 60.099 29.568 9.777 1.00 24.60 O -ANISOU 2409 O HOH A 753 2977 2412 3958 693 -301 427 O -HETATM 2410 O HOH A 754 41.697 38.757 34.454 1.00 41.89 O -ANISOU 2410 O HOH A 754 5361 5257 5296 -104 655 -711 O -HETATM 2411 O HOH A 755 41.570 15.861 -2.620 1.00 27.88 O -ANISOU 2411 O HOH A 755 2241 3712 4639 -1020 573 244 O -HETATM 2412 O HOH A 756 27.937 16.046 -3.675 1.00 23.25 O -ANISOU 2412 O HOH A 756 2761 3054 3018 6 197 205 O -HETATM 2413 O HOH A 757 47.465 15.826 29.506 1.00 28.78 O -ANISOU 2413 O HOH A 757 3952 4098 2886 304 -602 -839 O -HETATM 2414 O HOH A 758 64.843 32.255 13.653 1.00 23.52 O -ANISOU 2414 O HOH A 758 2579 3156 3198 356 -1106 23 O -HETATM 2415 O HOH A 759 26.298 37.957 13.702 1.00 26.20 O -ANISOU 2415 O HOH A 759 3530 2380 4042 229 -472 365 O -HETATM 2416 O HOH A 760 17.857 19.682 -0.805 1.00 22.77 O -ANISOU 2416 O HOH A 760 2111 3859 2681 576 -431 -377 O -HETATM 2417 O HOH A 761 37.368 34.762 40.781 1.00 30.12 O -ANISOU 2417 O HOH A 761 4330 4227 2887 -282 -269 -920 O -HETATM 2418 O HOH A 762 23.338 20.995 -5.087 1.00 24.46 O -ANISOU 2418 O HOH A 762 3074 4347 1871 -268 1 -503 O -HETATM 2419 O HOH A 763 59.940 22.806 8.188 1.00 34.80 O -ANISOU 2419 O HOH A 763 3524 4876 4822 402 453 41 O -HETATM 2420 O HOH A 764 16.578 9.815 11.847 1.00 24.93 O -ANISOU 2420 O HOH A 764 3025 2180 4265 -584 -112 -708 O -HETATM 2421 O HOH A 765 22.263 34.136 16.218 1.00 34.15 O -ANISOU 2421 O HOH A 765 3898 3731 5344 572 159 232 O -HETATM 2422 O HOH A 766 25.845 21.397 -5.032 1.00 25.14 O -ANISOU 2422 O HOH A 766 3488 3577 2484 -769 -263 -612 O -HETATM 2423 O HOH A 767 55.518 29.857 38.995 1.00 22.35 O -ANISOU 2423 O HOH A 767 4065 2527 1899 -239 286 -261 O -HETATM 2424 O HOH A 768 27.125 19.316 -6.141 1.00 35.97 O -ANISOU 2424 O HOH A 768 4999 4444 4221 363 -374 -291 O -HETATM 2425 O HOH A 769 43.947 36.357 0.365 1.00 20.93 O -ANISOU 2425 O HOH A 769 3374 1632 2945 17 -974 668 O -HETATM 2426 O HOH A 770 38.154 20.936 -5.053 1.00 26.89 O -ANISOU 2426 O HOH A 770 3498 3394 3324 545 -480 -1694 O -HETATM 2427 O HOH A 771 60.218 43.344 13.167 1.00 30.43 O -ANISOU 2427 O HOH A 771 5576 2192 3793 -1437 -125 -275 O -HETATM 2428 O HOH A 772 45.477 20.873 -4.141 1.00 21.11 O -ANISOU 2428 O HOH A 772 2458 3277 2285 -398 681 -498 O -HETATM 2429 O HOH A 773 62.422 34.677 4.288 1.00 29.88 O -ANISOU 2429 O HOH A 773 3690 2868 4793 1341 -480 777 O -HETATM 2430 O HOH A 774 52.336 33.986 -5.563 1.00 32.42 O -ANISOU 2430 O HOH A 774 3555 4586 4176 -1359 -194 -231 O -HETATM 2431 O HOH A 775 59.494 38.909 31.323 1.00 26.99 O -ANISOU 2431 O HOH A 775 4264 2791 3198 -1135 -491 -1034 O -HETATM 2432 O HOH A 776 62.379 43.859 6.063 1.00 30.21 O -ANISOU 2432 O HOH A 776 4384 3231 3862 -222 -50 -18 O -HETATM 2433 O HOH A 777 46.353 15.691 17.755 1.00 18.73 O -ANISOU 2433 O HOH A 777 2507 2409 2201 562 311 684 O -HETATM 2434 O HOH A 778 27.416 41.759 31.248 1.00 36.13 O -ANISOU 2434 O HOH A 778 4376 4295 5057 -22 561 -243 O -HETATM 2435 O HOH A 779 55.453 41.674 8.977 1.00 24.32 O -ANISOU 2435 O HOH A 779 3591 2805 2842 469 25 318 O -HETATM 2436 O HOH A 780 21.548 24.154 29.857 1.00 26.95 O -ANISOU 2436 O HOH A 780 2273 3590 4374 526 882 -15 O -HETATM 2437 O HOH A 781 14.920 22.599 4.023 1.00 27.82 O -ANISOU 2437 O HOH A 781 3847 3745 2976 243 526 -242 O -HETATM 2438 O HOH A 782 54.557 35.293 -5.132 1.00 19.21 O -ANISOU 2438 O HOH A 782 1895 1667 3735 -213 -263 473 O -HETATM 2439 O HOH A 783 58.999 24.803 9.380 1.00 28.21 O -ANISOU 2439 O HOH A 783 4007 2443 4266 550 -638 -238 O -HETATM 2440 O HOH A 784 25.594 13.965 -0.956 1.00 25.95 O -ANISOU 2440 O HOH A 784 1698 3252 4909 483 622 1204 O -HETATM 2441 O HOH A 785 33.130 39.873 12.905 1.00 22.30 O -ANISOU 2441 O HOH A 785 3590 1937 2944 195 -338 651 O -HETATM 2442 O HOH A 786 46.508 23.982 35.592 1.00 26.51 O -ANISOU 2442 O HOH A 786 3775 3583 2712 656 -898 -990 O -HETATM 2443 O HOH A 787 20.015 10.033 18.784 1.00 41.97 O -ANISOU 2443 O HOH A 787 5863 4711 5373 679 -36 -143 O -HETATM 2444 O HOH A 788 65.337 35.582 11.445 1.00 28.47 O -ANISOU 2444 O HOH A 788 3130 3354 4333 371 178 -368 O -HETATM 2445 O HOH A 789 50.773 33.884 32.528 1.00 28.90 O -ANISOU 2445 O HOH A 789 3185 4185 3608 -1111 -444 -391 O -HETATM 2446 O HOH A 790 18.963 26.917 9.798 1.00 32.93 O -ANISOU 2446 O HOH A 790 3395 3554 5562 814 541 335 O -HETATM 2447 O HOH A 791 21.360 17.947 -2.683 1.00 26.31 O -ANISOU 2447 O HOH A 791 2364 3228 4405 -328 -651 -383 O -HETATM 2448 O HOH A 792 52.149 18.829 -2.280 1.00 29.50 O -ANISOU 2448 O HOH A 792 2746 4730 3731 202 1389 -307 O -HETATM 2449 O HOH A 793 23.201 13.758 34.548 1.00 24.88 O -ANISOU 2449 O HOH A 793 3592 2048 3814 -84 99 1005 O -HETATM 2450 O HOH A 794 31.074 18.446 -5.872 1.00 30.82 O -ANISOU 2450 O HOH A 794 5207 3179 3321 -36 812 -979 O -HETATM 2451 O HOH A 795 49.393 18.881 21.559 1.00 18.08 O -ANISOU 2451 O HOH A 795 2369 1917 2581 541 -120 251 O -HETATM 2452 O HOH A 796 26.158 19.330 23.125 1.00 33.65 O -ANISOU 2452 O HOH A 796 3516 4414 4855 217 -433 600 O -HETATM 2453 O HOH A 797 62.432 40.346 30.679 1.00 32.32 O -ANISOU 2453 O HOH A 797 4578 4205 3496 -145 448 221 O -HETATM 2454 O HOH A 798 53.254 34.203 32.637 1.00 22.99 O -ANISOU 2454 O HOH A 798 3098 2604 3031 198 344 403 O -HETATM 2455 O HOH A 799 51.351 35.238 30.262 1.00 33.31 O -ANISOU 2455 O HOH A 799 4151 4418 4086 -105 -866 -53 O -HETATM 2456 O HOH A 800 31.692 27.292 -3.136 1.00 25.93 O -ANISOU 2456 O HOH A 800 3405 3975 2472 643 194 151 O -HETATM 2457 O HOH A 801 65.919 38.064 19.933 1.00 31.34 O -ANISOU 2457 O HOH A 801 3911 4144 3851 -588 415 183 O -HETATM 2458 O HOH A 802 61.282 36.991 33.536 1.00 23.19 O -ANISOU 2458 O HOH A 802 3605 1922 3283 -627 1339 -824 O -HETATM 2459 O HOH A 803 21.001 31.596 15.983 1.00 20.96 O -ANISOU 2459 O HOH A 803 2632 3092 2239 1187 409 199 O -HETATM 2460 O HOH A 804 64.967 25.793 28.766 1.00 30.03 O -ANISOU 2460 O HOH A 804 3863 2703 4841 815 131 -62 O -HETATM 2461 O HOH A 805 17.424 9.605 19.297 1.00 25.75 O -ANISOU 2461 O HOH A 805 3891 2298 3593 621 1073 877 O -HETATM 2462 O HOH A 806 48.537 17.723 19.154 1.00 23.78 O -ANISOU 2462 O HOH A 806 2715 3713 2606 1132 -412 -820 O -HETATM 2463 O HOH A 807 59.005 26.367 2.642 1.00 39.96 O -ANISOU 2463 O HOH A 807 5168 4982 5030 -110 321 -204 O -HETATM 2464 O HOH A 808 52.418 20.423 16.445 1.00 23.36 O -ANISOU 2464 O HOH A 808 3348 2623 2902 -1288 -35 747 O -HETATM 2465 O HOH A 809 20.134 7.864 1.883 1.00 26.32 O -ANISOU 2465 O HOH A 809 3086 3962 2952 -491 -293 -659 O -HETATM 2466 O HOH A 810 28.793 20.057 23.248 1.00 32.70 O -ANISOU 2466 O HOH A 810 3819 3628 4978 -524 -669 489 O -HETATM 2467 O HOH A 811 28.109 41.722 28.785 1.00 28.51 O -ANISOU 2467 O HOH A 811 3294 4012 3524 855 413 -14 O -HETATM 2468 O HOH A 812 31.020 19.916 20.859 1.00 36.96 O -ANISOU 2468 O HOH A 812 4566 4222 5256 1410 -656 -470 O -HETATM 2469 O HOH A 813 21.519 21.315 29.052 1.00 27.49 O -ANISOU 2469 O HOH A 813 3156 3773 3516 -470 612 718 O -HETATM 2470 O HOH A 814 44.894 41.335 18.827 1.00 33.89 O -ANISOU 2470 O HOH A 814 3335 3886 5654 -541 70 178 O -HETATM 2471 O HOH A 815 45.670 26.252 -6.949 1.00 22.80 O -ANISOU 2471 O HOH A 815 2860 3961 1840 -887 55 222 O -HETATM 2472 O HOH A 816 16.906 8.287 9.104 1.00 35.60 O -ANISOU 2472 O HOH A 816 4527 4423 4575 362 -153 656 O -HETATM 2473 O HOH A 817 35.986 13.870 22.222 1.00 26.67 O -ANISOU 2473 O HOH A 817 4796 2662 2674 -564 216 698 O -HETATM 2474 O HOH A 818 63.923 29.068 14.798 1.00 31.22 O -ANISOU 2474 O HOH A 818 2874 4678 4308 654 559 -401 O -HETATM 2475 O HOH A 819 36.873 31.027 -0.212 1.00 24.08 O -ANISOU 2475 O HOH A 819 2722 3362 3063 -238 77 415 O -HETATM 2476 O HOH A 820 20.505 38.443 32.190 1.00 27.61 O -ANISOU 2476 O HOH A 820 3055 4489 2946 -179 1034 -1047 O -HETATM 2477 O HOH A 821 34.477 15.686 25.096 1.00 29.24 O -ANISOU 2477 O HOH A 821 3201 3923 3983 -1079 807 -222 O -HETATM 2478 O HOH A 822 44.201 19.755 -7.901 1.00 37.51 O -ANISOU 2478 O HOH A 822 5005 5604 3643 463 769 -45 O -HETATM 2479 O HOH A 823 20.024 31.300 6.044 1.00 25.36 O -ANISOU 2479 O HOH A 823 3857 2397 3380 714 -406 522 O -HETATM 2480 O HOH A 824 48.826 15.244 21.599 1.00 22.90 O -ANISOU 2480 O HOH A 824 3170 2908 2620 -520 -462 390 O -HETATM 2481 O HOH A 825 49.658 30.259 -6.068 1.00 37.11 O -ANISOU 2481 O HOH A 825 5209 5251 3637 -29 754 -37 O -HETATM 2482 O HOH A 826 57.991 22.973 24.726 1.00 26.70 O -ANISOU 2482 O HOH A 826 3394 3333 3417 854 -478 421 O -HETATM 2483 O HOH A 827 40.724 39.955 14.855 1.00 40.96 O -ANISOU 2483 O HOH A 827 5645 4924 4993 -330 171 -541 O -HETATM 2484 O HOH A 828 62.630 25.316 30.111 1.00 24.66 O -ANISOU 2484 O HOH A 828 2997 2745 3625 922 13 532 O -HETATM 2485 O HOH A 829 47.103 13.915 14.401 1.00 40.71 O -ANISOU 2485 O HOH A 829 5663 4305 5497 838 70 -112 O -HETATM 2486 O HOH A 830 45.268 37.884 16.123 1.00 25.94 O -ANISOU 2486 O HOH A 830 3091 2755 4007 56 841 -949 O -HETATM 2487 O HOH A 831 26.239 6.866 18.139 1.00 30.27 O -ANISOU 2487 O HOH A 831 2759 3670 5069 908 -1195 573 O -HETATM 2488 O HOH A 832 46.910 38.721 18.628 1.00 25.42 O -ANISOU 2488 O HOH A 832 2606 3646 3406 982 26 -60 O -HETATM 2489 O HOH A 833 25.857 18.066 25.503 1.00 33.70 O -ANISOU 2489 O HOH A 833 4407 3467 4928 382 -323 -478 O -HETATM 2490 O HOH A 834 51.352 17.788 11.298 1.00 35.60 O -ANISOU 2490 O HOH A 834 4642 3142 5740 234 -305 -100 O -HETATM 2491 O HOH A 835 49.381 31.327 35.941 1.00 27.09 O -ANISOU 2491 O HOH A 835 3021 3836 3434 627 364 -234 O -HETATM 2492 O HOH A 836 28.150 41.870 16.398 1.00 34.16 O -ANISOU 2492 O HOH A 836 4108 4209 4662 1194 -480 97 O -HETATM 2493 O HOH A 837 51.974 39.505 25.605 1.00 25.81 O -ANISOU 2493 O HOH A 837 2857 2183 4764 -625 -593 -668 O -HETATM 2494 O HOH A 838 46.969 16.138 34.627 1.00 25.00 O -ANISOU 2494 O HOH A 838 3596 2511 3390 362 -1316 1102 O -HETATM 2495 O HOH A 839 21.987 33.554 7.266 1.00 39.39 O -ANISOU 2495 O HOH A 839 4169 5490 5307 617 -247 370 O -HETATM 2496 O HOH A 840 43.889 38.842 18.208 1.00 29.39 O -ANISOU 2496 O HOH A 840 3748 3548 3871 257 427 -336 O -HETATM 2497 O HOH A 841 34.373 16.053 33.974 1.00 35.62 O -ANISOU 2497 O HOH A 841 5245 3845 4441 -21 -4 394 O -HETATM 2498 O HOH A 842 48.793 18.610 30.765 1.00 30.28 O -ANISOU 2498 O HOH A 842 3246 2973 5284 1130 520 363 O -HETATM 2499 O HOH A 843 27.461 15.845 17.861 1.00 33.03 O -ANISOU 2499 O HOH A 843 2652 5263 4633 -417 760 388 O -HETATM 2500 O HOH A 844 41.380 40.044 3.233 1.00 29.73 O -ANISOU 2500 O HOH A 844 4032 2064 5200 277 198 687 O -HETATM 2501 O HOH A 845 27.731 17.982 19.359 1.00 33.06 O -ANISOU 2501 O HOH A 845 4186 3495 4878 -374 385 681 O -HETATM 2502 O HOH A 846 62.703 30.021 10.049 1.00 31.50 O -ANISOU 2502 O HOH A 846 3554 3822 4589 557 -111 548 O -HETATM 2503 O HOH A 847 12.842 17.151 17.507 1.00 30.10 O -ANISOU 2503 O HOH A 847 3731 3011 4694 211 837 661 O -HETATM 2504 O HOH A 848 45.454 34.322 -2.775 1.00 42.79 O -ANISOU 2504 O HOH A 848 5987 5171 5100 236 -642 548 O -HETATM 2505 O HOH A 849 43.238 34.570 35.389 1.00 26.06 O -ANISOU 2505 O HOH A 849 4637 3636 1626 238 568 -154 O -HETATM 2506 O HOH A 850 45.989 33.376 -5.452 1.00 33.11 O -ANISOU 2506 O HOH A 850 5104 3803 3673 -214 -513 554 O -HETATM 2507 O HOH A 851 60.455 24.303 26.231 1.00 39.74 O -ANISOU 2507 O HOH A 851 5295 5119 4683 306 1082 -298 O -HETATM 2508 O HOH A 852 26.787 23.920 -5.852 1.00 31.28 O -ANISOU 2508 O HOH A 852 4248 4900 2737 112 -749 538 O -HETATM 2509 O HOH A 853 14.508 16.804 19.716 1.00 31.73 O -ANISOU 2509 O HOH A 853 2644 4589 4822 122 811 26 O -HETATM 2510 O HOH A 854 19.794 24.659 3.056 1.00 25.16 O -ANISOU 2510 O HOH A 854 3778 3440 2339 1842 -258 251 O -HETATM 2511 O HOH A 855 55.539 22.621 34.276 1.00 35.67 O -ANISOU 2511 O HOH A 855 3947 4275 5330 134 136 585 O -HETATM 2512 O HOH A 856 16.229 24.906 19.318 1.00 25.20 O -ANISOU 2512 O HOH A 856 2371 2992 4212 -65 315 -51 O -HETATM 2513 O HOH A 857 41.687 41.486 9.570 1.00 33.44 O -ANISOU 2513 O HOH A 857 4040 4330 4335 309 146 -300 O -HETATM 2514 O HOH A 858 34.967 34.172 2.476 1.00 32.57 O -ANISOU 2514 O HOH A 858 3283 3890 5202 638 -55 306 O -HETATM 2515 O HOH A 859 47.335 18.546 36.809 1.00 31.62 O -ANISOU 2515 O HOH A 859 4767 3242 4004 -1190 -468 647 O -HETATM 2516 O HOH A 860 47.272 12.870 -4.358 1.00 32.05 O -ANISOU 2516 O HOH A 860 4314 3574 4286 -252 -48 -566 O -HETATM 2517 O HOH A 861 16.209 22.897 16.373 1.00 35.79 O -ANISOU 2517 O HOH A 861 4252 4717 4626 1039 -607 324 O -HETATM 2518 O HOH A 862 14.383 19.505 20.829 1.00 36.49 O -ANISOU 2518 O HOH A 862 3931 4975 4955 393 -238 328 O -HETATM 2519 O HOH A 863 53.101 42.660 9.543 1.00 32.89 O -ANISOU 2519 O HOH A 863 4609 3868 4018 -140 -797 -143 O -HETATM 2520 O HOH A 864 61.517 25.695 23.135 1.00 27.99 O -ANISOU 2520 O HOH A 864 3264 2963 4406 1026 228 525 O -HETATM 2521 O HOH A 865 60.327 45.390 7.934 1.00 33.57 O -ANISOU 2521 O HOH A 865 5364 3449 3940 -75 347 -113 O -HETATM 2522 O HOH A 866 34.326 14.261 31.905 1.00 29.34 O -ANISOU 2522 O HOH A 866 4414 3301 3431 -455 664 -313 O -HETATM 2523 O HOH A 867 58.352 21.651 16.170 1.00 27.42 O -ANISOU 2523 O HOH A 867 3257 2686 4476 1094 -364 1122 O -HETATM 2524 O HOH A 868 62.356 24.280 4.300 1.00 32.55 O -ANISOU 2524 O HOH A 868 5012 3155 4199 378 -1024 988 O -HETATM 2525 O HOH A 869 24.129 10.187 19.250 1.00 31.89 O -ANISOU 2525 O HOH A 869 4946 3617 3553 -414 118 -575 O -HETATM 2526 O HOH A 870 51.076 29.992 38.005 1.00 34.67 O -ANISOU 2526 O HOH A 870 5448 4982 2743 -476 281 44 O -HETATM 2527 O HOH A 871 49.426 17.465 15.933 1.00 28.04 O -ANISOU 2527 O HOH A 871 2724 3103 4824 718 -547 -738 O -HETATM 2528 O HOH A 872 18.497 6.758 15.373 1.00 28.56 O -ANISOU 2528 O HOH A 872 2898 5100 2852 386 35 1430 O -HETATM 2529 O HOH A 873 55.429 17.042 6.573 1.00 34.56 O -ANISOU 2529 O HOH A 873 3396 4408 5325 329 225 -369 O -HETATM 2530 O HOH A 874 56.254 18.677 4.649 1.00 33.06 O -ANISOU 2530 O HOH A 874 3356 4188 5014 1085 299 96 O -HETATM 2531 O HOH A 875 49.554 36.520 -5.512 1.00 27.45 O -ANISOU 2531 O HOH A 875 3736 3497 3194 -712 -843 -124 O -HETATM 2532 O HOH A 876 17.920 24.176 -0.695 1.00 31.11 O -ANISOU 2532 O HOH A 876 3250 3976 4594 840 -829 549 O -HETATM 2533 O HOH A 877 24.354 25.427 -6.384 1.00 43.39 O -ANISOU 2533 O HOH A 877 5589 5509 5387 -105 -727 254 O -HETATM 2534 O HOH A 878 52.519 17.951 24.013 1.00 32.40 O -ANISOU 2534 O HOH A 878 3657 4147 4506 1241 498 -597 O -HETATM 2535 O HOH A 879 19.047 8.612 11.709 1.00 24.64 O -ANISOU 2535 O HOH A 879 2626 3854 2882 -143 -150 -295 O -HETATM 2536 O HOH A 880 56.904 21.231 13.856 1.00 30.00 O -ANISOU 2536 O HOH A 880 3342 4037 4019 -85 -108 -725 O -HETATM 2537 O HOH A 881 18.235 32.211 35.680 1.00 23.35 O -ANISOU 2537 O HOH A 881 2562 4320 1987 49 244 612 O -HETATM 2538 O HOH A 882 22.809 30.093 1.696 1.00 33.80 O -ANISOU 2538 O HOH A 882 4560 4232 4049 920 -266 637 O -HETATM 2539 O HOH A 883 36.933 10.212 16.059 1.00 29.57 O -ANISOU 2539 O HOH A 883 3372 4252 3609 -121 -378 -106 O -HETATM 2540 O HOH A 884 25.651 42.711 22.635 1.00 37.92 O -ANISOU 2540 O HOH A 884 4839 4574 4995 542 72 -195 O -HETATM 2541 O HOH A 885 46.357 13.692 -6.648 1.00 38.13 O -ANISOU 2541 O HOH A 885 5358 3862 5266 -621 -122 -120 O -HETATM 2542 O HOH A 886 49.183 18.237 13.042 1.00 24.98 O -ANISOU 2542 O HOH A 886 1768 2784 4938 167 434 1420 O -HETATM 2543 O HOH A 887 28.676 43.823 22.300 1.00 26.84 O -ANISOU 2543 O HOH A 887 3683 2746 3768 321 -1180 -1091 O -HETATM 2544 O HOH A 888 62.831 22.797 11.174 1.00 27.99 O -ANISOU 2544 O HOH A 888 1805 4585 4243 769 474 22 O -HETATM 2545 O HOH A 889 44.193 26.545 6.340 1.00 5.93 O -ANISOU 2545 O HOH A 889 666 941 646 -142 33 36 O -HETATM 2546 O HOH A 890 21.864 25.437 17.622 1.00 24.67 O -ANISOU 2546 O HOH A 890 2661 3312 3401 398 -568 16 O -HETATM 2547 O HOH A 891 21.611 23.620 35.078 1.00 35.52 O -ANISOU 2547 O HOH A 891 4791 4165 4537 -114 409 110 O -HETATM 2548 O HOH A 892 51.935 41.819 16.302 1.00 34.17 O -ANISOU 2548 O HOH A 892 4514 4145 4323 1068 -1121 -175 O -HETATM 2549 O HOH A 893 20.950 24.229 21.657 1.00 33.03 O -ANISOU 2549 O HOH A 893 3689 4370 4489 -919 -420 891 O -HETATM 2550 O HOH A 894 24.389 39.038 33.754 1.00 28.67 O -ANISOU 2550 O HOH A 894 3487 3540 3865 203 882 -1170 O -HETATM 2551 O HOH A 895 52.757 25.219 8.099 1.00 24.63 O -ANISOU 2551 O HOH A 895 3420 3874 2063 1996 146 -15 O -HETATM 2552 O HOH A 896 43.112 34.532 -1.430 1.00 42.44 O -ANISOU 2552 O HOH A 896 5566 4902 5654 192 -442 -70 O -HETATM 2553 O HOH A 897 29.061 31.867 2.923 1.00 30.18 O -ANISOU 2553 O HOH A 897 4273 3606 3587 349 -38 -273 O -HETATM 2554 O HOH A 898 21.305 28.395 3.121 1.00 28.52 O -ANISOU 2554 O HOH A 898 3783 4094 2958 636 284 -722 O -HETATM 2555 O HOH A 899 19.588 8.209 8.948 1.00 25.26 O -ANISOU 2555 O HOH A 899 3871 2953 2772 -165 104 -519 O -HETATM 2556 O HOH A 900 54.049 38.881 27.406 1.00 31.41 O -ANISOU 2556 O HOH A 900 3335 3551 5047 783 -238 -225 O -HETATM 2557 O HOH A 901 31.641 29.920 -1.844 1.00 28.57 O -ANISOU 2557 O HOH A 901 4425 4278 2149 -423 -221 -219 O -HETATM 2558 O HOH A 902 18.801 32.151 8.325 1.00 26.95 O -ANISOU 2558 O HOH A 902 2537 3836 3865 564 -162 59 O -HETATM 2559 O HOH A 903 58.374 22.128 18.693 1.00 26.58 O -ANISOU 2559 O HOH A 903 2973 2095 5031 493 -180 -205 O -HETATM 2560 O HOH A 904 51.967 17.265 29.271 1.00 33.39 O -ANISOU 2560 O HOH A 904 4673 4475 3539 -48 -441 618 O -HETATM 2561 O HOH A 905 31.789 12.647 32.154 1.00 30.15 O -ANISOU 2561 O HOH A 905 4420 3110 3925 -66 -633 -648 O -HETATM 2562 O HOH A 906 20.589 5.842 8.379 1.00 33.01 O -ANISOU 2562 O HOH A 906 4352 4095 4093 138 680 -272 O -HETATM 2563 O HOH A 907 22.153 17.902 22.163 1.00 30.75 O -ANISOU 2563 O HOH A 907 4304 3313 4065 -908 274 977 O -HETATM 2564 O HOH A 908 64.343 27.572 29.981 1.00 24.21 O -ANISOU 2564 O HOH A 908 3270 3120 2807 382 272 29 O -HETATM 2565 O HOH A 909 62.763 42.734 12.602 1.00 35.42 O -ANISOU 2565 O HOH A 909 4667 4331 4460 -669 -376 -635 O -HETATM 2566 O HOH A 910 58.712 44.835 16.217 1.00 39.96 O -ANISOU 2566 O HOH A 910 5745 4577 4860 -423 334 544 O -HETATM 2567 O HOH A 911 58.595 15.841 4.732 1.00 36.90 O -ANISOU 2567 O HOH A 911 4125 4941 4954 68 -183 -414 O -HETATM 2568 O HOH A 912 59.823 15.896 9.545 1.00 26.64 O -ANISOU 2568 O HOH A 912 4265 2926 2930 1719 746 -308 O -HETATM 2569 O HOH A 913 32.571 31.455 35.964 1.00 20.77 O -ANISOU 2569 O HOH A 913 2227 2848 2815 48 -336 274 O -HETATM 2570 O HOH A 914 32.282 20.774 18.922 1.00 23.77 O -ANISOU 2570 O HOH A 914 2559 3057 3412 -25 283 -23 O -HETATM 2571 O HOH A 915 41.522 22.667 35.995 1.00 28.37 O -ANISOU 2571 O HOH A 915 5459 3369 1951 1133 -119 578 O -HETATM 2572 O HOH A 916 21.366 5.375 5.849 1.00 27.01 O -ANISOU 2572 O HOH A 916 2475 3086 4700 -433 329 -810 O -HETATM 2573 O HOH A 917 56.894 23.833 37.535 1.00 42.79 O -ANISOU 2573 O HOH A 917 4976 5436 5844 34 -285 277 O -HETATM 2574 O HOH A 918 34.739 37.534 35.019 1.00 29.85 O -ANISOU 2574 O HOH A 918 4093 4274 2974 336 -840 -62 O -HETATM 2575 O HOH A 919 58.024 44.777 8.833 1.00 28.59 O -ANISOU 2575 O HOH A 919 3986 2944 3930 -164 -202 -240 O -HETATM 2576 O HOH A 920 25.504 16.006 14.921 1.00 19.07 O -ANISOU 2576 O HOH A 920 2547 2576 2123 -253 921 -128 O -HETATM 2577 O HOH A 921 64.972 35.188 13.990 1.00 26.90 O -ANISOU 2577 O HOH A 921 2186 4712 3322 -603 -368 -81 O -HETATM 2578 O HOH A 922 30.071 31.308 -0.884 1.00 32.80 O -ANISOU 2578 O HOH A 922 4562 4329 3569 450 -684 744 O -HETATM 2579 O HOH A 923 43.597 32.412 -5.696 1.00 38.82 O -ANISOU 2579 O HOH A 923 5240 4972 4536 -226 129 108 O -HETATM 2580 O HOH A 924 22.877 29.472 16.051 1.00 11.50 O -ANISOU 2580 O HOH A 924 1417 1176 1775 184 266 123 O -HETATM 2581 O HOH A 925 46.878 42.398 4.075 1.00 12.95 O -ANISOU 2581 O HOH A 925 1565 1299 2057 299 646 611 O -HETATM 2582 O HOH A 926 28.569 15.981 15.071 1.00 14.91 O -ANISOU 2582 O HOH A 926 1894 1684 2085 -179 193 120 O -HETATM 2583 O HOH A 927 40.282 23.184 20.626 1.00 13.91 O -ANISOU 2583 O HOH A 927 1852 1536 1896 -41 316 -70 O -HETATM 2584 O HOH A 928 29.397 8.068 10.931 1.00 27.00 O -ANISOU 2584 O HOH A 928 4479 2257 3521 477 813 -54 O -HETATM 2585 O HOH A 929 51.081 20.409 31.746 1.00 15.73 O -ANISOU 2585 O HOH A 929 2336 1210 2429 310 195 84 O -HETATM 2586 O HOH A 930 51.266 24.482 -2.961 1.00 28.66 O -ANISOU 2586 O HOH A 930 4579 2830 3479 522 114 -1017 O -HETATM 2587 O HOH A 931 59.120 46.278 3.983 1.00 23.56 O -ANISOU 2587 O HOH A 931 2922 2714 3315 -696 -897 1282 O -HETATM 2588 O HOH A 932 25.251 40.332 26.256 1.00 32.79 O -ANISOU 2588 O HOH A 932 3700 4729 4028 374 446 -53 O -HETATM 2589 O HOH A 933 48.001 38.515 -1.583 1.00 25.06 O -ANISOU 2589 O HOH A 933 3325 3087 3108 -1390 -551 -365 O -HETATM 2590 O HOH A 934 22.525 40.964 26.745 1.00 36.40 O -ANISOU 2590 O HOH A 934 4234 4058 5536 223 342 -73 O -HETATM 2591 O HOH A 935 59.889 44.197 5.600 1.00 26.57 O -ANISOU 2591 O HOH A 935 4709 2195 3190 -467 -1165 0 O -HETATM 2592 O HOH A 936 22.762 24.292 37.416 1.00 35.61 O -ANISOU 2592 O HOH A 936 4516 4576 4436 -58 897 182 O -HETATM 2593 O HOH A 937 22.233 23.679 -5.606 1.00 33.83 O -ANISOU 2593 O HOH A 937 4157 5022 3672 111 212 -272 O -HETATM 2594 O HOH A 938 15.954 9.146 15.144 1.00 40.23 O -ANISOU 2594 O HOH A 938 5144 4676 5462 -400 -116 708 O -HETATM 2595 O HOH A 939 26.733 1.174 -2.562 1.00 34.97 O -ANISOU 2595 O HOH A 939 4015 4252 5019 -440 274 -362 O -HETATM 2596 O HOH A 940 52.175 41.324 22.151 1.00 33.14 O -ANISOU 2596 O HOH A 940 4232 4168 4191 -200 490 -592 O -HETATM 2597 O HOH A 941 45.057 13.303 18.392 1.00 31.99 O -ANISOU 2597 O HOH A 941 4340 4137 3675 -943 605 569 O -HETATM 2598 O HOH A 942 47.583 44.846 5.544 1.00 28.65 O -ANISOU 2598 O HOH A 942 4042 2640 4203 733 19 1339 O -CONECT 494 500 -CONECT 500 494 501 -CONECT 501 500 502 504 -CONECT 502 501 503 508 -CONECT 503 502 -CONECT 504 501 505 -CONECT 505 504 506 -CONECT 506 505 507 -CONECT 507 506 -CONECT 508 502 -CONECT 1698 1707 -CONECT 1707 1698 1708 -CONECT 1708 1707 1709 1711 -CONECT 1709 1708 1710 1715 -CONECT 1710 1709 -CONECT 1711 1708 1712 -CONECT 1712 1711 1713 -CONECT 1713 1712 1714 -CONECT 1714 1713 -CONECT 1715 1709 -CONECT 2086 2095 -CONECT 2095 2086 2096 -CONECT 2096 2095 2097 2099 -CONECT 2097 2096 2098 2105 -CONECT 2098 2097 -CONECT 2099 2096 2100 -CONECT 2100 2099 2101 2102 -CONECT 2101 2100 2103 -CONECT 2102 2100 2104 -CONECT 2103 2101 -CONECT 2104 2102 -CONECT 2105 2097 -CONECT 2123 2125 2130 2166 2172 -CONECT 2123 2180 2182 -CONECT 2124 2125 2126 2127 2131 -CONECT 2125 2123 2124 -CONECT 2126 2124 -CONECT 2127 2124 -CONECT 2128 2129 2130 2131 2135 -CONECT 2129 2128 -CONECT 2130 2123 2128 -CONECT 2131 2124 2128 -CONECT 2132 2133 2134 2135 2136 -CONECT 2133 2132 -CONECT 2134 2132 -CONECT 2135 2128 2132 -CONECT 2136 2132 2137 -CONECT 2137 2136 2138 -CONECT 2138 2137 2139 2140 -CONECT 2139 2138 2144 -CONECT 2140 2138 2141 2142 -CONECT 2141 2140 -CONECT 2142 2140 2143 2144 -CONECT 2143 2142 -CONECT 2144 2139 2142 2145 -CONECT 2145 2144 2146 2154 -CONECT 2146 2145 2147 -CONECT 2147 2146 2148 -CONECT 2148 2147 2149 2154 -CONECT 2149 2148 2150 2151 -CONECT 2150 2149 -CONECT 2151 2149 2152 -CONECT 2152 2151 2153 -CONECT 2153 2152 2154 -CONECT 2154 2145 2148 2153 -CONECT 2166 2123 -CONECT 2172 2123 -CONECT 2180 2123 -CONECT 2182 2123 -MASTER 304 0 5 12 18 0 9 6 2591 1 69 22 -END |